data_7HFX
# 
_entry.id   7HFX 
# 
_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   7HFX         pdb_00007hfx 10.2210/pdb7hfx/pdb 
WWPDB D_1001407423 ?            ?                   
# 
_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                        7HFX 
_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 '2-methyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 206.244   1   ?                      ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                   35.453    1   ?                      ? ? ? 
4 water       nat water                                                            18.015    425 ?                      ? ? ? 
# 
_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 '2-methyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1BCC 
3 'CHLORIDE ION'                                                   CL    
4 water                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BCC non-polymer         . '2-methyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C10 H14 N4 O'   206.244 
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 
CL    non-polymer         . 'CHLORIDE ION'                                                   ? 'Cl -1'          35.453  
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 A1BCC 1   201  201  A1BCC LA1 A . 
D 3 CL    1   202  1    CL    CL  A . 
E 4 HOH   1   1301 1301 HOH   HOH A . 
E 4 HOH   2   1302 1290 HOH   HOH A . 
E 4 HOH   3   1303 196  HOH   HOH A . 
E 4 HOH   4   1304 1289 HOH   HOH A . 
E 4 HOH   5   1305 109  HOH   HOH A . 
E 4 HOH   6   1306 625  HOH   HOH A . 
E 4 HOH   7   1307 292  HOH   HOH A . 
E 4 HOH   8   1308 86   HOH   HOH A . 
E 4 HOH   9   1309 105  HOH   HOH A . 
E 4 HOH   10  1310 247  HOH   HOH A . 
E 4 HOH   11  1311 209  HOH   HOH A . 
E 4 HOH   12  1312 151  HOH   HOH A . 
E 4 HOH   13  1313 1310 HOH   HOH A . 
E 4 HOH   14  1314 337  HOH   HOH A . 
E 4 HOH   15  1315 76   HOH   HOH A . 
E 4 HOH   16  1316 229  HOH   HOH A . 
E 4 HOH   17  1317 57   HOH   HOH A . 
E 4 HOH   18  1318 1295 HOH   HOH A . 
E 4 HOH   19  1319 1275 HOH   HOH A . 
E 4 HOH   20  1320 195  HOH   HOH A . 
E 4 HOH   21  1321 236  HOH   HOH A . 
E 4 HOH   22  1322 630  HOH   HOH A . 
E 4 HOH   23  1323 124  HOH   HOH A . 
E 4 HOH   24  1324 493  HOH   HOH A . 
E 4 HOH   25  1325 225  HOH   HOH A . 
E 4 HOH   26  1326 136  HOH   HOH A . 
E 4 HOH   27  1327 21   HOH   HOH A . 
E 4 HOH   28  1328 393  HOH   HOH A . 
E 4 HOH   29  1329 36   HOH   HOH A . 
E 4 HOH   30  1330 192  HOH   HOH A . 
E 4 HOH   31  1331 153  HOH   HOH A . 
E 4 HOH   32  1332 15   HOH   HOH A . 
E 4 HOH   33  1333 8    HOH   HOH A . 
E 4 HOH   34  1334 2    HOH   HOH A . 
E 4 HOH   35  1335 5    HOH   HOH A . 
E 4 HOH   36  1336 148  HOH   HOH A . 
E 4 HOH   37  1337 164  HOH   HOH A . 
E 4 HOH   38  1338 19   HOH   HOH A . 
E 4 HOH   39  1339 49   HOH   HOH A . 
E 4 HOH   40  1340 96   HOH   HOH A . 
E 4 HOH   41  1341 140  HOH   HOH A . 
E 4 HOH   42  1342 964  HOH   HOH A . 
E 4 HOH   43  1343 241  HOH   HOH A . 
E 4 HOH   44  1344 42   HOH   HOH A . 
E 4 HOH   45  1345 381  HOH   HOH A . 
E 4 HOH   46  1346 4    HOH   HOH A . 
E 4 HOH   47  1347 199  HOH   HOH A . 
E 4 HOH   48  1348 320  HOH   HOH A . 
E 4 HOH   49  1349 39   HOH   HOH A . 
E 4 HOH   50  1350 2    HOH   HOH A . 
E 4 HOH   51  1351 102  HOH   HOH A . 
E 4 HOH   52  1352 14   HOH   HOH A . 
E 4 HOH   53  1353 68   HOH   HOH A . 
E 4 HOH   54  1354 139  HOH   HOH A . 
E 4 HOH   55  1355 469  HOH   HOH A . 
E 4 HOH   56  1356 354  HOH   HOH A . 
E 4 HOH   57  1357 1283 HOH   HOH A . 
E 4 HOH   58  1358 27   HOH   HOH A . 
E 4 HOH   59  1359 92   HOH   HOH A . 
E 4 HOH   60  1360 93   HOH   HOH A . 
E 4 HOH   61  1361 162  HOH   HOH A . 
E 4 HOH   62  1362 66   HOH   HOH A . 
E 4 HOH   63  1363 33   HOH   HOH A . 
E 4 HOH   64  1364 26   HOH   HOH A . 
E 4 HOH   65  1365 165  HOH   HOH A . 
E 4 HOH   66  1366 396  HOH   HOH A . 
E 4 HOH   67  1367 159  HOH   HOH A . 
E 4 HOH   68  1368 939  HOH   HOH A . 
E 4 HOH   69  1369 281  HOH   HOH A . 
E 4 HOH   70  1370 19   HOH   HOH A . 
E 4 HOH   71  1371 186  HOH   HOH A . 
E 4 HOH   72  1372 81   HOH   HOH A . 
E 4 HOH   73  1373 45   HOH   HOH A . 
E 4 HOH   74  1374 169  HOH   HOH A . 
E 4 HOH   75  1375 12   HOH   HOH A . 
E 4 HOH   76  1376 5    HOH   HOH A . 
E 4 HOH   77  1377 56   HOH   HOH A . 
E 4 HOH   78  1378 138  HOH   HOH A . 
E 4 HOH   79  1379 461  HOH   HOH A . 
E 4 HOH   80  1380 13   HOH   HOH A . 
E 4 HOH   81  1381 18   HOH   HOH A . 
E 4 HOH   82  1382 409  HOH   HOH A . 
E 4 HOH   83  1383 74   HOH   HOH A . 
E 4 HOH   84  1384 17   HOH   HOH A . 
E 4 HOH   85  1385 296  HOH   HOH A . 
E 4 HOH   86  1386 1300 HOH   HOH A . 
E 4 HOH   87  1387 46   HOH   HOH A . 
E 4 HOH   88  1388 218  HOH   HOH A . 
E 4 HOH   89  1389 17   HOH   HOH A . 
E 4 HOH   90  1390 134  HOH   HOH A . 
E 4 HOH   91  1391 662  HOH   HOH A . 
E 4 HOH   92  1392 154  HOH   HOH A . 
E 4 HOH   93  1393 661  HOH   HOH A . 
E 4 HOH   94  1394 155  HOH   HOH A . 
E 4 HOH   95  1395 35   HOH   HOH A . 
E 4 HOH   96  1396 34   HOH   HOH A . 
E 4 HOH   97  1397 24   HOH   HOH A . 
E 4 HOH   98  1398 78   HOH   HOH A . 
E 4 HOH   99  1399 366  HOH   HOH A . 
E 4 HOH   100 1400 116  HOH   HOH A . 
E 4 HOH   101 1401 58   HOH   HOH A . 
E 4 HOH   102 1402 1315 HOH   HOH A . 
E 4 HOH   103 1403 1313 HOH   HOH A . 
E 4 HOH   104 1404 397  HOH   HOH A . 
E 4 HOH   105 1405 70   HOH   HOH A . 
E 4 HOH   106 1406 1308 HOH   HOH A . 
E 4 HOH   107 1407 85   HOH   HOH A . 
E 4 HOH   108 1408 4    HOH   HOH A . 
E 4 HOH   109 1409 132  HOH   HOH A . 
E 4 HOH   110 1410 12   HOH   HOH A . 
E 4 HOH   111 1411 303  HOH   HOH A . 
E 4 HOH   112 1412 67   HOH   HOH A . 
E 4 HOH   113 1413 6    HOH   HOH A . 
E 4 HOH   114 1414 121  HOH   HOH A . 
E 4 HOH   115 1415 3    HOH   HOH A . 
E 4 HOH   116 1416 25   HOH   HOH A . 
E 4 HOH   117 1417 83   HOH   HOH A . 
E 4 HOH   118 1418 351  HOH   HOH A . 
E 4 HOH   119 1419 9    HOH   HOH A . 
E 4 HOH   120 1420 278  HOH   HOH A . 
E 4 HOH   121 1421 333  HOH   HOH A . 
E 4 HOH   122 1422 1068 HOH   HOH A . 
E 4 HOH   123 1423 53   HOH   HOH A . 
E 4 HOH   124 1424 125  HOH   HOH A . 
E 4 HOH   125 1425 115  HOH   HOH A . 
E 4 HOH   126 1426 1    HOH   HOH A . 
E 4 HOH   127 1427 123  HOH   HOH A . 
E 4 HOH   128 1428 95   HOH   HOH A . 
E 4 HOH   129 1429 156  HOH   HOH A . 
E 4 HOH   130 1430 1279 HOH   HOH A . 
E 4 HOH   131 1431 405  HOH   HOH A . 
E 4 HOH   132 1432 7    HOH   HOH A . 
E 4 HOH   133 1433 11   HOH   HOH A . 
E 4 HOH   134 1434 51   HOH   HOH A . 
E 4 HOH   135 1435 1222 HOH   HOH A . 
E 4 HOH   136 1436 122  HOH   HOH A . 
E 4 HOH   137 1437 212  HOH   HOH A . 
E 4 HOH   138 1438 1286 HOH   HOH A . 
E 4 HOH   139 1439 582  HOH   HOH A . 
E 4 HOH   140 1440 16   HOH   HOH A . 
E 4 HOH   141 1441 71   HOH   HOH A . 
E 4 HOH   142 1442 1189 HOH   HOH A . 
E 4 HOH   143 1443 188  HOH   HOH A . 
E 4 HOH   144 1444 1309 HOH   HOH A . 
E 4 HOH   145 1445 80   HOH   HOH A . 
E 4 HOH   146 1446 576  HOH   HOH A . 
E 4 HOH   147 1447 40   HOH   HOH A . 
E 4 HOH   148 1448 94   HOH   HOH A . 
E 4 HOH   149 1449 952  HOH   HOH A . 
E 4 HOH   150 1450 97   HOH   HOH A . 
E 4 HOH   151 1451 1296 HOH   HOH A . 
E 4 HOH   152 1452 1119 HOH   HOH A . 
E 4 HOH   153 1453 944  HOH   HOH A . 
E 4 HOH   154 1454 104  HOH   HOH A . 
E 4 HOH   155 1455 73   HOH   HOH A . 
E 4 HOH   156 1456 1094 HOH   HOH A . 
E 4 HOH   157 1457 1238 HOH   HOH A . 
E 4 HOH   158 1458 79   HOH   HOH A . 
E 4 HOH   159 1459 330  HOH   HOH A . 
E 4 HOH   160 1460 107  HOH   HOH A . 
E 4 HOH   161 1461 3    HOH   HOH A . 
E 4 HOH   162 1462 509  HOH   HOH A . 
E 4 HOH   163 1463 1134 HOH   HOH A . 
E 4 HOH   164 1464 163  HOH   HOH A . 
E 4 HOH   165 1465 408  HOH   HOH A . 
E 4 HOH   166 1466 726  HOH   HOH A . 
E 4 HOH   167 1467 756  HOH   HOH A . 
E 4 HOH   168 1468 7    HOH   HOH A . 
E 4 HOH   169 1469 361  HOH   HOH A . 
E 4 HOH   170 1470 556  HOH   HOH A . 
E 4 HOH   171 1471 126  HOH   HOH A . 
E 4 HOH   172 1472 280  HOH   HOH A . 
E 4 HOH   173 1473 1276 HOH   HOH A . 
E 4 HOH   174 1474 342  HOH   HOH A . 
E 4 HOH   175 1475 801  HOH   HOH A . 
E 4 HOH   176 1476 319  HOH   HOH A . 
E 4 HOH   177 1477 250  HOH   HOH A . 
E 4 HOH   178 1478 63   HOH   HOH A . 
E 4 HOH   179 1479 1307 HOH   HOH A . 
E 4 HOH   180 1480 135  HOH   HOH A . 
E 4 HOH   181 1481 1287 HOH   HOH A . 
E 4 HOH   182 1482 1306 HOH   HOH A . 
E 4 HOH   183 1483 695  HOH   HOH A . 
E 4 HOH   184 1484 370  HOH   HOH A . 
E 4 HOH   185 1485 674  HOH   HOH A . 
E 4 HOH   186 1486 224  HOH   HOH A . 
E 4 HOH   187 1487 326  HOH   HOH A . 
E 4 HOH   188 1488 202  HOH   HOH A . 
E 4 HOH   189 1489 919  HOH   HOH A . 
E 4 HOH   190 1490 711  HOH   HOH A . 
E 4 HOH   191 1491 267  HOH   HOH A . 
E 4 HOH   192 1492 10   HOH   HOH A . 
E 4 HOH   193 1493 521  HOH   HOH A . 
E 4 HOH   194 1494 318  HOH   HOH A . 
E 4 HOH   195 1495 309  HOH   HOH A . 
E 4 HOH   196 1496 1299 HOH   HOH A . 
E 4 HOH   197 1497 315  HOH   HOH A . 
E 4 HOH   198 1498 18   HOH   HOH A . 
E 4 HOH   199 1499 263  HOH   HOH A . 
E 4 HOH   200 1500 8    HOH   HOH A . 
E 4 HOH   201 1501 331  HOH   HOH A . 
E 4 HOH   202 1502 1314 HOH   HOH A . 
E 4 HOH   203 1503 805  HOH   HOH A . 
E 4 HOH   204 1504 152  HOH   HOH A . 
E 4 HOH   205 1505 941  HOH   HOH A . 
E 4 HOH   206 1506 208  HOH   HOH A . 
E 4 HOH   207 1507 1071 HOH   HOH A . 
E 4 HOH   208 1508 356  HOH   HOH A . 
E 4 HOH   209 1509 180  HOH   HOH A . 
E 4 HOH   210 1510 350  HOH   HOH A . 
E 4 HOH   211 1511 371  HOH   HOH A . 
E 4 HOH   212 1512 16   HOH   HOH A . 
E 4 HOH   213 1513 363  HOH   HOH A . 
E 4 HOH   214 1514 15   HOH   HOH A . 
E 4 HOH   215 1515 313  HOH   HOH A . 
E 4 HOH   216 1516 376  HOH   HOH A . 
E 4 HOH   217 1517 1284 HOH   HOH A . 
E 4 HOH   218 1518 429  HOH   HOH A . 
E 4 HOH   219 1519 185  HOH   HOH A . 
E 4 HOH   220 1520 772  HOH   HOH A . 
E 4 HOH   221 1521 1074 HOH   HOH A . 
E 4 HOH   222 1522 346  HOH   HOH A . 
E 4 HOH   223 1523 1292 HOH   HOH A . 
E 4 HOH   224 1524 1078 HOH   HOH A . 
F 4 HOH   1   201  64   HOH   HOH B . 
F 4 HOH   2   202  276  HOH   HOH B . 
F 4 HOH   3   203  358  HOH   HOH B . 
F 4 HOH   4   204  531  HOH   HOH B . 
F 4 HOH   5   205  240  HOH   HOH B . 
F 4 HOH   6   206  364  HOH   HOH B . 
F 4 HOH   7   207  549  HOH   HOH B . 
F 4 HOH   8   208  758  HOH   HOH B . 
F 4 HOH   9   209  343  HOH   HOH B . 
F 4 HOH   10  210  398  HOH   HOH B . 
F 4 HOH   11  211  654  HOH   HOH B . 
F 4 HOH   12  212  900  HOH   HOH B . 
F 4 HOH   13  213  1249 HOH   HOH B . 
F 4 HOH   14  214  232  HOH   HOH B . 
F 4 HOH   15  215  743  HOH   HOH B . 
F 4 HOH   16  216  264  HOH   HOH B . 
F 4 HOH   17  217  120  HOH   HOH B . 
F 4 HOH   18  218  50   HOH   HOH B . 
F 4 HOH   19  219  452  HOH   HOH B . 
F 4 HOH   20  220  353  HOH   HOH B . 
F 4 HOH   21  221  1140 HOH   HOH B . 
F 4 HOH   22  222  131  HOH   HOH B . 
F 4 HOH   23  223  444  HOH   HOH B . 
F 4 HOH   24  224  205  HOH   HOH B . 
F 4 HOH   25  225  128  HOH   HOH B . 
F 4 HOH   26  226  75   HOH   HOH B . 
F 4 HOH   27  227  82   HOH   HOH B . 
F 4 HOH   28  228  1278 HOH   HOH B . 
F 4 HOH   29  229  54   HOH   HOH B . 
F 4 HOH   30  230  723  HOH   HOH B . 
F 4 HOH   31  231  282  HOH   HOH B . 
F 4 HOH   32  232  332  HOH   HOH B . 
F 4 HOH   33  233  69   HOH   HOH B . 
F 4 HOH   34  234  127  HOH   HOH B . 
F 4 HOH   35  235  181  HOH   HOH B . 
F 4 HOH   36  236  272  HOH   HOH B . 
F 4 HOH   37  237  1312 HOH   HOH B . 
F 4 HOH   38  238  1    HOH   HOH B . 
F 4 HOH   39  239  231  HOH   HOH B . 
F 4 HOH   40  240  110  HOH   HOH B . 
F 4 HOH   41  241  129  HOH   HOH B . 
F 4 HOH   42  242  60   HOH   HOH B . 
F 4 HOH   43  243  14   HOH   HOH B . 
F 4 HOH   44  244  271  HOH   HOH B . 
F 4 HOH   45  245  172  HOH   HOH B . 
F 4 HOH   46  246  325  HOH   HOH B . 
F 4 HOH   47  247  30   HOH   HOH B . 
F 4 HOH   48  248  300  HOH   HOH B . 
F 4 HOH   49  249  9    HOH   HOH B . 
F 4 HOH   50  250  143  HOH   HOH B . 
F 4 HOH   51  251  72   HOH   HOH B . 
F 4 HOH   52  252  166  HOH   HOH B . 
F 4 HOH   53  253  52   HOH   HOH B . 
F 4 HOH   54  254  133  HOH   HOH B . 
F 4 HOH   55  255  47   HOH   HOH B . 
F 4 HOH   56  256  144  HOH   HOH B . 
F 4 HOH   57  257  150  HOH   HOH B . 
F 4 HOH   58  258  31   HOH   HOH B . 
F 4 HOH   59  259  41   HOH   HOH B . 
F 4 HOH   60  260  347  HOH   HOH B . 
F 4 HOH   61  261  103  HOH   HOH B . 
F 4 HOH   62  262  416  HOH   HOH B . 
F 4 HOH   63  263  10   HOH   HOH B . 
F 4 HOH   64  264  59   HOH   HOH B . 
F 4 HOH   65  265  243  HOH   HOH B . 
F 4 HOH   66  266  1106 HOH   HOH B . 
F 4 HOH   67  267  62   HOH   HOH B . 
F 4 HOH   68  268  391  HOH   HOH B . 
F 4 HOH   69  269  61   HOH   HOH B . 
F 4 HOH   70  270  20   HOH   HOH B . 
F 4 HOH   71  271  11   HOH   HOH B . 
F 4 HOH   72  272  77   HOH   HOH B . 
F 4 HOH   73  273  114  HOH   HOH B . 
F 4 HOH   74  274  302  HOH   HOH B . 
F 4 HOH   75  275  84   HOH   HOH B . 
F 4 HOH   76  276  242  HOH   HOH B . 
F 4 HOH   77  277  221  HOH   HOH B . 
F 4 HOH   78  278  117  HOH   HOH B . 
F 4 HOH   79  279  635  HOH   HOH B . 
F 4 HOH   80  280  387  HOH   HOH B . 
F 4 HOH   81  281  175  HOH   HOH B . 
F 4 HOH   82  282  252  HOH   HOH B . 
F 4 HOH   83  283  1277 HOH   HOH B . 
F 4 HOH   84  284  43   HOH   HOH B . 
F 4 HOH   85  285  1305 HOH   HOH B . 
F 4 HOH   86  286  13   HOH   HOH B . 
F 4 HOH   87  287  22   HOH   HOH B . 
F 4 HOH   88  288  88   HOH   HOH B . 
F 4 HOH   89  289  235  HOH   HOH B . 
F 4 HOH   90  290  89   HOH   HOH B . 
F 4 HOH   91  291  106  HOH   HOH B . 
F 4 HOH   92  292  147  HOH   HOH B . 
F 4 HOH   93  293  99   HOH   HOH B . 
F 4 HOH   94  294  1066 HOH   HOH B . 
F 4 HOH   95  295  141  HOH   HOH B . 
F 4 HOH   96  296  287  HOH   HOH B . 
F 4 HOH   97  297  137  HOH   HOH B . 
F 4 HOH   98  298  112  HOH   HOH B . 
F 4 HOH   99  299  216  HOH   HOH B . 
F 4 HOH   100 300  297  HOH   HOH B . 
F 4 HOH   101 301  316  HOH   HOH B . 
F 4 HOH   102 302  215  HOH   HOH B . 
F 4 HOH   103 303  118  HOH   HOH B . 
F 4 HOH   104 304  142  HOH   HOH B . 
F 4 HOH   105 305  311  HOH   HOH B . 
F 4 HOH   106 306  160  HOH   HOH B . 
F 4 HOH   107 307  341  HOH   HOH B . 
F 4 HOH   108 308  32   HOH   HOH B . 
F 4 HOH   109 309  704  HOH   HOH B . 
F 4 HOH   110 310  1126 HOH   HOH B . 
F 4 HOH   111 311  299  HOH   HOH B . 
F 4 HOH   112 312  220  HOH   HOH B . 
F 4 HOH   113 313  91   HOH   HOH B . 
F 4 HOH   114 314  38   HOH   HOH B . 
F 4 HOH   115 315  48   HOH   HOH B . 
F 4 HOH   116 316  101  HOH   HOH B . 
F 4 HOH   117 317  170  HOH   HOH B . 
F 4 HOH   118 318  37   HOH   HOH B . 
F 4 HOH   119 319  1291 HOH   HOH B . 
F 4 HOH   120 320  23   HOH   HOH B . 
F 4 HOH   121 321  28   HOH   HOH B . 
F 4 HOH   122 322  161  HOH   HOH B . 
F 4 HOH   123 323  1285 HOH   HOH B . 
F 4 HOH   124 324  44   HOH   HOH B . 
F 4 HOH   125 325  177  HOH   HOH B . 
F 4 HOH   126 326  1274 HOH   HOH B . 
F 4 HOH   127 327  55   HOH   HOH B . 
F 4 HOH   128 328  100  HOH   HOH B . 
F 4 HOH   129 329  717  HOH   HOH B . 
F 4 HOH   130 330  197  HOH   HOH B . 
F 4 HOH   131 331  29   HOH   HOH B . 
F 4 HOH   132 332  339  HOH   HOH B . 
F 4 HOH   133 333  207  HOH   HOH B . 
F 4 HOH   134 334  98   HOH   HOH B . 
F 4 HOH   135 335  182  HOH   HOH B . 
F 4 HOH   136 336  1294 HOH   HOH B . 
F 4 HOH   137 337  445  HOH   HOH B . 
F 4 HOH   138 338  334  HOH   HOH B . 
F 4 HOH   139 339  234  HOH   HOH B . 
F 4 HOH   140 340  65   HOH   HOH B . 
F 4 HOH   141 341  619  HOH   HOH B . 
F 4 HOH   142 342  1293 HOH   HOH B . 
F 4 HOH   143 343  362  HOH   HOH B . 
F 4 HOH   144 344  178  HOH   HOH B . 
F 4 HOH   145 345  463  HOH   HOH B . 
F 4 HOH   146 346  960  HOH   HOH B . 
F 4 HOH   147 347  90   HOH   HOH B . 
F 4 HOH   148 348  191  HOH   HOH B . 
F 4 HOH   149 349  1304 HOH   HOH B . 
F 4 HOH   150 350  335  HOH   HOH B . 
F 4 HOH   151 351  623  HOH   HOH B . 
F 4 HOH   152 352  304  HOH   HOH B . 
F 4 HOH   153 353  1046 HOH   HOH B . 
F 4 HOH   154 354  1280 HOH   HOH B . 
F 4 HOH   155 355  203  HOH   HOH B . 
F 4 HOH   156 356  541  HOH   HOH B . 
F 4 HOH   157 357  290  HOH   HOH B . 
F 4 HOH   158 358  87   HOH   HOH B . 
F 4 HOH   159 359  479  HOH   HOH B . 
F 4 HOH   160 360  1077 HOH   HOH B . 
F 4 HOH   161 361  389  HOH   HOH B . 
F 4 HOH   162 362  283  HOH   HOH B . 
F 4 HOH   163 363  1072 HOH   HOH B . 
F 4 HOH   164 364  718  HOH   HOH B . 
F 4 HOH   165 365  898  HOH   HOH B . 
F 4 HOH   166 366  1316 HOH   HOH B . 
F 4 HOH   167 367  373  HOH   HOH B . 
F 4 HOH   168 368  340  HOH   HOH B . 
F 4 HOH   169 369  1303 HOH   HOH B . 
F 4 HOH   170 370  310  HOH   HOH B . 
F 4 HOH   171 371  667  HOH   HOH B . 
F 4 HOH   172 372  291  HOH   HOH B . 
F 4 HOH   173 373  615  HOH   HOH B . 
F 4 HOH   174 374  183  HOH   HOH B . 
F 4 HOH   175 375  149  HOH   HOH B . 
F 4 HOH   176 376  190  HOH   HOH B . 
F 4 HOH   177 377  431  HOH   HOH B . 
F 4 HOH   178 378  1173 HOH   HOH B . 
F 4 HOH   179 379  1163 HOH   HOH B . 
F 4 HOH   180 380  1000 HOH   HOH B . 
F 4 HOH   181 381  418  HOH   HOH B . 
F 4 HOH   182 382  176  HOH   HOH B . 
F 4 HOH   183 383  424  HOH   HOH B . 
F 4 HOH   184 384  1311 HOH   HOH B . 
F 4 HOH   185 385  491  HOH   HOH B . 
F 4 HOH   186 386  1298 HOH   HOH B . 
F 4 HOH   187 387  248  HOH   HOH B . 
F 4 HOH   188 388  470  HOH   HOH B . 
F 4 HOH   189 389  265  HOH   HOH B . 
F 4 HOH   190 390  981  HOH   HOH B . 
F 4 HOH   191 391  184  HOH   HOH B . 
F 4 HOH   192 392  360  HOH   HOH B . 
F 4 HOH   193 393  410  HOH   HOH B . 
F 4 HOH   194 394  355  HOH   HOH B . 
F 4 HOH   195 395  566  HOH   HOH B . 
F 4 HOH   196 396  314  HOH   HOH B . 
F 4 HOH   197 397  274  HOH   HOH B . 
F 4 HOH   198 398  157  HOH   HOH B . 
F 4 HOH   199 399  792  HOH   HOH B . 
F 4 HOH   200 400  321  HOH   HOH B . 
F 4 HOH   201 401  558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HFX 
_cell.length_a           88.746 
_cell.length_b           88.746 
_cell.length_c           39.528 
_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                         7HFX 
_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          7HFX 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.65 
_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   2023-12-22 
_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   0.88556 
_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        0.88556 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HFX 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.370 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156154 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.040 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.600 
_reflns.B_iso_Wilson_estimate        11.190 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.044 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1006278 
_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 1.020 1.040  ? 44551 7482 ? 0.640 ? ? ? 6.000 ? 1.900  ? ? ? ? ? ? 97.100 0.703 0.284 0.891 
1 2 5.590 44.370 ? 7109  1039 ? 0.026 ? ? ? 6.800 ? 57.200 ? ? ? ? ? ? 99.800 0.028 0.011 0.999 
# 
_refine.entry_id                                 7HFX 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.3700 
_refine.pdbx_ls_sigma_F                          1.370 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7600 
_refine.ls_number_reflns_obs                     156084 
_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                          0.1383 
_refine.ls_R_factor_R_work                       0.1377 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1511 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7527 
_refine.ls_number_reflns_R_work                  148557 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.4468 
_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                            0.0800 
_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                                60.130 
_refine.B_iso_min                                8.170 
_refine.pdbx_overall_phase_error                 14.8100 
_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                       1.0200 
_refine_hist.d_res_low                        44.3700 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             425 
_refine_hist.number_atoms_total               2997 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           13.82 
_refine_hist.pdbx_B_iso_mean_solvent          28.65 
_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 
1.0200 1.0300  30 96.0000  4762 . 0.2592 0.2806 . 190 0.0000 4952 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4934 . 0.2034 0.2060 . 280 0.0000 5214 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4870 . 0.1807 0.1820 . 277 0.0000 5147 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4919 . 0.1689 0.1939 . 279 0.0000 5198 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4924 . 0.1696 0.1935 . 233 0.0000 5157 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4972 . 0.1594 0.1913 . 241 0.0000 5213 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4856 . 0.1499 0.1756 . 268 0.0000 5124 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 4997 . 0.1404 0.1623 . 212 0.0000 5209 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4911 . 0.1342 0.1556 . 241 0.0000 5152 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4979 . 0.1237 0.1401 . 262 0.0000 5241 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4907 . 0.1200 0.1432 . 248 0.0000 5155 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4910 . 0.1147 0.1464 . 270 0.0000 5180 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5038 . 0.1128 0.1360 . 217 0.0000 5255 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4879 . 0.1163 0.1297 . 252 0.0000 5131 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4964 . 0.1176 0.1425 . 247 0.0000 5211 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4931 . 0.1196 0.1317 . 270 0.0000 5201 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4947 . 0.1231 0.1433 . 249 0.0000 5196 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4942 . 0.1223 0.1385 . 261 0.0000 5203 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4972 . 0.1207 0.1417 . 240 0.0000 5212 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4955 . 0.1191 0.1291 . 244 0.0000 5199 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4988 . 0.1166 0.1329 . 237 0.0000 5225 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 4951 . 0.1187 0.1303 . 265 0.0000 5216 . 'X-RAY DIFFRACTION' 
1.5900 1.6600  30 100.0000 4938 . 0.1186 0.1348 . 260 0.0000 5198 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5020 . 0.1264 0.1370 . 206 0.0000 5226 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4952 . 0.1311 0.1335 . 292 0.0000 5244 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4993 . 0.1355 0.1400 . 244 0.0000 5237 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4949 . 0.1379 0.1432 . 287 0.0000 5236 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 4998 . 0.1389 0.1443 . 256 0.0000 5254 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5030 . 0.1511 0.1648 . 249 0.0000 5279 . 'X-RAY DIFFRACTION' 
3.1700 44.3700 30 100.0000 5169 . 0.1483 0.1695 . 250 0.0000 5419 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFX 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0005266' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFX 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HFX A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFX 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 7HFX SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFX MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFX SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFX MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? PHE A 168 ? ASP A 157 PHE A 168 1 ? 12 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HFX 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 HH A TYR 42 ? B 1_555 OD1 B ASP 67 ? ? 2_654 1.57 
2 1 O  A ASP 66 ? ? 1_555 HG  B SER 1  ? B 2_655 1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.43   -133.23 
2 1 SER A 128 ? B 68.81   -4.90   
3 1 SER A 167 ? B -111.48 52.45   
4 1 HIS B 86  ? ? 57.59   -128.29 
# 
_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 1522 ? 5.86 . 
2 1 O ? A HOH 1523 ? 6.05 . 
3 1 O ? A HOH 1524 ? 7.48 . 
4 1 O ? B HOH 401  ? 6.22 . 
# 
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 
A1BCC N2   N  Y N 1   
A1BCC C3   C  N N 2   
A1BCC C6   C  Y N 3   
A1BCC C9   C  Y N 4   
A1BCC C1   C  N N 5   
A1BCC C10  C  Y N 6   
A1BCC C2   C  N N 7   
A1BCC C4   C  N N 8   
A1BCC C5   C  Y N 9   
A1BCC C7   C  Y N 10  
A1BCC C8   C  Y N 11  
A1BCC N1   N  N N 12  
A1BCC N3   N  Y N 13  
A1BCC N4   N  Y N 14  
A1BCC O1   O  N N 15  
A1BCC H6   H  N N 16  
A1BCC H4   H  N N 17  
A1BCC H5   H  N N 18  
A1BCC H11  H  N N 19  
A1BCC H12  H  N N 20  
A1BCC H1   H  N N 21  
A1BCC H3   H  N N 22  
A1BCC H2   H  N N 23  
A1BCC H13  H  N N 24  
A1BCC H7   H  N N 25  
A1BCC H8   H  N N 26  
A1BCC H10  H  N N 27  
A1BCC H14  H  N N 28  
A1BCC H9   H  N N 29  
ALA   N    N  N N 30  
ALA   CA   C  N S 31  
ALA   C    C  N N 32  
ALA   O    O  N N 33  
ALA   CB   C  N N 34  
ALA   OXT  O  N N 35  
ALA   H    H  N N 36  
ALA   H2   H  N N 37  
ALA   HA   H  N N 38  
ALA   HB1  H  N N 39  
ALA   HB2  H  N N 40  
ALA   HB3  H  N N 41  
ALA   HXT  H  N N 42  
ARG   N    N  N N 43  
ARG   CA   C  N S 44  
ARG   C    C  N N 45  
ARG   O    O  N N 46  
ARG   CB   C  N N 47  
ARG   CG   C  N N 48  
ARG   CD   C  N N 49  
ARG   NE   N  N N 50  
ARG   CZ   C  N N 51  
ARG   NH1  N  N N 52  
ARG   NH2  N  N N 53  
ARG   OXT  O  N N 54  
ARG   H    H  N N 55  
ARG   H2   H  N N 56  
ARG   HA   H  N N 57  
ARG   HB2  H  N N 58  
ARG   HB3  H  N N 59  
ARG   HG2  H  N N 60  
ARG   HG3  H  N N 61  
ARG   HD2  H  N N 62  
ARG   HD3  H  N N 63  
ARG   HE   H  N N 64  
ARG   HH11 H  N N 65  
ARG   HH12 H  N N 66  
ARG   HH21 H  N N 67  
ARG   HH22 H  N N 68  
ARG   HXT  H  N N 69  
ASN   N    N  N N 70  
ASN   CA   C  N S 71  
ASN   C    C  N N 72  
ASN   O    O  N N 73  
ASN   CB   C  N N 74  
ASN   CG   C  N N 75  
ASN   OD1  O  N N 76  
ASN   ND2  N  N N 77  
ASN   OXT  O  N N 78  
ASN   H    H  N N 79  
ASN   H2   H  N N 80  
ASN   HA   H  N N 81  
ASN   HB2  H  N N 82  
ASN   HB3  H  N N 83  
ASN   HD21 H  N N 84  
ASN   HD22 H  N N 85  
ASN   HXT  H  N N 86  
ASP   N    N  N N 87  
ASP   CA   C  N S 88  
ASP   C    C  N N 89  
ASP   O    O  N N 90  
ASP   CB   C  N N 91  
ASP   CG   C  N N 92  
ASP   OD1  O  N N 93  
ASP   OD2  O  N N 94  
ASP   OXT  O  N N 95  
ASP   H    H  N N 96  
ASP   H2   H  N N 97  
ASP   HA   H  N N 98  
ASP   HB2  H  N N 99  
ASP   HB3  H  N N 100 
ASP   HD2  H  N N 101 
ASP   HXT  H  N N 102 
CL    CL   CL N N 103 
CYS   N    N  N N 104 
CYS   CA   C  N R 105 
CYS   C    C  N N 106 
CYS   O    O  N N 107 
CYS   CB   C  N N 108 
CYS   SG   S  N N 109 
CYS   OXT  O  N N 110 
CYS   H    H  N N 111 
CYS   H2   H  N N 112 
CYS   HA   H  N N 113 
CYS   HB2  H  N N 114 
CYS   HB3  H  N N 115 
CYS   HG   H  N N 116 
CYS   HXT  H  N N 117 
GLN   N    N  N N 118 
GLN   CA   C  N S 119 
GLN   C    C  N N 120 
GLN   O    O  N N 121 
GLN   CB   C  N N 122 
GLN   CG   C  N N 123 
GLN   CD   C  N N 124 
GLN   OE1  O  N N 125 
GLN   NE2  N  N N 126 
GLN   OXT  O  N N 127 
GLN   H    H  N N 128 
GLN   H2   H  N N 129 
GLN   HA   H  N N 130 
GLN   HB2  H  N N 131 
GLN   HB3  H  N N 132 
GLN   HG2  H  N N 133 
GLN   HG3  H  N N 134 
GLN   HE21 H  N N 135 
GLN   HE22 H  N N 136 
GLN   HXT  H  N N 137 
GLU   N    N  N N 138 
GLU   CA   C  N S 139 
GLU   C    C  N N 140 
GLU   O    O  N N 141 
GLU   CB   C  N N 142 
GLU   CG   C  N N 143 
GLU   CD   C  N N 144 
GLU   OE1  O  N N 145 
GLU   OE2  O  N N 146 
GLU   OXT  O  N N 147 
GLU   H    H  N N 148 
GLU   H2   H  N N 149 
GLU   HA   H  N N 150 
GLU   HB2  H  N N 151 
GLU   HB3  H  N N 152 
GLU   HG2  H  N N 153 
GLU   HG3  H  N N 154 
GLU   HE2  H  N N 155 
GLU   HXT  H  N N 156 
GLY   N    N  N N 157 
GLY   CA   C  N N 158 
GLY   C    C  N N 159 
GLY   O    O  N N 160 
GLY   OXT  O  N N 161 
GLY   H    H  N N 162 
GLY   H2   H  N N 163 
GLY   HA2  H  N N 164 
GLY   HA3  H  N N 165 
GLY   HXT  H  N N 166 
HIS   N    N  N N 167 
HIS   CA   C  N S 168 
HIS   C    C  N N 169 
HIS   O    O  N N 170 
HIS   CB   C  N N 171 
HIS   CG   C  Y N 172 
HIS   ND1  N  Y N 173 
HIS   CD2  C  Y N 174 
HIS   CE1  C  Y N 175 
HIS   NE2  N  Y N 176 
HIS   OXT  O  N N 177 
HIS   H    H  N N 178 
HIS   H2   H  N N 179 
HIS   HA   H  N N 180 
HIS   HB2  H  N N 181 
HIS   HB3  H  N N 182 
HIS   HD1  H  N N 183 
HIS   HD2  H  N N 184 
HIS   HE1  H  N N 185 
HIS   HE2  H  N N 186 
HIS   HXT  H  N N 187 
HOH   O    O  N N 188 
HOH   H1   H  N N 189 
HOH   H2   H  N N 190 
ILE   N    N  N N 191 
ILE   CA   C  N S 192 
ILE   C    C  N N 193 
ILE   O    O  N N 194 
ILE   CB   C  N S 195 
ILE   CG1  C  N N 196 
ILE   CG2  C  N N 197 
ILE   CD1  C  N N 198 
ILE   OXT  O  N N 199 
ILE   H    H  N N 200 
ILE   H2   H  N N 201 
ILE   HA   H  N N 202 
ILE   HB   H  N N 203 
ILE   HG12 H  N N 204 
ILE   HG13 H  N N 205 
ILE   HG21 H  N N 206 
ILE   HG22 H  N N 207 
ILE   HG23 H  N N 208 
ILE   HD11 H  N N 209 
ILE   HD12 H  N N 210 
ILE   HD13 H  N N 211 
ILE   HXT  H  N N 212 
LEU   N    N  N N 213 
LEU   CA   C  N S 214 
LEU   C    C  N N 215 
LEU   O    O  N N 216 
LEU   CB   C  N N 217 
LEU   CG   C  N N 218 
LEU   CD1  C  N N 219 
LEU   CD2  C  N N 220 
LEU   OXT  O  N N 221 
LEU   H    H  N N 222 
LEU   H2   H  N N 223 
LEU   HA   H  N N 224 
LEU   HB2  H  N N 225 
LEU   HB3  H  N N 226 
LEU   HG   H  N N 227 
LEU   HD11 H  N N 228 
LEU   HD12 H  N N 229 
LEU   HD13 H  N N 230 
LEU   HD21 H  N N 231 
LEU   HD22 H  N N 232 
LEU   HD23 H  N N 233 
LEU   HXT  H  N N 234 
LYS   N    N  N N 235 
LYS   CA   C  N S 236 
LYS   C    C  N N 237 
LYS   O    O  N N 238 
LYS   CB   C  N N 239 
LYS   CG   C  N N 240 
LYS   CD   C  N N 241 
LYS   CE   C  N N 242 
LYS   NZ   N  N N 243 
LYS   OXT  O  N N 244 
LYS   H    H  N N 245 
LYS   H2   H  N N 246 
LYS   HA   H  N N 247 
LYS   HB2  H  N N 248 
LYS   HB3  H  N N 249 
LYS   HG2  H  N N 250 
LYS   HG3  H  N N 251 
LYS   HD2  H  N N 252 
LYS   HD3  H  N N 253 
LYS   HE2  H  N N 254 
LYS   HE3  H  N N 255 
LYS   HZ1  H  N N 256 
LYS   HZ2  H  N N 257 
LYS   HZ3  H  N N 258 
LYS   HXT  H  N N 259 
MET   N    N  N N 260 
MET   CA   C  N S 261 
MET   C    C  N N 262 
MET   O    O  N N 263 
MET   CB   C  N N 264 
MET   CG   C  N N 265 
MET   SD   S  N N 266 
MET   CE   C  N N 267 
MET   OXT  O  N N 268 
MET   H    H  N N 269 
MET   H2   H  N N 270 
MET   HA   H  N N 271 
MET   HB2  H  N N 272 
MET   HB3  H  N N 273 
MET   HG2  H  N N 274 
MET   HG3  H  N N 275 
MET   HE1  H  N N 276 
MET   HE2  H  N N 277 
MET   HE3  H  N N 278 
MET   HXT  H  N N 279 
PHE   N    N  N N 280 
PHE   CA   C  N S 281 
PHE   C    C  N N 282 
PHE   O    O  N N 283 
PHE   CB   C  N N 284 
PHE   CG   C  Y N 285 
PHE   CD1  C  Y N 286 
PHE   CD2  C  Y N 287 
PHE   CE1  C  Y N 288 
PHE   CE2  C  Y N 289 
PHE   CZ   C  Y N 290 
PHE   OXT  O  N N 291 
PHE   H    H  N N 292 
PHE   H2   H  N N 293 
PHE   HA   H  N N 294 
PHE   HB2  H  N N 295 
PHE   HB3  H  N N 296 
PHE   HD1  H  N N 297 
PHE   HD2  H  N N 298 
PHE   HE1  H  N N 299 
PHE   HE2  H  N N 300 
PHE   HZ   H  N N 301 
PHE   HXT  H  N N 302 
PRO   N    N  N N 303 
PRO   CA   C  N S 304 
PRO   C    C  N N 305 
PRO   O    O  N N 306 
PRO   CB   C  N N 307 
PRO   CG   C  N N 308 
PRO   CD   C  N N 309 
PRO   OXT  O  N N 310 
PRO   H    H  N N 311 
PRO   HA   H  N N 312 
PRO   HB2  H  N N 313 
PRO   HB3  H  N N 314 
PRO   HG2  H  N N 315 
PRO   HG3  H  N N 316 
PRO   HD2  H  N N 317 
PRO   HD3  H  N N 318 
PRO   HXT  H  N N 319 
SER   N    N  N N 320 
SER   CA   C  N S 321 
SER   C    C  N N 322 
SER   O    O  N N 323 
SER   CB   C  N N 324 
SER   OG   O  N N 325 
SER   OXT  O  N N 326 
SER   H    H  N N 327 
SER   H2   H  N N 328 
SER   HA   H  N N 329 
SER   HB2  H  N N 330 
SER   HB3  H  N N 331 
SER   HG   H  N N 332 
SER   HXT  H  N N 333 
THR   N    N  N N 334 
THR   CA   C  N S 335 
THR   C    C  N N 336 
THR   O    O  N N 337 
THR   CB   C  N R 338 
THR   OG1  O  N N 339 
THR   CG2  C  N N 340 
THR   OXT  O  N N 341 
THR   H    H  N N 342 
THR   H2   H  N N 343 
THR   HA   H  N N 344 
THR   HB   H  N N 345 
THR   HG1  H  N N 346 
THR   HG21 H  N N 347 
THR   HG22 H  N N 348 
THR   HG23 H  N N 349 
THR   HXT  H  N N 350 
TYR   N    N  N N 351 
TYR   CA   C  N S 352 
TYR   C    C  N N 353 
TYR   O    O  N N 354 
TYR   CB   C  N N 355 
TYR   CG   C  Y N 356 
TYR   CD1  C  Y N 357 
TYR   CD2  C  Y N 358 
TYR   CE1  C  Y N 359 
TYR   CE2  C  Y N 360 
TYR   CZ   C  Y N 361 
TYR   OH   O  N N 362 
TYR   OXT  O  N N 363 
TYR   H    H  N N 364 
TYR   H2   H  N N 365 
TYR   HA   H  N N 366 
TYR   HB2  H  N N 367 
TYR   HB3  H  N N 368 
TYR   HD1  H  N N 369 
TYR   HD2  H  N N 370 
TYR   HE1  H  N N 371 
TYR   HE2  H  N N 372 
TYR   HH   H  N N 373 
TYR   HXT  H  N N 374 
VAL   N    N  N N 375 
VAL   CA   C  N S 376 
VAL   C    C  N N 377 
VAL   O    O  N N 378 
VAL   CB   C  N N 379 
VAL   CG1  C  N N 380 
VAL   CG2  C  N N 381 
VAL   OXT  O  N N 382 
VAL   H    H  N N 383 
VAL   H2   H  N N 384 
VAL   HA   H  N N 385 
VAL   HB   H  N N 386 
VAL   HG11 H  N N 387 
VAL   HG12 H  N N 388 
VAL   HG13 H  N N 389 
VAL   HG21 H  N N 390 
VAL   HG22 H  N N 391 
VAL   HG23 H  N N 392 
VAL   HXT  H  N N 393 
# 
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 
A1BCC C3  C2   sing N N 1   
A1BCC C1  C2   sing N N 2   
A1BCC C2  N1   sing N N 3   
A1BCC C2  C4   sing N N 4   
A1BCC N1  C5   sing N N 5   
A1BCC C4  O1   sing N N 6   
A1BCC C9  C8   sing Y N 7   
A1BCC C9  C10  doub Y N 8   
A1BCC C5  C8   doub Y N 9   
A1BCC C5  N2   sing Y N 10  
A1BCC C8  C7   sing Y N 11  
A1BCC N2  C6   doub Y N 12  
A1BCC C10 N4   sing Y N 13  
A1BCC C7  N4   sing Y N 14  
A1BCC C7  N3   doub Y N 15  
A1BCC C6  N3   sing Y N 16  
A1BCC C3  H6   sing N N 17  
A1BCC C3  H4   sing N N 18  
A1BCC C3  H5   sing N N 19  
A1BCC C6  H11  sing N N 20  
A1BCC C9  H12  sing N N 21  
A1BCC C1  H1   sing N N 22  
A1BCC C1  H3   sing N N 23  
A1BCC C1  H2   sing N N 24  
A1BCC C10 H13  sing N N 25  
A1BCC C4  H7   sing N N 26  
A1BCC C4  H8   sing N N 27  
A1BCC N1  H10  sing N N 28  
A1BCC N4  H14  sing N N 29  
A1BCC O1  H9   sing N N 30  
ALA   N   CA   sing N N 31  
ALA   N   H    sing N N 32  
ALA   N   H2   sing N N 33  
ALA   CA  C    sing N N 34  
ALA   CA  CB   sing N N 35  
ALA   CA  HA   sing N N 36  
ALA   C   O    doub N N 37  
ALA   C   OXT  sing N N 38  
ALA   CB  HB1  sing N N 39  
ALA   CB  HB2  sing N N 40  
ALA   CB  HB3  sing N N 41  
ALA   OXT HXT  sing N N 42  
ARG   N   CA   sing N N 43  
ARG   N   H    sing N N 44  
ARG   N   H2   sing N N 45  
ARG   CA  C    sing N N 46  
ARG   CA  CB   sing N N 47  
ARG   CA  HA   sing N N 48  
ARG   C   O    doub N N 49  
ARG   C   OXT  sing N N 50  
ARG   CB  CG   sing N N 51  
ARG   CB  HB2  sing N N 52  
ARG   CB  HB3  sing N N 53  
ARG   CG  CD   sing N N 54  
ARG   CG  HG2  sing N N 55  
ARG   CG  HG3  sing N N 56  
ARG   CD  NE   sing N N 57  
ARG   CD  HD2  sing N N 58  
ARG   CD  HD3  sing N N 59  
ARG   NE  CZ   sing N N 60  
ARG   NE  HE   sing N N 61  
ARG   CZ  NH1  sing N N 62  
ARG   CZ  NH2  doub N N 63  
ARG   NH1 HH11 sing N N 64  
ARG   NH1 HH12 sing N N 65  
ARG   NH2 HH21 sing N N 66  
ARG   NH2 HH22 sing N N 67  
ARG   OXT HXT  sing N N 68  
ASN   N   CA   sing N N 69  
ASN   N   H    sing N N 70  
ASN   N   H2   sing N N 71  
ASN   CA  C    sing N N 72  
ASN   CA  CB   sing N N 73  
ASN   CA  HA   sing N N 74  
ASN   C   O    doub N N 75  
ASN   C   OXT  sing N N 76  
ASN   CB  CG   sing N N 77  
ASN   CB  HB2  sing N N 78  
ASN   CB  HB3  sing N N 79  
ASN   CG  OD1  doub N N 80  
ASN   CG  ND2  sing N N 81  
ASN   ND2 HD21 sing N N 82  
ASN   ND2 HD22 sing N N 83  
ASN   OXT HXT  sing N N 84  
ASP   N   CA   sing N N 85  
ASP   N   H    sing N N 86  
ASP   N   H2   sing N N 87  
ASP   CA  C    sing N N 88  
ASP   CA  CB   sing N N 89  
ASP   CA  HA   sing N N 90  
ASP   C   O    doub N N 91  
ASP   C   OXT  sing N N 92  
ASP   CB  CG   sing N N 93  
ASP   CB  HB2  sing N N 94  
ASP   CB  HB3  sing N N 95  
ASP   CG  OD1  doub N N 96  
ASP   CG  OD2  sing N N 97  
ASP   OD2 HD2  sing N N 98  
ASP   OXT HXT  sing N N 99  
CYS   N   CA   sing N N 100 
CYS   N   H    sing N N 101 
CYS   N   H2   sing N N 102 
CYS   CA  C    sing N N 103 
CYS   CA  CB   sing N N 104 
CYS   CA  HA   sing N N 105 
CYS   C   O    doub N N 106 
CYS   C   OXT  sing N N 107 
CYS   CB  SG   sing N N 108 
CYS   CB  HB2  sing N N 109 
CYS   CB  HB3  sing N N 110 
CYS   SG  HG   sing N N 111 
CYS   OXT HXT  sing N N 112 
GLN   N   CA   sing N N 113 
GLN   N   H    sing N N 114 
GLN   N   H2   sing N N 115 
GLN   CA  C    sing N N 116 
GLN   CA  CB   sing N N 117 
GLN   CA  HA   sing N N 118 
GLN   C   O    doub N N 119 
GLN   C   OXT  sing N N 120 
GLN   CB  CG   sing N N 121 
GLN   CB  HB2  sing N N 122 
GLN   CB  HB3  sing N N 123 
GLN   CG  CD   sing N N 124 
GLN   CG  HG2  sing N N 125 
GLN   CG  HG3  sing N N 126 
GLN   CD  OE1  doub N N 127 
GLN   CD  NE2  sing N N 128 
GLN   NE2 HE21 sing N N 129 
GLN   NE2 HE22 sing N N 130 
GLN   OXT HXT  sing N N 131 
GLU   N   CA   sing N N 132 
GLU   N   H    sing N N 133 
GLU   N   H2   sing N N 134 
GLU   CA  C    sing N N 135 
GLU   CA  CB   sing N N 136 
GLU   CA  HA   sing N N 137 
GLU   C   O    doub N N 138 
GLU   C   OXT  sing N N 139 
GLU   CB  CG   sing N N 140 
GLU   CB  HB2  sing N N 141 
GLU   CB  HB3  sing N N 142 
GLU   CG  CD   sing N N 143 
GLU   CG  HG2  sing N N 144 
GLU   CG  HG3  sing N N 145 
GLU   CD  OE1  doub N N 146 
GLU   CD  OE2  sing N N 147 
GLU   OE2 HE2  sing N N 148 
GLU   OXT HXT  sing N N 149 
GLY   N   CA   sing N N 150 
GLY   N   H    sing N N 151 
GLY   N   H2   sing N N 152 
GLY   CA  C    sing N N 153 
GLY   CA  HA2  sing N N 154 
GLY   CA  HA3  sing N N 155 
GLY   C   O    doub N N 156 
GLY   C   OXT  sing N N 157 
GLY   OXT HXT  sing N N 158 
HIS   N   CA   sing N N 159 
HIS   N   H    sing N N 160 
HIS   N   H2   sing N N 161 
HIS   CA  C    sing N N 162 
HIS   CA  CB   sing N N 163 
HIS   CA  HA   sing N N 164 
HIS   C   O    doub N N 165 
HIS   C   OXT  sing N N 166 
HIS   CB  CG   sing N N 167 
HIS   CB  HB2  sing N N 168 
HIS   CB  HB3  sing N N 169 
HIS   CG  ND1  sing Y N 170 
HIS   CG  CD2  doub Y N 171 
HIS   ND1 CE1  doub Y N 172 
HIS   ND1 HD1  sing N N 173 
HIS   CD2 NE2  sing Y N 174 
HIS   CD2 HD2  sing N N 175 
HIS   CE1 NE2  sing Y N 176 
HIS   CE1 HE1  sing N N 177 
HIS   NE2 HE2  sing N N 178 
HIS   OXT HXT  sing N N 179 
HOH   O   H1   sing N N 180 
HOH   O   H2   sing N N 181 
ILE   N   CA   sing N N 182 
ILE   N   H    sing N N 183 
ILE   N   H2   sing N N 184 
ILE   CA  C    sing N N 185 
ILE   CA  CB   sing N N 186 
ILE   CA  HA   sing N N 187 
ILE   C   O    doub N N 188 
ILE   C   OXT  sing N N 189 
ILE   CB  CG1  sing N N 190 
ILE   CB  CG2  sing N N 191 
ILE   CB  HB   sing N N 192 
ILE   CG1 CD1  sing N N 193 
ILE   CG1 HG12 sing N N 194 
ILE   CG1 HG13 sing N N 195 
ILE   CG2 HG21 sing N N 196 
ILE   CG2 HG22 sing N N 197 
ILE   CG2 HG23 sing N N 198 
ILE   CD1 HD11 sing N N 199 
ILE   CD1 HD12 sing N N 200 
ILE   CD1 HD13 sing N N 201 
ILE   OXT HXT  sing N N 202 
LEU   N   CA   sing N N 203 
LEU   N   H    sing N N 204 
LEU   N   H2   sing N N 205 
LEU   CA  C    sing N N 206 
LEU   CA  CB   sing N N 207 
LEU   CA  HA   sing N N 208 
LEU   C   O    doub N N 209 
LEU   C   OXT  sing N N 210 
LEU   CB  CG   sing N N 211 
LEU   CB  HB2  sing N N 212 
LEU   CB  HB3  sing N N 213 
LEU   CG  CD1  sing N N 214 
LEU   CG  CD2  sing N N 215 
LEU   CG  HG   sing N N 216 
LEU   CD1 HD11 sing N N 217 
LEU   CD1 HD12 sing N N 218 
LEU   CD1 HD13 sing N N 219 
LEU   CD2 HD21 sing N N 220 
LEU   CD2 HD22 sing N N 221 
LEU   CD2 HD23 sing N N 222 
LEU   OXT HXT  sing N N 223 
LYS   N   CA   sing N N 224 
LYS   N   H    sing N N 225 
LYS   N   H2   sing N N 226 
LYS   CA  C    sing N N 227 
LYS   CA  CB   sing N N 228 
LYS   CA  HA   sing N N 229 
LYS   C   O    doub N N 230 
LYS   C   OXT  sing N N 231 
LYS   CB  CG   sing N N 232 
LYS   CB  HB2  sing N N 233 
LYS   CB  HB3  sing N N 234 
LYS   CG  CD   sing N N 235 
LYS   CG  HG2  sing N N 236 
LYS   CG  HG3  sing N N 237 
LYS   CD  CE   sing N N 238 
LYS   CD  HD2  sing N N 239 
LYS   CD  HD3  sing N N 240 
LYS   CE  NZ   sing N N 241 
LYS   CE  HE2  sing N N 242 
LYS   CE  HE3  sing N N 243 
LYS   NZ  HZ1  sing N N 244 
LYS   NZ  HZ2  sing N N 245 
LYS   NZ  HZ3  sing N N 246 
LYS   OXT HXT  sing N N 247 
MET   N   CA   sing N N 248 
MET   N   H    sing N N 249 
MET   N   H2   sing N N 250 
MET   CA  C    sing N N 251 
MET   CA  CB   sing N N 252 
MET   CA  HA   sing N N 253 
MET   C   O    doub N N 254 
MET   C   OXT  sing N N 255 
MET   CB  CG   sing N N 256 
MET   CB  HB2  sing N N 257 
MET   CB  HB3  sing N N 258 
MET   CG  SD   sing N N 259 
MET   CG  HG2  sing N N 260 
MET   CG  HG3  sing N N 261 
MET   SD  CE   sing N N 262 
MET   CE  HE1  sing N N 263 
MET   CE  HE2  sing N N 264 
MET   CE  HE3  sing N N 265 
MET   OXT HXT  sing N N 266 
PHE   N   CA   sing N N 267 
PHE   N   H    sing N N 268 
PHE   N   H2   sing N N 269 
PHE   CA  C    sing N N 270 
PHE   CA  CB   sing N N 271 
PHE   CA  HA   sing N N 272 
PHE   C   O    doub N N 273 
PHE   C   OXT  sing N N 274 
PHE   CB  CG   sing N N 275 
PHE   CB  HB2  sing N N 276 
PHE   CB  HB3  sing N N 277 
PHE   CG  CD1  doub Y N 278 
PHE   CG  CD2  sing Y N 279 
PHE   CD1 CE1  sing Y N 280 
PHE   CD1 HD1  sing N N 281 
PHE   CD2 CE2  doub Y N 282 
PHE   CD2 HD2  sing N N 283 
PHE   CE1 CZ   doub Y N 284 
PHE   CE1 HE1  sing N N 285 
PHE   CE2 CZ   sing Y N 286 
PHE   CE2 HE2  sing N N 287 
PHE   CZ  HZ   sing N N 288 
PHE   OXT HXT  sing N N 289 
PRO   N   CA   sing N N 290 
PRO   N   CD   sing N N 291 
PRO   N   H    sing N N 292 
PRO   CA  C    sing N N 293 
PRO   CA  CB   sing N N 294 
PRO   CA  HA   sing N N 295 
PRO   C   O    doub N N 296 
PRO   C   OXT  sing N N 297 
PRO   CB  CG   sing N N 298 
PRO   CB  HB2  sing N N 299 
PRO   CB  HB3  sing N N 300 
PRO   CG  CD   sing N N 301 
PRO   CG  HG2  sing N N 302 
PRO   CG  HG3  sing N N 303 
PRO   CD  HD2  sing N N 304 
PRO   CD  HD3  sing N N 305 
PRO   OXT HXT  sing N N 306 
SER   N   CA   sing N N 307 
SER   N   H    sing N N 308 
SER   N   H2   sing N N 309 
SER   CA  C    sing N N 310 
SER   CA  CB   sing N N 311 
SER   CA  HA   sing N N 312 
SER   C   O    doub N N 313 
SER   C   OXT  sing N N 314 
SER   CB  OG   sing N N 315 
SER   CB  HB2  sing N N 316 
SER   CB  HB3  sing N N 317 
SER   OG  HG   sing N N 318 
SER   OXT HXT  sing N N 319 
THR   N   CA   sing N N 320 
THR   N   H    sing N N 321 
THR   N   H2   sing N N 322 
THR   CA  C    sing N N 323 
THR   CA  CB   sing N N 324 
THR   CA  HA   sing N N 325 
THR   C   O    doub N N 326 
THR   C   OXT  sing N N 327 
THR   CB  OG1  sing N N 328 
THR   CB  CG2  sing N N 329 
THR   CB  HB   sing N N 330 
THR   OG1 HG1  sing N N 331 
THR   CG2 HG21 sing N N 332 
THR   CG2 HG22 sing N N 333 
THR   CG2 HG23 sing N N 334 
THR   OXT HXT  sing N N 335 
TYR   N   CA   sing N N 336 
TYR   N   H    sing N N 337 
TYR   N   H2   sing N N 338 
TYR   CA  C    sing N N 339 
TYR   CA  CB   sing N N 340 
TYR   CA  HA   sing N N 341 
TYR   C   O    doub N N 342 
TYR   C   OXT  sing N N 343 
TYR   CB  CG   sing N N 344 
TYR   CB  HB2  sing N N 345 
TYR   CB  HB3  sing N N 346 
TYR   CG  CD1  doub Y N 347 
TYR   CG  CD2  sing Y N 348 
TYR   CD1 CE1  sing Y N 349 
TYR   CD1 HD1  sing N N 350 
TYR   CD2 CE2  doub Y N 351 
TYR   CD2 HD2  sing N N 352 
TYR   CE1 CZ   doub Y N 353 
TYR   CE1 HE1  sing N N 354 
TYR   CE2 CZ   sing Y N 355 
TYR   CE2 HE2  sing N N 356 
TYR   CZ  OH   sing N N 357 
TYR   OH  HH   sing N N 358 
TYR   OXT HXT  sing N N 359 
VAL   N   CA   sing N N 360 
VAL   N   H    sing N N 361 
VAL   N   H2   sing N N 362 
VAL   CA  C    sing N N 363 
VAL   CA  CB   sing N N 364 
VAL   CA  HA   sing N N 365 
VAL   C   O    doub N N 366 
VAL   C   OXT  sing N N 367 
VAL   CB  CG1  sing N N 368 
VAL   CB  CG2  sing N N 369 
VAL   CB  HB   sing N N 370 
VAL   CG1 HG11 sing N N 371 
VAL   CG1 HG12 sing N N 372 
VAL   CG1 HG13 sing N N 373 
VAL   CG2 HG21 sing N N 374 
VAL   CG2 HG22 sing N N 375 
VAL   CG2 HG23 sing N N 376 
VAL   OXT HXT  sing N N 377 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HFX 
_atom_sites.fract_transf_matrix[1][1]   0.011268 
_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]   0.011268 
_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]   0.025299 
_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  
CL 
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   ? 19.737 -16.358 22.293  0.60 46.33 ?  3    VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.657 -16.334 22.368  0.40 46.20 ?  3    VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.774 -15.277 22.465  0.60 46.09 ?  3    VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.718 -15.233 22.544  0.40 45.96 ?  3    VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.425 -13.934 22.153  0.60 44.92 ?  3    VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.386 -13.905 22.212  0.40 44.88 ?  3    VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.537 -13.656 22.601  0.60 45.17 ?  3    VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.477 -13.611 22.702  0.40 45.18 ?  3    VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.159 -15.293 23.881  0.60 46.79 ?  3    VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.128 -15.221 23.970  0.40 46.58 ?  3    VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.150 -14.163 24.042  0.60 47.01 ?  3    VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.177 -14.045 24.147  0.40 46.77 ?  3    VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.504 -16.639 24.159  0.60 47.02 ?  3    VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.417 -16.535 24.263  0.40 46.78 ?  3    VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 18.051 -15.399 21.835  0.60 55.33 ?  3    VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.981 -15.347 21.929  0.40 55.17 ?  3    VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.862 -15.162 24.536  0.60 56.18 ?  3    VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.848 -15.121 24.612  0.40 55.92 ?  3    VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.649 -14.303 24.862  0.60 56.44 ?  3    VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.668 -14.172 24.963  0.40 56.15 ?  3    VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.624 -13.318 24.087  0.60 56.44 ?  3    VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.691 -13.225 24.204  0.40 56.15 ?  3    VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.547 -14.168 23.283  0.60 56.44 ?  3    VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.575 -14.009 23.387  0.40 56.15 ?  3    VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.070 -16.606 25.026  0.60 56.45 ?  3    VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.010 -16.485 25.142  0.40 56.16 ?  3    VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.848 -16.819 23.467  0.60 56.45 ?  3    VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.734 -16.681 23.590  0.40 56.16 ?  3    VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.186 -17.329 24.156  0.60 56.45 ?  3    VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.065 -17.257 24.239  0.40 56.16 ?  3    VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.731 -13.109 21.370  1.00 43.23 ?  4    ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.182 -11.760 21.048  1.00 39.66 ?  4    ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 18.045 -10.778 21.302  1.00 36.41 ?  4    ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.922 -11.163 21.644  1.00 36.15 ?  4    ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.720 -11.641 19.615  1.00 39.09 ?  4    ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.705 -12.039 18.572  1.00 38.46 ?  4    ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.610 -11.481 18.509  1.00 38.31 ?  4    ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.073 -12.994 17.724  1.00 38.24 ?  4    ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.978 -13.318 21.004  0.60 51.90 ?  4    ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 18.003 -13.336 20.965  0.40 51.90 ?  4    ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.902 -11.523 21.644  1.00 47.62 ?  4    ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.972 -10.716 19.449  1.00 46.93 ?  4    ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.493 -12.216 19.518  1.00 46.93 ?  4    ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.533 -13.253 17.108  1.00 45.91 ?  4    ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.852 -13.354 17.794  1.00 45.91 ?  4    ASN   A HD22 1 
ATOM   46   N  N    . SER   A 1 5   ? 18.347 -9.494  21.127  1.00 33.12 ?  5    SER   A N    1 
ATOM   47   C  CA   . SER   A 1 5   ? 17.449 -8.422  21.532  1.00 30.12 ?  5    SER   A CA   1 
ATOM   48   C  C    . SER   A 1 5   ? 16.543 -7.922  20.408  1.00 25.89 ?  5    SER   A C    1 
ATOM   49   O  O    . SER   A 1 5   ? 15.817 -6.944  20.611  1.00 26.60 ?  5    SER   A O    1 
ATOM   50   C  CB   . SER   A 1 5   ? 18.250 -7.262  22.127  1.00 31.28 ?  5    SER   A CB   1 
ATOM   51   O  OG   . SER   A 1 5   ? 19.161 -6.732  21.183  1.00 31.69 ?  5    SER   A OG   1 
ATOM   52   H  H    . SER   A 1 5   ? 19.084 -9.217  20.774  1.00 39.77 ?  5    SER   A H    1 
ATOM   53   H  HA   . SER   A 1 5   ? 16.879 -8.761  22.234  1.00 36.17 ?  5    SER   A HA   1 
ATOM   54   H  HB2  . SER   A 1 5   ? 17.638 -6.562  22.401  1.00 37.56 ?  5    SER   A HB2  1 
ATOM   55   H  HB3  . SER   A 1 5   ? 18.749 -7.583  22.898  1.00 37.56 ?  5    SER   A HB3  1 
ATOM   56   H  HG   . SER   A 1 5   ? 19.595 -6.094  21.526  1.00 38.05 ?  5    SER   A HG   1 
ATOM   57   N  N    A PHE   A 1 6   ? 16.561 -8.566  19.243  0.60 23.10 ?  6    PHE   A N    1 
ATOM   58   N  N    B PHE   A 1 6   ? 16.561 -8.556  19.240  0.40 23.58 ?  6    PHE   A N    1 
ATOM   59   C  CA   A PHE   A 1 6   ? 15.652 -8.183  18.171  0.60 20.42 ?  6    PHE   A CA   1 
ATOM   60   C  CA   B PHE   A 1 6   ? 15.681 -8.135  18.155  0.40 21.24 ?  6    PHE   A CA   1 
ATOM   61   C  C    A PHE   A 1 6   ? 14.225 -8.572  18.539  0.60 20.20 ?  6    PHE   A C    1 
ATOM   62   C  C    B PHE   A 1 6   ? 14.228 -8.385  18.552  0.40 20.85 ?  6    PHE   A C    1 
ATOM   63   O  O    A PHE   A 1 6   ? 13.982 -9.648  19.091  0.60 21.23 ?  6    PHE   A O    1 
ATOM   64   O  O    B PHE   A 1 6   ? 13.823 -9.533  18.761  0.40 21.10 ?  6    PHE   A O    1 
ATOM   65   C  CB   A PHE   A 1 6   ? 16.060 -8.854  16.860  0.60 18.59 ?  6    PHE   A CB   1 
ATOM   66   C  CB   B PHE   A 1 6   ? 16.033 -8.882  16.872  0.40 19.69 ?  6    PHE   A CB   1 
ATOM   67   C  CG   A PHE   A 1 6   ? 17.317 -8.286  16.255  0.60 17.18 ?  6    PHE   A CG   1 
ATOM   68   C  CG   B PHE   A 1 6   ? 17.345 -8.455  16.262  0.40 18.35 ?  6    PHE   A CG   1 
ATOM   69   C  CD1  A PHE   A 1 6   ? 17.294 -7.063  15.602  0.60 16.61 ?  6    PHE   A CD1  1 
ATOM   70   C  CD1  B PHE   A 1 6   ? 17.425 -7.308  15.488  0.40 17.67 ?  6    PHE   A CD1  1 
ATOM   71   C  CD2  A PHE   A 1 6   ? 18.515 -8.976  16.335  0.60 17.64 ?  6    PHE   A CD2  1 
ATOM   72   C  CD2  B PHE   A 1 6   ? 18.495 -9.203  16.460  0.40 18.31 ?  6    PHE   A CD2  1 
ATOM   73   C  CE1  A PHE   A 1 6   ? 18.445 -6.540  15.044  0.60 16.56 ?  6    PHE   A CE1  1 
ATOM   74   C  CE1  B PHE   A 1 6   ? 18.628 -6.914  14.925  0.40 17.22 ?  6    PHE   A CE1  1 
ATOM   75   C  CE2  A PHE   A 1 6   ? 19.665 -8.460  15.778  0.60 17.72 ?  6    PHE   A CE2  1 
ATOM   76   C  CE2  B PHE   A 1 6   ? 19.698 -8.815  15.899  0.40 17.85 ?  6    PHE   A CE2  1 
ATOM   77   C  CZ   A PHE   A 1 6   ? 19.632 -7.240  15.132  0.60 17.15 ?  6    PHE   A CZ   1 
ATOM   78   C  CZ   B PHE   A 1 6   ? 19.765 -7.668  15.130  0.40 17.27 ?  6    PHE   A CZ   1 
ATOM   79   H  H    A PHE   A 1 6   ? 17.081 -9.226  19.056  0.60 27.75 ?  6    PHE   A H    1 
ATOM   80   H  H    B PHE   A 1 6   ? 17.066 -9.226  19.052  0.40 28.32 ?  6    PHE   A H    1 
ATOM   81   H  HA   A PHE   A 1 6   ? 15.683 -7.226  18.052  0.60 24.53 ?  6    PHE   A HA   1 
ATOM   82   H  HA   B PHE   A 1 6   ? 15.795 -7.188  18.000  0.40 25.52 ?  6    PHE   A HA   1 
ATOM   83   H  HB2  A PHE   A 1 6   ? 16.210 -9.799  17.025  0.60 22.34 ?  6    PHE   A HB2  1 
ATOM   84   H  HB2  B PHE   A 1 6   ? 16.089 -9.831  17.069  0.40 23.65 ?  6    PHE   A HB2  1 
ATOM   85   H  HB3  A PHE   A 1 6   ? 15.341 -8.744  16.218  0.60 22.34 ?  6    PHE   A HB3  1 
ATOM   86   H  HB3  B PHE   A 1 6   ? 15.334 -8.724  16.219  0.40 23.65 ?  6    PHE   A HB3  1 
ATOM   87   H  HD1  A PHE   A 1 6   ? 16.494 -6.588  15.540  0.60 19.96 ?  6    PHE   A HD1  1 
ATOM   88   H  HD1  B PHE   A 1 6   ? 16.662 -6.797  15.345  0.40 21.23 ?  6    PHE   A HD1  1 
ATOM   89   H  HD2  A PHE   A 1 6   ? 18.540 -9.797  16.772  0.60 21.19 ?  6    PHE   A HD2  1 
ATOM   90   H  HD2  B PHE   A 1 6   ? 18.456 -9.974  16.976  0.40 21.99 ?  6    PHE   A HD2  1 
ATOM   91   H  HE1  A PHE   A 1 6   ? 18.417 -5.715  14.607  0.60 19.90 ?  6    PHE   A HE1  1 
ATOM   92   H  HE1  B PHE   A 1 6   ? 18.670 -6.143  14.406  0.40 20.69 ?  6    PHE   A HE1  1 
ATOM   93   H  HE2  A PHE   A 1 6   ? 20.464 -8.928  15.841  0.60 21.29 ?  6    PHE   A HE2  1 
ATOM   94   H  HE2  B PHE   A 1 6   ? 20.465 -9.324  16.039  0.40 21.44 ?  6    PHE   A HE2  1 
ATOM   95   H  HZ   A PHE   A 1 6   ? 20.405 -6.884  14.757  0.60 20.61 ?  6    PHE   A HZ   1 
ATOM   96   H  HZ   B PHE   A 1 6   ? 20.574 -7.405  14.751  0.40 20.75 ?  6    PHE   A HZ   1 
ATOM   97   N  N    A SER   A 1 7   ? 13.274 -7.686  18.232  0.60 18.95 ?  7    SER   A N    1 
ATOM   98   N  N    B SER   A 1 7   ? 13.446 -7.310  18.653  0.40 20.18 ?  7    SER   A N    1 
ATOM   99   C  CA   A SER   A 1 7   ? 11.907 -7.822  18.720  0.60 18.75 ?  7    SER   A CA   1 
ATOM   100  C  CA   B SER   A 1 7   ? 12.096 -7.354  19.199  0.40 20.21 ?  7    SER   A CA   1 
ATOM   101  C  C    A SER   A 1 7   ? 10.904 -7.510  17.616  0.60 17.07 ?  7    SER   A C    1 
ATOM   102  C  C    B SER   A 1 7   ? 11.064 -7.155  18.096  0.40 19.19 ?  7    SER   A C    1 
ATOM   103  O  O    A SER   A 1 7   ? 11.126 -6.613  16.800  0.60 16.98 ?  7    SER   A O    1 
ATOM   104  O  O    B SER   A 1 7   ? 11.229 -6.297  17.223  0.40 19.43 ?  7    SER   A O    1 
ATOM   105  C  CB   A SER   A 1 7   ? 11.672 -6.878  19.905  0.60 20.46 ?  7    SER   A CB   1 
ATOM   106  C  CB   B SER   A 1 7   ? 11.914 -6.265  20.265  0.40 21.08 ?  7    SER   A CB   1 
ATOM   107  O  OG   A SER   A 1 7   ? 10.334 -6.948  20.359  0.60 21.86 ?  7    SER   A OG   1 
ATOM   108  O  OG   B SER   A 1 7   ? 10.545 -6.079  20.577  0.40 21.92 ?  7    SER   A OG   1 
ATOM   109  H  H    A SER   A 1 7   ? 13.402 -6.997  17.734  0.60 22.77 ?  7    SER   A H    1 
ATOM   110  H  H    B SER   A 1 7   ? 13.683 -6.521  18.401  0.40 24.25 ?  7    SER   A H    1 
ATOM   111  H  HA   A SER   A 1 7   ? 11.758 -8.731  19.016  0.60 22.52 ?  7    SER   A HA   1 
ATOM   112  H  HA   B SER   A 1 7   ? 11.938 -8.212  19.620  0.40 24.28 ?  7    SER   A HA   1 
ATOM   113  H  HB2  A SER   A 1 7   ? 12.269 -7.132  20.629  0.60 24.58 ?  7    SER   A HB2  1 
ATOM   114  H  HB2  B SER   A 1 7   ? 12.380 -6.530  21.076  0.40 25.32 ?  7    SER   A HB2  1 
ATOM   115  H  HB3  A SER   A 1 7   ? 11.865 -5.968  19.627  0.60 24.58 ?  7    SER   A HB3  1 
ATOM   116  H  HB3  B SER   A 1 7   ? 12.281 -5.430  19.934  0.40 25.32 ?  7    SER   A HB3  1 
ATOM   117  H  HG   A SER   A 1 7   ? 10.228 -6.430  21.010  0.60 26.25 ?  7    SER   A HG   1 
ATOM   118  H  HG   B SER   A 1 7   ? 10.459 -5.473  21.156  0.40 26.33 ?  7    SER   A HG   1 
ATOM   119  N  N    A GLY   A 1 8   ? 9.798  -8.256  17.599  0.60 16.15 ?  8    GLY   A N    1 
ATOM   120  N  N    B GLY   A 1 8   ? 9.999  -7.955  18.141  0.40 18.17 ?  8    GLY   A N    1 
ATOM   121  C  CA   A GLY   A 1 8   ? 8.721  -7.992  16.664  0.60 15.54 ?  8    GLY   A CA   1 
ATOM   122  C  CA   B GLY   A 1 8   ? 8.871  -7.767  17.253  0.40 17.00 ?  8    GLY   A CA   1 
ATOM   123  C  C    A GLY   A 1 8   ? 8.922  -8.519  15.260  0.60 14.57 ?  8    GLY   A C    1 
ATOM   124  C  C    B GLY   A 1 8   ? 9.049  -8.278  15.844  0.40 15.75 ?  8    GLY   A C    1 
ATOM   125  O  O    A GLY   A 1 8   ? 8.182  -8.114  14.355  0.60 15.22 ?  8    GLY   A O    1 
ATOM   126  O  O    B GLY   A 1 8   ? 8.285  -7.883  14.959  0.40 16.16 ?  8    GLY   A O    1 
ATOM   127  H  H    A GLY   A 1 8   ? 9.653  -8.923  18.125  0.60 19.41 ?  8    GLY   A H    1 
ATOM   128  H  H    B GLY   A 1 8   ? 9.911  -8.612  18.682  0.40 21.83 ?  8    GLY   A H    1 
ATOM   129  H  HA2  A GLY   A 1 8   ? 7.902  -8.379  17.013  0.60 18.68 ?  8    GLY   A HA2  1 
ATOM   130  H  HA2  B GLY   A 1 8   ? 8.099  -8.215  17.632  0.40 20.43 ?  8    GLY   A HA2  1 
ATOM   131  H  HA3  A GLY   A 1 8   ? 8.592  -7.032  16.601  0.60 18.68 ?  8    GLY   A HA3  1 
ATOM   132  H  HA3  B GLY   A 1 8   ? 8.668  -6.822  17.193  0.40 20.43 ?  8    GLY   A HA3  1 
ATOM   133  N  N    A TYR   A 1 9   ? 9.892  -9.404  15.042  0.60 13.21 ?  9    TYR   A N    1 
ATOM   134  N  N    B TYR   A 1 9   ? 10.027 -9.144  15.601  0.40 14.58 ?  9    TYR   A N    1 
ATOM   135  C  CA   A TYR   A 1 9   ? 10.150 -9.962  13.721  0.60 12.19 ?  9    TYR   A CA   1 
ATOM   136  C  CA   B TYR   A 1 9   ? 10.250 -9.668  14.262  0.40 13.56 ?  9    TYR   A CA   1 
ATOM   137  C  C    A TYR   A 1 9   ? 9.265  -11.172 13.451  0.60 11.93 ?  9    TYR   A C    1 
ATOM   138  C  C    B TYR   A 1 9   ? 9.370  -10.884 13.996  0.40 12.76 ?  9    TYR   A C    1 
ATOM   139  O  O    A TYR   A 1 9   ? 8.971  -11.972 14.348  0.60 13.52 ?  9    TYR   A O    1 
ATOM   140  O  O    B TYR   A 1 9   ? 9.039  -11.650 14.906  0.40 13.84 ?  9    TYR   A O    1 
ATOM   141  C  CB   A TYR   A 1 9   ? 11.621 -10.377 13.574  0.60 12.14 ?  9    TYR   A CB   1 
ATOM   142  C  CB   B TYR   A 1 9   ? 11.726 -10.028 14.059  0.40 13.53 ?  9    TYR   A CB   1 
ATOM   143  C  CG   A TYR   A 1 9   ? 12.556 -9.199  13.414  0.60 12.24 ?  9    TYR   A CG   1 
ATOM   144  C  CG   B TYR   A 1 9   ? 12.608 -8.818  13.837  0.40 13.06 ?  9    TYR   A CG   1 
ATOM   145  C  CD1  A TYR   A 1 9   ? 12.907 -8.419  14.506  0.60 12.72 ?  9    TYR   A CD1  1 
ATOM   146  C  CD1  B TYR   A 1 9   ? 12.904 -7.953  14.881  0.40 13.12 ?  9    TYR   A CD1  1 
ATOM   147  C  CD2  A TYR   A 1 9   ? 13.070 -8.856  12.167  0.60 12.24 ?  9    TYR   A CD2  1 
ATOM   148  C  CD2  B TYR   A 1 9   ? 13.129 -8.533  12.580  0.40 12.60 ?  9    TYR   A CD2  1 
ATOM   149  C  CE1  A TYR   A 1 9   ? 13.742 -7.324  14.367  0.60 13.15 ?  9    TYR   A CE1  1 
ATOM   150  C  CE1  B TYR   A 1 9   ? 13.696 -6.842  14.683  0.40 13.09 ?  9    TYR   A CE1  1 
ATOM   151  C  CE2  A TYR   A 1 9   ? 13.907 -7.767  12.017  0.60 12.66 ?  9    TYR   A CE2  1 
ATOM   152  C  CE2  B TYR   A 1 9   ? 13.923 -7.418  12.372  0.40 12.72 ?  9    TYR   A CE2  1 
ATOM   153  C  CZ   A TYR   A 1 9   ? 14.238 -7.003  13.119  0.60 13.32 ?  9    TYR   A CZ   1 
ATOM   154  C  CZ   B TYR   A 1 9   ? 14.202 -6.579  13.428  0.40 13.00 ?  9    TYR   A CZ   1 
ATOM   155  O  OH   A TYR   A 1 9   ? 15.066 -5.924  12.967  0.60 14.27 ?  9    TYR   A OH   1 
ATOM   156  O  OH   B TYR   A 1 9   ? 14.983 -5.466  13.227  0.40 13.74 ?  9    TYR   A OH   1 
ATOM   157  H  H    A TYR   A 1 9   ? 10.415 -9.699  15.649  0.60 15.88 ?  9    TYR   A H    1 
ATOM   158  H  H    B TYR   A 1 9   ? 10.582 -9.443  16.195  0.40 17.52 ?  9    TYR   A H    1 
ATOM   159  H  HA   A TYR   A 1 9   ? 9.958  -9.293  13.045  0.60 14.65 ?  9    TYR   A HA   1 
ATOM   160  H  HA   B TYR   A 1 9   ? 10.020 -8.984  13.617  0.40 16.30 ?  9    TYR   A HA   1 
ATOM   161  H  HB2  A TYR   A 1 9   ? 11.892 -10.875 14.361  0.60 14.59 ?  9    TYR   A HB2  1 
ATOM   162  H  HB2  B TYR   A 1 9   ? 12.053 -10.504 14.838  0.40 16.26 ?  9    TYR   A HB2  1 
ATOM   163  H  HB3  A TYR   A 1 9   ? 11.708 -10.939 12.784  0.60 14.59 ?  9    TYR   A HB3  1 
ATOM   164  H  HB3  B TYR   A 1 9   ? 11.792 -10.591 13.275  0.40 16.26 ?  9    TYR   A HB3  1 
ATOM   165  H  HD1  A TYR   A 1 9   ? 12.563 -8.634  15.345  0.60 15.30 ?  9    TYR   A HD1  1 
ATOM   166  H  HD1  B TYR   A 1 9   ? 12.558 -8.129  15.728  0.40 15.78 ?  9    TYR   A HD1  1 
ATOM   167  H  HD2  A TYR   A 1 9   ? 12.845 -9.371  11.420  0.60 14.71 ?  9    TYR   A HD2  1 
ATOM   168  H  HD2  B TYR   A 1 9   ? 12.941 -9.099  11.867  0.40 15.14 ?  9    TYR   A HD2  1 
ATOM   169  H  HE1  A TYR   A 1 9   ? 13.967 -6.816  15.109  0.60 15.81 ?  9    TYR   A HE1  1 
ATOM   170  H  HE1  B TYR   A 1 9   ? 13.883 -6.273  15.394  0.40 15.74 ?  9    TYR   A HE1  1 
ATOM   171  H  HE2  A TYR   A 1 9   ? 14.250 -7.552  11.177  0.60 15.22 ?  9    TYR   A HE2  1 
ATOM   172  H  HE2  B TYR   A 1 9   ? 14.271 -7.237  11.528  0.40 15.29 ?  9    TYR   A HE2  1 
ATOM   173  H  HH   A TYR   A 1 9   ? 15.192 -5.554  13.711  0.60 17.15 ?  9    TYR   A HH   1 
ATOM   174  H  HH   B TYR   A 1 9   ? 15.078 -5.044  13.947  0.40 16.51 ?  9    TYR   A HH   1 
ATOM   175  N  N    A LEU   A 1 10  ? 8.862  -11.310 12.194  0.60 11.19 ?  10   LEU   A N    1 
ATOM   176  N  N    B LEU   A 1 10  ? 8.962  -11.024 12.736  0.40 12.01 ?  10   LEU   A N    1 
ATOM   177  C  CA   A LEU   A 1 10  ? 8.262  -12.538 11.703  0.60 10.81 ?  10   LEU   A CA   1 
ATOM   178  C  CA   B LEU   A 1 10  ? 8.305  -12.227 12.243  0.40 11.64 ?  10   LEU   A CA   1 
ATOM   179  C  C    A LEU   A 1 10  ? 9.382  -13.467 11.240  0.60 10.70 ?  10   LEU   A C    1 
ATOM   180  C  C    B LEU   A 1 10  ? 9.371  -13.191 11.739  0.40 10.79 ?  10   LEU   A C    1 
ATOM   181  O  O    A LEU   A 1 10  ? 10.316 -13.039 10.556  0.60 10.96 ?  10   LEU   A O    1 
ATOM   182  O  O    B LEU   A 1 10  ? 10.271 -12.796 10.991  0.40 10.67 ?  10   LEU   A O    1 
ATOM   183  C  CB   A LEU   A 1 10  ? 7.340  -12.220 10.526  0.60 12.25 ?  10   LEU   A CB   1 
ATOM   184  C  CB   B LEU   A 1 10  ? 7.362  -11.867 11.095  0.40 12.27 ?  10   LEU   A CB   1 
ATOM   185  C  CG   A LEU   A 1 10  ? 6.642  -13.416 9.876   0.60 14.25 ?  10   LEU   A CG   1 
ATOM   186  C  CG   B LEU   A 1 10  ? 6.571  -13.006 10.451  0.40 13.77 ?  10   LEU   A CG   1 
ATOM   187  C  CD1  A LEU   A 1 10  ? 5.604  -14.018 10.808  0.60 15.45 ?  10   LEU   A CD1  1 
ATOM   188  C  CD1  B LEU   A 1 10  ? 5.600  -13.610 11.450  0.40 14.78 ?  10   LEU   A CD1  1 
ATOM   189  C  CD2  A LEU   A 1 10  ? 6.013  -13.019 8.555   0.60 15.33 ?  10   LEU   A CD2  1 
ATOM   190  C  CD2  B LEU   A 1 10  ? 5.838  -12.480 9.231   0.40 15.33 ?  10   LEU   A CD2  1 
ATOM   191  H  H    A LEU   A 1 10  ? 8.935  -10.701 11.587  0.60 13.46 ?  10   LEU   A H    1 
ATOM   192  H  H    B LEU   A 1 10  ? 9.039  -10.407 12.140  0.40 14.44 ?  10   LEU   A H    1 
ATOM   193  H  HA   A LEU   A 1 10  ? 7.748  -12.972 12.406  0.60 13.00 ?  10   LEU   A HA   1 
ATOM   194  H  HA   B LEU   A 1 10  ? 7.793  -12.645 12.959  0.40 13.99 ?  10   LEU   A HA   1 
ATOM   195  H  HB2  A LEU   A 1 10  ? 6.643  -11.619 10.831  0.60 14.73 ?  10   LEU   A HB2  1 
ATOM   196  H  HB2  B LEU   A 1 10  ? 6.715  -11.222 11.421  0.40 14.75 ?  10   LEU   A HB2  1 
ATOM   197  H  HB3  A LEU   A 1 10  ? 7.862  -11.788 9.834   0.60 14.73 ?  10   LEU   A HB3  1 
ATOM   198  H  HB3  B LEU   A 1 10  ? 7.891  -11.460 10.393  0.40 14.75 ?  10   LEU   A HB3  1 
ATOM   199  H  HG   A LEU   A 1 10  ? 7.299  -14.109 9.689   0.60 17.12 ?  10   LEU   A HG   1 
ATOM   200  H  HG   B LEU   A 1 10  ? 7.181  -13.703 10.163  0.40 16.55 ?  10   LEU   A HG   1 
ATOM   201  H  HD11 A LEU   A 1 10  ? 5.243  -14.826 10.406  0.60 18.57 ?  10   LEU   A HD11 1 
ATOM   202  H  HD11 B LEU   A 1 10  ? 5.147  -14.362 11.038  0.40 17.76 ?  10   LEU   A HD11 1 
ATOM   203  H  HD12 A LEU   A 1 10  ? 6.022  -14.232 11.656  0.60 18.57 ?  10   LEU   A HD12 1 
ATOM   204  H  HD12 B LEU   A 1 10  ? 6.090  -13.908 12.231  0.40 17.76 ?  10   LEU   A HD12 1 
ATOM   205  H  HD13 A LEU   A 1 10  ? 4.892  -13.373 10.946  0.60 18.57 ?  10   LEU   A HD13 1 
ATOM   206  H  HD13 B LEU   A 1 10  ? 4.951  -12.935 11.707  0.40 17.76 ?  10   LEU   A HD13 1 
ATOM   207  H  HD21 A LEU   A 1 10  ? 5.574  -13.794 8.169   0.60 18.43 ?  10   LEU   A HD21 1 
ATOM   208  H  HD21 B LEU   A 1 10  ? 5.333  -13.202 8.829   0.40 18.42 ?  10   LEU   A HD21 1 
ATOM   209  H  HD22 A LEU   A 1 10  ? 5.366  -12.317 8.717   0.60 18.43 ?  10   LEU   A HD22 1 
ATOM   210  H  HD22 B LEU   A 1 10  ? 5.237  -11.769 9.508   0.40 18.42 ?  10   LEU   A HD22 1 
ATOM   211  H  HD23 A LEU   A 1 10  ? 6.710  -12.702 7.962   0.60 18.43 ?  10   LEU   A HD23 1 
ATOM   212  H  HD23 B LEU   A 1 10  ? 6.488  -12.136 8.599   0.40 18.42 ?  10   LEU   A HD23 1 
ATOM   213  N  N    A LYS   A 1 11  ? 9.282  -14.740 11.615  0.60 11.01 ?  11   LYS   A N    1 
ATOM   214  N  N    B LYS   A 1 11  ? 9.271  -14.448 12.152  0.40 11.12 ?  11   LYS   A N    1 
ATOM   215  C  CA   A LYS   A 1 11  ? 10.278 -15.744 11.261  0.60 11.01 ?  11   LYS   A CA   1 
ATOM   216  C  CA   B LYS   A 1 11  ? 10.221 -15.467 11.730  0.40 11.20 ?  11   LYS   A CA   1 
ATOM   217  C  C    A LYS   A 1 11  ? 9.919  -16.336 9.905   0.60 10.99 ?  11   LYS   A C    1 
ATOM   218  C  C    B LYS   A 1 11  ? 9.817  -15.983 10.353  0.40 10.59 ?  11   LYS   A C    1 
ATOM   219  O  O    A LYS   A 1 11  ? 8.860  -16.951 9.763   0.60 12.57 ?  11   LYS   A O    1 
ATOM   220  O  O    B LYS   A 1 11  ? 8.682  -16.429 10.161  0.40 11.17 ?  11   LYS   A O    1 
ATOM   221  C  CB   A LYS   A 1 11  ? 10.292 -16.836 12.331  0.60 11.16 ?  11   LYS   A CB   1 
ATOM   222  C  CB   B LYS   A 1 11  ? 10.239 -16.604 12.749  0.40 11.59 ?  11   LYS   A CB   1 
ATOM   223  C  CG   A LYS   A 1 11  ? 11.314 -17.943 12.130  0.60 11.47 ?  11   LYS   A CG   1 
ATOM   224  C  CG   B LYS   A 1 11  ? 11.288 -17.681 12.484  0.40 11.58 ?  11   LYS   A CG   1 
ATOM   225  C  CD   A LYS   A 1 11  ? 11.372 -18.812 13.380  0.60 12.48 ?  11   LYS   A CD   1 
ATOM   226  C  CD   B LYS   A 1 11  ? 11.398 -18.644 13.664  0.40 11.88 ?  11   LYS   A CD   1 
ATOM   227  C  CE   A LYS   A 1 11  ? 12.371 -19.953 13.266  0.60 12.77 ?  11   LYS   A CE   1 
ATOM   228  C  CE   B LYS   A 1 11  ? 12.415 -19.759 13.415  0.40 11.97 ?  11   LYS   A CE   1 
ATOM   229  N  NZ   A LYS   A 1 11  ? 13.741 -19.475 12.972  0.60 12.36 ?  11   LYS   A NZ   1 
ATOM   230  N  NZ   B LYS   A 1 11  ? 13.810 -19.246 13.340  0.40 12.14 ?  11   LYS   A NZ   1 
ATOM   231  H  H    A LYS   A 1 11  ? 8.627  -15.061 12.078  0.60 13.24 ?  11   LYS   A H    1 
ATOM   232  H  H    B LYS   A 1 11  ? 8.650  -14.729 12.675  0.40 13.37 ?  11   LYS   A H    1 
ATOM   233  H  HA   A LYS   A 1 11  ? 11.154 -15.342 11.207  0.60 13.24 ?  11   LYS   A HA   1 
ATOM   234  H  HA   B LYS   A 1 11  ? 11.105 -15.076 11.669  0.40 13.47 ?  11   LYS   A HA   1 
ATOM   235  H  HB2  A LYS   A 1 11  ? 10.483 -16.421 13.186  0.60 13.42 ?  11   LYS   A HB2  1 
ATOM   236  H  HB2  B LYS   A 1 11  ? 10.416 -16.223 13.624  0.40 13.93 ?  11   LYS   A HB2  1 
ATOM   237  H  HB3  A LYS   A 1 11  ? 9.416  -17.252 12.361  0.60 13.42 ?  11   LYS   A HB3  1 
ATOM   238  H  HB3  B LYS   A 1 11  ? 9.367  -17.027 12.748  0.40 13.93 ?  11   LYS   A HB3  1 
ATOM   239  H  HG2  A LYS   A 1 11  ? 11.049 -18.499 11.379  0.60 13.79 ?  11   LYS   A HG2  1 
ATOM   240  H  HG2  B LYS   A 1 11  ? 11.032 -18.186 11.698  0.40 13.92 ?  11   LYS   A HG2  1 
ATOM   241  H  HG3  A LYS   A 1 11  ? 12.189 -17.558 11.980  0.60 13.79 ?  11   LYS   A HG3  1 
ATOM   242  H  HG3  B LYS   A 1 11  ? 12.150 -17.260 12.351  0.40 13.92 ?  11   LYS   A HG3  1 
ATOM   243  H  HD2  A LYS   A 1 11  ? 11.625 -18.261 14.135  0.60 15.00 ?  11   LYS   A HD2  1 
ATOM   244  H  HD2  B LYS   A 1 11  ? 11.676 -18.152 14.452  0.40 14.28 ?  11   LYS   A HD2  1 
ATOM   245  H  HD3  A LYS   A 1 11  ? 10.491 -19.198 13.535  0.60 15.00 ?  11   LYS   A HD3  1 
ATOM   246  H  HD3  B LYS   A 1 11  ? 10.531 -19.055 13.820  0.40 14.28 ?  11   LYS   A HD3  1 
ATOM   247  H  HE2  A LYS   A 1 11  ? 12.394 -20.441 14.106  0.60 15.35 ?  11   LYS   A HE2  1 
ATOM   248  H  HE2  B LYS   A 1 11  ? 12.370 -20.402 14.142  0.40 14.39 ?  11   LYS   A HE2  1 
ATOM   249  H  HE3  A LYS   A 1 11  ? 12.097 -20.543 12.547  0.60 15.35 ?  11   LYS   A HE3  1 
ATOM   250  H  HE3  B LYS   A 1 11  ? 12.210 -20.198 12.573  0.40 14.39 ?  11   LYS   A HE3  1 
ATOM   251  H  HZ1  A LYS   A 1 11  ? 14.299 -20.164 12.914  0.60 14.86 ?  11   LYS   A HZ1  1 
ATOM   252  H  HZ1  B LYS   A 1 11  ? 14.329 -19.832 12.915  0.40 14.59 ?  11   LYS   A HZ1  1 
ATOM   253  H  HZ2  A LYS   A 1 11  ? 13.749 -19.029 12.202  0.60 14.86 ?  11   LYS   A HZ2  1 
ATOM   254  H  HZ2  B LYS   A 1 11  ? 13.827 -18.473 12.899  0.40 14.59 ?  11   LYS   A HZ2  1 
ATOM   255  H  HZ3  A LYS   A 1 11  ? 14.019 -18.932 13.622  0.60 14.86 ?  11   LYS   A HZ3  1 
ATOM   256  H  HZ3  B LYS   A 1 11  ? 14.132 -19.117 14.160  0.40 14.59 ?  11   LYS   A HZ3  1 
ATOM   257  N  N    A LEU   A 1 12  ? 10.798 -16.174 8.914   0.60 10.16 ?  12   LEU   A N    1 
ATOM   258  N  N    B LEU   A 1 12  ? 10.730 -15.898 9.389   0.40 10.68 ?  12   LEU   A N    1 
ATOM   259  C  CA   A LEU   A 1 12  ? 10.534 -16.757 7.599   0.60 10.82 ?  12   LEU   A CA   1 
ATOM   260  C  CA   B LEU   A 1 12  ? 10.472 -16.409 8.050   0.40 11.04 ?  12   LEU   A CA   1 
ATOM   261  C  C    A LEU   A 1 12  ? 11.111 -18.162 7.444   0.60 10.97 ?  12   LEU   A C    1 
ATOM   262  C  C    B LEU   A 1 12  ? 11.054 -17.797 7.826   0.40 10.65 ?  12   LEU   A C    1 
ATOM   263  O  O    A LEU   A 1 12  ? 10.464 -19.031 6.852   0.60 11.25 ?  12   LEU   A O    1 
ATOM   264  O  O    B LEU   A 1 12  ? 10.405 -18.641 7.200   0.40 10.62 ?  12   LEU   A O    1 
ATOM   265  C  CB   A LEU   A 1 12  ? 11.072 -15.856 6.482   0.60 10.88 ?  12   LEU   A CB   1 
ATOM   266  C  CB   B LEU   A 1 12  ? 11.031 -15.452 6.993   0.40 11.69 ?  12   LEU   A CB   1 
ATOM   267  C  CG   A LEU   A 1 12  ? 10.425 -14.480 6.311   0.60 12.19 ?  12   LEU   A CG   1 
ATOM   268  C  CG   B LEU   A 1 12  ? 10.363 -14.083 6.893   0.40 12.21 ?  12   LEU   A CG   1 
ATOM   269  C  CD1  A LEU   A 1 12  ? 11.138 -13.723 5.211   0.60 13.00 ?  12   LEU   A CD1  1 
ATOM   270  C  CD1  B LEU   A 1 12  ? 11.023 -13.263 5.797   0.40 12.61 ?  12   LEU   A CD1  1 
ATOM   271  C  CD2  A LEU   A 1 12  ? 8.938  -14.596 5.998   0.60 13.13 ?  12   LEU   A CD2  1 
ATOM   272  C  CD2  B LEU   A 1 12  ? 8.866  -14.238 6.637   0.40 12.94 ?  12   LEU   A CD2  1 
ATOM   273  H  H    A LEU   A 1 12  ? 11.546 -15.740 8.972   0.60 12.21 ?  12   LEU   A H    1 
ATOM   274  H  H    B LEU   A 1 12  ? 11.507 -15.531 9.487   0.40 12.84 ?  12   LEU   A H    1 
ATOM   275  H  HA   A LEU   A 1 12  ? 9.577  -16.827 7.484   0.60 13.01 ?  12   LEU   A HA   1 
ATOM   276  H  HA   B LEU   A 1 12  ? 9.514  -16.464 7.921   0.40 13.27 ?  12   LEU   A HA   1 
ATOM   277  H  HB2  A LEU   A 1 12  ? 12.014 -15.708 6.642   0.60 13.08 ?  12   LEU   A HB2  1 
ATOM   278  H  HB2  B LEU   A 1 12  ? 11.968 -15.296 7.185   0.40 14.06 ?  12   LEU   A HB2  1 
ATOM   279  H  HB3  A LEU   A 1 12  ? 10.961 -16.329 5.640   0.60 13.08 ?  12   LEU   A HB3  1 
ATOM   280  H  HB3  B LEU   A 1 12  ? 10.944 -15.874 6.126   0.40 14.06 ?  12   LEU   A HB3  1 
ATOM   281  H  HG   A LEU   A 1 12  ? 10.519 -13.980 7.132   0.60 14.66 ?  12   LEU   A HG   1 
ATOM   282  H  HG   B LEU   A 1 12  ? 10.475 -13.609 7.734   0.40 14.68 ?  12   LEU   A HG   1 
ATOM   283  H  HD11 A LEU   A 1 12  ? 10.722 -12.853 5.104   0.60 15.63 ?  12   LEU   A HD11 1 
ATOM   284  H  HD11 B LEU   A 1 12  ? 10.588 -12.397 5.744   0.40 15.16 ?  12   LEU   A HD11 1 
ATOM   285  H  HD12 A LEU   A 1 12  ? 12.070 -13.616 5.455   0.60 15.63 ?  12   LEU   A HD12 1 
ATOM   286  H  HD12 B LEU   A 1 12  ? 11.961 -13.151 6.011   0.40 15.16 ?  12   LEU   A HD12 1 
ATOM   287  H  HD13 A LEU   A 1 12  ? 11.069 -14.226 4.382   0.60 15.63 ?  12   LEU   A HD13 1 
ATOM   288  H  HD13 B LEU   A 1 12  ? 10.928 -13.732 4.953   0.40 15.16 ?  12   LEU   A HD13 1 
ATOM   289  H  HD21 A LEU   A 1 12  ? 8.584  -13.714 5.799   0.60 15.79 ?  12   LEU   A HD21 1 
ATOM   290  H  HD21 B LEU   A 1 12  ? 8.497  -13.381 6.373   0.40 15.56 ?  12   LEU   A HD21 1 
ATOM   291  H  HD22 A LEU   A 1 12  ? 8.817  -15.179 5.230   0.60 15.79 ?  12   LEU   A HD22 1 
ATOM   292  H  HD22 B LEU   A 1 12  ? 8.733  -14.888 5.929   0.40 15.56 ?  12   LEU   A HD22 1 
ATOM   293  H  HD23 A LEU   A 1 12  ? 8.477  -14.969 6.768   0.60 15.79 ?  12   LEU   A HD23 1 
ATOM   294  H  HD23 B LEU   A 1 12  ? 8.434  -14.546 7.451   0.40 15.56 ?  12   LEU   A HD23 1 
ATOM   295  N  N    A THR   A 1 13  ? 12.328 -18.382 7.933   0.60 10.92 ?  13   THR   A N    1 
ATOM   296  N  N    B THR   A 1 13  ? 12.269 -18.045 8.310   0.40 10.14 ?  13   THR   A N    1 
ATOM   297  C  CA   A THR   A 1 13  ? 13.010 -19.669 7.849   0.60 11.47 ?  13   THR   A CA   1 
ATOM   298  C  CA   B THR   A 1 13  ? 12.931 -19.333 8.153   0.40 10.58 ?  13   THR   A CA   1 
ATOM   299  C  C    A THR   A 1 13  ? 13.782 -19.866 9.144   0.60 11.74 ?  13   THR   A C    1 
ATOM   300  C  C    B THR   A 1 13  ? 13.728 -19.636 9.414   0.40 11.19 ?  13   THR   A C    1 
ATOM   301  O  O    A THR   A 1 13  ? 13.702 -19.046 10.065  0.60 12.08 ?  13   THR   A O    1 
ATOM   302  O  O    B THR   A 1 13  ? 13.652 -18.927 10.422  0.40 11.12 ?  13   THR   A O    1 
ATOM   303  C  CB   A THR   A 1 13  ? 13.977 -19.729 6.661   0.60 11.84 ?  13   THR   A CB   1 
ATOM   304  C  CB   B THR   A 1 13  ? 13.889 -19.342 6.954   0.40 10.82 ?  13   THR   A CB   1 
ATOM   305  O  OG1  A THR   A 1 13  ? 15.052 -18.818 6.896   0.60 12.02 ?  13   THR   A OG1  1 
ATOM   306  O  OG1  B THR   A 1 13  ? 14.956 -18.427 7.210   0.40 10.48 ?  13   THR   A OG1  1 
ATOM   307  C  CG2  A THR   A 1 13  ? 13.282 -19.394 5.352   0.60 13.12 ?  13   THR   A CG2  1 
ATOM   308  C  CG2  B THR   A 1 13  ? 13.186 -18.976 5.651   0.40 11.18 ?  13   THR   A CG2  1 
ATOM   309  H  H    A THR   A 1 13  ? 12.798 -17.781 8.324   0.60 13.13 ?  13   THR   A H    1 
ATOM   310  H  H    B THR   A 1 13  ? 12.740 -17.459 8.728   0.40 12.20 ?  13   THR   A H    1 
ATOM   311  H  HA   A THR   A 1 13  ? 12.358 -20.384 7.750   0.60 13.79 ?  13   THR   A HA   1 
ATOM   312  H  HA   B THR   A 1 13  ? 12.269 -20.027 8.029   0.40 12.73 ?  13   THR   A HA   1 
ATOM   313  H  HB   A THR   A 1 13  ? 14.348 -20.621 6.587   0.60 14.23 ?  13   THR   A HB   1 
ATOM   314  H  HB   B THR   A 1 13  ? 14.267 -20.224 6.849   0.40 13.01 ?  13   THR   A HB   1 
ATOM   315  H  HG1  A THR   A 1 13  ? 15.584 -18.816 6.240   0.60 14.46 ?  13   THR   A HG1  1 
ATOM   316  H  HG1  B THR   A 1 13  ? 15.485 -18.401 6.552   0.40 12.60 ?  13   THR   A HG1  1 
ATOM   317  H  HG21 A THR   A 1 13  ? 13.861 -19.615 4.605   0.60 15.77 ?  13   THR   A HG21 1 
ATOM   318  H  HG21 B THR   A 1 13  ? 13.810 -19.044 4.907   0.40 13.44 ?  13   THR   A HG21 1 
ATOM   319  H  HG22 A THR   A 1 13  ? 12.464 -19.911 5.276   0.60 15.77 ?  13   THR   A HG22 1 
ATOM   320  H  HG22 B THR   A 1 13  ? 12.448 -19.588 5.493   0.40 13.44 ?  13   THR   A HG22 1 
ATOM   321  H  HG23 A THR   A 1 13  ? 13.065 -18.452 5.320   0.60 15.77 ?  13   THR   A HG23 1 
ATOM   322  H  HG23 B THR   A 1 13  ? 12.844 -18.073 5.693   0.40 13.44 ?  13   THR   A HG23 1 
ATOM   323  N  N    A ASP   A 1 14  ? 14.576 -20.938 9.201   0.60 12.40 ?  14   ASP   A N    1 
ATOM   324  N  N    B ASP   A 1 14  ? 14.524 -20.700 9.316   0.40 11.99 ?  14   ASP   A N    1 
ATOM   325  C  CA   A ASP   A 1 14  ? 15.402 -21.160 10.381  0.60 13.13 ?  14   ASP   A CA   1 
ATOM   326  C  CA   B ASP   A 1 14  ? 15.425 -21.102 10.386  0.40 12.59 ?  14   ASP   A CA   1 
ATOM   327  C  C    A ASP   A 1 14  ? 16.218 -19.919 10.730  0.60 12.45 ?  14   ASP   A C    1 
ATOM   328  C  C    B ASP   A 1 14  ? 16.316 -19.957 10.857  0.40 12.10 ?  14   ASP   A C    1 
ATOM   329  O  O    A ASP   A 1 14  ? 16.371 -19.583 11.910  0.60 12.79 ?  14   ASP   A O    1 
ATOM   330  O  O    B ASP   A 1 14  ? 16.680 -19.907 12.036  0.40 11.94 ?  14   ASP   A O    1 
ATOM   331  C  CB   A ASP   A 1 14  ? 16.344 -22.341 10.164  0.60 15.09 ?  14   ASP   A CB   1 
ATOM   332  C  CB   B ASP   A 1 14  ? 16.273 -22.278 9.892   0.40 13.98 ?  14   ASP   A CB   1 
ATOM   333  C  CG   A ASP   A 1 14  ? 17.285 -22.534 11.324  0.60 18.01 ?  14   ASP   A CG   1 
ATOM   334  C  CG   B ASP   A 1 14  ? 17.134 -22.878 10.990  0.40 15.94 ?  14   ASP   A CG   1 
ATOM   335  O  OD1  A ASP   A 1 14  ? 16.819 -22.937 12.409  0.60 19.05 ?  14   ASP   A OD1  1 
ATOM   336  O  OD1  B ASP   A 1 14  ? 16.570 -23.284 12.031  0.40 16.45 ?  14   ASP   A OD1  1 
ATOM   337  O  OD2  A ASP   A 1 14  ? 18.488 -22.257 11.148  0.60 19.71 -1 14   ASP   A OD2  1 
ATOM   338  O  OD2  B ASP   A 1 14  ? 18.367 -22.956 10.812  0.40 17.18 -1 14   ASP   A OD2  1 
ATOM   339  H  H    A ASP   A 1 14  ? 14.666 -21.535 8.577   0.60 14.91 ?  14   ASP   A H    1 
ATOM   340  H  H    B ASP   A 1 14  ? 14.552 -21.202 8.629   0.40 14.41 ?  14   ASP   A H    1 
ATOM   341  H  HA   A ASP   A 1 14  ? 14.827 -21.374 11.134  0.60 15.78 ?  14   ASP   A HA   1 
ATOM   342  H  HA   B ASP   A 1 14  ? 14.905 -21.400 11.143  0.40 15.13 ?  14   ASP   A HA   1 
ATOM   343  H  HB2  A ASP   A 1 14  ? 15.815 -23.154 10.032  0.60 18.14 ?  14   ASP   A HB2  1 
ATOM   344  H  HB2  B ASP   A 1 14  ? 15.674 -22.979 9.565   0.40 16.81 ?  14   ASP   A HB2  1 
ATOM   345  H  HB3  A ASP   A 1 14  ? 16.896 -22.180 9.389   0.60 18.14 ?  14   ASP   A HB3  1 
ATOM   346  H  HB3  B ASP   A 1 14  ? 16.837 -21.977 9.156   0.40 16.81 ?  14   ASP   A HB3  1 
ATOM   347  N  N    A ASN   A 1 15  ? 16.746 -19.219 9.715   0.60 11.17 ?  15   ASN   A N    1 
ATOM   348  N  N    B ASN   A 1 15  ? 16.666 -19.017 9.968   0.40 11.67 ?  15   ASN   A N    1 
ATOM   349  C  CA   A ASN   A 1 15  ? 17.748 -18.177 9.934   0.60 11.13 ?  15   ASN   A CA   1 
ATOM   350  C  CA   B ASN   A 1 15  ? 17.646 -17.992 10.314  0.40 11.14 ?  15   ASN   A CA   1 
ATOM   351  C  C    A ASN   A 1 15  ? 17.379 -16.791 9.411   0.60 11.17 ?  15   ASN   A C    1 
ATOM   352  C  C    B ASN   A 1 15  ? 17.282 -16.576 9.893   0.40 10.29 ?  15   ASN   A C    1 
ATOM   353  O  O    A ASN   A 1 15  ? 18.175 -15.860 9.590   0.60 11.82 ?  15   ASN   A O    1 
ATOM   354  O  O    B ASN   A 1 15  ? 18.045 -15.658 10.207  0.40 10.00 ?  15   ASN   A O    1 
ATOM   355  C  CB   A ASN   A 1 15  ? 19.103 -18.601 9.339   0.60 10.83 ?  15   ASN   A CB   1 
ATOM   356  C  CB   B ASN   A 1 15  ? 19.037 -18.330 9.739   0.40 11.53 ?  15   ASN   A CB   1 
ATOM   357  C  CG   A ASN   A 1 15  ? 19.079 -18.654 7.829   0.60 11.27 ?  15   ASN   A CG   1 
ATOM   358  C  CG   B ASN   A 1 15  ? 19.028 -18.513 8.233   0.40 11.58 ?  15   ASN   A CG   1 
ATOM   359  O  OD1  A ASN   A 1 15  ? 18.393 -19.489 7.244   0.60 11.69 ?  15   ASN   A OD1  1 
ATOM   360  O  OD1  B ASN   A 1 15  ? 18.197 -19.246 7.692   0.40 11.90 ?  15   ASN   A OD1  1 
ATOM   361  N  ND2  A ASN   A 1 15  ? 19.811 -17.750 7.186   0.60 11.39 ?  15   ASN   A ND2  1 
ATOM   362  N  ND2  B ASN   A 1 15  ? 19.950 -17.839 7.544   0.40 12.04 ?  15   ASN   A ND2  1 
ATOM   363  H  H    A ASN   A 1 15  ? 16.546 -19.350 8.890   0.60 13.43 ?  15   ASN   A H    1 
ATOM   364  H  H    B ASN   A 1 15  ? 16.337 -18.939 9.180   0.40 14.03 ?  15   ASN   A H    1 
ATOM   365  H  HA   A ASN   A 1 15  ? 17.884 -18.090 10.884  0.60 13.38 ?  15   ASN   A HA   1 
ATOM   366  H  HA   B ASN   A 1 15  ? 17.743 -17.979 11.279  0.40 13.40 ?  15   ASN   A HA   1 
ATOM   367  H  HB2  A ASN   A 1 15  ? 19.785 -17.960 9.603   0.60 13.02 ?  15   ASN   A HB2  1 
ATOM   368  H  HB2  B ASN   A 1 15  ? 19.647 -17.601 9.950   0.40 13.87 ?  15   ASN   A HB2  1 
ATOM   369  H  HB3  A ASN   A 1 15  ? 19.344 -19.487 9.667   0.60 13.02 ?  15   ASN   A HB3  1 
ATOM   370  H  HB3  B ASN   A 1 15  ? 19.349 -19.151 10.134  0.40 13.87 ?  15   ASN   A HB3  1 
ATOM   371  H  HD21 A ASN   A 1 15  ? 19.831 -17.745 6.326   0.60 13.69 ?  15   ASN   A HD21 1 
ATOM   372  H  HD21 B ASN   A 1 15  ? 19.988 -17.907 6.684   0.40 14.48 ?  15   ASN   A HD21 1 
ATOM   373  H  HD22 A ASN   A 1 15  ? 20.281 -17.183 7.630   0.60 13.69 ?  15   ASN   A HD22 1 
ATOM   374  H  HD22 B ASN   A 1 15  ? 20.516 -17.338 7.955   0.40 14.48 ?  15   ASN   A HD22 1 
ATOM   375  N  N    A VAL   A 1 16  ? 16.220 -16.615 8.778   0.60 10.84 ?  16   VAL   A N    1 
ATOM   376  N  N    B VAL   A 1 16  ? 16.160 -16.358 9.211   0.40 10.18 ?  16   VAL   A N    1 
ATOM   377  C  CA   A VAL   A 1 16  ? 15.825 -15.337 8.194   0.60 10.56 ?  16   VAL   A CA   1 
ATOM   378  C  CA   B VAL   A 1 16  ? 15.805 -15.049 8.673   0.40 9.78  ?  16   VAL   A CA   1 
ATOM   379  C  C    A VAL   A 1 16  ? 14.557 -14.836 8.883   0.60 10.12 ?  16   VAL   A C    1 
ATOM   380  C  C    B VAL   A 1 16  ? 14.535 -14.552 9.356   0.40 9.92  ?  16   VAL   A C    1 
ATOM   381  O  O    A VAL   A 1 16  ? 13.558 -15.560 8.979   0.60 9.84  ?  16   VAL   A O    1 
ATOM   382  O  O    B VAL   A 1 16  ? 13.544 -15.287 9.463   0.40 10.36 ?  16   VAL   A O    1 
ATOM   383  C  CB   A VAL   A 1 16  ? 15.624 -15.436 6.671   0.60 11.39 ?  16   VAL   A CB   1 
ATOM   384  C  CB   B VAL   A 1 16  ? 15.651 -15.078 7.139   0.40 9.68  ?  16   VAL   A CB   1 
ATOM   385  C  CG1  A VAL   A 1 16  ? 15.151 -14.105 6.110   0.60 11.88 ?  16   VAL   A CG1  1 
ATOM   386  C  CG1  B VAL   A 1 16  ? 15.331 -13.684 6.604   0.40 9.76  ?  16   VAL   A CG1  1 
ATOM   387  C  CG2  A VAL   A 1 16  ? 16.906 -15.887 5.980   0.60 11.87 ?  16   VAL   A CG2  1 
ATOM   388  C  CG2  B VAL   A 1 16  ? 16.912 -15.611 6.483   0.40 10.69 ?  16   VAL   A CG2  1 
ATOM   389  H  H    A VAL   A 1 16  ? 15.631 -17.241 8.682   0.60 13.03 ?  16   VAL   A H    1 
ATOM   390  H  H    B VAL   A 1 16  ? 15.574 -16.965 9.055   0.40 12.24 ?  16   VAL   A H    1 
ATOM   391  H  HA   A VAL   A 1 16  ? 16.532 -14.693 8.356   0.60 12.70 ?  16   VAL   A HA   1 
ATOM   392  H  HA   B VAL   A 1 16  ? 16.510 -14.420 8.883   0.40 11.76 ?  16   VAL   A HA   1 
ATOM   393  H  HB   A VAL   A 1 16  ? 14.943 -16.106 6.490   0.60 13.70 ?  16   VAL   A HB   1 
ATOM   394  H  HB   B VAL   A 1 16  ? 14.915 -15.667 6.905   0.40 11.64 ?  16   VAL   A HB   1 
ATOM   395  H  HG11 A VAL   A 1 16  ? 15.224 -14.131 5.144   0.60 14.29 ?  16   VAL   A HG11 1 
ATOM   396  H  HG11 B VAL   A 1 16  ? 15.378 -13.700 5.636   0.40 11.74 ?  16   VAL   A HG11 1 
ATOM   397  H  HG12 A VAL   A 1 16  ? 14.227 -13.967 6.367   0.60 14.29 ?  16   VAL   A HG12 1 
ATOM   398  H  HG12 B VAL   A 1 16  ? 14.439 -13.433 6.887   0.40 11.74 ?  16   VAL   A HG12 1 
ATOM   399  H  HG13 A VAL   A 1 16  ? 15.708 -13.400 6.468   0.60 14.29 ?  16   VAL   A HG13 1 
ATOM   400  H  HG13 B VAL   A 1 16  ? 15.980 -13.056 6.957   0.40 11.74 ?  16   VAL   A HG13 1 
ATOM   401  H  HG21 A VAL   A 1 16  ? 16.805 -15.768 5.023   0.60 14.27 ?  16   VAL   A HG21 1 
ATOM   402  H  HG21 B VAL   A 1 16  ? 16.967 -15.274 5.576   0.40 12.86 ?  16   VAL   A HG21 1 
ATOM   403  H  HG22 A VAL   A 1 16  ? 17.645 -15.345 6.302   0.60 14.27 ?  16   VAL   A HG22 1 
ATOM   404  H  HG22 B VAL   A 1 16  ? 17.679 -15.320 6.995   0.40 12.86 ?  16   VAL   A HG22 1 
ATOM   405  H  HG23 A VAL   A 1 16  ? 17.071 -16.821 6.183   0.60 14.27 ?  16   VAL   A HG23 1 
ATOM   406  H  HG23 B VAL   A 1 16  ? 16.874 -16.581 6.474   0.40 12.86 ?  16   VAL   A HG23 1 
ATOM   407  N  N    A TYR   A 1 17  ? 14.597 -13.570 9.308   0.60 9.90  ?  17   TYR   A N    1 
ATOM   408  N  N    B TYR   A 1 17  ? 14.570 -13.293 9.794   0.40 9.61  ?  17   TYR   A N    1 
ATOM   409  C  CA   A TYR   A 1 17  ? 13.529 -12.890 10.024  0.60 9.98  ?  17   TYR   A CA   1 
ATOM   410  C  CA   B TYR   A 1 17  ? 13.483 -12.622 10.491  0.40 9.56  ?  17   TYR   A CA   1 
ATOM   411  C  C    A TYR   A 1 17  ? 13.256 -11.561 9.328   0.60 10.18 ?  17   TYR   A C    1 
ATOM   412  C  C    B TYR   A 1 17  ? 13.234 -11.286 9.811   0.40 9.69  ?  17   TYR   A C    1 
ATOM   413  O  O    A TYR   A 1 17  ? 14.147 -11.006 8.681   0.60 10.34 ?  17   TYR   A O    1 
ATOM   414  O  O    B TYR   A 1 17  ? 14.143 -10.723 9.198   0.40 9.45  ?  17   TYR   A O    1 
ATOM   415  C  CB   A TYR   A 1 17  ? 13.978 -12.641 11.469  0.60 10.40 ?  17   TYR   A CB   1 
ATOM   416  C  CB   B TYR   A 1 17  ? 13.869 -12.381 11.952  0.40 10.35 ?  17   TYR   A CB   1 
ATOM   417  C  CG   A TYR   A 1 17  ? 14.173 -13.912 12.276  0.60 11.17 ?  17   TYR   A CG   1 
ATOM   418  C  CG   B TYR   A 1 17  ? 14.082 -13.660 12.724  0.40 10.97 ?  17   TYR   A CG   1 
ATOM   419  C  CD1  A TYR   A 1 17  ? 15.328 -14.679 12.156  0.60 11.80 ?  17   TYR   A CD1  1 
ATOM   420  C  CD1  B TYR   A 1 17  ? 15.275 -14.372 12.630  0.40 11.16 ?  17   TYR   A CD1  1 
ATOM   421  C  CD2  A TYR   A 1 17  ? 13.199 -14.343 13.161  0.60 11.90 ?  17   TYR   A CD2  1 
ATOM   422  C  CD2  B TYR   A 1 17  ? 13.084 -14.164 13.540  0.40 11.79 ?  17   TYR   A CD2  1 
ATOM   423  C  CE1  A TYR   A 1 17  ? 15.495 -15.852 12.893  0.60 12.29 ?  17   TYR   A CE1  1 
ATOM   424  C  CE1  B TYR   A 1 17  ? 15.462 -15.552 13.335  0.40 11.96 ?  17   TYR   A CE1  1 
ATOM   425  C  CE2  A TYR   A 1 17  ? 13.358 -15.506 13.901  0.60 12.56 ?  17   TYR   A CE2  1 
ATOM   426  C  CE2  B TYR   A 1 17  ? 13.259 -15.341 14.244  0.40 12.39 ?  17   TYR   A CE2  1 
ATOM   427  C  CZ   A TYR   A 1 17  ? 14.506 -16.254 13.768  0.60 12.78 ?  17   TYR   A CZ   1 
ATOM   428  C  CZ   B TYR   A 1 17  ? 14.447 -16.031 14.141  0.40 12.31 ?  17   TYR   A CZ   1 
ATOM   429  O  OH   A TYR   A 1 17  ? 14.655 -17.410 14.508  0.60 13.77 ?  17   TYR   A OH   1 
ATOM   430  O  OH   B TYR   A 1 17  ? 14.612 -17.199 14.850  0.40 13.24 ?  17   TYR   A OH   1 
ATOM   431  H  H    A TYR   A 1 17  ? 15.284 -13.063 9.176   0.60 11.91 ?  17   TYR   A H    1 
ATOM   432  H  H    B TYR   A 1 17  ? 15.251 -12.773 9.680   0.40 11.55 ?  17   TYR   A H    1 
ATOM   433  H  HA   A TYR   A 1 17  ? 12.729 -13.436 10.017  0.60 12.00 ?  17   TYR   A HA   1 
ATOM   434  H  HA   B TYR   A 1 17  ? 12.673 -13.146 10.450  0.40 11.50 ?  17   TYR   A HA   1 
ATOM   435  H  HB2  A TYR   A 1 17  ? 14.824 -12.169 11.459  0.60 12.51 ?  17   TYR   A HB2  1 
ATOM   436  H  HB2  B TYR   A 1 17  ? 14.694 -11.875 11.972  0.40 12.45 ?  17   TYR   A HB2  1 
ATOM   437  H  HB3  A TYR   A 1 17  ? 13.307 -12.112 11.915  0.60 12.51 ?  17   TYR   A HB3  1 
ATOM   438  H  HB3  B TYR   A 1 17  ? 13.163 -11.879 12.390  0.40 12.45 ?  17   TYR   A HB3  1 
ATOM   439  H  HD1  A TYR   A 1 17  ? 16.000 -14.419 11.567  0.60 14.19 ?  17   TYR   A HD1  1 
ATOM   440  H  HD1  B TYR   A 1 17  ? 15.958 -14.046 12.084  0.40 13.42 ?  17   TYR   A HD1  1 
ATOM   441  H  HD2  A TYR   A 1 17  ? 12.421 -13.851 13.259  0.60 14.31 ?  17   TYR   A HD2  1 
ATOM   442  H  HD2  B TYR   A 1 17  ? 12.278 -13.705 13.613  0.40 14.17 ?  17   TYR   A HD2  1 
ATOM   443  H  HE1  A TYR   A 1 17  ? 16.276 -16.356 12.804  0.60 14.77 ?  17   TYR   A HE1  1 
ATOM   444  H  HE1  B TYR   A 1 17  ? 16.268 -16.015 13.259  0.40 14.38 ?  17   TYR   A HE1  1 
ATOM   445  H  HE2  A TYR   A 1 17  ? 12.693 -15.781 14.494  0.60 15.10 ?  17   TYR   A HE2  1 
ATOM   446  H  HE2  B TYR   A 1 17  ? 12.581 -15.668 14.788  0.40 14.89 ?  17   TYR   A HE2  1 
ATOM   447  H  HH   A TYR   A 1 17  ? 13.963 -17.549 14.969  0.60 16.55 ?  17   TYR   A HH   1 
ATOM   448  H  HH   B TYR   A 1 17  ? 13.862 -17.504 15.076  0.40 15.92 ?  17   TYR   A HH   1 
ATOM   449  N  N    A ILE   A 1 18  ? 12.031 -11.035 9.458   0.60 10.12 ?  18   ILE   A N    1 
ATOM   450  N  N    B ILE   A 1 18  ? 12.010 -10.763 9.919   0.40 9.91  ?  18   ILE   A N    1 
ATOM   451  C  CA   A ILE   A 1 18  ? 11.645 -9.832  8.716   0.60 10.61 ?  18   ILE   A CA   1 
ATOM   452  C  CA   B ILE   A 1 18  ? 11.640 -9.551  9.192   0.40 9.69  ?  18   ILE   A CA   1 
ATOM   453  C  C    A ILE   A 1 18  ? 10.680 -8.981  9.537   0.60 11.27 ?  18   ILE   A C    1 
ATOM   454  C  C    B ILE   A 1 18  ? 10.727 -8.676  10.042  0.40 9.76  ?  18   ILE   A C    1 
ATOM   455  O  O    A ILE   A 1 18  ? 9.855  -9.500  10.294  0.60 11.64 ?  18   ILE   A O    1 
ATOM   456  O  O    B ILE   A 1 18  ? 9.883  -9.177  10.793  0.40 10.00 ?  18   ILE   A O    1 
ATOM   457  C  CB   A ILE   A 1 18  ? 11.073 -10.213 7.328   0.60 10.82 ?  18   ILE   A CB   1 
ATOM   458  C  CB   B ILE   A 1 18  ? 11.015 -9.885  7.821   0.40 9.38  ?  18   ILE   A CB   1 
ATOM   459  C  CG1  A ILE   A 1 18  ? 11.027 -8.995  6.406   0.60 10.84 ?  18   ILE   A CG1  1 
ATOM   460  C  CG1  B ILE   A 1 18  ? 10.924 -8.636  6.945   0.40 9.91  ?  18   ILE   A CG1  1 
ATOM   461  C  CG2  A ILE   A 1 18  ? 9.708  -10.905 7.465   0.60 11.34 ?  18   ILE   A CG2  1 
ATOM   462  C  CG2  B ILE   A 1 18  ? 9.647  -10.537 7.992   0.40 9.57  ?  18   ILE   A CG2  1 
ATOM   463  C  CD1  A ILE   A 1 18  ? 10.737 -9.354  4.974   0.60 12.50 ?  18   ILE   A CD1  1 
ATOM   464  C  CD1  B ILE   A 1 18  ? 10.599 -8.948  5.510   0.40 11.24 ?  18   ILE   A CD1  1 
ATOM   465  H  H    A ILE   A 1 18  ? 11.418 -11.365 9.965   0.60 12.17 ?  18   ILE   A H    1 
ATOM   466  H  H    B ILE   A 1 18  ? 11.380 -11.089 10.411  0.40 11.92 ?  18   ILE   A H    1 
ATOM   467  H  HA   A ILE   A 1 18  ? 12.441 -9.308  8.564   0.60 12.76 ?  18   ILE   A HA   1 
ATOM   468  H  HA   B ILE   A 1 18  ? 12.445 -9.039  9.026   0.40 11.66 ?  18   ILE   A HA   1 
ATOM   469  H  HB   A ILE   A 1 18  ? 11.679 -10.859 6.929   0.60 13.01 ?  18   ILE   A HB   1 
ATOM   470  H  HB   B ILE   A 1 18  ? 11.599 -10.516 7.380   0.40 11.28 ?  18   ILE   A HB   1 
ATOM   471  H  HG12 A ILE   A 1 18  ? 10.337 -8.394  6.711   0.60 13.03 ?  18   ILE   A HG12 1 
ATOM   472  H  HG12 B ILE   A 1 18  ? 10.224 -8.057  7.292   0.40 11.92 ?  18   ILE   A HG12 1 
ATOM   473  H  HG13 A ILE   A 1 18  ? 11.892 -8.555  6.430   0.60 13.03 ?  18   ILE   A HG13 1 
ATOM   474  H  HG13 B ILE   A 1 18  ? 11.775 -8.170  6.966   0.40 11.92 ?  18   ILE   A HG13 1 
ATOM   475  H  HG21 A ILE   A 1 18  ? 9.453  -11.278 6.604   0.60 13.64 ?  18   ILE   A HG21 1 
ATOM   476  H  HG21 B ILE   A 1 18  ? 9.361  -10.896 7.136   0.40 11.51 ?  18   ILE   A HG21 1 
ATOM   477  H  HG22 A ILE   A 1 18  ? 9.778  -11.618 8.121   0.60 13.64 ?  18   ILE   A HG22 1 
ATOM   478  H  HG22 B ILE   A 1 18  ? 9.717  -11.254 8.641   0.40 11.51 ?  18   ILE   A HG22 1 
ATOM   479  H  HG23 A ILE   A 1 18  ? 9.049  -10.256 7.752   0.60 13.64 ?  18   ILE   A HG23 1 
ATOM   480  H  HG23 B ILE   A 1 18  ? 9.011  -9.873  8.300   0.40 11.51 ?  18   ILE   A HG23 1 
ATOM   481  H  HD11 A ILE   A 1 18  ? 10.785 -8.548  4.434   0.60 15.02 ?  18   ILE   A HD11 1 
ATOM   482  H  HD11 B ILE   A 1 18  ? 10.625 -8.128  4.994   0.40 13.51 ?  18   ILE   A HD11 1 
ATOM   483  H  HD12 A ILE   A 1 18  ? 11.391 -9.998  4.667   0.60 15.02 ?  18   ILE   A HD12 1 
ATOM   484  H  HD12 B ILE   A 1 18  ? 11.256 -9.576  5.169   0.40 13.51 ?  18   ILE   A HD12 1 
ATOM   485  H  HD13 A ILE   A 1 18  ? 9.845  -9.733  4.919   0.60 15.02 ?  18   ILE   A HD13 1 
ATOM   486  H  HD13 B ILE   A 1 18  ? 9.713  -9.341  5.464   0.40 13.51 ?  18   ILE   A HD13 1 
ATOM   487  N  N    A LYS   A 1 19  ? 10.766 -7.659  9.355   0.60 11.54 ?  19   LYS   A N    1 
ATOM   488  N  N    B LYS   A 1 19  ? 10.903 -7.360  9.915   0.40 9.97  ?  19   LYS   A N    1 
ATOM   489  C  CA   A LYS   A 1 19  ? 9.957  -6.709  10.110  0.60 12.84 ?  19   LYS   A CA   1 
ATOM   490  C  CA   B LYS   A 1 19  ? 10.136 -6.383  10.677  0.40 10.54 ?  19   LYS   A CA   1 
ATOM   491  C  C    A LYS   A 1 19  ? 9.763  -5.440  9.286   0.60 13.31 ?  19   LYS   A C    1 
ATOM   492  C  C    B LYS   A 1 19  ? 9.905  -5.152  9.811   0.40 11.33 ?  19   LYS   A C    1 
ATOM   493  O  O    A LYS   A 1 19  ? 10.648 -5.040  8.524   0.60 13.43 ?  19   LYS   A O    1 
ATOM   494  O  O    B LYS   A 1 19  ? 10.760 -4.776  9.006   0.40 11.41 ?  19   LYS   A O    1 
ATOM   495  C  CB   A LYS   A 1 19  ? 10.667 -6.372  11.429  0.60 14.05 ?  19   LYS   A CB   1 
ATOM   496  C  CB   B LYS   A 1 19  ? 10.896 -5.986  11.953  0.40 11.24 ?  19   LYS   A CB   1 
ATOM   497  C  CG   A LYS   A 1 19  ? 9.939  -5.428  12.380  0.60 15.23 ?  19   LYS   A CG   1 
ATOM   498  C  CG   B LYS   A 1 19  ? 10.165 -5.058  12.910  0.40 12.49 ?  19   LYS   A CG   1 
ATOM   499  C  CD   A LYS   A 1 19  ? 10.835 -5.148  13.586  0.60 16.46 ?  19   LYS   A CD   1 
ATOM   500  C  CD   B LYS   A 1 19  ? 11.092 -4.669  14.060  0.40 13.22 ?  19   LYS   A CD   1 
ATOM   501  C  CE   A LYS   A 1 19  ? 10.195 -4.215  14.595  0.60 17.17 ?  19   LYS   A CE   1 
ATOM   502  C  CE   B LYS   A 1 19  ? 10.393 -3.819  15.106  0.40 14.11 ?  19   LYS   A CE   1 
ATOM   503  N  NZ   A LYS   A 1 19  ? 11.115 -3.962  15.744  0.60 17.43 ?  19   LYS   A NZ   1 
ATOM   504  N  NZ   B LYS   A 1 19  ? 11.265 -3.604  16.296  0.40 14.59 ?  19   LYS   A NZ   1 
ATOM   505  H  H    A LYS   A 1 19  ? 11.295 -7.293  8.789   0.60 13.87 ?  19   LYS   A H    1 
ATOM   506  H  H    B LYS   A 1 19  ? 11.492 -6.995  9.398   0.40 12.00 ?  19   LYS   A H    1 
ATOM   507  H  HA   A LYS   A 1 19  ? 9.086  -7.107  10.307  0.60 15.43 ?  19   LYS   A HA   1 
ATOM   508  H  HA   B LYS   A 1 19  ? 9.282  -6.763  10.938  0.40 12.68 ?  19   LYS   A HA   1 
ATOM   509  H  HB2  A LYS   A 1 19  ? 10.819 -7.202  11.906  0.60 16.88 ?  19   LYS   A HB2  1 
ATOM   510  H  HB2  B LYS   A 1 19  ? 11.105 -6.787  12.456  0.40 13.51 ?  19   LYS   A HB2  1 
ATOM   511  H  HB3  A LYS   A 1 19  ? 11.517 -5.965  11.209  0.60 16.88 ?  19   LYS   A HB3  1 
ATOM   512  H  HB3  B LYS   A 1 19  ? 11.720 -5.539  11.700  0.40 13.51 ?  19   LYS   A HB3  1 
ATOM   513  H  HG2  A LYS   A 1 19  ? 9.749  -4.591  11.930  0.60 18.31 ?  19   LYS   A HG2  1 
ATOM   514  H  HG2  B LYS   A 1 19  ? 9.896  -4.250  12.450  0.40 15.02 ?  19   LYS   A HG2  1 
ATOM   515  H  HG3  A LYS   A 1 19  ? 9.119  -5.845  12.691  0.60 18.31 ?  19   LYS   A HG3  1 
ATOM   516  H  HG3  B LYS   A 1 19  ? 9.393  -5.512  13.285  0.40 15.02 ?  19   LYS   A HG3  1 
ATOM   517  H  HD2  A LYS   A 1 19  ? 11.031 -5.986  14.036  0.60 19.78 ?  19   LYS   A HD2  1 
ATOM   518  H  HD2  B LYS   A 1 19  ? 11.407 -5.473  14.498  0.40 15.89 ?  19   LYS   A HD2  1 
ATOM   519  H  HD3  A LYS   A 1 19  ? 11.659 -4.739  13.278  0.60 19.78 ?  19   LYS   A HD3  1 
ATOM   520  H  HD3  B LYS   A 1 19  ? 11.841 -4.162  13.709  0.40 15.89 ?  19   LYS   A HD3  1 
ATOM   521  H  HE2  A LYS   A 1 19  ? 9.998  -3.364  14.170  0.60 20.63 ?  19   LYS   A HE2  1 
ATOM   522  H  HE2  B LYS   A 1 19  ? 10.178 -2.952  14.726  0.40 16.96 ?  19   LYS   A HE2  1 
ATOM   523  H  HE3  A LYS   A 1 19  ? 9.382  -4.616  14.938  0.60 20.63 ?  19   LYS   A HE3  1 
ATOM   524  H  HE3  B LYS   A 1 19  ? 9.585  -4.269  15.398  0.40 16.96 ?  19   LYS   A HE3  1 
ATOM   525  H  HZ1  A LYS   A 1 19  ? 10.722 -3.430  16.338  0.60 20.94 ?  19   LYS   A HZ1  1 
ATOM   526  H  HZ1  B LYS   A 1 19  ? 10.828 -3.133  16.913  0.40 17.53 ?  19   LYS   A HZ1  1 
ATOM   527  H  HZ2  A LYS   A 1 19  ? 11.327 -4.731  16.138  0.60 20.94 ?  19   LYS   A HZ2  1 
ATOM   528  H  HZ2  B LYS   A 1 19  ? 11.502 -4.387  16.646  0.40 17.53 ?  19   LYS   A HZ2  1 
ATOM   529  H  HZ3  A LYS   A 1 19  ? 11.861 -3.572  15.454  0.60 20.94 ?  19   LYS   A HZ3  1 
ATOM   530  H  HZ3  B LYS   A 1 19  ? 11.998 -3.158  16.061  0.40 17.53 ?  19   LYS   A HZ3  1 
ATOM   531  N  N    A ASN   A 1 20  ? 8.592  -4.811  9.435   0.60 14.08 ?  20   ASN   A N    1 
ATOM   532  N  N    B ASN   A 1 20  ? 8.740  -4.527  9.983   0.40 12.63 ?  20   ASN   A N    1 
ATOM   533  C  CA   A ASN   A 1 20  ? 8.367  -3.474  8.886   0.60 15.69 ?  20   ASN   A CA   1 
ATOM   534  C  CA   B ASN   A 1 20  ? 8.417  -3.274  9.300   0.40 14.28 ?  20   ASN   A CA   1 
ATOM   535  C  C    A ASN   A 1 20  ? 8.981  -2.472  9.856   0.60 16.09 ?  20   ASN   A C    1 
ATOM   536  C  C    B ASN   A 1 20  ? 9.005  -2.135  10.123  0.40 14.93 ?  20   ASN   A C    1 
ATOM   537  O  O    A ASN   A 1 20  ? 8.460  -2.261  10.956  0.60 16.76 ?  20   ASN   A O    1 
ATOM   538  O  O    B ASN   A 1 20  ? 8.387  -1.667  11.083  0.40 16.01 ?  20   ASN   A O    1 
ATOM   539  C  CB   A ASN   A 1 20  ? 6.875  -3.203  8.680   0.60 16.77 ?  20   ASN   A CB   1 
ATOM   540  C  CB   B ASN   A 1 20  ? 6.902  -3.128  9.162   0.40 15.06 ?  20   ASN   A CB   1 
ATOM   541  C  CG   A ASN   A 1 20  ? 6.567  -1.717  8.446   0.60 18.17 ?  20   ASN   A CG   1 
ATOM   542  C  CG   B ASN   A 1 20  ? 6.475  -1.921  8.311   0.40 16.10 ?  20   ASN   A CG   1 
ATOM   543  O  OD1  A ASN   A 1 20  ? 5.713  -1.131  9.120   0.60 19.53 ?  20   ASN   A OD1  1 
ATOM   544  O  OD1  B ASN   A 1 20  ? 5.306  -1.508  8.349   0.40 16.20 ?  20   ASN   A OD1  1 
ATOM   545  N  ND2  A ASN   A 1 20  ? 7.264  -1.108  7.495   0.60 18.34 ?  20   ASN   A ND2  1 
ATOM   546  N  ND2  B ASN   A 1 20  ? 7.408  -1.360  7.544   0.40 16.85 ?  20   ASN   A ND2  1 
ATOM   547  H  H    A ASN   A 1 20  ? 7.910  -5.142  9.853   0.60 16.92 ?  20   ASN   A H    1 
ATOM   548  H  H    B ASN   A 1 20  ? 8.113  -4.813  10.493  0.40 15.18 ?  20   ASN   A H    1 
ATOM   549  H  HA   A ASN   A 1 20  ? 8.812  -3.401  8.029   0.60 18.85 ?  20   ASN   A HA   1 
ATOM   550  H  HA   B ASN   A 1 20  ? 8.828  -3.277  8.423   0.40 17.16 ?  20   ASN   A HA   1 
ATOM   551  H  HB2  A ASN   A 1 20  ? 6.566  -3.700  7.902   0.60 20.16 ?  20   ASN   A HB2  1 
ATOM   552  H  HB2  B ASN   A 1 20  ? 6.550  -3.928  8.749   0.40 18.09 ?  20   ASN   A HB2  1 
ATOM   553  H  HB3  A ASN   A 1 20  ? 6.387  -3.493  9.467   0.60 20.16 ?  20   ASN   A HB3  1 
ATOM   554  H  HB3  B ASN   A 1 20  ? 6.521  -3.019  10.048  0.40 18.09 ?  20   ASN   A HB3  1 
ATOM   555  H  HD21 A ASN   A 1 20  ? 7.128  -0.276  7.330   0.60 22.04 ?  20   ASN   A HD21 1 
ATOM   556  H  HD21 B ASN   A 1 20  ? 7.203  -0.685  7.057   0.40 20.25 ?  20   ASN   A HD21 1 
ATOM   557  H  HD22 A ASN   A 1 20  ? 7.855  -1.545  7.047   0.60 22.04 ?  20   ASN   A HD22 1 
ATOM   558  H  HD22 B ASN   A 1 20  ? 8.211  -1.666  7.528   0.40 20.25 ?  20   ASN   A HD22 1 
ATOM   559  N  N    A ALA   A 1 21  ? 10.103 -1.873  9.470   0.60 16.48 ?  21   ALA   A N    1 
ATOM   560  N  N    B ALA   A 1 21  ? 10.207 -1.688  9.756   0.40 14.99 ?  21   ALA   A N    1 
ATOM   561  C  CA   A ALA   A 1 21  ? 10.788 -0.966  10.378  0.60 16.19 ?  21   ALA   A CA   1 
ATOM   562  C  CA   B ALA   A 1 21  ? 10.856 -0.598  10.469  0.40 14.98 ?  21   ALA   A CA   1 
ATOM   563  C  C    A ALA   A 1 21  ? 11.751 -0.086  9.601   0.60 15.86 ?  21   ALA   A C    1 
ATOM   564  C  C    B ALA   A 1 21  ? 11.972 -0.023  9.610   0.40 14.14 ?  21   ALA   A C    1 
ATOM   565  O  O    A ALA   A 1 21  ? 12.195 -0.432  8.503   0.60 15.53 ?  21   ALA   A O    1 
ATOM   566  O  O    B ALA   A 1 21  ? 12.513 -0.704  8.736   0.40 14.01 ?  21   ALA   A O    1 
ATOM   567  C  CB   A ALA   A 1 21  ? 11.538 -1.729  11.473  0.60 16.82 ?  21   ALA   A CB   1 
ATOM   568  C  CB   B ALA   A 1 21  ? 11.406 -1.060  11.826  0.40 15.86 ?  21   ALA   A CB   1 
ATOM   569  H  H    A ALA   A 1 21  ? 10.481 -1.982  8.705   0.60 19.80 ?  21   ALA   A H    1 
ATOM   570  H  H    B ALA   A 1 21  ? 10.671 -2.002  9.100   0.40 18.01 ?  21   ALA   A H    1 
ATOM   571  H  HA   A ALA   A 1 21  ? 10.127 -0.393  10.802  0.60 19.45 ?  21   ALA   A HA   1 
ATOM   572  H  HA   B ALA   A 1 21  ? 10.214 0.105   10.631  0.40 18.00 ?  21   ALA   A HA   1 
ATOM   573  H  HB1  A ALA   A 1 21  ? 11.965 -1.088  12.060  0.60 20.21 ?  21   ALA   A HB1  1 
ATOM   574  H  HB1  B ALA   A 1 21  ? 11.830 -0.306  12.269  0.40 19.06 ?  21   ALA   A HB1  1 
ATOM   575  H  HB2  A ALA   A 1 21  ? 10.901 -2.265  11.974  0.60 20.21 ?  21   ALA   A HB2  1 
ATOM   576  H  HB2  B ALA   A 1 21  ? 10.671 -1.388  12.370  0.40 19.06 ?  21   ALA   A HB2  1 
ATOM   577  H  HB3  A ALA   A 1 21  ? 12.200 -2.300  11.060  0.60 20.21 ?  21   ALA   A HB3  1 
ATOM   578  H  HB3  B ALA   A 1 21  ? 12.054 -1.767  11.685  0.40 19.06 ?  21   ALA   A HB3  1 
ATOM   579  N  N    A ASP   A 1 22  ? 12.050 1.068   10.197  0.60 15.94 ?  22   ASP   A N    1 
ATOM   580  N  N    B ASP   A 1 22  ? 12.277 1.251   9.852   0.40 13.64 ?  22   ASP   A N    1 
ATOM   581  C  CA   A ASP   A 1 22  ? 13.084 1.970   9.714   0.60 15.93 ?  22   ASP   A CA   1 
ATOM   582  C  CA   B ASP   A 1 22  ? 13.481 1.868   9.311   0.40 13.33 ?  22   ASP   A CA   1 
ATOM   583  C  C    A ASP   A 1 22  ? 14.422 1.481   10.257  0.60 14.81 ?  22   ASP   A C    1 
ATOM   584  C  C    B ASP   A 1 22  ? 14.693 1.187   9.935   0.40 12.40 ?  22   ASP   A C    1 
ATOM   585  O  O    A ASP   A 1 22  ? 14.638 1.477   11.473  0.60 15.19 ?  22   ASP   A O    1 
ATOM   586  O  O    B ASP   A 1 22  ? 14.777 1.056   11.159  0.40 12.26 ?  22   ASP   A O    1 
ATOM   587  C  CB   A ASP   A 1 22  ? 12.777 3.377   10.224  0.60 17.62 ?  22   ASP   A CB   1 
ATOM   588  C  CB   B ASP   A 1 22  ? 13.484 3.359   9.669   0.40 14.32 ?  22   ASP   A CB   1 
ATOM   589  C  CG   A ASP   A 1 22  ? 13.775 4.418   9.741   0.60 19.05 ?  22   ASP   A CG   1 
ATOM   590  C  CG   B ASP   A 1 22  ? 14.530 4.167   8.901   0.40 14.70 ?  22   ASP   A CG   1 
ATOM   591  O  OD1  A ASP   A 1 22  ? 14.836 4.051   9.202   0.60 18.99 ?  22   ASP   A OD1  1 
ATOM   592  O  OD1  B ASP   A 1 22  ? 15.476 3.572   8.344   0.40 14.32 ?  22   ASP   A OD1  1 
ATOM   593  O  OD2  A ASP   A 1 22  ? 13.495 5.623   9.908   0.60 20.43 -1 22   ASP   A OD2  1 
ATOM   594  O  OD2  B ASP   A 1 22  ? 14.407 5.413   8.868   0.40 15.40 -1 22   ASP   A OD2  1 
ATOM   595  H  H    A ASP   A 1 22  ? 11.644 1.358   10.899  0.60 19.16 ?  22   ASP   A H    1 
ATOM   596  H  H    B ASP   A 1 22  ? 11.791 1.783   10.321  0.40 16.40 ?  22   ASP   A H    1 
ATOM   597  H  HA   A ASP   A 1 22  ? 13.108 1.975   8.743   0.60 19.15 ?  22   ASP   A HA   1 
ATOM   598  H  HA   B ASP   A 1 22  ? 13.508 1.763   8.345   0.40 16.03 ?  22   ASP   A HA   1 
ATOM   599  H  HB2  A ASP   A 1 22  ? 11.890 3.638   9.924   0.60 21.17 ?  22   ASP   A HB2  1 
ATOM   600  H  HB2  B ASP   A 1 22  ? 12.611 3.729   9.473   0.40 17.22 ?  22   ASP   A HB2  1 
ATOM   601  H  HB3  A ASP   A 1 22  ? 12.806 3.375   11.194  0.60 21.17 ?  22   ASP   A HB3  1 
ATOM   602  H  HB3  B ASP   A 1 22  ? 13.676 3.446   10.615  0.40 17.22 ?  22   ASP   A HB3  1 
ATOM   603  N  N    A ILE   A 1 23  ? 15.314 1.056   9.358   0.60 14.07 ?  23   ILE   A N    1 
ATOM   604  N  N    B ILE   A 1 23  ? 15.625 0.732   9.093   0.40 11.88 ?  23   ILE   A N    1 
ATOM   605  C  CA   A ILE   A 1 23  ? 16.580 0.459   9.782   0.60 13.34 ?  23   ILE   A CA   1 
ATOM   606  C  CA   B ILE   A 1 23  ? 16.838 0.097   9.603   0.40 11.45 ?  23   ILE   A CA   1 
ATOM   607  C  C    A ILE   A 1 23  ? 17.390 1.418   10.645  0.60 13.13 ?  23   ILE   A C    1 
ATOM   608  C  C    B ILE   A 1 23  ? 17.583 1.043   10.533  0.40 11.63 ?  23   ILE   A C    1 
ATOM   609  O  O    A ILE   A 1 23  ? 18.131 0.984   11.534  0.60 13.33 ?  23   ILE   A O    1 
ATOM   610  O  O    B ILE   A 1 23  ? 18.224 0.607   11.496  0.40 11.63 ?  23   ILE   A O    1 
ATOM   611  C  CB   A ILE   A 1 23  ? 17.370 -0.060  8.560   0.60 12.86 ?  23   ILE   A CB   1 
ATOM   612  C  CB   B ILE   A 1 23  ? 17.725 -0.413  8.444   0.40 10.71 ?  23   ILE   A CB   1 
ATOM   613  C  CG1  A ILE   A 1 23  ? 18.553 -0.922  9.014   0.60 12.94 ?  23   ILE   A CG1  1 
ATOM   614  C  CG1  B ILE   A 1 23  ? 18.824 -1.338  8.981   0.40 10.97 ?  23   ILE   A CG1  1 
ATOM   615  C  CG2  A ILE   A 1 23  ? 17.812 1.097   7.665   0.60 12.86 ?  23   ILE   A CG2  1 
ATOM   616  C  CG2  B ILE   A 1 23  ? 18.328 0.749   7.655   0.40 10.76 ?  23   ILE   A CG2  1 
ATOM   617  C  CD1  A ILE   A 1 23  ? 19.276 -1.612  7.876   0.60 12.88 ?  23   ILE   A CD1  1 
ATOM   618  C  CD1  B ILE   A 1 23  ? 19.618 -2.050  7.896   0.40 11.05 ?  23   ILE   A CD1  1 
ATOM   619  H  H    A ILE   A 1 23  ? 15.203 1.098   8.511   0.60 16.91 ?  23   ILE   A H    1 
ATOM   620  H  H    B ILE   A 1 23  ? 15.584 0.778   8.245   0.40 14.29 ?  23   ILE   A H    1 
ATOM   621  H  HA   A ILE   A 1 23  ? 16.379 -0.309  10.335  0.60 16.04 ?  23   ILE   A HA   1 
ATOM   622  H  HA   B ILE   A 1 23  ? 16.578 -0.677  10.122  0.40 13.77 ?  23   ILE   A HA   1 
ATOM   623  H  HB   A ILE   A 1 23  ? 16.776 -0.622  8.046   0.60 15.46 ?  23   ILE   A HB   1 
ATOM   624  H  HB   B ILE   A 1 23  ? 17.171 -0.931  7.840   0.40 12.88 ?  23   ILE   A HB   1 
ATOM   625  H  HG12 A ILE   A 1 23  ? 19.196 -0.362  9.475   0.60 15.55 ?  23   ILE   A HG12 1 
ATOM   626  H  HG12 B ILE   A 1 23  ? 19.448 -0.812  9.505   0.40 13.19 ?  23   ILE   A HG12 1 
ATOM   627  H  HG13 A ILE   A 1 23  ? 18.227 -1.611  9.616   0.60 15.55 ?  23   ILE   A HG13 1 
ATOM   628  H  HG13 B ILE   A 1 23  ? 18.415 -2.017  9.540   0.40 13.19 ?  23   ILE   A HG13 1 
ATOM   629  H  HG21 A ILE   A 1 23  ? 18.176 0.738   6.841   0.60 15.46 ?  23   ILE   A HG21 1 
ATOM   630  H  HG21 B ILE   A 1 23  ? 18.727 0.401   6.838   0.40 12.93 ?  23   ILE   A HG21 1 
ATOM   631  H  HG22 A ILE   A 1 23  ? 17.040 1.654   7.467   0.60 15.46 ?  23   ILE   A HG22 1 
ATOM   632  H  HG22 B ILE   A 1 23  ? 17.626 1.377   7.436   0.40 12.93 ?  23   ILE   A HG22 1 
ATOM   633  H  HG23 A ILE   A 1 23  ? 18.485 1.620   8.126   0.60 15.46 ?  23   ILE   A HG23 1 
ATOM   634  H  HG23 B ILE   A 1 23  ? 19.008 1.180   8.194   0.40 12.93 ?  23   ILE   A HG23 1 
ATOM   635  H  HD11 A ILE   A 1 23  ? 19.954 -2.200  8.244   0.60 15.49 ?  23   ILE   A HD11 1 
ATOM   636  H  HD11 B ILE   A 1 23  ? 20.245 -2.664  8.315   0.40 13.29 ?  23   ILE   A HD11 1 
ATOM   637  H  HD12 A ILE   A 1 23  ? 18.635 -2.127  7.362   0.60 15.49 ?  23   ILE   A HD12 1 
ATOM   638  H  HD12 B ILE   A 1 23  ? 19.007 -2.543  7.327   0.40 13.29 ?  23   ILE   A HD12 1 
ATOM   639  H  HD13 A ILE   A 1 23  ? 19.691 -0.941  7.313   0.60 15.49 ?  23   ILE   A HD13 1 
ATOM   640  H  HD13 B ILE   A 1 23  ? 20.102 -1.393  7.372   0.40 13.29 ?  23   ILE   A HD13 1 
ATOM   641  N  N    A VAL   A 1 24  ? 17.254 2.727   10.418  0.60 13.50 ?  24   VAL   A N    1 
ATOM   642  N  N    B VAL   A 1 24  ? 17.496 2.348   10.272  0.40 13.00 ?  24   VAL   A N    1 
ATOM   643  C  CA   A VAL   A 1 24  ? 17.947 3.703   11.258  0.60 14.51 ?  24   VAL   A CA   1 
ATOM   644  C  CA   B VAL   A 1 24  ? 18.130 3.338   11.136  0.40 14.12 ?  24   VAL   A CA   1 
ATOM   645  C  C    A VAL   A 1 24  ? 17.464 3.601   12.698  0.60 15.14 ?  24   VAL   A C    1 
ATOM   646  C  C    B VAL   A 1 24  ? 17.533 3.283   12.536  0.40 14.92 ?  24   VAL   A C    1 
ATOM   647  O  O    A VAL   A 1 24  ? 18.263 3.537   13.641  0.60 15.28 ?  24   VAL   A O    1 
ATOM   648  O  O    B VAL   A 1 24  ? 18.259 3.298   13.537  0.40 15.33 ?  24   VAL   A O    1 
ATOM   649  C  CB   A VAL   A 1 24  ? 17.758 5.124   10.699  0.60 15.16 ?  24   VAL   A CB   1 
ATOM   650  C  CB   B VAL   A 1 24  ? 17.999 4.737   10.506  0.40 14.90 ?  24   VAL   A CB   1 
ATOM   651  C  CG1  A VAL   A 1 24  ? 18.252 6.170   11.699  0.60 15.57 ?  24   VAL   A CG1  1 
ATOM   652  C  CG1  B VAL   A 1 24  ? 18.567 5.798   11.430  0.40 15.67 ?  24   VAL   A CG1  1 
ATOM   653  C  CG2  A VAL   A 1 24  ? 18.477 5.268   9.370   0.60 15.91 ?  24   VAL   A CG2  1 
ATOM   654  C  CG2  B VAL   A 1 24  ? 18.687 4.767   9.146   0.40 15.10 ?  24   VAL   A CG2  1 
ATOM   655  H  H    A VAL   A 1 24  ? 16.780 3.072   9.791   0.60 16.23 ?  24   VAL   A H    1 
ATOM   656  H  H    B VAL   A 1 24  ? 17.078 2.680   9.605   0.40 15.63 ?  24   VAL   A H    1 
ATOM   657  H  HA   A VAL   A 1 24  ? 18.896 3.512   11.252  0.60 17.44 ?  24   VAL   A HA   1 
ATOM   658  H  HA   B VAL   A 1 24  ? 19.075 3.134   11.212  0.40 16.97 ?  24   VAL   A HA   1 
ATOM   659  H  HB   A VAL   A 1 24  ? 16.813 5.284   10.544  0.60 18.22 ?  24   VAL   A HB   1 
ATOM   660  H  HB   B VAL   A 1 24  ? 17.060 4.931   10.366  0.40 17.91 ?  24   VAL   A HB   1 
ATOM   661  H  HG11 A VAL   A 1 24  ? 18.385 7.012   11.234  0.60 18.71 ?  24   VAL   A HG11 1 
ATOM   662  H  HG11 B VAL   A 1 24  ? 18.667 6.623   10.931  0.40 18.83 ?  24   VAL   A HG11 1 
ATOM   663  H  HG12 A VAL   A 1 24  ? 17.590 6.282   12.397  0.60 18.71 ?  24   VAL   A HG12 1 
ATOM   664  H  HG12 B VAL   A 1 24  ? 17.955 5.931   12.170  0.40 18.83 ?  24   VAL   A HG12 1 
ATOM   665  H  HG13 A VAL   A 1 24  ? 19.093 5.870   12.079  0.60 18.71 ?  24   VAL   A HG13 1 
ATOM   666  H  HG13 B VAL   A 1 24  ? 19.429 5.501   11.757  0.40 18.83 ?  24   VAL   A HG13 1 
ATOM   667  H  HG21 A VAL   A 1 24  ? 18.236 6.119   8.970   0.60 19.12 ?  24   VAL   A HG21 1 
ATOM   668  H  HG21 B VAL   A 1 24  ? 18.593 5.653   8.765   0.40 18.15 ?  24   VAL   A HG21 1 
ATOM   669  H  HG22 A VAL   A 1 24  ? 19.434 5.238   9.526   0.60 19.12 ?  24   VAL   A HG22 1 
ATOM   670  H  HG22 B VAL   A 1 24  ? 19.627 4.557   9.263   0.40 18.15 ?  24   VAL   A HG22 1 
ATOM   671  H  HG23 A VAL   A 1 24  ? 18.212 4.542   8.786   0.60 19.12 ?  24   VAL   A HG23 1 
ATOM   672  H  HG23 B VAL   A 1 24  ? 18.272 4.112   8.562   0.40 18.15 ?  24   VAL   A HG23 1 
ATOM   673  N  N    A GLU   A 1 25  ? 16.143 3.594   12.888  0.60 16.20 ?  25   GLU   A N    1 
ATOM   674  N  N    B GLU   A 1 25  ? 16.202 3.205   12.629  0.40 15.54 ?  25   GLU   A N    1 
ATOM   675  C  CA   A GLU   A 1 25  ? 15.590 3.530   14.235  0.60 17.76 ?  25   GLU   A CA   1 
ATOM   676  C  CA   B GLU   A 1 25  ? 15.555 3.138   13.936  0.40 16.93 ?  25   GLU   A CA   1 
ATOM   677  C  C    A GLU   A 1 25  ? 15.834 2.171   14.872  0.60 17.10 ?  25   GLU   A C    1 
ATOM   678  C  C    B GLU   A 1 25  ? 15.825 1.801   14.617  0.40 16.67 ?  25   GLU   A C    1 
ATOM   679  O  O    A GLU   A 1 25  ? 16.065 2.088   16.083  0.60 17.58 ?  25   GLU   A O    1 
ATOM   680  O  O    B GLU   A 1 25  ? 16.068 1.756   15.829  0.40 16.89 ?  25   GLU   A O    1 
ATOM   681  C  CB   A GLU   A 1 25  ? 14.097 3.860   14.202  0.60 20.04 ?  25   GLU   A CB   1 
ATOM   682  C  CB   B GLU   A 1 25  ? 14.054 3.409   13.796  0.40 18.48 ?  25   GLU   A CB   1 
ATOM   683  C  CG   A GLU   A 1 25  ? 13.813 5.302   13.811  0.60 22.37 ?  25   GLU   A CG   1 
ATOM   684  C  CG   B GLU   A 1 25  ? 13.735 4.813   13.301  0.40 20.37 ?  25   GLU   A CG   1 
ATOM   685  C  CD   A GLU   A 1 25  ? 14.578 6.302   14.664  0.60 24.47 ?  25   GLU   A CD   1 
ATOM   686  C  CD   B GLU   A 1 25  ? 14.198 5.881   14.265  0.40 21.95 ?  25   GLU   A CD   1 
ATOM   687  O  OE1  A GLU   A 1 25  ? 14.608 6.131   15.901  0.60 25.12 ?  25   GLU   A OE1  1 
ATOM   688  O  OE1  B GLU   A 1 25  ? 14.171 5.628   15.489  0.40 22.63 ?  25   GLU   A OE1  1 
ATOM   689  O  OE2  A GLU   A 1 25  ? 15.170 7.241   14.093  0.60 25.45 -1 25   GLU   A OE2  1 
ATOM   690  O  OE2  B GLU   A 1 25  ? 14.593 6.970   13.801  0.40 22.66 -1 25   GLU   A OE2  1 
ATOM   691  H  H    A GLU   A 1 25  ? 15.556 3.628   12.260  0.60 19.46 ?  25   GLU   A H    1 
ATOM   692  H  H    B GLU   A 1 25  ? 15.663 3.183   11.962  0.40 18.68 ?  25   GLU   A H    1 
ATOM   693  H  HA   A GLU   A 1 25  ? 16.031 4.194   14.788  0.60 21.34 ?  25   GLU   A HA   1 
ATOM   694  H  HA   B GLU   A 1 25  ? 15.927 3.827   14.503  0.40 20.35 ?  25   GLU   A HA   1 
ATOM   695  H  HB2  A GLU   A 1 25  ? 13.658 3.285   13.553  0.60 24.08 ?  25   GLU   A HB2  1 
ATOM   696  H  HB2  B GLU   A 1 25  ? 13.676 2.784   13.162  0.40 22.20 ?  25   GLU   A HB2  1 
ATOM   697  H  HB3  A GLU   A 1 25  ? 13.716 3.710   15.082  0.60 24.08 ?  25   GLU   A HB3  1 
ATOM   698  H  HB3  B GLU   A 1 25  ? 13.631 3.301   14.662  0.40 22.20 ?  25   GLU   A HB3  1 
ATOM   699  H  HG2  A GLU   A 1 25  ? 14.088 5.438   12.893  0.60 26.87 ?  25   GLU   A HG2  1 
ATOM   700  H  HG2  B GLU   A 1 25  ? 14.181 4.965   12.453  0.40 24.47 ?  25   GLU   A HG2  1 
ATOM   701  H  HG3  A GLU   A 1 25  ? 12.861 5.472   13.905  0.60 26.87 ?  25   GLU   A HG3  1 
ATOM   702  H  HG3  B GLU   A 1 25  ? 12.775 4.907   13.192  0.40 24.47 ?  25   GLU   A HG3  1 
ATOM   703  N  N    A GLU   A 1 26  ? 15.800 1.101   14.074  0.60 16.61 ?  26   GLU   A N    1 
ATOM   704  N  N    B GLU   A 1 26  ? 15.805 0.702   13.858  0.40 16.44 ?  26   GLU   A N    1 
ATOM   705  C  CA   A GLU   A 1 26  ? 16.107 -0.226  14.598  0.60 16.15 ?  26   GLU   A CA   1 
ATOM   706  C  CA   B GLU   A 1 26  ? 16.180 -0.589  14.428  0.40 16.51 ?  26   GLU   A CA   1 
ATOM   707  C  C    A GLU   A 1 26  ? 17.537 -0.289  15.119  0.60 15.20 ?  26   GLU   A C    1 
ATOM   708  C  C    B GLU   A 1 26  ? 17.610 -0.558  14.946  0.40 15.82 ?  26   GLU   A C    1 
ATOM   709  O  O    A GLU   A 1 26  ? 17.787 -0.769  16.229  0.60 15.12 ?  26   GLU   A O    1 
ATOM   710  O  O    B GLU   A 1 26  ? 17.914 -1.146  15.990  0.40 15.80 ?  26   GLU   A O    1 
ATOM   711  C  CB   A GLU   A 1 26  ? 15.902 -1.278  13.506  0.60 17.55 ?  26   GLU   A CB   1 
ATOM   712  C  CB   B GLU   A 1 26  ? 16.017 -1.695  13.384  0.40 17.77 ?  26   GLU   A CB   1 
ATOM   713  C  CG   A GLU   A 1 26  ? 14.502 -1.841  13.397  0.60 19.71 ?  26   GLU   A CG   1 
ATOM   714  C  CG   B GLU   A 1 26  ? 14.585 -2.118  13.155  0.40 18.59 ?  26   GLU   A CG   1 
ATOM   715  C  CD   A GLU   A 1 26  ? 14.118 -2.682  14.602  0.60 20.68 ?  26   GLU   A CD   1 
ATOM   716  C  CD   B GLU   A 1 26  ? 13.919 -2.599  14.420  0.40 19.03 ?  26   GLU   A CD   1 
ATOM   717  O  OE1  A GLU   A 1 26  ? 14.514 -3.871  14.704  0.60 20.85 ?  26   GLU   A OE1  1 
ATOM   718  O  OE1  B GLU   A 1 26  ? 14.514 -3.445  15.123  0.40 19.42 ?  26   GLU   A OE1  1 
ATOM   719  O  OE2  A GLU   A 1 26  ? 13.418 -2.133  15.463  0.60 21.07 -1 26   GLU   A OE2  1 
ATOM   720  O  OE2  B GLU   A 1 26  ? 12.813 -2.109  14.717  0.40 18.45 -1 26   GLU   A OE2  1 
ATOM   721  H  H    A GLU   A 1 26  ? 15.609 1.127   13.238  0.60 19.96 ?  26   GLU   A H    1 
ATOM   722  H  H    B GLU   A 1 26  ? 15.587 0.676   13.027  0.40 19.75 ?  26   GLU   A H    1 
ATOM   723  H  HA   A GLU   A 1 26  ? 15.507 -0.420  15.332  0.60 19.40 ?  26   GLU   A HA   1 
ATOM   724  H  HA   B GLU   A 1 26  ? 15.601 -0.788  15.178  0.40 19.83 ?  26   GLU   A HA   1 
ATOM   725  H  HB2  A GLU   A 1 26  ? 16.125 -0.877  12.651  0.60 21.09 ?  26   GLU   A HB2  1 
ATOM   726  H  HB2  B GLU   A 1 26  ? 16.368 -1.381  12.534  0.40 21.35 ?  26   GLU   A HB2  1 
ATOM   727  H  HB3  A GLU   A 1 26  ? 16.501 -2.017  13.685  0.60 21.09 ?  26   GLU   A HB3  1 
ATOM   728  H  HB3  B GLU   A 1 26  ? 16.514 -2.479  13.671  0.40 21.35 ?  26   GLU   A HB3  1 
ATOM   729  H  HG2  A GLU   A 1 26  ? 13.873 -1.101  13.311  0.60 23.68 ?  26   GLU   A HG2  1 
ATOM   730  H  HG2  B GLU   A 1 26  ? 14.078 -1.362  12.824  0.40 22.33 ?  26   GLU   A HG2  1 
ATOM   731  H  HG3  A GLU   A 1 26  ? 14.448 -2.407  12.615  0.60 23.68 ?  26   GLU   A HG3  1 
ATOM   732  H  HG3  B GLU   A 1 26  ? 14.562 -2.845  12.515  0.40 22.33 ?  26   GLU   A HG3  1 
ATOM   733  N  N    A ALA   A 1 27  ? 18.497 0.187   14.321  0.60 14.38 ?  27   ALA   A N    1 
ATOM   734  N  N    B ALA   A 1 27  ? 18.504 0.120   14.228  0.40 15.14 ?  27   ALA   A N    1 
ATOM   735  C  CA   A ALA   A 1 27  ? 19.897 0.116   14.730  0.60 14.52 ?  27   ALA   A CA   1 
ATOM   736  C  CA   B ALA   A 1 27  ? 19.884 0.225   14.691  0.40 15.14 ?  27   ALA   A CA   1 
ATOM   737  C  C    A ALA   A 1 27  ? 20.137 0.907   16.009  0.60 15.38 ?  27   ALA   A C    1 
ATOM   738  C  C    B ALA   A 1 27  ? 19.975 1.067   15.959  0.40 16.33 ?  27   ALA   A C    1 
ATOM   739  O  O    A ALA   A 1 27  ? 20.818 0.432   16.925  0.60 15.76 ?  27   ALA   A O    1 
ATOM   740  O  O    B ALA   A 1 27  ? 20.645 0.682   16.924  0.40 16.36 ?  27   ALA   A O    1 
ATOM   741  C  CB   A ALA   A 1 27  ? 20.803 0.619   13.602  0.60 14.10 ?  27   ALA   A CB   1 
ATOM   742  C  CB   B ALA   A 1 27  ? 20.769 0.794   13.580  0.40 14.52 ?  27   ALA   A CB   1 
ATOM   743  H  H    A ALA   A 1 27  ? 18.365 0.556   13.559  0.60 17.28 ?  27   ALA   A H    1 
ATOM   744  H  H    B ALA   A 1 27  ? 18.338 0.511   13.479  0.40 18.20 ?  27   ALA   A H    1 
ATOM   745  H  HA   A ALA   A 1 27  ? 20.125 -0.809  14.904  0.60 17.45 ?  27   ALA   A HA   1 
ATOM   746  H  HA   B ALA   A 1 27  ? 20.208 -0.662  14.900  0.40 18.20 ?  27   ALA   A HA   1 
ATOM   747  H  HB1  A ALA   A 1 27  ? 21.729 0.560   13.889  0.60 16.95 ?  27   ALA   A HB1  1 
ATOM   748  H  HB1  B ALA   A 1 27  ? 21.680 0.850   13.906  0.40 17.46 ?  27   ALA   A HB1  1 
ATOM   749  H  HB2  A ALA   A 1 27  ? 20.666 0.062   12.818  0.60 16.95 ?  27   ALA   A HB2  1 
ATOM   750  H  HB2  B ALA   A 1 27  ? 20.730 0.201   12.811  0.40 17.46 ?  27   ALA   A HB2  1 
ATOM   751  H  HB3  A ALA   A 1 27  ? 20.577 1.538   13.398  0.60 16.95 ?  27   ALA   A HB3  1 
ATOM   752  H  HB3  B ALA   A 1 27  ? 20.447 1.674   13.336  0.40 17.46 ?  27   ALA   A HB3  1 
ATOM   753  N  N    A LYS   A 1 28  ? 19.565 2.109   16.100  0.60 17.45 ?  28   LYS   A N    1 
ATOM   754  N  N    B LYS   A 1 28  ? 19.286 2.212   15.988  0.40 17.81 ?  28   LYS   A N    1 
ATOM   755  C  CA   A LYS   A 1 28  ? 19.719 2.910   17.309  0.60 20.06 ?  28   LYS   A CA   1 
ATOM   756  C  CA   B LYS   A 1 28  ? 19.338 3.077   17.163  0.40 19.82 ?  28   LYS   A CA   1 
ATOM   757  C  C    A LYS   A 1 28  ? 19.171 2.178   18.526  0.60 20.48 ?  28   LYS   A C    1 
ATOM   758  C  C    B LYS   A 1 28  ? 18.765 2.410   18.408  0.40 20.77 ?  28   LYS   A C    1 
ATOM   759  O  O    A LYS   A 1 28  ? 19.767 2.226   19.608  0.60 21.22 ?  28   LYS   A O    1 
ATOM   760  O  O    B LYS   A 1 28  ? 19.103 2.818   19.525  0.40 21.36 ?  28   LYS   A O    1 
ATOM   761  C  CB   A LYS   A 1 28  ? 19.033 4.267   17.133  0.60 22.06 ?  28   LYS   A CB   1 
ATOM   762  C  CB   B LYS   A 1 28  ? 18.613 4.396   16.890  0.40 20.95 ?  28   LYS   A CB   1 
ATOM   763  C  CG   A LYS   A 1 28  ? 19.833 5.250   16.287  0.60 23.92 ?  28   LYS   A CG   1 
ATOM   764  C  CG   B LYS   A 1 28  ? 19.328 5.288   15.885  0.40 22.26 ?  28   LYS   A CG   1 
ATOM   765  C  CD   A LYS   A 1 28  ? 19.295 6.672   16.381  0.60 25.85 ?  28   LYS   A CD   1 
ATOM   766  C  CD   B LYS   A 1 28  ? 18.820 6.719   15.941  0.40 23.88 ?  28   LYS   A CD   1 
ATOM   767  C  CE   A LYS   A 1 28  ? 18.040 6.856   15.548  0.60 27.08 ?  28   LYS   A CE   1 
ATOM   768  C  CE   B LYS   A 1 28  ? 17.357 6.809   15.554  0.40 25.08 ?  28   LYS   A CE   1 
ATOM   769  N  NZ   A LYS   A 1 28  ? 17.615 8.286   15.501  0.60 27.96 ?  28   LYS   A NZ   1 
ATOM   770  N  NZ   B LYS   A 1 28  ? 16.889 8.221   15.536  0.40 25.63 ?  28   LYS   A NZ   1 
ATOM   771  H  H    A LYS   A 1 28  ? 19.094 2.471   15.487  0.60 20.97 ?  28   LYS   A H    1 
ATOM   772  H  H    B LYS   A 1 28  ? 18.794 2.509   15.348  0.40 21.39 ?  28   LYS   A H    1 
ATOM   773  H  HA   A LYS   A 1 28  ? 20.661 3.071   17.468  0.60 24.10 ?  28   LYS   A HA   1 
ATOM   774  H  HA   B LYS   A 1 28  ? 20.263 3.290   17.347  0.40 23.81 ?  28   LYS   A HA   1 
ATOM   775  H  HB2  A LYS   A 1 28  ? 18.177 4.131   16.699  0.60 26.51 ?  28   LYS   A HB2  1 
ATOM   776  H  HB2  B LYS   A 1 28  ? 17.730 4.202   16.540  0.40 25.17 ?  28   LYS   A HB2  1 
ATOM   777  H  HB3  A LYS   A 1 28  ? 18.900 4.668   18.006  0.60 26.51 ?  28   LYS   A HB3  1 
ATOM   778  H  HB3  B LYS   A 1 28  ? 18.536 4.889   17.722  0.40 25.17 ?  28   LYS   A HB3  1 
ATOM   779  H  HG2  A LYS   A 1 28  ? 20.753 5.257   16.592  0.60 28.73 ?  28   LYS   A HG2  1 
ATOM   780  H  HG2  B LYS   A 1 28  ? 20.278 5.294   16.081  0.40 26.74 ?  28   LYS   A HG2  1 
ATOM   781  H  HG3  A LYS   A 1 28  ? 19.792 4.975   15.358  0.60 28.73 ?  28   LYS   A HG3  1 
ATOM   782  H  HG3  B LYS   A 1 28  ? 19.177 4.949   14.988  0.40 26.74 ?  28   LYS   A HG3  1 
ATOM   783  H  HD2  A LYS   A 1 28  ? 19.076 6.873   17.305  0.60 31.05 ?  28   LYS   A HD2  1 
ATOM   784  H  HD2  B LYS   A 1 28  ? 18.916 7.055   16.847  0.40 28.68 ?  28   LYS   A HD2  1 
ATOM   785  H  HD3  A LYS   A 1 28  ? 19.967 7.292   16.055  0.60 31.05 ?  28   LYS   A HD3  1 
ATOM   786  H  HD3  B LYS   A 1 28  ? 19.333 7.266   15.325  0.40 28.68 ?  28   LYS   A HD3  1 
ATOM   787  H  HE2  A LYS   A 1 28  ? 18.212 6.563   14.639  0.60 32.52 ?  28   LYS   A HE2  1 
ATOM   788  H  HE2  B LYS   A 1 28  ? 17.239 6.436   14.666  0.40 30.13 ?  28   LYS   A HE2  1 
ATOM   789  H  HE3  A LYS   A 1 28  ? 17.317 6.339   15.936  0.60 32.52 ?  28   LYS   A HE3  1 
ATOM   790  H  HE3  B LYS   A 1 28  ? 16.823 6.320   16.199  0.40 30.13 ?  28   LYS   A HE3  1 
ATOM   791  H  HZ1  A LYS   A 1 28  ? 16.879 8.370   15.008  0.60 33.58 ?  28   LYS   A HZ1  1 
ATOM   792  H  HZ1  B LYS   A 1 28  ? 16.031 8.253   15.306  0.40 30.78 ?  28   LYS   A HZ1  1 
ATOM   793  H  HZ2  A LYS   A 1 28  ? 17.446 8.581   16.324  0.60 33.58 ?  28   LYS   A HZ2  1 
ATOM   794  H  HZ2  B LYS   A 1 28  ? 16.988 8.584   16.343  0.40 30.78 ?  28   LYS   A HZ2  1 
ATOM   795  H  HZ3  A LYS   A 1 28  ? 18.261 8.784   15.143  0.60 33.58 ?  28   LYS   A HZ3  1 
ATOM   796  H  HZ3  B LYS   A 1 28  ? 17.364 8.691   14.948  0.40 30.78 ?  28   LYS   A HZ3  1 
ATOM   797  N  N    A LYS   A 1 29  ? 18.043 1.483   18.366  0.60 21.00 ?  29   LYS   A N    1 
ATOM   798  N  N    B LYS   A 1 29  ? 17.911 1.399   18.247  0.40 21.47 ?  29   LYS   A N    1 
ATOM   799  C  CA   A LYS   A 1 29  ? 17.447 0.764   19.488  0.60 22.71 ?  29   LYS   A CA   1 
ATOM   800  C  CA   B LYS   A 1 29  ? 17.308 0.706   19.380  0.40 22.53 ?  29   LYS   A CA   1 
ATOM   801  C  C    A LYS   A 1 29  ? 18.276 -0.460  19.859  0.60 22.20 ?  29   LYS   A C    1 
ATOM   802  C  C    B LYS   A 1 29  ? 18.124 -0.503  19.827  0.40 22.00 ?  29   LYS   A C    1 
ATOM   803  O  O    A LYS   A 1 29  ? 18.620 -0.658  21.031  0.60 23.05 ?  29   LYS   A O    1 
ATOM   804  O  O    B LYS   A 1 29  ? 18.309 -0.719  21.030  0.40 22.26 ?  29   LYS   A O    1 
ATOM   805  C  CB   A LYS   A 1 29  ? 16.014 0.358   19.137  0.60 25.08 ?  29   LYS   A CB   1 
ATOM   806  C  CB   B LYS   A 1 29  ? 15.886 0.259   19.017  0.40 24.02 ?  29   LYS   A CB   1 
ATOM   807  C  CG   A LYS   A 1 29  ? 15.255 -0.315  20.271  0.60 27.56 ?  29   LYS   A CG   1 
ATOM   808  C  CG   B LYS   A 1 29  ? 15.243 -0.678  20.032  0.40 25.50 ?  29   LYS   A CG   1 
ATOM   809  C  CD   A LYS   A 1 29  ? 14.852 0.685   21.344  0.60 29.92 ?  29   LYS   A CD   1 
ATOM   810  C  CD   B LYS   A 1 29  ? 15.021 0.017   21.363  0.40 26.91 ?  29   LYS   A CD   1 
ATOM   811  C  CE   A LYS   A 1 29  ? 13.987 0.031   22.410  0.60 31.44 ?  29   LYS   A CE   1 
ATOM   812  C  CE   B LYS   A 1 29  ? 14.865 -0.986  22.489  0.40 27.85 ?  29   LYS   A CE   1 
ATOM   813  N  NZ   A LYS   A 1 29  ? 13.517 1.012   23.426  0.60 32.35 ?  29   LYS   A NZ   1 
ATOM   814  N  NZ   B LYS   A 1 29  ? 14.565 -0.314  23.781  0.40 28.32 ?  29   LYS   A NZ   1 
ATOM   815  H  H    A LYS   A 1 29  ? 17.612 1.409   17.625  0.60 25.23 ?  29   LYS   A H    1 
ATOM   816  H  H    B LYS   A 1 29  ? 17.661 1.097   17.482  0.40 25.79 ?  29   LYS   A H    1 
ATOM   817  H  HA   A LYS   A 1 29  ? 17.411 1.349   20.259  0.60 27.28 ?  29   LYS   A HA   1 
ATOM   818  H  HA   B LYS   A 1 29  ? 17.246 1.319   20.127  0.40 27.07 ?  29   LYS   A HA   1 
ATOM   819  H  HB2  A LYS   A 1 29  ? 15.517 1.152   18.885  0.60 30.13 ?  29   LYS   A HB2  1 
ATOM   820  H  HB2  B LYS   A 1 29  ? 15.319 1.045   18.946  0.40 28.85 ?  29   LYS   A HB2  1 
ATOM   821  H  HB3  A LYS   A 1 29  ? 16.038 -0.263  18.393  0.60 30.13 ?  29   LYS   A HB3  1 
ATOM   822  H  HB3  B LYS   A 1 29  ? 15.910 -0.203  18.164  0.40 28.85 ?  29   LYS   A HB3  1 
ATOM   823  H  HG2  A LYS   A 1 29  ? 14.447 -0.720  19.917  0.60 33.10 ?  29   LYS   A HG2  1 
ATOM   824  H  HG2  B LYS   A 1 29  ? 14.378 -0.956  19.695  0.40 30.62 ?  29   LYS   A HG2  1 
ATOM   825  H  HG3  A LYS   A 1 29  ? 15.814 -0.994  20.682  0.60 33.10 ?  29   LYS   A HG3  1 
ATOM   826  H  HG3  B LYS   A 1 29  ? 15.802 -1.458  20.177  0.40 30.62 ?  29   LYS   A HG3  1 
ATOM   827  H  HD2  A LYS   A 1 29  ? 15.650 1.036   21.770  0.60 35.93 ?  29   LYS   A HD2  1 
ATOM   828  H  HD2  B LYS   A 1 29  ? 15.778 0.586   21.567  0.40 32.32 ?  29   LYS   A HD2  1 
ATOM   829  H  HD3  A LYS   A 1 29  ? 14.344 1.404   20.937  0.60 35.93 ?  29   LYS   A HD3  1 
ATOM   830  H  HD3  B LYS   A 1 29  ? 14.209 0.547   21.311  0.40 32.32 ?  29   LYS   A HD3  1 
ATOM   831  H  HE2  A LYS   A 1 29  ? 13.208 -0.367  21.989  0.60 37.75 ?  29   LYS   A HE2  1 
ATOM   832  H  HE2  B LYS   A 1 29  ? 14.135 -1.589  22.280  0.40 33.44 ?  29   LYS   A HE2  1 
ATOM   833  H  HE3  A LYS   A 1 29  ? 14.505 -0.652  22.866  0.60 37.75 ?  29   LYS   A HE3  1 
ATOM   834  H  HE3  B LYS   A 1 29  ? 15.693 -1.483  22.588  0.40 33.44 ?  29   LYS   A HE3  1 
ATOM   835  H  HZ1  A LYS   A 1 29  ? 13.014 0.602   24.035  0.60 38.84 ?  29   LYS   A HZ1  1 
ATOM   836  H  HZ1  B LYS   A 1 29  ? 14.478 -0.921  24.425  0.40 34.02 ?  29   LYS   A HZ1  1 
ATOM   837  H  HZ2  A LYS   A 1 29  ? 14.213 1.388   23.832  0.60 38.84 ?  29   LYS   A HZ2  1 
ATOM   838  H  HZ2  B LYS   A 1 29  ? 15.225 0.243   23.994  0.40 34.02 ?  29   LYS   A HZ2  1 
ATOM   839  H  HZ3  A LYS   A 1 29  ? 13.033 1.648   23.033  0.60 38.84 ?  29   LYS   A HZ3  1 
ATOM   840  H  HZ3  B LYS   A 1 29  ? 13.807 0.148   23.713  0.40 34.02 ?  29   LYS   A HZ3  1 
ATOM   841  N  N    . VAL   A 1 30  ? 18.599 -1.299  18.875  1.00 21.35 ?  30   VAL   A N    1 
ATOM   842  C  CA   . VAL   A 1 30  ? 19.264 -2.562  19.179  1.00 20.51 ?  30   VAL   A CA   1 
ATOM   843  C  C    . VAL   A 1 30  ? 20.770 -2.407  19.389  1.00 19.25 ?  30   VAL   A C    1 
ATOM   844  O  O    . VAL   A 1 30  ? 21.360 -3.137  20.193  1.00 19.59 ?  30   VAL   A O    1 
ATOM   845  C  CB   . VAL   A 1 30  ? 18.960 -3.557  18.046  1.00 21.49 ?  30   VAL   A CB   1 
ATOM   846  C  CG1  . VAL   A 1 30  ? 19.711 -4.864  18.251  1.00 22.04 ?  30   VAL   A CG1  1 
ATOM   847  C  CG2  . VAL   A 1 30  ? 17.460 -3.807  17.945  1.00 22.42 ?  30   VAL   A CG2  1 
ATOM   848  H  H    A VAL   A 1 30  ? 18.435 -1.171  18.039  0.60 25.65 ?  30   VAL   A H    1 
ATOM   849  H  H    B VAL   A 1 30  ? 18.541 -1.133  18.033  0.40 25.65 ?  30   VAL   A H    1 
ATOM   850  H  HA   . VAL   A 1 30  ? 18.880 -2.925  19.993  1.00 24.64 ?  30   VAL   A HA   1 
ATOM   851  H  HB   . VAL   A 1 30  ? 19.253 -3.176  17.204  1.00 25.81 ?  30   VAL   A HB   1 
ATOM   852  H  HG11 . VAL   A 1 30  ? 19.333 -5.539  17.665  1.00 26.47 ?  30   VAL   A HG11 1 
ATOM   853  H  HG12 . VAL   A 1 30  ? 20.646 -4.730  18.039  1.00 26.47 ?  30   VAL   A HG12 1 
ATOM   854  H  HG13 . VAL   A 1 30  ? 19.613 -5.140  19.176  1.00 26.47 ?  30   VAL   A HG13 1 
ATOM   855  H  HG21 . VAL   A 1 30  ? 17.298 -4.491  17.275  1.00 26.93 ?  30   VAL   A HG21 1 
ATOM   856  H  HG22 . VAL   A 1 30  ? 17.131 -4.105  18.807  1.00 26.93 ?  30   VAL   A HG22 1 
ATOM   857  H  HG23 . VAL   A 1 30  ? 17.018 -2.984  17.688  1.00 26.93 ?  30   VAL   A HG23 1 
ATOM   858  N  N    . LYS   A 1 31  ? 21.410 -1.478  18.687  1.00 18.54 ?  31   LYS   A N    1 
ATOM   859  C  CA   . LYS   A 1 31  ? 22.864 -1.381  18.637  1.00 18.99 ?  31   LYS   A CA   1 
ATOM   860  C  C    . LYS   A 1 31  ? 23.475 -2.738  18.274  1.00 17.32 ?  31   LYS   A C    1 
ATOM   861  O  O    . LYS   A 1 31  ? 24.270 -3.295  19.038  1.00 18.49 ?  31   LYS   A O    1 
ATOM   862  C  CB   . LYS   A 1 31  ? 23.450 -0.845  19.936  1.00 23.68 ?  31   LYS   A CB   1 
ATOM   863  C  CG   . LYS   A 1 31  ? 22.791 0.435   20.421  1.00 29.72 ?  31   LYS   A CG   1 
ATOM   864  C  CD   . LYS   A 1 31  ? 23.819 1.466   20.859  1.00 34.27 ?  31   LYS   A CD   1 
ATOM   865  C  CE   . LYS   A 1 31  ? 23.202 2.509   21.778  1.00 37.46 ?  31   LYS   A CE   1 
ATOM   866  N  NZ   . LYS   A 1 31  ? 21.992 3.149   21.193  1.00 39.09 ?  31   LYS   A NZ   1 
ATOM   867  H  H    . LYS   A 1 31  ? 21.011 -0.876  18.221  1.00 22.28 ?  31   LYS   A H    1 
ATOM   868  H  HA   . LYS   A 1 31  ? 23.094 -0.762  17.933  1.00 22.82 ?  31   LYS   A HA   1 
ATOM   869  H  HB2  . LYS   A 1 31  ? 23.350 -1.517  20.626  1.00 28.44 ?  31   LYS   A HB2  1 
ATOM   870  H  HB3  . LYS   A 1 31  ? 24.392 -0.660  19.791  1.00 28.44 ?  31   LYS   A HB3  1 
ATOM   871  H  HG2  . LYS   A 1 31  ? 22.265 0.818   19.700  1.00 35.69 ?  31   LYS   A HG2  1 
ATOM   872  H  HG3  . LYS   A 1 31  ? 22.221 0.233   21.179  1.00 35.69 ?  31   LYS   A HG3  1 
ATOM   873  H  HD2  . LYS   A 1 31  ? 24.535 1.021   21.339  1.00 41.15 ?  31   LYS   A HD2  1 
ATOM   874  H  HD3  . LYS   A 1 31  ? 24.170 1.920   20.076  1.00 41.15 ?  31   LYS   A HD3  1 
ATOM   875  H  HE2  . LYS   A 1 31  ? 22.943 2.080   22.606  1.00 44.97 ?  31   LYS   A HE2  1 
ATOM   876  H  HE3  . LYS   A 1 31  ? 23.855 3.204   21.955  1.00 44.97 ?  31   LYS   A HE3  1 
ATOM   877  H  HZ1  . LYS   A 1 31  ? 21.678 3.771   21.748  1.00 46.93 ?  31   LYS   A HZ1  1 
ATOM   878  H  HZ2  . LYS   A 1 31  ? 22.195 3.530   20.416  1.00 46.93 ?  31   LYS   A HZ2  1 
ATOM   879  H  HZ3  . LYS   A 1 31  ? 21.359 2.538   21.059  1.00 46.93 ?  31   LYS   A HZ3  1 
ATOM   880  N  N    . PRO   A 1 32  ? 23.121 -3.286  17.119  1.00 15.58 ?  32   PRO   A N    1 
ATOM   881  C  CA   . PRO   A 1 32  ? 23.596 -4.621  16.756  1.00 15.60 ?  32   PRO   A CA   1 
ATOM   882  C  C    . PRO   A 1 32  ? 25.097 -4.630  16.535  1.00 15.60 ?  32   PRO   A C    1 
ATOM   883  O  O    . PRO   A 1 32  ? 25.730 -3.597  16.302  1.00 15.41 ?  32   PRO   A O    1 
ATOM   884  C  CB   . PRO   A 1 32  ? 22.851 -4.907  15.448  1.00 15.96 ?  32   PRO   A CB   1 
ATOM   885  C  CG   . PRO   A 1 32  ? 22.659 -3.538  14.845  1.00 14.78 ?  32   PRO   A CG   1 
ATOM   886  C  CD   . PRO   A 1 32  ? 22.371 -2.653  16.022  1.00 14.75 ?  32   PRO   A CD   1 
ATOM   887  H  HA   . PRO   A 1 32  ? 23.355 -5.278  17.423  1.00 18.75 ?  32   PRO   A HA   1 
ATOM   888  H  HB2  . PRO   A 1 32  ? 23.388 -5.472  14.866  1.00 19.18 ?  32   PRO   A HB2  1 
ATOM   889  H  HB3  . PRO   A 1 32  ? 21.993 -5.329  15.635  1.00 19.18 ?  32   PRO   A HB3  1 
ATOM   890  H  HG2  . PRO   A 1 32  ? 23.468 -3.269  14.389  1.00 17.76 ?  32   PRO   A HG2  1 
ATOM   891  H  HG3  . PRO   A 1 32  ? 21.905 -3.558  14.229  1.00 17.76 ?  32   PRO   A HG3  1 
ATOM   892  H  HD2  . PRO   A 1 32  ? 22.706 -1.761  15.846  1.00 17.73 ?  32   PRO   A HD2  1 
ATOM   893  H  HD3  . PRO   A 1 32  ? 21.422 -2.650  16.211  1.00 17.73 ?  32   PRO   A HD3  1 
ATOM   894  N  N    . THR   A 1 33  ? 25.665 -5.834  16.593  1.00 15.46 ?  33   THR   A N    1 
ATOM   895  C  CA   . THR   A 1 33  ? 27.072 -5.993  16.255  1.00 15.75 ?  33   THR   A CA   1 
ATOM   896  C  C    . THR   A 1 33  ? 27.347 -5.535  14.830  1.00 14.05 ?  33   THR   A C    1 
ATOM   897  O  O    . THR   A 1 33  ? 28.375 -4.897  14.564  1.00 14.19 ?  33   THR   A O    1 
ATOM   898  C  CB   . THR   A 1 33  ? 27.485 -7.451  16.458  1.00 17.41 ?  33   THR   A CB   1 
ATOM   899  O  OG1  . THR   A 1 33  ? 27.191 -7.831  17.805  1.00 19.13 ?  33   THR   A OG1  1 
ATOM   900  C  CG2  . THR   A 1 33  ? 28.975 -7.642  16.192  1.00 18.50 ?  33   THR   A CG2  1 
ATOM   901  H  H    . THR   A 1 33  ? 25.264 -6.565  16.815  1.00 18.57 ?  33   THR   A H    1 
ATOM   902  H  HA   . THR   A 1 33  ? 27.605 -5.450  16.849  1.00 18.93 ?  33   THR   A HA   1 
ATOM   903  H  HB   . THR   A 1 33  ? 26.993 -8.024  15.846  1.00 20.92 ?  33   THR   A HB   1 
ATOM   904  H  HG1  . THR   A 1 33  ? 27.626 -7.352  18.342  1.00 22.99 ?  33   THR   A HG1  1 
ATOM   905  H  HG21 . THR   A 1 33  ? 29.252 -8.532  16.466  1.00 22.22 ?  33   THR   A HG21 1 
ATOM   906  H  HG22 . THR   A 1 33  ? 29.164 -7.534  15.247  1.00 22.22 ?  33   THR   A HG22 1 
ATOM   907  H  HG23 . THR   A 1 33  ? 29.487 -6.988  16.693  1.00 22.22 ?  33   THR   A HG23 1 
ATOM   908  N  N    . VAL   A 1 34  ? 26.442 -5.850  13.902  1.00 12.74 ?  34   VAL   A N    1 
ATOM   909  C  CA   . VAL   A 1 34  ? 26.613 -5.510  12.494  1.00 11.90 ?  34   VAL   A CA   1 
ATOM   910  C  C    . VAL   A 1 34  ? 25.303 -4.949  11.949  1.00 11.21 ?  34   VAL   A C    1 
ATOM   911  O  O    . VAL   A 1 34  ? 24.265 -5.622  12.003  1.00 11.90 ?  34   VAL   A O    1 
ATOM   912  C  CB   . VAL   A 1 34  ? 27.052 -6.717  11.643  1.00 12.53 ?  34   VAL   A CB   1 
ATOM   913  C  CG1  . VAL   A 1 34  ? 27.212 -6.303  10.187  1.00 12.70 ?  34   VAL   A CG1  1 
ATOM   914  C  CG2  . VAL   A 1 34  ? 28.343 -7.333  12.174  1.00 13.69 ?  34   VAL   A CG2  1 
ATOM   915  H  H    . VAL   A 1 34  ? 25.709 -6.275  14.063  1.00 15.31 ?  34   VAL   A H    1 
ATOM   916  H  HA   . VAL   A 1 34  ? 27.289 -4.819  12.408  1.00 14.31 ?  34   VAL   A HA   1 
ATOM   917  H  HB   . VAL   A 1 34  ? 26.359 -7.393  11.679  1.00 15.07 ?  34   VAL   A HB   1 
ATOM   918  H  HG11 . VAL   A 1 34  ? 27.703 -6.993  9.714   1.00 15.27 ?  34   VAL   A HG11 1 
ATOM   919  H  HG12 . VAL   A 1 34  ? 26.338 -6.187  9.784   1.00 15.27 ?  34   VAL   A HG12 1 
ATOM   920  H  HG13 . VAL   A 1 34  ? 27.707 -5.466  10.147  1.00 15.27 ?  34   VAL   A HG13 1 
ATOM   921  H  HG21 . VAL   A 1 34  ? 28.604 -8.069  11.597  1.00 16.45 ?  34   VAL   A HG21 1 
ATOM   922  H  HG22 . VAL   A 1 34  ? 29.039 -6.656  12.179  1.00 16.45 ?  34   VAL   A HG22 1 
ATOM   923  H  HG23 . VAL   A 1 34  ? 28.192 -7.657  13.075  1.00 16.45 ?  34   VAL   A HG23 1 
ATOM   924  N  N    . VAL   A 1 35  ? 25.355 -3.734  11.395  1.00 10.51 ?  35   VAL   A N    1 
ATOM   925  C  CA   . VAL   A 1 35  ? 24.306 -3.218  10.521  1.00 10.10 ?  35   VAL   A CA   1 
ATOM   926  C  C    . VAL   A 1 35  ? 24.848 -3.221  9.098   1.00 9.52  ?  35   VAL   A C    1 
ATOM   927  O  O    . VAL   A 1 35  ? 25.992 -2.818  8.856   1.00 10.14 ?  35   VAL   A O    1 
ATOM   928  C  CB   . VAL   A 1 35  ? 23.783 -1.822  10.937  1.00 10.66 ?  35   VAL   A CB   1 
ATOM   929  C  CG1  . VAL   A 1 35  ? 24.858 -0.729  10.801  1.00 11.43 ?  35   VAL   A CG1  1 
ATOM   930  C  CG2  . VAL   A 1 35  ? 22.534 -1.462  10.137  1.00 11.40 ?  35   VAL   A CG2  1 
ATOM   931  H  H    . VAL   A 1 35  ? 25.999 -3.178  11.508  1.00 12.64 ?  35   VAL   A H    1 
ATOM   932  H  HA   . VAL   A 1 35  ? 23.546 -3.827  10.550  1.00 12.15 ?  35   VAL   A HA   1 
ATOM   933  H  HB   . VAL   A 1 35  ? 23.520 -1.854  11.868  1.00 12.82 ?  35   VAL   A HB   1 
ATOM   934  H  HG11 . VAL   A 1 35  ? 24.517 0.105   11.169  1.00 13.74 ?  35   VAL   A HG11 1 
ATOM   935  H  HG12 . VAL   A 1 35  ? 25.651 -1.001  11.289  1.00 13.74 ?  35   VAL   A HG12 1 
ATOM   936  H  HG13 . VAL   A 1 35  ? 25.076 -0.605  9.862   1.00 13.74 ?  35   VAL   A HG13 1 
ATOM   937  H  HG21 . VAL   A 1 35  ? 22.188 -0.610  10.446  1.00 13.71 ?  35   VAL   A HG21 1 
ATOM   938  H  HG22 . VAL   A 1 35  ? 22.765 -1.399  9.194   1.00 13.71 ?  35   VAL   A HG22 1 
ATOM   939  H  HG23 . VAL   A 1 35  ? 21.864 -2.154  10.263  1.00 13.71 ?  35   VAL   A HG23 1 
ATOM   940  N  N    . VAL   A 1 36  ? 24.026 -3.669  8.159   1.00 9.26  ?  36   VAL   A N    1 
ATOM   941  C  CA   . VAL   A 1 36  ? 24.391 -3.682  6.749   1.00 8.72  ?  36   VAL   A CA   1 
ATOM   942  C  C    . VAL   A 1 36  ? 23.926 -2.389  6.095   1.00 9.03  ?  36   VAL   A C    1 
ATOM   943  O  O    . VAL   A 1 36  ? 22.765 -1.985  6.247   1.00 9.58  ?  36   VAL   A O    1 
ATOM   944  C  CB   . VAL   A 1 36  ? 23.774 -4.899  6.037   1.00 8.90  ?  36   VAL   A CB   1 
ATOM   945  C  CG1  . VAL   A 1 36  ? 24.022 -4.827  4.554   1.00 9.26  ?  36   VAL   A CG1  1 
ATOM   946  C  CG2  . VAL   A 1 36  ? 24.321 -6.191  6.613   1.00 10.06 ?  36   VAL   A CG2  1 
ATOM   947  H  H    . VAL   A 1 36  ? 23.232 -3.976  8.316   1.00 11.13 ?  36   VAL   A H    1 
ATOM   948  H  HA   . VAL   A 1 36  ? 25.361 -3.741  6.672   1.00 10.49 ?  36   VAL   A HA   1 
ATOM   949  H  HB   . VAL   A 1 36  ? 22.818 -4.889  6.178   1.00 10.71 ?  36   VAL   A HB   1 
ATOM   950  H  HG11 . VAL   A 1 36  ? 23.874 -5.705  4.170   1.00 11.14 ?  36   VAL   A HG11 1 
ATOM   951  H  HG12 . VAL   A 1 36  ? 23.409 -4.187  4.160   1.00 11.14 ?  36   VAL   A HG12 1 
ATOM   952  H  HG13 . VAL   A 1 36  ? 24.939 -4.550  4.400   1.00 11.14 ?  36   VAL   A HG13 1 
ATOM   953  H  HG21 . VAL   A 1 36  ? 23.925 -6.942  6.143   1.00 12.10 ?  36   VAL   A HG21 1 
ATOM   954  H  HG22 . VAL   A 1 36  ? 25.287 -6.207  6.504   1.00 12.10 ?  36   VAL   A HG22 1 
ATOM   955  H  HG23 . VAL   A 1 36  ? 24.098 -6.240  7.557   1.00 12.10 ?  36   VAL   A HG23 1 
ATOM   956  N  N    . ASN   A 1 37  ? 24.825 -1.761  5.341   1.00 8.55  ?  37   ASN   A N    1 
ATOM   957  C  CA   . ASN   A 1 37  ? 24.482 -0.640  4.483   1.00 8.30  ?  37   ASN   A CA   1 
ATOM   958  C  C    . ASN   A 1 37  ? 24.332 -1.102  3.043   1.00 8.49  ?  37   ASN   A C    1 
ATOM   959  O  O    . ASN   A 1 37  ? 25.110 -1.933  2.555   1.00 9.15  ?  37   ASN   A O    1 
ATOM   960  C  CB   . ASN   A 1 37  ? 25.557 0.441   4.561   1.00 8.72  ?  37   ASN   A CB   1 
ATOM   961  C  CG   . ASN   A 1 37  ? 25.225 1.650   3.713   1.00 8.87  ?  37   ASN   A CG   1 
ATOM   962  O  OD1  . ASN   A 1 37  ? 24.052 1.989   3.545   1.00 9.28  ?  37   ASN   A OD1  1 
ATOM   963  N  ND2  . ASN   A 1 37  ? 26.248 2.302   3.181   1.00 9.15  ?  37   ASN   A ND2  1 
ATOM   964  H  H    . ASN   A 1 37  ? 25.663 -1.968  5.320   1.00 10.28 ?  37   ASN   A H    1 
ATOM   965  H  HA   . ASN   A 1 37  ? 23.645 -0.256  4.778   1.00 9.99  ?  37   ASN   A HA   1 
ATOM   966  H  HB2  . ASN   A 1 37  ? 25.645 0.737   5.484   1.00 10.49 ?  37   ASN   A HB2  1 
ATOM   967  H  HB3  . ASN   A 1 37  ? 26.404 0.075   4.253   1.00 10.49 ?  37   ASN   A HB3  1 
ATOM   968  H  HD21 . ASN   A 1 37  ? 26.107 2.993   2.688   1.00 11.00 ?  37   ASN   A HD21 1 
ATOM   969  H  HD22 . ASN   A 1 37  ? 27.050 2.038   3.319   1.00 11.00 ?  37   ASN   A HD22 1 
ATOM   970  N  N    A ALA   A 1 38  ? 23.321 -0.535  2.376   0.60 8.94  ?  38   ALA   A N    1 
ATOM   971  N  N    B ALA   A 1 38  ? 23.299 -0.601  2.368   0.40 9.01  ?  38   ALA   A N    1 
ATOM   972  C  CA   A ALA   A 1 38  ? 23.102 -0.632  0.932   0.60 8.74  ?  38   ALA   A CA   1 
ATOM   973  C  CA   B ALA   A 1 38  ? 23.108 -0.870  0.943   0.40 9.52  ?  38   ALA   A CA   1 
ATOM   974  C  C    A ALA   A 1 38  ? 24.032 0.361   0.232   0.60 8.23  ?  38   ALA   A C    1 
ATOM   975  C  C    B ALA   A 1 38  ? 23.945 0.141   0.162   0.40 9.44  ?  38   ALA   A C    1 
ATOM   976  O  O    A ALA   A 1 38  ? 23.646 1.464   -0.161  0.60 8.25  ?  38   ALA   A O    1 
ATOM   977  O  O    B ALA   A 1 38  ? 23.468 1.175   -0.315  0.40 9.40  ?  38   ALA   A O    1 
ATOM   978  C  CB   A ALA   A 1 38  ? 21.639 -0.337  0.615   0.60 9.24  ?  38   ALA   A CB   1 
ATOM   979  C  CB   B ALA   A 1 38  ? 21.633 -0.800  0.577   0.40 10.36 ?  38   ALA   A CB   1 
ATOM   980  H  H    A ALA   A 1 38  ? 22.726 -0.054  2.766   0.60 10.75 ?  38   ALA   A H    1 
ATOM   981  H  H    B ALA   A 1 38  ? 22.694 -0.098  2.716   0.40 10.84 ?  38   ALA   A H    1 
ATOM   982  H  HA   A ALA   A 1 38  ? 23.312 -1.524  0.625   0.60 10.52 ?  38   ALA   A HA   1 
ATOM   983  H  HA   B ALA   A 1 38  ? 23.437 -1.762  0.737   0.40 11.45 ?  38   ALA   A HA   1 
ATOM   984  H  HB1  A ALA   A 1 38  ? 21.496 -0.407  -0.340  0.60 11.11 ?  38   ALA   A HB1  1 
ATOM   985  H  HB1  B ALA   A 1 38  ? 21.536 -0.982  -0.370  0.40 12.46 ?  38   ALA   A HB1  1 
ATOM   986  H  HB2  A ALA   A 1 38  ? 21.077 -0.979  1.081   0.60 11.11 ?  38   ALA   A HB2  1 
ATOM   987  H  HB2  B ALA   A 1 38  ? 21.149 -1.461  1.095   0.40 12.46 ?  38   ALA   A HB2  1 
ATOM   988  H  HB3  A ALA   A 1 38  ? 21.421 0.563   0.916   0.60 11.11 ?  38   ALA   A HB3  1 
ATOM   989  H  HB3  B ALA   A 1 38  ? 21.303 0.088   0.781   0.40 12.46 ?  38   ALA   A HB3  1 
ATOM   990  N  N    A ALA   A 1 39  ? 25.288 -0.049  0.080   0.60 8.31  ?  39   ALA   A N    1 
ATOM   991  N  N    B ALA   A 1 39  ? 25.229 -0.172  0.036   0.40 10.09 ?  39   ALA   A N    1 
ATOM   992  C  CA   A ALA   A 1 39  ? 26.364 0.809   -0.393  0.60 8.58  ?  39   ALA   A CA   1 
ATOM   993  C  CA   B ALA   A 1 39  ? 26.202 0.781   -0.469  0.40 9.94  ?  39   ALA   A CA   1 
ATOM   994  C  C    A ALA   A 1 39  ? 26.497 0.766   -1.911  0.60 8.53  ?  39   ALA   A C    1 
ATOM   995  C  C    B ALA   A 1 39  ? 26.316 0.705   -1.989  0.40 9.40  ?  39   ALA   A C    1 
ATOM   996  O  O    A ALA   A 1 39  ? 26.020 -0.156  -2.576  0.60 9.08  ?  39   ALA   A O    1 
ATOM   997  O  O    B ALA   A 1 39  ? 25.821 -0.221  -2.636  0.40 9.71  ?  39   ALA   A O    1 
ATOM   998  C  CB   A ALA   A 1 39  ? 27.684 0.360   0.237   0.60 9.16  ?  39   ALA   A CB   1 
ATOM   999  C  CB   B ALA   A 1 39  ? 27.563 0.531   0.183   0.40 10.48 ?  39   ALA   A CB   1 
ATOM   1000 H  H    A ALA   A 1 39  ? 25.546 -0.851  0.250   0.60 9.99  ?  39   ALA   A H    1 
ATOM   1001 H  H    B ALA   A 1 39  ? 25.563 -0.945  0.232   0.40 12.14 ?  39   ALA   A H    1 
ATOM   1002 H  HA   A ALA   A 1 39  ? 26.187 1.725   -0.129  0.60 10.32 ?  39   ALA   A HA   1 
ATOM   1003 H  HA   B ALA   A 1 39  ? 25.914 1.675   -0.234  0.40 11.95 ?  39   ALA   A HA   1 
ATOM   1004 H  HB1  A ALA   A 1 39  ? 28.393 0.937   -0.082  0.60 11.02 ?  39   ALA   A HB1  1 
ATOM   1005 H  HB1  B ALA   A 1 39  ? 28.199 1.176   -0.160  0.40 12.60 ?  39   ALA   A HB1  1 
ATOM   1006 H  HB2  A ALA   A 1 39  ? 27.606 0.432   1.202   0.60 11.02 ?  39   ALA   A HB2  1 
ATOM   1007 H  HB2  B ALA   A 1 39  ? 27.474 0.636   1.146   0.40 12.60 ?  39   ALA   A HB2  1 
ATOM   1008 H  HB3  A ALA   A 1 39  ? 27.856 -0.556  -0.017  0.60 11.02 ?  39   ALA   A HB3  1 
ATOM   1009 H  HB3  B ALA   A 1 39  ? 27.855 -0.369  -0.024  0.40 12.60 ?  39   ALA   A HB3  1 
ATOM   1010 N  N    A ASN   A 1 40  ? 27.181 1.777   -2.455  0.60 8.72  ?  40   ASN   A N    1 
ATOM   1011 N  N    B ASN   A 1 40  ? 26.965 1.718   -2.560  0.40 9.32  ?  40   ASN   A N    1 
ATOM   1012 C  CA   A ASN   A 1 40  ? 27.721 1.724   -3.809  0.60 8.89  ?  40   ASN   A CA   1 
ATOM   1013 C  CA   B ASN   A 1 40  ? 27.427 1.688   -3.939  0.40 9.28  ?  40   ASN   A CA   1 
ATOM   1014 C  C    A ASN   A 1 40  ? 29.246 1.614   -3.755  0.60 8.33  ?  40   ASN   A C    1 
ATOM   1015 C  C    B ASN   A 1 40  ? 28.952 1.600   -3.961  0.40 8.91  ?  40   ASN   A C    1 
ATOM   1016 O  O    A ASN   A 1 40  ? 29.859 1.716   -2.689  0.60 8.53  ?  40   ASN   A O    1 
ATOM   1017 O  O    B ASN   A 1 40  ? 29.614 1.703   -2.927  0.40 9.01  ?  40   ASN   A O    1 
ATOM   1018 C  CB   A ASN   A 1 40  ? 27.237 2.899   -4.679  0.60 9.85  ?  40   ASN   A CB   1 
ATOM   1019 C  CB   B ASN   A 1 40  ? 26.917 2.907   -4.718  0.40 10.11 ?  40   ASN   A CB   1 
ATOM   1020 C  CG   A ASN   A 1 40  ? 27.618 4.258   -4.127  0.60 10.51 ?  40   ASN   A CG   1 
ATOM   1021 C  CG   B ASN   A 1 40  ? 27.276 4.223   -4.054  0.40 10.68 ?  40   ASN   A CG   1 
ATOM   1022 O  OD1  A ASN   A 1 40  ? 28.788 4.516   -3.811  0.60 11.44 ?  40   ASN   A OD1  1 
ATOM   1023 O  OD1  B ASN   A 1 40  ? 28.451 4.526   -3.846  0.40 12.85 ?  40   ASN   A OD1  1 
ATOM   1024 N  ND2  A ASN   A 1 40  ? 26.625 5.153   -4.034  0.60 11.11 ?  40   ASN   A ND2  1 
ATOM   1025 N  ND2  B ASN   A 1 40  ? 26.262 5.023   -3.739  0.40 10.54 ?  40   ASN   A ND2  1 
ATOM   1026 H  H    A ASN   A 1 40  ? 27.357 2.513   -2.049  0.60 10.49 ?  40   ASN   A H    1 
ATOM   1027 H  H    B ASN   A 1 40  ? 27.149 2.454   -2.155  0.40 11.21 ?  40   ASN   A H    1 
ATOM   1028 H  HA   A ASN   A 1 40  ? 27.406 0.914   -4.232  0.60 10.69 ?  40   ASN   A HA   1 
ATOM   1029 H  HA   B ASN   A 1 40  ? 27.072 0.890   -4.370  0.40 11.16 ?  40   ASN   A HA   1 
ATOM   1030 H  HB2  A ASN   A 1 40  ? 27.625 2.814   -5.568  0.60 11.85 ?  40   ASN   A HB2  1 
ATOM   1031 H  HB2  B ASN   A 1 40  ? 27.307 2.895   -5.606  0.40 12.16 ?  40   ASN   A HB2  1 
ATOM   1032 H  HB3  A ASN   A 1 40  ? 26.271 2.860   -4.742  0.60 11.85 ?  40   ASN   A HB3  1 
ATOM   1033 H  HB3  B ASN   A 1 40  ? 25.948 2.854   -4.783  0.40 12.16 ?  40   ASN   A HB3  1 
ATOM   1034 H  HD21 A ASN   A 1 40  ? 26.780 5.946   -3.737  0.60 13.35 ?  40   ASN   A HD21 1 
ATOM   1035 H  HD21 B ASN   A 1 40  ? 26.416 5.780   -3.364  0.40 12.68 ?  40   ASN   A HD21 1 
ATOM   1036 H  HD22 A ASN   A 1 40  ? 25.825 4.935   -4.269  0.60 13.35 ?  40   ASN   A HD22 1 
ATOM   1037 H  HD22 B ASN   A 1 40  ? 25.453 4.777   -3.898  0.40 12.68 ?  40   ASN   A HD22 1 
ATOM   1038 N  N    A VAL   A 1 41  ? 29.860 1.363   -4.918  0.60 8.50  ?  41   VAL   A N    1 
ATOM   1039 N  N    B VAL   A 1 41  ? 29.511 1.397   -5.158  0.40 9.30  ?  41   VAL   A N    1 
ATOM   1040 C  CA   A VAL   A 1 41  ? 31.291 1.059   -4.951  0.60 8.96  ?  41   VAL   A CA   1 
ATOM   1041 C  CA   B VAL   A 1 41  ? 30.937 1.082   -5.269  0.40 10.05 ?  41   VAL   A CA   1 
ATOM   1042 C  C    A VAL   A 1 41  ? 32.146 2.221   -4.481  0.60 8.96  ?  41   VAL   A C    1 
ATOM   1043 C  C    B VAL   A 1 41  ? 31.821 2.212   -4.757  0.40 9.84  ?  41   VAL   A C    1 
ATOM   1044 O  O    A VAL   A 1 41  ? 33.288 2.008   -4.056  0.60 9.61  ?  41   VAL   A O    1 
ATOM   1045 O  O    B VAL   A 1 41  ? 32.965 1.972   -4.351  0.40 9.83  ?  41   VAL   A O    1 
ATOM   1046 C  CB   A VAL   A 1 41  ? 31.767 0.563   -6.339  0.60 9.16  ?  41   VAL   A CB   1 
ATOM   1047 C  CB   B VAL   A 1 41  ? 31.314 0.673   -6.708  0.40 10.96 ?  41   VAL   A CB   1 
ATOM   1048 C  CG1  A VAL   A 1 41  ? 31.062 -0.735  -6.723  0.60 9.52  ?  41   VAL   A CG1  1 
ATOM   1049 C  CG1  B VAL   A 1 41  ? 30.630 -0.631  -7.084  0.40 11.60 ?  41   VAL   A CG1  1 
ATOM   1050 C  CG2  A VAL   A 1 41  ? 31.608 1.633   -7.423  0.60 9.27  ?  41   VAL   A CG2  1 
ATOM   1051 C  CG2  B VAL   A 1 41  ? 30.967 1.775   -7.698  0.40 11.50 ?  41   VAL   A CG2  1 
ATOM   1052 H  H    A VAL   A 1 41  ? 29.481 1.357   -5.689  0.60 10.23 ?  41   VAL   A H    1 
ATOM   1053 H  H    B VAL   A 1 41  ? 29.088 1.424   -5.907  0.40 11.19 ?  41   VAL   A H    1 
ATOM   1054 H  HA   A VAL   A 1 41  ? 31.455 0.333   -4.332  0.60 10.78 ?  41   VAL   A HA   1 
ATOM   1055 H  HA   B VAL   A 1 41  ? 31.114 0.312   -4.707  0.40 12.08 ?  41   VAL   A HA   1 
ATOM   1056 H  HB   A VAL   A 1 41  ? 32.713 0.357   -6.280  0.60 11.02 ?  41   VAL   A HB   1 
ATOM   1057 H  HB   B VAL   A 1 41  ? 32.272 0.524   -6.750  0.40 13.17 ?  41   VAL   A HB   1 
ATOM   1058 H  HG11 A VAL   A 1 41  ? 31.390 -1.038  -7.584  0.60 11.46 ?  41   VAL   A HG11 1 
ATOM   1059 H  HG11 B VAL   A 1 41  ? 30.794 -0.815  -8.020  0.40 13.94 ?  41   VAL   A HG11 1 
ATOM   1060 H  HG12 A VAL   A 1 41  ? 31.240 -1.408  -6.046  0.60 11.46 ?  41   VAL   A HG12 1 
ATOM   1061 H  HG12 B VAL   A 1 41  ? 30.995 -1.347  -6.538  0.40 13.94 ?  41   VAL   A HG12 1 
ATOM   1062 H  HG13 A VAL   A 1 41  ? 30.104 -0.572  -6.776  0.60 11.46 ?  41   VAL   A HG13 1 
ATOM   1063 H  HG13 B VAL   A 1 41  ? 29.679 -0.550  -6.923  0.40 13.94 ?  41   VAL   A HG13 1 
ATOM   1064 H  HG21 A VAL   A 1 41  ? 31.838 1.244   -8.284  0.60 11.15 ?  41   VAL   A HG21 1 
ATOM   1065 H  HG21 B VAL   A 1 41  ? 31.239 1.497   -8.586  0.40 13.82 ?  41   VAL   A HG21 1 
ATOM   1066 H  HG22 A VAL   A 1 41  ? 30.693 1.940   -7.430  0.60 11.15 ?  41   VAL   A HG22 1 
ATOM   1067 H  HG22 B VAL   A 1 41  ? 30.008 1.928   -7.681  0.40 13.82 ?  41   VAL   A HG22 1 
ATOM   1068 H  HG23 A VAL   A 1 41  ? 32.208 2.369   -7.225  0.60 11.15 ?  41   VAL   A HG23 1 
ATOM   1069 H  HG23 B VAL   A 1 41  ? 31.436 2.583   -7.446  0.40 13.82 ?  41   VAL   A HG23 1 
ATOM   1070 N  N    A TYR   A 1 42  ? 31.633 3.450   -4.564  0.60 9.33  ?  42   TYR   A N    1 
ATOM   1071 N  N    B TYR   A 1 42  ? 31.333 3.454   -4.784  0.40 9.94  ?  42   TYR   A N    1 
ATOM   1072 C  CA   A TYR   A 1 42  ? 32.356 4.648   -4.154  0.60 9.60  ?  42   TYR   A CA   1 
ATOM   1073 C  CA   B TYR   A 1 42  ? 32.124 4.601   -4.346  0.40 10.27 ?  42   TYR   A CA   1 
ATOM   1074 C  C    A TYR   A 1 42  ? 32.095 5.016   -2.703  0.60 9.45  ?  42   TYR   A C    1 
ATOM   1075 C  C    B TYR   A 1 42  ? 31.863 4.991   -2.900  0.40 10.11 ?  42   TYR   A C    1 
ATOM   1076 O  O    A TYR   A 1 42  ? 32.663 6.001   -2.211  0.60 9.94  ?  42   TYR   A O    1 
ATOM   1077 O  O    B TYR   A 1 42  ? 32.426 5.986   -2.429  0.40 10.54 ?  42   TYR   A O    1 
ATOM   1078 C  CB   A TYR   A 1 42  ? 31.977 5.834   -5.064  0.60 10.44 ?  42   TYR   A CB   1 
ATOM   1079 C  CB   B TYR   A 1 42  ? 31.887 5.809   -5.263  0.40 10.99 ?  42   TYR   A CB   1 
ATOM   1080 C  CG   A TYR   A 1 42  ? 32.084 5.531   -6.549  0.60 11.39 ?  42   TYR   A CG   1 
ATOM   1081 C  CG   B TYR   A 1 42  ? 32.184 5.487   -6.700  0.40 11.80 ?  42   TYR   A CG   1 
ATOM   1082 C  CD1  A TYR   A 1 42  ? 33.316 5.333   -7.149  0.60 12.03 ?  42   TYR   A CD1  1 
ATOM   1083 C  CD1  B TYR   A 1 42  ? 33.485 5.279   -7.132  0.40 12.52 ?  42   TYR   A CD1  1 
ATOM   1084 C  CD2  A TYR   A 1 42  ? 30.952 5.438   -7.350  0.60 12.70 ?  42   TYR   A CD2  1 
ATOM   1085 C  CD2  B TYR   A 1 42  ? 31.159 5.357   -7.619  0.40 12.06 ?  42   TYR   A CD2  1 
ATOM   1086 C  CE1  A TYR   A 1 42  ? 33.427 5.045   -8.500  0.60 12.22 ?  42   TYR   A CE1  1 
ATOM   1087 C  CE1  B TYR   A 1 42  ? 33.755 4.960   -8.449  0.40 12.35 ?  42   TYR   A CE1  1 
ATOM   1088 C  CE2  A TYR   A 1 42  ? 31.052 5.160   -8.709  0.60 13.18 ?  42   TYR   A CE2  1 
ATOM   1089 C  CE2  B TYR   A 1 42  ? 31.416 5.043   -8.934  0.40 12.43 ?  42   TYR   A CE2  1 
ATOM   1090 C  CZ   A TYR   A 1 42  ? 32.298 4.964   -9.277  0.60 12.82 ?  42   TYR   A CZ   1 
ATOM   1091 C  CZ   B TYR   A 1 42  ? 32.713 4.847   -9.347  0.40 12.13 ?  42   TYR   A CZ   1 
ATOM   1092 O  OH   A TYR   A 1 42  ? 32.416 4.684   -10.621 0.60 13.94 ?  42   TYR   A OH   1 
ATOM   1093 O  OH   B TYR   A 1 42  ? 32.960 4.526   -10.660 0.40 12.94 ?  42   TYR   A OH   1 
ATOM   1094 H  H    A TYR   A 1 42  ? 30.851 3.616   -4.870  0.60 11.22 ?  42   TYR   A H    1 
ATOM   1095 H  H    B TYR   A 1 42  ? 30.542 3.658   -5.065  0.40 11.96 ?  42   TYR   A H    1 
ATOM   1096 H  HA   A TYR   A 1 42  ? 33.310 4.496   -4.255  0.60 11.55 ?  42   TYR   A HA   1 
ATOM   1097 H  HA   B TYR   A 1 42  ? 33.060 4.367   -4.426  0.40 12.35 ?  42   TYR   A HA   1 
ATOM   1098 H  HB2  A TYR   A 1 42  ? 31.060 6.091   -4.881  0.60 12.55 ?  42   TYR   A HB2  1 
ATOM   1099 H  HB2  B TYR   A 1 42  ? 30.959 6.083   -5.200  0.40 13.21 ?  42   TYR   A HB2  1 
ATOM   1100 H  HB3  A TYR   A 1 42  ? 32.570 6.581   -4.874  0.60 12.55 ?  42   TYR   A HB3  1 
ATOM   1101 H  HB3  B TYR   A 1 42  ? 32.470 6.535   -4.988  0.40 13.21 ?  42   TYR   A HB3  1 
ATOM   1102 H  HD1  A TYR   A 1 42  ? 34.087 5.382   -6.636  0.60 14.46 ?  42   TYR   A HD1  1 
ATOM   1103 H  HD1  B TYR   A 1 42  ? 34.189 5.353   -6.524  0.40 15.05 ?  42   TYR   A HD1  1 
ATOM   1104 H  HD2  A TYR   A 1 42  ? 30.113 5.574   -6.975  0.60 15.27 ?  42   TYR   A HD2  1 
ATOM   1105 H  HD2  B TYR   A 1 42  ? 30.282 5.493   -7.341  0.40 14.50 ?  42   TYR   A HD2  1 
ATOM   1106 H  HE1  A TYR   A 1 42  ? 34.263 4.911   -8.889  0.60 14.70 ?  42   TYR   A HE1  1 
ATOM   1107 H  HE1  B TYR   A 1 42  ? 34.634 4.828   -8.726  0.40 14.85 ?  42   TYR   A HE1  1 
ATOM   1108 H  HE2  A TYR   A 1 42  ? 30.284 5.103   -9.238  0.60 15.84 ?  42   TYR   A HE2  1 
ATOM   1109 H  HE2  B TYR   A 1 42  ? 30.716 4.970   -9.539  0.40 14.95 ?  42   TYR   A HE2  1 
ATOM   1110 H  HH   A TYR   A 1 42  ? 33.222 4.579   -10.832 0.60 16.76 ?  42   TYR   A HH   1 
ATOM   1111 H  HH   B TYR   A 1 42  ? 33.731 4.197   -10.726 0.40 15.56 ?  42   TYR   A HH   1 
ATOM   1112 N  N    A LEU   A 1 43  ? 31.248 4.250   -2.015  0.60 9.07  ?  43   LEU   A N    1 
ATOM   1113 N  N    B LEU   A 1 43  ? 31.029 4.232   -2.192  0.40 9.90  ?  43   LEU   A N    1 
ATOM   1114 C  CA   A LEU   A 1 43  ? 30.789 4.587   -0.669  0.60 9.15  ?  43   LEU   A CA   1 
ATOM   1115 C  CA   B LEU   A 1 43  ? 30.639 4.552   -0.821  0.40 9.78  ?  43   LEU   A CA   1 
ATOM   1116 C  C    A LEU   A 1 43  ? 30.311 6.037   -0.585  0.60 9.27  ?  43   LEU   A C    1 
ATOM   1117 C  C    B LEU   A 1 43  ? 30.153 5.994   -0.691  0.40 9.86  ?  43   LEU   A C    1 
ATOM   1118 O  O    A LEU   A 1 43  ? 30.602 6.757   0.373   0.60 10.35 ?  43   LEU   A O    1 
ATOM   1119 O  O    B LEU   A 1 43  ? 30.388 6.664   0.316   0.40 10.02 ?  43   LEU   A O    1 
ATOM   1120 C  CB   A LEU   A 1 43  ? 31.840 4.282   0.398   0.60 9.46  ?  43   LEU   A CB   1 
ATOM   1121 C  CB   B LEU   A 1 43  ? 31.746 4.238   0.186   0.40 9.65  ?  43   LEU   A CB   1 
ATOM   1122 C  CG   A LEU   A 1 43  ? 32.369 2.845   0.465   0.60 9.92  ?  43   LEU   A CG   1 
ATOM   1123 C  CG   B LEU   A 1 43  ? 32.167 2.771   0.303   0.40 9.42  ?  43   LEU   A CG   1 
ATOM   1124 C  CD1  A LEU   A 1 43  ? 33.428 2.756   1.552   0.60 10.74 ?  43   LEU   A CD1  1 
ATOM   1125 C  CD1  B LEU   A 1 43  ? 33.221 2.629   1.387   0.40 9.71  ?  43   LEU   A CD1  1 
ATOM   1126 C  CD2  A LEU   A 1 43  ? 31.261 1.831   0.706   0.60 9.99  ?  43   LEU   A CD2  1 
ATOM   1127 C  CD2  B LEU   A 1 43  ? 30.972 1.866   0.583   0.40 9.70  ?  43   LEU   A CD2  1 
ATOM   1128 H  H    A LEU   A 1 43  ? 30.910 3.511   -2.312  0.60 10.92 ?  43   LEU   A H    1 
ATOM   1129 H  H    B LEU   A 1 43  ? 30.669 3.510   -2.491  0.40 11.91 ?  43   LEU   A H    1 
ATOM   1130 H  HA   A LEU   A 1 43  ? 30.025 4.022   -0.468  0.60 11.01 ?  43   LEU   A HA   1 
ATOM   1131 H  HA   B LEU   A 1 43  ? 29.885 3.992   -0.594  0.40 11.76 ?  43   LEU   A HA   1 
ATOM   1132 H  HB2  A LEU   A 1 43  ? 32.602 4.865   0.250   0.60 11.37 ?  43   LEU   A HB2  1 
ATOM   1133 H  HB2  B LEU   A 1 43  ? 32.535 4.746   -0.056  0.40 11.61 ?  43   LEU   A HB2  1 
ATOM   1134 H  HB3  A LEU   A 1 43  ? 31.450 4.481   1.266   0.60 11.37 ?  43   LEU   A HB3  1 
ATOM   1135 H  HB3  B LEU   A 1 43  ? 31.442 4.517   1.065   0.40 11.61 ?  43   LEU   A HB3  1 
ATOM   1136 H  HG   A LEU   A 1 43  ? 32.793 2.629   -0.379  0.60 11.93 ?  43   LEU   A HG   1 
ATOM   1137 H  HG   B LEU   A 1 43  ? 32.566 2.490   -0.536  0.40 11.33 ?  43   LEU   A HG   1 
ATOM   1138 H  HD11 A LEU   A 1 43  ? 33.762 1.846   1.593   0.60 12.91 ?  43   LEU   A HD11 1 
ATOM   1139 H  HD11 B LEU   A 1 43  ? 33.485 1.698   1.453   0.40 11.68 ?  43   LEU   A HD11 1 
ATOM   1140 H  HD12 A LEU   A 1 43  ? 34.152 3.366   1.340   0.60 12.91 ?  43   LEU   A HD12 1 
ATOM   1141 H  HD12 B LEU   A 1 43  ? 33.990 3.175   1.157   0.40 11.68 ?  43   LEU   A HD12 1 
ATOM   1142 H  HD13 A LEU   A 1 43  ? 33.029 3.000   2.403   0.60 12.91 ?  43   LEU   A HD13 1 
ATOM   1143 H  HD13 B LEU   A 1 43  ? 32.847 2.926   2.233   0.40 11.68 ?  43   LEU   A HD13 1 
ATOM   1144 H  HD21 A LEU   A 1 43  ? 31.657 0.955   0.810   0.60 12.01 ?  43   LEU   A HD21 1 
ATOM   1145 H  HD21 B LEU   A 1 43  ? 31.294 0.984   0.821   0.40 11.67 ?  43   LEU   A HD21 1 
ATOM   1146 H  HD22 A LEU   A 1 43  ? 30.782 2.080   1.512   0.60 12.01 ?  43   LEU   A HD22 1 
ATOM   1147 H  HD22 B LEU   A 1 43  ? 30.460 2.242   1.316   0.40 11.67 ?  43   LEU   A HD22 1 
ATOM   1148 H  HD23 A LEU   A 1 43  ? 30.660 1.840   -0.054  0.60 12.01 ?  43   LEU   A HD23 1 
ATOM   1149 H  HD23 B LEU   A 1 43  ? 30.423 1.817   -0.214  0.40 11.67 ?  43   LEU   A HD23 1 
ATOM   1150 N  N    A LYS   A 1 44  ? 29.559 6.467   -1.601  0.60 9.35  ?  44   LYS   A N    1 
ATOM   1151 N  N    B LYS   A 1 44  ? 29.436 6.463   -1.711  0.40 9.99  ?  44   LYS   A N    1 
ATOM   1152 C  CA   A LYS   A 1 44  ? 28.894 7.768   -1.598  0.60 9.75  ?  44   LYS   A CA   1 
ATOM   1153 C  CA   B LYS   A 1 44  ? 28.806 7.783   -1.680  0.40 10.34 ?  44   LYS   A CA   1 
ATOM   1154 C  C    A LYS   A 1 44  ? 27.465 7.551   -1.104  0.60 9.22  ?  44   LYS   A C    1 
ATOM   1155 C  C    B LYS   A 1 44  ? 27.397 7.606   -1.137  0.40 9.53  ?  44   LYS   A C    1 
ATOM   1156 O  O    A LYS   A 1 44  ? 26.617 7.010   -1.825  0.60 10.41 ?  44   LYS   A O    1 
ATOM   1157 O  O    B LYS   A 1 44  ? 26.488 7.169   -1.848  0.40 10.23 ?  44   LYS   A O    1 
ATOM   1158 C  CB   A LYS   A 1 44  ? 28.931 8.404   -2.984  0.60 12.11 ?  44   LYS   A CB   1 
ATOM   1159 C  CB   B LYS   A 1 44  ? 28.813 8.421   -3.064  0.40 12.99 ?  44   LYS   A CB   1 
ATOM   1160 C  CG   A LYS   A 1 44  ? 30.318 8.859   -3.423  0.60 14.95 ?  44   LYS   A CG   1 
ATOM   1161 C  CG   B LYS   A 1 44  ? 30.175 8.949   -3.492  0.40 15.72 ?  44   LYS   A CG   1 
ATOM   1162 C  CD   A LYS   A 1 44  ? 30.942 9.853   -2.447  0.60 20.07 ?  44   LYS   A CD   1 
ATOM   1163 C  CD   B LYS   A 1 44  ? 30.891 9.661   -2.346  0.40 19.26 ?  44   LYS   A CD   1 
ATOM   1164 C  CE   A LYS   A 1 44  ? 32.277 10.364  -2.959  0.60 23.22 ?  44   LYS   A CE   1 
ATOM   1165 C  CE   B LYS   A 1 44  ? 32.179 10.311  -2.804  0.40 21.15 ?  44   LYS   A CE   1 
ATOM   1166 N  NZ   A LYS   A 1 44  ? 33.046 11.083  -1.909  0.60 24.85 ?  44   LYS   A NZ   1 
ATOM   1167 N  NZ   B LYS   A 1 44  ? 33.083 10.634  -1.663  0.40 21.47 ?  44   LYS   A NZ   1 
ATOM   1168 H  H    A LYS   A 1 44  ? 29.424 6.014   -2.322  0.60 11.24 ?  44   LYS   A H    1 
ATOM   1169 H  H    B LYS   A 1 44  ? 29.295 6.026   -2.440  0.40 12.01 ?  44   LYS   A H    1 
ATOM   1170 H  HA   A LYS   A 1 44  ? 29.344 8.354   -0.968  0.60 11.73 ?  44   LYS   A HA   1 
ATOM   1171 H  HA   B LYS   A 1 44  ? 29.270 8.347   -1.046  0.40 12.43 ?  44   LYS   A HA   1 
ATOM   1172 H  HB2  A LYS   A 1 44  ? 28.616 7.759   -3.634  0.60 14.56 ?  44   LYS   A HB2  1 
ATOM   1173 H  HB2  B LYS   A 1 44  ? 28.535 7.756   -3.717  0.40 15.62 ?  44   LYS   A HB2  1 
ATOM   1174 H  HB3  A LYS   A 1 44  ? 28.356 9.184   -2.985  0.60 14.56 ?  44   LYS   A HB3  1 
ATOM   1175 H  HB3  B LYS   A 1 44  ? 28.191 9.164   -3.070  0.40 15.62 ?  44   LYS   A HB3  1 
ATOM   1176 H  HG2  A LYS   A 1 44  ? 30.905 8.087   -3.483  0.60 17.97 ?  44   LYS   A HG2  1 
ATOM   1177 H  HG2  B LYS   A 1 44  ? 30.728 8.207   -3.783  0.40 18.89 ?  44   LYS   A HG2  1 
ATOM   1178 H  HG3  A LYS   A 1 44  ? 30.254 9.293   -4.290  0.60 17.97 ?  44   LYS   A HG3  1 
ATOM   1179 H  HG3  B LYS   A 1 44  ? 30.057 9.583   -4.218  0.40 18.89 ?  44   LYS   A HG3  1 
ATOM   1180 H  HD2  A LYS   A 1 44  ? 30.339 10.602  -2.330  0.60 24.11 ?  44   LYS   A HD2  1 
ATOM   1181 H  HD2  B LYS   A 1 44  ? 30.302 10.342  -1.974  0.40 23.14 ?  44   LYS   A HD2  1 
ATOM   1182 H  HD3  A LYS   A 1 44  ? 31.095 9.407   -1.596  0.60 24.11 ?  44   LYS   A HD3  1 
ATOM   1183 H  HD3  B LYS   A 1 44  ? 31.126 9.013   -1.662  0.40 23.14 ?  44   LYS   A HD3  1 
ATOM   1184 H  HE2  A LYS   A 1 44  ? 32.809 9.610   -3.261  0.60 27.89 ?  44   LYS   A HE2  1 
ATOM   1185 H  HE2  B LYS   A 1 44  ? 32.647 9.702   -3.394  0.40 25.41 ?  44   LYS   A HE2  1 
ATOM   1186 H  HE3  A LYS   A 1 44  ? 32.118 10.975  -3.692  0.60 27.89 ?  44   LYS   A HE3  1 
ATOM   1187 H  HE3  B LYS   A 1 44  ? 31.970 11.135  -3.268  0.40 25.41 ?  44   LYS   A HE3  1 
ATOM   1188 H  HZ1  A LYS   A 1 44  ? 33.823 11.361  -2.241  0.60 29.85 ?  44   LYS   A HZ1  1 
ATOM   1189 H  HZ1  B LYS   A 1 44  ? 33.828 11.016  -1.965  0.40 25.79 ?  44   LYS   A HZ1  1 
ATOM   1190 H  HZ2  A LYS   A 1 44  ? 32.584 11.787  -1.623  0.60 29.85 ?  44   LYS   A HZ2  1 
ATOM   1191 H  HZ2  B LYS   A 1 44  ? 32.677 11.200  -1.105  0.40 25.79 ?  44   LYS   A HZ2  1 
ATOM   1192 H  HZ3  A LYS   A 1 44  ? 33.203 10.540  -1.221  0.60 29.85 ?  44   LYS   A HZ3  1 
ATOM   1193 H  HZ3  B LYS   A 1 44  ? 33.294 9.894   -1.219  0.40 25.79 ?  44   LYS   A HZ3  1 
ATOM   1194 N  N    . HIS   A 1 45  ? 27.213 7.953   0.137   1.00 9.21  ?  45   HIS   A N    1 
ATOM   1195 C  CA   . HIS   A 1 45  ? 25.980 7.610   0.840   1.00 9.29  ?  45   HIS   A CA   1 
ATOM   1196 C  C    . HIS   A 1 45  ? 24.948 8.729   0.697   1.00 10.13 ?  45   HIS   A C    1 
ATOM   1197 O  O    . HIS   A 1 45  ? 24.660 9.473   1.632   1.00 11.52 ?  45   HIS   A O    1 
ATOM   1198 C  CB   . HIS   A 1 45  ? 26.291 7.352   2.302   1.00 9.30  ?  45   HIS   A CB   1 
ATOM   1199 C  CG   . HIS   A 1 45  ? 27.405 6.383   2.519   1.00 8.73  ?  45   HIS   A CG   1 
ATOM   1200 N  ND1  . HIS   A 1 45  ? 27.401 5.095   2.016   1.00 9.27  ?  45   HIS   A ND1  1 
ATOM   1201 C  CD2  . HIS   A 1 45  ? 28.575 6.536   3.185   1.00 9.05  ?  45   HIS   A CD2  1 
ATOM   1202 C  CE1  . HIS   A 1 45  ? 28.527 4.503   2.376   1.00 9.01  ?  45   HIS   A CE1  1 
ATOM   1203 N  NE2  . HIS   A 1 45  ? 29.252 5.350   3.090   1.00 9.28  ?  45   HIS   A NE2  1 
ATOM   1204 H  H    A HIS   A 1 45  ? 27.751 8.434   0.607   0.60 11.08 ?  45   HIS   A H    1 
ATOM   1205 H  H    B HIS   A 1 45  ? 27.781 8.392   0.613   0.40 11.08 ?  45   HIS   A H    1 
ATOM   1206 H  HA   . HIS   A 1 45  ? 25.605 6.801   0.457   1.00 11.17 ?  45   HIS   A HA   1 
ATOM   1207 H  HB2  . HIS   A 1 45  ? 26.536 8.195   2.720   1.00 11.19 ?  45   HIS   A HB2  1 
ATOM   1208 H  HB3  . HIS   A 1 45  ? 25.496 6.996   2.730   1.00 11.19 ?  45   HIS   A HB3  1 
ATOM   1209 H  HD2  . HIS   A 1 45  ? 28.866 7.301   3.631   1.00 10.89 ?  45   HIS   A HD2  1 
ATOM   1210 H  HE1  . HIS   A 1 45  ? 28.760 3.627   2.175   1.00 10.84 ?  45   HIS   A HE1  1 
ATOM   1211 H  HE2  . HIS   A 1 45  ? 30.024 5.181   3.431   1.00 11.17 ?  45   HIS   A HE2  1 
ATOM   1212 N  N    A GLY   A 1 46  ? 24.453 8.885   -0.526  0.60 10.92 ?  46   GLY   A N    1 
ATOM   1213 N  N    B GLY   A 1 46  ? 24.283 8.761   -0.457  0.40 10.48 ?  46   GLY   A N    1 
ATOM   1214 C  CA   A GLY   A 1 46  ? 23.685 10.068  -0.863  0.60 11.12 ?  46   GLY   A CA   1 
ATOM   1215 C  CA   B GLY   A 1 46  ? 23.387 9.864   -0.764  0.40 10.74 ?  46   GLY   A CA   1 
ATOM   1216 C  C    A GLY   A 1 46  ? 22.198 9.950   -0.614  0.60 10.33 ?  46   GLY   A C    1 
ATOM   1217 C  C    B GLY   A 1 46  ? 21.929 9.721   -0.365  0.40 10.61 ?  46   GLY   A C    1 
ATOM   1218 O  O    A GLY   A 1 46  ? 21.521 10.949  -0.349  0.60 10.65 ?  46   GLY   A O    1 
ATOM   1219 O  O    B GLY   A 1 46  ? 21.325 10.688  0.110   0.40 10.60 ?  46   GLY   A O    1 
ATOM   1220 H  H    A GLY   A 1 46  ? 24.541 8.322   -1.169  0.60 13.13 ?  46   GLY   A H    1 
ATOM   1221 H  H    B GLY   A 1 46  ? 24.326 8.162   -1.068  0.40 12.60 ?  46   GLY   A H    1 
ATOM   1222 H  HA2  A GLY   A 1 46  ? 24.022 10.819  -0.348  0.60 13.37 ?  46   GLY   A HA2  1 
ATOM   1223 H  HA2  B GLY   A 1 46  ? 23.707 10.659  -0.316  0.40 12.92 ?  46   GLY   A HA2  1 
ATOM   1224 H  HA3  A GLY   A 1 46  ? 23.808 10.267  -1.802  0.60 13.37 ?  46   GLY   A HA3  1 
ATOM   1225 H  HA3  B GLY   A 1 46  ? 23.417 10.029  -1.716  0.40 12.92 ?  46   GLY   A HA3  1 
ATOM   1226 N  N    A GLY   A 1 47  ? 21.672 8.736   -0.715  0.60 10.51 ?  47   GLY   A N    1 
ATOM   1227 N  N    B GLY   A 1 47  ? 21.338 8.542   -0.561  0.40 10.87 ?  47   GLY   A N    1 
ATOM   1228 C  CA   A GLY   A 1 47  ? 20.238 8.532   -0.668  0.60 11.25 ?  47   GLY   A CA   1 
ATOM   1229 C  CA   B GLY   A 1 47  ? 19.914 8.369   -0.357  0.40 10.61 ?  47   GLY   A CA   1 
ATOM   1230 C  C    A GLY   A 1 47  ? 19.917 7.086   -0.368  0.60 10.68 ?  47   GLY   A C    1 
ATOM   1231 C  C    B GLY   A 1 47  ? 19.584 6.936   -0.005  0.40 9.48  ?  47   GLY   A C    1 
ATOM   1232 O  O    A GLY   A 1 47  ? 20.807 6.257   -0.168  0.60 10.53 ?  47   GLY   A O    1 
ATOM   1233 O  O    B GLY   A 1 47  ? 20.473 6.094   0.141   0.40 9.16  ?  47   GLY   A O    1 
ATOM   1234 H  H    A GLY   A 1 47  ? 22.129 8.017   -0.799  0.60 12.63 ?  47   GLY   A H    1 
ATOM   1235 H  H    B GLY   A 1 47  ? 21.749 7.822   -0.802  0.40 13.07 ?  47   GLY   A H    1 
ATOM   1236 H  HA2  A GLY   A 1 47  ? 19.841 9.097   0.016   0.60 13.53 ?  47   GLY   A HA2  1 
ATOM   1237 H  HA2  B GLY   A 1 47  ? 19.611 8.934   0.371   0.40 12.76 ?  47   GLY   A HA2  1 
ATOM   1238 H  HA3  A GLY   A 1 47  ? 19.850 8.760   -1.526  0.60 13.53 ?  47   GLY   A HA3  1 
ATOM   1239 H  HA3  B GLY   A 1 47  ? 19.426 8.614   -1.163  0.40 12.76 ?  47   GLY   A HA3  1 
ATOM   1240 N  N    A GLY   A 1 48  ? 18.624 6.783   -0.351  0.60 10.75 ?  48   GLY   A N    1 
ATOM   1241 N  N    B GLY   A 1 48  ? 18.287 6.657   0.123   0.40 9.63  ?  48   GLY   A N    1 
ATOM   1242 C  CA   A GLY   A 1 48  ? 18.210 5.450   0.029   0.60 10.70 ?  48   GLY   A CA   1 
ATOM   1243 C  CA   B GLY   A 1 48  ? 17.886 5.324   0.523   0.40 8.86  ?  48   GLY   A CA   1 
ATOM   1244 C  C    A GLY   A 1 48  ? 18.624 5.138   1.454   0.60 10.17 ?  48   GLY   A C    1 
ATOM   1245 C  C    B GLY   A 1 48  ? 18.486 4.947   1.865   0.40 9.00  ?  48   GLY   A C    1 
ATOM   1246 O  O    A GLY   A 1 48  ? 18.780 6.029   2.300   0.60 10.29 ?  48   GLY   A O    1 
ATOM   1247 O  O    B GLY   A 1 48  ? 18.681 5.785   2.755   0.40 9.41  ?  48   GLY   A O    1 
ATOM   1248 H  H    A GLY   A 1 48  ? 17.985 7.320   -0.550  0.60 12.93 ?  48   GLY   A H    1 
ATOM   1249 H  H    B GLY   A 1 48  ? 17.632 7.211   -0.010  0.40 11.58 ?  48   GLY   A H    1 
ATOM   1250 H  HA2  A GLY   A 1 48  ? 17.251 5.366   -0.047  0.60 12.87 ?  48   GLY   A HA2  1 
ATOM   1251 H  HA2  B GLY   A 1 48  ? 16.916 5.272   0.583   0.40 10.66 ?  48   GLY   A HA2  1 
ATOM   1252 H  HA3  A GLY   A 1 48  ? 18.631 4.798   -0.555  0.60 12.87 ?  48   GLY   A HA3  1 
ATOM   1253 H  HA3  B GLY   A 1 48  ? 18.186 4.679   -0.138  0.40 10.66 ?  48   GLY   A HA3  1 
ATOM   1254 N  N    A VAL   A 1 49  ? 18.816 3.845   1.722   0.60 10.03 ?  49   VAL   A N    1 
ATOM   1255 N  N    B VAL   A 1 49  ? 18.774 3.653   2.014   0.40 9.13  ?  49   VAL   A N    1 
ATOM   1256 C  CA   A VAL   A 1 49  ? 19.253 3.404   3.046   0.60 10.08 ?  49   VAL   A CA   1 
ATOM   1257 C  CA   B VAL   A 1 49  ? 19.405 3.156   3.234   0.40 9.28  ?  49   VAL   A CA   1 
ATOM   1258 C  C    A VAL   A 1 49  ? 20.574 4.069   3.432   0.60 9.35  ?  49   VAL   A C    1 
ATOM   1259 C  C    B VAL   A 1 49  ? 20.686 3.923   3.521   0.40 9.06  ?  49   VAL   A C    1 
ATOM   1260 O  O    A VAL   A 1 49  ? 20.749 4.517   4.571   0.60 9.95  ?  49   VAL   A O    1 
ATOM   1261 O  O    B VAL   A 1 49  ? 20.944 4.323   4.662   0.40 8.60  ?  49   VAL   A O    1 
ATOM   1262 C  CB   A VAL   A 1 49  ? 19.345 1.866   3.086   0.60 11.01 ?  49   VAL   A CB   1 
ATOM   1263 C  CB   B VAL   A 1 49  ? 19.677 1.645   3.123   0.40 9.39  ?  49   VAL   A CB   1 
ATOM   1264 C  CG1  A VAL   A 1 49  ? 20.098 1.395   4.327   0.60 11.40 ?  49   VAL   A CG1  1 
ATOM   1265 C  CG1  B VAL   A 1 49  ? 20.592 1.195   4.257   0.40 8.69  ?  49   VAL   A CG1  1 
ATOM   1266 C  CG2  A VAL   A 1 49  ? 17.950 1.248   3.032   0.60 12.51 ?  49   VAL   A CG2  1 
ATOM   1267 C  CG2  B VAL   A 1 49  ? 18.381 0.859   3.132   0.40 9.94  ?  49   VAL   A CG2  1 
ATOM   1268 H  H    A VAL   A 1 49  ? 18.688 3.205   1.160   0.60 12.06 ?  49   VAL   A H    1 
ATOM   1269 H  H    B VAL   A 1 49  ? 18.615 3.048   1.430   0.40 10.98 ?  49   VAL   A H    1 
ATOM   1270 H  HA   A VAL   A 1 49  ? 18.588 3.663   3.701   0.60 12.12 ?  49   VAL   A HA   1 
ATOM   1271 H  HA   B VAL   A 1 49  ? 18.804 3.293   3.985   0.40 11.17 ?  49   VAL   A HA   1 
ATOM   1272 H  HB   A VAL   A 1 49  ? 19.837 1.553   2.308   0.60 13.24 ?  49   VAL   A HB   1 
ATOM   1273 H  HB   B VAL   A 1 49  ? 20.129 1.464   2.285   0.40 11.30 ?  49   VAL   A HB   1 
ATOM   1274 H  HG11 A VAL   A 1 49  ? 19.909 0.456   4.474   0.60 13.70 ?  49   VAL   A HG11 1 
ATOM   1275 H  HG11 B VAL   A 1 49  ? 20.510 0.235   4.368   0.40 10.45 ?  49   VAL   A HG11 1 
ATOM   1276 H  HG12 A VAL   A 1 49  ? 21.049 1.524   4.190   0.60 13.70 ?  49   VAL   A HG12 1 
ATOM   1277 H  HG12 B VAL   A 1 49  ? 21.512 1.420   4.035   0.40 10.45 ?  49   VAL   A HG12 1 
ATOM   1278 H  HG13 A VAL   A 1 49  ? 19.797 1.915   5.090   0.60 13.70 ?  49   VAL   A HG13 1 
ATOM   1279 H  HG13 B VAL   A 1 49  ? 20.330 1.644   5.076   0.40 10.45 ?  49   VAL   A HG13 1 
ATOM   1280 H  HG21 A VAL   A 1 49  ? 18.031 0.279   3.055   0.60 15.04 ?  49   VAL   A HG21 1 
ATOM   1281 H  HG21 B VAL   A 1 49  ? 18.579 -0.086  3.050   0.40 11.96 ?  49   VAL   A HG21 1 
ATOM   1282 H  HG22 A VAL   A 1 49  ? 17.443 1.554   3.799   0.60 15.04 ?  49   VAL   A HG22 1 
ATOM   1283 H  HG22 B VAL   A 1 49  ? 17.914 1.027   3.968   0.40 11.96 ?  49   VAL   A HG22 1 
ATOM   1284 H  HG23 A VAL   A 1 49  ? 17.516 1.524   2.212   0.60 15.04 ?  49   VAL   A HG23 1 
ATOM   1285 H  HG23 B VAL   A 1 49  ? 17.831 1.148   2.386   0.40 11.96 ?  49   VAL   A HG23 1 
ATOM   1286 N  N    . ALA   A 1 50  ? 21.531 4.101   2.501   1.00 9.01  ?  50   ALA   A N    1 
ATOM   1287 C  CA   . ALA   A 1 50  ? 22.849 4.670   2.772   1.00 8.70  ?  50   ALA   A CA   1 
ATOM   1288 C  C    . ALA   A 1 50  ? 22.753 6.124   3.210   1.00 8.72  ?  50   ALA   A C    1 
ATOM   1289 O  O    . ALA   A 1 50  ? 23.395 6.538   4.185   1.00 9.06  ?  50   ALA   A O    1 
ATOM   1290 C  CB   . ALA   A 1 50  ? 23.736 4.545   1.538   1.00 8.94  ?  50   ALA   A CB   1 
ATOM   1291 H  H    A ALA   A 1 50  ? 21.440 3.790   1.701   0.60 10.84 ?  50   ALA   A H    1 
ATOM   1292 H  H    B ALA   A 1 50  ? 21.370 3.906   1.677   0.40 10.84 ?  50   ALA   A H    1 
ATOM   1293 H  HA   . ALA   A 1 50  ? 23.268 4.176   3.489   1.00 10.47 ?  50   ALA   A HA   1 
ATOM   1294 H  HB1  . ALA   A 1 50  ? 24.631 4.840   1.758   1.00 10.75 ?  50   ALA   A HB1  1 
ATOM   1295 H  HB2  . ALA   A 1 50  ? 23.746 3.624   1.244   1.00 10.75 ?  50   ALA   A HB2  1 
ATOM   1296 H  HB3  . ALA   A 1 50  ? 23.368 5.110   0.836   1.00 10.75 ?  50   ALA   A HB3  1 
ATOM   1297 N  N    . GLY   A 1 51  ? 21.967 6.922   2.493   1.00 8.99  ?  51   GLY   A N    1 
ATOM   1298 C  CA   . GLY   A 1 51  ? 21.817 8.312   2.881   1.00 9.42  ?  51   GLY   A CA   1 
ATOM   1299 C  C    . GLY   A 1 51  ? 21.215 8.454   4.262   1.00 9.53  ?  51   GLY   A C    1 
ATOM   1300 O  O    . GLY   A 1 51  ? 21.600 9.339   5.032   1.00 10.03 ?  51   GLY   A O    1 
ATOM   1301 H  H    . GLY   A 1 51  ? 21.522 6.689   1.787   1.00 10.81 ?  51   GLY   A H    1 
ATOM   1302 H  HA2  . GLY   A 1 51  ? 22.683 8.744   2.875   1.00 11.34 ?  51   GLY   A HA2  1 
ATOM   1303 H  HA3  . GLY   A 1 51  ? 21.239 8.767   2.246   1.00 11.34 ?  51   GLY   A HA3  1 
ATOM   1304 N  N    . ALA   A 1 52  ? 20.256 7.586   4.591   1.00 9.72  ?  52   ALA   A N    1 
ATOM   1305 C  CA   . ALA   A 1 52  ? 19.615 7.635   5.899   1.00 10.26 ?  52   ALA   A CA   1 
ATOM   1306 C  C    . ALA   A 1 52  ? 20.573 7.220   7.013   1.00 9.52  ?  52   ALA   A C    1 
ATOM   1307 O  O    . ALA   A 1 52  ? 20.652 7.882   8.051   1.00 10.31 ?  52   ALA   A O    1 
ATOM   1308 C  CB   . ALA   A 1 52  ? 18.359 6.766   5.895   1.00 11.47 ?  52   ALA   A CB   1 
ATOM   1309 H  H    . ALA   A 1 52  ? 19.973 6.950   4.079   1.00 11.69 ?  52   ALA   A H    1 
ATOM   1310 H  HA   . ALA   A 1 52  ? 19.341 8.544   6.072   1.00 12.34 ?  52   ALA   A HA   1 
ATOM   1311 H  HB1  . ALA   A 1 52  ? 17.935 6.817   6.769   1.00 13.80 ?  52   ALA   A HB1  1 
ATOM   1312 H  HB2  . ALA   A 1 52  ? 17.748 7.096   5.216   1.00 13.80 ?  52   ALA   A HB2  1 
ATOM   1313 H  HB3  . ALA   A 1 52  ? 18.603 5.848   5.701   1.00 13.80 ?  52   ALA   A HB3  1 
ATOM   1314 N  N    A LEU   A 1 53  ? 21.319 6.130   6.814   0.60 9.42  ?  53   LEU   A N    1 
ATOM   1315 N  N    B LEU   A 1 53  ? 21.287 6.104   6.831   0.40 9.22  ?  53   LEU   A N    1 
ATOM   1316 C  CA   A LEU   A 1 53  ? 22.285 5.713   7.828   0.60 9.56  ?  53   LEU   A CA   1 
ATOM   1317 C  CA   B LEU   A 1 53  ? 22.286 5.710   7.821   0.40 9.05  ?  53   LEU   A CA   1 
ATOM   1318 C  C    A LEU   A 1 53  ? 23.360 6.773   8.019   0.60 9.17  ?  53   LEU   A C    1 
ATOM   1319 C  C    B LEU   A 1 53  ? 23.302 6.826   8.020   0.40 8.89  ?  53   LEU   A C    1 
ATOM   1320 O  O    A LEU   A 1 53  ? 23.747 7.085   9.151   0.60 9.88  ?  53   LEU   A O    1 
ATOM   1321 O  O    B LEU   A 1 53  ? 23.571 7.248   9.151   0.40 9.45  ?  53   LEU   A O    1 
ATOM   1322 C  CB   A LEU   A 1 53  ? 22.916 4.372   7.443   0.60 10.34 ?  53   LEU   A CB   1 
ATOM   1323 C  CB   B LEU   A 1 53  ? 22.993 4.417   7.394   0.40 9.13  ?  53   LEU   A CB   1 
ATOM   1324 C  CG   A LEU   A 1 53  ? 21.977 3.158   7.473   0.60 10.54 ?  53   LEU   A CG   1 
ATOM   1325 C  CG   B LEU   A 1 53  ? 22.286 3.059   7.537   0.40 9.07  ?  53   LEU   A CG   1 
ATOM   1326 C  CD1  A LEU   A 1 53  ? 22.668 1.930   6.892   0.60 10.51 ?  53   LEU   A CD1  1 
ATOM   1327 C  CD1  B LEU   A 1 53  ? 23.129 1.957   6.896   0.40 9.11  ?  53   LEU   A CD1  1 
ATOM   1328 C  CD2  A LEU   A 1 53  ? 21.499 2.877   8.887   0.60 11.47 ?  53   LEU   A CD2  1 
ATOM   1329 C  CD2  B LEU   A 1 53  ? 21.999 2.709   8.991   0.40 9.10  ?  53   LEU   A CD2  1 
ATOM   1330 H  H    A LEU   A 1 53  ? 21.286 5.625   6.116   0.60 11.33 ?  53   LEU   A H    1 
ATOM   1331 H  H    B LEU   A 1 53  ? 21.216 5.571   6.157   0.40 11.09 ?  53   LEU   A H    1 
ATOM   1332 H  HA   A LEU   A 1 53  ? 21.826 5.598   8.672   0.60 11.50 ?  53   LEU   A HA   1 
ATOM   1333 H  HA   B LEU   A 1 53  ? 21.845 5.549   8.668   0.40 10.89 ?  53   LEU   A HA   1 
ATOM   1334 H  HB2  A LEU   A 1 53  ? 23.264 4.442   6.540   0.60 12.43 ?  53   LEU   A HB2  1 
ATOM   1335 H  HB2  B LEU   A 1 53  ? 23.216 4.503   6.457   0.40 10.99 ?  53   LEU   A HB2  1 
ATOM   1336 H  HB3  A LEU   A 1 53  ? 23.643 4.186   8.056   0.60 12.43 ?  53   LEU   A HB3  1 
ATOM   1337 H  HB3  B LEU   A 1 53  ? 23.810 4.349   7.907   0.40 10.99 ?  53   LEU   A HB3  1 
ATOM   1338 H  HG   A LEU   A 1 53  ? 21.196 3.348   6.926   0.60 12.68 ?  53   LEU   A HG   1 
ATOM   1339 H  HG   B LEU   A 1 53  ? 21.441 3.086   7.066   0.40 10.91 ?  53   LEU   A HG   1 
ATOM   1340 H  HD11 A LEU   A 1 53  ? 22.054 1.180   6.921   0.60 12.64 ?  53   LEU   A HD11 1 
ATOM   1341 H  HD11 B LEU   A 1 53  ? 22.673 1.105   6.997   0.40 10.96 ?  53   LEU   A HD11 1 
ATOM   1342 H  HD12 A LEU   A 1 53  ? 22.921 2.116   5.975   0.60 12.64 ?  53   LEU   A HD12 1 
ATOM   1343 H  HD12 B LEU   A 1 53  ? 23.249 2.156   5.955   0.40 10.96 ?  53   LEU   A HD12 1 
ATOM   1344 H  HD13 A LEU   A 1 53  ? 23.456 1.735   7.422   0.60 12.64 ?  53   LEU   A HD13 1 
ATOM   1345 H  HD13 B LEU   A 1 53  ? 23.994 1.920   7.338   0.40 10.96 ?  53   LEU   A HD13 1 
ATOM   1346 H  HD21 A LEU   A 1 53  ? 21.009 2.041   8.896   0.60 13.79 ?  53   LEU   A HD21 1 
ATOM   1347 H  HD21 B LEU   A 1 53  ? 21.441 1.914   9.023   0.40 10.94 ?  53   LEU   A HD21 1 
ATOM   1348 H  HD22 A LEU   A 1 53  ? 22.270 2.816   9.473   0.60 13.79 ?  53   LEU   A HD22 1 
ATOM   1349 H  HD22 B LEU   A 1 53  ? 22.835 2.545   9.451   0.40 10.94 ?  53   LEU   A HD22 1 
ATOM   1350 H  HD23 A LEU   A 1 53  ? 20.922 3.601   9.177   0.60 13.79 ?  53   LEU   A HD23 1 
ATOM   1351 H  HD23 B LEU   A 1 53  ? 21.533 3.452   9.407   0.40 10.94 ?  53   LEU   A HD23 1 
ATOM   1352 N  N    . ASN   A 1 54  ? 23.859 7.337   6.921   1.00 8.94  ?  54   ASN   A N    1 
ATOM   1353 C  CA   . ASN   A 1 54  ? 24.907 8.336   7.043   1.00 8.93  ?  54   ASN   A CA   1 
ATOM   1354 C  C    . ASN   A 1 54  ? 24.404 9.584   7.767   1.00 9.36  ?  54   ASN   A C    1 
ATOM   1355 O  O    . ASN   A 1 54  ? 25.096 10.137  8.630   1.00 9.79  ?  54   ASN   A O    1 
ATOM   1356 C  CB   . ASN   A 1 54  ? 25.472 8.694   5.676   1.00 9.05  ?  54   ASN   A CB   1 
ATOM   1357 C  CG   . ASN   A 1 54  ? 26.483 9.805   5.779   1.00 9.43  ?  54   ASN   A CG   1 
ATOM   1358 O  OD1  . ASN   A 1 54  ? 27.492 9.665   6.478   1.00 9.38  ?  54   ASN   A OD1  1 
ATOM   1359 N  ND2  . ASN   A 1 54  ? 26.211 10.931  5.134   1.00 10.02 ?  54   ASN   A ND2  1 
ATOM   1360 H  H    A ASN   A 1 54  ? 23.609 7.158   6.117   0.60 10.75 ?  54   ASN   A H    1 
ATOM   1361 H  H    B ASN   A 1 54  ? 23.646 7.121   6.116   0.40 10.75 ?  54   ASN   A H    1 
ATOM   1362 H  HA   . ASN   A 1 54  ? 25.625 7.963   7.569   1.00 10.75 ?  54   ASN   A HA   1 
ATOM   1363 H  HB2  . ASN   A 1 54  ? 25.913 7.907   5.303   1.00 10.89 ?  54   ASN   A HB2  1 
ATOM   1364 H  HB3  . ASN   A 1 54  ? 24.752 8.976   5.093   1.00 10.89 ?  54   ASN   A HB3  1 
ATOM   1365 H  HD21 . ASN   A 1 54  ? 26.757 11.590  5.174   1.00 12.05 ?  54   ASN   A HD21 1 
ATOM   1366 H  HD22 . ASN   A 1 54  ? 25.489 10.996  4.668   1.00 12.05 ?  54   ASN   A HD22 1 
ATOM   1367 N  N    . LYS   A 1 55  ? 23.189 10.033  7.438   1.00 9.82  ?  55   LYS   A N    1 
ATOM   1368 C  CA   . LYS   A 1 55  ? 22.609 11.188  8.115   1.00 10.05 ?  55   LYS   A CA   1 
ATOM   1369 C  C    . LYS   A 1 55  ? 22.524 10.952  9.616   1.00 10.35 ?  55   LYS   A C    1 
ATOM   1370 O  O    . LYS   A 1 55  ? 22.813 11.853  10.415  1.00 10.88 ?  55   LYS   A O    1 
ATOM   1371 C  CB   . LYS   A 1 55  ? 21.234 11.492  7.513   1.00 10.80 ?  55   LYS   A CB   1 
ATOM   1372 C  CG   . LYS   A 1 55  ? 20.499 12.658  8.157   1.00 12.04 ?  55   LYS   A CG   1 
ATOM   1373 C  CD   . LYS   A 1 55  ? 19.160 12.916  7.449   1.00 13.41 ?  55   LYS   A CD   1 
ATOM   1374 C  CE   . LYS   A 1 55  ? 18.343 14.016  8.116   1.00 15.11 ?  55   LYS   A CE   1 
ATOM   1375 N  NZ   . LYS   A 1 55  ? 17.008 14.180  7.466   1.00 15.90 ?  55   LYS   A NZ   1 
ATOM   1376 H  H    . LYS   A 1 55  ? 22.675 9.681   6.837   1.00 11.81 ?  55   LYS   A H    1 
ATOM   1377 H  HA   . LYS   A 1 55  ? 23.177 11.955  7.966   1.00 12.08 ?  55   LYS   A HA   1 
ATOM   1378 H  HB2  . LYS   A 1 55  ? 21.345 11.707  6.574   1.00 12.99 ?  55   LYS   A HB2  1 
ATOM   1379 H  HB3  . LYS   A 1 55  ? 20.669 10.708  7.603   1.00 12.99 ?  55   LYS   A HB3  1 
ATOM   1380 H  HG2  . LYS   A 1 55  ? 20.314 12.448  9.088   1.00 14.47 ?  55   LYS   A HG2  1 
ATOM   1381 H  HG3  . LYS   A 1 55  ? 21.039 13.457  8.091   1.00 14.47 ?  55   LYS   A HG3  1 
ATOM   1382 H  HD2  . LYS   A 1 55  ? 19.335 13.182  6.535   1.00 16.12 ?  55   LYS   A HD2  1 
ATOM   1383 H  HD3  . LYS   A 1 55  ? 18.634 12.100  7.464   1.00 16.12 ?  55   LYS   A HD3  1 
ATOM   1384 H  HE2  . LYS   A 1 55  ? 18.201 13.788  9.049   1.00 18.16 ?  55   LYS   A HE2  1 
ATOM   1385 H  HE3  . LYS   A 1 55  ? 18.822 14.856  8.045   1.00 18.16 ?  55   LYS   A HE3  1 
ATOM   1386 H  HZ1  . LYS   A 1 55  ? 16.413 14.470  8.060   1.00 19.11 ?  55   LYS   A HZ1  1 
ATOM   1387 H  HZ2  . LYS   A 1 55  ? 17.061 14.770  6.801   1.00 19.11 ?  55   LYS   A HZ2  1 
ATOM   1388 H  HZ3  . LYS   A 1 55  ? 16.728 13.399  7.139   1.00 19.11 ?  55   LYS   A HZ3  1 
ATOM   1389 N  N    . ALA   A 1 56  ? 22.148 9.735   10.019  1.00 10.51 ?  56   ALA   A N    1 
ATOM   1390 C  CA   . ALA   A 1 56  ? 22.032 9.415   11.434  1.00 11.42 ?  56   ALA   A CA   1 
ATOM   1391 C  C    . ALA   A 1 56  ? 23.379 9.439   12.149  1.00 11.09 ?  56   ALA   A C    1 
ATOM   1392 O  O    . ALA   A 1 56  ? 23.409 9.624   13.368  1.00 12.72 ?  56   ALA   A O    1 
ATOM   1393 C  CB   . ALA   A 1 56  ? 21.339 8.059   11.614  1.00 12.41 ?  56   ALA   A CB   1 
ATOM   1394 H  H    . ALA   A 1 56  ? 21.965 9.082   9.489   1.00 12.64 ?  56   ALA   A H    1 
ATOM   1395 H  HA   . ALA   A 1 56  ? 21.469 10.078  11.852  1.00 13.73 ?  56   ALA   A HA   1 
ATOM   1396 H  HB1  . ALA   A 1 56  ? 21.265 7.861   12.564  1.00 14.91 ?  56   ALA   A HB1  1 
ATOM   1397 H  HB2  . ALA   A 1 56  ? 20.452 8.098   11.220  1.00 14.91 ?  56   ALA   A HB2  1 
ATOM   1398 H  HB3  . ALA   A 1 56  ? 21.862 7.368   11.177  1.00 14.91 ?  56   ALA   A HB3  1 
ATOM   1399 N  N    . THR   A 1 57  ? 24.488 9.268   11.419  1.00 10.33 ?  57   THR   A N    1 
ATOM   1400 C  CA   . THR   A 1 57  ? 25.834 9.389   11.985  1.00 10.31 ?  57   THR   A CA   1 
ATOM   1401 C  C    . THR   A 1 57  ? 26.386 10.808  11.910  1.00 10.46 ?  57   THR   A C    1 
ATOM   1402 O  O    . THR   A 1 57  ? 27.572 11.018  12.200  1.00 11.16 ?  57   THR   A O    1 
ATOM   1403 C  CB   . THR   A 1 57  ? 26.844 8.443   11.306  1.00 10.23 ?  57   THR   A CB   1 
ATOM   1404 O  OG1  . THR   A 1 57  ? 27.217 8.942   10.010  1.00 10.04 ?  57   THR   A OG1  1 
ATOM   1405 C  CG2  . THR   A 1 57  ? 26.319 7.026   11.207  1.00 10.42 ?  57   THR   A CG2  1 
ATOM   1406 H  H    . THR   A 1 57  ? 24.481 9.061   10.582  1.00 12.42 ?  57   THR   A H    1 
ATOM   1407 H  HA   . THR   A 1 57  ? 25.790 9.131   12.922  1.00 12.40 ?  57   THR   A HA   1 
ATOM   1408 H  HB   . THR   A 1 57  ? 27.644 8.408   11.860  1.00 12.31 ?  57   THR   A HB   1 
ATOM   1409 H  HG1  . THR   A 1 57  ? 26.534 9.002   9.524   1.00 12.07 ?  57   THR   A HG1  1 
ATOM   1410 H  HG21 . THR   A 1 57  ? 26.988 6.450   10.796  1.00 12.53 ?  57   THR   A HG21 1 
ATOM   1411 H  HG22 . THR   A 1 57  ? 26.113 6.681   12.090  1.00 12.53 ?  57   THR   A HG22 1 
ATOM   1412 H  HG23 . THR   A 1 57  ? 25.517 7.003   10.666  1.00 12.53 ?  57   THR   A HG23 1 
ATOM   1413 N  N    . ASN   A 1 58  ? 25.570 11.784  11.515  1.00 11.06 ?  58   ASN   A N    1 
ATOM   1414 C  CA   . ASN   A 1 58  ? 26.034 13.168  11.419  1.00 11.90 ?  58   ASN   A CA   1 
ATOM   1415 C  C    . ASN   A 1 58  ? 27.168 13.296  10.398  1.00 10.70 ?  58   ASN   A C    1 
ATOM   1416 O  O    . ASN   A 1 58  ? 28.065 14.128  10.544  1.00 11.46 ?  58   ASN   A O    1 
ATOM   1417 C  CB   . ASN   A 1 58  ? 26.425 13.695  12.815  1.00 14.14 ?  58   ASN   A CB   1 
ATOM   1418 C  CG   . ASN   A 1 58  ? 26.868 15.149  12.818  1.00 17.40 ?  58   ASN   A CG   1 
ATOM   1419 O  OD1  . ASN   A 1 58  ? 26.257 15.990  12.170  1.00 18.89 ?  58   ASN   A OD1  1 
ATOM   1420 N  ND2  . ASN   A 1 58  ? 27.925 15.455  13.581  1.00 18.36 ?  58   ASN   A ND2  1 
ATOM   1421 H  H    . ASN   A 1 58  ? 24.747 11.661  11.289  1.00 13.29 ?  58   ASN   A H    1 
ATOM   1422 H  HA   . ASN   A 1 58  ? 25.295 13.703  11.100  1.00 14.31 ?  58   ASN   A HA   1 
ATOM   1423 H  HB2  . ASN   A 1 58  ? 25.652 13.615  13.405  1.00 16.99 ?  58   ASN   A HB2  1 
ATOM   1424 H  HB3  . ASN   A 1 58  ? 27.154 13.165  13.164  1.00 16.99 ?  58   ASN   A HB3  1 
ATOM   1425 H  HD21 . ASN   A 1 58  ? 28.205 16.266  13.620  1.00 22.06 ?  58   ASN   A HD21 1 
ATOM   1426 H  HD22 . ASN   A 1 58  ? 28.320 14.839  14.029  1.00 22.06 ?  58   ASN   A HD22 1 
ATOM   1427 N  N    . ASN   A 1 59  ? 27.141 12.472  9.348   1.00 10.08 ?  59   ASN   A N    1 
ATOM   1428 C  CA   . ASN   A 1 59  ? 28.110 12.459  8.244   1.00 9.92  ?  59   ASN   A CA   1 
ATOM   1429 C  C    . ASN   A 1 59  ? 29.433 11.776  8.617   1.00 9.65  ?  59   ASN   A C    1 
ATOM   1430 O  O    . ASN   A 1 59  ? 30.348 11.737  7.783   1.00 9.97  ?  59   ASN   A O    1 
ATOM   1431 C  CB   . ASN   A 1 59  ? 28.387 13.846  7.638   1.00 10.24 ?  59   ASN   A CB   1 
ATOM   1432 C  CG   . ASN   A 1 59  ? 28.739 13.777  6.168   1.00 10.47 ?  59   ASN   A CG   1 
ATOM   1433 O  OD1  . ASN   A 1 59  ? 28.033 13.145  5.375   1.00 10.76 ?  59   ASN   A OD1  1 
ATOM   1434 N  ND2  . ASN   A 1 59  ? 29.818 14.447  5.787   1.00 11.16 ?  59   ASN   A ND2  1 
ATOM   1435 H  H    . ASN   A 1 59  ? 26.535 11.874  9.245   1.00 12.13 ?  59   ASN   A H    1 
ATOM   1436 H  HA   . ASN   A 1 59  ? 27.725 11.928  7.535   1.00 11.93 ?  59   ASN   A HA   1 
ATOM   1437 H  HB2  . ASN   A 1 59  ? 27.596 14.399  7.722   1.00 12.31 ?  59   ASN   A HB2  1 
ATOM   1438 H  HB3  . ASN   A 1 59  ? 29.132 14.259  8.101   1.00 12.31 ?  59   ASN   A HB3  1 
ATOM   1439 H  HD21 . ASN   A 1 59  ? 30.062 14.448  4.964   1.00 13.42 ?  59   ASN   A HD21 1 
ATOM   1440 H  HD22 . ASN   A 1 59  ? 30.289 14.884  6.370   1.00 13.42 ?  59   ASN   A HD22 1 
ATOM   1441 N  N    . ALA   A 1 60  ? 29.572 11.234  9.825   1.00 9.67  ?  60   ALA   A N    1 
ATOM   1442 C  CA   . ALA   A 1 60  ? 30.812 10.549  10.177  1.00 9.85  ?  60   ALA   A CA   1 
ATOM   1443 C  C    . ALA   A 1 60  ? 31.033 9.312   9.309   1.00 9.90  ?  60   ALA   A C    1 
ATOM   1444 O  O    . ALA   A 1 60  ? 32.175 8.991   8.959   1.00 10.32 ?  60   ALA   A O    1 
ATOM   1445 C  CB   . ALA   A 1 60  ? 30.814 10.189  11.662  1.00 10.64 ?  60   ALA   A CB   1 
ATOM   1446 H  H    . ALA   A 1 60  ? 28.978 11.245  10.446  1.00 11.63 ?  60   ALA   A H    1 
ATOM   1447 H  HA   . ALA   A 1 60  ? 31.557 11.155  10.019  1.00 11.84 ?  60   ALA   A HA   1 
ATOM   1448 H  HB1  . ALA   A 1 60  ? 31.647 9.739   11.878  1.00 12.79 ?  60   ALA   A HB1  1 
ATOM   1449 H  HB2  . ALA   A 1 60  ? 30.737 11.005  12.186  1.00 12.79 ?  60   ALA   A HB2  1 
ATOM   1450 H  HB3  . ALA   A 1 60  ? 30.064 9.606   11.847  1.00 12.79 ?  60   ALA   A HB3  1 
ATOM   1451 N  N    . MET   A 1 61  ? 29.960 8.612   8.942   1.00 9.68  ?  61   MET   A N    1 
ATOM   1452 C  CA   . MET   A 1 61  ? 30.098 7.478   8.034   1.00 9.55  ?  61   MET   A CA   1 
ATOM   1453 C  C    . MET   A 1 61  ? 30.715 7.908   6.706   1.00 9.28  ?  61   MET   A C    1 
ATOM   1454 O  O    . MET   A 1 61  ? 31.601 7.227   6.172   1.00 9.53  ?  61   MET   A O    1 
ATOM   1455 C  CB   . MET   A 1 61  ? 28.737 6.806   7.832   1.00 9.51  ?  61   MET   A CB   1 
ATOM   1456 C  CG   . MET   A 1 61  ? 28.739 5.651   6.838   1.00 10.09 ?  61   MET   A CG   1 
ATOM   1457 S  SD   . MET   A 1 61  ? 27.116 4.905   6.642   1.00 10.67 ?  61   MET   A SD   1 
ATOM   1458 C  CE   . MET   A 1 61  ? 26.987 3.998   8.187   1.00 12.20 ?  61   MET   A CE   1 
ATOM   1459 H  H    . MET   A 1 61  ? 29.157 8.770   9.202   1.00 11.65 ?  61   MET   A H    1 
ATOM   1460 H  HA   . MET   A 1 61  ? 30.685 6.825   8.446   1.00 11.49 ?  61   MET   A HA   1 
ATOM   1461 H  HB2  . MET   A 1 61  ? 28.440 6.457   8.686   1.00 11.44 ?  61   MET   A HB2  1 
ATOM   1462 H  HB3  . MET   A 1 61  ? 28.112 7.471   7.513   1.00 11.44 ?  61   MET   A HB3  1 
ATOM   1463 H  HG2  . MET   A 1 61  ? 29.012 5.977   5.964   1.00 12.13 ?  61   MET   A HG2  1 
ATOM   1464 H  HG3  . MET   A 1 61  ? 29.347 4.963   7.141   1.00 12.13 ?  61   MET   A HG3  1 
ATOM   1465 H  HE1  . MET   A 1 61  ? 26.147 3.514   8.199   1.00 14.66 ?  61   MET   A HE1  1 
ATOM   1466 H  HE2  . MET   A 1 61  ? 27.730 3.379   8.248   1.00 14.66 ?  61   MET   A HE2  1 
ATOM   1467 H  HE3  . MET   A 1 61  ? 27.018 4.627   8.926   1.00 14.66 ?  61   MET   A HE3  1 
ATOM   1468 N  N    . GLN   A 1 62  ? 30.271 9.044   6.160   1.00 9.22  ?  62   GLN   A N    1 
ATOM   1469 C  CA   . GLN   A 1 62  ? 30.816 9.514   4.891   1.00 9.51  ?  62   GLN   A CA   1 
ATOM   1470 C  C    . GLN   A 1 62  ? 32.288 9.893   5.019   1.00 9.43  ?  62   GLN   A C    1 
ATOM   1471 O  O    . GLN   A 1 62  ? 33.088 9.586   4.127   1.00 10.22 ?  62   GLN   A O    1 
ATOM   1472 C  CB   . GLN   A 1 62  ? 30.003 10.695  4.361   1.00 9.56  ?  62   GLN   A CB   1 
ATOM   1473 C  CG   . GLN   A 1 62  ? 30.381 11.063  2.940   1.00 9.42  ?  62   GLN   A CG   1 
ATOM   1474 C  CD   . GLN   A 1 62  ? 30.045 9.936   1.991   1.00 9.70  ?  62   GLN   A CD   1 
ATOM   1475 O  OE1  . GLN   A 1 62  ? 28.860 9.624   1.801   1.00 10.38 ?  62   GLN   A OE1  1 
ATOM   1476 N  NE2  . GLN   A 1 62  ? 31.061 9.271   1.448   1.00 10.35 ?  62   GLN   A NE2  1 
ATOM   1477 H  H    . GLN   A 1 62  ? 29.657 9.542   6.494   1.00 11.09 ?  62   GLN   A H    1 
ATOM   1478 H  HA   . GLN   A 1 62  ? 30.758 8.795   4.243   1.00 11.44 ?  62   GLN   A HA   1 
ATOM   1479 H  HB2  . GLN   A 1 62  ? 29.065 10.467  4.374   1.00 11.50 ?  62   GLN   A HB2  1 
ATOM   1480 H  HB3  . GLN   A 1 62  ? 30.170 11.471  4.922   1.00 11.50 ?  62   GLN   A HB3  1 
ATOM   1481 H  HG2  . GLN   A 1 62  ? 29.885 11.845  2.666   1.00 11.33 ?  62   GLN   A HG2  1 
ATOM   1482 H  HG3  . GLN   A 1 62  ? 31.336 11.229  2.886   1.00 11.33 ?  62   GLN   A HG3  1 
ATOM   1483 H  HE21 . GLN   A 1 62  ? 31.870 9.508   1.617   1.00 12.45 ?  62   GLN   A HE21 1 
ATOM   1484 H  HE22 . GLN   A 1 62  ? 30.909 8.617   0.909   1.00 12.45 ?  62   GLN   A HE22 1 
ATOM   1485 N  N    . VAL   A 1 63  ? 32.658 10.583  6.103   1.00 9.83  ?  63   VAL   A N    1 
ATOM   1486 C  CA   . VAL   A 1 63  ? 34.052 10.978  6.304   1.00 11.03 ?  63   VAL   A CA   1 
ATOM   1487 C  C    . VAL   A 1 63  ? 34.953 9.746   6.355   1.00 10.33 ?  63   VAL   A C    1 
ATOM   1488 O  O    . VAL   A 1 63  ? 36.002 9.685   5.694   1.00 10.88 ?  63   VAL   A O    1 
ATOM   1489 C  CB   . VAL   A 1 63  ? 34.169 11.853  7.567   1.00 12.30 ?  63   VAL   A CB   1 
ATOM   1490 C  CG1  . VAL   A 1 63  ? 35.614 12.099  7.923   1.00 14.27 ?  63   VAL   A CG1  1 
ATOM   1491 C  CG2  . VAL   A 1 63  ? 33.427 13.177  7.361   1.00 12.83 ?  63   VAL   A CG2  1 
ATOM   1492 H  H    . VAL   A 1 63  ? 32.121 10.829  6.733   1.00 11.82 ?  63   VAL   A H    1 
ATOM   1493 H  HA   . VAL   A 1 63  ? 34.329 11.517  5.549   1.00 13.27 ?  63   VAL   A HA   1 
ATOM   1494 H  HB   . VAL   A 1 63  ? 33.754 11.387  8.313   1.00 14.79 ?  63   VAL   A HB   1 
ATOM   1495 H  HG11 . VAL   A 1 63  ? 35.658 12.828  8.559   1.00 17.16 ?  63   VAL   A HG11 1 
ATOM   1496 H  HG12 . VAL   A 1 63  ? 35.988 11.295  8.312   1.00 17.16 ?  63   VAL   A HG12 1 
ATOM   1497 H  HG13 . VAL   A 1 63  ? 36.097 12.335  7.115   1.00 17.16 ?  63   VAL   A HG13 1 
ATOM   1498 H  HG21 . VAL   A 1 63  ? 33.524 13.721  8.161   1.00 15.42 ?  63   VAL   A HG21 1 
ATOM   1499 H  HG22 . VAL   A 1 63  ? 33.811 13.640  6.601   1.00 15.42 ?  63   VAL   A HG22 1 
ATOM   1500 H  HG23 . VAL   A 1 63  ? 32.489 12.995  7.200   1.00 15.42 ?  63   VAL   A HG23 1 
ATOM   1501 N  N    . GLU   A 1 64  ? 34.545 8.739   7.131   1.00 10.29 ?  64   GLU   A N    1 
ATOM   1502 C  CA   . GLU   A 1 64  ? 35.313 7.504   7.226   1.00 10.11 ?  64   GLU   A CA   1 
ATOM   1503 C  C    . GLU   A 1 64  ? 35.391 6.810   5.874   1.00 9.78  ?  64   GLU   A C    1 
ATOM   1504 O  O    . GLU   A 1 64  ? 36.440 6.268   5.489   1.00 10.39 ?  64   GLU   A O    1 
ATOM   1505 C  CB   . GLU   A 1 64  ? 34.637 6.596   8.253   1.00 10.85 ?  64   GLU   A CB   1 
ATOM   1506 C  CG   . GLU   A 1 64  ? 35.296 5.250   8.419   1.00 11.41 ?  64   GLU   A CG   1 
ATOM   1507 C  CD   . GLU   A 1 64  ? 34.412 4.246   9.137   1.00 11.62 ?  64   GLU   A CD   1 
ATOM   1508 O  OE1  . GLU   A 1 64  ? 33.168 4.330   8.994   1.00 12.50 ?  64   GLU   A OE1  1 
ATOM   1509 O  OE2  . GLU   A 1 64  ? 34.967 3.356   9.826   1.00 12.31 -1 64   GLU   A OE2  1 
ATOM   1510 H  H    . GLU   A 1 64  ? 33.820 8.740   7.593   1.00 12.38 ?  64   GLU   A H    1 
ATOM   1511 H  HA   . GLU   A 1 64  ? 36.213 7.710   7.528   1.00 12.16 ?  64   GLU   A HA   1 
ATOM   1512 H  HB2  . GLU   A 1 64  ? 34.660 7.046   9.119   1.00 13.05 ?  64   GLU   A HB2  1 
ATOM   1513 H  HB3  . GLU   A 1 64  ? 33.721 6.457   7.984   1.00 13.05 ?  64   GLU   A HB3  1 
ATOM   1514 H  HG2  . GLU   A 1 64  ? 35.514 4.882   7.546   1.00 13.72 ?  64   GLU   A HG2  1 
ATOM   1515 H  HG3  . GLU   A 1 64  ? 36.109 5.357   8.939   1.00 13.72 ?  64   GLU   A HG3  1 
ATOM   1516 N  N    . SER   A 1 65  ? 34.270 6.799   5.150   1.00 9.54  ?  65   SER   A N    1 
ATOM   1517 C  CA   . SER   A 1 65  ? 34.210 6.141   3.850   1.00 9.42  ?  65   SER   A CA   1 
ATOM   1518 C  C    . SER   A 1 65  ? 35.123 6.814   2.834   1.00 9.98  ?  65   SER   A C    1 
ATOM   1519 O  O    . SER   A 1 65  ? 35.757 6.136   2.016   1.00 10.73 ?  65   SER   A O    1 
ATOM   1520 C  CB   . SER   A 1 65  ? 32.774 6.149   3.332   1.00 9.44  ?  65   SER   A CB   1 
ATOM   1521 O  OG   . SER   A 1 65  ? 31.927 5.332   4.128   1.00 10.08 ?  65   SER   A OG   1 
ATOM   1522 H  H    . SER   A 1 65  ? 33.536 7.167   5.390   1.00 11.48 ?  65   SER   A H    1 
ATOM   1523 H  HA   . SER   A 1 65  ? 34.496 5.221   3.940   1.00 11.33 ?  65   SER   A HA   1 
ATOM   1524 H  HB2  . SER   A 1 65  ? 32.438 7.059   3.355   1.00 11.35 ?  65   SER   A HB2  1 
ATOM   1525 H  HB3  . SER   A 1 65  ? 32.769 5.819   2.423   1.00 11.35 ?  65   SER   A HB3  1 
ATOM   1526 H  HG   . SER   A 1 65  ? 31.925 5.609   4.922   1.00 12.12 ?  65   SER   A HG   1 
ATOM   1527 N  N    . ASP   A 1 66  ? 35.192 8.149   2.853   1.00 10.01 ?  66   ASP   A N    1 
ATOM   1528 C  CA   . ASP   A 1 66  ? 36.045 8.849   1.897   1.00 10.94 ?  66   ASP   A CA   1 
ATOM   1529 C  C    . ASP   A 1 66  ? 37.511 8.490   2.118   1.00 10.81 ?  66   ASP   A C    1 
ATOM   1530 O  O    . ASP   A 1 66  ? 38.273 8.318   1.158   1.00 11.81 ?  66   ASP   A O    1 
ATOM   1531 C  CB   . ASP   A 1 66  ? 35.830 10.357  2.010   1.00 12.02 ?  66   ASP   A CB   1 
ATOM   1532 C  CG   . ASP   A 1 66  ? 34.489 10.818  1.427   1.00 13.40 ?  66   ASP   A CG   1 
ATOM   1533 O  OD1  . ASP   A 1 66  ? 33.761 10.019  0.798   1.00 13.70 ?  66   ASP   A OD1  1 
ATOM   1534 O  OD2  . ASP   A 1 66  ? 34.190 12.017  1.583   1.00 16.29 -1 66   ASP   A OD2  1 
ATOM   1535 H  H    . ASP   A 1 66  ? 34.758 8.662   3.398   1.00 12.04 ?  66   ASP   A H    1 
ATOM   1536 H  HA   . ASP   A 1 66  ? 35.794 8.579   1.002   1.00 13.16 ?  66   ASP   A HA   1 
ATOM   1537 H  HB2  . ASP   A 1 66  ? 35.845 10.613  2.948   1.00 14.46 ?  66   ASP   A HB2  1 
ATOM   1538 H  HB3  . ASP   A 1 66  ? 36.540 10.814  1.533   1.00 14.46 ?  66   ASP   A HB3  1 
ATOM   1539 N  N    . ASP   A 1 67  ? 37.922 8.359   3.378   1.00 11.03 ?  67   ASP   A N    1 
ATOM   1540 C  CA   . ASP   A 1 67  ? 39.277 7.904   3.666   1.00 11.74 ?  67   ASP   A CA   1 
ATOM   1541 C  C    . ASP   A 1 67  ? 39.490 6.468   3.193   1.00 11.69 ?  67   ASP   A C    1 
ATOM   1542 O  O    . ASP   A 1 67  ? 40.549 6.141   2.645   1.00 12.57 ?  67   ASP   A O    1 
ATOM   1543 C  CB   . ASP   A 1 67  ? 39.558 8.033   5.161   1.00 13.06 ?  67   ASP   A CB   1 
ATOM   1544 C  CG   . ASP   A 1 67  ? 40.858 7.373   5.567   1.00 14.35 ?  67   ASP   A CG   1 
ATOM   1545 O  OD1  . ASP   A 1 67  ? 41.930 8.000   5.401   1.00 17.17 ?  67   ASP   A OD1  1 
ATOM   1546 O  OD2  . ASP   A 1 67  ? 40.809 6.215   6.044   1.00 13.89 -1 67   ASP   A OD2  1 
ATOM   1547 H  H    . ASP   A 1 67  ? 37.444 8.524   4.069   1.00 13.26 ?  67   ASP   A H    1 
ATOM   1548 H  HA   . ASP   A 1 67  ? 39.906 8.464   3.190   1.00 14.12 ?  67   ASP   A HA   1 
ATOM   1549 H  HB2  . ASP   A 1 67  ? 39.611 8.968   5.387   1.00 15.70 ?  67   ASP   A HB2  1 
ATOM   1550 H  HB3  . ASP   A 1 67  ? 38.835 7.606   5.652   1.00 15.70 ?  67   ASP   A HB3  1 
ATOM   1551 N  N    A TYR   A 1 68  ? 38.494 5.601   3.386   0.60 11.18 ?  68   TYR   A N    1 
ATOM   1552 N  N    B TYR   A 1 68  ? 38.498 5.587   3.406   0.40 11.34 ?  68   TYR   A N    1 
ATOM   1553 C  CA   A TYR   A 1 68  ? 38.618 4.220   2.927   0.60 11.10 ?  68   TYR   A CA   1 
ATOM   1554 C  CA   B TYR   A 1 68  ? 38.605 4.211   2.911   0.40 11.31 ?  68   TYR   A CA   1 
ATOM   1555 C  C    A TYR   A 1 68  ? 38.838 4.153   1.415   0.60 11.22 ?  68   TYR   A C    1 
ATOM   1556 C  C    B TYR   A 1 68  ? 38.872 4.192   1.411   0.40 11.14 ?  68   TYR   A C    1 
ATOM   1557 O  O    A TYR   A 1 68  ? 39.691 3.395   0.934   0.60 11.61 ?  68   TYR   A O    1 
ATOM   1558 O  O    B TYR   A 1 68  ? 39.786 3.505   0.937   0.40 11.26 ?  68   TYR   A O    1 
ATOM   1559 C  CB   A TYR   A 1 68  ? 37.387 3.400   3.350   0.60 11.48 ?  68   TYR   A CB   1 
ATOM   1560 C  CB   B TYR   A 1 68  ? 37.339 3.389   3.230   0.40 11.80 ?  68   TYR   A CB   1 
ATOM   1561 C  CG   A TYR   A 1 68  ? 37.450 1.992   2.809   0.60 12.32 ?  68   TYR   A CG   1 
ATOM   1562 C  CG   B TYR   A 1 68  ? 37.345 2.030   2.527   0.40 12.26 ?  68   TYR   A CG   1 
ATOM   1563 C  CD1  A TYR   A 1 68  ? 36.985 1.706   1.534   0.60 13.81 ?  68   TYR   A CD1  1 
ATOM   1564 C  CD1  B TYR   A 1 68  ? 36.856 1.893   1.228   0.40 12.30 ?  68   TYR   A CD1  1 
ATOM   1565 C  CD2  A TYR   A 1 68  ? 38.033 0.964   3.539   0.60 13.90 ?  68   TYR   A CD2  1 
ATOM   1566 C  CD2  B TYR   A 1 68  ? 37.874 0.898   3.145   0.40 12.45 ?  68   TYR   A CD2  1 
ATOM   1567 C  CE1  A TYR   A 1 68  ? 37.086 0.447   1.001   0.60 15.43 ?  68   TYR   A CE1  1 
ATOM   1568 C  CE1  B TYR   A 1 68  ? 36.892 0.677   0.571   0.40 11.83 ?  68   TYR   A CE1  1 
ATOM   1569 C  CE2  A TYR   A 1 68  ? 38.132 -0.317  3.011   0.60 15.03 ?  68   TYR   A CE2  1 
ATOM   1570 C  CE2  B TYR   A 1 68  ? 37.910 -0.328  2.496   0.40 11.99 ?  68   TYR   A CE2  1 
ATOM   1571 C  CZ   A TYR   A 1 68  ? 37.655 -0.561  1.742   0.60 15.98 ?  68   TYR   A CZ   1 
ATOM   1572 C  CZ   B TYR   A 1 68  ? 37.421 -0.425  1.215   0.40 11.30 ?  68   TYR   A CZ   1 
ATOM   1573 O  OH   A TYR   A 1 68  ? 37.757 -1.815  1.195   0.60 17.96 ?  68   TYR   A OH   1 
ATOM   1574 O  OH   B TYR   A 1 68  ? 37.475 -1.643  0.583   0.40 11.77 ?  68   TYR   A OH   1 
ATOM   1575 H  H    A TYR   A 1 68  ? 37.746 5.780   3.776   0.60 13.44 ?  68   TYR   A H    1 
ATOM   1576 H  H    B TYR   A 1 68  ? 37.765 5.757   3.828   0.40 13.64 ?  68   TYR   A H    1 
ATOM   1577 H  HA   A TYR   A 1 68  ? 39.391 3.820   3.349   0.60 13.35 ?  68   TYR   A HA   1 
ATOM   1578 H  HA   B TYR   A 1 68  ? 39.349 3.775   3.350   0.40 13.60 ?  68   TYR   A HA   1 
ATOM   1579 H  HB2  A TYR   A 1 68  ? 37.352 3.350   4.316   0.60 13.80 ?  68   TYR   A HB2  1 
ATOM   1580 H  HB2  B TYR   A 1 68  ? 37.288 3.227   4.184   0.40 14.18 ?  68   TYR   A HB2  1 
ATOM   1581 H  HB3  A TYR   A 1 68  ? 36.585 3.820   3.002   0.60 13.80 ?  68   TYR   A HB3  1 
ATOM   1582 H  HB3  B TYR   A 1 68  ? 36.552 3.875   2.932   0.40 14.18 ?  68   TYR   A HB3  1 
ATOM   1583 H  HD1  A TYR   A 1 68  ? 36.609 2.387   1.023   0.60 16.59 ?  68   TYR   A HD1  1 
ATOM   1584 H  HD1  B TYR   A 1 68  ? 36.500 2.629   0.787   0.40 14.79 ?  68   TYR   A HD1  1 
ATOM   1585 H  HD2  A TYR   A 1 68  ? 38.371 1.141   4.387   0.60 16.71 ?  68   TYR   A HD2  1 
ATOM   1586 H  HD2  B TYR   A 1 68  ? 38.211 0.966   4.002   0.40 14.96 ?  68   TYR   A HD2  1 
ATOM   1587 H  HE1  A TYR   A 1 68  ? 36.761 0.279   0.146   0.60 18.55 ?  68   TYR   A HE1  1 
ATOM   1588 H  HE1  B TYR   A 1 68  ? 36.558 0.592   -0.300  0.40 14.23 ?  68   TYR   A HE1  1 
ATOM   1589 H  HE2  A TYR   A 1 68  ? 38.528 -0.997  3.504   0.60 18.07 ?  68   TYR   A HE2  1 
ATOM   1590 H  HE2  B TYR   A 1 68  ? 38.269 -1.080  2.913   0.40 14.41 ?  68   TYR   A HE2  1 
ATOM   1591 H  HH   A TYR   A 1 68  ? 38.115 -2.335  1.741   0.60 21.57 ?  68   TYR   A HH   1 
ATOM   1592 H  HH   B TYR   A 1 68  ? 37.824 -2.222  1.085   0.40 14.15 ?  68   TYR   A HH   1 
ATOM   1593 N  N    . ILE   A 1 69  ? 38.063 4.928   0.647   1.00 10.82 ?  69   ILE   A N    1 
ATOM   1594 C  CA   . ILE   A 1 69  ? 38.191 4.919   -0.807  1.00 10.99 ?  69   ILE   A CA   1 
ATOM   1595 C  C    . ILE   A 1 69  ? 39.523 5.524   -1.239  1.00 10.79 ?  69   ILE   A C    1 
ATOM   1596 O  O    . ILE   A 1 69  ? 40.166 5.032   -2.174  1.00 11.07 ?  69   ILE   A O    1 
ATOM   1597 C  CB   . ILE   A 1 69  ? 36.990 5.637   -1.459  1.00 11.63 ?  69   ILE   A CB   1 
ATOM   1598 C  CG1  . ILE   A 1 69  ? 35.675 4.903   -1.185  1.00 12.12 ?  69   ILE   A CG1  1 
ATOM   1599 C  CG2  . ILE   A 1 69  ? 37.223 5.835   -2.958  1.00 12.69 ?  69   ILE   A CG2  1 
ATOM   1600 C  CD1  . ILE   A 1 69  ? 35.513 3.609   -1.951  1.00 12.70 ?  69   ILE   A CD1  1 
ATOM   1601 H  H    A ILE   A 1 69  ? 37.460 5.462   0.944   0.60 13.01 ?  69   ILE   A H    1 
ATOM   1602 H  H    B ILE   A 1 69  ? 37.439 5.437   0.943   0.40 13.01 ?  69   ILE   A H    1 
ATOM   1603 H  HA   . ILE   A 1 69  ? 38.184 3.998   -1.111  1.00 13.21 ?  69   ILE   A HA   1 
ATOM   1604 H  HB   . ILE   A 1 69  ? 36.921 6.510   -1.056  1.00 13.99 ?  69   ILE   A HB   1 
ATOM   1605 H  HG12 . ILE   A 1 69  ? 35.628 4.690   -0.239  1.00 14.57 ?  69   ILE   A HG12 1 
ATOM   1606 H  HG13 . ILE   A 1 69  ? 34.939 5.483   -1.428  1.00 14.57 ?  69   ILE   A HG13 1 
ATOM   1607 H  HG21 . ILE   A 1 69  ? 36.375 6.045   -3.383  1.00 15.25 ?  69   ILE   A HG21 1 
ATOM   1608 H  HG22 . ILE   A 1 69  ? 37.842 6.575   -3.086  1.00 15.25 ?  69   ILE   A HG22 1 
ATOM   1609 H  HG23 . ILE   A 1 69  ? 37.591 5.025   -3.337  1.00 15.25 ?  69   ILE   A HG23 1 
ATOM   1610 H  HD11 . ILE   A 1 69  ? 34.707 3.165   -1.645  1.00 15.27 ?  69   ILE   A HD11 1 
ATOM   1611 H  HD12 . ILE   A 1 69  ? 35.438 3.810   -2.897  1.00 15.27 ?  69   ILE   A HD12 1 
ATOM   1612 H  HD13 . ILE   A 1 69  ? 36.283 3.045   -1.790  1.00 15.27 ?  69   ILE   A HD13 1 
ATOM   1613 N  N    . ALA   A 1 70  ? 39.945 6.605   -0.584  1.00 11.15 ?  70   ALA   A N    1 
ATOM   1614 C  CA   . ALA   A 1 70  ? 41.219 7.214   -0.947  1.00 11.94 ?  70   ALA   A CA   1 
ATOM   1615 C  C    . ALA   A 1 70  ? 42.370 6.231   -0.775  1.00 12.36 ?  70   ALA   A C    1 
ATOM   1616 O  O    . ALA   A 1 70  ? 43.327 6.253   -1.551  1.00 14.20 ?  70   ALA   A O    1 
ATOM   1617 C  CB   . ALA   A 1 70  ? 41.457 8.473   -0.112  1.00 12.55 ?  70   ALA   A CB   1 
ATOM   1618 H  H    . ALA   A 1 70  ? 39.524 6.997   0.052   1.00 13.41 ?  70   ALA   A H    1 
ATOM   1619 H  HA   . ALA   A 1 70  ? 41.187 7.483   -1.880  1.00 14.35 ?  70   ALA   A HA   1 
ATOM   1620 H  HB1  . ALA   A 1 70  ? 42.312 8.863   -0.367  1.00 15.09 ?  70   ALA   A HB1  1 
ATOM   1621 H  HB2  . ALA   A 1 70  ? 40.744 9.106   -0.276  1.00 15.09 ?  70   ALA   A HB2  1 
ATOM   1622 H  HB3  . ALA   A 1 70  ? 41.478 8.229   0.828   1.00 15.09 ?  70   ALA   A HB3  1 
ATOM   1623 N  N    . THR   A 1 71  ? 42.273 5.338   0.208   1.00 11.81 ?  71   THR   A N    1 
ATOM   1624 C  CA   . THR   A 1 71  ? 43.325 4.358   0.453   1.00 13.16 ?  71   THR   A CA   1 
ATOM   1625 C  C    . THR   A 1 71  ? 43.204 3.133   -0.444  1.00 13.36 ?  71   THR   A C    1 
ATOM   1626 O  O    . THR   A 1 71  ? 44.217 2.626   -0.947  1.00 15.22 ?  71   THR   A O    1 
ATOM   1627 C  CB   . THR   A 1 71  ? 43.263 3.911   1.908   1.00 15.01 ?  71   THR   A CB   1 
ATOM   1628 O  OG1  . THR   A 1 71  ? 43.525 5.034   2.754   1.00 16.32 ?  71   THR   A OG1  1 
ATOM   1629 C  CG2  . THR   A 1 71  ? 44.268 2.791   2.184   1.00 16.32 ?  71   THR   A CG2  1 
ATOM   1630 H  H    . THR   A 1 71  ? 41.604 5.275   0.745   1.00 14.20 ?  71   THR   A H    1 
ATOM   1631 H  HA   . THR   A 1 71  ? 44.190 4.764   0.290   1.00 15.81 ?  71   THR   A HA   1 
ATOM   1632 H  HB   . THR   A 1 71  ? 42.377 3.565   2.098   1.00 18.04 ?  71   THR   A HB   1 
ATOM   1633 H  HG1  . THR   A 1 71  ? 43.503 4.786   3.559   1.00 19.61 ?  71   THR   A HG1  1 
ATOM   1634 H  HG21 . THR   A 1 71  ? 44.420 2.712   3.139   1.00 19.61 ?  71   THR   A HG21 1 
ATOM   1635 H  HG22 . THR   A 1 71  ? 43.935 1.944   1.849   1.00 19.61 ?  71   THR   A HG22 1 
ATOM   1636 H  HG23 . THR   A 1 71  ? 45.115 2.990   1.751   1.00 19.61 ?  71   THR   A HG23 1 
ATOM   1637 N  N    . ASN   A 1 72  ? 41.978 2.630   -0.635  1.00 12.33 ?  72   ASN   A N    1 
ATOM   1638 C  CA   . ASN   A 1 72  ? 41.761 1.303   -1.195  1.00 12.60 ?  72   ASN   A CA   1 
ATOM   1639 C  C    . ASN   A 1 72  ? 41.127 1.293   -2.574  1.00 12.94 ?  72   ASN   A C    1 
ATOM   1640 O  O    . ASN   A 1 72  ? 41.129 0.239   -3.220  1.00 14.04 ?  72   ASN   A O    1 
ATOM   1641 C  CB   . ASN   A 1 72  ? 40.881 0.477   -0.249  1.00 13.44 ?  72   ASN   A CB   1 
ATOM   1642 C  CG   . ASN   A 1 72  ? 41.499 0.328   1.115   1.00 14.23 ?  72   ASN   A CG   1 
ATOM   1643 O  OD1  . ASN   A 1 72  ? 41.046 0.932   2.087   1.00 16.10 ?  72   ASN   A OD1  1 
ATOM   1644 N  ND2  . ASN   A 1 72  ? 42.549 -0.454  1.195   1.00 14.75 ?  72   ASN   A ND2  1 
ATOM   1645 H  H    . ASN   A 1 72  ? 41.243 3.051   -0.447  1.00 14.82 ?  72   ASN   A H    1 
ATOM   1646 H  HA   . ASN   A 1 72  ? 42.614 0.859   -1.269  1.00 15.15 ?  72   ASN   A HA   1 
ATOM   1647 H  HB2  . ASN   A 1 72  ? 40.023 0.910   -0.147  1.00 16.16 ?  72   ASN   A HB2  1 
ATOM   1648 H  HB3  . ASN   A 1 72  ? 40.767 -0.413  -0.622  1.00 16.16 ?  72   ASN   A HB3  1 
ATOM   1649 H  HD21 . ASN   A 1 72  ? 42.943 -0.565  1.954   1.00 17.73 ?  72   ASN   A HD21 1 
ATOM   1650 H  HD22 . ASN   A 1 72  ? 42.846 -0.853  0.496   1.00 17.73 ?  72   ASN   A HD22 1 
ATOM   1651 N  N    . GLY   A 1 73  ? 40.565 2.403   -3.030  1.00 12.54 ?  73   GLY   A N    1 
ATOM   1652 C  CA   . GLY   A 1 73  ? 39.827 2.414   -4.267  1.00 12.33 ?  73   GLY   A CA   1 
ATOM   1653 C  C    . GLY   A 1 73  ? 38.431 1.846   -4.091  1.00 11.73 ?  73   GLY   A C    1 
ATOM   1654 O  O    . GLY   A 1 73  ? 38.046 1.385   -3.009  1.00 12.32 ?  73   GLY   A O    1 
ATOM   1655 H  H    . GLY   A 1 73  ? 40.602 3.173   -2.641  1.00 15.07 ?  73   GLY   A H    1 
ATOM   1656 H  HA2  . GLY   A 1 73  ? 39.757 3.325   -4.594  1.00 14.83 ?  73   GLY   A HA2  1 
ATOM   1657 H  HA3  . GLY   A 1 73  ? 40.300 1.885   -4.933  1.00 14.83 ?  73   GLY   A HA3  1 
ATOM   1658 N  N    . PRO   A 1 74  ? 37.651 1.870   -5.170  1.00 12.03 ?  74   PRO   A N    1 
ATOM   1659 C  CA   . PRO   A 1 74  ? 36.254 1.438   -5.087  1.00 11.96 ?  74   PRO   A CA   1 
ATOM   1660 C  C    . PRO   A 1 74  ? 36.109 -0.045  -4.769  1.00 11.49 ?  74   PRO   A C    1 
ATOM   1661 O  O    . PRO   A 1 74  ? 36.978 -0.877  -5.055  1.00 12.40 ?  74   PRO   A O    1 
ATOM   1662 C  CB   . PRO   A 1 74  ? 35.704 1.747   -6.487  1.00 13.68 ?  74   PRO   A CB   1 
ATOM   1663 C  CG   . PRO   A 1 74  ? 36.644 2.744   -7.078  1.00 16.14 ?  74   PRO   A CG   1 
ATOM   1664 C  CD   . PRO   A 1 74  ? 37.987 2.398   -6.503  1.00 14.06 ?  74   PRO   A CD   1 
ATOM   1665 H  HA   . PRO   A 1 74  ? 35.771 1.966   -4.430  1.00 14.38 ?  74   PRO   A HA   1 
ATOM   1666 H  HB2  . PRO   A 1 74  ? 35.685 0.936   -7.016  1.00 16.44 ?  74   PRO   A HB2  1 
ATOM   1667 H  HB3  . PRO   A 1 74  ? 34.810 2.126   -6.411  1.00 16.44 ?  74   PRO   A HB3  1 
ATOM   1668 H  HG2  . PRO   A 1 74  ? 36.654 2.658   -8.044  1.00 19.40 ?  74   PRO   A HG2  1 
ATOM   1669 H  HG3  . PRO   A 1 74  ? 36.383 3.641   -6.817  1.00 19.40 ?  74   PRO   A HG3  1 
ATOM   1670 H  HD2  . PRO   A 1 74  ? 38.424 1.717   -7.040  1.00 16.89 ?  74   PRO   A HD2  1 
ATOM   1671 H  HD3  . PRO   A 1 74  ? 38.537 3.199   -6.437  1.00 16.89 ?  74   PRO   A HD3  1 
ATOM   1672 N  N    . LEU   A 1 75  ? 34.968 -0.366  -4.171  1.00 10.79 ?  75   LEU   A N    1 
ATOM   1673 C  CA   . LEU   A 1 75  ? 34.567 -1.755  -4.017  1.00 10.74 ?  75   LEU   A CA   1 
ATOM   1674 C  C    . LEU   A 1 75  ? 34.174 -2.334  -5.374  1.00 11.29 ?  75   LEU   A C    1 
ATOM   1675 O  O    . LEU   A 1 75  ? 34.054 -1.623  -6.377  1.00 12.91 ?  75   LEU   A O    1 
ATOM   1676 C  CB   . LEU   A 1 75  ? 33.384 -1.877  -3.055  1.00 10.69 ?  75   LEU   A CB   1 
ATOM   1677 C  CG   . LEU   A 1 75  ? 33.607 -1.463  -1.602  1.00 12.18 ?  75   LEU   A CG   1 
ATOM   1678 C  CD1  . LEU   A 1 75  ? 32.324 -1.648  -0.798  1.00 13.91 ?  75   LEU   A CD1  1 
ATOM   1679 C  CD2  . LEU   A 1 75  ? 34.738 -2.213  -0.969  1.00 15.18 ?  75   LEU   A CD2  1 
ATOM   1680 H  H    . LEU   A 1 75  ? 34.402 0.202   -3.857  1.00 12.98 ?  75   LEU   A H    1 
ATOM   1681 H  HA   . LEU   A 1 75  ? 35.310 -2.267  -3.671  1.00 12.91 ?  75   LEU   A HA   1 
ATOM   1682 H  HB2  . LEU   A 1 75  ? 32.660 -1.332  -3.400  1.00 12.86 ?  75   LEU   A HB2  1 
ATOM   1683 H  HB3  . LEU   A 1 75  ? 33.104 -2.806  -3.047  1.00 12.86 ?  75   LEU   A HB3  1 
ATOM   1684 H  HG   . LEU   A 1 75  ? 33.836 -0.521  -1.583  1.00 14.64 ?  75   LEU   A HG   1 
ATOM   1685 H  HD11 . LEU   A 1 75  ? 32.487 -1.376  0.119   1.00 16.71 ?  75   LEU   A HD11 1 
ATOM   1686 H  HD12 . LEU   A 1 75  ? 31.628 -1.095  -1.188  1.00 16.71 ?  75   LEU   A HD12 1 
ATOM   1687 H  HD13 . LEU   A 1 75  ? 32.064 -2.580  -0.829  1.00 16.71 ?  75   LEU   A HD13 1 
ATOM   1688 H  HD21 . LEU   A 1 75  ? 34.794 -1.973  -0.032  1.00 18.25 ?  75   LEU   A HD21 1 
ATOM   1689 H  HD22 . LEU   A 1 75  ? 34.577 -3.167  -1.057  1.00 18.25 ?  75   LEU   A HD22 1 
ATOM   1690 H  HD23 . LEU   A 1 75  ? 35.569 -1.979  -1.419  1.00 18.25 ?  75   LEU   A HD23 1 
ATOM   1691 N  N    . LYS   A 1 76  ? 33.985 -3.651  -5.390  1.00 11.52 ?  76   LYS   A N    1 
ATOM   1692 C  CA   . LYS   A 1 76  ? 33.386 -4.368  -6.508  1.00 12.25 ?  76   LYS   A CA   1 
ATOM   1693 C  C    . LYS   A 1 76  ? 31.875 -4.454  -6.306  1.00 10.91 ?  76   LYS   A C    1 
ATOM   1694 O  O    . LYS   A 1 76  ? 31.402 -4.584  -5.179  1.00 10.84 ?  76   LYS   A O    1 
ATOM   1695 C  CB   . LYS   A 1 76  ? 33.934 -5.807  -6.561  1.00 14.02 ?  76   LYS   A CB   1 
ATOM   1696 C  CG   . LYS   A 1 76  ? 35.449 -5.920  -6.755  1.00 15.64 ?  76   LYS   A CG   1 
ATOM   1697 C  CD   . LYS   A 1 76  ? 35.976 -7.326  -6.540  1.00 17.15 ?  76   LYS   A CD   1 
ATOM   1698 C  CE   . LYS   A 1 76  ? 37.478 -7.384  -6.732  1.00 19.51 ?  76   LYS   A CE   1 
ATOM   1699 N  NZ   . LYS   A 1 76  ? 38.022 -8.739  -6.517  1.00 20.61 ?  76   LYS   A NZ   1 
ATOM   1700 H  H    . LYS   A 1 76  ? 34.205 -4.168  -4.739  1.00 13.85 ?  76   LYS   A H    1 
ATOM   1701 H  HA   . LYS   A 1 76  ? 33.579 -3.920  -7.348  1.00 14.72 ?  76   LYS   A HA   1 
ATOM   1702 H  HB2  . LYS   A 1 76  ? 33.712 -6.253  -5.729  1.00 16.85 ?  76   LYS   A HB2  1 
ATOM   1703 H  HB3  . LYS   A 1 76  ? 33.510 -6.273  -7.301  1.00 16.85 ?  76   LYS   A HB3  1 
ATOM   1704 H  HG2  . LYS   A 1 76  ? 35.672 -5.651  -7.661  1.00 18.80 ?  76   LYS   A HG2  1 
ATOM   1705 H  HG3  . LYS   A 1 76  ? 35.891 -5.334  -6.119  1.00 18.80 ?  76   LYS   A HG3  1 
ATOM   1706 H  HD2  . LYS   A 1 76  ? 35.769 -7.611  -5.635  1.00 20.61 ?  76   LYS   A HD2  1 
ATOM   1707 H  HD3  . LYS   A 1 76  ? 35.560 -7.925  -7.183  1.00 20.61 ?  76   LYS   A HD3  1 
ATOM   1708 H  HE2  . LYS   A 1 76  ? 37.690 -7.113  -7.637  1.00 23.44 ?  76   LYS   A HE2  1 
ATOM   1709 H  HE3  . LYS   A 1 76  ? 37.898 -6.786  -6.095  1.00 23.44 ?  76   LYS   A HE3  1 
ATOM   1710 H  HZ1  . LYS   A 1 76  ? 38.902 -8.740  -6.637  1.00 24.76 ?  76   LYS   A HZ1  1 
ATOM   1711 H  HZ2  . LYS   A 1 76  ? 37.842 -9.016  -5.688  1.00 24.76 ?  76   LYS   A HZ2  1 
ATOM   1712 H  HZ3  . LYS   A 1 76  ? 37.652 -9.313  -7.094  1.00 24.76 ?  76   LYS   A HZ3  1 
ATOM   1713 N  N    . VAL   A 1 77  ? 31.117 -4.430  -7.408  1.00 11.19 ?  77   VAL   A N    1 
ATOM   1714 C  CA   . VAL   A 1 77  ? 29.711 -4.818  -7.317  1.00 11.31 ?  77   VAL   A CA   1 
ATOM   1715 C  C    . VAL   A 1 77  ? 29.649 -6.271  -6.870  1.00 10.92 ?  77   VAL   A C    1 
ATOM   1716 O  O    . VAL   A 1 77  ? 30.309 -7.138  -7.454  1.00 11.09 ?  77   VAL   A O    1 
ATOM   1717 C  CB   . VAL   A 1 77  ? 28.978 -4.601  -8.651  1.00 12.52 ?  77   VAL   A CB   1 
ATOM   1718 C  CG1  . VAL   A 1 77  ? 27.523 -5.057  -8.536  1.00 13.10 ?  77   VAL   A CG1  1 
ATOM   1719 C  CG2  . VAL   A 1 77  ? 29.041 -3.140  -9.065  1.00 14.20 ?  77   VAL   A CG2  1 
ATOM   1720 H  H    . VAL   A 1 77  ? 31.391 -4.199  -8.190  1.00 13.45 ?  77   VAL   A H    1 
ATOM   1721 H  HA   . VAL   A 1 77  ? 29.279 -4.275  -6.641  1.00 13.60 ?  77   VAL   A HA   1 
ATOM   1722 H  HB   . VAL   A 1 77  ? 29.413 -5.130  -9.341  1.00 15.05 ?  77   VAL   A HB   1 
ATOM   1723 H  HG11 . VAL   A 1 77  ? 27.045 -4.763  -9.324  1.00 15.74 ?  77   VAL   A HG11 1 
ATOM   1724 H  HG12 . VAL   A 1 77  ? 27.499 -6.022  -8.471  1.00 15.74 ?  77   VAL   A HG12 1 
ATOM   1725 H  HG13 . VAL   A 1 77  ? 27.136 -4.657  -7.742  1.00 15.74 ?  77   VAL   A HG13 1 
ATOM   1726 H  HG21 . VAL   A 1 77  ? 28.540 -3.026  -9.887  1.00 17.07 ?  77   VAL   A HG21 1 
ATOM   1727 H  HG22 . VAL   A 1 77  ? 28.649 -2.598  -8.361  1.00 17.07 ?  77   VAL   A HG22 1 
ATOM   1728 H  HG23 . VAL   A 1 77  ? 29.966 -2.886  -9.201  1.00 17.07 ?  77   VAL   A HG23 1 
ATOM   1729 N  N    . GLY   A 1 78  ? 28.864 -6.545  -5.825  1.00 10.51 ?  78   GLY   A N    1 
ATOM   1730 C  CA   . GLY   A 1 78  ? 28.855 -7.837  -5.166  1.00 10.58 ?  78   GLY   A CA   1 
ATOM   1731 C  C    . GLY   A 1 78  ? 29.785 -7.927  -3.974  1.00 10.11 ?  78   GLY   A C    1 
ATOM   1732 O  O    . GLY   A 1 78  ? 29.740 -8.931  -3.246  1.00 10.79 ?  78   GLY   A O    1 
ATOM   1733 H  H    . GLY   A 1 78  ? 28.311 -5.977  -5.481  1.00 12.64 ?  78   GLY   A H    1 
ATOM   1734 H  HA2  . GLY   A 1 78  ? 27.954 -8.029  -4.867  1.00 12.72 ?  78   GLY   A HA2  1 
ATOM   1735 H  HA3  . GLY   A 1 78  ? 29.114 -8.516  -5.807  1.00 12.72 ?  78   GLY   A HA3  1 
ATOM   1736 N  N    . GLY   A 1 79  ? 30.634 -6.920  -3.760  1.00 10.14 ?  79   GLY   A N    1 
ATOM   1737 C  CA   . GLY   A 1 79  ? 31.609 -6.934  -2.694  1.00 10.43 ?  79   GLY   A CA   1 
ATOM   1738 C  C    . GLY   A 1 79  ? 31.174 -6.142  -1.475  1.00 9.94  ?  79   GLY   A C    1 
ATOM   1739 O  O    . GLY   A 1 79  ? 30.054 -5.635  -1.384  1.00 10.48 ?  79   GLY   A O    1 
ATOM   1740 H  H    . GLY   A 1 79  ? 30.664 -6.202  -4.237  1.00 12.19 ?  79   GLY   A H    1 
ATOM   1741 H  HA2  . GLY   A 1 79  ? 31.764 -7.860  -2.421  1.00 12.54 ?  79   GLY   A HA2  1 
ATOM   1742 H  HA3  . GLY   A 1 79  ? 32.446 -6.575  -3.017  1.00 12.54 ?  79   GLY   A HA3  1 
ATOM   1743 N  N    . SER   A 1 80  ? 32.094 -6.040  -0.518  1.00 10.51 ?  80   SER   A N    1 
ATOM   1744 C  CA   . SER   A 1 80  ? 31.788 -5.415  0.756   1.00 9.86  ?  80   SER   A CA   1 
ATOM   1745 C  C    . SER   A 1 80  ? 33.066 -4.970  1.447   1.00 10.01 ?  80   SER   A C    1 
ATOM   1746 O  O    . SER   A 1 80  ? 34.178 -5.403  1.108   1.00 11.44 ?  80   SER   A O    1 
ATOM   1747 C  CB   . SER   A 1 80  ? 31.041 -6.381  1.684   1.00 11.31 ?  80   SER   A CB   1 
ATOM   1748 O  OG   . SER   A 1 80  ? 31.878 -7.432  2.141   1.00 12.74 ?  80   SER   A OG   1 
ATOM   1749 H  H    . SER   A 1 80  ? 32.906 -6.311  -0.593  1.00 12.64 ?  80   SER   A H    1 
ATOM   1750 H  HA   . SER   A 1 80  ? 31.231 -4.635  0.592   1.00 11.86 ?  80   SER   A HA   1 
ATOM   1751 H  HB2  . SER   A 1 80  ? 30.711 -5.887  2.448   1.00 13.60 ?  80   SER   A HB2  1 
ATOM   1752 H  HB3  . SER   A 1 80  ? 30.292 -6.764  1.193   1.00 13.60 ?  80   SER   A HB3  1 
ATOM   1753 H  HG   . SER   A 1 80  ? 32.168 -7.864  1.475   1.00 15.31 ?  80   SER   A HG   1 
ATOM   1754 N  N    . CYS   A 1 81  ? 32.878 -4.117  2.452   1.00 9.69  ?  81   CYS   A N    1 
ATOM   1755 C  CA   . CYS   A 1 81  ? 33.932 -3.836  3.411   1.00 10.00 ?  81   CYS   A CA   1 
ATOM   1756 C  C    . CYS   A 1 81  ? 33.301 -3.606  4.776   1.00 9.64  ?  81   CYS   A C    1 
ATOM   1757 O  O    . CYS   A 1 81  ? 32.134 -3.209  4.879   1.00 10.75 ?  81   CYS   A O    1 
ATOM   1758 C  CB   . CYS   A 1 81  ? 34.806 -2.645  2.991   1.00 10.77 ?  81   CYS   A CB   1 
ATOM   1759 S  SG   . CYS   A 1 81  ? 33.908 -1.067  3.026   1.00 10.64 ?  81   CYS   A SG   1 
ATOM   1760 H  H    . CYS   A 1 81  ? 32.144 -3.683  2.601   1.00 11.66 ?  81   CYS   A H    1 
ATOM   1761 H  HA   . CYS   A 1 81  ? 34.508 -4.610  3.476   1.00 12.02 ?  81   CYS   A HA   1 
ATOM   1762 H  HB2  . CYS   A 1 81  ? 35.562 -2.578  3.595   1.00 12.95 ?  81   CYS   A HB2  1 
ATOM   1763 H  HB3  . CYS   A 1 81  ? 35.123 -2.794  2.083   1.00 12.95 ?  81   CYS   A HB3  1 
ATOM   1764 H  HG   . CYS   A 1 81  ? 34.652 -0.187  2.683   1.00 12.79 ?  81   CYS   A HG   1 
ATOM   1765 N  N    . VAL   A 1 82  ? 34.084 -3.859  5.823   1.00 10.18 ?  82   VAL   A N    1 
ATOM   1766 C  CA   . VAL   A 1 82  ? 33.669 -3.616  7.200   1.00 10.56 ?  82   VAL   A CA   1 
ATOM   1767 C  C    . VAL   A 1 82  ? 34.270 -2.299  7.671   1.00 10.41 ?  82   VAL   A C    1 
ATOM   1768 O  O    . VAL   A 1 82  ? 35.494 -2.123  7.647   1.00 11.44 ?  82   VAL   A O    1 
ATOM   1769 C  CB   . VAL   A 1 82  ? 34.100 -4.756  8.135   1.00 12.01 ?  82   VAL   A CB   1 
ATOM   1770 C  CG1  . VAL   A 1 82  ? 33.661 -4.449  9.559   1.00 13.37 ?  82   VAL   A CG1  1 
ATOM   1771 C  CG2  . VAL   A 1 82  ? 33.536 -6.086  7.670   1.00 12.95 ?  82   VAL   A CG2  1 
ATOM   1772 H  H    . VAL   A 1 82  ? 34.882 -4.188  5.760   1.00 12.24 ?  82   VAL   A H    1 
ATOM   1773 H  HA   . VAL   A 1 82  ? 32.702 -3.541  7.233   1.00 12.69 ?  82   VAL   A HA   1 
ATOM   1774 H  HB   . VAL   A 1 82  ? 35.067 -4.815  8.133   1.00 14.44 ?  82   VAL   A HB   1 
ATOM   1775 H  HG11 . VAL   A 1 82  ? 33.731 -5.256  10.093  1.00 16.08 ?  82   VAL   A HG11 1 
ATOM   1776 H  HG12 . VAL   A 1 82  ? 34.230 -3.757  9.933   1.00 16.08 ?  82   VAL   A HG12 1 
ATOM   1777 H  HG13 . VAL   A 1 82  ? 32.737 -4.144  9.549   1.00 16.08 ?  82   VAL   A HG13 1 
ATOM   1778 H  HG21 . VAL   A 1 82  ? 33.793 -6.773  8.302   1.00 15.56 ?  82   VAL   A HG21 1 
ATOM   1779 H  HG22 . VAL   A 1 82  ? 32.571 -6.018  7.622   1.00 15.56 ?  82   VAL   A HG22 1 
ATOM   1780 H  HG23 . VAL   A 1 82  ? 33.900 -6.288  6.794   1.00 15.56 ?  82   VAL   A HG23 1 
ATOM   1781 N  N    . LEU   A 1 83  ? 33.413 -1.381  8.105   1.00 10.00 ?  83   LEU   A N    1 
ATOM   1782 C  CA   . LEU   A 1 83  ? 33.839 -0.119  8.688   1.00 10.08 ?  83   LEU   A CA   1 
ATOM   1783 C  C    . LEU   A 1 83  ? 33.130 0.054   10.027  1.00 10.28 ?  83   LEU   A C    1 
ATOM   1784 O  O    . LEU   A 1 83  ? 32.412 -0.837  10.496  1.00 10.85 ?  83   LEU   A O    1 
ATOM   1785 C  CB   . LEU   A 1 83  ? 33.590 1.047   7.715   1.00 10.60 ?  83   LEU   A CB   1 
ATOM   1786 C  CG   . LEU   A 1 83  ? 34.474 1.053   6.461   1.00 11.22 ?  83   LEU   A CG   1 
ATOM   1787 C  CD1  . LEU   A 1 83  ? 34.007 2.091   5.459   1.00 11.81 ?  83   LEU   A CD1  1 
ATOM   1788 C  CD2  . LEU   A 1 83  ? 35.939 1.271   6.822   1.00 12.00 ?  83   LEU   A CD2  1 
ATOM   1789 H  H    . LEU   A 1 83  ? 32.558 -1.468  8.059   1.00 12.02 ?  83   LEU   A H    1 
ATOM   1790 H  HA   . LEU   A 1 83  ? 34.791 -0.156  8.859   1.00 12.13 ?  83   LEU   A HA   1 
ATOM   1791 H  HB2  . LEU   A 1 83  ? 32.669 1.018   7.416   1.00 12.74 ?  83   LEU   A HB2  1 
ATOM   1792 H  HB3  . LEU   A 1 83  ? 33.749 1.884   8.185   1.00 12.74 ?  83   LEU   A HB3  1 
ATOM   1793 H  HG   . LEU   A 1 83  ? 34.414 0.185   6.039   1.00 13.49 ?  83   LEU   A HG   1 
ATOM   1794 H  HD11 . LEU   A 1 83  ? 34.589 2.058   4.680   1.00 14.19 ?  83   LEU   A HD11 1 
ATOM   1795 H  HD12 . LEU   A 1 83  ? 33.097 1.878   5.197   1.00 14.19 ?  83   LEU   A HD12 1 
ATOM   1796 H  HD13 . LEU   A 1 83  ? 34.043 2.965   5.866   1.00 14.19 ?  83   LEU   A HD13 1 
ATOM   1797 H  HD21 . LEU   A 1 83  ? 36.453 1.408   6.006   1.00 14.43 ?  83   LEU   A HD21 1 
ATOM   1798 H  HD22 . LEU   A 1 83  ? 36.016 2.059   7.388   1.00 14.43 ?  83   LEU   A HD22 1 
ATOM   1799 H  HD23 . LEU   A 1 83  ? 36.276 0.495   7.294   1.00 14.43 ?  83   LEU   A HD23 1 
ATOM   1800 N  N    . SER   A 1 84  ? 33.345 1.204   10.658  1.00 10.72 ?  84   SER   A N    1 
ATOM   1801 C  CA   . SER   A 1 84  ? 32.705 1.460   11.937  1.00 10.92 ?  84   SER   A CA   1 
ATOM   1802 C  C    . SER   A 1 84  ? 31.187 1.541   11.795  1.00 10.74 ?  84   SER   A C    1 
ATOM   1803 O  O    . SER   A 1 84  ? 30.656 2.009   10.787  1.00 11.12 ?  84   SER   A O    1 
ATOM   1804 C  CB   . SER   A 1 84  ? 33.208 2.776   12.520  1.00 11.95 ?  84   SER   A CB   1 
ATOM   1805 O  OG   . SER   A 1 84  ? 32.575 3.051   13.756  1.00 12.72 ?  84   SER   A OG   1 
ATOM   1806 H  H    . SER   A 1 84  ? 33.840 1.848   10.357  1.00 12.89 ?  84   SER   A H    1 
ATOM   1807 H  HA   . SER   A 1 84  ? 32.923 0.745   12.545  1.00 13.13 ?  84   SER   A HA   1 
ATOM   1808 H  HB2  . SER   A 1 84  ? 34.167 2.713   12.661  1.00 14.37 ?  84   SER   A HB2  1 
ATOM   1809 H  HB3  . SER   A 1 84  ? 33.015 3.496   11.897  1.00 14.37 ?  84   SER   A HB3  1 
ATOM   1810 H  HG   . SER   A 1 84  ? 32.859 3.775   14.071  1.00 15.30 ?  84   SER   A HG   1 
ATOM   1811 N  N    . GLY   A 1 85  ? 30.487 1.120   12.844  1.00 11.66 ?  85   GLY   A N    1 
ATOM   1812 C  CA   . GLY   A 1 85  ? 29.066 1.359   12.944  1.00 12.62 ?  85   GLY   A CA   1 
ATOM   1813 C  C    . GLY   A 1 85  ? 28.702 2.673   13.598  1.00 11.90 ?  85   GLY   A C    1 
ATOM   1814 O  O    . GLY   A 1 85  ? 27.513 2.990   13.726  1.00 12.26 ?  85   GLY   A O    1 
ATOM   1815 H  H    . GLY   A 1 85  ? 30.829 0.692   13.512  1.00 14.02 ?  85   GLY   A H    1 
ATOM   1816 H  HA2  . GLY   A 1 85  ? 28.686 1.349   12.056  1.00 15.17 ?  85   GLY   A HA2  1 
ATOM   1817 H  HA3  . GLY   A 1 85  ? 28.666 0.650   13.460  1.00 15.17 ?  85   GLY   A HA3  1 
ATOM   1818 N  N    . HIS   A 1 86  ? 29.692 3.448   14.027  1.00 11.43 ?  86   HIS   A N    1 
ATOM   1819 C  CA   . HIS   A 1 86  ? 29.474 4.778   14.605  1.00 11.86 ?  86   HIS   A CA   1 
ATOM   1820 C  C    . HIS   A 1 86  ? 28.505 4.649   15.773  1.00 12.76 ?  86   HIS   A C    1 
ATOM   1821 O  O    . HIS   A 1 86  ? 28.698 3.770   16.628  1.00 13.74 ?  86   HIS   A O    1 
ATOM   1822 C  CB   . HIS   A 1 86  ? 29.078 5.759   13.510  1.00 11.90 ?  86   HIS   A CB   1 
ATOM   1823 C  CG   . HIS   A 1 86  ? 30.118 5.867   12.459  1.00 11.75 ?  86   HIS   A CG   1 
ATOM   1824 N  ND1  . HIS   A 1 86  ? 31.207 6.704   12.582  1.00 12.86 ?  86   HIS   A ND1  1 
ATOM   1825 C  CD2  . HIS   A 1 86  ? 30.294 5.176   11.311  1.00 11.68 ?  86   HIS   A CD2  1 
ATOM   1826 C  CE1  . HIS   A 1 86  ? 31.992 6.539   11.533  1.00 12.70 ?  86   HIS   A CE1  1 
ATOM   1827 N  NE2  . HIS   A 1 86  ? 31.466 5.614   10.753  1.00 12.11 ?  86   HIS   A NE2  1 
ATOM   1828 H  H    . HIS   A 1 86  ? 30.522 3.224   14.008  1.00 13.74 ?  86   HIS   A H    1 
ATOM   1829 H  HA   . HIS   A 1 86  ? 30.317 5.092   14.971  1.00 14.25 ?  86   HIS   A HA   1 
ATOM   1830 H  HB2  . HIS   A 1 86  ? 28.254 5.465   13.093  1.00 14.31 ?  86   HIS   A HB2  1 
ATOM   1831 H  HB3  . HIS   A 1 86  ? 28.954 6.645   13.898  1.00 14.31 ?  86   HIS   A HB3  1 
ATOM   1832 H  HD2  . HIS   A 1 86  ? 29.730 4.515   10.968  1.00 14.05 ?  86   HIS   A HD2  1 
ATOM   1833 H  HE1  . HIS   A 1 86  ? 32.781 7.000   11.355  1.00 15.27 ?  86   HIS   A HE1  1 
ATOM   1834 H  HE2  . HIS   A 1 86  ? 31.795 5.338   9.998   1.00 14.56 ?  86   HIS   A HE2  1 
ATOM   1835 N  N    . ASN   A 1 87  ? 27.495 5.501   15.860  1.00 13.55 ?  87   ASN   A N    1 
ATOM   1836 C  CA   . ASN   A 1 87  ? 26.516 5.489   16.931  1.00 14.64 ?  87   ASN   A CA   1 
ATOM   1837 C  C    . ASN   A 1 87  ? 25.395 4.487   16.699  1.00 15.42 ?  87   ASN   A C    1 
ATOM   1838 O  O    . ASN   A 1 87  ? 24.487 4.409   17.531  1.00 17.71 ?  87   ASN   A O    1 
ATOM   1839 C  CB   . ASN   A 1 87  ? 25.914 6.892   17.094  1.00 15.37 ?  87   ASN   A CB   1 
ATOM   1840 C  CG   . ASN   A 1 87  ? 25.383 7.467   15.783  1.00 16.16 ?  87   ASN   A CG   1 
ATOM   1841 O  OD1  . ASN   A 1 87  ? 26.014 7.360   14.734  1.00 16.68 ?  87   ASN   A OD1  1 
ATOM   1842 N  ND2  . ASN   A 1 87  ? 24.219 8.086   15.848  1.00 17.20 ?  87   ASN   A ND2  1 
ATOM   1843 H  H    . ASN   A 1 87  ? 27.350 6.116   15.286  1.00 16.29 ?  87   ASN   A H    1 
ATOM   1844 H  HA   . ASN   A 1 87  ? 26.955 5.247   17.764  1.00 17.59 ?  87   ASN   A HA   1 
ATOM   1845 H  HB2  . ASN   A 1 87  ? 25.175 6.840   17.729  1.00 18.47 ?  87   ASN   A HB2  1 
ATOM   1846 H  HB3  . ASN   A 1 87  ? 26.597 7.485   17.431  1.00 18.47 ?  87   ASN   A HB3  1 
ATOM   1847 H  HD21 . ASN   A 1 87  ? 23.876 8.427   15.140  1.00 20.67 ?  87   ASN   A HD21 1 
ATOM   1848 H  HD22 . ASN   A 1 87  ? 23.805 8.152   16.602  1.00 20.67 ?  87   ASN   A HD22 1 
ATOM   1849 N  N    . LEU   A 1 88  ? 25.441 3.715   15.614  1.00 14.71 ?  88   LEU   A N    1 
ATOM   1850 C  CA   . LEU   A 1 88  ? 24.329 2.851   15.235  1.00 14.69 ?  88   LEU   A CA   1 
ATOM   1851 C  C    . LEU   A 1 88  ? 24.555 1.375   15.532  1.00 14.48 ?  88   LEU   A C    1 
ATOM   1852 O  O    . LEU   A 1 88  ? 23.583 0.639   15.718  1.00 15.40 ?  88   LEU   A O    1 
ATOM   1853 C  CB   . LEU   A 1 88  ? 24.053 3.008   13.738  1.00 15.28 ?  88   LEU   A CB   1 
ATOM   1854 C  CG   . LEU   A 1 88  ? 23.746 4.431   13.271  1.00 16.79 ?  88   LEU   A CG   1 
ATOM   1855 C  CD1  . LEU   A 1 88  ? 23.536 4.450   11.770  1.00 17.11 ?  88   LEU   A CD1  1 
ATOM   1856 C  CD2  . LEU   A 1 88  ? 22.526 4.991   13.996  1.00 18.49 ?  88   LEU   A CD2  1 
ATOM   1857 H  H    . LEU   A 1 88  ? 26.115 3.671   15.080  1.00 17.68 ?  88   LEU   A H    1 
ATOM   1858 H  HA   . LEU   A 1 88  ? 23.536 3.129   15.717  1.00 17.65 ?  88   LEU   A HA   1 
ATOM   1859 H  HB2  . LEU   A 1 88  ? 24.828 2.705   13.244  1.00 18.36 ?  88   LEU   A HB2  1 
ATOM   1860 H  HB3  . LEU   A 1 88  ? 23.286 2.460   13.505  1.00 18.36 ?  88   LEU   A HB3  1 
ATOM   1861 H  HG   . LEU   A 1 88  ? 24.503 5.002   13.473  1.00 20.18 ?  88   LEU   A HG   1 
ATOM   1862 H  HD11 . LEU   A 1 88  ? 23.346 5.360   11.488  1.00 20.56 ?  88   LEU   A HD11 1 
ATOM   1863 H  HD12 . LEU   A 1 88  ? 24.342 4.132   11.334  1.00 20.56 ?  88   LEU   A HD12 1 
ATOM   1864 H  HD13 . LEU   A 1 88  ? 22.789 3.873   11.548  1.00 20.56 ?  88   LEU   A HD13 1 
ATOM   1865 H  HD21 . LEU   A 1 88  ? 22.278 5.834   13.587  1.00 22.21 ?  88   LEU   A HD21 1 
ATOM   1866 H  HD22 . LEU   A 1 88  ? 21.799 4.357   13.920  1.00 22.21 ?  88   LEU   A HD22 1 
ATOM   1867 H  HD23 . LEU   A 1 88  ? 22.753 5.129   14.929  1.00 22.21 ?  88   LEU   A HD23 1 
ATOM   1868 N  N    . ALA   A 1 89  ? 25.806 0.929   15.564  1.00 13.74 ?  89   ALA   A N    1 
ATOM   1869 C  CA   . ALA   A 1 89  ? 26.154 -0.483  15.649  1.00 13.11 ?  89   ALA   A CA   1 
ATOM   1870 C  C    . ALA   A 1 89  ? 27.642 -0.544  15.954  1.00 13.49 ?  89   ALA   A C    1 
ATOM   1871 O  O    . ALA   A 1 89  ? 28.350 0.456   15.833  1.00 14.30 ?  89   ALA   A O    1 
ATOM   1872 C  CB   . ALA   A 1 89  ? 25.865 -1.186  14.324  1.00 12.62 ?  89   ALA   A CB   1 
ATOM   1873 H  H    . ALA   A 1 89  ? 26.492 1.442   15.536  1.00 16.52 ?  89   ALA   A H    1 
ATOM   1874 H  HA   . ALA   A 1 89  ? 25.660 -0.917  16.364  1.00 15.76 ?  89   ALA   A HA   1 
ATOM   1875 H  HB1  . ALA   A 1 89  ? 26.126 -2.121  14.392  1.00 15.17 ?  89   ALA   A HB1  1 
ATOM   1876 H  HB2  . ALA   A 1 89  ? 24.911 -1.130  14.133  1.00 15.17 ?  89   ALA   A HB2  1 
ATOM   1877 H  HB3  . ALA   A 1 89  ? 26.367 -0.757  13.616  1.00 15.17 ?  89   ALA   A HB3  1 
ATOM   1878 N  N    . LYS   A 1 90  ? 28.131 -1.724  16.330  1.00 14.22 ?  90   LYS   A N    1 
ATOM   1879 C  CA   . LYS   A 1 90  ? 29.577 -1.866  16.465  1.00 14.98 ?  90   LYS   A CA   1 
ATOM   1880 C  C    . LYS   A 1 90  ? 30.261 -1.672  15.115  1.00 13.72 ?  90   LYS   A C    1 
ATOM   1881 O  O    . LYS   A 1 90  ? 31.192 -0.862  14.980  1.00 14.58 ?  90   LYS   A O    1 
ATOM   1882 C  CB   . LYS   A 1 90  ? 29.929 -3.223  17.078  1.00 17.31 ?  90   LYS   A CB   1 
ATOM   1883 C  CG   . LYS   A 1 90  ? 31.403 -3.351  17.423  1.00 21.26 ?  90   LYS   A CG   1 
ATOM   1884 C  CD   . LYS   A 1 90  ? 31.661 -4.567  18.296  1.00 25.70 ?  90   LYS   A CD   1 
ATOM   1885 C  CE   . LYS   A 1 90  ? 33.076 -4.574  18.852  1.00 29.04 ?  90   LYS   A CE   1 
ATOM   1886 N  NZ   . LYS   A 1 90  ? 34.078 -4.999  17.840  1.00 30.83 ?  90   LYS   A NZ   1 
ATOM   1887 H  H    . LYS   A 1 90  ? 27.670 -2.426  16.503  1.00 17.09 ?  90   LYS   A H    1 
ATOM   1888 H  HA   . LYS   A 1 90  ? 29.907 -1.178  17.061  1.00 18.01 ?  90   LYS   A HA   1 
ATOM   1889 H  HB2  . LYS   A 1 90  ? 29.417 -3.341  17.896  1.00 20.80 ?  90   LYS   A HB2  1 
ATOM   1890 H  HB3  . LYS   A 1 90  ? 29.706 -3.925  16.446  1.00 20.80 ?  90   LYS   A HB3  1 
ATOM   1891 H  HG2  . LYS   A 1 90  ? 31.918 -3.446  16.607  1.00 25.54 ?  90   LYS   A HG2  1 
ATOM   1892 H  HG3  . LYS   A 1 90  ? 31.688 -2.561  17.911  1.00 25.54 ?  90   LYS   A HG3  1 
ATOM   1893 H  HD2  . LYS   A 1 90  ? 31.041 -4.564  19.043  1.00 30.87 ?  90   LYS   A HD2  1 
ATOM   1894 H  HD3  . LYS   A 1 90  ? 31.540 -5.372  17.766  1.00 30.87 ?  90   LYS   A HD3  1 
ATOM   1895 H  HE2  . LYS   A 1 90  ? 33.306 -3.677  19.144  1.00 34.88 ?  90   LYS   A HE2  1 
ATOM   1896 H  HE3  . LYS   A 1 90  ? 33.122 -5.189  19.600  1.00 34.88 ?  90   LYS   A HE3  1 
ATOM   1897 H  HZ1  . LYS   A 1 90  ? 33.887 -5.819  17.550  1.00 37.02 ?  90   LYS   A HZ1  1 
ATOM   1898 H  HZ2  . LYS   A 1 90  ? 34.070 -4.439  17.149  1.00 37.02 ?  90   LYS   A HZ2  1 
ATOM   1899 H  HZ3  . LYS   A 1 90  ? 34.892 -5.003  18.201  1.00 37.02 ?  90   LYS   A HZ3  1 
ATOM   1900 N  N    . HIS   A 1 91  ? 29.788 -2.393  14.099  1.00 12.00 ?  91   HIS   A N    1 
ATOM   1901 C  CA   . HIS   A 1 91  ? 30.352 -2.375  12.762  1.00 11.74 ?  91   HIS   A CA   1 
ATOM   1902 C  C    . HIS   A 1 91  ? 29.253 -2.102  11.752  1.00 10.76 ?  91   HIS   A C    1 
ATOM   1903 O  O    . HIS   A 1 91  ? 28.090 -2.471  11.956  1.00 11.22 ?  91   HIS   A O    1 
ATOM   1904 C  CB   . HIS   A 1 91  ? 30.944 -3.745  12.396  1.00 14.06 ?  91   HIS   A CB   1 
ATOM   1905 C  CG   . HIS   A 1 91  ? 31.929 -4.272  13.390  1.00 18.13 ?  91   HIS   A CG   1 
ATOM   1906 N  ND1  . HIS   A 1 91  ? 33.205 -3.769  13.511  1.00 20.16 ?  91   HIS   A ND1  1 
ATOM   1907 C  CD2  . HIS   A 1 91  ? 31.829 -5.270  14.299  1.00 19.91 ?  91   HIS   A CD2  1 
ATOM   1908 C  CE1  . HIS   A 1 91  ? 33.849 -4.431  14.458  1.00 20.85 ?  91   HIS   A CE1  1 
ATOM   1909 N  NE2  . HIS   A 1 91  ? 33.035 -5.347  14.952  1.00 21.29 ?  91   HIS   A NE2  1 
ATOM   1910 H  H    . HIS   A 1 91  ? 29.115 -2.935  14.174  1.00 14.43 ?  91   HIS   A H    1 
ATOM   1911 H  HA   . HIS   A 1 91  ? 31.038 -1.701  12.691  1.00 14.12 ?  91   HIS   A HA   1 
ATOM   1912 H  HB2  . HIS   A 1 91  ? 30.224 -4.393  12.328  1.00 16.90 ?  91   HIS   A HB2  1 
ATOM   1913 H  HB3  . HIS   A 1 91  ? 31.398 -3.671  11.542  1.00 16.90 ?  91   HIS   A HB3  1 
ATOM   1914 H  HD1  . HIS   A 1 91  ? 33.535 -3.125  13.043  1.00 24.22 ?  91   HIS   A HD1  1 
ATOM   1915 H  HD2  . HIS   A 1 91  ? 31.086 -5.801  14.456  1.00 23.92 ?  91   HIS   A HD2  1 
ATOM   1916 H  HE1  . HIS   A 1 91  ? 34.728 -4.275  14.729  1.00 25.05 ?  91   HIS   A HE1  1 
ATOM   1917 N  N    . CYS   A 1 92  ? 29.645 -1.503  10.630  1.00 10.25 ?  92   CYS   A N    1 
ATOM   1918 C  CA   . CYS   A 1 92  ? 28.796 -1.427  9.451   1.00 10.12 ?  92   CYS   A CA   1 
ATOM   1919 C  C    . CYS   A 1 92  ? 29.432 -2.243  8.336   1.00 9.40  ?  92   CYS   A C    1 
ATOM   1920 O  O    . CYS   A 1 92  ? 30.588 -1.995  7.962   1.00 10.23 ?  92   CYS   A O    1 
ATOM   1921 C  CB   . CYS   A 1 92  ? 28.572 0.013   8.991   1.00 10.45 ?  92   CYS   A CB   1 
ATOM   1922 S  SG   . CYS   A 1 92  ? 27.548 0.123   7.492   1.00 9.90  ?  92   CYS   A SG   1 
ATOM   1923 H  H    . CYS   A 1 92  ? 30.416 -1.129  10.527  1.00 12.33 ?  92   CYS   A H    1 
ATOM   1924 H  HA   . CYS   A 1 92  ? 27.934 -1.815  9.652   1.00 12.17 ?  92   CYS   A HA   1 
ATOM   1925 H  HB2  . CYS   A 1 92  ? 28.125 0.505   9.696   1.00 12.57 ?  92   CYS   A HB2  1 
ATOM   1926 H  HB3  . CYS   A 1 92  ? 29.429 0.421   8.792   1.00 12.57 ?  92   CYS   A HB3  1 
ATOM   1927 H  HG   . CYS   A 1 92  ? 27.403 1.277   7.209   1.00 11.91 ?  92   CYS   A HG   1 
ATOM   1928 N  N    . LEU   A 1 93  ? 28.693 -3.237  7.842   1.00 9.28  ?  93   LEU   A N    1 
ATOM   1929 C  CA   . LEU   A 1 93  ? 29.084 -3.998  6.660   1.00 9.06  ?  93   LEU   A CA   1 
ATOM   1930 C  C    . LEU   A 1 93  ? 28.481 -3.299  5.447   1.00 8.82  ?  93   LEU   A C    1 
ATOM   1931 O  O    . LEU   A 1 93  ? 27.263 -3.358  5.231   1.00 9.04  ?  93   LEU   A O    1 
ATOM   1932 C  CB   . LEU   A 1 93  ? 28.597 -5.441  6.768   1.00 9.75  ?  93   LEU   A CB   1 
ATOM   1933 C  CG   . LEU   A 1 93  ? 28.982 -6.331  5.593   1.00 9.80  ?  93   LEU   A CG   1 
ATOM   1934 C  CD1  . LEU   A 1 93  ? 30.488 -6.576  5.571   1.00 10.94 ?  93   LEU   A CD1  1 
ATOM   1935 C  CD2  . LEU   A 1 93  ? 28.218 -7.658  5.632   1.00 10.71 ?  93   LEU   A CD2  1 
ATOM   1936 H  H    . LEU   A 1 93  ? 27.948 -3.492  8.191   1.00 11.16 ?  93   LEU   A H    1 
ATOM   1937 H  HA   . LEU   A 1 93  ? 30.046 -3.997  6.577   1.00 10.90 ?  93   LEU   A HA   1 
ATOM   1938 H  HB2  . LEU   A 1 93  ? 28.973 -5.837  7.574   1.00 11.72 ?  93   LEU   A HB2  1 
ATOM   1939 H  HB3  . LEU   A 1 93  ? 27.628 -5.442  6.833   1.00 11.72 ?  93   LEU   A HB3  1 
ATOM   1940 H  HG   . LEU   A 1 93  ? 28.747 -5.887  4.770   1.00 11.79 ?  93   LEU   A HG   1 
ATOM   1941 H  HD11 . LEU   A 1 93  ? 30.702 -7.207  4.867   1.00 13.15 ?  93   LEU   A HD11 1 
ATOM   1942 H  HD12 . LEU   A 1 93  ? 30.945 -5.735  5.410   1.00 13.15 ?  93   LEU   A HD12 1 
ATOM   1943 H  HD13 . LEU   A 1 93  ? 30.767 -6.940  6.431   1.00 13.15 ?  93   LEU   A HD13 1 
ATOM   1944 H  HD21 . LEU   A 1 93  ? 28.491 -8.204  4.869   1.00 12.88 ?  93   LEU   A HD21 1 
ATOM   1945 H  HD22 . LEU   A 1 93  ? 28.427 -8.128  6.455   1.00 12.88 ?  93   LEU   A HD22 1 
ATOM   1946 H  HD23 . LEU   A 1 93  ? 27.267 -7.483  5.581   1.00 12.88 ?  93   LEU   A HD23 1 
ATOM   1947 N  N    . HIS   A 1 94  ? 29.325 -2.604  4.685   1.00 8.70  ?  94   HIS   A N    1 
ATOM   1948 C  CA   . HIS   A 1 94  ? 28.892 -1.929  3.466   1.00 8.68  ?  94   HIS   A CA   1 
ATOM   1949 C  C    . HIS   A 1 94  ? 28.886 -2.959  2.351   1.00 8.71  ?  94   HIS   A C    1 
ATOM   1950 O  O    . HIS   A 1 94  ? 29.947 -3.470  1.990   1.00 10.27 ?  94   HIS   A O    1 
ATOM   1951 C  CB   . HIS   A 1 94  ? 29.845 -0.783  3.128   1.00 8.96  ?  94   HIS   A CB   1 
ATOM   1952 C  CG   . HIS   A 1 94  ? 29.837 0.314   4.138   1.00 8.91  ?  94   HIS   A CG   1 
ATOM   1953 N  ND1  . HIS   A 1 94  ? 28.958 1.378   4.087   1.00 8.84  ?  94   HIS   A ND1  1 
ATOM   1954 C  CD2  . HIS   A 1 94  ? 30.579 0.480   5.255   1.00 9.18  ?  94   HIS   A CD2  1 
ATOM   1955 C  CE1  . HIS   A 1 94  ? 29.177 2.156   5.132   1.00 9.11  ?  94   HIS   A CE1  1 
ATOM   1956 N  NE2  . HIS   A 1 94  ? 30.158 1.639   5.851   1.00 9.46  ?  94   HIS   A NE2  1 
ATOM   1957 H  H    . HIS   A 1 94  ? 30.165 -2.507  4.858   1.00 10.47 ?  94   HIS   A H    1 
ATOM   1958 H  HA   . HIS   A 1 94  ? 27.993 -1.583  3.580   1.00 10.45 ?  94   HIS   A HA   1 
ATOM   1959 H  HB2  . HIS   A 1 94  ? 30.742 -1.131  3.067   1.00 10.78 ?  94   HIS   A HB2  1 
ATOM   1960 H  HB3  . HIS   A 1 94  ? 29.575 -0.402  2.275   1.00 10.78 ?  94   HIS   A HB3  1 
ATOM   1961 H  HD2  . HIS   A 1 94  ? 31.255 -0.078  5.560   1.00 11.04 ?  94   HIS   A HD2  1 
ATOM   1962 H  HE1  . HIS   A 1 94  ? 28.714 2.942   5.321   1.00 10.95 ?  94   HIS   A HE1  1 
ATOM   1963 H  HE2  . HIS   A 1 94  ? 30.472 1.980   6.576   1.00 11.38 ?  94   HIS   A HE2  1 
ATOM   1964 N  N    . VAL   A 1 95  ? 27.710 -3.279  1.811   1.00 8.17  ?  95   VAL   A N    1 
ATOM   1965 C  CA   . VAL   A 1 95  ? 27.564 -4.314  0.789   1.00 8.74  ?  95   VAL   A CA   1 
ATOM   1966 C  C    . VAL   A 1 95  ? 27.010 -3.675  -0.470  1.00 8.42  ?  95   VAL   A C    1 
ATOM   1967 O  O    . VAL   A 1 95  ? 26.008 -2.956  -0.408  1.00 9.22  ?  95   VAL   A O    1 
ATOM   1968 C  CB   . VAL   A 1 95  ? 26.638 -5.461  1.245   1.00 9.13  ?  95   VAL   A CB   1 
ATOM   1969 C  CG1  . VAL   A 1 95  ? 26.530 -6.505  0.141   1.00 10.04 ?  95   VAL   A CG1  1 
ATOM   1970 C  CG2  . VAL   A 1 95  ? 27.155 -6.084  2.517   1.00 9.50  ?  95   VAL   A CG2  1 
ATOM   1971 H  H    . VAL   A 1 95  ? 26.962 -2.905  2.026   1.00 9.84  ?  95   VAL   A H    1 
ATOM   1972 H  HA   . VAL   A 1 95  ? 28.427 -4.689  0.581   1.00 10.52 ?  95   VAL   A HA   1 
ATOM   1973 H  HB   . VAL   A 1 95  ? 25.751 -5.118  1.416   1.00 10.98 ?  95   VAL   A HB   1 
ATOM   1974 H  HG11 . VAL   A 1 95  ? 26.142 -7.319  0.505   1.00 12.08 ?  95   VAL   A HG11 1 
ATOM   1975 H  HG12 . VAL   A 1 95  ? 25.970 -6.167  -0.573  1.00 12.08 ?  95   VAL   A HG12 1 
ATOM   1976 H  HG13 . VAL   A 1 95  ? 27.421 -6.701  -0.203  1.00 12.08 ?  95   VAL   A HG13 1 
ATOM   1977 H  HG21 . VAL   A 1 95  ? 26.602 -6.848  2.744   1.00 11.43 ?  95   VAL   A HG21 1 
ATOM   1978 H  HG22 . VAL   A 1 95  ? 28.072 -6.368  2.379   1.00 11.43 ?  95   VAL   A HG22 1 
ATOM   1979 H  HG23 . VAL   A 1 95  ? 27.115 -5.423  3.225   1.00 11.43 ?  95   VAL   A HG23 1 
ATOM   1980 N  N    . VAL   A 1 96  ? 27.633 -3.959  -1.611  1.00 8.64  ?  96   VAL   A N    1 
ATOM   1981 C  CA   . VAL   A 1 96  ? 27.213 -3.404  -2.892  1.00 9.21  ?  96   VAL   A CA   1 
ATOM   1982 C  C    . VAL   A 1 96  ? 26.401 -4.453  -3.644  1.00 9.40  ?  96   VAL   A C    1 
ATOM   1983 O  O    . VAL   A 1 96  ? 26.955 -5.393  -4.223  1.00 10.40 ?  96   VAL   A O    1 
ATOM   1984 C  CB   . VAL   A 1 96  ? 28.401 -2.930  -3.729  1.00 9.66  ?  96   VAL   A CB   1 
ATOM   1985 C  CG1  . VAL   A 1 96  ? 27.892 -2.290  -5.004  1.00 9.77  ?  96   VAL   A CG1  1 
ATOM   1986 C  CG2  . VAL   A 1 96  ? 29.266 -1.951  -2.943  1.00 10.19 ?  96   VAL   A CG2  1 
ATOM   1987 H  H    . VAL   A 1 96  ? 28.325 -4.473  -1.667  1.00 10.39 ?  96   VAL   A H    1 
ATOM   1988 H  HA   . VAL   A 1 96  ? 26.643 -2.638  -2.733  1.00 11.08 ?  96   VAL   A HA   1 
ATOM   1989 H  HB   . VAL   A 1 96  ? 28.950 -3.691  -3.973  1.00 11.62 ?  96   VAL   A HB   1 
ATOM   1990 H  HG11 . VAL   A 1 96  ? 28.636 -1.833  -5.437  1.00 11.76 ?  96   VAL   A HG11 1 
ATOM   1991 H  HG12 . VAL   A 1 96  ? 27.544 -2.974  -5.589  1.00 11.76 ?  96   VAL   A HG12 1 
ATOM   1992 H  HG13 . VAL   A 1 96  ? 27.203 -1.648  -4.781  1.00 11.76 ?  96   VAL   A HG13 1 
ATOM   1993 H  HG21 . VAL   A 1 96  ? 29.970 -1.609  -3.517  1.00 12.25 ?  96   VAL   A HG21 1 
ATOM   1994 H  HG22 . VAL   A 1 96  ? 28.711 -1.214  -2.632  1.00 12.25 ?  96   VAL   A HG22 1 
ATOM   1995 H  HG23 . VAL   A 1 96  ? 29.656 -2.409  -2.181  1.00 12.25 ?  96   VAL   A HG23 1 
ATOM   1996 N  N    . GLY   A 1 97  ? 25.081 -4.296  -3.661  1.00 9.56  ?  97   GLY   A N    1 
ATOM   1997 C  CA   . GLY   A 1 97  ? 24.257 -5.059  -4.564  1.00 10.07 ?  97   GLY   A CA   1 
ATOM   1998 C  C    . GLY   A 1 97  ? 24.250 -4.403  -5.931  1.00 10.13 ?  97   GLY   A C    1 
ATOM   1999 O  O    . GLY   A 1 97  ? 24.530 -3.206  -6.070  1.00 11.30 ?  97   GLY   A O    1 
ATOM   2000 H  H    . GLY   A 1 97  ? 24.641 -3.751  -3.151  1.00 11.50 ?  97   GLY   A H    1 
ATOM   2001 H  HA2  . GLY   A 1 97  ? 24.609 -5.958  -4.627  1.00 12.11 ?  97   GLY   A HA2  1 
ATOM   2002 H  HA3  . GLY   A 1 97  ? 23.345 -5.101  -4.227  1.00 12.11 ?  97   GLY   A HA3  1 
ATOM   2003 N  N    A PRO   A 1 98  ? 23.870 -5.135  -6.972  0.60 10.50 ?  98   PRO   A N    1 
ATOM   2004 N  N    B PRO   A 1 98  ? 23.980 -5.204  -6.964  0.40 10.72 ?  98   PRO   A N    1 
ATOM   2005 C  CA   A PRO   A 1 98  ? 23.729 -4.495  -8.288  0.60 11.23 ?  98   PRO   A CA   1 
ATOM   2006 C  CA   B PRO   A 1 98  ? 23.915 -4.666  -8.324  0.40 11.75 ?  98   PRO   A CA   1 
ATOM   2007 C  C    A PRO   A 1 98  ? 22.628 -3.436  -8.297  0.60 10.94 ?  98   PRO   A C    1 
ATOM   2008 C  C    B PRO   A 1 98  ? 22.782 -3.665  -8.459  0.40 12.24 ?  98   PRO   A C    1 
ATOM   2009 O  O    A PRO   A 1 98  ? 21.557 -3.618  -7.714  0.60 10.74 ?  98   PRO   A O    1 
ATOM   2010 O  O    B PRO   A 1 98  ? 21.704 -3.826  -7.882  0.40 12.55 ?  98   PRO   A O    1 
ATOM   2011 C  CB   A PRO   A 1 98  ? 23.399 -5.669  -9.218  0.60 11.44 ?  98   PRO   A CB   1 
ATOM   2012 C  CB   B PRO   A 1 98  ? 23.664 -5.911  -9.184  0.40 11.57 ?  98   PRO   A CB   1 
ATOM   2013 C  CG   A PRO   A 1 98  ? 22.798 -6.716  -8.319  0.60 11.55 ?  98   PRO   A CG   1 
ATOM   2014 C  CG   B PRO   A 1 98  ? 23.019 -6.893  -8.253  0.40 11.85 ?  98   PRO   A CG   1 
ATOM   2015 C  CD   A PRO   A 1 98  ? 23.535 -6.572  -7.008  0.60 10.85 ?  98   PRO   A CD   1 
ATOM   2016 C  CD   B PRO   A 1 98  ? 23.687 -6.650  -6.929  0.40 10.88 ?  98   PRO   A CD   1 
ATOM   2017 H  HA   A PRO   A 1 98  ? 24.567 -4.097  -8.554  0.60 13.51 ?  98   PRO   A HA   1 
ATOM   2018 H  HA   B PRO   A 1 98  ? 24.758 -4.255  -8.571  0.40 14.12 ?  98   PRO   A HA   1 
ATOM   2019 H  HB2  A PRO   A 1 98  ? 22.758 -5.388  -9.886  0.60 13.76 ?  98   PRO   A HB2  1 
ATOM   2020 H  HB2  B PRO   A 1 98  ? 23.066 -5.686  -9.914  0.40 13.91 ?  98   PRO   A HB2  1 
ATOM   2021 H  HB3  A PRO   A 1 98  ? 24.211 -5.999  -9.630  0.60 13.76 ?  98   PRO   A HB3  1 
ATOM   2022 H  HB3  B PRO   A 1 98  ? 24.504 -6.256  -9.518  0.40 13.91 ?  98   PRO   A HB3  1 
ATOM   2023 H  HG2  A PRO   A 1 98  ? 21.851 -6.547  -8.201  0.60 13.89 ?  98   PRO   A HG2  1 
ATOM   2024 H  HG2  B PRO   A 1 98  ? 22.065 -6.715  -8.198  0.40 14.25 ?  98   PRO   A HG2  1 
ATOM   2025 H  HG3  A PRO   A 1 98  ? 22.945 -7.599  -8.698  0.60 13.89 ?  98   PRO   A HG3  1 
ATOM   2026 H  HG3  B PRO   A 1 98  ? 23.182 -7.797  -8.567  0.40 14.25 ?  98   PRO   A HG3  1 
ATOM   2027 H  HD2  A PRO   A 1 98  ? 22.954 -6.811  -6.264  0.60 13.04 ?  98   PRO   A HD2  1 
ATOM   2028 H  HD2  B PRO   A 1 98  ? 23.079 -6.864  -6.201  0.40 13.09 ?  98   PRO   A HD2  1 
ATOM   2029 H  HD3  A PRO   A 1 98  ? 24.344 -7.109  -7.008  0.60 13.04 ?  98   PRO   A HD3  1 
ATOM   2030 H  HD3  B PRO   A 1 98  ? 24.509 -7.166  -6.865  0.40 13.09 ?  98   PRO   A HD3  1 
ATOM   2031 N  N    A ASN   A 1 99  ? 22.907 -2.312  -8.966  0.60 12.03 ?  99   ASN   A N    1 
ATOM   2032 N  N    B ASN   A 1 99  ? 23.035 -2.622  -9.233  0.40 12.73 ?  99   ASN   A N    1 
ATOM   2033 C  CA   A ASN   A 1 99  ? 21.933 -1.234  -9.163  0.60 12.59 ?  99   ASN   A CA   1 
ATOM   2034 C  CA   B ASN   A 1 99  ? 22.038 -1.599  -9.517  0.40 13.56 ?  99   ASN   A CA   1 
ATOM   2035 C  C    A ASN   A 1 99  ? 21.386 -1.352  -10.585 0.60 13.39 ?  99   ASN   A C    1 
ATOM   2036 C  C    B ASN   A 1 99  ? 21.401 -1.926  -10.861 0.40 14.59 ?  99   ASN   A C    1 
ATOM   2037 O  O    A ASN   A 1 99  ? 22.063 -1.008  -11.560 0.60 14.06 ?  99   ASN   A O    1 
ATOM   2038 O  O    B ASN   A 1 99  ? 22.052 -1.827  -11.906 0.40 14.04 ?  99   ASN   A O    1 
ATOM   2039 C  CB   A ASN   A 1 99  ? 22.575 0.130   -8.914  0.60 12.20 ?  99   ASN   A CB   1 
ATOM   2040 C  CB   B ASN   A 1 99  ? 22.688 -0.221  -9.535  0.40 14.25 ?  99   ASN   A CB   1 
ATOM   2041 C  CG   A ASN   A 1 99  ? 21.560 1.272   -8.927  0.60 12.43 ?  99   ASN   A CG   1 
ATOM   2042 C  CG   B ASN   A 1 99  ? 21.679 0.892   -9.691  0.40 15.25 ?  99   ASN   A CG   1 
ATOM   2043 O  OD1  A ASN   A 1 99  ? 20.578 1.234   -9.671  0.60 12.90 ?  99   ASN   A OD1  1 
ATOM   2044 O  OD1  B ASN   A 1 99  ? 20.749 0.791   -10.489 0.40 15.72 ?  99   ASN   A OD1  1 
ATOM   2045 N  ND2  A ASN   A 1 99  ? 21.801 2.294   -8.109  0.60 12.89 ?  99   ASN   A ND2  1 
ATOM   2046 N  ND2  B ASN   A 1 99  ? 21.846 1.957   -8.915  0.40 15.89 ?  99   ASN   A ND2  1 
ATOM   2047 H  H    A ASN   A 1 99  ? 23.675 -2.146  -9.304  0.60 14.47 ?  99   ASN   A H    1 
ATOM   2048 H  H    B ASN   A 1 99  ? 23.798 -2.475  -9.600  0.40 15.31 ?  99   ASN   A H    1 
ATOM   2049 H  HA   A ASN   A 1 99  ? 21.202 -1.348  -8.528  0.60 15.13 ?  99   ASN   A HA   1 
ATOM   2050 H  HA   B ASN   A 1 99  ? 21.350 -1.615  -8.828  0.40 16.30 ?  99   ASN   A HA   1 
ATOM   2051 H  HB2  A ASN   A 1 99  ? 23.013 0.128   -8.048  0.60 14.67 ?  99   ASN   A HB2  1 
ATOM   2052 H  HB2  B ASN   A 1 99  ? 23.165 -0.083  -8.703  0.40 17.13 ?  99   ASN   A HB2  1 
ATOM   2053 H  HB3  A ASN   A 1 99  ? 23.228 0.299   -9.613  0.60 14.67 ?  99   ASN   A HB3  1 
ATOM   2054 H  HB3  B ASN   A 1 99  ? 23.297 -0.178  -10.284 0.40 17.13 ?  99   ASN   A HB3  1 
ATOM   2055 H  HD21 A ASN   A 1 99  ? 21.259 2.962   -8.085  0.60 15.50 ?  99   ASN   A HD21 1 
ATOM   2056 H  HD21 B ASN   A 1 99  ? 21.294 2.616   -8.958  0.40 19.09 ?  99   ASN   A HD21 1 
ATOM   2057 H  HD22 A ASN   A 1 99  ? 22.497 2.287   -7.607  0.60 15.50 ?  99   ASN   A HD22 1 
ATOM   2058 H  HD22 B ASN   A 1 99  ? 22.506 1.986   -8.364  0.40 19.09 ?  99   ASN   A HD22 1 
ATOM   2059 N  N    A VAL   A 1 100 ? 20.149 -1.851  -10.691 0.60 14.05 ?  100  VAL   A N    1 
ATOM   2060 N  N    B VAL   A 1 100 ? 20.127 -2.317  -10.822 0.40 16.50 ?  100  VAL   A N    1 
ATOM   2061 C  CA   A VAL   A 1 100 ? 19.517 -2.071  -11.989 0.60 15.83 ?  100  VAL   A CA   1 
ATOM   2062 C  CA   B VAL   A 1 100 ? 19.436 -2.762  -12.027 0.40 18.03 ?  100  VAL   A CA   1 
ATOM   2063 C  C    A VAL   A 1 100 ? 19.396 -0.768  -12.763 0.60 16.09 ?  100  VAL   A C    1 
ATOM   2064 C  C    B VAL   A 1 100 ? 19.212 -1.600  -12.988 0.40 18.86 ?  100  VAL   A C    1 
ATOM   2065 O  O    A VAL   A 1 100 ? 19.439 -0.761  -13.999 0.60 16.66 ?  100  VAL   A O    1 
ATOM   2066 O  O    B VAL   A 1 100 ? 19.278 -1.771  -14.212 0.40 18.56 ?  100  VAL   A O    1 
ATOM   2067 C  CB   A VAL   A 1 100 ? 18.151 -2.767  -11.799 0.60 17.31 ?  100  VAL   A CB   1 
ATOM   2068 C  CB   B VAL   A 1 100 ? 18.128 -3.482  -11.644 0.40 18.79 ?  100  VAL   A CB   1 
ATOM   2069 C  CG1  A VAL   A 1 100 ? 17.419 -2.910  -13.129 0.60 18.06 ?  100  VAL   A CG1  1 
ATOM   2070 C  CG1  B VAL   A 1 100 ? 17.285 -3.774  -12.872 0.40 19.31 ?  100  VAL   A CG1  1 
ATOM   2071 C  CG2  A VAL   A 1 100 ? 18.339 -4.130  -11.151 0.60 18.07 ?  100  VAL   A CG2  1 
ATOM   2072 C  CG2  B VAL   A 1 100 ? 18.448 -4.769  -10.897 0.40 19.09 ?  100  VAL   A CG2  1 
ATOM   2073 H  H    A VAL   A 1 100 ? 19.655 -2.084  -10.016 0.60 16.88 ?  100  VAL   A H    1 
ATOM   2074 H  H    B VAL   A 1 100 ? 19.648 -2.347  -10.108 0.40 19.82 ?  100  VAL   A H    1 
ATOM   2075 H  HA   A VAL   A 1 100 ? 20.077 -2.671  -12.504 0.60 19.02 ?  100  VAL   A HA   1 
ATOM   2076 H  HA   B VAL   A 1 100 ? 19.995 -3.406  -12.484 0.40 21.67 ?  100  VAL   A HA   1 
ATOM   2077 H  HB   A VAL   A 1 100 ? 17.599 -2.230  -11.212 0.60 20.80 ?  100  VAL   A HB   1 
ATOM   2078 H  HB   B VAL   A 1 100 ? 17.613 -2.914  -11.050 0.40 22.58 ?  100  VAL   A HB   1 
ATOM   2079 H  HG11 A VAL   A 1 100 ? 16.666 -3.511  -13.012 0.60 21.70 ?  100  VAL   A HG11 1 
ATOM   2080 H  HG11 B VAL   A 1 100 ? 16.600 -4.421  -12.635 0.40 23.20 ?  100  VAL   A HG11 1 
ATOM   2081 H  HG12 A VAL   A 1 100 ? 17.101 -2.038  -13.413 0.60 21.70 ?  100  VAL   A HG12 1 
ATOM   2082 H  HG12 B VAL   A 1 100 ? 16.871 -2.952  -13.174 0.40 23.20 ?  100  VAL   A HG12 1 
ATOM   2083 H  HG13 A VAL   A 1 100 ? 18.030 -3.272  -13.790 0.60 21.70 ?  100  VAL   A HG13 1 
ATOM   2084 H  HG13 B VAL   A 1 100 ? 17.855 -4.138  -13.565 0.40 23.20 ?  100  VAL   A HG13 1 
ATOM   2085 H  HG21 A VAL   A 1 100 ? 17.478 -4.574  -11.092 0.60 21.72 ?  100  VAL   A HG21 1 
ATOM   2086 H  HG21 B VAL   A 1 100 ? 17.620 -5.221  -10.678 0.40 22.93 ?  100  VAL   A HG21 1 
ATOM   2087 H  HG22 A VAL   A 1 100 ? 18.946 -4.658  -11.694 0.60 21.72 ?  100  VAL   A HG22 1 
ATOM   2088 H  HG22 B VAL   A 1 100 ? 18.995 -5.334  -11.465 0.40 22.93 ?  100  VAL   A HG22 1 
ATOM   2089 H  HG23 A VAL   A 1 100 ? 18.710 -4.010  -10.263 0.60 21.72 ?  100  VAL   A HG23 1 
ATOM   2090 H  HG23 B VAL   A 1 100 ? 18.931 -4.550  -10.084 0.40 22.93 ?  100  VAL   A HG23 1 
ATOM   2091 N  N    A ASN   A 1 101 ? 19.231 0.349   -12.063 0.60 17.20 ?  101  ASN   A N    1 
ATOM   2092 N  N    B ASN   A 1 101 ? 18.947 -0.401  -12.462 0.40 19.98 ?  101  ASN   A N    1 
ATOM   2093 C  CA   A ASN   A 1 101 ? 19.186 1.633   -12.747 0.60 18.78 ?  101  ASN   A CA   1 
ATOM   2094 C  CA   B ASN   A 1 101 ? 18.755 0.752   -13.338 0.40 21.17 ?  101  ASN   A CA   1 
ATOM   2095 C  C    A ASN   A 1 101 ? 20.549 2.064   -13.292 0.60 20.86 ?  101  ASN   A C    1 
ATOM   2096 C  C    B ASN   A 1 101 ? 20.000 1.035   -14.168 0.40 22.32 ?  101  ASN   A C    1 
ATOM   2097 O  O    A ASN   A 1 101 ? 20.635 3.130   -13.914 0.60 22.59 ?  101  ASN   A O    1 
ATOM   2098 O  O    B ASN   A 1 101 ? 19.902 1.613   -15.257 0.40 22.43 ?  101  ASN   A O    1 
ATOM   2099 C  CB   A ASN   A 1 101 ? 18.553 2.670   -11.819 0.60 18.68 ?  101  ASN   A CB   1 
ATOM   2100 C  CB   B ASN   A 1 101 ? 18.374 1.989   -12.524 0.40 21.19 ?  101  ASN   A CB   1 
ATOM   2101 C  CG   A ASN   A 1 101 ? 17.184 2.221   -11.315 0.60 18.69 ?  101  ASN   A CG   1 
ATOM   2102 C  CG   B ASN   A 1 101 ? 17.206 1.739   -11.591 0.40 21.49 ?  101  ASN   A CG   1 
ATOM   2103 O  OD1  A ASN   A 1 101 ? 16.382 1.672   -12.073 0.60 19.57 ?  101  ASN   A OD1  1 
ATOM   2104 O  OD1  B ASN   A 1 101 ? 16.088 1.469   -12.031 0.40 21.46 ?  101  ASN   A OD1  1 
ATOM   2105 N  ND2  A ASN   A 1 101 ? 16.925 2.425   -10.033 0.60 18.29 ?  101  ASN   A ND2  1 
ATOM   2106 N  ND2  B ASN   A 1 101 ? 17.456 1.842   -10.293 0.40 21.83 ?  101  ASN   A ND2  1 
ATOM   2107 H  H    A ASN   A 1 101 ? 19.138 0.390   -11.209 0.60 20.67 ?  101  ASN   A H    1 
ATOM   2108 H  H    B ASN   A 1 101 ? 18.869 -0.232  -11.622 0.40 24.01 ?  101  ASN   A H    1 
ATOM   2109 H  HA   A ASN   A 1 101 ? 18.603 1.542   -13.510 0.60 22.56 ?  101  ASN   A HA   1 
ATOM   2110 H  HA   B ASN   A 1 101 ? 18.030 0.567   -13.952 0.40 25.43 ?  101  ASN   A HA   1 
ATOM   2111 H  HB2  A ASN   A 1 101 ? 19.132 2.813   -11.054 0.60 22.45 ?  101  ASN   A HB2  1 
ATOM   2112 H  HB2  B ASN   A 1 101 ? 19.132 2.264   -11.986 0.40 25.45 ?  101  ASN   A HB2  1 
ATOM   2113 H  HB3  A ASN   A 1 101 ? 18.444 3.505   -12.310 0.60 22.45 ?  101  ASN   A HB3  1 
ATOM   2114 H  HB3  B ASN   A 1 101 ? 18.124 2.705   -13.133 0.40 25.45 ?  101  ASN   A HB3  1 
ATOM   2115 H  HD21 A ASN   A 1 101 ? 16.166 2.186   -9.711  0.60 21.97 ?  101  ASN   A HD21 1 
ATOM   2116 H  HD21 B ASN   A 1 101 ? 16.826 1.709   -9.724  0.40 26.22 ?  101  ASN   A HD21 1 
ATOM   2117 H  HD22 A ASN   A 1 101 ? 17.508 2.806   -9.531  0.60 21.97 ?  101  ASN   A HD22 1 
ATOM   2118 H  HD22 B ASN   A 1 101 ? 18.250 2.027   -10.024 0.40 26.22 ?  101  ASN   A HD22 1 
ATOM   2119 N  N    A LYS   A 1 102 ? 21.594 1.250   -13.098 0.60 22.15 ?  102  LYS   A N    1 
ATOM   2120 N  N    B LYS   A 1 102 ? 21.171 0.645   -13.673 0.40 23.45 ?  102  LYS   A N    1 
ATOM   2121 C  CA   A LYS   A 1 102 ? 22.890 1.431   -13.743 0.60 23.68 ?  102  LYS   A CA   1 
ATOM   2122 C  CA   B LYS   A 1 102 ? 22.423 0.795   -14.396 0.40 24.04 ?  102  LYS   A CA   1 
ATOM   2123 C  C    A LYS   A 1 102 ? 23.203 0.345   -14.762 0.60 23.92 ?  102  LYS   A C    1 
ATOM   2124 C  C    B LYS   A 1 102 ? 22.785 -0.454  -15.190 0.40 23.19 ?  102  LYS   A C    1 
ATOM   2125 O  O    A LYS   A 1 102 ? 24.280 0.379   -15.365 0.60 24.46 ?  102  LYS   A O    1 
ATOM   2126 O  O    B LYS   A 1 102 ? 23.917 -0.561  -15.675 0.40 22.90 ?  102  LYS   A O    1 
ATOM   2127 C  CB   A LYS   A 1 102 ? 24.015 1.450   -12.700 0.60 25.11 ?  102  LYS   A CB   1 
ATOM   2128 C  CB   B LYS   A 1 102 ? 23.552 1.143   -13.422 0.40 25.71 ?  102  LYS   A CB   1 
ATOM   2129 C  CG   A LYS   A 1 102 ? 23.959 2.597   -11.715 0.60 26.57 ?  102  LYS   A CG   1 
ATOM   2130 C  CG   B LYS   A 1 102 ? 23.297 2.408   -12.616 0.40 27.25 ?  102  LYS   A CG   1 
ATOM   2131 C  CD   A LYS   A 1 102 ? 25.127 2.520   -10.739 0.60 27.75 ?  102  LYS   A CD   1 
ATOM   2132 C  CD   B LYS   A 1 102 ? 24.254 2.527   -11.441 0.40 28.73 ?  102  LYS   A CD   1 
ATOM   2133 C  CE   A LYS   A 1 102 ? 25.108 3.667   -9.744  0.60 28.83 ?  102  LYS   A CE   1 
ATOM   2134 C  CE   B LYS   A 1 102 ? 23.986 3.792   -10.639 0.40 29.86 ?  102  LYS   A CE   1 
ATOM   2135 N  NZ   A LYS   A 1 102 ? 26.186 3.536   -8.721  0.60 29.22 ?  102  LYS   A NZ   1 
ATOM   2136 N  NZ   B LYS   A 1 102 ? 24.749 3.826   -9.359  0.40 30.46 ?  102  LYS   A NZ   1 
ATOM   2137 H  H    A LYS   A 1 102 ? 21.574 0.556   -12.586 0.60 26.61 ?  102  LYS   A H    1 
ATOM   2138 H  H    B LYS   A 1 102 ? 21.266 0.283   -12.901 0.40 28.17 ?  102  LYS   A H    1 
ATOM   2139 H  HA   A LYS   A 1 102 ? 22.897 2.278   -14.207 0.60 28.44 ?  102  LYS   A HA   1 
ATOM   2140 H  HA   B LYS   A 1 102 ? 22.332 1.538   -15.012 0.40 28.88 ?  102  LYS   A HA   1 
ATOM   2141 H  HB2  A LYS   A 1 102 ? 23.979 0.624   -12.192 0.60 30.16 ?  102  LYS   A HB2  1 
ATOM   2142 H  HB2  B LYS   A 1 102 ? 23.662 0.410   -12.798 0.40 30.88 ?  102  LYS   A HB2  1 
ATOM   2143 H  HB3  A LYS   A 1 102 ? 24.866 1.505   -13.166 0.60 30.16 ?  102  LYS   A HB3  1 
ATOM   2144 H  HB3  B LYS   A 1 102 ? 24.371 1.273   -13.927 0.40 30.88 ?  102  LYS   A HB3  1 
ATOM   2145 H  HG2  A LYS   A 1 102 ? 24.013 3.438   -12.196 0.60 31.91 ?  102  LYS   A HG2  1 
ATOM   2146 H  HG2  B LYS   A 1 102 ? 23.422 3.183   -13.187 0.40 32.73 ?  102  LYS   A HG2  1 
ATOM   2147 H  HG3  A LYS   A 1 102 ? 23.132 2.548   -11.210 0.60 31.91 ?  102  LYS   A HG3  1 
ATOM   2148 H  HG3  B LYS   A 1 102 ? 22.392 2.393   -12.267 0.40 32.73 ?  102  LYS   A HG3  1 
ATOM   2149 H  HD2  A LYS   A 1 102 ? 25.075 1.687   -10.244 0.60 33.33 ?  102  LYS   A HD2  1 
ATOM   2150 H  HD2  B LYS   A 1 102 ? 24.140 1.764   -10.854 0.40 34.50 ?  102  LYS   A HD2  1 
ATOM   2151 H  HD3  A LYS   A 1 102 ? 25.961 2.562   -11.235 0.60 33.33 ?  102  LYS   A HD3  1 
ATOM   2152 H  HD3  B LYS   A 1 102 ? 25.165 2.562   -11.772 0.40 34.50 ?  102  LYS   A HD3  1 
ATOM   2153 H  HE2  A LYS   A 1 102 ? 25.241 4.503   -10.219 0.60 34.62 ?  102  LYS   A HE2  1 
ATOM   2154 H  HE2  B LYS   A 1 102 ? 24.248 4.563   -11.166 0.40 35.86 ?  102  LYS   A HE2  1 
ATOM   2155 H  HE3  A LYS   A 1 102 ? 24.253 3.677   -9.286  0.60 34.62 ?  102  LYS   A HE3  1 
ATOM   2156 H  HE3  B LYS   A 1 102 ? 23.041 3.839   -10.428 0.40 35.86 ?  102  LYS   A HE3  1 
ATOM   2157 H  HZ1  A LYS   A 1 102 ? 26.150 4.219   -8.153  0.60 35.09 ?  102  LYS   A HZ1  1 
ATOM   2158 H  HZ1  B LYS   A 1 102 ? 24.568 4.578   -8.917  0.40 36.58 ?  102  LYS   A HZ1  1 
ATOM   2159 H  HZ2  A LYS   A 1 102 ? 26.082 2.776   -8.269  0.60 35.09 ?  102  LYS   A HZ2  1 
ATOM   2160 H  HZ2  B LYS   A 1 102 ? 24.521 3.131   -8.851  0.40 36.58 ?  102  LYS   A HZ2  1 
ATOM   2161 H  HZ3  A LYS   A 1 102 ? 26.982 3.529   -9.119  0.60 35.09 ?  102  LYS   A HZ3  1 
ATOM   2162 H  HZ3  B LYS   A 1 102 ? 25.622 3.790   -9.523  0.40 36.58 ?  102  LYS   A HZ3  1 
ATOM   2163 N  N    A GLY   A 1 103 ? 22.311 -0.624  -14.959 0.60 24.11 ?  103  GLY   A N    1 
ATOM   2164 N  N    B GLY   A 1 103 ? 21.856 -1.401  -15.318 0.40 22.57 ?  103  GLY   A N    1 
ATOM   2165 C  CA   A GLY   A 1 103 ? 22.568 -1.707  -15.887 0.60 24.17 ?  103  GLY   A CA   1 
ATOM   2166 C  CA   B GLY   A 1 103 ? 22.089 -2.590  -16.114 0.40 21.69 ?  103  GLY   A CA   1 
ATOM   2167 C  C    A GLY   A 1 103 ? 23.438 -2.817  -15.346 0.60 24.24 ?  103  GLY   A C    1 
ATOM   2168 C  C    B GLY   A 1 103 ? 23.044 -3.595  -15.510 0.40 20.70 ?  103  GLY   A C    1 
ATOM   2169 O  O    A GLY   A 1 103 ? 24.047 -3.546  -16.134 0.60 25.13 ?  103  GLY   A O    1 
ATOM   2170 O  O    B GLY   A 1 103 ? 23.545 -4.465  -16.226 0.40 20.64 ?  103  GLY   A O    1 
ATOM   2171 H  H    A GLY   A 1 103 ? 21.552 -0.681  -14.563 0.60 28.96 ?  103  GLY   A H    1 
ATOM   2172 H  H    B GLY   A 1 103 ? 21.077 -1.370  -14.951 0.40 27.11 ?  103  GLY   A H    1 
ATOM   2173 H  HA2  A GLY   A 1 103 ? 21.723 -2.097  -16.169 0.60 29.03 ?  103  GLY   A HA2  1 
ATOM   2174 H  HA2  B GLY   A 1 103 ? 21.238 -3.032  -16.267 0.40 26.05 ?  103  GLY   A HA2  1 
ATOM   2175 H  HA3  A GLY   A 1 103 ? 23.011 -1.357  -16.675 0.60 29.03 ?  103  GLY   A HA3  1 
ATOM   2176 H  HA3  B GLY   A 1 103 ? 22.441 -2.321  -16.978 0.40 26.05 ?  103  GLY   A HA3  1 
ATOM   2177 N  N    A GLU   A 1 104 ? 23.518 -2.972  -14.029 0.60 22.93 ?  104  GLU   A N    1 
ATOM   2178 N  N    B GLU   A 1 104 ? 23.309 -3.511  -14.211 0.40 20.07 ?  104  GLU   A N    1 
ATOM   2179 C  CA   A GLU   A 1 104 ? 24.390 -3.970  -13.429 0.60 21.71 ?  104  GLU   A CA   1 
ATOM   2180 C  CA   B GLU   A 1 104 ? 24.267 -4.411  -13.584 0.40 19.20 ?  104  GLU   A CA   1 
ATOM   2181 C  C    A GLU   A 1 104 ? 23.700 -5.327  -13.336 0.60 22.67 ?  104  GLU   A C    1 
ATOM   2182 C  C    B GLU   A 1 104 ? 23.669 -5.805  -13.399 0.40 18.31 ?  104  GLU   A C    1 
ATOM   2183 O  O    A GLU   A 1 104 ? 22.485 -5.423  -13.142 0.60 23.18 ?  104  GLU   A O    1 
ATOM   2184 O  O    B GLU   A 1 104 ? 22.454 -5.974  -13.268 0.40 18.68 ?  104  GLU   A O    1 
ATOM   2185 C  CB   A GLU   A 1 104 ? 24.877 -3.495  -12.058 0.60 19.89 ?  104  GLU   A CB   1 
ATOM   2186 C  CB   B GLU   A 1 104 ? 24.747 -3.828  -12.253 0.40 19.70 ?  104  GLU   A CB   1 
ATOM   2187 C  CG   A GLU   A 1 104 ? 25.877 -2.357  -12.206 0.60 18.79 ?  104  GLU   A CG   1 
ATOM   2188 C  CG   B GLU   A 1 104 ? 25.486 -2.501  -12.421 0.40 20.89 ?  104  GLU   A CG   1 
ATOM   2189 C  CD   A GLU   A 1 104 ? 26.159 -1.579  -10.941 0.60 17.36 ?  104  GLU   A CD   1 
ATOM   2190 C  CD   B GLU   A 1 104 ? 25.781 -1.796  -11.111 0.40 21.83 ?  104  GLU   A CD   1 
ATOM   2191 O  OE1  A GLU   A 1 104 ? 25.535 -1.844  -9.890  0.60 15.94 ?  104  GLU   A OE1  1 
ATOM   2192 O  OE1  B GLU   A 1 104 ? 25.631 -2.414  -10.040 0.40 22.23 ?  104  GLU   A OE1  1 
ATOM   2193 O  OE2  A GLU   A 1 104 ? 27.015 -0.670  -11.022 0.60 17.64 -1 104  GLU   A OE2  1 
ATOM   2194 O  OE2  B GLU   A 1 104 ? 26.158 -0.607  -11.156 0.40 22.32 -1 104  GLU   A OE2  1 
ATOM   2195 H  H    A GLU   A 1 104 ? 23.077 -2.504  -13.457 0.60 27.54 ?  104  GLU   A H    1 
ATOM   2196 H  H    B GLU   A 1 104 ? 22.954 -2.936  -13.678 0.40 24.11 ?  104  GLU   A H    1 
ATOM   2197 H  HA   A GLU   A 1 104 ? 25.169 -4.078  -13.994 0.60 26.08 ?  104  GLU   A HA   1 
ATOM   2198 H  HA   B GLU   A 1 104 ? 25.038 -4.492  -14.168 0.40 23.06 ?  104  GLU   A HA   1 
ATOM   2199 H  HB2  A GLU   A 1 104 ? 24.122 -3.178  -11.541 0.60 23.89 ?  104  GLU   A HB2  1 
ATOM   2200 H  HB2  B GLU   A 1 104 ? 23.981 -3.674  -11.682 0.40 23.67 ?  104  GLU   A HB2  1 
ATOM   2201 H  HB3  A GLU   A 1 104 ? 25.315 -4.231  -11.601 0.60 23.89 ?  104  GLU   A HB3  1 
ATOM   2202 H  HB3  B GLU   A 1 104 ? 25.354 -4.459  -11.838 0.40 23.67 ?  104  GLU   A HB3  1 
ATOM   2203 H  HG2  A GLU   A 1 104 ? 26.719 -2.721  -12.515 0.60 22.57 ?  104  GLU   A HG2  1 
ATOM   2204 H  HG2  B GLU   A 1 104 ? 26.330 -2.666  -12.873 0.40 25.10 ?  104  GLU   A HG2  1 
ATOM   2205 H  HG3  A GLU   A 1 104 ? 25.534 -1.724  -12.854 0.60 22.57 ?  104  GLU   A HG3  1 
ATOM   2206 H  HG3  B GLU   A 1 104 ? 24.942 -1.900  -12.952 0.40 25.10 ?  104  GLU   A HG3  1 
ATOM   2207 N  N    A ASP   A 1 105 ? 24.502 -6.378  -13.485 0.60 23.72 ?  105  ASP   A N    1 
ATOM   2208 N  N    B ASP   A 1 105 ? 24.552 -6.805  -13.382 0.40 17.73 ?  105  ASP   A N    1 
ATOM   2209 C  CA   A ASP   A 1 105 ? 23.987 -7.736  -13.586 0.60 24.80 ?  105  ASP   A CA   1 
ATOM   2210 C  CA   B ASP   A 1 105 ? 24.162 -8.211  -13.468 0.40 17.73 ?  105  ASP   A CA   1 
ATOM   2211 C  C    A ASP   A 1 105 ? 23.287 -8.138  -12.295 0.60 23.23 ?  105  ASP   A C    1 
ATOM   2212 C  C    B ASP   A 1 105 ? 23.422 -8.647  -12.206 0.40 16.44 ?  105  ASP   A C    1 
ATOM   2213 O  O    A ASP   A 1 105 ? 23.907 -8.170  -11.229 0.60 21.84 ?  105  ASP   A O    1 
ATOM   2214 O  O    B ASP   A 1 105 ? 24.002 -8.677  -11.118 0.40 14.80 ?  105  ASP   A O    1 
ATOM   2215 C  CB   A ASP   A 1 105 ? 25.149 -8.686  -13.874 0.60 27.27 ?  105  ASP   A CB   1 
ATOM   2216 C  CB   B ASP   A 1 105 ? 25.424 -9.051  -13.664 0.40 19.15 ?  105  ASP   A CB   1 
ATOM   2217 C  CG   A ASP   A 1 105 ? 24.681 -10.080 -14.227 0.60 29.45 ?  105  ASP   A CG   1 
ATOM   2218 C  CG   B ASP   A 1 105 ? 25.144 -10.537 -13.759 0.40 20.29 ?  105  ASP   A CG   1 
ATOM   2219 O  OD1  A ASP   A 1 105 ? 23.452 -10.288 -14.293 0.60 29.92 ?  105  ASP   A OD1  1 
ATOM   2220 O  OD1  B ASP   A 1 105 ? 23.961 -10.925 -13.855 0.40 20.40 ?  105  ASP   A OD1  1 
ATOM   2221 O  OD2  A ASP   A 1 105 ? 25.538 -10.962 -14.451 0.60 30.58 -1 105  ASP   A OD2  1 
ATOM   2222 O  OD2  B ASP   A 1 105 ? 26.123 -11.319 -13.732 0.40 21.08 -1 105  ASP   A OD2  1 
ATOM   2223 H  H    A ASP   A 1 105 ? 25.360 -6.332  -13.527 0.60 28.49 ?  105  ASP   A H    1 
ATOM   2224 H  H    B ASP   A 1 105 ? 25.401 -6.686  -13.318 0.40 21.30 ?  105  ASP   A H    1 
ATOM   2225 H  HA   A ASP   A 1 105 ? 23.355 -7.802  -14.317 0.60 29.79 ?  105  ASP   A HA   1 
ATOM   2226 H  HA   B ASP   A 1 105 ? 23.578 -8.341  -14.229 0.40 21.30 ?  105  ASP   A HA   1 
ATOM   2227 H  HB2  A ASP   A 1 105 ? 25.657 -8.354  -14.633 0.60 32.75 ?  105  ASP   A HB2  1 
ATOM   2228 H  HB2  B ASP   A 1 105 ? 25.865 -8.766  -14.482 0.40 23.01 ?  105  ASP   A HB2  1 
ATOM   2229 H  HB3  A ASP   A 1 105 ? 25.728 -8.732  -13.091 0.60 32.75 ?  105  ASP   A HB3  1 
ATOM   2230 H  HB3  B ASP   A 1 105 ? 26.012 -8.921  -12.908 0.40 23.01 ?  105  ASP   A HB3  1 
ATOM   2231 N  N    A ILE   A 1 106 ? 21.995 -8.464  -12.394 0.60 22.86 ?  106  ILE   A N    1 
ATOM   2232 N  N    B ILE   A 1 106 ? 22.147 -9.015  -12.357 0.40 17.00 ?  106  ILE   A N    1 
ATOM   2233 C  CA   A ILE   A 1 106 ? 21.236 -8.867  -11.217 0.60 21.96 ?  106  ILE   A CA   1 
ATOM   2234 C  CA   B ILE   A 1 106 ? 21.339 -9.406  -11.203 0.40 17.55 ?  106  ILE   A CA   1 
ATOM   2235 C  C    A ILE   A 1 106 ? 21.757 -10.172 -10.637 0.60 20.63 ?  106  ILE   A C    1 
ATOM   2236 C  C    B ILE   A 1 106 ? 21.908 -10.642 -10.518 0.40 17.64 ?  106  ILE   A C    1 
ATOM   2237 O  O    A ILE   A 1 106 ? 21.533 -10.454 -9.456  0.60 19.89 ?  106  ILE   A O    1 
ATOM   2238 O  O    B ILE   A 1 106 ? 21.709 -10.834 -9.311  0.40 17.75 ?  106  ILE   A O    1 
ATOM   2239 C  CB   A ILE   A 1 106 ? 19.730 -8.954  -11.541 0.60 23.37 ?  106  ILE   A CB   1 
ATOM   2240 C  CB   B ILE   A 1 106 ? 19.861 -9.589  -11.612 0.40 18.72 ?  106  ILE   A CB   1 
ATOM   2241 C  CG1  A ILE   A 1 106 ? 18.900 -9.078  -10.259 0.60 23.94 ?  106  ILE   A CG1  1 
ATOM   2242 C  CG1  B ILE   A 1 106 ? 18.960 -9.695  -10.378 0.40 18.92 ?  106  ILE   A CG1  1 
ATOM   2243 C  CG2  A ILE   A 1 106 ? 19.445 -10.139 -12.457 0.60 23.84 ?  106  ILE   A CG2  1 
ATOM   2244 C  CG2  B ILE   A 1 106 ? 19.688 -10.828 -12.468 0.40 19.22 ?  106  ILE   A CG2  1 
ATOM   2245 C  CD1  A ILE   A 1 106 ? 19.087 -7.930  -9.289  0.60 24.21 ?  106  ILE   A CD1  1 
ATOM   2246 C  CD1  B ILE   A 1 106 ? 18.936 -8.449  -9.525  0.40 18.91 ?  106  ILE   A CD1  1 
ATOM   2247 H  H    A ILE   A 1 106 ? 21.549 -8.467  -13.124 0.60 27.46 ?  106  ILE   A H    1 
ATOM   2248 H  H    B ILE   A 1 106 ? 21.735 -9.041  -13.105 0.40 20.43 ?  106  ILE   A H    1 
ATOM   2249 H  HA   A ILE   A 1 106 ? 21.352 -8.189  -10.542 0.60 26.38 ?  106  ILE   A HA   1 
ATOM   2250 H  HA   B ILE   A 1 106 ? 21.375 -8.694  -10.555 0.40 21.08 ?  106  ILE   A HA   1 
ATOM   2251 H  HB   A ILE   A 1 106 ? 19.463 -8.145  -12.003 0.60 28.07 ?  106  ILE   A HB   1 
ATOM   2252 H  HB   B ILE   A 1 106 ? 19.586 -8.815  -12.128 0.40 22.49 ?  106  ILE   A HB   1 
ATOM   2253 H  HG12 A ILE   A 1 106 ? 17.959 -9.110  -10.498 0.60 28.75 ?  106  ILE   A HG12 1 
ATOM   2254 H  HG12 B ILE   A 1 106 ? 18.051 -9.872  -10.668 0.40 22.73 ?  106  ILE   A HG12 1 
ATOM   2255 H  HG13 A ILE   A 1 106 ? 19.147 -9.897  -9.803  0.60 28.75 ?  106  ILE   A HG13 1 
ATOM   2256 H  HG13 B ILE   A 1 106 ? 19.273 -10.424 -9.822  0.40 22.73 ?  106  ILE   A HG13 1 
ATOM   2257 H  HG21 A ILE   A 1 106 ? 18.547 -10.056 -12.814 0.60 28.64 ?  106  ILE   A HG21 1 
ATOM   2258 H  HG21 B ILE   A 1 106 ? 18.808 -10.807 -12.875 0.40 23.10 ?  106  ILE   A HG21 1 
ATOM   2259 H  HG22 A ILE   A 1 106 ? 20.090 -10.139 -13.181 0.60 28.64 ?  106  ILE   A HG22 1 
ATOM   2260 H  HG22 B ILE   A 1 106 ? 20.371 -10.833 -13.154 0.40 23.10 ?  106  ILE   A HG22 1 
ATOM   2261 H  HG23 A ILE   A 1 106 ? 19.523 -10.961 -11.947 0.60 28.64 ?  106  ILE   A HG23 1 
ATOM   2262 H  HG23 B ILE   A 1 106 ? 19.774 -11.614 -11.906 0.40 23.10 ?  106  ILE   A HG23 1 
ATOM   2263 H  HD11 A ILE   A 1 106 ? 18.358 -7.935  -8.652  0.60 29.08 ?  106  ILE   A HD11 1 
ATOM   2264 H  HD11 B ILE   A 1 106 ? 18.192 -8.506  -8.907  0.40 22.72 ?  106  ILE   A HD11 1 
ATOM   2265 H  HD12 A ILE   A 1 106 ? 19.933 -8.044  -8.825  0.60 29.08 ?  106  ILE   A HD12 1 
ATOM   2266 H  HD12 B ILE   A 1 106 ? 19.771 -8.387  -9.032  0.40 22.72 ?  106  ILE   A HD12 1 
ATOM   2267 H  HD13 A ILE   A 1 106 ? 19.089 -7.097  -9.785  0.60 29.08 ?  106  ILE   A HD13 1 
ATOM   2268 H  HD13 B ILE   A 1 106 ? 18.832 -7.676  -10.100 0.40 22.72 ?  106  ILE   A HD13 1 
ATOM   2269 N  N    A GLN   A 1 107 ? 22.451 -10.982 -11.444 0.60 21.18 ?  107  GLN   A N    1 
ATOM   2270 N  N    B GLN   A 1 107 ? 22.626 -11.495 -11.258 0.40 17.95 ?  107  GLN   A N    1 
ATOM   2271 C  CA   A GLN   A 1 107 ? 23.054 -12.209 -10.942 0.60 22.35 ?  107  GLN   A CA   1 
ATOM   2272 C  CA   B GLN   A 1 107 ? 23.243 -12.659 -10.632 0.40 19.29 ?  107  GLN   A CA   1 
ATOM   2273 C  C    A GLN   A 1 107 ? 24.038 -11.936 -9.815  0.60 20.12 ?  107  GLN   A C    1 
ATOM   2274 C  C    B GLN   A 1 107 ? 24.246 -12.254 -9.560  0.40 17.46 ?  107  GLN   A C    1 
ATOM   2275 O  O    A GLN   A 1 107 ? 24.281 -12.820 -8.988  0.60 21.59 ?  107  GLN   A O    1 
ATOM   2276 O  O    B GLN   A 1 107 ? 24.518 -13.038 -8.643  0.40 17.44 ?  107  GLN   A O    1 
ATOM   2277 C  CB   A GLN   A 1 107 ? 23.780 -12.942 -12.075 0.60 25.71 ?  107  GLN   A CB   1 
ATOM   2278 C  CB   B GLN   A 1 107 ? 23.901 -13.547 -11.692 0.40 22.41 ?  107  GLN   A CB   1 
ATOM   2279 C  CG   A GLN   A 1 107 ? 22.914 -13.236 -13.289 0.60 29.11 ?  107  GLN   A CG   1 
ATOM   2280 C  CG   B GLN   A 1 107 ? 22.923 -14.071 -12.738 0.40 25.21 ?  107  GLN   A CG   1 
ATOM   2281 C  CD   A GLN   A 1 107 ? 21.670 -14.024 -12.941 0.60 31.84 ?  107  GLN   A CD   1 
ATOM   2282 C  CD   B GLN   A 1 107 ? 21.851 -14.964 -12.143 0.40 27.64 ?  107  GLN   A CD   1 
ATOM   2283 O  OE1  A GLN   A 1 107 ? 21.744 -15.077 -12.309 0.60 33.04 ?  107  GLN   A OE1  1 
ATOM   2284 O  OE1  B GLN   A 1 107 ? 22.080 -15.643 -11.141 0.40 28.35 ?  107  GLN   A OE1  1 
ATOM   2285 N  NE2  A GLN   A 1 107 ? 20.515 -13.513 -13.345 0.60 32.69 ?  107  GLN   A NE2  1 
ATOM   2286 N  NE2  B GLN   A 1 107 ? 20.669 -14.965 -12.756 0.40 28.35 ?  107  GLN   A NE2  1 
ATOM   2287 H  H    A GLN   A 1 107 ? 22.581 -10.841 -12.278 0.60 25.45 ?  107  GLN   A H    1 
ATOM   2288 H  H    B GLN   A 1 107 ? 22.770 -11.422 -12.104 0.40 21.57 ?  107  GLN   A H    1 
ATOM   2289 H  HA   A GLN   A 1 107 ? 22.363 -12.796 -10.599 0.60 26.85 ?  107  GLN   A HA   1 
ATOM   2290 H  HA   B GLN   A 1 107 ? 22.552 -13.184 -10.208 0.40 23.18 ?  107  GLN   A HA   1 
ATOM   2291 H  HB2  A GLN   A 1 107 ? 24.526 -12.397 -12.371 0.60 30.88 ?  107  GLN   A HB2  1 
ATOM   2292 H  HB2  B GLN   A 1 107 ? 24.583 -13.038 -12.154 0.40 26.92 ?  107  GLN   A HB2  1 
ATOM   2293 H  HB3  A GLN   A 1 107 ? 24.111 -13.790 -11.739 0.60 30.88 ?  107  GLN   A HB3  1 
ATOM   2294 H  HB3  B GLN   A 1 107 ? 24.304 -14.316 -11.254 0.40 26.92 ?  107  GLN   A HB3  1 
ATOM   2295 H  HG2  A GLN   A 1 107 ? 22.635 -12.401 -13.691 0.60 34.96 ?  107  GLN   A HG2  1 
ATOM   2296 H  HG2  B GLN   A 1 107 ? 22.484 -13.320 -13.165 0.40 30.28 ?  107  GLN   A HG2  1 
ATOM   2297 H  HG3  A GLN   A 1 107 ? 23.431 -13.755 -13.927 0.60 34.96 ?  107  GLN   A HG3  1 
ATOM   2298 H  HG3  B GLN   A 1 107 ? 23.410 -14.589 -13.397 0.40 30.28 ?  107  GLN   A HG3  1 
ATOM   2299 H  HE21 A GLN   A 1 107 ? 20.504 -12.774 -13.784 0.60 39.25 ?  107  GLN   A HE21 1 
ATOM   2300 H  HE21 B GLN   A 1 107 ? 20.546 -14.477 -13.454 0.40 34.04 ?  107  GLN   A HE21 1 
ATOM   2301 H  HE22 A GLN   A 1 107 ? 19.781 -13.923 -13.171 0.60 39.25 ?  107  GLN   A HE22 1 
ATOM   2302 H  HE22 B GLN   A 1 107 ? 20.027 -15.456 -12.458 0.40 34.04 ?  107  GLN   A HE22 1 
ATOM   2303 N  N    A LEU   A 1 108 ? 24.602 -10.728 -9.754  0.60 16.03 ?  108  LEU   A N    1 
ATOM   2304 N  N    B LEU   A 1 108 ? 24.787 -11.038 -9.644  0.40 16.02 ?  108  LEU   A N    1 
ATOM   2305 C  CA   A LEU   A 1 108 ? 25.557 -10.397 -8.705  0.60 14.10 ?  108  LEU   A CA   1 
ATOM   2306 C  CA   B LEU   A 1 108 ? 25.646 -10.510 -8.595  0.40 14.71 ?  108  LEU   A CA   1 
ATOM   2307 C  C    A LEU   A 1 108 ? 24.898 -10.264 -7.340  0.60 12.48 ?  108  LEU   A C    1 
ATOM   2308 C  C    B LEU   A 1 108 ? 24.904 -10.272 -7.287  0.40 13.18 ?  108  LEU   A C    1 
ATOM   2309 O  O    A LEU   A 1 108 ? 25.606 -10.140 -6.337  0.60 12.49 ?  108  LEU   A O    1 
ATOM   2310 O  O    B LEU   A 1 108 ? 25.561 -10.057 -6.263  0.40 13.41 ?  108  LEU   A O    1 
ATOM   2311 C  CB   A LEU   A 1 108 ? 26.316 -9.120  -9.075  0.60 14.17 ?  108  LEU   A CB   1 
ATOM   2312 C  CB   B LEU   A 1 108 ? 26.329 -9.220  -9.064  0.40 14.90 ?  108  LEU   A CB   1 
ATOM   2313 C  CG   A LEU   A 1 108 ? 27.266 -9.311  -10.260 0.60 15.57 ?  108  LEU   A CG   1 
ATOM   2314 C  CG   B LEU   A 1 108 ? 27.396 -9.416  -10.145 0.40 15.72 ?  108  LEU   A CG   1 
ATOM   2315 C  CD1  A LEU   A 1 108 ? 27.745 -7.975  -10.804 0.60 16.17 ?  108  LEU   A CD1  1 
ATOM   2316 C  CD1  B LEU   A 1 108 ? 27.870 -8.081  -10.697 0.40 16.03 ?  108  LEU   A CD1  1 
ATOM   2317 C  CD2  A LEU   A 1 108 ? 28.453 -10.179 -9.861  0.60 17.15 ?  108  LEU   A CD2  1 
ATOM   2318 C  CD2  B LEU   A 1 108 ? 28.570 -10.209 -9.592  0.40 16.65 ?  108  LEU   A CD2  1 
ATOM   2319 H  H    A LEU   A 1 108 ? 24.441 -10.092 -10.302 0.60 19.27 ?  108  LEU   A H    1 
ATOM   2320 H  H    B LEU   A 1 108 ? 24.675 -10.507 -10.303 0.40 19.25 ?  108  LEU   A H    1 
ATOM   2321 H  HA   A LEU   A 1 108 ? 26.202 -11.115 -8.638  0.60 16.94 ?  108  LEU   A HA   1 
ATOM   2322 H  HA   B LEU   A 1 108 ? 26.340 -11.159 -8.408  0.40 17.68 ?  108  LEU   A HA   1 
ATOM   2323 H  HB2  A LEU   A 1 108 ? 25.675 -8.432  -9.315  0.60 17.04 ?  108  LEU   A HB2  1 
ATOM   2324 H  HB2  B LEU   A 1 108 ? 25.656 -8.622  -9.419  0.40 17.90 ?  108  LEU   A HB2  1 
ATOM   2325 H  HB3  A LEU   A 1 108 ? 26.840 -8.834  -8.313  0.60 17.04 ?  108  LEU   A HB3  1 
ATOM   2326 H  HB3  B LEU   A 1 108 ? 26.762 -8.807  -8.302  0.40 17.90 ?  108  LEU   A HB3  1 
ATOM   2327 H  HG   A LEU   A 1 108 ? 26.792 -9.768  -10.972 0.60 18.71 ?  108  LEU   A HG   1 
ATOM   2328 H  HG   B LEU   A 1 108 ? 27.013 -9.923  -10.878 0.40 18.89 ?  108  LEU   A HG   1 
ATOM   2329 H  HD11 A LEU   A 1 108 ? 28.321 -8.134  -11.569 0.60 19.43 ?  108  LEU   A HD11 1 
ATOM   2330 H  HD11 B LEU   A 1 108 ? 28.506 -8.242  -11.412 0.40 19.27 ?  108  LEU   A HD11 1 
ATOM   2331 H  HD12 A LEU   A 1 108 ? 26.976 -7.450  -11.074 0.60 19.43 ?  108  LEU   A HD12 1 
ATOM   2332 H  HD12 B LEU   A 1 108 ? 27.105 -7.591  -11.040 0.40 19.27 ?  108  LEU   A HD12 1 
ATOM   2333 H  HD13 A LEU   A 1 108 ? 28.238 -7.510  -10.111 0.60 19.43 ?  108  LEU   A HD13 1 
ATOM   2334 H  HD13 B LEU   A 1 108 ? 28.294 -7.576  -9.986  0.40 19.27 ?  108  LEU   A HD13 1 
ATOM   2335 H  HD21 A LEU   A 1 108 ? 29.117 -10.147 -10.566 0.60 20.60 ?  108  LEU   A HD21 1 
ATOM   2336 H  HD21 B LEU   A 1 108 ? 29.309 -10.151 -10.216 0.40 20.01 ?  108  LEU   A HD21 1 
ATOM   2337 H  HD22 A LEU   A 1 108 ? 28.829 -9.837  -9.035  0.60 20.60 ?  108  LEU   A HD22 1 
ATOM   2338 H  HD22 B LEU   A 1 108 ? 28.827 -9.832  -8.736  0.40 20.01 ?  108  LEU   A HD22 1 
ATOM   2339 H  HD23 A LEU   A 1 108 ? 28.149 -11.091 -9.733  0.60 20.60 ?  108  LEU   A HD23 1 
ATOM   2340 H  HD23 B LEU   A 1 108 ? 28.301 -11.133 -9.479  0.40 20.01 ?  108  LEU   A HD23 1 
ATOM   2341 N  N    . LEU   A 1 109 ? 23.568 -10.321 -7.277  1.00 12.27 ?  109  LEU   A N    1 
ATOM   2342 C  CA   . LEU   A 1 109 ? 22.871 -10.196 -6.004  1.00 11.64 ?  109  LEU   A CA   1 
ATOM   2343 C  C    . LEU   A 1 109 ? 23.223 -11.346 -5.068  1.00 10.80 ?  109  LEU   A C    1 
ATOM   2344 O  O    . LEU   A 1 109 ? 23.366 -11.146 -3.856  1.00 11.33 ?  109  LEU   A O    1 
ATOM   2345 C  CB   . LEU   A 1 109 ? 21.365 -10.112 -6.249  1.00 12.10 ?  109  LEU   A CB   1 
ATOM   2346 C  CG   . LEU   A 1 109 ? 20.483 -9.826  -5.038  1.00 12.36 ?  109  LEU   A CG   1 
ATOM   2347 C  CD1  . LEU   A 1 109 ? 20.929 -8.556  -4.327  1.00 12.73 ?  109  LEU   A CD1  1 
ATOM   2348 C  CD2  . LEU   A 1 109 ? 19.028 -9.716  -5.470  1.00 13.52 ?  109  LEU   A CD2  1 
ATOM   2349 H  H    A LEU   A 1 109 ? 23.048 -10.432 -7.951  0.60 14.75 ?  109  LEU   A H    1 
ATOM   2350 H  H    B LEU   A 1 109 ? 23.062 -10.426 -7.963  0.40 14.75 ?  109  LEU   A H    1 
ATOM   2351 H  HA   . LEU   A 1 109 ? 23.153 -9.372  -5.576  1.00 14.00 ?  109  LEU   A HA   1 
ATOM   2352 H  HB2  . LEU   A 1 109 ? 21.205 -9.403  -6.891  1.00 14.54 ?  109  LEU   A HB2  1 
ATOM   2353 H  HB3  . LEU   A 1 109 ? 21.073 -10.956 -6.623  1.00 14.54 ?  109  LEU   A HB3  1 
ATOM   2354 H  HG   . LEU   A 1 109 ? 20.551 -10.564 -4.413  1.00 14.86 ?  109  LEU   A HG   1 
ATOM   2355 H  HD11 . LEU   A 1 109 ? 20.247 -8.289  -3.695  1.00 15.30 ?  109  LEU   A HD11 1 
ATOM   2356 H  HD12 . LEU   A 1 109 ? 21.764 -8.729  -3.866  1.00 15.30 ?  109  LEU   A HD12 1 
ATOM   2357 H  HD13 . LEU   A 1 109 ? 21.057 -7.854  -4.989  1.00 15.30 ?  109  LEU   A HD13 1 
ATOM   2358 H  HD21 . LEU   A 1 109 ? 18.491 -9.424  -4.714  1.00 16.25 ?  109  LEU   A HD21 1 
ATOM   2359 H  HD22 . LEU   A 1 109 ? 18.953 -9.078  -6.194  1.00 16.25 ?  109  LEU   A HD22 1 
ATOM   2360 H  HD23 . LEU   A 1 109 ? 18.715 -10.590 -5.770  1.00 16.25 ?  109  LEU   A HD23 1 
ATOM   2361 N  N    . LYS   A 1 110 ? 23.378 -12.559 -5.605  1.00 10.77 ?  110  LYS   A N    1 
ATOM   2362 C  CA   . LYS   A 1 110 ? 23.759 -13.678 -4.749  1.00 10.64 ?  110  LYS   A CA   1 
ATOM   2363 C  C    . LYS   A 1 110 ? 25.144 -13.454 -4.152  1.00 10.00 ?  110  LYS   A C    1 
ATOM   2364 O  O    . LYS   A 1 110 ? 25.353 -13.656 -2.951  1.00 10.32 ?  110  LYS   A O    1 
ATOM   2365 C  CB   . LYS   A 1 110 ? 23.666 -15.004 -5.510  1.00 11.42 ?  110  LYS   A CB   1 
ATOM   2366 C  CG   . LYS   A 1 110 ? 23.885 -16.217 -4.608  1.00 11.88 ?  110  LYS   A CG   1 
ATOM   2367 C  CD   . LYS   A 1 110 ? 23.641 -17.539 -5.316  1.00 12.42 ?  110  LYS   A CD   1 
ATOM   2368 C  CE   . LYS   A 1 110 ? 23.748 -18.715 -4.364  1.00 13.14 ?  110  LYS   A CE   1 
ATOM   2369 N  NZ   . LYS   A 1 110 ? 22.580 -18.844 -3.458  1.00 13.72 ?  110  LYS   A NZ   1 
ATOM   2370 H  H    . LYS   A 1 110 ? 23.258 -12.758 -6.434  1.00 12.95 ?  110  LYS   A H    1 
ATOM   2371 H  HA   . LYS   A 1 110 ? 23.125 -13.725 -4.010  1.00 12.79 ?  110  LYS   A HA   1 
ATOM   2372 H  HB2  . LYS   A 1 110 ? 22.780 -15.084 -5.903  1.00 13.73 ?  110  LYS   A HB2  1 
ATOM   2373 H  HB3  . LYS   A 1 110 ? 24.340 -15.021 -6.200  1.00 13.73 ?  110  LYS   A HB3  1 
ATOM   2374 H  HG2  . LYS   A 1 110 ? 24.799 -16.213 -4.286  1.00 14.29 ?  110  LYS   A HG2  1 
ATOM   2375 H  HG3  . LYS   A 1 110 ? 23.272 -16.168 -3.853  1.00 14.29 ?  110  LYS   A HG3  1 
ATOM   2376 H  HD2  . LYS   A 1 110 ? 22.753 -17.537 -5.699  1.00 14.94 ?  110  LYS   A HD2  1 
ATOM   2377 H  HD3  . LYS   A 1 110 ? 24.309 -17.653 -6.010  1.00 14.94 ?  110  LYS   A HD3  1 
ATOM   2378 H  HE2  . LYS   A 1 110 ? 23.814 -19.534 -4.876  1.00 15.79 ?  110  LYS   A HE2  1 
ATOM   2379 H  HE3  . LYS   A 1 110 ? 24.537 -18.606 -3.809  1.00 15.79 ?  110  LYS   A HE3  1 
ATOM   2380 H  HZ1  . LYS   A 1 110 ? 22.680 -19.542 -2.919  1.00 16.50 ?  110  LYS   A HZ1  1 
ATOM   2381 H  HZ2  . LYS   A 1 110 ? 22.492 -18.106 -2.963  1.00 16.50 ?  110  LYS   A HZ2  1 
ATOM   2382 H  HZ3  . LYS   A 1 110 ? 21.833 -18.952 -3.937  1.00 16.50 ?  110  LYS   A HZ3  1 
ATOM   2383 N  N    . SER   A 1 111 ? 26.098 -13.016 -4.978  1.00 10.48 ?  111  SER   A N    1 
ATOM   2384 C  CA   . SER   A 1 111 ? 27.432 -12.706 -4.473  1.00 10.64 ?  111  SER   A CA   1 
ATOM   2385 C  C    . SER   A 1 111 ? 27.374 -11.662 -3.362  1.00 10.17 ?  111  SER   A C    1 
ATOM   2386 O  O    . SER   A 1 111 ? 28.077 -11.769 -2.351  1.00 10.64 ?  111  SER   A O    1 
ATOM   2387 C  CB   . SER   A 1 111 ? 28.316 -12.217 -5.621  1.00 11.71 ?  111  SER   A CB   1 
ATOM   2388 O  OG   . SER   A 1 111 ? 28.398 -13.203 -6.635  1.00 13.84 ?  111  SER   A OG   1 
ATOM   2389 H  H    . SER   A 1 111 ? 25.993 -12.895 -5.821  1.00 12.60 ?  111  SER   A H    1 
ATOM   2390 H  HA   . SER   A 1 111 ? 27.827 -13.514 -4.110  1.00 12.80 ?  111  SER   A HA   1 
ATOM   2391 H  HB2  . SER   A 1 111 ? 27.922 -11.413 -5.999  1.00 14.08 ?  111  SER   A HB2  1 
ATOM   2392 H  HB3  . SER   A 1 111 ? 29.199 -12.024 -5.276  1.00 14.08 ?  111  SER   A HB3  1 
ATOM   2393 H  HG   . SER   A 1 111 ? 28.902 -12.923 -7.258  1.00 16.64 ?  111  SER   A HG   1 
ATOM   2394 N  N    . ALA   A 1 112 ? 26.531 -10.641 -3.533  1.00 10.38 ?  112  ALA   A N    1 
ATOM   2395 C  CA   . ALA   A 1 112 ? 26.388 -9.605  -2.514  1.00 10.16 ?  112  ALA   A CA   1 
ATOM   2396 C  C    . ALA   A 1 112 ? 25.913 -10.200 -1.193  1.00 10.02 ?  112  ALA   A C    1 
ATOM   2397 O  O    . ALA   A 1 112 ? 26.471 -9.912  -0.127  1.00 10.38 ?  112  ALA   A O    1 
ATOM   2398 C  CB   . ALA   A 1 112 ? 25.434 -8.511  -3.007  1.00 10.61 ?  112  ALA   A CB   1 
ATOM   2399 H  H    . ALA   A 1 112 ? 26.038 -10.522 -4.224  1.00 12.49 ?  112  ALA   A H    1 
ATOM   2400 H  HA   . ALA   A 1 112 ? 27.250 -9.186  -2.357  1.00 12.22 ?  112  ALA   A HA   1 
ATOM   2401 H  HB1  . ALA   A 1 112 ? 25.371 -7.809  -2.331  1.00 12.76 ?  112  ALA   A HB1  1 
ATOM   2402 H  HB2  . ALA   A 1 112 ? 25.776 -8.134  -3.832  1.00 12.76 ?  112  ALA   A HB2  1 
ATOM   2403 H  HB3  . ALA   A 1 112 ? 24.555 -8.894  -3.158  1.00 12.76 ?  112  ALA   A HB3  1 
ATOM   2404 N  N    . TYR   A 1 113 ? 24.884 -11.049 -1.241  1.00 9.98  ?  113  TYR   A N    1 
ATOM   2405 C  CA   . TYR   A 1 113 ? 24.378 -11.650 -0.010  1.00 9.89  ?  113  TYR   A CA   1 
ATOM   2406 C  C    . TYR   A 1 113 ? 25.384 -12.602 0.634   1.00 9.69  ?  113  TYR   A C    1 
ATOM   2407 O  O    . TYR   A 1 113 ? 25.348 -12.790 1.856   1.00 10.16 ?  113  TYR   A O    1 
ATOM   2408 C  CB   . TYR   A 1 113 ? 23.061 -12.384 -0.273  1.00 10.37 ?  113  TYR   A CB   1 
ATOM   2409 C  CG   . TYR   A 1 113 ? 21.836 -11.495 -0.173  1.00 10.24 ?  113  TYR   A CG   1 
ATOM   2410 C  CD1  . TYR   A 1 113 ? 21.480 -10.902 1.033   1.00 10.56 ?  113  TYR   A CD1  1 
ATOM   2411 C  CD2  . TYR   A 1 113 ? 21.027 -11.258 -1.275  1.00 10.51 ?  113  TYR   A CD2  1 
ATOM   2412 C  CE1  . TYR   A 1 113 ? 20.359 -10.102 1.140   1.00 10.57 ?  113  TYR   A CE1  1 
ATOM   2413 C  CE2  . TYR   A 1 113 ? 19.878 -10.458 -1.173  1.00 10.42 ?  113  TYR   A CE2  1 
ATOM   2414 C  CZ   . TYR   A 1 113 ? 19.563 -9.885  0.035   1.00 10.39 ?  113  TYR   A CZ   1 
ATOM   2415 O  OH   . TYR   A 1 113 ? 18.440 -9.093  0.171   1.00 11.21 ?  113  TYR   A OH   1 
ATOM   2416 H  H    . TYR   A 1 113 ? 24.468 -11.282 -1.956  1.00 12.00 ?  113  TYR   A H    1 
ATOM   2417 H  HA   . TYR   A 1 113 ? 24.199 -10.946 0.629   1.00 11.89 ?  113  TYR   A HA   1 
ATOM   2418 H  HB2  . TYR   A 1 113 ? 23.081 -12.747 -1.172  1.00 12.47 ?  113  TYR   A HB2  1 
ATOM   2419 H  HB3  . TYR   A 1 113 ? 22.962 -13.094 0.372   1.00 12.47 ?  113  TYR   A HB3  1 
ATOM   2420 H  HD1  . TYR   A 1 113 ? 22.014 -11.047 1.783   1.00 12.70 ?  113  TYR   A HD1  1 
ATOM   2421 H  HD2  . TYR   A 1 113 ? 21.233 -11.648 -2.090  1.00 12.64 ?  113  TYR   A HD2  1 
ATOM   2422 H  HE1  . TYR   A 1 113 ? 20.144 -9.718  1.959   1.00 12.71 ?  113  TYR   A HE1  1 
ATOM   2423 H  HE2  . TYR   A 1 113 ? 19.334 -10.301 -1.915  1.00 12.53 ?  113  TYR   A HE2  1 
ATOM   2424 H  HH   . TYR   A 1 113 ? 18.016 -9.073  -0.559  1.00 13.48 ?  113  TYR   A HH   1 
ATOM   2425 N  N    . GLU   A 1 114 ? 26.274 -13.223 -0.156  1.00 10.07 ?  114  GLU   A N    1 
ATOM   2426 C  CA   . GLU   A 1 114 ? 27.273 -14.116 0.429   1.00 10.10 ?  114  GLU   A CA   1 
ATOM   2427 C  C    . GLU   A 1 114 ? 28.130 -13.408 1.473   1.00 10.11 ?  114  GLU   A C    1 
ATOM   2428 O  O    . GLU   A 1 114 ? 28.615 -14.045 2.416   1.00 10.32 ?  114  GLU   A O    1 
ATOM   2429 C  CB   . GLU   A 1 114 ? 28.136 -14.750 -0.669  1.00 10.11 ?  114  GLU   A CB   1 
ATOM   2430 C  CG   . GLU   A 1 114 ? 27.368 -15.806 -1.449  1.00 10.60 ?  114  GLU   A CG   1 
ATOM   2431 C  CD   . GLU   A 1 114 ? 28.071 -16.340 -2.686  1.00 10.96 ?  114  GLU   A CD   1 
ATOM   2432 O  OE1  . GLU   A 1 114 ? 29.019 -15.705 -3.185  1.00 11.33 ?  114  GLU   A OE1  1 
ATOM   2433 O  OE2  . GLU   A 1 114 ? 27.624 -17.401 -3.178  1.00 12.02 -1 114  GLU   A OE2  1 
ATOM   2434 H  H    . GLU   A 1 114 ? 26.315 -13.137 -1.018  1.00 12.11 ?  114  GLU   A H    1 
ATOM   2435 H  HA   . GLU   A 1 114 ? 26.807 -14.835 0.872   1.00 12.15 ?  114  GLU   A HA   1 
ATOM   2436 H  HB2  . GLU   A 1 114 ? 28.419 -14.066 -1.300  1.00 12.15 ?  114  GLU   A HB2  1 
ATOM   2437 H  HB3  . GLU   A 1 114 ? 28.907 -15.177 -0.271  1.00 12.15 ?  114  GLU   A HB3  1 
ATOM   2438 H  HG2  . GLU   A 1 114 ? 27.203 -16.564 -0.865  1.00 12.74 ?  114  GLU   A HG2  1 
ATOM   2439 H  HG3  . GLU   A 1 114 ? 26.519 -15.430 -1.735  1.00 12.74 ?  114  GLU   A HG3  1 
ATOM   2440 N  N    . ASN   A 1 115 ? 28.312 -12.089 1.344   1.00 9.76  ?  115  ASN   A N    1 
ATOM   2441 C  CA   . ASN   A 1 115 ? 29.084 -11.361 2.344   1.00 9.90  ?  115  ASN   A CA   1 
ATOM   2442 C  C    . ASN   A 1 115 ? 28.477 -11.501 3.735   1.00 9.70  ?  115  ASN   A C    1 
ATOM   2443 O  O    . ASN   A 1 115 ? 29.201 -11.430 4.736   1.00 10.25 ?  115  ASN   A O    1 
ATOM   2444 C  CB   . ASN   A 1 115 ? 29.184 -9.879  1.972   1.00 10.27 ?  115  ASN   A CB   1 
ATOM   2445 C  CG   . ASN   A 1 115 ? 29.972 -9.650  0.704   1.00 11.14 ?  115  ASN   A CG   1 
ATOM   2446 O  OD1  . ASN   A 1 115 ? 31.188 -9.743  0.703   1.00 14.54 ?  115  ASN   A OD1  1 
ATOM   2447 N  ND2  . ASN   A 1 115 ? 29.284 -9.357  -0.381  1.00 10.47 ?  115  ASN   A ND2  1 
ATOM   2448 H  H    . ASN   A 1 115 ? 27.999 -11.599 0.705   1.00 11.74 ?  115  ASN   A H    1 
ATOM   2449 H  HA   . ASN   A 1 115 ? 29.980 -11.724 2.375   1.00 11.91 ?  115  ASN   A HA   1 
ATOM   2450 H  HB2  . ASN   A 1 115 ? 28.288 -9.523  1.853   1.00 12.35 ?  115  ASN   A HB2  1 
ATOM   2451 H  HB3  . ASN   A 1 115 ? 29.627 -9.404  2.700   1.00 12.35 ?  115  ASN   A HB3  1 
ATOM   2452 H  HD21 . ASN   A 1 115 ? 29.693 -9.213  -1.118  1.00 12.60 ?  115  ASN   A HD21 1 
ATOM   2453 H  HD22 . ASN   A 1 115 ? 28.422 -9.319  -0.348  1.00 12.60 ?  115  ASN   A HD22 1 
ATOM   2454 N  N    . PHE   A 1 116 ? 27.151 -11.660 3.824   1.00 9.95  ?  116  PHE   A N    1 
ATOM   2455 C  CA   . PHE   A 1 116 ? 26.513 -11.763 5.132   1.00 9.96  ?  116  PHE   A CA   1 
ATOM   2456 C  C    . PHE   A 1 116 ? 26.990 -12.999 5.896   1.00 10.25 ?  116  PHE   A C    1 
ATOM   2457 O  O    . PHE   A 1 116 ? 26.926 -13.017 7.125   1.00 10.92 ?  116  PHE   A O    1 
ATOM   2458 C  CB   . PHE   A 1 116 ? 24.986 -11.892 5.009   1.00 10.06 ?  116  PHE   A CB   1 
ATOM   2459 C  CG   . PHE   A 1 116 ? 24.223 -10.645 4.552   1.00 10.05 ?  116  PHE   A CG   1 
ATOM   2460 C  CD1  . PHE   A 1 116 ? 24.792 -9.616  3.807   1.00 10.04 ?  116  PHE   A CD1  1 
ATOM   2461 C  CD2  . PHE   A 1 116 ? 22.870 -10.545 4.877   1.00 10.63 ?  116  PHE   A CD2  1 
ATOM   2462 C  CE1  . PHE   A 1 116 ? 24.022 -8.537  3.399   1.00 10.31 ?  116  PHE   A CE1  1 
ATOM   2463 C  CE2  . PHE   A 1 116 ? 22.100 -9.475  4.474   1.00 10.95 ?  116  PHE   A CE2  1 
ATOM   2464 C  CZ   . PHE   A 1 116 ? 22.668 -8.466  3.735   1.00 10.24 ?  116  PHE   A CZ   1 
ATOM   2465 H  H    . PHE   A 1 116 ? 26.611 -11.704 3.150   1.00 11.97 ?  116  PHE   A H    1 
ATOM   2466 H  HA   . PHE   A 1 116 ? 26.710 -10.970 5.655   1.00 11.98 ?  116  PHE   A HA   1 
ATOM   2467 H  HB2  . PHE   A 1 116 ? 24.793 -12.599 4.368   1.00 12.09 ?  116  PHE   A HB2  1 
ATOM   2468 H  HB3  . PHE   A 1 116 ? 24.631 -12.146 5.875   1.00 12.09 ?  116  PHE   A HB3  1 
ATOM   2469 H  HD1  . PHE   A 1 116 ? 25.687 -9.675  3.567   1.00 12.07 ?  116  PHE   A HD1  1 
ATOM   2470 H  HD2  . PHE   A 1 116 ? 22.470 -11.235 5.365   1.00 12.78 ?  116  PHE   A HD2  1 
ATOM   2471 H  HE1  . PHE   A 1 116 ? 24.415 -7.859  2.901   1.00 12.40 ?  116  PHE   A HE1  1 
ATOM   2472 H  HE2  . PHE   A 1 116 ? 21.202 -9.441  4.710   1.00 13.16 ?  116  PHE   A HE2  1 
ATOM   2473 H  HZ   . PHE   A 1 116 ? 22.160 -7.737  3.474   1.00 12.32 ?  116  PHE   A HZ   1 
ATOM   2474 N  N    . ASN   A 1 117 ? 27.430 -14.048 5.191   1.00 10.41 ?  117  ASN   A N    1 
ATOM   2475 C  CA   . ASN   A 1 117 ? 27.807 -15.298 5.850   1.00 10.57 ?  117  ASN   A CA   1 
ATOM   2476 C  C    . ASN   A 1 117 ? 29.076 -15.177 6.676   1.00 11.01 ?  117  ASN   A C    1 
ATOM   2477 O  O    . ASN   A 1 117 ? 29.381 -16.095 7.445   1.00 12.05 ?  117  ASN   A O    1 
ATOM   2478 C  CB   . ASN   A 1 117 ? 27.911 -16.417 4.815   1.00 10.67 ?  117  ASN   A CB   1 
ATOM   2479 C  CG   . ASN   A 1 117 ? 26.553 -16.801 4.289   1.00 10.88 ?  117  ASN   A CG   1 
ATOM   2480 O  OD1  . ASN   A 1 117 ? 25.590 -16.849 5.056   1.00 11.68 ?  117  ASN   A OD1  1 
ATOM   2481 N  ND2  . ASN   A 1 117 ? 26.451 -17.056 2.994   1.00 10.71 ?  117  ASN   A ND2  1 
ATOM   2482 H  H    . ASN   A 1 117 ? 27.506 -14.056 4.333   1.00 12.52 ?  117  ASN   A H    1 
ATOM   2483 H  HA   . ASN   A 1 117 ? 27.092 -15.536 6.456   1.00 12.71 ?  117  ASN   A HA   1 
ATOM   2484 H  HB2  . ASN   A 1 117 ? 28.456 -16.115 4.068   1.00 12.84 ?  117  ASN   A HB2  1 
ATOM   2485 H  HB3  . ASN   A 1 117 ? 28.305 -17.196 5.226   1.00 12.84 ?  117  ASN   A HB3  1 
ATOM   2486 H  HD21 . ASN   A 1 117 ? 25.692 -17.266 2.654   1.00 12.88 ?  117  ASN   A HD21 1 
ATOM   2487 H  HD22 . ASN   A 1 117 ? 27.147 -16.992 2.487   1.00 12.88 ?  117  ASN   A HD22 1 
ATOM   2488 N  N    . GLN   A 1 118 ? 29.806 -14.069 6.549   1.00 10.93 ?  118  GLN   A N    1 
ATOM   2489 C  CA   . GLN   A 1 118 ? 30.991 -13.828 7.359   1.00 11.40 ?  118  GLN   A CA   1 
ATOM   2490 C  C    . GLN   A 1 118 ? 30.656 -13.252 8.729   1.00 11.39 ?  118  GLN   A C    1 
ATOM   2491 O  O    . GLN   A 1 118 ? 31.573 -12.953 9.500   1.00 12.97 ?  118  GLN   A O    1 
ATOM   2492 C  CB   . GLN   A 1 118 ? 31.969 -12.918 6.613   1.00 11.60 ?  118  GLN   A CB   1 
ATOM   2493 C  CG   . GLN   A 1 118 ? 32.438 -13.500 5.290   1.00 11.61 ?  118  GLN   A CG   1 
ATOM   2494 C  CD   . GLN   A 1 118 ? 33.266 -14.767 5.465   1.00 11.91 ?  118  GLN   A CD   1 
ATOM   2495 O  OE1  . GLN   A 1 118 ? 34.129 -14.841 6.346   1.00 12.50 ?  118  GLN   A OE1  1 
ATOM   2496 N  NE2  . GLN   A 1 118 ? 33.007 -15.766 4.624   1.00 12.14 ?  118  GLN   A NE2  1 
ATOM   2497 H  H    . GLN   A 1 118 ? 29.620 -13.423 6.001   1.00 13.15 ?  118  GLN   A H    1 
ATOM   2498 H  HA   . GLN   A 1 118 ? 31.428 -14.680 7.500   1.00 13.71 ?  118  GLN   A HA   1 
ATOM   2499 H  HB2  . GLN   A 1 118 ? 31.535 -12.071 6.437   1.00 13.95 ?  118  GLN   A HB2  1 
ATOM   2500 H  HB3  . GLN   A 1 118 ? 32.749 -12.781 7.174   1.00 13.95 ?  118  GLN   A HB3  1 
ATOM   2501 H  HG2  . GLN   A 1 118 ? 31.662 -13.713 4.745   1.00 13.96 ?  118  GLN   A HG2  1 
ATOM   2502 H  HG3  . GLN   A 1 118 ? 32.987 -12.840 4.835   1.00 13.96 ?  118  GLN   A HG3  1 
ATOM   2503 H  HE21 . GLN   A 1 118 ? 32.393 -15.676 4.020   1.00 14.59 ?  118  GLN   A HE21 1 
ATOM   2504 H  HE22 . GLN   A 1 118 ? 33.445 -16.501 4.677   1.00 14.59 ?  118  GLN   A HE22 1 
ATOM   2505 N  N    . HIS   A 1 119 ? 29.371 -13.113 9.056   1.00 11.17 ?  119  HIS   A N    1 
ATOM   2506 C  CA   . HIS   A 1 119 ? 28.924 -12.504 10.306  1.00 11.71 ?  119  HIS   A CA   1 
ATOM   2507 C  C    . HIS   A 1 119 ? 27.793 -13.331 10.889  1.00 11.92 ?  119  HIS   A C    1 
ATOM   2508 O  O    . HIS   A 1 119 ? 26.835 -13.654 10.184  1.00 12.59 ?  119  HIS   A O    1 
ATOM   2509 C  CB   . HIS   A 1 119 ? 28.465 -11.067 10.046  1.00 12.19 ?  119  HIS   A CB   1 
ATOM   2510 C  CG   . HIS   A 1 119 ? 29.539 -10.255 9.421   1.00 13.50 ?  119  HIS   A CG   1 
ATOM   2511 N  ND1  . HIS   A 1 119 ? 30.530 -9.656  10.164  1.00 15.78 ?  119  HIS   A ND1  1 
ATOM   2512 C  CD2  . HIS   A 1 119 ? 29.859 -10.055 8.123   1.00 14.70 ?  119  HIS   A CD2  1 
ATOM   2513 C  CE1  . HIS   A 1 119 ? 31.386 -9.070  9.346   1.00 16.24 ?  119  HIS   A CE1  1 
ATOM   2514 N  NE2  . HIS   A 1 119 ? 31.009 -9.306  8.103   1.00 16.10 ?  119  HIS   A NE2  1 
ATOM   2515 H  H    . HIS   A 1 119 ? 28.715 -13.370 8.555   1.00 13.43 ?  119  HIS   A H    1 
ATOM   2516 H  HA   . HIS   A 1 119 ? 29.662 -12.494 10.940  1.00 14.08 ?  119  HIS   A HA   1 
ATOM   2517 H  HB2  . HIS   A 1 119 ? 27.704 -11.088 9.448   1.00 14.66 ?  119  HIS   A HB2  1 
ATOM   2518 H  HB3  . HIS   A 1 119 ? 28.223 -10.661 10.891  1.00 14.66 ?  119  HIS   A HB3  1 
ATOM   2519 H  HD2  . HIS   A 1 119 ? 29.384 -10.363 7.382   1.00 17.67 ?  119  HIS   A HD2  1 
ATOM   2520 H  HE1  . HIS   A 1 119 ? 32.127 -8.573  9.599   1.00 19.52 ?  119  HIS   A HE1  1 
ATOM   2521 H  HE2  . HIS   A 1 119 ? 31.401 -9.012  7.394   1.00 19.34 ?  119  HIS   A HE2  1 
ATOM   2522 N  N    . GLU   A 1 120 ? 27.892 -13.648 12.180  1.00 12.76 ?  120  GLU   A N    1 
ATOM   2523 C  CA   . GLU   A 1 120 ? 26.946 -14.588 12.778  1.00 14.46 ?  120  GLU   A CA   1 
ATOM   2524 C  C    . GLU   A 1 120 ? 25.528 -14.026 12.854  1.00 13.11 ?  120  GLU   A C    1 
ATOM   2525 O  O    . GLU   A 1 120 ? 24.552 -14.788 12.744  1.00 13.37 ?  120  GLU   A O    1 
ATOM   2526 C  CB   . GLU   A 1 120 ? 27.434 -15.003 14.169  1.00 18.96 ?  120  GLU   A CB   1 
ATOM   2527 C  CG   . GLU   A 1 120 ? 28.622 -15.951 14.149  1.00 26.61 ?  120  GLU   A CG   1 
ATOM   2528 C  CD   . GLU   A 1 120 ? 28.808 -16.673 15.468  1.00 33.18 ?  120  GLU   A CD   1 
ATOM   2529 O  OE1  . GLU   A 1 120 ? 28.379 -16.134 16.512  1.00 34.88 ?  120  GLU   A OE1  1 
ATOM   2530 O  OE2  . GLU   A 1 120 ? 29.373 -17.787 15.461  1.00 36.77 -1 120  GLU   A OE2  1 
ATOM   2531 H  H    . GLU   A 1 120 ? 28.492 -13.347 12.724  1.00 15.34 ?  120  GLU   A H    1 
ATOM   2532 H  HA   . GLU   A 1 120 ? 26.919 -15.390 12.235  1.00 17.38 ?  120  GLU   A HA   1 
ATOM   2533 H  HB2  . GLU   A 1 120 ? 27.703 -14.211 14.663  1.00 22.79 ?  120  GLU   A HB2  1 
ATOM   2534 H  HB3  . GLU   A 1 120 ? 26.712 -15.450 14.641  1.00 22.79 ?  120  GLU   A HB3  1 
ATOM   2535 H  HG2  . GLU   A 1 120 ? 28.489 -16.621 13.461  1.00 31.96 ?  120  GLU   A HG2  1 
ATOM   2536 H  HG3  . GLU   A 1 120 ? 29.434 -15.450 13.972  1.00 31.96 ?  120  GLU   A HG3  1 
ATOM   2537 N  N    . VAL   A 1 121 ? 25.397 -12.716 13.074  1.00 12.51 ?  121  VAL   A N    1 
ATOM   2538 C  CA   . VAL   A 1 121 ? 24.107 -12.046 13.218  1.00 12.58 ?  121  VAL   A CA   1 
ATOM   2539 C  C    . VAL   A 1 121 ? 24.214 -10.658 12.590  1.00 11.47 ?  121  VAL   A C    1 
ATOM   2540 O  O    . VAL   A 1 121 ? 25.190 -9.938  12.826  1.00 12.34 ?  121  VAL   A O    1 
ATOM   2541 C  CB   . VAL   A 1 121 ? 23.694 -11.909 14.701  1.00 15.35 ?  121  VAL   A CB   1 
ATOM   2542 C  CG1  . VAL   A 1 121 ? 22.322 -11.249 14.820  1.00 15.94 ?  121  VAL   A CG1  1 
ATOM   2543 C  CG2  . VAL   A 1 121 ? 23.699 -13.250 15.410  1.00 17.72 ?  121  VAL   A CG2  1 
ATOM   2544 H  H    . VAL   A 1 121 ? 26.066 -12.181 13.153  1.00 15.04 ?  121  VAL   A H    1 
ATOM   2545 H  HA   . VAL   A 1 121 ? 23.426 -12.556 12.753  1.00 15.12 ?  121  VAL   A HA   1 
ATOM   2546 H  HB   . VAL   A 1 121 ? 24.334 -11.338 15.149  1.00 18.44 ?  121  VAL   A HB   1 
ATOM   2547 H  HG11 . VAL   A 1 121 ? 22.017 -11.324 15.737  1.00 19.16 ?  121  VAL   A HG11 1 
ATOM   2548 H  HG12 . VAL   A 1 121 ? 22.400 -10.313 14.575  1.00 19.16 ?  121  VAL   A HG12 1 
ATOM   2549 H  HG13 . VAL   A 1 121 ? 21.703 -11.698 14.226  1.00 19.16 ?  121  VAL   A HG13 1 
ATOM   2550 H  HG21 . VAL   A 1 121 ? 23.359 -13.132 16.315  1.00 21.30 ?  121  VAL   A HG21 1 
ATOM   2551 H  HG22 . VAL   A 1 121 ? 23.125 -13.869 14.928  1.00 21.30 ?  121  VAL   A HG22 1 
ATOM   2552 H  HG23 . VAL   A 1 121 ? 24.603 -13.594 15.441  1.00 21.30 ?  121  VAL   A HG23 1 
ATOM   2553 N  N    . LEU   A 1 122 ? 23.196 -10.262 11.818  1.00 11.35 ?  122  LEU   A N    1 
ATOM   2554 C  CA   . LEU   A 1 122 ? 23.195 -8.967  11.146  1.00 11.19 ?  122  LEU   A CA   1 
ATOM   2555 C  C    . LEU   A 1 122 ? 21.797 -8.375  11.114  1.00 10.84 ?  122  LEU   A C    1 
ATOM   2556 O  O    . LEU   A 1 122 ? 20.805 -9.094  10.993  1.00 11.93 ?  122  LEU   A O    1 
ATOM   2557 C  CB   . LEU   A 1 122 ? 23.609 -9.057  9.670   1.00 12.54 ?  122  LEU   A CB   1 
ATOM   2558 C  CG   . LEU   A 1 122 ? 24.809 -9.907  9.289   1.00 12.52 ?  122  LEU   A CG   1 
ATOM   2559 C  CD1  . LEU   A 1 122 ? 24.420 -11.365 9.077   1.00 13.66 ?  122  LEU   A CD1  1 
ATOM   2560 C  CD2  . LEU   A 1 122 ? 25.459 -9.337  8.036   1.00 11.96 ?  122  LEU   A CD2  1 
ATOM   2561 H  H    . LEU   A 1 122 ? 22.488 -10.734 11.665  1.00 13.65 ?  122  LEU   A H    1 
ATOM   2562 H  HA   . LEU   A 1 122 ? 23.790 -8.354  11.602  1.00 13.46 ?  122  LEU   A HA   1 
ATOM   2563 H  HB2  . LEU   A 1 122 ? 22.863 -9.413  9.170   1.00 15.08 ?  122  LEU   A HB2  1 
ATOM   2564 H  HB3  . LEU   A 1 122 ? 23.802 -8.161  9.359   1.00 15.08 ?  122  LEU   A HB3  1 
ATOM   2565 H  HG   . LEU   A 1 122 ? 25.477 -9.872  9.995   1.00 15.05 ?  122  LEU   A HG   1 
ATOM   2566 H  HD11 . LEU   A 1 122 ? 25.198 -11.868 8.782   1.00 16.42 ?  122  LEU   A HD11 1 
ATOM   2567 H  HD12 . LEU   A 1 122 ? 24.097 -11.727 9.917   1.00 16.42 ?  122  LEU   A HD12 1 
ATOM   2568 H  HD13 . LEU   A 1 122 ? 23.724 -11.413 8.405   1.00 16.42 ?  122  LEU   A HD13 1 
ATOM   2569 H  HD21 . LEU   A 1 122 ? 26.200 -9.907  7.764   1.00 14.38 ?  122  LEU   A HD21 1 
ATOM   2570 H  HD22 . LEU   A 1 122 ? 24.800 -9.298  7.324   1.00 14.38 ?  122  LEU   A HD22 1 
ATOM   2571 H  HD23 . LEU   A 1 122 ? 25.791 -8.443  8.225   1.00 14.38 ?  122  LEU   A HD23 1 
ATOM   2572 N  N    A LEU   A 1 123 ? 21.737 -7.048  11.223  0.60 10.47 ?  123  LEU   A N    1 
ATOM   2573 N  N    B LEU   A 1 123 ? 21.745 -7.046  11.204  0.40 10.76 ?  123  LEU   A N    1 
ATOM   2574 C  CA   A LEU   A 1 123 ? 20.571 -6.252  10.854  0.60 10.24 ?  123  LEU   A CA   1 
ATOM   2575 C  CA   B LEU   A 1 123 ? 20.567 -6.248  10.887  0.40 10.76 ?  123  LEU   A CA   1 
ATOM   2576 C  C    A LEU   A 1 123 ? 20.802 -5.734  9.443   0.60 9.30  ?  123  LEU   A C    1 
ATOM   2577 C  C    B LEU   A 1 123 ? 20.778 -5.681  9.488   0.40 10.41 ?  123  LEU   A C    1 
ATOM   2578 O  O    A LEU   A 1 123 ? 21.892 -5.240  9.144   0.60 8.92  ?  123  LEU   A O    1 
ATOM   2579 O  O    B LEU   A 1 123 ? 21.718 -4.908  9.274   0.40 10.32 ?  123  LEU   A O    1 
ATOM   2580 C  CB   A LEU   A 1 123 ? 20.434 -5.063  11.804  0.60 11.05 ?  123  LEU   A CB   1 
ATOM   2581 C  CB   B LEU   A 1 123 ? 20.438 -5.110  11.901  0.40 11.10 ?  123  LEU   A CB   1 
ATOM   2582 C  CG   A LEU   A 1 123 ? 19.357 -4.031  11.460  0.60 11.94 ?  123  LEU   A CG   1 
ATOM   2583 C  CG   B LEU   A 1 123 ? 19.453 -3.985  11.570  0.40 11.20 ?  123  LEU   A CG   1 
ATOM   2584 C  CD1  A LEU   A 1 123 ? 17.972 -4.663  11.474  0.60 12.74 ?  123  LEU   A CD1  1 
ATOM   2585 C  CD1  B LEU   A 1 123 ? 18.022 -4.493  11.615  0.40 11.88 ?  123  LEU   A CD1  1 
ATOM   2586 C  CD2  A LEU   A 1 123 ? 19.430 -2.862  12.430  0.60 12.38 ?  123  LEU   A CD2  1 
ATOM   2587 C  CD2  B LEU   A 1 123 ? 19.639 -2.806  12.512  0.40 11.29 ?  123  LEU   A CD2  1 
ATOM   2588 H  H    A LEU   A 1 123 ? 22.390 -6.568  11.516  0.60 12.59 ?  123  LEU   A H    1 
ATOM   2589 H  H    B LEU   A 1 123 ? 22.415 -6.563  11.450  0.40 12.94 ?  123  LEU   A H    1 
ATOM   2590 H  HA   A LEU   A 1 123 ? 19.763 -6.792  10.881  0.60 12.32 ?  123  LEU   A HA   1 
ATOM   2591 H  HA   B LEU   A 1 123 ? 19.764 -6.794  10.906  0.40 12.94 ?  123  LEU   A HA   1 
ATOM   2592 H  HB2  A LEU   A 1 123 ? 20.224 -5.402  12.688  0.60 13.29 ?  123  LEU   A HB2  1 
ATOM   2593 H  HB2  B LEU   A 1 123 ? 20.154 -5.490  12.750  0.40 13.35 ?  123  LEU   A HB2  1 
ATOM   2594 H  HB3  A LEU   A 1 123 ? 21.277 -4.593  11.829  0.60 13.29 ?  123  LEU   A HB3  1 
ATOM   2595 H  HB3  B LEU   A 1 123 ? 21.307 -4.700  12.011  0.40 13.35 ?  123  LEU   A HB3  1 
ATOM   2596 H  HG   A LEU   A 1 123 ? 19.515 -3.681  10.567  0.60 14.36 ?  123  LEU   A HG   1 
ATOM   2597 H  HG   B LEU   A 1 123 ? 19.622 -3.663  10.671  0.40 13.47 ?  123  LEU   A HG   1 
ATOM   2598 H  HD11 A LEU   A 1 123 ? 17.306 -3.973  11.327  0.60 15.31 ?  123  LEU   A HD11 1 
ATOM   2599 H  HD11 B LEU   A 1 123 ? 17.419 -3.764  11.408  0.40 14.29 ?  123  LEU   A HD11 1 
ATOM   2600 H  HD12 A LEU   A 1 123 ? 17.920 -5.328  10.771  0.60 15.31 ?  123  LEU   A HD12 1 
ATOM   2601 H  HD12 B LEU   A 1 123 ? 17.920 -5.204  10.961  0.40 14.29 ?  123  LEU   A HD12 1 
ATOM   2602 H  HD13 A LEU   A 1 123 ? 17.827 -5.082  12.338  0.60 15.31 ?  123  LEU   A HD13 1 
ATOM   2603 H  HD13 B LEU   A 1 123 ? 17.837 -4.835  12.504  0.40 14.29 ?  123  LEU   A HD13 1 
ATOM   2604 H  HD21 A LEU   A 1 123 ? 18.745 -2.216  12.202  0.60 14.88 ?  123  LEU   A HD21 1 
ATOM   2605 H  HD21 B LEU   A 1 123 ? 19.002 -2.113  12.279  0.40 13.58 ?  123  LEU   A HD21 1 
ATOM   2606 H  HD22 A LEU   A 1 123 ? 19.286 -3.194  13.331  0.60 14.88 ?  123  LEU   A HD22 1 
ATOM   2607 H  HD22 B LEU   A 1 123 ? 19.485 -3.104  13.422  0.40 13.58 ?  123  LEU   A HD22 1 
ATOM   2608 H  HD23 A LEU   A 1 123 ? 20.307 -2.454  12.365  0.60 14.88 ?  123  LEU   A HD23 1 
ATOM   2609 H  HD23 B LEU   A 1 123 ? 20.543 -2.471  12.421  0.40 13.58 ?  123  LEU   A HD23 1 
ATOM   2610 N  N    A ALA   A 1 124 ? 19.790 -5.824  8.580   0.60 9.01  ?  124  ALA   A N    1 
ATOM   2611 N  N    B ALA   A 1 124 ? 19.918 -6.054  8.540   0.40 10.25 ?  124  ALA   A N    1 
ATOM   2612 C  CA   A ALA   A 1 124 ? 20.037 -5.539  7.175   0.60 8.78  ?  124  ALA   A CA   1 
ATOM   2613 C  CA   B ALA   A 1 124 ? 20.198 -5.793  7.135   0.40 10.51 ?  124  ALA   A CA   1 
ATOM   2614 C  C    A ALA   A 1 124 ? 18.779 -5.079  6.454   0.60 8.56  ?  124  ALA   A C    1 
ATOM   2615 C  C    B ALA   A 1 124 ? 18.967 -5.323  6.372   0.40 10.11 ?  124  ALA   A C    1 
ATOM   2616 O  O    A ALA   A 1 124 ? 17.657 -5.419  6.860   0.60 9.40  ?  124  ALA   A O    1 
ATOM   2617 O  O    B ALA   A 1 124 ? 17.832 -5.664  6.731   0.40 10.21 ?  124  ALA   A O    1 
ATOM   2618 C  CB   A ALA   A 1 124 ? 20.603 -6.774  6.459   0.60 8.95  ?  124  ALA   A CB   1 
ATOM   2619 C  CB   B ALA   A 1 124 ? 20.766 -7.041  6.439   0.40 11.07 ?  124  ALA   A CB   1 
ATOM   2620 H  H    A ALA   A 1 124 ? 18.976 -6.033  8.775   0.60 10.84 ?  124  ALA   A H    1 
ATOM   2621 H  H    B ALA   A 1 124 ? 19.173 -6.458  8.686   0.40 12.33 ?  124  ALA   A H    1 
ATOM   2622 H  HA   A ALA   A 1 124 ? 20.710 -4.841  7.123   0.60 10.56 ?  124  ALA   A HA   1 
ATOM   2623 H  HA   B ALA   A 1 124 ? 20.865 -5.098  7.085   0.40 12.64 ?  124  ALA   A HA   1 
ATOM   2624 H  HB1  A ALA   A 1 124 ? 20.768 -6.555  5.528   0.60 10.77 ?  124  ALA   A HB1  1 
ATOM   2625 H  HB1  B ALA   A 1 124 ? 20.941 -6.835  5.507   0.40 13.31 ?  124  ALA   A HB1  1 
ATOM   2626 H  HB2  A ALA   A 1 124 ? 21.440 -7.036  6.885   0.60 10.77 ?  124  ALA   A HB2  1 
ATOM   2627 H  HB2  B ALA   A 1 124 ? 21.593 -7.301  6.879   0.40 13.31 ?  124  ALA   A HB2  1 
ATOM   2628 H  HB3  A ALA   A 1 124 ? 19.964 -7.498  6.522   0.60 10.77 ?  124  ALA   A HB3  1 
ATOM   2629 H  HB3  B ALA   A 1 124 ? 20.121 -7.764  6.502   0.40 13.31 ?  124  ALA   A HB3  1 
ATOM   2630 N  N    A PRO   A 1 125 ? 18.940 -4.318  5.375   0.60 8.65  ?  125  PRO   A N    1 
ATOM   2631 N  N    B PRO   A 1 125 ? 19.168 -4.558  5.300   0.40 9.10  ?  125  PRO   A N    1 
ATOM   2632 C  CA   A PRO   A 1 125 ? 17.863 -4.096  4.413   0.60 9.78  ?  125  PRO   A CA   1 
ATOM   2633 C  CA   B PRO   A 1 125 ? 18.081 -4.210  4.388   0.40 9.62  ?  125  PRO   A CA   1 
ATOM   2634 C  C    A PRO   A 1 125 ? 17.945 -5.160  3.321   0.60 9.38  ?  125  PRO   A C    1 
ATOM   2635 C  C    B PRO   A 1 125 ? 18.021 -5.230  3.257   0.40 10.22 ?  125  PRO   A C    1 
ATOM   2636 O  O    A PRO   A 1 125 ? 18.915 -5.915  3.226   0.60 9.87  ?  125  PRO   A O    1 
ATOM   2637 O  O    B PRO   A 1 125 ? 18.886 -6.096  3.118   0.40 10.78 ?  125  PRO   A O    1 
ATOM   2638 C  CB   A PRO   A 1 125 ? 18.243 -2.726  3.832   0.60 10.14 ?  125  PRO   A CB   1 
ATOM   2639 C  CB   B PRO   A 1 125 ? 18.562 -2.863  3.834   0.40 9.21  ?  125  PRO   A CB   1 
ATOM   2640 C  CG   A PRO   A 1 125 ? 19.751 -2.816  3.745   0.60 10.08 ?  125  PRO   A CG   1 
ATOM   2641 C  CG   B PRO   A 1 125 ? 20.038 -3.081  3.676   0.40 8.60  ?  125  PRO   A CG   1 
ATOM   2642 C  CD   A PRO   A 1 125 ? 20.176 -3.616  4.976   0.60 9.56  ?  125  PRO   A CD   1 
ATOM   2643 C  CD   B PRO   A 1 125 ? 20.445 -3.971  4.849   0.40 8.18  ?  125  PRO   A CD   1 
ATOM   2644 H  HA   A PRO   A 1 125 ? 16.988 -4.075  4.837   0.60 11.76 ?  125  PRO   A HA   1 
ATOM   2645 H  HA   B PRO   A 1 125 ? 17.224 -4.132  4.840   0.40 11.57 ?  125  PRO   A HA   1 
ATOM   2646 H  HB2  A PRO   A 1 125 ? 17.846 -2.616  2.956   0.60 12.19 ?  125  PRO   A HB2  1 
ATOM   2647 H  HB2  B PRO   A 1 125 ? 18.149 -2.694  2.975   0.40 11.08 ?  125  PRO   A HB2  1 
ATOM   2648 H  HB3  A PRO   A 1 125 ? 17.969 -2.018  4.437   0.60 12.19 ?  125  PRO   A HB3  1 
ATOM   2649 H  HB3  B PRO   A 1 125 ? 18.371 -2.151  4.465   0.40 11.08 ?  125  PRO   A HB3  1 
ATOM   2650 H  HG2  A PRO   A 1 125 ? 20.008 -3.284  2.932   0.60 12.12 ?  125  PRO   A HG2  1 
ATOM   2651 H  HG2  B PRO   A 1 125 ? 20.209 -3.524  2.826   0.40 10.34 ?  125  PRO   A HG2  1 
ATOM   2652 H  HG3  A PRO   A 1 125 ? 20.137 -1.926  3.761   0.60 12.12 ?  125  PRO   A HG3  1 
ATOM   2653 H  HG3  B PRO   A 1 125 ? 20.496 -2.228  3.710   0.40 10.34 ?  125  PRO   A HG3  1 
ATOM   2654 H  HD2  A PRO   A 1 125 ? 20.874 -4.247  4.747   0.60 11.49 ?  125  PRO   A HD2  1 
ATOM   2655 H  HD2  B PRO   A 1 125 ? 21.058 -4.663  4.547   0.40 9.85  ?  125  PRO   A HD2  1 
ATOM   2656 H  HD3  A PRO   A 1 125 ? 20.467 -3.009  5.682   0.60 11.49 ?  125  PRO   A HD3  1 
ATOM   2657 H  HD3  B PRO   A 1 125 ? 20.835 -3.434  5.554   0.40 9.85  ?  125  PRO   A HD3  1 
ATOM   2658 N  N    A LEU   A 1 126 ? 16.918 -5.193  2.476   0.60 9.73  ?  126  LEU   A N    1 
ATOM   2659 N  N    B LEU   A 1 126 ? 16.989 -5.097  2.429   0.40 10.57 ?  126  LEU   A N    1 
ATOM   2660 C  CA   A LEU   A 1 126 ? 16.961 -6.041  1.290   0.60 10.22 ?  126  LEU   A CA   1 
ATOM   2661 C  CA   B LEU   A 1 126 ? 16.901 -5.882  1.202   0.40 10.19 ?  126  LEU   A CA   1 
ATOM   2662 C  C    A LEU   A 1 126 ? 17.904 -5.440  0.252   0.60 10.59 ?  126  LEU   A C    1 
ATOM   2663 C  C    B LEU   A 1 126 ? 17.844 -5.297  0.156   0.40 9.52  ?  126  LEU   A C    1 
ATOM   2664 O  O    A LEU   A 1 126 ? 17.738 -4.286  -0.159  0.60 11.20 ?  126  LEU   A O    1 
ATOM   2665 O  O    B LEU   A 1 126 ? 17.570 -4.240  -0.423  0.40 9.39  ?  126  LEU   A O    1 
ATOM   2666 C  CB   A LEU   A 1 126 ? 15.565 -6.226  0.702   0.60 10.68 ?  126  LEU   A CB   1 
ATOM   2667 C  CB   B LEU   A 1 126 ? 15.469 -5.894  0.685   0.40 10.58 ?  126  LEU   A CB   1 
ATOM   2668 C  CG   A LEU   A 1 126 ? 14.649 -7.229  1.410   0.60 11.80 ?  126  LEU   A CG   1 
ATOM   2669 C  CG   B LEU   A 1 126 ? 14.530 -6.737  1.537   0.40 10.90 ?  126  LEU   A CG   1 
ATOM   2670 C  CD1  A LEU   A 1 126 ? 13.232 -7.127  0.865   0.60 12.97 ?  126  LEU   A CD1  1 
ATOM   2671 C  CD1  B LEU   A 1 126 ? 13.132 -6.583  0.999   0.40 11.37 ?  126  LEU   A CD1  1 
ATOM   2672 C  CD2  A LEU   A 1 126 ? 15.164 -8.647  1.249   0.60 11.78 ?  126  LEU   A CD2  1 
ATOM   2673 C  CD2  B LEU   A 1 126 ? 14.947 -8.201  1.531   0.40 11.20 ?  126  LEU   A CD2  1 
ATOM   2674 H  H    A LEU   A 1 126 ? 16.203 -4.721  2.552   0.60 11.70 ?  126  LEU   A H    1 
ATOM   2675 H  H    B LEU   A 1 126 ? 16.320 -4.564  2.559   0.40 12.71 ?  126  LEU   A H    1 
ATOM   2676 H  HA   A LEU   A 1 126 ? 17.309 -6.904  1.532   0.60 12.30 ?  126  LEU   A HA   1 
ATOM   2677 H  HA   B LEU   A 1 126 ? 17.172 -6.795  1.387   0.40 12.26 ?  126  LEU   A HA   1 
ATOM   2678 H  HB2  A LEU   A 1 126 ? 15.110 -5.370  0.716   0.60 12.85 ?  126  LEU   A HB2  1 
ATOM   2679 H  HB2  B LEU   A 1 126 ? 15.128 -4.984  0.675   0.40 12.72 ?  126  LEU   A HB2  1 
ATOM   2680 H  HB3  A LEU   A 1 126 ? 15.657 -6.525  -0.216  0.60 12.85 ?  126  LEU   A HB3  1 
ATOM   2681 H  HB3  B LEU   A 1 126 ? 15.461 -6.258  -0.214  0.40 12.72 ?  126  LEU   A HB3  1 
ATOM   2682 H  HG   A LEU   A 1 126 ? 14.620 -7.027  2.358   0.60 14.18 ?  126  LEU   A HG   1 
ATOM   2683 H  HG   B LEU   A 1 126 ? 14.544 -6.412  2.454   0.40 13.11 ?  126  LEU   A HG   1 
ATOM   2684 H  HD11 A LEU   A 1 126 ? 12.668 -7.770  1.325   0.60 15.59 ?  126  LEU   A HD11 1 
ATOM   2685 H  HD11 B LEU   A 1 126 ? 12.532 -7.130  1.525   0.40 13.67 ?  126  LEU   A HD11 1 
ATOM   2686 H  HD12 A LEU   A 1 126 ? 12.900 -6.229  1.017   0.60 15.59 ?  126  LEU   A HD12 1 
ATOM   2687 H  HD12 B LEU   A 1 126 ? 12.873 -5.651  1.056   0.40 13.67 ?  126  LEU   A HD12 1 
ATOM   2688 H  HD13 A LEU   A 1 126 ? 13.244 -7.320  -0.086  0.60 15.59 ?  126  LEU   A HD13 1 
ATOM   2689 H  HD13 B LEU   A 1 126 ? 13.123 -6.874  0.073   0.40 13.67 ?  126  LEU   A HD13 1 
ATOM   2690 H  HD21 A LEU   A 1 126 ? 14.510 -9.262  1.603   0.60 14.17 ?  126  LEU   A HD21 1 
ATOM   2691 H  HD21 B LEU   A 1 126 ? 14.210 -8.741  1.845   0.40 13.47 ?  126  LEU   A HD21 1 
ATOM   2692 H  HD22 A LEU   A 1 126 ? 15.311 -8.818  0.305   0.60 14.17 ?  126  LEU   A HD22 1 
ATOM   2693 H  HD22 B LEU   A 1 126 ? 15.185 -8.454  0.624   0.40 13.47 ?  126  LEU   A HD22 1 
ATOM   2694 H  HD23 A LEU   A 1 126 ? 16.001 -8.730  1.733   0.60 14.17 ?  126  LEU   A HD23 1 
ATOM   2695 H  HD23 B LEU   A 1 126 ? 15.715 -8.313  2.115   0.40 13.47 ?  126  LEU   A HD23 1 
ATOM   2696 N  N    A LEU   A 1 127 ? 18.891 -6.224  -0.174  0.60 10.82 ?  127  LEU   A N    1 
ATOM   2697 N  N    B LEU   A 1 127 ? 18.944 -5.997  -0.106  0.40 9.38  ?  127  LEU   A N    1 
ATOM   2698 C  CA   A LEU   A 1 127 ? 19.873 -5.744  -1.134  0.60 10.43 ?  127  LEU   A CA   1 
ATOM   2699 C  CA   B LEU   A 1 127 ? 19.923 -5.512  -1.065  0.40 9.41  ?  127  LEU   A CA   1 
ATOM   2700 C  C    A LEU   A 1 127 ? 19.230 -5.500  -2.490  0.60 10.09 ?  127  LEU   A C    1 
ATOM   2701 C  C    B LEU   A 1 127 ? 19.330 -5.464  -2.468  0.40 9.48  ?  127  LEU   A C    1 
ATOM   2702 O  O    A LEU   A 1 127 ? 18.379 -6.265  -2.954  0.60 10.44 ?  127  LEU   A O    1 
ATOM   2703 O  O    B LEU   A 1 127 ? 18.511 -6.300  -2.859  0.40 9.85  ?  127  LEU   A O    1 
ATOM   2704 C  CB   A LEU   A 1 127 ? 21.014 -6.751  -1.278  0.60 10.10 ?  127  LEU   A CB   1 
ATOM   2705 C  CB   B LEU   A 1 127 ? 21.151 -6.420  -1.055  0.40 9.56  ?  127  LEU   A CB   1 
ATOM   2706 C  CG   A LEU   A 1 127 ? 21.852 -6.994  -0.024  0.60 9.79  ?  127  LEU   A CG   1 
ATOM   2707 C  CG   B LEU   A 1 127 ? 21.913 -6.501  0.268   0.40 9.95  ?  127  LEU   A CG   1 
ATOM   2708 C  CD1  A LEU   A 1 127 ? 22.964 -7.978  -0.326  0.60 9.52  ?  127  LEU   A CD1  1 
ATOM   2709 C  CD1  B LEU   A 1 127 ? 23.044 -7.499  0.145   0.40 10.64 ?  127  LEU   A CD1  1 
ATOM   2710 C  CD2  A LEU   A 1 127 ? 22.434 -5.703  0.515   0.60 10.63 ?  127  LEU   A CD2  1 
ATOM   2711 C  CD2  B LEU   A 1 127 ? 22.451 -5.136  0.669   0.40 10.78 ?  127  LEU   A CD2  1 
ATOM   2712 H  H    A LEU   A 1 127 ? 19.018 -7.033  0.089   0.60 13.01 ?  127  LEU   A H    1 
ATOM   2713 H  H    B LEU   A 1 127 ? 19.144 -6.751  0.264   0.40 11.28 ?  127  LEU   A H    1 
ATOM   2714 H  HA   A LEU   A 1 127 ? 20.244 -4.907  -0.820  0.60 12.54 ?  127  LEU   A HA   1 
ATOM   2715 H  HA   B LEU   A 1 127 ? 20.201 -4.617  -0.816  0.40 11.32 ?  127  LEU   A HA   1 
ATOM   2716 H  HB2  A LEU   A 1 127 ? 20.637 -7.606  -1.545  0.60 12.14 ?  127  LEU   A HB2  1 
ATOM   2717 H  HB2  B LEU   A 1 127 ? 20.866 -7.320  -1.278  0.40 11.50 ?  127  LEU   A HB2  1 
ATOM   2718 H  HB3  A LEU   A 1 127 ? 21.617 -6.437  -1.969  0.60 12.14 ?  127  LEU   A HB3  1 
ATOM   2719 H  HB3  B LEU   A 1 127 ? 21.771 -6.099  -1.724  0.40 11.50 ?  127  LEU   A HB3  1 
ATOM   2720 H  HG   A LEU   A 1 127 ? 21.284 -7.385  0.664   0.60 11.78 ?  127  LEU   A HG   1 
ATOM   2721 H  HG   B LEU   A 1 127 ? 21.311 -6.807  0.968   0.40 11.96 ?  127  LEU   A HG   1 
ATOM   2722 H  HD11 A LEU   A 1 127 ? 23.451 -8.168  0.493   0.60 11.45 ?  127  LEU   A HD11 1 
ATOM   2723 H  HD11 B LEU   A 1 127 ? 23.627 -7.407  0.914   0.40 12.79 ?  127  LEU   A HD11 1 
ATOM   2724 H  HD12 A LEU   A 1 127 ? 22.577 -8.802  -0.673  0.60 11.45 ?  127  LEU   A HD12 1 
ATOM   2725 H  HD12 B LEU   A 1 127 ? 22.672 -8.393  0.113   0.40 12.79 ?  127  LEU   A HD12 1 
ATOM   2726 H  HD13 A LEU   A 1 127 ? 23.558 -7.592  -0.984  0.60 11.45 ?  127  LEU   A HD13 1 
ATOM   2727 H  HD13 B LEU   A 1 127 ? 23.537 -7.312  -0.668  0.40 12.79 ?  127  LEU   A HD13 1 
ATOM   2728 H  HD21 A LEU   A 1 127 ? 23.085 -5.912  1.202   0.60 12.78 ?  127  LEU   A HD21 1 
ATOM   2729 H  HD21 B LEU   A 1 127 ? 23.022 -5.239  1.446   0.40 12.97 ?  127  LEU   A HD21 1 
ATOM   2730 H  HD22 A LEU   A 1 127 ? 22.863 -5.226  -0.213  0.60 12.78 ?  127  LEU   A HD22 1 
ATOM   2731 H  HD22 B LEU   A 1 127 ? 22.959 -4.771  -0.071  0.40 12.97 ?  127  LEU   A HD22 1 
ATOM   2732 H  HD23 A LEU   A 1 127 ? 21.719 -5.164  0.887   0.60 12.78 ?  127  LEU   A HD23 1 
ATOM   2733 H  HD23 B LEU   A 1 127 ? 21.706 -4.552  0.881   0.40 12.97 ?  127  LEU   A HD23 1 
ATOM   2734 N  N    A SER   A 1 128 ? 19.658 -4.417  -3.127  0.60 9.62  ?  128  SER   A N    1 
ATOM   2735 N  N    B SER   A 1 128 ? 19.765 -4.463  -3.230  0.40 9.42  ?  128  SER   A N    1 
ATOM   2736 C  CA   A SER   A 1 128 ? 19.232 -3.993  -4.453  0.60 9.91  ?  128  SER   A CA   1 
ATOM   2737 C  CA   B SER   A 1 128 ? 19.365 -4.166  -4.602  0.40 9.28  ?  128  SER   A CA   1 
ATOM   2738 C  C    A SER   A 1 128 ? 17.769 -3.564  -4.512  0.60 10.07 ?  128  SER   A C    1 
ATOM   2739 C  C    B SER   A 1 128 ? 17.923 -3.682  -4.732  0.40 9.31  ?  128  SER   A C    1 
ATOM   2740 O  O    A SER   A 1 128 ? 17.261 -3.295  -5.603  0.60 11.55 ?  128  SER   A O    1 
ATOM   2741 O  O    B SER   A 1 128 ? 17.526 -3.286  -5.830  0.40 9.71  ?  128  SER   A O    1 
ATOM   2742 C  CB   A SER   A 1 128 ? 19.569 -5.015  -5.548  0.60 10.00 ?  128  SER   A CB   1 
ATOM   2743 C  CB   B SER   A 1 128 ? 19.659 -5.303  -5.596  0.40 9.62  ?  128  SER   A CB   1 
ATOM   2744 O  OG   A SER   A 1 128 ? 20.976 -5.212  -5.625  0.60 10.32 ?  128  SER   A OG   1 
ATOM   2745 O  OG   B SER   A 1 128 ? 21.059 -5.511  -5.719  0.40 10.28 ?  128  SER   A OG   1 
ATOM   2746 H  H    A SER   A 1 128 ? 20.246 -3.881  -2.790  0.60 11.57 ?  128  SER   A H    1 
ATOM   2747 H  H    B SER   A 1 128 ? 20.353 -3.900  -2.948  0.40 11.33 ?  128  SER   A H    1 
ATOM   2748 H  HA   A SER   A 1 128 ? 19.752 -3.210  -4.665  0.60 11.91 ?  128  SER   A HA   1 
ATOM   2749 H  HA   B SER   A 1 128 ? 19.906 -3.423  -4.892  0.40 11.16 ?  128  SER   A HA   1 
ATOM   2750 H  HB2  A SER   A 1 128 ? 19.136 -5.858  -5.346  0.60 12.03 ?  128  SER   A HB2  1 
ATOM   2751 H  HB2  B SER   A 1 128 ? 19.243 -6.121  -5.285  0.40 11.57 ?  128  SER   A HB2  1 
ATOM   2752 H  HB3  A SER   A 1 128 ? 19.245 -4.676  -6.404  0.60 12.03 ?  128  SER   A HB3  1 
ATOM   2753 H  HB3  B SER   A 1 128 ? 19.298 -5.061  -6.469  0.40 11.57 ?  128  SER   A HB3  1 
ATOM   2754 H  HG   A SER   A 1 128 ? 21.359 -4.491  -5.813  0.60 12.41 ?  128  SER   A HG   1 
ATOM   2755 H  HG   B SER   A 1 128 ? 21.429 -4.808  -5.993  0.40 12.36 ?  128  SER   A HG   1 
ATOM   2756 N  N    A ALA   A 1 129 ? 17.088 -3.463  -3.371  0.60 10.63 ?  129  ALA   A N    1 
ATOM   2757 N  N    B ALA   A 1 129 ? 17.144 -3.666  -3.651  0.40 9.98  ?  129  ALA   A N    1 
ATOM   2758 C  CA   A ALA   A 1 129 ? 15.730 -2.950  -3.329  0.60 10.69 ?  129  ALA   A CA   1 
ATOM   2759 C  CA   B ALA   A 1 129 ? 15.767 -3.189  -3.687  0.40 10.36 ?  129  ALA   A CA   1 
ATOM   2760 C  C    A ALA   A 1 129 ? 15.752 -1.422  -3.367  0.60 10.61 ?  129  ALA   A C    1 
ATOM   2761 C  C    B ALA   A 1 129 ? 15.741 -1.665  -3.538  0.40 10.71 ?  129  ALA   A C    1 
ATOM   2762 O  O    A ALA   A 1 129 ? 16.806 -0.786  -3.480  0.60 10.56 ?  129  ALA   A O    1 
ATOM   2763 O  O    B ALA   A 1 129 ? 16.777 -0.993  -3.533  0.40 11.27 ?  129  ALA   A O    1 
ATOM   2764 C  CB   A ALA   A 1 129 ? 14.996 -3.490  -2.101  0.60 11.55 ?  129  ALA   A CB   1 
ATOM   2765 C  CB   B ALA   A 1 129 ? 14.935 -3.907  -2.624  0.40 10.21 ?  129  ALA   A CB   1 
ATOM   2766 H  H    A ALA   A 1 129 ? 17.394 -3.698  -2.600  0.60 12.79 ?  129  ALA   A H    1 
ATOM   2767 H  H    B ALA   A 1 129 ? 17.393 -3.941  -2.872  0.40 12.00 ?  129  ALA   A H    1 
ATOM   2768 H  HA   A ALA   A 1 129 ? 15.253 -3.259  -4.111  0.60 12.85 ?  129  ALA   A HA   1 
ATOM   2769 H  HA   B ALA   A 1 129 ? 15.388 -3.412  -4.549  0.40 12.46 ?  129  ALA   A HA   1 
ATOM   2770 H  HB1  A ALA   A 1 129 ? 14.087 -3.143  -2.095  0.60 13.89 ?  129  ALA   A HB1  1 
ATOM   2771 H  HB1  B ALA   A 1 129 ? 14.023 -3.581  -2.664  0.40 12.28 ?  129  ALA   A HB1  1 
ATOM   2772 H  HB2  A ALA   A 1 129 ? 14.972 -4.461  -2.142  0.60 13.89 ?  129  ALA   A HB2  1 
ATOM   2773 H  HB2  B ALA   A 1 129 ? 14.953 -4.862  -2.797  0.40 12.28 ?  129  ALA   A HB2  1 
ATOM   2774 H  HB3  A ALA   A 1 129 ? 15.460 -3.207  -1.298  0.60 13.89 ?  129  ALA   A HB3  1 
ATOM   2775 H  HB3  B ALA   A 1 129 ? 15.313 -3.725  -1.748  0.40 12.28 ?  129  ALA   A HB3  1 
ATOM   2776 N  N    A GLY   A 1 130 ? 14.571 -0.821  -3.287  0.60 11.46 ?  130  GLY   A N    1 
ATOM   2777 N  N    B GLY   A 1 130 ? 14.541 -1.099  -3.430  0.40 10.94 ?  130  GLY   A N    1 
ATOM   2778 C  CA   A GLY   A 1 130 ? 14.505 0.630   -3.306  0.60 12.16 ?  130  GLY   A CA   1 
ATOM   2779 C  CA   B GLY   A 1 130 ? 14.416 0.338   -3.246  0.40 11.22 ?  130  GLY   A CA   1 
ATOM   2780 C  C    A GLY   A 1 130 ? 15.153 1.196   -4.555  0.60 12.28 ?  130  GLY   A C    1 
ATOM   2781 C  C    B GLY   A 1 130 ? 14.923 1.103   -4.454  0.40 10.95 ?  130  GLY   A C    1 
ATOM   2782 O  O    A GLY   A 1 130 ? 14.932 0.716   -5.671  0.60 12.52 ?  130  GLY   A O    1 
ATOM   2783 O  O    B GLY   A 1 130 ? 14.652 0.750   -5.606  0.40 10.73 ?  130  GLY   A O    1 
ATOM   2784 H  H    A GLY   A 1 130 ? 13.814 -1.225  -3.220  0.60 13.77 ?  130  GLY   A H    1 
ATOM   2785 H  H    B GLY   A 1 130 ? 13.798 -1.527  -3.459  0.40 13.16 ?  130  GLY   A H    1 
ATOM   2786 H  HA2  A GLY   A 1 130 ? 13.579 0.913   -3.280  0.60 14.62 ?  130  GLY   A HA2  1 
ATOM   2787 H  HA2  B GLY   A 1 130 ? 13.484 0.564   -3.086  0.40 13.49 ?  130  GLY   A HA2  1 
ATOM   2788 H  HA3  A GLY   A 1 130 ? 14.964 0.988   -2.530  0.60 14.62 ?  130  GLY   A HA3  1 
ATOM   2789 H  HA3  B GLY   A 1 130 ? 14.936 0.614   -2.475  0.40 13.49 ?  130  GLY   A HA3  1 
ATOM   2790 N  N    A ILE   A 1 131 ? 15.991 2.220   -4.365  0.60 11.90 ?  131  ILE   A N    1 
ATOM   2791 N  N    B ILE   A 1 131 ? 15.676 2.174   -4.186  0.40 11.48 ?  131  ILE   A N    1 
ATOM   2792 C  CA   A ILE   A 1 131 ? 16.548 2.963   -5.492  0.60 11.54 ?  131  ILE   A CA   1 
ATOM   2793 C  CA   B ILE   A 1 131 ? 16.239 3.007   -5.241  0.40 11.42 ?  131  ILE   A CA   1 
ATOM   2794 C  C    A ILE   A 1 131 ? 17.554 2.172   -6.311  0.60 10.61 ?  131  ILE   A C    1 
ATOM   2795 C  C    B ILE   A 1 131 ? 17.245 2.262   -6.109  0.40 10.92 ?  131  ILE   A C    1 
ATOM   2796 O  O    A ILE   A 1 131 ? 17.967 2.650   -7.376  0.60 11.69 ?  131  ILE   A O    1 
ATOM   2797 O  O    B ILE   A 1 131 ? 17.667 2.791   -7.141  0.40 11.04 ?  131  ILE   A O    1 
ATOM   2798 C  CB   A ILE   A 1 131 ? 17.112 4.338   -5.075  0.60 12.91 ?  131  ILE   A CB   1 
ATOM   2799 C  CB   B ILE   A 1 131 ? 16.881 4.281   -4.644  0.40 12.43 ?  131  ILE   A CB   1 
ATOM   2800 C  CG1  A ILE   A 1 131 ? 18.345 4.194   -4.177  0.60 13.74 ?  131  ILE   A CG1  1 
ATOM   2801 C  CG1  B ILE   A 1 131 ? 18.074 3.915   -3.755  0.40 13.44 ?  131  ILE   A CG1  1 
ATOM   2802 C  CG2  A ILE   A 1 131 ? 16.036 5.158   -4.379  0.60 13.46 ?  131  ILE   A CG2  1 
ATOM   2803 C  CG2  B ILE   A 1 131 ? 15.854 5.079   -3.848  0.40 12.52 ?  131  ILE   A CG2  1 
ATOM   2804 C  CD1  A ILE   A 1 131 ? 18.960 5.532   -3.783  0.60 14.49 ?  131  ILE   A CD1  1 
ATOM   2805 C  CD1  B ILE   A 1 131 ? 18.796 5.117   -3.167  0.40 14.06 ?  131  ILE   A CD1  1 
ATOM   2806 H  H    A ILE   A 1 131 ? 16.245 2.497   -3.595  0.60 14.30 ?  131  ILE   A H    1 
ATOM   2807 H  H    B ILE   A 1 131 ? 15.863 2.445   -3.392  0.40 13.80 ?  131  ILE   A H    1 
ATOM   2808 H  HA   A ILE   A 1 131 ? 15.824 3.146   -6.092  0.60 13.88 ?  131  ILE   A HA   1 
ATOM   2809 H  HA   B ILE   A 1 131 ? 15.515 3.300   -5.818  0.40 13.73 ?  131  ILE   A HA   1 
ATOM   2810 H  HB   A ILE   A 1 131 ? 17.380 4.810   -5.878  0.60 15.52 ?  131  ILE   A HB   1 
ATOM   2811 H  HB   B ILE   A 1 131 ? 17.197 4.838   -5.374  0.40 14.94 ?  131  ILE   A HB   1 
ATOM   2812 H  HG12 A ILE   A 1 131 ? 18.094 3.730   -3.364  0.60 16.51 ?  131  ILE   A HG12 1 
ATOM   2813 H  HG12 B ILE   A 1 131 ? 17.758 3.370   -3.019  0.40 16.16 ?  131  ILE   A HG12 1 
ATOM   2814 H  HG13 A ILE   A 1 131 ? 19.027 3.686   -4.649  0.60 16.51 ?  131  ILE   A HG13 1 
ATOM   2815 H  HG13 B ILE   A 1 131 ? 18.719 3.418   -4.281  0.40 16.16 ?  131  ILE   A HG13 1 
ATOM   2816 H  HG21 A ILE   A 1 131 ? 16.338 6.074   -4.297  0.60 16.18 ?  131  ILE   A HG21 1 
ATOM   2817 H  HG21 B ILE   A 1 131 ? 16.225 5.951   -3.638  0.40 15.06 ?  131  ILE   A HG21 1 
ATOM   2818 H  HG22 A ILE   A 1 131 ? 15.226 5.122   -4.911  0.60 16.18 ?  131  ILE   A HG22 1 
ATOM   2819 H  HG22 B ILE   A 1 131 ? 15.052 5.181   -4.382  0.40 15.06 ?  131  ILE   A HG22 1 
ATOM   2820 H  HG23 A ILE   A 1 131 ? 15.872 4.780   -3.501  0.60 16.18 ?  131  ILE   A HG23 1 
ATOM   2821 H  HG23 B ILE   A 1 131 ? 15.651 4.599   -3.030  0.40 15.06 ?  131  ILE   A HG23 1 
ATOM   2822 H  HD11 A ILE   A 1 131 ? 19.813 5.374   -3.350  0.60 17.42 ?  131  ILE   A HD11 1 
ATOM   2823 H  HD11 B ILE   A 1 131 ? 19.609 4.813   -2.733  0.40 16.90 ?  131  ILE   A HD11 1 
ATOM   2824 H  HD12 A ILE   A 1 131 ? 19.089 6.067   -4.582  0.60 17.42 ?  131  ILE   A HD12 1 
ATOM   2825 H  HD12 B ILE   A 1 131 ? 19.015 5.735   -3.882  0.40 16.90 ?  131  ILE   A HD12 1 
ATOM   2826 H  HD13 A ILE   A 1 131 ? 18.359 5.989   -3.173  0.60 17.42 ?  131  ILE   A HD13 1 
ATOM   2827 H  HD13 B ILE   A 1 131 ? 18.218 5.551   -2.520  0.40 16.90 ?  131  ILE   A HD13 1 
ATOM   2828 N  N    A PHE   A 1 132 ? 17.958 0.979   -5.859  0.60 10.13 ?  132  PHE   A N    1 
ATOM   2829 N  N    B PHE   A 1 132 ? 17.650 1.051   -5.712  0.40 11.09 ?  132  PHE   A N    1 
ATOM   2830 C  CA   A PHE   A 1 132 ? 18.789 0.119   -6.693  0.60 10.49 ?  132  PHE   A CA   1 
ATOM   2831 C  CA   B PHE   A 1 132 ? 18.559 0.257   -6.530  0.40 11.19 ?  132  PHE   A CA   1 
ATOM   2832 C  C    A PHE   A 1 132 ? 17.982 -0.638  -7.745  0.60 11.49 ?  132  PHE   A C    1 
ATOM   2833 C  C    B PHE   A 1 132 ? 17.850 -0.453  -7.681  0.40 11.48 ?  132  PHE   A C    1 
ATOM   2834 O  O    A PHE   A 1 132 ? 18.576 -1.312  -8.591  0.60 12.19 ?  132  PHE   A O    1 
ATOM   2835 O  O    B PHE   A 1 132 ? 18.521 -0.902  -8.614  0.40 11.63 ?  132  PHE   A O    1 
ATOM   2836 C  CB   A PHE   A 1 132 ? 19.614 -0.856  -5.840  0.60 10.06 ?  132  PHE   A CB   1 
ATOM   2837 C  CB   B PHE   A 1 132 ? 19.320 -0.754  -5.664  0.40 11.34 ?  132  PHE   A CB   1 
ATOM   2838 C  CG   A PHE   A 1 132 ? 20.826 -0.232  -5.171  0.60 10.01 ?  132  PHE   A CG   1 
ATOM   2839 C  CG   B PHE   A 1 132 ? 20.560 -0.200  -5.000  0.40 11.26 ?  132  PHE   A CG   1 
ATOM   2840 C  CD1  A PHE   A 1 132 ? 20.692 0.809   -4.266  0.60 10.92 ?  132  PHE   A CD1  1 
ATOM   2841 C  CD1  B PHE   A 1 132 ? 20.466 0.702   -3.952  0.40 11.58 ?  132  PHE   A CD1  1 
ATOM   2842 C  CD2  A PHE   A 1 132 ? 22.099 -0.731  -5.417  0.60 11.14 ?  132  PHE   A CD2  1 
ATOM   2843 C  CD2  B PHE   A 1 132 ? 21.819 -0.619  -5.400  0.40 11.40 ?  132  PHE   A CD2  1 
ATOM   2844 C  CE1  A PHE   A 1 132 ? 21.809 1.362   -3.645  0.60 11.31 ?  132  PHE   A CE1  1 
ATOM   2845 C  CE1  B PHE   A 1 132 ? 21.606 1.194   -3.334  0.40 11.66 ?  132  PHE   A CE1  1 
ATOM   2846 C  CE2  A PHE   A 1 132 ? 23.214 -0.186  -4.795  0.60 11.71 ?  132  PHE   A CE2  1 
ATOM   2847 C  CE2  B PHE   A 1 132 ? 22.962 -0.133  -4.785  0.40 11.75 ?  132  PHE   A CE2  1 
ATOM   2848 C  CZ   A PHE   A 1 132 ? 23.065 0.862   -3.909  0.60 11.32 ?  132  PHE   A CZ   1 
ATOM   2849 C  CZ   B PHE   A 1 132 ? 22.854 0.777   -3.751  0.40 11.45 ?  132  PHE   A CZ   1 
ATOM   2850 H  H    A PHE   A 1 132 ? 17.776 0.656   -5.079  0.60 12.18 ?  132  PHE   A H    1 
ATOM   2851 H  H    B PHE   A 1 132 ? 17.414 0.677   -4.976  0.40 13.33 ?  132  PHE   A H    1 
ATOM   2852 H  HA   A PHE   A 1 132 ? 19.421 0.675   -7.166  0.60 12.61 ?  132  PHE   A HA   1 
ATOM   2853 H  HA   B PHE   A 1 132 ? 19.214 0.853   -6.922  0.40 13.45 ?  132  PHE   A HA   1 
ATOM   2854 H  HB2  A PHE   A 1 132 ? 19.050 -1.210  -5.138  0.60 12.10 ?  132  PHE   A HB2  1 
ATOM   2855 H  HB2  B PHE   A 1 132 ? 18.733 -1.069  -4.961  0.40 13.63 ?  132  PHE   A HB2  1 
ATOM   2856 H  HB3  A PHE   A 1 132 ? 19.931 -1.584  -6.405  0.60 12.10 ?  132  PHE   A HB3  1 
ATOM   2857 H  HB3  B PHE   A 1 132 ? 19.594 -1.496  -6.221  0.40 13.63 ?  132  PHE   A HB3  1 
ATOM   2858 H  HD1  A PHE   A 1 132 ? 19.851 1.150   -4.079  0.60 13.13 ?  132  PHE   A HD1  1 
ATOM   2859 H  HD1  B PHE   A 1 132 ? 19.632 0.989   -3.665  0.40 13.93 ?  132  PHE   A HD1  1 
ATOM   2860 H  HD2  A PHE   A 1 132 ? 22.211 -1.436  -6.016  0.60 13.39 ?  132  PHE   A HD2  1 
ATOM   2861 H  HD2  B PHE   A 1 132 ? 21.901 -1.229  -6.099  0.40 13.71 ?  132  PHE   A HD2  1 
ATOM   2862 H  HE1  A PHE   A 1 132 ? 21.709 2.068   -3.044  0.60 13.60 ?  132  PHE   A HE1  1 
ATOM   2863 H  HE1  B PHE   A 1 132 ? 21.532 1.804   -2.637  0.40 14.01 ?  132  PHE   A HE1  1 
ATOM   2864 H  HE2  A PHE   A 1 132 ? 24.061 -0.521  -4.983  0.60 14.07 ?  132  PHE   A HE2  1 
ATOM   2865 H  HE2  B PHE   A 1 132 ? 23.802 -0.416  -5.073  0.40 14.13 ?  132  PHE   A HE2  1 
ATOM   2866 H  HZ   A PHE   A 1 132 ? 23.814 1.234   -3.497  0.60 13.61 ?  132  PHE   A HZ   1 
ATOM   2867 H  HZ   B PHE   A 1 132 ? 23.620 1.106   -3.338  0.40 13.77 ?  132  PHE   A HZ   1 
ATOM   2868 N  N    A GLY   A 1 133 ? 16.652 -0.562  -7.704  0.60 12.03 ?  133  GLY   A N    1 
ATOM   2869 N  N    B GLY   A 1 133 ? 16.522 -0.579  -7.641  0.40 11.89 ?  133  GLY   A N    1 
ATOM   2870 C  CA   A GLY   A 1 133 ? 15.840 -0.923  -8.849  0.60 12.61 ?  133  GLY   A CA   1 
ATOM   2871 C  CA   B GLY   A 1 133 ? 15.752 -0.930  -8.817  0.40 12.31 ?  133  GLY   A CA   1 
ATOM   2872 C  C    A GLY   A 1 133 ? 15.508 -2.387  -9.038  0.60 12.76 ?  133  GLY   A C    1 
ATOM   2873 C  C    B GLY   A 1 133 ? 15.356 -2.387  -8.966  0.40 12.24 ?  133  GLY   A C    1 
ATOM   2874 O  O    A GLY   A 1 133 ? 14.939 -2.727  -10.082 0.60 13.48 ?  133  GLY   A O    1 
ATOM   2875 O  O    B GLY   A 1 133 ? 14.494 -2.680  -9.804  0.40 12.58 ?  133  GLY   A O    1 
ATOM   2876 H  H    A GLY   A 1 133 ? 16.195 -0.304  -7.018  0.60 14.47 ?  133  GLY   A H    1 
ATOM   2877 H  H    B GLY   A 1 133 ? 16.044 -0.462  -6.935  0.40 14.30 ?  133  GLY   A H    1 
ATOM   2878 H  HA2  A GLY   A 1 133 ? 14.999 -0.448  -8.791  0.60 15.16 ?  133  GLY   A HA2  1 
ATOM   2879 H  HA2  B GLY   A 1 133 ? 14.936 -0.410  -8.818  0.40 14.80 ?  133  GLY   A HA2  1 
ATOM   2880 H  HA3  A GLY   A 1 133 ? 16.295 -0.625  -9.650  0.60 15.16 ?  133  GLY   A HA3  1 
ATOM   2881 H  HA3  B GLY   A 1 133 ? 16.262 -0.682  -9.606  0.40 14.80 ?  133  GLY   A HA3  1 
ATOM   2882 N  N    A ALA   A 1 134 ? 15.833 -3.265  -8.089  0.60 12.26 ?  134  ALA   A N    1 
ATOM   2883 N  N    B ALA   A 1 134 ? 15.953 -3.310  -8.211  0.40 12.36 ?  134  ALA   A N    1 
ATOM   2884 C  CA   A ALA   A 1 134 ? 15.458 -4.665  -8.220  0.60 12.45 ?  134  ALA   A CA   1 
ATOM   2885 C  CA   B ALA   A 1 134 ? 15.638 -4.718  -8.409  0.40 12.71 ?  134  ALA   A CA   1 
ATOM   2886 C  C    A ALA   A 1 134 ? 14.121 -4.926  -7.537  0.60 12.57 ?  134  ALA   A C    1 
ATOM   2887 C  C    B ALA   A 1 134 ? 14.285 -5.073  -7.786  0.40 12.74 ?  134  ALA   A C    1 
ATOM   2888 O  O    A ALA   A 1 134 ? 13.647 -4.137  -6.716  0.60 13.58 ?  134  ALA   A O    1 
ATOM   2889 O  O    B ALA   A 1 134 ? 13.707 -4.312  -7.006  0.40 13.62 ?  134  ALA   A O    1 
ATOM   2890 C  CB   A ALA   A 1 134 ? 16.529 -5.584  -7.631  0.60 13.34 ?  134  ALA   A CB   1 
ATOM   2891 C  CB   B ALA   A 1 134 ? 16.744 -5.606  -7.837  0.40 13.36 ?  134  ALA   A CB   1 
ATOM   2892 H  H    A ALA   A 1 134 ? 16.274 -3.072  -7.370  0.60 14.74 ?  134  ALA   A H    1 
ATOM   2893 H  H    B ALA   A 1 134 ? 16.542 -3.146  -7.599  0.40 14.86 ?  134  ALA   A H    1 
ATOM   2894 H  HA   A ALA   A 1 134 ? 15.362 -4.877  -9.160  0.60 14.96 ?  134  ALA   A HA   1 
ATOM   2895 H  HA   B ALA   A 1 134 ? 15.583 -4.891  -9.361  0.40 15.28 ?  134  ALA   A HA   1 
ATOM   2896 H  HB1  A ALA   A 1 134 ? 16.253 -6.504  -7.754  0.60 16.04 ?  134  ALA   A HB1  1 
ATOM   2897 H  HB1  B ALA   A 1 134 ? 16.517 -6.534  -8.001  0.40 16.06 ?  134  ALA   A HB1  1 
ATOM   2898 H  HB2  A ALA   A 1 134 ? 17.368 -5.424  -8.093  0.60 16.04 ?  134  ALA   A HB2  1 
ATOM   2899 H  HB2  B ALA   A 1 134 ? 17.583 -5.389  -8.275  0.40 16.06 ?  134  ALA   A HB2  1 
ATOM   2900 H  HB3  A ALA   A 1 134 ? 16.629 -5.388  -6.687  0.60 16.04 ?  134  ALA   A HB3  1 
ATOM   2901 H  HB3  B ALA   A 1 134 ? 16.818 -5.446  -6.884  0.40 16.06 ?  134  ALA   A HB3  1 
ATOM   2902 N  N    A ASP   A 1 135 ? 13.515 -6.053  -7.895  0.60 13.10 ?  135  ASP   A N    1 
ATOM   2903 N  N    B ASP   A 1 135 ? 13.785 -6.255  -8.146  0.40 12.83 ?  135  ASP   A N    1 
ATOM   2904 C  CA   A ASP   A 1 135 ? 12.272 -6.496  -7.274  0.60 14.20 ?  135  ASP   A CA   1 
ATOM   2905 C  CA   B ASP   A 1 135 ? 12.528 -6.774  -7.600  0.40 13.49 ?  135  ASP   A CA   1 
ATOM   2906 C  C    A ASP   A 1 135 ? 12.552 -6.954  -5.846  0.60 13.61 ?  135  ASP   A C    1 
ATOM   2907 C  C    B ASP   A 1 135 ? 12.742 -7.176  -6.146  0.40 13.55 ?  135  ASP   A C    1 
ATOM   2908 O  O    A ASP   A 1 135 ? 13.296 -7.925  -5.658  0.60 13.45 ?  135  ASP   A O    1 
ATOM   2909 O  O    B ASP   A 1 135 ? 13.580 -8.045  -5.872  0.40 13.25 ?  135  ASP   A O    1 
ATOM   2910 C  CB   A ASP   A 1 135 ? 11.723 -7.663  -8.088  0.60 16.22 ?  135  ASP   A CB   1 
ATOM   2911 C  CB   B ASP   A 1 135 ? 12.090 -7.988  -8.425  0.40 14.97 ?  135  ASP   A CB   1 
ATOM   2912 C  CG   A ASP   A 1 135 ? 10.376 -8.157  -7.578  0.60 18.43 ?  135  ASP   A CG   1 
ATOM   2913 C  CG   B ASP   A 1 135 ? 10.880 -8.725  -7.838  0.40 16.29 ?  135  ASP   A CG   1 
ATOM   2914 O  OD1  A ASP   A 1 135 ? 9.904  -7.658  -6.530  0.60 18.64 ?  135  ASP   A OD1  1 
ATOM   2915 O  OD1  B ASP   A 1 135 ? 10.254 -8.232  -6.879  0.40 16.27 ?  135  ASP   A OD1  1 
ATOM   2916 O  OD2  A ASP   A 1 135 ? 9.776  -9.029  -8.243  0.60 20.41 -1 135  ASP   A OD2  1 
ATOM   2917 O  OD2  B ASP   A 1 135 ? 10.559 -9.819  -8.348  0.40 17.97 -1 135  ASP   A OD2  1 
ATOM   2918 H  H    A ASP   A 1 135 ? 13.802 -6.579  -8.507  0.60 15.75 ?  135  ASP   A H    1 
ATOM   2919 H  H    B ASP   A 1 135 ? 14.163 -6.780  -8.710  0.40 15.42 ?  135  ASP   A H    1 
ATOM   2920 H  HA   A ASP   A 1 135 ? 11.614 -5.778  -7.280  0.60 17.07 ?  135  ASP   A HA   1 
ATOM   2921 H  HA   B ASP   A 1 135 ? 11.845 -6.090  -7.661  0.40 16.22 ?  135  ASP   A HA   1 
ATOM   2922 H  HB2  A ASP   A 1 135 ? 11.597 -7.374  -9.004  0.60 19.49 ?  135  ASP   A HB2  1 
ATOM   2923 H  HB2  B ASP   A 1 135 ? 11.849 -7.689  -9.313  0.40 17.99 ?  135  ASP   A HB2  1 
ATOM   2924 H  HB3  A ASP   A 1 135 ? 12.373 -8.389  -8.061  0.60 19.49 ?  135  ASP   A HB3  1 
ATOM   2925 H  HB3  B ASP   A 1 135 ? 12.828 -8.613  -8.472  0.40 17.99 ?  135  ASP   A HB3  1 
ATOM   2926 N  N    A PRO   A 1 136 ? 12.005 -6.293  -4.821  0.60 13.29 ?  136  PRO   A N    1 
ATOM   2927 N  N    B PRO   A 1 136 ? 12.027 -6.578  -5.189  0.40 13.72 ?  136  PRO   A N    1 
ATOM   2928 C  CA   A PRO   A 1 136 ? 12.284 -6.729  -3.441  0.60 13.26 ?  136  PRO   A CA   1 
ATOM   2929 C  CA   B PRO   A 1 136 ? 12.268 -6.933  -3.780  0.40 13.69 ?  136  PRO   A CA   1 
ATOM   2930 C  C    A PRO   A 1 136 ? 11.848 -8.158  -3.138  0.60 12.79 ?  136  PRO   A C    1 
ATOM   2931 C  C    B PRO   A 1 136 ? 11.854 -8.351  -3.437  0.40 13.38 ?  136  PRO   A C    1 
ATOM   2932 O  O    A PRO   A 1 136 ? 12.423 -8.792  -2.244  0.60 11.90 ?  136  PRO   A O    1 
ATOM   2933 O  O    B PRO   A 1 136 ? 12.505 -8.993  -2.603  0.40 13.26 ?  136  PRO   A O    1 
ATOM   2934 C  CB   A PRO   A 1 136 ? 11.541 -5.690  -2.585  0.60 14.03 ?  136  PRO   A CB   1 
ATOM   2935 C  CB   B PRO   A 1 136 ? 11.447 -5.888  -3.014  0.40 13.89 ?  136  PRO   A CB   1 
ATOM   2936 C  CG   A PRO   A 1 136 ? 10.529 -5.083  -3.505  0.60 14.80 ?  136  PRO   A CG   1 
ATOM   2937 C  CG   B PRO   A 1 136 ? 10.349 -5.517  -3.962  0.40 14.30 ?  136  PRO   A CG   1 
ATOM   2938 C  CD   A PRO   A 1 136 ? 11.152 -5.091  -4.855  0.60 13.71 ?  136  PRO   A CD   1 
ATOM   2939 C  CD   B PRO   A 1 136 ? 10.960 -5.572  -5.333  0.40 14.07 ?  136  PRO   A CD   1 
ATOM   2940 H  HA   A PRO   A 1 136 ? 13.234 -6.645  -3.261  0.60 15.94 ?  136  PRO   A HA   1 
ATOM   2941 H  HA   B PRO   A 1 136 ? 13.211 -6.819  -3.560  0.40 16.46 ?  136  PRO   A HA   1 
ATOM   2942 H  HB2  A PRO   A 1 136 ? 11.105 -6.128  -1.839  0.60 16.86 ?  136  PRO   A HB2  1 
ATOM   2943 H  HB2  B PRO   A 1 136 ? 11.089 -6.285  -2.205  0.40 16.69 ?  136  PRO   A HB2  1 
ATOM   2944 H  HB3  A PRO   A 1 136 ? 12.164 -5.013  -2.269  0.60 16.86 ?  136  PRO   A HB3  1 
ATOM   2945 H  HB3  B PRO   A 1 136 ? 12.003 -5.121  -2.807  0.40 16.69 ?  136  PRO   A HB3  1 
ATOM   2946 H  HG2  A PRO   A 1 136 ? 9.728  -5.625  -3.508  0.60 17.79 ?  136  PRO   A HG2  1 
ATOM   2947 H  HG2  B PRO   A 1 136 ? 9.626  -6.157  -3.886  0.40 17.19 ?  136  PRO   A HG2  1 
ATOM   2948 H  HG3  A PRO   A 1 136 ? 10.332 -4.176  -3.225  0.60 17.79 ?  136  PRO   A HG3  1 
ATOM   2949 H  HG3  B PRO   A 1 136 ? 10.041 -4.621  -3.764  0.40 17.19 ?  136  PRO   A HG3  1 
ATOM   2950 H  HD2  A PRO   A 1 136 ? 10.466 -5.175  -5.538  0.60 16.48 ?  136  PRO   A HD2  1 
ATOM   2951 H  HD2  B PRO   A 1 136 ? 10.309 -5.875  -5.986  0.40 16.92 ?  136  PRO   A HD2  1 
ATOM   2952 H  HD3  A PRO   A 1 136 ? 11.688 -4.291  -4.989  0.60 16.48 ?  136  PRO   A HD3  1 
ATOM   2953 H  HD3  B PRO   A 1 136 ? 11.334 -4.710  -5.579  0.40 16.92 ?  136  PRO   A HD3  1 
ATOM   2954 N  N    A ILE   A 1 137 ? 10.842 -8.683  -3.844  0.60 13.51 ?  137  ILE   A N    1 
ATOM   2955 N  N    B ILE   A 1 137 ? 10.775 -8.856  -4.039  0.40 13.45 ?  137  ILE   A N    1 
ATOM   2956 C  CA   A ILE   A 1 137 ? 10.447 -10.076 -3.640  0.60 14.17 ?  137  ILE   A CA   1 
ATOM   2957 C  CA   B ILE   A 1 137 ? 10.407 -10.253 -3.832  0.40 13.91 ?  137  ILE   A CA   1 
ATOM   2958 C  C    A ILE   A 1 137 ? 11.579 -11.008 -4.061  0.60 13.76 ?  137  ILE   A C    1 
ATOM   2959 C  C    B ILE   A 1 137 ? 11.578 -11.151 -4.199  0.40 13.62 ?  137  ILE   A C    1 
ATOM   2960 O  O    A ILE   A 1 137 ? 11.900 -11.979 -3.365  0.60 14.06 ?  137  ILE   A O    1 
ATOM   2961 O  O    B ILE   A 1 137 ? 11.886 -12.122 -3.498  0.40 13.81 ?  137  ILE   A O    1 
ATOM   2962 C  CB   A ILE   A 1 137 ? 9.128  -10.381 -4.382  0.60 15.64 ?  137  ILE   A CB   1 
ATOM   2963 C  CB   B ILE   A 1 137 ? 9.143  -10.602 -4.641  0.40 15.14 ?  137  ILE   A CB   1 
ATOM   2964 C  CG1  A ILE   A 1 137 ? 7.954  -9.613  -3.756  0.60 16.79 ?  137  ILE   A CG1  1 
ATOM   2965 C  CG1  B ILE   A 1 137 ? 7.999  -9.640  -4.298  0.40 16.25 ?  137  ILE   A CG1  1 
ATOM   2966 C  CG2  A ILE   A 1 137 ? 8.846  -11.884 -4.384  0.60 16.54 ?  137  ILE   A CG2  1 
ATOM   2967 C  CG2  B ILE   A 1 137 ? 8.731  -12.044 -4.380  0.40 15.51 ?  137  ILE   A CG2  1 
ATOM   2968 C  CD1  A ILE   A 1 137 ? 6.652  -9.766  -4.511  0.60 17.96 ?  137  ILE   A CD1  1 
ATOM   2969 C  CD1  B ILE   A 1 137 ? 6.749  -9.850  -5.124  0.40 17.36 ?  137  ILE   A CD1  1 
ATOM   2970 H  H    A ILE   A 1 137 ? 10.389 -8.257  -4.436  0.60 16.24 ?  137  ILE   A H    1 
ATOM   2971 H  H    B ILE   A 1 137 ? 10.256 -8.421  -4.567  0.40 16.17 ?  137  ILE   A H    1 
ATOM   2972 H  HA   A ILE   A 1 137 ? 10.293 -10.215 -2.696  0.60 17.03 ?  137  ILE   A HA   1 
ATOM   2973 H  HA   B ILE   A 1 137 ? 10.209 -10.395 -2.894  0.40 16.71 ?  137  ILE   A HA   1 
ATOM   2974 H  HB   A ILE   A 1 137 ? 9.220  -10.085 -5.298  0.60 18.79 ?  137  ILE   A HB   1 
ATOM   2975 H  HB   B ILE   A 1 137 ? 9.346  -10.512 -5.585  0.40 18.19 ?  137  ILE   A HB   1 
ATOM   2976 H  HG12 A ILE   A 1 137 ? 7.808  -9.936  -2.853  0.60 20.17 ?  137  ILE   A HG12 1 
ATOM   2977 H  HG12 B ILE   A 1 137 ? 7.766  -9.758  -3.365  0.40 19.53 ?  137  ILE   A HG12 1 
ATOM   2978 H  HG13 A ILE   A 1 137 ? 8.171  -8.664  -3.732  0.60 20.17 ?  137  ILE   A HG13 1 
ATOM   2979 H  HG13 B ILE   A 1 137 ? 8.297  -8.729  -4.448  0.40 19.53 ?  137  ILE   A HG13 1 
ATOM   2980 H  HG21 A ILE   A 1 137 ? 7.998  -12.053 -4.819  0.60 19.88 ?  137  ILE   A HG21 1 
ATOM   2981 H  HG21 B ILE   A 1 137 ? 7.923  -12.239 -4.878  0.40 18.63 ?  137  ILE   A HG21 1 
ATOM   2982 H  HG22 A ILE   A 1 137 ? 9.547  -12.338 -4.871  0.60 19.88 ?  137  ILE   A HG22 1 
ATOM   2983 H  HG22 B ILE   A 1 137 ? 9.443  -12.635 -4.670  0.40 18.63 ?  137  ILE   A HG22 1 
ATOM   2984 H  HG23 A ILE   A 1 137 ? 8.816  -12.198 -3.468  0.60 19.88 ?  137  ILE   A HG23 1 
ATOM   2985 H  HG23 B ILE   A 1 137 ? 8.572  -12.157 -3.431  0.40 18.63 ?  137  ILE   A HG23 1 
ATOM   2986 H  HD11 A ILE   A 1 137 ? 5.965  -9.308  -4.014  0.60 21.58 ?  137  ILE   A HD11 1 
ATOM   2987 H  HD11 B ILE   A 1 137 ? 6.157  -9.094  -4.993  0.40 20.86 ?  137  ILE   A HD11 1 
ATOM   2988 H  HD12 A ILE   A 1 137 ? 6.748  -9.375  -5.396  0.60 21.58 ?  137  ILE   A HD12 1 
ATOM   2989 H  HD12 B ILE   A 1 137 ? 6.998  -9.919  -6.059  0.40 20.86 ?  137  ILE   A HD12 1 
ATOM   2990 H  HD13 A ILE   A 1 137 ? 6.423  -10.706 -4.587  0.60 21.58 ?  137  ILE   A HD13 1 
ATOM   2991 H  HD13 B ILE   A 1 137 ? 6.315  -10.667 -4.836  0.40 20.86 ?  137  ILE   A HD13 1 
ATOM   2992 N  N    A HIS   A 1 138 ? 12.200 -10.725 -5.209  0.60 13.89 ?  138  HIS   A N    1 
ATOM   2993 N  N    B HIS   A 1 138 ? 12.247 -10.835 -5.307  0.40 13.48 ?  138  HIS   A N    1 
ATOM   2994 C  CA   A HIS   A 1 138 ? 13.341 -11.515 -5.660  0.60 13.89 ?  138  HIS   A CA   1 
ATOM   2995 C  CA   B HIS   A 1 138 ? 13.429 -11.586 -5.705  0.40 13.47 ?  138  HIS   A CA   1 
ATOM   2996 C  C    A HIS   A 1 138 ? 14.511 -11.392 -4.691  0.60 13.07 ?  138  HIS   A C    1 
ATOM   2997 C  C    B HIS   A 1 138 ? 14.566 -11.403 -4.706  0.40 12.82 ?  138  HIS   A C    1 
ATOM   2998 O  O    A HIS   A 1 138 ? 15.164 -12.388 -4.360  0.60 13.51 ?  138  HIS   A O    1 
ATOM   2999 O  O    B HIS   A 1 138 ? 15.251 -12.373 -4.358  0.40 12.91 ?  138  HIS   A O    1 
ATOM   3000 C  CB   A HIS   A 1 138 ? 13.742 -11.074 -7.068  0.60 14.64 ?  138  HIS   A CB   1 
ATOM   3001 C  CB   B HIS   A 1 138 ? 13.852 -11.169 -7.111  0.40 14.45 ?  138  HIS   A CB   1 
ATOM   3002 C  CG   A HIS   A 1 138 ? 15.009 -11.701 -7.556  0.60 15.52 ?  138  HIS   A CG   1 
ATOM   3003 C  CG   B HIS   A 1 138 ? 15.135 -11.790 -7.560  0.40 15.44 ?  138  HIS   A CG   1 
ATOM   3004 N  ND1  A HIS   A 1 138 ? 15.132 -13.056 -7.780  0.60 16.63 ?  138  HIS   A ND1  1 
ATOM   3005 N  ND1  B HIS   A 1 138 ? 15.245 -13.127 -7.878  0.40 16.44 ?  138  HIS   A ND1  1 
ATOM   3006 C  CD2  A HIS   A 1 138 ? 16.212 -11.158 -7.857  0.60 15.76 ?  138  HIS   A CD2  1 
ATOM   3007 C  CD2  B HIS   A 1 138 ? 16.366 -11.258 -7.733  0.40 15.75 ?  138  HIS   A CD2  1 
ATOM   3008 C  CE1  A HIS   A 1 138 ? 16.355 -13.319 -8.203  0.60 16.63 ?  138  HIS   A CE1  1 
ATOM   3009 C  CE1  B HIS   A 1 138 ? 16.490 -13.389 -8.235  0.40 16.54 ?  138  HIS   A CE1  1 
ATOM   3010 N  NE2  A HIS   A 1 138 ? 17.031 -12.186 -8.259  0.60 16.08 ?  138  HIS   A NE2  1 
ATOM   3011 N  NE2  B HIS   A 1 138 ? 17.191 -12.272 -8.154  0.40 16.16 ?  138  HIS   A NE2  1 
ATOM   3012 H  H    A HIS   A 1 138 ? 11.979 -10.082 -5.740  0.60 16.70 ?  138  HIS   A H    1 
ATOM   3013 H  H    B HIS   A 1 138 ? 12.031 -10.196 -5.844  0.40 16.21 ?  138  HIS   A H    1 
ATOM   3014 H  HA   A HIS   A 1 138 ? 13.079 -12.447 -5.704  0.60 16.69 ?  138  HIS   A HA   1 
ATOM   3015 H  HA   B HIS   A 1 138 ? 13.201 -12.527 -5.734  0.40 16.19 ?  138  HIS   A HA   1 
ATOM   3016 H  HB2  A HIS   A 1 138 ? 13.033 -11.317 -7.689  0.60 17.60 ?  138  HIS   A HB2  1 
ATOM   3017 H  HB2  B HIS   A 1 138 ? 13.157 -11.434 -7.739  0.40 17.37 ?  138  HIS   A HB2  1 
ATOM   3018 H  HB3  A HIS   A 1 138 ? 13.866 -10.113 -7.075  0.60 17.60 ?  138  HIS   A HB3  1 
ATOM   3019 H  HB3  B HIS   A 1 138 ? 13.963 -10.207 -7.135  0.40 17.37 ?  138  HIS   A HB3  1 
ATOM   3020 H  HD1  A HIS   A 1 138 ? 14.510 -13.639 -7.666  0.60 19.98 ?  138  HIS   A HD1  1 
ATOM   3021 H  HD2  A HIS   A 1 138 ? 16.440 -10.259 -7.806  0.60 18.94 ?  138  HIS   A HD2  1 
ATOM   3022 H  HD2  B HIS   A 1 138 ? 16.604 -10.372 -7.593  0.40 18.93 ?  138  HIS   A HD2  1 
ATOM   3023 H  HE1  A HIS   A 1 138 ? 16.687 -14.161 -8.422  0.60 19.99 ?  138  HIS   A HE1  1 
ATOM   3024 H  HE1  B HIS   A 1 138 ? 16.816 -14.219 -8.496  0.40 19.87 ?  138  HIS   A HE1  1 
ATOM   3025 H  HE2  B HIS   A 1 138 ? 18.026 -12.192 -8.335  0.40 19.42 ?  138  HIS   A HE2  1 
ATOM   3026 N  N    . SER   A 1 139 ? 14.785 -10.177 -4.222  1.00 12.72 ?  139  SER   A N    1 
ATOM   3027 C  CA   . SER   A 1 139 ? 15.859 -9.979  -3.260  1.00 12.37 ?  139  SER   A CA   1 
ATOM   3028 C  C    . SER   A 1 139 ? 15.646 -10.819 -2.006  1.00 12.03 ?  139  SER   A C    1 
ATOM   3029 O  O    . SER   A 1 139 ? 16.597 -11.415 -1.485  1.00 12.04 ?  139  SER   A O    1 
ATOM   3030 C  CB   . SER   A 1 139 ? 15.992 -8.502  -2.911  1.00 12.25 ?  139  SER   A CB   1 
ATOM   3031 O  OG   . SER   A 1 139 ? 17.076 -8.333  -2.025  1.00 12.38 ?  139  SER   A OG   1 
ATOM   3032 H  H    A SER   A 1 139 ? 14.360 -9.462  -4.440  0.60 15.29 ?  139  SER   A H    1 
ATOM   3033 H  H    B SER   A 1 139 ? 14.339 -9.472  -4.431  0.40 15.29 ?  139  SER   A H    1 
ATOM   3034 H  HA   . SER   A 1 139 ? 16.692 -10.261 -3.663  1.00 14.87 ?  139  SER   A HA   1 
ATOM   3035 H  HB2  . SER   A 1 139 ? 16.153 -7.988  -3.721  1.00 14.73 ?  139  SER   A HB2  1 
ATOM   3036 H  HB3  . SER   A 1 139 ? 15.177 -8.193  -2.479  1.00 14.73 ?  139  SER   A HB3  1 
ATOM   3037 H  HG   . SER   A 1 139 ? 17.798 -8.552  -2.410  1.00 14.88 ?  139  SER   A HG   1 
ATOM   3038 N  N    . LEU   A 1 140 ? 14.410 -10.876 -1.501  1.00 12.05 ?  140  LEU   A N    1 
ATOM   3039 C  CA   . LEU   A 1 140 ? 14.146 -11.691 -0.320  1.00 12.19 ?  140  LEU   A CA   1 
ATOM   3040 C  C    . LEU   A 1 140 ? 14.410 -13.170 -0.602  1.00 12.09 ?  140  LEU   A C    1 
ATOM   3041 O  O    . LEU   A 1 140 ? 14.954 -13.888 0.247   1.00 12.73 ?  140  LEU   A O    1 
ATOM   3042 C  CB   . LEU   A 1 140 ? 12.712 -11.462 0.156   1.00 12.31 ?  140  LEU   A CB   1 
ATOM   3043 C  CG   . LEU   A 1 140 ? 12.259 -12.326 1.330   1.00 12.95 ?  140  LEU   A CG   1 
ATOM   3044 C  CD1  . LEU   A 1 140 ? 13.172 -12.157 2.540   1.00 12.94 ?  140  LEU   A CD1  1 
ATOM   3045 C  CD2  . LEU   A 1 140 ? 10.809 -12.004 1.693   1.00 13.86 ?  140  LEU   A CD2  1 
ATOM   3046 H  H    . LEU   A 1 140 ? 13.730 -10.453 -1.808  1.00 14.49 ?  140  LEU   A H    1 
ATOM   3047 H  HA   . LEU   A 1 140 ? 14.742 -11.421 0.395   1.00 14.66 ?  140  LEU   A HA   1 
ATOM   3048 H  HB2  . LEU   A 1 140 ? 12.622 -10.540 0.430   1.00 14.80 ?  140  LEU   A HB2  1 
ATOM   3049 H  HB3  . LEU   A 1 140 ? 12.111 -11.645 -0.582  1.00 14.80 ?  140  LEU   A HB3  1 
ATOM   3050 H  HG   . LEU   A 1 140 ? 12.283 -13.261 1.066   1.00 15.57 ?  140  LEU   A HG   1 
ATOM   3051 H  HD11 . LEU   A 1 140 ? 12.799 -12.652 3.289   1.00 15.56 ?  140  LEU   A HD11 1 
ATOM   3052 H  HD12 . LEU   A 1 140 ? 14.049 -12.514 2.320   1.00 15.56 ?  140  LEU   A HD12 1 
ATOM   3053 H  HD13 . LEU   A 1 140 ? 13.237 -11.220 2.759   1.00 15.56 ?  140  LEU   A HD13 1 
ATOM   3054 H  HD21 . LEU   A 1 140 ? 10.536 -12.569 2.438   1.00 16.66 ?  140  LEU   A HD21 1 
ATOM   3055 H  HD22 . LEU   A 1 140 ? 10.746 -11.072 1.947   1.00 16.66 ?  140  LEU   A HD22 1 
ATOM   3056 H  HD23 . LEU   A 1 140 ? 10.242 -12.180 0.925   1.00 16.66 ?  140  LEU   A HD23 1 
ATOM   3057 N  N    . ARG   A 1 141 ? 14.011 -13.645 -1.785  1.00 12.71 ?  141  ARG   A N    1 
ATOM   3058 C  CA   . ARG   A 1 141 ? 14.244 -15.037 -2.154  1.00 13.74 ?  141  ARG   A CA   1 
ATOM   3059 C  C    . ARG   A 1 141 ? 15.737 -15.346 -2.187  1.00 12.83 ?  141  ARG   A C    1 
ATOM   3060 O  O    . ARG   A 1 141 ? 16.188 -16.363 -1.644  1.00 12.79 ?  141  ARG   A O    1 
ATOM   3061 C  CB   . ARG   A 1 141 ? 13.608 -15.291 -3.521  1.00 15.67 ?  141  ARG   A CB   1 
ATOM   3062 C  CG   . ARG   A 1 141 ? 13.597 -16.728 -3.970  1.00 18.80 ?  141  ARG   A CG   1 
ATOM   3063 C  CD   . ARG   A 1 141 ? 12.559 -17.497 -3.220  1.00 21.19 ?  141  ARG   A CD   1 
ATOM   3064 N  NE   . ARG   A 1 141 ? 13.167 -18.322 -2.192  1.00 22.08 ?  141  ARG   A NE   1 
ATOM   3065 C  CZ   . ARG   A 1 141 ? 12.493 -18.894 -1.204  1.00 23.03 ?  141  ARG   A CZ   1 
ATOM   3066 N  NH1  . ARG   A 1 141 ? 11.207 -18.647 -1.011  1.00 22.77 ?  141  ARG   A NH1  1 
ATOM   3067 N  NH2  . ARG   A 1 141 ? 13.125 -19.730 -0.385  1.00 23.94 ?  141  ARG   A NH2  1 
ATOM   3068 H  H    . ARG   A 1 141 ? 13.612 -13.181 -2.390  1.00 15.28 ?  141  ARG   A H    1 
ATOM   3069 H  HA   . ARG   A 1 141 ? 13.825 -15.621 -1.505  1.00 16.52 ?  141  ARG   A HA   1 
ATOM   3070 H  HB2  . ARG   A 1 141 ? 12.693 -14.975 -3.499  1.00 18.83 ?  141  ARG   A HB2  1 
ATOM   3071 H  HB3  . ARG   A 1 141 ? 14.106 -14.782 -4.184  1.00 18.83 ?  141  ARG   A HB3  1 
ATOM   3072 H  HG2  . ARG   A 1 141 ? 13.392 -16.769 -4.919  1.00 22.59 ?  141  ARG   A HG2  1 
ATOM   3073 H  HG3  . ARG   A 1 141 ? 14.467 -17.131 -3.800  1.00 22.59 ?  141  ARG   A HG3  1 
ATOM   3074 H  HD2  . ARG   A 1 141 ? 11.947 -16.881 -2.784  1.00 25.46 ?  141  ARG   A HD2  1 
ATOM   3075 H  HD3  . ARG   A 1 141 ? 12.071 -18.068 -3.837  1.00 25.46 ?  141  ARG   A HD3  1 
ATOM   3076 H  HE   . ARG   A 1 141 ? 13.986 -18.554 -2.298  1.00 26.52 ?  141  ARG   A HE   1 
ATOM   3077 H  HH11 . ARG   A 1 141 ? 10.779 -18.121 -1.543  1.00 27.35 ?  141  ARG   A HH11 1 
ATOM   3078 H  HH12 . ARG   A 1 141 ? 10.785 -19.029 -0.363  1.00 27.35 ?  141  ARG   A HH12 1 
ATOM   3079 H  HH21 . ARG   A 1 141 ? 13.959 -19.898 -0.502  1.00 28.75 ?  141  ARG   A HH21 1 
ATOM   3080 H  HH22 . ARG   A 1 141 ? 12.700 -20.101 0.266   1.00 28.75 ?  141  ARG   A HH22 1 
ATOM   3081 N  N    . VAL   A 1 142 ? 16.525 -14.477 -2.826  1.00 12.13 ?  142  VAL   A N    1 
ATOM   3082 C  CA   . VAL   A 1 142 ? 17.968 -14.696 -2.870  1.00 12.12 ?  142  VAL   A CA   1 
ATOM   3083 C  C    . VAL   A 1 142 ? 18.551 -14.676 -1.464  1.00 11.43 ?  142  VAL   A C    1 
ATOM   3084 O  O    . VAL   A 1 142 ? 19.415 -15.493 -1.125  1.00 11.77 ?  142  VAL   A O    1 
ATOM   3085 C  CB   . VAL   A 1 142 ? 18.654 -13.673 -3.795  1.00 12.17 ?  142  VAL   A CB   1 
ATOM   3086 C  CG1  . VAL   A 1 142 ? 20.163 -13.876 -3.773  1.00 12.20 ?  142  VAL   A CG1  1 
ATOM   3087 C  CG2  . VAL   A 1 142 ? 18.136 -13.807 -5.217  1.00 13.09 ?  142  VAL   A CG2  1 
ATOM   3088 H  H    . VAL   A 1 142 ? 16.257 -13.759 -3.229  1.00 14.58 ?  142  VAL   A H    1 
ATOM   3089 H  HA   . VAL   A 1 142 ? 18.136 -15.568 -3.244  1.00 14.57 ?  142  VAL   A HA   1 
ATOM   3090 H  HB   . VAL   A 1 142 ? 18.468 -12.767 -3.484  1.00 14.63 ?  142  VAL   A HB   1 
ATOM   3091 H  HG11 . VAL   A 1 142 ? 20.562 -13.378 -4.507  1.00 14.66 ?  142  VAL   A HG11 1 
ATOM   3092 H  HG12 . VAL   A 1 142 ? 20.519 -13.545 -2.929  1.00 14.66 ?  142  VAL   A HG12 1 
ATOM   3093 H  HG13 . VAL   A 1 142 ? 20.356 -14.817 -3.868  1.00 14.66 ?  142  VAL   A HG13 1 
ATOM   3094 H  HG21 . VAL   A 1 142 ? 18.593 -13.160 -5.780  1.00 15.73 ?  142  VAL   A HG21 1 
ATOM   3095 H  HG22 . VAL   A 1 142 ? 18.321 -14.705 -5.528  1.00 15.73 ?  142  VAL   A HG22 1 
ATOM   3096 H  HG23 . VAL   A 1 142 ? 17.186 -13.637 -5.220  1.00 15.73 ?  142  VAL   A HG23 1 
ATOM   3097 N  N    . CYS   A 1 143 ? 18.088 -13.753 -0.622  1.00 11.41 ?  143  CYS   A N    1 
ATOM   3098 C  CA   . CYS   A 1 143 ? 18.558 -13.708 0.756   1.00 11.41 ?  143  CYS   A CA   1 
ATOM   3099 C  C    . CYS   A 1 143 ? 18.339 -15.051 1.445   1.00 11.46 ?  143  CYS   A C    1 
ATOM   3100 O  O    . CYS   A 1 143 ? 19.265 -15.636 2.014   1.00 11.43 ?  143  CYS   A O    1 
ATOM   3101 C  CB   . CYS   A 1 143 ? 17.825 -12.599 1.506   1.00 11.68 ?  143  CYS   A CB   1 
ATOM   3102 S  SG   . CYS   A 1 143 ? 18.332 -12.419 3.224   1.00 12.24 ?  143  CYS   A SG   1 
ATOM   3103 H  H    . CYS   A 1 143 ? 17.510 -13.152 -0.826  1.00 13.72 ?  143  CYS   A H    1 
ATOM   3104 H  HA   . CYS   A 1 143 ? 19.503 -13.518 0.769   1.00 13.71 ?  143  CYS   A HA   1 
ATOM   3105 H  HB2  . CYS   A 1 143 ? 17.989 -11.758 1.057   1.00 14.04 ?  143  CYS   A HB2  1 
ATOM   3106 H  HB3  . CYS   A 1 143 ? 16.876 -12.793 1.499   1.00 14.04 ?  143  CYS   A HB3  1 
ATOM   3107 H  HG   . CYS   A 1 143 ? 17.774 -11.467 3.688   1.00 14.71 ?  143  CYS   A HG   1 
ATOM   3108 N  N    . VAL   A 1 144 ? 17.109 -15.554 1.402   1.00 12.12 ?  144  VAL   A N    1 
ATOM   3109 C  CA   . VAL   A 1 144 ? 16.777 -16.784 2.110   1.00 13.42 ?  144  VAL   A CA   1 
ATOM   3110 C  C    . VAL   A 1 144 ? 17.576 -17.957 1.569   1.00 12.93 ?  144  VAL   A C    1 
ATOM   3111 O  O    . VAL   A 1 144 ? 17.946 -18.871 2.316   1.00 13.50 ?  144  VAL   A O    1 
ATOM   3112 C  CB   . VAL   A 1 144 ? 15.258 -17.019 2.016   1.00 16.46 ?  144  VAL   A CB   1 
ATOM   3113 C  CG1  . VAL   A 1 144 ? 14.902 -18.447 2.366   1.00 18.57 ?  144  VAL   A CG1  1 
ATOM   3114 C  CG2  . VAL   A 1 144 ? 14.524 -16.011 2.901   1.00 16.54 ?  144  VAL   A CG2  1 
ATOM   3115 H  H    . VAL   A 1 144 ? 16.444 -15.200 0.974   1.00 14.57 ?  144  VAL   A H    1 
ATOM   3116 H  HA   . VAL   A 1 144 ? 16.998 -16.678 3.044   1.00 16.13 ?  144  VAL   A HA   1 
ATOM   3117 H  HB   . VAL   A 1 144 ? 14.971 -16.861 1.101   1.00 19.77 ?  144  VAL   A HB   1 
ATOM   3118 H  HG11 . VAL   A 1 144 ? 13.951 -18.496 2.564   1.00 22.31 ?  144  VAL   A HG11 1 
ATOM   3119 H  HG12 . VAL   A 1 144 ? 15.107 -19.021 1.612   1.00 22.31 ?  144  VAL   A HG12 1 
ATOM   3120 H  HG13 . VAL   A 1 144 ? 15.412 -18.718 3.143   1.00 22.31 ?  144  VAL   A HG13 1 
ATOM   3121 H  HG21 . VAL   A 1 144 ? 13.566 -16.166 2.837   1.00 19.88 ?  144  VAL   A HG21 1 
ATOM   3122 H  HG22 . VAL   A 1 144 ? 14.814 -16.121 3.818   1.00 19.88 ?  144  VAL   A HG22 1 
ATOM   3123 H  HG23 . VAL   A 1 144 ? 14.727 -15.110 2.595   1.00 19.88 ?  144  VAL   A HG23 1 
ATOM   3124 N  N    . ASP   A 1 145 ? 17.837 -17.966 0.266   1.00 13.01 ?  145  ASP   A N    1 
ATOM   3125 C  CA   . ASP   A 1 145 ? 18.537 -19.071 -0.376  1.00 13.59 ?  145  ASP   A CA   1 
ATOM   3126 C  C    . ASP   A 1 145 ? 20.058 -18.926 -0.355  1.00 13.18 ?  145  ASP   A C    1 
ATOM   3127 O  O    . ASP   A 1 145 ? 20.755 -19.824 -0.844  1.00 15.20 ?  145  ASP   A O    1 
ATOM   3128 C  CB   . ASP   A 1 145 ? 18.074 -19.215 -1.825  1.00 15.12 ?  145  ASP   A CB   1 
ATOM   3129 C  CG   . ASP   A 1 145 ? 16.627 -19.656 -1.938  1.00 17.35 ?  145  ASP   A CG   1 
ATOM   3130 O  OD1  . ASP   A 1 145 ? 16.072 -20.202 -0.958  1.00 17.86 ?  145  ASP   A OD1  1 
ATOM   3131 O  OD2  . ASP   A 1 145 ? 16.046 -19.456 -3.020  1.00 18.90 -1 145  ASP   A OD2  1 
ATOM   3132 H  H    . ASP   A 1 145 ? 17.594 -17.343 -0.278  1.00 15.64 ?  145  ASP   A H    1 
ATOM   3133 H  HA   . ASP   A 1 145 ? 18.306 -19.892 0.086   1.00 16.33 ?  145  ASP   A HA   1 
ATOM   3134 H  HB2  . ASP   A 1 145 ? 18.165 -18.362 -2.274  1.00 18.17 ?  145  ASP   A HB2  1 
ATOM   3135 H  HB3  . ASP   A 1 145 ? 18.616 -19.887 -2.264  1.00 18.17 ?  145  ASP   A HB3  1 
ATOM   3136 N  N    . THR   A 1 146 ? 20.590 -17.841 0.196   1.00 11.89 ?  146  THR   A N    1 
ATOM   3137 C  CA   . THR   A 1 146 ? 22.031 -17.595 0.200   1.00 10.96 ?  146  THR   A CA   1 
ATOM   3138 C  C    . THR   A 1 146 ? 22.601 -17.415 1.593   1.00 10.86 ?  146  THR   A C    1 
ATOM   3139 O  O    . THR   A 1 146 ? 23.681 -17.944 1.891   1.00 11.94 ?  146  THR   A O    1 
ATOM   3140 C  CB   . THR   A 1 146 ? 22.350 -16.346 -0.642  1.00 11.13 ?  146  THR   A CB   1 
ATOM   3141 O  OG1  . THR   A 1 146 ? 21.816 -16.510 -1.958  1.00 11.80 ?  146  THR   A OG1  1 
ATOM   3142 C  CG2  . THR   A 1 146 ? 23.852 -16.111 -0.732  1.00 11.84 ?  146  THR   A CG2  1 
ATOM   3143 H  H    . THR   A 1 146 ? 20.132 -17.218 0.572   1.00 14.29 ?  146  THR   A H    1 
ATOM   3144 H  HA   . THR   A 1 146 ? 22.482 -18.349 -0.205  1.00 13.17 ?  146  THR   A HA   1 
ATOM   3145 H  HB   . THR   A 1 146 ? 21.950 -15.567 -0.231  1.00 13.38 ?  146  THR   A HB   1 
ATOM   3146 H  HG1  . THR   A 1 146 ? 20.981 -16.587 -1.924  1.00 14.18 ?  146  THR   A HG1  1 
ATOM   3147 H  HG21 . THR   A 1 146 ? 24.044 -15.455 -1.417  1.00 14.23 ?  146  THR   A HG21 1 
ATOM   3148 H  HG22 . THR   A 1 146 ? 24.189 -15.791 0.118   1.00 14.23 ?  146  THR   A HG22 1 
ATOM   3149 H  HG23 . THR   A 1 146 ? 24.302 -16.942 -0.959  1.00 14.23 ?  146  THR   A HG23 1 
ATOM   3150 N  N    . VAL   A 1 147 ? 21.931 -16.637 2.435   1.00 11.18 ?  147  VAL   A N    1 
ATOM   3151 C  CA   . VAL   A 1 147 ? 22.432 -16.343 3.768   1.00 10.90 ?  147  VAL   A CA   1 
ATOM   3152 C  C    . VAL   A 1 147 ? 22.118 -17.514 4.685   1.00 11.50 ?  147  VAL   A C    1 
ATOM   3153 O  O    . VAL   A 1 147 ? 20.975 -17.983 4.749   1.00 12.22 ?  147  VAL   A O    1 
ATOM   3154 C  CB   . VAL   A 1 147 ? 21.821 -15.039 4.302   1.00 11.22 ?  147  VAL   A CB   1 
ATOM   3155 C  CG1  . VAL   A 1 147 ? 22.386 -14.733 5.664   1.00 12.44 ?  147  VAL   A CG1  1 
ATOM   3156 C  CG2  . VAL   A 1 147 ? 22.062 -13.888 3.336   1.00 11.45 ?  147  VAL   A CG2  1 
ATOM   3157 H  H    . VAL   A 1 147 ? 21.169 -16.267 2.259   1.00 13.44 ?  147  VAL   A H    1 
ATOM   3158 H  HA   . VAL   A 1 147 ? 23.393 -16.231 3.727   1.00 13.11 ?  147  VAL   A HA   1 
ATOM   3159 H  HB   . VAL   A 1 147 ? 20.864 -15.152 4.400   1.00 13.49 ?  147  VAL   A HB   1 
ATOM   3160 H  HG11 . VAL   A 1 147 ? 22.154 -13.828 5.910   1.00 14.96 ?  147  VAL   A HG11 1 
ATOM   3161 H  HG12 . VAL   A 1 147 ? 22.012 -15.357 6.310   1.00 14.96 ?  147  VAL   A HG12 1 
ATOM   3162 H  HG13 . VAL   A 1 147 ? 23.352 -14.832 5.635   1.00 14.96 ?  147  VAL   A HG13 1 
ATOM   3163 H  HG21 . VAL   A 1 147 ? 21.735 -13.065 3.739   1.00 13.76 ?  147  VAL   A HG21 1 
ATOM   3164 H  HG22 . VAL   A 1 147 ? 23.010 -13.816 3.160   1.00 13.76 ?  147  VAL   A HG22 1 
ATOM   3165 H  HG23 . VAL   A 1 147 ? 21.580 -14.063 2.513   1.00 13.76 ?  147  VAL   A HG23 1 
ATOM   3166 N  N    . ARG   A 1 148 ? 23.146 -17.994 5.384   1.00 11.88 ?  148  ARG   A N    1 
ATOM   3167 C  CA   . ARG   A 1 148 ? 23.019 -19.072 6.348   1.00 12.11 ?  148  ARG   A CA   1 
ATOM   3168 C  C    . ARG   A 1 148 ? 23.158 -18.597 7.784   1.00 12.22 ?  148  ARG   A C    1 
ATOM   3169 O  O    . ARG   A 1 148 ? 22.762 -19.321 8.705   1.00 13.90 ?  148  ARG   A O    1 
ATOM   3170 C  CB   . ARG   A 1 148 ? 24.055 -20.167 6.057   1.00 12.69 ?  148  ARG   A CB   1 
ATOM   3171 C  CG   . ARG   A 1 148 ? 23.877 -20.804 4.691   1.00 13.77 ?  148  ARG   A CG   1 
ATOM   3172 C  CD   . ARG   A 1 148 ? 24.957 -21.832 4.385   1.00 14.71 ?  148  ARG   A CD   1 
ATOM   3173 N  NE   . ARG   A 1 148 ? 26.292 -21.247 4.403   1.00 14.44 ?  148  ARG   A NE   1 
ATOM   3174 C  CZ   . ARG   A 1 148 ? 26.796 -20.507 3.425   1.00 13.95 ?  148  ARG   A CZ   1 
ATOM   3175 N  NH1  . ARG   A 1 148 ? 26.115 -20.267 2.316   1.00 14.42 ?  148  ARG   A NH1  1 
ATOM   3176 N  NH2  . ARG   A 1 148 ? 28.018 -19.992 3.561   1.00 14.48 ?  148  ARG   A NH2  1 
ATOM   3177 H  H    . ARG   A 1 148 ? 23.955 -17.694 5.303   1.00 14.28 ?  148  ARG   A H    1 
ATOM   3178 H  HA   . ARG   A 1 148 ? 22.142 -19.463 6.251   1.00 14.55 ?  148  ARG   A HA   1 
ATOM   3179 H  HB2  . ARG   A 1 148 ? 24.942 -19.790 6.094   1.00 15.25 ?  148  ARG   A HB2  1 
ATOM   3180 H  HB3  . ARG   A 1 148 ? 23.959 -20.871 6.720   1.00 15.25 ?  148  ARG   A HB3  1 
ATOM   3181 H  HG2  . ARG   A 1 148 ? 23.014 -21.249 4.659   1.00 16.55 ?  148  ARG   A HG2  1 
ATOM   3182 H  HG3  . ARG   A 1 148 ? 23.916 -20.109 4.014   1.00 16.55 ?  148  ARG   A HG3  1 
ATOM   3183 H  HD2  . ARG   A 1 148 ? 24.930 -22.533 5.053   1.00 17.68 ?  148  ARG   A HD2  1 
ATOM   3184 H  HD3  . ARG   A 1 148 ? 24.801 -22.207 3.502   1.00 17.68 ?  148  ARG   A HD3  1 
ATOM   3185 H  HE   . ARG   A 1 148 ? 26.788 -21.393 5.085   1.00 17.35 ?  148  ARG   A HE   1 
ATOM   3186 H  HH11 . ARG   A 1 148 ? 25.327 -20.589 2.213   1.00 17.33 ?  148  ARG   A HH11 1 
ATOM   3187 H  HH12 . ARG   A 1 148 ? 26.464 -19.780 1.694   1.00 17.33 ?  148  ARG   A HH12 1 
ATOM   3188 H  HH21 . ARG   A 1 148 ? 28.468 -20.135 4.275   1.00 17.40 ?  148  ARG   A HH21 1 
ATOM   3189 H  HH22 . ARG   A 1 148 ? 28.354 -19.504 2.931   1.00 17.40 ?  148  ARG   A HH22 1 
ATOM   3190 N  N    . THR   A 1 149 ? 23.710 -17.406 7.992   1.00 12.22 ?  149  THR   A N    1 
ATOM   3191 C  CA   . THR   A 1 149 ? 23.800 -16.818 9.312   1.00 12.41 ?  149  THR   A CA   1 
ATOM   3192 C  C    . THR   A 1 149 ? 22.476 -16.123 9.636   1.00 12.04 ?  149  THR   A C    1 
ATOM   3193 O  O    . THR   A 1 149 ? 21.531 -16.123 8.840   1.00 12.62 ?  149  THR   A O    1 
ATOM   3194 C  CB   . THR   A 1 149 ? 25.001 -15.879 9.368   1.00 12.74 ?  149  THR   A CB   1 
ATOM   3195 O  OG1  . THR   A 1 149 ? 24.863 -14.936 8.306   1.00 12.84 ?  149  THR   A OG1  1 
ATOM   3196 C  CG2  . THR   A 1 149 ? 26.314 -16.667 9.227   1.00 13.48 ?  149  THR   A CG2  1 
ATOM   3197 H  H    . THR   A 1 149 ? 24.052 -16.915 7.368   1.00 14.69 ?  149  THR   A H    1 
ATOM   3198 H  HA   . THR   A 1 149 ? 23.933 -17.523 9.960   1.00 14.92 ?  149  THR   A HA   1 
ATOM   3199 H  HB   . THR   A 1 149 ? 25.005 -15.418 10.218  1.00 15.32 ?  149  THR   A HB   1 
ATOM   3200 H  HG1  . THR   A 1 149 ? 25.516 -14.401 8.310   1.00 15.44 ?  149  THR   A HG1  1 
ATOM   3201 H  HG21 . THR   A 1 149 ? 27.072 -16.064 9.280   1.00 16.20 ?  149  THR   A HG21 1 
ATOM   3202 H  HG22 . THR   A 1 149 ? 26.389 -17.327 9.937   1.00 16.20 ?  149  THR   A HG22 1 
ATOM   3203 H  HG23 . THR   A 1 149 ? 26.340 -17.129 8.371   1.00 16.20 ?  149  THR   A HG23 1 
ATOM   3204 N  N    . ASN   A 1 150 ? 22.371 -15.573 10.838  1.00 12.25 ?  150  ASN   A N    1 
ATOM   3205 C  CA   . ASN   A 1 150 ? 21.093 -15.067 11.343  1.00 12.68 ?  150  ASN   A CA   1 
ATOM   3206 C  C    . ASN   A 1 150 ? 20.901 -13.624 10.893  1.00 12.17 ?  150  ASN   A C    1 
ATOM   3207 O  O    . ASN   A 1 150 ? 21.641 -12.727 11.316  1.00 13.47 ?  150  ASN   A O    1 
ATOM   3208 C  CB   . ASN   A 1 150 ? 21.058 -15.177 12.861  1.00 15.05 ?  150  ASN   A CB   1 
ATOM   3209 C  CG   . ASN   A 1 150 ? 20.905 -16.602 13.326  1.00 19.38 ?  150  ASN   A CG   1 
ATOM   3210 O  OD1  . ASN   A 1 150 ? 20.308 -17.425 12.634  1.00 20.90 ?  150  ASN   A OD1  1 
ATOM   3211 N  ND2  . ASN   A 1 150 ? 21.453 -16.910 14.495  1.00 21.73 ?  150  ASN   A ND2  1 
ATOM   3212 H  H    . ASN   A 1 150 ? 23.027 -15.482 11.383  1.00 14.73 ?  150  ASN   A H    1 
ATOM   3213 H  HA   . ASN   A 1 150 ? 20.370 -15.602 10.980  1.00 15.25 ?  150  ASN   A HA   1 
ATOM   3214 H  HB2  . ASN   A 1 150 ? 21.886 -14.831 13.226  1.00 18.09 ?  150  ASN   A HB2  1 
ATOM   3215 H  HB3  . ASN   A 1 150 ? 20.304 -14.670 13.200  1.00 18.09 ?  150  ASN   A HB3  1 
ATOM   3216 H  HD21 . ASN   A 1 150 ? 21.394 -17.713 14.806  1.00 26.10 ?  150  ASN   A HD21 1 
ATOM   3217 H  HD22 . ASN   A 1 150 ? 21.866 -16.308 14.952  1.00 26.10 ?  150  ASN   A HD22 1 
ATOM   3218 N  N    . VAL   A 1 151 ? 19.908 -13.393 10.045  1.00 11.82 ?  151  VAL   A N    1 
ATOM   3219 C  CA   . VAL   A 1 151 ? 19.685 -12.082 9.459   1.00 11.75 ?  151  VAL   A CA   1 
ATOM   3220 C  C    . VAL   A 1 151 ? 18.302 -11.568 9.844   1.00 11.68 ?  151  VAL   A C    1 
ATOM   3221 O  O    . VAL   A 1 151 ? 17.292 -12.276 9.706   1.00 12.78 ?  151  VAL   A O    1 
ATOM   3222 C  CB   . VAL   A 1 151 ? 19.958 -12.060 7.939   1.00 12.98 ?  151  VAL   A CB   1 
ATOM   3223 C  CG1  . VAL   A 1 151 ? 19.124 -13.068 7.189   1.00 14.10 ?  151  VAL   A CG1  1 
ATOM   3224 C  CG2  . VAL   A 1 151 ? 19.762 -10.651 7.379   1.00 13.32 ?  151  VAL   A CG2  1 
ATOM   3225 H  H    . VAL   A 1 151 ? 19.343 -13.992 9.789   1.00 14.21 ?  151  VAL   A H    1 
ATOM   3226 H  HA   . VAL   A 1 151 ? 20.328 -11.473 9.851   1.00 14.13 ?  151  VAL   A HA   1 
ATOM   3227 H  HB   . VAL   A 1 151 ? 20.892 -12.294 7.790   1.00 15.60 ?  151  VAL   A HB   1 
ATOM   3228 H  HG11 . VAL   A 1 151 ? 19.255 -12.945 6.234   1.00 16.95 ?  151  VAL   A HG11 1 
ATOM   3229 H  HG12 . VAL   A 1 151 ? 19.405 -13.961 7.446   1.00 16.95 ?  151  VAL   A HG12 1 
ATOM   3230 H  HG13 . VAL   A 1 151 ? 18.191 -12.936 7.413   1.00 16.95 ?  151  VAL   A HG13 1 
ATOM   3231 H  HG21 . VAL   A 1 151 ? 20.075 -10.628 6.460   1.00 16.01 ?  151  VAL   A HG21 1 
ATOM   3232 H  HG22 . VAL   A 1 151 ? 18.821 -10.423 7.412   1.00 16.01 ?  151  VAL   A HG22 1 
ATOM   3233 H  HG23 . VAL   A 1 151 ? 20.275 -10.023 7.914   1.00 16.01 ?  151  VAL   A HG23 1 
ATOM   3234 N  N    . TYR   A 1 152 ? 18.291 -10.326 10.331  1.00 11.58 ?  152  TYR   A N    1 
ATOM   3235 C  CA   . TYR   A 1 152 ? 17.107 -9.583  10.727  1.00 11.30 ?  152  TYR   A CA   1 
ATOM   3236 C  C    . TYR   A 1 152 ? 16.912 -8.481  9.697   1.00 11.01 ?  152  TYR   A C    1 
ATOM   3237 O  O    . TYR   A 1 152 ? 17.686 -7.517  9.648   1.00 11.50 ?  152  TYR   A O    1 
ATOM   3238 C  CB   . TYR   A 1 152 ? 17.304 -9.045  12.142  1.00 11.79 ?  152  TYR   A CB   1 
ATOM   3239 C  CG   . TYR   A 1 152 ? 17.267 -10.182 13.133  1.00 12.68 ?  152  TYR   A CG   1 
ATOM   3240 C  CD1  . TYR   A 1 152 ? 18.397 -10.940 13.403  1.00 13.77 ?  152  TYR   A CD1  1 
ATOM   3241 C  CD2  . TYR   A 1 152 ? 16.085 -10.537 13.752  1.00 13.16 ?  152  TYR   A CD2  1 
ATOM   3242 C  CE1  . TYR   A 1 152 ? 18.358 -12.009 14.275  1.00 14.92 ?  152  TYR   A CE1  1 
ATOM   3243 C  CE2  . TYR   A 1 152 ? 16.029 -11.610 14.629  1.00 14.28 ?  152  TYR   A CE2  1 
ATOM   3244 C  CZ   . TYR   A 1 152 ? 17.172 -12.341 14.887  1.00 15.26 ?  152  TYR   A CZ   1 
ATOM   3245 O  OH   . TYR   A 1 152 ? 17.129 -13.415 15.759  1.00 17.37 ?  152  TYR   A OH   1 
ATOM   3246 H  H    . TYR   A 1 152 ? 19.014 -9.859  10.424  1.00 13.92 ?  152  TYR   A H    1 
ATOM   3247 H  HA   . TYR   A 1 152 ? 16.333 -10.173 10.718  1.00 13.59 ?  152  TYR   A HA   1 
ATOM   3248 H  HB2  . TYR   A 1 152 ? 18.166 -8.615  12.206  1.00 14.18 ?  152  TYR   A HB2  1 
ATOM   3249 H  HB3  . TYR   A 1 152 ? 16.591 -8.428  12.356  1.00 14.18 ?  152  TYR   A HB3  1 
ATOM   3250 H  HD1  . TYR   A 1 152 ? 19.197 -10.721 12.982  1.00 16.55 ?  152  TYR   A HD1  1 
ATOM   3251 H  HD2  . TYR   A 1 152 ? 15.307 -10.055 13.576  1.00 15.82 ?  152  TYR   A HD2  1 
ATOM   3252 H  HE1  . TYR   A 1 152 ? 19.128 -12.499 14.450  1.00 17.93 ?  152  TYR   A HE1  1 
ATOM   3253 H  HE2  . TYR   A 1 152 ? 15.226 -11.834 15.048  1.00 17.16 ?  152  TYR   A HE2  1 
ATOM   3254 H  HH   . TYR   A 1 152 ? 16.350 -13.500 16.068  1.00 20.87 ?  152  TYR   A HH   1 
ATOM   3255 N  N    A LEU   A 1 153 ? 15.906 -8.666  8.839   0.60 11.25 ?  153  LEU   A N    1 
ATOM   3256 N  N    B LEU   A 1 153 ? 15.873 -8.605  8.890   0.40 11.09 ?  153  LEU   A N    1 
ATOM   3257 C  CA   A LEU   A 1 153 ? 15.635 -7.792  7.703   0.60 11.21 ?  153  LEU   A CA   1 
ATOM   3258 C  CA   B LEU   A 1 153 ? 15.611 -7.623  7.854   0.40 10.78 ?  153  LEU   A CA   1 
ATOM   3259 C  C    A LEU   A 1 153 ? 14.620 -6.719  8.073   0.60 11.19 ?  153  LEU   A C    1 
ATOM   3260 C  C    B LEU   A 1 153 ? 14.666 -6.547  8.370   0.40 10.60 ?  153  LEU   A C    1 
ATOM   3261 O  O    A LEU   A 1 153 ? 13.534 -7.026  8.577   0.60 12.43 ?  153  LEU   A O    1 
ATOM   3262 O  O    B LEU   A 1 153 ? 13.589 -6.850  8.895   0.40 11.49 ?  153  LEU   A O    1 
ATOM   3263 C  CB   A LEU   A 1 153 ? 15.068 -8.610  6.539   0.60 11.06 ?  153  LEU   A CB   1 
ATOM   3264 C  CB   B LEU   A 1 153 ? 15.012 -8.303  6.629   0.40 10.77 ?  153  LEU   A CB   1 
ATOM   3265 C  CG   A LEU   A 1 153 ? 16.005 -9.574  5.810   0.60 11.01 ?  153  LEU   A CG   1 
ATOM   3266 C  CG   B LEU   A 1 153 ? 15.887 -9.405  6.027   0.40 10.92 ?  153  LEU   A CG   1 
ATOM   3267 C  CD1  A LEU   A 1 153 ? 15.219 -10.481 4.881   0.60 11.44 ?  153  LEU   A CD1  1 
ATOM   3268 C  CD1  B LEU   A 1 153 ? 15.089 -10.198 5.008   0.40 10.94 ?  153  LEU   A CD1  1 
ATOM   3269 C  CD2  A LEU   A 1 153 ? 17.035 -8.785  5.025   0.60 11.30 ?  153  LEU   A CD2  1 
ATOM   3270 C  CD2  B LEU   A 1 153 ? 17.167 -8.835  5.408   0.40 11.66 ?  153  LEU   A CD2  1 
ATOM   3271 H  H    A LEU   A 1 153 ? 15.338 -9.316  8.908   0.60 13.53 ?  153  LEU   A H    1 
ATOM   3272 H  H    B LEU   A 1 153 ? 15.299 -9.249  8.925   0.40 13.34 ?  153  LEU   A H    1 
ATOM   3273 H  HA   A LEU   A 1 153 ? 16.455 -7.370  7.416   0.60 13.47 ?  153  LEU   A HA   1 
ATOM   3274 H  HA   B LEU   A 1 153 ? 16.446 -7.206  7.610   0.40 12.97 ?  153  LEU   A HA   1 
ATOM   3275 H  HB2  A LEU   A 1 153 ? 14.330 -9.142  6.874   0.60 13.30 ?  153  LEU   A HB2  1 
ATOM   3276 H  HB2  B LEU   A 1 153 ? 14.166 -8.698  6.884   0.40 12.95 ?  153  LEU   A HB2  1 
ATOM   3277 H  HB3  A LEU   A 1 153 ? 14.734 -7.991  5.871   0.60 13.30 ?  153  LEU   A HB3  1 
ATOM   3278 H  HB3  B LEU   A 1 153 ? 14.870 -7.625  5.951   0.40 12.95 ?  153  LEU   A HB3  1 
ATOM   3279 H  HG   A LEU   A 1 153 ? 16.475 -10.125 6.458   0.60 13.24 ?  153  LEU   A HG   1 
ATOM   3280 H  HG   B LEU   A 1 153 ? 16.154 -10.009 6.736   0.40 13.13 ?  153  LEU   A HG   1 
ATOM   3281 H  HD11 A LEU   A 1 153 ? 15.791 -11.206 4.588   0.60 13.75 ?  153  LEU   A HD11 1 
ATOM   3282 H  HD11 B LEU   A 1 153 ? 15.658 -10.888 4.634   0.40 13.15 ?  153  LEU   A HD11 1 
ATOM   3283 H  HD12 A LEU   A 1 153 ? 14.457 -10.833 5.360   0.60 13.75 ?  153  LEU   A HD12 1 
ATOM   3284 H  HD12 B LEU   A 1 153 ? 14.327 -10.600 5.452   0.40 13.15 ?  153  LEU   A HD12 1 
ATOM   3285 H  HD13 A LEU   A 1 153 ? 14.922 -9.962  4.117   0.60 13.75 ?  153  LEU   A HD13 1 
ATOM   3286 H  HD13 B LEU   A 1 153 ? 14.788 -9.599  4.307   0.40 13.15 ?  153  LEU   A HD13 1 
ATOM   3287 H  HD21 A LEU   A 1 153 ? 17.607 -9.401  4.547   0.60 13.59 ?  153  LEU   A HD21 1 
ATOM   3288 H  HD21 B LEU   A 1 153 ? 17.671 -9.560  5.006   0.40 14.02 ?  153  LEU   A HD21 1 
ATOM   3289 H  HD22 A LEU   A 1 153 ? 16.571 -8.207  4.400   0.60 13.59 ?  153  LEU   A HD22 1 
ATOM   3290 H  HD22 B LEU   A 1 153 ? 16.929 -8.181  4.733   0.40 14.02 ?  153  LEU   A HD22 1 
ATOM   3291 H  HD23 A LEU   A 1 153 ? 17.559 -8.252  5.642   0.60 13.59 ?  153  LEU   A HD23 1 
ATOM   3292 H  HD23 B LEU   A 1 153 ? 17.698 -8.412  6.104   0.40 14.02 ?  153  LEU   A HD23 1 
ATOM   3293 N  N    A ALA   A 1 154 ? 14.960 -5.467  7.777   0.60 10.46 ?  154  ALA   A N    1 
ATOM   3294 N  N    B ALA   A 1 154 ? 15.083 -5.292  8.228   0.40 10.15 ?  154  ALA   A N    1 
ATOM   3295 C  CA   A ALA   A 1 154 ? 14.083 -4.326  8.006   0.60 10.93 ?  154  ALA   A CA   1 
ATOM   3296 C  CA   B ALA   A 1 154 ? 14.240 -4.140  8.509   0.40 10.39 ?  154  ALA   A CA   1 
ATOM   3297 C  C    A ALA   A 1 154 ? 13.597 -3.799  6.662   0.60 11.04 ?  154  ALA   A C    1 
ATOM   3298 C  C    B ALA   A 1 154 ? 13.773 -3.571  7.174   0.40 10.17 ?  154  ALA   A C    1 
ATOM   3299 O  O    A ALA   A 1 154 ? 14.406 -3.439  5.798   0.60 11.77 ?  154  ALA   A O    1 
ATOM   3300 O  O    B ALA   A 1 154 ? 14.598 -3.221  6.321   0.40 10.45 ?  154  ALA   A O    1 
ATOM   3301 C  CB   A ALA   A 1 154 ? 14.821 -3.223  8.763   0.60 11.59 ?  154  ALA   A CB   1 
ATOM   3302 C  CB   B ALA   A 1 154 ? 15.013 -3.085  9.303   0.40 10.84 ?  154  ALA   A CB   1 
ATOM   3303 H  H    A ALA   A 1 154 ? 15.716 -5.254  7.430   0.60 12.57 ?  154  ALA   A H    1 
ATOM   3304 H  H    B ALA   A 1 154 ? 15.876 -5.075  7.968   0.40 12.21 ?  154  ALA   A H    1 
ATOM   3305 H  HA   A ALA   A 1 154 ? 13.315 -4.604  8.530   0.60 13.15 ?  154  ALA   A HA   1 
ATOM   3306 H  HA   B ALA   A 1 154 ? 13.467 -4.409  9.031   0.40 12.50 ?  154  ALA   A HA   1 
ATOM   3307 H  HB1  A ALA   A 1 154 ? 14.218 -2.479  8.902   0.60 13.93 ?  154  ALA   A HB1  1 
ATOM   3308 H  HB1  B ALA   A 1 154 ? 14.431 -2.328  9.478   0.40 13.03 ?  154  ALA   A HB1  1 
ATOM   3309 H  HB2  A ALA   A 1 154 ? 15.123 -3.573  9.615   0.60 13.93 ?  154  ALA   A HB2  1 
ATOM   3310 H  HB2  B ALA   A 1 154 ? 15.311 -3.471  10.145  0.40 13.03 ?  154  ALA   A HB2  1 
ATOM   3311 H  HB3  A ALA   A 1 154 ? 15.585 -2.937  8.234   0.60 13.93 ?  154  ALA   A HB3  1 
ATOM   3312 H  HB3  B ALA   A 1 154 ? 15.782 -2.798  8.785   0.40 13.03 ?  154  ALA   A HB3  1 
ATOM   3313 N  N    A VAL   A 1 155 ? 12.276 -3.744  6.498   0.60 11.45 ?  155  VAL   A N    1 
ATOM   3314 N  N    B VAL   A 1 155 ? 12.458 -3.490  6.995   0.40 10.41 ?  155  VAL   A N    1 
ATOM   3315 C  CA   A VAL   A 1 155 ? 11.624 -3.269  5.282   0.60 12.54 ?  155  VAL   A CA   1 
ATOM   3316 C  CA   B VAL   A 1 155 ? 11.848 -2.956  5.782   0.40 11.10 ?  155  VAL   A CA   1 
ATOM   3317 C  C    A VAL   A 1 155 ? 10.866 -1.994  5.632   0.60 13.93 ?  155  VAL   A C    1 
ATOM   3318 C  C    B VAL   A 1 155 ? 11.045 -1.723  6.170   0.40 12.29 ?  155  VAL   A C    1 
ATOM   3319 O  O    A VAL   A 1 155 ? 9.920  -2.029  6.426   0.60 14.18 ?  155  VAL   A O    1 
ATOM   3320 O  O    B VAL   A 1 155 ? 10.075 -1.824  6.931   0.40 12.51 ?  155  VAL   A O    1 
ATOM   3321 C  CB   A VAL   A 1 155 ? 10.676 -4.332  4.701   0.60 12.92 ?  155  VAL   A CB   1 
ATOM   3322 C  CB   B VAL   A 1 155 ? 10.958 -3.998  5.088   0.40 11.50 ?  155  VAL   A CB   1 
ATOM   3323 C  CG1  A VAL   A 1 155 ? 9.966  -3.803  3.463   0.60 13.47 ?  155  VAL   A CG1  1 
ATOM   3324 C  CG1  B VAL   A 1 155 ? 10.201 -3.356  3.936   0.40 11.64 ?  155  VAL   A CG1  1 
ATOM   3325 C  CG2  A VAL   A 1 155 ? 11.436 -5.612  4.367   0.60 13.84 ?  155  VAL   A CG2  1 
ATOM   3326 C  CG2  B VAL   A 1 155 ? 11.808 -5.168  4.597   0.40 11.87 ?  155  VAL   A CG2  1 
ATOM   3327 H  H    A VAL   A 1 155 ? 11.714 -3.997  7.103   0.60 13.77 ?  155  VAL   A H    1 
ATOM   3328 H  H    B VAL   A 1 155 ? 11.886 -3.753  7.584   0.40 12.52 ?  155  VAL   A H    1 
ATOM   3329 H  HA   A VAL   A 1 155 ? 12.293 -3.064  4.614   0.60 15.07 ?  155  VAL   A HA   1 
ATOM   3330 H  HA   B VAL   A 1 155 ? 12.547 -2.686  5.169   0.40 13.35 ?  155  VAL   A HA   1 
ATOM   3331 H  HB   A VAL   A 1 155 ? 10.000 -4.556  5.364   0.60 15.53 ?  155  VAL   A HB   1 
ATOM   3332 H  HB   B VAL   A 1 155 ? 10.310 -4.336  5.730   0.40 13.83 ?  155  VAL   A HB   1 
ATOM   3333 H  HG11 A VAL   A 1 155 ? 9.529  -4.543  3.009   0.60 16.19 ?  155  VAL   A HG11 1 
ATOM   3334 H  HG11 B VAL   A 1 155 ? 9.840  -4.056  3.374   0.40 14.00 ?  155  VAL   A HG11 1 
ATOM   3335 H  HG12 A VAL   A 1 155 ? 9.305  -3.147  3.732   0.60 16.19 ?  155  VAL   A HG12 1 
ATOM   3336 H  HG12 B VAL   A 1 155 ? 9.479  -2.813  4.292   0.40 14.00 ?  155  VAL   A HG12 1 
ATOM   3337 H  HG13 A VAL   A 1 155 ? 10.621 -3.398  2.875   0.60 16.19 ?  155  VAL   A HG13 1 
ATOM   3338 H  HG13 B VAL   A 1 155 ? 10.813 -2.803  3.428   0.40 14.00 ?  155  VAL   A HG13 1 
ATOM   3339 H  HG21 A VAL   A 1 155 ? 10.825 -6.248  3.963   0.60 16.63 ?  155  VAL   A HG21 1 
ATOM   3340 H  HG21 B VAL   A 1 155 ? 11.233 -5.810  4.154   0.40 14.28 ?  155  VAL   A HG21 1 
ATOM   3341 H  HG22 A VAL   A 1 155 ? 12.150 -5.398  3.746   0.60 16.63 ?  155  VAL   A HG22 1 
ATOM   3342 H  HG22 B VAL   A 1 155 ? 12.474 -4.834  3.976   0.40 14.28 ?  155  VAL   A HG22 1 
ATOM   3343 H  HG23 A VAL   A 1 155 ? 11.807 -5.982  5.183   0.60 16.63 ?  155  VAL   A HG23 1 
ATOM   3344 H  HG23 B VAL   A 1 155 ? 12.245 -5.585  5.358   0.40 14.28 ?  155  VAL   A HG23 1 
ATOM   3345 N  N    A PHE   A 1 156 ? 11.267 -0.874  5.024   0.60 15.58 ?  156  PHE   A N    1 
ATOM   3346 N  N    B PHE   A 1 156 ? 11.440 -0.560  5.641   0.40 12.67 ?  156  PHE   A N    1 
ATOM   3347 C  CA   A PHE   A 1 156 ? 10.739 0.433   5.419   0.60 17.48 ?  156  PHE   A CA   1 
ATOM   3348 C  CA   B PHE   A 1 156 ? 10.819 0.689   6.078   0.40 14.20 ?  156  PHE   A CA   1 
ATOM   3349 C  C    A PHE   A 1 156 ? 9.267  0.595   5.050   0.60 18.51 ?  156  PHE   A C    1 
ATOM   3350 C  C    B PHE   A 1 156 ? 9.393  0.821   5.557   0.40 14.61 ?  156  PHE   A C    1 
ATOM   3351 O  O    A PHE   A 1 156 ? 8.493  1.185   5.813   0.60 19.57 ?  156  PHE   A O    1 
ATOM   3352 O  O    B PHE   A 1 156 ? 8.487  1.212   6.303   0.40 15.39 ?  156  PHE   A O    1 
ATOM   3353 C  CB   A PHE   A 1 156 ? 11.583 1.524   4.757   0.60 18.32 ?  156  PHE   A CB   1 
ATOM   3354 C  CB   B PHE   A 1 156 ? 11.661 1.889   5.637   0.40 15.72 ?  156  PHE   A CB   1 
ATOM   3355 C  CG   A PHE   A 1 156 ? 11.183 2.934   5.124   0.60 19.12 ?  156  PHE   A CG   1 
ATOM   3356 C  CG   B PHE   A 1 156 ? 11.009 3.216   5.925   0.40 18.01 ?  156  PHE   A CG   1 
ATOM   3357 C  CD1  A PHE   A 1 156 ? 11.149 3.339   6.449   0.60 19.87 ?  156  PHE   A CD1  1 
ATOM   3358 C  CD1  B PHE   A 1 156 ? 10.911 3.681   7.226   0.40 18.80 ?  156  PHE   A CD1  1 
ATOM   3359 C  CD2  A PHE   A 1 156 ? 10.878 3.858   4.137   0.60 19.70 ?  156  PHE   A CD2  1 
ATOM   3360 C  CD2  B PHE   A 1 156 ? 10.485 3.989   4.901   0.40 19.26 ?  156  PHE   A CD2  1 
ATOM   3361 C  CE1  A PHE   A 1 156 ? 10.798 4.638   6.783   0.60 20.47 ?  156  PHE   A CE1  1 
ATOM   3362 C  CE1  B PHE   A 1 156 ? 10.307 4.896   7.501   0.40 19.76 ?  156  PHE   A CE1  1 
ATOM   3363 C  CE2  A PHE   A 1 156 ? 10.525 5.158   4.465   0.60 20.52 ?  156  PHE   A CE2  1 
ATOM   3364 C  CE2  B PHE   A 1 156 ? 9.878  5.206   5.171   0.40 20.02 ?  156  PHE   A CE2  1 
ATOM   3365 C  CZ   A PHE   A 1 156 ? 10.489 5.548   5.789   0.60 20.69 ?  156  PHE   A CZ   1 
ATOM   3366 C  CZ   B PHE   A 1 156 ? 9.790  5.658   6.472   0.40 20.35 ?  156  PHE   A CZ   1 
ATOM   3367 H  H    A PHE   A 1 156 ? 11.839 -0.858  4.387   0.60 18.72 ?  156  PHE   A H    1 
ATOM   3368 H  H    B PHE   A 1 156 ? 12.050 -0.473  5.039   0.40 15.23 ?  156  PHE   A H    1 
ATOM   3369 H  HA   A PHE   A 1 156 ? 10.823 0.517   6.381   0.60 21.00 ?  156  PHE   A HA   1 
ATOM   3370 H  HA   B PHE   A 1 156 ? 10.787 0.700   7.046   0.40 17.06 ?  156  PHE   A HA   1 
ATOM   3371 H  HB2  A PHE   A 1 156 ? 12.507 1.395   5.020   0.60 22.01 ?  156  PHE   A HB2  1 
ATOM   3372 H  HB2  B PHE   A 1 156 ? 12.514 1.870   6.106   0.40 18.89 ?  156  PHE   A HB2  1 
ATOM   3373 H  HB3  A PHE   A 1 156 ? 11.500 1.429   3.795   0.60 22.01 ?  156  PHE   A HB3  1 
ATOM   3374 H  HB3  B PHE   A 1 156 ? 11.815 1.836   4.680   0.40 18.89 ?  156  PHE   A HB3  1 
ATOM   3375 H  HD1  A PHE   A 1 156 ? 11.359 2.723   7.124   0.60 23.87 ?  156  PHE   A HD1  1 
ATOM   3376 H  HD1  B PHE   A 1 156 ? 11.258 3.171   7.923   0.40 22.59 ?  156  PHE   A HD1  1 
ATOM   3377 H  HD2  A PHE   A 1 156 ? 10.900 3.592   3.245   0.60 23.66 ?  156  PHE   A HD2  1 
ATOM   3378 H  HD2  B PHE   A 1 156 ? 10.543 3.688   4.023   0.40 23.14 ?  156  PHE   A HD2  1 
ATOM   3379 H  HE1  A PHE   A 1 156 ? 10.776 4.893   7.677   0.60 24.59 ?  156  PHE   A HE1  1 
ATOM   3380 H  HE1  B PHE   A 1 156 ? 10.248 5.198   8.380   0.40 23.73 ?  156  PHE   A HE1  1 
ATOM   3381 H  HE2  A PHE   A 1 156 ? 10.317 5.762   3.796   0.60 24.66 ?  156  PHE   A HE2  1 
ATOM   3382 H  HE2  B PHE   A 1 156 ? 9.531  5.718   4.476   0.40 24.05 ?  156  PHE   A HE2  1 
ATOM   3383 H  HZ   A PHE   A 1 156 ? 10.253 6.415   6.014   0.60 24.85 ?  156  PHE   A HZ   1 
ATOM   3384 H  HZ   B PHE   A 1 156 ? 9.383  6.475   6.656   0.40 24.44 ?  156  PHE   A HZ   1 
ATOM   3385 N  N    A ASP   A 1 157 ? 8.866  0.087   3.890   0.60 18.96 ?  157  ASP   A N    1 
ATOM   3386 N  N    B ASP   A 1 157 ? 9.178  0.501   4.284   0.40 14.62 ?  157  ASP   A N    1 
ATOM   3387 C  CA   A ASP   A 1 157 ? 7.538  0.336   3.345   0.60 19.72 ?  157  ASP   A CA   1 
ATOM   3388 C  CA   B ASP   A 1 157 ? 7.899  0.750   3.631   0.40 15.84 ?  157  ASP   A CA   1 
ATOM   3389 C  C    A ASP   A 1 157 ? 6.568  -0.730  3.844   0.60 19.44 ?  157  ASP   A C    1 
ATOM   3390 C  C    B ASP   A 1 157 ? 6.867  -0.267  4.102   0.40 16.36 ?  157  ASP   A C    1 
ATOM   3391 O  O    A ASP   A 1 157 ? 6.741  -1.916  3.545   0.60 18.69 ?  157  ASP   A O    1 
ATOM   3392 O  O    B ASP   A 1 157 ? 7.078  -1.480  3.983   0.40 15.87 ?  157  ASP   A O    1 
ATOM   3393 C  CB   A ASP   A 1 157 ? 7.607  0.319   1.821   0.60 20.89 ?  157  ASP   A CB   1 
ATOM   3394 C  CB   B ASP   A 1 157 ? 8.087  0.664   2.119   0.40 16.51 ?  157  ASP   A CB   1 
ATOM   3395 C  CG   A ASP   A 1 157 ? 6.322  0.808   1.176   0.60 22.29 ?  157  ASP   A CG   1 
ATOM   3396 C  CG   B ASP   A 1 157 ? 6.863  1.134   1.352   0.40 16.80 ?  157  ASP   A CG   1 
ATOM   3397 O  OD1  A ASP   A 1 157 ? 5.965  1.990   1.370   0.60 23.56 ?  157  ASP   A OD1  1 
ATOM   3398 O  OD1  B ASP   A 1 157 ? 5.806  0.477   1.471   0.40 17.03 ?  157  ASP   A OD1  1 
ATOM   3399 O  OD2  A ASP   A 1 157 ? 5.660  0.004   0.485   0.60 22.28 -1 157  ASP   A OD2  1 
ATOM   3400 O  OD2  B ASP   A 1 157 ? 6.949  2.161   0.646   0.40 17.32 -1 157  ASP   A OD2  1 
ATOM   3401 H  H    A ASP   A 1 157 ? 9.351  -0.429  3.399   0.60 22.78 ?  157  ASP   A H    1 
ATOM   3402 H  H    B ASP   A 1 157 ? 9.769  0.137   3.776   0.40 17.57 ?  157  ASP   A H    1 
ATOM   3403 H  HA   A ASP   A 1 157 ? 7.223  1.200   3.639   0.60 23.69 ?  157  ASP   A HA   1 
ATOM   3404 H  HA   B ASP   A 1 157 ? 7.588  1.638   3.856   0.40 19.03 ?  157  ASP   A HA   1 
ATOM   3405 H  HB2  A ASP   A 1 157 ? 8.365  0.869   1.546   0.60 25.09 ?  157  ASP   A HB2  1 
ATOM   3406 H  HB2  B ASP   A 1 157 ? 8.852  1.206   1.870   0.40 19.84 ?  157  ASP   A HB2  1 
ATOM   3407 H  HB3  A ASP   A 1 157 ? 7.752  -0.595  1.525   0.60 25.09 ?  157  ASP   A HB3  1 
ATOM   3408 H  HB3  B ASP   A 1 157 ? 8.262  -0.263  1.878   0.40 19.84 ?  157  ASP   A HB3  1 
ATOM   3409 N  N    A LYS   A 1 158 ? 5.548  -0.301  4.598   0.60 20.52 ?  158  LYS   A N    1 
ATOM   3410 N  N    B LYS   A 1 158 ? 5.744  0.226   4.624   0.40 17.76 ?  158  LYS   A N    1 
ATOM   3411 C  CA   A LYS   A 1 158 ? 4.591  -1.241  5.180   0.60 21.28 ?  158  LYS   A CA   1 
ATOM   3412 C  CA   B LYS   A 1 158 ? 4.732  -0.675  5.162   0.40 18.87 ?  158  LYS   A CA   1 
ATOM   3413 C  C    A LYS   A 1 158 ? 3.869  -2.035  4.097   0.60 20.83 ?  158  LYS   A C    1 
ATOM   3414 C  C    B LYS   A 1 158 ? 4.078  -1.487  4.052   0.40 18.24 ?  158  LYS   A C    1 
ATOM   3415 O  O    A LYS   A 1 158 ? 3.686  -3.252  4.224   0.60 20.61 ?  158  LYS   A O    1 
ATOM   3416 O  O    B LYS   A 1 158 ? 3.924  -2.708  4.170   0.40 18.26 ?  158  LYS   A O    1 
ATOM   3417 C  CB   A LYS   A 1 158 ? 3.601  -0.479  6.070   0.60 22.19 ?  158  LYS   A CB   1 
ATOM   3418 C  CB   B LYS   A 1 158 ? 3.680  0.111   5.943   0.40 20.57 ?  158  LYS   A CB   1 
ATOM   3419 C  CG   A LYS   A 1 158 ? 2.407  -1.291  6.574   0.60 23.33 ?  158  LYS   A CG   1 
ATOM   3420 C  CG   B LYS   A 1 158 ? 2.477  -0.732  6.348   0.40 22.07 ?  158  LYS   A CG   1 
ATOM   3421 C  CD   A LYS   A 1 158 ? 2.829  -2.482  7.420   0.60 23.93 ?  158  LYS   A CD   1 
ATOM   3422 C  CD   B LYS   A 1 158 ? 1.332  0.126   6.834   0.40 23.23 ?  158  LYS   A CD   1 
ATOM   3423 C  CE   A LYS   A 1 158 ? 1.605  -3.209  7.967   0.60 24.53 ?  158  LYS   A CE   1 
ATOM   3424 C  CE   B LYS   A 1 158 ? 0.048  -0.193  6.085   0.40 23.98 ?  158  LYS   A CE   1 
ATOM   3425 N  NZ   A LYS   A 1 158 ? 1.935  -4.538  8.555   0.60 24.82 ?  158  LYS   A NZ   1 
ATOM   3426 N  NZ   B LYS   A 1 158 ? -0.414 -1.591  6.315   0.40 24.24 ?  158  LYS   A NZ   1 
ATOM   3427 H  H    A LYS   A 1 158 ? 5.394  0.520   4.786   0.60 24.65 ?  158  LYS   A H    1 
ATOM   3428 H  H    B LYS   A 1 158 ? 5.546  1.060   4.663   0.40 21.34 ?  158  LYS   A H    1 
ATOM   3429 H  HA   A LYS   A 1 158 ? 5.065  -1.869  5.747   0.60 25.57 ?  158  LYS   A HA   1 
ATOM   3430 H  HA   B LYS   A 1 158 ? 5.153  -1.295  5.776   0.40 22.67 ?  158  LYS   A HA   1 
ATOM   3431 H  HB2  A LYS   A 1 158 ? 4.075  -0.150  6.854   0.60 26.66 ?  158  LYS   A HB2  1 
ATOM   3432 H  HB2  B LYS   A 1 158 ? 4.085  0.459   6.758   0.40 24.71 ?  158  LYS   A HB2  1 
ATOM   3433 H  HB3  A LYS   A 1 158 ? 3.248  0.275   5.571   0.60 26.66 ?  158  LYS   A HB3  1 
ATOM   3434 H  HB3  B LYS   A 1 158 ? 3.361  0.845   5.396   0.40 24.71 ?  158  LYS   A HB3  1 
ATOM   3435 H  HG2  A LYS   A 1 158 ? 1.846  -0.717  7.124   0.60 28.02 ?  158  LYS   A HG2  1 
ATOM   3436 H  HG2  B LYS   A 1 158 ? 2.151  -1.243  5.590   0.40 26.51 ?  158  LYS   A HG2  1 
ATOM   3437 H  HG3  A LYS   A 1 158 ? 1.895  -1.617  5.818   0.60 28.02 ?  158  LYS   A HG3  1 
ATOM   3438 H  HG3  B LYS   A 1 158 ? 2.741  -1.333  7.063   0.40 26.51 ?  158  LYS   A HG3  1 
ATOM   3439 H  HD2  A LYS   A 1 158 ? 3.335  -3.100  6.874   0.60 28.75 ?  158  LYS   A HD2  1 
ATOM   3440 H  HD2  B LYS   A 1 158 ? 1.188  -0.046  7.776   0.40 27.91 ?  158  LYS   A HD2  1 
ATOM   3441 H  HD3  A LYS   A 1 158 ? 3.363  -2.170  8.168   0.60 28.75 ?  158  LYS   A HD3  1 
ATOM   3442 H  HD3  B LYS   A 1 158 ? 1.547  1.060   6.690   0.40 27.91 ?  158  LYS   A HD3  1 
ATOM   3443 H  HE2  A LYS   A 1 158 ? 1.195  -2.666  8.658   0.60 29.46 ?  158  LYS   A HE2  1 
ATOM   3444 H  HE2  B LYS   A 1 158 ? -0.649 0.408   6.386   0.40 28.81 ?  158  LYS   A HE2  1 
ATOM   3445 H  HE3  A LYS   A 1 158 ? 0.976  -3.350  7.244   0.60 29.46 ?  158  LYS   A HE3  1 
ATOM   3446 H  HE3  B LYS   A 1 158 ? 0.199  -0.079  5.133   0.40 28.81 ?  158  LYS   A HE3  1 
ATOM   3447 H  HZ1  A LYS   A 1 158 ? 1.195  -4.932  8.850   0.60 29.81 ?  158  LYS   A HZ1  1 
ATOM   3448 H  HZ1  B LYS   A 1 158 ? -1.169 -1.739  5.865   0.40 29.11 ?  158  LYS   A HZ1  1 
ATOM   3449 H  HZ2  A LYS   A 1 158 ? 2.312  -5.057  7.937   0.60 29.81 ?  158  LYS   A HZ2  1 
ATOM   3450 H  HZ2  B LYS   A 1 158 ? 0.205  -2.167  6.038   0.40 29.11 ?  158  LYS   A HZ2  1 
ATOM   3451 H  HZ3  A LYS   A 1 158 ? 2.502  -4.439  9.233   0.60 29.81 ?  158  LYS   A HZ3  1 
ATOM   3452 H  HZ3  B LYS   A 1 158 ? -0.565 -1.722  7.182   0.40 29.11 ?  158  LYS   A HZ3  1 
ATOM   3453 N  N    A ASN   A 1 159 ? 3.458  -1.370  3.019   0.60 21.26 ?  159  ASN   A N    1 
ATOM   3454 N  N    B ASN   A 1 159 ? 3.659  -0.822  2.974   0.40 18.29 ?  159  ASN   A N    1 
ATOM   3455 C  CA   A ASN   A 1 159 ? 2.773  -2.075  1.941   0.60 21.37 ?  159  ASN   A CA   1 
ATOM   3456 C  CA   B ASN   A 1 159 ? 3.049  -1.548  1.867   0.40 18.32 ?  159  ASN   A CA   1 
ATOM   3457 C  C    A ASN   A 1 159 ? 3.667  -3.155  1.329   0.60 19.77 ?  159  ASN   A C    1 
ATOM   3458 C  C    B ASN   A 1 159 ? 3.989  -2.618  1.340   0.40 17.33 ?  159  ASN   A C    1 
ATOM   3459 O  O    A ASN   A 1 159 ? 3.222  -4.287  1.101   0.60 19.60 ?  159  ASN   A O    1 
ATOM   3460 O  O    B ASN   A 1 159 ? 3.550  -3.709  0.961   0.40 16.93 ?  159  ASN   A O    1 
ATOM   3461 C  CB   A ASN   A 1 159 ? 2.292  -1.064  0.897   0.60 23.58 ?  159  ASN   A CB   1 
ATOM   3462 C  CB   B ASN   A 1 159 ? 2.660  -0.581  0.746   0.40 19.94 ?  159  ASN   A CB   1 
ATOM   3463 C  CG   A ASN   A 1 159 ? 1.138  -0.212  1.405   0.60 25.74 ?  159  ASN   A CG   1 
ATOM   3464 C  CG   B ASN   A 1 159 ? 1.492  0.310   1.120   0.40 21.78 ?  159  ASN   A CG   1 
ATOM   3465 O  OD1  A ASN   A 1 159 ? 0.283  -0.700  2.141   0.60 26.53 ?  159  ASN   A OD1  1 
ATOM   3466 O  OD1  B ASN   A 1 159 ? 1.409  1.462   0.687   0.40 22.75 ?  159  ASN   A OD1  1 
ATOM   3467 N  ND2  A ASN   A 1 159 ? 1.114  1.065   1.021   0.60 26.81 ?  159  ASN   A ND2  1 
ATOM   3468 N  ND2  B ASN   A 1 159 ? 0.580  -0.218  1.928   0.40 22.42 ?  159  ASN   A ND2  1 
ATOM   3469 H  H    A ASN   A 1 159 ? 3.566  -0.528  2.895   0.60 25.54 ?  159  ASN   A H    1 
ATOM   3470 H  H    B ASN   A 1 159 ? 3.717  0.028   2.863   0.40 21.98 ?  159  ASN   A H    1 
ATOM   3471 H  HA   A ASN   A 1 159 ? 1.988  -2.511  2.308   0.60 25.67 ?  159  ASN   A HA   1 
ATOM   3472 H  HA   B ASN   A 1 159 ? 2.252  -2.004  2.182   0.40 22.01 ?  159  ASN   A HA   1 
ATOM   3473 H  HB2  A ASN   A 1 159 ? 3.023  -0.469  0.668   0.60 28.33 ?  159  ASN   A HB2  1 
ATOM   3474 H  HB2  B ASN   A 1 159 ? 3.416  -0.009  0.544   0.40 23.95 ?  159  ASN   A HB2  1 
ATOM   3475 H  HB3  A ASN   A 1 159 ? 1.988  -1.540  0.111   0.60 28.33 ?  159  ASN   A HB3  1 
ATOM   3476 H  HB3  B ASN   A 1 159 ? 2.410  -1.092  -0.042  0.40 23.95 ?  159  ASN   A HB3  1 
ATOM   3477 H  HD21 A ASN   A 1 159 ? 0.482  1.587   1.285   0.60 32.20 ?  159  ASN   A HD21 1 
ATOM   3478 H  HD21 B ASN   A 1 159 ? -0.096 0.249   2.160   0.40 26.93 ?  159  ASN   A HD21 1 
ATOM   3479 H  HD22 A ASN   A 1 159 ? 1.735  1.374   0.512   0.60 32.20 ?  159  ASN   A HD22 1 
ATOM   3480 H  HD22 B ASN   A 1 159 ? 0.660  -1.024  2.218   0.40 26.93 ?  159  ASN   A HD22 1 
ATOM   3481 N  N    A LEU   A 1 160 ? 4.939  -2.833  1.082   0.60 18.24 ?  160  LEU   A N    1 
ATOM   3482 N  N    B LEU   A 1 160 ? 5.287  -2.327  1.315   0.40 16.33 ?  160  LEU   A N    1 
ATOM   3483 C  CA   A LEU   A 1 160 ? 5.862  -3.816  0.520   0.60 17.26 ?  160  LEU   A CA   1 
ATOM   3484 C  CA   B LEU   A 1 160 ? 6.252  -3.326  0.872   0.40 15.11 ?  160  LEU   A CA   1 
ATOM   3485 C  C    A LEU   A 1 160 ? 6.087  -4.975  1.481   0.60 16.52 ?  160  LEU   A C    1 
ATOM   3486 C  C    B LEU   A 1 160 ? 6.355  -4.477  1.867   0.40 13.95 ?  160  LEU   A C    1 
ATOM   3487 O  O    A LEU   A 1 160 ? 6.127  -6.144  1.070   0.60 16.98 ?  160  LEU   A O    1 
ATOM   3488 O  O    B LEU   A 1 160 ? 6.362  -5.647  1.473   0.40 14.16 ?  160  LEU   A O    1 
ATOM   3489 C  CB   A LEU   A 1 160 ? 7.196  -3.141  0.210   0.60 16.48 ?  160  LEU   A CB   1 
ATOM   3490 C  CB   B LEU   A 1 160 ? 7.616  -2.679  0.655   0.40 15.36 ?  160  LEU   A CB   1 
ATOM   3491 C  CG   A LEU   A 1 160 ? 8.315  -4.099  -0.188  0.60 16.49 ?  160  LEU   A CG   1 
ATOM   3492 C  CG   B LEU   A 1 160 ? 8.729  -3.663  0.287   0.40 15.79 ?  160  LEU   A CG   1 
ATOM   3493 C  CD1  A LEU   A 1 160 ? 7.869  -4.889  -1.399  0.60 16.96 ?  160  LEU   A CD1  1 
ATOM   3494 C  CD1  B LEU   A 1 160 ? 8.382  -4.456  -0.967  0.40 15.89 ?  160  LEU   A CD1  1 
ATOM   3495 C  CD2  A LEU   A 1 160 ? 9.612  -3.349  -0.460  0.60 16.35 ?  160  LEU   A CD2  1 
ATOM   3496 C  CD2  B LEU   A 1 160 ? 10.051 -2.937  0.114   0.40 15.97 ?  160  LEU   A CD2  1 
ATOM   3497 H  H    A LEU   A 1 160 ? 5.287  -2.064  1.238   0.60 21.92 ?  160  LEU   A H    1 
ATOM   3498 H  H    B LEU   A 1 160 ? 5.620  -1.567  1.536   0.40 19.62 ?  160  LEU   A H    1 
ATOM   3499 H  HA   A LEU   A 1 160 ? 5.489  -4.165  -0.302  0.60 20.74 ?  160  LEU   A HA   1 
ATOM   3500 H  HA   B LEU   A 1 160 ? 5.951  -3.687  0.026   0.40 18.16 ?  160  LEU   A HA   1 
ATOM   3501 H  HB2  A LEU   A 1 160 ? 7.067  -2.515  -0.520  0.60 19.81 ?  160  LEU   A HB2  1 
ATOM   3502 H  HB2  B LEU   A 1 160 ? 7.546  -2.018  -0.054  0.40 18.45 ?  160  LEU   A HB2  1 
ATOM   3503 H  HB3  A LEU   A 1 160 ? 7.491  -2.667  1.002   0.60 19.81 ?  160  LEU   A HB3  1 
ATOM   3504 H  HB3  B LEU   A 1 160 ? 7.877  -2.251  1.482   0.40 18.45 ?  160  LEU   A HB3  1 
ATOM   3505 H  HG   A LEU   A 1 160 ? 8.484  -4.722  0.536   0.60 19.82 ?  160  LEU   A HG   1 
ATOM   3506 H  HG   B LEU   A 1 160 ? 8.839  -4.293  1.015   0.40 18.98 ?  160  LEU   A HG   1 
ATOM   3507 H  HD11 A LEU   A 1 160 ? 8.589  -5.470  -1.670  0.60 20.38 ?  160  LEU   A HD11 1 
ATOM   3508 H  HD11 B LEU   A 1 160 ? 9.158  -4.974  -1.234  0.40 19.10 ?  160  LEU   A HD11 1 
ATOM   3509 H  HD12 A LEU   A 1 160 ? 7.090  -5.422  -1.166  0.60 20.38 ?  160  LEU   A HD12 1 
ATOM   3510 H  HD12 B LEU   A 1 160 ? 7.641  -5.051  -0.770  0.40 19.10 ?  160  LEU   A HD12 1 
ATOM   3511 H  HD13 A LEU   A 1 160 ? 7.645  -4.272  -2.114  0.60 20.38 ?  160  LEU   A HD13 1 
ATOM   3512 H  HD13 B LEU   A 1 160 ? 8.135  -3.840  -1.673  0.40 19.10 ?  160  LEU   A HD13 1 
ATOM   3513 H  HD21 A LEU   A 1 160 ? 10.302 -3.987  -0.696  0.60 19.65 ?  160  LEU   A HD21 1 
ATOM   3514 H  HD21 B LEU   A 1 160 ? 10.738 -3.584  -0.114  0.40 19.19 ?  160  LEU   A HD21 1 
ATOM   3515 H  HD22 A LEU   A 1 160 ? 9.470  -2.728  -1.192  0.60 19.65 ?  160  LEU   A HD22 1 
ATOM   3516 H  HD22 B LEU   A 1 160 ? 9.963  -2.283  -0.596  0.40 19.19 ?  160  LEU   A HD22 1 
ATOM   3517 H  HD23 A LEU   A 1 160 ? 9.870  -2.863  0.339   0.60 19.65 ?  160  LEU   A HD23 1 
ATOM   3518 H  HD23 B LEU   A 1 160 ? 10.280 -2.493  0.947   0.40 19.19 ?  160  LEU   A HD23 1 
ATOM   3519 N  N    A TYR   A 1 161 ? 6.263  -4.665  2.763   0.60 15.74 ?  161  TYR   A N    1 
ATOM   3520 N  N    B TYR   A 1 161 ? 6.458  -4.167  3.162   0.40 13.08 ?  161  TYR   A N    1 
ATOM   3521 C  CA   A TYR   A 1 161 ? 6.426  -5.705  3.768   0.60 15.63 ?  161  TYR   A CA   1 
ATOM   3522 C  CA   B TYR   A 1 161 ? 6.539  -5.228  4.161   0.40 12.87 ?  161  TYR   A CA   1 
ATOM   3523 C  C    A TYR   A 1 161 ? 5.288  -6.715  3.703   0.60 15.92 ?  161  TYR   A C    1 
ATOM   3524 C  C    B TYR   A 1 161 ? 5.353  -6.178  4.045   0.40 13.15 ?  161  TYR   A C    1 
ATOM   3525 O  O    A TYR   A 1 161 ? 5.521  -7.927  3.645   0.60 15.75 ?  161  TYR   A O    1 
ATOM   3526 O  O    B TYR   A 1 161 ? 5.516  -7.402  4.114   0.40 12.88 ?  161  TYR   A O    1 
ATOM   3527 C  CB   A TYR   A 1 161 ? 6.497  -5.065  5.153   0.60 15.75 ?  161  TYR   A CB   1 
ATOM   3528 C  CB   B TYR   A 1 161 ? 6.621  -4.631  5.569   0.40 12.92 ?  161  TYR   A CB   1 
ATOM   3529 C  CG   A TYR   A 1 161 ? 6.405  -6.069  6.270   0.60 15.93 ?  161  TYR   A CG   1 
ATOM   3530 C  CG   B TYR   A 1 161 ? 6.524  -5.672  6.661   0.40 12.67 ?  161  TYR   A CG   1 
ATOM   3531 C  CD1  A TYR   A 1 161 ? 7.515  -6.802  6.654   0.60 16.07 ?  161  TYR   A CD1  1 
ATOM   3532 C  CD1  B TYR   A 1 161 ? 7.651  -6.347  7.109   0.40 12.43 ?  161  TYR   A CD1  1 
ATOM   3533 C  CD2  A TYR   A 1 161 ? 5.205  -6.296  6.938   0.60 16.19 ?  161  TYR   A CD2  1 
ATOM   3534 C  CD2  B TYR   A 1 161 ? 5.301  -5.987  7.238   0.40 13.06 ?  161  TYR   A CD2  1 
ATOM   3535 C  CE1  A TYR   A 1 161 ? 7.440  -7.728  7.664   0.60 16.16 ?  161  TYR   A CE1  1 
ATOM   3536 C  CE1  B TYR   A 1 161 ? 7.566  -7.303  8.100   0.40 13.08 ?  161  TYR   A CE1  1 
ATOM   3537 C  CE2  A TYR   A 1 161 ? 5.120  -7.223  7.956   0.60 16.20 ?  161  TYR   A CE2  1 
ATOM   3538 C  CE2  B TYR   A 1 161 ? 5.205  -6.944  8.230   0.40 13.55 ?  161  TYR   A CE2  1 
ATOM   3539 C  CZ   A TYR   A 1 161 ? 6.243  -7.936  8.313   0.60 16.27 ?  161  TYR   A CZ   1 
ATOM   3540 C  CZ   B TYR   A 1 161 ? 6.340  -7.598  8.657   0.40 13.99 ?  161  TYR   A CZ   1 
ATOM   3541 O  OH   A TYR   A 1 161 ? 6.188  -8.870  9.322   0.60 17.00 ?  161  TYR   A OH   1 
ATOM   3542 O  OH   B TYR   A 1 161 ? 6.257  -8.550  9.646   0.40 15.48 ?  161  TYR   A OH   1 
ATOM   3543 H  H    A TYR   A 1 161 ? 6.283  -3.872  3.075   0.60 18.91 ?  161  TYR   A H    1 
ATOM   3544 H  H    B TYR   A 1 161 ? 6.482  -3.369  3.484   0.40 15.72 ?  161  TYR   A H    1 
ATOM   3545 H  HA   A TYR   A 1 161 ? 7.253  -6.185  3.610   0.60 18.79 ?  161  TYR   A HA   1 
ATOM   3546 H  HA   B TYR   A 1 161 ? 7.343  -5.742  4.013   0.40 15.47 ?  161  TYR   A HA   1 
ATOM   3547 H  HB2  A TYR   A 1 161 ? 7.345  -4.604  5.238   0.60 18.93 ?  161  TYR   A HB2  1 
ATOM   3548 H  HB2  B TYR   A 1 161 ? 7.472  -4.173  5.671   0.40 15.53 ?  161  TYR   A HB2  1 
ATOM   3549 H  HB3  A TYR   A 1 161 ? 5.764  -4.443  5.251   0.60 18.93 ?  161  TYR   A HB3  1 
ATOM   3550 H  HB3  B TYR   A 1 161 ? 5.892  -4.000  5.693   0.40 15.53 ?  161  TYR   A HB3  1 
ATOM   3551 H  HD1  A TYR   A 1 161 ? 8.323  -6.674  6.217   0.60 19.31 ?  161  TYR   A HD1  1 
ATOM   3552 H  HD1  B TYR   A 1 161 ? 8.481  -6.147  6.738   0.40 14.94 ?  161  TYR   A HD1  1 
ATOM   3553 H  HD2  A TYR   A 1 161 ? 4.447  -5.814  6.697   0.60 19.45 ?  161  TYR   A HD2  1 
ATOM   3554 H  HD2  B TYR   A 1 161 ? 4.531  -5.551  6.954   0.40 15.70 ?  161  TYR   A HD2  1 
ATOM   3555 H  HE1  A TYR   A 1 161 ? 8.193  -8.216  7.912   0.60 19.42 ?  161  TYR   A HE1  1 
ATOM   3556 H  HE1  B TYR   A 1 161 ? 8.333  -7.745  8.391   0.40 15.73 ?  161  TYR   A HE1  1 
ATOM   3557 H  HE2  A TYR   A 1 161 ? 4.310  -7.364  8.402   0.60 19.47 ?  161  TYR   A HE2  1 
ATOM   3558 H  HE2  B TYR   A 1 161 ? 4.376  -7.148  8.607   0.40 16.29 ?  161  TYR   A HE2  1 
ATOM   3559 H  HH   A TYR   A 1 161 ? 5.407  -8.902  9.647   0.60 20.43 ?  161  TYR   A HH   1 
ATOM   3560 H  HH   B TYR   A 1 161 ? 5.452  -8.638  9.893   0.40 18.61 ?  161  TYR   A HH   1 
ATOM   3561 N  N    A ASP   A 1 162 ? 4.044  -6.233  3.723   0.60 16.84 ?  162  ASP   A N    1 
ATOM   3562 N  N    B ASP   A 1 162 ? 4.153  -5.626  3.849   0.40 14.10 ?  162  ASP   A N    1 
ATOM   3563 C  CA   A ASP   A 1 162 ? 2.899  -7.139  3.672   0.60 17.54 ?  162  ASP   A CA   1 
ATOM   3564 C  CA   B ASP   A 1 162 ? 2.947  -6.446  3.767   0.40 15.48 ?  162  ASP   A CA   1 
ATOM   3565 C  C    A ASP   A 1 162 ? 2.933  -7.996  2.410   0.60 18.09 ?  162  ASP   A C    1 
ATOM   3566 C  C    B ASP   A 1 162 ? 2.998  -7.389  2.572   0.40 15.96 ?  162  ASP   A C    1 
ATOM   3567 O  O    A ASP   A 1 162 ? 2.562  -9.175  2.437   0.60 18.55 ?  162  ASP   A O    1 
ATOM   3568 O  O    B ASP   A 1 162 ? 2.679  -8.577  2.693   0.40 16.46 ?  162  ASP   A O    1 
ATOM   3569 C  CB   A ASP   A 1 162 ? 1.586  -6.346  3.749   0.60 18.24 ?  162  ASP   A CB   1 
ATOM   3570 C  CB   B ASP   A 1 162 ? 1.709  -5.549  3.681   0.40 16.97 ?  162  ASP   A CB   1 
ATOM   3571 C  CG   A ASP   A 1 162 ? 1.321  -5.753  5.127   0.60 19.55 ?  162  ASP   A CG   1 
ATOM   3572 C  CG   B ASP   A 1 162 ? 1.368  -4.890  5.006   0.40 18.06 ?  162  ASP   A CG   1 
ATOM   3573 O  OD1  A ASP   A 1 162 ? 2.003  -6.145  6.095   0.60 20.62 ?  162  ASP   A OD1  1 
ATOM   3574 O  OD1  B ASP   A 1 162 ? 1.912  -5.311  6.049   0.40 18.52 ?  162  ASP   A OD1  1 
ATOM   3575 O  OD2  A ASP   A 1 162 ? 0.411  -4.895  5.236   0.60 20.23 -1 162  ASP   A OD2  1 
ATOM   3576 O  OD2  B ASP   A 1 162 ? 0.544  -3.955  5.006   0.40 18.86 -1 162  ASP   A OD2  1 
ATOM   3577 H  H    A ASP   A 1 162 ? 3.835  -5.409  3.769   0.60 20.24 ?  162  ASP   A H    1 
ATOM   3578 H  H    B ASP   A 1 162 ? 4.013  -4.782  3.759   0.40 16.95 ?  162  ASP   A H    1 
ATOM   3579 H  HA   A ASP   A 1 162 ? 2.927  -7.747  4.431   0.60 21.07 ?  162  ASP   A HA   1 
ATOM   3580 H  HA   B ASP   A 1 162 ? 2.867  -6.982  4.568   0.40 18.61 ?  162  ASP   A HA   1 
ATOM   3581 H  HB2  A ASP   A 1 162 ? 1.621  -5.617  3.123   0.60 21.91 ?  162  ASP   A HB2  1 
ATOM   3582 H  HB2  B ASP   A 1 162 ? 1.861  -4.860  3.008   0.40 20.39 ?  162  ASP   A HB2  1 
ATOM   3583 H  HB3  A ASP   A 1 162 ? 0.843  -6.937  3.543   0.60 21.91 ?  162  ASP   A HB3  1 
ATOM   3584 H  HB3  B ASP   A 1 162 ? 0.941  -6.084  3.433   0.40 20.39 ?  162  ASP   A HB3  1 
ATOM   3585 N  N    A LYS   A 1 163 ? 3.392  -7.426  1.297   0.60 18.97 ?  163  LYS   A N    1 
ATOM   3586 N  N    B LYS   A 1 163 ? 3.372  -6.875  1.397   0.40 16.74 ?  163  LYS   A N    1 
ATOM   3587 C  CA   A LYS   A 1 163 ? 3.484  -8.179  0.049   0.60 19.79 ?  163  LYS   A CA   1 
ATOM   3588 C  CA   B LYS   A 1 163 ? 3.443  -7.749  0.231   0.40 17.70 ?  163  LYS   A CA   1 
ATOM   3589 C  C    A LYS   A 1 163 ? 4.559  -9.260  0.127   0.60 18.74 ?  163  LYS   A C    1 
ATOM   3590 C  C    B LYS   A 1 163 ? 4.573  -8.757  0.364   0.40 16.22 ?  163  LYS   A C    1 
ATOM   3591 O  O    A LYS   A 1 163 ? 4.358  -10.381 -0.355  0.60 19.69 ?  163  LYS   A O    1 
ATOM   3592 O  O    B LYS   A 1 163 ? 4.457  -9.876  -0.143  0.40 15.90 ?  163  LYS   A O    1 
ATOM   3593 C  CB   A LYS   A 1 163 ? 3.772  -7.207  -1.093  0.60 22.04 ?  163  LYS   A CB   1 
ATOM   3594 C  CB   B LYS   A 1 163 ? 3.609  -6.953  -1.064  0.40 20.45 ?  163  LYS   A CB   1 
ATOM   3595 C  CG   A LYS   A 1 163 ? 3.767  -7.833  -2.466  0.60 24.54 ?  163  LYS   A CG   1 
ATOM   3596 C  CG   B LYS   A 1 163 ? 3.519  -7.818  -2.332  0.40 22.92 ?  163  LYS   A CG   1 
ATOM   3597 C  CD   A LYS   A 1 163 ? 4.168  -6.827  -3.530  0.60 26.90 ?  163  LYS   A CD   1 
ATOM   3598 C  CD   B LYS   A 1 163 ? 3.922  -7.041  -3.579  0.40 24.97 ?  163  LYS   A CD   1 
ATOM   3599 C  CE   A LYS   A 1 163 ? 4.033  -7.428  -4.919  0.60 28.38 ?  163  LYS   A CE   1 
ATOM   3600 C  CE   B LYS   A 1 163 ? 3.345  -7.656  -4.851  0.40 26.37 ?  163  LYS   A CE   1 
ATOM   3601 N  NZ   A LYS   A 1 163 ? 4.700  -6.604  -5.959  0.60 29.16 ?  163  LYS   A NZ   1 
ATOM   3602 N  NZ   B LYS   A 1 163 ? 3.773  -6.908  -6.072  0.40 27.00 ?  163  LYS   A NZ   1 
ATOM   3603 H  H    A LYS   A 1 163 ? 3.654  -6.615  1.240   0.60 22.79 ?  163  LYS   A H    1 
ATOM   3604 H  H    B LYS   A 1 163 ? 3.583  -6.055  1.253   0.40 20.11 ?  163  LYS   A H    1 
ATOM   3605 H  HA   A LYS   A 1 163 ? 2.635  -8.612  -0.131  0.60 23.78 ?  163  LYS   A HA   1 
ATOM   3606 H  HA   B LYS   A 1 163 ? 2.611  -8.246  0.163   0.40 21.27 ?  163  LYS   A HA   1 
ATOM   3607 H  HB2  A LYS   A 1 163 ? 3.095  -6.510  -1.085  0.60 26.48 ?  163  LYS   A HB2  1 
ATOM   3608 H  HB2  B LYS   A 1 163 ? 2.907  -6.285  -1.115  0.40 24.57 ?  163  LYS   A HB2  1 
ATOM   3609 H  HB3  A LYS   A 1 163 ? 4.646  -6.811  -0.954  0.60 26.48 ?  163  LYS   A HB3  1 
ATOM   3610 H  HB3  B LYS   A 1 163 ? 4.476  -6.522  -1.062  0.40 24.57 ?  163  LYS   A HB3  1 
ATOM   3611 H  HG2  A LYS   A 1 163 ? 4.398  -8.566  -2.487  0.60 29.48 ?  163  LYS   A HG2  1 
ATOM   3612 H  HG2  B LYS   A 1 163 ? 4.116  -8.581  -2.249  0.40 27.53 ?  163  LYS   A HG2  1 
ATOM   3613 H  HG3  A LYS   A 1 163 ? 2.872  -8.149  -2.668  0.60 29.48 ?  163  LYS   A HG3  1 
ATOM   3614 H  HG3  B LYS   A 1 163 ? 2.605  -8.125  -2.450  0.40 27.53 ?  163  LYS   A HG3  1 
ATOM   3615 H  HD2  A LYS   A 1 163 ? 3.586  -6.050  -3.475  0.60 32.31 ?  163  LYS   A HD2  1 
ATOM   3616 H  HD2  B LYS   A 1 163 ? 3.595  -6.132  -3.509  0.40 30.00 ?  163  LYS   A HD2  1 
ATOM   3617 H  HD3  A LYS   A 1 163 ? 5.092  -6.565  -3.394  0.60 32.31 ?  163  LYS   A HD3  1 
ATOM   3618 H  HD3  B LYS   A 1 163 ? 4.890  -7.043  -3.659  0.40 30.00 ?  163  LYS   A HD3  1 
ATOM   3619 H  HE2  A LYS   A 1 163 ? 4.422  -8.315  -4.931  0.60 34.09 ?  163  LYS   A HE2  1 
ATOM   3620 H  HE2  B LYS   A 1 163 ? 3.653  -8.572  -4.936  0.40 31.67 ?  163  LYS   A HE2  1 
ATOM   3621 H  HE3  A LYS   A 1 163 ? 3.093  -7.485  -5.140  0.60 34.09 ?  163  LYS   A HE3  1 
ATOM   3622 H  HE3  B LYS   A 1 163 ? 2.375  -7.631  -4.809  0.40 31.67 ?  163  LYS   A HE3  1 
ATOM   3623 H  HZ1  A LYS   A 1 163 ? 4.604  -6.986  -6.756  0.60 35.02 ?  163  LYS   A HZ1  1 
ATOM   3624 H  HZ1  B LYS   A 1 163 ? 3.424  -7.283  -6.800  0.40 32.42 ?  163  LYS   A HZ1  1 
ATOM   3625 H  HZ2  A LYS   A 1 163 ? 4.336  -5.792  -5.980  0.60 35.02 ?  163  LYS   A HZ2  1 
ATOM   3626 H  HZ2  B LYS   A 1 163 ? 3.499  -6.062  -6.024  0.40 32.42 ?  163  LYS   A HZ2  1 
ATOM   3627 H  HZ3  A LYS   A 1 163 ? 5.568  -6.527  -5.777  0.60 35.02 ?  163  LYS   A HZ3  1 
ATOM   3628 H  HZ3  B LYS   A 1 163 ? 4.661  -6.919  -6.140  0.40 32.42 ?  163  LYS   A HZ3  1 
ATOM   3629 N  N    A LEU   A 1 164 ? 5.712  -8.936  0.722   0.60 16.94 ?  164  LEU   A N    1 
ATOM   3630 N  N    B LEU   A 1 164 ? 5.669  -8.384  1.026   0.40 14.61 ?  164  LEU   A N    1 
ATOM   3631 C  CA   A LEU   A 1 164 ? 6.794  -9.912  0.844   0.60 15.88 ?  164  LEU   A CA   1 
ATOM   3632 C  CA   B LEU   A 1 164 ? 6.767  -9.328  1.222   0.40 13.88 ?  164  LEU   A CA   1 
ATOM   3633 C  C    A LEU   A 1 164 ? 6.370  -11.088 1.710   0.60 15.83 ?  164  LEU   A C    1 
ATOM   3634 C  C    B LEU   A 1 164 ? 6.329  -10.512 2.075   0.40 13.76 ?  164  LEU   A C    1 
ATOM   3635 O  O    A LEU   A 1 164 ? 6.677  -12.243 1.396   0.60 15.95 ?  164  LEU   A O    1 
ATOM   3636 O  O    B LEU   A 1 164 ? 6.628  -11.669 1.754   0.40 14.09 ?  164  LEU   A O    1 
ATOM   3637 C  CB   A LEU   A 1 164 ? 8.028  -9.251  1.458   0.60 15.47 ?  164  LEU   A CB   1 
ATOM   3638 C  CB   B LEU   A 1 164 ? 7.961  -8.617  1.857   0.40 13.45 ?  164  LEU   A CB   1 
ATOM   3639 C  CG   A LEU   A 1 164 ? 8.721  -8.161  0.644   0.60 15.80 ?  164  LEU   A CG   1 
ATOM   3640 C  CG   B LEU   A 1 164 ? 8.756  -7.727  0.902   0.40 13.99 ?  164  LEU   A CG   1 
ATOM   3641 C  CD1  A LEU   A 1 164 ? 9.610  -7.301  1.534   0.60 15.85 ?  164  LEU   A CD1  1 
ATOM   3642 C  CD1  B LEU   A 1 164 ? 9.752  -6.882  1.671   0.40 13.79 ?  164  LEU   A CD1  1 
ATOM   3643 C  CD2  A LEU   A 1 164 ? 9.531  -8.782  -0.474  0.60 16.63 ?  164  LEU   A CD2  1 
ATOM   3644 C  CD2  B LEU   A 1 164 ? 9.463  -8.571  -0.148  0.40 14.55 ?  164  LEU   A CD2  1 
ATOM   3645 H  H    A LEU   A 1 164 ? 5.892  -8.173  1.064   0.60 20.36 ?  164  LEU   A H    1 
ATOM   3646 H  H    B LEU   A 1 164 ? 5.803  -7.594  1.351   0.40 17.56 ?  164  LEU   A H    1 
ATOM   3647 H  HA   A LEU   A 1 164 ? 7.026  -10.254 -0.034  0.60 19.08 ?  164  LEU   A HA   1 
ATOM   3648 H  HA   B LEU   A 1 164 ? 7.043  -9.667  0.360   0.40 16.68 ?  164  LEU   A HA   1 
ATOM   3649 H  HB2  A LEU   A 1 164 ? 7.768  -8.863  2.303   0.60 18.59 ?  164  LEU   A HB2  1 
ATOM   3650 H  HB2  B LEU   A 1 164 ? 7.641  -8.054  2.581   0.40 16.17 ?  164  LEU   A HB2  1 
ATOM   3651 H  HB3  A LEU   A 1 164 ? 8.688  -9.950  1.619   0.60 18.59 ?  164  LEU   A HB3  1 
ATOM   3652 H  HB3  B LEU   A 1 164 ? 8.569  -9.285  2.208   0.40 16.17 ?  164  LEU   A HB3  1 
ATOM   3653 H  HG   A LEU   A 1 164 ? 8.046  -7.590  0.249   0.60 18.99 ?  164  LEU   A HG   1 
ATOM   3654 H  HG   B LEU   A 1 164 ? 8.146  -7.126  0.444   0.40 16.82 ?  164  LEU   A HG   1 
ATOM   3655 H  HD11 A LEU   A 1 164 ? 10.036 -6.623  0.991   0.60 19.05 ?  164  LEU   A HD11 1 
ATOM   3656 H  HD11 B LEU   A 1 164 ? 10.269 -6.354  1.045   0.40 16.57 ?  164  LEU   A HD11 1 
ATOM   3657 H  HD12 A LEU   A 1 164 ? 9.060  -6.881  2.217   0.60 19.05 ?  164  LEU   A HD12 1 
ATOM   3658 H  HD12 B LEU   A 1 164 ? 9.266  -6.298  2.276   0.40 16.57 ?  164  LEU   A HD12 1 
ATOM   3659 H  HD13 A LEU   A 1 164 ? 10.279 -7.864  1.952   0.60 19.05 ?  164  LEU   A HD13 1 
ATOM   3660 H  HD13 B LEU   A 1 164 ? 10.336 -7.468  2.176   0.40 16.57 ?  164  LEU   A HD13 1 
ATOM   3661 H  HD21 A LEU   A 1 164 ? 9.900  -8.073  -1.022  0.60 19.98 ?  164  LEU   A HD21 1 
ATOM   3662 H  HD21 B LEU   A 1 164 ? 10.109 -8.020  -0.617  0.40 17.49 ?  164  LEU   A HD21 1 
ATOM   3663 H  HD22 A LEU   A 1 164 ? 10.244 -9.312  -0.090  0.60 19.98 ?  164  LEU   A HD22 1 
ATOM   3664 H  HD22 B LEU   A 1 164 ? 9.915  -9.308  0.292   0.40 17.49 ?  164  LEU   A HD22 1 
ATOM   3665 H  HD23 A LEU   A 1 164 ? 8.948  -9.344  -1.007  0.60 19.98 ?  164  LEU   A HD23 1 
ATOM   3666 H  HD23 B LEU   A 1 164 ? 8.806  -8.914  -0.775  0.40 17.49 ?  164  LEU   A HD23 1 
ATOM   3667 N  N    A VAL   A 1 165 ? 5.684  -10.810 2.818   0.60 15.57 ?  165  VAL   A N    1 
ATOM   3668 N  N    B VAL   A 1 165 ? 5.620  -10.239 3.171   0.40 13.50 ?  165  VAL   A N    1 
ATOM   3669 C  CA   A VAL   A 1 165 ? 5.209  -11.872 3.696   0.60 15.70 ?  165  VAL   A CA   1 
ATOM   3670 C  CA   B VAL   A 1 165 ? 5.130  -11.318 4.022   0.40 14.05 ?  165  VAL   A CA   1 
ATOM   3671 C  C    A VAL   A 1 165 ? 4.148  -12.700 2.993   0.60 15.83 ?  165  VAL   A C    1 
ATOM   3672 C  C    B VAL   A 1 165 ? 4.098  -12.156 3.277   0.40 14.16 ?  165  VAL   A C    1 
ATOM   3673 O  O    A VAL   A 1 165 ? 4.250  -13.929 2.905   0.60 15.53 ?  165  VAL   A O    1 
ATOM   3674 O  O    B VAL   A 1 165 ? 4.142  -13.393 3.306   0.40 13.94 ?  165  VAL   A O    1 
ATOM   3675 C  CB   A VAL   A 1 165 ? 4.671  -11.265 5.003   0.60 15.88 ?  165  VAL   A CB   1 
ATOM   3676 C  CB   B VAL   A 1 165 ? 4.574  -10.744 5.340   0.40 14.75 ?  165  VAL   A CB   1 
ATOM   3677 C  CG1  A VAL   A 1 165 ? 3.887  -12.304 5.804   0.60 16.08 ?  165  VAL   A CG1  1 
ATOM   3678 C  CG1  B VAL   A 1 165 ? 3.882  -11.830 6.150   0.40 15.25 ?  165  VAL   A CG1  1 
ATOM   3679 C  CG2  A VAL   A 1 165 ? 5.809  -10.667 5.814   0.60 16.36 ?  165  VAL   A CG2  1 
ATOM   3680 C  CG2  B VAL   A 1 165 ? 5.690  -10.097 6.152   0.40 14.70 ?  165  VAL   A CG2  1 
ATOM   3681 H  H    A VAL   A 1 165 ? 5.484  -10.029 3.084   0.60 18.72 ?  165  VAL   A H    1 
ATOM   3682 H  H    B VAL   A 1 165 ? 5.411  -9.446  3.439   0.40 16.23 ?  165  VAL   A H    1 
ATOM   3683 H  HA   A VAL   A 1 165 ? 5.947  -12.468 3.922   0.60 18.87 ?  165  VAL   A HA   1 
ATOM   3684 H  HA   B VAL   A 1 165 ? 5.874  -11.892 4.250   0.40 16.89 ?  165  VAL   A HA   1 
ATOM   3685 H  HB   A VAL   A 1 165 ? 4.060  -10.550 4.778   0.60 19.09 ?  165  VAL   A HB   1 
ATOM   3686 H  HB   B VAL   A 1 165 ? 3.919  -10.055 5.140   0.40 17.73 ?  165  VAL   A HB   1 
ATOM   3687 H  HG11 A VAL   A 1 165 ? 3.808  -11.997 6.721   0.60 19.33 ?  165  VAL   A HG11 1 
ATOM   3688 H  HG11 B VAL   A 1 165 ? 3.770  -11.519 7.062   0.40 18.33 ?  165  VAL   A HG11 1 
ATOM   3689 H  HG12 A VAL   A 1 165 ? 3.001  -12.403 5.416   0.60 19.33 ?  165  VAL   A HG12 1 
ATOM   3690 H  HG12 B VAL   A 1 165 ? 3.016  -12.014 5.756   0.40 18.33 ?  165  VAL   A HG12 1 
ATOM   3691 H  HG13 A VAL   A 1 165 ? 4.357  -13.149 5.778   0.60 19.33 ?  165  VAL   A HG13 1 
ATOM   3692 H  HG13 B VAL   A 1 165 ? 4.433  -12.627 6.139   0.40 18.33 ?  165  VAL   A HG13 1 
ATOM   3693 H  HG21 A VAL   A 1 165 ? 5.452  -10.297 6.635   0.60 19.66 ?  165  VAL   A HG21 1 
ATOM   3694 H  HG21 B VAL   A 1 165 ? 5.321  -9.750  6.981   0.40 17.66 ?  165  VAL   A HG21 1 
ATOM   3695 H  HG22 A VAL   A 1 165 ? 6.455  -11.363 6.016   0.60 19.66 ?  165  VAL   A HG22 1 
ATOM   3696 H  HG22 B VAL   A 1 165 ? 6.368  -10.763 6.345   0.40 17.66 ?  165  VAL   A HG22 1 
ATOM   3697 H  HG23 A VAL   A 1 165 ? 6.232  -9.967  5.291   0.60 19.66 ?  165  VAL   A HG23 1 
ATOM   3698 H  HG23 B VAL   A 1 165 ? 6.078  -9.371  5.636   0.40 17.66 ?  165  VAL   A HG23 1 
ATOM   3699 N  N    A SER   A 1 166 ? 3.110  -12.035 2.484   0.60 16.77 ?  166  SER   A N    1 
ATOM   3700 N  N    B SER   A 1 166 ? 3.167  -11.494 2.583   0.40 14.95 ?  166  SER   A N    1 
ATOM   3701 C  CA   A SER   A 1 166 ? 1.981  -12.736 1.893   0.60 17.70 ?  166  SER   A CA   1 
ATOM   3702 C  CA   B SER   A 1 166 ? 2.034  -12.187 1.970   0.40 16.54 ?  166  SER   A CA   1 
ATOM   3703 C  C    A SER   A 1 166 ? 2.359  -13.428 0.601   0.60 18.45 ?  166  SER   A C    1 
ATOM   3704 C  C    B SER   A 1 166 ? 2.475  -13.336 1.066   0.40 17.14 ?  166  SER   A C    1 
ATOM   3705 O  O    A SER   A 1 166 ? 1.673  -14.373 0.197   0.60 19.54 ?  166  SER   A O    1 
ATOM   3706 O  O    B SER   A 1 166 ? 1.880  -14.421 1.095   0.40 17.53 ?  166  SER   A O    1 
ATOM   3707 C  CB   A SER   A 1 166 ? 0.847  -11.754 1.594   0.60 18.67 ?  166  SER   A CB   1 
ATOM   3708 C  CB   B SER   A 1 166 ? 1.172  -11.182 1.191   0.40 18.02 ?  166  SER   A CB   1 
ATOM   3709 O  OG   A SER   A 1 166 ? 0.376  -11.103 2.759   0.60 20.90 ?  166  SER   A OG   1 
ATOM   3710 O  OG   B SER   A 1 166 ? 0.531  -10.263 2.062   0.40 20.05 ?  166  SER   A OG   1 
ATOM   3711 H  H    A SER   A 1 166 ? 3.044  -11.190 2.462   0.60 20.15 ?  166  SER   A H    1 
ATOM   3712 H  H    B SER   A 1 166 ? 3.165  -10.641 2.465   0.40 17.96 ?  166  SER   A H    1 
ATOM   3713 H  HA   A SER   A 1 166 ? 1.648  -13.413 2.510   0.60 21.26 ?  166  SER   A HA   1 
ATOM   3714 H  HA   B SER   A 1 166 ? 1.478  -12.559 2.670   0.40 19.88 ?  166  SER   A HA   1 
ATOM   3715 H  HB2  A SER   A 1 166 ? 1.175  -11.082 0.984   0.60 22.43 ?  166  SER   A HB2  1 
ATOM   3716 H  HB2  B SER   A 1 166 ? 1.740  -10.681 0.583   0.40 21.65 ?  166  SER   A HB2  1 
ATOM   3717 H  HB3  A SER   A 1 166 ? 0.110  -12.242 1.187   0.60 22.43 ?  166  SER   A HB3  1 
ATOM   3718 H  HB3  B SER   A 1 166 ? 0.497  -11.663 0.692   0.40 21.65 ?  166  SER   A HB3  1 
ATOM   3719 H  HG   A SER   A 1 166 ? 1.016  -10.709 3.138   0.60 25.11 ?  166  SER   A HG   1 
ATOM   3720 H  HG   B SER   A 1 166 ? 0.054  -9.729  1.619   0.40 24.08 ?  166  SER   A HG   1 
ATOM   3721 N  N    A SER   A 1 167 ? 3.408  -12.959 -0.071  0.60 17.81 ?  167  SER   A N    1 
ATOM   3722 N  N    B SER   A 1 167 ? 3.524  -13.128 0.266   0.40 17.73 ?  167  SER   A N    1 
ATOM   3723 C  CA   A SER   A 1 167 ? 3.916  -13.635 -1.250  0.60 17.87 ?  167  SER   A CA   1 
ATOM   3724 C  CA   B SER   A 1 167 ? 3.851  -14.073 -0.800  0.40 18.44 ?  167  SER   A CA   1 
ATOM   3725 C  C    A SER   A 1 167 ? 5.060  -14.589 -0.933  0.60 17.82 ?  167  SER   A C    1 
ATOM   3726 C  C    B SER   A 1 167 ? 5.143  -14.839 -0.556  0.40 18.59 ?  167  SER   A C    1 
ATOM   3727 O  O    A SER   A 1 167 ? 5.499  -15.318 -1.827  0.60 18.29 ?  167  SER   A O    1 
ATOM   3728 O  O    B SER   A 1 167 ? 6.000  -14.883 -1.443  0.40 19.71 ?  167  SER   A O    1 
ATOM   3729 C  CB   A SER   A 1 167 ? 4.362  -12.614 -2.311  0.60 17.76 ?  167  SER   A CB   1 
ATOM   3730 C  CB   B SER   A 1 167 ? 3.992  -13.335 -2.134  0.40 19.22 ?  167  SER   A CB   1 
ATOM   3731 O  OG   A SER   A 1 167 ? 5.410  -11.788 -1.815  0.60 17.70 ?  167  SER   A OG   1 
ATOM   3732 O  OG   B SER   A 1 167 ? 5.229  -12.638 -2.211  0.40 19.74 ?  167  SER   A OG   1 
ATOM   3733 H  H    A SER   A 1 167 ? 3.823  -12.234 0.133   0.60 21.40 ?  167  SER   A H    1 
ATOM   3734 H  H    B SER   A 1 167 ? 4.057  -12.452 0.320   0.40 21.30 ?  167  SER   A H    1 
ATOM   3735 H  HA   A SER   A 1 167 ? 3.198  -14.154 -1.641  0.60 21.48 ?  167  SER   A HA   1 
ATOM   3736 H  HA   B SER   A 1 167 ? 3.137  -14.719 -0.886  0.40 22.15 ?  167  SER   A HA   1 
ATOM   3737 H  HB2  A SER   A 1 167 ? 4.689  -13.093 -3.092  0.60 21.34 ?  167  SER   A HB2  1 
ATOM   3738 H  HB2  B SER   A 1 167 ? 3.950  -13.986 -2.853  0.40 23.09 ?  167  SER   A HB2  1 
ATOM   3739 H  HB3  A SER   A 1 167 ? 3.592  -12.069 -2.570  0.60 21.34 ?  167  SER   A HB3  1 
ATOM   3740 H  HB3  B SER   A 1 167 ? 3.264  -12.703 -2.217  0.40 23.09 ?  167  SER   A HB3  1 
ATOM   3741 H  HG   A SER   A 1 167 ? 5.235  -11.567 -1.022  0.60 21.27 ?  167  SER   A HG   1 
ATOM   3742 H  HG   B SER   A 1 167 ? 5.858  -13.182 -2.328  0.40 23.72 ?  167  SER   A HG   1 
ATOM   3743 N  N    A PHE   A 1 168 ? 5.536  -14.629 0.312   0.60 16.94 ?  168  PHE   A N    1 
ATOM   3744 N  N    B PHE   A 1 168 ? 5.292  -15.474 0.606   0.40 17.37 ?  168  PHE   A N    1 
ATOM   3745 C  CA   A PHE   A 1 168 ? 6.704  -15.447 0.608   0.60 16.99 ?  168  PHE   A CA   1 
ATOM   3746 C  CA   B PHE   A 1 168 ? 6.555  -16.113 0.959   0.40 16.75 ?  168  PHE   A CA   1 
ATOM   3747 C  C    A PHE   A 1 168 ? 6.364  -16.923 0.494   0.60 17.93 ?  168  PHE   A C    1 
ATOM   3748 C  C    B PHE   A 1 168 ? 6.518  -17.632 0.898   0.40 16.97 ?  168  PHE   A C    1 
ATOM   3749 O  O    A PHE   A 1 168 ? 5.381  -17.394 1.074   0.60 18.68 ?  168  PHE   A O    1 
ATOM   3750 O  O    B PHE   A 1 168 ? 7.397  -18.240 0.274   0.40 17.11 ?  168  PHE   A O    1 
ATOM   3751 C  CB   A PHE   A 1 168 ? 7.256  -15.181 2.003   0.60 16.19 ?  168  PHE   A CB   1 
ATOM   3752 C  CB   B PHE   A 1 168 ? 7.023  -15.654 2.347   0.40 16.70 ?  168  PHE   A CB   1 
ATOM   3753 C  CG   A PHE   A 1 168 ? 8.484  -15.994 2.302   0.60 15.63 ?  168  PHE   A CG   1 
ATOM   3754 C  CG   B PHE   A 1 168 ? 8.385  -16.163 2.721   0.40 17.04 ?  168  PHE   A CG   1 
ATOM   3755 C  CD1  A PHE   A 1 168 ? 9.678  -15.707 1.666   0.60 15.74 ?  168  PHE   A CD1  1 
ATOM   3756 C  CD1  B PHE   A 1 168 ? 9.522  -15.620 2.146   0.40 16.98 ?  168  PHE   A CD1  1 
ATOM   3757 C  CD2  A PHE   A 1 168 ? 8.444  -17.069 3.175   0.60 15.31 ?  168  PHE   A CD2  1 
ATOM   3758 C  CD2  B PHE   A 1 168 ? 8.533  -17.184 3.645   0.40 17.05 ?  168  PHE   A CD2  1 
ATOM   3759 C  CE1  A PHE   A 1 168 ? 10.815 -16.454 1.914   0.60 15.08 ?  168  PHE   A CE1  1 
ATOM   3760 C  CE1  B PHE   A 1 168 ? 10.780 -16.085 2.485   0.40 16.90 ?  168  PHE   A CE1  1 
ATOM   3761 C  CE2  A PHE   A 1 168 ? 9.585  -17.820 3.427   0.60 15.18 ?  168  PHE   A CE2  1 
ATOM   3762 C  CE2  B PHE   A 1 168 ? 9.788  -17.650 3.988   0.40 16.97 ?  168  PHE   A CE2  1 
ATOM   3763 C  CZ   A PHE   A 1 168 ? 10.771 -17.507 2.794   0.60 15.00 ?  168  PHE   A CZ   1 
ATOM   3764 C  CZ   B PHE   A 1 168 ? 10.912 -17.101 3.407   0.40 17.02 ?  168  PHE   A CZ   1 
ATOM   3765 H  H    A PHE   A 1 168 ? 5.202  -14.204 0.982   0.60 20.36 ?  168  PHE   A H    1 
ATOM   3766 H  H    B PHE   A 1 168 ? 4.676  -15.557 1.204   0.40 20.88 ?  168  PHE   A H    1 
ATOM   3767 H  HA   A PHE   A 1 168 ? 7.397  -15.246 -0.038  0.60 20.42 ?  168  PHE   A HA   1 
ATOM   3768 H  HA   B PHE   A 1 168 ? 7.231  -15.830 0.328   0.40 20.13 ?  168  PHE   A HA   1 
ATOM   3769 H  HB2  A PHE   A 1 168 ? 7.497  -14.247 2.080   0.60 19.45 ?  168  PHE   A HB2  1 
ATOM   3770 H  HB2  B PHE   A 1 168 ? 7.058  -14.686 2.357   0.40 20.07 ?  168  PHE   A HB2  1 
ATOM   3771 H  HB3  A PHE   A 1 168 ? 6.576  -15.403 2.660   0.60 19.45 ?  168  PHE   A HB3  1 
ATOM   3772 H  HB3  B PHE   A 1 168 ? 6.396  -15.972 3.012   0.40 20.07 ?  168  PHE   A HB3  1 
ATOM   3773 H  HD1  A PHE   A 1 168 ? 9.720  -14.993 1.071   0.60 18.91 ?  168  PHE   A HD1  1 
ATOM   3774 H  HD1  B PHE   A 1 168 ? 9.440  -14.935 1.523   0.40 20.40 ?  168  PHE   A HD1  1 
ATOM   3775 H  HD2  A PHE   A 1 168 ? 7.646  -17.283 3.606   0.60 18.40 ?  168  PHE   A HD2  1 
ATOM   3776 H  HD2  B PHE   A 1 168 ? 7.779  -17.558 4.040   0.40 20.48 ?  168  PHE   A HD2  1 
ATOM   3777 H  HE1  A PHE   A 1 168 ? 11.614 -16.246 1.486   0.60 18.12 ?  168  PHE   A HE1  1 
ATOM   3778 H  HE1  B PHE   A 1 168 ? 11.537 -15.710 2.093   0.40 20.31 ?  168  PHE   A HE1  1 
ATOM   3779 H  HE2  A PHE   A 1 168 ? 9.548  -18.537 4.021   0.60 18.24 ?  168  PHE   A HE2  1 
ATOM   3780 H  HE2  B PHE   A 1 168 ? 9.873  -18.335 4.611   0.40 20.39 ?  168  PHE   A HE2  1 
ATOM   3781 H  HZ   A PHE   A 1 168 ? 11.534 -18.014 2.958   0.60 18.02 ?  168  PHE   A HZ   1 
ATOM   3782 H  HZ   B PHE   A 1 168 ? 11.757 -17.413 3.639   0.40 20.45 ?  168  PHE   A HZ   1 
ATOM   3783 N  N    A LEU   A 1 169 ? 7.204  -17.660 -0.224  0.60 18.90 ?  169  LEU   A N    1 
ATOM   3784 N  N    B LEU   A 1 169 ? 5.544  -18.269 1.542   0.40 17.42 ?  169  LEU   A N    1 
ATOM   3785 C  CA   A LEU   A 1 169 ? 7.009  -19.093 -0.368  0.60 20.62 ?  169  LEU   A CA   1 
ATOM   3786 C  CA   B LEU   A 1 169 ? 5.529  -19.729 1.625   0.40 18.74 ?  169  LEU   A CA   1 
ATOM   3787 C  C    A LEU   A 1 169 ? 7.852  -19.856 0.651   0.60 20.90 ?  169  LEU   A C    1 
ATOM   3788 C  C    B LEU   A 1 169 ? 5.004  -20.375 0.345   0.40 19.74 ?  169  LEU   A C    1 
ATOM   3789 O  O    A LEU   A 1 169 ? 7.318  -20.334 1.653   0.60 21.43 ?  169  LEU   A O    1 
ATOM   3790 O  O    B LEU   A 1 169 ? 4.092  -19.867 -0.310  0.40 20.09 ?  169  LEU   A O    1 
ATOM   3791 C  CB   A LEU   A 1 169 ? 7.343  -19.542 -1.793  0.60 21.84 ?  169  LEU   A CB   1 
ATOM   3792 C  CB   B LEU   A 1 169 ? 4.697  -20.200 2.821   0.40 18.98 ?  169  LEU   A CB   1 
ATOM   3793 C  CG   A LEU   A 1 169 ? 7.069  -21.014 -2.112  0.60 22.92 ?  169  LEU   A CG   1 
ATOM   3794 C  CG   B LEU   A 1 169 ? 4.882  -21.674 3.194   0.40 19.22 ?  169  LEU   A CG   1 
ATOM   3795 C  CD1  A LEU   A 1 169 ? 5.651  -21.408 -1.722  0.60 23.27 ?  169  LEU   A CD1  1 
ATOM   3796 C  CD1  B LEU   A 1 169 ? 6.316  -21.931 3.638   0.40 19.58 ?  169  LEU   A CD1  1 
ATOM   3797 C  CD2  A LEU   A 1 169 ? 7.310  -21.297 -3.589  0.60 23.31 ?  169  LEU   A CD2  1 
ATOM   3798 C  CD2  B LEU   A 1 169 ? 3.900  -22.087 4.280   0.40 19.36 ?  169  LEU   A CD2  1 
ATOM   3799 O  OXT  A LEU   A 1 169 ? 9.068  -20.009 0.514   0.60 20.94 -1 169  LEU   A OXT  1 
ATOM   3800 O  OXT  B LEU   A 1 169 ? 5.485  -21.436 -0.056  0.40 20.57 -1 169  LEU   A OXT  1 
ATOM   3801 H  H    A LEU   A 1 169 ? 7.897  -17.354 -0.631  0.60 22.71 ?  169  LEU   A H    1 
ATOM   3802 H  H    B LEU   A 1 169 ? 4.886  -17.884 1.943   0.40 20.93 ?  169  LEU   A H    1 
ATOM   3803 H  HA   A LEU   A 1 169 ? 6.080  -19.299 -0.195  0.60 24.77 ?  169  LEU   A HA   1 
ATOM   3804 H  HA   B LEU   A 1 169 ? 6.439  -20.033 1.759   0.40 22.52 ?  169  LEU   A HA   1 
ATOM   3805 H  HB2  A LEU   A 1 169 ? 6.813  -19.011 -2.409  0.60 26.23 ?  169  LEU   A HB2  1 
ATOM   3806 H  HB2  B LEU   A 1 169 ? 4.938  -19.672 3.597   0.40 22.80 ?  169  LEU   A HB2  1 
ATOM   3807 H  HB3  A LEU   A 1 169 ? 8.283  -19.383 -1.954  0.60 26.23 ?  169  LEU   A HB3  1 
ATOM   3808 H  HB3  B LEU   A 1 169 ? 3.758  -20.071 2.617   0.40 22.80 ?  169  LEU   A HB3  1 
ATOM   3809 H  HG   A LEU   A 1 169 ? 7.680  -21.567 -1.602  0.60 27.53 ?  169  LEU   A HG   1 
ATOM   3810 H  HG   B LEU   A 1 169 ? 4.713  -22.223 2.413   0.40 23.09 ?  169  LEU   A HG   1 
ATOM   3811 H  HD11 A LEU   A 1 169 ? 5.447  -22.278 -2.103  0.60 27.95 ?  169  LEU   A HD11 1 
ATOM   3812 H  HD11 B LEU   A 1 169 ? 6.363  -22.796 4.073   0.40 23.52 ?  169  LEU   A HD11 1 
ATOM   3813 H  HD12 A LEU   A 1 169 ? 5.587  -21.450 -0.755  0.60 27.95 ?  169  LEU   A HD12 1 
ATOM   3814 H  HD12 B LEU   A 1 169 ? 6.897  -21.921 2.860   0.40 23.52 ?  169  LEU   A HD12 1 
ATOM   3815 H  HD13 A LEU   A 1 169 ? 5.031  -20.746 -2.068  0.60 27.95 ?  169  LEU   A HD13 1 
ATOM   3816 H  HD13 B LEU   A 1 169 ? 6.585  -21.235 4.260   0.40 23.52 ?  169  LEU   A HD13 1 
ATOM   3817 H  HD21 A LEU   A 1 169 ? 7.135  -22.236 -3.763  0.60 28.00 ?  169  LEU   A HD21 1 
ATOM   3818 H  HD21 B LEU   A 1 169 ? 4.040  -23.024 4.492   0.40 23.26 ?  169  LEU   A HD21 1 
ATOM   3819 H  HD22 A LEU   A 1 169 ? 6.711  -20.747 -4.118  0.60 28.00 ?  169  LEU   A HD22 1 
ATOM   3820 H  HD22 B LEU   A 1 169 ? 4.056  -21.543 5.068   0.40 23.26 ?  169  LEU   A HD22 1 
ATOM   3821 H  HD23 A LEU   A 1 169 ? 8.231  -21.086 -3.803  0.60 28.00 ?  169  LEU   A HD23 1 
ATOM   3822 H  HD23 B LEU   A 1 169 ? 2.998  -21.951 3.955   0.40 23.26 ?  169  LEU   A HD23 1 
ATOM   3823 N  N    A SER   B 1 1   ? 50.737 -9.196  -23.740 0.60 28.64 ?  1    SER   B N    1 
ATOM   3824 N  N    B SER   B 1 1   ? 50.849 -9.253  -23.828 0.40 23.80 ?  1    SER   B N    1 
ATOM   3825 C  CA   A SER   B 1 1   ? 51.243 -10.261 -22.850 0.60 28.23 ?  1    SER   B CA   1 
ATOM   3826 C  CA   B SER   B 1 1   ? 51.262 -10.223 -22.793 0.40 23.62 ?  1    SER   B CA   1 
ATOM   3827 C  C    A SER   B 1 1   ? 50.181 -11.322 -22.612 0.60 26.75 ?  1    SER   B C    1 
ATOM   3828 C  C    B SER   B 1 1   ? 50.157 -11.235 -22.528 0.40 22.84 ?  1    SER   B C    1 
ATOM   3829 O  O    A SER   B 1 1   ? 48.985 -11.111 -22.853 0.60 26.14 ?  1    SER   B O    1 
ATOM   3830 O  O    B SER   B 1 1   ? 49.005 -11.065 -22.945 0.40 22.54 ?  1    SER   B O    1 
ATOM   3831 C  CB   A SER   B 1 1   ? 51.686 -9.681  -21.510 0.60 29.15 ?  1    SER   B CB   1 
ATOM   3832 C  CB   B SER   B 1 1   ? 51.625 -9.508  -21.496 0.40 24.08 ?  1    SER   B CB   1 
ATOM   3833 O  OG   A SER   B 1 1   ? 50.566 -9.271  -20.751 0.60 30.69 ?  1    SER   B OG   1 
ATOM   3834 O  OG   B SER   B 1 1   ? 50.556 -9.577  -20.570 0.40 25.20 ?  1    SER   B OG   1 
ATOM   3835 H  H1   A SER   B 1 1   ? 50.556 -9.545  -24.536 0.60 34.40 ?  1    SER   B H1   1 
ATOM   3836 H  H1   B SER   B 1 1   ? 51.571 -8.835  -24.134 0.40 28.59 ?  1    SER   B H1   1 
ATOM   3837 H  H2   A SER   B 1 1   ? 50.004 -8.847  -23.386 0.60 34.40 ?  1    SER   B H2   1 
ATOM   3838 H  H2   B SER   B 1 1   ? 50.450 -9.689  -24.489 0.40 28.59 ?  1    SER   B H2   1 
ATOM   3839 H  H3   A SER   B 1 1   ? 51.363 -8.571  -23.821 0.60 34.40 ?  1    SER   B H3   1 
ATOM   3840 H  H3   B SER   B 1 1   ? 50.290 -8.668  -23.467 0.40 28.59 ?  1    SER   B H3   1 
ATOM   3841 H  HA   A SER   B 1 1   ? 52.005 -10.676 -23.276 0.60 33.91 ?  1    SER   B HA   1 
ATOM   3842 H  HA   B SER   B 1 1   ? 52.045 -10.693 -23.112 0.40 28.37 ?  1    SER   B HA   1 
ATOM   3843 H  HB2  A SER   B 1 1   ? 52.174 -10.366 -21.026 0.60 35.01 ?  1    SER   B HB2  1 
ATOM   3844 H  HB2  B SER   B 1 1   ? 52.406 -9.935  -21.114 0.40 28.92 ?  1    SER   B HB2  1 
ATOM   3845 H  HB3  A SER   B 1 1   ? 52.255 -8.915  -21.668 0.60 35.01 ?  1    SER   B HB3  1 
ATOM   3846 H  HB3  B SER   B 1 1   ? 51.818 -8.577  -21.691 0.40 28.92 ?  1    SER   B HB3  1 
ATOM   3847 H  HG   A SER   B 1 1   ? 50.812 -8.758  -20.135 0.60 36.86 ?  1    SER   B HG   1 
ATOM   3848 H  HG   B SER   B 1 1   ? 50.546 -8.882  -20.098 0.40 30.27 ?  1    SER   B HG   1 
ATOM   3849 N  N    A MET   B 1 2   ? 50.640 -12.463 -22.117 0.60 25.91 ?  2    MET   B N    1 
ATOM   3850 N  N    B MET   B 1 2   ? 50.528 -12.282 -21.803 0.40 22.43 ?  2    MET   B N    1 
ATOM   3851 C  CA   A MET   B 1 2   ? 49.816 -13.650 -21.940 0.60 25.67 ?  2    MET   B CA   1 
ATOM   3852 C  CA   B MET   B 1 2   ? 49.702 -13.468 -21.621 0.40 22.51 ?  2    MET   B CA   1 
ATOM   3853 C  C    A MET   B 1 2   ? 49.588 -13.860 -20.450 0.60 22.75 ?  2    MET   B C    1 
ATOM   3854 C  C    B MET   B 1 2   ? 49.431 -13.621 -20.131 0.40 20.28 ?  2    MET   B C    1 
ATOM   3855 O  O    A MET   B 1 2   ? 50.534 -14.127 -19.703 0.60 22.74 ?  2    MET   B O    1 
ATOM   3856 O  O    B MET   B 1 2   ? 50.341 -13.955 -19.363 0.40 20.41 ?  2    MET   B O    1 
ATOM   3857 C  CB   A MET   B 1 2   ? 50.521 -14.851 -22.553 0.60 29.32 ?  2    MET   B CB   1 
ATOM   3858 C  CB   B MET   B 1 2   ? 50.453 -14.678 -22.169 0.40 25.50 ?  2    MET   B CB   1 
ATOM   3859 C  CG   A MET   B 1 2   ? 49.650 -16.084 -22.693 0.60 32.52 ?  2    MET   B CG   1 
ATOM   3860 C  CG   B MET   B 1 2   ? 49.589 -15.819 -22.672 0.40 27.91 ?  2    MET   B CG   1 
ATOM   3861 S  SD   A MET   B 1 2   ? 50.465 -17.363 -23.664 0.60 35.35 ?  2    MET   B SD   1 
ATOM   3862 S  SD   B MET   B 1 2   ? 50.529 -16.933 -23.727 0.40 30.04 ?  2    MET   B SD   1 
ATOM   3863 C  CE   A MET   B 1 2   ? 51.075 -16.357 -25.012 0.60 35.68 ?  2    MET   B CE   1 
ATOM   3864 C  CE   B MET   B 1 2   ? 51.359 -15.762 -24.786 0.40 30.21 ?  2    MET   B CE   1 
ATOM   3865 H  H    A MET   B 1 2   ? 51.456 -12.578 -21.873 0.60 31.12 ?  2    MET   B H    1 
ATOM   3866 H  H    B MET   B 1 2   ? 51.282 -12.339 -21.393 0.40 26.95 ?  2    MET   B H    1 
ATOM   3867 H  HA   A MET   B 1 2   ? 48.967 -13.533 -22.391 0.60 30.83 ?  2    MET   B HA   1 
ATOM   3868 H  HA   B MET   B 1 2   ? 48.871 -13.382 -22.109 0.40 27.04 ?  2    MET   B HA   1 
ATOM   3869 H  HB2  A MET   B 1 2   ? 50.827 -14.573 -23.425 0.60 35.21 ?  2    MET   B HB2  1 
ATOM   3870 H  HB2  B MET   B 1 2   ? 51.006 -14.356 -22.893 0.40 30.63 ?  2    MET   B HB2  1 
ATOM   3871 H  HB3  A MET   B 1 2   ? 51.280 -15.099 -22.004 0.60 35.21 ?  2    MET   B HB3  1 
ATOM   3872 H  HB3  B MET   B 1 2   ? 51.016 -15.050 -21.481 0.40 30.63 ?  2    MET   B HB3  1 
ATOM   3873 H  HG2  A MET   B 1 2   ? 49.461 -16.435 -21.807 0.60 39.06 ?  2    MET   B HG2  1 
ATOM   3874 H  HG2  B MET   B 1 2   ? 49.256 -16.326 -21.913 0.40 33.52 ?  2    MET   B HG2  1 
ATOM   3875 H  HG3  A MET   B 1 2   ? 48.826 -15.847 -23.146 0.60 39.06 ?  2    MET   B HG3  1 
ATOM   3876 H  HG3  B MET   B 1 2   ? 48.852 -15.477 -23.192 0.40 33.52 ?  2    MET   B HG3  1 
ATOM   3877 H  HE1  A MET   B 1 2   ? 51.251 -16.928 -25.762 0.60 42.85 ?  2    MET   B HE1  1 
ATOM   3878 H  HE1  B MET   B 1 2   ? 51.568 -16.199 -25.613 0.40 36.28 ?  2    MET   B HE1  1 
ATOM   3879 H  HE2  A MET   B 1 2   ? 50.392 -15.701 -25.240 0.60 42.85 ?  2    MET   B HE2  1 
ATOM   3880 H  HE2  B MET   B 1 2   ? 50.766 -15.009 -24.944 0.40 36.28 ?  2    MET   B HE2  1 
ATOM   3881 H  HE3  A MET   B 1 2   ? 51.891 -15.897 -24.740 0.60 42.85 ?  2    MET   B HE3  1 
ATOM   3882 H  HE3  B MET   B 1 2   ? 52.173 -15.458 -24.347 0.40 36.28 ?  2    MET   B HE3  1 
ATOM   3883 N  N    A VAL   B 1 3   ? 48.334 -13.735 -20.024 0.60 20.44 ?  3    VAL   B N    1 
ATOM   3884 N  N    B VAL   B 1 3   ? 48.194 -13.352 -19.719 0.40 18.40 ?  3    VAL   B N    1 
ATOM   3885 C  CA   A VAL   B 1 3   ? 47.937 -13.971 -18.644 0.60 19.16 ?  3    VAL   B CA   1 
ATOM   3886 C  CA   B VAL   B 1 3   ? 47.740 -13.624 -18.360 0.40 17.25 ?  3    VAL   B CA   1 
ATOM   3887 C  C    A VAL   B 1 3   ? 46.692 -14.843 -18.655 0.60 17.03 ?  3    VAL   B C    1 
ATOM   3888 C  C    B VAL   B 1 3   ? 46.497 -14.498 -18.428 0.40 16.03 ?  3    VAL   B C    1 
ATOM   3889 O  O    A VAL   B 1 3   ? 45.985 -14.944 -19.661 0.60 16.96 ?  3    VAL   B O    1 
ATOM   3890 O  O    B VAL   B 1 3   ? 45.658 -14.338 -19.320 0.40 15.67 ?  3    VAL   B O    1 
ATOM   3891 C  CB   A VAL   B 1 3   ? 47.642 -12.660 -17.888 0.60 20.48 ?  3    VAL   B CB   1 
ATOM   3892 C  CB   B VAL   B 1 3   ? 47.491 -12.342 -17.532 0.40 17.47 ?  3    VAL   B CB   1 
ATOM   3893 C  CG1  A VAL   B 1 3   ? 48.890 -11.794 -17.801 0.60 20.97 ?  3    VAL   B CG1  1 
ATOM   3894 C  CG1  B VAL   B 1 3   ? 48.786 -11.546 -17.384 0.40 17.84 ?  3    VAL   B CG1  1 
ATOM   3895 C  CG2  A VAL   B 1 3   ? 46.500 -11.913 -18.564 0.60 21.08 ?  3    VAL   B CG2  1 
ATOM   3896 C  CG2  B VAL   B 1 3   ? 46.395 -11.487 -18.148 0.40 17.37 ?  3    VAL   B CG2  1 
ATOM   3897 H  H    A VAL   B 1 3   ? 47.682 -13.514 -20.536 0.60 24.56 ?  3    VAL   B H    1 
ATOM   3898 H  H    B VAL   B 1 3   ? 47.588 -13.005 -20.225 0.40 22.11 ?  3    VAL   B H    1 
ATOM   3899 H  HA   A VAL   B 1 3   ? 48.657 -14.444 -18.182 0.60 23.02 ?  3    VAL   B HA   1 
ATOM   3900 H  HA   B VAL   B 1 3   ? 48.417 -14.133 -17.904 0.40 20.73 ?  3    VAL   B HA   1 
ATOM   3901 H  HB   A VAL   B 1 3   ? 47.366 -12.883 -16.984 0.60 24.61 ?  3    VAL   B HB   1 
ATOM   3902 H  HB   B VAL   B 1 3   ? 47.201 -12.595 -16.641 0.40 21.00 ?  3    VAL   B HB   1 
ATOM   3903 H  HG11 A VAL   B 1 3   ? 48.673 -10.988 -17.308 0.60 25.19 ?  3    VAL   B HG11 1 
ATOM   3904 H  HG11 B VAL   B 1 3   ? 48.617 -10.762 -16.839 0.40 21.43 ?  3    VAL   B HG11 1 
ATOM   3905 H  HG12 A VAL   B 1 3   ? 49.585 -12.289 -17.338 0.60 25.19 ?  3    VAL   B HG12 1 
ATOM   3906 H  HG12 B VAL   B 1 3   ? 49.455 -12.106 -16.960 0.40 21.43 ?  3    VAL   B HG12 1 
ATOM   3907 H  HG13 A VAL   B 1 3   ? 49.180 -11.571 -18.696 0.60 25.19 ?  3    VAL   B HG13 1 
ATOM   3908 H  HG13 B VAL   B 1 3   ? 49.092 -11.276 -18.265 0.40 21.43 ?  3    VAL   B HG13 1 
ATOM   3909 H  HG21 A VAL   B 1 3   ? 46.432 -11.031 -18.174 0.60 25.32 ?  3    VAL   B HG21 1 
ATOM   3910 H  HG21 B VAL   B 1 3   ? 46.343 -10.645 -17.667 0.40 20.87 ?  3    VAL   B HG21 1 
ATOM   3911 H  HG22 A VAL   B 1 3   ? 46.684 -11.844 -19.513 0.60 25.32 ?  3    VAL   B HG22 1 
ATOM   3912 H  HG22 B VAL   B 1 3   ? 46.609 -11.324 -19.079 0.40 20.87 ?  3    VAL   B HG22 1 
ATOM   3913 H  HG23 A VAL   B 1 3   ? 45.673 -12.402 -18.424 0.60 25.32 ?  3    VAL   B HG23 1 
ATOM   3914 H  HG23 B VAL   B 1 3   ? 45.550 -11.959 -18.079 0.40 20.87 ?  3    VAL   B HG23 1 
ATOM   3915 N  N    . ASN   B 1 4   ? 46.407 -15.449 -17.502 1.00 15.54 ?  4    ASN   B N    1 
ATOM   3916 C  CA   . ASN   B 1 4   ? 45.274 -16.370 -17.393 1.00 14.94 ?  4    ASN   B CA   1 
ATOM   3917 C  C    . ASN   B 1 4   ? 45.233 -17.332 -18.580 1.00 15.02 ?  4    ASN   B C    1 
ATOM   3918 O  O    . ASN   B 1 4   ? 44.176 -17.597 -19.149 1.00 15.98 ?  4    ASN   B O    1 
ATOM   3919 C  CB   . ASN   B 1 4   ? 43.942 -15.631 -17.224 1.00 14.14 ?  4    ASN   B CB   1 
ATOM   3920 C  CG   . ASN   B 1 4   ? 43.892 -14.812 -15.949 1.00 13.46 ?  4    ASN   B CG   1 
ATOM   3921 O  OD1  . ASN   B 1 4   ? 44.171 -15.320 -14.866 1.00 13.08 ?  4    ASN   B OD1  1 
ATOM   3922 N  ND2  . ASN   B 1 4   ? 43.545 -13.535 -16.073 1.00 14.39 ?  4    ASN   B ND2  1 
ATOM   3923 H  H    A ASN   B 1 4   ? 46.842 -15.333 -16.771 0.60 18.68 ?  4    ASN   B H    1 
ATOM   3924 H  H    B ASN   B 1 4   ? 47.018 -15.590 -16.913 0.40 18.68 ?  4    ASN   B H    1 
ATOM   3925 H  HA   . ASN   B 1 4   ? 45.407 -16.908 -16.595 1.00 17.95 ?  4    ASN   B HA   1 
ATOM   3926 H  HB2  . ASN   B 1 4   ? 43.807 -15.033 -17.970 1.00 16.99 ?  4    ASN   B HB2  1 
ATOM   3927 H  HB3  . ASN   B 1 4   ? 43.224 -16.284 -17.187 1.00 16.99 ?  4    ASN   B HB3  1 
ATOM   3928 H  HD21 . ASN   B 1 4   ? 43.502 -13.031 -15.376 1.00 17.30 ?  4    ASN   B HD21 1 
ATOM   3929 H  HD22 . ASN   B 1 4   ? 43.356 -13.214 -16.847 1.00 17.30 ?  4    ASN   B HD22 1 
ATOM   3930 N  N    . SER   B 1 5   ? 46.399 -17.853 -18.961 1.00 15.92 ?  5    SER   B N    1 
ATOM   3931 C  CA   . SER   B 1 5   ? 46.503 -18.761 -20.105 1.00 18.23 ?  5    SER   B CA   1 
ATOM   3932 C  C    . SER   B 1 5   ? 46.468 -20.201 -19.606 1.00 19.74 ?  5    SER   B C    1 
ATOM   3933 O  O    . SER   B 1 5   ? 47.457 -20.930 -19.630 1.00 22.08 ?  5    SER   B O    1 
ATOM   3934 C  CB   . SER   B 1 5   ? 47.770 -18.473 -20.904 1.00 19.56 ?  5    SER   B CB   1 
ATOM   3935 O  OG   . SER   B 1 5   ? 48.931 -18.685 -20.120 1.00 22.00 ?  5    SER   B OG   1 
ATOM   3936 H  H    . SER   B 1 5   ? 47.150 -17.698 -18.567 1.00 19.13 ?  5    SER   B H    1 
ATOM   3937 H  HA   . SER   B 1 5   ? 45.742 -18.626 -20.687 1.00 21.90 ?  5    SER   B HA   1 
ATOM   3938 H  HB2  . SER   B 1 5   ? 47.790 -19.056 -21.681 1.00 23.50 ?  5    SER   B HB2  1 
ATOM   3939 H  HB3  . SER   B 1 5   ? 47.731 -17.549 -21.188 1.00 23.50 ?  5    SER   B HB3  1 
ATOM   3940 H  HG   . SER   B 1 5   ? 48.976 -19.493 -19.893 1.00 26.43 ?  5    SER   B HG   1 
ATOM   3941 N  N    . PHE   B 1 6   ? 45.290 -20.591 -19.130 1.00 19.70 ?  6    PHE   B N    1 
ATOM   3942 C  CA   . PHE   B 1 6   ? 45.082 -21.944 -18.639 1.00 19.18 ?  6    PHE   B CA   1 
ATOM   3943 C  C    . PHE   B 1 6   ? 45.001 -22.911 -19.811 1.00 21.97 ?  6    PHE   B C    1 
ATOM   3944 O  O    . PHE   B 1 6   ? 44.360 -22.623 -20.825 1.00 24.28 ?  6    PHE   B O    1 
ATOM   3945 C  CB   . PHE   B 1 6   ? 43.787 -22.001 -17.829 1.00 17.55 ?  6    PHE   B CB   1 
ATOM   3946 C  CG   . PHE   B 1 6   ? 43.810 -21.152 -16.590 1.00 15.63 ?  6    PHE   B CG   1 
ATOM   3947 C  CD1  . PHE   B 1 6   ? 44.330 -21.651 -15.414 1.00 14.27 ?  6    PHE   B CD1  1 
ATOM   3948 C  CD2  . PHE   B 1 6   ? 43.315 -19.855 -16.600 1.00 15.20 ?  6    PHE   B CD2  1 
ATOM   3949 C  CE1  . PHE   B 1 6   ? 44.352 -20.879 -14.260 1.00 13.92 ?  6    PHE   B CE1  1 
ATOM   3950 C  CE2  . PHE   B 1 6   ? 43.340 -19.072 -15.452 1.00 15.43 ?  6    PHE   B CE2  1 
ATOM   3951 C  CZ   . PHE   B 1 6   ? 43.864 -19.581 -14.283 1.00 14.33 ?  6    PHE   B CZ   1 
ATOM   3952 H  H    . PHE   B 1 6   ? 44.591 -20.093 -19.088 1.00 23.67 ?  6    PHE   B H    1 
ATOM   3953 H  HA   . PHE   B 1 6   ? 45.815 -22.208 -18.067 1.00 23.04 ?  6    PHE   B HA   1 
ATOM   3954 H  HB2  . PHE   B 1 6   ? 43.052 -21.695 -18.383 1.00 21.09 ?  6    PHE   B HB2  1 
ATOM   3955 H  HB3  . PHE   B 1 6   ? 43.626 -22.919 -17.553 1.00 21.09 ?  6    PHE   B HB3  1 
ATOM   3956 H  HD1  . PHE   B 1 6   ? 44.668 -22.517 -15.388 1.00 17.15 ?  6    PHE   B HD1  1 
ATOM   3957 H  HD2  . PHE   B 1 6   ? 42.958 -19.508 -17.384 1.00 18.26 ?  6    PHE   B HD2  1 
ATOM   3958 H  HE1  . PHE   B 1 6   ? 44.715 -21.222 -13.471 1.00 16.73 ?  6    PHE   B HE1  1 
ATOM   3959 H  HE2  . PHE   B 1 6   ? 43.001 -18.205 -15.471 1.00 18.54 ?  6    PHE   B HE2  1 
ATOM   3960 H  HZ   . PHE   B 1 6   ? 43.881 -19.063 -13.511 1.00 17.23 ?  6    PHE   B HZ   1 
ATOM   3961 N  N    . SER   B 1 7   ? 45.662 -24.061 -19.670 1.00 22.85 ?  7    SER   B N    1 
ATOM   3962 C  CA   . SER   B 1 7   ? 45.741 -25.043 -20.743 1.00 25.34 ?  7    SER   B CA   1 
ATOM   3963 C  C    . SER   B 1 7   ? 45.700 -26.454 -20.175 1.00 24.89 ?  7    SER   B C    1 
ATOM   3964 O  O    . SER   B 1 7   ? 46.313 -26.738 -19.142 1.00 26.07 ?  7    SER   B O    1 
ATOM   3965 C  CB   . SER   B 1 7   ? 47.028 -24.859 -21.557 1.00 27.92 ?  7    SER   B CB   1 
ATOM   3966 O  OG   . SER   B 1 7   ? 47.055 -25.733 -22.670 1.00 29.87 ?  7    SER   B OG   1 
ATOM   3967 H  H    . SER   B 1 7   ? 46.076 -24.295 -18.948 1.00 27.45 ?  7    SER   B H    1 
ATOM   3968 H  HA   . SER   B 1 7   ? 44.984 -24.934 -21.334 1.00 30.44 ?  7    SER   B HA   1 
ATOM   3969 H  HB2  . SER   B 1 7   ? 47.070 -23.943 -21.874 1.00 33.53 ?  7    SER   B HB2  1 
ATOM   3970 H  HB3  . SER   B 1 7   ? 47.792 -25.048 -20.988 1.00 33.53 ?  7    SER   B HB3  1 
ATOM   3971 H  HG   . SER   B 1 7   ? 47.764 -25.621 -23.107 1.00 35.87 ?  7    SER   B HG   1 
ATOM   3972 N  N    . GLY   B 1 8   ? 44.983 -27.337 -20.867 1.00 24.75 ?  8    GLY   B N    1 
ATOM   3973 C  CA   . GLY   B 1 8   ? 44.953 -28.734 -20.496 1.00 24.08 ?  8    GLY   B CA   1 
ATOM   3974 C  C    . GLY   B 1 8   ? 44.022 -29.076 -19.361 1.00 22.67 ?  8    GLY   B C    1 
ATOM   3975 O  O    . GLY   B 1 8   ? 44.169 -30.147 -18.758 1.00 24.09 ?  8    GLY   B O    1 
ATOM   3976 H  H    . GLY   B 1 8   ? 44.509 -27.142 -21.556 1.00 29.72 ?  8    GLY   B H    1 
ATOM   3977 H  HA2  . GLY   B 1 8   ? 44.683 -29.256 -21.268 1.00 28.92 ?  8    GLY   B HA2  1 
ATOM   3978 H  HA3  . GLY   B 1 8   ? 45.842 -29.012 -20.239 1.00 28.92 ?  8    GLY   B HA3  1 
ATOM   3979 N  N    . TYR   B 1 9   ? 43.050 -28.219 -19.060 1.00 20.58 ?  9    TYR   B N    1 
ATOM   3980 C  CA   . TYR   B 1 9   ? 42.098 -28.507 -18.001 1.00 18.40 ?  9    TYR   B CA   1 
ATOM   3981 C  C    . TYR   B 1 9   ? 40.920 -29.302 -18.530 1.00 17.87 ?  9    TYR   B C    1 
ATOM   3982 O  O    . TYR   B 1 9   ? 40.497 -29.152 -19.681 1.00 19.88 ?  9    TYR   B O    1 
ATOM   3983 C  CB   . TYR   B 1 9   ? 41.578 -27.227 -17.349 1.00 17.70 ?  9    TYR   B CB   1 
ATOM   3984 C  CG   . TYR   B 1 9   ? 42.602 -26.591 -16.442 1.00 17.33 ?  9    TYR   B CG   1 
ATOM   3985 C  CD1  . TYR   B 1 9   ? 43.688 -25.913 -16.969 1.00 17.81 ?  9    TYR   B CD1  1 
ATOM   3986 C  CD2  . TYR   B 1 9   ? 42.499 -26.692 -15.063 1.00 16.69 ?  9    TYR   B CD2  1 
ATOM   3987 C  CE1  . TYR   B 1 9   ? 44.642 -25.345 -16.151 1.00 18.18 ?  9    TYR   B CE1  1 
ATOM   3988 C  CE2  . TYR   B 1 9   ? 43.449 -26.126 -14.234 1.00 17.12 ?  9    TYR   B CE2  1 
ATOM   3989 C  CZ   . TYR   B 1 9   ? 44.520 -25.453 -14.785 1.00 18.04 ?  9    TYR   B CZ   1 
ATOM   3990 O  OH   . TYR   B 1 9   ? 45.470 -24.893 -13.966 1.00 18.74 ?  9    TYR   B OH   1 
ATOM   3991 H  H    . TYR   B 1 9   ? 42.905 -27.476 -19.465 1.00 24.73 ?  9    TYR   B H    1 
ATOM   3992 H  HA   . TYR   B 1 9   ? 42.527 -29.038 -17.314 1.00 22.11 ?  9    TYR   B HA   1 
ATOM   3993 H  HB2  . TYR   B 1 9   ? 41.335 -26.586 -18.037 1.00 21.26 ?  9    TYR   B HB2  1 
ATOM   3994 H  HB3  . TYR   B 1 9   ? 40.802 -27.453 -16.814 1.00 21.26 ?  9    TYR   B HB3  1 
ATOM   3995 H  HD1  . TYR   B 1 9   ? 43.771 -25.845 -17.894 1.00 21.40 ?  9    TYR   B HD1  1 
ATOM   3996 H  HD2  . TYR   B 1 9   ? 41.773 -27.152 -14.689 1.00 20.06 ?  9    TYR   B HD2  1 
ATOM   3997 H  HE1  . TYR   B 1 9   ? 45.357 -24.897 -16.522 1.00 21.85 ?  9    TYR   B HE1  1 
ATOM   3998 H  HE2  . TYR   B 1 9   ? 43.357 -26.204 -13.311 1.00 20.57 ?  9    TYR   B HE2  1 
ATOM   3999 H  HH   . TYR   B 1 9   ? 46.056 -24.520 -14.430 1.00 22.52 ?  9    TYR   B HH   1 
ATOM   4000 N  N    . LEU   B 1 10  ? 40.397 -30.160 -17.665 1.00 16.17 ?  10   LEU   B N    1 
ATOM   4001 C  CA   . LEU   B 1 10  ? 39.188 -30.915 -17.938 1.00 16.27 ?  10   LEU   B CA   1 
ATOM   4002 C  C    . LEU   B 1 10  ? 38.003 -30.148 -17.366 1.00 15.71 ?  10   LEU   B C    1 
ATOM   4003 O  O    . LEU   B 1 10  ? 38.021 -29.738 -16.202 1.00 15.44 ?  10   LEU   B O    1 
ATOM   4004 C  CB   . LEU   B 1 10  ? 39.294 -32.292 -17.282 1.00 17.13 ?  10   LEU   B CB   1 
ATOM   4005 C  CG   . LEU   B 1 10  ? 38.149 -33.251 -17.585 1.00 18.96 ?  10   LEU   B CG   1 
ATOM   4006 C  CD1  . LEU   B 1 10  ? 38.236 -33.760 -19.017 1.00 20.19 ?  10   LEU   B CD1  1 
ATOM   4007 C  CD2  . LEU   B 1 10  ? 38.133 -34.400 -16.592 1.00 20.23 ?  10   LEU   B CD2  1 
ATOM   4008 H  H    . LEU   B 1 10  ? 40.728 -30.327 -16.886 1.00 19.43 ?  10   LEU   B H    1 
ATOM   4009 H  HA   . LEU   B 1 10  ? 39.065 -31.032 -18.891 1.00 19.55 ?  10   LEU   B HA   1 
ATOM   4010 H  HB2  . LEU   B 1 10  ? 40.115 -32.719 -17.579 1.00 20.58 ?  10   LEU   B HB2  1 
ATOM   4011 H  HB3  . LEU   B 1 10  ? 39.326 -32.178 -16.315 1.00 20.58 ?  10   LEU   B HB3  1 
ATOM   4012 H  HG   . LEU   B 1 10  ? 37.310 -32.776 -17.491 1.00 22.77 ?  10   LEU   B HG   1 
ATOM   4013 H  HD11 . LEU   B 1 10  ? 37.519 -34.397 -19.168 1.00 24.26 ?  10   LEU   B HD11 1 
ATOM   4014 H  HD12 . LEU   B 1 10  ? 38.142 -33.008 -19.622 1.00 24.26 ?  10   LEU   B HD12 1 
ATOM   4015 H  HD13 . LEU   B 1 10  ? 39.094 -34.188 -19.149 1.00 24.26 ?  10   LEU   B HD13 1 
ATOM   4016 H  HD21 . LEU   B 1 10  ? 37.401 -34.993 -16.814 1.00 24.30 ?  10   LEU   B HD21 1 
ATOM   4017 H  HD22 . LEU   B 1 10  ? 38.976 -34.870 -16.645 1.00 24.30 ?  10   LEU   B HD22 1 
ATOM   4018 H  HD23 . LEU   B 1 10  ? 38.008 -34.036 -15.700 1.00 24.30 ?  10   LEU   B HD23 1 
ATOM   4019 N  N    . LYS   B 1 11  ? 36.975 -29.960 -18.184 1.00 16.85 ?  11   LYS   B N    1 
ATOM   4020 C  CA   . LYS   B 1 11  ? 35.780 -29.249 -17.758 1.00 18.64 ?  11   LYS   B CA   1 
ATOM   4021 C  C    . LYS   B 1 11  ? 34.902 -30.178 -16.927 1.00 17.84 ?  11   LYS   B C    1 
ATOM   4022 O  O    . LYS   B 1 11  ? 34.513 -31.255 -17.392 1.00 19.50 ?  11   LYS   B O    1 
ATOM   4023 C  CB   . LYS   B 1 11  ? 35.026 -28.766 -18.995 1.00 22.32 ?  11   LYS   B CB   1 
ATOM   4024 C  CG   . LYS   B 1 11  ? 33.900 -27.787 -18.728 1.00 25.69 ?  11   LYS   B CG   1 
ATOM   4025 C  CD   . LYS   B 1 11  ? 33.178 -27.451 -20.027 1.00 28.54 ?  11   LYS   B CD   1 
ATOM   4026 C  CE   . LYS   B 1 11  ? 32.143 -26.358 -19.836 1.00 30.71 ?  11   LYS   B CE   1 
ATOM   4027 N  NZ   . LYS   B 1 11  ? 32.776 -25.052 -19.517 1.00 31.93 ?  11   LYS   B NZ   1 
ATOM   4028 H  H    . LYS   B 1 11  ? 36.944 -30.246 -18.996 1.00 20.25 ?  11   LYS   B H    1 
ATOM   4029 H  HA   . LYS   B 1 11  ? 36.027 -28.484 -17.219 1.00 22.39 ?  11   LYS   B HA   1 
ATOM   4030 H  HB2  . LYS   B 1 11  ? 35.657 -28.328 -19.587 1.00 26.81 ?  11   LYS   B HB2  1 
ATOM   4031 H  HB3  . LYS   B 1 11  ? 34.642 -29.536 -19.443 1.00 26.81 ?  11   LYS   B HB3  1 
ATOM   4032 H  HG2  . LYS   B 1 11  ? 33.261 -28.185 -18.116 1.00 30.86 ?  11   LYS   B HG2  1 
ATOM   4033 H  HG3  . LYS   B 1 11  ? 34.262 -26.968 -18.356 1.00 30.86 ?  11   LYS   B HG3  1 
ATOM   4034 H  HD2  . LYS   B 1 11  ? 33.827 -27.144 -20.680 1.00 34.28 ?  11   LYS   B HD2  1 
ATOM   4035 H  HD3  . LYS   B 1 11  ? 32.726 -28.245 -20.354 1.00 34.28 ?  11   LYS   B HD3  1 
ATOM   4036 H  HE2  . LYS   B 1 11  ? 31.631 -26.259 -20.654 1.00 36.88 ?  11   LYS   B HE2  1 
ATOM   4037 H  HE3  . LYS   B 1 11  ? 31.558 -26.603 -19.102 1.00 36.88 ?  11   LYS   B HE3  1 
ATOM   4038 H  HZ1  . LYS   B 1 11  ? 32.153 -24.419 -19.460 1.00 38.35 ?  11   LYS   B HZ1  1 
ATOM   4039 H  HZ2  . LYS   B 1 11  ? 33.209 -25.104 -18.742 1.00 38.35 ?  11   LYS   B HZ2  1 
ATOM   4040 H  HZ3  . LYS   B 1 11  ? 33.354 -24.831 -20.158 1.00 38.35 ?  11   LYS   B HZ3  1 
ATOM   4041 N  N    . LEU   B 1 12  ? 34.580 -29.762 -15.703 1.00 16.43 ?  12   LEU   B N    1 
ATOM   4042 C  CA   . LEU   B 1 12  ? 33.613 -30.466 -14.868 1.00 16.30 ?  12   LEU   B CA   1 
ATOM   4043 C  C    . LEU   B 1 12  ? 32.224 -29.855 -14.962 1.00 16.23 ?  12   LEU   B C    1 
ATOM   4044 O  O    . LEU   B 1 12  ? 31.237 -30.571 -15.132 1.00 16.66 ?  12   LEU   B O    1 
ATOM   4045 C  CB   . LEU   B 1 12  ? 34.072 -30.485 -13.407 1.00 15.65 ?  12   LEU   B CB   1 
ATOM   4046 C  CG   . LEU   B 1 12  ? 35.416 -31.155 -13.139 1.00 15.72 ?  12   LEU   B CG   1 
ATOM   4047 C  CD1  . LEU   B 1 12  ? 35.737 -31.105 -11.658 1.00 15.94 ?  12   LEU   B CD1  1 
ATOM   4048 C  CD2  . LEU   B 1 12  ? 35.427 -32.590 -13.658 1.00 16.59 ?  12   LEU   B CD2  1 
ATOM   4049 H  H    . LEU   B 1 12  ? 34.915 -29.064 -15.332 1.00 19.75 ?  12   LEU   B H    1 
ATOM   4050 H  HA   . LEU   B 1 12  ? 33.543 -31.380 -15.175 1.00 19.59 ?  12   LEU   B HA   1 
ATOM   4051 H  HB2  . LEU   B 1 12  ? 34.133 -29.571 -13.094 1.00 18.80 ?  12   LEU   B HB2  1 
ATOM   4052 H  HB3  . LEU   B 1 12  ? 33.402 -30.960 -12.888 1.00 18.80 ?  12   LEU   B HB3  1 
ATOM   4053 H  HG   . LEU   B 1 12  ? 36.108 -30.663 -13.611 1.00 18.89 ?  12   LEU   B HG   1 
ATOM   4054 H  HD11 . LEU   B 1 12  ? 36.596 -31.533 -11.508 1.00 19.15 ?  12   LEU   B HD11 1 
ATOM   4055 H  HD12 . LEU   B 1 12  ? 35.775 -30.179 -11.373 1.00 19.15 ?  12   LEU   B HD12 1 
ATOM   4056 H  HD13 . LEU   B 1 12  ? 35.044 -31.575 -11.169 1.00 19.15 ?  12   LEU   B HD13 1 
ATOM   4057 H  HD21 . LEU   B 1 12  ? 36.234 -33.030 -13.348 1.00 19.93 ?  12   LEU   B HD21 1 
ATOM   4058 H  HD22 . LEU   B 1 12  ? 34.646 -33.053 -13.321 1.00 19.93 ?  12   LEU   B HD22 1 
ATOM   4059 H  HD23 . LEU   B 1 12  ? 35.411 -32.576 -14.629 1.00 19.93 ?  12   LEU   B HD23 1 
ATOM   4060 N  N    . THR   B 1 13  ? 32.136 -28.535 -14.850 1.00 16.10 ?  13   THR   B N    1 
ATOM   4061 C  CA   . THR   B 1 13  ? 30.907 -27.785 -15.041 1.00 16.06 ?  13   THR   B CA   1 
ATOM   4062 C  C    . THR   B 1 13  ? 31.232 -26.579 -15.915 1.00 18.03 ?  13   THR   B C    1 
ATOM   4063 O  O    . THR   B 1 13  ? 32.375 -26.380 -16.344 1.00 18.58 ?  13   THR   B O    1 
ATOM   4064 C  CB   . THR   B 1 13  ? 30.323 -27.320 -13.702 1.00 15.85 ?  13   THR   B CB   1 
ATOM   4065 O  OG1  . THR   B 1 13  ? 31.174 -26.303 -13.159 1.00 15.42 ?  13   THR   B OG1  1 
ATOM   4066 C  CG2  . THR   B 1 13  ? 30.215 -28.479 -12.713 1.00 16.44 ?  13   THR   B CG2  1 
ATOM   4067 H  H    . THR   B 1 13  ? 32.805 -28.029 -14.654 1.00 19.34 ?  13   THR   B H    1 
ATOM   4068 H  HA   . THR   B 1 13  ? 30.248 -28.338 -15.491 1.00 19.30 ?  13   THR   B HA   1 
ATOM   4069 H  HB   . THR   B 1 13  ? 29.429 -26.956 -13.845 1.00 19.05 ?  13   THR   B HB   1 
ATOM   4070 H  HG1  . THR   B 1 13  ? 30.847 -25.542 -13.322 1.00 18.53 ?  13   THR   B HG1  1 
ATOM   4071 H  HG21 . THR   B 1 13  ? 29.710 -28.205 -11.930 1.00 19.76 ?  13   THR   B HG21 1 
ATOM   4072 H  HG22 . THR   B 1 13  ? 29.766 -29.232 -13.128 1.00 19.76 ?  13   THR   B HG22 1 
ATOM   4073 H  HG23 . THR   B 1 13  ? 31.101 -28.758 -12.432 1.00 19.76 ?  13   THR   B HG23 1 
ATOM   4074 N  N    A ASP   B 1 14  ? 30.214 -25.758 -16.173 0.60 19.23 ?  14   ASP   B N    1 
ATOM   4075 N  N    B ASP   B 1 14  ? 30.219 -25.746 -16.162 0.40 19.02 ?  14   ASP   B N    1 
ATOM   4076 C  CA   A ASP   B 1 14  ? 30.422 -24.586 -17.016 0.60 20.57 ?  14   ASP   B CA   1 
ATOM   4077 C  CA   B ASP   B 1 14  ? 30.414 -24.582 -17.019 0.40 20.00 ?  14   ASP   B CA   1 
ATOM   4078 C  C    A ASP   B 1 14  ? 31.527 -23.682 -16.479 0.60 18.73 ?  14   ASP   B C    1 
ATOM   4079 C  C    B ASP   B 1 14  ? 31.401 -23.576 -16.447 0.40 18.34 ?  14   ASP   B C    1 
ATOM   4080 O  O    A ASP   B 1 14  ? 32.196 -22.997 -17.263 0.60 19.51 ?  14   ASP   B O    1 
ATOM   4081 O  O    B ASP   B 1 14  ? 31.818 -22.669 -17.177 0.40 18.78 ?  14   ASP   B O    1 
ATOM   4082 C  CB   A ASP   B 1 14  ? 29.113 -23.812 -17.174 0.60 23.87 ?  14   ASP   B CB   1 
ATOM   4083 C  CB   B ASP   B 1 14  ? 29.086 -23.872 -17.273 0.40 22.67 ?  14   ASP   B CB   1 
ATOM   4084 C  CG   A ASP   B 1 14  ? 28.142 -24.491 -18.110 0.60 27.03 ?  14   ASP   B CG   1 
ATOM   4085 C  CG   B ASP   B 1 14  ? 28.212 -24.616 -18.260 0.40 25.08 ?  14   ASP   B CG   1 
ATOM   4086 O  OD1  A ASP   B 1 14  ? 28.505 -25.518 -18.727 0.60 28.17 ?  14   ASP   B OD1  1 
ATOM   4087 O  OD1  B ASP   B 1 14  ? 28.769 -25.261 -19.174 0.40 25.84 ?  14   ASP   B OD1  1 
ATOM   4088 O  OD2  A ASP   B 1 14  ? 27.005 -23.991 -18.227 0.60 28.07 -1 14   ASP   B OD2  1 
ATOM   4089 O  OD2  B ASP   B 1 14  ? 26.973 -24.561 -18.124 0.40 25.91 -1 14   ASP   B OD2  1 
ATOM   4090 H  H    A ASP   B 1 14  ? 29.411 -25.852 -15.876 0.60 23.10 ?  14   ASP   B H    1 
ATOM   4091 H  H    B ASP   B 1 14  ? 29.422 -25.825 -15.843 0.40 22.85 ?  14   ASP   B H    1 
ATOM   4092 H  HA   A ASP   B 1 14  ? 30.699 -24.874 -17.894 0.60 24.71 ?  14   ASP   B HA   1 
ATOM   4093 H  HA   B ASP   B 1 14  ? 30.753 -24.886 -17.875 0.40 24.03 ?  14   ASP   B HA   1 
ATOM   4094 H  HB2  A ASP   B 1 14  ? 28.670 -23.736 -16.316 0.60 28.68 ?  14   ASP   B HB2  1 
ATOM   4095 H  HB2  B ASP   B 1 14  ? 28.605 -23.792 -16.434 0.40 27.23 ?  14   ASP   B HB2  1 
ATOM   4096 H  HB3  A ASP   B 1 14  ? 29.294 -22.934 -17.538 0.60 28.68 ?  14   ASP   B HB3  1 
ATOM   4097 H  HB3  B ASP   B 1 14  ? 29.267 -22.986 -17.634 0.40 27.23 ?  14   ASP   B HB3  1 
ATOM   4098 N  N    . ASN   B 1 15  ? 31.758 -23.685 -15.164 1.00 16.42 ?  15   ASN   B N    1 
ATOM   4099 C  CA   . ASN   B 1 15  ? 32.712 -22.762 -14.558 1.00 14.34 ?  15   ASN   B CA   1 
ATOM   4100 C  C    . ASN   B 1 15  ? 33.805 -23.418 -13.724 1.00 13.27 ?  15   ASN   B C    1 
ATOM   4101 O  O    . ASN   B 1 15  ? 34.649 -22.691 -13.191 1.00 13.53 ?  15   ASN   B O    1 
ATOM   4102 C  CB   . ASN   B 1 15  ? 31.990 -21.712 -13.694 1.00 14.49 ?  15   ASN   B CB   1 
ATOM   4103 C  CG   . ASN   B 1 15  ? 31.376 -22.316 -12.452 1.00 14.24 ?  15   ASN   B CG   1 
ATOM   4104 O  OD1  . ASN   B 1 15  ? 30.434 -23.112 -12.535 1.00 15.64 ?  15   ASN   B OD1  1 
ATOM   4105 N  ND2  . ASN   B 1 15  ? 31.905 -21.966 -11.293 1.00 13.68 ?  15   ASN   B ND2  1 
ATOM   4106 H  H    A ASN   B 1 15  ? 31.388 -24.228 -14.604 0.60 19.73 ?  15   ASN   B H    1 
ATOM   4107 H  H    B ASN   B 1 15  ? 31.428 -24.263 -14.616 0.40 19.73 ?  15   ASN   B H    1 
ATOM   4108 H  HA   . ASN   B 1 15  ? 33.155 -22.277 -15.263 1.00 17.24 ?  15   ASN   B HA   1 
ATOM   4109 H  HB2  . ASN   B 1 15  ? 32.631 -21.032 -13.416 1.00 17.42 ?  15   ASN   B HB2  1 
ATOM   4110 H  HB3  . ASN   B 1 15  ? 31.280 -21.296 -14.213 1.00 17.42 ?  15   ASN   B HB3  1 
ATOM   4111 H  HD21 . ASN   B 1 15  ? 31.587 -22.280 -10.557 1.00 16.44 ?  15   ASN   B HD21 1 
ATOM   4112 H  HD22 . ASN   B 1 15  ? 32.565 -21.408 -11.266 1.00 16.44 ?  15   ASN   B HD22 1 
ATOM   4113 N  N    . VAL   B 1 16  ? 33.822 -24.744 -13.586 1.00 13.09 ?  16   VAL   B N    1 
ATOM   4114 C  CA   . VAL   B 1 16  ? 34.824 -25.438 -12.782 1.00 12.57 ?  16   VAL   B CA   1 
ATOM   4115 C  C    . VAL   B 1 16  ? 35.619 -26.372 -13.678 1.00 12.38 ?  16   VAL   B C    1 
ATOM   4116 O  O    . VAL   B 1 16  ? 35.045 -27.247 -14.342 1.00 13.62 ?  16   VAL   B O    1 
ATOM   4117 C  CB   . VAL   B 1 16  ? 34.201 -26.209 -11.605 1.00 13.00 ?  16   VAL   B CB   1 
ATOM   4118 C  CG1  . VAL   B 1 16  ? 35.284 -26.947 -10.817 1.00 13.23 ?  16   VAL   B CG1  1 
ATOM   4119 C  CG2  . VAL   B 1 16  ? 33.413 -25.265 -10.706 1.00 13.60 ?  16   VAL   B CG2  1 
ATOM   4120 H  H    . VAL   B 1 16  ? 33.250 -25.270 -13.954 1.00 15.73 ?  16   VAL   B H    1 
ATOM   4121 H  HA   . VAL   B 1 16  ? 35.438 -24.783 -12.412 1.00 15.11 ?  16   VAL   B HA   1 
ATOM   4122 H  HB   . VAL   B 1 16  ? 33.584 -26.871 -11.954 1.00 15.63 ?  16   VAL   B HB   1 
ATOM   4123 H  HG11 . VAL   B 1 16  ? 34.908 -27.246 -9.974  1.00 15.91 ?  16   VAL   B HG11 1 
ATOM   4124 H  HG12 . VAL   B 1 16  ? 35.590 -27.707 -11.331 1.00 15.91 ?  16   VAL   B HG12 1 
ATOM   4125 H  HG13 . VAL   B 1 16  ? 36.020 -26.337 -10.650 1.00 15.91 ?  16   VAL   B HG13 1 
ATOM   4126 H  HG21 . VAL   B 1 16  ? 33.072 -25.763 -9.946  1.00 16.34 ?  16   VAL   B HG21 1 
ATOM   4127 H  HG22 . VAL   B 1 16  ? 33.999 -24.556 -10.401 1.00 16.34 ?  16   VAL   B HG22 1 
ATOM   4128 H  HG23 . VAL   B 1 16  ? 32.675 -24.890 -11.212 1.00 16.34 ?  16   VAL   B HG23 1 
ATOM   4129 N  N    . TYR   B 1 17  ? 36.942 -26.204 -13.651 1.00 12.87 ?  17   TYR   B N    1 
ATOM   4130 C  CA   . TYR   B 1 17  ? 37.892 -26.947 -14.463 1.00 13.32 ?  17   TYR   B CA   1 
ATOM   4131 C  C    . TYR   B 1 17  ? 38.943 -27.561 -13.550 1.00 12.63 ?  17   TYR   B C    1 
ATOM   4132 O  O    . TYR   B 1 17  ? 39.229 -27.032 -12.472 1.00 13.06 ?  17   TYR   B O    1 
ATOM   4133 C  CB   . TYR   B 1 17  ? 38.601 -26.012 -15.449 1.00 15.59 ?  17   TYR   B CB   1 
ATOM   4134 C  CG   . TYR   B 1 17  ? 37.676 -25.244 -16.358 1.00 18.46 ?  17   TYR   B CG   1 
ATOM   4135 C  CD1  . TYR   B 1 17  ? 37.078 -24.059 -15.942 1.00 19.66 ?  17   TYR   B CD1  1 
ATOM   4136 C  CD2  . TYR   B 1 17  ? 37.402 -25.703 -17.638 1.00 20.22 ?  17   TYR   B CD2  1 
ATOM   4137 C  CE1  . TYR   B 1 17  ? 36.229 -23.356 -16.776 1.00 21.06 ?  17   TYR   B CE1  1 
ATOM   4138 C  CE2  . TYR   B 1 17  ? 36.559 -25.006 -18.481 1.00 21.71 ?  17   TYR   B CE2  1 
ATOM   4139 C  CZ   . TYR   B 1 17  ? 35.973 -23.837 -18.043 1.00 22.16 ?  17   TYR   B CZ   1 
ATOM   4140 O  OH   . TYR   B 1 17  ? 35.134 -23.142 -18.880 1.00 23.57 ?  17   TYR   B OH   1 
ATOM   4141 H  H    . TYR   B 1 17  ? 37.334 -25.627 -13.138 1.00 15.47 ?  17   TYR   B H    1 
ATOM   4142 H  HA   . TYR   B 1 17  ? 37.434 -27.653 -14.953 1.00 16.01 ?  17   TYR   B HA   1 
ATOM   4143 H  HB2  . TYR   B 1 17  ? 39.129 -25.373 -14.951 1.00 18.73 ?  17   TYR   B HB2  1 
ATOM   4144 H  HB3  . TYR   B 1 17  ? 39.174 -26.546 -16.014 1.00 18.73 ?  17   TYR   B HB3  1 
ATOM   4145 H  HD1  . TYR   B 1 17  ? 37.251 -23.737 -15.089 1.00 23.62 ?  17   TYR   B HD1  1 
ATOM   4146 H  HD2  . TYR   B 1 17  ? 37.788 -26.492 -17.936 1.00 24.29 ?  17   TYR   B HD2  1 
ATOM   4147 H  HE1  . TYR   B 1 17  ? 35.835 -22.562 -16.487 1.00 25.30 ?  17   TYR   B HE1  1 
ATOM   4148 H  HE2  . TYR   B 1 17  ? 36.376 -25.327 -19.338 1.00 26.08 ?  17   TYR   B HE2  1 
ATOM   4149 H  HH   . TYR   B 1 17  ? 35.057 -23.535 -19.620 1.00 28.31 ?  17   TYR   B HH   1 
ATOM   4150 N  N    . ILE   B 1 18  ? 39.553 -28.663 -13.990 1.00 12.40 ?  18   ILE   B N    1 
ATOM   4151 C  CA   . ILE   B 1 18  ? 40.488 -29.388 -13.136 1.00 12.46 ?  18   ILE   B CA   1 
ATOM   4152 C  C    . ILE   B 1 18  ? 41.649 -29.931 -13.962 1.00 13.03 ?  18   ILE   B C    1 
ATOM   4153 O  O    . ILE   B 1 18  ? 41.485 -30.325 -15.121 1.00 14.07 ?  18   ILE   B O    1 
ATOM   4154 C  CB   . ILE   B 1 18  ? 39.742 -30.495 -12.339 1.00 13.02 ?  18   ILE   B CB   1 
ATOM   4155 C  CG1  . ILE   B 1 18  ? 40.600 -31.049 -11.202 1.00 13.35 ?  18   ILE   B CG1  1 
ATOM   4156 C  CG2  . ILE   B 1 18  ? 39.244 -31.608 -13.265 1.00 13.68 ?  18   ILE   B CG2  1 
ATOM   4157 C  CD1  . ILE   B 1 18  ? 39.784 -31.833 -10.171 1.00 14.97 ?  18   ILE   B CD1  1 
ATOM   4158 H  H    . ILE   B 1 18  ? 39.446 -29.007 -14.772 1.00 14.91 ?  18   ILE   B H    1 
ATOM   4159 H  HA   . ILE   B 1 18  ? 40.853 -28.772 -12.485 1.00 14.98 ?  18   ILE   B HA   1 
ATOM   4160 H  HB   . ILE   B 1 18  ? 38.958 -30.090 -11.934 1.00 15.65 ?  18   ILE   B HB   1 
ATOM   4161 H  HG12 . ILE   B 1 18  ? 41.267 -31.645 -11.568 1.00 16.04 ?  18   ILE   B HG12 1 
ATOM   4162 H  HG13 . ILE   B 1 18  ? 41.027 -30.310 -10.740 1.00 16.04 ?  18   ILE   B HG13 1 
ATOM   4163 H  HG21 . ILE   B 1 18  ? 38.660 -32.200 -12.762 1.00 16.44 ?  18   ILE   B HG21 1 
ATOM   4164 H  HG22 . ILE   B 1 18  ? 38.757 -31.210 -14.000 1.00 16.44 ?  18   ILE   B HG22 1 
ATOM   4165 H  HG23 . ILE   B 1 18  ? 40.006 -32.105 -13.599 1.00 16.44 ?  18   ILE   B HG23 1 
ATOM   4166 H  HD11 . ILE   B 1 18  ? 40.369 -32.120 -9.454  1.00 17.99 ?  18   ILE   B HD11 1 
ATOM   4167 H  HD12 . ILE   B 1 18  ? 39.084 -31.259 -9.818  1.00 17.99 ?  18   ILE   B HD12 1 
ATOM   4168 H  HD13 . ILE   B 1 18  ? 39.386 -32.606 -10.604 1.00 17.99 ?  18   ILE   B HD13 1 
ATOM   4169 N  N    . LYS   B 1 19  ? 42.831 -29.966 -13.344 1.00 13.41 ?  19   LYS   B N    1 
ATOM   4170 C  CA   . LYS   B 1 19  ? 44.040 -30.441 -14.002 1.00 14.25 ?  19   LYS   B CA   1 
ATOM   4171 C  C    . LYS   B 1 19  ? 44.940 -31.117 -12.980 1.00 13.95 ?  19   LYS   B C    1 
ATOM   4172 O  O    . LYS   B 1 19  ? 45.027 -30.681 -11.829 1.00 13.58 ?  19   LYS   B O    1 
ATOM   4173 C  CB   . LYS   B 1 19  ? 44.807 -29.275 -14.639 1.00 15.55 ?  19   LYS   B CB   1 
ATOM   4174 C  CG   . LYS   B 1 19  ? 46.009 -29.674 -15.475 1.00 17.61 ?  19   LYS   B CG   1 
ATOM   4175 C  CD   . LYS   B 1 19  ? 46.725 -28.434 -15.997 1.00 19.15 ?  19   LYS   B CD   1 
ATOM   4176 C  CE   . LYS   B 1 19  ? 47.895 -28.799 -16.887 1.00 21.03 ?  19   LYS   B CE   1 
ATOM   4177 N  NZ   . LYS   B 1 19  ? 48.632 -27.603 -17.369 1.00 22.31 ?  19   LYS   B NZ   1 
ATOM   4178 H  H    . LYS   B 1 19  ? 42.950 -29.714 -12.528 1.00 16.12 ?  19   LYS   B H    1 
ATOM   4179 H  HA   . LYS   B 1 19  ? 43.804 -31.081 -14.692 1.00 17.12 ?  19   LYS   B HA   1 
ATOM   4180 H  HB2  . LYS   B 1 19  ? 44.198 -28.788 -15.214 1.00 18.68 ?  19   LYS   B HB2  1 
ATOM   4181 H  HB3  . LYS   B 1 19  ? 45.119 -28.690 -13.927 1.00 18.68 ?  19   LYS   B HB3  1 
ATOM   4182 H  HG2  . LYS   B 1 19  ? 46.626 -30.183 -14.929 1.00 21.16 ?  19   LYS   B HG2  1 
ATOM   4183 H  HG3  . LYS   B 1 19  ? 45.708 -30.201 -16.232 1.00 21.16 ?  19   LYS   B HG3  1 
ATOM   4184 H  HD2  . LYS   B 1 19  ? 46.100 -27.898 -16.512 1.00 23.01 ?  19   LYS   B HD2  1 
ATOM   4185 H  HD3  . LYS   B 1 19  ? 47.060 -27.921 -15.243 1.00 23.01 ?  19   LYS   B HD3  1 
ATOM   4186 H  HE2  . LYS   B 1 19  ? 48.510 -29.357 -16.387 1.00 25.26 ?  19   LYS   B HE2  1 
ATOM   4187 H  HE3  . LYS   B 1 19  ? 47.562 -29.283 -17.661 1.00 25.26 ?  19   LYS   B HE3  1 
ATOM   4188 H  HZ1  . LYS   B 1 19  ? 49.275 -27.850 -17.933 1.00 26.80 ?  19   LYS   B HZ1  1 
ATOM   4189 H  HZ2  . LYS   B 1 19  ? 48.076 -27.050 -17.788 1.00 26.80 ?  19   LYS   B HZ2  1 
ATOM   4190 H  HZ3  . LYS   B 1 19  ? 49.001 -27.176 -16.681 1.00 26.80 ?  19   LYS   B HZ3  1 
ATOM   4191 N  N    . ASN   B 1 20  ? 45.624 -32.172 -13.418 1.00 15.08 ?  20   ASN   B N    1 
ATOM   4192 C  CA   . ASN   B 1 20  ? 46.668 -32.798 -12.615 1.00 16.22 ?  20   ASN   B CA   1 
ATOM   4193 C  C    . ASN   B 1 20  ? 47.932 -31.968 -12.804 1.00 16.54 ?  20   ASN   B C    1 
ATOM   4194 O  O    . ASN   B 1 20  ? 48.562 -32.023 -13.867 1.00 18.12 ?  20   ASN   B O    1 
ATOM   4195 C  CB   . ASN   B 1 20  ? 46.859 -34.246 -13.067 1.00 17.76 ?  20   ASN   B CB   1 
ATOM   4196 C  CG   . ASN   B 1 20  ? 48.025 -34.947 -12.378 1.00 19.43 ?  20   ASN   B CG   1 
ATOM   4197 O  OD1  . ASN   B 1 20  ? 48.700 -35.784 -12.985 1.00 21.57 ?  20   ASN   B OD1  1 
ATOM   4198 N  ND2  . ASN   B 1 20  ? 48.262 -34.621 -11.117 1.00 19.06 ?  20   ASN   B ND2  1 
ATOM   4199 H  H    . ASN   B 1 20  ? 45.507 -32.536 -14.190 1.00 18.12 ?  20   ASN   B H    1 
ATOM   4200 H  HA   . ASN   B 1 20  ? 46.406 -32.785 -11.681 1.00 19.49 ?  20   ASN   B HA   1 
ATOM   4201 H  HB2  . ASN   B 1 20  ? 46.051 -34.743 -12.864 1.00 21.33 ?  20   ASN   B HB2  1 
ATOM   4202 H  HB3  . ASN   B 1 20  ? 47.022 -34.251 -14.021 1.00 21.33 ?  20   ASN   B HB3  1 
ATOM   4203 H  HD21 . ASN   B 1 20  ? 48.916 -34.986 -10.699 1.00 22.90 ?  20   ASN   B HD21 1 
ATOM   4204 H  HD22 . ASN   B 1 20  ? 47.772 -34.034 -10.716 1.00 22.90 ?  20   ASN   B HD22 1 
ATOM   4205 N  N    . ALA   B 1 21  ? 48.290 -31.175 -11.793 1.00 16.03 ?  21   ALA   B N    1 
ATOM   4206 C  CA   . ALA   B 1 21  ? 49.387 -30.229 -11.939 1.00 16.73 ?  21   ALA   B CA   1 
ATOM   4207 C  C    . ALA   B 1 21  ? 49.854 -29.754 -10.571 1.00 15.59 ?  21   ALA   B C    1 
ATOM   4208 O  O    . ALA   B 1 21  ? 49.111 -29.792 -9.585  1.00 15.34 ?  21   ALA   B O    1 
ATOM   4209 C  CB   . ALA   B 1 21  ? 48.970 -29.039 -12.804 1.00 17.88 ?  21   ALA   B CB   1 
ATOM   4210 H  H    . ALA   B 1 21  ? 47.913 -31.172 -11.016 1.00 19.26 ?  21   ALA   B H    1 
ATOM   4211 H  HA   . ALA   B 1 21  ? 50.128 -30.676 -12.372 1.00 20.11 ?  21   ALA   B HA   1 
ATOM   4212 H  HB1  . ALA   B 1 21  ? 49.746 -28.488 -12.961 1.00 21.48 ?  21   ALA   B HB1  1 
ATOM   4213 H  HB2  . ALA   B 1 21  ? 48.621 -29.373 -13.645 1.00 21.48 ?  21   ALA   B HB2  1 
ATOM   4214 H  HB3  . ALA   B 1 21  ? 48.282 -28.536 -12.339 1.00 21.48 ?  21   ALA   B HB3  1 
ATOM   4215 N  N    . ASP   B 1 22  ? 51.112 -29.313 -10.544 1.00 15.02 ?  22   ASP   B N    1 
ATOM   4216 C  CA   . ASP   B 1 22  ? 51.726 -28.626 -9.412  1.00 14.39 ?  22   ASP   B CA   1 
ATOM   4217 C  C    . ASP   B 1 22  ? 51.325 -27.155 -9.487  1.00 12.98 ?  22   ASP   B C    1 
ATOM   4218 O  O    . ASP   B 1 22  ? 51.645 -26.476 -10.467 1.00 13.21 ?  22   ASP   B O    1 
ATOM   4219 C  CB   . ASP   B 1 22  ? 53.244 -28.803 -9.565  1.00 16.07 ?  22   ASP   B CB   1 
ATOM   4220 C  CG   . ASP   B 1 22  ? 54.073 -28.044 -8.533  1.00 17.41 ?  22   ASP   B CG   1 
ATOM   4221 O  OD1  . ASP   B 1 22  ? 53.707 -26.929 -8.127  1.00 17.56 ?  22   ASP   B OD1  1 
ATOM   4222 O  OD2  . ASP   B 1 22  ? 55.150 -28.562 -8.156  1.00 19.90 -1 22   ASP   B OD2  1 
ATOM   4223 H  H    . ASP   B 1 22  ? 51.656 -29.411 -11.207 1.00 18.05 ?  22   ASP   B H    1 
ATOM   4224 H  HA   . ASP   B 1 22  ? 51.433 -29.017 -8.570  1.00 17.30 ?  22   ASP   B HA   1 
ATOM   4225 H  HB2  . ASP   B 1 22  ? 53.465 -29.740 -9.482  1.00 19.31 ?  22   ASP   B HB2  1 
ATOM   4226 H  HB3  . ASP   B 1 22  ? 53.507 -28.475 -10.439 1.00 19.31 ?  22   ASP   B HB3  1 
ATOM   4227 N  N    . ILE   B 1 23  ? 50.618 -26.667 -8.461  1.00 12.45 ?  23   ILE   B N    1 
ATOM   4228 C  CA   . ILE   B 1 23  ? 50.025 -25.329 -8.525  1.00 11.62 ?  23   ILE   B CA   1 
ATOM   4229 C  C    . ILE   B 1 23  ? 51.078 -24.237 -8.659  1.00 11.40 ?  23   ILE   B C    1 
ATOM   4230 O  O    . ILE   B 1 23  ? 50.809 -23.190 -9.256  1.00 11.25 ?  23   ILE   B O    1 
ATOM   4231 C  CB   . ILE   B 1 23  ? 49.082 -25.094 -7.330  1.00 12.30 ?  23   ILE   B CB   1 
ATOM   4232 C  CG1  . ILE   B 1 23  ? 48.243 -23.832 -7.538  1.00 13.25 ?  23   ILE   B CG1  1 
ATOM   4233 C  CG2  . ILE   B 1 23  ? 49.845 -25.036 -6.025  1.00 13.23 ?  23   ILE   B CG2  1 
ATOM   4234 C  CD1  . ILE   B 1 23  ? 47.124 -23.666 -6.520  1.00 13.86 ?  23   ILE   B CD1  1 
ATOM   4235 H  H    . ILE   B 1 23  ? 50.480 -27.090 -7.723  1.00 14.97 ?  23   ILE   B H    1 
ATOM   4236 H  HA   . ILE   B 1 23  ? 49.483 -25.292 -9.324  1.00 13.97 ?  23   ILE   B HA   1 
ATOM   4237 H  HB   . ILE   B 1 23  ? 48.472 -25.849 -7.286  1.00 14.79 ?  23   ILE   B HB   1 
ATOM   4238 H  HG12 . ILE   B 1 23  ? 48.824 -23.055 -7.471  1.00 15.93 ?  23   ILE   B HG12 1 
ATOM   4239 H  HG13 . ILE   B 1 23  ? 47.843 -23.862 -8.424  1.00 15.93 ?  23   ILE   B HG13 1 
ATOM   4240 H  HG21 . ILE   B 1 23  ? 49.212 -25.051 -5.290  1.00 15.90 ?  23   ILE   B HG21 1 
ATOM   4241 H  HG22 . ILE   B 1 23  ? 50.434 -25.804 -5.969  1.00 15.90 ?  23   ILE   B HG22 1 
ATOM   4242 H  HG23 . ILE   B 1 23  ? 50.363 -24.217 -5.999  1.00 15.90 ?  23   ILE   B HG23 1 
ATOM   4243 H  HD11 . ILE   B 1 23  ? 46.587 -22.898 -6.765  1.00 16.66 ?  23   ILE   B HD11 1 
ATOM   4244 H  HD12 . ILE   B 1 23  ? 46.576 -24.469 -6.529  1.00 16.66 ?  23   ILE   B HD12 1 
ATOM   4245 H  HD13 . ILE   B 1 23  ? 47.512 -23.540 -5.643  1.00 16.66 ?  23   ILE   B HD13 1 
ATOM   4246 N  N    . VAL   B 1 24  ? 52.273 -24.441 -8.102  1.00 11.81 ?  24   VAL   B N    1 
ATOM   4247 C  CA   . VAL   B 1 24  ? 53.345 -23.457 -8.266  1.00 12.32 ?  24   VAL   B CA   1 
ATOM   4248 C  C    . VAL   B 1 24  ? 53.794 -23.403 -9.720  1.00 12.37 ?  24   VAL   B C    1 
ATOM   4249 O  O    . VAL   B 1 24  ? 53.931 -22.326 -10.313 1.00 13.00 ?  24   VAL   B O    1 
ATOM   4250 C  CB   . VAL   B 1 24  ? 54.526 -23.776 -7.329  1.00 13.28 ?  24   VAL   B CB   1 
ATOM   4251 C  CG1  . VAL   B 1 24  ? 55.741 -22.913 -7.682  1.00 14.27 ?  24   VAL   B CG1  1 
ATOM   4252 C  CG2  . VAL   B 1 24  ? 54.129 -23.576 -5.885  1.00 14.53 ?  24   VAL   B CG2  1 
ATOM   4253 H  H    . VAL   B 1 24  ? 52.484 -25.124 -7.626  1.00 14.20 ?  24   VAL   B H    1 
ATOM   4254 H  HA   . VAL   B 1 24  ? 53.009 -22.580 -8.025  1.00 14.81 ?  24   VAL   B HA   1 
ATOM   4255 H  HB   . VAL   B 1 24  ? 54.779 -24.706 -7.439  1.00 15.97 ?  24   VAL   B HB   1 
ATOM   4256 H  HG11 . VAL   B 1 24  ? 56.335 -22.878 -6.915  1.00 17.16 ?  24   VAL   B HG11 1 
ATOM   4257 H  HG12 . VAL   B 1 24  ? 56.201 -23.313 -8.436  1.00 17.16 ?  24   VAL   B HG12 1 
ATOM   4258 H  HG13 . VAL   B 1 24  ? 55.440 -22.020 -7.906  1.00 17.16 ?  24   VAL   B HG13 1 
ATOM   4259 H  HG21 . VAL   B 1 24  ? 54.856 -23.864 -5.312  1.00 17.46 ?  24   VAL   B HG21 1 
ATOM   4260 H  HG22 . VAL   B 1 24  ? 53.946 -22.634 -5.737  1.00 17.46 ?  24   VAL   B HG22 1 
ATOM   4261 H  HG23 . VAL   B 1 24  ? 53.334 -24.100 -5.700  1.00 17.46 ?  24   VAL   B HG23 1 
ATOM   4262 N  N    . GLU   B 1 25  ? 54.062 -24.571 -10.309 1.00 13.30 ?  25   GLU   B N    1 
ATOM   4263 C  CA   . GLU   B 1 25  ? 54.454 -24.606 -11.712 1.00 14.54 ?  25   GLU   B CA   1 
ATOM   4264 C  C    . GLU   B 1 25  ? 53.349 -24.057 -12.601 1.00 13.69 ?  25   GLU   B C    1 
ATOM   4265 O  O    . GLU   B 1 25  ? 53.620 -23.345 -13.577 1.00 14.90 ?  25   GLU   B O    1 
ATOM   4266 C  CB   . GLU   B 1 25  ? 54.838 -26.030 -12.109 1.00 18.28 ?  25   GLU   B CB   1 
ATOM   4267 C  CG   . GLU   B 1 25  ? 56.120 -26.496 -11.445 1.00 23.60 ?  25   GLU   B CG   1 
ATOM   4268 C  CD   . GLU   B 1 25  ? 57.245 -25.476 -11.547 1.00 28.20 ?  25   GLU   B CD   1 
ATOM   4269 O  OE1  . GLU   B 1 25  ? 57.637 -25.125 -12.681 1.00 29.87 ?  25   GLU   B OE1  1 
ATOM   4270 O  OE2  . GLU   B 1 25  ? 57.727 -25.002 -10.490 1.00 29.95 -1 25   GLU   B OE2  1 
ATOM   4271 H  H    . GLU   B 1 25  ? 54.024 -25.340 -9.923  1.00 15.99 ?  25   GLU   B H    1 
ATOM   4272 H  HA   . GLU   B 1 25  ? 55.216 -24.028 -11.836 1.00 17.47 ?  25   GLU   B HA   1 
ATOM   4273 H  HB2  . GLU   B 1 25  ? 54.128 -26.638 -11.843 1.00 21.96 ?  25   GLU   B HB2  1 
ATOM   4274 H  HB3  . GLU   B 1 25  ? 54.963 -26.069 -13.070 1.00 21.96 ?  25   GLU   B HB3  1 
ATOM   4275 H  HG2  . GLU   B 1 25  ? 55.957 -26.641 -10.505 1.00 28.34 ?  25   GLU   B HG2  1 
ATOM   4276 H  HG3  . GLU   B 1 25  ? 56.415 -27.317 -11.870 1.00 28.34 ?  25   GLU   B HG3  1 
ATOM   4277 N  N    . GLU   B 1 26  ? 52.095 -24.368 -12.268 1.00 12.96 ?  26   GLU   B N    1 
ATOM   4278 C  CA   . GLU   B 1 26  ? 50.971 -23.842 -13.035 1.00 13.38 ?  26   GLU   B CA   1 
ATOM   4279 C  C    . GLU   B 1 26  ? 50.918 -22.324 -12.952 1.00 12.68 ?  26   GLU   B C    1 
ATOM   4280 O  O    . GLU   B 1 26  ? 50.719 -21.647 -13.965 1.00 14.10 ?  26   GLU   B O    1 
ATOM   4281 C  CB   . GLU   B 1 26  ? 49.654 -24.434 -12.525 1.00 15.09 ?  26   GLU   B CB   1 
ATOM   4282 C  CG   . GLU   B 1 26  ? 49.220 -25.712 -13.205 1.00 18.73 ?  26   GLU   B CG   1 
ATOM   4283 C  CD   . GLU   B 1 26  ? 48.959 -25.549 -14.698 1.00 20.61 ?  26   GLU   B CD   1 
ATOM   4284 O  OE1  . GLU   B 1 26  ? 47.983 -24.879 -15.102 1.00 20.88 ?  26   GLU   B OE1  1 
ATOM   4285 O  OE2  . GLU   B 1 26  ? 49.736 -26.122 -15.472 1.00 22.97 -1 26   GLU   B OE2  1 
ATOM   4286 H  H    . GLU   B 1 26  ? 51.865 -24.877 -11.607 1.00 15.58 ?  26   GLU   B H    1 
ATOM   4287 H  HA   . GLU   B 1 26  ? 51.077 -24.092 -13.964 1.00 16.09 ?  26   GLU   B HA   1 
ATOM   4288 H  HB2  . GLU   B 1 26  ? 49.741 -24.625 -11.578 1.00 18.14 ?  26   GLU   B HB2  1 
ATOM   4289 H  HB3  . GLU   B 1 26  ? 48.947 -23.779 -12.658 1.00 18.14 ?  26   GLU   B HB3  1 
ATOM   4290 H  HG2  . GLU   B 1 26  ? 49.924 -26.361 -13.104 1.00 22.51 ?  26   GLU   B HG2  1 
ATOM   4291 H  HG3  . GLU   B 1 26  ? 48.402 -26.027 -12.792 1.00 22.51 ?  26   GLU   B HG3  1 
ATOM   4292 N  N    . ALA   B 1 27  ? 51.058 -21.774 -11.744 1.00 12.09 ?  27   ALA   B N    1 
ATOM   4293 C  CA   . ALA   B 1 27  ? 51.018 -20.324 -11.592 1.00 12.63 ?  27   ALA   B CA   1 
ATOM   4294 C  C    . ALA   B 1 27  ? 52.094 -19.658 -12.435 1.00 13.59 ?  27   ALA   B C    1 
ATOM   4295 O  O    . ALA   B 1 27  ? 51.840 -18.646 -13.104 1.00 14.23 ?  27   ALA   B O    1 
ATOM   4296 C  CB   . ALA   B 1 27  ? 51.173 -19.951 -10.120 1.00 12.74 ?  27   ALA   B CB   1 
ATOM   4297 H  H    . ALA   B 1 27  ? 51.169 -22.212 -11.011 1.00 14.53 ?  27   ALA   B H    1 
ATOM   4298 H  HA   . ALA   B 1 27  ? 50.160 -19.996 -11.892 1.00 15.18 ?  27   ALA   B HA   1 
ATOM   4299 H  HB1  . ALA   B 1 27  ? 51.138 -18.985 -10.032 1.00 15.32 ?  27   ALA   B HB1  1 
ATOM   4300 H  HB2  . ALA   B 1 27  ? 50.444 -20.351 -9.616  1.00 15.32 ?  27   ALA   B HB2  1 
ATOM   4301 H  HB3  . ALA   B 1 27  ? 52.021 -20.283 -9.793  1.00 15.32 ?  27   ALA   B HB3  1 
ATOM   4302 N  N    . LYS   B 1 28  ? 53.304 -20.214 -12.425 1.00 14.98 ?  28   LYS   B N    1 
ATOM   4303 C  CA   . LYS   B 1 28  ? 54.385 -19.585 -13.172 1.00 17.09 ?  28   LYS   B CA   1 
ATOM   4304 C  C    . LYS   B 1 28  ? 54.137 -19.639 -14.674 1.00 18.01 ?  28   LYS   B C    1 
ATOM   4305 O  O    . LYS   B 1 28  ? 54.561 -18.732 -15.402 1.00 18.81 ?  28   LYS   B O    1 
ATOM   4306 C  CB   . LYS   B 1 28  ? 55.736 -20.194 -12.782 1.00 19.76 ?  28   LYS   B CB   1 
ATOM   4307 C  CG   . LYS   B 1 28  ? 56.135 -19.889 -11.337 1.00 22.60 ?  28   LYS   B CG   1 
ATOM   4308 C  CD   . LYS   B 1 28  ? 57.569 -20.282 -11.019 1.00 26.66 ?  28   LYS   B CD   1 
ATOM   4309 C  CE   . LYS   B 1 28  ? 57.683 -21.751 -10.684 1.00 29.76 ?  28   LYS   B CE   1 
ATOM   4310 N  NZ   . LYS   B 1 28  ? 59.035 -22.089 -10.159 1.00 30.61 ?  28   LYS   B NZ   1 
ATOM   4311 H  H    . LYS   B 1 28  ? 53.523 -20.930 -11.999 1.00 18.00 ?  28   LYS   B H    1 
ATOM   4312 H  HA   . LYS   B 1 28  ? 54.420 -18.649 -12.927 1.00 20.54 ?  28   LYS   B HA   1 
ATOM   4313 H  HB2  . LYS   B 1 28  ? 55.695 -21.156 -12.878 1.00 23.74 ?  28   LYS   B HB2  1 
ATOM   4314 H  HB3  . LYS   B 1 28  ? 56.428 -19.831 -13.357 1.00 23.74 ?  28   LYS   B HB3  1 
ATOM   4315 H  HG2  . LYS   B 1 28  ? 56.041 -18.935 -11.179 1.00 27.15 ?  28   LYS   B HG2  1 
ATOM   4316 H  HG3  . LYS   B 1 28  ? 55.548 -20.380 -10.739 1.00 27.15 ?  28   LYS   B HG3  1 
ATOM   4317 H  HD2  . LYS   B 1 28  ? 58.126 -20.099 -11.791 1.00 32.02 ?  28   LYS   B HD2  1 
ATOM   4318 H  HD3  . LYS   B 1 28  ? 57.876 -19.768 -10.254 1.00 32.02 ?  28   LYS   B HD3  1 
ATOM   4319 H  HE2  . LYS   B 1 28  ? 57.027 -21.976 -10.004 1.00 35.73 ?  28   LYS   B HE2  1 
ATOM   4320 H  HE3  . LYS   B 1 28  ? 57.526 -22.276 -11.484 1.00 35.73 ?  28   LYS   B HE3  1 
ATOM   4321 H  HZ1  . LYS   B 1 28  ? 59.079 -22.957 -9.968  1.00 36.76 ?  28   LYS   B HZ1  1 
ATOM   4322 H  HZ2  . LYS   B 1 28  ? 59.653 -21.894 -10.767 1.00 36.76 ?  28   LYS   B HZ2  1 
ATOM   4323 H  HZ3  . LYS   B 1 28  ? 59.198 -21.622 -9.418  1.00 36.76 ?  28   LYS   B HZ3  1 
ATOM   4324 N  N    A LYS   B 1 29  ? 53.435 -20.669 -15.151 0.60 18.83 ?  29   LYS   B N    1 
ATOM   4325 N  N    B LYS   B 1 29  ? 53.438 -20.668 -15.151 0.40 18.96 ?  29   LYS   B N    1 
ATOM   4326 C  CA   A LYS   B 1 29  ? 53.152 -20.817 -16.575 0.60 21.17 ?  29   LYS   B CA   1 
ATOM   4327 C  CA   B LYS   B 1 29  ? 53.155 -20.783 -16.576 0.40 20.88 ?  29   LYS   B CA   1 
ATOM   4328 C  C    A LYS   B 1 29  ? 51.885 -20.087 -17.016 0.60 20.34 ?  29   LYS   B C    1 
ATOM   4329 C  C    B LYS   B 1 29  ? 51.910 -19.994 -16.976 0.40 20.04 ?  29   LYS   B C    1 
ATOM   4330 O  O    A LYS   B 1 29  ? 51.856 -19.515 -18.111 0.60 21.31 ?  29   LYS   B O    1 
ATOM   4331 O  O    B LYS   B 1 29  ? 51.928 -19.264 -17.972 0.40 20.69 ?  29   LYS   B O    1 
ATOM   4332 C  CB   A LYS   B 1 29  ? 53.034 -22.301 -16.936 0.60 24.81 ?  29   LYS   B CB   1 
ATOM   4333 C  CB   B LYS   B 1 29  ? 53.005 -22.259 -16.959 0.40 23.99 ?  29   LYS   B CB   1 
ATOM   4334 C  CG   A LYS   B 1 29  ? 52.783 -22.556 -18.415 0.60 28.11 ?  29   LYS   B CG   1 
ATOM   4335 C  CG   B LYS   B 1 29  ? 52.905 -22.509 -18.456 0.40 26.80 ?  29   LYS   B CG   1 
ATOM   4336 C  CD   A LYS   B 1 29  ? 52.994 -24.018 -18.785 0.60 30.71 ?  29   LYS   B CD   1 
ATOM   4337 C  CD   B LYS   B 1 29  ? 53.150 -23.973 -18.797 0.40 28.97 ?  29   LYS   B CD   1 
ATOM   4338 C  CE   A LYS   B 1 29  ? 51.910 -24.916 -18.211 0.60 32.50 ?  29   LYS   B CE   1 
ATOM   4339 C  CE   B LYS   B 1 29  ? 52.097 -24.880 -18.178 0.40 30.44 ?  29   LYS   B CE   1 
ATOM   4340 N  NZ   A LYS   B 1 29  ? 52.108 -26.340 -18.608 0.60 33.48 ?  29   LYS   B NZ   1 
ATOM   4341 N  NZ   B LYS   B 1 29  ? 52.324 -26.310 -18.529 0.40 31.33 ?  29   LYS   B NZ   1 
ATOM   4342 H  H    A LYS   B 1 29  ? 53.116 -21.301 -14.661 0.60 22.63 ?  29   LYS   B H    1 
ATOM   4343 H  H    B LYS   B 1 29  ? 53.115 -21.308 -14.669 0.40 22.78 ?  29   LYS   B H    1 
ATOM   4344 H  HA   A LYS   B 1 29  ? 53.893 -20.448 -17.075 0.60 25.43 ?  29   LYS   B HA   1 
ATOM   4345 H  HA   B LYS   B 1 29  ? 53.904 -20.424 -17.073 0.40 25.08 ?  29   LYS   B HA   1 
ATOM   4346 H  HB2  A LYS   B 1 29  ? 53.861 -22.748 -16.696 0.60 29.80 ?  29   LYS   B HB2  1 
ATOM   4347 H  HB2  B LYS   B 1 29  ? 53.778 -22.745 -16.631 0.40 28.81 ?  29   LYS   B HB2  1 
ATOM   4348 H  HB3  A LYS   B 1 29  ? 52.296 -22.687 -16.441 0.60 29.80 ?  29   LYS   B HB3  1 
ATOM   4349 H  HB3  B LYS   B 1 29  ? 52.200 -22.607 -16.547 0.40 28.81 ?  29   LYS   B HB3  1 
ATOM   4350 H  HG2  A LYS   B 1 29  ? 51.866 -22.320 -18.627 0.60 33.76 ?  29   LYS   B HG2  1 
ATOM   4351 H  HG2  B LYS   B 1 29  ? 52.015 -22.271 -18.761 0.40 32.18 ?  29   LYS   B HG2  1 
ATOM   4352 H  HG3  A LYS   B 1 29  ? 53.397 -22.018 -18.939 0.60 33.76 ?  29   LYS   B HG3  1 
ATOM   4353 H  HG3  B LYS   B 1 29  ? 53.572 -21.975 -18.915 0.40 32.18 ?  29   LYS   B HG3  1 
ATOM   4354 H  HD2  A LYS   B 1 29  ? 52.981 -24.106 -19.751 0.60 36.88 ?  29   LYS   B HD2  1 
ATOM   4355 H  HD2  B LYS   B 1 29  ? 53.119 -24.087 -19.760 0.40 34.79 ?  29   LYS   B HD2  1 
ATOM   4356 H  HD3  A LYS   B 1 29  ? 53.849 -24.315 -18.435 0.60 36.88 ?  29   LYS   B HD3  1 
ATOM   4357 H  HD3  B LYS   B 1 29  ? 54.018 -24.241 -18.456 0.40 34.79 ?  29   LYS   B HD3  1 
ATOM   4358 H  HE2  A LYS   B 1 29  ? 51.930 -24.867 -17.243 0.60 39.03 ?  29   LYS   B HE2  1 
ATOM   4359 H  HE2  B LYS   B 1 29  ? 52.130 -24.799 -17.212 0.40 36.56 ?  29   LYS   B HE2  1 
ATOM   4360 H  HE3  A LYS   B 1 29  ? 51.045 -24.627 -18.543 0.60 39.03 ?  29   LYS   B HE3  1 
ATOM   4361 H  HE3  B LYS   B 1 29  ? 51.221 -24.621 -18.506 0.40 36.56 ?  29   LYS   B HE3  1 
ATOM   4362 H  HZ1  A LYS   B 1 29  ? 51.462 -26.846 -18.261 0.60 40.20 ?  29   LYS   B HZ1  1 
ATOM   4363 H  HZ1  B LYS   B 1 29  ? 51.696 -26.818 -18.155 0.40 37.62 ?  29   LYS   B HZ1  1 
ATOM   4364 H  HZ2  A LYS   B 1 29  ? 52.089 -26.415 -19.495 0.60 40.20 ?  29   LYS   B HZ2  1 
ATOM   4365 H  HZ2  B LYS   B 1 29  ? 52.293 -26.415 -19.412 0.40 37.62 ?  29   LYS   B HZ2  1 
ATOM   4366 H  HZ3  A LYS   B 1 29  ? 52.895 -26.632 -18.311 0.60 40.20 ?  29   LYS   B HZ3  1 
ATOM   4367 H  HZ3  B LYS   B 1 29  ? 53.122 -26.572 -18.234 0.40 37.62 ?  29   LYS   B HZ3  1 
ATOM   4368 N  N    . VAL   B 1 30  ? 50.831 -20.121 -16.197 1.00 19.02 ?  30   VAL   B N    1 
ATOM   4369 C  CA   . VAL   B 1 30  ? 49.544 -19.521 -16.570 1.00 19.07 ?  30   VAL   B CA   1 
ATOM   4370 C  C    . VAL   B 1 30  ? 49.540 -18.008 -16.396 1.00 18.11 ?  30   VAL   B C    1 
ATOM   4371 O  O    . VAL   B 1 30  ? 48.795 -17.295 -17.084 1.00 19.10 ?  30   VAL   B O    1 
ATOM   4372 C  CB   . VAL   B 1 30  ? 48.432 -20.159 -15.709 1.00 20.27 ?  30   VAL   B CB   1 
ATOM   4373 C  CG1  . VAL   B 1 30  ? 47.138 -19.353 -15.787 1.00 20.45 ?  30   VAL   B CG1  1 
ATOM   4374 C  CG2  . VAL   B 1 30  ? 48.201 -21.610 -16.114 1.00 21.06 ?  30   VAL   B CG2  1 
ATOM   4375 H  H    A VAL   B 1 30  ? 50.827 -20.507 -15.422 0.60 22.86 ?  30   VAL   B H    1 
ATOM   4376 H  H    B VAL   B 1 30  ? 50.813 -20.560 -15.450 0.40 22.86 ?  30   VAL   B H    1 
ATOM   4377 H  HA   . VAL   B 1 30  ? 49.353 -19.738 -17.498 1.00 22.91 ?  30   VAL   B HA   1 
ATOM   4378 H  HB   . VAL   B 1 30  ? 48.717 -20.164 -14.782 1.00 24.35 ?  30   VAL   B HB   1 
ATOM   4379 H  HG11 . VAL   B 1 30  ? 46.394 -19.937 -15.564 1.00 24.57 ?  30   VAL   B HG11 1 
ATOM   4380 H  HG12 . VAL   B 1 30  ? 47.177 -18.622 -15.153 1.00 24.57 ?  30   VAL   B HG12 1 
ATOM   4381 H  HG13 . VAL   B 1 30  ? 47.022 -19.019 -16.686 1.00 24.57 ?  30   VAL   B HG13 1 
ATOM   4382 H  HG21 . VAL   B 1 30  ? 47.503 -21.993 -15.552 1.00 25.30 ?  30   VAL   B HG21 1 
ATOM   4383 H  HG22 . VAL   B 1 30  ? 47.921 -21.641 -17.044 1.00 25.30 ?  30   VAL   B HG22 1 
ATOM   4384 H  HG23 . VAL   B 1 30  ? 49.023 -22.109 -15.999 1.00 25.30 ?  30   VAL   B HG23 1 
ATOM   4385 N  N    . LYS   B 1 31  ? 50.319 -17.505 -15.451 1.00 17.84 ?  31   LYS   B N    1 
ATOM   4386 C  CA   . LYS   B 1 31  ? 50.336 -16.099 -15.081 1.00 18.32 ?  31   LYS   B CA   1 
ATOM   4387 C  C    . LYS   B 1 31  ? 48.934 -15.633 -14.689 1.00 16.16 ?  31   LYS   B C    1 
ATOM   4388 O  O    . LYS   B 1 31  ? 48.391 -14.706 -15.303 1.00 17.44 ?  31   LYS   B O    1 
ATOM   4389 C  CB   . LYS   B 1 31  ? 50.964 -15.270 -16.210 1.00 21.69 ?  31   LYS   B CB   1 
ATOM   4390 C  CG   . LYS   B 1 31  ? 52.381 -15.728 -16.563 1.00 24.76 ?  31   LYS   B CG   1 
ATOM   4391 C  CD   . LYS   B 1 31  ? 52.969 -14.947 -17.720 1.00 27.62 ?  31   LYS   B CD   1 
ATOM   4392 C  CE   . LYS   B 1 31  ? 54.442 -15.252 -17.890 1.00 29.74 ?  31   LYS   B CE   1 
ATOM   4393 N  NZ   . LYS   B 1 31  ? 55.204 -14.905 -16.660 1.00 30.61 ?  31   LYS   B NZ   1 
ATOM   4394 H  H    . LYS   B 1 31  ? 50.859 -17.990 -14.998 1.00 21.43 ?  31   LYS   B H    1 
ATOM   4395 H  HA   . LYS   B 1 31  ? 50.890 -16.013 -14.306 1.00 22.01 ?  31   LYS   B HA   1 
ATOM   4396 H  HB2  . LYS   B 1 31  ? 50.414 -15.349 -17.008 1.00 26.05 ?  31   LYS   B HB2  1 
ATOM   4397 H  HB3  . LYS   B 1 31  ? 51.004 -14.347 -15.925 1.00 26.05 ?  31   LYS   B HB3  1 
ATOM   4398 H  HG2  . LYS   B 1 31  ? 52.946 -15.607 -15.785 1.00 29.74 ?  31   LYS   B HG2  1 
ATOM   4399 H  HG3  . LYS   B 1 31  ? 52.357 -16.669 -16.811 1.00 29.74 ?  31   LYS   B HG3  1 
ATOM   4400 H  HD2  . LYS   B 1 31  ? 52.506 -15.194 -18.536 1.00 33.17 ?  31   LYS   B HD2  1 
ATOM   4401 H  HD3  . LYS   B 1 31  ? 52.866 -14.000 -17.546 1.00 33.17 ?  31   LYS   B HD3  1 
ATOM   4402 H  HE2  . LYS   B 1 31  ? 54.558 -16.200 -18.064 1.00 35.72 ?  31   LYS   B HE2  1 
ATOM   4403 H  HE3  . LYS   B 1 31  ? 54.794 -14.729 -18.626 1.00 35.72 ?  31   LYS   B HE3  1 
ATOM   4404 H  HZ1  . LYS   B 1 31  ? 56.077 -14.943 -16.822 1.00 36.75 ?  31   LYS   B HZ1  1 
ATOM   4405 H  HZ2  . LYS   B 1 31  ? 54.994 -14.081 -16.395 1.00 36.75 ?  31   LYS   B HZ2  1 
ATOM   4406 H  HZ3  . LYS   B 1 31  ? 55.005 -15.476 -16.006 1.00 36.75 ?  31   LYS   B HZ3  1 
ATOM   4407 N  N    . PRO   B 1 32  ? 48.316 -16.251 -13.673 1.00 13.49 ?  32   PRO   B N    1 
ATOM   4408 C  CA   . PRO   B 1 32  ? 46.931 -15.903 -13.326 1.00 12.49 ?  32   PRO   B CA   1 
ATOM   4409 C  C    . PRO   B 1 32  ? 46.838 -14.560 -12.625 1.00 12.54 ?  32   PRO   B C    1 
ATOM   4410 O  O    . PRO   B 1 32  ? 47.756 -14.137 -11.917 1.00 14.13 ?  32   PRO   B O    1 
ATOM   4411 C  CB   . PRO   B 1 32  ? 46.527 -17.025 -12.363 1.00 12.84 ?  32   PRO   B CB   1 
ATOM   4412 C  CG   . PRO   B 1 32  ? 47.827 -17.359 -11.672 1.00 13.10 ?  32   PRO   B CG   1 
ATOM   4413 C  CD   . PRO   B 1 32  ? 48.882 -17.245 -12.740 1.00 13.44 ?  32   PRO   B CD   1 
ATOM   4414 H  HA   . PRO   B 1 32  ? 46.354 -15.919 -14.110 1.00 15.01 ?  32   PRO   B HA   1 
ATOM   4415 H  HB2  . PRO   B 1 32  ? 45.866 -16.699 -11.727 1.00 15.43 ?  32   PRO   B HB2  1 
ATOM   4416 H  HB3  . PRO   B 1 32  ? 46.186 -17.787 -12.856 1.00 15.43 ?  32   PRO   B HB3  1 
ATOM   4417 H  HG2  . PRO   B 1 32  ? 47.991 -16.720 -10.959 1.00 15.74 ?  32   PRO   B HG2  1 
ATOM   4418 H  HG3  . PRO   B 1 32  ? 47.789 -18.262 -11.320 1.00 15.74 ?  32   PRO   B HG3  1 
ATOM   4419 H  HD2  . PRO   B 1 32  ? 49.708 -16.919 -12.359 1.00 16.16 ?  32   PRO   B HD2  1 
ATOM   4420 H  HD3  . PRO   B 1 32  ? 48.998 -18.099 -13.181 1.00 16.16 ?  32   PRO   B HD3  1 
ATOM   4421 N  N    . THR   B 1 33  ? 45.688 -13.905 -12.795 1.00 12.07 ?  33   THR   B N    1 
ATOM   4422 C  CA   . THR   B 1 33  ? 45.394 -12.728 -11.987 1.00 12.35 ?  33   THR   B CA   1 
ATOM   4423 C  C    . THR   B 1 33  ? 45.351 -13.081 -10.507 1.00 11.89 ?  33   THR   B C    1 
ATOM   4424 O  O    . THR   B 1 33  ? 45.817 -12.300 -9.664  1.00 13.03 ?  33   THR   B O    1 
ATOM   4425 C  CB   . THR   B 1 33  ? 44.074 -12.096 -12.433 1.00 13.08 ?  33   THR   B CB   1 
ATOM   4426 O  OG1  . THR   B 1 33  ? 44.122 -11.831 -13.837 1.00 13.15 ?  33   THR   B OG1  1 
ATOM   4427 C  CG2  . THR   B 1 33  ? 43.814 -10.801 -11.683 1.00 14.39 ?  33   THR   B CG2  1 
ATOM   4428 H  H    . THR   B 1 33  ? 45.066 -14.124 -13.356 1.00 14.52 ?  33   THR   B H    1 
ATOM   4429 H  HA   . THR   B 1 33  ? 46.094 -12.077 -12.118 1.00 14.85 ?  33   THR   B HA   1 
ATOM   4430 H  HB   . THR   B 1 33  ? 43.340 -12.710 -12.247 1.00 15.72 ?  33   THR   B HB   1 
ATOM   4431 H  HG1  . THR   B 1 33  ? 43.397 -11.475 -14.091 1.00 15.81 ?  33   THR   B HG1  1 
ATOM   4432 H  HG21 . THR   B 1 33  ? 43.059 -10.337 -12.072 1.00 17.29 ?  33   THR   B HG21 1 
ATOM   4433 H  HG22 . THR   B 1 33  ? 43.624 -10.989 -10.750 1.00 17.29 ?  33   THR   B HG22 1 
ATOM   4434 H  HG23 . THR   B 1 33  ? 44.597 -10.230 -11.735 1.00 17.29 ?  33   THR   B HG23 1 
ATOM   4435 N  N    . VAL   B 1 34  ? 44.811 -14.256 -10.171 1.00 11.24 ?  34   VAL   B N    1 
ATOM   4436 C  CA   . VAL   B 1 34  ? 44.614 -14.654 -8.781  1.00 10.65 ?  34   VAL   B CA   1 
ATOM   4437 C  C    . VAL   B 1 34  ? 45.054 -16.103 -8.618  1.00 9.75  ?  34   VAL   B C    1 
ATOM   4438 O  O    . VAL   B 1 34  ? 44.536 -16.993 -9.304  1.00 10.62 ?  34   VAL   B O    1 
ATOM   4439 C  CB   . VAL   B 1 34  ? 43.147 -14.512 -8.328  1.00 11.88 ?  34   VAL   B CB   1 
ATOM   4440 C  CG1  . VAL   B 1 34  ? 42.991 -14.979 -6.887  1.00 12.22 ?  34   VAL   B CG1  1 
ATOM   4441 C  CG2  . VAL   B 1 34  ? 42.643 -13.088 -8.505  1.00 13.04 ?  34   VAL   B CG2  1 
ATOM   4442 H  H    . VAL   B 1 34  ? 44.554 -14.854 -10.738 1.00 13.51 ?  34   VAL   B H    1 
ATOM   4443 H  HA   . VAL   B 1 34  ? 45.167 -14.101 -8.204  1.00 12.80 ?  34   VAL   B HA   1 
ATOM   4444 H  HB   . VAL   B 1 34  ? 42.597 -15.089 -8.883  1.00 14.28 ?  34   VAL   B HB   1 
ATOM   4445 H  HG11 . VAL   B 1 34  ? 42.140 -14.664 -6.544  1.00 14.69 ?  34   VAL   B HG11 1 
ATOM   4446 H  HG12 . VAL   B 1 34  ? 43.014 -15.950 -6.860  1.00 14.69 ?  34   VAL   B HG12 1 
ATOM   4447 H  HG13 . VAL   B 1 34  ? 43.715 -14.615 -6.356  1.00 14.69 ?  34   VAL   B HG13 1 
ATOM   4448 H  HG21 . VAL   B 1 34  ? 41.725 -13.036 -8.194  1.00 15.68 ?  34   VAL   B HG21 1 
ATOM   4449 H  HG22 . VAL   B 1 34  ? 43.201 -12.488 -7.986  1.00 15.68 ?  34   VAL   B HG22 1 
ATOM   4450 H  HG23 . VAL   B 1 34  ? 42.687 -12.851 -9.445  1.00 15.68 ?  34   VAL   B HG23 1 
ATOM   4451 N  N    . VAL   B 1 35  ? 45.969 -16.349 -7.682  1.00 9.39  ?  35   VAL   B N    1 
ATOM   4452 C  CA   . VAL   B 1 35  ? 46.205 -17.695 -7.168  1.00 9.48  ?  35   VAL   B CA   1 
ATOM   4453 C  C    . VAL   B 1 35  ? 45.670 -17.758 -5.746  1.00 9.06  ?  35   VAL   B C    1 
ATOM   4454 O  O    . VAL   B 1 35  ? 45.893 -16.838 -4.952  1.00 9.44  ?  35   VAL   B O    1 
ATOM   4455 C  CB   . VAL   B 1 35  ? 47.690 -18.122 -7.251  1.00 9.92  ?  35   VAL   B CB   1 
ATOM   4456 C  CG1  . VAL   B 1 35  ? 48.597 -17.274 -6.346  1.00 10.40 ?  35   VAL   B CG1  1 
ATOM   4457 C  CG2  . VAL   B 1 35  ? 47.840 -19.616 -6.935  1.00 10.49 ?  35   VAL   B CG2  1 
ATOM   4458 H  H    . VAL   B 1 35  ? 46.474 -15.748 -7.330  1.00 11.29 ?  35   VAL   B H    1 
ATOM   4459 H  HA   . VAL   B 1 35  ? 45.692 -18.325 -7.700  1.00 11.40 ?  35   VAL   B HA   1 
ATOM   4460 H  HB   . VAL   B 1 35  ? 47.992 -17.997 -8.167  1.00 11.94 ?  35   VAL   B HB   1 
ATOM   4461 H  HG11 . VAL   B 1 35  ? 49.519 -17.511 -6.517  1.00 12.51 ?  35   VAL   B HG11 1 
ATOM   4462 H  HG12 . VAL   B 1 35  ? 48.444 -16.341 -6.538  1.00 12.51 ?  35   VAL   B HG12 1 
ATOM   4463 H  HG13 . VAL   B 1 35  ? 48.374 -17.465 -5.418  1.00 12.51 ?  35   VAL   B HG13 1 
ATOM   4464 H  HG21 . VAL   B 1 35  ? 48.763 -19.882 -7.043  1.00 12.62 ?  35   VAL   B HG21 1 
ATOM   4465 H  HG22 . VAL   B 1 35  ? 47.552 -19.783 -6.020  1.00 12.62 ?  35   VAL   B HG22 1 
ATOM   4466 H  HG23 . VAL   B 1 35  ? 47.278 -20.134 -7.546  1.00 12.62 ?  35   VAL   B HG23 1 
ATOM   4467 N  N    . VAL   B 1 36  ? 44.950 -18.836 -5.430  1.00 9.09  ?  36   VAL   B N    1 
ATOM   4468 C  CA   . VAL   B 1 36  ? 44.406 -19.041 -4.098  1.00 8.69  ?  36   VAL   B CA   1 
ATOM   4469 C  C    . VAL   B 1 36  ? 45.421 -19.801 -3.252  1.00 8.47  ?  36   VAL   B C    1 
ATOM   4470 O  O    . VAL   B 1 36  ? 45.957 -20.834 -3.676  1.00 9.61  ?  36   VAL   B O    1 
ATOM   4471 C  CB   . VAL   B 1 36  ? 43.075 -19.806 -4.171  1.00 9.17  ?  36   VAL   B CB   1 
ATOM   4472 C  CG1  . VAL   B 1 36  ? 42.580 -20.162 -2.777  1.00 9.95  ?  36   VAL   B CG1  1 
ATOM   4473 C  CG2  . VAL   B 1 36  ? 42.038 -18.980 -4.915  1.00 9.80  ?  36   VAL   B CG2  1 
ATOM   4474 H  H    . VAL   B 1 36  ? 44.773 -19.477 -5.981  1.00 10.93 ?  36   VAL   B H    1 
ATOM   4475 H  HA   . VAL   B 1 36  ? 44.243 -18.179 -3.684  1.00 10.46 ?  36   VAL   B HA   1 
ATOM   4476 H  HB   . VAL   B 1 36  ? 43.212 -20.630 -4.664  1.00 11.03 ?  36   VAL   B HB   1 
ATOM   4477 H  HG11 . VAL   B 1 36  ? 41.642 -20.398 -2.830  1.00 11.96 ?  36   VAL   B HG11 1 
ATOM   4478 H  HG12 . VAL   B 1 36  ? 43.092 -20.909 -2.437  1.00 11.96 ?  36   VAL   B HG12 1 
ATOM   4479 H  HG13 . VAL   B 1 36  ? 42.691 -19.389 -2.197  1.00 11.96 ?  36   VAL   B HG13 1 
ATOM   4480 H  HG21 . VAL   B 1 36  ? 41.201 -19.461 -4.935  1.00 11.78 ?  36   VAL   B HG21 1 
ATOM   4481 H  HG22 . VAL   B 1 36  ? 41.925 -18.129 -4.458  1.00 11.78 ?  36   VAL   B HG22 1 
ATOM   4482 H  HG23 . VAL   B 1 36  ? 42.352 -18.820 -5.824  1.00 11.78 ?  36   VAL   B HG23 1 
ATOM   4483 N  N    . ASN   B 1 37  ? 45.646 -19.310 -2.035  1.00 8.78  ?  37   ASN   B N    1 
ATOM   4484 C  CA   . ASN   B 1 37  ? 46.403 -20.037 -1.030  1.00 9.33  ?  37   ASN   B CA   1 
ATOM   4485 C  C    . ASN   B 1 37  ? 45.459 -20.715 -0.043  1.00 9.16  ?  37   ASN   B C    1 
ATOM   4486 O  O    . ASN   B 1 37  ? 44.448 -20.140 0.373   1.00 9.58  ?  37   ASN   B O    1 
ATOM   4487 C  CB   . ASN   B 1 37  ? 47.336 -19.090 -0.274  1.00 9.44  ?  37   ASN   B CB   1 
ATOM   4488 C  CG   . ASN   B 1 37  ? 48.192 -19.808 0.737   1.00 9.39  ?  37   ASN   B CG   1 
ATOM   4489 O  OD1  . ASN   B 1 37  ? 48.532 -20.979 0.556   1.00 10.17 ?  37   ASN   B OD1  1 
ATOM   4490 N  ND2  . ASN   B 1 37  ? 48.550 -19.113 1.810   1.00 9.74  ?  37   ASN   B ND2  1 
ATOM   4491 H  H    . ASN   B 1 37  ? 45.365 -18.543 -1.756  1.00 10.57 ?  37   ASN   B H    1 
ATOM   4492 H  HA   . ASN   B 1 37  ? 46.937 -20.728 -1.453  1.00 11.22 ?  37   ASN   B HA   1 
ATOM   4493 H  HB2  . ASN   B 1 37  ? 47.926 -18.662 -0.912  1.00 11.36 ?  37   ASN   B HB2  1 
ATOM   4494 H  HB3  . ASN   B 1 37  ? 46.810 -18.433 0.197   1.00 11.36 ?  37   ASN   B HB3  1 
ATOM   4495 H  HD21 . ASN   B 1 37  ? 49.040 -19.481 2.416   1.00 11.71 ?  37   ASN   B HD21 1 
ATOM   4496 H  HD22 . ASN   B 1 37  ? 48.292 -18.306 1.904   1.00 11.71 ?  37   ASN   B HD22 1 
ATOM   4497 N  N    . ALA   B 1 38  ? 45.810 -21.947 0.331   1.00 9.32  ?  38   ALA   B N    1 
ATOM   4498 C  CA   . ALA   B 1 38  ? 45.161 -22.695 1.408   1.00 9.68  ?  38   ALA   B CA   1 
ATOM   4499 C  C    . ALA   B 1 38  ? 45.747 -22.212 2.732   1.00 9.66  ?  38   ALA   B C    1 
ATOM   4500 O  O    . ALA   B 1 38  ? 46.655 -22.814 3.313   1.00 10.56 ?  38   ALA   B O    1 
ATOM   4501 C  CB   . ALA   B 1 38  ? 45.393 -24.186 1.209   1.00 10.71 ?  38   ALA   B CB   1 
ATOM   4502 H  H    . ALA   B 1 38  ? 46.457 -22.383 -0.025  1.00 11.21 ?  38   ALA   B H    1 
ATOM   4503 H  HA   . ALA   B 1 38  ? 44.206 -22.520 1.408   1.00 11.64 ?  38   ALA   B HA   1 
ATOM   4504 H  HB1  . ALA   B 1 38  ? 44.951 -24.676 1.932   1.00 12.87 ?  38   ALA   B HB1  1 
ATOM   4505 H  HB2  . ALA   B 1 38  ? 45.013 -24.457 0.359   1.00 12.87 ?  38   ALA   B HB2  1 
ATOM   4506 H  HB3  . ALA   B 1 38  ? 46.341 -24.370 1.227   1.00 12.87 ?  38   ALA   B HB3  1 
ATOM   4507 N  N    . ALA   B 1 39  ? 45.232 -21.071 3.193   1.00 9.66  ?  39   ALA   B N    1 
ATOM   4508 C  CA   . ALA   B 1 39  ? 45.783 -20.334 4.318   1.00 9.91  ?  39   ALA   B CA   1 
ATOM   4509 C  C    . ALA   B 1 39  ? 45.168 -20.784 5.641   1.00 9.99  ?  39   ALA   B C    1 
ATOM   4510 O  O    . ALA   B 1 39  ? 44.145 -21.466 5.689   1.00 10.83 ?  39   ALA   B O    1 
ATOM   4511 C  CB   . ALA   B 1 39  ? 45.541 -18.834 4.116   1.00 10.48 ?  39   ALA   B CB   1 
ATOM   4512 H  H    . ALA   B 1 39  ? 44.535 -20.699 2.855   1.00 11.62 ?  39   ALA   B H    1 
ATOM   4513 H  HA   . ALA   B 1 39  ? 46.737 -20.485 4.360   1.00 11.92 ?  39   ALA   B HA   1 
ATOM   4514 H  HB1  . ALA   B 1 39  ? 45.914 -18.351 4.870   1.00 12.61 ?  39   ALA   B HB1  1 
ATOM   4515 H  HB2  . ALA   B 1 39  ? 45.980 -18.552 3.296   1.00 12.61 ?  39   ALA   B HB2  1 
ATOM   4516 H  HB3  . ALA   B 1 39  ? 44.589 -18.670 4.054   1.00 12.61 ?  39   ALA   B HB3  1 
ATOM   4517 N  N    . ASN   B 1 40  ? 45.806 -20.355 6.729   1.00 10.80 ?  40   ASN   B N    1 
ATOM   4518 C  CA   . ASN   B 1 40  ? 45.250 -20.416 8.071   1.00 11.53 ?  40   ASN   B CA   1 
ATOM   4519 C  C    . ASN   B 1 40  ? 45.068 -18.991 8.601   1.00 10.91 ?  40   ASN   B C    1 
ATOM   4520 O  O    . ASN   B 1 40  ? 45.481 -18.007 7.976   1.00 11.07 ?  40   ASN   B O    1 
ATOM   4521 C  CB   . ASN   B 1 40  ? 46.106 -21.293 9.005   1.00 12.45 ?  40   ASN   B CB   1 
ATOM   4522 C  CG   . ASN   B 1 40  ? 47.564 -20.894 9.020   1.00 13.26 ?  40   ASN   B CG   1 
ATOM   4523 O  OD1  . ASN   B 1 40  ? 47.882 -19.714 9.065   1.00 15.07 ?  40   ASN   B OD1  1 
ATOM   4524 N  ND2  . ASN   B 1 40  ? 48.456 -21.872 8.989   1.00 13.29 ?  40   ASN   B ND2  1 
ATOM   4525 H  H    . ASN   B 1 40  ? 46.597 -20.013 6.707   1.00 12.99 ?  40   ASN   B H    1 
ATOM   4526 H  HA   . ASN   B 1 40  ? 44.372 -20.816 8.026   1.00 13.86 ?  40   ASN   B HA   1 
ATOM   4527 H  HB2  . ASN   B 1 40  ? 45.764 -21.221 9.911   1.00 14.97 ?  40   ASN   B HB2  1 
ATOM   4528 H  HB3  . ASN   B 1 40  ? 46.053 -22.216 8.706   1.00 14.97 ?  40   ASN   B HB3  1 
ATOM   4529 H  HD21 . ASN   B 1 40  ? 49.298 -21.688 8.999   1.00 15.97 ?  40   ASN   B HD21 1 
ATOM   4530 H  HD22 . ASN   B 1 40  ? 48.197 -22.691 8.957   1.00 15.97 ?  40   ASN   B HD22 1 
ATOM   4531 N  N    . VAL   B 1 41  ? 44.417 -18.870 9.761   1.00 11.42 ?  41   VAL   B N    1 
ATOM   4532 C  CA   . VAL   B 1 41  ? 43.959 -17.551 10.208  1.00 12.36 ?  41   VAL   B CA   1 
ATOM   4533 C  C    . VAL   B 1 41  ? 45.112 -16.600 10.506  1.00 11.97 ?  41   VAL   B C    1 
ATOM   4534 O  O    . VAL   B 1 41  ? 44.936 -15.379 10.432  1.00 12.21 ?  41   VAL   B O    1 
ATOM   4535 C  CB   . VAL   B 1 41  ? 42.984 -17.635 11.399  1.00 13.95 ?  41   VAL   B CB   1 
ATOM   4536 C  CG1  . VAL   B 1 41  ? 41.694 -18.329 10.993  1.00 14.44 ?  41   VAL   B CG1  1 
ATOM   4537 C  CG2  . VAL   B 1 41  ? 43.634 -18.325 12.589  1.00 14.98 ?  41   VAL   B CG2  1 
ATOM   4538 H  H    . VAL   B 1 41  ? 44.237 -19.516 10.295  1.00 13.73 ?  41   VAL   B H    1 
ATOM   4539 H  HA   . VAL   B 1 41  ? 43.464 -17.155 9.479   1.00 14.86 ?  41   VAL   B HA   1 
ATOM   4540 H  HB   . VAL   B 1 41  ? 42.757 -16.733 11.676  1.00 16.76 ?  41   VAL   B HB   1 
ATOM   4541 H  HG11 . VAL   B 1 41  ? 41.091 -18.345 11.754  1.00 17.35 ?  41   VAL   B HG11 1 
ATOM   4542 H  HG12 . VAL   B 1 41  ? 41.288 -17.839 10.261  1.00 17.35 ?  41   VAL   B HG12 1 
ATOM   4543 H  HG13 . VAL   B 1 41  ? 41.897 -19.235 10.714  1.00 17.35 ?  41   VAL   B HG13 1 
ATOM   4544 H  HG21 . VAL   B 1 41  ? 43.000 -18.354 13.321  1.00 18.00 ?  41   VAL   B HG21 1 
ATOM   4545 H  HG22 . VAL   B 1 41  ? 43.885 -19.228 12.333  1.00 18.00 ?  41   VAL   B HG22 1 
ATOM   4546 H  HG23 . VAL   B 1 41  ? 44.423 -17.826 12.853  1.00 18.00 ?  41   VAL   B HG23 1 
ATOM   4547 N  N    . TYR   B 1 42  ? 46.285 -17.115 10.877  1.00 12.52 ?  42   TYR   B N    1 
ATOM   4548 C  CA   . TYR   B 1 42  ? 47.439 -16.265 11.149  1.00 13.06 ?  42   TYR   B CA   1 
ATOM   4549 C  C    . TYR   B 1 42  ? 48.401 -16.185 9.969   1.00 12.21 ?  42   TYR   B C    1 
ATOM   4550 O  O    . TYR   B 1 42  ? 49.493 -15.621 10.105  1.00 13.00 ?  42   TYR   B O    1 
ATOM   4551 C  CB   . TYR   B 1 42  ? 48.141 -16.674 12.451  1.00 14.78 ?  42   TYR   B CB   1 
ATOM   4552 C  CG   . TYR   B 1 42  ? 47.531 -16.000 13.678  1.00 14.91 ?  42   TYR   B CG   1 
ATOM   4553 C  CD1  . TYR   B 1 42  ? 47.744 -14.645 13.919  1.00 13.98 ?  42   TYR   B CD1  1 
ATOM   4554 C  CD2  . TYR   B 1 42  ? 46.741 -16.702 14.573  1.00 16.92 ?  42   TYR   B CD2  1 
ATOM   4555 C  CE1  . TYR   B 1 42  ? 47.195 -14.013 15.020  1.00 15.16 ?  42   TYR   B CE1  1 
ATOM   4556 C  CE2  . TYR   B 1 42  ? 46.187 -16.075 15.681  1.00 17.07 ?  42   TYR   B CE2  1 
ATOM   4557 C  CZ   . TYR   B 1 42  ? 46.415 -14.727 15.897  1.00 16.86 ?  42   TYR   B CZ   1 
ATOM   4558 O  OH   . TYR   B 1 42  ? 45.880 -14.091 16.997  1.00 19.39 ?  42   TYR   B OH   1 
ATOM   4559 H  H    . TYR   B 1 42  ? 46.436 -17.960 10.975  1.00 15.05 ?  42   TYR   B H    1 
ATOM   4560 H  HA   . TYR   B 1 42  ? 47.111 -15.367 11.288  1.00 15.70 ?  42   TYR   B HA   1 
ATOM   4561 H  HB2  . TYR   B 1 42  ? 48.065 -17.633 12.567  1.00 17.76 ?  42   TYR   B HB2  1 
ATOM   4562 H  HB3  . TYR   B 1 42  ? 49.076 -16.418 12.399  1.00 17.76 ?  42   TYR   B HB3  1 
ATOM   4563 H  HD1  . TYR   B 1 42  ? 48.275 -14.154 13.326  1.00 16.81 ?  42   TYR   B HD1  1 
ATOM   4564 H  HD2  . TYR   B 1 42  ? 46.582 -17.608 14.427  1.00 20.33 ?  42   TYR   B HD2  1 
ATOM   4565 H  HE1  . TYR   B 1 42  ? 47.354 -13.107 15.164  1.00 18.22 ?  42   TYR   B HE1  1 
ATOM   4566 H  HE2  . TYR   B 1 42  ? 45.658 -16.561 16.271  1.00 20.51 ?  42   TYR   B HE2  1 
ATOM   4567 H  HH   . TYR   B 1 42  ? 46.101 -13.283 16.992  1.00 23.30 ?  42   TYR   B HH   1 
ATOM   4568 N  N    . LEU   B 1 43  ? 48.001 -16.698 8.807   1.00 11.16 ?  43   LEU   B N    1 
ATOM   4569 C  CA   . LEU   B 1 43  ? 48.813 -16.626 7.598   1.00 10.80 ?  43   LEU   B CA   1 
ATOM   4570 C  C    . LEU   B 1 43  ? 50.228 -17.131 7.857   1.00 11.44 ?  43   LEU   B C    1 
ATOM   4571 O  O    . LEU   B 1 43  ? 51.209 -16.535 7.412   1.00 11.81 ?  43   LEU   B O    1 
ATOM   4572 C  CB   . LEU   B 1 43  ? 48.829 -15.220 6.999   1.00 11.13 ?  43   LEU   B CB   1 
ATOM   4573 C  CG   . LEU   B 1 43  ? 47.471 -14.608 6.628   1.00 11.21 ?  43   LEU   B CG   1 
ATOM   4574 C  CD1  . LEU   B 1 43  ? 47.680 -13.214 6.046   1.00 12.60 ?  43   LEU   B CD1  1 
ATOM   4575 C  CD2  . LEU   B 1 43  ? 46.703 -15.498 5.653   1.00 11.47 ?  43   LEU   B CD2  1 
ATOM   4576 H  H    . LEU   B 1 43  ? 47.257 -17.111 8.691   1.00 13.42 ?  43   LEU   B H    1 
ATOM   4577 H  HA   . LEU   B 1 43  ? 48.418 -17.211 6.929   1.00 12.98 ?  43   LEU   B HA   1 
ATOM   4578 H  HB2  . LEU   B 1 43  ? 49.247 -14.622 7.641   1.00 13.39 ?  43   LEU   B HB2  1 
ATOM   4579 H  HB3  . LEU   B 1 43  ? 49.364 -15.241 6.190   1.00 13.39 ?  43   LEU   B HB3  1 
ATOM   4580 H  HG   . LEU   B 1 43  ? 46.938 -14.519 7.430   1.00 13.48 ?  43   LEU   B HG   1 
ATOM   4581 H  HD11 . LEU   B 1 43  ? 46.817 -12.835 5.813   1.00 15.15 ?  43   LEU   B HD11 1 
ATOM   4582 H  HD12 . LEU   B 1 43  ? 48.115 -12.655 6.712   1.00 15.15 ?  43   LEU   B HD12 1 
ATOM   4583 H  HD13 . LEU   B 1 43  ? 48.237 -13.277 5.255   1.00 15.15 ?  43   LEU   B HD13 1 
ATOM   4584 H  HD21 . LEU   B 1 43  ? 45.899 -15.037 5.365   1.00 13.79 ?  43   LEU   B HD21 1 
ATOM   4585 H  HD22 . LEU   B 1 43  ? 47.264 -15.692 4.885   1.00 13.79 ?  43   LEU   B HD22 1 
ATOM   4586 H  HD23 . LEU   B 1 43  ? 46.463 -16.328 6.100   1.00 13.79 ?  43   LEU   B HD23 1 
ATOM   4587 N  N    . LYS   B 1 44  ? 50.330 -18.260 8.563   1.00 11.30 ?  44   LYS   B N    1 
ATOM   4588 C  CA   . LYS   B 1 44  ? 51.600 -18.936 8.797   1.00 11.91 ?  44   LYS   B CA   1 
ATOM   4589 C  C    . LYS   B 1 44  ? 51.718 -20.050 7.766   1.00 11.29 ?  44   LYS   B C    1 
ATOM   4590 O  O    . LYS   B 1 44  ? 51.023 -21.066 7.852   1.00 12.70 ?  44   LYS   B O    1 
ATOM   4591 C  CB   . LYS   B 1 44  ? 51.667 -19.453 10.232  1.00 13.59 ?  44   LYS   B CB   1 
ATOM   4592 C  CG   . LYS   B 1 44  ? 51.822 -18.345 11.262  1.00 16.23 ?  44   LYS   B CG   1 
ATOM   4593 C  CD   . LYS   B 1 44  ? 53.028 -17.477 10.906  1.00 19.13 ?  44   LYS   B CD   1 
ATOM   4594 C  CE   . LYS   B 1 44  ? 53.459 -16.566 12.026  1.00 21.69 ?  44   LYS   B CE   1 
ATOM   4595 N  NZ   . LYS   B 1 44  ? 54.662 -15.775 11.665  1.00 23.09 ?  44   LYS   B NZ   1 
ATOM   4596 H  H    . LYS   B 1 44  ? 49.657 -18.651 8.929   1.00 13.59 ?  44   LYS   B H    1 
ATOM   4597 H  HA   . LYS   B 1 44  ? 52.327 -18.316 8.637   1.00 14.32 ?  44   LYS   B HA   1 
ATOM   4598 H  HB2  . LYS   B 1 44  ? 50.843 -19.929 10.431  1.00 16.34 ?  44   LYS   B HB2  1 
ATOM   4599 H  HB3  . LYS   B 1 44  ? 52.423 -20.048 10.316  1.00 16.34 ?  44   LYS   B HB3  1 
ATOM   4600 H  HG2  . LYS   B 1 44  ? 51.028 -17.790 11.268  1.00 19.51 ?  44   LYS   B HG2  1 
ATOM   4601 H  HG3  . LYS   B 1 44  ? 51.972 -18.739 12.138  1.00 19.51 ?  44   LYS   B HG3  1 
ATOM   4602 H  HD2  . LYS   B 1 44  ? 53.772 -18.062 10.670  1.00 22.99 ?  44   LYS   B HD2  1 
ATOM   4603 H  HD3  . LYS   B 1 44  ? 52.796 -16.920 10.146  1.00 22.99 ?  44   LYS   B HD3  1 
ATOM   4604 H  HE2  . LYS   B 1 44  ? 52.742 -15.945 12.204  1.00 26.06 ?  44   LYS   B HE2  1 
ATOM   4605 H  HE3  . LYS   B 1 44  ? 53.660 -17.097 12.811  1.00 26.06 ?  44   LYS   B HE3  1 
ATOM   4606 H  HZ1  . LYS   B 1 44  ? 54.890 -15.246 12.342  1.00 27.73 ?  44   LYS   B HZ1  1 
ATOM   4607 H  HZ2  . LYS   B 1 44  ? 55.341 -16.317 11.477  1.00 27.73 ?  44   LYS   B HZ2  1 
ATOM   4608 H  HZ3  . LYS   B 1 44  ? 54.490 -15.270 10.950  1.00 27.73 ?  44   LYS   B HZ3  1 
ATOM   4609 N  N    . HIS   B 1 45  ? 52.564 -19.826 6.763   1.00 11.13 ?  45   HIS   B N    1 
ATOM   4610 C  CA   . HIS   B 1 45  ? 52.576 -20.657 5.560   1.00 11.29 ?  45   HIS   B CA   1 
ATOM   4611 C  C    . HIS   B 1 45  ? 53.598 -21.778 5.713   1.00 13.34 ?  45   HIS   B C    1 
ATOM   4612 O  O    . HIS   B 1 45  ? 54.658 -21.788 5.095   1.00 15.62 ?  45   HIS   B O    1 
ATOM   4613 C  CB   . HIS   B 1 45  ? 52.889 -19.801 4.347   1.00 11.16 ?  45   HIS   B CB   1 
ATOM   4614 C  CG   . HIS   B 1 45  ? 52.016 -18.600 4.241   1.00 11.02 ?  45   HIS   B CG   1 
ATOM   4615 N  ND1  . HIS   B 1 45  ? 50.638 -18.678 4.220   1.00 11.07 ?  45   HIS   B ND1  1 
ATOM   4616 C  CD2  . HIS   B 1 45  ? 52.333 -17.287 4.162   1.00 11.64 ?  45   HIS   B CD2  1 
ATOM   4617 C  CE1  . HIS   B 1 45  ? 50.151 -17.454 4.117   1.00 10.68 ?  45   HIS   B CE1  1 
ATOM   4618 N  NE2  . HIS   B 1 45  ? 51.155 -16.593 4.081   1.00 11.22 ?  45   HIS   B NE2  1 
ATOM   4619 H  H    . HIS   B 1 45  ? 53.139 -19.186 6.749   1.00 13.38 ?  45   HIS   B H    1 
ATOM   4620 H  HA   . HIS   B 1 45  ? 51.696 -21.051 5.433   1.00 13.57 ?  45   HIS   B HA   1 
ATOM   4621 H  HB2  . HIS   B 1 45  ? 53.808 -19.502 4.398   1.00 13.42 ?  45   HIS   B HB2  1 
ATOM   4622 H  HB3  . HIS   B 1 45  ? 52.761 -20.336 3.542   1.00 13.42 ?  45   HIS   B HB3  1 
ATOM   4623 H  HD2  . HIS   B 1 45  ? 53.188 -16.920 4.157   1.00 14.00 ?  45   HIS   B HD2  1 
ATOM   4624 H  HE1  . HIS   B 1 45  ? 49.247 -17.236 4.070   1.00 12.84 ?  45   HIS   B HE1  1 
ATOM   4625 H  HE2  . HIS   B 1 45  ? 51.074 -15.736 4.021   1.00 13.49 ?  45   HIS   B HE2  1 
ATOM   4626 N  N    A GLY   B 1 46  ? 53.240 -22.753 6.542   0.60 14.17 ?  46   GLY   B N    1 
ATOM   4627 N  N    B GLY   B 1 46  ? 53.250 -22.740 6.559   0.40 14.19 ?  46   GLY   B N    1 
ATOM   4628 C  CA   A GLY   B 1 46  ? 54.169 -23.808 6.905   0.60 15.74 ?  46   GLY   B CA   1 
ATOM   4629 C  CA   B GLY   B 1 46  ? 54.173 -23.806 6.888   0.40 15.41 ?  46   GLY   B CA   1 
ATOM   4630 C  C    A GLY   B 1 46  ? 54.204 -25.025 6.004   0.60 17.25 ?  46   GLY   B C    1 
ATOM   4631 C  C    B GLY   B 1 46  ? 54.189 -24.959 5.906   0.40 16.64 ?  46   GLY   B C    1 
ATOM   4632 O  O    A GLY   B 1 46  ? 55.279 -25.458 5.575   0.60 19.71 ?  46   GLY   B O    1 
ATOM   4633 O  O    B GLY   B 1 46  ? 55.222 -25.255 5.296   0.40 17.78 ?  46   GLY   B O    1 
ATOM   4634 H  H    A GLY   B 1 46  ? 52.469 -22.808 6.928   0.60 17.03 ?  46   GLY   B H    1 
ATOM   4635 H  H    B GLY   B 1 46  ? 52.490 -22.785 6.966   0.40 17.06 ?  46   GLY   B H    1 
ATOM   4636 H  HA2  A GLY   B 1 46  ? 55.062 -23.431 6.936   0.60 18.92 ?  46   GLY   B HA2  1 
ATOM   4637 H  HA2  B GLY   B 1 46  ? 55.069 -23.438 6.936   0.40 18.52 ?  46   GLY   B HA2  1 
ATOM   4638 H  HA3  A GLY   B 1 46  ? 53.948 -24.120 7.795   0.60 18.92 ?  46   GLY   B HA3  1 
ATOM   4639 H  HA3  B GLY   B 1 46  ? 53.947 -24.155 7.766   0.40 18.52 ?  46   GLY   B HA3  1 
ATOM   4640 N  N    . GLY   B 1 47  ? 53.043 -25.613 5.729   1.00 16.90 ?  47   GLY   B N    1 
ATOM   4641 C  CA   . GLY   B 1 47  ? 52.978 -26.883 5.037   1.00 14.63 ?  47   GLY   B CA   1 
ATOM   4642 C  C    . GLY   B 1 47  ? 52.066 -26.861 3.826   1.00 12.62 ?  47   GLY   B C    1 
ATOM   4643 O  O    . GLY   B 1 47  ? 51.416 -25.861 3.530   1.00 12.88 ?  47   GLY   B O    1 
ATOM   4644 H  H    A GLY   B 1 47  ? 52.275 -25.301 5.961   0.60 20.31 ?  47   GLY   B H    1 
ATOM   4645 H  H    B GLY   B 1 47  ? 52.280 -25.331 6.011   0.40 20.31 ?  47   GLY   B H    1 
ATOM   4646 H  HA2  . GLY   B 1 47  ? 53.865 -27.143 4.746   1.00 17.58 ?  47   GLY   B HA2  1 
ATOM   4647 H  HA3  . GLY   B 1 47  ? 52.654 -27.561 5.654   1.00 17.58 ?  47   GLY   B HA3  1 
ATOM   4648 N  N    . GLY   B 1 48  ? 52.026 -27.999 3.136   1.00 11.92 ?  48   GLY   B N    1 
ATOM   4649 C  CA   . GLY   B 1 48  ? 51.095 -28.141 2.034   1.00 11.68 ?  48   GLY   B CA   1 
ATOM   4650 C  C    . GLY   B 1 48  ? 51.233 -27.032 1.016   1.00 11.34 ?  48   GLY   B C    1 
ATOM   4651 O  O    . GLY   B 1 48  ? 52.337 -26.573 0.702   1.00 11.69 ?  48   GLY   B O    1 
ATOM   4652 H  H    . GLY   B 1 48  ? 52.528 -28.680 3.280   1.00 14.33 ?  48   GLY   B H    1 
ATOM   4653 H  HA2  . GLY   B 1 48  ? 51.248 -28.989 1.592   1.00 14.05 ?  48   GLY   B HA2  1 
ATOM   4654 H  HA3  . GLY   B 1 48  ? 50.188 -28.131 2.379   1.00 14.05 ?  48   GLY   B HA3  1 
ATOM   4655 N  N    . VAL   B 1 49  ? 50.085 -26.598 0.486   1.00 11.03 ?  49   VAL   B N    1 
ATOM   4656 C  CA   . VAL   B 1 49  ? 50.064 -25.570 -0.553  1.00 11.24 ?  49   VAL   B CA   1 
ATOM   4657 C  C    . VAL   B 1 49  ? 50.727 -24.285 -0.065  1.00 10.34 ?  49   VAL   B C    1 
ATOM   4658 O  O    . VAL   B 1 49  ? 51.515 -23.665 -0.790  1.00 10.92 ?  49   VAL   B O    1 
ATOM   4659 C  CB   . VAL   B 1 49  ? 48.620 -25.318 -1.028  1.00 12.43 ?  49   VAL   B CB   1 
ATOM   4660 C  CG1  . VAL   B 1 49  ? 48.546 -24.067 -1.895  1.00 12.35 ?  49   VAL   B CG1  1 
ATOM   4661 C  CG2  . VAL   B 1 49  ? 48.068 -26.530 -1.777  1.00 13.60 ?  49   VAL   B CG2  1 
ATOM   4662 H  H    . VAL   B 1 49  ? 49.301 -26.884 0.713   1.00 13.26 ?  49   VAL   B H    1 
ATOM   4663 H  HA   . VAL   B 1 49  ? 50.565 -25.893 -1.316  1.00 13.51 ?  49   VAL   B HA   1 
ATOM   4664 H  HB   . VAL   B 1 49  ? 48.053 -25.173 -0.255  1.00 14.94 ?  49   VAL   B HB   1 
ATOM   4665 H  HG11 . VAL   B 1 49  ? 47.719 -24.075 -2.401  1.00 14.84 ?  49   VAL   B HG11 1 
ATOM   4666 H  HG12 . VAL   B 1 49  ? 48.571 -23.280 -1.324  1.00 14.84 ?  49   VAL   B HG12 1 
ATOM   4667 H  HG13 . VAL   B 1 49  ? 49.303 -24.056 -2.504  1.00 14.84 ?  49   VAL   B HG13 1 
ATOM   4668 H  HG21 . VAL   B 1 49  ? 47.160 -26.341 -2.062  1.00 16.35 ?  49   VAL   B HG21 1 
ATOM   4669 H  HG22 . VAL   B 1 49  ? 48.628 -26.701 -2.553  1.00 16.35 ?  49   VAL   B HG22 1 
ATOM   4670 H  HG23 . VAL   B 1 49  ? 48.079 -27.297 -1.186  1.00 16.35 ?  49   VAL   B HG23 1 
ATOM   4671 N  N    . ALA   B 1 50  ? 50.391 -23.845 1.151   1.00 10.15 ?  50   ALA   B N    1 
ATOM   4672 C  CA   . ALA   B 1 50  ? 50.908 -22.568 1.630   1.00 10.03 ?  50   ALA   B CA   1 
ATOM   4673 C  C    . ALA   B 1 50  ? 52.428 -22.598 1.731   1.00 10.32 ?  50   ALA   B C    1 
ATOM   4674 O  O    . ALA   B 1 50  ? 53.105 -21.630 1.362   1.00 10.39 ?  50   ALA   B O    1 
ATOM   4675 C  CB   . ALA   B 1 50  ? 50.278 -22.206 2.972   1.00 10.41 ?  50   ALA   B CB   1 
ATOM   4676 H  H    . ALA   B 1 50  ? 49.881 -24.261 1.706   1.00 12.20 ?  50   ALA   B H    1 
ATOM   4677 H  HA   . ALA   B 1 50  ? 50.678 -21.879 0.996   1.00 12.07 ?  50   ALA   B HA   1 
ATOM   4678 H  HB1  . ALA   B 1 50  ? 50.634 -21.354 3.270   1.00 12.52 ?  50   ALA   B HB1  1 
ATOM   4679 H  HB2  . ALA   B 1 50  ? 49.315 -22.138 2.857   1.00 12.52 ?  50   ALA   B HB2  1 
ATOM   4680 H  HB3  . ALA   B 1 50  ? 50.484 -22.897 3.619   1.00 12.52 ?  50   ALA   B HB3  1 
ATOM   4681 N  N    . GLY   B 1 51  ? 52.984 -23.691 2.247   1.00 10.69 ?  51   GLY   B N    1 
ATOM   4682 C  CA   . GLY   B 1 51  ? 54.429 -23.791 2.316   1.00 11.42 ?  51   GLY   B CA   1 
ATOM   4683 C  C    . GLY   B 1 51  ? 55.071 -23.737 0.946   1.00 11.14 ?  51   GLY   B C    1 
ATOM   4684 O  O    . GLY   B 1 51  ? 56.108 -23.097 0.759   1.00 12.14 ?  51   GLY   B O    1 
ATOM   4685 H  H    . GLY   B 1 51  ? 52.562 -24.374 2.554   1.00 12.86 ?  51   GLY   B H    1 
ATOM   4686 H  HA2  . GLY   B 1 51  ? 54.783 -23.059 2.849   1.00 13.73 ?  51   GLY   B HA2  1 
ATOM   4687 H  HA3  . GLY   B 1 51  ? 54.682 -24.627 2.743   1.00 13.73 ?  51   GLY   B HA3  1 
ATOM   4688 N  N    . ALA   B 1 52  ? 54.465 -24.403 -0.033  1.00 11.08 ?  52   ALA   B N    1 
ATOM   4689 C  CA   . ALA   B 1 52  ? 55.025 -24.409 -1.377  1.00 11.33 ?  52   ALA   B CA   1 
ATOM   4690 C  C    . ALA   B 1 52  ? 54.936 -23.031 -2.027  1.00 10.60 ?  52   ALA   B C    1 
ATOM   4691 O  O    . ALA   B 1 52  ? 55.903 -22.572 -2.654  1.00 11.32 ?  52   ALA   B O    1 
ATOM   4692 C  CB   . ALA   B 1 52  ? 54.320 -25.459 -2.232  1.00 12.23 ?  52   ALA   B CB   1 
ATOM   4693 H  H    . ALA   B 1 52  ? 53.732 -24.846 0.056   1.00 13.32 ?  52   ALA   B H    1 
ATOM   4694 H  HA   . ALA   B 1 52  ? 55.961 -24.650 -1.320  1.00 13.63 ?  52   ALA   B HA   1 
ATOM   4695 H  HB1  . ALA   B 1 52  ? 54.710 -25.448 -3.121  1.00 14.71 ?  52   ALA   B HB1  1 
ATOM   4696 H  HB2  . ALA   B 1 52  ? 54.447 -26.330 -1.826  1.00 14.71 ?  52   ALA   B HB2  1 
ATOM   4697 H  HB3  . ALA   B 1 52  ? 53.378 -25.246 -2.280  1.00 14.71 ?  52   ALA   B HB3  1 
ATOM   4698 N  N    . LEU   B 1 53  ? 53.788 -22.360 -1.905  1.00 10.33 ?  53   LEU   B N    1 
ATOM   4699 C  CA   . LEU   B 1 53  ? 53.675 -21.020 -2.473  1.00 10.67 ?  53   LEU   B CA   1 
ATOM   4700 C  C    . LEU   B 1 53  ? 54.681 -20.075 -1.827  1.00 10.45 ?  53   LEU   B C    1 
ATOM   4701 O  O    . LEU   B 1 53  ? 55.378 -19.320 -2.514  1.00 11.16 ?  53   LEU   B O    1 
ATOM   4702 C  CB   . LEU   B 1 53  ? 52.249 -20.482 -2.312  1.00 11.12 ?  53   LEU   B CB   1 
ATOM   4703 C  CG   . LEU   B 1 53  ? 51.123 -21.211 -3.052  1.00 11.33 ?  53   LEU   B CG   1 
ATOM   4704 C  CD1  . LEU   B 1 53  ? 49.782 -20.598 -2.700  1.00 12.78 ?  53   LEU   B CD1  1 
ATOM   4705 C  CD2  . LEU   B 1 53  ? 51.330 -21.186 -4.558  1.00 13.22 ?  53   LEU   B CD2  1 
ATOM   4706 H  H    . LEU   B 1 53  ? 53.081 -22.651 -1.506  1.00 12.42 ?  53   LEU   B H    1 
ATOM   4707 H  HA   . LEU   B 1 53  ? 53.871 -21.066 -3.424  1.00 12.83 ?  53   LEU   B HA   1 
ATOM   4708 H  HB2  . LEU   B 1 53  ? 52.025 -20.502 -1.373  1.00 13.37 ?  53   LEU   B HB2  1 
ATOM   4709 H  HB3  . LEU   B 1 53  ? 52.238 -19.566 -2.627  1.00 13.37 ?  53   LEU   B HB3  1 
ATOM   4710 H  HG   . LEU   B 1 53  ? 51.101 -22.140 -2.769  1.00 13.63 ?  53   LEU   B HG   1 
ATOM   4711 H  HD11 . LEU   B 1 53  ? 49.078 -21.076 -3.172  1.00 15.37 ?  53   LEU   B HD11 1 
ATOM   4712 H  HD12 . LEU   B 1 53  ? 49.640 -20.678 -1.740  1.00 15.37 ?  53   LEU   B HD12 1 
ATOM   4713 H  HD13 . LEU   B 1 53  ? 49.779 -19.667 -2.957  1.00 15.37 ?  53   LEU   B HD13 1 
ATOM   4714 H  HD21 . LEU   B 1 53  ? 50.594 -21.646 -4.992  1.00 15.89 ?  53   LEU   B HD21 1 
ATOM   4715 H  HD22 . LEU   B 1 53  ? 51.364 -20.264 -4.858  1.00 15.89 ?  53   LEU   B HD22 1 
ATOM   4716 H  HD23 . LEU   B 1 53  ? 52.165 -21.633 -4.769  1.00 15.89 ?  53   LEU   B HD23 1 
ATOM   4717 N  N    . ASN   B 1 54  ? 54.780 -20.108 -0.500  1.00 10.22 ?  54   ASN   B N    1 
ATOM   4718 C  CA   . ASN   B 1 54  ? 55.695 -19.195 0.167   1.00 11.02 ?  54   ASN   B CA   1 
ATOM   4719 C  C    . ASN   B 1 54  ? 57.139 -19.467 -0.237  1.00 11.19 ?  54   ASN   B C    1 
ATOM   4720 O  O    . ASN   B 1 54  ? 57.912 -18.528 -0.468  1.00 11.77 ?  54   ASN   B O    1 
ATOM   4721 C  CB   . ASN   B 1 54  ? 55.536 -19.276 1.676   1.00 11.58 ?  54   ASN   B CB   1 
ATOM   4722 C  CG   . ASN   B 1 54  ? 56.512 -18.367 2.386   1.00 11.59 ?  54   ASN   B CG   1 
ATOM   4723 O  OD1  . ASN   B 1 54  ? 56.517 -17.156 2.160   1.00 11.67 ?  54   ASN   B OD1  1 
ATOM   4724 N  ND2  . ASN   B 1 54  ? 57.369 -18.944 3.220   1.00 13.36 ?  54   ASN   B ND2  1 
ATOM   4725 H  H    . ASN   B 1 54  ? 54.346 -20.637 0.020   1.00 12.30 ?  54   ASN   B H    1 
ATOM   4726 H  HA   . ASN   B 1 54  ? 55.479 -18.289 -0.106  1.00 13.25 ?  54   ASN   B HA   1 
ATOM   4727 H  HB2  . ASN   B 1 54  ? 54.634 -18.998 1.915   1.00 13.92 ?  54   ASN   B HB2  1 
ATOM   4728 H  HB3  . ASN   B 1 54  ? 55.695 -20.182 1.968   1.00 13.92 ?  54   ASN   B HB3  1 
ATOM   4729 H  HD21 . ASN   B 1 54  ? 57.950 -18.468 3.641   1.00 16.06 ?  54   ASN   B HD21 1 
ATOM   4730 H  HD22 . ASN   B 1 54  ? 57.346 -19.796 3.340   1.00 16.06 ?  54   ASN   B HD22 1 
ATOM   4731 N  N    . LYS   B 1 55  ? 57.528 -20.744 -0.302  1.00 11.88 ?  55   LYS   B N    1 
ATOM   4732 C  CA   . LYS   B 1 55  ? 58.880 -21.085 -0.733  1.00 12.62 ?  55   LYS   B CA   1 
ATOM   4733 C  C    . LYS   B 1 55  ? 59.171 -20.531 -2.123  1.00 12.44 ?  55   LYS   B C    1 
ATOM   4734 O  O    . LYS   B 1 55  ? 60.269 -20.025 -2.377  1.00 13.16 ?  55   LYS   B O    1 
ATOM   4735 C  CB   . LYS   B 1 55  ? 59.068 -22.603 -0.695  1.00 13.83 ?  55   LYS   B CB   1 
ATOM   4736 C  CG   . LYS   B 1 55  ? 60.455 -23.073 -1.088  1.00 18.13 ?  55   LYS   B CG   1 
ATOM   4737 C  CD   . LYS   B 1 55  ? 60.615 -24.575 -0.914  1.00 21.91 ?  55   LYS   B CD   1 
ATOM   4738 C  CE   . LYS   B 1 55  ? 60.597 -24.978 0.558   1.00 24.76 ?  55   LYS   B CE   1 
ATOM   4739 N  NZ   . LYS   B 1 55  ? 61.003 -26.390 0.752   1.00 26.24 ?  55   LYS   B NZ   1 
ATOM   4740 H  H    . LYS   B 1 55  ? 57.032 -21.417 -0.108  1.00 14.29 ?  55   LYS   B H    1 
ATOM   4741 H  HA   . LYS   B 1 55  ? 59.515 -20.688 -0.120  1.00 15.17 ?  55   LYS   B HA   1 
ATOM   4742 H  HB2  . LYS   B 1 55  ? 58.895 -22.907 0.207   1.00 16.62 ?  55   LYS   B HB2  1 
ATOM   4743 H  HB3  . LYS   B 1 55  ? 58.437 -23.010 -1.307  1.00 16.62 ?  55   LYS   B HB3  1 
ATOM   4744 H  HG2  . LYS   B 1 55  ? 60.615 -22.859 -2.021  1.00 21.79 ?  55   LYS   B HG2  1 
ATOM   4745 H  HG3  . LYS   B 1 55  ? 61.113 -22.631 -0.527  1.00 21.79 ?  55   LYS   B HG3  1 
ATOM   4746 H  HD2  . LYS   B 1 55  ? 59.883 -25.030 -1.360  1.00 26.32 ?  55   LYS   B HD2  1 
ATOM   4747 H  HD3  . LYS   B 1 55  ? 61.464 -24.855 -1.291  1.00 26.32 ?  55   LYS   B HD3  1 
ATOM   4748 H  HE2  . LYS   B 1 55  ? 61.214 -24.407 1.047   1.00 29.74 ?  55   LYS   B HE2  1 
ATOM   4749 H  HE3  . LYS   B 1 55  ? 59.696 -24.864 0.905   1.00 29.74 ?  55   LYS   B HE3  1 
ATOM   4750 H  HZ1  . LYS   B 1 55  ? 60.941 -26.604 1.613   1.00 31.51 ?  55   LYS   B HZ1  1 
ATOM   4751 H  HZ2  . LYS   B 1 55  ? 60.467 -26.922 0.281   1.00 31.51 ?  55   LYS   B HZ2  1 
ATOM   4752 H  HZ3  . LYS   B 1 55  ? 61.840 -26.503 0.481   1.00 31.51 ?  55   LYS   B HZ3  1 
ATOM   4753 N  N    . ALA   B 1 56  ? 58.200 -20.618 -3.037  1.00 11.87 ?  56   ALA   B N    1 
ATOM   4754 C  CA   . ALA   B 1 56  ? 58.415 -20.110 -4.387  1.00 12.61 ?  56   ALA   B CA   1 
ATOM   4755 C  C    . ALA   B 1 56  ? 58.691 -18.614 -4.380  1.00 12.39 ?  56   ALA   B C    1 
ATOM   4756 O  O    . ALA   B 1 56  ? 59.414 -18.110 -5.250  1.00 13.44 ?  56   ALA   B O    1 
ATOM   4757 C  CB   . ALA   B 1 56  ? 57.213 -20.430 -5.278  1.00 13.44 ?  56   ALA   B CB   1 
ATOM   4758 H  H    . ALA   B 1 56  ? 57.417 -20.951 -2.902  1.00 14.27 ?  56   ALA   B H    1 
ATOM   4759 H  HA   . ALA   B 1 56  ? 59.190 -20.544 -4.766  1.00 15.16 ?  56   ALA   B HA   1 
ATOM   4760 H  HB1  . ALA   B 1 56  ? 57.383 -20.088 -6.174  1.00 16.16 ?  56   ALA   B HB1  1 
ATOM   4761 H  HB2  . ALA   B 1 56  ? 57.097 -21.392 -5.313  1.00 16.16 ?  56   ALA   B HB2  1 
ATOM   4762 H  HB3  . ALA   B 1 56  ? 56.421 -20.012 -4.911  1.00 16.16 ?  56   ALA   B HB3  1 
ATOM   4763 N  N    . THR   B 1 57  ? 58.128 -17.886 -3.413  1.00 12.49 ?  57   THR   B N    1 
ATOM   4764 C  CA   . THR   B 1 57  ? 58.363 -16.451 -3.276  1.00 12.50 ?  57   THR   B CA   1 
ATOM   4765 C  C    . THR   B 1 57  ? 59.617 -16.123 -2.470  1.00 13.40 ?  57   THR   B C    1 
ATOM   4766 O  O    . THR   B 1 57  ? 59.850 -14.948 -2.162  1.00 13.76 ?  57   THR   B O    1 
ATOM   4767 C  CB   . THR   B 1 57  ? 57.162 -15.732 -2.628  1.00 12.04 ?  57   THR   B CB   1 
ATOM   4768 O  OG1  . THR   B 1 57  ? 57.150 -15.939 -1.206  1.00 12.13 ?  57   THR   B OG1  1 
ATOM   4769 C  CG2  . THR   B 1 57  ? 55.836 -16.146 -3.259  1.00 11.91 ?  57   THR   B CG2  1 
ATOM   4770 H  H    . THR   B 1 57  ? 57.585 -18.203 -2.823  1.00 15.01 ?  57   THR   B H    1 
ATOM   4771 H  HA   . THR   B 1 57  ? 58.477 -16.073 -4.163  1.00 15.03 ?  57   THR   B HA   1 
ATOM   4772 H  HB   . THR   B 1 57  ? 57.263 -14.780 -2.791  1.00 14.48 ?  57   THR   B HB   1 
ATOM   4773 H  HG1  . THR   B 1 57  ? 57.091 -16.759 -1.038  1.00 14.58 ?  57   THR   B HG1  1 
ATOM   4774 H  HG21 . THR   B 1 57  ? 55.108 -15.631 -2.875  1.00 14.31 ?  57   THR   B HG21 1 
ATOM   4775 H  HG22 . THR   B 1 57  ? 55.858 -15.992 -4.217  1.00 14.31 ?  57   THR   B HG22 1 
ATOM   4776 H  HG23 . THR   B 1 57  ? 55.669 -17.088 -3.099  1.00 14.31 ?  57   THR   B HG23 1 
ATOM   4777 N  N    . ASN   B 1 58  ? 60.417 -17.125 -2.110  1.00 13.67 ?  58   ASN   B N    1 
ATOM   4778 C  CA   . ASN   B 1 58  ? 61.616 -16.904 -1.310  1.00 16.33 ?  58   ASN   B CA   1 
ATOM   4779 C  C    . ASN   B 1 58  ? 61.277 -16.202 0.004   1.00 14.56 ?  58   ASN   B C    1 
ATOM   4780 O  O    . ASN   B 1 58  ? 62.016 -15.335 0.478   1.00 15.04 ?  58   ASN   B O    1 
ATOM   4781 C  CB   . ASN   B 1 58  ? 62.684 -16.137 -2.096  1.00 23.58 ?  58   ASN   B CB   1 
ATOM   4782 C  CG   . ASN   B 1 58  ? 64.057 -16.232 -1.462  1.00 31.67 ?  58   ASN   B CG   1 
ATOM   4783 O  OD1  . ASN   B 1 58  ? 64.365 -17.200 -0.766  1.00 34.30 ?  58   ASN   B OD1  1 
ATOM   4784 N  ND2  . ASN   B 1 58  ? 64.890 -15.225 -1.697  1.00 35.94 ?  58   ASN   B ND2  1 
ATOM   4785 H  H    . ASN   B 1 58  ? 60.275 -17.954 -2.309  1.00 16.43 ?  58   ASN   B H    1 
ATOM   4786 H  HA   . ASN   B 1 58  ? 61.990 -17.771 -1.088  1.00 19.62 ?  58   ASN   B HA   1 
ATOM   4787 H  HB2  . ASN   B 1 58  ? 62.740 -16.504 -2.995  1.00 28.33 ?  58   ASN   B HB2  1 
ATOM   4788 H  HB3  . ASN   B 1 58  ? 62.437 -15.201 -2.137  1.00 28.33 ?  58   ASN   B HB3  1 
ATOM   4789 H  HD21 . ASN   B 1 58  ? 65.681 -15.233 -1.360  1.00 43.16 ?  58   ASN   B HD21 1 
ATOM   4790 H  HD22 . ASN   B 1 58  ? 64.638 -14.564 -2.186  1.00 43.16 ?  58   ASN   B HD22 1 
ATOM   4791 N  N    . ASN   B 1 59  ? 60.145 -16.578 0.598   1.00 13.49 ?  59   ASN   B N    1 
ATOM   4792 C  CA   . ASN   B 1 59  ? 59.676 -16.119 1.904   1.00 13.35 ?  59   ASN   B CA   1 
ATOM   4793 C  C    . ASN   B 1 59  ? 59.083 -14.714 1.856   1.00 12.63 ?  59   ASN   B C    1 
ATOM   4794 O  O    . ASN   B 1 59  ? 58.650 -14.213 2.903   1.00 12.94 ?  59   ASN   B O    1 
ATOM   4795 C  CB   . ASN   B 1 59  ? 60.751 -16.183 3.003   1.00 14.74 ?  59   ASN   B CB   1 
ATOM   4796 C  CG   . ASN   B 1 59  ? 60.167 -16.370 4.382   1.00 15.91 ?  59   ASN   B CG   1 
ATOM   4797 O  OD1  . ASN   B 1 59  ? 59.343 -17.261 4.605   1.00 16.16 ?  59   ASN   B OD1  1 
ATOM   4798 N  ND2  . ASN   B 1 59  ? 60.586 -15.528 5.321   1.00 16.95 ?  59   ASN   B ND2  1 
ATOM   4799 H  H    . ASN   B 1 59  ? 59.599 -17.142 0.244   1.00 16.22 ?  59   ASN   B H    1 
ATOM   4800 H  HA   . ASN   B 1 59  ? 58.965 -16.715 2.186   1.00 16.05 ?  59   ASN   B HA   1 
ATOM   4801 H  HB2  . ASN   B 1 59  ? 61.340 -16.932 2.836   1.00 17.71 ?  59   ASN   B HB2  1 
ATOM   4802 H  HB3  . ASN   B 1 59  ? 61.254 -15.355 3.010   1.00 17.71 ?  59   ASN   B HB3  1 
ATOM   4803 H  HD21 . ASN   B 1 59  ? 60.280 -15.588 6.124   1.00 20.37 ?  59   ASN   B HD21 1 
ATOM   4804 H  HD22 . ASN   B 1 59  ? 61.159 -14.916 5.126   1.00 20.37 ?  59   ASN   B HD22 1 
ATOM   4805 N  N    . ALA   B 1 60  ? 59.020 -14.067 0.689   1.00 12.65 ?  60   ALA   B N    1 
ATOM   4806 C  CA   . ALA   B 1 60  ? 58.422 -12.737 0.625   1.00 12.77 ?  60   ALA   B CA   1 
ATOM   4807 C  C    . ALA   B 1 60  ? 56.954 -12.767 1.027   1.00 11.77 ?  60   ALA   B C    1 
ATOM   4808 O  O    . ALA   B 1 60  ? 56.448 -11.815 1.639   1.00 12.39 ?  60   ALA   B O    1 
ATOM   4809 C  CB   . ALA   B 1 60  ? 58.585 -12.149 -0.776  1.00 13.44 ?  60   ALA   B CB   1 
ATOM   4810 H  H    . ALA   B 1 60  ? 59.307 -14.373 -0.058  1.00 15.21 ?  60   ALA   B H    1 
ATOM   4811 H  HA   . ALA   B 1 60  ? 58.882 -12.157 1.251   1.00 15.35 ?  60   ALA   B HA   1 
ATOM   4812 H  HB1  . ALA   B 1 60  ? 58.187 -11.265 -0.795  1.00 16.15 ?  60   ALA   B HB1  1 
ATOM   4813 H  HB2  . ALA   B 1 60  ? 59.535 -12.086 -0.980  1.00 16.15 ?  60   ALA   B HB2  1 
ATOM   4814 H  HB3  . ALA   B 1 60  ? 58.148 -12.728 -1.416  1.00 16.15 ?  60   ALA   B HB3  1 
ATOM   4815 N  N    . MET   B 1 61  ? 56.249 -13.845 0.678   1.00 11.44 ?  61   MET   B N    1 
ATOM   4816 C  CA   . MET   B 1 61  ? 54.855 -13.967 1.074   1.00 10.99 ?  61   MET   B CA   1 
ATOM   4817 C  C    . MET   B 1 61  ? 54.724 -13.983 2.596   1.00 11.33 ?  61   MET   B C    1 
ATOM   4818 O  O    . MET   B 1 61  ? 53.824 -13.342 3.153   1.00 11.18 ?  61   MET   B O    1 
ATOM   4819 C  CB   . MET   B 1 61  ? 54.272 -15.232 0.439   1.00 10.82 ?  61   MET   B CB   1 
ATOM   4820 C  CG   . MET   B 1 61  ? 52.833 -15.530 0.857   1.00 10.66 ?  61   MET   B CG   1 
ATOM   4821 S  SD   . MET   B 1 61  ? 52.186 -17.038 0.096   1.00 11.28 ?  61   MET   B SD   1 
ATOM   4822 C  CE   . MET   B 1 61  ? 51.916 -16.457 -1.571  1.00 12.56 ?  61   MET   B CE   1 
ATOM   4823 H  H    . MET   B 1 61  ? 56.552 -14.509 0.218   1.00 13.76 ?  61   MET   B H    1 
ATOM   4824 H  HA   . MET   B 1 61  ? 54.361 -13.209 0.720   1.00 13.21 ?  61   MET   B HA   1 
ATOM   4825 H  HB2  . MET   B 1 61  ? 54.279 -15.129 -0.530  1.00 13.01 ?  61   MET   B HB2  1 
ATOM   4826 H  HB3  . MET   B 1 61  ? 54.818 -15.990 0.689   1.00 13.01 ?  61   MET   B HB3  1 
ATOM   4827 H  HG2  . MET   B 1 61  ? 52.799 -15.650 1.820   1.00 12.82 ?  61   MET   B HG2  1 
ATOM   4828 H  HG3  . MET   B 1 61  ? 52.263 -14.791 0.594   1.00 12.82 ?  61   MET   B HG3  1 
ATOM   4829 H  HE1  . MET   B 1 61  ? 51.537 -17.177 -2.097  1.00 15.10 ?  61   MET   B HE1  1 
ATOM   4830 H  HE2  . MET   B 1 61  ? 51.306 -15.703 -1.550  1.00 15.10 ?  61   MET   B HE2  1 
ATOM   4831 H  HE3  . MET   B 1 61  ? 52.767 -16.182 -1.950  1.00 15.10 ?  61   MET   B HE3  1 
ATOM   4832 N  N    . GLN   B 1 62  ? 55.609 -14.702 3.291   1.00 11.15 ?  62   GLN   B N    1 
ATOM   4833 C  CA   . GLN   B 1 62  ? 55.501 -14.765 4.745   1.00 11.72 ?  62   GLN   B CA   1 
ATOM   4834 C  C    . GLN   B 1 62  ? 55.788 -13.412 5.386   1.00 11.76 ?  62   GLN   B C    1 
ATOM   4835 O  O    . GLN   B 1 62  ? 55.108 -13.019 6.339   1.00 12.17 ?  62   GLN   B O    1 
ATOM   4836 C  CB   . GLN   B 1 62  ? 56.454 -15.818 5.303   1.00 11.76 ?  62   GLN   B CB   1 
ATOM   4837 C  CG   . GLN   B 1 62  ? 56.242 -16.095 6.781   1.00 12.27 ?  62   GLN   B CG   1 
ATOM   4838 C  CD   . GLN   B 1 62  ? 54.869 -16.685 7.034   1.00 11.53 ?  62   GLN   B CD   1 
ATOM   4839 O  OE1  . GLN   B 1 62  ? 54.612 -17.835 6.676   1.00 12.06 ?  62   GLN   B OE1  1 
ATOM   4840 N  NE2  . GLN   B 1 62  ? 53.963 -15.894 7.602   1.00 12.10 ?  62   GLN   B NE2  1 
ATOM   4841 H  H    . GLN   B 1 62  ? 56.259 -15.149 2.947   1.00 13.41 ?  62   GLN   B H    1 
ATOM   4842 H  HA   . GLN   B 1 62  ? 54.595 -15.021 4.976   1.00 14.09 ?  62   GLN   B HA   1 
ATOM   4843 H  HB2  . GLN   B 1 62  ? 56.328 -16.647 4.817   1.00 14.14 ?  62   GLN   B HB2  1 
ATOM   4844 H  HB3  . GLN   B 1 62  ? 57.368 -15.505 5.184   1.00 14.14 ?  62   GLN   B HB3  1 
ATOM   4845 H  HG2  . GLN   B 1 62  ? 56.909 -16.736 7.078   1.00 14.75 ?  62   GLN   B HG2  1 
ATOM   4846 H  HG3  . GLN   B 1 62  ? 56.320 -15.271 7.278   1.00 14.75 ?  62   GLN   B HG3  1 
ATOM   4847 H  HE21 . GLN   B 1 62  ? 54.176 -15.094 7.828   1.00 14.55 ?  62   GLN   B HE21 1 
ATOM   4848 H  HE22 . GLN   B 1 62  ? 53.173 -16.193 7.757   1.00 14.55 ?  62   GLN   B HE22 1 
ATOM   4849 N  N    . VAL   B 1 63  ? 56.796 -12.691 4.892   1.00 12.20 ?  63   VAL   B N    1 
ATOM   4850 C  CA   . VAL   B 1 63  ? 57.105 -11.378 5.454   1.00 13.12 ?  63   VAL   B CA   1 
ATOM   4851 C  C    . VAL   B 1 63  ? 55.914 -10.444 5.278   1.00 12.41 ?  63   VAL   B C    1 
ATOM   4852 O  O    . VAL   B 1 63  ? 55.502 -9.743  6.213   1.00 13.25 ?  63   VAL   B O    1 
ATOM   4853 C  CB   . VAL   B 1 63  ? 58.394 -10.814 4.830   1.00 14.60 ?  63   VAL   B CB   1 
ATOM   4854 C  CG1  . VAL   B 1 63  ? 58.620 -9.380  5.287   1.00 15.51 ?  63   VAL   B CG1  1 
ATOM   4855 C  CG2  . VAL   B 1 63  ? 59.579 -11.689 5.212   1.00 15.23 ?  63   VAL   B CG2  1 
ATOM   4856 H  H    . VAL   B 1 63  ? 57.300 -12.932 4.236   1.00 14.66 ?  63   VAL   B H    1 
ATOM   4857 H  HA   . VAL   B 1 63  ? 57.261 -11.483 6.403   1.00 15.77 ?  63   VAL   B HA   1 
ATOM   4858 H  HB   . VAL   B 1 63  ? 58.318 -10.820 3.864   1.00 17.55 ?  63   VAL   B HB   1 
ATOM   4859 H  HG11 . VAL   B 1 63  ? 59.537 -9.129  5.102   1.00 18.63 ?  63   VAL   B HG11 1 
ATOM   4860 H  HG12 . VAL   B 1 63  ? 58.012 -8.796  4.810   1.00 18.63 ?  63   VAL   B HG12 1 
ATOM   4861 H  HG13 . VAL   B 1 63  ? 58.451 -9.325  6.244   1.00 18.63 ?  63   VAL   B HG13 1 
ATOM   4862 H  HG21 . VAL   B 1 63  ? 60.390 -11.312 4.831   1.00 18.31 ?  63   VAL   B HG21 1 
ATOM   4863 H  HG22 . VAL   B 1 63  ? 59.657 -11.713 6.182   1.00 18.31 ?  63   VAL   B HG22 1 
ATOM   4864 H  HG23 . VAL   B 1 63  ? 59.440 -12.585 4.872   1.00 18.31 ?  63   VAL   B HG23 1 
ATOM   4865 N  N    . GLU   B 1 64  ? 55.342 -10.428 4.072   1.00 12.12 ?  64   GLU   B N    1 
ATOM   4866 C  CA   . GLU   B 1 64  ? 54.169 -9.598  3.801   1.00 11.52 ?  64   GLU   B CA   1 
ATOM   4867 C  C    . GLU   B 1 64  ? 52.993 -10.000 4.686   1.00 11.13 ?  64   GLU   B C    1 
ATOM   4868 O  O    . GLU   B 1 64  ? 52.254 -9.141  5.197   1.00 11.96 ?  64   GLU   B O    1 
ATOM   4869 C  CB   . GLU   B 1 64  ? 53.803 -9.755  2.324   1.00 11.72 ?  64   GLU   B CB   1 
ATOM   4870 C  CG   . GLU   B 1 64  ? 52.547 -9.006  1.892   1.00 12.02 ?  64   GLU   B CG   1 
ATOM   4871 C  CD   . GLU   B 1 64  ? 51.991 -9.505  0.567   1.00 12.64 ?  64   GLU   B CD   1 
ATOM   4872 O  OE1  . GLU   B 1 64  ? 52.175 -10.709 0.246   1.00 13.53 ?  64   GLU   B OE1  1 
ATOM   4873 O  OE2  . GLU   B 1 64  ? 51.364 -8.688  -0.150  1.00 13.42 -1 64   GLU   B OE2  1 
ATOM   4874 H  H    . GLU   B 1 64  ? 55.620 -10.883 3.394   1.00 14.57 ?  64   GLU   B H    1 
ATOM   4875 H  HA   . GLU   B 1 64  ? 54.385 -8.667  3.968   1.00 13.85 ?  64   GLU   B HA   1 
ATOM   4876 H  HB2  . GLU   B 1 64  ? 54.538 -9.420  1.781   1.00 14.09 ?  64   GLU   B HB2  1 
ATOM   4877 H  HB3  . GLU   B 1 64  ? 53.663 -10.693 2.138   1.00 14.09 ?  64   GLU   B HB3  1 
ATOM   4878 H  HG2  . GLU   B 1 64  ? 51.854 -9.115  2.563   1.00 14.45 ?  64   GLU   B HG2  1 
ATOM   4879 H  HG3  . GLU   B 1 64  ? 52.761 -8.063  1.793   1.00 14.45 ?  64   GLU   B HG3  1 
ATOM   4880 N  N    . SER   B 1 65  ? 52.808 -11.309 4.868   1.00 11.19 ?  65   SER   B N    1 
ATOM   4881 C  CA   . SER   B 1 65  ? 51.703 -11.815 5.670   1.00 11.17 ?  65   SER   B CA   1 
ATOM   4882 C  C    . SER   B 1 65  ? 51.843 -11.420 7.135   1.00 11.24 ?  65   SER   B C    1 
ATOM   4883 O  O    . SER   B 1 65  ? 50.846 -11.056 7.779   1.00 11.84 ?  65   SER   B O    1 
ATOM   4884 C  CB   . SER   B 1 65  ? 51.627 -13.335 5.533   1.00 11.37 ?  65   SER   B CB   1 
ATOM   4885 O  OG   . SER   B 1 65  ? 51.276 -13.725 4.213   1.00 11.45 ?  65   SER   B OG   1 
ATOM   4886 H  H    . SER   B 1 65  ? 53.310 -11.928 4.532   1.00 13.46 ?  65   SER   B H    1 
ATOM   4887 H  HA   . SER   B 1 65  ? 50.871 -11.445 5.333   1.00 13.44 ?  65   SER   B HA   1 
ATOM   4888 H  HB2  . SER   B 1 65  ? 52.490 -13.715 5.746   1.00 13.67 ?  65   SER   B HB2  1 
ATOM   4889 H  HB3  . SER   B 1 65  ? 50.954 -13.672 6.144   1.00 13.67 ?  65   SER   B HB3  1 
ATOM   4890 H  HG   . SER   B 1 65  ? 51.847 -13.436 3.662   1.00 13.77 ?  65   SER   B HG   1 
ATOM   4891 N  N    . ASP   B 1 66  ? 53.056 -11.520 7.693   1.00 11.90 ?  66   ASP   B N    1 
ATOM   4892 C  CA   . ASP   B 1 66  ? 53.253 -11.134 9.088   1.00 11.91 ?  66   ASP   B CA   1 
ATOM   4893 C  C    . ASP   B 1 66  ? 52.936 -9.659  9.297   1.00 12.23 ?  66   ASP   B C    1 
ATOM   4894 O  O    . ASP   B 1 66  ? 52.355 -9.278  10.320  1.00 12.71 ?  66   ASP   B O    1 
ATOM   4895 C  CB   . ASP   B 1 66  ? 54.685 -11.438 9.525   1.00 13.27 ?  66   ASP   B CB   1 
ATOM   4896 C  CG   . ASP   B 1 66  ? 54.954 -12.925 9.677   1.00 15.06 ?  66   ASP   B CG   1 
ATOM   4897 O  OD1  . ASP   B 1 66  ? 54.007 -13.739 9.606   1.00 15.60 ?  66   ASP   B OD1  1 
ATOM   4898 O  OD2  . ASP   B 1 66  ? 56.131 -13.288 9.880   1.00 17.78 -1 66   ASP   B OD2  1 
ATOM   4899 H  H    . ASP   B 1 66  ? 53.756 -11.818 7.295   1.00 14.31 ?  66   ASP   B H    1 
ATOM   4900 H  HA   . ASP   B 1 66  ? 52.653 -11.647 9.649   1.00 14.32 ?  66   ASP   B HA   1 
ATOM   4901 H  HB2  . ASP   B 1 66  ? 55.299 -11.092 8.858   1.00 15.95 ?  66   ASP   B HB2  1 
ATOM   4902 H  HB3  . ASP   B 1 66  ? 54.850 -11.010 10.381  1.00 15.95 ?  66   ASP   B HB3  1 
ATOM   4903 N  N    . ASP   B 1 67  ? 53.308 -8.811  8.338   1.00 11.94 ?  67   ASP   B N    1 
ATOM   4904 C  CA   . ASP   B 1 67  ? 52.959 -7.400  8.434   1.00 12.57 ?  67   ASP   B CA   1 
ATOM   4905 C  C    . ASP   B 1 67  ? 51.448 -7.196  8.352   1.00 12.59 ?  67   ASP   B C    1 
ATOM   4906 O  O    . ASP   B 1 67  ? 50.886 -6.391  9.103   1.00 13.08 ?  67   ASP   B O    1 
ATOM   4907 C  CB   . ASP   B 1 67  ? 53.677 -6.618  7.342   1.00 13.83 ?  67   ASP   B CB   1 
ATOM   4908 C  CG   . ASP   B 1 67  ? 53.252 -5.175  7.309   1.00 15.14 ?  67   ASP   B CG   1 
ATOM   4909 O  OD1  . ASP   B 1 67  ? 53.751 -4.373  8.131   1.00 16.30 ?  67   ASP   B OD1  1 
ATOM   4910 O  OD2  . ASP   B 1 67  ? 52.385 -4.860  6.476   1.00 16.09 -1 67   ASP   B OD2  1 
ATOM   4911 H  H    . ASP   B 1 67  ? 53.757 -9.025  7.634   1.00 14.36 ?  67   ASP   B H    1 
ATOM   4912 H  HA   . ASP   B 1 67  ? 53.261 -7.059  9.288   1.00 15.11 ?  67   ASP   B HA   1 
ATOM   4913 H  HB2  . ASP   B 1 67  ? 54.635 -6.643  7.506   1.00 16.63 ?  67   ASP   B HB2  1 
ATOM   4914 H  HB3  . ASP   B 1 67  ? 53.482 -7.021  6.478   1.00 16.63 ?  67   ASP   B HB3  1 
ATOM   4915 N  N    . TYR   B 1 68  ? 50.770 -7.929  7.459   1.00 12.25 ?  68   TYR   B N    1 
ATOM   4916 C  CA   . TYR   B 1 68  ? 49.311 -7.859  7.389   1.00 12.93 ?  68   TYR   B CA   1 
ATOM   4917 C  C    . TYR   B 1 68  ? 48.679 -8.198  8.736   1.00 12.45 ?  68   TYR   B C    1 
ATOM   4918 O  O    . TYR   B 1 68  ? 47.746 -7.521  9.185   1.00 13.30 ?  68   TYR   B O    1 
ATOM   4919 C  CB   . TYR   B 1 68  ? 48.777 -8.790  6.291   1.00 13.74 ?  68   TYR   B CB   1 
ATOM   4920 C  CG   . TYR   B 1 68  ? 47.268 -8.936  6.349   1.00 14.59 ?  68   TYR   B CG   1 
ATOM   4921 C  CD1  . TYR   B 1 68  ? 46.674 -9.891  7.170   1.00 15.50 ?  68   TYR   B CD1  1 
ATOM   4922 C  CD2  . TYR   B 1 68  ? 46.442 -8.097  5.620   1.00 15.48 ?  68   TYR   B CD2  1 
ATOM   4923 C  CE1  . TYR   B 1 68  ? 45.309 -10.011 7.260   1.00 16.72 ?  68   TYR   B CE1  1 
ATOM   4924 C  CE2  . TYR   B 1 68  ? 45.060 -8.219  5.696   1.00 16.07 ?  68   TYR   B CE2  1 
ATOM   4925 C  CZ   . TYR   B 1 68  ? 44.513 -9.176  6.519   1.00 16.35 ?  68   TYR   B CZ   1 
ATOM   4926 O  OH   . TYR   B 1 68  ? 43.146 -9.289  6.612   1.00 17.16 ?  68   TYR   B OH   1 
ATOM   4927 H  H    . TYR   B 1 68  ? 51.130 -8.476  6.893   1.00 14.73 ?  68   TYR   B H    1 
ATOM   4928 H  HA   . TYR   B 1 68  ? 49.056 -6.957  7.163   1.00 15.54 ?  68   TYR   B HA   1 
ATOM   4929 H  HB2  . TYR   B 1 68  ? 49.007 -8.425  5.426   1.00 16.51 ?  68   TYR   B HB2  1 
ATOM   4930 H  HB3  . TYR   B 1 68  ? 49.167 -9.671  6.401   1.00 16.51 ?  68   TYR   B HB3  1 
ATOM   4931 H  HD1  . TYR   B 1 68  ? 47.210 -10.460 7.674   1.00 18.63 ?  68   TYR   B HD1  1 
ATOM   4932 H  HD2  . TYR   B 1 68  ? 46.820 -7.449  5.078   1.00 18.60 ?  68   TYR   B HD2  1 
ATOM   4933 H  HE1  . TYR   B 1 68  ? 44.924 -10.665 7.805   1.00 20.10 ?  68   TYR   B HE1  1 
ATOM   4934 H  HE2  . TYR   B 1 68  ? 44.510 -7.654  5.206   1.00 19.32 ?  68   TYR   B HE2  1 
ATOM   4935 H  HH   . TYR   B 1 68  ? 42.760 -8.734  6.103   1.00 20.62 ?  68   TYR   B HH   1 
ATOM   4936 N  N    . ILE   B 1 69  ? 49.162 -9.263  9.383   1.00 12.46 ?  69   ILE   B N    1 
ATOM   4937 C  CA   . ILE   B 1 69  ? 48.607 -9.688  10.665  1.00 13.02 ?  69   ILE   B CA   1 
ATOM   4938 C  C    . ILE   B 1 69  ? 48.859 -8.639  11.741  1.00 12.54 ?  69   ILE   B C    1 
ATOM   4939 O  O    . ILE   B 1 69  ? 47.989 -8.363  12.571  1.00 12.98 ?  69   ILE   B O    1 
ATOM   4940 C  CB   . ILE   B 1 69  ? 49.177 -11.067 11.058  1.00 13.78 ?  69   ILE   B CB   1 
ATOM   4941 C  CG1  . ILE   B 1 69  ? 48.647 -12.165 10.127  1.00 14.08 ?  69   ILE   B CG1  1 
ATOM   4942 C  CG2  . ILE   B 1 69  ? 48.884 -11.392 12.518  1.00 14.85 ?  69   ILE   B CG2  1 
ATOM   4943 C  CD1  . ILE   B 1 69  ? 47.172 -12.486 10.294  1.00 14.27 ?  69   ILE   B CD1  1 
ATOM   4944 H  H    . ILE   B 1 69  ? 49.814 -9.750  9.108   1.00 14.98 ?  69   ILE   B H    1 
ATOM   4945 H  HA   . ILE   B 1 69  ? 47.649 -9.782  10.573  1.00 15.66 ?  69   ILE   B HA   1 
ATOM   4946 H  HB   . ILE   B 1 69  ? 50.142 -11.030 10.954  1.00 16.56 ?  69   ILE   B HB   1 
ATOM   4947 H  HG12 . ILE   B 1 69  ? 48.783 -11.879 9.210   1.00 16.93 ?  69   ILE   B HG12 1 
ATOM   4948 H  HG13 . ILE   B 1 69  ? 49.147 -12.977 10.294  1.00 16.93 ?  69   ILE   B HG13 1 
ATOM   4949 H  HG21 . ILE   B 1 69  ? 49.035 -12.341 12.663  1.00 17.85 ?  69   ILE   B HG21 1 
ATOM   4950 H  HG22 . ILE   B 1 69  ? 49.478 -10.878 13.088  1.00 17.85 ?  69   ILE   B HG22 1 
ATOM   4951 H  HG23 . ILE   B 1 69  ? 47.960 -11.173 12.712  1.00 17.85 ?  69   ILE   B HG23 1 
ATOM   4952 H  HD11 . ILE   B 1 69  ? 46.930 -13.176 9.660   1.00 17.15 ?  69   ILE   B HD11 1 
ATOM   4953 H  HD12 . ILE   B 1 69  ? 47.016 -12.801 11.199  1.00 17.15 ?  69   ILE   B HD12 1 
ATOM   4954 H  HD13 . ILE   B 1 69  ? 46.650 -11.686 10.129  1.00 17.15 ?  69   ILE   B HD13 1 
ATOM   4955 N  N    . ALA   B 1 70  ? 50.053 -8.052  11.762  1.00 12.65 ?  70   ALA   B N    1 
ATOM   4956 C  CA   . ALA   B 1 70  ? 50.336 -7.019  12.751  1.00 12.56 ?  70   ALA   B CA   1 
ATOM   4957 C  C    . ALA   B 1 70  ? 49.337 -5.875  12.638  1.00 12.70 ?  70   ALA   B C    1 
ATOM   4958 O  O    . ALA   B 1 70  ? 48.906 -5.317  13.652  1.00 13.27 ?  70   ALA   B O    1 
ATOM   4959 C  CB   . ALA   B 1 70  ? 51.767 -6.508  12.584  1.00 13.25 ?  70   ALA   B CB   1 
ATOM   4960 H  H    . ALA   B 1 70  ? 50.698 -8.227  11.230  1.00 15.21 ?  70   ALA   B H    1 
ATOM   4961 H  HA   . ALA   B 1 70  ? 50.259 -7.396  13.643  1.00 15.10 ?  70   ALA   B HA   1 
ATOM   4962 H  HB1  . ALA   B 1 70  ? 51.953 -5.845  13.271  1.00 15.92 ?  70   ALA   B HB1  1 
ATOM   4963 H  HB2  . ALA   B 1 70  ? 52.384 -7.254  12.677  1.00 15.92 ?  70   ALA   B HB2  1 
ATOM   4964 H  HB3  . ALA   B 1 70  ? 51.865 -6.109  11.706  1.00 15.92 ?  70   ALA   B HB3  1 
ATOM   4965 N  N    . THR   B 1 71  ? 48.955 -5.516  11.413  1.00 13.28 ?  71   THR   B N    1 
ATOM   4966 C  CA   . THR   B 1 71  ? 48.069 -4.377  11.202  1.00 14.30 ?  71   THR   B CA   1 
ATOM   4967 C  C    . THR   B 1 71  ? 46.600 -4.739  11.402  1.00 14.73 ?  71   THR   B C    1 
ATOM   4968 O  O    . THR   B 1 71  ? 45.821 -3.920  11.909  1.00 16.35 ?  71   THR   B O    1 
ATOM   4969 C  CB   . THR   B 1 71  ? 48.295 -3.810  9.799   1.00 16.09 ?  71   THR   B CB   1 
ATOM   4970 O  OG1  . THR   B 1 71  ? 49.622 -3.281  9.709   1.00 18.24 ?  71   THR   B OG1  1 
ATOM   4971 C  CG2  . THR   B 1 71  ? 47.278 -2.719  9.467   1.00 17.19 ?  71   THR   B CG2  1 
ATOM   4972 H  H    . THR   B 1 71  ? 49.204 -5.912  10.693  1.00 15.97 ?  71   THR   B H    1 
ATOM   4973 H  HA   . THR   B 1 71  ? 48.293 -3.681  11.840  1.00 17.19 ?  71   THR   B HA   1 
ATOM   4974 H  HB   . THR   B 1 71  ? 48.199 -4.520  9.146   1.00 19.33 ?  71   THR   B HB   1 
ATOM   4975 H  HG1  . THR   B 1 71  ? 49.756 -2.958  8.941   1.00 21.92 ?  71   THR   B HG1  1 
ATOM   4976 H  HG21 . THR   B 1 71  ? 47.585 -2.200  8.706   1.00 20.66 ?  71   THR   B HG21 1 
ATOM   4977 H  HG22 . THR   B 1 71  ? 46.421 -3.116  9.250   1.00 20.66 ?  71   THR   B HG22 1 
ATOM   4978 H  HG23 . THR   B 1 71  ? 47.171 -2.124  10.227  1.00 20.66 ?  71   THR   B HG23 1 
ATOM   4979 N  N    . ASN   B 1 72  ? 46.205 -5.953  11.009  1.00 14.43 ?  72   ASN   B N    1 
ATOM   4980 C  CA   . ASN   B 1 72  ? 44.801 -6.312  10.878  1.00 14.96 ?  72   ASN   B CA   1 
ATOM   4981 C  C    . ASN   B 1 72  ? 44.328 -7.415  11.812  1.00 15.46 ?  72   ASN   B C    1 
ATOM   4982 O  O    . ASN   B 1 72  ? 43.112 -7.578  11.969  1.00 16.67 ?  72   ASN   B O    1 
ATOM   4983 C  CB   . ASN   B 1 72  ? 44.500 -6.738  9.434   1.00 15.81 ?  72   ASN   B CB   1 
ATOM   4984 C  CG   . ASN   B 1 72  ? 44.776 -5.634  8.442   1.00 16.94 ?  72   ASN   B CG   1 
ATOM   4985 O  OD1  . ASN   B 1 72  ? 45.794 -5.638  7.744   1.00 18.15 ?  72   ASN   B OD1  1 
ATOM   4986 N  ND2  . ASN   B 1 72  ? 43.888 -4.664  8.396   1.00 18.56 ?  72   ASN   B ND2  1 
ATOM   4987 H  H    . ASN   B 1 72  ? 46.748 -6.594  10.801  1.00 17.35 ?  72   ASN   B H    1 
ATOM   4988 H  HA   . ASN   B 1 72  ? 44.270 -5.525  11.062  1.00 17.98 ?  72   ASN   B HA   1 
ATOM   4989 H  HB2  . ASN   B 1 72  ? 45.058 -7.499  9.202   1.00 19.00 ?  72   ASN   B HB2  1 
ATOM   4990 H  HB3  . ASN   B 1 72  ? 43.564 -6.980  9.364   1.00 19.00 ?  72   ASN   B HB3  1 
ATOM   4991 H  HD21 . ASN   B 1 72  ? 43.993 -4.010  7.848   1.00 22.30 ?  72   ASN   B HD21 1 
ATOM   4992 H  HD22 . ASN   B 1 72  ? 43.189 -4.692  8.900   1.00 22.30 ?  72   ASN   B HD22 1 
ATOM   4993 N  N    . GLY   B 1 73  ? 45.230 -8.169  12.431  1.00 14.88 ?  73   GLY   B N    1 
ATOM   4994 C  CA   . GLY   B 1 73  ? 44.838 -9.311  13.219  1.00 14.39 ?  73   GLY   B CA   1 
ATOM   4995 C  C    . GLY   B 1 73  ? 44.469 -10.494 12.348  1.00 13.05 ?  73   GLY   B C    1 
ATOM   4996 O  O    . GLY   B 1 73  ? 44.449 -10.408 11.117  1.00 13.28 ?  73   GLY   B O    1 
ATOM   4997 H  H    . GLY   B 1 73  ? 46.080 -8.032  12.407  1.00 17.89 ?  73   GLY   B H    1 
ATOM   4998 H  HA2  . GLY   B 1 73  ? 45.569 -9.567  13.804  1.00 17.29 ?  73   GLY   B HA2  1 
ATOM   4999 H  HA3  . GLY   B 1 73  ? 44.072 -9.079  13.770  1.00 17.29 ?  73   GLY   B HA3  1 
ATOM   5000 N  N    . PRO   B 1 74  ? 44.163 -11.621 12.984  1.00 13.41 ?  74   PRO   B N    1 
ATOM   5001 C  CA   . PRO   B 1 74  ? 43.911 -12.852 12.234  1.00 13.12 ?  74   PRO   B CA   1 
ATOM   5002 C  C    . PRO   B 1 74  ? 42.610 -12.796 11.446  1.00 12.40 ?  74   PRO   B C    1 
ATOM   5003 O  O    . PRO   B 1 74  ? 41.668 -12.057 11.761  1.00 13.53 ?  74   PRO   B O    1 
ATOM   5004 C  CB   . PRO   B 1 74  ? 43.838 -13.919 13.333  1.00 14.00 ?  74   PRO   B CB   1 
ATOM   5005 C  CG   . PRO   B 1 74  ? 43.394 -13.174 14.545  1.00 15.36 ?  74   PRO   B CG   1 
ATOM   5006 C  CD   . PRO   B 1 74  ? 44.069 -11.833 14.438  1.00 14.71 ?  74   PRO   B CD   1 
ATOM   5007 H  HA   . PRO   B 1 74  ? 44.656 -13.044 11.637  1.00 15.77 ?  74   PRO   B HA   1 
ATOM   5008 H  HB2  . PRO   B 1 74  ? 43.189 -14.596 13.086  1.00 16.83 ?  74   PRO   B HB2  1 
ATOM   5009 H  HB3  . PRO   B 1 74  ? 44.714 -14.312 13.469  1.00 16.83 ?  74   PRO   B HB3  1 
ATOM   5010 H  HG2  . PRO   B 1 74  ? 42.429 -13.074 14.533  1.00 18.45 ?  74   PRO   B HG2  1 
ATOM   5011 H  HG3  . PRO   B 1 74  ? 43.684 -13.641 15.342  1.00 18.45 ?  74   PRO   B HG3  1 
ATOM   5012 H  HD2  . PRO   B 1 74  ? 43.520 -11.143 14.852  1.00 17.68 ?  74   PRO   B HD2  1 
ATOM   5013 H  HD3  . PRO   B 1 74  ? 44.954 -11.864 14.833  1.00 17.68 ?  74   PRO   B HD3  1 
ATOM   5014 N  N    . LEU   B 1 75  ? 42.580 -13.612 10.396  1.00 11.65 ?  75   LEU   B N    1 
ATOM   5015 C  CA   . LEU   B 1 75  ? 41.366 -13.839 9.633   1.00 11.93 ?  75   LEU   B CA   1 
ATOM   5016 C  C    . LEU   B 1 75  ? 40.402 -14.708 10.440  1.00 12.29 ?  75   LEU   B C    1 
ATOM   5017 O  O    . LEU   B 1 75  ? 40.749 -15.262 11.486  1.00 13.27 ?  75   LEU   B O    1 
ATOM   5018 C  CB   . LEU   B 1 75  ? 41.691 -14.550 8.319   1.00 11.93 ?  75   LEU   B CB   1 
ATOM   5019 C  CG   . LEU   B 1 75  ? 42.551 -13.802 7.295   1.00 13.58 ?  75   LEU   B CG   1 
ATOM   5020 C  CD1  . LEU   B 1 75  ? 42.725 -14.634 6.027   1.00 15.05 ?  75   LEU   B CD1  1 
ATOM   5021 C  CD2  . LEU   B 1 75  ? 41.978 -12.452 6.959   1.00 16.70 ?  75   LEU   B CD2  1 
ATOM   5022 H  H    . LEU   B 1 75  ? 43.259 -14.051 10.096  1.00 14.01 ?  75   LEU   B H    1 
ATOM   5023 H  HA   . LEU   B 1 75  ? 40.932 -12.994 9.435   1.00 14.34 ?  75   LEU   B HA   1 
ATOM   5024 H  HB2  . LEU   B 1 75  ? 42.155 -15.375 8.529   1.00 14.34 ?  75   LEU   B HB2  1 
ATOM   5025 H  HB3  . LEU   B 1 75  ? 40.852 -14.765 7.875   1.00 14.34 ?  75   LEU   B HB3  1 
ATOM   5026 H  HG   . LEU   B 1 75  ? 43.433 -13.665 7.673   1.00 16.32 ?  75   LEU   B HG   1 
ATOM   5027 H  HD11 . LEU   B 1 75  ? 43.278 -14.140 5.396   1.00 18.09 ?  75   LEU   B HD11 1 
ATOM   5028 H  HD12 . LEU   B 1 75  ? 43.157 -15.474 6.252   1.00 18.09 ?  75   LEU   B HD12 1 
ATOM   5029 H  HD13 . LEU   B 1 75  ? 41.855 -14.805 5.635   1.00 18.09 ?  75   LEU   B HD13 1 
ATOM   5030 H  HD21 . LEU   B 1 75  ? 42.502 -12.054 6.248   1.00 20.07 ?  75   LEU   B HD21 1 
ATOM   5031 H  HD22 . LEU   B 1 75  ? 41.058 -12.562 6.673   1.00 20.07 ?  75   LEU   B HD22 1 
ATOM   5032 H  HD23 . LEU   B 1 75  ? 42.013 -11.891 7.750   1.00 20.07 ?  75   LEU   B HD23 1 
ATOM   5033 N  N    . LYS   B 1 76  ? 39.169 -14.810 9.942   1.00 13.50 ?  76   LYS   B N    1 
ATOM   5034 C  CA   . LYS   B 1 76  ? 38.189 -15.780 10.416  1.00 14.77 ?  76   LYS   B CA   1 
ATOM   5035 C  C    . LYS   B 1 76  ? 38.278 -17.046 9.570   1.00 13.36 ?  76   LYS   B C    1 
ATOM   5036 O  O    . LYS   B 1 76  ? 38.543 -16.981 8.370   1.00 12.89 ?  76   LYS   B O    1 
ATOM   5037 C  CB   . LYS   B 1 76  ? 36.766 -15.215 10.252  1.00 17.59 ?  76   LYS   B CB   1 
ATOM   5038 C  CG   . LYS   B 1 76  ? 36.501 -13.816 10.843  1.00 19.91 ?  76   LYS   B CG   1 
ATOM   5039 C  CD   . LYS   B 1 76  ? 35.094 -13.278 10.497  1.00 21.44 ?  76   LYS   B CD   1 
ATOM   5040 C  CE   . LYS   B 1 76  ? 34.837 -11.918 11.133  1.00 23.60 ?  76   LYS   B CE   1 
ATOM   5041 N  NZ   . LYS   B 1 76  ? 33.551 -11.305 10.689  1.00 24.50 ?  76   LYS   B NZ   1 
ATOM   5042 H  H    . LYS   B 1 76  ? 38.868 -14.311 9.314   1.00 16.23 ?  76   LYS   B H    1 
ATOM   5043 H  HA   . LYS   B 1 76  ? 38.340 -16.004 11.350  1.00 17.76 ?  76   LYS   B HA   1 
ATOM   5044 H  HB2  . LYS   B 1 76  ? 36.566 -15.166 9.302   1.00 21.13 ?  76   LYS   B HB2  1 
ATOM   5045 H  HB3  . LYS   B 1 76  ? 36.140 -15.825 10.676  1.00 21.13 ?  76   LYS   B HB3  1 
ATOM   5046 H  HG2  . LYS   B 1 76  ? 36.578 -13.860 11.808  1.00 23.92 ?  76   LYS   B HG2  1 
ATOM   5047 H  HG3  . LYS   B 1 76  ? 37.156 -13.193 10.486  1.00 23.92 ?  76   LYS   B HG3  1 
ATOM   5048 H  HD2  . LYS   B 1 76  ? 35.014 -13.182 9.534   1.00 25.76 ?  76   LYS   B HD2  1 
ATOM   5049 H  HD3  . LYS   B 1 76  ? 34.424 -13.898 10.827  1.00 25.76 ?  76   LYS   B HD3  1 
ATOM   5050 H  HE2  . LYS   B 1 76  ? 34.805 -12.022 12.097  1.00 28.35 ?  76   LYS   B HE2  1 
ATOM   5051 H  HE3  . LYS   B 1 76  ? 35.557 -11.315 10.889  1.00 28.35 ?  76   LYS   B HE3  1 
ATOM   5052 H  HZ1  . LYS   B 1 76  ? 33.438 -10.513 11.082  1.00 29.43 ?  76   LYS   B HZ1  1 
ATOM   5053 H  HZ2  . LYS   B 1 76  ? 33.555 -11.190 9.806   1.00 29.43 ?  76   LYS   B HZ2  1 
ATOM   5054 H  HZ3  . LYS   B 1 76  ? 32.868 -11.834 10.908  1.00 29.43 ?  76   LYS   B HZ3  1 
ATOM   5055 N  N    . VAL   B 1 77  ? 38.031 -18.206 10.191  1.00 13.73 ?  77   VAL   B N    1 
ATOM   5056 C  CA   . VAL   B 1 77  ? 37.818 -19.414 9.401   1.00 13.79 ?  77   VAL   B CA   1 
ATOM   5057 C  C    . VAL   B 1 77  ? 36.622 -19.175 8.491   1.00 12.77 ?  77   VAL   B C    1 
ATOM   5058 O  O    . VAL   B 1 77  ? 35.559 -18.722 8.941   1.00 12.96 ?  77   VAL   B O    1 
ATOM   5059 C  CB   . VAL   B 1 77  ? 37.626 -20.645 10.302  1.00 15.05 ?  77   VAL   B CB   1 
ATOM   5060 C  CG1  . VAL   B 1 77  ? 37.328 -21.873 9.449   1.00 15.88 ?  77   VAL   B CG1  1 
ATOM   5061 C  CG2  . VAL   B 1 77  ? 38.866 -20.890 11.157  1.00 16.41 ?  77   VAL   B CG2  1 
ATOM   5062 H  H    . VAL   B 1 77  ? 37.997 -18.318 11.039  1.00 16.50 ?  77   VAL   B H    1 
ATOM   5063 H  HA   . VAL   B 1 77  ? 38.590 -19.571 8.838   1.00 16.57 ?  77   VAL   B HA   1 
ATOM   5064 H  HB   . VAL   B 1 77  ? 36.868 -20.492 10.892  1.00 18.09 ?  77   VAL   B HB   1 
ATOM   5065 H  HG11 . VAL   B 1 77  ? 37.387 -22.664 10.009  1.00 19.09 ?  77   VAL   B HG11 1 
ATOM   5066 H  HG12 . VAL   B 1 77  ? 36.430 -21.800 9.083   1.00 19.09 ?  77   VAL   B HG12 1 
ATOM   5067 H  HG13 . VAL   B 1 77  ? 37.976 -21.926 8.733   1.00 19.09 ?  77   VAL   B HG13 1 
ATOM   5068 H  HG21 . VAL   B 1 77  ? 38.724 -21.685 11.690  1.00 19.72 ?  77   VAL   B HG21 1 
ATOM   5069 H  HG22 . VAL   B 1 77  ? 39.628 -21.009 10.572  1.00 19.72 ?  77   VAL   B HG22 1 
ATOM   5070 H  HG23 . VAL   B 1 77  ? 39.004 -20.122 11.733  1.00 19.72 ?  77   VAL   B HG23 1 
ATOM   5071 N  N    . GLY   B 1 78  ? 36.801 -19.454 7.202   1.00 12.35 ?  78   GLY   B N    1 
ATOM   5072 C  CA   . GLY   B 1 78  ? 35.828 -19.125 6.187   1.00 12.00 ?  78   GLY   B CA   1 
ATOM   5073 C  C    . GLY   B 1 78  ? 36.068 -17.801 5.498   1.00 11.46 ?  78   GLY   B C    1 
ATOM   5074 O  O    . GLY   B 1 78  ? 35.389 -17.507 4.510   1.00 11.82 ?  78   GLY   B O    1 
ATOM   5075 H  H    . GLY   B 1 78  ? 37.504 -19.836 6.884   1.00 14.84 ?  78   GLY   B H    1 
ATOM   5076 H  HA2  . GLY   B 1 78  ? 35.823 -19.815 5.510   1.00 14.43 ?  78   GLY   B HA2  1 
ATOM   5077 H  HA3  . GLY   B 1 78  ? 34.945 -19.090 6.591   1.00 14.43 ?  78   GLY   B HA3  1 
ATOM   5078 N  N    . GLY   B 1 79  ? 37.019 -17.001 5.982   1.00 11.62 ?  79   GLY   B N    1 
ATOM   5079 C  CA   . GLY   B 1 79  ? 37.310 -15.699 5.418   1.00 11.21 ?  79   GLY   B CA   1 
ATOM   5080 C  C    . GLY   B 1 79  ? 38.546 -15.709 4.527   1.00 10.58 ?  79   GLY   B C    1 
ATOM   5081 O  O    . GLY   B 1 79  ? 39.157 -16.744 4.263   1.00 11.19 ?  79   GLY   B O    1 
ATOM   5082 H  H    . GLY   B 1 79  ? 37.526 -17.204 6.642   1.00 13.97 ?  79   GLY   B H    1 
ATOM   5083 H  HA2  . GLY   B 1 79  ? 36.556 -15.394 4.890   1.00 13.48 ?  79   GLY   B HA2  1 
ATOM   5084 H  HA3  . GLY   B 1 79  ? 37.459 -15.063 6.135   1.00 13.48 ?  79   GLY   B HA3  1 
ATOM   5085 N  N    . SER   B 1 80  ? 38.910 -14.511 4.059   1.00 10.70 ?  80   SER   B N    1 
ATOM   5086 C  CA   . SER   B 1 80  ? 40.013 -14.375 3.117   1.00 10.49 ?  80   SER   B CA   1 
ATOM   5087 C  C    . SER   B 1 80  ? 40.591 -12.967 3.180   1.00 10.29 ?  80   SER   B C    1 
ATOM   5088 O  O    . SER   B 1 80  ? 39.972 -12.036 3.699   1.00 11.54 ?  80   SER   B O    1 
ATOM   5089 C  CB   . SER   B 1 80  ? 39.568 -14.662 1.678   1.00 11.00 ?  80   SER   B CB   1 
ATOM   5090 O  OG   . SER   B 1 80  ? 38.725 -13.637 1.175   1.00 12.08 ?  80   SER   B OG   1 
ATOM   5091 H  H    . SER   B 1 80  ? 38.540 -13.769 4.274   1.00 12.87 ?  80   SER   B H    1 
ATOM   5092 H  HA   . SER   B 1 80  ? 40.708 -15.005 3.358   1.00 12.62 ?  80   SER   B HA   1 
ATOM   5093 H  HB2  . SER   B 1 80  ? 40.351 -14.725 1.112   1.00 13.23 ?  80   SER   B HB2  1 
ATOM   5094 H  HB3  . SER   B 1 80  ? 39.082 -15.503 1.663   1.00 13.23 ?  80   SER   B HB3  1 
ATOM   5095 H  HG   . SER   B 1 80  ? 38.035 -13.576 1.653   1.00 14.53 ?  80   SER   B HG   1 
ATOM   5096 N  N    . CYS   B 1 81  ? 41.779 -12.816 2.594   1.00 10.24 ?  81   CYS   B N    1 
ATOM   5097 C  CA   . CYS   B 1 81  ? 42.319 -11.500 2.291   1.00 10.44 ?  81   CYS   B CA   1 
ATOM   5098 C  C    . CYS   B 1 81  ? 43.087 -11.576 0.980   1.00 9.68  ?  81   CYS   B C    1 
ATOM   5099 O  O    . CYS   B 1 81  ? 43.601 -12.634 0.598   1.00 10.66 ?  81   CYS   B O    1 
ATOM   5100 C  CB   . CYS   B 1 81  ? 43.218 -10.952 3.409   1.00 11.04 ?  81   CYS   B CB   1 
ATOM   5101 S  SG   . CYS   B 1 81  ? 44.737 -11.877 3.646   1.00 11.39 ?  81   CYS   B SG   1 
ATOM   5102 H  H    . CYS   B 1 81  ? 42.291 -13.468 2.353   1.00 12.31 ?  81   CYS   B H    1 
ATOM   5103 H  HA   . CYS   B 1 81  ? 41.585 -10.878 2.170   1.00 12.56 ?  81   CYS   B HA   1 
ATOM   5104 H  HB2  . CYS   B 1 81  ? 43.462 -10.035 3.198   1.00 13.28 ?  81   CYS   B HB2  1 
ATOM   5105 H  HB3  . CYS   B 1 81  ? 42.723 -10.969 4.247   1.00 13.28 ?  81   CYS   B HB3  1 
ATOM   5106 H  HG   . CYS   B 1 81  ? 45.367 -11.382 4.541   1.00 13.69 ?  81   CYS   B HG   1 
ATOM   5107 N  N    . VAL   B 1 82  ? 43.181 -10.432 0.308   1.00 10.09 ?  82   VAL   B N    1 
ATOM   5108 C  CA   . VAL   B 1 82  ? 43.945 -10.301 -0.930  1.00 10.48 ?  82   VAL   B CA   1 
ATOM   5109 C  C    . VAL   B 1 82  ? 45.287 -9.662  -0.612  1.00 10.68 ?  82   VAL   B C    1 
ATOM   5110 O  O    . VAL   B 1 82  ? 45.339 -8.548  -0.074  1.00 11.74 ?  82   VAL   B O    1 
ATOM   5111 C  CB   . VAL   B 1 82  ? 43.196 -9.458  -1.973  1.00 11.67 ?  82   VAL   B CB   1 
ATOM   5112 C  CG1  . VAL   B 1 82  ? 44.049 -9.303  -3.229  1.00 12.96 ?  82   VAL   B CG1  1 
ATOM   5113 C  CG2  . VAL   B 1 82  ? 41.840 -10.057 -2.292  1.00 12.50 ?  82   VAL   B CG2  1 
ATOM   5114 H  H    . VAL   B 1 82  ? 42.796 -9.698  0.549   1.00 12.13 ?  82   VAL   B H    1 
ATOM   5115 H  HA   . VAL   B 1 82  ? 44.101 -11.182 -1.307  1.00 12.61 ?  82   VAL   B HA   1 
ATOM   5116 H  HB   . VAL   B 1 82  ? 43.045 -8.575  -1.607  1.00 14.03 ?  82   VAL   B HB   1 
ATOM   5117 H  HG11 . VAL   B 1 82  ? 43.487 -8.998  -3.957  1.00 15.58 ?  82   VAL   B HG11 1 
ATOM   5118 H  HG12 . VAL   B 1 82  ? 44.748 -8.648  -3.058  1.00 15.58 ?  82   VAL   B HG12 1 
ATOM   5119 H  HG13 . VAL   B 1 82  ? 44.445 -10.159 -3.451  1.00 15.58 ?  82   VAL   B HG13 1 
ATOM   5120 H  HG21 . VAL   B 1 82  ? 41.407 -9.523  -2.978  1.00 15.03 ?  82   VAL   B HG21 1 
ATOM   5121 H  HG22 . VAL   B 1 82  ? 41.958 -10.967 -2.610  1.00 15.03 ?  82   VAL   B HG22 1 
ATOM   5122 H  HG23 . VAL   B 1 82  ? 41.294 -10.060 -1.487  1.00 15.03 ?  82   VAL   B HG23 1 
ATOM   5123 N  N    . LEU   B 1 83  ? 46.368 -10.346 -0.983  1.00 10.38 ?  83   LEU   B N    1 
ATOM   5124 C  CA   . LEU   B 1 83  ? 47.722 -9.830  -0.865  1.00 10.24 ?  83   LEU   B CA   1 
ATOM   5125 C  C    . LEU   B 1 83  ? 48.421 -9.966  -2.218  1.00 10.17 ?  83   LEU   B C    1 
ATOM   5126 O  O    . LEU   B 1 83  ? 47.819 -10.377 -3.215  1.00 10.23 ?  83   LEU   B O    1 
ATOM   5127 C  CB   . LEU   B 1 83  ? 48.477 -10.508 0.287   1.00 10.86 ?  83   LEU   B CB   1 
ATOM   5128 C  CG   . LEU   B 1 83  ? 47.969 -10.142 1.688   1.00 12.10 ?  83   LEU   B CG   1 
ATOM   5129 C  CD1  . LEU   B 1 83  ? 48.604 -11.007 2.760   1.00 12.64 ?  83   LEU   B CD1  1 
ATOM   5130 C  CD2  . LEU   B 1 83  ? 48.181 -8.657  2.004   1.00 12.87 ?  83   LEU   B CD2  1 
ATOM   5131 H  H    . LEU   B 1 83  ? 46.334 -11.143 -1.317  1.00 12.49 ?  83   LEU   B H    1 
ATOM   5132 H  HA   . LEU   B 1 83  ? 47.668 -8.887  -0.662  1.00 12.31 ?  83   LEU   B HA   1 
ATOM   5133 H  HB2  . LEU   B 1 83  ? 48.404 -11.468 0.192   1.00 13.06 ?  83   LEU   B HB2  1 
ATOM   5134 H  HB3  . LEU   B 1 83  ? 49.413 -10.246 0.239   1.00 13.06 ?  83   LEU   B HB3  1 
ATOM   5135 H  HG   . LEU   B 1 83  ? 47.015 -10.303 1.713   1.00 14.55 ?  83   LEU   B HG   1 
ATOM   5136 H  HD11 . LEU   B 1 83  ? 48.247 -10.747 3.626   1.00 15.20 ?  83   LEU   B HD11 1 
ATOM   5137 H  HD12 . LEU   B 1 83  ? 48.387 -11.936 2.581   1.00 15.20 ?  83   LEU   B HD12 1 
ATOM   5138 H  HD13 . LEU   B 1 83  ? 49.563 -10.880 2.745   1.00 15.20 ?  83   LEU   B HD13 1 
ATOM   5139 H  HD21 . LEU   B 1 83  ? 47.986 -8.502  2.941   1.00 15.47 ?  83   LEU   B HD21 1 
ATOM   5140 H  HD22 . LEU   B 1 83  ? 49.101 -8.419  1.813   1.00 15.47 ?  83   LEU   B HD22 1 
ATOM   5141 H  HD23 . LEU   B 1 83  ? 47.583 -8.126  1.451   1.00 15.47 ?  83   LEU   B HD23 1 
ATOM   5142 N  N    . SER   B 1 84  ? 49.698 -9.590  -2.268  1.00 11.19 ?  84   SER   B N    1 
ATOM   5143 C  CA   . SER   B 1 84  ? 50.433 -9.696  -3.519  1.00 11.45 ?  84   SER   B CA   1 
ATOM   5144 C  C    . SER   B 1 84  ? 50.581 -11.153 -3.949  1.00 10.73 ?  84   SER   B C    1 
ATOM   5145 O  O    . SER   B 1 84  ? 50.702 -12.061 -3.128  1.00 10.62 ?  84   SER   B O    1 
ATOM   5146 C  CB   . SER   B 1 84  ? 51.828 -9.094  -3.365  1.00 13.40 ?  84   SER   B CB   1 
ATOM   5147 O  OG   . SER   B 1 84  ? 52.571 -9.292  -4.552  1.00 14.93 ?  84   SER   B OG   1 
ATOM   5148 H  H    . SER   B 1 84  ? 50.143 -9.261  -1.606  1.00 13.45 ?  84   SER   B H    1 
ATOM   5149 H  HA   . SER   B 1 84  ? 49.960 -9.218  -4.216  1.00 13.77 ?  84   SER   B HA   1 
ATOM   5150 H  HB2  . SER   B 1 84  ? 51.743 -8.141  -3.188  1.00 16.11 ?  84   SER   B HB2  1 
ATOM   5151 H  HB3  . SER   B 1 84  ? 52.285 -9.528  -2.631  1.00 16.11 ?  84   SER   B HB3  1 
ATOM   5152 H  HG   . SER   B 1 84  ? 53.338 -8.946  -4.473  1.00 17.94 ?  84   SER   B HG   1 
ATOM   5153 N  N    . GLY   B 1 85  ? 50.643 -11.365 -5.258  1.00 11.90 ?  85   GLY   B N    1 
ATOM   5154 C  CA   . GLY   B 1 85  ? 50.999 -12.653 -5.804  1.00 12.30 ?  85   GLY   B CA   1 
ATOM   5155 C  C    . GLY   B 1 85  ? 52.469 -12.847 -6.108  1.00 11.45 ?  85   GLY   B C    1 
ATOM   5156 O  O    . GLY   B 1 85  ? 52.838 -13.928 -6.571  1.00 11.70 ?  85   GLY   B O    1 
ATOM   5157 H  H    . GLY   B 1 85  ? 50.486 -10.768 -5.850  1.00 14.31 ?  85   GLY   B H    1 
ATOM   5158 H  HA2  . GLY   B 1 85  ? 50.733 -13.346 -5.176  1.00 14.79 ?  85   GLY   B HA2  1 
ATOM   5159 H  HA3  . GLY   B 1 85  ? 50.510 -12.792 -6.624  1.00 14.79 ?  85   GLY   B HA3  1 
ATOM   5160 N  N    . HIS   B 1 86  ? 53.327 -11.853 -5.877  1.00 11.31 ?  86   HIS   B N    1 
ATOM   5161 C  CA   . HIS   B 1 86  ? 54.788 -12.037 -5.959  1.00 11.56 ?  86   HIS   B CA   1 
ATOM   5162 C  C    . HIS   B 1 86  ? 55.156 -12.544 -7.352  1.00 11.88 ?  86   HIS   B C    1 
ATOM   5163 O  O    . HIS   B 1 86  ? 54.767 -11.918 -8.350  1.00 12.63 ?  86   HIS   B O    1 
ATOM   5164 C  CB   . HIS   B 1 86  ? 55.279 -12.885 -4.787  1.00 11.72 ?  86   HIS   B CB   1 
ATOM   5165 C  CG   . HIS   B 1 86  ? 54.965 -12.282 -3.459  1.00 12.04 ?  86   HIS   B CG   1 
ATOM   5166 N  ND1  . HIS   B 1 86  ? 55.795 -11.372 -2.836  1.00 13.17 ?  86   HIS   B ND1  1 
ATOM   5167 C  CD2  . HIS   B 1 86  ? 53.886 -12.426 -2.654  1.00 12.14 ?  86   HIS   B CD2  1 
ATOM   5168 C  CE1  . HIS   B 1 86  ? 55.236 -10.988 -1.702  1.00 13.24 ?  86   HIS   B CE1  1 
ATOM   5169 N  NE2  . HIS   B 1 86  ? 54.078 -11.610 -1.569  1.00 12.42 ?  86   HIS   B NE2  1 
ATOM   5170 H  H    . HIS   B 1 86  ? 53.093 -11.055 -5.672  1.00 13.60 ?  86   HIS   B H    1 
ATOM   5171 H  HA   . HIS   B 1 86  ? 55.202 -11.170 -5.864  1.00 13.90 ?  86   HIS   B HA   1 
ATOM   5172 H  HB2  . HIS   B 1 86  ? 54.865 -13.759 -4.826  1.00 14.09 ?  86   HIS   B HB2  1 
ATOM   5173 H  HB3  . HIS   B 1 86  ? 56.248 -12.977 -4.848  1.00 14.09 ?  86   HIS   B HB3  1 
ATOM   5174 H  HD2  . HIS   B 1 86  ? 53.146 -12.971 -2.814  1.00 14.60 ?  86   HIS   B HD2  1 
ATOM   5175 H  HE1  . HIS   B 1 86  ? 55.601 -10.391 -1.089  1.00 15.92 ?  86   HIS   B HE1  1 
ATOM   5176 H  HE2  . HIS   B 1 86  ? 53.538 -11.531 -0.903  1.00 14.93 ?  86   HIS   B HE2  1 
ATOM   5177 N  N    . ASN   B 1 87  ? 55.916 -13.632 -7.470  1.00 11.97 ?  87   ASN   B N    1 
ATOM   5178 C  CA   . ASN   B 1 87  ? 56.304 -14.200 -8.754  1.00 12.45 ?  87   ASN   B CA   1 
ATOM   5179 C  C    . ASN   B 1 87  ? 55.322 -15.245 -9.252  1.00 12.07 ?  87   ASN   B C    1 
ATOM   5180 O  O    . ASN   B 1 87  ? 55.634 -15.958 -10.212 1.00 13.72 ?  87   ASN   B O    1 
ATOM   5181 C  CB   . ASN   B 1 87  ? 57.698 -14.829 -8.652  1.00 14.47 ?  87   ASN   B CB   1 
ATOM   5182 C  CG   . ASN   B 1 87  ? 57.763 -15.950 -7.617  1.00 15.38 ?  87   ASN   B CG   1 
ATOM   5183 O  OD1  . ASN   B 1 87  ? 57.132 -15.874 -6.555  1.00 14.58 ?  87   ASN   B OD1  1 
ATOM   5184 N  ND2  . ASN   B 1 87  ? 58.503 -17.013 -7.941  1.00 17.64 ?  87   ASN   B ND2  1 
ATOM   5185 H  H    . ASN   B 1 87  ? 56.220 -14.080 -6.800  1.00 14.39 ?  87   ASN   B H    1 
ATOM   5186 H  HA   . ASN   B 1 87  ? 56.341 -13.487 -9.410  1.00 14.97 ?  87   ASN   B HA   1 
ATOM   5187 H  HB2  . ASN   B 1 87  ? 57.937 -15.200 -9.520  1.00 17.39 ?  87   ASN   B HB2  1 
ATOM   5188 H  HB3  . ASN   B 1 87  ? 58.334 -14.145 -8.400  1.00 17.39 ?  87   ASN   B HB3  1 
ATOM   5189 H  HD21 . ASN   B 1 87  ? 58.574 -17.667 -7.394  1.00 21.19 ?  87   ASN   B HD21 1 
ATOM   5190 H  HD22 . ASN   B 1 87  ? 58.921 -17.033 -8.697  1.00 21.19 ?  87   ASN   B HD22 1 
ATOM   5191 N  N    . LEU   B 1 88  ? 54.145 -15.344 -8.633  1.00 11.38 ?  88   LEU   B N    1 
ATOM   5192 C  CA   . LEU   B 1 88  ? 53.165 -16.373 -8.957  1.00 11.45 ?  88   LEU   B CA   1 
ATOM   5193 C  C    . LEU   B 1 88  ? 51.929 -15.851 -9.674  1.00 11.48 ?  88   LEU   B C    1 
ATOM   5194 O  O    . LEU   B 1 88  ? 51.325 -16.595 -10.458 1.00 13.08 ?  88   LEU   B O    1 
ATOM   5195 C  CB   . LEU   B 1 88  ? 52.702 -17.055 -7.667  1.00 12.21 ?  88   LEU   B CB   1 
ATOM   5196 C  CG   . LEU   B 1 88  ? 53.810 -17.722 -6.865  1.00 14.54 ?  88   LEU   B CG   1 
ATOM   5197 C  CD1  . LEU   B 1 88  ? 53.321 -18.006 -5.452  1.00 16.00 ?  88   LEU   B CD1  1 
ATOM   5198 C  CD2  . LEU   B 1 88  ? 54.238 -18.999 -7.556  1.00 17.49 ?  88   LEU   B CD2  1 
ATOM   5199 H  H    . LEU   B 1 88  ? 53.891 -14.817 -7.995  1.00 13.68 ?  88   LEU   B H    1 
ATOM   5200 H  HA   . LEU   B 1 88  ? 53.580 -17.039 -9.518  1.00 13.77 ?  88   LEU   B HA   1 
ATOM   5201 H  HB2  . LEU   B 1 88  ? 52.284 -16.394 -7.095  1.00 14.67 ?  88   LEU   B HB2  1 
ATOM   5202 H  HB3  . LEU   B 1 88  ? 52.055 -17.742 -7.899  1.00 14.67 ?  88   LEU   B HB3  1 
ATOM   5203 H  HG   . LEU   B 1 88  ? 54.578 -17.130 -6.813  1.00 17.48 ?  88   LEU   B HG   1 
ATOM   5204 H  HD11 . LEU   B 1 88  ? 53.960 -18.581 -5.006  1.00 19.22 ?  88   LEU   B HD11 1 
ATOM   5205 H  HD12 . LEU   B 1 88  ? 53.239 -17.166 -4.974  1.00 19.22 ?  88   LEU   B HD12 1 
ATOM   5206 H  HD13 . LEU   B 1 88  ? 52.458 -18.443 -5.503  1.00 19.22 ?  88   LEU   B HD13 1 
ATOM   5207 H  HD21 . LEU   B 1 88  ? 54.920 -19.435 -7.021  1.00 21.01 ?  88   LEU   B HD21 1 
ATOM   5208 H  HD22 . LEU   B 1 88  ? 53.467 -19.582 -7.647  1.00 21.01 ?  88   LEU   B HD22 1 
ATOM   5209 H  HD23 . LEU   B 1 88  ? 54.594 -18.783 -8.432  1.00 21.01 ?  88   LEU   B HD23 1 
ATOM   5210 N  N    . ALA   B 1 89  ? 51.524 -14.613 -9.406  1.00 10.80 ?  89   ALA   B N    1 
ATOM   5211 C  CA   . ALA   B 1 89  ? 50.228 -14.116 -9.847  1.00 10.11 ?  89   ALA   B CA   1 
ATOM   5212 C  C    . ALA   B 1 89  ? 50.201 -12.624 -9.571  1.00 10.58 ?  89   ALA   B C    1 
ATOM   5213 O  O    . ALA   B 1 89  ? 51.046 -12.105 -8.840  1.00 11.47 ?  89   ALA   B O    1 
ATOM   5214 C  CB   . ALA   B 1 89  ? 49.100 -14.801 -9.079  1.00 10.42 ?  89   ALA   B CB   1 
ATOM   5215 H  H    . ALA   B 1 89  ? 51.979 -14.032 -8.956  1.00 12.98 ?  89   ALA   B H    1 
ATOM   5216 H  HA   . ALA   B 1 89  ? 50.110 -14.270 -10.798 1.00 12.16 ?  89   ALA   B HA   1 
ATOM   5217 H  HB1  . ALA   B 1 89  ? 48.246 -14.474 -9.407  1.00 12.53 ?  89   ALA   B HB1  1 
ATOM   5218 H  HB2  . ALA   B 1 89  ? 49.158 -15.763 -9.226  1.00 12.53 ?  89   ALA   B HB2  1 
ATOM   5219 H  HB3  . ALA   B 1 89  ? 49.192 -14.608 -8.137  1.00 12.53 ?  89   ALA   B HB3  1 
ATOM   5220 N  N    . LYS   B 1 90  ? 49.201 -11.936 -10.121 1.00 11.48 ?  90   LYS   B N    1 
ATOM   5221 C  CA   . LYS   B 1 90  ? 49.014 -10.549 -9.717  1.00 11.90 ?  90   LYS   B CA   1 
ATOM   5222 C  C    . LYS   B 1 90  ? 48.699 -10.474 -8.228  1.00 11.70 ?  90   LYS   B C    1 
ATOM   5223 O  O    . LYS   B 1 90  ? 49.336 -9.721  -7.478  1.00 12.82 ?  90   LYS   B O    1 
ATOM   5224 C  CB   . LYS   B 1 90  ? 47.933 -9.888  -10.572 1.00 13.35 ?  90   LYS   B CB   1 
ATOM   5225 C  CG   . LYS   B 1 90  ? 47.643 -8.447  -10.196 1.00 13.96 ?  90   LYS   B CG   1 
ATOM   5226 C  CD   . LYS   B 1 90  ? 48.853 -7.553  -10.299 1.00 16.94 ?  90   LYS   B CD   1 
ATOM   5227 C  CE   . LYS   B 1 90  ? 48.421 -6.127  -10.062 1.00 18.77 ?  90   LYS   B CE   1 
ATOM   5228 N  NZ   . LYS   B 1 90  ? 49.575 -5.204  -9.953  1.00 18.78 ?  90   LYS   B NZ   1 
ATOM   5229 H  H    . LYS   B 1 90  ? 48.642 -12.241 -10.702 1.00 13.80 ?  90   LYS   B H    1 
ATOM   5230 H  HA   . LYS   B 1 90  ? 49.844 -10.075 -9.868  1.00 14.30 ?  90   LYS   B HA   1 
ATOM   5231 H  HB2  . LYS   B 1 90  ? 48.225 -9.898  -11.502 1.00 16.05 ?  90   LYS   B HB2  1 
ATOM   5232 H  HB3  . LYS   B 1 90  ? 47.112 -10.394 -10.486 1.00 16.05 ?  90   LYS   B HB3  1 
ATOM   5233 H  HG2  . LYS   B 1 90  ? 46.962 -8.100  -10.790 1.00 16.78 ?  90   LYS   B HG2  1 
ATOM   5234 H  HG3  . LYS   B 1 90  ? 47.323 -8.420  -9.278  1.00 16.78 ?  90   LYS   B HG3  1 
ATOM   5235 H  HD2  . LYS   B 1 90  ? 49.504 -7.798  -9.619  1.00 20.35 ?  90   LYS   B HD2  1 
ATOM   5236 H  HD3  . LYS   B 1 90  ? 49.240 -7.623  -11.185 1.00 20.35 ?  90   LYS   B HD3  1 
ATOM   5237 H  HE2  . LYS   B 1 90  ? 47.871 -5.831  -10.805 1.00 22.55 ?  90   LYS   B HE2  1 
ATOM   5238 H  HE3  . LYS   B 1 90  ? 47.919 -6.075  -9.234  1.00 22.55 ?  90   LYS   B HE3  1 
ATOM   5239 H  HZ1  . LYS   B 1 90  ? 49.291 -4.370  -9.817  1.00 22.56 ?  90   LYS   B HZ1  1 
ATOM   5240 H  HZ2  . LYS   B 1 90  ? 50.098 -5.444  -9.275  1.00 22.56 ?  90   LYS   B HZ2  1 
ATOM   5241 H  HZ3  . LYS   B 1 90  ? 50.053 -5.222  -10.706 1.00 22.56 ?  90   LYS   B HZ3  1 
ATOM   5242 N  N    . HIS   B 1 91  ? 47.747 -11.297 -7.781  1.00 10.29 ?  91   HIS   B N    1 
ATOM   5243 C  CA   . HIS   B 1 91  ? 47.283 -11.324 -6.407  1.00 10.32 ?  91   HIS   B CA   1 
ATOM   5244 C  C    . HIS   B 1 91  ? 47.292 -12.755 -5.892  1.00 9.49  ?  91   HIS   B C    1 
ATOM   5245 O  O    . HIS   B 1 91  ? 47.054 -13.709 -6.642  1.00 10.31 ?  91   HIS   B O    1 
ATOM   5246 C  CB   . HIS   B 1 91  ? 45.830 -10.850 -6.294  1.00 11.77 ?  91   HIS   B CB   1 
ATOM   5247 C  CG   . HIS   B 1 91  ? 45.613 -9.445  -6.729  1.00 15.31 ?  91   HIS   B CG   1 
ATOM   5248 N  ND1  . HIS   B 1 91  ? 46.197 -8.370  -6.095  1.00 18.03 ?  91   HIS   B ND1  1 
ATOM   5249 C  CD2  . HIS   B 1 91  ? 44.853 -8.932  -7.721  1.00 17.70 ?  91   HIS   B CD2  1 
ATOM   5250 C  CE1  . HIS   B 1 91  ? 45.818 -7.252  -6.688  1.00 18.83 ?  91   HIS   B CE1  1 
ATOM   5251 N  NE2  . HIS   B 1 91  ? 44.994 -7.566  -7.673  1.00 18.86 ?  91   HIS   B NE2  1 
ATOM   5252 H  H    . HIS   B 1 91  ? 47.344 -11.871 -8.282  1.00 12.38 ?  91   HIS   B H    1 
ATOM   5253 H  HA   . HIS   B 1 91  ? 47.852 -10.768 -5.845  1.00 12.41 ?  91   HIS   B HA   1 
ATOM   5254 H  HB2  . HIS   B 1 91  ? 45.275 -11.421 -6.847  1.00 14.15 ?  91   HIS   B HB2  1 
ATOM   5255 H  HB3  . HIS   B 1 91  ? 45.551 -10.922 -5.367  1.00 14.15 ?  91   HIS   B HB3  1 
ATOM   5256 H  HD1  . HIS   B 1 91  ? 46.728 -8.420  -5.417  1.00 21.67 ?  91   HIS   B HD1  1 
ATOM   5257 H  HD2  . HIS   B 1 91  ? 44.336 -9.402  -8.329  1.00 21.27 ?  91   HIS   B HD2  1 
ATOM   5258 H  HE1  . HIS   B 1 91  ? 46.081 -6.391  -6.443  1.00 22.62 ?  91   HIS   B HE1  1 
ATOM   5259 N  N    . CYS   B 1 92  ? 47.490 -12.889 -4.590  1.00 9.40  ?  92   CYS   B N    1 
ATOM   5260 C  CA   . CYS   B 1 92  ? 47.193 -14.124 -3.881  1.00 9.25  ?  92   CYS   B CA   1 
ATOM   5261 C  C    . CYS   B 1 92  ? 45.977 -13.896 -2.992  1.00 8.94  ?  92   CYS   B C    1 
ATOM   5262 O  O    . CYS   B 1 92  ? 45.977 -12.991 -2.145  1.00 9.95  ?  92   CYS   B O    1 
ATOM   5263 C  CB   . CYS   B 1 92  ? 48.378 -14.584 -3.038  1.00 9.68  ?  92   CYS   B CB   1 
ATOM   5264 S  SG   . CYS   B 1 92  ? 48.023 -16.125 -2.135  1.00 10.03 ?  92   CYS   B SG   1 
ATOM   5265 H  H    . CYS   B 1 92  ? 47.816 -12.269 -4.083  1.00 11.31 ?  92   CYS   B H    1 
ATOM   5266 H  HA   . CYS   B 1 92  ? 46.989 -14.821 -4.525  1.00 11.13 ?  92   CYS   B HA   1 
ATOM   5267 H  HB2  . CYS   B 1 92  ? 49.139 -14.735 -3.612  1.00 11.65 ?  92   CYS   B HB2  1 
ATOM   5268 H  HB3  . CYS   B 1 92  ? 48.581 -13.895 -2.383  1.00 11.65 ?  92   CYS   B HB3  1 
ATOM   5269 H  HG   . CYS   B 1 92  ? 49.000 -16.438 -1.516  1.00 12.06 ?  92   CYS   B HG   1 
ATOM   5270 N  N    . LEU   B 1 93  ? 44.942 -14.704 -3.207  1.00 9.02  ?  93   LEU   B N    1 
ATOM   5271 C  CA   . LEU   B 1 93  ? 43.769 -14.726 -2.345  1.00 9.21  ?  93   LEU   B CA   1 
ATOM   5272 C  C    . LEU   B 1 93  ? 43.997 -15.793 -1.282  1.00 8.82  ?  93   LEU   B C    1 
ATOM   5273 O  O    . LEU   B 1 93  ? 43.946 -16.996 -1.574  1.00 9.25  ?  93   LEU   B O    1 
ATOM   5274 C  CB   . LEU   B 1 93  ? 42.504 -15.004 -3.153  1.00 9.54  ?  93   LEU   B CB   1 
ATOM   5275 C  CG   . LEU   B 1 93  ? 41.211 -15.031 -2.337  1.00 10.15 ?  93   LEU   B CG   1 
ATOM   5276 C  CD1  . LEU   B 1 93  ? 40.854 -13.644 -1.823  1.00 10.72 ?  93   LEU   B CD1  1 
ATOM   5277 C  CD2  . LEU   B 1 93  ? 40.084 -15.616 -3.168  1.00 10.61 ?  93   LEU   B CD2  1 
ATOM   5278 H  H    . LEU   B 1 93  ? 44.899 -15.275 -3.860  1.00 10.85 ?  93   LEU   B H    1 
ATOM   5279 H  HA   . LEU   B 1 93  ? 43.679 -13.868 -1.908  1.00 11.08 ?  93   LEU   B HA   1 
ATOM   5280 H  HB2  . LEU   B 1 93  ? 42.409 -14.303 -3.820  1.00 11.48 ?  93   LEU   B HB2  1 
ATOM   5281 H  HB3  . LEU   B 1 93  ? 42.594 -15.860 -3.589  1.00 11.48 ?  93   LEU   B HB3  1 
ATOM   5282 H  HG   . LEU   B 1 93  ? 41.336 -15.607 -1.567  1.00 12.21 ?  93   LEU   B HG   1 
ATOM   5283 H  HD11 . LEU   B 1 93  ? 40.006 -13.688 -1.356  1.00 12.89 ?  93   LEU   B HD11 1 
ATOM   5284 H  HD12 . LEU   B 1 93  ? 41.551 -13.345 -1.215  1.00 12.89 ?  93   LEU   B HD12 1 
ATOM   5285 H  HD13 . LEU   B 1 93  ? 40.789 -13.036 -2.575  1.00 12.89 ?  93   LEU   B HD13 1 
ATOM   5286 H  HD21 . LEU   B 1 93  ? 39.268 -15.619 -2.642  1.00 12.76 ?  93   LEU   B HD21 1 
ATOM   5287 H  HD22 . LEU   B 1 93  ? 39.961 -15.071 -3.963  1.00 12.76 ?  93   LEU   B HD22 1 
ATOM   5288 H  HD23 . LEU   B 1 93  ? 40.315 -16.523 -3.424  1.00 12.76 ?  93   LEU   B HD23 1 
ATOM   5289 N  N    . HIS   B 1 94  ? 44.278 -15.358 -0.059  1.00 8.76  ?  94   HIS   B N    1 
ATOM   5290 C  CA   . HIS   B 1 94  ? 44.500 -16.260 1.062   1.00 9.20  ?  94   HIS   B CA   1 
ATOM   5291 C  C    . HIS   B 1 94  ? 43.142 -16.623 1.643   1.00 9.57  ?  94   HIS   B C    1 
ATOM   5292 O  O    . HIS   B 1 94  ? 42.470 -15.755 2.201   1.00 10.68 ?  94   HIS   B O    1 
ATOM   5293 C  CB   . HIS   B 1 94  ? 45.372 -15.578 2.116   1.00 9.43  ?  94   HIS   B CB   1 
ATOM   5294 C  CG   . HIS   B 1 94  ? 46.755 -15.279 1.644   1.00 9.25  ?  94   HIS   B CG   1 
ATOM   5295 N  ND1  . HIS   B 1 94  ? 47.782 -16.194 1.723   1.00 9.54  ?  94   HIS   B ND1  1 
ATOM   5296 C  CD2  . HIS   B 1 94  ? 47.263 -14.169 1.055   1.00 9.45  ?  94   HIS   B CD2  1 
ATOM   5297 C  CE1  . HIS   B 1 94  ? 48.868 -15.644 1.210   1.00 9.48  ?  94   HIS   B CE1  1 
ATOM   5298 N  NE2  . HIS   B 1 94  ? 48.583 -14.417 0.802   1.00 9.60  ?  94   HIS   B NE2  1 
ATOM   5299 H  H    . HIS   B 1 94  ? 44.351 -14.523 0.151   1.00 10.53 ?  94   HIS   B H    1 
ATOM   5300 H  HA   . HIS   B 1 94  ? 44.940 -17.067 0.758   1.00 11.06 ?  94   HIS   B HA   1 
ATOM   5301 H  HB2  . HIS   B 1 94  ? 44.959 -14.740 2.373   1.00 11.34 ?  94   HIS   B HB2  1 
ATOM   5302 H  HB3  . HIS   B 1 94  ? 45.443 -16.161 2.890   1.00 11.34 ?  94   HIS   B HB3  1 
ATOM   5303 H  HD2  . HIS   B 1 94  ? 46.809 -13.384 0.869   1.00 11.37 ?  94   HIS   B HD2  1 
ATOM   5304 H  HE1  . HIS   B 1 94  ? 49.702 -16.061 1.153   1.00 11.41 ?  94   HIS   B HE1  1 
ATOM   5305 H  HE2  . HIS   B 1 94  ? 49.143 -13.876 0.439   1.00 11.55 ?  94   HIS   B HE2  1 
ATOM   5306 N  N    . VAL   B 1 95  ? 42.709 -17.877 1.489   1.00 9.29  ?  95   VAL   B N    1 
ATOM   5307 C  CA   . VAL   B 1 95  ? 41.383 -18.319 1.920   1.00 9.46  ?  95   VAL   B CA   1 
ATOM   5308 C  C    . VAL   B 1 95  ? 41.556 -19.357 3.012   1.00 9.56  ?  95   VAL   B C    1 
ATOM   5309 O  O    . VAL   B 1 95  ? 42.327 -20.308 2.848   1.00 10.19 ?  95   VAL   B O    1 
ATOM   5310 C  CB   . VAL   B 1 95  ? 40.568 -18.919 0.759   1.00 9.74  ?  95   VAL   B CB   1 
ATOM   5311 C  CG1  . VAL   B 1 95  ? 39.192 -19.376 1.242   1.00 10.86 ?  95   VAL   B CG1  1 
ATOM   5312 C  CG2  . VAL   B 1 95  ? 40.448 -17.934 -0.371  1.00 9.88  ?  95   VAL   B CG2  1 
ATOM   5313 H  H    . VAL   B 1 95  ? 43.169 -18.501 1.119   1.00 11.18 ?  95   VAL   B H    1 
ATOM   5314 H  HA   . VAL   B 1 95  ? 40.887 -17.570 2.286   1.00 11.38 ?  95   VAL   B HA   1 
ATOM   5315 H  HB   . VAL   B 1 95  ? 41.032 -19.697 0.418   1.00 11.71 ?  95   VAL   B HB   1 
ATOM   5316 H  HG11 . VAL   B 1 95  ? 38.631 -19.572 0.468   1.00 13.06 ?  95   VAL   B HG11 1 
ATOM   5317 H  HG12 . VAL   B 1 95  ? 39.288 -20.177 1.781   1.00 13.06 ?  95   VAL   B HG12 1 
ATOM   5318 H  HG13 . VAL   B 1 95  ? 38.783 -18.669 1.766   1.00 13.06 ?  95   VAL   B HG13 1 
ATOM   5319 H  HG21 . VAL   B 1 95  ? 39.866 -18.305 -1.053  1.00 11.88 ?  95   VAL   B HG21 1 
ATOM   5320 H  HG22 . VAL   B 1 95  ? 40.067 -17.108 -0.028  1.00 11.88 ?  95   VAL   B HG22 1 
ATOM   5321 H  HG23 . VAL   B 1 95  ? 41.327 -17.767 -0.737  1.00 11.88 ?  95   VAL   B HG23 1 
ATOM   5322 N  N    . VAL   B 1 96  ? 40.827 -19.192 4.110   1.00 10.12 ?  96   VAL   B N    1 
ATOM   5323 C  CA   . VAL   B 1 96  ? 40.910 -20.112 5.241   1.00 10.39 ?  96   VAL   B CA   1 
ATOM   5324 C  C    . VAL   B 1 96  ? 39.721 -21.071 5.194   1.00 10.41 ?  96   VAL   B C    1 
ATOM   5325 O  O    . VAL   B 1 96  ? 38.604 -20.717 5.580   1.00 11.48 ?  96   VAL   B O    1 
ATOM   5326 C  CB   . VAL   B 1 96  ? 40.959 -19.369 6.578   1.00 11.37 ?  96   VAL   B CB   1 
ATOM   5327 C  CG1  . VAL   B 1 96  ? 41.139 -20.362 7.714   1.00 11.96 ?  96   VAL   B CG1  1 
ATOM   5328 C  CG2  . VAL   B 1 96  ? 42.069 -18.329 6.588   1.00 12.28 ?  96   VAL   B CG2  1 
ATOM   5329 H  H    . VAL   B 1 96  ? 40.269 -18.551 4.228   1.00 12.18 ?  96   VAL   B H    1 
ATOM   5330 H  HA   . VAL   B 1 96  ? 41.727 -20.637 5.167   1.00 12.49 ?  96   VAL   B HA   1 
ATOM   5331 H  HB   . VAL   B 1 96  ? 40.115 -18.911 6.717   1.00 13.67 ?  96   VAL   B HB   1 
ATOM   5332 H  HG11 . VAL   B 1 96  ? 41.334 -19.877 8.534   1.00 14.38 ?  96   VAL   B HG11 1 
ATOM   5333 H  HG12 . VAL   B 1 96  ? 40.327 -20.879 7.825   1.00 14.38 ?  96   VAL   B HG12 1 
ATOM   5334 H  HG13 . VAL   B 1 96  ? 41.882 -20.954 7.505   1.00 14.38 ?  96   VAL   B HG13 1 
ATOM   5335 H  HG21 . VAL   B 1 96  ? 42.120 -17.925 7.472   1.00 14.76 ?  96   VAL   B HG21 1 
ATOM   5336 H  HG22 . VAL   B 1 96  ? 42.911 -18.758 6.375   1.00 14.76 ?  96   VAL   B HG22 1 
ATOM   5337 H  HG23 . VAL   B 1 96  ? 41.870 -17.644 5.929   1.00 14.76 ?  96   VAL   B HG23 1 
ATOM   5338 N  N    . GLY   B 1 97  ? 39.954 -22.306 4.754   1.00 10.78 ?  97   GLY   B N    1 
ATOM   5339 C  CA   . GLY   B 1 97  ? 38.976 -23.359 4.920   1.00 11.27 ?  97   GLY   B CA   1 
ATOM   5340 C  C    . GLY   B 1 97  ? 39.105 -23.974 6.295   1.00 12.08 ?  97   GLY   B C    1 
ATOM   5341 O  O    . GLY   B 1 97  ? 40.151 -23.860 6.947   1.00 12.59 ?  97   GLY   B O    1 
ATOM   5342 H  H    . GLY   B 1 97  ? 40.677 -22.549 4.348   1.00 12.96 ?  97   GLY   B H    1 
ATOM   5343 H  HA2  . GLY   B 1 97  ? 38.084 -22.986 4.810   1.00 13.55 ?  97   GLY   B HA2  1 
ATOM   5344 H  HA3  . GLY   B 1 97  ? 39.112 -24.043 4.247   1.00 13.55 ?  97   GLY   B HA3  1 
ATOM   5345 N  N    . PRO   B 1 98  ? 38.059 -24.660 6.756   1.00 12.86 ?  98   PRO   B N    1 
ATOM   5346 C  CA   . PRO   B 1 98  ? 38.149 -25.357 8.042   1.00 13.75 ?  98   PRO   B CA   1 
ATOM   5347 C  C    . PRO   B 1 98  ? 39.175 -26.478 7.997   1.00 13.46 ?  98   PRO   B C    1 
ATOM   5348 O  O    . PRO   B 1 98  ? 39.282 -27.209 7.014   1.00 13.61 ?  98   PRO   B O    1 
ATOM   5349 C  CB   . PRO   B 1 98  ? 36.729 -25.901 8.244   1.00 14.36 ?  98   PRO   B CB   1 
ATOM   5350 C  CG   . PRO   B 1 98  ? 36.180 -26.045 6.863   1.00 13.83 ?  98   PRO   B CG   1 
ATOM   5351 C  CD   . PRO   B 1 98  ? 36.744 -24.854 6.118   1.00 13.07 ?  98   PRO   B CD   1 
ATOM   5352 H  HA   . PRO   B 1 98  ? 38.366 -24.737 8.750   1.00 16.53 ?  98   PRO   B HA   1 
ATOM   5353 H  HB2  . PRO   B 1 98  ? 36.768 -26.764 8.687   1.00 17.26 ?  98   PRO   B HB2  1 
ATOM   5354 H  HB3  . PRO   B 1 98  ? 36.204 -25.271 8.754   1.00 17.26 ?  98   PRO   B HB3  1 
ATOM   5355 H  HG2  . PRO   B 1 98  ? 36.493 -26.880 6.471   1.00 16.63 ?  98   PRO   B HG2  1 
ATOM   5356 H  HG3  . PRO   B 1 98  ? 35.215 -26.015 6.886   1.00 16.63 ?  98   PRO   B HG3  1 
ATOM   5357 H  HD2  . PRO   B 1 98  ? 36.850 -25.066 5.171   1.00 15.71 ?  98   PRO   B HD2  1 
ATOM   5358 H  HD3  . PRO   B 1 98  ? 36.187 -24.075 6.245   1.00 15.71 ?  98   PRO   B HD3  1 
ATOM   5359 N  N    . ASN   B 1 99  ? 39.925 -26.609 9.084   1.00 14.48 ?  99   ASN   B N    1 
ATOM   5360 C  CA   . ASN   B 1 99  ? 40.903 -27.681 9.241   1.00 15.13 ?  99   ASN   B CA   1 
ATOM   5361 C  C    . ASN   B 1 99  ? 40.273 -28.766 10.114  1.00 17.31 ?  99   ASN   B C    1 
ATOM   5362 O  O    . ASN   B 1 99  ? 40.182 -28.622 11.335  1.00 17.92 ?  99   ASN   B O    1 
ATOM   5363 C  CB   . ASN   B 1 99  ? 42.178 -27.123 9.856   1.00 15.54 ?  99   ASN   B CB   1 
ATOM   5364 C  CG   . ASN   B 1 99  ? 43.307 -28.128 9.861   1.00 16.49 ?  99   ASN   B CG   1 
ATOM   5365 O  OD1  . ASN   B 1 99  ? 43.080 -29.322 10.016  1.00 17.54 ?  99   ASN   B OD1  1 
ATOM   5366 N  ND2  . ASN   B 1 99  ? 44.528 -27.652 9.681   1.00 16.85 ?  99   ASN   B ND2  1 
ATOM   5367 H  H    . ASN   B 1 99  ? 39.883 -26.078 9.759   1.00 17.40 ?  99   ASN   B H    1 
ATOM   5368 H  HA   . ASN   B 1 99  ? 41.113 -28.065 8.378   1.00 18.18 ?  99   ASN   B HA   1 
ATOM   5369 H  HB2  . ASN   B 1 99  ? 42.463 -26.354 9.349   1.00 18.68 ?  99   ASN   B HB2  1 
ATOM   5370 H  HB3  . ASN   B 1 99  ? 41.996 -26.867 10.778  1.00 18.68 ?  99   ASN   B HB3  1 
ATOM   5371 H  HD21 . ASN   B 1 99  ? 45.200 -28.187 9.677   1.00 20.25 ?  99   ASN   B HD21 1 
ATOM   5372 H  HD22 . ASN   B 1 99  ? 44.643 -26.809 9.573   1.00 20.25 ?  99   ASN   B HD22 1 
ATOM   5373 N  N    A VAL   B 1 100 ? 39.821 -29.851 9.478   0.60 19.16 ?  100  VAL   B N    1 
ATOM   5374 N  N    B VAL   B 1 100 ? 39.824 -29.850 9.472   0.40 19.25 ?  100  VAL   B N    1 
ATOM   5375 C  CA   A VAL   B 1 100 ? 39.208 -30.950 10.222  0.60 21.84 ?  100  VAL   B CA   1 
ATOM   5376 C  CA   B VAL   B 1 100 ? 39.211 -30.961 10.197  0.40 21.66 ?  100  VAL   B CA   1 
ATOM   5377 C  C    A VAL   B 1 100 ? 40.218 -31.602 11.157  0.60 22.47 ?  100  VAL   B C    1 
ATOM   5378 C  C    B VAL   B 1 100 ? 40.213 -31.617 11.139  0.40 22.40 ?  100  VAL   B C    1 
ATOM   5379 O  O    A VAL   B 1 100 ? 39.854 -32.087 12.236  0.60 23.13 ?  100  VAL   B O    1 
ATOM   5380 O  O    B VAL   B 1 100 ? 39.838 -32.116 12.208  0.40 22.82 ?  100  VAL   B O    1 
ATOM   5381 C  CB   A VAL   B 1 100 ? 38.571 -31.967 9.252   0.60 24.22 ?  100  VAL   B CB   1 
ATOM   5382 C  CB   B VAL   B 1 100 ? 38.601 -31.969 9.200   0.40 23.48 ?  100  VAL   B CB   1 
ATOM   5383 C  CG1  A VAL   B 1 100 ? 38.083 -33.197 10.006  0.60 25.13 ?  100  VAL   B CG1  1 
ATOM   5384 C  CG1  B VAL   B 1 100 ? 38.088 -33.206 9.924   0.40 24.18 ?  100  VAL   B CG1  1 
ATOM   5385 C  CG2  A VAL   B 1 100 ? 37.423 -31.323 8.491   0.60 24.90 ?  100  VAL   B CG2  1 
ATOM   5386 C  CG2  B VAL   B 1 100 ? 37.478 -31.314 8.408   0.40 24.00 ?  100  VAL   B CG2  1 
ATOM   5387 H  H    A VAL   B 1 100 ? 39.857 -29.972 8.628   0.60 23.02 ?  100  VAL   B H    1 
ATOM   5388 H  H    B VAL   B 1 100 ? 39.857 -29.961 8.619   0.40 23.12 ?  100  VAL   B H    1 
ATOM   5389 H  HA   A VAL   B 1 100 ? 38.492 -30.590 10.768  0.60 26.23 ?  100  VAL   B HA   1 
ATOM   5390 H  HA   B VAL   B 1 100 ? 38.485 -30.617 10.737  0.40 26.02 ?  100  VAL   B HA   1 
ATOM   5391 H  HB   A VAL   B 1 100 ? 39.238 -32.256 8.610   0.60 29.09 ?  100  VAL   B HB   1 
ATOM   5392 H  HB   B VAL   B 1 100 ? 39.284 -32.253 8.573   0.40 28.20 ?  100  VAL   B HB   1 
ATOM   5393 H  HG11 A VAL   B 1 100 ? 37.494 -33.710 9.427   0.60 30.19 ?  100  VAL   B HG11 1 
ATOM   5394 H  HG11 B VAL   B 1 100 ? 37.523 -33.715 9.319   0.40 29.05 ?  100  VAL   B HG11 1 
ATOM   5395 H  HG12 A VAL   B 1 100 ? 38.845 -33.742 10.261  0.60 30.19 ?  100  VAL   B HG12 1 
ATOM   5396 H  HG12 B VAL   B 1 100 ? 38.842 -33.750 10.202  0.40 29.05 ?  100  VAL   B HG12 1 
ATOM   5397 H  HG13 A VAL   B 1 100 ? 37.598 -32.914 10.798  0.60 30.19 ?  100  VAL   B HG13 1 
ATOM   5398 H  HG13 B VAL   B 1 100 ? 37.573 -32.930 10.698  0.40 29.05 ?  100  VAL   B HG13 1 
ATOM   5399 H  HG21 A VAL   B 1 100 ? 37.048 -31.974 7.877   0.60 29.90 ?  100  VAL   B HG21 1 
ATOM   5400 H  HG21 B VAL   B 1 100 ? 37.101 -31.966 7.797   0.40 28.83 ?  100  VAL   B HG21 1 
ATOM   5401 H  HG22 A VAL   B 1 100 ? 36.746 -31.038 9.125   0.60 29.90 ?  100  VAL   B HG22 1 
ATOM   5402 H  HG22 B VAL   B 1 100 ? 36.796 -31.006 9.026   0.40 28.83 ?  100  VAL   B HG22 1 
ATOM   5403 H  HG23 A VAL   B 1 100 ? 37.761 -30.560 8.000   0.60 29.90 ?  100  VAL   B HG23 1 
ATOM   5404 H  HG23 B VAL   B 1 100 ? 37.839 -30.564 7.912   0.40 28.83 ?  100  VAL   B HG23 1 
ATOM   5405 N  N    . ASN   B 1 101 ? 41.494 -31.642 10.761  1.00 23.00 ?  101  ASN   B N    1 
ATOM   5406 C  CA   . ASN   B 1 101 ? 42.530 -32.167 11.649  1.00 25.27 ?  101  ASN   B CA   1 
ATOM   5407 C  C    . ASN   B 1 101 ? 42.693 -31.327 12.911  1.00 27.93 ?  101  ASN   B C    1 
ATOM   5408 O  O    . ASN   B 1 101 ? 43.287 -31.803 13.887  1.00 28.70 ?  101  ASN   B O    1 
ATOM   5409 C  CB   . ASN   B 1 101 ? 43.861 -32.291 10.900  1.00 25.10 ?  101  ASN   B CB   1 
ATOM   5410 C  CG   . ASN   B 1 101 ? 43.852 -33.417 9.884   1.00 24.72 ?  101  ASN   B CG   1 
ATOM   5411 O  OD1  . ASN   B 1 101 ? 43.177 -34.425 10.073  1.00 25.61 ?  101  ASN   B OD1  1 
ATOM   5412 N  ND2  . ASN   B 1 101 ? 44.594 -33.248 8.798   1.00 24.29 ?  101  ASN   B ND2  1 
ATOM   5413 H  H    A ASN   B 1 101 ? 41.771 -31.392 9.987   0.60 27.63 ?  101  ASN   B H    1 
ATOM   5414 H  H    B ASN   B 1 101 ? 41.779 -31.375 9.995   0.40 27.63 ?  101  ASN   B H    1 
ATOM   5415 H  HA   . ASN   B 1 101 ? 42.275 -33.054 11.930  1.00 30.35 ?  101  ASN   B HA   1 
ATOM   5416 H  HB2  . ASN   B 1 101 ? 44.047 -31.466 10.425  1.00 30.15 ?  101  ASN   B HB2  1 
ATOM   5417 H  HB3  . ASN   B 1 101 ? 44.570 -32.471 11.538  1.00 30.15 ?  101  ASN   B HB3  1 
ATOM   5418 H  HD21 . ASN   B 1 101 ? 44.621 -33.861 8.194   1.00 29.18 ?  101  ASN   B HD21 1 
ATOM   5419 H  HD22 . ASN   B 1 101 ? 45.051 -32.527 8.697   1.00 29.18 ?  101  ASN   B HD22 1 
ATOM   5420 N  N    A LYS   B 1 102 ? 42.198 -30.088 12.906  0.60 29.30 ?  102  LYS   B N    1 
ATOM   5421 N  N    B LYS   B 1 102 ? 42.171 -30.099 12.918  0.40 29.29 ?  102  LYS   B N    1 
ATOM   5422 C  CA   A LYS   B 1 102 ? 42.207 -29.223 14.079  0.60 31.10 ?  102  LYS   B CA   1 
ATOM   5423 C  CA   B LYS   B 1 102 ? 42.132 -29.262 14.111  0.40 30.86 ?  102  LYS   B CA   1 
ATOM   5424 C  C    A LYS   B 1 102 ? 40.851 -29.172 14.770  0.60 30.48 ?  102  LYS   B C    1 
ATOM   5425 C  C    B LYS   B 1 102 ? 40.758 -29.242 14.769  0.40 30.37 ?  102  LYS   B C    1 
ATOM   5426 O  O    A LYS   B 1 102 ? 40.656 -28.347 15.668  0.60 30.88 ?  102  LYS   B O    1 
ATOM   5427 O  O    B LYS   B 1 102 ? 40.559 -28.494 15.731  0.40 30.64 ?  102  LYS   B O    1 
ATOM   5428 C  CB   A LYS   B 1 102 ? 42.621 -27.800 13.695  0.60 33.63 ?  102  LYS   B CB   1 
ATOM   5429 C  CB   B LYS   B 1 102 ? 42.544 -27.825 13.773  0.40 32.96 ?  102  LYS   B CB   1 
ATOM   5430 C  CG   A LYS   B 1 102 ? 44.095 -27.611 13.381  0.60 35.99 ?  102  LYS   B CG   1 
ATOM   5431 C  CG   B LYS   B 1 102 ? 44.004 -27.649 13.392  0.40 34.89 ?  102  LYS   B CG   1 
ATOM   5432 C  CD   A LYS   B 1 102 ? 44.375 -26.157 13.024  0.60 38.10 ?  102  LYS   B CD   1 
ATOM   5433 C  CD   B LYS   B 1 102 ? 44.277 -26.214 12.969  0.40 36.57 ?  102  LYS   B CD   1 
ATOM   5434 C  CE   A LYS   B 1 102 ? 45.849 -25.905 12.759  0.60 39.71 ?  102  LYS   B CE   1 
ATOM   5435 C  CE   B LYS   B 1 102 ? 45.753 -25.974 12.713  0.40 37.84 ?  102  LYS   B CE   1 
ATOM   5436 N  NZ   A LYS   B 1 102 ? 46.100 -24.486 12.372  0.60 40.61 ?  102  LYS   B NZ   1 
ATOM   5437 N  NZ   B LYS   B 1 102 ? 46.012 -24.579 12.260  0.40 38.54 ?  102  LYS   B NZ   1 
ATOM   5438 H  H    A LYS   B 1 102 ? 41.835 -29.718 12.217  0.60 35.18 ?  102  LYS   B H    1 
ATOM   5439 H  H    B LYS   B 1 102 ? 41.820 -29.721 12.229  0.40 35.18 ?  102  LYS   B H    1 
ATOM   5440 H  HA   A LYS   B 1 102 ? 42.864 -29.560 14.709  0.60 37.35 ?  102  LYS   B HA   1 
ATOM   5441 H  HA   B LYS   B 1 102 ? 42.769 -29.605 14.755  0.40 37.06 ?  102  LYS   B HA   1 
ATOM   5442 H  HB2  A LYS   B 1 102 ? 42.118 -27.534 12.911  0.60 40.38 ?  102  LYS   B HB2  1 
ATOM   5443 H  HB2  B LYS   B 1 102 ? 42.008 -27.515 13.029  0.40 39.58 ?  102  LYS   B HB2  1 
ATOM   5444 H  HB3  A LYS   B 1 102 ? 42.405 -27.207 14.433  0.60 40.38 ?  102  LYS   B HB3  1 
ATOM   5445 H  HB3  B LYS   B 1 102 ? 42.377 -27.266 14.550  0.40 39.58 ?  102  LYS   B HB3  1 
ATOM   5446 H  HG2  A LYS   B 1 102 ? 44.626 -27.844 14.159  0.60 43.21 ?  102  LYS   B HG2  1 
ATOM   5447 H  HG2  B LYS   B 1 102 ? 44.568 -27.853 14.156  0.40 41.89 ?  102  LYS   B HG2  1 
ATOM   5448 H  HG3  A LYS   B 1 102 ? 44.340 -28.166 12.624  0.60 43.21 ?  102  LYS   B HG3  1 
ATOM   5449 H  HG3  B LYS   B 1 102 ? 44.218 -28.233 12.648  0.40 41.89 ?  102  LYS   B HG3  1 
ATOM   5450 H  HD2  A LYS   B 1 102 ? 43.879 -25.925 12.222  0.60 45.75 ?  102  LYS   B HD2  1 
ATOM   5451 H  HD2  B LYS   B 1 102 ? 43.792 -26.025 12.149  0.40 43.92 ?  102  LYS   B HD2  1 
ATOM   5452 H  HD3  A LYS   B 1 102 ? 44.099 -25.589 13.761  0.60 45.75 ?  102  LYS   B HD3  1 
ATOM   5453 H  HD3  B LYS   B 1 102 ? 43.988 -25.612 13.673  0.40 43.92 ?  102  LYS   B HD3  1 
ATOM   5454 H  HE2  A LYS   B 1 102 ? 46.356 -26.095 13.564  0.60 47.68 ?  102  LYS   B HE2  1 
ATOM   5455 H  HE2  B LYS   B 1 102 ? 46.248 -26.124 13.534  0.40 45.43 ?  102  LYS   B HE2  1 
ATOM   5456 H  HE3  A LYS   B 1 102 ? 46.146 -26.475 12.033  0.60 47.68 ?  102  LYS   B HE3  1 
ATOM   5457 H  HE3  B LYS   B 1 102 ? 46.060 -26.580 12.021  0.40 45.43 ?  102  LYS   B HE3  1 
ATOM   5458 H  HZ1  A LYS   B 1 102 ? 46.968 -24.361 12.222  0.60 48.76 ?  102  LYS   B HZ1  1 
ATOM   5459 H  HZ1  B LYS   B 1 102 ? 46.883 -24.463 12.117  0.40 46.28 ?  102  LYS   B HZ1  1 
ATOM   5460 H  HZ2  A LYS   B 1 102 ? 45.647 -24.288 11.632  0.60 48.76 ?  102  LYS   B HZ2  1 
ATOM   5461 H  HZ2  B LYS   B 1 102 ? 45.571 -24.418 11.504  0.40 46.28 ?  102  LYS   B HZ2  1 
ATOM   5462 H  HZ3  A LYS   B 1 102 ? 45.838 -23.942 13.026  0.60 48.76 ?  102  LYS   B HZ3  1 
ATOM   5463 H  HZ3  B LYS   B 1 102 ? 45.741 -24.002 12.882  0.40 46.28 ?  102  LYS   B HZ3  1 
ATOM   5464 N  N    A GLY   B 1 103 ? 39.906 -30.014 14.359  0.60 29.76 ?  103  GLY   B N    1 
ATOM   5465 N  N    B GLY   B 1 103 ? 39.808 -30.030 14.271  0.40 29.65 ?  103  GLY   B N    1 
ATOM   5466 C  CA   A GLY   B 1 103 ? 38.588 -30.043 14.957  0.60 29.55 ?  103  GLY   B CA   1 
ATOM   5467 C  CA   B GLY   B 1 103 ? 38.485 -30.091 14.858  0.40 29.12 ?  103  GLY   B CA   1 
ATOM   5468 C  C    A GLY   B 1 103 ? 37.627 -28.992 14.449  0.60 28.87 ?  103  GLY   B C    1 
ATOM   5469 C  C    B GLY   B 1 103 ? 37.529 -29.009 14.413  0.40 28.28 ?  103  GLY   B C    1 
ATOM   5470 O  O    A GLY   B 1 103 ? 36.495 -28.922 14.945  0.60 29.60 ?  103  GLY   B O    1 
ATOM   5471 O  O    B GLY   B 1 103 ? 36.479 -28.836 15.043  0.40 28.78 ?  103  GLY   B O    1 
ATOM   5472 H  H    A GLY   B 1 103 ? 40.011 -30.582 13.724  0.60 35.74 ?  103  GLY   B H    1 
ATOM   5473 H  H    B GLY   B 1 103 ? 39.911 -30.542 13.588  0.40 35.61 ?  103  GLY   B H    1 
ATOM   5474 H  HA2  A GLY   B 1 103 ? 38.189 -30.910 14.791  0.60 35.48 ?  103  GLY   B HA2  1 
ATOM   5475 H  HA2  B GLY   B 1 103 ? 38.086 -30.946 14.640  0.40 34.97 ?  103  GLY   B HA2  1 
ATOM   5476 H  HA3  A GLY   B 1 103 ? 38.678 -29.936 15.919  0.60 35.48 ?  103  GLY   B HA3  1 
ATOM   5477 H  HA3  B GLY   B 1 103 ? 38.570 -30.039 15.824  0.40 34.97 ?  103  GLY   B HA3  1 
ATOM   5478 N  N    A GLU   B 1 104 ? 38.030 -28.180 13.475  0.60 27.38 ?  104  GLU   B N    1 
ATOM   5479 N  N    B GLU   B 1 104 ? 37.847 -28.280 13.347  0.40 26.80 ?  104  GLU   B N    1 
ATOM   5480 C  CA   A GLU   B 1 104 ? 37.181 -27.099 13.000  0.60 25.85 ?  104  GLU   B CA   1 
ATOM   5481 C  CA   B GLU   B 1 104 ? 37.006 -27.180 12.904  0.40 25.34 ?  104  GLU   B CA   1 
ATOM   5482 C  C    A GLU   B 1 104 ? 36.003 -27.649 12.195  0.60 26.44 ?  104  GLU   B C    1 
ATOM   5483 C  C    B GLU   B 1 104 ? 35.854 -27.692 12.045  0.40 25.37 ?  104  GLU   B C    1 
ATOM   5484 O  O    A GLU   B 1 104 ? 36.048 -28.751 11.639  0.60 27.36 ?  104  GLU   B O    1 
ATOM   5485 O  O    B GLU   B 1 104 ? 35.961 -28.719 11.366  0.40 25.67 ?  104  GLU   B O    1 
ATOM   5486 C  CB   A GLU   B 1 104 ? 38.006 -26.103 12.185  0.60 24.47 ?  104  GLU   B CB   1 
ATOM   5487 C  CB   B GLU   B 1 104 ? 37.845 -26.157 12.139  0.40 24.08 ?  104  GLU   B CB   1 
ATOM   5488 C  CG   A GLU   B 1 104 ? 39.108 -25.457 13.014  0.60 23.37 ?  104  GLU   B CG   1 
ATOM   5489 C  CG   B GLU   B 1 104 ? 38.945 -25.555 13.003  0.40 22.98 ?  104  GLU   B CG   1 
ATOM   5490 C  CD   A GLU   B 1 104 ? 40.030 -24.566 12.211  0.60 22.17 ?  104  GLU   B CD   1 
ATOM   5491 C  CD   B GLU   B 1 104 ? 39.895 -24.655 12.241  0.40 21.92 ?  104  GLU   B CD   1 
ATOM   5492 O  OE1  A GLU   B 1 104 ? 40.009 -24.627 10.963  0.60 20.25 ?  104  GLU   B OE1  1 
ATOM   5493 O  OE1  B GLU   B 1 104 ? 39.854 -24.635 10.993  0.40 21.07 ?  104  GLU   B OE1  1 
ATOM   5494 O  OE2  A GLU   B 1 104 ? 40.781 -23.795 12.843  0.60 23.04 -1 104  GLU   B OE2  1 
ATOM   5495 O  OE2  B GLU   B 1 104 ? 40.690 -23.963 12.908  0.40 21.76 -1 104  GLU   B OE2  1 
ATOM   5496 H  H    A GLU   B 1 104 ? 38.791 -28.235 13.079  0.60 32.88 ?  104  GLU   B H    1 
ATOM   5497 H  H    B GLU   B 1 104 ? 38.549 -28.403 12.867  0.40 32.19 ?  104  GLU   B H    1 
ATOM   5498 H  HA   A GLU   B 1 104 ? 36.824 -26.624 13.768  0.60 31.05 ?  104  GLU   B HA   1 
ATOM   5499 H  HA   B GLU   B 1 104 ? 36.630 -26.738 13.682  0.40 30.43 ?  104  GLU   B HA   1 
ATOM   5500 H  HB2  A GLU   B 1 104 ? 38.422 -26.565 11.441  0.60 29.39 ?  104  GLU   B HB2  1 
ATOM   5501 H  HB2  B GLU   B 1 104 ? 38.260 -26.592 11.379  0.40 28.92 ?  104  GLU   B HB2  1 
ATOM   5502 H  HB3  A GLU   B 1 104 ? 37.424 -25.399 11.858  0.60 29.39 ?  104  GLU   B HB3  1 
ATOM   5503 H  HB3  B GLU   B 1 104 ? 37.269 -25.436 11.839  0.40 28.92 ?  104  GLU   B HB3  1 
ATOM   5504 H  HG2  A GLU   B 1 104 ? 38.705 -24.905 13.704  0.60 28.07 ?  104  GLU   B HG2  1 
ATOM   5505 H  HG2  B GLU   B 1 104 ? 38.537 -25.024 13.705  0.40 27.60 ?  104  GLU   B HG2  1 
ATOM   5506 H  HG3  A GLU   B 1 104 ? 39.647 -26.151 13.425  0.60 28.07 ?  104  GLU   B HG3  1 
ATOM   5507 H  HG3  B GLU   B 1 104 ? 39.466 -26.274 13.396  0.40 27.60 ?  104  GLU   B HG3  1 
ATOM   5508 N  N    A ASP   B 1 105 ? 34.934 -26.856 12.147  0.60 26.47 ?  105  ASP   B N    1 
ATOM   5509 N  N    B ASP   B 1 105 ? 34.743 -26.961 12.084  0.40 25.24 ?  105  ASP   B N    1 
ATOM   5510 C  CA   A ASP   B 1 105 ? 33.653 -27.310 11.617  0.60 27.02 ?  105  ASP   B CA   1 
ATOM   5511 C  CA   B ASP   B 1 105 ? 33.496 -27.440 11.501  0.40 25.55 ?  105  ASP   B CA   1 
ATOM   5512 C  C    A ASP   B 1 105 ? 33.696 -27.358 10.094  0.60 25.36 ?  105  ASP   B C    1 
ATOM   5513 C  C    B ASP   B 1 105 ? 33.588 -27.446 9.979   0.40 24.54 ?  105  ASP   B C    1 
ATOM   5514 O  O    A ASP   B 1 105 ? 33.868 -26.326 9.437   0.60 24.83 ?  105  ASP   B O    1 
ATOM   5515 O  O    B ASP   B 1 105 ? 33.775 -26.397 9.353   0.40 23.96 ?  105  ASP   B O    1 
ATOM   5516 C  CB   A ASP   B 1 105 ? 32.548 -26.367 12.088  0.60 29.71 ?  105  ASP   B CB   1 
ATOM   5517 C  CB   B ASP   B 1 105 ? 32.336 -26.560 11.962  0.40 26.85 ?  105  ASP   B CB   1 
ATOM   5518 C  CG   A ASP   B 1 105 ? 31.171 -26.797 11.621  0.60 31.94 ?  105  ASP   B CG   1 
ATOM   5519 C  CG   B ASP   B 1 105 ? 30.982 -27.163 11.638  0.40 27.87 ?  105  ASP   B CG   1 
ATOM   5520 O  OD1  A ASP   B 1 105 ? 31.039 -27.919 11.089  0.60 32.35 ?  105  ASP   B OD1  1 
ATOM   5521 O  OD1  B ASP   B 1 105 ? 30.934 -28.142 10.864  0.40 28.13 ?  105  ASP   B OD1  1 
ATOM   5522 O  OD2  A ASP   B 1 105 ? 30.218 -26.002 11.777  0.60 33.27 -1 105  ASP   B OD2  1 
ATOM   5523 O  OD2  B ASP   B 1 105 ? 29.964 -26.665 12.166  0.40 28.02 -1 105  ASP   B OD2  1 
ATOM   5524 H  H    A ASP   B 1 105 ? 34.930 -26.040 12.419  0.60 31.79 ?  105  ASP   B H    1 
ATOM   5525 H  H    B ASP   B 1 105 ? 34.687 -26.181 12.442  0.40 30.32 ?  105  ASP   B H    1 
ATOM   5526 H  HA   A ASP   B 1 105 ? 33.464 -28.201 11.953  0.60 32.45 ?  105  ASP   B HA   1 
ATOM   5527 H  HA   B ASP   B 1 105 ? 33.326 -28.347 11.800  0.40 30.68 ?  105  ASP   B HA   1 
ATOM   5528 H  HB2  A ASP   B 1 105 ? 32.565 -26.322 13.060  0.60 35.68 ?  105  ASP   B HB2  1 
ATOM   5529 H  HB2  B ASP   B 1 105 ? 32.394 -26.439 12.924  0.40 32.24 ?  105  ASP   B HB2  1 
ATOM   5530 H  HB3  A ASP   B 1 105 ? 32.702 -25.489 11.714  0.60 35.68 ?  105  ASP   B HB3  1 
ATOM   5531 H  HB3  B ASP   B 1 105 ? 32.397 -25.698 11.518  0.40 32.24 ?  105  ASP   B HB3  1 
ATOM   5532 N  N    A ILE   B 1 106 ? 33.508 -28.558 9.537   0.60 24.69 ?  106  ILE   B N    1 
ATOM   5533 N  N    B ILE   B 1 106 ? 33.438 -28.635 9.387   0.40 24.19 ?  106  ILE   B N    1 
ATOM   5534 C  CA   A ILE   B 1 106 ? 33.509 -28.739 8.089   0.60 23.89 ?  106  ILE   B CA   1 
ATOM   5535 C  CA   B ILE   B 1 106 ? 33.454 -28.776 7.936   0.40 23.91 ?  106  ILE   B CA   1 
ATOM   5536 C  C    A ILE   B 1 106 ? 32.410 -27.924 7.414   0.60 22.73 ?  106  ILE   B C    1 
ATOM   5537 C  C    B ILE   B 1 106 ? 32.357 -27.947 7.279   0.40 23.39 ?  106  ILE   B C    1 
ATOM   5538 O  O    A ILE   B 1 106 ? 32.518 -27.606 6.224   0.60 22.07 ?  106  ILE   B O    1 
ATOM   5539 O  O    B ILE   B 1 106 ? 32.445 -27.637 6.086   0.40 22.94 ?  106  ILE   B O    1 
ATOM   5540 C  CB   A ILE   B 1 106 ? 33.421 -30.248 7.758   0.60 24.61 ?  106  ILE   B CB   1 
ATOM   5541 C  CB   B ILE   B 1 106 ? 33.358 -30.274 7.564   0.40 24.41 ?  106  ILE   B CB   1 
ATOM   5542 C  CG1  A ILE   B 1 106 ? 33.659 -30.499 6.268   0.60 24.99 ?  106  ILE   B CG1  1 
ATOM   5543 C  CG1  B ILE   B 1 106 ? 33.639 -30.489 6.075   0.40 24.70 ?  106  ILE   B CG1  1 
ATOM   5544 C  CG2  A ILE   B 1 106 ? 32.075 -30.818 8.193   0.60 25.15 ?  106  ILE   B CG2  1 
ATOM   5545 C  CG2  B ILE   B 1 106 ? 31.992 -30.835 7.937   0.40 24.78 ?  106  ILE   B CG2  1 
ATOM   5546 C  CD1  A ILE   B 1 106 ? 35.020 -30.050 5.789   0.60 25.06 ?  106  ILE   B CD1  1 
ATOM   5547 C  CD1  B ILE   B 1 106 ? 35.013 -30.030 5.647   0.40 24.83 ?  106  ILE   B CD1  1 
ATOM   5548 H  H    A ILE   B 1 106 ? 33.381 -29.282 9.982   0.60 29.65 ?  106  ILE   B H    1 
ATOM   5549 H  H    B ILE   B 1 106 ? 33.332 -29.374 9.809   0.40 29.06 ?  106  ILE   B H    1 
ATOM   5550 H  HA   A ILE   B 1 106 ? 34.354 -28.415 7.751   0.60 28.70 ?  106  ILE   B HA   1 
ATOM   5551 H  HA   B ILE   B 1 106 ? 34.301 -28.443 7.610   0.40 28.72 ?  106  ILE   B HA   1 
ATOM   5552 H  HB   A ILE   B 1 106 ? 34.115 -30.710 8.255   0.60 29.56 ?  106  ILE   B HB   1 
ATOM   5553 H  HB   B ILE   B 1 106 ? 34.030 -30.756 8.071   0.40 29.32 ?  106  ILE   B HB   1 
ATOM   5554 H  HG12 A ILE   B 1 106 ? 33.588 -31.453 6.096   0.60 30.01 ?  106  ILE   B HG12 1 
ATOM   5555 H  HG12 B ILE   B 1 106 ? 33.572 -31.438 5.878   0.40 29.66 ?  106  ILE   B HG12 1 
ATOM   5556 H  HG13 A ILE   B 1 106 ? 32.990 -30.024 5.755   0.60 30.01 ?  106  ILE   B HG13 1 
ATOM   5557 H  HG13 B ILE   B 1 106 ? 32.985 -30.000 5.555   0.40 29.66 ?  106  ILE   B HG13 1 
ATOM   5558 H  HG21 A ILE   B 1 106 ? 32.090 -31.782 8.084   0.60 30.21 ?  106  ILE   B HG21 1 
ATOM   5559 H  HG21 B ILE   B 1 106 ? 32.010 -31.800 7.840   0.40 29.77 ?  106  ILE   B HG21 1 
ATOM   5560 H  HG22 A ILE   B 1 106 ? 31.924 -30.595 9.126   0.60 30.21 ?  106  ILE   B HG22 1 
ATOM   5561 H  HG22 B ILE   B 1 106 ? 31.796 -30.600 8.858   0.40 29.77 ?  106  ILE   B HG22 1 
ATOM   5562 H  HG23 A ILE   B 1 106 ? 31.375 -30.434 7.644   0.60 30.21 ?  106  ILE   B HG23 1 
ATOM   5563 H  HG23 B ILE   B 1 106 ? 31.321 -30.456 7.350   0.40 29.77 ?  106  ILE   B HG23 1 
ATOM   5564 H  HD11 A ILE   B 1 106 ? 35.194 -30.442 4.920   0.60 30.10 ?  106  ILE   B HD11 1 
ATOM   5565 H  HD11 B ILE   B 1 106 ? 35.219 -30.418 4.783   0.40 29.83 ?  106  ILE   B HD11 1 
ATOM   5566 H  HD12 A ILE   B 1 106 ? 35.029 -29.082 5.723   0.60 30.10 ?  106  ILE   B HD12 1 
ATOM   5567 H  HD12 B ILE   B 1 106 ? 35.018 -29.062 5.585   0.40 29.83 ?  106  ILE   B HD12 1 
ATOM   5568 H  HD13 A ILE   B 1 106 ? 35.692 -30.345 6.425   0.60 30.10 ?  106  ILE   B HD13 1 
ATOM   5569 H  HD13 B ILE   B 1 106 ? 35.663 -30.325 6.305   0.40 29.83 ?  106  ILE   B HD13 1 
ATOM   5570 N  N    A GLN   B 1 107 ? 31.358 -27.558 8.150   0.60 23.17 ?  107  GLN   B N    1 
ATOM   5571 N  N    B GLN   B 1 107 ? 31.324 -27.569 8.035   0.40 23.70 ?  107  GLN   B N    1 
ATOM   5572 C  CA   A GLN   B 1 107 ? 30.275 -26.771 7.567   0.60 23.44 ?  107  GLN   B CA   1 
ATOM   5573 C  CA   B GLN   B 1 107 ? 30.250 -26.753 7.482   0.40 23.91 ?  107  GLN   B CA   1 
ATOM   5574 C  C    A GLN   B 1 107 ? 30.755 -25.424 7.035   0.60 21.42 ?  107  GLN   B C    1 
ATOM   5575 C  C    B GLN   B 1 107 ? 30.740 -25.384 7.023   0.40 21.76 ?  107  GLN   B C    1 
ATOM   5576 O  O    A GLN   B 1 107 ? 30.110 -24.859 6.148   0.60 21.97 ?  107  GLN   B O    1 
ATOM   5577 O  O    B GLN   B 1 107 ? 30.085 -24.757 6.184   0.40 22.16 ?  107  GLN   B O    1 
ATOM   5578 C  CB   A GLN   B 1 107 ? 29.171 -26.563 8.609   0.60 26.67 ?  107  GLN   B CB   1 
ATOM   5579 C  CB   B GLN   B 1 107 ? 29.134 -26.599 8.520   0.40 26.57 ?  107  GLN   B CB   1 
ATOM   5580 C  CG   A GLN   B 1 107 ? 27.846 -26.056 8.045   0.60 30.01 ?  107  GLN   B CG   1 
ATOM   5581 C  CG   B GLN   B 1 107 ? 27.808 -26.103 7.960   0.40 29.13 ?  107  GLN   B CG   1 
ATOM   5582 C  CD   A GLN   B 1 107 ? 27.790 -24.543 7.924   0.60 32.53 ?  107  GLN   B CD   1 
ATOM   5583 C  CD   B GLN   B 1 107 ? 27.705 -24.589 7.939   0.40 31.13 ?  107  GLN   B CD   1 
ATOM   5584 O  OE1  A GLN   B 1 107 ? 28.628 -23.830 8.480   0.60 33.41 ?  107  GLN   B OE1  1 
ATOM   5585 O  OE1  B GLN   B 1 107 ? 28.528 -23.889 8.531   0.40 31.83 ?  107  GLN   B OE1  1 
ATOM   5586 N  NE2  A GLN   B 1 107 ? 26.795 -24.044 7.195   0.60 33.38 ?  107  GLN   B NE2  1 
ATOM   5587 N  NE2  B GLN   B 1 107 ? 26.686 -24.076 7.259   0.40 31.83 ?  107  GLN   B NE2  1 
ATOM   5588 H  H    A GLN   B 1 107 ? 31.252 -27.747 8.979   0.60 27.83 ?  107  GLN   B H    1 
ATOM   5589 H  H    B GLN   B 1 107 ? 31.221 -27.774 8.862   0.40 28.47 ?  107  GLN   B H    1 
ATOM   5590 H  HA   A GLN   B 1 107 ? 29.894 -27.268 6.824   0.60 28.15 ?  107  GLN   B HA   1 
ATOM   5591 H  HA   B GLN   B 1 107 ? 29.876 -27.210 6.711   0.40 28.72 ?  107  GLN   B HA   1 
ATOM   5592 H  HB2  A GLN   B 1 107 ? 28.996 -27.408 9.046   0.60 32.03 ?  107  GLN   B HB2  1 
ATOM   5593 H  HB2  B GLN   B 1 107 ? 28.971 -27.462 8.928   0.40 31.91 ?  107  GLN   B HB2  1 
ATOM   5594 H  HB3  A GLN   B 1 107 ? 29.480 -25.916 9.263   0.60 32.03 ?  107  GLN   B HB3  1 
ATOM   5595 H  HB3  B GLN   B 1 107 ? 29.424 -25.969 9.199   0.40 31.91 ?  107  GLN   B HB3  1 
ATOM   5596 H  HG2  A GLN   B 1 107 ? 27.714 -26.428 7.160   0.60 36.04 ?  107  GLN   B HG2  1 
ATOM   5597 H  HG2  B GLN   B 1 107 ? 27.709 -26.421 7.049   0.40 34.98 ?  107  GLN   B HG2  1 
ATOM   5598 H  HG3  A GLN   B 1 107 ? 27.124 -26.339 8.632   0.60 36.04 ?  107  GLN   B HG3  1 
ATOM   5599 H  HG3  B GLN   B 1 107 ? 27.084 -26.449 8.510   0.40 34.98 ?  107  GLN   B HG3  1 
ATOM   5600 H  HE21 A GLN   B 1 107 ? 26.228 -24.573 6.819   0.60 40.08 ?  107  GLN   B HE21 1 
ATOM   5601 H  HE21 B GLN   B 1 107 ? 26.130 -24.596 6.856   0.40 38.22 ?  107  GLN   B HE21 1 
ATOM   5602 H  HE22 A GLN   B 1 107 ? 26.714 -23.193 7.099   0.60 40.08 ?  107  GLN   B HE22 1 
ATOM   5603 H  HE22 B GLN   B 1 107 ? 26.581 -23.224 7.221   0.40 38.22 ?  107  GLN   B HE22 1 
ATOM   5604 N  N    . LEU   B 1 108 ? 31.876 -24.907 7.541   1.00 19.52 ?  108  LEU   B N    1 
ATOM   5605 C  CA   . LEU   B 1 108 ? 32.414 -23.610 7.125   1.00 17.17 ?  108  LEU   B CA   1 
ATOM   5606 C  C    . LEU   B 1 108 ? 33.058 -23.632 5.746   1.00 14.91 ?  108  LEU   B C    1 
ATOM   5607 O  O    . LEU   B 1 108 ? 33.488 -22.575 5.259   1.00 14.81 ?  108  LEU   B O    1 
ATOM   5608 C  CB   . LEU   B 1 108 ? 33.422 -23.116 8.158   1.00 17.46 ?  108  LEU   B CB   1 
ATOM   5609 C  CG   . LEU   B 1 108 ? 32.800 -22.671 9.480   1.00 18.64 ?  108  LEU   B CG   1 
ATOM   5610 C  CD1  . LEU   B 1 108 ? 33.827 -22.651 10.597  1.00 18.66 ?  108  LEU   B CD1  1 
ATOM   5611 C  CD2  . LEU   B 1 108 ? 32.172 -21.299 9.314   1.00 19.88 ?  108  LEU   B CD2  1 
ATOM   5612 H  H    A LEU   B 1 108 ? 32.343 -25.295 8.145   0.60 23.45 ?  108  LEU   B H    1 
ATOM   5613 H  H    B LEU   B 1 108 ? 32.341 -25.311 8.136   0.40 23.45 ?  108  LEU   B H    1 
ATOM   5614 H  HA   . LEU   B 1 108 ? 31.686 -22.977 7.093   1.00 20.64 ?  108  LEU   B HA   1 
ATOM   5615 H  HB2  . LEU   B 1 108 ? 34.046 -23.831 8.354   1.00 20.98 ?  108  LEU   B HB2  1 
ATOM   5616 H  HB3  . LEU   B 1 108 ? 33.897 -22.357 7.788   1.00 20.98 ?  108  LEU   B HB3  1 
ATOM   5617 H  HG   . LEU   B 1 108 ? 32.098 -23.295 9.730   1.00 22.40 ?  108  LEU   B HG   1 
ATOM   5618 H  HD11 . LEU   B 1 108 ? 33.389 -22.390 11.425  1.00 22.42 ?  108  LEU   B HD11 1 
ATOM   5619 H  HD12 . LEU   B 1 108 ? 34.209 -23.536 10.692  1.00 22.42 ?  108  LEU   B HD12 1 
ATOM   5620 H  HD13 . LEU   B 1 108 ? 34.520 -22.010 10.377  1.00 22.42 ?  108  LEU   B HD13 1 
ATOM   5621 H  HD21 . LEU   B 1 108 ? 31.819 -21.009 10.169  1.00 23.88 ?  108  LEU   B HD21 1 
ATOM   5622 H  HD22 . LEU   B 1 108 ? 32.850 -20.679 9.007   1.00 23.88 ?  108  LEU   B HD22 1 
ATOM   5623 H  HD23 . LEU   B 1 108 ? 31.456 -21.358 8.662   1.00 23.88 ?  108  LEU   B HD23 1 
ATOM   5624 N  N    . LEU   B 1 109 ? 33.123 -24.801 5.110   1.00 13.78 ?  109  LEU   B N    1 
ATOM   5625 C  CA   . LEU   B 1 109 ? 33.747 -24.905 3.800   1.00 13.04 ?  109  LEU   B CA   1 
ATOM   5626 C  C    . LEU   B 1 109 ? 32.981 -24.116 2.746   1.00 12.48 ?  109  LEU   B C    1 
ATOM   5627 O  O    . LEU   B 1 109 ? 33.594 -23.521 1.853   1.00 12.38 ?  109  LEU   B O    1 
ATOM   5628 C  CB   . LEU   B 1 109 ? 33.866 -26.378 3.412   1.00 13.21 ?  109  LEU   B CB   1 
ATOM   5629 C  CG   . LEU   B 1 109 ? 34.655 -26.707 2.147   1.00 12.88 ?  109  LEU   B CG   1 
ATOM   5630 C  CD1  . LEU   B 1 109 ? 36.025 -26.050 2.177   1.00 13.21 ?  109  LEU   B CD1  1 
ATOM   5631 C  CD2  . LEU   B 1 109 ? 34.782 -28.220 1.983   1.00 13.71 ?  109  LEU   B CD2  1 
ATOM   5632 H  H    . LEU   B 1 109 ? 32.816 -25.547 5.408   1.00 16.57 ?  109  LEU   B H    1 
ATOM   5633 H  HA   . LEU   B 1 109 ? 34.639 -24.539 3.843   1.00 15.67 ?  109  LEU   B HA   1 
ATOM   5634 H  HB2  . LEU   B 1 109 ? 34.301 -26.851 4.140   1.00 15.88 ?  109  LEU   B HB2  1 
ATOM   5635 H  HB3  . LEU   B 1 109 ? 32.974 -26.741 3.288   1.00 15.88 ?  109  LEU   B HB3  1 
ATOM   5636 H  HG   . LEU   B 1 109 ? 34.173 -26.373 1.373   1.00 15.49 ?  109  LEU   B HG   1 
ATOM   5637 H  HD11 . LEU   B 1 109 ? 36.571 -26.419 1.466   1.00 15.88 ?  109  LEU   B HD11 1 
ATOM   5638 H  HD12 . LEU   B 1 109 ? 35.916 -25.096 2.051   1.00 15.88 ?  109  LEU   B HD12 1 
ATOM   5639 H  HD13 . LEU   B 1 109 ? 36.438 -26.228 3.037   1.00 15.88 ?  109  LEU   B HD13 1 
ATOM   5640 H  HD21 . LEU   B 1 109 ? 35.365 -28.410 1.228   1.00 16.48 ?  109  LEU   B HD21 1 
ATOM   5641 H  HD22 . LEU   B 1 109 ? 35.159 -28.596 2.792   1.00 16.48 ?  109  LEU   B HD22 1 
ATOM   5642 H  HD23 . LEU   B 1 109 ? 33.902 -28.599 1.820   1.00 16.48 ?  109  LEU   B HD23 1 
ATOM   5643 N  N    . LYS   B 1 110 ? 31.647 -24.081 2.828   1.00 12.10 ?  110  LYS   B N    1 
ATOM   5644 C  CA   . LYS   B 1 110 ? 30.889 -23.316 1.842   1.00 11.94 ?  110  LYS   B CA   1 
ATOM   5645 C  C    . LYS   B 1 110 ? 31.226 -21.829 1.935   1.00 11.72 ?  110  LYS   B C    1 
ATOM   5646 O  O    . LYS   B 1 110 ? 31.485 -21.177 0.920   1.00 11.63 ?  110  LYS   B O    1 
ATOM   5647 C  CB   . LYS   B 1 110 ? 29.386 -23.565 1.992   1.00 12.83 ?  110  LYS   B CB   1 
ATOM   5648 C  CG   . LYS   B 1 110 ? 28.575 -22.926 0.870   1.00 13.17 ?  110  LYS   B CG   1 
ATOM   5649 C  CD   . LYS   B 1 110 ? 27.120 -23.363 0.896   1.00 13.32 ?  110  LYS   B CD   1 
ATOM   5650 C  CE   . LYS   B 1 110 ? 26.350 -22.836 -0.318  1.00 14.08 ?  110  LYS   B CE   1 
ATOM   5651 N  NZ   . LYS   B 1 110 ? 26.681 -23.546 -1.582  1.00 14.10 ?  110  LYS   B NZ   1 
ATOM   5652 H  H    . LYS   B 1 110 ? 31.176 -24.489 3.420   1.00 14.55 ?  110  LYS   B H    1 
ATOM   5653 H  HA   . LYS   B 1 110 ? 31.146 -23.619 0.955   1.00 14.36 ?  110  LYS   B HA   1 
ATOM   5654 H  HB2  . LYS   B 1 110 ? 29.219 -24.524 1.973   1.00 15.43 ?  110  LYS   B HB2  1 
ATOM   5655 H  HB3  . LYS   B 1 110 ? 29.084 -23.193 2.833   1.00 15.43 ?  110  LYS   B HB3  1 
ATOM   5656 H  HG2  . LYS   B 1 110 ? 28.595 -21.961 0.969   1.00 15.83 ?  110  LYS   B HG2  1 
ATOM   5657 H  HG3  . LYS   B 1 110 ? 28.948 -23.183 0.014   1.00 15.83 ?  110  LYS   B HG3  1 
ATOM   5658 H  HD2  . LYS   B 1 110 ? 27.073 -24.336 0.884   1.00 16.02 ?  110  LYS   B HD2  1 
ATOM   5659 H  HD3  . LYS   B 1 110 ? 26.691 -23.022 1.698   1.00 16.02 ?  110  LYS   B HD3  1 
ATOM   5660 H  HE2  . LYS   B 1 110 ? 25.399 -22.939 -0.161  1.00 16.92 ?  110  LYS   B HE2  1 
ATOM   5661 H  HE3  . LYS   B 1 110 ? 26.565 -21.898 -0.440  1.00 16.92 ?  110  LYS   B HE3  1 
ATOM   5662 H  HZ1  . LYS   B 1 110 ? 26.215 -23.204 -2.256  1.00 16.95 ?  110  LYS   B HZ1  1 
ATOM   5663 H  HZ2  . LYS   B 1 110 ? 27.551 -23.462 -1.758  1.00 16.95 ?  110  LYS   B HZ2  1 
ATOM   5664 H  HZ3  . LYS   B 1 110 ? 26.487 -24.412 -1.503  1.00 16.95 ?  110  LYS   B HZ3  1 
ATOM   5665 N  N    . SER   B 1 111 ? 31.248 -21.277 3.155   1.00 12.02 ?  111  SER   B N    1 
ATOM   5666 C  CA   . SER   B 1 111 ? 31.637 -19.878 3.333   1.00 12.01 ?  111  SER   B CA   1 
ATOM   5667 C  C    . SER   B 1 111 ? 33.019 -19.618 2.747   1.00 11.39 ?  111  SER   B C    1 
ATOM   5668 O  O    . SER   B 1 111 ? 33.244 -18.586 2.100   1.00 11.59 ?  111  SER   B O    1 
ATOM   5669 C  CB   . SER   B 1 111 ? 31.632 -19.516 4.818   1.00 13.00 ?  111  SER   B CB   1 
ATOM   5670 O  OG   . SER   B 1 111 ? 30.322 -19.514 5.344   1.00 14.99 ?  111  SER   B OG   1 
ATOM   5671 H  H    . SER   B 1 111 ? 31.054 -21.693 3.883   1.00 14.45 ?  111  SER   B H    1 
ATOM   5672 H  HA   . SER   B 1 111 ? 31.003 -19.311 2.877   1.00 14.44 ?  111  SER   B HA   1 
ATOM   5673 H  HB2  . SER   B 1 111 ? 32.159 -20.168 5.306   1.00 15.62 ?  111  SER   B HB2  1 
ATOM   5674 H  HB3  . SER   B 1 111 ? 32.014 -18.633 4.928   1.00 15.62 ?  111  SER   B HB3  1 
ATOM   5675 H  HG   . SER   B 1 111 ? 30.339 -19.309 6.163   1.00 18.01 ?  111  SER   B HG   1 
ATOM   5676 N  N    . ALA   B 1 112 ? 33.958 -20.542 2.964   1.00 11.38 ?  112  ALA   B N    1 
ATOM   5677 C  CA   . ALA   B 1 112 ? 35.303 -20.368 2.420   1.00 11.43 ?  112  ALA   B CA   1 
ATOM   5678 C  C    . ALA   B 1 112 ? 35.269 -20.267 0.899   1.00 10.78 ?  112  ALA   B C    1 
ATOM   5679 O  O    . ALA   B 1 112 ? 35.894 -19.377 0.311   1.00 11.10 ?  112  ALA   B O    1 
ATOM   5680 C  CB   . ALA   B 1 112 ? 36.220 -21.503 2.885   1.00 11.79 ?  112  ALA   B CB   1 
ATOM   5681 H  H    . ALA   B 1 112 ? 33.844 -21.266 3.419   1.00 13.68 ?  112  ALA   B H    1 
ATOM   5682 H  HA   . ALA   B 1 112 ? 35.668 -19.538 2.764   1.00 13.74 ?  112  ALA   B HA   1 
ATOM   5683 H  HB1  . ALA   B 1 112 ? 37.107 -21.357 2.518   1.00 14.17 ?  112  ALA   B HB1  1 
ATOM   5684 H  HB2  . ALA   B 1 112 ? 36.263 -21.496 3.856   1.00 14.17 ?  112  ALA   B HB2  1 
ATOM   5685 H  HB3  . ALA   B 1 112 ? 35.864 -22.346 2.574   1.00 14.17 ?  112  ALA   B HB3  1 
ATOM   5686 N  N    . TYR   B 1 113 ? 34.534 -21.167 0.239   1.00 10.84 ?  113  TYR   B N    1 
ATOM   5687 C  CA   . TYR   B 1 113 ? 34.455 -21.115 -1.215  1.00 10.52 ?  113  TYR   B CA   1 
ATOM   5688 C  C    . TYR   B 1 113 ? 33.744 -19.863 -1.726  1.00 10.32 ?  113  TYR   B C    1 
ATOM   5689 O  O    . TYR   B 1 113 ? 34.020 -19.423 -2.848  1.00 10.44 ?  113  TYR   B O    1 
ATOM   5690 C  CB   . TYR   B 1 113 ? 33.788 -22.378 -1.767  1.00 10.78 ?  113  TYR   B CB   1 
ATOM   5691 C  CG   . TYR   B 1 113 ? 34.751 -23.516 -2.033  1.00 11.08 ?  113  TYR   B CG   1 
ATOM   5692 C  CD1  . TYR   B 1 113 ? 35.735 -23.412 -3.011  1.00 11.51 ?  113  TYR   B CD1  1 
ATOM   5693 C  CD2  . TYR   B 1 113 ? 34.662 -24.707 -1.327  1.00 11.14 ?  113  TYR   B CD2  1 
ATOM   5694 C  CE1  . TYR   B 1 113 ? 36.612 -24.446 -3.261  1.00 11.47 ?  113  TYR   B CE1  1 
ATOM   5695 C  CE2  . TYR   B 1 113 ? 35.532 -25.753 -1.578  1.00 11.55 ?  113  TYR   B CE2  1 
ATOM   5696 C  CZ   . TYR   B 1 113 ? 36.502 -25.619 -2.550  1.00 11.52 ?  113  TYR   B CZ   1 
ATOM   5697 O  OH   . TYR   B 1 113 ? 37.380 -26.635 -2.829  1.00 12.21 ?  113  TYR   B OH   1 
ATOM   5698 H  H    . TYR   B 1 113 ? 34.075 -21.799 0.609   1.00 13.04 ?  113  TYR   B H    1 
ATOM   5699 H  HA   . TYR   B 1 113 ? 35.358 -21.091 -1.556  1.00 12.66 ?  113  TYR   B HA   1 
ATOM   5700 H  HB2  . TYR   B 1 113 ? 33.130 -22.696 -1.128  1.00 12.96 ?  113  TYR   B HB2  1 
ATOM   5701 H  HB3  . TYR   B 1 113 ? 33.351 -22.160 -2.605  1.00 12.96 ?  113  TYR   B HB3  1 
ATOM   5702 H  HD1  . TYR   B 1 113 ? 35.815 -22.622 -3.502  1.00 13.84 ?  113  TYR   B HD1  1 
ATOM   5703 H  HD2  . TYR   B 1 113 ? 34.006 -24.805 -0.681  1.00 13.39 ?  113  TYR   B HD2  1 
ATOM   5704 H  HE1  . TYR   B 1 113 ? 37.263 -24.356 -3.927  1.00 13.79 ?  113  TYR   B HE1  1 
ATOM   5705 H  HE2  . TYR   B 1 113 ? 35.455 -26.545 -1.105  1.00 13.89 ?  113  TYR   B HE2  1 
ATOM   5706 H  HH   . TYR   B 1 113 ? 37.206 -27.300 -2.344  1.00 14.68 ?  113  TYR   B HH   1 
ATOM   5707 N  N    . GLU   B 1 114 ? 32.823 -19.286 -0.948  1.00 10.57 ?  114  GLU   B N    1 
ATOM   5708 C  CA   . GLU   B 1 114 ? 32.136 -18.079 -1.397  1.00 10.37 ?  114  GLU   B CA   1 
ATOM   5709 C  C    . GLU   B 1 114 ? 33.120 -16.954 -1.695  1.00 10.15 ?  114  GLU   B C    1 
ATOM   5710 O  O    . GLU   B 1 114 ? 32.844 -16.099 -2.537  1.00 10.43 ?  114  GLU   B O    1 
ATOM   5711 C  CB   . GLU   B 1 114 ? 31.077 -17.658 -0.376  1.00 10.75 ?  114  GLU   B CB   1 
ATOM   5712 C  CG   . GLU   B 1 114 ? 29.863 -18.583 -0.441  1.00 11.02 ?  114  GLU   B CG   1 
ATOM   5713 C  CD   . GLU   B 1 114 ? 28.846 -18.397 0.670   1.00 10.90 ?  114  GLU   B CD   1 
ATOM   5714 O  OE1  . GLU   B 1 114 ? 29.142 -17.780 1.715   1.00 11.36 ?  114  GLU   B OE1  1 
ATOM   5715 O  OE2  . GLU   B 1 114 ? 27.724 -18.928 0.509   1.00 11.74 -1 114  GLU   B OE2  1 
ATOM   5716 H  H    . GLU   B 1 114 ? 32.571 -19.582 -0.174  1.00 12.72 ?  114  GLU   B H    1 
ATOM   5717 H  HA   . GLU   B 1 114 ? 31.675 -18.279 -2.219  1.00 12.47 ?  114  GLU   B HA   1 
ATOM   5718 H  HB2  . GLU   B 1 114 ? 31.448 -17.711 0.522   1.00 12.93 ?  114  GLU   B HB2  1 
ATOM   5719 H  HB3  . GLU   B 1 114 ? 30.781 -16.758 -0.566  1.00 12.93 ?  114  GLU   B HB3  1 
ATOM   5720 H  HG2  . GLU   B 1 114 ? 29.413 -18.436 -1.284  1.00 13.25 ?  114  GLU   B HG2  1 
ATOM   5721 H  HG3  . GLU   B 1 114 ? 30.179 -19.504 -0.399  1.00 13.25 ?  114  GLU   B HG3  1 
ATOM   5722 N  N    . ASN   B 1 115 ? 34.282 -16.947 -1.040  1.00 10.15 ?  115  ASN   B N    1 
ATOM   5723 C  CA   . ASN   B 1 115 ? 35.272 -15.910 -1.335  1.00 10.10 ?  115  ASN   B CA   1 
ATOM   5724 C  C    . ASN   B 1 115 ? 35.683 -15.927 -2.802  1.00 9.82  ?  115  ASN   B C    1 
ATOM   5725 O  O    . ASN   B 1 115 ? 36.067 -14.886 -3.355  1.00 10.62 ?  115  ASN   B O    1 
ATOM   5726 C  CB   . ASN   B 1 115 ? 36.513 -16.093 -0.458  1.00 10.71 ?  115  ASN   B CB   1 
ATOM   5727 C  CG   . ASN   B 1 115 ? 36.253 -15.824 1.009   1.00 10.90 ?  115  ASN   B CG   1 
ATOM   5728 O  OD1  . ASN   B 1 115 ? 36.259 -14.681 1.452   1.00 12.88 ?  115  ASN   B OD1  1 
ATOM   5729 N  ND2  . ASN   B 1 115 ? 36.094 -16.891 1.789   1.00 11.12 ?  115  ASN   B ND2  1 
ATOM   5730 H  H    . ASN   B 1 115 ? 34.515 -17.510 -0.426  1.00 12.21 ?  115  ASN   B H    1 
ATOM   5731 H  HA   . ASN   B 1 115 ? 34.892 -15.043 -1.138  1.00 12.14 ?  115  ASN   B HA   1 
ATOM   5732 H  HB2  . ASN   B 1 115 ? 36.829 -17.008 -0.544  1.00 12.87 ?  115  ASN   B HB2  1 
ATOM   5733 H  HB3  . ASN   B 1 115 ? 37.200 -15.478 -0.753  1.00 12.87 ?  115  ASN   B HB3  1 
ATOM   5734 H  HD21 . ASN   B 1 115 ? 35.951 -16.787 2.634   1.00 13.37 ?  115  ASN   B HD21 1 
ATOM   5735 H  HD22 . ASN   B 1 115 ? 36.110 -17.681 1.454   1.00 13.37 ?  115  ASN   B HD22 1 
ATOM   5736 N  N    . PHE   B 1 116 ? 35.658 -17.107 -3.440  1.00 9.62  ?  116  PHE   B N    1 
ATOM   5737 C  CA   . PHE   B 1 116 ? 36.082 -17.202 -4.831  1.00 9.89  ?  116  PHE   B CA   1 
ATOM   5738 C  C    . PHE   B 1 116 ? 35.178 -16.374 -5.738  1.00 9.61  ?  116  PHE   B C    1 
ATOM   5739 O  O    . PHE   B 1 116 ? 35.610 -15.946 -6.813  1.00 10.32 ?  116  PHE   B O    1 
ATOM   5740 C  CB   . PHE   B 1 116 ? 36.051 -18.649 -5.351  1.00 9.71  ?  116  PHE   B CB   1 
ATOM   5741 C  CG   . PHE   B 1 116 ? 37.127 -19.595 -4.811  1.00 9.80  ?  116  PHE   B CG   1 
ATOM   5742 C  CD1  . PHE   B 1 116 ? 37.790 -19.407 -3.611  1.00 10.58 ?  116  PHE   B CD1  1 
ATOM   5743 C  CD2  . PHE   B 1 116 ? 37.423 -20.735 -5.549  1.00 10.12 ?  116  PHE   B CD2  1 
ATOM   5744 C  CE1  . PHE   B 1 116 ? 38.727 -20.341 -3.165  1.00 10.49 ?  116  PHE   B CE1  1 
ATOM   5745 C  CE2  . PHE   B 1 116 ? 38.354 -21.665 -5.109  1.00 10.08 ?  116  PHE   B CE2  1 
ATOM   5746 C  CZ   . PHE   B 1 116 ? 39.008 -21.470 -3.920  1.00 10.36 ?  116  PHE   B CZ   1 
ATOM   5747 H  H    . PHE   B 1 116 ? 35.393 -17.858 -3.093  1.00 11.57 ?  116  PHE   B H    1 
ATOM   5748 H  HA   . PHE   B 1 116 ? 36.988 -16.871 -4.914  1.00 11.89 ?  116  PHE   B HA   1 
ATOM   5749 H  HB2  . PHE   B 1 116 ? 35.185 -19.035 -5.121  1.00 11.68 ?  116  PHE   B HB2  1 
ATOM   5750 H  HB3  . PHE   B 1 116 ? 36.138 -18.629 -6.317  1.00 11.68 ?  116  PHE   B HB3  1 
ATOM   5751 H  HD1  . PHE   B 1 116 ? 37.599 -18.657 -3.093  1.00 12.72 ?  116  PHE   B HD1  1 
ATOM   5752 H  HD2  . PHE   B 1 116 ? 36.975 -20.886 -6.352  1.00 12.18 ?  116  PHE   B HD2  1 
ATOM   5753 H  HE1  . PHE   B 1 116 ? 39.176 -20.200 -2.361  1.00 12.61 ?  116  PHE   B HE1  1 
ATOM   5754 H  HE2  . PHE   B 1 116 ? 38.541 -22.416 -5.625  1.00 12.12 ?  116  PHE   B HE2  1 
ATOM   5755 H  HZ   . PHE   B 1 116 ? 39.648 -22.079 -3.627  1.00 12.45 ?  116  PHE   B HZ   1 
ATOM   5756 N  N    . ASN   B 1 117 ? 33.910 -16.176 -5.349  1.00 10.21 ?  117  ASN   B N    1 
ATOM   5757 C  CA   . ASN   B 1 117 ? 32.962 -15.470 -6.209  1.00 10.36 ?  117  ASN   B CA   1 
ATOM   5758 C  C    . ASN   B 1 117 ? 33.271 -13.991 -6.357  1.00 10.57 ?  117  ASN   B C    1 
ATOM   5759 O  O    . ASN   B 1 117 ? 32.669 -13.334 -7.211  1.00 11.85 ?  117  ASN   B O    1 
ATOM   5760 C  CB   . ASN   B 1 117 ? 31.536 -15.688 -5.724  1.00 10.57 ?  117  ASN   B CB   1 
ATOM   5761 C  CG   . ASN   B 1 117 ? 31.088 -17.104 -5.972  1.00 11.09 ?  117  ASN   B CG   1 
ATOM   5762 O  OD1  . ASN   B 1 117 ? 31.436 -17.694 -6.997  1.00 11.63 ?  117  ASN   B OD1  1 
ATOM   5763 N  ND2  . ASN   B 1 117 ? 30.350 -17.675 -5.032  1.00 10.86 ?  117  ASN   B ND2  1 
ATOM   5764 H  H    . ASN   B 1 117 ? 33.586 -16.435 -4.591  1.00 12.28 ?  117  ASN   B H    1 
ATOM   5765 H  HA   . ASN   B 1 117 ? 33.022 -15.860 -7.088  1.00 12.46 ?  117  ASN   B HA   1 
ATOM   5766 H  HB2  . ASN   B 1 117 ? 31.489 -15.520 -4.766  1.00 12.71 ?  117  ASN   B HB2  1 
ATOM   5767 H  HB3  . ASN   B 1 117 ? 30.940 -15.087 -6.196  1.00 12.71 ?  117  ASN   B HB3  1 
ATOM   5768 H  HD21 . ASN   B 1 117 ? 30.073 -18.481 -5.130  1.00 13.06 ?  117  ASN   B HD21 1 
ATOM   5769 H  HD22 . ASN   B 1 117 ? 30.133 -17.229 -4.325  1.00 13.06 ?  117  ASN   B HD22 1 
ATOM   5770 N  N    . GLN   B 1 118 ? 34.205 -13.461 -5.578  1.00 10.28 ?  118  GLN   B N    1 
ATOM   5771 C  CA   . GLN   B 1 118 ? 34.634 -12.074 -5.716  1.00 10.88 ?  118  GLN   B CA   1 
ATOM   5772 C  C    . GLN   B 1 118 ? 35.704 -11.880 -6.786  1.00 10.97 ?  118  GLN   B C    1 
ATOM   5773 O  O    . GLN   B 1 118 ? 36.178 -10.748 -6.961  1.00 12.21 ?  118  GLN   B O    1 
ATOM   5774 C  CB   . GLN   B 1 118 ? 35.116 -11.549 -4.362  1.00 11.75 ?  118  GLN   B CB   1 
ATOM   5775 C  CG   . GLN   B 1 118 ? 34.028 -11.590 -3.296  1.00 11.54 ?  118  GLN   B CG   1 
ATOM   5776 C  CD   . GLN   B 1 118 ? 32.850 -10.688 -3.632  1.00 11.59 ?  118  GLN   B CD   1 
ATOM   5777 O  OE1  . GLN   B 1 118 ? 33.032 -9.548  -4.079  1.00 12.25 ?  118  GLN   B OE1  1 
ATOM   5778 N  NE2  . GLN   B 1 118 ? 31.637 -11.179 -3.414  1.00 12.11 ?  118  GLN   B NE2  1 
ATOM   5779 H  H    . GLN   B 1 118 ? 34.623 -13.886 -4.951  1.00 12.36 ?  118  GLN   B H    1 
ATOM   5780 H  HA   . GLN   B 1 118 ? 33.868 -11.541 -5.979  1.00 13.08 ?  118  GLN   B HA   1 
ATOM   5781 H  HB2  . GLN   B 1 118 ? 35.859 -12.083 -4.054  1.00 14.12 ?  118  GLN   B HB2  1 
ATOM   5782 H  HB3  . GLN   B 1 118 ? 35.396 -10.618 -4.462  1.00 14.12 ?  118  GLN   B HB3  1 
ATOM   5783 H  HG2  . GLN   B 1 118 ? 33.701 -12.497 -3.214  1.00 13.88 ?  118  GLN   B HG2  1 
ATOM   5784 H  HG3  . GLN   B 1 118 ? 34.403 -11.293 -2.450  1.00 13.88 ?  118  GLN   B HG3  1 
ATOM   5785 H  HE21 . GLN   B 1 118 ? 31.548 -11.978 -3.102  1.00 14.56 ?  118  GLN   B HE21 1 
ATOM   5786 H  HE22 . GLN   B 1 118 ? 30.948 -10.705 -3.591  1.00 14.56 ?  118  GLN   B HE22 1 
ATOM   5787 N  N    . HIS   B 1 119 ? 36.055 -12.934 -7.527  1.00 10.40 ?  119  HIS   B N    1 
ATOM   5788 C  CA   . HIS   B 1 119 ? 37.097 -12.889 -8.546  1.00 10.91 ?  119  HIS   B CA   1 
ATOM   5789 C  C    . HIS   B 1 119 ? 36.621 -13.623 -9.785  1.00 10.81 ?  119  HIS   B C    1 
ATOM   5790 O  O    . HIS   B 1 119 ? 36.117 -14.742 -9.685  1.00 11.44 ?  119  HIS   B O    1 
ATOM   5791 C  CB   . HIS   B 1 119 ? 38.379 -13.520 -8.001  1.00 11.52 ?  119  HIS   B CB   1 
ATOM   5792 C  CG   . HIS   B 1 119 ? 38.864 -12.820 -6.780  1.00 12.63 ?  119  HIS   B CG   1 
ATOM   5793 N  ND1  . HIS   B 1 119 ? 39.656 -11.693 -6.839  1.00 14.42 ?  119  HIS   B ND1  1 
ATOM   5794 C  CD2  . HIS   B 1 119 ? 38.585 -13.021 -5.472  1.00 13.51 ?  119  HIS   B CD2  1 
ATOM   5795 C  CE1  . HIS   B 1 119 ? 39.867 -11.249 -5.615  1.00 15.49 ?  119  HIS   B CE1  1 
ATOM   5796 N  NE2  . HIS   B 1 119 ? 39.223 -12.032 -4.768  1.00 15.10 ?  119  HIS   B NE2  1 
ATOM   5797 H  H    . HIS   B 1 119 ? 35.681 -13.708 -7.455  1.00 12.51 ?  119  HIS   B H    1 
ATOM   5798 H  HA   . HIS   B 1 119 ? 37.276 -11.966 -8.785  1.00 13.12 ?  119  HIS   B HA   1 
ATOM   5799 H  HB2  . HIS   B 1 119 ? 38.207 -14.445 -7.776  1.00 13.85 ?  119  HIS   B HB2  1 
ATOM   5800 H  HB3  . HIS   B 1 119 ? 39.071 -13.462 -8.681  1.00 13.85 ?  119  HIS   B HB3  1 
ATOM   5801 H  HD2  . HIS   B 1 119 ? 38.061 -13.704 -5.117  1.00 16.24 ?  119  HIS   B HD2  1 
ATOM   5802 H  HE1  . HIS   B 1 119 ? 40.393 -10.518 -5.383  1.00 18.62 ?  119  HIS   B HE1  1 
ATOM   5803 H  HE2  . HIS   B 1 119 ? 39.236 -11.958 -3.910  1.00 18.15 ?  119  HIS   B HE2  1 
ATOM   5804 N  N    . GLU   B 1 120 ? 36.764 -12.997 -10.954 1.00 11.40 ?  120  GLU   B N    1 
ATOM   5805 C  CA   . GLU   B 1 120 ? 36.170 -13.578 -12.154 1.00 12.84 ?  120  GLU   B CA   1 
ATOM   5806 C  C    . GLU   B 1 120 ? 36.848 -14.877 -12.572 1.00 11.69 ?  120  GLU   B C    1 
ATOM   5807 O  O    . GLU   B 1 120 ? 36.188 -15.753 -13.143 1.00 11.98 ?  120  GLU   B O    1 
ATOM   5808 C  CB   . GLU   B 1 120 ? 36.183 -12.569 -13.299 1.00 16.96 ?  120  GLU   B CB   1 
ATOM   5809 C  CG   . GLU   B 1 120 ? 35.251 -11.395 -13.063 1.00 23.33 ?  120  GLU   B CG   1 
ATOM   5810 C  CD   . GLU   B 1 120 ? 35.061 -10.532 -14.292 1.00 28.95 ?  120  GLU   B CD   1 
ATOM   5811 O  OE1  . GLU   B 1 120 ? 36.039 -10.344 -15.047 1.00 31.03 ?  120  GLU   B OE1  1 
ATOM   5812 O  OE2  . GLU   B 1 120 ? 33.930 -10.045 -14.501 1.00 31.32 -1 120  GLU   B OE2  1 
ATOM   5813 H  H    . GLU   B 1 120 ? 37.183 -12.254 -11.077 1.00 13.71 ?  120  GLU   B H    1 
ATOM   5814 H  HA   . GLU   B 1 120 ? 35.245 -13.786 -11.967 1.00 15.43 ?  120  GLU   B HA   1 
ATOM   5815 H  HB2  . GLU   B 1 120 ? 37.077 -12.217 -13.409 1.00 20.38 ?  120  GLU   B HB2  1 
ATOM   5816 H  HB3  . GLU   B 1 120 ? 35.896 -13.010 -14.116 1.00 20.38 ?  120  GLU   B HB3  1 
ATOM   5817 H  HG2  . GLU   B 1 120 ? 34.376 -11.727 -12.807 1.00 28.02 ?  120  GLU   B HG2  1 
ATOM   5818 H  HG3  . GLU   B 1 120 ? 35.614 -10.837 -12.358 1.00 28.02 ?  120  GLU   B HG3  1 
ATOM   5819 N  N    . VAL   B 1 121 ? 38.147 -15.019 -12.305 1.00 11.27 ?  121  VAL   B N    1 
ATOM   5820 C  CA   . VAL   B 1 121 ? 38.899 -16.224 -12.655 1.00 11.25 ?  121  VAL   B CA   1 
ATOM   5821 C  C    . VAL   B 1 121 ? 40.016 -16.429 -11.636 1.00 10.73 ?  121  VAL   B C    1 
ATOM   5822 O  O    . VAL   B 1 121 ? 40.692 -15.473 -11.238 1.00 11.37 ?  121  VAL   B O    1 
ATOM   5823 C  CB   . VAL   B 1 121 ? 39.409 -16.180 -14.115 1.00 12.94 ?  121  VAL   B CB   1 
ATOM   5824 C  CG1  . VAL   B 1 121 ? 40.278 -14.952 -14.375 1.00 14.18 ?  121  VAL   B CG1  1 
ATOM   5825 C  CG2  . VAL   B 1 121 ? 40.138 -17.463 -14.471 1.00 14.21 ?  121  VAL   B CG2  1 
ATOM   5826 H  H    . VAL   B 1 121 ? 38.626 -14.416 -11.918 1.00 13.55 ?  121  VAL   B H    1 
ATOM   5827 H  HA   . VAL   B 1 121 ? 38.295 -16.979 -12.587 1.00 13.53 ?  121  VAL   B HA   1 
ATOM   5828 H  HB   . VAL   B 1 121 ? 38.637 -16.116 -14.705 1.00 15.55 ?  121  VAL   B HB   1 
ATOM   5829 H  HG11 . VAL   B 1 121 ? 40.576 -14.966 -15.300 1.00 17.04 ?  121  VAL   B HG11 1 
ATOM   5830 H  HG12 . VAL   B 1 121 ? 39.753 -14.152 -14.212 1.00 17.04 ?  121  VAL   B HG12 1 
ATOM   5831 H  HG13 . VAL   B 1 121 ? 41.042 -14.974 -13.781 1.00 17.04 ?  121  VAL   B HG13 1 
ATOM   5832 H  HG21 . VAL   B 1 121 ? 40.334 -17.460 -15.423 1.00 17.07 ?  121  VAL   B HG21 1 
ATOM   5833 H  HG22 . VAL   B 1 121 ? 40.963 -17.509 -13.966 1.00 17.07 ?  121  VAL   B HG22 1 
ATOM   5834 H  HG23 . VAL   B 1 121 ? 39.572 -18.220 -14.255 1.00 17.07 ?  121  VAL   B HG23 1 
ATOM   5835 N  N    . LEU   B 1 122 ? 40.203 -17.682 -11.208 1.00 10.26 ?  122  LEU   B N    1 
ATOM   5836 C  CA   . LEU   B 1 122 ? 41.188 -18.032 -10.191 1.00 10.13 ?  122  LEU   B CA   1 
ATOM   5837 C  C    . LEU   B 1 122 ? 41.843 -19.363 -10.523 1.00 9.96  ?  122  LEU   B C    1 
ATOM   5838 O  O    . LEU   B 1 122 ? 41.180 -20.284 -11.023 1.00 11.04 ?  122  LEU   B O    1 
ATOM   5839 C  CB   . LEU   B 1 122 ? 40.534 -18.263 -8.816  1.00 11.89 ?  122  LEU   B CB   1 
ATOM   5840 C  CG   . LEU   B 1 122 ? 39.501 -17.248 -8.318  1.00 11.47 ?  122  LEU   B CG   1 
ATOM   5841 C  CD1  . LEU   B 1 122 ? 38.109 -17.632 -8.784  1.00 12.50 ?  122  LEU   B CD1  1 
ATOM   5842 C  CD2  . LEU   B 1 122 ? 39.560 -17.150 -6.810  1.00 11.29 ?  122  LEU   B CD2  1 
ATOM   5843 H  H    . LEU   B 1 122 ? 39.759 -18.358 -11.502 1.00 12.33 ?  122  LEU   B H    1 
ATOM   5844 H  HA   . LEU   B 1 122 ? 41.863 -17.339 -10.114 1.00 12.18 ?  122  LEU   B HA   1 
ATOM   5845 H  HB2  . LEU   B 1 122 ? 40.090 -19.121 -8.839  1.00 14.29 ?  122  LEU   B HB2  1 
ATOM   5846 H  HB3  . LEU   B 1 122 ? 41.240 -18.286 -8.153  1.00 14.29 ?  122  LEU   B HB3  1 
ATOM   5847 H  HG   . LEU   B 1 122 ? 39.708 -16.372 -8.680  1.00 13.79 ?  122  LEU   B HG   1 
ATOM   5848 H  HD11 . LEU   B 1 122 ? 37.471 -16.989 -8.438  1.00 15.02 ?  122  LEU   B HD11 1 
ATOM   5849 H  HD12 . LEU   B 1 122 ? 38.090 -17.628 -9.753  1.00 15.02 ?  122  LEU   B HD12 1 
ATOM   5850 H  HD13 . LEU   B 1 122 ? 37.899 -18.519 -8.452  1.00 15.02 ?  122  LEU   B HD13 1 
ATOM   5851 H  HD21 . LEU   B 1 122 ? 38.877 -16.537 -6.500  1.00 13.58 ?  122  LEU   B HD21 1 
ATOM   5852 H  HD22 . LEU   B 1 122 ? 39.413 -18.030 -6.427  1.00 13.58 ?  122  LEU   B HD22 1 
ATOM   5853 H  HD23 . LEU   B 1 122 ? 40.439 -16.823 -6.547  1.00 13.58 ?  122  LEU   B HD23 1 
ATOM   5854 N  N    . LEU   B 1 123 ? 43.132 -19.471 -10.170 1.00 9.77  ?  123  LEU   B N    1 
ATOM   5855 C  CA   . LEU   B 1 123 ? 43.847 -20.740 -10.049 1.00 9.93  ?  123  LEU   B CA   1 
ATOM   5856 C  C    . LEU   B 1 123 ? 43.820 -21.139 -8.579  1.00 9.60  ?  123  LEU   B C    1 
ATOM   5857 O  O    . LEU   B 1 123 ? 44.168 -20.317 -7.724  1.00 10.12 ?  123  LEU   B O    1 
ATOM   5858 C  CB   . LEU   B 1 123 ? 45.297 -20.556 -10.505 1.00 10.34 ?  123  LEU   B CB   1 
ATOM   5859 C  CG   . LEU   B 1 123 ? 46.246 -21.738 -10.273 1.00 10.73 ?  123  LEU   B CG   1 
ATOM   5860 C  CD1  . LEU   B 1 123 ? 45.817 -22.970 -11.063 1.00 11.34 ?  123  LEU   B CD1  1 
ATOM   5861 C  CD2  . LEU   B 1 123 ? 47.659 -21.342 -10.640 1.00 11.39 ?  123  LEU   B CD2  1 
ATOM   5862 H  H    . LEU   B 1 123 ? 43.631 -18.787 -9.983  1.00 11.75 ?  123  LEU   B H    1 
ATOM   5863 H  HA   . LEU   B 1 123 ? 43.410 -21.423 -10.586 1.00 11.95 ?  123  LEU   B HA   1 
ATOM   5864 H  HB2  . LEU   B 1 123 ? 45.289 -20.378 -11.460 1.00 12.44 ?  123  LEU   B HB2  1 
ATOM   5865 H  HB3  . LEU   B 1 123 ? 45.665 -19.797 -10.037 1.00 12.44 ?  123  LEU   B HB3  1 
ATOM   5866 H  HG   . LEU   B 1 123 ? 46.239 -21.977 -9.335  1.00 12.90 ?  123  LEU   B HG   1 
ATOM   5867 H  HD11 . LEU   B 1 123 ? 46.453 -23.684 -10.904 1.00 13.63 ?  123  LEU   B HD11 1 
ATOM   5868 H  HD12 . LEU   B 1 123 ? 44.933 -23.242 -10.768 1.00 13.63 ?  123  LEU   B HD12 1 
ATOM   5869 H  HD13 . LEU   B 1 123 ? 45.796 -22.748 -12.007 1.00 13.63 ?  123  LEU   B HD13 1 
ATOM   5870 H  HD21 . LEU   B 1 123 ? 48.248 -22.097 -10.492 1.00 13.69 ?  123  LEU   B HD21 1 
ATOM   5871 H  HD22 . LEU   B 1 123 ? 47.681 -21.083 -11.575 1.00 13.69 ?  123  LEU   B HD22 1 
ATOM   5872 H  HD23 . LEU   B 1 123 ? 47.928 -20.595 -10.084 1.00 13.69 ?  123  LEU   B HD23 1 
ATOM   5873 N  N    . ALA   B 1 124 ? 43.393 -22.371 -8.271  1.00 9.50  ?  124  ALA   B N    1 
ATOM   5874 C  CA   . ALA   B 1 124 ? 43.134 -22.692 -6.873  1.00 9.73  ?  124  ALA   B CA   1 
ATOM   5875 C  C    . ALA   B 1 124 ? 43.412 -24.151 -6.556  1.00 9.55  ?  124  ALA   B C    1 
ATOM   5876 O  O    . ALA   B 1 124 ? 43.283 -25.023 -7.425  1.00 10.18 ?  124  ALA   B O    1 
ATOM   5877 C  CB   . ALA   B 1 124 ? 41.682 -22.380 -6.495  1.00 10.28 ?  124  ALA   B CB   1 
ATOM   5878 H  H    . ALA   B 1 124 ? 43.237 -23.009 -8.834  1.00 11.43 ?  124  ALA   B H    1 
ATOM   5879 H  HA   . ALA   B 1 124 ? 43.714 -22.147 -6.330  1.00 11.70 ?  124  ALA   B HA   1 
ATOM   5880 H  HB1  . ALA   B 1 124 ? 41.540 -22.605 -5.562  1.00 12.36 ?  124  ALA   B HB1  1 
ATOM   5881 H  HB2  . ALA   B 1 124 ? 41.520 -21.431 -6.632  1.00 12.36 ?  124  ALA   B HB2  1 
ATOM   5882 H  HB3  . ALA   B 1 124 ? 41.085 -22.899 -7.055  1.00 12.36 ?  124  ALA   B HB3  1 
ATOM   5883 N  N    . PRO   B 1 125 ? 43.709 -24.451 -5.291  1.00 9.74  ?  125  PRO   B N    1 
ATOM   5884 C  CA   . PRO   B 1 125 ? 43.652 -25.819 -4.775  1.00 10.56 ?  125  PRO   B CA   1 
ATOM   5885 C  C    . PRO   B 1 125 ? 42.253 -26.093 -4.228  1.00 10.48 ?  125  PRO   B C    1 
ATOM   5886 O  O    . PRO   B 1 125 ? 41.456 -25.181 -4.017  1.00 10.99 ?  125  PRO   B O    1 
ATOM   5887 C  CB   . PRO   B 1 125 ? 44.643 -25.748 -3.605  1.00 11.60 ?  125  PRO   B CB   1 
ATOM   5888 C  CG   . PRO   B 1 125 ? 44.393 -24.355 -3.029  1.00 11.46 ?  125  PRO   B CG   1 
ATOM   5889 C  CD   . PRO   B 1 125 ? 44.043 -23.483 -4.227  1.00 10.48 ?  125  PRO   B CD   1 
ATOM   5890 H  HA   . PRO   B 1 125 ? 43.927 -26.483 -5.426  1.00 12.70 ?  125  PRO   B HA   1 
ATOM   5891 H  HB2  . PRO   B 1 125 ? 44.436 -26.436 -2.946  1.00 13.95 ?  125  PRO   B HB2  1 
ATOM   5892 H  HB3  . PRO   B 1 125 ? 45.553 -25.836 -3.924  1.00 13.95 ?  125  PRO   B HB3  1 
ATOM   5893 H  HG2  . PRO   B 1 125 ? 43.648 -24.378 -2.403  1.00 13.77 ?  125  PRO   B HG2  1 
ATOM   5894 H  HG3  . PRO   B 1 125 ? 45.194 -24.024 -2.587  1.00 13.77 ?  125  PRO   B HG3  1 
ATOM   5895 H  HD2  . PRO   B 1 125 ? 43.280 -22.920 -4.032  1.00 12.60 ?  125  PRO   B HD2  1 
ATOM   5896 H  HD3  . PRO   B 1 125 ? 44.817 -22.946 -4.487  1.00 12.60 ?  125  PRO   B HD3  1 
ATOM   5897 N  N    . LEU   B 1 126 ? 41.985 -27.372 -3.959  1.00 10.86 ?  126  LEU   B N    1 
ATOM   5898 C  CA   . LEU   B 1 126 ? 40.764 -27.743 -3.252  1.00 11.62 ?  126  LEU   B CA   1 
ATOM   5899 C  C    . LEU   B 1 126 ? 40.880 -27.338 -1.790  1.00 11.83 ?  126  LEU   B C    1 
ATOM   5900 O  O    . LEU   B 1 126 ? 41.770 -27.800 -1.070  1.00 13.34 ?  126  LEU   B O    1 
ATOM   5901 C  CB   . LEU   B 1 126 ? 40.506 -29.240 -3.367  1.00 12.82 ?  126  LEU   B CB   1 
ATOM   5902 C  CG   . LEU   B 1 126 ? 39.983 -29.718 -4.722  1.00 13.36 ?  126  LEU   B CG   1 
ATOM   5903 C  CD1  . LEU   B 1 126 ? 40.044 -31.230 -4.820  1.00 15.01 ?  126  LEU   B CD1  1 
ATOM   5904 C  CD2  . LEU   B 1 126 ? 38.566 -29.233 -4.959  1.00 13.83 ?  126  LEU   B CD2  1 
ATOM   5905 H  H    . LEU   B 1 126 ? 42.492 -28.039 -4.162  1.00 13.06 ?  126  LEU   B H    1 
ATOM   5906 H  HA   . LEU   B 1 126 ? 40.013 -27.268 -3.644  1.00 13.98 ?  126  LEU   B HA   1 
ATOM   5907 H  HB2  . LEU   B 1 126 ? 41.335 -29.707 -3.194  1.00 15.42 ?  126  LEU   B HB2  1 
ATOM   5908 H  HB3  . LEU   B 1 126 ? 39.846 -29.489 -2.702  1.00 15.42 ?  126  LEU   B HB3  1 
ATOM   5909 H  HG   . LEU   B 1 126 ? 40.549 -29.352 -5.424  1.00 16.06 ?  126  LEU   B HG   1 
ATOM   5910 H  HD11 . LEU   B 1 126 ? 39.710 -31.506 -5.689  1.00 18.04 ?  126  LEU   B HD11 1 
ATOM   5911 H  HD12 . LEU   B 1 126 ? 40.963 -31.522 -4.712  1.00 18.04 ?  126  LEU   B HD12 1 
ATOM   5912 H  HD13 . LEU   B 1 126 ? 39.491 -31.614 -4.119  1.00 18.04 ?  126  LEU   B HD13 1 
ATOM   5913 H  HD21 . LEU   B 1 126 ? 38.223 -29.645 -5.766  1.00 16.63 ?  126  LEU   B HD21 1 
ATOM   5914 H  HD22 . LEU   B 1 126 ? 38.019 -29.482 -4.199  1.00 16.63 ?  126  LEU   B HD22 1 
ATOM   5915 H  HD23 . LEU   B 1 126 ? 38.575 -28.267 -5.059  1.00 16.63 ?  126  LEU   B HD23 1 
ATOM   5916 N  N    . LEU   B 1 127 ? 39.951 -26.505 -1.336  1.00 11.43 ?  127  LEU   B N    1 
ATOM   5917 C  CA   . LEU   B 1 127 ? 40.001 -26.015 0.031   1.00 11.85 ?  127  LEU   B CA   1 
ATOM   5918 C  C    . LEU   B 1 127 ? 39.733 -27.139 1.027   1.00 11.54 ?  127  LEU   B C    1 
ATOM   5919 O  O    . LEU   B 1 127 ? 38.916 -28.039 0.798   1.00 11.80 ?  127  LEU   B O    1 
ATOM   5920 C  CB   . LEU   B 1 127 ? 38.982 -24.894 0.241   1.00 12.33 ?  127  LEU   B CB   1 
ATOM   5921 C  CG   . LEU   B 1 127 ? 39.157 -23.626 -0.593  1.00 12.99 ?  127  LEU   B CG   1 
ATOM   5922 C  CD1  . LEU   B 1 127 ? 38.030 -22.656 -0.273  1.00 12.97 ?  127  LEU   B CD1  1 
ATOM   5923 C  CD2  . LEU   B 1 127 ? 40.518 -22.980 -0.353  1.00 13.66 ?  127  LEU   B CD2  1 
ATOM   5924 H  H    . LEU   B 1 127 ? 39.282 -26.204 -1.798  1.00 13.75 ?  127  LEU   B H    1 
ATOM   5925 H  HA   . LEU   B 1 127 ? 40.884 -25.654 0.204   1.00 14.25 ?  127  LEU   B HA   1 
ATOM   5926 H  HB2  . LEU   B 1 127 ? 38.099 -25.241 0.044   1.00 14.82 ?  127  LEU   B HB2  1 
ATOM   5927 H  HB3  . LEU   B 1 127 ? 39.016 -24.622 1.172   1.00 14.82 ?  127  LEU   B HB3  1 
ATOM   5928 H  HG   . LEU   B 1 127 ? 39.084 -23.848 -1.532  1.00 15.62 ?  127  LEU   B HG   1 
ATOM   5929 H  HD11 . LEU   B 1 127 ? 38.145 -21.846 -0.799  1.00 15.59 ?  127  LEU   B HD11 1 
ATOM   5930 H  HD12 . LEU   B 1 127 ? 37.178 -23.068 -0.487  1.00 15.59 ?  127  LEU   B HD12 1 
ATOM   5931 H  HD13 . LEU   B 1 127 ? 38.059 -22.435 0.674   1.00 15.59 ?  127  LEU   B HD13 1 
ATOM   5932 H  HD21 . LEU   B 1 127 ? 40.555 -22.127 -0.816  1.00 16.42 ?  127  LEU   B HD21 1 
ATOM   5933 H  HD22 . LEU   B 1 127 ? 40.640 -22.841 0.601   1.00 16.42 ?  127  LEU   B HD22 1 
ATOM   5934 H  HD23 . LEU   B 1 127 ? 41.208 -23.570 -0.692  1.00 16.42 ?  127  LEU   B HD23 1 
ATOM   5935 N  N    . SER   B 1 128 ? 40.420 -27.052 2.158   1.00 11.72 ?  128  SER   B N    1 
ATOM   5936 C  CA   . SER   B 1 128 ? 40.316 -27.972 3.280   1.00 12.30 ?  128  SER   B CA   1 
ATOM   5937 C  C    . SER   B 1 128 ? 40.810 -29.378 2.954   1.00 12.89 ?  128  SER   B C    1 
ATOM   5938 O  O    . SER   B 1 128 ? 40.725 -30.257 3.810   1.00 14.22 ?  128  SER   B O    1 
ATOM   5939 C  CB   . SER   B 1 128 ? 38.919 -27.985 3.915   1.00 12.49 ?  128  SER   B CB   1 
ATOM   5940 O  OG   . SER   B 1 128 ? 38.609 -26.718 4.474   1.00 13.15 ?  128  SER   B OG   1 
ATOM   5941 H  H    . SER   B 1 128 ? 40.985 -26.419 2.308   1.00 14.09 ?  128  SER   B H    1 
ATOM   5942 H  HA   . SER   B 1 128 ? 40.906 -27.636 3.965   1.00 14.78 ?  128  SER   B HA   1 
ATOM   5943 H  HB2  . SER   B 1 128 ? 38.259 -28.217 3.241   1.00 15.01 ?  128  SER   B HB2  1 
ATOM   5944 H  HB3  . SER   B 1 128 ? 38.904 -28.665 4.624   1.00 15.01 ?  128  SER   B HB3  1 
ATOM   5945 H  HG   . SER   B 1 128 ? 39.177 -26.526 5.061   1.00 15.81 ?  128  SER   B HG   1 
ATOM   5946 N  N    . ALA   B 1 129 ? 41.377 -29.600 1.768   1.00 13.90 ?  129  ALA   B N    1 
ATOM   5947 C  CA   . ALA   B 1 129 ? 41.921 -30.898 1.409   1.00 14.83 ?  129  ALA   B CA   1 
ATOM   5948 C  C    . ALA   B 1 129 ? 43.313 -31.072 2.002   1.00 13.90 ?  129  ALA   B C    1 
ATOM   5949 O  O    . ALA   B 1 129 ? 43.876 -30.172 2.640   1.00 13.64 ?  129  ALA   B O    1 
ATOM   5950 C  CB   . ALA   B 1 129 ? 41.962 -31.058 -0.109  1.00 16.62 ?  129  ALA   B CB   1 
ATOM   5951 H  H    . ALA   B 1 129 ? 41.454 -29.008 1.145   1.00 16.71 ?  129  ALA   B H    1 
ATOM   5952 H  HA   . ALA   B 1 129 ? 41.351 -31.590 1.768   1.00 17.82 ?  129  ALA   B HA   1 
ATOM   5953 H  HB1  . ALA   B 1 129 ? 42.321 -31.934 -0.324  1.00 19.97 ?  129  ALA   B HB1  1 
ATOM   5954 H  HB2  . ALA   B 1 129 ? 41.061 -30.976 -0.457  1.00 19.97 ?  129  ALA   B HB2  1 
ATOM   5955 H  HB3  . ALA   B 1 129 ? 42.527 -30.367 -0.486  1.00 19.97 ?  129  ALA   B HB3  1 
ATOM   5956 N  N    . GLY   B 1 130 ? 43.870 -32.263 1.782   1.00 13.88 ?  130  GLY   B N    1 
ATOM   5957 C  CA   . GLY   B 1 130 ? 45.261 -32.499 2.124   1.00 14.70 ?  130  GLY   B CA   1 
ATOM   5958 C  C    . GLY   B 1 130 ? 45.483 -32.404 3.615   1.00 14.62 ?  130  GLY   B C    1 
ATOM   5959 O  O    . GLY   B 1 130 ? 44.788 -33.046 4.416   1.00 15.51 ?  130  GLY   B O    1 
ATOM   5960 H  H    . GLY   B 1 130 ? 43.471 -32.941 1.432   1.00 16.68 ?  130  GLY   B H    1 
ATOM   5961 H  HA2  . GLY   B 1 130 ? 45.525 -33.386 1.826   1.00 17.67 ?  130  GLY   B HA2  1 
ATOM   5962 H  HA3  . GLY   B 1 130 ? 45.822 -31.845 1.681   1.00 17.67 ?  130  GLY   B HA3  1 
ATOM   5963 N  N    . ILE   B 1 131 ? 46.459 -31.575 3.999   1.00 14.63 ?  131  ILE   B N    1 
ATOM   5964 C  CA   . ILE   B 1 131 ? 46.815 -31.448 5.404   1.00 15.64 ?  131  ILE   B CA   1 
ATOM   5965 C  C    . ILE   B 1 131 ? 45.702 -30.847 6.243   1.00 15.16 ?  131  ILE   B C    1 
ATOM   5966 O  O    . ILE   B 1 131 ? 45.786 -30.910 7.473   1.00 16.38 ?  131  ILE   B O    1 
ATOM   5967 C  CB   . ILE   B 1 131 ? 48.136 -30.673 5.603   1.00 17.42 ?  131  ILE   B CB   1 
ATOM   5968 C  CG1  . ILE   B 1 131 ? 47.965 -29.192 5.233   1.00 18.26 ?  131  ILE   B CG1  1 
ATOM   5969 C  CG2  . ILE   B 1 131 ? 49.255 -31.315 4.791   1.00 18.48 ?  131  ILE   B CG2  1 
ATOM   5970 C  CD1  . ILE   B 1 131 ? 49.177 -28.335 5.559   1.00 19.21 ?  131  ILE   B CD1  1 
ATOM   5971 H  H    . ILE   B 1 131 ? 46.923 -31.084 3.469   1.00 17.58 ?  131  ILE   B H    1 
ATOM   5972 H  HA   . ILE   B 1 131 ? 46.961 -32.343 5.749   1.00 18.80 ?  131  ILE   B HA   1 
ATOM   5973 H  HB   . ILE   B 1 131 ? 48.371 -30.724 6.542   1.00 20.93 ?  131  ILE   B HB   1 
ATOM   5974 H  HG12 . ILE   B 1 131 ? 47.798 -29.129 4.280   1.00 21.94 ?  131  ILE   B HG12 1 
ATOM   5975 H  HG13 . ILE   B 1 131 ? 47.208 -28.825 5.720   1.00 21.94 ?  131  ILE   B HG13 1 
ATOM   5976 H  HG21 . ILE   B 1 131 ? 50.096 -30.910 5.049   1.00 22.21 ?  131  ILE   B HG21 1 
ATOM   5977 H  HG22 . ILE   B 1 131 ? 49.269 -32.264 4.974   1.00 22.21 ?  131  ILE   B HG22 1 
ATOM   5978 H  HG23 . ILE   B 1 131 ? 49.084 -31.159 3.849   1.00 22.21 ?  131  ILE   B HG23 1 
ATOM   5979 H  HD11 . ILE   B 1 131 ? 48.957 -27.407 5.386   1.00 23.08 ?  131  ILE   B HD11 1 
ATOM   5980 H  HD12 . ILE   B 1 131 ? 49.400 -28.454 6.496   1.00 23.08 ?  131  ILE   B HD12 1 
ATOM   5981 H  HD13 . ILE   B 1 131 ? 49.916 -28.613 5.002   1.00 23.08 ?  131  ILE   B HD13 1 
ATOM   5982 N  N    . PHE   B 1 132 ? 44.668 -30.267 5.617   1.00 13.99 ?  132  PHE   B N    1 
ATOM   5983 C  CA   . PHE   B 1 132 ? 43.510 -29.763 6.349   1.00 14.22 ?  132  PHE   B CA   1 
ATOM   5984 C  C    . PHE   B 1 132 ? 42.489 -30.854 6.678   1.00 15.62 ?  132  PHE   B C    1 
ATOM   5985 O  O    . PHE   B 1 132 ? 41.583 -30.605 7.479   1.00 17.27 ?  132  PHE   B O    1 
ATOM   5986 C  CB   . PHE   B 1 132 ? 42.836 -28.624 5.568   1.00 13.42 ?  132  PHE   B CB   1 
ATOM   5987 C  CG   . PHE   B 1 132 ? 43.536 -27.284 5.689   1.00 13.30 ?  132  PHE   B CG   1 
ATOM   5988 C  CD1  . PHE   B 1 132 ? 44.835 -27.098 5.232   1.00 14.34 ?  132  PHE   B CD1  1 
ATOM   5989 C  CD2  . PHE   B 1 132 ? 42.859 -26.192 6.209   1.00 12.98 ?  132  PHE   B CD2  1 
ATOM   5990 C  CE1  . PHE   B 1 132 ? 45.457 -25.857 5.331   1.00 14.93 ?  132  PHE   B CE1  1 
ATOM   5991 C  CE2  . PHE   B 1 132 ? 43.468 -24.950 6.302   1.00 13.30 ?  132  PHE   B CE2  1 
ATOM   5992 C  CZ   . PHE   B 1 132 ? 44.765 -24.783 5.863   1.00 14.39 ?  132  PHE   B CZ   1 
ATOM   5993 H  H    . PHE   B 1 132 ? 44.614 -30.158 4.763   1.00 16.82 ?  132  PHE   B H    1 
ATOM   5994 H  HA   . PHE   B 1 132 ? 43.820 -29.390 7.186   1.00 17.09 ?  132  PHE   B HA   1 
ATOM   5995 H  HB2  . PHE   B 1 132 ? 42.824 -28.860 4.628   1.00 16.13 ?  132  PHE   B HB2  1 
ATOM   5996 H  HB3  . PHE   B 1 132 ? 41.931 -28.514 5.894   1.00 16.13 ?  132  PHE   B HB3  1 
ATOM   5997 H  HD1  . PHE   B 1 132 ? 45.307 -27.820 4.877   1.00 17.24 ?  132  PHE   B HD1  1 
ATOM   5998 H  HD2  . PHE   B 1 132 ? 41.982 -26.296 6.504   1.00 15.60 ?  132  PHE   B HD2  1 
ATOM   5999 H  HE1  . PHE   B 1 132 ? 46.334 -25.751 5.036   1.00 17.94 ?  132  PHE   B HE1  1 
ATOM   6000 H  HE2  . PHE   B 1 132 ? 43.002 -24.227 6.666   1.00 15.99 ?  132  PHE   B HE2  1 
ATOM   6001 H  HZ   . PHE   B 1 132 ? 45.177 -23.950 5.936   1.00 17.30 ?  132  PHE   B HZ   1 
ATOM   6002 N  N    . GLY   B 1 133 ? 42.594 -32.049 6.083   1.00 15.28 ?  133  GLY   B N    1 
ATOM   6003 C  CA   . GLY   B 1 133 ? 41.881 -33.216 6.577   1.00 15.87 ?  133  GLY   B CA   1 
ATOM   6004 C  C    . GLY   B 1 133 ? 40.486 -33.482 6.036   1.00 16.22 ?  133  GLY   B C    1 
ATOM   6005 O  O    . GLY   B 1 133 ? 39.892 -34.499 6.410   1.00 18.26 ?  133  GLY   B O    1 
ATOM   6006 H  H    . GLY   B 1 133 ? 43.088 -32.201 5.394   1.00 18.36 ?  133  GLY   B H    1 
ATOM   6007 H  HA2  . GLY   B 1 133 ? 42.420 -33.999 6.388   1.00 19.07 ?  133  GLY   B HA2  1 
ATOM   6008 H  HA3  . GLY   B 1 133 ? 41.807 -33.138 7.541   1.00 19.07 ?  133  GLY   B HA3  1 
ATOM   6009 N  N    . ALA   B 1 134 ? 39.933 -32.620 5.192   1.00 15.44 ?  134  ALA   B N    1 
ATOM   6010 C  CA   . ALA   B 1 134 ? 38.608 -32.895 4.657   1.00 15.67 ?  134  ALA   B CA   1 
ATOM   6011 C  C    . ALA   B 1 134 ? 38.694 -33.881 3.497   1.00 15.57 ?  134  ALA   B C    1 
ATOM   6012 O  O    . ALA   B 1 134 ? 39.749 -34.074 2.885   1.00 16.53 ?  134  ALA   B O    1 
ATOM   6013 C  CB   . ALA   B 1 134 ? 37.926 -31.608 4.198   1.00 16.45 ?  134  ALA   B CB   1 
ATOM   6014 H  H    . ALA   B 1 134 ? 40.294 -31.883 4.920   1.00 18.56 ?  134  ALA   B H    1 
ATOM   6015 H  HA   . ALA   B 1 134 ? 38.064 -33.291 5.356   1.00 18.84 ?  134  ALA   B HA   1 
ATOM   6016 H  HB1  . ALA   B 1 134 ? 37.041 -31.825 3.865   1.00 19.77 ?  134  ALA   B HB1  1 
ATOM   6017 H  HB2  . ALA   B 1 134 ? 37.857 -31.002 4.952   1.00 19.77 ?  134  ALA   B HB2  1 
ATOM   6018 H  HB3  . ALA   B 1 134 ? 38.456 -31.204 3.495   1.00 19.77 ?  134  ALA   B HB3  1 
ATOM   6019 N  N    . ASP   B 1 135 ? 37.562 -34.508 3.205   1.00 15.59 ?  135  ASP   B N    1 
ATOM   6020 C  CA   . ASP   B 1 135 ? 37.464 -35.410 2.065   1.00 16.38 ?  135  ASP   B CA   1 
ATOM   6021 C  C    . ASP   B 1 135 ? 37.558 -34.573 0.796   1.00 15.36 ?  135  ASP   B C    1 
ATOM   6022 O  O    . ASP   B 1 135 ? 36.702 -33.707 0.577   1.00 15.45 ?  135  ASP   B O    1 
ATOM   6023 C  CB   . ASP   B 1 135 ? 36.117 -36.135 2.123   1.00 18.00 ?  135  ASP   B CB   1 
ATOM   6024 C  CG   . ASP   B 1 135 ? 35.925 -37.129 0.989   1.00 20.02 ?  135  ASP   B CG   1 
ATOM   6025 O  OD1  . ASP   B 1 135 ? 36.786 -37.184 0.084   1.00 20.05 ?  135  ASP   B OD1  1 
ATOM   6026 O  OD2  . ASP   B 1 135 ? 34.914 -37.873 1.017   1.00 22.79 -1 135  ASP   B OD2  1 
ATOM   6027 H  H    . ASP   B 1 135 ? 36.835 -34.429 3.654   1.00 18.73 ?  135  ASP   B H    1 
ATOM   6028 H  HA   . ASP   B 1 135 ? 38.183 -36.065 2.096   1.00 19.68 ?  135  ASP   B HA   1 
ATOM   6029 H  HB2  . ASP   B 1 135 ? 36.063 -36.621 2.958   1.00 21.63 ?  135  ASP   B HB2  1 
ATOM   6030 H  HB3  . ASP   B 1 135 ? 35.411 -35.473 2.074   1.00 21.63 ?  135  ASP   B HB3  1 
ATOM   6031 N  N    . PRO   B 1 136 ? 38.570 -34.773 -0.052  1.00 15.44 ?  136  PRO   B N    1 
ATOM   6032 C  CA   . PRO   B 1 136 ? 38.665 -33.948 -1.266  1.00 14.75 ?  136  PRO   B CA   1 
ATOM   6033 C  C    . PRO   B 1 136 ? 37.474 -34.103 -2.191  1.00 14.09 ?  136  PRO   B C    1 
ATOM   6034 O  O    . PRO   B 1 136 ? 37.141 -33.156 -2.912  1.00 13.44 ?  136  PRO   B O    1 
ATOM   6035 C  CB   . PRO   B 1 136 ? 39.976 -34.418 -1.914  1.00 15.72 ?  136  PRO   B CB   1 
ATOM   6036 C  CG   . PRO   B 1 136 ? 40.183 -35.802 -1.377  1.00 16.73 ?  136  PRO   B CG   1 
ATOM   6037 C  CD   . PRO   B 1 136 ? 39.653 -35.765 0.025   1.00 16.31 ?  136  PRO   B CD   1 
ATOM   6038 H  HA   . PRO   B 1 136 ? 38.753 -33.011 -1.031  1.00 17.73 ?  136  PRO   B HA   1 
ATOM   6039 H  HB2  . PRO   B 1 136 ? 39.879 -34.437 -2.881  1.00 18.89 ?  136  PRO   B HB2  1 
ATOM   6040 H  HB3  . PRO   B 1 136 ? 40.701 -33.833 -1.651  1.00 18.89 ?  136  PRO   B HB3  1 
ATOM   6041 H  HG2  . PRO   B 1 136 ? 39.688 -36.440 -1.912  1.00 20.10 ?  136  PRO   B HG2  1 
ATOM   6042 H  HG3  . PRO   B 1 136 ? 41.130 -36.014 -1.376  1.00 20.10 ?  136  PRO   B HG3  1 
ATOM   6043 H  HD2  . PRO   B 1 136 ? 39.295 -36.632 0.276   1.00 19.60 ?  136  PRO   B HD2  1 
ATOM   6044 H  HD3  . PRO   B 1 136 ? 40.339 -35.471 0.647   1.00 19.60 ?  136  PRO   B HD3  1 
ATOM   6045 N  N    . ILE   B 1 137 ? 36.820 -35.270 -2.196  1.00 14.45 ?  137  ILE   B N    1 
ATOM   6046 C  CA   . ILE   B 1 137 ? 35.602 -35.438 -2.984  1.00 15.22 ?  137  ILE   B CA   1 
ATOM   6047 C  C    . ILE   B 1 137 ? 34.527 -34.473 -2.506  1.00 14.92 ?  137  ILE   B C    1 
ATOM   6048 O  O    . ILE   B 1 137 ? 33.805 -33.866 -3.308  1.00 14.52 ?  137  ILE   B O    1 
ATOM   6049 C  CB   . ILE   B 1 137 ? 35.128 -36.904 -2.925  1.00 17.36 ?  137  ILE   B CB   1 
ATOM   6050 C  CG1  . ILE   B 1 137 ? 36.114 -37.805 -3.667  1.00 19.87 ?  137  ILE   B CG1  1 
ATOM   6051 C  CG2  . ILE   B 1 137 ? 33.725 -37.042 -3.514  1.00 17.68 ?  137  ILE   B CG2  1 
ATOM   6052 C  CD1  . ILE   B 1 137 ? 35.796 -39.283 -3.562  1.00 21.96 ?  137  ILE   B CD1  1 
ATOM   6053 H  H    . ILE   B 1 137 ? 37.059 -35.971 -1.759  1.00 17.37 ?  137  ILE   B H    1 
ATOM   6054 H  HA   . ILE   B 1 137 ? 35.792 -35.232 -3.912  1.00 18.29 ?  137  ILE   B HA   1 
ATOM   6055 H  HB   . ILE   B 1 137 ? 35.094 -37.185 -2.001  1.00 20.86 ?  137  ILE   B HB   1 
ATOM   6056 H  HG12 . ILE   B 1 137 ? 36.109 -37.572 -4.609  1.00 23.87 ?  137  ILE   B HG12 1 
ATOM   6057 H  HG13 . ILE   B 1 137 ? 36.999 -37.670 -3.298  1.00 23.87 ?  137  ILE   B HG13 1 
ATOM   6058 H  HG21 . ILE   B 1 137 ? 33.472 -37.980 -3.544  1.00 21.25 ?  137  ILE   B HG21 1 
ATOM   6059 H  HG22 . ILE   B 1 137 ? 33.093 -36.567 -2.957  1.00 21.25 ?  137  ILE   B HG22 1 
ATOM   6060 H  HG23 . ILE   B 1 137 ? 33.721 -36.676 -4.412  1.00 21.25 ?  137  ILE   B HG23 1 
ATOM   6061 H  HD11 . ILE   B 1 137 ? 36.456 -39.770 -4.073  1.00 26.38 ?  137  ILE   B HD11 1 
ATOM   6062 H  HD12 . ILE   B 1 137 ? 35.828 -39.551 -2.629  1.00 26.38 ?  137  ILE   B HD12 1 
ATOM   6063 H  HD13 . ILE   B 1 137 ? 34.914 -39.458 -3.927  1.00 26.38 ?  137  ILE   B HD13 1 
ATOM   6064 N  N    A HIS   B 1 138 ? 34.402 -34.323 -1.191  0.60 14.92 ?  138  HIS   B N    1 
ATOM   6065 N  N    B HIS   B 1 138 ? 34.400 -34.312 -1.189  0.40 14.78 ?  138  HIS   B N    1 
ATOM   6066 C  CA   A HIS   B 1 138 ? 33.454 -33.364 -0.643  0.60 15.26 ?  138  HIS   B CA   1 
ATOM   6067 C  CA   B HIS   B 1 138 ? 33.430 -33.354 -0.672  0.40 14.87 ?  138  HIS   B CA   1 
ATOM   6068 C  C    A HIS   B 1 138 ? 33.860 -31.934 -0.972  0.60 14.22 ?  138  HIS   B C    1 
ATOM   6069 C  C    B HIS   B 1 138 ? 33.853 -31.920 -0.968  0.40 14.14 ?  138  HIS   B C    1 
ATOM   6070 O  O    A HIS   B 1 138 ? 33.007 -31.097 -1.290  0.60 14.74 ?  138  HIS   B O    1 
ATOM   6071 O  O    B HIS   B 1 138 ? 33.007 -31.066 -1.257  0.40 14.53 ?  138  HIS   B O    1 
ATOM   6072 C  CB   A HIS   B 1 138 ? 33.363 -33.556 0.865   0.60 16.51 ?  138  HIS   B CB   1 
ATOM   6073 C  CB   B HIS   B 1 138 ? 33.228 -33.547 0.827   0.40 15.68 ?  138  HIS   B CB   1 
ATOM   6074 C  CG   A HIS   B 1 138 ? 32.483 -32.558 1.540   0.60 17.41 ?  138  HIS   B CG   1 
ATOM   6075 C  CG   B HIS   B 1 138 ? 32.252 -32.581 1.420   0.40 15.99 ?  138  HIS   B CG   1 
ATOM   6076 N  ND1  A HIS   B 1 138 ? 31.131 -32.469 1.287   0.60 18.38 ?  138  HIS   B ND1  1 
ATOM   6077 N  ND1  B HIS   B 1 138 ? 30.921 -32.560 1.065   0.40 16.43 ?  138  HIS   B ND1  1 
ATOM   6078 C  CD2  A HIS   B 1 138 ? 32.760 -31.594 2.449   0.60 17.74 ?  138  HIS   B CD2  1 
ATOM   6079 C  CD2  B HIS   B 1 138 ? 32.417 -31.586 2.322   0.40 16.09 ?  138  HIS   B CD2  1 
ATOM   6080 C  CE1  A HIS   B 1 138 ? 30.612 -31.499 2.017   0.60 18.33 ?  138  HIS   B CE1  1 
ATOM   6081 C  CE1  B HIS   B 1 138 ? 30.304 -31.602 1.733   0.40 16.40 ?  138  HIS   B CE1  1 
ATOM   6082 N  NE2  A HIS   B 1 138 ? 31.579 -30.953 2.732   0.60 17.97 ?  138  HIS   B NE2  1 
ATOM   6083 N  NE2  B HIS   B 1 138 ? 31.189 -30.996 2.504   0.40 16.14 ?  138  HIS   B NE2  1 
ATOM   6084 H  H    A HIS   B 1 138 ? 34.858 -34.757 -0.604  0.60 17.93 ?  138  HIS   B H    1 
ATOM   6085 H  H    B HIS   B 1 138 ? 34.854 -34.735 -0.593  0.40 17.77 ?  138  HIS   B H    1 
ATOM   6086 H  HA   A HIS   B 1 138 ? 32.578 -33.535 -1.025  0.60 18.33 ?  138  HIS   B HA   1 
ATOM   6087 H  HA   B HIS   B 1 138 ? 32.577 -33.513 -1.107  0.40 17.87 ?  138  HIS   B HA   1 
ATOM   6088 H  HB2  A HIS   B 1 138 ? 33.003 -34.443 1.046   0.60 19.84 ?  138  HIS   B HB2  1 
ATOM   6089 H  HB2  B HIS   B 1 138 ? 32.890 -34.445 0.986   0.40 18.85 ?  138  HIS   B HB2  1 
ATOM   6090 H  HB3  A HIS   B 1 138 ? 34.249 -33.479 1.245   0.60 19.84 ?  138  HIS   B HB3  1 
ATOM   6091 H  HB3  B HIS   B 1 138 ? 34.077 -33.430 1.277   0.40 18.85 ?  138  HIS   B HB3  1 
ATOM   6092 H  HD1  B HIS   B 1 138 ? 30.549 -33.091 0.502   0.40 19.74 ?  138  HIS   B HD1  1 
ATOM   6093 H  HD2  A HIS   B 1 138 ? 33.591 -31.409 2.814   0.60 21.31 ?  138  HIS   B HD2  1 
ATOM   6094 H  HD2  B HIS   B 1 138 ? 33.212 -31.350 2.745   0.40 19.33 ?  138  HIS   B HD2  1 
ATOM   6095 H  HE1  A HIS   B 1 138 ? 29.715 -31.251 2.028   0.60 22.02 ?  138  HIS   B HE1  1 
ATOM   6096 H  HE1  B HIS   B 1 138 ? 29.401 -31.390 1.672   0.40 19.71 ?  138  HIS   B HE1  1 
ATOM   6097 H  HE2  A HIS   B 1 138 ? 31.483 -30.304 3.283   0.60 21.59 ?  138  HIS   B HE2  1 
ATOM   6098 N  N    . SER   B 1 139 ? 35.152 -31.627 -0.895  1.00 13.61 ?  139  SER   B N    1 
ATOM   6099 C  CA   . SER   B 1 139 ? 35.596 -30.277 -1.211  1.00 13.27 ?  139  SER   B CA   1 
ATOM   6100 C  C    . SER   B 1 139 ? 35.253 -29.919 -2.649  1.00 12.55 ?  139  SER   B C    1 
ATOM   6101 O  O    . SER   B 1 139 ? 34.801 -28.802 -2.923  1.00 12.44 ?  139  SER   B O    1 
ATOM   6102 C  CB   . SER   B 1 139 ? 37.092 -30.134 -0.946  1.00 13.40 ?  139  SER   B CB   1 
ATOM   6103 O  OG   . SER   B 1 139 ? 37.499 -28.803 -1.218  1.00 13.33 ?  139  SER   B OG   1 
ATOM   6104 H  H    A SER   B 1 139 ? 35.773 -32.174 -0.672  0.60 16.36 ?  139  SER   B H    1 
ATOM   6105 H  H    B SER   B 1 139 ? 35.771 -32.179 -0.677  0.40 16.36 ?  139  SER   B H    1 
ATOM   6106 H  HA   . SER   B 1 139 ? 35.129 -29.656 -0.637  1.00 15.96 ?  139  SER   B HA   1 
ATOM   6107 H  HB2  . SER   B 1 139 ? 37.272 -30.340 -0.015  1.00 16.11 ?  139  SER   B HB2  1 
ATOM   6108 H  HB3  . SER   B 1 139 ? 37.582 -30.741 -1.524  1.00 16.11 ?  139  SER   B HB3  1 
ATOM   6109 H  HG   . SER   B 1 139 ? 38.324 -28.714 -1.070  1.00 16.02 ?  139  SER   B HG   1 
ATOM   6110 N  N    . LEU   B 1 140 ? 35.430 -30.863 -3.578  1.00 12.45 ?  140  LEU   B N    1 
ATOM   6111 C  CA   . LEU   B 1 140 ? 35.065 -30.607 -4.966  1.00 12.46 ?  140  LEU   B CA   1 
ATOM   6112 C  C    . LEU   B 1 140 ? 33.562 -30.388 -5.097  1.00 12.72 ?  140  LEU   B C    1 
ATOM   6113 O  O    . LEU   B 1 140 ? 33.121 -29.496 -5.827  1.00 12.81 ?  140  LEU   B O    1 
ATOM   6114 C  CB   . LEU   B 1 140 ? 35.540 -31.760 -5.850  1.00 12.60 ?  140  LEU   B CB   1 
ATOM   6115 C  CG   . LEU   B 1 140 ? 35.167 -31.665 -7.322  1.00 12.70 ?  140  LEU   B CG   1 
ATOM   6116 C  CD1  . LEU   B 1 140 ? 35.741 -30.390 -7.917  1.00 13.42 ?  140  LEU   B CD1  1 
ATOM   6117 C  CD2  . LEU   B 1 140 ? 35.644 -32.887 -8.080  1.00 13.59 ?  140  LEU   B CD2  1 
ATOM   6118 H  H    . LEU   B 1 140 ? 35.759 -31.640 -3.434  1.00 14.97 ?  140  LEU   B H    1 
ATOM   6119 H  HA   . LEU   B 1 140 ? 35.515 -29.797 -5.263  1.00 14.97 ?  140  LEU   B HA   1 
ATOM   6120 H  HB2  . LEU   B 1 140 ? 36.512 -31.805 -5.802  1.00 15.14 ?  140  LEU   B HB2  1 
ATOM   6121 H  HB3  . LEU   B 1 140 ? 35.163 -32.584 -5.513  1.00 15.14 ?  140  LEU   B HB3  1 
ATOM   6122 H  HG   . LEU   B 1 140 ? 34.205 -31.617 -7.400  1.00 15.26 ?  140  LEU   B HG   1 
ATOM   6123 H  HD11 . LEU   B 1 140 ? 35.620 -30.410 -8.878  1.00 16.13 ?  140  LEU   B HD11 1 
ATOM   6124 H  HD12 . LEU   B 1 140 ? 35.269 -29.625 -7.543  1.00 16.13 ?  140  LEU   B HD12 1 
ATOM   6125 H  HD13 . LEU   B 1 140 ? 36.683 -30.333 -7.702  1.00 16.13 ?  140  LEU   B HD13 1 
ATOM   6126 H  HD21 . LEU   B 1 140 ? 35.387 -32.789 -9.012  1.00 16.34 ?  140  LEU   B HD21 1 
ATOM   6127 H  HD22 . LEU   B 1 140 ? 36.605 -32.948 -8.004  1.00 16.34 ?  140  LEU   B HD22 1 
ATOM   6128 H  HD23 . LEU   B 1 140 ? 35.221 -33.668 -7.699  1.00 16.34 ?  140  LEU   B HD23 1 
ATOM   6129 N  N    . ARG   B 1 141 ? 32.767 -31.183 -4.378  1.00 12.80 ?  141  ARG   B N    1 
ATOM   6130 C  CA   . ARG   B 1 141 ? 31.316 -31.011 -4.356  1.00 13.83 ?  141  ARG   B CA   1 
ATOM   6131 C  C    . ARG   B 1 141 ? 30.935 -29.600 -3.923  1.00 13.22 ?  141  ARG   B C    1 
ATOM   6132 O  O    . ARG   B 1 141 ? 30.132 -28.922 -4.579  1.00 13.36 ?  141  ARG   B O    1 
ATOM   6133 C  CB   . ARG   B 1 141 ? 30.740 -32.049 -3.382  1.00 15.56 ?  141  ARG   B CB   1 
ATOM   6134 C  CG   . ARG   B 1 141 ? 29.279 -31.942 -3.028  1.00 17.65 ?  141  ARG   B CG   1 
ATOM   6135 C  CD   . ARG   B 1 141 ? 28.463 -32.561 -4.089  1.00 19.70 ?  141  ARG   B CD   1 
ATOM   6136 N  NE   . ARG   B 1 141 ? 28.198 -31.649 -5.188  1.00 20.12 ?  141  ARG   B NE   1 
ATOM   6137 C  CZ   . ARG   B 1 141 ? 28.195 -31.993 -6.468  1.00 19.55 ?  141  ARG   B CZ   1 
ATOM   6138 N  NH1  . ARG   B 1 141 ? 28.646 -33.171 -6.870  1.00 19.46 ?  141  ARG   B NH1  1 
ATOM   6139 N  NH2  . ARG   B 1 141 ? 27.724 -31.132 -7.366  1.00 20.57 ?  141  ARG   B NH2  1 
ATOM   6140 H  H    . ARG   B 1 141 ? 33.053 -31.830 -3.893  1.00 15.38 ?  141  ARG   B H    1 
ATOM   6141 H  HA   . ARG   B 1 141 ? 30.957 -31.178 -5.241  1.00 16.63 ?  141  ARG   B HA   1 
ATOM   6142 H  HB2  . ARG   B 1 141 ? 30.891 -32.932 -3.763  1.00 18.70 ?  141  ARG   B HB2  1 
ATOM   6143 H  HB3  . ARG   B 1 141 ? 31.239 -31.989 -2.552  1.00 18.70 ?  141  ARG   B HB3  1 
ATOM   6144 H  HG2  . ARG   B 1 141 ? 29.123 -32.409 -2.194  1.00 21.20 ?  141  ARG   B HG2  1 
ATOM   6145 H  HG3  . ARG   B 1 141 ? 29.029 -31.008 -2.943  1.00 21.20 ?  141  ARG   B HG3  1 
ATOM   6146 H  HD2  . ARG   B 1 141 ? 28.930 -33.345 -4.431  1.00 23.67 ?  141  ARG   B HD2  1 
ATOM   6147 H  HD3  . ARG   B 1 141 ? 27.618 -32.832 -3.710  1.00 23.67 ?  141  ARG   B HD3  1 
ATOM   6148 H  HE   . ARG   B 1 141 ? 28.037 -30.826 -4.992  1.00 24.17 ?  141  ARG   B HE   1 
ATOM   6149 H  HH11 . ARG   B 1 141 ? 28.945 -33.742 -6.301  1.00 23.38 ?  141  ARG   B HH11 1 
ATOM   6150 H  HH12 . ARG   B 1 141 ? 28.641 -33.365 -7.705  1.00 23.38 ?  141  ARG   B HH12 1 
ATOM   6151 H  HH21 . ARG   B 1 141 ? 27.436 -30.360 -7.114  1.00 24.71 ?  141  ARG   B HH21 1 
ATOM   6152 H  HH22 . ARG   B 1 141 ? 27.733 -31.333 -8.201  1.00 24.71 ?  141  ARG   B HH22 1 
ATOM   6153 N  N    . VAL   B 1 142 ? 31.480 -29.155 -2.795  1.00 12.72 ?  142  VAL   B N    1 
ATOM   6154 C  CA   . VAL   B 1 142 ? 31.146 -27.822 -2.307  1.00 12.39 ?  142  VAL   B CA   1 
ATOM   6155 C  C    . VAL   B 1 142 ? 31.617 -26.761 -3.295  1.00 12.36 ?  142  VAL   B C    1 
ATOM   6156 O  O    . VAL   B 1 142 ? 30.910 -25.778 -3.548  1.00 12.77 ?  142  VAL   B O    1 
ATOM   6157 C  CB   . VAL   B 1 142 ? 31.697 -27.596 -0.887  1.00 13.35 ?  142  VAL   B CB   1 
ATOM   6158 C  CG1  . VAL   B 1 142 ? 31.374 -26.175 -0.407  1.00 13.20 ?  142  VAL   B CG1  1 
ATOM   6159 C  CG2  . VAL   B 1 142 ? 31.122 -28.623 0.069   1.00 14.46 ?  142  VAL   B CG2  1 
ATOM   6160 H  H    . VAL   B 1 142 ? 32.037 -29.592 -2.310  1.00 15.30 ?  142  VAL   B H    1 
ATOM   6161 H  HA   . VAL   B 1 142 ? 30.186 -27.753 -2.254  1.00 14.90 ?  142  VAL   B HA   1 
ATOM   6162 H  HB   . VAL   B 1 142 ? 32.662 -27.704 -0.896  1.00 16.04 ?  142  VAL   B HB   1 
ATOM   6163 H  HG11 . VAL   B 1 142 ? 31.555 -26.115 0.543   1.00 15.87 ?  142  VAL   B HG11 1 
ATOM   6164 H  HG12 . VAL   B 1 142 ? 31.929 -25.543 -0.890  1.00 15.87 ?  142  VAL   B HG12 1 
ATOM   6165 H  HG13 . VAL   B 1 142 ? 30.437 -25.991 -0.577  1.00 15.87 ?  142  VAL   B HG13 1 
ATOM   6166 H  HG21 . VAL   B 1 142 ? 31.454 -28.444 0.960   1.00 17.38 ?  142  VAL   B HG21 1 
ATOM   6167 H  HG22 . VAL   B 1 142 ? 30.154 -28.557 0.054   1.00 17.38 ?  142  VAL   B HG22 1 
ATOM   6168 H  HG23 . VAL   B 1 142 ? 31.396 -29.510 -0.215  1.00 17.38 ?  142  VAL   B HG23 1 
ATOM   6169 N  N    . CYS   B 1 143 ? 32.802 -26.950 -3.881  1.00 11.89 ?  143  CYS   B N    1 
ATOM   6170 C  CA   . CYS   B 1 143 ? 33.293 -26.012 -4.887  1.00 11.94 ?  143  CYS   B CA   1 
ATOM   6171 C  C    . CYS   B 1 143 ? 32.286 -25.863 -6.023  1.00 12.03 ?  143  CYS   B C    1 
ATOM   6172 O  O    . CYS   B 1 143 ? 31.874 -24.752 -6.374  1.00 12.28 ?  143  CYS   B O    1 
ATOM   6173 C  CB   . CYS   B 1 143 ? 34.643 -26.502 -5.421  1.00 12.39 ?  143  CYS   B CB   1 
ATOM   6174 S  SG   . CYS   B 1 143 ? 35.393 -25.386 -6.632  1.00 12.49 ?  143  CYS   B SG   1 
ATOM   6175 H  H    . CYS   B 1 143 ? 33.333 -27.603 -3.715  1.00 14.30 ?  143  CYS   B H    1 
ATOM   6176 H  HA   . CYS   B 1 143 ? 33.425 -25.140 -4.479  1.00 14.35 ?  143  CYS   B HA   1 
ATOM   6177 H  HB2  . CYS   B 1 143 ? 35.266 -26.593 -4.681  1.00 14.90 ?  143  CYS   B HB2  1 
ATOM   6178 H  HB3  . CYS   B 1 143 ? 34.519 -27.360 -5.848  1.00 14.90 ?  143  CYS   B HB3  1 
ATOM   6179 H  HG   . CYS   B 1 143 ? 36.461 -25.825 -6.966  1.00 15.02 ?  143  CYS   B HG   1 
ATOM   6180 N  N    . VAL   B 1 144 ? 31.875 -26.982 -6.611  1.00 12.59 ?  144  VAL   B N    1 
ATOM   6181 C  CA   . VAL   B 1 144 ? 30.970 -26.930 -7.753  1.00 13.46 ?  144  VAL   B CA   1 
ATOM   6182 C  C    . VAL   B 1 144 ? 29.635 -26.309 -7.368  1.00 13.63 ?  144  VAL   B C    1 
ATOM   6183 O  O    . VAL   B 1 144 ? 29.014 -25.600 -8.169  1.00 14.84 ?  144  VAL   B O    1 
ATOM   6184 C  CB   . VAL   B 1 144 ? 30.808 -28.337 -8.336  1.00 16.20 ?  144  VAL   B CB   1 
ATOM   6185 C  CG1  . VAL   B 1 144 ? 29.551 -28.445 -9.190  1.00 18.87 ?  144  VAL   B CG1  1 
ATOM   6186 C  CG2  . VAL   B 1 144 ? 32.065 -28.729 -9.108  1.00 16.28 ?  144  VAL   B CG2  1 
ATOM   6187 H  H    . VAL   B 1 144 ? 32.114 -27.776 -6.383  1.00 15.13 ?  144  VAL   B H    1 
ATOM   6188 H  HA   . VAL   B 1 144 ? 31.362 -26.370 -8.442  1.00 16.18 ?  144  VAL   B HA   1 
ATOM   6189 H  HB   . VAL   B 1 144 ? 30.716 -28.967 -7.599  1.00 19.47 ?  144  VAL   B HB   1 
ATOM   6190 H  HG11 . VAL   B 1 144 ? 29.636 -29.224 -9.766  1.00 22.67 ?  144  VAL   B HG11 1 
ATOM   6191 H  HG12 . VAL   B 1 144 ? 28.786 -28.549 -8.609  1.00 22.67 ?  144  VAL   B HG12 1 
ATOM   6192 H  HG13 . VAL   B 1 144 ? 29.468 -27.646 -9.727  1.00 22.67 ?  144  VAL   B HG13 1 
ATOM   6193 H  HG21 . VAL   B 1 144 ? 31.953 -29.626 -9.461  1.00 19.56 ?  144  VAL   B HG21 1 
ATOM   6194 H  HG22 . VAL   B 1 144 ? 32.197 -28.101 -9.834  1.00 19.56 ?  144  VAL   B HG22 1 
ATOM   6195 H  HG23 . VAL   B 1 144 ? 32.827 -28.705 -8.506  1.00 19.56 ?  144  VAL   B HG23 1 
ATOM   6196 N  N    . ASP   B 1 145 ? 29.172 -26.564 -6.148  1.00 13.69 ?  145  ASP   B N    1 
ATOM   6197 C  CA   . ASP   B 1 145 ? 27.861 -26.100 -5.713  1.00 14.41 ?  145  ASP   B CA   1 
ATOM   6198 C  C    . ASP   B 1 145 ? 27.885 -24.678 -5.162  1.00 13.84 ?  145  ASP   B C    1 
ATOM   6199 O  O    . ASP   B 1 145 ? 26.822 -24.136 -4.834  1.00 15.58 ?  145  ASP   B O    1 
ATOM   6200 C  CB   . ASP   B 1 145 ? 27.283 -27.029 -4.639  1.00 15.86 ?  145  ASP   B CB   1 
ATOM   6201 C  CG   . ASP   B 1 145 ? 26.915 -28.401 -5.158  1.00 17.74 ?  145  ASP   B CG   1 
ATOM   6202 O  OD1  . ASP   B 1 145 ? 26.809 -28.591 -6.386  1.00 18.31 ?  145  ASP   B OD1  1 
ATOM   6203 O  OD2  . ASP   B 1 145 ? 26.721 -29.291 -4.308  1.00 20.19 -1 145  ASP   B OD2  1 
ATOM   6204 H  H    . ASP   B 1 145 ? 29.614 -26.986 -5.546  1.00 16.45 ?  145  ASP   B H    1 
ATOM   6205 H  HA   . ASP   B 1 145 ? 27.266 -26.098 -6.472  1.00 17.32 ?  145  ASP   B HA   1 
ATOM   6206 H  HB2  . ASP   B 1 145 ? 27.934 -27.156 -3.944  1.00 19.06 ?  145  ASP   B HB2  1 
ATOM   6207 H  HB3  . ASP   B 1 145 ? 26.475 -26.628 -4.285  1.00 19.06 ?  145  ASP   B HB3  1 
ATOM   6208 N  N    . THR   B 1 146 ? 29.062 -24.059 -5.047  1.00 12.24 ?  146  THR   B N    1 
ATOM   6209 C  CA   . THR   B 1 146 ? 29.190 -22.736 -4.441  1.00 11.99 ?  146  THR   B CA   1 
ATOM   6210 C  C    . THR   B 1 146 ? 29.823 -21.704 -5.359  1.00 11.83 ?  146  THR   B C    1 
ATOM   6211 O  O    . THR   B 1 146 ? 29.368 -20.548 -5.400  1.00 12.24 ?  146  THR   B O    1 
ATOM   6212 C  CB   . THR   B 1 146 ? 30.022 -22.844 -3.153  1.00 12.31 ?  146  THR   B CB   1 
ATOM   6213 O  OG1  . THR   B 1 146 ? 29.458 -23.840 -2.291  1.00 12.45 ?  146  THR   B OG1  1 
ATOM   6214 C  CG2  . THR   B 1 146 ? 30.108 -21.504 -2.433  1.00 12.71 ?  146  THR   B CG2  1 
ATOM   6215 H  H    . THR   B 1 146 ? 29.814 -24.388 -5.318  1.00 14.72 ?  146  THR   B H    1 
ATOM   6216 H  HA   . THR   B 1 146 ? 28.317 -22.412 -4.201  1.00 14.42 ?  146  THR   B HA   1 
ATOM   6217 H  HB   . THR   B 1 146 ? 30.926 -23.106 -3.383  1.00 14.80 ?  146  THR   B HB   1 
ATOM   6218 H  HG1  . THR   B 1 146 ? 29.492 -24.598 -2.672  1.00 14.96 ?  146  THR   B HG1  1 
ATOM   6219 H  HG21 . THR   B 1 146 ? 30.464 -21.627 -1.541  1.00 15.28 ?  146  THR   B HG21 1 
ATOM   6220 H  HG22 . THR   B 1 146 ? 30.696 -20.900 -2.922  1.00 15.28 ?  146  THR   B HG22 1 
ATOM   6221 H  HG23 . THR   B 1 146 ? 29.229 -21.102 -2.370  1.00 15.28 ?  146  THR   B HG23 1 
ATOM   6222 N  N    . VAL   B 1 147 ? 30.883 -22.074 -6.066  1.00 11.83 ?  147  VAL   B N    1 
ATOM   6223 C  CA   . VAL   B 1 147 ? 31.608 -21.127 -6.899  1.00 11.38 ?  147  VAL   B CA   1 
ATOM   6224 C  C    . VAL   B 1 147 ? 30.876 -20.991 -8.222  1.00 11.56 ?  147  VAL   B C    1 
ATOM   6225 O  O    . VAL   B 1 147 ? 30.507 -21.994 -8.848  1.00 12.47 ?  147  VAL   B O    1 
ATOM   6226 C  CB   . VAL   B 1 147 ? 33.061 -21.582 -7.105  1.00 11.46 ?  147  VAL   B CB   1 
ATOM   6227 C  CG1  . VAL   B 1 147 ? 33.821 -20.548 -7.907  1.00 11.74 ?  147  VAL   B CG1  1 
ATOM   6228 C  CG2  . VAL   B 1 147 ? 33.740 -21.802 -5.765  1.00 11.86 ?  147  VAL   B CG2  1 
ATOM   6229 H  H    . VAL   B 1 147 ? 31.210 -22.876 -6.082  1.00 14.22 ?  147  VAL   B H    1 
ATOM   6230 H  HA   . VAL   B 1 147 ? 31.625 -20.264 -6.465  1.00 13.69 ?  147  VAL   B HA   1 
ATOM   6231 H  HB   . VAL   B 1 147 ? 33.077 -22.423 -7.597  1.00 13.78 ?  147  VAL   B HB   1 
ATOM   6232 H  HG11 . VAL   B 1 147 ? 34.767 -20.769 -7.897  1.00 14.11 ?  147  VAL   B HG11 1 
ATOM   6233 H  HG12 . VAL   B 1 147 ? 33.494 -20.543 -8.818  1.00 14.11 ?  147  VAL   B HG12 1 
ATOM   6234 H  HG13 . VAL   B 1 147 ? 33.686 -19.676 -7.500  1.00 14.11 ?  147  VAL   B HG13 1 
ATOM   6235 H  HG21 . VAL   B 1 147 ? 34.681 -21.992 -5.913  1.00 14.26 ?  147  VAL   B HG21 1 
ATOM   6236 H  HG22 . VAL   B 1 147 ? 33.649 -20.994 -5.233  1.00 14.26 ?  147  VAL   B HG22 1 
ATOM   6237 H  HG23 . VAL   B 1 147 ? 33.319 -22.546 -5.312  1.00 14.26 ?  147  VAL   B HG23 1 
ATOM   6238 N  N    . ARG   B 1 148 ? 30.663 -19.744 -8.641  1.00 11.44 ?  148  ARG   B N    1 
ATOM   6239 C  CA   . ARG   B 1 148 ? 30.038 -19.425 -9.912  1.00 11.77 ?  148  ARG   B CA   1 
ATOM   6240 C  C    . ARG   B 1 148 ? 30.986 -18.743 -10.885 1.00 11.90 ?  148  ARG   B C    1 
ATOM   6241 O  O    . ARG   B 1 148 ? 30.698 -18.725 -12.086 1.00 13.22 ?  148  ARG   B O    1 
ATOM   6242 C  CB   . ARG   B 1 148 ? 28.798 -18.547 -9.684  1.00 12.52 ?  148  ARG   B CB   1 
ATOM   6243 C  CG   . ARG   B 1 148 ? 27.731 -19.255 -8.862  1.00 13.33 ?  148  ARG   B CG   1 
ATOM   6244 C  CD   . ARG   B 1 148 ? 26.519 -18.369 -8.561  1.00 13.99 ?  148  ARG   B CD   1 
ATOM   6245 N  NE   . ARG   B 1 148 ? 26.895 -17.169 -7.825  1.00 13.64 ?  148  ARG   B NE   1 
ATOM   6246 C  CZ   . ARG   B 1 148 ? 27.196 -17.138 -6.533  1.00 12.58 ?  148  ARG   B CZ   1 
ATOM   6247 N  NH1  . ARG   B 1 148 ? 27.136 -18.227 -5.781  1.00 12.75 ?  148  ARG   B NH1  1 
ATOM   6248 N  NH2  . ARG   B 1 148 ? 27.585 -15.989 -5.985  1.00 12.79 ?  148  ARG   B NH2  1 
ATOM   6249 H  H    . ARG   B 1 148 ? 30.883 -19.045 -8.179  1.00 13.75 ?  148  ARG   B H    1 
ATOM   6250 H  HA   . ARG   B 1 148 ? 29.744 -20.247 -10.321 1.00 14.15 ?  148  ARG   B HA   1 
ATOM   6251 H  HB2  . ARG   B 1 148 ? 29.063 -17.742 -9.206  1.00 15.05 ?  148  ARG   B HB2  1 
ATOM   6252 H  HB3  . ARG   B 1 148 ? 28.417 -18.313 -10.542 1.00 15.05 ?  148  ARG   B HB3  1 
ATOM   6253 H  HG2  . ARG   B 1 148 ? 27.418 -20.029 -9.355  1.00 16.03 ?  148  ARG   B HG2  1 
ATOM   6254 H  HG3  . ARG   B 1 148 ? 28.114 -19.533 -8.016  1.00 16.03 ?  148  ARG   B HG3  1 
ATOM   6255 H  HD2  . ARG   B 1 148 ? 26.110 -18.095 -9.395  1.00 16.82 ?  148  ARG   B HD2  1 
ATOM   6256 H  HD3  . ARG   B 1 148 ? 25.884 -18.870 -8.024  1.00 16.82 ?  148  ARG   B HD3  1 
ATOM   6257 H  HE   . ARG   B 1 148 ? 26.929 -16.429 -8.256  1.00 16.40 ?  148  ARG   B HE   1 
ATOM   6258 H  HH11 . ARG   B 1 148 ? 26.881 -18.978 -6.119  1.00 15.33 ?  148  ARG   B HH11 1 
ATOM   6259 H  HH12 . ARG   B 1 148 ? 27.329 -18.185 -4.941  1.00 15.33 ?  148  ARG   B HH12 1 
ATOM   6260 H  HH21 . ARG   B 1 148 ? 27.637 -15.280 -6.465  1.00 15.38 ?  148  ARG   B HH21 1 
ATOM   6261 H  HH22 . ARG   B 1 148 ? 27.785 -15.957 -5.147  1.00 15.38 ?  148  ARG   B HH22 1 
ATOM   6262 N  N    . THR   B 1 149 ? 32.098 -18.193 -10.399 1.00 11.72 ?  149  THR   B N    1 
ATOM   6263 C  CA   . THR   B 1 149 ? 33.133 -17.626 -11.248 1.00 11.70 ?  149  THR   B CA   1 
ATOM   6264 C  C    . THR   B 1 149 ? 34.022 -18.759 -11.760 1.00 11.34 ?  149  THR   B C    1 
ATOM   6265 O  O    . THR   B 1 149 ? 33.832 -19.930 -11.421 1.00 12.05 ?  149  THR   B O    1 
ATOM   6266 C  CB   . THR   B 1 149 ? 33.903 -16.573 -10.462 1.00 11.89 ?  149  THR   B CB   1 
ATOM   6267 O  OG1  . THR   B 1 149 ? 34.364 -17.174 -9.250  1.00 11.84 ?  149  THR   B OG1  1 
ATOM   6268 C  CG2  . THR   B 1 149 ? 33.008 -15.374 -10.157 1.00 12.49 ?  149  THR   B CG2  1 
ATOM   6269 H  H    . THR   B 1 149 ? 32.270 -18.127 -9.557  1.00 14.09 ?  149  THR   B H    1 
ATOM   6270 H  HA   . THR   B 1 149 ? 32.714 -17.191 -12.011 1.00 14.06 ?  149  THR   B HA   1 
ATOM   6271 H  HB   . THR   B 1 149 ? 34.661 -16.273 -10.982 1.00 14.29 ?  149  THR   B HB   1 
ATOM   6272 H  HG1  . THR   B 1 149 ? 34.777 -16.600 -8.789  1.00 14.24 ?  149  THR   B HG1  1 
ATOM   6273 H  HG21 . THR   B 1 149 ? 33.513 -14.700 -9.676  1.00 15.01 ?  149  THR   B HG21 1 
ATOM   6274 H  HG22 . THR   B 1 149 ? 32.679 -14.987 -10.986 1.00 15.01 ?  149  THR   B HG22 1 
ATOM   6275 H  HG23 . THR   B 1 149 ? 32.252 -15.649 -9.617  1.00 15.01 ?  149  THR   B HG23 1 
ATOM   6276 N  N    . ASN   B 1 150 ? 34.987 -18.436 -12.607 1.00 11.57 ?  150  ASN   B N    1 
ATOM   6277 C  CA   . ASN   B 1 150 ? 35.749 -19.463 -13.308 1.00 11.93 ?  150  ASN   B CA   1 
ATOM   6278 C  C    . ASN   B 1 150 ? 36.916 -19.915 -12.440 1.00 11.52 ?  150  ASN   B C    1 
ATOM   6279 O  O    . ASN   B 1 150 ? 37.841 -19.142 -12.174 1.00 12.39 ?  150  ASN   B O    1 
ATOM   6280 C  CB   . ASN   B 1 150 ? 36.219 -18.934 -14.656 1.00 13.52 ?  150  ASN   B CB   1 
ATOM   6281 C  CG   . ASN   B 1 150 ? 35.075 -18.716 -15.601 1.00 16.24 ?  150  ASN   B CG   1 
ATOM   6282 O  OD1  . ASN   B 1 150 ? 34.186 -19.551 -15.701 1.00 17.39 ?  150  ASN   B OD1  1 
ATOM   6283 N  ND2  . ASN   B 1 150 ? 35.070 -17.581 -16.280 1.00 18.13 ?  150  ASN   B ND2  1 
ATOM   6284 H  H    . ASN   B 1 150 ? 35.230 -17.627 -12.787 1.00 13.91 ?  150  ASN   B H    1 
ATOM   6285 H  HA   . ASN   B 1 150 ? 35.168 -20.227 -13.470 1.00 14.34 ?  150  ASN   B HA   1 
ATOM   6286 H  HB2  . ASN   B 1 150 ? 36.666 -18.082 -14.522 1.00 16.25 ?  150  ASN   B HB2  1 
ATOM   6287 H  HB3  . ASN   B 1 150 ? 36.824 -19.573 -15.055 1.00 16.25 ?  150  ASN   B HB3  1 
ATOM   6288 H  HD21 . ASN   B 1 150 ? 34.434 -17.409 -16.836 1.00 21.78 ?  150  ASN   B HD21 1 
ATOM   6289 H  HD22 . ASN   B 1 150 ? 35.710 -17.012 -16.178 1.00 21.78 ?  150  ASN   B HD22 1 
ATOM   6290 N  N    . VAL   B 1 151 ? 36.882 -21.165 -12.000 1.00 11.37 ?  151  VAL   B N    1 
ATOM   6291 C  CA   . VAL   B 1 151 ? 37.904 -21.693 -11.111 1.00 11.27 ?  151  VAL   B CA   1 
ATOM   6292 C  C    . VAL   B 1 151 ? 38.611 -22.863 -11.784 1.00 11.09 ?  151  VAL   B C    1 
ATOM   6293 O  O    . VAL   B 1 151 ? 37.970 -23.803 -12.281 1.00 12.10 ?  151  VAL   B O    1 
ATOM   6294 C  CB   . VAL   B 1 151 ? 37.344 -22.029 -9.713  1.00 12.43 ?  151  VAL   B CB   1 
ATOM   6295 C  CG1  . VAL   B 1 151 ? 36.187 -23.030 -9.786  1.00 13.31 ?  151  VAL   B CG1  1 
ATOM   6296 C  CG2  . VAL   B 1 151 ? 38.455 -22.513 -8.797  1.00 13.17 ?  151  VAL   B CG2  1 
ATOM   6297 H  H    . VAL   B 1 151 ? 36.266 -21.735 -12.207 1.00 13.67 ?  151  VAL   B H    1 
ATOM   6298 H  HA   . VAL   B 1 151 ? 38.569 -20.998 -10.982 1.00 13.55 ?  151  VAL   B HA   1 
ATOM   6299 H  HB   . VAL   B 1 151 ? 36.990 -21.212 -9.328  1.00 14.95 ?  151  VAL   B HB   1 
ATOM   6300 H  HG11 . VAL   B 1 151 ? 35.872 -23.214 -8.888  1.00 16.00 ?  151  VAL   B HG11 1 
ATOM   6301 H  HG12 . VAL   B 1 151 ? 35.468 -22.648 -10.316 1.00 16.00 ?  151  VAL   B HG12 1 
ATOM   6302 H  HG13 . VAL   B 1 151 ? 36.501 -23.850 -10.200 1.00 16.00 ?  151  VAL   B HG13 1 
ATOM   6303 H  HG21 . VAL   B 1 151 ? 38.105 -22.592 -7.895  1.00 15.83 ?  151  VAL   B HG21 1 
ATOM   6304 H  HG22 . VAL   B 1 151 ? 38.768 -23.377 -9.105  1.00 15.83 ?  151  VAL   B HG22 1 
ATOM   6305 H  HG23 . VAL   B 1 151 ? 39.182 -21.871 -8.813  1.00 15.83 ?  151  VAL   B HG23 1 
ATOM   6306 N  N    . TYR   B 1 152 ? 39.942 -22.774 -11.804 1.00 10.65 ?  152  TYR   B N    1 
ATOM   6307 C  CA   . TYR   B 1 152 ? 40.846 -23.753 -12.388 1.00 11.23 ?  152  TYR   B CA   1 
ATOM   6308 C  C    . TYR   B 1 152 ? 41.570 -24.432 -11.230 1.00 10.41 ?  152  TYR   B C    1 
ATOM   6309 O  O    . TYR   B 1 152 ? 42.413 -23.814 -10.570 1.00 10.83 ?  152  TYR   B O    1 
ATOM   6310 C  CB   . TYR   B 1 152 ? 41.812 -23.036 -13.335 1.00 11.94 ?  152  TYR   B CB   1 
ATOM   6311 C  CG   . TYR   B 1 152 ? 41.129 -22.570 -14.596 1.00 12.22 ?  152  TYR   B CG   1 
ATOM   6312 C  CD1  . TYR   B 1 152 ? 40.462 -21.347 -14.657 1.00 12.78 ?  152  TYR   B CD1  1 
ATOM   6313 C  CD2  . TYR   B 1 152 ? 41.129 -23.371 -15.724 1.00 13.11 ?  152  TYR   B CD2  1 
ATOM   6314 C  CE1  . TYR   B 1 152 ? 39.818 -20.948 -15.817 1.00 13.99 ?  152  TYR   B CE1  1 
ATOM   6315 C  CE2  . TYR   B 1 152 ? 40.494 -22.982 -16.882 1.00 14.39 ?  152  TYR   B CE2  1 
ATOM   6316 C  CZ   . TYR   B 1 152 ? 39.841 -21.770 -16.930 1.00 14.73 ?  152  TYR   B CZ   1 
ATOM   6317 O  OH   . TYR   B 1 152 ? 39.207 -21.395 -18.093 1.00 16.97 ?  152  TYR   B OH   1 
ATOM   6318 H  H    . TYR   B 1 152 ? 40.373 -22.111 -11.456 1.00 12.81 ?  152  TYR   B H    1 
ATOM   6319 H  HA   . TYR   B 1 152 ? 40.344 -24.419 -12.887 1.00 13.50 ?  152  TYR   B HA   1 
ATOM   6320 H  HB2  . TYR   B 1 152 ? 42.178 -22.260 -12.879 1.00 14.36 ?  152  TYR   B HB2  1 
ATOM   6321 H  HB3  . TYR   B 1 152 ? 42.528 -23.642 -13.582 1.00 14.36 ?  152  TYR   B HB3  1 
ATOM   6322 H  HD1  . TYR   B 1 152 ? 40.444 -20.796 -13.905 1.00 15.37 ?  152  TYR   B HD1  1 
ATOM   6323 H  HD2  . TYR   B 1 152 ? 41.564 -24.195 -15.695 1.00 15.76 ?  152  TYR   B HD2  1 
ATOM   6324 H  HE1  . TYR   B 1 152 ? 39.380 -20.130 -15.847 1.00 16.81 ?  152  TYR   B HE1  1 
ATOM   6325 H  HE2  . TYR   B 1 152 ? 40.508 -23.536 -17.627 1.00 17.30 ?  152  TYR   B HE2  1 
ATOM   6326 H  HH   . TYR   B 1 152 ? 38.853 -20.642 -17.987 1.00 20.39 ?  152  TYR   B HH   1 
ATOM   6327 N  N    . LEU   B 1 153 ? 41.206 -25.688 -10.965 1.00 10.56 ?  153  LEU   B N    1 
ATOM   6328 C  CA   . LEU   B 1 153 ? 41.710 -26.436 -9.824  1.00 10.24 ?  153  LEU   B CA   1 
ATOM   6329 C  C    . LEU   B 1 153 ? 42.942 -27.234 -10.218 1.00 10.58 ?  153  LEU   B C    1 
ATOM   6330 O  O    . LEU   B 1 153 ? 42.924 -27.960 -11.214 1.00 11.97 ?  153  LEU   B O    1 
ATOM   6331 C  CB   . LEU   B 1 153 ? 40.632 -27.397 -9.321  1.00 10.94 ?  153  LEU   B CB   1 
ATOM   6332 C  CG   . LEU   B 1 153 ? 39.375 -26.749 -8.746  1.00 11.87 ?  153  LEU   B CG   1 
ATOM   6333 C  CD1  . LEU   B 1 153 ? 38.285 -27.800 -8.590  1.00 12.22 ?  153  LEU   B CD1  1 
ATOM   6334 C  CD2  . LEU   B 1 153 ? 39.679 -26.093 -7.408  1.00 12.02 ?  153  LEU   B CD2  1 
ATOM   6335 H  H    . LEU   B 1 153 ? 40.638 -26.132 -11.446 1.00 12.70 ?  153  LEU   B H    1 
ATOM   6336 H  HA   . LEU   B 1 153 ? 41.935 -25.821 -9.114  1.00 12.31 ?  153  LEU   B HA   1 
ATOM   6337 H  HB2  . LEU   B 1 153 ? 40.350 -27.961 -10.057 1.00 13.15 ?  153  LEU   B HB2  1 
ATOM   6338 H  HB3  . LEU   B 1 153 ? 41.017 -27.947 -8.620  1.00 13.15 ?  153  LEU   B HB3  1 
ATOM   6339 H  HG   . LEU   B 1 153 ? 39.055 -26.058 -9.353  1.00 14.27 ?  153  LEU   B HG   1 
ATOM   6340 H  HD11 . LEU   B 1 153 ? 37.482 -27.370 -8.254  1.00 14.69 ?  153  LEU   B HD11 1 
ATOM   6341 H  HD12 . LEU   B 1 153 ? 38.113 -28.197 -9.454  1.00 14.69 ?  153  LEU   B HD12 1 
ATOM   6342 H  HD13 . LEU   B 1 153 ? 38.590 -28.471 -7.964  1.00 14.69 ?  153  LEU   B HD13 1 
ATOM   6343 H  HD21 . LEU   B 1 153 ? 38.864 -25.730 -7.034  1.00 14.45 ?  153  LEU   B HD21 1 
ATOM   6344 H  HD22 . LEU   B 1 153 ? 40.054 -26.759 -6.809  1.00 14.45 ?  153  LEU   B HD22 1 
ATOM   6345 H  HD23 . LEU   B 1 153 ? 40.327 -25.378 -7.545  1.00 14.45 ?  153  LEU   B HD23 1 
ATOM   6346 N  N    . ALA   B 1 154 ? 43.995 -27.126 -9.417  1.00 10.81 ?  154  ALA   B N    1 
ATOM   6347 C  CA   . ALA   B 1 154 ? 45.223 -27.884 -9.606  1.00 11.89 ?  154  ALA   B CA   1 
ATOM   6348 C  C    . ALA   B 1 154 ? 45.296 -28.964 -8.537  1.00 12.39 ?  154  ALA   B C    1 
ATOM   6349 O  O    . ALA   B 1 154 ? 45.221 -28.668 -7.336  1.00 13.75 ?  154  ALA   B O    1 
ATOM   6350 C  CB   . ALA   B 1 154 ? 46.443 -26.967 -9.532  1.00 13.04 ?  154  ALA   B CB   1 
ATOM   6351 H  H    . ALA   B 1 154 ? 44.017 -26.593 -8.736  1.00 13.00 ?  154  ALA   B H    1 
ATOM   6352 H  HA   . ALA   B 1 154 ? 45.213 -28.305 -10.475 1.00 14.30 ?  154  ALA   B HA   1 
ATOM   6353 H  HB1  . ALA   B 1 154 ? 47.247 -27.495 -9.656  1.00 15.67 ?  154  ALA   B HB1  1 
ATOM   6354 H  HB2  . ALA   B 1 154 ? 46.380 -26.291 -10.226 1.00 15.67 ?  154  ALA   B HB2  1 
ATOM   6355 H  HB3  . ALA   B 1 154 ? 46.467 -26.536 -8.658  1.00 15.67 ?  154  ALA   B HB3  1 
ATOM   6356 N  N    . VAL   B 1 155 ? 45.418 -30.211 -8.975  1.00 11.62 ?  155  VAL   B N    1 
ATOM   6357 C  CA   . VAL   B 1 155 ? 45.526 -31.360 -8.087  1.00 11.82 ?  155  VAL   B CA   1 
ATOM   6358 C  C    . VAL   B 1 155 ? 46.869 -32.028 -8.368  1.00 11.81 ?  155  VAL   B C    1 
ATOM   6359 O  O    . VAL   B 1 155 ? 47.105 -32.515 -9.482  1.00 13.66 ?  155  VAL   B O    1 
ATOM   6360 C  CB   . VAL   B 1 155 ? 44.370 -32.353 -8.291  1.00 13.27 ?  155  VAL   B CB   1 
ATOM   6361 C  CG1  . VAL   B 1 155 ? 44.557 -33.564 -7.393  1.00 13.14 ?  155  VAL   B CG1  1 
ATOM   6362 C  CG2  . VAL   B 1 155 ? 43.028 -31.673 -8.009  1.00 14.33 ?  155  VAL   B CG2  1 
ATOM   6363 H  H    . VAL   B 1 155 ? 45.448 -30.420 -9.812  1.00 13.97 ?  155  VAL   B H    1 
ATOM   6364 H  HA   . VAL   B 1 155 ? 45.515 -31.063 -7.166  1.00 14.22 ?  155  VAL   B HA   1 
ATOM   6365 H  HB   . VAL   B 1 155 ? 44.367 -32.653 -9.214  1.00 15.95 ?  155  VAL   B HB   1 
ATOM   6366 H  HG11 . VAL   B 1 155 ? 43.729 -34.067 -7.362  1.00 15.79 ?  155  VAL   B HG11 1 
ATOM   6367 H  HG12 . VAL   B 1 155 ? 45.266 -34.125 -7.755  1.00 15.79 ?  155  VAL   B HG12 1 
ATOM   6368 H  HG13 . VAL   B 1 155 ? 44.797 -33.266 -6.502  1.00 15.79 ?  155  VAL   B HG13 1 
ATOM   6369 H  HG21 . VAL   B 1 155 ? 42.317 -32.325 -8.112  1.00 17.22 ?  155  VAL   B HG21 1 
ATOM   6370 H  HG22 . VAL   B 1 155 ? 43.034 -31.331 -7.100  1.00 17.22 ?  155  VAL   B HG22 1 
ATOM   6371 H  HG23 . VAL   B 1 155 ? 42.903 -30.944 -8.636  1.00 17.22 ?  155  VAL   B HG23 1 
ATOM   6372 N  N    . PHE   B 1 156 ? 47.738 -32.067 -7.355  1.00 12.34 ?  156  PHE   B N    1 
ATOM   6373 C  CA   . PHE   B 1 156 ? 49.118 -32.517 -7.554  1.00 13.43 ?  156  PHE   B CA   1 
ATOM   6374 C  C    . PHE   B 1 156 ? 49.221 -34.016 -7.842  1.00 14.45 ?  156  PHE   B C    1 
ATOM   6375 O  O    . PHE   B 1 156 ? 49.947 -34.436 -8.753  1.00 16.35 ?  156  PHE   B O    1 
ATOM   6376 C  CB   . PHE   B 1 156 ? 49.947 -32.152 -6.323  1.00 13.56 ?  156  PHE   B CB   1 
ATOM   6377 C  CG   . PHE   B 1 156 ? 51.371 -32.615 -6.384  1.00 14.10 ?  156  PHE   B CG   1 
ATOM   6378 C  CD1  . PHE   B 1 156 ? 52.250 -32.085 -7.311  1.00 15.89 ?  156  PHE   B CD1  1 
ATOM   6379 C  CD2  . PHE   B 1 156 ? 51.831 -33.566 -5.504  1.00 14.34 ?  156  PHE   B CD2  1 
ATOM   6380 C  CE1  . PHE   B 1 156 ? 53.572 -32.497 -7.359  1.00 16.74 ?  156  PHE   B CE1  1 
ATOM   6381 C  CE2  . PHE   B 1 156 ? 53.149 -33.986 -5.550  1.00 15.77 ?  156  PHE   B CE2  1 
ATOM   6382 C  CZ   . PHE   B 1 156 ? 54.013 -33.453 -6.482  1.00 16.41 ?  156  PHE   B CZ   1 
ATOM   6383 H  H    . PHE   B 1 156 ? 47.555 -31.836 -6.544  1.00 14.84 ?  156  PHE   B H    1 
ATOM   6384 H  HA   . PHE   B 1 156 ? 49.492 -32.043 -8.309  1.00 16.14 ?  156  PHE   B HA   1 
ATOM   6385 H  HB2  . PHE   B 1 156 ? 49.955 -31.186 -6.228  1.00 16.30 ?  156  PHE   B HB2  1 
ATOM   6386 H  HB3  . PHE   B 1 156 ? 49.542 -32.554 -5.538  1.00 16.30 ?  156  PHE   B HB3  1 
ATOM   6387 H  HD1  . PHE   B 1 156 ? 51.953 -31.428 -7.906  1.00 19.10 ?  156  PHE   B HD1  1 
ATOM   6388 H  HD2  . PHE   B 1 156 ? 51.250 -33.933 -4.876  1.00 17.24 ?  156  PHE   B HD2  1 
ATOM   6389 H  HE1  . PHE   B 1 156 ? 54.151 -32.131 -7.990  1.00 20.12 ?  156  PHE   B HE1  1 
ATOM   6390 H  HE2  . PHE   B 1 156 ? 53.447 -34.639 -4.957  1.00 18.95 ?  156  PHE   B HE2  1 
ATOM   6391 H  HZ   . PHE   B 1 156 ? 54.897 -33.740 -6.514  1.00 19.72 ?  156  PHE   B HZ   1 
ATOM   6392 N  N    . ASP   B 1 157 ? 48.557 -34.841 -7.046  1.00 14.82 ?  157  ASP   B N    1 
ATOM   6393 C  CA   . ASP   B 1 157 ? 48.707 -36.287 -7.155  1.00 16.12 ?  157  ASP   B CA   1 
ATOM   6394 C  C    . ASP   B 1 157 ? 47.788 -36.826 -8.249  1.00 16.19 ?  157  ASP   B C    1 
ATOM   6395 O  O    . ASP   B 1 157 ? 46.562 -36.715 -8.143  1.00 15.59 ?  157  ASP   B O    1 
ATOM   6396 C  CB   . ASP   B 1 157 ? 48.357 -36.906 -5.810  1.00 17.69 ?  157  ASP   B CB   1 
ATOM   6397 C  CG   . ASP   B 1 157 ? 48.485 -38.418 -5.802  1.00 19.48 ?  157  ASP   B CG   1 
ATOM   6398 O  OD1  . ASP   B 1 157 ? 48.817 -39.026 -6.849  1.00 19.94 ?  157  ASP   B OD1  1 
ATOM   6399 O  OD2  . ASP   B 1 157 ? 48.273 -39.007 -4.723  1.00 21.72 -1 157  ASP   B OD2  1 
ATOM   6400 H  H    . ASP   B 1 157 ? 48.014 -34.593 -6.432  1.00 17.81 ?  157  ASP   B H    1 
ATOM   6401 H  HA   . ASP   B 1 157 ? 49.628 -36.512 -7.378  1.00 19.37 ?  157  ASP   B HA   1 
ATOM   6402 H  HB2  . ASP   B 1 157 ? 48.948 -36.538 -5.138  1.00 21.26 ?  157  ASP   B HB2  1 
ATOM   6403 H  HB3  . ASP   B 1 157 ? 47.436 -36.683 -5.598  1.00 21.26 ?  157  ASP   B HB3  1 
ATOM   6404 N  N    . LYS   B 1 158 ? 48.381 -37.444 -9.280  1.00 17.17 ?  158  LYS   B N    1 
ATOM   6405 C  CA   . LYS   B 1 158 ? 47.602 -38.050 -10.363 1.00 18.28 ?  158  LYS   B CA   1 
ATOM   6406 C  C    . LYS   B 1 158 ? 46.542 -39.016 -9.834  1.00 18.03 ?  158  LYS   B C    1 
ATOM   6407 O  O    . LYS   B 1 158 ? 45.439 -39.107 -10.387 1.00 18.06 ?  158  LYS   B O    1 
ATOM   6408 C  CB   . LYS   B 1 158 ? 48.549 -38.764 -11.338 1.00 19.89 ?  158  LYS   B CB   1 
ATOM   6409 C  CG   . LYS   B 1 158 ? 47.873 -39.658 -12.369 1.00 22.11 ?  158  LYS   B CG   1 
ATOM   6410 C  CD   . LYS   B 1 158 ? 47.018 -38.877 -13.343 1.00 24.32 ?  158  LYS   B CD   1 
ATOM   6411 C  CE   . LYS   B 1 158 ? 46.416 -39.802 -14.390 1.00 25.78 ?  158  LYS   B CE   1 
ATOM   6412 N  NZ   . LYS   B 1 158 ? 45.357 -39.128 -15.194 1.00 26.21 ?  158  LYS   B NZ   1 
ATOM   6413 H  H    . LYS   B 1 158 ? 49.238 -37.533 -9.375  1.00 20.64 ?  158  LYS   B H    1 
ATOM   6414 H  HA   . LYS   B 1 158 ? 47.154 -37.347 -10.860 1.00 21.97 ?  158  LYS   B HA   1 
ATOM   6415 H  HB2  . LYS   B 1 158 ? 49.056 -38.096 -11.832 1.00 23.90 ?  158  LYS   B HB2  1 
ATOM   6416 H  HB3  . LYS   B 1 158 ? 49.161 -39.320 -10.832 1.00 23.90 ?  158  LYS   B HB3  1 
ATOM   6417 H  HG2  . LYS   B 1 158 ? 48.559 -40.117 -12.882 1.00 26.56 ?  158  LYS   B HG2  1 
ATOM   6418 H  HG3  . LYS   B 1 158 ? 47.312 -40.314 -11.924 1.00 26.56 ?  158  LYS   B HG3  1 
ATOM   6419 H  HD2  . LYS   B 1 158 ? 46.295 -38.443 -12.865 1.00 29.21 ?  158  LYS   B HD2  1 
ATOM   6420 H  HD3  . LYS   B 1 158 ? 47.566 -38.218 -13.799 1.00 29.21 ?  158  LYS   B HD3  1 
ATOM   6421 H  HE2  . LYS   B 1 158 ? 47.112 -40.097 -14.996 1.00 30.96 ?  158  LYS   B HE2  1 
ATOM   6422 H  HE3  . LYS   B 1 158 ? 46.015 -40.568 -13.947 1.00 30.96 ?  158  LYS   B HE3  1 
ATOM   6423 H  HZ1  . LYS   B 1 158 ? 45.023 -39.692 -15.795 1.00 31.48 ?  158  LYS   B HZ1  1 
ATOM   6424 H  HZ2  . LYS   B 1 158 ? 44.700 -38.850 -14.661 1.00 31.48 ?  158  LYS   B HZ2  1 
ATOM   6425 H  HZ3  . LYS   B 1 158 ? 45.701 -38.424 -15.618 1.00 31.48 ?  158  LYS   B HZ3  1 
ATOM   6426 N  N    . ASN   B 1 159 ? 46.864 -39.775 -8.784  1.00 18.36 ?  159  ASN   B N    1 
ATOM   6427 C  CA   . ASN   B 1 159 ? 45.910 -40.759 -8.281  1.00 18.87 ?  159  ASN   B CA   1 
ATOM   6428 C  C    . ASN   B 1 159 ? 44.718 -40.095 -7.595  1.00 17.91 ?  159  ASN   B C    1 
ATOM   6429 O  O    . ASN   B 1 159 ? 43.589 -40.593 -7.700  1.00 18.06 ?  159  ASN   B O    1 
ATOM   6430 C  CB   . ASN   B 1 159 ? 46.618 -41.742 -7.355  1.00 20.36 ?  159  ASN   B CB   1 
ATOM   6431 C  CG   . ASN   B 1 159 ? 47.658 -42.569 -8.082  1.00 22.21 ?  159  ASN   B CG   1 
ATOM   6432 O  OD1  . ASN   B 1 159 ? 47.406 -43.077 -9.181  1.00 22.79 ?  159  ASN   B OD1  1 
ATOM   6433 N  ND2  . ASN   B 1 159 ? 48.835 -42.708 -7.479  1.00 23.09 ?  159  ASN   B ND2  1 
ATOM   6434 H  H    . ASN   B 1 159 ? 47.610 -39.733 -8.362  1.00 22.06 ?  159  ASN   B H    1 
ATOM   6435 H  HA   . ASN   B 1 159 ? 45.569 -41.261 -9.038  1.00 22.67 ?  159  ASN   B HA   1 
ATOM   6436 H  HB2  . ASN   B 1 159 ? 47.065 -41.253 -6.650  1.00 24.46 ?  159  ASN   B HB2  1 
ATOM   6437 H  HB3  . ASN   B 1 159 ? 45.966 -42.352 -6.985  1.00 24.46 ?  159  ASN   B HB3  1 
ATOM   6438 H  HD21 . ASN   B 1 159 ? 49.463 -43.169 -7.854  1.00 27.74 ?  159  ASN   B HD21 1 
ATOM   6439 H  HD22 . ASN   B 1 159 ? 48.971 -42.354 -6.709  1.00 27.74 ?  159  ASN   B HD22 1 
ATOM   6440 N  N    . LEU   B 1 160 ? 44.929 -38.963 -6.916  1.00 16.89 ?  160  LEU   B N    1 
ATOM   6441 C  CA   . LEU   B 1 160 ? 43.792 -38.233 -6.365  1.00 15.93 ?  160  LEU   B CA   1 
ATOM   6442 C  C    . LEU   B 1 160 ? 42.998 -37.562 -7.473  1.00 15.40 ?  160  LEU   B C    1 
ATOM   6443 O  O    . LEU   B 1 160 ? 41.762 -37.576 -7.453  1.00 14.80 ?  160  LEU   B O    1 
ATOM   6444 C  CB   . LEU   B 1 160 ? 44.251 -37.207 -5.330  1.00 15.40 ?  160  LEU   B CB   1 
ATOM   6445 C  CG   . LEU   B 1 160 ? 43.128 -36.316 -4.782  1.00 15.45 ?  160  LEU   B CG   1 
ATOM   6446 C  CD1  . LEU   B 1 160 ? 42.012 -37.142 -4.143  1.00 15.95 ?  160  LEU   B CD1  1 
ATOM   6447 C  CD2  . LEU   B 1 160 ? 43.681 -35.308 -3.787  1.00 15.71 ?  160  LEU   B CD2  1 
ATOM   6448 H  H    . LEU   B 1 160 ? 45.702 -38.600 -6.778  1.00 20.30 ?  160  LEU   B H    1 
ATOM   6449 H  HA   . LEU   B 1 160 ? 43.210 -38.866 -5.927  1.00 19.14 ?  160  LEU   B HA   1 
ATOM   6450 H  HB2  . LEU   B 1 160 ? 44.652 -37.686 -4.583  1.00 18.51 ?  160  LEU   B HB2  1 
ATOM   6451 H  HB3  . LEU   B 1 160 ? 44.921 -36.633 -5.739  1.00 18.51 ?  160  LEU   B HB3  1 
ATOM   6452 H  HG   . LEU   B 1 160 ? 42.743 -35.820 -5.516  1.00 18.56 ?  160  LEU   B HG   1 
ATOM   6453 H  HD11 . LEU   B 1 160 ? 41.368 -36.541 -3.744  1.00 19.17 ?  160  LEU   B HD11 1 
ATOM   6454 H  HD12 . LEU   B 1 160 ? 41.583 -37.682 -4.827  1.00 19.17 ?  160  LEU   B HD12 1 
ATOM   6455 H  HD13 . LEU   B 1 160 ? 42.394 -37.719 -3.461  1.00 19.17 ?  160  LEU   B HD13 1 
ATOM   6456 H  HD21 . LEU   B 1 160 ? 42.958 -34.730 -3.498  1.00 18.88 ?  160  LEU   B HD21 1 
ATOM   6457 H  HD22 . LEU   B 1 160 ? 44.051 -35.783 -3.028  1.00 18.88 ?  160  LEU   B HD22 1 
ATOM   6458 H  HD23 . LEU   B 1 160 ? 44.371 -34.784 -4.222  1.00 18.88 ?  160  LEU   B HD23 1 
ATOM   6459 N  N    . TYR   B 1 161 ? 43.692 -36.985 -8.458  1.00 15.34 ?  161  TYR   B N    1 
ATOM   6460 C  CA   . TYR   B 1 161 ? 43.017 -36.418 -9.620  1.00 15.24 ?  161  TYR   B CA   1 
ATOM   6461 C  C    . TYR   B 1 161 ? 42.076 -37.438 -10.247 1.00 14.95 ?  161  TYR   B C    1 
ATOM   6462 O  O    . TYR   B 1 161 ? 40.908 -37.141 -10.518 1.00 14.92 ?  161  TYR   B O    1 
ATOM   6463 C  CB   . TYR   B 1 161 ? 44.059 -35.932 -10.637 1.00 15.79 ?  161  TYR   B CB   1 
ATOM   6464 C  CG   . TYR   B 1 161 ? 43.480 -35.466 -11.951 1.00 16.18 ?  161  TYR   B CG   1 
ATOM   6465 C  CD1  . TYR   B 1 161 ? 43.077 -34.148 -12.118 1.00 16.31 ?  161  TYR   B CD1  1 
ATOM   6466 C  CD2  . TYR   B 1 161 ? 43.319 -36.340 -13.020 1.00 16.79 ?  161  TYR   B CD2  1 
ATOM   6467 C  CE1  . TYR   B 1 161 ? 42.543 -33.713 -13.305 1.00 17.24 ?  161  TYR   B CE1  1 
ATOM   6468 C  CE2  . TYR   B 1 161 ? 42.778 -35.912 -14.214 1.00 17.89 ?  161  TYR   B CE2  1 
ATOM   6469 C  CZ   . TYR   B 1 161 ? 42.396 -34.596 -14.352 1.00 17.81 ?  161  TYR   B CZ   1 
ATOM   6470 O  OH   . TYR   B 1 161 ? 41.853 -34.151 -15.533 1.00 19.74 ?  161  TYR   B OH   1 
ATOM   6471 H  H    . TYR   B 1 161 ? 44.549 -36.917 -8.482  1.00 18.44 ?  161  TYR   B H    1 
ATOM   6472 H  HA   . TYR   B 1 161 ? 42.490 -35.652 -9.344  1.00 18.31 ?  161  TYR   B HA   1 
ATOM   6473 H  HB2  . TYR   B 1 161 ? 44.547 -35.183 -10.254 1.00 18.97 ?  161  TYR   B HB2  1 
ATOM   6474 H  HB3  . TYR   B 1 161 ? 44.672 -36.655 -10.833 1.00 18.97 ?  161  TYR   B HB3  1 
ATOM   6475 H  HD1  . TYR   B 1 161 ? 43.179 -33.540 -11.418 1.00 19.60 ?  161  TYR   B HD1  1 
ATOM   6476 H  HD2  . TYR   B 1 161 ? 43.574 -37.226 -12.932 1.00 20.18 ?  161  TYR   B HD2  1 
ATOM   6477 H  HE1  . TYR   B 1 161 ? 42.283 -32.819 -13.399 1.00 20.72 ?  161  TYR   B HE1  1 
ATOM   6478 H  HE2  . TYR   B 1 161 ? 42.673 -36.503 -14.924 1.00 21.50 ?  161  TYR   B HE2  1 
ATOM   6479 H  HH   . TYR   B 1 161 ? 41.812 -34.786 -16.085 1.00 23.71 ?  161  TYR   B HH   1 
ATOM   6480 N  N    . ASP   B 1 162 ? 42.574 -38.655 -10.472 1.00 15.49 ?  162  ASP   B N    1 
ATOM   6481 C  CA   . ASP   B 1 162 ? 41.750 -39.691 -11.085 1.00 15.97 ?  162  ASP   B CA   1 
ATOM   6482 C  C    . ASP   B 1 162 ? 40.548 -40.037 -10.214 1.00 15.50 ?  162  ASP   B C    1 
ATOM   6483 O  O    . ASP   B 1 162 ? 39.444 -40.255 -10.726 1.00 15.76 ?  162  ASP   B O    1 
ATOM   6484 C  CB   . ASP   B 1 162 ? 42.591 -40.946 -11.341 1.00 17.59 ?  162  ASP   B CB   1 
ATOM   6485 C  CG   . ASP   B 1 162 ? 43.582 -40.786 -12.489 1.00 18.74 ?  162  ASP   B CG   1 
ATOM   6486 O  OD1  . ASP   B 1 162 ? 43.453 -39.838 -13.285 1.00 18.87 ?  162  ASP   B OD1  1 
ATOM   6487 O  OD2  . ASP   B 1 162 ? 44.483 -41.644 -12.607 1.00 20.33 -1 162  ASP   B OD2  1 
ATOM   6488 H  H    . ASP   B 1 162 ? 43.377 -38.897 -10.284 1.00 18.61 ?  162  ASP   B H    1 
ATOM   6489 H  HA   . ASP   B 1 162 ? 41.420 -39.368 -11.936 1.00 19.19 ?  162  ASP   B HA   1 
ATOM   6490 H  HB2  . ASP   B 1 162 ? 43.100 -41.152 -10.543 1.00 21.14 ?  162  ASP   B HB2  1 
ATOM   6491 H  HB3  . ASP   B 1 162 ? 41.998 -41.679 -11.558 1.00 21.14 ?  162  ASP   B HB3  1 
ATOM   6492 N  N    A LYS   B 1 163 ? 40.743 -40.116 -8.896  0.60 14.82 ?  163  LYS   B N    1 
ATOM   6493 N  N    B LYS   B 1 163 ? 40.741 -40.103 -8.894  0.40 15.38 ?  163  LYS   B N    1 
ATOM   6494 C  CA   A LYS   B 1 163 ? 39.619 -40.400 -8.010  0.60 15.34 ?  163  LYS   B CA   1 
ATOM   6495 C  CA   B LYS   B 1 163 ? 39.622 -40.397 -8.004  0.40 16.00 ?  163  LYS   B CA   1 
ATOM   6496 C  C    A LYS   B 1 163 ? 38.575 -39.290 -8.074  0.60 14.32 ?  163  LYS   B C    1 
ATOM   6497 C  C    B LYS   B 1 163 ? 38.577 -39.289 -8.049  0.40 14.71 ?  163  LYS   B C    1 
ATOM   6498 O  O    A LYS   B 1 163 ? 37.366 -39.560 -8.095  0.60 15.22 ?  163  LYS   B O    1 
ATOM   6499 O  O    B LYS   B 1 163 ? 37.369 -39.557 -8.022  0.40 15.35 ?  163  LYS   B O    1 
ATOM   6500 C  CB   A LYS   B 1 163 ? 40.102 -40.595 -6.575  0.60 18.06 ?  163  LYS   B CB   1 
ATOM   6501 C  CB   B LYS   B 1 163 ? 40.122 -40.599 -6.575  0.40 18.55 ?  163  LYS   B CB   1 
ATOM   6502 C  CG   A LYS   B 1 163 ? 39.022 -41.141 -5.659  0.60 22.29 ?  163  LYS   B CG   1 
ATOM   6503 C  CG   B LYS   B 1 163 ? 39.045 -41.098 -5.631  0.40 21.91 ?  163  LYS   B CG   1 
ATOM   6504 C  CD   A LYS   B 1 163 ? 39.433 -41.132 -4.199  0.60 25.89 ?  163  LYS   B CD   1 
ATOM   6505 C  CD   B LYS   B 1 163 ? 39.551 -41.254 -4.209  0.40 24.98 ?  163  LYS   B CD   1 
ATOM   6506 C  CE   A LYS   B 1 163 ? 38.373 -41.817 -3.345  0.60 28.08 ?  163  LYS   B CE   1 
ATOM   6507 C  CE   B LYS   B 1 163 ? 38.503 -41.940 -3.345  0.40 26.94 ?  163  LYS   B CE   1 
ATOM   6508 N  NZ   A LYS   B 1 163 ? 38.500 -41.497 -1.896  0.60 29.53 ?  163  LYS   B NZ   1 
ATOM   6509 N  NZ   B LYS   B 1 163 ? 38.709 -41.694 -1.891  0.40 28.03 ?  163  LYS   B NZ   1 
ATOM   6510 H  H    A LYS   B 1 163 ? 41.502 -40.011 -8.500  0.60 17.81 ?  163  LYS   B H    1 
ATOM   6511 H  H    B LYS   B 1 163 ? 41.497 -39.985 -8.498  0.40 18.49 ?  163  LYS   B H    1 
ATOM   6512 H  HA   A LYS   B 1 163 ? 39.197 -41.220 -8.299  0.60 18.44 ?  163  LYS   B HA   1 
ATOM   6513 H  HA   B LYS   B 1 163 ? 39.199 -41.218 -8.293  0.40 19.23 ?  163  LYS   B HA   1 
ATOM   6514 H  HB2  A LYS   B 1 163 ? 40.841 -41.226 -6.574  0.60 21.70 ?  163  LYS   B HB2  1 
ATOM   6515 H  HB2  B LYS   B 1 163 ? 40.839 -41.253 -6.582  0.40 22.29 ?  163  LYS   B HB2  1 
ATOM   6516 H  HB3  A LYS   B 1 163 ? 40.395 -39.743 -6.218  0.60 21.70 ?  163  LYS   B HB3  1 
ATOM   6517 H  HB3  B LYS   B 1 163 ? 40.450 -39.753 -6.233  0.40 22.29 ?  163  LYS   B HB3  1 
ATOM   6518 H  HG2  A LYS   B 1 163 ? 38.224 -40.598 -5.748  0.60 26.78 ?  163  LYS   B HG2  1 
ATOM   6519 H  HG2  B LYS   B 1 163 ? 38.311 -40.464 -5.619  0.40 26.32 ?  163  LYS   B HG2  1 
ATOM   6520 H  HG3  A LYS   B 1 163 ? 38.828 -42.059 -5.911  0.60 26.78 ?  163  LYS   B HG3  1 
ATOM   6521 H  HG3  B LYS   B 1 163 ? 38.732 -41.964 -5.936  0.40 26.32 ?  163  LYS   B HG3  1 
ATOM   6522 H  HD2  A LYS   B 1 163 ? 40.269 -41.615 -4.096  0.60 31.10 ?  163  LYS   B HD2  1 
ATOM   6523 H  HD2  B LYS   B 1 163 ? 40.353 -41.800 -4.211  0.40 30.00 ?  163  LYS   B HD2  1 
ATOM   6524 H  HD3  A LYS   B 1 163 ? 39.529 -40.217 -3.896  0.60 31.10 ?  163  LYS   B HD3  1 
ATOM   6525 H  HD3  B LYS   B 1 163 ? 39.736 -40.380 -3.834  0.40 30.00 ?  163  LYS   B HD3  1 
ATOM   6526 H  HE2  A LYS   B 1 163 ? 37.492 -41.543 -3.643  0.60 33.73 ?  163  LYS   B HE2  1 
ATOM   6527 H  HE2  B LYS   B 1 163 ? 37.625 -41.607 -3.587  0.40 32.36 ?  163  LYS   B HE2  1 
ATOM   6528 H  HE3  A LYS   B 1 163 ? 38.466 -42.776 -3.445  0.60 33.73 ?  163  LYS   B HE3  1 
ATOM   6529 H  HE3  B LYS   B 1 163 ? 38.547 -42.897 -3.496  0.40 32.36 ?  163  LYS   B HE3  1 
ATOM   6530 H  HZ1  A LYS   B 1 163 ? 37.862 -41.915 -1.436  0.60 35.47 ?  163  LYS   B HZ1  1 
ATOM   6531 H  HZ1  B LYS   B 1 163 ? 38.077 -42.109 -1.421  0.40 33.66 ?  163  LYS   B HZ1  1 
ATOM   6532 H  HZ2  A LYS   B 1 163 ? 39.294 -41.761 -1.595  0.60 35.47 ?  163  LYS   B HZ2  1 
ATOM   6533 H  HZ2  B LYS   B 1 163 ? 39.505 -41.999 -1.641  0.40 33.66 ?  163  LYS   B HZ2  1 
ATOM   6534 H  HZ3  A LYS   B 1 163 ? 38.419 -40.620 -1.770  0.60 35.47 ?  163  LYS   B HZ3  1 
ATOM   6535 H  HZ3  B LYS   B 1 163 ? 38.667 -40.820 -1.723  0.40 33.66 ?  163  LYS   B HZ3  1 
ATOM   6536 N  N    . LEU   B 1 164 ? 39.028 -38.035 -8.116  1.00 13.55 ?  164  LEU   B N    1 
ATOM   6537 C  CA   . LEU   B 1 164 ? 38.113 -36.899 -8.161  1.00 13.06 ?  164  LEU   B CA   1 
ATOM   6538 C  C    . LEU   B 1 164 ? 37.323 -36.873 -9.465  1.00 13.19 ?  164  LEU   B C    1 
ATOM   6539 O  O    . LEU   B 1 164 ? 36.101 -36.676 -9.460  1.00 14.25 ?  164  LEU   B O    1 
ATOM   6540 C  CB   . LEU   B 1 164 ? 38.916 -35.603 -8.003  1.00 12.59 ?  164  LEU   B CB   1 
ATOM   6541 C  CG   . LEU   B 1 164 ? 39.448 -35.338 -6.600  1.00 13.52 ?  164  LEU   B CG   1 
ATOM   6542 C  CD1  . LEU   B 1 164 ? 40.531 -34.270 -6.646  1.00 13.59 ?  164  LEU   B CD1  1 
ATOM   6543 C  CD2  . LEU   B 1 164 ? 38.332 -34.922 -5.661  1.00 15.28 ?  164  LEU   B CD2  1 
ATOM   6544 H  H    A LEU   B 1 164 ? 39.863 -37.814 -8.121  0.60 16.28 ?  164  LEU   B H    1 
ATOM   6545 H  H    B LEU   B 1 164 ? 39.863 -37.815 -8.138  0.40 16.28 ?  164  LEU   B H    1 
ATOM   6546 H  HA   . LEU   B 1 164 ? 37.487 -36.959 -7.430  1.00 15.70 ?  164  LEU   B HA   1 
ATOM   6547 H  HB2  . LEU   B 1 164 ? 39.683 -35.637 -8.605  1.00 15.13 ?  164  LEU   B HB2  1 
ATOM   6548 H  HB3  . LEU   B 1 164 ? 38.353 -34.854 -8.250  1.00 15.13 ?  164  LEU   B HB3  1 
ATOM   6549 H  HG   . LEU   B 1 164 ? 39.849 -36.147 -6.259  1.00 16.25 ?  164  LEU   B HG   1 
ATOM   6550 H  HD11 . LEU   B 1 164 ? 40.855 -34.103 -5.745  1.00 16.34 ?  164  LEU   B HD11 1 
ATOM   6551 H  HD12 . LEU   B 1 164 ? 41.267 -34.578 -7.204  1.00 16.34 ?  164  LEU   B HD12 1 
ATOM   6552 H  HD13 . LEU   B 1 164 ? 40.163 -33.450 -7.018  1.00 16.34 ?  164  LEU   B HD13 1 
ATOM   6553 H  HD21 . LEU   B 1 164 ? 38.713 -34.692 -4.801  1.00 18.36 ?  164  LEU   B HD21 1 
ATOM   6554 H  HD22 . LEU   B 1 164 ? 37.869 -34.158 -6.036  1.00 18.36 ?  164  LEU   B HD22 1 
ATOM   6555 H  HD23 . LEU   B 1 164 ? 37.716 -35.666 -5.562  1.00 18.36 ?  164  LEU   B HD23 1 
ATOM   6556 N  N    . VAL   B 1 165 ? 38.008 -37.043 -10.597 1.00 14.73 ?  165  VAL   B N    1 
ATOM   6557 C  CA   . VAL   B 1 165 ? 37.348 -36.975 -11.897 1.00 15.95 ?  165  VAL   B CA   1 
ATOM   6558 C  C    . VAL   B 1 165 ? 36.436 -38.176 -12.089 1.00 17.71 ?  165  VAL   B C    1 
ATOM   6559 O  O    . VAL   B 1 165 ? 35.275 -38.040 -12.495 1.00 18.48 ?  165  VAL   B O    1 
ATOM   6560 C  CB   . VAL   B 1 165 ? 38.394 -36.888 -13.023 1.00 16.71 ?  165  VAL   B CB   1 
ATOM   6561 C  CG1  . VAL   B 1 165 ? 37.735 -37.004 -14.377 1.00 17.91 ?  165  VAL   B CG1  1 
ATOM   6562 C  CG2  . VAL   B 1 165 ? 39.182 -35.605 -12.921 1.00 16.49 ?  165  VAL   B CG2  1 
ATOM   6563 H  H    . VAL   B 1 165 ? 38.855 -37.185 -10.638 1.00 17.70 ?  165  VAL   B H    1 
ATOM   6564 H  HA   . VAL   B 1 165 ? 36.803 -36.175 -11.937 1.00 19.17 ?  165  VAL   B HA   1 
ATOM   6565 H  HB   . VAL   B 1 165 ? 39.022 -37.621 -12.928 1.00 20.08 ?  165  VAL   B HB   1 
ATOM   6566 H  HG11 . VAL   B 1 165 ? 38.349 -36.689 -15.055 1.00 21.52 ?  165  VAL   B HG11 1 
ATOM   6567 H  HG12 . VAL   B 1 165 ? 37.522 -37.938 -14.538 1.00 21.52 ?  165  VAL   B HG12 1 
ATOM   6568 H  HG13 . VAL   B 1 165 ? 36.927 -36.473 -14.382 1.00 21.52 ?  165  VAL   B HG13 1 
ATOM   6569 H  HG21 . VAL   B 1 165 ? 39.822 -35.564 -13.651 1.00 19.82 ?  165  VAL   B HG21 1 
ATOM   6570 H  HG22 . VAL   B 1 165 ? 38.571 -34.851 -12.978 1.00 19.82 ?  165  VAL   B HG22 1 
ATOM   6571 H  HG23 . VAL   B 1 165 ? 39.651 -35.582 -12.071 1.00 19.82 ?  165  VAL   B HG23 1 
ATOM   6572 N  N    A SER   B 1 166 ? 36.952 -39.374 -11.798 0.60 18.39 ?  166  SER   B N    1 
ATOM   6573 N  N    B SER   B 1 166 ? 36.952 -39.376 -11.805 0.40 18.21 ?  166  SER   B N    1 
ATOM   6574 C  CA   A SER   B 1 166 ? 36.200 -40.589 -12.085 0.60 19.54 ?  166  SER   B CA   1 
ATOM   6575 C  CA   B SER   B 1 166 ? 36.192 -40.586 -12.088 0.40 18.99 ?  166  SER   B CA   1 
ATOM   6576 C  C    A SER   B 1 166 ? 34.948 -40.693 -11.225 0.60 19.85 ?  166  SER   B C    1 
ATOM   6577 C  C    B SER   B 1 166 ? 34.932 -40.671 -11.237 0.40 19.31 ?  166  SER   B C    1 
ATOM   6578 O  O    A SER   B 1 166 ? 33.982 -41.338 -11.635 0.60 21.11 ?  166  SER   B O    1 
ATOM   6579 O  O    B SER   B 1 166 ? 33.945 -41.272 -11.667 0.40 20.14 ?  166  SER   B O    1 
ATOM   6580 C  CB   A SER   B 1 166 ? 37.082 -41.834 -11.926 0.60 20.52 ?  166  SER   B CB   1 
ATOM   6581 C  CB   B SER   B 1 166 ? 37.063 -41.835 -11.907 0.40 19.51 ?  166  SER   B CB   1 
ATOM   6582 O  OG   A SER   B 1 166 ? 37.447 -42.055 -10.574 0.60 20.70 ?  166  SER   B OG   1 
ATOM   6583 O  OG   B SER   B 1 166 ? 37.412 -42.041 -10.548 0.40 19.57 ?  166  SER   B OG   1 
ATOM   6584 H  H    A SER   B 1 166 ? 37.726 -39.503 -11.442 0.60 22.09 ?  166  SER   B H    1 
ATOM   6585 H  H    B SER   B 1 166 ? 37.727 -39.509 -11.453 0.40 21.88 ?  166  SER   B H    1 
ATOM   6586 H  HA   A SER   B 1 166 ? 35.917 -40.557 -13.012 0.60 23.48 ?  166  SER   B HA   1 
ATOM   6587 H  HA   B SER   B 1 166 ? 35.913 -40.563 -13.016 0.40 22.81 ?  166  SER   B HA   1 
ATOM   6588 H  HB2  A SER   B 1 166 ? 36.592 -42.605 -12.250 0.60 24.66 ?  166  SER   B HB2  1 
ATOM   6589 H  HB2  B SER   B 1 166 ? 36.571 -42.608 -12.226 0.40 23.44 ?  166  SER   B HB2  1 
ATOM   6590 H  HB3  A SER   B 1 166 ? 37.889 -41.715 -12.457 0.60 24.66 ?  166  SER   B HB3  1 
ATOM   6591 H  HB3  B SER   B 1 166 ? 37.876 -41.728 -12.430 0.40 23.44 ?  166  SER   B HB3  1 
ATOM   6592 H  HG   A SER   B 1 166 ? 37.881 -41.393 -10.288 0.60 24.87 ?  166  SER   B HG   1 
ATOM   6593 H  HG   B SER   B 1 166 ? 37.846 -41.380 -10.263 0.40 23.51 ?  166  SER   B HG   1 
ATOM   6594 N  N    . SER   B 1 167 ? 34.930 -40.067 -10.050 1.00 18.70 ?  167  SER   B N    1 
ATOM   6595 C  CA   . SER   B 1 167 ? 33.780 -40.128 -9.155  1.00 18.01 ?  167  SER   B CA   1 
ATOM   6596 C  C    . SER   B 1 167 ? 32.857 -38.912 -9.247  1.00 17.68 ?  167  SER   B C    1 
ATOM   6597 O  O    . SER   B 1 167 ? 31.782 -38.922 -8.635  1.00 17.96 ?  167  SER   B O    1 
ATOM   6598 C  CB   . SER   B 1 167 ? 34.230 -40.319 -7.701  1.00 18.04 ?  167  SER   B CB   1 
ATOM   6599 O  OG   . SER   B 1 167 ? 34.880 -39.152 -7.213  1.00 17.78 ?  167  SER   B OG   1 
ATOM   6600 H  H    A SER   B 1 167 ? 35.580 -39.593 -9.750  0.60 22.47 ?  167  SER   B H    1 
ATOM   6601 H  H    B SER   B 1 167 ? 35.586 -39.603 -9.746  0.40 22.47 ?  167  SER   B H    1 
ATOM   6602 H  HA   . SER   B 1 167 ? 33.249 -40.905 -9.397  1.00 21.64 ?  167  SER   B HA   1 
ATOM   6603 H  HB2  . SER   B 1 167 ? 33.450 -40.507 -7.155  1.00 21.68 ?  167  SER   B HB2  1 
ATOM   6604 H  HB3  . SER   B 1 167 ? 34.846 -41.073 -7.662  1.00 21.68 ?  167  SER   B HB3  1 
ATOM   6605 H  HG   . SER   B 1 167 ? 35.556 -38.992 -7.684  1.00 21.36 ?  167  SER   B HG   1 
ATOM   6606 N  N    . PHE   B 1 168 ? 33.225 -37.874 -10.003 1.00 17.42 ?  168  PHE   B N    1 
ATOM   6607 C  CA   . PHE   B 1 168 ? 32.383 -36.675 -10.060 1.00 16.72 ?  168  PHE   B CA   1 
ATOM   6608 C  C    . PHE   B 1 168 ? 31.068 -36.941 -10.789 1.00 14.34 ?  168  PHE   B C    1 
ATOM   6609 O  O    . PHE   B 1 168 ? 30.022 -36.351 -10.454 1.00 15.21 ?  168  PHE   B O    1 
ATOM   6610 C  CB   . PHE   B 1 168 ? 33.137 -35.534 -10.736 1.00 17.46 ?  168  PHE   B CB   1 
ATOM   6611 C  CG   . PHE   B 1 168 ? 32.329 -34.290 -10.857 1.00 17.73 ?  168  PHE   B CG   1 
ATOM   6612 C  CD1  . PHE   B 1 168 ? 32.016 -33.548 -9.727  1.00 18.97 ?  168  PHE   B CD1  1 
ATOM   6613 C  CD2  . PHE   B 1 168 ? 31.871 -33.862 -12.084 1.00 17.36 ?  168  PHE   B CD2  1 
ATOM   6614 C  CE1  . PHE   B 1 168 ? 31.253 -32.402 -9.819  1.00 19.53 ?  168  PHE   B CE1  1 
ATOM   6615 C  CE2  . PHE   B 1 168 ? 31.118 -32.701 -12.190 1.00 18.29 ?  168  PHE   B CE2  1 
ATOM   6616 C  CZ   . PHE   B 1 168 ? 30.807 -31.968 -11.054 1.00 18.70 ?  168  PHE   B CZ   1 
ATOM   6617 H  H    . PHE   B 1 168 ? 33.944 -37.837 -10.476 1.00 20.93 ?  168  PHE   B H    1 
ATOM   6618 H  HA   . PHE   B 1 168 ? 32.173 -36.400 -9.157  1.00 20.09 ?  168  PHE   B HA   1 
ATOM   6619 H  HB2  . PHE   B 1 168 ? 33.927 -35.322 -10.215 1.00 20.98 ?  168  PHE   B HB2  1 
ATOM   6620 H  HB3  . PHE   B 1 168 ? 33.393 -35.806 -11.630 1.00 20.98 ?  168  PHE   B HB3  1 
ATOM   6621 H  HD1  . PHE   B 1 168 ? 32.312 -33.836 -8.895  1.00 22.80 ?  168  PHE   B HD1  1 
ATOM   6622 H  HD2  . PHE   B 1 168 ? 32.076 -34.344 -12.849 1.00 20.86 ?  168  PHE   B HD2  1 
ATOM   6623 H  HE1  . PHE   B 1 168 ? 31.049 -31.910 -9.055  1.00 23.47 ?  168  PHE   B HE1  1 
ATOM   6624 H  HE2  . PHE   B 1 168 ? 30.810 -32.415 -13.024 1.00 21.98 ?  168  PHE   B HE2  1 
ATOM   6625 H  HZ   . PHE   B 1 168 ? 30.294 -31.193 -11.125 1.00 22.46 ?  168  PHE   B HZ   1 
ATOM   6626 N  N    . LEU   B 1 169 ? 31.106 -37.827 -11.781 1.00 14.69 ?  169  LEU   B N    1 
ATOM   6627 C  CA   . LEU   B 1 169 ? 29.927 -38.143 -12.578 1.00 17.21 ?  169  LEU   B CA   1 
ATOM   6628 C  C    . LEU   B 1 169 ? 29.909 -39.582 -13.067 1.00 19.90 ?  169  LEU   B C    1 
ATOM   6629 O  O    . LEU   B 1 169 ? 29.000 -39.992 -13.789 1.00 22.55 ?  169  LEU   B O    1 
ATOM   6630 C  CB   . LEU   B 1 169 ? 29.854 -37.210 -13.782 1.00 19.12 ?  169  LEU   B CB   1 
ATOM   6631 C  CG   . LEU   B 1 169 ? 28.608 -36.330 -13.867 1.00 22.20 ?  169  LEU   B CG   1 
ATOM   6632 C  CD1  . LEU   B 1 169 ? 28.574 -35.622 -15.206 1.00 23.06 ?  169  LEU   B CD1  1 
ATOM   6633 C  CD2  . LEU   B 1 169 ? 27.336 -37.135 -13.651 1.00 22.44 ?  169  LEU   B CD2  1 
ATOM   6634 O  OXT  . LEU   B 1 169 ? 30.811 -40.350 -12.762 1.00 20.83 -1 169  LEU   B OXT  1 
ATOM   6635 H  H    . LEU   B 1 169 ? 31.816 -38.264 -12.018 1.00 17.66 ?  169  LEU   B H    1 
ATOM   6636 H  HA   . LEU   B 1 169 ? 29.146 -38.002 -12.029 1.00 20.68 ?  169  LEU   B HA   1 
ATOM   6637 H  HB2  . LEU   B 1 169 ? 30.624 -36.619 -13.762 1.00 22.97 ?  169  LEU   B HB2  1 
ATOM   6638 H  HB3  . LEU   B 1 169 ? 29.882 -37.747 -14.589 1.00 22.97 ?  169  LEU   B HB3  1 
ATOM   6639 H  HG   . LEU   B 1 169 ? 28.653 -35.651 -13.174 1.00 26.67 ?  169  LEU   B HG   1 
ATOM   6640 H  HD11 . LEU   B 1 169 ? 27.792 -35.049 -15.240 1.00 27.70 ?  169  LEU   B HD11 1 
ATOM   6641 H  HD12 . LEU   B 1 169 ? 29.379 -35.090 -15.301 1.00 27.70 ?  169  LEU   B HD12 1 
ATOM   6642 H  HD13 . LEU   B 1 169 ? 28.530 -36.286 -15.911 1.00 27.70 ?  169  LEU   B HD13 1 
ATOM   6643 H  HD21 . LEU   B 1 169 ? 26.592 -36.672 -14.062 1.00 26.95 ?  169  LEU   B HD21 1 
ATOM   6644 H  HD22 . LEU   B 1 169 ? 27.446 -38.012 -14.058 1.00 26.95 ?  169  LEU   B HD22 1 
ATOM   6645 H  HD23 . LEU   B 1 169 ? 27.184 -37.233 -12.699 1.00 26.95 ?  169  LEU   B HD23 1 
HETATM 6646 N  N2   B A1BCC C 2 .   ? 14.681 -0.590  4.378   0.40 11.47 ?  201  A1BCC A N2   1 
HETATM 6647 C  C3   B A1BCC C 2 .   ? 13.889 -1.046  -0.004  0.40 13.12 ?  201  A1BCC A C3   1 
HETATM 6648 C  C6   B A1BCC C 2 .   ? 14.924 -0.285  5.701   0.40 11.87 ?  201  A1BCC A C6   1 
HETATM 6649 C  C9   B A1BCC C 2 .   ? 15.325 3.088   3.334   0.40 12.04 ?  201  A1BCC A C9   1 
HETATM 6650 C  C1   B A1BCC C 2 .   ? 16.139 -1.491  1.076   0.40 12.93 ?  201  A1BCC A C1   1 
HETATM 6651 C  C10  B A1BCC C 2 .   ? 15.653 3.929   4.390   0.40 12.13 ?  201  A1BCC A C10  1 
HETATM 6652 C  C2   B A1BCC C 2 .   ? 14.650 -1.191  1.320   0.40 13.12 ?  201  A1BCC A C2   1 
HETATM 6653 C  C4   B A1BCC C 2 .   ? 13.993 -2.454  2.093   0.40 12.87 ?  201  A1BCC A C4   1 
HETATM 6654 C  C5   B A1BCC C 2 .   ? 14.768 0.416   3.411   0.40 11.67 ?  201  A1BCC A C5   1 
HETATM 6655 C  C7   B A1BCC C 2 .   ? 15.328 1.889   5.279   0.40 11.63 ?  201  A1BCC A C7   1 
HETATM 6656 C  C8   B A1BCC C 2 .   ? 15.102 1.747   3.857   0.40 11.48 ?  201  A1BCC A C8   1 
HETATM 6657 N  N1   B A1BCC C 2 .   ? 14.498 0.129   2.059   0.40 12.89 ?  201  A1BCC A N1   1 
HETATM 6658 N  N3   B A1BCC C 2 .   ? 15.246 0.902   6.215   0.40 11.69 ?  201  A1BCC A N3   1 
HETATM 6659 N  N4   B A1BCC C 2 .   ? 15.648 3.189   5.544   0.40 12.01 ?  201  A1BCC A N4   1 
HETATM 6660 O  O1   B A1BCC C 2 .   ? 14.886 -2.970  3.060   0.40 12.63 ?  201  A1BCC A O1   1 
HETATM 6661 H  H6   B A1BCC C 2 .   ? 14.226 -0.186  -0.595  0.40 15.78 ?  201  A1BCC A H6   1 
HETATM 6662 H  H4   B A1BCC C 2 .   ? 12.810 -0.899  0.156   0.40 15.78 ?  201  A1BCC A H4   1 
HETATM 6663 H  H5   B A1BCC C 2 .   ? 13.973 -1.919  -0.676  0.40 15.78 ?  201  A1BCC A H5   1 
HETATM 6664 H  H11  B A1BCC C 2 .   ? 14.849 -1.086  6.461   0.40 14.27 ?  201  A1BCC A H11  1 
HETATM 6665 H  H12  B A1BCC C 2 .   ? 15.277 3.501   2.333   0.40 14.48 ?  201  A1BCC A H12  1 
HETATM 6666 H  H1   B A1BCC C 2 .   ? 16.649 -0.685  0.531   0.40 15.54 ?  201  A1BCC A H1   1 
HETATM 6667 H  H3   B A1BCC C 2 .   ? 16.311 -2.408  0.478   0.40 15.54 ?  201  A1BCC A H3   1 
HETATM 6668 H  H2   B A1BCC C 2 .   ? 16.715 -1.635  1.993   0.40 15.54 ?  201  A1BCC A H2   1 
HETATM 6669 H  H13  B A1BCC C 2 .   ? 15.895 4.986   4.505   0.40 14.58 ?  201  A1BCC A H13  1 
HETATM 6670 H  H7   B A1BCC C 2 .   ? 13.738 -3.266  1.365   0.40 15.47 ?  201  A1BCC A H7   1 
HETATM 6671 H  H8   B A1BCC C 2 .   ? 13.043 -2.170  2.589   0.40 15.47 ?  201  A1BCC A H8   1 
HETATM 6672 H  H10  B A1BCC C 2 .   ? 14.154 0.885   1.483   0.40 15.50 ?  201  A1BCC A H10  1 
HETATM 6673 H  H14  B A1BCC C 2 .   ? 15.860 3.587   6.463   0.40 14.44 ?  201  A1BCC A H14  1 
HETATM 6674 H  H9   B A1BCC C 2 .   ? 14.475 -3.722  3.541   0.40 15.19 ?  201  A1BCC A H9   1 
HETATM 6675 CL CL   B CL    D 3 .   ? 15.787 2.621   -0.830  0.40 17.56 ?  202  CL    A CL   1 
HETATM 6676 O  O    . HOH   E 4 .   ? 11.574 -10.860 -10.045 1.00 38.98 ?  1301 HOH   A O    1 
HETATM 6677 O  O    . HOH   E 4 .   ? -0.727 -8.426  2.355   1.00 46.39 ?  1302 HOH   A O    1 
HETATM 6678 O  O    . HOH   E 4 .   ? 4.728  3.931   0.877   1.00 21.85 ?  1303 HOH   A O    1 
HETATM 6679 O  O    . HOH   E 4 .   ? 18.485 -2.443  -16.400 1.00 45.34 ?  1304 HOH   A O    1 
HETATM 6680 O  O    . HOH   E 4 .   ? 28.787 0.444   -9.755  1.00 21.37 ?  1305 HOH   A O    1 
HETATM 6681 O  O    . HOH   E 4 .   ? 34.390 -1.886  12.455  1.00 35.82 ?  1306 HOH   A O    1 
HETATM 6682 O  O    . HOH   E 4 .   ? 14.851 -4.663  20.558  1.00 42.77 ?  1307 HOH   A O    1 
HETATM 6683 O  O    . HOH   E 4 .   ? 6.975  -8.125  12.006  1.00 20.64 ?  1308 HOH   A O    1 
HETATM 6684 O  O    . HOH   E 4 .   ? 7.943  -12.588 -0.739  1.00 21.98 ?  1309 HOH   A O    1 
HETATM 6685 O  O    . HOH   E 4 .   ? 0.810  -4.466  0.365   1.00 31.50 ?  1310 HOH   A O    1 
HETATM 6686 O  O    . HOH   E 4 .   ? 15.220 -12.299 18.723  1.00 35.73 ?  1311 HOH   A O    1 
HETATM 6687 O  O    . HOH   E 4 .   ? 19.806 -12.496 -8.970  1.00 25.39 ?  1312 HOH   A O    1 
HETATM 6688 O  O    . HOH   E 4 .   ? 28.568 -10.592 -14.048 1.00 40.62 ?  1313 HOH   A O    1 
HETATM 6689 O  O    . HOH   E 4 .   ? 18.833 -22.010 6.926   1.00 30.15 ?  1314 HOH   A O    1 
HETATM 6690 O  O    . HOH   E 4 .   ? 42.467 10.514  5.178   1.00 19.17 ?  1315 HOH   A O    1 
HETATM 6691 O  O    . HOH   E 4 .   ? 12.150 0.376   14.990  1.00 35.08 ?  1316 HOH   A O    1 
HETATM 6692 O  O    . HOH   E 4 .   ? 9.845  -21.326 5.785   1.00 17.08 ?  1317 HOH   A O    1 
HETATM 6693 O  O    . HOH   E 4 .   ? 28.234 -6.279  19.621  1.00 40.43 ?  1318 HOH   A O    1 
HETATM 6694 O  O    . HOH   E 4 .   ? 14.434 -24.727 11.607  1.00 34.14 ?  1319 HOH   A O    1 
HETATM 6695 O  O    . HOH   E 4 .   ? 14.389 -0.525  -11.958 1.00 22.94 ?  1320 HOH   A O    1 
HETATM 6696 O  O    . HOH   E 4 .   ? 36.155 -5.087  -0.589  1.00 31.27 ?  1321 HOH   A O    1 
HETATM 6697 O  O    . HOH   E 4 .   ? 18.695 -19.380 13.633  1.00 31.60 ?  1322 HOH   A O    1 
HETATM 6698 O  O    . HOH   E 4 .   ? 30.194 -13.325 -8.547  1.00 18.55 ?  1323 HOH   A O    1 
HETATM 6699 O  O    . HOH   E 4 .   ? 7.650  -6.299  -6.539  1.00 39.70 ?  1324 HOH   A O    1 
HETATM 6700 O  O    . HOH   E 4 .   ? 33.944 -1.021  -8.942  1.00 27.88 ?  1325 HOH   A O    1 
HETATM 6701 O  O    . HOH   E 4 .   ? 14.764 -14.040 16.744  1.00 21.17 ?  1326 HOH   A O    1 
HETATM 6702 O  O    A HOH   E 4 .   ? 14.627 -3.679  3.170   0.60 16.70 ?  1327 HOH   A O    1 
HETATM 6703 O  O    . HOH   E 4 .   ? 3.680  -9.419  9.982   1.00 33.82 ?  1328 HOH   A O    1 
HETATM 6704 O  O    A HOH   E 4 .   ? 17.476 -1.731  0.507   0.60 15.90 ?  1329 HOH   A O    1 
HETATM 6705 O  O    . HOH   E 4 .   ? 14.039 -4.538  -11.804 1.00 33.25 ?  1330 HOH   A O    1 
HETATM 6706 O  O    . HOH   E 4 .   ? 17.133 -18.102 15.173  1.00 24.02 ?  1331 HOH   A O    1 
HETATM 6707 O  O    . HOH   E 4 .   ? 26.461 -19.359 -1.802  1.00 12.90 ?  1332 HOH   A O    1 
HETATM 6708 O  O    . HOH   E 4 .   ? 27.843 0.825   -7.153  1.00 13.17 ?  1333 HOH   A O    1 
HETATM 6709 O  O    B HOH   E 4 .   ? 21.312 -2.459  -2.404  0.40 16.32 ?  1334 HOH   A O    1 
HETATM 6710 O  O    B HOH   E 4 .   ? 22.698 5.643   -1.258  0.40 24.92 ?  1335 HOH   A O    1 
HETATM 6711 O  O    . HOH   E 4 .   ? 14.038 -4.937  17.566  1.00 24.16 ?  1336 HOH   A O    1 
HETATM 6712 O  O    . HOH   E 4 .   ? 37.560 2.799   10.186  1.00 26.29 ?  1337 HOH   A O    1 
HETATM 6713 O  O    B HOH   E 4 .   ? 14.812 3.697   17.228  0.40 30.03 ?  1338 HOH   A O    1 
HETATM 6714 O  O    . HOH   E 4 .   ? 16.990 -19.270 4.975   1.00 14.25 ?  1339 HOH   A O    1 
HETATM 6715 O  O    . HOH   E 4 .   ? 15.120 -8.102  -9.554  1.00 21.05 ?  1340 HOH   A O    1 
HETATM 6716 O  O    . HOH   E 4 .   ? 31.053 -18.166 7.797   1.00 19.23 ?  1341 HOH   A O    1 
HETATM 6717 O  O    . HOH   E 4 .   ? 28.130 -0.139  -13.412 1.00 33.53 ?  1342 HOH   A O    1 
HETATM 6718 O  O    . HOH   E 4 .   ? 27.267 13.709  2.857   1.00 28.89 ?  1343 HOH   A O    1 
HETATM 6719 O  O    . HOH   E 4 .   ? 38.575 4.974   6.891   1.00 14.87 ?  1344 HOH   A O    1 
HETATM 6720 O  O    . HOH   E 4 .   ? 5.259  2.805   5.236   1.00 31.78 ?  1345 HOH   A O    1 
HETATM 6721 O  O    B HOH   E 4 .   ? 21.166 2.549   0.003   0.40 16.75 ?  1346 HOH   A O    1 
HETATM 6722 O  O    . HOH   E 4 .   ? 23.861 -15.707 -9.110  1.00 31.21 ?  1347 HOH   A O    1 
HETATM 6723 O  O    . HOH   E 4 .   ? 20.566 -19.763 -5.014  1.00 26.68 ?  1348 HOH   A O    1 
HETATM 6724 O  O    . HOH   E 4 .   ? 13.254 -1.462  -6.572  1.00 15.99 ?  1349 HOH   A O    1 
HETATM 6725 O  O    . HOH   E 4 .   ? 23.987 -2.136  -2.082  1.00 9.62  ?  1350 HOH   A O    1 
HETATM 6726 O  O    . HOH   E 4 .   ? 31.702 8.246   14.754  1.00 22.13 ?  1351 HOH   A O    1 
HETATM 6727 O  O    B HOH   E 4 .   ? 12.388 6.877   9.928   0.40 30.17 ?  1352 HOH   A O    1 
HETATM 6728 O  O    . HOH   E 4 .   ? 38.092 -1.381  -2.046  1.00 17.62 ?  1353 HOH   A O    1 
HETATM 6729 O  O    . HOH   E 4 .   ? 17.107 -17.850 -4.933  1.00 26.09 ?  1354 HOH   A O    1 
HETATM 6730 O  O    . HOH   E 4 .   ? 38.280 10.103  7.110   1.00 31.90 ?  1355 HOH   A O    1 
HETATM 6731 O  O    . HOH   E 4 .   ? 42.507 4.260   5.229   1.00 30.07 ?  1356 HOH   A O    1 
HETATM 6732 O  O    A HOH   E 4 .   ? 15.229 3.931   17.906  0.60 33.58 ?  1357 HOH   A O    1 
HETATM 6733 O  O    . HOH   E 4 .   ? 24.351 3.540   -1.778  1.00 12.92 ?  1358 HOH   A O    1 
HETATM 6734 O  O    . HOH   E 4 .   ? 39.693 -1.031  -5.257  1.00 18.86 ?  1359 HOH   A O    1 
HETATM 6735 O  O    . HOH   E 4 .   ? 26.774 11.378  1.671   1.00 14.46 ?  1360 HOH   A O    1 
HETATM 6736 O  O    . HOH   E 4 .   ? 37.376 11.908  4.896   1.00 33.38 ?  1361 HOH   A O    1 
HETATM 6737 O  O    . HOH   E 4 .   ? 35.786 -12.712 6.781   1.00 15.13 ?  1362 HOH   A O    1 
HETATM 6738 O  O    A HOH   E 4 .   ? 14.278 0.542   6.881   0.60 19.31 ?  1363 HOH   A O    1 
HETATM 6739 O  O    . HOH   E 4 .   ? 25.607 -0.823  -7.350  1.00 14.37 ?  1364 HOH   A O    1 
HETATM 6740 O  O    . HOH   E 4 .   ? 44.303 7.069   6.414   1.00 25.06 ?  1365 HOH   A O    1 
HETATM 6741 O  O    . HOH   E 4 .   ? 22.317 -19.233 11.412  1.00 32.09 ?  1366 HOH   A O    1 
HETATM 6742 O  O    . HOH   E 4 .   ? 43.873 8.402   -3.171  1.00 23.18 ?  1367 HOH   A O    1 
HETATM 6743 O  O    . HOH   E 4 .   ? 37.213 -2.840  9.665   1.00 39.15 ?  1368 HOH   A O    1 
HETATM 6744 O  O    . HOH   E 4 .   ? 30.875 6.254   -12.274 1.00 28.39 ?  1369 HOH   A O    1 
HETATM 6745 O  O    . HOH   E 4 .   ? 31.034 -13.958 -2.494  1.00 12.60 ?  1370 HOH   A O    1 
HETATM 6746 O  O    . HOH   E 4 .   ? 16.490 -22.070 1.025   1.00 26.83 ?  1371 HOH   A O    1 
HETATM 6747 O  O    . HOH   E 4 .   ? 31.725 -9.376  -6.688  1.00 21.08 ?  1372 HOH   A O    1 
HETATM 6748 O  O    . HOH   E 4 .   ? 33.667 -7.169  4.226   1.00 15.38 ?  1373 HOH   A O    1 
HETATM 6749 O  O    . HOH   E 4 .   ? 14.289 -21.269 -4.135  1.00 29.84 ?  1374 HOH   A O    1 
HETATM 6750 O  O    B HOH   E 4 .   ? 16.068 7.559   9.391   0.40 23.62 ?  1375 HOH   A O    1 
HETATM 6751 O  O    . HOH   E 4 .   ? 30.824 3.072   8.241   1.00 10.94 ?  1376 HOH   A O    1 
HETATM 6752 O  O    A HOH   E 4 .   ? 18.551 9.422   8.982   0.60 16.29 ?  1377 HOH   A O    1 
HETATM 6753 O  O    . HOH   E 4 .   ? 21.915 -21.943 8.457   1.00 26.72 ?  1378 HOH   A O    1 
HETATM 6754 O  O    . HOH   E 4 .   ? 22.682 -12.061 21.886  1.00 38.10 ?  1379 HOH   A O    1 
HETATM 6755 O  O    B HOH   E 4 .   ? 18.248 9.003   8.839   0.40 20.77 ?  1380 HOH   A O    1 
HETATM 6756 O  O    . HOH   E 4 .   ? 22.714 12.483  1.696   1.00 13.25 ?  1381 HOH   A O    1 
HETATM 6757 O  O    A HOH   E 4 .   ? -0.486 -3.128  3.231   0.60 29.45 ?  1382 HOH   A O    1 
HETATM 6758 O  O    . HOH   E 4 .   ? 15.230 -21.619 14.257  1.00 16.59 ?  1383 HOH   A O    1 
HETATM 6759 O  O    B HOH   E 4 .   ? 10.963 2.444   11.983  0.40 24.51 ?  1384 HOH   A O    1 
HETATM 6760 O  O    . HOH   E 4 .   ? 15.533 11.888  7.979   1.00 27.43 ?  1385 HOH   A O    1 
HETATM 6761 O  O    . HOH   E 4 .   ? 22.366 5.335   19.063  1.00 42.26 ?  1386 HOH   A O    1 
HETATM 6762 O  O    . HOH   E 4 .   ? 27.582 -10.671 14.032  1.00 16.08 ?  1387 HOH   A O    1 
HETATM 6763 O  O    . HOH   E 4 .   ? 43.342 7.802   2.600   1.00 21.06 ?  1388 HOH   A O    1 
HETATM 6764 O  O    A HOH   E 4 .   ? 21.218 -2.407  -2.002  0.60 11.14 ?  1389 HOH   A O    1 
HETATM 6765 O  O    . HOH   E 4 .   ? 31.669 -7.288  -9.879  1.00 20.52 ?  1390 HOH   A O    1 
HETATM 6766 O  O    A HOH   E 4 .   ? 8.199  -21.428 4.058   0.60 30.91 ?  1391 HOH   A O    1 
HETATM 6767 O  O    . HOH   E 4 .   ? 24.755 -17.576 12.759  1.00 23.72 ?  1392 HOH   A O    1 
HETATM 6768 O  O    A HOH   E 4 .   ? 9.308  -10.285 19.463  0.60 31.81 ?  1393 HOH   A O    1 
HETATM 6769 O  O    . HOH   E 4 .   ? 13.504 -15.293 -7.337  1.00 24.60 ?  1394 HOH   A O    1 
HETATM 6770 O  O    . HOH   E 4 .   ? 24.362 -7.826  14.472  1.00 16.08 ?  1395 HOH   A O    1 
HETATM 6771 O  O    . HOH   E 4 .   ? 14.072 -23.075 7.458   1.00 17.01 ?  1396 HOH   A O    1 
HETATM 6772 O  O    . HOH   E 4 .   ? 6.513  -5.564  11.339  1.00 19.40 ?  1397 HOH   A O    1 
HETATM 6773 O  O    A HOH   E 4 .   ? 20.043 4.541   -7.479  0.60 15.30 ?  1398 HOH   A O    1 
HETATM 6774 O  O    . HOH   E 4 .   ? 21.239 10.252  15.042  1.00 31.69 ?  1399 HOH   A O    1 
HETATM 6775 O  O    . HOH   E 4 .   ? 37.519 -2.018  5.690   1.00 26.24 ?  1400 HOH   A O    1 
HETATM 6776 O  O    . HOH   E 4 .   ? 32.807 -9.262  5.931   1.00 19.25 ?  1401 HOH   A O    1 
HETATM 6777 O  O    . HOH   E 4 .   ? 27.433 2.311   18.709  1.00 28.36 ?  1402 HOH   A O    1 
HETATM 6778 O  O    . HOH   E 4 .   ? 15.847 2.052   24.694  1.00 49.16 ?  1403 HOH   A O    1 
HETATM 6779 O  O    . HOH   E 4 .   ? 41.591 1.529   4.814   1.00 36.22 ?  1404 HOH   A O    1 
HETATM 6780 O  O    . HOH   E 4 .   ? 11.755 -10.770 17.170  1.00 27.42 ?  1405 HOH   A O    1 
HETATM 6781 O  O    . HOH   E 4 .   ? 27.278 -6.026  -14.031 1.00 36.09 ?  1406 HOH   A O    1 
HETATM 6782 O  O    . HOH   E 4 .   ? 24.520 1.969   -7.011  1.00 19.03 ?  1407 HOH   A O    1 
HETATM 6783 O  O    A HOH   E 4 .   ? 18.930 -0.682  -1.564  0.60 10.47 ?  1408 HOH   A O    1 
HETATM 6784 O  O    A HOH   E 4 .   ? 11.061 1.507   12.847  0.60 19.50 ?  1409 HOH   A O    1 
HETATM 6785 O  O    . HOH   E 4 .   ? 23.434 11.346  4.120   1.00 11.12 ?  1410 HOH   A O    1 
HETATM 6786 O  O    A HOH   E 4 .   ? 15.798 -0.973  5.343   0.60 21.48 ?  1411 HOH   A O    1 
HETATM 6787 O  O    . HOH   E 4 .   ? 20.546 -20.043 2.800   1.00 16.76 ?  1412 HOH   A O    1 
HETATM 6788 O  O    A HOH   E 4 .   ? 21.321 3.143   -0.290  0.60 9.50  ?  1413 HOH   A O    1 
HETATM 6789 O  O    . HOH   E 4 .   ? 30.148 -10.186 12.964  1.00 20.64 ?  1414 HOH   A O    1 
HETATM 6790 O  O    . HOH   E 4 .   ? 26.902 4.127   -0.645  1.00 11.59 ?  1415 HOH   A O    1 
HETATM 6791 O  O    . HOH   E 4 .   ? 23.883 -20.290 -1.341  1.00 14.52 ?  1416 HOH   A O    1 
HETATM 6792 O  O    . HOH   E 4 .   ? 30.813 1.820   16.666  1.00 19.11 ?  1417 HOH   A O    1 
HETATM 6793 O  O    . HOH   E 4 .   ? 6.789  -3.315  13.056  1.00 29.98 ?  1418 HOH   A O    1 
HETATM 6794 O  O    B HOH   E 4 .   ? 11.843 -2.075  -3.044  0.40 12.68 ?  1419 HOH   A O    1 
HETATM 6795 O  O    . HOH   E 4 .   ? 16.242 16.662  8.760   1.00 26.45 ?  1420 HOH   A O    1 
HETATM 6796 O  O    . HOH   E 4 .   ? 21.699 -13.794 -8.074  1.00 35.79 ?  1421 HOH   A O    1 
HETATM 6797 O  O    . HOH   E 4 .   ? 40.879 -8.246  -6.730  1.00 35.99 ?  1422 HOH   A O    1 
HETATM 6798 O  O    . HOH   E 4 .   ? 34.974 -5.218  -3.149  1.00 17.27 ?  1423 HOH   A O    1 
HETATM 6799 O  O    . HOH   E 4 .   ? 32.594 -4.329  -9.917  1.00 26.79 ?  1424 HOH   A O    1 
HETATM 6800 O  O    A HOH   E 4 .   ? 11.052 -0.405  2.026   0.60 20.49 ?  1425 HOH   A O    1 
HETATM 6801 O  O    B HOH   E 4 .   ? 18.698 -1.555  -1.414  0.40 23.05 ?  1426 HOH   A O    1 
HETATM 6802 O  O    . HOH   E 4 .   ? 30.422 -13.000 13.477  1.00 18.99 ?  1427 HOH   A O    1 
HETATM 6803 O  O    . HOH   E 4 .   ? 36.733 -4.992  5.343   1.00 23.14 ?  1428 HOH   A O    1 
HETATM 6804 O  O    . HOH   E 4 .   ? 32.561 -10.662 3.116   1.00 29.65 ?  1429 HOH   A O    1 
HETATM 6805 O  O    . HOH   E 4 .   ? 44.903 -0.583  2.926   1.00 43.35 ?  1430 HOH   A O    1 
HETATM 6806 O  O    A HOH   E 4 .   ? 9.060  -12.176 17.268  0.60 39.01 ?  1431 HOH   A O    1 
HETATM 6807 O  O    . HOH   E 4 .   ? 16.023 6.977   3.064   1.00 17.53 ?  1432 HOH   A O    1 
HETATM 6808 O  O    B HOH   E 4 .   ? 11.454 0.505   2.432   0.40 25.10 ?  1433 HOH   A O    1 
HETATM 6809 O  O    . HOH   E 4 .   ? 10.350 -13.725 -1.565  1.00 16.67 ?  1434 HOH   A O    1 
HETATM 6810 O  O    . HOH   E 4 .   ? 22.710 8.068   18.395  1.00 42.71 ?  1435 HOH   A O    1 
HETATM 6811 O  O    A HOH   E 4 .   ? 24.046 3.956   -4.866  0.60 18.10 ?  1436 HOH   A O    1 
HETATM 6812 O  O    . HOH   E 4 .   ? 27.225 -3.209  19.273  1.00 31.71 ?  1437 HOH   A O    1 
HETATM 6813 O  O    . HOH   E 4 .   ? 21.309 -9.318  21.315  1.00 44.57 ?  1438 HOH   A O    1 
HETATM 6814 O  O    . HOH   E 4 .   ? 16.194 -14.254 20.323  1.00 44.81 ?  1439 HOH   A O    1 
HETATM 6815 O  O    A HOH   E 4 .   ? 18.836 2.019   -0.685  0.60 11.27 ?  1440 HOH   A O    1 
HETATM 6816 O  O    . HOH   E 4 .   ? 23.667 -8.065  17.079  1.00 20.14 ?  1441 HOH   A O    1 
HETATM 6817 O  O    . HOH   E 4 .   ? 20.575 -17.902 24.801  1.00 43.44 ?  1442 HOH   A O    1 
HETATM 6818 O  O    . HOH   E 4 .   ? 23.170 7.649   -3.134  1.00 23.05 ?  1443 HOH   A O    1 
HETATM 6819 O  O    . HOH   E 4 .   ? 10.400 -22.178 -1.185  1.00 49.69 ?  1444 HOH   A O    1 
HETATM 6820 O  O    . HOH   E 4 .   ? 23.304 -20.969 1.302   1.00 17.19 ?  1445 HOH   A O    1 
HETATM 6821 O  O    . HOH   E 4 .   ? 21.614 -14.739 17.981  1.00 48.32 ?  1446 HOH   A O    1 
HETATM 6822 O  O    A HOH   E 4 .   ? 16.228 2.932   -1.363  0.60 18.34 ?  1447 HOH   A O    1 
HETATM 6823 O  O    . HOH   E 4 .   ? 34.394 -8.110  -0.597  1.00 27.83 ?  1448 HOH   A O    1 
HETATM 6824 O  O    . HOH   E 4 .   ? 9.421  -16.286 -1.923  1.00 39.72 ?  1449 HOH   A O    1 
HETATM 6825 O  O    . HOH   E 4 .   ? 30.596 14.764  2.801   1.00 17.28 ?  1450 HOH   A O    1 
HETATM 6826 O  O    . HOH   E 4 .   ? 19.528 -10.941 23.976  1.00 60.13 ?  1451 HOH   A O    1 
HETATM 6827 O  O    . HOH   E 4 .   ? 27.652 6.963   -6.361  1.00 31.41 ?  1452 HOH   A O    1 
HETATM 6828 O  O    . HOH   E 4 .   ? 18.437 -16.156 16.520  1.00 34.65 ?  1453 HOH   A O    1 
HETATM 6829 O  O    . HOH   E 4 .   ? 31.306 -12.799 0.004   1.00 17.82 ?  1454 HOH   A O    1 
HETATM 6830 O  O    . HOH   E 4 .   ? 37.657 -8.810  -3.401  1.00 24.34 ?  1455 HOH   A O    1 
HETATM 6831 O  O    . HOH   E 4 .   ? -1.338 -4.956  7.856   1.00 41.81 ?  1456 HOH   A O    1 
HETATM 6832 O  O    . HOH   E 4 .   ? 18.358 4.997   -15.051 1.00 46.94 ?  1457 HOH   A O    1 
HETATM 6833 O  O    A HOH   E 4 .   ? 14.018 -0.364  3.543   0.60 20.58 ?  1458 HOH   A O    1 
HETATM 6834 O  O    . HOH   E 4 .   ? 29.838 -16.088 10.595  1.00 34.30 ?  1459 HOH   A O    1 
HETATM 6835 O  O    . HOH   E 4 .   ? 25.359 8.239   -4.790  1.00 20.45 ?  1460 HOH   A O    1 
HETATM 6836 O  O    B HOH   E 4 .   ? 18.687 1.234   -0.342  0.40 16.76 ?  1461 HOH   A O    1 
HETATM 6837 O  O    . HOH   E 4 .   ? 32.480 -16.002 10.750  1.00 33.85 ?  1462 HOH   A O    1 
HETATM 6838 O  O    . HOH   E 4 .   ? 29.684 -1.988  -12.760 1.00 44.37 ?  1463 HOH   A O    1 
HETATM 6839 O  O    . HOH   E 4 .   ? 19.837 -17.327 -5.010  1.00 22.78 ?  1464 HOH   A O    1 
HETATM 6840 O  O    . HOH   E 4 .   ? 23.175 -22.303 -3.421  1.00 33.67 ?  1465 HOH   A O    1 
HETATM 6841 O  O    . HOH   E 4 .   ? 24.805 5.599   20.840  1.00 46.04 ?  1466 HOH   A O    1 
HETATM 6842 O  O    . HOH   E 4 .   ? 24.561 14.493  7.903   1.00 29.10 ?  1467 HOH   A O    1 
HETATM 6843 O  O    B HOH   E 4 .   ? 12.821 2.416   -0.265  0.40 22.89 ?  1468 HOH   A O    1 
HETATM 6844 O  O    . HOH   E 4 .   ? 26.822 11.626  -1.206  1.00 24.75 ?  1469 HOH   A O    1 
HETATM 6845 O  O    . HOH   E 4 .   ? 39.581 -7.055  -3.592  1.00 46.87 ?  1470 HOH   A O    1 
HETATM 6846 O  O    . HOH   E 4 .   ? 15.681 -21.483 3.694   1.00 21.58 ?  1471 HOH   A O    1 
HETATM 6847 O  O    A HOH   E 4 .   ? 21.915 5.264   -5.775  0.60 23.87 ?  1472 HOH   A O    1 
HETATM 6848 O  O    . HOH   E 4 .   ? 12.033 -13.406 16.426  1.00 44.76 ?  1473 HOH   A O    1 
HETATM 6849 O  O    . HOH   E 4 .   ? 11.050 -14.770 -6.078  1.00 30.19 ?  1474 HOH   A O    1 
HETATM 6850 O  O    . HOH   E 4 .   ? 27.561 -11.402 16.554  1.00 36.94 ?  1475 HOH   A O    1 
HETATM 6851 O  O    . HOH   E 4 .   ? 18.701 10.737  11.380  1.00 29.90 ?  1476 HOH   A O    1 
HETATM 6852 O  O    . HOH   E 4 .   ? 25.810 10.754  -3.639  1.00 21.85 ?  1477 HOH   A O    1 
HETATM 6853 O  O    . HOH   E 4 .   ? 23.515 13.693  5.561   1.00 17.44 ?  1478 HOH   A O    1 
HETATM 6854 O  O    . HOH   E 4 .   ? 12.375 1.651   17.375  1.00 38.20 ?  1479 HOH   A O    1 
HETATM 6855 O  O    . HOH   E 4 .   ? 23.117 11.821  -3.979  1.00 17.65 ?  1480 HOH   A O    1 
HETATM 6856 O  O    . HOH   E 4 .   ? 28.860 8.994   17.452  1.00 35.58 ?  1481 HOH   A O    1 
HETATM 6857 O  O    . HOH   E 4 .   ? 35.215 7.439   12.217  1.00 46.98 ?  1482 HOH   A O    1 
HETATM 6858 O  O    . HOH   E 4 .   ? 17.365 -18.715 19.861  1.00 43.25 ?  1483 HOH   A O    1 
HETATM 6859 O  O    . HOH   E 4 .   ? 18.057 -16.295 -8.684  1.00 38.92 ?  1484 HOH   A O    1 
HETATM 6860 O  O    . HOH   E 4 .   ? 40.926 -4.002  -0.360  1.00 35.11 ?  1485 HOH   A O    1 
HETATM 6861 O  O    . HOH   E 4 .   ? 15.600 -17.164 -6.924  1.00 28.82 ?  1486 HOH   A O    1 
HETATM 6862 O  O    . HOH   E 4 .   ? 20.455 -16.126 -7.315  1.00 26.17 ?  1487 HOH   A O    1 
HETATM 6863 O  O    . HOH   E 4 .   ? 16.753 -20.610 16.237  1.00 27.38 ?  1488 HOH   A O    1 
HETATM 6864 O  O    . HOH   E 4 .   ? 30.940 0.729   19.148  1.00 37.68 ?  1489 HOH   A O    1 
HETATM 6865 O  O    . HOH   E 4 .   ? 15.895 -6.758  -11.769 1.00 41.85 ?  1490 HOH   A O    1 
HETATM 6866 O  O    . HOH   E 4 .   ? 13.995 -10.306 -10.811 1.00 32.72 ?  1491 HOH   A O    1 
HETATM 6867 O  O    B HOH   E 4 .   ? 10.684 -1.633  -5.538  0.40 17.97 ?  1492 HOH   A O    1 
HETATM 6868 O  O    . HOH   E 4 .   ? 28.478 -4.682  -12.326 1.00 36.44 ?  1493 HOH   A O    1 
HETATM 6869 O  O    . HOH   E 4 .   ? 44.470 10.395  -1.676  1.00 27.56 ?  1494 HOH   A O    1 
HETATM 6870 O  O    . HOH   E 4 .   ? 41.629 9.246   -4.175  1.00 29.87 ?  1495 HOH   A O    1 
HETATM 6871 O  O    . HOH   E 4 .   ? 23.333 -12.912 19.383  1.00 41.45 ?  1496 HOH   A O    1 
HETATM 6872 O  O    . HOH   E 4 .   ? 31.334 -0.578  -10.643 1.00 29.57 ?  1497 HOH   A O    1 
HETATM 6873 O  O    B HOH   E 4 .   ? 10.248 6.906   14.117  0.40 35.41 ?  1498 HOH   A O    1 
HETATM 6874 O  O    . HOH   E 4 .   ? 40.460 -0.265  -7.810  1.00 32.47 ?  1499 HOH   A O    1 
HETATM 6875 O  O    B HOH   E 4 .   ? 10.863 0.165   -1.347  0.40 27.57 ?  1500 HOH   A O    1 
HETATM 6876 O  O    . HOH   E 4 .   ? 39.190 2.396   7.562   1.00 31.32 ?  1501 HOH   A O    1 
HETATM 6877 O  O    . HOH   E 4 .   ? 28.615 -7.876  -15.256 1.00 46.82 ?  1502 HOH   A O    1 
HETATM 6878 O  O    . HOH   E 4 .   ? 18.534 -23.247 1.913   1.00 37.47 ?  1503 HOH   A O    1 
HETATM 6879 O  O    . HOH   E 4 .   ? 19.984 -22.365 4.183   1.00 28.59 ?  1504 HOH   A O    1 
HETATM 6880 O  O    . HOH   E 4 .   ? 14.100 -25.386 8.880   1.00 27.80 ?  1505 HOH   A O    1 
HETATM 6881 O  O    . HOH   E 4 .   ? 16.123 -23.360 5.711   1.00 29.08 ?  1506 HOH   A O    1 
HETATM 6882 O  O    . HOH   E 4 .   ? 30.662 -5.781  -11.848 1.00 43.62 ?  1507 HOH   A O    1 
HETATM 6883 O  O    . HOH   E 4 .   ? 30.641 5.837   -14.760 1.00 36.21 ?  1508 HOH   A O    1 
HETATM 6884 O  O    . HOH   E 4 .   ? 37.407 -6.678  7.470   1.00 22.84 ?  1509 HOH   A O    1 
HETATM 6885 O  O    . HOH   E 4 .   ? 23.130 -23.794 1.697   1.00 30.53 ?  1510 HOH   A O    1 
HETATM 6886 O  O    . HOH   E 4 .   ? 28.970 14.357  0.959   1.00 45.98 ?  1511 HOH   A O    1 
HETATM 6887 O  O    B HOH   E 4 .   ? 10.515 5.402   11.514  0.40 33.29 ?  1512 HOH   A O    1 
HETATM 6888 O  O    . HOH   E 4 .   ? 39.561 0.028   6.553   1.00 29.47 ?  1513 HOH   A O    1 
HETATM 6889 O  O    B HOH   E 4 .   ? 11.192 8.806   7.902   0.40 32.30 ?  1514 HOH   A O    1 
HETATM 6890 O  O    . HOH   E 4 .   ? 38.059 13.877  6.685   1.00 52.27 ?  1515 HOH   A O    1 
HETATM 6891 O  O    . HOH   E 4 .   ? 14.846 8.540   5.052   1.00 36.56 ?  1516 HOH   A O    1 
HETATM 6892 O  O    . HOH   E 4 .   ? 8.203  -3.022  -5.681  1.00 43.86 ?  1517 HOH   A O    1 
HETATM 6893 O  O    . HOH   E 4 .   ? 36.466 -6.497  10.094  1.00 41.34 ?  1518 HOH   A O    1 
HETATM 6894 O  O    . HOH   E 4 .   ? 21.988 -24.084 4.456   1.00 24.92 ?  1519 HOH   A O    1 
HETATM 6895 O  O    . HOH   E 4 .   ? 17.405 -6.765  -14.151 1.00 34.47 ?  1520 HOH   A O    1 
HETATM 6896 O  O    . HOH   E 4 .   ? 24.019 8.995   -7.223  1.00 31.93 ?  1521 HOH   A O    1 
HETATM 6897 O  O    . HOH   E 4 .   ? 16.413 -21.084 18.856  1.00 33.78 ?  1522 HOH   A O    1 
HETATM 6898 O  O    . HOH   E 4 .   ? 15.943 -12.308 27.508  1.00 39.95 ?  1523 HOH   A O    1 
HETATM 6899 O  O    . HOH   E 4 .   ? 14.631 -22.812 19.865  1.00 31.27 ?  1524 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 4 .   ? 29.830 -22.462 5.459   1.00 19.17 ?  201  HOH   B O    1 
HETATM 6901 O  O    . HOH   F 4 .   ? 29.755 -34.123 -0.501  1.00 32.99 ?  202  HOH   B O    1 
HETATM 6902 O  O    . HOH   F 4 .   ? 48.115 -6.873  15.488  1.00 36.85 ?  203  HOH   B O    1 
HETATM 6903 O  O    . HOH   F 4 .   ? 52.910 -13.386 -20.348 1.00 33.44 ?  204  HOH   B O    1 
HETATM 6904 O  O    . HOH   F 4 .   ? 27.759 -29.214 -1.954  1.00 34.43 ?  205  HOH   B O    1 
HETATM 6905 O  O    . HOH   F 4 .   ? 59.165 -18.792 6.667   1.00 37.00 ?  206  HOH   B O    1 
HETATM 6906 O  O    . HOH   F 4 .   ? 41.789 -35.856 -17.464 1.00 27.12 ?  207  HOH   B O    1 
HETATM 6907 O  O    . HOH   F 4 .   ? 41.406 -7.757  5.458   1.00 36.05 ?  208  HOH   B O    1 
HETATM 6908 O  O    . HOH   F 4 .   ? 55.317 -16.457 -14.408 1.00 34.36 ?  209  HOH   B O    1 
HETATM 6909 O  O    . HOH   F 4 .   ? 27.827 -41.852 -15.177 1.00 35.35 ?  210  HOH   B O    1 
HETATM 6910 O  O    . HOH   F 4 .   ? 47.406 -7.377  -4.000  1.00 39.95 ?  211  HOH   B O    1 
HETATM 6911 O  O    . HOH   F 4 .   ? 49.347 -22.730 -19.789 1.00 46.45 ?  212  HOH   B O    1 
HETATM 6912 O  O    . HOH   F 4 .   ? 37.986 -39.489 -0.285  1.00 41.04 ?  213  HOH   B O    1 
HETATM 6913 O  O    . HOH   F 4 .   ? 29.896 -26.345 3.990   1.00 26.37 ?  214  HOH   B O    1 
HETATM 6914 O  O    . HOH   F 4 .   ? 56.397 -19.713 7.149   1.00 32.39 ?  215  HOH   B O    1 
HETATM 6915 O  O    . HOH   F 4 .   ? 58.236 -12.959 8.329   1.00 32.47 ?  216  HOH   B O    1 
HETATM 6916 O  O    . HOH   F 4 .   ? 54.436 -9.351  -8.851  1.00 17.34 ?  217  HOH   B O    1 
HETATM 6917 O  O    . HOH   F 4 .   ? 30.214 -41.004 -8.227  1.00 15.32 ?  218  HOH   B O    1 
HETATM 6918 O  O    . HOH   F 4 .   ? 57.718 -24.412 4.994   1.00 33.55 ?  219  HOH   B O    1 
HETATM 6919 O  O    . HOH   F 4 .   ? 50.272 -3.347  7.134   1.00 34.01 ?  220  HOH   B O    1 
HETATM 6920 O  O    . HOH   F 4 .   ? 57.147 -26.853 -7.687  1.00 39.24 ?  221  HOH   B O    1 
HETATM 6921 O  O    . HOH   F 4 .   ? 50.747 -6.100  0.114   1.00 25.73 ?  222  HOH   B O    1 
HETATM 6922 O  O    . HOH   F 4 .   ? 44.413 -7.226  2.063   1.00 32.37 ?  223  HOH   B O    1 
HETATM 6923 O  O    . HOH   F 4 .   ? 30.882 -28.812 4.256   1.00 24.68 ?  224  HOH   B O    1 
HETATM 6924 O  O    . HOH   F 4 .   ? 40.646 -16.023 14.058  1.00 23.80 ?  225  HOH   B O    1 
HETATM 6925 O  O    . HOH   F 4 .   ? 34.544 -36.367 -7.290  1.00 17.14 ?  226  HOH   B O    1 
HETATM 6926 O  O    . HOH   F 4 .   ? 41.508 -39.130 -15.001 1.00 20.26 ?  227  HOH   B O    1 
HETATM 6927 O  O    . HOH   F 4 .   ? 37.075 -19.748 -18.101 1.00 36.37 ?  228  HOH   B O    1 
HETATM 6928 O  O    . HOH   F 4 .   ? 57.413 -16.245 -12.222 1.00 17.77 ?  229  HOH   B O    1 
HETATM 6929 O  O    . HOH   F 4 .   ? 45.153 -34.996 6.796   1.00 38.90 ?  230  HOH   B O    1 
HETATM 6930 O  O    . HOH   F 4 .   ? 35.927 -43.234 -8.609  1.00 31.04 ?  231  HOH   B O    1 
HETATM 6931 O  O    . HOH   F 4 .   ? 56.704 -30.759 -7.773  1.00 31.01 ?  232  HOH   B O    1 
HETATM 6932 O  O    . HOH   F 4 .   ? 32.808 -43.781 -11.427 1.00 18.55 ?  233  HOH   B O    1 
HETATM 6933 O  O    . HOH   F 4 .   ? 41.377 -9.649  12.991  1.00 20.81 ?  234  HOH   B O    1 
HETATM 6934 O  O    . HOH   F 4 .   ? 28.360 -19.664 -13.127 1.00 23.65 ?  235  HOH   B O    1 
HETATM 6935 O  O    . HOH   F 4 .   ? 39.333 -10.886 6.087   1.00 25.95 ?  236  HOH   B O    1 
HETATM 6936 O  O    . HOH   F 4 .   ? 48.505 -36.492 -15.619 1.00 45.41 ?  237  HOH   B O    1 
HETATM 6937 O  O    . HOH   F 4 .   ? 50.717 -12.950 -0.539  1.00 10.83 ?  238  HOH   B O    1 
HETATM 6938 O  O    . HOH   F 4 .   ? 51.595 -13.853 10.903  1.00 30.03 ?  239  HOH   B O    1 
HETATM 6939 O  O    . HOH   F 4 .   ? 35.066 -8.011  -3.071  1.00 17.77 ?  240  HOH   B O    1 
HETATM 6940 O  O    . HOH   F 4 .   ? 43.107 -43.220 -8.324  1.00 27.43 ?  241  HOH   B O    1 
HETATM 6941 O  O    . HOH   F 4 .   ? 51.671 -6.502  4.398   1.00 18.39 ?  242  HOH   B O    1 
HETATM 6942 O  O    . HOH   F 4 .   ? 42.570 -25.389 2.561   1.00 14.03 ?  243  HOH   B O    1 
HETATM 6943 O  O    . HOH   F 4 .   ? 31.780 -17.967 -14.497 1.00 32.06 ?  244  HOH   B O    1 
HETATM 6944 O  O    . HOH   F 4 .   ? 34.901 -24.666 13.812  1.00 30.13 ?  245  HOH   B O    1 
HETATM 6945 O  O    . HOH   F 4 .   ? 46.360 -1.573  13.241  1.00 29.79 ?  246  HOH   B O    1 
HETATM 6946 O  O    . HOH   F 4 .   ? 39.488 -11.141 0.300   1.00 15.78 ?  247  HOH   B O    1 
HETATM 6947 O  O    . HOH   F 4 .   ? 25.439 -25.995 -1.387  1.00 30.32 ?  248  HOH   B O    1 
HETATM 6948 O  O    . HOH   F 4 .   ? 42.645 -22.883 3.785   1.00 10.76 ?  249  HOH   B O    1 
HETATM 6949 O  O    . HOH   F 4 .   ? 43.174 -32.344 -17.164 1.00 21.34 ?  250  HOH   B O    1 
HETATM 6950 O  O    . HOH   F 4 .   ? 41.868 -23.536 9.216   1.00 15.33 ?  251  HOH   B O    1 
HETATM 6951 O  O    . HOH   F 4 .   ? 45.002 -43.490 -10.597 1.00 26.99 ?  252  HOH   B O    1 
HETATM 6952 O  O    . HOH   F 4 .   ? 57.605 -24.372 -3.912  1.00 20.96 ?  253  HOH   B O    1 
HETATM 6953 O  O    . HOH   F 4 .   ? 44.533 -27.765 -0.766  1.00 20.30 ?  254  HOH   B O    1 
HETATM 6954 O  O    . HOH   F 4 .   ? 29.703 -25.213 -10.866 1.00 15.11 ?  255  HOH   B O    1 
HETATM 6955 O  O    . HOH   F 4 .   ? 34.216 -18.582 11.373  1.00 22.31 ?  256  HOH   B O    1 
HETATM 6956 O  O    . HOH   F 4 .   ? 58.154 -10.628 -4.111  1.00 19.40 ?  257  HOH   B O    1 
HETATM 6957 O  O    . HOH   F 4 .   ? 40.284 -12.728 -11.538 1.00 14.27 ?  258  HOH   B O    1 
HETATM 6958 O  O    . HOH   F 4 .   ? 38.429 -11.043 -2.281  1.00 18.23 ?  259  HOH   B O    1 
HETATM 6959 O  O    . HOH   F 4 .   ? 38.925 -12.062 12.296  1.00 33.37 ?  260  HOH   B O    1 
HETATM 6960 O  O    . HOH   F 4 .   ? 27.126 -31.839 -10.005 1.00 19.45 ?  261  HOH   B O    1 
HETATM 6961 O  O    . HOH   F 4 .   ? 42.807 -20.293 -20.802 1.00 37.07 ?  262  HOH   B O    1 
HETATM 6962 O  O    . HOH   F 4 .   ? 30.860 -15.755 2.616   1.00 12.88 ?  263  HOH   B O    1 
HETATM 6963 O  O    . HOH   F 4 .   ? 48.013 -22.797 5.767   1.00 15.59 ?  264  HOH   B O    1 
HETATM 6964 O  O    . HOH   F 4 .   ? 28.456 -30.765 -14.811 1.00 27.61 ?  265  HOH   B O    1 
HETATM 6965 O  O    . HOH   F 4 .   ? 57.129 -12.096 12.218  1.00 35.14 ?  266  HOH   B O    1 
HETATM 6966 O  O    . HOH   F 4 .   ? 33.515 -17.036 8.006   1.00 18.11 ?  267  HOH   B O    1 
HETATM 6967 O  O    . HOH   F 4 .   ? 50.999 -39.931 -8.373  1.00 27.90 ?  268  HOH   B O    1 
HETATM 6968 O  O    . HOH   F 4 .   ? 57.477 -9.214  1.324   1.00 18.75 ?  269  HOH   B O    1 
HETATM 6969 O  O    . HOH   F 4 .   ? 49.324 -28.702 -6.997  1.00 14.47 ?  270  HOH   B O    1 
HETATM 6970 O  O    . HOH   F 4 .   ? 43.337 -15.778 -12.214 1.00 13.22 ?  271  HOH   B O    1 
HETATM 6971 O  O    . HOH   F 4 .   ? 28.281 -34.353 -9.493  1.00 17.42 ?  272  HOH   B O    1 
HETATM 6972 O  O    . HOH   F 4 .   ? 46.605 -31.266 -4.896  1.00 19.75 ?  273  HOH   B O    1 
HETATM 6973 O  O    . HOH   F 4 .   ? 49.742 -0.502  10.223  1.00 30.84 ?  274  HOH   B O    1 
HETATM 6974 O  O    . HOH   F 4 .   ? 56.931 -8.645  8.394   1.00 18.89 ?  275  HOH   B O    1 
HETATM 6975 O  O    . HOH   F 4 .   ? 56.161 -23.415 -14.831 1.00 25.10 ?  276  HOH   B O    1 
HETATM 6976 O  O    . HOH   F 4 .   ? 30.569 -42.246 -10.668 1.00 27.38 ?  277  HOH   B O    1 
HETATM 6977 O  O    . HOH   F 4 .   ? 42.329 -9.916  9.299   1.00 19.67 ?  278  HOH   B O    1 
HETATM 6978 O  O    . HOH   F 4 .   ? 37.401 -35.650 7.140   1.00 31.81 ?  279  HOH   B O    1 
HETATM 6979 O  O    . HOH   F 4 .   ? 42.206 -10.093 -15.010 1.00 34.34 ?  280  HOH   B O    1 
HETATM 6980 O  O    . HOH   F 4 .   ? 34.450 -12.786 2.555   1.00 22.33 ?  281  HOH   B O    1 
HETATM 6981 O  O    . HOH   F 4 .   ? 47.955 -24.379 -17.902 1.00 31.45 ?  282  HOH   B O    1 
HETATM 6982 O  O    . HOH   F 4 .   ? 34.894 -33.330 -19.319 1.00 33.58 ?  283  HOH   B O    1 
HETATM 6983 O  O    . HOH   F 4 .   ? 27.916 -22.891 -8.044  1.00 15.89 ?  284  HOH   B O    1 
HETATM 6984 O  O    . HOH   F 4 .   ? 41.210 -5.488  11.531  1.00 43.43 ?  285  HOH   B O    1 
HETATM 6985 O  O    . HOH   F 4 .   ? 48.732 -20.037 5.867   1.00 13.03 ?  286  HOH   B O    1 
HETATM 6986 O  O    . HOH   F 4 .   ? 48.421 -25.056 3.039   1.00 12.24 ?  287  HOH   B O    1 
HETATM 6987 O  O    . HOH   F 4 .   ? 52.539 -10.456 12.934  1.00 21.15 ?  288  HOH   B O    1 
HETATM 6988 O  O    . HOH   F 4 .   ? 27.549 -26.752 -15.761 1.00 32.56 ?  289  HOH   B O    1 
HETATM 6989 O  O    . HOH   F 4 .   ? 47.088 -33.966 -4.730  1.00 15.75 ?  290  HOH   B O    1 
HETATM 6990 O  O    . HOH   F 4 .   ? 33.470 -15.297 -13.980 1.00 19.71 ?  291  HOH   B O    1 
HETATM 6991 O  O    . HOH   F 4 .   ? 42.433 -34.697 3.727   1.00 25.79 ?  292  HOH   B O    1 
HETATM 6992 O  O    . HOH   F 4 .   ? 45.355 -33.350 -16.034 1.00 22.01 ?  293  HOH   B O    1 
HETATM 6993 O  O    . HOH   F 4 .   ? 36.786 -12.783 -1.520  1.00 26.10 ?  294  HOH   B O    1 
HETATM 6994 O  O    . HOH   F 4 .   ? 57.675 -22.092 2.964   1.00 25.04 ?  295  HOH   B O    1 
HETATM 6995 O  O    . HOH   F 4 .   ? 46.882 -29.593 9.796   1.00 30.28 ?  296  HOH   B O    1 
HETATM 6996 O  O    . HOH   F 4 .   ? 51.233 -37.598 -9.702  1.00 24.02 ?  297  HOH   B O    1 
HETATM 6997 O  O    . HOH   F 4 .   ? 44.605 -27.472 1.918   1.00 13.87 ?  298  HOH   B O    1 
HETATM 6998 O  O    . HOH   F 4 .   ? 59.797 -15.345 8.103   1.00 29.95 ?  299  HOH   B O    1 
HETATM 6999 O  O    . HOH   F 4 .   ? 35.068 -33.622 4.406   1.00 26.79 ?  300  HOH   B O    1 
HETATM 7000 O  O    . HOH   F 4 .   ? 52.601 -35.626 -8.700  1.00 29.45 ?  301  HOH   B O    1 
HETATM 7001 O  O    . HOH   F 4 .   ? 53.141 -16.062 -12.789 1.00 28.12 ?  302  HOH   B O    1 
HETATM 7002 O  O    . HOH   F 4 .   ? 52.532 -29.238 -13.084 1.00 23.17 ?  303  HOH   B O    1 
HETATM 7003 O  O    . HOH   F 4 .   ? 44.048 -29.344 -4.755  1.00 21.89 ?  304  HOH   B O    1 
HETATM 7004 O  O    . HOH   F 4 .   ? 37.554 -18.287 13.066  1.00 27.26 ?  305  HOH   B O    1 
HETATM 7005 O  O    . HOH   F 4 .   ? 42.692 -12.238 -18.541 1.00 27.63 ?  306  HOH   B O    1 
HETATM 7006 O  O    . HOH   F 4 .   ? 43.520 -15.355 18.160  1.00 29.88 ?  307  HOH   B O    1 
HETATM 7007 O  O    . HOH   F 4 .   ? 40.212 -10.809 -9.566  1.00 15.77 ?  308  HOH   B O    1 
HETATM 7008 O  O    . HOH   F 4 .   ? 62.823 -20.123 -0.964  1.00 36.57 ?  309  HOH   B O    1 
HETATM 7009 O  O    . HOH   F 4 .   ? 41.267 -24.495 15.729  1.00 41.65 ?  310  HOH   B O    1 
HETATM 7010 O  O    . HOH   F 4 .   ? 45.906 -40.405 -3.713  1.00 30.22 ?  311  HOH   B O    1 
HETATM 7011 O  O    . HOH   F 4 .   ? 49.983 -24.649 5.781   1.00 32.24 ?  312  HOH   B O    1 
HETATM 7012 O  O    . HOH   F 4 .   ? 41.711 -8.097  1.300   1.00 23.13 ?  313  HOH   B O    1 
HETATM 7013 O  O    . HOH   F 4 .   ? 25.926 -21.499 -3.541  1.00 14.94 ?  314  HOH   B O    1 
HETATM 7014 O  O    . HOH   F 4 .   ? 32.816 -34.609 -5.970  1.00 15.73 ?  315  HOH   B O    1 
HETATM 7015 O  O    . HOH   F 4 .   ? 53.466 -30.207 4.437   1.00 17.39 ?  316  HOH   B O    1 
HETATM 7016 O  O    . HOH   F 4 .   ? 62.689 -13.555 4.726   1.00 26.07 ?  317  HOH   B O    1 
HETATM 7017 O  O    . HOH   F 4 .   ? 37.792 -10.241 -10.773 1.00 15.85 ?  318  HOH   B O    1 
HETATM 7018 O  O    . HOH   F 4 .   ? 48.102 -32.633 -16.717 1.00 42.78 ?  319  HOH   B O    1 
HETATM 7019 O  O    . HOH   F 4 .   ? 43.237 -21.441 10.635  1.00 15.03 ?  320  HOH   B O    1 
HETATM 7020 O  O    . HOH   F 4 .   ? 26.310 -21.035 -6.275  1.00 15.21 ?  321  HOH   B O    1 
HETATM 7021 O  O    . HOH   F 4 .   ? 59.930 -17.143 -10.544 1.00 32.80 ?  322  HOH   B O    1 
HETATM 7022 O  O    . HOH   F 4 .   ? 51.698 -5.970  -8.016  1.00 47.25 ?  323  HOH   B O    1 
HETATM 7023 O  O    . HOH   F 4 .   ? 38.358 -12.807 7.888   1.00 17.66 ?  324  HOH   B O    1 
HETATM 7024 O  O    . HOH   F 4 .   ? 37.183 -30.520 -21.125 1.00 28.58 ?  325  HOH   B O    1 
HETATM 7025 O  O    . HOH   F 4 .   ? 51.421 -32.924 -10.886 1.00 37.42 ?  326  HOH   B O    1 
HETATM 7026 O  O    . HOH   F 4 .   ? 43.135 -34.584 -0.010  1.00 20.27 ?  327  HOH   B O    1 
HETATM 7027 O  O    . HOH   F 4 .   ? 44.635 -24.623 9.516   1.00 18.03 ?  328  HOH   B O    1 
HETATM 7028 O  O    . HOH   F 4 .   ? 33.746 -31.176 11.057  1.00 35.85 ?  329  HOH   B O    1 
HETATM 7029 O  O    . HOH   F 4 .   ? 53.669 -12.543 -22.317 1.00 34.19 ?  330  HOH   B O    1 
HETATM 7030 O  O    . HOH   F 4 .   ? 36.696 -12.437 4.232   1.00 17.46 ?  331  HOH   B O    1 
HETATM 7031 O  O    . HOH   F 4 .   ? 39.456 -23.434 -20.349 1.00 36.19 ?  332  HOH   B O    1 
HETATM 7032 O  O    . HOH   F 4 .   ? 48.551 -11.866 -13.803 1.00 24.93 ?  333  HOH   B O    1 
HETATM 7033 O  O    . HOH   F 4 .   ? 47.190 -24.507 8.092   1.00 25.61 ?  334  HOH   B O    1 
HETATM 7034 O  O    . HOH   F 4 .   ? 38.346 -9.334  -13.299 1.00 27.14 ?  335  HOH   B O    1 
HETATM 7035 O  O    . HOH   F 4 .   ? 44.126 -1.726  7.539   1.00 43.18 ?  336  HOH   B O    1 
HETATM 7036 O  O    . HOH   F 4 .   ? 45.779 -36.239 -16.179 1.00 32.74 ?  337  HOH   B O    1 
HETATM 7037 O  O    . HOH   F 4 .   ? 27.868 -14.767 -9.494  1.00 32.80 ?  338  HOH   B O    1 
HETATM 7038 O  O    . HOH   F 4 .   ? 42.833 -43.490 -14.481 1.00 39.02 ?  339  HOH   B O    1 
HETATM 7039 O  O    . HOH   F 4 .   ? 47.476 -27.445 1.943   1.00 13.58 ?  340  HOH   B O    1 
HETATM 7040 O  O    . HOH   F 4 .   ? 46.863 -19.882 12.205  1.00 29.72 ?  341  HOH   B O    1 
HETATM 7041 O  O    . HOH   F 4 .   ? 36.978 -15.007 -16.536 1.00 37.30 ?  342  HOH   B O    1 
HETATM 7042 O  O    . HOH   F 4 .   ? 28.865 -42.929 -12.455 1.00 38.53 ?  343  HOH   B O    1 
HETATM 7043 O  O    . HOH   F 4 .   ? 37.045 -45.173 -9.820  1.00 36.25 ?  344  HOH   B O    1 
HETATM 7044 O  O    . HOH   F 4 .   ? 39.760 -44.240 -11.261 1.00 35.50 ?  345  HOH   B O    1 
HETATM 7045 O  O    . HOH   F 4 .   ? 38.361 -12.275 -16.282 1.00 40.71 ?  346  HOH   B O    1 
HETATM 7046 O  O    . HOH   F 4 .   ? 32.978 -14.693 0.985   1.00 16.93 ?  347  HOH   B O    1 
HETATM 7047 O  O    . HOH   F 4 .   ? 40.411 -43.458 -9.184  1.00 26.58 ?  348  HOH   B O    1 
HETATM 7048 O  O    . HOH   F 4 .   ? 38.583 -22.392 15.032  1.00 38.60 ?  349  HOH   B O    1 
HETATM 7049 O  O    . HOH   F 4 .   ? 27.760 -26.606 -0.637  1.00 27.92 ?  350  HOH   B O    1 
HETATM 7050 O  O    . HOH   F 4 .   ? 33.696 -9.353  -8.810  1.00 30.83 ?  351  HOH   B O    1 
HETATM 7051 O  O    . HOH   F 4 .   ? 55.634 -8.278  10.784  1.00 23.24 ?  352  HOH   B O    1 
HETATM 7052 O  O    . HOH   F 4 .   ? 62.492 -20.055 -5.017  1.00 43.07 ?  353  HOH   B O    1 
HETATM 7053 O  O    . HOH   F 4 .   ? 44.154 -37.318 -17.964 1.00 32.50 ?  354  HOH   B O    1 
HETATM 7054 O  O    . HOH   F 4 .   ? 23.213 -23.718 6.774   1.00 34.85 ?  355  HOH   B O    1 
HETATM 7055 O  O    . HOH   F 4 .   ? 36.025 -8.542  -9.709  1.00 34.23 ?  356  HOH   B O    1 
HETATM 7056 O  O    . HOH   F 4 .   ? 56.579 -7.282  3.041   1.00 27.12 ?  357  HOH   B O    1 
HETATM 7057 O  O    . HOH   F 4 .   ? 34.685 -10.330 7.449   1.00 23.36 ?  358  HOH   B O    1 
HETATM 7058 O  O    . HOH   F 4 .   ? 43.095 -12.719 -21.252 1.00 37.09 ?  359  HOH   B O    1 
HETATM 7059 O  O    . HOH   F 4 .   ? 34.119 -7.802  11.416  1.00 40.04 ?  360  HOH   B O    1 
HETATM 7060 O  O    . HOH   F 4 .   ? 61.480 -19.842 1.554   1.00 31.67 ?  361  HOH   B O    1 
HETATM 7061 O  O    . HOH   F 4 .   ? 40.239 -8.821  9.872   1.00 36.29 ?  362  HOH   B O    1 
HETATM 7062 O  O    . HOH   F 4 .   ? 27.106 -25.968 -11.407 1.00 33.17 ?  363  HOH   B O    1 
HETATM 7063 O  O    . HOH   F 4 .   ? 56.952 -21.539 -16.457 1.00 40.86 ?  364  HOH   B O    1 
HETATM 7064 O  O    . HOH   F 4 .   ? 32.479 -23.645 14.033  1.00 38.44 ?  365  HOH   B O    1 
HETATM 7065 O  O    . HOH   F 4 .   ? 54.159 -5.715  2.968   1.00 34.28 ?  366  HOH   B O    1 
HETATM 7066 O  O    . HOH   F 4 .   ? 58.985 -10.519 9.085   1.00 37.35 ?  367  HOH   B O    1 
HETATM 7067 O  O    . HOH   F 4 .   ? 36.236 -8.749  8.946   1.00 39.08 ?  368  HOH   B O    1 
HETATM 7068 O  O    . HOH   F 4 .   ? 41.787 -10.075 -17.477 1.00 50.42 ?  369  HOH   B O    1 
HETATM 7069 O  O    . HOH   F 4 .   ? 52.077 -12.938 13.245  1.00 31.27 ?  370  HOH   B O    1 
HETATM 7070 O  O    . HOH   F 4 .   ? 39.844 -7.055  7.781   1.00 42.50 ?  371  HOH   B O    1 
HETATM 7071 O  O    . HOH   F 4 .   ? 39.942 -11.373 -14.009 1.00 29.92 ?  372  HOH   B O    1 
HETATM 7072 O  O    . HOH   F 4 .   ? 48.443 -26.529 8.690   1.00 38.74 ?  373  HOH   B O    1 
HETATM 7073 O  O    . HOH   F 4 .   ? 36.570 -22.845 13.266  1.00 22.22 ?  374  HOH   B O    1 
HETATM 7074 O  O    . HOH   F 4 .   ? 38.031 -10.612 10.015  1.00 28.04 ?  375  HOH   B O    1 
HETATM 7075 O  O    . HOH   F 4 .   ? 55.990 -7.713  -0.608  1.00 34.55 ?  376  HOH   B O    1 
HETATM 7076 O  O    . HOH   F 4 .   ? 63.058 -12.380 6.879   1.00 37.04 ?  377  HOH   B O    1 
HETATM 7077 O  O    . HOH   F 4 .   ? 41.824 -6.761  -4.868  1.00 45.82 ?  378  HOH   B O    1 
HETATM 7078 O  O    . HOH   F 4 .   ? 44.041 -5.603  -3.525  1.00 45.94 ?  379  HOH   B O    1 
HETATM 7079 O  O    . HOH   F 4 .   ? 42.642 -17.103 -23.266 1.00 40.57 ?  380  HOH   B O    1 
HETATM 7080 O  O    . HOH   F 4 .   ? 40.126 -7.637  3.195   1.00 34.58 ?  381  HOH   B O    1 
HETATM 7081 O  O    . HOH   F 4 .   ? 52.834 -29.925 7.072   1.00 22.46 ?  382  HOH   B O    1 
HETATM 7082 O  O    . HOH   F 4 .   ? 60.496 -22.290 2.663   1.00 51.03 ?  383  HOH   B O    1 
HETATM 7083 O  O    . HOH   F 4 .   ? 39.699 -14.097 15.690  1.00 45.33 ?  384  HOH   B O    1 
HETATM 7084 O  O    . HOH   F 4 .   ? 46.750 -5.374  2.864   1.00 40.98 ?  385  HOH   B O    1 
HETATM 7085 O  O    . HOH   F 4 .   ? 40.967 -9.791  15.757  1.00 46.58 ?  386  HOH   B O    1 
HETATM 7086 O  O    . HOH   F 4 .   ? 23.879 -20.866 -7.702  1.00 26.55 ?  387  HOH   B O    1 
HETATM 7087 O  O    . HOH   F 4 .   ? 35.418 -33.708 7.228   1.00 41.48 ?  388  HOH   B O    1 
HETATM 7088 O  O    . HOH   F 4 .   ? 35.325 -20.344 13.289  1.00 28.33 ?  389  HOH   B O    1 
HETATM 7089 O  O    . HOH   F 4 .   ? 25.773 -18.953 -12.038 1.00 36.85 ?  390  HOH   B O    1 
HETATM 7090 O  O    . HOH   F 4 .   ? 40.684 -6.630  -0.924  1.00 23.60 ?  391  HOH   B O    1 
HETATM 7091 O  O    . HOH   F 4 .   ? 44.035 -31.703 -3.910  1.00 31.86 ?  392  HOH   B O    1 
HETATM 7092 O  O    . HOH   F 4 .   ? 27.978 -27.107 2.254   1.00 32.23 ?  393  HOH   B O    1 
HETATM 7093 O  O    . HOH   F 4 .   ? 26.586 -27.953 -13.482 1.00 35.39 ?  394  HOH   B O    1 
HETATM 7094 O  O    . HOH   F 4 .   ? 34.420 -33.471 9.604   1.00 33.50 ?  395  HOH   B O    1 
HETATM 7095 O  O    . HOH   F 4 .   ? 50.612 -30.795 8.636   1.00 26.33 ?  396  HOH   B O    1 
HETATM 7096 O  O    . HOH   F 4 .   ? 24.558 -20.720 -10.457 1.00 33.59 ?  397  HOH   B O    1 
HETATM 7097 O  O    . HOH   F 4 .   ? 26.840 -30.652 -12.660 1.00 27.38 ?  398  HOH   B O    1 
HETATM 7098 O  O    . HOH   F 4 .   ? 45.764 -20.241 15.132  1.00 51.10 ?  399  HOH   B O    1 
HETATM 7099 O  O    . HOH   F 4 .   ? 57.530 -6.394  -2.314  1.00 33.36 ?  400  HOH   B O    1 
HETATM 7100 O  O    . HOH   F 4 .   ? 40.871 -11.802 -22.382 1.00 41.34 ?  401  HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.5791 0.5661 0.6151 0.0070  -0.0300 0.0989  3    VAL   A N   
2    N  N   B VAL   A 3   ? 0.5788 0.5680 0.6087 0.0041  -0.0270 0.0839  3    VAL   A N   
3    C  CA  A VAL   A 3   ? 0.5772 0.5648 0.6090 0.0059  -0.0292 0.0986  3    VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.5768 0.5664 0.6029 0.0035  -0.0269 0.0850  3    VAL   A CA  
5    C  C   A VAL   A 3   ? 0.5657 0.5573 0.5837 0.0024  -0.0308 0.1032  3    VAL   A C   
6    C  C   B VAL   A 3   ? 0.5659 0.5584 0.5810 0.0008  -0.0294 0.0955  3    VAL   A C   
7    O  O   A VAL   A 3   ? 0.5677 0.5587 0.5898 0.0040  -0.0321 0.1049  3    VAL   A O   
8    O  O   B VAL   A 3   ? 0.5684 0.5602 0.5879 0.0019  -0.0303 0.0961  3    VAL   A O   
9    C  CB  A VAL   A 3   ? 0.5850 0.5695 0.6234 0.0074  -0.0260 0.0946  3    VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.5837 0.5713 0.6148 0.0048  -0.0238 0.0774  3    VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.5877 0.5711 0.6273 0.0078  -0.0249 0.0931  3    VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.5861 0.5728 0.6180 0.0051  -0.0227 0.0747  3    VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.5876 0.5711 0.6278 0.0079  -0.0246 0.0941  3    VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.5861 0.5729 0.6184 0.0053  -0.0226 0.0754  3    VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.5496 0.5463 0.5466 -0.0031 -0.0301 0.1060  4    ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5157 0.5205 0.4708 -0.0132 -0.0273 0.1171  4    ASN   A CA  
33   C  C   . ASN   A 4   ? 0.4723 0.4882 0.4229 -0.0253 -0.0137 0.1000  4    ASN   A C   
34   O  O   . ASN   A 4   ? 0.4743 0.4892 0.4100 -0.0270 -0.0145 0.1071  4    ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5230 0.5246 0.4376 -0.0115 -0.0379 0.1416  4    ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.5281 0.5256 0.4078 -0.0106 -0.0487 0.1658  4    ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.5314 0.5250 0.3992 -0.0105 -0.0510 0.1733  4    ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.5283 0.5246 0.4000 -0.0087 -0.0532 0.1793  4    ASN   A ND2 
46   N  N   . SER   A 5   ? 0.4245 0.4509 0.3831 -0.0360 -0.0010 0.0756  5    SER   A N   
47   C  CA  . SER   A 5   ? 0.3766 0.4194 0.3483 -0.0438 0.0141  0.0469  5    SER   A CA  
48   C  C   . SER   A 5   ? 0.3222 0.3686 0.2930 -0.0439 0.0277  0.0231  5    SER   A C   
49   O  O   . SER   A 5   ? 0.3333 0.3788 0.2986 -0.0306 0.0252  0.0083  5    SER   A O   
50   C  CB  . SER   A 5   ? 0.3833 0.4355 0.3697 -0.0491 0.0176  0.0420  5    SER   A CB  
51   O  OG  . SER   A 5   ? 0.3882 0.4365 0.3794 -0.0507 0.0221  0.0401  5    SER   A OG  
57   N  N   A PHE   A 6   ? 0.2806 0.3350 0.2621 -0.0542 0.0400  0.0248  6    PHE   A N   
58   N  N   B PHE   A 6   ? 0.2946 0.3384 0.2630 -0.0496 0.0376  0.0182  6    PHE   A N   
59   C  CA  A PHE   A 6   ? 0.2452 0.3019 0.2288 -0.0631 0.0491  0.0336  6    PHE   A CA  
60   C  CA  B PHE   A 6   ? 0.2695 0.3078 0.2298 -0.0545 0.0469  0.0192  6    PHE   A CA  
61   C  C   A PHE   A 6   ? 0.2347 0.2962 0.2368 -0.0698 0.0617  0.0247  6    PHE   A C   
62   C  C   B PHE   A 6   ? 0.2679 0.3002 0.2241 -0.0587 0.0593  0.0249  6    PHE   A C   
63   O  O   A PHE   A 6   ? 0.2377 0.3069 0.2623 -0.0701 0.0609  0.0364  6    PHE   A O   
64   O  O   B PHE   A 6   ? 0.2702 0.3033 0.2281 -0.0624 0.0609  0.0371  6    PHE   A O   
65   C  CB  A PHE   A 6   ? 0.2282 0.2769 0.2012 -0.0569 0.0431  0.0484  6    PHE   A CB  
66   C  CB  B PHE   A 6   ? 0.2500 0.2861 0.2119 -0.0499 0.0418  0.0120  6    PHE   A CB  
67   C  CG  A PHE   A 6   ? 0.2150 0.2569 0.1810 -0.0498 0.0376  0.0584  6    PHE   A CG  
68   C  CG  B PHE   A 6   ? 0.2321 0.2662 0.1988 -0.0458 0.0383  0.0051  6    PHE   A CG  
69   C  CD1 A PHE   A 6   ? 0.2112 0.2484 0.1715 -0.0452 0.0274  0.0612  6    PHE   A CD1 
70   C  CD1 B PHE   A 6   ? 0.2234 0.2569 0.1911 -0.0436 0.0364  0.0018  6    PHE   A CD1 
71   C  CD2 A PHE   A 6   ? 0.2184 0.2523 0.1995 -0.0396 0.0326  0.0582  6    PHE   A CD2 
72   C  CD2 B PHE   A 6   ? 0.2294 0.2583 0.2079 -0.0416 0.0344  0.0012  6    PHE   A CD2 
73   C  CE1 A PHE   A 6   ? 0.2099 0.2416 0.1776 -0.0441 0.0235  0.0603  6    PHE   A CE1 
74   C  CE1 B PHE   A 6   ? 0.2187 0.2496 0.1859 -0.0453 0.0396  0.0011  6    PHE   A CE1 
75   C  CE2 A PHE   A 6   ? 0.2186 0.2492 0.2055 -0.0358 0.0290  0.0526  6    PHE   A CE2 
76   C  CE2 B PHE   A 6   ? 0.2246 0.2499 0.2035 -0.0430 0.0358  -0.0013 6    PHE   A CE2 
77   C  CZ  A PHE   A 6   ? 0.2149 0.2435 0.1933 -0.0407 0.0237  0.0516  6    PHE   A CZ  
78   C  CZ  B PHE   A 6   ? 0.2203 0.2468 0.1892 -0.0455 0.0392  -0.0005 6    PHE   A CZ  
97   N  N   A SER   A 7   ? 0.2219 0.2791 0.2191 -0.0708 0.0730  0.0064  7    SER   A N   
98   N  N   B SER   A 7   ? 0.2626 0.2867 0.2175 -0.0571 0.0656  0.0172  7    SER   A N   
99   C  CA  A SER   A 7   ? 0.2225 0.2707 0.2192 -0.0654 0.0756  -0.0140 7    SER   A CA  
100  C  CA  B SER   A 7   ? 0.2636 0.2792 0.2252 -0.0526 0.0579  0.0040  7    SER   A CA  
101  C  C   A SER   A 7   ? 0.2069 0.2414 0.2003 -0.0660 0.0842  -0.0133 7    SER   A C   
102  C  C   B SER   A 7   ? 0.2498 0.2660 0.2131 -0.0485 0.0571  -0.0004 7    SER   A C   
103  O  O   A SER   A 7   ? 0.2144 0.2311 0.1998 -0.0719 0.0829  -0.0104 7    SER   A O   
104  O  O   B SER   A 7   ? 0.2549 0.2663 0.2169 -0.0482 0.0515  0.0037  7    SER   A O   
105  C  CB  A SER   A 7   ? 0.2415 0.2903 0.2456 -0.0567 0.0687  -0.0232 7    SER   A CB  
106  C  CB  B SER   A 7   ? 0.2746 0.2828 0.2435 -0.0560 0.0535  -0.0004 7    SER   A CB  
107  O  OG  A SER   A 7   ? 0.2556 0.3015 0.2733 -0.0526 0.0626  -0.0230 7    SER   A OG  
108  O  OG  B SER   A 7   ? 0.2835 0.2863 0.2630 -0.0548 0.0490  -0.0002 7    SER   A OG  
119  N  N   A GLY   A 8   ? 0.1924 0.2238 0.1975 -0.0592 0.0713  -0.0242 8    GLY   A N   
120  N  N   B GLY   A 8   ? 0.2359 0.2561 0.1985 -0.0415 0.0575  -0.0070 8    GLY   A N   
121  C  CA  A GLY   A 8   ? 0.1839 0.2094 0.1972 -0.0422 0.0636  -0.0192 8    GLY   A CA  
122  C  CA  B GLY   A 8   ? 0.2209 0.2424 0.1826 -0.0347 0.0554  -0.0074 8    GLY   A CA  
123  C  C   A GLY   A 8   ? 0.1715 0.1944 0.1878 -0.0310 0.0518  -0.0128 8    GLY   A C   
124  C  C   B GLY   A 8   ? 0.2050 0.2286 0.1647 -0.0288 0.0518  -0.0079 8    GLY   A C   
125  O  O   A GLY   A 8   ? 0.1760 0.1981 0.2044 -0.0195 0.0449  -0.0378 8    GLY   A O   
126  O  O   B GLY   A 8   ? 0.2065 0.2352 0.1724 -0.0217 0.0577  -0.0207 8    GLY   A O   
133  N  N   A TYR   A 9   ? 0.1546 0.1804 0.1667 -0.0261 0.0369  0.0053  9    TYR   A N   
134  N  N   B TYR   A 9   ? 0.1881 0.2091 0.1568 -0.0265 0.0374  0.0027  9    TYR   A N   
135  C  CA  A TYR   A 9   ? 0.1478 0.1575 0.1577 -0.0292 0.0299  0.0063  9    TYR   A CA  
136  C  CA  B TYR   A 9   ? 0.1747 0.1890 0.1514 -0.0193 0.0265  0.0103  9    TYR   A CA  
137  C  C   A TYR   A 9   ? 0.1569 0.1439 0.1525 -0.0286 0.0318  0.0266  9    TYR   A C   
138  C  C   B TYR   A 9   ? 0.1708 0.1731 0.1410 -0.0156 0.0257  0.0207  9    TYR   A C   
139  O  O   A TYR   A 9   ? 0.1883 0.1634 0.1619 -0.0373 0.0323  0.0208  9    TYR   A O   
140  O  O   B TYR   A 9   ? 0.1856 0.1872 0.1531 -0.0182 0.0215  0.0225  9    TYR   A O   
141  C  CB  A TYR   A 9   ? 0.1387 0.1606 0.1618 -0.0168 0.0263  -0.0006 9    TYR   A CB  
142  C  CB  B TYR   A 9   ? 0.1663 0.1859 0.1618 -0.0181 0.0126  -0.0003 9    TYR   A CB  
143  C  CG  A TYR   A 9   ? 0.1386 0.1608 0.1656 -0.0123 0.0424  -0.0139 9    TYR   A CG  
144  C  CG  B TYR   A 9   ? 0.1581 0.1818 0.1562 -0.0163 0.0129  -0.0109 9    TYR   A CG  
145  C  CD1 A TYR   A 9   ? 0.1410 0.1632 0.1793 -0.0159 0.0558  -0.0210 9    TYR   A CD1 
146  C  CD1 B TYR   A 9   ? 0.1579 0.1812 0.1595 -0.0177 0.0174  -0.0183 9    TYR   A CD1 
147  C  CD2 A TYR   A 9   ? 0.1371 0.1544 0.1735 -0.0110 0.0396  -0.0041 9    TYR   A CD2 
148  C  CD2 B TYR   A 9   ? 0.1529 0.1774 0.1483 -0.0134 0.0063  -0.0101 9    TYR   A CD2 
149  C  CE1 A TYR   A 9   ? 0.1469 0.1642 0.1887 -0.0169 0.0602  -0.0352 9    TYR   A CE1 
150  C  CE1 B TYR   A 9   ? 0.1593 0.1755 0.1626 -0.0174 0.0207  -0.0187 9    TYR   A CE1 
151  C  CE2 A TYR   A 9   ? 0.1397 0.1582 0.1830 -0.0108 0.0521  -0.0186 9    TYR   A CE2 
152  C  CE2 B TYR   A 9   ? 0.1522 0.1771 0.1539 -0.0095 0.0134  -0.0151 9    TYR   A CE2 
153  C  CZ  A TYR   A 9   ? 0.1451 0.1646 0.1965 -0.0256 0.0639  -0.0286 9    TYR   A CZ  
154  C  CZ  B TYR   A 9   ? 0.1561 0.1726 0.1651 -0.0114 0.0256  -0.0173 9    TYR   A CZ  
155  O  OH  A TYR   A 9   ? 0.1545 0.1726 0.2150 -0.0429 0.0710  -0.0391 9    TYR   A OH  
156  O  OH  B TYR   A 9   ? 0.1623 0.1760 0.1837 -0.0119 0.0315  -0.0163 9    TYR   A OH  
175  N  N   A LEU   A 10  ? 0.1417 0.1305 0.1531 -0.0202 0.0260  0.0213  10   LEU   A N   
176  N  N   B LEU   A 10  ? 0.1572 0.1568 0.1426 -0.0123 0.0263  0.0227  10   LEU   A N   
177  C  CA  A LEU   A 10  ? 0.1263 0.1286 0.1560 -0.0198 0.0256  0.0266  10   LEU   A CA  
178  C  CA  B LEU   A 10  ? 0.1453 0.1493 0.1476 -0.0092 0.0258  0.0217  10   LEU   A CA  
179  C  C   A LEU   A 10  ? 0.1220 0.1271 0.1574 -0.0180 0.0243  0.0233  10   LEU   A C   
180  C  C   B LEU   A 10  ? 0.1422 0.1398 0.1282 -0.0131 0.0172  0.0266  10   LEU   A C   
181  O  O   A LEU   A 10  ? 0.1283 0.1240 0.1641 -0.0185 0.0368  0.0214  10   LEU   A O   
182  O  O   B LEU   A 10  ? 0.1461 0.1399 0.1193 -0.0143 0.0271  0.0289  10   LEU   A O   
183  C  CB  A LEU   A 10  ? 0.1356 0.1378 0.1923 -0.0141 0.0105  0.0290  10   LEU   A CB  
184  C  CB  B LEU   A 10  ? 0.1460 0.1483 0.1720 -0.0138 0.0179  0.0220  10   LEU   A CB  
185  C  CG  A LEU   A 10  ? 0.1546 0.1502 0.2366 -0.0101 0.0025  0.0284  10   LEU   A CG  
186  C  CG  B LEU   A 10  ? 0.1551 0.1580 0.2101 -0.0073 0.0050  0.0098  10   LEU   A CG  
187  C  CD1 A LEU   A 10  ? 0.1653 0.1587 0.2629 -0.0148 0.0142  0.0239  10   LEU   A CD1 
188  C  CD1 B LEU   A 10  ? 0.1583 0.1648 0.2384 -0.0131 -0.0008 0.0047  10   LEU   A CD1 
189  C  CD2 A LEU   A 10  ? 0.1658 0.1619 0.2549 0.0041  0.0064  0.0101  10   LEU   A CD2 
190  C  CD2 B LEU   A 10  ? 0.1745 0.1714 0.2366 0.0011  -0.0083 0.0013  10   LEU   A CD2 
213  N  N   A LYS   A 11  ? 0.1293 0.1294 0.1597 -0.0168 0.0280  0.0231  11   LYS   A N   
214  N  N   B LYS   A 11  ? 0.1479 0.1341 0.1405 -0.0185 0.0139  0.0213  11   LYS   A N   
215  C  CA  A LYS   A 11  ? 0.1271 0.1279 0.1635 -0.0262 0.0284  0.0212  11   LYS   A CA  
216  C  CA  B LYS   A 11  ? 0.1481 0.1297 0.1477 -0.0233 0.0142  0.0210  11   LYS   A CA  
217  C  C   A LYS   A 11  ? 0.1236 0.1309 0.1629 -0.0236 0.0249  0.0133  11   LYS   A C   
218  C  C   B LYS   A 11  ? 0.1335 0.1205 0.1486 -0.0272 0.0059  0.0111  11   LYS   A C   
219  O  O   A LYS   A 11  ? 0.1340 0.1556 0.1881 -0.0425 0.0341  -0.0005 11   LYS   A O   
220  O  O   B LYS   A 11  ? 0.1258 0.1227 0.1760 -0.0275 0.0097  -0.0067 11   LYS   A O   
221  C  CB  A LYS   A 11  ? 0.1350 0.1284 0.1607 -0.0262 0.0218  0.0164  11   LYS   A CB  
222  C  CB  B LYS   A 11  ? 0.1631 0.1253 0.1519 -0.0227 0.0099  0.0213  11   LYS   A CB  
223  C  CG  A LYS   A 11  ? 0.1490 0.1236 0.1630 -0.0221 0.0253  0.0238  11   LYS   A CG  
224  C  CG  B LYS   A 11  ? 0.1763 0.1242 0.1393 -0.0231 0.0051  0.0187  11   LYS   A CG  
225  C  CD  A LYS   A 11  ? 0.1662 0.1286 0.1793 -0.0184 0.0192  0.0247  11   LYS   A CD  
226  C  CD  B LYS   A 11  ? 0.1854 0.1303 0.1356 -0.0211 0.0065  0.0240  11   LYS   A CD  
227  C  CE  A LYS   A 11  ? 0.1765 0.1257 0.1832 -0.0196 0.0154  0.0285  11   LYS   A CE  
228  C  CE  B LYS   A 11  ? 0.1932 0.1306 0.1309 -0.0176 0.0091  0.0373  11   LYS   A CE  
229  N  NZ  A LYS   A 11  ? 0.1701 0.1266 0.1728 -0.0129 0.0022  0.0121  11   LYS   A NZ  
230  N  NZ  B LYS   A 11  ? 0.1911 0.1385 0.1317 -0.0070 0.0027  0.0448  11   LYS   A NZ  
257  N  N   A LEU   A 12  ? 0.1208 0.1216 0.1435 -0.0272 0.0229  0.0032  12   LEU   A N   
258  N  N   B LEU   A 12  ? 0.1328 0.1270 0.1461 -0.0153 0.0004  0.0037  12   LEU   A N   
259  C  CA  A LEU   A 12  ? 0.1271 0.1301 0.1540 -0.0264 0.0155  0.0111  12   LEU   A CA  
260  C  CA  B LEU   A 12  ? 0.1285 0.1393 0.1517 -0.0087 -0.0016 0.0036  12   LEU   A CA  
261  C  C   A LEU   A 12  ? 0.1322 0.1284 0.1560 -0.0306 0.0112  0.0116  12   LEU   A C   
262  C  C   B LEU   A 12  ? 0.1279 0.1380 0.1387 -0.0073 0.0086  0.0128  12   LEU   A C   
263  O  O   A LEU   A 12  ? 0.1375 0.1293 0.1607 -0.0285 0.0144  -0.0023 12   LEU   A O   
264  O  O   B LEU   A 12  ? 0.1323 0.1348 0.1366 -0.0021 0.0065  0.0073  12   LEU   A O   
265  C  CB  A LEU   A 12  ? 0.1309 0.1282 0.1543 -0.0205 0.0056  0.0211  12   LEU   A CB  
266  C  CB  B LEU   A 12  ? 0.1325 0.1481 0.1637 -0.0022 -0.0077 0.0021  12   LEU   A CB  
267  C  CG  A LEU   A 12  ? 0.1478 0.1393 0.1761 -0.0074 0.0137  0.0224  12   LEU   A CG  
268  C  CG  B LEU   A 12  ? 0.1368 0.1524 0.1748 0.0028  -0.0046 0.0041  12   LEU   A CG  
269  C  CD1 A LEU   A 12  ? 0.1610 0.1454 0.1876 0.0045  0.0261  0.0404  12   LEU   A CD1 
270  C  CD1 B LEU   A 12  ? 0.1459 0.1562 0.1771 0.0037  0.0007  0.0022  12   LEU   A CD1 
271  C  CD2 A LEU   A 12  ? 0.1542 0.1458 0.1989 -0.0047 0.0011  0.0143  12   LEU   A CD2 
272  C  CD2 B LEU   A 12  ? 0.1410 0.1568 0.1940 0.0052  -0.0112 -0.0074 12   LEU   A CD2 
295  N  N   A THR   A 13  ? 0.1267 0.1280 0.1603 -0.0258 0.0139  -0.0008 13   THR   A N   
296  N  N   B THR   A 13  ? 0.1214 0.1303 0.1336 -0.0075 0.0151  0.0172  13   THR   A N   
297  C  CA  A THR   A 13  ? 0.1344 0.1295 0.1719 -0.0188 0.0233  0.0032  13   THR   A CA  
298  C  CA  B THR   A 13  ? 0.1234 0.1280 0.1509 -0.0149 0.0127  0.0219  13   THR   A CA  
299  C  C   A THR   A 13  ? 0.1369 0.1281 0.1812 -0.0236 0.0258  0.0158  13   THR   A C   
300  C  C   B THR   A 13  ? 0.1266 0.1368 0.1619 -0.0154 0.0040  0.0366  13   THR   A C   
301  O  O   A THR   A 13  ? 0.1387 0.1357 0.1845 -0.0171 0.0309  0.0158  13   THR   A O   
302  O  O   B THR   A 13  ? 0.1271 0.1401 0.1552 -0.0146 -0.0089 0.0468  13   THR   A O   
303  C  CB  A THR   A 13  ? 0.1406 0.1336 0.1756 -0.0148 0.0285  0.0108  13   THR   A CB  
304  C  CB  B THR   A 13  ? 0.1219 0.1290 0.1601 -0.0085 0.0200  0.0163  13   THR   A CB  
305  O  OG1 A THR   A 13  ? 0.1470 0.1272 0.1827 -0.0157 0.0172  0.0060  13   THR   A OG1 
306  O  OG1 B THR   A 13  ? 0.1099 0.1372 0.1509 -0.0096 0.0317  0.0235  13   THR   A OG1 
307  C  CG2 A THR   A 13  ? 0.1520 0.1435 0.2031 -0.0045 0.0329  0.0009  13   THR   A CG2 
308  C  CG2 B THR   A 13  ? 0.1273 0.1328 0.1646 -0.0062 0.0238  0.0034  13   THR   A CG2 
323  N  N   A ASP   A 14  ? 0.1434 0.1286 0.1993 -0.0235 0.0153  0.0316  14   ASP   A N   
324  N  N   B ASP   A 14  ? 0.1331 0.1429 0.1796 -0.0156 0.0077  0.0420  14   ASP   A N   
325  C  CA  A ASP   A 14  ? 0.1471 0.1379 0.2139 -0.0223 0.0071  0.0458  14   ASP   A CA  
326  C  CA  B ASP   A 14  ? 0.1370 0.1524 0.1890 -0.0157 0.0052  0.0529  14   ASP   A CA  
327  C  C   A ASP   A 14  ? 0.1396 0.1357 0.1979 -0.0174 0.0098  0.0440  14   ASP   A C   
328  C  C   B ASP   A 14  ? 0.1318 0.1474 0.1806 -0.0052 -0.0105 0.0586  14   ASP   A C   
329  O  O   A ASP   A 14  ? 0.1425 0.1423 0.2011 -0.0206 -0.0071 0.0577  14   ASP   A O   
330  O  O   B ASP   A 14  ? 0.1342 0.1458 0.1736 -0.0044 -0.0299 0.0691  14   ASP   A O   
331  C  CB  A ASP   A 14  ? 0.1668 0.1548 0.2519 -0.0206 -0.0096 0.0597  14   ASP   A CB  
332  C  CB  B ASP   A 14  ? 0.1495 0.1651 0.2167 -0.0260 0.0127  0.0542  14   ASP   A CB  
333  C  CG  A ASP   A 14  ? 0.1843 0.1829 0.3170 -0.0230 -0.0254 0.0480  14   ASP   A CG  
334  C  CG  B ASP   A 14  ? 0.1584 0.1842 0.2630 -0.0330 0.0037  0.0386  14   ASP   A CG  
335  O  OD1 A ASP   A 14  ? 0.1933 0.1966 0.3339 -0.0124 -0.0424 0.0524  14   ASP   A OD1 
336  O  OD1 B ASP   A 14  ? 0.1635 0.1872 0.2744 -0.0382 -0.0041 0.0351  14   ASP   A OD1 
337  O  OD2 A ASP   A 14  ? 0.1963 0.1962 0.3565 -0.0322 -0.0299 0.0299  14   ASP   A OD2 
338  O  OD2 B ASP   A 14  ? 0.1662 0.1971 0.2897 -0.0261 -0.0036 0.0257  14   ASP   A OD2 
347  N  N   A ASN   A 15  ? 0.1312 0.1199 0.1733 -0.0209 0.0247  0.0293  15   ASN   A N   
348  N  N   B ASN   A 15  ? 0.1220 0.1399 0.1813 -0.0000 -0.0090 0.0577  15   ASN   A N   
349  C  CA  A ASN   A 15  ? 0.1282 0.1287 0.1659 -0.0220 0.0193  0.0104  15   ASN   A CA  
350  C  CA  B ASN   A 15  ? 0.1180 0.1401 0.1653 0.0018  -0.0046 0.0385  15   ASN   A CA  
351  C  C   A ASN   A 15  ? 0.1287 0.1267 0.1692 -0.0188 0.0288  0.0034  15   ASN   A C   
352  C  C   B ASN   A 15  ? 0.1139 0.1320 0.1452 -0.0042 0.0066  0.0275  15   ASN   A C   
353  O  O   A ASN   A 15  ? 0.1299 0.1329 0.1862 -0.0114 0.0175  0.0002  15   ASN   A O   
354  O  O   B ASN   A 15  ? 0.1129 0.1357 0.1313 -0.0018 0.0018  0.0200  15   ASN   A O   
355  C  CB  A ASN   A 15  ? 0.1229 0.1310 0.1577 -0.0217 0.0161  0.0118  15   ASN   A CB  
356  C  CB  B ASN   A 15  ? 0.1237 0.1488 0.1657 0.0052  -0.0083 0.0373  15   ASN   A CB  
357  C  CG  A ASN   A 15  ? 0.1204 0.1414 0.1664 -0.0164 0.0195  0.0206  15   ASN   A CG  
358  C  CG  B ASN   A 15  ? 0.1292 0.1605 0.1505 0.0063  -0.0000 0.0342  15   ASN   A CG  
359  O  OD1 A ASN   A 15  ? 0.1260 0.1424 0.1758 -0.0272 0.0278  0.0018  15   ASN   A OD1 
360  O  OD1 B ASN   A 15  ? 0.1320 0.1600 0.1601 0.0017  0.0187  0.0237  15   ASN   A OD1 
361  N  ND2 A ASN   A 15  ? 0.1206 0.1510 0.1612 -0.0182 0.0149  0.0365  15   ASN   A ND2 
362  N  ND2 B ASN   A 15  ? 0.1391 0.1736 0.1449 -0.0029 -0.0037 0.0380  15   ASN   A ND2 
375  N  N   A VAL   A 16  ? 0.1314 0.1211 0.1593 -0.0134 0.0183  0.0135  16   VAL   A N   
376  N  N   B VAL   A 16  ? 0.1186 0.1241 0.1440 -0.0064 0.0004  0.0293  16   VAL   A N   
377  C  CA  A VAL   A 16  ? 0.1291 0.1196 0.1528 -0.0148 0.0142  0.0065  16   VAL   A CA  
378  C  CA  B VAL   A 16  ? 0.1200 0.1213 0.1302 -0.0086 0.0014  0.0284  16   VAL   A CA  
379  C  C   A VAL   A 16  ? 0.1206 0.1170 0.1471 -0.0163 0.0099  0.0117  16   VAL   A C   
380  C  C   B VAL   A 16  ? 0.1228 0.1296 0.1246 -0.0109 0.0056  0.0272  16   VAL   A C   
381  O  O   A VAL   A 16  ? 0.1141 0.1142 0.1456 -0.0242 0.0124  0.0065  16   VAL   A O   
382  O  O   B VAL   A 16  ? 0.1264 0.1330 0.1343 -0.0087 0.0077  0.0209  16   VAL   A O   
383  C  CB  A VAL   A 16  ? 0.1455 0.1340 0.1534 -0.0061 0.0246  0.0043  16   VAL   A CB  
384  C  CB  B VAL   A 16  ? 0.1297 0.1168 0.1212 0.0002  0.0024  0.0237  16   VAL   A CB  
385  C  CG1 A VAL   A 16  ? 0.1544 0.1384 0.1588 -0.0059 0.0110  0.0010  16   VAL   A CG1 
386  C  CG1 B VAL   A 16  ? 0.1397 0.1123 0.1189 0.0015  0.0019  0.0183  16   VAL   A CG1 
387  C  CG2 A VAL   A 16  ? 0.1525 0.1485 0.1500 -0.0064 0.0416  -0.0000 16   VAL   A CG2 
388  C  CG2 B VAL   A 16  ? 0.1355 0.1335 0.1371 0.0132  0.0147  0.0277  16   VAL   A CG2 
407  N  N   A TYR   A 17  ? 0.1223 0.1129 0.1411 -0.0137 0.0220  0.0090  17   TYR   A N   
408  N  N   B TYR   A 17  ? 0.1209 0.1213 0.1228 -0.0114 0.0089  0.0227  17   TYR   A N   
409  C  CA  A TYR   A 17  ? 0.1239 0.1229 0.1323 -0.0112 0.0239  0.0103  17   TYR   A CA  
410  C  CA  B TYR   A 17  ? 0.1213 0.1237 0.1183 -0.0135 0.0043  0.0248  17   TYR   A CA  
411  C  C   A TYR   A 17  ? 0.1271 0.1161 0.1437 -0.0130 0.0241  0.0069  17   TYR   A C   
412  C  C   B TYR   A 17  ? 0.1200 0.1285 0.1198 -0.0125 0.0091  0.0230  17   TYR   A C   
413  O  O   A TYR   A 17  ? 0.1271 0.1116 0.1543 -0.0106 0.0220  0.0124  17   TYR   A O   
414  O  O   B TYR   A 17  ? 0.1158 0.1301 0.1130 -0.0199 0.0081  0.0217  17   TYR   A O   
415  C  CB  A TYR   A 17  ? 0.1369 0.1306 0.1278 -0.0063 0.0215  0.0104  17   TYR   A CB  
416  C  CB  B TYR   A 17  ? 0.1423 0.1223 0.1287 -0.0174 0.0030  0.0273  17   TYR   A CB  
417  C  CG  A TYR   A 17  ? 0.1501 0.1411 0.1334 -0.0138 0.0132  0.0082  17   TYR   A CG  
418  C  CG  B TYR   A 17  ? 0.1615 0.1280 0.1271 -0.0191 -0.0019 0.0229  17   TYR   A CG  
419  C  CD1 A TYR   A 17  ? 0.1614 0.1402 0.1468 -0.0091 0.0041  -0.0038 17   TYR   A CD1 
420  C  CD1 B TYR   A 17  ? 0.1719 0.1278 0.1243 -0.0117 -0.0049 0.0268  17   TYR   A CD1 
421  C  CD2 A TYR   A 17  ? 0.1573 0.1517 0.1433 -0.0200 0.0235  0.0187  17   TYR   A CD2 
422  C  CD2 B TYR   A 17  ? 0.1763 0.1376 0.1340 -0.0282 0.0028  0.0199  17   TYR   A CD2 
423  C  CE1 A TYR   A 17  ? 0.1683 0.1392 0.1594 -0.0134 -0.0021 -0.0061 17   TYR   A CE1 
424  C  CE1 B TYR   A 17  ? 0.1821 0.1357 0.1365 -0.0113 -0.0119 0.0332  17   TYR   A CE1 
425  C  CE2 A TYR   A 17  ? 0.1697 0.1510 0.1565 -0.0228 0.0155  0.0075  17   TYR   A CE2 
426  C  CE2 B TYR   A 17  ? 0.1899 0.1422 0.1386 -0.0275 -0.0041 0.0218  17   TYR   A CE2 
427  C  CZ  A TYR   A 17  ? 0.1755 0.1435 0.1668 -0.0188 0.0004  0.0071  17   TYR   A CZ  
428  C  CZ  B TYR   A 17  ? 0.1935 0.1384 0.1360 -0.0183 -0.0141 0.0358  17   TYR   A CZ  
429  O  OH  A TYR   A 17  ? 0.1890 0.1501 0.1842 -0.0213 0.0014  0.0069  17   TYR   A OH  
430  O  OH  B TYR   A 17  ? 0.2109 0.1424 0.1498 -0.0129 -0.0182 0.0485  17   TYR   A OH  
449  N  N   A ILE   A 18  ? 0.1318 0.1138 0.1390 -0.0177 0.0255  0.0144  18   ILE   A N   
450  N  N   B ILE   A 18  ? 0.1204 0.1274 0.1287 -0.0111 0.0149  0.0221  18   ILE   A N   
451  C  CA  A ILE   A 18  ? 0.1384 0.1165 0.1483 -0.0125 0.0282  0.0071  18   ILE   A CA  
452  C  CA  B ILE   A 18  ? 0.1226 0.1259 0.1199 -0.0093 0.0229  0.0197  18   ILE   A CA  
453  C  C   A ILE   A 18  ? 0.1393 0.1208 0.1680 -0.0181 0.0269  0.0071  18   ILE   A C   
454  C  C   B ILE   A 18  ? 0.1207 0.1365 0.1136 -0.0116 0.0173  0.0155  18   ILE   A C   
455  O  O   A ILE   A 18  ? 0.1320 0.1335 0.1770 -0.0182 0.0350  0.0179  18   ILE   A O   
456  O  O   B ILE   A 18  ? 0.1170 0.1440 0.1189 -0.0095 0.0213  0.0168  18   ILE   A O   
457  C  CB  A ILE   A 18  ? 0.1461 0.1269 0.1381 0.0019  0.0215  0.0148  18   ILE   A CB  
458  C  CB  B ILE   A 18  ? 0.1290 0.1229 0.1046 -0.0025 0.0203  0.0194  18   ILE   A CB  
459  C  CG1 A ILE   A 18  ? 0.1485 0.1292 0.1341 0.0143  0.0040  0.0183  18   ILE   A CG1 
460  C  CG1 B ILE   A 18  ? 0.1416 0.1267 0.1083 -0.0062 0.0293  0.0142  18   ILE   A CG1 
461  C  CG2 A ILE   A 18  ? 0.1499 0.1305 0.1507 0.0022  0.0220  0.0075  18   ILE   A CG2 
462  C  CG2 B ILE   A 18  ? 0.1334 0.1322 0.0978 -0.0037 0.0110  0.0233  18   ILE   A CG2 
463  C  CD1 A ILE   A 18  ? 0.1701 0.1404 0.1644 0.0191  0.0046  0.0116  18   ILE   A CD1 
464  C  CD1 B ILE   A 18  ? 0.1589 0.1381 0.1300 -0.0085 0.0239  0.0035  18   ILE   A CD1 
487  N  N   A LYS   A 19  ? 0.1471 0.1248 0.1665 -0.0171 0.0346  0.0113  19   LYS   A N   
488  N  N   B LYS   A 19  ? 0.1228 0.1368 0.1193 -0.0184 0.0218  0.0131  19   LYS   A N   
489  C  CA  A LYS   A 19  ? 0.1555 0.1386 0.1938 -0.0105 0.0408  0.0131  19   LYS   A CA  
490  C  CA  B LYS   A 19  ? 0.1333 0.1435 0.1238 -0.0154 0.0289  0.0147  19   LYS   A CA  
491  C  C   A LYS   A 19  ? 0.1471 0.1364 0.2221 -0.0030 0.0450  0.0294  19   LYS   A C   
492  C  C   B LYS   A 19  ? 0.1401 0.1479 0.1423 -0.0040 0.0314  0.0165  19   LYS   A C   
493  O  O   A LYS   A 19  ? 0.1413 0.1317 0.2374 0.0030  0.0347  0.0369  19   LYS   A O   
494  O  O   B LYS   A 19  ? 0.1437 0.1452 0.1445 -0.0051 0.0312  0.0124  19   LYS   A O   
495  C  CB  A LYS   A 19  ? 0.1720 0.1547 0.2070 -0.0172 0.0386  -0.0036 19   LYS   A CB  
496  C  CB  B LYS   A 19  ? 0.1404 0.1551 0.1315 -0.0110 0.0286  0.0051  19   LYS   A CB  
497  C  CG  A LYS   A 19  ? 0.1992 0.1670 0.2126 -0.0209 0.0351  -0.0227 19   LYS   A CG  
498  C  CG  B LYS   A 19  ? 0.1625 0.1706 0.1416 -0.0079 0.0276  -0.0001 19   LYS   A CG  
499  C  CD  A LYS   A 19  ? 0.2202 0.1849 0.2205 -0.0231 0.0340  -0.0311 19   LYS   A CD  
500  C  CD  B LYS   A 19  ? 0.1787 0.1798 0.1437 -0.0150 0.0364  -0.0014 19   LYS   A CD  
501  C  CE  A LYS   A 19  ? 0.2375 0.1934 0.2213 -0.0276 0.0383  -0.0365 19   LYS   A CE  
502  C  CE  B LYS   A 19  ? 0.1902 0.1929 0.1531 -0.0200 0.0322  -0.0109 19   LYS   A CE  
503  N  NZ  A LYS   A 19  ? 0.2478 0.2018 0.2125 -0.0323 0.0438  -0.0432 19   LYS   A NZ  
504  N  NZ  B LYS   A 19  ? 0.2010 0.1997 0.1536 -0.0245 0.0398  -0.0202 19   LYS   A NZ  
531  N  N   A ASN   A 20  ? 0.1530 0.1380 0.2439 0.0004  0.0498  0.0409  20   ASN   A N   
532  N  N   B ASN   A 20  ? 0.1498 0.1575 0.1724 0.0067  0.0386  0.0200  20   ASN   A N   
533  C  CA  A ASN   A 20  ? 0.1704 0.1543 0.2714 0.0166  0.0680  0.0441  20   ASN   A CA  
534  C  CA  B ASN   A 20  ? 0.1625 0.1713 0.2086 0.0143  0.0402  0.0218  20   ASN   A CA  
535  C  C   A ASN   A 20  ? 0.1857 0.1533 0.2724 0.0165  0.0739  0.0362  20   ASN   A C   
536  C  C   B ASN   A 20  ? 0.1795 0.1702 0.2176 0.0111  0.0479  0.0195  20   ASN   A C   
537  O  O   A ASN   A 20  ? 0.2043 0.1542 0.2783 0.0038  0.0785  0.0275  20   ASN   A O   
538  O  O   B ASN   A 20  ? 0.1948 0.1741 0.2395 0.0057  0.0523  0.0144  20   ASN   A O   
539  C  CB  A ASN   A 20  ? 0.1748 0.1658 0.2968 0.0277  0.0732  0.0609  20   ASN   A CB  
540  C  CB  B ASN   A 20  ? 0.1599 0.1830 0.2291 0.0289  0.0376  0.0243  20   ASN   A CB  
541  C  CG  A ASN   A 20  ? 0.1863 0.1703 0.3337 0.0321  0.0721  0.0688  20   ASN   A CG  
542  C  CG  B ASN   A 20  ? 0.1643 0.1918 0.2558 0.0364  0.0371  0.0291  20   ASN   A CG  
543  O  OD1 A ASN   A 20  ? 0.2075 0.1784 0.3561 0.0312  0.0709  0.0587  20   ASN   A OD1 
544  O  OD1 B ASN   A 20  ? 0.1608 0.1909 0.2639 0.0422  0.0384  0.0238  20   ASN   A OD1 
545  N  ND2 A ASN   A 20  ? 0.1881 0.1665 0.3422 0.0366  0.0623  0.0821  20   ASN   A ND2 
546  N  ND2 B ASN   A 20  ? 0.1761 0.1942 0.2700 0.0324  0.0357  0.0389  20   ASN   A ND2 
559  N  N   A ALA   A 21  ? 0.1891 0.1621 0.2748 0.0161  0.0607  0.0259  21   ALA   A N   
560  N  N   B ALA   A 21  ? 0.1876 0.1699 0.2119 0.0107  0.0385  0.0196  21   ALA   A N   
561  C  CA  A ALA   A 21  ? 0.1886 0.1597 0.2668 0.0152  0.0506  0.0230  21   ALA   A CA  
562  C  CA  B ALA   A 21  ? 0.1933 0.1680 0.2079 0.0060  0.0349  0.0246  21   ALA   A CA  
563  C  C   A ALA   A 21  ? 0.1776 0.1635 0.2615 0.0091  0.0454  0.0339  21   ALA   A C   
564  C  C   B ALA   A 21  ? 0.1849 0.1605 0.1921 0.0076  0.0373  0.0264  21   ALA   A C   
565  O  O   A ALA   A 21  ? 0.1682 0.1626 0.2592 0.0130  0.0387  0.0380  21   ALA   A O   
566  O  O   B ALA   A 21  ? 0.1896 0.1535 0.1891 0.0144  0.0382  0.0147  21   ALA   A O   
567  C  CB  A ALA   A 21  ? 0.2001 0.1628 0.2761 0.0103  0.0382  0.0236  21   ALA   A CB  
568  C  CB  B ALA   A 21  ? 0.2054 0.1689 0.2284 0.0026  0.0269  0.0234  21   ALA   A CB  
579  N  N   A ASP   A 22  ? 0.1764 0.1663 0.2631 -0.0011 0.0456  0.0305  22   ASP   A N   
580  N  N   B ASP   A 22  ? 0.1737 0.1575 0.1871 -0.0021 0.0361  0.0319  22   ASP   A N   
581  C  CA  A ASP   A 22  ? 0.1788 0.1718 0.2548 -0.0039 0.0417  0.0231  22   ASP   A CA  
582  C  CA  B ASP   A 22  ? 0.1675 0.1584 0.1807 -0.0034 0.0282  0.0290  22   ASP   A CA  
583  C  C   A ASP   A 22  ? 0.1708 0.1682 0.2239 -0.0054 0.0396  0.0220  22   ASP   A C   
584  C  C   B ASP   A 22  ? 0.1568 0.1560 0.1584 -0.0065 0.0288  0.0224  22   ASP   A C   
585  O  O   A ASP   A 22  ? 0.1745 0.1717 0.2310 -0.0084 0.0437  0.0215  22   ASP   A O   
586  O  O   B ASP   A 22  ? 0.1520 0.1568 0.1570 -0.0085 0.0343  0.0155  22   ASP   A O   
587  C  CB  A ASP   A 22  ? 0.1948 0.1816 0.2929 -0.0043 0.0372  0.0113  22   ASP   A CB  
588  C  CB  B ASP   A 22  ? 0.1691 0.1628 0.2124 -0.0021 0.0182  0.0207  22   ASP   A CB  
589  C  CG  A ASP   A 22  ? 0.2068 0.1895 0.3274 -0.0068 0.0224  0.0105  22   ASP   A CG  
590  C  CG  B ASP   A 22  ? 0.1733 0.1604 0.2247 0.0001  0.0103  0.0256  22   ASP   A CG  
591  O  OD1 A ASP   A 22  ? 0.1990 0.1864 0.3361 -0.0203 0.0111  0.0197  22   ASP   A OD1 
592  O  OD1 B ASP   A 22  ? 0.1753 0.1512 0.2176 0.0036  0.0046  0.0240  22   ASP   A OD1 
593  O  OD2 A ASP   A 22  ? 0.2248 0.1990 0.3523 -0.0012 0.0258  -0.0004 22   ASP   A OD2 
594  O  OD2 B ASP   A 22  ? 0.1760 0.1699 0.2391 0.0011  0.0032  0.0273  22   ASP   A OD2 
603  N  N   A ILE   A 23  ? 0.1679 0.1668 0.1998 -0.0046 0.0413  0.0171  23   ILE   A N   
604  N  N   B ILE   A 23  ? 0.1526 0.1537 0.1452 -0.0025 0.0260  0.0239  23   ILE   A N   
605  C  CA  A ILE   A 23  ? 0.1676 0.1593 0.1800 -0.0023 0.0365  0.0149  23   ILE   A CA  
606  C  CA  B ILE   A 23  ? 0.1451 0.1577 0.1322 -0.0038 0.0188  0.0301  23   ILE   A CA  
607  C  C   A ILE   A 23  ? 0.1671 0.1652 0.1666 -0.0080 0.0456  0.0103  23   ILE   A C   
608  C  C   B ILE   A 23  ? 0.1468 0.1622 0.1328 -0.0084 0.0196  0.0229  23   ILE   A C   
609  O  O   A ILE   A 23  ? 0.1719 0.1712 0.1634 -0.0029 0.0463  0.0093  23   ILE   A O   
610  O  O   B ILE   A 23  ? 0.1494 0.1553 0.1371 -0.0076 0.0134  0.0188  23   ILE   A O   
611  C  CB  A ILE   A 23  ? 0.1746 0.1572 0.1570 0.0061  0.0301  0.0207  23   ILE   A CB  
612  C  CB  B ILE   A 23  ? 0.1418 0.1545 0.1107 -0.0027 0.0152  0.0304  23   ILE   A CB  
613  C  CG1 A ILE   A 23  ? 0.1816 0.1582 0.1517 0.0085  0.0277  0.0133  23   ILE   A CG1 
614  C  CG1 B ILE   A 23  ? 0.1448 0.1565 0.1154 0.0030  0.0009  0.0179  23   ILE   A CG1 
615  C  CG2 A ILE   A 23  ? 0.1720 0.1566 0.1601 0.0064  0.0284  0.0249  23   ILE   A CG2 
616  C  CG2 B ILE   A 23  ? 0.1400 0.1543 0.1144 -0.0015 0.0126  0.0281  23   ILE   A CG2 
617  C  CD1 A ILE   A 23  ? 0.1837 0.1570 0.1487 0.0048  0.0156  0.0070  23   ILE   A CD1 
618  C  CD1 B ILE   A 23  ? 0.1431 0.1564 0.1203 0.0098  -0.0095 0.0123  23   ILE   A CD1 
641  N  N   A VAL   A 24  ? 0.1712 0.1669 0.1749 -0.0156 0.0437  0.0024  24   VAL   A N   
642  N  N   B VAL   A 24  ? 0.1587 0.1744 0.1610 -0.0149 0.0129  0.0171  24   VAL   A N   
643  C  CA  A VAL   A 24  ? 0.1860 0.1782 0.1871 -0.0246 0.0402  -0.0034 24   VAL   A CA  
644  C  CA  B VAL   A 24  ? 0.1742 0.1847 0.1775 -0.0153 0.0173  0.0125  24   VAL   A CA  
645  C  C   A VAL   A 24  ? 0.1947 0.1936 0.1870 -0.0321 0.0385  -0.0074 24   VAL   A C   
646  C  C   B VAL   A 24  ? 0.1831 0.2028 0.1811 -0.0151 0.0346  -0.0027 24   VAL   A C   
647  O  O   A VAL   A 24  ? 0.2061 0.1910 0.1836 -0.0232 0.0314  -0.0077 24   VAL   A O   
648  O  O   B VAL   A 24  ? 0.1879 0.2055 0.1891 -0.0088 0.0313  0.0007  24   VAL   A O   
649  C  CB  A VAL   A 24  ? 0.1909 0.1802 0.2050 -0.0208 0.0472  -0.0028 24   VAL   A CB  
650  C  CB  B VAL   A 24  ? 0.1816 0.1833 0.2012 -0.0132 0.0124  0.0198  24   VAL   A CB  
651  C  CG1 A VAL   A 24  ? 0.1951 0.1854 0.2112 -0.0157 0.0488  -0.0112 24   VAL   A CG1 
652  C  CG1 B VAL   A 24  ? 0.1926 0.1863 0.2163 -0.0120 0.0053  0.0174  24   VAL   A CG1 
653  C  CG2 A VAL   A 24  ? 0.2029 0.1837 0.2178 -0.0145 0.0603  0.0098  24   VAL   A CG2 
654  C  CG2 B VAL   A 24  ? 0.1843 0.1830 0.2063 -0.0105 0.0209  0.0214  24   VAL   A CG2 
673  N  N   A GLU   A 25  ? 0.2001 0.2222 0.1932 -0.0375 0.0510  -0.0247 25   GLU   A N   
674  N  N   B GLU   A 25  ? 0.1874 0.2205 0.1826 -0.0195 0.0551  -0.0213 25   GLU   A N   
675  C  CA  A GLU   A 25  ? 0.2189 0.2510 0.2049 -0.0352 0.0605  -0.0337 25   GLU   A CA  
676  C  CA  B GLU   A 25  ? 0.2016 0.2420 0.1998 -0.0282 0.0633  -0.0244 25   GLU   A CA  
677  C  C   A GLU   A 25  ? 0.2133 0.2534 0.1830 -0.0463 0.0693  -0.0295 25   GLU   A C   
678  C  C   B GLU   A 25  ? 0.1986 0.2527 0.1823 -0.0310 0.0712  -0.0238 25   GLU   A C   
679  O  O   A GLU   A 25  ? 0.2234 0.2590 0.1857 -0.0460 0.0673  -0.0351 25   GLU   A O   
680  O  O   B GLU   A 25  ? 0.2050 0.2578 0.1788 -0.0315 0.0765  -0.0287 25   GLU   A O   
681  C  CB  A GLU   A 25  ? 0.2389 0.2743 0.2483 -0.0275 0.0567  -0.0386 25   GLU   A CB  
682  C  CB  B GLU   A 25  ? 0.2160 0.2514 0.2347 -0.0308 0.0606  -0.0218 25   GLU   A CB  
683  C  CG  A GLU   A 25  ? 0.2585 0.2942 0.2972 -0.0254 0.0372  -0.0404 25   GLU   A CG  
684  C  CG  B GLU   A 25  ? 0.2335 0.2619 0.2785 -0.0330 0.0497  -0.0158 25   GLU   A CG  
685  C  CD  A GLU   A 25  ? 0.2758 0.3120 0.3419 -0.0249 0.0238  -0.0372 25   GLU   A CD  
686  C  CD  B GLU   A 25  ? 0.2471 0.2700 0.3168 -0.0360 0.0378  -0.0086 25   GLU   A CD  
687  O  OE1 A GLU   A 25  ? 0.2849 0.3184 0.3510 -0.0250 0.0082  -0.0407 25   GLU   A OE1 
688  O  OE1 B GLU   A 25  ? 0.2522 0.2726 0.3349 -0.0348 0.0313  -0.0019 25   GLU   A OE1 
689  O  OE2 A GLU   A 25  ? 0.2788 0.3198 0.3682 -0.0231 0.0225  -0.0397 25   GLU   A OE2 
690  O  OE2 B GLU   A 25  ? 0.2552 0.2725 0.3331 -0.0392 0.0342  -0.0077 25   GLU   A OE2 
703  N  N   A GLU   A 26  ? 0.2031 0.2467 0.1814 -0.0604 0.0755  -0.0256 26   GLU   A N   
704  N  N   B GLU   A 26  ? 0.1943 0.2543 0.1760 -0.0338 0.0733  -0.0230 26   GLU   A N   
705  C  CA  A GLU   A 26  ? 0.2108 0.2433 0.1594 -0.0700 0.0766  -0.0161 26   GLU   A CA  
706  C  CA  B GLU   A 26  ? 0.2003 0.2560 0.1708 -0.0331 0.0671  -0.0168 26   GLU   A CA  
707  C  C   A GLU   A 26  ? 0.2077 0.2370 0.1330 -0.0652 0.0618  -0.0148 26   GLU   A C   
708  C  C   B GLU   A 26  ? 0.1984 0.2472 0.1556 -0.0287 0.0627  -0.0067 26   GLU   A C   
709  O  O   A GLU   A 26  ? 0.2170 0.2395 0.1178 -0.0644 0.0634  -0.0158 26   GLU   A O   
710  O  O   B GLU   A 26  ? 0.2029 0.2449 0.1525 -0.0310 0.0671  -0.0079 26   GLU   A O   
711  C  CB  A GLU   A 26  ? 0.2314 0.2408 0.1948 -0.0785 0.0712  -0.0058 26   GLU   A CB  
712  C  CB  B GLU   A 26  ? 0.2132 0.2667 0.1954 -0.0369 0.0448  -0.0178 26   GLU   A CB  
713  C  CG  A GLU   A 26  ? 0.2517 0.2451 0.2523 -0.0790 0.0700  -0.0070 26   GLU   A CG  
714  C  CG  B GLU   A 26  ? 0.2218 0.2753 0.2092 -0.0415 0.0376  -0.0180 26   GLU   A CG  
715  C  CD  A GLU   A 26  ? 0.2616 0.2444 0.2798 -0.0856 0.0883  -0.0034 26   GLU   A CD  
716  C  CD  B GLU   A 26  ? 0.2275 0.2814 0.2140 -0.0513 0.0357  -0.0148 26   GLU   A CD  
717  O  OE1 A GLU   A 26  ? 0.2529 0.2586 0.2807 -0.0730 0.1225  -0.0487 26   GLU   A OE1 
718  O  OE1 B GLU   A 26  ? 0.2309 0.2951 0.2117 -0.0468 0.0338  -0.0272 26   GLU   A OE1 
719  O  OE2 A GLU   A 26  ? 0.2738 0.2454 0.2812 -0.0868 0.0828  0.0161  26   GLU   A OE2 
720  O  OE2 B GLU   A 26  ? 0.2261 0.2764 0.1985 -0.0609 0.0453  -0.0129 26   GLU   A OE2 
733  N  N   A ALA   A 27  ? 0.1928 0.2243 0.1292 -0.0696 0.0504  -0.0093 27   ALA   A N   
734  N  N   B ALA   A 27  ? 0.1928 0.2397 0.1428 -0.0224 0.0503  0.0027  27   ALA   A N   
735  C  CA  A ALA   A 27  ? 0.1973 0.2259 0.1284 -0.0653 0.0443  -0.0037 27   ALA   A CA  
736  C  CA  B ALA   A 27  ? 0.1986 0.2404 0.1364 -0.0130 0.0340  0.0103  27   ALA   A CA  
737  C  C   A ALA   A 27  ? 0.2139 0.2374 0.1332 -0.0725 0.0522  -0.0168 27   ALA   A C   
738  C  C   B ALA   A 27  ? 0.2154 0.2531 0.1519 -0.0099 0.0283  -0.0035 27   ALA   A C   
739  O  O   A ALA   A 27  ? 0.2214 0.2349 0.1424 -0.0761 0.0433  -0.0166 27   ALA   A O   
740  O  O   B ALA   A 27  ? 0.2146 0.2512 0.1560 -0.0074 0.0234  -0.0082 27   ALA   A O   
741  C  CB  A ALA   A 27  ? 0.1903 0.2165 0.1290 -0.0637 0.0353  -0.0034 27   ALA   A CB  
742  C  CB  B ALA   A 27  ? 0.1923 0.2321 0.1274 -0.0138 0.0324  0.0170  27   ALA   A CB  
753  N  N   A LYS   A 28  ? 0.2411 0.2640 0.1579 -0.0619 0.0473  -0.0412 28   LYS   A N   
754  N  N   B LYS   A 28  ? 0.2368 0.2692 0.1705 -0.0052 0.0231  -0.0196 28   LYS   A N   
755  C  CA  A LYS   A 28  ? 0.2708 0.2954 0.1959 -0.0526 0.0451  -0.0543 28   LYS   A CA  
756  C  CA  B LYS   A 28  ? 0.2615 0.2889 0.2026 -0.0010 0.0170  -0.0316 28   LYS   A CA  
757  C  C   A LYS   A 28  ? 0.2852 0.3183 0.1746 -0.0480 0.0661  -0.0446 28   LYS   A C   
758  C  C   B LYS   A 28  ? 0.2814 0.3082 0.1994 -0.0075 0.0286  -0.0295 28   LYS   A C   
759  O  O   A LYS   A 28  ? 0.2865 0.3200 0.1999 -0.0434 0.0490  -0.0391 28   LYS   A O   
760  O  O   B LYS   A 28  ? 0.2878 0.3120 0.2120 -0.0044 0.0235  -0.0314 28   LYS   A O   
761  C  CB  A LYS   A 28  ? 0.2829 0.3088 0.2467 -0.0440 0.0300  -0.0708 28   LYS   A CB  
762  C  CB  B LYS   A 28  ? 0.2669 0.2927 0.2365 0.0096  0.0032  -0.0414 28   LYS   A CB  
763  C  CG  A LYS   A 28  ? 0.2920 0.3197 0.2970 -0.0373 0.0199  -0.0775 28   LYS   A CG  
764  C  CG  B LYS   A 28  ? 0.2744 0.2969 0.2745 0.0157  -0.0069 -0.0445 28   LYS   A CG  
765  C  CD  A LYS   A 28  ? 0.2978 0.3324 0.3521 -0.0314 0.0106  -0.0787 28   LYS   A CD  
766  C  CD  B LYS   A 28  ? 0.2835 0.3053 0.3183 0.0198  -0.0133 -0.0438 28   LYS   A CD  
767  C  CE  A LYS   A 28  ? 0.2988 0.3399 0.3901 -0.0284 0.0023  -0.0829 28   LYS   A CE  
768  C  CE  B LYS   A 28  ? 0.2902 0.3113 0.3515 0.0186  -0.0175 -0.0424 28   LYS   A CE  
769  N  NZ  A LYS   A 28  ? 0.3020 0.3450 0.4153 -0.0246 0.0019  -0.0847 28   LYS   A NZ  
770  N  NZ  B LYS   A 28  ? 0.2925 0.3142 0.3671 0.0178  -0.0200 -0.0419 28   LYS   A NZ  
797  N  N   A LYS   A 29  ? 0.2960 0.3400 0.1618 -0.0521 0.0938  -0.0278 29   LYS   A N   
798  N  N   B LYS   A 29  ? 0.2933 0.3236 0.1988 -0.0180 0.0499  -0.0196 29   LYS   A N   
799  C  CA  A LYS   A 29  ? 0.3131 0.3625 0.1873 -0.0537 0.1003  -0.0102 29   LYS   A CA  
800  C  CA  B LYS   A 29  ? 0.3074 0.3397 0.2091 -0.0281 0.0633  -0.0113 29   LYS   A CA  
801  C  C   A LYS   A 29  ? 0.3114 0.3596 0.1726 -0.0594 0.0871  -0.0035 29   LYS   A C   
802  C  C   B LYS   A 29  ? 0.3078 0.3464 0.1818 -0.0484 0.0702  -0.0030 29   LYS   A C   
803  O  O   A LYS   A 29  ? 0.3189 0.3688 0.1882 -0.0541 0.0774  -0.0016 29   LYS   A O   
804  O  O   B LYS   A 29  ? 0.3126 0.3519 0.1812 -0.0483 0.0743  0.0048  29   LYS   A O   
805  C  CB  A LYS   A 29  ? 0.3275 0.3849 0.2406 -0.0475 0.1134  -0.0006 29   LYS   A CB  
806  C  CB  B LYS   A 29  ? 0.3188 0.3479 0.2460 -0.0164 0.0658  -0.0126 29   LYS   A CB  
807  C  CG  A LYS   A 29  ? 0.3423 0.4024 0.3026 -0.0424 0.1152  0.0053  29   LYS   A CG  
808  C  CG  B LYS   A 29  ? 0.3305 0.3536 0.2847 -0.0064 0.0635  -0.0155 29   LYS   A CG  
809  C  CD  A LYS   A 29  ? 0.3558 0.4167 0.3644 -0.0378 0.1104  0.0072  29   LYS   A CD  
810  C  CD  B LYS   A 29  ? 0.3406 0.3581 0.3239 0.0022  0.0585  -0.0210 29   LYS   A CD  
811  C  CE  A LYS   A 29  ? 0.3641 0.4270 0.4034 -0.0339 0.1095  0.0066  29   LYS   A CE  
812  C  CE  B LYS   A 29  ? 0.3470 0.3612 0.3499 0.0087  0.0537  -0.0254 29   LYS   A CE  
813  N  NZ  A LYS   A 29  ? 0.3676 0.4327 0.4287 -0.0317 0.1085  0.0050  29   LYS   A NZ  
814  N  NZ  B LYS   A 29  ? 0.3502 0.3631 0.3629 0.0121  0.0509  -0.0284 29   LYS   A NZ  
841  N  N   . VAL   A 30  ? 0.3005 0.3453 0.1655 -0.0673 0.0744  -0.0017 30   VAL   A N   
842  C  CA  . VAL   A 30  ? 0.2971 0.3339 0.1483 -0.0873 0.0529  0.0196  30   VAL   A CA  
843  C  C   . VAL   A 30  ? 0.2981 0.3182 0.1152 -0.0881 0.0359  0.0255  30   VAL   A C   
844  O  O   . VAL   A 30  ? 0.3089 0.3243 0.1112 -0.0924 0.0230  0.0236  30   VAL   A O   
845  C  CB  . VAL   A 30  ? 0.2905 0.3322 0.1937 -0.1008 0.0325  0.0298  30   VAL   A CB  
846  C  CG1 . VAL   A 30  ? 0.2925 0.3319 0.2128 -0.1057 0.0176  0.0370  30   VAL   A CG1 
847  C  CG2 . VAL   A 30  ? 0.2884 0.3355 0.2279 -0.1065 0.0348  0.0276  30   VAL   A CG2 
858  N  N   . LYS   A 31  ? 0.2915 0.3050 0.1081 -0.0943 0.0250  0.0205  31   LYS   A N   
859  C  CA  . LYS   A 31  ? 0.3060 0.3025 0.1131 -0.0861 0.0006  0.0157  31   LYS   A CA  
860  C  C   . LYS   A 31  ? 0.2814 0.2783 0.0982 -0.0676 -0.0020 0.0423  31   LYS   A C   
861  O  O   . LYS   A 31  ? 0.2914 0.2890 0.1221 -0.0651 -0.0072 0.0553  31   LYS   A O   
862  C  CB  . LYS   A 31  ? 0.3573 0.3302 0.2121 -0.0835 -0.0208 -0.0084 31   LYS   A CB  
863  C  CG  . LYS   A 31  ? 0.4102 0.3628 0.3563 -0.0724 -0.0375 -0.0236 31   LYS   A CG  
864  C  CD  . LYS   A 31  ? 0.4450 0.3918 0.4652 -0.0627 -0.0514 -0.0347 31   LYS   A CD  
865  C  CE  . LYS   A 31  ? 0.4730 0.4139 0.5362 -0.0565 -0.0650 -0.0449 31   LYS   A CE  
866  N  NZ  . LYS   A 31  ? 0.4937 0.4193 0.5721 -0.0540 -0.0729 -0.0508 31   LYS   A NZ  
880  N  N   . PRO   A 32  ? 0.2495 0.2505 0.0920 -0.0591 0.0062  0.0352  32   PRO   A N   
881  C  CA  . PRO   A 32  ? 0.2407 0.2320 0.1201 -0.0529 0.0022  0.0492  32   PRO   A CA  
882  C  C   . PRO   A 32  ? 0.2365 0.2286 0.1276 -0.0406 -0.0097 0.0520  32   PRO   A C   
883  O  O   . PRO   A 32  ? 0.2242 0.2231 0.1381 -0.0469 -0.0248 0.0511  32   PRO   A O   
884  C  CB  . PRO   A 32  ? 0.2349 0.2379 0.1335 -0.0488 -0.0007 0.0364  32   PRO   A CB  
885  C  CG  . PRO   A 32  ? 0.2287 0.2410 0.0917 -0.0452 -0.0069 0.0315  32   PRO   A CG  
886  C  CD  . PRO   A 32  ? 0.2342 0.2405 0.0858 -0.0491 -0.0040 0.0316  32   PRO   A CD  
894  N  N   . THR   A 33  ? 0.2439 0.2245 0.1188 -0.0377 -0.0111 0.0554  33   THR   A N   
895  C  CA  . THR   A 33  ? 0.2438 0.2227 0.1321 -0.0254 -0.0238 0.0588  33   THR   A CA  
896  C  C   . THR   A 33  ? 0.2127 0.2009 0.1200 -0.0270 -0.0232 0.0470  33   THR   A C   
897  O  O   . THR   A 33  ? 0.2011 0.2036 0.1344 -0.0269 -0.0373 0.0463  33   THR   A O   
898  C  CB  . THR   A 33  ? 0.2701 0.2404 0.1510 -0.0168 -0.0320 0.0721  33   THR   A CB  
899  O  OG1 . THR   A 33  ? 0.2923 0.2514 0.1832 -0.0086 -0.0185 0.0854  33   THR   A OG1 
900  C  CG2 . THR   A 33  ? 0.2742 0.2510 0.1775 -0.0114 -0.0333 0.0651  33   THR   A CG2 
908  N  N   . VAL   A 34  ? 0.1885 0.1824 0.1131 -0.0294 -0.0179 0.0435  34   VAL   A N   
909  C  CA  . VAL   A 34  ? 0.1750 0.1688 0.1086 -0.0252 -0.0093 0.0373  34   VAL   A CA  
910  C  C   . VAL   A 34  ? 0.1591 0.1621 0.1046 -0.0254 0.0031  0.0254  34   VAL   A C   
911  O  O   . VAL   A 34  ? 0.1616 0.1658 0.1247 -0.0307 0.0021  0.0397  34   VAL   A O   
912  C  CB  . VAL   A 34  ? 0.1804 0.1678 0.1281 -0.0220 -0.0057 0.0250  34   VAL   A CB  
913  C  CG1 . VAL   A 34  ? 0.1856 0.1725 0.1245 -0.0221 0.0007  0.0224  34   VAL   A CG1 
914  C  CG2 . VAL   A 34  ? 0.1820 0.1811 0.1569 -0.0096 -0.0207 0.0236  34   VAL   A CG2 
924  N  N   . VAL   A 35  ? 0.1459 0.1481 0.1054 -0.0275 -0.0051 0.0263  35   VAL   A N   
925  C  CA  . VAL   A 35  ? 0.1396 0.1453 0.0989 -0.0262 0.0005  0.0212  35   VAL   A CA  
926  C  C   . VAL   A 35  ? 0.1319 0.1346 0.0951 -0.0182 -0.0002 0.0217  35   VAL   A C   
927  O  O   . VAL   A 35  ? 0.1255 0.1454 0.1145 -0.0245 0.0100  0.0146  35   VAL   A O   
928  C  CB  . VAL   A 35  ? 0.1473 0.1561 0.1017 -0.0179 0.0148  0.0116  35   VAL   A CB  
929  C  CG1 . VAL   A 35  ? 0.1569 0.1585 0.1188 -0.0064 0.0033  0.0055  35   VAL   A CG1 
930  C  CG2 . VAL   A 35  ? 0.1487 0.1574 0.1272 -0.0103 0.0136  0.0081  35   VAL   A CG2 
940  N  N   . VAL   A 36  ? 0.1184 0.1362 0.0970 -0.0194 0.0031  0.0234  36   VAL   A N   
941  C  CA  . VAL   A 36  ? 0.1145 0.1242 0.0926 -0.0098 0.0021  0.0166  36   VAL   A CA  
942  C  C   . VAL   A 36  ? 0.1113 0.1306 0.1013 -0.0119 0.0084  0.0140  36   VAL   A C   
943  O  O   . VAL   A 36  ? 0.1177 0.1262 0.1202 -0.0057 0.0151  0.0148  36   VAL   A O   
944  C  CB  . VAL   A 36  ? 0.1185 0.1163 0.1035 -0.0075 0.0005  0.0159  36   VAL   A CB  
945  C  CG1 . VAL   A 36  ? 0.1210 0.1166 0.1142 -0.0130 0.0042  0.0096  36   VAL   A CG1 
946  C  CG2 . VAL   A 36  ? 0.1303 0.1197 0.1322 -0.0093 0.0006  0.0221  36   VAL   A CG2 
956  N  N   . ASN   A 37  ? 0.1027 0.1192 0.1029 -0.0027 0.0083  0.0178  37   ASN   A N   
957  C  CA  . ASN   A 37  ? 0.1056 0.1133 0.0964 0.0006  0.0100  0.0159  37   ASN   A CA  
958  C  C   . ASN   A 37  ? 0.1105 0.1112 0.1010 -0.0022 0.0151  0.0199  37   ASN   A C   
959  O  O   . ASN   A 37  ? 0.1218 0.1213 0.1045 0.0057  0.0097  0.0096  37   ASN   A O   
960  C  CB  . ASN   A 37  ? 0.1131 0.1155 0.1028 0.0021  0.0024  0.0108  37   ASN   A CB  
961  C  CG  . ASN   A 37  ? 0.1094 0.1175 0.1102 -0.0011 0.0037  0.0119  37   ASN   A CG  
962  O  OD1 . ASN   A 37  ? 0.1105 0.1187 0.1235 -0.0004 0.0032  0.0150  37   ASN   A OD1 
963  N  ND2 . ASN   A 37  ? 0.1149 0.1176 0.1151 -0.0021 0.0014  0.0249  37   ASN   A ND2 
970  N  N   A ALA   A 38  ? 0.1080 0.1258 0.1058 -0.0053 0.0093  0.0124  38   ALA   A N   
971  N  N   B ALA   A 38  ? 0.1134 0.1192 0.1097 -0.0019 0.0098  0.0078  38   ALA   A N   
972  C  CA  A ALA   A 38  ? 0.1121 0.1218 0.0983 -0.0023 0.0033  0.0071  38   ALA   A CA  
973  C  CA  B ALA   A 38  ? 0.1234 0.1201 0.1183 -0.0025 -0.0008 0.0063  38   ALA   A CA  
974  C  C   A ALA   A 38  ? 0.1098 0.1201 0.0828 -0.0032 -0.0037 0.0032  38   ALA   A C   
975  C  C   B ALA   A 38  ? 0.1194 0.1217 0.1177 -0.0009 -0.0097 -0.0033 38   ALA   A C   
976  O  O   A ALA   A 38  ? 0.1101 0.1073 0.0961 -0.0021 -0.0108 -0.0053 38   ALA   A O   
977  O  O   B ALA   A 38  ? 0.1157 0.1135 0.1281 -0.0105 -0.0221 0.0021  38   ALA   A O   
978  C  CB  A ALA   A 38  ? 0.1104 0.1321 0.1084 -0.0156 0.0001  -0.0005 38   ALA   A CB  
979  C  CB  B ALA   A 38  ? 0.1312 0.1245 0.1379 -0.0072 -0.0088 -0.0035 38   ALA   A CB  
990  N  N   A ALA   A 39  ? 0.1083 0.1179 0.0893 -0.0008 0.0063  0.0130  39   ALA   A N   
991  N  N   B ALA   A 39  ? 0.1225 0.1282 0.1328 0.0025  -0.0048 0.0036  39   ALA   A N   
992  C  CA  A ALA   A 39  ? 0.1089 0.1230 0.0940 0.0038  0.0105  0.0167  39   ALA   A CA  
993  C  CA  B ALA   A 39  ? 0.1266 0.1288 0.1222 0.0010  -0.0125 0.0021  39   ALA   A CA  
994  C  C   A ALA   A 39  ? 0.1114 0.1206 0.0920 -0.0014 0.0068  0.0104  39   ALA   A C   
995  C  C   B ALA   A 39  ? 0.1246 0.1173 0.1150 -0.0001 -0.0102 0.0004  39   ALA   A C   
996  O  O   A ALA   A 39  ? 0.1162 0.1294 0.0995 -0.0116 0.0123  0.0145  39   ALA   A O   
997  O  O   B ALA   A 39  ? 0.1379 0.1144 0.1166 0.0003  -0.0162 -0.0129 39   ALA   A O   
998  C  CB  A ALA   A 39  ? 0.1063 0.1308 0.1109 0.0069  0.0040  0.0123  39   ALA   A CB  
999  C  CB  B ALA   A 39  ? 0.1336 0.1385 0.1261 -0.0024 -0.0202 -0.0004 39   ALA   A CB  
1010 N  N   A ASN   A 40  ? 0.1127 0.1209 0.0975 -0.0092 0.0159  0.0021  40   ASN   A N   
1011 N  N   B ASN   A 40  ? 0.1221 0.1186 0.1134 -0.0030 -0.0003 0.0090  40   ASN   A N   
1012 C  CA  A ASN   A 40  ? 0.1171 0.1166 0.1040 0.0009  -0.0016 -0.0016 40   ASN   A CA  
1013 C  CA  B ASN   A 40  ? 0.1217 0.1137 0.1171 -0.0001 -0.0119 0.0179  40   ASN   A CA  
1014 C  C   A ASN   A 40  ? 0.1166 0.1091 0.0909 0.0021  0.0104  0.0073  40   ASN   A C   
1015 C  C   B ASN   A 40  ? 0.1217 0.1145 0.1025 -0.0050 -0.0018 0.0233  40   ASN   A C   
1016 O  O   A ASN   A 40  ? 0.1239 0.1061 0.0942 -0.0056 0.0103  0.0133  40   ASN   A O   
1017 O  O   B ASN   A 40  ? 0.1190 0.1186 0.1049 -0.0065 -0.0029 0.0224  40   ASN   A O   
1018 C  CB  A ASN   A 40  ? 0.1249 0.1293 0.1201 0.0085  -0.0093 -0.0010 40   ASN   A CB  
1019 C  CB  B ASN   A 40  ? 0.1290 0.1111 0.1440 0.0050  -0.0155 0.0162  40   ASN   A CB  
1020 C  CG  A ASN   A 40  ? 0.1281 0.1318 0.1396 0.0052  -0.0012 0.0088  40   ASN   A CG  
1021 C  CG  B ASN   A 40  ? 0.1365 0.1063 0.1631 0.0029  -0.0212 0.0123  40   ASN   A CG  
1022 O  OD1 A ASN   A 40  ? 0.1336 0.1417 0.1593 0.0015  0.0196  0.0155  40   ASN   A OD1 
1023 O  OD1 B ASN   A 40  ? 0.1489 0.1153 0.2239 0.0066  -0.0266 -0.0089 40   ASN   A OD1 
1024 N  ND2 A ASN   A 40  ? 0.1320 0.1406 0.1494 -0.0003 0.0125  0.0044  40   ASN   A ND2 
1025 N  ND2 B ASN   A 40  ? 0.1308 0.1158 0.1539 -0.0082 -0.0020 -0.0026 40   ASN   A ND2 
1038 N  N   A VAL   A 41  ? 0.1173 0.1114 0.0943 0.0029  0.0104  0.0066  41   VAL   A N   
1039 N  N   B VAL   A 41  ? 0.1283 0.1201 0.1049 -0.0039 -0.0010 0.0318  41   VAL   A N   
1040 C  CA  A VAL   A 41  ? 0.1180 0.1185 0.1040 -0.0004 0.0093  0.0060  41   VAL   A CA  
1041 C  CA  B VAL   A 41  ? 0.1362 0.1293 0.1163 -0.0024 0.0051  0.0233  41   VAL   A CA  
1042 C  C   A VAL   A 41  ? 0.1147 0.1174 0.1085 0.0038  0.0144  0.0068  41   VAL   A C   
1043 C  C   B VAL   A 41  ? 0.1341 0.1234 0.1165 -0.0077 0.0120  0.0216  41   VAL   A C   
1044 O  O   A VAL   A 41  ? 0.1210 0.1134 0.1306 0.0018  0.0137  -0.0058 41   VAL   A O   
1045 O  O   B VAL   A 41  ? 0.1399 0.1153 0.1183 -0.0080 -0.0005 0.0172  41   VAL   A O   
1046 C  CB  A VAL   A 41  ? 0.1258 0.1223 0.0999 -0.0020 0.0118  0.0086  41   VAL   A CB  
1047 C  CB  B VAL   A 41  ? 0.1440 0.1419 0.1304 0.0001  0.0174  0.0204  41   VAL   A CB  
1048 C  CG1 A VAL   A 41  ? 0.1324 0.1335 0.0960 0.0009  0.0042  0.0041  41   VAL   A CG1 
1049 C  CG1 B VAL   A 41  ? 0.1543 0.1516 0.1346 -0.0023 0.0205  0.0137  41   VAL   A CG1 
1050 C  CG2 A VAL   A 41  ? 0.1340 0.1236 0.0946 -0.0010 0.0268  0.0075  41   VAL   A CG2 
1051 C  CG2 B VAL   A 41  ? 0.1489 0.1496 0.1383 0.0010  0.0122  0.0209  41   VAL   A CG2 
1070 N  N   A TYR   A 42  ? 0.1097 0.1088 0.1360 -0.0013 0.0158  0.0125  42   TYR   A N   
1071 N  N   B TYR   A 42  ? 0.1305 0.1230 0.1242 -0.0062 0.0169  0.0308  42   TYR   A N   
1072 C  CA  A TYR   A 42  ? 0.1235 0.1066 0.1347 -0.0040 0.0216  0.0167  42   TYR   A CA  
1073 C  CA  B TYR   A 42  ? 0.1329 0.1277 0.1298 -0.0072 0.0266  0.0326  42   TYR   A CA  
1074 C  C   A TYR   A 42  ? 0.1166 0.1058 0.1366 -0.0023 0.0128  0.0178  42   TYR   A C   
1075 C  C   B TYR   A 42  ? 0.1291 0.1336 0.1216 -0.0099 0.0138  0.0382  42   TYR   A C   
1076 O  O   A TYR   A 42  ? 0.1149 0.1048 0.1580 -0.0074 0.0072  -0.0025 42   TYR   A O   
1077 O  O   B TYR   A 42  ? 0.1238 0.1441 0.1327 -0.0158 0.0141  0.0259  42   TYR   A O   
1078 C  CB  A TYR   A 42  ? 0.1529 0.1157 0.1280 -0.0018 0.0271  0.0209  42   TYR   A CB  
1079 C  CB  B TYR   A 42  ? 0.1480 0.1322 0.1373 -0.0064 0.0282  0.0269  42   TYR   A CB  
1080 C  CG  A TYR   A 42  ? 0.1721 0.1302 0.1306 0.0023  0.0316  0.0338  42   TYR   A CG  
1081 C  CG  B TYR   A 42  ? 0.1583 0.1449 0.1452 -0.0071 0.0342  0.0229  42   TYR   A CG  
1082 C  CD1 A TYR   A 42  ? 0.1769 0.1455 0.1346 0.0014  0.0285  0.0395  42   TYR   A CD1 
1083 C  CD1 B TYR   A 42  ? 0.1646 0.1579 0.1532 -0.0076 0.0307  0.0188  42   TYR   A CD1 
1084 C  CD2 A TYR   A 42  ? 0.1790 0.1563 0.1472 0.0089  0.0384  0.0167  42   TYR   A CD2 
1085 C  CD2 B TYR   A 42  ? 0.1556 0.1592 0.1437 -0.0030 0.0449  0.0135  42   TYR   A CD2 
1086 C  CE1 A TYR   A 42  ? 0.1743 0.1566 0.1335 -0.0010 0.0322  0.0321  42   TYR   A CE1 
1087 C  CE1 B TYR   A 42  ? 0.1613 0.1624 0.1457 -0.0088 0.0311  0.0134  42   TYR   A CE1 
1088 C  CE2 A TYR   A 42  ? 0.1817 0.1710 0.1479 0.0048  0.0404  0.0191  42   TYR   A CE2 
1089 C  CE2 B TYR   A 42  ? 0.1549 0.1669 0.1507 -0.0086 0.0436  0.0145  42   TYR   A CE2 
1090 C  CZ  A TYR   A 42  ? 0.1730 0.1688 0.1454 -0.0022 0.0415  0.0255  42   TYR   A CZ  
1091 C  CZ  B TYR   A 42  ? 0.1572 0.1657 0.1380 -0.0110 0.0414  0.0124  42   TYR   A CZ  
1092 O  OH  A TYR   A 42  ? 0.1636 0.1929 0.1732 -0.0134 0.0447  0.0157  42   TYR   A OH  
1093 O  OH  B TYR   A 42  ? 0.1636 0.1748 0.1533 -0.0100 0.0372  0.0028  42   TYR   A OH  
1112 N  N   A LEU   A 43  ? 0.1175 0.1063 0.1209 -0.0059 0.0096  0.0001  43   LEU   A N   
1113 N  N   B LEU   A 43  ? 0.1236 0.1291 0.1235 -0.0099 0.0082  0.0343  43   LEU   A N   
1114 C  CA  A LEU   A 43  ? 0.1113 0.1086 0.1278 -0.0039 0.0086  -0.0043 43   LEU   A CA  
1115 C  CA  B LEU   A 43  ? 0.1234 0.1257 0.1225 -0.0111 0.0046  0.0292  43   LEU   A CA  
1116 C  C   A LEU   A 43  ? 0.1084 0.1155 0.1284 -0.0001 0.0037  -0.0057 43   LEU   A C   
1117 C  C   B LEU   A 43  ? 0.1274 0.1225 0.1249 -0.0131 0.0027  0.0242  43   LEU   A C   
1118 O  O   A LEU   A 43  ? 0.1200 0.1203 0.1530 0.0105  -0.0096 -0.0054 43   LEU   A O   
1119 O  O   B LEU   A 43  ? 0.1303 0.1206 0.1298 -0.0175 -0.0026 0.0198  43   LEU   A O   
1120 C  CB  A LEU   A 43  ? 0.1187 0.1091 0.1315 -0.0077 0.0048  -0.0049 43   LEU   A CB  
1121 C  CB  B LEU   A 43  ? 0.1181 0.1232 0.1255 -0.0149 0.0019  0.0311  43   LEU   A CB  
1122 C  CG  A LEU   A 43  ? 0.1206 0.1103 0.1461 -0.0054 0.0011  0.0001  43   LEU   A CG  
1123 C  CG  B LEU   A 43  ? 0.1142 0.1190 0.1249 -0.0094 -0.0008 0.0295  43   LEU   A CG  
1124 C  CD1 A LEU   A 43  ? 0.1243 0.1119 0.1719 -0.0054 -0.0046 0.0078  43   LEU   A CD1 
1125 C  CD1 B LEU   A 43  ? 0.1167 0.1214 0.1310 -0.0067 -0.0134 0.0322  43   LEU   A CD1 
1126 C  CD2 A LEU   A 43  ? 0.1273 0.1190 0.1331 -0.0044 -0.0026 0.0041  43   LEU   A CD2 
1127 C  CD2 B LEU   A 43  ? 0.1216 0.1167 0.1302 -0.0091 -0.0044 0.0388  43   LEU   A CD2 
1150 N  N   A LYS   A 44  ? 0.1213 0.1160 0.1179 0.0008  0.0111  -0.0003 44   LYS   A N   
1151 N  N   B LYS   A 44  ? 0.1337 0.1229 0.1229 -0.0027 -0.0012 0.0253  44   LYS   A N   
1152 C  CA  A LYS   A 44  ? 0.1337 0.1085 0.1283 -0.0051 0.0216  0.0125  44   LYS   A CA  
1153 C  CA  B LYS   A 44  ? 0.1437 0.1225 0.1266 0.0041  -0.0009 0.0256  44   LYS   A CA  
1154 C  C   A LYS   A 44  ? 0.1247 0.1088 0.1170 0.0011  0.0046  0.0112  44   LYS   A C   
1155 C  C   B LYS   A 44  ? 0.1322 0.1143 0.1156 0.0065  -0.0024 0.0158  44   LYS   A C   
1156 O  O   A LYS   A 44  ? 0.1303 0.1262 0.1391 -0.0013 0.0004  0.0061  44   LYS   A O   
1157 O  O   B LYS   A 44  ? 0.1387 0.1216 0.1285 0.0094  -0.0027 0.0074  44   LYS   A O   
1158 C  CB  A LYS   A 44  ? 0.1652 0.1239 0.1712 -0.0048 0.0386  0.0268  44   LYS   A CB  
1159 C  CB  B LYS   A 44  ? 0.1715 0.1453 0.1769 0.0108  0.0060  0.0221  44   LYS   A CB  
1160 C  CG  A LYS   A 44  ? 0.1949 0.1451 0.2281 -0.0132 0.0645  0.0493  44   LYS   A CG  
1161 C  CG  B LYS   A 44  ? 0.1946 0.1661 0.2366 0.0136  0.0157  0.0220  44   LYS   A CG  
1162 C  CD  A LYS   A 44  ? 0.2326 0.1906 0.3393 -0.0210 0.0526  0.0382  44   LYS   A CD  
1163 C  CD  B LYS   A 44  ? 0.2211 0.2000 0.3108 0.0087  0.0082  0.0154  44   LYS   A CD  
1164 C  CE  A LYS   A 44  ? 0.2532 0.2183 0.4107 -0.0244 0.0489  0.0339  44   LYS   A CE  
1165 C  CE  B LYS   A 44  ? 0.2314 0.2159 0.3564 0.0063  0.0063  0.0120  44   LYS   A CE  
1166 N  NZ  A LYS   A 44  ? 0.2634 0.2355 0.4452 -0.0275 0.0482  0.0351  44   LYS   A NZ  
1167 N  NZ  B LYS   A 44  ? 0.2319 0.2116 0.3724 0.0062  0.0051  0.0131  44   LYS   A NZ  
1194 N  N   . HIS   A 45  ? 0.1212 0.1121 0.1168 0.0012  0.0002  0.0138  45   HIS   A N   
1195 C  CA  . HIS   A 45  ? 0.1185 0.1136 0.1208 0.0021  -0.0076 0.0045  45   HIS   A CA  
1196 C  C   . HIS   A 45  ? 0.1253 0.1270 0.1325 0.0042  -0.0048 0.0084  45   HIS   A C   
1197 O  O   . HIS   A 45  ? 0.1434 0.1375 0.1568 0.0222  -0.0071 -0.0075 45   HIS   A O   
1198 C  CB  . HIS   A 45  ? 0.1183 0.1147 0.1203 0.0013  -0.0043 0.0054  45   HIS   A CB  
1199 C  CG  . HIS   A 45  ? 0.1172 0.1117 0.1029 -0.0041 0.0020  0.0045  45   HIS   A CG  
1200 N  ND1 . HIS   A 45  ? 0.1097 0.1188 0.1237 -0.0026 0.0006  0.0117  45   HIS   A ND1 
1201 C  CD2 . HIS   A 45  ? 0.1140 0.1138 0.1163 -0.0082 -0.0049 0.0178  45   HIS   A CD2 
1202 C  CE1 . HIS   A 45  ? 0.1101 0.1200 0.1124 -0.0050 -0.0014 0.0184  45   HIS   A CE1 
1203 N  NE2 . HIS   A 45  ? 0.1107 0.1271 0.1149 -0.0041 -0.0063 0.0171  45   HIS   A NE2 
1212 N  N   A GLY   A 46  ? 0.1318 0.1335 0.1495 0.0172  -0.0112 0.0181  46   GLY   A N   
1213 N  N   B GLY   A 46  ? 0.1386 0.1206 0.1388 -0.0015 -0.0176 0.0071  46   GLY   A N   
1214 C  CA  A GLY   A 46  ? 0.1301 0.1323 0.1601 0.0120  -0.0116 0.0321  46   GLY   A CA  
1215 C  CA  B GLY   A 46  ? 0.1372 0.1220 0.1489 -0.0068 -0.0149 0.0127  46   GLY   A CA  
1216 C  C   A GLY   A 46  ? 0.1320 0.1239 0.1365 0.0180  -0.0205 0.0449  46   GLY   A C   
1217 C  C   B GLY   A 46  ? 0.1367 0.1246 0.1419 0.0006  -0.0086 0.0227  46   GLY   A C   
1218 O  O   A GLY   A 46  ? 0.1408 0.1243 0.1395 0.0188  -0.0222 0.0461  46   GLY   A O   
1219 O  O   B GLY   A 46  ? 0.1416 0.1248 0.1364 -0.0015 -0.0045 0.0236  46   GLY   A O   
1226 N  N   A GLY   A 47  ? 0.1290 0.1247 0.1455 0.0220  -0.0210 0.0277  47   GLY   A N   
1227 N  N   B GLY   A 47  ? 0.1361 0.1287 0.1481 0.0027  -0.0083 0.0122  47   GLY   A N   
1228 C  CA  A GLY   A 47  ? 0.1322 0.1363 0.1590 0.0221  -0.0223 0.0233  47   GLY   A CA  
1229 C  CA  B GLY   A 47  ? 0.1311 0.1317 0.1402 0.0008  -0.0135 0.0131  47   GLY   A CA  
1230 C  C   A GLY   A 47  ? 0.1307 0.1296 0.1454 0.0197  -0.0245 0.0157  47   GLY   A C   
1231 C  C   B GLY   A 47  ? 0.1248 0.1234 0.1119 -0.0024 -0.0158 0.0094  47   GLY   A C   
1232 O  O   A GLY   A 47  ? 0.1233 0.1265 0.1502 0.0237  -0.0138 0.0219  47   GLY   A O   
1233 O  O   B GLY   A 47  ? 0.1236 0.1242 0.1002 -0.0035 -0.0142 0.0159  47   GLY   A O   
1240 N  N   A GLY   A 48  ? 0.1312 0.1338 0.1436 0.0202  -0.0228 0.0050  48   GLY   A N   
1241 N  N   B GLY   A 48  ? 0.1213 0.1275 0.1171 -0.0019 -0.0035 0.0096  48   GLY   A N   
1242 C  CA  A GLY   A 48  ? 0.1227 0.1332 0.1506 0.0135  -0.0133 -0.0024 48   GLY   A CA  
1243 C  CA  B GLY   A 48  ? 0.1142 0.1165 0.1061 -0.0114 -0.0023 -0.0029 48   GLY   A CA  
1244 C  C   A GLY   A 48  ? 0.1192 0.1267 0.1405 0.0004  0.0016  0.0009  48   GLY   A C   
1245 C  C   B GLY   A 48  ? 0.1170 0.1133 0.1116 -0.0174 -0.0025 0.0053  48   GLY   A C   
1246 O  O   A GLY   A 48  ? 0.1312 0.1230 0.1367 0.0016  -0.0000 -0.0015 48   GLY   A O   
1247 O  O   B GLY   A 48  ? 0.1293 0.1174 0.1106 -0.0190 0.0009  0.0046  48   GLY   A O   
1254 N  N   A VAL   A 49  ? 0.1150 0.1197 0.1464 -0.0059 -0.0075 0.0018  49   VAL   A N   
1255 N  N   B VAL   A 49  ? 0.1141 0.1096 0.1230 -0.0158 -0.0055 0.0032  49   VAL   A N   
1256 C  CA  A VAL   A 49  ? 0.1253 0.1176 0.1401 -0.0034 0.0090  -0.0018 49   VAL   A CA  
1257 C  CA  B VAL   A 49  ? 0.1119 0.1154 0.1254 -0.0117 0.0001  0.0033  49   VAL   A CA  
1258 C  C   A VAL   A 49  ? 0.1196 0.1105 0.1252 -0.0001 0.0090  0.0009  49   VAL   A C   
1259 C  C   B VAL   A 49  ? 0.1118 0.1121 0.1202 -0.0001 0.0018  0.0001  49   VAL   A C   
1260 O  O   A VAL   A 49  ? 0.1234 0.1182 0.1365 -0.0140 0.0133  -0.0052 49   VAL   A O   
1261 O  O   B VAL   A 49  ? 0.1115 0.1089 0.1063 0.0079  0.0030  0.0056  49   VAL   A O   
1262 C  CB  A VAL   A 49  ? 0.1413 0.1170 0.1600 -0.0011 0.0125  -0.0003 49   VAL   A CB  
1263 C  CB  B VAL   A 49  ? 0.1117 0.1157 0.1296 -0.0047 0.0009  0.0012  49   VAL   A CB  
1264 C  CG1 A VAL   A 49  ? 0.1491 0.1126 0.1713 0.0039  0.0161  0.0026  49   VAL   A CG1 
1265 C  CG1 B VAL   A 49  ? 0.1022 0.1166 0.1113 0.0083  0.0034  0.0010  49   VAL   A CG1 
1266 C  CG2 A VAL   A 49  ? 0.1543 0.1253 0.1956 -0.0158 0.0005  -0.0074 49   VAL   A CG2 
1267 C  CG2 B VAL   A 49  ? 0.1154 0.1155 0.1467 -0.0070 -0.0035 0.0023  49   VAL   A CG2 
1286 N  N   . ALA   A 50  ? 0.1136 0.1117 0.1171 -0.0040 -0.0013 0.0081  50   ALA   A N   
1287 C  CA  . ALA   A 50  ? 0.1105 0.1105 0.1095 -0.0082 -0.0069 0.0071  50   ALA   A CA  
1288 C  C   . ALA   A 50  ? 0.1040 0.1166 0.1109 -0.0069 -0.0084 0.0011  50   ALA   A C   
1289 O  O   . ALA   A 50  ? 0.1099 0.1143 0.1201 -0.0017 -0.0054 0.0053  50   ALA   A O   
1290 C  CB  . ALA   A 50  ? 0.1159 0.1117 0.1120 -0.0057 0.0020  0.0036  50   ALA   A CB  
1297 N  N   . GLY   A 51  ? 0.1124 0.1077 0.1214 0.0025  -0.0153 0.0028  51   GLY   A N   
1298 C  CA  . GLY   A 51  ? 0.1237 0.1111 0.1233 0.0047  -0.0204 0.0002  51   GLY   A CA  
1299 C  C   . GLY   A 51  ? 0.1147 0.1240 0.1233 0.0042  -0.0126 -0.0084 51   GLY   A C   
1300 O  O   . GLY   A 51  ? 0.1199 0.1260 0.1352 0.0024  -0.0101 -0.0103 51   GLY   A O   
1304 N  N   . ALA   A 52  ? 0.1164 0.1310 0.1220 0.0026  -0.0052 -0.0176 52   ALA   A N   
1305 C  CA  . ALA   A 52  ? 0.1163 0.1407 0.1330 -0.0009 -0.0012 -0.0152 52   ALA   A CA  
1306 C  C   . ALA   A 52  ? 0.1143 0.1345 0.1130 -0.0091 0.0002  -0.0086 52   ALA   A C   
1307 O  O   . ALA   A 52  ? 0.1245 0.1363 0.1311 -0.0035 0.0026  -0.0128 52   ALA   A O   
1308 C  CB  . ALA   A 52  ? 0.1238 0.1689 0.1432 -0.0082 -0.0035 -0.0123 52   ALA   A CB  
1314 N  N   A LEU   A 53  ? 0.1138 0.1299 0.1141 -0.0079 0.0016  -0.0035 53   LEU   A N   
1315 N  N   B LEU   A 53  ? 0.1113 0.1312 0.1079 -0.0054 -0.0020 -0.0037 53   LEU   A N   
1316 C  CA  A LEU   A 53  ? 0.1229 0.1331 0.1074 -0.0083 0.0048  0.0013  53   LEU   A CA  
1317 C  CA  B LEU   A 53  ? 0.1158 0.1304 0.0977 -0.0048 -0.0027 -0.0004 53   LEU   A CA  
1318 C  C   A LEU   A 53  ? 0.1212 0.1295 0.0979 -0.0002 0.0052  0.0006  53   LEU   A C   
1319 C  C   B LEU   A 53  ? 0.1151 0.1278 0.0951 0.0024  -0.0036 -0.0018 53   LEU   A C   
1320 O  O   A LEU   A 53  ? 0.1288 0.1385 0.1083 -0.0082 0.0040  0.0061  53   LEU   A O   
1321 O  O   B LEU   A 53  ? 0.1214 0.1349 0.1026 -0.0006 -0.0101 0.0000  53   LEU   A O   
1322 C  CB  A LEU   A 53  ? 0.1301 0.1391 0.1235 -0.0091 0.0094  0.0071  53   LEU   A CB  
1323 C  CB  B LEU   A 53  ? 0.1177 0.1311 0.0983 -0.0056 -0.0009 0.0035  53   LEU   A CB  
1324 C  CG  A LEU   A 53  ? 0.1292 0.1359 0.1355 -0.0099 0.0124  0.0097  53   LEU   A CG  
1325 C  CG  B LEU   A 53  ? 0.1168 0.1273 0.1006 -0.0037 -0.0096 0.0043  53   LEU   A CG  
1326 C  CD1 A LEU   A 53  ? 0.1224 0.1355 0.1414 -0.0026 0.0094  0.0182  53   LEU   A CD1 
1327 C  CD1 B LEU   A 53  ? 0.1185 0.1326 0.0952 -0.0053 -0.0015 0.0006  53   LEU   A CD1 
1328 C  CD2 A LEU   A 53  ? 0.1412 0.1475 0.1470 -0.0151 0.0152  0.0126  53   LEU   A CD2 
1329 C  CD2 B LEU   A 53  ? 0.1105 0.1249 0.1102 -0.0051 -0.0050 -0.0023 53   LEU   A CD2 
1352 N  N   . ASN   A 54  ? 0.1168 0.1241 0.0987 -0.0020 -0.0024 0.0038  54   ASN   A N   
1353 C  CA  . ASN   A 54  ? 0.1063 0.1197 0.1135 -0.0023 -0.0127 -0.0005 54   ASN   A CA  
1354 C  C   . ASN   A 54  ? 0.1160 0.1266 0.1130 -0.0075 -0.0075 -0.0006 54   ASN   A C   
1355 O  O   . ASN   A 54  ? 0.1186 0.1327 0.1208 -0.0042 -0.0078 -0.0100 54   ASN   A O   
1356 C  CB  . ASN   A 54  ? 0.1033 0.1164 0.1242 -0.0043 -0.0097 -0.0043 54   ASN   A CB  
1357 C  CG  . ASN   A 54  ? 0.1108 0.1235 0.1238 0.0016  -0.0067 -0.0001 54   ASN   A CG  
1358 O  OD1 . ASN   A 54  ? 0.1086 0.1211 0.1269 0.0034  -0.0093 0.0035  54   ASN   A OD1 
1359 N  ND2 . ASN   A 54  ? 0.1127 0.1274 0.1404 -0.0055 -0.0143 0.0109  54   ASN   A ND2 
1367 N  N   . LYS   A 55  ? 0.1176 0.1270 0.1286 -0.0041 -0.0066 -0.0058 55   LYS   A N   
1368 C  CA  . LYS   A 55  ? 0.1261 0.1290 0.1266 0.0004  -0.0131 -0.0164 55   LYS   A CA  
1369 C  C   . LYS   A 55  ? 0.1250 0.1407 0.1275 0.0012  -0.0026 -0.0235 55   LYS   A C   
1370 O  O   . LYS   A 55  ? 0.1300 0.1524 0.1311 0.0058  -0.0069 -0.0240 55   LYS   A O   
1371 C  CB  . LYS   A 55  ? 0.1363 0.1384 0.1357 0.0127  -0.0138 -0.0151 55   LYS   A CB  
1372 C  CG  . LYS   A 55  ? 0.1435 0.1591 0.1547 0.0176  -0.0234 -0.0155 55   LYS   A CG  
1373 C  CD  . LYS   A 55  ? 0.1512 0.1798 0.1784 0.0268  -0.0131 -0.0209 55   LYS   A CD  
1374 C  CE  . LYS   A 55  ? 0.1644 0.2075 0.2022 0.0358  -0.0281 -0.0256 55   LYS   A CE  
1375 N  NZ  . LYS   A 55  ? 0.1626 0.2235 0.2181 0.0445  -0.0292 -0.0258 55   LYS   A NZ  
1389 N  N   . ALA   A 56  ? 0.1267 0.1504 0.1224 -0.0065 0.0007  -0.0202 56   ALA   A N   
1390 C  CA  . ALA   A 56  ? 0.1373 0.1653 0.1313 -0.0137 0.0048  -0.0141 56   ALA   A CA  
1391 C  C   . ALA   A 56  ? 0.1404 0.1762 0.1049 -0.0099 0.0057  -0.0194 56   ALA   A C   
1392 O  O   . ALA   A 56  ? 0.1528 0.2081 0.1223 0.0024  0.0080  -0.0168 56   ALA   A O   
1393 C  CB  . ALA   A 56  ? 0.1464 0.1861 0.1389 -0.0157 0.0108  -0.0037 56   ALA   A CB  
1399 N  N   . THR   A 57  ? 0.1251 0.1548 0.1124 -0.0032 0.0041  -0.0139 57   THR   A N   
1400 C  CA  . THR   A 57  ? 0.1314 0.1510 0.1094 -0.0064 -0.0004 -0.0074 57   THR   A CA  
1401 C  C   . THR   A 57  ? 0.1337 0.1538 0.1099 -0.0051 -0.0090 -0.0143 57   THR   A C   
1402 O  O   . THR   A 57  ? 0.1291 0.1595 0.1355 -0.0102 -0.0155 -0.0199 57   THR   A O   
1403 C  CB  . THR   A 57  ? 0.1309 0.1469 0.1110 -0.0064 0.0000  -0.0077 57   THR   A CB  
1404 O  OG1 . THR   A 57  ? 0.1228 0.1443 0.1142 -0.0052 -0.0030 -0.0054 57   THR   A OG1 
1405 C  CG2 . THR   A 57  ? 0.1346 0.1533 0.1080 -0.0053 -0.0023 -0.0007 57   THR   A CG2 
1413 N  N   . ASN   A 58  ? 0.1339 0.1527 0.1334 -0.0073 -0.0010 -0.0275 58   ASN   A N   
1414 C  CA  . ASN   A 58  ? 0.1511 0.1509 0.1502 -0.0085 0.0019  -0.0320 58   ASN   A CA  
1415 C  C   . ASN   A 58  ? 0.1322 0.1399 0.1346 -0.0013 -0.0042 -0.0246 58   ASN   A C   
1416 O  O   . ASN   A 58  ? 0.1352 0.1529 0.1474 -0.0100 -0.0086 -0.0250 58   ASN   A O   
1417 C  CB  . ASN   A 58  ? 0.1891 0.1673 0.1807 -0.0184 0.0202  -0.0488 58   ASN   A CB  
1418 C  CG  . ASN   A 58  ? 0.2252 0.1940 0.2421 -0.0097 0.0133  -0.0389 58   ASN   A CG  
1419 O  OD1 . ASN   A 58  ? 0.2484 0.1949 0.2743 0.0199  0.0374  -0.0309 58   ASN   A OD1 
1420 N  ND2 . ASN   A 58  ? 0.2345 0.1986 0.2644 -0.0123 -0.0025 -0.0368 58   ASN   A ND2 
1427 N  N   . ASN   A 59  ? 0.1192 0.1351 0.1288 -0.0060 -0.0141 -0.0114 59   ASN   A N   
1428 C  CA  . ASN   A 59  ? 0.1207 0.1209 0.1353 -0.0062 -0.0093 -0.0091 59   ASN   A CA  
1429 C  C   . ASN   A 59  ? 0.1212 0.1232 0.1224 -0.0048 -0.0081 -0.0072 59   ASN   A C   
1430 O  O   . ASN   A 59  ? 0.1183 0.1277 0.1329 -0.0054 -0.0044 0.0046  59   ASN   A O   
1431 C  CB  . ASN   A 59  ? 0.1244 0.1177 0.1469 0.0003  -0.0178 -0.0124 59   ASN   A CB  
1432 C  CG  . ASN   A 59  ? 0.1270 0.1263 0.1444 -0.0014 -0.0282 0.0002  59   ASN   A CG  
1433 O  OD1 . ASN   A 59  ? 0.1423 0.1273 0.1393 -0.0126 -0.0313 0.0079  59   ASN   A OD1 
1434 N  ND2 . ASN   A 59  ? 0.1360 0.1299 0.1583 -0.0122 -0.0229 0.0079  59   ASN   A ND2 
1441 N  N   . ALA   A 60  ? 0.1162 0.1319 0.1191 -0.0039 -0.0103 -0.0033 60   ALA   A N   
1442 C  CA  . ALA   A 60  ? 0.1112 0.1298 0.1331 -0.0035 -0.0154 -0.0005 60   ALA   A CA  
1443 C  C   . ALA   A 60  ? 0.1157 0.1257 0.1347 -0.0008 -0.0058 -0.0035 60   ALA   A C   
1444 O  O   . ALA   A 60  ? 0.1127 0.1257 0.1538 -0.0038 -0.0086 -0.0051 60   ALA   A O   
1445 C  CB  . ALA   A 60  ? 0.1286 0.1393 0.1363 -0.0049 -0.0183 -0.0109 60   ALA   A CB  
1451 N  N   . MET   A 61  ? 0.1146 0.1242 0.1291 -0.0073 -0.0067 -0.0052 61   MET   A N   
1452 C  CA  . MET   A 61  ? 0.1176 0.1216 0.1238 -0.0097 -0.0025 0.0032  61   MET   A CA  
1453 C  C   . MET   A 61  ? 0.1136 0.1154 0.1238 -0.0036 -0.0001 -0.0031 61   MET   A C   
1454 O  O   . MET   A 61  ? 0.1203 0.1148 0.1272 -0.0040 0.0033  0.0036  61   MET   A O   
1455 C  CB  . MET   A 61  ? 0.1191 0.1238 0.1186 -0.0063 -0.0046 0.0040  61   MET   A CB  
1456 C  CG  . MET   A 61  ? 0.1197 0.1307 0.1328 0.0041  -0.0011 0.0020  61   MET   A CG  
1457 S  SD  . MET   A 61  ? 0.1209 0.1279 0.1568 -0.0088 -0.0019 -0.0171 61   MET   A SD  
1458 C  CE  . MET   A 61  ? 0.1444 0.1471 0.1720 -0.0135 0.0106  -0.0104 61   MET   A CE  
1468 N  N   . GLN   A 62  ? 0.1119 0.1121 0.1262 -0.0073 -0.0026 -0.0016 62   GLN   A N   
1469 C  CA  . GLN   A 62  ? 0.1210 0.1139 0.1267 -0.0027 0.0032  0.0025  62   GLN   A CA  
1470 C  C   . GLN   A 62  ? 0.1184 0.1063 0.1335 -0.0033 0.0050  0.0050  62   GLN   A C   
1471 O  O   . GLN   A 62  ? 0.1221 0.1209 0.1454 -0.0050 0.0043  0.0024  62   GLN   A O   
1472 C  CB  . GLN   A 62  ? 0.1205 0.1078 0.1349 -0.0031 -0.0039 0.0053  62   GLN   A CB  
1473 C  CG  . GLN   A 62  ? 0.1224 0.1065 0.1290 -0.0047 -0.0102 0.0118  62   GLN   A CG  
1474 C  CD  . GLN   A 62  ? 0.1274 0.1162 0.1249 -0.0004 0.0001  0.0136  62   GLN   A CD  
1475 O  OE1 . GLN   A 62  ? 0.1344 0.1243 0.1356 -0.0019 -0.0010 0.0056  62   GLN   A OE1 
1476 N  NE2 . GLN   A 62  ? 0.1373 0.1247 0.1312 0.0002  -0.0024 -0.0025 62   GLN   A NE2 
1485 N  N   . VAL   A 63  ? 0.1137 0.1125 0.1471 -0.0052 0.0071  -0.0106 63   VAL   A N   
1486 C  CA  . VAL   A 63  ? 0.1184 0.1243 0.1766 -0.0162 -0.0018 -0.0134 63   VAL   A CA  
1487 C  C   . VAL   A 63  ? 0.1086 0.1231 0.1608 -0.0120 -0.0104 -0.0139 63   VAL   A C   
1488 O  O   . VAL   A 63  ? 0.1087 0.1286 0.1759 -0.0139 -0.0009 -0.0119 63   VAL   A O   
1489 C  CB  . VAL   A 63  ? 0.1261 0.1393 0.2020 -0.0163 -0.0026 -0.0345 63   VAL   A CB  
1490 C  CG1 . VAL   A 63  ? 0.1424 0.1608 0.2392 -0.0158 -0.0084 -0.0576 63   VAL   A CG1 
1491 C  CG2 . VAL   A 63  ? 0.1351 0.1320 0.2203 -0.0159 0.0155  -0.0315 63   VAL   A CG2 
1501 N  N   . GLU   A 64  ? 0.1139 0.1300 0.1472 -0.0067 -0.0063 -0.0081 64   GLU   A N   
1502 C  CA  . GLU   A 64  ? 0.1092 0.1269 0.1482 -0.0049 -0.0025 0.0021  64   GLU   A CA  
1503 C  C   . GLU   A 64  ? 0.1039 0.1204 0.1475 -0.0130 0.0020  -0.0020 64   GLU   A C   
1504 O  O   . GLU   A 64  ? 0.1134 0.1308 0.1507 -0.0054 -0.0009 -0.0010 64   GLU   A O   
1505 C  CB  . GLU   A 64  ? 0.1168 0.1430 0.1524 -0.0022 0.0011  -0.0067 64   GLU   A CB  
1506 C  CG  . GLU   A 64  ? 0.1255 0.1490 0.1591 -0.0056 0.0058  -0.0035 64   GLU   A CG  
1507 C  CD  . GLU   A 64  ? 0.1379 0.1496 0.1541 -0.0114 0.0161  -0.0009 64   GLU   A CD  
1508 O  OE1 . GLU   A 64  ? 0.1352 0.1530 0.1869 -0.0221 0.0172  -0.0001 64   GLU   A OE1 
1509 O  OE2 . GLU   A 64  ? 0.1585 0.1521 0.1569 -0.0205 -0.0023 0.0088  64   GLU   A OE2 
1516 N  N   . SER   A 65  ? 0.1028 0.1231 0.1366 -0.0016 0.0034  -0.0023 65   SER   A N   
1517 C  CA  . SER   A 65  ? 0.1089 0.1169 0.1320 -0.0050 -0.0024 -0.0009 65   SER   A CA  
1518 C  C   . SER   A 65  ? 0.1142 0.1252 0.1399 -0.0047 -0.0020 0.0013  65   SER   A C   
1519 O  O   . SER   A 65  ? 0.1239 0.1247 0.1591 -0.0001 0.0155  -0.0036 65   SER   A O   
1520 C  CB  . SER   A 65  ? 0.1125 0.1176 0.1285 -0.0072 0.0037  0.0053  65   SER   A CB  
1521 O  OG  . SER   A 65  ? 0.1110 0.1267 0.1453 -0.0083 -0.0044 0.0099  65   SER   A OG  
1527 N  N   . ASP   A 66  ? 0.1125 0.1199 0.1481 -0.0070 0.0154  0.0069  66   ASP   A N   
1528 C  CA  . ASP   A 66  ? 0.1226 0.1319 0.1614 -0.0012 0.0131  0.0175  66   ASP   A CA  
1529 C  C   . ASP   A 66  ? 0.1227 0.1254 0.1626 -0.0054 0.0129  0.0215  66   ASP   A C   
1530 O  O   . ASP   A 66  ? 0.1312 0.1395 0.1780 -0.0042 0.0255  0.0239  66   ASP   A O   
1531 C  CB  . ASP   A 66  ? 0.1310 0.1392 0.1866 0.0038  0.0152  0.0279  66   ASP   A CB  
1532 C  CG  . ASP   A 66  ? 0.1526 0.1511 0.2055 0.0041  -0.0015 0.0415  66   ASP   A CG  
1533 O  OD1 . ASP   A 66  ? 0.1526 0.1813 0.1865 -0.0015 -0.0073 0.0429  66   ASP   A OD1 
1534 O  OD2 . ASP   A 66  ? 0.1701 0.1614 0.2875 0.0209  -0.0191 0.0207  66   ASP   A OD2 
1539 N  N   . ASP   A 67  ? 0.1158 0.1295 0.1739 -0.0044 0.0092  0.0193  67   ASP   A N   
1540 C  CA  . ASP   A 67  ? 0.1159 0.1440 0.1863 -0.0024 -0.0014 0.0313  67   ASP   A CA  
1541 C  C   . ASP   A 67  ? 0.1162 0.1435 0.1844 0.0002  0.0137  0.0305  67   ASP   A C   
1542 O  O   . ASP   A 67  ? 0.1177 0.1533 0.2065 -0.0003 0.0276  0.0338  67   ASP   A O   
1543 C  CB  . ASP   A 67  ? 0.1230 0.1561 0.2173 -0.0034 -0.0152 0.0316  67   ASP   A CB  
1544 C  CG  . ASP   A 67  ? 0.1233 0.1670 0.2548 -0.0067 -0.0330 0.0283  67   ASP   A CG  
1545 O  OD1 . ASP   A 67  ? 0.1316 0.1842 0.3364 -0.0127 -0.0366 0.0422  67   ASP   A OD1 
1546 O  OD2 . ASP   A 67  ? 0.1229 0.1686 0.2364 0.0004  -0.0208 0.0271  67   ASP   A OD2 
1551 N  N   A TYR   A 68  ? 0.1150 0.1326 0.1771 -0.0006 0.0238  0.0298  68   TYR   A N   
1552 N  N   B TYR   A 68  ? 0.1202 0.1378 0.1729 0.0009  0.0106  0.0337  68   TYR   A N   
1553 C  CA  A TYR   A 68  ? 0.1291 0.1243 0.1684 0.0008  0.0340  0.0251  68   TYR   A CA  
1554 C  CA  B TYR   A 68  ? 0.1333 0.1343 0.1621 0.0027  0.0106  0.0317  68   TYR   A CA  
1555 C  C   A TYR   A 68  ? 0.1268 0.1258 0.1736 -0.0025 0.0269  0.0251  68   TYR   A C   
1556 C  C   B TYR   A 68  ? 0.1279 0.1301 0.1652 0.0004  0.0158  0.0234  68   TYR   A C   
1557 O  O   A TYR   A 68  ? 0.1296 0.1330 0.1786 0.0037  0.0334  0.0284  68   TYR   A O   
1558 O  O   B TYR   A 68  ? 0.1312 0.1331 0.1636 0.0064  0.0232  0.0167  68   TYR   A O   
1559 C  CB  A TYR   A 68  ? 0.1328 0.1231 0.1801 0.0062  0.0514  0.0207  68   TYR   A CB  
1560 C  CB  B TYR   A 68  ? 0.1451 0.1389 0.1642 0.0059  0.0081  0.0368  68   TYR   A CB  
1561 C  CG  A TYR   A 68  ? 0.1280 0.1330 0.2070 0.0034  0.0693  0.0215  68   TYR   A CG  
1562 C  CG  B TYR   A 68  ? 0.1523 0.1457 0.1678 0.0083  0.0051  0.0383  68   TYR   A CG  
1563 C  CD1 A TYR   A 68  ? 0.1323 0.1455 0.2468 -0.0208 0.0572  0.0004  68   TYR   A CD1 
1564 C  CD1 B TYR   A 68  ? 0.1569 0.1480 0.1625 0.0070  -0.0037 0.0386  68   TYR   A CD1 
1565 C  CD2 A TYR   A 68  ? 0.1462 0.1380 0.2439 0.0087  0.0693  0.0230  68   TYR   A CD2 
1566 C  CD2 B TYR   A 68  ? 0.1616 0.1447 0.1667 0.0078  -0.0056 0.0375  68   TYR   A CD2 
1567 C  CE1 A TYR   A 68  ? 0.1367 0.1600 0.2897 -0.0232 0.0582  -0.0226 68   TYR   A CE1 
1568 C  CE1 B TYR   A 68  ? 0.1595 0.1410 0.1490 0.0111  -0.0074 0.0554  68   TYR   A CE1 
1569 C  CE2 A TYR   A 68  ? 0.1431 0.1487 0.2794 0.0066  0.0730  0.0007  68   TYR   A CE2 
1570 C  CE2 B TYR   A 68  ? 0.1614 0.1446 0.1494 0.0075  -0.0069 0.0336  68   TYR   A CE2 
1571 C  CZ  A TYR   A 68  ? 0.1375 0.1549 0.3149 -0.0145 0.0614  -0.0371 68   TYR   A CZ  
1572 C  CZ  B TYR   A 68  ? 0.1631 0.1361 0.1301 0.0129  -0.0035 0.0556  68   TYR   A CZ  
1573 O  OH  A TYR   A 68  ? 0.1513 0.1641 0.3668 -0.0133 0.0355  -0.0743 68   TYR   A OH  
1574 O  OH  B TYR   A 68  ? 0.1812 0.1314 0.1347 0.0137  -0.0141 0.0499  68   TYR   A OH  
1593 N  N   . ILE   A 69  ? 0.1199 0.1271 0.1639 0.0011  0.0215  0.0241  69   ILE   A N   
1594 C  CA  . ILE   A 69  ? 0.1278 0.1300 0.1597 0.0041  0.0190  0.0114  69   ILE   A CA  
1595 C  C   . ILE   A 69  ? 0.1327 0.1308 0.1464 0.0042  0.0188  0.0177  69   ILE   A C   
1596 O  O   . ILE   A 69  ? 0.1367 0.1392 0.1449 -0.0012 0.0237  0.0196  69   ILE   A O   
1597 C  CB  . ILE   A 69  ? 0.1349 0.1467 0.1604 0.0036  0.0161  0.0048  69   ILE   A CB  
1598 C  CG1 . ILE   A 69  ? 0.1359 0.1592 0.1652 0.0022  0.0223  -0.0106 69   ILE   A CG1 
1599 C  CG2 . ILE   A 69  ? 0.1533 0.1634 0.1654 0.0091  0.0054  -0.0059 69   ILE   A CG2 
1600 C  CD1 . ILE   A 69  ? 0.1339 0.1651 0.1835 -0.0061 0.0187  -0.0149 69   ILE   A CD1 
1613 N  N   . ALA   A 70  ? 0.1362 0.1310 0.1565 -0.0044 0.0232  0.0161  70   ALA   A N   
1614 C  CA  . ALA   A 70  ? 0.1384 0.1400 0.1752 -0.0131 0.0301  0.0283  70   ALA   A CA  
1615 C  C   . ALA   A 70  ? 0.1326 0.1586 0.1782 -0.0112 0.0311  0.0277  70   ALA   A C   
1616 O  O   . ALA   A 70  ? 0.1512 0.1910 0.1974 0.0037  0.0484  0.0421  70   ALA   A O   
1617 C  CB  . ALA   A 70  ? 0.1402 0.1341 0.2026 -0.0156 0.0301  0.0182  70   ALA   A CB  
1623 N  N   . THR   A 71  ? 0.1253 0.1512 0.1722 -0.0048 0.0230  0.0264  71   THR   A N   
1624 C  CA  . THR   A 71  ? 0.1352 0.1678 0.1969 0.0072  0.0293  0.0303  71   THR   A CA  
1625 C  C   . THR   A 71  ? 0.1307 0.1637 0.2131 0.0134  0.0323  0.0255  71   THR   A C   
1626 O  O   . THR   A 71  ? 0.1364 0.1898 0.2522 0.0119  0.0461  0.0010  71   THR   A O   
1627 C  CB  . THR   A 71  ? 0.1635 0.1946 0.2123 0.0170  -0.0028 0.0370  71   THR   A CB  
1628 O  OG1 . THR   A 71  ? 0.1885 0.2136 0.2181 0.0073  -0.0272 0.0327  71   THR   A OG1 
1629 C  CG2 . THR   A 71  ? 0.1764 0.2085 0.2350 0.0255  -0.0146 0.0426  71   THR   A CG2 
1637 N  N   . ASN   A 72  ? 0.1329 0.1427 0.1928 0.0161  0.0318  0.0227  72   ASN   A N   
1638 C  CA  . ASN   A 72  ? 0.1412 0.1427 0.1947 0.0224  0.0390  0.0289  72   ASN   A CA  
1639 C  C   . ASN   A 72  ? 0.1545 0.1456 0.1914 0.0136  0.0486  0.0196  72   ASN   A C   
1640 O  O   . ASN   A 72  ? 0.1672 0.1437 0.2227 0.0191  0.0428  0.0012  72   ASN   A O   
1641 C  CB  . ASN   A 72  ? 0.1616 0.1479 0.2013 0.0187  0.0393  0.0302  72   ASN   A CB  
1642 C  CG  . ASN   A 72  ? 0.1810 0.1570 0.2029 0.0279  0.0338  0.0303  72   ASN   A CG  
1643 O  OD1 . ASN   A 72  ? 0.2014 0.1915 0.2187 0.0253  0.0432  0.0285  72   ASN   A OD1 
1644 N  ND2 . ASN   A 72  ? 0.1918 0.1591 0.2096 0.0466  0.0095  0.0120  72   ASN   A ND2 
1651 N  N   . GLY   A 73  ? 0.1591 0.1422 0.1751 0.0110  0.0456  0.0164  73   GLY   A N   
1652 C  CA  . GLY   A 73  ? 0.1659 0.1407 0.1619 0.0014  0.0425  0.0123  73   GLY   A CA  
1653 C  C   . GLY   A 73  ? 0.1627 0.1335 0.1493 0.0018  0.0547  0.0244  73   GLY   A C   
1654 O  O   . GLY   A 73  ? 0.1617 0.1415 0.1650 0.0117  0.0424  0.0299  73   GLY   A O   
1658 N  N   . PRO   A 74  ? 0.1679 0.1366 0.1525 -0.0114 0.0458  0.0154  74   PRO   A N   
1659 C  CA  . PRO   A 74  ? 0.1620 0.1372 0.1554 -0.0008 0.0441  0.0164  74   PRO   A CA  
1660 C  C   . PRO   A 74  ? 0.1577 0.1246 0.1541 0.0021  0.0323  0.0023  74   PRO   A C   
1661 O  O   . PRO   A 74  ? 0.1662 0.1266 0.1785 0.0079  0.0317  0.0014  74   PRO   A O   
1662 C  CB  . PRO   A 74  ? 0.1760 0.1669 0.1769 0.0009  0.0450  0.0267  74   PRO   A CB  
1663 C  CG  . PRO   A 74  ? 0.1995 0.1947 0.2191 -0.0155 0.0344  0.0164  74   PRO   A CG  
1664 C  CD  . PRO   A 74  ? 0.1856 0.1741 0.1744 -0.0193 0.0359  0.0058  74   PRO   A CD  
1672 N  N   . LEU   A 75  ? 0.1514 0.1167 0.1420 0.0037  0.0274  0.0085  75   LEU   A N   
1673 C  CA  . LEU   A 75  ? 0.1557 0.1181 0.1341 0.0010  0.0086  0.0051  75   LEU   A CA  
1674 C  C   . LEU   A 75  ? 0.1661 0.1281 0.1347 0.0056  0.0103  0.0137  75   LEU   A C   
1675 O  O   . LEU   A 75  ? 0.2019 0.1435 0.1450 0.0111  0.0059  0.0087  75   LEU   A O   
1676 C  CB  . LEU   A 75  ? 0.1580 0.1242 0.1242 -0.0069 0.0093  0.0113  75   LEU   A CB  
1677 C  CG  . LEU   A 75  ? 0.1717 0.1535 0.1376 -0.0361 0.0052  0.0147  75   LEU   A CG  
1678 C  CD1 . LEU   A 75  ? 0.1804 0.1977 0.1503 -0.0322 -0.0028 -0.0006 75   LEU   A CD1 
1679 C  CD2 . LEU   A 75  ? 0.1964 0.1950 0.1854 -0.0116 0.0050  0.0179  75   LEU   A CD2 
1691 N  N   . LYS   A 76  ? 0.1679 0.1241 0.1457 -0.0069 0.0161  -0.0023 76   LYS   A N   
1692 C  CA  . LYS   A 76  ? 0.1659 0.1475 0.1519 -0.0076 0.0172  -0.0141 76   LYS   A CA  
1693 C  C   . LYS   A 76  ? 0.1604 0.1308 0.1234 -0.0013 0.0181  0.0013  76   LYS   A C   
1694 O  O   . LYS   A 76  ? 0.1601 0.1252 0.1266 -0.0027 0.0207  0.0093  76   LYS   A O   
1695 C  CB  . LYS   A 76  ? 0.1668 0.1716 0.1942 0.0006  0.0219  -0.0337 76   LYS   A CB  
1696 C  CG  . LYS   A 76  ? 0.1702 0.1650 0.2592 0.0031  0.0195  -0.0293 76   LYS   A CG  
1697 C  CD  . LYS   A 76  ? 0.1811 0.1673 0.3033 0.0056  0.0168  -0.0409 76   LYS   A CD  
1698 C  CE  . LYS   A 76  ? 0.1931 0.1867 0.3615 -0.0004 0.0157  -0.0487 76   LYS   A CE  
1699 N  NZ  . LYS   A 76  ? 0.1937 0.1846 0.4047 -0.0143 0.0041  -0.0541 76   LYS   A NZ  
1713 N  N   . VAL   A 77  ? 0.1743 0.1364 0.1144 0.0004  0.0320  0.0064  77   VAL   A N   
1714 C  CA  . VAL   A 77  ? 0.1682 0.1380 0.1236 0.0098  0.0185  0.0089  77   VAL   A CA  
1715 C  C   . VAL   A 77  ? 0.1617 0.1374 0.1159 0.0096  0.0163  0.0019  77   VAL   A C   
1716 O  O   . VAL   A 77  ? 0.1659 0.1357 0.1199 0.0104  0.0274  -0.0040 77   VAL   A O   
1717 C  CB  . VAL   A 77  ? 0.1846 0.1531 0.1380 0.0057  0.0121  0.0181  77   VAL   A CB  
1718 C  CG1 . VAL   A 77  ? 0.1761 0.1680 0.1536 0.0118  -0.0001 0.0086  77   VAL   A CG1 
1719 C  CG2 . VAL   A 77  ? 0.2142 0.1650 0.1604 -0.0008 0.0066  0.0269  77   VAL   A CG2 
1729 N  N   . GLY   A 78  ? 0.1565 0.1287 0.1142 0.0046  0.0240  0.0031  78   GLY   A N   
1730 C  CA  . GLY   A 78  ? 0.1492 0.1237 0.1290 0.0022  0.0244  0.0102  78   GLY   A CA  
1731 C  C   . GLY   A 78  ? 0.1367 0.1226 0.1248 0.0017  0.0251  0.0072  78   GLY   A C   
1732 O  O   . GLY   A 78  ? 0.1388 0.1262 0.1449 0.0033  0.0217  0.0206  78   GLY   A O   
1736 N  N   . GLY   A 79  ? 0.1394 0.1225 0.1233 0.0014  0.0193  0.0132  79   GLY   A N   
1737 C  CA  . GLY   A 79  ? 0.1356 0.1250 0.1357 -0.0003 0.0201  0.0067  79   GLY   A CA  
1738 C  C   . GLY   A 79  ? 0.1265 0.1223 0.1288 0.0023  0.0130  0.0026  79   GLY   A C   
1739 O  O   . GLY   A 79  ? 0.1296 0.1316 0.1371 0.0217  0.0174  0.0056  79   GLY   A O   
1743 N  N   . SER   A 80  ? 0.1245 0.1300 0.1449 -0.0001 0.0196  -0.0018 80   SER   A N   
1744 C  CA  . SER   A 80  ? 0.1192 0.1198 0.1358 -0.0032 0.0106  0.0014  80   SER   A CA  
1745 C  C   . SER   A 80  ? 0.1207 0.1222 0.1376 -0.0068 0.0091  0.0058  80   SER   A C   
1746 O  O   . SER   A 80  ? 0.1185 0.1475 0.1688 0.0064  0.0220  -0.0030 80   SER   A O   
1747 C  CB  . SER   A 80  ? 0.1282 0.1273 0.1744 -0.0073 0.0082  0.0070  80   SER   A CB  
1748 O  OG  . SER   A 80  ? 0.1552 0.1227 0.2060 0.0041  -0.0034 0.0191  80   SER   A OG  
1754 N  N   . CYS   A 81  ? 0.1099 0.1217 0.1367 0.0039  -0.0029 0.0085  81   CYS   A N   
1755 C  CA  . CYS   A 81  ? 0.1121 0.1301 0.1376 0.0009  -0.0014 0.0250  81   CYS   A CA  
1756 C  C   . CYS   A 81  ? 0.1100 0.1260 0.1304 -0.0105 -0.0033 0.0250  81   CYS   A C   
1757 O  O   . CYS   A 81  ? 0.1115 0.1509 0.1459 -0.0035 0.0048  0.0340  81   CYS   A O   
1758 C  CB  . CYS   A 81  ? 0.1241 0.1398 0.1452 -0.0103 -0.0007 0.0255  81   CYS   A CB  
1759 S  SG  . CYS   A 81  ? 0.1349 0.1253 0.1439 -0.0119 0.0032  0.0138  81   CYS   A SG  
1765 N  N   . VAL   A 82  ? 0.1177 0.1344 0.1346 -0.0027 -0.0086 0.0153  82   VAL   A N   
1766 C  CA  . VAL   A 82  ? 0.1293 0.1361 0.1356 0.0011  -0.0069 0.0250  82   VAL   A CA  
1767 C  C   . VAL   A 82  ? 0.1258 0.1372 0.1327 -0.0015 -0.0107 0.0231  82   VAL   A C   
1768 O  O   . VAL   A 82  ? 0.1201 0.1500 0.1647 -0.0005 -0.0055 0.0025  82   VAL   A O   
1769 C  CB  . VAL   A 82  ? 0.1597 0.1503 0.1465 0.0035  -0.0022 0.0258  82   VAL   A CB  
1770 C  CG1 . VAL   A 82  ? 0.1764 0.1619 0.1699 0.0135  0.0022  0.0274  82   VAL   A CG1 
1771 C  CG2 . VAL   A 82  ? 0.1697 0.1556 0.1667 -0.0038 -0.0029 0.0354  82   VAL   A CG2 
1781 N  N   . LEU   A 83  ? 0.1219 0.1318 0.1261 -0.0048 -0.0064 0.0158  83   LEU   A N   
1782 C  CA  . LEU   A 83  ? 0.1234 0.1380 0.1217 -0.0086 -0.0083 0.0106  83   LEU   A CA  
1783 C  C   . LEU   A 83  ? 0.1283 0.1471 0.1153 -0.0076 -0.0123 0.0119  83   LEU   A C   
1784 O  O   . LEU   A 83  ? 0.1386 0.1462 0.1275 -0.0125 -0.0042 0.0192  83   LEU   A O   
1785 C  CB  . LEU   A 83  ? 0.1319 0.1413 0.1295 -0.0105 -0.0037 0.0160  83   LEU   A CB  
1786 C  CG  . LEU   A 83  ? 0.1418 0.1533 0.1313 -0.0110 0.0003  0.0088  83   LEU   A CG  
1787 C  CD1 . LEU   A 83  ? 0.1552 0.1525 0.1409 -0.0243 0.0035  0.0201  83   LEU   A CD1 
1788 C  CD2 . LEU   A 83  ? 0.1408 0.1713 0.1437 -0.0085 0.0138  0.0187  83   LEU   A CD2 
1800 N  N   . SER   A 84  ? 0.1363 0.1519 0.1189 -0.0118 -0.0078 0.0122  84   SER   A N   
1801 C  CA  . SER   A 84  ? 0.1457 0.1545 0.1146 -0.0103 -0.0082 0.0146  84   SER   A CA  
1802 C  C   . SER   A 84  ? 0.1473 0.1509 0.1100 -0.0145 0.0019  0.0115  84   SER   A C   
1803 O  O   . SER   A 84  ? 0.1483 0.1639 0.1104 -0.0118 -0.0039 0.0078  84   SER   A O   
1804 C  CB  . SER   A 84  ? 0.1537 0.1762 0.1241 -0.0081 -0.0111 0.0062  84   SER   A CB  
1805 O  OG  . SER   A 84  ? 0.1640 0.1978 0.1217 -0.0082 -0.0207 -0.0022 84   SER   A OG  
1811 N  N   . GLY   A 85  ? 0.1617 0.1625 0.1189 -0.0187 0.0102  0.0116  85   GLY   A N   
1812 C  CA  . GLY   A 85  ? 0.1689 0.1783 0.1321 -0.0221 0.0164  0.0039  85   GLY   A CA  
1813 C  C   . GLY   A 85  ? 0.1615 0.1824 0.1083 -0.0168 0.0013  0.0043  85   GLY   A C   
1814 O  O   . GLY   A 85  ? 0.1590 0.1917 0.1152 -0.0205 0.0116  -0.0016 85   GLY   A O   
1818 N  N   . HIS   A 86  ? 0.1616 0.1708 0.1017 -0.0137 -0.0032 0.0020  86   HIS   A N   
1819 C  CA  . HIS   A 86  ? 0.1778 0.1776 0.0951 -0.0163 0.0011  0.0013  86   HIS   A CA  
1820 C  C   . HIS   A 86  ? 0.1972 0.1863 0.1013 -0.0123 -0.0064 0.0022  86   HIS   A C   
1821 O  O   . HIS   A 86  ? 0.2061 0.2051 0.1110 -0.0092 -0.0009 0.0068  86   HIS   A O   
1822 C  CB  . HIS   A 86  ? 0.1757 0.1703 0.1063 -0.0136 0.0046  0.0033  86   HIS   A CB  
1823 C  CG  . HIS   A 86  ? 0.1703 0.1646 0.1116 -0.0049 0.0032  0.0104  86   HIS   A CG  
1824 N  ND1 . HIS   A 86  ? 0.1766 0.1649 0.1470 -0.0168 0.0007  0.0128  86   HIS   A ND1 
1825 C  CD2 . HIS   A 86  ? 0.1755 0.1611 0.1072 0.0033  0.0089  0.0112  86   HIS   A CD2 
1826 C  CE1 . HIS   A 86  ? 0.1765 0.1647 0.1415 -0.0120 0.0169  0.0169  86   HIS   A CE1 
1827 N  NE2 . HIS   A 86  ? 0.1782 0.1569 0.1251 0.0032  0.0144  0.0227  86   HIS   A NE2 
1835 N  N   . ASN   A 87  ? 0.2050 0.1980 0.1120 -0.0105 0.0123  -0.0006 87   ASN   A N   
1836 C  CA  . ASN   A 87  ? 0.2223 0.2095 0.1243 -0.0106 0.0370  -0.0054 87   ASN   A CA  
1837 C  C   . ASN   A 87  ? 0.2195 0.2242 0.1421 -0.0145 0.0555  0.0059  87   ASN   A C   
1838 O  O   . ASN   A 87  ? 0.2450 0.2412 0.1868 -0.0238 0.0779  -0.0033 87   ASN   A O   
1839 C  CB  . ASN   A 87  ? 0.2394 0.2170 0.1277 -0.0029 0.0426  -0.0046 87   ASN   A CB  
1840 C  CG  . ASN   A 87  ? 0.2472 0.2237 0.1431 0.0075  0.0529  0.0032  87   ASN   A CG  
1841 O  OD1 . ASN   A 87  ? 0.2658 0.2230 0.1449 0.0247  0.0509  0.0146  87   ASN   A OD1 
1842 N  ND2 . ASN   A 87  ? 0.2495 0.2443 0.1599 0.0088  0.0469  0.0061  87   ASN   A ND2 
1849 N  N   . LEU   A 88  ? 0.1955 0.2200 0.1434 -0.0197 0.0291  0.0270  88   LEU   A N   
1850 C  CA  . LEU   A 88  ? 0.1812 0.2164 0.1604 -0.0284 0.0214  0.0346  88   LEU   A CA  
1851 C  C   . LEU   A 88  ? 0.1787 0.2160 0.1556 -0.0292 0.0164  0.0388  88   LEU   A C   
1852 O  O   . LEU   A 88  ? 0.1785 0.2199 0.1867 -0.0249 0.0173  0.0596  88   LEU   A O   
1853 C  CB  . LEU   A 88  ? 0.1826 0.2235 0.1744 -0.0338 -0.0075 0.0443  88   LEU   A CB  
1854 C  CG  . LEU   A 88  ? 0.1994 0.2320 0.2066 -0.0346 -0.0205 0.0423  88   LEU   A CG  
1855 C  CD1 . LEU   A 88  ? 0.2116 0.2360 0.2024 -0.0368 -0.0206 0.0312  88   LEU   A CD1 
1856 C  CD2 . LEU   A 88  ? 0.2160 0.2411 0.2454 -0.0253 -0.0197 0.0327  88   LEU   A CD2 
1868 N  N   . ALA   A 89  ? 0.1820 0.2061 0.1340 -0.0286 0.0153  0.0161  89   ALA   A N   
1869 C  CA  . ALA   A 89  ? 0.1907 0.1997 0.1075 -0.0273 0.0074  0.0226  89   ALA   A CA  
1870 C  C   . ALA   A 89  ? 0.1971 0.2046 0.1108 -0.0193 -0.0100 0.0147  89   ALA   A C   
1871 O  O   . ALA   A 89  ? 0.1932 0.2010 0.1494 -0.0241 -0.0163 -0.0019 89   ALA   A O   
1872 C  CB  . ALA   A 89  ? 0.1837 0.1951 0.1006 -0.0254 0.0018  0.0246  89   ALA   A CB  
1878 N  N   . LYS   A 90  ? 0.2057 0.2161 0.1184 -0.0215 -0.0225 0.0229  90   LYS   A N   
1879 C  CA  . LYS   A 90  ? 0.2136 0.2275 0.1282 -0.0171 -0.0309 0.0235  90   LYS   A CA  
1880 C  C   . LYS   A 90  ? 0.1853 0.2093 0.1269 -0.0172 -0.0267 0.0137  90   LYS   A C   
1881 O  O   . LYS   A 90  ? 0.1870 0.2213 0.1456 -0.0220 -0.0292 0.0042  90   LYS   A O   
1882 C  CB  . LYS   A 90  ? 0.2399 0.2570 0.1610 -0.0086 -0.0364 0.0431  90   LYS   A CB  
1883 C  CG  . LYS   A 90  ? 0.2698 0.2829 0.2550 -0.0034 -0.0345 0.0535  90   LYS   A CG  
1884 C  CD  . LYS   A 90  ? 0.3081 0.3137 0.3546 -0.0029 -0.0196 0.0585  90   LYS   A CD  
1885 C  CE  . LYS   A 90  ? 0.3337 0.3422 0.4276 -0.0049 -0.0045 0.0519  90   LYS   A CE  
1886 N  NZ  . LYS   A 90  ? 0.3444 0.3508 0.4760 -0.0072 0.0026  0.0418  90   LYS   A NZ  
1900 N  N   . HIS   A 91  ? 0.1719 0.1840 0.1003 -0.0177 -0.0261 0.0183  91   HIS   A N   
1901 C  CA  . HIS   A 91  ? 0.1639 0.1722 0.1100 -0.0167 -0.0245 0.0239  91   HIS   A CA  
1902 C  C   . HIS   A 91  ? 0.1472 0.1581 0.1035 -0.0186 -0.0165 0.0259  91   HIS   A C   
1903 O  O   . HIS   A 91  ? 0.1477 0.1688 0.1099 -0.0198 -0.0059 0.0287  91   HIS   A O   
1904 C  CB  . HIS   A 91  ? 0.1784 0.1976 0.1582 0.0046  -0.0429 0.0194  91   HIS   A CB  
1905 C  CG  . HIS   A 91  ? 0.2164 0.2428 0.2296 0.0166  -0.0709 0.0129  91   HIS   A CG  
1906 N  ND1 . HIS   A 91  ? 0.2249 0.2696 0.2715 0.0186  -0.0743 -0.0080 91   HIS   A ND1 
1907 C  CD2 . HIS   A 91  ? 0.2408 0.2620 0.2536 0.0240  -0.0802 0.0202  91   HIS   A CD2 
1908 C  CE1 . HIS   A 91  ? 0.2353 0.2769 0.2800 0.0244  -0.0784 0.0016  91   HIS   A CE1 
1909 N  NE2 . HIS   A 91  ? 0.2509 0.2778 0.2802 0.0285  -0.0803 0.0108  91   HIS   A NE2 
1917 N  N   . CYS   A 92  ? 0.1367 0.1500 0.1029 -0.0190 -0.0114 0.0214  92   CYS   A N   
1918 C  CA  . CYS   A 92  ? 0.1281 0.1407 0.1157 -0.0132 -0.0025 0.0123  92   CYS   A CA  
1919 C  C   . CYS   A 92  ? 0.1214 0.1372 0.0985 -0.0114 0.0000  0.0189  92   CYS   A C   
1920 O  O   . CYS   A 92  ? 0.1267 0.1399 0.1220 -0.0154 -0.0040 0.0134  92   CYS   A O   
1921 C  CB  . CYS   A 92  ? 0.1298 0.1432 0.1239 -0.0040 -0.0006 0.0142  92   CYS   A CB  
1922 S  SG  . CYS   A 92  ? 0.1282 0.1287 0.1194 -0.0126 -0.0020 0.0132  92   CYS   A SG  
1928 N  N   . LEU   A 93  ? 0.1174 0.1239 0.1113 -0.0103 0.0078  0.0178  93   LEU   A N   
1929 C  CA  . LEU   A 93  ? 0.1139 0.1191 0.1113 -0.0043 0.0081  0.0138  93   LEU   A CA  
1930 C  C   . LEU   A 93  ? 0.1128 0.1120 0.1106 -0.0023 0.0070  0.0108  93   LEU   A C   
1931 O  O   . LEU   A 93  ? 0.1094 0.1234 0.1108 -0.0017 0.0036  0.0122  93   LEU   A O   
1932 C  CB  . LEU   A 93  ? 0.1221 0.1215 0.1268 -0.0002 0.0035  0.0234  93   LEU   A CB  
1933 C  CG  . LEU   A 93  ? 0.1269 0.1228 0.1228 -0.0047 0.0028  0.0235  93   LEU   A CG  
1934 C  CD1 . LEU   A 93  ? 0.1350 0.1288 0.1518 -0.0030 0.0085  0.0217  93   LEU   A CD1 
1935 C  CD2 . LEU   A 93  ? 0.1386 0.1233 0.1449 -0.0034 0.0015  0.0114  93   LEU   A CD2 
1947 N  N   . HIS   A 94  ? 0.1070 0.1123 0.1113 -0.0016 0.0074  0.0172  94   HIS   A N   
1948 C  CA  . HIS   A 94  ? 0.1078 0.1110 0.1111 -0.0085 0.0038  0.0165  94   HIS   A CA  
1949 C  C   . HIS   A 94  ? 0.1042 0.1105 0.1160 -0.0063 0.0049  0.0114  94   HIS   A C   
1950 O  O   . HIS   A 94  ? 0.1058 0.1343 0.1499 0.0002  0.0057  -0.0044 94   HIS   A O   
1951 C  CB  . HIS   A 94  ? 0.1096 0.1134 0.1176 -0.0009 0.0006  0.0154  94   HIS   A CB  
1952 C  CG  . HIS   A 94  ? 0.1105 0.1165 0.1114 -0.0024 -0.0031 0.0177  94   HIS   A CG  
1953 N  ND1 . HIS   A 94  ? 0.1121 0.1076 0.1161 -0.0064 0.0017  0.0150  94   HIS   A ND1 
1954 C  CD2 . HIS   A 94  ? 0.1143 0.1212 0.1133 -0.0026 -0.0058 0.0088  94   HIS   A CD2 
1955 C  CE1 . HIS   A 94  ? 0.1192 0.1183 0.1084 -0.0089 -0.0052 0.0053  94   HIS   A CE1 
1956 N  NE2 . HIS   A 94  ? 0.1202 0.1199 0.1194 -0.0075 -0.0082 0.0083  94   HIS   A NE2 
1964 N  N   . VAL   A 95  ? 0.1020 0.1051 0.1035 -0.0049 0.0106  0.0081  95   VAL   A N   
1965 C  CA  . VAL   A 95  ? 0.1137 0.1099 0.1085 -0.0021 0.0114  0.0135  95   VAL   A CA  
1966 C  C   . VAL   A 95  ? 0.1142 0.1099 0.0957 -0.0116 0.0048  0.0083  95   VAL   A C   
1967 O  O   . VAL   A 95  ? 0.1219 0.1217 0.1065 0.0038  0.0073  0.0076  95   VAL   A O   
1968 C  CB  . VAL   A 95  ? 0.1178 0.1120 0.1171 -0.0141 0.0055  0.0112  95   VAL   A CB  
1969 C  CG1 . VAL   A 95  ? 0.1357 0.1155 0.1303 -0.0172 0.0069  0.0012  95   VAL   A CG1 
1970 C  CG2 . VAL   A 95  ? 0.1237 0.1137 0.1235 -0.0153 0.0081  0.0149  95   VAL   A CG2 
1980 N  N   . VAL   A 96  ? 0.1189 0.1129 0.0964 -0.0044 0.0063  0.0101  96   VAL   A N   
1981 C  CA  . VAL   A 96  ? 0.1281 0.1107 0.1110 0.0009  0.0116  0.0145  96   VAL   A CA  
1982 C  C   . VAL   A 96  ? 0.1295 0.1207 0.1072 0.0004  0.0121  0.0148  96   VAL   A C   
1983 O  O   . VAL   A 96  ? 0.1400 0.1253 0.1299 -0.0035 0.0184  -0.0030 96   VAL   A O   
1984 C  CB  . VAL   A 96  ? 0.1321 0.1191 0.1158 0.0003  0.0203  0.0138  96   VAL   A CB  
1985 C  CG1 . VAL   A 96  ? 0.1342 0.1243 0.1129 0.0003  0.0158  0.0124  96   VAL   A CG1 
1986 C  CG2 . VAL   A 96  ? 0.1313 0.1256 0.1301 -0.0093 0.0164  0.0146  96   VAL   A CG2 
1996 N  N   . GLY   A 97  ? 0.1262 0.1237 0.1132 -0.0067 0.0076  0.0092  97   GLY   A N   
1997 C  CA  . GLY   A 97  ? 0.1360 0.1384 0.1081 -0.0046 0.0027  0.0112  97   GLY   A CA  
1998 C  C   . GLY   A 97  ? 0.1404 0.1504 0.0942 -0.0013 0.0070  0.0106  97   GLY   A C   
1999 O  O   . GLY   A 97  ? 0.1547 0.1545 0.1203 -0.0071 0.0041  0.0237  97   GLY   A O   
2003 N  N   A PRO   A 98  ? 0.1461 0.1626 0.0904 0.0029  -0.0031 0.0122  98   PRO   A N   
2004 N  N   B PRO   A 98  ? 0.1528 0.1492 0.1053 0.0017  0.0082  0.0182  98   PRO   A N   
2005 C  CA  A PRO   A 98  ? 0.1550 0.1843 0.0876 0.0062  -0.0006 0.0029  98   PRO   A CA  
2006 C  CA  B PRO   A 98  ? 0.1703 0.1592 0.1168 0.0005  0.0072  0.0129  98   PRO   A CA  
2007 C  C   A PRO   A 98  ? 0.1522 0.1847 0.0789 -0.0020 0.0020  0.0114  98   PRO   A C   
2008 C  C   B PRO   A 98  ? 0.1961 0.1535 0.1154 -0.0083 0.0051  0.0283  98   PRO   A C   
2009 O  O   A PRO   A 98  ? 0.1400 0.1682 0.1000 0.0009  -0.0020 0.0148  98   PRO   A O   
2010 O  O   B PRO   A 98  ? 0.1921 0.1450 0.1397 -0.0095 0.0069  0.0224  98   PRO   A O   
2011 C  CB  A PRO   A 98  ? 0.1620 0.1924 0.0804 0.0150  -0.0173 -0.0050 98   PRO   A CB  
2012 C  CB  B PRO   A 98  ? 0.1665 0.1593 0.1137 0.0136  -0.0013 0.0073  98   PRO   A CB  
2013 C  CG  A PRO   A 98  ? 0.1622 0.1813 0.0954 0.0144  -0.0180 -0.0101 98   PRO   A CG  
2014 C  CG  B PRO   A 98  ? 0.1700 0.1539 0.1264 0.0117  -0.0005 0.0064  98   PRO   A CG  
2015 C  CD  A PRO   A 98  ? 0.1525 0.1658 0.0937 0.0120  -0.0106 0.0085  98   PRO   A CD  
2016 C  CD  B PRO   A 98  ? 0.1586 0.1451 0.1098 0.0102  0.0031  0.0176  98   PRO   A CD  
2031 N  N   A ASN   A 99  ? 0.1593 0.2065 0.0914 -0.0045 0.0056  0.0238  99   ASN   A N   
2032 N  N   B ASN   A 99  ? 0.2260 0.1551 0.1026 -0.0072 0.0021  0.0383  99   ASN   A N   
2033 C  CA  A ASN   A 99  ? 0.1736 0.2161 0.0886 -0.0096 -0.0001 0.0311  99   ASN   A CA  
2034 C  CA  B ASN   A 99  ? 0.2539 0.1573 0.1042 -0.0018 -0.0105 0.0434  99   ASN   A CA  
2035 C  C   A ASN   A 99  ? 0.1902 0.2329 0.0855 -0.0241 0.0060  0.0371  99   ASN   A C   
2036 C  C   B ASN   A 99  ? 0.2725 0.1601 0.1218 -0.0011 -0.0179 0.0296  99   ASN   A C   
2037 O  O   A ASN   A 99  ? 0.1984 0.2446 0.0912 -0.0165 -0.0010 0.0283  99   ASN   A O   
2038 O  O   B ASN   A 99  ? 0.2713 0.1442 0.1180 0.0019  -0.0185 0.0104  99   ASN   A O   
2039 C  CB  A ASN   A 99  ? 0.1703 0.2099 0.0835 -0.0133 -0.0046 0.0339  99   ASN   A CB  
2040 C  CB  B ASN   A 99  ? 0.2610 0.1627 0.1177 0.0008  -0.0199 0.0456  99   ASN   A CB  
2041 C  CG  A ASN   A 99  ? 0.1754 0.2037 0.0933 -0.0102 -0.0160 0.0196  99   ASN   A CG  
2042 C  CG  B ASN   A 99  ? 0.2687 0.1717 0.1391 0.0036  -0.0221 0.0446  99   ASN   A CG  
2043 O  OD1 A ASN   A 99  ? 0.1808 0.2110 0.0986 0.0048  -0.0119 0.0160  99   ASN   A OD1 
2044 O  OD1 B ASN   A 99  ? 0.2775 0.1811 0.1388 0.0004  -0.0233 0.0461  99   ASN   A OD1 
2045 N  ND2 A ASN   A 99  ? 0.1811 0.2017 0.1070 -0.0108 -0.0286 0.0194  99   ASN   A ND2 
2046 N  ND2 B ASN   A 99  ? 0.2680 0.1781 0.1576 0.0137  -0.0277 0.0244  99   ASN   A ND2 
2059 N  N   A VAL   A 100 ? 0.2059 0.2382 0.0895 -0.0427 -0.0220 0.0383  100  VAL   A N   
2060 N  N   B VAL   A 100 ? 0.2907 0.1850 0.1511 -0.0042 -0.0310 0.0304  100  VAL   A N   
2061 C  CA  A VAL   A 100 ? 0.2289 0.2518 0.1207 -0.0482 -0.0364 0.0457  100  VAL   A CA  
2062 C  CA  B VAL   A 100 ? 0.3062 0.2003 0.1788 -0.0087 -0.0367 0.0351  100  VAL   A CA  
2063 C  C   A VAL   A 100 ? 0.2334 0.2649 0.1130 -0.0567 -0.0485 0.0639  100  VAL   A C   
2064 C  C   B VAL   A 100 ? 0.3199 0.2087 0.1879 -0.0085 -0.0403 0.0351  100  VAL   A C   
2065 O  O   A VAL   A 100 ? 0.2432 0.2773 0.1126 -0.0556 -0.0275 0.0635  100  VAL   A O   
2066 O  O   B VAL   A 100 ? 0.3236 0.2045 0.1770 -0.0099 -0.0364 0.0269  100  VAL   A O   
2067 C  CB  A VAL   A 100 ? 0.2460 0.2448 0.1669 -0.0532 -0.0465 0.0442  100  VAL   A CB  
2068 C  CB  B VAL   A 100 ? 0.3080 0.2128 0.1933 -0.0083 -0.0455 0.0378  100  VAL   A CB  
2069 C  CG1 A VAL   A 100 ? 0.2476 0.2482 0.1903 -0.0598 -0.0403 0.0412  100  VAL   A CG1 
2070 C  CG1 B VAL   A 100 ? 0.3092 0.2164 0.2082 -0.0072 -0.0457 0.0368  100  VAL   A CG1 
2071 C  CG2 A VAL   A 100 ? 0.2595 0.2439 0.1833 -0.0528 -0.0485 0.0438  100  VAL   A CG2 
2072 C  CG2 B VAL   A 100 ? 0.3083 0.2178 0.1993 -0.0091 -0.0466 0.0371  100  VAL   A CG2 
2091 N  N   A ASN   A 101 ? 0.2402 0.2719 0.1416 -0.0674 -0.0611 0.0861  101  ASN   A N   
2092 N  N   B ASN   A 101 ? 0.3273 0.2235 0.2085 -0.0074 -0.0464 0.0457  101  ASN   A N   
2093 C  CA  A ASN   A 101 ? 0.2676 0.2839 0.1619 -0.0720 -0.0652 0.1007  101  ASN   A CA  
2094 C  CA  B ASN   A 101 ? 0.3345 0.2414 0.2286 -0.0080 -0.0454 0.0497  101  ASN   A CA  
2095 C  C   A ASN   A 101 ? 0.2908 0.3152 0.1865 -0.0809 -0.0288 0.1220  101  ASN   A C   
2096 C  C   B ASN   A 101 ? 0.3473 0.2604 0.2404 -0.0128 -0.0236 0.0560  101  ASN   A C   
2097 O  O   A ASN   A 101 ? 0.3090 0.3204 0.2288 -0.0760 -0.0202 0.1158  101  ASN   A O   
2098 O  O   B ASN   A 101 ? 0.3515 0.2635 0.2374 -0.0089 -0.0196 0.0656  101  ASN   A O   
2099 C  CB  A ASN   A 101 ? 0.2771 0.2685 0.1643 -0.0633 -0.0883 0.0858  101  ASN   A CB  
2100 C  CB  B ASN   A 101 ? 0.3289 0.2425 0.2337 -0.0060 -0.0581 0.0476  101  ASN   A CB  
2101 C  CG  A ASN   A 101 ? 0.2892 0.2551 0.1657 -0.0570 -0.0994 0.0602  101  ASN   A CG  
2102 C  CG  B ASN   A 101 ? 0.3247 0.2483 0.2435 -0.0062 -0.0636 0.0438  101  ASN   A CG  
2103 O  OD1 A ASN   A 101 ? 0.2917 0.2675 0.1844 -0.0482 -0.1008 0.0257  101  ASN   A OD1 
2104 O  OD1 B ASN   A 101 ? 0.3206 0.2475 0.2473 -0.0079 -0.0630 0.0348  101  ASN   A OD1 
2105 N  ND2 A ASN   A 101 ? 0.2957 0.2363 0.1629 -0.0609 -0.0942 0.0618  101  ASN   A ND2 
2106 N  ND2 B ASN   A 101 ? 0.3244 0.2512 0.2539 -0.0076 -0.0597 0.0405  101  ASN   A ND2 
2119 N  N   A LYS   A 102 ? 0.2911 0.3463 0.2042 -0.0923 -0.0219 0.1211  102  LYS   A N   
2120 N  N   B LYS   A 102 ? 0.3553 0.2797 0.2560 -0.0248 -0.0070 0.0430  102  LYS   A N   
2121 C  CA  A LYS   A 102 ? 0.2987 0.3765 0.2244 -0.0902 -0.0276 0.1033  102  LYS   A CA  
2122 C  CA  B LYS   A 102 ? 0.3615 0.2967 0.2554 -0.0321 0.0093  0.0430  102  LYS   A CA  
2123 C  C   A LYS   A 102 ? 0.3038 0.3941 0.2110 -0.0829 -0.0244 0.0921  102  LYS   A C   
2124 C  C   B LYS   A 102 ? 0.3578 0.2974 0.2259 -0.0374 0.0102  0.0579  102  LYS   A C   
2125 O  O   A LYS   A 102 ? 0.3072 0.4037 0.2185 -0.0812 -0.0159 0.0869  102  LYS   A O   
2126 O  O   B LYS   A 102 ? 0.3602 0.2957 0.2142 -0.0426 0.0140  0.0687  102  LYS   A O   
2127 C  CB  A LYS   A 102 ? 0.3057 0.3877 0.2606 -0.0915 -0.0409 0.0870  102  LYS   A CB  
2128 C  CB  B LYS   A 102 ? 0.3704 0.3121 0.2943 -0.0391 0.0221  0.0236  102  LYS   A CB  
2129 C  CG  A LYS   A 102 ? 0.3136 0.3973 0.2985 -0.0903 -0.0548 0.0647  102  LYS   A CG  
2130 C  CG  B LYS   A 102 ? 0.3785 0.3252 0.3318 -0.0445 0.0290  0.0087  102  LYS   A CG  
2131 C  CD  A LYS   A 102 ? 0.3212 0.4058 0.3274 -0.0878 -0.0680 0.0440  102  LYS   A CD  
2132 C  CD  B LYS   A 102 ? 0.3858 0.3383 0.3675 -0.0462 0.0292  -0.0038 102  LYS   A CD  
2133 C  CE  A LYS   A 102 ? 0.3294 0.4122 0.3538 -0.0842 -0.0730 0.0312  102  LYS   A CE  
2134 C  CE  B LYS   A 102 ? 0.3916 0.3483 0.3946 -0.0468 0.0289  -0.0145 102  LYS   A CE  
2135 N  NZ  A LYS   A 102 ? 0.3337 0.4141 0.3625 -0.0850 -0.0763 0.0221  102  LYS   A NZ  
2136 N  NZ  B LYS   A 102 ? 0.3951 0.3539 0.4086 -0.0464 0.0289  -0.0187 102  LYS   A NZ  
2163 N  N   A GLY   A 103 ? 0.3061 0.4042 0.2057 -0.0730 -0.0248 0.0735  103  GLY   A N   
2164 N  N   B GLY   A 103 ? 0.3511 0.2980 0.2083 -0.0377 0.0028  0.0563  103  GLY   A N   
2165 C  CA  A GLY   A 103 ? 0.3100 0.4105 0.1978 -0.0604 -0.0190 0.0552  103  GLY   A CA  
2166 C  CA  B GLY   A 103 ? 0.3423 0.2952 0.1865 -0.0400 0.0008  0.0552  103  GLY   A CA  
2167 C  C   A GLY   A 103 ? 0.3104 0.4158 0.1950 -0.0513 -0.0077 0.0353  103  GLY   A C   
2168 C  C   B GLY   A 103 ? 0.3341 0.2904 0.1618 -0.0399 -0.0030 0.0529  103  GLY   A C   
2169 O  O   A GLY   A 103 ? 0.3179 0.4210 0.2160 -0.0501 -0.0057 0.0252  103  GLY   A O   
2170 O  O   B GLY   A 103 ? 0.3350 0.2922 0.1572 -0.0411 -0.0007 0.0577  103  GLY   A O   
2177 N  N   A GLU   A 104 ? 0.2984 0.4119 0.1610 -0.0480 0.0015  0.0246  104  GLU   A N   
2178 N  N   B GLU   A 104 ? 0.3261 0.2821 0.1542 -0.0362 -0.0090 0.0421  104  GLU   A N   
2179 C  CA  A GLU   A 104 ? 0.2806 0.4054 0.1387 -0.0493 0.0053  0.0144  104  GLU   A CA  
2180 C  CA  B GLU   A 104 ? 0.3146 0.2707 0.1442 -0.0333 -0.0142 0.0348  104  GLU   A CA  
2181 C  C   A GLU   A 104 ? 0.2849 0.4172 0.1591 -0.0454 0.0065  -0.0051 104  GLU   A C   
2182 C  C   B GLU   A 104 ? 0.2949 0.2596 0.1413 -0.0239 -0.0110 0.0217  104  GLU   A C   
2183 O  O   A GLU   A 104 ? 0.2814 0.4178 0.1817 -0.0492 0.0010  -0.0177 104  GLU   A O   
2184 O  O   B GLU   A 104 ? 0.2917 0.2557 0.1624 -0.0226 -0.0123 0.0299  104  GLU   A O   
2185 C  CB  A GLU   A 104 ? 0.2551 0.3846 0.1159 -0.0539 0.0115  0.0324  104  GLU   A CB  
2186 C  CB  B GLU   A 104 ? 0.3202 0.2730 0.1553 -0.0363 -0.0175 0.0446  104  GLU   A CB  
2187 C  CG  A GLU   A 104 ? 0.2333 0.3601 0.1203 -0.0551 0.0071  0.0482  104  GLU   A CG  
2188 C  CG  B GLU   A 104 ? 0.3289 0.2815 0.1834 -0.0371 -0.0211 0.0486  104  GLU   A CG  
2189 C  CD  A GLU   A 104 ? 0.2092 0.3351 0.1151 -0.0551 0.0086  0.0652  104  GLU   A CD  
2190 C  CD  B GLU   A 104 ? 0.3356 0.2899 0.2040 -0.0378 -0.0205 0.0492  104  GLU   A CD  
2191 O  OE1 A GLU   A 104 ? 0.1944 0.3074 0.1040 -0.0471 0.0115  0.0571  104  GLU   A OE1 
2192 O  OE1 B GLU   A 104 ? 0.3394 0.2943 0.2109 -0.0365 -0.0197 0.0545  104  GLU   A OE1 
2193 O  OE2 A GLU   A 104 ? 0.2086 0.3298 0.1318 -0.0575 0.0120  0.0815  104  GLU   A OE2 
2194 O  OE2 B GLU   A 104 ? 0.3385 0.2925 0.2170 -0.0385 -0.0224 0.0458  104  GLU   A OE2 
2207 N  N   A ASP   A 105 ? 0.2924 0.4285 0.1803 -0.0369 0.0129  -0.0159 105  ASP   A N   
2208 N  N   B ASP   A 105 ? 0.2802 0.2526 0.1408 -0.0182 -0.0034 0.0023  105  ASP   A N   
2209 C  CA  A ASP   A 105 ? 0.2924 0.4356 0.2142 -0.0312 0.0181  -0.0343 105  ASP   A CA  
2210 C  CA  B ASP   A 105 ? 0.2639 0.2483 0.1615 -0.0087 0.0019  -0.0267 105  ASP   A CA  
2211 C  C   A ASP   A 105 ? 0.2619 0.4238 0.1970 -0.0391 0.0109  -0.0521 105  ASP   A C   
2212 C  C   B ASP   A 105 ? 0.2455 0.2348 0.1444 -0.0161 0.0049  -0.0281 105  ASP   A C   
2213 O  O   A ASP   A 105 ? 0.2492 0.4227 0.1579 -0.0416 0.0118  -0.0660 105  ASP   A O   
2214 O  O   B ASP   A 105 ? 0.2277 0.2289 0.1058 -0.0222 0.0016  -0.0388 105  ASP   A O   
2215 C  CB  A ASP   A 105 ? 0.3173 0.4506 0.2682 -0.0182 0.0263  -0.0356 105  ASP   A CB  
2216 C  CB  B ASP   A 105 ? 0.2649 0.2610 0.2018 0.0072  0.0005  -0.0443 105  ASP   A CB  
2217 C  CG  A ASP   A 105 ? 0.3381 0.4629 0.3180 -0.0073 0.0261  -0.0386 105  ASP   A CG  
2218 C  CG  B ASP   A 105 ? 0.2656 0.2703 0.2350 0.0205  -0.0043 -0.0625 105  ASP   A CG  
2219 O  OD1 A ASP   A 105 ? 0.3446 0.4681 0.3242 -0.0045 0.0265  -0.0463 105  ASP   A OD1 
2220 O  OD1 B ASP   A 105 ? 0.2669 0.2718 0.2365 0.0236  -0.0053 -0.0724 105  ASP   A OD1 
2221 O  OD2 A ASP   A 105 ? 0.3471 0.4679 0.3469 -0.0029 0.0261  -0.0338 105  ASP   A OD2 
2222 O  OD2 B ASP   A 105 ? 0.2649 0.2750 0.2610 0.0241  -0.0128 -0.0576 105  ASP   A OD2 
2231 N  N   A ILE   A 106 ? 0.2413 0.4091 0.2183 -0.0483 -0.0129 -0.0613 106  ILE   A N   
2232 N  N   B ILE   A 106 ? 0.2436 0.2327 0.1697 -0.0127 -0.0023 -0.0178 106  ILE   A N   
2233 C  CA  A ILE   A 106 ? 0.2100 0.3886 0.2358 -0.0591 -0.0282 -0.0792 106  ILE   A CA  
2234 C  CA  B ILE   A 106 ? 0.2393 0.2330 0.1944 -0.0163 -0.0064 -0.0121 106  ILE   A CA  
2235 C  C   A ILE   A 106 ? 0.1849 0.3606 0.2385 -0.0764 -0.0266 -0.1069 106  ILE   A C   
2236 C  C   B ILE   A 106 ? 0.2418 0.2276 0.2007 -0.0135 -0.0016 0.0131  106  ILE   A C   
2237 O  O   A ILE   A 106 ? 0.1610 0.3526 0.2423 -0.0776 -0.0045 -0.1163 106  ILE   A O   
2238 O  O   B ILE   A 106 ? 0.2377 0.2312 0.2056 -0.0143 0.0042  0.0158  106  ILE   A O   
2239 C  CB  A ILE   A 106 ? 0.2161 0.3953 0.2764 -0.0459 -0.0358 -0.0588 106  ILE   A CB  
2240 C  CB  B ILE   A 106 ? 0.2373 0.2449 0.2289 -0.0222 -0.0235 -0.0220 106  ILE   A CB  
2241 C  CG1 A ILE   A 106 ? 0.2166 0.3949 0.2979 -0.0359 -0.0379 -0.0465 106  ILE   A CG1 
2242 C  CG1 B ILE   A 106 ? 0.2293 0.2498 0.2397 -0.0237 -0.0339 -0.0271 106  ILE   A CG1 
2243 C  CG2 A ILE   A 106 ? 0.2203 0.3985 0.2871 -0.0433 -0.0432 -0.0565 106  ILE   A CG2 
2244 C  CG2 B ILE   A 106 ? 0.2414 0.2502 0.2388 -0.0237 -0.0260 -0.0268 106  ILE   A CG2 
2245 C  CD1 A ILE   A 106 ? 0.2180 0.3922 0.3096 -0.0270 -0.0301 -0.0387 106  ILE   A CD1 
2246 C  CD1 B ILE   A 106 ? 0.2220 0.2522 0.2442 -0.0263 -0.0340 -0.0300 106  ILE   A CD1 
2269 N  N   A GLN   A 107 ? 0.1997 0.3405 0.2647 -0.0794 -0.0166 -0.1176 107  GLN   A N   
2270 N  N   B GLN   A 107 ? 0.2496 0.2151 0.2173 -0.0048 -0.0048 0.0308  107  GLN   A N   
2271 C  CA  A GLN   A 107 ? 0.2179 0.3155 0.3158 -0.0643 0.0106  -0.1133 107  GLN   A CA  
2272 C  CA  B GLN   A 107 ? 0.2624 0.2163 0.2543 -0.0043 -0.0014 0.0400  107  GLN   A CA  
2273 C  C   A GLN   A 107 ? 0.1948 0.2665 0.3032 -0.0567 0.0333  -0.0979 107  GLN   A C   
2274 C  C   B GLN   A 107 ? 0.2427 0.1891 0.2316 -0.0002 0.0024  0.0587  107  GLN   A C   
2275 O  O   A GLN   A 107 ? 0.2020 0.2594 0.3591 -0.0445 0.0489  -0.0868 107  GLN   A O   
2276 O  O   B GLN   A 107 ? 0.2435 0.1830 0.2360 0.0029  -0.0113 0.0684  107  GLN   A O   
2277 C  CB  A GLN   A 107 ? 0.2518 0.3350 0.3900 -0.0641 0.0075  -0.1077 107  GLN   A CB  
2278 C  CB  B GLN   A 107 ? 0.2906 0.2505 0.3103 -0.0094 -0.0096 0.0323  107  GLN   A CB  
2279 C  CG  A GLN   A 107 ? 0.2843 0.3565 0.4654 -0.0610 0.0004  -0.0965 107  GLN   A CG  
2280 C  CG  B GLN   A 107 ? 0.3143 0.2786 0.3649 -0.0125 -0.0211 0.0338  107  GLN   A CG  
2281 C  CD  A GLN   A 107 ? 0.3097 0.3714 0.5288 -0.0601 -0.0048 -0.0849 107  GLN   A CD  
2282 C  CD  B GLN   A 107 ? 0.3349 0.3040 0.4113 -0.0135 -0.0279 0.0382  107  GLN   A CD  
2283 O  OE1 A GLN   A 107 ? 0.3206 0.3772 0.5577 -0.0590 -0.0091 -0.0825 107  GLN   A OE1 
2284 O  OE1 B GLN   A 107 ? 0.3422 0.3125 0.4226 -0.0133 -0.0282 0.0444  107  GLN   A OE1 
2285 N  NE2 A GLN   A 107 ? 0.3167 0.3761 0.5492 -0.0621 -0.0058 -0.0830 107  GLN   A NE2 
2286 N  NE2 B GLN   A 107 ? 0.3404 0.3120 0.4247 -0.0132 -0.0330 0.0392  107  GLN   A NE2 
2303 N  N   A LEU   A 108 ? 0.1641 0.2195 0.2255 -0.0525 0.0394  -0.1001 108  LEU   A N   
2304 N  N   B LEU   A 108 ? 0.2218 0.1764 0.2105 -0.0079 0.0199  0.0453  108  LEU   A N   
2305 C  CA  A LEU   A 108 ? 0.1568 0.1806 0.1982 -0.0269 0.0349  -0.0537 108  LEU   A CA  
2306 C  CA  B LEU   A 108 ? 0.2003 0.1631 0.1956 -0.0035 0.0251  0.0301  108  LEU   A CA  
2307 C  C   A LEU   A 108 ? 0.1403 0.1414 0.1925 -0.0135 0.0237  -0.0120 108  LEU   A C   
2308 C  C   B LEU   A 108 ? 0.1689 0.1415 0.1904 -0.0024 0.0237  0.0282  108  LEU   A C   
2309 O  O   A LEU   A 108 ? 0.1282 0.1402 0.2061 -0.0092 0.0246  -0.0101 108  LEU   A O   
2310 O  O   B LEU   A 108 ? 0.1682 0.1426 0.1988 -0.0016 0.0336  0.0319  108  LEU   A O   
2311 C  CB  A LEU   A 108 ? 0.1650 0.1925 0.1810 -0.0280 0.0403  -0.0404 108  LEU   A CB  
2312 C  CB  B LEU   A 108 ? 0.2081 0.1740 0.1839 -0.0052 0.0286  0.0225  108  LEU   A CB  
2313 C  CG  A LEU   A 108 ? 0.1795 0.2138 0.1984 -0.0276 0.0459  -0.0355 108  LEU   A CG  
2314 C  CG  B LEU   A 108 ? 0.2175 0.1857 0.1942 -0.0051 0.0307  0.0125  108  LEU   A CG  
2315 C  CD1 A LEU   A 108 ? 0.1960 0.2218 0.1965 -0.0327 0.0491  -0.0344 108  LEU   A CD1 
2316 C  CD1 B LEU   A 108 ? 0.2258 0.1903 0.1931 -0.0099 0.0369  0.0091  108  LEU   A CD1 
2317 C  CD2 A LEU   A 108 ? 0.1826 0.2302 0.2387 -0.0204 0.0404  -0.0261 108  LEU   A CD2 
2318 C  CD2 B LEU   A 108 ? 0.2188 0.1978 0.2160 -0.0010 0.0243  0.0085  108  LEU   A CD2 
2341 N  N   . LEU   A 109 ? 0.1410 0.1400 0.1853 -0.0009 0.0199  0.0179  109  LEU   A N   
2342 C  CA  . LEU   A 109 ? 0.1398 0.1334 0.1693 -0.0027 0.0078  0.0181  109  LEU   A CA  
2343 C  C   . LEU   A 109 ? 0.1276 0.1249 0.1579 -0.0100 0.0087  0.0092  109  LEU   A C   
2344 O  O   . LEU   A 109 ? 0.1348 0.1187 0.1770 -0.0068 -0.0011 0.0014  109  LEU   A O   
2345 C  CB  . LEU   A 109 ? 0.1431 0.1359 0.1806 0.0056  0.0003  0.0332  109  LEU   A CB  
2346 C  CG  . LEU   A 109 ? 0.1363 0.1461 0.1874 -0.0012 0.0071  0.0332  109  LEU   A CG  
2347 C  CD1 . LEU   A 109 ? 0.1430 0.1385 0.2022 0.0017  0.0186  0.0158  109  LEU   A CD1 
2348 C  CD2 . LEU   A 109 ? 0.1346 0.1690 0.2099 0.0005  0.0023  0.0391  109  LEU   A CD2 
2361 N  N   . LYS   A 110 ? 0.1251 0.1220 0.1621 -0.0081 0.0053  0.0025  110  LYS   A N   
2362 C  CA  . LYS   A 110 ? 0.1281 0.1189 0.1573 -0.0064 0.0031  0.0049  110  LYS   A CA  
2363 C  C   . LYS   A 110 ? 0.1256 0.1137 0.1405 -0.0048 0.0058  -0.0017 110  LYS   A C   
2364 O  O   . LYS   A 110 ? 0.1249 0.1191 0.1481 -0.0117 0.0112  -0.0003 110  LYS   A O   
2365 C  CB  . LYS   A 110 ? 0.1347 0.1211 0.1781 -0.0107 -0.0050 -0.0062 110  LYS   A CB  
2366 C  CG  . LYS   A 110 ? 0.1377 0.1188 0.1951 -0.0060 -0.0064 -0.0095 110  LYS   A CG  
2367 C  CD  . LYS   A 110 ? 0.1416 0.1265 0.2040 -0.0098 -0.0088 -0.0050 110  LYS   A CD  
2368 C  CE  . LYS   A 110 ? 0.1450 0.1323 0.2219 -0.0051 0.0106  -0.0094 110  LYS   A CE  
2369 N  NZ  . LYS   A 110 ? 0.1497 0.1353 0.2364 -0.0161 0.0170  -0.0065 110  LYS   A NZ  
2383 N  N   . SER   A 111 ? 0.1266 0.1211 0.1504 -0.0047 0.0081  0.0032  111  SER   A N   
2384 C  CA  . SER   A 111 ? 0.1240 0.1238 0.1565 -0.0012 0.0089  0.0005  111  SER   A CA  
2385 C  C   . SER   A 111 ? 0.1204 0.1189 0.1472 -0.0081 0.0114  0.0052  111  SER   A C   
2386 O  O   . SER   A 111 ? 0.1314 0.1113 0.1616 -0.0050 0.0100  0.0099  111  SER   A O   
2387 C  CB  . SER   A 111 ? 0.1393 0.1410 0.1645 -0.0028 0.0242  -0.0126 111  SER   A CB  
2388 O  OG  . SER   A 111 ? 0.1920 0.1573 0.1768 -0.0007 0.0251  -0.0151 111  SER   A OG  
2394 N  N   . ALA   A 112 ? 0.1204 0.1130 0.1610 -0.0017 0.0160  0.0062  112  ALA   A N   
2395 C  CA  . ALA   A 112 ? 0.1277 0.1101 0.1481 -0.0040 0.0210  -0.0011 112  ALA   A CA  
2396 C  C   . ALA   A 112 ? 0.1220 0.1077 0.1511 -0.0024 0.0119  0.0029  112  ALA   A C   
2397 O  O   . ALA   A 112 ? 0.1232 0.1106 0.1607 -0.0121 0.0150  0.0093  112  ALA   A O   
2398 C  CB  . ALA   A 112 ? 0.1358 0.1137 0.1537 -0.0026 0.0135  0.0019  112  ALA   A CB  
2404 N  N   . TYR   A 113 ? 0.1105 0.1139 0.1549 -0.0015 0.0115  0.0090  113  TYR   A N   
2405 C  CA  . TYR   A 113 ? 0.1149 0.1094 0.1513 -0.0027 0.0115  0.0098  113  TYR   A CA  
2406 C  C   . TYR   A 113 ? 0.1100 0.1130 0.1453 -0.0086 0.0154  0.0074  113  TYR   A C   
2407 O  O   . TYR   A 113 ? 0.1146 0.1139 0.1577 -0.0040 0.0198  0.0057  113  TYR   A O   
2408 C  CB  . TYR   A 113 ? 0.1168 0.1178 0.1592 -0.0070 0.0031  0.0186  113  TYR   A CB  
2409 C  CG  . TYR   A 113 ? 0.1117 0.1210 0.1562 -0.0056 0.0117  0.0224  113  TYR   A CG  
2410 C  CD1 . TYR   A 113 ? 0.1224 0.1284 0.1506 -0.0021 0.0075  0.0278  113  TYR   A CD1 
2411 C  CD2 . TYR   A 113 ? 0.1218 0.1266 0.1511 -0.0128 0.0006  0.0206  113  TYR   A CD2 
2412 C  CE1 . TYR   A 113 ? 0.1208 0.1313 0.1495 0.0012  0.0107  0.0344  113  TYR   A CE1 
2413 C  CE2 . TYR   A 113 ? 0.1170 0.1344 0.1444 -0.0091 -0.0017 0.0248  113  TYR   A CE2 
2414 C  CZ  . TYR   A 113 ? 0.1193 0.1313 0.1444 0.0014  0.0094  0.0356  113  TYR   A CZ  
2415 O  OH  . TYR   A 113 ? 0.1187 0.1463 0.1610 0.0110  0.0078  0.0358  113  TYR   A OH  
2425 N  N   . GLU   A 114 ? 0.1124 0.1090 0.1612 -0.0041 0.0135  0.0095  114  GLU   A N   
2426 C  CA  . GLU   A 114 ? 0.1171 0.1045 0.1622 0.0017  0.0094  0.0157  114  GLU   A CA  
2427 C  C   . GLU   A 114 ? 0.1138 0.1124 0.1578 0.0043  0.0155  0.0119  114  GLU   A C   
2428 O  O   . GLU   A 114 ? 0.1187 0.1091 0.1645 -0.0012 0.0110  0.0093  114  GLU   A O   
2429 C  CB  . GLU   A 114 ? 0.1152 0.1099 0.1588 -0.0033 0.0107  0.0076  114  GLU   A CB  
2430 C  CG  . GLU   A 114 ? 0.1231 0.1121 0.1674 0.0004  0.0121  0.0036  114  GLU   A CG  
2431 C  CD  . GLU   A 114 ? 0.1313 0.1146 0.1703 -0.0013 0.0028  0.0042  114  GLU   A CD  
2432 O  OE1 . GLU   A 114 ? 0.1312 0.1139 0.1855 -0.0077 0.0150  -0.0054 114  GLU   A OE1 
2433 O  OE2 . GLU   A 114 ? 0.1498 0.1187 0.1879 -0.0089 0.0083  -0.0128 114  GLU   A OE2 
2440 N  N   . ASN   A 115 ? 0.1135 0.1101 0.1472 -0.0022 0.0121  0.0049  115  ASN   A N   
2441 C  CA  . ASN   A 115 ? 0.1130 0.1179 0.1454 -0.0098 0.0104  0.0111  115  ASN   A CA  
2442 C  C   . ASN   A 115 ? 0.1173 0.1102 0.1411 -0.0108 0.0037  0.0114  115  ASN   A C   
2443 O  O   . ASN   A 115 ? 0.1227 0.1252 0.1416 -0.0090 0.0146  0.0146  115  ASN   A O   
2444 C  CB  . ASN   A 115 ? 0.1217 0.1207 0.1477 -0.0105 0.0129  0.0096  115  ASN   A CB  
2445 C  CG  . ASN   A 115 ? 0.1247 0.1459 0.1526 -0.0141 0.0238  0.0095  115  ASN   A CG  
2446 O  OD1 . ASN   A 115 ? 0.1281 0.2380 0.1861 -0.0148 0.0270  0.0219  115  ASN   A OD1 
2447 N  ND2 . ASN   A 115 ? 0.1300 0.1282 0.1398 -0.0111 0.0271  0.0136  115  ASN   A ND2 
2454 N  N   . PHE   A 116 ? 0.1130 0.1108 0.1542 -0.0031 0.0145  0.0170  116  PHE   A N   
2455 C  CA  . PHE   A 116 ? 0.1133 0.1218 0.1434 -0.0046 0.0148  0.0162  116  PHE   A CA  
2456 C  C   . PHE   A 116 ? 0.1118 0.1260 0.1515 -0.0063 0.0161  0.0201  116  PHE   A C   
2457 O  O   . PHE   A 116 ? 0.1190 0.1335 0.1625 0.0012  0.0142  0.0231  116  PHE   A O   
2458 C  CB  . PHE   A 116 ? 0.1177 0.1132 0.1513 -0.0007 0.0183  0.0156  116  PHE   A CB  
2459 C  CG  . PHE   A 116 ? 0.1193 0.1173 0.1452 -0.0070 0.0140  0.0076  116  PHE   A CG  
2460 C  CD1 . PHE   A 116 ? 0.1211 0.1140 0.1462 -0.0061 0.0164  0.0120  116  PHE   A CD1 
2461 C  CD2 . PHE   A 116 ? 0.1213 0.1202 0.1624 -0.0049 0.0197  0.0102  116  PHE   A CD2 
2462 C  CE1 . PHE   A 116 ? 0.1246 0.1121 0.1550 -0.0128 0.0129  0.0146  116  PHE   A CE1 
2463 C  CE2 . PHE   A 116 ? 0.1258 0.1228 0.1673 -0.0038 0.0202  0.0137  116  PHE   A CE2 
2464 C  CZ  . PHE   A 116 ? 0.1303 0.1052 0.1537 -0.0048 0.0134  0.0170  116  PHE   A CZ  
2474 N  N   . ASN   A 117 ? 0.1124 0.1222 0.1608 -0.0046 0.0188  0.0193  117  ASN   A N   
2475 C  CA  . ASN   A 117 ? 0.1185 0.1172 0.1659 -0.0021 0.0189  0.0259  117  ASN   A CA  
2476 C  C   . ASN   A 117 ? 0.1178 0.1245 0.1761 -0.0001 0.0132  0.0217  117  ASN   A C   
2477 O  O   . ASN   A 117 ? 0.1264 0.1298 0.2014 -0.0055 -0.0030 0.0386  117  ASN   A O   
2478 C  CB  . ASN   A 117 ? 0.1134 0.1202 0.1720 -0.0031 0.0155  0.0281  117  ASN   A CB  
2479 C  CG  . ASN   A 117 ? 0.1158 0.1259 0.1715 -0.0030 0.0166  0.0342  117  ASN   A CG  
2480 O  OD1 . ASN   A 117 ? 0.1209 0.1444 0.1786 -0.0122 0.0178  0.0209  117  ASN   A OD1 
2481 N  ND2 . ASN   A 117 ? 0.1140 0.1253 0.1677 -0.0008 0.0145  0.0239  117  ASN   A ND2 
2488 N  N   . GLN   A 118 ? 0.1147 0.1265 0.1742 -0.0062 0.0065  0.0295  118  GLN   A N   
2489 C  CA  . GLN   A 118 ? 0.1232 0.1365 0.1735 -0.0069 -0.0001 0.0216  118  GLN   A CA  
2490 C  C   . GLN   A 118 ? 0.1260 0.1420 0.1648 -0.0062 -0.0008 0.0242  118  GLN   A C   
2491 O  O   . GLN   A 118 ? 0.1277 0.1737 0.1913 0.0007  -0.0126 0.0037  118  GLN   A O   
2492 C  CB  . GLN   A 118 ? 0.1186 0.1399 0.1823 -0.0081 0.0100  0.0265  118  GLN   A CB  
2493 C  CG  . GLN   A 118 ? 0.1143 0.1452 0.1818 -0.0036 0.0072  0.0257  118  GLN   A CG  
2494 C  CD  . GLN   A 118 ? 0.1138 0.1474 0.1913 -0.0020 0.0131  0.0186  118  GLN   A CD  
2495 O  OE1 . GLN   A 118 ? 0.1233 0.1587 0.1927 0.0085  0.0034  0.0048  118  GLN   A OE1 
2496 N  NE2 . GLN   A 118 ? 0.1242 0.1397 0.1973 0.0022  0.0070  0.0255  118  GLN   A NE2 
2505 N  N   . HIS   A 119 ? 0.1290 0.1362 0.1592 -0.0054 0.0065  0.0248  119  HIS   A N   
2506 C  CA  . HIS   A 119 ? 0.1336 0.1506 0.1609 -0.0070 0.0080  0.0332  119  HIS   A CA  
2507 C  C   . HIS   A 119 ? 0.1412 0.1542 0.1573 -0.0037 0.0104  0.0339  119  HIS   A C   
2508 O  O   . HIS   A 119 ? 0.1494 0.1632 0.1658 -0.0252 0.0039  0.0319  119  HIS   A O   
2509 C  CB  . HIS   A 119 ? 0.1383 0.1468 0.1781 0.0006  0.0230  0.0335  119  HIS   A CB  
2510 C  CG  . HIS   A 119 ? 0.1378 0.1540 0.2212 0.0051  0.0240  0.0471  119  HIS   A CG  
2511 N  ND1 . HIS   A 119 ? 0.1498 0.1720 0.2779 -0.0055 0.0161  0.0337  119  HIS   A ND1 
2512 C  CD2 . HIS   A 119 ? 0.1493 0.1624 0.2468 0.0143  0.0387  0.0621  119  HIS   A CD2 
2513 C  CE1 . HIS   A 119 ? 0.1487 0.1697 0.2986 -0.0103 0.0360  0.0521  119  HIS   A CE1 
2514 N  NE2 . HIS   A 119 ? 0.1586 0.1652 0.2878 0.0034  0.0560  0.0641  119  HIS   A NE2 
2522 N  N   . GLU   A 120 ? 0.1494 0.1778 0.1576 -0.0038 0.0046  0.0521  120  GLU   A N   
2523 C  CA  . GLU   A 120 ? 0.1648 0.2035 0.1810 0.0065  0.0088  0.0847  120  GLU   A CA  
2524 C  C   . GLU   A 120 ? 0.1530 0.1861 0.1589 -0.0082 0.0059  0.0752  120  GLU   A C   
2525 O  O   . GLU   A 120 ? 0.1549 0.1800 0.1730 -0.0100 0.0065  0.0697  120  GLU   A O   
2526 C  CB  . GLU   A 120 ? 0.2241 0.2686 0.2278 0.0266  0.0074  0.1412  120  GLU   A CB  
2527 C  CG  . GLU   A 120 ? 0.3262 0.3471 0.3378 0.0431  0.0050  0.1490  120  GLU   A CG  
2528 C  CD  . GLU   A 120 ? 0.4021 0.4075 0.4512 0.0555  0.0142  0.1405  120  GLU   A CD  
2529 O  OE1 . GLU   A 120 ? 0.4226 0.4256 0.4771 0.0572  0.0151  0.1363  120  GLU   A OE1 
2530 O  OE2 . GLU   A 120 ? 0.4467 0.4467 0.5036 0.0599  0.0190  0.1381  120  GLU   A OE2 
2537 N  N   . VAL   A 121 ? 0.1505 0.1860 0.1390 -0.0095 0.0060  0.0582  121  VAL   A N   
2538 C  CA  . VAL   A 121 ? 0.1590 0.1925 0.1265 -0.0089 0.0106  0.0548  121  VAL   A CA  
2539 C  C   . VAL   A 121 ? 0.1422 0.1733 0.1201 -0.0172 0.0049  0.0416  121  VAL   A C   
2540 O  O   . VAL   A 121 ? 0.1488 0.1813 0.1389 -0.0295 -0.0047 0.0359  121  VAL   A O   
2541 C  CB  . VAL   A 121 ? 0.1971 0.2304 0.1556 0.0028  0.0284  0.0624  121  VAL   A CB  
2542 C  CG1 . VAL   A 121 ? 0.2000 0.2464 0.1594 0.0080  0.0427  0.0631  121  VAL   A CG1 
2543 C  CG2 . VAL   A 121 ? 0.2210 0.2483 0.2042 -0.0036 0.0222  0.0526  121  VAL   A CG2 
2553 N  N   . LEU   A 122 ? 0.1388 0.1532 0.1394 -0.0192 0.0131  0.0397  122  LEU   A N   
2554 C  CA  . LEU   A 122 ? 0.1443 0.1406 0.1403 -0.0227 0.0280  0.0328  122  LEU   A CA  
2555 C  C   . LEU   A 122 ? 0.1391 0.1424 0.1305 -0.0216 0.0103  0.0297  122  LEU   A C   
2556 O  O   . LEU   A 122 ? 0.1395 0.1516 0.1623 -0.0262 0.0061  0.0331  122  LEU   A O   
2557 C  CB  . LEU   A 122 ? 0.1617 0.1468 0.1682 -0.0114 0.0196  0.0417  122  LEU   A CB  
2558 C  CG  . LEU   A 122 ? 0.1643 0.1527 0.1587 -0.0065 0.0205  0.0312  122  LEU   A CG  
2559 C  CD1 . LEU   A 122 ? 0.1834 0.1618 0.1739 -0.0131 0.0196  0.0314  122  LEU   A CD1 
2560 C  CD2 . LEU   A 122 ? 0.1560 0.1452 0.1532 -0.0062 0.0283  0.0266  122  LEU   A CD2 
2572 N  N   A LEU   A 123 ? 0.1334 0.1402 0.1243 -0.0225 0.0070  0.0290  123  LEU   A N   
2573 N  N   B LEU   A 123 ? 0.1352 0.1397 0.1341 -0.0207 0.0021  0.0249  123  LEU   A N   
2574 C  CA  A LEU   A 123 ? 0.1315 0.1396 0.1181 -0.0197 0.0165  0.0328  123  LEU   A CA  
2575 C  CA  B LEU   A 123 ? 0.1327 0.1389 0.1373 -0.0170 0.0021  0.0224  123  LEU   A CA  
2576 C  C   A LEU   A 123 ? 0.1234 0.1297 0.1002 -0.0113 0.0129  0.0295  123  LEU   A C   
2577 C  C   B LEU   A 123 ? 0.1316 0.1326 0.1311 -0.0109 0.0034  0.0155  123  LEU   A C   
2578 O  O   A LEU   A 123 ? 0.1133 0.1227 0.1027 -0.0129 0.0135  0.0237  123  LEU   A O   
2579 O  O   B LEU   A 123 ? 0.1260 0.1330 0.1331 -0.0064 0.0048  0.0088  123  LEU   A O   
2580 C  CB  A LEU   A 123 ? 0.1431 0.1582 0.1185 -0.0194 0.0295  0.0286  123  LEU   A CB  
2581 C  CB  B LEU   A 123 ? 0.1356 0.1497 0.1364 -0.0159 0.0009  0.0208  123  LEU   A CB  
2582 C  CG  A LEU   A 123 ? 0.1500 0.1748 0.1289 -0.0124 0.0357  0.0135  123  LEU   A CG  
2583 C  CG  B LEU   A 123 ? 0.1350 0.1573 0.1332 -0.0143 -0.0003 0.0178  123  LEU   A CG  
2584 C  CD1 A LEU   A 123 ? 0.1572 0.1831 0.1435 -0.0074 0.0296  0.0030  123  LEU   A CD1 
2585 C  CD1 B LEU   A 123 ? 0.1413 0.1596 0.1506 -0.0080 -0.0026 0.0191  123  LEU   A CD1 
2586 C  CD2 A LEU   A 123 ? 0.1569 0.1811 0.1325 -0.0116 0.0258  0.0126  123  LEU   A CD2 
2587 C  CD2 B LEU   A 123 ? 0.1376 0.1607 0.1307 -0.0158 -0.0078 0.0153  123  LEU   A CD2 
2610 N  N   A ALA   A 124 ? 0.1216 0.1193 0.1014 -0.0099 0.0143  0.0263  124  ALA   A N   
2611 N  N   B ALA   A 124 ? 0.1336 0.1217 0.1343 -0.0138 0.0051  0.0118  124  ALA   A N   
2612 C  CA  A ALA   A 124 ? 0.1101 0.1177 0.1057 -0.0023 0.0110  0.0172  124  ALA   A CA  
2613 C  CA  B ALA   A 124 ? 0.1323 0.1186 0.1486 -0.0189 0.0043  0.0175  124  ALA   A CA  
2614 C  C   A ALA   A 124 ? 0.1044 0.1114 0.1093 -0.0005 0.0154  0.0139  124  ALA   A C   
2615 C  C   B ALA   A 124 ? 0.1252 0.1139 0.1449 -0.0114 0.0088  0.0189  124  ALA   A C   
2616 O  O   A ALA   A 124 ? 0.1074 0.1220 0.1278 -0.0066 0.0236  0.0193  124  ALA   A O   
2617 O  O   B ALA   A 124 ? 0.1237 0.1120 0.1524 0.0009  0.0172  0.0221  124  ALA   A O   
2618 C  CB  A ALA   A 124 ? 0.1078 0.1116 0.1207 0.0013  0.0060  0.0209  124  ALA   A CB  
2619 C  CB  B ALA   A 124 ? 0.1445 0.1167 0.1593 -0.0255 0.0027  0.0210  124  ALA   A CB  
2630 N  N   A PRO   A 125 ? 0.1013 0.1122 0.1151 0.0018  0.0178  0.0271  125  PRO   A N   
2631 N  N   B PRO   A 125 ? 0.1084 0.1108 0.1264 -0.0058 0.0019  0.0208  125  PRO   A N   
2632 C  CA  A PRO   A 125 ? 0.1135 0.1269 0.1311 0.0024  0.0071  0.0216  125  PRO   A CA  
2633 C  CA  B PRO   A 125 ? 0.1117 0.1219 0.1319 -0.0034 0.0072  0.0216  125  PRO   A CA  
2634 C  C   A PRO   A 125 ? 0.1116 0.1329 0.1119 -0.0074 0.0092  0.0301  125  PRO   A C   
2635 C  C   B PRO   A 125 ? 0.1192 0.1310 0.1383 -0.0060 0.0024  0.0188  125  PRO   A C   
2636 O  O   A PRO   A 125 ? 0.1241 0.1266 0.1244 0.0021  -0.0042 0.0199  125  PRO   A O   
2637 O  O   B PRO   A 125 ? 0.1268 0.1262 0.1566 -0.0008 -0.0035 0.0092  125  PRO   A O   
2638 C  CB  A PRO   A 125 ? 0.1246 0.1235 0.1372 0.0028  0.0078  0.0227  125  PRO   A CB  
2639 C  CB  B PRO   A 125 ? 0.1062 0.1194 0.1242 -0.0050 0.0182  0.0237  125  PRO   A CB  
2640 C  CG  A PRO   A 125 ? 0.1294 0.1140 0.1395 -0.0012 0.0124  0.0245  125  PRO   A CG  
2641 C  CG  B PRO   A 125 ? 0.0980 0.1114 0.1172 -0.0057 0.0228  0.0146  125  PRO   A CG  
2642 C  CD  A PRO   A 125 ? 0.1186 0.1184 0.1261 0.0028  0.0168  0.0134  125  PRO   A CD  
2643 C  CD  B PRO   A 125 ? 0.0979 0.0991 0.1139 -0.0029 0.0082  0.0127  125  PRO   A CD  
2658 N  N   A LEU   A 126 ? 0.1144 0.1422 0.1130 -0.0043 0.0024  0.0322  126  LEU   A N   
2659 N  N   B LEU   A 126 ? 0.1226 0.1426 0.1362 -0.0013 -0.0032 0.0129  126  LEU   A N   
2660 C  CA  A LEU   A 126 ? 0.1194 0.1384 0.1307 -0.0014 0.0023  0.0373  126  LEU   A CA  
2661 C  CA  B LEU   A 126 ? 0.1200 0.1364 0.1309 -0.0043 -0.0034 0.0175  126  LEU   A CA  
2662 C  C   A LEU   A 126 ? 0.1294 0.1380 0.1351 0.0082  0.0013  0.0314  126  LEU   A C   
2663 C  C   B LEU   A 126 ? 0.1210 0.1308 0.1099 0.0029  -0.0010 0.0226  126  LEU   A C   
2664 O  O   A LEU   A 126 ? 0.1370 0.1396 0.1490 0.0147  0.0063  0.0279  126  LEU   A O   
2665 O  O   B LEU   A 126 ? 0.1256 0.1255 0.1059 -0.0004 0.0015  0.0251  126  LEU   A O   
2666 C  CB  A LEU   A 126 ? 0.1240 0.1352 0.1467 -0.0015 -0.0020 0.0327  126  LEU   A CB  
2667 C  CB  B LEU   A 126 ? 0.1224 0.1404 0.1393 -0.0102 -0.0047 0.0060  126  LEU   A CB  
2668 C  CG  A LEU   A 126 ? 0.1254 0.1403 0.1825 0.0057  0.0132  0.0187  126  LEU   A CG  
2669 C  CG  B LEU   A 126 ? 0.1199 0.1397 0.1546 -0.0083 0.0059  -0.0052 126  LEU   A CG  
2670 C  CD1 A LEU   A 126 ? 0.1364 0.1493 0.2071 0.0040  0.0136  0.0183  126  LEU   A CD1 
2671 C  CD1 B LEU   A 126 ? 0.1258 0.1340 0.1722 -0.0096 0.0003  -0.0183 126  LEU   A CD1 
2672 C  CD2 A LEU   A 126 ? 0.1348 0.1344 0.1785 0.0044  0.0263  0.0180  126  LEU   A CD2 
2673 C  CD2 B LEU   A 126 ? 0.1155 0.1482 0.1619 -0.0094 0.0160  0.0024  126  LEU   A CD2 
2696 N  N   A LEU   A 127 ? 0.1349 0.1326 0.1435 0.0055  -0.0014 0.0279  127  LEU   A N   
2697 N  N   B LEU   A 127 ? 0.1170 0.1264 0.1128 0.0057  0.0015  0.0263  127  LEU   A N   
2698 C  CA  A LEU   A 127 ? 0.1350 0.1325 0.1288 -0.0040 -0.0008 0.0174  127  LEU   A CA  
2699 C  CA  B LEU   A 127 ? 0.1155 0.1279 0.1142 -0.0010 0.0013  0.0280  127  LEU   A CA  
2700 C  C   A LEU   A 127 ? 0.1338 0.1308 0.1189 -0.0028 -0.0011 0.0139  127  LEU   A C   
2701 C  C   B LEU   A 127 ? 0.1166 0.1231 0.1206 -0.0005 0.0029  0.0204  127  LEU   A C   
2702 O  O   A LEU   A 127 ? 0.1379 0.1326 0.1260 -0.0113 -0.0043 0.0153  127  LEU   A O   
2703 O  O   B LEU   A 127 ? 0.1188 0.1257 0.1296 -0.0008 0.0043  0.0278  127  LEU   A O   
2704 C  CB  A LEU   A 127 ? 0.1337 0.1254 0.1245 -0.0006 0.0034  0.0132  127  LEU   A CB  
2705 C  CB  B LEU   A 127 ? 0.1137 0.1342 0.1155 -0.0010 -0.0048 0.0159  127  LEU   A CB  
2706 C  CG  A LEU   A 127 ? 0.1324 0.1160 0.1238 0.0038  -0.0013 0.0115  127  LEU   A CG  
2707 C  CG  B LEU   A 127 ? 0.1236 0.1405 0.1138 0.0030  -0.0082 0.0187  127  LEU   A CG  
2708 C  CD1 A LEU   A 127 ? 0.1328 0.1133 0.1156 -0.0014 -0.0061 0.0006  127  LEU   A CD1 
2709 C  CD1 B LEU   A 127 ? 0.1246 0.1419 0.1376 0.0109  -0.0031 0.0144  127  LEU   A CD1 
2710 C  CD2 A LEU   A 127 ? 0.1421 0.1083 0.1533 0.0114  -0.0123 0.0057  127  LEU   A CD2 
2711 C  CD2 B LEU   A 127 ? 0.1386 0.1538 0.1172 0.0002  -0.0203 0.0007  127  LEU   A CD2 
2734 N  N   A SER   A 128 ? 0.1340 0.1321 0.0994 -0.0042 -0.0026 0.0162  128  SER   A N   
2735 N  N   B SER   A 128 ? 0.1237 0.1185 0.1156 -0.0094 -0.0043 0.0158  128  SER   A N   
2736 C  CA  A SER   A 128 ? 0.1403 0.1368 0.0993 0.0010  0.0014  0.0146  128  SER   A CA  
2737 C  CA  B SER   A 128 ? 0.1277 0.1185 0.1062 -0.0088 -0.0034 0.0120  128  SER   A CA  
2738 C  C   A SER   A 128 ? 0.1458 0.1404 0.0965 0.0107  0.0015  0.0220  128  SER   A C   
2739 C  C   B SER   A 128 ? 0.1302 0.1193 0.1041 -0.0065 -0.0122 0.0166  128  SER   A C   
2740 O  O   A SER   A 128 ? 0.1617 0.1599 0.1174 0.0051  0.0019  0.0181  128  SER   A O   
2741 O  O   B SER   A 128 ? 0.1273 0.1215 0.1201 -0.0044 -0.0099 0.0107  128  SER   A O   
2742 C  CB  A SER   A 128 ? 0.1355 0.1331 0.1114 -0.0003 0.0002  0.0111  128  SER   A CB  
2743 C  CB  B SER   A 128 ? 0.1328 0.1234 0.1093 -0.0071 -0.0006 0.0098  128  SER   A CB  
2744 O  OG  A SER   A 128 ? 0.1363 0.1364 0.1195 0.0043  0.0024  0.0043  128  SER   A OG  
2745 O  OG  B SER   A 128 ? 0.1378 0.1312 0.1215 -0.0056 0.0098  0.0127  128  SER   A OG  
2756 N  N   A ALA   A 129 ? 0.1391 0.1421 0.1229 0.0094  -0.0020 0.0177  129  ALA   A N   
2757 N  N   B ALA   A 129 ? 0.1335 0.1245 0.1210 -0.0100 -0.0172 0.0137  129  ALA   A N   
2758 C  CA  A ALA   A 129 ? 0.1310 0.1421 0.1329 0.0084  0.0013  0.0145  129  ALA   A CA  
2759 C  CA  B ALA   A 129 ? 0.1376 0.1252 0.1308 -0.0074 -0.0107 0.0107  129  ALA   A CA  
2760 C  C   A ALA   A 129 ? 0.1335 0.1384 0.1314 0.0012  -0.0127 0.0041  129  ALA   A C   
2761 C  C   B ALA   A 129 ? 0.1469 0.1303 0.1298 -0.0006 -0.0148 0.0078  129  ALA   A C   
2762 O  O   A ALA   A 129 ? 0.1367 0.1385 0.1259 -0.0110 -0.0089 0.0108  129  ALA   A O   
2763 O  O   B ALA   A 129 ? 0.1526 0.1360 0.1397 0.0007  -0.0129 0.0151  129  ALA   A O   
2764 C  CB  A ALA   A 129 ? 0.1342 0.1539 0.1510 0.0116  0.0093  0.0123  129  ALA   A CB  
2765 C  CB  B ALA   A 129 ? 0.1344 0.1250 0.1284 -0.0051 -0.0086 0.0078  129  ALA   A CB  
2776 N  N   A GLY   A 130 ? 0.1367 0.1332 0.1654 -0.0047 -0.0050 -0.0038 130  GLY   A N   
2777 N  N   B GLY   A 130 ? 0.1479 0.1303 0.1375 -0.0048 -0.0136 0.0101  130  GLY   A N   
2778 C  CA  A GLY   A 130 ? 0.1543 0.1346 0.1732 -0.0021 -0.0045 0.0000  130  GLY   A CA  
2779 C  CA  B GLY   A 130 ? 0.1575 0.1335 0.1354 0.0003  -0.0045 0.0079  130  GLY   A CA  
2780 C  C   A GLY   A 130 ? 0.1557 0.1389 0.1720 0.0017  -0.0126 0.0059  130  GLY   A C   
2781 C  C   B GLY   A 130 ? 0.1575 0.1337 0.1250 -0.0006 0.0025  -0.0012 130  GLY   A C   
2782 O  O   A GLY   A 130 ? 0.1558 0.1384 0.1815 0.0073  -0.0312 0.0085  130  GLY   A O   
2783 O  O   B GLY   A 130 ? 0.1603 0.1316 0.1157 -0.0029 0.0035  -0.0034 130  GLY   A O   
2790 N  N   A ILE   A 131 ? 0.1588 0.1387 0.1544 -0.0060 -0.0119 0.0133  131  ILE   A N   
2791 N  N   B ILE   A 131 ? 0.1617 0.1355 0.1388 -0.0026 0.0032  -0.0098 131  ILE   A N   
2792 C  CA  A ILE   A 131 ? 0.1732 0.1337 0.1315 -0.0147 -0.0190 0.0141  131  ILE   A CA  
2793 C  CA  B ILE   A 131 ? 0.1701 0.1308 0.1329 -0.0094 0.0054  -0.0147 131  ILE   A CA  
2794 C  C   A ILE   A 131 ? 0.1587 0.1329 0.1117 -0.0133 -0.0208 0.0254  131  ILE   A C   
2795 C  C   B ILE   A 131 ? 0.1601 0.1330 0.1219 -0.0044 0.0006  -0.0101 131  ILE   A C   
2796 O  O   A ILE   A 131 ? 0.1664 0.1401 0.1379 -0.0027 -0.0157 0.0300  131  ILE   A O   
2797 O  O   B ILE   A 131 ? 0.1547 0.1340 0.1308 0.0016  -0.0062 -0.0009 131  ILE   A O   
2798 C  CB  A ILE   A 131 ? 0.2004 0.1508 0.1393 -0.0297 -0.0182 -0.0010 131  ILE   A CB  
2799 C  CB  B ILE   A 131 ? 0.1890 0.1373 0.1458 -0.0240 0.0098  -0.0087 131  ILE   A CB  
2800 C  CG1 A ILE   A 131 ? 0.2082 0.1706 0.1430 -0.0472 -0.0161 0.0063  131  ILE   A CG1 
2801 C  CG1 B ILE   A 131 ? 0.1978 0.1556 0.1574 -0.0338 0.0016  0.0007  131  ILE   A CG1 
2802 C  CG2 A ILE   A 131 ? 0.2133 0.1488 0.1493 -0.0230 -0.0155 -0.0118 131  ILE   A CG2 
2803 C  CG2 B ILE   A 131 ? 0.1967 0.1325 0.1466 -0.0224 0.0167  -0.0114 131  ILE   A CG2 
2804 C  CD1 A ILE   A 131 ? 0.2142 0.1777 0.1586 -0.0565 -0.0169 0.0012  131  ILE   A CD1 
2805 C  CD1 B ILE   A 131 ? 0.2053 0.1612 0.1678 -0.0380 -0.0011 0.0112  131  ILE   A CD1 
2828 N  N   A PHE   A 132 ? 0.1487 0.1325 0.1034 0.0013  -0.0159 0.0225  132  PHE   A N   
2829 N  N   B PHE   A 132 ? 0.1578 0.1381 0.1253 0.0012  0.0052  -0.0012 132  PHE   A N   
2830 C  CA  A PHE   A 132 ? 0.1567 0.1347 0.1071 -0.0031 -0.0101 0.0154  132  PHE   A CA  
2831 C  CA  B PHE   A 132 ? 0.1617 0.1488 0.1146 0.0016  0.0061  -0.0030 132  PHE   A CA  
2832 C  C   A PHE   A 132 ? 0.1775 0.1426 0.1164 -0.0083 -0.0230 0.0197  132  PHE   A C   
2833 C  C   B PHE   A 132 ? 0.1670 0.1616 0.1075 -0.0004 0.0013  -0.0009 132  PHE   A C   
2834 O  O   A PHE   A 132 ? 0.1903 0.1432 0.1295 -0.0051 -0.0214 0.0140  132  PHE   A O   
2835 O  O   B PHE   A 132 ? 0.1687 0.1666 0.1064 0.0025  0.0008  -0.0016 132  PHE   A O   
2836 C  CB  A PHE   A 132 ? 0.1424 0.1301 0.1097 -0.0061 -0.0017 0.0250  132  PHE   A CB  
2837 C  CB  B PHE   A 132 ? 0.1580 0.1496 0.1231 0.0051  0.0090  -0.0060 132  PHE   A CB  
2838 C  CG  A PHE   A 132 ? 0.1418 0.1290 0.1096 -0.0005 -0.0075 0.0168  132  PHE   A CG  
2839 C  CG  B PHE   A 132 ? 0.1588 0.1532 0.1157 0.0069  0.0074  -0.0057 132  PHE   A CG  
2840 C  CD1 A PHE   A 132 ? 0.1415 0.1448 0.1287 0.0051  -0.0060 0.0015  132  PHE   A CD1 
2841 C  CD1 B PHE   A 132 ? 0.1632 0.1610 0.1159 0.0038  0.0070  -0.0073 132  PHE   A CD1 
2842 C  CD2 A PHE   A 132 ? 0.1458 0.1394 0.1378 0.0081  -0.0178 0.0103  132  PHE   A CD2 
2843 C  CD2 B PHE   A 132 ? 0.1590 0.1593 0.1148 0.0089  0.0086  -0.0146 132  PHE   A CD2 
2844 C  CE1 A PHE   A 132 ? 0.1444 0.1485 0.1369 0.0041  -0.0142 -0.0067 132  PHE   A CE1 
2845 C  CE1 B PHE   A 132 ? 0.1646 0.1643 0.1140 0.0012  0.0052  -0.0059 132  PHE   A CE1 
2846 C  CE2 A PHE   A 132 ? 0.1441 0.1495 0.1511 0.0085  -0.0271 0.0108  132  PHE   A CE2 
2847 C  CE2 B PHE   A 132 ? 0.1587 0.1655 0.1223 0.0098  0.0113  -0.0080 132  PHE   A CE2 
2848 C  CZ  A PHE   A 132 ? 0.1371 0.1465 0.1465 0.0027  -0.0254 0.0050  132  PHE   A CZ  
2849 C  CZ  B PHE   A 132 ? 0.1577 0.1633 0.1142 0.0032  0.0065  -0.0018 132  PHE   A CZ  
2868 N  N   A GLY   A 133 ? 0.1842 0.1493 0.1237 -0.0152 -0.0383 0.0273  133  GLY   A N   
2869 N  N   B GLY   A 133 ? 0.1675 0.1706 0.1137 -0.0005 -0.0098 0.0004  133  GLY   A N   
2870 C  CA  A GLY   A 133 ? 0.1883 0.1586 0.1323 -0.0174 -0.0462 0.0207  133  GLY   A CA  
2871 C  CA  B GLY   A 133 ? 0.1669 0.1772 0.1237 0.0007  -0.0188 -0.0036 133  GLY   A CA  
2872 C  C   A GLY   A 133 ? 0.1839 0.1693 0.1318 -0.0203 -0.0444 0.0080  133  GLY   A C   
2873 C  C   B GLY   A 133 ? 0.1570 0.1821 0.1261 0.0029  -0.0211 -0.0101 133  GLY   A C   
2874 O  O   A GLY   A 133 ? 0.1899 0.1845 0.1378 -0.0226 -0.0365 -0.0073 133  GLY   A O   
2875 O  O   B GLY   A 133 ? 0.1517 0.1870 0.1394 0.0036  -0.0136 -0.0210 133  GLY   A O   
2882 N  N   A ALA   A 134 ? 0.1801 0.1572 0.1286 -0.0203 -0.0230 0.0059  134  ALA   A N   
2883 N  N   B ALA   A 134 ? 0.1611 0.1769 0.1315 0.0010  -0.0244 -0.0050 134  ALA   A N   
2884 C  CA  A ALA   A 134 ? 0.1742 0.1512 0.1475 -0.0158 -0.0171 -0.0059 134  ALA   A CA  
2885 C  CA  B ALA   A 134 ? 0.1620 0.1773 0.1435 -0.0024 -0.0249 -0.0023 134  ALA   A CA  
2886 C  C   A ALA   A 134 ? 0.1769 0.1571 0.1435 -0.0064 -0.0103 -0.0030 134  ALA   A C   
2887 C  C   B ALA   A 134 ? 0.1639 0.1802 0.1401 -0.0066 -0.0217 0.0115  134  ALA   A C   
2888 O  O   A ALA   A 134 ? 0.1914 0.1657 0.1587 -0.0035 0.0181  -0.0110 134  ALA   A O   
2889 O  O   B ALA   A 134 ? 0.1796 0.1854 0.1526 -0.0060 -0.0163 0.0081  134  ALA   A O   
2890 C  CB  A ALA   A 134 ? 0.1758 0.1500 0.1811 -0.0182 -0.0155 -0.0134 134  ALA   A CB  
2891 C  CB  B ALA   A 134 ? 0.1672 0.1782 0.1622 0.0014  -0.0216 -0.0087 134  ALA   A CB  
2902 N  N   A ASP   A 135 ? 0.1739 0.1641 0.1599 -0.0105 -0.0161 0.0112  135  ASP   A N   
2903 N  N   B ASP   A 135 ? 0.1574 0.1795 0.1504 -0.0091 -0.0193 0.0174  135  ASP   A N   
2904 C  CA  A ASP   A 135 ? 0.1689 0.1818 0.1889 -0.0138 -0.0261 0.0222  135  ASP   A CA  
2905 C  CA  B ASP   A 135 ? 0.1558 0.1862 0.1707 -0.0145 -0.0285 0.0248  135  ASP   A CA  
2906 C  C   A ASP   A 135 ? 0.1568 0.1726 0.1878 -0.0083 -0.0154 0.0298  135  ASP   A C   
2907 C  C   B ASP   A 135 ? 0.1588 0.1802 0.1760 -0.0173 -0.0206 0.0399  135  ASP   A C   
2908 O  O   A ASP   A 135 ? 0.1482 0.1696 0.1934 -0.0102 -0.0145 0.0293  135  ASP   A O   
2909 O  O   B ASP   A 135 ? 0.1537 0.1751 0.1745 -0.0179 -0.0184 0.0430  135  ASP   A O   
2910 C  CB  A ASP   A 135 ? 0.1833 0.2093 0.2238 -0.0230 -0.0415 0.0144  135  ASP   A CB  
2911 C  CB  B ASP   A 135 ? 0.1626 0.2008 0.2054 -0.0252 -0.0376 0.0117  135  ASP   A CB  
2912 C  CG  A ASP   A 135 ? 0.1949 0.2391 0.2663 -0.0287 -0.0455 0.0141  135  ASP   A CG  
2913 C  CG  B ASP   A 135 ? 0.1693 0.2127 0.2371 -0.0353 -0.0437 0.0035  135  ASP   A CG  
2914 O  OD1 A ASP   A 135 ? 0.1908 0.2434 0.2740 -0.0229 -0.0451 0.0264  135  ASP   A OD1 
2915 O  OD1 B ASP   A 135 ? 0.1669 0.2192 0.2322 -0.0424 -0.0534 0.0031  135  ASP   A OD1 
2916 O  OD2 A ASP   A 135 ? 0.2123 0.2591 0.3040 -0.0356 -0.0475 0.0110  135  ASP   A OD2 
2917 O  OD2 B ASP   A 135 ? 0.1838 0.2222 0.2768 -0.0343 -0.0200 0.0022  135  ASP   A OD2 
2926 N  N   A PRO   A 136 ? 0.1503 0.1685 0.1861 0.0022  -0.0127 0.0380  136  PRO   A N   
2927 N  N   B PRO   A 136 ? 0.1591 0.1785 0.1837 -0.0115 -0.0180 0.0453  136  PRO   A N   
2928 C  CA  A PRO   A 136 ? 0.1425 0.1707 0.1906 -0.0013 -0.0114 0.0294  136  PRO   A CA  
2929 C  CA  B PRO   A 136 ? 0.1558 0.1757 0.1887 -0.0121 -0.0113 0.0458  136  PRO   A CA  
2930 C  C   A PRO   A 136 ? 0.1218 0.1734 0.1910 -0.0037 -0.0090 0.0329  136  PRO   A C   
2931 C  C   B PRO   A 136 ? 0.1408 0.1727 0.1949 -0.0123 -0.0048 0.0453  136  PRO   A C   
2932 O  O   A PRO   A 136 ? 0.1167 0.1636 0.1720 -0.0017 0.0010  0.0264  136  PRO   A O   
2933 O  O   B PRO   A 136 ? 0.1386 0.1737 0.1916 -0.0122 0.0010  0.0427  136  PRO   A O   
2934 C  CB  A PRO   A 136 ? 0.1586 0.1671 0.2074 -0.0011 -0.0135 0.0197  136  PRO   A CB  
2935 C  CB  B PRO   A 136 ? 0.1659 0.1739 0.1879 -0.0102 -0.0116 0.0487  136  PRO   A CB  
2936 C  CG  A PRO   A 136 ? 0.1717 0.1703 0.2202 0.0042  -0.0142 0.0173  136  PRO   A CG  
2937 C  CG  B PRO   A 136 ? 0.1695 0.1769 0.1971 -0.0112 -0.0190 0.0415  136  PRO   A CG  
2938 C  CD  A PRO   A 136 ? 0.1569 0.1633 0.2006 0.0071  -0.0075 0.0392  136  PRO   A CD  
2939 C  CD  B PRO   A 136 ? 0.1662 0.1769 0.1916 -0.0102 -0.0174 0.0456  136  PRO   A CD  
2954 N  N   A ILE   A 137 ? 0.1200 0.1821 0.2112 -0.0027 -0.0202 0.0384  137  ILE   A N   
2955 N  N   B ILE   A 137 ? 0.1375 0.1738 0.1998 -0.0134 -0.0145 0.0519  137  ILE   A N   
2956 C  CA  A ILE   A 137 ? 0.1239 0.1919 0.2225 -0.0138 -0.0237 0.0374  137  ILE   A CA  
2957 C  CA  B ILE   A 137 ? 0.1396 0.1780 0.2107 -0.0216 -0.0210 0.0473  137  ILE   A CA  
2958 C  C   A ILE   A 137 ? 0.1258 0.1838 0.2131 -0.0222 -0.0152 0.0342  137  ILE   A C   
2959 C  C   B ILE   A 137 ? 0.1395 0.1737 0.2043 -0.0199 -0.0205 0.0445  137  ILE   A C   
2960 O  O   A ILE   A 137 ? 0.1303 0.1839 0.2200 -0.0252 -0.0108 0.0324  137  ILE   A O   
2961 O  O   B ILE   A 137 ? 0.1466 0.1697 0.2084 -0.0196 -0.0201 0.0403  137  ILE   A O   
2962 C  CB  A ILE   A 137 ? 0.1328 0.2171 0.2444 -0.0126 -0.0308 0.0339  137  ILE   A CB  
2963 C  CB  B ILE   A 137 ? 0.1484 0.1954 0.2312 -0.0230 -0.0324 0.0398  137  ILE   A CB  
2964 C  CG1 A ILE   A 137 ? 0.1392 0.2386 0.2600 -0.0022 -0.0298 0.0349  137  ILE   A CG1 
2965 C  CG1 B ILE   A 137 ? 0.1572 0.2156 0.2447 -0.0094 -0.0372 0.0374  137  ILE   A CG1 
2966 C  CG2 A ILE   A 137 ? 0.1444 0.2208 0.2633 -0.0195 -0.0366 0.0263  137  ILE   A CG2 
2967 C  CG2 B ILE   A 137 ? 0.1538 0.1924 0.2429 -0.0349 -0.0334 0.0350  137  ILE   A CG2 
2968 C  CD1 A ILE   A 137 ? 0.1522 0.2540 0.2763 0.0038  -0.0241 0.0366  137  ILE   A CD1 
2969 C  CD1 B ILE   A 137 ? 0.1678 0.2295 0.2621 -0.0027 -0.0328 0.0353  137  ILE   A CD1 
2992 N  N   A HIS   A 138 ? 0.1288 0.1933 0.2057 -0.0191 -0.0076 0.0283  138  HIS   A N   
2993 N  N   B HIS   A 138 ? 0.1372 0.1807 0.1945 -0.0151 -0.0205 0.0414  138  HIS   A N   
2994 C  CA  A HIS   A 138 ? 0.1406 0.1931 0.1939 -0.0217 -0.0034 0.0230  138  HIS   A CA  
2995 C  CA  B HIS   A 138 ? 0.1396 0.1849 0.1872 -0.0175 -0.0176 0.0310  138  HIS   A CA  
2996 C  C   A HIS   A 138 ? 0.1353 0.1798 0.1815 -0.0155 0.0001  0.0337  138  HIS   A C   
2997 C  C   B HIS   A 138 ? 0.1337 0.1764 0.1773 -0.0152 -0.0127 0.0366  138  HIS   A C   
2998 O  O   A HIS   A 138 ? 0.1411 0.1764 0.1959 -0.0153 0.0077  0.0263  138  HIS   A O   
2999 O  O   B HIS   A 138 ? 0.1379 0.1722 0.1804 -0.0175 -0.0107 0.0310  138  HIS   A O   
3000 C  CB  A HIS   A 138 ? 0.1527 0.2099 0.1937 -0.0184 -0.0028 0.0063  138  HIS   A CB  
3001 C  CB  B HIS   A 138 ? 0.1531 0.2001 0.1960 -0.0182 -0.0170 0.0182  138  HIS   A CB  
3002 C  CG  A HIS   A 138 ? 0.1672 0.2252 0.1975 -0.0194 -0.0101 -0.0047 138  HIS   A CG  
3003 C  CG  B HIS   A 138 ? 0.1654 0.2124 0.2090 -0.0209 -0.0142 0.0090  138  HIS   A CG  
3004 N  ND1 A HIS   A 138 ? 0.1790 0.2363 0.2166 -0.0210 -0.0139 -0.0163 138  HIS   A ND1 
3005 N  ND1 B HIS   A 138 ? 0.1754 0.2228 0.2264 -0.0239 -0.0107 -0.0031 138  HIS   A ND1 
3006 C  CD2 A HIS   A 138 ? 0.1681 0.2321 0.1988 -0.0117 -0.0117 -0.0015 138  HIS   A CD2 
3007 C  CD2 B HIS   A 138 ? 0.1664 0.2189 0.2132 -0.0178 -0.0136 0.0086  138  HIS   A CD2 
3008 C  CE1 A HIS   A 138 ? 0.1784 0.2397 0.2139 -0.0109 -0.0173 -0.0162 138  HIS   A CE1 
3009 C  CE1 B HIS   A 138 ? 0.1756 0.2261 0.2267 -0.0185 -0.0098 -0.0058 138  HIS   A CE1 
3010 N  NE2 A HIS   A 138 ? 0.1728 0.2389 0.1991 -0.0081 -0.0087 -0.0092 138  HIS   A NE2 
3011 N  NE2 B HIS   A 138 ? 0.1694 0.2254 0.2192 -0.0165 -0.0054 0.0010  138  HIS   A NE2 
3026 N  N   . SER   A 139 ? 0.1284 0.1735 0.1812 -0.0115 -0.0064 0.0444  139  SER   A N   
3027 C  CA  . SER   A 139 ? 0.1202 0.1641 0.1858 -0.0126 -0.0053 0.0467  139  SER   A CA  
3028 C  C   . SER   A 139 ? 0.1170 0.1556 0.1846 -0.0073 -0.0032 0.0355  139  SER   A C   
3029 O  O   . SER   A 139 ? 0.1146 0.1472 0.1956 -0.0120 0.0025  0.0401  139  SER   A O   
3030 C  CB  . SER   A 139 ? 0.1206 0.1641 0.1807 -0.0161 -0.0116 0.0511  139  SER   A CB  
3031 O  OG  . SER   A 139 ? 0.1257 0.1633 0.1813 -0.0174 -0.0111 0.0586  139  SER   A OG  
3038 N  N   . LEU   A 140 ? 0.1156 0.1594 0.1830 -0.0090 0.0005  0.0516  140  LEU   A N   
3039 C  CA  . LEU   A 140 ? 0.1201 0.1568 0.1863 -0.0106 -0.0026 0.0517  140  LEU   A CA  
3040 C  C   . LEU   A 140 ? 0.1088 0.1624 0.1881 -0.0102 -0.0020 0.0490  140  LEU   A C   
3041 O  O   . LEU   A 140 ? 0.1159 0.1569 0.2109 -0.0055 0.0003  0.0471  140  LEU   A O   
3042 C  CB  . LEU   A 140 ? 0.1164 0.1651 0.1862 -0.0077 0.0012  0.0475  140  LEU   A CB  
3043 C  CG  . LEU   A 140 ? 0.1198 0.1833 0.1891 -0.0187 0.0043  0.0512  140  LEU   A CG  
3044 C  CD1 . LEU   A 140 ? 0.1192 0.1855 0.1871 -0.0083 0.0038  0.0488  140  LEU   A CD1 
3045 C  CD2 . LEU   A 140 ? 0.1280 0.1987 0.2001 -0.0173 0.0100  0.0571  140  LEU   A CD2 
3057 N  N   . ARG   A 141 ? 0.1176 0.1651 0.2003 -0.0095 0.0013  0.0422  141  ARG   A N   
3058 C  CA  . ARG   A 141 ? 0.1247 0.1819 0.2155 -0.0231 -0.0060 0.0235  141  ARG   A CA  
3059 C  C   . ARG   A 141 ? 0.1283 0.1661 0.1931 -0.0152 -0.0091 0.0259  141  ARG   A C   
3060 O  O   . ARG   A 141 ? 0.1241 0.1584 0.2036 -0.0165 0.0011  0.0173  141  ARG   A O   
3061 C  CB  . ARG   A 141 ? 0.1384 0.2098 0.2473 -0.0319 -0.0130 0.0029  141  ARG   A CB  
3062 C  CG  . ARG   A 141 ? 0.1751 0.2555 0.2838 -0.0309 0.0084  -0.0015 141  ARG   A CG  
3063 C  CD  . ARG   A 141 ? 0.2033 0.2869 0.3150 -0.0379 0.0195  -0.0063 141  ARG   A CD  
3064 N  NE  . ARG   A 141 ? 0.1970 0.3119 0.3300 -0.0440 0.0008  -0.0091 141  ARG   A NE  
3065 C  CZ  . ARG   A 141 ? 0.1991 0.3307 0.3450 -0.0632 0.0050  -0.0026 141  ARG   A CZ  
3066 N  NH1 . ARG   A 141 ? 0.1903 0.3330 0.3418 -0.0770 0.0244  -0.0153 141  ARG   A NH1 
3067 N  NH2 . ARG   A 141 ? 0.2021 0.3443 0.3631 -0.0622 -0.0062 0.0079  141  ARG   A NH2 
3081 N  N   . VAL   A 142 ? 0.1203 0.1605 0.1800 -0.0126 -0.0052 0.0197  142  VAL   A N   
3082 C  CA  . VAL   A 142 ? 0.1292 0.1518 0.1794 -0.0126 0.0110  0.0196  142  VAL   A CA  
3083 C  C   . VAL   A 142 ? 0.1150 0.1444 0.1750 -0.0121 0.0073  0.0263  142  VAL   A C   
3084 O  O   . VAL   A 142 ? 0.1208 0.1453 0.1810 -0.0040 0.0106  0.0204  142  VAL   A O   
3085 C  CB  . VAL   A 142 ? 0.1376 0.1552 0.1695 -0.0103 0.0071  0.0194  142  VAL   A CB  
3086 C  CG1 . VAL   A 142 ? 0.1366 0.1525 0.1743 -0.0187 0.0145  0.0146  142  VAL   A CG1 
3087 C  CG2 . VAL   A 142 ? 0.1487 0.1675 0.1810 -0.0051 0.0000  0.0209  142  VAL   A CG2 
3097 N  N   . CYS   A 143 ? 0.1174 0.1443 0.1719 -0.0137 0.0033  0.0246  143  CYS   A N   
3098 C  CA  . CYS   A 143 ? 0.1193 0.1386 0.1755 -0.0065 0.0091  0.0265  143  CYS   A CA  
3099 C  C   . CYS   A 143 ? 0.1195 0.1389 0.1769 -0.0092 0.0065  0.0318  143  CYS   A C   
3100 O  O   . CYS   A 143 ? 0.1154 0.1326 0.1861 -0.0041 0.0071  0.0311  143  CYS   A O   
3101 C  CB  . CYS   A 143 ? 0.1280 0.1376 0.1781 -0.0046 0.0184  0.0338  143  CYS   A CB  
3102 S  SG  . CYS   A 143 ? 0.1452 0.1482 0.1716 0.0038  0.0158  0.0258  143  CYS   A SG  
3108 N  N   . VAL   A 144 ? 0.1177 0.1453 0.1976 -0.0092 0.0082  0.0417  144  VAL   A N   
3109 C  CA  . VAL   A 144 ? 0.1228 0.1496 0.2373 -0.0123 0.0202  0.0419  144  VAL   A CA  
3110 C  C   . VAL   A 144 ? 0.1243 0.1394 0.2275 -0.0198 -0.0030 0.0347  144  VAL   A C   
3111 O  O   . VAL   A 144 ? 0.1364 0.1429 0.2336 -0.0052 -0.0143 0.0364  144  VAL   A O   
3112 C  CB  . VAL   A 144 ? 0.1501 0.1728 0.3023 0.0044  0.0346  0.0456  144  VAL   A CB  
3113 C  CG1 . VAL   A 144 ? 0.1654 0.1975 0.3426 -0.0036 0.0233  0.0391  144  VAL   A CG1 
3114 C  CG2 . VAL   A 144 ? 0.1400 0.1801 0.3085 0.0022  0.0466  0.0586  144  VAL   A CG2 
3124 N  N   . ASP   A 145 ? 0.1297 0.1368 0.2276 -0.0188 0.0031  0.0266  145  ASP   A N   
3125 C  CA  . ASP   A 145 ? 0.1404 0.1418 0.2340 -0.0253 -0.0053 0.0210  145  ASP   A CA  
3126 C  C   . ASP   A 145 ? 0.1419 0.1329 0.2261 -0.0139 0.0007  0.0025  145  ASP   A C   
3127 O  O   . ASP   A 145 ? 0.1559 0.1407 0.2808 -0.0180 -0.0016 -0.0218 145  ASP   A O   
3128 C  CB  . ASP   A 145 ? 0.1497 0.1692 0.2556 -0.0313 -0.0214 0.0196  145  ASP   A CB  
3129 C  CG  . ASP   A 145 ? 0.1669 0.2047 0.2875 -0.0488 -0.0318 0.0231  145  ASP   A CG  
3130 O  OD1 . ASP   A 145 ? 0.1654 0.2201 0.2929 -0.0554 -0.0177 0.0217  145  ASP   A OD1 
3131 O  OD2 . ASP   A 145 ? 0.1864 0.2286 0.3031 -0.0539 -0.0488 0.0240  145  ASP   A OD2 
3136 N  N   . THR   A 146 ? 0.1249 0.1248 0.2020 -0.0120 0.0109  0.0063  146  THR   A N   
3137 C  CA  . THR   A 146 ? 0.1206 0.1214 0.1743 -0.0055 0.0101  0.0032  146  THR   A CA  
3138 C  C   . THR   A 146 ? 0.1199 0.1230 0.1700 -0.0020 0.0103  0.0121  146  THR   A C   
3139 O  O   . THR   A 146 ? 0.1317 0.1373 0.1848 0.0049  0.0061  0.0093  146  THR   A O   
3140 C  CB  . THR   A 146 ? 0.1208 0.1299 0.1722 -0.0036 0.0059  0.0161  146  THR   A CB  
3141 O  OG1 . THR   A 146 ? 0.1179 0.1495 0.1808 -0.0036 0.0020  0.0138  146  THR   A OG1 
3142 C  CG2 . THR   A 146 ? 0.1222 0.1320 0.1956 -0.0086 0.0060  0.0107  146  THR   A CG2 
3150 N  N   . VAL   A 147 ? 0.1196 0.1277 0.1774 -0.0050 0.0117  0.0138  147  VAL   A N   
3151 C  CA  . VAL   A 147 ? 0.1193 0.1292 0.1656 -0.0089 0.0224  0.0225  147  VAL   A CA  
3152 C  C   . VAL   A 147 ? 0.1216 0.1285 0.1866 -0.0122 0.0193  0.0281  147  VAL   A C   
3153 O  O   . VAL   A 147 ? 0.1204 0.1396 0.2043 -0.0144 0.0112  0.0311  147  VAL   A O   
3154 C  CB  . VAL   A 147 ? 0.1336 0.1284 0.1642 -0.0132 0.0251  0.0258  147  VAL   A CB  
3155 C  CG1 . VAL   A 147 ? 0.1680 0.1386 0.1661 -0.0098 0.0223  0.0346  147  VAL   A CG1 
3156 C  CG2 . VAL   A 147 ? 0.1390 0.1305 0.1654 -0.0121 0.0120  0.0216  147  VAL   A CG2 
3166 N  N   . ARG   A 148 ? 0.1230 0.1265 0.2018 -0.0097 0.0145  0.0425  148  ARG   A N   
3167 C  CA  . ARG   A 148 ? 0.1315 0.1277 0.2007 -0.0093 0.0085  0.0471  148  ARG   A CA  
3168 C  C   . ARG   A 148 ? 0.1362 0.1298 0.1983 -0.0157 0.0132  0.0532  148  ARG   A C   
3169 O  O   . ARG   A 148 ? 0.1606 0.1456 0.2220 -0.0210 0.0219  0.0500  148  ARG   A O   
3170 C  CB  . ARG   A 148 ? 0.1367 0.1319 0.2135 -0.0064 0.0191  0.0434  148  ARG   A CB  
3171 C  CG  . ARG   A 148 ? 0.1504 0.1363 0.2366 -0.0102 0.0339  0.0270  148  ARG   A CG  
3172 C  CD  . ARG   A 148 ? 0.1646 0.1339 0.2605 -0.0060 0.0423  0.0439  148  ARG   A CD  
3173 N  NE  . ARG   A 148 ? 0.1528 0.1379 0.2578 0.0068  0.0481  0.0477  148  ARG   A NE  
3174 C  CZ  . ARG   A 148 ? 0.1582 0.1293 0.2424 0.0050  0.0522  0.0421  148  ARG   A CZ  
3175 N  NH1 . ARG   A 148 ? 0.1657 0.1333 0.2487 -0.0040 0.0457  0.0167  148  ARG   A NH1 
3176 N  NH2 . ARG   A 148 ? 0.1538 0.1481 0.2482 0.0161  0.0557  0.0494  148  ARG   A NH2 
3190 N  N   . THR   A 149 ? 0.1380 0.1403 0.1860 -0.0162 0.0109  0.0457  149  THR   A N   
3191 C  CA  . THR   A 149 ? 0.1392 0.1478 0.1847 -0.0112 0.0119  0.0479  149  THR   A CA  
3192 C  C   . THR   A 149 ? 0.1311 0.1495 0.1767 -0.0169 0.0109  0.0491  149  THR   A C   
3193 O  O   . THR   A 149 ? 0.1323 0.1539 0.1933 -0.0187 0.0121  0.0478  149  THR   A O   
3194 C  CB  . THR   A 149 ? 0.1372 0.1587 0.1882 -0.0093 0.0107  0.0424  149  THR   A CB  
3195 O  OG1 . THR   A 149 ? 0.1403 0.1521 0.1955 -0.0231 0.0078  0.0356  149  THR   A OG1 
3196 C  CG2 . THR   A 149 ? 0.1362 0.1731 0.2028 -0.0077 0.0032  0.0366  149  THR   A CG2 
3204 N  N   . ASN   A 150 ? 0.1354 0.1495 0.1805 -0.0073 0.0005  0.0551  150  ASN   A N   
3205 C  CA  . ASN   A 150 ? 0.1439 0.1610 0.1770 -0.0076 0.0143  0.0510  150  ASN   A CA  
3206 C  C   . ASN   A 150 ? 0.1297 0.1513 0.1815 -0.0143 0.0086  0.0452  150  ASN   A C   
3207 O  O   . ASN   A 150 ? 0.1450 0.1601 0.2067 -0.0117 -0.0105 0.0356  150  ASN   A O   
3208 C  CB  . ASN   A 150 ? 0.1803 0.1912 0.2004 -0.0128 0.0364  0.0725  150  ASN   A CB  
3209 C  CG  . ASN   A 150 ? 0.2352 0.2252 0.2759 -0.0079 0.0150  0.0839  150  ASN   A CG  
3210 O  OD1 . ASN   A 150 ? 0.2575 0.2397 0.2969 -0.0152 0.0193  0.0993  150  ASN   A OD1 
3211 N  ND2 . ASN   A 150 ? 0.2671 0.2449 0.3135 -0.0058 -0.0016 0.0817  150  ASN   A ND2 
3218 N  N   . VAL   A 151 ? 0.1321 0.1411 0.1759 -0.0140 0.0081  0.0464  151  VAL   A N   
3219 C  CA  . VAL   A 151 ? 0.1388 0.1441 0.1637 -0.0184 0.0099  0.0408  151  VAL   A CA  
3220 C  C   . VAL   A 151 ? 0.1300 0.1397 0.1742 -0.0227 0.0127  0.0451  151  VAL   A C   
3221 O  O   . VAL   A 151 ? 0.1373 0.1478 0.2003 -0.0192 0.0108  0.0388  151  VAL   A O   
3222 C  CB  . VAL   A 151 ? 0.1664 0.1614 0.1653 -0.0053 0.0062  0.0349  151  VAL   A CB  
3223 C  CG1 . VAL   A 151 ? 0.1585 0.1798 0.1975 -0.0062 0.0032  0.0323  151  VAL   A CG1 
3224 C  CG2 . VAL   A 151 ? 0.1798 0.1546 0.1718 0.0018  0.0201  0.0287  151  VAL   A CG2 
3234 N  N   . TYR   A 152 ? 0.1266 0.1404 0.1730 -0.0218 0.0135  0.0398  152  TYR   A N   
3235 C  CA  . TYR   A 152 ? 0.1290 0.1444 0.1560 -0.0190 0.0124  0.0373  152  TYR   A CA  
3236 C  C   . TYR   A 152 ? 0.1272 0.1354 0.1558 -0.0199 0.0181  0.0358  152  TYR   A C   
3237 O  O   . TYR   A 152 ? 0.1355 0.1410 0.1602 -0.0256 0.0177  0.0329  152  TYR   A O   
3238 C  CB  . TYR   A 152 ? 0.1407 0.1481 0.1592 -0.0139 0.0189  0.0417  152  TYR   A CB  
3239 C  CG  . TYR   A 152 ? 0.1540 0.1650 0.1628 -0.0202 0.0287  0.0428  152  TYR   A CG  
3240 C  CD1 . TYR   A 152 ? 0.1630 0.1852 0.1749 -0.0101 0.0249  0.0519  152  TYR   A CD1 
3241 C  CD2 . TYR   A 152 ? 0.1579 0.1786 0.1635 -0.0333 0.0212  0.0419  152  TYR   A CD2 
3242 C  CE1 . TYR   A 152 ? 0.1847 0.1966 0.1856 -0.0082 0.0065  0.0637  152  TYR   A CE1 
3243 C  CE2 . TYR   A 152 ? 0.1782 0.1942 0.1702 -0.0367 0.0196  0.0512  152  TYR   A CE2 
3244 C  CZ  . TYR   A 152 ? 0.1999 0.1996 0.1801 -0.0227 0.0100  0.0678  152  TYR   A CZ  
3245 O  OH  . TYR   A 152 ? 0.2298 0.2189 0.2112 -0.0147 0.0116  0.0794  152  TYR   A OH  
3255 N  N   A LEU   A 153 ? 0.1253 0.1286 0.1737 -0.0218 0.0201  0.0427  153  LEU   A N   
3256 N  N   B LEU   A 153 ? 0.1289 0.1402 0.1524 -0.0201 0.0122  0.0341  153  LEU   A N   
3257 C  CA  A LEU   A 153 ? 0.1234 0.1196 0.1828 -0.0097 0.0225  0.0417  153  LEU   A CA  
3258 C  CA  B LEU   A 153 ? 0.1280 0.1388 0.1428 -0.0086 0.0139  0.0249  153  LEU   A CA  
3259 C  C   A LEU   A 153 ? 0.1248 0.1229 0.1773 -0.0101 0.0317  0.0264  153  LEU   A C   
3260 C  C   B LEU   A 153 ? 0.1293 0.1443 0.1291 -0.0061 0.0171  0.0169  153  LEU   A C   
3261 O  O   A LEU   A 153 ? 0.1293 0.1355 0.2074 -0.0132 0.0423  0.0183  153  LEU   A O   
3262 O  O   B LEU   A 153 ? 0.1313 0.1531 0.1520 -0.0074 0.0265  0.0278  153  LEU   A O   
3263 C  CB  A LEU   A 153 ? 0.1152 0.1197 0.1853 -0.0088 0.0123  0.0421  153  LEU   A CB  
3264 C  CB  B LEU   A 153 ? 0.1245 0.1393 0.1453 0.0021  0.0097  0.0303  153  LEU   A CB  
3265 C  CG  A LEU   A 153 ? 0.1156 0.1264 0.1764 -0.0158 0.0133  0.0296  153  LEU   A CG  
3266 C  CG  B LEU   A 153 ? 0.1295 0.1448 0.1407 0.0051  0.0046  0.0281  153  LEU   A CG  
3267 C  CD1 A LEU   A 153 ? 0.1246 0.1231 0.1868 -0.0143 0.0115  0.0305  153  LEU   A CD1 
3268 C  CD1 B LEU   A 153 ? 0.1303 0.1445 0.1406 0.0128  0.0054  0.0299  153  LEU   A CD1 
3269 C  CD2 A LEU   A 153 ? 0.1245 0.1384 0.1664 -0.0171 0.0213  0.0225  153  LEU   A CD2 
3270 C  CD2 B LEU   A 153 ? 0.1396 0.1534 0.1502 -0.0006 0.0045  0.0219  153  LEU   A CD2 
3293 N  N   A ALA   A 154 ? 0.1230 0.1167 0.1575 -0.0133 0.0314  0.0278  154  ALA   A N   
3294 N  N   B ALA   A 154 ? 0.1334 0.1414 0.1109 -0.0058 0.0076  0.0122  154  ALA   A N   
3295 C  CA  A ALA   A 154 ? 0.1317 0.1233 0.1604 -0.0134 0.0301  0.0223  154  ALA   A CA  
3296 C  CA  B ALA   A 154 ? 0.1381 0.1424 0.1144 -0.0070 0.0053  0.0102  154  ALA   A CA  
3297 C  C   A ALA   A 154 ? 0.1395 0.1186 0.1614 -0.0072 0.0261  0.0229  154  ALA   A C   
3298 C  C   B ALA   A 154 ? 0.1406 0.1429 0.1030 -0.0097 0.0014  0.0220  154  ALA   A C   
3299 O  O   A ALA   A 154 ? 0.1480 0.1363 0.1630 -0.0123 0.0245  0.0153  154  ALA   A O   
3300 O  O   B ALA   A 154 ? 0.1501 0.1518 0.0952 -0.0114 0.0100  0.0328  154  ALA   A O   
3301 C  CB  A ALA   A 154 ? 0.1422 0.1307 0.1675 -0.0065 0.0232  0.0137  154  ALA   A CB  
3302 C  CB  B ALA   A 154 ? 0.1430 0.1400 0.1288 -0.0097 -0.0112 -0.0009 154  ALA   A CB  
3313 N  N   A VAL   A 155 ? 0.1441 0.1223 0.1688 0.0012  0.0246  0.0286  155  VAL   A N   
3314 N  N   B VAL   A 155 ? 0.1411 0.1384 0.1161 -0.0093 -0.0071 0.0196  155  VAL   A N   
3315 C  CA  A VAL   A 155 ? 0.1553 0.1283 0.1928 -0.0025 0.0182  0.0380  155  VAL   A CA  
3316 C  CA  B VAL   A 155 ? 0.1572 0.1400 0.1246 -0.0042 -0.0179 0.0240  155  VAL   A CA  
3317 C  C   A VAL   A 155 ? 0.1683 0.1396 0.2215 0.0114  0.0333  0.0522  155  VAL   A C   
3318 C  C   B VAL   A 155 ? 0.1644 0.1475 0.1551 0.0028  -0.0178 0.0248  155  VAL   A C   
3319 O  O   A VAL   A 155 ? 0.1645 0.1436 0.2306 0.0189  0.0437  0.0430  155  VAL   A O   
3320 O  O   B VAL   A 155 ? 0.1610 0.1573 0.1570 0.0062  -0.0290 0.0192  155  VAL   A O   
3321 C  CB  A VAL   A 155 ? 0.1635 0.1318 0.1955 -0.0035 -0.0030 0.0307  155  VAL   A CB  
3322 C  CB  B VAL   A 155 ? 0.1671 0.1364 0.1337 -0.0125 -0.0228 0.0139  155  VAL   A CB  
3323 C  CG1 A VAL   A 155 ? 0.1785 0.1421 0.1911 -0.0007 -0.0054 0.0270  155  VAL   A CG1 
3324 C  CG1 B VAL   A 155 ? 0.1666 0.1338 0.1420 -0.0177 -0.0340 0.0084  155  VAL   A CG1 
3325 C  CG2 A VAL   A 155 ? 0.1752 0.1392 0.2114 0.0060  -0.0150 0.0226  155  VAL   A CG2 
3326 C  CG2 B VAL   A 155 ? 0.1748 0.1354 0.1409 -0.0181 -0.0298 0.0080  155  VAL   A CG2 
3345 N  N   A PHE   A 156 ? 0.1854 0.1501 0.2563 0.0127  0.0386  0.0677  156  PHE   A N   
3346 N  N   B PHE   A 156 ? 0.1715 0.1467 0.1630 0.0099  -0.0020 0.0248  156  PHE   A N   
3347 C  CA  A PHE   A 156 ? 0.2070 0.1602 0.2969 0.0186  0.0404  0.0776  156  PHE   A CA  
3348 C  CA  B PHE   A 156 ? 0.1908 0.1603 0.1883 0.0234  0.0094  0.0369  156  PHE   A CA  
3349 C  C   A PHE   A 156 ? 0.2140 0.1704 0.3190 0.0243  0.0445  0.0831  156  PHE   A C   
3350 C  C   B PHE   A 156 ? 0.1854 0.1709 0.1989 0.0288  0.0101  0.0538  156  PHE   A C   
3351 O  O   A PHE   A 156 ? 0.2258 0.1842 0.3334 0.0197  0.0581  0.0632  156  PHE   A O   
3352 O  O   B PHE   A 156 ? 0.1905 0.1792 0.2149 0.0234  0.0154  0.0438  156  PHE   A O   
3353 C  CB  A PHE   A 156 ? 0.2231 0.1612 0.3118 0.0204  0.0357  0.0867  156  PHE   A CB  
3354 C  CB  B PHE   A 156 ? 0.2172 0.1703 0.2098 0.0262  0.0139  0.0301  156  PHE   A CB  
3355 C  CG  A PHE   A 156 ? 0.2382 0.1697 0.3188 0.0297  0.0305  0.0878  156  PHE   A CG  
3356 C  CG  B PHE   A 156 ? 0.2424 0.1864 0.2556 0.0357  0.0102  0.0124  156  PHE   A CG  
3357 C  CD1 A PHE   A 156 ? 0.2459 0.1767 0.3322 0.0300  0.0305  0.0763  156  PHE   A CD1 
3358 C  CD1 B PHE   A 156 ? 0.2529 0.1913 0.2701 0.0405  0.0150  0.0040  156  PHE   A CD1 
3359 C  CD2 A PHE   A 156 ? 0.2458 0.1811 0.3215 0.0425  0.0333  0.0969  156  PHE   A CD2 
3360 C  CD2 B PHE   A 156 ? 0.2557 0.1986 0.2776 0.0408  0.0089  0.0027  156  PHE   A CD2 
3361 C  CE1 A PHE   A 156 ? 0.2512 0.1833 0.3433 0.0350  0.0364  0.0644  156  PHE   A CE1 
3362 C  CE1 B PHE   A 156 ? 0.2621 0.1995 0.2891 0.0428  0.0174  -0.0023 156  PHE   A CE1 
3363 C  CE2 A PHE   A 156 ? 0.2542 0.1915 0.3341 0.0454  0.0344  0.0819  156  PHE   A CE2 
3364 C  CE2 B PHE   A 156 ? 0.2625 0.2044 0.2939 0.0434  0.0134  -0.0054 156  PHE   A CE2 
3365 C  CZ  A PHE   A 156 ? 0.2523 0.1914 0.3422 0.0437  0.0360  0.0625  156  PHE   A CZ  
3366 C  CZ  B PHE   A 156 ? 0.2671 0.2063 0.2997 0.0440  0.0161  -0.0064 156  PHE   A CZ  
3385 N  N   A ASP   A 157 ? 0.2139 0.1815 0.3248 0.0229  0.0292  0.1004  157  ASP   A N   
3386 N  N   B ASP   A 157 ? 0.1786 0.1737 0.2032 0.0309  0.0076  0.0625  157  ASP   A N   
3387 C  CA  A ASP   A 157 ? 0.2199 0.2007 0.3287 0.0220  0.0232  0.1041  157  ASP   A CA  
3388 C  CA  B ASP   A 157 ? 0.1829 0.1903 0.2286 0.0322  0.0000  0.0759  157  ASP   A CA  
3389 C  C   A ASP   A 157 ? 0.2006 0.2008 0.3372 0.0274  0.0379  0.1136  157  ASP   A C   
3390 C  C   B ASP   A 157 ? 0.1779 0.1994 0.2444 0.0386  0.0042  0.0783  157  ASP   A C   
3391 O  O   A ASP   A 157 ? 0.1881 0.1898 0.3323 0.0284  0.0383  0.1154  157  ASP   A O   
3392 O  O   B ASP   A 157 ? 0.1675 0.1945 0.2409 0.0433  0.0044  0.0765  157  ASP   A O   
3393 C  CB  A ASP   A 157 ? 0.2421 0.2162 0.3353 0.0283  0.0070  0.0993  157  ASP   A CB  
3394 C  CB  B ASP   A 157 ? 0.1891 0.1994 0.2387 0.0312  -0.0088 0.0769  157  ASP   A CB  
3395 C  CG  A ASP   A 157 ? 0.2651 0.2330 0.3489 0.0372  -0.0045 0.0909  157  ASP   A CG  
3396 C  CG  B ASP   A 157 ? 0.1884 0.2041 0.2458 0.0327  -0.0176 0.0854  157  ASP   A CG  
3397 O  OD1 A ASP   A 157 ? 0.2812 0.2427 0.3715 0.0362  -0.0080 0.0771  157  ASP   A OD1 
3398 O  OD1 B ASP   A 157 ? 0.1864 0.2009 0.2599 0.0324  -0.0162 0.0811  157  ASP   A OD1 
3399 O  OD2 A ASP   A 157 ? 0.2682 0.2342 0.3442 0.0406  -0.0069 0.0952  157  ASP   A OD2 
3400 O  OD2 B ASP   A 157 ? 0.1912 0.2145 0.2526 0.0369  -0.0169 0.0952  157  ASP   A OD2 
3409 N  N   A LYS   A 158 ? 0.2014 0.2165 0.3617 0.0327  0.0487  0.1081  158  LYS   A N   
3410 N  N   B LYS   A 158 ? 0.1883 0.2134 0.2732 0.0381  0.0103  0.0783  158  LYS   A N   
3411 C  CA  A LYS   A 158 ? 0.1978 0.2382 0.3725 0.0421  0.0620  0.1089  158  LYS   A CA  
3412 C  CA  B LYS   A 158 ? 0.1975 0.2231 0.2963 0.0366  0.0104  0.0768  158  LYS   A CA  
3413 C  C   A LYS   A 158 ? 0.1796 0.2466 0.3653 0.0433  0.0573  0.1284  158  LYS   A C   
3414 C  C   B LYS   A 158 ? 0.1904 0.2138 0.2887 0.0368  0.0059  0.0901  158  LYS   A C   
3415 O  O   A LYS   A 158 ? 0.1734 0.2426 0.3671 0.0320  0.0583  0.1401  158  LYS   A O   
3416 O  O   B LYS   A 158 ? 0.1905 0.2161 0.2871 0.0373  0.0103  0.0906  158  LYS   A O   
3417 C  CB  A LYS   A 158 ? 0.2083 0.2536 0.3813 0.0505  0.0773  0.1020  158  LYS   A CB  
3418 C  CB  B LYS   A 158 ? 0.2134 0.2395 0.3286 0.0282  0.0180  0.0562  158  LYS   A CB  
3419 C  CG  A LYS   A 158 ? 0.2186 0.2730 0.3946 0.0530  0.0874  0.0934  158  LYS   A CG  
3420 C  CG  B LYS   A 158 ? 0.2290 0.2539 0.3556 0.0215  0.0170  0.0391  158  LYS   A CG  
3421 C  CD  A LYS   A 158 ? 0.2225 0.2901 0.3967 0.0506  0.1056  0.0911  158  LYS   A CD  
3422 C  CD  B LYS   A 158 ? 0.2404 0.2659 0.3764 0.0190  0.0170  0.0271  158  LYS   A CD  
3423 C  CE  A LYS   A 158 ? 0.2253 0.3033 0.4035 0.0448  0.1193  0.0912  158  LYS   A CE  
3424 C  CE  B LYS   A 158 ? 0.2468 0.2714 0.3930 0.0223  0.0135  0.0201  158  LYS   A CE  
3425 N  NZ  A LYS   A 158 ? 0.2291 0.3084 0.4056 0.0374  0.1218  0.0985  158  LYS   A NZ  
3426 N  NZ  B LYS   A 158 ? 0.2485 0.2730 0.3993 0.0259  0.0086  0.0158  158  LYS   A NZ  
3453 N  N   A ASN   A 159 ? 0.1802 0.2603 0.3674 0.0449  0.0434  0.1343  159  ASN   A N   
3454 N  N   B ASN   A 159 ? 0.1918 0.2076 0.2955 0.0275  -0.0070 0.0898  159  ASN   A N   
3455 C  CA  A ASN   A 159 ? 0.1735 0.2719 0.3666 0.0457  0.0181  0.1455  159  ASN   A CA  
3456 C  CA  B ASN   A 159 ? 0.1937 0.2025 0.2999 0.0112  -0.0136 0.0891  159  ASN   A CA  
3457 C  C   A ASN   A 159 ? 0.1574 0.2664 0.3272 0.0277  0.0094  0.1353  159  ASN   A C   
3458 C  C   B ASN   A 159 ? 0.1813 0.1984 0.2786 -0.0017 -0.0107 0.0654  159  ASN   A C   
3459 O  O   A ASN   A 159 ? 0.1466 0.2730 0.3251 0.0221  0.0087  0.1401  159  ASN   A O   
3460 O  O   B ASN   A 159 ? 0.1774 0.1878 0.2782 -0.0045 -0.0153 0.0552  159  ASN   A O   
3461 C  CB  A ASN   A 159 ? 0.1916 0.2912 0.4132 0.0463  0.0160  0.1541  159  ASN   A CB  
3462 C  CB  B ASN   A 159 ? 0.2142 0.2099 0.3334 0.0045  -0.0153 0.1045  159  ASN   A CB  
3463 C  CG  A ASN   A 159 ? 0.2097 0.3060 0.4623 0.0434  0.0200  0.1519  159  ASN   A CG  
3464 C  CG  B ASN   A 159 ? 0.2347 0.2202 0.3727 0.0025  -0.0073 0.1087  159  ASN   A CG  
3465 O  OD1 A ASN   A 159 ? 0.2171 0.3103 0.4806 0.0440  0.0254  0.1519  159  ASN   A OD1 
3466 O  OD1 B ASN   A 159 ? 0.2488 0.2241 0.3916 0.0008  -0.0081 0.1078  159  ASN   A OD1 
3467 N  ND2 A ASN   A 159 ? 0.2185 0.3142 0.4859 0.0386  0.0213  0.1445  159  ASN   A ND2 
3468 N  ND2 B ASN   A 159 ? 0.2358 0.2282 0.3878 0.0036  0.0057  0.1087  159  ASN   A ND2 
3481 N  N   A LEU   A 160 ? 0.1483 0.2508 0.2940 0.0147  -0.0054 0.1213  160  LEU   A N   
3482 N  N   B LEU   A 160 ? 0.1713 0.2002 0.2489 -0.0060 -0.0105 0.0543  160  LEU   A N   
3483 C  CA  A LEU   A 160 ? 0.1492 0.2385 0.2681 -0.0011 -0.0026 0.0992  160  LEU   A CA  
3484 C  CA  B LEU   A 160 ? 0.1605 0.1980 0.2157 -0.0093 -0.0106 0.0442  160  LEU   A CA  
3485 C  C   A LEU   A 160 ? 0.1348 0.2272 0.2656 -0.0034 0.0034  0.0894  160  LEU   A C   
3486 C  C   B LEU   A 160 ? 0.1419 0.1878 0.2005 -0.0108 0.0021  0.0317  160  LEU   A C   
3487 O  O   A LEU   A 160 ? 0.1251 0.2344 0.2857 -0.0127 0.0019  0.0737  160  LEU   A O   
3488 O  O   B LEU   A 160 ? 0.1436 0.1934 0.2010 -0.0096 -0.0090 0.0194  160  LEU   A O   
3489 C  CB  A LEU   A 160 ? 0.1528 0.2359 0.2376 -0.0102 -0.0062 0.0921  160  LEU   A CB  
3490 C  CB  B LEU   A 160 ? 0.1708 0.2091 0.2036 -0.0094 -0.0117 0.0460  160  LEU   A CB  
3491 C  CG  A LEU   A 160 ? 0.1616 0.2380 0.2271 -0.0254 0.0020  0.0713  160  LEU   A CG  
3492 C  CG  B LEU   A 160 ? 0.1788 0.2222 0.1990 -0.0074 -0.0122 0.0339  160  LEU   A CG  
3493 C  CD1 A LEU   A 160 ? 0.1712 0.2433 0.2298 -0.0315 -0.0013 0.0600  160  LEU   A CD1 
3494 C  CD1 B LEU   A 160 ? 0.1821 0.2256 0.1962 -0.0101 -0.0110 0.0336  160  LEU   A CD1 
3495 C  CD2 A LEU   A 160 ? 0.1613 0.2381 0.2219 -0.0277 0.0076  0.0646  160  LEU   A CD2 
3496 C  CD2 B LEU   A 160 ? 0.1817 0.2289 0.1961 -0.0083 -0.0064 0.0287  160  LEU   A CD2 
3519 N  N   A TYR   A 161 ? 0.1364 0.2113 0.2503 0.0002  0.0042  0.0907  161  TYR   A N   
3520 N  N   B TYR   A 161 ? 0.1343 0.1741 0.1884 -0.0045 0.0156  0.0362  161  TYR   A N   
3521 C  CA  A TYR   A 161 ? 0.1466 0.1991 0.2482 0.0046  0.0066  0.0938  161  TYR   A CA  
3522 C  CA  B TYR   A 161 ? 0.1379 0.1685 0.1824 0.0055  0.0204  0.0327  161  TYR   A CA  
3523 C  C   A TYR   A 161 ? 0.1407 0.2002 0.2639 0.0079  0.0161  0.0871  161  TYR   A C   
3524 C  C   B TYR   A 161 ? 0.1370 0.1763 0.1864 0.0045  0.0233  0.0351  161  TYR   A C   
3525 O  O   A TYR   A 161 ? 0.1370 0.2014 0.2599 0.0081  0.0223  0.0699  161  TYR   A O   
3526 O  O   B TYR   A 161 ? 0.1300 0.1738 0.1856 0.0057  0.0238  0.0278  161  TYR   A O   
3527 C  CB  A TYR   A 161 ? 0.1593 0.1939 0.2452 0.0035  0.0072  0.0787  161  TYR   A CB  
3528 C  CB  B TYR   A 161 ? 0.1368 0.1663 0.1877 0.0111  0.0237  0.0206  161  TYR   A CB  
3529 C  CG  A TYR   A 161 ? 0.1644 0.1952 0.2457 -0.0034 0.0097  0.0598  161  TYR   A CG  
3530 C  CG  B TYR   A 161 ? 0.1283 0.1657 0.1873 0.0120  0.0343  0.0155  161  TYR   A CG  
3531 C  CD1 A TYR   A 161 ? 0.1648 0.1947 0.2509 -0.0051 0.0091  0.0539  161  TYR   A CD1 
3532 C  CD1 B TYR   A 161 ? 0.1244 0.1599 0.1878 0.0073  0.0325  0.0141  161  TYR   A CD1 
3533 C  CD2 A TYR   A 161 ? 0.1675 0.2042 0.2432 0.0022  0.0036  0.0467  161  TYR   A CD2 
3534 C  CD2 B TYR   A 161 ? 0.1279 0.1726 0.1958 0.0191  0.0360  0.0211  161  TYR   A CD2 
3535 C  CE1 A TYR   A 161 ? 0.1734 0.1909 0.2497 -0.0062 0.0010  0.0571  161  TYR   A CE1 
3536 C  CE1 B TYR   A 161 ? 0.1305 0.1661 0.2005 0.0053  0.0296  0.0164  161  TYR   A CE1 
3537 C  CE2 A TYR   A 161 ? 0.1709 0.2002 0.2444 0.0001  0.0000  0.0493  161  TYR   A CE2 
3538 C  CE2 B TYR   A 161 ? 0.1308 0.1735 0.2105 0.0126  0.0386  0.0332  161  TYR   A CE2 
3539 C  CZ  A TYR   A 161 ? 0.1770 0.1910 0.2502 -0.0082 -0.0058 0.0595  161  TYR   A CZ  
3540 C  CZ  B TYR   A 161 ? 0.1395 0.1745 0.2175 0.0093  0.0304  0.0320  161  TYR   A CZ  
3541 O  OH  A TYR   A 161 ? 0.1882 0.1912 0.2665 -0.0145 -0.0080 0.0617  161  TYR   A OH  
3542 O  OH  B TYR   A 161 ? 0.1546 0.1874 0.2463 0.0073  0.0235  0.0412  161  TYR   A OH  
3561 N  N   A ASP   A 162 ? 0.1432 0.2055 0.2912 0.0052  0.0272  0.0924  162  ASP   A N   
3562 N  N   B ASP   A 162 ? 0.1390 0.1912 0.2055 0.0000  0.0271  0.0447  162  ASP   A N   
3563 C  CA  A ASP   A 162 ? 0.1392 0.2218 0.3052 0.0009  0.0337  0.0996  162  ASP   A CA  
3564 C  CA  B ASP   A 162 ? 0.1443 0.2104 0.2336 0.0039  0.0248  0.0372  162  ASP   A CA  
3565 C  C   A ASP   A 162 ? 0.1341 0.2458 0.3073 -0.0029 0.0272  0.0969  162  ASP   A C   
3566 C  C   B ASP   A 162 ? 0.1443 0.2207 0.2415 0.0040  0.0150  0.0352  162  ASP   A C   
3567 O  O   A ASP   A 162 ? 0.1318 0.2442 0.3290 -0.0224 0.0215  0.0924  162  ASP   A O   
3568 O  O   B ASP   A 162 ? 0.1466 0.2209 0.2580 0.0003  0.0175  0.0261  162  ASP   A O   
3569 C  CB  A ASP   A 162 ? 0.1451 0.2245 0.3234 0.0016  0.0468  0.0912  162  ASP   A CB  
3570 C  CB  B ASP   A 162 ? 0.1546 0.2200 0.2700 0.0116  0.0293  0.0345  162  ASP   A CB  
3571 C  CG  A ASP   A 162 ? 0.1577 0.2313 0.3537 0.0169  0.0482  0.0740  162  ASP   A CG  
3572 C  CG  B ASP   A 162 ? 0.1615 0.2252 0.2994 0.0140  0.0359  0.0365  162  ASP   A CG  
3573 O  OD1 A ASP   A 162 ? 0.1776 0.2374 0.3683 0.0176  0.0455  0.0682  162  ASP   A OD1 
3574 O  OD1 B ASP   A 162 ? 0.1735 0.2242 0.3059 0.0178  0.0412  0.0384  162  ASP   A OD1 
3575 O  OD2 A ASP   A 162 ? 0.1664 0.2380 0.3641 0.0280  0.0612  0.0662  162  ASP   A OD2 
3576 O  OD2 B ASP   A 162 ? 0.1663 0.2317 0.3184 0.0175  0.0343  0.0369  162  ASP   A OD2 
3585 N  N   A LYS   A 163 ? 0.1402 0.2702 0.3105 0.0058  0.0047  0.0891  163  LYS   A N   
3586 N  N   B LYS   A 163 ? 0.1526 0.2382 0.2451 0.0043  -0.0003 0.0306  163  LYS   A N   
3587 C  CA  A LYS   A 163 ? 0.1550 0.2919 0.3052 -0.0002 -0.0040 0.0795  163  LYS   A CA  
3588 C  CA  B LYS   A 163 ? 0.1660 0.2572 0.2494 -0.0042 -0.0083 0.0240  163  LYS   A CA  
3589 C  C   A LYS   A 163 ? 0.1490 0.2802 0.2829 -0.0101 0.0130  0.0652  163  LYS   A C   
3590 C  C   B LYS   A 163 ? 0.1526 0.2432 0.2205 -0.0148 -0.0052 0.0114  163  LYS   A C   
3591 O  O   A LYS   A 163 ? 0.1500 0.2994 0.2988 -0.0204 0.0076  0.0556  163  LYS   A O   
3592 O  O   B LYS   A 163 ? 0.1436 0.2390 0.2216 -0.0320 -0.0043 -0.0081 163  LYS   A O   
3593 C  CB  A LYS   A 163 ? 0.1818 0.3204 0.3352 0.0049  -0.0236 0.0781  163  LYS   A CB  
3594 C  CB  B LYS   A 163 ? 0.1968 0.2852 0.2951 -0.0011 -0.0125 0.0318  163  LYS   A CB  
3595 C  CG  A LYS   A 163 ? 0.2147 0.3452 0.3725 0.0006  -0.0211 0.0750  163  LYS   A CG  
3596 C  CG  B LYS   A 163 ? 0.2253 0.3074 0.3380 -0.0048 -0.0081 0.0385  163  LYS   A CG  
3597 C  CD  A LYS   A 163 ? 0.2433 0.3643 0.4146 -0.0037 -0.0220 0.0718  163  LYS   A CD  
3598 C  CD  B LYS   A 163 ? 0.2456 0.3254 0.3779 -0.0067 -0.0091 0.0448  163  LYS   A CD  
3599 C  CE  A LYS   A 163 ? 0.2603 0.3760 0.4420 -0.0072 -0.0194 0.0719  163  LYS   A CE  
3600 C  CE  B LYS   A 163 ? 0.2568 0.3380 0.4072 -0.0091 -0.0090 0.0496  163  LYS   A CE  
3601 N  NZ  A LYS   A 163 ? 0.2673 0.3821 0.4586 -0.0096 -0.0177 0.0727  163  LYS   A NZ  
3602 N  NZ  B LYS   A 163 ? 0.2622 0.3444 0.4191 -0.0103 -0.0099 0.0550  163  LYS   A NZ  
3629 N  N   A LEU   A 164 ? 0.1358 0.2521 0.2558 -0.0155 0.0158  0.0582  164  LEU   A N   
3630 N  N   B LEU   A 164 ? 0.1378 0.2223 0.1951 -0.0122 -0.0027 0.0164  164  LEU   A N   
3631 C  CA  A LEU   A 164 ? 0.1328 0.2289 0.2416 -0.0217 0.0269  0.0483  164  LEU   A CA  
3632 C  CA  B LEU   A 164 ? 0.1383 0.2028 0.1861 -0.0157 0.0069  0.0170  164  LEU   A CA  
3633 C  C   A LEU   A 164 ? 0.1380 0.2194 0.2440 -0.0205 0.0348  0.0408  164  LEU   A C   
3634 C  C   B LEU   A 164 ? 0.1423 0.1951 0.1853 -0.0180 0.0177  0.0070  164  LEU   A C   
3635 O  O   A LEU   A 164 ? 0.1421 0.2173 0.2466 -0.0274 0.0536  0.0147  164  LEU   A O   
3636 O  O   B LEU   A 164 ? 0.1496 0.1953 0.1905 -0.0236 0.0261  -0.0078 164  LEU   A O   
3637 C  CB  A LEU   A 164 ? 0.1285 0.2199 0.2394 -0.0285 0.0300  0.0552  164  LEU   A CB  
3638 C  CB  B LEU   A 164 ? 0.1357 0.1927 0.1825 -0.0076 0.0060  0.0181  164  LEU   A CB  
3639 C  CG  A LEU   A 164 ? 0.1307 0.2189 0.2509 -0.0253 0.0234  0.0502  164  LEU   A CG  
3640 C  CG  B LEU   A 164 ? 0.1460 0.1888 0.1968 -0.0036 0.0019  0.0154  164  LEU   A CG  
3641 C  CD1 A LEU   A 164 ? 0.1291 0.2175 0.2556 -0.0239 0.0161  0.0455  164  LEU   A CD1 
3642 C  CD1 B LEU   A 164 ? 0.1425 0.1832 0.1982 -0.0013 0.0002  0.0148  164  LEU   A CD1 
3643 C  CD2 A LEU   A 164 ? 0.1448 0.2265 0.2604 -0.0223 0.0281  0.0430  164  LEU   A CD2 
3644 C  CD2 B LEU   A 164 ? 0.1590 0.1918 0.2021 -0.0069 0.0087  0.0135  164  LEU   A CD2 
3667 N  N   A VAL   A 165 ? 0.1371 0.2127 0.2420 -0.0156 0.0310  0.0461  165  VAL   A N   
3668 N  N   B VAL   A 165 ? 0.1359 0.1936 0.1836 -0.0142 0.0200  0.0174  165  VAL   A N   
3669 C  CA  A VAL   A 165 ? 0.1402 0.2133 0.2431 -0.0117 0.0392  0.0471  165  VAL   A CA  
3670 C  CA  B VAL   A 165 ? 0.1464 0.1991 0.1884 -0.0097 0.0259  0.0237  165  VAL   A CA  
3671 C  C   A VAL   A 165 ? 0.1303 0.2302 0.2409 -0.0098 0.0366  0.0544  165  VAL   A C   
3672 C  C   B VAL   A 165 ? 0.1399 0.2095 0.1887 -0.0125 0.0275  0.0220  165  VAL   A C   
3673 O  O   A VAL   A 165 ? 0.1320 0.2274 0.2305 -0.0037 0.0397  0.0447  165  VAL   A O   
3674 O  O   B VAL   A 165 ? 0.1451 0.2092 0.1753 -0.0129 0.0303  0.0119  165  VAL   A O   
3675 C  CB  A VAL   A 165 ? 0.1550 0.2020 0.2465 -0.0062 0.0444  0.0366  165  VAL   A CB  
3676 C  CB  B VAL   A 165 ? 0.1650 0.2003 0.1952 -0.0055 0.0277  0.0282  165  VAL   A CB  
3677 C  CG1 A VAL   A 165 ? 0.1580 0.1998 0.2533 -0.0082 0.0483  0.0338  165  VAL   A CG1 
3678 C  CG1 B VAL   A 165 ? 0.1699 0.2049 0.2047 -0.0064 0.0315  0.0207  165  VAL   A CG1 
3679 C  CG2 A VAL   A 165 ? 0.1676 0.2013 0.2528 -0.0051 0.0480  0.0346  165  VAL   A CG2 
3680 C  CG2 B VAL   A 165 ? 0.1705 0.1957 0.1922 -0.0007 0.0268  0.0304  165  VAL   A CG2 
3699 N  N   A SER   A 166 ? 0.1264 0.2491 0.2616 -0.0166 0.0207  0.0660  166  SER   A N   
3700 N  N   B SER   A 166 ? 0.1266 0.2284 0.2129 -0.0148 0.0275  0.0256  166  SER   A N   
3701 C  CA  A SER   A 166 ? 0.1335 0.2758 0.2631 -0.0224 0.0107  0.0671  166  SER   A CA  
3702 C  CA  B SER   A 166 ? 0.1348 0.2581 0.2357 -0.0151 0.0114  0.0154  166  SER   A CA  
3703 C  C   A SER   A 166 ? 0.1404 0.3069 0.2538 -0.0155 -0.0146 0.0575  166  SER   A C   
3704 C  C   B SER   A 166 ? 0.1420 0.2806 0.2287 -0.0189 0.0000  0.0171  166  SER   A C   
3705 O  O   A SER   A 166 ? 0.1507 0.3281 0.2638 -0.0249 -0.0178 0.0397  166  SER   A O   
3706 O  O   B SER   A 166 ? 0.1554 0.2926 0.2182 -0.0207 -0.0063 0.0106  166  SER   A O   
3707 C  CB  A SER   A 166 ? 0.1559 0.2758 0.2778 -0.0260 0.0183  0.0744  166  SER   A CB  
3708 C  CB  B SER   A 166 ? 0.1458 0.2684 0.2703 -0.0090 -0.0033 0.0048  166  SER   A CB  
3709 O  OG  A SER   A 166 ? 0.1948 0.2800 0.3194 -0.0273 0.0090  0.0690  166  SER   A OG  
3710 O  OG  B SER   A 166 ? 0.1857 0.2796 0.2963 -0.0095 -0.0096 0.0067  166  SER   A OG  
3721 N  N   A SER   A 167 ? 0.1452 0.3075 0.2240 0.0040  -0.0293 0.0644  167  SER   A N   
3722 N  N   B SER   A 167 ? 0.1473 0.2882 0.2382 -0.0110 0.0037  0.0322  167  SER   A N   
3723 C  CA  A SER   A 167 ? 0.1571 0.3042 0.2178 0.0015  -0.0265 0.0467  167  SER   A CA  
3724 C  CA  B SER   A 167 ? 0.1668 0.2913 0.2424 -0.0127 0.0129  0.0405  167  SER   A CA  
3725 C  C   A SER   A 167 ? 0.1544 0.2976 0.2250 0.0003  -0.0207 0.0364  167  SER   A C   
3726 C  C   B SER   A 167 ? 0.1642 0.2967 0.2454 -0.0049 0.0122  0.0422  167  SER   A C   
3727 O  O   A SER   A 167 ? 0.1525 0.3041 0.2384 -0.0046 -0.0303 0.0206  167  SER   A O   
3728 O  O   B SER   A 167 ? 0.1788 0.3018 0.2682 -0.0065 0.0041  0.0339  167  SER   A O   
3729 C  CB  A SER   A 167 ? 0.1539 0.3055 0.2154 -0.0045 -0.0105 0.0402  167  SER   A CB  
3730 C  CB  B SER   A 167 ? 0.1844 0.2892 0.2566 -0.0183 0.0239  0.0337  167  SER   A CB  
3731 O  OG  A SER   A 167 ? 0.1571 0.3048 0.2107 -0.0102 0.0079  0.0307  167  SER   A OG  
3732 O  OG  B SER   A 167 ? 0.1942 0.2889 0.2670 -0.0195 0.0348  0.0227  167  SER   A OG  
3743 N  N   A PHE   A 168 ? 0.1461 0.2798 0.2180 0.0072  -0.0070 0.0441  168  PHE   A N   
3744 N  N   B PHE   A 168 ? 0.1450 0.2926 0.2225 0.0026  0.0276  0.0514  168  PHE   A N   
3745 C  CA  A PHE   A 168 ? 0.1507 0.2709 0.2241 0.0054  0.0132  0.0466  168  PHE   A CA  
3746 C  CA  B PHE   A 168 ? 0.1333 0.2910 0.2120 0.0108  0.0323  0.0564  168  PHE   A CA  
3747 C  C   A PHE   A 168 ? 0.1594 0.2758 0.2461 0.0029  0.0359  0.0389  168  PHE   A C   
3748 C  C   B PHE   A 168 ? 0.1317 0.2911 0.2222 0.0074  0.0337  0.0498  168  PHE   A C   
3749 O  O   A PHE   A 168 ? 0.1636 0.2779 0.2681 -0.0007 0.0452  0.0438  168  PHE   A O   
3750 O  O   B PHE   A 168 ? 0.1271 0.2919 0.2311 0.0076  0.0417  0.0519  168  PHE   A O   
3751 C  CB  A PHE   A 168 ? 0.1518 0.2605 0.2028 -0.0033 0.0049  0.0411  168  PHE   A CB  
3752 C  CB  B PHE   A 168 ? 0.1373 0.2916 0.2057 0.0139  0.0266  0.0600  168  PHE   A CB  
3753 C  CG  A PHE   A 168 ? 0.1510 0.2553 0.1875 -0.0101 -0.0116 0.0351  168  PHE   A CG  
3754 C  CG  B PHE   A 168 ? 0.1431 0.2907 0.2134 0.0163  0.0190  0.0621  168  PHE   A CG  
3755 C  CD1 A PHE   A 168 ? 0.1484 0.2549 0.1946 -0.0146 -0.0136 0.0318  168  PHE   A CD1 
3756 C  CD1 B PHE   A 168 ? 0.1446 0.2898 0.2107 0.0203  0.0245  0.0678  168  PHE   A CD1 
3757 C  CD2 A PHE   A 168 ? 0.1494 0.2511 0.1813 -0.0108 -0.0134 0.0284  168  PHE   A CD2 
3758 C  CD2 B PHE   A 168 ? 0.1451 0.2878 0.2147 0.0199  0.0097  0.0659  168  PHE   A CD2 
3759 C  CE1 A PHE   A 168 ? 0.1374 0.2509 0.1846 -0.0181 -0.0200 0.0278  168  PHE   A CE1 
3760 C  CE1 B PHE   A 168 ? 0.1450 0.2882 0.2090 0.0186  0.0193  0.0753  168  PHE   A CE1 
3761 C  CE2 A PHE   A 168 ? 0.1475 0.2453 0.1840 -0.0158 -0.0134 0.0317  168  PHE   A CE2 
3762 C  CE2 B PHE   A 168 ? 0.1468 0.2859 0.2120 0.0183  0.0048  0.0731  168  PHE   A CE2 
3763 C  CZ  A PHE   A 168 ? 0.1404 0.2461 0.1833 -0.0205 -0.0194 0.0303  168  PHE   A CZ  
3764 C  CZ  B PHE   A 168 ? 0.1494 0.2866 0.2107 0.0144  0.0105  0.0768  168  PHE   A CZ  
3783 N  N   A LEU   A 169 ? 0.1768 0.2736 0.2678 0.0026  0.0395  0.0276  169  LEU   A N   
3784 N  N   B LEU   A 169 ? 0.1417 0.2944 0.2256 0.0063  0.0193  0.0460  169  LEU   A N   
3785 C  CA  A LEU   A 169 ? 0.2013 0.2799 0.3023 0.0087  0.0374  0.0141  169  LEU   A CA  
3786 C  CA  B LEU   A 169 ? 0.1577 0.3026 0.2520 0.0044  0.0104  0.0313  169  LEU   A CA  
3787 C  C   A LEU   A 169 ? 0.1939 0.2795 0.3208 0.0076  0.0566  0.0251  169  LEU   A C   
3788 C  C   B LEU   A 169 ? 0.1737 0.3085 0.2680 0.0064  0.0107  0.0271  169  LEU   A C   
3789 O  O   A LEU   A 169 ? 0.2007 0.2829 0.3308 0.0067  0.0527  0.0253  169  LEU   A O   
3790 O  O   B LEU   A 169 ? 0.1784 0.3118 0.2732 0.0051  0.0068  0.0246  169  LEU   A O   
3791 C  CB  A LEU   A 169 ? 0.2285 0.2900 0.3113 0.0104  0.0284  0.0023  169  LEU   A CB  
3792 C  CB  B LEU   A 169 ? 0.1566 0.3066 0.2579 -0.0015 0.0029  0.0232  169  LEU   A CB  
3793 C  CG  A LEU   A 169 ? 0.2526 0.2998 0.3184 0.0126  0.0211  -0.0128 169  LEU   A CG  
3794 C  CG  B LEU   A 169 ? 0.1566 0.3089 0.2646 -0.0047 0.0013  0.0201  169  LEU   A CG  
3795 C  CD1 A LEU   A 169 ? 0.2628 0.3015 0.3199 0.0129  0.0147  -0.0147 169  LEU   A CD1 
3796 C  CD1 B LEU   A 169 ? 0.1572 0.3110 0.2757 -0.0060 -0.0024 0.0185  169  LEU   A CD1 
3797 C  CD2 A LEU   A 169 ? 0.2586 0.3063 0.3209 0.0105  0.0246  -0.0147 169  LEU   A CD2 
3798 C  CD2 B LEU   A 169 ? 0.1613 0.3096 0.2647 -0.0066 0.0053  0.0167  169  LEU   A CD2 
3799 O  OXT A LEU   A 169 ? 0.1855 0.2842 0.3259 0.0055  0.0737  0.0303  169  LEU   A OXT 
3800 O  OXT B LEU   A 169 ? 0.1892 0.3114 0.2808 0.0033  0.0087  0.0257  169  LEU   A OXT 
3823 N  N   A SER   B 1   ? 0.3639 0.3580 0.3663 -0.0929 -0.0714 0.0593  1    SER   B N   
3824 N  N   B SER   B 1   ? 0.3127 0.2943 0.2974 -0.0955 -0.0544 0.0369  1    SER   B N   
3825 C  CA  A SER   B 1   ? 0.3527 0.3579 0.3621 -0.0957 -0.0767 0.0589  1    SER   B CA  
3826 C  CA  B SER   B 1   ? 0.3046 0.2965 0.2962 -0.0986 -0.0609 0.0341  1    SER   B CA  
3827 C  C   A SER   B 1   ? 0.3257 0.3547 0.3361 -0.0944 -0.0839 0.0715  1    SER   B C   
3828 C  C   B SER   B 1   ? 0.2866 0.3001 0.2810 -0.0967 -0.0644 0.0511  1    SER   B C   
3829 O  O   A SER   B 1   ? 0.3321 0.3545 0.3065 -0.0898 -0.0780 0.0716  1    SER   B O   
3830 O  O   B SER   B 1   ? 0.2928 0.3007 0.2628 -0.0902 -0.0647 0.0542  1    SER   B O   
3831 C  CB  A SER   B 1   ? 0.3652 0.3588 0.3836 -0.0971 -0.0676 0.0479  1    SER   B CB  
3832 C  CB  B SER   B 1   ? 0.3128 0.2926 0.3095 -0.0996 -0.0530 0.0173  1    SER   B CB  
3833 O  OG  A SER   B 1   ? 0.3778 0.3673 0.4211 -0.0953 -0.0586 0.0428  1    SER   B OG  
3834 O  OG  B SER   B 1   ? 0.3235 0.2965 0.3376 -0.0965 -0.0454 0.0074  1    SER   B OG  
3849 N  N   A MET   B 2   ? 0.2966 0.3497 0.3382 -0.0920 -0.0889 0.0961  2    MET   B N   
3850 N  N   B MET   B 2   ? 0.2686 0.3023 0.2814 -0.0933 -0.0575 0.0770  2    MET   B N   
3851 C  CA  A MET   B 2   ? 0.2745 0.3449 0.3559 -0.0754 -0.0912 0.1081  2    MET   B CA  
3852 C  CA  B MET   B 2   ? 0.2599 0.3060 0.2894 -0.0744 -0.0497 0.0865  2    MET   B CA  
3853 C  C   A MET   B 2   ? 0.2319 0.3167 0.3159 -0.0670 -0.0949 0.1327  2    MET   B C   
3854 C  C   B MET   B 2   ? 0.2356 0.2884 0.2464 -0.0591 -0.0396 0.0923  2    MET   B C   
3855 O  O   A MET   B 2   ? 0.2227 0.3280 0.3132 -0.0566 -0.1048 0.1360  2    MET   B O   
3856 O  O   B MET   B 2   ? 0.2338 0.2964 0.2454 -0.0529 -0.0349 0.0842  2    MET   B O   
3857 C  CB  A MET   B 2   ? 0.3042 0.3724 0.4372 -0.0560 -0.0771 0.0824  2    MET   B CB  
3858 C  CB  B MET   B 2   ? 0.2835 0.3308 0.3546 -0.0617 -0.0505 0.0779  2    MET   B CB  
3859 C  CG  A MET   B 2   ? 0.3292 0.3945 0.5120 -0.0364 -0.0622 0.0682  2    MET   B CG  
3860 C  CG  B MET   B 2   ? 0.3018 0.3503 0.4084 -0.0497 -0.0490 0.0805  2    MET   B CG  
3861 S  SD  A MET   B 2   ? 0.3513 0.4137 0.5780 -0.0218 -0.0500 0.0575  2    MET   B SD  
3862 S  SD  B MET   B 2   ? 0.3187 0.3682 0.4545 -0.0389 -0.0480 0.0835  2    MET   B SD  
3863 C  CE  A MET   B 2   ? 0.3538 0.4190 0.5830 -0.0198 -0.0442 0.0573  2    MET   B CE  
3864 C  CE  B MET   B 2   ? 0.3181 0.3705 0.4591 -0.0387 -0.0481 0.0791  2    MET   B CE  
3883 N  N   A VAL   B 3   ? 0.2044 0.2746 0.2977 -0.0726 -0.0849 0.1391  3    VAL   B N   
3884 N  N   B VAL   B 3   ? 0.2151 0.2623 0.2219 -0.0536 -0.0306 0.0950  3    VAL   B N   
3885 C  CA  A VAL   B 3   ? 0.1964 0.2402 0.2915 -0.0640 -0.0746 0.1247  3    VAL   B CA  
3886 C  CA  B VAL   B 3   ? 0.2047 0.2390 0.2118 -0.0393 -0.0243 0.0800  3    VAL   B CA  
3887 C  C   A VAL   B 3   ? 0.1752 0.2206 0.2511 -0.0552 -0.0722 0.1146  3    VAL   B C   
3888 C  C   B VAL   B 3   ? 0.1850 0.2275 0.1967 -0.0316 -0.0339 0.0808  3    VAL   B C   
3889 O  O   A VAL   B 3   ? 0.1694 0.2111 0.2637 -0.0545 -0.0767 0.1252  3    VAL   B O   
3890 O  O   B VAL   B 3   ? 0.1856 0.2293 0.1807 -0.0101 -0.0345 0.0725  3    VAL   B O   
3891 C  CB  A VAL   B 3   ? 0.2137 0.2372 0.3274 -0.0644 -0.0662 0.1043  3    VAL   B CB  
3892 C  CB  B VAL   B 3   ? 0.2175 0.2275 0.2190 -0.0338 -0.0185 0.0678  3    VAL   B CB  
3893 C  CG1 A VAL   B 3   ? 0.2216 0.2310 0.3440 -0.0638 -0.0648 0.0979  3    VAL   B CG1 
3894 C  CG1 B VAL   B 3   ? 0.2235 0.2238 0.2306 -0.0347 -0.0158 0.0624  3    VAL   B CG1 
3895 C  CG2 A VAL   B 3   ? 0.2176 0.2406 0.3428 -0.0638 -0.0571 0.1040  3    VAL   B CG2 
3896 C  CG2 B VAL   B 3   ? 0.2209 0.2245 0.2146 -0.0329 -0.0173 0.0652  3    VAL   B CG2 
3915 N  N   . ASN   B 4   ? 0.1707 0.2112 0.2087 -0.0483 -0.0552 0.0870  4    ASN   B N   
3916 C  CA  . ASN   B 4   ? 0.1739 0.2135 0.1802 -0.0512 -0.0441 0.0477  4    ASN   B CA  
3917 C  C   . ASN   B 4   ? 0.1816 0.2276 0.1616 -0.0533 -0.0326 0.0315  4    ASN   B C   
3918 O  O   . ASN   B 4   ? 0.1804 0.2356 0.1912 -0.0521 -0.0214 0.0151  4    ASN   B O   
3919 C  CB  . ASN   B 4   ? 0.1707 0.2045 0.1619 -0.0468 -0.0484 0.0418  4    ASN   B CB  
3920 C  CG  . ASN   B 4   ? 0.1744 0.1875 0.1496 -0.0456 -0.0422 0.0333  4    ASN   B CG  
3921 O  OD1 . ASN   B 4   ? 0.1795 0.1692 0.1481 -0.0461 -0.0445 0.0251  4    ASN   B OD1 
3922 N  ND2 . ASN   B 4   ? 0.1924 0.1928 0.1615 -0.0247 -0.0310 0.0275  4    ASN   B ND2 
3930 N  N   . SER   B 5   ? 0.1983 0.2465 0.1602 -0.0527 -0.0202 0.0338  5    SER   B N   
3931 C  CA  . SER   B 5   ? 0.2239 0.2786 0.1901 -0.0410 -0.0032 0.0403  5    SER   B CA  
3932 C  C   . SER   B 5   ? 0.2406 0.2811 0.2283 -0.0585 0.0258  0.0368  5    SER   B C   
3933 O  O   . SER   B 5   ? 0.2577 0.2768 0.3046 -0.0549 0.0528  0.0344  5    SER   B O   
3934 C  CB  . SER   B 5   ? 0.2341 0.2995 0.2097 -0.0289 0.0057  0.0544  5    SER   B CB  
3935 O  OG  . SER   B 5   ? 0.2512 0.3205 0.2644 -0.0179 0.0026  0.0594  5    SER   B OG  
3941 N  N   . PHE   B 6   ? 0.2578 0.2960 0.1947 -0.0615 0.0370  0.0315  6    PHE   B N   
3942 C  CA  . PHE   B 6   ? 0.2695 0.2959 0.1632 -0.0795 0.0442  0.0110  6    PHE   B CA  
3943 C  C   . PHE   B 6   ? 0.3168 0.3171 0.2009 -0.0884 0.0679  -0.0148 6    PHE   B C   
3944 O  O   . PHE   B 6   ? 0.3332 0.3435 0.2458 -0.0802 0.0482  -0.0271 6    PHE   B O   
3945 C  CB  . PHE   B 6   ? 0.2378 0.2745 0.1546 -0.0754 0.0166  0.0092  6    PHE   B CB  
3946 C  CG  . PHE   B 6   ? 0.2046 0.2440 0.1452 -0.0670 0.0045  0.0042  6    PHE   B CG  
3947 C  CD1 . PHE   B 6   ? 0.2041 0.2124 0.1257 -0.0594 -0.0075 0.0066  6    PHE   B CD1 
3948 C  CD2 . PHE   B 6   ? 0.1860 0.2401 0.1514 -0.0584 0.0078  0.0292  6    PHE   B CD2 
3949 C  CE1 . PHE   B 6   ? 0.1983 0.1919 0.1386 -0.0475 -0.0107 0.0022  6    PHE   B CE1 
3950 C  CE2 . PHE   B 6   ? 0.1848 0.2234 0.1780 -0.0443 0.0073  0.0212  6    PHE   B CE2 
3951 C  CZ  . PHE   B 6   ? 0.1839 0.1994 0.1612 -0.0455 0.0005  0.0047  6    PHE   B CZ  
3961 N  N   . SER   B 7   ? 0.3488 0.3003 0.2192 -0.1084 0.0930  -0.0477 7    SER   B N   
3962 C  CA  . SER   B 7   ? 0.3811 0.3073 0.2744 -0.1056 0.1118  -0.0586 7    SER   B CA  
3963 C  C   . SER   B 7   ? 0.3784 0.2944 0.2728 -0.1040 0.1295  -0.0695 7    SER   B C   
3964 O  O   . SER   B 7   ? 0.3865 0.2980 0.3059 -0.1050 0.1265  -0.0671 7    SER   B O   
3965 C  CB  . SER   B 7   ? 0.4044 0.3243 0.3321 -0.1023 0.1227  -0.0578 7    SER   B CB  
3966 O  OG  . SER   B 7   ? 0.4184 0.3352 0.3813 -0.1010 0.1256  -0.0497 7    SER   B OG  
3972 N  N   . GLY   B 8   ? 0.3728 0.2841 0.2834 -0.0904 0.1318  -0.0734 8    GLY   B N   
3973 C  CA  . GLY   B 8   ? 0.3563 0.2667 0.2919 -0.0860 0.1264  -0.0733 8    GLY   B CA  
3974 C  C   . GLY   B 8   ? 0.3335 0.2399 0.2879 -0.0857 0.1264  -0.0623 8    GLY   B C   
3975 O  O   . GLY   B 8   ? 0.3443 0.2474 0.3237 -0.0768 0.1272  -0.0684 8    GLY   B O   
3979 N  N   . TYR   B 9   ? 0.3096 0.2225 0.2499 -0.0725 0.1055  -0.0653 9    TYR   B N   
3980 C  CA  . TYR   B 9   ? 0.2851 0.1964 0.2176 -0.0608 0.0769  -0.0506 9    TYR   B CA  
3981 C  C   . TYR   B 9   ? 0.2816 0.1980 0.1992 -0.0540 0.0442  -0.0358 9    TYR   B C   
3982 O  O   . TYR   B 9   ? 0.2948 0.2193 0.2414 -0.0576 0.0396  -0.0220 9    TYR   B O   
3983 C  CB  . TYR   B 9   ? 0.2751 0.1822 0.2151 -0.0501 0.0716  -0.0449 9    TYR   B CB  
3984 C  CG  . TYR   B 9   ? 0.2663 0.1698 0.2225 -0.0553 0.0662  -0.0507 9    TYR   B CG  
3985 C  CD1 . TYR   B 9   ? 0.2695 0.1697 0.2376 -0.0701 0.0687  -0.0428 9    TYR   B CD1 
3986 C  CD2 . TYR   B 9   ? 0.2497 0.1640 0.2205 -0.0515 0.0672  -0.0558 9    TYR   B CD2 
3987 C  CE1 . TYR   B 9   ? 0.2627 0.1790 0.2491 -0.0728 0.0727  -0.0568 9    TYR   B CE1 
3988 C  CE2 . TYR   B 9   ? 0.2483 0.1678 0.2345 -0.0502 0.0670  -0.0616 9    TYR   B CE2 
3989 C  CZ  . TYR   B 9   ? 0.2533 0.1828 0.2492 -0.0653 0.0695  -0.0680 9    TYR   B CZ  
3990 O  OH  . TYR   B 9   ? 0.2529 0.1982 0.2609 -0.0771 0.0679  -0.0795 9    TYR   B OH  
4000 N  N   . LEU   B 10  ? 0.2620 0.1783 0.1740 -0.0503 0.0198  -0.0284 10   LEU   B N   
4001 C  CA  . LEU   B 10  ? 0.2623 0.1780 0.1779 -0.0590 -0.0100 -0.0307 10   LEU   B CA  
4002 C  C   . LEU   B 10  ? 0.2397 0.1766 0.1806 -0.0563 -0.0209 -0.0298 10   LEU   B C   
4003 O  O   . LEU   B 10  ? 0.2237 0.1789 0.1838 -0.0412 -0.0135 -0.0219 10   LEU   B O   
4004 C  CB  . LEU   B 10  ? 0.2828 0.1779 0.1902 -0.0636 -0.0237 -0.0202 10   LEU   B CB  
4005 C  CG  . LEU   B 10  ? 0.3013 0.1835 0.2354 -0.0592 -0.0524 -0.0081 10   LEU   B CG  
4006 C  CD1 . LEU   B 10  ? 0.3167 0.1941 0.2563 -0.0548 -0.0501 -0.0119 10   LEU   B CD1 
4007 C  CD2 . LEU   B 10  ? 0.3119 0.1902 0.2664 -0.0555 -0.0541 0.0090  10   LEU   B CD2 
4019 N  N   . LYS   B 11  ? 0.2483 0.1971 0.1950 -0.0520 -0.0289 -0.0233 11   LYS   B N   
4020 C  CA  . LYS   B 11  ? 0.2671 0.2242 0.2167 -0.0391 -0.0436 -0.0258 11   LYS   B CA  
4021 C  C   . LYS   B 11  ? 0.2504 0.2073 0.2202 -0.0598 -0.0432 -0.0328 11   LYS   B C   
4022 O  O   . LYS   B 11  ? 0.2639 0.2271 0.2500 -0.0731 -0.0389 -0.0638 11   LYS   B O   
4023 C  CB  . LYS   B 11  ? 0.3018 0.2731 0.2731 -0.0138 -0.0507 -0.0164 11   LYS   B CB  
4024 C  CG  . LYS   B 11  ? 0.3303 0.3057 0.3401 0.0008  -0.0527 -0.0155 11   LYS   B CG  
4025 C  CD  . LYS   B 11  ? 0.3522 0.3273 0.4050 0.0095  -0.0515 -0.0177 11   LYS   B CD  
4026 C  CE  . LYS   B 11  ? 0.3706 0.3418 0.4545 0.0100  -0.0521 -0.0207 11   LYS   B CE  
4027 N  NZ  . LYS   B 11  ? 0.3801 0.3511 0.4822 0.0079  -0.0536 -0.0212 11   LYS   B NZ  
4041 N  N   . LEU   B 12  ? 0.2196 0.1824 0.2224 -0.0517 -0.0340 -0.0376 12   LEU   B N   
4042 C  CA  . LEU   B 12  ? 0.2097 0.1702 0.2394 -0.0492 -0.0288 -0.0369 12   LEU   B CA  
4043 C  C   . LEU   B 12  ? 0.1975 0.1737 0.2452 -0.0491 -0.0408 -0.0335 12   LEU   B C   
4044 O  O   . LEU   B 12  ? 0.1934 0.1749 0.2648 -0.0551 -0.0525 -0.0224 12   LEU   B O   
4045 C  CB  . LEU   B 12  ? 0.2110 0.1507 0.2328 -0.0368 -0.0192 -0.0397 12   LEU   B CB  
4046 C  CG  . LEU   B 12  ? 0.2122 0.1455 0.2395 -0.0412 -0.0136 -0.0266 12   LEU   B CG  
4047 C  CD1 . LEU   B 12  ? 0.2244 0.1479 0.2332 -0.0263 -0.0164 -0.0108 12   LEU   B CD1 
4048 C  CD2 . LEU   B 12  ? 0.2179 0.1508 0.2614 -0.0394 -0.0105 -0.0360 12   LEU   B CD2 
4060 N  N   . THR   B 13  ? 0.1876 0.1790 0.2451 -0.0474 -0.0434 -0.0416 13   THR   B N   
4061 C  CA  . THR   B 13  ? 0.1861 0.1823 0.2419 -0.0574 -0.0485 -0.0287 13   THR   B CA  
4062 C  C   . THR   B 13  ? 0.2280 0.1978 0.2591 -0.0650 -0.0628 -0.0282 13   THR   B C   
4063 O  O   . THR   B 13  ? 0.2441 0.1990 0.2627 -0.0637 -0.0291 -0.0288 13   THR   B O   
4064 C  CB  . THR   B 13  ? 0.1744 0.1843 0.2437 -0.0530 -0.0438 -0.0182 13   THR   B CB  
4065 O  OG1 . THR   B 13  ? 0.1679 0.1768 0.2412 -0.0472 -0.0326 -0.0160 13   THR   B OG1 
4066 C  CG2 . THR   B 13  ? 0.1878 0.1859 0.2512 -0.0489 -0.0316 -0.0132 13   THR   B CG2 
4074 N  N   A ASP   B 14  ? 0.2415 0.2095 0.2796 -0.0678 -0.0904 -0.0154 14   ASP   B N   
4075 N  N   B ASP   B 14  ? 0.2393 0.2080 0.2755 -0.0623 -0.0786 -0.0145 14   ASP   B N   
4076 C  CA  A ASP   B 14  ? 0.2533 0.2218 0.3065 -0.0653 -0.0981 0.0031  14   ASP   B CA  
4077 C  CA  B ASP   B 14  ? 0.2482 0.2179 0.2939 -0.0569 -0.0836 0.0006  14   ASP   B CA  
4078 C  C   A ASP   B 14  ? 0.2388 0.2059 0.2668 -0.0649 -0.0833 0.0075  14   ASP   B C   
4079 C  C   B ASP   B 14  ? 0.2324 0.2010 0.2636 -0.0564 -0.0800 0.0022  14   ASP   B C   
4080 O  O   A ASP   B 14  ? 0.2567 0.2180 0.2665 -0.0658 -0.0807 0.0167  14   ASP   B O   
4081 O  O   B ASP   B 14  ? 0.2431 0.2041 0.2664 -0.0526 -0.0819 0.0025  14   ASP   B O   
4082 C  CB  A ASP   B 14  ? 0.2770 0.2525 0.3776 -0.0588 -0.1121 0.0076  14   ASP   B CB  
4083 C  CB  B ASP   B 14  ? 0.2707 0.2456 0.3452 -0.0490 -0.0864 0.0070  14   ASP   B CB  
4084 C  CG  A ASP   B 14  ? 0.3030 0.2768 0.4470 -0.0543 -0.1102 0.0050  14   ASP   B CG  
4085 C  CG  B ASP   B 14  ? 0.2927 0.2687 0.3914 -0.0438 -0.0838 0.0067  14   ASP   B CG  
4086 O  OD1 A ASP   B 14  ? 0.3179 0.2862 0.4661 -0.0558 -0.1091 -0.0040 14   ASP   B OD1 
4087 O  OD1 B ASP   B 14  ? 0.2994 0.2790 0.4033 -0.0438 -0.0793 0.0046  14   ASP   B OD1 
4088 O  OD2 A ASP   B 14  ? 0.3062 0.2835 0.4766 -0.0552 -0.1088 0.0099  14   ASP   B OD2 
4089 O  OD2 B ASP   B 14  ? 0.3002 0.2750 0.4094 -0.0460 -0.0866 0.0073  14   ASP   B OD2 
4098 N  N   . ASN   B 15  ? 0.2072 0.1804 0.2361 -0.0524 -0.0781 0.0041  15   ASN   B N   
4099 C  CA  . ASN   B 15  ? 0.1692 0.1595 0.2164 -0.0345 -0.0545 -0.0024 15   ASN   B CA  
4100 C  C   . ASN   B 15  ? 0.1536 0.1505 0.2000 -0.0225 -0.0364 -0.0071 15   ASN   B C   
4101 O  O   . ASN   B 15  ? 0.1541 0.1455 0.2144 -0.0211 -0.0459 -0.0173 15   ASN   B O   
4102 C  CB  . ASN   B 15  ? 0.1647 0.1531 0.2328 -0.0190 -0.0502 -0.0000 15   ASN   B CB  
4103 C  CG  . ASN   B 15  ? 0.1536 0.1540 0.2335 -0.0255 -0.0244 0.0047  15   ASN   B CG  
4104 O  OD1 . ASN   B 15  ? 0.1581 0.1786 0.2575 -0.0383 -0.0292 0.0082  15   ASN   B OD1 
4105 N  ND2 . ASN   B 15  ? 0.1566 0.1319 0.2313 -0.0173 0.0026  -0.0110 15   ASN   B ND2 
4113 N  N   . VAL   B 16  ? 0.1572 0.1402 0.1998 -0.0263 -0.0444 -0.0027 16   VAL   B N   
4114 C  CA  . VAL   B 16  ? 0.1579 0.1387 0.1810 -0.0256 -0.0301 -0.0226 16   VAL   B CA  
4115 C  C   . VAL   B 16  ? 0.1522 0.1474 0.1710 -0.0321 -0.0256 -0.0135 16   VAL   B C   
4116 O  O   . VAL   B 16  ? 0.1565 0.1582 0.2027 -0.0291 -0.0239 -0.0283 16   VAL   B O   
4117 C  CB  . VAL   B 16  ? 0.1651 0.1373 0.1915 -0.0126 -0.0185 -0.0204 16   VAL   B CB  
4118 C  CG1 . VAL   B 16  ? 0.1718 0.1376 0.1934 0.0043  -0.0121 -0.0123 16   VAL   B CG1 
4119 C  CG2 . VAL   B 16  ? 0.1641 0.1429 0.2096 -0.0058 -0.0088 -0.0145 16   VAL   B CG2 
4129 N  N   . TYR   B 17  ? 0.1574 0.1549 0.1768 -0.0283 -0.0198 -0.0215 17   TYR   B N   
4130 C  CA  . TYR   B 17  ? 0.1671 0.1697 0.1692 -0.0334 -0.0229 -0.0048 17   TYR   B CA  
4131 C  C   . TYR   B 17  ? 0.1650 0.1453 0.1695 -0.0320 -0.0185 -0.0089 17   TYR   B C   
4132 O  O   . TYR   B 17  ? 0.1612 0.1492 0.1858 -0.0292 -0.0247 -0.0355 17   TYR   B O   
4133 C  CB  . TYR   B 17  ? 0.1913 0.2128 0.1882 -0.0234 -0.0249 0.0198  17   TYR   B CB  
4134 C  CG  . TYR   B 17  ? 0.2186 0.2567 0.2263 -0.0127 -0.0340 0.0323  17   TYR   B CG  
4135 C  CD1 . TYR   B 17  ? 0.2331 0.2726 0.2414 -0.0081 -0.0463 0.0436  17   TYR   B CD1 
4136 C  CD2 . TYR   B 17  ? 0.2387 0.2849 0.2447 -0.0018 -0.0412 0.0324  17   TYR   B CD2 
4137 C  CE1 . TYR   B 17  ? 0.2508 0.2980 0.2512 -0.0015 -0.0553 0.0417  17   TYR   B CE1 
4138 C  CE2 . TYR   B 17  ? 0.2546 0.3066 0.2638 0.0065  -0.0555 0.0379  17   TYR   B CE2 
4139 C  CZ  . TYR   B 17  ? 0.2635 0.3149 0.2636 0.0082  -0.0637 0.0434  17   TYR   B CZ  
4140 O  OH  . TYR   B 17  ? 0.2823 0.3300 0.2832 0.0149  -0.0683 0.0438  17   TYR   B OH  
4150 N  N   . ILE   B 18  ? 0.1705 0.1414 0.1593 -0.0296 -0.0124 -0.0201 18   ILE   B N   
4151 C  CA  . ILE   B 18  ? 0.1728 0.1416 0.1592 -0.0302 -0.0077 -0.0285 18   ILE   B CA  
4152 C  C   . ILE   B 18  ? 0.1807 0.1467 0.1675 -0.0358 -0.0068 -0.0358 18   ILE   B C   
4153 O  O   . ILE   B 18  ? 0.2027 0.1591 0.1728 -0.0300 0.0085  -0.0364 18   ILE   B O   
4154 C  CB  . ILE   B 18  ? 0.1805 0.1424 0.1717 -0.0391 -0.0091 -0.0166 18   ILE   B CB  
4155 C  CG1 . ILE   B 18  ? 0.1813 0.1467 0.1791 -0.0331 0.0024  -0.0021 18   ILE   B CG1 
4156 C  CG2 . ILE   B 18  ? 0.1871 0.1501 0.1825 -0.0414 -0.0099 -0.0181 18   ILE   B CG2 
4157 C  CD1 . ILE   B 18  ? 0.1872 0.1755 0.2060 -0.0249 -0.0176 0.0142  18   ILE   B CD1 
4169 N  N   . LYS   B 19  ? 0.1780 0.1483 0.1832 -0.0191 0.0213  -0.0368 19   LYS   B N   
4170 C  CA  . LYS   B 19  ? 0.1907 0.1527 0.1979 -0.0218 0.0219  -0.0390 19   LYS   B CA  
4171 C  C   . LYS   B 19  ? 0.1755 0.1465 0.2079 -0.0217 0.0272  -0.0521 19   LYS   B C   
4172 O  O   . LYS   B 19  ? 0.1722 0.1496 0.1939 -0.0150 0.0199  -0.0426 19   LYS   B O   
4173 C  CB  . LYS   B 19  ? 0.2161 0.1679 0.2067 -0.0278 0.0377  -0.0252 19   LYS   B CB  
4174 C  CG  . LYS   B 19  ? 0.2388 0.1945 0.2360 -0.0320 0.0526  -0.0335 19   LYS   B CG  
4175 C  CD  . LYS   B 19  ? 0.2624 0.2224 0.2428 -0.0420 0.0605  -0.0288 19   LYS   B CD  
4176 C  CE  . LYS   B 19  ? 0.2891 0.2480 0.2619 -0.0429 0.0591  -0.0337 19   LYS   B CE  
4177 N  NZ  . LYS   B 19  ? 0.3060 0.2669 0.2749 -0.0502 0.0618  -0.0300 19   LYS   B NZ  
4191 N  N   . ASN   B 20  ? 0.1746 0.1565 0.2418 -0.0144 0.0369  -0.0623 20   ASN   B N   
4192 C  CA  . ASN   B 20  ? 0.1800 0.1731 0.2630 -0.0127 0.0412  -0.0724 20   ASN   B CA  
4193 C  C   . ASN   B 20  ? 0.1788 0.1908 0.2589 -0.0165 0.0461  -0.0749 20   ASN   B C   
4194 O  O   . ASN   B 20  ? 0.1975 0.2220 0.2687 -0.0307 0.0463  -0.0734 20   ASN   B O   
4195 C  CB  . ASN   B 20  ? 0.2057 0.1767 0.2922 0.0053  0.0308  -0.0742 20   ASN   B CB  
4196 C  CG  . ASN   B 20  ? 0.2309 0.1837 0.3238 0.0313  0.0200  -0.0804 20   ASN   B CG  
4197 O  OD1 . ASN   B 20  ? 0.2570 0.2115 0.3512 0.0448  0.0168  -0.0837 20   ASN   B OD1 
4198 N  ND2 . ASN   B 20  ? 0.2226 0.1845 0.3170 0.0317  0.0154  -0.0795 20   ASN   B ND2 
4205 N  N   . ALA   B 21  ? 0.1752 0.1773 0.2566 -0.0260 0.0469  -0.0613 21   ALA   B N   
4206 C  CA  . ALA   B 21  ? 0.1847 0.1867 0.2644 -0.0295 0.0329  -0.0496 21   ALA   B CA  
4207 C  C   . ALA   B 21  ? 0.1858 0.1610 0.2457 -0.0192 0.0388  -0.0398 21   ALA   B C   
4208 O  O   . ALA   B 21  ? 0.1878 0.1486 0.2465 -0.0264 0.0345  -0.0320 21   ALA   B O   
4209 C  CB  . ALA   B 21  ? 0.1957 0.2096 0.2739 -0.0432 0.0260  -0.0338 21   ALA   B CB  
4215 N  N   . ASP   B 22  ? 0.1798 0.1541 0.2368 -0.0188 0.0299  -0.0342 22   ASP   B N   
4216 C  CA  . ASP   B 22  ? 0.1755 0.1435 0.2278 -0.0089 0.0222  -0.0251 22   ASP   B CA  
4217 C  C   . ASP   B 22  ? 0.1676 0.1401 0.1855 -0.0125 0.0195  -0.0111 22   ASP   B C   
4218 O  O   . ASP   B 22  ? 0.1671 0.1429 0.1918 -0.0109 0.0106  -0.0050 22   ASP   B O   
4219 C  CB  . ASP   B 22  ? 0.1830 0.1492 0.2783 -0.0069 0.0171  -0.0112 22   ASP   B CB  
4220 C  CG  . ASP   B 22  ? 0.1830 0.1684 0.3103 -0.0011 -0.0031 -0.0101 22   ASP   B CG  
4221 O  OD1 . ASP   B 22  ? 0.1968 0.1671 0.3035 0.0065  -0.0229 -0.0132 22   ASP   B OD1 
4222 O  OD2 . ASP   B 22  ? 0.1921 0.1972 0.3669 0.0064  -0.0195 -0.0187 22   ASP   B OD2 
4227 N  N   . ILE   B 23  ? 0.1724 0.1366 0.1641 -0.0063 0.0026  0.0098  23   ILE   B N   
4228 C  CA  . ILE   B 23  ? 0.1585 0.1340 0.1490 -0.0077 -0.0059 0.0042  23   ILE   B CA  
4229 C  C   . ILE   B 23  ? 0.1483 0.1342 0.1508 -0.0066 -0.0042 0.0035  23   ILE   B C   
4230 O  O   . ILE   B 23  ? 0.1448 0.1351 0.1475 -0.0057 -0.0040 0.0061  23   ILE   B O   
4231 C  CB  . ILE   B 23  ? 0.1571 0.1388 0.1715 -0.0136 -0.0002 0.0097  23   ILE   B CB  
4232 C  CG1 . ILE   B 23  ? 0.1659 0.1488 0.1887 -0.0107 0.0103  0.0155  23   ILE   B CG1 
4233 C  CG2 . ILE   B 23  ? 0.1634 0.1649 0.1743 -0.0128 0.0030  0.0027  23   ILE   B CG2 
4234 C  CD1 . ILE   B 23  ? 0.1647 0.1648 0.1972 -0.0088 0.0145  0.0067  23   ILE   B CD1 
4246 N  N   . VAL   B 24  ? 0.1511 0.1368 0.1610 -0.0082 -0.0063 -0.0017 24   VAL   B N   
4247 C  CA  . VAL   B 24  ? 0.1471 0.1425 0.1784 -0.0009 -0.0160 -0.0070 24   VAL   B CA  
4248 C  C   . VAL   B 24  ? 0.1434 0.1439 0.1827 -0.0086 -0.0118 0.0012  24   VAL   B C   
4249 O  O   . VAL   B 24  ? 0.1461 0.1497 0.1983 -0.0150 -0.0088 0.0114  24   VAL   B O   
4250 C  CB  . VAL   B 24  ? 0.1568 0.1609 0.1871 0.0041  -0.0196 -0.0003 24   VAL   B CB  
4251 C  CG1 . VAL   B 24  ? 0.1566 0.1690 0.2168 -0.0024 -0.0184 -0.0037 24   VAL   B CG1 
4252 C  CG2 . VAL   B 24  ? 0.1697 0.1857 0.1964 0.0104  -0.0118 -0.0019 24   VAL   B CG2 
4262 N  N   . GLU   B 25  ? 0.1661 0.1568 0.1826 -0.0085 -0.0020 -0.0025 25   GLU   B N   
4263 C  CA  . GLU   B 25  ? 0.1731 0.1806 0.1986 0.0007  0.0105  -0.0036 25   GLU   B CA  
4264 C  C   . GLU   B 25  ? 0.1713 0.1710 0.1779 -0.0129 0.0155  0.0046  25   GLU   B C   
4265 O  O   . GLU   B 25  ? 0.1837 0.1904 0.1919 -0.0119 0.0255  0.0145  25   GLU   B O   
4266 C  CB  . GLU   B 25  ? 0.2060 0.2234 0.2650 0.0233  0.0288  -0.0065 25   GLU   B CB  
4267 C  CG  . GLU   B 25  ? 0.2460 0.2846 0.3661 0.0289  0.0295  -0.0111 25   GLU   B CG  
4268 C  CD  . GLU   B 25  ? 0.2816 0.3398 0.4500 0.0229  0.0263  -0.0186 25   GLU   B CD  
4269 O  OE1 . GLU   B 25  ? 0.2967 0.3586 0.4795 0.0238  0.0342  -0.0160 25   GLU   B OE1 
4270 O  OE2 . GLU   B 25  ? 0.2975 0.3549 0.4853 0.0209  0.0181  -0.0297 25   GLU   B OE2 
4277 N  N   . GLU   B 26  ? 0.1686 0.1644 0.1595 -0.0267 0.0069  0.0075  26   GLU   B N   
4278 C  CA  . GLU   B 26  ? 0.1668 0.1722 0.1695 -0.0360 -0.0080 -0.0002 26   GLU   B CA  
4279 C  C   . GLU   B 26  ? 0.1509 0.1684 0.1624 -0.0188 0.0007  0.0142  26   GLU   B C   
4280 O  O   . GLU   B 26  ? 0.1754 0.1937 0.1665 -0.0170 -0.0037 0.0283  26   GLU   B O   
4281 C  CB  . GLU   B 26  ? 0.1948 0.1912 0.1875 -0.0451 -0.0118 0.0083  26   GLU   B CB  
4282 C  CG  . GLU   B 26  ? 0.2383 0.2277 0.2457 -0.0466 0.0029  -0.0145 26   GLU   B CG  
4283 C  CD  . GLU   B 26  ? 0.2634 0.2554 0.2643 -0.0647 0.0185  -0.0445 26   GLU   B CD  
4284 O  OE1 . GLU   B 26  ? 0.2849 0.2444 0.2642 -0.0743 0.0674  -0.0388 26   GLU   B OE1 
4285 O  OE2 . GLU   B 26  ? 0.2622 0.2931 0.3174 -0.0550 0.0128  -0.0293 26   GLU   B OE2 
4292 N  N   . ALA   B 27  ? 0.1391 0.1575 0.1628 -0.0168 0.0074  0.0140  27   ALA   B N   
4293 C  CA  . ALA   B 27  ? 0.1457 0.1525 0.1817 -0.0120 0.0047  0.0260  27   ALA   B CA  
4294 C  C   . ALA   B 27  ? 0.1471 0.1640 0.2054 -0.0115 0.0136  0.0393  27   ALA   B C   
4295 O  O   . ALA   B 27  ? 0.1580 0.1694 0.2133 -0.0029 0.0119  0.0489  27   ALA   B O   
4296 C  CB  . ALA   B 27  ? 0.1618 0.1407 0.1816 -0.0175 -0.0022 0.0244  27   ALA   B CB  
4302 N  N   . LYS   B 28  ? 0.1443 0.1854 0.2394 -0.0190 0.0224  0.0591  28   LYS   B N   
4303 C  CA  . LYS   B 28  ? 0.1615 0.2252 0.2628 -0.0143 0.0450  0.0913  28   LYS   B CA  
4304 C  C   . LYS   B 28  ? 0.1918 0.2474 0.2450 -0.0030 0.0605  0.0782  28   LYS   B C   
4305 O  O   . LYS   B 28  ? 0.2134 0.2462 0.2550 -0.0039 0.0555  0.0736  28   LYS   B O   
4306 C  CB  . LYS   B 28  ? 0.1764 0.2594 0.3148 -0.0059 0.0629  0.1148  28   LYS   B CB  
4307 C  CG  . LYS   B 28  ? 0.1934 0.3052 0.3602 0.0049  0.0605  0.1273  28   LYS   B CG  
4308 C  CD  . LYS   B 28  ? 0.2286 0.3659 0.4187 0.0140  0.0785  0.1263  28   LYS   B CD  
4309 C  CE  . LYS   B 28  ? 0.2595 0.4069 0.4642 0.0278  0.0852  0.1251  28   LYS   B CE  
4310 N  NZ  . LYS   B 28  ? 0.2616 0.4149 0.4866 0.0378  0.0850  0.1284  28   LYS   B NZ  
4324 N  N   A LYS   B 29  ? 0.2082 0.2648 0.2426 0.0127  0.0619  0.0685  29   LYS   B N   
4325 N  N   B LYS   B 29  ? 0.2072 0.2661 0.2473 0.0059  0.0577  0.0690  29   LYS   B N   
4326 C  CA  A LYS   B 29  ? 0.2442 0.2915 0.2685 0.0130  0.0594  0.0604  29   LYS   B CA  
4327 C  CA  B LYS   B 29  ? 0.2347 0.2904 0.2683 0.0056  0.0531  0.0610  29   LYS   B CA  
4328 C  C   A LYS   B 29  ? 0.2389 0.2959 0.2382 0.0154  0.0504  0.0719  29   LYS   B C   
4329 C  C   B LYS   B 29  ? 0.2286 0.2937 0.2392 0.0072  0.0448  0.0688  29   LYS   B C   
4330 O  O   A LYS   B 29  ? 0.2547 0.3094 0.2456 0.0204  0.0480  0.0766  29   LYS   B O   
4331 O  O   B LYS   B 29  ? 0.2359 0.3042 0.2462 0.0071  0.0381  0.0665  29   LYS   B O   
4332 C  CB  A LYS   B 29  ? 0.2874 0.3164 0.3390 0.0070  0.0565  0.0442  29   LYS   B CB  
4333 C  CB  B LYS   B 29  ? 0.2695 0.3124 0.3295 0.0020  0.0499  0.0472  29   LYS   B CB  
4334 C  CG  A LYS   B 29  ? 0.3208 0.3369 0.4105 0.0003  0.0576  0.0371  29   LYS   B CG  
4335 C  CG  B LYS   B 29  ? 0.2975 0.3300 0.3906 -0.0022 0.0501  0.0401  29   LYS   B CG  
4336 C  CD  A LYS   B 29  ? 0.3485 0.3506 0.4678 -0.0062 0.0638  0.0284  29   LYS   B CD  
4337 C  CD  B LYS   B 29  ? 0.3188 0.3420 0.4400 -0.0062 0.0524  0.0317  29   LYS   B CD  
4338 C  CE  A LYS   B 29  ? 0.3687 0.3579 0.5083 -0.0108 0.0689  0.0216  29   LYS   B CE  
4339 C  CE  B LYS   B 29  ? 0.3330 0.3489 0.4748 -0.0090 0.0550  0.0255  29   LYS   B CE  
4340 N  NZ  A LYS   B 29  ? 0.3757 0.3622 0.5343 -0.0140 0.0707  0.0177  29   LYS   B NZ  
4341 N  NZ  B LYS   B 29  ? 0.3403 0.3530 0.4972 -0.0101 0.0556  0.0223  29   LYS   B NZ  
4368 N  N   . VAL   B 30  ? 0.2122 0.2868 0.2239 0.0046  0.0388  0.0762  30   VAL   B N   
4369 C  CA  . VAL   B 30  ? 0.1911 0.2776 0.2559 -0.0075 -0.0006 0.0810  30   VAL   B CA  
4370 C  C   . VAL   B 30  ? 0.1688 0.2680 0.2513 -0.0104 0.0080  0.1044  30   VAL   B C   
4371 O  O   . VAL   B 30  ? 0.1851 0.2863 0.2545 -0.0014 0.0137  0.1176  30   VAL   B O   
4372 C  CB  . VAL   B 30  ? 0.1970 0.2746 0.2985 -0.0247 -0.0312 0.0707  30   VAL   B CB  
4373 C  CG1 . VAL   B 30  ? 0.1982 0.2802 0.2986 -0.0289 -0.0258 0.0725  30   VAL   B CG1 
4374 C  CG2 . VAL   B 30  ? 0.2107 0.2730 0.3166 -0.0343 -0.0413 0.0565  30   VAL   B CG2 
4385 N  N   . LYS   B 31  ? 0.1575 0.2286 0.2916 -0.0301 0.0039  0.1117  31   LYS   B N   
4386 C  CA  . LYS   B 31  ? 0.1477 0.2179 0.3305 -0.0430 -0.0097 0.1131  31   LYS   B CA  
4387 C  C   . LYS   B 31  ? 0.1453 0.1835 0.2853 -0.0371 -0.0271 0.0940  31   LYS   B C   
4388 O  O   . LYS   B 31  ? 0.1545 0.2027 0.3054 -0.0253 -0.0225 0.1127  31   LYS   B O   
4389 C  CB  . LYS   B 31  ? 0.1679 0.2634 0.3926 -0.0405 0.0183  0.1221  31   LYS   B CB  
4390 C  CG  . LYS   B 31  ? 0.1987 0.3073 0.4349 -0.0380 0.0374  0.1205  31   LYS   B CG  
4391 C  CD  . LYS   B 31  ? 0.2315 0.3543 0.4637 -0.0295 0.0372  0.1121  31   LYS   B CD  
4392 C  CE  . LYS   B 31  ? 0.2542 0.3825 0.4934 -0.0273 0.0300  0.1004  31   LYS   B CE  
4393 N  NZ  . LYS   B 31  ? 0.2635 0.3961 0.5033 -0.0197 0.0190  0.0888  31   LYS   B NZ  
4407 N  N   . PRO   B 32  ? 0.1551 0.1500 0.2075 -0.0365 -0.0447 0.0485  32   PRO   B N   
4408 C  CA  . PRO   B 32  ? 0.1663 0.1476 0.1605 -0.0364 -0.0478 0.0314  32   PRO   B CA  
4409 C  C   . PRO   B 32  ? 0.1753 0.1345 0.1665 -0.0380 -0.0564 0.0315  32   PRO   B C   
4410 O  O   . PRO   B 32  ? 0.1912 0.1374 0.2082 -0.0391 -0.0720 0.0349  32   PRO   B O   
4411 C  CB  . PRO   B 32  ? 0.1825 0.1419 0.1635 -0.0375 -0.0352 0.0196  32   PRO   B CB  
4412 C  CG  . PRO   B 32  ? 0.1976 0.1351 0.1649 -0.0329 -0.0489 0.0194  32   PRO   B CG  
4413 C  CD  . PRO   B 32  ? 0.1848 0.1384 0.1876 -0.0257 -0.0584 0.0311  32   PRO   B CD  
4421 N  N   . THR   B 33  ? 0.1747 0.1302 0.1538 -0.0320 -0.0513 0.0244  33   THR   B N   
4422 C  CA  . THR   B 33  ? 0.1838 0.1333 0.1523 -0.0351 -0.0454 0.0277  33   THR   B CA  
4423 C  C   . THR   B 33  ? 0.1860 0.1232 0.1428 -0.0276 -0.0444 0.0201  33   THR   B C   
4424 O  O   . THR   B 33  ? 0.2120 0.1282 0.1547 -0.0360 -0.0565 0.0138  33   THR   B O   
4425 C  CB  . THR   B 33  ? 0.1943 0.1401 0.1624 -0.0189 -0.0593 0.0291  33   THR   B CB  
4426 O  OG1 . THR   B 33  ? 0.1882 0.1525 0.1589 -0.0232 -0.0555 0.0338  33   THR   B OG1 
4427 C  CG2 . THR   B 33  ? 0.2191 0.1438 0.1838 -0.0131 -0.0594 0.0225  33   THR   B CG2 
4435 N  N   . VAL   B 34  ? 0.1710 0.1224 0.1335 -0.0313 -0.0420 0.0117  34   VAL   B N   
4436 C  CA  . VAL   B 34  ? 0.1554 0.1209 0.1282 -0.0246 -0.0341 0.0088  34   VAL   B CA  
4437 C  C   . VAL   B 34  ? 0.1370 0.1188 0.1148 -0.0289 -0.0208 0.0032  34   VAL   B C   
4438 O  O   . VAL   B 34  ? 0.1580 0.1194 0.1262 -0.0234 -0.0295 0.0090  34   VAL   B O   
4439 C  CB  . VAL   B 34  ? 0.1613 0.1292 0.1609 -0.0090 -0.0325 -0.0015 34   VAL   B CB  
4440 C  CG1 . VAL   B 34  ? 0.1595 0.1430 0.1617 -0.0112 -0.0164 -0.0032 34   VAL   B CG1 
4441 C  CG2 . VAL   B 34  ? 0.1652 0.1357 0.1946 -0.0082 -0.0305 0.0022  34   VAL   B CG2 
4451 N  N   . VAL   B 35  ? 0.1336 0.1142 0.1087 -0.0252 -0.0142 0.0062  35   VAL   B N   
4452 C  CA  . VAL   B 35  ? 0.1308 0.1168 0.1125 -0.0198 -0.0100 0.0038  35   VAL   B CA  
4453 C  C   . VAL   B 35  ? 0.1194 0.1109 0.1138 -0.0132 -0.0095 0.0003  35   VAL   B C   
4454 O  O   . VAL   B 35  ? 0.1255 0.1150 0.1183 -0.0196 -0.0014 -0.0051 35   VAL   B O   
4455 C  CB  . VAL   B 35  ? 0.1302 0.1326 0.1142 -0.0148 0.0066  0.0061  35   VAL   B CB  
4456 C  CG1 . VAL   B 35  ? 0.1225 0.1448 0.1280 -0.0238 0.0059  0.0001  35   VAL   B CG1 
4457 C  CG2 . VAL   B 35  ? 0.1309 0.1333 0.1346 -0.0055 0.0044  -0.0025 35   VAL   B CG2 
4467 N  N   . VAL   B 36  ? 0.1235 0.1111 0.1107 -0.0158 -0.0155 0.0075  36   VAL   B N   
4468 C  CA  . VAL   B 36  ? 0.1201 0.1067 0.1035 -0.0094 -0.0027 0.0032  36   VAL   B CA  
4469 C  C   . VAL   B 36  ? 0.1206 0.1059 0.0953 -0.0113 0.0003  0.0010  36   VAL   B C   
4470 O  O   . VAL   B 36  ? 0.1276 0.1160 0.1214 -0.0113 0.0046  -0.0075 36   VAL   B O   
4471 C  CB  . VAL   B 36  ? 0.1201 0.1169 0.1114 -0.0117 -0.0034 0.0030  36   VAL   B CB  
4472 C  CG1 . VAL   B 36  ? 0.1196 0.1240 0.1344 -0.0171 -0.0045 0.0015  36   VAL   B CG1 
4473 C  CG2 . VAL   B 36  ? 0.1290 0.1191 0.1241 -0.0097 -0.0123 0.0083  36   VAL   B CG2 
4483 N  N   . ASN   B 37  ? 0.1212 0.1121 0.1004 -0.0010 -0.0035 0.0051  37   ASN   B N   
4484 C  CA  . ASN   B 37  ? 0.1248 0.1156 0.1139 0.0004  -0.0078 0.0093  37   ASN   B CA  
4485 C  C   . ASN   B 37  ? 0.1216 0.1168 0.1097 0.0051  -0.0040 -0.0002 37   ASN   B C   
4486 O  O   . ASN   B 37  ? 0.1308 0.1242 0.1090 0.0041  0.0019  0.0053  37   ASN   B O   
4487 C  CB  . ASN   B 37  ? 0.1209 0.1208 0.1171 0.0037  -0.0110 0.0038  37   ASN   B CB  
4488 C  CG  . ASN   B 37  ? 0.1232 0.1183 0.1154 -0.0007 -0.0081 -0.0020 37   ASN   B CG  
4489 O  OD1 . ASN   B 37  ? 0.1346 0.1271 0.1246 0.0106  -0.0092 0.0019  37   ASN   B OD1 
4490 N  ND2 . ASN   B 37  ? 0.1288 0.1186 0.1226 -0.0006 -0.0121 0.0037  37   ASN   B ND2 
4497 N  N   . ALA   B 38  ? 0.1296 0.1136 0.1109 0.0107  0.0027  -0.0011 38   ALA   B N   
4498 C  CA  . ALA   B 38  ? 0.1391 0.1189 0.1098 0.0018  0.0057  0.0086  38   ALA   B CA  
4499 C  C   . ALA   B 38  ? 0.1384 0.1162 0.1124 0.0003  0.0068  0.0087  38   ALA   B C   
4500 O  O   . ALA   B 38  ? 0.1453 0.1272 0.1287 0.0059  0.0017  0.0109  38   ALA   B O   
4501 C  CB  . ALA   B 38  ? 0.1544 0.1276 0.1248 -0.0108 0.0091  0.0052  38   ALA   B CB  
4507 N  N   . ALA   B 39  ? 0.1353 0.1199 0.1119 0.0108  -0.0027 0.0033  39   ALA   B N   
4508 C  CA  . ALA   B 39  ? 0.1410 0.1273 0.1081 0.0082  -0.0019 0.0049  39   ALA   B CA  
4509 C  C   . ALA   B 39  ? 0.1417 0.1319 0.1059 0.0060  -0.0013 -0.0009 39   ALA   B C   
4510 O  O   . ALA   B 39  ? 0.1427 0.1401 0.1286 0.0016  0.0050  0.0079  39   ALA   B O   
4511 C  CB  . ALA   B 39  ? 0.1409 0.1336 0.1238 0.0018  0.0027  -0.0007 39   ALA   B CB  
4517 N  N   . ASN   B 40  ? 0.1496 0.1512 0.1095 -0.0051 0.0039  -0.0044 40   ASN   B N   
4518 C  CA  . ASN   B 40  ? 0.1598 0.1586 0.1196 0.0019  -0.0022 -0.0030 40   ASN   B CA  
4519 C  C   . ASN   B 40  ? 0.1608 0.1584 0.0955 0.0106  -0.0023 0.0037  40   ASN   B C   
4520 O  O   . ASN   B 40  ? 0.1604 0.1496 0.1107 0.0100  -0.0011 0.0021  40   ASN   B O   
4521 C  CB  . ASN   B 40  ? 0.1718 0.1584 0.1429 0.0095  -0.0087 0.0153  40   ASN   B CB  
4522 C  CG  . ASN   B 40  ? 0.1756 0.1620 0.1662 0.0074  -0.0190 0.0144  40   ASN   B CG  
4523 O  OD1 . ASN   B 40  ? 0.1755 0.1617 0.2354 0.0081  -0.0302 0.0166  40   ASN   B OD1 
4524 N  ND2 . ASN   B 40  ? 0.1751 0.1607 0.1690 0.0072  -0.0126 0.0122  40   ASN   B ND2 
4531 N  N   . VAL   B 41  ? 0.1689 0.1657 0.0991 0.0145  0.0054  0.0041  41   VAL   B N   
4532 C  CA  . VAL   B 41  ? 0.1763 0.1806 0.1129 0.0131  0.0063  -0.0086 41   VAL   B CA  
4533 C  C   . VAL   B 41  ? 0.1714 0.1776 0.1057 0.0180  0.0001  -0.0145 41   VAL   B C   
4534 O  O   . VAL   B 41  ? 0.1723 0.1730 0.1188 0.0128  -0.0046 -0.0164 41   VAL   B O   
4535 C  CB  . VAL   B 41  ? 0.1951 0.1952 0.1397 -0.0033 0.0231  -0.0219 41   VAL   B CB  
4536 C  CG1 . VAL   B 41  ? 0.1923 0.1976 0.1585 -0.0073 0.0374  -0.0226 41   VAL   B CG1 
4537 C  CG2 . VAL   B 41  ? 0.2082 0.2187 0.1423 -0.0077 0.0308  -0.0205 41   VAL   B CG2 
4547 N  N   . TYR   B 42  ? 0.1783 0.1809 0.1167 0.0212  -0.0131 -0.0002 42   TYR   B N   
4548 C  CA  . TYR   B 42  ? 0.1830 0.1840 0.1292 0.0177  -0.0205 -0.0126 42   TYR   B CA  
4549 C  C   . TYR   B 42  ? 0.1684 0.1646 0.1308 0.0187  -0.0179 -0.0123 42   TYR   B C   
4550 O  O   . TYR   B 42  ? 0.1714 0.1740 0.1483 0.0177  -0.0224 -0.0222 42   TYR   B O   
4551 C  CB  . TYR   B 42  ? 0.2086 0.2090 0.1439 0.0096  -0.0242 -0.0006 42   TYR   B CB  
4552 C  CG  . TYR   B 42  ? 0.2104 0.2223 0.1338 0.0013  -0.0282 0.0146  42   TYR   B CG  
4553 C  CD1 . TYR   B 42  ? 0.2044 0.2220 0.1049 -0.0057 -0.0091 -0.0002 42   TYR   B CD1 
4554 C  CD2 . TYR   B 42  ? 0.2286 0.2354 0.1788 -0.0016 -0.0129 0.0168  42   TYR   B CD2 
4555 C  CE1 . TYR   B 42  ? 0.2202 0.2440 0.1120 -0.0035 -0.0061 -0.0056 42   TYR   B CE1 
4556 C  CE2 . TYR   B 42  ? 0.2331 0.2446 0.1709 -0.0024 0.0048  0.0252  42   TYR   B CE2 
4557 C  CZ  . TYR   B 42  ? 0.2405 0.2573 0.1427 0.0101  0.0066  0.0084  42   TYR   B CZ  
4558 O  OH  . TYR   B 42  ? 0.2682 0.2802 0.1885 0.0278  0.0225  0.0100  42   TYR   B OH  
4568 N  N   . LEU   B 43  ? 0.1560 0.1505 0.1178 0.0088  -0.0131 -0.0126 43   LEU   B N   
4569 C  CA  . LEU   B 43  ? 0.1523 0.1454 0.1125 0.0066  -0.0108 -0.0063 43   LEU   B CA  
4570 C  C   . LEU   B 43  ? 0.1598 0.1499 0.1251 0.0067  -0.0099 -0.0053 43   LEU   B C   
4571 O  O   . LEU   B 43  ? 0.1537 0.1535 0.1416 0.0041  -0.0166 0.0045  43   LEU   B O   
4572 C  CB  . LEU   B 43  ? 0.1507 0.1388 0.1335 0.0007  -0.0208 -0.0167 43   LEU   B CB  
4573 C  CG  . LEU   B 43  ? 0.1554 0.1382 0.1325 0.0041  -0.0201 -0.0145 43   LEU   B CG  
4574 C  CD1 . LEU   B 43  ? 0.1644 0.1437 0.1708 0.0062  -0.0350 -0.0148 43   LEU   B CD1 
4575 C  CD2 . LEU   B 43  ? 0.1507 0.1404 0.1447 -0.0036 -0.0261 -0.0102 43   LEU   B CD2 
4587 N  N   . LYS   B 44  ? 0.1575 0.1493 0.1226 0.0116  -0.0073 -0.0098 44   LYS   B N   
4588 C  CA  . LYS   B 44  ? 0.1711 0.1591 0.1223 0.0127  -0.0116 0.0004  44   LYS   B CA  
4589 C  C   . LYS   B 44  ? 0.1571 0.1517 0.1201 0.0167  -0.0111 0.0010  44   LYS   B C   
4590 O  O   . LYS   B 44  ? 0.1801 0.1504 0.1522 0.0030  -0.0028 0.0033  44   LYS   B O   
4591 C  CB  . LYS   B 44  ? 0.1998 0.1801 0.1366 0.0192  -0.0235 -0.0020 44   LYS   B CB  
4592 C  CG  . LYS   B 44  ? 0.2333 0.2055 0.1779 0.0125  -0.0459 -0.0079 44   LYS   B CG  
4593 C  CD  . LYS   B 44  ? 0.2659 0.2239 0.2372 0.0008  -0.0515 -0.0035 44   LYS   B CD  
4594 C  CE  . LYS   B 44  ? 0.2973 0.2460 0.2809 -0.0064 -0.0569 0.0031  44   LYS   B CE  
4595 N  NZ  . LYS   B 44  ? 0.3096 0.2565 0.3110 -0.0044 -0.0650 0.0106  44   LYS   B NZ  
4609 N  N   . HIS   B 45  ? 0.1546 0.1506 0.1176 0.0092  -0.0053 0.0089  45   HIS   B N   
4610 C  CA  . HIS   B 45  ? 0.1595 0.1458 0.1236 0.0119  -0.0044 -0.0053 45   HIS   B CA  
4611 C  C   . HIS   B 45  ? 0.1816 0.1622 0.1629 0.0187  -0.0166 -0.0097 45   HIS   B C   
4612 O  O   . HIS   B 45  ? 0.1910 0.1873 0.2150 0.0443  0.0138  -0.0024 45   HIS   B O   
4613 C  CB  . HIS   B 45  ? 0.1488 0.1489 0.1263 0.0013  -0.0062 -0.0049 45   HIS   B CB  
4614 C  CG  . HIS   B 45  ? 0.1507 0.1444 0.1236 -0.0044 -0.0084 -0.0033 45   HIS   B CG  
4615 N  ND1 . HIS   B 45  ? 0.1550 0.1373 0.1282 0.0007  -0.0127 -0.0058 45   HIS   B ND1 
4616 C  CD2 . HIS   B 45  ? 0.1594 0.1489 0.1341 -0.0086 -0.0101 0.0020  45   HIS   B CD2 
4617 C  CE1 . HIS   B 45  ? 0.1642 0.1301 0.1114 -0.0033 -0.0235 -0.0092 45   HIS   B CE1 
4618 N  NE2 . HIS   B 45  ? 0.1636 0.1405 0.1220 -0.0010 -0.0180 -0.0072 45   HIS   B NE2 
4626 N  N   A GLY   B 46  ? 0.1884 0.1612 0.1888 0.0175  -0.0350 -0.0001 46   GLY   B N   
4627 N  N   B GLY   B 46  ? 0.1892 0.1673 0.1827 0.0179  -0.0302 0.0017  46   GLY   B N   
4628 C  CA  A GLY   B 46  ? 0.1994 0.1738 0.2250 0.0140  -0.0403 0.0007  46   GLY   B CA  
4629 C  CA  B GLY   B 46  ? 0.1990 0.1792 0.2072 0.0151  -0.0375 0.0074  46   GLY   B CA  
4630 C  C   A GLY   B 46  ? 0.2004 0.1877 0.2675 0.0188  -0.0366 0.0014  46   GLY   B C   
4631 C  C   B GLY   B 46  ? 0.2027 0.1920 0.2373 0.0176  -0.0377 0.0141  46   GLY   B C   
4632 O  O   A GLY   B 46  ? 0.2074 0.2005 0.3409 0.0249  -0.0195 -0.0137 46   GLY   B O   
4633 O  O   B GLY   B 46  ? 0.2109 0.2041 0.2604 0.0225  -0.0358 0.0253  46   GLY   B O   
4640 N  N   . GLY   B 47  ? 0.2022 0.1956 0.2445 0.0084  -0.0220 0.0004  47   GLY   B N   
4641 C  CA  . GLY   B 47  ? 0.1933 0.1668 0.1957 0.0040  -0.0138 0.0026  47   GLY   B CA  
4642 C  C   . GLY   B 47  ? 0.1707 0.1443 0.1645 0.0050  0.0012  0.0049  47   GLY   B C   
4643 O  O   . GLY   B 47  ? 0.1855 0.1331 0.1708 0.0051  -0.0031 0.0087  47   GLY   B O   
4648 N  N   . GLY   B 48  ? 0.1508 0.1374 0.1646 0.0047  -0.0096 0.0163  48   GLY   B N   
4649 C  CA  . GLY   B 48  ? 0.1490 0.1332 0.1617 0.0029  -0.0030 0.0104  48   GLY   B CA  
4650 C  C   . GLY   B 48  ? 0.1432 0.1302 0.1575 0.0004  0.0083  0.0022  48   GLY   B C   
4651 O  O   . GLY   B 48  ? 0.1396 0.1314 0.1733 0.0022  -0.0047 0.0055  48   GLY   B O   
4655 N  N   . VAL   B 49  ? 0.1393 0.1366 0.1432 0.0083  0.0048  0.0089  49   VAL   B N   
4656 C  CA  . VAL   B 49  ? 0.1452 0.1462 0.1355 0.0060  -0.0093 -0.0017 49   VAL   B CA  
4657 C  C   . VAL   B 49  ? 0.1353 0.1377 0.1197 0.0115  -0.0008 0.0059  49   VAL   B C   
4658 O  O   . VAL   B 49  ? 0.1464 0.1410 0.1277 0.0062  0.0000  0.0068  49   VAL   B O   
4659 C  CB  . VAL   B 49  ? 0.1462 0.1623 0.1638 0.0032  -0.0174 0.0002  49   VAL   B CB  
4660 C  CG1 . VAL   B 49  ? 0.1429 0.1671 0.1591 0.0070  -0.0224 0.0047  49   VAL   B CG1 
4661 C  CG2 . VAL   B 49  ? 0.1629 0.1724 0.1815 -0.0027 -0.0333 -0.0057 49   VAL   B CG2 
4671 N  N   . ALA   B 50  ? 0.1282 0.1282 0.1291 0.0033  -0.0027 0.0071  50   ALA   B N   
4672 C  CA  . ALA   B 50  ? 0.1265 0.1260 0.1288 0.0083  -0.0050 0.0056  50   ALA   B CA  
4673 C  C   . ALA   B 50  ? 0.1380 0.1264 0.1278 0.0057  -0.0013 0.0032  50   ALA   B C   
4674 O  O   . ALA   B 50  ? 0.1347 0.1317 0.1284 0.0063  -0.0005 -0.0011 50   ALA   B O   
4675 C  CB  . ALA   B 50  ? 0.1343 0.1279 0.1334 0.0030  0.0059  0.0086  50   ALA   B CB  
4681 N  N   . GLY   B 51  ? 0.1384 0.1352 0.1328 0.0105  -0.0114 0.0064  51   GLY   B N   
4682 C  CA  . GLY   B 51  ? 0.1375 0.1420 0.1542 0.0196  -0.0131 0.0058  51   GLY   B CA  
4683 C  C   . GLY   B 51  ? 0.1345 0.1369 0.1516 0.0225  -0.0050 0.0084  51   GLY   B C   
4684 O  O   . GLY   B 51  ? 0.1380 0.1485 0.1748 0.0087  -0.0086 0.0044  51   GLY   B O   
4688 N  N   . ALA   B 52  ? 0.1380 0.1334 0.1497 0.0182  -0.0011 0.0083  52   ALA   B N   
4689 C  CA  . ALA   B 52  ? 0.1379 0.1379 0.1548 0.0173  0.0038  0.0005  52   ALA   B CA  
4690 C  C   . ALA   B 52  ? 0.1283 0.1359 0.1384 0.0111  0.0044  0.0013  52   ALA   B C   
4691 O  O   . ALA   B 52  ? 0.1376 0.1410 0.1516 0.0119  0.0077  -0.0018 52   ALA   B O   
4692 C  CB  . ALA   B 52  ? 0.1596 0.1458 0.1593 0.0085  0.0047  -0.0016 52   ALA   B CB  
4698 N  N   . LEU   B 53  ? 0.1231 0.1340 0.1354 0.0148  0.0024  0.0025  53   LEU   B N   
4699 C  CA  . LEU   B 53  ? 0.1280 0.1444 0.1329 0.0120  -0.0011 0.0038  53   LEU   B CA  
4700 C  C   . LEU   B 53  ? 0.1311 0.1356 0.1305 0.0092  0.0139  0.0070  53   LEU   B C   
4701 O  O   . LEU   B 53  ? 0.1383 0.1457 0.1401 0.0046  0.0082  0.0144  53   LEU   B O   
4702 C  CB  . LEU   B 53  ? 0.1296 0.1506 0.1423 0.0093  0.0040  0.0177  53   LEU   B CB  
4703 C  CG  . LEU   B 53  ? 0.1253 0.1608 0.1445 0.0051  -0.0024 0.0215  53   LEU   B CG  
4704 C  CD1 . LEU   B 53  ? 0.1378 0.1849 0.1630 0.0119  -0.0077 0.0059  53   LEU   B CD1 
4705 C  CD2 . LEU   B 53  ? 0.1427 0.1888 0.1707 -0.0060 -0.0030 -0.0133 53   LEU   B CD2 
4717 N  N   . ASN   B 54  ? 0.1297 0.1279 0.1309 0.0034  0.0046  0.0062  54   ASN   B N   
4718 C  CA  . ASN   B 54  ? 0.1362 0.1420 0.1404 0.0019  -0.0020 -0.0048 54   ASN   B CA  
4719 C  C   . ASN   B 54  ? 0.1284 0.1435 0.1533 0.0004  0.0012  -0.0002 54   ASN   B C   
4720 O  O   . ASN   B 54  ? 0.1275 0.1475 0.1723 0.0008  0.0047  -0.0012 54   ASN   B O   
4721 C  CB  . ASN   B 54  ? 0.1410 0.1483 0.1505 0.0039  -0.0007 0.0014  54   ASN   B CB  
4722 C  CG  . ASN   B 54  ? 0.1361 0.1555 0.1487 0.0043  -0.0058 0.0006  54   ASN   B CG  
4723 O  OD1 . ASN   B 54  ? 0.1328 0.1520 0.1585 0.0018  -0.0081 -0.0147 54   ASN   B OD1 
4724 N  ND2 . ASN   B 54  ? 0.1522 0.1778 0.1777 -0.0009 -0.0261 0.0114  54   ASN   B ND2 
4731 N  N   . LYS   B 55  ? 0.1333 0.1542 0.1641 0.0118  0.0062  0.0034  55   LYS   B N   
4732 C  CA  . LYS   B 55  ? 0.1340 0.1636 0.1819 0.0188  -0.0004 0.0025  55   LYS   B CA  
4733 C  C   . LYS   B 55  ? 0.1295 0.1577 0.1854 0.0144  0.0085  -0.0039 55   LYS   B C   
4734 O  O   . LYS   B 55  ? 0.1266 0.1751 0.1984 0.0165  0.0121  -0.0021 55   LYS   B O   
4735 C  CB  . LYS   B 55  ? 0.1475 0.1709 0.2070 0.0254  0.0127  0.0091  55   LYS   B CB  
4736 C  CG  . LYS   B 55  ? 0.1886 0.1991 0.3012 0.0305  0.0274  0.0230  55   LYS   B CG  
4737 C  CD  . LYS   B 55  ? 0.2292 0.2199 0.3833 0.0393  0.0416  0.0293  55   LYS   B CD  
4738 C  CE  . LYS   B 55  ? 0.2550 0.2343 0.4513 0.0407  0.0528  0.0336  55   LYS   B CE  
4739 N  NZ  . LYS   B 55  ? 0.2615 0.2460 0.4894 0.0393  0.0432  0.0381  55   LYS   B NZ  
4753 N  N   . ALA   B 56  ? 0.1293 0.1580 0.1638 0.0033  0.0046  -0.0084 56   ALA   B N   
4754 C  CA  . ALA   B 56  ? 0.1468 0.1740 0.1584 0.0019  0.0101  -0.0033 56   ALA   B CA  
4755 C  C   . ALA   B 56  ? 0.1467 0.1690 0.1551 0.0027  0.0195  0.0024  56   ALA   B C   
4756 O  O   . ALA   B 56  ? 0.1593 0.1790 0.1722 0.0064  0.0320  0.0082  56   ALA   B O   
4757 C  CB  . ALA   B 56  ? 0.1617 0.1941 0.1550 -0.0134 0.0106  -0.0078 56   ALA   B CB  
4763 N  N   . THR   B 57  ? 0.1389 0.1632 0.1724 0.0088  0.0178  0.0072  57   THR   B N   
4764 C  CA  . THR   B 57  ? 0.1459 0.1588 0.1702 -0.0016 0.0215  0.0074  57   THR   B CA  
4765 C  C   . THR   B 57  ? 0.1536 0.1660 0.1894 -0.0011 0.0253  0.0027  57   THR   B C   
4766 O  O   . THR   B 57  ? 0.1597 0.1660 0.1973 -0.0141 0.0235  0.0032  57   THR   B O   
4767 C  CB  . THR   B 57  ? 0.1538 0.1512 0.1526 0.0005  0.0188  0.0148  57   THR   B CB  
4768 O  OG1 . THR   B 57  ? 0.1555 0.1447 0.1606 0.0021  0.0178  0.0060  57   THR   B OG1 
4769 C  CG2 . THR   B 57  ? 0.1440 0.1580 0.1504 0.0026  0.0205  0.0134  57   THR   B CG2 
4777 N  N   . ASN   B 58  ? 0.1353 0.1809 0.2032 -0.0124 0.0094  -0.0143 58   ASN   B N   
4778 C  CA  . ASN   B 58  ? 0.1494 0.2258 0.2452 -0.0201 0.0320  -0.0106 58   ASN   B CA  
4779 C  C   . ASN   B 58  ? 0.1344 0.2077 0.2112 -0.0109 0.0029  -0.0088 58   ASN   B C   
4780 O  O   . ASN   B 58  ? 0.1414 0.2163 0.2136 -0.0171 0.0070  -0.0121 58   ASN   B O   
4781 C  CB  . ASN   B 58  ? 0.2309 0.2965 0.3687 -0.0360 0.0700  -0.0002 58   ASN   B CB  
4782 C  CG  . ASN   B 58  ? 0.3244 0.3591 0.5198 -0.0414 0.0864  0.0245  58   ASN   B CG  
4783 O  OD1 . ASN   B 58  ? 0.3466 0.3786 0.5779 -0.0421 0.0906  0.0323  58   ASN   B OD1 
4784 N  ND2 . ASN   B 58  ? 0.3985 0.3985 0.5688 -0.0453 0.0929  0.0310  58   ASN   B ND2 
4791 N  N   . ASN   B 59  ? 0.1333 0.1900 0.1893 -0.0042 0.0047  0.0019  59   ASN   B N   
4792 C  CA  . ASN   B 59  ? 0.1314 0.1881 0.1877 -0.0049 -0.0082 0.0121  59   ASN   B CA  
4793 C  C   . ASN   B 59  ? 0.1282 0.1781 0.1738 -0.0082 -0.0049 -0.0013 59   ASN   B C   
4794 O  O   . ASN   B 59  ? 0.1349 0.1835 0.1732 -0.0111 -0.0092 -0.0059 59   ASN   B O   
4795 C  CB  . ASN   B 59  ? 0.1465 0.2073 0.2061 -0.0005 -0.0220 0.0154  59   ASN   B CB  
4796 C  CG  . ASN   B 59  ? 0.1577 0.2209 0.2258 0.0044  -0.0350 0.0096  59   ASN   B CG  
4797 O  OD1 . ASN   B 59  ? 0.1662 0.2266 0.2213 0.0039  -0.0285 0.0159  59   ASN   B OD1 
4798 N  ND2 . ASN   B 59  ? 0.1692 0.2336 0.2412 -0.0032 -0.0342 0.0055  59   ASN   B ND2 
4805 N  N   . ALA   B 60  ? 0.1375 0.1672 0.1761 -0.0086 0.0006  -0.0038 60   ALA   B N   
4806 C  CA  . ALA   B 60  ? 0.1472 0.1540 0.1841 -0.0194 0.0024  -0.0023 60   ALA   B CA  
4807 C  C   . ALA   B 60  ? 0.1429 0.1440 0.1603 -0.0128 -0.0048 0.0003  60   ALA   B C   
4808 O  O   . ALA   B 60  ? 0.1521 0.1484 0.1702 -0.0151 -0.0024 -0.0094 60   ALA   B O   
4809 C  CB  . ALA   B 60  ? 0.1561 0.1490 0.2053 -0.0190 0.0163  -0.0007 60   ALA   B CB  
4815 N  N   . MET   B 61  ? 0.1355 0.1419 0.1573 -0.0064 0.0005  0.0046  61   MET   B N   
4816 C  CA  . MET   B 61  ? 0.1297 0.1373 0.1505 -0.0065 -0.0035 -0.0019 61   MET   B CA  
4817 C  C   . MET   B 61  ? 0.1388 0.1378 0.1539 -0.0063 -0.0074 0.0021  61   MET   B C   
4818 O  O   . MET   B 61  ? 0.1444 0.1374 0.1431 -0.0020 -0.0077 -0.0099 61   MET   B O   
4819 C  CB  . MET   B 61  ? 0.1274 0.1414 0.1422 0.0022  -0.0040 -0.0043 61   MET   B CB  
4820 C  CG  . MET   B 61  ? 0.1300 0.1432 0.1318 -0.0020 -0.0089 0.0040  61   MET   B CG  
4821 S  SD  . MET   B 61  ? 0.1299 0.1431 0.1557 -0.0027 -0.0022 -0.0083 61   MET   B SD  
4822 C  CE  . MET   B 61  ? 0.1355 0.1641 0.1777 0.0057  0.0046  -0.0193 61   MET   B CE  
4832 N  N   . GLN   B 62  ? 0.1371 0.1423 0.1444 0.0008  -0.0132 -0.0002 62   GLN   B N   
4833 C  CA  . GLN   B 62  ? 0.1424 0.1466 0.1562 0.0008  -0.0158 -0.0067 62   GLN   B CA  
4834 C  C   . GLN   B 62  ? 0.1398 0.1560 0.1509 -0.0030 -0.0233 -0.0124 62   GLN   B C   
4835 O  O   . GLN   B 62  ? 0.1502 0.1548 0.1573 -0.0011 -0.0242 -0.0197 62   GLN   B O   
4836 C  CB  . GLN   B 62  ? 0.1431 0.1522 0.1515 -0.0024 -0.0154 -0.0010 62   GLN   B CB  
4837 C  CG  . GLN   B 62  ? 0.1495 0.1649 0.1518 0.0022  -0.0179 -0.0055 62   GLN   B CG  
4838 C  CD  . GLN   B 62  ? 0.1496 0.1538 0.1348 0.0079  -0.0251 0.0069  62   GLN   B CD  
4839 O  OE1 . GLN   B 62  ? 0.1514 0.1513 0.1554 0.0048  -0.0175 -0.0073 62   GLN   B OE1 
4840 N  NE2 . GLN   B 62  ? 0.1537 0.1630 0.1431 0.0027  -0.0189 -0.0049 62   GLN   B NE2 
4849 N  N   . VAL   B 63  ? 0.1361 0.1604 0.1670 -0.0064 -0.0212 -0.0179 63   VAL   B N   
4850 C  CA  . VAL   B 63  ? 0.1469 0.1617 0.1900 -0.0094 -0.0297 -0.0172 63   VAL   B CA  
4851 C  C   . VAL   B 63  ? 0.1458 0.1472 0.1786 -0.0120 -0.0280 -0.0165 63   VAL   B C   
4852 O  O   . VAL   B 63  ? 0.1555 0.1513 0.1966 -0.0042 -0.0394 -0.0154 63   VAL   B O   
4853 C  CB  . VAL   B 63  ? 0.1497 0.1757 0.2295 -0.0174 -0.0317 -0.0150 63   VAL   B CB  
4854 C  CG1 . VAL   B 63  ? 0.1622 0.1813 0.2457 -0.0269 -0.0215 -0.0167 63   VAL   B CG1 
4855 C  CG2 . VAL   B 63  ? 0.1458 0.1914 0.2417 -0.0089 -0.0342 -0.0137 63   VAL   B CG2 
4865 N  N   . GLU   B 64  ? 0.1480 0.1401 0.1722 -0.0093 -0.0202 -0.0086 64   GLU   B N   
4866 C  CA  . GLU   B 64  ? 0.1488 0.1337 0.1551 -0.0104 -0.0259 -0.0083 64   GLU   B CA  
4867 C  C   . GLU   B 64  ? 0.1429 0.1346 0.1455 -0.0021 -0.0242 -0.0118 64   GLU   B C   
4868 O  O   . GLU   B 64  ? 0.1547 0.1496 0.1503 -0.0064 -0.0230 -0.0162 64   GLU   B O   
4869 C  CB  . GLU   B 64  ? 0.1466 0.1438 0.1550 -0.0092 -0.0167 -0.0077 64   GLU   B CB  
4870 C  CG  . GLU   B 64  ? 0.1526 0.1502 0.1537 -0.0257 -0.0196 -0.0143 64   GLU   B CG  
4871 C  CD  . GLU   B 64  ? 0.1568 0.1611 0.1624 -0.0267 -0.0218 -0.0138 64   GLU   B CD  
4872 O  OE1 . GLU   B 64  ? 0.1597 0.1802 0.1742 -0.0310 -0.0200 -0.0296 64   GLU   B OE1 
4873 O  OE2 . GLU   B 64  ? 0.1747 0.1692 0.1661 -0.0287 -0.0422 -0.0091 64   GLU   B OE2 
4880 N  N   . SER   B 65  ? 0.1459 0.1347 0.1448 -0.0051 -0.0141 -0.0168 65   SER   B N   
4881 C  CA  . SER   B 65  ? 0.1464 0.1330 0.1451 -0.0058 -0.0117 -0.0140 65   SER   B CA  
4882 C  C   . SER   B 65  ? 0.1477 0.1385 0.1409 -0.0015 -0.0204 -0.0173 65   SER   B C   
4883 O  O   . SER   B 65  ? 0.1540 0.1483 0.1476 0.0016  -0.0262 -0.0281 65   SER   B O   
4884 C  CB  . SER   B 65  ? 0.1480 0.1416 0.1424 -0.0072 -0.0143 -0.0078 65   SER   B CB  
4885 O  OG  . SER   B 65  ? 0.1508 0.1384 0.1459 -0.0096 -0.0132 -0.0180 65   SER   B OG  
4891 N  N   . ASP   B 66  ? 0.1590 0.1456 0.1478 0.0015  -0.0250 -0.0190 66   ASP   B N   
4892 C  CA  . ASP   B 66  ? 0.1651 0.1480 0.1395 0.0018  -0.0260 -0.0163 66   ASP   B CA  
4893 C  C   . ASP   B 66  ? 0.1649 0.1548 0.1449 0.0005  -0.0257 -0.0178 66   ASP   B C   
4894 O  O   . ASP   B 66  ? 0.1703 0.1632 0.1496 0.0082  -0.0293 -0.0230 66   ASP   B O   
4895 C  CB  . ASP   B 66  ? 0.1793 0.1648 0.1600 0.0119  -0.0382 -0.0158 66   ASP   B CB  
4896 C  CG  . ASP   B 66  ? 0.2091 0.1805 0.1825 0.0218  -0.0523 -0.0064 66   ASP   B CG  
4897 O  OD1 . ASP   B 66  ? 0.2303 0.1731 0.1894 0.0140  -0.0479 -0.0036 66   ASP   B OD1 
4898 O  OD2 . ASP   B 66  ? 0.2252 0.2067 0.2436 0.0403  -0.0572 -0.0116 66   ASP   B OD2 
4903 N  N   . ASP   B 67  ? 0.1614 0.1480 0.1443 -0.0039 -0.0217 -0.0202 67   ASP   B N   
4904 C  CA  . ASP   B 67  ? 0.1757 0.1454 0.1565 -0.0054 -0.0263 -0.0166 67   ASP   B CA  
4905 C  C   . ASP   B 67  ? 0.1721 0.1438 0.1625 0.0037  -0.0267 -0.0198 67   ASP   B C   
4906 O  O   . ASP   B 67  ? 0.1742 0.1510 0.1719 0.0035  -0.0223 -0.0217 67   ASP   B O   
4907 C  CB  . ASP   B 67  ? 0.1964 0.1553 0.1738 -0.0082 -0.0394 -0.0100 67   ASP   B CB  
4908 C  CG  . ASP   B 67  ? 0.2287 0.1664 0.1802 -0.0101 -0.0650 -0.0141 67   ASP   B CG  
4909 O  OD1 . ASP   B 67  ? 0.2489 0.1748 0.1956 -0.0148 -0.0671 -0.0094 67   ASP   B OD1 
4910 O  OD2 . ASP   B 67  ? 0.2437 0.1696 0.1980 0.0029  -0.0708 -0.0097 67   ASP   B OD2 
4915 N  N   . TYR   B 68  ? 0.1661 0.1459 0.1535 -0.0001 -0.0355 -0.0234 68   TYR   B N   
4916 C  CA  . TYR   B 68  ? 0.1594 0.1641 0.1678 0.0070  -0.0390 -0.0308 68   TYR   B CA  
4917 C  C   . TYR   B 68  ? 0.1533 0.1608 0.1590 0.0045  -0.0342 -0.0397 68   TYR   B C   
4918 O  O   . TYR   B 68  ? 0.1587 0.1747 0.1718 0.0079  -0.0317 -0.0533 68   TYR   B O   
4919 C  CB  . TYR   B 68  ? 0.1651 0.1842 0.1727 0.0109  -0.0415 -0.0448 68   TYR   B CB  
4920 C  CG  . TYR   B 68  ? 0.1744 0.1959 0.1839 0.0171  -0.0303 -0.0642 68   TYR   B CG  
4921 C  CD1 . TYR   B 68  ? 0.1765 0.1976 0.2150 -0.0050 -0.0321 -0.0747 68   TYR   B CD1 
4922 C  CD2 . TYR   B 68  ? 0.1779 0.2120 0.1982 0.0235  -0.0418 -0.0520 68   TYR   B CD2 
4923 C  CE1 . TYR   B 68  ? 0.1819 0.2132 0.2403 0.0019  -0.0310 -0.0648 68   TYR   B CE1 
4924 C  CE2 . TYR   B 68  ? 0.1806 0.2161 0.2140 0.0219  -0.0325 -0.0631 68   TYR   B CE2 
4925 C  CZ  . TYR   B 68  ? 0.1770 0.2146 0.2296 0.0097  -0.0323 -0.0671 68   TYR   B CZ  
4926 O  OH  . TYR   B 68  ? 0.1738 0.2300 0.2482 0.0058  -0.0318 -0.0459 68   TYR   B OH  
4936 N  N   . ILE   B 69  ? 0.1564 0.1506 0.1664 0.0073  -0.0291 -0.0346 69   ILE   B N   
4937 C  CA  . ILE   B 69  ? 0.1667 0.1568 0.1714 0.0004  -0.0198 -0.0399 69   ILE   B CA  
4938 C  C   . ILE   B 69  ? 0.1670 0.1530 0.1564 0.0099  -0.0333 -0.0307 69   ILE   B C   
4939 O  O   . ILE   B 69  ? 0.1718 0.1613 0.1602 0.0083  -0.0215 -0.0366 69   ILE   B O   
4940 C  CB  . ILE   B 69  ? 0.1761 0.1606 0.1868 0.0010  -0.0039 -0.0359 69   ILE   B CB  
4941 C  CG1 . ILE   B 69  ? 0.1744 0.1651 0.1956 -0.0019 0.0014  -0.0375 69   ILE   B CG1 
4942 C  CG2 . ILE   B 69  ? 0.1922 0.1695 0.2026 -0.0005 -0.0065 -0.0272 69   ILE   B CG2 
4943 C  CD1 . ILE   B 69  ? 0.1629 0.1703 0.2091 -0.0109 0.0009  -0.0377 69   ILE   B CD1 
4955 N  N   . ALA   B 70  ? 0.1642 0.1542 0.1623 0.0090  -0.0389 -0.0313 70   ALA   B N   
4956 C  CA  . ALA   B 70  ? 0.1679 0.1542 0.1552 0.0062  -0.0413 -0.0292 70   ALA   B CA  
4957 C  C   . ALA   B 70  ? 0.1737 0.1534 0.1555 0.0053  -0.0469 -0.0334 70   ALA   B C   
4958 O  O   . ALA   B 70  ? 0.1802 0.1554 0.1686 0.0088  -0.0392 -0.0406 70   ALA   B O   
4959 C  CB  . ALA   B 70  ? 0.1691 0.1712 0.1631 0.0017  -0.0441 -0.0264 70   ALA   B CB  
4965 N  N   . THR   B 71  ? 0.1851 0.1539 0.1657 0.0073  -0.0489 -0.0382 71   THR   B N   
4966 C  CA  . THR   B 71  ? 0.1953 0.1585 0.1896 0.0120  -0.0610 -0.0398 71   THR   B CA  
4967 C  C   . THR   B 71  ? 0.1870 0.1604 0.2122 0.0285  -0.0616 -0.0581 71   THR   B C   
4968 O  O   . THR   B 71  ? 0.2016 0.1688 0.2507 0.0278  -0.0567 -0.0680 71   THR   B O   
4969 C  CB  . THR   B 71  ? 0.2163 0.1811 0.2138 0.0026  -0.0725 -0.0185 71   THR   B CB  
4970 O  OG1 . THR   B 71  ? 0.2329 0.2094 0.2508 -0.0154 -0.0687 0.0046  71   THR   B OG1 
4971 C  CG2 . THR   B 71  ? 0.2333 0.1821 0.2378 0.0067  -0.0610 -0.0082 71   THR   B CG2 
4979 N  N   . ASN   B 72  ? 0.1742 0.1682 0.2060 0.0209  -0.0571 -0.0686 72   ASN   B N   
4980 C  CA  . ASN   B 72  ? 0.1775 0.1826 0.2082 0.0238  -0.0425 -0.0761 72   ASN   B CA  
4981 C  C   . ASN   B 72  ? 0.1756 0.1948 0.2171 0.0098  -0.0234 -0.0781 72   ASN   B C   
4982 O  O   . ASN   B 72  ? 0.1744 0.2149 0.2441 0.0113  -0.0115 -0.0742 72   ASN   B O   
4983 C  CB  . ASN   B 72  ? 0.1878 0.1993 0.2134 0.0160  -0.0560 -0.0675 72   ASN   B CB  
4984 C  CG  . ASN   B 72  ? 0.2018 0.2166 0.2252 0.0339  -0.0609 -0.0462 72   ASN   B CG  
4985 O  OD1 . ASN   B 72  ? 0.2235 0.2346 0.2316 0.0202  -0.0435 -0.0493 72   ASN   B OD1 
4986 N  ND2 . ASN   B 72  ? 0.2121 0.2255 0.2678 0.0511  -0.0449 -0.0119 72   ASN   B ND2 
4993 N  N   . GLY   B 73  ? 0.1777 0.1936 0.1943 0.0025  -0.0248 -0.0733 73   GLY   B N   
4994 C  CA  . GLY   B 73  ? 0.1738 0.2024 0.1704 -0.0006 -0.0207 -0.0552 73   GLY   B CA  
4995 C  C   . GLY   B 73  ? 0.1674 0.2016 0.1270 0.0072  -0.0110 -0.0513 73   GLY   B C   
4996 O  O   . GLY   B 73  ? 0.1669 0.1899 0.1476 0.0136  -0.0153 -0.0374 73   GLY   B O   
5000 N  N   . PRO   B 74  ? 0.1730 0.2082 0.1282 0.0119  -0.0215 -0.0399 74   PRO   B N   
5001 C  CA  . PRO   B 74  ? 0.1645 0.2101 0.1240 0.0110  -0.0180 -0.0257 74   PRO   B CA  
5002 C  C   . PRO   B 74  ? 0.1516 0.1950 0.1245 0.0077  -0.0134 -0.0236 74   PRO   B C   
5003 O  O   . PRO   B 74  ? 0.1547 0.1944 0.1652 0.0125  -0.0127 -0.0375 74   PRO   B O   
5004 C  CB  . PRO   B 74  ? 0.1789 0.2285 0.1247 0.0103  -0.0157 -0.0157 74   PRO   B CB  
5005 C  CG  . PRO   B 74  ? 0.1959 0.2349 0.1526 0.0134  -0.0134 -0.0163 74   PRO   B CG  
5006 C  CD  . PRO   B 74  ? 0.1932 0.2254 0.1403 0.0151  -0.0136 -0.0308 74   PRO   B CD  
5014 N  N   . LEU   B 75  ? 0.1480 0.1859 0.1089 0.0130  -0.0167 -0.0234 75   LEU   B N   
5015 C  CA  . LEU   B 75  ? 0.1473 0.1839 0.1220 0.0075  -0.0140 -0.0063 75   LEU   B CA  
5016 C  C   . LEU   B 75  ? 0.1535 0.1916 0.1219 0.0079  -0.0019 -0.0082 75   LEU   B C   
5017 O  O   . LEU   B 75  ? 0.1692 0.2002 0.1347 0.0017  -0.0023 0.0006  75   LEU   B O   
5018 C  CB  . LEU   B 75  ? 0.1596 0.1847 0.1089 -0.0019 -0.0170 0.0023  75   LEU   B CB  
5019 C  CG  . LEU   B 75  ? 0.1898 0.2022 0.1238 -0.0270 -0.0071 -0.0049 75   LEU   B CG  
5020 C  CD1 . LEU   B 75  ? 0.2222 0.2174 0.1323 -0.0375 0.0136  -0.0022 75   LEU   B CD1 
5021 C  CD2 . LEU   B 75  ? 0.2237 0.2199 0.1911 -0.0261 0.0009  0.0009  75   LEU   B CD2 
5033 N  N   . LYS   B 76  ? 0.1528 0.2134 0.1469 0.0038  -0.0001 -0.0001 76   LYS   B N   
5034 C  CA  . LYS   B 76  ? 0.1650 0.2200 0.1764 -0.0020 0.0248  0.0004  76   LYS   B CA  
5035 C  C   . LYS   B 76  ? 0.1580 0.2020 0.1476 0.0049  0.0101  0.0171  76   LYS   B C   
5036 O  O   . LYS   B 76  ? 0.1570 0.1857 0.1470 0.0020  0.0059  0.0184  76   LYS   B O   
5037 C  CB  . LYS   B 76  ? 0.1846 0.2305 0.2531 -0.0059 0.0442  -0.0333 76   LYS   B CB  
5038 C  CG  . LYS   B 76  ? 0.1961 0.2440 0.3163 0.0026  0.0355  -0.0485 76   LYS   B CG  
5039 C  CD  . LYS   B 76  ? 0.1981 0.2493 0.3674 0.0090  0.0182  -0.0681 76   LYS   B CD  
5040 C  CE  . LYS   B 76  ? 0.2077 0.2681 0.4210 0.0113  0.0046  -0.0793 76   LYS   B CE  
5041 N  NZ  . LYS   B 76  ? 0.2108 0.2739 0.4462 0.0111  -0.0091 -0.0955 76   LYS   B NZ  
5055 N  N   . VAL   B 77  ? 0.1696 0.2116 0.1404 0.0202  0.0145  0.0203  77   VAL   B N   
5056 C  CA  . VAL   B 77  ? 0.1709 0.1993 0.1535 0.0276  0.0236  0.0402  77   VAL   B CA  
5057 C  C   . VAL   B 77  ? 0.1574 0.1785 0.1495 0.0238  0.0259  0.0337  77   VAL   B C   
5058 O  O   . VAL   B 77  ? 0.1618 0.1760 0.1545 0.0289  0.0297  0.0288  77   VAL   B O   
5059 C  CB  . VAL   B 77  ? 0.1804 0.2064 0.1852 0.0257  0.0315  0.0540  77   VAL   B CB  
5060 C  CG1 . VAL   B 77  ? 0.1865 0.1958 0.2211 0.0124  0.0370  0.0646  77   VAL   B CG1 
5061 C  CG2 . VAL   B 77  ? 0.1875 0.2233 0.2129 0.0243  0.0174  0.0646  77   VAL   B CG2 
5071 N  N   . GLY   B 78  ? 0.1517 0.1694 0.1481 0.0154  0.0236  0.0270  78   GLY   B N   
5072 C  CA  . GLY   B 78  ? 0.1459 0.1600 0.1501 0.0186  0.0269  0.0144  78   GLY   B CA  
5073 C  C   . GLY   B 78  ? 0.1427 0.1572 0.1356 0.0105  0.0177  0.0172  78   GLY   B C   
5074 O  O   . GLY   B 78  ? 0.1478 0.1503 0.1510 0.0154  0.0197  0.0180  78   GLY   B O   
5078 N  N   . GLY   B 79  ? 0.1395 0.1644 0.1375 0.0081  0.0204  0.0120  79   GLY   B N   
5079 C  CA  . GLY   B 79  ? 0.1379 0.1535 0.1347 0.0148  0.0073  0.0053  79   GLY   B CA  
5080 C  C   . GLY   B 79  ? 0.1273 0.1414 0.1335 0.0136  0.0079  0.0029  79   GLY   B C   
5081 O  O   . GLY   B 79  ? 0.1404 0.1424 0.1423 0.0178  0.0189  0.0113  79   GLY   B O   
5085 N  N   . SER   B 80  ? 0.1298 0.1329 0.1439 0.0060  0.0153  -0.0020 80   SER   B N   
5086 C  CA  . SER   B 80  ? 0.1252 0.1327 0.1408 0.0032  0.0107  -0.0013 80   SER   B CA  
5087 C  C   . SER   B 80  ? 0.1274 0.1263 0.1372 0.0084  -0.0093 -0.0037 80   SER   B C   
5088 O  O   . SER   B 80  ? 0.1441 0.1336 0.1606 0.0133  0.0028  -0.0143 80   SER   B O   
5089 C  CB  . SER   B 80  ? 0.1324 0.1326 0.1531 -0.0034 0.0036  0.0008  80   SER   B CB  
5090 O  OG  . SER   B 80  ? 0.1399 0.1491 0.1701 0.0015  -0.0079 0.0079  80   SER   B OG  
5096 N  N   . CYS   B 81  ? 0.1288 0.1190 0.1411 0.0044  -0.0054 -0.0072 81   CYS   B N   
5097 C  CA  . CYS   B 81  ? 0.1355 0.1189 0.1424 0.0045  -0.0092 -0.0052 81   CYS   B CA  
5098 C  C   . CYS   B 81  ? 0.1304 0.1128 0.1246 0.0004  -0.0129 -0.0025 81   CYS   B C   
5099 O  O   . CYS   B 81  ? 0.1566 0.1217 0.1265 0.0098  -0.0043 -0.0061 81   CYS   B O   
5100 C  CB  . CYS   B 81  ? 0.1497 0.1307 0.1390 -0.0073 -0.0134 -0.0048 81   CYS   B CB  
5101 S  SG  . CYS   B 81  ? 0.1483 0.1486 0.1358 -0.0038 -0.0214 -0.0143 81   CYS   B SG  
5107 N  N   . VAL   B 82  ? 0.1301 0.1163 0.1370 -0.0014 -0.0116 -0.0058 82   VAL   B N   
5108 C  CA  . VAL   B 82  ? 0.1391 0.1240 0.1352 -0.0058 -0.0115 0.0018  82   VAL   B CA  
5109 C  C   . VAL   B 82  ? 0.1483 0.1160 0.1417 0.0006  -0.0033 -0.0061 82   VAL   B C   
5110 O  O   . VAL   B 82  ? 0.1562 0.1168 0.1729 -0.0014 -0.0012 -0.0195 82   VAL   B O   
5111 C  CB  . VAL   B 82  ? 0.1473 0.1397 0.1563 -0.0002 -0.0125 0.0072  82   VAL   B CB  
5112 C  CG1 . VAL   B 82  ? 0.1657 0.1595 0.1671 0.0033  -0.0140 0.0154  82   VAL   B CG1 
5113 C  CG2 . VAL   B 82  ? 0.1569 0.1560 0.1620 -0.0028 -0.0293 0.0147  82   VAL   B CG2 
5123 N  N   . LEU   B 83  ? 0.1366 0.1129 0.1450 -0.0155 -0.0164 -0.0084 83   LEU   B N   
5124 C  CA  . LEU   B 83  ? 0.1355 0.1186 0.1349 -0.0098 -0.0186 -0.0090 83   LEU   B CA  
5125 C  C   . LEU   B 83  ? 0.1384 0.1150 0.1331 -0.0176 -0.0145 -0.0027 83   LEU   B C   
5126 O  O   . LEU   B 83  ? 0.1409 0.1284 0.1194 -0.0190 -0.0125 0.0029  83   LEU   B O   
5127 C  CB  . LEU   B 83  ? 0.1410 0.1317 0.1399 -0.0086 -0.0230 -0.0149 83   LEU   B CB  
5128 C  CG  . LEU   B 83  ? 0.1581 0.1534 0.1483 -0.0082 -0.0084 -0.0144 83   LEU   B CG  
5129 C  CD1 . LEU   B 83  ? 0.1737 0.1609 0.1458 -0.0076 -0.0212 0.0033  83   LEU   B CD1 
5130 C  CD2 . LEU   B 83  ? 0.1714 0.1528 0.1648 0.0008  -0.0009 -0.0291 83   LEU   B CD2 
5142 N  N   . SER   B 84  ? 0.1424 0.1279 0.1548 -0.0209 -0.0113 -0.0021 84   SER   B N   
5143 C  CA  . SER   B 84  ? 0.1473 0.1437 0.1441 -0.0245 -0.0120 0.0103  84   SER   B CA  
5144 C  C   . SER   B 84  ? 0.1348 0.1622 0.1107 -0.0186 -0.0118 0.0171  84   SER   B C   
5145 O  O   . SER   B 84  ? 0.1401 0.1498 0.1138 -0.0158 -0.0055 -0.0004 84   SER   B O   
5146 C  CB  . SER   B 84  ? 0.1657 0.1545 0.1889 -0.0281 0.0088  0.0164  84   SER   B CB  
5147 O  OG  . SER   B 84  ? 0.1622 0.1690 0.2360 -0.0368 0.0094  0.0224  84   SER   B OG  
5153 N  N   . GLY   B 85  ? 0.1414 0.1840 0.1269 -0.0176 -0.0101 0.0221  85   GLY   B N   
5154 C  CA  . GLY   B 85  ? 0.1402 0.1912 0.1359 -0.0286 0.0025  0.0003  85   GLY   B CA  
5155 C  C   . GLY   B 85  ? 0.1369 0.1684 0.1299 -0.0374 -0.0020 0.0110  85   GLY   B C   
5156 O  O   . GLY   B 85  ? 0.1463 0.1687 0.1295 -0.0471 0.0155  -0.0025 85   GLY   B O   
5160 N  N   . HIS   B 86  ? 0.1355 0.1498 0.1445 -0.0271 -0.0169 0.0158  86   HIS   B N   
5161 C  CA  . HIS   B 86  ? 0.1404 0.1534 0.1456 -0.0299 -0.0172 0.0160  86   HIS   B CA  
5162 C  C   . HIS   B 86  ? 0.1420 0.1675 0.1420 -0.0395 -0.0140 0.0290  86   HIS   B C   
5163 O  O   . HIS   B 86  ? 0.1508 0.1781 0.1508 -0.0356 -0.0038 0.0301  86   HIS   B O   
5164 C  CB  . HIS   B 86  ? 0.1474 0.1543 0.1436 -0.0172 -0.0256 0.0046  86   HIS   B CB  
5165 C  CG  . HIS   B 86  ? 0.1505 0.1648 0.1423 -0.0087 -0.0203 0.0075  86   HIS   B CG  
5166 N  ND1 . HIS   B 86  ? 0.1556 0.1870 0.1576 -0.0201 -0.0193 -0.0062 86   HIS   B ND1 
5167 C  CD2 . HIS   B 86  ? 0.1508 0.1614 0.1491 -0.0058 -0.0179 0.0090  86   HIS   B CD2 
5168 C  CE1 . HIS   B 86  ? 0.1651 0.1850 0.1530 -0.0171 -0.0038 -0.0167 86   HIS   B CE1 
5169 N  NE2 . HIS   B 86  ? 0.1568 0.1726 0.1424 0.0018  -0.0092 -0.0108 86   HIS   B NE2 
5177 N  N   . ASN   B 87  ? 0.1409 0.1711 0.1428 -0.0353 -0.0020 0.0284  87   ASN   B N   
5178 C  CA  . ASN   B 87  ? 0.1427 0.1894 0.1410 -0.0317 0.0111  0.0182  87   ASN   B CA  
5179 C  C   . ASN   B 87  ? 0.1568 0.1699 0.1321 -0.0269 0.0230  0.0142  87   ASN   B C   
5180 O  O   . ASN   B 87  ? 0.1768 0.1770 0.1674 -0.0202 0.0416  0.0072  87   ASN   B O   
5181 C  CB  . ASN   B 87  ? 0.1490 0.2283 0.1724 -0.0294 0.0230  0.0148  87   ASN   B CB  
5182 C  CG  . ASN   B 87  ? 0.1533 0.2471 0.1839 0.0045  0.0281  0.0279  87   ASN   B CG  
5183 O  OD1 . ASN   B 87  ? 0.1515 0.2322 0.1703 0.0066  0.0373  0.0442  87   ASN   B OD1 
5184 N  ND2 . ASN   B 87  ? 0.1869 0.2605 0.2228 0.0093  0.0293  0.0229  87   ASN   B ND2 
5191 N  N   . LEU   B 88  ? 0.1492 0.1588 0.1243 -0.0271 0.0108  0.0144  88   LEU   B N   
5192 C  CA  . LEU   B 88  ? 0.1560 0.1547 0.1245 -0.0312 0.0058  0.0014  88   LEU   B CA  
5193 C  C   . LEU   B 88  ? 0.1595 0.1500 0.1267 -0.0359 0.0020  0.0042  88   LEU   B C   
5194 O  O   . LEU   B 88  ? 0.1838 0.1556 0.1575 -0.0220 -0.0260 -0.0095 88   LEU   B O   
5195 C  CB  . LEU   B 88  ? 0.1618 0.1558 0.1461 -0.0386 -0.0100 0.0123  88   LEU   B CB  
5196 C  CG  . LEU   B 88  ? 0.2011 0.1892 0.1623 -0.0281 -0.0245 0.0340  88   LEU   B CG  
5197 C  CD1 . LEU   B 88  ? 0.2137 0.2173 0.1769 -0.0396 -0.0164 0.0434  88   LEU   B CD1 
5198 C  CD2 . LEU   B 88  ? 0.2325 0.2099 0.2220 0.0093  -0.0453 0.0107  88   LEU   B CD2 
5210 N  N   . ALA   B 89  ? 0.1447 0.1463 0.1193 -0.0330 0.0121  0.0013  89   ALA   B N   
5211 C  CA  . ALA   B 89  ? 0.1442 0.1420 0.0978 -0.0313 -0.0020 0.0111  89   ALA   B CA  
5212 C  C   . ALA   B 89  ? 0.1540 0.1434 0.1045 -0.0345 0.0150  0.0077  89   ALA   B C   
5213 O  O   . ALA   B 89  ? 0.1392 0.1511 0.1457 -0.0373 0.0150  -0.0260 89   ALA   B O   
5214 C  CB  . ALA   B 89  ? 0.1371 0.1401 0.1188 -0.0330 0.0007  0.0148  89   ALA   B CB  
5220 N  N   . LYS   B 90  ? 0.1862 0.1317 0.1182 -0.0391 -0.0061 0.0100  90   LYS   B N   
5221 C  CA  . LYS   B 90  ? 0.2011 0.1310 0.1200 -0.0374 -0.0093 0.0086  90   LYS   B CA  
5222 C  C   . LYS   B 90  ? 0.1864 0.1286 0.1293 -0.0381 -0.0071 -0.0018 90   LYS   B C   
5223 O  O   . LYS   B 90  ? 0.1995 0.1422 0.1454 -0.0539 -0.0003 -0.0004 90   LYS   B O   
5224 C  CB  . LYS   B 90  ? 0.2215 0.1360 0.1497 -0.0307 -0.0035 0.0210  90   LYS   B CB  
5225 C  CG  . LYS   B 90  ? 0.2282 0.1527 0.1495 -0.0140 0.0257  0.0202  90   LYS   B CG  
5226 C  CD  . LYS   B 90  ? 0.2578 0.1824 0.2034 -0.0068 0.0440  0.0032  90   LYS   B CD  
5227 C  CE  . LYS   B 90  ? 0.2669 0.1999 0.2462 -0.0171 0.0476  -0.0037 90   LYS   B CE  
5228 N  NZ  . LYS   B 90  ? 0.2781 0.1905 0.2450 -0.0312 0.0595  -0.0060 90   LYS   B NZ  
5242 N  N   . HIS   B 91  ? 0.1583 0.1172 0.1157 -0.0266 -0.0159 0.0018  91   HIS   B N   
5243 C  CA  . HIS   B 91  ? 0.1456 0.1211 0.1253 -0.0217 -0.0109 0.0005  91   HIS   B CA  
5244 C  C   . HIS   B 91  ? 0.1355 0.1233 0.1016 -0.0225 -0.0053 -0.0027 91   HIS   B C   
5245 O  O   . HIS   B 91  ? 0.1534 0.1243 0.1141 -0.0211 -0.0158 0.0036  91   HIS   B O   
5246 C  CB  . HIS   B 91  ? 0.1578 0.1232 0.1662 -0.0059 -0.0042 0.0078  91   HIS   B CB  
5247 C  CG  . HIS   B 91  ? 0.2029 0.1363 0.2425 0.0067  0.0258  0.0219  91   HIS   B CG  
5248 N  ND1 . HIS   B 91  ? 0.2369 0.1476 0.3006 0.0055  0.0363  0.0114  91   HIS   B ND1 
5249 C  CD2 . HIS   B 91  ? 0.2201 0.1643 0.2882 0.0230  0.0135  0.0508  91   HIS   B CD2 
5250 C  CE1 . HIS   B 91  ? 0.2411 0.1589 0.3153 0.0223  0.0338  0.0193  91   HIS   B CE1 
5251 N  NE2 . HIS   B 91  ? 0.2314 0.1707 0.3143 0.0318  0.0285  0.0614  91   HIS   B NE2 
5259 N  N   . CYS   B 92  ? 0.1310 0.1210 0.1053 -0.0225 -0.0120 -0.0060 92   CYS   B N   
5260 C  CA  . CYS   B 92  ? 0.1316 0.1143 0.1055 -0.0210 -0.0055 -0.0013 92   CYS   B CA  
5261 C  C   . CYS   B 92  ? 0.1288 0.1120 0.0989 -0.0106 -0.0026 0.0024  92   CYS   B C   
5262 O  O   . CYS   B 92  ? 0.1330 0.1212 0.1238 -0.0129 -0.0042 -0.0036 92   CYS   B O   
5263 C  CB  . CYS   B 92  ? 0.1319 0.1249 0.1111 -0.0129 -0.0052 -0.0045 92   CYS   B CB  
5264 S  SG  . CYS   B 92  ? 0.1303 0.1278 0.1231 -0.0101 -0.0091 0.0026  92   CYS   B SG  
5270 N  N   . LEU   B 93  ? 0.1221 0.1151 0.1054 -0.0134 -0.0043 -0.0051 93   LEU   B N   
5271 C  CA  . LEU   B 93  ? 0.1231 0.1164 0.1105 -0.0047 -0.0052 -0.0011 93   LEU   B CA  
5272 C  C   . LEU   B 93  ? 0.1154 0.1130 0.1068 -0.0022 -0.0052 0.0029  93   LEU   B C   
5273 O  O   . LEU   B 93  ? 0.1201 0.1145 0.1169 -0.0033 -0.0010 0.0014  93   LEU   B O   
5274 C  CB  . LEU   B 93  ? 0.1231 0.1130 0.1265 -0.0062 -0.0082 -0.0020 93   LEU   B CB  
5275 C  CG  . LEU   B 93  ? 0.1216 0.1259 0.1382 -0.0052 -0.0047 0.0149  93   LEU   B CG  
5276 C  CD1 . LEU   B 93  ? 0.1247 0.1415 0.1412 0.0059  -0.0002 0.0016  93   LEU   B CD1 
5277 C  CD2 . LEU   B 93  ? 0.1214 0.1306 0.1511 -0.0019 -0.0050 0.0030  93   LEU   B CD2 
5289 N  N   . HIS   B 94  ? 0.1192 0.1105 0.1029 -0.0050 -0.0103 0.0035  94   HIS   B N   
5290 C  CA  . HIS   B 94  ? 0.1220 0.1141 0.1133 -0.0044 -0.0031 0.0038  94   HIS   B CA  
5291 C  C   . HIS   B 94  ? 0.1216 0.1137 0.1283 0.0010  -0.0037 0.0017  94   HIS   B C   
5292 O  O   . HIS   B 94  ? 0.1225 0.1250 0.1582 0.0000  0.0171  -0.0080 94   HIS   B O   
5293 C  CB  . HIS   B 94  ? 0.1224 0.1194 0.1166 0.0004  -0.0049 0.0039  94   HIS   B CB  
5294 C  CG  . HIS   B 94  ? 0.1235 0.1159 0.1119 -0.0061 -0.0170 0.0013  94   HIS   B CG  
5295 N  ND1 . HIS   B 94  ? 0.1275 0.1236 0.1114 -0.0071 -0.0165 -0.0034 94   HIS   B ND1 
5296 C  CD2 . HIS   B 94  ? 0.1262 0.1159 0.1170 -0.0020 -0.0130 0.0027  94   HIS   B CD2 
5297 C  CE1 . HIS   B 94  ? 0.1300 0.1243 0.1060 -0.0106 -0.0197 -0.0009 94   HIS   B CE1 
5298 N  NE2 . HIS   B 94  ? 0.1248 0.1247 0.1152 -0.0143 -0.0126 0.0034  94   HIS   B NE2 
5306 N  N   . VAL   B 95  ? 0.1129 0.1154 0.1247 0.0025  0.0018  0.0006  95   VAL   B N   
5307 C  CA  . VAL   B 95  ? 0.1177 0.1220 0.1198 0.0034  0.0039  0.0115  95   VAL   B CA  
5308 C  C   . VAL   B 95  ? 0.1235 0.1211 0.1186 0.0026  0.0107  0.0025  95   VAL   B C   
5309 O  O   . VAL   B 95  ? 0.1287 0.1216 0.1368 0.0026  0.0102  0.0104  95   VAL   B O   
5310 C  CB  . VAL   B 95  ? 0.1265 0.1195 0.1239 -0.0059 -0.0031 0.0021  95   VAL   B CB  
5311 C  CG1 . VAL   B 95  ? 0.1325 0.1340 0.1460 -0.0115 0.0016  0.0070  95   VAL   B CG1 
5312 C  CG2 . VAL   B 95  ? 0.1293 0.1182 0.1278 0.0005  -0.0071 0.0025  95   VAL   B CG2 
5322 N  N   . VAL   B 96  ? 0.1370 0.1290 0.1186 0.0089  0.0108  0.0144  96   VAL   B N   
5323 C  CA  . VAL   B 96  ? 0.1393 0.1422 0.1131 0.0101  0.0069  0.0140  96   VAL   B CA  
5324 C  C   . VAL   B 96  ? 0.1386 0.1411 0.1158 0.0118  0.0107  0.0154  96   VAL   B C   
5325 O  O   . VAL   B 96  ? 0.1408 0.1461 0.1494 0.0052  0.0182  0.0047  96   VAL   B O   
5326 C  CB  . VAL   B 96  ? 0.1451 0.1590 0.1280 0.0109  0.0130  0.0046  96   VAL   B CB  
5327 C  CG1 . VAL   B 96  ? 0.1500 0.1697 0.1347 0.0172  0.0137  0.0033  96   VAL   B CG1 
5328 C  CG2 . VAL   B 96  ? 0.1574 0.1727 0.1363 0.0103  0.0145  -0.0035 96   VAL   B CG2 
5338 N  N   . GLY   B 97  ? 0.1435 0.1430 0.1230 0.0105  0.0086  0.0175  97   GLY   B N   
5339 C  CA  . GLY   B 97  ? 0.1575 0.1436 0.1271 0.0025  0.0196  0.0154  97   GLY   B CA  
5340 C  C   . GLY   B 97  ? 0.1724 0.1496 0.1370 0.0081  0.0125  0.0143  97   GLY   B C   
5341 O  O   . GLY   B 97  ? 0.1849 0.1577 0.1360 0.0055  0.0100  0.0132  97   GLY   B O   
5345 N  N   . PRO   B 98  ? 0.1798 0.1523 0.1566 0.0112  0.0337  0.0341  98   PRO   B N   
5346 C  CA  . PRO   B 98  ? 0.1935 0.1667 0.1623 0.0185  0.0453  0.0273  98   PRO   B CA  
5347 C  C   . PRO   B 98  ? 0.2066 0.1654 0.1392 0.0246  0.0385  0.0431  98   PRO   B C   
5348 O  O   . PRO   B 98  ? 0.1986 0.1622 0.1562 0.0254  0.0402  0.0385  98   PRO   B O   
5349 C  CB  . PRO   B 98  ? 0.1850 0.1742 0.1864 0.0131  0.0513  0.0264  98   PRO   B CB  
5350 C  CG  . PRO   B 98  ? 0.1796 0.1666 0.1794 0.0100  0.0435  0.0352  98   PRO   B CG  
5351 C  CD  . PRO   B 98  ? 0.1651 0.1587 0.1727 0.0162  0.0413  0.0353  98   PRO   B CD  
5359 N  N   . ASN   B 99  ? 0.2224 0.1806 0.1472 0.0397  0.0376  0.0263  99   ASN   B N   
5360 C  CA  . ASN   B 99  ? 0.2405 0.1882 0.1461 0.0495  0.0366  0.0424  99   ASN   B CA  
5361 C  C   . ASN   B 99  ? 0.2653 0.2164 0.1761 0.0460  0.0568  0.0654  99   ASN   B C   
5362 O  O   . ASN   B 99  ? 0.2786 0.2223 0.1802 0.0429  0.0522  0.0571  99   ASN   B O   
5363 C  CB  . ASN   B 99  ? 0.2521 0.1871 0.1513 0.0476  0.0256  0.0353  99   ASN   B CB  
5364 C  CG  . ASN   B 99  ? 0.2535 0.1961 0.1768 0.0462  0.0125  0.0376  99   ASN   B CG  
5365 O  OD1 . ASN   B 99  ? 0.2604 0.2001 0.2058 0.0488  0.0062  0.0458  99   ASN   B OD1 
5366 N  ND2 . ASN   B 99  ? 0.2517 0.1998 0.1887 0.0492  -0.0108 0.0264  99   ASN   B ND2 
5373 N  N   A VAL   B 100 ? 0.2832 0.2303 0.2144 0.0324  0.0604  0.0867  100  VAL   B N   
5374 N  N   B VAL   B 100 ? 0.2857 0.2306 0.2149 0.0349  0.0543  0.0829  100  VAL   B N   
5375 C  CA  A VAL   B 100 ? 0.3117 0.2459 0.2721 0.0224  0.0604  0.0998  100  VAL   B CA  
5376 C  CA  B VAL   B 100 ? 0.3129 0.2452 0.2651 0.0253  0.0505  0.0948  100  VAL   B CA  
5377 C  C   A VAL   B 100 ? 0.3355 0.2520 0.2662 0.0278  0.0586  0.1166  100  VAL   B C   
5378 C  C   B VAL   B 100 ? 0.3353 0.2518 0.2642 0.0291  0.0496  0.1115  100  VAL   B C   
5379 O  O   A VAL   B 100 ? 0.3422 0.2627 0.2740 0.0256  0.0681  0.1103  100  VAL   B O   
5380 O  O   B VAL   B 100 ? 0.3399 0.2588 0.2686 0.0263  0.0547  0.1073  100  VAL   B O   
5381 C  CB  A VAL   B 100 ? 0.3202 0.2604 0.3398 0.0056  0.0536  0.0988  100  VAL   B CB  
5382 C  CB  B VAL   B 100 ? 0.3198 0.2561 0.3161 0.0112  0.0435  0.0932  100  VAL   B CB  
5383 C  CG1 A VAL   B 100 ? 0.3243 0.2658 0.3648 0.0023  0.0522  0.0973  100  VAL   B CG1 
5384 C  CG1 B VAL   B 100 ? 0.3231 0.2600 0.3357 0.0084  0.0416  0.0924  100  VAL   B CG1 
5385 C  CG2 A VAL   B 100 ? 0.3222 0.2643 0.3595 0.0011  0.0545  0.1005  100  VAL   B CG2 
5386 C  CG2 B VAL   B 100 ? 0.3219 0.2590 0.3310 0.0072  0.0432  0.0944  100  VAL   B CG2 
5405 N  N   . ASN   B 101 ? 0.3537 0.2579 0.2625 0.0369  0.0422  0.1210  101  ASN   B N   
5406 C  CA  . ASN   B 101 ? 0.3952 0.2815 0.2835 0.0443  0.0187  0.1245  101  ASN   B CA  
5407 C  C   . ASN   B 101 ? 0.4385 0.3265 0.2963 0.0435  0.0095  0.1218  101  ASN   B C   
5408 O  O   . ASN   B 101 ? 0.4441 0.3381 0.3084 0.0505  0.0059  0.1069  101  ASN   B O   
5409 C  CB  . ASN   B 101 ? 0.3936 0.2688 0.2914 0.0421  0.0195  0.1133  101  ASN   B CB  
5410 C  CG  . ASN   B 101 ? 0.3914 0.2552 0.2927 0.0405  0.0255  0.1137  101  ASN   B CG  
5411 O  OD1 . ASN   B 101 ? 0.3960 0.2569 0.3200 0.0327  0.0429  0.1065  101  ASN   B OD1 
5412 N  ND2 . ASN   B 101 ? 0.3879 0.2531 0.2819 0.0403  0.0187  0.1043  101  ASN   B ND2 
5420 N  N   A LYS   B 102 ? 0.4606 0.3468 0.3057 0.0372  0.0164  0.1174  102  LYS   B N   
5421 N  N   B LYS   B 102 ? 0.4511 0.3449 0.3169 0.0350  0.0121  0.1056  102  LYS   B N   
5422 C  CA  A LYS   B 102 ? 0.4812 0.3729 0.3276 0.0283  0.0306  0.0985  102  LYS   B CA  
5423 C  CA  B LYS   B 102 ? 0.4621 0.3662 0.3444 0.0249  0.0204  0.0811  102  LYS   B CA  
5424 C  C   A LYS   B 102 ? 0.4813 0.3766 0.3004 0.0301  0.0457  0.1072  102  LYS   B C   
5425 C  C   B LYS   B 102 ? 0.4582 0.3663 0.3293 0.0216  0.0283  0.0805  102  LYS   B C   
5426 O  O   A LYS   B 102 ? 0.4888 0.3799 0.3045 0.0320  0.0361  0.1046  102  LYS   B O   
5427 O  O   B LYS   B 102 ? 0.4630 0.3690 0.3320 0.0229  0.0238  0.0775  102  LYS   B O   
5428 C  CB  A LYS   B 102 ? 0.4986 0.3935 0.3856 0.0187  0.0362  0.0655  102  LYS   B CB  
5429 C  CB  B LYS   B 102 ? 0.4749 0.3856 0.3919 0.0190  0.0245  0.0538  102  LYS   B CB  
5430 C  CG  A LYS   B 102 ? 0.5133 0.4116 0.4424 0.0115  0.0427  0.0337  102  LYS   B CG  
5431 C  CG  B LYS   B 102 ? 0.4856 0.4023 0.4376 0.0145  0.0294  0.0276  102  LYS   B CG  
5432 C  CD  A LYS   B 102 ? 0.5260 0.4259 0.4957 0.0062  0.0489  0.0076  102  LYS   B CD  
5433 C  CD  B LYS   B 102 ? 0.4947 0.4153 0.4796 0.0112  0.0338  0.0064  102  LYS   B CD  
5434 C  CE  A LYS   B 102 ? 0.5353 0.4361 0.5373 0.0020  0.0528  -0.0112 102  LYS   B CE  
5435 C  CE  B LYS   B 102 ? 0.5013 0.4244 0.5120 0.0086  0.0368  -0.0087 102  LYS   B CE  
5436 N  NZ  A LYS   B 102 ? 0.5405 0.4422 0.5603 -0.0004 0.0538  -0.0216 102  LYS   B NZ  
5437 N  NZ  B LYS   B 102 ? 0.5050 0.4297 0.5297 0.0072  0.0378  -0.0167 102  LYS   B NZ  
5464 N  N   A GLY   B 103 ? 0.4704 0.3747 0.2856 0.0296  0.0719  0.1118  103  GLY   B N   
5465 N  N   B GLY   B 103 ? 0.4465 0.3612 0.3189 0.0161  0.0421  0.0808  103  GLY   B N   
5466 C  CA  A GLY   B 103 ? 0.4578 0.3730 0.2918 0.0316  0.0950  0.1007  103  GLY   B CA  
5467 C  CA  B GLY   B 103 ? 0.4339 0.3551 0.3173 0.0108  0.0538  0.0717  103  GLY   B CA  
5468 C  C   A GLY   B 103 ? 0.4417 0.3670 0.2884 0.0311  0.1157  0.0883  103  GLY   B C   
5469 C  C   B GLY   B 103 ? 0.4189 0.3461 0.3096 0.0026  0.0639  0.0604  103  GLY   B C   
5470 O  O   A GLY   B 103 ? 0.4475 0.3751 0.3018 0.0293  0.1143  0.0901  103  GLY   B O   
5471 O  O   B GLY   B 103 ? 0.4229 0.3518 0.3187 0.0039  0.0650  0.0603  103  GLY   B O   
5478 N  N   A GLU   B 104 ? 0.4174 0.3503 0.2725 0.0335  0.1342  0.0666  104  GLU   B N   
5479 N  N   B GLU   B 104 ? 0.3989 0.3290 0.2905 -0.0080 0.0695  0.0448  104  GLU   B N   
5480 C  CA  A GLU   B 104 ? 0.3928 0.3344 0.2552 0.0375  0.1440  0.0438  104  GLU   B CA  
5481 C  CA  B GLU   B 104 ? 0.3793 0.3129 0.2705 -0.0189 0.0710  0.0304  104  GLU   B CA  
5482 C  C   A GLU   B 104 ? 0.3942 0.3333 0.2771 0.0202  0.1666  0.0402  104  GLU   B C   
5483 C  C   B GLU   B 104 ? 0.3753 0.3103 0.2786 -0.0264 0.0915  0.0263  104  GLU   B C   
5484 O  O   A GLU   B 104 ? 0.3970 0.3355 0.3073 0.0156  0.1617  0.0365  104  GLU   B O   
5485 O  O   B GLU   B 104 ? 0.3766 0.3110 0.2878 -0.0288 0.0917  0.0215  104  GLU   B O   
5486 C  CB  A GLU   B 104 ? 0.3722 0.3183 0.2393 0.0606  0.1140  0.0154  104  GLU   B CB  
5487 C  CB  B GLU   B 104 ? 0.3668 0.2977 0.2505 -0.0226 0.0470  0.0164  104  GLU   B CB  
5488 C  CG  A GLU   B 104 ? 0.3555 0.3068 0.2257 0.0809  0.0716  -0.0122 104  GLU   B CG  
5489 C  CG  B GLU   B 104 ? 0.3573 0.2844 0.2314 -0.0261 0.0179  0.0020  104  GLU   B CG  
5490 C  CD  A GLU   B 104 ? 0.3396 0.2952 0.2074 0.0992  0.0351  -0.0258 104  GLU   B CD  
5491 C  CD  B GLU   B 104 ? 0.3492 0.2714 0.2123 -0.0325 -0.0048 -0.0022 104  GLU   B CD  
5492 O  OE1 A GLU   B 104 ? 0.3219 0.2816 0.1660 0.1133  0.0399  -0.0271 104  GLU   B OE1 
5493 O  OE1 B GLU   B 104 ? 0.3413 0.2616 0.1978 -0.0396 -0.0052 0.0019  104  GLU   B OE1 
5494 O  OE2 A GLU   B 104 ? 0.3426 0.3016 0.2314 0.0985  0.0032  -0.0312 104  GLU   B OE2 
5495 O  OE2 B GLU   B 104 ? 0.3491 0.2706 0.2070 -0.0340 -0.0227 -0.0079 104  GLU   B OE2 
5508 N  N   A ASP   B 105 ? 0.3898 0.3327 0.2830 0.0056  0.1884  0.0456  105  ASP   B N   
5509 N  N   B ASP   B 105 ? 0.3694 0.3092 0.2805 -0.0327 0.1093  0.0282  105  ASP   B N   
5510 C  CA  A ASP   B 105 ? 0.3879 0.3311 0.3078 -0.0046 0.1988  0.0334  105  ASP   B CA  
5511 C  CA  B ASP   B 105 ? 0.3651 0.3079 0.2977 -0.0369 0.1217  0.0218  105  ASP   B CA  
5512 C  C   A ASP   B 105 ? 0.3683 0.3036 0.2915 -0.0106 0.1904  0.0275  105  ASP   B C   
5513 C  C   B ASP   B 105 ? 0.3559 0.2941 0.2825 -0.0389 0.1218  0.0151  105  ASP   B C   
5514 O  O   A ASP   B 105 ? 0.3586 0.2968 0.2882 -0.0062 0.1884  0.0232  105  ASP   B O   
5515 O  O   B ASP   B 105 ? 0.3507 0.2885 0.2711 -0.0411 0.1272  0.0153  105  ASP   B O   
5516 C  CB  A ASP   B 105 ? 0.4018 0.3526 0.3743 -0.0019 0.2031  0.0187  105  ASP   B CB  
5517 C  CB  B ASP   B 105 ? 0.3678 0.3176 0.3346 -0.0372 0.1309  0.0193  105  ASP   B CB  
5518 C  CG  A ASP   B 105 ? 0.4117 0.3671 0.4348 -0.0020 0.2090  0.0103  105  ASP   B CG  
5519 C  CG  B ASP   B 105 ? 0.3689 0.3223 0.3678 -0.0403 0.1409  0.0218  105  ASP   B CG  
5520 O  OD1 A ASP   B 105 ? 0.4126 0.3722 0.4445 -0.0072 0.2185  0.0156  105  ASP   B OD1 
5521 O  OD1 B ASP   B 105 ? 0.3684 0.3246 0.3757 -0.0453 0.1448  0.0244  105  ASP   B OD1 
5522 O  OD2 A ASP   B 105 ? 0.4171 0.3735 0.4736 0.0019  0.1979  0.0007  105  ASP   B OD2 
5523 O  OD2 B ASP   B 105 ? 0.3664 0.3235 0.3748 -0.0425 0.1503  0.0256  105  ASP   B OD2 
5532 N  N   A ILE   B 106 ? 0.3605 0.2788 0.2988 -0.0187 0.1825  0.0304  106  ILE   B N   
5533 N  N   B ILE   B 106 ? 0.3499 0.2848 0.2846 -0.0365 0.1117  0.0083  106  ILE   B N   
5534 C  CA  A ILE   B 106 ? 0.3417 0.2531 0.3131 -0.0295 0.1810  0.0277  106  ILE   B CA  
5535 C  CA  B ILE   B 106 ? 0.3388 0.2761 0.2935 -0.0355 0.1068  -0.0006 106  ILE   B CA  
5536 C  C   A ILE   B 106 ? 0.3107 0.2471 0.3058 -0.0242 0.1801  0.0146  106  ILE   B C   
5537 C  C   B ILE   B 106 ? 0.3188 0.2742 0.2958 -0.0307 0.1027  -0.0140 106  ILE   B C   
5538 O  O   A ILE   B 106 ? 0.3037 0.2282 0.3065 -0.0259 0.1773  0.0133  106  ILE   B O   
5539 O  O   B ILE   B 106 ? 0.3153 0.2659 0.2904 -0.0343 0.0927  -0.0227 106  ILE   B O   
5540 C  CB  A ILE   B 106 ? 0.3585 0.2427 0.3340 -0.0410 0.1672  0.0376  106  ILE   B CB  
5541 C  CB  B ILE   B 106 ? 0.3495 0.2751 0.3028 -0.0375 0.1034  0.0039  106  ILE   B CB  
5542 C  CG1 A ILE   B 106 ? 0.3660 0.2439 0.3396 -0.0355 0.1595  0.0301  106  ILE   B CG1 
5543 C  CG1 B ILE   B 106 ? 0.3546 0.2767 0.3072 -0.0327 0.0994  0.0031  106  ILE   B CG1 
5544 C  CG2 A ILE   B 106 ? 0.3637 0.2411 0.3509 -0.0510 0.1630  0.0474  106  ILE   B CG2 
5545 C  CG2 B ILE   B 106 ? 0.3528 0.2765 0.3124 -0.0411 0.1028  0.0061  106  ILE   B CG2 
5546 C  CD1 A ILE   B 106 ? 0.3687 0.2463 0.3373 -0.0293 0.1581  0.0274  106  ILE   B CD1 
5547 C  CD1 B ILE   B 106 ? 0.3566 0.2780 0.3089 -0.0284 0.0985  0.0037  106  ILE   B CD1 
5570 N  N   A GLN   B 107 ? 0.2951 0.2648 0.3204 -0.0251 0.1697  0.0085  107  GLN   B N   
5571 N  N   B GLN   B 107 ? 0.3054 0.2825 0.3126 -0.0254 0.0996  -0.0162 107  GLN   B N   
5572 C  CA  A GLN   B 107 ? 0.2766 0.2782 0.3358 -0.0261 0.1537  0.0061  107  GLN   B CA  
5573 C  CA  B GLN   B 107 ? 0.2911 0.2877 0.3297 -0.0201 0.0949  -0.0126 107  GLN   B CA  
5574 C  C   A GLN   B 107 ? 0.2490 0.2576 0.3074 -0.0182 0.1181  -0.0064 107  GLN   B C   
5575 C  C   B GLN   B 107 ? 0.2595 0.2657 0.3017 -0.0140 0.0901  -0.0160 107  GLN   B C   
5576 O  O   A GLN   B 107 ? 0.2444 0.2553 0.3351 -0.0121 0.0913  -0.0214 107  GLN   B O   
5577 O  O   B GLN   B 107 ? 0.2579 0.2683 0.3159 -0.0126 0.0747  -0.0286 107  GLN   B O   
5578 C  CB  A GLN   B 107 ? 0.3002 0.3123 0.4008 -0.0260 0.1393  0.0093  107  GLN   B CB  
5579 C  CB  B GLN   B 107 ? 0.3119 0.3141 0.3834 -0.0171 0.0844  -0.0077 107  GLN   B CB  
5580 C  CG  A GLN   B 107 ? 0.3284 0.3441 0.4676 -0.0181 0.1043  0.0083  107  GLN   B CG  
5581 C  CG  B GLN   B 107 ? 0.3328 0.3377 0.4363 -0.0110 0.0654  -0.0037 107  GLN   B CG  
5582 C  CD  A GLN   B 107 ? 0.3482 0.3681 0.5196 -0.0148 0.0799  0.0108  107  GLN   B CD  
5583 C  CD  B GLN   B 107 ? 0.3480 0.3555 0.4793 -0.0081 0.0510  0.0010  107  GLN   B CD  
5584 O  OE1 A GLN   B 107 ? 0.3544 0.3775 0.5376 -0.0121 0.0794  0.0094  107  GLN   B OE1 
5585 O  OE1 B GLN   B 107 ? 0.3532 0.3626 0.4939 -0.0068 0.0520  0.0018  107  GLN   B OE1 
5586 N  NE2 A GLN   B 107 ? 0.3560 0.3746 0.5375 -0.0120 0.0666  0.0155  107  GLN   B NE2 
5587 N  NE2 B GLN   B 107 ? 0.3540 0.3608 0.4946 -0.0059 0.0429  0.0049  107  GLN   B NE2 
5604 N  N   . LEU   B 108 ? 0.2297 0.2404 0.2714 -0.0023 0.0928  -0.0099 108  LEU   B N   
5605 C  CA  . LEU   B 108 ? 0.2093 0.2128 0.2304 0.0195  0.0632  0.0004  108  LEU   B CA  
5606 C  C   . LEU   B 108 ? 0.1808 0.1738 0.2119 0.0221  0.0415  0.0206  108  LEU   B C   
5607 O  O   . LEU   B 108 ? 0.1858 0.1675 0.2096 0.0208  0.0261  0.0193  108  LEU   B O   
5608 C  CB  . LEU   B 108 ? 0.2252 0.2331 0.2051 0.0188  0.0643  0.0008  108  LEU   B CB  
5609 C  CG  . LEU   B 108 ? 0.2415 0.2627 0.2041 0.0221  0.0530  -0.0168 108  LEU   B CG  
5610 C  CD1 . LEU   B 108 ? 0.2485 0.2758 0.1846 0.0136  0.0520  -0.0133 108  LEU   B CD1 
5611 C  CD2 . LEU   B 108 ? 0.2559 0.2759 0.2234 0.0289  0.0430  -0.0270 108  LEU   B CD2 
5624 N  N   . LEU   B 109 ? 0.1678 0.1559 0.2001 0.0161  0.0386  0.0233  109  LEU   B N   
5625 C  CA  . LEU   B 109 ? 0.1516 0.1344 0.2095 0.0107  0.0336  0.0263  109  LEU   B CA  
5626 C  C   . LEU   B 109 ? 0.1413 0.1245 0.2082 0.0061  0.0326  0.0163  109  LEU   B C   
5627 O  O   . LEU   B 109 ? 0.1364 0.1251 0.2088 0.0079  0.0307  0.0335  109  LEU   B O   
5628 C  CB  . LEU   B 109 ? 0.1606 0.1315 0.2100 0.0068  0.0285  0.0348  109  LEU   B CB  
5629 C  CG  . LEU   B 109 ? 0.1564 0.1309 0.2023 0.0045  0.0154  0.0215  109  LEU   B CG  
5630 C  CD1 . LEU   B 109 ? 0.1569 0.1420 0.2030 0.0104  0.0271  0.0226  109  LEU   B CD1 
5631 C  CD2 . LEU   B 109 ? 0.1642 0.1343 0.2226 0.0050  0.0134  0.0213  109  LEU   B CD2 
5643 N  N   . LYS   B 110 ? 0.1364 0.1247 0.1989 -0.0011 0.0322  0.0233  110  LYS   B N   
5644 C  CA  . LYS   B 110 ? 0.1393 0.1224 0.1920 -0.0012 0.0257  0.0129  110  LYS   B CA  
5645 C  C   . LYS   B 110 ? 0.1348 0.1235 0.1871 0.0013  0.0217  0.0116  110  LYS   B C   
5646 O  O   . LYS   B 110 ? 0.1330 0.1247 0.1843 -0.0021 0.0190  0.0080  110  LYS   B O   
5647 C  CB  . LYS   B 110 ? 0.1402 0.1258 0.2216 -0.0022 0.0265  0.0062  110  LYS   B CB  
5648 C  CG  . LYS   B 110 ? 0.1393 0.1253 0.2358 -0.0060 0.0187  0.0155  110  LYS   B CG  
5649 C  CD  . LYS   B 110 ? 0.1416 0.1277 0.2370 -0.0019 0.0169  0.0172  110  LYS   B CD  
5650 C  CE  . LYS   B 110 ? 0.1380 0.1403 0.2566 0.0011  0.0151  0.0087  110  LYS   B CE  
5651 N  NZ  . LYS   B 110 ? 0.1385 0.1485 0.2488 0.0049  0.0096  0.0031  110  LYS   B NZ  
5665 N  N   . SER   B 111 ? 0.1364 0.1251 0.1951 -0.0046 0.0279  0.0145  111  SER   B N   
5666 C  CA  . SER   B 111 ? 0.1442 0.1277 0.1844 0.0005  0.0211  0.0133  111  SER   B CA  
5667 C  C   . SER   B 111 ? 0.1373 0.1232 0.1721 -0.0001 0.0126  0.0098  111  SER   B C   
5668 O  O   . SER   B 111 ? 0.1324 0.1324 0.1755 -0.0034 0.0069  0.0133  111  SER   B O   
5669 C  CB  . SER   B 111 ? 0.1559 0.1482 0.1897 0.0013  0.0369  0.0258  111  SER   B CB  
5670 O  OG  . SER   B 111 ? 0.1753 0.1880 0.2062 0.0047  0.0480  0.0249  111  SER   B OG  
5676 N  N   . ALA   B 112 ? 0.1271 0.1261 0.1792 0.0056  0.0178  0.0186  112  ALA   B N   
5677 C  CA  . ALA   B 112 ? 0.1260 0.1345 0.1737 0.0032  0.0051  0.0052  112  ALA   B CA  
5678 C  C   . ALA   B 112 ? 0.1167 0.1255 0.1676 0.0037  0.0101  0.0063  112  ALA   B C   
5679 O  O   . ALA   B 112 ? 0.1178 0.1288 0.1750 -0.0017 0.0111  0.0014  112  ALA   B O   
5680 C  CB  . ALA   B 112 ? 0.1336 0.1417 0.1726 0.0050  0.0002  0.0068  112  ALA   B CB  
5686 N  N   . TYR   B 113 ? 0.1160 0.1195 0.1765 -0.0012 0.0133  0.0091  113  TYR   B N   
5687 C  CA  . TYR   B 113 ? 0.1168 0.1147 0.1683 -0.0021 0.0153  -0.0001 113  TYR   B CA  
5688 C  C   . TYR   B 113 ? 0.1146 0.1041 0.1734 -0.0097 0.0127  0.0026  113  TYR   B C   
5689 O  O   . TYR   B 113 ? 0.1171 0.1103 0.1691 -0.0052 0.0043  -0.0030 113  TYR   B O   
5690 C  CB  . TYR   B 113 ? 0.1271 0.1060 0.1764 -0.0059 0.0197  0.0083  113  TYR   B CB  
5691 C  CG  . TYR   B 113 ? 0.1234 0.1108 0.1868 -0.0050 0.0118  0.0071  113  TYR   B CG  
5692 C  CD1 . TYR   B 113 ? 0.1309 0.1140 0.1926 -0.0067 0.0195  0.0137  113  TYR   B CD1 
5693 C  CD2 . TYR   B 113 ? 0.1281 0.1086 0.1865 -0.0011 0.0090  0.0086  113  TYR   B CD2 
5694 C  CE1 . TYR   B 113 ? 0.1320 0.1188 0.1848 -0.0006 0.0190  0.0072  113  TYR   B CE1 
5695 C  CE2 . TYR   B 113 ? 0.1351 0.1083 0.1955 0.0002  0.0125  0.0160  113  TYR   B CE2 
5696 C  CZ  . TYR   B 113 ? 0.1292 0.1099 0.1986 0.0069  0.0110  0.0060  113  TYR   B CZ  
5697 O  OH  . TYR   B 113 ? 0.1393 0.1090 0.2156 0.0094  0.0200  0.0082  113  TYR   B OH  
5707 N  N   . GLU   B 114 ? 0.1194 0.1026 0.1798 -0.0028 0.0171  0.0006  114  GLU   B N   
5708 C  CA  . GLU   B 114 ? 0.1160 0.1062 0.1720 0.0010  0.0088  0.0008  114  GLU   B CA  
5709 C  C   . GLU   B 114 ? 0.1114 0.1102 0.1641 -0.0024 0.0090  0.0037  114  GLU   B C   
5710 O  O   . GLU   B 114 ? 0.1104 0.1113 0.1746 -0.0012 0.0091  0.0114  114  GLU   B O   
5711 C  CB  . GLU   B 114 ? 0.1146 0.1170 0.1769 -0.0040 0.0120  0.0028  114  GLU   B CB  
5712 C  CG  . GLU   B 114 ? 0.1243 0.1181 0.1763 -0.0013 0.0140  0.0116  114  GLU   B CG  
5713 C  CD  . GLU   B 114 ? 0.1163 0.1211 0.1767 -0.0042 0.0117  0.0038  114  GLU   B CD  
5714 O  OE1 . GLU   B 114 ? 0.1181 0.1320 0.1816 -0.0071 0.0202  0.0087  114  GLU   B OE1 
5715 O  OE2 . GLU   B 114 ? 0.1203 0.1358 0.1898 -0.0173 0.0163  0.0056  114  GLU   B OE2 
5722 N  N   . ASN   B 115 ? 0.1133 0.1074 0.1649 -0.0042 0.0044  0.0050  115  ASN   B N   
5723 C  CA  . ASN   B 115 ? 0.1143 0.1152 0.1541 -0.0059 0.0078  0.0055  115  ASN   B CA  
5724 C  C   . ASN   B 115 ? 0.1126 0.1107 0.1496 -0.0116 0.0018  -0.0022 115  ASN   B C   
5725 O  O   . ASN   B 115 ? 0.1258 0.1175 0.1602 -0.0138 0.0009  0.0040  115  ASN   B O   
5726 C  CB  . ASN   B 115 ? 0.1242 0.1262 0.1563 -0.0047 0.0122  0.0019  115  ASN   B CB  
5727 C  CG  . ASN   B 115 ? 0.1361 0.1297 0.1484 0.0044  0.0042  0.0002  115  ASN   B CG  
5728 O  OD1 . ASN   B 115 ? 0.1814 0.1368 0.1711 0.0012  0.0104  -0.0106 115  ASN   B OD1 
5729 N  ND2 . ASN   B 115 ? 0.1336 0.1383 0.1505 -0.0047 0.0059  0.0045  115  ASN   B ND2 
5736 N  N   . PHE   B 116 ? 0.1113 0.1109 0.1432 -0.0027 0.0066  -0.0010 116  PHE   B N   
5737 C  CA  . PHE   B 116 ? 0.1174 0.1130 0.1452 -0.0103 -0.0008 0.0009  116  PHE   B CA  
5738 C  C   . PHE   B 116 ? 0.1192 0.1034 0.1423 -0.0094 -0.0015 0.0057  116  PHE   B C   
5739 O  O   . PHE   B 116 ? 0.1226 0.1146 0.1549 -0.0026 -0.0000 0.0005  116  PHE   B O   
5740 C  CB  . PHE   B 116 ? 0.1135 0.1085 0.1470 -0.0044 -0.0101 0.0034  116  PHE   B CB  
5741 C  CG  . PHE   B 116 ? 0.1110 0.1111 0.1503 -0.0072 0.0001  -0.0014 116  PHE   B CG  
5742 C  CD1 . PHE   B 116 ? 0.1214 0.1150 0.1657 -0.0047 0.0029  0.0010  116  PHE   B CD1 
5743 C  CD2 . PHE   B 116 ? 0.1194 0.1182 0.1470 -0.0042 0.0032  -0.0103 116  PHE   B CD2 
5744 C  CE1 . PHE   B 116 ? 0.1202 0.1201 0.1582 -0.0008 -0.0090 0.0043  116  PHE   B CE1 
5745 C  CE2 . PHE   B 116 ? 0.1180 0.1164 0.1485 -0.0011 0.0016  -0.0013 116  PHE   B CE2 
5746 C  CZ  . PHE   B 116 ? 0.1141 0.1208 0.1585 -0.0017 -0.0044 0.0041  116  PHE   B CZ  
5756 N  N   . ASN   B 117 ? 0.1176 0.1077 0.1628 -0.0039 -0.0035 0.0051  117  ASN   B N   
5757 C  CA  . ASN   B 117 ? 0.1257 0.1082 0.1600 -0.0034 -0.0001 0.0001  117  ASN   B CA  
5758 C  C   . ASN   B 117 ? 0.1257 0.1089 0.1668 0.0002  0.0051  0.0034  117  ASN   B C   
5759 O  O   . ASN   B 117 ? 0.1330 0.1171 0.2002 -0.0014 -0.0224 0.0042  117  ASN   B O   
5760 C  CB  . ASN   B 117 ? 0.1242 0.1138 0.1635 -0.0048 -0.0030 -0.0067 117  ASN   B CB  
5761 C  CG  . ASN   B 117 ? 0.1229 0.1185 0.1800 0.0028  -0.0040 -0.0112 117  ASN   B CG  
5762 O  OD1 . ASN   B 117 ? 0.1411 0.1153 0.1856 -0.0137 0.0035  -0.0045 117  ASN   B OD1 
5763 N  ND2 . ASN   B 117 ? 0.1212 0.1204 0.1712 0.0012  -0.0008 -0.0040 117  ASN   B ND2 
5770 N  N   . GLN   B 118 ? 0.1279 0.1066 0.1561 -0.0075 -0.0144 -0.0007 118  GLN   B N   
5771 C  CA  . GLN   B 118 ? 0.1344 0.1122 0.1667 -0.0000 -0.0042 -0.0002 118  GLN   B CA  
5772 C  C   . GLN   B 118 ? 0.1355 0.1108 0.1705 0.0036  -0.0030 0.0004  118  GLN   B C   
5773 O  O   . GLN   B 118 ? 0.1535 0.1100 0.2002 -0.0069 0.0053  0.0010  118  GLN   B O   
5774 C  CB  . GLN   B 118 ? 0.1434 0.1199 0.1830 0.0036  -0.0091 -0.0041 118  GLN   B CB  
5775 C  CG  . GLN   B 118 ? 0.1461 0.1137 0.1788 0.0072  -0.0054 -0.0075 118  GLN   B CG  
5776 C  CD  . GLN   B 118 ? 0.1538 0.1122 0.1741 0.0016  0.0014  -0.0130 118  GLN   B CD  
5777 O  OE1 . GLN   B 118 ? 0.1575 0.1168 0.1911 0.0029  0.0145  -0.0001 118  GLN   B OE1 
5778 N  NE2 . GLN   B 118 ? 0.1593 0.1130 0.1880 0.0042  -0.0090 0.0029  118  GLN   B NE2 
5787 N  N   . HIS   B 119 ? 0.1322 0.1165 0.1466 -0.0023 -0.0068 0.0065  119  HIS   B N   
5788 C  CA  . HIS   B 119 ? 0.1443 0.1267 0.1436 -0.0014 -0.0141 0.0075  119  HIS   B CA  
5789 C  C   . HIS   B 119 ? 0.1469 0.1262 0.1378 -0.0031 -0.0248 0.0062  119  HIS   B C   
5790 O  O   . HIS   B 119 ? 0.1502 0.1240 0.1603 -0.0239 -0.0175 0.0066  119  HIS   B O   
5791 C  CB  . HIS   B 119 ? 0.1438 0.1391 0.1548 0.0006  -0.0193 -0.0029 119  HIS   B CB  
5792 C  CG  . HIS   B 119 ? 0.1498 0.1604 0.1697 0.0114  -0.0339 -0.0231 119  HIS   B CG  
5793 N  ND1 . HIS   B 119 ? 0.1675 0.1760 0.2043 0.0087  -0.0421 -0.0404 119  HIS   B ND1 
5794 C  CD2 . HIS   B 119 ? 0.1642 0.1775 0.1719 0.0404  -0.0420 -0.0310 119  HIS   B CD2 
5795 C  CE1 . HIS   B 119 ? 0.1880 0.1917 0.2089 0.0222  -0.0482 -0.0495 119  HIS   B CE1 
5796 N  NE2 . HIS   B 119 ? 0.1869 0.2033 0.1835 0.0365  -0.0463 -0.0415 119  HIS   B NE2 
5804 N  N   . GLU   B 120 ? 0.1629 0.1293 0.1408 -0.0118 -0.0301 0.0124  120  GLU   B N   
5805 C  CA  . GLU   B 120 ? 0.1868 0.1451 0.1558 -0.0033 -0.0427 0.0233  120  GLU   B CA  
5806 C  C   . GLU   B 120 ? 0.1669 0.1350 0.1422 -0.0084 -0.0295 0.0246  120  GLU   B C   
5807 O  O   . GLU   B 120 ? 0.1660 0.1438 0.1455 -0.0132 -0.0286 0.0121  120  GLU   B O   
5808 C  CB  . GLU   B 120 ? 0.2484 0.1769 0.2191 0.0158  -0.0703 0.0475  120  GLU   B CB  
5809 C  CG  . GLU   B 120 ? 0.3092 0.2536 0.3236 0.0244  -0.0924 0.0696  120  GLU   B CG  
5810 C  CD  . GLU   B 120 ? 0.3561 0.3154 0.4285 0.0249  -0.0975 0.0828  120  GLU   B CD  
5811 O  OE1 . GLU   B 120 ? 0.3750 0.3382 0.4657 0.0179  -0.0915 0.0949  120  GLU   B OE1 
5812 O  OE2 . GLU   B 120 ? 0.3735 0.3361 0.4805 0.0255  -0.0985 0.0769  120  GLU   B OE2 
5819 N  N   . VAL   B 121 ? 0.1569 0.1304 0.1408 -0.0155 -0.0172 0.0152  121  VAL   B N   
5820 C  CA  . VAL   B 121 ? 0.1525 0.1411 0.1338 -0.0169 -0.0212 0.0104  121  VAL   B CA  
5821 C  C   . VAL   B 121 ? 0.1446 0.1352 0.1277 -0.0238 -0.0137 0.0096  121  VAL   B C   
5822 O  O   . VAL   B 121 ? 0.1537 0.1293 0.1488 -0.0283 -0.0228 0.0026  121  VAL   B O   
5823 C  CB  . VAL   B 121 ? 0.1745 0.1783 0.1387 -0.0032 -0.0255 0.0176  121  VAL   B CB  
5824 C  CG1 . VAL   B 121 ? 0.1775 0.1893 0.1719 -0.0111 -0.0124 0.0157  121  VAL   B CG1 
5825 C  CG2 . VAL   B 121 ? 0.1986 0.1986 0.1426 0.0050  -0.0138 0.0121  121  VAL   B CG2 
5835 N  N   . LEU   B 122 ? 0.1372 0.1249 0.1276 -0.0169 -0.0223 0.0070  122  LEU   B N   
5836 C  CA  . LEU   B 122 ? 0.1322 0.1320 0.1206 -0.0191 -0.0143 0.0019  122  LEU   B CA  
5837 C  C   . LEU   B 122 ? 0.1338 0.1229 0.1217 -0.0256 -0.0126 0.0007  122  LEU   B C   
5838 O  O   . LEU   B 122 ? 0.1449 0.1248 0.1499 -0.0271 -0.0218 -0.0042 122  LEU   B O   
5839 C  CB  . LEU   B 122 ? 0.1563 0.1432 0.1522 -0.0050 -0.0189 0.0077  122  LEU   B CB  
5840 C  CG  . LEU   B 122 ? 0.1432 0.1464 0.1461 -0.0136 -0.0047 0.0037  122  LEU   B CG  
5841 C  CD1 . LEU   B 122 ? 0.1479 0.1672 0.1597 -0.0123 -0.0071 0.0000  122  LEU   B CD1 
5842 C  CD2 . LEU   B 122 ? 0.1414 0.1470 0.1406 -0.0098 0.0001  -0.0067 122  LEU   B CD2 
5854 N  N   . LEU   B 123 ? 0.1372 0.1125 0.1214 -0.0210 -0.0085 0.0039  123  LEU   B N   
5855 C  CA  . LEU   B 123 ? 0.1393 0.1174 0.1208 -0.0214 -0.0136 -0.0053 123  LEU   B CA  
5856 C  C   . LEU   B 123 ? 0.1323 0.1154 0.1172 -0.0229 -0.0106 0.0011  123  LEU   B C   
5857 O  O   . LEU   B 123 ? 0.1412 0.1198 0.1235 -0.0305 -0.0150 0.0030  123  LEU   B O   
5858 C  CB  . LEU   B 123 ? 0.1456 0.1190 0.1282 -0.0216 -0.0095 -0.0063 123  LEU   B CB  
5859 C  CG  . LEU   B 123 ? 0.1396 0.1226 0.1455 -0.0169 -0.0054 0.0100  123  LEU   B CG  
5860 C  CD1 . LEU   B 123 ? 0.1458 0.1293 0.1558 -0.0158 0.0013  -0.0088 123  LEU   B CD1 
5861 C  CD2 . LEU   B 123 ? 0.1450 0.1276 0.1601 -0.0116 0.0032  0.0151  123  LEU   B CD2 
5873 N  N   . ALA   B 124 ? 0.1282 0.1116 0.1214 -0.0225 -0.0042 -0.0051 124  ALA   B N   
5874 C  CA  . ALA   B 124 ? 0.1251 0.1132 0.1313 -0.0160 -0.0036 -0.0091 124  ALA   B CA  
5875 C  C   . ALA   B 124 ? 0.1239 0.1092 0.1299 -0.0135 -0.0071 -0.0013 124  ALA   B C   
5876 O  O   . ALA   B 124 ? 0.1339 0.1151 0.1380 -0.0110 -0.0081 -0.0008 124  ALA   B O   
5877 C  CB  . ALA   B 124 ? 0.1316 0.1192 0.1399 -0.0063 0.0057  -0.0000 124  ALA   B CB  
5883 N  N   . PRO   B 125 ? 0.1282 0.1152 0.1267 -0.0149 -0.0097 0.0078  125  PRO   B N   
5884 C  CA  . PRO   B 125 ? 0.1375 0.1168 0.1469 -0.0162 -0.0086 0.0156  125  PRO   B CA  
5885 C  C   . PRO   B 125 ? 0.1352 0.1110 0.1522 -0.0144 -0.0093 0.0042  125  PRO   B C   
5886 O  O   . PRO   B 125 ? 0.1391 0.1085 0.1701 -0.0086 -0.0011 0.0130  125  PRO   B O   
5887 C  CB  . PRO   B 125 ? 0.1427 0.1438 0.1542 -0.0207 -0.0200 0.0309  125  PRO   B CB  
5888 C  CG  . PRO   B 125 ? 0.1474 0.1471 0.1409 -0.0263 -0.0213 0.0164  125  PRO   B CG  
5889 C  CD  . PRO   B 125 ? 0.1425 0.1263 0.1293 -0.0268 -0.0097 0.0067  125  PRO   B CD  
5897 N  N   . LEU   B 126 ? 0.1385 0.1062 0.1679 -0.0137 0.0099  0.0055  126  LEU   B N   
5898 C  CA  . LEU   B 126 ? 0.1440 0.1154 0.1822 -0.0099 0.0181  0.0078  126  LEU   B CA  
5899 C  C   . LEU   B 126 ? 0.1415 0.1239 0.1840 0.0009  0.0239  0.0112  126  LEU   B C   
5900 O  O   . LEU   B 126 ? 0.1620 0.1495 0.1955 0.0146  0.0029  -0.0069 126  LEU   B O   
5901 C  CB  . LEU   B 126 ? 0.1545 0.1211 0.2117 -0.0121 0.0254  0.0049  126  LEU   B CB  
5902 C  CG  . LEU   B 126 ? 0.1676 0.1297 0.2104 -0.0187 0.0286  -0.0069 126  LEU   B CG  
5903 C  CD1 . LEU   B 126 ? 0.1844 0.1377 0.2482 -0.0212 0.0227  -0.0128 126  LEU   B CD1 
5904 C  CD2 . LEU   B 126 ? 0.1736 0.1396 0.2124 -0.0282 0.0165  -0.0006 126  LEU   B CD2 
5916 N  N   . LEU   B 127 ? 0.1376 0.1117 0.1850 0.0014  0.0239  0.0090  127  LEU   B N   
5917 C  CA  . LEU   B 127 ? 0.1387 0.1223 0.1892 -0.0058 0.0202  0.0156  127  LEU   B CA  
5918 C  C   . LEU   B 127 ? 0.1355 0.1186 0.1843 -0.0034 0.0223  0.0120  127  LEU   B C   
5919 O  O   . LEU   B 127 ? 0.1386 0.1247 0.1852 -0.0109 0.0145  0.0127  127  LEU   B O   
5920 C  CB  . LEU   B 127 ? 0.1509 0.1242 0.1932 0.0029  0.0168  0.0265  127  LEU   B CB  
5921 C  CG  . LEU   B 127 ? 0.1658 0.1270 0.2009 0.0059  0.0183  0.0194  127  LEU   B CG  
5922 C  CD1 . LEU   B 127 ? 0.1705 0.1222 0.2000 0.0084  0.0163  0.0093  127  LEU   B CD1 
5923 C  CD2 . LEU   B 127 ? 0.1634 0.1370 0.2188 -0.0080 0.0244  0.0286  127  LEU   B CD2 
5935 N  N   . SER   B 128 ? 0.1414 0.1192 0.1847 0.0012  0.0070  0.0122  128  SER   B N   
5936 C  CA  . SER   B 128 ? 0.1517 0.1275 0.1882 0.0059  -0.0020 0.0218  128  SER   B CA  
5937 C  C   . SER   B 128 ? 0.1636 0.1334 0.1928 0.0093  -0.0196 0.0226  128  SER   B C   
5938 O  O   . SER   B 128 ? 0.1794 0.1372 0.2238 0.0059  -0.0095 0.0308  128  SER   B O   
5939 C  CB  . SER   B 128 ? 0.1596 0.1299 0.1849 0.0042  0.0048  0.0296  128  SER   B CB  
5940 O  OG  . SER   B 128 ? 0.1657 0.1445 0.1895 0.0066  0.0135  0.0295  128  SER   B OG  
5946 N  N   . ALA   B 129 ? 0.1749 0.1387 0.2147 0.0249  -0.0142 0.0080  129  ALA   B N   
5947 C  CA  . ALA   B 129 ? 0.1868 0.1465 0.2301 0.0272  -0.0143 0.0003  129  ALA   B CA  
5948 C  C   . ALA   B 129 ? 0.1773 0.1394 0.2114 0.0199  0.0074  0.0030  129  ALA   B C   
5949 O  O   . ALA   B 129 ? 0.1616 0.1441 0.2126 0.0148  0.0018  0.0150  129  ALA   B O   
5950 C  CB  . ALA   B 129 ? 0.2032 0.1700 0.2584 0.0308  -0.0045 -0.0087 129  ALA   B CB  
5956 N  N   . GLY   B 130 ? 0.1793 0.1345 0.2135 0.0263  0.0172  -0.0017 130  GLY   B N   
5957 C  CA  . GLY   B 130 ? 0.1863 0.1495 0.2228 0.0285  0.0293  -0.0017 130  GLY   B CA  
5958 C  C   . GLY   B 130 ? 0.1848 0.1474 0.2231 0.0214  0.0178  0.0092  130  GLY   B C   
5959 O  O   . GLY   B 130 ? 0.2042 0.1554 0.2298 0.0180  0.0129  0.0173  130  GLY   B O   
5963 N  N   . ILE   B 131 ? 0.1702 0.1591 0.2265 0.0352  0.0159  0.0077  131  ILE   B N   
5964 C  CA  . ILE   B 131 ? 0.1888 0.1762 0.2294 0.0286  0.0084  0.0178  131  ILE   B CA  
5965 C  C   . ILE   B 131 ? 0.2007 0.1675 0.2076 0.0192  0.0034  0.0286  131  ILE   B C   
5966 O  O   . ILE   B 131 ? 0.2251 0.1821 0.2150 0.0219  -0.0151 0.0245  131  ILE   B O   
5967 C  CB  . ILE   B 131 ? 0.1900 0.2125 0.2593 0.0296  0.0020  0.0221  131  ILE   B CB  
5968 C  CG1 . ILE   B 131 ? 0.1931 0.2329 0.2679 0.0124  0.0113  0.0256  131  ILE   B CG1 
5969 C  CG2 . ILE   B 131 ? 0.1900 0.2289 0.2833 0.0277  0.0076  0.0149  131  ILE   B CG2 
5970 C  CD1 . ILE   B 131 ? 0.2041 0.2486 0.2772 -0.0026 -0.0017 0.0311  131  ILE   B CD1 
5982 N  N   . PHE   B 132 ? 0.1866 0.1485 0.1965 0.0168  0.0223  0.0287  132  PHE   B N   
5983 C  CA  . PHE   B 132 ? 0.1967 0.1501 0.1936 0.0100  0.0382  0.0170  132  PHE   B CA  
5984 C  C   . PHE   B 132 ? 0.2192 0.1635 0.2108 0.0100  0.0460  0.0182  132  PHE   B C   
5985 O  O   . PHE   B 132 ? 0.2386 0.1847 0.2330 0.0095  0.0612  0.0183  132  PHE   B O   
5986 C  CB  . PHE   B 132 ? 0.1838 0.1493 0.1768 0.0171  0.0318  0.0235  132  PHE   B CB  
5987 C  CG  . PHE   B 132 ? 0.1790 0.1521 0.1741 0.0226  0.0334  0.0191  132  PHE   B CG  
5988 C  CD1 . PHE   B 132 ? 0.1879 0.1509 0.2061 0.0165  0.0401  0.0141  132  PHE   B CD1 
5989 C  CD2 . PHE   B 132 ? 0.1797 0.1554 0.1579 0.0262  0.0238  0.0303  132  PHE   B CD2 
5990 C  CE1 . PHE   B 132 ? 0.1912 0.1552 0.2208 0.0149  0.0279  0.0174  132  PHE   B CE1 
5991 C  CE2 . PHE   B 132 ? 0.1871 0.1597 0.1586 0.0228  0.0205  0.0223  132  PHE   B CE2 
5992 C  CZ  . PHE   B 132 ? 0.1938 0.1563 0.1966 0.0143  0.0085  0.0306  132  PHE   B CZ  
6002 N  N   . GLY   B 133 ? 0.2157 0.1539 0.2109 0.0088  0.0320  0.0298  133  GLY   B N   
6003 C  CA  . GLY   B 133 ? 0.2238 0.1593 0.2198 -0.0100 0.0273  0.0390  133  GLY   B CA  
6004 C  C   . GLY   B 133 ? 0.2272 0.1708 0.2182 -0.0223 0.0357  0.0373  133  GLY   B C   
6005 O  O   . GLY   B 133 ? 0.2440 0.1861 0.2636 -0.0384 0.0360  0.0527  133  GLY   B O   
6009 N  N   . ALA   B 134 ? 0.2119 0.1687 0.2061 -0.0237 0.0346  0.0193  134  ALA   B N   
6010 C  CA  . ALA   B 134 ? 0.2063 0.1673 0.2220 -0.0186 0.0401  0.0098  134  ALA   B CA  
6011 C  C   . ALA   B 134 ? 0.2108 0.1587 0.2222 -0.0098 0.0363  0.0187  134  ALA   B C   
6012 O  O   . ALA   B 134 ? 0.2152 0.1766 0.2361 0.0055  0.0282  0.0131  134  ALA   B O   
6013 C  CB  . ALA   B 134 ? 0.2089 0.1651 0.2511 -0.0089 0.0308  0.0012  134  ALA   B CB  
6019 N  N   . ASP   B 135 ? 0.2265 0.1517 0.2141 -0.0151 0.0214  0.0229  135  ASP   B N   
6020 C  CA  . ASP   B 135 ? 0.2444 0.1430 0.2347 -0.0126 0.0071  0.0313  135  ASP   B CA  
6021 C  C   . ASP   B 135 ? 0.2239 0.1348 0.2249 -0.0048 0.0126  0.0255  135  ASP   B C   
6022 O  O   . ASP   B 135 ? 0.2201 0.1324 0.2344 -0.0024 0.0176  0.0309  135  ASP   B O   
6023 C  CB  . ASP   B 135 ? 0.2711 0.1535 0.2593 -0.0335 0.0013  0.0315  135  ASP   B CB  
6024 C  CG  . ASP   B 135 ? 0.2966 0.1619 0.3023 -0.0482 -0.0016 0.0267  135  ASP   B CG  
6025 O  OD1 . ASP   B 135 ? 0.3042 0.1530 0.3045 -0.0340 -0.0069 0.0252  135  ASP   B OD1 
6026 O  OD2 . ASP   B 135 ? 0.3159 0.1997 0.3504 -0.0610 -0.0025 0.0094  135  ASP   B OD2 
6031 N  N   . PRO   B 136 ? 0.2122 0.1406 0.2336 0.0163  -0.0013 0.0217  136  PRO   B N   
6032 C  CA  . PRO   B 136 ? 0.1915 0.1346 0.2343 0.0117  -0.0014 0.0111  136  PRO   B CA  
6033 C  C   . PRO   B 136 ? 0.1750 0.1238 0.2365 0.0137  -0.0004 0.0062  136  PRO   B C   
6034 O  O   . PRO   B 136 ? 0.1581 0.1208 0.2318 0.0108  0.0035  0.0097  136  PRO   B O   
6035 C  CB  . PRO   B 136 ? 0.1948 0.1584 0.2440 0.0268  -0.0073 0.0033  136  PRO   B CB  
6036 C  CG  . PRO   B 136 ? 0.2133 0.1603 0.2620 0.0272  -0.0054 0.0030  136  PRO   B CG  
6037 C  CD  . PRO   B 136 ? 0.2166 0.1511 0.2520 0.0333  -0.0009 0.0121  136  PRO   B CD  
6045 N  N   . ILE   B 137 ? 0.1861 0.1154 0.2477 0.0132  -0.0089 0.0065  137  ILE   B N   
6046 C  CA  . ILE   B 137 ? 0.1942 0.1133 0.2706 -0.0056 0.0049  0.0044  137  ILE   B CA  
6047 C  C   . ILE   B 137 ? 0.1855 0.1233 0.2581 -0.0089 0.0095  0.0133  137  ILE   B C   
6048 O  O   . ILE   B 137 ? 0.1708 0.1268 0.2540 -0.0109 0.0105  0.0089  137  ILE   B O   
6049 C  CB  . ILE   B 137 ? 0.2197 0.1262 0.3136 -0.0010 0.0034  -0.0014 137  ILE   B CB  
6050 C  CG1 . ILE   B 137 ? 0.2488 0.1418 0.3642 0.0070  0.0084  -0.0116 137  ILE   B CG1 
6051 C  CG2 . ILE   B 137 ? 0.2223 0.1275 0.3221 -0.0168 0.0017  0.0036  137  ILE   B CG2 
6052 C  CD1 . ILE   B 137 ? 0.2698 0.1674 0.3972 0.0205  0.0049  -0.0079 137  ILE   B CD1 
6064 N  N   A HIS   B 138 ? 0.1899 0.1197 0.2573 -0.0077 0.0233  0.0172  138  HIS   B N   
6065 N  N   B HIS   B 138 ? 0.1870 0.1256 0.2491 -0.0073 0.0123  0.0100  138  HIS   B N   
6066 C  CA  A HIS   B 138 ? 0.1951 0.1275 0.2570 -0.0047 0.0417  0.0190  138  HIS   B CA  
6067 C  CA  B HIS   B 138 ? 0.1896 0.1359 0.2394 -0.0056 0.0161  0.0054  138  HIS   B CA  
6068 C  C   A HIS   B 138 ? 0.1806 0.1249 0.2349 -0.0014 0.0405  0.0274  138  HIS   B C   
6069 C  C   B HIS   B 138 ? 0.1797 0.1286 0.2291 -0.0022 0.0262  0.0154  138  HIS   B C   
6070 O  O   A HIS   B 138 ? 0.1745 0.1316 0.2538 0.0040  0.0419  0.0369  138  HIS   B O   
6071 O  O   B HIS   B 138 ? 0.1764 0.1343 0.2412 0.0010  0.0286  0.0199  138  HIS   B O   
6072 C  CB  A HIS   B 138 ? 0.2156 0.1369 0.2750 -0.0053 0.0634  0.0176  138  HIS   B CB  
6073 C  CB  B HIS   B 138 ? 0.2024 0.1536 0.2399 -0.0092 0.0096  -0.0073 138  HIS   B CB  
6074 C  CG  A HIS   B 138 ? 0.2291 0.1509 0.2816 -0.0073 0.0823  0.0382  138  HIS   B CG  
6075 C  CG  B HIS   B 138 ? 0.2065 0.1690 0.2321 -0.0166 0.0016  -0.0069 138  HIS   B CG  
6076 N  ND1 A HIS   B 138 ? 0.2343 0.1672 0.2970 -0.0055 0.0929  0.0388  138  HIS   B ND1 
6077 N  ND1 B HIS   B 138 ? 0.2085 0.1813 0.2344 -0.0172 0.0009  -0.0106 138  HIS   B ND1 
6078 C  CD2 A HIS   B 138 ? 0.2372 0.1590 0.2777 -0.0038 0.0888  0.0356  138  HIS   B CD2 
6079 C  CD2 B HIS   B 138 ? 0.2092 0.1748 0.2273 -0.0178 -0.0011 -0.0135 138  HIS   B CD2 
6080 C  CE1 A HIS   B 138 ? 0.2355 0.1679 0.2929 -0.0035 0.0961  0.0401  138  HIS   B CE1 
6081 C  CE1 B HIS   B 138 ? 0.2104 0.1812 0.2317 -0.0146 0.0009  -0.0108 138  HIS   B CE1 
6082 N  NE2 A HIS   B 138 ? 0.2396 0.1604 0.2826 -0.0014 0.0967  0.0365  138  HIS   B NE2 
6083 N  NE2 B HIS   B 138 ? 0.2104 0.1750 0.2281 -0.0162 -0.0015 -0.0163 138  HIS   B NE2 
6098 N  N   . SER   B 139 ? 0.1745 0.1143 0.2284 0.0008  0.0286  0.0124  139  SER   B N   
6099 C  CA  . SER   B 139 ? 0.1677 0.1172 0.2194 0.0017  0.0270  -0.0028 139  SER   B CA  
6100 C  C   . SER   B 139 ? 0.1484 0.1069 0.2214 -0.0005 0.0179  0.0013  139  SER   B C   
6101 O  O   . SER   B 139 ? 0.1490 0.1090 0.2146 0.0017  0.0102  0.0118  139  SER   B O   
6102 C  CB  . SER   B 139 ? 0.1733 0.1168 0.2191 0.0019  0.0122  0.0041  139  SER   B CB  
6103 O  OG  . SER   B 139 ? 0.1753 0.1178 0.2133 -0.0014 -0.0029 0.0113  139  SER   B OG  
6110 N  N   . LEU   B 140 ? 0.1431 0.1030 0.2270 -0.0067 0.0193  -0.0038 140  LEU   B N   
6111 C  CA  . LEU   B 140 ? 0.1414 0.1086 0.2232 -0.0033 0.0125  0.0029  140  LEU   B CA  
6112 C  C   . LEU   B 140 ? 0.1376 0.1108 0.2350 -0.0038 0.0076  -0.0018 140  LEU   B C   
6113 O  O   . LEU   B 140 ? 0.1387 0.1144 0.2337 -0.0018 0.0035  0.0017  140  LEU   B O   
6114 C  CB  . LEU   B 140 ? 0.1409 0.1110 0.2267 -0.0085 0.0175  -0.0013 140  LEU   B CB  
6115 C  CG  . LEU   B 140 ? 0.1501 0.1121 0.2203 -0.0087 0.0066  0.0051  140  LEU   B CG  
6116 C  CD1 . LEU   B 140 ? 0.1565 0.1247 0.2287 -0.0090 0.0091  -0.0049 140  LEU   B CD1 
6117 C  CD2 . LEU   B 140 ? 0.1669 0.1230 0.2265 -0.0095 0.0017  -0.0083 140  LEU   B CD2 
6129 N  N   . ARG   B 141 ? 0.1324 0.1137 0.2401 -0.0091 0.0100  -0.0019 141  ARG   B N   
6130 C  CA  . ARG   B 141 ? 0.1373 0.1128 0.2755 -0.0118 0.0265  -0.0059 141  ARG   B CA  
6131 C  C   . ARG   B 141 ? 0.1308 0.1122 0.2594 -0.0132 0.0137  0.0022  141  ARG   B C   
6132 O  O   . ARG   B 141 ? 0.1398 0.1148 0.2532 -0.0172 0.0065  -0.0113 141  ARG   B O   
6133 C  CB  . ARG   B 141 ? 0.1554 0.1255 0.3103 -0.0180 0.0360  0.0019  141  ARG   B CB  
6134 C  CG  . ARG   B 141 ? 0.1874 0.1531 0.3300 -0.0198 0.0370  0.0012  141  ARG   B CG  
6135 C  CD  . ARG   B 141 ? 0.2302 0.1772 0.3412 -0.0103 0.0213  -0.0109 141  ARG   B CD  
6136 N  NE  . ARG   B 141 ? 0.2490 0.1752 0.3401 -0.0268 0.0281  -0.0137 141  ARG   B NE  
6137 C  CZ  . ARG   B 141 ? 0.2578 0.1572 0.3278 -0.0244 0.0384  -0.0240 141  ARG   B CZ  
6138 N  NH1 . ARG   B 141 ? 0.2697 0.1525 0.3173 -0.0197 0.0329  -0.0357 141  ARG   B NH1 
6139 N  NH2 . ARG   B 141 ? 0.2691 0.1701 0.3423 -0.0090 0.0226  -0.0106 141  ARG   B NH2 
6153 N  N   . VAL   B 142 ? 0.1331 0.1086 0.2418 -0.0065 0.0174  -0.0022 142  VAL   B N   
6154 C  CA  . VAL   B 142 ? 0.1265 0.1146 0.2299 -0.0067 0.0206  -0.0008 142  VAL   B CA  
6155 C  C   . VAL   B 142 ? 0.1311 0.1126 0.2259 -0.0032 0.0131  -0.0115 142  VAL   B C   
6156 O  O   . VAL   B 142 ? 0.1386 0.1078 0.2389 -0.0017 0.0159  -0.0008 142  VAL   B O   
6157 C  CB  . VAL   B 142 ? 0.1412 0.1269 0.2391 -0.0001 0.0249  0.0093  142  VAL   B CB  
6158 C  CG1 . VAL   B 142 ? 0.1380 0.1227 0.2410 0.0071  0.0254  0.0086  142  VAL   B CG1 
6159 C  CG2 . VAL   B 142 ? 0.1656 0.1305 0.2533 -0.0007 0.0207  0.0151  142  VAL   B CG2 
6169 N  N   . CYS   B 143 ? 0.1268 0.1135 0.2117 0.0010  0.0126  0.0078  143  CYS   B N   
6170 C  CA  . CYS   B 143 ? 0.1236 0.1158 0.2141 -0.0067 0.0050  0.0064  143  CYS   B CA  
6171 C  C   . CYS   B 143 ? 0.1218 0.1177 0.2177 -0.0058 0.0129  -0.0034 143  CYS   B C   
6172 O  O   . CYS   B 143 ? 0.1232 0.1197 0.2237 -0.0079 0.0014  -0.0037 143  CYS   B O   
6173 C  CB  . CYS   B 143 ? 0.1287 0.1209 0.2213 -0.0093 0.0045  -0.0010 143  CYS   B CB  
6174 S  SG  . CYS   B 143 ? 0.1318 0.1363 0.2066 -0.0041 0.0092  0.0019  143  CYS   B SG  
6180 N  N   . VAL   B 144 ? 0.1293 0.1152 0.2336 -0.0047 0.0065  -0.0170 144  VAL   B N   
6181 C  CA  . VAL   B 144 ? 0.1323 0.1215 0.2577 -0.0119 -0.0056 -0.0226 144  VAL   B CA  
6182 C  C   . VAL   B 144 ? 0.1280 0.1282 0.2616 -0.0121 -0.0063 -0.0089 144  VAL   B C   
6183 O  O   . VAL   B 144 ? 0.1374 0.1451 0.2812 0.0028  0.0024  0.0126  144  VAL   B O   
6184 C  CB  . VAL   B 144 ? 0.1560 0.1376 0.3220 -0.0176 -0.0188 -0.0342 144  VAL   B CB  
6185 C  CG1 . VAL   B 144 ? 0.1802 0.1821 0.3545 -0.0104 -0.0260 -0.0213 144  VAL   B CG1 
6186 C  CG2 . VAL   B 144 ? 0.1653 0.1405 0.3129 -0.0009 -0.0330 -0.0446 144  VAL   B CG2 
6196 N  N   . ASP   B 145 ? 0.1301 0.1205 0.2695 -0.0096 0.0008  -0.0182 145  ASP   B N   
6197 C  CA  . ASP   B 145 ? 0.1311 0.1279 0.2885 -0.0098 0.0114  -0.0166 145  ASP   B CA  
6198 C  C   . ASP   B 145 ? 0.1249 0.1294 0.2714 -0.0081 0.0181  -0.0113 145  ASP   B C   
6199 O  O   . ASP   B 145 ? 0.1290 0.1424 0.3203 -0.0169 0.0185  -0.0267 145  ASP   B O   
6200 C  CB  . ASP   B 145 ? 0.1433 0.1302 0.3290 -0.0154 0.0248  -0.0081 145  ASP   B CB  
6201 C  CG  . ASP   B 145 ? 0.1612 0.1347 0.3783 -0.0276 0.0369  -0.0016 145  ASP   B CG  
6202 O  OD1 . ASP   B 145 ? 0.1682 0.1367 0.3909 -0.0223 0.0033  -0.0120 145  ASP   B OD1 
6203 O  OD2 . ASP   B 145 ? 0.1960 0.1464 0.4246 -0.0280 0.0550  -0.0008 145  ASP   B OD2 
6208 N  N   . THR   B 146 ? 0.1208 0.1179 0.2266 -0.0099 0.0093  -0.0053 146  THR   B N   
6209 C  CA  . THR   B 146 ? 0.1289 0.1148 0.2120 -0.0041 0.0119  -0.0038 146  THR   B CA  
6210 C  C   . THR   B 146 ? 0.1258 0.1168 0.2068 -0.0025 0.0049  -0.0023 146  THR   B C   
6211 O  O   . THR   B 146 ? 0.1327 0.1179 0.2143 -0.0038 0.0022  -0.0011 146  THR   B O   
6212 C  CB  . THR   B 146 ? 0.1308 0.1161 0.2211 0.0004  0.0232  0.0039  146  THR   B CB  
6213 O  OG1 . THR   B 146 ? 0.1345 0.1147 0.2237 -0.0044 0.0197  0.0123  146  THR   B OG1 
6214 C  CG2 . THR   B 146 ? 0.1405 0.1218 0.2208 -0.0032 0.0215  0.0013  146  THR   B CG2 
6222 N  N   . VAL   B 147 ? 0.1299 0.1250 0.1945 -0.0054 0.0101  -0.0001 147  VAL   B N   
6223 C  CA  . VAL   B 147 ? 0.1281 0.1184 0.1860 -0.0107 -0.0009 -0.0059 147  VAL   B CA  
6224 C  C   . VAL   B 147 ? 0.1216 0.1199 0.1978 -0.0137 -0.0060 -0.0085 147  VAL   B C   
6225 O  O   . VAL   B 147 ? 0.1384 0.1277 0.2079 -0.0217 -0.0197 -0.0168 147  VAL   B O   
6226 C  CB  . VAL   B 147 ? 0.1323 0.1280 0.1753 -0.0067 -0.0022 0.0027  147  VAL   B CB  
6227 C  CG1 . VAL   B 147 ? 0.1324 0.1419 0.1716 -0.0130 -0.0043 0.0052  147  VAL   B CG1 
6228 C  CG2 . VAL   B 147 ? 0.1424 0.1299 0.1783 -0.0106 0.0014  0.0034  147  VAL   B CG2 
6238 N  N   . ARG   B 148 ? 0.1292 0.1153 0.1901 -0.0063 -0.0128 -0.0108 148  ARG   B N   
6239 C  CA  . ARG   B 148 ? 0.1304 0.1262 0.1906 -0.0068 -0.0229 -0.0169 148  ARG   B CA  
6240 C  C   . ARG   B 148 ? 0.1385 0.1371 0.1767 -0.0099 -0.0213 -0.0074 148  ARG   B C   
6241 O  O   . ARG   B 148 ? 0.1564 0.1605 0.1855 -0.0246 -0.0311 -0.0024 148  ARG   B O   
6242 C  CB  . ARG   B 148 ? 0.1348 0.1342 0.2067 -0.0079 -0.0279 -0.0224 148  ARG   B CB  
6243 C  CG  . ARG   B 148 ? 0.1370 0.1537 0.2159 -0.0107 -0.0222 -0.0362 148  ARG   B CG  
6244 C  CD  . ARG   B 148 ? 0.1474 0.1671 0.2170 0.0036  -0.0252 -0.0353 148  ARG   B CD  
6245 N  NE  . ARG   B 148 ? 0.1498 0.1600 0.2086 0.0196  -0.0230 -0.0310 148  ARG   B NE  
6246 C  CZ  . ARG   B 148 ? 0.1393 0.1507 0.1879 0.0134  -0.0178 -0.0201 148  ARG   B CZ  
6247 N  NH1 . ARG   B 148 ? 0.1389 0.1553 0.1902 -0.0035 -0.0019 -0.0172 148  ARG   B NH1 
6248 N  NH2 . ARG   B 148 ? 0.1615 0.1397 0.1849 0.0141  -0.0159 -0.0124 148  ARG   B NH2 
6262 N  N   . THR   B 149 ? 0.1384 0.1316 0.1753 -0.0122 -0.0232 -0.0015 149  THR   B N   
6263 C  CA  . THR   B 149 ? 0.1446 0.1301 0.1697 -0.0137 -0.0227 0.0024  149  THR   B CA  
6264 C  C   . THR   B 149 ? 0.1426 0.1293 0.1591 -0.0159 -0.0254 0.0042  149  THR   B C   
6265 O  O   . THR   B 149 ? 0.1530 0.1308 0.1740 -0.0189 -0.0133 0.0002  149  THR   B O   
6266 C  CB  . THR   B 149 ? 0.1465 0.1289 0.1762 -0.0152 -0.0183 -0.0023 149  THR   B CB  
6267 O  OG1 . THR   B 149 ? 0.1496 0.1351 0.1652 -0.0210 -0.0221 -0.0029 149  THR   B OG1 
6268 C  CG2 . THR   B 149 ? 0.1515 0.1284 0.1945 -0.0010 -0.0179 -0.0034 149  THR   B CG2 
6276 N  N   . ASN   B 150 ? 0.1495 0.1299 0.1603 -0.0150 -0.0292 -0.0008 150  ASN   B N   
6277 C  CA  . ASN   B 150 ? 0.1523 0.1392 0.1616 -0.0192 -0.0257 -0.0112 150  ASN   B CA  
6278 C  C   . ASN   B 150 ? 0.1418 0.1327 0.1633 -0.0124 -0.0245 -0.0062 150  ASN   B C   
6279 O  O   . ASN   B 150 ? 0.1519 0.1332 0.1855 -0.0224 -0.0398 -0.0089 150  ASN   B O   
6280 C  CB  . ASN   B 150 ? 0.1748 0.1727 0.1662 -0.0185 -0.0352 0.0057  150  ASN   B CB  
6281 C  CG  . ASN   B 150 ? 0.2018 0.2145 0.2008 -0.0210 -0.0334 0.0244  150  ASN   B CG  
6282 O  OD1 . ASN   B 150 ? 0.2113 0.2343 0.2150 -0.0327 -0.0472 0.0243  150  ASN   B OD1 
6283 N  ND2 . ASN   B 150 ? 0.2129 0.2329 0.2430 -0.0086 -0.0416 0.0539  150  ASN   B ND2 
6290 N  N   . VAL   B 151 ? 0.1371 0.1331 0.1619 -0.0159 -0.0238 -0.0003 151  VAL   B N   
6291 C  CA  . VAL   B 151 ? 0.1391 0.1336 0.1556 -0.0240 -0.0201 -0.0036 151  VAL   B CA  
6292 C  C   . VAL   B 151 ? 0.1434 0.1273 0.1507 -0.0268 -0.0204 -0.0073 151  VAL   B C   
6293 O  O   . VAL   B 151 ? 0.1495 0.1332 0.1769 -0.0257 -0.0163 -0.0110 151  VAL   B O   
6294 C  CB  . VAL   B 151 ? 0.1592 0.1448 0.1684 -0.0088 -0.0133 -0.0111 151  VAL   B CB  
6295 C  CG1 . VAL   B 151 ? 0.1704 0.1454 0.1898 -0.0161 -0.0002 -0.0144 151  VAL   B CG1 
6296 C  CG2 . VAL   B 151 ? 0.1721 0.1567 0.1715 -0.0001 -0.0156 0.0021  151  VAL   B CG2 
6306 N  N   . TYR   B 152 ? 0.1353 0.1217 0.1478 -0.0217 -0.0179 -0.0037 152  TYR   B N   
6307 C  CA  . TYR   B 152 ? 0.1392 0.1365 0.1508 -0.0268 -0.0160 -0.0079 152  TYR   B CA  
6308 C  C   . TYR   B 152 ? 0.1338 0.1259 0.1359 -0.0198 -0.0099 -0.0100 152  TYR   B C   
6309 O  O   . TYR   B 152 ? 0.1420 0.1279 0.1418 -0.0242 -0.0072 -0.0030 152  TYR   B O   
6310 C  CB  . TYR   B 152 ? 0.1526 0.1460 0.1551 -0.0304 -0.0159 -0.0022 152  TYR   B CB  
6311 C  CG  . TYR   B 152 ? 0.1649 0.1545 0.1448 -0.0398 -0.0128 -0.0005 152  TYR   B CG  
6312 C  CD1 . TYR   B 152 ? 0.1783 0.1668 0.1407 -0.0241 -0.0251 0.0005  152  TYR   B CD1 
6313 C  CD2 . TYR   B 152 ? 0.1848 0.1734 0.1399 -0.0353 -0.0077 -0.0033 152  TYR   B CD2 
6314 C  CE1 . TYR   B 152 ? 0.1964 0.1835 0.1515 -0.0257 -0.0307 0.0154  152  TYR   B CE1 
6315 C  CE2 . TYR   B 152 ? 0.2021 0.1974 0.1472 -0.0346 -0.0162 -0.0108 152  TYR   B CE2 
6316 C  CZ  . TYR   B 152 ? 0.2073 0.2086 0.1440 -0.0310 -0.0403 0.0099  152  TYR   B CZ  
6317 O  OH  . TYR   B 152 ? 0.2311 0.2423 0.1714 -0.0207 -0.0418 0.0103  152  TYR   B OH  
6327 N  N   . LEU   B 153 ? 0.1358 0.1188 0.1465 -0.0249 -0.0108 -0.0094 153  LEU   B N   
6328 C  CA  . LEU   B 153 ? 0.1417 0.1137 0.1337 -0.0208 -0.0044 -0.0123 153  LEU   B CA  
6329 C  C   . LEU   B 153 ? 0.1430 0.1140 0.1449 -0.0187 -0.0050 -0.0167 153  LEU   B C   
6330 O  O   . LEU   B 153 ? 0.1517 0.1374 0.1658 -0.0105 -0.0080 -0.0314 153  LEU   B O   
6331 C  CB  . LEU   B 153 ? 0.1449 0.1147 0.1560 -0.0222 0.0022  -0.0103 153  LEU   B CB  
6332 C  CG  . LEU   B 153 ? 0.1392 0.1281 0.1836 -0.0200 -0.0005 -0.0033 153  LEU   B CG  
6333 C  CD1 . LEU   B 153 ? 0.1484 0.1377 0.1782 -0.0244 0.0047  0.0040  153  LEU   B CD1 
6334 C  CD2 . LEU   B 153 ? 0.1420 0.1368 0.1778 -0.0255 0.0109  -0.0032 153  LEU   B CD2 
6346 N  N   . ALA   B 154 ? 0.1409 0.1184 0.1515 -0.0038 -0.0140 -0.0104 154  ALA   B N   
6347 C  CA  . ALA   B 154 ? 0.1502 0.1310 0.1707 -0.0001 -0.0157 -0.0246 154  ALA   B CA  
6348 C  C   . ALA   B 154 ? 0.1639 0.1315 0.1755 0.0032  -0.0246 -0.0247 154  ALA   B C   
6349 O  O   . ALA   B 154 ? 0.1918 0.1325 0.1982 0.0083  -0.0089 -0.0104 154  ALA   B O   
6350 C  CB  . ALA   B 154 ? 0.1496 0.1466 0.1993 -0.0021 -0.0114 -0.0335 154  ALA   B CB  
6356 N  N   . VAL   B 155 ? 0.1318 0.1198 0.1899 0.0022  -0.0088 -0.0164 155  VAL   B N   
6357 C  CA  . VAL   B 155 ? 0.1286 0.1209 0.1999 -0.0012 -0.0124 -0.0058 155  VAL   B CA  
6358 C  C   . VAL   B 155 ? 0.1295 0.1197 0.1994 -0.0011 -0.0086 -0.0189 155  VAL   B C   
6359 O  O   . VAL   B 155 ? 0.1439 0.1427 0.2323 0.0053  -0.0091 -0.0384 155  VAL   B O   
6360 C  CB  . VAL   B 155 ? 0.1325 0.1373 0.2345 -0.0048 -0.0123 0.0045  155  VAL   B CB  
6361 C  CG1 . VAL   B 155 ? 0.1348 0.1319 0.2325 -0.0122 -0.0172 -0.0020 155  VAL   B CG1 
6362 C  CG2 . VAL   B 155 ? 0.1274 0.1489 0.2681 -0.0087 -0.0115 0.0227  155  VAL   B CG2 
6372 N  N   . PHE   B 156 ? 0.1238 0.1271 0.2180 0.0027  -0.0052 -0.0150 156  PHE   B N   
6373 C  CA  . PHE   B 156 ? 0.1249 0.1378 0.2476 0.0081  -0.0012 -0.0166 156  PHE   B CA  
6374 C  C   . PHE   B 156 ? 0.1218 0.1497 0.2775 0.0136  -0.0124 -0.0386 156  PHE   B C   
6375 O  O   . PHE   B 156 ? 0.1439 0.1742 0.3030 0.0217  0.0007  -0.0436 156  PHE   B O   
6376 C  CB  . PHE   B 156 ? 0.1341 0.1350 0.2462 -0.0015 -0.0140 -0.0124 156  PHE   B CB  
6377 C  CG  . PHE   B 156 ? 0.1329 0.1422 0.2605 -0.0023 -0.0146 0.0056  156  PHE   B CG  
6378 C  CD1 . PHE   B 156 ? 0.1407 0.1689 0.2943 0.0001  -0.0051 0.0342  156  PHE   B CD1 
6379 C  CD2 . PHE   B 156 ? 0.1388 0.1510 0.2552 0.0067  -0.0216 0.0132  156  PHE   B CD2 
6380 C  CE1 . PHE   B 156 ? 0.1417 0.1837 0.3107 0.0053  -0.0058 0.0385  156  PHE   B CE1 
6381 C  CE2 . PHE   B 156 ? 0.1489 0.1700 0.2803 0.0105  -0.0192 0.0152  156  PHE   B CE2 
6382 C  CZ  . PHE   B 156 ? 0.1427 0.1797 0.3012 0.0144  -0.0202 0.0263  156  PHE   B CZ  
6392 N  N   . ASP   B 157 ? 0.1322 0.1370 0.2939 0.0109  -0.0237 -0.0277 157  ASP   B N   
6393 C  CA  . ASP   B 157 ? 0.1407 0.1445 0.3273 0.0062  -0.0289 -0.0294 157  ASP   B CA  
6394 C  C   . ASP   B 157 ? 0.1395 0.1422 0.3334 0.0102  -0.0232 -0.0488 157  ASP   B C   
6395 O  O   . ASP   B 157 ? 0.1336 0.1392 0.3194 0.0050  -0.0177 -0.0361 157  ASP   B O   
6396 C  CB  . ASP   B 157 ? 0.1628 0.1643 0.3450 0.0060  -0.0516 -0.0159 157  ASP   B CB  
6397 C  CG  . ASP   B 157 ? 0.1971 0.1747 0.3682 0.0054  -0.0386 -0.0104 157  ASP   B CG  
6398 O  OD1 . ASP   B 157 ? 0.2068 0.1670 0.3838 0.0151  -0.0335 -0.0140 157  ASP   B OD1 
6399 O  OD2 . ASP   B 157 ? 0.2308 0.1948 0.3997 0.0029  -0.0198 -0.0014 157  ASP   B OD2 
6404 N  N   . LYS   B 158 ? 0.1421 0.1656 0.3448 0.0083  -0.0071 -0.0722 158  LYS   B N   
6405 C  CA  . LYS   B 158 ? 0.1515 0.1840 0.3592 0.0126  -0.0040 -0.0845 158  LYS   B CA  
6406 C  C   . LYS   B 158 ? 0.1544 0.1704 0.3603 0.0122  -0.0098 -0.0797 158  LYS   B C   
6407 O  O   . LYS   B 158 ? 0.1601 0.1674 0.3588 -0.0013 -0.0125 -0.0883 158  LYS   B O   
6408 C  CB  . LYS   B 158 ? 0.1715 0.2200 0.3643 0.0123  0.0093  -0.1080 158  LYS   B CB  
6409 C  CG  . LYS   B 158 ? 0.2087 0.2609 0.3704 0.0126  0.0174  -0.1174 158  LYS   B CG  
6410 C  CD  . LYS   B 158 ? 0.2344 0.3068 0.3827 0.0094  0.0205  -0.1100 158  LYS   B CD  
6411 C  CE  . LYS   B 158 ? 0.2526 0.3315 0.3954 0.0096  0.0173  -0.1047 158  LYS   B CE  
6412 N  NZ  . LYS   B 158 ? 0.2549 0.3449 0.3962 0.0047  0.0168  -0.1025 158  LYS   B NZ  
6426 N  N   . ASN   B 159 ? 0.1580 0.1635 0.3762 0.0094  -0.0248 -0.0641 159  ASN   B N   
6427 C  CA  . ASN   B 159 ? 0.1692 0.1553 0.3924 0.0194  -0.0393 -0.0562 159  ASN   B CA  
6428 C  C   . ASN   B 159 ? 0.1580 0.1426 0.3801 0.0163  -0.0482 -0.0407 159  ASN   B C   
6429 O  O   . ASN   B 159 ? 0.1645 0.1373 0.3845 0.0010  -0.0497 -0.0297 159  ASN   B O   
6430 C  CB  . ASN   B 159 ? 0.1869 0.1671 0.4198 0.0266  -0.0444 -0.0523 159  ASN   B CB  
6431 C  CG  . ASN   B 159 ? 0.2112 0.1877 0.4450 0.0271  -0.0537 -0.0673 159  ASN   B CG  
6432 O  OD1 . ASN   B 159 ? 0.2272 0.1942 0.4445 0.0342  -0.0561 -0.0768 159  ASN   B OD1 
6433 N  ND2 . ASN   B 159 ? 0.2140 0.1981 0.4652 0.0352  -0.0586 -0.0610 159  ASN   B ND2 
6440 N  N   . LEU   B 160 ? 0.1471 0.1360 0.3587 0.0085  -0.0452 -0.0366 160  LEU   B N   
6441 C  CA  . LEU   B 160 ? 0.1446 0.1419 0.3189 0.0110  -0.0407 -0.0239 160  LEU   B CA  
6442 C  C   . LEU   B 160 ? 0.1415 0.1345 0.3090 0.0029  -0.0249 -0.0363 160  LEU   B C   
6443 O  O   . LEU   B 160 ? 0.1325 0.1345 0.2954 -0.0032 -0.0271 -0.0243 160  LEU   B O   
6444 C  CB  . LEU   B 160 ? 0.1442 0.1498 0.2911 0.0089  -0.0367 -0.0151 160  LEU   B CB  
6445 C  CG  . LEU   B 160 ? 0.1459 0.1671 0.2738 0.0175  -0.0356 -0.0090 160  LEU   B CG  
6446 C  CD1 . LEU   B 160 ? 0.1557 0.1829 0.2676 0.0020  -0.0296 -0.0095 160  LEU   B CD1 
6447 C  CD2 . LEU   B 160 ? 0.1468 0.1722 0.2778 0.0307  -0.0320 -0.0210 160  LEU   B CD2 
6459 N  N   . TYR   B 161 ? 0.1358 0.1381 0.3090 -0.0030 -0.0052 -0.0454 161  TYR   B N   
6460 C  CA  . TYR   B 161 ? 0.1451 0.1366 0.2972 -0.0065 0.0110  -0.0451 161  TYR   B CA  
6461 C  C   . TYR   B 161 ? 0.1452 0.1364 0.2866 -0.0095 0.0060  -0.0407 161  TYR   B C   
6462 O  O   . TYR   B 161 ? 0.1474 0.1372 0.2825 -0.0155 0.0009  -0.0378 161  TYR   B O   
6463 C  CB  . TYR   B 161 ? 0.1604 0.1392 0.3001 -0.0159 0.0285  -0.0442 161  TYR   B CB  
6464 C  CG  . TYR   B 161 ? 0.1823 0.1437 0.2887 -0.0214 0.0363  -0.0534 161  TYR   B CG  
6465 C  CD1 . TYR   B 161 ? 0.1893 0.1423 0.2882 -0.0342 0.0353  -0.0467 161  TYR   B CD1 
6466 C  CD2 . TYR   B 161 ? 0.2027 0.1540 0.2812 -0.0261 0.0294  -0.0610 161  TYR   B CD2 
6467 C  CE1 . TYR   B 161 ? 0.2059 0.1567 0.2926 -0.0373 0.0325  -0.0427 161  TYR   B CE1 
6468 C  CE2 . TYR   B 161 ? 0.2215 0.1653 0.2931 -0.0303 0.0309  -0.0496 161  TYR   B CE2 
6469 C  CZ  . TYR   B 161 ? 0.2178 0.1684 0.2905 -0.0421 0.0268  -0.0399 161  TYR   B CZ  
6470 O  OH  . TYR   B 161 ? 0.2447 0.1963 0.3090 -0.0417 0.0233  -0.0353 161  TYR   B OH  
6480 N  N   . ASP   B 162 ? 0.1523 0.1339 0.3021 -0.0017 -0.0082 -0.0527 162  ASP   B N   
6481 C  CA  . ASP   B 162 ? 0.1639 0.1404 0.3024 -0.0056 -0.0064 -0.0537 162  ASP   B CA  
6482 C  C   . ASP   B 162 ? 0.1631 0.1303 0.2954 -0.0113 -0.0076 -0.0431 162  ASP   B C   
6483 O  O   . ASP   B 162 ? 0.1686 0.1383 0.2919 -0.0138 -0.0119 -0.0331 162  ASP   B O   
6484 C  CB  . ASP   B 162 ? 0.1843 0.1606 0.3235 -0.0020 -0.0092 -0.0709 162  ASP   B CB  
6485 C  CG  . ASP   B 162 ? 0.1903 0.1833 0.3386 0.0065  -0.0045 -0.0815 162  ASP   B CG  
6486 O  OD1 . ASP   B 162 ? 0.1869 0.1998 0.3303 0.0020  0.0116  -0.0781 162  ASP   B OD1 
6487 O  OD2 . ASP   B 162 ? 0.2066 0.2018 0.3643 0.0211  -0.0033 -0.0791 162  ASP   B OD2 
6492 N  N   A LYS   B 163 ? 0.1593 0.1172 0.2865 -0.0128 -0.0158 -0.0309 163  LYS   B N   
6493 N  N   B LYS   B 163 ? 0.1645 0.1314 0.2886 -0.0124 -0.0144 -0.0282 163  LYS   B N   
6494 C  CA  A LYS   B 163 ? 0.1653 0.1300 0.2877 -0.0179 -0.0200 -0.0142 163  LYS   B CA  
6495 C  CA  B LYS   B 163 ? 0.1710 0.1471 0.2898 -0.0153 -0.0172 -0.0114 163  LYS   B CA  
6496 C  C   A LYS   B 163 ? 0.1410 0.1247 0.2784 -0.0197 -0.0177 -0.0065 163  LYS   B C   
6497 C  C   B LYS   B 163 ? 0.1472 0.1342 0.2777 -0.0168 -0.0165 -0.0040 163  LYS   B C   
6498 O  O   A LYS   B 163 ? 0.1414 0.1348 0.3021 -0.0202 -0.0151 -0.0035 163  LYS   B O   
6499 O  O   B LYS   B 163 ? 0.1480 0.1402 0.2950 -0.0177 -0.0155 0.0003  163  LYS   B O   
6500 C  CB  A LYS   B 163 ? 0.2046 0.1608 0.3207 -0.0112 -0.0189 0.0008  163  LYS   B CB  
6501 C  CB  B LYS   B 163 ? 0.2049 0.1812 0.3188 -0.0117 -0.0167 0.0003  163  LYS   B CB  
6502 C  CG  A LYS   B 163 ? 0.2620 0.2195 0.3654 -0.0151 -0.0124 0.0075  163  LYS   B CG  
6503 C  CG  B LYS   B 163 ? 0.2491 0.2269 0.3567 -0.0138 -0.0130 0.0068  163  LYS   B CG  
6504 C  CD  A LYS   B 163 ? 0.3111 0.2641 0.4086 -0.0222 -0.0154 0.0008  163  LYS   B CD  
6505 C  CD  B LYS   B 163 ? 0.2869 0.2676 0.3947 -0.0178 -0.0152 0.0052  163  LYS   B CD  
6506 C  CE  A LYS   B 163 ? 0.3401 0.2915 0.4355 -0.0263 -0.0156 0.0015  163  LYS   B CE  
6507 C  CE  B LYS   B 163 ? 0.3098 0.2931 0.4208 -0.0209 -0.0155 0.0067  163  LYS   B CE  
6508 N  NZ  A LYS   B 163 ? 0.3597 0.3055 0.4569 -0.0278 -0.0140 0.0009  163  LYS   B NZ  
6509 N  NZ  B LYS   B 163 ? 0.3245 0.3010 0.4395 -0.0221 -0.0150 0.0071  163  LYS   B NZ  
6536 N  N   . LEU   B 164 ? 0.1321 0.1229 0.2596 -0.0156 -0.0144 0.0003  164  LEU   B N   
6537 C  CA  . LEU   B 164 ? 0.1319 0.1227 0.2415 -0.0091 -0.0192 -0.0023 164  LEU   B CA  
6538 C  C   . LEU   B 164 ? 0.1372 0.1219 0.2419 -0.0132 -0.0272 -0.0071 164  LEU   B C   
6539 O  O   . LEU   B 164 ? 0.1387 0.1434 0.2594 -0.0089 -0.0282 -0.0084 164  LEU   B O   
6540 C  CB  . LEU   B 164 ? 0.1339 0.1239 0.2206 -0.0050 -0.0217 -0.0039 164  LEU   B CB  
6541 C  CG  . LEU   B 164 ? 0.1393 0.1388 0.2355 -0.0100 -0.0071 -0.0014 164  LEU   B CG  
6542 C  CD1 . LEU   B 164 ? 0.1466 0.1359 0.2339 -0.0108 -0.0157 -0.0093 164  LEU   B CD1 
6543 C  CD2 . LEU   B 164 ? 0.1535 0.1783 0.2487 -0.0068 0.0096  -0.0186 164  LEU   B CD2 
6556 N  N   . VAL   B 165 ? 0.1639 0.1326 0.2631 -0.0173 -0.0307 -0.0194 165  VAL   B N   
6557 C  CA  . VAL   B 165 ? 0.1991 0.1432 0.2637 -0.0226 -0.0479 -0.0152 165  VAL   B CA  
6558 C  C   . VAL   B 165 ? 0.2237 0.1515 0.2976 -0.0347 -0.0737 -0.0119 165  VAL   B C   
6559 O  O   . VAL   B 165 ? 0.2361 0.1714 0.2948 -0.0420 -0.0763 0.0003  165  VAL   B O   
6560 C  CB  . VAL   B 165 ? 0.2167 0.1604 0.2576 -0.0073 -0.0170 -0.0224 165  VAL   B CB  
6561 C  CG1 . VAL   B 165 ? 0.2327 0.1701 0.2779 -0.0127 -0.0053 -0.0161 165  VAL   B CG1 
6562 C  CG2 . VAL   B 165 ? 0.2084 0.1669 0.2514 -0.0044 -0.0016 -0.0224 165  VAL   B CG2 
6572 N  N   A SER   B 166 ? 0.2310 0.1437 0.3239 -0.0325 -0.0777 -0.0327 166  SER   B N   
6573 N  N   B SER   B 166 ? 0.2283 0.1477 0.3158 -0.0345 -0.0756 -0.0203 166  SER   B N   
6574 C  CA  A SER   B 166 ? 0.2255 0.1497 0.3673 -0.0331 -0.0696 -0.0370 166  SER   B CA  
6575 C  CA  B SER   B 166 ? 0.2238 0.1526 0.3451 -0.0357 -0.0694 -0.0203 166  SER   B CA  
6576 C  C   A SER   B 166 ? 0.2130 0.1583 0.3827 -0.0356 -0.0680 -0.0134 166  SER   B C   
6577 C  C   B SER   B 166 ? 0.2130 0.1567 0.3639 -0.0373 -0.0662 -0.0035 166  SER   B C   
6578 O  O   A SER   B 166 ? 0.2141 0.1766 0.4114 -0.0436 -0.0811 -0.0280 166  SER   B O   
6579 O  O   B SER   B 166 ? 0.2151 0.1677 0.3823 -0.0446 -0.0732 -0.0130 166  SER   B O   
6580 C  CB  A SER   B 166 ? 0.2270 0.1599 0.3929 -0.0236 -0.0641 -0.0429 166  SER   B CB  
6581 C  CB  B SER   B 166 ? 0.2260 0.1604 0.3548 -0.0298 -0.0668 -0.0224 166  SER   B CB  
6582 O  OG  A SER   B 166 ? 0.2202 0.1562 0.4102 -0.0177 -0.0627 -0.0302 166  SER   B OG  
6583 O  OG  B SER   B 166 ? 0.2220 0.1586 0.3628 -0.0264 -0.0660 -0.0111 166  SER   B OG  
6594 N  N   . SER   B 167 ? 0.2013 0.1526 0.3568 -0.0343 -0.0635 0.0148  167  SER   B N   
6595 C  CA  . SER   B 167 ? 0.1918 0.1555 0.3370 -0.0268 -0.0469 0.0168  167  SER   B CA  
6596 C  C   . SER   B 167 ? 0.1829 0.1653 0.3235 -0.0413 -0.0431 0.0399  167  SER   B C   
6597 O  O   . SER   B 167 ? 0.1843 0.1775 0.3206 -0.0484 -0.0436 0.0378  167  SER   B O   
6598 C  CB  . SER   B 167 ? 0.1841 0.1669 0.3345 -0.0256 -0.0215 0.0176  167  SER   B CB  
6599 O  OG  . SER   B 167 ? 0.1777 0.1755 0.3224 -0.0214 -0.0101 0.0190  167  SER   B OG  
6606 N  N   . PHE   B 168 ? 0.1800 0.1644 0.3175 -0.0371 -0.0295 0.0505  168  PHE   B N   
6607 C  CA  . PHE   B 168 ? 0.1836 0.1592 0.2924 -0.0395 -0.0209 0.0300  168  PHE   B CA  
6608 C  C   . PHE   B 168 ? 0.1555 0.1483 0.2409 -0.0219 -0.0062 0.0158  168  PHE   B C   
6609 O  O   . PHE   B 168 ? 0.1891 0.1419 0.2468 0.0006  -0.0055 0.0035  168  PHE   B O   
6610 C  CB  . PHE   B 168 ? 0.1997 0.1630 0.3006 -0.0468 -0.0423 0.0427  168  PHE   B CB  
6611 C  CG  . PHE   B 168 ? 0.2275 0.1471 0.2990 -0.0517 -0.0487 0.0174  168  PHE   B CG  
6612 C  CD1 . PHE   B 168 ? 0.2575 0.1549 0.3085 -0.0414 -0.0511 0.0129  168  PHE   B CD1 
6613 C  CD2 . PHE   B 168 ? 0.2187 0.1438 0.2971 -0.0395 -0.0472 0.0252  168  PHE   B CD2 
6614 C  CE1 . PHE   B 168 ? 0.2682 0.1659 0.3081 -0.0268 -0.0456 0.0181  168  PHE   B CE1 
6615 C  CE2 . PHE   B 168 ? 0.2420 0.1515 0.3015 -0.0265 -0.0518 0.0184  168  PHE   B CE2 
6616 C  CZ  . PHE   B 168 ? 0.2564 0.1514 0.3025 -0.0152 -0.0498 0.0316  168  PHE   B CZ  
6626 N  N   . LEU   B 169 ? 0.1612 0.1603 0.2367 -0.0027 0.0066  -0.0033 169  LEU   B N   
6627 C  CA  . LEU   B 169 ? 0.1885 0.1891 0.2763 -0.0074 0.0019  -0.0290 169  LEU   B CA  
6628 C  C   . LEU   B 169 ? 0.2162 0.2108 0.3291 0.0063  -0.0002 -0.0602 169  LEU   B C   
6629 O  O   . LEU   B 169 ? 0.2358 0.2331 0.3880 -0.0002 -0.0026 -0.0779 169  LEU   B O   
6630 C  CB  . LEU   B 169 ? 0.2123 0.2267 0.2876 -0.0159 -0.0088 -0.0052 169  LEU   B CB  
6631 C  CG  . LEU   B 169 ? 0.2535 0.2591 0.3309 -0.0060 -0.0050 0.0012  169  LEU   B CG  
6632 C  CD1 . LEU   B 169 ? 0.2654 0.2792 0.3318 -0.0046 -0.0092 0.0148  169  LEU   B CD1 
6633 C  CD2 . LEU   B 169 ? 0.2503 0.2643 0.3378 0.0076  0.0097  -0.0092 169  LEU   B CD2 
6634 O  OXT . LEU   B 169 ? 0.2369 0.2300 0.3244 0.0366  0.0030  -0.0554 169  LEU   B OXT 
6646 N  N2  B A1BCC C .   ? 0.1634 0.1431 0.1292 0.0059  0.0027  0.0431  201  A1BCC A N2  
6647 C  C3  B A1BCC C .   ? 0.1813 0.1589 0.1585 0.0115  -0.0176 0.0162  201  A1BCC A C3  
6648 C  C6  B A1BCC C .   ? 0.1557 0.1487 0.1466 0.0073  0.0073  0.0400  201  A1BCC A C6  
6649 C  C9  B A1BCC C .   ? 0.1456 0.1522 0.1598 0.0162  0.0126  0.0311  201  A1BCC A C9  
6650 C  C1  B A1BCC C .   ? 0.1715 0.1559 0.1638 0.0201  -0.0185 0.0137  201  A1BCC A C1  
6651 C  C10 B A1BCC C .   ? 0.1415 0.1559 0.1635 0.0121  0.0057  0.0265  201  A1BCC A C10 
6652 C  C2  B A1BCC C .   ? 0.1765 0.1579 0.1640 0.0174  -0.0182 0.0188  201  A1BCC A C2  
6653 C  C4  B A1BCC C .   ? 0.1709 0.1488 0.1694 0.0125  -0.0215 0.0289  201  A1BCC A C4  
6654 C  C5  B A1BCC C .   ? 0.1601 0.1489 0.1344 0.0058  -0.0000 0.0365  201  A1BCC A C5  
6655 C  C7  B A1BCC C .   ? 0.1466 0.1458 0.1493 0.0111  0.0058  0.0335  201  A1BCC A C7  
6656 C  C8  B A1BCC C .   ? 0.1455 0.1484 0.1422 0.0130  0.0089  0.0402  201  A1BCC A C8  
6657 N  N1  B A1BCC C .   ? 0.1775 0.1604 0.1519 0.0091  -0.0037 0.0202  201  A1BCC A N1  
6658 N  N3  B A1BCC C .   ? 0.1505 0.1461 0.1478 0.0067  0.0128  0.0378  201  A1BCC A N3  
6659 N  N4  B A1BCC C .   ? 0.1499 0.1459 0.1606 0.0144  0.0005  0.0317  201  A1BCC A N4  
6660 O  O1  B A1BCC C .   ? 0.1749 0.1439 0.1613 0.0131  -0.0153 0.0445  201  A1BCC A O1  
6675 CL CL  B CL    D .   ? 0.2257 0.1745 0.2670 0.0197  -0.0622 -0.0603 202  CL    A CL  
6676 O  O   . HOH   E .   ? 0.5213 0.5680 0.3918 -0.1285 -0.1021 -0.0768 1301 HOH   A O   
6677 O  O   . HOH   E .   ? 0.5803 0.5456 0.6367 0.0321  -0.1159 0.0677  1302 HOH   A O   
6678 O  O   . HOH   E .   ? 0.2936 0.2193 0.3172 -0.0155 -0.0438 0.0576  1303 HOH   A O   
6679 O  O   . HOH   E .   ? 0.7497 0.6331 0.3399 -0.0848 0.0400  0.2295  1304 HOH   A O   
6680 O  O   . HOH   E .   ? 0.3183 0.3341 0.1597 -0.0447 0.0525  0.0537  1305 HOH   A O   
6681 O  O   . HOH   E .   ? 0.6003 0.4373 0.3232 0.1698  -0.1240 0.0645  1306 HOH   A O   
6682 O  O   . HOH   E .   ? 0.4131 0.8174 0.3947 -0.1203 0.0834  0.0271  1307 HOH   A O   
6683 O  O   . HOH   E .   ? 0.2559 0.2311 0.2974 -0.0197 0.0721  0.0663  1308 HOH   A O   
6684 O  O   . HOH   E .   ? 0.1393 0.4330 0.2628 -0.0090 0.0167  0.0625  1309 HOH   A O   
6685 O  O   . HOH   E .   ? 0.2602 0.5569 0.3796 0.0233  -0.0690 0.0949  1310 HOH   A O   
6686 O  O   . HOH   E .   ? 0.5310 0.3623 0.4643 -0.0807 0.1350  0.1186  1311 HOH   A O   
6687 O  O   . HOH   E .   ? 0.1781 0.3436 0.4429 -0.0292 0.0358  -0.1484 1312 HOH   A O   
6688 O  O   . HOH   E .   ? 0.6063 0.6079 0.3291 0.2394  -0.0692 -0.0668 1313 HOH   A O   
6689 O  O   . HOH   E .   ? 0.5000 0.2007 0.4450 0.0652  0.0213  0.0143  1314 HOH   A O   
6690 O  O   . HOH   E .   ? 0.1963 0.1787 0.3535 -0.0458 0.0214  -0.0376 1315 HOH   A O   
6691 O  O   . HOH   E .   ? 0.4237 0.3510 0.5581 -0.0743 0.1226  -0.0944 1316 HOH   A O   
6692 O  O   . HOH   E .   ? 0.2221 0.1953 0.2316 -0.0220 0.0175  0.0072  1317 HOH   A O   
6693 O  O   . HOH   E .   ? 0.6919 0.5073 0.3370 -0.0131 -0.0434 0.1080  1318 HOH   A O   
6694 O  O   . HOH   E .   ? 0.4680 0.3423 0.4867 0.0547  0.1758  -0.0895 1319 HOH   A O   
6695 O  O   . HOH   E .   ? 0.3497 0.3024 0.2193 -0.0015 -0.1105 0.0298  1320 HOH   A O   
6696 O  O   . HOH   E .   ? 0.4528 0.3455 0.3898 -0.0292 0.2377  0.0200  1321 HOH   A O   
6697 O  O   . HOH   E .   ? 0.3851 0.3600 0.4556 -0.1542 -0.0624 0.1909  1322 HOH   A O   
6698 O  O   . HOH   E .   ? 0.1609 0.2699 0.2739 0.0260  -0.0172 -0.0149 1323 HOH   A O   
6699 O  O   . HOH   E .   ? 0.3046 0.7187 0.4853 -0.0085 -0.0644 0.1425  1324 HOH   A O   
6700 O  O   . HOH   E .   ? 0.2984 0.4623 0.2986 -0.0134 0.0644  0.0877  1325 HOH   A O   
6701 O  O   . HOH   E .   ? 0.2829 0.2713 0.2503 -0.0732 0.0316  0.0674  1326 HOH   A O   
6702 O  O   A HOH   E .   ? 0.1654 0.2368 0.2324 0.0561  0.0546  0.0898  1327 HOH   A O   
6703 O  O   . HOH   E .   ? 0.2726 0.4465 0.5660 -0.0119 0.1193  0.2175  1328 HOH   A O   
6704 O  O   A HOH   E .   ? 0.3105 0.1456 0.1482 0.0355  0.0131  0.0117  1329 HOH   A O   
6705 O  O   . HOH   E .   ? 0.5042 0.4332 0.3259 -0.0515 -0.1000 -0.0728 1330 HOH   A O   
6706 O  O   . HOH   E .   ? 0.2412 0.2336 0.4379 -0.0213 -0.0746 0.1324  1331 HOH   A O   
6707 O  O   . HOH   E .   ? 0.1400 0.1459 0.2042 -0.0169 0.0081  0.0086  1332 HOH   A O   
6708 O  O   . HOH   E .   ? 0.2047 0.1605 0.1352 -0.0070 0.0220  0.0151  1333 HOH   A O   
6709 O  O   B HOH   E .   ? 0.1934 0.2304 0.1962 -0.0069 -0.0359 -0.0536 1334 HOH   A O   
6710 O  O   B HOH   E .   ? 0.2709 0.2680 0.4080 0.1471  0.0574  0.0513  1335 HOH   A O   
6711 O  O   . HOH   E .   ? 0.2512 0.2732 0.3936 -0.0615 0.1147  0.0035  1336 HOH   A O   
6712 O  O   . HOH   E .   ? 0.2060 0.4281 0.3647 -0.0283 -0.0561 0.1654  1337 HOH   A O   
6713 O  O   B HOH   E .   ? 0.3084 0.5075 0.3250 0.0962  0.0315  -0.0199 1338 HOH   A O   
6714 O  O   . HOH   E .   ? 0.1567 0.1712 0.2134 -0.0226 0.0059  0.0465  1339 HOH   A O   
6715 O  O   . HOH   E .   ? 0.2301 0.2803 0.2895 0.0057  -0.0171 -0.0752 1340 HOH   A O   
6716 O  O   . HOH   E .   ? 0.2441 0.2201 0.2664 0.0472  0.0377  0.0486  1341 HOH   A O   
6717 O  O   . HOH   E .   ? 0.4870 0.5261 0.2607 -0.1185 0.1329  0.0799  1342 HOH   A O   
6718 O  O   . HOH   E .   ? 0.3818 0.2073 0.5085 0.0339  -0.1650 0.0777  1343 HOH   A O   
6719 O  O   . HOH   E .   ? 0.1422 0.2207 0.2023 0.0096  -0.0032 0.0569  1344 HOH   A O   
6720 O  O   . HOH   E .   ? 0.3713 0.3318 0.5045 0.1265  0.0821  0.0479  1345 HOH   A O   
6721 O  O   B HOH   E .   ? 0.1913 0.1337 0.3114 -0.0324 -0.0127 -0.0653 1346 HOH   A O   
6722 O  O   . HOH   E .   ? 0.4975 0.2887 0.3996 0.0897  -0.0272 -0.0443 1347 HOH   A O   
6723 O  O   . HOH   E .   ? 0.2908 0.3860 0.3368 -0.1166 -0.0718 -0.0451 1348 HOH   A O   
6724 O  O   . HOH   E .   ? 0.2043 0.1686 0.2348 -0.0117 -0.0511 -0.0028 1349 HOH   A O   
6725 O  O   . HOH   E .   ? 0.1246 0.1226 0.1184 -0.0040 0.0108  0.0092  1350 HOH   A O   
6726 O  O   . HOH   E .   ? 0.2885 0.3419 0.2103 -0.0710 -0.0294 -0.0687 1351 HOH   A O   
6727 O  O   B HOH   E .   ? 0.5078 0.2856 0.3527 0.1301  -0.0567 -0.0725 1352 HOH   A O   
6728 O  O   . HOH   E .   ? 0.2487 0.1987 0.2219 -0.0544 0.0105  0.0586  1353 HOH   A O   
6729 O  O   . HOH   E .   ? 0.2731 0.4346 0.2837 -0.0520 0.0525  -0.0046 1354 HOH   A O   
6730 O  O   . HOH   E .   ? 0.4854 0.3680 0.3586 0.0122  -0.0801 -0.0731 1355 HOH   A O   
6731 O  O   . HOH   E .   ? 0.3537 0.4652 0.3236 0.2084  0.0736  0.0739  1356 HOH   A O   
6732 O  O   A HOH   E .   ? 0.4249 0.4110 0.4400 0.1286  0.0864  -0.0733 1357 HOH   A O   
6733 O  O   . HOH   E .   ? 0.1755 0.1746 0.1407 0.0088  0.0006  0.0166  1358 HOH   A O   
6734 O  O   . HOH   E .   ? 0.1915 0.1969 0.3281 0.0189  0.0857  -0.0102 1359 HOH   A O   
6735 O  O   . HOH   E .   ? 0.1961 0.1604 0.1931 0.0171  -0.0221 -0.0033 1360 HOH   A O   
6736 O  O   . HOH   E .   ? 0.4683 0.3480 0.4521 -0.1990 0.2038  -0.1252 1361 HOH   A O   
6737 O  O   . HOH   E .   ? 0.1449 0.1769 0.2531 0.0079  -0.0117 0.0172  1362 HOH   A O   
6738 O  O   A HOH   E .   ? 0.2198 0.3165 0.1974 0.0712  0.0018  -0.0003 1363 HOH   A O   
6739 O  O   . HOH   E .   ? 0.1704 0.2163 0.1592 -0.0110 -0.0011 0.0557  1364 HOH   A O   
6740 O  O   . HOH   E .   ? 0.2337 0.3699 0.3485 0.0960  -0.0775 -0.0253 1365 HOH   A O   
6741 O  O   . HOH   E .   ? 0.5860 0.3726 0.2605 -0.0294 0.0351  0.1111  1366 HOH   A O   
6742 O  O   . HOH   E .   ? 0.2458 0.3858 0.2490 0.0235  0.0486  0.1382  1367 HOH   A O   
6743 O  O   . HOH   E .   ? 0.3644 0.7171 0.4061 -0.0530 -0.1297 0.0429  1368 HOH   A O   
6744 O  O   . HOH   E .   ? 0.4660 0.3166 0.2960 -0.1104 0.0365  0.0858  1369 HOH   A O   
6745 O  O   . HOH   E .   ? 0.1504 0.1227 0.2057 -0.0037 0.0130  -0.0090 1370 HOH   A O   
6746 O  O   . HOH   E .   ? 0.2793 0.2235 0.5164 -0.0491 -0.0405 0.0469  1371 HOH   A O   
6747 O  O   . HOH   E .   ? 0.4003 0.1998 0.2010 0.1139  0.0539  0.0166  1372 HOH   A O   
6748 O  O   . HOH   E .   ? 0.1822 0.1813 0.2209 -0.0265 0.0178  0.0285  1373 HOH   A O   
6749 O  O   . HOH   E .   ? 0.2659 0.3181 0.5497 -0.0512 -0.1232 -0.0712 1374 HOH   A O   
6750 O  O   B HOH   E .   ? 0.2189 0.2329 0.4456 0.0060  0.0018  0.0072  1375 HOH   A O   
6751 O  O   . HOH   E .   ? 0.1401 0.1434 0.1323 -0.0051 -0.0114 -0.0003 1376 HOH   A O   
6752 O  O   A HOH   E .   ? 0.1588 0.1825 0.2778 0.0166  0.0714  -0.0545 1377 HOH   A O   
6753 O  O   . HOH   E .   ? 0.3694 0.2136 0.4323 -0.1183 0.0657  0.0247  1378 HOH   A O   
6754 O  O   . HOH   E .   ? 0.4425 0.4659 0.5392 -0.0666 0.0089  0.0798  1379 HOH   A O   
6755 O  O   B HOH   E .   ? 0.2549 0.2957 0.2384 0.0034  0.0240  -0.0014 1380 HOH   A O   
6756 O  O   . HOH   E .   ? 0.1712 0.1484 0.1840 0.0142  -0.0269 0.0247  1381 HOH   A O   
6757 O  O   A HOH   E .   ? 0.2456 0.4297 0.4437 0.0620  0.0130  0.0526  1382 HOH   A O   
6758 O  O   . HOH   E .   ? 0.1800 0.1917 0.2587 -0.0092 -0.0100 0.0937  1383 HOH   A O   
6759 O  O   B HOH   E .   ? 0.2824 0.4483 0.2006 -0.0412 0.0466  -0.0525 1384 HOH   A O   
6760 O  O   . HOH   E .   ? 0.2665 0.4337 0.3419 0.0876  0.0376  0.0849  1385 HOH   A O   
6761 O  O   . HOH   E .   ? 0.5908 0.4991 0.5158 0.0915  0.1597  -0.0877 1386 HOH   A O   
6762 O  O   . HOH   E .   ? 0.1970 0.2118 0.2020 -0.0325 -0.0411 0.0412  1387 HOH   A O   
6763 O  O   . HOH   E .   ? 0.2136 0.3119 0.2745 -0.0097 -0.0066 0.0298  1388 HOH   A O   
6764 O  O   A HOH   E .   ? 0.1247 0.1386 0.1599 -0.0011 -0.0102 -0.0307 1389 HOH   A O   
6765 O  O   . HOH   E .   ? 0.2977 0.2802 0.2019 0.0126  0.0798  -0.0014 1390 HOH   A O   
6766 O  O   A HOH   E .   ? 0.5433 0.2158 0.4153 -0.0043 -0.0987 0.0414  1391 HOH   A O   
6767 O  O   . HOH   E .   ? 0.3239 0.2202 0.3570 -0.0004 -0.0438 0.0898  1392 HOH   A O   
6768 O  O   A HOH   E .   ? 0.5369 0.3554 0.3162 -0.0732 0.1229  0.1151  1393 HOH   A O   
6769 O  O   . HOH   E .   ? 0.3258 0.2903 0.3184 -0.0988 -0.0214 -0.0049 1394 HOH   A O   
6770 O  O   . HOH   E .   ? 0.2460 0.1933 0.1718 -0.0548 0.0218  0.0284  1395 HOH   A O   
6771 O  O   . HOH   E .   ? 0.2265 0.1692 0.2505 0.0017  0.0178  0.0283  1396 HOH   A O   
6772 O  O   . HOH   E .   ? 0.1709 0.2384 0.3278 -0.0068 0.0683  0.0838  1397 HOH   A O   
6773 O  O   A HOH   E .   ? 0.1998 0.1735 0.2079 0.0033  0.0090  0.0490  1398 HOH   A O   
6774 O  O   . HOH   E .   ? 0.2681 0.5912 0.3448 0.0961  0.0689  -0.1068 1399 HOH   A O   
6775 O  O   . HOH   E .   ? 0.2328 0.4263 0.3379 -0.0380 0.0970  -0.0907 1400 HOH   A O   
6776 O  O   . HOH   E .   ? 0.1846 0.1762 0.3704 0.0379  0.1126  0.0980  1401 HOH   A O   
6777 O  O   . HOH   E .   ? 0.4374 0.4376 0.2027 0.0427  0.1002  0.1092  1402 HOH   A O   
6778 O  O   . HOH   E .   ? 0.6070 0.7220 0.5387 0.1363  -0.1496 0.0747  1403 HOH   A O   
6779 O  O   . HOH   E .   ? 0.4483 0.6097 0.3180 -0.0516 -0.0154 0.1481  1404 HOH   A O   
6780 O  O   . HOH   E .   ? 0.4760 0.2635 0.3024 -0.0470 0.0517  0.0367  1405 HOH   A O   
6781 O  O   . HOH   E .   ? 0.3640 0.5847 0.4225 -0.0766 0.0533  0.1356  1406 HOH   A O   
6782 O  O   . HOH   E .   ? 0.1982 0.2091 0.3156 0.0145  -0.0545 0.0243  1407 HOH   A O   
6783 O  O   A HOH   E .   ? 0.1256 0.1482 0.1238 0.0050  -0.0312 -0.0236 1408 HOH   A O   
6784 O  O   A HOH   E .   ? 0.2277 0.2613 0.2517 -0.0051 0.0680  -0.0102 1409 HOH   A O   
6785 O  O   . HOH   E .   ? 0.1283 0.1330 0.1612 0.0004  -0.0211 0.0029  1410 HOH   A O   
6786 O  O   A HOH   E .   ? 0.2490 0.1707 0.3963 -0.0103 0.0919  0.0014  1411 HOH   A O   
6787 O  O   . HOH   E .   ? 0.2040 0.1660 0.2669 0.0017  -0.0261 0.0094  1412 HOH   A O   
6788 O  O   A HOH   E .   ? 0.1042 0.1144 0.1425 0.0055  -0.0256 -0.0279 1413 HOH   A O   
6789 O  O   . HOH   E .   ? 0.1856 0.2506 0.3481 -0.0203 -0.0229 0.0118  1414 HOH   A O   
6790 O  O   . HOH   E .   ? 0.1590 0.1332 0.1482 -0.0175 0.0071  0.0055  1415 HOH   A O   
6791 O  O   . HOH   E .   ? 0.1475 0.1586 0.2456 0.0022  0.0066  0.0216  1416 HOH   A O   
6792 O  O   . HOH   E .   ? 0.2858 0.2433 0.1968 -0.0565 -0.0831 0.0275  1417 HOH   A O   
6793 O  O   . HOH   E .   ? 0.3004 0.3598 0.4787 -0.0184 0.1589  -0.0098 1418 HOH   A O   
6794 O  O   B HOH   E .   ? 0.1222 0.1484 0.2113 0.0018  0.0173  0.0574  1419 HOH   A O   
6795 O  O   . HOH   E .   ? 0.3425 0.3695 0.2929 0.1417  -0.0688 -0.1136 1420 HOH   A O   
6796 O  O   . HOH   E .   ? 0.3250 0.5669 0.4679 0.0683  0.0367  0.0946  1421 HOH   A O   
6797 O  O   . HOH   E .   ? 0.3101 0.3509 0.7065 -0.0161 0.0996  -0.0281 1422 HOH   A O   
6798 O  O   . HOH   E .   ? 0.3271 0.1274 0.2018 0.0046  -0.0465 0.0044  1423 HOH   A O   
6799 O  O   . HOH   E .   ? 0.2742 0.5737 0.1699 -0.0477 0.0549  0.0022  1424 HOH   A O   
6800 O  O   A HOH   E .   ? 0.2598 0.2118 0.3068 0.0506  0.0772  0.1049  1425 HOH   A O   
6801 O  O   B HOH   E .   ? 0.1906 0.3359 0.3492 -0.0255 -0.1060 -0.1002 1426 HOH   A O   
6802 O  O   . HOH   E .   ? 0.2089 0.2810 0.2314 -0.0100 -0.0558 0.0481  1427 HOH   A O   
6803 O  O   . HOH   E .   ? 0.2174 0.4328 0.2290 0.1602  -0.0097 0.0150  1428 HOH   A O   
6804 O  O   . HOH   E .   ? 0.4016 0.2043 0.5205 -0.0661 -0.2171 0.0939  1429 HOH   A O   
6805 O  O   . HOH   E .   ? 0.6640 0.3949 0.5881 0.1982  -0.0486 0.1623  1430 HOH   A O   
6806 O  O   A HOH   E .   ? 0.5459 0.3740 0.5623 -0.1120 0.0172  -0.0068 1431 HOH   A O   
6807 O  O   . HOH   E .   ? 0.1992 0.1842 0.2826 0.0166  -0.0521 0.0297  1432 HOH   A O   
6808 O  O   B HOH   E .   ? 0.2359 0.3339 0.3838 0.0403  0.0898  0.0769  1433 HOH   A O   
6809 O  O   . HOH   E .   ? 0.1529 0.2007 0.2797 -0.0151 -0.0001 0.0694  1434 HOH   A O   
6810 O  O   . HOH   E .   ? 0.5714 0.6567 0.3949 0.0617  0.2561  -0.0854 1435 HOH   A O   
6811 O  O   A HOH   E .   ? 0.1705 0.1924 0.3249 0.0161  -0.0322 -0.0545 1436 HOH   A O   
6812 O  O   . HOH   E .   ? 0.4238 0.4709 0.3103 0.0114  -0.1258 0.0066  1437 HOH   A O   
6813 O  O   . HOH   E .   ? 0.6132 0.5410 0.5392 -0.1491 0.1039  -0.0946 1438 HOH   A O   
6814 O  O   . HOH   E .   ? 0.5216 0.5498 0.6313 -0.1073 -0.1144 -0.1258 1439 HOH   A O   
6815 O  O   A HOH   E .   ? 0.1679 0.1326 0.1277 0.0064  -0.0217 -0.0260 1440 HOH   A O   
6816 O  O   . HOH   E .   ? 0.3630 0.2442 0.1582 -0.0812 0.0374  0.0511  1441 HOH   A O   
6817 O  O   . HOH   E .   ? 0.5608 0.6215 0.4682 0.0484  -0.0710 0.0795  1442 HOH   A O   
6818 O  O   . HOH   E .   ? 0.2372 0.2645 0.3742 0.0066  0.0163  -0.0794 1443 HOH   A O   
6819 O  O   . HOH   E .   ? 0.6758 0.6541 0.5581 -0.1265 -0.0211 0.0722  1444 HOH   A O   
6820 O  O   . HOH   E .   ? 0.2460 0.1569 0.2501 0.0085  0.0115  0.0079  1445 HOH   A O   
6821 O  O   . HOH   E .   ? 0.5688 0.5101 0.7573 0.0261  -0.1296 0.2228  1446 HOH   A O   
6822 O  O   A HOH   E .   ? 0.2045 0.1873 0.3049 0.0343  -0.1046 -0.0805 1447 HOH   A O   
6823 O  O   . HOH   E .   ? 0.3693 0.3196 0.3684 0.1891  -0.0660 -0.0651 1448 HOH   A O   
6824 O  O   . HOH   E .   ? 0.4646 0.4869 0.5578 -0.0069 0.0561  -0.1247 1449 HOH   A O   
6825 O  O   . HOH   E .   ? 0.2214 0.2025 0.2328 0.0271  0.0382  0.0276  1450 HOH   A O   
6826 O  O   . HOH   E .   ? 0.7707 0.8831 0.6310 0.0075  0.0438  -0.0578 1451 HOH   A O   
6827 O  O   . HOH   E .   ? 0.3743 0.3957 0.4234 0.0449  -0.0556 0.1056  1452 HOH   A O   
6828 O  O   . HOH   E .   ? 0.4339 0.3897 0.4930 -0.0693 -0.1142 -0.1209 1453 HOH   A O   
6829 O  O   . HOH   E .   ? 0.2026 0.2503 0.2241 0.0138  -0.0123 -0.0333 1454 HOH   A O   
6830 O  O   . HOH   E .   ? 0.1802 0.2113 0.5332 -0.0264 -0.0991 0.0658  1455 HOH   A O   
6831 O  O   . HOH   E .   ? 0.5595 0.5424 0.4865 -0.0225 0.0623  0.2271  1456 HOH   A O   
6832 O  O   . HOH   E .   ? 0.6629 0.7154 0.4054 0.2562  -0.0940 0.1538  1457 HOH   A O   
6833 O  O   A HOH   E .   ? 0.2694 0.2142 0.2984 0.0687  0.1161  0.1282  1458 HOH   A O   
6834 O  O   . HOH   E .   ? 0.6395 0.2679 0.3959 0.0501  0.0255  0.0875  1459 HOH   A O   
6835 O  O   . HOH   E .   ? 0.2258 0.2326 0.3185 0.0254  -0.0358 0.0150  1460 HOH   A O   
6836 O  O   B HOH   E .   ? 0.1761 0.2570 0.2038 -0.0146 -0.0634 0.0256  1461 HOH   A O   
6837 O  O   . HOH   E .   ? 0.5040 0.3164 0.4657 0.0808  0.0966  -0.0072 1462 HOH   A O   
6838 O  O   . HOH   E .   ? 0.6612 0.5474 0.4774 -0.0830 0.1468  0.0507  1463 HOH   A O   
6839 O  O   . HOH   E .   ? 0.2648 0.2759 0.3248 -0.0581 0.0363  -0.0689 1464 HOH   A O   
6840 O  O   . HOH   E .   ? 0.2803 0.4847 0.5141 -0.1270 0.0785  -0.1435 1465 HOH   A O   
6841 O  O   . HOH   E .   ? 0.5937 0.7206 0.4349 0.0375  -0.1153 -0.0758 1466 HOH   A O   
6842 O  O   . HOH   E .   ? 0.3184 0.4192 0.3679 0.0443  -0.1151 0.0394  1467 HOH   A O   
6843 O  O   B HOH   E .   ? 0.3656 0.2029 0.3012 0.1155  0.0480  0.0583  1468 HOH   A O   
6844 O  O   . HOH   E .   ? 0.2653 0.3374 0.3377 -0.0183 -0.0477 0.0234  1469 HOH   A O   
6845 O  O   . HOH   E .   ? 0.6554 0.3465 0.7791 0.0912  0.1093  0.2381  1470 HOH   A O   
6846 O  O   . HOH   E .   ? 0.2343 0.2582 0.3276 -0.0730 0.0394  -0.0165 1471 HOH   A O   
6847 O  O   A HOH   E .   ? 0.2469 0.2035 0.4567 0.0622  -0.1673 -0.0669 1472 HOH   A O   
6848 O  O   . HOH   E .   ? 0.6360 0.5182 0.5466 0.1587  0.2489  0.2636  1473 HOH   A O   
6849 O  O   . HOH   E .   ? 0.3142 0.5238 0.3090 -0.0011 -0.0036 -0.0116 1474 HOH   A O   
6850 O  O   . HOH   E .   ? 0.4292 0.5692 0.4052 -0.0944 -0.0626 0.2220  1475 HOH   A O   
6851 O  O   . HOH   E .   ? 0.2929 0.3615 0.4816 0.0519  0.0381  -0.1678 1476 HOH   A O   
6852 O  O   . HOH   E .   ? 0.2567 0.2179 0.3557 0.0132  0.0387  -0.0045 1477 HOH   A O   
6853 O  O   . HOH   E .   ? 0.2788 0.1591 0.2245 0.0304  -0.0874 -0.0183 1478 HOH   A O   
6854 O  O   . HOH   E .   ? 0.5512 0.4941 0.4060 0.0027  0.1080  0.0626  1479 HOH   A O   
6855 O  O   . HOH   E .   ? 0.2256 0.2157 0.2295 0.0108  -0.0099 0.0203  1480 HOH   A O   
6856 O  O   . HOH   E .   ? 0.4462 0.3967 0.5092 -0.1844 -0.0660 0.0026  1481 HOH   A O   
6857 O  O   . HOH   E .   ? 0.5846 0.6884 0.5118 -0.1499 -0.0975 0.0450  1482 HOH   A O   
6858 O  O   . HOH   E .   ? 0.5843 0.4210 0.6381 -0.0725 -0.0304 0.0602  1483 HOH   A O   
6859 O  O   . HOH   E .   ? 0.5134 0.5454 0.4198 0.1152  -0.1259 -0.1038 1484 HOH   A O   
6860 O  O   . HOH   E .   ? 0.5385 0.4017 0.3938 0.0314  0.0396  -0.1342 1485 HOH   A O   
6861 O  O   . HOH   E .   ? 0.4030 0.4397 0.2523 -0.0135 0.0024  0.0081  1486 HOH   A O   
6862 O  O   . HOH   E .   ? 0.3107 0.4056 0.2780 -0.0107 -0.0287 -0.0690 1487 HOH   A O   
6863 O  O   . HOH   E .   ? 0.4665 0.2408 0.3328 -0.0696 -0.1279 0.0777  1488 HOH   A O   
6864 O  O   . HOH   E .   ? 0.7544 0.3843 0.2929 -0.0771 -0.0504 -0.0168 1489 HOH   A O   
6865 O  O   . HOH   E .   ? 0.6695 0.5142 0.4065 -0.0296 -0.1082 -0.0603 1490 HOH   A O   
6866 O  O   . HOH   E .   ? 0.4612 0.4339 0.3481 -0.0743 -0.0404 -0.0247 1491 HOH   A O   
6867 O  O   B HOH   E .   ? 0.1699 0.2005 0.3122 0.0479  -0.0014 0.0963  1492 HOH   A O   
6868 O  O   . HOH   E .   ? 0.5554 0.3814 0.4478 -0.0407 0.1406  -0.0149 1493 HOH   A O   
6869 O  O   . HOH   E .   ? 0.2453 0.3886 0.4131 0.0001  0.0698  0.1263  1494 HOH   A O   
6870 O  O   . HOH   E .   ? 0.2573 0.5202 0.3575 0.1196  0.0905  0.2401  1495 HOH   A O   
6871 O  O   . HOH   E .   ? 0.5573 0.6177 0.3997 -0.0372 0.1180  0.0835  1496 HOH   A O   
6872 O  O   . HOH   E .   ? 0.5386 0.3509 0.2342 -0.0655 0.1647  -0.0308 1497 HOH   A O   
6873 O  O   B HOH   E .   ? 0.3872 0.4612 0.4972 -0.0909 -0.0799 -0.0847 1498 HOH   A O   
6874 O  O   . HOH   E .   ? 0.4711 0.3001 0.4624 -0.0180 0.2234  -0.0051 1499 HOH   A O   
6875 O  O   B HOH   E .   ? 0.3067 0.3375 0.4034 -0.0574 0.0155  -0.0787 1500 HOH   A O   
6876 O  O   . HOH   E .   ? 0.2496 0.2518 0.6886 -0.0102 -0.1122 0.0263  1501 HOH   A O   
6877 O  O   . HOH   E .   ? 0.5413 0.5781 0.6595 0.1034  0.2060  -0.1156 1502 HOH   A O   
6878 O  O   . HOH   E .   ? 0.4792 0.4528 0.4916 -0.0418 -0.1121 0.0551  1503 HOH   A O   
6879 O  O   . HOH   E .   ? 0.2860 0.2051 0.5950 0.0182  0.0649  0.1116  1504 HOH   A O   
6880 O  O   . HOH   E .   ? 0.3485 0.2847 0.4230 -0.0758 0.0669  0.0527  1505 HOH   A O   
6881 O  O   . HOH   E .   ? 0.2251 0.3894 0.4903 0.0036  0.0895  -0.1014 1506 HOH   A O   
6882 O  O   . HOH   E .   ? 0.3844 0.7230 0.5500 -0.0911 -0.0442 0.3215  1507 HOH   A O   
6883 O  O   . HOH   E .   ? 0.6664 0.2506 0.4590 -0.0416 0.0973  0.0858  1508 HOH   A O   
6884 O  O   . HOH   E .   ? 0.2251 0.2675 0.3751 0.0233  -0.0459 0.0558  1509 HOH   A O   
6885 O  O   . HOH   E .   ? 0.4501 0.2690 0.4412 -0.1479 0.0199  0.0644  1510 HOH   A O   
6886 O  O   . HOH   E .   ? 0.5236 0.7482 0.4753 0.0876  -0.0904 0.1196  1511 HOH   A O   
6887 O  O   B HOH   E .   ? 0.3806 0.4817 0.4023 0.1466  0.1170  -0.0931 1512 HOH   A O   
6888 O  O   . HOH   E .   ? 0.2720 0.4668 0.3811 0.0873  0.0327  0.0786  1513 HOH   A O   
6889 O  O   B HOH   E .   ? 0.4513 0.3448 0.4312 0.0739  -0.0504 -0.0410 1514 HOH   A O   
6890 O  O   . HOH   E .   ? 0.7544 0.5964 0.6351 -0.0760 0.0932  -0.0614 1515 HOH   A O   
6891 O  O   . HOH   E .   ? 0.2756 0.7447 0.3687 0.0154  0.0918  -0.0001 1516 HOH   A O   
6892 O  O   . HOH   E .   ? 0.5953 0.5842 0.4869 0.0847  -0.1467 0.0124  1517 HOH   A O   
6893 O  O   . HOH   E .   ? 0.5069 0.6030 0.4607 0.2569  0.0053  0.0892  1518 HOH   A O   
6894 O  O   . HOH   E .   ? 0.2633 0.2181 0.4654 0.0076  0.0467  0.0566  1519 HOH   A O   
6895 O  O   . HOH   E .   ? 0.4039 0.4711 0.4346 0.0658  -0.0624 -0.1173 1520 HOH   A O   
6896 O  O   . HOH   E .   ? 0.2471 0.6803 0.2857 0.0547  -0.0047 0.0184  1521 HOH   A O   
6897 O  O   . HOH   E .   ? 0.4694 0.4697 0.3443 0.1478  -0.0594 0.0849  1522 HOH   A O   
6898 O  O   . HOH   E .   ? 0.4315 0.5718 0.5146 -0.0782 -0.0526 0.0086  1523 HOH   A O   
6899 O  O   . HOH   E .   ? 0.3032 0.3675 0.5175 -0.0277 -0.0953 0.2314  1524 HOH   A O   
6900 O  O   . HOH   F .   ? 0.2212 0.2199 0.2874 0.0283  0.0766  0.0360  201  HOH   B O   
6901 O  O   . HOH   F .   ? 0.3901 0.3803 0.4832 -0.1417 0.0352  0.0757  202  HOH   B O   
6902 O  O   . HOH   F .   ? 0.6009 0.5794 0.2200 0.1179  -0.0438 -0.1199 203  HOH   B O   
6903 O  O   . HOH   F .   ? 0.3453 0.4291 0.4961 -0.0949 0.0247  -0.1600 204  HOH   B O   
6904 O  O   . HOH   F .   ? 0.3279 0.2936 0.6867 -0.0306 0.0913  -0.0551 205  HOH   B O   
6905 O  O   . HOH   F .   ? 0.3378 0.7221 0.3460 0.1326  0.0184  0.2084  206  HOH   B O   
6906 O  O   . HOH   F .   ? 0.4116 0.2860 0.3326 -0.0842 0.0155  -0.0828 207  HOH   B O   
6907 O  O   . HOH   F .   ? 0.4476 0.5796 0.3427 0.2632  -0.1080 -0.0165 208  HOH   B O   
6908 O  O   . HOH   F .   ? 0.5974 0.3021 0.4058 -0.1804 0.0521  0.0318  209  HOH   B O   
6909 O  O   . HOH   F .   ? 0.2961 0.5388 0.5082 0.0088  0.1671  -0.1652 210  HOH   B O   
6910 O  O   . HOH   F .   ? 0.5323 0.4054 0.5804 0.0662  -0.0923 0.2524  211  HOH   B O   
6911 O  O   . HOH   F .   ? 0.6705 0.5789 0.5153 0.2087  0.0112  0.0184  212  HOH   B O   
6912 O  O   . HOH   F .   ? 0.7410 0.3326 0.4858 0.1073  0.1289  -0.0467 213  HOH   B O   
6913 O  O   . HOH   F .   ? 0.3024 0.1974 0.5021 0.0215  0.1899  0.0862  214  HOH   B O   
6914 O  O   . HOH   F .   ? 0.2814 0.2844 0.6650 0.0810  -0.1256 0.0112  215  HOH   B O   
6915 O  O   . HOH   F .   ? 0.4108 0.4415 0.3812 -0.0570 -0.1112 0.0832  216  HOH   B O   
6916 O  O   . HOH   F .   ? 0.1844 0.2221 0.2521 0.0083  0.0185  -0.0157 217  HOH   B O   
6917 O  O   . HOH   F .   ? 0.1497 0.1876 0.2449 -0.0187 -0.0038 0.0063  218  HOH   B O   
6918 O  O   . HOH   F .   ? 0.3031 0.5414 0.4301 0.1913  -0.0046 -0.0979 219  HOH   B O   
6919 O  O   . HOH   F .   ? 0.3666 0.5053 0.4205 0.2127  -0.0561 0.0157  220  HOH   B O   
6920 O  O   . HOH   F .   ? 0.4137 0.4415 0.6358 -0.0403 -0.1494 -0.1079 221  HOH   B O   
6921 O  O   . HOH   F .   ? 0.4627 0.1943 0.3205 -0.0049 -0.0983 0.0061  222  HOH   B O   
6922 O  O   . HOH   F .   ? 0.4204 0.4210 0.3885 0.0254  0.0864  -0.1456 223  HOH   B O   
6923 O  O   . HOH   F .   ? 0.2968 0.2140 0.4270 0.0017  0.1547  0.0160  224  HOH   B O   
6924 O  O   . HOH   F .   ? 0.3647 0.3244 0.2152 0.0304  0.0661  0.0512  225  HOH   B O   
6925 O  O   . HOH   F .   ? 0.1675 0.2001 0.2837 -0.0132 0.0072  -0.0177 226  HOH   B O   
6926 O  O   . HOH   F .   ? 0.2138 0.2046 0.3514 -0.0308 -0.0190 -0.0564 227  HOH   B O   
6927 O  O   . HOH   F .   ? 0.3797 0.6745 0.3279 0.2412  0.0050  -0.0027 228  HOH   B O   
6928 O  O   . HOH   F .   ? 0.2427 0.1701 0.2623 -0.0271 0.1115  -0.0009 229  HOH   B O   
6929 O  O   . HOH   F .   ? 0.5747 0.5978 0.3053 0.0719  -0.0387 -0.0339 230  HOH   B O   
6930 O  O   . HOH   F .   ? 0.3110 0.3066 0.5618 0.0268  0.0755  0.0177  231  HOH   B O   
6931 O  O   . HOH   F .   ? 0.3918 0.3182 0.4682 0.1257  -0.1255 -0.0251 232  HOH   B O   
6932 O  O   . HOH   F .   ? 0.2068 0.2313 0.2668 -0.0581 -0.0011 -0.0179 233  HOH   B O   
6933 O  O   . HOH   F .   ? 0.2553 0.2493 0.2862 0.0368  0.0218  -0.0841 234  HOH   B O   
6934 O  O   . HOH   F .   ? 0.2121 0.4015 0.2849 -0.0593 -0.0419 -0.0652 235  HOH   B O   
6935 O  O   . HOH   F .   ? 0.2458 0.4045 0.3356 -0.0802 0.0405  -0.0758 236  HOH   B O   
6936 O  O   . HOH   F .   ? 0.7131 0.4390 0.5734 0.2023  -0.0227 -0.1317 237  HOH   B O   
6937 O  O   . HOH   F .   ? 0.1395 0.1318 0.1401 -0.0113 -0.0014 -0.0003 238  HOH   B O   
6938 O  O   . HOH   F .   ? 0.2832 0.5439 0.3139 -0.1255 -0.0306 -0.1060 239  HOH   B O   
6939 O  O   . HOH   F .   ? 0.2082 0.1250 0.3421 0.0140  -0.0587 -0.0249 240  HOH   B O   
6940 O  O   . HOH   F .   ? 0.2958 0.1695 0.5770 -0.0045 -0.1474 -0.0419 241  HOH   B O   
6941 O  O   . HOH   F .   ? 0.3404 0.1787 0.1797 0.0240  -0.0674 -0.0118 242  HOH   B O   
6942 O  O   . HOH   F .   ? 0.1475 0.1446 0.2409 -0.0036 0.0080  -0.0126 243  HOH   B O   
6943 O  O   . HOH   F .   ? 0.3020 0.4474 0.4688 -0.0228 -0.1034 0.1695  244  HOH   B O   
6944 O  O   . HOH   F .   ? 0.6079 0.3174 0.2195 -0.0017 0.0615  -0.0295 245  HOH   B O   
6945 O  O   . HOH   F .   ? 0.3353 0.3813 0.4154 0.0878  -0.0842 -0.1876 246  HOH   B O   
6946 O  O   . HOH   F .   ? 0.2094 0.1951 0.1949 -0.0280 -0.0426 0.0021  247  HOH   B O   
6947 O  O   . HOH   F .   ? 0.4489 0.2891 0.4139 -0.2053 0.0276  -0.0104 248  HOH   B O   
6948 O  O   . HOH   F .   ? 0.1356 0.1282 0.1449 -0.0015 -0.0008 0.0050  249  HOH   B O   
6949 O  O   . HOH   F .   ? 0.2899 0.2427 0.2782 -0.0369 0.0282  -0.0492 250  HOH   B O   
6950 O  O   . HOH   F .   ? 0.2177 0.2043 0.1605 0.0118  0.0008  0.0069  251  HOH   B O   
6951 O  O   . HOH   F .   ? 0.3962 0.2373 0.3920 0.0929  -0.0478 -0.0735 252  HOH   B O   
6952 O  O   . HOH   F .   ? 0.2964 0.2291 0.2709 0.1047  0.0952  0.0178  253  HOH   B O   
6953 O  O   . HOH   F .   ? 0.1995 0.3609 0.2109 -0.0337 -0.0097 0.0538  254  HOH   B O   
6954 O  O   . HOH   F .   ? 0.1511 0.1626 0.2603 -0.0170 -0.0154 0.0052  255  HOH   B O   
6955 O  O   . HOH   F .   ? 0.3002 0.3618 0.1856 0.0548  0.0624  0.0120  256  HOH   B O   
6956 O  O   . HOH   F .   ? 0.2184 0.2952 0.2235 -0.0448 0.0310  0.0637  257  HOH   B O   
6957 O  O   . HOH   F .   ? 0.2014 0.1430 0.1978 -0.0296 -0.0358 0.0309  258  HOH   B O   
6958 O  O   . HOH   F .   ? 0.2312 0.2143 0.2473 0.0807  -0.0824 -0.0755 259  HOH   B O   
6959 O  O   . HOH   F .   ? 0.2616 0.4884 0.5177 0.0654  0.0725  -0.0677 260  HOH   B O   
6960 O  O   . HOH   F .   ? 0.2045 0.1857 0.3487 0.0077  -0.0428 -0.0422 261  HOH   B O   
6961 O  O   . HOH   F .   ? 0.5395 0.6254 0.2435 0.0433  -0.0422 0.0846  262  HOH   B O   
6962 O  O   . HOH   F .   ? 0.1296 0.1627 0.1970 -0.0083 0.0087  0.0140  263  HOH   B O   
6963 O  O   . HOH   F .   ? 0.2200 0.2027 0.1694 0.0142  0.0006  0.0022  264  HOH   B O   
6964 O  O   . HOH   F .   ? 0.1936 0.3795 0.4762 -0.0255 -0.0404 -0.1611 265  HOH   B O   
6965 O  O   . HOH   F .   ? 0.4201 0.4834 0.4314 0.0379  -0.1556 -0.0060 266  HOH   B O   
6966 O  O   . HOH   F .   ? 0.1782 0.2585 0.2513 0.0500  0.0439  0.0970  267  HOH   B O   
6967 O  O   . HOH   F .   ? 0.2583 0.3685 0.4334 0.1160  -0.0432 -0.0525 268  HOH   B O   
6968 O  O   . HOH   F .   ? 0.2514 0.1849 0.2760 -0.0663 0.0268  -0.0022 269  HOH   B O   
6969 O  O   . HOH   F .   ? 0.1959 0.1454 0.2086 -0.0245 -0.0114 0.0077  270  HOH   B O   
6970 O  O   . HOH   F .   ? 0.1779 0.1733 0.1511 -0.0415 -0.0392 0.0170  271  HOH   B O   
6971 O  O   . HOH   F .   ? 0.1668 0.1388 0.3563 -0.0083 -0.0195 0.0008  272  HOH   B O   
6972 O  O   . HOH   F .   ? 0.2405 0.2989 0.2109 0.1105  -0.0303 -0.0291 273  HOH   B O   
6973 O  O   . HOH   F .   ? 0.3997 0.3293 0.4426 0.0046  -0.1326 -0.0711 274  HOH   B O   
6974 O  O   . HOH   F .   ? 0.2459 0.2540 0.2180 -0.0461 -0.0615 -0.0373 275  HOH   B O   
6975 O  O   . HOH   F .   ? 0.2385 0.3844 0.3307 0.0317  0.0912  0.0249  276  HOH   B O   
6976 O  O   . HOH   F .   ? 0.4883 0.3040 0.2479 0.0405  -0.0117 -0.0864 277  HOH   B O   
6977 O  O   . HOH   F .   ? 0.2437 0.2815 0.2222 -0.0377 -0.0790 0.0164  278  HOH   B O   
6978 O  O   . HOH   F .   ? 0.4002 0.3069 0.5014 -0.0797 0.0519  0.1079  279  HOH   B O   
6979 O  O   . HOH   F .   ? 0.3295 0.6532 0.3222 0.2032  -0.0447 0.0622  280  HOH   B O   
6980 O  O   . HOH   F .   ? 0.2249 0.3153 0.3082 -0.0257 0.0340  -0.0933 281  HOH   B O   
6981 O  O   . HOH   F .   ? 0.4118 0.3812 0.4018 -0.0973 0.1275  -0.1362 282  HOH   B O   
6982 O  O   . HOH   F .   ? 0.3293 0.4145 0.5320 -0.0413 0.1513  -0.0221 283  HOH   B O   
6983 O  O   . HOH   F .   ? 0.1515 0.1490 0.3030 -0.0146 0.0098  -0.0080 284  HOH   B O   
6984 O  O   . HOH   F .   ? 0.2701 0.6327 0.7474 0.1453  -0.0454 -0.1001 285  HOH   B O   
6985 O  O   . HOH   F .   ? 0.1552 0.2075 0.1326 -0.0165 -0.0141 0.0043  286  HOH   B O   
6986 O  O   . HOH   F .   ? 0.1607 0.1471 0.1573 0.0048  0.0098  0.0020  287  HOH   B O   
6987 O  O   . HOH   F .   ? 0.3514 0.2639 0.1883 0.0529  -0.0818 -0.0202 288  HOH   B O   
6988 O  O   . HOH   F .   ? 0.2585 0.4739 0.5045 -0.0929 -0.1044 0.1480  289  HOH   B O   
6989 O  O   . HOH   F .   ? 0.1625 0.1829 0.2532 0.0202  -0.0107 -0.0035 290  HOH   B O   
6990 O  O   . HOH   F .   ? 0.2349 0.2606 0.2535 0.0246  -0.0749 0.0137  291  HOH   B O   
6991 O  O   . HOH   F .   ? 0.2680 0.2087 0.5030 0.0199  0.0477  0.0451  292  HOH   B O   
6992 O  O   . HOH   F .   ? 0.2814 0.2900 0.2650 -0.0059 0.0141  -0.1284 293  HOH   B O   
6993 O  O   . HOH   F .   ? 0.3615 0.2136 0.4165 -0.0910 -0.2083 0.0675  294  HOH   B O   
6994 O  O   . HOH   F .   ? 0.2245 0.3133 0.4137 -0.0242 -0.1162 0.0796  295  HOH   B O   
6995 O  O   . HOH   F .   ? 0.3562 0.3578 0.4366 0.1343  -0.0780 -0.0796 296  HOH   B O   
6996 O  O   . HOH   F .   ? 0.1718 0.3062 0.4346 0.0218  -0.0155 -0.1225 297  HOH   B O   
6997 O  O   . HOH   F .   ? 0.1640 0.1532 0.2097 0.0051  0.0006  0.0115  298  HOH   B O   
6998 O  O   . HOH   F .   ? 0.2380 0.6505 0.2495 0.0462  -0.0226 -0.0617 299  HOH   B O   
6999 O  O   . HOH   F .   ? 0.2882 0.3151 0.4146 -0.1125 0.1074  -0.0683 300  HOH   B O   
7000 O  O   . HOH   F .   ? 0.2049 0.2772 0.6367 0.0480  -0.0539 -0.1060 301  HOH   B O   
7001 O  O   . HOH   F .   ? 0.5579 0.2788 0.2318 -0.2029 0.0748  -0.0312 302  HOH   B O   
7002 O  O   . HOH   F .   ? 0.2626 0.2869 0.3308 -0.0334 0.0974  -0.0778 303  HOH   B O   
7003 O  O   . HOH   F .   ? 0.3205 0.1888 0.3226 0.0762  0.0868  0.0384  304  HOH   B O   
7004 O  O   . HOH   F .   ? 0.4198 0.4544 0.1616 -0.0101 0.0500  0.0263  305  HOH   B O   
7005 O  O   . HOH   F .   ? 0.4620 0.3652 0.2227 0.1158  -0.0740 0.0513  306  HOH   B O   
7006 O  O   . HOH   F .   ? 0.4235 0.4830 0.2287 0.1488  -0.0742 -0.0491 307  HOH   B O   
7007 O  O   . HOH   F .   ? 0.1995 0.1469 0.2529 -0.0188 -0.0268 -0.0008 308  HOH   B O   
7008 O  O   . HOH   F .   ? 0.4024 0.4010 0.5863 0.0678  -0.0067 0.0781  309  HOH   B O   
7009 O  O   . HOH   F .   ? 0.5949 0.4974 0.4904 -0.1267 -0.0202 0.1215  310  HOH   B O   
7010 O  O   . HOH   F .   ? 0.2854 0.2735 0.5895 -0.0355 -0.0962 0.1283  311  HOH   B O   
7011 O  O   . HOH   F .   ? 0.5733 0.3570 0.2946 0.2514  0.0777  0.0641  312  HOH   B O   
7012 O  O   . HOH   F .   ? 0.3800 0.2266 0.2722 0.1468  0.1114  0.0354  313  HOH   B O   
7013 O  O   . HOH   F .   ? 0.1497 0.1454 0.2724 0.0059  -0.0010 -0.0116 314  HOH   B O   
7014 O  O   . HOH   F .   ? 0.1568 0.1856 0.2554 -0.0326 -0.0092 0.0136  315  HOH   B O   
7015 O  O   . HOH   F .   ? 0.2001 0.1506 0.3100 0.0273  -0.0942 -0.0050 316  HOH   B O   
7016 O  O   . HOH   F .   ? 0.2039 0.2914 0.4951 -0.0123 -0.0404 -0.0212 317  HOH   B O   
7017 O  O   . HOH   F .   ? 0.2205 0.1437 0.2381 -0.0157 -0.0155 0.0255  318  HOH   B O   
7018 O  O   . HOH   F .   ? 0.6822 0.4910 0.4521 0.1667  0.0756  0.0470  319  HOH   B O   
7019 O  O   . HOH   F .   ? 0.2051 0.1910 0.1748 -0.0038 0.0324  0.0247  320  HOH   B O   
7020 O  O   . HOH   F .   ? 0.1469 0.1615 0.2695 -0.0106 -0.0093 -0.0084 321  HOH   B O   
7021 O  O   . HOH   F .   ? 0.4277 0.3107 0.5076 0.0887  0.2142  0.1727  322  HOH   B O   
7022 O  O   . HOH   F .   ? 0.6116 0.6176 0.5662 0.3070  0.0228  -0.0230 323  HOH   B O   
7023 O  O   . HOH   F .   ? 0.1507 0.2856 0.2346 -0.0117 -0.0212 0.0712  324  HOH   B O   
7024 O  O   . HOH   F .   ? 0.4559 0.3949 0.2350 0.0355  -0.0484 -0.0389 325  HOH   B O   
7025 O  O   . HOH   F .   ? 0.2968 0.4154 0.7097 -0.0453 -0.1050 0.2271  326  HOH   B O   
7026 O  O   . HOH   F .   ? 0.1791 0.3007 0.2902 0.0287  -0.0058 -0.0747 327  HOH   B O   
7027 O  O   . HOH   F .   ? 0.2624 0.2128 0.2098 0.0245  -0.0206 0.0238  328  HOH   B O   
7028 O  O   . HOH   F .   ? 0.6679 0.3417 0.3526 0.0119  0.1368  0.1188  329  HOH   B O   
7029 O  O   . HOH   F .   ? 0.2038 0.5574 0.5379 -0.0681 -0.0135 -0.0658 330  HOH   B O   
7030 O  O   . HOH   F .   ? 0.1843 0.2002 0.2788 0.0360  0.0386  0.0235  331  HOH   B O   
7031 O  O   . HOH   F .   ? 0.4692 0.5618 0.3441 0.0397  -0.1017 0.0558  332  HOH   B O   
7032 O  O   . HOH   F .   ? 0.2110 0.2212 0.5150 -0.0448 0.0165  0.1256  333  HOH   B O   
7033 O  O   . HOH   F .   ? 0.2429 0.1899 0.5404 0.0008  0.0118  0.0280  334  HOH   B O   
7034 O  O   . HOH   F .   ? 0.4639 0.2394 0.3281 0.0521  0.0759  0.0948  335  HOH   B O   
7035 O  O   . HOH   F .   ? 0.5487 0.4915 0.6005 0.1094  -0.0614 0.2007  336  HOH   B O   
7036 O  O   . HOH   F .   ? 0.5443 0.3275 0.3720 0.0329  0.0780  -0.1281 337  HOH   B O   
7037 O  O   . HOH   F .   ? 0.7682 0.1951 0.2829 0.0122  -0.0708 0.0027  338  HOH   B O   
7038 O  O   . HOH   F .   ? 0.5028 0.3849 0.5951 0.0109  -0.0608 -0.1487 339  HOH   B O   
7039 O  O   . HOH   F .   ? 0.1599 0.1454 0.2107 0.0072  -0.0128 0.0083  340  HOH   B O   
7040 O  O   . HOH   F .   ? 0.5710 0.2855 0.2727 0.0418  -0.1312 -0.0395 341  HOH   B O   
7041 O  O   . HOH   F .   ? 0.3957 0.6980 0.3237 0.0322  -0.0406 0.1312  342  HOH   B O   
7042 O  O   . HOH   F .   ? 0.1921 0.6466 0.6255 0.0120  0.0014  0.1305  343  HOH   B O   
7043 O  O   . HOH   F .   ? 0.3838 0.6310 0.3627 -0.0659 -0.0906 -0.0775 344  HOH   B O   
7044 O  O   . HOH   F .   ? 0.4293 0.3990 0.5206 0.0198  -0.1109 0.0669  345  HOH   B O   
7045 O  O   . HOH   F .   ? 0.5895 0.6809 0.2763 -0.0317 -0.0300 0.1404  346  HOH   B O   
7046 O  O   . HOH   F .   ? 0.1979 0.1905 0.2549 -0.0054 0.0524  -0.0108 347  HOH   B O   
7047 O  O   . HOH   F .   ? 0.2619 0.2145 0.5335 -0.0122 -0.1068 -0.0707 348  HOH   B O   
7048 O  O   . HOH   F .   ? 0.4629 0.5740 0.4298 -0.1203 0.0039  0.1020  349  HOH   B O   
7049 O  O   . HOH   F .   ? 0.2183 0.3252 0.5172 0.0199  0.0415  0.0345  350  HOH   B O   
7050 O  O   . HOH   F .   ? 0.2516 0.6175 0.3024 0.1696  -0.0609 -0.1426 351  HOH   B O   
7051 O  O   . HOH   F .   ? 0.3473 0.2187 0.3171 -0.0641 -0.0165 -0.0714 352  HOH   B O   
7052 O  O   . HOH   F .   ? 0.4273 0.5855 0.6238 0.0237  -0.0131 -0.1278 353  HOH   B O   
7053 O  O   . HOH   F .   ? 0.3335 0.4331 0.4684 -0.1557 0.0155  -0.0189 354  HOH   B O   
7054 O  O   . HOH   F .   ? 0.4738 0.3271 0.5232 -0.1252 0.1817  0.0247  355  HOH   B O   
7055 O  O   . HOH   F .   ? 0.5455 0.3567 0.3982 0.0744  0.1500  -0.0396 356  HOH   B O   
7056 O  O   . HOH   F .   ? 0.3345 0.2812 0.4149 -0.0924 0.0127  -0.0905 357  HOH   B O   
7057 O  O   . HOH   F .   ? 0.3246 0.1879 0.3750 0.0522  -0.1337 -0.0471 358  HOH   B O   
7058 O  O   . HOH   F .   ? 0.4507 0.4728 0.4856 -0.0718 -0.0340 -0.0359 359  HOH   B O   
7059 O  O   . HOH   F .   ? 0.4328 0.5439 0.5446 0.1908  -0.1200 0.1530  360  HOH   B O   
7060 O  O   . HOH   F .   ? 0.4306 0.3487 0.4242 0.0185  -0.1640 -0.0350 361  HOH   B O   
7061 O  O   . HOH   F .   ? 0.4059 0.6428 0.3300 0.2302  0.0331  0.0630  362  HOH   B O   
7062 O  O   . HOH   F .   ? 0.2164 0.3713 0.6725 -0.0706 -0.0594 -0.0817 363  HOH   B O   
7063 O  O   . HOH   F .   ? 0.5333 0.3851 0.6341 0.0034  0.1031  0.1177  364  HOH   B O   
7064 O  O   . HOH   F .   ? 0.5890 0.4679 0.4035 0.1633  0.1045  0.0799  365  HOH   B O   
7065 O  O   . HOH   F .   ? 0.4528 0.2955 0.5543 -0.1287 -0.0794 0.0298  366  HOH   B O   
7066 O  O   . HOH   F .   ? 0.5669 0.5308 0.3216 0.1901  -0.1523 -0.0021 367  HOH   B O   
7067 O  O   . HOH   F .   ? 0.6136 0.4200 0.4512 0.1655  -0.1180 0.0278  368  HOH   B O   
7068 O  O   . HOH   F .   ? 0.6849 0.7476 0.4832 0.2784  -0.1183 0.1657  369  HOH   B O   
7069 O  O   . HOH   F .   ? 0.5082 0.2937 0.3863 0.0803  -0.1618 -0.0460 370  HOH   B O   
7070 O  O   . HOH   F .   ? 0.4569 0.5998 0.5581 0.3021  0.0665  0.0770  371  HOH   B O   
7071 O  O   . HOH   F .   ? 0.5949 0.2156 0.3262 -0.0020 0.0776  0.0389  372  HOH   B O   
7072 O  O   . HOH   F .   ? 0.5390 0.5175 0.4153 -0.0620 -0.0675 -0.1064 373  HOH   B O   
7073 O  O   . HOH   F .   ? 0.3107 0.3372 0.1963 0.0561  0.0178  0.0126  374  HOH   B O   
7074 O  O   . HOH   F .   ? 0.2309 0.4086 0.4260 0.0461  -0.0680 -0.0655 375  HOH   B O   
7075 O  O   . HOH   F .   ? 0.6133 0.4200 0.2794 -0.0735 -0.1052 -0.0838 376  HOH   B O   
7076 O  O   . HOH   F .   ? 0.4389 0.4677 0.5008 -0.0941 -0.0796 0.0775  377  HOH   B O   
7077 O  O   . HOH   F .   ? 0.4466 0.7030 0.5914 0.1637  0.0936  0.3143  378  HOH   B O   
7078 O  O   . HOH   F .   ? 0.8068 0.3736 0.5653 -0.1250 -0.0633 -0.0392 379  HOH   B O   
7079 O  O   . HOH   F .   ? 0.5183 0.6900 0.3332 -0.1335 0.0430  -0.1538 380  HOH   B O   
7080 O  O   . HOH   F .   ? 0.3130 0.5011 0.4999 0.1136  -0.0654 0.0144  381  HOH   B O   
7081 O  O   . HOH   F .   ? 0.2720 0.2484 0.3331 0.0051  0.0027  0.0420  382  HOH   B O   
7082 O  O   . HOH   F .   ? 0.4822 0.8549 0.6019 0.0261  0.2692  0.1015  383  HOH   B O   
7083 O  O   . HOH   F .   ? 0.4883 0.6561 0.5777 0.0359  0.2428  0.1236  384  HOH   B O   
7084 O  O   . HOH   F .   ? 0.7554 0.3689 0.4327 0.1258  0.0609  -0.0749 385  HOH   B O   
7085 O  O   . HOH   F .   ? 0.7601 0.6001 0.4097 0.1996  0.0015  0.0141  386  HOH   B O   
7086 O  O   . HOH   F .   ? 0.2152 0.4248 0.3689 -0.0830 -0.0664 -0.0372 387  HOH   B O   
7087 O  O   . HOH   F .   ? 0.6250 0.4198 0.5315 -0.0839 0.0183  -0.0160 388  HOH   B O   
7088 O  O   . HOH   F .   ? 0.4288 0.3602 0.2875 0.0140  0.0460  -0.0217 389  HOH   B O   
7089 O  O   . HOH   F .   ? 0.5893 0.4485 0.3624 -0.0183 -0.0864 -0.0556 390  HOH   B O   
7090 O  O   . HOH   F .   ? 0.3895 0.2187 0.2884 0.0844  -0.0097 0.0285  391  HOH   B O   
7091 O  O   . HOH   F .   ? 0.4981 0.4152 0.2971 0.0157  0.0213  0.0634  392  HOH   B O   
7092 O  O   . HOH   F .   ? 0.4394 0.2067 0.5783 -0.0531 0.1010  0.0332  393  HOH   B O   
7093 O  O   . HOH   F .   ? 0.2330 0.4880 0.6236 -0.1440 -0.0544 -0.0246 394  HOH   B O   
7094 O  O   . HOH   F .   ? 0.4364 0.4062 0.4304 0.0110  0.1200  0.0692  395  HOH   B O   
7095 O  O   . HOH   F .   ? 0.3113 0.3665 0.3227 0.0491  0.0153  -0.0406 396  HOH   B O   
7096 O  O   . HOH   F .   ? 0.4044 0.5453 0.3266 0.0936  -0.0431 -0.1099 397  HOH   B O   
7097 O  O   . HOH   F .   ? 0.1984 0.3113 0.5307 -0.0522 -0.0823 -0.0015 398  HOH   B O   
7098 O  O   . HOH   F .   ? 0.6134 0.6126 0.7157 0.1738  -0.0734 0.1908  399  HOH   B O   
7099 O  O   . HOH   F .   ? 0.5236 0.4394 0.3046 -0.2118 -0.0088 0.1318  400  HOH   B O   
7100 O  O   . HOH   F .   ? 0.5860 0.6248 0.3598 0.1833  -0.0100 0.0128  401  HOH   B O   
# 
