data_7HF5
# 
_entry.id   7HF5 
# 
_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   7HF5         pdb_00007hf5 10.2210/pdb7hf5/pdb 
WWPDB D_1001407395 ?            ?                   
# 
_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                        7HF5 
_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-1-[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-2-ol' 220.271   2   ?                      ? 
? ?                                                                                    
3 non-polymer syn 'CHLORIDE ION'                                                            35.453    1   ?                      ? 
? ?                                                                                    
4 water       nat water                                                                     18.015    428 ?                      ? 
? ?                                                                                    
# 
_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-1-[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-2-ol' A1BAS 
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 
A1BAS non-polymer         . '2-methyl-1-[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-2-ol' ? 'C11 H16 N4 O'   220.271 
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 A1BAS 1   201  201  A1BAS LA1 A . 
D 2 A1BAS 1   202  301  A1BAS LA2 A . 
E 3 CL    1   203  1    CL    CL  A . 
F 4 HOH   1   1301 1301 HOH   HOH A . 
F 4 HOH   2   1302 1289 HOH   HOH A . 
F 4 HOH   3   1303 196  HOH   HOH A . 
F 4 HOH   4   1304 86   HOH   HOH A . 
F 4 HOH   5   1305 209  HOH   HOH A . 
F 4 HOH   6   1306 85   HOH   HOH A . 
F 4 HOH   7   1307 625  HOH   HOH A . 
F 4 HOH   8   1308 105  HOH   HOH A . 
F 4 HOH   9   1309 337  HOH   HOH A . 
F 4 HOH   10  1310 1310 HOH   HOH A . 
F 4 HOH   11  1311 1283 HOH   HOH A . 
F 4 HOH   12  1312 109  HOH   HOH A . 
F 4 HOH   13  1313 292  HOH   HOH A . 
F 4 HOH   14  1314 1313 HOH   HOH A . 
F 4 HOH   15  1315 76   HOH   HOH A . 
F 4 HOH   16  1316 964  HOH   HOH A . 
F 4 HOH   17  1317 124  HOH   HOH A . 
F 4 HOH   18  1318 151  HOH   HOH A . 
F 4 HOH   19  1319 236  HOH   HOH A . 
F 4 HOH   20  1320 136  HOH   HOH A . 
F 4 HOH   21  1321 247  HOH   HOH A . 
F 4 HOH   22  1322 229  HOH   HOH A . 
F 4 HOH   23  1323 662  HOH   HOH A . 
F 4 HOH   24  1324 661  HOH   HOH A . 
F 4 HOH   25  1325 140  HOH   HOH A . 
F 4 HOH   26  1326 15   HOH   HOH A . 
F 4 HOH   27  1327 630  HOH   HOH A . 
F 4 HOH   28  1328 241  HOH   HOH A . 
F 4 HOH   29  1329 49   HOH   HOH A . 
F 4 HOH   30  1330 6    HOH   HOH A . 
F 4 HOH   31  1331 320  HOH   HOH A . 
F 4 HOH   32  1332 164  HOH   HOH A . 
F 4 HOH   33  1333 5    HOH   HOH A . 
F 4 HOH   34  1334 225  HOH   HOH A . 
F 4 HOH   35  1335 148  HOH   HOH A . 
F 4 HOH   36  1336 165  HOH   HOH A . 
F 4 HOH   37  1337 192  HOH   HOH A . 
F 4 HOH   38  1338 393  HOH   HOH A . 
F 4 HOH   39  1339 42   HOH   HOH A . 
F 4 HOH   40  1340 469  HOH   HOH A . 
F 4 HOH   41  1341 93   HOH   HOH A . 
F 4 HOH   42  1342 21   HOH   HOH A . 
F 4 HOH   43  1343 33   HOH   HOH A . 
F 4 HOH   44  1344 56   HOH   HOH A . 
F 4 HOH   45  1345 396  HOH   HOH A . 
F 4 HOH   46  1346 1300 HOH   HOH A . 
F 4 HOH   47  1347 1295 HOH   HOH A . 
F 4 HOH   48  1348 26   HOH   HOH A . 
F 4 HOH   49  1349 92   HOH   HOH A . 
F 4 HOH   50  1350 66   HOH   HOH A . 
F 4 HOH   51  1351 405  HOH   HOH A . 
F 4 HOH   52  1352 3    HOH   HOH A . 
F 4 HOH   53  1353 36   HOH   HOH A . 
F 4 HOH   54  1354 493  HOH   HOH A . 
F 4 HOH   55  1355 218  HOH   HOH A . 
F 4 HOH   56  1356 2    HOH   HOH A . 
F 4 HOH   57  1357 102  HOH   HOH A . 
F 4 HOH   58  1358 354  HOH   HOH A . 
F 4 HOH   59  1359 14   HOH   HOH A . 
F 4 HOH   60  1360 333  HOH   HOH A . 
F 4 HOH   61  1361 939  HOH   HOH A . 
F 4 HOH   62  1362 81   HOH   HOH A . 
F 4 HOH   63  1363 5    HOH   HOH A . 
F 4 HOH   64  1364 169  HOH   HOH A . 
F 4 HOH   65  1365 12   HOH   HOH A . 
F 4 HOH   66  1366 19   HOH   HOH A . 
F 4 HOH   67  1367 45   HOH   HOH A . 
F 4 HOH   68  1368 155  HOH   HOH A . 
F 4 HOH   69  1369 162  HOH   HOH A . 
F 4 HOH   70  1370 57   HOH   HOH A . 
F 4 HOH   71  1371 139  HOH   HOH A . 
F 4 HOH   72  1372 1275 HOH   HOH A . 
F 4 HOH   73  1373 46   HOH   HOH A . 
F 4 HOH   74  1374 4    HOH   HOH A . 
F 4 HOH   75  1375 34   HOH   HOH A . 
F 4 HOH   76  1376 1296 HOH   HOH A . 
F 4 HOH   77  1377 138  HOH   HOH A . 
F 4 HOH   78  1378 39   HOH   HOH A . 
F 4 HOH   79  1379 27   HOH   HOH A . 
F 4 HOH   80  1380 159  HOH   HOH A . 
F 4 HOH   81  1381 18   HOH   HOH A . 
F 4 HOH   82  1382 96   HOH   HOH A . 
F 4 HOH   83  1383 78   HOH   HOH A . 
F 4 HOH   84  1384 17   HOH   HOH A . 
F 4 HOH   85  1385 1308 HOH   HOH A . 
F 4 HOH   86  1386 134  HOH   HOH A . 
F 4 HOH   87  1387 154  HOH   HOH A . 
F 4 HOH   88  1388 115  HOH   HOH A . 
F 4 HOH   89  1389 186  HOH   HOH A . 
F 4 HOH   90  1390 35   HOH   HOH A . 
F 4 HOH   91  1391 10   HOH   HOH A . 
F 4 HOH   92  1392 366  HOH   HOH A . 
F 4 HOH   93  1393 351  HOH   HOH A . 
F 4 HOH   94  1394 9    HOH   HOH A . 
F 4 HOH   95  1395 116  HOH   HOH A . 
F 4 HOH   96  1396 199  HOH   HOH A . 
F 4 HOH   97  1397 582  HOH   HOH A . 
F 4 HOH   98  1398 58   HOH   HOH A . 
F 4 HOH   99  1399 8    HOH   HOH A . 
F 4 HOH   100 1400 122  HOH   HOH A . 
F 4 HOH   101 1401 121  HOH   HOH A . 
F 4 HOH   102 1402 83   HOH   HOH A . 
F 4 HOH   103 1403 1315 HOH   HOH A . 
F 4 HOH   104 1404 21   HOH   HOH A . 
F 4 HOH   105 1405 296  HOH   HOH A . 
F 4 HOH   106 1406 1309 HOH   HOH A . 
F 4 HOH   107 1407 132  HOH   HOH A . 
F 4 HOH   108 1408 24   HOH   HOH A . 
F 4 HOH   109 1409 67   HOH   HOH A . 
F 4 HOH   110 1410 25   HOH   HOH A . 
F 4 HOH   111 1411 123  HOH   HOH A . 
F 4 HOH   112 1412 397  HOH   HOH A . 
F 4 HOH   113 1413 3    HOH   HOH A . 
F 4 HOH   114 1414 68   HOH   HOH A . 
F 4 HOH   115 1415 1068 HOH   HOH A . 
F 4 HOH   116 1416 74   HOH   HOH A . 
F 4 HOH   117 1417 6    HOH   HOH A . 
F 4 HOH   118 1418 1290 HOH   HOH A . 
F 4 HOH   119 1419 461  HOH   HOH A . 
F 4 HOH   120 1420 409  HOH   HOH A . 
F 4 HOH   121 1421 4    HOH   HOH A . 
F 4 HOH   122 1422 19   HOH   HOH A . 
F 4 HOH   123 1423 156  HOH   HOH A . 
F 4 HOH   124 1424 53   HOH   HOH A . 
F 4 HOH   125 1425 381  HOH   HOH A . 
F 4 HOH   126 1426 153  HOH   HOH A . 
F 4 HOH   127 1427 195  HOH   HOH A . 
F 4 HOH   128 1428 303  HOH   HOH A . 
F 4 HOH   129 1429 278  HOH   HOH A . 
F 4 HOH   130 1430 95   HOH   HOH A . 
F 4 HOH   131 1431 281  HOH   HOH A . 
F 4 HOH   132 1432 51   HOH   HOH A . 
F 4 HOH   133 1433 7    HOH   HOH A . 
F 4 HOH   134 1434 125  HOH   HOH A . 
F 4 HOH   135 1435 1238 HOH   HOH A . 
F 4 HOH   136 1436 212  HOH   HOH A . 
F 4 HOH   137 1437 1279 HOH   HOH A . 
F 4 HOH   138 1438 12   HOH   HOH A . 
F 4 HOH   139 1439 16   HOH   HOH A . 
F 4 HOH   140 1440 73   HOH   HOH A . 
F 4 HOH   141 1441 1222 HOH   HOH A . 
F 4 HOH   142 1442 71   HOH   HOH A . 
F 4 HOH   143 1443 70   HOH   HOH A . 
F 4 HOH   144 1444 7    HOH   HOH A . 
F 4 HOH   145 1445 40   HOH   HOH A . 
F 4 HOH   146 1446 80   HOH   HOH A . 
F 4 HOH   147 1447 944  HOH   HOH A . 
F 4 HOH   148 1448 1189 HOH   HOH A . 
F 4 HOH   149 1449 94   HOH   HOH A . 
F 4 HOH   150 1450 576  HOH   HOH A . 
F 4 HOH   151 1451 15   HOH   HOH A . 
F 4 HOH   152 1452 97   HOH   HOH A . 
F 4 HOH   153 1453 1094 HOH   HOH A . 
F 4 HOH   154 1454 104  HOH   HOH A . 
F 4 HOH   155 1455 1119 HOH   HOH A . 
F 4 HOH   156 1456 188  HOH   HOH A . 
F 4 HOH   157 1457 952  HOH   HOH A . 
F 4 HOH   158 1458 79   HOH   HOH A . 
F 4 HOH   159 1459 330  HOH   HOH A . 
F 4 HOH   160 1460 1134 HOH   HOH A . 
F 4 HOH   161 1461 1286 HOH   HOH A . 
F 4 HOH   162 1462 18   HOH   HOH A . 
F 4 HOH   163 1463 107  HOH   HOH A . 
F 4 HOH   164 1464 2    HOH   HOH A . 
F 4 HOH   165 1465 509  HOH   HOH A . 
F 4 HOH   166 1466 163  HOH   HOH A . 
F 4 HOH   167 1467 726  HOH   HOH A . 
F 4 HOH   168 1468 13   HOH   HOH A . 
F 4 HOH   169 1469 756  HOH   HOH A . 
F 4 HOH   170 1470 1299 HOH   HOH A . 
F 4 HOH   171 1471 408  HOH   HOH A . 
F 4 HOH   172 1472 280  HOH   HOH A . 
F 4 HOH   173 1473 17   HOH   HOH A . 
F 4 HOH   174 1474 801  HOH   HOH A . 
F 4 HOH   175 1475 319  HOH   HOH A . 
F 4 HOH   176 1476 126  HOH   HOH A . 
F 4 HOH   177 1477 361  HOH   HOH A . 
F 4 HOH   178 1478 556  HOH   HOH A . 
F 4 HOH   179 1479 1307 HOH   HOH A . 
F 4 HOH   180 1480 63   HOH   HOH A . 
F 4 HOH   181 1481 250  HOH   HOH A . 
F 4 HOH   182 1482 16   HOH   HOH A . 
F 4 HOH   183 1483 342  HOH   HOH A . 
F 4 HOH   184 1484 1276 HOH   HOH A . 
F 4 HOH   185 1485 202  HOH   HOH A . 
F 4 HOH   186 1486 1306 HOH   HOH A . 
F 4 HOH   187 1487 20   HOH   HOH A . 
F 4 HOH   188 1488 1284 HOH   HOH A . 
F 4 HOH   189 1489 1287 HOH   HOH A . 
F 4 HOH   190 1490 695  HOH   HOH A . 
F 4 HOH   191 1491 521  HOH   HOH A . 
F 4 HOH   192 1492 919  HOH   HOH A . 
F 4 HOH   193 1493 674  HOH   HOH A . 
F 4 HOH   194 1494 370  HOH   HOH A . 
F 4 HOH   195 1495 224  HOH   HOH A . 
F 4 HOH   196 1496 135  HOH   HOH A . 
F 4 HOH   197 1497 267  HOH   HOH A . 
F 4 HOH   198 1498 309  HOH   HOH A . 
F 4 HOH   199 1499 318  HOH   HOH A . 
F 4 HOH   200 1500 208  HOH   HOH A . 
F 4 HOH   201 1501 711  HOH   HOH A . 
F 4 HOH   202 1502 331  HOH   HOH A . 
F 4 HOH   203 1503 315  HOH   HOH A . 
F 4 HOH   204 1504 1314 HOH   HOH A . 
F 4 HOH   205 1505 263  HOH   HOH A . 
F 4 HOH   206 1506 152  HOH   HOH A . 
F 4 HOH   207 1507 805  HOH   HOH A . 
F 4 HOH   208 1508 941  HOH   HOH A . 
F 4 HOH   209 1509 11   HOH   HOH A . 
F 4 HOH   210 1510 8    HOH   HOH A . 
F 4 HOH   211 1511 1071 HOH   HOH A . 
F 4 HOH   212 1512 180  HOH   HOH A . 
F 4 HOH   213 1513 356  HOH   HOH A . 
F 4 HOH   214 1514 350  HOH   HOH A . 
F 4 HOH   215 1515 371  HOH   HOH A . 
F 4 HOH   216 1516 363  HOH   HOH A . 
F 4 HOH   217 1517 313  HOH   HOH A . 
F 4 HOH   218 1518 326  HOH   HOH A . 
F 4 HOH   219 1519 185  HOH   HOH A . 
F 4 HOH   220 1520 429  HOH   HOH A . 
F 4 HOH   221 1521 772  HOH   HOH A . 
F 4 HOH   222 1522 376  HOH   HOH A . 
F 4 HOH   223 1523 1074 HOH   HOH A . 
F 4 HOH   224 1524 22   HOH   HOH A . 
F 4 HOH   225 1525 1292 HOH   HOH A . 
F 4 HOH   226 1526 346  HOH   HOH A . 
F 4 HOH   227 1527 1078 HOH   HOH A . 
G 4 HOH   1   201  64   HOH   HOH B . 
G 4 HOH   2   202  240  HOH   HOH B . 
G 4 HOH   3   203  531  HOH   HOH B . 
G 4 HOH   4   204  364  HOH   HOH B . 
G 4 HOH   5   205  358  HOH   HOH B . 
G 4 HOH   6   206  549  HOH   HOH B . 
G 4 HOH   7   207  1249 HOH   HOH B . 
G 4 HOH   8   208  232  HOH   HOH B . 
G 4 HOH   9   209  654  HOH   HOH B . 
G 4 HOH   10  210  398  HOH   HOH B . 
G 4 HOH   11  211  758  HOH   HOH B . 
G 4 HOH   12  212  900  HOH   HOH B . 
G 4 HOH   13  213  264  HOH   HOH B . 
G 4 HOH   14  214  743  HOH   HOH B . 
G 4 HOH   15  215  120  HOH   HOH B . 
G 4 HOH   16  216  353  HOH   HOH B . 
G 4 HOH   17  217  50   HOH   HOH B . 
G 4 HOH   18  218  452  HOH   HOH B . 
G 4 HOH   19  219  276  HOH   HOH B . 
G 4 HOH   20  220  82   HOH   HOH B . 
G 4 HOH   21  221  332  HOH   HOH B . 
G 4 HOH   22  222  131  HOH   HOH B . 
G 4 HOH   23  223  54   HOH   HOH B . 
G 4 HOH   24  224  1140 HOH   HOH B . 
G 4 HOH   25  225  444  HOH   HOH B . 
G 4 HOH   26  226  723  HOH   HOH B . 
G 4 HOH   27  227  1278 HOH   HOH B . 
G 4 HOH   28  228  75   HOH   HOH B . 
G 4 HOH   29  229  166  HOH   HOH B . 
G 4 HOH   30  230  110  HOH   HOH B . 
G 4 HOH   31  231  127  HOH   HOH B . 
G 4 HOH   32  232  1312 HOH   HOH B . 
G 4 HOH   33  233  205  HOH   HOH B . 
G 4 HOH   34  234  181  HOH   HOH B . 
G 4 HOH   35  235  282  HOH   HOH B . 
G 4 HOH   36  236  272  HOH   HOH B . 
G 4 HOH   37  237  128  HOH   HOH B . 
G 4 HOH   38  238  60   HOH   HOH B . 
G 4 HOH   39  239  343  HOH   HOH B . 
G 4 HOH   40  240  1    HOH   HOH B . 
G 4 HOH   41  241  69   HOH   HOH B . 
G 4 HOH   42  242  325  HOH   HOH B . 
G 4 HOH   43  243  300  HOH   HOH B . 
G 4 HOH   44  244  133  HOH   HOH B . 
G 4 HOH   45  245  72   HOH   HOH B . 
G 4 HOH   46  246  144  HOH   HOH B . 
G 4 HOH   47  247  9    HOH   HOH B . 
G 4 HOH   48  248  52   HOH   HOH B . 
G 4 HOH   49  249  129  HOH   HOH B . 
G 4 HOH   50  250  31   HOH   HOH B . 
G 4 HOH   51  251  14   HOH   HOH B . 
G 4 HOH   52  252  30   HOH   HOH B . 
G 4 HOH   53  253  231  HOH   HOH B . 
G 4 HOH   54  254  41   HOH   HOH B . 
G 4 HOH   55  255  47   HOH   HOH B . 
G 4 HOH   56  256  150  HOH   HOH B . 
G 4 HOH   57  257  252  HOH   HOH B . 
G 4 HOH   58  258  175  HOH   HOH B . 
G 4 HOH   59  259  62   HOH   HOH B . 
G 4 HOH   60  260  103  HOH   HOH B . 
G 4 HOH   61  261  172  HOH   HOH B . 
G 4 HOH   62  262  271  HOH   HOH B . 
G 4 HOH   63  263  143  HOH   HOH B . 
G 4 HOH   64  264  10   HOH   HOH B . 
G 4 HOH   65  265  287  HOH   HOH B . 
G 4 HOH   66  266  20   HOH   HOH B . 
G 4 HOH   67  267  61   HOH   HOH B . 
G 4 HOH   68  268  347  HOH   HOH B . 
G 4 HOH   69  269  391  HOH   HOH B . 
G 4 HOH   70  270  221  HOH   HOH B . 
G 4 HOH   71  271  117  HOH   HOH B . 
G 4 HOH   72  272  416  HOH   HOH B . 
G 4 HOH   73  273  59   HOH   HOH B . 
G 4 HOH   74  274  11   HOH   HOH B . 
G 4 HOH   75  275  114  HOH   HOH B . 
G 4 HOH   76  276  77   HOH   HOH B . 
G 4 HOH   77  277  84   HOH   HOH B . 
G 4 HOH   78  278  243  HOH   HOH B . 
G 4 HOH   79  279  242  HOH   HOH B . 
G 4 HOH   80  280  43   HOH   HOH B . 
G 4 HOH   81  281  1277 HOH   HOH B . 
G 4 HOH   82  282  1106 HOH   HOH B . 
G 4 HOH   83  283  22   HOH   HOH B . 
G 4 HOH   84  284  635  HOH   HOH B . 
G 4 HOH   85  285  302  HOH   HOH B . 
G 4 HOH   86  286  89   HOH   HOH B . 
G 4 HOH   87  287  106  HOH   HOH B . 
G 4 HOH   88  288  13   HOH   HOH B . 
G 4 HOH   89  289  147  HOH   HOH B . 
G 4 HOH   90  290  88   HOH   HOH B . 
G 4 HOH   91  291  316  HOH   HOH B . 
G 4 HOH   92  292  387  HOH   HOH B . 
G 4 HOH   93  293  1066 HOH   HOH B . 
G 4 HOH   94  294  137  HOH   HOH B . 
G 4 HOH   95  295  1305 HOH   HOH B . 
G 4 HOH   96  296  160  HOH   HOH B . 
G 4 HOH   97  297  235  HOH   HOH B . 
G 4 HOH   98  298  99   HOH   HOH B . 
G 4 HOH   99  299  297  HOH   HOH B . 
G 4 HOH   100 300  112  HOH   HOH B . 
G 4 HOH   101 301  101  HOH   HOH B . 
G 4 HOH   102 302  299  HOH   HOH B . 
G 4 HOH   103 303  311  HOH   HOH B . 
G 4 HOH   104 304  341  HOH   HOH B . 
G 4 HOH   105 305  142  HOH   HOH B . 
G 4 HOH   106 306  38   HOH   HOH B . 
G 4 HOH   107 307  1126 HOH   HOH B . 
G 4 HOH   108 308  37   HOH   HOH B . 
G 4 HOH   109 309  220  HOH   HOH B . 
G 4 HOH   110 310  216  HOH   HOH B . 
G 4 HOH   111 311  1285 HOH   HOH B . 
G 4 HOH   112 312  215  HOH   HOH B . 
G 4 HOH   113 313  48   HOH   HOH B . 
G 4 HOH   114 314  170  HOH   HOH B . 
G 4 HOH   115 315  1291 HOH   HOH B . 
G 4 HOH   116 316  704  HOH   HOH B . 
G 4 HOH   117 317  177  HOH   HOH B . 
G 4 HOH   118 318  32   HOH   HOH B . 
G 4 HOH   119 319  91   HOH   HOH B . 
G 4 HOH   120 320  23   HOH   HOH B . 
G 4 HOH   121 321  197  HOH   HOH B . 
G 4 HOH   122 322  44   HOH   HOH B . 
G 4 HOH   123 323  118  HOH   HOH B . 
G 4 HOH   124 324  28   HOH   HOH B . 
G 4 HOH   125 325  100  HOH   HOH B . 
G 4 HOH   126 326  141  HOH   HOH B . 
G 4 HOH   127 327  29   HOH   HOH B . 
G 4 HOH   128 328  334  HOH   HOH B . 
G 4 HOH   129 329  717  HOH   HOH B . 
G 4 HOH   130 330  1274 HOH   HOH B . 
G 4 HOH   131 331  55   HOH   HOH B . 
G 4 HOH   132 332  161  HOH   HOH B . 
G 4 HOH   133 333  98   HOH   HOH B . 
G 4 HOH   134 334  1294 HOH   HOH B . 
G 4 HOH   135 335  182  HOH   HOH B . 
G 4 HOH   136 336  65   HOH   HOH B . 
G 4 HOH   137 337  445  HOH   HOH B . 
G 4 HOH   138 338  234  HOH   HOH B . 
G 4 HOH   139 339  207  HOH   HOH B . 
G 4 HOH   140 340  619  HOH   HOH B . 
G 4 HOH   141 341  339  HOH   HOH B . 
G 4 HOH   142 342  1293 HOH   HOH B . 
G 4 HOH   143 343  362  HOH   HOH B . 
G 4 HOH   144 344  960  HOH   HOH B . 
G 4 HOH   145 345  178  HOH   HOH B . 
G 4 HOH   146 346  90   HOH   HOH B . 
G 4 HOH   147 347  463  HOH   HOH B . 
G 4 HOH   148 348  1046 HOH   HOH B . 
G 4 HOH   149 349  191  HOH   HOH B . 
G 4 HOH   150 350  304  HOH   HOH B . 
G 4 HOH   151 351  335  HOH   HOH B . 
G 4 HOH   152 352  1304 HOH   HOH B . 
G 4 HOH   153 353  623  HOH   HOH B . 
G 4 HOH   154 354  203  HOH   HOH B . 
G 4 HOH   155 355  1280 HOH   HOH B . 
G 4 HOH   156 356  87   HOH   HOH B . 
G 4 HOH   157 357  290  HOH   HOH B . 
G 4 HOH   158 358  541  HOH   HOH B . 
G 4 HOH   159 359  1077 HOH   HOH B . 
G 4 HOH   160 360  479  HOH   HOH B . 
G 4 HOH   161 361  389  HOH   HOH B . 
G 4 HOH   162 362  283  HOH   HOH B . 
G 4 HOH   163 363  718  HOH   HOH B . 
G 4 HOH   164 364  1072 HOH   HOH B . 
G 4 HOH   165 365  898  HOH   HOH B . 
G 4 HOH   166 366  1316 HOH   HOH B . 
G 4 HOH   167 367  615  HOH   HOH B . 
G 4 HOH   168 368  373  HOH   HOH B . 
G 4 HOH   169 369  340  HOH   HOH B . 
G 4 HOH   170 370  667  HOH   HOH B . 
G 4 HOH   171 371  291  HOH   HOH B . 
G 4 HOH   172 372  310  HOH   HOH B . 
G 4 HOH   173 373  1303 HOH   HOH B . 
G 4 HOH   174 374  190  HOH   HOH B . 
G 4 HOH   175 375  431  HOH   HOH B . 
G 4 HOH   176 376  1173 HOH   HOH B . 
G 4 HOH   177 377  149  HOH   HOH B . 
G 4 HOH   178 378  1000 HOH   HOH B . 
G 4 HOH   179 379  418  HOH   HOH B . 
G 4 HOH   180 380  183  HOH   HOH B . 
G 4 HOH   181 381  1163 HOH   HOH B . 
G 4 HOH   182 382  176  HOH   HOH B . 
G 4 HOH   183 383  1311 HOH   HOH B . 
G 4 HOH   184 384  424  HOH   HOH B . 
G 4 HOH   185 385  248  HOH   HOH B . 
G 4 HOH   186 386  470  HOH   HOH B . 
G 4 HOH   187 387  491  HOH   HOH B . 
G 4 HOH   188 388  265  HOH   HOH B . 
G 4 HOH   189 389  981  HOH   HOH B . 
G 4 HOH   190 390  184  HOH   HOH B . 
G 4 HOH   191 391  1298 HOH   HOH B . 
G 4 HOH   192 392  360  HOH   HOH B . 
G 4 HOH   193 393  410  HOH   HOH B . 
G 4 HOH   194 394  355  HOH   HOH B . 
G 4 HOH   195 395  314  HOH   HOH B . 
G 4 HOH   196 396  274  HOH   HOH B . 
G 4 HOH   197 397  566  HOH   HOH B . 
G 4 HOH   198 398  157  HOH   HOH B . 
G 4 HOH   199 399  321  HOH   HOH B . 
G 4 HOH   200 400  792  HOH   HOH B . 
G 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           7HF5 
_cell.length_a           88.670 
_cell.length_b           88.670 
_cell.length_c           39.512 
_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                         7HF5 
_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          7HF5 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.52 
_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   2023-07-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HF5 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.330 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   175735 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.045 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.200 
_reflns.B_iso_Wilson_estimate        12.260 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.049 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1098952 
_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 0.980 1.000  ? 29578 8396 ? 1.857 ? ? ? 3.500 ? 0.500  ? ? ? ? ? ? 96.900 2.178 1.103 0.318 
1 2 5.370 44.330 ? 8069  1167 ? 0.024 ? ? ? 6.900 ? 62.200 ? ? ? ? ? ? 99.900 0.026 0.010 0.999 
# 
_refine.entry_id                                 7HF5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             44.3300 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.6700 
_refine.ls_number_reflns_obs                     175440 
_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                          0.1522 
_refine.ls_R_factor_R_work                       0.1515 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1658 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8464 
_refine.ls_number_reflns_R_work                  166976 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.5444 
_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                            0.1300 
_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                                65.350 
_refine.B_iso_min                                9.120 
_refine.pdbx_overall_phase_error                 20.4200 
_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                       0.9800 
_refine_hist.d_res_low                        44.3300 
_refine_hist.pdbx_number_atoms_ligand         65 
_refine_hist.number_atoms_solvent             428 
_refine_hist.number_atoms_total               3035 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           19.25 
_refine_hist.pdbx_B_iso_mean_solvent          30.81 
_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 
0.9800 0.9900  30 93.0000  5136 . 0.4646 0.4548 . 275 0.0000 5411 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 99.0000  5438 . 0.4265 0.4132 . 274 0.0000 5712 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 100.0000 5592 . 0.3797 0.3482 . 276 0.0000 5868 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5559 . 0.3311 0.3264 . 246 0.0000 5805 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5590 . 0.3070 0.3104 . 304 0.0000 5894 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5493 . 0.2724 0.2709 . 307 0.0000 5800 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5534 . 0.2564 0.2570 . 305 0.0000 5839 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5533 . 0.2226 0.2356 . 261 0.0000 5794 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5606 . 0.2085 0.2190 . 280 0.0000 5886 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5559 . 0.1890 0.2287 . 288 0.0000 5847 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5569 . 0.1772 0.1789 . 258 0.0000 5827 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5575 . 0.1649 0.2063 . 260 0.0000 5835 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5561 . 0.1569 0.1843 . 295 0.0000 5856 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5497 . 0.1426 0.1709 . 305 0.0000 5802 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5666 . 0.1359 0.1595 . 246 0.0000 5912 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5552 . 0.1346 0.1515 . 271 0.0000 5823 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5524 . 0.1325 0.1520 . 292 0.0000 5816 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5570 . 0.1321 0.1554 . 300 0.0000 5870 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5563 . 0.1387 0.1675 . 299 0.0000 5862 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5651 . 0.1342 0.1695 . 244 0.0000 5895 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5554 . 0.1316 0.1461 . 304 0.0000 5858 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5578 . 0.1218 0.1470 . 265 0.0000 5843 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5606 . 0.1190 0.1261 . 303 0.0000 5909 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5559 . 0.1198 0.1339 . 277 0.0000 5836 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5612 . 0.1318 0.1486 . 260 0.0000 5872 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5589 . 0.1336 0.1367 . 306 0.0000 5895 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5640 . 0.1371 0.1442 . 284 0.0000 5924 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5596 . 0.1376 0.1397 . 306 0.0000 5902 . 'X-RAY DIFFRACTION' 
2.4200 3.0400  30 100.0000 5683 . 0.1481 0.1697 . 292 0.0000 5975 . 'X-RAY DIFFRACTION' 
3.0400 44.3300 30 100.0000 5791 . 0.1514 0.1700 . 281 0.0000 6072 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HF5 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003758' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HF5 
_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 2 ? 
E N N 3 ? 
F N N 4 ? 
G 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 7HF5 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HF5 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 7HF5 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HF5 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HF5 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HF5 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,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HF5 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 4   ? B -120.87 -158.68 
2 1 ASN A 15  ? A -141.59 -1.15   
3 1 HIS A 86  ? ? 55.45   -133.56 
4 1 SER A 128 ? B 70.32   -5.77   
5 1 HIS B 86  ? ? 58.06   -127.90 
# 
_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 1526 ? 5.87 . 
2 1 O ? A HOH 1527 ? 7.57 . 
3 1 O ? B HOH 401  ? 6.31 . 
# 
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 
A1BAS N2   N  Y N 1   
A1BAS C3   C  Y N 2   
A1BAS C6   C  Y N 3   
A1BAS C9   C  N N 4   
A1BAS C1   C  N N 5   
A1BAS C10  C  N N 6   
A1BAS C11  C  Y N 7   
A1BAS C2   C  Y N 8   
A1BAS C4   C  Y N 9   
A1BAS C5   C  Y N 10  
A1BAS C7   C  N N 11  
A1BAS C8   C  N N 12  
A1BAS N1   N  Y N 13  
A1BAS N3   N  Y N 14  
A1BAS N4   N  N N 15  
A1BAS O1   O  N N 16  
A1BAS H4   H  N N 17  
A1BAS H12  H  N N 18  
A1BAS H10  H  N N 19  
A1BAS H11  H  N N 20  
A1BAS H1   H  N N 21  
A1BAS H2   H  N N 22  
A1BAS H3   H  N N 23  
A1BAS H15  H  N N 24  
A1BAS H13  H  N N 25  
A1BAS H14  H  N N 26  
A1BAS H6   H  N N 27  
A1BAS H8   H  N N 28  
A1BAS H9   H  N N 29  
A1BAS H5   H  N N 30  
A1BAS H7   H  N N 31  
A1BAS H16  H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CL    CL   CL N N 106 
CYS   N    N  N N 107 
CYS   CA   C  N R 108 
CYS   C    C  N N 109 
CYS   O    O  N N 110 
CYS   CB   C  N N 111 
CYS   SG   S  N N 112 
CYS   OXT  O  N N 113 
CYS   H    H  N N 114 
CYS   H2   H  N N 115 
CYS   HA   H  N N 116 
CYS   HB2  H  N N 117 
CYS   HB3  H  N N 118 
CYS   HG   H  N N 119 
CYS   HXT  H  N N 120 
GLN   N    N  N N 121 
GLN   CA   C  N S 122 
GLN   C    C  N N 123 
GLN   O    O  N N 124 
GLN   CB   C  N N 125 
GLN   CG   C  N N 126 
GLN   CD   C  N N 127 
GLN   OE1  O  N N 128 
GLN   NE2  N  N N 129 
GLN   OXT  O  N N 130 
GLN   H    H  N N 131 
GLN   H2   H  N N 132 
GLN   HA   H  N N 133 
GLN   HB2  H  N N 134 
GLN   HB3  H  N N 135 
GLN   HG2  H  N N 136 
GLN   HG3  H  N N 137 
GLN   HE21 H  N N 138 
GLN   HE22 H  N N 139 
GLN   HXT  H  N N 140 
GLU   N    N  N N 141 
GLU   CA   C  N S 142 
GLU   C    C  N N 143 
GLU   O    O  N N 144 
GLU   CB   C  N N 145 
GLU   CG   C  N N 146 
GLU   CD   C  N N 147 
GLU   OE1  O  N N 148 
GLU   OE2  O  N N 149 
GLU   OXT  O  N N 150 
GLU   H    H  N N 151 
GLU   H2   H  N N 152 
GLU   HA   H  N N 153 
GLU   HB2  H  N N 154 
GLU   HB3  H  N N 155 
GLU   HG2  H  N N 156 
GLU   HG3  H  N N 157 
GLU   HE2  H  N N 158 
GLU   HXT  H  N N 159 
GLY   N    N  N N 160 
GLY   CA   C  N N 161 
GLY   C    C  N N 162 
GLY   O    O  N N 163 
GLY   OXT  O  N N 164 
GLY   H    H  N N 165 
GLY   H2   H  N N 166 
GLY   HA2  H  N N 167 
GLY   HA3  H  N N 168 
GLY   HXT  H  N N 169 
HIS   N    N  N N 170 
HIS   CA   C  N S 171 
HIS   C    C  N N 172 
HIS   O    O  N N 173 
HIS   CB   C  N N 174 
HIS   CG   C  Y N 175 
HIS   ND1  N  Y N 176 
HIS   CD2  C  Y N 177 
HIS   CE1  C  Y N 178 
HIS   NE2  N  Y N 179 
HIS   OXT  O  N N 180 
HIS   H    H  N N 181 
HIS   H2   H  N N 182 
HIS   HA   H  N N 183 
HIS   HB2  H  N N 184 
HIS   HB3  H  N N 185 
HIS   HD1  H  N N 186 
HIS   HD2  H  N N 187 
HIS   HE1  H  N N 188 
HIS   HE2  H  N N 189 
HIS   HXT  H  N N 190 
HOH   O    O  N N 191 
HOH   H1   H  N N 192 
HOH   H2   H  N N 193 
ILE   N    N  N N 194 
ILE   CA   C  N S 195 
ILE   C    C  N N 196 
ILE   O    O  N N 197 
ILE   CB   C  N S 198 
ILE   CG1  C  N N 199 
ILE   CG2  C  N N 200 
ILE   CD1  C  N N 201 
ILE   OXT  O  N N 202 
ILE   H    H  N N 203 
ILE   H2   H  N N 204 
ILE   HA   H  N N 205 
ILE   HB   H  N N 206 
ILE   HG12 H  N N 207 
ILE   HG13 H  N N 208 
ILE   HG21 H  N N 209 
ILE   HG22 H  N N 210 
ILE   HG23 H  N N 211 
ILE   HD11 H  N N 212 
ILE   HD12 H  N N 213 
ILE   HD13 H  N N 214 
ILE   HXT  H  N N 215 
LEU   N    N  N N 216 
LEU   CA   C  N S 217 
LEU   C    C  N N 218 
LEU   O    O  N N 219 
LEU   CB   C  N N 220 
LEU   CG   C  N N 221 
LEU   CD1  C  N N 222 
LEU   CD2  C  N N 223 
LEU   OXT  O  N N 224 
LEU   H    H  N N 225 
LEU   H2   H  N N 226 
LEU   HA   H  N N 227 
LEU   HB2  H  N N 228 
LEU   HB3  H  N N 229 
LEU   HG   H  N N 230 
LEU   HD11 H  N N 231 
LEU   HD12 H  N N 232 
LEU   HD13 H  N N 233 
LEU   HD21 H  N N 234 
LEU   HD22 H  N N 235 
LEU   HD23 H  N N 236 
LEU   HXT  H  N N 237 
LYS   N    N  N N 238 
LYS   CA   C  N S 239 
LYS   C    C  N N 240 
LYS   O    O  N N 241 
LYS   CB   C  N N 242 
LYS   CG   C  N N 243 
LYS   CD   C  N N 244 
LYS   CE   C  N N 245 
LYS   NZ   N  N N 246 
LYS   OXT  O  N N 247 
LYS   H    H  N N 248 
LYS   H2   H  N N 249 
LYS   HA   H  N N 250 
LYS   HB2  H  N N 251 
LYS   HB3  H  N N 252 
LYS   HG2  H  N N 253 
LYS   HG3  H  N N 254 
LYS   HD2  H  N N 255 
LYS   HD3  H  N N 256 
LYS   HE2  H  N N 257 
LYS   HE3  H  N N 258 
LYS   HZ1  H  N N 259 
LYS   HZ2  H  N N 260 
LYS   HZ3  H  N N 261 
LYS   HXT  H  N N 262 
MET   N    N  N N 263 
MET   CA   C  N S 264 
MET   C    C  N N 265 
MET   O    O  N N 266 
MET   CB   C  N N 267 
MET   CG   C  N N 268 
MET   SD   S  N N 269 
MET   CE   C  N N 270 
MET   OXT  O  N N 271 
MET   H    H  N N 272 
MET   H2   H  N N 273 
MET   HA   H  N N 274 
MET   HB2  H  N N 275 
MET   HB3  H  N N 276 
MET   HG2  H  N N 277 
MET   HG3  H  N N 278 
MET   HE1  H  N N 279 
MET   HE2  H  N N 280 
MET   HE3  H  N N 281 
MET   HXT  H  N N 282 
PHE   N    N  N N 283 
PHE   CA   C  N S 284 
PHE   C    C  N N 285 
PHE   O    O  N N 286 
PHE   CB   C  N N 287 
PHE   CG   C  Y N 288 
PHE   CD1  C  Y N 289 
PHE   CD2  C  Y N 290 
PHE   CE1  C  Y N 291 
PHE   CE2  C  Y N 292 
PHE   CZ   C  Y N 293 
PHE   OXT  O  N N 294 
PHE   H    H  N N 295 
PHE   H2   H  N N 296 
PHE   HA   H  N N 297 
PHE   HB2  H  N N 298 
PHE   HB3  H  N N 299 
PHE   HD1  H  N N 300 
PHE   HD2  H  N N 301 
PHE   HE1  H  N N 302 
PHE   HE2  H  N N 303 
PHE   HZ   H  N N 304 
PHE   HXT  H  N N 305 
PRO   N    N  N N 306 
PRO   CA   C  N S 307 
PRO   C    C  N N 308 
PRO   O    O  N N 309 
PRO   CB   C  N N 310 
PRO   CG   C  N N 311 
PRO   CD   C  N N 312 
PRO   OXT  O  N N 313 
PRO   H    H  N N 314 
PRO   HA   H  N N 315 
PRO   HB2  H  N N 316 
PRO   HB3  H  N N 317 
PRO   HG2  H  N N 318 
PRO   HG3  H  N N 319 
PRO   HD2  H  N N 320 
PRO   HD3  H  N N 321 
PRO   HXT  H  N N 322 
SER   N    N  N N 323 
SER   CA   C  N S 324 
SER   C    C  N N 325 
SER   O    O  N N 326 
SER   CB   C  N N 327 
SER   OG   O  N N 328 
SER   OXT  O  N N 329 
SER   H    H  N N 330 
SER   H2   H  N N 331 
SER   HA   H  N N 332 
SER   HB2  H  N N 333 
SER   HB3  H  N N 334 
SER   HG   H  N N 335 
SER   HXT  H  N N 336 
THR   N    N  N N 337 
THR   CA   C  N S 338 
THR   C    C  N N 339 
THR   O    O  N N 340 
THR   CB   C  N R 341 
THR   OG1  O  N N 342 
THR   CG2  C  N N 343 
THR   OXT  O  N N 344 
THR   H    H  N N 345 
THR   H2   H  N N 346 
THR   HA   H  N N 347 
THR   HB   H  N N 348 
THR   HG1  H  N N 349 
THR   HG21 H  N N 350 
THR   HG22 H  N N 351 
THR   HG23 H  N N 352 
THR   HXT  H  N N 353 
TYR   N    N  N N 354 
TYR   CA   C  N S 355 
TYR   C    C  N N 356 
TYR   O    O  N N 357 
TYR   CB   C  N N 358 
TYR   CG   C  Y N 359 
TYR   CD1  C  Y N 360 
TYR   CD2  C  Y N 361 
TYR   CE1  C  Y N 362 
TYR   CE2  C  Y N 363 
TYR   CZ   C  Y N 364 
TYR   OH   O  N N 365 
TYR   OXT  O  N N 366 
TYR   H    H  N N 367 
TYR   H2   H  N N 368 
TYR   HA   H  N N 369 
TYR   HB2  H  N N 370 
TYR   HB3  H  N N 371 
TYR   HD1  H  N N 372 
TYR   HD2  H  N N 373 
TYR   HE1  H  N N 374 
TYR   HE2  H  N N 375 
TYR   HH   H  N N 376 
TYR   HXT  H  N N 377 
VAL   N    N  N N 378 
VAL   CA   C  N S 379 
VAL   C    C  N N 380 
VAL   O    O  N N 381 
VAL   CB   C  N N 382 
VAL   CG1  C  N N 383 
VAL   CG2  C  N N 384 
VAL   OXT  O  N N 385 
VAL   H    H  N N 386 
VAL   H2   H  N N 387 
VAL   HA   H  N N 388 
VAL   HB   H  N N 389 
VAL   HG11 H  N N 390 
VAL   HG12 H  N N 391 
VAL   HG13 H  N N 392 
VAL   HG21 H  N N 393 
VAL   HG22 H  N N 394 
VAL   HG23 H  N N 395 
VAL   HXT  H  N N 396 
# 
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 
A1BAS C9  C8   sing N N 1   
A1BAS O1  C8   sing N N 2   
A1BAS C10 C8   sing N N 3   
A1BAS C8  C7   sing N N 4   
A1BAS C7  N4   sing N N 5   
A1BAS N4  C6   sing N N 6   
A1BAS C1  C2   sing N N 7   
A1BAS C6  C11  doub Y N 8   
A1BAS C6  N3   sing Y N 9   
A1BAS C2  C11  sing Y N 10  
A1BAS C2  C3   doub Y N 11  
A1BAS C11 C4   sing Y N 12  
A1BAS N3  C5   doub Y N 13  
A1BAS C3  N1   sing Y N 14  
A1BAS C5  N2   sing Y N 15  
A1BAS C4  N1   sing Y N 16  
A1BAS C4  N2   doub Y N 17  
A1BAS C3  H4   sing N N 18  
A1BAS C9  H12  sing N N 19  
A1BAS C9  H10  sing N N 20  
A1BAS C9  H11  sing N N 21  
A1BAS C1  H1   sing N N 22  
A1BAS C1  H2   sing N N 23  
A1BAS C1  H3   sing N N 24  
A1BAS C10 H15  sing N N 25  
A1BAS C10 H13  sing N N 26  
A1BAS C10 H14  sing N N 27  
A1BAS C5  H6   sing N N 28  
A1BAS C7  H8   sing N N 29  
A1BAS C7  H9   sing N N 30  
A1BAS N1  H5   sing N N 31  
A1BAS N4  H7   sing N N 32  
A1BAS O1  H16  sing N N 33  
ALA   N   CA   sing N N 34  
ALA   N   H    sing N N 35  
ALA   N   H2   sing N N 36  
ALA   CA  C    sing N N 37  
ALA   CA  CB   sing N N 38  
ALA   CA  HA   sing N N 39  
ALA   C   O    doub N N 40  
ALA   C   OXT  sing N N 41  
ALA   CB  HB1  sing N N 42  
ALA   CB  HB2  sing N N 43  
ALA   CB  HB3  sing N N 44  
ALA   OXT HXT  sing N N 45  
ARG   N   CA   sing N N 46  
ARG   N   H    sing N N 47  
ARG   N   H2   sing N N 48  
ARG   CA  C    sing N N 49  
ARG   CA  CB   sing N N 50  
ARG   CA  HA   sing N N 51  
ARG   C   O    doub N N 52  
ARG   C   OXT  sing N N 53  
ARG   CB  CG   sing N N 54  
ARG   CB  HB2  sing N N 55  
ARG   CB  HB3  sing N N 56  
ARG   CG  CD   sing N N 57  
ARG   CG  HG2  sing N N 58  
ARG   CG  HG3  sing N N 59  
ARG   CD  NE   sing N N 60  
ARG   CD  HD2  sing N N 61  
ARG   CD  HD3  sing N N 62  
ARG   NE  CZ   sing N N 63  
ARG   NE  HE   sing N N 64  
ARG   CZ  NH1  sing N N 65  
ARG   CZ  NH2  doub N N 66  
ARG   NH1 HH11 sing N N 67  
ARG   NH1 HH12 sing N N 68  
ARG   NH2 HH21 sing N N 69  
ARG   NH2 HH22 sing N N 70  
ARG   OXT HXT  sing N N 71  
ASN   N   CA   sing N N 72  
ASN   N   H    sing N N 73  
ASN   N   H2   sing N N 74  
ASN   CA  C    sing N N 75  
ASN   CA  CB   sing N N 76  
ASN   CA  HA   sing N N 77  
ASN   C   O    doub N N 78  
ASN   C   OXT  sing N N 79  
ASN   CB  CG   sing N N 80  
ASN   CB  HB2  sing N N 81  
ASN   CB  HB3  sing N N 82  
ASN   CG  OD1  doub N N 83  
ASN   CG  ND2  sing N N 84  
ASN   ND2 HD21 sing N N 85  
ASN   ND2 HD22 sing N N 86  
ASN   OXT HXT  sing N N 87  
ASP   N   CA   sing N N 88  
ASP   N   H    sing N N 89  
ASP   N   H2   sing N N 90  
ASP   CA  C    sing N N 91  
ASP   CA  CB   sing N N 92  
ASP   CA  HA   sing N N 93  
ASP   C   O    doub N N 94  
ASP   C   OXT  sing N N 95  
ASP   CB  CG   sing N N 96  
ASP   CB  HB2  sing N N 97  
ASP   CB  HB3  sing N N 98  
ASP   CG  OD1  doub N N 99  
ASP   CG  OD2  sing N N 100 
ASP   OD2 HD2  sing N N 101 
ASP   OXT HXT  sing N N 102 
CYS   N   CA   sing N N 103 
CYS   N   H    sing N N 104 
CYS   N   H2   sing N N 105 
CYS   CA  C    sing N N 106 
CYS   CA  CB   sing N N 107 
CYS   CA  HA   sing N N 108 
CYS   C   O    doub N N 109 
CYS   C   OXT  sing N N 110 
CYS   CB  SG   sing N N 111 
CYS   CB  HB2  sing N N 112 
CYS   CB  HB3  sing N N 113 
CYS   SG  HG   sing N N 114 
CYS   OXT HXT  sing N N 115 
GLN   N   CA   sing N N 116 
GLN   N   H    sing N N 117 
GLN   N   H2   sing N N 118 
GLN   CA  C    sing N N 119 
GLN   CA  CB   sing N N 120 
GLN   CA  HA   sing N N 121 
GLN   C   O    doub N N 122 
GLN   C   OXT  sing N N 123 
GLN   CB  CG   sing N N 124 
GLN   CB  HB2  sing N N 125 
GLN   CB  HB3  sing N N 126 
GLN   CG  CD   sing N N 127 
GLN   CG  HG2  sing N N 128 
GLN   CG  HG3  sing N N 129 
GLN   CD  OE1  doub N N 130 
GLN   CD  NE2  sing N N 131 
GLN   NE2 HE21 sing N N 132 
GLN   NE2 HE22 sing N N 133 
GLN   OXT HXT  sing N N 134 
GLU   N   CA   sing N N 135 
GLU   N   H    sing N N 136 
GLU   N   H2   sing N N 137 
GLU   CA  C    sing N N 138 
GLU   CA  CB   sing N N 139 
GLU   CA  HA   sing N N 140 
GLU   C   O    doub N N 141 
GLU   C   OXT  sing N N 142 
GLU   CB  CG   sing N N 143 
GLU   CB  HB2  sing N N 144 
GLU   CB  HB3  sing N N 145 
GLU   CG  CD   sing N N 146 
GLU   CG  HG2  sing N N 147 
GLU   CG  HG3  sing N N 148 
GLU   CD  OE1  doub N N 149 
GLU   CD  OE2  sing N N 150 
GLU   OE2 HE2  sing N N 151 
GLU   OXT HXT  sing N N 152 
GLY   N   CA   sing N N 153 
GLY   N   H    sing N N 154 
GLY   N   H2   sing N N 155 
GLY   CA  C    sing N N 156 
GLY   CA  HA2  sing N N 157 
GLY   CA  HA3  sing N N 158 
GLY   C   O    doub N N 159 
GLY   C   OXT  sing N N 160 
GLY   OXT HXT  sing N N 161 
HIS   N   CA   sing N N 162 
HIS   N   H    sing N N 163 
HIS   N   H2   sing N N 164 
HIS   CA  C    sing N N 165 
HIS   CA  CB   sing N N 166 
HIS   CA  HA   sing N N 167 
HIS   C   O    doub N N 168 
HIS   C   OXT  sing N N 169 
HIS   CB  CG   sing N N 170 
HIS   CB  HB2  sing N N 171 
HIS   CB  HB3  sing N N 172 
HIS   CG  ND1  sing Y N 173 
HIS   CG  CD2  doub Y N 174 
HIS   ND1 CE1  doub Y N 175 
HIS   ND1 HD1  sing N N 176 
HIS   CD2 NE2  sing Y N 177 
HIS   CD2 HD2  sing N N 178 
HIS   CE1 NE2  sing Y N 179 
HIS   CE1 HE1  sing N N 180 
HIS   NE2 HE2  sing N N 181 
HIS   OXT HXT  sing N N 182 
HOH   O   H1   sing N N 183 
HOH   O   H2   sing N N 184 
ILE   N   CA   sing N N 185 
ILE   N   H    sing N N 186 
ILE   N   H2   sing N N 187 
ILE   CA  C    sing N N 188 
ILE   CA  CB   sing N N 189 
ILE   CA  HA   sing N N 190 
ILE   C   O    doub N N 191 
ILE   C   OXT  sing N N 192 
ILE   CB  CG1  sing N N 193 
ILE   CB  CG2  sing N N 194 
ILE   CB  HB   sing N N 195 
ILE   CG1 CD1  sing N N 196 
ILE   CG1 HG12 sing N N 197 
ILE   CG1 HG13 sing N N 198 
ILE   CG2 HG21 sing N N 199 
ILE   CG2 HG22 sing N N 200 
ILE   CG2 HG23 sing N N 201 
ILE   CD1 HD11 sing N N 202 
ILE   CD1 HD12 sing N N 203 
ILE   CD1 HD13 sing N N 204 
ILE   OXT HXT  sing N N 205 
LEU   N   CA   sing N N 206 
LEU   N   H    sing N N 207 
LEU   N   H2   sing N N 208 
LEU   CA  C    sing N N 209 
LEU   CA  CB   sing N N 210 
LEU   CA  HA   sing N N 211 
LEU   C   O    doub N N 212 
LEU   C   OXT  sing N N 213 
LEU   CB  CG   sing N N 214 
LEU   CB  HB2  sing N N 215 
LEU   CB  HB3  sing N N 216 
LEU   CG  CD1  sing N N 217 
LEU   CG  CD2  sing N N 218 
LEU   CG  HG   sing N N 219 
LEU   CD1 HD11 sing N N 220 
LEU   CD1 HD12 sing N N 221 
LEU   CD1 HD13 sing N N 222 
LEU   CD2 HD21 sing N N 223 
LEU   CD2 HD22 sing N N 224 
LEU   CD2 HD23 sing N N 225 
LEU   OXT HXT  sing N N 226 
LYS   N   CA   sing N N 227 
LYS   N   H    sing N N 228 
LYS   N   H2   sing N N 229 
LYS   CA  C    sing N N 230 
LYS   CA  CB   sing N N 231 
LYS   CA  HA   sing N N 232 
LYS   C   O    doub N N 233 
LYS   C   OXT  sing N N 234 
LYS   CB  CG   sing N N 235 
LYS   CB  HB2  sing N N 236 
LYS   CB  HB3  sing N N 237 
LYS   CG  CD   sing N N 238 
LYS   CG  HG2  sing N N 239 
LYS   CG  HG3  sing N N 240 
LYS   CD  CE   sing N N 241 
LYS   CD  HD2  sing N N 242 
LYS   CD  HD3  sing N N 243 
LYS   CE  NZ   sing N N 244 
LYS   CE  HE2  sing N N 245 
LYS   CE  HE3  sing N N 246 
LYS   NZ  HZ1  sing N N 247 
LYS   NZ  HZ2  sing N N 248 
LYS   NZ  HZ3  sing N N 249 
LYS   OXT HXT  sing N N 250 
MET   N   CA   sing N N 251 
MET   N   H    sing N N 252 
MET   N   H2   sing N N 253 
MET   CA  C    sing N N 254 
MET   CA  CB   sing N N 255 
MET   CA  HA   sing N N 256 
MET   C   O    doub N N 257 
MET   C   OXT  sing N N 258 
MET   CB  CG   sing N N 259 
MET   CB  HB2  sing N N 260 
MET   CB  HB3  sing N N 261 
MET   CG  SD   sing N N 262 
MET   CG  HG2  sing N N 263 
MET   CG  HG3  sing N N 264 
MET   SD  CE   sing N N 265 
MET   CE  HE1  sing N N 266 
MET   CE  HE2  sing N N 267 
MET   CE  HE3  sing N N 268 
MET   OXT HXT  sing N N 269 
PHE   N   CA   sing N N 270 
PHE   N   H    sing N N 271 
PHE   N   H2   sing N N 272 
PHE   CA  C    sing N N 273 
PHE   CA  CB   sing N N 274 
PHE   CA  HA   sing N N 275 
PHE   C   O    doub N N 276 
PHE   C   OXT  sing N N 277 
PHE   CB  CG   sing N N 278 
PHE   CB  HB2  sing N N 279 
PHE   CB  HB3  sing N N 280 
PHE   CG  CD1  doub Y N 281 
PHE   CG  CD2  sing Y N 282 
PHE   CD1 CE1  sing Y N 283 
PHE   CD1 HD1  sing N N 284 
PHE   CD2 CE2  doub Y N 285 
PHE   CD2 HD2  sing N N 286 
PHE   CE1 CZ   doub Y N 287 
PHE   CE1 HE1  sing N N 288 
PHE   CE2 CZ   sing Y N 289 
PHE   CE2 HE2  sing N N 290 
PHE   CZ  HZ   sing N N 291 
PHE   OXT HXT  sing N N 292 
PRO   N   CA   sing N N 293 
PRO   N   CD   sing N N 294 
PRO   N   H    sing N N 295 
PRO   CA  C    sing N N 296 
PRO   CA  CB   sing N N 297 
PRO   CA  HA   sing N N 298 
PRO   C   O    doub N N 299 
PRO   C   OXT  sing N N 300 
PRO   CB  CG   sing N N 301 
PRO   CB  HB2  sing N N 302 
PRO   CB  HB3  sing N N 303 
PRO   CG  CD   sing N N 304 
PRO   CG  HG2  sing N N 305 
PRO   CG  HG3  sing N N 306 
PRO   CD  HD2  sing N N 307 
PRO   CD  HD3  sing N N 308 
PRO   OXT HXT  sing N N 309 
SER   N   CA   sing N N 310 
SER   N   H    sing N N 311 
SER   N   H2   sing N N 312 
SER   CA  C    sing N N 313 
SER   CA  CB   sing N N 314 
SER   CA  HA   sing N N 315 
SER   C   O    doub N N 316 
SER   C   OXT  sing N N 317 
SER   CB  OG   sing N N 318 
SER   CB  HB2  sing N N 319 
SER   CB  HB3  sing N N 320 
SER   OG  HG   sing N N 321 
SER   OXT HXT  sing N N 322 
THR   N   CA   sing N N 323 
THR   N   H    sing N N 324 
THR   N   H2   sing N N 325 
THR   CA  C    sing N N 326 
THR   CA  CB   sing N N 327 
THR   CA  HA   sing N N 328 
THR   C   O    doub N N 329 
THR   C   OXT  sing N N 330 
THR   CB  OG1  sing N N 331 
THR   CB  CG2  sing N N 332 
THR   CB  HB   sing N N 333 
THR   OG1 HG1  sing N N 334 
THR   CG2 HG21 sing N N 335 
THR   CG2 HG22 sing N N 336 
THR   CG2 HG23 sing N N 337 
THR   OXT HXT  sing N N 338 
TYR   N   CA   sing N N 339 
TYR   N   H    sing N N 340 
TYR   N   H2   sing N N 341 
TYR   CA  C    sing N N 342 
TYR   CA  CB   sing N N 343 
TYR   CA  HA   sing N N 344 
TYR   C   O    doub N N 345 
TYR   C   OXT  sing N N 346 
TYR   CB  CG   sing N N 347 
TYR   CB  HB2  sing N N 348 
TYR   CB  HB3  sing N N 349 
TYR   CG  CD1  doub Y N 350 
TYR   CG  CD2  sing Y N 351 
TYR   CD1 CE1  sing Y N 352 
TYR   CD1 HD1  sing N N 353 
TYR   CD2 CE2  doub Y N 354 
TYR   CD2 HD2  sing N N 355 
TYR   CE1 CZ   doub Y N 356 
TYR   CE1 HE1  sing N N 357 
TYR   CE2 CZ   sing Y N 358 
TYR   CE2 HE2  sing N N 359 
TYR   CZ  OH   sing N N 360 
TYR   OH  HH   sing N N 361 
TYR   OXT HXT  sing N N 362 
VAL   N   CA   sing N N 363 
VAL   N   H    sing N N 364 
VAL   N   H2   sing N N 365 
VAL   CA  C    sing N N 366 
VAL   CA  CB   sing N N 367 
VAL   CA  HA   sing N N 368 
VAL   C   O    doub N N 369 
VAL   C   OXT  sing N N 370 
VAL   CB  CG1  sing N N 371 
VAL   CB  CG2  sing N N 372 
VAL   CB  HB   sing N N 373 
VAL   CG1 HG11 sing N N 374 
VAL   CG1 HG12 sing N N 375 
VAL   CG1 HG13 sing N N 376 
VAL   CG2 HG21 sing N N 377 
VAL   CG2 HG22 sing N N 378 
VAL   CG2 HG23 sing N N 379 
VAL   OXT HXT  sing N N 380 
# 
_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                    7HF5 
_atom_sites.fract_transf_matrix[1][1]   0.011278 
_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]   0.011278 
_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]   0.025309 
_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   ? 19.646 -16.335 22.285  0.50 40.45 ?  3    VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 20.440 -15.833 21.317  0.50 45.62 ?  3    VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.668 -15.267 22.455  0.50 40.13 ?  3    VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 19.391 -14.901 21.714  0.50 45.38 ?  3    VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.309 -13.912 22.186  0.50 38.59 ?  3    VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.857 -13.459 21.549  0.50 44.62 ?  3    VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.389 -13.616 22.697  0.50 38.79 ?  3    VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.946 -13.092 21.991  0.50 44.92 ?  3    VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.028 -15.312 23.857  0.50 41.00 ?  3    VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.900 -15.188 23.147  0.50 45.78 ?  3    VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.002 -14.197 24.013  0.50 41.28 ?  3    VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 18.092 -14.016 23.683  0.50 45.84 ?  3    VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.390 -16.670 24.105  0.50 41.24 ?  3    VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 18.067 -16.459 23.167  0.50 46.01 ?  3    VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.958 -15.385 21.809  0.50 48.15 ?  3    VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 18.633 -15.021 21.127  0.50 54.45 ?  3    VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.718 -15.179 24.525  0.50 49.19 ?  3    VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 19.666 -15.320 23.728  0.50 54.93 ?  3    VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.485 -14.356 24.818  0.50 49.53 ?  3    VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 17.562 -14.320 24.437  0.50 55.01 ?  3    VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.463 -13.347 24.080  0.50 49.53 ?  3    VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 18.698 -13.315 23.969  0.50 55.01 ?  3    VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.416 -14.197 23.240  0.50 49.53 ?  3    VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 17.507 -13.688 22.982  0.50 55.01 ?  3    VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.935 -16.652 24.961  0.50 49.48 ?  3    VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.779 -16.633 24.076  0.50 55.20 ?  3    VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.754 -16.852 23.396  0.50 49.48 ?  3    VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 17.295 -16.338 22.591  0.50 55.20 ?  3    VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.083 -17.348 24.112  0.50 49.48 ?  3    VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.608 -17.196 22.843  0.50 55.20 ?  3    VAL   A HG23 1 
ATOM   31   N  N    A ASN   A 1 4   ? 18.638 -13.093 21.378  0.50 36.53 ?  4    ASN   A N    1 
ATOM   32   N  N    B ASN   A 1 4   ? 19.016 -12.648 20.904  0.50 43.28 ?  4    ASN   A N    1 
ATOM   33   C  CA   A ASN   A 1 4   ? 19.080 -11.735 21.096  0.50 34.27 ?  4    ASN   A CA   1 
ATOM   34   C  CA   B ASN   A 1 4   ? 19.337 -11.251 20.639  0.50 41.79 ?  4    ASN   A CA   1 
ATOM   35   C  C    A ASN   A 1 4   ? 17.919 -10.772 21.312  0.50 31.70 ?  4    ASN   A C    1 
ATOM   36   C  C    B ASN   A 1 4   ? 18.298 -10.335 21.275  0.50 39.82 ?  4    ASN   A C    1 
ATOM   37   O  O    A ASN   A 1 4   ? 16.781 -11.178 21.567  0.50 31.09 ?  4    ASN   A O    1 
ATOM   38   O  O    B ASN   A 1 4   ? 17.581 -10.744 22.194  0.50 39.92 ?  4    ASN   A O    1 
ATOM   39   C  CB   A ASN   A 1 4   ? 19.659 -11.597 19.679  0.50 34.40 ?  4    ASN   A CB   1 
ATOM   40   C  CB   B ASN   A 1 4   ? 19.399 -11.003 19.130  0.50 42.13 ?  4    ASN   A CB   1 
ATOM   41   C  CG   A ASN   A 1 4   ? 18.686 -12.021 18.603  0.50 34.34 ?  4    ASN   A CG   1 
ATOM   42   C  CG   B ASN   A 1 4   ? 18.341 -11.769 18.375  0.50 42.33 ?  4    ASN   A CG   1 
ATOM   43   O  OD1  A ASN   A 1 4   ? 17.548 -11.557 18.560  0.50 34.30 ?  4    ASN   A OD1  1 
ATOM   44   O  OD1  B ASN   A 1 4   ? 17.147 -11.503 18.509  0.50 42.45 ?  4    ASN   A OD1  1 
ATOM   45   N  ND2  A ASN   A 1 4   ? 19.133 -12.911 17.723  0.50 34.32 ?  4    ASN   A ND2  1 
ATOM   46   N  ND2  B ASN   A 1 4   ? 18.776 -12.732 17.572  0.50 42.43 ?  4    ASN   A ND2  1 
ATOM   47   H  H    A ASN   A 1 4   ? 17.906 -13.308 20.977  0.50 43.83 ?  4    ASN   A H    1 
ATOM   48   H  H    B ASN   A 1 4   ? 18.243 -12.891 20.610  0.50 51.93 ?  4    ASN   A H    1 
ATOM   49   H  HA   A ASN   A 1 4   ? 19.782 -11.502 21.717  0.50 41.11 ?  4    ASN   A HA   1 
ATOM   50   H  HA   B ASN   A 1 4   ? 20.213 -11.057 21.015  0.50 50.15 ?  4    ASN   A HA   1 
ATOM   51   H  HB2  A ASN   A 1 4   ? 19.891 -10.666 19.522  0.50 41.28 ?  4    ASN   A HB2  1 
ATOM   52   H  HB2  B ASN   A 1 4   ? 19.299 -10.060 18.921  0.50 50.55 ?  4    ASN   A HB2  1 
ATOM   53   H  HB3  A ASN   A 1 4   ? 20.449 -12.152 19.607  0.50 41.28 ?  4    ASN   A HB3  1 
ATOM   54   H  HB3  B ASN   A 1 4   ? 20.254 -11.306 18.820  0.50 50.55 ?  4    ASN   A HB3  1 
ATOM   55   H  HD21 A ASN   A 1 4   ? 18.622 -13.186 17.089  0.50 41.18 ?  4    ASN   A HD21 1 
ATOM   56   H  HD21 B ASN   A 1 4   ? 18.216 -13.202 17.122  0.50 50.91 ?  4    ASN   A HD21 1 
ATOM   57   H  HD22 A ASN   A 1 4   ? 19.938 -13.210 17.786  0.50 41.18 ?  4    ASN   A HD22 1 
ATOM   58   H  HD22 B ASN   A 1 4   ? 19.620 -12.883 17.503  0.50 50.91 ?  4    ASN   A HD22 1 
ATOM   59   N  N    A SER   A 1 5   ? 18.220 -9.479  21.203  0.50 29.61 ?  5    SER   A N    1 
ATOM   60   N  N    B SER   A 1 5   ? 18.195 -9.101  20.775  0.50 37.76 ?  5    SER   A N    1 
ATOM   61   C  CA   A SER   A 1 5   ? 17.272 -8.427  21.546  0.50 27.73 ?  5    SER   A CA   1 
ATOM   62   C  CA   B SER   A 1 5   ? 17.292 -8.098  21.324  0.50 35.62 ?  5    SER   A CA   1 
ATOM   63   C  C    A SER   A 1 5   ? 16.406 -7.987  20.371  0.50 25.14 ?  5    SER   A C    1 
ATOM   64   C  C    B SER   A 1 5   ? 16.349 -7.536  20.265  0.50 32.97 ?  5    SER   A C    1 
ATOM   65   O  O    A SER   A 1 5   ? 15.600 -7.064  20.531  0.50 25.35 ?  5    SER   A O    1 
ATOM   66   O  O    B SER   A 1 5   ? 15.737 -6.484  20.478  0.50 33.04 ?  5    SER   A O    1 
ATOM   67   C  CB   A SER   A 1 5   ? 18.010 -7.222  22.141  0.50 28.69 ?  5    SER   A CB   1 
ATOM   68   C  CB   B SER   A 1 5   ? 18.081 -6.974  21.996  0.50 36.19 ?  5    SER   A CB   1 
ATOM   69   O  OG   A SER   A 1 5   ? 18.947 -6.689  21.222  0.50 29.24 ?  5    SER   A OG   1 
ATOM   70   O  OG   B SER   A 1 5   ? 19.169 -6.563  21.187  0.50 36.63 ?  5    SER   A OG   1 
ATOM   71   H  H    A SER   A 1 5   ? 18.976 -9.183  20.920  0.50 35.52 ?  5    SER   A H    1 
ATOM   72   H  H    B SER   A 1 5   ? 18.632 -8.820  20.088  0.50 45.30 ?  5    SER   A H    1 
ATOM   73   H  HA   A SER   A 1 5   ? 16.677 -8.759  22.230  0.50 33.27 ?  5    SER   A HA   1 
ATOM   74   H  HA   B SER   A 1 5   ? 16.753 -8.522  22.005  0.50 42.74 ?  5    SER   A HA   1 
ATOM   75   H  HB2  A SER   A 1 5   ? 17.364 -6.533  22.368  0.50 34.43 ?  5    SER   A HB2  1 
ATOM   76   H  HB2  B SER   A 1 5   ? 17.493 -6.216  22.134  0.50 43.42 ?  5    SER   A HB2  1 
ATOM   77   H  HB3  A SER   A 1 5   ? 18.482 -7.505  22.943  0.50 34.43 ?  5    SER   A HB3  1 
ATOM   78   H  HB3  B SER   A 1 5   ? 18.416 -7.292  22.850  0.50 43.42 ?  5    SER   A HB3  1 
ATOM   79   H  HG   A SER   A 1 5   ? 19.344 -6.029  21.567  0.50 35.08 ?  5    SER   A HG   1 
ATOM   80   H  HG   B SER   A 1 5   ? 19.599 -5.953  21.573  0.50 43.95 ?  5    SER   A HG   1 
ATOM   81   N  N    A PHE   A 1 6   ? 16.533 -8.619  19.207  0.50 22.16 ?  6    PHE   A N    1 
ATOM   82   N  N    B PHE   A 1 6   ? 16.225 -8.210  19.125  0.50 30.19 ?  6    PHE   A N    1 
ATOM   83   C  CA   A PHE   A 1 6   ? 15.652 -8.292  18.093  0.50 19.52 ?  6    PHE   A CA   1 
ATOM   84   C  CA   B PHE   A 1 6   ? 15.275 -7.801  18.103  0.50 27.29 ?  6    PHE   A CA   1 
ATOM   85   C  C    A PHE   A 1 6   ? 14.219 -8.666  18.451  0.50 19.91 ?  6    PHE   A C    1 
ATOM   86   C  C    B PHE   A 1 6   ? 13.867 -8.200  18.522  0.50 26.74 ?  6    PHE   A C    1 
ATOM   87   O  O    A PHE   A 1 6   ? 13.941 -9.807  18.830  0.50 20.95 ?  6    PHE   A O    1 
ATOM   88   O  O    B PHE   A 1 6   ? 13.659 -9.262  19.116  0.50 27.09 ?  6    PHE   A O    1 
ATOM   89   C  CB   A PHE   A 1 6   ? 16.090 -9.040  16.835  0.50 17.71 ?  6    PHE   A CB   1 
ATOM   90   C  CB   B PHE   A 1 6   ? 15.623 -8.464  16.772  0.50 25.25 ?  6    PHE   A CB   1 
ATOM   91   C  CG   A PHE   A 1 6   ? 17.351 -8.502  16.215  0.50 16.62 ?  6    PHE   A CG   1 
ATOM   92   C  CG   B PHE   A 1 6   ? 16.953 -8.040  16.216  0.50 23.70 ?  6    PHE   A CG   1 
ATOM   93   C  CD1  A PHE   A 1 6   ? 17.344 -7.310  15.513  0.50 16.02 ?  6    PHE   A CD1  1 
ATOM   94   C  CD1  B PHE   A 1 6   ? 17.061 -6.888  15.458  0.50 23.18 ?  6    PHE   A CD1  1 
ATOM   95   C  CD2  A PHE   A 1 6   ? 18.541 -9.200  16.326  0.50 16.72 ?  6    PHE   A CD2  1 
ATOM   96   C  CD2  B PHE   A 1 6   ? 18.091 -8.793  16.453  0.50 23.44 ?  6    PHE   A CD2  1 
ATOM   97   C  CE1  A PHE   A 1 6   ? 18.505 -6.819  14.939  0.50 16.25 ?  6    PHE   A CE1  1 
ATOM   98   C  CE1  B PHE   A 1 6   ? 18.281 -6.492  14.944  0.50 22.98 ?  6    PHE   A CE1  1 
ATOM   99   C  CE2  A PHE   A 1 6   ? 19.704 -8.717  15.753  0.50 16.89 ?  6    PHE   A CE2  1 
ATOM   100  C  CE2  B PHE   A 1 6   ? 19.314 -8.402  15.941  0.50 23.43 ?  6    PHE   A CE2  1 
ATOM   101  C  CZ   A PHE   A 1 6   ? 19.686 -7.526  15.059  0.50 16.72 ?  6    PHE   A CZ   1 
ATOM   102  C  CZ   B PHE   A 1 6   ? 19.408 -7.250  15.187  0.50 23.22 ?  6    PHE   A CZ   1 
ATOM   103  H  H    A PHE   A 1 6   ? 17.107 -9.238  19.046  0.50 26.59 ?  6    PHE   A H    1 
ATOM   104  H  H    B PHE   A 1 6   ? 16.682 -8.909  18.917  0.50 36.22 ?  6    PHE   A H    1 
ATOM   105  H  HA   A PHE   A 1 6   ? 15.690 -7.344  17.917  0.50 23.42 ?  6    PHE   A HA   1 
ATOM   106  H  HA   B PHE   A 1 6   ? 15.309 -6.840  17.994  0.50 32.74 ?  6    PHE   A HA   1 
ATOM   107  H  HB2  A PHE   A 1 6   ? 16.245 -9.973  17.065  0.50 21.25 ?  6    PHE   A HB2  1 
ATOM   108  H  HB2  B PHE   A 1 6   ? 15.645 -9.425  16.898  0.50 30.30 ?  6    PHE   A HB2  1 
ATOM   109  H  HB3  A PHE   A 1 6   ? 15.384 -8.980  16.176  0.50 21.25 ?  6    PHE   A HB3  1 
ATOM   110  H  HB3  B PHE   A 1 6   ? 14.941 -8.234  16.122  0.50 30.30 ?  6    PHE   A HB3  1 
ATOM   111  H  HD1  A PHE   A 1 6   ? 16.553 -6.834  15.429  0.50 19.22 ?  6    PHE   A HD1  1 
ATOM   112  H  HD1  B PHE   A 1 6   ? 16.303 -6.374  15.292  0.50 27.80 ?  6    PHE   A HD1  1 
ATOM   113  H  HD2  A PHE   A 1 6   ? 18.561 -10.006 16.795  0.50 20.05 ?  6    PHE   A HD2  1 
ATOM   114  H  HD2  B PHE   A 1 6   ? 18.032 -9.569  16.962  0.50 28.12 ?  6    PHE   A HD2  1 
ATOM   115  H  HE1  A PHE   A 1 6   ? 18.492 -6.018  14.469  0.50 19.49 ?  6    PHE   A HE1  1 
ATOM   116  H  HE1  B PHE   A 1 6   ? 18.342 -5.715  14.435  0.50 27.57 ?  6    PHE   A HE1  1 
ATOM   117  H  HE2  A PHE   A 1 6   ? 20.500 -9.195  15.839  0.50 20.27 ?  6    PHE   A HE2  1 
ATOM   118  H  HE2  B PHE   A 1 6   ? 20.074 -8.913  16.106  0.50 28.11 ?  6    PHE   A HE2  1 
ATOM   119  H  HZ   A PHE   A 1 6   ? 20.470 -7.199  14.674  0.50 20.06 ?  6    PHE   A HZ   1 
ATOM   120  H  HZ   B PHE   A 1 6   ? 20.229 -6.984  14.841  0.50 27.86 ?  6    PHE   A HZ   1 
ATOM   121  N  N    A SER   A 1 7   ? 13.307 -7.700  18.327  0.50 19.52 ?  7    SER   A N    1 
ATOM   122  N  N    B SER   A 1 7   ? 12.896 -7.343  18.212  0.50 25.90 ?  7    SER   A N    1 
ATOM   123  C  CA   A SER   A 1 7   ? 11.942 -7.843  18.816  0.50 20.07 ?  7    SER   A CA   1 
ATOM   124  C  CA   B SER   A 1 7   ? 11.515 -7.558  18.623  0.50 25.31 ?  7    SER   A CA   1 
ATOM   125  C  C    A SER   A 1 7   ? 10.940 -7.538  17.711  0.50 19.62 ?  7    SER   A C    1 
ATOM   126  C  C    B SER   A 1 7   ? 10.567 -7.377  17.448  0.50 23.34 ?  7    SER   A C    1 
ATOM   127  O  O    A SER   A 1 7   ? 11.192 -6.711  16.831  0.50 19.69 ?  7    SER   A O    1 
ATOM   128  O  O    B SER   A 1 7   ? 10.732 -6.460  16.638  0.50 23.07 ?  7    SER   A O    1 
ATOM   129  C  CB   A SER   A 1 7   ? 11.683 -6.894  19.996  0.50 20.80 ?  7    SER   A CB   1 
ATOM   130  C  CB   B SER   A 1 7   ? 11.115 -6.598  19.749  0.50 26.62 ?  7    SER   A CB   1 
ATOM   131  O  OG   A SER   A 1 7   ? 10.300 -6.833  20.305  0.50 21.47 ?  7    SER   A OG   1 
ATOM   132  O  OG   B SER   A 1 7   ? 11.139 -7.255  21.004  0.50 27.80 ?  7    SER   A OG   1 
ATOM   133  H  H    A SER   A 1 7   ? 13.461 -6.940  17.958  0.50 23.42 ?  7    SER   A H    1 
ATOM   134  H  H    B SER   A 1 7   ? 13.017 -6.618  17.762  0.50 31.08 ?  7    SER   A H    1 
ATOM   135  H  HA   A SER   A 1 7   ? 11.796 -8.751  19.120  0.50 24.08 ?  7    SER   A HA   1 
ATOM   136  H  HA   B SER   A 1 7   ? 11.416 -8.463  18.951  0.50 30.37 ?  7    SER   A HA   1 
ATOM   137  H  HB2  A SER   A 1 7   ? 12.165 -7.218  20.775  0.50 24.96 ?  7    SER   A HB2  1 
ATOM   138  H  HB2  B SER   A 1 7   ? 11.744 -5.864  19.779  0.50 31.94 ?  7    SER   A HB2  1 
ATOM   139  H  HB3  A SER   A 1 7   ? 11.996 -6.005  19.763  0.50 24.96 ?  7    SER   A HB3  1 
ATOM   140  H  HB3  B SER   A 1 7   ? 10.220 -6.262  19.572  0.50 31.94 ?  7    SER   A HB3  1 
ATOM   141  H  HG   A SER   A 1 7   ? 10.174 -6.308  20.951  0.50 25.75 ?  7    SER   A HG   1 
ATOM   142  H  HG   B SER   A 1 7   ? 10.893 -6.728  21.609  0.50 33.35 ?  7    SER   A HG   1 
ATOM   143  N  N    A GLY   A 1 8   ? 9.791  -8.209  17.778  0.50 19.08 ?  8    GLY   A N    1 
ATOM   144  N  N    B GLY   A 1 8   ? 9.571  -8.258  17.366  0.50 21.72 ?  8    GLY   A N    1 
ATOM   145  C  CA   A GLY   A 1 8   ? 8.695  -7.919  16.876  0.50 18.40 ?  8    GLY   A CA   1 
ATOM   146  C  CA   B GLY   A 1 8   ? 8.508  -8.108  16.395  0.50 20.73 ?  8    GLY   A CA   1 
ATOM   147  C  C    A GLY   A 1 8   ? 8.862  -8.418  15.460  0.50 17.38 ?  8    GLY   A C    1 
ATOM   148  C  C    B GLY   A 1 8   ? 8.797  -8.648  15.016  0.50 19.83 ?  8    GLY   A C    1 
ATOM   149  O  O    A GLY   A 1 8   ? 8.091  -8.011  14.586  0.50 17.66 ?  8    GLY   A O    1 
ATOM   150  O  O    B GLY   A 1 8   ? 8.110  -8.265  14.064  0.50 20.23 ?  8    GLY   A O    1 
ATOM   151  H  H    A GLY   A 1 8   ? 9.628  -8.832  18.345  0.50 22.88 ?  8    GLY   A H    1 
ATOM   152  H  H    B GLY   A 1 8   ? 9.495  -8.954  17.866  0.50 26.06 ?  8    GLY   A H    1 
ATOM   153  H  HA2  A GLY   A 1 8   ? 7.888  -8.320  17.234  0.50 22.08 ?  8    GLY   A HA2  1 
ATOM   154  H  HA2  B GLY   A 1 8   ? 7.713  -8.552  16.732  0.50 24.87 ?  8    GLY   A HA2  1 
ATOM   155  H  HA3  A GLY   A 1 8   ? 8.561  -6.957  16.850  0.50 22.08 ?  8    GLY   A HA3  1 
ATOM   156  H  HA3  B GLY   A 1 8   ? 8.304  -7.166  16.298  0.50 24.87 ?  8    GLY   A HA3  1 
ATOM   157  N  N    A TYR   A 1 9   ? 9.839  -9.284  15.200  0.50 16.59 ?  9    TYR   A N    1 
ATOM   158  N  N    B TYR   A 1 9   ? 9.787  -9.529  14.870  0.50 18.54 ?  9    TYR   A N    1 
ATOM   159  C  CA   A TYR   A 1 9   ? 10.053 -9.804  13.858  0.50 15.58 ?  9    TYR   A CA   1 
ATOM   160  C  CA   B TYR   A 1 9   ? 10.140 -10.071 13.566  0.50 17.36 ?  9    TYR   A CA   1 
ATOM   161  C  C    A TYR   A 1 9   ? 9.147  -10.997 13.579  0.50 14.65 ?  9    TYR   A C    1 
ATOM   162  C  C    B TYR   A 1 9   ? 9.356  -11.346 13.272  0.50 16.60 ?  9    TYR   A C    1 
ATOM   163  O  O    A TYR   A 1 9   ? 8.796  -11.773 14.476  0.50 15.42 ?  9    TYR   A O    1 
ATOM   164  O  O    B TYR   A 1 9   ? 9.160  -12.194 14.149  0.50 16.88 ?  9    TYR   A O    1 
ATOM   165  C  CB   A TYR   A 1 9   ? 11.500 -10.265 13.676  0.50 16.13 ?  9    TYR   A CB   1 
ATOM   166  C  CB   B TYR   A 1 9   ? 11.646 -10.349 13.483  0.50 17.15 ?  9    TYR   A CB   1 
ATOM   167  C  CG   A TYR   A 1 9   ? 12.481 -9.137  13.512  0.50 16.12 ?  9    TYR   A CG   1 
ATOM   168  C  CG   B TYR   A 1 9   ? 12.489 -9.096  13.308  0.50 17.21 ?  9    TYR   A CG   1 
ATOM   169  C  CD1  A TYR   A 1 9   ? 12.911 -8.413  14.609  0.50 16.10 ?  9    TYR   A CD1  1 
ATOM   170  C  CD1  B TYR   A 1 9   ? 12.679 -8.209  14.361  0.50 17.36 ?  9    TYR   A CD1  1 
ATOM   171  C  CD2  A TYR   A 1 9   ? 12.965 -8.787  12.259  0.50 15.97 ?  9    TYR   A CD2  1 
ATOM   172  C  CD2  B TYR   A 1 9   ? 13.083 -8.799  12.088  0.50 16.74 ?  9    TYR   A CD2  1 
ATOM   173  C  CE1  A TYR   A 1 9   ? 13.792 -7.371  14.470  0.50 16.23 ?  9    TYR   A CE1  1 
ATOM   174  C  CE1  B TYR   A 1 9   ? 13.440 -7.059  14.204  0.50 17.24 ?  9    TYR   A CE1  1 
ATOM   175  C  CE2  A TYR   A 1 9   ? 13.851 -7.746  12.109  0.50 16.37 ?  9    TYR   A CE2  1 
ATOM   176  C  CE2  B TYR   A 1 9   ? 13.846 -7.654  11.922  0.50 16.81 ?  9    TYR   A CE2  1 
ATOM   177  C  CZ   A TYR   A 1 9   ? 14.259 -7.042  13.217  0.50 16.69 ?  9    TYR   A CZ   1 
ATOM   178  C  CZ   B TYR   A 1 9   ? 14.018 -6.789  12.981  0.50 16.69 ?  9    TYR   A CZ   1 
ATOM   179  O  OH   A TYR   A 1 9   ? 15.142 -6.007  13.071  0.50 17.62 ?  9    TYR   A OH   1 
ATOM   180  O  OH   B TYR   A 1 9   ? 14.773 -5.654  12.808  0.50 16.55 ?  9    TYR   A OH   1 
ATOM   181  H  H    A TYR   A 1 9   ? 10.391 -9.579  15.785  0.50 19.90 ?  9    TYR   A H    1 
ATOM   182  H  H    B TYR   A 1 9   ? 10.271 -9.828  15.516  0.50 22.24 ?  9    TYR   A H    1 
ATOM   183  H  HA   A TYR   A 1 9   ? 9.870  -9.099  13.205  0.50 18.69 ?  9    TYR   A HA   1 
ATOM   184  H  HA   B TYR   A 1 9   ? 9.912  -9.427  12.885  0.50 20.83 ?  9    TYR   A HA   1 
ATOM   185  H  HB2  A TYR   A 1 9   ? 11.765 -10.792 14.444  0.50 19.34 ?  9    TYR   A HB2  1 
ATOM   186  H  HB2  B TYR   A 1 9   ? 11.925 -10.791 14.300  0.50 20.58 ?  9    TYR   A HB2  1 
ATOM   187  H  HB3  A TYR   A 1 9   ? 11.527 -10.805 12.873  0.50 19.34 ?  9    TYR   A HB3  1 
ATOM   188  H  HB3  B TYR   A 1 9   ? 11.809 -10.930 12.723  0.50 20.58 ?  9    TYR   A HB3  1 
ATOM   189  H  HD1  A TYR   A 1 9   ? 12.587 -8.633  15.454  0.50 19.31 ?  9    TYR   A HD1  1 
ATOM   190  H  HD1  B TYR   A 1 9   ? 12.282 -8.388  15.186  0.50 20.82 ?  9    TYR   A HD1  1 
ATOM   191  H  HD2  A TYR   A 1 9   ? 12.686 -9.262  11.508  0.50 19.16 ?  9    TYR   A HD2  1 
ATOM   192  H  HD2  B TYR   A 1 9   ? 12.965 -9.379  11.371  0.50 20.08 ?  9    TYR   A HD2  1 
ATOM   193  H  HE1  A TYR   A 1 9   ? 14.070 -6.897  15.217  0.50 19.47 ?  9    TYR   A HE1  1 
ATOM   194  H  HE1  B TYR   A 1 9   ? 13.560 -6.474  14.919  0.50 20.69 ?  9    TYR   A HE1  1 
ATOM   195  H  HE2  A TYR   A 1 9   ? 14.174 -7.521  11.265  0.50 19.64 ?  9    TYR   A HE2  1 
ATOM   196  H  HE2  B TYR   A 1 9   ? 14.242 -7.468  11.100  0.50 20.17 ?  9    TYR   A HE2  1 
ATOM   197  H  HH   A TYR   A 1 9   ? 15.303 -5.672  13.821  0.50 21.14 ?  9    TYR   A HH   1 
ATOM   198  H  HH   B TYR   A 1 9   ? 14.816 -5.213  13.523  0.50 19.85 ?  9    TYR   A HH   1 
ATOM   199  N  N    A LEU   A 1 10  ? 8.770  -11.132 12.314  0.50 14.23 ?  10   LEU   A N    1 
ATOM   200  N  N    B LEU   A 1 10  ? 8.916  -11.474 12.021  0.50 16.28 ?  10   LEU   A N    1 
ATOM   201  C  CA   A LEU   A 1 10  ? 8.152  -12.351 11.816  0.50 14.16 ?  10   LEU   A CA   1 
ATOM   202  C  CA   B LEU   A 1 10  ? 8.357  -12.720 11.516  0.50 16.28 ?  10   LEU   A CA   1 
ATOM   203  C  C    A LEU   A 1 10  ? 9.256  -13.297 11.330  0.50 13.40 ?  10   LEU   A C    1 
ATOM   204  C  C    B LEU   A 1 10  ? 9.515  -13.632 11.159  0.50 16.03 ?  10   LEU   A C    1 
ATOM   205  O  O    A LEU   A 1 10  ? 10.210 -12.867 10.674  0.50 13.38 ?  10   LEU   A O    1 
ATOM   206  O  O    B LEU   A 1 10  ? 10.454 -13.206 10.475  0.50 15.98 ?  10   LEU   A O    1 
ATOM   207  C  CB   A LEU   A 1 10  ? 7.186  -12.010 10.676  0.50 15.01 ?  10   LEU   A CB   1 
ATOM   208  C  CB   B LEU   A 1 10  ? 7.526  -12.444 10.261  0.50 16.75 ?  10   LEU   A CB   1 
ATOM   209  C  CG   A LEU   A 1 10  ? 6.524  -13.216 9.995   0.50 16.35 ?  10   LEU   A CG   1 
ATOM   210  C  CG   B LEU   A 1 10  ? 7.295  -13.572 9.238   0.50 17.40 ?  10   LEU   A CG   1 
ATOM   211  C  CD1  A LEU   A 1 10  ? 5.465  -13.853 10.885  0.50 17.61 ?  10   LEU   A CD1  1 
ATOM   212  C  CD1  B LEU   A 1 10  ? 6.413  -14.668 9.799   0.50 18.16 ?  10   LEU   A CD1  1 
ATOM   213  C  CD2  A LEU   A 1 10  ? 5.952  -12.839 8.634   0.50 17.94 ?  10   LEU   A CD2  1 
ATOM   214  C  CD2  B LEU   A 1 10  ? 6.697  -13.009 7.960   0.50 18.07 ?  10   LEU   A CD2  1 
ATOM   215  H  H    A LEU   A 1 10  ? 8.843  -10.500 11.718  0.50 17.07 ?  10   LEU   A H    1 
ATOM   216  H  H    B LEU   A 1 10  ? 8.952  -10.856 11.426  0.50 19.53 ?  10   LEU   A H    1 
ATOM   217  H  HA   A LEU   A 1 10  ? 7.640  -12.767 12.536  0.50 16.99 ?  10   LEU   A HA   1 
ATOM   218  H  HA   B LEU   A 1 10  ? 7.806  -13.152 12.187  0.50 19.53 ?  10   LEU   A HA   1 
ATOM   219  H  HB2  A LEU   A 1 10  ? 6.465  -11.443 11.022  0.50 18.00 ?  10   LEU   A HB2  1 
ATOM   220  H  HB2  B LEU   A 1 10  ? 6.649  -12.157 10.553  0.50 20.09 ?  10   LEU   A HB2  1 
ATOM   221  H  HB3  A LEU   A 1 10  ? 7.670  -11.518 9.996   0.50 18.00 ?  10   LEU   A HB3  1 
ATOM   222  H  HB3  B LEU   A 1 10  ? 7.953  -11.722 9.780   0.50 20.09 ?  10   LEU   A HB3  1 
ATOM   223  H  HG   A LEU   A 1 10  ? 7.205  -13.884 9.839   0.50 19.62 ?  10   LEU   A HG   1 
ATOM   224  H  HG   B LEU   A 1 10  ? 8.147  -13.971 9.000   0.50 20.88 ?  10   LEU   A HG   1 
ATOM   225  H  HD11 A LEU   A 1 10  ? 5.123  -14.646 10.445  0.50 21.13 ?  10   LEU   A HD11 1 
ATOM   226  H  HD11 B LEU   A 1 10  ? 6.275  -15.337 9.110   0.50 21.78 ?  10   LEU   A HD11 1 
ATOM   227  H  HD12 A LEU   A 1 10  ? 5.869  -14.093 11.734  0.50 21.13 ?  10   LEU   A HD12 1 
ATOM   228  H  HD12 B LEU   A 1 10  ? 6.855  -15.065 10.564  0.50 21.78 ?  10   LEU   A HD12 1 
ATOM   229  H  HD13 A LEU   A 1 10  ? 4.748  -13.217 11.028  0.50 21.13 ?  10   LEU   A HD13 1 
ATOM   230  H  HD13 B LEU   A 1 10  ? 5.565  -14.283 10.064  0.50 21.78 ?  10   LEU   A HD13 1 
ATOM   231  H  HD21 A LEU   A 1 10  ? 5.548  -13.628 8.240   0.50 21.52 ?  10   LEU   A HD21 1 
ATOM   232  H  HD21 B LEU   A 1 10  ? 6.488  -13.743 7.361   0.50 21.68 ?  10   LEU   A HD21 1 
ATOM   233  H  HD22 A LEU   A 1 10  ? 5.286  -12.147 8.754   0.50 21.52 ?  10   LEU   A HD22 1 
ATOM   234  H  HD22 B LEU   A 1 10  ? 5.890  -12.520 8.181   0.50 21.68 ?  10   LEU   A HD22 1 
ATOM   235  H  HD23 A LEU   A 1 10  ? 6.672  -12.518 8.071   0.50 21.52 ?  10   LEU   A HD23 1 
ATOM   236  H  HD23 B LEU   A 1 10  ? 7.343  -12.416 7.546   0.50 21.68 ?  10   LEU   A HD23 1 
ATOM   237  N  N    A LYS   A 1 11  ? 9.131  -14.583 11.671  0.50 12.65 ?  11   LYS   A N    1 
ATOM   238  N  N    B LYS   A 1 11  ? 9.471  -14.874 11.637  0.50 16.51 ?  11   LYS   A N    1 
ATOM   239  C  CA   A LYS   A 1 11  ? 10.135 -15.592 11.325  0.50 12.61 ?  11   LYS   A CA   1 
ATOM   240  C  CA   B LYS   A 1 11  ? 10.485 -15.846 11.242  0.50 17.47 ?  11   LYS   A CA   1 
ATOM   241  C  C    A LYS   A 1 11  ? 9.817  -16.200 9.962   0.50 12.94 ?  11   LYS   A C    1 
ATOM   242  C  C    B LYS   A 1 11  ? 10.062 -16.454 9.914   0.50 16.06 ?  11   LYS   A C    1 
ATOM   243  O  O    A LYS   A 1 11  ? 8.703  -16.676 9.741   0.50 13.31 ?  11   LYS   A O    1 
ATOM   244  O  O    B LYS   A 1 11  ? 9.128  -17.255 9.849   0.50 16.36 ?  11   LYS   A O    1 
ATOM   245  C  CB   A LYS   A 1 11  ? 10.186 -16.694 12.398  0.50 10.99 ?  11   LYS   A CB   1 
ATOM   246  C  CB   B LYS   A 1 11  ? 10.774 -16.856 12.353  0.50 19.78 ?  11   LYS   A CB   1 
ATOM   247  C  CG   A LYS   A 1 11  ? 11.233 -17.823 12.179  0.50 10.83 ?  11   LYS   A CG   1 
ATOM   248  C  CG   B LYS   A 1 11  ? 10.082 -18.193 12.362  0.50 22.07 ?  11   LYS   A CG   1 
ATOM   249  C  CD   A LYS   A 1 11  ? 11.410 -18.696 13.444  0.50 11.33 ?  11   LYS   A CD   1 
ATOM   250  C  CD   B LYS   A 1 11  ? 10.611 -18.956 13.566  0.50 23.19 ?  11   LYS   A CD   1 
ATOM   251  C  CE   A LYS   A 1 11  ? 12.404 -19.861 13.263  0.50 11.42 ?  11   LYS   A CE   1 
ATOM   252  C  CE   B LYS   A 1 11  ? 11.877 -19.754 13.254  0.50 23.95 ?  11   LYS   A CE   1 
ATOM   253  N  NZ   A LYS   A 1 11  ? 13.801 -19.411 12.995  0.50 11.06 ?  11   LYS   A NZ   1 
ATOM   254  N  NZ   B LYS   A 1 11  ? 13.155 -18.981 13.207  0.50 24.57 ?  11   LYS   A NZ   1 
ATOM   255  H  H    A LYS   A 1 11  ? 8.450  -14.879 12.112  0.50 15.17 ?  11   LYS   A H    1 
ATOM   256  H  H    B LYS   A 1 11  ? 8.880  -15.181 12.194  0.50 19.81 ?  11   LYS   A H    1 
ATOM   257  H  HA   A LYS   A 1 11  ? 10.994 -15.150 11.272  0.50 15.13 ?  11   LYS   A HA   1 
ATOM   258  H  HA   B LYS   A 1 11  ? 11.307 -15.381 11.081  0.50 20.95 ?  11   LYS   A HA   1 
ATOM   259  H  HB2  A LYS   A 1 11  ? 10.382 -16.262 13.247  0.50 13.18 ?  11   LYS   A HB2  1 
ATOM   260  H  HB2  B LYS   A 1 11  ? 11.722 -17.054 12.328  0.50 23.73 ?  11   LYS   A HB2  1 
ATOM   261  H  HB3  A LYS   A 1 11  ? 9.307  -17.098 12.442  0.50 13.18 ?  11   LYS   A HB3  1 
ATOM   262  H  HB3  B LYS   A 1 11  ? 10.559 -16.438 13.194  0.50 23.73 ?  11   LYS   A HB3  1 
ATOM   263  H  HG2  A LYS   A 1 11  ? 10.931 -18.385 11.450  0.50 12.99 ?  11   LYS   A HG2  1 
ATOM   264  H  HG2  B LYS   A 1 11  ? 9.124  -18.090 12.459  0.50 26.48 ?  11   LYS   A HG2  1 
ATOM   265  H  HG3  A LYS   A 1 11  ? 12.087 -17.417 11.959  0.50 12.99 ?  11   LYS   A HG3  1 
ATOM   266  H  HG3  B LYS   A 1 11  ? 10.298 -18.699 11.564  0.50 26.48 ?  11   LYS   A HG3  1 
ATOM   267  H  HD2  A LYS   A 1 11  ? 11.729 -18.133 14.165  0.50 13.59 ?  11   LYS   A HD2  1 
ATOM   268  H  HD2  B LYS   A 1 11  ? 10.818 -18.327 14.273  0.50 27.82 ?  11   LYS   A HD2  1 
ATOM   269  H  HD3  A LYS   A 1 11  ? 10.547 -19.073 13.679  0.50 13.59 ?  11   LYS   A HD3  1 
ATOM   270  H  HD3  B LYS   A 1 11  ? 9.940  -19.565 13.882  0.50 27.82 ?  11   LYS   A HD3  1 
ATOM   271  H  HE2  A LYS   A 1 11  ? 12.418 -20.393 14.070  0.50 13.69 ?  11   LYS   A HE2  1 
ATOM   272  H  HE2  B LYS   A 1 11  ? 11.979 -20.433 13.935  0.50 28.73 ?  11   LYS   A HE2  1 
ATOM   273  H  HE3  A LYS   A 1 11  ? 12.123 -20.403 12.510  0.50 13.69 ?  11   LYS   A HE3  1 
ATOM   274  H  HE3  B LYS   A 1 11  ? 11.764 -20.173 12.391  0.50 28.73 ?  11   LYS   A HE3  1 
ATOM   275  H  HZ1  A LYS   A 1 11  ? 14.333 -20.118 12.893  0.50 13.27 ?  11   LYS   A HZ1  1 
ATOM   276  H  HZ1  B LYS   A 1 11  ? 13.849 -19.536 13.296  0.50 29.48 ?  11   LYS   A HZ1  1 
ATOM   277  H  HZ2  A LYS   A 1 11  ? 13.826 -18.922 12.252  0.50 13.27 ?  11   LYS   A HZ2  1 
ATOM   278  H  HZ2  B LYS   A 1 11  ? 13.230 -18.551 12.432  0.50 29.48 ?  11   LYS   A HZ2  1 
ATOM   279  H  HZ3  A LYS   A 1 11  ? 14.098 -18.922 13.675  0.50 13.27 ?  11   LYS   A HZ3  1 
ATOM   280  H  HZ3  B LYS   A 1 11  ? 13.175 -18.390 13.871  0.50 29.48 ?  11   LYS   A HZ3  1 
ATOM   281  N  N    A LEU   A 1 12  ? 10.800 -16.211 9.060   0.50 13.15 ?  12   LEU   A N    1 
ATOM   282  N  N    B LEU   A 1 12  ? 10.713 -16.013 8.834   0.50 14.70 ?  12   LEU   A N    1 
ATOM   283  C  CA   A LEU   A 1 12  ? 10.594 -16.724 7.704   0.50 14.17 ?  12   LEU   A CA   1 
ATOM   284  C  CA   B LEU   A 1 12  ? 10.453 -16.614 7.533   0.50 14.82 ?  12   LEU   A CA   1 
ATOM   285  C  C    A LEU   A 1 12  ? 11.174 -18.121 7.483   0.50 14.57 ?  12   LEU   A C    1 
ATOM   286  C  C    B LEU   A 1 12  ? 11.030 -18.016 7.469   0.50 14.47 ?  12   LEU   A C    1 
ATOM   287  O  O    A LEU   A 1 12  ? 10.500 -18.981 6.908   0.50 15.53 ?  12   LEU   A O    1 
ATOM   288  O  O    B LEU   A 1 12  ? 10.433 -18.917 6.869   0.50 15.07 ?  12   LEU   A O    1 
ATOM   289  C  CB   A LEU   A 1 12  ? 11.151 -15.746 6.660   0.50 14.54 ?  12   LEU   A CB   1 
ATOM   290  C  CB   B LEU   A 1 12  ? 11.088 -15.776 6.429   0.50 15.72 ?  12   LEU   A CB   1 
ATOM   291  C  CG   A LEU   A 1 12  ? 10.467 -14.378 6.524   0.50 14.44 ?  12   LEU   A CG   1 
ATOM   292  C  CG   B LEU   A 1 12  ? 10.425 -14.454 6.082   0.50 16.59 ?  12   LEU   A CG   1 
ATOM   293  C  CD1  A LEU   A 1 12  ? 11.221 -13.489 5.532   0.50 14.94 ?  12   LEU   A CD1  1 
ATOM   294  C  CD1  B LEU   A 1 12  ? 11.242 -13.783 5.002   0.50 16.94 ?  12   LEU   A CD1  1 
ATOM   295  C  CD2  A LEU   A 1 12  ? 9.008  -14.523 6.102   0.50 14.58 ?  12   LEU   A CD2  1 
ATOM   296  C  CD2  B LEU   A 1 12  ? 8.995  -14.683 5.625   0.50 16.82 ?  12   LEU   A CD2  1 
ATOM   297  H  H    A LEU   A 1 12  ? 11.595 -15.944 9.222   0.50 15.77 ?  12   LEU   A H    1 
ATOM   298  H  H    B LEU   A 1 12  ? 11.305 -15.386 8.834   0.50 17.63 ?  12   LEU   A H    1 
ATOM   299  H  HA   A LEU   A 1 12  ? 9.644  -16.801 7.553   0.50 16.99 ?  12   LEU   A HA   1 
ATOM   300  H  HA   B LEU   A 1 12  ? 9.494  -16.657 7.384   0.50 17.78 ?  12   LEU   A HA   1 
ATOM   301  H  HB2  A LEU   A 1 12  ? 12.079 -15.576 6.877   0.50 17.44 ?  12   LEU   A HB2  1 
ATOM   302  H  HB2  B LEU   A 1 12  ? 12.000 -15.577 6.691   0.50 18.85 ?  12   LEU   A HB2  1 
ATOM   303  H  HB3  A LEU   A 1 12  ? 11.098 -16.177 5.795   0.50 17.44 ?  12   LEU   A HB3  1 
ATOM   304  H  HB3  B LEU   A 1 12  ? 11.099 -16.309 5.619   0.50 18.85 ?  12   LEU   A HB3  1 
ATOM   305  H  HG   A LEU   A 1 12  ? 10.480 -13.930 7.381   0.50 17.32 ?  12   LEU   A HG   1 
ATOM   306  H  HG   B LEU   A 1 12  ? 10.415 -13.882 6.866   0.50 19.90 ?  12   LEU   A HG   1 
ATOM   307  H  HD11 A LEU   A 1 12  ? 10.765 -12.634 5.460   0.50 17.92 ?  12   LEU   A HD11 1 
ATOM   308  H  HD11 B LEU   A 1 12  ? 10.837 -12.933 4.783   0.50 20.33 ?  12   LEU   A HD11 1 
ATOM   309  H  HD12 A LEU   A 1 12  ? 12.126 -13.353 5.853   0.50 17.92 ?  12   LEU   A HD12 1 
ATOM   310  H  HD12 B LEU   A 1 12  ? 12.147 -13.647 5.330   0.50 20.33 ?  12   LEU   A HD12 1 
ATOM   311  H  HD13 A LEU   A 1 12  ? 11.240 -13.925 4.665   0.50 17.92 ?  12   LEU   A HD13 1 
ATOM   312  H  HD13 B LEU   A 1 12  ? 11.260 -14.358 4.220   0.50 20.33 ?  12   LEU   A HD13 1 
ATOM   313  H  HD21 A LEU   A 1 12  ? 8.637  -13.640 5.937   0.50 17.49 ?  12   LEU   A HD21 1 
ATOM   314  H  HD21 B LEU   A 1 12  ? 8.773  -14.031 4.943   0.50 20.18 ?  12   LEU   A HD21 1 
ATOM   315  H  HD22 A LEU   A 1 12  ? 8.964  -15.055 5.292   0.50 17.49 ?  12   LEU   A HD22 1 
ATOM   316  H  HD22 B LEU   A 1 12  ? 8.923  -15.580 5.263   0.50 20.18 ?  12   LEU   A HD22 1 
ATOM   317  H  HD23 A LEU   A 1 12  ? 8.517  -14.959 6.814   0.50 17.49 ?  12   LEU   A HD23 1 
ATOM   318  H  HD23 B LEU   A 1 12  ? 8.402  -14.588 6.385   0.50 20.18 ?  12   LEU   A HD23 1 
ATOM   319  N  N    A THR   A 1 13  ? 12.419 -18.355 7.895   0.50 14.46 ?  13   THR   A N    1 
ATOM   320  N  N    B THR   A 1 13  ? 12.207 -18.204 8.059   0.50 14.00 ?  13   THR   A N    1 
ATOM   321  C  CA   A THR   A 1 13  ? 13.076 -19.657 7.785   0.50 14.82 ?  13   THR   A CA   1 
ATOM   322  C  CA   B THR   A 1 13  ? 12.912 -19.471 8.006   0.50 14.29 ?  13   THR   A CA   1 
ATOM   323  C  C    A THR   A 1 13  ? 13.868 -19.881 9.065   0.50 14.64 ?  13   THR   A C    1 
ATOM   324  C  C    B THR   A 1 13  ? 13.664 -19.669 9.313   0.50 14.75 ?  13   THR   A C    1 
ATOM   325  O  O    A THR   A 1 13  ? 13.745 -19.126 10.036  0.50 14.27 ?  13   THR   A O    1 
ATOM   326  O  O    B THR   A 1 13  ? 13.584 -18.858 10.240  0.50 14.90 ?  13   THR   A O    1 
ATOM   327  C  CB   A THR   A 1 13  ? 14.002 -19.741 6.561   0.50 15.49 ?  13   THR   A CB   1 
ATOM   328  C  CB   B THR   A 1 13  ? 13.920 -19.500 6.853   0.50 14.28 ?  13   THR   A CB   1 
ATOM   329  O  OG1  A THR   A 1 13  ? 15.125 -18.870 6.748   0.50 15.82 ?  13   THR   A OG1  1 
ATOM   330  O  OG1  B THR   A 1 13  ? 14.940 -18.527 7.098   0.50 14.05 ?  13   THR   A OG1  1 
ATOM   331  C  CG2  A THR   A 1 13  ? 13.279 -19.341 5.290   0.50 16.67 ?  13   THR   A CG2  1 
ATOM   332  C  CG2  B THR   A 1 13  ? 13.249 -19.245 5.501   0.50 15.44 ?  13   THR   A CG2  1 
ATOM   333  H  H    A THR   A 1 13  ? 12.924 -17.765 8.256   0.50 17.34 ?  13   THR   A H    1 
ATOM   334  H  H    B THR   A 1 13  ? 12.622 -17.590 8.497   0.50 16.79 ?  13   THR   A H    1 
ATOM   335  H  HA   A THR   A 1 13  ? 12.410 -20.364 7.713   0.50 17.78 ?  13   THR   A HA   1 
ATOM   336  H  HA   B THR   A 1 13  ? 12.271 -20.191 7.889   0.50 17.15 ?  13   THR   A HA   1 
ATOM   337  H  HB   A THR   A 1 13  ? 14.312 -20.662 6.457   0.50 18.58 ?  13   THR   A HB   1 
ATOM   338  H  HB   B THR   A 1 13  ? 14.336 -20.368 6.817   0.50 17.13 ?  13   THR   A HB   1 
ATOM   339  H  HG1  A THR   A 1 13  ? 15.648 -18.931 6.091   0.50 18.97 ?  13   THR   A HG1  1 
ATOM   340  H  HG1  B THR   A 1 13  ? 15.476 -18.506 6.453   0.50 16.85 ?  13   THR   A HG1  1 
ATOM   341  H  HG21 A THR   A 1 13  ? 13.831 -19.547 4.519   0.50 19.99 ?  13   THR   A HG21 1 
ATOM   342  H  HG21 B THR   A 1 13  ? 13.895 -19.362 4.784   0.50 18.52 ?  13   THR   A HG21 1 
ATOM   343  H  HG22 A THR   A 1 13  ? 12.445 -19.830 5.218   0.50 19.99 ?  13   THR   A HG22 1 
ATOM   344  H  HG22 B THR   A 1 13  ? 12.523 -19.881 5.367   0.50 18.52 ?  13   THR   A HG22 1 
ATOM   345  H  HG23 A THR   A 1 13  ? 13.092 -18.393 5.304   0.50 19.99 ?  13   THR   A HG23 1 
ATOM   346  H  HG23 B THR   A 1 13  ? 12.892 -18.349 5.462   0.50 18.52 ?  13   THR   A HG23 1 
ATOM   347  N  N    A ASP   A 1 14  ? 14.713 -20.914 9.061   0.50 14.89 ?  14   ASP   A N    1 
ATOM   348  N  N    B ASP   A 1 14  ? 14.422 -20.760 9.361   0.50 14.72 ?  14   ASP   A N    1 
ATOM   349  C  CA   A ASP   A 1 14  ? 15.512 -21.205 10.241  0.50 14.90 ?  14   ASP   A CA   1 
ATOM   350  C  CA   B ASP   A 1 14  ? 15.288 -21.024 10.500  0.50 15.88 ?  14   ASP   A CA   1 
ATOM   351  C  C    A ASP   A 1 14  ? 16.300 -19.994 10.736  0.50 14.35 ?  14   ASP   A C    1 
ATOM   352  C  C    B ASP   A 1 14  ? 16.210 -19.841 10.777  0.50 14.92 ?  14   ASP   A C    1 
ATOM   353  O  O    A ASP   A 1 14  ? 16.620 -19.928 11.926  0.50 14.37 ?  14   ASP   A O    1 
ATOM   354  O  O    B ASP   A 1 14  ? 16.367 -19.430 11.932  0.50 15.06 ?  14   ASP   A O    1 
ATOM   355  C  CB   A ASP   A 1 14  ? 16.466 -22.366 9.964   0.50 16.55 ?  14   ASP   A CB   1 
ATOM   356  C  CB   B ASP   A 1 14  ? 16.101 -22.290 10.230  0.50 18.78 ?  14   ASP   A CB   1 
ATOM   357  C  CG   A ASP   A 1 14  ? 17.304 -22.700 11.168  0.50 19.41 ?  14   ASP   A CG   1 
ATOM   358  C  CG   B ASP   A 1 14  ? 17.083 -22.607 11.336  0.50 21.35 ?  14   ASP   A CG   1 
ATOM   359  O  OD1  A ASP   A 1 14  ? 16.753 -23.319 12.106  0.50 19.99 ?  14   ASP   A OD1  1 
ATOM   360  O  OD1  B ASP   A 1 14  ? 16.672 -22.615 12.516  0.50 22.38 ?  14   ASP   A OD1  1 
ATOM   361  O  OD2  A ASP   A 1 14  ? 18.490 -22.303 11.189  0.50 21.09 -1 14   ASP   A OD2  1 
ATOM   362  O  OD2  B ASP   A 1 14  ? 18.260 -22.884 11.018  0.50 22.59 -1 14   ASP   A OD2  1 
ATOM   363  H  H    A ASP   A 1 14  ? 14.859 -21.451 8.400   0.50 17.86 ?  14   ASP   A H    1 
ATOM   364  H  H    B ASP   A 1 14  ? 14.444 -21.346 8.744   0.50 17.66 ?  14   ASP   A H    1 
ATOM   365  H  HA   A ASP   A 1 14  ? 14.936 -21.480 10.963  0.50 17.88 ?  14   ASP   A HA   1 
ATOM   366  H  HA   B ASP   A 1 14  ? 14.730 -21.173 11.286  0.50 19.05 ?  14   ASP   A HA   1 
ATOM   367  H  HB2  A ASP   A 1 14  ? 15.945 -23.157 9.720   0.50 19.86 ?  14   ASP   A HB2  1 
ATOM   368  H  HB2  B ASP   A 1 14  ? 15.489 -23.038 10.143  0.50 22.53 ?  14   ASP   A HB2  1 
ATOM   369  H  HB3  A ASP   A 1 14  ? 17.066 -22.138 9.236   0.50 19.86 ?  14   ASP   A HB3  1 
ATOM   370  H  HB3  B ASP   A 1 14  ? 16.599 -22.166 9.413   0.50 22.53 ?  14   ASP   A HB3  1 
ATOM   371  N  N    A ASN   A 1 15  ? 16.590 -19.011 9.872   0.50 13.81 ?  15   ASN   A N    1 
ATOM   372  N  N    B ASN   A 1 15  ? 16.830 -19.274 9.723   0.50 13.74 ?  15   ASN   A N    1 
ATOM   373  C  CA   A ASN   A 1 15  ? 17.554 -17.976 10.229  0.50 13.39 ?  15   ASN   A CA   1 
ATOM   374  C  CA   B ASN   A 1 15  ? 17.843 -18.227 9.875   0.50 13.28 ?  15   ASN   A CA   1 
ATOM   375  C  C    A ASN   A 1 15  ? 17.207 -16.572 9.757   0.50 12.84 ?  15   ASN   A C    1 
ATOM   376  C  C    B ASN   A 1 15  ? 17.456 -16.857 9.324   0.50 13.30 ?  15   ASN   A C    1 
ATOM   377  O  O    A ASN   A 1 15  ? 17.973 -15.649 10.053  0.50 13.33 ?  15   ASN   A O    1 
ATOM   378  O  O    B ASN   A 1 15  ? 18.227 -15.906 9.511   0.50 13.77 ?  15   ASN   A O    1 
ATOM   379  C  CB   A ASN   A 1 15  ? 18.949 -18.337 9.694   0.50 13.41 ?  15   ASN   A CB   1 
ATOM   380  C  CB   B ASN   A 1 15  ? 19.182 -18.659 9.243   0.50 12.86 ?  15   ASN   A CB   1 
ATOM   381  C  CG   A ASN   A 1 15  ? 18.980 -18.465 8.187   0.50 13.80 ?  15   ASN   A CG   1 
ATOM   382  C  CG   B ASN   A 1 15  ? 19.128 -18.721 7.722   0.50 13.29 ?  15   ASN   A CG   1 
ATOM   383  O  OD1  A ASN   A 1 15  ? 18.239 -19.257 7.602   0.50 14.01 ?  15   ASN   A OD1  1 
ATOM   384  O  OD1  B ASN   A 1 15  ? 18.432 -19.559 7.154   0.50 13.87 ?  15   ASN   A OD1  1 
ATOM   385  N  ND2  A ASN   A 1 15  ? 19.822 -17.664 7.545   0.50 14.05 ?  15   ASN   A ND2  1 
ATOM   386  N  ND2  B ASN   A 1 15  ? 19.882 -17.847 7.057   0.50 13.50 ?  15   ASN   A ND2  1 
ATOM   387  H  H    A ASN   A 1 15  ? 16.216 -18.911 9.107   0.50 16.56 ?  15   ASN   A H    1 
ATOM   388  H  H    B ASN   A 1 15  ? 16.694 -19.511 8.910   0.50 16.48 ?  15   ASN   A H    1 
ATOM   389  H  HA   A ASN   A 1 15  ? 17.614 -17.931 11.199  0.50 16.06 ?  15   ASN   A HA   1 
ATOM   390  H  HA   B ASN   A 1 15  ? 18.014 -18.119 10.818  0.50 15.93 ?  15   ASN   A HA   1 
ATOM   391  H  HB2  A ASN   A 1 15  ? 19.567 -17.635 9.953   0.50 16.08 ?  15   ASN   A HB2  1 
ATOM   392  H  HB2  B ASN   A 1 15  ? 19.873 -18.021 9.491   0.50 15.43 ?  15   ASN   A HB2  1 
ATOM   393  H  HB3  A ASN   A 1 15  ? 19.213 -19.180 10.076  0.50 16.08 ?  15   ASN   A HB3  1 
ATOM   394  H  HB3  B ASN   A 1 15  ? 19.429 -19.544 9.570   0.50 15.43 ?  15   ASN   A HB3  1 
ATOM   395  H  HD21 A ASN   A 1 15  ? 19.872 -17.695 6.688   0.50 16.86 ?  15   ASN   A HD21 1 
ATOM   396  H  HD21 B ASN   A 1 15  ? 19.890 -17.853 6.193   0.50 16.19 ?  15   ASN   A HD21 1 
ATOM   397  H  HD22 A ASN   A 1 15  ? 20.320 -17.120 7.987   0.50 16.86 ?  15   ASN   A HD22 1 
ATOM   398  H  HD22 B ASN   A 1 15  ? 20.362 -17.275 7.482   0.50 16.19 ?  15   ASN   A HD22 1 
ATOM   399  N  N    A VAL   A 1 16  ? 16.098 -16.371 9.050   0.50 12.10 ?  16   VAL   A N    1 
ATOM   400  N  N    B VAL   A 1 16  ? 16.314 -16.713 8.651   0.50 12.96 ?  16   VAL   A N    1 
ATOM   401  C  CA   A VAL   A 1 16  ? 15.746 -15.072 8.490   0.50 11.75 ?  16   VAL   A CA   1 
ATOM   402  C  CA   B VAL   A 1 16  ? 15.904 -15.440 8.061   0.50 12.61 ?  16   VAL   A CA   1 
ATOM   403  C  C    A VAL   A 1 16  ? 14.464 -14.572 9.143   0.50 12.03 ?  16   VAL   A C    1 
ATOM   404  C  C    B VAL   A 1 16  ? 14.646 -14.931 8.757   0.50 11.97 ?  16   VAL   A C    1 
ATOM   405  O  O    A VAL   A 1 16  ? 13.461 -15.296 9.208   0.50 12.02 ?  16   VAL   A O    1 
ATOM   406  O  O    B VAL   A 1 16  ? 13.639 -15.647 8.855   0.50 12.48 ?  16   VAL   A O    1 
ATOM   407  C  CB   A VAL   A 1 16  ? 15.608 -15.125 6.957   0.50 11.47 ?  16   VAL   A CB   1 
ATOM   408  C  CB   B VAL   A 1 16  ? 15.697 -15.545 6.539   0.50 13.22 ?  16   VAL   A CB   1 
ATOM   409  C  CG1  A VAL   A 1 16  ? 15.235 -13.749 6.412   0.50 11.47 ?  16   VAL   A CG1  1 
ATOM   410  C  CG1  B VAL   A 1 16  ? 15.236 -14.204 5.975   0.50 13.83 ?  16   VAL   A CG1  1 
ATOM   411  C  CG2  A VAL   A 1 16  ? 16.894 -15.618 6.314   0.50 12.56 ?  16   VAL   A CG2  1 
ATOM   412  C  CG2  B VAL   A 1 16  ? 16.974 -16.012 5.844   0.50 13.47 ?  16   VAL   A CG2  1 
ATOM   413  H  H    A VAL   A 1 16  ? 15.519 -16.981 8.880   0.50 14.51 ?  16   VAL   A H    1 
ATOM   414  H  H    B VAL   A 1 16  ? 15.763 -17.361 8.514   0.50 15.54 ?  16   VAL   A H    1 
ATOM   415  H  HA   A VAL   A 1 16  ? 16.444 -14.432 8.696   0.50 14.09 ?  16   VAL   A HA   1 
ATOM   416  H  HA   B VAL   A 1 16  ? 16.610 -14.794 8.213   0.50 15.12 ?  16   VAL   A HA   1 
ATOM   417  H  HB   A VAL   A 1 16  ? 14.897 -15.740 6.723   0.50 13.76 ?  16   VAL   A HB   1 
ATOM   418  H  HB   B VAL   A 1 16  ? 15.003 -16.198 6.359   0.50 15.85 ?  16   VAL   A HB   1 
ATOM   419  H  HG11 A VAL   A 1 16  ? 15.315 -13.760 5.444   0.50 13.76 ?  16   VAL   A HG11 1 
ATOM   420  H  HG11 B VAL   A 1 16  ? 15.264 -14.243 5.006   0.50 16.60 ?  16   VAL   A HG11 1 
ATOM   421  H  HG12 A VAL   A 1 16  ? 14.320 -13.544 6.661   0.50 13.76 ?  16   VAL   A HG12 1 
ATOM   422  H  HG12 B VAL   A 1 16  ? 14.327 -14.031 6.269   0.50 16.60 ?  16   VAL   A HG12 1 
ATOM   423  H  HG13 A VAL   A 1 16  ? 15.837 -13.087 6.785   0.50 13.76 ?  16   VAL   A HG13 1 
ATOM   424  H  HG13 B VAL   A 1 16  ? 15.828 -13.507 6.295   0.50 16.60 ?  16   VAL   A HG13 1 
ATOM   425  H  HG21 A VAL   A 1 16  ? 16.930 -15.312 5.394   0.50 15.07 ?  16   VAL   A HG21 1 
ATOM   426  H  HG21 B VAL   A 1 16  ? 16.953 -15.723 4.918   0.50 16.16 ?  16   VAL   A HG21 1 
ATOM   427  H  HG22 A VAL   A 1 16  ? 17.646 -15.270 6.812   0.50 15.07 ?  16   VAL   A HG22 1 
ATOM   428  H  HG22 B VAL   A 1 16  ? 17.739 -15.616 6.293   0.50 16.16 ?  16   VAL   A HG22 1 
ATOM   429  H  HG23 A VAL   A 1 16  ? 16.902 -16.588 6.342   0.50 15.07 ?  16   VAL   A HG23 1 
ATOM   430  H  HG23 B VAL   A 1 16  ? 17.028 -16.978 5.892   0.50 16.16 ?  16   VAL   A HG23 1 
ATOM   431  N  N    A TYR   A 1 17  ? 14.503 -13.317 9.595   0.50 12.08 ?  17   TYR   A N    1 
ATOM   432  N  N    B TYR   A 1 17  ? 14.696 -13.669 9.188   0.50 12.09 ?  17   TYR   A N    1 
ATOM   433  C  CA   A TYR   A 1 17  ? 13.404 -12.643 10.265  0.50 12.11 ?  17   TYR   A CA   1 
ATOM   434  C  CA   B TYR   A 1 17  ? 13.632 -12.994 9.918   0.50 12.22 ?  17   TYR   A CA   1 
ATOM   435  C  C    A TYR   A 1 17  ? 13.147 -11.326 9.553   0.50 12.97 ?  17   TYR   A C    1 
ATOM   436  C  C    B TYR   A 1 17  ? 13.361 -11.656 9.239   0.50 13.05 ?  17   TYR   A C    1 
ATOM   437  O  O    A TYR   A 1 17  ? 14.069 -10.736 8.987   0.50 12.59 ?  17   TYR   A O    1 
ATOM   438  O  O    B TYR   A 1 17  ? 14.238 -11.095 8.580   0.50 12.76 ?  17   TYR   A O    1 
ATOM   439  C  CB   A TYR   A 1 17  ? 13.774 -12.385 11.728  0.50 12.47 ?  17   TYR   A CB   1 
ATOM   440  C  CB   B TYR   A 1 17  ? 14.065 -12.742 11.370  0.50 12.40 ?  17   TYR   A CB   1 
ATOM   441  C  CG   A TYR   A 1 17  ? 13.950 -13.660 12.510  0.50 13.07 ?  17   TYR   A CG   1 
ATOM   442  C  CG   B TYR   A 1 17  ? 14.297 -13.998 12.188  0.50 13.54 ?  17   TYR   A CG   1 
ATOM   443  C  CD1  A TYR   A 1 17  ? 15.121 -14.408 12.424  0.50 13.58 ?  17   TYR   A CD1  1 
ATOM   444  C  CD1  B TYR   A 1 17  ? 15.476 -14.733 12.076  0.50 14.31 ?  17   TYR   A CD1  1 
ATOM   445  C  CD2  A TYR   A 1 17  ? 12.929 -14.135 13.318  0.50 13.29 ?  17   TYR   A CD2  1 
ATOM   446  C  CD2  B TYR   A 1 17  ? 13.337 -14.447 13.085  0.50 14.23 ?  17   TYR   A CD2  1 
ATOM   447  C  CE1  A TYR   A 1 17  ? 15.268 -15.594 13.136  0.50 13.92 ?  17   TYR   A CE1  1 
ATOM   448  C  CE1  B TYR   A 1 17  ? 15.681 -15.887 12.828  0.50 14.82 ?  17   TYR   A CE1  1 
ATOM   449  C  CE2  A TYR   A 1 17  ? 13.065 -15.318 14.030  0.50 13.55 ?  17   TYR   A CE2  1 
ATOM   450  C  CE2  B TYR   A 1 17  ? 13.535 -15.592 13.840  0.50 14.70 ?  17   TYR   A CE2  1 
ATOM   451  C  CZ   A TYR   A 1 17  ? 14.236 -16.044 13.939  0.50 13.74 ?  17   TYR   A CZ   1 
ATOM   452  C  CZ   B TYR   A 1 17  ? 14.706 -16.303 13.710  0.50 14.73 ?  17   TYR   A CZ   1 
ATOM   453  O  OH   A TYR   A 1 17  ? 14.369 -17.217 14.651  0.50 14.37 ?  17   TYR   A OH   1 
ATOM   454  O  OH   B TYR   A 1 17  ? 14.896 -17.440 14.463  0.50 15.29 ?  17   TYR   A OH   1 
ATOM   455  H  H    A TYR   A 1 17  ? 15.195 -12.807 9.511   0.50 14.49 ?  17   TYR   A H    1 
ATOM   456  H  H    B TYR   A 1 17  ? 15.372 -13.161 9.045   0.50 14.50 ?  17   TYR   A H    1 
ATOM   457  H  HA   A TYR   A 1 17  ? 12.598 -13.174 10.221  0.50 14.53 ?  17   TYR   A HA   1 
ATOM   458  H  HA   B TYR   A 1 17  ? 12.826 -13.536 9.907   0.50 14.66 ?  17   TYR   A HA   1 
ATOM   459  H  HB2  A TYR   A 1 17  ? 14.606 -11.891 11.760  0.50 14.96 ?  17   TYR   A HB2  1 
ATOM   460  H  HB2  B TYR   A 1 17  ? 14.892 -12.241 11.362  0.50 14.88 ?  17   TYR   A HB2  1 
ATOM   461  H  HB3  A TYR   A 1 17  ? 13.071 -11.868 12.148  0.50 14.96 ?  17   TYR   A HB3  1 
ATOM   462  H  HB3  B TYR   A 1 17  ? 13.372 -12.231 11.810  0.50 14.88 ?  17   TYR   A HB3  1 
ATOM   463  H  HD1  A TYR   A 1 17  ? 15.815 -14.108 11.883  0.50 16.29 ?  17   TYR   A HD1  1 
ATOM   464  H  HD1  B TYR   A 1 17  ? 16.134 -14.458 11.483  0.50 17.16 ?  17   TYR   A HD1  1 
ATOM   465  H  HD2  A TYR   A 1 17  ? 12.136 -13.655 13.386  0.50 15.94 ?  17   TYR   A HD2  1 
ATOM   466  H  HD2  B TYR   A 1 17  ? 12.543 -13.977 13.181  0.50 17.07 ?  17   TYR   A HD2  1 
ATOM   467  H  HE1  A TYR   A 1 17  ? 16.060 -16.081 13.070  0.50 16.69 ?  17   TYR   A HE1  1 
ATOM   468  H  HE1  B TYR   A 1 17  ? 16.475 -16.373 12.746  0.50 17.78 ?  17   TYR   A HE1  1 
ATOM   469  H  HE2  A TYR   A 1 17  ? 12.372 -15.622 14.573  0.50 16.26 ?  17   TYR   A HE2  1 
ATOM   470  H  HE2  B TYR   A 1 17  ? 12.882 -15.884 14.439  0.50 17.63 ?  17   TYR   A HE2  1 
ATOM   471  H  HH   A TYR   A 1 17  ? 13.626 -17.447 14.968  0.50 17.23 ?  17   TYR   A HH   1 
ATOM   472  H  HH   B TYR   A 1 17  ? 14.263 -17.542 15.009  0.50 18.34 ?  17   TYR   A HH   1 
ATOM   473  N  N    A ILE   A 1 18  ? 11.897 -10.856 9.569   0.50 13.60 ?  18   ILE   A N    1 
ATOM   474  N  N    B ILE   A 1 18  ? 12.145 -11.125 9.402   0.50 13.80 ?  18   ILE   A N    1 
ATOM   475  C  CA   A ILE   A 1 18  ? 11.521 -9.670  8.806   0.50 14.59 ?  18   ILE   A CA   1 
ATOM   476  C  CA   B ILE   A 1 18  ? 11.756 -9.913  8.682   0.50 14.41 ?  18   ILE   A CA   1 
ATOM   477  C  C    A ILE   A 1 18  ? 10.582 -8.804  9.631   0.50 15.37 ?  18   ILE   A C    1 
ATOM   478  C  C    B ILE   A 1 18  ? 10.769 -9.091  9.508   0.50 14.82 ?  18   ILE   A C    1 
ATOM   479  O  O    A ILE   A 1 18  ? 9.771  -9.303  10.418  0.50 15.65 ?  18   ILE   A O    1 
ATOM   480  O  O    B ILE   A 1 18  ? 9.933  -9.636  10.235  0.50 15.33 ?  18   ILE   A O    1 
ATOM   481  C  CB   A ILE   A 1 18  ? 10.914 -10.044 7.435   0.50 14.99 ?  18   ILE   A CB   1 
ATOM   482  C  CB   B ILE   A 1 18  ? 11.212 -10.265 7.276   0.50 14.34 ?  18   ILE   A CB   1 
ATOM   483  C  CG1  A ILE   A 1 18  ? 10.906 -8.849  6.479   0.50 16.23 ?  18   ILE   A CG1  1 
ATOM   484  C  CG1  B ILE   A 1 18  ? 11.064 -9.006  6.426   0.50 15.43 ?  18   ILE   A CG1  1 
ATOM   485  C  CG2  A ILE   A 1 18  ? 9.516  -10.639 7.600   0.50 15.50 ?  18   ILE   A CG2  1 
ATOM   486  C  CG2  B ILE   A 1 18  ? 9.889  -11.040 7.379   0.50 13.91 ?  18   ILE   A CG2  1 
ATOM   487  C  CD1  A ILE   A 1 18  ? 10.637 -9.247  5.042   0.50 17.67 ?  18   ILE   A CD1  1 
ATOM   488  C  CD1  B ILE   A 1 18  ? 10.792 -9.298  4.978   0.50 16.74 ?  18   ILE   A CD1  1 
ATOM   489  H  H    A ILE   A 1 18  ? 11.244 -11.205 10.016  0.50 16.31 ?  18   ILE   A H    1 
ATOM   490  H  H    B ILE   A 1 18  ? 11.539 -11.455 9.914   0.50 16.55 ?  18   ILE   A H    1 
ATOM   491  H  HA   A ILE   A 1 18  ? 12.313 -9.144  8.635   0.50 17.50 ?  18   ILE   A HA   1 
ATOM   492  H  HA   B ILE   A 1 18  ? 12.554 -9.378  8.552   0.50 17.28 ?  18   ILE   A HA   1 
ATOM   493  H  HB   A ILE   A 1 18  ? 11.475 -10.726 7.047   0.50 17.98 ?  18   ILE   A HB   1 
ATOM   494  H  HB   B ILE   A 1 18  ? 11.857 -10.846 6.840   0.50 17.20 ?  18   ILE   A HB   1 
ATOM   495  H  HG12 A ILE   A 1 18  ? 10.215 -8.225  6.747   0.50 19.48 ?  18   ILE   A HG12 1 
ATOM   496  H  HG12 B ILE   A 1 18  ? 10.327 -8.482  6.769   0.50 18.51 ?  18   ILE   A HG12 1 
ATOM   497  H  HG13 A ILE   A 1 18  ? 11.774 -8.415  6.505   0.50 19.48 ?  18   ILE   A HG13 1 
ATOM   498  H  HG13 B ILE   A 1 18  ? 11.888 -8.498  6.476   0.50 18.51 ?  18   ILE   A HG13 1 
ATOM   499  H  HG21 A ILE   A 1 18  ? 9.125  -10.776 6.722   0.50 18.59 ?  18   ILE   A HG21 1 
ATOM   500  H  HG21 B ILE   A 1 18  ? 9.646  -11.372 6.498   0.50 16.69 ?  18   ILE   A HG21 1 
ATOM   501  H  HG22 A ILE   A 1 18  ? 9.592  -11.485 8.061   0.50 18.59 ?  18   ILE   A HG22 1 
ATOM   502  H  HG22 B ILE   A 1 18  ? 10.007 -11.789 7.987   0.50 16.69 ?  18   ILE   A HG22 1 
ATOM   503  H  HG23 A ILE   A 1 18  ? 8.954  -10.038 8.112   0.50 18.59 ?  18   ILE   A HG23 1 
ATOM   504  H  HG23 B ILE   A 1 18  ? 9.199  -10.450 7.712   0.50 16.69 ?  18   ILE   A HG23 1 
ATOM   505  H  HD11 A ILE   A 1 18  ? 10.821 -8.491  4.463   0.50 21.20 ?  18   ILE   A HD11 1 
ATOM   506  H  HD11 B ILE   A 1 18  ? 10.785 -8.461  4.487   0.50 20.08 ?  18   ILE   A HD11 1 
ATOM   507  H  HD12 A ILE   A 1 18  ? 11.215 -9.990  4.807   0.50 21.20 ?  18   ILE   A HD12 1 
ATOM   508  H  HD12 B ILE   A 1 18  ? 11.488 -9.878  4.636   0.50 20.08 ?  18   ILE   A HD12 1 
ATOM   509  H  HD13 A ILE   A 1 18  ? 9.708  -9.511  4.955   0.50 21.20 ?  18   ILE   A HD13 1 
ATOM   510  H  HD13 B ILE   A 1 18  ? 9.928  -9.733  4.901   0.50 20.08 ?  18   ILE   A HD13 1 
ATOM   511  N  N    A LYS   A 1 19  ? 10.684 -7.490  9.429   0.50 15.70 ?  19   LYS   A N    1 
ATOM   512  N  N    B LYS   A 1 19  ? 10.861 -7.763  9.368   0.50 15.60 ?  19   LYS   A N    1 
ATOM   513  C  CA   A LYS   A 1 19  ? 9.920  -6.539  10.221  0.50 16.45 ?  19   LYS   A CA   1 
ATOM   514  C  CA   B LYS   A 1 19  ? 10.011 -6.817  10.090  0.50 16.94 ?  19   LYS   A CA   1 
ATOM   515  C  C    A LYS   A 1 19  ? 9.727  -5.277  9.398   0.50 16.76 ?  19   LYS   A C    1 
ATOM   516  C  C    B LYS   A 1 19  ? 9.796  -5.557  9.253   0.50 16.64 ?  19   LYS   A C    1 
ATOM   517  O  O    A LYS   A 1 19  ? 10.678 -4.799  8.777   0.50 16.69 ?  19   LYS   A O    1 
ATOM   518  O  O    B LYS   A 1 19  ? 10.635 -5.192  8.425   0.50 15.53 ?  19   LYS   A O    1 
ATOM   519  C  CB   A LYS   A 1 19  ? 10.687 -6.227  11.512  0.50 17.22 ?  19   LYS   A CB   1 
ATOM   520  C  CB   B LYS   A 1 19  ? 10.642 -6.429  11.436  0.50 18.32 ?  19   LYS   A CB   1 
ATOM   521  C  CG   A LYS   A 1 19  ? 10.015 -5.288  12.491  0.50 17.66 ?  19   LYS   A CG   1 
ATOM   522  C  CG   B LYS   A 1 19  ? 9.798  -5.505  12.316  0.50 19.30 ?  19   LYS   A CG   1 
ATOM   523  C  CD   A LYS   A 1 19  ? 10.928 -5.088  13.694  0.50 18.06 ?  19   LYS   A CD   1 
ATOM   524  C  CD   B LYS   A 1 19  ? 10.592 -5.041  13.532  0.50 19.99 ?  19   LYS   A CD   1 
ATOM   525  C  CE   A LYS   A 1 19  ? 10.307 -4.188  14.739  0.50 18.42 ?  19   LYS   A CE   1 
ATOM   526  C  CE   B LYS   A 1 19  ? 9.783  -4.122  14.436  0.50 20.26 ?  19   LYS   A CE   1 
ATOM   527  N  NZ   A LYS   A 1 19  ? 11.198 -4.029  15.921  0.50 18.34 ?  19   LYS   A NZ   1 
ATOM   528  N  NZ   B LYS   A 1 19  ? 10.605 -3.628  15.578  0.50 20.28 ?  19   LYS   A NZ   1 
ATOM   529  H  H    A LYS   A 1 19  ? 11.193 -7.109  8.835   0.50 18.83 ?  19   LYS   A H    1 
ATOM   530  H  H    B LYS   A 1 19  ? 11.427 -7.389  8.846   0.50 18.72 ?  19   LYS   A H    1 
ATOM   531  H  HA   A LYS   A 1 19  ? 9.052  -6.903  10.448  0.50 19.73 ?  19   LYS   A HA   1 
ATOM   532  H  HA   B LYS   A 1 19  ? 9.152  -7.231  10.261  0.50 20.32 ?  19   LYS   A HA   1 
ATOM   533  H  HB2  A LYS   A 1 19  ? 10.838 -7.063  11.981  0.50 20.66 ?  19   LYS   A HB2  1 
ATOM   534  H  HB2  B LYS   A 1 19  ? 10.804 -7.239  11.942  0.50 21.98 ?  19   LYS   A HB2  1 
ATOM   535  H  HB3  A LYS   A 1 19  ? 11.540 -5.833  11.276  0.50 20.66 ?  19   LYS   A HB3  1 
ATOM   536  H  HB3  B LYS   A 1 19  ? 11.482 -5.979  11.263  0.50 21.98 ?  19   LYS   A HB3  1 
ATOM   537  H  HG2  A LYS   A 1 19  ? 9.862  -4.429  12.071  0.50 21.18 ?  19   LYS   A HG2  1 
ATOM   538  H  HG2  B LYS   A 1 19  ? 9.537  -4.719  11.814  0.50 23.16 ?  19   LYS   A HG2  1 
ATOM   539  H  HG3  A LYS   A 1 19  ? 9.180  -5.676  12.797  0.50 21.18 ?  19   LYS   A HG3  1 
ATOM   540  H  HG3  B LYS   A 1 19  ? 9.014  -5.983  12.630  0.50 23.16 ?  19   LYS   A HG3  1 
ATOM   541  H  HD2  A LYS   A 1 19  ? 11.106 -5.951  14.103  0.50 21.67 ?  19   LYS   A HD2  1 
ATOM   542  H  HD2  B LYS   A 1 19  ? 10.860 -5.814  14.053  0.50 23.98 ?  19   LYS   A HD2  1 
ATOM   543  H  HD3  A LYS   A 1 19  ? 11.758 -4.683  13.397  0.50 21.67 ?  19   LYS   A HD3  1 
ATOM   544  H  HD3  B LYS   A 1 19  ? 11.377 -4.553  13.233  0.50 23.98 ?  19   LYS   A HD3  1 
ATOM   545  H  HE2  A LYS   A 1 19  ? 10.153 -3.311  14.353  0.50 22.10 ?  19   LYS   A HE2  1 
ATOM   546  H  HE2  B LYS   A 1 19  ? 9.478  -3.355  13.926  0.50 24.30 ?  19   LYS   A HE2  1 
ATOM   547  H  HE3  A LYS   A 1 19  ? 9.470  -4.575  15.038  0.50 22.10 ?  19   LYS   A HE3  1 
ATOM   548  H  HE3  B LYS   A 1 19  ? 9.026  -4.609  14.796  0.50 24.30 ?  19   LYS   A HE3  1 
ATOM   549  H  HZ1  A LYS   A 1 19  ? 10.816 -3.493  16.518  0.50 22.00 ?  19   LYS   A HZ1  1 
ATOM   550  H  HZ1  B LYS   A 1 19  ? 10.118 -3.092  16.095  0.50 24.33 ?  19   LYS   A HZ1  1 
ATOM   551  H  HZ2  A LYS   A 1 19  ? 11.348 -4.822  16.296  0.50 22.00 ?  19   LYS   A HZ2  1 
ATOM   552  H  HZ2  B LYS   A 1 19  ? 10.896 -4.314  16.063  0.50 24.33 ?  19   LYS   A HZ2  1 
ATOM   553  H  HZ3  A LYS   A 1 19  ? 11.975 -3.676  15.671  0.50 22.00 ?  19   LYS   A HZ3  1 
ATOM   554  H  HZ3  B LYS   A 1 19  ? 11.307 -3.173  15.271  0.50 24.33 ?  19   LYS   A HZ3  1 
ATOM   555  N  N    A ASN   A 1 20  ? 8.496  -4.767  9.360   0.50 17.44 ?  20   ASN   A N    1 
ATOM   556  N  N    B ASN   A 1 20  ? 8.664  -4.887  9.489   0.50 18.04 ?  20   ASN   A N    1 
ATOM   557  C  CA   A ASN   A 1 20  ? 8.268  -3.416  8.866   0.50 18.43 ?  20   ASN   A CA   1 
ATOM   558  C  CA   B ASN   A 1 20  ? 8.333  -3.616  8.834   0.50 19.08 ?  20   ASN   A CA   1 
ATOM   559  C  C    A ASN   A 1 20  ? 8.929  -2.462  9.848   0.50 18.84 ?  20   ASN   A C    1 
ATOM   560  C  C    B ASN   A 1 20  ? 8.851  -2.482  9.712   0.50 19.58 ?  20   ASN   A C    1 
ATOM   561  O  O    A ASN   A 1 20  ? 8.495  -2.345  10.998  0.50 19.12 ?  20   ASN   A O    1 
ATOM   562  O  O    B ASN   A 1 20  ? 8.170  -2.018  10.629  0.50 20.30 ?  20   ASN   A O    1 
ATOM   563  C  CB   A ASN   A 1 20  ? 6.770  -3.146  8.741   0.50 18.96 ?  20   ASN   A CB   1 
ATOM   564  C  CB   B ASN   A 1 20  ? 6.824  -3.517  8.612   0.50 19.74 ?  20   ASN   A CB   1 
ATOM   565  C  CG   A ASN   A 1 20  ? 6.455  -1.696  8.410   0.50 19.93 ?  20   ASN   A CG   1 
ATOM   566  C  CG   B ASN   A 1 20  ? 6.380  -2.152  8.087   0.50 20.61 ?  20   ASN   A CG   1 
ATOM   567  O  OD1  A ASN   A 1 20  ? 5.573  -1.091  9.020   0.50 21.40 ?  20   ASN   A OD1  1 
ATOM   568  O  OD1  B ASN   A 1 20  ? 5.287  -1.671  8.417   0.50 21.51 ?  20   ASN   A OD1  1 
ATOM   569  N  ND2  A ASN   A 1 20  ? 7.174  -1.132  7.445   0.50 19.81 ?  20   ASN   A ND2  1 
ATOM   570  N  ND2  B ASN   A 1 20  ? 7.218  -1.527  7.265   0.50 21.33 ?  20   ASN   A ND2  1 
ATOM   571  H  H    A ASN   A 1 20  ? 7.785  -5.178  9.608   0.50 20.93 ?  20   ASN   A H    1 
ATOM   572  H  H    B ASN   A 1 20  ? 8.062  -5.160  10.034  0.50 21.64 ?  20   ASN   A H    1 
ATOM   573  H  HA   A ASN   A 1 20  ? 8.675  -3.308  7.994   0.50 22.11 ?  20   ASN   A HA   1 
ATOM   574  H  HA   B ASN   A 1 20  ? 8.783  -3.570  7.974   0.50 22.89 ?  20   ASN   A HA   1 
ATOM   575  H  HB2  A ASN   A 1 20  ? 6.407  -3.703  8.031   0.50 22.74 ?  20   ASN   A HB2  1 
ATOM   576  H  HB2  B ASN   A 1 20  ? 6.555  -4.182  7.968   0.50 23.68 ?  20   ASN   A HB2  1 
ATOM   577  H  HB3  A ASN   A 1 20  ? 6.336  -3.359  9.580   0.50 22.74 ?  20   ASN   A HB3  1 
ATOM   578  H  HB3  B ASN   A 1 20  ? 6.377  -3.677  9.455   0.50 23.68 ?  20   ASN   A HB3  1 
ATOM   579  H  HD21 A ASN   A 1 20  ? 7.028  -0.315  7.220   0.50 23.76 ?  20   ASN   A HD21 1 
ATOM   580  H  HD21 B ASN   A 1 20  ? 7.008  -0.757  6.948   0.50 25.59 ?  20   ASN   A HD21 1 
ATOM   581  H  HD22 A ASN   A 1 20  ? 7.789  -1.584  7.045   0.50 23.76 ?  20   ASN   A HD22 1 
ATOM   582  H  HD22 B ASN   A 1 20  ? 7.969  -1.889  7.050   0.50 25.59 ?  20   ASN   A HD22 1 
ATOM   583  N  N    A ALA   A 1 21  ? 10.018 -1.826  9.426   0.50 18.87 ?  21   ALA   A N    1 
ATOM   584  N  N    B ALA   A 1 21  ? 10.069 -2.017  9.427   0.50 19.21 ?  21   ALA   A N    1 
ATOM   585  C  CA   A ALA   A 1 21  ? 10.767 -0.991  10.351  0.50 18.45 ?  21   ALA   A CA   1 
ATOM   586  C  CA   B ALA   A 1 21  ? 10.673 -0.967  10.240  0.50 18.97 ?  21   ALA   A CA   1 
ATOM   587  C  C    A ALA   A 1 21  ? 11.725 -0.106  9.575   0.50 18.13 ?  21   ALA   A C    1 
ATOM   588  C  C    B ALA   A 1 21  ? 11.788 -0.276  9.468   0.50 17.85 ?  21   ALA   A C    1 
ATOM   589  O  O    A ALA   A 1 21  ? 12.184 -0.470  8.489   0.50 18.34 ?  21   ALA   A O    1 
ATOM   590  O  O    B ALA   A 1 21  ? 12.278 -0.785  8.458   0.50 17.59 ?  21   ALA   A O    1 
ATOM   591  C  CB   A ALA   A 1 21  ? 11.550 -1.847  11.349  0.50 18.82 ?  21   ALA   A CB   1 
ATOM   592  C  CB   B ALA   A 1 21  ? 11.205 -1.515  11.569  0.50 20.16 ?  21   ALA   A CB   1 
ATOM   593  H  H    A ALA   A 1 21  ? 10.337 -1.866  8.630   0.50 22.64 ?  21   ALA   A H    1 
ATOM   594  H  H    B ALA   A 1 21  ? 10.557 -2.287  8.770   0.50 23.04 ?  21   ALA   A H    1 
ATOM   595  H  HA   A ALA   A 1 21  ? 10.152 -0.422  10.843  0.50 22.13 ?  21   ALA   A HA   1 
ATOM   596  H  HA   B ALA   A 1 21  ? 9.995  -0.305  10.443  0.50 22.76 ?  21   ALA   A HA   1 
ATOM   597  H  HB1  A ALA   A 1 21  ? 12.007 -1.259  11.964  0.50 22.58 ?  21   ALA   A HB1  1 
ATOM   598  H  HB1  B ALA   A 1 21  ? 11.594 -0.786  12.078  0.50 24.18 ?  21   ALA   A HB1  1 
ATOM   599  H  HB2  A ALA   A 1 21  ? 10.923 -2.410  11.831  0.50 22.58 ?  21   ALA   A HB2  1 
ATOM   600  H  HB2  B ALA   A 1 21  ? 10.470 -1.909  12.068  0.50 24.18 ?  21   ALA   A HB2  1 
ATOM   601  H  HB3  A ALA   A 1 21  ? 12.184 -2.392  10.864  0.50 22.58 ?  21   ALA   A HB3  1 
ATOM   602  H  HB3  B ALA   A 1 21  ? 11.879 -2.189  11.388  0.50 24.18 ?  21   ALA   A HB3  1 
ATOM   603  N  N    A ASP   A 1 22  ? 12.011 1.061   10.152  0.50 17.91 ?  22   ASP   A N    1 
ATOM   604  N  N    B ASP   A 1 22  ? 12.163 0.908   9.961   0.50 17.35 ?  22   ASP   A N    1 
ATOM   605  C  CA   A ASP   A 1 22  ? 13.055 1.945   9.654   0.50 17.38 ?  22   ASP   A CA   1 
ATOM   606  C  CA   B ASP   A 1 22  ? 13.316 1.657   9.463   0.50 17.28 ?  22   ASP   A CA   1 
ATOM   607  C  C    A ASP   A 1 22  ? 14.388 1.451   10.201  0.50 16.03 ?  22   ASP   A C    1 
ATOM   608  C  C    B ASP   A 1 22  ? 14.580 1.064   10.076  0.50 15.42 ?  22   ASP   A C    1 
ATOM   609  O  O    A ASP   A 1 22  ? 14.609 1.467   11.416  0.50 16.20 ?  22   ASP   A O    1 
ATOM   610  O  O    B ASP   A 1 22  ? 14.697 0.972   11.301  0.50 15.33 ?  22   ASP   A O    1 
ATOM   611  C  CB   A ASP   A 1 22  ? 12.778 3.369   10.133  0.50 18.56 ?  22   ASP   A CB   1 
ATOM   612  C  CB   B ASP   A 1 22  ? 13.166 3.122   9.881   0.50 18.47 ?  22   ASP   A CB   1 
ATOM   613  C  CG   A ASP   A 1 22  ? 13.781 4.378   9.598   0.50 19.39 ?  22   ASP   A CG   1 
ATOM   614  C  CG   B ASP   A 1 22  ? 14.247 4.032   9.317   0.50 19.31 ?  22   ASP   A CG   1 
ATOM   615  O  OD1  A ASP   A 1 22  ? 14.875 3.983   9.152   0.50 19.07 ?  22   ASP   A OD1  1 
ATOM   616  O  OD1  B ASP   A 1 22  ? 15.238 3.533   8.749   0.50 18.93 ?  22   ASP   A OD1  1 
ATOM   617  O  OD2  A ASP   A 1 22  ? 13.470 5.586   9.626   0.50 20.53 -1 22   ASP   A OD2  1 
ATOM   618  O  OD2  B ASP   A 1 22  ? 14.102 5.267   9.454   0.50 20.86 -1 22   ASP   A OD2  1 
ATOM   619  H  H    A ASP   A 1 22  ? 11.602 1.367   10.847  0.50 21.49 ?  22   ASP   A H    1 
ATOM   620  H  H    B ASP   A 1 22  ? 11.737 1.312   10.593  0.50 20.82 ?  22   ASP   A H    1 
ATOM   621  H  HA   A ASP   A 1 22  ? 13.080 1.933   8.685   0.50 20.85 ?  22   ASP   A HA   1 
ATOM   622  H  HA   B ASP   A 1 22  ? 13.361 1.587   8.495   0.50 20.73 ?  22   ASP   A HA   1 
ATOM   623  H  HB2  A ASP   A 1 22  ? 11.897 3.642   9.831   0.50 22.26 ?  22   ASP   A HB2  1 
ATOM   624  H  HB2  B ASP   A 1 22  ? 12.309 3.448   9.582   0.50 22.16 ?  22   ASP   A HB2  1 
ATOM   625  H  HB3  A ASP   A 1 22  ? 12.809 3.388   11.105  0.50 22.26 ?  22   ASP   A HB3  1 
ATOM   626  H  HB3  B ASP   A 1 22  ? 13.242 3.182   10.840  0.50 22.16 ?  22   ASP   A HB3  1 
ATOM   627  N  N    A ILE   A 1 23  ? 15.271 1.000   9.307   0.50 15.42 ?  23   ILE   A N    1 
ATOM   628  N  N    B ILE   A 1 23  ? 15.528 0.666   9.223   0.50 14.58 ?  23   ILE   A N    1 
ATOM   629  C  CA   A ILE   A 1 23  ? 16.540 0.418   9.738   0.50 14.61 ?  23   ILE   A CA   1 
ATOM   630  C  CA   B ILE   A 1 23  ? 16.763 0.049   9.697   0.50 14.13 ?  23   ILE   A CA   1 
ATOM   631  C  C    A ILE   A 1 23  ? 17.329 1.394   10.596  0.50 14.61 ?  23   ILE   A C    1 
ATOM   632  C  C    B ILE   A 1 23  ? 17.516 0.983   10.636  0.50 14.18 ?  23   ILE   A C    1 
ATOM   633  O  O    A ILE   A 1 23  ? 18.061 0.981   11.504  0.50 14.97 ?  23   ILE   A O    1 
ATOM   634  O  O    B ILE   A 1 23  ? 18.194 0.531   11.566  0.50 14.04 ?  23   ILE   A O    1 
ATOM   635  C  CB   A ILE   A 1 23  ? 17.343 -0.090  8.522   0.50 13.99 ?  23   ILE   A CB   1 
ATOM   636  C  CB   B ILE   A 1 23  ? 17.632 -0.425  8.508   0.50 13.56 ?  23   ILE   A CB   1 
ATOM   637  C  CG1  A ILE   A 1 23  ? 18.521 -0.952  8.986   0.50 14.12 ?  23   ILE   A CG1  1 
ATOM   638  C  CG1  B ILE   A 1 23  ? 18.714 -1.391  8.998   0.50 13.16 ?  23   ILE   A CG1  1 
ATOM   639  C  CG2  A ILE   A 1 23  ? 17.790 1.076   7.641   0.50 13.84 ?  23   ILE   A CG2  1 
ATOM   640  C  CG2  B ILE   A 1 23  ? 18.251 0.759   7.760   0.50 13.99 ?  23   ILE   A CG2  1 
ATOM   641  C  CD1  A ILE   A 1 23  ? 19.221 -1.681  7.861   0.50 14.27 ?  23   ILE   A CD1  1 
ATOM   642  C  CD1  B ILE   A 1 23  ? 19.535 -2.020  7.888   0.50 12.99 ?  23   ILE   A CD1  1 
ATOM   643  H  H    A ILE   A 1 23  ? 15.153 1.016   8.461   0.50 18.49 ?  23   ILE   A H    1 
ATOM   644  H  H    B ILE   A 1 23  ? 15.481 0.741   8.381   0.50 17.49 ?  23   ILE   A H    1 
ATOM   645  H  HA   A ILE   A 1 23  ? 16.347 -0.348  10.295  0.50 17.52 ?  23   ILE   A HA   1 
ATOM   646  H  HA   B ILE   A 1 23  ? 16.527 -0.742  10.202  0.50 16.95 ?  23   ILE   A HA   1 
ATOM   647  H  HB   A ILE   A 1 23  ? 16.755 -0.650  7.999   0.50 16.79 ?  23   ILE   A HB   1 
ATOM   648  H  HB   B ILE   A 1 23  ? 17.062 -0.908  7.886   0.50 16.27 ?  23   ILE   A HB   1 
ATOM   649  H  HG12 A ILE   A 1 23  ? 19.175 -0.385  9.423   0.50 16.93 ?  23   ILE   A HG12 1 
ATOM   650  H  HG12 B ILE   A 1 23  ? 19.324 -0.910  9.577   0.50 15.79 ?  23   ILE   A HG12 1 
ATOM   651  H  HG13 A ILE   A 1 23  ? 18.194 -1.619  9.612   0.50 16.93 ?  23   ILE   A HG13 1 
ATOM   652  H  HG13 B ILE   A 1 23  ? 18.290 -2.110  9.492   0.50 15.79 ?  23   ILE   A HG13 1 
ATOM   653  H  HG21 A ILE   A 1 23  ? 18.163 0.722   6.818   0.50 16.60 ?  23   ILE   A HG21 1 
ATOM   654  H  HG21 B ILE   A 1 23  ? 18.624 0.442   6.918   0.50 16.78 ?  23   ILE   A HG21 1 
ATOM   655  H  HG22 A ILE   A 1 23  ? 17.020 1.632   7.440   0.50 16.60 ?  23   ILE   A HG22 1 
ATOM   656  H  HG22 B ILE   A 1 23  ? 17.562 1.416   7.586   0.50 16.78 ?  23   ILE   A HG22 1 
ATOM   657  H  HG23 A ILE   A 1 23  ? 18.458 1.596   8.112   0.50 16.60 ?  23   ILE   A HG23 1 
ATOM   658  H  HG23 B ILE   A 1 23  ? 18.953 1.146   8.304   0.50 16.78 ?  23   ILE   A HG23 1 
ATOM   659  H  HD11 A ILE   A 1 23  ? 19.912 -2.248  8.235   0.50 17.12 ?  23   ILE   A HD11 1 
ATOM   660  H  HD11 B ILE   A 1 23  ? 20.134 -2.679  8.275   0.50 15.59 ?  23   ILE   A HD11 1 
ATOM   661  H  HD12 A ILE   A 1 23  ? 18.571 -2.221  7.384   0.50 17.12 ?  23   ILE   A HD12 1 
ATOM   662  H  HD12 B ILE   A 1 23  ? 18.936 -2.449  7.257   0.50 15.59 ?  23   ILE   A HD12 1 
ATOM   663  H  HD13 A ILE   A 1 23  ? 19.614 -1.030  7.260   0.50 17.12 ?  23   ILE   A HD13 1 
ATOM   664  H  HD13 B ILE   A 1 23  ? 20.047 -1.329  7.443   0.50 15.59 ?  23   ILE   A HD13 1 
ATOM   665  N  N    A VAL   A 1 24  ? 17.179 2.697   10.349  0.50 15.03 ?  24   VAL   A N    1 
ATOM   666  N  N    B VAL   A 1 24  ? 17.397 2.293   10.424  0.50 15.33 ?  24   VAL   A N    1 
ATOM   667  C  CA   A VAL   A 1 24  ? 17.839 3.692   11.191  0.50 15.80 ?  24   VAL   A CA   1 
ATOM   668  C  CA   B VAL   A 1 24  ? 18.067 3.253   11.297  0.50 16.56 ?  24   VAL   A CA   1 
ATOM   669  C  C    A VAL   A 1 24  ? 17.331 3.592   12.622  0.50 16.41 ?  24   VAL   A C    1 
ATOM   670  C  C    B VAL   A 1 24  ? 17.505 3.167   12.710  0.50 17.39 ?  24   VAL   A C    1 
ATOM   671  O  O    A VAL   A 1 24  ? 18.113 3.513   13.576  0.50 16.87 ?  24   VAL   A O    1 
ATOM   672  O  O    B VAL   A 1 24  ? 18.251 3.196   13.696  0.50 17.72 ?  24   VAL   A O    1 
ATOM   673  C  CB   A VAL   A 1 24  ? 17.635 5.105   10.615  0.50 16.39 ?  24   VAL   A CB   1 
ATOM   674  C  CB   B VAL   A 1 24  ? 17.947 4.670   10.709  0.50 17.55 ?  24   VAL   A CB   1 
ATOM   675  C  CG1  A VAL   A 1 24  ? 18.139 6.162   11.596  0.50 16.94 ?  24   VAL   A CG1  1 
ATOM   676  C  CG1  B VAL   A 1 24  ? 18.539 5.693   11.659  0.50 18.59 ?  24   VAL   A CG1  1 
ATOM   677  C  CG2  A VAL   A 1 24  ? 18.335 5.239   9.273   0.50 16.69 ?  24   VAL   A CG2  1 
ATOM   678  C  CG2  B VAL   A 1 24  ? 18.629 4.733   9.350   0.50 17.94 ?  24   VAL   A CG2  1 
ATOM   679  H  H    A VAL   A 1 24  ? 16.707 3.029   9.712   0.50 18.03 ?  24   VAL   A H    1 
ATOM   680  H  H    B VAL   A 1 24  ? 16.943 2.646   9.791   0.50 18.39 ?  24   VAL   A H    1 
ATOM   681  H  HA   A VAL   A 1 24  ? 18.790 3.519   11.205  0.50 18.95 ?  24   VAL   A HA   1 
ATOM   682  H  HA   B VAL   A 1 24  ? 19.011 3.030   11.341  0.50 19.87 ?  24   VAL   A HA   1 
ATOM   683  H  HB   A VAL   A 1 24  ? 16.687 5.262   10.472  0.50 19.66 ?  24   VAL   A HB   1 
ATOM   684  H  HB   B VAL   A 1 24  ? 17.010 4.881   10.583  0.50 21.06 ?  24   VAL   A HB   1 
ATOM   685  H  HG11 A VAL   A 1 24  ? 18.267 6.998   11.120  0.50 20.32 ?  24   VAL   A HG11 1 
ATOM   686  H  HG11 B VAL   A 1 24  ? 18.934 6.408   11.137  0.50 22.30 ?  24   VAL   A HG11 1 
ATOM   687  H  HG12 A VAL   A 1 24  ? 17.483 6.280   12.300  0.50 20.32 ?  24   VAL   A HG12 1 
ATOM   688  H  HG12 B VAL   A 1 24  ? 17.827 6.045   12.213  0.50 22.30 ?  24   VAL   A HG12 1 
ATOM   689  H  HG13 A VAL   A 1 24  ? 18.983 5.865   11.970  0.50 20.32 ?  24   VAL   A HG13 1 
ATOM   690  H  HG13 B VAL   A 1 24  ? 19.218 5.268   12.205  0.50 22.30 ?  24   VAL   A HG13 1 
ATOM   691  H  HG21 A VAL   A 1 24  ? 18.103 6.095   8.878   0.50 20.03 ?  24   VAL   A HG21 1 
ATOM   692  H  HG21 B VAL   A 1 24  ? 18.474 5.606   8.959   0.50 21.52 ?  24   VAL   A HG21 1 
ATOM   693  H  HG22 A VAL   A 1 24  ? 19.293 5.190   9.412   0.50 20.03 ?  24   VAL   A HG22 1 
ATOM   694  H  HG22 B VAL   A 1 24  ? 19.582 4.591   9.469   0.50 21.52 ?  24   VAL   A HG22 1 
ATOM   695  H  HG23 A VAL   A 1 24  ? 18.045 4.519   8.693   0.50 20.03 ?  24   VAL   A HG23 1 
ATOM   696  H  HG23 B VAL   A 1 24  ? 18.262 4.044   8.774   0.50 21.52 ?  24   VAL   A HG23 1 
ATOM   697  N  N    A GLU   A 1 25  ? 16.007 3.601   12.792  0.50 17.15 ?  25   GLU   A N    1 
ATOM   698  N  N    B GLU   A 1 25  ? 16.183 3.035   12.827  0.50 17.96 ?  25   GLU   A N    1 
ATOM   699  C  CA   A GLU   A 1 25  ? 15.440 3.551   14.136  0.50 17.87 ?  25   GLU   A CA   1 
ATOM   700  C  CA   B GLU   A 1 25  ? 15.558 2.923   14.141  0.50 19.20 ?  25   GLU   A CA   1 
ATOM   701  C  C    A GLU   A 1 25  ? 15.669 2.191   14.784  0.50 17.06 ?  25   GLU   A C    1 
ATOM   702  C  C    B GLU   A 1 25  ? 15.859 1.575   14.786  0.50 18.62 ?  25   GLU   A C    1 
ATOM   703  O  O    A GLU   A 1 25  ? 15.904 2.107   15.994  0.50 17.58 ?  25   GLU   A O    1 
ATOM   704  O  O    B GLU   A 1 25  ? 16.109 1.506   15.994  0.50 18.58 ?  25   GLU   A O    1 
ATOM   705  C  CB   A GLU   A 1 25  ? 13.953 3.911   14.097  0.50 19.77 ?  25   GLU   A CB   1 
ATOM   706  C  CB   B GLU   A 1 25  ? 14.051 3.157   14.022  0.50 20.80 ?  25   GLU   A CB   1 
ATOM   707  C  CG   A GLU   A 1 25  ? 13.697 5.373   13.750  0.50 22.09 ?  25   GLU   A CG   1 
ATOM   708  C  CG   B GLU   A 1 25  ? 13.695 4.536   13.496  0.50 22.90 ?  25   GLU   A CG   1 
ATOM   709  C  CD   A GLU   A 1 25  ? 14.503 6.332   14.610  0.50 24.05 ?  25   GLU   A CD   1 
ATOM   710  C  CD   B GLU   A 1 25  ? 14.208 5.639   14.399  0.50 24.84 ?  25   GLU   A CD   1 
ATOM   711  O  OE1  A GLU   A 1 25  ? 14.531 6.151   15.845  0.50 24.68 ?  25   GLU   A OE1  1 
ATOM   712  O  OE1  B GLU   A 1 25  ? 14.213 5.439   15.634  0.50 25.63 ?  25   GLU   A OE1  1 
ATOM   713  O  OE2  A GLU   A 1 25  ? 15.131 7.253   14.045  0.50 25.14 -1 25   GLU   A OE2  1 
ATOM   714  O  OE2  B GLU   A 1 25  ? 14.614 6.698   13.876  0.50 25.93 -1 25   GLU   A OE2  1 
ATOM   715  H  H    A GLU   A 1 25  ? 15.425 3.648   12.157  0.50 20.57 ?  25   GLU   A H    1 
ATOM   716  H  H    B GLU   A 1 25  ? 15.636 3.002   12.170  0.50 21.55 ?  25   GLU   A H    1 
ATOM   717  H  HA   A GLU   A 1 25  ? 15.890 4.208   14.687  0.50 21.44 ?  25   GLU   A HA   1 
ATOM   718  H  HA   B GLU   A 1 25  ? 15.923 3.603   14.722  0.50 23.04 ?  25   GLU   A HA   1 
ATOM   719  H  HB2  A GLU   A 1 25  ? 13.510 3.369   13.423  0.50 23.72 ?  25   GLU   A HB2  1 
ATOM   720  H  HB2  B GLU   A 1 25  ? 13.676 2.502   13.414  0.50 24.96 ?  25   GLU   A HB2  1 
ATOM   721  H  HB3  A GLU   A 1 25  ? 13.560 3.742   14.967  0.50 23.72 ?  25   GLU   A HB3  1 
ATOM   722  H  HB3  B GLU   A 1 25  ? 13.648 3.062   14.899  0.50 24.96 ?  25   GLU   A HB3  1 
ATOM   723  H  HG2  A GLU   A 1 25  ? 13.945 5.527   12.827  0.50 26.51 ?  25   GLU   A HG2  1 
ATOM   724  H  HG2  B GLU   A 1 25  ? 14.089 4.653   12.615  0.50 27.47 ?  25   GLU   A HG2  1 
ATOM   725  H  HG3  A GLU   A 1 25  ? 12.754 5.569   13.880  0.50 26.51 ?  25   GLU   A HG3  1 
ATOM   726  H  HG3  B GLU   A 1 25  ? 12.730 4.616   13.438  0.50 27.47 ?  25   GLU   A HG3  1 
ATOM   727  N  N    A GLU   A 1 26  ? 15.622 1.116   13.994  0.50 16.85 ?  26   GLU   A N    1 
ATOM   728  N  N    B GLU   A 1 26  ? 15.850 0.494   13.999  0.50 18.59 ?  26   GLU   A N    1 
ATOM   729  C  CA   A GLU   A 1 26  ? 15.939 -0.203  14.532  0.50 17.20 ?  26   GLU   A CA   1 
ATOM   730  C  CA   B GLU   A 1 26  ? 16.230 -0.808  14.540  0.50 18.59 ?  26   GLU   A CA   1 
ATOM   731  C  C    A GLU   A 1 26  ? 17.372 -0.248  15.041  0.50 16.38 ?  26   GLU   A C    1 
ATOM   732  C  C    B GLU   A 1 26  ? 17.653 -0.777  15.083  0.50 18.01 ?  26   GLU   A C    1 
ATOM   733  O  O    A GLU   A 1 26  ? 17.638 -0.766  16.132  0.50 16.08 ?  26   GLU   A O    1 
ATOM   734  O  O    B GLU   A 1 26  ? 17.922 -1.295  16.173  0.50 18.17 ?  26   GLU   A O    1 
ATOM   735  C  CB   A GLU   A 1 26  ? 15.743 -1.264  13.450  0.50 18.56 ?  26   GLU   A CB   1 
ATOM   736  C  CB   B GLU   A 1 26  ? 16.081 -1.897  13.471  0.50 20.11 ?  26   GLU   A CB   1 
ATOM   737  C  CG   A GLU   A 1 26  ? 14.343 -1.799  13.337  0.50 20.70 ?  26   GLU   A CG   1 
ATOM   738  C  CG   B GLU   A 1 26  ? 14.645 -2.226  13.115  0.50 21.21 ?  26   GLU   A CG   1 
ATOM   739  C  CD   A GLU   A 1 26  ? 13.980 -2.686  14.511  0.50 22.00 ?  26   GLU   A CD   1 
ATOM   740  C  CD   B GLU   A 1 26  ? 13.860 -2.729  14.305  0.50 21.86 ?  26   GLU   A CD   1 
ATOM   741  O  OE1  A GLU   A 1 26  ? 14.440 -3.852  14.561  0.50 22.51 ?  26   GLU   A OE1  1 
ATOM   742  O  OE1  B GLU   A 1 26  ? 14.330 -3.681  14.969  0.50 22.43 ?  26   GLU   A OE1  1 
ATOM   743  O  OE2  A GLU   A 1 26  ? 13.250 -2.205  15.393  0.50 22.59 -1 26   GLU   A OE2  1 
ATOM   744  O  OE2  B GLU   A 1 26  ? 12.785 -2.160  14.580  0.50 21.36 -1 26   GLU   A OE2  1 
ATOM   745  H  H    A GLU   A 1 26  ? 15.408 1.130   13.163  0.50 20.21 ?  26   GLU   A H    1 
ATOM   746  H  H    B GLU   A 1 26  ? 15.629 0.483   13.169  0.50 22.30 ?  26   GLU   A H    1 
ATOM   747  H  HA   A GLU   A 1 26  ? 15.343 -0.398  15.272  0.50 20.63 ?  26   GLU   A HA   1 
ATOM   748  H  HA   B GLU   A 1 26  ? 15.645 -1.037  15.277  0.50 22.30 ?  26   GLU   A HA   1 
ATOM   749  H  HB2  A GLU   A 1 26  ? 15.980 -0.877  12.595  0.50 22.27 ?  26   GLU   A HB2  1 
ATOM   750  H  HB2  B GLU   A 1 26  ? 16.522 -1.606  12.658  0.50 24.13 ?  26   GLU   A HB2  1 
ATOM   751  H  HB3  A GLU   A 1 26  ? 16.327 -2.010  13.647  0.50 22.27 ?  26   GLU   A HB3  1 
ATOM   752  H  HB3  B GLU   A 1 26  ? 16.496 -2.718  13.789  0.50 24.13 ?  26   GLU   A HB3  1 
ATOM   753  H  HG2  A GLU   A 1 26  ? 13.723 -1.051  13.299  0.50 24.83 ?  26   GLU   A HG2  1 
ATOM   754  H  HG2  B GLU   A 1 26  ? 14.207 -1.427  12.783  0.50 25.45 ?  26   GLU   A HG2  1 
ATOM   755  H  HG3  A GLU   A 1 26  ? 14.267 -2.331  12.530  0.50 24.83 ?  26   GLU   A HG3  1 
ATOM   756  H  HG3  B GLU   A 1 26  ? 14.630 -2.920  12.436  0.50 25.45 ?  26   GLU   A HG3  1 
ATOM   757  N  N    A ALA   A 1 27  ? 18.308 0.299   14.263  0.50 15.83 ?  27   ALA   A N    1 
ATOM   758  N  N    B ALA   A 1 27  ? 18.578 -0.160  14.346  0.50 17.50 ?  27   ALA   A N    1 
ATOM   759  C  CA   A ALA   A 1 27  ? 19.715 0.262   14.643  0.50 16.28 ?  27   ALA   A CA   1 
ATOM   760  C  CA   B ALA   A 1 27  ? 19.952 -0.076  14.832  0.50 17.63 ?  27   ALA   A CA   1 
ATOM   761  C  C    A ALA   A 1 27  ? 19.948 0.987   15.964  0.50 17.78 ?  27   ALA   A C    1 
ATOM   762  C  C    B ALA   A 1 27  ? 20.043 0.815   16.065  0.50 18.84 ?  27   ALA   A C    1 
ATOM   763  O  O    A ALA   A 1 27  ? 20.606 0.461   16.869  0.50 18.10 ?  27   ALA   A O    1 
ATOM   764  O  O    B ALA   A 1 27  ? 20.741 0.481   17.030  0.50 18.84 ?  27   ALA   A O    1 
ATOM   765  C  CB   A ALA   A 1 27  ? 20.566 0.870   13.526  0.50 15.77 ?  27   ALA   A CB   1 
ATOM   766  C  CB   B ALA   A 1 27  ? 20.881 0.420   13.721  0.50 17.30 ?  27   ALA   A CB   1 
ATOM   767  H  H    A ALA   A 1 27  ? 18.145 0.704   13.519  0.50 18.99 ?  27   ALA   A H    1 
ATOM   768  H  H    B ALA   A 1 27  ? 18.438 0.209   13.582  0.50 21.00 ?  27   ALA   A H    1 
ATOM   769  H  HA   A ALA   A 1 27  ? 19.981 -0.658  14.753  0.50 19.53 ?  27   ALA   A HA   1 
ATOM   770  H  HA   B ALA   A 1 27  ? 20.248 -0.965  15.085  0.50 21.15 ?  27   ALA   A HA   1 
ATOM   771  H  HB1  A ALA   A 1 27  ? 21.498 0.837   13.786  0.50 18.92 ?  27   ALA   A HB1  1 
ATOM   772  H  HB1  B ALA   A 1 27  ? 21.792 0.454   14.062  0.50 20.75 ?  27   ALA   A HB1  1 
ATOM   773  H  HB2  A ALA   A 1 27  ? 20.429 0.362   12.711  0.50 18.92 ?  27   ALA   A HB2  1 
ATOM   774  H  HB2  B ALA   A 1 27  ? 20.839 -0.199  12.972  0.50 20.75 ?  27   ALA   A HB2  1 
ATOM   775  H  HB3  A ALA   A 1 27  ? 20.295 1.794   13.385  0.50 18.92 ?  27   ALA   A HB3  1 
ATOM   776  H  HB3  B ALA   A 1 27  ? 20.601 1.301   13.439  0.50 20.75 ?  27   ALA   A HB3  1 
ATOM   777  N  N    A LYS   A 1 28  ? 19.405 2.200   16.098  0.50 19.84 ?  28   LYS   A N    1 
ATOM   778  N  N    B LYS   A 1 28  ? 19.331 1.946   16.062  0.50 20.63 ?  28   LYS   A N    1 
ATOM   779  C  CA   A LYS   A 1 28  ? 19.620 2.967   17.322  0.50 22.76 ?  28   LYS   A CA   1 
ATOM   780  C  CA   B LYS   A 1 28  ? 19.343 2.829   17.224  0.50 23.07 ?  28   LYS   A CA   1 
ATOM   781  C  C    A LYS   A 1 28  ? 19.082 2.238   18.546  0.50 23.81 ?  28   LYS   A C    1 
ATOM   782  C  C    B LYS   A 1 28  ? 18.835 2.116   18.472  0.50 24.32 ?  28   LYS   A C    1 
ATOM   783  O  O    A LYS   A 1 28  ? 19.644 2.370   19.639  0.50 25.00 ?  28   LYS   A O    1 
ATOM   784  O  O    B LYS   A 1 28  ? 19.344 2.344   19.575  0.50 25.23 ?  28   LYS   A O    1 
ATOM   785  C  CB   A LYS   A 1 28  ? 18.996 4.359   17.192  0.50 24.68 ?  28   LYS   A CB   1 
ATOM   786  C  CB   B LYS   A 1 28  ? 18.518 4.087   16.945  0.50 24.37 ?  28   LYS   A CB   1 
ATOM   787  C  CG   A LYS   A 1 28  ? 19.760 5.276   16.247  0.50 26.40 ?  28   LYS   A CG   1 
ATOM   788  C  CG   B LYS   A 1 28  ? 19.285 5.160   16.195  0.50 26.08 ?  28   LYS   A CG   1 
ATOM   789  C  CD   A LYS   A 1 28  ? 19.252 6.709   16.290  0.50 27.98 ?  28   LYS   A CD   1 
ATOM   790  C  CD   B LYS   A 1 28  ? 18.606 6.520   16.274  0.50 28.05 ?  28   LYS   A CD   1 
ATOM   791  C  CE   A LYS   A 1 28  ? 17.913 6.848   15.594  0.50 29.02 ?  28   LYS   A CE   1 
ATOM   792  C  CE   B LYS   A 1 28  ? 17.735 6.782   15.061  0.50 29.70 ?  28   LYS   A CE   1 
ATOM   793  N  NZ   A LYS   A 1 28  ? 17.460 8.266   15.550  0.50 29.57 ?  28   LYS   A NZ   1 
ATOM   794  N  NZ   B LYS   A 1 28  ? 17.626 8.239   14.766  0.50 30.53 ?  28   LYS   A NZ   1 
ATOM   795  H  H    A LYS   A 1 28  ? 18.918 2.592   15.511  0.50 23.80 ?  28   LYS   A H    1 
ATOM   796  H  H    B LYS   A 1 28  ? 18.845 2.213   15.408  0.50 24.75 ?  28   LYS   A H    1 
ATOM   797  H  HA   A LYS   A 1 28  ? 20.571 3.086   17.455  0.50 27.30 ?  28   LYS   A HA   1 
ATOM   798  H  HA   B LYS   A 1 28  ? 20.253 3.105   17.397  0.50 27.67 ?  28   LYS   A HA   1 
ATOM   799  H  HB2  A LYS   A 1 28  ? 18.093 4.270   16.854  0.50 29.61 ?  28   LYS   A HB2  1 
ATOM   800  H  HB2  B LYS   A 1 28  ? 17.745 3.847   16.410  0.50 29.24 ?  28   LYS   A HB2  1 
ATOM   801  H  HB3  A LYS   A 1 28  ? 18.981 4.782   18.066  0.50 29.61 ?  28   LYS   A HB3  1 
ATOM   802  H  HB3  B LYS   A 1 28  ? 18.228 4.464   17.790  0.50 29.24 ?  28   LYS   A HB3  1 
ATOM   803  H  HG2  A LYS   A 1 28  ? 20.696 5.281   16.498  0.50 31.67 ?  28   LYS   A HG2  1 
ATOM   804  H  HG2  B LYS   A 1 28  ? 20.169 5.247   16.582  0.50 31.29 ?  28   LYS   A HG2  1 
ATOM   805  H  HG3  A LYS   A 1 28  ? 19.659 4.949   15.339  0.50 31.67 ?  28   LYS   A HG3  1 
ATOM   806  H  HG3  B LYS   A 1 28  ? 19.357 4.905   15.261  0.50 31.29 ?  28   LYS   A HG3  1 
ATOM   807  H  HD2  A LYS   A 1 28  ? 19.143 6.982   17.214  0.50 33.57 ?  28   LYS   A HD2  1 
ATOM   808  H  HD2  B LYS   A 1 28  ? 18.045 6.556   17.066  0.50 33.66 ?  28   LYS   A HD2  1 
ATOM   809  H  HD3  A LYS   A 1 28  ? 19.889 7.287   15.842  0.50 33.57 ?  28   LYS   A HD3  1 
ATOM   810  H  HD3  B LYS   A 1 28  ? 19.285 7.213   16.317  0.50 33.66 ?  28   LYS   A HD3  1 
ATOM   811  H  HE2  A LYS   A 1 28  ? 17.992 6.527   14.681  0.50 34.82 ?  28   LYS   A HE2  1 
ATOM   812  H  HE2  B LYS   A 1 28  ? 18.127 6.348   14.289  0.50 35.63 ?  28   LYS   A HE2  1 
ATOM   813  H  HE3  A LYS   A 1 28  ? 17.247 6.332   16.074  0.50 34.82 ?  28   LYS   A HE3  1 
ATOM   814  H  HE3  B LYS   A 1 28  ? 16.844 6.436   15.225  0.50 35.63 ?  28   LYS   A HE3  1 
ATOM   815  H  HZ1  A LYS   A 1 28  ? 16.675 8.323   15.137  0.50 35.48 ?  28   LYS   A HZ1  1 
ATOM   816  H  HZ1  B LYS   A 1 28  ? 17.114 8.368   14.051  0.50 36.63 ?  28   LYS   A HZ1  1 
ATOM   817  H  HZ2  A LYS   A 1 28  ? 17.377 8.584   16.377  0.50 35.48 ?  28   LYS   A HZ2  1 
ATOM   818  H  HZ2  B LYS   A 1 28  ? 17.269 8.665   15.461  0.50 36.63 ?  28   LYS   A HZ2  1 
ATOM   819  H  HZ3  A LYS   A 1 28  ? 18.055 8.762   15.109  0.50 35.48 ?  28   LYS   A HZ3  1 
ATOM   820  H  HZ3  B LYS   A 1 28  ? 18.435 8.578   14.606  0.50 36.63 ?  28   LYS   A HZ3  1 
ATOM   821  N  N    A LYS   A 1 29  ? 18.013 1.457   18.385  0.50 24.05 ?  29   LYS   A N    1 
ATOM   822  N  N    B LYS   A 1 29  ? 17.837 1.244   18.320  0.50 25.02 ?  29   LYS   A N    1 
ATOM   823  C  CA   A LYS   A 1 29  ? 17.421 0.750   19.517  0.50 25.64 ?  29   LYS   A CA   1 
ATOM   824  C  CA   B LYS   A 1 29  ? 17.262 0.570   19.481  0.50 26.47 ?  29   LYS   A CA   1 
ATOM   825  C  C    A LYS   A 1 29  ? 18.240 -0.479  19.899  0.50 25.06 ?  29   LYS   A C    1 
ATOM   826  C  C    B LYS   A 1 29  ? 18.071 -0.658  19.883  0.50 25.61 ?  29   LYS   A C    1 
ATOM   827  O  O    A LYS   A 1 29  ? 18.591 -0.663  21.070  0.50 25.81 ?  29   LYS   A O    1 
ATOM   828  O  O    B LYS   A 1 29  ? 18.286 -0.900  21.077  0.50 25.71 ?  29   LYS   A O    1 
ATOM   829  C  CB   A LYS   A 1 29  ? 15.986 0.344   19.171  0.50 27.98 ?  29   LYS   A CB   1 
ATOM   830  C  CB   B LYS   A 1 29  ? 15.812 0.175   19.194  0.50 28.94 ?  29   LYS   A CB   1 
ATOM   831  C  CG   A LYS   A 1 29  ? 15.240 -0.365  20.292  0.50 30.53 ?  29   LYS   A CG   1 
ATOM   832  C  CG   B LYS   A 1 29  ? 15.071 -0.408  20.391  0.50 31.42 ?  29   LYS   A CG   1 
ATOM   833  C  CD   A LYS   A 1 29  ? 14.800 0.611   21.369  0.50 33.02 ?  29   LYS   A CD   1 
ATOM   834  C  CD   B LYS   A 1 29  ? 14.864 0.631   21.484  0.50 33.61 ?  29   LYS   A CD   1 
ATOM   835  C  CE   A LYS   A 1 29  ? 13.907 -0.066  22.397  0.50 34.71 ?  29   LYS   A CE   1 
ATOM   836  C  CE   B LYS   A 1 29  ? 14.046 0.072   22.638  0.50 35.12 ?  29   LYS   A CE   1 
ATOM   837  N  NZ   A LYS   A 1 29  ? 13.384 0.906   23.395  0.50 35.64 ?  29   LYS   A NZ   1 
ATOM   838  N  NZ   B LYS   A 1 29  ? 13.776 1.104   23.678  0.50 35.96 ?  29   LYS   A NZ   1 
ATOM   839  H  H    A LYS   A 1 29  ? 17.616 1.320   17.633  0.50 28.85 ?  29   LYS   A H    1 
ATOM   840  H  H    B LYS   A 1 29  ? 17.477 1.031   17.567  0.50 30.02 ?  29   LYS   A H    1 
ATOM   841  H  HA   A LYS   A 1 29  ? 17.389 1.344   20.282  0.50 30.76 ?  29   LYS   A HA   1 
ATOM   842  H  HA   B LYS   A 1 29  ? 17.263 1.182   20.230  0.50 31.76 ?  29   LYS   A HA   1 
ATOM   843  H  HB2  A LYS   A 1 29  ? 15.482 1.142   18.946  0.50 33.57 ?  29   LYS   A HB2  1 
ATOM   844  H  HB2  B LYS   A 1 29  ? 15.327 0.963   18.906  0.50 34.72 ?  29   LYS   A HB2  1 
ATOM   845  H  HB3  A LYS   A 1 29  ? 16.006 -0.255  18.409  0.50 33.57 ?  29   LYS   A HB3  1 
ATOM   846  H  HB3  B LYS   A 1 29  ? 15.802 -0.492  18.491  0.50 34.72 ?  29   LYS   A HB3  1 
ATOM   847  H  HG2  A LYS   A 1 29  ? 14.448 -0.790  19.929  0.50 36.64 ?  29   LYS   A HG2  1 
ATOM   848  H  HG2  B LYS   A 1 29  ? 14.199 -0.723  20.105  0.50 37.70 ?  29   LYS   A HG2  1 
ATOM   849  H  HG3  A LYS   A 1 29  ? 15.815 -1.031  20.702  0.50 36.64 ?  29   LYS   A HG3  1 
ATOM   850  H  HG3  B LYS   A 1 29  ? 15.584 -1.143  20.765  0.50 37.70 ?  29   LYS   A HG3  1 
ATOM   851  H  HD2  A LYS   A 1 29  ? 15.581 0.959   21.826  0.50 39.62 ?  29   LYS   A HD2  1 
ATOM   852  H  HD2  B LYS   A 1 29  ? 15.726 0.909   21.832  0.50 40.32 ?  29   LYS   A HD2  1 
ATOM   853  H  HD3  A LYS   A 1 29  ? 14.299 1.334   20.960  0.50 39.62 ?  29   LYS   A HD3  1 
ATOM   854  H  HD3  B LYS   A 1 29  ? 14.389 1.393   21.115  0.50 40.32 ?  29   LYS   A HD3  1 
ATOM   855  H  HE2  A LYS   A 1 29  ? 13.151 -0.474  21.945  0.50 41.65 ?  29   LYS   A HE2  1 
ATOM   856  H  HE2  B LYS   A 1 29  ? 13.194 -0.248  22.301  0.50 42.14 ?  29   LYS   A HE2  1 
ATOM   857  H  HE3  A LYS   A 1 29  ? 14.419 -0.742  22.870  0.50 41.65 ?  29   LYS   A HE3  1 
ATOM   858  H  HE3  B LYS   A 1 29  ? 14.535 -0.656  23.054  0.50 42.14 ?  29   LYS   A HE3  1 
ATOM   859  H  HZ1  A LYS   A 1 29  ? 12.865 0.487   23.985  0.50 42.76 ?  29   LYS   A HZ1  1 
ATOM   860  H  HZ1  B LYS   A 1 29  ? 13.308 0.749   24.346  0.50 43.14 ?  29   LYS   A HZ1  1 
ATOM   861  H  HZ2  A LYS   A 1 29  ? 14.060 1.292   23.827  0.50 42.76 ?  29   LYS   A HZ2  1 
ATOM   862  H  HZ2  B LYS   A 1 29  ? 14.544 1.419   23.999  0.50 43.14 ?  29   LYS   A HZ2  1 
ATOM   863  H  HZ3  A LYS   A 1 29  ? 12.906 1.535   22.985  0.50 42.76 ?  29   LYS   A HZ3  1 
ATOM   864  H  HZ3  B LYS   A 1 29  ? 13.312 1.777   23.325  0.50 43.14 ?  29   LYS   A HZ3  1 
ATOM   865  N  N    A VAL   A 1 30  ? 18.546 -1.332  18.922  0.50 24.16 ?  30   VAL   A N    1 
ATOM   866  N  N    B VAL   A 1 30  ? 18.515 -1.447  18.909  0.50 24.72 ?  30   VAL   A N    1 
ATOM   867  C  CA   A VAL   A 1 30  ? 19.170 -2.620  19.208  0.50 23.57 ?  30   VAL   A CA   1 
ATOM   868  C  CA   B VAL   A 1 30  ? 19.201 -2.697  19.209  0.50 24.11 ?  30   VAL   A CA   1 
ATOM   869  C  C    A VAL   A 1 30  ? 20.679 -2.485  19.405  0.50 22.90 ?  30   VAL   A C    1 
ATOM   870  C  C    B VAL   A 1 30  ? 20.703 -2.503  19.405  0.50 23.14 ?  30   VAL   A C    1 
ATOM   871  O  O    A VAL   A 1 30  ? 21.271 -3.213  20.210  0.50 23.25 ?  30   VAL   A O    1 
ATOM   872  O  O    B VAL   A 1 30  ? 21.313 -3.208  20.214  0.50 23.44 ?  30   VAL   A O    1 
ATOM   873  C  CB   A VAL   A 1 30  ? 18.833 -3.605  18.075  0.50 24.21 ?  30   VAL   A CB   1 
ATOM   874  C  CB   B VAL   A 1 30  ? 18.910 -3.734  18.110  0.50 24.89 ?  30   VAL   A CB   1 
ATOM   875  C  CG1  A VAL   A 1 30  ? 19.505 -4.948  18.312  0.50 24.72 ?  30   VAL   A CG1  1 
ATOM   876  C  CG1  B VAL   A 1 30  ? 19.866 -4.918  18.207  0.50 25.12 ?  30   VAL   A CG1  1 
ATOM   877  C  CG2  A VAL   A 1 30  ? 17.324 -3.773  17.943  0.50 24.35 ?  30   VAL   A CG2  1 
ATOM   878  C  CG2  B VAL   A 1 30  ? 17.473 -4.209  18.208  0.50 25.28 ?  30   VAL   A CG2  1 
ATOM   879  H  H    A VAL   A 1 30  ? 18.401 -1.187  18.088  0.50 28.99 ?  30   VAL   A H    1 
ATOM   880  H  H    B VAL   A 1 30  ? 18.432 -1.284  18.069  0.50 29.66 ?  30   VAL   A H    1 
ATOM   881  H  HA   A VAL   A 1 30  ? 18.787 -2.972  20.026  0.50 28.28 ?  30   VAL   A HA   1 
ATOM   882  H  HA   B VAL   A 1 30  ? 18.838 -3.051  20.038  0.50 28.92 ?  30   VAL   A HA   1 
ATOM   883  H  HB   A VAL   A 1 30  ? 19.167 -3.250  17.237  0.50 29.04 ?  30   VAL   A HB   1 
ATOM   884  H  HB   B VAL   A 1 30  ? 19.035 -3.322  17.241  0.50 29.87 ?  30   VAL   A HB   1 
ATOM   885  H  HG11 A VAL   A 1 30  ? 19.126 -5.600  17.701  0.50 29.66 ?  30   VAL   A HG11 1 
ATOM   886  H  HG11 B VAL   A 1 30  ? 19.502 -5.657  17.692  0.50 30.14 ?  30   VAL   A HG11 1 
ATOM   887  H  HG12 A VAL   A 1 30  ? 20.457 -4.860  18.151  0.50 29.66 ?  30   VAL   A HG12 1 
ATOM   888  H  HG12 B VAL   A 1 30  ? 20.729 -4.663  17.848  0.50 30.14 ?  30   VAL   A HG12 1 
ATOM   889  H  HG13 A VAL   A 1 30  ? 19.345 -5.223  19.227  0.50 29.66 ?  30   VAL   A HG13 1 
ATOM   890  H  HG13 B VAL   A 1 30  ? 19.953 -5.178  19.137  0.50 30.14 ?  30   VAL   A HG13 1 
ATOM   891  H  HG21 A VAL   A 1 30  ? 17.139 -4.455  17.278  0.50 29.21 ?  30   VAL   A HG21 1 
ATOM   892  H  HG21 B VAL   A 1 30  ? 17.303 -4.851  17.502  0.50 30.34 ?  30   VAL   A HG21 1 
ATOM   893  H  HG22 A VAL   A 1 30  ? 16.960 -4.042  18.801  0.50 29.21 ?  30   VAL   A HG22 1 
ATOM   894  H  HG22 B VAL   A 1 30  ? 17.339 -4.627  19.074  0.50 30.34 ?  30   VAL   A HG22 1 
ATOM   895  H  HG23 A VAL   A 1 30  ? 16.934 -2.929  17.668  0.50 29.21 ?  30   VAL   A HG23 1 
ATOM   896  H  HG23 B VAL   A 1 30  ? 16.884 -3.446  18.113  0.50 30.34 ?  30   VAL   A HG23 1 
ATOM   897  N  N    . LYS   A 1 31  ? 21.314 -1.566  18.688  1.00 22.03 ?  31   LYS   A N    1 
ATOM   898  C  CA   . LYS   A 1 31  ? 22.766 -1.431  18.651  1.00 22.45 ?  31   LYS   A CA   1 
ATOM   899  C  C    . LYS   A 1 31  ? 23.392 -2.780  18.288  1.00 20.32 ?  31   LYS   A C    1 
ATOM   900  O  O    . LYS   A 1 31  ? 24.180 -3.337  19.062  1.00 21.37 ?  31   LYS   A O    1 
ATOM   901  C  CB   . LYS   A 1 31  ? 23.339 -0.889  19.952  1.00 27.09 ?  31   LYS   A CB   1 
ATOM   902  C  CG   . LYS   A 1 31  ? 22.649 0.371   20.451  1.00 32.64 ?  31   LYS   A CG   1 
ATOM   903  C  CD   . LYS   A 1 31  ? 23.643 1.489   20.732  1.00 37.09 ?  31   LYS   A CD   1 
ATOM   904  C  CE   . LYS   A 1 31  ? 23.069 2.518   21.697  1.00 39.84 ?  31   LYS   A CE   1 
ATOM   905  N  NZ   . LYS   A 1 31  ? 21.794 3.119   21.217  1.00 41.34 ?  31   LYS   A NZ   1 
ATOM   906  H  H    A LYS   A 1 31  ? 20.910 -0.993  18.199  0.50 26.43 ?  31   LYS   A H    1 
ATOM   907  H  H    B LYS   A 1 31  ? 20.902 -0.995  18.203  0.50 26.43 ?  31   LYS   A H    1 
ATOM   908  H  HA   . LYS   A 1 31  ? 22.992 -0.806  17.956  1.00 26.93 ?  31   LYS   A HA   1 
ATOM   909  H  HB2  . LYS   A 1 31  ? 23.246 -1.570  20.623  1.00 32.50 ?  31   LYS   A HB2  1 
ATOM   910  H  HB3  . LYS   A 1 31  ? 24.283 -0.686  19.817  1.00 32.50 ?  31   LYS   A HB3  1 
ATOM   911  H  HG2  . LYS   A 1 31  ? 22.027 0.683   19.775  1.00 39.16 ?  31   LYS   A HG2  1 
ATOM   912  H  HG3  . LYS   A 1 31  ? 22.177 0.172   21.274  1.00 39.16 ?  31   LYS   A HG3  1 
ATOM   913  H  HD2  . LYS   A 1 31  ? 24.445 1.115   21.130  1.00 44.50 ?  31   LYS   A HD2  1 
ATOM   914  H  HD3  . LYS   A 1 31  ? 23.861 1.940   19.900  1.00 44.50 ?  31   LYS   A HD3  1 
ATOM   915  H  HE2  . LYS   A 1 31  ? 22.893 2.086   22.547  1.00 47.80 ?  31   LYS   A HE2  1 
ATOM   916  H  HE3  . LYS   A 1 31  ? 23.713 3.234   21.817  1.00 47.80 ?  31   LYS   A HE3  1 
ATOM   917  H  HZ1  . LYS   A 1 31  ? 21.500 3.719   21.806  1.00 49.60 ?  31   LYS   A HZ1  1 
ATOM   918  H  HZ2  . LYS   A 1 31  ? 21.923 3.521   20.435  1.00 49.60 ?  31   LYS   A HZ2  1 
ATOM   919  H  HZ3  . LYS   A 1 31  ? 21.177 2.485   21.119  1.00 49.60 ?  31   LYS   A HZ3  1 
ATOM   920  N  N    . PRO   A 1 32  ? 23.048 -3.330  17.131  1.00 18.11 ?  32   PRO   A N    1 
ATOM   921  C  CA   . PRO   A 1 32  ? 23.527 -4.664  16.774  1.00 18.61 ?  32   PRO   A CA   1 
ATOM   922  C  C    . PRO   A 1 32  ? 25.026 -4.668  16.556  1.00 18.19 ?  32   PRO   A C    1 
ATOM   923  O  O    . PRO   A 1 32  ? 25.657 -3.630  16.336  1.00 17.68 ?  32   PRO   A O    1 
ATOM   924  C  CB   . PRO   A 1 32  ? 22.793 -4.955  15.461  1.00 18.76 ?  32   PRO   A CB   1 
ATOM   925  C  CG   . PRO   A 1 32  ? 22.593 -3.596  14.856  1.00 17.45 ?  32   PRO   A CG   1 
ATOM   926  C  CD   . PRO   A 1 32  ? 22.307 -2.701  16.025  1.00 17.33 ?  32   PRO   A CD   1 
ATOM   927  H  HA   . PRO   A 1 32  ? 23.287 -5.319  17.444  1.00 22.32 ?  32   PRO   A HA   1 
ATOM   928  H  HB2  . PRO   A 1 32  ? 23.343 -5.517  14.886  1.00 22.50 ?  32   PRO   A HB2  1 
ATOM   929  H  HB3  . PRO   A 1 32  ? 21.943 -5.384  15.647  1.00 22.50 ?  32   PRO   A HB3  1 
ATOM   930  H  HG2  . PRO   A 1 32  ? 23.402 -3.327  14.395  1.00 20.93 ?  32   PRO   A HG2  1 
ATOM   931  H  HG3  . PRO   A 1 32  ? 21.841 -3.626  14.243  1.00 20.93 ?  32   PRO   A HG3  1 
ATOM   932  H  HD2  . PRO   A 1 32  ? 22.646 -1.811  15.843  1.00 20.79 ?  32   PRO   A HD2  1 
ATOM   933  H  HD3  . PRO   A 1 32  ? 21.359 -2.695  16.212  1.00 20.79 ?  32   PRO   A HD3  1 
ATOM   934  N  N    . THR   A 1 33  ? 25.591 -5.874  16.593  1.00 18.02 ?  33   THR   A N    1 
ATOM   935  C  CA   . THR   A 1 33  ? 26.998 -6.027  16.258  1.00 17.92 ?  33   THR   A CA   1 
ATOM   936  C  C    . THR   A 1 33  ? 27.273 -5.553  14.837  1.00 16.57 ?  33   THR   A C    1 
ATOM   937  O  O    . THR   A 1 33  ? 28.292 -4.894  14.583  1.00 16.81 ?  33   THR   A O    1 
ATOM   938  C  CB   . THR   A 1 33  ? 27.415 -7.485  16.444  1.00 19.24 ?  33   THR   A CB   1 
ATOM   939  O  OG1  . THR   A 1 33  ? 27.100 -7.895  17.777  1.00 20.80 ?  33   THR   A OG1  1 
ATOM   940  C  CG2  . THR   A 1 33  ? 28.908 -7.655  16.207  1.00 20.46 ?  33   THR   A CG2  1 
ATOM   941  H  H    . THR   A 1 33  ? 25.190 -6.610  16.795  1.00 21.61 ?  33   THR   A H    1 
ATOM   942  H  HA   . THR   A 1 33  ? 27.533 -5.491  16.860  1.00 21.50 ?  33   THR   A HA   1 
ATOM   943  H  HB   . THR   A 1 33  ? 26.943 -8.051  15.808  1.00 23.08 ?  33   THR   A HB   1 
ATOM   944  H  HG1  . THR   A 1 33  ? 27.518 -7.420  18.331  1.00 24.95 ?  33   THR   A HG1  1 
ATOM   945  H  HG21 . THR   A 1 33  ? 29.188 -8.548  16.468  1.00 24.55 ?  33   THR   A HG21 1 
ATOM   946  H  HG22 . THR   A 1 33  ? 29.116 -7.524  15.269  1.00 24.55 ?  33   THR   A HG22 1 
ATOM   947  H  HG23 . THR   A 1 33  ? 29.401 -7.007  16.734  1.00 24.55 ?  33   THR   A HG23 1 
ATOM   948  N  N    . VAL   A 1 34  ? 26.371 -5.861  13.902  1.00 14.94 ?  34   VAL   A N    1 
ATOM   949  C  CA   . VAL   A 1 34  ? 26.547 -5.518  12.495  1.00 13.54 ?  34   VAL   A CA   1 
ATOM   950  C  C    . VAL   A 1 34  ? 25.240 -4.961  11.946  1.00 12.99 ?  34   VAL   A C    1 
ATOM   951  O  O    . VAL   A 1 34  ? 24.200 -5.632  12.002  1.00 13.46 ?  34   VAL   A O    1 
ATOM   952  C  CB   . VAL   A 1 34  ? 26.997 -6.720  11.644  1.00 13.83 ?  34   VAL   A CB   1 
ATOM   953  C  CG1  . VAL   A 1 34  ? 27.153 -6.307  10.186  1.00 14.07 ?  34   VAL   A CG1  1 
ATOM   954  C  CG2  . VAL   A 1 34  ? 28.293 -7.321  12.179  1.00 15.19 ?  34   VAL   A CG2  1 
ATOM   955  H  H    . VAL   A 1 34  ? 25.639 -6.286  14.063  1.00 17.92 ?  34   VAL   A H    1 
ATOM   956  H  HA   . VAL   A 1 34  ? 27.222 -4.823  12.419  1.00 16.25 ?  34   VAL   A HA   1 
ATOM   957  H  HB   . VAL   A 1 34  ? 26.312 -7.402  11.686  1.00 16.59 ?  34   VAL   A HB   1 
ATOM   958  H  HG11 . VAL   A 1 34  ? 27.645 -6.994  9.714   1.00 16.88 ?  34   VAL   A HG11 1 
ATOM   959  H  HG12 . VAL   A 1 34  ? 26.275 -6.196  9.786   1.00 16.88 ?  34   VAL   A HG12 1 
ATOM   960  H  HG13 . VAL   A 1 34  ? 27.641 -5.466  10.144  1.00 16.88 ?  34   VAL   A HG13 1 
ATOM   961  H  HG21 . VAL   A 1 34  ? 28.563 -8.051  11.601  1.00 18.22 ?  34   VAL   A HG21 1 
ATOM   962  H  HG22 . VAL   A 1 34  ? 28.981 -6.634  12.184  1.00 18.22 ?  34   VAL   A HG22 1 
ATOM   963  H  HG23 . VAL   A 1 34  ? 28.145 -7.645  13.079  1.00 18.22 ?  34   VAL   A HG23 1 
ATOM   964  N  N    . VAL   A 1 35  ? 25.293 -3.745  11.402  1.00 12.40 ?  35   VAL   A N    1 
ATOM   965  C  CA   . VAL   A 1 35  ? 24.254 -3.226  10.522  1.00 11.97 ?  35   VAL   A CA   1 
ATOM   966  C  C    . VAL   A 1 35  ? 24.800 -3.223  9.102   1.00 11.25 ?  35   VAL   A C    1 
ATOM   967  O  O    . VAL   A 1 35  ? 25.943 -2.816  8.866   1.00 11.67 ?  35   VAL   A O    1 
ATOM   968  C  CB   . VAL   A 1 35  ? 23.723 -1.836  10.938  1.00 12.77 ?  35   VAL   A CB   1 
ATOM   969  C  CG1  . VAL   A 1 35  ? 24.787 -0.741  10.815  1.00 13.15 ?  35   VAL   A CG1  1 
ATOM   970  C  CG2  . VAL   A 1 35  ? 22.481 -1.485  10.120  1.00 13.29 ?  35   VAL   A CG2  1 
ATOM   971  H  H    . VAL   A 1 35  ? 25.934 -3.183  11.531  1.00 14.87 ?  35   VAL   A H    1 
ATOM   972  H  HA   . VAL   A 1 35  ? 23.498 -3.836  10.543  1.00 14.36 ?  35   VAL   A HA   1 
ATOM   973  H  HB   . VAL   A 1 35  ? 23.449 -1.871  11.864  1.00 15.31 ?  35   VAL   A HB   1 
ATOM   974  H  HG11 . VAL   A 1 35  ? 24.435 0.090   11.182  1.00 15.77 ?  35   VAL   A HG11 1 
ATOM   975  H  HG12 . VAL   A 1 35  ? 25.576 -1.008  11.310  1.00 15.77 ?  35   VAL   A HG12 1 
ATOM   976  H  HG13 . VAL   A 1 35  ? 25.012 -0.611  9.879   1.00 15.77 ?  35   VAL   A HG13 1 
ATOM   977  H  HG21 . VAL   A 1 35  ? 22.120 -0.641  10.430  1.00 15.94 ?  35   VAL   A HG21 1 
ATOM   978  H  HG22 . VAL   A 1 35  ? 22.729 -1.409  9.180   1.00 15.94 ?  35   VAL   A HG22 1 
ATOM   979  H  HG23 . VAL   A 1 35  ? 21.821 -2.188  10.226  1.00 15.94 ?  35   VAL   A HG23 1 
ATOM   980  N  N    . VAL   A 1 36  ? 23.989 -3.689  8.160   1.00 10.72 ?  36   VAL   A N    1 
ATOM   981  C  CA   . VAL   A 1 36  ? 24.358 -3.693  6.751   1.00 10.42 ?  36   VAL   A CA   1 
ATOM   982  C  C    . VAL   A 1 36  ? 23.895 -2.404  6.095   1.00 10.39 ?  36   VAL   A C    1 
ATOM   983  O  O    . VAL   A 1 36  ? 22.733 -2.001  6.243   1.00 11.06 ?  36   VAL   A O    1 
ATOM   984  C  CB   . VAL   A 1 36  ? 23.754 -4.907  6.032   1.00 10.56 ?  36   VAL   A CB   1 
ATOM   985  C  CG1  . VAL   A 1 36  ? 24.018 -4.828  4.543   1.00 11.06 ?  36   VAL   A CG1  1 
ATOM   986  C  CG2  . VAL   A 1 36  ? 24.289 -6.198  6.616   1.00 11.75 ?  36   VAL   A CG2  1 
ATOM   987  H  H    . VAL   A 1 36  ? 23.204 -4.019  8.314   1.00 12.86 ?  36   VAL   A H    1 
ATOM   988  H  HA   . VAL   A 1 36  ? 25.327 -3.752  6.677   1.00 12.50 ?  36   VAL   A HA   1 
ATOM   989  H  HB   . VAL   A 1 36  ? 22.792 -4.893  6.160   1.00 12.66 ?  36   VAL   A HB   1 
ATOM   990  H  HG11 . VAL   A 1 36  ? 23.878 -5.704  4.152   1.00 13.26 ?  36   VAL   A HG11 1 
ATOM   991  H  HG12 . VAL   A 1 36  ? 23.412 -4.187  4.141   1.00 13.26 ?  36   VAL   A HG12 1 
ATOM   992  H  HG13 . VAL   A 1 36  ? 24.938 -4.549  4.401   1.00 13.26 ?  36   VAL   A HG13 1 
ATOM   993  H  HG21 . VAL   A 1 36  ? 23.904 -6.948  6.130   1.00 14.09 ?  36   VAL   A HG21 1 
ATOM   994  H  HG22 . VAL   A 1 36  ? 25.252 -6.210  6.533   1.00 14.09 ?  36   VAL   A HG22 1 
ATOM   995  H  HG23 . VAL   A 1 36  ? 24.035 -6.253  7.552   1.00 14.09 ?  36   VAL   A HG23 1 
ATOM   996  N  N    . ASN   A 1 37  ? 24.799 -1.770  5.354   1.00 9.72  ?  37   ASN   A N    1 
ATOM   997  C  CA   . ASN   A 1 37  ? 24.459 -0.650  4.493   1.00 9.61  ?  37   ASN   A CA   1 
ATOM   998  C  C    . ASN   A 1 37  ? 24.315 -1.111  3.053   1.00 9.71  ?  37   ASN   A C    1 
ATOM   999  O  O    . ASN   A 1 37  ? 25.095 -1.938  2.567   1.00 9.84  ?  37   ASN   A O    1 
ATOM   1000 C  CB   . ASN   A 1 37  ? 25.536 0.435   4.565   1.00 9.93  ?  37   ASN   A CB   1 
ATOM   1001 C  CG   . ASN   A 1 37  ? 25.202 1.635   3.719   1.00 10.21 ?  37   ASN   A CG   1 
ATOM   1002 O  OD1  . ASN   A 1 37  ? 24.023 1.961   3.542   1.00 10.55 ?  37   ASN   A OD1  1 
ATOM   1003 N  ND2  . ASN   A 1 37  ? 26.224 2.304   3.200   1.00 10.29 ?  37   ASN   A ND2  1 
ATOM   1004 H  H    . ASN   A 1 37  ? 25.640 -1.971  5.342   1.00 11.66 ?  37   ASN   A H    1 
ATOM   1005 H  HA   . ASN   A 1 37  ? 23.622 -0.263  4.786   1.00 11.53 ?  37   ASN   A HA   1 
ATOM   1006 H  HB2  . ASN   A 1 37  ? 25.627 0.733   5.489   1.00 11.92 ?  37   ASN   A HB2  1 
ATOM   1007 H  HB3  . ASN   A 1 37  ? 26.381 0.071   4.254   1.00 11.92 ?  37   ASN   A HB3  1 
ATOM   1008 H  HD21 . ASN   A 1 37  ? 26.077 2.995   2.709   1.00 12.35 ?  37   ASN   A HD21 1 
ATOM   1009 H  HD22 . ASN   A 1 37  ? 27.025 2.048   3.346   1.00 12.35 ?  37   ASN   A HD22 1 
ATOM   1010 N  N    A ALA   A 1 38  ? 23.300 -0.553  2.387   0.50 10.06 ?  38   ALA   A N    1 
ATOM   1011 N  N    B ALA   A 1 38  ? 23.295 -0.589  2.371   0.50 10.36 ?  38   ALA   A N    1 
ATOM   1012 C  CA   A ALA   A 1 38  ? 23.080 -0.668  0.947   0.50 9.66  ?  38   ALA   A CA   1 
ATOM   1013 C  CA   B ALA   A 1 38  ? 23.116 -0.820  0.937   0.50 10.54 ?  38   ALA   A CA   1 
ATOM   1014 C  C    A ALA   A 1 38  ? 24.010 0.324   0.251   0.50 9.64  ?  38   ALA   A C    1 
ATOM   1015 C  C    B ALA   A 1 38  ? 23.960 0.201   0.174   0.50 10.39 ?  38   ALA   A C    1 
ATOM   1016 O  O    A ALA   A 1 38  ? 23.633 1.444   -0.102  0.50 9.49  ?  38   ALA   A O    1 
ATOM   1017 O  O    B ALA   A 1 38  ? 23.480 1.221   -0.330  0.50 10.15 ?  38   ALA   A O    1 
ATOM   1018 C  CB   A ALA   A 1 38  ? 21.616 -0.386  0.620   0.50 10.44 ?  38   ALA   A CB   1 
ATOM   1019 C  CB   B ALA   A 1 38  ? 21.643 -0.745  0.561   0.50 11.33 ?  38   ALA   A CB   1 
ATOM   1020 H  H    A ALA   A 1 38  ? 22.705 -0.065  2.772   0.50 12.06 ?  38   ALA   A H    1 
ATOM   1021 H  H    B ALA   A 1 38  ? 22.683 -0.098  2.727   0.50 12.43 ?  38   ALA   A H    1 
ATOM   1022 H  HA   A ALA   A 1 38  ? 23.295 -1.561  0.651   0.50 11.59 ?  38   ALA   A HA   1 
ATOM   1023 H  HA   B ALA   A 1 38  ? 23.444 -1.709  0.718   0.50 12.64 ?  38   ALA   A HA   1 
ATOM   1024 H  HB1  A ALA   A 1 38  ? 21.479 -0.468  -0.336  0.50 12.52 ?  38   ALA   A HB1  1 
ATOM   1025 H  HB1  B ALA   A 1 38  ? 21.558 -0.903  -0.391  0.50 13.59 ?  38   ALA   A HB1  1 
ATOM   1026 H  HB2  A ALA   A 1 38  ? 21.057 -1.027  1.090   0.50 12.52 ?  38   ALA   A HB2  1 
ATOM   1027 H  HB2  B ALA   A 1 38  ? 21.154 -1.424  1.054   0.50 13.59 ?  38   ALA   A HB2  1 
ATOM   1028 H  HB3  A ALA   A 1 38  ? 21.392 0.516   0.908   0.50 12.52 ?  38   ALA   A HB3  1 
ATOM   1029 H  HB3  B ALA   A 1 38  ? 21.306 0.134   0.786   0.50 13.59 ?  38   ALA   A HB3  1 
ATOM   1030 N  N    A ALA   A 1 39  ? 25.257 -0.099  0.066   0.50 9.53  ?  39   ALA   A N    1 
ATOM   1031 N  N    B ALA   A 1 39  ? 25.253 -0.093  0.085   0.50 10.92 ?  39   ALA   A N    1 
ATOM   1032 C  CA   A ALA   A 1 39  ? 26.332 0.760   -0.403  0.50 9.26  ?  39   ALA   A CA   1 
ATOM   1033 C  CA   B ALA   A 1 39  ? 26.242 0.849   -0.409  0.50 11.09 ?  39   ALA   A CA   1 
ATOM   1034 C  C    A ALA   A 1 39  ? 26.461 0.726   -1.923  0.50 9.69  ?  39   ALA   A C    1 
ATOM   1035 C  C    B ALA   A 1 39  ? 26.383 0.759   -1.926  0.50 10.61 ?  39   ALA   A C    1 
ATOM   1036 O  O    A ALA   A 1 39  ? 25.982 -0.190  -2.598  0.50 10.17 ?  39   ALA   A O    1 
ATOM   1037 O  O    B ALA   A 1 39  ? 25.922 -0.184  -2.572  0.50 11.16 ?  39   ALA   A O    1 
ATOM   1038 C  CB   A ALA   A 1 39  ? 27.648 0.305   0.230   0.50 9.42  ?  39   ALA   A CB   1 
ATOM   1039 C  CB   B ALA   A 1 39  ? 27.587 0.565   0.254   0.50 11.93 ?  39   ALA   A CB   1 
ATOM   1040 H  H    A ALA   A 1 39  ? 25.507 -0.912  0.212   0.50 11.43 ?  39   ALA   A H    1 
ATOM   1041 H  H    B ALA   A 1 39  ? 25.580 -0.862  0.299   0.50 13.09 ?  39   ALA   A H    1 
ATOM   1042 H  HA   A ALA   A 1 39  ? 26.156 1.672   -0.132  0.50 11.11 ?  39   ALA   A HA   1 
ATOM   1043 H  HA   B ALA   A 1 39  ? 25.965 1.747   -0.176  0.50 13.30 ?  39   ALA   A HA   1 
ATOM   1044 H  HB1  A ALA   A 1 39  ? 28.361 0.882   -0.081  0.50 11.29 ?  39   ALA   A HB1  1 
ATOM   1045 H  HB1  B ALA   A 1 39  ? 28.238 1.197   -0.081  0.50 14.31 ?  39   ALA   A HB1  1 
ATOM   1046 H  HB2  A ALA   A 1 39  ? 27.568 0.369   1.197   0.50 11.29 ?  39   ALA   A HB2  1 
ATOM   1047 H  HB2  B ALA   A 1 39  ? 27.490 0.665   1.215   0.50 14.31 ?  39   ALA   A HB2  1 
ATOM   1048 H  HB3  A ALA   A 1 39  ? 27.822 -0.612  -0.027  0.50 11.29 ?  39   ALA   A HB3  1 
ATOM   1049 H  HB3  B ALA   A 1 39  ? 27.858 -0.341  0.041   0.50 14.31 ?  39   ALA   A HB3  1 
ATOM   1050 N  N    A ASN   A 1 40  ? 27.144 1.741   -2.457  0.50 10.16 ?  40   ASN   A N    1 
ATOM   1051 N  N    B ASN   A 1 40  ? 27.047 1.766   -2.492  0.50 10.57 ?  40   ASN   A N    1 
ATOM   1052 C  CA   A ASN   A 1 40  ? 27.682 1.707   -3.811  0.50 10.52 ?  40   ASN   A CA   1 
ATOM   1053 C  CA   B ASN   A 1 40  ? 27.557 1.709   -3.855  0.50 10.86 ?  40   ASN   A CA   1 
ATOM   1054 C  C    A ASN   A 1 40  ? 29.205 1.598   -3.750  0.50 9.97  ?  40   ASN   A C    1 
ATOM   1055 C  C    B ASN   A 1 40  ? 29.082 1.610   -3.821  0.50 10.54 ?  40   ASN   A C    1 
ATOM   1056 O  O    A ASN   A 1 40  ? 29.811 1.724   -2.685  0.50 10.19 ?  40   ASN   A O    1 
ATOM   1057 O  O    B ASN   A 1 40  ? 29.705 1.689   -2.760  0.50 10.51 ?  40   ASN   A O    1 
ATOM   1058 C  CB   A ASN   A 1 40  ? 27.207 2.900   -4.657  0.50 11.17 ?  40   ASN   A CB   1 
ATOM   1059 C  CB   B ASN   A 1 40  ? 27.063 2.896   -4.698  0.50 11.69 ?  40   ASN   A CB   1 
ATOM   1060 C  CG   A ASN   A 1 40  ? 27.596 4.242   -4.074  0.50 12.14 ?  40   ASN   A CG   1 
ATOM   1061 C  CG   B ASN   A 1 40  ? 27.411 4.238   -4.092  0.50 12.45 ?  40   ASN   A CG   1 
ATOM   1062 O  OD1  A ASN   A 1 40  ? 28.755 4.467   -3.718  0.50 13.04 ?  40   ASN   A OD1  1 
ATOM   1063 O  OD1  B ASN   A 1 40  ? 28.588 4.568   -3.917  0.50 13.41 ?  40   ASN   A OD1  1 
ATOM   1064 N  ND2  A ASN   A 1 40  ? 26.624 5.151   -3.987  0.50 12.39 ?  40   ASN   A ND2  1 
ATOM   1065 N  ND2  B ASN   A 1 40  ? 26.388 5.034   -3.797  0.50 12.73 ?  40   ASN   A ND2  1 
ATOM   1066 H  H    A ASN   A 1 40  ? 27.322 2.468   -2.038  0.50 12.19 ?  40   ASN   A H    1 
ATOM   1067 H  H    B ASN   A 1 40  ? 27.223 2.503   -2.091  0.50 12.68 ?  40   ASN   A H    1 
ATOM   1068 H  HA   A ASN   A 1 40  ? 27.367 0.902   -4.245  0.50 12.61 ?  40   ASN   A HA   1 
ATOM   1069 H  HA   B ASN   A 1 40  ? 27.222 0.895   -4.272  0.50 13.03 ?  40   ASN   A HA   1 
ATOM   1070 H  HB2  A ASN   A 1 40  ? 27.597 2.827   -5.546  0.50 13.40 ?  40   ASN   A HB2  1 
ATOM   1071 H  HB2  B ASN   A 1 40  ? 27.469 2.844   -5.574  0.50 14.02 ?  40   ASN   A HB2  1 
ATOM   1072 H  HB3  A ASN   A 1 40  ? 26.243 2.870   -4.718  0.50 13.40 ?  40   ASN   A HB3  1 
ATOM   1073 H  HB3  B ASN   A 1 40  ? 26.096 2.836   -4.777  0.50 14.02 ?  40   ASN   A HB3  1 
ATOM   1074 H  HD21 A ASN   A 1 40  ? 26.791 5.934   -3.673  0.50 14.86 ?  40   ASN   A HD21 1 
ATOM   1075 H  HD21 B ASN   A 1 40  ? 26.532 5.806   -3.453  0.50 15.27 ?  40   ASN   A HD21 1 
ATOM   1076 H  HD22 A ASN   A 1 40  ? 25.828 4.949   -4.238  0.50 14.86 ?  40   ASN   A HD22 1 
ATOM   1077 H  HD22 B ASN   A 1 40  ? 25.580 4.772   -3.945  0.50 15.27 ?  40   ASN   A HD22 1 
ATOM   1078 N  N    A VAL   A 1 41  ? 29.820 1.319   -4.904  0.50 10.19 ?  41   VAL   A N    1 
ATOM   1079 N  N    B VAL   A 1 41  ? 29.681 1.410   -4.998  0.50 10.97 ?  41   VAL   A N    1 
ATOM   1080 C  CA   A VAL   A 1 41  ? 31.253 1.037   -4.924  0.50 10.83 ?  41   VAL   A CA   1 
ATOM   1081 C  CA   B VAL   A 1 41  ? 31.106 1.082   -5.076  0.50 11.74 ?  41   VAL   A CA   1 
ATOM   1082 C  C    A VAL   A 1 41  ? 32.067 2.229   -4.462  0.50 11.51 ?  41   VAL   A C    1 
ATOM   1083 C  C    B VAL   A 1 41  ? 32.008 2.201   -4.565  0.50 11.43 ?  41   VAL   A C    1 
ATOM   1084 O  O    A VAL   A 1 41  ? 33.200 2.053   -4.002  0.50 12.16 ?  41   VAL   A O    1 
ATOM   1085 O  O    B VAL   A 1 41  ? 33.156 1.944   -4.188  0.50 11.21 ?  41   VAL   A O    1 
ATOM   1086 C  CB   A VAL   A 1 41  ? 31.758 0.535   -6.299  0.50 10.94 ?  41   VAL   A CB   1 
ATOM   1087 C  CB   B VAL   A 1 41  ? 31.507 0.675   -6.512  0.50 12.74 ?  41   VAL   A CB   1 
ATOM   1088 C  CG1  A VAL   A 1 41  ? 31.016 -0.725  -6.717  0.50 11.97 ?  41   VAL   A CG1  1 
ATOM   1089 C  CG1  B VAL   A 1 41  ? 30.933 -0.691  -6.858  0.50 13.68 ?  41   VAL   A CG1  1 
ATOM   1090 C  CG2  A VAL   A 1 41  ? 31.663 1.626   -7.369  0.50 10.01 ?  41   VAL   A CG2  1 
ATOM   1091 C  CG2  B VAL   A 1 41  ? 31.073 1.732   -7.525  0.50 13.16 ?  41   VAL   A CG2  1 
ATOM   1092 H  H    A VAL   A 1 41  ? 29.442 1.281   -5.672  0.50 12.22 ?  41   VAL   A H    1 
ATOM   1093 H  H    B VAL   A 1 41  ? 29.278 1.449   -5.757  0.50 13.15 ?  41   VAL   A H    1 
ATOM   1094 H  HA   A VAL   A 1 41  ? 31.435 0.326   -4.293  0.50 12.99 ?  41   VAL   A HA   1 
ATOM   1095 H  HA   B VAL   A 1 41  ? 31.265 0.310   -4.514  0.50 14.09 ?  41   VAL   A HA   1 
ATOM   1096 H  HB   A VAL   A 1 41  ? 32.698 0.300   -6.218  0.50 13.13 ?  41   VAL   A HB   1 
ATOM   1097 H  HB   B VAL   A 1 41  ? 32.473 0.603   -6.556  0.50 15.29 ?  41   VAL   A HB   1 
ATOM   1098 H  HG11 A VAL   A 1 41  ? 31.370 -1.037  -7.565  0.50 14.36 ?  41   VAL   A HG11 1 
ATOM   1099 H  HG11 B VAL   A 1 41  ? 31.249 -0.953  -7.737  0.50 16.42 ?  41   VAL   A HG11 1 
ATOM   1100 H  HG12 A VAL   A 1 41  ? 31.142 -1.404  -6.036  0.50 14.36 ?  41   VAL   A HG12 1 
ATOM   1101 H  HG12 B VAL   A 1 41  ? 31.231 -1.336  -6.195  0.50 16.42 ?  41   VAL   A HG12 1 
ATOM   1102 H  HG13 A VAL   A 1 41  ? 30.073 -0.518  -6.808  0.50 14.36 ?  41   VAL   A HG13 1 
ATOM   1103 H  HG13 B VAL   A 1 41  ? 29.966 -0.637  -6.855  0.50 16.42 ?  41   VAL   A HG13 1 
ATOM   1104 H  HG21 A VAL   A 1 41  ? 31.835 1.231   -8.240  0.50 12.01 ?  41   VAL   A HG21 1 
ATOM   1105 H  HG21 B VAL   A 1 41  ? 31.486 1.538   -8.380  0.50 15.79 ?  41   VAL   A HG21 1 
ATOM   1106 H  HG22 A VAL   A 1 41  ? 30.776 2.009   -7.348  0.50 12.01 ?  41   VAL   A HG22 1 
ATOM   1107 H  HG22 B VAL   A 1 41  ? 30.106 1.711   -7.616  0.50 15.79 ?  41   VAL   A HG22 1 
ATOM   1108 H  HG23 A VAL   A 1 41  ? 32.327 2.310   -7.183  0.50 12.01 ?  41   VAL   A HG23 1 
ATOM   1109 H  HG23 B VAL   A 1 41  ? 31.356 2.604   -7.211  0.50 15.79 ?  41   VAL   A HG23 1 
ATOM   1110 N  N    . TYR   A 1 42  ? 31.529 3.443   -4.577  1.00 11.39 ?  42   TYR   A N    1 
ATOM   1111 C  CA   . TYR   A 1 42  ? 32.271 4.627   -4.156  1.00 11.48 ?  42   TYR   A CA   1 
ATOM   1112 C  C    . TYR   A 1 42  ? 32.007 4.994   -2.706  1.00 11.29 ?  42   TYR   A C    1 
ATOM   1113 O  O    . TYR   A 1 42  ? 32.564 5.987   -2.217  1.00 11.82 ?  42   TYR   A O    1 
ATOM   1114 C  CB   . TYR   A 1 42  ? 31.926 5.819   -5.066  1.00 12.19 ?  42   TYR   A CB   1 
ATOM   1115 C  CG   . TYR   A 1 42  ? 32.104 5.515   -6.538  1.00 13.11 ?  42   TYR   A CG   1 
ATOM   1116 C  CD1  . TYR   A 1 42  ? 33.363 5.326   -7.076  1.00 13.92 ?  42   TYR   A CD1  1 
ATOM   1117 C  CD2  . TYR   A 1 42  ? 31.013 5.387   -7.382  1.00 14.54 ?  42   TYR   A CD2  1 
ATOM   1118 C  CE1  . TYR   A 1 42  ? 33.534 5.021   -8.418  1.00 14.41 ?  42   TYR   A CE1  1 
ATOM   1119 C  CE2  . TYR   A 1 42  ? 31.176 5.099   -8.724  1.00 15.56 ?  42   TYR   A CE2  1 
ATOM   1120 C  CZ   . TYR   A 1 42  ? 32.442 4.912   -9.236  1.00 15.18 ?  42   TYR   A CZ   1 
ATOM   1121 O  OH   . TYR   A 1 42  ? 32.606 4.620   -10.568 1.00 17.15 ?  42   TYR   A OH   1 
ATOM   1122 H  H    A TYR   A 1 42  ? 30.740 3.604   -4.883  0.50 13.66 ?  42   TYR   A H    1 
ATOM   1123 H  H    B TYR   A 1 42  ? 30.736 3.635   -4.856  0.50 13.66 ?  42   TYR   A H    1 
ATOM   1124 H  HA   . TYR   A 1 42  ? 33.220 4.455   -4.253  1.00 13.77 ?  42   TYR   A HA   1 
ATOM   1125 H  HB2  . TYR   A 1 42  ? 31.000 6.072   -4.921  1.00 14.63 ?  42   TYR   A HB2  1 
ATOM   1126 H  HB3  . TYR   A 1 42  ? 32.508 6.567   -4.843  1.00 14.63 ?  42   TYR   A HB3  1 
ATOM   1127 H  HD1  . TYR   A 1 42  ? 34.109 5.391   -6.526  1.00 16.70 ?  42   TYR   A HD1  1 
ATOM   1128 H  HD2  . TYR   A 1 42  ? 30.157 5.516   -7.040  1.00 17.44 ?  42   TYR   A HD2  1 
ATOM   1129 H  HE1  . TYR   A 1 42  ? 34.387 4.897   -8.763  1.00 17.29 ?  42   TYR   A HE1  1 
ATOM   1130 H  HE2  . TYR   A 1 42  ? 30.431 5.023   -9.279  1.00 18.67 ?  42   TYR   A HE2  1 
ATOM   1131 H  HH   . TYR   A 1 42  ? 33.424 4.527   -10.744 1.00 20.58 ?  42   TYR   A HH   1 
ATOM   1132 N  N    . LEU   A 1 43  ? 31.162 4.229   -2.020  1.00 10.86 ?  43   LEU   A N    1 
ATOM   1133 C  CA   . LEU   A 1 43  ? 30.723 4.558   -0.669  1.00 10.38 ?  43   LEU   A CA   1 
ATOM   1134 C  C    . LEU   A 1 43  ? 30.234 6.002   -0.567  1.00 10.49 ?  43   LEU   A C    1 
ATOM   1135 O  O    . LEU   A 1 43  ? 30.495 6.697   0.416   1.00 11.62 ?  43   LEU   A O    1 
ATOM   1136 C  CB   . LEU   A 1 43  ? 31.778 4.255   0.390   1.00 10.68 ?  43   LEU   A CB   1 
ATOM   1137 C  CG   . LEU   A 1 43  ? 32.272 2.806   0.480   1.00 11.35 ?  43   LEU   A CG   1 
ATOM   1138 C  CD1  . LEU   A 1 43  ? 33.304 2.701   1.585   1.00 12.45 ?  43   LEU   A CD1  1 
ATOM   1139 C  CD2  . LEU   A 1 43  ? 31.134 1.821   0.725   1.00 11.27 ?  43   LEU   A CD2  1 
ATOM   1140 H  H    . LEU   A 1 43  ? 30.823 3.488   -2.319  1.00 13.02 ?  43   LEU   A H    1 
ATOM   1141 H  HA   . LEU   A 1 43  ? 29.956 3.992   -0.465  1.00 12.46 ?  43   LEU   A HA   1 
ATOM   1142 H  HB2  . LEU   A 1 43  ? 32.548 4.813   0.220   1.00 12.81 ?  43   LEU   A HB2  1 
ATOM   1143 H  HB3  . LEU   A 1 43  ? 31.402 4.479   1.259   1.00 12.81 ?  43   LEU   A HB3  1 
ATOM   1144 H  HG   . LEU   A 1 43  ? 32.704 2.561   -0.354  1.00 13.62 ?  43   LEU   A HG   1 
ATOM   1145 H  HD11 . LEU   A 1 43  ? 33.617 1.784   1.641   1.00 14.94 ?  43   LEU   A HD11 1 
ATOM   1146 H  HD12 . LEU   A 1 43  ? 34.042 3.293   1.383   1.00 14.94 ?  43   LEU   A HD12 1 
ATOM   1147 H  HD13 . LEU   A 1 43  ? 32.890 2.959   2.425   1.00 14.94 ?  43   LEU   A HD13 1 
ATOM   1148 H  HD21 . LEU   A 1 43  ? 31.508 0.939   0.871   1.00 13.51 ?  43   LEU   A HD21 1 
ATOM   1149 H  HD22 . LEU   A 1 43  ? 30.640 2.106   1.509   1.00 13.51 ?  43   LEU   A HD22 1 
ATOM   1150 H  HD23 . LEU   A 1 43  ? 30.555 1.815   -0.050  1.00 13.51 ?  43   LEU   A HD23 1 
ATOM   1151 N  N    A LYS   A 1 44  ? 29.505 6.450   -1.588  0.50 10.69 ?  44   LYS   A N    1 
ATOM   1152 N  N    B LYS   A 1 44  ? 29.512 6.449   -1.596  0.50 10.65 ?  44   LYS   A N    1 
ATOM   1153 C  CA   A LYS   A 1 44  ? 28.870 7.767   -1.577  0.50 11.29 ?  44   LYS   A CA   1 
ATOM   1154 C  CA   B LYS   A 1 44  ? 28.853 7.754   -1.596  0.50 11.14 ?  44   LYS   A CA   1 
ATOM   1155 C  C    A LYS   A 1 44  ? 27.439 7.582   -1.089  0.50 10.68 ?  44   LYS   A C    1 
ATOM   1156 C  C    B LYS   A 1 44  ? 27.438 7.540   -1.076  0.50 10.60 ?  44   LYS   A C    1 
ATOM   1157 O  O    A LYS   A 1 44  ? 26.566 7.125   -1.830  0.50 11.69 ?  44   LYS   A O    1 
ATOM   1158 O  O    B LYS   A 1 44  ? 26.575 7.008   -1.779  0.50 11.48 ?  44   LYS   A O    1 
ATOM   1159 C  CB   A LYS   A 1 44  ? 28.931 8.412   -2.955  0.50 13.62 ?  44   LYS   A CB   1 
ATOM   1160 C  CB   B LYS   A 1 44  ? 28.852 8.362   -2.992  0.50 13.59 ?  44   LYS   A CB   1 
ATOM   1161 C  CG   A LYS   A 1 44  ? 30.330 8.833   -3.379  0.50 16.84 ?  44   LYS   A CG   1 
ATOM   1162 C  CG   B LYS   A 1 44  ? 30.199 8.891   -3.451  0.50 16.94 ?  44   LYS   A CG   1 
ATOM   1163 C  CD   A LYS   A 1 44  ? 31.002 9.748   -2.360  0.50 21.41 ?  44   LYS   A CD   1 
ATOM   1164 C  CD   B LYS   A 1 44  ? 30.856 9.787   -2.408  0.50 21.38 ?  44   LYS   A CD   1 
ATOM   1165 C  CE   A LYS   A 1 44  ? 32.345 10.240  -2.865  0.50 24.26 ?  44   LYS   A CE   1 
ATOM   1166 C  CE   B LYS   A 1 44  ? 32.106 10.442  -2.960  0.50 23.95 ?  44   LYS   A CE   1 
ATOM   1167 N  NZ   A LYS   A 1 44  ? 33.110 10.953  -1.808  0.50 25.90 ?  44   LYS   A NZ   1 
ATOM   1168 N  NZ   B LYS   A 1 44  ? 33.028 10.884  -1.879  0.50 25.50 ?  44   LYS   A NZ   1 
ATOM   1169 H  H    A LYS   A 1 44  ? 29.368 6.003   -2.312  0.50 12.83 ?  44   LYS   A H    1 
ATOM   1170 H  H    B LYS   A 1 44  ? 29.391 6.004   -2.324  0.50 12.77 ?  44   LYS   A H    1 
ATOM   1171 H  HA   A LYS   A 1 44  ? 29.324 8.335   -0.939  0.50 13.54 ?  44   LYS   A HA   1 
ATOM   1172 H  HA   B LYS   A 1 44  ? 29.306 8.347   -0.978  0.50 13.36 ?  44   LYS   A HA   1 
ATOM   1173 H  HB2  A LYS   A 1 44  ? 28.599 7.780   -3.611  0.50 16.33 ?  44   LYS   A HB2  1 
ATOM   1174 H  HB2  B LYS   A 1 44  ? 28.572 7.684   -3.627  0.50 16.31 ?  44   LYS   A HB2  1 
ATOM   1175 H  HB3  A LYS   A 1 44  ? 28.372 9.205   -2.950  0.50 16.33 ?  44   LYS   A HB3  1 
ATOM   1176 H  HB3  B LYS   A 1 44  ? 28.226 9.103   -3.009  0.50 16.31 ?  44   LYS   A HB3  1 
ATOM   1177 H  HG2  A LYS   A 1 44  ? 30.882 8.042   -3.483  0.50 20.20 ?  44   LYS   A HG2  1 
ATOM   1178 H  HG2  B LYS   A 1 44  ? 30.794 8.144   -3.625  0.50 20.32 ?  44   LYS   A HG2  1 
ATOM   1179 H  HG3  A LYS   A 1 44  ? 30.275 9.313   -4.221  0.50 20.20 ?  44   LYS   A HG3  1 
ATOM   1180 H  HG3  B LYS   A 1 44  ? 30.078 9.415   -4.261  0.50 20.32 ?  44   LYS   A HG3  1 
ATOM   1181 H  HD2  A LYS   A 1 44  ? 30.427 10.513  -2.192  0.50 25.68 ?  44   LYS   A HD2  1 
ATOM   1182 H  HD2  B LYS   A 1 44  ? 30.230 10.477  -2.139  0.50 25.65 ?  44   LYS   A HD2  1 
ATOM   1183 H  HD3  A LYS   A 1 44  ? 31.153 9.254   -1.538  0.50 25.68 ?  44   LYS   A HD3  1 
ATOM   1184 H  HD3  B LYS   A 1 44  ? 31.115 9.248   -1.642  0.50 25.65 ?  44   LYS   A HD3  1 
ATOM   1185 H  HE2  A LYS   A 1 44  ? 32.870 9.480   -3.160  0.50 29.11 ?  44   LYS   A HE2  1 
ATOM   1186 H  HE2  B LYS   A 1 44  ? 32.580 9.803   -3.516  0.50 28.74 ?  44   LYS   A HE2  1 
ATOM   1187 H  HE3  A LYS   A 1 44  ? 32.199 10.853  -3.602  0.50 29.11 ?  44   LYS   A HE3  1 
ATOM   1188 H  HE3  B LYS   A 1 44  ? 31.854 11.218  -3.481  0.50 28.74 ?  44   LYS   A HE3  1 
ATOM   1189 H  HZ1  A LYS   A 1 44  ? 33.891 11.227  -2.132  0.50 31.07 ?  44   LYS   A HZ1  1 
ATOM   1190 H  HZ1  B LYS   A 1 44  ? 33.750 11.266  -2.233  0.50 30.59 ?  44   LYS   A HZ1  1 
ATOM   1191 H  HZ2  A LYS   A 1 44  ? 32.649 11.662  -1.526  0.50 31.07 ?  44   LYS   A HZ2  1 
ATOM   1192 H  HZ2  B LYS   A 1 44  ? 32.617 11.477  -1.355  0.50 30.59 ?  44   LYS   A HZ2  1 
ATOM   1193 H  HZ3  A LYS   A 1 44  ? 33.254 10.411  -1.118  0.50 31.07 ?  44   LYS   A HZ3  1 
ATOM   1194 H  HZ3  B LYS   A 1 44  ? 33.279 10.188  -1.387  0.50 30.59 ?  44   LYS   A HZ3  1 
ATOM   1195 N  N    . HIS   A 1 45  ? 27.206 7.931   0.173   1.00 10.34 ?  45   HIS   A N    1 
ATOM   1196 C  CA   . HIS   A 1 45  ? 25.966 7.595   0.863   1.00 10.65 ?  45   HIS   A CA   1 
ATOM   1197 C  C    . HIS   A 1 45  ? 24.944 8.718   0.704   1.00 11.06 ?  45   HIS   A C    1 
ATOM   1198 O  O    . HIS   A 1 45  ? 24.629 9.450   1.638   1.00 12.80 ?  45   HIS   A O    1 
ATOM   1199 C  CB   . HIS   A 1 45  ? 26.259 7.330   2.326   1.00 10.71 ?  45   HIS   A CB   1 
ATOM   1200 C  CG   . HIS   A 1 45  ? 27.384 6.371   2.549   1.00 10.14 ?  45   HIS   A CG   1 
ATOM   1201 N  ND1  . HIS   A 1 45  ? 27.385 5.084   2.047   1.00 10.75 ?  45   HIS   A ND1  1 
ATOM   1202 C  CD2  . HIS   A 1 45  ? 28.549 6.528   3.222   1.00 10.55 ?  45   HIS   A CD2  1 
ATOM   1203 C  CE1  . HIS   A 1 45  ? 28.507 4.493   2.418   1.00 10.27 ?  45   HIS   A CE1  1 
ATOM   1204 N  NE2  . HIS   A 1 45  ? 29.231 5.344   3.129   1.00 10.62 ?  45   HIS   A NE2  1 
ATOM   1205 H  H    A HIS   A 1 45  ? 27.758 8.379   0.658   0.50 12.40 ?  45   HIS   A H    1 
ATOM   1206 H  H    B HIS   A 1 45  ? 27.754 8.394   0.648   0.50 12.40 ?  45   HIS   A H    1 
ATOM   1207 H  HA   . HIS   A 1 45  ? 25.592 6.788   0.478   1.00 12.77 ?  45   HIS   A HA   1 
ATOM   1208 H  HB2  . HIS   A 1 45  ? 26.485 8.167   2.760   1.00 12.85 ?  45   HIS   A HB2  1 
ATOM   1209 H  HB3  . HIS   A 1 45  ? 25.460 6.955   2.742   1.00 12.85 ?  45   HIS   A HB3  1 
ATOM   1210 H  HD2  . HIS   A 1 45  ? 28.831 7.295   3.668   1.00 12.66 ?  45   HIS   A HD2  1 
ATOM   1211 H  HE1  . HIS   A 1 45  ? 28.745 3.616   2.220   1.00 12.32 ?  45   HIS   A HE1  1 
ATOM   1212 H  HE2  . HIS   A 1 45  ? 30.000 5.180   3.476   1.00 12.74 ?  45   HIS   A HE2  1 
ATOM   1213 N  N    . GLY   A 1 46  ? 24.406 8.823   -0.504  1.00 11.96 ?  46   GLY   A N    1 
ATOM   1214 C  CA   . GLY   A 1 46  ? 23.594 9.977   -0.842  1.00 12.76 ?  46   GLY   A CA   1 
ATOM   1215 C  C    . GLY   A 1 46  ? 22.112 9.855   -0.552  1.00 12.64 ?  46   GLY   A C    1 
ATOM   1216 O  O    . GLY   A 1 46  ? 21.452 10.844  -0.217  1.00 14.31 ?  46   GLY   A O    1 
ATOM   1217 H  H    . GLY   A 1 46  ? 24.478 8.243   -1.133  1.00 14.35 ?  46   GLY   A H    1 
ATOM   1218 H  HA2  . GLY   A 1 46  ? 23.919 10.751  -0.352  1.00 15.31 ?  46   GLY   A HA2  1 
ATOM   1219 H  HA3  . GLY   A 1 46  ? 23.691 10.167  -1.790  1.00 15.31 ?  46   GLY   A HA3  1 
ATOM   1220 N  N    A GLY   A 1 47  ? 21.579 8.654   -0.719  0.50 12.51 ?  47   GLY   A N    1 
ATOM   1221 N  N    B GLY   A 1 47  ? 21.565 8.645   -0.668  0.50 12.65 ?  47   GLY   A N    1 
ATOM   1222 C  CA   A GLY   A 1 47  ? 20.147 8.456   -0.657  0.50 12.73 ?  47   GLY   A CA   1 
ATOM   1223 C  CA   B GLY   A 1 47  ? 20.133 8.449   -0.525  0.50 13.05 ?  47   GLY   A CA   1 
ATOM   1224 C  C    A GLY   A 1 47  ? 19.837 7.006   -0.376  0.50 11.64 ?  47   GLY   A C    1 
ATOM   1225 C  C    B GLY   A 1 47  ? 19.796 7.030   -0.111  0.50 12.19 ?  47   GLY   A C    1 
ATOM   1226 O  O    A GLY   A 1 47  ? 20.731 6.176   -0.191  0.50 11.44 ?  47   GLY   A O    1 
ATOM   1227 O  O    B GLY   A 1 47  ? 20.678 6.196   0.110   0.50 12.13 ?  47   GLY   A O    1 
ATOM   1228 H  H    A GLY   A 1 47  ? 22.031 7.942   -0.863  0.50 15.00 ?  47   GLY   A H    1 
ATOM   1229 H  H    B GLY   A 1 47  ? 22.005 7.924   -0.825  0.50 15.17 ?  47   GLY   A H    1 
ATOM   1230 H  HA2  A GLY   A 1 47  ? 19.767 9.001   0.047   0.50 15.27 ?  47   GLY   A HA2  1 
ATOM   1231 H  HA2  B GLY   A 1 47  ? 19.783 9.045   0.152   0.50 15.65 ?  47   GLY   A HA2  1 
ATOM   1232 H  HA3  A GLY   A 1 47  ? 19.746 8.704   -1.502  0.50 15.27 ?  47   GLY   A HA3  1 
ATOM   1233 H  HA3  B GLY   A 1 47  ? 19.689 8.644   -1.367  0.50 15.65 ?  47   GLY   A HA3  1 
ATOM   1234 N  N    A GLY   A 1 48  ? 18.545 6.701   -0.366  0.50 11.01 ?  48   GLY   A N    1 
ATOM   1235 N  N    B GLY   A 1 48  ? 18.492 6.762   -0.004  0.50 11.94 ?  48   GLY   A N    1 
ATOM   1236 C  CA   A GLY   A 1 48  ? 18.154 5.366   0.012   0.50 11.35 ?  48   GLY   A CA   1 
ATOM   1237 C  CA   B GLY   A 1 48  ? 18.048 5.433   0.390   0.50 11.27 ?  48   GLY   A CA   1 
ATOM   1238 C  C    A GLY   A 1 48  ? 18.577 5.068   1.436   0.50 10.42 ?  48   GLY   A C    1 
ATOM   1239 C  C    B GLY   A 1 48  ? 18.564 5.049   1.766   0.50 11.20 ?  48   GLY   A C    1 
ATOM   1240 O  O    A GLY   A 1 48  ? 18.731 5.964   2.275   0.50 10.91 ?  48   GLY   A O    1 
ATOM   1241 O  O    B GLY   A 1 48  ? 18.731 5.886   2.664   0.50 11.48 ?  48   GLY   A O    1 
ATOM   1242 H  H    A GLY   A 1 48  ? 17.902 7.237   -0.562  0.50 13.20 ?  48   GLY   A H    1 
ATOM   1243 H  H    B GLY   A 1 48  ? 17.843 7.324   -0.148  0.50 14.33 ?  48   GLY   A H    1 
ATOM   1244 H  HA2  A GLY   A 1 48  ? 17.195 5.272   -0.051  0.50 13.61 ?  48   GLY   A HA2  1 
ATOM   1245 H  HA2  B GLY   A 1 48  ? 17.075 5.390   0.388   0.50 13.52 ?  48   GLY   A HA2  1 
ATOM   1246 H  HA3  A GLY   A 1 48  ? 18.577 4.722   -0.577  0.50 13.61 ?  48   GLY   A HA3  1 
ATOM   1247 H  HA3  B GLY   A 1 48  ? 18.376 4.779   -0.250  0.50 13.52 ?  48   GLY   A HA3  1 
ATOM   1248 N  N    A VAL   A 1 49  ? 18.768 3.777   1.716   0.50 10.86 ?  49   VAL   A N    1 
ATOM   1249 N  N    B VAL   A 1 49  ? 18.798 3.744   1.940   0.50 10.67 ?  49   VAL   A N    1 
ATOM   1250 C  CA   A VAL   A 1 49  ? 19.218 3.357   3.039   0.50 10.94 ?  49   VAL   A CA   1 
ATOM   1251 C  CA   B VAL   A 1 49  ? 19.360 3.232   3.188   0.50 10.49 ?  49   VAL   A CA   1 
ATOM   1252 C  C    A VAL   A 1 49  ? 20.542 4.023   3.402   0.50 10.58 ?  49   VAL   A C    1 
ATOM   1253 C  C    B VAL   A 1 49  ? 20.656 3.958   3.528   0.50 9.97  ?  49   VAL   A C    1 
ATOM   1254 O  O    A VAL   A 1 49  ? 20.741 4.450   4.543   0.50 11.03 ?  49   VAL   A O    1 
ATOM   1255 O  O    B VAL   A 1 49  ? 20.875 4.372   4.671   0.50 10.07 ?  49   VAL   A O    1 
ATOM   1256 C  CB   A VAL   A 1 49  ? 19.314 1.821   3.104   0.50 11.89 ?  49   VAL   A CB   1 
ATOM   1257 C  CB   B VAL   A 1 49  ? 19.582 1.711   3.085   0.50 11.10 ?  49   VAL   A CB   1 
ATOM   1258 C  CG1  A VAL   A 1 49  ? 20.037 1.381   4.372   0.50 12.39 ?  49   VAL   A CG1  1 
ATOM   1259 C  CG1  B VAL   A 1 49  ? 20.456 1.218   4.232   0.50 10.37 ?  49   VAL   A CG1  1 
ATOM   1260 C  CG2  A VAL   A 1 49  ? 17.925 1.197   3.029   0.50 13.06 ?  49   VAL   A CG2  1 
ATOM   1261 C  CG2  B VAL   A 1 49  ? 18.254 0.972   3.062   0.50 12.34 ?  49   VAL   A CG2  1 
ATOM   1262 H  H    A VAL   A 1 49  ? 18.636 3.133   1.166   0.50 13.03 ?  49   VAL   A H    1 
ATOM   1263 H  H    B VAL   A 1 49  ? 18.637 3.137   1.353   0.50 12.80 ?  49   VAL   A H    1 
ATOM   1264 H  HA   A VAL   A 1 49  ? 18.562 3.633   3.697   0.50 13.12 ?  49   VAL   A HA   1 
ATOM   1265 H  HA   B VAL   A 1 49  ? 18.735 3.391   3.911   0.50 12.58 ?  49   VAL   A HA   1 
ATOM   1266 H  HB   A VAL   A 1 49  ? 19.829 1.504   2.345   0.50 14.27 ?  49   VAL   A HB   1 
ATOM   1267 H  HB   B VAL   A 1 49  ? 20.046 1.517   2.256   0.50 13.31 ?  49   VAL   A HB   1 
ATOM   1268 H  HG11 A VAL   A 1 49  ? 19.846 0.443   4.532   0.50 14.86 ?  49   VAL   A HG11 1 
ATOM   1269 H  HG11 B VAL   A 1 49  ? 20.343 0.259   4.323   0.50 12.43 ?  49   VAL   A HG11 1 
ATOM   1270 H  HG12 A VAL   A 1 49  ? 20.990 1.509   4.259   0.50 14.86 ?  49   VAL   A HG12 1 
ATOM   1271 H  HG12 B VAL   A 1 49  ? 21.386 1.420   4.036   0.50 12.43 ?  49   VAL   A HG12 1 
ATOM   1272 H  HG13 A VAL   A 1 49  ? 19.713 1.912   5.118   0.50 14.86 ?  49   VAL   A HG13 1 
ATOM   1273 H  HG13 B VAL   A 1 49  ? 20.186 1.661   5.051   0.50 12.43 ?  49   VAL   A HG13 1 
ATOM   1274 H  HG21 A VAL   A 1 49  ? 18.012 0.231   3.070   0.50 15.67 ?  49   VAL   A HG21 1 
ATOM   1275 H  HG21 B VAL   A 1 49  ? 18.423 0.023   2.957   0.50 14.80 ?  49   VAL   A HG21 1 
ATOM   1276 H  HG22 A VAL   A 1 49  ? 17.397 1.513   3.777   0.50 15.67 ?  49   VAL   A HG22 1 
ATOM   1277 H  HG22 B VAL   A 1 49  ? 17.789 1.134   3.898   0.50 14.80 ?  49   VAL   A HG22 1 
ATOM   1278 H  HG23 A VAL   A 1 49  ? 17.509 1.457   2.193   0.50 15.67 ?  49   VAL   A HG23 1 
ATOM   1279 H  HG23 B VAL   A 1 49  ? 17.724 1.299   2.319   0.50 14.80 ?  49   VAL   A HG23 1 
ATOM   1280 N  N    A ALA   A 1 50  ? 21.480 4.088   2.453   0.50 10.34 ?  50   ALA   A N    1 
ATOM   1281 N  N    B ALA   A 1 50  ? 21.547 4.087   2.543   0.50 9.87  ?  50   ALA   A N    1 
ATOM   1282 C  CA   A ALA   A 1 50  ? 22.798 4.639   2.759   0.50 10.28 ?  50   ALA   A CA   1 
ATOM   1283 C  CA   B ALA   A 1 50  ? 22.861 4.666   2.801   0.50 9.89  ?  50   ALA   A CA   1 
ATOM   1284 C  C    A ALA   A 1 50  ? 22.716 6.107   3.145   0.50 10.18 ?  50   ALA   A C    1 
ATOM   1285 C  C    B ALA   A 1 50  ? 22.743 6.101   3.287   0.50 9.59  ?  50   ALA   A C    1 
ATOM   1286 O  O    A ALA   A 1 50  ? 23.385 6.546   4.089   0.50 10.90 ?  50   ALA   A O    1 
ATOM   1287 O  O    B ALA   A 1 50  ? 23.353 6.482   4.294   0.50 9.76  ?  50   ALA   A O    1 
ATOM   1288 C  CB   A ALA   A 1 50  ? 23.732 4.463   1.567   0.50 10.49 ?  50   ALA   A CB   1 
ATOM   1289 C  CB   B ALA   A 1 50  ? 23.718 4.593   1.541   0.50 10.17 ?  50   ALA   A CB   1 
ATOM   1290 H  H    A ALA   A 1 50  ? 21.380 3.821   1.643   0.50 12.40 ?  50   ALA   A H    1 
ATOM   1291 H  H    B ALA   A 1 50  ? 21.412 3.855   1.726   0.50 11.84 ?  50   ALA   A H    1 
ATOM   1292 H  HA   A ALA   A 1 50  ? 23.175 4.158   3.511   0.50 12.34 ?  50   ALA   A HA   1 
ATOM   1293 H  HA   B ALA   A 1 50  ? 23.301 4.160   3.496   0.50 11.86 ?  50   ALA   A HA   1 
ATOM   1294 H  HB1  A ALA   A 1 50  ? 24.600 4.838   1.790   0.50 12.58 ?  50   ALA   A HB1  1 
ATOM   1295 H  HB1  B ALA   A 1 50  ? 24.589 4.980   1.727   0.50 12.20 ?  50   ALA   A HB1  1 
ATOM   1296 H  HB2  A ALA   A 1 50  ? 23.818 3.519   1.371   0.50 12.58 ?  50   ALA   A HB2  1 
ATOM   1297 H  HB2  B ALA   A 1 50  ? 23.821 3.662   1.283   0.50 12.20 ?  50   ALA   A HB2  1 
ATOM   1298 H  HB3  A ALA   A 1 50  ? 23.358 4.930   0.803   0.50 12.58 ?  50   ALA   A HB3  1 
ATOM   1299 H  HB3  B ALA   A 1 50  ? 23.282 5.086   0.829   0.50 12.20 ?  50   ALA   A HB3  1 
ATOM   1300 N  N    A GLY   A 1 51  ? 21.930 6.892   2.409   0.50 10.16 ?  51   GLY   A N    1 
ATOM   1301 N  N    B GLY   A 1 51  ? 21.963 6.918   2.580   0.50 10.44 ?  51   GLY   A N    1 
ATOM   1302 C  CA   A GLY   A 1 51  ? 21.787 8.295   2.759   0.50 10.34 ?  51   GLY   A CA   1 
ATOM   1303 C  CA   B GLY   A 1 51  ? 21.778 8.285   3.026   0.50 10.51 ?  51   GLY   A CA   1 
ATOM   1304 C  C    A GLY   A 1 51  ? 21.178 8.488   4.135   0.50 9.70  ?  51   GLY   A C    1 
ATOM   1305 C  C    B GLY   A 1 51  ? 21.193 8.342   4.423   0.50 10.93 ?  51   GLY   A C    1 
ATOM   1306 O  O    A GLY   A 1 51  ? 21.546 9.411   4.865   0.50 9.75  ?  51   GLY   A O    1 
ATOM   1307 O  O    B GLY   A 1 51  ? 21.584 9.179   5.241   0.50 11.12 ?  51   GLY   A O    1 
ATOM   1308 H  H    A GLY   A 1 51  ? 21.497 6.643   1.710   0.50 12.19 ?  51   GLY   A H    1 
ATOM   1309 H  H    B GLY   A 1 51  ? 21.535 6.705   1.863   0.50 12.53 ?  51   GLY   A H    1 
ATOM   1310 H  HA2  A GLY   A 1 51  ? 22.656 8.725   2.740   0.50 12.40 ?  51   GLY   A HA2  1 
ATOM   1311 H  HA2  B GLY   A 1 51  ? 22.632 8.744   3.033   0.50 12.61 ?  51   GLY   A HA2  1 
ATOM   1312 H  HA3  A GLY   A 1 51  ? 21.214 8.731   2.109   0.50 12.40 ?  51   GLY   A HA3  1 
ATOM   1313 H  HA3  B GLY   A 1 51  ? 21.189 8.752   2.402   0.50 12.61 ?  51   GLY   A HA3  1 
ATOM   1314 N  N    A ALA   A 1 52  ? 20.232 7.621   4.507   0.50 10.01 ?  52   ALA   A N    1 
ATOM   1315 N  N    B ALA   A 1 52  ? 20.224 7.467   4.704   0.50 11.24 ?  52   ALA   A N    1 
ATOM   1316 C  CA   A ALA   A 1 52  ? 19.584 7.736   5.809   0.50 10.70 ?  52   ALA   A CA   1 
ATOM   1317 C  CA   B ALA   A 1 52  ? 19.578 7.458   6.012   0.50 11.50 ?  52   ALA   A CA   1 
ATOM   1318 C  C    A ALA   A 1 52  ? 20.517 7.313   6.942   0.50 10.10 ?  52   ALA   A C    1 
ATOM   1319 C  C    B ALA   A 1 52  ? 20.561 7.056   7.105   0.50 11.06 ?  52   ALA   A C    1 
ATOM   1320 O  O    A ALA   A 1 52  ? 20.598 7.993   7.971   0.50 10.66 ?  52   ALA   A O    1 
ATOM   1321 O  O    B ALA   A 1 52  ? 20.632 7.698   8.160   0.50 11.73 ?  52   ALA   A O    1 
ATOM   1322 C  CB   A ALA   A 1 52  ? 18.295 6.913   5.822   0.50 11.46 ?  52   ALA   A CB   1 
ATOM   1323 C  CB   B ALA   A 1 52  ? 18.378 6.511   5.982   0.50 11.97 ?  52   ALA   A CB   1 
ATOM   1324 H  H    A ALA   A 1 52  ? 19.956 6.964   4.026   0.50 12.01 ?  52   ALA   A H    1 
ATOM   1325 H  H    B ALA   A 1 52  ? 19.937 6.861   4.156   0.50 13.48 ?  52   ALA   A H    1 
ATOM   1326 H  HA   A ALA   A 1 52  ? 19.342 8.661   5.953   0.50 12.83 ?  52   ALA   A HA   1 
ATOM   1327 H  HA   B ALA   A 1 52  ? 19.253 8.348   6.207   0.50 13.79 ?  52   ALA   A HA   1 
ATOM   1328 H  HB1  A ALA   A 1 52  ? 17.870 7.001   6.692   0.50 13.75 ?  52   ALA   A HB1  1 
ATOM   1329 H  HB1  B ALA   A 1 52  ? 17.955 6.515   6.854   0.50 14.35 ?  52   ALA   A HB1  1 
ATOM   1330 H  HB2  A ALA   A 1 52  ? 17.698 7.246   5.131   0.50 13.75 ?  52   ALA   A HB2  1 
ATOM   1331 H  HB2  B ALA   A 1 52  ? 17.749 6.817   5.308   0.50 14.35 ?  52   ALA   A HB2  1 
ATOM   1332 H  HB3  A ALA   A 1 52  ? 18.507 5.982   5.652   0.50 13.75 ?  52   ALA   A HB3  1 
ATOM   1333 H  HB3  B ALA   A 1 52  ? 18.684 5.617   5.765   0.50 14.35 ?  52   ALA   A HB3  1 
ATOM   1334 N  N    A LEU   A 1 53  ? 21.225 6.192   6.781   0.50 9.94  ?  53   LEU   A N    1 
ATOM   1335 N  N    B LEU   A 1 53  ? 21.323 5.983   6.877   0.50 10.67 ?  53   LEU   A N    1 
ATOM   1336 C  CA   A LEU   A 1 53  ? 22.164 5.765   7.815   0.50 10.60 ?  53   LEU   A CA   1 
ATOM   1337 C  CA   B LEU   A 1 53  ? 22.341 5.600   7.850   0.50 10.62 ?  53   LEU   A CA   1 
ATOM   1338 C  C    A LEU   A 1 53  ? 23.239 6.820   8.026   0.50 10.27 ?  53   LEU   A C    1 
ATOM   1339 C  C    B LEU   A 1 53  ? 23.362 6.712   8.032   0.50 10.34 ?  53   LEU   A C    1 
ATOM   1340 O  O    A LEU   A 1 53  ? 23.538 7.207   9.160   0.50 10.72 ?  53   LEU   A O    1 
ATOM   1341 O  O    B LEU   A 1 53  ? 23.728 7.047   9.162   0.50 11.31 ?  53   LEU   A O    1 
ATOM   1342 C  CB   A LEU   A 1 53  ? 22.801 4.427   7.434   0.50 11.33 ?  53   LEU   A CB   1 
ATOM   1343 C  CB   B LEU   A 1 53  ? 23.035 4.305   7.424   0.50 10.57 ?  53   LEU   A CB   1 
ATOM   1344 C  CG   A LEU   A 1 53  ? 21.905 3.182   7.474   0.50 11.77 ?  53   LEU   A CG   1 
ATOM   1345 C  CG   B LEU   A 1 53  ? 22.236 3.004   7.531   0.50 10.52 ?  53   LEU   A CG   1 
ATOM   1346 C  CD1  A LEU   A 1 53  ? 22.630 1.978   6.892   0.50 11.58 ?  53   LEU   A CD1  1 
ATOM   1347 C  CD1  B LEU   A 1 53  ? 23.016 1.870   6.884   0.50 10.97 ?  53   LEU   A CD1  1 
ATOM   1348 C  CD2  A LEU   A 1 53  ? 21.430 2.881   8.891   0.50 13.01 ?  53   LEU   A CD2  1 
ATOM   1349 C  CD2  B LEU   A 1 53  ? 21.919 2.663   8.979   0.50 10.85 ?  53   LEU   A CD2  1 
ATOM   1350 H  H    A LEU   A 1 53  ? 21.178 5.676   6.098   0.50 11.92 ?  53   LEU   A H    1 
ATOM   1351 H  H    B LEU   A 1 53  ? 21.266 5.470   6.185   0.50 12.80 ?  53   LEU   A H    1 
ATOM   1352 H  HA   A LEU   A 1 53  ? 21.689 5.651   8.652   0.50 12.71 ?  53   LEU   A HA   1 
ATOM   1353 H  HA   B LEU   A 1 53  ? 21.911 5.442   8.703   0.50 12.73 ?  53   LEU   A HA   1 
ATOM   1354 H  HB2  A LEU   A 1 53  ? 23.140 4.505   6.528   0.50 13.59 ?  53   LEU   A HB2  1 
ATOM   1355 H  HB2  B LEU   A 1 53  ? 23.303 4.394   6.496   0.50 12.68 ?  53   LEU   A HB2  1 
ATOM   1356 H  HB3  A LEU   A 1 53  ? 23.541 4.264   8.038   0.50 13.59 ?  53   LEU   A HB3  1 
ATOM   1357 H  HB3  B LEU   A 1 53  ? 23.827 4.192   7.973   0.50 12.68 ?  53   LEU   A HB3  1 
ATOM   1358 H  HG   A LEU   A 1 53  ? 21.119 3.344   6.926   0.50 14.12 ?  53   LEU   A HG   1 
ATOM   1359 H  HG   B LEU   A 1 53  ? 21.399 3.097   7.049   0.50 12.62 ?  53   LEU   A HG   1 
ATOM   1360 H  HD11 A LEU   A 1 53  ? 22.041 1.208   6.930   0.50 13.89 ?  53   LEU   A HD11 1 
ATOM   1361 H  HD11 B LEU   A 1 53  ? 22.505 1.048   6.959   0.50 13.15 ?  53   LEU   A HD11 1 
ATOM   1362 H  HD12 A LEU   A 1 53  ? 22.869 2.167   5.972   0.50 13.89 ?  53   LEU   A HD12 1 
ATOM   1363 H  HD12 B LEU   A 1 53  ? 23.166 2.082   5.950   0.50 13.15 ?  53   LEU   A HD12 1 
ATOM   1364 H  HD13 A LEU   A 1 53  ? 23.429 1.810   7.416   0.50 13.89 ?  53   LEU   A HD13 1 
ATOM   1365 H  HD13 B LEU   A 1 53  ? 23.867 1.773   7.342   0.50 13.15 ?  53   LEU   A HD13 1 
ATOM   1366 H  HD21 A LEU   A 1 53  ? 20.916 2.058   8.882   0.50 15.60 ?  53   LEU   A HD21 1 
ATOM   1367 H  HD21 B LEU   A 1 53  ? 21.387 1.850   9.006   0.50 13.02 ?  53   LEU   A HD21 1 
ATOM   1368 H  HD22 A LEU   A 1 53  ? 22.204 2.781   9.466   0.50 15.60 ?  53   LEU   A HD22 1 
ATOM   1369 H  HD22 B LEU   A 1 53  ? 22.746 2.533   9.464   0.50 13.02 ?  53   LEU   A HD22 1 
ATOM   1370 H  HD23 A LEU   A 1 53  ? 20.877 3.613   9.202   0.50 15.60 ?  53   LEU   A HD23 1 
ATOM   1371 H  HD23 B LEU   A 1 53  ? 21.415 3.393   9.373   0.50 13.02 ?  53   LEU   A HD23 1 
ATOM   1372 N  N    . ASN   A 1 54  ? 23.817 7.311   6.934   1.00 10.30 ?  54   ASN   A N    1 
ATOM   1373 C  CA   . ASN   A 1 54  ? 24.867 8.309   7.063   1.00 10.21 ?  54   ASN   A CA   1 
ATOM   1374 C  C    . ASN   A 1 54  ? 24.358 9.551   7.789   1.00 10.90 ?  54   ASN   A C    1 
ATOM   1375 O  O    . ASN   A 1 54  ? 25.047 10.104  8.656   1.00 11.44 ?  54   ASN   A O    1 
ATOM   1376 C  CB   . ASN   A 1 54  ? 25.429 8.671   5.703   1.00 10.50 ?  54   ASN   A CB   1 
ATOM   1377 C  CG   . ASN   A 1 54  ? 26.437 9.778   5.814   1.00 10.55 ?  54   ASN   A CG   1 
ATOM   1378 O  OD1  . ASN   A 1 54  ? 27.452 9.635   6.508   1.00 10.95 ?  54   ASN   A OD1  1 
ATOM   1379 N  ND2  . ASN   A 1 54  ? 26.167 10.902  5.169   1.00 11.49 ?  54   ASN   A ND2  1 
ATOM   1380 H  H    A ASN   A 1 54  ? 23.614 7.090   6.128   0.50 12.35 ?  54   ASN   A H    1 
ATOM   1381 H  H    B ASN   A 1 54  ? 23.539 7.162   6.133   0.50 12.35 ?  54   ASN   A H    1 
ATOM   1382 H  HA   . ASN   A 1 54  ? 25.583 7.933   7.591   1.00 12.24 ?  54   ASN   A HA   1 
ATOM   1383 H  HB2  . ASN   A 1 54  ? 25.870 7.887   5.323   1.00 12.59 ?  54   ASN   A HB2  1 
ATOM   1384 H  HB3  . ASN   A 1 54  ? 24.712 8.960   5.120   1.00 12.59 ?  54   ASN   A HB3  1 
ATOM   1385 H  HD21 . ASN   A 1 54  ? 26.712 11.562  5.213   1.00 13.79 ?  54   ASN   A HD21 1 
ATOM   1386 H  HD22 . ASN   A 1 54  ? 25.442 10.970  4.708   1.00 13.79 ?  54   ASN   A HD22 1 
ATOM   1387 N  N    . LYS   A 1 55  ? 23.147 10.004  7.449   1.00 11.18 ?  55   LYS   A N    1 
ATOM   1388 C  CA   . LYS   A 1 55  ? 22.564 11.156  8.123   1.00 11.74 ?  55   LYS   A CA   1 
ATOM   1389 C  C    . LYS   A 1 55  ? 22.473 10.915  9.621   1.00 11.98 ?  55   LYS   A C    1 
ATOM   1390 O  O    . LYS   A 1 55  ? 22.757 11.811  10.423  1.00 12.65 ?  55   LYS   A O    1 
ATOM   1391 C  CB   . LYS   A 1 55  ? 21.190 11.452  7.523   1.00 13.16 ?  55   LYS   A CB   1 
ATOM   1392 C  CG   . LYS   A 1 55  ? 20.451 12.622  8.162   1.00 14.59 ?  55   LYS   A CG   1 
ATOM   1393 C  CD   . LYS   A 1 55  ? 19.146 12.898  7.419   1.00 16.04 ?  55   LYS   A CD   1 
ATOM   1394 C  CE   . LYS   A 1 55  ? 18.318 13.978  8.093   1.00 17.83 ?  55   LYS   A CE   1 
ATOM   1395 N  NZ   . LYS   A 1 55  ? 17.013 14.190  7.400   1.00 18.44 ?  55   LYS   A NZ   1 
ATOM   1396 H  H    . LYS   A 1 55  ? 22.638 9.654   6.841   1.00 13.41 ?  55   LYS   A H    1 
ATOM   1397 H  HA   . LYS   A 1 55  ? 23.130 11.929  7.975   1.00 14.09 ?  55   LYS   A HA   1 
ATOM   1398 H  HB2  . LYS   A 1 55  ? 21.299 11.661  6.583   1.00 15.79 ?  55   LYS   A HB2  1 
ATOM   1399 H  HB3  . LYS   A 1 55  ? 20.631 10.667  7.621   1.00 15.79 ?  55   LYS   A HB3  1 
ATOM   1400 H  HG2  . LYS   A 1 55  ? 20.235 12.404  9.085   1.00 17.50 ?  55   LYS   A HG2  1 
ATOM   1401 H  HG3  . LYS   A 1 55  ? 21.003 13.417  8.124   1.00 17.50 ?  55   LYS   A HG3  1 
ATOM   1402 H  HD2  . LYS   A 1 55  ? 19.353 13.194  6.518   1.00 19.24 ?  55   LYS   A HD2  1 
ATOM   1403 H  HD3  . LYS   A 1 55  ? 18.618 12.085  7.389   1.00 19.24 ?  55   LYS   A HD3  1 
ATOM   1404 H  HE2  . LYS   A 1 55  ? 18.133 13.714  9.008   1.00 21.39 ?  55   LYS   A HE2  1 
ATOM   1405 H  HE3  . LYS   A 1 55  ? 18.808 14.814  8.078   1.00 21.39 ?  55   LYS   A HE3  1 
ATOM   1406 H  HZ1  . LYS   A 1 55  ? 16.377 14.370  7.996   1.00 22.13 ?  55   LYS   A HZ1  1 
ATOM   1407 H  HZ2  . LYS   A 1 55  ? 17.076 14.875  6.833   1.00 22.13 ?  55   LYS   A HZ2  1 
ATOM   1408 H  HZ3  . LYS   A 1 55  ? 16.784 13.459  6.947   1.00 22.13 ?  55   LYS   A HZ3  1 
ATOM   1409 N  N    . ALA   A 1 56  ? 22.098 9.699   10.019  1.00 12.30 ?  56   ALA   A N    1 
ATOM   1410 C  CA   . ALA   A 1 56  ? 21.977 9.371   11.432  1.00 13.41 ?  56   ALA   A CA   1 
ATOM   1411 C  C    . ALA   A 1 56  ? 23.319 9.399   12.156  1.00 13.10 ?  56   ALA   A C    1 
ATOM   1412 O  O    . ALA   A 1 56  ? 23.339 9.575   13.377  1.00 14.43 ?  56   ALA   A O    1 
ATOM   1413 C  CB   . ALA   A 1 56  ? 21.282 8.014   11.600  1.00 14.19 ?  56   ALA   A CB   1 
ATOM   1414 H  H    . ALA   A 1 56  ? 21.911 9.054   9.486   1.00 14.75 ?  56   ALA   A H    1 
ATOM   1415 H  HA   . ALA   A 1 56  ? 21.417 10.032  11.853  1.00 16.09 ?  56   ALA   A HA   1 
ATOM   1416 H  HB1  . ALA   A 1 56  ? 21.208 7.809   12.546  1.00 17.02 ?  56   ALA   A HB1  1 
ATOM   1417 H  HB2  . ALA   A 1 56  ? 20.394 8.068   11.207  1.00 17.02 ?  56   ALA   A HB2  1 
ATOM   1418 H  HB3  . ALA   A 1 56  ? 21.798 7.328   11.151  1.00 17.02 ?  56   ALA   A HB3  1 
ATOM   1419 N  N    . THR   A 1 57  ? 24.434 9.235   11.436  1.00 12.03 ?  57   THR   A N    1 
ATOM   1420 C  CA   . THR   A 1 57  ? 25.771 9.365   12.012  1.00 12.45 ?  57   THR   A CA   1 
ATOM   1421 C  C    . THR   A 1 57  ? 26.313 10.783  11.934  1.00 12.61 ?  57   THR   A C    1 
ATOM   1422 O  O    . THR   A 1 57  ? 27.496 10.999  12.222  1.00 13.04 ?  57   THR   A O    1 
ATOM   1423 C  CB   . THR   A 1 57  ? 26.783 8.419   11.337  1.00 11.87 ?  57   THR   A CB   1 
ATOM   1424 O  OG1  . THR   A 1 57  ? 27.160 8.915   10.040  1.00 11.41 ?  57   THR   A OG1  1 
ATOM   1425 C  CG2  . THR   A 1 57  ? 26.255 6.998   11.234  1.00 11.93 ?  57   THR   A CG2  1 
ATOM   1426 H  H    . THR   A 1 57  ? 24.441 9.036   10.595  1.00 14.43 ?  57   THR   A H    1 
ATOM   1427 H  HA   . THR   A 1 57  ? 25.724 9.108   12.951  1.00 14.94 ?  57   THR   A HA   1 
ATOM   1428 H  HB   . THR   A 1 57  ? 27.582 8.379   11.899  1.00 14.24 ?  57   THR   A HB   1 
ATOM   1429 H  HG1  . THR   A 1 57  ? 26.482 8.977   9.559   1.00 13.69 ?  57   THR   A HG1  1 
ATOM   1430 H  HG21 . THR   A 1 57  ? 26.915 6.421   10.812  1.00 14.32 ?  57   THR   A HG21 1 
ATOM   1431 H  HG22 . THR   A 1 57  ? 26.051 6.643   12.115  1.00 14.32 ?  57   THR   A HG22 1 
ATOM   1432 H  HG23 . THR   A 1 57  ? 25.445 6.979   10.699  1.00 14.32 ?  57   THR   A HG23 1 
ATOM   1433 N  N    . ASN   A 1 58  ? 25.494 11.749  11.532  1.00 13.25 ?  58   ASN   A N    1 
ATOM   1434 C  CA   . ASN   A 1 58  ? 25.944 13.134  11.434  1.00 14.16 ?  58   ASN   A CA   1 
ATOM   1435 C  C    . ASN   A 1 58  ? 27.088 13.268  10.428  1.00 12.71 ?  58   ASN   A C    1 
ATOM   1436 O  O    . ASN   A 1 58  ? 27.984 14.098  10.596  1.00 13.49 ?  58   ASN   A O    1 
ATOM   1437 C  CB   . ASN   A 1 58  ? 26.318 13.682  12.824  1.00 16.63 ?  58   ASN   A CB   1 
ATOM   1438 C  CG   . ASN   A 1 58  ? 26.707 15.144  12.808  1.00 20.61 ?  58   ASN   A CG   1 
ATOM   1439 O  OD1  . ASN   A 1 58  ? 26.074 15.952  12.137  1.00 22.34 ?  58   ASN   A OD1  1 
ATOM   1440 N  ND2  . ASN   A 1 58  ? 27.752 15.496  13.561  1.00 22.10 ?  58   ASN   A ND2  1 
ATOM   1441 H  H    . ASN   A 1 58  ? 24.674 11.621  11.304  1.00 15.89 ?  58   ASN   A H    1 
ATOM   1442 H  HA   . ASN   A 1 58  ? 25.203 13.660  11.104  1.00 16.98 ?  58   ASN   A HA   1 
ATOM   1443 H  HB2  . ASN   A 1 58  ? 25.549 13.581  13.417  1.00 19.95 ?  58   ASN   A HB2  1 
ATOM   1444 H  HB3  . ASN   A 1 58  ? 27.067 13.182  13.174  1.00 19.95 ?  58   ASN   A HB3  1 
ATOM   1445 H  HD21 . ASN   A 1 58  ? 28.004 16.320  13.589  1.00 26.52 ?  58   ASN   A HD21 1 
ATOM   1446 H  HD22 . ASN   A 1 58  ? 28.161 14.903  14.022  1.00 26.52 ?  58   ASN   A HD22 1 
ATOM   1447 N  N    . ASN   A 1 59  ? 27.072 12.450  9.374   1.00 11.57 ?  59   ASN   A N    1 
ATOM   1448 C  CA   . ASN   A 1 59  ? 28.054 12.434  8.284   1.00 11.57 ?  59   ASN   A CA   1 
ATOM   1449 C  C    . ASN   A 1 59  ? 29.373 11.758  8.681   1.00 11.11 ?  59   ASN   A C    1 
ATOM   1450 O  O    . ASN   A 1 59  ? 30.292 11.721  7.854   1.00 11.30 ?  59   ASN   A O    1 
ATOM   1451 C  CB   . ASN   A 1 59  ? 28.339 13.819  7.674   1.00 11.51 ?  59   ASN   A CB   1 
ATOM   1452 C  CG   . ASN   A 1 59  ? 28.690 13.748  6.203   1.00 11.98 ?  59   ASN   A CG   1 
ATOM   1453 O  OD1  . ASN   A 1 59  ? 27.980 13.126  5.414   1.00 12.12 ?  59   ASN   A OD1  1 
ATOM   1454 N  ND2  . ASN   A 1 59  ? 29.776 14.409  5.819   1.00 12.44 ?  59   ASN   A ND2  1 
ATOM   1455 H  H    . ASN   A 1 59  ? 26.463 11.854  9.258   1.00 13.87 ?  59   ASN   A H    1 
ATOM   1456 H  HA   . ASN   A 1 59  ? 27.682 11.900  7.570   1.00 13.88 ?  59   ASN   A HA   1 
ATOM   1457 H  HB2  . ASN   A 1 59  ? 27.555 14.379  7.761   1.00 13.81 ?  59   ASN   A HB2  1 
ATOM   1458 H  HB3  . ASN   A 1 59  ? 29.092 14.226  8.135   1.00 13.81 ?  59   ASN   A HB3  1 
ATOM   1459 H  HD21 . ASN   A 1 59  ? 30.020 14.404  4.992   1.00 14.92 ?  59   ASN   A HD21 1 
ATOM   1460 H  HD22 . ASN   A 1 59  ? 30.253 14.838  6.398   1.00 14.92 ?  59   ASN   A HD22 1 
ATOM   1461 N  N    . ALA   A 1 60  ? 29.497 11.207  9.890   1.00 10.94 ?  60   ALA   A N    1 
ATOM   1462 C  CA   . ALA   A 1 60  ? 30.742 10.530  10.242  1.00 11.25 ?  60   ALA   A CA   1 
ATOM   1463 C  C    . ALA   A 1 60  ? 30.974 9.300   9.366   1.00 11.28 ?  60   ALA   A C    1 
ATOM   1464 O  O    . ALA   A 1 60  ? 32.116 8.983   9.021   1.00 11.66 ?  60   ALA   A O    1 
ATOM   1465 C  CB   . ALA   A 1 60  ? 30.738 10.160  11.722  1.00 11.82 ?  60   ALA   A CB   1 
ATOM   1466 H  H    . ALA   A 1 60  ? 28.893 11.207  10.502  1.00 13.12 ?  60   ALA   A H    1 
ATOM   1467 H  HA   . ALA   A 1 60  ? 31.481 11.144  10.092  1.00 13.49 ?  60   ALA   A HA   1 
ATOM   1468 H  HB1  . ALA   A 1 60  ? 31.569 9.716   11.941  1.00 14.18 ?  60   ALA   A HB1  1 
ATOM   1469 H  HB2  . ALA   A 1 60  ? 30.645 10.971  12.252  1.00 14.18 ?  60   ALA   A HB2  1 
ATOM   1470 H  HB3  . ALA   A 1 60  ? 29.987 9.569   11.897  1.00 14.18 ?  60   ALA   A HB3  1 
ATOM   1471 N  N    . MET   A 1 61  ? 29.902 8.593   8.997   1.00 10.89 ?  61   MET   A N    1 
ATOM   1472 C  CA   . MET   A 1 61  ? 30.042 7.459   8.087   1.00 10.72 ?  61   MET   A CA   1 
ATOM   1473 C  C    . MET   A 1 61  ? 30.665 7.892   6.761   1.00 10.40 ?  61   MET   A C    1 
ATOM   1474 O  O    . MET   A 1 61  ? 31.560 7.220   6.238   1.00 10.78 ?  61   MET   A O    1 
ATOM   1475 C  CB   . MET   A 1 61  ? 28.680 6.792   7.879   1.00 10.77 ?  61   MET   A CB   1 
ATOM   1476 C  CG   . MET   A 1 61  ? 28.696 5.631   6.896   1.00 11.29 ?  61   MET   A CG   1 
ATOM   1477 S  SD   . MET   A 1 61  ? 27.077 4.883   6.685   1.00 12.03 ?  61   MET   A SD   1 
ATOM   1478 C  CE   . MET   A 1 61  ? 26.951 3.994   8.241   1.00 13.66 ?  61   MET   A CE   1 
ATOM   1479 H  H    . MET   A 1 61  ? 29.095 8.749   9.256   1.00 13.06 ?  61   MET   A H    1 
ATOM   1480 H  HA   . MET   A 1 61  ? 30.627 6.807   8.501   1.00 12.85 ?  61   MET   A HA   1 
ATOM   1481 H  HB2  . MET   A 1 61  ? 28.371 6.452   8.733   1.00 12.92 ?  61   MET   A HB2  1 
ATOM   1482 H  HB3  . MET   A 1 61  ? 28.058 7.455   7.546   1.00 12.92 ?  61   MET   A HB3  1 
ATOM   1483 H  HG2  . MET   A 1 61  ? 28.985 5.946   6.026   1.00 13.54 ?  61   MET   A HG2  1 
ATOM   1484 H  HG3  . MET   A 1 61  ? 29.298 4.943   7.219   1.00 13.54 ?  61   MET   A HG3  1 
ATOM   1485 H  HE1  . MET   A 1 61  ? 26.114 3.500   8.256   1.00 16.39 ?  61   MET   A HE1  1 
ATOM   1486 H  HE2  . MET   A 1 61  ? 27.698 3.382   8.314   1.00 16.39 ?  61   MET   A HE2  1 
ATOM   1487 H  HE3  . MET   A 1 61  ? 26.970 4.630   8.974   1.00 16.39 ?  61   MET   A HE3  1 
ATOM   1488 N  N    . GLN   A 1 62  ? 30.216 9.020   6.206   1.00 10.34 ?  62   GLN   A N    1 
ATOM   1489 C  CA   . GLN   A 1 62  ? 30.773 9.495   4.942   1.00 10.77 ?  62   GLN   A CA   1 
ATOM   1490 C  C    . GLN   A 1 62  ? 32.242 9.876   5.082   1.00 10.64 ?  62   GLN   A C    1 
ATOM   1491 O  O    . GLN   A 1 62  ? 33.047 9.571   4.199   1.00 11.31 ?  62   GLN   A O    1 
ATOM   1492 C  CB   . GLN   A 1 62  ? 29.970 10.685  4.416   1.00 10.75 ?  62   GLN   A CB   1 
ATOM   1493 C  CG   . GLN   A 1 62  ? 30.335 11.052  2.986   1.00 10.51 ?  62   GLN   A CG   1 
ATOM   1494 C  CD   . GLN   A 1 62  ? 30.011 9.918   2.042   1.00 11.06 ?  62   GLN   A CD   1 
ATOM   1495 O  OE1  . GLN   A 1 62  ? 28.834 9.607   1.836   1.00 11.80 ?  62   GLN   A OE1  1 
ATOM   1496 N  NE2  . GLN   A 1 62  ? 31.035 9.250   1.511   1.00 11.52 ?  62   GLN   A NE2  1 
ATOM   1497 H  H    . GLN   A 1 62  ? 29.598 9.517   6.537   1.00 12.40 ?  62   GLN   A H    1 
ATOM   1498 H  HA   . GLN   A 1 62  ? 30.716 8.780   4.290   1.00 12.92 ?  62   GLN   A HA   1 
ATOM   1499 H  HB2  . GLN   A 1 62  ? 29.026 10.471  4.440   1.00 12.89 ?  62   GLN   A HB2  1 
ATOM   1500 H  HB3  . GLN   A 1 62  ? 30.149 11.461  4.974   1.00 12.89 ?  62   GLN   A HB3  1 
ATOM   1501 H  HG2  . GLN   A 1 62  ? 29.819 11.826  2.713   1.00 12.60 ?  62   GLN   A HG2  1 
ATOM   1502 H  HG3  . GLN   A 1 62  ? 31.282 11.237  2.929   1.00 12.60 ?  62   GLN   A HG3  1 
ATOM   1503 H  HE21 . GLN   A 1 62  ? 31.845 9.485   1.696   1.00 13.82 ?  62   GLN   A HE21 1 
ATOM   1504 H  HE22 . GLN   A 1 62  ? 30.896 8.587   0.982   1.00 13.82 ?  62   GLN   A HE22 1 
ATOM   1505 N  N    . VAL   A 1 63  ? 32.602 10.566  6.167   1.00 11.41 ?  63   VAL   A N    1 
ATOM   1506 C  CA   . VAL   A 1 63  ? 33.993 10.965  6.379   1.00 11.99 ?  63   VAL   A CA   1 
ATOM   1507 C  C    . VAL   A 1 63  ? 34.892 9.733   6.436   1.00 11.43 ?  63   VAL   A C    1 
ATOM   1508 O  O    . VAL   A 1 63  ? 35.942 9.667   5.779   1.00 11.78 ?  63   VAL   A O    1 
ATOM   1509 C  CB   . VAL   A 1 63  ? 34.104 11.831  7.647   1.00 13.81 ?  63   VAL   A CB   1 
ATOM   1510 C  CG1  . VAL   A 1 63  ? 35.551 12.071  8.016   1.00 15.59 ?  63   VAL   A CG1  1 
ATOM   1511 C  CG2  . VAL   A 1 63  ? 33.370 13.163  7.446   1.00 14.16 ?  63   VAL   A CG2  1 
ATOM   1512 H  H    . VAL   A 1 63  ? 32.058 10.814  6.788   1.00 13.68 ?  63   VAL   A H    1 
ATOM   1513 H  HA   . VAL   A 1 63  ? 34.276 11.507  5.627   1.00 14.38 ?  63   VAL   A HA   1 
ATOM   1514 H  HB   . VAL   A 1 63  ? 33.677 11.367  8.386   1.00 16.56 ?  63   VAL   A HB   1 
ATOM   1515 H  HG11 . VAL   A 1 63  ? 35.592 12.803  8.650   1.00 18.70 ?  63   VAL   A HG11 1 
ATOM   1516 H  HG12 . VAL   A 1 63  ? 35.910 11.265  8.414   1.00 18.70 ?  63   VAL   A HG12 1 
ATOM   1517 H  HG13 . VAL   A 1 63  ? 36.041 12.299  7.213   1.00 18.70 ?  63   VAL   A HG13 1 
ATOM   1518 H  HG21 . VAL   A 1 63  ? 33.459 13.698  8.255   1.00 16.98 ?  63   VAL   A HG21 1 
ATOM   1519 H  HG22 . VAL   A 1 63  ? 33.765 13.633  6.697   1.00 16.98 ?  63   VAL   A HG22 1 
ATOM   1520 H  HG23 . VAL   A 1 63  ? 32.432 12.988  7.272   1.00 16.98 ?  63   VAL   A HG23 1 
ATOM   1521 N  N    . GLU   A 1 64  ? 34.480 8.728   7.211   1.00 11.56 ?  64   GLU   A N    1 
ATOM   1522 C  CA   . GLU   A 1 64  ? 35.253 7.494   7.304   1.00 11.40 ?  64   GLU   A CA   1 
ATOM   1523 C  C    . GLU   A 1 64  ? 35.342 6.808   5.948   1.00 11.09 ?  64   GLU   A C    1 
ATOM   1524 O  O    . GLU   A 1 64  ? 36.390 6.259   5.571   1.00 11.48 ?  64   GLU   A O    1 
ATOM   1525 C  CB   . GLU   A 1 64  ? 34.570 6.579   8.319   1.00 11.97 ?  64   GLU   A CB   1 
ATOM   1526 C  CG   . GLU   A 1 64  ? 35.222 5.229   8.460   1.00 12.22 ?  64   GLU   A CG   1 
ATOM   1527 C  CD   . GLU   A 1 64  ? 34.346 4.227   9.183   1.00 12.89 ?  64   GLU   A CD   1 
ATOM   1528 O  OE1  . GLU   A 1 64  ? 33.104 4.310   9.058   1.00 13.78 ?  64   GLU   A OE1  1 
ATOM   1529 O  OE2  . GLU   A 1 64  ? 34.905 3.332   9.861   1.00 13.30 -1 64   GLU   A OE2  1 
ATOM   1530 H  H    . GLU   A 1 64  ? 33.751 8.730   7.671   1.00 13.87 ?  64   GLU   A H    1 
ATOM   1531 H  HA   . GLU   A 1 64  ? 36.148 7.703   7.616   1.00 13.67 ?  64   GLU   A HA   1 
ATOM   1532 H  HB2  . GLU   A 1 64  ? 34.598 7.017   9.193   1.00 14.36 ?  64   GLU   A HB2  1 
ATOM   1533 H  HB3  . GLU   A 1 64  ? 33.651 6.452   8.051   1.00 14.36 ?  64   GLU   A HB3  1 
ATOM   1534 H  HG2  . GLU   A 1 64  ? 35.421 4.871   7.579   1.00 14.65 ?  64   GLU   A HG2  1 
ATOM   1535 H  HG3  . GLU   A 1 64  ? 36.044 5.331   8.964   1.00 14.65 ?  64   GLU   A HG3  1 
ATOM   1536 N  N    . SER   A 1 65  ? 34.220 6.793   5.222   1.00 10.90 ?  65   SER   A N    1 
ATOM   1537 C  CA   . SER   A 1 65  ? 34.167 6.140   3.923   1.00 10.65 ?  65   SER   A CA   1 
ATOM   1538 C  C    . SER   A 1 65  ? 35.083 6.813   2.912   1.00 10.97 ?  65   SER   A C    1 
ATOM   1539 O  O    . SER   A 1 65  ? 35.717 6.136   2.096   1.00 11.70 ?  65   SER   A O    1 
ATOM   1540 C  CB   . SER   A 1 65  ? 32.730 6.150   3.399   1.00 10.82 ?  65   SER   A CB   1 
ATOM   1541 O  OG   . SER   A 1 65  ? 31.879 5.321   4.184   1.00 11.39 ?  65   SER   A OG   1 
ATOM   1542 H  H    . SER   A 1 65  ? 33.484 7.164   5.463   1.00 13.07 ?  65   SER   A H    1 
ATOM   1543 H  HA   . SER   A 1 65  ? 34.451 5.219   4.018   1.00 12.78 ?  65   SER   A HA   1 
ATOM   1544 H  HB2  . SER   A 1 65  ? 32.393 7.058   3.424   1.00 12.98 ?  65   SER   A HB2  1 
ATOM   1545 H  HB3  . SER   A 1 65  ? 32.732 5.824   2.485   1.00 12.98 ?  65   SER   A HB3  1 
ATOM   1546 H  HG   . SER   A 1 65  ? 31.877 5.592   4.983   1.00 13.66 ?  65   SER   A HG   1 
ATOM   1547 N  N    . ASP   A 1 66  ? 35.146 8.145   2.928   1.00 11.28 ?  66   ASP   A N    1 
ATOM   1548 C  CA   . ASP   A 1 66  ? 35.997 8.837   1.970   1.00 12.13 ?  66   ASP   A CA   1 
ATOM   1549 C  C    . ASP   A 1 66  ? 37.462 8.488   2.204   1.00 12.09 ?  66   ASP   A C    1 
ATOM   1550 O  O    . ASP   A 1 66  ? 38.231 8.314   1.250   1.00 13.30 ?  66   ASP   A O    1 
ATOM   1551 C  CB   . ASP   A 1 66  ? 35.777 10.343  2.063   1.00 13.46 ?  66   ASP   A CB   1 
ATOM   1552 C  CG   . ASP   A 1 66  ? 34.436 10.797  1.471   1.00 14.75 ?  66   ASP   A CG   1 
ATOM   1553 O  OD1  . ASP   A 1 66  ? 33.723 9.997   0.820   1.00 15.24 ?  66   ASP   A OD1  1 
ATOM   1554 O  OD2  . ASP   A 1 66  ? 34.129 11.996  1.644   1.00 18.00 -1 66   ASP   A OD2  1 
ATOM   1555 H  H    . ASP   A 1 66  ? 34.709 8.660   3.467   1.00 13.53 ?  66   ASP   A H    1 
ATOM   1556 H  HA   . ASP   A 1 66  ? 35.756 8.553   1.073   1.00 14.55 ?  66   ASP   A HA   1 
ATOM   1557 H  HB2  . ASP   A 1 66  ? 35.790 10.606  2.996   1.00 16.15 ?  66   ASP   A HB2  1 
ATOM   1558 H  HB3  . ASP   A 1 66  ? 36.487 10.794  1.581   1.00 16.15 ?  66   ASP   A HB3  1 
ATOM   1559 N  N    . ASP   A 1 67  ? 37.865 8.361   3.468   1.00 12.20 ?  67   ASP   A N    1 
ATOM   1560 C  CA   . ASP   A 1 67  ? 39.224 7.921   3.763   1.00 12.81 ?  67   ASP   A CA   1 
ATOM   1561 C  C    . ASP   A 1 67  ? 39.447 6.488   3.295   1.00 12.60 ?  67   ASP   A C    1 
ATOM   1562 O  O    . ASP   A 1 67  ? 40.509 6.167   2.747   1.00 13.48 ?  67   ASP   A O    1 
ATOM   1563 C  CB   . ASP   A 1 67  ? 39.492 8.048   5.260   1.00 14.11 ?  67   ASP   A CB   1 
ATOM   1564 C  CG   . ASP   A 1 67  ? 40.791 7.389   5.677   1.00 15.41 ?  67   ASP   A CG   1 
ATOM   1565 O  OD1  . ASP   A 1 67  ? 41.864 8.022   5.535   1.00 18.20 ?  67   ASP   A OD1  1 
ATOM   1566 O  OD2  . ASP   A 1 67  ? 40.735 6.225   6.138   1.00 14.99 -1 67   ASP   A OD2  1 
ATOM   1567 H  H    . ASP   A 1 67  ? 37.384 8.530   4.154   1.00 14.64 ?  67   ASP   A H    1 
ATOM   1568 H  HA   . ASP   A 1 67  ? 39.853 8.489   3.292   1.00 15.37 ?  67   ASP   A HA   1 
ATOM   1569 H  HB2  . ASP   A 1 67  ? 39.539 8.986   5.487   1.00 16.92 ?  67   ASP   A HB2  1 
ATOM   1570 H  HB3  . ASP   A 1 67  ? 38.763 7.622   5.743   1.00 16.92 ?  67   ASP   A HB3  1 
ATOM   1571 N  N    . TYR   A 1 68  ? 38.455 5.610   3.493   1.00 12.20 ?  68   TYR   A N    1 
ATOM   1572 C  CA   . TYR   A 1 68  ? 38.578 4.231   3.020   1.00 12.63 ?  68   TYR   A CA   1 
ATOM   1573 C  C    . TYR   A 1 68  ? 38.814 4.184   1.513   1.00 12.55 ?  68   TYR   A C    1 
ATOM   1574 O  O    . TYR   A 1 68  ? 39.691 3.453   1.033   1.00 12.96 ?  68   TYR   A O    1 
ATOM   1575 C  CB   . TYR   A 1 68  ? 37.334 3.405   3.405   1.00 13.17 ?  68   TYR   A CB   1 
ATOM   1576 C  CG   . TYR   A 1 68  ? 37.364 2.020   2.776   1.00 14.66 ?  68   TYR   A CG   1 
ATOM   1577 C  CD1  . TYR   A 1 68  ? 36.908 1.829   1.476   1.00 16.13 ?  68   TYR   A CD1  1 
ATOM   1578 C  CD2  . TYR   A 1 68  ? 37.917 0.936   3.438   1.00 16.58 ?  68   TYR   A CD2  1 
ATOM   1579 C  CE1  . TYR   A 1 68  ? 36.980 0.616   0.857   1.00 17.75 ?  68   TYR   A CE1  1 
ATOM   1580 C  CE2  . TYR   A 1 68  ? 37.974 -0.324  2.819   1.00 16.93 ?  68   TYR   A CE2  1 
ATOM   1581 C  CZ   . TYR   A 1 68  ? 37.522 -0.451  1.525   1.00 17.63 ?  68   TYR   A CZ   1 
ATOM   1582 O  OH   . TYR   A 1 68  ? 37.605 -1.653  0.883   1.00 18.92 ?  68   TYR   A OH   1 
ATOM   1583 H  H    . TYR   A 1 68  ? 37.711 5.782   3.898   1.00 14.63 ?  68   TYR   A H    1 
ATOM   1584 H  HA   . TYR   A 1 68  ? 39.340 3.819   3.450   1.00 15.15 ?  68   TYR   A HA   1 
ATOM   1585 H  HB2  . TYR   A 1 68  ? 37.304 3.295   4.370   1.00 15.80 ?  68   TYR   A HB2  1 
ATOM   1586 H  HB3  . TYR   A 1 68  ? 36.533 3.860   3.096   1.00 15.80 ?  68   TYR   A HB3  1 
ATOM   1587 H  HD1  . TYR   A 1 68  ? 36.556 2.558   1.012   1.00 19.35 ?  68   TYR   A HD1  1 
ATOM   1588 H  HD2  . TYR   A 1 68  ? 38.245 1.035   4.299   1.00 19.89 ?  68   TYR   A HD2  1 
ATOM   1589 H  HE1  . TYR   A 1 68  ? 36.665 0.520   -0.011  1.00 21.29 ?  68   TYR   A HE1  1 
ATOM   1590 H  HE2  . TYR   A 1 68  ? 38.356 -1.054  3.251   1.00 20.31 ?  68   TYR   A HE2  1 
ATOM   1591 H  HH   . TYR   A 1 68  ? 37.944 -2.228  1.391   1.00 22.70 ?  68   TYR   A HH   1 
ATOM   1592 N  N    . ILE   A 1 69  ? 38.029 4.948   0.744   1.00 11.98 ?  69   ILE   A N    1 
ATOM   1593 C  CA   . ILE   A 1 69  ? 38.157 4.925   -0.712  1.00 12.28 ?  69   ILE   A CA   1 
ATOM   1594 C  C    . ILE   A 1 69  ? 39.479 5.540   -1.147  1.00 11.99 ?  69   ILE   A C    1 
ATOM   1595 O  O    . ILE   A 1 69  ? 40.122 5.060   -2.087  1.00 12.33 ?  69   ILE   A O    1 
ATOM   1596 C  CB   . ILE   A 1 69  ? 36.952 5.628   -1.369  1.00 13.21 ?  69   ILE   A CB   1 
ATOM   1597 C  CG1  . ILE   A 1 69  ? 35.642 4.883   -1.084  1.00 13.76 ?  69   ILE   A CG1  1 
ATOM   1598 C  CG2  . ILE   A 1 69  ? 37.184 5.826   -2.873  1.00 14.65 ?  69   ILE   A CG2  1 
ATOM   1599 C  CD1  . ILE   A 1 69  ? 35.471 3.597   -1.861  1.00 14.59 ?  69   ILE   A CD1  1 
ATOM   1600 H  H    . ILE   A 1 69  ? 37.429 5.488   1.041   1.00 14.37 ?  69   ILE   A H    1 
ATOM   1601 H  HA   . ILE   A 1 69  ? 38.156 4.001   -1.005  1.00 14.73 ?  69   ILE   A HA   1 
ATOM   1602 H  HB   . ILE   A 1 69  ? 36.875 6.504   -0.973  1.00 15.84 ?  69   ILE   A HB   1 
ATOM   1603 H  HG12 . ILE   A 1 69  ? 35.612 4.659   -0.138  1.00 16.51 ?  69   ILE   A HG12 1 
ATOM   1604 H  HG13 . ILE   A 1 69  ? 34.898 5.462   -1.305  1.00 16.51 ?  69   ILE   A HG13 1 
ATOM   1605 H  HG21 . ILE   A 1 69  ? 36.335 6.027   -3.301  1.00 17.57 ?  69   ILE   A HG21 1 
ATOM   1606 H  HG22 . ILE   A 1 69  ? 37.797 6.571   -3.005  1.00 17.57 ?  69   ILE   A HG22 1 
ATOM   1607 H  HG23 . ILE   A 1 69  ? 37.559 5.018   -3.251  1.00 17.57 ?  69   ILE   A HG23 1 
ATOM   1608 H  HD11 . ILE   A 1 69  ? 34.675 3.141   -1.540  1.00 17.50 ?  69   ILE   A HD11 1 
ATOM   1609 H  HD12 . ILE   A 1 69  ? 35.372 3.807   -2.802  1.00 17.50 ?  69   ILE   A HD12 1 
ATOM   1610 H  HD13 . ILE   A 1 69  ? 36.248 3.036   -1.724  1.00 17.50 ?  69   ILE   A HD13 1 
ATOM   1611 N  N    . ALA   A 1 70  ? 39.891 6.620   -0.491  1.00 12.34 ?  70   ALA   A N    1 
ATOM   1612 C  CA   . ALA   A 1 70  ? 41.160 7.238   -0.853  1.00 13.18 ?  70   ALA   A CA   1 
ATOM   1613 C  C    . ALA   A 1 70  ? 42.316 6.258   -0.692  1.00 13.48 ?  70   ALA   A C    1 
ATOM   1614 O  O    . ALA   A 1 70  ? 43.276 6.291   -1.465  1.00 15.53 ?  70   ALA   A O    1 
ATOM   1615 C  CB   . ALA   A 1 70  ? 41.389 8.489   -0.008  1.00 13.80 ?  70   ALA   A CB   1 
ATOM   1616 H  H    . ALA   A 1 70  ? 39.461 7.013   0.139   1.00 14.80 ?  70   ALA   A H    1 
ATOM   1617 H  HA   . ALA   A 1 70  ? 41.127 7.517   -1.784  1.00 15.81 ?  70   ALA   A HA   1 
ATOM   1618 H  HB1  . ALA   A 1 70  ? 42.243 8.888   -0.258  1.00 16.55 ?  70   ALA   A HB1  1 
ATOM   1619 H  HB2  . ALA   A 1 70  ? 40.674 9.121   -0.167  1.00 16.55 ?  70   ALA   A HB2  1 
ATOM   1620 H  HB3  . ALA   A 1 70  ? 41.411 8.238   0.929   1.00 16.55 ?  70   ALA   A HB3  1 
ATOM   1621 N  N    . THR   A 1 71  ? 42.226 5.361   0.285   1.00 13.00 ?  71   THR   A N    1 
ATOM   1622 C  CA   . THR   A 1 71  ? 43.283 4.387   0.533   1.00 14.61 ?  71   THR   A CA   1 
ATOM   1623 C  C    . THR   A 1 71  ? 43.169 3.163   -0.366  1.00 14.78 ?  71   THR   A C    1 
ATOM   1624 O  O    . THR   A 1 71  ? 44.183 2.660   -0.868  1.00 16.90 ?  71   THR   A O    1 
ATOM   1625 C  CB   . THR   A 1 71  ? 43.221 3.943   1.992   1.00 16.21 ?  71   THR   A CB   1 
ATOM   1626 O  OG1  . THR   A 1 71  ? 43.467 5.074   2.835   1.00 17.70 ?  71   THR   A OG1  1 
ATOM   1627 C  CG2  . THR   A 1 71  ? 44.240 2.838   2.283   1.00 17.91 ?  71   THR   A CG2  1 
ATOM   1628 H  H    . THR   A 1 71  ? 41.553 5.284   0.811   1.00 15.59 ?  71   THR   A H    1 
ATOM   1629 H  HA   . THR   A 1 71  ? 44.145 4.795   0.372   1.00 17.53 ?  71   THR   A HA   1 
ATOM   1630 H  HB   . THR   A 1 71  ? 42.337 3.584   2.178   1.00 19.44 ?  71   THR   A HB   1 
ATOM   1631 H  HG1  . THR   A 1 71  ? 43.434 4.833   3.641   1.00 21.24 ?  71   THR   A HG1  1 
ATOM   1632 H  HG21 . THR   A 1 71  ? 44.372 2.758   3.241   1.00 21.49 ?  71   THR   A HG21 1 
ATOM   1633 H  HG22 . THR   A 1 71  ? 43.929 1.989   1.936   1.00 21.49 ?  71   THR   A HG22 1 
ATOM   1634 H  HG23 . THR   A 1 71  ? 45.091 3.058   1.869   1.00 21.49 ?  71   THR   A HG23 1 
ATOM   1635 N  N    . ASN   A 1 72  ? 41.948 2.657   -0.560  1.00 13.75 ?  72   ASN   A N    1 
ATOM   1636 C  CA   . ASN   A 1 72  ? 41.729 1.329   -1.118  1.00 14.03 ?  72   ASN   A CA   1 
ATOM   1637 C  C    . ASN   A 1 72  ? 41.101 1.319   -2.498  1.00 14.01 ?  72   ASN   A C    1 
ATOM   1638 O  O    . ASN   A 1 72  ? 41.107 0.265   -3.147  1.00 15.18 ?  72   ASN   A O    1 
ATOM   1639 C  CB   . ASN   A 1 72  ? 40.839 0.509   -0.176  1.00 14.83 ?  72   ASN   A CB   1 
ATOM   1640 C  CG   . ASN   A 1 72  ? 41.461 0.346   1.189   1.00 15.82 ?  72   ASN   A CG   1 
ATOM   1641 O  OD1  . ASN   A 1 72  ? 41.014 0.944   2.166   1.00 17.66 ?  72   ASN   A OD1  1 
ATOM   1642 N  ND2  . ASN   A 1 72  ? 42.518 -0.433  1.257   1.00 16.40 ?  72   ASN   A ND2  1 
ATOM   1643 H  H    . ASN   A 1 72  ? 41.214 3.077   -0.377  1.00 16.49 ?  72   ASN   A H    1 
ATOM   1644 H  HA   . ASN   A 1 72  ? 42.583 0.880   -1.187  1.00 16.83 ?  72   ASN   A HA   1 
ATOM   1645 H  HB2  . ASN   A 1 72  ? 39.988 0.957   -0.072  1.00 17.80 ?  72   ASN   A HB2  1 
ATOM   1646 H  HB3  . ASN   A 1 72  ? 40.712 -0.375  -0.553  1.00 17.80 ?  72   ASN   A HB3  1 
ATOM   1647 H  HD21 . ASN   A 1 72  ? 42.916 -0.545  2.012   1.00 19.68 ?  72   ASN   A HD21 1 
ATOM   1648 H  HD22 . ASN   A 1 72  ? 42.815 -0.818  0.551   1.00 19.68 ?  72   ASN   A HD22 1 
ATOM   1649 N  N    . GLY   A 1 73  ? 40.554 2.435   -2.958  1.00 13.72 ?  73   GLY   A N    1 
ATOM   1650 C  CA   . GLY   A 1 73  ? 39.821 2.458   -4.198  1.00 13.25 ?  73   GLY   A CA   1 
ATOM   1651 C  C    . GLY   A 1 73  ? 38.432 1.876   -4.027  1.00 12.71 ?  73   GLY   A C    1 
ATOM   1652 O  O    . GLY   A 1 73  ? 38.055 1.413   -2.945  1.00 13.47 ?  73   GLY   A O    1 
ATOM   1653 H  H    . GLY   A 1 73  ? 40.594 3.203   -2.567  1.00 16.46 ?  73   GLY   A H    1 
ATOM   1654 H  HA2  . GLY   A 1 73  ? 39.739 3.376   -4.511  1.00 15.90 ?  73   GLY   A HA2  1 
ATOM   1655 H  HA3  . GLY   A 1 73  ? 40.296 1.945   -4.870  1.00 15.90 ?  73   GLY   A HA3  1 
ATOM   1656 N  N    . PRO   A 1 74  ? 37.647 1.885   -5.103  1.00 13.30 ?  74   PRO   A N    1 
ATOM   1657 C  CA   . PRO   A 1 74  ? 36.252 1.448   -5.013  1.00 13.33 ?  74   PRO   A CA   1 
ATOM   1658 C  C    . PRO   A 1 74  ? 36.111 -0.036  -4.706  1.00 12.84 ?  74   PRO   A C    1 
ATOM   1659 O  O    . PRO   A 1 74  ? 36.980 -0.864  -5.004  1.00 13.70 ?  74   PRO   A O    1 
ATOM   1660 C  CB   . PRO   A 1 74  ? 35.691 1.761   -6.406  1.00 15.22 ?  74   PRO   A CB   1 
ATOM   1661 C  CG   . PRO   A 1 74  ? 36.630 2.756   -7.003  1.00 17.79 ?  74   PRO   A CG   1 
ATOM   1662 C  CD   . PRO   A 1 74  ? 37.975 2.404   -6.440  1.00 15.61 ?  74   PRO   A CD   1 
ATOM   1663 H  HA   . PRO   A 1 74  ? 35.773 1.963   -4.346  1.00 15.99 ?  74   PRO   A HA   1 
ATOM   1664 H  HB2  . PRO   A 1 74  ? 35.662 0.950   -6.936  1.00 18.26 ?  74   PRO   A HB2  1 
ATOM   1665 H  HB3  . PRO   A 1 74  ? 34.799 2.140   -6.318  1.00 18.26 ?  74   PRO   A HB3  1 
ATOM   1666 H  HG2  . PRO   A 1 74  ? 36.630 2.669   -7.968  1.00 21.35 ?  74   PRO   A HG2  1 
ATOM   1667 H  HG3  . PRO   A 1 74  ? 36.372 3.651   -6.737  1.00 21.35 ?  74   PRO   A HG3  1 
ATOM   1668 H  HD2  . PRO   A 1 74  ? 38.402 1.718   -6.978  1.00 18.72 ?  74   PRO   A HD2  1 
ATOM   1669 H  HD3  . PRO   A 1 74  ? 38.528 3.201   -6.377  1.00 18.72 ?  74   PRO   A HD3  1 
ATOM   1670 N  N    . LEU   A 1 75  ? 34.972 -0.362  -4.107  1.00 11.98 ?  75   LEU   A N    1 
ATOM   1671 C  CA   . LEU   A 1 75  ? 34.572 -1.751  -3.958  1.00 11.78 ?  75   LEU   A CA   1 
ATOM   1672 C  C    . LEU   A 1 75  ? 34.184 -2.332  -5.314  1.00 12.21 ?  75   LEU   A C    1 
ATOM   1673 O  O    . LEU   A 1 75  ? 34.038 -1.625  -6.310  1.00 13.86 ?  75   LEU   A O    1 
ATOM   1674 C  CB   . LEU   A 1 75  ? 33.387 -1.875  -2.999  1.00 11.92 ?  75   LEU   A CB   1 
ATOM   1675 C  CG   . LEU   A 1 75  ? 33.614 -1.467  -1.546  1.00 13.67 ?  75   LEU   A CG   1 
ATOM   1676 C  CD1  . LEU   A 1 75  ? 32.334 -1.650  -0.737  1.00 15.38 ?  75   LEU   A CD1  1 
ATOM   1677 C  CD2  . LEU   A 1 75  ? 34.765 -2.196  -0.909  1.00 17.49 ?  75   LEU   A CD2  1 
ATOM   1678 H  H    . LEU   A 1 75  ? 34.410 0.203   -3.783  1.00 14.37 ?  75   LEU   A H    1 
ATOM   1679 H  HA   . LEU   A 1 75  ? 35.312 -2.264  -3.606  1.00 14.13 ?  75   LEU   A HA   1 
ATOM   1680 H  HB2  . LEU   A 1 75  ? 32.664 -1.327  -3.340  1.00 14.30 ?  75   LEU   A HB2  1 
ATOM   1681 H  HB3  . LEU   A 1 75  ? 33.104 -2.805  -2.992  1.00 14.30 ?  75   LEU   A HB3  1 
ATOM   1682 H  HG   . LEU   A 1 75  ? 33.839 -0.521  -1.532  1.00 16.39 ?  75   LEU   A HG   1 
ATOM   1683 H  HD11 . LEU   A 1 75  ? 32.503 -1.380  0.180   1.00 18.45 ?  75   LEU   A HD11 1 
ATOM   1684 H  HD12 . LEU   A 1 75  ? 31.640 -1.093  -1.124  1.00 18.45 ?  75   LEU   A HD12 1 
ATOM   1685 H  HD13 . LEU   A 1 75  ? 32.074 -2.580  -0.769  1.00 18.45 ?  75   LEU   A HD13 1 
ATOM   1686 H  HD21 . LEU   A 1 75  ? 34.814 -1.953  0.028   1.00 20.98 ?  75   LEU   A HD21 1 
ATOM   1687 H  HD22 . LEU   A 1 75  ? 34.620 -3.152  -0.997  1.00 20.98 ?  75   LEU   A HD22 1 
ATOM   1688 H  HD23 . LEU   A 1 75  ? 35.591 -1.947  -1.358  1.00 20.98 ?  75   LEU   A HD23 1 
ATOM   1689 N  N    . LYS   A 1 76  ? 34.027 -3.651  -5.335  1.00 12.54 ?  76   LYS   A N    1 
ATOM   1690 C  CA   . LYS   A 1 76  ? 33.428 -4.367  -6.452  1.00 13.04 ?  76   LYS   A CA   1 
ATOM   1691 C  C    . LYS   A 1 76  ? 31.918 -4.451  -6.253  1.00 11.72 ?  76   LYS   A C    1 
ATOM   1692 O  O    . LYS   A 1 76  ? 31.438 -4.569  -5.127  1.00 11.84 ?  76   LYS   A O    1 
ATOM   1693 C  CB   . LYS   A 1 76  ? 33.976 -5.804  -6.503  1.00 14.73 ?  76   LYS   A CB   1 
ATOM   1694 C  CG   . LYS   A 1 76  ? 35.483 -5.908  -6.686  1.00 16.24 ?  76   LYS   A CG   1 
ATOM   1695 C  CD   . LYS   A 1 76  ? 36.003 -7.312  -6.489  1.00 17.52 ?  76   LYS   A CD   1 
ATOM   1696 C  CE   . LYS   A 1 76  ? 37.496 -7.373  -6.704  1.00 20.01 ?  76   LYS   A CE   1 
ATOM   1697 N  NZ   . LYS   A 1 76  ? 38.026 -8.733  -6.520  1.00 21.23 ?  76   LYS   A NZ   1 
ATOM   1698 H  H    . LYS   A 1 76  ? 34.269 -4.171  -4.691  1.00 15.04 ?  76   LYS   A H    1 
ATOM   1699 H  HA   . LYS   A 1 76  ? 33.623 -3.918  -7.291  1.00 15.64 ?  76   LYS   A HA   1 
ATOM   1700 H  HB2  . LYS   A 1 76  ? 33.750 -6.249  -5.673  1.00 17.67 ?  76   LYS   A HB2  1 
ATOM   1701 H  HB3  . LYS   A 1 76  ? 33.559 -6.267  -7.247  1.00 17.67 ?  76   LYS   A HB3  1 
ATOM   1702 H  HG2  . LYS   A 1 76  ? 35.711 -5.622  -7.586  1.00 19.49 ?  76   LYS   A HG2  1 
ATOM   1703 H  HG3  . LYS   A 1 76  ? 35.919 -5.329  -6.037  1.00 19.49 ?  76   LYS   A HG3  1 
ATOM   1704 H  HD2  . LYS   A 1 76  ? 35.810 -7.600  -5.583  1.00 21.01 ?  76   LYS   A HD2  1 
ATOM   1705 H  HD3  . LYS   A 1 76  ? 35.576 -7.903  -7.129  1.00 21.01 ?  76   LYS   A HD3  1 
ATOM   1706 H  HE2  . LYS   A 1 76  ? 37.699 -7.088  -7.607  1.00 24.00 ?  76   LYS   A HE2  1 
ATOM   1707 H  HE3  . LYS   A 1 76  ? 37.933 -6.791  -6.062  1.00 24.00 ?  76   LYS   A HE3  1 
ATOM   1708 H  HZ1  . LYS   A 1 76  ? 38.904 -8.744  -6.653  1.00 25.47 ?  76   LYS   A HZ1  1 
ATOM   1709 H  HZ2  . LYS   A 1 76  ? 37.854 -9.023  -5.695  1.00 25.47 ?  76   LYS   A HZ2  1 
ATOM   1710 H  HZ3  . LYS   A 1 76  ? 37.641 -9.293  -7.102  1.00 25.47 ?  76   LYS   A HZ3  1 
ATOM   1711 N  N    . VAL   A 1 77  ? 31.166 -4.423  -7.356  1.00 12.21 ?  77   VAL   A N    1 
ATOM   1712 C  CA   . VAL   A 1 77  ? 29.757 -4.803  -7.263  1.00 12.09 ?  77   VAL   A CA   1 
ATOM   1713 C  C    . VAL   A 1 77  ? 29.697 -6.255  -6.820  1.00 11.91 ?  77   VAL   A C    1 
ATOM   1714 O  O    . VAL   A 1 77  ? 30.355 -7.121  -7.407  1.00 12.06 ?  77   VAL   A O    1 
ATOM   1715 C  CB   . VAL   A 1 77  ? 29.032 -4.594  -8.600  1.00 13.22 ?  77   VAL   A CB   1 
ATOM   1716 C  CG1  . VAL   A 1 77  ? 27.582 -5.040  -8.488  1.00 14.22 ?  77   VAL   A CG1  1 
ATOM   1717 C  CG2  . VAL   A 1 77  ? 29.112 -3.139  -9.029  1.00 14.78 ?  77   VAL   A CG2  1 
ATOM   1718 H  H    . VAL   A 1 77  ? 31.442 -4.195  -8.136  1.00 14.64 ?  77   VAL   A H    1 
ATOM   1719 H  HA   . VAL   A 1 77  ? 29.325 -4.257  -6.589  1.00 14.50 ?  77   VAL   A HA   1 
ATOM   1720 H  HB   . VAL   A 1 77  ? 29.467 -5.132  -9.282  1.00 15.86 ?  77   VAL   A HB   1 
ATOM   1721 H  HG11 . VAL   A 1 77  ? 27.103 -4.735  -9.271  1.00 17.06 ?  77   VAL   A HG11 1 
ATOM   1722 H  HG12 . VAL   A 1 77  ? 27.555 -6.009  -8.438  1.00 17.06 ?  77   VAL   A HG12 1 
ATOM   1723 H  HG13 . VAL   A 1 77  ? 27.198 -4.653  -7.688  1.00 17.06 ?  77   VAL   A HG13 1 
ATOM   1724 H  HG21 . VAL   A 1 77  ? 28.610 -3.027  -9.851  1.00 17.73 ?  77   VAL   A HG21 1 
ATOM   1725 H  HG22 . VAL   A 1 77  ? 28.731 -2.584  -8.330  1.00 17.73 ?  77   VAL   A HG22 1 
ATOM   1726 H  HG23 . VAL   A 1 77  ? 30.041 -2.899  -9.173  1.00 17.73 ?  77   VAL   A HG23 1 
ATOM   1727 N  N    . GLY   A 1 78  ? 28.917 -6.528  -5.772  1.00 11.59 ?  78   GLY   A N    1 
ATOM   1728 C  CA   . GLY   A 1 78  ? 28.902 -7.822  -5.125  1.00 11.63 ?  78   GLY   A CA   1 
ATOM   1729 C  C    . GLY   A 1 78  ? 29.817 -7.915  -3.927  1.00 11.48 ?  78   GLY   A C    1 
ATOM   1730 O  O    . GLY   A 1 78  ? 29.757 -8.911  -3.193  1.00 12.24 ?  78   GLY   A O    1 
ATOM   1731 H  H    . GLY   A 1 78  ? 28.371 -5.958  -5.426  1.00 13.90 ?  78   GLY   A H    1 
ATOM   1732 H  HA2  . GLY   A 1 78  ? 27.999 -8.017  -4.836  1.00 13.95 ?  78   GLY   A HA2  1 
ATOM   1733 H  HA3  . GLY   A 1 78  ? 29.168 -8.498  -5.767  1.00 13.95 ?  78   GLY   A HA3  1 
ATOM   1734 N  N    . GLY   A 1 79  ? 30.670 -6.909  -3.707  1.00 11.46 ?  79   GLY   A N    1 
ATOM   1735 C  CA   . GLY   A 1 79  ? 31.635 -6.926  -2.633  1.00 11.69 ?  79   GLY   A CA   1 
ATOM   1736 C  C    . GLY   A 1 79  ? 31.185 -6.136  -1.416  1.00 10.87 ?  79   GLY   A C    1 
ATOM   1737 O  O    . GLY   A 1 79  ? 30.064 -5.631  -1.335  1.00 11.61 ?  79   GLY   A O    1 
ATOM   1738 H  H    . GLY   A 1 79  ? 30.710 -6.192  -4.187  1.00 13.75 ?  79   GLY   A H    1 
ATOM   1739 H  HA2  . GLY   A 1 79  ? 31.791 -7.853  -2.365  1.00 14.02 ?  79   GLY   A HA2  1 
ATOM   1740 H  HA3  . GLY   A 1 79  ? 32.474 -6.562  -2.947  1.00 14.02 ?  79   GLY   A HA3  1 
ATOM   1741 N  N    . SER   A 1 80  ? 32.089 -6.046  -0.447  1.00 11.72 ?  80   SER   A N    1 
ATOM   1742 C  CA   . SER   A 1 80  ? 31.773 -5.413  0.821   1.00 11.47 ?  80   SER   A CA   1 
ATOM   1743 C  C    . SER   A 1 80  ? 33.044 -4.963  1.514   1.00 11.18 ?  80   SER   A C    1 
ATOM   1744 O  O    . SER   A 1 80  ? 34.156 -5.390  1.182   1.00 12.65 ?  80   SER   A O    1 
ATOM   1745 C  CB   . SER   A 1 80  ? 31.023 -6.379  1.743   1.00 12.35 ?  80   SER   A CB   1 
ATOM   1746 O  OG   . SER   A 1 80  ? 31.858 -7.426  2.211   1.00 13.79 ?  80   SER   A OG   1 
ATOM   1747 H  H    . SER   A 1 80  ? 32.898 -6.330  -0.507  1.00 14.06 ?  80   SER   A H    1 
ATOM   1748 H  HA   . SER   A 1 80  ? 31.216 -4.637  0.652   1.00 13.76 ?  80   SER   A HA   1 
ATOM   1749 H  HB2  . SER   A 1 80  ? 30.683 -5.885  2.504   1.00 14.81 ?  80   SER   A HB2  1 
ATOM   1750 H  HB3  . SER   A 1 80  ? 30.281 -6.767  1.248   1.00 14.81 ?  80   SER   A HB3  1 
ATOM   1751 H  HG   . SER   A 1 80  ? 32.158 -7.863  1.556   1.00 16.55 ?  80   SER   A HG   1 
ATOM   1752 N  N    . CYS   A 1 81  ? 32.855 -4.116  2.521   1.00 10.82 ?  81   CYS   A N    1 
ATOM   1753 C  CA   . CYS   A 1 81  ? 33.907 -3.838  3.486   1.00 11.10 ?  81   CYS   A CA   1 
ATOM   1754 C  C    . CYS   A 1 81  ? 33.269 -3.606  4.845   1.00 11.04 ?  81   CYS   A C    1 
ATOM   1755 O  O    . CYS   A 1 81  ? 32.102 -3.207  4.936   1.00 12.24 ?  81   CYS   A O    1 
ATOM   1756 C  CB   . CYS   A 1 81  ? 34.777 -2.645  3.075   1.00 12.05 ?  81   CYS   A CB   1 
ATOM   1757 S  SG   . CYS   A 1 81  ? 33.872 -1.068  3.086   1.00 11.96 ?  81   CYS   A SG   1 
ATOM   1758 H  H    . CYS   A 1 81  ? 32.122 -3.686  2.673   1.00 12.98 ?  81   CYS   A H    1 
ATOM   1759 H  HA   . CYS   A 1 81  ? 34.488 -4.613  3.551   1.00 13.31 ?  81   CYS   A HA   1 
ATOM   1760 H  HB2  . CYS   A 1 81  ? 35.525 -2.568  3.691   1.00 14.46 ?  81   CYS   A HB2  1 
ATOM   1761 H  HB3  . CYS   A 1 81  ? 35.114 -2.794  2.173   1.00 14.46 ?  81   CYS   A HB3  1 
ATOM   1762 H  HG   . CYS   A 1 81  ? 34.615 -0.185  2.752   1.00 14.34 ?  81   CYS   A HG   1 
ATOM   1763 N  N    . VAL   A 1 82  ? 34.042 -3.865  5.896   1.00 11.35 ?  82   VAL   A N    1 
ATOM   1764 C  CA   . VAL   A 1 82  ? 33.620 -3.627  7.268   1.00 11.81 ?  82   VAL   A CA   1 
ATOM   1765 C  C    . VAL   A 1 82  ? 34.217 -2.309  7.732   1.00 12.18 ?  82   VAL   A C    1 
ATOM   1766 O  O    . VAL   A 1 82  ? 35.442 -2.132  7.714   1.00 12.87 ?  82   VAL   A O    1 
ATOM   1767 C  CB   . VAL   A 1 82  ? 34.049 -4.766  8.205   1.00 13.46 ?  82   VAL   A CB   1 
ATOM   1768 C  CG1  . VAL   A 1 82  ? 33.592 -4.472  9.627   1.00 15.07 ?  82   VAL   A CG1  1 
ATOM   1769 C  CG2  . VAL   A 1 82  ? 33.506 -6.100  7.730   1.00 14.61 ?  82   VAL   A CG2  1 
ATOM   1770 H  H    . VAL   A 1 82  ? 34.839 -4.209  5.835   1.00 13.62 ?  82   VAL   A H    1 
ATOM   1771 H  HA   . VAL   A 1 82  ? 32.655 -3.555  7.294   1.00 14.17 ?  82   VAL   A HA   1 
ATOM   1772 H  HB   . VAL   A 1 82  ? 35.016 -4.819  8.214   1.00 16.14 ?  82   VAL   A HB   1 
ATOM   1773 H  HG11 . VAL   A 1 82  ? 33.683 -5.274  10.163  1.00 18.07 ?  82   VAL   A HG11 1 
ATOM   1774 H  HG12 . VAL   A 1 82  ? 34.138 -3.762  10.003  1.00 18.07 ?  82   VAL   A HG12 1 
ATOM   1775 H  HG13 . VAL   A 1 82  ? 32.659 -4.193  9.611   1.00 18.07 ?  82   VAL   A HG13 1 
ATOM   1776 H  HG21 . VAL   A 1 82  ? 33.754 -6.785  8.370   1.00 17.52 ?  82   VAL   A HG21 1 
ATOM   1777 H  HG22 . VAL   A 1 82  ? 32.541 -6.041  7.664   1.00 17.52 ?  82   VAL   A HG22 1 
ATOM   1778 H  HG23 . VAL   A 1 82  ? 33.888 -6.302  6.862   1.00 17.52 ?  82   VAL   A HG23 1 
ATOM   1779 N  N    . LEU   A 1 83  ? 33.357 -1.389  8.150   1.00 11.63 ?  83   LEU   A N    1 
ATOM   1780 C  CA   . LEU   A 1 83  ? 33.775 -0.125  8.737   1.00 11.15 ?  83   LEU   A CA   1 
ATOM   1781 C  C    . LEU   A 1 83  ? 33.063 0.046   10.075  1.00 11.44 ?  83   LEU   A C    1 
ATOM   1782 O  O    . LEU   A 1 83  ? 32.346 -0.847  10.541  1.00 12.20 ?  83   LEU   A O    1 
ATOM   1783 C  CB   . LEU   A 1 83  ? 33.522 1.038   7.766   1.00 12.00 ?  83   LEU   A CB   1 
ATOM   1784 C  CG   . LEU   A 1 83  ? 34.410 1.031   6.515   1.00 12.78 ?  83   LEU   A CG   1 
ATOM   1785 C  CD1  . LEU   A 1 83  ? 33.962 2.070   5.504   1.00 13.17 ?  83   LEU   A CD1  1 
ATOM   1786 C  CD2  . LEU   A 1 83  ? 35.874 1.263   6.882   1.00 13.87 ?  83   LEU   A CD2  1 
ATOM   1787 H  H    . LEU   A 1 83  ? 32.506 -1.474  8.091   1.00 13.96 ?  83   LEU   A H    1 
ATOM   1788 H  HA   . LEU   A 1 83  ? 34.728 -0.153  8.909   1.00 13.37 ?  83   LEU   A HA   1 
ATOM   1789 H  HB2  . LEU   A 1 83  ? 32.600 1.004   7.462   1.00 14.39 ?  83   LEU   A HB2  1 
ATOM   1790 H  HB3  . LEU   A 1 83  ? 33.678 1.877   8.227   1.00 14.39 ?  83   LEU   A HB3  1 
ATOM   1791 H  HG   . LEU   A 1 83  ? 34.352 0.161   6.095   1.00 15.32 ?  83   LEU   A HG   1 
ATOM   1792 H  HD11 . LEU   A 1 83  ? 34.544 2.026   4.726   1.00 15.79 ?  83   LEU   A HD11 1 
ATOM   1793 H  HD12 . LEU   A 1 83  ? 33.048 1.874   5.239   1.00 15.79 ?  83   LEU   A HD12 1 
ATOM   1794 H  HD13 . LEU   A 1 83  ? 34.011 2.948   5.906   1.00 15.79 ?  83   LEU   A HD13 1 
ATOM   1795 H  HD21 . LEU   A 1 83  ? 36.386 1.409   6.068   1.00 16.64 ?  83   LEU   A HD21 1 
ATOM   1796 H  HD22 . LEU   A 1 83  ? 35.937 2.050   7.451   1.00 16.64 ?  83   LEU   A HD22 1 
ATOM   1797 H  HD23 . LEU   A 1 83  ? 36.214 0.489   7.351   1.00 16.64 ?  83   LEU   A HD23 1 
ATOM   1798 N  N    . SER   A 1 84  ? 33.280 1.194   10.710  1.00 11.83 ?  84   SER   A N    1 
ATOM   1799 C  CA   . SER   A 1 84  ? 32.632 1.450   11.984  1.00 12.16 ?  84   SER   A CA   1 
ATOM   1800 C  C    . SER   A 1 84  ? 31.113 1.524   11.832  1.00 12.23 ?  84   SER   A C    1 
ATOM   1801 O  O    . SER   A 1 84  ? 30.587 1.990   10.823  1.00 12.44 ?  84   SER   A O    1 
ATOM   1802 C  CB   . SER   A 1 84  ? 33.120 2.777   12.551  1.00 13.04 ?  84   SER   A CB   1 
ATOM   1803 O  OG   . SER   A 1 84  ? 32.491 3.046   13.785  1.00 14.31 ?  84   SER   A OG   1 
ATOM   1804 H  H    . SER   A 1 84  ? 33.790 1.829   10.421  1.00 14.19 ?  84   SER   A H    1 
ATOM   1805 H  HA   . SER   A 1 84  ? 32.853 0.741   12.603  1.00 14.59 ?  84   SER   A HA   1 
ATOM   1806 H  HB2  . SER   A 1 84  ? 34.084 2.730   12.676  1.00 15.65 ?  84   SER   A HB2  1 
ATOM   1807 H  HB3  . SER   A 1 84  ? 32.906 3.488   11.925  1.00 15.65 ?  84   SER   A HB3  1 
ATOM   1808 H  HG   . SER   A 1 84  ? 32.779 3.774   14.095  1.00 17.16 ?  84   SER   A HG   1 
ATOM   1809 N  N    . GLY   A 1 85  ? 30.407 1.105   12.879  1.00 13.12 ?  85   GLY   A N    1 
ATOM   1810 C  CA   . GLY   A 1 85  ? 28.983 1.336   12.965  1.00 13.97 ?  85   GLY   A CA   1 
ATOM   1811 C  C    . GLY   A 1 85  ? 28.618 2.639   13.629  1.00 13.76 ?  85   GLY   A C    1 
ATOM   1812 O  O    . GLY   A 1 85  ? 27.429 2.948   13.762  1.00 14.17 ?  85   GLY   A O    1 
ATOM   1813 H  H    . GLY   A 1 85  ? 30.741 0.677   13.546  1.00 15.74 ?  85   GLY   A H    1 
ATOM   1814 H  HA2  . GLY   A 1 85  ? 28.611 1.333   12.066  1.00 16.75 ?  85   GLY   A HA2  1 
ATOM   1815 H  HA3  . GLY   A 1 85  ? 28.577 0.619   13.463  1.00 16.75 ?  85   GLY   A HA3  1 
ATOM   1816 N  N    . HIS   A 1 86  ? 29.608 3.417   14.056  1.00 13.59 ?  86   HIS   A N    1 
ATOM   1817 C  CA   . HIS   A 1 86  ? 29.384 4.749   14.628  1.00 13.78 ?  86   HIS   A CA   1 
ATOM   1818 C  C    . HIS   A 1 86  ? 28.413 4.624   15.796  1.00 14.60 ?  86   HIS   A C    1 
ATOM   1819 O  O    . HIS   A 1 86  ? 28.609 3.749   16.656  1.00 15.88 ?  86   HIS   A O    1 
ATOM   1820 C  CB   . HIS   A 1 86  ? 28.996 5.733   13.531  1.00 13.48 ?  86   HIS   A CB   1 
ATOM   1821 C  CG   . HIS   A 1 86  ? 30.046 5.843   12.487  1.00 13.62 ?  86   HIS   A CG   1 
ATOM   1822 N  ND1  . HIS   A 1 86  ? 31.126 6.691   12.611  1.00 14.53 ?  86   HIS   A ND1  1 
ATOM   1823 C  CD2  . HIS   A 1 86  ? 30.233 5.150   11.344  1.00 12.89 ?  86   HIS   A CD2  1 
ATOM   1824 C  CE1  . HIS   A 1 86  ? 31.917 6.533   11.566  1.00 13.92 ?  86   HIS   A CE1  1 
ATOM   1825 N  NE2  . HIS   A 1 86  ? 31.404 5.597   10.789  1.00 13.46 ?  86   HIS   A NE2  1 
ATOM   1826 H  H    . HIS   A 1 86  ? 30.436 3.195   14.036  1.00 16.30 ?  86   HIS   A H    1 
ATOM   1827 H  HA   . HIS   A 1 86  ? 30.222 5.065   14.991  1.00 16.53 ?  86   HIS   A HA   1 
ATOM   1828 H  HB2  . HIS   A 1 86  ? 28.173 5.440   13.104  1.00 16.17 ?  86   HIS   A HB2  1 
ATOM   1829 H  HB3  . HIS   A 1 86  ? 28.865 6.619   13.917  1.00 16.17 ?  86   HIS   A HB3  1 
ATOM   1830 H  HD2  . HIS   A 1 86  ? 29.678 4.483   10.998  1.00 15.46 ?  86   HIS   A HD2  1 
ATOM   1831 H  HE1  . HIS   A 1 86  ? 32.701 7.002   11.391  1.00 16.70 ?  86   HIS   A HE1  1 
ATOM   1832 H  HE2  . HIS   A 1 86  ? 31.739 5.321   10.037  1.00 16.15 ?  86   HIS   A HE2  1 
ATOM   1833 N  N    . ASN   A 1 87  ? 27.402 5.478   15.883  1.00 15.79 ?  87   ASN   A N    1 
ATOM   1834 C  CA   . ASN   A 1 87  ? 26.422 5.460   16.955  1.00 17.03 ?  87   ASN   A CA   1 
ATOM   1835 C  C    . ASN   A 1 87  ? 25.308 4.449   16.727  1.00 17.85 ?  87   ASN   A C    1 
ATOM   1836 O  O    . ASN   A 1 87  ? 24.408 4.352   17.566  1.00 20.29 ?  87   ASN   A O    1 
ATOM   1837 C  CB   . ASN   A 1 87  ? 25.817 6.863   17.119  1.00 18.22 ?  87   ASN   A CB   1 
ATOM   1838 C  CG   . ASN   A 1 87  ? 25.300 7.444   15.804  1.00 18.82 ?  87   ASN   A CG   1 
ATOM   1839 O  OD1  . ASN   A 1 87  ? 25.933 7.325   14.760  1.00 19.32 ?  87   ASN   A OD1  1 
ATOM   1840 N  ND2  . ASN   A 1 87  ? 24.150 8.090   15.861  1.00 19.77 ?  87   ASN   A ND2  1 
ATOM   1841 H  H    . ASN   A 1 87  ? 27.259 6.102   15.312  1.00 18.94 ?  87   ASN   A H    1 
ATOM   1842 H  HA   . ASN   A 1 87  ? 26.862 5.225   17.789  1.00 20.44 ?  87   ASN   A HA   1 
ATOM   1843 H  HB2  . ASN   A 1 87  ? 25.070 6.812   17.744  1.00 21.86 ?  87   ASN   A HB2  1 
ATOM   1844 H  HB3  . ASN   A 1 87  ? 26.496 7.458   17.468  1.00 21.86 ?  87   ASN   A HB3  1 
ATOM   1845 H  HD21 . ASN   A 1 87  ? 23.819 8.434   15.149  1.00 23.72 ?  87   ASN   A HD21 1 
ATOM   1846 H  HD22 . ASN   A 1 87  ? 23.735 8.168   16.612  1.00 23.72 ?  87   ASN   A HD22 1 
ATOM   1847 N  N    . LEU   A 1 88  ? 25.353 3.688   15.637  1.00 16.98 ?  88   LEU   A N    1 
ATOM   1848 C  CA   . LEU   A 1 88  ? 24.244 2.822   15.250  1.00 16.77 ?  88   LEU   A CA   1 
ATOM   1849 C  C    . LEU   A 1 88  ? 24.471 1.345   15.545  1.00 16.45 ?  88   LEU   A C    1 
ATOM   1850 O  O    . LEU   A 1 88  ? 23.498 0.612   15.744  1.00 17.64 ?  88   LEU   A O    1 
ATOM   1851 C  CB   . LEU   A 1 88  ? 23.972 2.983   13.753  1.00 17.29 ?  88   LEU   A CB   1 
ATOM   1852 C  CG   . LEU   A 1 88  ? 23.667 4.405   13.275  1.00 18.69 ?  88   LEU   A CG   1 
ATOM   1853 C  CD1  . LEU   A 1 88  ? 23.496 4.422   11.766  1.00 19.00 ?  88   LEU   A CD1  1 
ATOM   1854 C  CD2  . LEU   A 1 88  ? 22.431 4.973   13.965  1.00 20.35 ?  88   LEU   A CD2  1 
ATOM   1855 H  H    . LEU   A 1 88  ? 26.025 3.653   15.102  1.00 20.37 ?  88   LEU   A H    1 
ATOM   1856 H  HA   . LEU   A 1 88  ? 23.448 3.101   15.727  1.00 20.12 ?  88   LEU   A HA   1 
ATOM   1857 H  HB2  . LEU   A 1 88  ? 24.749 2.679   13.262  1.00 20.74 ?  88   LEU   A HB2  1 
ATOM   1858 H  HB3  . LEU   A 1 88  ? 23.206 2.436   13.519  1.00 20.74 ?  88   LEU   A HB3  1 
ATOM   1859 H  HG   . LEU   A 1 88  ? 24.419 4.979   13.489  1.00 22.42 ?  88   LEU   A HG   1 
ATOM   1860 H  HD11 . LEU   A 1 88  ? 23.306 5.330   11.477  1.00 22.80 ?  88   LEU   A HD11 1 
ATOM   1861 H  HD12 . LEU   A 1 88  ? 24.314 4.109   11.349  1.00 22.80 ?  88   LEU   A HD12 1 
ATOM   1862 H  HD13 . LEU   A 1 88  ? 22.758 3.840   11.524  1.00 22.80 ?  88   LEU   A HD13 1 
ATOM   1863 H  HD21 . LEU   A 1 88  ? 22.216 5.831   13.565  1.00 24.42 ?  88   LEU   A HD21 1 
ATOM   1864 H  HD22 . LEU   A 1 88  ? 21.695 4.356   13.844  1.00 24.42 ?  88   LEU   A HD22 1 
ATOM   1865 H  HD23 . LEU   A 1 88  ? 22.624 5.084   14.907  1.00 24.42 ?  88   LEU   A HD23 1 
ATOM   1866 N  N    . ALA   A 1 89  ? 25.721 0.897   15.564  1.00 15.66 ?  89   ALA   A N    1 
ATOM   1867 C  CA   . ALA   A 1 89  ? 26.063 -0.514  15.668  1.00 15.16 ?  89   ALA   A CA   1 
ATOM   1868 C  C    . ALA   A 1 89  ? 27.549 -0.567  15.979  1.00 15.63 ?  89   ALA   A C    1 
ATOM   1869 O  O    . ALA   A 1 89  ? 28.251 0.437   15.867  1.00 16.42 ?  89   ALA   A O    1 
ATOM   1870 C  CB   . ALA   A 1 89  ? 25.778 -1.236  14.352  1.00 14.59 ?  89   ALA   A CB   1 
ATOM   1871 H  H    . ALA   A 1 89  ? 26.409 1.410   15.506  1.00 18.78 ?  89   ALA   A H    1 
ATOM   1872 H  HA   . ALA   A 1 89  ? 25.565 -0.932  16.387  1.00 18.19 ?  89   ALA   A HA   1 
ATOM   1873 H  HB1  . ALA   A 1 89  ? 26.036 -2.169  14.440  1.00 17.50 ?  89   ALA   A HB1  1 
ATOM   1874 H  HB2  . ALA   A 1 89  ? 24.827 -1.178  14.158  1.00 17.50 ?  89   ALA   A HB2  1 
ATOM   1875 H  HB3  . ALA   A 1 89  ? 26.286 -0.819  13.643  1.00 17.50 ?  89   ALA   A HB3  1 
ATOM   1876 N  N    . LYS   A 1 90  ? 28.041 -1.746  16.353  1.00 16.08 ?  90   LYS   A N    1 
ATOM   1877 C  CA   . LYS   A 1 90  ? 29.487 -1.885  16.497  1.00 16.74 ?  90   LYS   A CA   1 
ATOM   1878 C  C    . LYS   A 1 90  ? 30.181 -1.691  15.153  1.00 15.58 ?  90   LYS   A C    1 
ATOM   1879 O  O    . LYS   A 1 90  ? 31.116 -0.884  15.025  1.00 16.85 ?  90   LYS   A O    1 
ATOM   1880 C  CB   . LYS   A 1 90  ? 29.835 -3.241  17.108  1.00 19.50 ?  90   LYS   A CB   1 
ATOM   1881 C  CG   . LYS   A 1 90  ? 31.313 -3.373  17.447  1.00 23.80 ?  90   LYS   A CG   1 
ATOM   1882 C  CD   . LYS   A 1 90  ? 31.567 -4.572  18.344  1.00 28.23 ?  90   LYS   A CD   1 
ATOM   1883 C  CE   . LYS   A 1 90  ? 32.982 -4.573  18.899  1.00 31.59 ?  90   LYS   A CE   1 
ATOM   1884 N  NZ   . LYS   A 1 90  ? 33.994 -4.922  17.868  1.00 33.84 ?  90   LYS   A NZ   1 
ATOM   1885 H  H    . LYS   A 1 90  ? 27.578 -2.449  16.523  1.00 19.29 ?  90   LYS   A H    1 
ATOM   1886 H  HA   . LYS   A 1 90  ? 29.808 -1.196  17.095  1.00 20.09 ?  90   LYS   A HA   1 
ATOM   1887 H  HB2  . LYS   A 1 90  ? 29.326 -3.356  17.928  1.00 23.39 ?  90   LYS   A HB2  1 
ATOM   1888 H  HB3  . LYS   A 1 90  ? 29.607 -3.942  16.478  1.00 23.39 ?  90   LYS   A HB3  1 
ATOM   1889 H  HG2  . LYS   A 1 90  ? 31.820 -3.489  16.629  1.00 28.55 ?  90   LYS   A HG2  1 
ATOM   1890 H  HG3  . LYS   A 1 90  ? 31.606 -2.574  17.915  1.00 28.55 ?  90   LYS   A HG3  1 
ATOM   1891 H  HD2  . LYS   A 1 90  ? 30.947 -4.550  19.091  1.00 33.87 ?  90   LYS   A HD2  1 
ATOM   1892 H  HD3  . LYS   A 1 90  ? 31.441 -5.386  17.830  1.00 33.87 ?  90   LYS   A HD3  1 
ATOM   1893 H  HE2  . LYS   A 1 90  ? 33.190 -3.688  19.239  1.00 37.90 ?  90   LYS   A HE2  1 
ATOM   1894 H  HE3  . LYS   A 1 90  ? 33.042 -5.226  19.615  1.00 37.90 ?  90   LYS   A HE3  1 
ATOM   1895 H  HZ1  . LYS   A 1 90  ? 33.829 -5.735  17.543  1.00 40.61 ?  90   LYS   A HZ1  1 
ATOM   1896 H  HZ2  . LYS   A 1 90  ? 33.967 -4.333  17.202  1.00 40.61 ?  90   LYS   A HZ2  1 
ATOM   1897 H  HZ3  . LYS   A 1 90  ? 34.809 -4.916  18.227  1.00 40.61 ?  90   LYS   A HZ3  1 
ATOM   1898 N  N    . HIS   A 1 91  ? 29.710 -2.407  14.132  1.00 13.66 ?  91   HIS   A N    1 
ATOM   1899 C  CA   . HIS   A 1 91  ? 30.276 -2.383  12.799  1.00 13.07 ?  91   HIS   A CA   1 
ATOM   1900 C  C    . HIS   A 1 91  ? 29.181 -2.110  11.787  1.00 11.95 ?  91   HIS   A C    1 
ATOM   1901 O  O    . HIS   A 1 91  ? 28.014 -2.474  11.987  1.00 12.92 ?  91   HIS   A O    1 
ATOM   1902 C  CB   . HIS   A 1 91  ? 30.874 -3.749  12.426  1.00 15.63 ?  91   HIS   A CB   1 
ATOM   1903 C  CG   . HIS   A 1 91  ? 31.873 -4.269  13.409  1.00 19.68 ?  91   HIS   A CG   1 
ATOM   1904 N  ND1  . HIS   A 1 91  ? 33.142 -3.745  13.529  1.00 21.63 ?  91   HIS   A ND1  1 
ATOM   1905 C  CD2  . HIS   A 1 91  ? 31.798 -5.282  14.304  1.00 21.16 ?  91   HIS   A CD2  1 
ATOM   1906 C  CE1  . HIS   A 1 91  ? 33.802 -4.406  14.464  1.00 22.25 ?  91   HIS   A CE1  1 
ATOM   1907 N  NE2  . HIS   A 1 91  ? 33.008 -5.344  14.950  1.00 22.42 ?  91   HIS   A NE2  1 
ATOM   1908 H  H    . HIS   A 1 91  ? 29.037 -2.953  14.201  1.00 16.39 ?  91   HIS   A H    1 
ATOM   1909 H  HA   . HIS   A 1 91  ? 30.964 -1.710  12.733  1.00 15.68 ?  91   HIS   A HA   1 
ATOM   1910 H  HB2  . HIS   A 1 91  ? 30.155 -4.403  12.369  1.00 18.75 ?  91   HIS   A HB2  1 
ATOM   1911 H  HB3  . HIS   A 1 91  ? 31.316 -3.677  11.567  1.00 18.75 ?  91   HIS   A HB3  1 
ATOM   1912 H  HD1  . HIS   A 1 91  ? 33.454 -3.088  13.069  1.00 25.95 ?  91   HIS   A HD1  1 
ATOM   1913 H  HD2  . HIS   A 1 91  ? 31.068 -5.833  14.460  1.00 25.39 ?  91   HIS   A HD2  1 
ATOM   1914 H  HE1  . HIS   A 1 91  ? 34.680 -4.235  14.733  1.00 26.69 ?  91   HIS   A HE1  1 
ATOM   1915 N  N    . CYS   A 1 92  ? 29.578 -1.508  10.673  1.00 11.60 ?  92   CYS   A N    1 
ATOM   1916 C  CA   . CYS   A 1 92  ? 28.738 -1.436  9.487   1.00 11.76 ?  92   CYS   A CA   1 
ATOM   1917 C  C    . CYS   A 1 92  ? 29.383 -2.252  8.376   1.00 11.08 ?  92   CYS   A C    1 
ATOM   1918 O  O    . CYS   A 1 92  ? 30.540 -1.997  8.003   1.00 11.67 ?  92   CYS   A O    1 
ATOM   1919 C  CB   . CYS   A 1 92  ? 28.528 0.006   9.021   1.00 12.02 ?  92   CYS   A CB   1 
ATOM   1920 S  SG   . CYS   A 1 92  ? 27.498 0.109   7.516   1.00 11.56 ?  92   CYS   A SG   1 
ATOM   1921 H  H    . CYS   A 1 92  ? 30.344 -1.121  10.580  1.00 13.91 ?  92   CYS   A H    1 
ATOM   1922 H  HA   . CYS   A 1 92  ? 27.871 -1.817  9.685   1.00 14.11 ?  92   CYS   A HA   1 
ATOM   1923 H  HB2  . CYS   A 1 92  ? 28.085 0.509   9.723   1.00 14.41 ?  92   CYS   A HB2  1 
ATOM   1924 H  HB3  . CYS   A 1 92  ? 29.389 0.406   8.819   1.00 14.41 ?  92   CYS   A HB3  1 
ATOM   1925 H  HG   . CYS   A 1 92  ? 27.357 1.262   7.224   1.00 13.87 ?  92   CYS   A HG   1 
ATOM   1926 N  N    . LEU   A 1 93  ? 28.648 -3.242  7.873   1.00 10.86 ?  93   LEU   A N    1 
ATOM   1927 C  CA   . LEU   A 1 93  ? 29.052 -3.997  6.691   1.00 10.45 ?  93   LEU   A CA   1 
ATOM   1928 C  C    . LEU   A 1 93  ? 28.449 -3.302  5.477   1.00 9.96  ?  93   LEU   A C    1 
ATOM   1929 O  O    . LEU   A 1 93  ? 27.232 -3.355  5.259   1.00 10.28 ?  93   LEU   A O    1 
ATOM   1930 C  CB   . LEU   A 1 93  ? 28.577 -5.446  6.795   1.00 11.18 ?  93   LEU   A CB   1 
ATOM   1931 C  CG   . LEU   A 1 93  ? 28.967 -6.339  5.622   1.00 11.28 ?  93   LEU   A CG   1 
ATOM   1932 C  CD1  . LEU   A 1 93  ? 30.468 -6.590  5.605   1.00 12.06 ?  93   LEU   A CD1  1 
ATOM   1933 C  CD2  . LEU   A 1 93  ? 28.196 -7.659  5.658   1.00 12.31 ?  93   LEU   A CD2  1 
ATOM   1934 H  H    . LEU   A 1 93  ? 27.892 -3.493  8.209   1.00 13.03 ?  93   LEU   A H    1 
ATOM   1935 H  HA   . LEU   A 1 93  ? 30.014 -3.980  6.619   1.00 12.54 ?  93   LEU   A HA   1 
ATOM   1936 H  HB2  . LEU   A 1 93  ? 28.957 -5.831  7.603   1.00 13.41 ?  93   LEU   A HB2  1 
ATOM   1937 H  HB3  . LEU   A 1 93  ? 27.611 -5.448  6.860   1.00 13.41 ?  93   LEU   A HB3  1 
ATOM   1938 H  HG   . LEU   A 1 93  ? 28.743 -5.886  4.800   1.00 13.53 ?  93   LEU   A HG   1 
ATOM   1939 H  HD11 . LEU   A 1 93  ? 30.684 -7.201  4.883   1.00 14.47 ?  93   LEU   A HD11 1 
ATOM   1940 H  HD12 . LEU   A 1 93  ? 30.939 -5.751  5.479   1.00 14.47 ?  93   LEU   A HD12 1 
ATOM   1941 H  HD13 . LEU   A 1 93  ? 30.738 -6.988  6.456   1.00 14.47 ?  93   LEU   A HD13 1 
ATOM   1942 H  HD21 . LEU   A 1 93  ? 28.473 -8.203  4.900   1.00 14.76 ?  93   LEU   A HD21 1 
ATOM   1943 H  HD22 . LEU   A 1 93  ? 28.397 -8.124  6.485   1.00 14.76 ?  93   LEU   A HD22 1 
ATOM   1944 H  HD23 . LEU   A 1 93  ? 27.248 -7.473  5.601   1.00 14.76 ?  93   LEU   A HD23 1 
ATOM   1945 N  N    . HIS   A 1 94  ? 29.294 -2.605  4.717   1.00 10.05 ?  94   HIS   A N    1 
ATOM   1946 C  CA   . HIS   A 1 94  ? 28.862 -1.930  3.495   1.00 9.85  ?  94   HIS   A CA   1 
ATOM   1947 C  C    . HIS   A 1 94  ? 28.869 -2.960  2.383   1.00 10.06 ?  94   HIS   A C    1 
ATOM   1948 O  O    . HIS   A 1 94  ? 29.934 -3.466  2.031   1.00 11.66 ?  94   HIS   A O    1 
ATOM   1949 C  CB   . HIS   A 1 94  ? 29.809 -0.777  3.159   1.00 10.14 ?  94   HIS   A CB   1 
ATOM   1950 C  CG   . HIS   A 1 94  ? 29.800 0.309   4.176   1.00 9.92  ?  94   HIS   A CG   1 
ATOM   1951 N  ND1  . HIS   A 1 94  ? 28.921 1.370   4.126   1.00 10.01 ?  94   HIS   A ND1  1 
ATOM   1952 C  CD2  . HIS   A 1 94  ? 30.548 0.479   5.289   1.00 10.73 ?  94   HIS   A CD2  1 
ATOM   1953 C  CE1  . HIS   A 1 94  ? 29.134 2.147   5.171   1.00 10.22 ?  94   HIS   A CE1  1 
ATOM   1954 N  NE2  . HIS   A 1 94  ? 30.117 1.632   5.891   1.00 10.59 ?  94   HIS   A NE2  1 
ATOM   1955 H  H    . HIS   A 1 94  ? 30.133 -2.505  4.890   1.00 12.05 ?  94   HIS   A H    1 
ATOM   1956 H  HA   . HIS   A 1 94  ? 27.959 -1.586  3.604   1.00 11.81 ?  94   HIS   A HA   1 
ATOM   1957 H  HB2  . HIS   A 1 94  ? 30.708 -1.117  3.094   1.00 12.16 ?  94   HIS   A HB2  1 
ATOM   1958 H  HB3  . HIS   A 1 94  ? 29.536 -0.387  2.311   1.00 12.16 ?  94   HIS   A HB3  1 
ATOM   1959 H  HD2  . HIS   A 1 94  ? 31.226 -0.076  5.593   1.00 12.88 ?  94   HIS   A HD2  1 
ATOM   1960 H  HE1  . HIS   A 1 94  ? 28.668 2.931   5.366   1.00 12.26 ?  94   HIS   A HE1  1 
ATOM   1961 H  HE2  . HIS   A 1 94  ? 30.434 1.975   6.616   1.00 12.71 ?  94   HIS   A HE2  1 
ATOM   1962 N  N    . VAL   A 1 95  ? 27.700 -3.279  1.836   1.00 9.37  ?  95   VAL   A N    1 
ATOM   1963 C  CA   . VAL   A 1 95  ? 27.562 -4.317  0.818   1.00 9.87  ?  95   VAL   A CA   1 
ATOM   1964 C  C    . VAL   A 1 95  ? 27.015 -3.679  -0.445  1.00 9.67  ?  95   VAL   A C    1 
ATOM   1965 O  O    . VAL   A 1 95  ? 26.006 -2.964  -0.392  1.00 10.26 ?  95   VAL   A O    1 
ATOM   1966 C  CB   . VAL   A 1 95  ? 26.637 -5.460  1.272   1.00 10.49 ?  95   VAL   A CB   1 
ATOM   1967 C  CG1  . VAL   A 1 95  ? 26.537 -6.504  0.166   1.00 11.47 ?  95   VAL   A CG1  1 
ATOM   1968 C  CG2  . VAL   A 1 95  ? 27.140 -6.073  2.558   1.00 10.45 ?  95   VAL   A CG2  1 
ATOM   1969 H  H    . VAL   A 1 95  ? 26.953 -2.905  2.048   1.00 11.24 ?  95   VAL   A H    1 
ATOM   1970 H  HA   . VAL   A 1 95  ? 28.434 -4.687  0.616   1.00 11.84 ?  95   VAL   A HA   1 
ATOM   1971 H  HB   . VAL   A 1 95  ? 25.754 -5.108  1.430   1.00 12.58 ?  95   VAL   A HB   1 
ATOM   1972 H  HG11 . VAL   A 1 95  ? 26.152 -7.318  0.530   1.00 13.76 ?  95   VAL   A HG11 1 
ATOM   1973 H  HG12 . VAL   A 1 95  ? 25.973 -6.166  -0.548  1.00 13.76 ?  95   VAL   A HG12 1 
ATOM   1974 H  HG13 . VAL   A 1 95  ? 27.427 -6.694  -0.181  1.00 13.76 ?  95   VAL   A HG13 1 
ATOM   1975 H  HG21 . VAL   A 1 95  ? 26.581 -6.831  2.782   1.00 12.53 ?  95   VAL   A HG21 1 
ATOM   1976 H  HG22 . VAL   A 1 95  ? 28.058 -6.357  2.437   1.00 12.53 ?  95   VAL   A HG22 1 
ATOM   1977 H  HG23 . VAL   A 1 95  ? 27.089 -5.404  3.260   1.00 12.53 ?  95   VAL   A HG23 1 
ATOM   1978 N  N    . VAL   A 1 96  ? 27.648 -3.958  -1.581  1.00 9.53  ?  96   VAL   A N    1 
ATOM   1979 C  CA   . VAL   A 1 96  ? 27.233 -3.403  -2.863  1.00 10.34 ?  96   VAL   A CA   1 
ATOM   1980 C  C    . VAL   A 1 96  ? 26.430 -4.457  -3.617  1.00 10.82 ?  96   VAL   A C    1 
ATOM   1981 O  O    . VAL   A 1 96  ? 26.991 -5.396  -4.189  1.00 11.63 ?  96   VAL   A O    1 
ATOM   1982 C  CB   . VAL   A 1 96  ? 28.423 -2.923  -3.695  1.00 10.73 ?  96   VAL   A CB   1 
ATOM   1983 C  CG1  . VAL   A 1 96  ? 27.907 -2.283  -4.964  1.00 10.81 ?  96   VAL   A CG1  1 
ATOM   1984 C  CG2  . VAL   A 1 96  ? 29.285 -1.955  -2.904  1.00 11.35 ?  96   VAL   A CG2  1 
ATOM   1985 H  H    . VAL   A 1 96  ? 28.341 -4.471  -1.634  1.00 11.43 ?  96   VAL   A H    1 
ATOM   1986 H  HA   . VAL   A 1 96  ? 26.655 -2.641  -2.703  1.00 12.41 ?  96   VAL   A HA   1 
ATOM   1987 H  HB   . VAL   A 1 96  ? 28.966 -3.685  -3.942  1.00 12.87 ?  96   VAL   A HB   1 
ATOM   1988 H  HG11 . VAL   A 1 96  ? 28.638 -1.810  -5.397  1.00 12.97 ?  96   VAL   A HG11 1 
ATOM   1989 H  HG12 . VAL   A 1 96  ? 27.565 -2.968  -5.558  1.00 12.97 ?  96   VAL   A HG12 1 
ATOM   1990 H  HG13 . VAL   A 1 96  ? 27.201 -1.653  -4.742  1.00 12.97 ?  96   VAL   A HG13 1 
ATOM   1991 H  HG21 . VAL   A 1 96  ? 29.981 -1.609  -3.481  1.00 13.62 ?  96   VAL   A HG21 1 
ATOM   1992 H  HG22 . VAL   A 1 96  ? 28.728 -1.227  -2.582  1.00 13.62 ?  96   VAL   A HG22 1 
ATOM   1993 H  HG23 . VAL   A 1 96  ? 29.678 -2.425  -2.152  1.00 13.62 ?  96   VAL   A HG23 1 
ATOM   1994 N  N    . GLY   A 1 97  ? 25.111 -4.302  -3.643  1.00 10.56 ?  97   GLY   A N    1 
ATOM   1995 C  CA   . GLY   A 1 97  ? 24.292 -5.061  -4.552  1.00 11.16 ?  97   GLY   A CA   1 
ATOM   1996 C  C    . GLY   A 1 97  ? 24.297 -4.405  -5.919  1.00 11.33 ?  97   GLY   A C    1 
ATOM   1997 O  O    . GLY   A 1 97  ? 24.585 -3.210  -6.055  1.00 12.32 ?  97   GLY   A O    1 
ATOM   1998 H  H    . GLY   A 1 97  ? 24.669 -3.753  -3.136  1.00 12.67 ?  97   GLY   A H    1 
ATOM   1999 H  HA2  . GLY   A 1 97  ? 24.643 -5.961  -4.611  1.00 13.38 ?  97   GLY   A HA2  1 
ATOM   2000 H  HA3  . GLY   A 1 97  ? 23.378 -5.103  -4.218  1.00 13.38 ?  97   GLY   A HA3  1 
ATOM   2001 N  N    A PRO   A 1 98  ? 23.910 -5.127  -6.964  0.50 10.93 ?  98   PRO   A N    1 
ATOM   2002 N  N    B PRO   A 1 98  ? 24.040 -5.207  -6.954  0.50 11.63 ?  98   PRO   A N    1 
ATOM   2003 C  CA   A PRO   A 1 98  ? 23.771 -4.470  -8.271  0.50 11.51 ?  98   PRO   A CA   1 
ATOM   2004 C  CA   B PRO   A 1 98  ? 24.006 -4.673  -8.316  0.50 12.61 ?  98   PRO   A CA   1 
ATOM   2005 C  C    A PRO   A 1 98  ? 22.669 -3.415  -8.263  0.50 10.79 ?  98   PRO   A C    1 
ATOM   2006 C  C    B PRO   A 1 98  ? 22.888 -3.660  -8.482  0.50 13.04 ?  98   PRO   A C    1 
ATOM   2007 O  O    A PRO   A 1 98  ? 21.612 -3.597  -7.656  0.50 10.43 ?  98   PRO   A O    1 
ATOM   2008 O  O    B PRO   A 1 98  ? 21.784 -3.817  -7.955  0.50 13.29 ?  98   PRO   A O    1 
ATOM   2009 C  CB   A PRO   A 1 98  ? 23.436 -5.628  -9.217  0.50 11.58 ?  98   PRO   A CB   1 
ATOM   2010 C  CB   B PRO   A 1 98  ? 23.759 -5.916  -9.179  0.50 12.68 ?  98   PRO   A CB   1 
ATOM   2011 C  CG   A PRO   A 1 98  ? 22.834 -6.677  -8.338  0.50 11.75 ?  98   PRO   A CG   1 
ATOM   2012 C  CG   B PRO   A 1 98  ? 23.100 -6.895  -8.258  0.50 12.92 ?  98   PRO   A CG   1 
ATOM   2013 C  CD   A PRO   A 1 98  ? 23.562 -6.558  -7.022  0.50 11.30 ?  98   PRO   A CD   1 
ATOM   2014 C  CD   B PRO   A 1 98  ? 23.752 -6.653  -6.923  0.50 11.89 ?  98   PRO   A CD   1 
ATOM   2015 H  HA   A PRO   A 1 98  ? 24.608 -4.062  -8.529  0.50 13.81 ?  98   PRO   A HA   1 
ATOM   2016 H  HA   B PRO   A 1 98  ? 24.858 -4.271  -8.546  0.50 15.12 ?  98   PRO   A HA   1 
ATOM   2017 H  HB2  A PRO   A 1 98  ? 22.798 -5.330  -9.884  0.50 13.89 ?  98   PRO   A HB2  1 
ATOM   2018 H  HB2  B PRO   A 1 98  ? 23.169 -5.684  -9.914  0.50 15.21 ?  98   PRO   A HB2  1 
ATOM   2019 H  HB3  A PRO   A 1 98  ? 24.249 -5.950  -9.634  0.50 13.89 ?  98   PRO   A HB3  1 
ATOM   2020 H  HB3  B PRO   A 1 98  ? 24.600 -6.262  -9.505  0.50 15.21 ?  98   PRO   A HB3  1 
ATOM   2021 H  HG2  A PRO   A 1 98  ? 21.887 -6.506  -8.222  0.50 14.09 ?  98   PRO   A HG2  1 
ATOM   2022 H  HG2  B PRO   A 1 98  ? 22.146 -6.716  -8.216  0.50 15.50 ?  98   PRO   A HG2  1 
ATOM   2023 H  HG3  A PRO   A 1 98  ? 22.980 -7.553  -8.728  0.50 14.09 ?  98   PRO   A HG3  1 
ATOM   2024 H  HG3  B PRO   A 1 98  ? 23.266 -7.799  -8.570  0.50 15.50 ?  98   PRO   A HG3  1 
ATOM   2025 H  HD2  A PRO   A 1 98  ? 22.973 -6.802  -6.285  0.50 13.55 ?  98   PRO   A HD2  1 
ATOM   2026 H  HD2  B PRO   A 1 98  ? 23.135 -6.866  -6.202  0.50 14.26 ?  98   PRO   A HD2  1 
ATOM   2027 H  HD3  A PRO   A 1 98  ? 24.367 -7.096  -7.024  0.50 13.55 ?  98   PRO   A HD3  1 
ATOM   2028 H  HD3  B PRO   A 1 98  ? 24.573 -7.168  -6.847  0.50 14.26 ?  98   PRO   A HD3  1 
ATOM   2029 N  N    A ASN   A 1 99  ? 22.931 -2.298  -8.951  0.50 11.67 ?  99   ASN   A N    1 
ATOM   2030 N  N    B ASN   A 1 99  ? 23.185 -2.615  -9.227  0.50 13.44 ?  99   ASN   A N    1 
ATOM   2031 C  CA   A ASN   A 1 99  ? 21.955 -1.225  -9.139  0.50 12.17 ?  99   ASN   A CA   1 
ATOM   2032 C  CA   B ASN   A 1 99  ? 22.219 -1.579  -9.549  0.50 14.86 ?  99   ASN   A CA   1 
ATOM   2033 C  C    A ASN   A 1 99  ? 21.396 -1.332  -10.556 0.50 12.52 ?  99   ASN   A C    1 
ATOM   2034 C  C    B ASN   A 1 99  ? 21.654 -1.897  -10.929 0.50 15.33 ?  99   ASN   A C    1 
ATOM   2035 O  O    A ASN   A 1 99  ? 22.077 -0.987  -11.532 0.50 13.60 ?  99   ASN   A O    1 
ATOM   2036 O  O    B ASN   A 1 99  ? 22.349 -1.766  -11.941 0.50 15.24 ?  99   ASN   A O    1 
ATOM   2037 C  CB   A ASN   A 1 99  ? 22.603 0.139   -8.905  0.50 11.45 ?  99   ASN   A CB   1 
ATOM   2038 C  CB   B ASN   A 1 99  ? 22.908 -0.220  -9.532  0.50 16.34 ?  99   ASN   A CB   1 
ATOM   2039 C  CG   A ASN   A 1 99  ? 21.594 1.288   -8.924  0.50 11.55 ?  99   ASN   A CG   1 
ATOM   2040 C  CG   B ASN   A 1 99  ? 21.946 0.922   -9.757  0.50 17.93 ?  99   ASN   A CG   1 
ATOM   2041 O  OD1  A ASN   A 1 99  ? 20.611 1.260   -9.663  0.50 12.51 ?  99   ASN   A OD1  1 
ATOM   2042 O  OD1  B ASN   A 1 99  ? 20.910 0.758   -10.398 0.50 18.24 ?  99   ASN   A OD1  1 
ATOM   2043 N  ND2  A ASN   A 1 99  ? 21.849 2.306   -8.116  0.50 11.69 ?  99   ASN   A ND2  1 
ATOM   2044 N  ND2  B ASN   A 1 99  ? 22.284 2.092   -9.228  0.50 19.30 ?  99   ASN   A ND2  1 
ATOM   2045 H  H    A ASN   A 1 99  ? 23.690 -2.132  -9.313  0.50 14.00 ?  99   ASN   A H    1 
ATOM   2046 H  H    B ASN   A 1 99  ? 23.968 -2.472  -9.549  0.50 16.13 ?  99   ASN   A H    1 
ATOM   2047 H  HA   A ASN   A 1 99  ? 21.225 -1.333  -8.502  0.50 14.59 ?  99   ASN   A HA   1 
ATOM   2048 H  HA   B ASN   A 1 99  ? 21.497 -1.579  -8.889  0.50 17.83 ?  99   ASN   A HA   1 
ATOM   2049 H  HB2  A ASN   A 1 99  ? 23.043 0.141   -8.042  0.50 13.74 ?  99   ASN   A HB2  1 
ATOM   2050 H  HB2  B ASN   A 1 99  ? 23.340 -0.088  -8.670  0.50 19.60 ?  99   ASN   A HB2  1 
ATOM   2051 H  HB3  A ASN   A 1 99  ? 23.251 0.302   -9.609  0.50 13.74 ?  99   ASN   A HB3  1 
ATOM   2052 H  HB3  B ASN   A 1 99  ? 23.564 -0.199  -10.240 0.50 19.60 ?  99   ASN   A HB3  1 
ATOM   2053 H  HD21 A ASN   A 1 99  ? 21.310 2.977   -8.087  0.50 14.02 ?  99   ASN   A HD21 1 
ATOM   2054 H  HD21 B ASN   A 1 99  ? 21.772 2.776   -9.327  0.50 23.15 ?  99   ASN   A HD21 1 
ATOM   2055 H  HD22 A ASN   A 1 99  ? 22.547 2.294   -7.616  0.50 14.02 ?  99   ASN   A HD22 1 
ATOM   2056 H  HD22 B ASN   A 1 99  ? 23.023 2.170   -8.793  0.50 23.15 ?  99   ASN   A HD22 1 
ATOM   2057 N  N    A VAL   A 1 100 ? 20.152 -1.816  -10.658 0.50 12.73 ?  100  VAL   A N    1 
ATOM   2058 N  N    B VAL   A 1 100 ? 20.392 -2.327  -10.960 0.50 17.12 ?  100  VAL   A N    1 
ATOM   2059 C  CA   A VAL   A 1 100 ? 19.523 -2.045  -11.956 0.50 14.22 ?  100  VAL   A CA   1 
ATOM   2060 C  CA   B VAL   A 1 100 ? 19.773 -2.743  -12.214 0.50 19.33 ?  100  VAL   A CA   1 
ATOM   2061 C  C    A VAL   A 1 100 ? 19.416 -0.749  -12.740 0.50 14.48 ?  100  VAL   A C    1 
ATOM   2062 C  C    B VAL   A 1 100 ? 19.691 -1.583  -13.192 0.50 20.32 ?  100  VAL   A C    1 
ATOM   2063 O  O    A VAL   A 1 100 ? 19.506 -0.748  -13.972 0.50 15.11 ?  100  VAL   A O    1 
ATOM   2064 O  O    B VAL   A 1 100 ? 19.695 -1.788  -14.412 0.50 20.71 ?  100  VAL   A O    1 
ATOM   2065 C  CB   A VAL   A 1 100 ? 18.156 -2.739  -11.766 0.50 16.12 ?  100  VAL   A CB   1 
ATOM   2066 C  CB   B VAL   A 1 100 ? 18.389 -3.352  -11.933 0.50 20.62 ?  100  VAL   A CB   1 
ATOM   2067 C  CG1  A VAL   A 1 100 ? 17.433 -2.910  -13.096 0.50 16.58 ?  100  VAL   A CG1  1 
ATOM   2068 C  CG1  B VAL   A 1 100 ? 17.694 -3.716  -13.233 0.50 20.98 ?  100  VAL   A CG1  1 
ATOM   2069 C  CG2  A VAL   A 1 100 ? 18.346 -4.091  -11.094 0.50 16.91 ?  100  VAL   A CG2  1 
ATOM   2070 C  CG2  B VAL   A 1 100 ? 18.532 -4.566  -11.039 0.50 21.13 ?  100  VAL   A CG2  1 
ATOM   2071 H  H    A VAL   A 1 100 ? 19.647 -2.021  -9.982  0.50 15.27 ?  100  VAL   A H    1 
ATOM   2072 H  H    B VAL   A 1 100 ? 19.884 -2.395  -10.267 0.50 20.54 ?  100  VAL   A H    1 
ATOM   2073 H  HA   A VAL   A 1 100 ? 20.078 -2.651  -12.465 0.50 17.06 ?  100  VAL   A HA   1 
ATOM   2074 H  HA   B VAL   A 1 100 ? 20.326 -3.433  -12.613 0.50 23.19 ?  100  VAL   A HA   1 
ATOM   2075 H  HB   A VAL   A 1 100 ? 17.595 -2.201  -11.187 0.50 19.34 ?  100  VAL   A HB   1 
ATOM   2076 H  HB   B VAL   A 1 100 ? 17.845 -2.693  -11.472 0.50 24.73 ?  100  VAL   A HB   1 
ATOM   2077 H  HG11 A VAL   A 1 100 ? 16.684 -3.519  -12.976 0.50 19.89 ?  100  VAL   A HG11 1 
ATOM   2078 H  HG11 B VAL   A 1 100 ? 16.924 -4.267  -13.030 0.50 25.17 ?  100  VAL   A HG11 1 
ATOM   2079 H  HG12 A VAL   A 1 100 ? 17.108 -2.047  -13.392 0.50 19.89 ?  100  VAL   A HG12 1 
ATOM   2080 H  HG12 B VAL   A 1 100 ? 17.410 -2.904  -13.683 0.50 25.17 ?  100  VAL   A HG12 1 
ATOM   2081 H  HG13 A VAL   A 1 100 ? 18.051 -3.277  -13.747 0.50 19.89 ?  100  VAL   A HG13 1 
ATOM   2082 H  HG13 B VAL   A 1 100 ? 18.314 -4.207  -13.795 0.50 25.17 ?  100  VAL   A HG13 1 
ATOM   2083 H  HG21 A VAL   A 1 100 ? 17.488 -4.544  -11.036 0.50 20.28 ?  100  VAL   A HG21 1 
ATOM   2084 H  HG21 B VAL   A 1 100 ? 17.663 -4.979  -10.934 0.50 25.36 ?  100  VAL   A HG21 1 
ATOM   2085 H  HG22 A VAL   A 1 100 ? 18.963 -4.624  -11.620 0.50 20.28 ?  100  VAL   A HG22 1 
ATOM   2086 H  HG22 B VAL   A 1 100 ? 19.150 -5.187  -11.453 0.50 25.36 ?  100  VAL   A HG22 1 
ATOM   2087 H  HG23 A VAL   A 1 100 ? 18.705 -3.955  -10.202 0.50 20.28 ?  100  VAL   A HG23 1 
ATOM   2088 H  HG23 B VAL   A 1 100 ? 18.873 -4.284  -10.176 0.50 25.36 ?  100  VAL   A HG23 1 
ATOM   2089 N  N    A ASN   A 1 101 ? 19.226 0.372   -12.054 0.50 15.49 ?  101  ASN   A N    1 
ATOM   2090 N  N    B ASN   A 1 101 ? 19.594 -0.353  -12.685 0.50 21.39 ?  101  ASN   A N    1 
ATOM   2091 C  CA   A ASN   A 1 101 ? 19.164 1.646   -12.755 0.50 16.74 ?  101  ASN   A CA   1 
ATOM   2092 C  CA   B ASN   A 1 101 ? 19.534 0.809   -13.563 0.50 22.73 ?  101  ASN   A CA   1 
ATOM   2093 C  C    A ASN   A 1 101 ? 20.522 2.090   -13.296 0.50 18.73 ?  101  ASN   A C    1 
ATOM   2094 C  C    B ASN   A 1 101 ? 20.857 1.073   -14.271 0.50 24.02 ?  101  ASN   A C    1 
ATOM   2095 O  O    A ASN   A 1 101 ? 20.593 3.141   -13.946 0.50 20.32 ?  101  ASN   A O    1 
ATOM   2096 O  O    B ASN   A 1 101 ? 20.864 1.744   -15.310 0.50 24.39 ?  101  ASN   A O    1 
ATOM   2097 C  CB   A ASN   A 1 101 ? 18.534 2.695   -11.842 0.50 16.45 ?  101  ASN   A CB   1 
ATOM   2098 C  CB   B ASN   A 1 101 ? 19.106 2.039   -12.765 0.50 23.06 ?  101  ASN   A CB   1 
ATOM   2099 C  CG   A ASN   A 1 101 ? 17.179 2.252   -11.312 0.50 16.01 ?  101  ASN   A CG   1 
ATOM   2100 C  CG   B ASN   A 1 101 ? 17.828 1.806   -11.978 0.50 23.69 ?  101  ASN   A CG   1 
ATOM   2101 O  OD1  A ASN   A 1 101 ? 16.349 1.714   -12.055 0.50 16.67 ?  101  ASN   A OD1  1 
ATOM   2102 O  OD1  B ASN   A 1 101 ? 16.878 1.195   -12.474 0.50 24.49 ?  101  ASN   A OD1  1 
ATOM   2103 N  ND2  A ASN   A 1 101 ? 16.961 2.445   -10.019 0.50 16.13 ?  101  ASN   A ND2  1 
ATOM   2104 N  ND2  B ASN   A 1 101 ? 17.804 2.281   -10.741 0.50 24.01 ?  101  ASN   A ND2  1 
ATOM   2105 H  H    A ASN   A 1 101 ? 19.127 0.419   -11.205 0.50 18.59 ?  101  ASN   A H    1 
ATOM   2106 H  H    B ASN   A 1 101 ? 19.546 -0.169  -11.844 0.50 25.66 ?  101  ASN   A H    1 
ATOM   2107 H  HA   A ASN   A 1 101 ? 18.575 1.542   -13.520 0.50 20.09 ?  101  ASN   A HA   1 
ATOM   2108 H  HA   B ASN   A 1 101 ? 18.863 0.650   -14.241 0.50 27.27 ?  101  ASN   A HA   1 
ATOM   2109 H  HB2  A ASN   A 1 101 ? 19.119 2.854   -11.089 0.50 19.74 ?  101  ASN   A HB2  1 
ATOM   2110 H  HB2  B ASN   A 1 101 ? 19.808 2.273   -12.138 0.50 27.66 ?  101  ASN   A HB2  1 
ATOM   2111 H  HB3  A ASN   A 1 101 ? 18.409 3.517   -12.349 0.50 19.74 ?  101  ASN   A HB3  1 
ATOM   2112 H  HB3  B ASN   A 1 101 ? 18.954 2.777   -13.380 0.50 27.66 ?  101  ASN   A HB3  1 
ATOM   2113 H  HD21 A ASN   A 1 101 ? 16.218 2.217   -9.669  0.50 19.35 ?  101  ASN   A HD21 1 
ATOM   2114 H  HD21 B ASN   A 1 101 ? 17.103 2.176   -10.256 0.50 28.81 ?  101  ASN   A HD21 1 
ATOM   2115 H  HD22 A ASN   A 1 101 ? 17.562 2.820   -9.536  0.50 19.35 ?  101  ASN   A HD22 1 
ATOM   2116 H  HD22 B ASN   A 1 101 ? 18.487 2.698   -10.426 0.50 28.81 ?  101  ASN   A HD22 1 
ATOM   2117 N  N    A LYS   A 1 102 ? 21.581 1.308   -13.064 0.50 20.35 ?  102  LYS   A N    1 
ATOM   2118 N  N    B LYS   A 1 102 ? 21.970 0.572   -13.737 0.50 25.22 ?  102  LYS   A N    1 
ATOM   2119 C  CA   A LYS   A 1 102 ? 22.870 1.487   -13.720 0.50 21.72 ?  102  LYS   A CA   1 
ATOM   2120 C  CA   B LYS   A 1 102 ? 23.280 0.712   -14.361 0.50 26.12 ?  102  LYS   A CA   1 
ATOM   2121 C  C    A LYS   A 1 102 ? 23.169 0.395   -14.738 0.50 22.51 ?  102  LYS   A C    1 
ATOM   2122 C  C    B LYS   A 1 102 ? 23.625 -0.462  -15.269 0.50 25.47 ?  102  LYS   A C    1 
ATOM   2123 O  O    A LYS   A 1 102 ? 24.237 0.425   -15.358 0.50 23.40 ?  102  LYS   A O    1 
ATOM   2124 O  O    B LYS   A 1 102 ? 24.765 -0.552  -15.737 0.50 25.77 ?  102  LYS   A O    1 
ATOM   2125 C  CB   A LYS   A 1 102 ? 24.002 1.527   -12.685 0.50 22.87 ?  102  LYS   A CB   1 
ATOM   2126 C  CB   B LYS   A 1 102 ? 24.373 0.847   -13.294 0.50 27.61 ?  102  LYS   A CB   1 
ATOM   2127 C  CG   A LYS   A 1 102 ? 23.898 2.654   -11.675 0.50 23.94 ?  102  LYS   A CG   1 
ATOM   2128 C  CG   B LYS   A 1 102 ? 24.245 2.056   -12.385 0.50 29.22 ?  102  LYS   A CG   1 
ATOM   2129 C  CD   A LYS   A 1 102 ? 25.079 2.633   -10.715 0.50 25.28 ?  102  LYS   A CD   1 
ATOM   2130 C  CD   B LYS   A 1 102 ? 25.288 2.001   -11.273 0.50 30.98 ?  102  LYS   A CD   1 
ATOM   2131 C  CE   A LYS   A 1 102 ? 25.013 3.778   -9.716  0.50 26.28 ?  102  LYS   A CE   1 
ATOM   2132 C  CE   B LYS   A 1 102 ? 25.171 3.189   -10.333 0.50 32.38 ?  102  LYS   A CE   1 
ATOM   2133 N  NZ   A LYS   A 1 102 ? 26.152 3.735   -8.755  0.50 26.74 ?  102  LYS   A NZ   1 
ATOM   2134 N  NZ   B LYS   A 1 102 ? 25.684 2.872   -8.968  0.50 33.35 ?  102  LYS   A NZ   1 
ATOM   2135 H  H    A LYS   A 1 102 ? 21.573 0.641   -12.518 0.50 24.41 ?  102  LYS   A H    1 
ATOM   2136 H  H    B LYS   A 1 102 ? 21.992 0.137   -12.995 0.50 30.25 ?  102  LYS   A H    1 
ATOM   2137 H  HA   A LYS   A 1 102 ? 22.869 2.327   -14.194 0.50 26.06 ?  102  LYS   A HA   1 
ATOM   2138 H  HA   B LYS   A 1 102 ? 23.290 1.522   -14.891 0.50 31.34 ?  102  LYS   A HA   1 
ATOM   2139 H  HB2  A LYS   A 1 102 ? 24.002 0.690   -12.194 0.50 27.43 ?  102  LYS   A HB2  1 
ATOM   2140 H  HB2  B LYS   A 1 102 ? 24.345 0.063   -12.727 0.50 33.12 ?  102  LYS   A HB2  1 
ATOM   2141 H  HB3  A LYS   A 1 102 ? 24.845 1.628   -13.154 0.50 27.43 ?  102  LYS   A HB3  1 
ATOM   2142 H  HB3  B LYS   A 1 102 ? 25.239 0.899   -13.736 0.50 33.12 ?  102  LYS   A HB3  1 
ATOM   2143 H  HG2  A LYS   A 1 102 ? 23.895 3.504   -12.143 0.50 28.73 ?  102  LYS   A HG2  1 
ATOM   2144 H  HG2  B LYS   A 1 102 ? 24.386 2.866   -12.900 0.50 35.06 ?  102  LYS   A HG2  1 
ATOM   2145 H  HG3  A LYS   A 1 102 ? 23.081 2.549   -11.161 0.50 28.73 ?  102  LYS   A HG3  1 
ATOM   2146 H  HG3  B LYS   A 1 102 ? 23.363 2.062   -11.979 0.50 35.06 ?  102  LYS   A HG3  1 
ATOM   2147 H  HD2  A LYS   A 1 102 ? 25.074 1.798   -10.221 0.50 30.33 ?  102  LYS   A HD2  1 
ATOM   2148 H  HD2  B LYS   A 1 102 ? 25.166 1.189   -10.756 0.50 37.17 ?  102  LYS   A HD2  1 
ATOM   2149 H  HD3  A LYS   A 1 102 ? 25.903 2.717   -11.221 0.50 30.33 ?  102  LYS   A HD3  1 
ATOM   2150 H  HD3  B LYS   A 1 102 ? 26.174 2.012   -11.669 0.50 37.17 ?  102  LYS   A HD3  1 
ATOM   2151 H  HE2  A LYS   A 1 102 ? 25.050 4.621   -10.196 0.50 31.53 ?  102  LYS   A HE2  1 
ATOM   2152 H  HE2  B LYS   A 1 102 ? 25.694 3.926   -10.688 0.50 38.85 ?  102  LYS   A HE2  1 
ATOM   2153 H  HE3  A LYS   A 1 102 ? 24.186 3.715   -9.213  0.50 31.53 ?  102  LYS   A HE3  1 
ATOM   2154 H  HE3  B LYS   A 1 102 ? 24.240 3.447   -10.257 0.50 38.85 ?  102  LYS   A HE3  1 
ATOM   2155 H  HZ1  A LYS   A 1 102 ? 26.092 4.413   -8.183  0.50 32.08 ?  102  LYS   A HZ1  1 
ATOM   2156 H  HZ1  B LYS   A 1 102 ? 25.600 3.583   -8.439  0.50 40.01 ?  102  LYS   A HZ1  1 
ATOM   2157 H  HZ2  A LYS   A 1 102 ? 26.137 2.970   -8.301  0.50 32.08 ?  102  LYS   A HZ2  1 
ATOM   2158 H  HZ2  B LYS   A 1 102 ? 25.221 2.196   -8.619  0.50 40.01 ?  102  LYS   A HZ2  1 
ATOM   2159 H  HZ3  A LYS   A 1 102 ? 26.923 3.795   -9.196  0.50 32.08 ?  102  LYS   A HZ3  1 
ATOM   2160 H  HZ3  B LYS   A 1 102 ? 26.543 2.643   -9.011  0.50 40.01 ?  102  LYS   A HZ3  1 
ATOM   2161 N  N    A GLY   A 1 103 ? 22.263 -0.565  -14.926 0.50 23.33 ?  103  GLY   A N    1 
ATOM   2162 N  N    B GLY   A 1 103 ? 22.683 -1.369  -15.520 0.50 24.72 ?  103  GLY   A N    1 
ATOM   2163 C  CA   A GLY   A 1 103 ? 22.485 -1.658  -15.854 0.50 24.22 ?  103  GLY   A CA   1 
ATOM   2164 C  CA   B GLY   A 1 103 ? 22.978 -2.547  -16.308 0.50 24.12 ?  103  GLY   A CA   1 
ATOM   2165 C  C    A GLY   A 1 103 ? 23.331 -2.788  -15.317 0.50 24.88 ?  103  GLY   A C    1 
ATOM   2166 C  C    B GLY   A 1 103 ? 23.748 -3.620  -15.577 0.50 23.21 ?  103  GLY   A C    1 
ATOM   2167 O  O    A GLY   A 1 103 ? 23.822 -3.603  -16.103 0.50 25.89 ?  103  GLY   A O    1 
ATOM   2168 O  O    B GLY   A 1 103 ? 24.248 -4.550  -16.220 0.50 23.88 ?  103  GLY   A O    1 
ATOM   2169 H  H    A GLY   A 1 103 ? 21.507 -0.606  -14.527 0.50 27.99 ?  103  GLY   A H    1 
ATOM   2170 H  H    B GLY   A 1 103 ? 21.869 -1.314  -15.248 0.50 29.66 ?  103  GLY   A H    1 
ATOM   2171 H  HA2  A GLY   A 1 103 ? 21.624 -2.019  -16.132 0.50 29.06 ?  103  GLY   A HA2  1 
ATOM   2172 H  HA2  B GLY   A 1 103 ? 22.154 -2.942  -16.628 0.50 28.94 ?  103  GLY   A HA2  1 
ATOM   2173 H  HA3  A GLY   A 1 103 ? 22.933 -1.321  -16.644 0.50 29.06 ?  103  GLY   A HA3  1 
ATOM   2174 H  HA3  B GLY   A 1 103 ? 23.504 -2.275  -17.077 0.50 28.94 ?  103  GLY   A HA3  1 
ATOM   2175 N  N    A GLU   A 1 104 ? 23.520 -2.864  -14.003 0.50 24.14 ?  104  GLU   A N    1 
ATOM   2176 N  N    B GLU   A 1 104 ? 23.851 -3.529  -14.257 0.50 21.46 ?  104  GLU   A N    1 
ATOM   2177 C  CA   A GLU   A 1 104 ? 24.378 -3.880  -13.414 0.50 23.74 ?  104  GLU   A CA   1 
ATOM   2178 C  CA   B GLU   A 1 104 ? 24.690 -4.447  -13.504 0.50 19.52 ?  104  GLU   A CA   1 
ATOM   2179 C  C    A GLU   A 1 104 ? 23.672 -5.231  -13.346 0.50 24.07 ?  104  GLU   A C    1 
ATOM   2180 C  C    B GLU   A 1 104 ? 23.994 -5.792  -13.335 0.50 19.06 ?  104  GLU   A C    1 
ATOM   2181 O  O    A GLU   A 1 104 ? 22.452 -5.318  -13.174 0.50 24.14 ?  104  GLU   A O    1 
ATOM   2182 O  O    B GLU   A 1 104 ? 22.773 -5.868  -13.159 0.50 19.24 ?  104  GLU   A O    1 
ATOM   2183 C  CB   A GLU   A 1 104 ? 24.862 -3.422  -12.033 0.50 22.97 ?  104  GLU   A CB   1 
ATOM   2184 C  CB   B GLU   A 1 104 ? 25.068 -3.828  -12.156 0.50 18.69 ?  104  GLU   A CB   1 
ATOM   2185 C  CG   A GLU   A 1 104 ? 25.928 -2.325  -12.150 0.50 22.62 ?  104  GLU   A CG   1 
ATOM   2186 C  CG   B GLU   A 1 104 ? 25.780 -2.485  -12.334 0.50 18.68 ?  104  GLU   A CG   1 
ATOM   2187 C  CD   A GLU   A 1 104 ? 26.150 -1.495  -10.898 0.50 22.02 ?  104  GLU   A CD   1 
ATOM   2188 C  CD   B GLU   A 1 104 ? 26.251 -1.815  -11.056 0.50 17.84 ?  104  GLU   A CD   1 
ATOM   2189 O  OE1  A GLU   A 1 104 ? 25.502 -1.749  -9.865  0.50 20.82 ?  104  GLU   A OE1  1 
ATOM   2190 O  OE1  B GLU   A 1 104 ? 25.750 -2.133  -9.960  0.50 17.19 ?  104  GLU   A OE1  1 
ATOM   2191 O  OE2  A GLU   A 1 104 ? 26.981 -0.560  -10.965 0.50 22.82 -1 104  GLU   A OE2  1 
ATOM   2192 O  OE2  B GLU   A 1 104 ? 27.131 -0.933  -11.170 0.50 18.50 -1 104  GLU   A OE2  1 
ATOM   2193 H  H    A GLU   A 1 104 ? 23.169 -2.332  -13.433 0.50 28.96 ?  104  GLU   A H    1 
ATOM   2194 H  H    B GLU   A 1 104 ? 23.439 -2.942  -13.783 0.50 25.74 ?  104  GLU   A H    1 
ATOM   2195 H  HA   A GLU   A 1 104 ? 25.158 -3.992  -13.975 0.50 28.48 ?  104  GLU   A HA   1 
ATOM   2196 H  HA   B GLU   A 1 104 ? 25.511 -4.594  -14.000 0.50 23.42 ?  104  GLU   A HA   1 
ATOM   2197 H  HB2  A GLU   A 1 104 ? 24.108 -3.071  -11.534 0.50 27.56 ?  104  GLU   A HB2  1 
ATOM   2198 H  HB2  B GLU   A 1 104 ? 24.265 -3.682  -11.637 0.50 22.42 ?  104  GLU   A HB2  1 
ATOM   2199 H  HB3  A GLU   A 1 104 ? 25.249 -4.180  -11.564 0.50 27.56 ?  104  GLU   A HB3  1 
ATOM   2200 H  HB3  B GLU   A 1 104 ? 25.668 -4.430  -11.691 0.50 22.42 ?  104  GLU   A HB3  1 
ATOM   2201 H  HG2  A GLU   A 1 104 ? 26.768 -2.741  -12.383 0.50 27.14 ?  104  GLU   A HG2  1 
ATOM   2202 H  HG2  B GLU   A 1 104 ? 26.560 -2.618  -12.890 0.50 22.41 ?  104  GLU   A HG2  1 
ATOM   2203 H  HG3  A GLU   A 1 104 ? 25.656 -1.710  -12.844 0.50 27.14 ?  104  GLU   A HG3  1 
ATOM   2204 H  HG3  B GLU   A 1 104 ? 25.171 -1.869  -12.764 0.50 22.41 ?  104  GLU   A HG3  1 
ATOM   2205 N  N    A ASP   A 1 105 ? 24.466 -6.291  -13.493 0.50 24.91 ?  105  ASP   A N    1 
ATOM   2206 N  N    B ASP   A 1 105 ? 24.793 -6.856  -13.405 0.50 19.94 ?  105  ASP   A N    1 
ATOM   2207 C  CA   A ASP   A 1 105 ? 23.944 -7.647  -13.604 0.50 25.78 ?  105  ASP   A CA   1 
ATOM   2208 C  CA   B ASP   A 1 105 ? 24.331 -8.238  -13.429 0.50 20.69 ?  105  ASP   A CA   1 
ATOM   2209 C  C    A ASP   A 1 105 ? 23.291 -8.076  -12.295 0.50 24.46 ?  105  ASP   A C    1 
ATOM   2210 C  C    B ASP   A 1 105 ? 23.534 -8.598  -12.180 0.50 19.33 ?  105  ASP   A C    1 
ATOM   2211 O  O    A ASP   A 1 105 ? 23.905 -7.992  -11.229 0.50 23.19 ?  105  ASP   A O    1 
ATOM   2212 O  O    B ASP   A 1 105 ? 24.096 -8.664  -11.085 0.50 17.23 ?  105  ASP   A O    1 
ATOM   2213 C  CB   A ASP   A 1 105 ? 25.093 -8.594  -13.949 0.50 27.91 ?  105  ASP   A CB   1 
ATOM   2214 C  CB   B ASP   A 1 105 ? 25.559 -9.145  -13.550 0.50 22.78 ?  105  ASP   A CB   1 
ATOM   2215 C  CG   A ASP   A 1 105 ? 24.616 -10.003 -14.223 0.50 29.65 ?  105  ASP   A CG   1 
ATOM   2216 C  CG   B ASP   A 1 105 ? 25.205 -10.587 -13.816 0.50 24.48 ?  105  ASP   A CG   1 
ATOM   2217 O  OD1  A ASP   A 1 105 ? 23.384 -10.209 -14.261 0.50 29.68 ?  105  ASP   A OD1  1 
ATOM   2218 O  OD1  B ASP   A 1 105 ? 24.006 -10.879 -13.993 0.50 24.86 ?  105  ASP   A OD1  1 
ATOM   2219 O  OD2  A ASP   A 1 105 ? 25.466 -10.898 -14.408 0.50 30.87 -1 105  ASP   A OD2  1 
ATOM   2220 O  OD2  B ASP   A 1 105 ? 26.136 -11.425 -13.855 0.50 25.52 -1 105  ASP   A OD2  1 
ATOM   2221 H  H    A ASP   A 1 105 ? 25.323 -6.255  -13.529 0.50 29.89 ?  105  ASP   A H    1 
ATOM   2222 H  H    B ASP   A 1 105 ? 25.648 -6.789  -13.445 0.50 23.92 ?  105  ASP   A H    1 
ATOM   2223 H  HA   A ASP   A 1 105 ? 23.288 -7.706  -14.316 0.50 30.93 ?  105  ASP   A HA   1 
ATOM   2224 H  HA   B ASP   A 1 105 ? 23.767 -8.376  -14.203 0.50 24.82 ?  105  ASP   A HA   1 
ATOM   2225 H  HB2  A ASP   A 1 105 ? 25.542 -8.279  -14.754 0.50 33.49 ?  105  ASP   A HB2  1 
ATOM   2226 H  HB2  B ASP   A 1 105 ? 26.114 -8.826  -14.279 0.50 27.33 ?  105  ASP   A HB2  1 
ATOM   2227 H  HB3  A ASP   A 1 105 ? 25.734 -8.607  -13.212 0.50 33.49 ?  105  ASP   A HB3  1 
ATOM   2228 H  HB3  B ASP   A 1 105 ? 26.056 -9.113  -12.720 0.50 27.33 ?  105  ASP   A HB3  1 
ATOM   2229 N  N    A ILE   A 1 106 ? 22.047 -8.557  -12.380 0.50 24.20 ?  106  ILE   A N    1 
ATOM   2230 N  N    B ILE   A 1 106 ? 22.227 -8.838  -12.327 0.50 20.31 ?  106  ILE   A N    1 
ATOM   2231 C  CA   A ILE   A 1 106 ? 21.312 -8.951  -11.182 0.50 23.39 ?  106  ILE   A CA   1 
ATOM   2232 C  CA   B ILE   A 1 106 ? 21.412 -9.207  -11.170 0.50 21.11 ?  106  ILE   A CA   1 
ATOM   2233 C  C    A ILE   A 1 106 ? 21.852 -10.243 -10.581 0.50 22.36 ?  106  ILE   A C    1 
ATOM   2234 C  C    B ILE   A 1 106 ? 21.919 -10.491 -10.535 0.50 21.43 ?  106  ILE   A C    1 
ATOM   2235 O  O    A ILE   A 1 106 ? 21.625 -10.505 -9.395  0.50 21.43 ?  106  ILE   A O    1 
ATOM   2236 O  O    B ILE   A 1 106 ? 21.718 -10.715 -9.335  0.50 21.53 ?  106  ILE   A O    1 
ATOM   2237 C  CB   A ILE   A 1 106 ? 19.800 -9.037  -11.477 0.50 24.68 ?  106  ILE   A CB   1 
ATOM   2238 C  CB   B ILE   A 1 106 ? 19.911 -9.275  -11.528 0.50 22.81 ?  106  ILE   A CB   1 
ATOM   2239 C  CG1  A ILE   A 1 106 ? 18.989 -9.117  -10.179 0.50 25.29 ?  106  ILE   A CG1  1 
ATOM   2240 C  CG1  B ILE   A 1 106 ? 19.054 -9.321  -10.258 0.50 23.77 ?  106  ILE   A CG1  1 
ATOM   2241 C  CG2  A ILE   A 1 106 ? 19.492 -10.235 -12.365 0.50 25.18 ?  106  ILE   A CG2  1 
ATOM   2242 C  CG2  B ILE   A 1 106 ? 19.609 -10.490 -12.386 0.50 23.27 ?  106  ILE   A CG2  1 
ATOM   2243 C  CD1  A ILE   A 1 106 ? 19.119 -7.894  -9.291  0.50 25.56 ?  106  ILE   A CD1  1 
ATOM   2244 C  CD1  B ILE   A 1 106 ? 19.185 -8.091  -9.381  0.50 24.20 ?  106  ILE   A CD1  1 
ATOM   2245 H  H    A ILE   A 1 106 ? 21.613 -8.662  -13.112 0.50 29.03 ?  106  ILE   A H    1 
ATOM   2246 H  H    B ILE   A 1 106 ? 21.799 -8.776  -13.064 0.50 24.36 ?  106  ILE   A H    1 
ATOM   2247 H  HA   A ILE   A 1 106 ? 21.440 -8.263  -10.519 0.50 28.06 ?  106  ILE   A HA   1 
ATOM   2248 H  HA   B ILE   A 1 106 ? 21.521 -8.522  -10.503 0.50 25.32 ?  106  ILE   A HA   1 
ATOM   2249 H  HB   A ILE   A 1 106 ? 19.538 -8.233  -11.951 0.50 29.60 ?  106  ILE   A HB   1 
ATOM   2250 H  HB   B ILE   A 1 106 ? 19.676 -8.477  -12.027 0.50 27.37 ?  106  ILE   A HB   1 
ATOM   2251 H  HG12 A ILE   A 1 106 ? 18.050 -9.215  -10.405 0.50 30.34 ?  106  ILE   A HG12 1 
ATOM   2252 H  HG12 B ILE   A 1 106 ? 18.122 -9.399  -10.513 0.50 28.52 ?  106  ILE   A HG12 1 
ATOM   2253 H  HG13 A ILE   A 1 106 ? 19.283 -9.886  -9.669  0.50 30.34 ?  106  ILE   A HG13 1 
ATOM   2254 H  HG13 B ILE   A 1 106 ? 19.315 -10.089 -9.729  0.50 28.52 ?  106  ILE   A HG13 1 
ATOM   2255 H  HG21 A ILE   A 1 106 ? 18.582 -10.158 -12.692 0.50 30.21 ?  106  ILE   A HG21 1 
ATOM   2256 H  HG21 B ILE   A 1 106 ? 18.723 -10.390 -12.768 0.50 27.92 ?  106  ILE   A HG21 1 
ATOM   2257 H  HG22 A ILE   A 1 106 ? 20.112 -10.240 -13.111 0.50 30.21 ?  106  ILE   A HG22 1 
ATOM   2258 H  HG22 B ILE   A 1 106 ? 20.271 -10.544 -13.090 0.50 27.92 ?  106  ILE   A HG22 1 
ATOM   2259 H  HG23 A ILE   A 1 106 ? 19.591 -11.048 -11.847 0.50 30.21 ?  106  ILE   A HG23 1 
ATOM   2260 H  HG23 B ILE   A 1 106 ? 19.644 -11.284 -11.832 0.50 27.92 ?  106  ILE   A HG23 1 
ATOM   2261 H  HD11 A ILE   A 1 106 ? 18.418 -7.915  -8.622  0.50 30.66 ?  106  ILE   A HD11 1 
ATOM   2262 H  HD11 B ILE   A 1 106 ? 18.446 -8.071  -8.755  0.50 29.03 ?  106  ILE   A HD11 1 
ATOM   2263 H  HD12 A ILE   A 1 106 ? 19.988 -7.907  -8.860  0.50 30.66 ?  106  ILE   A HD12 1 
ATOM   2264 H  HD12 B ILE   A 1 106 ? 20.026 -8.135  -8.897  0.50 29.03 ?  106  ILE   A HD12 1 
ATOM   2265 H  HD13 A ILE   A 1 106 ? 19.031 -7.097  -9.838  0.50 30.66 ?  106  ILE   A HD13 1 
ATOM   2266 H  HD13 B ILE   A 1 106 ? 19.166 -7.300  -9.942  0.50 29.03 ?  106  ILE   A HD13 1 
ATOM   2267 N  N    A GLN   A 1 107 ? 22.578 -11.049 -11.365 0.50 23.24 ?  107  GLN   A N    1 
ATOM   2268 N  N    B GLN   A 1 107 ? 22.594 -11.345 -11.313 0.50 22.32 ?  107  GLN   A N    1 
ATOM   2269 C  CA   A GLN   A 1 107 ? 23.146 -12.291 -10.844 0.50 25.06 ?  107  GLN   A CA   1 
ATOM   2270 C  CA   B GLN   A 1 107 ? 23.251 -12.507 -10.729 0.50 24.50 ?  107  GLN   A CA   1 
ATOM   2271 C  C    A GLN   A 1 107 ? 24.106 -12.021 -9.692  0.50 22.64 ?  107  GLN   A C    1 
ATOM   2272 C  C    B GLN   A 1 107 ? 24.268 -12.100 -9.671  0.50 22.48 ?  107  GLN   A C    1 
ATOM   2273 O  O    A GLN   A 1 107 ? 24.260 -12.860 -8.796  0.50 23.27 ?  107  GLN   A O    1 
ATOM   2274 O  O    B GLN   A 1 107 ? 24.621 -12.921 -8.818  0.50 23.44 ?  107  GLN   A O    1 
ATOM   2275 C  CB   A GLN   A 1 107 ? 23.854 -13.047 -11.974 0.50 29.00 ?  107  GLN   A CB   1 
ATOM   2276 C  CB   B GLN   A 1 107 ? 23.924 -13.347 -11.823 0.50 28.38 ?  107  GLN   A CB   1 
ATOM   2277 C  CG   A GLN   A 1 107 ? 22.987 -13.267 -13.210 0.50 33.01 ?  107  GLN   A CG   1 
ATOM   2278 C  CG   B GLN   A 1 107 ? 23.052 -13.596 -13.052 0.50 32.30 ?  107  GLN   A CG   1 
ATOM   2279 C  CD   A GLN   A 1 107 ? 21.748 -14.088 -12.915 0.50 36.26 ?  107  GLN   A CD   1 
ATOM   2280 C  CD   B GLN   A 1 107 ? 21.697 -14.185 -12.712 0.50 35.63 ?  107  GLN   A CD   1 
ATOM   2281 O  OE1  A GLN   A 1 107 ? 21.827 -15.151 -12.298 0.50 37.63 ?  107  GLN   A OE1  1 
ATOM   2282 O  OE1  B GLN   A 1 107 ? 21.594 -15.129 -11.928 0.50 37.01 ?  107  GLN   A OE1  1 
ATOM   2283 N  NE2  A GLN   A 1 107 ? 20.593 -13.595 -13.348 0.50 37.37 ?  107  GLN   A NE2  1 
ATOM   2284 N  NE2  B GLN   A 1 107 ? 20.645 -13.625 -13.302 0.50 36.78 ?  107  GLN   A NE2  1 
ATOM   2285 H  H    A GLN   A 1 107 ? 22.759 -10.896 -12.191 0.50 27.88 ?  107  GLN   A H    1 
ATOM   2286 H  H    B GLN   A 1 107 ? 22.688 -11.273 -12.164 0.50 26.78 ?  107  GLN   A H    1 
ATOM   2287 H  HA   A GLN   A 1 107 ? 22.436 -12.856 -10.511 0.50 30.06 ?  107  GLN   A HA   1 
ATOM   2288 H  HA   B GLN   A 1 107 ? 22.586 -13.069 -10.304 0.50 29.39 ?  107  GLN   A HA   1 
ATOM   2289 H  HB2  A GLN   A 1 107 ? 24.636 -12.546 -12.252 0.50 34.79 ?  107  GLN   A HB2  1 
ATOM   2290 H  HB2  B GLN   A 1 107 ? 24.728 -12.893 -12.120 0.50 34.05 ?  107  GLN   A HB2  1 
ATOM   2291 H  HB3  A GLN   A 1 107 ? 24.123 -13.922 -11.651 0.50 34.79 ?  107  GLN   A HB3  1 
ATOM   2292 H  HB3  B GLN   A 1 107 ? 24.159 -14.216 -11.455 0.50 34.05 ?  107  GLN   A HB3  1 
ATOM   2293 H  HG2  A GLN   A 1 107 ? 22.702 -12.408 -13.560 0.50 39.60 ?  107  GLN   A HG2  1 
ATOM   2294 H  HG2  B GLN   A 1 107 ? 22.901 -12.757 -13.514 0.50 38.76 ?  107  GLN   A HG2  1 
ATOM   2295 H  HG3  A GLN   A 1 107 ? 23.507 -13.737 -13.881 0.50 39.60 ?  107  GLN   A HG3  1 
ATOM   2296 H  HG3  B GLN   A 1 107 ? 23.509 -14.215 -13.642 0.50 38.76 ?  107  GLN   A HG3  1 
ATOM   2297 H  HE21 A GLN   A 1 107 ? 20.575 -12.849 -13.774 0.50 44.83 ?  107  GLN   A HE21 1 
ATOM   2298 H  HE21 B GLN   A 1 107 ? 20.754 -12.965 -13.844 0.50 44.14 ?  107  GLN   A HE21 1 
ATOM   2299 H  HE22 A GLN   A 1 107 ? 19.862 -14.025 -13.203 0.50 44.83 ?  107  GLN   A HE22 1 
ATOM   2300 H  HE22 B GLN   A 1 107 ? 19.854 -13.924 -13.145 0.50 44.14 ?  107  GLN   A HE22 1 
ATOM   2301 N  N    . LEU   A 1 108 ? 24.737 -10.847 -9.688  1.00 19.56 ?  108  LEU   A N    1 
ATOM   2302 C  CA   . LEU   A 1 108 ? 25.650 -10.418 -8.637  1.00 16.33 ?  108  LEU   A CA   1 
ATOM   2303 C  C    . LEU   A 1 108 ? 24.951 -10.237 -7.300  1.00 14.44 ?  108  LEU   A C    1 
ATOM   2304 O  O    . LEU   A 1 108 ? 25.635 -10.071 -6.287  1.00 14.94 ?  108  LEU   A O    1 
ATOM   2305 C  CB   . LEU   A 1 108 ? 26.369 -9.127  -9.045  1.00 16.31 ?  108  LEU   A CB   1 
ATOM   2306 C  CG   . LEU   A 1 108 ? 27.380 -9.326  -10.172 1.00 17.73 ?  108  LEU   A CG   1 
ATOM   2307 C  CD1  . LEU   A 1 108 ? 27.842 -7.994  -10.742 1.00 18.32 ?  108  LEU   A CD1  1 
ATOM   2308 C  CD2  . LEU   A 1 108 ? 28.577 -10.126 -9.680  1.00 19.66 ?  108  LEU   A CD2  1 
ATOM   2309 H  H    A LEU   A 1 108 ? 24.646 -10.265 -10.308 0.50 23.46 ?  108  LEU   A H    1 
ATOM   2310 H  H    B LEU   A 1 108 ? 24.559 -10.259 -10.282 0.50 23.46 ?  108  LEU   A H    1 
ATOM   2311 H  HA   . LEU   A 1 108 ? 26.325 -11.104 -8.513  1.00 19.59 ?  108  LEU   A HA   1 
ATOM   2312 H  HB2  . LEU   A 1 108 ? 25.712 -8.482  -9.345  1.00 19.56 ?  108  LEU   A HB2  1 
ATOM   2313 H  HB3  . LEU   A 1 108 ? 26.847 -8.780  -8.279  1.00 19.56 ?  108  LEU   A HB3  1 
ATOM   2314 H  HG   . LEU   A 1 108 ? 26.964 -9.832  -10.888 1.00 21.27 ?  108  LEU   A HG   1 
ATOM   2315 H  HD11 . LEU   A 1 108 ? 28.448 -8.158  -11.484 1.00 21.97 ?  108  LEU   A HD11 1 
ATOM   2316 H  HD12 . LEU   A 1 108 ? 27.070 -7.496  -11.051 1.00 21.97 ?  108  LEU   A HD12 1 
ATOM   2317 H  HD13 . LEU   A 1 108 ? 28.301 -7.495  -10.047 1.00 21.97 ?  108  LEU   A HD13 1 
ATOM   2318 H  HD21 . LEU   A 1 108 ? 29.278 -10.085 -10.345 1.00 23.58 ?  108  LEU   A HD21 1 
ATOM   2319 H  HD22 . LEU   A 1 108 ? 28.886 -9.741  -8.845  1.00 23.58 ?  108  LEU   A HD22 1 
ATOM   2320 H  HD23 . LEU   A 1 108 ? 28.303 -11.046 -9.539  1.00 23.58 ?  108  LEU   A HD23 1 
ATOM   2321 N  N    . LEU   A 1 109 ? 23.617 -10.285 -7.263  1.00 14.03 ?  109  LEU   A N    1 
ATOM   2322 C  CA   . LEU   A 1 109 ? 22.922 -10.160 -5.990  1.00 13.08 ?  109  LEU   A CA   1 
ATOM   2323 C  C    . LEU   A 1 109 ? 23.266 -11.319 -5.059  1.00 12.04 ?  109  LEU   A C    1 
ATOM   2324 O  O    . LEU   A 1 109 ? 23.402 -11.134 -3.845  1.00 12.66 ?  109  LEU   A O    1 
ATOM   2325 C  CB   . LEU   A 1 109 ? 21.418 -10.070 -6.240  1.00 13.87 ?  109  LEU   A CB   1 
ATOM   2326 C  CG   . LEU   A 1 109 ? 20.541 -9.790  -5.025  1.00 13.99 ?  109  LEU   A CG   1 
ATOM   2327 C  CD1  . LEU   A 1 109 ? 21.018 -8.535  -4.321  1.00 14.35 ?  109  LEU   A CD1  1 
ATOM   2328 C  CD2  . LEU   A 1 109 ? 19.082 -9.649  -5.448  1.00 14.96 ?  109  LEU   A CD2  1 
ATOM   2329 H  H    . LEU   A 1 109 ? 23.105 -10.387 -7.948  1.00 16.83 ?  109  LEU   A H    1 
ATOM   2330 H  HA   . LEU   A 1 109 ? 23.209 -9.339  -5.564  1.00 15.69 ?  109  LEU   A HA   1 
ATOM   2331 H  HB2  . LEU   A 1 109 ? 21.259 -9.357  -6.878  1.00 16.64 ?  109  LEU   A HB2  1 
ATOM   2332 H  HB3  . LEU   A 1 109 ? 21.122 -10.911 -6.619  1.00 16.64 ?  109  LEU   A HB3  1 
ATOM   2333 H  HG   . LEU   A 1 109 ? 20.604 -10.531 -4.404  1.00 16.78 ?  109  LEU   A HG   1 
ATOM   2334 H  HD11 . LEU   A 1 109 ? 20.329 -8.220  -3.725  1.00 17.21 ?  109  LEU   A HD11 1 
ATOM   2335 H  HD12 . LEU   A 1 109 ? 21.827 -8.739  -3.825  1.00 17.21 ?  109  LEU   A HD12 1 
ATOM   2336 H  HD13 . LEU   A 1 109 ? 21.212 -7.853  -4.992  1.00 17.21 ?  109  LEU   A HD13 1 
ATOM   2337 H  HD21 . LEU   A 1 109 ? 18.558 -9.352  -4.686  1.00 17.95 ?  109  LEU   A HD21 1 
ATOM   2338 H  HD22 . LEU   A 1 109 ? 19.018 -9.000  -6.165  1.00 17.95 ?  109  LEU   A HD22 1 
ATOM   2339 H  HD23 . LEU   A 1 109 ? 18.754 -10.512 -5.755  1.00 17.95 ?  109  LEU   A HD23 1 
ATOM   2340 N  N    . LYS   A 1 110 ? 23.410 -12.530 -5.603  1.00 12.21 ?  110  LYS   A N    1 
ATOM   2341 C  CA   . LYS   A 1 110 ? 23.791 -13.650 -4.747  1.00 12.36 ?  110  LYS   A CA   1 
ATOM   2342 C  C    . LYS   A 1 110 ? 25.174 -13.426 -4.145  1.00 11.94 ?  110  LYS   A C    1 
ATOM   2343 O  O    . LYS   A 1 110 ? 25.375 -13.629 -2.945  1.00 12.03 ?  110  LYS   A O    1 
ATOM   2344 C  CB   . LYS   A 1 110 ? 23.711 -14.971 -5.512  1.00 13.29 ?  110  LYS   A CB   1 
ATOM   2345 C  CG   . LYS   A 1 110 ? 23.891 -16.180 -4.601  1.00 13.76 ?  110  LYS   A CG   1 
ATOM   2346 C  CD   . LYS   A 1 110 ? 23.676 -17.495 -5.326  1.00 14.41 ?  110  LYS   A CD   1 
ATOM   2347 C  CE   . LYS   A 1 110 ? 23.779 -18.686 -4.388  1.00 15.00 ?  110  LYS   A CE   1 
ATOM   2348 N  NZ   . LYS   A 1 110 ? 22.599 -18.825 -3.497  1.00 15.47 ?  110  LYS   A NZ   1 
ATOM   2349 H  H    . LYS   A 1 110 ? 23.294 -12.725 -6.429  1.00 14.65 ?  110  LYS   A H    1 
ATOM   2350 H  HA   . LYS   A 1 110 ? 23.153 -13.705 -4.013  1.00 14.82 ?  110  LYS   A HA   1 
ATOM   2351 H  HB2  . LYS   A 1 110 ? 22.842 -15.040 -5.937  1.00 15.94 ?  110  LYS   A HB2  1 
ATOM   2352 H  HB3  . LYS   A 1 110 ? 24.413 -14.992 -6.177  1.00 15.94 ?  110  LYS   A HB3  1 
ATOM   2353 H  HG2  . LYS   A 1 110 ? 24.787 -16.178 -4.239  1.00 16.51 ?  110  LYS   A HG2  1 
ATOM   2354 H  HG3  . LYS   A 1 110 ? 23.240 -16.128 -3.878  1.00 16.51 ?  110  LYS   A HG3  1 
ATOM   2355 H  HD2  . LYS   A 1 110 ? 22.791 -17.499 -5.724  1.00 17.28 ?  110  LYS   A HD2  1 
ATOM   2356 H  HD3  . LYS   A 1 110 ? 24.353 -17.591 -6.012  1.00 17.28 ?  110  LYS   A HD3  1 
ATOM   2357 H  HE2  . LYS   A 1 110 ? 23.855 -19.497 -4.911  1.00 18.00 ?  110  LYS   A HE2  1 
ATOM   2358 H  HE3  . LYS   A 1 110 ? 24.563 -18.579 -3.824  1.00 18.00 ?  110  LYS   A HE3  1 
ATOM   2359 H  HZ1  . LYS   A 1 110 ? 22.695 -19.529 -2.966  1.00 18.56 ?  110  LYS   A HZ1  1 
ATOM   2360 H  HZ2  . LYS   A 1 110 ? 22.506 -18.093 -2.996  1.00 18.56 ?  110  LYS   A HZ2  1 
ATOM   2361 H  HZ3  . LYS   A 1 110 ? 21.860 -18.930 -3.987  1.00 18.56 ?  110  LYS   A HZ3  1 
ATOM   2362 N  N    . SER   A 1 111 ? 26.130 -12.981 -4.960  1.00 12.00 ?  111  SER   A N    1 
ATOM   2363 C  CA   . SER   A 1 111 ? 27.458 -12.678 -4.440  1.00 12.18 ?  111  SER   A CA   1 
ATOM   2364 C  C    . SER   A 1 111 ? 27.389 -11.637 -3.330  1.00 11.74 ?  111  SER   A C    1 
ATOM   2365 O  O    . SER   A 1 111 ? 28.087 -11.747 -2.316  1.00 12.38 ?  111  SER   A O    1 
ATOM   2366 C  CB   . SER   A 1 111 ? 28.351 -12.184 -5.576  1.00 13.57 ?  111  SER   A CB   1 
ATOM   2367 O  OG   . SER   A 1 111 ? 28.443 -13.165 -6.598  1.00 15.49 ?  111  SER   A OG   1 
ATOM   2368 H  H    . SER   A 1 111 ? 26.025 -12.847 -5.801  1.00 14.39 ?  111  SER   A H    1 
ATOM   2369 H  HA   . SER   A 1 111 ? 27.848 -13.489 -4.076  1.00 14.61 ?  111  SER   A HA   1 
ATOM   2370 H  HB2  . SER   A 1 111 ? 27.962 -11.384 -5.960  1.00 16.28 ?  111  SER   A HB2  1 
ATOM   2371 H  HB3  . SER   A 1 111 ? 29.232 -11.990 -5.222  1.00 16.28 ?  111  SER   A HB3  1 
ATOM   2372 H  HG   . SER   A 1 111 ? 28.965 -12.891 -7.212  1.00 18.58 ?  111  SER   A HG   1 
ATOM   2373 N  N    . ALA   A 1 112 ? 26.546 -10.615 -3.509  1.00 11.79 ?  112  ALA   A N    1 
ATOM   2374 C  CA   . ALA   A 1 112 ? 26.397 -9.581  -2.488  1.00 11.55 ?  112  ALA   A CA   1 
ATOM   2375 C  C    . ALA   A 1 112 ? 25.924 -10.185 -1.168  1.00 11.58 ?  112  ALA   A C    1 
ATOM   2376 O  O    . ALA   A 1 112 ? 26.480 -9.903  -0.102  1.00 11.85 ?  112  ALA   A O    1 
ATOM   2377 C  CB   . ALA   A 1 112 ? 25.439 -8.495  -2.983  1.00 12.17 ?  112  ALA   A CB   1 
ATOM   2378 H  H    . ALA   A 1 112 ? 26.055 -10.497 -4.204  1.00 14.14 ?  112  ALA   A H    1 
ATOM   2379 H  HA   . ALA   A 1 112 ? 27.256 -9.160  -2.331  1.00 13.85 ?  112  ALA   A HA   1 
ATOM   2380 H  HB1  . ALA   A 1 112 ? 25.377 -7.790  -2.314  1.00 14.59 ?  112  ALA   A HB1  1 
ATOM   2381 H  HB2  . ALA   A 1 112 ? 25.773 -8.126  -3.814  1.00 14.59 ?  112  ALA   A HB2  1 
ATOM   2382 H  HB3  . ALA   A 1 112 ? 24.558 -8.884  -3.126  1.00 14.59 ?  112  ALA   A HB3  1 
ATOM   2383 N  N    . TYR   A 1 113 ? 24.893 -11.035 -1.219  1.00 11.54 ?  113  TYR   A N    1 
ATOM   2384 C  CA   . TYR   A 1 113 ? 24.384 -11.639 0.008   1.00 11.34 ?  113  TYR   A CA   1 
ATOM   2385 C  C    . TYR   A 1 113 ? 25.386 -12.595 0.649   1.00 10.75 ?  113  TYR   A C    1 
ATOM   2386 O  O    . TYR   A 1 113 ? 25.355 -12.787 1.868   1.00 11.44 ?  113  TYR   A O    1 
ATOM   2387 C  CB   . TYR   A 1 113 ? 23.066 -12.362 -0.272  1.00 11.92 ?  113  TYR   A CB   1 
ATOM   2388 C  CG   . TYR   A 1 113 ? 21.849 -11.463 -0.183  1.00 11.93 ?  113  TYR   A CG   1 
ATOM   2389 C  CD1  . TYR   A 1 113 ? 21.495 -10.868 1.020   1.00 12.03 ?  113  TYR   A CD1  1 
ATOM   2390 C  CD2  . TYR   A 1 113 ? 21.040 -11.238 -1.288  1.00 12.17 ?  113  TYR   A CD2  1 
ATOM   2391 C  CE1  . TYR   A 1 113 ? 20.375 -10.067 1.119   1.00 12.43 ?  113  TYR   A CE1  1 
ATOM   2392 C  CE2  . TYR   A 1 113 ? 19.902 -10.428 -1.198  1.00 12.16 ?  113  TYR   A CE2  1 
ATOM   2393 C  CZ   . TYR   A 1 113 ? 19.582 -9.854  0.010   1.00 12.08 ?  113  TYR   A CZ   1 
ATOM   2394 O  OH   . TYR   A 1 113 ? 18.464 -9.055  0.136   1.00 12.87 ?  113  TYR   A OH   1 
ATOM   2395 H  H    . TYR   A 1 113 ? 24.484 -11.270 -1.936  1.00 13.84 ?  113  TYR   A H    1 
ATOM   2396 H  HA   . TYR   A 1 113 ? 24.205 -10.933 0.648   1.00 13.61 ?  113  TYR   A HA   1 
ATOM   2397 H  HB2  . TYR   A 1 113 ? 23.092 -12.728 -1.169  1.00 14.30 ?  113  TYR   A HB2  1 
ATOM   2398 H  HB3  . TYR   A 1 113 ? 22.956 -13.074 0.374   1.00 14.30 ?  113  TYR   A HB3  1 
ATOM   2399 H  HD1  . TYR   A 1 113 ? 22.031 -11.016 1.775   1.00 14.43 ?  113  TYR   A HD1  1 
ATOM   2400 H  HD2  . TYR   A 1 113 ? 21.252 -11.636 -2.098  1.00 14.60 ?  113  TYR   A HD2  1 
ATOM   2401 H  HE1  . TYR   A 1 113 ? 20.160 -9.677  1.936   1.00 14.91 ?  113  TYR   A HE1  1 
ATOM   2402 H  HE2  . TYR   A 1 113 ? 19.362 -10.285 -1.942  1.00 14.59 ?  113  TYR   A HE2  1 
ATOM   2403 H  HH   . TYR   A 1 113 ? 18.068 -9.006  -0.609  1.00 15.44 ?  113  TYR   A HH   1 
ATOM   2404 N  N    . GLU   A 1 114 ? 26.281 -13.196 -0.143  1.00 11.19 ?  114  GLU   A N    1 
ATOM   2405 C  CA   . GLU   A 1 114 ? 27.274 -14.099 0.440   1.00 11.73 ?  114  GLU   A CA   1 
ATOM   2406 C  C    . GLU   A 1 114 ? 28.129 -13.398 1.489   1.00 11.56 ?  114  GLU   A C    1 
ATOM   2407 O  O    . GLU   A 1 114 ? 28.605 -14.035 2.435   1.00 11.87 ?  114  GLU   A O    1 
ATOM   2408 C  CB   . GLU   A 1 114 ? 28.143 -14.726 -0.660  1.00 11.97 ?  114  GLU   A CB   1 
ATOM   2409 C  CG   . GLU   A 1 114 ? 27.382 -15.787 -1.439  1.00 12.48 ?  114  GLU   A CG   1 
ATOM   2410 C  CD   . GLU   A 1 114 ? 28.093 -16.310 -2.680  1.00 12.81 ?  114  GLU   A CD   1 
ATOM   2411 O  OE1  . GLU   A 1 114 ? 29.045 -15.677 -3.173  1.00 13.02 ?  114  GLU   A OE1  1 
ATOM   2412 O  OE2  . GLU   A 1 114 ? 27.656 -17.370 -3.185  1.00 13.85 -1 114  GLU   A OE2  1 
ATOM   2413 H  H    . GLU   A 1 114 ? 26.332 -13.093 -1.001  1.00 13.42 ?  114  GLU   A H    1 
ATOM   2414 H  HA   . GLU   A 1 114 ? 26.802 -14.819 0.879   1.00 14.07 ?  114  GLU   A HA   1 
ATOM   2415 H  HB2  . GLU   A 1 114 ? 28.416 -14.033 -1.288  1.00 14.36 ?  114  GLU   A HB2  1 
ATOM   2416 H  HB3  . GLU   A 1 114 ? 28.917 -15.141 -0.261  1.00 14.36 ?  114  GLU   A HB3  1 
ATOM   2417 H  HG2  . GLU   A 1 114 ? 27.227 -16.546 -0.858  1.00 14.97 ?  114  GLU   A HG2  1 
ATOM   2418 H  HG3  . GLU   A 1 114 ? 26.529 -15.417 -1.724  1.00 14.97 ?  114  GLU   A HG3  1 
ATOM   2419 N  N    . ASN   A 1 115 ? 28.311 -12.081 1.360   1.00 11.32 ?  115  ASN   A N    1 
ATOM   2420 C  CA   . ASN   A 1 115 ? 29.076 -11.354 2.367   1.00 11.71 ?  115  ASN   A CA   1 
ATOM   2421 C  C    . ASN   A 1 115 ? 28.463 -11.488 3.752   1.00 11.43 ?  115  ASN   A C    1 
ATOM   2422 O  O    . ASN   A 1 115 ? 29.179 -11.417 4.758   1.00 12.07 ?  115  ASN   A O    1 
ATOM   2423 C  CB   . ASN   A 1 115 ? 29.178 -9.875  1.994   1.00 11.93 ?  115  ASN   A CB   1 
ATOM   2424 C  CG   . ASN   A 1 115 ? 29.976 -9.648  0.733   1.00 12.54 ?  115  ASN   A CG   1 
ATOM   2425 O  OD1  . ASN   A 1 115 ? 31.199 -9.733  0.747   1.00 15.67 ?  115  ASN   A OD1  1 
ATOM   2426 N  ND2  . ASN   A 1 115 ? 29.302 -9.349  -0.357  1.00 11.89 ?  115  ASN   A ND2  1 
ATOM   2427 H  H    . ASN   A 1 115 ? 28.005 -11.594 0.715   1.00 13.58 ?  115  ASN   A H    1 
ATOM   2428 H  HA   . ASN   A 1 115 ? 29.973 -11.718 2.401   1.00 14.04 ?  115  ASN   A HA   1 
ATOM   2429 H  HB2  . ASN   A 1 115 ? 28.284 -9.522  1.861   1.00 14.31 ?  115  ASN   A HB2  1 
ATOM   2430 H  HB3  . ASN   A 1 115 ? 29.616 -9.400  2.720   1.00 14.31 ?  115  ASN   A HB3  1 
ATOM   2431 H  HD21 . ASN   A 1 115 ? 29.720 -9.211  -1.094  1.00 14.26 ?  115  ASN   A HD21 1 
ATOM   2432 H  HD22 . ASN   A 1 115 ? 28.442 -9.312  -0.336  1.00 14.26 ?  115  ASN   A HD22 1 
ATOM   2433 N  N    . PHE   A 1 116 ? 27.139 -11.656 3.833   1.00 11.53 ?  116  PHE   A N    1 
ATOM   2434 C  CA   . PHE   A 1 116 ? 26.498 -11.759 5.138   1.00 11.46 ?  116  PHE   A CA   1 
ATOM   2435 C  C    . PHE   A 1 116 ? 26.977 -12.993 5.905   1.00 11.98 ?  116  PHE   A C    1 
ATOM   2436 O  O    . PHE   A 1 116 ? 26.899 -13.017 7.135   1.00 12.38 ?  116  PHE   A O    1 
ATOM   2437 C  CB   . PHE   A 1 116 ? 24.973 -11.892 5.003   1.00 11.85 ?  116  PHE   A CB   1 
ATOM   2438 C  CG   . PHE   A 1 116 ? 24.217 -10.646 4.550   1.00 11.57 ?  116  PHE   A CG   1 
ATOM   2439 C  CD1  . PHE   A 1 116 ? 24.788 -9.620  3.801   1.00 11.70 ?  116  PHE   A CD1  1 
ATOM   2440 C  CD2  . PHE   A 1 116 ? 22.865 -10.545 4.875   1.00 12.15 ?  116  PHE   A CD2  1 
ATOM   2441 C  CE1  . PHE   A 1 116 ? 24.017 -8.540  3.393   1.00 11.91 ?  116  PHE   A CE1  1 
ATOM   2442 C  CE2  . PHE   A 1 116 ? 22.095 -9.468  4.478   1.00 12.34 ?  116  PHE   A CE2  1 
ATOM   2443 C  CZ   . PHE   A 1 116 ? 22.663 -8.465  3.733   1.00 11.85 ?  116  PHE   A CZ   1 
ATOM   2444 H  H    . PHE   A 1 116 ? 26.604 -11.711 3.158   1.00 13.83 ?  116  PHE   A H    1 
ATOM   2445 H  HA   . PHE   A 1 116 ? 26.692 -10.965 5.661   1.00 13.74 ?  116  PHE   A HA   1 
ATOM   2446 H  HB2  . PHE   A 1 116 ? 24.788 -12.595 4.357   1.00 14.21 ?  116  PHE   A HB2  1 
ATOM   2447 H  HB3  . PHE   A 1 116 ? 24.616 -12.153 5.867   1.00 14.21 ?  116  PHE   A HB3  1 
ATOM   2448 H  HD1  . PHE   A 1 116 ? 25.678 -9.678  3.561   1.00 14.03 ?  116  PHE   A HD1  1 
ATOM   2449 H  HD2  . PHE   A 1 116 ? 22.463 -11.235 5.372   1.00 14.57 ?  116  PHE   A HD2  1 
ATOM   2450 H  HE1  . PHE   A 1 116 ? 24.405 -7.861  2.895   1.00 14.29 ?  116  PHE   A HE1  1 
ATOM   2451 H  HE2  . PHE   A 1 116 ? 21.191 -9.434  4.716   1.00 14.80 ?  116  PHE   A HE2  1 
ATOM   2452 H  HZ   . PHE   A 1 116 ? 22.151 -7.733  3.473   1.00 14.21 ?  116  PHE   A HZ   1 
ATOM   2453 N  N    . ASN   A 1 117 ? 27.416 -14.041 5.199   1.00 11.87 ?  117  ASN   A N    1 
ATOM   2454 C  CA   . ASN   A 1 117 ? 27.787 -15.291 5.858   1.00 12.60 ?  117  ASN   A CA   1 
ATOM   2455 C  C    . ASN   A 1 117 ? 29.052 -15.176 6.685   1.00 13.00 ?  117  ASN   A C    1 
ATOM   2456 O  O    . ASN   A 1 117 ? 29.360 -16.102 7.444   1.00 13.83 ?  117  ASN   A O    1 
ATOM   2457 C  CB   . ASN   A 1 117 ? 27.904 -16.403 4.824   1.00 12.55 ?  117  ASN   A CB   1 
ATOM   2458 C  CG   . ASN   A 1 117 ? 26.553 -16.787 4.289   1.00 12.48 ?  117  ASN   A CG   1 
ATOM   2459 O  OD1  . ASN   A 1 117 ? 25.582 -16.828 5.044   1.00 13.22 ?  117  ASN   A OD1  1 
ATOM   2460 N  ND2  . ASN   A 1 117 ? 26.464 -17.041 2.993   1.00 12.28 ?  117  ASN   A ND2  1 
ATOM   2461 H  H    . ASN   A 1 117 ? 27.493 -14.049 4.341   1.00 14.23 ?  117  ASN   A H    1 
ATOM   2462 H  HA   . ASN   A 1 117 ? 27.067 -15.528 6.463   1.00 15.11 ?  117  ASN   A HA   1 
ATOM   2463 H  HB2  . ASN   A 1 117 ? 28.453 -16.096 4.083   1.00 15.05 ?  117  ASN   A HB2  1 
ATOM   2464 H  HB3  . ASN   A 1 117 ? 28.300 -17.181 5.239   1.00 15.05 ?  117  ASN   A HB3  1 
ATOM   2465 H  HD21 . ASN   A 1 117 ? 25.712 -17.255 2.650   1.00 14.73 ?  117  ASN   A HD21 1 
ATOM   2466 H  HD22 . ASN   A 1 117 ? 27.168 -16.982 2.497   1.00 14.73 ?  117  ASN   A HD22 1 
ATOM   2467 N  N    . GLN   A 1 118 ? 29.774 -14.061 6.571   1.00 12.77 ?  118  GLN   A N    1 
ATOM   2468 C  CA   . GLN   A 1 118 ? 30.955 -13.826 7.389   1.00 13.44 ?  118  GLN   A CA   1 
ATOM   2469 C  C    . GLN   A 1 118 ? 30.618 -13.256 8.761   1.00 13.21 ?  118  GLN   A C    1 
ATOM   2470 O  O    . GLN   A 1 118 ? 31.535 -12.974 9.541   1.00 14.84 ?  118  GLN   A O    1 
ATOM   2471 C  CB   . GLN   A 1 118 ? 31.935 -12.909 6.651   1.00 13.49 ?  118  GLN   A CB   1 
ATOM   2472 C  CG   . GLN   A 1 118 ? 32.413 -13.487 5.327   1.00 13.50 ?  118  GLN   A CG   1 
ATOM   2473 C  CD   . GLN   A 1 118 ? 33.243 -14.746 5.503   1.00 13.92 ?  118  GLN   A CD   1 
ATOM   2474 O  OE1  . GLN   A 1 118 ? 34.102 -14.811 6.388   1.00 15.00 ?  118  GLN   A OE1  1 
ATOM   2475 N  NE2  . GLN   A 1 118 ? 32.993 -15.751 4.661   1.00 13.81 ?  118  GLN   A NE2  1 
ATOM   2476 H  H    . GLN   A 1 118 ? 29.593 -13.411 6.027   1.00 15.32 ?  118  GLN   A H    1 
ATOM   2477 H  HA   . GLN   A 1 118 ? 31.393 -14.679 7.526   1.00 16.12 ?  118  GLN   A HA   1 
ATOM   2478 H  HB2  . GLN   A 1 118 ? 31.501 -12.063 6.472   1.00 16.18 ?  118  GLN   A HB2  1 
ATOM   2479 H  HB3  . GLN   A 1 118 ? 32.713 -12.771 7.215   1.00 16.18 ?  118  GLN   A HB3  1 
ATOM   2480 H  HG2  . GLN   A 1 118 ? 31.641 -13.704 4.779   1.00 16.20 ?  118  GLN   A HG2  1 
ATOM   2481 H  HG3  . GLN   A 1 118 ? 32.963 -12.826 4.876   1.00 16.20 ?  118  GLN   A HG3  1 
ATOM   2482 H  HE21 . GLN   A 1 118 ? 32.376 -15.664 4.056   1.00 16.57 ?  118  GLN   A HE21 1 
ATOM   2483 H  HE22 . GLN   A 1 118 ? 33.429 -16.485 4.717   1.00 16.57 ?  118  GLN   A HE22 1 
ATOM   2484 N  N    . HIS   A 1 119 ? 29.332 -13.104 9.080   1.00 12.82 ?  119  HIS   A N    1 
ATOM   2485 C  CA   . HIS   A 1 119 ? 28.882 -12.503 10.329  1.00 13.56 ?  119  HIS   A CA   1 
ATOM   2486 C  C    . HIS   A 1 119 ? 27.747 -13.329 10.903  1.00 14.14 ?  119  HIS   A C    1 
ATOM   2487 O  O    . HIS   A 1 119 ? 26.798 -13.657 10.187  1.00 14.58 ?  119  HIS   A O    1 
ATOM   2488 C  CB   . HIS   A 1 119 ? 28.421 -11.069 10.067  1.00 13.83 ?  119  HIS   A CB   1 
ATOM   2489 C  CG   . HIS   A 1 119 ? 29.499 -10.250 9.459   1.00 15.30 ?  119  HIS   A CG   1 
ATOM   2490 N  ND1  . HIS   A 1 119 ? 30.473 -9.651  10.220  1.00 17.32 ?  119  HIS   A ND1  1 
ATOM   2491 C  CD2  . HIS   A 1 119 ? 29.840 -10.044 8.168   1.00 16.04 ?  119  HIS   A CD2  1 
ATOM   2492 C  CE1  . HIS   A 1 119 ? 31.340 -9.056  9.423   1.00 17.67 ?  119  HIS   A CE1  1 
ATOM   2493 N  NE2  . HIS   A 1 119 ? 30.990 -9.293  8.171   1.00 17.38 ?  119  HIS   A NE2  1 
ATOM   2494 H  H    . HIS   A 1 119 ? 28.677 -13.362 8.574   1.00 15.38 ?  119  HIS   A H    1 
ATOM   2495 H  HA   . HIS   A 1 119 ? 29.615 -12.495 10.966  1.00 16.27 ?  119  HIS   A HA   1 
ATOM   2496 H  HB2  . HIS   A 1 119 ? 27.666 -11.094 9.457   1.00 16.59 ?  119  HIS   A HB2  1 
ATOM   2497 H  HB3  . HIS   A 1 119 ? 28.161 -10.669 10.908  1.00 16.59 ?  119  HIS   A HB3  1 
ATOM   2498 H  HD1  . HIS   A 1 119 ? 30.497 -9.647  11.080  1.00 20.78 ?  119  HIS   A HD1  1 
ATOM   2499 H  HD2  . HIS   A 1 119 ? 29.380 -10.350 7.418   1.00 19.25 ?  119  HIS   A HD2  1 
ATOM   2500 H  HE1  . HIS   A 1 119 ? 32.072 -8.554  9.697   1.00 21.19 ?  119  HIS   A HE1  1 
ATOM   2501 N  N    . GLU   A 1 120 ? 27.845 -13.653 12.194  1.00 15.27 ?  120  GLU   A N    1 
ATOM   2502 C  CA   . GLU   A 1 120 ? 26.894 -14.587 12.796  1.00 17.09 ?  120  GLU   A CA   1 
ATOM   2503 C  C    . GLU   A 1 120 ? 25.477 -14.022 12.848  1.00 15.76 ?  120  GLU   A C    1 
ATOM   2504 O  O    . GLU   A 1 120 ? 24.501 -14.777 12.721  1.00 15.62 ?  120  GLU   A O    1 
ATOM   2505 C  CB   . GLU   A 1 120 ? 27.366 -14.989 14.195  1.00 22.58 ?  120  GLU   A CB   1 
ATOM   2506 C  CG   . GLU   A 1 120 ? 28.568 -15.922 14.204  1.00 30.03 ?  120  GLU   A CG   1 
ATOM   2507 C  CD   . GLU   A 1 120 ? 28.702 -16.681 15.508  1.00 36.27 ?  120  GLU   A CD   1 
ATOM   2508 O  OE1  . GLU   A 1 120 ? 28.234 -16.169 16.548  1.00 38.27 ?  120  GLU   A OE1  1 
ATOM   2509 O  OE2  . GLU   A 1 120 ? 29.270 -17.793 15.493  1.00 40.86 -1 120  GLU   A OE2  1 
ATOM   2510 H  H    . GLU   A 1 120 ? 28.454 -13.363 12.736  1.00 18.32 ?  120  GLU   A H    1 
ATOM   2511 H  HA   . GLU   A 1 120 ? 26.869 -15.393 12.263  1.00 20.51 ?  120  GLU   A HA   1 
ATOM   2512 H  HB2  . GLU   A 1 120 ? 27.615 -14.195 14.692  1.00 27.09 ?  120  GLU   A HB2  1 
ATOM   2513 H  HB3  . GLU   A 1 120 ? 26.642 -15.448 14.655  1.00 27.09 ?  120  GLU   A HB3  1 
ATOM   2514 H  HG2  . GLU   A 1 120 ? 28.482 -16.561 13.478  1.00 36.03 ?  120  GLU   A HG2  1 
ATOM   2515 H  HG3  . GLU   A 1 120 ? 29.378 -15.402 14.096  1.00 36.03 ?  120  GLU   A HG3  1 
ATOM   2516 N  N    . VAL   A 1 121 ? 25.345 -12.716 13.082  1.00 15.08 ?  121  VAL   A N    1 
ATOM   2517 C  CA   . VAL   A 1 121 ? 24.051 -12.050 13.205  1.00 15.13 ?  121  VAL   A CA   1 
ATOM   2518 C  C    . VAL   A 1 121 ? 24.164 -10.670 12.569  1.00 13.66 ?  121  VAL   A C    1 
ATOM   2519 O  O    . VAL   A 1 121 ? 25.136 -9.946  12.809  1.00 14.65 ?  121  VAL   A O    1 
ATOM   2520 C  CB   . VAL   A 1 121 ? 23.620 -11.903 14.681  1.00 18.36 ?  121  VAL   A CB   1 
ATOM   2521 C  CG1  . VAL   A 1 121 ? 22.231 -11.286 14.770  1.00 19.10 ?  121  VAL   A CG1  1 
ATOM   2522 C  CG2  . VAL   A 1 121 ? 23.649 -13.234 15.410  1.00 20.52 ?  121  VAL   A CG2  1 
ATOM   2523 H  H    . VAL   A 1 121 ? 26.012 -12.177 13.183  1.00 18.09 ?  121  VAL   A H    1 
ATOM   2524 H  HA   . VAL   A 1 121 ? 23.379 -12.563 12.734  1.00 18.15 ?  121  VAL   A HA   1 
ATOM   2525 H  HB   . VAL   A 1 121 ? 24.235 -11.306 15.131  1.00 22.02 ?  121  VAL   A HB   1 
ATOM   2526 H  HG11 . VAL   A 1 121 ? 21.917 -11.342 15.687  1.00 22.92 ?  121  VAL   A HG11 1 
ATOM   2527 H  HG12 . VAL   A 1 121 ? 22.275 -10.357 14.494  1.00 22.92 ?  121  VAL   A HG12 1 
ATOM   2528 H  HG13 . VAL   A 1 121 ? 21.628 -11.776 14.187  1.00 22.92 ?  121  VAL   A HG13 1 
ATOM   2529 H  HG21 . VAL   A 1 121 ? 23.298 -13.111 16.311  1.00 24.62 ?  121  VAL   A HG21 1 
ATOM   2530 H  HG22 . VAL   A 1 121 ? 23.094 -13.872 14.932  1.00 24.62 ?  121  VAL   A HG22 1 
ATOM   2531 H  HG23 . VAL   A 1 121 ? 24.560 -13.555 15.455  1.00 24.62 ?  121  VAL   A HG23 1 
ATOM   2532 N  N    . LEU   A 1 122 ? 23.154 -10.286 11.785  1.00 13.19 ?  122  LEU   A N    1 
ATOM   2533 C  CA   . LEU   A 1 122 ? 23.158 -8.982  11.134  1.00 13.13 ?  122  LEU   A CA   1 
ATOM   2534 C  C    . LEU   A 1 122 ? 21.762 -8.395  11.086  1.00 13.20 ?  122  LEU   A C    1 
ATOM   2535 O  O    . LEU   A 1 122 ? 20.770 -9.115  10.956  1.00 14.08 ?  122  LEU   A O    1 
ATOM   2536 C  CB   . LEU   A 1 122 ? 23.579 -9.061  9.664   1.00 14.75 ?  122  LEU   A CB   1 
ATOM   2537 C  CG   . LEU   A 1 122 ? 24.777 -9.913  9.279   1.00 14.81 ?  122  LEU   A CG   1 
ATOM   2538 C  CD1  . LEU   A 1 122 ? 24.351 -11.354 9.043   1.00 15.36 ?  122  LEU   A CD1  1 
ATOM   2539 C  CD2  . LEU   A 1 122 ? 25.442 -9.337  8.039   1.00 13.82 ?  122  LEU   A CD2  1 
ATOM   2540 H  H    . LEU   A 1 122 ? 22.454 -10.762 11.617  1.00 15.82 ?  122  LEU   A H    1 
ATOM   2541 H  HA   . LEU   A 1 122 ? 23.750 -8.370  11.603  1.00 15.75 ?  122  LEU   A HA   1 
ATOM   2542 H  HB2  . LEU   A 1 122 ? 22.836 -9.405  9.157   1.00 17.69 ?  122  LEU   A HB2  1 
ATOM   2543 H  HB3  . LEU   A 1 122 ? 23.784 -8.163  9.363   1.00 17.69 ?  122  LEU   A HB3  1 
ATOM   2544 H  HG   . LEU   A 1 122 ? 25.441 -9.906  9.990   1.00 17.77 ?  122  LEU   A HG   1 
ATOM   2545 H  HD11 . LEU   A 1 122 ? 25.115 -11.876 8.751   1.00 18.43 ?  122  LEU   A HD11 1 
ATOM   2546 H  HD12 . LEU   A 1 122 ? 24.002 -11.716 9.871   1.00 18.43 ?  122  LEU   A HD12 1 
ATOM   2547 H  HD13 . LEU   A 1 122 ? 23.662 -11.370 8.359   1.00 18.43 ?  122  LEU   A HD13 1 
ATOM   2548 H  HD21 . LEU   A 1 122 ? 26.185 -9.909  7.766   1.00 16.57 ?  122  LEU   A HD21 1 
ATOM   2549 H  HD22 . LEU   A 1 122 ? 24.793 -9.288  7.319   1.00 16.57 ?  122  LEU   A HD22 1 
ATOM   2550 H  HD23 . LEU   A 1 122 ? 25.781 -8.447  8.236   1.00 16.57 ?  122  LEU   A HD23 1 
ATOM   2551 N  N    A LEU   A 1 123 ? 21.701 -7.068  11.168  0.50 12.63 ?  123  LEU   A N    1 
ATOM   2552 N  N    B LEU   A 1 123 ? 21.707 -7.067  11.191  0.50 12.68 ?  123  LEU   A N    1 
ATOM   2553 C  CA   A LEU   A 1 123 ? 20.530 -6.291  10.782  0.50 12.45 ?  123  LEU   A CA   1 
ATOM   2554 C  CA   B LEU   A 1 123 ? 20.527 -6.273  10.868  0.50 12.63 ?  123  LEU   A CA   1 
ATOM   2555 C  C    A LEU   A 1 123 ? 20.770 -5.755  9.378   0.50 11.70 ?  123  LEU   A C    1 
ATOM   2556 C  C    B LEU   A 1 123 ? 20.740 -5.706  9.471   0.50 11.93 ?  123  LEU   A C    1 
ATOM   2557 O  O    A LEU   A 1 123 ? 21.870 -5.284  9.082   0.50 11.86 ?  123  LEU   A O    1 
ATOM   2558 O  O    B LEU   A 1 123 ? 21.706 -4.967  9.252   0.50 11.67 ?  123  LEU   A O    1 
ATOM   2559 C  CB   A LEU   A 1 123 ? 20.363 -5.107  11.732  0.50 12.94 ?  123  LEU   A CB   1 
ATOM   2560 C  CB   B LEU   A 1 123 ? 20.386 -5.129  11.872  0.50 13.33 ?  123  LEU   A CB   1 
ATOM   2561 C  CG   A LEU   A 1 123 ? 19.291 -4.073  11.387  0.50 13.81 ?  123  LEU   A CG   1 
ATOM   2562 C  CG   B LEU   A 1 123 ? 19.372 -4.033  11.538  0.50 13.68 ?  123  LEU   A CG   1 
ATOM   2563 C  CD1  A LEU   A 1 123 ? 17.913 -4.716  11.386  0.50 14.18 ?  123  LEU   A CD1  1 
ATOM   2564 C  CD1  B LEU   A 1 123 ? 17.947 -4.575  11.547  0.50 14.26 ?  123  LEU   A CD1  1 
ATOM   2565 C  CD2  A LEU   A 1 123 ? 19.343 -2.907  12.366  0.50 14.47 ?  123  LEU   A CD2  1 
ATOM   2566 C  CD2  B LEU   A 1 123 ? 19.516 -2.887  12.518  0.50 14.19 ?  123  LEU   A CD2  1 
ATOM   2567 H  H    A LEU   A 1 123 ? 22.354 -6.578  11.451  0.50 15.14 ?  123  LEU   A H    1 
ATOM   2568 H  H    B LEU   A 1 123 ? 22.371 -6.580  11.449  0.50 15.21 ?  123  LEU   A H    1 
ATOM   2569 H  HA   A LEU   A 1 123 ? 19.737 -6.844  10.788  0.50 14.93 ?  123  LEU   A HA   1 
ATOM   2570 H  HA   B LEU   A 1 123 ? 19.728 -6.816  10.878  0.50 15.15 ?  123  LEU   A HA   1 
ATOM   2571 H  HB2  A LEU   A 1 123 ? 20.141 -5.459  12.607  0.50 15.52 ?  123  LEU   A HB2  1 
ATOM   2572 H  HB2  B LEU   A 1 123 ? 20.119 -5.507  12.726  0.50 15.99 ?  123  LEU   A HB2  1 
ATOM   2573 H  HB3  A LEU   A 1 123 ? 21.205 -4.636  11.777  0.50 15.52 ?  123  LEU   A HB3  1 
ATOM   2574 H  HB3  B LEU   A 1 123 ? 21.246 -4.696  11.969  0.50 15.99 ?  123  LEU   A HB3  1 
ATOM   2575 H  HG   A LEU   A 1 123 ? 19.456 -3.721  10.497  0.50 16.57 ?  123  LEU   A HG   1 
ATOM   2576 H  HG   B LEU   A 1 123 ? 19.548 -3.682  10.650  0.50 16.41 ?  123  LEU   A HG   1 
ATOM   2577 H  HD11 A LEU   A 1 123 ? 17.244 -4.028  11.249  0.50 17.01 ?  123  LEU   A HD11 1 
ATOM   2578 H  HD11 B LEU   A 1 123 ? 17.331 -3.854  11.339  0.50 17.11 ?  123  LEU   A HD11 1 
ATOM   2579 H  HD12 A LEU   A 1 123 ? 17.870 -5.369  10.671  0.50 17.01 ?  123  LEU   A HD12 1 
ATOM   2580 H  HD12 B LEU   A 1 123 ? 17.870 -5.276  10.881  0.50 17.11 ?  123  LEU   A HD12 1 
ATOM   2581 H  HD13 A LEU   A 1 123 ? 17.770 -5.151  12.242  0.50 17.01 ?  123  LEU   A HD13 1 
ATOM   2582 H  HD13 B LEU   A 1 123 ? 17.751 -4.932  12.428  0.50 17.11 ?  123  LEU   A HD13 1 
ATOM   2583 H  HD21 A LEU   A 1 123 ? 18.657 -2.265  12.132  0.50 17.36 ?  123  LEU   A HD21 1 
ATOM   2584 H  HD21 B LEU   A 1 123 ? 18.865 -2.204  12.302  0.50 17.02 ?  123  LEU   A HD21 1 
ATOM   2585 H  HD22 A LEU   A 1 123 ? 19.187 -3.246  13.264  0.50 17.36 ?  123  LEU   A HD22 1 
ATOM   2586 H  HD22 B LEU   A 1 123 ? 19.359 -3.225  13.414  0.50 17.02 ?  123  LEU   A HD22 1 
ATOM   2587 H  HD23 A LEU   A 1 123 ? 20.218 -2.494  12.318  0.50 17.36 ?  123  LEU   A HD23 1 
ATOM   2588 H  HD23 B LEU   A 1 123 ? 20.413 -2.531  12.449  0.50 17.02 ?  123  LEU   A HD23 1 
ATOM   2589 N  N    A ALA   A 1 124 ? 19.757 -5.806  8.511   0.50 10.79 ?  124  ALA   A N    1 
ATOM   2590 N  N    B ALA   A 1 124 ? 19.856 -6.038  8.531   0.50 11.76 ?  124  ALA   A N    1 
ATOM   2591 C  CA   A ALA   A 1 124 ? 20.034 -5.530  7.107   0.50 10.10 ?  124  ALA   A CA   1 
ATOM   2592 C  CA   B ALA   A 1 124 ? 20.125 -5.759  7.127   0.50 12.28 ?  124  ALA   A CA   1 
ATOM   2593 C  C    A ALA   A 1 124 ? 18.769 -5.061  6.401   0.50 10.23 ?  124  ALA   A C    1 
ATOM   2594 C  C    B ALA   A 1 124 ? 18.897 -5.272  6.371   0.50 11.64 ?  124  ALA   A C    1 
ATOM   2595 O  O    A ALA   A 1 124 ? 17.647 -5.347  6.850   0.50 10.94 ?  124  ALA   A O    1 
ATOM   2596 O  O    B ALA   A 1 124 ? 17.760 -5.641  6.698   0.50 12.30 ?  124  ALA   A O    1 
ATOM   2597 C  CB   A ALA   A 1 124 ? 20.579 -6.772  6.397   0.50 10.49 ?  124  ALA   A CB   1 
ATOM   2598 C  CB   B ALA   A 1 124 ? 20.684 -6.999  6.410   0.50 13.33 ?  124  ALA   A CB   1 
ATOM   2599 H  H    A ALA   A 1 124 ? 18.934 -5.978  8.704   0.50 12.95 ?  124  ALA   A H    1 
ATOM   2600 H  H    B ALA   A 1 124 ? 19.105 -6.420  8.675   0.50 14.11 ?  124  ALA   A H    1 
ATOM   2601 H  HA   A ALA   A 1 124 ? 20.703 -4.823  7.056   0.50 12.11 ?  124  ALA   A HA   1 
ATOM   2602 H  HA   B ALA   A 1 124 ? 20.804 -5.069  7.076   0.50 14.73 ?  124  ALA   A HA   1 
ATOM   2603 H  HB1  A ALA   A 1 124 ? 20.753 -6.550  5.469   0.50 12.58 ?  124  ALA   A HB1  1 
ATOM   2604 H  HB1  B ALA   A 1 124 ? 20.855 -6.782  5.478   0.50 15.98 ?  124  ALA   A HB1  1 
ATOM   2605 H  HB2  A ALA   A 1 124 ? 21.397 -7.047  6.834   0.50 12.58 ?  124  ALA   A HB2  1 
ATOM   2606 H  HB2  B ALA   A 1 124 ? 21.515 -7.267  6.840   0.50 15.98 ?  124  ALA   A HB2  1 
ATOM   2607 H  HB3  A ALA   A 1 124 ? 19.915 -7.475  6.452   0.50 12.58 ?  124  ALA   A HB3  1 
ATOM   2608 H  HB3  B ALA   A 1 124 ? 20.037 -7.718  6.468   0.50 15.98 ?  124  ALA   A HB3  1 
ATOM   2609 N  N    A PRO   A 1 125 ? 18.925 -4.359  5.281   0.50 11.28 ?  125  PRO   A N    1 
ATOM   2610 N  N    B PRO   A 1 125 ? 19.109 -4.461  5.325   0.50 10.88 ?  125  PRO   A N    1 
ATOM   2611 C  CA   A PRO   A 1 125 ? 17.848 -4.200  4.305   0.50 11.74 ?  125  PRO   A CA   1 
ATOM   2612 C  CA   B PRO   A 1 125 ? 18.019 -4.069  4.431   0.50 11.36 ?  125  PRO   A CA   1 
ATOM   2613 C  C    A PRO   A 1 125 ? 17.966 -5.260  3.213   0.50 11.29 ?  125  PRO   A C    1 
ATOM   2614 C  C    B PRO   A 1 125 ? 17.923 -5.052  3.278   0.50 12.45 ?  125  PRO   A C    1 
ATOM   2615 O  O    A PRO   A 1 125 ? 18.962 -5.980  3.109   0.50 11.34 ?  125  PRO   A O    1 
ATOM   2616 O  O    B PRO   A 1 125 ? 18.765 -5.949  3.153   0.50 12.85 ?  125  PRO   A O    1 
ATOM   2617 C  CB   A PRO   A 1 125 ? 18.172 -2.828  3.705   0.50 12.16 ?  125  PRO   A CB   1 
ATOM   2618 C  CB   B PRO   A 1 125 ? 18.505 -2.712  3.915   0.50 10.45 ?  125  PRO   A CB   1 
ATOM   2619 C  CG   A PRO   A 1 125 ? 19.673 -2.839  3.643   0.50 12.58 ?  125  PRO   A CG   1 
ATOM   2620 C  CG   B PRO   A 1 125 ? 19.991 -2.967  3.717   0.50 10.42 ?  125  PRO   A CG   1 
ATOM   2621 C  CD   A PRO   A 1 125 ? 20.116 -3.572  4.900   0.50 11.91 ?  125  PRO   A CD   1 
ATOM   2622 C  CD   B PRO   A 1 125 ? 20.396 -3.905  4.858   0.50 10.25 ?  125  PRO   A CD   1 
ATOM   2623 H  HA   A PRO   A 1 125 ? 16.973 -4.213  4.715   0.50 14.08 ?  125  PRO   A HA   1 
ATOM   2624 H  HA   B PRO   A 1 125 ? 17.171 -3.982  4.904   0.50 13.62 ?  125  PRO   A HA   1 
ATOM   2625 H  HB2  A PRO   A 1 125 ? 17.783 -2.752  2.817   0.50 14.59 ?  125  PRO   A HB2  1 
ATOM   2626 H  HB2  B PRO   A 1 125 ? 18.063 -2.492  3.079   0.50 12.53 ?  125  PRO   A HB2  1 
ATOM   2627 H  HB3  A PRO   A 1 125 ? 17.848 -2.125  4.289   0.50 14.59 ?  125  PRO   A HB3  1 
ATOM   2628 H  HB3  B PRO   A 1 125 ? 18.349 -2.020  4.584   0.50 12.53 ?  125  PRO   A HB3  1 
ATOM   2629 H  HG2  A PRO   A 1 125 ? 19.966 -3.314  2.848   0.50 15.10 ?  125  PRO   A HG2  1 
ATOM   2630 H  HG2  B PRO   A 1 125 ? 20.136 -3.393  2.855   0.50 12.50 ?  125  PRO   A HG2  1 
ATOM   2631 H  HG3  A PRO   A 1 125 ? 20.007 -1.927  3.637   0.50 15.10 ?  125  PRO   A HG3  1 
ATOM   2632 H  HG3  B PRO   A 1 125 ? 20.478 -2.130  3.769   0.50 12.50 ?  125  PRO   A HG3  1 
ATOM   2633 H  HD2  A PRO   A 1 125 ? 20.865 -4.152  4.704   0.50 14.29 ?  125  PRO   A HD2  1 
ATOM   2634 H  HD2  B PRO   A 1 125 ? 20.976 -4.610  4.521   0.50 12.29 ?  125  PRO   A HD2  1 
ATOM   2635 H  HD3  A PRO   A 1 125 ? 20.336 -2.930  5.598   0.50 14.29 ?  125  PRO   A HD3  1 
ATOM   2636 H  HD3  B PRO   A 1 125 ? 20.830 -3.399  5.563   0.50 12.29 ?  125  PRO   A HD3  1 
ATOM   2637 N  N    A LEU   A 1 126 ? 16.932 -5.321  2.380   0.50 11.10 ?  126  LEU   A N    1 
ATOM   2638 N  N    B LEU   A 1 126 ? 16.931 -4.876  2.411   0.50 13.43 ?  126  LEU   A N    1 
ATOM   2639 C  CA   A LEU   A 1 126 ? 16.978 -6.138  1.177   0.50 11.03 ?  126  LEU   A CA   1 
ATOM   2640 C  CA   B LEU   A 1 126 ? 16.794 -5.701  1.215   0.50 13.89 ?  126  LEU   A CA   1 
ATOM   2641 C  C    A LEU   A 1 126 ? 17.920 -5.507  0.161   0.50 11.07 ?  126  LEU   A C    1 
ATOM   2642 C  C    B LEU   A 1 126 ? 17.741 -5.173  0.140   0.50 12.70 ?  126  LEU   A C    1 
ATOM   2643 O  O    A LEU   A 1 126 ? 17.730 -4.356  -0.251  0.50 12.51 ?  126  LEU   A O    1 
ATOM   2644 O  O    B LEU   A 1 126 ? 17.487 -4.122  -0.460  0.50 13.08 ?  126  LEU   A O    1 
ATOM   2645 C  CB   A LEU   A 1 126 ? 15.575 -6.262  0.593   0.50 10.79 ?  126  LEU   A CB   1 
ATOM   2646 C  CB   B LEU   A 1 126 ? 15.348 -5.627  0.738   0.50 16.98 ?  126  LEU   A CB   1 
ATOM   2647 C  CG   A LEU   A 1 126 ? 14.641 -7.182  1.381   0.50 11.32 ?  126  LEU   A CG   1 
ATOM   2648 C  CG   B LEU   A 1 126 ? 14.686 -6.857  0.134   0.50 19.89 ?  126  LEU   A CG   1 
ATOM   2649 C  CD1  A LEU   A 1 126 ? 13.215 -7.061  0.876   0.50 12.15 ?  126  LEU   A CD1  1 
ATOM   2650 C  CD1  B LEU   A 1 126 ? 14.833 -8.047  1.051   0.50 20.27 ?  126  LEU   A CD1  1 
ATOM   2651 C  CD2  A LEU   A 1 126 ? 15.133 -8.636  1.294   0.50 11.99 ?  126  LEU   A CD2  1 
ATOM   2652 C  CD2  B LEU   A 1 126 ? 13.221 -6.553  -0.096  0.50 20.34 ?  126  LEU   A CD2  1 
ATOM   2653 H  H    A LEU   A 1 126 ? 16.197 -4.900  2.483   0.50 13.31 ?  126  LEU   A H    1 
ATOM   2654 H  H    B LEU   A 1 126 ? 16.310 -4.281  2.500   0.50 16.10 ?  126  LEU   A H    1 
ATOM   2655 H  HA   A LEU   A 1 126 ? 17.309 -7.029  1.389   0.50 13.23 ?  126  LEU   A HA   1 
ATOM   2656 H  HA   B LEU   A 1 126 ? 17.025 -6.623  1.427   0.50 16.67 ?  126  LEU   A HA   1 
ATOM   2657 H  HB2  A LEU   A 1 126 ? 15.170 -5.384  0.577   0.50 12.94 ?  126  LEU   A HB2  1 
ATOM   2658 H  HB2  B LEU   A 1 126 ? 14.802 -5.371  1.496   0.50 20.37 ?  126  LEU   A HB2  1 
ATOM   2659 H  HB3  A LEU   A 1 126 ? 15.640 -6.612  -0.309  0.50 12.94 ?  126  LEU   A HB3  1 
ATOM   2660 H  HB3  B LEU   A 1 126 ? 15.299 -4.929  0.068   0.50 20.37 ?  126  LEU   A HB3  1 
ATOM   2661 H  HG   A LEU   A 1 126 ? 14.653 -6.926  2.314   0.50 13.57 ?  126  LEU   A HG   1 
ATOM   2662 H  HG   B LEU   A 1 126 ? 15.098 -7.062  -0.722  0.50 23.87 ?  126  LEU   A HG   1 
ATOM   2663 H  HD11 A LEU   A 1 126 ? 12.646 -7.657  1.388   0.50 14.58 ?  126  LEU   A HD11 1 
ATOM   2664 H  HD11 B LEU   A 1 126 ? 14.199 -8.727  0.785   0.50 24.32 ?  126  LEU   A HD11 1 
ATOM   2665 H  HD12 A LEU   A 1 126 ? 12.922 -6.145  0.985   0.50 14.58 ?  126  LEU   A HD12 1 
ATOM   2666 H  HD12 B LEU   A 1 126 ? 15.737 -8.387  0.981   0.50 24.32 ?  126  LEU   A HD12 1 
ATOM   2667 H  HD13 A LEU   A 1 126 ? 13.191 -7.309  -0.063  0.50 14.58 ?  126  LEU   A HD13 1 
ATOM   2668 H  HD13 B LEU   A 1 126 ? 14.652 -7.761  1.960   0.50 24.32 ?  126  LEU   A HD13 1 
ATOM   2669 H  HD21 A LEU   A 1 126 ? 14.442 -9.230  1.625   0.50 14.39 ?  126  LEU   A HD21 1 
ATOM   2670 H  HD21 B LEU   A 1 126 ? 12.795 -7.328  -0.494  0.50 24.41 ?  126  LEU   A HD21 1 
ATOM   2671 H  HD22 A LEU   A 1 126 ? 15.335 -8.850  0.367   0.50 14.39 ?  126  LEU   A HD22 1 
ATOM   2672 H  HD22 B LEU   A 1 126 ? 12.805 -6.351  0.758   0.50 24.41 ?  126  LEU   A HD22 1 
ATOM   2673 H  HD23 A LEU   A 1 126 ? 15.937 -8.736  1.832   0.50 14.39 ?  126  LEU   A HD23 1 
ATOM   2674 H  HD23 B LEU   A 1 126 ? 13.143 -5.791  -0.690  0.50 24.41 ?  126  LEU   A HD23 1 
ATOM   2675 N  N    A LEU   A 1 127 ? 18.932 -6.266  -0.248  0.50 11.33 ?  127  LEU   A N    1 
ATOM   2676 N  N    B LEU   A 1 127 ? 18.827 -5.898  -0.121  0.50 11.92 ?  127  LEU   A N    1 
ATOM   2677 C  CA   A LEU   A 1 127 ? 19.916 -5.761  -1.191  0.50 11.26 ?  127  LEU   A CA   1 
ATOM   2678 C  CA   B LEU   A 1 127 ? 19.821 -5.417  -1.071  0.50 11.16 ?  127  LEU   A CA   1 
ATOM   2679 C  C    A LEU   A 1 127 ? 19.288 -5.531  -2.557  0.50 10.54 ?  127  LEU   A C    1 
ATOM   2680 C  C    B LEU   A 1 127 ? 19.249 -5.339  -2.482  0.50 11.20 ?  127  LEU   A C    1 
ATOM   2681 O  O    A LEU   A 1 127 ? 18.475 -6.327  -3.036  0.50 11.16 ?  127  LEU   A O    1 
ATOM   2682 O  O    B LEU   A 1 127 ? 18.399 -6.138  -2.886  0.50 12.05 ?  127  LEU   A O    1 
ATOM   2683 C  CB   A LEU   A 1 127 ? 21.070 -6.753  -1.310  0.50 11.73 ?  127  LEU   A CB   1 
ATOM   2684 C  CB   B LEU   A 1 127 ? 21.041 -6.337  -1.076  0.50 11.70 ?  127  LEU   A CB   1 
ATOM   2685 C  CG   A LEU   A 1 127 ? 21.869 -6.987  -0.030  0.50 11.91 ?  127  LEU   A CG   1 
ATOM   2686 C  CG   B LEU   A 1 127 ? 21.844 -6.387  0.226   0.50 12.62 ?  127  LEU   A CG   1 
ATOM   2687 C  CD1  A LEU   A 1 127 ? 22.990 -7.963  -0.311  0.50 11.99 ?  127  LEU   A CD1  1 
ATOM   2688 C  CD1  B LEU   A 1 127 ? 23.010 -7.352  0.105   0.50 13.72 ?  127  LEU   A CD1  1 
ATOM   2689 C  CD2  A LEU   A 1 127 ? 22.430 -5.686  0.513   0.50 12.42 ?  127  LEU   A CD2  1 
ATOM   2690 C  CD2  B LEU   A 1 127 ? 22.340 -4.997  0.612   0.50 13.25 ?  127  LEU   A CD2  1 
ATOM   2691 H  H    A LEU   A 1 127 ? 19.072 -7.079  0.011   0.50 13.59 ?  127  LEU   A H    1 
ATOM   2692 H  H    B LEU   A 1 127 ? 19.011 -6.662  0.242   0.50 14.29 ?  127  LEU   A H    1 
ATOM   2693 H  HA   A LEU   A 1 127 ? 20.268 -4.921  -0.872  0.50 13.50 ?  127  LEU   A HA   1 
ATOM   2694 H  HA   B LEU   A 1 127 ? 20.109 -4.529  -0.802  0.50 13.38 ?  127  LEU   A HA   1 
ATOM   2695 H  HB2  A LEU   A 1 127 ? 20.716 -7.613  -1.587  0.50 14.07 ?  127  LEU   A HB2  1 
ATOM   2696 H  HB2  B LEU   A 1 127 ? 20.740 -7.239  -1.270  0.50 14.03 ?  127  LEU   A HB2  1 
ATOM   2697 H  HB3  A LEU   A 1 127 ? 21.693 -6.429  -1.978  0.50 14.07 ?  127  LEU   A HB3  1 
ATOM   2698 H  HB3  B LEU   A 1 127 ? 21.641 -6.039  -1.779  0.50 14.03 ?  127  LEU   A HB3  1 
ATOM   2699 H  HG   A LEU   A 1 127 ? 21.288 -7.381  0.647   0.50 14.29 ?  127  LEU   A HG   1 
ATOM   2700 H  HG   B LEU   A 1 127 ? 21.267 -6.707  0.937   0.50 15.14 ?  127  LEU   A HG   1 
ATOM   2701 H  HD11 A LEU   A 1 127 ? 23.455 -8.163  0.519   0.50 14.39 ?  127  LEU   A HD11 1 
ATOM   2702 H  HD11 B LEU   A 1 127 ? 23.536 -7.310  0.919   0.50 16.46 ?  127  LEU   A HD11 1 
ATOM   2703 H  HD12 A LEU   A 1 127 ? 22.617 -8.781  -0.682  0.50 14.39 ?  127  LEU   A HD12 1 
ATOM   2704 H  HD12 B LEU   A 1 127 ? 22.665 -8.249  -0.021  0.50 16.46 ?  127  LEU   A HD12 1 
ATOM   2705 H  HD13 A LEU   A 1 127 ? 23.603 -7.564  -0.945  0.50 14.39 ?  127  LEU   A HD13 1 
ATOM   2706 H  HD13 B LEU   A 1 127 ? 23.554 -7.094  -0.654  0.50 16.46 ?  127  LEU   A HD13 1 
ATOM   2707 H  HD21 A LEU   A 1 127 ? 23.072 -5.885  1.209   0.50 14.90 ?  127  LEU   A HD21 1 
ATOM   2708 H  HD21 B LEU   A 1 127 ? 22.984 -5.081  1.332   0.50 15.89 ?  127  LEU   A HD21 1 
ATOM   2709 H  HD22 A LEU   A 1 127 ? 22.861 -5.210  -0.214  0.50 14.90 ?  127  LEU   A HD22 1 
ATOM   2710 H  HD22 B LEU   A 1 127 ? 22.757 -4.585  -0.160  0.50 15.89 ?  127  LEU   A HD22 1 
ATOM   2711 H  HD23 A LEU   A 1 127 ? 21.701 -5.156  0.870   0.50 14.90 ?  127  LEU   A HD23 1 
ATOM   2712 H  HD23 B LEU   A 1 127 ? 21.585 -4.462  0.904   0.50 15.89 ?  127  LEU   A HD23 1 
ATOM   2713 N  N    A SER   A 1 128 ? 19.689 -4.435  -3.186  0.50 10.47 ?  128  SER   A N    1 
ATOM   2714 N  N    B SER   A 1 128 ? 19.731 -4.345  -3.228  0.50 11.47 ?  128  SER   A N    1 
ATOM   2715 C  CA   A SER   A 1 128 ? 19.257 -4.003  -4.509  0.50 10.92 ?  128  SER   A CA   1 
ATOM   2716 C  CA   B SER   A 1 128 ? 19.407 -4.118  -4.632  0.50 11.01 ?  128  SER   A CA   1 
ATOM   2717 C  C    A SER   A 1 128 ? 17.794 -3.570  -4.566  0.50 12.10 ?  128  SER   A C    1 
ATOM   2718 C  C    B SER   A 1 128 ? 17.977 -3.641  -4.863  0.50 10.79 ?  128  SER   A C    1 
ATOM   2719 O  O    A SER   A 1 128 ? 17.300 -3.277  -5.656  0.50 13.22 ?  128  SER   A O    1 
ATOM   2720 O  O    B SER   A 1 128 ? 17.628 -3.279  -5.989  0.50 10.83 ?  128  SER   A O    1 
ATOM   2721 C  CB   A SER   A 1 128 ? 19.587 -5.010  -5.619  0.50 10.44 ?  128  SER   A CB   1 
ATOM   2722 C  CB   B SER   A 1 128 ? 19.743 -5.337  -5.494  0.50 11.41 ?  128  SER   A CB   1 
ATOM   2723 O  OG   A SER   A 1 128 ? 20.988 -5.249  -5.675  0.50 11.43 ?  128  SER   A OG   1 
ATOM   2724 O  OG   B SER   A 1 128 ? 21.151 -5.451  -5.649  0.50 12.29 ?  128  SER   A OG   1 
ATOM   2725 H  H    A SER   A 1 128 ? 20.264 -3.892  -2.841  0.50 12.56 ?  128  SER   A H    1 
ATOM   2726 H  H    B SER   A 1 128 ? 20.291 -3.766  -2.925  0.50 13.75 ?  128  SER   A H    1 
ATOM   2727 H  HA   A SER   A 1 128 ? 19.779 -3.219  -4.712  0.50 13.10 ?  128  SER   A HA   1 
ATOM   2728 H  HA   B SER   A 1 128 ? 19.971 -3.399  -4.942  0.50 13.20 ?  128  SER   A HA   1 
ATOM   2729 H  HB2  A SER   A 1 128 ? 19.124 -5.841  -5.446  0.50 12.53 ?  128  SER   A HB2  1 
ATOM   2730 H  HB2  B SER   A 1 128 ? 19.407 -6.139  -5.069  0.50 13.68 ?  128  SER   A HB2  1 
ATOM   2731 H  HB3  A SER   A 1 128 ? 19.297 -4.640  -6.473  0.50 12.53 ?  128  SER   A HB3  1 
ATOM   2732 H  HB3  B SER   A 1 128 ? 19.338 -5.227  -6.368  0.50 13.68 ?  128  SER   A HB3  1 
ATOM   2733 H  HG   A SER   A 1 128 ? 21.396 -4.529  -5.818  0.50 13.71 ?  128  SER   A HG   1 
ATOM   2734 H  HG   B SER   A 1 128 ? 21.455 -4.758  -6.019  0.50 14.74 ?  128  SER   A HG   1 
ATOM   2735 N  N    A ALA   A 1 129 ? 17.097 -3.500  -3.430  0.50 12.80 ?  129  ALA   A N    1 
ATOM   2736 N  N    B ALA   A 1 129 ? 17.165 -3.599  -3.811  0.50 11.27 ?  129  ALA   A N    1 
ATOM   2737 C  CA   A ALA   A 1 129 ? 15.736 -2.985  -3.391  0.50 12.51 ?  129  ALA   A CA   1 
ATOM   2738 C  CA   B ALA   A 1 129 ? 15.791 -3.132  -3.904  0.50 11.66 ?  129  ALA   A CA   1 
ATOM   2739 C  C    A ALA   A 1 129 ? 15.761 -1.458  -3.363  0.50 12.38 ?  129  ALA   A C    1 
ATOM   2740 C  C    B ALA   A 1 129 ? 15.756 -1.608  -3.762  0.50 11.74 ?  129  ALA   A C    1 
ATOM   2741 O  O    A ALA   A 1 129 ? 16.821 -0.825  -3.400  0.50 12.75 ?  129  ALA   A O    1 
ATOM   2742 O  O    B ALA   A 1 129 ? 16.791 -0.934  -3.766  0.50 11.61 ?  129  ALA   A O    1 
ATOM   2743 C  CB   A ALA   A 1 129 ? 14.981 -3.548  -2.186  0.50 12.96 ?  129  ALA   A CB   1 
ATOM   2744 C  CB   B ALA   A 1 129 ? 14.918 -3.871  -2.886  0.50 11.78 ?  129  ALA   A CB   1 
ATOM   2745 H  H    A ALA   A 1 129 ? 17.390 -3.745  -2.661  0.50 15.35 ?  129  ALA   A H    1 
ATOM   2746 H  H    B ALA   A 1 129 ? 17.395 -3.835  -3.016  0.50 13.52 ?  129  ALA   A H    1 
ATOM   2747 H  HA   A ALA   A 1 129 ? 15.267 -3.263  -4.191  0.50 15.01 ?  129  ALA   A HA   1 
ATOM   2748 H  HA   B ALA   A 1 129 ? 15.455 -3.348  -4.783  0.50 13.98 ?  129  ALA   A HA   1 
ATOM   2749 H  HB1  A ALA   A 1 129 ? 14.074 -3.199  -2.185  0.50 15.55 ?  129  ALA   A HB1  1 
ATOM   2750 H  HB1  B ALA   A 1 129 ? 14.007 -3.553  -2.962  0.50 14.13 ?  129  ALA   A HB1  1 
ATOM   2751 H  HB2  A ALA   A 1 129 ? 14.961 -4.515  -2.253  0.50 15.55 ?  129  ALA   A HB2  1 
ATOM   2752 H  HB2  B ALA   A 1 129 ? 14.953 -4.824  -3.071  0.50 14.13 ?  129  ALA   A HB2  1 
ATOM   2753 H  HB3  A ALA   A 1 129 ? 15.437 -3.282  -1.372  0.50 15.55 ?  129  ALA   A HB3  1 
ATOM   2754 H  HB3  B ALA   A 1 129 ? 15.256 -3.699  -1.991  0.50 14.13 ?  129  ALA   A HB3  1 
ATOM   2755 N  N    A GLY   A 1 130 ? 14.579 -0.853  -3.300  0.50 12.77 ?  130  GLY   A N    1 
ATOM   2756 N  N    B GLY   A 1 130 ? 14.553 -1.049  -3.656  0.50 11.99 ?  130  GLY   A N    1 
ATOM   2757 C  CA   A GLY   A 1 130 ? 14.523 0.599   -3.277  0.50 13.10 ?  130  GLY   A CA   1 
ATOM   2758 C  CA   B GLY   A 1 130 ? 14.408 0.390   -3.535  0.50 12.80 ?  130  GLY   A CA   1 
ATOM   2759 C  C    A GLY   A 1 130 ? 15.143 1.185   -4.529  0.50 12.90 ?  130  GLY   A C    1 
ATOM   2760 C  C    B GLY   A 1 130 ? 15.026 1.105   -4.715  0.50 12.77 ?  130  GLY   A C    1 
ATOM   2761 O  O    A GLY   A 1 130 ? 14.852 0.752   -5.647  0.50 13.28 ?  130  GLY   A O    1 
ATOM   2762 O  O    B GLY   A 1 130 ? 14.878 0.694   -5.871  0.50 13.47 ?  130  GLY   A O    1 
ATOM   2763 H  H    A GLY   A 1 130 ? 13.807 -1.247  -3.266  0.50 15.32 ?  130  GLY   A H    1 
ATOM   2764 H  H    B GLY   A 1 130 ? 13.815 -1.483  -3.651  0.50 14.38 ?  130  GLY   A H    1 
ATOM   2765 H  HA2  A GLY   A 1 130 ? 13.600 0.898   -3.225  0.50 15.72 ?  130  GLY   A HA2  1 
ATOM   2766 H  HA2  B GLY   A 1 130 ? 13.464 0.621   -3.477  0.50 15.36 ?  130  GLY   A HA2  1 
ATOM   2767 H  HA3  A GLY   A 1 130 ? 15.006 0.935   -2.511  0.50 15.72 ?  130  GLY   A HA3  1 
ATOM   2768 H  HA3  B GLY   A 1 130 ? 14.851 0.701   -2.736  0.50 15.36 ?  130  GLY   A HA3  1 
ATOM   2769 N  N    A ILE   A 1 131 ? 16.020 2.180   -4.346  0.50 12.81 ?  131  ILE   A N    1 
ATOM   2770 N  N    B ILE   A 1 131 ? 15.744 2.194   -4.422  0.50 12.95 ?  131  ILE   A N    1 
ATOM   2771 C  CA   A ILE   A 1 131 ? 16.577 2.933   -5.469  0.50 12.85 ?  131  ILE   A CA   1 
ATOM   2772 C  CA   B ILE   A 1 131 ? 16.350 3.008   -5.467  0.50 12.99 ?  131  ILE   A CA   1 
ATOM   2773 C  C    A ILE   A 1 131 ? 17.564 2.142   -6.311  0.50 12.56 ?  131  ILE   A C    1 
ATOM   2774 C  C    B ILE   A 1 131 ? 17.411 2.261   -6.267  0.50 12.63 ?  131  ILE   A C    1 
ATOM   2775 O  O    A ILE   A 1 131 ? 17.927 2.606   -7.398  0.50 13.37 ?  131  ILE   A O    1 
ATOM   2776 O  O    B ILE   A 1 131 ? 17.886 2.786   -7.278  0.50 13.19 ?  131  ILE   A O    1 
ATOM   2777 C  CB   A ILE   A 1 131 ? 17.183 4.291   -5.046  0.50 14.29 ?  131  ILE   A CB   1 
ATOM   2778 C  CB   B ILE   A 1 131 ? 16.889 4.350   -4.912  0.50 14.38 ?  131  ILE   A CB   1 
ATOM   2779 C  CG1  A ILE   A 1 131 ? 18.449 4.108   -4.205  0.50 14.75 ?  131  ILE   A CG1  1 
ATOM   2780 C  CG1  B ILE   A 1 131 ? 18.023 4.118   -3.907  0.50 15.11 ?  131  ILE   A CG1  1 
ATOM   2781 C  CG2  A ILE   A 1 131 ? 16.156 5.109   -4.287  0.50 14.73 ?  131  ILE   A CG2  1 
ATOM   2782 C  CG2  B ILE   A 1 131 ? 15.754 5.165   -4.294  0.50 15.24 ?  131  ILE   A CG2  1 
ATOM   2783 C  CD1  A ILE   A 1 131 ? 19.120 5.428   -3.832  0.50 15.68 ?  131  ILE   A CD1  1 
ATOM   2784 C  CD1  B ILE   A 1 131 ? 18.705 5.400   -3.432  0.50 16.14 ?  131  ILE   A CD1  1 
ATOM   2785 H  H    A ILE   A 1 131 ? 16.307 2.435   -3.581  0.50 15.37 ?  131  ILE   A H    1 
ATOM   2786 H  H    B ILE   A 1 131 ? 15.883 2.485   -3.622  0.50 15.53 ?  131  ILE   A H    1 
ATOM   2787 H  HA   A ILE   A 1 131 ? 15.853 3.136   -6.068  0.50 15.41 ?  131  ILE   A HA   1 
ATOM   2788 H  HA   B ILE   A 1 131 ? 15.648 3.241   -6.090  0.50 15.58 ?  131  ILE   A HA   1 
ATOM   2789 H  HB   A ILE   A 1 131 ? 17.422 4.779   -5.850  0.50 17.15 ?  131  ILE   A HB   1 
ATOM   2790 H  HB   B ILE   A 1 131 ? 17.248 4.858   -5.655  0.50 17.25 ?  131  ILE   A HB   1 
ATOM   2791 H  HG12 A ILE   A 1 131 ? 18.218 3.647   -3.384  0.50 17.69 ?  131  ILE   A HG12 1 
ATOM   2792 H  HG12 B ILE   A 1 131 ? 17.663 3.670   -3.126  0.50 18.13 ?  131  ILE   A HG12 1 
ATOM   2793 H  HG13 A ILE   A 1 131 ? 19.095 3.586   -4.707  0.50 17.69 ?  131  ILE   A HG13 1 
ATOM   2794 H  HG13 B ILE   A 1 131 ? 18.702 3.562   -4.320  0.50 18.13 ?  131  ILE   A HG13 1 
ATOM   2795 H  HG21 A ILE   A 1 131 ? 16.500 6.003   -4.148  0.50 17.67 ?  131  ILE   A HG21 1 
ATOM   2796 H  HG21 B ILE   A 1 131 ? 16.083 6.048   -4.065  0.50 18.28 ?  131  ILE   A HG21 1 
ATOM   2797 H  HG22 A ILE   A 1 131 ? 15.341 5.147   -4.811  0.50 17.67 ?  131  ILE   A HG22 1 
ATOM   2798 H  HG22 B ILE   A 1 131 ? 15.033 5.239   -4.940  0.50 18.28 ?  131  ILE   A HG22 1 
ATOM   2799 H  HG23 A ILE   A 1 131 ? 15.981 4.680   -3.435  0.50 17.67 ?  131  ILE   A HG23 1 
ATOM   2800 H  HG23 B ILE   A 1 131 ? 15.437 4.712   -3.497  0.50 18.28 ?  131  ILE   A HG23 1 
ATOM   2801 H  HD11 A ILE   A 1 131 ? 19.992 5.244   -3.450  0.50 18.81 ?  131  ILE   A HD11 1 
ATOM   2802 H  HD11 B ILE   A 1 131 ? 19.466 5.166   -2.874  0.50 19.37 ?  131  ILE   A HD11 1 
ATOM   2803 H  HD12 A ILE   A 1 131 ? 19.217 5.972   -4.630  0.50 18.81 ?  131  ILE   A HD12 1 
ATOM   2804 H  HD12 B ILE   A 1 131 ? 19.007 5.903   -4.205  0.50 19.37 ?  131  ILE   A HD12 1 
ATOM   2805 H  HD13 A ILE   A 1 131 ? 18.567 5.893   -3.182  0.50 18.81 ?  131  ILE   A HD13 1 
ATOM   2806 H  HD13 B ILE   A 1 131 ? 18.072 5.927   -2.920  0.50 19.37 ?  131  ILE   A HD13 1 
ATOM   2807 N  N    A PHE   A 1 132 ? 18.002 0.964   -5.860  0.50 11.92 ?  132  PHE   A N    1 
ATOM   2808 N  N    B PHE   A 1 132 ? 17.785 1.041   -5.856  0.50 12.39 ?  132  PHE   A N    1 
ATOM   2809 C  CA   A PHE   A 1 132 ? 18.816 0.113   -6.723  0.50 12.05 ?  132  PHE   A CA   1 
ATOM   2810 C  CA   B PHE   A 1 132 ? 18.717 0.234   -6.639  0.50 12.88 ?  132  PHE   A CA   1 
ATOM   2811 C  C    A PHE   A 1 132 ? 17.980 -0.627  -7.769  0.50 12.47 ?  132  PHE   A C    1 
ATOM   2812 C  C    B PHE   A 1 132 ? 18.050 -0.501  -7.801  0.50 13.73 ?  132  PHE   A C    1 
ATOM   2813 O  O    A PHE   A 1 132 ? 18.550 -1.291  -8.641  0.50 13.18 ?  132  PHE   A O    1 
ATOM   2814 O  O    B PHE   A 1 132 ? 18.761 -1.048  -8.650  0.50 14.86 ?  132  PHE   A O    1 
ATOM   2815 C  CB   A PHE   A 1 132 ? 19.657 -0.870  -5.896  0.50 11.69 ?  132  PHE   A CB   1 
ATOM   2816 C  CB   B PHE   A 1 132 ? 19.464 -0.765  -5.746  0.50 12.34 ?  132  PHE   A CB   1 
ATOM   2817 C  CG   A PHE   A 1 132 ? 20.874 -0.251  -5.226  0.50 11.94 ?  132  PHE   A CG   1 
ATOM   2818 C  CG   B PHE   A 1 132 ? 20.681 -0.195  -5.049  0.50 12.17 ?  132  PHE   A CG   1 
ATOM   2819 C  CD1  A PHE   A 1 132 ? 20.750 0.819   -4.353  0.50 12.94 ?  132  PHE   A CD1  1 
ATOM   2820 C  CD1  B PHE   A 1 132 ? 20.549 0.697   -3.998  0.50 12.92 ?  132  PHE   A CD1  1 
ATOM   2821 C  CD2  A PHE   A 1 132 ? 22.138 -0.782  -5.443  0.50 13.05 ?  132  PHE   A CD2  1 
ATOM   2822 C  CD2  B PHE   A 1 132 ? 21.956 -0.595  -5.420  0.50 12.67 ?  132  PHE   A CD2  1 
ATOM   2823 C  CE1  A PHE   A 1 132 ? 21.870 1.366   -3.733  0.50 13.30 ?  132  PHE   A CE1  1 
ATOM   2824 C  CE1  B PHE   A 1 132 ? 21.666 1.203   -3.352  0.50 12.99 ?  132  PHE   A CE1  1 
ATOM   2825 C  CE2  A PHE   A 1 132 ? 23.254 -0.244  -4.825  0.50 13.64 ?  132  PHE   A CE2  1 
ATOM   2826 C  CE2  B PHE   A 1 132 ? 23.074 -0.097  -4.775  0.50 13.05 ?  132  PHE   A CE2  1 
ATOM   2827 C  CZ   A PHE   A 1 132 ? 23.118 0.832   -3.970  0.50 13.36 ?  132  PHE   A CZ   1 
ATOM   2828 C  CZ   B PHE   A 1 132 ? 22.926 0.806   -3.741  0.50 12.73 ?  132  PHE   A CZ   1 
ATOM   2829 H  H    A PHE   A 1 132 ? 17.848 0.640   -5.074  0.50 14.30 ?  132  PHE   A H    1 
ATOM   2830 H  H    B PHE   A 1 132 ? 17.521 0.665   -5.127  0.50 14.86 ?  132  PHE   A H    1 
ATOM   2831 H  HA   A PHE   A 1 132 ? 19.440 0.677   -7.199  0.50 14.46 ?  132  PHE   A HA   1 
ATOM   2832 H  HA   B PHE   A 1 132 ? 19.380 0.825   -7.022  0.50 15.45 ?  132  PHE   A HA   1 
ATOM   2833 H  HB2  A PHE   A 1 132 ? 19.102 -1.239  -5.194  0.50 14.02 ?  132  PHE   A HB2  1 
ATOM   2834 H  HB2  B PHE   A 1 132 ? 18.859 -1.082  -5.059  0.50 14.81 ?  132  PHE   A HB2  1 
ATOM   2835 H  HB3  A PHE   A 1 132 ? 19.974 -1.586  -6.475  0.50 14.02 ?  132  PHE   A HB3  1 
ATOM   2836 H  HB3  B PHE   A 1 132 ? 19.760 -1.511  -6.292  0.50 14.81 ?  132  PHE   A HB3  1 
ATOM   2837 H  HD1  A PHE   A 1 132 ? 19.913 1.183   -4.186  0.50 15.52 ?  132  PHE   A HD1  1 
ATOM   2838 H  HD1  B PHE   A 1 132 ? 19.702 0.971   -3.732  0.50 15.50 ?  132  PHE   A HD1  1 
ATOM   2839 H  HD2  A PHE   A 1 132 ? 22.244 -1.507  -6.019  0.50 15.65 ?  132  PHE   A HD2  1 
ATOM   2840 H  HD2  B PHE   A 1 132 ? 22.064 -1.201  -6.120  0.50 15.20 ?  132  PHE   A HD2  1 
ATOM   2841 H  HE1  A PHE   A 1 132 ? 21.778 2.090   -3.154  0.50 15.95 ?  132  PHE   A HE1  1 
ATOM   2842 H  HE1  B PHE   A 1 132 ? 21.566 1.809   -2.654  0.50 15.58 ?  132  PHE   A HE1  1 
ATOM   2843 H  HE2  A PHE   A 1 132 ? 24.098 -0.603  -4.991  0.50 16.36 ?  132  PHE   A HE2  1 
ATOM   2844 H  HE2  B PHE   A 1 132 ? 23.925 -0.365  -5.045  0.50 15.65 ?  132  PHE   A HE2  1 
ATOM   2845 H  HZ   A PHE   A 1 132 ? 23.871 1.199   -3.557  0.50 16.03 ?  132  PHE   A HZ   1 
ATOM   2846 H  HZ   B PHE   A 1 132 ? 23.677 1.145   -3.308  0.50 15.28 ?  132  PHE   A HZ   1 
ATOM   2847 N  N    A GLY   A 1 133 ? 16.651 -0.545  -7.696  0.50 12.99 ?  133  GLY   A N    1 
ATOM   2848 N  N    B GLY   A 1 133 ? 16.715 -0.547  -7.862  0.50 13.97 ?  133  GLY   A N    1 
ATOM   2849 C  CA   A GLY   A 1 133 ? 15.803 -0.907  -8.816  0.50 13.57 ?  133  GLY   A CA   1 
ATOM   2850 C  CA   B GLY   A 1 133 ? 16.009 -0.916  -9.070  0.50 14.24 ?  133  GLY   A CA   1 
ATOM   2851 C  C    A GLY   A 1 133 ? 15.556 -2.381  -9.051  0.50 13.77 ?  133  GLY   A C    1 
ATOM   2852 C  C    B GLY   A 1 133 ? 15.499 -2.343  -9.150  0.50 14.25 ?  133  GLY   A C    1 
ATOM   2853 O  O    A GLY   A 1 133 ? 15.062 -2.731  -10.131 0.50 14.63 ?  133  GLY   A O    1 
ATOM   2854 O  O    B GLY   A 1 133 ? 14.629 -2.615  -9.988  0.50 14.97 ?  133  GLY   A O    1 
ATOM   2855 H  H    A GLY   A 1 133 ? 16.215 -0.278  -7.002  0.50 15.58 ?  133  GLY   A H    1 
ATOM   2856 H  H    B GLY   A 1 133 ? 16.194 -0.355  -7.202  0.50 16.76 ?  133  GLY   A H    1 
ATOM   2857 H  HA2  A GLY   A 1 133 ? 14.937 -0.490  -8.700  0.50 16.27 ?  133  GLY   A HA2  1 
ATOM   2858 H  HA2  B GLY   A 1 133 ? 15.246 -0.332  -9.176  0.50 17.09 ?  133  GLY   A HA2  1 
ATOM   2859 H  HA3  A GLY   A 1 133 ? 16.196 -0.557  -9.628  0.50 16.27 ?  133  GLY   A HA3  1 
ATOM   2860 H  HA3  B GLY   A 1 133 ? 16.598 -0.781  -9.828  0.50 17.09 ?  133  GLY   A HA3  1 
ATOM   2861 N  N    A ALA   A 1 134 ? 15.880 -3.257  -8.103  0.50 13.08 ?  134  ALA   A N    1 
ATOM   2862 N  N    B ALA   A 1 134 ? 16.011 -3.264  -8.333  0.50 13.55 ?  134  ALA   A N    1 
ATOM   2863 C  CA   A ALA   A 1 134 ? 15.533 -4.661  -8.252  0.50 13.45 ?  134  ALA   A CA   1 
ATOM   2864 C  CA   B ALA   A 1 134 ? 15.655 -4.663  -8.522  0.50 13.64 ?  134  ALA   A CA   1 
ATOM   2865 C  C    A ALA   A 1 134 ? 14.181 -4.946  -7.606  0.50 14.01 ?  134  ALA   A C    1 
ATOM   2866 C  C    B ALA   A 1 134 ? 14.320 -4.993  -7.853  0.50 14.15 ?  134  ALA   A C    1 
ATOM   2867 O  O    A ALA   A 1 134 ? 13.680 -4.177  -6.782  0.50 14.96 ?  134  ALA   A O    1 
ATOM   2868 O  O    B ALA   A 1 134 ? 13.767 -4.216  -7.071  0.50 14.98 ?  134  ALA   A O    1 
ATOM   2869 C  CB   A ALA   A 1 134 ? 16.600 -5.565  -7.636  0.50 13.81 ?  134  ALA   A CB   1 
ATOM   2870 C  CB   B ALA   A 1 134 ? 16.766 -5.581  -8.012  0.50 14.33 ?  134  ALA   A CB   1 
ATOM   2871 H  H    A ALA   A 1 134 ? 16.305 -3.064  -7.372  0.50 15.69 ?  134  ALA   A H    1 
ATOM   2872 H  H    B ALA   A 1 134 ? 16.560 -3.106  -7.679  0.50 16.25 ?  134  ALA   A H    1 
ATOM   2873 H  HA   A ALA   A 1 134 ? 15.471 -4.871  -9.196  0.50 16.14 ?  134  ALA   A HA   1 
ATOM   2874 H  HA   B ALA   A 1 134 ? 15.554 -4.825  -9.467  0.50 16.37 ?  134  ALA   A HA   1 
ATOM   2875 H  HB1  A ALA   A 1 134 ? 16.344 -6.489  -7.777  0.50 16.56 ?  134  ALA   A HB1  1 
ATOM   2876 H  HB1  B ALA   A 1 134 ? 16.508 -6.502  -8.169  0.50 17.19 ?  134  ALA   A HB1  1 
ATOM   2877 H  HB2  A ALA   A 1 134 ? 17.450 -5.387  -8.069  0.50 16.56 ?  134  ALA   A HB2  1 
ATOM   2878 H  HB2  B ALA   A 1 134 ? 17.585 -5.380  -8.494  0.50 17.19 ?  134  ALA   A HB2  1 
ATOM   2879 H  HB3  A ALA   A 1 134 ? 16.664 -5.378  -6.688  0.50 16.56 ?  134  ALA   A HB3  1 
ATOM   2880 H  HB3  B ALA   A 1 134 ? 16.896 -5.428  -7.064  0.50 17.19 ?  134  ALA   A HB3  1 
ATOM   2881 N  N    A ASP   A 1 135 ? 13.600 -6.071  -7.994  0.50 14.46 ?  135  ASP   A N    1 
ATOM   2882 N  N    B ASP   A 1 135 ? 13.808 -6.177  -8.175  0.50 14.90 ?  135  ASP   A N    1 
ATOM   2883 C  CA   A ASP   A 1 135 ? 12.349 -6.535  -7.407  0.50 15.41 ?  135  ASP   A CA   1 
ATOM   2884 C  CA   B ASP   A 1 135 ? 12.547 -6.663  -7.619  0.50 15.81 ?  135  ASP   A CA   1 
ATOM   2885 C  C    A ASP   A 1 135 ? 12.607 -7.022  -5.986  0.50 15.02 ?  135  ASP   A C    1 
ATOM   2886 C  C    B ASP   A 1 135 ? 12.751 -7.057  -6.162  0.50 15.52 ?  135  ASP   A C    1 
ATOM   2887 O  O    A ASP   A 1 135 ? 13.341 -8.003  -5.805  0.50 14.96 ?  135  ASP   A O    1 
ATOM   2888 O  O    B ASP   A 1 135 ? 13.572 -7.940  -5.879  0.50 14.91 ?  135  ASP   A O    1 
ATOM   2889 C  CB   A ASP   A 1 135 ? 11.831 -7.694  -8.253  0.50 17.52 ?  135  ASP   A CB   1 
ATOM   2890 C  CB   B ASP   A 1 135 ? 12.094 -7.875  -8.434  0.50 18.05 ?  135  ASP   A CB   1 
ATOM   2891 C  CG   A ASP   A 1 135 ? 10.475 -8.212  -7.783  0.50 19.67 ?  135  ASP   A CG   1 
ATOM   2892 C  CG   B ASP   A 1 135 ? 10.920 -8.622  -7.807  0.50 20.33 ?  135  ASP   A CG   1 
ATOM   2893 O  OD1  A ASP   A 1 135 ? 10.001 -7.779  -6.708  0.50 20.46 ?  135  ASP   A OD1  1 
ATOM   2894 O  OD1  B ASP   A 1 135 ? 10.237 -8.072  -6.920  0.50 21.04 ?  135  ASP   A OD1  1 
ATOM   2895 O  OD2  A ASP   A 1 135 ? 9.870  -9.034  -8.508  0.50 21.20 -1 135  ASP   A OD2  1 
ATOM   2896 O  OD2  B ASP   A 1 135 ? 10.689 -9.782  -8.208  0.50 22.21 -1 135  ASP   A OD2  1 
ATOM   2897 H  H    A ASP   A 1 135 ? 13.906 -6.587  -8.608  0.50 17.34 ?  135  ASP   A H    1 
ATOM   2898 H  H    B ASP   A 1 135 ? 14.178 -6.728  -8.720  0.50 17.87 ?  135  ASP   A H    1 
ATOM   2899 H  HA   A ASP   A 1 135 ? 11.687 -5.821  -7.413  0.50 18.48 ?  135  ASP   A HA   1 
ATOM   2900 H  HA   B ASP   A 1 135 ? 11.872 -5.970  -7.689  0.50 18.96 ?  135  ASP   A HA   1 
ATOM   2901 H  HB2  A ASP   A 1 135 ? 11.714 -7.396  -9.164  0.50 21.02 ?  135  ASP   A HB2  1 
ATOM   2902 H  HB2  B ASP   A 1 135 ? 11.824 -7.576  -9.315  0.50 21.65 ?  135  ASP   A HB2  1 
ATOM   2903 H  HB3  A ASP   A 1 135 ? 12.492 -8.413  -8.225  0.50 21.02 ?  135  ASP   A HB3  1 
ATOM   2904 H  HB3  B ASP   A 1 135 ? 12.830 -8.498  -8.502  0.50 21.65 ?  135  ASP   A HB3  1 
ATOM   2905 N  N    A PRO   A 1 136 ? 12.041 -6.385  -4.957  0.50 15.14 ?  136  PRO   A N    1 
ATOM   2906 N  N    B PRO   A 1 136 ? 12.041 -6.442  -5.213  0.50 16.01 ?  136  PRO   A N    1 
ATOM   2907 C  CA   A PRO   A 1 136 ? 12.308 -6.846  -3.584  0.50 15.31 ?  136  PRO   A CA   1 
ATOM   2908 C  CA   B PRO   A 1 136 ? 12.260 -6.787  -3.799  0.50 15.74 ?  136  PRO   A CA   1 
ATOM   2909 C  C    A PRO   A 1 136 ? 11.883 -8.281  -3.311  0.50 14.54 ?  136  PRO   A C    1 
ATOM   2910 C  C    B PRO   A 1 136 ? 11.851 -8.207  -3.446  0.50 15.15 ?  136  PRO   A C    1 
ATOM   2911 O  O    A PRO   A 1 136 ? 12.480 -8.934  -2.446  0.50 14.33 ?  136  PRO   A O    1 
ATOM   2912 O  O    B PRO   A 1 136 ? 12.452 -8.804  -2.544  0.50 14.91 ?  136  PRO   A O    1 
ATOM   2913 C  CB   A PRO   A 1 136 ? 11.538 -5.840  -2.716  0.50 16.19 ?  136  PRO   A CB   1 
ATOM   2914 C  CB   B PRO   A 1 136 ? 11.418 -5.744  -3.052  0.50 16.45 ?  136  PRO   A CB   1 
ATOM   2915 C  CG   A PRO   A 1 136 ? 10.529 -5.226  -3.636  0.50 16.73 ?  136  PRO   A CG   1 
ATOM   2916 C  CG   B PRO   A 1 136 ? 10.353 -5.360  -4.032  0.50 17.22 ?  136  PRO   A CG   1 
ATOM   2917 C  CD   A PRO   A 1 136 ? 11.177 -5.192  -4.979  0.50 15.43 ?  136  PRO   A CD   1 
ATOM   2918 C  CD   B PRO   A 1 136 ? 10.999 -5.415  -5.378  0.50 16.82 ?  136  PRO   A CD   1 
ATOM   2919 H  HA   A PRO   A 1 136 ? 13.256 -6.760  -3.391  0.50 18.36 ?  136  PRO   A HA   1 
ATOM   2920 H  HA   B PRO   A 1 136 ? 13.193 -6.664  -3.562  0.50 18.88 ?  136  PRO   A HA   1 
ATOM   2921 H  HB2  A PRO   A 1 136 ? 11.101 -6.308  -1.988  0.50 19.42 ?  136  PRO   A HB2  1 
ATOM   2922 H  HB2  B PRO   A 1 136 ? 11.030 -6.140  -2.256  0.50 19.73 ?  136  PRO   A HB2  1 
ATOM   2923 H  HB3  A PRO   A 1 136 ? 12.149 -5.168  -2.377  0.50 19.42 ?  136  PRO   A HB3  1 
ATOM   2924 H  HB3  B PRO   A 1 136 ? 11.970 -4.978  -2.822  0.50 19.73 ?  136  PRO   A HB3  1 
ATOM   2925 H  HG2  A PRO   A 1 136 ? 9.731  -5.778  -3.661  0.50 20.07 ?  136  PRO   A HG2  1 
ATOM   2926 H  HG2  B PRO   A 1 136 ? 9.624  -5.994  -3.979  0.50 20.66 ?  136  PRO   A HG2  1 
ATOM   2927 H  HG3  A PRO   A 1 136 ? 10.317 -4.330  -3.338  0.50 20.07 ?  136  PRO   A HG3  1 
ATOM   2928 H  HG3  B PRO   A 1 136 ? 10.046 -4.463  -3.840  0.50 20.66 ?  136  PRO   A HG3  1 
ATOM   2929 H  HD2  A PRO   A 1 136 ? 10.503 -5.270  -5.678  0.50 18.51 ?  136  PRO   A HD2  1 
ATOM   2930 H  HD2  B PRO   A 1 136 ? 10.357 -5.695  -6.050  0.50 20.17 ?  136  PRO   A HD2  1 
ATOM   2931 H  HD3  A PRO   A 1 136 ? 11.705 -4.385  -5.085  0.50 18.51 ?  136  PRO   A HD3  1 
ATOM   2932 H  HD3  B PRO   A 1 136 ? 11.398 -4.559  -5.603  0.50 20.17 ?  136  PRO   A HD3  1 
ATOM   2933 N  N    A ILE   A 1 137 ? 10.853 -8.788  -3.996  0.50 14.89 ?  137  ILE   A N    1 
ATOM   2934 N  N    B ILE   A 1 137 ? 10.831 -8.761  -4.107  0.50 15.46 ?  137  ILE   A N    1 
ATOM   2935 C  CA   A ILE   A 1 137 ? 10.476 -10.191 -3.826  0.50 15.23 ?  137  ILE   A CA   1 
ATOM   2936 C  CA   B ILE   A 1 137 ? 10.466 -10.155 -3.866  0.50 15.83 ?  137  ILE   A CA   1 
ATOM   2937 C  C    A ILE   A 1 137 ? 11.630 -11.095 -4.237  0.50 14.92 ?  137  ILE   A C    1 
ATOM   2938 C  C    B ILE   A 1 137 ? 11.631 -11.063 -4.230  0.50 15.26 ?  137  ILE   A C    1 
ATOM   2939 O  O    A ILE   A 1 137 ? 11.949 -12.077 -3.552  0.50 14.92 ?  137  ILE   A O    1 
ATOM   2940 O  O    B ILE   A 1 137 ? 11.955 -12.017 -3.509  0.50 15.27 ?  137  ILE   A O    1 
ATOM   2941 C  CB   A ILE   A 1 137 ? 9.183  -10.507 -4.603  0.50 16.32 ?  137  ILE   A CB   1 
ATOM   2942 C  CB   B ILE   A 1 137 ? 9.196  -10.523 -4.657  0.50 17.21 ?  137  ILE   A CB   1 
ATOM   2943 C  CG1  A ILE   A 1 137 ? 7.992  -9.763  -3.987  0.50 17.61 ?  137  ILE   A CG1  1 
ATOM   2944 C  CG1  B ILE   A 1 137 ? 8.057  -9.544  -4.348  0.50 18.59 ?  137  ILE   A CG1  1 
ATOM   2945 C  CG2  A ILE   A 1 137 ? 8.927  -12.015 -4.632  0.50 16.65 ?  137  ILE   A CG2  1 
ATOM   2946 C  CG2  B ILE   A 1 137 ? 8.782  -11.954 -4.343  0.50 17.59 ?  137  ILE   A CG2  1 
ATOM   2947 C  CD1  A ILE   A 1 137 ? 6.689  -9.968  -4.726  0.50 18.63 ?  137  ILE   A CD1  1 
ATOM   2948 C  CD1  B ILE   A 1 137 ? 6.824  -9.758  -5.201  0.50 19.76 ?  137  ILE   A CD1  1 
ATOM   2949 H  H    A ILE   A 1 137 ? 10.366 -8.350  -4.553  0.50 17.86 ?  137  ILE   A H    1 
ATOM   2950 H  H    B ILE   A 1 137 ? 10.350 -8.355  -4.692  0.50 18.54 ?  137  ILE   A H    1 
ATOM   2951 H  HA   A ILE   A 1 137 ? 10.304 -10.355 -2.890  0.50 18.27 ?  137  ILE   A HA   1 
ATOM   2952 H  HA   B ILE   A 1 137 ? 10.277 -10.275 -2.925  0.50 18.99 ?  137  ILE   A HA   1 
ATOM   2953 H  HB   A ILE   A 1 137 ? 9.288  -10.199 -5.515  0.50 19.57 ?  137  ILE   A HB   1 
ATOM   2954 H  HB   B ILE   A 1 137 ? 9.397  -10.464 -5.604  0.50 20.64 ?  137  ILE   A HB   1 
ATOM   2955 H  HG12 A ILE   A 1 137 ? 7.868  -10.069 -3.074  0.50 21.12 ?  137  ILE   A HG12 1 
ATOM   2956 H  HG12 B ILE   A 1 137 ? 7.802  -9.649  -3.419  0.50 22.30 ?  137  ILE   A HG12 1 
ATOM   2957 H  HG13 A ILE   A 1 137 ? 8.186  -8.809  -3.986  0.50 21.12 ?  137  ILE   A HG13 1 
ATOM   2958 H  HG13 B ILE   A 1 137 ? 8.365  -8.637  -4.504  0.50 22.30 ?  137  ILE   A HG13 1 
ATOM   2959 H  HG21 A ILE   A 1 137 ? 8.099  -12.193 -5.104  0.50 19.97 ?  137  ILE   A HG21 1 
ATOM   2960 H  HG21 B ILE   A 1 137 ? 7.965  -12.160 -4.822  0.50 21.10 ?  137  ILE   A HG21 1 
ATOM   2961 H  HG22 A ILE   A 1 137 ? 9.651  -12.455 -5.094  0.50 19.97 ?  137  ILE   A HG22 1 
ATOM   2962 H  HG22 B ILE   A 1 137 ? 9.486  -12.557 -4.625  0.50 21.10 ?  137  ILE   A HG22 1 
ATOM   2963 H  HG23 A ILE   A 1 137 ? 8.862  -12.338 -3.721  0.50 19.97 ?  137  ILE   A HG23 1 
ATOM   2964 H  HG23 B ILE   A 1 137 ? 8.636  -12.035 -3.389  0.50 21.10 ?  137  ILE   A HG23 1 
ATOM   2965 H  HD11 A ILE   A 1 137 ? 5.997  -9.516  -4.232  0.50 22.35 ?  137  ILE   A HD11 1 
ATOM   2966 H  HD11 B ILE   A 1 137 ? 6.231  -9.001  -5.090  0.50 23.71 ?  137  ILE   A HD11 1 
ATOM   2967 H  HD12 A ILE   A 1 137 ? 6.767  -9.594  -5.620  0.50 22.35 ?  137  ILE   A HD12 1 
ATOM   2968 H  HD12 B ILE   A 1 137 ? 7.092  -9.837  -6.130  0.50 23.71 ?  137  ILE   A HD12 1 
ATOM   2969 H  HD13 A ILE   A 1 137 ? 6.483  -10.913 -4.778  0.50 22.35 ?  137  ILE   A HD13 1 
ATOM   2970 H  HD13 B ILE   A 1 137 ? 6.379  -10.572 -4.916  0.50 23.71 ?  137  ILE   A HD13 1 
ATOM   2971 N  N    . HIS   A 1 138 ? 12.270 -10.780 -5.365  1.00 15.16 ?  138  HIS   A N    1 
ATOM   2972 C  CA   . HIS   A 1 138 ? 13.438 -11.538 -5.781  1.00 14.61 ?  138  HIS   A CA   1 
ATOM   2973 C  C    . HIS   A 1 138 ? 14.576 -11.389 -4.778  1.00 14.27 ?  138  HIS   A C    1 
ATOM   2974 O  O    . HIS   A 1 138 ? 15.236 -12.374 -4.426  1.00 14.66 ?  138  HIS   A O    1 
ATOM   2975 C  CB   . HIS   A 1 138 ? 13.858 -11.088 -7.177  1.00 15.55 ?  138  HIS   A CB   1 
ATOM   2976 C  CG   . HIS   A 1 138 ? 15.122 -11.726 -7.649  1.00 16.50 ?  138  HIS   A CG   1 
ATOM   2977 N  ND1  . HIS   A 1 138 ? 15.224 -13.078 -7.896  1.00 17.67 ?  138  HIS   A ND1  1 
ATOM   2978 C  CD2  . HIS   A 1 138 ? 16.345 -11.202 -7.897  1.00 16.71 ?  138  HIS   A CD2  1 
ATOM   2979 C  CE1  . HIS   A 1 138 ? 16.453 -13.358 -8.290  1.00 18.11 ?  138  HIS   A CE1  1 
ATOM   2980 N  NE2  . HIS   A 1 138 ? 17.154 -12.238 -8.298  1.00 17.37 ?  138  HIS   A NE2  1 
ATOM   2981 H  H    A HIS   A 1 138 ? 12.049 -10.137 -5.898  0.50 18.19 ?  138  HIS   A H    1 
ATOM   2982 H  H    B HIS   A 1 138 ? 12.040 -10.155 -5.915  0.50 18.19 ?  138  HIS   A H    1 
ATOM   2983 H  HA   . HIS   A 1 138 ? 13.203 -12.474 -5.832  1.00 17.53 ?  138  HIS   A HA   1 
ATOM   2984 H  HB2  . HIS   A 1 138 ? 13.151 -11.319 -7.809  1.00 18.66 ?  138  HIS   A HB2  1 
ATOM   2985 H  HB3  . HIS   A 1 138 ? 13.990 -10.128 -7.177  1.00 18.66 ?  138  HIS   A HB3  1 
ATOM   2986 H  HD1  . HIS   A 1 138 ? 14.581 -13.649 -7.815  1.00 21.20 ?  138  HIS   A HD1  1 
ATOM   2987 H  HD2  . HIS   A 1 138 ? 16.583 -10.309 -7.818  1.00 20.04 ?  138  HIS   A HD2  1 
ATOM   2988 H  HE1  . HIS   A 1 138 ? 16.768 -14.202 -8.516  1.00 21.73 ?  138  HIS   A HE1  1 
ATOM   2989 N  N    . SER   A 1 139 ? 14.821 -10.168 -4.299  1.00 13.68 ?  139  SER   A N    1 
ATOM   2990 C  CA   . SER   A 1 139 ? 15.895 -9.972  -3.337  1.00 13.44 ?  139  SER   A CA   1 
ATOM   2991 C  C    . SER   A 1 139 ? 15.680 -10.815 -2.086  1.00 13.14 ?  139  SER   A C    1 
ATOM   2992 O  O    . SER   A 1 139 ? 16.628 -11.411 -1.561  1.00 13.26 ?  139  SER   A O    1 
ATOM   2993 C  CB   . SER   A 1 139 ? 16.018 -8.492  -2.984  1.00 13.17 ?  139  SER   A CB   1 
ATOM   2994 O  OG   . SER   A 1 139 ? 17.101 -8.324  -2.088  1.00 13.73 ?  139  SER   A OG   1 
ATOM   2995 H  H    . SER   A 1 139 ? 14.386 -9.455  -4.509  1.00 16.41 ?  139  SER   A H    1 
ATOM   2996 H  HA   . SER   A 1 139 ? 16.733 -10.246 -3.740  1.00 16.12 ?  139  SER   A HA   1 
ATOM   2997 H  HB2  . SER   A 1 139 ? 16.186 -7.975  -3.789  1.00 15.80 ?  139  SER   A HB2  1 
ATOM   2998 H  HB3  . SER   A 1 139 ? 15.200 -8.191  -2.558  1.00 15.80 ?  139  SER   A HB3  1 
ATOM   2999 H  HG   . SER   A 1 139 ? 17.192 -7.513  -1.882  1.00 16.47 ?  139  SER   A HG   1 
ATOM   3000 N  N    . LEU   A 1 140 ? 14.446 -10.875 -1.587  1.00 13.13 ?  140  LEU   A N    1 
ATOM   3001 C  CA   . LEU   A 1 140 ? 14.175 -11.691 -0.409  1.00 13.17 ?  140  LEU   A CA   1 
ATOM   3002 C  C    . LEU   A 1 140 ? 14.438 -13.165 -0.689  1.00 13.09 ?  140  LEU   A C    1 
ATOM   3003 O  O    . LEU   A 1 140 ? 15.000 -13.876 0.156   1.00 13.95 ?  140  LEU   A O    1 
ATOM   3004 C  CB   . LEU   A 1 140 ? 12.733 -11.471 0.040   1.00 13.39 ?  140  LEU   A CB   1 
ATOM   3005 C  CG   . LEU   A 1 140 ? 12.290 -12.329 1.220   1.00 14.44 ?  140  LEU   A CG   1 
ATOM   3006 C  CD1  . LEU   A 1 140 ? 13.193 -12.133 2.429   1.00 15.01 ?  140  LEU   A CD1  1 
ATOM   3007 C  CD2  . LEU   A 1 140 ? 10.833 -12.027 1.581   1.00 15.51 ?  140  LEU   A CD2  1 
ATOM   3008 H  H    . LEU   A 1 140 ? 13.765 -10.454 -1.901  1.00 15.75 ?  140  LEU   A H    1 
ATOM   3009 H  HA   . LEU   A 1 140 ? 14.763 -11.415 0.310   1.00 15.80 ?  140  LEU   A HA   1 
ATOM   3010 H  HB2  . LEU   A 1 140 ? 12.629 -10.549 0.300   1.00 16.06 ?  140  LEU   A HB2  1 
ATOM   3011 H  HB3  . LEU   A 1 140 ? 12.147 -11.675 -0.704  1.00 16.06 ?  140  LEU   A HB3  1 
ATOM   3012 H  HG   . LEU   A 1 140 ? 12.326 -13.270 0.966   1.00 17.32 ?  140  LEU   A HG   1 
ATOM   3013 H  HD11 . LEU   A 1 140 ? 12.816 -12.612 3.185   1.00 18.01 ?  140  LEU   A HD11 1 
ATOM   3014 H  HD12 . LEU   A 1 140 ? 14.071 -12.492 2.221   1.00 18.01 ?  140  LEU   A HD12 1 
ATOM   3015 H  HD13 . LEU   A 1 140 ? 13.251 -11.192 2.626   1.00 18.01 ?  140  LEU   A HD13 1 
ATOM   3016 H  HD21 . LEU   A 1 140 ? 10.568 -12.587 2.332   1.00 18.60 ?  140  LEU   A HD21 1 
ATOM   3017 H  HD22 . LEU   A 1 140 ? 10.758 -11.093 1.826   1.00 18.60 ?  140  LEU   A HD22 1 
ATOM   3018 H  HD23 . LEU   A 1 140 ? 10.268 -12.217 0.816   1.00 18.60 ?  140  LEU   A HD23 1 
ATOM   3019 N  N    . ARG   A 1 141 ? 14.044 -13.639 -1.874  1.00 13.66 ?  141  ARG   A N    1 
ATOM   3020 C  CA   . ARG   A 1 141 ? 14.283 -15.030 -2.244  1.00 15.28 ?  141  ARG   A CA   1 
ATOM   3021 C  C    . ARG   A 1 141 ? 15.778 -15.336 -2.261  1.00 14.32 ?  141  ARG   A C    1 
ATOM   3022 O  O    . ARG   A 1 141 ? 16.225 -16.352 -1.713  1.00 14.45 ?  141  ARG   A O    1 
ATOM   3023 C  CB   . ARG   A 1 141 ? 13.668 -15.281 -3.621  1.00 17.40 ?  141  ARG   A CB   1 
ATOM   3024 C  CG   . ARG   A 1 141 ? 13.642 -16.727 -4.060  1.00 20.51 ?  141  ARG   A CG   1 
ATOM   3025 C  CD   . ARG   A 1 141 ? 12.605 -17.488 -3.288  1.00 22.82 ?  141  ARG   A CD   1 
ATOM   3026 N  NE   . ARG   A 1 141 ? 13.219 -18.297 -2.249  1.00 23.62 ?  141  ARG   A NE   1 
ATOM   3027 C  CZ   . ARG   A 1 141 ? 12.547 -18.879 -1.265  1.00 24.67 ?  141  ARG   A CZ   1 
ATOM   3028 N  NH1  . ARG   A 1 141 ? 11.256 -18.659 -1.083  1.00 24.18 ?  141  ARG   A NH1  1 
ATOM   3029 N  NH2  . ARG   A 1 141 ? 13.190 -19.695 -0.436  1.00 25.71 ?  141  ARG   A NH2  1 
ATOM   3030 H  H    . ARG   A 1 141 ? 13.638 -13.178 -2.477  1.00 16.38 ?  141  ARG   A H    1 
ATOM   3031 H  HA   . ARG   A 1 141 ? 13.858 -15.617 -1.604  1.00 18.33 ?  141  ARG   A HA   1 
ATOM   3032 H  HB2  . ARG   A 1 141 ? 12.753 -14.957 -3.616  1.00 20.87 ?  141  ARG   A HB2  1 
ATOM   3033 H  HB3  . ARG   A 1 141 ? 14.179 -14.789 -4.281  1.00 20.87 ?  141  ARG   A HB3  1 
ATOM   3034 H  HG2  . ARG   A 1 141 ? 13.421 -16.779 -5.005  1.00 24.60 ?  141  ARG   A HG2  1 
ATOM   3035 H  HG3  . ARG   A 1 141 ? 14.508 -17.137 -3.896  1.00 24.60 ?  141  ARG   A HG3  1 
ATOM   3036 H  HD2  . ARG   A 1 141 ? 11.995 -16.865 -2.859  1.00 27.37 ?  141  ARG   A HD2  1 
ATOM   3037 H  HD3  . ARG   A 1 141 ? 12.113 -18.071 -3.892  1.00 27.37 ?  141  ARG   A HD3  1 
ATOM   3038 H  HE   . ARG   A 1 141 ? 14.049 -18.495 -2.336  1.00 28.33 ?  141  ARG   A HE   1 
ATOM   3039 H  HH11 . ARG   A 1 141 ? 10.824 -18.143 -1.618  1.00 29.01 ?  141  ARG   A HH11 1 
ATOM   3040 H  HH12 . ARG   A 1 141 ? 10.840 -19.045 -0.434  1.00 29.01 ?  141  ARG   A HH12 1 
ATOM   3041 H  HH21 . ARG   A 1 141 ? 14.031 -19.844 -0.546  1.00 30.84 ?  141  ARG   A HH21 1 
ATOM   3042 H  HH22 . ARG   A 1 141 ? 12.770 -20.071 0.214   1.00 30.84 ?  141  ARG   A HH22 1 
ATOM   3043 N  N    . VAL   A 1 142 ? 16.571 -14.467 -2.893  1.00 13.53 ?  142  VAL   A N    1 
ATOM   3044 C  CA   . VAL   A 1 142 ? 18.014 -14.681 -2.926  1.00 13.51 ?  142  VAL   A CA   1 
ATOM   3045 C  C    . VAL   A 1 142 ? 18.583 -14.668 -1.517  1.00 12.99 ?  142  VAL   A C    1 
ATOM   3046 O  O    . VAL   A 1 142 ? 19.446 -15.483 -1.173  1.00 13.34 ?  142  VAL   A O    1 
ATOM   3047 C  CB   . VAL   A 1 142 ? 18.708 -13.655 -3.841  1.00 13.98 ?  142  VAL   A CB   1 
ATOM   3048 C  CG1  . VAL   A 1 142 ? 20.216 -13.859 -3.800  1.00 13.64 ?  142  VAL   A CG1  1 
ATOM   3049 C  CG2  . VAL   A 1 142 ? 18.205 -13.782 -5.270  1.00 14.96 ?  142  VAL   A CG2  1 
ATOM   3050 H  H    . VAL   A 1 142 ? 16.305 -13.751 -3.295  1.00 16.23 ?  142  VAL   A H    1 
ATOM   3051 H  HA   . VAL   A 1 142 ? 18.187 -15.552 -3.300  1.00 16.21 ?  142  VAL   A HA   1 
ATOM   3052 H  HB   . VAL   A 1 142 ? 18.518 -12.751 -3.530  1.00 16.77 ?  142  VAL   A HB   1 
ATOM   3053 H  HG11 . VAL   A 1 142 ? 20.625 -13.367 -4.532  1.00 16.37 ?  142  VAL   A HG11 1 
ATOM   3054 H  HG12 . VAL   A 1 142 ? 20.563 -13.524 -2.954  1.00 16.37 ?  142  VAL   A HG12 1 
ATOM   3055 H  HG13 . VAL   A 1 142 ? 20.411 -14.802 -3.887  1.00 16.37 ?  142  VAL   A HG13 1 
ATOM   3056 H  HG21 . VAL   A 1 142 ? 18.677 -13.144 -5.830  1.00 17.94 ?  142  VAL   A HG21 1 
ATOM   3057 H  HG22 . VAL   A 1 142 ? 18.383 -14.685 -5.580  1.00 17.94 ?  142  VAL   A HG22 1 
ATOM   3058 H  HG23 . VAL   A 1 142 ? 17.257 -13.604 -5.286  1.00 17.94 ?  142  VAL   A HG23 1 
ATOM   3059 N  N    . CYS   A 1 143 ? 18.123 -13.739 -0.680  1.00 13.03 ?  143  CYS   A N    1 
ATOM   3060 C  CA   . CYS   A 1 143 ? 18.587 -13.692 0.701   1.00 12.80 ?  143  CYS   A CA   1 
ATOM   3061 C  C    . CYS   A 1 143 ? 18.356 -15.030 1.394   1.00 13.07 ?  143  CYS   A C    1 
ATOM   3062 O  O    . CYS   A 1 143 ? 19.274 -15.620 1.973   1.00 13.22 ?  143  CYS   A O    1 
ATOM   3063 C  CB   . CYS   A 1 143 ? 17.856 -12.579 1.444   1.00 13.63 ?  143  CYS   A CB   1 
ATOM   3064 S  SG   . CYS   A 1 143 ? 18.356 -12.407 3.165   1.00 13.81 ?  143  CYS   A SG   1 
ATOM   3065 H  H    . CYS   A 1 143 ? 17.548 -13.140 -0.885  1.00 15.64 ?  143  CYS   A H    1 
ATOM   3066 H  HA   . CYS   A 1 143 ? 19.537 -13.504 0.717   1.00 15.36 ?  143  CYS   A HA   1 
ATOM   3067 H  HB2  . CYS   A 1 143 ? 18.027 -11.737 0.994   1.00 16.35 ?  143  CYS   A HB2  1 
ATOM   3068 H  HB3  . CYS   A 1 143 ? 16.907 -12.767 1.431   1.00 16.35 ?  143  CYS   A HB3  1 
ATOM   3069 H  HG   . CYS   A 1 143 ? 17.779 -11.471 3.643   1.00 16.57 ?  143  CYS   A HG   1 
ATOM   3070 N  N    . VAL   A 1 144 ? 17.127 -15.531 1.334   1.00 14.03 ?  144  VAL   A N    1 
ATOM   3071 C  CA   . VAL   A 1 144 ? 16.784 -16.763 2.034   1.00 15.61 ?  144  VAL   A CA   1 
ATOM   3072 C  C    . VAL   A 1 144 ? 17.593 -17.936 1.503   1.00 15.07 ?  144  VAL   A C    1 
ATOM   3073 O  O    . VAL   A 1 144 ? 17.963 -18.844 2.258   1.00 15.66 ?  144  VAL   A O    1 
ATOM   3074 C  CB   . VAL   A 1 144 ? 15.265 -16.996 1.926   1.00 18.35 ?  144  VAL   A CB   1 
ATOM   3075 C  CG1  . VAL   A 1 144 ? 14.895 -18.430 2.251   1.00 20.01 ?  144  VAL   A CG1  1 
ATOM   3076 C  CG2  . VAL   A 1 144 ? 14.532 -16.002 2.829   1.00 18.03 ?  144  VAL   A CG2  1 
ATOM   3077 H  H    . VAL   A 1 144 ? 16.473 -15.172 0.900   1.00 16.83 ?  144  VAL   A H    1 
ATOM   3078 H  HA   . VAL   A 1 144 ? 16.993 -16.661 2.968   1.00 18.72 ?  144  VAL   A HA   1 
ATOM   3079 H  HB   . VAL   A 1 144 ? 14.980 -16.816 1.011   1.00 22.02 ?  144  VAL   A HB   1 
ATOM   3080 H  HG11 . VAL   A 1 144 ? 13.939 -18.475 2.434   1.00 24.00 ?  144  VAL   A HG11 1 
ATOM   3081 H  HG12 . VAL   A 1 144 ? 15.106 -18.993 1.491   1.00 24.00 ?  144  VAL   A HG12 1 
ATOM   3082 H  HG13 . VAL   A 1 144 ? 15.390 -18.714 3.031   1.00 24.00 ?  144  VAL   A HG13 1 
ATOM   3083 H  HG21 . VAL   A 1 144 ? 13.573 -16.132 2.741   1.00 21.63 ?  144  VAL   A HG21 1 
ATOM   3084 H  HG22 . VAL   A 1 144 ? 14.801 -16.150 3.748   1.00 21.63 ?  144  VAL   A HG22 1 
ATOM   3085 H  HG23 . VAL   A 1 144 ? 14.762 -15.095 2.561   1.00 21.63 ?  144  VAL   A HG23 1 
ATOM   3086 N  N    . ASP   A 1 145 ? 17.858 -17.952 0.199   1.00 15.02 ?  145  ASP   A N    1 
ATOM   3087 C  CA   . ASP   A 1 145 ? 18.565 -19.056 -0.440  1.00 15.98 ?  145  ASP   A CA   1 
ATOM   3088 C  C    . ASP   A 1 145 ? 20.086 -18.912 -0.404  1.00 15.58 ?  145  ASP   A C    1 
ATOM   3089 O  O    . ASP   A 1 145 ? 20.789 -19.802 -0.901  1.00 17.49 ?  145  ASP   A O    1 
ATOM   3090 C  CB   . ASP   A 1 145 ? 18.107 -19.191 -1.894  1.00 17.54 ?  145  ASP   A CB   1 
ATOM   3091 C  CG   . ASP   A 1 145 ? 16.665 -19.634 -2.013  1.00 19.54 ?  145  ASP   A CG   1 
ATOM   3092 O  OD1  . ASP   A 1 145 ? 16.114 -20.182 -1.036  1.00 20.21 ?  145  ASP   A OD1  1 
ATOM   3093 O  OD2  . ASP   A 1 145 ? 16.086 -19.426 -3.093  1.00 20.95 -1 145  ASP   A OD2  1 
ATOM   3094 H  H    . ASP   A 1 145 ? 17.613 -17.335 -0.348  1.00 18.02 ?  145  ASP   A H    1 
ATOM   3095 H  HA   . ASP   A 1 145 ? 18.330 -19.880 0.016   1.00 19.17 ?  145  ASP   A HA   1 
ATOM   3096 H  HB2  . ASP   A 1 145 ? 18.195 -18.333 -2.337  1.00 21.04 ?  145  ASP   A HB2  1 
ATOM   3097 H  HB3  . ASP   A 1 145 ? 18.655 -19.855 -2.339  1.00 21.04 ?  145  ASP   A HB3  1 
ATOM   3098 N  N    . THR   A 1 146 ? 20.613 -17.830 0.163   1.00 13.75 ?  146  THR   A N    1 
ATOM   3099 C  CA   . THR   A 1 146 ? 22.050 -17.580 0.174   1.00 13.29 ?  146  THR   A CA   1 
ATOM   3100 C  C    . THR   A 1 146 ? 22.613 -17.394 1.569   1.00 13.19 ?  146  THR   A C    1 
ATOM   3101 O  O    . THR   A 1 146 ? 23.690 -17.925 1.873   1.00 14.18 ?  146  THR   A O    1 
ATOM   3102 C  CB   . THR   A 1 146 ? 22.369 -16.324 -0.659  1.00 12.91 ?  146  THR   A CB   1 
ATOM   3103 O  OG1  . THR   A 1 146 ? 21.838 -16.480 -1.974  1.00 13.63 ?  146  THR   A OG1  1 
ATOM   3104 C  CG2  . THR   A 1 146 ? 23.871 -16.092 -0.748  1.00 13.35 ?  146  THR   A CG2  1 
ATOM   3105 H  H    . THR   A 1 146 ? 20.152 -17.217 0.555   1.00 16.50 ?  146  THR   A H    1 
ATOM   3106 H  HA   . THR   A 1 146 ? 22.507 -18.328 -0.231  1.00 15.94 ?  146  THR   A HA   1 
ATOM   3107 H  HB   . THR   A 1 146 ? 21.968 -15.548 -0.239  1.00 15.49 ?  146  THR   A HB   1 
ATOM   3108 H  HG1  . THR   A 1 146 ? 21.000 -16.558 -1.937  1.00 16.35 ?  146  THR   A HG1  1 
ATOM   3109 H  HG21 . THR   A 1 146 ? 24.063 -15.431 -1.431  1.00 16.02 ?  146  THR   A HG21 1 
ATOM   3110 H  HG22 . THR   A 1 146 ? 24.211 -15.771 0.103   1.00 16.02 ?  146  THR   A HG22 1 
ATOM   3111 H  HG23 . THR   A 1 146 ? 24.321 -16.920 -0.976  1.00 16.02 ?  146  THR   A HG23 1 
ATOM   3112 N  N    . VAL   A 1 147 ? 21.936 -16.621 2.410   1.00 13.13 ?  147  VAL   A N    1 
ATOM   3113 C  CA   . VAL   A 1 147 ? 22.431 -16.332 3.746   1.00 13.05 ?  147  VAL   A CA   1 
ATOM   3114 C  C    . VAL   A 1 147 ? 22.116 -17.506 4.660   1.00 13.42 ?  147  VAL   A C    1 
ATOM   3115 O  O    . VAL   A 1 147 ? 20.972 -17.977 4.722   1.00 14.19 ?  147  VAL   A O    1 
ATOM   3116 C  CB   . VAL   A 1 147 ? 21.813 -15.032 4.276   1.00 13.12 ?  147  VAL   A CB   1 
ATOM   3117 C  CG1  . VAL   A 1 147 ? 22.367 -14.723 5.644   1.00 14.22 ?  147  VAL   A CG1  1 
ATOM   3118 C  CG2  . VAL   A 1 147 ? 22.067 -13.876 3.309   1.00 13.58 ?  147  VAL   A CG2  1 
ATOM   3119 H  H    . VAL   A 1 147 ? 21.177 -16.252 2.229   1.00 15.75 ?  147  VAL   A H    1 
ATOM   3120 H  HA   . VAL   A 1 147 ? 23.394 -16.217 3.710   1.00 15.66 ?  147  VAL   A HA   1 
ATOM   3121 H  HB   . VAL   A 1 147 ? 20.856 -15.145 4.361   1.00 15.74 ?  147  VAL   A HB   1 
ATOM   3122 H  HG11 . VAL   A 1 147 ? 22.127 -13.819 5.885   1.00 17.06 ?  147  VAL   A HG11 1 
ATOM   3123 H  HG12 . VAL   A 1 147 ? 21.987 -15.349 6.284   1.00 17.06 ?  147  VAL   A HG12 1 
ATOM   3124 H  HG13 . VAL   A 1 147 ? 23.331 -14.819 5.621   1.00 17.06 ?  147  VAL   A HG13 1 
ATOM   3125 H  HG21 . VAL   A 1 147 ? 21.740 -13.054 3.709   1.00 16.29 ?  147  VAL   A HG21 1 
ATOM   3126 H  HG22 . VAL   A 1 147 ? 23.016 -13.808 3.139   1.00 16.29 ?  147  VAL   A HG22 1 
ATOM   3127 H  HG23 . VAL   A 1 147 ? 21.591 -14.050 2.481   1.00 16.29 ?  147  VAL   A HG23 1 
ATOM   3128 N  N    . ARG   A 1 148 ? 23.141 -17.981 5.367   1.00 13.56 ?  148  ARG   A N    1 
ATOM   3129 C  CA   . ARG   A 1 148 ? 23.009 -19.062 6.326   1.00 13.79 ?  148  ARG   A CA   1 
ATOM   3130 C  C    . ARG   A 1 148 ? 23.145 -18.595 7.763   1.00 14.34 ?  148  ARG   A C    1 
ATOM   3131 O  O    . ARG   A 1 148 ? 22.741 -19.320 8.678   1.00 16.16 ?  148  ARG   A O    1 
ATOM   3132 C  CB   . ARG   A 1 148 ? 24.038 -20.160 6.037   1.00 14.29 ?  148  ARG   A CB   1 
ATOM   3133 C  CG   . ARG   A 1 148 ? 23.879 -20.780 4.664   1.00 15.65 ?  148  ARG   A CG   1 
ATOM   3134 C  CD   . ARG   A 1 148 ? 24.964 -21.811 4.375   1.00 16.78 ?  148  ARG   A CD   1 
ATOM   3135 N  NE   . ARG   A 1 148 ? 26.299 -21.226 4.403   1.00 16.74 ?  148  ARG   A NE   1 
ATOM   3136 C  CZ   . ARG   A 1 148 ? 26.809 -20.485 3.429   1.00 15.76 ?  148  ARG   A CZ   1 
ATOM   3137 N  NH1  . ARG   A 1 148 ? 26.137 -20.252 2.312   1.00 16.07 ?  148  ARG   A NH1  1 
ATOM   3138 N  NH2  . ARG   A 1 148 ? 28.026 -19.962 3.578   1.00 15.97 ?  148  ARG   A NH2  1 
ATOM   3139 H  H    . ARG   A 1 148 ? 23.947 -17.677 5.296   1.00 16.27 ?  148  ARG   A H    1 
ATOM   3140 H  HA   . ARG   A 1 148 ? 22.131 -19.451 6.228   1.00 16.54 ?  148  ARG   A HA   1 
ATOM   3141 H  HB2  . ARG   A 1 148 ? 24.929 -19.790 6.093   1.00 17.14 ?  148  ARG   A HB2  1 
ATOM   3142 H  HB3  . ARG   A 1 148 ? 23.930 -20.871 6.692   1.00 17.14 ?  148  ARG   A HB3  1 
ATOM   3143 H  HG2  . ARG   A 1 148 ? 23.014 -21.218 4.615   1.00 18.77 ?  148  ARG   A HG2  1 
ATOM   3144 H  HG3  . ARG   A 1 148 ? 23.935 -20.078 3.997   1.00 18.77 ?  148  ARG   A HG3  1 
ATOM   3145 H  HD2  . ARG   A 1 148 ? 24.926 -22.508 5.048   1.00 20.13 ?  148  ARG   A HD2  1 
ATOM   3146 H  HD3  . ARG   A 1 148 ? 24.813 -22.190 3.495   1.00 20.13 ?  148  ARG   A HD3  1 
ATOM   3147 H  HE   . ARG   A 1 148 ? 26.788 -21.371 5.093   1.00 20.09 ?  148  ARG   A HE   1 
ATOM   3148 H  HH11 . ARG   A 1 148 ? 25.352 -20.580 2.202   1.00 19.28 ?  148  ARG   A HH11 1 
ATOM   3149 H  HH12 . ARG   A 1 148 ? 26.488 -19.766 1.692   1.00 19.28 ?  148  ARG   A HH12 1 
ATOM   3150 H  HH21 . ARG   A 1 148 ? 28.471 -20.103 4.299   1.00 19.16 ?  148  ARG   A HH21 1 
ATOM   3151 H  HH22 . ARG   A 1 148 ? 28.369 -19.476 2.952   1.00 19.16 ?  148  ARG   A HH22 1 
ATOM   3152 N  N    . THR   A 1 149 ? 23.697 -17.405 7.977   1.00 14.40 ?  149  THR   A N    1 
ATOM   3153 C  CA   . THR   A 1 149 ? 23.776 -16.810 9.296   1.00 14.44 ?  149  THR   A CA   1 
ATOM   3154 C  C    . THR   A 1 149 ? 22.451 -16.115 9.610   1.00 13.99 ?  149  THR   A C    1 
ATOM   3155 O  O    . THR   A 1 149 ? 21.511 -16.110 8.804   1.00 14.64 ?  149  THR   A O    1 
ATOM   3156 C  CB   . THR   A 1 149 ? 24.970 -15.868 9.352   1.00 14.73 ?  149  THR   A CB   1 
ATOM   3157 O  OG1  . THR   A 1 149 ? 24.840 -14.931 8.280   1.00 14.98 ?  149  THR   A OG1  1 
ATOM   3158 C  CG2  . THR   A 1 149 ? 26.274 -16.656 9.208   1.00 15.54 ?  149  THR   A CG2  1 
ATOM   3159 H  H    . THR   A 1 149 ? 24.041 -16.912 7.358   1.00 17.28 ?  149  THR   A H    1 
ATOM   3160 H  HA   . THR   A 1 149 ? 23.907 -17.515 9.951   1.00 17.32 ?  149  THR   A HA   1 
ATOM   3161 H  HB   . THR   A 1 149 ? 24.972 -15.404 10.201  1.00 17.67 ?  149  THR   A HB   1 
ATOM   3162 H  HG1  . THR   A 1 149 ? 25.486 -14.399 8.287   1.00 17.97 ?  149  THR   A HG1  1 
ATOM   3163 H  HG21 . THR   A 1 149 ? 27.032 -16.057 9.271   1.00 18.64 ?  149  THR   A HG21 1 
ATOM   3164 H  HG22 . THR   A 1 149 ? 26.341 -17.325 9.910   1.00 18.64 ?  149  THR   A HG22 1 
ATOM   3165 H  HG23 . THR   A 1 149 ? 26.301 -17.107 8.347   1.00 18.64 ?  149  THR   A HG23 1 
ATOM   3166 N  N    . ASN   A 1 150 ? 22.338 -15.574 10.817  1.00 14.51 ?  150  ASN   A N    1 
ATOM   3167 C  CA   . ASN   A 1 150 ? 21.056 -15.072 11.312  1.00 15.31 ?  150  ASN   A CA   1 
ATOM   3168 C  C    . ASN   A 1 150 ? 20.872 -13.629 10.861  1.00 14.60 ?  150  ASN   A C    1 
ATOM   3169 O  O    . ASN   A 1 150 ? 21.614 -12.734 11.285  1.00 15.60 ?  150  ASN   A O    1 
ATOM   3170 C  CB   . ASN   A 1 150 ? 20.998 -15.197 12.830  1.00 18.13 ?  150  ASN   A CB   1 
ATOM   3171 C  CG   . ASN   A 1 150 ? 20.845 -16.628 13.278  1.00 22.17 ?  150  ASN   A CG   1 
ATOM   3172 O  OD1  . ASN   A 1 150 ? 20.239 -17.439 12.579  1.00 23.37 ?  150  ASN   A OD1  1 
ATOM   3173 N  ND2  . ASN   A 1 150 ? 21.406 -16.955 14.440  1.00 24.79 ?  150  ASN   A ND2  1 
ATOM   3174 H  H    . ASN   A 1 150 ? 22.987 -15.487 11.371  1.00 17.40 ?  150  ASN   A H    1 
ATOM   3175 H  HA   . ASN   A 1 150 ? 20.336 -15.608 10.940  1.00 18.37 ?  150  ASN   A HA   1 
ATOM   3176 H  HB2  . ASN   A 1 150 ? 21.817 -14.850 13.213  1.00 21.75 ?  150  ASN   A HB2  1 
ATOM   3177 H  HB3  . ASN   A 1 150 ? 20.235 -14.698 13.164  1.00 21.75 ?  150  ASN   A HB3  1 
ATOM   3178 H  HD21 . ASN   A 1 150 ? 21.346 -17.764 14.744  1.00 29.75 ?  150  ASN   A HD21 1 
ATOM   3179 H  HD22 . ASN   A 1 150 ? 21.825 -16.362 14.903  1.00 29.75 ?  150  ASN   A HD22 1 
ATOM   3180 N  N    . VAL   A 1 151 ? 19.888 -13.400 9.997   1.00 14.30 ?  151  VAL   A N    1 
ATOM   3181 C  CA   . VAL   A 1 151 ? 19.676 -12.093 9.400   1.00 14.02 ?  151  VAL   A CA   1 
ATOM   3182 C  C    . VAL   A 1 151 ? 18.288 -11.582 9.765   1.00 13.95 ?  151  VAL   A C    1 
ATOM   3183 O  O    . VAL   A 1 151 ? 17.280 -12.292 9.618   1.00 15.10 ?  151  VAL   A O    1 
ATOM   3184 C  CB   . VAL   A 1 151 ? 19.974 -12.080 7.884   1.00 15.12 ?  151  VAL   A CB   1 
ATOM   3185 C  CG1  . VAL   A 1 151 ? 19.151 -13.097 7.129   1.00 16.14 ?  151  VAL   A CG1  1 
ATOM   3186 C  CG2  . VAL   A 1 151 ? 19.782 -10.675 7.310   1.00 15.34 ?  151  VAL   A CG2  1 
ATOM   3187 H  H    . VAL   A 1 151 ? 19.324 -13.996 9.737   1.00 17.16 ?  151  VAL   A H    1 
ATOM   3188 H  HA   . VAL   A 1 151 ? 20.316 -11.479 9.801   1.00 16.82 ?  151  VAL   A HA   1 
ATOM   3189 H  HB   . VAL   A 1 151 ? 20.911 -12.311 7.752   1.00 18.13 ?  151  VAL   A HB   1 
ATOM   3190 H  HG11 . VAL   A 1 151 ? 19.330 -13.011 6.177   1.00 19.36 ?  151  VAL   A HG11 1 
ATOM   3191 H  HG12 . VAL   A 1 151 ? 19.398 -13.987 7.429   1.00 19.36 ?  151  VAL   A HG12 1 
ATOM   3192 H  HG13 . VAL   A 1 151 ? 18.211 -12.937 7.302   1.00 19.36 ?  151  VAL   A HG13 1 
ATOM   3193 H  HG21 . VAL   A 1 151 ? 20.107 -10.661 6.393   1.00 18.40 ?  151  VAL   A HG21 1 
ATOM   3194 H  HG22 . VAL   A 1 151 ? 18.839 -10.452 7.326   1.00 18.40 ?  151  VAL   A HG22 1 
ATOM   3195 H  HG23 . VAL   A 1 151 ? 20.284 -10.041 7.844   1.00 18.40 ?  151  VAL   A HG23 1 
ATOM   3196 N  N    . TYR   A 1 152 ? 18.270 -10.342 10.263  1.00 13.65 ?  152  TYR   A N    1 
ATOM   3197 C  CA   . TYR   A 1 152 ? 17.072 -9.607  10.639  1.00 13.37 ?  152  TYR   A CA   1 
ATOM   3198 C  C    . TYR   A 1 152 ? 16.880 -8.503  9.612   1.00 13.27 ?  152  TYR   A C    1 
ATOM   3199 O  O    . TYR   A 1 152 ? 17.657 -7.540  9.572   1.00 13.72 ?  152  TYR   A O    1 
ATOM   3200 C  CB   . TYR   A 1 152 ? 17.242 -9.058  12.052  1.00 13.91 ?  152  TYR   A CB   1 
ATOM   3201 C  CG   . TYR   A 1 152 ? 17.207 -10.188 13.048  1.00 15.12 ?  152  TYR   A CG   1 
ATOM   3202 C  CD1  . TYR   A 1 152 ? 18.341 -10.945 13.322  1.00 16.26 ?  152  TYR   A CD1  1 
ATOM   3203 C  CD2  . TYR   A 1 152 ? 16.028 -10.538 13.675  1.00 15.06 ?  152  TYR   A CD2  1 
ATOM   3204 C  CE1  . TYR   A 1 152 ? 18.301 -12.008 14.208  1.00 17.47 ?  152  TYR   A CE1  1 
ATOM   3205 C  CE2  . TYR   A 1 152 ? 15.972 -11.603 14.564  1.00 16.37 ?  152  TYR   A CE2  1 
ATOM   3206 C  CZ   . TYR   A 1 152 ? 17.115 -12.331 14.828  1.00 17.52 ?  152  TYR   A CZ   1 
ATOM   3207 O  OH   . TYR   A 1 152 ? 17.069 -13.394 15.710  1.00 19.86 ?  152  TYR   A OH   1 
ATOM   3208 H  H    . TYR   A 1 152 ? 18.990 -9.873  10.377  1.00 16.37 ?  152  TYR   A H    1 
ATOM   3209 H  HA   . TYR   A 1 152 ? 16.306 -10.202 10.617  1.00 16.04 ?  152  TYR   A HA   1 
ATOM   3210 H  HB2  . TYR   A 1 152 ? 18.099 -8.614  12.125  1.00 16.69 ?  152  TYR   A HB2  1 
ATOM   3211 H  HB3  . TYR   A 1 152 ? 16.519 -8.450  12.253  1.00 16.69 ?  152  TYR   A HB3  1 
ATOM   3212 H  HD1  . TYR   A 1 152 ? 19.142 -10.732 12.898  1.00 19.50 ?  152  TYR   A HD1  1 
ATOM   3213 H  HD2  . TYR   A 1 152 ? 15.253 -10.053 13.497  1.00 18.07 ?  152  TYR   A HD2  1 
ATOM   3214 H  HE1  . TYR   A 1 152 ? 19.072 -12.496 14.384  1.00 20.96 ?  152  TYR   A HE1  1 
ATOM   3215 H  HE2  . TYR   A 1 152 ? 15.172 -11.816 14.985  1.00 19.64 ?  152  TYR   A HE2  1 
ATOM   3216 H  HH   . TYR   A 1 152 ? 16.290 -13.467 16.019  1.00 23.83 ?  152  TYR   A HH   1 
ATOM   3217 N  N    . LEU   A 1 153 ? 15.868 -8.665  8.765   1.00 13.36 ?  153  LEU   A N    1 
ATOM   3218 C  CA   . LEU   A 1 153 ? 15.600 -7.749  7.668   1.00 13.77 ?  153  LEU   A CA   1 
ATOM   3219 C  C    . LEU   A 1 153 ? 14.597 -6.685  8.087   1.00 14.00 ?  153  LEU   A C    1 
ATOM   3220 O  O    . LEU   A 1 153 ? 13.500 -7.004  8.564   1.00 15.07 ?  153  LEU   A O    1 
ATOM   3221 C  CB   . LEU   A 1 153 ? 15.039 -8.507  6.463   1.00 14.22 ?  153  LEU   A CB   1 
ATOM   3222 C  CG   . LEU   A 1 153 ? 15.973 -9.518  5.798   1.00 13.89 ?  153  LEU   A CG   1 
ATOM   3223 C  CD1  . LEU   A 1 153 ? 15.195 -10.399 4.833   1.00 14.43 ?  153  LEU   A CD1  1 
ATOM   3224 C  CD2  . LEU   A 1 153 ? 17.116 -8.809  5.081   1.00 14.10 ?  153  LEU   A CD2  1 
ATOM   3225 H  H    . LEU   A 1 153 ? 15.303 -9.321  8.813   1.00 16.03 ?  153  LEU   A H    1 
ATOM   3226 H  HA   . LEU   A 1 153 ? 16.427 -7.321  7.413   1.00 16.51 ?  153  LEU   A HA   1 
ATOM   3227 H  HB2  . LEU   A 1 153 ? 14.250 -8.986  6.753   1.00 17.05 ?  153  LEU   A HB2  1 
ATOM   3228 H  HB3  . LEU   A 1 153 ? 14.791 -7.851  5.792   1.00 17.05 ?  153  LEU   A HB3  1 
ATOM   3229 H  HG   . LEU   A 1 153 ? 16.361 -10.081 6.486   1.00 16.66 ?  153  LEU   A HG   1 
ATOM   3230 H  HD11 . LEU   A 1 153 ? 15.775 -11.113 4.526   1.00 17.31 ?  153  LEU   A HD11 1 
ATOM   3231 H  HD12 . LEU   A 1 153 ? 14.430 -10.768 5.295   1.00 17.31 ?  153  LEU   A HD12 1 
ATOM   3232 H  HD13 . LEU   A 1 153 ? 14.904 -9.860  4.082   1.00 17.31 ?  153  LEU   A HD13 1 
ATOM   3233 H  HD21 . LEU   A 1 153 ? 17.691 -9.475  4.676   1.00 16.92 ?  153  LEU   A HD21 1 
ATOM   3234 H  HD22 . LEU   A 1 153 ? 16.746 -8.229  4.397   1.00 16.92 ?  153  LEU   A HD22 1 
ATOM   3235 H  HD23 . LEU   A 1 153 ? 17.619 -8.284  5.723   1.00 16.92 ?  153  LEU   A HD23 1 
ATOM   3236 N  N    A ALA   A 1 154 ? 14.971 -5.427  7.879   0.50 13.92 ?  154  ALA   A N    1 
ATOM   3237 N  N    B ALA   A 1 154 ? 14.974 -5.423  7.914   0.50 13.88 ?  154  ALA   A N    1 
ATOM   3238 C  CA   A ALA   A 1 154 ? 14.083 -4.289  8.069   0.50 14.43 ?  154  ALA   A CA   1 
ATOM   3239 C  CA   B ALA   A 1 154 ? 14.115 -4.284  8.218   0.50 14.36 ?  154  ALA   A CA   1 
ATOM   3240 C  C    A ALA   A 1 154 ? 13.576 -3.828  6.709   0.50 14.59 ?  154  ALA   A C    1 
ATOM   3241 C  C    B ALA   A 1 154 ? 13.663 -3.671  6.899   0.50 14.52 ?  154  ALA   A C    1 
ATOM   3242 O  O    A ALA   A 1 154 ? 14.374 -3.497  5.824   0.50 14.57 ?  154  ALA   A O    1 
ATOM   3243 O  O    B ALA   A 1 154 ? 14.501 -3.273  6.082   0.50 14.12 ?  154  ALA   A O    1 
ATOM   3244 C  CB   A ALA   A 1 154 ? 14.817 -3.139  8.757   0.50 14.79 ?  154  ALA   A CB   1 
ATOM   3245 C  CB   B ALA   A 1 154 ? 14.868 -3.251  9.058   0.50 14.69 ?  154  ALA   A CB   1 
ATOM   3246 H  H    A ALA   A 1 154 ? 15.767 -5.201  7.628   0.50 16.69 ?  154  ALA   A H    1 
ATOM   3247 H  H    B ALA   A 1 154 ? 15.748 -5.190  7.611   0.50 16.65 ?  154  ALA   A H    1 
ATOM   3248 H  HA   A ALA   A 1 154 ? 13.329 -4.549  8.617   0.50 17.32 ?  154  ALA   A HA   1 
ATOM   3249 H  HA   B ALA   A 1 154 ? 13.337 -4.575  8.718   0.50 17.23 ?  154  ALA   A HA   1 
ATOM   3250 H  HB1  A ALA   A 1 154 ? 14.203 -2.395  8.865   0.50 17.74 ?  154  ALA   A HB1  1 
ATOM   3251 H  HB1  B ALA   A 1 154 ? 14.281 -2.502  9.250   0.50 17.63 ?  154  ALA   A HB1  1 
ATOM   3252 H  HB2  A ALA   A 1 154 ? 15.135 -3.435  9.622   0.50 17.74 ?  154  ALA   A HB2  1 
ATOM   3253 H  HB2  B ALA   A 1 154 ? 15.159 -3.661  9.890   0.50 17.63 ?  154  ALA   A HB2  1 
ATOM   3254 H  HB3  A ALA   A 1 154 ? 15.568 -2.867  8.203   0.50 17.74 ?  154  ALA   A HB3  1 
ATOM   3255 H  HB3  B ALA   A 1 154 ? 15.644 -2.939  8.561   0.50 17.63 ?  154  ALA   A HB3  1 
ATOM   3256 N  N    A VAL   A 1 155 ? 12.255 -3.811  6.550   0.50 15.02 ?  155  VAL   A N    1 
ATOM   3257 N  N    B VAL   A 1 155 ? 12.349 -3.605  6.689   0.50 15.36 ?  155  VAL   A N    1 
ATOM   3258 C  CA   A VAL   A 1 155 ? 11.591 -3.310  5.351   0.50 15.37 ?  155  VAL   A CA   1 
ATOM   3259 C  CA   B VAL   A 1 155 ? 11.760 -3.143  5.432   0.50 16.66 ?  155  VAL   A CA   1 
ATOM   3260 C  C    A VAL   A 1 155 ? 10.880 -2.017  5.728   0.50 15.96 ?  155  VAL   A C    1 
ATOM   3261 C  C    B VAL   A 1 155 ? 10.890 -1.929  5.731   0.50 18.28 ?  155  VAL   A C    1 
ATOM   3262 O  O    A VAL   A 1 155 ? 10.003 -2.014  6.600   0.50 16.05 ?  155  VAL   A O    1 
ATOM   3263 O  O    B VAL   A 1 155 ? 9.783  -2.066  6.265   0.50 18.39 ?  155  VAL   A O    1 
ATOM   3264 C  CB   A VAL   A 1 155 ? 10.604 -4.343  4.781   0.50 15.39 ?  155  VAL   A CB   1 
ATOM   3265 C  CB   B VAL   A 1 155 ? 10.953 -4.248  4.734   0.50 16.73 ?  155  VAL   A CB   1 
ATOM   3266 C  CG1  A VAL   A 1 155 ? 9.900  -3.793  3.552   0.50 16.32 ?  155  VAL   A CG1  1 
ATOM   3267 C  CG1  B VAL   A 1 155 ? 10.257 -3.706  3.490   0.50 17.11 ?  155  VAL   A CG1  1 
ATOM   3268 C  CG2  A VAL   A 1 155 ? 11.329 -5.644  4.443   0.50 15.24 ?  155  VAL   A CG2  1 
ATOM   3269 C  CG2  B VAL   A 1 155 ? 11.863 -5.407  4.366   0.50 16.60 ?  155  VAL   A CG2  1 
ATOM   3270 H  H    A VAL   A 1 155 ? 11.708 -4.106  7.147   0.50 18.02 ?  155  VAL   A H    1 
ATOM   3271 H  H    B VAL   A 1 155 ? 11.761 -3.834  7.279   0.50 18.43 ?  155  VAL   A H    1 
ATOM   3272 H  HA   A VAL   A 1 155 ? 12.252 -3.116  4.674   0.50 18.44 ?  155  VAL   A HA   1 
ATOM   3273 H  HA   B VAL   A 1 155 ? 12.470 -2.865  4.834   0.50 19.98 ?  155  VAL   A HA   1 
ATOM   3274 H  HB   A VAL   A 1 155 ? 9.928  -4.543  5.452   0.50 18.46 ?  155  VAL   A HB   1 
ATOM   3275 H  HB   B VAL   A 1 155 ? 10.275 -4.580  5.345   0.50 20.07 ?  155  VAL   A HB   1 
ATOM   3276 H  HG11 A VAL   A 1 155 ? 9.404  -4.508  3.126   0.50 19.58 ?  155  VAL   A HG11 1 
ATOM   3277 H  HG11 B VAL   A 1 155 ? 9.944  -4.454  2.956   0.50 20.52 ?  155  VAL   A HG11 1 
ATOM   3278 H  HG12 A VAL   A 1 155 ? 9.294  -3.085  3.822   0.50 19.58 ?  155  VAL   A HG12 1 
ATOM   3279 H  HG12 B VAL   A 1 155 ? 9.503  -3.158  3.761   0.50 20.52 ?  155  VAL   A HG12 1 
ATOM   3280 H  HG13 A VAL   A 1 155 ? 10.567 -3.443  2.940   0.50 19.58 ?  155  VAL   A HG13 1 
ATOM   3281 H  HG13 B VAL   A 1 155 ? 10.888 -3.177  2.981   0.50 20.52 ?  155  VAL   A HG13 1 
ATOM   3282 H  HG21 A VAL   A 1 155 ? 10.707 -6.248  4.007   0.50 18.29 ?  155  VAL   A HG21 1 
ATOM   3283 H  HG21 B VAL   A 1 155 ? 11.339 -6.087  3.915   0.50 19.91 ?  155  VAL   A HG21 1 
ATOM   3284 H  HG22 A VAL   A 1 155 ? 12.069 -5.446  3.848   0.50 18.29 ?  155  VAL   A HG22 1 
ATOM   3285 H  HG22 B VAL   A 1 155 ? 12.562 -5.083  3.777   0.50 19.91 ?  155  VAL   A HG22 1 
ATOM   3286 H  HG23 A VAL   A 1 155 ? 11.661 -6.046  5.261   0.50 18.29 ?  155  VAL   A HG23 1 
ATOM   3287 H  HG23 B VAL   A 1 155 ? 12.254 -5.773  5.175   0.50 19.91 ?  155  VAL   A HG23 1 
ATOM   3288 N  N    A PHE   A 1 156 ? 11.251 -0.918  5.067   0.50 16.79 ?  156  PHE   A N    1 
ATOM   3289 N  N    B PHE   A 1 156 ? 11.380 -0.744  5.365   0.50 19.82 ?  156  PHE   A N    1 
ATOM   3290 C  CA   A PHE   A 1 156 ? 10.748 0.394   5.472   0.50 18.32 ?  156  PHE   A CA   1 
ATOM   3291 C  CA   B PHE   A 1 156 ? 10.714 0.524   5.673   0.50 22.06 ?  156  PHE   A CA   1 
ATOM   3292 C  C    A PHE   A 1 156 ? 9.287  0.580   5.088   0.50 18.71 ?  156  PHE   A C    1 
ATOM   3293 C  C    B PHE   A 1 156 ? 9.667  0.872   4.608   0.50 23.37 ?  156  PHE   A C    1 
ATOM   3294 O  O    A PHE   A 1 156 ? 8.495  1.115   5.874   0.50 19.83 ?  156  PHE   A O    1 
ATOM   3295 O  O    B PHE   A 1 156 ? 9.692  1.934   3.984   0.50 23.70 ?  156  PHE   A O    1 
ATOM   3296 C  CB   A PHE   A 1 156 ? 11.610 1.492   4.845   0.50 19.33 ?  156  PHE   A CB   1 
ATOM   3297 C  CB   B PHE   A 1 156 ? 11.761 1.626   5.806   0.50 22.95 ?  156  PHE   A CB   1 
ATOM   3298 C  CG   A PHE   A 1 156 ? 11.143 2.888   5.160   0.50 20.93 ?  156  PHE   A CG   1 
ATOM   3299 C  CG   B PHE   A 1 156 ? 11.259 2.888   6.456   0.50 24.06 ?  156  PHE   A CG   1 
ATOM   3300 C  CD1  A PHE   A 1 156 ? 11.108 3.338   6.470   0.50 21.74 ?  156  PHE   A CD1  1 
ATOM   3301 C  CD1  B PHE   A 1 156 ? 10.161 2.874   7.303   0.50 24.48 ?  156  PHE   A CD1  1 
ATOM   3302 C  CD2  A PHE   A 1 156 ? 10.753 3.752   4.148   0.50 21.74 ?  156  PHE   A CD2  1 
ATOM   3303 C  CD2  B PHE   A 1 156 ? 11.899 4.093   6.217   0.50 24.38 ?  156  PHE   A CD2  1 
ATOM   3304 C  CE1  A PHE   A 1 156 ? 10.682 4.617   6.766   0.50 22.50 ?  156  PHE   A CE1  1 
ATOM   3305 C  CE1  B PHE   A 1 156 ? 9.713  4.038   7.897   0.50 24.65 ?  156  PHE   A CE1  1 
ATOM   3306 C  CE2  A PHE   A 1 156 ? 10.329 5.035   4.437   0.50 22.56 ?  156  PHE   A CE2  1 
ATOM   3307 C  CE2  B PHE   A 1 156 ? 11.455 5.260   6.806   0.50 24.81 ?  156  PHE   A CE2  1 
ATOM   3308 C  CZ   A PHE   A 1 156 ? 10.297 5.469   5.749   0.50 22.79 ?  156  PHE   A CZ   1 
ATOM   3309 C  CZ   B PHE   A 1 156 ? 10.360 5.232   7.648   0.50 24.78 ?  156  PHE   A CZ   1 
ATOM   3310 H  H    A PHE   A 1 156 ? 11.773 -0.916  4.386   0.50 20.14 ?  156  PHE   A H    1 
ATOM   3311 H  H    B PHE   A 1 156 ? 12.118 -0.646  4.942   0.50 23.78 ?  156  PHE   A H    1 
ATOM   3312 H  HA   A PHE   A 1 156 ? 10.816 0.469   6.433   0.50 21.98 ?  156  PHE   A HA   1 
ATOM   3313 H  HA   B PHE   A 1 156 ? 10.253 0.420   6.516   0.50 26.47 ?  156  PHE   A HA   1 
ATOM   3314 H  HB2  A PHE   A 1 156 ? 12.519 1.398   5.175   0.50 23.19 ?  156  PHE   A HB2  1 
ATOM   3315 H  HB2  B PHE   A 1 156 ? 12.497 1.294   6.344   0.50 27.53 ?  156  PHE   A HB2  1 
ATOM   3316 H  HB3  A PHE   A 1 156 ? 11.600 1.384   3.881   0.50 23.19 ?  156  PHE   A HB3  1 
ATOM   3317 H  HB3  B PHE   A 1 156 ? 12.085 1.862   4.921   0.50 27.53 ?  156  PHE   A HB3  1 
ATOM   3318 H  HD1  A PHE   A 1 156 ? 11.370 2.767   7.160   0.50 26.08 ?  156  PHE   A HD1  1 
ATOM   3319 H  HD1  B PHE   A 1 156 ? 9.723  2.071   7.476   0.50 29.37 ?  156  PHE   A HD1  1 
ATOM   3320 H  HD2  A PHE   A 1 156 ? 10.775 3.458   3.265   0.50 26.08 ?  156  PHE   A HD2  1 
ATOM   3321 H  HD2  B PHE   A 1 156 ? 12.637 4.117   5.651   0.50 29.25 ?  156  PHE   A HD2  1 
ATOM   3322 H  HE1  A PHE   A 1 156 ? 10.663 4.908   7.650   0.50 27.00 ?  156  PHE   A HE1  1 
ATOM   3323 H  HE1  B PHE   A 1 156 ? 8.976  4.015   8.463   0.50 29.58 ?  156  PHE   A HE1  1 
ATOM   3324 H  HE2  A PHE   A 1 156 ? 10.068 5.602   3.751   0.50 27.07 ?  156  PHE   A HE2  1 
ATOM   3325 H  HE2  B PHE   A 1 156 ? 11.892 6.063   6.637   0.50 29.77 ?  156  PHE   A HE2  1 
ATOM   3326 H  HZ   A PHE   A 1 156 ? 10.011 6.330   5.948   0.50 27.35 ?  156  PHE   A HZ   1 
ATOM   3327 H  HZ   B PHE   A 1 156 ? 10.058 6.015   8.046   0.50 29.73 ?  156  PHE   A HZ   1 
ATOM   3328 N  N    A ASP   A 1 157 ? 8.921  0.164   3.883   0.50 19.04 ?  157  ASP   A N    1 
ATOM   3329 N  N    B ASP   A 1 157 ? 8.724  -0.048  4.423   0.50 24.26 ?  157  ASP   A N    1 
ATOM   3330 C  CA   A ASP   A 1 157 ? 7.591  0.410   3.347   0.50 20.24 ?  157  ASP   A CA   1 
ATOM   3331 C  CA   B ASP   A 1 157 ? 7.650  0.120   3.445   0.50 25.50 ?  157  ASP   A CA   1 
ATOM   3332 C  C    A ASP   A 1 157 ? 6.631  -0.654  3.872   0.50 20.21 ?  157  ASP   A C    1 
ATOM   3333 C  C    B ASP   A 1 157 ? 6.514  -0.801  3.856   0.50 25.29 ?  157  ASP   A C    1 
ATOM   3334 O  O    A ASP   A 1 157 ? 6.791  -1.844  3.571   0.50 19.58 ?  157  ASP   A O    1 
ATOM   3335 O  O    B ASP   A 1 157 ? 6.717  -2.014  3.979   0.50 25.14 ?  157  ASP   A O    1 
ATOM   3336 C  CB   A ASP   A 1 157 ? 7.673  0.362   1.824   0.50 21.72 ?  157  ASP   A CB   1 
ATOM   3337 C  CB   B ASP   A 1 157 ? 8.144  -0.241  2.046   0.50 26.66 ?  157  ASP   A CB   1 
ATOM   3338 C  CG   A ASP   A 1 157 ? 6.410  0.852   1.156   0.50 23.15 ?  157  ASP   A CG   1 
ATOM   3339 C  CG   B ASP   A 1 157 ? 7.132  0.080   0.963   0.50 27.76 ?  157  ASP   A CG   1 
ATOM   3340 O  OD1  A ASP   A 1 157 ? 6.135  2.069   1.198   0.50 24.58 ?  157  ASP   A OD1  1 
ATOM   3341 O  OD1  B ASP   A 1 157 ? 5.927  0.195   1.278   0.50 27.73 ?  157  ASP   A OD1  1 
ATOM   3342 O  OD2  A ASP   A 1 157 ? 5.686  0.011   0.583   0.50 23.55 -1 157  ASP   A OD2  1 
ATOM   3343 O  OD2  B ASP   A 1 157 ? 7.542  0.198   -0.210  0.50 28.56 -1 157  ASP   A OD2  1 
ATOM   3344 H  H    A ASP   A 1 157 ? 9.440  -0.262  3.341   0.50 22.84 ?  157  ASP   A H    1 
ATOM   3345 H  H    B ASP   A 1 157 ? 8.680  -0.785  4.857   0.50 29.11 ?  157  ASP   A H    1 
ATOM   3346 H  HA   A ASP   A 1 157 ? 7.277  1.286   3.617   0.50 24.28 ?  157  ASP   A HA   1 
ATOM   3347 H  HA   B ASP   A 1 157 ? 7.334  1.041   3.443   0.50 30.59 ?  157  ASP   A HA   1 
ATOM   3348 H  HB2  A ASP   A 1 157 ? 8.427  0.901   1.530   0.50 26.06 ?  157  ASP   A HB2  1 
ATOM   3349 H  HB2  B ASP   A 1 157 ? 8.958  0.250   1.869   0.50 31.98 ?  157  ASP   A HB2  1 
ATOM   3350 H  HB3  A ASP   A 1 157 ? 7.799  -0.552  1.540   0.50 26.06 ?  157  ASP   A HB3  1 
ATOM   3351 H  HB3  B ASP   A 1 157 ? 8.316  -1.192  2.003   0.50 31.98 ?  157  ASP   A HB3  1 
ATOM   3352 N  N    A LYS   A 1 158 ? 5.646  -0.227  4.675   0.50 21.15 ?  158  LYS   A N    1 
ATOM   3353 N  N    B LYS   A 1 158 ? 5.323  -0.235  4.053   0.50 25.16 ?  158  LYS   A N    1 
ATOM   3354 C  CA   A LYS   A 1 158 ? 4.674  -1.172  5.220   0.50 21.58 ?  158  LYS   A CA   1 
ATOM   3355 C  CA   B LYS   A 1 158 ? 4.212  -1.001  4.613   0.50 25.65 ?  158  LYS   A CA   1 
ATOM   3356 C  C    A LYS   A 1 158 ? 3.939  -1.896  4.103   0.50 21.57 ?  158  LYS   A C    1 
ATOM   3357 C  C    B LYS   A 1 158 ? 3.683  -2.028  3.615   0.50 24.83 ?  158  LYS   A C    1 
ATOM   3358 O  O    A LYS   A 1 158 ? 3.724  -3.112  4.174   0.50 21.96 ?  158  LYS   A O    1 
ATOM   3359 O  O    B LYS   A 1 158 ? 3.670  -3.234  3.891   0.50 24.78 ?  158  LYS   A O    1 
ATOM   3360 C  CB   A LYS   A 1 158 ? 3.688  -0.444  6.141   0.50 22.13 ?  158  LYS   A CB   1 
ATOM   3361 C  CB   B LYS   A 1 158 ? 3.105  -0.040  5.059   0.50 27.10 ?  158  LYS   A CB   1 
ATOM   3362 C  CG   A LYS   A 1 158 ? 2.445  -1.253  6.524   0.50 23.08 ?  158  LYS   A CG   1 
ATOM   3363 C  CG   B LYS   A 1 158 ? 1.891  -0.721  5.666   0.50 28.79 ?  158  LYS   A CG   1 
ATOM   3364 C  CD   A LYS   A 1 158 ? 2.788  -2.505  7.328   0.50 23.72 ?  158  LYS   A CD   1 
ATOM   3365 C  CD   B LYS   A 1 158 ? 0.879  0.292   6.178   0.50 30.28 ?  158  LYS   A CD   1 
ATOM   3366 C  CE   A LYS   A 1 158 ? 1.524  -3.238  7.770   0.50 24.31 ?  158  LYS   A CE   1 
ATOM   3367 C  CE   B LYS   A 1 158 ? -0.323 -0.398  6.801   0.50 31.46 ?  158  LYS   A CE   1 
ATOM   3368 N  NZ   A LYS   A 1 158 ? 1.828  -4.522  8.464   0.50 24.63 ?  158  LYS   A NZ   1 
ATOM   3369 N  NZ   B LYS   A 1 158 ? -1.303 0.572   7.365   0.50 32.18 ?  158  LYS   A NZ   1 
ATOM   3370 H  H    A LYS   A 1 158 ? 5.538  0.587   4.921   0.50 25.38 ?  158  LYS   A H    1 
ATOM   3371 H  H    B LYS   A 1 158 ? 5.135  0.585   3.872   0.50 30.18 ?  158  LYS   A H    1 
ATOM   3372 H  HA   A LYS   A 1 158 ? 5.141  -1.836  5.753   0.50 25.89 ?  158  LYS   A HA   1 
ATOM   3373 H  HA   B LYS   A 1 158 ? 4.524  -1.475  5.399   0.50 30.77 ?  158  LYS   A HA   1 
ATOM   3374 H  HB2  A LYS   A 1 158 ? 4.150  -0.210  6.966   0.50 26.55 ?  158  LYS   A HB2  1 
ATOM   3375 H  HB2  B LYS   A 1 158 ? 3.467  0.567   5.727   0.50 32.52 ?  158  LYS   A HB2  1 
ATOM   3376 H  HB3  A LYS   A 1 158 ? 3.390  0.366   5.699   0.50 26.55 ?  158  LYS   A HB3  1 
ATOM   3377 H  HB3  B LYS   A 1 158 ? 2.805  0.469   4.289   0.50 32.52 ?  158  LYS   A HB3  1 
ATOM   3378 H  HG2  A LYS   A 1 158 ? 1.872  -0.699  7.071   0.50 27.68 ?  158  LYS   A HG2  1 
ATOM   3379 H  HG2  B LYS   A 1 158 ? 1.456  -1.264  4.991   0.50 34.55 ?  158  LYS   A HG2  1 
ATOM   3380 H  HG3  A LYS   A 1 158 ? 1.969  -1.525  5.722   0.50 27.68 ?  158  LYS   A HG3  1 
ATOM   3381 H  HG3  B LYS   A 1 158 ? 2.172  -1.272  6.412   0.50 34.55 ?  158  LYS   A HG3  1 
ATOM   3382 H  HD2  A LYS   A 1 158 ? 3.315  -3.106  6.780   0.50 28.46 ?  158  LYS   A HD2  1 
ATOM   3383 H  HD2  B LYS   A 1 158 ? 1.294  0.850   6.855   0.50 36.33 ?  158  LYS   A HD2  1 
ATOM   3384 H  HD3  A LYS   A 1 158 ? 3.286  -2.248  8.121   0.50 28.46 ?  158  LYS   A HD3  1 
ATOM   3385 H  HD3  B LYS   A 1 158 ? 0.567  0.839   5.438   0.50 36.33 ?  158  LYS   A HD3  1 
ATOM   3386 H  HE2  A LYS   A 1 158 ? 1.031  -2.674  8.385   0.50 29.17 ?  158  LYS   A HE2  1 
ATOM   3387 H  HE2  B LYS   A 1 158 ? -0.776 -0.923  6.122   0.50 37.75 ?  158  LYS   A HE2  1 
ATOM   3388 H  HE3  A LYS   A 1 158 ? 0.984  -3.436  6.990   0.50 29.17 ?  158  LYS   A HE3  1 
ATOM   3389 H  HE3  B LYS   A 1 158 ? -0.021 -0.975  7.520   0.50 37.75 ?  158  LYS   A HE3  1 
ATOM   3390 H  HZ1  A LYS   A 1 158 ? 1.072  -4.922  8.706   0.50 29.54 ?  158  LYS   A HZ1  1 
ATOM   3391 H  HZ1  B LYS   A 1 158 ? -1.992 0.135   7.721   0.50 38.61 ?  158  LYS   A HZ1  1 
ATOM   3392 H  HZ2  A LYS   A 1 158 ? 2.280  -5.062  7.918   0.50 29.54 ?  158  LYS   A HZ2  1 
ATOM   3393 H  HZ2  B LYS   A 1 158 ? -0.914 1.063   7.997   0.50 38.61 ?  158  LYS   A HZ2  1 
ATOM   3394 H  HZ3  A LYS   A 1 158 ? 2.320  -4.367  9.189   0.50 29.54 ?  158  LYS   A HZ3  1 
ATOM   3395 H  HZ3  B LYS   A 1 158 ? -1.602 1.110   6.723   0.50 38.61 ?  158  LYS   A HZ3  1 
ATOM   3396 N  N    A ASN   A 1 159 ? 3.544  -1.164  3.060   0.50 21.65 ?  159  ASN   A N    1 
ATOM   3397 N  N    B ASN   A 1 159 ? 3.229  -1.565  2.448   0.50 24.58 ?  159  ASN   A N    1 
ATOM   3398 C  CA   A ASN   A 1 159 ? 2.881  -1.809  1.934   0.50 21.87 ?  159  ASN   A CA   1 
ATOM   3399 C  CA   B ASN   A 1 159 ? 2.638  -2.476  1.470   0.50 24.06 ?  159  ASN   A CA   1 
ATOM   3400 C  C    A ASN   A 1 159 ? 3.785  -2.851  1.287   0.50 21.40 ?  159  ASN   A C    1 
ATOM   3401 C  C    B ASN   A 1 159 ? 3.652  -3.518  1.009   0.50 21.78 ?  159  ASN   A C    1 
ATOM   3402 O  O    A ASN   A 1 159 ? 3.330  -3.946  0.942   0.50 20.99 ?  159  ASN   A O    1 
ATOM   3403 O  O    B ASN   A 1 159 ? 3.301  -4.679  0.771   0.50 21.06 ?  159  ASN   A O    1 
ATOM   3404 C  CB   A ASN   A 1 159 ? 2.416  -0.761  0.923   0.50 22.51 ?  159  ASN   A CB   1 
ATOM   3405 C  CB   B ASN   A 1 159 ? 2.102  -1.678  0.279   0.50 25.99 ?  159  ASN   A CB   1 
ATOM   3406 C  CG   A ASN   A 1 159 ? 1.181  -0.014  1.390   0.50 23.94 ?  159  ASN   A CG   1 
ATOM   3407 C  CG   B ASN   A 1 159 ? 1.284  -0.475  0.702   0.50 27.98 ?  159  ASN   A CG   1 
ATOM   3408 O  OD1  A ASN   A 1 159 ? 0.361  -0.564  2.120   0.50 24.75 ?  159  ASN   A OD1  1 
ATOM   3409 O  OD1  B ASN   A 1 159 ? 0.167  -0.615  1.196   0.50 28.78 ?  159  ASN   A OD1  1 
ATOM   3410 N  ND2  A ASN   A 1 159 ? 1.044  1.239   0.973   0.50 24.42 ?  159  ASN   A ND2  1 
ATOM   3411 N  ND2  B ASN   A 1 159 ? 1.838  0.718   0.509   0.50 28.63 ?  159  ASN   A ND2  1 
ATOM   3412 H  H    A ASN   A 1 159 ? 3.645  -0.312  2.985   0.50 25.97 ?  159  ASN   A H    1 
ATOM   3413 H  H    B ASN   A 1 159 ? 3.252  -0.741  2.208   0.50 29.49 ?  159  ASN   A H    1 
ATOM   3414 H  HA   A ASN   A 1 159 ? 2.091  -2.268  2.265   0.50 26.23 ?  159  ASN   A HA   1 
ATOM   3415 H  HA   B ASN   A 1 159 ? 1.888  -2.937  1.880   0.50 28.86 ?  159  ASN   A HA   1 
ATOM   3416 H  HB2  A ASN   A 1 159 ? 3.120  -0.113  0.788   0.50 27.01 ?  159  ASN   A HB2  1 
ATOM   3417 H  HB2  B ASN   A 1 159 ? 2.848  -1.358  -0.251  0.50 31.18 ?  159  ASN   A HB2  1 
ATOM   3418 H  HB3  A ASN   A 1 159 ? 2.202  -1.205  0.086   0.50 27.01 ?  159  ASN   A HB3  1 
ATOM   3419 H  HB3  B ASN   A 1 159 ? 1.531  -2.248  -0.256  0.50 31.18 ?  159  ASN   A HB3  1 
ATOM   3420 H  HD21 A ASN   A 1 159 ? 0.357  1.700   1.210   0.50 29.30 ?  159  ASN   A HD21 1 
ATOM   3421 H  HD21 B ASN   A 1 159 ? 1.415  1.433   0.734   0.50 34.35 ?  159  ASN   A HD21 1 
ATOM   3422 H  HD22 A ASN   A 1 159 ? 1.645  1.589   0.469   0.50 29.30 ?  159  ASN   A HD22 1 
ATOM   3423 H  HD22 B ASN   A 1 159 ? 2.621  0.777   0.157   0.50 34.35 ?  159  ASN   A HD22 1 
ATOM   3424 N  N    A LEU   A 1 160 ? 5.072  -2.539  1.121   0.50 20.93 ?  160  LEU   A N    1 
ATOM   3425 N  N    B LEU   A 1 160 ? 4.917  -3.117  0.885   0.50 21.00 ?  160  LEU   A N    1 
ATOM   3426 C  CA   A LEU   A 1 160 ? 5.977  -3.541  0.570   0.50 20.45 ?  160  LEU   A CA   1 
ATOM   3427 C  CA   B LEU   A 1 160 ? 5.964  -4.037  0.455   0.50 20.09 ?  160  LEU   A CA   1 
ATOM   3428 C  C    A LEU   A 1 160 ? 6.160  -4.705  1.535   0.50 19.46 ?  160  LEU   A C    1 
ATOM   3429 C  C    B LEU   A 1 160 ? 6.160  -5.160  1.466   0.50 19.36 ?  160  LEU   A C    1 
ATOM   3430 O  O    A LEU   A 1 160 ? 6.249  -5.862  1.109   0.50 20.01 ?  160  LEU   A O    1 
ATOM   3431 O  O    B LEU   A 1 160 ? 6.154  -6.343  1.106   0.50 19.49 ?  160  LEU   A O    1 
ATOM   3432 C  CB   A LEU   A 1 160 ? 7.325  -2.923  0.207   0.50 20.78 ?  160  LEU   A CB   1 
ATOM   3433 C  CB   B LEU   A 1 160 ? 7.264  -3.263  0.264   0.50 20.11 ?  160  LEU   A CB   1 
ATOM   3434 C  CG   A LEU   A 1 160 ? 8.344  -3.957  -0.279  0.50 21.26 ?  160  LEU   A CG   1 
ATOM   3435 C  CG   B LEU   A 1 160 ? 8.472  -4.125  -0.084  0.50 20.16 ?  160  LEU   A CG   1 
ATOM   3436 C  CD1  A LEU   A 1 160 ? 7.809  -4.729  -1.475  0.50 21.78 ?  160  LEU   A CD1  1 
ATOM   3437 C  CD1  B LEU   A 1 160 ? 8.178  -4.869  -1.361  0.50 20.28 ?  160  LEU   A CD1  1 
ATOM   3438 C  CD2  A LEU   A 1 160 ? 9.669  -3.302  -0.612  0.50 21.33 ?  160  LEU   A CD2  1 
ATOM   3439 C  CD2  B LEU   A 1 160 ? 9.735  -3.287  -0.215  0.50 20.22 ?  160  LEU   A CD2  1 
ATOM   3440 H  H    A LEU   A 1 160 ? 5.428  -1.779  1.313   0.50 25.11 ?  160  LEU   A H    1 
ATOM   3441 H  H    B LEU   A 1 160 ? 5.190  -2.328  1.046   0.50 25.19 ?  160  LEU   A H    1 
ATOM   3442 H  HA   A LEU   A 1 160 ? 5.580  -3.888  -0.240  0.50 24.54 ?  160  LEU   A HA   1 
ATOM   3443 H  HA   B LEU   A 1 160 ? 5.713  -4.435  -0.393  0.50 24.11 ?  160  LEU   A HA   1 
ATOM   3444 H  HB2  A LEU   A 1 160 ? 7.199  -2.258  -0.495  0.50 24.93 ?  160  LEU   A HB2  1 
ATOM   3445 H  HB2  B LEU   A 1 160 ? 7.143  -2.614  -0.449  0.50 24.12 ?  160  LEU   A HB2  1 
ATOM   3446 H  HB3  A LEU   A 1 160 ? 7.696  -2.508  0.997   0.50 24.93 ?  160  LEU   A HB3  1 
ATOM   3447 H  HB3  B LEU   A 1 160 ? 7.461  -2.807  1.093   0.50 24.12 ?  160  LEU   A HB3  1 
ATOM   3448 H  HG   A LEU   A 1 160 ? 8.510  -4.594  0.433   0.50 25.51 ?  160  LEU   A HG   1 
ATOM   3449 H  HG   B LEU   A 1 160 ? 8.620  -4.775  0.622   0.50 24.19 ?  160  LEU   A HG   1 
ATOM   3450 H  HD11 A LEU   A 1 160 ? 8.515  -5.296  -1.820  0.50 26.13 ?  160  LEU   A HD11 1 
ATOM   3451 H  HD11 B LEU   A 1 160 ? 8.994  -5.270  -1.681  0.50 24.33 ?  160  LEU   A HD11 1 
ATOM   3452 H  HD12 A LEU   A 1 160 ? 7.059  -5.276  -1.193  0.50 26.13 ?  160  LEU   A HD12 1 
ATOM   3453 H  HD12 B LEU   A 1 160 ? 7.516  -5.554  -1.181  0.50 24.33 ?  160  LEU   A HD12 1 
ATOM   3454 H  HD13 A LEU   A 1 160 ? 7.525  -4.100  -2.156  0.50 26.13 ?  160  LEU   A HD13 1 
ATOM   3455 H  HD13 B LEU   A 1 160 ? 7.835  -4.238  -2.016  0.50 24.33 ?  160  LEU   A HD13 1 
ATOM   3456 H  HD21 A LEU   A 1 160 ? 10.292 -3.985  -0.909  0.50 25.59 ?  160  LEU   A HD21 1 
ATOM   3457 H  HD21 B LEU   A 1 160 ? 10.481 -3.870  -0.432  0.50 24.26 ?  160  LEU   A HD21 1 
ATOM   3458 H  HD22 A LEU   A 1 160 ? 9.532  -2.650  -1.315  0.50 25.59 ?  160  LEU   A HD22 1 
ATOM   3459 H  HD22 B LEU   A 1 160 ? 9.611  -2.634  -0.922  0.50 24.26 ?  160  LEU   A HD22 1 
ATOM   3460 H  HD23 A LEU   A 1 160 ? 10.014 -2.866  0.184   0.50 25.59 ?  160  LEU   A HD23 1 
ATOM   3461 H  HD23 B LEU   A 1 160 ? 9.907  -2.834  0.626   0.50 24.26 ?  160  LEU   A HD23 1 
ATOM   3462 N  N    A TYR   A 1 161 ? 6.218  -4.419  2.836   0.50 18.59 ?  161  TYR   A N    1 
ATOM   3463 N  N    B TYR   A 1 161 ? 6.374  -4.807  2.735   0.50 19.43 ?  161  TYR   A N    1 
ATOM   3464 C  CA   A TYR   A 1 161 ? 6.402  -5.486  3.814   0.50 18.60 ?  161  TYR   A CA   1 
ATOM   3465 C  CA   B TYR   A 1 161 ? 6.440  -5.821  3.782   0.50 19.83 ?  161  TYR   A CA   1 
ATOM   3466 C  C    A TYR   A 1 161 ? 5.302  -6.544  3.718   0.50 19.08 ?  161  TYR   A C    1 
ATOM   3467 C  C    B TYR   A 1 161 ? 5.222  -6.731  3.708   0.50 20.63 ?  161  TYR   A C    1 
ATOM   3468 O  O    A TYR   A 1 161 ? 5.584  -7.746  3.770   0.50 18.77 ?  161  TYR   A O    1 
ATOM   3469 O  O    B TYR   A 1 161 ? 5.348  -7.957  3.625   0.50 20.25 ?  161  TYR   A O    1 
ATOM   3470 C  CB   A TYR   A 1 161 ? 6.483  -4.908  5.227   0.50 19.12 ?  161  TYR   A CB   1 
ATOM   3471 C  CB   B TYR   A 1 161 ? 6.528  -5.143  5.153   0.50 20.00 ?  161  TYR   A CB   1 
ATOM   3472 C  CG   A TYR   A 1 161 ? 6.403  -5.983  6.275   0.50 18.99 ?  161  TYR   A CG   1 
ATOM   3473 C  CG   B TYR   A 1 161 ? 6.407  -6.086  6.336   0.50 19.77 ?  161  TYR   A CG   1 
ATOM   3474 C  CD1  A TYR   A 1 161 ? 7.493  -6.800  6.534   0.50 18.76 ?  161  TYR   A CD1  1 
ATOM   3475 C  CD1  B TYR   A 1 161 ? 5.161  -6.425  6.858   0.50 20.14 ?  161  TYR   A CD1  1 
ATOM   3476 C  CD2  A TYR   A 1 161 ? 5.229  -6.203  6.982   0.50 18.98 ?  161  TYR   A CD2  1 
ATOM   3477 C  CD2  B TYR   A 1 161 ? 7.537  -6.611  6.951   0.50 19.28 ?  161  TYR   A CD2  1 
ATOM   3478 C  CE1  A TYR   A 1 161 ? 7.425  -7.794  7.477   0.50 18.08 ?  161  TYR   A CE1  1 
ATOM   3479 C  CE1  B TYR   A 1 161 ? 5.046  -7.273  7.939   0.50 20.33 ?  161  TYR   A CE1  1 
ATOM   3480 C  CE2  A TYR   A 1 161 ? 5.149  -7.197  7.929   0.50 18.60 ?  161  TYR   A CE2  1 
ATOM   3481 C  CE2  B TYR   A 1 161 ? 7.428  -7.464  8.033   0.50 19.53 ?  161  TYR   A CE2  1 
ATOM   3482 C  CZ   A TYR   A 1 161 ? 6.251  -7.992  8.170   0.50 18.30 ?  161  TYR   A CZ   1 
ATOM   3483 C  CZ   B TYR   A 1 161 ? 6.180  -7.789  8.525   0.50 20.45 ?  161  TYR   A CZ   1 
ATOM   3484 O  OH   A TYR   A 1 161 ? 6.189  -8.986  9.114   0.50 18.53 ?  161  TYR   A OH   1 
ATOM   3485 O  OH   B TYR   A 1 161 ? 6.064  -8.636  9.605   0.50 21.58 ?  161  TYR   A OH   1 
ATOM   3486 H  H    A TYR   A 1 161 ? 6.154  -3.630  3.172   0.50 22.31 ?  161  TYR   A H    1 
ATOM   3487 H  H    B TYR   A 1 161 ? 6.472  -4.005  3.012   0.50 23.31 ?  161  TYR   A H    1 
ATOM   3488 H  HA   A TYR   A 1 161 ? 7.238  -5.929  3.635   0.50 22.31 ?  161  TYR   A HA   1 
ATOM   3489 H  HA   B TYR   A 1 161 ? 7.235  -6.364  3.661   0.50 23.79 ?  161  TYR   A HA   1 
ATOM   3490 H  HB2  A TYR   A 1 161 ? 7.331  -4.444  5.333   0.50 22.94 ?  161  TYR   A HB2  1 
ATOM   3491 H  HB2  B TYR   A 1 161 ? 7.384  -4.694  5.222   0.50 23.99 ?  161  TYR   A HB2  1 
ATOM   3492 H  HB3  A TYR   A 1 161 ? 5.747  -4.291  5.370   0.50 22.94 ?  161  TYR   A HB3  1 
ATOM   3493 H  HB3  B TYR   A 1 161 ? 5.811  -4.493  5.223   0.50 23.99 ?  161  TYR   A HB3  1 
ATOM   3494 H  HD1  A TYR   A 1 161 ? 8.285  -6.672  6.065   0.50 22.50 ?  161  TYR   A HD1  1 
ATOM   3495 H  HD1  B TYR   A 1 161 ? 4.391  -6.080  6.469   0.50 24.16 ?  161  TYR   A HD1  1 
ATOM   3496 H  HD2  A TYR   A 1 161 ? 4.486  -5.665  6.818   0.50 22.77 ?  161  TYR   A HD2  1 
ATOM   3497 H  HD2  B TYR   A 1 161 ? 8.379  -6.392  6.625   0.50 23.13 ?  161  TYR   A HD2  1 
ATOM   3498 H  HE1  A TYR   A 1 161 ? 8.162  -8.336  7.639   0.50 21.69 ?  161  TYR   A HE1  1 
ATOM   3499 H  HE1  B TYR   A 1 161 ? 4.204  -7.495  8.274   0.50 24.39 ?  161  TYR   A HE1  1 
ATOM   3500 H  HE2  A TYR   A 1 161 ? 4.355  -7.334  8.400   0.50 22.32 ?  161  TYR   A HE2  1 
ATOM   3501 H  HE2  B TYR   A 1 161 ? 8.193  -7.809  8.432   0.50 23.42 ?  161  TYR   A HE2  1 
ATOM   3502 H  HH   A TYR   A 1 161 ? 6.914  -9.401  9.160   0.50 22.23 ?  161  TYR   A HH   1 
ATOM   3503 H  HH   B TYR   A 1 161 ? 5.250  -8.750  9.795   0.50 25.89 ?  161  TYR   A HH   1 
ATOM   3504 N  N    A ASP   A 1 162 ? 4.042  -6.125  3.577   0.50 19.78 ?  162  ASP   A N    1 
ATOM   3505 N  N    B ASP   A 1 162 ? 4.028  -6.134  3.730   0.50 21.90 ?  162  ASP   A N    1 
ATOM   3506 C  CA   A ASP   A 1 162 ? 2.946  -7.097  3.595   0.50 19.88 ?  162  ASP   A CA   1 
ATOM   3507 C  CA   B ASP   A 1 162 ? 2.797  -6.876  3.468   0.50 22.72 ?  162  ASP   A CA   1 
ATOM   3508 C  C    A ASP   A 1 162 ? 2.957  -8.000  2.364   0.50 19.95 ?  162  ASP   A C    1 
ATOM   3509 C  C    B ASP   A 1 162 ? 2.928  -7.711  2.202   0.50 22.57 ?  162  ASP   A C    1 
ATOM   3510 O  O    A ASP   A 1 162 ? 2.571  -9.172  2.452   0.50 20.42 ?  162  ASP   A O    1 
ATOM   3511 O  O    B ASP   A 1 162 ? 2.612  -8.906  2.189   0.50 22.65 ?  162  ASP   A O    1 
ATOM   3512 C  CB   A ASP   A 1 162 ? 1.590  -6.390  3.725   0.50 20.15 ?  162  ASP   A CB   1 
ATOM   3513 C  CB   B ASP   A 1 162 ? 1.633  -5.894  3.303   0.50 23.64 ?  162  ASP   A CB   1 
ATOM   3514 C  CG   A ASP   A 1 162 ? 1.324  -5.863  5.128   0.50 20.97 ?  162  ASP   A CG   1 
ATOM   3515 C  CG   B ASP   A 1 162 ? 1.274  -5.180  4.598   0.50 24.45 ?  162  ASP   A CG   1 
ATOM   3516 O  OD1  A ASP   A 1 162 ? 1.985  -6.327  6.081   0.50 21.55 ?  162  ASP   A OD1  1 
ATOM   3517 O  OD1  B ASP   A 1 162 ? 1.799  -5.562  5.664   0.50 24.58 ?  162  ASP   A OD1  1 
ATOM   3518 O  OD2  A ASP   A 1 162 ? 0.430  -4.997  5.276   0.50 21.59 -1 162  ASP   A OD2  1 
ATOM   3519 O  OD2  B ASP   A 1 162 ? 0.450  -4.244  4.553   0.50 25.21 -1 162  ASP   A OD2  1 
ATOM   3520 H  H    A ASP   A 1 162 ? 3.791  -5.309  3.472   0.50 23.73 ?  162  ASP   A H    1 
ATOM   3521 H  H    B ASP   A 1 162 ? 3.910  -5.304  3.899   0.50 26.28 ?  162  ASP   A H    1 
ATOM   3522 H  HA   A ASP   A 1 162 ? 3.042  -7.671  4.367   0.50 23.85 ?  162  ASP   A HA   1 
ATOM   3523 H  HA   B ASP   A 1 162 ? 2.595  -7.462  4.218   0.50 27.26 ?  162  ASP   A HA   1 
ATOM   3524 H  HB2  A ASP   A 1 162 ? 1.556  -5.639  3.115   0.50 24.18 ?  162  ASP   A HB2  1 
ATOM   3525 H  HB2  B ASP   A 1 162 ? 1.873  -5.234  2.625   0.50 28.36 ?  162  ASP   A HB2  1 
ATOM   3526 H  HB3  A ASP   A 1 162 ? 0.874  -7.015  3.522   0.50 24.18 ?  162  ASP   A HB3  1 
ATOM   3527 H  HB3  B ASP   A 1 162 ? 0.845  -6.381  3.012   0.50 28.36 ?  162  ASP   A HB3  1 
ATOM   3528 N  N    A LYS   A 1 163 ? 3.405  -7.482  1.218   0.50 20.46 ?  163  LYS   A N    1 
ATOM   3529 N  N    B LYS   A 1 163 ? 3.376  -7.081  1.116   0.50 22.94 ?  163  LYS   A N    1 
ATOM   3530 C  CA   A LYS   A 1 163 ? 3.440  -8.279  -0.005  0.50 20.67 ?  163  LYS   A CA   1 
ATOM   3531 C  CA   B LYS   A 1 163 ? 3.579  -7.805  -0.133  0.50 22.99 ?  163  LYS   A CA   1 
ATOM   3532 C  C    A LYS   A 1 163 ? 4.540  -9.336  0.050   0.50 20.11 ?  163  LYS   A C    1 
ATOM   3533 C  C    B LYS   A 1 163 ? 4.621  -8.899  0.036   0.50 21.59 ?  163  LYS   A C    1 
ATOM   3534 O  O    A LYS   A 1 163 ? 4.367  -10.451 -0.455  0.50 21.01 ?  163  LYS   A O    1 
ATOM   3535 O  O    B LYS   A 1 163 ? 4.448  -10.014 -0.467  0.50 21.70 ?  163  LYS   A O    1 
ATOM   3536 C  CB   A LYS   A 1 163 ? 3.634  -7.346  -1.201  0.50 22.47 ?  163  LYS   A CB   1 
ATOM   3537 C  CB   B LYS   A 1 163 ? 4.029  -6.829  -1.218  0.50 25.12 ?  163  LYS   A CB   1 
ATOM   3538 C  CG   A LYS   A 1 163 ? 3.650  -8.023  -2.555  0.50 24.82 ?  163  LYS   A CG   1 
ATOM   3539 C  CG   B LYS   A 1 163 ? 3.965  -7.360  -2.635  0.50 27.45 ?  163  LYS   A CG   1 
ATOM   3540 C  CD   A LYS   A 1 163 ? 4.009  -7.028  -3.648  0.50 27.17 ?  163  LYS   A CD   1 
ATOM   3541 C  CD   B LYS   A 1 163 ? 4.595  -6.352  -3.585  0.50 29.69 ?  163  LYS   A CD   1 
ATOM   3542 C  CE   A LYS   A 1 163 ? 3.954  -7.672  -5.021  0.50 28.75 ?  163  LYS   A CE   1 
ATOM   3543 C  CE   B LYS   A 1 163 ? 4.283  -6.657  -5.038  0.50 31.48 ?  163  LYS   A CE   1 
ATOM   3544 N  NZ   A LYS   A 1 163 ? 4.613  -6.837  -6.060  0.50 29.56 ?  163  LYS   A NZ   1 
ATOM   3545 N  NZ   B LYS   A 1 163 ? 5.044  -5.758  -5.950  0.50 32.59 ?  163  LYS   A NZ   1 
ATOM   3546 H  H    A LYS   A 1 163 ? 3.695  -6.682  1.128   0.50 24.55 ?  163  LYS   A H    1 
ATOM   3547 H  H    B LYS   A 1 163 ? 3.565  -6.243  1.081   0.50 27.52 ?  163  LYS   A H    1 
ATOM   3548 H  HA   A LYS   A 1 163 ? 2.593  -8.737  -0.114  0.50 24.79 ?  163  LYS   A HA   1 
ATOM   3549 H  HA   B LYS   A 1 163 ? 2.744  -8.213  -0.406  0.50 27.58 ?  163  LYS   A HA   1 
ATOM   3550 H  HB2  A LYS   A 1 163 ? 2.907  -6.701  -1.208  0.50 26.95 ?  163  LYS   A HB2  1 
ATOM   3551 H  HB2  B LYS   A 1 163 ? 3.467  -6.045  -1.179  0.50 30.13 ?  163  LYS   A HB2  1 
ATOM   3552 H  HB3  A LYS   A 1 163 ? 4.477  -6.880  -1.097  0.50 26.95 ?  163  LYS   A HB3  1 
ATOM   3553 H  HB3  B LYS   A 1 163 ? 4.951  -6.582  -1.043  0.50 30.13 ?  163  LYS   A HB3  1 
ATOM   3554 H  HG2  A LYS   A 1 163 ? 4.314  -8.728  -2.559  0.50 29.78 ?  163  LYS   A HG2  1 
ATOM   3555 H  HG2  B LYS   A 1 163 ? 4.457  -8.195  -2.697  0.50 32.93 ?  163  LYS   A HG2  1 
ATOM   3556 H  HG3  A LYS   A 1 163 ? 2.770  -8.382  -2.747  0.50 29.78 ?  163  LYS   A HG3  1 
ATOM   3557 H  HG3  B LYS   A 1 163 ? 3.038  -7.492  -2.892  0.50 32.93 ?  163  LYS   A HG3  1 
ATOM   3558 H  HD2  A LYS   A 1 163 ? 3.376  -6.291  -3.634  0.50 32.60 ?  163  LYS   A HD2  1 
ATOM   3559 H  HD2  B LYS   A 1 163 ? 4.252  -5.468  -3.380  0.50 35.63 ?  163  LYS   A HD2  1 
ATOM   3560 H  HD3  A LYS   A 1 163 ? 4.910  -6.698  -3.500  0.50 32.60 ?  163  LYS   A HD3  1 
ATOM   3561 H  HD3  B LYS   A 1 163 ? 5.558  -6.370  -3.471  0.50 35.63 ?  163  LYS   A HD3  1 
ATOM   3562 H  HE2  A LYS   A 1 163 ? 4.390  -8.535  -4.996  0.50 34.50 ?  163  LYS   A HE2  1 
ATOM   3563 H  HE2  B LYS   A 1 163 ? 4.528  -7.574  -5.235  0.50 37.77 ?  163  LYS   A HE2  1 
ATOM   3564 H  HE3  A LYS   A 1 163 ? 3.028  -7.783  -5.273  0.50 34.50 ?  163  LYS   A HE3  1 
ATOM   3565 H  HE3  B LYS   A 1 163 ? 3.336  -6.521  -5.197  0.50 37.77 ?  163  LYS   A HE3  1 
ATOM   3566 H  HZ1  A LYS   A 1 163 ? 4.566  -7.243  -6.849  0.50 35.47 ?  163  LYS   A HZ1  1 
ATOM   3567 H  HZ1  B LYS   A 1 163 ? 4.851  -5.950  -6.797  0.50 39.10 ?  163  LYS   A HZ1  1 
ATOM   3568 H  HZ2  A LYS   A 1 163 ? 4.207  -6.047  -6.115  0.50 35.47 ?  163  LYS   A HZ2  1 
ATOM   3569 H  HZ2  B LYS   A 1 163 ? 4.831  -4.909  -5.789  0.50 39.10 ?  163  LYS   A HZ2  1 
ATOM   3570 H  HZ3  A LYS   A 1 163 ? 5.469  -6.708  -5.851  0.50 35.47 ?  163  LYS   A HZ3  1 
ATOM   3571 H  HZ3  B LYS   A 1 163 ? 5.919  -5.865  -5.822  0.50 39.10 ?  163  LYS   A HZ3  1 
ATOM   3572 N  N    A LEU   A 1 164 ? 5.683  -8.999  0.656   0.50 18.58 ?  164  LEU   A N    1 
ATOM   3573 N  N    B LEU   A 1 164 ? 5.716  -8.594  0.736   0.50 19.81 ?  164  LEU   A N    1 
ATOM   3574 C  CA   A LEU   A 1 164 ? 6.783  -9.954  0.776   0.50 17.73 ?  164  LEU   A CA   1 
ATOM   3575 C  CA   B LEU   A 1 164 ? 6.774  -9.581  0.926   0.50 18.71 ?  164  LEU   A CA   1 
ATOM   3576 C  C    A LEU   A 1 164 ? 6.365  -11.161 1.603   0.50 17.65 ?  164  LEU   A C    1 
ATOM   3577 C  C    B LEU   A 1 164 ? 6.313  -10.722 1.819   0.50 18.46 ?  164  LEU   A C    1 
ATOM   3578 O  O    A LEU   A 1 164 ? 6.724  -12.300 1.285   0.50 18.34 ?  164  LEU   A O    1 
ATOM   3579 O  O    B LEU   A 1 164 ? 6.576  -11.891 1.520   0.50 18.53 ?  164  LEU   A O    1 
ATOM   3580 C  CB   A LEU   A 1 164 ? 7.982  -9.267  1.433   0.50 17.55 ?  164  LEU   A CB   1 
ATOM   3581 C  CB   B LEU   A 1 164 ? 8.010  -8.912  1.520   0.50 18.25 ?  164  LEU   A CB   1 
ATOM   3582 C  CG   A LEU   A 1 164 ? 8.621  -8.100  0.671   0.50 17.63 ?  164  LEU   A CG   1 
ATOM   3583 C  CG   B LEU   A 1 164 ? 8.846  -8.081  0.549   0.50 18.05 ?  164  LEU   A CG   1 
ATOM   3584 C  CD1  A LEU   A 1 164 ? 9.535  -7.255  1.563   0.50 17.14 ?  164  LEU   A CD1  1 
ATOM   3585 C  CD1  B LEU   A 1 164 ? 9.833  -7.240  1.327   0.50 17.65 ?  164  LEU   A CD1  1 
ATOM   3586 C  CD2  A LEU   A 1 164 ? 9.396  -8.628  -0.520  0.50 18.01 ?  164  LEU   A CD2  1 
ATOM   3587 C  CD2  B LEU   A 1 164 ? 9.569  -8.971  -0.459  0.50 18.12 ?  164  LEU   A CD2  1 
ATOM   3588 H  H    A LEU   A 1 164 ? 5.843  -8.241  1.011   0.50 22.28 ?  164  LEU   A H    1 
ATOM   3589 H  H    B LEU   A 1 164 ? 5.869  -7.834  1.106   0.50 23.77 ?  164  LEU   A H    1 
ATOM   3590 H  HA   A LEU   A 1 164 ? 7.046  -10.269 -0.103  0.50 21.27 ?  164  LEU   A HA   1 
ATOM   3591 H  HA   B LEU   A 1 164 ? 7.018  -9.956  0.067   0.50 22.44 ?  164  LEU   A HA   1 
ATOM   3592 H  HB2  A LEU   A 1 164 ? 7.696  -8.928  2.294   0.50 21.06 ?  164  LEU   A HB2  1 
ATOM   3593 H  HB2  B LEU   A 1 164 ? 7.729  -8.321  2.234   0.50 21.89 ?  164  LEU   A HB2  1 
ATOM   3594 H  HB3  A LEU   A 1 164 ? 8.675  -9.934  1.567   0.50 21.06 ?  164  LEU   A HB3  1 
ATOM   3595 H  HB3  B LEU   A 1 164 ? 8.591  -9.602  1.881   0.50 21.89 ?  164  LEU   A HB3  1 
ATOM   3596 H  HG   A LEU   A 1 164 ? 7.919  -7.522  0.337   0.50 21.15 ?  164  LEU   A HG   1 
ATOM   3597 H  HG   B LEU   A 1 164 ? 8.261  -7.485  0.057   0.50 21.66 ?  164  LEU   A HG   1 
ATOM   3598 H  HD11 A LEU   A 1 164 ? 9.911  -6.532  1.036   0.50 20.56 ?  164  LEU   A HD11 1 
ATOM   3599 H  HD11 B LEU   A 1 164 ? 10.368 -6.726  0.706   0.50 21.17 ?  164  LEU   A HD11 1 
ATOM   3600 H  HD12 A LEU   A 1 164 ? 9.013  -6.890  2.296   0.50 20.56 ?  164  LEU   A HD12 1 
ATOM   3601 H  HD12 B LEU   A 1 164 ? 9.344  -6.648  1.918   0.50 21.17 ?  164  LEU   A HD12 1 
ATOM   3602 H  HD13 A LEU   A 1 164 ? 10.246 -7.815  1.911   0.50 20.56 ?  164  LEU   A HD13 1 
ATOM   3603 H  HD13 B LEU   A 1 164 ? 10.404 -7.829  1.848   0.50 21.17 ?  164  LEU   A HD13 1 
ATOM   3604 H  HD21 A LEU   A 1 164 ? 9.793  -7.881  -0.993  0.50 21.61 ?  164  LEU   A HD21 1 
ATOM   3605 H  HD21 B LEU   A 1 164 ? 10.162 -8.422  -0.996  0.50 21.74 ?  164  LEU   A HD21 1 
ATOM   3606 H  HD22 A LEU   A 1 164 ? 10.090 -9.227  -0.204  0.50 21.61 ?  164  LEU   A HD22 1 
ATOM   3607 H  HD22 B LEU   A 1 164 ? 10.081 -9.641  0.019   0.50 21.74 ?  164  LEU   A HD22 1 
ATOM   3608 H  HD23 A LEU   A 1 164 ? 8.787  -9.105  -1.104  0.50 21.61 ?  164  LEU   A HD23 1 
ATOM   3609 H  HD23 B LEU   A 1 164 ? 8.914  -9.403  -1.031  0.50 21.74 ?  164  LEU   A HD23 1 
ATOM   3610 N  N    A VAL   A 1 165 ? 5.611  -10.924 2.676   0.50 17.51 ?  165  VAL   A N    1 
ATOM   3611 N  N    B VAL   A 1 165 ? 5.641  -10.403 2.926   0.50 17.99 ?  165  VAL   A N    1 
ATOM   3612 C  CA   A VAL   A 1 165 ? 5.158  -12.006 3.544   0.50 17.14 ?  165  VAL   A CA   1 
ATOM   3613 C  CA   B VAL   A 1 165 ? 5.107  -11.452 3.790   0.50 17.92 ?  165  VAL   A CA   1 
ATOM   3614 C  C    A VAL   A 1 165 ? 4.113  -12.853 2.832   0.50 17.28 ?  165  VAL   A C    1 
ATOM   3615 C  C    B VAL   A 1 165 ? 4.074  -12.275 3.034   0.50 17.81 ?  165  VAL   A C    1 
ATOM   3616 O  O    A VAL   A 1 165 ? 4.236  -14.080 2.743   0.50 16.55 ?  165  VAL   A O    1 
ATOM   3617 O  O    B VAL   A 1 165 ? 4.133  -13.511 3.010   0.50 17.51 ?  165  VAL   A O    1 
ATOM   3618 C  CB   A VAL   A 1 165 ? 4.609  -11.419 4.858   0.50 17.50 ?  165  VAL   A CB   1 
ATOM   3619 C  CB   B VAL   A 1 165 ? 4.524  -10.847 5.080   0.50 18.45 ?  165  VAL   A CB   1 
ATOM   3620 C  CG1  A VAL   A 1 165 ? 3.906  -12.496 5.679   0.50 17.80 ?  165  VAL   A CG1  1 
ATOM   3621 C  CG1  B VAL   A 1 165 ? 3.768  -11.908 5.875   0.50 18.61 ?  165  VAL   A CG1  1 
ATOM   3622 C  CG2  A VAL   A 1 165 ? 5.724  -10.757 5.653   0.50 17.67 ?  165  VAL   A CG2  1 
ATOM   3623 C  CG2  B VAL   A 1 165 ? 5.627  -10.223 5.921   0.50 18.83 ?  165  VAL   A CG2  1 
ATOM   3624 H  H    A VAL   A 1 165 ? 5.346  -10.153 2.922   0.50 21.01 ?  165  VAL   A H    1 
ATOM   3625 H  H    B VAL   A 1 165 ? 5.485  -9.599  3.195   0.50 21.58 ?  165  VAL   A H    1 
ATOM   3626 H  HA   A VAL   A 1 165 ? 5.908  -12.584 3.766   0.50 20.56 ?  165  VAL   A HA   1 
ATOM   3627 H  HA   B VAL   A 1 165 ? 5.827  -12.045 4.046   0.50 21.49 ?  165  VAL   A HA   1 
ATOM   3628 H  HB   A VAL   A 1 165 ? 3.953  -10.740 4.646   0.50 20.99 ?  165  VAL   A HB   1 
ATOM   3629 H  HB   B VAL   A 1 165 ? 3.896  -10.145 4.849   0.50 22.14 ?  165  VAL   A HB   1 
ATOM   3630 H  HG11 A VAL   A 1 165 ? 3.798  -12.178 6.589   0.50 21.35 ?  165  VAL   A HG11 1 
ATOM   3631 H  HG11 B VAL   A 1 165 ? 3.647  -11.593 6.785   0.50 22.33 ?  165  VAL   A HG11 1 
ATOM   3632 H  HG12 A VAL   A 1 165 ? 3.034  -12.677 5.290   0.50 21.35 ?  165  VAL   A HG12 1 
ATOM   3633 H  HG12 B VAL   A 1 165 ? 2.904  -12.058 5.461   0.50 22.33 ?  165  VAL   A HG12 1 
ATOM   3634 H  HG13 A VAL   A 1 165 ? 4.445  -13.302 5.674   0.50 21.35 ?  165  VAL   A HG13 1 
ATOM   3635 H  HG13 B VAL   A 1 165 ? 4.285  -12.728 5.876   0.50 22.33 ?  165  VAL   A HG13 1 
ATOM   3636 H  HG21 A VAL   A 1 165 ? 5.359  -10.406 6.480   0.50 21.20 ?  165  VAL   A HG21 1 
ATOM   3637 H  HG21 B VAL   A 1 165 ? 5.242  -9.867  6.738   0.50 22.59 ?  165  VAL   A HG21 1 
ATOM   3638 H  HG22 A VAL   A 1 165 ? 6.410  -11.416 5.847   0.50 21.20 ?  165  VAL   A HG22 1 
ATOM   3639 H  HG22 B VAL   A 1 165 ? 6.285  -10.903 6.135   0.50 22.59 ?  165  VAL   A HG22 1 
ATOM   3640 H  HG23 A VAL   A 1 165 ? 6.100  -10.035 5.125   0.50 21.20 ?  165  VAL   A HG23 1 
ATOM   3641 H  HG23 B VAL   A 1 165 ? 6.045  -9.508  5.415   0.50 22.59 ?  165  VAL   A HG23 1 
ATOM   3642 N  N    A SER   A 1 166 ? 3.071  -12.207 2.308   0.50 18.27 ?  166  SER   A N    1 
ATOM   3643 N  N    B SER   A 1 166 ? 3.121  -11.598 2.390   0.50 18.01 ?  166  SER   A N    1 
ATOM   3644 C  CA   A SER   A 1 166 ? 1.953  -12.945 1.736   0.50 19.09 ?  166  SER   A CA   1 
ATOM   3645 C  CA   B SER   A 1 166 ? 1.990  -12.288 1.779   0.50 19.29 ?  166  SER   A CA   1 
ATOM   3646 C  C    A SER   A 1 166 ? 2.387  -13.758 0.533   0.50 19.79 ?  166  SER   A C    1 
ATOM   3647 C  C    B SER   A 1 166 ? 2.385  -13.144 0.582   0.50 19.72 ?  166  SER   A C    1 
ATOM   3648 O  O    A SER   A 1 166 ? 1.850  -14.845 0.293   0.50 20.35 ?  166  SER   A O    1 
ATOM   3649 O  O    B SER   A 1 166 ? 1.601  -14.013 0.184   0.50 20.80 ?  166  SER   A O    1 
ATOM   3650 C  CB   A SER   A 1 166 ? 0.844  -11.978 1.319   0.50 20.21 ?  166  SER   A CB   1 
ATOM   3651 C  CB   B SER   A 1 166 ? 0.926  -11.278 1.339   0.50 20.96 ?  166  SER   A CB   1 
ATOM   3652 O  OG   A SER   A 1 166 ? 0.342  -11.251 2.427   0.50 21.46 ?  166  SER   A OG   1 
ATOM   3653 O  OG   B SER   A 1 166 ? 0.536  -10.429 2.407   0.50 23.42 ?  166  SER   A OG   1 
ATOM   3654 H  H    A SER   A 1 166 ? 2.995  -11.363 2.265   0.50 21.92 ?  166  SER   A H    1 
ATOM   3655 H  H    B SER   A 1 166 ? 3.099  -10.738 2.309   0.50 21.61 ?  166  SER   A H    1 
ATOM   3656 H  HA   A SER   A 1 166 ? 1.592  -13.561 2.394   0.50 22.90 ?  166  SER   A HA   1 
ATOM   3657 H  HA   B SER   A 1 166 ? 1.582  -12.869 2.436   0.50 23.14 ?  166  SER   A HA   1 
ATOM   3658 H  HB2  A SER   A 1 166 ? 1.204  -11.357 0.670   0.50 24.24 ?  166  SER   A HB2  1 
ATOM   3659 H  HB2  B SER   A 1 166 ? 1.275  -10.733 0.619   0.50 25.14 ?  166  SER   A HB2  1 
ATOM   3660 H  HB3  A SER   A 1 166 ? 0.118  -12.488 0.922   0.50 24.24 ?  166  SER   A HB3  1 
ATOM   3661 H  HB3  B SER   A 1 166 ? 0.137  -11.761 1.031   0.50 25.14 ?  166  SER   A HB3  1 
ATOM   3662 H  HG   A SER   A 1 166 ? 0.971  -10.816 2.783   0.50 25.74 ?  166  SER   A HG   1 
ATOM   3663 H  HG   B SER   A 1 166 ? 1.196  -9.985  2.679   0.50 28.10 ?  166  SER   A HG   1 
ATOM   3664 N  N    A SER   A 1 167 ? 3.343  -13.244 -0.234  0.50 20.44 ?  167  SER   A N    1 
ATOM   3665 N  N    B SER   A 1 167 ? 3.563  -12.924 -0.006  0.50 19.69 ?  167  SER   A N    1 
ATOM   3666 C  CA   A SER   A 1 167 ? 3.880  -13.951 -1.380  0.50 21.81 ?  167  SER   A CA   1 
ATOM   3667 C  CA   B SER   A 1 167 ? 3.956  -13.633 -1.220  0.50 20.79 ?  167  SER   A CA   1 
ATOM   3668 C  C    A SER   A 1 167 ? 5.010  -14.896 -1.007  0.50 21.63 ?  167  SER   A C    1 
ATOM   3669 C  C    B SER   A 1 167 ? 5.130  -14.586 -1.005  0.50 21.11 ?  167  SER   A C    1 
ATOM   3670 O  O    A SER   A 1 167 ? 5.459  -15.661 -1.866  0.50 21.77 ?  167  SER   A O    1 
ATOM   3671 O  O    B SER   A 1 167 ? 5.717  -15.064 -1.982  0.50 21.25 ?  167  SER   A O    1 
ATOM   3672 C  CB   A SER   A 1 167 ? 4.374  -12.947 -2.433  0.50 22.74 ?  167  SER   A CB   1 
ATOM   3673 C  CB   B SER   A 1 167 ? 4.276  -12.643 -2.345  0.50 21.42 ?  167  SER   A CB   1 
ATOM   3674 O  OG   A SER   A 1 167 ? 5.328  -12.052 -1.886  0.50 23.43 ?  167  SER   A OG   1 
ATOM   3675 O  OG   B SER   A 1 167 ? 5.520  -12.000 -2.120  0.50 21.77 ?  167  SER   A OG   1 
ATOM   3676 H  H    A SER   A 1 167 ? 3.695  -12.473 -0.107  0.50 24.53 ?  167  SER   A H    1 
ATOM   3677 H  H    B SER   A 1 167 ? 4.154  -12.366 0.289   0.50 23.62 ?  167  SER   A H    1 
ATOM   3678 H  HA   A SER   A 1 167 ? 3.182  -14.481 -1.787  0.50 26.16 ?  167  SER   A HA   1 
ATOM   3679 H  HA   B SER   A 1 167 ? 3.202  -14.163 -1.512  0.50 24.94 ?  167  SER   A HA   1 
ATOM   3680 H  HB2  A SER   A 1 167 ? 4.782  -13.430 -3.168  0.50 27.29 ?  167  SER   A HB2  1 
ATOM   3681 H  HB2  B SER   A 1 167 ? 4.313  -13.133 -3.183  0.50 25.70 ?  167  SER   A HB2  1 
ATOM   3682 H  HB3  A SER   A 1 167 ? 3.614  -12.434 -2.759  0.50 27.29 ?  167  SER   A HB3  1 
ATOM   3683 H  HB3  B SER   A 1 167 ? 3.567  -11.977 -2.389  0.50 25.70 ?  167  SER   A HB3  1 
ATOM   3684 H  HG   A SER   A 1 167 ? 4.958  -11.323 -1.687  0.50 28.11 ?  167  SER   A HG   1 
ATOM   3685 H  HG   B SER   A 1 167 ? 5.485  -11.568 -1.403  0.50 26.12 ?  167  SER   A HG   1 
ATOM   3686 N  N    . PHE   A 1 168 ? 5.472  -14.884 0.244   1.00 21.38 ?  168  PHE   A N    1 
ATOM   3687 C  CA   . PHE   A 1 168 ? 6.649  -15.679 0.570   1.00 22.33 ?  168  PHE   A CA   1 
ATOM   3688 C  C    . PHE   A 1 168 ? 6.343  -17.163 0.472   1.00 25.22 ?  168  PHE   A C    1 
ATOM   3689 O  O    . PHE   A 1 168 ? 5.379  -17.654 1.069   1.00 26.15 ?  168  PHE   A O    1 
ATOM   3690 C  CB   . PHE   A 1 168 ? 7.161  -15.376 1.976   1.00 21.36 ?  168  PHE   A CB   1 
ATOM   3691 C  CG   . PHE   A 1 168 ? 8.436  -16.102 2.302   1.00 20.35 ?  168  PHE   A CG   1 
ATOM   3692 C  CD1  . PHE   A 1 168 ? 9.621  -15.720 1.706   1.00 20.35 ?  168  PHE   A CD1  1 
ATOM   3693 C  CD2  . PHE   A 1 168 ? 8.452  -17.184 3.169   1.00 19.80 ?  168  PHE   A CD2  1 
ATOM   3694 C  CE1  . PHE   A 1 168 ? 10.798 -16.385 1.979   1.00 19.40 ?  168  PHE   A CE1  1 
ATOM   3695 C  CE2  . PHE   A 1 168 ? 9.632  -17.850 3.447   1.00 19.48 ?  168  PHE   A CE2  1 
ATOM   3696 C  CZ   . PHE   A 1 168 ? 10.803 -17.449 2.848   1.00 19.33 ?  168  PHE   A CZ   1 
ATOM   3697 H  H    A PHE   A 1 168 ? 5.131  -14.443 0.898   0.50 25.65 ?  168  PHE   A H    1 
ATOM   3698 H  H    B PHE   A 1 168 ? 5.034  -14.623 0.934   0.50 25.65 ?  168  PHE   A H    1 
ATOM   3699 H  HA   . PHE   A 1 168 ? 7.358  -15.471 -0.063  1.00 26.79 ?  168  PHE   A HA   1 
ATOM   3700 H  HB2  . PHE   A 1 168 ? 7.335  -14.426 2.053   1.00 25.63 ?  168  PHE   A HB2  1 
ATOM   3701 H  HB3  . PHE   A 1 168 ? 6.490  -15.646 2.619   1.00 25.63 ?  168  PHE   A HB3  1 
ATOM   3702 H  HD1  . PHE   A 1 168 ? 9.633  -15.002 1.116   1.00 24.42 ?  168  PHE   A HD1  1 
ATOM   3703 H  HD2  . PHE   A 1 168 ? 7.660  -17.459 3.574   1.00 23.76 ?  168  PHE   A HD2  1 
ATOM   3704 H  HE1  . PHE   A 1 168 ? 11.597 -16.115 1.577   1.00 23.28 ?  168  PHE   A HE1  1 
ATOM   3705 H  HE2  . PHE   A 1 168 ? 9.630  -18.573 4.035   1.00 23.37 ?  168  PHE   A HE2  1 
ATOM   3706 H  HZ   . PHE   A 1 168 ? 11.601 -17.897 3.035   1.00 23.19 ?  168  PHE   A HZ   1 
ATOM   3707 N  N    . LEU   A 1 169 ? 7.195  -17.882 -0.253  1.00 29.60 ?  169  LEU   A N    1 
ATOM   3708 C  CA   . LEU   A 1 169 ? 7.027  -19.311 -0.409  1.00 35.46 ?  169  LEU   A CA   1 
ATOM   3709 C  C    . LEU   A 1 169 ? 7.905  -20.020 0.611   1.00 37.03 ?  169  LEU   A C    1 
ATOM   3710 O  O    . LEU   A 1 169 ? 7.420  -20.422 1.669   1.00 37.56 ?  169  LEU   A O    1 
ATOM   3711 C  CB   . LEU   A 1 169 ? 7.383  -19.742 -1.835  1.00 38.95 ?  169  LEU   A CB   1 
ATOM   3712 C  CG   . LEU   A 1 169 ? 6.970  -21.160 -2.236  1.00 41.53 ?  169  LEU   A CG   1 
ATOM   3713 C  CD1  . LEU   A 1 169 ? 5.547  -21.454 -1.784  1.00 42.46 ?  169  LEU   A CD1  1 
ATOM   3714 C  CD2  . LEU   A 1 169 ? 7.097  -21.342 -3.741  1.00 42.39 ?  169  LEU   A CD2  1 
ATOM   3715 O  OXT  . LEU   A 1 169 ? 9.112  -20.183 0.414   1.00 36.93 -1 169  LEU   A OXT  1 
ATOM   3716 H  H    . LEU   A 1 169 ? 7.884  -17.564 -0.660  1.00 35.52 ?  169  LEU   A H    1 
ATOM   3717 H  HA   . LEU   A 1 169 ? 6.101  -19.534 -0.233  1.00 42.55 ?  169  LEU   A HA   1 
ATOM   3718 H  HB2  . LEU   A 1 169 ? 6.952  -19.132 -2.453  1.00 46.74 ?  169  LEU   A HB2  1 
ATOM   3719 H  HB3  . LEU   A 1 169 ? 8.345  -19.683 -1.942  1.00 46.74 ?  169  LEU   A HB3  1 
ATOM   3720 H  HG   . LEU   A 1 169 ? 7.561  -21.798 -1.806  1.00 49.83 ?  169  LEU   A HG   1 
ATOM   3721 H  HD11 . LEU   A 1 169 ? 5.216  -22.225 -2.266  1.00 50.95 ?  169  LEU   A HD11 1 
ATOM   3722 H  HD12 . LEU   A 1 169 ? 5.550  -21.635 -0.830  1.00 50.95 ?  169  LEU   A HD12 1 
ATOM   3723 H  HD13 . LEU   A 1 169 ? 4.992  -20.681 -1.974  1.00 50.95 ?  169  LEU   A HD13 1 
ATOM   3724 H  HD21 . LEU   A 1 169 ? 6.843  -22.249 -3.972  1.00 50.86 ?  169  LEU   A HD21 1 
ATOM   3725 H  HD22 . LEU   A 1 169 ? 6.508  -20.711 -4.185  1.00 50.86 ?  169  LEU   A HD22 1 
ATOM   3726 H  HD23 . LEU   A 1 169 ? 8.016  -21.178 -4.002  1.00 50.86 ?  169  LEU   A HD23 1 
ATOM   3727 N  N    A SER   B 1 1   ? 50.720 -9.141  -23.698 0.50 29.23 ?  1    SER   B N    1 
ATOM   3728 N  N    B SER   B 1 1   ? 50.785 -9.277  -23.787 0.50 24.95 ?  1    SER   B N    1 
ATOM   3729 C  CA   A SER   B 1 1   ? 51.247 -10.225 -22.846 0.50 28.82 ?  1    SER   B CA   1 
ATOM   3730 C  CA   B SER   B 1 1   ? 51.221 -10.258 -22.770 0.50 24.89 ?  1    SER   B CA   1 
ATOM   3731 C  C    A SER   B 1 1   ? 50.188 -11.291 -22.607 0.50 27.59 ?  1    SER   B C    1 
ATOM   3732 C  C    B SER   B 1 1   ? 50.131 -11.291 -22.497 0.50 24.84 ?  1    SER   B C    1 
ATOM   3733 O  O    A SER   B 1 1   ? 48.995 -11.095 -22.875 0.50 27.49 ?  1    SER   B O    1 
ATOM   3734 O  O    B SER   B 1 1   ? 48.949 -11.099 -22.828 0.50 24.68 ?  1    SER   B O    1 
ATOM   3735 C  CB   A SER   B 1 1   ? 51.734 -9.671  -21.509 0.50 29.44 ?  1    SER   B CB   1 
ATOM   3736 C  CB   B SER   B 1 1   ? 51.615 -9.556  -21.473 0.50 24.82 ?  1    SER   B CB   1 
ATOM   3737 O  OG   A SER   B 1 1   ? 50.646 -9.237  -20.716 0.50 30.64 ?  1    SER   B OG   1 
ATOM   3738 O  OG   B SER   B 1 1   ? 50.641 -9.761  -20.467 0.50 25.87 ?  1    SER   B OG   1 
ATOM   3739 H  H1   A SER   B 1 1   ? 50.499 -9.477  -24.489 0.50 35.07 ?  1    SER   B H1   1 
ATOM   3740 H  H1   B SER   B 1 1   ? 51.504 -8.894  -24.144 0.50 29.93 ?  1    SER   B H1   1 
ATOM   3741 H  H2   A SER   B 1 1   ? 50.007 -8.788  -23.308 0.50 35.07 ?  1    SER   B H2   1 
ATOM   3742 H  H2   B SER   B 1 1   ? 50.323 -9.697  -24.416 0.50 29.93 ?  1    SER   B H2   1 
ATOM   3743 H  H3   A SER   B 1 1   ? 51.350 -8.524  -23.798 0.50 35.07 ?  1    SER   B H3   1 
ATOM   3744 H  H3   B SER   B 1 1   ? 50.279 -8.663  -23.396 0.50 29.93 ?  1    SER   B H3   1 
ATOM   3745 H  HA   A SER   B 1 1   ? 51.996 -10.633 -23.301 0.50 34.58 ?  1    SER   B HA   1 
ATOM   3746 H  HA   B SER   B 1 1   ? 52.000 -10.715 -23.116 0.50 29.87 ?  1    SER   B HA   1 
ATOM   3747 H  HB2  A SER   B 1 1   ? 52.222 -10.370 -21.045 0.50 35.32 ?  1    SER   B HB2  1 
ATOM   3748 H  HB2  B SER   B 1 1   ? 52.458 -9.921  -21.169 0.50 29.78 ?  1    SER   B HB2  1 
ATOM   3749 H  HB3  A SER   B 1 1   ? 52.314 -8.914  -21.673 0.50 35.32 ?  1    SER   B HB3  1 
ATOM   3750 H  HB3  B SER   B 1 1   ? 51.707 -8.604  -21.643 0.50 29.78 ?  1    SER   B HB3  1 
ATOM   3751 H  HG   A SER   B 1 1   ? 50.932 -8.836  -20.037 0.50 36.76 ?  1    SER   B HG   1 
ATOM   3752 H  HG   B SER   B 1 1   ? 50.717 -9.166  -19.877 0.50 31.04 ?  1    SER   B HG   1 
ATOM   3753 N  N    A MET   B 1 2   ? 50.646 -12.424 -22.090 0.50 26.61 ?  2    MET   B N    1 
ATOM   3754 N  N    B MET   B 1 2   ? 50.547 -12.392 -21.882 0.50 25.24 ?  2    MET   B N    1 
ATOM   3755 C  CA   A MET   B 1 2   ? 49.825 -13.610 -21.910 0.50 26.47 ?  2    MET   B CA   1 
ATOM   3756 C  CA   B MET   B 1 2   ? 49.727 -13.590 -21.727 0.50 26.07 ?  2    MET   B CA   1 
ATOM   3757 C  C    A MET   B 1 2   ? 49.595 -13.816 -20.421 0.50 23.83 ?  2    MET   B C    1 
ATOM   3758 C  C    B MET   B 1 2   ? 49.456 -13.809 -20.243 0.50 24.57 ?  2    MET   B C    1 
ATOM   3759 O  O    A MET   B 1 2   ? 50.549 -14.026 -19.667 0.50 23.19 ?  2    MET   B O    1 
ATOM   3760 O  O    B MET   B 1 2   ? 50.336 -14.265 -19.505 0.50 25.02 ?  2    MET   B O    1 
ATOM   3761 C  CB   A MET   B 1 2   ? 50.535 -14.816 -22.517 0.50 29.99 ?  2    MET   B CB   1 
ATOM   3762 C  CB   B MET   B 1 2   ? 50.471 -14.772 -22.325 0.50 29.20 ?  2    MET   B CB   1 
ATOM   3763 C  CG   A MET   B 1 2   ? 49.685 -16.071 -22.622 0.50 33.20 ?  2    MET   B CG   1 
ATOM   3764 C  CG   B MET   B 1 2   ? 49.606 -15.952 -22.742 0.50 31.82 ?  2    MET   B CG   1 
ATOM   3765 S  SD   A MET   B 1 2   ? 50.510 -17.347 -23.593 0.50 36.13 ?  2    MET   B SD   1 
ATOM   3766 S  SD   B MET   B 1 2   ? 50.520 -17.082 -23.802 0.50 34.23 ?  2    MET   B SD   1 
ATOM   3767 C  CE   A MET   B 1 2   ? 51.050 -16.359 -24.987 0.50 36.24 ?  2    MET   B CE   1 
ATOM   3768 C  CE   B MET   B 1 2   ? 51.450 -15.914 -24.778 0.50 34.39 ?  2    MET   B CE   1 
ATOM   3769 H  H    A MET   B 1 2   ? 51.458 -12.536 -21.825 0.50 31.93 ?  2    MET   B H    1 
ATOM   3770 H  H    B MET   B 1 2   ? 51.335 -12.480 -21.545 0.50 30.28 ?  2    MET   B H    1 
ATOM   3771 H  HA   A MET   B 1 2   ? 48.975 -13.503 -22.362 0.50 31.76 ?  2    MET   B HA   1 
ATOM   3772 H  HA   B MET   B 1 2   ? 48.894 -13.485 -22.213 0.50 31.27 ?  2    MET   B HA   1 
ATOM   3773 H  HB2  A MET   B 1 2   ? 50.817 -14.551 -23.403 0.50 35.98 ?  2    MET   B HB2  1 
ATOM   3774 H  HB2  B MET   B 1 2   ? 50.929 -14.413 -23.091 0.50 35.03 ?  2    MET   B HB2  1 
ATOM   3775 H  HB3  A MET   B 1 2   ? 51.310 -15.040 -21.982 0.50 35.98 ?  2    MET   B HB3  1 
ATOM   3776 H  HB3  B MET   B 1 2   ? 51.117 -15.115 -21.692 0.50 35.03 ?  2    MET   B HB3  1 
ATOM   3777 H  HG2  A MET   B 1 2   ? 49.521 -16.420 -21.730 0.50 39.83 ?  2    MET   B HG2  1 
ATOM   3778 H  HG2  B MET   B 1 2   ? 49.322 -16.440 -21.949 0.50 38.18 ?  2    MET   B HG2  1 
ATOM   3779 H  HG3  A MET   B 1 2   ? 48.847 -15.860 -23.061 0.50 39.83 ?  2    MET   B HG3  1 
ATOM   3780 H  HG3  B MET   B 1 2   ? 48.836 -15.646 -23.238 0.50 38.18 ?  2    MET   B HG3  1 
ATOM   3781 H  HE1  A MET   B 1 2   ? 51.214 -16.942 -25.732 0.50 43.49 ?  2    MET   B HE1  1 
ATOM   3782 H  HE1  B MET   B 1 2   ? 51.761 -16.370 -25.552 0.50 41.26 ?  2    MET   B HE1  1 
ATOM   3783 H  HE2  A MET   B 1 2   ? 50.346 -15.723 -25.205 0.50 43.49 ?  2    MET   B HE2  1 
ATOM   3784 H  HE2  B MET   B 1 2   ? 50.864 -15.178 -25.032 0.50 41.26 ?  2    MET   B HE2  1 
ATOM   3785 H  HE3  A MET   B 1 2   ? 51.863 -15.877 -24.752 0.50 43.49 ?  2    MET   B HE3  1 
ATOM   3786 H  HE3  B MET   B 1 2   ? 52.205 -15.580 -24.257 0.50 41.26 ?  2    MET   B HE3  1 
ATOM   3787 N  N    A VAL   B 1 3   ? 48.335 -13.725 -20.002 0.50 21.54 ?  3    VAL   B N    1 
ATOM   3788 N  N    B VAL   B 1 3   ? 48.242 -13.486 -19.810 0.50 22.54 ?  3    VAL   B N    1 
ATOM   3789 C  CA   A VAL   B 1 3   ? 47.938 -13.968 -18.623 0.50 20.22 ?  3    VAL   B CA   1 
ATOM   3790 C  CA   B VAL   B 1 3   ? 47.806 -13.744 -18.443 0.50 21.21 ?  3    VAL   B CA   1 
ATOM   3791 C  C    A VAL   B 1 3   ? 46.697 -14.853 -18.630 0.50 18.61 ?  3    VAL   B C    1 
ATOM   3792 C  C    B VAL   B 1 3   ? 46.552 -14.604 -18.483 0.50 19.39 ?  3    VAL   B C    1 
ATOM   3793 O  O    A VAL   B 1 3   ? 45.998 -14.982 -19.638 0.50 18.33 ?  3    VAL   B O    1 
ATOM   3794 O  O    B VAL   B 1 3   ? 45.728 -14.504 -19.396 0.50 19.56 ?  3    VAL   B O    1 
ATOM   3795 C  CB   A VAL   B 1 3   ? 47.665 -12.658 -17.850 0.50 21.90 ?  3    VAL   B CB   1 
ATOM   3796 C  CB   B VAL   B 1 3   ? 47.571 -12.456 -17.621 0.50 22.35 ?  3    VAL   B CB   1 
ATOM   3797 C  CG1  A VAL   B 1 3   ? 48.927 -11.799 -17.777 0.50 22.43 ?  3    VAL   B CG1  1 
ATOM   3798 C  CG1  B VAL   B 1 3   ? 48.856 -11.639 -17.522 0.50 22.78 ?  3    VAL   B CG1  1 
ATOM   3799 C  CG2  A VAL   B 1 3   ? 46.520 -11.887 -18.495 0.50 22.59 ?  3    VAL   B CG2  1 
ATOM   3800 C  CG2  B VAL   B 1 3   ? 46.437 -11.634 -18.215 0.50 22.64 ?  3    VAL   B CG2  1 
ATOM   3801 H  H    A VAL   B 1 3   ? 47.678 -13.516 -20.513 0.50 25.84 ?  3    VAL   B H    1 
ATOM   3802 H  H    B VAL   B 1 3   ? 47.643 -13.120 -20.304 0.50 27.04 ?  3    VAL   B H    1 
ATOM   3803 H  HA   A VAL   B 1 3   ? 48.654 -14.443 -18.165 0.50 24.25 ?  3    VAL   B HA   1 
ATOM   3804 H  HA   B VAL   B 1 3   ? 48.489 -14.255 -17.990 0.50 25.44 ?  3    VAL   B HA   1 
ATOM   3805 H  HB   A VAL   B 1 3   ? 47.404 -12.879 -16.942 0.50 26.27 ?  3    VAL   B HB   1 
ATOM   3806 H  HB   B VAL   B 1 3   ? 47.316 -12.706 -16.720 0.50 26.82 ?  3    VAL   B HB   1 
ATOM   3807 H  HG11 A VAL   B 1 3   ? 48.729 -10.993 -17.274 0.50 26.91 ?  3    VAL   B HG11 1 
ATOM   3808 H  HG11 B VAL   B 1 3   ? 48.684 -10.846 -16.989 0.50 27.33 ?  3    VAL   B HG11 1 
ATOM   3809 H  HG12 A VAL   B 1 3   ? 49.626 -12.303 -17.332 0.50 26.91 ?  3    VAL   B HG12 1 
ATOM   3810 H  HG12 B VAL   B 1 3   ? 49.541 -12.180 -17.099 0.50 27.33 ?  3    VAL   B HG12 1 
ATOM   3811 H  HG13 A VAL   B 1 3   ? 49.204 -11.569 -18.676 0.50 26.91 ?  3    VAL   B HG13 1 
ATOM   3812 H  HG13 B VAL   B 1 3   ? 49.137 -11.384 -18.414 0.50 27.33 ?  3    VAL   B HG13 1 
ATOM   3813 H  HG21 A VAL   B 1 3   ? 46.463 -11.010 -18.088 0.50 27.10 ?  3    VAL   B HG21 1 
ATOM   3814 H  HG21 B VAL   B 1 3   ? 46.428 -10.760 -17.797 0.50 27.16 ?  3    VAL   B HG21 1 
ATOM   3815 H  HG22 A VAL   B 1 3   ? 46.693 -11.802 -19.445 0.50 27.10 ?  3    VAL   B HG22 1 
ATOM   3816 H  HG22 B VAL   B 1 3   ? 46.579 -11.545 -19.169 0.50 27.16 ?  3    VAL   B HG22 1 
ATOM   3817 H  HG23 A VAL   B 1 3   ? 45.692 -12.373 -18.352 0.50 27.10 ?  3    VAL   B HG23 1 
ATOM   3818 H  HG23 B VAL   B 1 3   ? 45.597 -12.090 -18.046 0.50 27.16 ?  3    VAL   B HG23 1 
ATOM   3819 N  N    . ASN   B 1 4   ? 46.423 -15.466 -17.479 1.00 17.62 ?  4    ASN   B N    1 
ATOM   3820 C  CA   . ASN   B 1 4   ? 45.284 -16.373 -17.356 1.00 16.35 ?  4    ASN   B CA   1 
ATOM   3821 C  C    . ASN   B 1 4   ? 45.228 -17.342 -18.537 1.00 16.60 ?  4    ASN   B C    1 
ATOM   3822 O  O    . ASN   B 1 4   ? 44.167 -17.598 -19.104 1.00 17.27 ?  4    ASN   B O    1 
ATOM   3823 C  CB   . ASN   B 1 4   ? 43.964 -15.612 -17.199 1.00 15.67 ?  4    ASN   B CB   1 
ATOM   3824 C  CG   . ASN   B 1 4   ? 43.916 -14.795 -15.924 1.00 14.96 ?  4    ASN   B CG   1 
ATOM   3825 O  OD1  . ASN   B 1 4   ? 44.205 -15.300 -14.845 1.00 14.59 ?  4    ASN   B OD1  1 
ATOM   3826 N  ND2  . ASN   B 1 4   ? 43.572 -13.520 -16.044 1.00 15.84 ?  4    ASN   B ND2  1 
ATOM   3827 H  H    A ASN   B 1 4   ? 46.878 -15.367 -16.760 0.50 21.13 ?  4    ASN   B H    1 
ATOM   3828 H  H    B ASN   B 1 4   ? 47.006 -15.556 -16.857 0.50 21.13 ?  4    ASN   B H    1 
ATOM   3829 H  HA   . ASN   B 1 4   ? 45.413 -16.903 -16.551 1.00 19.62 ?  4    ASN   B HA   1 
ATOM   3830 H  HB2  . ASN   B 1 4   ? 43.848 -15.012 -17.946 1.00 18.80 ?  4    ASN   B HB2  1 
ATOM   3831 H  HB3  . ASN   B 1 4   ? 43.235 -16.257 -17.173 1.00 18.80 ?  4    ASN   B HB3  1 
ATOM   3832 H  HD21 . ASN   B 1 4   ? 43.537 -13.017 -15.345 1.00 19.00 ?  4    ASN   B HD21 1 
ATOM   3833 H  HD22 . ASN   B 1 4   ? 43.387 -13.196 -16.816 1.00 19.00 ?  4    ASN   B HD22 1 
ATOM   3834 N  N    . SER   B 1 5   ? 46.389 -17.877 -18.917 1.00 17.97 ?  5    SER   B N    1 
ATOM   3835 C  CA   . SER   B 1 5   ? 46.484 -18.792 -20.054 1.00 20.36 ?  5    SER   B CA   1 
ATOM   3836 C  C    . SER   B 1 5   ? 46.470 -20.226 -19.539 1.00 21.83 ?  5    SER   B C    1 
ATOM   3837 O  O    . SER   B 1 5   ? 47.480 -20.923 -19.513 1.00 23.87 ?  5    SER   B O    1 
ATOM   3838 C  CB   . SER   B 1 5   ? 47.739 -18.500 -20.873 1.00 22.00 ?  5    SER   B CB   1 
ATOM   3839 O  OG   . SER   B 1 5   ? 48.917 -18.686 -20.104 1.00 24.70 ?  5    SER   B OG   1 
ATOM   3840 H  H    . SER   B 1 5   ? 47.144 -17.731 -18.527 1.00 21.56 ?  5    SER   B H    1 
ATOM   3841 H  HA   . SER   B 1 5   ? 45.714 -18.675 -20.626 1.00 24.42 ?  5    SER   B HA   1 
ATOM   3842 H  HB2  . SER   B 1 5   ? 47.755 -19.097 -21.641 1.00 26.39 ?  5    SER   B HB2  1 
ATOM   3843 H  HB3  . SER   B 1 5   ? 47.691 -17.582 -21.173 1.00 26.39 ?  5    SER   B HB3  1 
ATOM   3844 H  HG   . SER   B 1 5   ? 48.978 -19.489 -19.865 1.00 29.63 ?  5    SER   B HG   1 
ATOM   3845 N  N    . PHE   B 1 6   ? 45.285 -20.643 -19.104 1.00 21.92 ?  6    PHE   B N    1 
ATOM   3846 C  CA   . PHE   B 1 6   ? 45.085 -21.986 -18.582 1.00 21.31 ?  6    PHE   B CA   1 
ATOM   3847 C  C    . PHE   B 1 6   ? 45.006 -22.971 -19.738 1.00 24.65 ?  6    PHE   B C    1 
ATOM   3848 O  O    . PHE   B 1 6   ? 44.322 -22.715 -20.733 1.00 26.53 ?  6    PHE   B O    1 
ATOM   3849 C  CB   . PHE   B 1 6   ? 43.794 -22.031 -17.765 1.00 19.38 ?  6    PHE   B CB   1 
ATOM   3850 C  CG   . PHE   B 1 6   ? 43.823 -21.167 -16.535 1.00 17.37 ?  6    PHE   B CG   1 
ATOM   3851 C  CD1  . PHE   B 1 6   ? 44.339 -21.656 -15.353 1.00 16.29 ?  6    PHE   B CD1  1 
ATOM   3852 C  CD2  . PHE   B 1 6   ? 43.342 -19.865 -16.566 1.00 16.68 ?  6    PHE   B CD2  1 
ATOM   3853 C  CE1  . PHE   B 1 6   ? 44.360 -20.873 -14.213 1.00 15.94 ?  6    PHE   B CE1  1 
ATOM   3854 C  CE2  . PHE   B 1 6   ? 43.372 -19.069 -15.433 1.00 16.79 ?  6    PHE   B CE2  1 
ATOM   3855 C  CZ   . PHE   B 1 6   ? 43.884 -19.569 -14.258 1.00 15.91 ?  6    PHE   B CZ   1 
ATOM   3856 H  H    . PHE   B 1 6   ? 44.572 -20.164 -19.102 1.00 26.30 ?  6    PHE   B H    1 
ATOM   3857 H  HA   . PHE   B 1 6   ? 45.825 -22.236 -18.010 1.00 25.57 ?  6    PHE   B HA   1 
ATOM   3858 H  HB2  . PHE   B 1 6   ? 43.060 -21.730 -18.323 1.00 23.25 ?  6    PHE   B HB2  1 
ATOM   3859 H  HB3  . PHE   B 1 6   ? 43.635 -22.945 -17.480 1.00 23.25 ?  6    PHE   B HB3  1 
ATOM   3860 H  HD1  . PHE   B 1 6   ? 44.669 -22.524 -15.319 1.00 19.54 ?  6    PHE   B HD1  1 
ATOM   3861 H  HD2  . PHE   B 1 6   ? 42.991 -19.525 -17.358 1.00 20.01 ?  6    PHE   B HD2  1 
ATOM   3862 H  HE1  . PHE   B 1 6   ? 44.723 -21.207 -13.420 1.00 19.12 ?  6    PHE   B HE1  1 
ATOM   3863 H  HE2  . PHE   B 1 6   ? 43.042 -18.198 -15.465 1.00 20.14 ?  6    PHE   B HE2  1 
ATOM   3864 H  HZ   . PHE   B 1 6   ? 43.908 -19.039 -13.493 1.00 19.09 ?  6    PHE   B HZ   1 
ATOM   3865 N  N    . SER   B 1 7   ? 45.717 -24.089 -19.610 1.00 25.65 ?  7    SER   B N    1 
ATOM   3866 C  CA   . SER   B 1 7   ? 45.802 -25.075 -20.678 1.00 28.29 ?  7    SER   B CA   1 
ATOM   3867 C  C    . SER   B 1 7   ? 45.757 -26.478 -20.093 1.00 27.52 ?  7    SER   B C    1 
ATOM   3868 O  O    . SER   B 1 7   ? 46.350 -26.748 -19.045 1.00 28.38 ?  7    SER   B O    1 
ATOM   3869 C  CB   . SER   B 1 7   ? 47.093 -24.894 -21.487 1.00 30.93 ?  7    SER   B CB   1 
ATOM   3870 O  OG   . SER   B 1 7   ? 47.042 -25.631 -22.696 1.00 33.07 ?  7    SER   B OG   1 
ATOM   3871 H  H    . SER   B 1 7   ? 46.169 -24.296 -18.905 1.00 30.77 ?  7    SER   B H    1 
ATOM   3872 H  HA   . SER   B 1 7   ? 45.049 -24.969 -21.276 1.00 33.95 ?  7    SER   B HA   1 
ATOM   3873 H  HB2  . SER   B 1 7   ? 47.211 -23.949 -21.686 1.00 37.11 ?  7    SER   B HB2  1 
ATOM   3874 H  HB3  . SER   B 1 7   ? 47.844 -25.214 -20.963 1.00 37.11 ?  7    SER   B HB3  1 
ATOM   3875 H  HG   . SER   B 1 7   ? 47.749 -25.507 -23.138 1.00 39.68 ?  7    SER   B HG   1 
ATOM   3876 N  N    . GLY   B 1 8   ? 45.049 -27.370 -20.782 1.00 27.43 ?  8    GLY   B N    1 
ATOM   3877 C  CA   . GLY   B 1 8   ? 45.016 -28.761 -20.392 1.00 26.35 ?  8    GLY   B CA   1 
ATOM   3878 C  C    . GLY   B 1 8   ? 44.070 -29.084 -19.264 1.00 24.80 ?  8    GLY   B C    1 
ATOM   3879 O  O    . GLY   B 1 8   ? 44.215 -30.140 -18.634 1.00 26.37 ?  8    GLY   B O    1 
ATOM   3880 H  H    . GLY   B 1 8   ? 44.584 -27.183 -21.477 1.00 32.91 ?  8    GLY   B H    1 
ATOM   3881 H  HA2  . GLY   B 1 8   ? 44.759 -29.294 -21.159 1.00 31.61 ?  8    GLY   B HA2  1 
ATOM   3882 H  HA3  . GLY   B 1 8   ? 45.902 -29.034 -20.116 1.00 31.61 ?  8    GLY   B HA3  1 
ATOM   3883 N  N    . TYR   B 1 9   ? 43.089 -28.225 -18.996 1.00 22.92 ?  9    TYR   B N    1 
ATOM   3884 C  CA   . TYR   B 1 9   ? 42.128 -28.492 -17.941 1.00 20.81 ?  9    TYR   B CA   1 
ATOM   3885 C  C    . TYR   B 1 9   ? 40.942 -29.276 -18.466 1.00 20.31 ?  9    TYR   B C    1 
ATOM   3886 O  O    . TYR   B 1 9   ? 40.523 -29.126 -19.618 1.00 22.08 ?  9    TYR   B O    1 
ATOM   3887 C  CB   . TYR   B 1 9   ? 41.623 -27.201 -17.300 1.00 20.14 ?  9    TYR   B CB   1 
ATOM   3888 C  CG   . TYR   B 1 9   ? 42.644 -26.582 -16.380 1.00 19.55 ?  9    TYR   B CG   1 
ATOM   3889 C  CD1  . TYR   B 1 9   ? 43.745 -25.918 -16.895 1.00 20.04 ?  9    TYR   B CD1  1 
ATOM   3890 C  CD2  . TYR   B 1 9   ? 42.523 -26.678 -15.003 1.00 18.84 ?  9    TYR   B CD2  1 
ATOM   3891 C  CE1  . TYR   B 1 9   ? 44.697 -25.367 -16.065 1.00 20.43 ?  9    TYR   B CE1  1 
ATOM   3892 C  CE2  . TYR   B 1 9   ? 43.470 -26.127 -14.162 1.00 19.37 ?  9    TYR   B CE2  1 
ATOM   3893 C  CZ   . TYR   B 1 9   ? 44.555 -25.469 -14.702 1.00 20.09 ?  9    TYR   B CZ   1 
ATOM   3894 O  OH   . TYR   B 1 9   ? 45.504 -24.920 -13.876 1.00 20.67 ?  9    TYR   B OH   1 
ATOM   3895 H  H    . TYR   B 1 9   ? 42.942 -27.496 -19.427 1.00 27.50 ?  9    TYR   B H    1 
ATOM   3896 H  HA   . TYR   B 1 9   ? 42.547 -29.020 -17.251 1.00 24.97 ?  9    TYR   B HA   1 
ATOM   3897 H  HB2  . TYR   B 1 9   ? 41.404 -26.554 -17.991 1.00 24.16 ?  9    TYR   B HB2  1 
ATOM   3898 H  HB3  . TYR   B 1 9   ? 40.837 -27.406 -16.774 1.00 24.16 ?  9    TYR   B HB3  1 
ATOM   3899 H  HD1  . TYR   B 1 9   ? 43.846 -25.850 -17.817 1.00 24.04 ?  9    TYR   B HD1  1 
ATOM   3900 H  HD2  . TYR   B 1 9   ? 41.788 -27.127 -14.639 1.00 22.60 ?  9    TYR   B HD2  1 
ATOM   3901 H  HE1  . TYR   B 1 9   ? 45.427 -24.926 -16.425 1.00 24.51 ?  9    TYR   B HE1  1 
ATOM   3902 H  HE2  . TYR   B 1 9   ? 43.370 -26.203 -13.239 1.00 23.23 ?  9    TYR   B HE2  1 
ATOM   3903 H  HH   . TYR   B 1 9   ? 46.095 -24.547 -14.333 1.00 24.80 ?  9    TYR   B HH   1 
ATOM   3904 N  N    . LEU   B 1 10  ? 40.408 -30.121 -17.595 1.00 18.37 ?  10   LEU   B N    1 
ATOM   3905 C  CA   . LEU   B 1 10  ? 39.209 -30.887 -17.869 1.00 18.30 ?  10   LEU   B CA   1 
ATOM   3906 C  C    . LEU   B 1 10  ? 38.017 -30.126 -17.309 1.00 17.91 ?  10   LEU   B C    1 
ATOM   3907 O  O    . LEU   B 1 10  ? 38.023 -29.716 -16.145 1.00 17.47 ?  10   LEU   B O    1 
ATOM   3908 C  CB   . LEU   B 1 10  ? 39.324 -32.255 -17.198 1.00 18.99 ?  10   LEU   B CB   1 
ATOM   3909 C  CG   . LEU   B 1 10  ? 38.209 -33.230 -17.558 1.00 20.48 ?  10   LEU   B CG   1 
ATOM   3910 C  CD1  . LEU   B 1 10  ? 38.398 -33.765 -18.972 1.00 21.52 ?  10   LEU   B CD1  1 
ATOM   3911 C  CD2  . LEU   B 1 10  ? 38.124 -34.361 -16.546 1.00 21.75 ?  10   LEU   B CD2  1 
ATOM   3912 H  H    . LEU   B 1 10  ? 40.729 -30.269 -16.807 1.00 22.04 ?  10   LEU   B H    1 
ATOM   3913 H  HA   . LEU   B 1 10  ? 39.093 -31.012 -18.821 1.00 21.96 ?  10   LEU   B HA   1 
ATOM   3914 H  HB2  . LEU   B 1 10  ? 40.167 -32.664 -17.458 1.00 22.78 ?  10   LEU   B HB2  1 
ATOM   3915 H  HB3  . LEU   B 1 10  ? 39.309 -32.137 -16.232 1.00 22.78 ?  10   LEU   B HB3  1 
ATOM   3916 H  HG   . LEU   B 1 10  ? 37.365 -32.757 -17.536 1.00 24.57 ?  10   LEU   B HG   1 
ATOM   3917 H  HD11 . LEU   B 1 10  ? 37.704 -34.415 -19.156 1.00 25.82 ?  10   LEU   B HD11 1 
ATOM   3918 H  HD12 . LEU   B 1 10  ? 38.335 -33.025 -19.596 1.00 25.82 ?  10   LEU   B HD12 1 
ATOM   3919 H  HD13 . LEU   B 1 10  ? 39.271 -34.181 -19.036 1.00 25.82 ?  10   LEU   B HD13 1 
ATOM   3920 H  HD21 . LEU   B 1 10  ? 37.408 -34.961 -16.809 1.00 26.09 ?  10   LEU   B HD21 1 
ATOM   3921 H  HD22 . LEU   B 1 10  ? 38.967 -34.833 -16.529 1.00 26.09 ?  10   LEU   B HD22 1 
ATOM   3922 H  HD23 . LEU   B 1 10  ? 37.933 -33.983 -15.672 1.00 26.09 ?  10   LEU   B HD23 1 
ATOM   3923 N  N    . LYS   B 1 11  ? 36.995 -29.950 -18.135 1.00 19.20 ?  11   LYS   B N    1 
ATOM   3924 C  CA   . LYS   B 1 11  ? 35.795 -29.243 -17.722 1.00 21.04 ?  11   LYS   B CA   1 
ATOM   3925 C  C    . LYS   B 1 11  ? 34.928 -30.171 -16.878 1.00 20.34 ?  11   LYS   B C    1 
ATOM   3926 O  O    . LYS   B 1 11  ? 34.558 -31.262 -17.327 1.00 22.19 ?  11   LYS   B O    1 
ATOM   3927 C  CB   . LYS   B 1 11  ? 35.038 -28.783 -18.966 1.00 24.74 ?  11   LYS   B CB   1 
ATOM   3928 C  CG   . LYS   B 1 11  ? 33.877 -27.847 -18.699 1.00 28.42 ?  11   LYS   B CG   1 
ATOM   3929 C  CD   . LYS   B 1 11  ? 33.093 -27.588 -19.979 1.00 31.46 ?  11   LYS   B CD   1 
ATOM   3930 C  CE   . LYS   B 1 11  ? 32.087 -26.466 -19.804 1.00 33.70 ?  11   LYS   B CE   1 
ATOM   3931 N  NZ   . LYS   B 1 11  ? 32.757 -25.147 -19.649 1.00 35.03 ?  11   LYS   B NZ   1 
ATOM   3932 H  H    . LYS   B 1 11  ? 36.968 -30.244 -18.943 1.00 23.03 ?  11   LYS   B H    1 
ATOM   3933 H  HA   . LYS   B 1 11  ? 36.036 -28.468 -17.191 1.00 25.24 ?  11   LYS   B HA   1 
ATOM   3934 H  HB2  . LYS   B 1 11  ? 35.659 -28.319 -19.550 1.00 29.68 ?  11   LYS   B HB2  1 
ATOM   3935 H  HB3  . LYS   B 1 11  ? 34.686 -29.563 -19.421 1.00 29.68 ?  11   LYS   B HB3  1 
ATOM   3936 H  HG2  . LYS   B 1 11  ? 33.279 -28.250 -18.051 1.00 34.10 ?  11   LYS   B HG2  1 
ATOM   3937 H  HG3  . LYS   B 1 11  ? 34.214 -27.000 -18.370 1.00 34.10 ?  11   LYS   B HG3  1 
ATOM   3938 H  HD2  . LYS   B 1 11  ? 33.710 -27.337 -20.686 1.00 37.75 ?  11   LYS   B HD2  1 
ATOM   3939 H  HD3  . LYS   B 1 11  ? 32.612 -28.393 -20.227 1.00 37.75 ?  11   LYS   B HD3  1 
ATOM   3940 H  HE2  . LYS   B 1 11  ? 31.513 -26.426 -20.585 1.00 40.44 ?  11   LYS   B HE2  1 
ATOM   3941 H  HE3  . LYS   B 1 11  ? 31.559 -26.638 -19.009 1.00 40.44 ?  11   LYS   B HE3  1 
ATOM   3942 H  HZ1  . LYS   B 1 11  ? 32.147 -24.503 -19.575 1.00 42.03 ?  11   LYS   B HZ1  1 
ATOM   3943 H  HZ2  . LYS   B 1 11  ? 33.268 -25.147 -18.921 1.00 42.03 ?  11   LYS   B HZ2  1 
ATOM   3944 H  HZ3  . LYS   B 1 11  ? 33.267 -24.979 -20.360 1.00 42.03 ?  11   LYS   B HZ3  1 
ATOM   3945 N  N    . LEU   B 1 12  ? 34.601 -29.743 -15.658 1.00 18.79 ?  12   LEU   B N    1 
ATOM   3946 C  CA   . LEU   B 1 12  ? 33.638 -30.444 -14.815 1.00 18.19 ?  12   LEU   B CA   1 
ATOM   3947 C  C    . LEU   B 1 12  ? 32.250 -29.832 -14.908 1.00 17.95 ?  12   LEU   B C    1 
ATOM   3948 O  O    . LEU   B 1 12  ? 31.264 -30.543 -15.092 1.00 18.60 ?  12   LEU   B O    1 
ATOM   3949 C  CB   . LEU   B 1 12  ? 34.094 -30.454 -13.352 1.00 17.59 ?  12   LEU   B CB   1 
ATOM   3950 C  CG   . LEU   B 1 12  ? 35.430 -31.139 -13.079 1.00 17.46 ?  12   LEU   B CG   1 
ATOM   3951 C  CD1  . LEU   B 1 12  ? 35.758 -31.091 -11.596 1.00 17.96 ?  12   LEU   B CD1  1 
ATOM   3952 C  CD2  . LEU   B 1 12  ? 35.415 -32.565 -13.590 1.00 17.88 ?  12   LEU   B CD2  1 
ATOM   3953 H  H    . LEU   B 1 12  ? 34.930 -29.039 -15.293 1.00 22.54 ?  12   LEU   B H    1 
ATOM   3954 H  HA   . LEU   B 1 12  ? 33.567 -31.363 -15.115 1.00 21.82 ?  12   LEU   B HA   1 
ATOM   3955 H  HB2  . LEU   B 1 12  ? 34.164 -29.536 -13.049 1.00 21.10 ?  12   LEU   B HB2  1 
ATOM   3956 H  HB3  . LEU   B 1 12  ? 33.417 -30.914 -12.827 1.00 21.10 ?  12   LEU   B HB3  1 
ATOM   3957 H  HG   . LEU   B 1 12  ? 36.125 -30.655 -13.552 1.00 20.95 ?  12   LEU   B HG   1 
ATOM   3958 H  HD11 . LEU   B 1 12  ? 36.613 -31.527 -11.450 1.00 21.54 ?  12   LEU   B HD11 1 
ATOM   3959 H  HD12 . LEU   B 1 12  ? 35.805 -30.166 -11.309 1.00 21.54 ?  12   LEU   B HD12 1 
ATOM   3960 H  HD13 . LEU   B 1 12  ? 35.062 -31.556 -11.103 1.00 21.54 ?  12   LEU   B HD13 1 
ATOM   3961 H  HD21 . LEU   B 1 12  ? 36.197 -33.027 -13.254 1.00 21.45 ?  12   LEU   B HD21 1 
ATOM   3962 H  HD22 . LEU   B 1 12  ? 34.609 -33.004 -13.276 1.00 21.45 ?  12   LEU   B HD22 1 
ATOM   3963 H  HD23 . LEU   B 1 12  ? 35.428 -32.553 -14.561 1.00 21.45 ?  12   LEU   B HD23 1 
ATOM   3964 N  N    . THR   B 1 13  ? 32.162 -28.517 -14.774 1.00 18.06 ?  13   THR   B N    1 
ATOM   3965 C  CA   . THR   B 1 13  ? 30.935 -27.771 -14.982 1.00 17.97 ?  13   THR   B CA   1 
ATOM   3966 C  C    . THR   B 1 13  ? 31.277 -26.573 -15.859 1.00 19.96 ?  13   THR   B C    1 
ATOM   3967 O  O    . THR   B 1 13  ? 32.428 -26.378 -16.267 1.00 20.90 ?  13   THR   B O    1 
ATOM   3968 C  CB   . THR   B 1 13  ? 30.337 -27.293 -13.654 1.00 18.00 ?  13   THR   B CB   1 
ATOM   3969 O  OG1  . THR   B 1 13  ? 31.177 -26.268 -13.107 1.00 17.69 ?  13   THR   B OG1  1 
ATOM   3970 C  CG2  . THR   B 1 13  ? 30.216 -28.442 -12.660 1.00 18.43 ?  13   THR   B CG2  1 
ATOM   3971 H  H    . THR   B 1 13  ? 32.827 -28.018 -14.556 1.00 21.67 ?  13   THR   B H    1 
ATOM   3972 H  HA   . THR   B 1 13  ? 30.282 -28.327 -15.434 1.00 21.55 ?  13   THR   B HA   1 
ATOM   3973 H  HB   . THR   B 1 13  ? 29.448 -26.930 -13.812 1.00 21.59 ?  13   THR   B HB   1 
ATOM   3974 H  HG1  . THR   B 1 13  ? 30.861 -25.506 -13.290 1.00 21.22 ?  13   THR   B HG1  1 
ATOM   3975 H  HG21 . THR   B 1 13  ? 29.715 -28.157 -11.880 1.00 22.11 ?  13   THR   B HG21 1 
ATOM   3976 H  HG22 . THR   B 1 13  ? 29.755 -29.190 -13.074 1.00 22.11 ?  13   THR   B HG22 1 
ATOM   3977 H  HG23 . THR   B 1 13  ? 31.098 -28.733 -12.380 1.00 22.11 ?  13   THR   B HG23 1 
ATOM   3978 N  N    A ASP   B 1 14  ? 30.264 -25.754 -16.139 0.50 20.95 ?  14   ASP   B N    1 
ATOM   3979 N  N    B ASP   B 1 14  ? 30.265 -25.755 -16.149 0.50 20.90 ?  14   ASP   B N    1 
ATOM   3980 C  CA   A ASP   B 1 14  ? 30.478 -24.593 -16.994 0.50 22.31 ?  14   ASP   B CA   1 
ATOM   3981 C  CA   B ASP   B 1 14  ? 30.481 -24.592 -17.003 0.50 22.17 ?  14   ASP   B CA   1 
ATOM   3982 C  C    A ASP   B 1 14  ? 31.572 -23.682 -16.452 0.50 20.69 ?  14   ASP   B C    1 
ATOM   3983 C  C    B ASP   B 1 14  ? 31.528 -23.639 -16.444 0.50 20.59 ?  14   ASP   B C    1 
ATOM   3984 O  O    A ASP   B 1 14  ? 32.237 -22.988 -17.231 0.50 21.87 ?  14   ASP   B O    1 
ATOM   3985 O  O    B ASP   B 1 14  ? 32.098 -22.853 -17.210 0.50 21.71 ?  14   ASP   B O    1 
ATOM   3986 C  CB   A ASP   B 1 14  ? 29.172 -23.817 -17.163 0.50 25.25 ?  14   ASP   B CB   1 
ATOM   3987 C  CB   B ASP   B 1 14  ? 29.171 -23.833 -17.214 0.50 25.00 ?  14   ASP   B CB   1 
ATOM   3988 C  CG   A ASP   B 1 14  ? 28.188 -24.518 -18.076 0.50 28.09 ?  14   ASP   B CG   1 
ATOM   3989 C  CG   B ASP   B 1 14  ? 28.261 -24.514 -18.216 0.50 27.75 ?  14   ASP   B CG   1 
ATOM   3990 O  OD1  A ASP   B 1 14  ? 28.527 -25.586 -18.634 0.50 28.82 ?  14   ASP   B OD1  1 
ATOM   3991 O  OD1  B ASP   B 1 14  ? 28.778 -25.199 -19.124 0.50 28.49 ?  14   ASP   B OD1  1 
ATOM   3992 O  OD2  A ASP   B 1 14  ? 27.064 -23.997 -18.231 0.50 29.31 -1 14   ASP   B OD2  1 
ATOM   3993 O  OD2  B ASP   B 1 14  ? 27.028 -24.369 -18.094 0.50 28.95 -1 14   ASP   B OD2  1 
ATOM   3994 H  H    A ASP   B 1 14  ? 29.461 -25.841 -15.846 0.50 25.13 ?  14   ASP   B H    1 
ATOM   3995 H  H    B ASP   B 1 14  ? 29.458 -25.847 -15.868 0.50 25.07 ?  14   ASP   B H    1 
ATOM   3996 H  HA   A ASP   B 1 14  ? 30.762 -24.891 -17.869 0.50 26.77 ?  14   ASP   B HA   1 
ATOM   3997 H  HA   B ASP   B 1 14  ? 30.793 -24.892 -17.869 0.50 26.60 ?  14   ASP   B HA   1 
ATOM   3998 H  HB2  A ASP   B 1 14  ? 28.736 -23.730 -16.303 0.50 30.30 ?  14   ASP   B HB2  1 
ATOM   3999 H  HB2  B ASP   B 1 14  ? 28.695 -23.781 -16.372 0.50 30.00 ?  14   ASP   B HB2  1 
ATOM   4000 H  HB3  A ASP   B 1 14  ? 29.365 -22.941 -17.532 0.50 30.30 ?  14   ASP   B HB3  1 
ATOM   4001 H  HB3  B ASP   B 1 14  ? 29.373 -22.938 -17.536 0.50 30.00 ?  14   ASP   B HB3  1 
ATOM   4002 N  N    . ASN   B 1 15  ? 31.785 -23.673 -15.133 1.00 18.38 ?  15   ASN   B N    1 
ATOM   4003 C  CA   . ASN   B 1 15  ? 32.741 -22.753 -14.520 1.00 16.31 ?  15   ASN   B CA   1 
ATOM   4004 C  C    . ASN   B 1 15  ? 33.831 -23.406 -13.681 1.00 14.98 ?  15   ASN   B C    1 
ATOM   4005 O  O    . ASN   B 1 15  ? 34.679 -22.677 -13.152 1.00 15.17 ?  15   ASN   B O    1 
ATOM   4006 C  CB   . ASN   B 1 15  ? 32.020 -21.701 -13.661 1.00 16.45 ?  15   ASN   B CB   1 
ATOM   4007 C  CG   . ASN   B 1 15  ? 31.397 -22.298 -12.419 1.00 15.68 ?  15   ASN   B CG   1 
ATOM   4008 O  OD1  . ASN   B 1 15  ? 30.455 -23.097 -12.503 1.00 17.47 ?  15   ASN   B OD1  1 
ATOM   4009 N  ND2  . ASN   B 1 15  ? 31.915 -21.937 -11.260 1.00 14.95 ?  15   ASN   B ND2  1 
ATOM   4010 H  H    A ASN   B 1 15  ? 31.379 -24.188 -14.572 0.50 22.05 ?  15   ASN   B H    1 
ATOM   4011 H  H    B ASN   B 1 15  ? 31.397 -24.205 -14.575 0.50 22.05 ?  15   ASN   B H    1 
ATOM   4012 H  HA   . ASN   B 1 15  ? 33.189 -22.271 -15.222 1.00 19.57 ?  15   ASN   B HA   1 
ATOM   4013 H  HB2  . ASN   B 1 15  ? 32.664 -21.023 -13.384 1.00 19.74 ?  15   ASN   B HB2  1 
ATOM   4014 H  HB3  . ASN   B 1 15  ? 31.314 -21.285 -14.183 1.00 19.74 ?  15   ASN   B HB3  1 
ATOM   4015 H  HD21 . ASN   B 1 15  ? 31.593 -22.246 -10.524 1.00 17.94 ?  15   ASN   B HD21 1 
ATOM   4016 H  HD22 . ASN   B 1 15  ? 32.578 -21.381 -11.232 1.00 17.94 ?  15   ASN   B HD22 1 
ATOM   4017 N  N    . VAL   B 1 16  ? 33.839 -24.729 -13.529 1.00 14.94 ?  16   VAL   B N    1 
ATOM   4018 C  CA   . VAL   B 1 16  ? 34.839 -25.422 -12.720 1.00 14.64 ?  16   VAL   B CA   1 
ATOM   4019 C  C    . VAL   B 1 16  ? 35.630 -26.357 -13.620 1.00 14.48 ?  16   VAL   B C    1 
ATOM   4020 O  O    . VAL   B 1 16  ? 35.051 -27.239 -14.275 1.00 15.60 ?  16   VAL   B O    1 
ATOM   4021 C  CB   . VAL   B 1 16  ? 34.214 -26.184 -11.542 1.00 14.92 ?  16   VAL   B CB   1 
ATOM   4022 C  CG1  . VAL   B 1 16  ? 35.296 -26.904 -10.746 1.00 15.13 ?  16   VAL   B CG1  1 
ATOM   4023 C  CG2  . VAL   B 1 16  ? 33.416 -25.234 -10.650 1.00 15.35 ?  16   VAL   B CG2  1 
ATOM   4024 H  H    . VAL   B 1 16  ? 33.254 -25.261 -13.881 1.00 17.92 ?  16   VAL   B H    1 
ATOM   4025 H  HA   . VAL   B 1 16  ? 35.452 -24.767 -12.351 1.00 17.56 ?  16   VAL   B HA   1 
ATOM   4026 H  HB   . VAL   B 1 16  ? 33.602 -26.854 -11.885 1.00 17.90 ?  16   VAL   B HB   1 
ATOM   4027 H  HG11 . VAL   B 1 16  ? 34.919 -27.200 -9.901  1.00 18.16 ?  16   VAL   B HG11 1 
ATOM   4028 H  HG12 . VAL   B 1 16  ? 35.613 -27.662 -11.253 1.00 18.16 ?  16   VAL   B HG12 1 
ATOM   4029 H  HG13 . VAL   B 1 16  ? 36.025 -26.283 -10.578 1.00 18.16 ?  16   VAL   B HG13 1 
ATOM   4030 H  HG21 . VAL   B 1 16  ? 33.081 -25.726 -9.882  1.00 18.41 ?  16   VAL   B HG21 1 
ATOM   4031 H  HG22 . VAL   B 1 16  ? 33.994 -24.515 -10.355 1.00 18.41 ?  16   VAL   B HG22 1 
ATOM   4032 H  HG23 . VAL   B 1 16  ? 32.672 -24.873 -11.158 1.00 18.41 ?  16   VAL   B HG23 1 
ATOM   4033 N  N    . TYR   B 1 17  ? 36.952 -26.183 -13.612 1.00 14.79 ?  17   TYR   B N    1 
ATOM   4034 C  CA   . TYR   B 1 17  ? 37.895 -26.930 -14.428 1.00 15.17 ?  17   TYR   B CA   1 
ATOM   4035 C  C    . TYR   B 1 17  ? 38.945 -27.541 -13.513 1.00 14.13 ?  17   TYR   B C    1 
ATOM   4036 O  O    . TYR   B 1 17  ? 39.220 -27.011 -12.433 1.00 14.65 ?  17   TYR   B O    1 
ATOM   4037 C  CB   . TYR   B 1 17  ? 38.611 -25.991 -15.410 1.00 17.91 ?  17   TYR   B CB   1 
ATOM   4038 C  CG   . TYR   B 1 17  ? 37.693 -25.215 -16.318 1.00 21.03 ?  17   TYR   B CG   1 
ATOM   4039 C  CD1  . TYR   B 1 17  ? 37.107 -24.023 -15.904 1.00 22.50 ?  17   TYR   B CD1  1 
ATOM   4040 C  CD2  . TYR   B 1 17  ? 37.403 -25.677 -17.593 1.00 23.24 ?  17   TYR   B CD2  1 
ATOM   4041 C  CE1  . TYR   B 1 17  ? 36.260 -23.312 -16.740 1.00 24.18 ?  17   TYR   B CE1  1 
ATOM   4042 C  CE2  . TYR   B 1 17  ? 36.562 -24.975 -18.436 1.00 24.74 ?  17   TYR   B CE2  1 
ATOM   4043 C  CZ   . TYR   B 1 17  ? 35.992 -23.796 -18.003 1.00 25.18 ?  17   TYR   B CZ   1 
ATOM   4044 O  OH   . TYR   B 1 17  ? 35.156 -23.096 -18.839 1.00 26.41 ?  17   TYR   B OH   1 
ATOM   4045 H  H    . TYR   B 1 17  ? 37.349 -25.597 -13.113 1.00 17.75 ?  17   TYR   B H    1 
ATOM   4046 H  HA   . TYR   B 1 17  ? 37.437 -27.629 -14.923 1.00 18.19 ?  17   TYR   B HA   1 
ATOM   4047 H  HB2  . TYR   B 1 17  ? 39.141 -25.354 -14.909 1.00 21.48 ?  17   TYR   B HB2  1 
ATOM   4048 H  HB3  . TYR   B 1 17  ? 39.185 -26.523 -15.977 1.00 21.48 ?  17   TYR   B HB3  1 
ATOM   4049 H  HD1  . TYR   B 1 17  ? 37.290 -23.697 -15.054 1.00 26.99 ?  17   TYR   B HD1  1 
ATOM   4050 H  HD2  . TYR   B 1 17  ? 37.780 -26.472 -17.890 1.00 27.88 ?  17   TYR   B HD2  1 
ATOM   4051 H  HE1  . TYR   B 1 17  ? 35.876 -22.513 -16.451 1.00 29.02 ?  17   TYR   B HE1  1 
ATOM   4052 H  HE2  . TYR   B 1 17  ? 36.372 -25.298 -19.289 1.00 29.68 ?  17   TYR   B HE2  1 
ATOM   4053 H  HH   . TYR   B 1 17  ? 35.072 -23.496 -19.573 1.00 31.69 ?  17   TYR   B HH   1 
ATOM   4054 N  N    . ILE   B 1 18  ? 39.560 -28.644 -13.951 1.00 14.19 ?  18   ILE   B N    1 
ATOM   4055 C  CA   . ILE   B 1 18  ? 40.493 -29.361 -13.089 1.00 14.02 ?  18   ILE   B CA   1 
ATOM   4056 C  C    . ILE   B 1 18  ? 41.652 -29.913 -13.909 1.00 14.39 ?  18   ILE   B C    1 
ATOM   4057 O  O    . ILE   B 1 18  ? 41.491 -30.303 -15.069 1.00 15.78 ?  18   ILE   B O    1 
ATOM   4058 C  CB   . ILE   B 1 18  ? 39.743 -30.461 -12.296 1.00 14.31 ?  18   ILE   B CB   1 
ATOM   4059 C  CG1  . ILE   B 1 18  ? 40.583 -30.988 -11.132 1.00 15.20 ?  18   ILE   B CG1  1 
ATOM   4060 C  CG2  . ILE   B 1 18  ? 39.264 -31.586 -13.222 1.00 14.97 ?  18   ILE   B CG2  1 
ATOM   4061 C  CD1  . ILE   B 1 18  ? 39.761 -31.810 -10.143 1.00 16.44 ?  18   ILE   B CD1  1 
ATOM   4062 H  H    . ILE   B 1 18  ? 39.462 -28.985 -14.736 1.00 17.02 ?  18   ILE   B H    1 
ATOM   4063 H  HA   . ILE   B 1 18  ? 40.859 -28.738 -12.443 1.00 16.82 ?  18   ILE   B HA   1 
ATOM   4064 H  HB   . ILE   B 1 18  ? 38.949 -30.055 -11.912 1.00 17.17 ?  18   ILE   B HB   1 
ATOM   4065 H  HG12 . ILE   B 1 18  ? 41.289 -31.549 -11.476 1.00 18.23 ?  18   ILE   B HG12 1 
ATOM   4066 H  HG13 . ILE   B 1 18  ? 40.958 -30.232 -10.649 1.00 18.23 ?  18   ILE   B HG13 1 
ATOM   4067 H  HG21 . ILE   B 1 18  ? 38.660 -32.166 -12.728 1.00 17.96 ?  18   ILE   B HG21 1 
ATOM   4068 H  HG22 . ILE   B 1 18  ? 38.798 -31.193 -13.976 1.00 17.96 ?  18   ILE   B HG22 1 
ATOM   4069 H  HG23 . ILE   B 1 18  ? 40.030 -32.091 -13.529 1.00 17.96 ?  18   ILE   B HG23 1 
ATOM   4070 H  HD11 . ILE   B 1 18  ? 40.325 -32.066 -9.398  1.00 19.72 ?  18   ILE   B HD11 1 
ATOM   4071 H  HD12 . ILE   B 1 18  ? 39.016 -31.274 -9.825  1.00 19.72 ?  18   ILE   B HD12 1 
ATOM   4072 H  HD13 . ILE   B 1 18  ? 39.427 -32.602 -10.593 1.00 19.72 ?  18   ILE   B HD13 1 
ATOM   4073 N  N    . LYS   B 1 19  ? 42.833 -29.945 -13.291 1.00 14.87 ?  19   LYS   B N    1 
ATOM   4074 C  CA   . LYS   B 1 19  ? 44.042 -30.422 -13.948 1.00 15.69 ?  19   LYS   B CA   1 
ATOM   4075 C  C    . LYS   B 1 19  ? 44.937 -31.099 -12.922 1.00 15.62 ?  19   LYS   B C    1 
ATOM   4076 O  O    . LYS   B 1 19  ? 45.022 -30.663 -11.772 1.00 15.08 ?  19   LYS   B O    1 
ATOM   4077 C  CB   . LYS   B 1 19  ? 44.811 -29.260 -14.588 1.00 16.96 ?  19   LYS   B CB   1 
ATOM   4078 C  CG   . LYS   B 1 19  ? 46.031 -29.676 -15.392 1.00 18.68 ?  19   LYS   B CG   1 
ATOM   4079 C  CD   . LYS   B 1 19  ? 46.747 -28.453 -15.948 1.00 20.66 ?  19   LYS   B CD   1 
ATOM   4080 C  CE   . LYS   B 1 19  ? 47.933 -28.833 -16.811 1.00 22.68 ?  19   LYS   B CE   1 
ATOM   4081 N  NZ   . LYS   B 1 19  ? 48.652 -27.634 -17.313 1.00 24.00 ?  19   LYS   B NZ   1 
ATOM   4082 H  H    . LYS   B 1 19  ? 42.952 -29.687 -12.477 1.00 17.83 ?  19   LYS   B H    1 
ATOM   4083 H  HA   . LYS   B 1 19  ? 43.803 -31.063 -14.638 1.00 18.82 ?  19   LYS   B HA   1 
ATOM   4084 H  HB2  . LYS   B 1 19  ? 44.211 -28.789 -15.187 1.00 20.35 ?  19   LYS   B HB2  1 
ATOM   4085 H  HB3  . LYS   B 1 19  ? 45.105 -28.662 -13.883 1.00 20.35 ?  19   LYS   B HB3  1 
ATOM   4086 H  HG2  . LYS   B 1 19  ? 46.645 -30.162 -14.820 1.00 22.41 ?  19   LYS   B HG2  1 
ATOM   4087 H  HG3  . LYS   B 1 19  ? 45.748 -30.235 -16.135 1.00 22.41 ?  19   LYS   B HG3  1 
ATOM   4088 H  HD2  . LYS   B 1 19  ? 46.127 -27.939 -16.490 1.00 24.78 ?  19   LYS   B HD2  1 
ATOM   4089 H  HD3  . LYS   B 1 19  ? 47.070 -27.912 -15.209 1.00 24.78 ?  19   LYS   B HD3  1 
ATOM   4090 H  HE2  . LYS   B 1 19  ? 48.552 -29.365 -16.287 1.00 27.20 ?  19   LYS   B HE2  1 
ATOM   4091 H  HE3  . LYS   B 1 19  ? 47.618 -29.343 -17.576 1.00 27.20 ?  19   LYS   B HE3  1 
ATOM   4092 H  HZ1  . LYS   B 1 19  ? 49.291 -27.878 -17.882 1.00 28.79 ?  19   LYS   B HZ1  1 
ATOM   4093 H  HZ2  . LYS   B 1 19  ? 48.084 -27.091 -17.732 1.00 28.79 ?  19   LYS   B HZ2  1 
ATOM   4094 H  HZ3  . LYS   B 1 19  ? 49.022 -27.194 -16.634 1.00 28.79 ?  19   LYS   B HZ3  1 
ATOM   4095 N  N    . ASN   B 1 20  ? 45.624 -32.152 -13.353 1.00 16.78 ?  20   ASN   B N    1 
ATOM   4096 C  CA   . ASN   B 1 20  ? 46.653 -32.781 -12.533 1.00 17.92 ?  20   ASN   B CA   1 
ATOM   4097 C  C    . ASN   B 1 20  ? 47.929 -31.970 -12.714 1.00 18.30 ?  20   ASN   B C    1 
ATOM   4098 O  O    . ASN   B 1 20  ? 48.573 -32.042 -13.768 1.00 20.08 ?  20   ASN   B O    1 
ATOM   4099 C  CB   . ASN   B 1 20  ? 46.825 -34.236 -12.968 1.00 19.45 ?  20   ASN   B CB   1 
ATOM   4100 C  CG   . ASN   B 1 20  ? 47.984 -34.941 -12.278 1.00 21.13 ?  20   ASN   B CG   1 
ATOM   4101 O  OD1  . ASN   B 1 20  ? 48.640 -35.803 -12.876 1.00 23.46 ?  20   ASN   B OD1  1 
ATOM   4102 N  ND2  . ASN   B 1 20  ? 48.232 -34.601 -11.023 1.00 20.77 ?  20   ASN   B ND2  1 
ATOM   4103 H  H    . ASN   B 1 20  ? 45.521 -32.511 -14.126 1.00 20.13 ?  20   ASN   B H    1 
ATOM   4104 H  HA   . ASN   B 1 20  ? 46.379 -32.760 -11.602 1.00 21.50 ?  20   ASN   B HA   1 
ATOM   4105 H  HB2  . ASN   B 1 20  ? 46.012 -34.726 -12.757 1.00 23.33 ?  20   ASN   B HB2  1 
ATOM   4106 H  HB3  . ASN   B 1 20  ? 46.983 -34.259 -13.923 1.00 23.33 ?  20   ASN   B HB3  1 
ATOM   4107 H  HD21 . ASN   B 1 20  ? 48.881 -34.967 -10.601 1.00 24.92 ?  20   ASN   B HD21 1 
ATOM   4108 H  HD22 . ASN   B 1 20  ? 47.753 -33.998 -10.631 1.00 24.92 ?  20   ASN   B HD22 1 
ATOM   4109 N  N    . ALA   B 1 21  ? 48.286 -31.178 -11.702 1.00 17.86 ?  21   ALA   B N    1 
ATOM   4110 C  CA   . ALA   B 1 21  ? 49.391 -30.245 -11.858 1.00 18.64 ?  21   ALA   B CA   1 
ATOM   4111 C  C    . ALA   B 1 21  ? 49.851 -29.745 -10.497 1.00 17.56 ?  21   ALA   B C    1 
ATOM   4112 O  O    . ALA   B 1 21  ? 49.108 -29.775 -9.511  1.00 17.21 ?  21   ALA   B O    1 
ATOM   4113 C  CB   . ALA   B 1 21  ? 48.982 -29.078 -12.753 1.00 19.82 ?  21   ALA   B CB   1 
ATOM   4114 H  H    . ALA   B 1 21  ? 47.909 -31.173 -10.926 1.00 21.42 ?  21   ALA   B H    1 
ATOM   4115 H  HA   . ALA   B 1 21  ? 50.133 -30.710 -12.275 1.00 22.36 ?  21   ALA   B HA   1 
ATOM   4116 H  HB1  . ALA   B 1 21  ? 49.765 -28.548 -12.933 1.00 23.78 ?  21   ALA   B HB1  1 
ATOM   4117 H  HB2  . ALA   B 1 21  ? 48.622 -29.438 -13.579 1.00 23.78 ?  21   ALA   B HB2  1 
ATOM   4118 H  HB3  . ALA   B 1 21  ? 48.306 -28.557 -12.297 1.00 23.78 ?  21   ALA   B HB3  1 
ATOM   4119 N  N    . ASP   B 1 22  ? 51.110 -29.306 -10.476 1.00 16.72 ?  22   ASP   B N    1 
ATOM   4120 C  CA   . ASP   B 1 22  ? 51.723 -28.617 -9.347  1.00 15.97 ?  22   ASP   B CA   1 
ATOM   4121 C  C    . ASP   B 1 22  ? 51.317 -27.147 -9.432  1.00 14.89 ?  22   ASP   B C    1 
ATOM   4122 O  O    . ASP   B 1 22  ? 51.624 -26.474 -10.421 1.00 15.32 ?  22   ASP   B O    1 
ATOM   4123 C  CB   . ASP   B 1 22  ? 53.240 -28.802 -9.493  1.00 17.43 ?  22   ASP   B CB   1 
ATOM   4124 C  CG   . ASP   B 1 22  ? 54.062 -28.038 -8.464  1.00 19.05 ?  22   ASP   B CG   1 
ATOM   4125 O  OD1  . ASP   B 1 22  ? 53.699 -26.915 -8.080  1.00 19.39 ?  22   ASP   B OD1  1 
ATOM   4126 O  OD2  . ASP   B 1 22  ? 55.127 -28.559 -8.066  1.00 21.25 -1 22   ASP   B OD2  1 
ATOM   4127 H  H    . ASP   B 1 22  ? 51.654 -29.407 -11.138 1.00 20.06 ?  22   ASP   B H    1 
ATOM   4128 H  HA   . ASP   B 1 22  ? 51.427 -29.004 -8.503  1.00 19.15 ?  22   ASP   B HA   1 
ATOM   4129 H  HB2  . ASP   B 1 22  ? 53.458 -29.741 -9.404  1.00 20.92 ?  22   ASP   B HB2  1 
ATOM   4130 H  HB3  . ASP   B 1 22  ? 53.510 -28.480 -10.367 1.00 20.92 ?  22   ASP   B HB3  1 
ATOM   4131 N  N    . ILE   B 1 23  ? 50.608 -26.652 -8.410  1.00 14.36 ?  23   ILE   B N    1 
ATOM   4132 C  CA   . ILE   B 1 23  ? 50.011 -25.317 -8.489  1.00 13.55 ?  23   ILE   B CA   1 
ATOM   4133 C  C    . ILE   B 1 23  ? 51.064 -24.227 -8.615  1.00 13.25 ?  23   ILE   B C    1 
ATOM   4134 O  O    . ILE   B 1 23  ? 50.798 -23.181 -9.210  1.00 13.10 ?  23   ILE   B O    1 
ATOM   4135 C  CB   . ILE   B 1 23  ? 49.064 -25.078 -7.299  1.00 13.87 ?  23   ILE   B CB   1 
ATOM   4136 C  CG1  . ILE   B 1 23  ? 48.243 -23.802 -7.498  1.00 14.58 ?  23   ILE   B CG1  1 
ATOM   4137 C  CG2  . ILE   B 1 23  ? 49.830 -25.044 -5.994  1.00 15.00 ?  23   ILE   B CG2  1 
ATOM   4138 C  CD1  . ILE   B 1 23  ? 47.134 -23.631 -6.470  1.00 15.41 ?  23   ILE   B CD1  1 
ATOM   4139 H  H    . ILE   B 1 23  ? 50.467 -27.066 -7.671  1.00 17.22 ?  23   ILE   B H    1 
ATOM   4140 H  HA   . ILE   B 1 23  ? 49.473 -25.282 -9.293  1.00 16.25 ?  23   ILE   B HA   1 
ATOM   4141 H  HB   . ILE   B 1 23  ? 48.444 -25.826 -7.264  1.00 16.64 ?  23   ILE   B HB   1 
ATOM   4142 H  HG12 . ILE   B 1 23  ? 48.838 -23.035 -7.428  1.00 17.49 ?  23   ILE   B HG12 1 
ATOM   4143 H  HG13 . ILE   B 1 23  ? 47.839 -23.820 -8.381  1.00 17.49 ?  23   ILE   B HG13 1 
ATOM   4144 H  HG21 . ILE   B 1 23  ? 49.198 -25.056 -5.260  1.00 17.99 ?  23   ILE   B HG21 1 
ATOM   4145 H  HG22 . ILE   B 1 23  ? 50.407 -25.822 -5.946  1.00 17.99 ?  23   ILE   B HG22 1 
ATOM   4146 H  HG23 . ILE   B 1 23  ? 50.361 -24.235 -5.963  1.00 17.99 ?  23   ILE   B HG23 1 
ATOM   4147 H  HD11 . ILE   B 1 23  ? 46.602 -22.858 -6.708  1.00 18.49 ?  23   ILE   B HD11 1 
ATOM   4148 H  HD12 . ILE   B 1 23  ? 46.581 -24.429 -6.475  1.00 18.49 ?  23   ILE   B HD12 1 
ATOM   4149 H  HD13 . ILE   B 1 23  ? 47.531 -23.508 -5.595  1.00 18.49 ?  23   ILE   B HD13 1 
ATOM   4150 N  N    . VAL   B 1 24  ? 52.257 -24.432 -8.052  1.00 13.68 ?  24   VAL   B N    1 
ATOM   4151 C  CA   . VAL   B 1 24  ? 53.335 -23.454 -8.214  1.00 14.18 ?  24   VAL   B CA   1 
ATOM   4152 C  C    . VAL   B 1 24  ? 53.788 -23.401 -9.666  1.00 14.48 ?  24   VAL   B C    1 
ATOM   4153 O  O    . VAL   B 1 24  ? 53.922 -22.320 -10.259 1.00 14.42 ?  24   VAL   B O    1 
ATOM   4154 C  CB   . VAL   B 1 24  ? 54.509 -23.778 -7.270  1.00 14.88 ?  24   VAL   B CB   1 
ATOM   4155 C  CG1  . VAL   B 1 24  ? 55.716 -22.885 -7.580  1.00 15.52 ?  24   VAL   B CG1  1 
ATOM   4156 C  CG2  . VAL   B 1 24  ? 54.088 -23.617 -5.834  1.00 15.96 ?  24   VAL   B CG2  1 
ATOM   4157 H  H    . VAL   B 1 24  ? 52.464 -25.114 -7.575  1.00 16.41 ?  24   VAL   B H    1 
ATOM   4158 H  HA   . VAL   B 1 24  ? 52.999 -22.577 -7.977  1.00 17.01 ?  24   VAL   B HA   1 
ATOM   4159 H  HB   . VAL   B 1 24  ? 54.778 -24.700 -7.399  1.00 17.85 ?  24   VAL   B HB   1 
ATOM   4160 H  HG11 . VAL   B 1 24  ? 56.306 -22.873 -6.810  1.00 18.61 ?  24   VAL   B HG11 1 
ATOM   4161 H  HG12 . VAL   B 1 24  ? 56.184 -23.245 -8.348  1.00 18.61 ?  24   VAL   B HG12 1 
ATOM   4162 H  HG13 . VAL   B 1 24  ? 55.404 -21.985 -7.770  1.00 18.61 ?  24   VAL   B HG13 1 
ATOM   4163 H  HG21 . VAL   B 1 24  ? 54.815 -23.895 -5.256  1.00 19.14 ?  24   VAL   B HG21 1 
ATOM   4164 H  HG22 . VAL   B 1 24  ? 53.873 -22.685 -5.671  1.00 19.14 ?  24   VAL   B HG22 1 
ATOM   4165 H  HG23 . VAL   B 1 24  ? 53.306 -24.170 -5.669  1.00 19.14 ?  24   VAL   B HG23 1 
ATOM   4166 N  N    . GLU   B 1 25  ? 54.052 -24.571 -10.257 1.00 15.39 ?  25   GLU   B N    1 
ATOM   4167 C  CA   . GLU   B 1 25  ? 54.444 -24.604 -11.660 1.00 16.94 ?  25   GLU   B CA   1 
ATOM   4168 C  C    . GLU   B 1 25  ? 53.335 -24.060 -12.546 1.00 15.69 ?  25   GLU   B C    1 
ATOM   4169 O  O    . GLU   B 1 25  ? 53.603 -23.343 -13.520 1.00 16.31 ?  25   GLU   B O    1 
ATOM   4170 C  CB   . GLU   B 1 25  ? 54.844 -26.023 -12.057 1.00 21.04 ?  25   GLU   B CB   1 
ATOM   4171 C  CG   . GLU   B 1 25  ? 56.142 -26.467 -11.398 1.00 26.48 ?  25   GLU   B CG   1 
ATOM   4172 C  CD   . GLU   B 1 25  ? 57.250 -25.421 -11.488 1.00 31.38 ?  25   GLU   B CD   1 
ATOM   4173 O  OE1  . GLU   B 1 25  ? 57.610 -25.021 -12.616 1.00 33.02 ?  25   GLU   B OE1  1 
ATOM   4174 O  OE2  . GLU   B 1 25  ? 57.752 -24.983 -10.426 1.00 32.99 -1 25   GLU   B OE2  1 
ATOM   4175 H  H    . GLU   B 1 25  ? 54.008 -25.340 -9.872  1.00 18.46 ?  25   GLU   B H    1 
ATOM   4176 H  HA   . GLU   B 1 25  ? 55.199 -24.016 -11.783 1.00 20.32 ?  25   GLU   B HA   1 
ATOM   4177 H  HB2  . GLU   B 1 25  ? 54.145 -26.641 -11.783 1.00 25.24 ?  25   GLU   B HB2  1 
ATOM   4178 H  HB3  . GLU   B 1 25  ? 54.962 -26.063 -13.019 1.00 25.24 ?  25   GLU   B HB3  1 
ATOM   4179 H  HG2  . GLU   B 1 25  ? 55.984 -26.626 -10.460 1.00 31.77 ?  25   GLU   B HG2  1 
ATOM   4180 H  HG3  . GLU   B 1 25  ? 56.457 -27.273 -11.833 1.00 31.77 ?  25   GLU   B HG3  1 
ATOM   4181 N  N    A GLU   B 1 26  ? 52.082 -24.372 -12.214 0.50 14.78 ?  26   GLU   B N    1 
ATOM   4182 N  N    B GLU   B 1 26  ? 52.080 -24.381 -12.216 0.50 15.19 ?  26   GLU   B N    1 
ATOM   4183 C  CA   A GLU   B 1 26  ? 50.958 -23.845 -12.981 0.50 15.07 ?  26   GLU   B CA   1 
ATOM   4184 C  CA   B GLU   B 1 26  ? 50.948 -23.855 -12.972 0.50 15.84 ?  26   GLU   B CA   1 
ATOM   4185 C  C    A GLU   B 1 26  ? 50.906 -22.329 -12.896 0.50 14.61 ?  26   GLU   B C    1 
ATOM   4186 C  C    B GLU   B 1 26  ? 50.902 -22.336 -12.895 0.50 14.93 ?  26   GLU   B C    1 
ATOM   4187 O  O    A GLU   B 1 26  ? 50.717 -21.647 -13.909 0.50 15.43 ?  26   GLU   B O    1 
ATOM   4188 O  O    B GLU   B 1 26  ? 50.714 -21.658 -13.910 0.50 15.66 ?  26   GLU   B O    1 
ATOM   4189 C  CB   A GLU   B 1 26  ? 49.647 -24.438 -12.467 0.50 16.07 ?  26   GLU   B CB   1 
ATOM   4190 C  CB   B GLU   B 1 26  ? 49.635 -24.440 -12.439 0.50 17.53 ?  26   GLU   B CB   1 
ATOM   4191 C  CG   A GLU   B 1 26  ? 49.346 -25.806 -13.014 0.50 17.54 ?  26   GLU   B CG   1 
ATOM   4192 C  CG   B GLU   B 1 26  ? 49.101 -25.639 -13.205 0.50 19.76 ?  26   GLU   B CG   1 
ATOM   4193 C  CD   A GLU   B 1 26  ? 49.176 -25.810 -14.522 0.50 17.84 ?  26   GLU   B CD   1 
ATOM   4194 C  CD   B GLU   B 1 26  ? 48.778 -25.320 -14.658 0.50 20.31 ?  26   GLU   B CD   1 
ATOM   4195 O  OE1  A GLU   B 1 26  ? 48.339 -25.035 -15.037 0.50 17.47 ?  26   GLU   B OE1  1 
ATOM   4196 O  OE1  B GLU   B 1 26  ? 47.720 -24.713 -14.942 0.50 21.17 ?  26   GLU   B OE1  1 
ATOM   4197 O  OE2  A GLU   B 1 26  ? 49.881 -26.587 -15.190 0.50 18.99 -1 26   GLU   B OE2  1 
ATOM   4198 O  OE2  B GLU   B 1 26  ? 49.594 -25.687 -15.520 0.50 19.80 -1 26   GLU   B OE2  1 
ATOM   4199 H  H    A GLU   B 1 26  ? 51.855 -24.885 -11.557 0.50 17.73 ?  26   GLU   B H    1 
ATOM   4200 H  H    B GLU   B 1 26  ? 51.859 -24.900 -11.563 0.50 18.22 ?  26   GLU   B H    1 
ATOM   4201 H  HA   A GLU   B 1 26  ? 51.062 -24.091 -13.910 0.50 18.08 ?  26   GLU   B HA   1 
ATOM   4202 H  HA   B GLU   B 1 26  ? 51.039 -24.108 -13.901 0.50 19.00 ?  26   GLU   B HA   1 
ATOM   4203 H  HB2  A GLU   B 1 26  ? 49.690 -24.510 -11.499 0.50 19.27 ?  26   GLU   B HB2  1 
ATOM   4204 H  HB2  B GLU   B 1 26  ? 49.768 -24.719 -11.521 0.50 21.03 ?  26   GLU   B HB2  1 
ATOM   4205 H  HB3  A GLU   B 1 26  ? 48.915 -23.850 -12.717 0.50 19.27 ?  26   GLU   B HB3  1 
ATOM   4206 H  HB3  B GLU   B 1 26  ? 48.953 -23.750 -12.472 0.50 21.03 ?  26   GLU   B HB3  1 
ATOM   4207 H  HG2  A GLU   B 1 26  ? 50.080 -26.389 -12.791 0.50 21.04 ?  26   GLU   B HG2  1 
ATOM   4208 H  HG2  B GLU   B 1 26  ? 49.767 -26.343 -13.185 0.50 23.71 ?  26   GLU   B HG2  1 
ATOM   4209 H  HG3  A GLU   B 1 26  ? 48.522 -26.125 -12.617 0.50 21.04 ?  26   GLU   B HG3  1 
ATOM   4210 H  HG3  B GLU   B 1 26  ? 48.282 -25.945 -12.785 0.50 23.71 ?  26   GLU   B HG3  1 
ATOM   4211 N  N    . ALA   B 1 27  ? 51.050 -21.785 -11.688 1.00 13.79 ?  27   ALA   B N    1 
ATOM   4212 C  CA   . ALA   B 1 27  ? 51.016 -20.336 -11.534 1.00 14.17 ?  27   ALA   B CA   1 
ATOM   4213 C  C    . ALA   B 1 27  ? 52.088 -19.670 -12.385 1.00 15.12 ?  27   ALA   B C    1 
ATOM   4214 O  O    . ALA   B 1 27  ? 51.826 -18.666 -13.061 1.00 15.94 ?  27   ALA   B O    1 
ATOM   4215 C  CB   . ALA   B 1 27  ? 51.158 -19.961 -10.059 1.00 14.45 ?  27   ALA   B CB   1 
ATOM   4216 H  H    A ALA   B 1 27  ? 51.163 -22.225 -10.956 0.50 16.54 ?  27   ALA   B H    1 
ATOM   4217 H  H    B ALA   B 1 27  ? 51.167 -22.223 -10.955 0.50 16.54 ?  27   ALA   B H    1 
ATOM   4218 H  HA   . ALA   B 1 27  ? 50.156 -20.007 -11.835 1.00 16.99 ?  27   ALA   B HA   1 
ATOM   4219 H  HB1  . ALA   B 1 27  ? 51.129 -18.995 -9.971  1.00 17.33 ?  27   ALA   B HB1  1 
ATOM   4220 H  HB2  . ALA   B 1 27  ? 50.423 -20.358 -9.560  1.00 17.33 ?  27   ALA   B HB2  1 
ATOM   4221 H  HB3  . ALA   B 1 27  ? 52.002 -20.299 -9.724  1.00 17.33 ?  27   ALA   B HB3  1 
ATOM   4222 N  N    . LYS   B 1 28  ? 53.299 -20.225 -12.386 1.00 16.30 ?  28   LYS   B N    1 
ATOM   4223 C  CA   . LYS   B 1 28  ? 54.374 -19.609 -13.151 1.00 18.44 ?  28   LYS   B CA   1 
ATOM   4224 C  C    . LYS   B 1 28  ? 54.120 -19.688 -14.650 1.00 19.23 ?  28   LYS   B C    1 
ATOM   4225 O  O    . LYS   B 1 28  ? 54.535 -18.790 -15.393 1.00 20.37 ?  28   LYS   B O    1 
ATOM   4226 C  CB   . LYS   B 1 28  ? 55.728 -20.210 -12.759 1.00 21.29 ?  28   LYS   B CB   1 
ATOM   4227 C  CG   . LYS   B 1 28  ? 56.128 -19.867 -11.323 1.00 24.36 ?  28   LYS   B CG   1 
ATOM   4228 C  CD   . LYS   B 1 28  ? 57.566 -20.248 -10.992 1.00 28.16 ?  28   LYS   B CD   1 
ATOM   4229 C  CE   . LYS   B 1 28  ? 57.675 -21.692 -10.571 1.00 30.94 ?  28   LYS   B CE   1 
ATOM   4230 N  NZ   . LYS   B 1 28  ? 59.037 -22.006 -10.052 1.00 32.06 ?  28   LYS   B NZ   1 
ATOM   4231 H  H    . LYS   B 1 28  ? 53.519 -20.937 -11.959 1.00 19.56 ?  28   LYS   B H    1 
ATOM   4232 H  HA   . LYS   B 1 28  ? 54.409 -18.668 -12.928 1.00 22.12 ?  28   LYS   B HA   1 
ATOM   4233 H  HB2  . LYS   B 1 28  ? 55.686 -21.175 -12.832 1.00 25.54 ?  28   LYS   B HB2  1 
ATOM   4234 H  HB3  . LYS   B 1 28  ? 56.417 -19.862 -13.350 1.00 25.54 ?  28   LYS   B HB3  1 
ATOM   4235 H  HG2  . LYS   B 1 28  ? 56.033 -18.907 -11.196 1.00 29.22 ?  28   LYS   B HG2  1 
ATOM   4236 H  HG3  . LYS   B 1 28  ? 55.541 -20.339 -10.715 1.00 29.22 ?  28   LYS   B HG3  1 
ATOM   4237 H  HD2  . LYS   B 1 28  ? 58.118 -20.113 -11.777 1.00 33.79 ?  28   LYS   B HD2  1 
ATOM   4238 H  HD3  . LYS   B 1 28  ? 57.878 -19.690 -10.262 1.00 33.79 ?  28   LYS   B HD3  1 
ATOM   4239 H  HE2  . LYS   B 1 28  ? 57.033 -21.869 -9.865  1.00 37.12 ?  28   LYS   B HE2  1 
ATOM   4240 H  HE3  . LYS   B 1 28  ? 57.500 -22.265 -11.334 1.00 37.12 ?  28   LYS   B HE3  1 
ATOM   4241 H  HZ1  . LYS   B 1 28  ? 59.082 -22.861 -9.809  1.00 38.47 ?  28   LYS   B HZ1  1 
ATOM   4242 H  HZ2  . LYS   B 1 28  ? 59.646 -21.853 -10.684 1.00 38.47 ?  28   LYS   B HZ2  1 
ATOM   4243 H  HZ3  . LYS   B 1 28  ? 59.220 -21.495 -9.346  1.00 38.47 ?  28   LYS   B HZ3  1 
ATOM   4244 N  N    . LYS   B 1 29  ? 53.418 -20.722 -15.111 1.00 20.36 ?  29   LYS   B N    1 
ATOM   4245 C  CA   . LYS   B 1 29  ? 53.130 -20.855 -16.535 1.00 23.12 ?  29   LYS   B CA   1 
ATOM   4246 C  C    . LYS   B 1 29  ? 51.884 -20.085 -16.961 1.00 22.18 ?  29   LYS   B C    1 
ATOM   4247 O  O    . LYS   B 1 29  ? 51.886 -19.456 -18.025 1.00 23.40 ?  29   LYS   B O    1 
ATOM   4248 C  CB   . LYS   B 1 29  ? 52.982 -22.333 -16.904 1.00 27.46 ?  29   LYS   B CB   1 
ATOM   4249 C  CG   . LYS   B 1 29  ? 52.850 -22.594 -18.394 1.00 31.57 ?  29   LYS   B CG   1 
ATOM   4250 C  CD   . LYS   B 1 29  ? 53.092 -24.063 -18.723 1.00 34.81 ?  29   LYS   B CD   1 
ATOM   4251 C  CE   . LYS   B 1 29  ? 52.038 -24.969 -18.102 1.00 37.02 ?  29   LYS   B CE   1 
ATOM   4252 N  NZ   . LYS   B 1 29  ? 52.260 -26.402 -18.452 1.00 38.31 ?  29   LYS   B NZ   1 
ATOM   4253 H  H    . LYS   B 1 29  ? 53.095 -21.360 -14.619 1.00 24.42 ?  29   LYS   B H    1 
ATOM   4254 H  HA   . LYS   B 1 29  ? 53.878 -20.499 -17.033 1.00 27.73 ?  29   LYS   B HA   1 
ATOM   4255 H  HB2  . LYS   B 1 29  ? 53.768 -22.810 -16.593 1.00 32.94 ?  29   LYS   B HB2  1 
ATOM   4256 H  HB3  . LYS   B 1 29  ? 52.191 -22.686 -16.474 1.00 32.94 ?  29   LYS   B HB3  1 
ATOM   4257 H  HG2  . LYS   B 1 29  ? 51.954 -22.361 -18.681 1.00 37.88 ?  29   LYS   B HG2  1 
ATOM   4258 H  HG3  . LYS   B 1 29  ? 53.506 -22.063 -18.873 1.00 37.88 ?  29   LYS   B HG3  1 
ATOM   4259 H  HD2  . LYS   B 1 29  ? 53.066 -24.182 -19.685 1.00 41.76 ?  29   LYS   B HD2  1 
ATOM   4260 H  HD3  . LYS   B 1 29  ? 53.960 -24.328 -18.378 1.00 41.76 ?  29   LYS   B HD3  1 
ATOM   4261 H  HE2  . LYS   B 1 29  ? 52.071 -24.887 -17.136 1.00 44.42 ?  29   LYS   B HE2  1 
ATOM   4262 H  HE3  . LYS   B 1 29  ? 51.162 -24.710 -18.429 1.00 44.42 ?  29   LYS   B HE3  1 
ATOM   4263 H  HZ1  . LYS   B 1 29  ? 51.631 -26.909 -18.077 1.00 45.96 ?  29   LYS   B HZ1  1 
ATOM   4264 H  HZ2  . LYS   B 1 29  ? 52.228 -26.509 -19.335 1.00 45.96 ?  29   LYS   B HZ2  1 
ATOM   4265 H  HZ3  . LYS   B 1 29  ? 53.057 -26.667 -18.157 1.00 45.96 ?  29   LYS   B HZ3  1 
ATOM   4266 N  N    . VAL   B 1 30  ? 50.820 -20.132 -16.153 1.00 20.39 ?  30   VAL   B N    1 
ATOM   4267 C  CA   . VAL   B 1 30  ? 49.533 -19.543 -16.527 1.00 20.53 ?  30   VAL   B CA   1 
ATOM   4268 C  C    . VAL   B 1 30  ? 49.536 -18.030 -16.371 1.00 19.59 ?  30   VAL   B C    1 
ATOM   4269 O  O    . VAL   B 1 30  ? 48.799 -17.321 -17.073 1.00 20.26 ?  30   VAL   B O    1 
ATOM   4270 C  CB   . VAL   B 1 30  ? 48.425 -20.165 -15.656 1.00 21.58 ?  30   VAL   B CB   1 
ATOM   4271 C  CG1  . VAL   B 1 30  ? 47.137 -19.359 -15.747 1.00 22.07 ?  30   VAL   B CG1  1 
ATOM   4272 C  CG2  . VAL   B 1 30  ? 48.197 -21.620 -16.041 1.00 22.25 ?  30   VAL   B CG2  1 
ATOM   4273 H  H    . VAL   B 1 30  ? 50.814 -20.521 -15.375 1.00 24.46 ?  30   VAL   B H    1 
ATOM   4274 H  HA   . VAL   B 1 30  ? 49.343 -19.771 -17.451 1.00 24.63 ?  30   VAL   B HA   1 
ATOM   4275 H  HB   . VAL   B 1 30  ? 48.710 -20.158 -14.728 1.00 25.89 ?  30   VAL   B HB   1 
ATOM   4276 H  HG11 . VAL   B 1 30  ? 46.392 -19.942 -15.530 1.00 26.48 ?  30   VAL   B HG11 1 
ATOM   4277 H  HG12 . VAL   B 1 30  ? 47.173 -18.627 -15.115 1.00 26.48 ?  30   VAL   B HG12 1 
ATOM   4278 H  HG13 . VAL   B 1 30  ? 47.032 -19.028 -16.648 1.00 26.48 ?  30   VAL   B HG13 1 
ATOM   4279 H  HG21 . VAL   B 1 30  ? 47.501 -21.995 -15.474 1.00 26.70 ?  30   VAL   B HG21 1 
ATOM   4280 H  HG22 . VAL   B 1 30  ? 47.918 -21.660 -16.970 1.00 26.70 ?  30   VAL   B HG22 1 
ATOM   4281 H  HG23 . VAL   B 1 30  ? 49.021 -22.112 -15.920 1.00 26.70 ?  30   VAL   B HG23 1 
ATOM   4282 N  N    . LYS   B 1 31  ? 50.312 -17.529 -15.426 1.00 19.27 ?  31   LYS   B N    1 
ATOM   4283 C  CA   . LYS   B 1 31  ? 50.344 -16.121 -15.070 1.00 19.77 ?  31   LYS   B CA   1 
ATOM   4284 C  C    . LYS   B 1 31  ? 48.945 -15.658 -14.676 1.00 17.52 ?  31   LYS   B C    1 
ATOM   4285 O  O    . LYS   B 1 31  ? 48.395 -14.745 -15.302 1.00 18.31 ?  31   LYS   B O    1 
ATOM   4286 C  CB   . LYS   B 1 31  ? 50.967 -15.305 -16.211 1.00 22.70 ?  31   LYS   B CB   1 
ATOM   4287 C  CG   . LYS   B 1 31  ? 52.378 -15.778 -16.577 1.00 26.01 ?  31   LYS   B CG   1 
ATOM   4288 C  CD   . LYS   B 1 31  ? 52.989 -14.938 -17.688 1.00 28.87 ?  31   LYS   B CD   1 
ATOM   4289 C  CE   . LYS   B 1 31  ? 54.470 -15.218 -17.848 1.00 31.06 ?  31   LYS   B CE   1 
ATOM   4290 N  NZ   . LYS   B 1 31  ? 55.212 -14.868 -16.607 1.00 32.20 ?  31   LYS   B NZ   1 
ATOM   4291 H  H    . LYS   B 1 31  ? 50.837 -18.015 -14.961 1.00 23.12 ?  31   LYS   B H    1 
ATOM   4292 H  HA   . LYS   B 1 31  ? 50.904 -16.028 -14.297 1.00 23.71 ?  31   LYS   B HA   1 
ATOM   4293 H  HB2  . LYS   B 1 31  ? 50.415 -15.383 -17.006 1.00 27.23 ?  31   LYS   B HB2  1 
ATOM   4294 H  HB3  . LYS   B 1 31  ? 51.027 -14.378 -15.938 1.00 27.23 ?  31   LYS   B HB3  1 
ATOM   4295 H  HG2  . LYS   B 1 31  ? 52.943 -15.715 -15.789 1.00 31.20 ?  31   LYS   B HG2  1 
ATOM   4296 H  HG3  . LYS   B 1 31  ? 52.336 -16.703 -16.878 1.00 31.20 ?  31   LYS   B HG3  1 
ATOM   4297 H  HD2  . LYS   B 1 31  ? 52.543 -15.150 -18.522 1.00 34.64 ?  31   LYS   B HD2  1 
ATOM   4298 H  HD3  . LYS   B 1 31  ? 52.873 -14.001 -17.471 1.00 34.64 ?  31   LYS   B HD3  1 
ATOM   4299 H  HE2  . LYS   B 1 31  ? 54.607 -16.163 -18.028 1.00 37.27 ?  31   LYS   B HE2  1 
ATOM   4300 H  HE3  . LYS   B 1 31  ? 54.824 -14.682 -18.576 1.00 37.27 ?  31   LYS   B HE3  1 
ATOM   4301 H  HZ1  . LYS   B 1 31  ? 56.088 -14.912 -16.752 1.00 38.63 ?  31   LYS   B HZ1  1 
ATOM   4302 H  HZ2  . LYS   B 1 31  ? 55.002 -14.041 -16.353 1.00 38.63 ?  31   LYS   B HZ2  1 
ATOM   4303 H  HZ3  . LYS   B 1 31  ? 54.997 -15.434 -15.954 1.00 38.63 ?  31   LYS   B HZ3  1 
ATOM   4304 N  N    . PRO   B 1 32  ? 48.339 -16.263 -13.645 1.00 15.43 ?  32   PRO   B N    1 
ATOM   4305 C  CA   . PRO   B 1 32  ? 46.959 -15.906 -13.288 1.00 14.32 ?  32   PRO   B CA   1 
ATOM   4306 C  C    . PRO   B 1 32  ? 46.878 -14.559 -12.593 1.00 14.31 ?  32   PRO   B C    1 
ATOM   4307 O  O    . PRO   B 1 32  ? 47.804 -14.136 -11.895 1.00 15.79 ?  32   PRO   B O    1 
ATOM   4308 C  CB   . PRO   B 1 32  ? 46.561 -17.020 -12.314 1.00 14.74 ?  32   PRO   B CB   1 
ATOM   4309 C  CG   . PRO   B 1 32  ? 47.859 -17.360 -11.636 1.00 15.06 ?  32   PRO   B CG   1 
ATOM   4310 C  CD   . PRO   B 1 32  ? 48.911 -17.251 -12.707 1.00 15.19 ?  32   PRO   B CD   1 
ATOM   4311 H  HA   . PRO   B 1 32  ? 46.374 -15.926 -14.065 1.00 17.18 ?  32   PRO   B HA   1 
ATOM   4312 H  HB2  . PRO   B 1 32  ? 45.908 -16.690 -11.675 1.00 17.68 ?  32   PRO   B HB2  1 
ATOM   4313 H  HB3  . PRO   B 1 32  ? 46.213 -17.786 -12.801 1.00 17.68 ?  32   PRO   B HB3  1 
ATOM   4314 H  HG2  . PRO   B 1 32  ? 48.031 -16.720 -10.923 1.00 18.06 ?  32   PRO   B HG2  1 
ATOM   4315 H  HG3  . PRO   B 1 32  ? 47.822 -18.261 -11.281 1.00 18.06 ?  32   PRO   B HG3  1 
ATOM   4316 H  HD2  . PRO   B 1 32  ? 49.739 -16.920 -12.330 1.00 18.22 ?  32   PRO   B HD2  1 
ATOM   4317 H  HD3  . PRO   B 1 32  ? 49.030 -18.108 -13.141 1.00 18.22 ?  32   PRO   B HD3  1 
ATOM   4318 N  N    . THR   B 1 33  ? 45.725 -13.905 -12.755 1.00 13.86 ?  33   THR   B N    1 
ATOM   4319 C  CA   . THR   B 1 33  ? 45.433 -12.728 -11.946 1.00 14.10 ?  33   THR   B CA   1 
ATOM   4320 C  C    . THR   B 1 33  ? 45.381 -13.083 -10.466 1.00 13.85 ?  33   THR   B C    1 
ATOM   4321 O  O    . THR   B 1 33  ? 45.846 -12.307 -9.618  1.00 14.86 ?  33   THR   B O    1 
ATOM   4322 C  CB   . THR   B 1 33  ? 44.114 -12.095 -12.393 1.00 14.82 ?  33   THR   B CB   1 
ATOM   4323 O  OG1  . THR   B 1 33  ? 44.159 -11.844 -13.798 1.00 14.52 ?  33   THR   B OG1  1 
ATOM   4324 C  CG2  . THR   B 1 33  ? 43.874 -10.789 -11.655 1.00 16.24 ?  33   THR   B CG2  1 
ATOM   4325 H  H    . THR   B 1 33  ? 45.104 -14.124 -13.315 1.00 16.63 ?  33   THR   B H    1 
ATOM   4326 H  HA   . THR   B 1 33  ? 46.134 -12.077 -12.074 1.00 16.92 ?  33   THR   B HA   1 
ATOM   4327 H  HB   . THR   B 1 33  ? 43.377 -12.698 -12.192 1.00 17.77 ?  33   THR   B HB   1 
ATOM   4328 H  HG1  . THR   B 1 33  ? 43.433 -11.482 -14.048 1.00 17.41 ?  33   THR   B HG1  1 
ATOM   4329 H  HG21 . THR   B 1 33  ? 43.122 -10.321 -12.042 1.00 19.49 ?  33   THR   B HG21 1 
ATOM   4330 H  HG22 . THR   B 1 33  ? 43.693 -10.962 -10.718 1.00 19.49 ?  33   THR   B HG22 1 
ATOM   4331 H  HG23 . THR   B 1 33  ? 44.665 -10.225 -11.722 1.00 19.49 ?  33   THR   B HG23 1 
ATOM   4332 N  N    . VAL   B 1 34  ? 44.834 -14.259 -10.136 1.00 13.07 ?  34   VAL   B N    1 
ATOM   4333 C  CA   . VAL   B 1 34  ? 44.633 -14.659 -8.747  1.00 12.39 ?  34   VAL   B CA   1 
ATOM   4334 C  C    . VAL   B 1 34  ? 45.067 -16.106 -8.580  1.00 11.01 ?  34   VAL   B C    1 
ATOM   4335 O  O    . VAL   B 1 34  ? 44.546 -16.996 -9.265  1.00 12.17 ?  34   VAL   B O    1 
ATOM   4336 C  CB   . VAL   B 1 34  ? 43.167 -14.515 -8.300  1.00 13.65 ?  34   VAL   B CB   1 
ATOM   4337 C  CG1  . VAL   B 1 34  ? 43.018 -14.964 -6.857  1.00 14.14 ?  34   VAL   B CG1  1 
ATOM   4338 C  CG2  . VAL   B 1 34  ? 42.665 -13.088 -8.485  1.00 14.38 ?  34   VAL   B CG2  1 
ATOM   4339 H  H    . VAL   B 1 34  ? 44.583 -14.854 -10.702 1.00 15.68 ?  34   VAL   B H    1 
ATOM   4340 H  HA   . VAL   B 1 34  ? 45.183 -14.103 -8.165  1.00 14.87 ?  34   VAL   B HA   1 
ATOM   4341 H  HB   . VAL   B 1 34  ? 42.616 -15.095 -8.850  1.00 16.38 ?  34   VAL   B HB   1 
ATOM   4342 H  HG11 . VAL   B 1 34  ? 42.171 -14.634 -6.511  1.00 16.96 ?  34   VAL   B HG11 1 
ATOM   4343 H  HG12 . VAL   B 1 34  ? 43.031 -15.932 -6.820  1.00 16.96 ?  34   VAL   B HG12 1 
ATOM   4344 H  HG13 . VAL   B 1 34  ? 43.749 -14.599 -6.335  1.00 16.96 ?  34   VAL   B HG13 1 
ATOM   4345 H  HG21 . VAL   B 1 34  ? 41.745 -13.035 -8.179  1.00 17.25 ?  34   VAL   B HG21 1 
ATOM   4346 H  HG22 . VAL   B 1 34  ? 43.222 -12.487 -7.971  1.00 17.25 ?  34   VAL   B HG22 1 
ATOM   4347 H  HG23 . VAL   B 1 34  ? 42.710 -12.859 -9.429  1.00 17.25 ?  34   VAL   B HG23 1 
ATOM   4348 N  N    . VAL   B 1 35  ? 45.977 -16.350 -7.642  1.00 10.87 ?  35   VAL   B N    1 
ATOM   4349 C  CA   . VAL   B 1 35  ? 46.216 -17.693 -7.128  1.00 10.66 ?  35   VAL   B CA   1 
ATOM   4350 C  C    . VAL   B 1 35  ? 45.674 -17.754 -5.709  1.00 10.46 ?  35   VAL   B C    1 
ATOM   4351 O  O    . VAL   B 1 35  ? 45.885 -16.831 -4.914  1.00 10.71 ?  35   VAL   B O    1 
ATOM   4352 C  CB   . VAL   B 1 35  ? 47.698 -18.119 -7.218  1.00 11.46 ?  35   VAL   B CB   1 
ATOM   4353 C  CG1  . VAL   B 1 35  ? 48.593 -17.297 -6.291  1.00 12.15 ?  35   VAL   B CG1  1 
ATOM   4354 C  CG2  . VAL   B 1 35  ? 47.833 -19.617 -6.919  1.00 12.43 ?  35   VAL   B CG2  1 
ATOM   4355 H  H    . VAL   B 1 35  ? 46.474 -15.746 -7.282  1.00 13.04 ?  35   VAL   B H    1 
ATOM   4356 H  HA   . VAL   B 1 35  ? 45.699 -18.322 -7.657  1.00 12.78 ?  35   VAL   B HA   1 
ATOM   4357 H  HB   . VAL   B 1 35  ? 48.002 -17.978 -8.129  1.00 13.74 ?  35   VAL   B HB   1 
ATOM   4358 H  HG11 . VAL   B 1 35  ? 49.517 -17.521 -6.475  1.00 14.57 ?  35   VAL   B HG11 1 
ATOM   4359 H  HG12 . VAL   B 1 35  ? 48.432 -16.361 -6.450  1.00 14.57 ?  35   VAL   B HG12 1 
ATOM   4360 H  HG13 . VAL   B 1 35  ? 48.377 -17.525 -5.370  1.00 14.57 ?  35   VAL   B HG13 1 
ATOM   4361 H  HG21 . VAL   B 1 35  ? 48.757 -19.885 -7.025  1.00 14.91 ?  35   VAL   B HG21 1 
ATOM   4362 H  HG22 . VAL   B 1 35  ? 47.542 -19.790 -6.006  1.00 14.91 ?  35   VAL   B HG22 1 
ATOM   4363 H  HG23 . VAL   B 1 35  ? 47.272 -20.122 -7.537  1.00 14.91 ?  35   VAL   B HG23 1 
ATOM   4364 N  N    . VAL   B 1 36  ? 44.956 -18.833 -5.398  1.00 10.39 ?  36   VAL   B N    1 
ATOM   4365 C  CA   . VAL   B 1 36  ? 44.406 -19.036 -4.068  1.00 10.28 ?  36   VAL   B CA   1 
ATOM   4366 C  C    . VAL   B 1 36  ? 45.410 -19.798 -3.216  1.00 10.11 ?  36   VAL   B C    1 
ATOM   4367 O  O    . VAL   B 1 36  ? 45.954 -20.828 -3.639  1.00 10.94 ?  36   VAL   B O    1 
ATOM   4368 C  CB   . VAL   B 1 36  ? 43.070 -19.794 -4.143  1.00 10.77 ?  36   VAL   B CB   1 
ATOM   4369 C  CG1  . VAL   B 1 36  ? 42.575 -20.150 -2.754  1.00 11.45 ?  36   VAL   B CG1  1 
ATOM   4370 C  CG2  . VAL   B 1 36  ? 42.046 -18.964 -4.891  1.00 11.25 ?  36   VAL   B CG2  1 
ATOM   4371 H  H    . VAL   B 1 36  ? 44.787 -19.476 -5.945  1.00 12.47 ?  36   VAL   B H    1 
ATOM   4372 H  HA   . VAL   B 1 36  ? 44.242 -18.177 -3.652  1.00 12.33 ?  36   VAL   B HA   1 
ATOM   4373 H  HB   . VAL   B 1 36  ? 43.199 -20.620 -4.634  1.00 12.92 ?  36   VAL   B HB   1 
ATOM   4374 H  HG11 . VAL   B 1 36  ? 41.631 -20.374 -2.803  1.00 13.73 ?  36   VAL   B HG11 1 
ATOM   4375 H  HG12 . VAL   B 1 36  ? 43.076 -20.907 -2.419  1.00 13.73 ?  36   VAL   B HG12 1 
ATOM   4376 H  HG13 . VAL   B 1 36  ? 42.697 -19.383 -2.170  1.00 13.73 ?  36   VAL   B HG13 1 
ATOM   4377 H  HG21 . VAL   B 1 36  ? 41.203 -19.440 -4.910  1.00 13.50 ?  36   VAL   B HG21 1 
ATOM   4378 H  HG22 . VAL   B 1 36  ? 41.939 -18.113 -4.439  1.00 13.50 ?  36   VAL   B HG22 1 
ATOM   4379 H  HG23 . VAL   B 1 36  ? 42.364 -18.816 -5.798  1.00 13.50 ?  36   VAL   B HG23 1 
ATOM   4380 N  N    . ASN   B 1 37  ? 45.634 -19.307 -2.000  1.00 10.31 ?  37   ASN   B N    1 
ATOM   4381 C  CA   . ASN   B 1 37  ? 46.390 -20.028 -0.991  1.00 10.63 ?  37   ASN   B CA   1 
ATOM   4382 C  C    . ASN   B 1 37  ? 45.441 -20.703 -0.008  1.00 10.37 ?  37   ASN   B C    1 
ATOM   4383 O  O    . ASN   B 1 37  ? 44.431 -20.126 0.405   1.00 11.02 ?  37   ASN   B O    1 
ATOM   4384 C  CB   . ASN   B 1 37  ? 47.327 -19.081 -0.235  1.00 10.49 ?  37   ASN   B CB   1 
ATOM   4385 C  CG   . ASN   B 1 37  ? 48.166 -19.800 0.785   1.00 10.64 ?  37   ASN   B CG   1 
ATOM   4386 O  OD1  . ASN   B 1 37  ? 48.507 -20.971 0.602   1.00 11.52 ?  37   ASN   B OD1  1 
ATOM   4387 N  ND2  . ASN   B 1 37  ? 48.510 -19.112 1.867   1.00 10.88 ?  37   ASN   B ND2  1 
ATOM   4388 H  H    . ASN   B 1 37  ? 45.352 -18.540 -1.727  1.00 12.37 ?  37   ASN   B H    1 
ATOM   4389 H  HA   . ASN   B 1 37  ? 46.923 -20.719 -1.411  1.00 12.75 ?  37   ASN   B HA   1 
ATOM   4390 H  HB2  . ASN   B 1 37  ? 47.927 -18.662 -0.870  1.00 12.59 ?  37   ASN   B HB2  1 
ATOM   4391 H  HB3  . ASN   B 1 37  ? 46.806 -18.413 0.229   1.00 12.59 ?  37   ASN   B HB3  1 
ATOM   4392 H  HD21 . ASN   B 1 37  ? 48.989 -19.488 2.477   1.00 13.06 ?  37   ASN   B HD21 1 
ATOM   4393 H  HD22 . ASN   B 1 37  ? 48.252 -18.307 1.964   1.00 13.06 ?  37   ASN   B HD22 1 
ATOM   4394 N  N    . ALA   B 1 38  ? 45.790 -21.935 0.365   1.00 10.88 ?  38   ALA   B N    1 
ATOM   4395 C  CA   . ALA   B 1 38  ? 45.135 -22.681 1.442   1.00 11.14 ?  38   ALA   B CA   1 
ATOM   4396 C  C    . ALA   B 1 38  ? 45.724 -22.196 2.765   1.00 11.17 ?  38   ALA   B C    1 
ATOM   4397 O  O    . ALA   B 1 38  ? 46.625 -22.805 3.352   1.00 12.06 ?  38   ALA   B O    1 
ATOM   4398 C  CB   . ALA   B 1 38  ? 45.354 -24.176 1.251   1.00 12.56 ?  38   ALA   B CB   1 
ATOM   4399 H  H    . ALA   B 1 38  ? 46.436 -22.376 0.007   1.00 13.05 ?  38   ALA   B H    1 
ATOM   4400 H  HA   . ALA   B 1 38  ? 44.181 -22.499 1.440   1.00 13.36 ?  38   ALA   B HA   1 
ATOM   4401 H  HB1  . ALA   B 1 38  ? 44.907 -24.657 1.976   1.00 15.07 ?  38   ALA   B HB1  1 
ATOM   4402 H  HB2  . ALA   B 1 38  ? 44.968 -24.445 0.403   1.00 15.07 ?  38   ALA   B HB2  1 
ATOM   4403 H  HB3  . ALA   B 1 38  ? 46.299 -24.367 1.267   1.00 15.07 ?  38   ALA   B HB3  1 
ATOM   4404 N  N    . ALA   B 1 39  ? 45.212 -21.055 3.224   1.00 10.90 ?  39   ALA   B N    1 
ATOM   4405 C  CA   . ALA   B 1 39  ? 45.764 -20.326 4.354   1.00 11.23 ?  39   ALA   B CA   1 
ATOM   4406 C  C    . ALA   B 1 39  ? 45.145 -20.779 5.675   1.00 11.17 ?  39   ALA   B C    1 
ATOM   4407 O  O    . ALA   B 1 39  ? 44.115 -21.457 5.719   1.00 12.16 ?  39   ALA   B O    1 
ATOM   4408 C  CB   . ALA   B 1 39  ? 45.517 -18.826 4.168   1.00 11.97 ?  39   ALA   B CB   1 
ATOM   4409 H  H    . ALA   B 1 39  ? 44.515 -20.678 2.888   1.00 13.08 ?  39   ALA   B H    1 
ATOM   4410 H  HA   . ALA   B 1 39  ? 46.719 -20.474 4.398   1.00 13.47 ?  39   ALA   B HA   1 
ATOM   4411 H  HB1  . ALA   B 1 39  ? 45.891 -18.346 4.925   1.00 14.36 ?  39   ALA   B HB1  1 
ATOM   4412 H  HB2  . ALA   B 1 39  ? 45.947 -18.534 3.348   1.00 14.36 ?  39   ALA   B HB2  1 
ATOM   4413 H  HB3  . ALA   B 1 39  ? 44.562 -18.665 4.115   1.00 14.36 ?  39   ALA   B HB3  1 
ATOM   4414 N  N    . ASN   B 1 40  ? 45.782 -20.354 6.765   1.00 12.37 ?  40   ASN   B N    1 
ATOM   4415 C  CA   . ASN   B 1 40  ? 45.218 -20.401 8.105   1.00 12.90 ?  40   ASN   B CA   1 
ATOM   4416 C  C    . ASN   B 1 40  ? 45.039 -18.975 8.629   1.00 12.56 ?  40   ASN   B C    1 
ATOM   4417 O  O    . ASN   B 1 40  ? 45.460 -17.996 8.002   1.00 12.49 ?  40   ASN   B O    1 
ATOM   4418 C  CB   . ASN   B 1 40  ? 46.074 -21.268 9.046   1.00 13.79 ?  40   ASN   B CB   1 
ATOM   4419 C  CG   . ASN   B 1 40  ? 47.530 -20.870 9.050   1.00 14.69 ?  40   ASN   B CG   1 
ATOM   4420 O  OD1  . ASN   B 1 40  ? 47.852 -19.689 9.098   1.00 16.39 ?  40   ASN   B OD1  1 
ATOM   4421 N  ND2  . ASN   B 1 40  ? 48.421 -21.850 9.008   1.00 14.65 ?  40   ASN   B ND2  1 
ATOM   4422 H  H    . ASN   B 1 40  ? 46.574 -20.018 6.746   1.00 14.83 ?  40   ASN   B H    1 
ATOM   4423 H  HA   . ASN   B 1 40  ? 44.337 -20.800 8.061   1.00 15.48 ?  40   ASN   B HA   1 
ATOM   4424 H  HB2  . ASN   B 1 40  ? 45.738 -21.178 9.950   1.00 16.54 ?  40   ASN   B HB2  1 
ATOM   4425 H  HB3  . ASN   B 1 40  ? 46.017 -22.190 8.757   1.00 16.54 ?  40   ASN   B HB3  1 
ATOM   4426 H  HD21 . ASN   B 1 40  ? 49.264 -21.672 9.008   1.00 17.58 ?  40   ASN   B HD21 1 
ATOM   4427 H  HD22 . ASN   B 1 40  ? 48.158 -22.670 8.978   1.00 17.58 ?  40   ASN   B HD22 1 
ATOM   4428 N  N    . VAL   B 1 41  ? 44.388 -18.847 9.787   1.00 12.98 ?  41   VAL   B N    1 
ATOM   4429 C  CA   . VAL   B 1 41  ? 43.939 -17.525 10.239  1.00 14.03 ?  41   VAL   B CA   1 
ATOM   4430 C  C    . VAL   B 1 41  ? 45.094 -16.574 10.529  1.00 13.53 ?  41   VAL   B C    1 
ATOM   4431 O  O    . VAL   B 1 41  ? 44.920 -15.353 10.443  1.00 13.71 ?  41   VAL   B O    1 
ATOM   4432 C  CB   . VAL   B 1 41  ? 42.971 -17.610 11.438  1.00 15.08 ?  41   VAL   B CB   1 
ATOM   4433 C  CG1  . VAL   B 1 41  ? 41.662 -18.272 11.034  1.00 16.03 ?  41   VAL   B CG1  1 
ATOM   4434 C  CG2  . VAL   B 1 41  ? 43.618 -18.322 12.617  1.00 15.91 ?  41   VAL   B CG2  1 
ATOM   4435 H  H    . VAL   B 1 41  ? 44.197 -19.491 10.315  1.00 15.57 ?  41   VAL   B H    1 
ATOM   4436 H  HA   . VAL   B 1 41  ? 43.434 -17.126 9.514   1.00 16.83 ?  41   VAL   B HA   1 
ATOM   4437 H  HB   . VAL   B 1 41  ? 42.759 -16.708 11.728  1.00 18.09 ?  41   VAL   B HB   1 
ATOM   4438 H  HG11 . VAL   B 1 41  ? 41.065 -18.289 11.801  1.00 19.22 ?  41   VAL   B HG11 1 
ATOM   4439 H  HG12 . VAL   B 1 41  ? 41.258 -17.762 10.314  1.00 19.22 ?  41   VAL   B HG12 1 
ATOM   4440 H  HG13 . VAL   B 1 41  ? 41.844 -19.177 10.738  1.00 19.22 ?  41   VAL   B HG13 1 
ATOM   4441 H  HG21 . VAL   B 1 41  ? 42.997 -18.333 13.360  1.00 19.09 ?  41   VAL   B HG21 1 
ATOM   4442 H  HG22 . VAL   B 1 41  ? 43.836 -19.232 12.356  1.00 19.09 ?  41   VAL   B HG22 1 
ATOM   4443 H  HG23 . VAL   B 1 41  ? 44.426 -17.848 12.867  1.00 19.09 ?  41   VAL   B HG23 1 
ATOM   4444 N  N    . TYR   B 1 42  ? 46.262 -17.090 10.912  1.00 13.86 ?  42   TYR   B N    1 
ATOM   4445 C  CA   . TYR   B 1 42  ? 47.413 -16.238 11.175  1.00 14.14 ?  42   TYR   B CA   1 
ATOM   4446 C  C    . TYR   B 1 42  ? 48.376 -16.172 9.995   1.00 13.28 ?  42   TYR   B C    1 
ATOM   4447 O  O    . TYR   B 1 42  ? 49.466 -15.607 10.128  1.00 14.43 ?  42   TYR   B O    1 
ATOM   4448 C  CB   . TYR   B 1 42  ? 48.115 -16.642 12.478  1.00 15.92 ?  42   TYR   B CB   1 
ATOM   4449 C  CG   . TYR   B 1 42  ? 47.514 -15.965 13.703  1.00 16.26 ?  42   TYR   B CG   1 
ATOM   4450 C  CD1  . TYR   B 1 42  ? 47.745 -14.616 13.951  1.00 15.64 ?  42   TYR   B CD1  1 
ATOM   4451 C  CD2  . TYR   B 1 42  ? 46.712 -16.661 14.598  1.00 18.10 ?  42   TYR   B CD2  1 
ATOM   4452 C  CE1  . TYR   B 1 42  ? 47.203 -13.981 15.049  1.00 16.76 ?  42   TYR   B CE1  1 
ATOM   4453 C  CE2  . TYR   B 1 42  ? 46.166 -16.032 15.707  1.00 18.48 ?  42   TYR   B CE2  1 
ATOM   4454 C  CZ   . TYR   B 1 42  ? 46.416 -14.689 15.926  1.00 18.73 ?  42   TYR   B CZ   1 
ATOM   4455 O  OH   . TYR   B 1 42  ? 45.883 -14.046 17.025  1.00 21.75 ?  42   TYR   B OH   1 
ATOM   4456 H  H    . TYR   B 1 42  ? 46.407 -17.936 11.019  1.00 16.62 ?  42   TYR   B H    1 
ATOM   4457 H  HA   . TYR   B 1 42  ? 47.082 -15.340 11.309  1.00 16.96 ?  42   TYR   B HA   1 
ATOM   4458 H  HB2  . TYR   B 1 42  ? 48.036 -17.599 12.599  1.00 19.09 ?  42   TYR   B HB2  1 
ATOM   4459 H  HB3  . TYR   B 1 42  ? 49.049 -16.387 12.422  1.00 19.09 ?  42   TYR   B HB3  1 
ATOM   4460 H  HD1  . TYR   B 1 42  ? 48.282 -14.130 13.357  1.00 18.76 ?  42   TYR   B HD1  1 
ATOM   4461 H  HD2  . TYR   B 1 42  ? 46.540 -17.563 14.448  1.00 21.71 ?  42   TYR   B HD2  1 
ATOM   4462 H  HE1  . TYR   B 1 42  ? 47.377 -13.078 15.197  1.00 20.10 ?  42   TYR   B HE1  1 
ATOM   4463 H  HE2  . TYR   B 1 42  ? 45.629 -16.511 16.296  1.00 22.17 ?  42   TYR   B HE2  1 
ATOM   4464 H  HH   . TYR   B 1 42  ? 46.118 -13.242 17.024  1.00 26.09 ?  42   TYR   B HH   1 
ATOM   4465 N  N    . LEU   B 1 43  ? 47.975 -16.686 8.836   1.00 12.27 ?  43   LEU   B N    1 
ATOM   4466 C  CA   . LEU   B 1 43  ? 48.788 -16.620 7.628   1.00 11.89 ?  43   LEU   B CA   1 
ATOM   4467 C  C    . LEU   B 1 43  ? 50.199 -17.125 7.891   1.00 12.47 ?  43   LEU   B C    1 
ATOM   4468 O  O    . LEU   B 1 43  ? 51.182 -16.524 7.453   1.00 13.31 ?  43   LEU   B O    1 
ATOM   4469 C  CB   . LEU   B 1 43  ? 48.810 -15.216 7.020   1.00 12.31 ?  43   LEU   B CB   1 
ATOM   4470 C  CG   . LEU   B 1 43  ? 47.452 -14.601 6.655   1.00 12.71 ?  43   LEU   B CG   1 
ATOM   4471 C  CD1  . LEU   B 1 43  ? 47.662 -13.209 6.073   1.00 13.94 ?  43   LEU   B CD1  1 
ATOM   4472 C  CD2  . LEU   B 1 43  ? 46.684 -15.487 5.689   1.00 12.94 ?  43   LEU   B CD2  1 
ATOM   4473 H  H    . LEU   B 1 43  ? 47.224 -17.094 8.724   1.00 14.72 ?  43   LEU   B H    1 
ATOM   4474 H  HA   . LEU   B 1 43  ? 48.387 -17.211 6.965   1.00 14.26 ?  43   LEU   B HA   1 
ATOM   4475 H  HB2  . LEU   B 1 43  ? 49.235 -14.620 7.653   1.00 14.77 ?  43   LEU   B HB2  1 
ATOM   4476 H  HB3  . LEU   B 1 43  ? 49.336 -15.250 6.205   1.00 14.77 ?  43   LEU   B HB3  1 
ATOM   4477 H  HG   . LEU   B 1 43  ? 46.924 -14.507 7.459   1.00 15.24 ?  43   LEU   B HG   1 
ATOM   4478 H  HD11 . LEU   B 1 43  ? 46.799 -12.828 5.846   1.00 16.72 ?  43   LEU   B HD11 1 
ATOM   4479 H  HD12 . LEU   B 1 43  ? 48.103 -12.653 6.735   1.00 16.72 ?  43   LEU   B HD12 1 
ATOM   4480 H  HD13 . LEU   B 1 43  ? 48.213 -13.275 5.278   1.00 16.72 ?  43   LEU   B HD13 1 
ATOM   4481 H  HD21 . LEU   B 1 43  ? 45.881 -15.022 5.398   1.00 15.52 ?  43   LEU   B HD21 1 
ATOM   4482 H  HD22 . LEU   B 1 43  ? 47.242 -15.689 4.922   1.00 15.52 ?  43   LEU   B HD22 1 
ATOM   4483 H  HD23 . LEU   B 1 43  ? 46.436 -16.312 6.141   1.00 15.52 ?  43   LEU   B HD23 1 
ATOM   4484 N  N    . LYS   B 1 44  ? 50.297 -18.251 8.601   1.00 12.51 ?  44   LYS   B N    1 
ATOM   4485 C  CA   . LYS   B 1 44  ? 51.565 -18.928 8.840   1.00 13.15 ?  44   LYS   B CA   1 
ATOM   4486 C  C    . LYS   B 1 44  ? 51.679 -20.039 7.805   1.00 12.69 ?  44   LYS   B C    1 
ATOM   4487 O  O    . LYS   B 1 44  ? 50.980 -21.054 7.886   1.00 13.89 ?  44   LYS   B O    1 
ATOM   4488 C  CB   . LYS   B 1 44  ? 51.620 -19.450 10.274  1.00 15.08 ?  44   LYS   B CB   1 
ATOM   4489 C  CG   . LYS   B 1 44  ? 51.810 -18.341 11.300  1.00 17.64 ?  44   LYS   B CG   1 
ATOM   4490 C  CD   . LYS   B 1 44  ? 53.007 -17.471 10.905  1.00 20.75 ?  44   LYS   B CD   1 
ATOM   4491 C  CE   . LYS   B 1 44  ? 53.463 -16.553 12.007  1.00 23.66 ?  44   LYS   B CE   1 
ATOM   4492 N  NZ   . LYS   B 1 44  ? 54.650 -15.752 11.618  1.00 25.10 ?  44   LYS   B NZ   1 
ATOM   4493 H  H    . LYS   B 1 44  ? 49.620 -18.644 8.964   1.00 15.00 ?  44   LYS   B H    1 
ATOM   4494 H  HA   . LYS   B 1 44  ? 52.292 -18.311 8.678   1.00 15.77 ?  44   LYS   B HA   1 
ATOM   4495 H  HB2  . LYS   B 1 44  ? 50.780 -19.903 10.476  1.00 18.09 ?  44   LYS   B HB2  1 
ATOM   4496 H  HB3  . LYS   B 1 44  ? 52.356 -20.070 10.356  1.00 18.09 ?  44   LYS   B HB3  1 
ATOM   4497 H  HG2  . LYS   B 1 44  ? 51.017 -17.788 11.332  1.00 21.16 ?  44   LYS   B HG2  1 
ATOM   4498 H  HG3  . LYS   B 1 44  ? 51.989 -18.737 12.170  1.00 21.16 ?  44   LYS   B HG3  1 
ATOM   4499 H  HD2  . LYS   B 1 44  ? 53.746 -18.055 10.649  1.00 24.90 ?  44   LYS   B HD2  1 
ATOM   4500 H  HD3  . LYS   B 1 44  ? 52.752 -16.916 10.151  1.00 24.90 ?  44   LYS   B HD3  1 
ATOM   4501 H  HE2  . LYS   B 1 44  ? 52.747 -15.935 12.197  1.00 28.38 ?  44   LYS   B HE2  1 
ATOM   4502 H  HE3  . LYS   B 1 44  ? 53.685 -17.078 12.791  1.00 28.38 ?  44   LYS   B HE3  1 
ATOM   4503 H  HZ1  . LYS   B 1 44  ? 54.884 -15.214 12.287  1.00 30.12 ?  44   LYS   B HZ1  1 
ATOM   4504 H  HZ2  . LYS   B 1 44  ? 55.332 -16.287 11.422  1.00 30.12 ?  44   LYS   B HZ2  1 
ATOM   4505 H  HZ3  . LYS   B 1 44  ? 54.459 -15.254 10.902  1.00 30.12 ?  44   LYS   B HZ3  1 
ATOM   4506 N  N    . HIS   B 1 45  ? 52.528 -19.819 6.805   1.00 12.43 ?  45   HIS   B N    1 
ATOM   4507 C  CA   . HIS   B 1 45  ? 52.547 -20.648 5.600   1.00 12.69 ?  45   HIS   B CA   1 
ATOM   4508 C  C    . HIS   B 1 45  ? 53.566 -21.770 5.758   1.00 14.83 ?  45   HIS   B C    1 
ATOM   4509 O  O    . HIS   B 1 45  ? 54.631 -21.782 5.149   1.00 17.26 ?  45   HIS   B O    1 
ATOM   4510 C  CB   . HIS   B 1 45  ? 52.862 -19.792 4.387   1.00 12.32 ?  45   HIS   B CB   1 
ATOM   4511 C  CG   . HIS   B 1 45  ? 51.991 -18.589 4.279   1.00 12.09 ?  45   HIS   B CG   1 
ATOM   4512 N  ND1  . HIS   B 1 45  ? 50.613 -18.668 4.246   1.00 12.61 ?  45   HIS   B ND1  1 
ATOM   4513 C  CD2  . HIS   B 1 45  ? 52.307 -17.276 4.220   1.00 12.79 ?  45   HIS   B CD2  1 
ATOM   4514 C  CE1  . HIS   B 1 45  ? 50.125 -17.445 4.145   1.00 12.27 ?  45   HIS   B CE1  1 
ATOM   4515 N  NE2  . HIS   B 1 45  ? 51.128 -16.583 4.126   1.00 12.95 ?  45   HIS   B NE2  1 
ATOM   4516 H  H    . HIS   B 1 45  ? 53.102 -19.176 6.792   1.00 14.90 ?  45   HIS   B H    1 
ATOM   4517 H  HA   . HIS   B 1 45  ? 51.666 -21.043 5.472   1.00 15.22 ?  45   HIS   B HA   1 
ATOM   4518 H  HB2  . HIS   B 1 45  ? 53.780 -19.499 4.436   1.00 14.78 ?  45   HIS   B HB2  1 
ATOM   4519 H  HB3  . HIS   B 1 45  ? 52.732 -20.333 3.583   1.00 14.78 ?  45   HIS   B HB3  1 
ATOM   4520 H  HD2  . HIS   B 1 45  ? 53.164 -16.912 4.224   1.00 15.34 ?  45   HIS   B HD2  1 
ATOM   4521 H  HE1  . HIS   B 1 45  ? 49.223 -17.225 4.091   1.00 14.72 ?  45   HIS   B HE1  1 
ATOM   4522 H  HE2  . HIS   B 1 45  ? 51.051 -15.729 4.075   1.00 15.54 ?  45   HIS   B HE2  1 
ATOM   4523 N  N    A GLY   B 1 46  ? 53.195 -22.745 6.582   0.50 15.94 ?  46   GLY   B N    1 
ATOM   4524 N  N    B GLY   B 1 46  ? 53.209 -22.729 6.602   0.50 15.94 ?  46   GLY   B N    1 
ATOM   4525 C  CA   A GLY   B 1 46  ? 54.121 -23.794 6.968   0.50 17.62 ?  46   GLY   B CA   1 
ATOM   4526 C  CA   B GLY   B 1 46  ? 54.132 -23.794 6.936   0.50 17.47 ?  46   GLY   B CA   1 
ATOM   4527 C  C    A GLY   B 1 46  ? 54.165 -25.024 6.083   0.50 18.96 ?  46   GLY   B C    1 
ATOM   4528 C  C    B GLY   B 1 46  ? 54.151 -24.946 5.954   0.50 18.77 ?  46   GLY   B C    1 
ATOM   4529 O  O    A GLY   B 1 46  ? 55.247 -25.478 5.699   0.50 20.94 ?  46   GLY   B O    1 
ATOM   4530 O  O    B GLY   B 1 46  ? 55.185 -25.248 5.351   0.50 20.32 ?  46   GLY   B O    1 
ATOM   4531 H  H    A GLY   B 1 46  ? 52.414 -22.806 6.945   0.50 19.13 ?  46   GLY   B H    1 
ATOM   4532 H  H    B GLY   B 1 46  ? 52.445 -22.774 7.002   0.50 19.12 ?  46   GLY   B H    1 
ATOM   4533 H  HA2  A GLY   B 1 46  ? 55.013 -23.418 7.000   0.50 21.13 ?  46   GLY   B HA2  1 
ATOM   4534 H  HA2  B GLY   B 1 46  ? 55.027 -23.426 6.988   0.50 20.96 ?  46   GLY   B HA2  1 
ATOM   4535 H  HA3  A GLY   B 1 46  ? 53.891 -24.094 7.859   0.50 21.13 ?  46   GLY   B HA3  1 
ATOM   4536 H  HA3  B GLY   B 1 46  ? 53.900 -24.144 7.810   0.50 20.96 ?  46   GLY   B HA3  1 
ATOM   4537 N  N    . GLY   B 1 47  ? 53.005 -25.599 5.774   1.00 18.77 ?  47   GLY   B N    1 
ATOM   4538 C  CA   . GLY   B 1 47  ? 52.942 -26.868 5.079   1.00 16.56 ?  47   GLY   B CA   1 
ATOM   4539 C  C    . GLY   B 1 47  ? 52.036 -26.843 3.865   1.00 14.20 ?  47   GLY   B C    1 
ATOM   4540 O  O    . GLY   B 1 47  ? 51.392 -25.838 3.564   1.00 14.25 ?  47   GLY   B O    1 
ATOM   4541 H  H    A GLY   B 1 47  ? 52.233 -25.278 5.982   0.50 22.51 ?  47   GLY   B H    1 
ATOM   4542 H  H    B GLY   B 1 47  ? 52.240 -25.322 6.058   0.50 22.51 ?  47   GLY   B H    1 
ATOM   4543 H  HA2  . GLY   B 1 47  ? 53.829 -27.127 4.786   1.00 19.86 ?  47   GLY   B HA2  1 
ATOM   4544 H  HA3  . GLY   B 1 47  ? 52.617 -27.550 5.690   1.00 19.86 ?  47   GLY   B HA3  1 
ATOM   4545 N  N    . GLY   B 1 48  ? 51.988 -27.985 3.180   1.00 13.19 ?  48   GLY   B N    1 
ATOM   4546 C  CA   . GLY   B 1 48  ? 51.061 -28.133 2.076   1.00 13.25 ?  48   GLY   B CA   1 
ATOM   4547 C  C    . GLY   B 1 48  ? 51.201 -27.021 1.059   1.00 12.47 ?  48   GLY   B C    1 
ATOM   4548 O  O    . GLY   B 1 48  ? 52.306 -26.556 0.751   1.00 12.91 ?  48   GLY   B O    1 
ATOM   4549 H  H    . GLY   B 1 48  ? 52.479 -28.667 3.332   1.00 15.82 ?  48   GLY   B H    1 
ATOM   4550 H  HA2  . GLY   B 1 48  ? 51.219 -28.980 1.632   1.00 15.89 ?  48   GLY   B HA2  1 
ATOM   4551 H  HA3  . GLY   B 1 48  ? 50.150 -28.126 2.411   1.00 15.89 ?  48   GLY   B HA3  1 
ATOM   4552 N  N    . VAL   B 1 49  ? 50.055 -26.584 0.532   1.00 12.32 ?  49   VAL   B N    1 
ATOM   4553 C  CA   . VAL   B 1 49  ? 50.045 -25.558 -0.507  1.00 12.70 ?  49   VAL   B CA   1 
ATOM   4554 C  C    . VAL   B 1 49  ? 50.706 -24.275 -0.014  1.00 11.96 ?  49   VAL   B C    1 
ATOM   4555 O  O    . VAL   B 1 49  ? 51.496 -23.653 -0.734  1.00 12.48 ?  49   VAL   B O    1 
ATOM   4556 C  CB   . VAL   B 1 49  ? 48.605 -25.300 -0.994  1.00 13.74 ?  49   VAL   B CB   1 
ATOM   4557 C  CG1  . VAL   B 1 49  ? 48.547 -24.039 -1.855  1.00 13.95 ?  49   VAL   B CG1  1 
ATOM   4558 C  CG2  . VAL   B 1 49  ? 48.070 -26.505 -1.758  1.00 15.29 ?  49   VAL   B CG2  1 
ATOM   4559 H  H    . VAL   B 1 49  ? 49.269 -26.862 0.757   1.00 14.78 ?  49   VAL   B H    1 
ATOM   4560 H  HA   . VAL   B 1 49  ? 50.555 -25.875 -1.266  1.00 15.23 ?  49   VAL   B HA   1 
ATOM   4561 H  HB   . VAL   B 1 49  ? 48.033 -25.159 -0.225  1.00 16.49 ?  49   VAL   B HB   1 
ATOM   4562 H  HG11 . VAL   B 1 49  ? 47.726 -24.048 -2.373  1.00 16.73 ?  49   VAL   B HG11 1 
ATOM   4563 H  HG12 . VAL   B 1 49  ? 48.559 -23.256 -1.278  1.00 16.73 ?  49   VAL   B HG12 1 
ATOM   4564 H  HG13 . VAL   B 1 49  ? 49.312 -24.023 -2.451  1.00 16.73 ?  49   VAL   B HG13 1 
ATOM   4565 H  HG21 . VAL   B 1 49  ? 47.165 -26.315 -2.051  1.00 18.34 ?  49   VAL   B HG21 1 
ATOM   4566 H  HG22 . VAL   B 1 49  ? 48.639 -26.664 -2.531  1.00 18.34 ?  49   VAL   B HG22 1 
ATOM   4567 H  HG23 . VAL   B 1 49  ? 48.078 -27.276 -1.176  1.00 18.34 ?  49   VAL   B HG23 1 
ATOM   4568 N  N    . ALA   B 1 50  ? 50.359 -23.830 1.195   1.00 11.62 ?  50   ALA   B N    1 
ATOM   4569 C  CA   . ALA   B 1 50  ? 50.881 -22.554 1.674   1.00 11.37 ?  50   ALA   B CA   1 
ATOM   4570 C  C    . ALA   B 1 50  ? 52.400 -22.584 1.774   1.00 11.78 ?  50   ALA   B C    1 
ATOM   4571 O  O    . ALA   B 1 50  ? 53.079 -21.613 1.418   1.00 11.68 ?  50   ALA   B O    1 
ATOM   4572 C  CB   . ALA   B 1 50  ? 50.257 -22.200 3.023   1.00 11.73 ?  50   ALA   B CB   1 
ATOM   4573 H  H    . ALA   B 1 50  ? 49.841 -24.239 1.748   1.00 13.94 ?  50   ALA   B H    1 
ATOM   4574 H  HA   . ALA   B 1 50  ? 50.648 -21.859 1.049   1.00 13.64 ?  50   ALA   B HA   1 
ATOM   4575 H  HB1  . ALA   B 1 50  ? 50.616 -21.347 3.327   1.00 14.07 ?  50   ALA   B HB1  1 
ATOM   4576 H  HB2  . ALA   B 1 50  ? 49.295 -22.131 2.921   1.00 14.07 ?  50   ALA   B HB2  1 
ATOM   4577 H  HB3  . ALA   B 1 50  ? 50.472 -22.892 3.670   1.00 14.07 ?  50   ALA   B HB3  1 
ATOM   4578 N  N    . GLY   B 1 51  ? 52.950 -23.677 2.293   1.00 12.49 ?  51   GLY   B N    1 
ATOM   4579 C  CA   . GLY   B 1 51  ? 54.395 -23.781 2.371   1.00 13.12 ?  51   GLY   B CA   1 
ATOM   4580 C  C    . GLY   B 1 51  ? 55.048 -23.735 1.004   1.00 12.99 ?  51   GLY   B C    1 
ATOM   4581 O  O    . GLY   B 1 51  ? 56.088 -23.098 0.821   1.00 13.67 ?  51   GLY   B O    1 
ATOM   4582 H  H    . GLY   B 1 51  ? 52.523 -24.361 2.598   1.00 14.99 ?  51   GLY   B H    1 
ATOM   4583 H  HA2  . GLY   B 1 51  ? 54.746 -23.048 2.904   1.00 15.74 ?  51   GLY   B HA2  1 
ATOM   4584 H  HA3  . GLY   B 1 51  ? 54.642 -24.616 2.802   1.00 15.74 ?  51   GLY   B HA3  1 
ATOM   4585 N  N    . ALA   B 1 52  ? 54.436 -24.391 0.018   1.00 12.68 ?  52   ALA   B N    1 
ATOM   4586 C  CA   . ALA   B 1 52  ? 55.000 -24.395 -1.324  1.00 12.85 ?  52   ALA   B CA   1 
ATOM   4587 C  C    . ALA   B 1 52  ? 54.922 -23.018 -1.972  1.00 12.44 ?  52   ALA   B C    1 
ATOM   4588 O  O    . ALA   B 1 52  ? 55.895 -22.564 -2.595  1.00 13.19 ?  52   ALA   B O    1 
ATOM   4589 C  CB   . ALA   B 1 52  ? 54.291 -25.434 -2.183  1.00 13.60 ?  52   ALA   B CB   1 
ATOM   4590 H  H    . ALA   B 1 52  ? 53.695 -24.826 0.101   1.00 15.21 ?  52   ALA   B H    1 
ATOM   4591 H  HA   . ALA   B 1 52  ? 55.934 -24.642 -1.264  1.00 15.41 ?  52   ALA   B HA   1 
ATOM   4592 H  HB1  . ALA   B 1 52  ? 54.682 -25.427 -3.070  1.00 16.32 ?  52   ALA   B HB1  1 
ATOM   4593 H  HB2  . ALA   B 1 52  ? 54.408 -26.309 -1.778  1.00 16.32 ?  52   ALA   B HB2  1 
ATOM   4594 H  HB3  . ALA   B 1 52  ? 53.349 -25.215 -2.232  1.00 16.32 ?  52   ALA   B HB3  1 
ATOM   4595 N  N    . LEU   B 1 53  ? 53.774 -22.344 -1.857  1.00 11.65 ?  53   LEU   B N    1 
ATOM   4596 C  CA   . LEU   B 1 53  ? 53.663 -21.002 -2.422  1.00 12.20 ?  53   LEU   B CA   1 
ATOM   4597 C  C    . LEU   B 1 53  ? 54.668 -20.062 -1.771  1.00 12.14 ?  53   LEU   B C    1 
ATOM   4598 O  O    . LEU   B 1 53  ? 55.372 -19.312 -2.455  1.00 12.63 ?  53   LEU   B O    1 
ATOM   4599 C  CB   . LEU   B 1 53  ? 52.241 -20.465 -2.245  1.00 12.89 ?  53   LEU   B CB   1 
ATOM   4600 C  CG   . LEU   B 1 53  ? 51.107 -21.185 -2.986  1.00 13.26 ?  53   LEU   B CG   1 
ATOM   4601 C  CD1  . LEU   B 1 53  ? 49.774 -20.567 -2.638  1.00 14.13 ?  53   LEU   B CD1  1 
ATOM   4602 C  CD2  . LEU   B 1 53  ? 51.322 -21.153 -4.489  1.00 15.30 ?  53   LEU   B CD2  1 
ATOM   4603 H  H    . LEU   B 1 53  ? 53.066 -22.634 -1.464  1.00 13.97 ?  53   LEU   B H    1 
ATOM   4604 H  HA   . LEU   B 1 53  ? 53.856 -21.046 -3.377  1.00 14.63 ?  53   LEU   B HA   1 
ATOM   4605 H  HB2  . LEU   B 1 53  ? 52.027 -20.505 -1.302  1.00 15.46 ?  53   LEU   B HB2  1 
ATOM   4606 H  HB3  . LEU   B 1 53  ? 52.231 -19.548 -2.542  1.00 15.46 ?  53   LEU   B HB3  1 
ATOM   4607 H  HG   . LEU   B 1 53  ? 51.081 -22.113 -2.706  1.00 15.90 ?  53   LEU   B HG   1 
ATOM   4608 H  HD11 . LEU   B 1 53  ? 49.070 -21.036 -3.113  1.00 16.95 ?  53   LEU   B HD11 1 
ATOM   4609 H  HD12 . LEU   B 1 53  ? 49.629 -20.643 -1.679  1.00 16.95 ?  53   LEU   B HD12 1 
ATOM   4610 H  HD13 . LEU   B 1 53  ? 49.779 -19.631 -2.895  1.00 16.95 ?  53   LEU   B HD13 1 
ATOM   4611 H  HD21 . LEU   B 1 53  ? 50.582 -21.598 -4.927  1.00 18.36 ?  53   LEU   B HD21 1 
ATOM   4612 H  HD22 . LEU   B 1 53  ? 51.373 -20.229 -4.781  1.00 18.36 ?  53   LEU   B HD22 1 
ATOM   4613 H  HD23 . LEU   B 1 53  ? 52.153 -21.610 -4.699  1.00 18.36 ?  53   LEU   B HD23 1 
ATOM   4614 N  N    . ASN   B 1 54  ? 54.757 -20.091 -0.446  1.00 11.70 ?  54   ASN   B N    1 
ATOM   4615 C  CA   . ASN   B 1 54  ? 55.670 -19.176 0.222   1.00 12.32 ?  54   ASN   B CA   1 
ATOM   4616 C  C    . ASN   B 1 54  ? 57.113 -19.458 -0.173  1.00 12.95 ?  54   ASN   B C    1 
ATOM   4617 O  O    . ASN   B 1 54  ? 57.893 -18.525 -0.409  1.00 13.41 ?  54   ASN   B O    1 
ATOM   4618 C  CB   . ASN   B 1 54  ? 55.497 -19.247 1.730   1.00 12.99 ?  54   ASN   B CB   1 
ATOM   4619 C  CG   . ASN   B 1 54  ? 56.486 -18.350 2.443   1.00 13.34 ?  54   ASN   B CG   1 
ATOM   4620 O  OD1  . ASN   B 1 54  ? 56.510 -17.137 2.208   1.00 13.45 ?  54   ASN   B OD1  1 
ATOM   4621 N  ND2  . ASN   B 1 54  ? 57.340 -18.937 3.273   1.00 15.05 ?  54   ASN   B ND2  1 
ATOM   4622 H  H    . ASN   B 1 54  ? 54.314 -20.616 0.068   1.00 14.04 ?  54   ASN   B H    1 
ATOM   4623 H  HA   . ASN   B 1 54  ? 55.455 -18.272 -0.060  1.00 14.78 ?  54   ASN   B HA   1 
ATOM   4624 H  HB2  . ASN   B 1 54  ? 54.599 -18.953 1.962   1.00 15.58 ?  54   ASN   B HB2  1 
ATOM   4625 H  HB3  . ASN   B 1 54  ? 55.640 -20.155 2.027   1.00 15.58 ?  54   ASN   B HB3  1 
ATOM   4626 H  HD21 . ASN   B 1 54  ? 57.931 -18.468 3.687   1.00 18.05 ?  54   ASN   B HD21 1 
ATOM   4627 H  HD22 . ASN   B 1 54  ? 57.308 -19.788 3.392   1.00 18.05 ?  54   ASN   B HD22 1 
ATOM   4628 N  N    . LYS   B 1 55  ? 57.495 -20.737 -0.231  1.00 13.53 ?  55   LYS   B N    1 
ATOM   4629 C  CA   . LYS   B 1 55  ? 58.848 -21.080 -0.653  1.00 14.82 ?  55   LYS   B CA   1 
ATOM   4630 C  C    . LYS   B 1 55  ? 59.144 -20.534 -2.044  1.00 14.27 ?  55   LYS   B C    1 
ATOM   4631 O  O    . LYS   B 1 55  ? 60.241 -20.021 -2.297  1.00 14.88 ?  55   LYS   B O    1 
ATOM   4632 C  CB   . LYS   B 1 55  ? 59.032 -22.595 -0.617  1.00 16.36 ?  55   LYS   B CB   1 
ATOM   4633 C  CG   . LYS   B 1 55  ? 60.423 -23.052 -1.011  1.00 20.49 ?  55   LYS   B CG   1 
ATOM   4634 C  CD   . LYS   B 1 55  ? 60.591 -24.554 -0.851  1.00 23.74 ?  55   LYS   B CD   1 
ATOM   4635 C  CE   . LYS   B 1 55  ? 60.610 -24.971 0.618   1.00 26.48 ?  55   LYS   B CE   1 
ATOM   4636 N  NZ   . LYS   B 1 55  ? 60.981 -26.398 0.785   1.00 27.90 ?  55   LYS   B NZ   1 
ATOM   4637 H  H    . LYS   B 1 55  ? 56.992 -21.405 -0.037  1.00 16.22 ?  55   LYS   B H    1 
ATOM   4638 H  HA   . LYS   B 1 55  ? 59.480 -20.683 -0.036  1.00 17.78 ?  55   LYS   B HA   1 
ATOM   4639 H  HB2  . LYS   B 1 55  ? 58.859 -22.903 0.286   1.00 19.62 ?  55   LYS   B HB2  1 
ATOM   4640 H  HB3  . LYS   B 1 55  ? 58.401 -23.002 -1.230  1.00 19.62 ?  55   LYS   B HB3  1 
ATOM   4641 H  HG2  . LYS   B 1 55  ? 60.584 -22.827 -1.941  1.00 24.58 ?  55   LYS   B HG2  1 
ATOM   4642 H  HG3  . LYS   B 1 55  ? 61.077 -22.610 -0.444  1.00 24.58 ?  55   LYS   B HG3  1 
ATOM   4643 H  HD2  . LYS   B 1 55  ? 59.849 -25.008 -1.283  1.00 28.48 ?  55   LYS   B HD2  1 
ATOM   4644 H  HD3  . LYS   B 1 55  ? 61.431 -24.829 -1.253  1.00 28.48 ?  55   LYS   B HD3  1 
ATOM   4645 H  HE2  . LYS   B 1 55  ? 61.260 -24.426 1.093   1.00 31.77 ?  55   LYS   B HE2  1 
ATOM   4646 H  HE3  . LYS   B 1 55  ? 59.726 -24.837 0.998   1.00 31.77 ?  55   LYS   B HE3  1 
ATOM   4647 H  HZ1  . LYS   B 1 55  ? 60.959 -26.617 1.648   1.00 33.48 ?  55   LYS   B HZ1  1 
ATOM   4648 H  HZ2  . LYS   B 1 55  ? 60.405 -26.913 0.342   1.00 33.48 ?  55   LYS   B HZ2  1 
ATOM   4649 H  HZ3  . LYS   B 1 55  ? 61.799 -26.538 0.470   1.00 33.48 ?  55   LYS   B HZ3  1 
ATOM   4650 N  N    . ALA   B 1 56  ? 58.178 -20.622 -2.960  1.00 13.68 ?  56   ALA   B N    1 
ATOM   4651 C  CA   . ALA   B 1 56  ? 58.396 -20.111 -4.307  1.00 14.31 ?  56   ALA   B CA   1 
ATOM   4652 C  C    . ALA   B 1 56  ? 58.678 -18.615 -4.293  1.00 14.01 ?  56   ALA   B C    1 
ATOM   4653 O  O    . ALA   B 1 56  ? 59.409 -18.116 -5.160  1.00 15.47 ?  56   ALA   B O    1 
ATOM   4654 C  CB   . ALA   B 1 56  ? 57.190 -20.425 -5.193  1.00 15.41 ?  56   ALA   B CB   1 
ATOM   4655 H  H    . ALA   B 1 56  ? 57.391 -20.951 -2.825  1.00 16.41 ?  56   ALA   B H    1 
ATOM   4656 H  HA   . ALA   B 1 56  ? 59.168 -20.548 -4.687  1.00 17.17 ?  56   ALA   B HA   1 
ATOM   4657 H  HB1  . ALA   B 1 56  ? 57.359 -20.087 -6.089  1.00 18.49 ?  56   ALA   B HB1  1 
ATOM   4658 H  HB2  . ALA   B 1 56  ? 57.066 -21.386 -5.223  1.00 18.49 ?  56   ALA   B HB2  1 
ATOM   4659 H  HB3  . ALA   B 1 56  ? 56.402 -20.000 -4.824  1.00 18.49 ?  56   ALA   B HB3  1 
ATOM   4660 N  N    . THR   B 1 57  ? 58.104 -17.885 -3.334  1.00 13.87 ?  57   THR   B N    1 
ATOM   4661 C  CA   . THR   B 1 57  ? 58.346 -16.450 -3.211  1.00 14.00 ?  57   THR   B CA   1 
ATOM   4662 C  C    . THR   B 1 57  ? 59.597 -16.129 -2.406  1.00 14.76 ?  57   THR   B C    1 
ATOM   4663 O  O    . THR   B 1 57  ? 59.836 -14.957 -2.097  1.00 15.29 ?  57   THR   B O    1 
ATOM   4664 C  CB   . THR   B 1 57  ? 57.150 -15.719 -2.574  1.00 13.65 ?  57   THR   B CB   1 
ATOM   4665 O  OG1  . THR   B 1 57  ? 57.127 -15.935 -1.157  1.00 13.51 ?  57   THR   B OG1  1 
ATOM   4666 C  CG2  . THR   B 1 57  ? 55.833 -16.141 -3.207  1.00 13.57 ?  57   THR   B CG2  1 
ATOM   4667 H  H    . THR   B 1 57  ? 57.550 -18.194 -2.748  1.00 16.64 ?  57   THR   B H    1 
ATOM   4668 H  HA   . THR   B 1 57  ? 58.464 -16.079 -4.100  1.00 16.79 ?  57   THR   B HA   1 
ATOM   4669 H  HB   . THR   B 1 57  ? 57.252 -14.764 -2.736  1.00 16.37 ?  57   THR   B HB   1 
ATOM   4670 H  HG1  . THR   B 1 57  ? 57.057 -16.756 -0.995  1.00 16.21 ?  57   THR   B HG1  1 
ATOM   4671 H  HG21 . THR   B 1 57  ? 55.114 -15.573 -2.894  1.00 16.28 ?  57   THR   B HG21 1 
ATOM   4672 H  HG22 . THR   B 1 57  ? 55.892 -16.075 -4.173  1.00 16.28 ?  57   THR   B HG22 1 
ATOM   4673 H  HG23 . THR   B 1 57  ? 55.633 -17.061 -2.969  1.00 16.28 ?  57   THR   B HG23 1 
ATOM   4674 N  N    . ASN   B 1 58  ? 60.390 -17.132 -2.048  1.00 15.64 ?  58   ASN   B N    1 
ATOM   4675 C  CA   . ASN   B 1 58  ? 61.590 -16.915 -1.246  1.00 18.60 ?  58   ASN   B CA   1 
ATOM   4676 C  C    . ASN   B 1 58  ? 61.252 -16.210 0.067   1.00 16.29 ?  58   ASN   B C    1 
ATOM   4677 O  O    . ASN   B 1 58  ? 61.986 -15.334 0.534   1.00 16.89 ?  58   ASN   B O    1 
ATOM   4678 C  CB   . ASN   B 1 58  ? 62.667 -16.153 -2.024  1.00 25.54 ?  58   ASN   B CB   1 
ATOM   4679 C  CG   . ASN   B 1 58  ? 64.042 -16.295 -1.401  1.00 33.19 ?  58   ASN   B CG   1 
ATOM   4680 O  OD1  . ASN   B 1 58  ? 64.351 -17.311 -0.778  1.00 35.80 ?  58   ASN   B OD1  1 
ATOM   4681 N  ND2  . ASN   B 1 58  ? 64.874 -15.272 -1.562  1.00 38.47 ?  58   ASN   B ND2  1 
ATOM   4682 H  H    . ASN   B 1 58  ? 60.253 -17.959 -2.253  1.00 18.76 ?  58   ASN   B H    1 
ATOM   4683 H  HA   . ASN   B 1 58  ? 61.962 -17.785 -1.025  1.00 22.31 ?  58   ASN   B HA   1 
ATOM   4684 H  HB2  . ASN   B 1 58  ? 62.712 -16.499 -2.931  1.00 30.64 ?  58   ASN   B HB2  1 
ATOM   4685 H  HB3  . ASN   B 1 58  ? 62.445 -15.211 -2.038  1.00 30.64 ?  58   ASN   B HB3  1 
ATOM   4686 H  HD21 . ASN   B 1 58  ? 65.666 -15.305 -1.228  1.00 46.16 ?  58   ASN   B HD21 1 
ATOM   4687 H  HD22 . ASN   B 1 58  ? 64.620 -14.578 -2.001  1.00 46.16 ?  58   ASN   B HD22 1 
ATOM   4688 N  N    . ASN   B 1 59  ? 60.128 -16.599 0.670   1.00 14.97 ?  59   ASN   B N    1 
ATOM   4689 C  CA   . ASN   B 1 59  ? 59.651 -16.133 1.971   1.00 14.89 ?  59   ASN   B CA   1 
ATOM   4690 C  C    . ASN   B 1 59  ? 59.054 -14.727 1.917   1.00 14.28 ?  59   ASN   B C    1 
ATOM   4691 O  O    . ASN   B 1 59  ? 58.628 -14.221 2.963   1.00 14.38 ?  59   ASN   B O    1 
ATOM   4692 C  CB   . ASN   B 1 59  ? 60.725 -16.186 3.073   1.00 16.22 ?  59   ASN   B CB   1 
ATOM   4693 C  CG   . ASN   B 1 59  ? 60.140 -16.367 4.456   1.00 17.38 ?  59   ASN   B CG   1 
ATOM   4694 O  OD1  . ASN   B 1 59  ? 59.306 -17.249 4.680   1.00 17.42 ?  59   ASN   B OD1  1 
ATOM   4695 N  ND2  . ASN   B 1 59  ? 60.564 -15.531 5.393   1.00 18.23 ?  59   ASN   B ND2  1 
ATOM   4696 H  H    . ASN   B 1 59  ? 59.592 -17.177 0.321   1.00 17.96 ?  59   ASN   B H    1 
ATOM   4697 H  HA   . ASN   B 1 59  ? 58.943 -16.731 2.252   1.00 17.86 ?  59   ASN   B HA   1 
ATOM   4698 H  HB2  . ASN   B 1 59  ? 61.319 -16.935 2.910   1.00 19.46 ?  59   ASN   B HB2  1 
ATOM   4699 H  HB3  . ASN   B 1 59  ? 61.227 -15.357 3.073   1.00 19.46 ?  59   ASN   B HB3  1 
ATOM   4700 H  HD21 . ASN   B 1 59  ? 60.257 -15.589 6.197   1.00 21.87 ?  59   ASN   B HD21 1 
ATOM   4701 H  HD22 . ASN   B 1 59  ? 61.146 -14.928 5.201   1.00 21.87 ?  59   ASN   B HD22 1 
ATOM   4702 N  N    . ALA   B 1 60  ? 58.998 -14.079 0.750   1.00 13.93 ?  60   ALA   B N    1 
ATOM   4703 C  CA   . ALA   B 1 60  ? 58.404 -12.747 0.681   1.00 14.20 ?  60   ALA   B CA   1 
ATOM   4704 C  C    . ALA   B 1 60  ? 56.933 -12.773 1.075   1.00 13.29 ?  60   ALA   B C    1 
ATOM   4705 O  O    . ALA   B 1 60  ? 56.431 -11.826 1.692   1.00 13.92 ?  60   ALA   B O    1 
ATOM   4706 C  CB   . ALA   B 1 60  ? 58.571 -12.169 -0.723  1.00 15.28 ?  60   ALA   B CB   1 
ATOM   4707 H  H    . ALA   B 1 60  ? 59.294 -14.385 0.003   1.00 16.71 ?  60   ALA   B H    1 
ATOM   4708 H  HA   . ALA   B 1 60  ? 58.867 -12.166 1.302   1.00 17.03 ?  60   ALA   B HA   1 
ATOM   4709 H  HB1  . ALA   B 1 60  ? 58.174 -11.288 -0.750  1.00 18.33 ?  60   ALA   B HB1  1 
ATOM   4710 H  HB2  . ALA   B 1 60  ? 59.520 -12.113 -0.929  1.00 18.33 ?  60   ALA   B HB2  1 
ATOM   4711 H  HB3  . ALA   B 1 60  ? 58.132 -12.754 -1.360  1.00 18.33 ?  60   ALA   B HB3  1 
ATOM   4712 N  N    . MET   B 1 61  ? 56.223 -13.845 0.718   1.00 12.59 ?  61   MET   B N    1 
ATOM   4713 C  CA   . MET   B 1 61  ? 54.830 -13.969 1.120   1.00 12.24 ?  61   MET   B CA   1 
ATOM   4714 C  C    . MET   B 1 61  ? 54.696 -13.981 2.642   1.00 12.55 ?  61   MET   B C    1 
ATOM   4715 O  O    . MET   B 1 61  ? 53.793 -13.345 3.199   1.00 12.54 ?  61   MET   B O    1 
ATOM   4716 C  CB   . MET   B 1 61  ? 54.251 -15.237 0.493   1.00 12.34 ?  61   MET   B CB   1 
ATOM   4717 C  CG   . MET   B 1 61  ? 52.817 -15.534 0.917   1.00 12.51 ?  61   MET   B CG   1 
ATOM   4718 S  SD   . MET   B 1 61  ? 52.169 -17.027 0.138   1.00 12.84 ?  61   MET   B SD   1 
ATOM   4719 C  CE   . MET   B 1 61  ? 51.949 -16.433 -1.532  1.00 13.68 ?  61   MET   B CE   1 
ATOM   4720 H  H    . MET   B 1 61  ? 56.522 -14.507 0.249   1.00 15.10 ?  61   MET   B H    1 
ATOM   4721 H  HA   . MET   B 1 61  ? 54.333 -13.217 0.763   1.00 14.68 ?  61   MET   B HA   1 
ATOM   4722 H  HB2  . MET   B 1 61  ? 54.259 -15.146 -0.474  1.00 14.80 ?  61   MET   B HB2  1 
ATOM   4723 H  HB3  . MET   B 1 61  ? 54.801 -15.996 0.751   1.00 14.80 ?  61   MET   B HB3  1 
ATOM   4724 H  HG2  . MET   B 1 61  ? 52.790 -15.670 1.879   1.00 15.01 ?  61   MET   B HG2  1 
ATOM   4725 H  HG3  . MET   B 1 61  ? 52.251 -14.793 0.667   1.00 15.01 ?  61   MET   B HG3  1 
ATOM   4726 H  HE1  . MET   B 1 61  ? 51.536 -17.127 -2.062  1.00 16.41 ?  61   MET   B HE1  1 
ATOM   4727 H  HE2  . MET   B 1 61  ? 51.385 -15.643 -1.514  1.00 16.41 ?  61   MET   B HE2  1 
ATOM   4728 H  HE3  . MET   B 1 61  ? 52.820 -16.205 -1.902  1.00 16.41 ?  61   MET   B HE3  1 
ATOM   4729 N  N    . GLN   B 1 62  ? 55.576 -14.702 3.339   1.00 12.25 ?  62   GLN   B N    1 
ATOM   4730 C  CA   . GLN   B 1 62  ? 55.470 -14.760 4.793   1.00 12.73 ?  62   GLN   B CA   1 
ATOM   4731 C  C    . GLN   B 1 62  ? 55.754 -13.407 5.429   1.00 13.14 ?  62   GLN   B C    1 
ATOM   4732 O  O    . GLN   B 1 62  ? 55.076 -13.011 6.383   1.00 13.49 ?  62   GLN   B O    1 
ATOM   4733 C  CB   . GLN   B 1 62  ? 56.415 -15.818 5.360   1.00 13.12 ?  62   GLN   B CB   1 
ATOM   4734 C  CG   . GLN   B 1 62  ? 56.191 -16.085 6.836   1.00 13.12 ?  62   GLN   B CG   1 
ATOM   4735 C  CD   . GLN   B 1 62  ? 54.819 -16.679 7.074   1.00 13.01 ?  62   GLN   B CD   1 
ATOM   4736 O  OE1  . GLN   B 1 62  ? 54.564 -17.825 6.708   1.00 13.31 ?  62   GLN   B OE1  1 
ATOM   4737 N  NE2  . GLN   B 1 62  ? 53.911 -15.891 7.644   1.00 13.37 ?  62   GLN   B NE2  1 
ATOM   4738 H  H    . GLN   B 1 62  ? 56.222 -15.158 2.998   1.00 14.69 ?  62   GLN   B H    1 
ATOM   4739 H  HA   . GLN   B 1 62  ? 54.563 -15.012 5.025   1.00 15.27 ?  62   GLN   B HA   1 
ATOM   4740 H  HB2  . GLN   B 1 62  ? 56.281 -16.653 4.881   1.00 15.74 ?  62   GLN   B HB2  1 
ATOM   4741 H  HB3  . GLN   B 1 62  ? 57.331 -15.518 5.247   1.00 15.74 ?  62   GLN   B HB3  1 
ATOM   4742 H  HG2  . GLN   B 1 62  ? 56.856 -16.721 7.150   1.00 15.74 ?  62   GLN   B HG2  1 
ATOM   4743 H  HG3  . GLN   B 1 62  ? 56.258 -15.257 7.331   1.00 15.74 ?  62   GLN   B HG3  1 
ATOM   4744 H  HE21 . GLN   B 1 62  ? 54.119 -15.090 7.873   1.00 16.03 ?  62   GLN   B HE21 1 
ATOM   4745 H  HE22 . GLN   B 1 62  ? 53.119 -16.191 7.793   1.00 16.03 ?  62   GLN   B HE22 1 
ATOM   4746 N  N    . VAL   B 1 63  ? 56.772 -12.697 4.939   1.00 13.66 ?  63   VAL   B N    1 
ATOM   4747 C  CA   . VAL   B 1 63  ? 57.078 -11.381 5.494   1.00 14.81 ?  63   VAL   B CA   1 
ATOM   4748 C  C    . VAL   B 1 63  ? 55.886 -10.449 5.316   1.00 13.66 ?  63   VAL   B C    1 
ATOM   4749 O  O    . VAL   B 1 63  ? 55.472 -9.750  6.249   1.00 14.74 ?  63   VAL   B O    1 
ATOM   4750 C  CB   . VAL   B 1 63  ? 58.362 -10.820 4.861   1.00 16.11 ?  63   VAL   B CB   1 
ATOM   4751 C  CG1  . VAL   B 1 63  ? 58.586 -9.382  5.307   1.00 16.71 ?  63   VAL   B CG1  1 
ATOM   4752 C  CG2  . VAL   B 1 63  ? 59.543 -11.700 5.242   1.00 16.61 ?  63   VAL   B CG2  1 
ATOM   4753 H  H    . VAL   B 1 63  ? 57.288 -12.951 4.296   1.00 16.38 ?  63   VAL   B H    1 
ATOM   4754 H  HA   . VAL   B 1 63  ? 57.238 -11.479 6.443   1.00 17.76 ?  63   VAL   B HA   1 
ATOM   4755 H  HB   . VAL   B 1 63  ? 58.278 -10.834 3.896   1.00 19.33 ?  63   VAL   B HB   1 
ATOM   4756 H  HG11 . VAL   B 1 63  ? 59.502 -9.135  5.116   1.00 20.04 ?  63   VAL   B HG11 1 
ATOM   4757 H  HG12 . VAL   B 1 63  ? 57.977 -8.805  4.822   1.00 20.04 ?  63   VAL   B HG12 1 
ATOM   4758 H  HG13 . VAL   B 1 63  ? 58.416 -9.320  6.260   1.00 20.04 ?  63   VAL   B HG13 1 
ATOM   4759 H  HG21 . VAL   B 1 63  ? 60.355 -11.322 4.867   1.00 19.92 ?  63   VAL   B HG21 1 
ATOM   4760 H  HG22 . VAL   B 1 63  ? 59.615 -11.732 6.212   1.00 19.92 ?  63   VAL   B HG22 1 
ATOM   4761 H  HG23 . VAL   B 1 63  ? 59.404 -12.594 4.894   1.00 19.92 ?  63   VAL   B HG23 1 
ATOM   4762 N  N    . GLU   B 1 64  ? 55.322 -10.427 4.108   1.00 13.44 ?  64   GLU   B N    1 
ATOM   4763 C  CA   . GLU   B 1 64  ? 54.151 -9.594  3.838   1.00 13.07 ?  64   GLU   B CA   1 
ATOM   4764 C  C    . GLU   B 1 64  ? 52.973 -9.999  4.717   1.00 12.81 ?  64   GLU   B C    1 
ATOM   4765 O  O    . GLU   B 1 64  ? 52.229 -9.142  5.222   1.00 13.56 ?  64   GLU   B O    1 
ATOM   4766 C  CB   . GLU   B 1 64  ? 53.783 -9.745  2.363   1.00 13.09 ?  64   GLU   B CB   1 
ATOM   4767 C  CG   . GLU   B 1 64  ? 52.517 -9.010  1.937   1.00 13.13 ?  64   GLU   B CG   1 
ATOM   4768 C  CD   . GLU   B 1 64  ? 51.974 -9.508  0.605   1.00 14.12 ?  64   GLU   B CD   1 
ATOM   4769 O  OE1  . GLU   B 1 64  ? 52.164 -10.712 0.283   1.00 14.95 ?  64   GLU   B OE1  1 
ATOM   4770 O  OE2  . GLU   B 1 64  ? 51.347 -8.688  -0.117  1.00 15.02 -1 64   GLU   B OE2  1 
ATOM   4771 H  H    . GLU   B 1 64  ? 55.608 -10.872 3.427   1.00 16.12 ?  64   GLU   B H    1 
ATOM   4772 H  HA   . GLU   B 1 64  ? 54.365 -8.665  4.011   1.00 15.68 ?  64   GLU   B HA   1 
ATOM   4773 H  HB2  . GLU   B 1 64  ? 54.513 -9.396  1.822   1.00 15.70 ?  64   GLU   B HB2  1 
ATOM   4774 H  HB3  . GLU   B 1 64  ? 53.657 -10.684 2.169   1.00 15.70 ?  64   GLU   B HB3  1 
ATOM   4775 H  HG2  . GLU   B 1 64  ? 51.821 -9.138  2.605   1.00 15.75 ?  64   GLU   B HG2  1 
ATOM   4776 H  HG3  . GLU   B 1 64  ? 52.714 -8.063  1.851   1.00 15.75 ?  64   GLU   B HG3  1 
ATOM   4777 N  N    . SER   B 1 65  ? 52.789 -11.309 4.902   1.00 12.28 ?  65   SER   B N    1 
ATOM   4778 C  CA   . SER   B 1 65  ? 51.681 -11.817 5.699   1.00 12.62 ?  65   SER   B CA   1 
ATOM   4779 C  C    . SER   B 1 65  ? 51.812 -11.418 7.162   1.00 12.71 ?  65   SER   B C    1 
ATOM   4780 O  O    . SER   B 1 65  ? 50.812 -11.049 7.795   1.00 13.29 ?  65   SER   B O    1 
ATOM   4781 C  CB   . SER   B 1 65  ? 51.603 -13.340 5.561   1.00 12.71 ?  65   SER   B CB   1 
ATOM   4782 O  OG   . SER   B 1 65  ? 51.245 -13.728 4.241   1.00 12.97 ?  65   SER   B OG   1 
ATOM   4783 H  H    . SER   B 1 65  ? 53.301 -11.929 4.579   1.00 14.73 ?  65   SER   B H    1 
ATOM   4784 H  HA   . SER   B 1 65  ? 50.853 -11.447 5.360   1.00 15.13 ?  65   SER   B HA   1 
ATOM   4785 H  HB2  . SER   B 1 65  ? 52.465 -13.724 5.776   1.00 15.25 ?  65   SER   B HB2  1 
ATOM   4786 H  HB3  . SER   B 1 65  ? 50.930 -13.677 6.177   1.00 15.25 ?  65   SER   B HB3  1 
ATOM   4787 H  HG   . SER   B 1 65  ? 51.819 -13.432 3.693   1.00 15.56 ?  65   SER   B HG   1 
ATOM   4788 N  N    . ASP   B 1 66  ? 53.023 -11.514 7.728   1.00 13.03 ?  66   ASP   B N    1 
ATOM   4789 C  CA   . ASP   B 1 66  ? 53.209 -11.132 9.126   1.00 13.17 ?  66   ASP   B CA   1 
ATOM   4790 C  C    . ASP   B 1 66  ? 52.899 -9.653  9.331   1.00 13.59 ?  66   ASP   B C    1 
ATOM   4791 O  O    . ASP   B 1 66  ? 52.324 -9.262  10.355  1.00 13.85 ?  66   ASP   B O    1 
ATOM   4792 C  CB   . ASP   B 1 66  ? 54.642 -11.436 9.568   1.00 14.72 ?  66   ASP   B CB   1 
ATOM   4793 C  CG   . ASP   B 1 66  ? 54.915 -12.924 9.725   1.00 16.41 ?  66   ASP   B CG   1 
ATOM   4794 O  OD1  . ASP   B 1 66  ? 53.963 -13.732 9.658   1.00 17.06 ?  66   ASP   B OD1  1 
ATOM   4795 O  OD2  . ASP   B 1 66  ? 56.097 -13.290 9.928   1.00 19.17 -1 66   ASP   B OD2  1 
ATOM   4796 H  H    . ASP   B 1 66  ? 53.731 -11.801 7.335   1.00 15.62 ?  66   ASP   B H    1 
ATOM   4797 H  HA   . ASP   B 1 66  ? 52.605 -11.644 9.685   1.00 15.79 ?  66   ASP   B HA   1 
ATOM   4798 H  HB2  . ASP   B 1 66  ? 55.258 -11.091 8.902   1.00 17.65 ?  66   ASP   B HB2  1 
ATOM   4799 H  HB3  . ASP   B 1 66  ? 54.806 -11.005 10.424  1.00 17.65 ?  66   ASP   B HB3  1 
ATOM   4800 N  N    . ASP   B 1 67  ? 53.275 -8.812  8.367   1.00 13.14 ?  67   ASP   B N    1 
ATOM   4801 C  CA   . ASP   B 1 67  ? 52.932 -7.400  8.457   1.00 13.76 ?  67   ASP   B CA   1 
ATOM   4802 C  C    . ASP   B 1 67  ? 51.421 -7.193  8.372   1.00 13.80 ?  67   ASP   B C    1 
ATOM   4803 O  O    . ASP   B 1 67  ? 50.858 -6.381  9.116   1.00 14.65 ?  67   ASP   B O    1 
ATOM   4804 C  CB   . ASP   B 1 67  ? 53.653 -6.631  7.359   1.00 15.12 ?  67   ASP   B CB   1 
ATOM   4805 C  CG   . ASP   B 1 67  ? 53.243 -5.189  7.324   1.00 16.30 ?  67   ASP   B CG   1 
ATOM   4806 O  OD1  . ASP   B 1 67  ? 53.749 -4.391  8.144   1.00 17.53 ?  67   ASP   B OD1  1 
ATOM   4807 O  OD2  . ASP   B 1 67  ? 52.374 -4.875  6.495   1.00 17.37 -1 67   ASP   B OD2  1 
ATOM   4808 H  H    . ASP   B 1 67  ? 53.729 -9.031  7.670   1.00 15.77 ?  67   ASP   B H    1 
ATOM   4809 H  HA   . ASP   B 1 67  ? 53.235 -7.054  9.310   1.00 16.51 ?  67   ASP   B HA   1 
ATOM   4810 H  HB2  . ASP   B 1 67  ? 54.611 -6.667  7.519   1.00 18.13 ?  67   ASP   B HB2  1 
ATOM   4811 H  HB3  . ASP   B 1 67  ? 53.450 -7.037  6.498   1.00 18.13 ?  67   ASP   B HB3  1 
ATOM   4812 N  N    . TYR   B 1 68  ? 50.743 -7.926  7.480   1.00 13.66 ?  68   TYR   B N    1 
ATOM   4813 C  CA   . TYR   B 1 68  ? 49.287 -7.842  7.406   1.00 14.31 ?  68   TYR   B CA   1 
ATOM   4814 C  C    . TYR   B 1 68  ? 48.653 -8.188  8.747   1.00 13.81 ?  68   TYR   B C    1 
ATOM   4815 O  O    . TYR   B 1 68  ? 47.719 -7.512  9.195   1.00 14.88 ?  68   TYR   B O    1 
ATOM   4816 C  CB   . TYR   B 1 68  ? 48.756 -8.775  6.313   1.00 15.27 ?  68   TYR   B CB   1 
ATOM   4817 C  CG   . TYR   B 1 68  ? 47.249 -8.927  6.372   1.00 16.52 ?  68   TYR   B CG   1 
ATOM   4818 C  CD1  . TYR   B 1 68  ? 46.655 -9.879  7.199   1.00 17.09 ?  68   TYR   B CD1  1 
ATOM   4819 C  CD2  . TYR   B 1 68  ? 46.422 -8.095  5.640   1.00 17.40 ?  68   TYR   B CD2  1 
ATOM   4820 C  CE1  . TYR   B 1 68  ? 45.290 -10.002 7.285   1.00 18.34 ?  68   TYR   B CE1  1 
ATOM   4821 C  CE2  . TYR   B 1 68  ? 45.043 -8.224  5.712   1.00 18.12 ?  68   TYR   B CE2  1 
ATOM   4822 C  CZ   . TYR   B 1 68  ? 44.497 -9.173  6.542   1.00 18.39 ?  68   TYR   B CZ   1 
ATOM   4823 O  OH   . TYR   B 1 68  ? 43.131 -9.292  6.634   1.00 19.36 ?  68   TYR   B OH   1 
ATOM   4824 H  H    . TYR   B 1 68  ? 51.100 -8.479  6.921   1.00 16.39 ?  68   TYR   B H    1 
ATOM   4825 H  HA   . TYR   B 1 68  ? 49.036 -6.936  7.183   1.00 17.17 ?  68   TYR   B HA   1 
ATOM   4826 H  HB2  . TYR   B 1 68  ? 48.984 -8.408  5.448   1.00 18.32 ?  68   TYR   B HB2  1 
ATOM   4827 H  HB3  . TYR   B 1 68  ? 49.150 -9.653  6.423   1.00 18.32 ?  68   TYR   B HB3  1 
ATOM   4828 H  HD1  . TYR   B 1 68  ? 47.194 -10.443 7.708   1.00 20.50 ?  68   TYR   B HD1  1 
ATOM   4829 H  HD2  . TYR   B 1 68  ? 46.795 -7.448  5.091   1.00 20.87 ?  68   TYR   B HD2  1 
ATOM   4830 H  HE1  . TYR   B 1 68  ? 44.908 -10.653 7.835   1.00 22.00 ?  68   TYR   B HE1  1 
ATOM   4831 H  HE2  . TYR   B 1 68  ? 44.490 -7.662  5.219   1.00 21.74 ?  68   TYR   B HE2  1 
ATOM   4832 H  HH   . TYR   B 1 68  ? 42.745 -8.743  6.122   1.00 23.22 ?  68   TYR   B HH   1 
ATOM   4833 N  N    . ILE   B 1 69  ? 49.133 -9.258  9.389   1.00 13.84 ?  69   ILE   B N    1 
ATOM   4834 C  CA   . ILE   B 1 69  ? 48.574 -9.687  10.668  1.00 14.24 ?  69   ILE   B CA   1 
ATOM   4835 C  C    . ILE   B 1 69  ? 48.825 -8.644  11.745  1.00 13.88 ?  69   ILE   B C    1 
ATOM   4836 O  O    . ILE   B 1 69  ? 47.952 -8.366  12.573  1.00 14.39 ?  69   ILE   B O    1 
ATOM   4837 C  CB   . ILE   B 1 69  ? 49.144 -11.065 11.058  1.00 15.31 ?  69   ILE   B CB   1 
ATOM   4838 C  CG1  . ILE   B 1 69  ? 48.616 -12.164 10.125  1.00 15.72 ?  69   ILE   B CG1  1 
ATOM   4839 C  CG2  . ILE   B 1 69  ? 48.839 -11.388 12.511  1.00 16.60 ?  69   ILE   B CG2  1 
ATOM   4840 C  CD1  . ILE   B 1 69  ? 47.126 -12.465 10.270  1.00 15.94 ?  69   ILE   B CD1  1 
ATOM   4841 H  H    . ILE   B 1 69  ? 49.779 -9.749  9.108   1.00 16.60 ?  69   ILE   B H    1 
ATOM   4842 H  HA   . ILE   B 1 69  ? 47.616 -9.782  10.574  1.00 17.08 ?  69   ILE   B HA   1 
ATOM   4843 H  HB   . ILE   B 1 69  ? 50.110 -11.029 10.960  1.00 18.37 ?  69   ILE   B HB   1 
ATOM   4844 H  HG12 . ILE   B 1 69  ? 48.774 -11.889 9.207   1.00 18.86 ?  69   ILE   B HG12 1 
ATOM   4845 H  HG13 . ILE   B 1 69  ? 49.104 -12.983 10.305  1.00 18.86 ?  69   ILE   B HG13 1 
ATOM   4846 H  HG21 . ILE   B 1 69  ? 48.984 -12.339 12.653  1.00 19.92 ?  69   ILE   B HG21 1 
ATOM   4847 H  HG22 . ILE   B 1 69  ? 49.429 -10.879 13.084  1.00 19.92 ?  69   ILE   B HG22 1 
ATOM   4848 H  HG23 . ILE   B 1 69  ? 47.914 -11.168 12.695  1.00 19.92 ?  69   ILE   B HG23 1 
ATOM   4849 H  HD11 . ILE   B 1 69  ? 46.890 -13.174 9.652   1.00 19.12 ?  69   ILE   B HD11 1 
ATOM   4850 H  HD12 . ILE   B 1 69  ? 46.947 -12.751 11.180  1.00 19.12 ?  69   ILE   B HD12 1 
ATOM   4851 H  HD13 . ILE   B 1 69  ? 46.617 -11.667 10.066  1.00 19.12 ?  69   ILE   B HD13 1 
ATOM   4852 N  N    . ALA   B 1 70  ? 50.023 -8.062  11.770  1.00 13.79 ?  70   ALA   B N    1 
ATOM   4853 C  CA   . ALA   B 1 70  ? 50.300 -7.021  12.754  1.00 13.55 ?  70   ALA   B CA   1 
ATOM   4854 C  C    . ALA   B 1 70  ? 49.305 -5.875  12.635  1.00 13.87 ?  70   ALA   B C    1 
ATOM   4855 O  O    . ALA   B 1 70  ? 48.861 -5.325  13.647  1.00 14.33 ?  70   ALA   B O    1 
ATOM   4856 C  CB   . ALA   B 1 70  ? 51.727 -6.505  12.591  1.00 14.50 ?  70   ALA   B CB   1 
ATOM   4857 H  H    . ALA   B 1 70  ? 50.673 -8.247  11.245  1.00 16.55 ?  70   ALA   B H    1 
ATOM   4858 H  HA   . ALA   B 1 70  ? 50.222 -7.395  13.648  1.00 16.26 ?  70   ALA   B HA   1 
ATOM   4859 H  HB1  . ALA   B 1 70  ? 51.909 -5.846  13.281  1.00 17.40 ?  70   ALA   B HB1  1 
ATOM   4860 H  HB2  . ALA   B 1 70  ? 52.346 -7.247  12.676  1.00 17.40 ?  70   ALA   B HB2  1 
ATOM   4861 H  HB3  . ALA   B 1 70  ? 51.819 -6.098  11.714  1.00 17.40 ?  70   ALA   B HB3  1 
ATOM   4862 N  N    . THR   B 1 71  ? 48.936 -5.514  11.409  1.00 14.37 ?  71   THR   B N    1 
ATOM   4863 C  CA   . THR   B 1 71  ? 48.045 -4.379  11.197  1.00 15.58 ?  71   THR   B CA   1 
ATOM   4864 C  C    . THR   B 1 71  ? 46.579 -4.744  11.409  1.00 16.21 ?  71   THR   B C    1 
ATOM   4865 O  O    . THR   B 1 71  ? 45.802 -3.922  11.914  1.00 17.91 ?  71   THR   B O    1 
ATOM   4866 C  CB   . THR   B 1 71  ? 48.267 -3.811  9.794   1.00 17.40 ?  71   THR   B CB   1 
ATOM   4867 O  OG1  . THR   B 1 71  ? 49.597 -3.288  9.701   1.00 19.45 ?  71   THR   B OG1  1 
ATOM   4868 C  CG2  . THR   B 1 71  ? 47.262 -2.713  9.476   1.00 18.16 ?  71   THR   B CG2  1 
ATOM   4869 H  H    . THR   B 1 71  ? 49.188 -5.912  10.688  1.00 17.24 ?  71   THR   B H    1 
ATOM   4870 H  HA   . THR   B 1 71  ? 48.273 -3.685  11.833  1.00 18.69 ?  71   THR   B HA   1 
ATOM   4871 H  HB   . THR   B 1 71  ? 48.168 -4.517  9.137   1.00 20.87 ?  71   THR   B HB   1 
ATOM   4872 H  HG1  . THR   B 1 71  ? 49.730 -2.958  8.936   1.00 23.34 ?  71   THR   B HG1  1 
ATOM   4873 H  HG21 . THR   B 1 71  ? 47.568 -2.196  8.713   1.00 21.79 ?  71   THR   B HG21 1 
ATOM   4874 H  HG22 . THR   B 1 71  ? 46.401 -3.101  9.268   1.00 21.79 ?  71   THR   B HG22 1 
ATOM   4875 H  HG23 . THR   B 1 71  ? 47.171 -2.119  10.238  1.00 21.79 ?  71   THR   B HG23 1 
ATOM   4876 N  N    . ASN   B 1 72  ? 46.182 -5.962  11.035  1.00 15.65 ?  72   ASN   B N    1 
ATOM   4877 C  CA   . ASN   B 1 72  ? 44.778 -6.318  10.908  1.00 15.94 ?  72   ASN   B CA   1 
ATOM   4878 C  C    . ASN   B 1 72  ? 44.308 -7.416  11.849  1.00 16.45 ?  72   ASN   B C    1 
ATOM   4879 O  O    . ASN   B 1 72  ? 43.092 -7.572  12.020  1.00 17.66 ?  72   ASN   B O    1 
ATOM   4880 C  CB   . ASN   B 1 72  ? 44.475 -6.745  9.464   1.00 16.71 ?  72   ASN   B CB   1 
ATOM   4881 C  CG   . ASN   B 1 72  ? 44.740 -5.637  8.471   1.00 17.87 ?  72   ASN   B CG   1 
ATOM   4882 O  OD1  . ASN   B 1 72  ? 45.751 -5.640  7.766   1.00 19.24 ?  72   ASN   B OD1  1 
ATOM   4883 N  ND2  . ASN   B 1 72  ? 43.856 -4.660  8.438   1.00 19.42 ?  72   ASN   B ND2  1 
ATOM   4884 H  H    . ASN   B 1 72  ? 46.723 -6.607  10.841  1.00 18.78 ?  72   ASN   B H    1 
ATOM   4885 H  HA   . ASN   B 1 72  ? 44.248 -5.530  11.093  1.00 19.13 ?  72   ASN   B HA   1 
ATOM   4886 H  HB2  . ASN   B 1 72  ? 45.042 -7.500  9.230   1.00 20.04 ?  72   ASN   B HB2  1 
ATOM   4887 H  HB3  . ASN   B 1 72  ? 43.544 -6.993  9.395   1.00 20.04 ?  72   ASN   B HB3  1 
ATOM   4888 H  HD21 . ASN   B 1 72  ? 43.959 -4.006  7.890   1.00 23.30 ?  72   ASN   B HD21 1 
ATOM   4889 H  HD22 . ASN   B 1 72  ? 43.163 -4.691  8.947   1.00 23.30 ?  72   ASN   B HD22 1 
ATOM   4890 N  N    . GLY   B 1 73  ? 45.212 -8.165  12.469  1.00 16.21 ?  73   GLY   B N    1 
ATOM   4891 C  CA   . GLY   B 1 73  ? 44.817 -9.304  13.259  1.00 15.54 ?  73   GLY   B CA   1 
ATOM   4892 C  C    . GLY   B 1 73  ? 44.453 -10.484 12.386  1.00 14.16 ?  73   GLY   B C    1 
ATOM   4893 O  O    . GLY   B 1 73  ? 44.442 -10.396 11.157  1.00 14.32 ?  73   GLY   B O    1 
ATOM   4894 H  H    . GLY   B 1 73  ? 46.064 -8.026  12.450  1.00 19.44 ?  73   GLY   B H    1 
ATOM   4895 H  HA2  . GLY   B 1 73  ? 45.549 -9.563  13.844  1.00 18.64 ?  73   GLY   B HA2  1 
ATOM   4896 H  HA3  . GLY   B 1 73  ? 44.052 -9.074  13.807  1.00 18.64 ?  73   GLY   B HA3  1 
ATOM   4897 N  N    . PRO   B 1 74  ? 44.143 -11.612 13.016  1.00 14.56 ?  74   PRO   B N    1 
ATOM   4898 C  CA   . PRO   B 1 74  ? 43.904 -12.845 12.265  1.00 14.21 ?  74   PRO   B CA   1 
ATOM   4899 C  C    . PRO   B 1 74  ? 42.599 -12.795 11.484  1.00 13.66 ?  74   PRO   B C    1 
ATOM   4900 O  O    . PRO   B 1 74  ? 41.659 -12.061 11.808  1.00 15.02 ?  74   PRO   B O    1 
ATOM   4901 C  CB   . PRO   B 1 74  ? 43.844 -13.911 13.364  1.00 15.29 ?  74   PRO   B CB   1 
ATOM   4902 C  CG   . PRO   B 1 74  ? 43.379 -13.170 14.570  1.00 16.83 ?  74   PRO   B CG   1 
ATOM   4903 C  CD   . PRO   B 1 74  ? 44.038 -11.824 14.468  1.00 16.12 ?  74   PRO   B CD   1 
ATOM   4904 H  HA   . PRO   B 1 74  ? 44.649 -13.029 11.663  1.00 17.05 ?  74   PRO   B HA   1 
ATOM   4905 H  HB2  . PRO   B 1 74  ? 43.212 -14.602 13.111  1.00 18.35 ?  74   PRO   B HB2  1 
ATOM   4906 H  HB3  . PRO   B 1 74  ? 44.728 -14.286 13.505  1.00 18.35 ?  74   PRO   B HB3  1 
ATOM   4907 H  HG2  . PRO   B 1 74  ? 42.412 -13.083 14.546  1.00 20.19 ?  74   PRO   B HG2  1 
ATOM   4908 H  HG3  . PRO   B 1 74  ? 43.664 -13.636 15.370  1.00 20.19 ?  74   PRO   B HG3  1 
ATOM   4909 H  HD2  . PRO   B 1 74  ? 43.479 -11.140 14.875  1.00 19.33 ?  74   PRO   B HD2  1 
ATOM   4910 H  HD3  . PRO   B 1 74  ? 44.921 -11.845 14.872  1.00 19.33 ?  74   PRO   B HD3  1 
ATOM   4911 N  N    . LEU   B 1 75  ? 42.569 -13.597 10.424  1.00 12.94 ?  75   LEU   B N    1 
ATOM   4912 C  CA   . LEU   B 1 75  ? 41.354 -13.818 9.660   1.00 13.12 ?  75   LEU   B CA   1 
ATOM   4913 C  C    . LEU   B 1 75  ? 40.385 -14.681 10.466  1.00 13.62 ?  75   LEU   B C    1 
ATOM   4914 O  O    . LEU   B 1 75  ? 40.727 -15.240 11.509  1.00 14.54 ?  75   LEU   B O    1 
ATOM   4915 C  CB   . LEU   B 1 75  ? 41.681 -14.536 8.349   1.00 13.02 ?  75   LEU   B CB   1 
ATOM   4916 C  CG   . LEU   B 1 75  ? 42.521 -13.782 7.313   1.00 15.27 ?  75   LEU   B CG   1 
ATOM   4917 C  CD1  . LEU   B 1 75  ? 42.700 -14.609 6.045   1.00 16.62 ?  75   LEU   B CD1  1 
ATOM   4918 C  CD2  . LEU   B 1 75  ? 41.929 -12.438 6.984   1.00 18.52 ?  75   LEU   B CD2  1 
ATOM   4919 H  H    . LEU   B 1 75  ? 43.250 -14.031 10.121  1.00 15.52 ?  75   LEU   B H    1 
ATOM   4920 H  HA   . LEU   B 1 75  ? 40.927 -12.972 9.459   1.00 15.74 ?  75   LEU   B HA   1 
ATOM   4921 H  HB2  . LEU   B 1 75  ? 42.164 -15.351 8.564   1.00 15.62 ?  75   LEU   B HB2  1 
ATOM   4922 H  HB3  . LEU   B 1 75  ? 40.845 -14.771 7.915   1.00 15.62 ?  75   LEU   B HB3  1 
ATOM   4923 H  HG   . LEU   B 1 75  ? 43.404 -13.632 7.683   1.00 18.32 ?  75   LEU   B HG   1 
ATOM   4924 H  HD11 . LEU   B 1 75  ? 43.242 -14.107 5.410   1.00 19.93 ?  75   LEU   B HD11 1 
ATOM   4925 H  HD12 . LEU   B 1 75  ? 43.148 -15.443 6.266   1.00 19.93 ?  75   LEU   B HD12 1 
ATOM   4926 H  HD13 . LEU   B 1 75  ? 41.831 -14.795 5.657   1.00 19.93 ?  75   LEU   B HD13 1 
ATOM   4927 H  HD21 . LEU   B 1 75  ? 42.428 -12.043 6.255   1.00 22.22 ?  75   LEU   B HD21 1 
ATOM   4928 H  HD22 . LEU   B 1 75  ? 41.002 -12.558 6.729   1.00 22.22 ?  75   LEU   B HD22 1 
ATOM   4929 H  HD23 . LEU   B 1 75  ? 41.985 -11.871 7.770   1.00 22.22 ?  75   LEU   B HD23 1 
ATOM   4930 N  N    . LYS   B 1 76  ? 39.155 -14.782 9.961   1.00 15.00 ?  76   LYS   B N    1 
ATOM   4931 C  CA   . LYS   B 1 76  ? 38.172 -15.746 10.439  1.00 15.95 ?  76   LYS   B CA   1 
ATOM   4932 C  C    . LYS   B 1 76  ? 38.263 -17.013 9.596   1.00 14.28 ?  76   LYS   B C    1 
ATOM   4933 O  O    . LYS   B 1 76  ? 38.532 -16.946 8.397   1.00 14.07 ?  76   LYS   B O    1 
ATOM   4934 C  CB   . LYS   B 1 76  ? 36.753 -15.180 10.261  1.00 18.48 ?  76   LYS   B CB   1 
ATOM   4935 C  CG   . LYS   B 1 76  ? 36.474 -13.797 10.874  1.00 20.98 ?  76   LYS   B CG   1 
ATOM   4936 C  CD   . LYS   B 1 76  ? 35.072 -13.271 10.502  1.00 22.65 ?  76   LYS   B CD   1 
ATOM   4937 C  CE   . LYS   B 1 76  ? 34.783 -11.925 11.149  1.00 24.62 ?  76   LYS   B CE   1 
ATOM   4938 N  NZ   . LYS   B 1 76  ? 33.518 -11.304 10.657  1.00 25.17 ?  76   LYS   B NZ   1 
ATOM   4939 H  H    . LYS   B 1 76  ? 38.863 -14.294 9.318   1.00 18.00 ?  76   LYS   B H    1 
ATOM   4940 H  HA   . LYS   B 1 76  ? 38.323 -15.965 11.373  1.00 19.14 ?  76   LYS   B HA   1 
ATOM   4941 H  HB2  . LYS   B 1 76  ? 36.571 -15.112 9.310   1.00 22.17 ?  76   LYS   B HB2  1 
ATOM   4942 H  HB3  . LYS   B 1 76  ? 36.125 -15.800 10.662  1.00 22.17 ?  76   LYS   B HB3  1 
ATOM   4943 H  HG2  . LYS   B 1 76  ? 36.528 -13.858 11.841  1.00 25.17 ?  76   LYS   B HG2  1 
ATOM   4944 H  HG3  . LYS   B 1 76  ? 37.132 -13.162 10.544  1.00 25.17 ?  76   LYS   B HG3  1 
ATOM   4945 H  HD2  . LYS   B 1 76  ? 35.016 -13.161 9.539   1.00 27.18 ?  76   LYS   B HD2  1 
ATOM   4946 H  HD3  . LYS   B 1 76  ? 34.402 -13.903 10.806  1.00 27.18 ?  76   LYS   B HD3  1 
ATOM   4947 H  HE2  . LYS   B 1 76  ? 34.704 -12.046 12.108  1.00 29.54 ?  76   LYS   B HE2  1 
ATOM   4948 H  HE3  . LYS   B 1 76  ? 35.512 -11.316 10.951  1.00 29.54 ?  76   LYS   B HE3  1 
ATOM   4949 H  HZ1  . LYS   B 1 76  ? 33.386 -10.519 11.060  1.00 30.20 ?  76   LYS   B HZ1  1 
ATOM   4950 H  HZ2  . LYS   B 1 76  ? 33.564 -11.171 9.778   1.00 30.20 ?  76   LYS   B HZ2  1 
ATOM   4951 H  HZ3  . LYS   B 1 76  ? 32.827 -11.836 10.833  1.00 30.20 ?  76   LYS   B HZ3  1 
ATOM   4952 N  N    . VAL   B 1 77  ? 38.017 -18.172 10.220  1.00 14.95 ?  77   VAL   B N    1 
ATOM   4953 C  CA   . VAL   B 1 77  ? 37.803 -19.378 9.428   1.00 14.83 ?  77   VAL   B CA   1 
ATOM   4954 C  C    . VAL   B 1 77  ? 36.609 -19.137 8.516   1.00 13.68 ?  77   VAL   B C    1 
ATOM   4955 O  O    . VAL   B 1 77  ? 35.546 -18.681 8.963   1.00 14.19 ?  77   VAL   B O    1 
ATOM   4956 C  CB   . VAL   B 1 77  ? 37.616 -20.611 10.326  1.00 16.21 ?  77   VAL   B CB   1 
ATOM   4957 C  CG1  . VAL   B 1 77  ? 37.323 -21.835 9.466   1.00 17.05 ?  77   VAL   B CG1  1 
ATOM   4958 C  CG2  . VAL   B 1 77  ? 38.863 -20.850 11.183  1.00 17.91 ?  77   VAL   B CG2  1 
ATOM   4959 H  H    . VAL   B 1 77  ? 37.974 -18.284 11.067  1.00 17.94 ?  77   VAL   B H    1 
ATOM   4960 H  HA   . VAL   B 1 77  ? 38.580 -19.531 8.866   1.00 17.79 ?  77   VAL   B HA   1 
ATOM   4961 H  HB   . VAL   B 1 77  ? 36.859 -20.465 10.915  1.00 19.45 ?  77   VAL   B HB   1 
ATOM   4962 H  HG11 . VAL   B 1 77  ? 37.394 -22.631 10.019  1.00 20.45 ?  77   VAL   B HG11 1 
ATOM   4963 H  HG12 . VAL   B 1 77  ? 36.423 -21.768 9.106   1.00 20.45 ?  77   VAL   B HG12 1 
ATOM   4964 H  HG13 . VAL   B 1 77  ? 37.967 -21.878 8.744   1.00 20.45 ?  77   VAL   B HG13 1 
ATOM   4965 H  HG21 . VAL   B 1 77  ? 38.727 -21.649 11.711  1.00 21.49 ?  77   VAL   B HG21 1 
ATOM   4966 H  HG22 . VAL   B 1 77  ? 39.626 -20.959 10.597  1.00 21.49 ?  77   VAL   B HG22 1 
ATOM   4967 H  HG23 . VAL   B 1 77  ? 38.992 -20.083 11.762  1.00 21.49 ?  77   VAL   B HG23 1 
ATOM   4968 N  N    . GLY   B 1 78  ? 36.792 -19.416 7.225   1.00 13.08 ?  78   GLY   B N    1 
ATOM   4969 C  CA   . GLY   B 1 78  ? 35.819 -19.089 6.210   1.00 13.04 ?  78   GLY   B CA   1 
ATOM   4970 C  C    . GLY   B 1 78  ? 36.061 -17.768 5.520   1.00 12.98 ?  78   GLY   B C    1 
ATOM   4971 O  O    . GLY   B 1 78  ? 35.384 -17.479 4.530   1.00 13.52 ?  78   GLY   B O    1 
ATOM   4972 H  H    . GLY   B 1 78  ? 37.497 -19.801 6.912   1.00 15.69 ?  78   GLY   B H    1 
ATOM   4973 H  HA2  . GLY   B 1 78  ? 35.820 -19.783 5.535   1.00 15.64 ?  78   GLY   B HA2  1 
ATOM   4974 H  HA3  . GLY   B 1 78  ? 34.939 -19.057 6.613   1.00 15.64 ?  78   GLY   B HA3  1 
ATOM   4975 N  N    . GLY   B 1 79  ? 37.009 -16.961 6.008   1.00 12.91 ?  79   GLY   B N    1 
ATOM   4976 C  CA   . GLY   B 1 79  ? 37.308 -15.666 5.434   1.00 12.57 ?  79   GLY   B CA   1 
ATOM   4977 C  C    . GLY   B 1 79  ? 38.541 -15.683 4.544   1.00 12.11 ?  79   GLY   B C    1 
ATOM   4978 O  O    . GLY   B 1 79  ? 39.153 -16.720 4.298   1.00 12.72 ?  79   GLY   B O    1 
ATOM   4979 H  H    . GLY   B 1 79  ? 37.507 -17.158 6.680   1.00 15.49 ?  79   GLY   B H    1 
ATOM   4980 H  HA2  . GLY   B 1 79  ? 36.555 -15.365 4.902   1.00 15.07 ?  79   GLY   B HA2  1 
ATOM   4981 H  HA3  . GLY   B 1 79  ? 37.457 -15.026 6.145   1.00 15.07 ?  79   GLY   B HA3  1 
ATOM   4982 N  N    . SER   B 1 80  ? 38.904 -14.488 4.066   1.00 12.22 ?  80   SER   B N    1 
ATOM   4983 C  CA   . SER   B 1 80  ? 40.015 -14.360 3.134   1.00 12.13 ?  80   SER   B CA   1 
ATOM   4984 C  C    . SER   B 1 80  ? 40.592 -12.953 3.194   1.00 11.71 ?  80   SER   B C    1 
ATOM   4985 O  O    . SER   B 1 80  ? 39.973 -12.023 3.723   1.00 12.75 ?  80   SER   B O    1 
ATOM   4986 C  CB   . SER   B 1 80  ? 39.572 -14.659 1.698   1.00 12.02 ?  80   SER   B CB   1 
ATOM   4987 O  OG   . SER   B 1 80  ? 38.733 -13.637 1.190   1.00 13.25 ?  80   SER   B OG   1 
ATOM   4988 H  H    . SER   B 1 80  ? 38.523 -13.743 4.265   1.00 14.65 ?  80   SER   B H    1 
ATOM   4989 H  HA   . SER   B 1 80  ? 40.705 -14.987 3.383   1.00 14.55 ?  80   SER   B HA   1 
ATOM   4990 H  HB2  . SER   B 1 80  ? 40.354 -14.727 1.128   1.00 14.41 ?  80   SER   B HB2  1 
ATOM   4991 H  HB3  . SER   B 1 80  ? 39.080 -15.498 1.684   1.00 14.41 ?  80   SER   B HB3  1 
ATOM   4992 H  HG   . SER   B 1 80  ? 38.046 -13.563 1.679   1.00 15.90 ?  80   SER   B HG   1 
ATOM   4993 N  N    . CYS   B 1 81  ? 41.779 -12.805 2.610   1.00 11.71 ?  81   CYS   B N    1 
ATOM   4994 C  CA   . CYS   B 1 81  ? 42.321 -11.491 2.306   1.00 11.64 ?  81   CYS   B CA   1 
ATOM   4995 C  C    . CYS   B 1 81  ? 43.089 -11.573 0.998   1.00 11.00 ?  81   CYS   B C    1 
ATOM   4996 O  O    . CYS   B 1 81  ? 43.601 -12.633 0.618   1.00 12.02 ?  81   CYS   B O    1 
ATOM   4997 C  CB   . CYS   B 1 81  ? 43.205 -10.945 3.436   1.00 12.24 ?  81   CYS   B CB   1 
ATOM   4998 S  SG   . CYS   B 1 81  ? 44.723 -11.879 3.673   1.00 12.92 ?  81   CYS   B SG   1 
ATOM   4999 H  H    . CYS   B 1 81  ? 42.291 -13.456 2.370   1.00 14.05 ?  81   CYS   B H    1 
ATOM   5000 H  HA   . CYS   B 1 81  ? 41.587 -10.868 2.179   1.00 13.96 ?  81   CYS   B HA   1 
ATOM   5001 H  HB2  . CYS   B 1 81  ? 43.449 -10.028 3.236   1.00 14.68 ?  81   CYS   B HB2  1 
ATOM   5002 H  HB3  . CYS   B 1 81  ? 42.698 -10.970 4.270   1.00 14.68 ?  81   CYS   B HB3  1 
ATOM   5003 H  HG   . CYS   B 1 81  ? 45.346 -11.393 4.585   1.00 15.50 ?  81   CYS   B HG   1 
ATOM   5004 N  N    . VAL   B 1 82  ? 43.183 -10.430 0.324   1.00 11.30 ?  82   VAL   B N    1 
ATOM   5005 C  CA   . VAL   B 1 82  ? 43.943 -10.304 -0.914  1.00 11.59 ?  82   VAL   B CA   1 
ATOM   5006 C  C    . VAL   B 1 82  ? 45.285 -9.665  -0.598  1.00 11.90 ?  82   VAL   B C    1 
ATOM   5007 O  O    . VAL   B 1 82  ? 45.338 -8.548  -0.067  1.00 12.79 ?  82   VAL   B O    1 
ATOM   5008 C  CB   . VAL   B 1 82  ? 43.193 -9.461  -1.957  1.00 12.86 ?  82   VAL   B CB   1 
ATOM   5009 C  CG1  . VAL   B 1 82  ? 44.017 -9.328  -3.228  1.00 14.56 ?  82   VAL   B CG1  1 
ATOM   5010 C  CG2  . VAL   B 1 82  ? 41.823 -10.051 -2.244  1.00 14.01 ?  82   VAL   B CG2  1 
ATOM   5011 H  H    . VAL   B 1 82  ? 42.807 -9.690  0.571   1.00 13.56 ?  82   VAL   B H    1 
ATOM   5012 H  HA   . VAL   B 1 82  ? 44.098 -11.181 -1.288  1.00 13.90 ?  82   VAL   B HA   1 
ATOM   5013 H  HB   . VAL   B 1 82  ? 43.059 -8.568  -1.604  1.00 15.42 ?  82   VAL   B HB   1 
ATOM   5014 H  HG11 . VAL   B 1 82  ? 43.448 -8.995  -3.941  1.00 17.46 ?  82   VAL   B HG11 1 
ATOM   5015 H  HG12 . VAL   B 1 82  ? 44.747 -8.709  -3.074  1.00 17.46 ?  82   VAL   B HG12 1 
ATOM   5016 H  HG13 . VAL   B 1 82  ? 44.366 -10.201 -3.470  1.00 17.46 ?  82   VAL   B HG13 1 
ATOM   5017 H  HG21 . VAL   B 1 82  ? 41.390 -9.529  -2.941  1.00 16.80 ?  82   VAL   B HG21 1 
ATOM   5018 H  HG22 . VAL   B 1 82  ? 41.927 -10.969 -2.538  1.00 16.80 ?  82   VAL   B HG22 1 
ATOM   5019 H  HG23 . VAL   B 1 82  ? 41.289 -10.022 -1.434  1.00 16.80 ?  82   VAL   B HG23 1 
ATOM   5020 N  N    . LEU   B 1 83  ? 46.366 -10.351 -0.963  1.00 11.47 ?  83   LEU   B N    1 
ATOM   5021 C  CA   . LEU   B 1 83  ? 47.716 -9.836  -0.840  1.00 11.41 ?  83   LEU   B CA   1 
ATOM   5022 C  C    . LEU   B 1 83  ? 48.417 -9.974  -2.190  1.00 11.45 ?  83   LEU   B C    1 
ATOM   5023 O  O    . LEU   B 1 83  ? 47.815 -10.386 -3.189  1.00 11.60 ?  83   LEU   B O    1 
ATOM   5024 C  CB   . LEU   B 1 83  ? 48.463 -10.513 0.314   1.00 12.01 ?  83   LEU   B CB   1 
ATOM   5025 C  CG   . LEU   B 1 83  ? 47.960 -10.154 1.715   1.00 13.47 ?  83   LEU   B CG   1 
ATOM   5026 C  CD1  . LEU   B 1 83  ? 48.598 -11.020 2.783   1.00 14.12 ?  83   LEU   B CD1  1 
ATOM   5027 C  CD2  . LEU   B 1 83  ? 48.182 -8.673  2.027   1.00 14.47 ?  83   LEU   B CD2  1 
ATOM   5028 H  H    . LEU   B 1 83  ? 46.328 -11.148 -1.299  1.00 13.75 ?  83   LEU   B H    1 
ATOM   5029 H  HA   . LEU   B 1 83  ? 47.661 -8.891  -0.643  1.00 13.68 ?  83   LEU   B HA   1 
ATOM   5030 H  HB2  . LEU   B 1 83  ? 48.386 -11.473 0.212   1.00 14.41 ?  83   LEU   B HB2  1 
ATOM   5031 H  HB3  . LEU   B 1 83  ? 49.398 -10.255 0.262   1.00 14.41 ?  83   LEU   B HB3  1 
ATOM   5032 H  HG   . LEU   B 1 83  ? 47.008 -10.313 1.743   1.00 16.16 ?  83   LEU   B HG   1 
ATOM   5033 H  HD11 . LEU   B 1 83  ? 48.245 -10.764 3.651   1.00 16.94 ?  83   LEU   B HD11 1 
ATOM   5034 H  HD12 . LEU   B 1 83  ? 48.382 -11.951 2.604   1.00 16.94 ?  83   LEU   B HD12 1 
ATOM   5035 H  HD13 . LEU   B 1 83  ? 49.558 -10.896 2.767   1.00 16.94 ?  83   LEU   B HD13 1 
ATOM   5036 H  HD21 . LEU   B 1 83  ? 47.994 -8.517  2.965   1.00 17.35 ?  83   LEU   B HD21 1 
ATOM   5037 H  HD22 . LEU   B 1 83  ? 49.104 -8.441  1.831   1.00 17.35 ?  83   LEU   B HD22 1 
ATOM   5038 H  HD23 . LEU   B 1 83  ? 47.585 -8.141  1.477   1.00 17.35 ?  83   LEU   B HD23 1 
ATOM   5039 N  N    . SER   B 1 84  ? 49.693 -9.594  -2.238  1.00 12.58 ?  84   SER   B N    1 
ATOM   5040 C  CA   . SER   B 1 84  ? 50.429 -9.714  -3.488  1.00 12.83 ?  84   SER   B CA   1 
ATOM   5041 C  C    . SER   B 1 84  ? 50.583 -11.174 -3.899  1.00 11.69 ?  84   SER   B C    1 
ATOM   5042 O  O    . SER   B 1 84  ? 50.699 -12.069 -3.062  1.00 11.71 ?  84   SER   B O    1 
ATOM   5043 C  CB   . SER   B 1 84  ? 51.823 -9.106  -3.343  1.00 14.61 ?  84   SER   B CB   1 
ATOM   5044 O  OG   . SER   B 1 84  ? 52.560 -9.327  -4.528  1.00 16.09 ?  84   SER   B OG   1 
ATOM   5045 H  H    . SER   B 1 84  ? 50.137 -9.262  -1.579  1.00 15.09 ?  84   SER   B H    1 
ATOM   5046 H  HA   . SER   B 1 84  ? 49.958 -9.251  -4.189  1.00 15.39 ?  84   SER   B HA   1 
ATOM   5047 H  HB2  . SER   B 1 84  ? 51.737 -8.149  -3.185  1.00 17.52 ?  84   SER   B HB2  1 
ATOM   5048 H  HB3  . SER   B 1 84  ? 52.287 -9.524  -2.602  1.00 17.52 ?  84   SER   B HB3  1 
ATOM   5049 H  HG   . SER   B 1 84  ? 53.328 -8.975  -4.462  1.00 19.30 ?  84   SER   B HG   1 
ATOM   5050 N  N    . GLY   B 1 85  ? 50.654 -11.401 -5.204  1.00 12.96 ?  85   GLY   B N    1 
ATOM   5051 C  CA   . GLY   B 1 85  ? 51.003 -12.695 -5.738  1.00 13.39 ?  85   GLY   B CA   1 
ATOM   5052 C  C    . GLY   B 1 85  ? 52.472 -12.877 -6.049  1.00 12.86 ?  85   GLY   B C    1 
ATOM   5053 O  O    . GLY   B 1 85  ? 52.857 -13.955 -6.509  1.00 13.49 ?  85   GLY   B O    1 
ATOM   5054 H  H    . GLY   B 1 85  ? 50.503 -10.813 -5.803  1.00 15.55 ?  85   GLY   B H    1 
ATOM   5055 H  HA2  . GLY   B 1 85  ? 50.749 -13.386 -5.097  1.00 16.06 ?  85   GLY   B HA2  1 
ATOM   5056 H  HA3  . GLY   B 1 85  ? 50.505 -12.851 -6.551  1.00 16.06 ?  85   GLY   B HA3  1 
ATOM   5057 N  N    . HIS   B 1 86  ? 53.320 -11.871 -5.828  1.00 12.90 ?  86   HIS   B N    1 
ATOM   5058 C  CA   . HIS   B 1 86  ? 54.782 -12.036 -5.905  1.00 12.92 ?  86   HIS   B CA   1 
ATOM   5059 C  C    . HIS   B 1 86  ? 55.158 -12.542 -7.295  1.00 12.80 ?  86   HIS   B C    1 
ATOM   5060 O  O    . HIS   B 1 86  ? 54.774 -11.925 -8.300  1.00 13.49 ?  86   HIS   B O    1 
ATOM   5061 C  CB   . HIS   B 1 86  ? 55.270 -12.881 -4.733  1.00 13.59 ?  86   HIS   B CB   1 
ATOM   5062 C  CG   . HIS   B 1 86  ? 54.957 -12.274 -3.407  1.00 13.41 ?  86   HIS   B CG   1 
ATOM   5063 N  ND1  . HIS   B 1 86  ? 55.781 -11.354 -2.793  1.00 15.01 ?  86   HIS   B ND1  1 
ATOM   5064 C  CD2  . HIS   B 1 86  ? 53.882 -12.421 -2.597  1.00 13.62 ?  86   HIS   B CD2  1 
ATOM   5065 C  CE1  . HIS   B 1 86  ? 55.226 -10.968 -1.658  1.00 14.42 ?  86   HIS   B CE1  1 
ATOM   5066 N  NE2  . HIS   B 1 86  ? 54.071 -11.597 -1.517  1.00 13.63 ?  86   HIS   B NE2  1 
ATOM   5067 H  H    . HIS   B 1 86  ? 53.074 -11.072 -5.632  1.00 15.47 ?  86   HIS   B H    1 
ATOM   5068 H  HA   . HIS   B 1 86  ? 55.186 -11.164 -5.803  1.00 15.49 ?  86   HIS   B HA   1 
ATOM   5069 H  HB2  . HIS   B 1 86  ? 54.855 -13.757 -4.772  1.00 16.30 ?  86   HIS   B HB2  1 
ATOM   5070 H  HB3  . HIS   B 1 86  ? 56.239 -12.979 -4.794  1.00 16.30 ?  86   HIS   B HB3  1 
ATOM   5071 H  HD2  . HIS   B 1 86  ? 53.145 -12.971 -2.752  1.00 16.34 ?  86   HIS   B HD2  1 
ATOM   5072 H  HE1  . HIS   B 1 86  ? 55.590 -10.365 -1.052  1.00 17.30 ?  86   HIS   B HE1  1 
ATOM   5073 H  HE2  . HIS   B 1 86  ? 53.532 -11.518 -0.852  1.00 16.35 ?  86   HIS   B HE2  1 
ATOM   5074 N  N    . ASN   B 1 87  ? 55.925 -13.625 -7.403  1.00 13.29 ?  87   ASN   B N    1 
ATOM   5075 C  CA   . ASN   B 1 87  ? 56.320 -14.192 -8.684  1.00 14.49 ?  87   ASN   B CA   1 
ATOM   5076 C  C    . ASN   B 1 87  ? 55.343 -15.239 -9.181  1.00 13.82 ?  87   ASN   B C    1 
ATOM   5077 O  O    . ASN   B 1 87  ? 55.656 -15.951 -10.138 1.00 15.57 ?  87   ASN   B O    1 
ATOM   5078 C  CB   . ASN   B 1 87  ? 57.713 -14.819 -8.572  1.00 16.02 ?  87   ASN   B CB   1 
ATOM   5079 C  CG   . ASN   B 1 87  ? 57.772 -15.934 -7.532  1.00 16.88 ?  87   ASN   B CG   1 
ATOM   5080 O  OD1  . ASN   B 1 87  ? 57.132 -15.861 -6.476  1.00 15.97 ?  87   ASN   B OD1  1 
ATOM   5081 N  ND2  . ASN   B 1 87  ? 58.524 -16.990 -7.843  1.00 19.27 ?  87   ASN   B ND2  1 
ATOM   5082 H  H    . ASN   B 1 87  ? 56.228 -14.064 -6.732  1.00 15.95 ?  87   ASN   B H    1 
ATOM   5083 H  HA   . ASN   B 1 87  ? 56.361 -13.484 -9.343  1.00 17.38 ?  87   ASN   B HA   1 
ATOM   5084 H  HB2  . ASN   B 1 87  ? 57.959 -15.196 -9.436  1.00 19.21 ?  87   ASN   B HB2  1 
ATOM   5085 H  HB3  . ASN   B 1 87  ? 58.348 -14.135 -8.318  1.00 19.21 ?  87   ASN   B HB3  1 
ATOM   5086 H  HD21 . ASN   B 1 87  ? 58.593 -17.642 -7.291  1.00 23.12 ?  87   ASN   B HD21 1 
ATOM   5087 H  HD22 . ASN   B 1 87  ? 58.953 -17.011 -8.591  1.00 23.12 ?  87   ASN   B HD22 1 
ATOM   5088 N  N    . LEU   B 1 88  ? 54.166 -15.336 -8.566  1.00 13.05 ?  88   LEU   B N    1 
ATOM   5089 C  CA   . LEU   B 1 88  ? 53.190 -16.368 -8.894  1.00 13.33 ?  88   LEU   B CA   1 
ATOM   5090 C  C    . LEU   B 1 88  ? 51.957 -15.852 -9.614  1.00 13.10 ?  88   LEU   B C    1 
ATOM   5091 O  O    . LEU   B 1 88  ? 51.356 -16.595 -10.401 1.00 14.77 ?  88   LEU   B O    1 
ATOM   5092 C  CB   . LEU   B 1 88  ? 52.714 -17.048 -7.609  1.00 14.36 ?  88   LEU   B CB   1 
ATOM   5093 C  CG   . LEU   B 1 88  ? 53.829 -17.704 -6.808  1.00 16.43 ?  88   LEU   B CG   1 
ATOM   5094 C  CD1  . LEU   B 1 88  ? 53.323 -18.051 -5.422  1.00 17.59 ?  88   LEU   B CD1  1 
ATOM   5095 C  CD2  . LEU   B 1 88  ? 54.311 -18.942 -7.537  1.00 19.30 ?  88   LEU   B CD2  1 
ATOM   5096 H  H    . LEU   B 1 88  ? 53.904 -14.809 -7.934  1.00 15.65 ?  88   LEU   B H    1 
ATOM   5097 H  HA   . LEU   B 1 88  ? 53.602 -17.035 -9.454  1.00 15.99 ?  88   LEU   B HA   1 
ATOM   5098 H  HB2  . LEU   B 1 88  ? 52.290 -16.391 -7.037  1.00 17.22 ?  88   LEU   B HB2  1 
ATOM   5099 H  HB3  . LEU   B 1 88  ? 52.073 -17.742 -7.840  1.00 17.22 ?  88   LEU   B HB3  1 
ATOM   5100 H  HG   . LEU   B 1 88  ? 54.573 -17.088 -6.722  1.00 19.71 ?  88   LEU   B HG   1 
ATOM   5101 H  HD11 . LEU   B 1 88  ? 53.941 -18.674 -5.008  1.00 21.10 ?  88   LEU   B HD11 1 
ATOM   5102 H  HD12 . LEU   B 1 88  ? 53.267 -17.239 -4.895  1.00 21.10 ?  88   LEU   B HD12 1 
ATOM   5103 H  HD13 . LEU   B 1 88  ? 52.447 -18.457 -5.503  1.00 21.10 ?  88   LEU   B HD13 1 
ATOM   5104 H  HD21 . LEU   B 1 88  ? 54.965 -19.398 -6.983  1.00 23.16 ?  88   LEU   B HD21 1 
ATOM   5105 H  HD22 . LEU   B 1 88  ? 53.555 -19.525 -7.704  1.00 23.16 ?  88   LEU   B HD22 1 
ATOM   5106 H  HD23 . LEU   B 1 88  ? 54.718 -18.678 -8.377  1.00 23.16 ?  88   LEU   B HD23 1 
ATOM   5107 N  N    . ALA   B 1 89  ? 51.549 -14.620 -9.340  1.00 12.55 ?  89   ALA   B N    1 
ATOM   5108 C  CA   . ALA   B 1 89  ? 50.258 -14.126 -9.792  1.00 12.01 ?  89   ALA   B CA   1 
ATOM   5109 C  C    . ALA   B 1 89  ? 50.227 -12.636 -9.508  1.00 12.24 ?  89   ALA   B C    1 
ATOM   5110 O  O    . ALA   B 1 89  ? 51.061 -12.120 -8.764  1.00 13.18 ?  89   ALA   B O    1 
ATOM   5111 C  CB   . ALA   B 1 89  ? 49.121 -14.810 -9.038  1.00 11.89 ?  89   ALA   B CB   1 
ATOM   5112 H  H    . ALA   B 1 89  ? 51.996 -14.039 -8.882  1.00 15.06 ?  89   ALA   B H    1 
ATOM   5113 H  HA   . ALA   B 1 89  ? 50.149 -14.273 -10.747 1.00 14.41 ?  89   ALA   B HA   1 
ATOM   5114 H  HB1  . ALA   B 1 89  ? 48.272 -14.481 -9.377  1.00 14.26 ?  89   ALA   B HB1  1 
ATOM   5115 H  HB2  . ALA   B 1 89  ? 49.182 -15.768 -9.184  1.00 14.26 ?  89   ALA   B HB2  1 
ATOM   5116 H  HB3  . ALA   B 1 89  ? 49.203 -14.611 -8.096  1.00 14.26 ?  89   ALA   B HB3  1 
ATOM   5117 N  N    . LYS   B 1 90  ? 49.235 -11.949 -10.072 1.00 13.31 ?  90   LYS   B N    1 
ATOM   5118 C  CA   . LYS   B 1 90  ? 49.038 -10.564 -9.666  1.00 13.75 ?  90   LYS   B CA   1 
ATOM   5119 C  C    . LYS   B 1 90  ? 48.720 -10.495 -8.179  1.00 13.26 ?  90   LYS   B C    1 
ATOM   5120 O  O    . LYS   B 1 90  ? 49.360 -9.743  -7.426  1.00 14.73 ?  90   LYS   B O    1 
ATOM   5121 C  CB   . LYS   B 1 90  ? 47.956 -9.906  -10.522 1.00 15.04 ?  90   LYS   B CB   1 
ATOM   5122 C  CG   . LYS   B 1 90  ? 47.653 -8.469  -10.141 1.00 15.39 ?  90   LYS   B CG   1 
ATOM   5123 C  CD   . LYS   B 1 90  ? 48.857 -7.571  -10.227 1.00 18.12 ?  90   LYS   B CD   1 
ATOM   5124 C  CE   . LYS   B 1 90  ? 48.410 -6.149  -9.989  1.00 20.39 ?  90   LYS   B CE   1 
ATOM   5125 N  NZ   . LYS   B 1 90  ? 49.558 -5.223  -9.875  1.00 20.21 ?  90   LYS   B NZ   1 
ATOM   5126 H  H    . LYS   B 1 90  ? 48.686 -12.247 -10.662 1.00 15.97 ?  90   LYS   B H    1 
ATOM   5127 H  HA   . LYS   B 1 90  ? 49.863 -10.079 -9.813  1.00 16.49 ?  90   LYS   B HA   1 
ATOM   5128 H  HB2  . LYS   B 1 90  ? 48.249 -9.905  -11.450 1.00 18.04 ?  90   LYS   B HB2  1 
ATOM   5129 H  HB3  . LYS   B 1 90  ? 47.136 -10.416 -10.443 1.00 18.04 ?  90   LYS   B HB3  1 
ATOM   5130 H  HG2  . LYS   B 1 90  ? 46.972 -8.120  -10.740 1.00 18.46 ?  90   LYS   B HG2  1 
ATOM   5131 H  HG3  . LYS   B 1 90  ? 47.319 -8.447  -9.226  1.00 18.46 ?  90   LYS   B HG3  1 
ATOM   5132 H  HD2  . LYS   B 1 90  ? 49.499 -7.815  -9.542  1.00 21.74 ?  90   LYS   B HD2  1 
ATOM   5133 H  HD3  . LYS   B 1 90  ? 49.251 -7.635  -11.110 1.00 21.74 ?  90   LYS   B HD3  1 
ATOM   5134 H  HE2  . LYS   B 1 90  ? 47.861 -5.855  -10.735 1.00 24.46 ?  90   LYS   B HE2  1 
ATOM   5135 H  HE3  . LYS   B 1 90  ? 47.903 -6.102  -9.164  1.00 24.46 ?  90   LYS   B HE3  1 
ATOM   5136 H  HZ1  . LYS   B 1 90  ? 49.270 -4.390  -9.738  1.00 24.25 ?  90   LYS   B HZ1  1 
ATOM   5137 H  HZ2  . LYS   B 1 90  ? 50.079 -5.462  -9.195  1.00 24.25 ?  90   LYS   B HZ2  1 
ATOM   5138 H  HZ3  . LYS   B 1 90  ? 50.040 -5.238  -10.625 1.00 24.25 ?  90   LYS   B HZ3  1 
ATOM   5139 N  N    . HIS   B 1 91  ? 47.763 -11.315 -7.735  1.00 11.46 ?  91   HIS   B N    1 
ATOM   5140 C  CA   . HIS   B 1 91  ? 47.296 -11.335 -6.364  1.00 11.63 ?  91   HIS   B CA   1 
ATOM   5141 C  C    . HIS   B 1 91  ? 47.299 -12.762 -5.850  1.00 10.87 ?  91   HIS   B C    1 
ATOM   5142 O  O    . HIS   B 1 91  ? 47.076 -13.715 -6.607  1.00 11.45 ?  91   HIS   B O    1 
ATOM   5143 C  CB   . HIS   B 1 91  ? 45.840 -10.862 -6.249  1.00 13.28 ?  91   HIS   B CB   1 
ATOM   5144 C  CG   . HIS   B 1 91  ? 45.626 -9.453  -6.675  1.00 16.49 ?  91   HIS   B CG   1 
ATOM   5145 N  ND1  . HIS   B 1 91  ? 46.241 -8.383  -6.060  1.00 18.88 ?  91   HIS   B ND1  1 
ATOM   5146 C  CD2  . HIS   B 1 91  ? 44.845 -8.931  -7.645  1.00 19.26 ?  91   HIS   B CD2  1 
ATOM   5147 C  CE1  . HIS   B 1 91  ? 45.858 -7.260  -6.644  1.00 20.06 ?  91   HIS   B CE1  1 
ATOM   5148 N  NE2  . HIS   B 1 91  ? 45.005 -7.567  -7.605  1.00 20.51 ?  91   HIS   B NE2  1 
ATOM   5149 H  H    . HIS   B 1 91  ? 47.360 -11.890 -8.231  1.00 13.75 ?  91   HIS   B H    1 
ATOM   5150 H  HA   . HIS   B 1 91  ? 47.860 -10.781 -5.796  1.00 13.95 ?  91   HIS   B HA   1 
ATOM   5151 H  HB2  . HIS   B 1 91  ? 45.280 -11.425 -6.807  1.00 15.93 ?  91   HIS   B HB2  1 
ATOM   5152 H  HB3  . HIS   B 1 91  ? 45.553 -10.937 -5.322  1.00 15.93 ?  91   HIS   B HB3  1 
ATOM   5153 H  HD1  . HIS   B 1 91  ? 46.790 -8.436  -5.398  1.00 22.65 ?  91   HIS   B HD1  1 
ATOM   5154 H  HD2  . HIS   B 1 91  ? 44.303 -9.396  -8.236  1.00 23.10 ?  91   HIS   B HD2  1 
ATOM   5155 H  HE1  . HIS   B 1 91  ? 46.138 -6.401  -6.408  1.00 24.06 ?  91   HIS   B HE1  1 
ATOM   5156 N  N    . CYS   B 1 92  ? 47.493 -12.895 -4.550  1.00 10.87 ?  92   CYS   B N    1 
ATOM   5157 C  CA   . CYS   B 1 92  ? 47.194 -14.131 -3.844  1.00 10.75 ?  92   CYS   B CA   1 
ATOM   5158 C  C    . CYS   B 1 92  ? 45.975 -13.896 -2.959  1.00 10.42 ?  92   CYS   B C    1 
ATOM   5159 O  O    . CYS   B 1 92  ? 45.979 -12.996 -2.109  1.00 11.38 ?  92   CYS   B O    1 
ATOM   5160 C  CB   . CYS   B 1 92  ? 48.374 -14.593 -2.996  1.00 11.11 ?  92   CYS   B CB   1 
ATOM   5161 S  SG   . CYS   B 1 92  ? 48.014 -16.123 -2.097  1.00 11.54 ?  92   CYS   B SG   1 
ATOM   5162 H  H    . CYS   B 1 92  ? 47.814 -12.276 -4.040  1.00 13.04 ?  92   CYS   B H    1 
ATOM   5163 H  HA   . CYS   B 1 92  ? 46.993 -14.829 -4.488  1.00 12.90 ?  92   CYS   B HA   1 
ATOM   5164 H  HB2  . CYS   B 1 92  ? 49.140 -14.752 -3.568  1.00 13.32 ?  92   CYS   B HB2  1 
ATOM   5165 H  HB3  . CYS   B 1 92  ? 48.582 -13.905 -2.343  1.00 13.32 ?  92   CYS   B HB3  1 
ATOM   5166 H  HG   . CYS   B 1 92  ? 48.988 -16.441 -1.471  1.00 13.84 ?  92   CYS   B HG   1 
ATOM   5167 N  N    . LEU   B 1 93  ? 44.935 -14.701 -3.172  1.00 10.47 ?  93   LEU   B N    1 
ATOM   5168 C  CA   . LEU   B 1 93  ? 43.765 -14.713 -2.308  1.00 10.48 ?  93   LEU   B CA   1 
ATOM   5169 C  C    . LEU   B 1 93  ? 43.993 -15.781 -1.247  1.00 10.27 ?  93   LEU   B C    1 
ATOM   5170 O  O    . LEU   B 1 93  ? 43.946 -16.983 -1.543  1.00 10.90 ?  93   LEU   B O    1 
ATOM   5171 C  CB   . LEU   B 1 93  ? 42.503 -15.000 -3.117  1.00 10.99 ?  93   LEU   B CB   1 
ATOM   5172 C  CG   . LEU   B 1 93  ? 41.204 -15.024 -2.311  1.00 11.87 ?  93   LEU   B CG   1 
ATOM   5173 C  CD1  . LEU   B 1 93  ? 40.842 -13.638 -1.806  1.00 12.56 ?  93   LEU   B CD1  1 
ATOM   5174 C  CD2  . LEU   B 1 93  ? 40.081 -15.616 -3.148  1.00 11.88 ?  93   LEU   B CD2  1 
ATOM   5175 H  H    . LEU   B 1 93  ? 44.895 -15.274 -3.824  1.00 12.55 ?  93   LEU   B H    1 
ATOM   5176 H  HA   . LEU   B 1 93  ? 43.675 -13.854 -1.877  1.00 12.57 ?  93   LEU   B HA   1 
ATOM   5177 H  HB2  . LEU   B 1 93  ? 42.411 -14.311 -3.796  1.00 13.18 ?  93   LEU   B HB2  1 
ATOM   5178 H  HB3  . LEU   B 1 93  ? 42.597 -15.864 -3.545  1.00 13.18 ?  93   LEU   B HB3  1 
ATOM   5179 H  HG   . LEU   B 1 93  ? 41.324 -15.595 -1.539  1.00 14.24 ?  93   LEU   B HG   1 
ATOM   5180 H  HD11 . LEU   B 1 93  ? 39.993 -13.682 -1.339  1.00 15.06 ?  93   LEU   B HD11 1 
ATOM   5181 H  HD12 . LEU   B 1 93  ? 41.536 -13.329 -1.202  1.00 15.06 ?  93   LEU   B HD12 1 
ATOM   5182 H  HD13 . LEU   B 1 93  ? 40.770 -13.033 -2.563  1.00 15.06 ?  93   LEU   B HD13 1 
ATOM   5183 H  HD21 . LEU   B 1 93  ? 39.260 -15.608 -2.630  1.00 14.25 ?  93   LEU   B HD21 1 
ATOM   5184 H  HD22 . LEU   B 1 93  ? 39.968 -15.081 -3.952  1.00 14.25 ?  93   LEU   B HD22 1 
ATOM   5185 H  HD23 . LEU   B 1 93  ? 40.311 -16.527 -3.389  1.00 14.25 ?  93   LEU   B HD23 1 
ATOM   5186 N  N    . HIS   B 1 94  ? 44.273 -15.354 -0.021  1.00 10.33 ?  94   HIS   B N    1 
ATOM   5187 C  CA   . HIS   B 1 94  ? 44.491 -16.263 1.098   1.00 10.20 ?  94   HIS   B CA   1 
ATOM   5188 C  C    . HIS   B 1 94  ? 43.127 -16.617 1.669   1.00 10.83 ?  94   HIS   B C    1 
ATOM   5189 O  O    . HIS   B 1 94  ? 42.455 -15.747 2.224   1.00 12.15 ?  94   HIS   B O    1 
ATOM   5190 C  CB   . HIS   B 1 94  ? 45.361 -15.582 2.151   1.00 10.80 ?  94   HIS   B CB   1 
ATOM   5191 C  CG   . HIS   B 1 94  ? 46.741 -15.277 1.677   1.00 10.61 ?  94   HIS   B CG   1 
ATOM   5192 N  ND1  . HIS   B 1 94  ? 47.764 -16.198 1.752   1.00 10.95 ?  94   HIS   B ND1  1 
ATOM   5193 C  CD2  . HIS   B 1 94  ? 47.251 -14.165 1.092   1.00 10.75 ?  94   HIS   B CD2  1 
ATOM   5194 C  CE1  . HIS   B 1 94  ? 48.856 -15.645 1.252   1.00 10.86 ?  94   HIS   B CE1  1 
ATOM   5195 N  NE2  . HIS   B 1 94  ? 48.571 -14.420 0.836   1.00 11.04 ?  94   HIS   B NE2  1 
ATOM   5196 H  H    . HIS   B 1 94  ? 44.341 -14.519 0.190   1.00 12.39 ?  94   HIS   B H    1 
ATOM   5197 H  HA   . HIS   B 1 94  ? 44.932 -17.068 0.787   1.00 12.23 ?  94   HIS   B HA   1 
ATOM   5198 H  HB2  . HIS   B 1 94  ? 44.945 -14.744 2.406   1.00 12.95 ?  94   HIS   B HB2  1 
ATOM   5199 H  HB3  . HIS   B 1 94  ? 45.433 -16.165 2.919   1.00 12.95 ?  94   HIS   B HB3  1 
ATOM   5200 H  HD2  . HIS   B 1 94  ? 46.796 -13.381 0.900   1.00 12.90 ?  94   HIS   B HD2  1 
ATOM   5201 H  HE1  . HIS   B 1 94  ? 49.690 -16.061 1.191   1.00 13.03 ?  94   HIS   B HE1  1 
ATOM   5202 H  HE2  . HIS   B 1 94  ? 49.132 -13.876 0.475   1.00 13.25 ?  94   HIS   B HE2  1 
ATOM   5203 N  N    . VAL   B 1 95  ? 42.694 -17.869 1.511   1.00 10.78 ?  95   VAL   B N    1 
ATOM   5204 C  CA   . VAL   B 1 95  ? 41.368 -18.308 1.945   1.00 10.90 ?  95   VAL   B CA   1 
ATOM   5205 C  C    . VAL   B 1 95  ? 41.534 -19.349 3.037   1.00 11.18 ?  95   VAL   B C    1 
ATOM   5206 O  O    . VAL   B 1 95  ? 42.307 -20.301 2.876   1.00 11.79 ?  95   VAL   B O    1 
ATOM   5207 C  CB   . VAL   B 1 95  ? 40.550 -18.908 0.786   1.00 11.02 ?  95   VAL   B CB   1 
ATOM   5208 C  CG1  . VAL   B 1 95  ? 39.177 -19.359 1.275   1.00 12.34 ?  95   VAL   B CG1  1 
ATOM   5209 C  CG2  . VAL   B 1 95  ? 40.423 -17.922 -0.343  1.00 11.19 ?  95   VAL   B CG2  1 
ATOM   5210 H  H    . VAL   B 1 95  ? 43.156 -18.496 1.139   1.00 12.93 ?  95   VAL   B H    1 
ATOM   5211 H  HA   . VAL   B 1 95  ? 40.875 -17.557 2.307   1.00 13.07 ?  95   VAL   B HA   1 
ATOM   5212 H  HB   . VAL   B 1 95  ? 41.010 -19.689 0.444   1.00 13.22 ?  95   VAL   B HB   1 
ATOM   5213 H  HG11 . VAL   B 1 95  ? 38.607 -19.546 0.507   1.00 14.81 ?  95   VAL   B HG11 1 
ATOM   5214 H  HG12 . VAL   B 1 95  ? 39.271 -20.165 1.809   1.00 14.81 ?  95   VAL   B HG12 1 
ATOM   5215 H  HG13 . VAL   B 1 95  ? 38.777 -18.654 1.809   1.00 14.81 ?  95   VAL   B HG13 1 
ATOM   5216 H  HG21 . VAL   B 1 95  ? 39.841 -18.297 -1.026  1.00 13.42 ?  95   VAL   B HG21 1 
ATOM   5217 H  HG22 . VAL   B 1 95  ? 40.037 -17.100 0.001   1.00 13.42 ?  95   VAL   B HG22 1 
ATOM   5218 H  HG23 . VAL   B 1 95  ? 41.299 -17.751 -0.711  1.00 13.42 ?  95   VAL   B HG23 1 
ATOM   5219 N  N    . VAL   B 1 96  ? 40.813 -19.174 4.137   1.00 11.83 ?  96   VAL   B N    1 
ATOM   5220 C  CA   . VAL   B 1 96  ? 40.895 -20.090 5.274   1.00 12.04 ?  96   VAL   B CA   1 
ATOM   5221 C  C    . VAL   B 1 96  ? 39.707 -21.049 5.225   1.00 12.28 ?  96   VAL   B C    1 
ATOM   5222 O  O    . VAL   B 1 96  ? 38.586 -20.691 5.602   1.00 12.91 ?  96   VAL   B O    1 
ATOM   5223 C  CB   . VAL   B 1 96  ? 40.946 -19.344 6.609   1.00 12.39 ?  96   VAL   B CB   1 
ATOM   5224 C  CG1  . VAL   B 1 96  ? 41.121 -20.336 7.742   1.00 13.16 ?  96   VAL   B CG1  1 
ATOM   5225 C  CG2  . VAL   B 1 96  ? 42.063 -18.306 6.617   1.00 13.03 ?  96   VAL   B CG2  1 
ATOM   5226 H  H    . VAL   B 1 96  ? 40.259 -18.526 4.252   1.00 14.20 ?  96   VAL   B H    1 
ATOM   5227 H  HA   . VAL   B 1 96  ? 41.709 -20.616 5.197   1.00 14.44 ?  96   VAL   B HA   1 
ATOM   5228 H  HB   . VAL   B 1 96  ? 40.105 -18.882 6.745   1.00 14.86 ?  96   VAL   B HB   1 
ATOM   5229 H  HG11 . VAL   B 1 96  ? 41.317 -19.851 8.562   1.00 15.78 ?  96   VAL   B HG11 1 
ATOM   5230 H  HG12 . VAL   B 1 96  ? 40.307 -20.849 7.852   1.00 15.78 ?  96   VAL   B HG12 1 
ATOM   5231 H  HG13 . VAL   B 1 96  ? 41.862 -20.931 7.534   1.00 15.78 ?  96   VAL   B HG13 1 
ATOM   5232 H  HG21 . VAL   B 1 96  ? 42.112 -17.897 7.497   1.00 15.63 ?  96   VAL   B HG21 1 
ATOM   5233 H  HG22 . VAL   B 1 96  ? 42.904 -18.739 6.407   1.00 15.63 ?  96   VAL   B HG22 1 
ATOM   5234 H  HG23 . VAL   B 1 96  ? 41.869 -17.624 5.951   1.00 15.63 ?  96   VAL   B HG23 1 
ATOM   5235 N  N    . GLY   B 1 97  ? 39.944 -22.281 4.781   1.00 12.34 ?  97   GLY   B N    1 
ATOM   5236 C  CA   . GLY   B 1 97  ? 38.972 -23.339 4.938   1.00 12.73 ?  97   GLY   B CA   1 
ATOM   5237 C  C    . GLY   B 1 97  ? 39.086 -23.937 6.322   1.00 13.74 ?  97   GLY   B C    1 
ATOM   5238 O  O    . GLY   B 1 97  ? 40.123 -23.814 6.984   1.00 14.39 ?  97   GLY   B O    1 
ATOM   5239 H  H    . GLY   B 1 97  ? 40.675 -22.523 4.382   1.00 14.80 ?  97   GLY   B H    1 
ATOM   5240 H  HA2  . GLY   B 1 97  ? 38.080 -22.976 4.811   1.00 15.27 ?  97   GLY   B HA2  1 
ATOM   5241 H  HA3  . GLY   B 1 97  ? 39.126 -24.029 4.269   1.00 15.27 ?  97   GLY   B HA3  1 
ATOM   5242 N  N    . PRO   B 1 98  ? 38.035 -24.615 6.785   1.00 14.29 ?  98   PRO   B N    1 
ATOM   5243 C  CA   . PRO   B 1 98  ? 38.126 -25.309 8.075   1.00 15.24 ?  98   PRO   B CA   1 
ATOM   5244 C  C    . PRO   B 1 98  ? 39.149 -26.433 8.031   1.00 14.76 ?  98   PRO   B C    1 
ATOM   5245 O  O    . PRO   B 1 98  ? 39.261 -27.163 7.047   1.00 14.97 ?  98   PRO   B O    1 
ATOM   5246 C  CB   . PRO   B 1 98  ? 36.708 -25.854 8.278   1.00 15.33 ?  98   PRO   B CB   1 
ATOM   5247 C  CG   . PRO   B 1 98  ? 36.166 -26.004 6.904   1.00 15.04 ?  98   PRO   B CG   1 
ATOM   5248 C  CD   . PRO   B 1 98  ? 36.725 -24.825 6.144   1.00 14.44 ?  98   PRO   B CD   1 
ATOM   5249 H  HA   . PRO   B 1 98  ? 38.348 -24.687 8.780   1.00 18.28 ?  98   PRO   B HA   1 
ATOM   5250 H  HB2  . PRO   B 1 98  ? 36.749 -26.715 8.728   1.00 18.38 ?  98   PRO   B HB2  1 
ATOM   5251 H  HB3  . PRO   B 1 98  ? 36.183 -25.222 8.788   1.00 18.38 ?  98   PRO   B HB3  1 
ATOM   5252 H  HG2  . PRO   B 1 98  ? 36.475 -26.844 6.520   1.00 18.04 ?  98   PRO   B HG2  1 
ATOM   5253 H  HG3  . PRO   B 1 98  ? 35.198 -25.975 6.928   1.00 18.04 ?  98   PRO   B HG3  1 
ATOM   5254 H  HD2  . PRO   B 1 98  ? 36.830 -25.051 5.201   1.00 17.33 ?  98   PRO   B HD2  1 
ATOM   5255 H  HD3  . PRO   B 1 98  ? 36.163 -24.047 6.262   1.00 17.33 ?  98   PRO   B HD3  1 
ATOM   5256 N  N    . ASN   B 1 99  ? 39.896 -26.566 9.118   1.00 16.20 ?  99   ASN   B N    1 
ATOM   5257 C  CA   . ASN   B 1 99  ? 40.876 -27.636 9.273   1.00 16.85 ?  99   ASN   B CA   1 
ATOM   5258 C  C    . ASN   B 1 99  ? 40.249 -28.723 10.144  1.00 19.22 ?  99   ASN   B C    1 
ATOM   5259 O  O    . ASN   B 1 99  ? 40.168 -28.583 11.365  1.00 19.87 ?  99   ASN   B O    1 
ATOM   5260 C  CB   . ASN   B 1 99  ? 42.151 -27.081 9.890   1.00 17.10 ?  99   ASN   B CB   1 
ATOM   5261 C  CG   . ASN   B 1 99  ? 43.274 -28.090 9.904   1.00 18.11 ?  99   ASN   B CG   1 
ATOM   5262 O  OD1  . ASN   B 1 99  ? 43.043 -29.281 10.063  1.00 18.70 ?  99   ASN   B OD1  1 
ATOM   5263 N  ND2  . ASN   B 1 99  ? 44.495 -27.619 9.728   1.00 18.39 ?  99   ASN   B ND2  1 
ATOM   5264 H  H    . ASN   B 1 99  ? 39.852 -26.038 9.794   1.00 19.43 ?  99   ASN   B H    1 
ATOM   5265 H  HA   . ASN   B 1 99  ? 41.084 -28.022 8.410   1.00 20.21 ?  99   ASN   B HA   1 
ATOM   5266 H  HB2  . ASN   B 1 99  ? 42.440 -26.317 9.382   1.00 20.51 ?  99   ASN   B HB2  1 
ATOM   5267 H  HB3  . ASN   B 1 99  ? 41.965 -26.824 10.811  1.00 20.51 ?  99   ASN   B HB3  1 
ATOM   5268 H  HD21 . ASN   B 1 99  ? 45.166 -28.157 9.730   1.00 22.07 ?  99   ASN   B HD21 1 
ATOM   5269 H  HD22 . ASN   B 1 99  ? 44.613 -26.778 9.621   1.00 22.07 ?  99   ASN   B HD22 1 
ATOM   5270 N  N    A VAL   B 1 100 ? 39.787 -29.802 9.505   0.50 20.73 ?  100  VAL   B N    1 
ATOM   5271 N  N    B VAL   B 1 100 ? 39.800 -29.805 9.502   0.50 20.69 ?  100  VAL   B N    1 
ATOM   5272 C  CA   A VAL   B 1 100 ? 39.171 -30.902 10.246  0.50 23.24 ?  100  VAL   B CA   1 
ATOM   5273 C  CA   B VAL   B 1 100 ? 39.179 -30.911 10.228  0.50 23.17 ?  100  VAL   B CA   1 
ATOM   5274 C  C    A VAL   B 1 100 ? 40.175 -31.557 11.186  0.50 23.69 ?  100  VAL   B C    1 
ATOM   5275 C  C    B VAL   B 1 100 ? 40.173 -31.569 11.173  0.50 23.63 ?  100  VAL   B C    1 
ATOM   5276 O  O    A VAL   B 1 100 ? 39.803 -32.047 12.259  0.50 24.33 ?  100  VAL   B O    1 
ATOM   5277 O  O    B VAL   B 1 100 ? 39.791 -32.075 12.235  0.50 24.20 ?  100  VAL   B O    1 
ATOM   5278 C  CB   A VAL   B 1 100 ? 38.530 -31.917 9.277   0.50 25.28 ?  100  VAL   B CB   1 
ATOM   5279 C  CB   B VAL   B 1 100 ? 38.572 -31.920 9.231   0.50 25.15 ?  100  VAL   B CB   1 
ATOM   5280 C  CG1  A VAL   B 1 100 ? 38.048 -33.150 10.028  0.50 26.08 ?  100  VAL   B CG1  1 
ATOM   5281 C  CG1  B VAL   B 1 100 ? 38.082 -33.166 9.953   0.50 25.94 ?  100  VAL   B CG1  1 
ATOM   5282 C  CG2  A VAL   B 1 100 ? 37.374 -31.273 8.525   0.50 25.88 ?  100  VAL   B CG2  1 
ATOM   5283 C  CG2  B VAL   B 1 100 ? 37.437 -31.270 8.459   0.50 25.73 ?  100  VAL   B CG2  1 
ATOM   5284 H  H    A VAL   B 1 100 ? 39.807 -29.915 8.650   0.50 24.86 ?  100  VAL   B H    1 
ATOM   5285 H  H    B VAL   B 1 100 ? 39.842 -29.917 8.651   0.50 24.82 ?  100  VAL   B H    1 
ATOM   5286 H  HA   A VAL   B 1 100 ? 38.455 -30.542 10.790  0.50 27.88 ?  100  VAL   B HA   1 
ATOM   5287 H  HA   B VAL   B 1 100 ? 38.451 -30.562 10.764  0.50 27.79 ?  100  VAL   B HA   1 
ATOM   5288 H  HB   A VAL   B 1 100 ? 39.192 -32.201 8.631   0.50 30.33 ?  100  VAL   B HB   1 
ATOM   5289 H  HB   B VAL   B 1 100 ? 39.254 -32.192 8.598   0.50 30.17 ?  100  VAL   B HB   1 
ATOM   5290 H  HG11 A VAL   B 1 100 ? 37.461 -33.662 9.447   0.50 31.29 ?  100  VAL   B HG11 1 
ATOM   5291 H  HG11 B VAL   B 1 100 ? 37.511 -33.672 9.353   0.50 31.12 ?  100  VAL   B HG11 1 
ATOM   5292 H  HG12 A VAL   B 1 100 ? 38.813 -33.692 10.279  0.50 31.29 ?  100  VAL   B HG12 1 
ATOM   5293 H  HG12 B VAL   B 1 100 ? 38.845 -33.706 10.213  0.50 31.12 ?  100  VAL   B HG12 1 
ATOM   5294 H  HG13 A VAL   B 1 100 ? 37.563 -32.871 10.820  0.50 31.29 ?  100  VAL   B HG13 1 
ATOM   5295 H  HG13 B VAL   B 1 100 ? 37.580 -32.900 10.739  0.50 31.12 ?  100  VAL   B HG13 1 
ATOM   5296 H  HG21 A VAL   B 1 100 ? 36.981 -31.930 7.928   0.50 31.05 ?  100  VAL   B HG21 1 
ATOM   5297 H  HG21 B VAL   B 1 100 ? 37.051 -31.924 7.856   0.50 30.87 ?  100  VAL   B HG21 1 
ATOM   5298 H  HG22 A VAL   B 1 100 ? 36.710 -30.969 9.164   0.50 31.05 ?  100  VAL   B HG22 1 
ATOM   5299 H  HG22 B VAL   B 1 100 ? 36.765 -30.963 9.087   0.50 30.87 ?  100  VAL   B HG22 1 
ATOM   5300 H  HG23 A VAL   B 1 100 ? 37.710 -30.522 8.014   0.50 31.05 ?  100  VAL   B HG23 1 
ATOM   5301 H  HG23 B VAL   B 1 100 ? 37.788 -30.521 7.956   0.50 30.87 ?  100  VAL   B HG23 1 
ATOM   5302 N  N    . ASN   B 1 101 ? 41.455 -31.588 10.806  1.00 23.98 ?  101  ASN   B N    1 
ATOM   5303 C  CA   . ASN   B 1 101 ? 42.486 -32.124 11.692  1.00 26.34 ?  101  ASN   B CA   1 
ATOM   5304 C  C    . ASN   B 1 101 ? 42.669 -31.288 12.952  1.00 28.69 ?  101  ASN   B C    1 
ATOM   5305 O  O    . ASN   B 1 101 ? 43.307 -31.759 13.902  1.00 29.90 ?  101  ASN   B O    1 
ATOM   5306 C  CB   . ASN   B 1 101 ? 43.816 -32.253 10.945  1.00 26.50 ?  101  ASN   B CB   1 
ATOM   5307 C  CG   . ASN   B 1 101 ? 43.808 -33.389 9.941   1.00 26.26 ?  101  ASN   B CG   1 
ATOM   5308 O  OD1  . ASN   B 1 101 ? 43.140 -34.396 10.142  1.00 27.44 ?  101  ASN   B OD1  1 
ATOM   5309 N  ND2  . ASN   B 1 101 ? 44.543 -33.224 8.850   1.00 26.03 ?  101  ASN   B ND2  1 
ATOM   5310 H  H    A ASN   B 1 101 ? 41.743 -31.320 10.041  0.50 28.77 ?  101  ASN   B H    1 
ATOM   5311 H  H    B ASN   B 1 101 ? 41.747 -31.306 10.047  0.50 28.77 ?  101  ASN   B H    1 
ATOM   5312 H  HA   . ASN   B 1 101 ? 42.220 -33.010 11.971  1.00 31.61 ?  101  ASN   B HA   1 
ATOM   5313 H  HB2  . ASN   B 1 101 ? 43.999 -31.430 10.466  1.00 31.79 ?  101  ASN   B HB2  1 
ATOM   5314 H  HB3  . ASN   B 1 101 ? 44.523 -32.426 11.586  1.00 31.79 ?  101  ASN   B HB3  1 
ATOM   5315 H  HD21 . ASN   B 1 101 ? 44.567 -33.842 8.251   1.00 31.23 ?  101  ASN   B HD21 1 
ATOM   5316 H  HD22 . ASN   B 1 101 ? 44.995 -32.501 8.740   1.00 31.23 ?  101  ASN   B HD22 1 
ATOM   5317 N  N    . LYS   B 1 102 ? 42.132 -30.067 12.977  1.00 30.49 ?  102  LYS   B N    1 
ATOM   5318 C  CA   . LYS   B 1 102 ? 42.106 -29.223 14.164  1.00 32.91 ?  102  LYS   B CA   1 
ATOM   5319 C  C    . LYS   B 1 102 ? 40.727 -29.177 14.810  1.00 32.63 ?  102  LYS   B C    1 
ATOM   5320 O  O    . LYS   B 1 102 ? 40.510 -28.377 15.725  1.00 33.24 ?  102  LYS   B O    1 
ATOM   5321 C  CB   . LYS   B 1 102 ? 42.537 -27.798 13.811  1.00 36.08 ?  102  LYS   B CB   1 
ATOM   5322 C  CG   . LYS   B 1 102 ? 43.995 -27.643 13.421  1.00 39.21 ?  102  LYS   B CG   1 
ATOM   5323 C  CD   . LYS   B 1 102 ? 44.264 -26.215 12.968  1.00 42.12 ?  102  LYS   B CD   1 
ATOM   5324 C  CE   . LYS   B 1 102 ? 45.741 -25.958 12.731  1.00 44.41 ?  102  LYS   B CE   1 
ATOM   5325 N  NZ   . LYS   B 1 102 ? 45.985 -24.561 12.265  1.00 45.77 ?  102  LYS   B NZ   1 
ATOM   5326 H  H    . LYS   B 1 102 ? 41.756 -29.699 12.297  1.00 36.58 ?  102  LYS   B H    1 
ATOM   5327 H  HA   . LYS   B 1 102 ? 42.735 -29.571 14.813  1.00 39.49 ?  102  LYS   B HA   1 
ATOM   5328 H  HB2  . LYS   B 1 102 ? 41.999 -27.488 13.065  1.00 43.29 ?  102  LYS   B HB2  1 
ATOM   5329 H  HB3  . LYS   B 1 102 ? 42.379 -27.228 14.582  1.00 43.29 ?  102  LYS   B HB3  1 
ATOM   5330 H  HG2  . LYS   B 1 102 ? 44.560 -27.835 14.187  1.00 47.05 ?  102  LYS   B HG2  1 
ATOM   5331 H  HG3  . LYS   B 1 102 ? 44.201 -28.243 12.687  1.00 47.05 ?  102  LYS   B HG3  1 
ATOM   5332 H  HD2  . LYS   B 1 102 ? 43.791 -26.051 12.136  1.00 50.54 ?  102  LYS   B HD2  1 
ATOM   5333 H  HD3  . LYS   B 1 102 ? 43.955 -25.601 13.653  1.00 50.54 ?  102  LYS   B HD3  1 
ATOM   5334 H  HE2  . LYS   B 1 102 ? 46.226 -26.091 13.562  1.00 53.29 ?  102  LYS   B HE2  1 
ATOM   5335 H  HE3  . LYS   B 1 102 ? 46.067 -26.568 12.051  1.00 53.29 ?  102  LYS   B HE3  1 
ATOM   5336 H  HZ1  . LYS   B 1 102 ? 46.855 -24.432 12.133  1.00 54.92 ?  102  LYS   B HZ1  1 
ATOM   5337 H  HZ2  . LYS   B 1 102 ? 45.551 -24.416 11.501  1.00 54.92 ?  102  LYS   B HZ2  1 
ATOM   5338 H  HZ3  . LYS   B 1 102 ? 45.695 -23.982 12.876  1.00 54.92 ?  102  LYS   B HZ3  1 
ATOM   5339 N  N    A GLY   B 1 103 ? 39.797 -30.018 14.364  0.50 32.24 ?  103  GLY   B N    1 
ATOM   5340 N  N    B GLY   B 1 103 ? 39.786 -29.991 14.339  0.50 32.06 ?  103  GLY   B N    1 
ATOM   5341 C  CA   A GLY   B 1 103 ? 38.464 -30.052 14.924  0.50 32.10 ?  103  GLY   B CA   1 
ATOM   5342 C  CA   B GLY   B 1 103 ? 38.457 -30.035 14.913  0.50 31.75 ?  103  GLY   B CA   1 
ATOM   5343 C  C    A GLY   B 1 103 ? 37.539 -28.958 14.441  0.50 31.39 ?  103  GLY   B C    1 
ATOM   5344 C  C    B GLY   B 1 103 ? 37.516 -28.944 14.453  0.50 30.81 ?  103  GLY   B C    1 
ATOM   5345 O  O    A GLY   B 1 103 ? 36.402 -28.874 14.924  0.50 31.96 ?  103  GLY   B O    1 
ATOM   5346 O  O    B GLY   B 1 103 ? 36.462 -28.760 15.071  0.50 31.42 ?  103  GLY   B O    1 
ATOM   5347 H  H    A GLY   B 1 103 ? 39.920 -30.582 13.728  0.50 38.68 ?  103  GLY   B H    1 
ATOM   5348 H  H    B GLY   B 1 103 ? 39.898 -30.529 13.680  0.50 38.47 ?  103  GLY   B H    1 
ATOM   5349 H  HA2  A GLY   B 1 103 ? 38.054 -30.903 14.706  0.50 38.52 ?  103  GLY   B HA2  1 
ATOM   5350 H  HA2  B GLY   B 1 103 ? 38.054 -30.892 14.701  0.50 38.09 ?  103  GLY   B HA2  1 
ATOM   5351 H  HA3  A GLY   B 1 103 ? 38.528 -29.989 15.891  0.50 38.52 ?  103  GLY   B HA3  1 
ATOM   5352 H  HA3  B GLY   B 1 103 ? 38.529 -29.971 15.878  0.50 38.09 ?  103  GLY   B HA3  1 
ATOM   5353 N  N    A GLU   B 1 104 ? 37.981 -28.121 13.508  0.50 29.82 ?  104  GLU   B N    1 
ATOM   5354 N  N    B GLU   B 1 104 ? 37.855 -28.216 13.393  0.50 28.92 ?  104  GLU   B N    1 
ATOM   5355 C  CA   A GLU   B 1 104 ? 37.145 -27.035 13.021  0.50 28.23 ?  104  GLU   B CA   1 
ATOM   5356 C  CA   B GLU   B 1 104 ? 37.017 -27.119 12.934  0.50 27.05 ?  104  GLU   B CA   1 
ATOM   5357 C  C    A GLU   B 1 104 ? 35.975 -27.582 12.208  0.50 28.65 ?  104  GLU   B C    1 
ATOM   5358 C  C    B GLU   B 1 104 ? 35.854 -27.639 12.095  0.50 27.20 ?  104  GLU   B C    1 
ATOM   5359 O  O    A GLU   B 1 104 ? 36.033 -28.679 11.645  0.50 29.12 ?  104  GLU   B O    1 
ATOM   5360 O  O    B GLU   B 1 104 ? 35.929 -28.706 11.477  0.50 27.61 ?  104  GLU   B O    1 
ATOM   5361 C  CB   A GLU   B 1 104 ? 37.987 -26.056 12.200  0.50 26.65 ?  104  GLU   B CB   1 
ATOM   5362 C  CB   B GLU   B 1 104 ? 37.856 -26.107 12.152  0.50 25.49 ?  104  GLU   B CB   1 
ATOM   5363 C  CG   A GLU   B 1 104 ? 39.109 -25.431 13.021  0.50 25.25 ?  104  GLU   B CG   1 
ATOM   5364 C  CG   B GLU   B 1 104 ? 38.964 -25.506 13.008  0.50 24.09 ?  104  GLU   B CG   1 
ATOM   5365 C  CD   A GLU   B 1 104 ? 40.022 -24.531 12.214  0.50 23.86 ?  104  GLU   B CD   1 
ATOM   5366 C  CD   B GLU   B 1 104 ? 39.913 -24.606 12.244  0.50 22.66 ?  104  GLU   B CD   1 
ATOM   5367 O  OE1  A GLU   B 1 104 ? 39.997 -24.595 10.968  0.50 22.02 ?  104  GLU   B OE1  1 
ATOM   5368 O  OE1  B GLU   B 1 104 ? 39.891 -24.600 10.995  0.50 21.19 ?  104  GLU   B OE1  1 
ATOM   5369 O  OE2  A GLU   B 1 104 ? 40.767 -23.749 12.839  0.50 24.31 -1 104  GLU   B OE2  1 
ATOM   5370 O  OE2  B GLU   B 1 104 ? 40.691 -23.898 12.915  0.50 22.65 -1 104  GLU   B OE2  1 
ATOM   5371 H  H    A GLU   B 1 104 ? 38.760 -28.158 13.149  0.50 35.78 ?  104  GLU   B H    1 
ATOM   5372 H  H    B GLU   B 1 104 ? 38.570 -28.332 12.930  0.50 34.70 ?  104  GLU   B H    1 
ATOM   5373 H  HA   A GLU   B 1 104 ? 36.786 -26.551 13.779  0.50 33.87 ?  104  GLU   B HA   1 
ATOM   5374 H  HA   B GLU   B 1 104 ? 36.648 -26.665 13.706  0.50 32.45 ?  104  GLU   B HA   1 
ATOM   5375 H  HB2  A GLU   B 1 104 ? 38.388 -26.526 11.453  0.50 31.98 ?  104  GLU   B HB2  1 
ATOM   5376 H  HB2  B GLU   B 1 104 ? 38.265 -26.550 11.393  0.50 30.58 ?  104  GLU   B HB2  1 
ATOM   5377 H  HB3  A GLU   B 1 104 ? 37.418 -25.339 11.878  0.50 31.98 ?  104  GLU   B HB3  1 
ATOM   5378 H  HB3  B GLU   B 1 104 ? 37.282 -25.386 11.849  0.50 30.58 ?  104  GLU   B HB3  1 
ATOM   5379 H  HG2  A GLU   B 1 104 ? 38.723 -24.891 13.728  0.50 30.30 ?  104  GLU   B HG2  1 
ATOM   5380 H  HG2  B GLU   B 1 104 ? 38.562 -24.974 13.713  0.50 28.90 ?  104  GLU   B HG2  1 
ATOM   5381 H  HG3  A GLU   B 1 104 ? 39.653 -26.136 13.407  0.50 30.30 ?  104  GLU   B HG3  1 
ATOM   5382 H  HG3  B GLU   B 1 104 ? 39.487 -26.224 13.397  0.50 28.90 ?  104  GLU   B HG3  1 
ATOM   5383 N  N    A ASP   B 1 105 ? 34.898 -26.801 12.163  0.50 28.62 ?  105  ASP   B N    1 
ATOM   5384 N  N    B ASP   B 1 105 ? 34.767 -26.869 12.086  0.50 26.96 ?  105  ASP   B N    1 
ATOM   5385 C  CA   A ASP   B 1 105 ? 33.623 -27.266 11.632  0.50 29.12 ?  105  ASP   B CA   1 
ATOM   5386 C  CA   B ASP   B 1 105 ? 33.504 -27.338 11.527  0.50 27.39 ?  105  ASP   B CA   1 
ATOM   5387 C  C    A ASP   B 1 105 ? 33.672 -27.317 10.110  0.50 27.51 ?  105  ASP   B C    1 
ATOM   5388 C  C    B ASP   B 1 105 ? 33.572 -27.358 10.005  0.50 25.84 ?  105  ASP   B C    1 
ATOM   5389 O  O    A ASP   B 1 105 ? 33.856 -26.286 9.453   0.50 27.11 ?  105  ASP   B O    1 
ATOM   5390 O  O    B ASP   B 1 105 ? 33.734 -26.312 9.368   0.50 25.13 ?  105  ASP   B O    1 
ATOM   5391 C  CB   A ASP   B 1 105 ? 32.506 -26.334 12.095  0.50 31.26 ?  105  ASP   B CB   1 
ATOM   5392 C  CB   B ASP   B 1 105 ? 32.364 -26.437 11.998  0.50 29.38 ?  105  ASP   B CB   1 
ATOM   5393 C  CG   A ASP   B 1 105 ? 31.135 -26.800 11.650  0.50 33.07 ?  105  ASP   B CG   1 
ATOM   5394 C  CG   B ASP   B 1 105 ? 30.996 -27.009 11.671  0.50 30.91 ?  105  ASP   B CG   1 
ATOM   5395 O  OD1  A ASP   B 1 105 ? 31.027 -27.936 11.143  0.50 33.26 ?  105  ASP   B OD1  1 
ATOM   5396 O  OD1  B ASP   B 1 105 ? 30.929 -27.985 10.895  0.50 31.09 ?  105  ASP   B OD1  1 
ATOM   5397 O  OD2  A ASP   B 1 105 ? 30.167 -26.024 11.798  0.50 34.24 -1 105  ASP   B OD2  1 
ATOM   5398 O  OD2  B ASP   B 1 105 ? 29.988 -26.491 12.199  0.50 31.42 -1 105  ASP   B OD2  1 
ATOM   5399 H  H    A ASP   B 1 105 ? 34.885 -25.987 12.436  0.50 34.34 ?  105  ASP   B H    1 
ATOM   5400 H  H    B ASP   B 1 105 ? 34.737 -26.068 12.395  0.50 32.34 ?  105  ASP   B H    1 
ATOM   5401 H  HA   A ASP   B 1 105 ? 33.437 -28.159 11.964  0.50 34.94 ?  105  ASP   B HA   1 
ATOM   5402 H  HA   B ASP   B 1 105 ? 33.326 -28.238 11.836  0.50 32.86 ?  105  ASP   B HA   1 
ATOM   5403 H  HB2  A ASP   B 1 105 ? 32.525 -26.276 13.066  0.50 37.51 ?  105  ASP   B HB2  1 
ATOM   5404 H  HB2  B ASP   B 1 105 ? 32.424 -26.327 12.960  0.50 35.24 ?  105  ASP   B HB2  1 
ATOM   5405 H  HB3  A ASP   B 1 105 ? 32.645 -25.456 11.710  0.50 37.51 ?  105  ASP   B HB3  1 
ATOM   5406 H  HB3  B ASP   B 1 105 ? 32.443 -25.571 11.562  0.50 35.24 ?  105  ASP   B HB3  1 
ATOM   5407 N  N    A ILE   B 1 106 ? 33.484 -28.516 9.552   0.50 26.86 ?  106  ILE   B N    1 
ATOM   5408 N  N    B ILE   B 1 106 ? 33.426 -28.552 9.425   0.50 25.48 ?  106  ILE   B N    1 
ATOM   5409 C  CA   A ILE   B 1 106 ? 33.490 -28.698 8.105   0.50 25.95 ?  106  ILE   B CA   1 
ATOM   5410 C  CA   B ILE   B 1 106 ? 33.429 -28.707 7.975   0.50 24.99 ?  106  ILE   B CA   1 
ATOM   5411 C  C    A ILE   B 1 106 ? 32.404 -27.873 7.424   0.50 24.74 ?  106  ILE   B C    1 
ATOM   5412 C  C    B ILE   B 1 106 ? 32.335 -27.874 7.318   0.50 24.01 ?  106  ILE   B C    1 
ATOM   5413 O  O    A ILE   B 1 106 ? 32.529 -27.541 6.240   0.50 24.11 ?  106  ILE   B O    1 
ATOM   5414 O  O    B ILE   B 1 106 ? 32.438 -27.541 6.132   0.50 23.18 ?  106  ILE   B O    1 
ATOM   5415 C  CB   A ILE   B 1 106 ? 33.385 -30.205 7.772   0.50 26.40 ?  106  ILE   B CB   1 
ATOM   5416 C  CB   B ILE   B 1 106 ? 33.327 -30.208 7.613   0.50 25.69 ?  106  ILE   B CB   1 
ATOM   5417 C  CG1  A ILE   B 1 106 ? 33.622 -30.457 6.281   0.50 26.62 ?  106  ILE   B CG1  1 
ATOM   5418 C  CG1  B ILE   B 1 106 ? 33.623 -30.436 6.130   0.50 26.22 ?  106  ILE   B CG1  1 
ATOM   5419 C  CG2  A ILE   B 1 106 ? 32.031 -30.758 8.195   0.50 27.03 ?  106  ILE   B CG2  1 
ATOM   5420 C  CG2  B ILE   B 1 106 ? 31.953 -30.758 7.972   0.50 26.35 ?  106  ILE   B CG2  1 
ATOM   5421 C  CD1  A ILE   B 1 106 ? 34.978 -30.002 5.797   0.50 26.67 ?  106  ILE   B CD1  1 
ATOM   5422 C  CD1  B ILE   B 1 106 ? 34.999 -29.978 5.712   0.50 26.44 ?  106  ILE   B CD1  1 
ATOM   5423 H  H    A ILE   B 1 106 ? 33.356 -29.239 9.997   0.50 32.23 ?  106  ILE   B H    1 
ATOM   5424 H  H    B ILE   B 1 106 ? 33.327 -29.288 9.854   0.50 30.57 ?  106  ILE   B H    1 
ATOM   5425 H  HA   A ILE   B 1 106 ? 34.339 -28.384 7.769   0.50 31.14 ?  106  ILE   B HA   1 
ATOM   5426 H  HA   B ILE   B 1 106 ? 34.272 -28.378 7.640   0.50 29.99 ?  106  ILE   B HA   1 
ATOM   5427 H  HB   A ILE   B 1 106 ? 34.071 -30.676 8.271   0.50 31.68 ?  106  ILE   B HB   1 
ATOM   5428 H  HB   B ILE   B 1 106 ? 33.990 -30.691 8.131   0.50 30.83 ?  106  ILE   B HB   1 
ATOM   5429 H  HG12 A ILE   B 1 106 ? 33.557 -31.412 6.111   0.50 31.94 ?  106  ILE   B HG12 1 
ATOM   5430 H  HG12 B ILE   B 1 106 ? 33.560 -31.387 5.941   0.50 31.46 ?  106  ILE   B HG12 1 
ATOM   5431 H  HG13 A ILE   B 1 106 ? 32.950 -29.987 5.768   0.50 31.94 ?  106  ILE   B HG13 1 
ATOM   5432 H  HG13 B ILE   B 1 106 ? 32.973 -29.953 5.599   0.50 31.46 ?  106  ILE   B HG13 1 
ATOM   5433 H  HG21 A ILE   B 1 106 ? 32.039 -31.723 8.092   0.50 32.43 ?  106  ILE   B HG21 1 
ATOM   5434 H  HG21 B ILE   B 1 106 ? 31.972 -31.725 7.898   0.50 31.61 ?  106  ILE   B HG21 1 
ATOM   5435 H  HG22 A ILE   B 1 106 ? 31.873 -30.526 9.123   0.50 32.43 ?  106  ILE   B HG22 1 
ATOM   5436 H  HG22 B ILE   B 1 106 ? 31.740 -30.500 8.882   0.50 31.61 ?  106  ILE   B HG22 1 
ATOM   5437 H  HG23 A ILE   B 1 106 ? 31.341 -30.371 7.634   0.50 32.43 ?  106  ILE   B HG23 1 
ATOM   5438 H  HG23 B ILE   B 1 106 ? 31.295 -30.392 7.361   0.50 31.61 ?  106  ILE   B HG23 1 
ATOM   5439 H  HD11 A ILE   B 1 106 ? 35.153 -30.399 4.931   0.50 32.00 ?  106  ILE   B HD11 1 
ATOM   5440 H  HD11 B ILE   B 1 106 ? 35.221 -30.385 4.861   0.50 31.72 ?  106  ILE   B HD11 1 
ATOM   5441 H  HD12 A ILE   B 1 106 ? 34.978 -29.034 5.723   0.50 32.00 ?  106  ILE   B HD12 1 
ATOM   5442 H  HD12 B ILE   B 1 106 ? 34.998 -29.011 5.626   0.50 31.72 ?  106  ILE   B HD12 1 
ATOM   5443 H  HD13 A ILE   B 1 106 ? 35.653 -30.286 6.434   0.50 32.00 ?  106  ILE   B HD13 1 
ATOM   5444 H  HD13 B ILE   B 1 106 ? 35.641 -30.250 6.387   0.50 31.72 ?  106  ILE   B HD13 1 
ATOM   5445 N  N    A GLN   B 1 107 ? 31.339 -27.519 8.149   0.50 24.77 ?  107  GLN   B N    1 
ATOM   5446 N  N    B GLN   B 1 107 ? 31.292 -27.511 8.068   0.50 24.39 ?  107  GLN   B N    1 
ATOM   5447 C  CA   A GLN   B 1 107 ? 30.262 -26.726 7.562   0.50 25.09 ?  107  GLN   B CA   1 
ATOM   5448 C  CA   B GLN   B 1 107 ? 30.223 -26.691 7.513   0.50 25.00 ?  107  GLN   B CA   1 
ATOM   5449 C  C    A GLN   B 1 107 ? 30.748 -25.378 7.038   0.50 22.99 ?  107  GLN   B C    1 
ATOM   5450 C  C    B GLN   B 1 107 ? 30.722 -25.329 7.048   0.50 23.01 ?  107  GLN   B C    1 
ATOM   5451 O  O    A GLN   B 1 107 ? 30.119 -24.815 6.138   0.50 23.38 ?  107  GLN   B O    1 
ATOM   5452 O  O    B GLN   B 1 107 ? 30.078 -24.705 6.201   0.50 23.61 ?  107  GLN   B O    1 
ATOM   5453 C  CB   A GLN   B 1 107 ? 29.151 -26.523 8.598   0.50 28.13 ?  107  GLN   B CB   1 
ATOM   5454 C  CB   B GLN   B 1 107 ? 29.106 -26.524 8.547   0.50 28.17 ?  107  GLN   B CB   1 
ATOM   5455 C  CG   A GLN   B 1 107 ? 27.828 -26.018 8.030   0.50 31.17 ?  107  GLN   B CG   1 
ATOM   5456 C  CG   B GLN   B 1 107 ? 27.758 -26.110 7.968   0.50 31.32 ?  107  GLN   B CG   1 
ATOM   5457 C  CD   A GLN   B 1 107 ? 27.768 -24.505 7.917   0.50 33.53 ?  107  GLN   B CD   1 
ATOM   5458 C  CD   B GLN   B 1 107 ? 27.611 -24.606 7.826   0.50 33.79 ?  107  GLN   B CD   1 
ATOM   5459 O  OE1  A GLN   B 1 107 ? 28.602 -23.793 8.480   0.50 34.50 ?  107  GLN   B OE1  1 
ATOM   5460 O  OE1  B GLN   B 1 107 ? 28.391 -23.837 8.389   0.50 34.82 ?  107  GLN   B OE1  1 
ATOM   5461 N  NE2  A GLN   B 1 107 ? 26.772 -24.004 7.187   0.50 34.36 ?  107  GLN   B NE2  1 
ATOM   5462 N  NE2  B GLN   B 1 107 ? 26.600 -24.180 7.075   0.50 34.64 ?  107  GLN   B NE2  1 
ATOM   5463 H  H    A GLN   B 1 107 ? 31.220 -27.728 8.973   0.50 29.72 ?  107  GLN   B H    1 
ATOM   5464 H  H    B GLN   B 1 107 ? 31.184 -27.722 8.892   0.50 29.26 ?  107  GLN   B H    1 
ATOM   5465 H  HA   A GLN   B 1 107 ? 29.885 -27.217 6.814   0.50 30.10 ?  107  GLN   B HA   1 
ATOM   5466 H  HA   B GLN   B 1 107 ? 29.846 -27.147 6.744   0.50 30.00 ?  107  GLN   B HA   1 
ATOM   5467 H  HB2  A GLN   B 1 107 ? 28.977 -27.370 9.032   0.50 33.75 ?  107  GLN   B HB2  1 
ATOM   5468 H  HB2  B GLN   B 1 107 ? 28.978 -27.369 9.001   0.50 33.80 ?  107  GLN   B HB2  1 
ATOM   5469 H  HB3  A GLN   B 1 107 ? 29.456 -25.878 9.255   0.50 33.75 ?  107  GLN   B HB3  1 
ATOM   5470 H  HB3  B GLN   B 1 107 ? 29.373 -25.847 9.188   0.50 33.80 ?  107  GLN   B HB3  1 
ATOM   5471 H  HG2  A GLN   B 1 107 ? 27.701 -26.388 7.144   0.50 37.40 ?  107  GLN   B HG2  1 
ATOM   5472 H  HG2  B GLN   B 1 107 ? 27.656 -26.502 7.087   0.50 37.57 ?  107  GLN   B HG2  1 
ATOM   5473 H  HG3  A GLN   B 1 107 ? 27.105 -26.307 8.614   0.50 37.40 ?  107  GLN   B HG3  1 
ATOM   5474 H  HG3  B GLN   B 1 107 ? 27.052 -26.429 8.555   0.50 37.57 ?  107  GLN   B HG3  1 
ATOM   5475 H  HE21 A GLN   B 1 107 ? 26.208 -24.532 6.807   0.50 41.23 ?  107  GLN   B HE21 1 
ATOM   5476 H  HE21 B GLN   B 1 107 ? 26.076 -24.747 6.696   0.50 41.57 ?  107  GLN   B HE21 1 
ATOM   5477 H  HE22 A GLN   B 1 107 ? 26.689 -23.153 7.095   0.50 41.23 ?  107  GLN   B HE22 1 
ATOM   5478 H  HE22 B GLN   B 1 107 ? 26.471 -23.337 6.967   0.50 41.57 ?  107  GLN   B HE22 1 
ATOM   5479 N  N    . LEU   B 1 108 ? 31.860 -24.859 7.564   1.00 20.60 ?  108  LEU   B N    1 
ATOM   5480 C  CA   . LEU   B 1 108 ? 32.404 -23.566 7.151   1.00 18.49 ?  108  LEU   B CA   1 
ATOM   5481 C  C    . LEU   B 1 108 ? 33.049 -23.594 5.774   1.00 16.39 ?  108  LEU   B C    1 
ATOM   5482 O  O    . LEU   B 1 108 ? 33.484 -22.540 5.287   1.00 16.13 ?  108  LEU   B O    1 
ATOM   5483 C  CB   . LEU   B 1 108 ? 33.411 -23.071 8.185   1.00 18.92 ?  108  LEU   B CB   1 
ATOM   5484 C  CG   . LEU   B 1 108 ? 32.776 -22.598 9.492   1.00 20.37 ?  108  LEU   B CG   1 
ATOM   5485 C  CD1  . LEU   B 1 108 ? 33.795 -22.537 10.617  1.00 21.01 ?  108  LEU   B CD1  1 
ATOM   5486 C  CD2  . LEU   B 1 108 ? 32.138 -21.235 9.287   1.00 21.76 ?  108  LEU   B CD2  1 
ATOM   5487 H  H    A LEU   B 1 108 ? 32.322 -25.245 8.176   0.50 24.71 ?  108  LEU   B H    1 
ATOM   5488 H  H    B LEU   B 1 108 ? 32.328 -25.267 8.157   0.50 24.71 ?  108  LEU   B H    1 
ATOM   5489 H  HA   . LEU   B 1 108 ? 31.676 -22.928 7.116   1.00 22.18 ?  108  LEU   B HA   1 
ATOM   5490 H  HB2  . LEU   B 1 108 ? 34.018 -23.794 8.400   1.00 22.70 ?  108  LEU   B HB2  1 
ATOM   5491 H  HB3  . LEU   B 1 108 ? 33.902 -22.326 7.810   1.00 22.70 ?  108  LEU   B HB3  1 
ATOM   5492 H  HG   . LEU   B 1 108 ? 32.075 -23.219 9.754   1.00 24.43 ?  108  LEU   B HG   1 
ATOM   5493 H  HD11 . LEU   B 1 108 ? 33.351 -22.257 11.434  1.00 25.20 ?  108  LEU   B HD11 1 
ATOM   5494 H  HD12 . LEU   B 1 108 ? 34.185 -23.416 10.737  1.00 25.20 ?  108  LEU   B HD12 1 
ATOM   5495 H  HD13 . LEU   B 1 108 ? 34.485 -21.897 10.382  1.00 25.20 ?  108  LEU   B HD13 1 
ATOM   5496 H  HD21 . LEU   B 1 108 ? 31.809 -20.909 10.137  1.00 26.11 ?  108  LEU   B HD21 1 
ATOM   5497 H  HD22 . LEU   B 1 108 ? 32.807 -20.627 8.935   1.00 26.11 ?  108  LEU   B HD22 1 
ATOM   5498 H  HD23 . LEU   B 1 108 ? 31.405 -21.321 8.658   1.00 26.11 ?  108  LEU   B HD23 1 
ATOM   5499 N  N    . LEU   B 1 109 ? 33.112 -24.760 5.139   1.00 15.50 ?  109  LEU   B N    1 
ATOM   5500 C  CA   . LEU   B 1 109 ? 33.742 -24.861 3.832   1.00 14.69 ?  109  LEU   B CA   1 
ATOM   5501 C  C    . LEU   B 1 109 ? 32.977 -24.074 2.776   1.00 13.93 ?  109  LEU   B C    1 
ATOM   5502 O  O    . LEU   B 1 109 ? 33.590 -23.481 1.883   1.00 13.62 ?  109  LEU   B O    1 
ATOM   5503 C  CB   . LEU   B 1 109 ? 33.857 -26.332 3.446   1.00 15.05 ?  109  LEU   B CB   1 
ATOM   5504 C  CG   . LEU   B 1 109 ? 34.642 -26.667 2.183   1.00 14.77 ?  109  LEU   B CG   1 
ATOM   5505 C  CD1  . LEU   B 1 109 ? 36.020 -26.018 2.192   1.00 14.64 ?  109  LEU   B CD1  1 
ATOM   5506 C  CD2  . LEU   B 1 109 ? 34.757 -28.184 2.053   1.00 15.46 ?  109  LEU   B CD2  1 
ATOM   5507 H  H    . LEU   B 1 109 ? 32.802 -25.503 5.434   1.00 18.59 ?  109  LEU   B H    1 
ATOM   5508 H  HA   . LEU   B 1 109 ? 34.636 -24.494 3.880   1.00 17.62 ?  109  LEU   B HA   1 
ATOM   5509 H  HB2  . LEU   B 1 109 ? 34.285 -26.803 4.175   1.00 18.05 ?  109  LEU   B HB2  1 
ATOM   5510 H  HB3  . LEU   B 1 109 ? 32.959 -26.686 3.323   1.00 18.05 ?  109  LEU   B HB3  1 
ATOM   5511 H  HG   . LEU   B 1 109 ? 34.154 -26.344 1.406   1.00 17.71 ?  109  LEU   B HG   1 
ATOM   5512 H  HD11 . LEU   B 1 109 ? 36.547 -26.382 1.464   1.00 17.56 ?  109  LEU   B HD11 1 
ATOM   5513 H  HD12 . LEU   B 1 109 ? 35.916 -25.062 2.082   1.00 17.56 ?  109  LEU   B HD12 1 
ATOM   5514 H  HD13 . LEU   B 1 109 ? 36.451 -26.213 3.040   1.00 17.56 ?  109  LEU   B HD13 1 
ATOM   5515 H  HD21 . LEU   B 1 109 ? 35.325 -28.396 1.295   1.00 18.55 ?  109  LEU   B HD21 1 
ATOM   5516 H  HD22 . LEU   B 1 109 ? 35.138 -28.544 2.866   1.00 18.55 ?  109  LEU   B HD22 1 
ATOM   5517 H  HD23 . LEU   B 1 109 ? 33.869 -28.560 1.911   1.00 18.55 ?  109  LEU   B HD23 1 
ATOM   5518 N  N    . LYS   B 1 110 ? 31.645 -24.039 2.858   1.00 13.67 ?  110  LYS   B N    1 
ATOM   5519 C  CA   . LYS   B 1 110 ? 30.891 -23.276 1.868   1.00 13.79 ?  110  LYS   B CA   1 
ATOM   5520 C  C    . LYS   B 1 110 ? 31.230 -21.791 1.962   1.00 13.42 ?  110  LYS   B C    1 
ATOM   5521 O  O    . LYS   B 1 110 ? 31.478 -21.137 0.945   1.00 12.97 ?  110  LYS   B O    1 
ATOM   5522 C  CB   . LYS   B 1 110 ? 29.387 -23.519 2.018   1.00 14.45 ?  110  LYS   B CB   1 
ATOM   5523 C  CG   . LYS   B 1 110 ? 28.579 -22.899 0.883   1.00 14.87 ?  110  LYS   B CG   1 
ATOM   5524 C  CD   . LYS   B 1 110 ? 27.117 -23.326 0.913   1.00 15.25 ?  110  LYS   B CD   1 
ATOM   5525 C  CE   . LYS   B 1 110 ? 26.354 -22.790 -0.298  1.00 15.83 ?  110  LYS   B CE   1 
ATOM   5526 N  NZ   . LYS   B 1 110 ? 26.686 -23.501 -1.561  1.00 16.13 ?  110  LYS   B NZ   1 
ATOM   5527 H  H    . LYS   B 1 110 ? 31.172 -24.440 3.451   1.00 16.40 ?  110  LYS   B H    1 
ATOM   5528 H  HA   . LYS   B 1 110 ? 31.148 -23.579 0.983   1.00 16.54 ?  110  LYS   B HA   1 
ATOM   5529 H  HB2  . LYS   B 1 110 ? 29.220 -24.478 2.016   1.00 17.34 ?  110  LYS   B HB2  1 
ATOM   5530 H  HB3  . LYS   B 1 110 ? 29.083 -23.133 2.851   1.00 17.34 ?  110  LYS   B HB3  1 
ATOM   5531 H  HG2  . LYS   B 1 110 ? 28.604 -21.934 0.960   1.00 17.84 ?  110  LYS   B HG2  1 
ATOM   5532 H  HG3  . LYS   B 1 110 ? 28.949 -23.178 0.032   1.00 17.84 ?  110  LYS   B HG3  1 
ATOM   5533 H  HD2  . LYS   B 1 110 ? 27.060 -24.297 0.899   1.00 18.29 ?  110  LYS   B HD2  1 
ATOM   5534 H  HD3  . LYS   B 1 110 ? 26.692 -22.979 1.715   1.00 18.29 ?  110  LYS   B HD3  1 
ATOM   5535 H  HE2  . LYS   B 1 110 ? 25.403 -22.883 -0.146  1.00 18.99 ?  110  LYS   B HE2  1 
ATOM   5536 H  HE3  . LYS   B 1 110 ? 26.580 -21.852 -0.420  1.00 18.99 ?  110  LYS   B HE3  1 
ATOM   5537 H  HZ1  . LYS   B 1 110 ? 26.225 -23.153 -2.237  1.00 19.35 ?  110  LYS   B HZ1  1 
ATOM   5538 H  HZ2  . LYS   B 1 110 ? 27.556 -23.424 -1.735  1.00 19.35 ?  110  LYS   B HZ2  1 
ATOM   5539 H  HZ3  . LYS   B 1 110 ? 26.483 -24.364 -1.485  1.00 19.35 ?  110  LYS   B HZ3  1 
ATOM   5540 N  N    . SER   B 1 111 ? 31.251 -21.245 3.183   1.00 13.78 ?  111  SER   B N    1 
ATOM   5541 C  CA   . SER   B 1 111 ? 31.638 -19.845 3.363   1.00 13.67 ?  111  SER   B CA   1 
ATOM   5542 C  C    . SER   B 1 111 ? 33.017 -19.583 2.776   1.00 12.90 ?  111  SER   B C    1 
ATOM   5543 O  O    . SER   B 1 111 ? 33.241 -18.551 2.126   1.00 13.12 ?  111  SER   B O    1 
ATOM   5544 C  CB   . SER   B 1 111 ? 31.634 -19.496 4.850   1.00 14.63 ?  111  SER   B CB   1 
ATOM   5545 O  OG   . SER   B 1 111 ? 30.329 -19.515 5.386   1.00 16.29 ?  111  SER   B OG   1 
ATOM   5546 H  H    . SER   B 1 111 ? 31.049 -21.659 3.910   1.00 16.53 ?  111  SER   B H    1 
ATOM   5547 H  HA   . SER   B 1 111 ? 30.999 -19.273 2.914   1.00 16.40 ?  111  SER   B HA   1 
ATOM   5548 H  HB2  . SER   B 1 111 ? 32.172 -20.144 5.330   1.00 17.55 ?  111  SER   B HB2  1 
ATOM   5549 H  HB3  . SER   B 1 111 ? 32.006 -18.608 4.967   1.00 17.55 ?  111  SER   B HB3  1 
ATOM   5550 H  HG   . SER   B 1 111 ? 30.350 -19.312 6.211   1.00 19.54 ?  111  SER   B HG   1 
ATOM   5551 N  N    . ALA   B 1 112 ? 33.957 -20.504 2.994   1.00 13.09 ?  112  ALA   B N    1 
ATOM   5552 C  CA   . ALA   B 1 112 ? 35.301 -20.327 2.453   1.00 13.03 ?  112  ALA   B CA   1 
ATOM   5553 C  C    . ALA   B 1 112 ? 35.268 -20.229 0.929   1.00 12.39 ?  112  ALA   B C    1 
ATOM   5554 O  O    . ALA   B 1 112 ? 35.891 -19.342 0.336   1.00 12.54 ?  112  ALA   B O    1 
ATOM   5555 C  CB   . ALA   B 1 112 ? 36.207 -21.469 2.919   1.00 13.68 ?  112  ALA   B CB   1 
ATOM   5556 H  H    . ALA   B 1 112 ? 33.840 -21.231 3.449   1.00 15.70 ?  112  ALA   B H    1 
ATOM   5557 H  HA   . ALA   B 1 112 ? 35.664 -19.499 2.801   1.00 15.63 ?  112  ALA   B HA   1 
ATOM   5558 H  HB1  . ALA   B 1 112 ? 37.097 -21.329 2.559   1.00 16.41 ?  112  ALA   B HB1  1 
ATOM   5559 H  HB2  . ALA   B 1 112 ? 36.245 -21.466 3.893   1.00 16.41 ?  112  ALA   B HB2  1 
ATOM   5560 H  HB3  . ALA   B 1 112 ? 35.848 -22.310 2.607   1.00 16.41 ?  112  ALA   B HB3  1 
ATOM   5561 N  N    . TYR   B 1 113 ? 34.536 -21.132 0.273   1.00 12.12 ?  113  TYR   B N    1 
ATOM   5562 C  CA   . TYR   B 1 113 ? 34.462 -21.082 -1.183  1.00 11.91 ?  113  TYR   B CA   1 
ATOM   5563 C  C    . TYR   B 1 113 ? 33.759 -19.831 -1.694  1.00 11.69 ?  113  TYR   B C    1 
ATOM   5564 O  O    . TYR   B 1 113 ? 34.026 -19.398 -2.822  1.00 11.95 ?  113  TYR   B O    1 
ATOM   5565 C  CB   . TYR   B 1 113 ? 33.787 -22.336 -1.734  1.00 12.18 ?  113  TYR   B CB   1 
ATOM   5566 C  CG   . TYR   B 1 113 ? 34.746 -23.485 -1.998  1.00 12.61 ?  113  TYR   B CG   1 
ATOM   5567 C  CD1  . TYR   B 1 113 ? 35.737 -23.387 -2.971  1.00 13.32 ?  113  TYR   B CD1  1 
ATOM   5568 C  CD2  . TYR   B 1 113 ? 34.649 -24.675 -1.295  1.00 12.82 ?  113  TYR   B CD2  1 
ATOM   5569 C  CE1  . TYR   B 1 113 ? 36.619 -24.417 -3.217  1.00 13.01 ?  113  TYR   B CE1  1 
ATOM   5570 C  CE2  . TYR   B 1 113 ? 35.525 -25.729 -1.542  1.00 13.01 ?  113  TYR   B CE2  1 
ATOM   5571 C  CZ   . TYR   B 1 113 ? 36.499 -25.594 -2.510  1.00 13.33 ?  113  TYR   B CZ   1 
ATOM   5572 O  OH   . TYR   B 1 113 ? 37.380 -26.609 -2.791  1.00 13.84 ?  113  TYR   B OH   1 
ATOM   5573 H  H    . TYR   B 1 113 ? 34.074 -21.764 0.645   1.00 14.54 ?  113  TYR   B H    1 
ATOM   5574 H  HA   . TYR   B 1 113 ? 35.365 -21.063 -1.519  1.00 14.29 ?  113  TYR   B HA   1 
ATOM   5575 H  HB2  . TYR   B 1 113 ? 33.127 -22.650 -1.093  1.00 14.61 ?  113  TYR   B HB2  1 
ATOM   5576 H  HB3  . TYR   B 1 113 ? 33.351 -22.112 -2.569  1.00 14.61 ?  113  TYR   B HB3  1 
ATOM   5577 H  HD1  . TYR   B 1 113 ? 35.824 -22.594 -3.457  1.00 15.98 ?  113  TYR   B HD1  1 
ATOM   5578 H  HD2  . TYR   B 1 113 ? 33.992 -24.768 -0.650  1.00 15.38 ?  113  TYR   B HD2  1 
ATOM   5579 H  HE1  . TYR   B 1 113 ? 37.274 -24.328 -3.880  1.00 15.61 ?  113  TYR   B HE1  1 
ATOM   5580 H  HE2  . TYR   B 1 113 ? 35.447 -26.522 -1.069  1.00 15.60 ?  113  TYR   B HE2  1 
ATOM   5581 H  HH   . TYR   B 1 113 ? 37.210 -27.278 -2.311  1.00 16.60 ?  113  TYR   B HH   1 
ATOM   5582 N  N    . GLU   B 1 114 ? 32.833 -19.261 -0.913  1.00 11.87 ?  114  GLU   B N    1 
ATOM   5583 C  CA   . GLU   B 1 114 ? 32.143 -18.057 -1.367  1.00 11.80 ?  114  GLU   B CA   1 
ATOM   5584 C  C    . GLU   B 1 114 ? 33.127 -16.936 -1.665  1.00 11.62 ?  114  GLU   B C    1 
ATOM   5585 O  O    . GLU   B 1 114 ? 32.842 -16.072 -2.497  1.00 12.30 ?  114  GLU   B O    1 
ATOM   5586 C  CB   . GLU   B 1 114 ? 31.087 -17.626 -0.346  1.00 12.53 ?  114  GLU   B CB   1 
ATOM   5587 C  CG   . GLU   B 1 114 ? 29.866 -18.546 -0.409  1.00 12.83 ?  114  GLU   B CG   1 
ATOM   5588 C  CD   . GLU   B 1 114 ? 28.850 -18.364 0.699   1.00 12.99 ?  114  GLU   B CD   1 
ATOM   5589 O  OE1  . GLU   B 1 114 ? 29.145 -17.753 1.747   1.00 13.13 ?  114  GLU   B OE1  1 
ATOM   5590 O  OE2  . GLU   B 1 114 ? 27.725 -18.892 0.523   1.00 13.77 -1 114  GLU   B OE2  1 
ATOM   5591 H  H    . GLU   B 1 114 ? 32.586 -19.553 -0.135  1.00 14.24 ?  114  GLU   B H    1 
ATOM   5592 H  HA   . GLU   B 1 114 ? 31.685 -18.260 -2.189  1.00 14.16 ?  114  GLU   B HA   1 
ATOM   5593 H  HB2  . GLU   B 1 114 ? 31.459 -17.673 0.550   1.00 15.02 ?  114  GLU   B HB2  1 
ATOM   5594 H  HB3  . GLU   B 1 114 ? 30.797 -16.723 -0.543  1.00 15.02 ?  114  GLU   B HB3  1 
ATOM   5595 H  HG2  . GLU   B 1 114 ? 29.411 -18.390 -1.246  1.00 15.39 ?  114  GLU   B HG2  1 
ATOM   5596 H  HG3  . GLU   B 1 114 ? 30.178 -19.465 -0.372  1.00 15.39 ?  114  GLU   B HG3  1 
ATOM   5597 N  N    . ASN   B 1 115 ? 34.294 -16.934 -1.017  1.00 11.71 ?  115  ASN   B N    1 
ATOM   5598 C  CA   . ASN   B 1 115 ? 35.282 -15.895 -1.308  1.00 11.61 ?  115  ASN   B CA   1 
ATOM   5599 C  C    . ASN   B 1 115 ? 35.694 -15.915 -2.774  1.00 11.54 ?  115  ASN   B C    1 
ATOM   5600 O  O    . ASN   B 1 115 ? 36.076 -14.873 -3.330  1.00 11.84 ?  115  ASN   B O    1 
ATOM   5601 C  CB   . ASN   B 1 115 ? 36.521 -16.068 -0.427  1.00 12.33 ?  115  ASN   B CB   1 
ATOM   5602 C  CG   . ASN   B 1 115 ? 36.253 -15.807 1.037   1.00 12.46 ?  115  ASN   B CG   1 
ATOM   5603 O  OD1  . ASN   B 1 115 ? 36.255 -14.660 1.481   1.00 14.31 ?  115  ASN   B OD1  1 
ATOM   5604 N  ND2  . ASN   B 1 115 ? 36.088 -16.879 1.813   1.00 12.49 ?  115  ASN   B ND2  1 
ATOM   5605 H  H    . ASN   B 1 115 ? 34.532 -17.500 -0.408  1.00 14.04 ?  115  ASN   B H    1 
ATOM   5606 H  HA   . ASN   B 1 115 ? 34.896 -15.025 -1.114  1.00 13.92 ?  115  ASN   B HA   1 
ATOM   5607 H  HB2  . ASN   B 1 115 ? 36.850 -16.974 -0.515  1.00 14.79 ?  115  ASN   B HB2  1 
ATOM   5608 H  HB3  . ASN   B 1 115 ? 37.202 -15.439 -0.714  1.00 14.79 ?  115  ASN   B HB3  1 
ATOM   5609 H  HD21 . ASN   B 1 115 ? 35.944 -16.782 2.659   1.00 14.98 ?  115  ASN   B HD21 1 
ATOM   5610 H  HD22 . ASN   B 1 115 ? 36.109 -17.668 1.472   1.00 14.98 ?  115  ASN   B HD22 1 
ATOM   5611 N  N    . PHE   B 1 116 ? 35.669 -17.092 -3.408  1.00 11.27 ?  116  PHE   B N    1 
ATOM   5612 C  CA   . PHE   B 1 116 ? 36.095 -17.184 -4.798  1.00 11.44 ?  116  PHE   B CA   1 
ATOM   5613 C  C    . PHE   B 1 116 ? 35.190 -16.359 -5.708  1.00 11.44 ?  116  PHE   B C    1 
ATOM   5614 O  O    . PHE   B 1 116 ? 35.619 -15.927 -6.781  1.00 11.72 ?  116  PHE   B O    1 
ATOM   5615 C  CB   . PHE   B 1 116 ? 36.062 -18.629 -5.322  1.00 11.43 ?  116  PHE   B CB   1 
ATOM   5616 C  CG   . PHE   B 1 116 ? 37.132 -19.582 -4.777  1.00 11.48 ?  116  PHE   B CG   1 
ATOM   5617 C  CD1  . PHE   B 1 116 ? 37.785 -19.391 -3.572  1.00 12.37 ?  116  PHE   B CD1  1 
ATOM   5618 C  CD2  . PHE   B 1 116 ? 37.430 -20.720 -5.512  1.00 11.94 ?  116  PHE   B CD2  1 
ATOM   5619 C  CE1  . PHE   B 1 116 ? 38.718 -20.324 -3.119  1.00 12.69 ?  116  PHE   B CE1  1 
ATOM   5620 C  CE2  . PHE   B 1 116 ? 38.362 -21.651 -5.066  1.00 11.85 ?  116  PHE   B CE2  1 
ATOM   5621 C  CZ   . PHE   B 1 116 ? 39.005 -21.450 -3.875  1.00 11.90 ?  116  PHE   B CZ   1 
ATOM   5622 H  H    . PHE   B 1 116 ? 35.399 -17.839 -3.065  1.00 13.51 ?  116  PHE   B H    1 
ATOM   5623 H  HA   . PHE   B 1 116 ? 37.000 -16.850 -4.878  1.00 13.72 ?  116  PHE   B HA   1 
ATOM   5624 H  HB2  . PHE   B 1 116 ? 35.194 -19.011 -5.103  1.00 13.71 ?  116  PHE   B HB2  1 
ATOM   5625 H  HB3  . PHE   B 1 116 ? 36.162 -18.605 -6.286  1.00 13.71 ?  116  PHE   B HB3  1 
ATOM   5626 H  HD1  . PHE   B 1 116 ? 37.590 -18.642 -3.054  1.00 14.84 ?  116  PHE   B HD1  1 
ATOM   5627 H  HD2  . PHE   B 1 116 ? 36.992 -20.870 -6.319  1.00 14.32 ?  116  PHE   B HD2  1 
ATOM   5628 H  HE1  . PHE   B 1 116 ? 39.161 -20.186 -2.313  1.00 15.22 ?  116  PHE   B HE1  1 
ATOM   5629 H  HE2  . PHE   B 1 116 ? 38.554 -22.400 -5.579  1.00 14.21 ?  116  PHE   B HE2  1 
ATOM   5630 H  HZ   . PHE   B 1 116 ? 39.639 -22.059 -3.576  1.00 14.27 ?  116  PHE   B HZ   1 
ATOM   5631 N  N    . ASN   B 1 117 ? 33.925 -16.164 -5.322  1.00 11.92 ?  117  ASN   B N    1 
ATOM   5632 C  CA   . ASN   B 1 117 ? 32.976 -15.453 -6.180  1.00 12.06 ?  117  ASN   B CA   1 
ATOM   5633 C  C    . ASN   B 1 117 ? 33.291 -13.975 -6.332  1.00 12.44 ?  117  ASN   B C    1 
ATOM   5634 O  O    . ASN   B 1 117 ? 32.694 -13.316 -7.187  1.00 13.55 ?  117  ASN   B O    1 
ATOM   5635 C  CB   . ASN   B 1 117 ? 31.558 -15.676 -5.682  1.00 12.34 ?  117  ASN   B CB   1 
ATOM   5636 C  CG   . ASN   B 1 117 ? 31.103 -17.081 -5.943  1.00 12.46 ?  117  ASN   B CG   1 
ATOM   5637 O  OD1  . ASN   B 1 117 ? 31.462 -17.667 -6.966  1.00 13.94 ?  117  ASN   B OD1  1 
ATOM   5638 N  ND2  . ASN   B 1 117 ? 30.371 -17.657 -5.009  1.00 12.38 ?  117  ASN   B ND2  1 
ATOM   5639 H  H    . ASN   B 1 117 ? 33.599 -16.427 -4.570  1.00 14.30 ?  117  ASN   B H    1 
ATOM   5640 H  HA   . ASN   B 1 117 ? 33.027 -15.848 -7.060  1.00 14.46 ?  117  ASN   B HA   1 
ATOM   5641 H  HB2  . ASN   B 1 117 ? 31.518 -15.519 -4.720  1.00 14.80 ?  117  ASN   B HB2  1 
ATOM   5642 H  HB3  . ASN   B 1 117 ? 30.953 -15.064 -6.138  1.00 14.80 ?  117  ASN   B HB3  1 
ATOM   5643 H  HD21 . ASN   B 1 117 ? 30.091 -18.465 -5.116  1.00 14.85 ?  117  ASN   B HD21 1 
ATOM   5644 H  HD22 . ASN   B 1 117 ? 30.145 -17.219 -4.301  1.00 14.85 ?  117  ASN   B HD22 1 
ATOM   5645 N  N    . GLN   B 1 118 ? 34.226 -13.454 -5.554  1.00 11.92 ?  118  GLN   B N    1 
ATOM   5646 C  CA   . GLN   B 1 118 ? 34.652 -12.067 -5.686  1.00 12.56 ?  118  GLN   B CA   1 
ATOM   5647 C  C    . GLN   B 1 118 ? 35.719 -11.874 -6.757  1.00 12.90 ?  118  GLN   B C    1 
ATOM   5648 O  O    . GLN   B 1 118 ? 36.189 -10.745 -6.936  1.00 14.27 ?  118  GLN   B O    1 
ATOM   5649 C  CB   . GLN   B 1 118 ? 35.128 -11.534 -4.329  1.00 13.18 ?  118  GLN   B CB   1 
ATOM   5650 C  CG   . GLN   B 1 118 ? 34.049 -11.576 -3.260  1.00 13.40 ?  118  GLN   B CG   1 
ATOM   5651 C  CD   . GLN   B 1 118 ? 32.875 -10.671 -3.591  1.00 13.17 ?  118  GLN   B CD   1 
ATOM   5652 O  OE1  . GLN   B 1 118 ? 33.057 -9.530  -4.041  1.00 13.97 ?  118  GLN   B OE1  1 
ATOM   5653 N  NE2  . GLN   B 1 118 ? 31.665 -11.168 -3.374  1.00 13.78 ?  118  GLN   B NE2  1 
ATOM   5654 H  H    . GLN   B 1 118 ? 34.640 -13.883 -4.930  1.00 14.30 ?  118  GLN   B H    1 
ATOM   5655 H  HA   . GLN   B 1 118 ? 33.883 -11.538 -5.951  1.00 15.06 ?  118  GLN   B HA   1 
ATOM   5656 H  HB2  . GLN   B 1 118 ? 35.873 -12.065 -4.019  1.00 15.81 ?  118  GLN   B HB2  1 
ATOM   5657 H  HB3  . GLN   B 1 118 ? 35.401 -10.605 -4.430  1.00 15.81 ?  118  GLN   B HB3  1 
ATOM   5658 H  HG2  . GLN   B 1 118 ? 33.717 -12.485 -3.180  1.00 16.07 ?  118  GLN   B HG2  1 
ATOM   5659 H  HG3  . GLN   B 1 118 ? 34.426 -11.286 -2.413  1.00 16.07 ?  118  GLN   B HG3  1 
ATOM   5660 H  HE21 . GLN   B 1 118 ? 31.581 -11.963 -3.056  1.00 16.53 ?  118  GLN   B HE21 1 
ATOM   5661 H  HE22 . GLN   B 1 118 ? 30.975 -10.693 -3.543  1.00 16.53 ?  118  GLN   B HE22 1 
ATOM   5662 N  N    . HIS   B 1 119 ? 36.071 -12.928 -7.495  1.00 12.38 ?  119  HIS   B N    1 
ATOM   5663 C  CA   . HIS   B 1 119 ? 37.113 -12.877 -8.511  1.00 12.78 ?  119  HIS   B CA   1 
ATOM   5664 C  C    . HIS   B 1 119 ? 36.636 -13.607 -9.752  1.00 12.93 ?  119  HIS   B C    1 
ATOM   5665 O  O    . HIS   B 1 119 ? 36.124 -14.724 -9.652  1.00 13.69 ?  119  HIS   B O    1 
ATOM   5666 C  CB   . HIS   B 1 119 ? 38.399 -13.506 -7.971  1.00 13.31 ?  119  HIS   B CB   1 
ATOM   5667 C  CG   . HIS   B 1 119 ? 38.878 -12.825 -6.735  1.00 14.27 ?  119  HIS   B CG   1 
ATOM   5668 N  ND1  . HIS   B 1 119 ? 39.674 -11.700 -6.769  1.00 16.12 ?  119  HIS   B ND1  1 
ATOM   5669 C  CD2  . HIS   B 1 119 ? 38.585 -13.043 -5.433  1.00 15.51 ?  119  HIS   B CD2  1 
ATOM   5670 C  CE1  . HIS   B 1 119 ? 39.881 -11.278 -5.535  1.00 16.94 ?  119  HIS   B CE1  1 
ATOM   5671 N  NE2  . HIS   B 1 119 ? 39.220 -12.067 -4.707  1.00 16.89 ?  119  HIS   B NE2  1 
ATOM   5672 H  H    . HIS   B 1 119 ? 35.697 -13.704 -7.430  1.00 14.85 ?  119  HIS   B H    1 
ATOM   5673 H  HA   . HIS   B 1 119 ? 37.291 -11.949 -8.744  1.00 15.33 ?  119  HIS   B HA   1 
ATOM   5674 H  HB2  . HIS   B 1 119 ? 38.235 -14.436 -7.764  1.00 15.97 ?  119  HIS   B HB2  1 
ATOM   5675 H  HB3  . HIS   B 1 119 ? 39.094 -13.430 -8.647  1.00 15.97 ?  119  HIS   B HB3  1 
ATOM   5676 H  HD2  . HIS   B 1 119 ? 38.053 -13.728 -5.095  1.00 18.61 ?  119  HIS   B HD2  1 
ATOM   5677 H  HE1  . HIS   B 1 119 ? 40.413 -10.556 -5.285  1.00 20.32 ?  119  HIS   B HE1  1 
ATOM   5678 H  HE2  . HIS   B 1 119 ? 39.228 -12.010 -3.847  1.00 20.26 ?  119  HIS   B HE2  1 
ATOM   5679 N  N    . GLU   B 1 120 ? 36.800 -12.987 -10.921 1.00 13.24 ?  120  GLU   B N    1 
ATOM   5680 C  CA   . GLU   B 1 120 ? 36.204 -13.564 -12.121 1.00 15.04 ?  120  GLU   B CA   1 
ATOM   5681 C  C    . GLU   B 1 120 ? 36.880 -14.864 -12.541 1.00 13.51 ?  120  GLU   B C    1 
ATOM   5682 O  O    . GLU   B 1 120 ? 36.217 -15.739 -13.109 1.00 13.82 ?  120  GLU   B O    1 
ATOM   5683 C  CB   . GLU   B 1 120 ? 36.212 -12.549 -13.260 1.00 18.99 ?  120  GLU   B CB   1 
ATOM   5684 C  CG   . GLU   B 1 120 ? 35.260 -11.390 -13.027 1.00 24.93 ?  120  GLU   B CG   1 
ATOM   5685 C  CD   . GLU   B 1 120 ? 35.050 -10.542 -14.259 1.00 30.07 ?  120  GLU   B CD   1 
ATOM   5686 O  OE1  . GLU   B 1 120 ? 36.023 -10.339 -15.015 1.00 32.00 ?  120  GLU   B OE1  1 
ATOM   5687 O  OE2  . GLU   B 1 120 ? 33.908 -10.082 -14.470 1.00 32.97 -1 120  GLU   B OE2  1 
ATOM   5688 H  H    . GLU   B 1 120 ? 37.232 -12.251 -11.044 1.00 15.88 ?  120  GLU   B H    1 
ATOM   5689 H  HA   . GLU   B 1 120 ? 35.279 -13.773 -11.930 1.00 18.04 ?  120  GLU   B HA   1 
ATOM   5690 H  HB2  . GLU   B 1 120 ? 37.100 -12.182 -13.361 1.00 22.78 ?  120  GLU   B HB2  1 
ATOM   5691 H  HB3  . GLU   B 1 120 ? 35.938 -12.990 -14.082 1.00 22.78 ?  120  GLU   B HB3  1 
ATOM   5692 H  HG2  . GLU   B 1 120 ? 34.394 -11.736 -12.755 1.00 29.91 ?  120  GLU   B HG2  1 
ATOM   5693 H  HG3  . GLU   B 1 120 ? 35.619 -10.816 -12.334 1.00 29.91 ?  120  GLU   B HG3  1 
ATOM   5694 N  N    . VAL   B 1 121 ? 38.178 -15.006 -12.279 1.00 13.03 ?  121  VAL   B N    1 
ATOM   5695 C  CA   . VAL   B 1 121 ? 38.922 -16.214 -12.627 1.00 12.78 ?  121  VAL   B CA   1 
ATOM   5696 C  C    . VAL   B 1 121 ? 40.032 -16.425 -11.605 1.00 12.33 ?  121  VAL   B C    1 
ATOM   5697 O  O    . VAL   B 1 121 ? 40.713 -15.473 -11.205 1.00 13.13 ?  121  VAL   B O    1 
ATOM   5698 C  CB   . VAL   B 1 121 ? 39.433 -16.171 -14.086 1.00 14.77 ?  121  VAL   B CB   1 
ATOM   5699 C  CG1  . VAL   B 1 121 ? 40.285 -14.937 -14.343 1.00 15.91 ?  121  VAL   B CG1  1 
ATOM   5700 C  CG2  . VAL   B 1 121 ? 40.193 -17.439 -14.431 1.00 16.34 ?  121  VAL   B CG2  1 
ATOM   5701 H  H    . VAL   B 1 121 ? 38.662 -14.400 -11.902 1.00 15.63 ?  121  VAL   B H    1 
ATOM   5702 H  HA   . VAL   B 1 121 ? 38.312 -16.964 -12.561 1.00 15.33 ?  121  VAL   B HA   1 
ATOM   5703 H  HB   . VAL   B 1 121 ? 38.666 -16.121 -14.681 1.00 17.72 ?  121  VAL   B HB   1 
ATOM   5704 H  HG11 . VAL   B 1 121 ? 40.603 -14.956 -15.261 1.00 19.09 ?  121  VAL   B HG11 1 
ATOM   5705 H  HG12 . VAL   B 1 121 ? 39.747 -14.141 -14.201 1.00 19.09 ?  121  VAL   B HG12 1 
ATOM   5706 H  HG13 . VAL   B 1 121 ? 41.040 -14.938 -13.734 1.00 19.09 ?  121  VAL   B HG13 1 
ATOM   5707 H  HG21 . VAL   B 1 121 ? 40.385 -17.443 -15.383 1.00 19.60 ?  121  VAL   B HG21 1 
ATOM   5708 H  HG22 . VAL   B 1 121 ? 41.024 -17.457 -13.930 1.00 19.60 ?  121  VAL   B HG22 1 
ATOM   5709 H  HG23 . VAL   B 1 121 ? 39.649 -18.207 -14.201 1.00 19.60 ?  121  VAL   B HG23 1 
ATOM   5710 N  N    . LEU   B 1 122 ? 40.211 -17.679 -11.178 1.00 11.91 ?  122  LEU   B N    1 
ATOM   5711 C  CA   . LEU   B 1 122 ? 41.196 -18.024 -10.160 1.00 11.61 ?  122  LEU   B CA   1 
ATOM   5712 C  C    . LEU   B 1 122 ? 41.858 -19.353 -10.488 1.00 11.38 ?  122  LEU   B C    1 
ATOM   5713 O  O    . LEU   B 1 122 ? 41.200 -20.280 -10.983 1.00 12.62 ?  122  LEU   B O    1 
ATOM   5714 C  CB   . LEU   B 1 122 ? 40.549 -18.256 -8.781  1.00 13.35 ?  122  LEU   B CB   1 
ATOM   5715 C  CG   . LEU   B 1 122 ? 39.516 -17.235 -8.296  1.00 13.89 ?  122  LEU   B CG   1 
ATOM   5716 C  CD1  . LEU   B 1 122 ? 38.115 -17.606 -8.764  1.00 14.79 ?  122  LEU   B CD1  1 
ATOM   5717 C  CD2  . LEU   B 1 122 ? 39.567 -17.122 -6.789  1.00 13.16 ?  122  LEU   B CD2  1 
ATOM   5718 H  H    . LEU   B 1 122 ? 39.773 -18.355 -11.469 1.00 14.28 ?  122  LEU   B H    1 
ATOM   5719 H  HA   . LEU   B 1 122 ? 41.869 -17.324 -10.081 1.00 13.92 ?  122  LEU   B HA   1 
ATOM   5720 H  HB2  . LEU   B 1 122 ? 40.107 -19.112 -8.797  1.00 16.02 ?  122  LEU   B HB2  1 
ATOM   5721 H  HB3  . LEU   B 1 122 ? 41.256 -18.270 -8.116  1.00 16.02 ?  122  LEU   B HB3  1 
ATOM   5722 H  HG   . LEU   B 1 122 ? 39.731 -16.360 -8.663  1.00 16.66 ?  122  LEU   B HG   1 
ATOM   5723 H  HD11 . LEU   B 1 122 ? 37.482 -16.962 -8.409  1.00 17.74 ?  122  LEU   B HD11 1 
ATOM   5724 H  HD12 . LEU   B 1 122 ? 38.093 -17.588 -9.734  1.00 17.74 ?  122  LEU   B HD12 1 
ATOM   5725 H  HD13 . LEU   B 1 122 ? 37.902 -18.494 -8.443  1.00 17.74 ?  122  LEU   B HD13 1 
ATOM   5726 H  HD21 . LEU   B 1 122 ? 38.884 -16.502 -6.488  1.00 15.79 ?  122  LEU   B HD21 1 
ATOM   5727 H  HD22 . LEU   B 1 122 ? 39.415 -17.996 -6.399  1.00 15.79 ?  122  LEU   B HD22 1 
ATOM   5728 H  HD23 . LEU   B 1 122 ? 40.445 -16.793 -6.524  1.00 15.79 ?  122  LEU   B HD23 1 
ATOM   5729 N  N    . LEU   B 1 123 ? 43.143 -19.455 -10.129 1.00 11.18 ?  123  LEU   B N    1 
ATOM   5730 C  CA   . LEU   B 1 123 ? 43.855 -20.725 -10.011 1.00 11.52 ?  123  LEU   B CA   1 
ATOM   5731 C  C    . LEU   B 1 123 ? 43.828 -21.123 -8.541  1.00 11.18 ?  123  LEU   B C    1 
ATOM   5732 O  O    . LEU   B 1 123 ? 44.176 -20.302 -7.684  1.00 11.61 ?  123  LEU   B O    1 
ATOM   5733 C  CB   . LEU   B 1 123 ? 45.300 -20.550 -10.475 1.00 12.11 ?  123  LEU   B CB   1 
ATOM   5734 C  CG   . LEU   B 1 123 ? 46.245 -21.731 -10.229 1.00 12.32 ?  123  LEU   B CG   1 
ATOM   5735 C  CD1  . LEU   B 1 123 ? 45.818 -22.982 -10.995 1.00 12.70 ?  123  LEU   B CD1  1 
ATOM   5736 C  CD2  . LEU   B 1 123 ? 47.668 -21.345 -10.594 1.00 13.14 ?  123  LEU   B CD2  1 
ATOM   5737 H  H    . LEU   B 1 123 ? 43.632 -18.770 -9.923  1.00 13.40 ?  123  LEU   B H    1 
ATOM   5738 H  HA   . LEU   B 1 123 ? 43.412 -21.405 -10.539 1.00 13.82 ?  123  LEU   B HA   1 
ATOM   5739 H  HB2  . LEU   B 1 123 ? 45.286 -20.381 -11.430 1.00 14.53 ?  123  LEU   B HB2  1 
ATOM   5740 H  HB3  . LEU   B 1 123 ? 45.671 -19.779 -10.019 1.00 14.53 ?  123  LEU   B HB3  1 
ATOM   5741 H  HG   . LEU   B 1 123 ? 46.233 -21.948 -9.284  1.00 14.78 ?  123  LEU   B HG   1 
ATOM   5742 H  HD11 . LEU   B 1 123 ? 46.453 -23.691 -10.812 1.00 15.24 ?  123  LEU   B HD11 1 
ATOM   5743 H  HD12 . LEU   B 1 123 ? 44.932 -23.247 -10.698 1.00 15.24 ?  123  LEU   B HD12 1 
ATOM   5744 H  HD13 . LEU   B 1 123 ? 45.804 -22.781 -11.942 1.00 15.24 ?  123  LEU   B HD13 1 
ATOM   5745 H  HD21 . LEU   B 1 123 ? 48.253 -22.099 -10.433 1.00 15.76 ?  123  LEU   B HD21 1 
ATOM   5746 H  HD22 . LEU   B 1 123 ? 47.699 -21.093 -11.531 1.00 15.76 ?  123  LEU   B HD22 1 
ATOM   5747 H  HD23 . LEU   B 1 123 ? 47.942 -20.590 -10.044 1.00 15.76 ?  123  LEU   B HD23 1 
ATOM   5748 N  N    . ALA   B 1 124 ? 43.397 -22.353 -8.237  1.00 11.05 ?  124  ALA   B N    1 
ATOM   5749 C  CA   . ALA   B 1 124 ? 43.133 -22.674 -6.841  1.00 11.26 ?  124  ALA   B CA   1 
ATOM   5750 C  C    . ALA   B 1 124 ? 43.410 -24.135 -6.519  1.00 10.92 ?  124  ALA   B C    1 
ATOM   5751 O  O    . ALA   B 1 124 ? 43.273 -25.012 -7.385  1.00 11.49 ?  124  ALA   B O    1 
ATOM   5752 C  CB   . ALA   B 1 124 ? 41.679 -22.364 -6.469  1.00 12.05 ?  124  ALA   B CB   1 
ATOM   5753 H  H    . ALA   B 1 124 ? 43.237 -22.991 -8.803  1.00 13.26 ?  124  ALA   B H    1 
ATOM   5754 H  HA   . ALA   B 1 124 ? 43.708 -22.127 -6.294  1.00 13.50 ?  124  ALA   B HA   1 
ATOM   5755 H  HB1  . ALA   B 1 124 ? 41.531 -22.586 -5.536  1.00 14.45 ?  124  ALA   B HB1  1 
ATOM   5756 H  HB2  . ALA   B 1 124 ? 41.512 -21.416 -6.611  1.00 14.45 ?  124  ALA   B HB2  1 
ATOM   5757 H  HB3  . ALA   B 1 124 ? 41.084 -22.888 -7.031  1.00 14.45 ?  124  ALA   B HB3  1 
ATOM   5758 N  N    . PRO   B 1 125 ? 43.701 -24.432 -5.253  1.00 11.25 ?  125  PRO   B N    1 
ATOM   5759 C  CA   . PRO   B 1 125 ? 43.642 -25.798 -4.731  1.00 12.00 ?  125  PRO   B CA   1 
ATOM   5760 C  C    . PRO   B 1 125 ? 42.241 -26.070 -4.185  1.00 12.13 ?  125  PRO   B C    1 
ATOM   5761 O  O    . PRO   B 1 125 ? 41.443 -25.152 -3.981  1.00 12.47 ?  125  PRO   B O    1 
ATOM   5762 C  CB   . PRO   B 1 125 ? 44.633 -25.722 -3.563  1.00 12.87 ?  125  PRO   B CB   1 
ATOM   5763 C  CG   . PRO   B 1 125 ? 44.387 -24.337 -2.992  1.00 12.86 ?  125  PRO   B CG   1 
ATOM   5764 C  CD   . PRO   B 1 125 ? 44.033 -23.465 -4.190  1.00 11.66 ?  125  PRO   B CD   1 
ATOM   5765 H  HA   . PRO   B 1 125 ? 43.917 -26.461 -5.380  1.00 14.40 ?  125  PRO   B HA   1 
ATOM   5766 H  HB2  . PRO   B 1 125 ? 44.430 -26.404 -2.902  1.00 15.43 ?  125  PRO   B HB2  1 
ATOM   5767 H  HB3  . PRO   B 1 125 ? 45.543 -25.806 -3.884  1.00 15.43 ?  125  PRO   B HB3  1 
ATOM   5768 H  HG2  . PRO   B 1 125 ? 43.650 -24.358 -2.360  1.00 15.43 ?  125  PRO   B HG2  1 
ATOM   5769 H  HG3  . PRO   B 1 125 ? 45.195 -24.006 -2.555  1.00 15.43 ?  125  PRO   B HG3  1 
ATOM   5770 H  HD2  . PRO   B 1 125 ? 43.271 -22.899 -3.989  1.00 13.99 ?  125  PRO   B HD2  1 
ATOM   5771 H  HD3  . PRO   B 1 125 ? 44.806 -22.924 -4.452  1.00 13.99 ?  125  PRO   B HD3  1 
ATOM   5772 N  N    . LEU   B 1 126 ? 41.968 -27.347 -3.909  1.00 12.40 ?  126  LEU   B N    1 
ATOM   5773 C  CA   . LEU   B 1 126 ? 40.745 -27.710 -3.201  1.00 13.11 ?  126  LEU   B CA   1 
ATOM   5774 C  C    . LEU   B 1 126 ? 40.863 -27.313 -1.738  1.00 12.96 ?  126  LEU   B C    1 
ATOM   5775 O  O    . LEU   B 1 126 ? 41.759 -27.771 -1.023  1.00 14.92 ?  126  LEU   B O    1 
ATOM   5776 C  CB   . LEU   B 1 126 ? 40.489 -29.204 -3.318  1.00 14.40 ?  126  LEU   B CB   1 
ATOM   5777 C  CG   . LEU   B 1 126 ? 39.975 -29.693 -4.671  1.00 15.29 ?  126  LEU   B CG   1 
ATOM   5778 C  CD1  . LEU   B 1 126 ? 40.016 -31.202 -4.724  1.00 16.88 ?  126  LEU   B CD1  1 
ATOM   5779 C  CD2  . LEU   B 1 126 ? 38.563 -29.189 -4.930  1.00 15.50 ?  126  LEU   B CD2  1 
ATOM   5780 H  H    . LEU   B 1 126 ? 42.478 -28.011 -4.106  1.00 14.87 ?  126  LEU   B H    1 
ATOM   5781 H  HA   . LEU   B 1 126 ? 39.998 -27.229 -3.591  1.00 15.73 ?  126  LEU   B HA   1 
ATOM   5782 H  HB2  . LEU   B 1 126 ? 41.316 -29.668 -3.138  1.00 17.28 ?  126  LEU   B HB2  1 
ATOM   5783 H  HB3  . LEU   B 1 126 ? 39.825 -29.447 -2.655  1.00 17.28 ?  126  LEU   B HB3  1 
ATOM   5784 H  HG   . LEU   B 1 126 ? 40.551 -29.346 -5.376  1.00 18.34 ?  126  LEU   B HG   1 
ATOM   5785 H  HD11 . LEU   B 1 126 ? 39.683 -31.498 -5.587  1.00 20.24 ?  126  LEU   B HD11 1 
ATOM   5786 H  HD12 . LEU   B 1 126 ? 40.928 -31.500 -4.600  1.00 20.24 ?  126  LEU   B HD12 1 
ATOM   5787 H  HD13 . LEU   B 1 126 ? 39.452 -31.556 -4.016  1.00 20.24 ?  126  LEU   B HD13 1 
ATOM   5788 H  HD21 . LEU   B 1 126 ? 38.222 -29.603 -5.739  1.00 18.59 ?  126  LEU   B HD21 1 
ATOM   5789 H  HD22 . LEU   B 1 126 ? 38.001 -29.424 -4.176  1.00 18.59 ?  126  LEU   B HD22 1 
ATOM   5790 H  HD23 . LEU   B 1 126 ? 38.582 -28.223 -5.038  1.00 18.59 ?  126  LEU   B HD23 1 
ATOM   5791 N  N    . LEU   B 1 127 ? 39.942 -26.474 -1.283  1.00 12.96 ?  127  LEU   B N    1 
ATOM   5792 C  CA   . LEU   B 1 127 ? 39.995 -25.988 0.083   1.00 13.16 ?  127  LEU   B CA   1 
ATOM   5793 C  C    . LEU   B 1 127 ? 39.717 -27.110 1.072   1.00 13.13 ?  127  LEU   B C    1 
ATOM   5794 O  O    . LEU   B 1 127 ? 38.898 -28.006 0.837   1.00 13.38 ?  127  LEU   B O    1 
ATOM   5795 C  CB   . LEU   B 1 127 ? 38.971 -24.870 0.289   1.00 13.69 ?  127  LEU   B CB   1 
ATOM   5796 C  CG   . LEU   B 1 127 ? 39.153 -23.606 -0.548  1.00 14.57 ?  127  LEU   B CG   1 
ATOM   5797 C  CD1  . LEU   B 1 127 ? 38.038 -22.631 -0.225  1.00 14.95 ?  127  LEU   B CD1  1 
ATOM   5798 C  CD2  . LEU   B 1 127 ? 40.518 -22.969 -0.316  1.00 14.96 ?  127  LEU   B CD2  1 
ATOM   5799 H  H    . LEU   B 1 127 ? 39.278 -26.159 -1.746  1.00 15.54 ?  127  LEU   B H    1 
ATOM   5800 H  HA   . LEU   B 1 127 ? 40.877 -25.624 0.263   1.00 15.79 ?  127  LEU   B HA   1 
ATOM   5801 H  HB2  . LEU   B 1 127 ? 38.088 -25.226 0.085   1.00 16.42 ?  127  LEU   B HB2  1 
ATOM   5802 H  HB3  . LEU   B 1 127 ? 38.993 -24.603 1.222   1.00 16.42 ?  127  LEU   B HB3  1 
ATOM   5803 H  HG   . LEU   B 1 127 ? 39.075 -23.832 -1.486  1.00 17.48 ?  127  LEU   B HG   1 
ATOM   5804 H  HD11 . LEU   B 1 127 ? 38.163 -21.821 -0.750  1.00 17.93 ?  127  LEU   B HD11 1 
ATOM   5805 H  HD12 . LEU   B 1 127 ? 37.185 -23.034 -0.439  1.00 17.93 ?  127  LEU   B HD12 1 
ATOM   5806 H  HD13 . LEU   B 1 127 ? 38.073 -22.412 0.722   1.00 17.93 ?  127  LEU   B HD13 1 
ATOM   5807 H  HD21 . LEU   B 1 127 ? 40.550 -22.113 -0.773  1.00 17.94 ?  127  LEU   B HD21 1 
ATOM   5808 H  HD22 . LEU   B 1 127 ? 40.648 -22.837 0.637   1.00 17.94 ?  127  LEU   B HD22 1 
ATOM   5809 H  HD23 . LEU   B 1 127 ? 41.202 -23.558 -0.666  1.00 17.94 ?  127  LEU   B HD23 1 
ATOM   5810 N  N    . SER   B 1 128 ? 40.398 -27.028 2.204   1.00 13.19 ?  128  SER   B N    1 
ATOM   5811 C  CA   . SER   B 1 128 ? 40.293 -27.949 3.324   1.00 13.54 ?  128  SER   B CA   1 
ATOM   5812 C  C    . SER   B 1 128 ? 40.783 -29.356 2.994   1.00 14.38 ?  128  SER   B C    1 
ATOM   5813 O  O    . SER   B 1 128 ? 40.693 -30.236 3.846   1.00 15.82 ?  128  SER   B O    1 
ATOM   5814 C  CB   . SER   B 1 128 ? 38.894 -27.954 3.958   1.00 13.93 ?  128  SER   B CB   1 
ATOM   5815 O  OG   . SER   B 1 128 ? 38.585 -26.676 4.512   1.00 14.50 ?  128  SER   B OG   1 
ATOM   5816 H  H    . SER   B 1 128 ? 40.967 -26.400 2.352   1.00 15.82 ?  128  SER   B H    1 
ATOM   5817 H  HA   . SER   B 1 128 ? 40.884 -27.617 4.007   1.00 16.25 ?  128  SER   B HA   1 
ATOM   5818 H  HB2  . SER   B 1 128 ? 38.232 -28.185 3.285   1.00 16.71 ?  128  SER   B HB2  1 
ATOM   5819 H  HB3  . SER   B 1 128 ? 38.874 -28.630 4.670   1.00 16.71 ?  128  SER   B HB3  1 
ATOM   5820 H  HG   . SER   B 1 128 ? 39.156 -26.487 5.100   1.00 17.39 ?  128  SER   B HG   1 
ATOM   5821 N  N    . ALA   B 1 129 ? 41.346 -29.577 1.802   1.00 15.20 ?  129  ALA   B N    1 
ATOM   5822 C  CA   . ALA   B 1 129 ? 41.892 -30.874 1.443   1.00 16.44 ?  129  ALA   B CA   1 
ATOM   5823 C  C    . ALA   B 1 129 ? 43.281 -31.054 2.048   1.00 15.74 ?  129  ALA   B C    1 
ATOM   5824 O  O    . ALA   B 1 129 ? 43.843 -30.157 2.693   1.00 15.41 ?  129  ALA   B O    1 
ATOM   5825 C  CB   . ALA   B 1 129 ? 41.953 -31.028 -0.076  1.00 18.49 ?  129  ALA   B CB   1 
ATOM   5826 H  H    . ALA   B 1 129 ? 41.417 -28.985 1.176   1.00 18.23 ?  129  ALA   B H    1 
ATOM   5827 H  HA   . ALA   B 1 129 ? 41.315 -31.569 1.789   1.00 19.72 ?  129  ALA   B HA   1 
ATOM   5828 H  HB1  . ALA   B 1 129 ? 42.312 -31.906 -0.292  1.00 22.19 ?  129  ALA   B HB1  1 
ATOM   5829 H  HB2  . ALA   B 1 129 ? 41.060 -30.940 -0.440  1.00 22.19 ?  129  ALA   B HB2  1 
ATOM   5830 H  HB3  . ALA   B 1 129 ? 42.530 -30.339 -0.443  1.00 22.19 ?  129  ALA   B HB3  1 
ATOM   5831 N  N    . GLY   B 1 130 ? 43.843 -32.239 1.818   1.00 15.53 ?  130  GLY   B N    1 
ATOM   5832 C  CA   . GLY   B 1 130 ? 45.228 -32.480 2.174   1.00 16.21 ?  130  GLY   B CA   1 
ATOM   5833 C  C    . GLY   B 1 130 ? 45.438 -32.379 3.666   1.00 16.16 ?  130  GLY   B C    1 
ATOM   5834 O  O    . GLY   B 1 130 ? 44.736 -33.017 4.466   1.00 17.02 ?  130  GLY   B O    1 
ATOM   5835 H  H    . GLY   B 1 130 ? 43.450 -32.911 1.448   1.00 18.63 ?  130  GLY   B H    1 
ATOM   5836 H  HA2  . GLY   B 1 130 ? 45.492 -33.371 1.883   1.00 19.44 ?  130  GLY   B HA2  1 
ATOM   5837 H  HA3  . GLY   B 1 130 ? 45.799 -31.832 1.733   1.00 19.44 ?  130  GLY   B HA3  1 
ATOM   5838 N  N    . ILE   B 1 131 ? 46.416 -31.554 4.051   1.00 16.24 ?  131  ILE   B N    1 
ATOM   5839 C  CA   . ILE   B 1 131 ? 46.778 -31.424 5.455   1.00 17.06 ?  131  ILE   B CA   1 
ATOM   5840 C  C    . ILE   B 1 131 ? 45.664 -30.825 6.294   1.00 16.61 ?  131  ILE   B C    1 
ATOM   5841 O  O    . ILE   B 1 131 ? 45.742 -30.893 7.525   1.00 18.09 ?  131  ILE   B O    1 
ATOM   5842 C  CB   . ILE   B 1 131 ? 48.101 -30.646 5.644   1.00 18.83 ?  131  ILE   B CB   1 
ATOM   5843 C  CG1  . ILE   B 1 131 ? 47.940 -29.167 5.257   1.00 19.84 ?  131  ILE   B CG1  1 
ATOM   5844 C  CG2  . ILE   B 1 131 ? 49.219 -31.296 4.835   1.00 19.59 ?  131  ILE   B CG2  1 
ATOM   5845 C  CD1  . ILE   B 1 131 ? 49.171 -28.320 5.544   1.00 21.30 ?  131  ILE   B CD1  1 
ATOM   5846 H  H    . ILE   B 1 131 ? 46.881 -31.064 3.520   1.00 19.49 ?  131  ILE   B H    1 
ATOM   5847 H  HA   . ILE   B 1 131 ? 46.926 -32.312 5.804   1.00 20.46 ?  131  ILE   B HA   1 
ATOM   5848 H  HB   . ILE   B 1 131 ? 48.337 -30.684 6.584   1.00 22.58 ?  131  ILE   B HB   1 
ATOM   5849 H  HG12 . ILE   B 1 131 ? 47.752 -29.113 4.307   1.00 23.80 ?  131  ILE   B HG12 1 
ATOM   5850 H  HG13 . ILE   B 1 131 ? 47.198 -28.783 5.757   1.00 23.80 ?  131  ILE   B HG13 1 
ATOM   5851 H  HG21 . ILE   B 1 131 ? 50.062 -30.902 5.099   1.00 23.50 ?  131  ILE   B HG21 1 
ATOM   5852 H  HG22 . ILE   B 1 131 ? 49.219 -32.245 5.017   1.00 23.50 ?  131  ILE   B HG22 1 
ATOM   5853 H  HG23 . ILE   B 1 131 ? 49.053 -31.135 3.893   1.00 23.50 ?  131  ILE   B HG23 1 
ATOM   5854 H  HD11 . ILE   B 1 131 ? 48.956 -27.389 5.377   1.00 25.55 ?  131  ILE   B HD11 1 
ATOM   5855 H  HD12 . ILE   B 1 131 ? 49.424 -28.441 6.472   1.00 25.55 ?  131  ILE   B HD12 1 
ATOM   5856 H  HD13 . ILE   B 1 131 ? 49.890 -28.605 4.962   1.00 25.55 ?  131  ILE   B HD13 1 
ATOM   5857 N  N    . PHE   B 1 132 ? 44.636 -30.239 5.668   1.00 15.39 ?  132  PHE   B N    1 
ATOM   5858 C  CA   . PHE   B 1 132 ? 43.483 -29.728 6.400   1.00 15.73 ?  132  PHE   B CA   1 
ATOM   5859 C  C    . PHE   B 1 132 ? 42.459 -30.816 6.725   1.00 17.25 ?  132  PHE   B C    1 
ATOM   5860 O  O    . PHE   B 1 132 ? 41.553 -30.569 7.527   1.00 18.86 ?  132  PHE   B O    1 
ATOM   5861 C  CB   . PHE   B 1 132 ? 42.807 -28.593 5.620   1.00 14.76 ?  132  PHE   B CB   1 
ATOM   5862 C  CG   . PHE   B 1 132 ? 43.510 -27.256 5.728   1.00 14.73 ?  132  PHE   B CG   1 
ATOM   5863 C  CD1  . PHE   B 1 132 ? 44.803 -27.080 5.260   1.00 15.95 ?  132  PHE   B CD1  1 
ATOM   5864 C  CD2  . PHE   B 1 132 ? 42.837 -26.155 6.249   1.00 14.54 ?  132  PHE   B CD2  1 
ATOM   5865 C  CE1  . PHE   B 1 132 ? 45.427 -25.844 5.349   1.00 16.55 ?  132  PHE   B CE1  1 
ATOM   5866 C  CE2  . PHE   B 1 132 ? 43.450 -24.915 6.334   1.00 15.15 ?  132  PHE   B CE2  1 
ATOM   5867 C  CZ   . PHE   B 1 132 ? 44.750 -24.764 5.884   1.00 16.00 ?  132  PHE   B CZ   1 
ATOM   5868 H  H    . PHE   B 1 132 ? 44.587 -30.122 4.815   1.00 18.46 ?  132  PHE   B H    1 
ATOM   5869 H  HA   . PHE   B 1 132 ? 43.793 -29.357 7.239   1.00 18.87 ?  132  PHE   B HA   1 
ATOM   5870 H  HB2  . PHE   B 1 132 ? 42.784 -28.833 4.684   1.00 17.71 ?  132  PHE   B HB2  1 
ATOM   5871 H  HB3  . PHE   B 1 132 ? 41.903 -28.480 5.955   1.00 17.71 ?  132  PHE   B HB3  1 
ATOM   5872 H  HD1  . PHE   B 1 132 ? 45.264 -27.808 4.906   1.00 19.13 ?  132  PHE   B HD1  1 
ATOM   5873 H  HD2  . PHE   B 1 132 ? 41.963 -26.254 6.555   1.00 17.44 ?  132  PHE   B HD2  1 
ATOM   5874 H  HE1  . PHE   B 1 132 ? 46.300 -25.743 5.046   1.00 19.86 ?  132  PHE   B HE1  1 
ATOM   5875 H  HE2  . PHE   B 1 132 ? 42.993 -24.186 6.697   1.00 18.18 ?  132  PHE   B HE2  1 
ATOM   5876 H  HZ   . PHE   B 1 132 ? 45.169 -23.930 5.943   1.00 19.20 ?  132  PHE   B HZ   1 
ATOM   5877 N  N    . GLY   B 1 133 ? 42.562 -32.006 6.122   1.00 16.79 ?  133  GLY   B N    1 
ATOM   5878 C  CA   . GLY   B 1 133 ? 41.854 -33.173 6.616   1.00 17.47 ?  133  GLY   B CA   1 
ATOM   5879 C  C    . GLY   B 1 133 ? 40.458 -33.435 6.083   1.00 17.83 ?  133  GLY   B C    1 
ATOM   5880 O  O    . GLY   B 1 133 ? 39.868 -34.450 6.460   1.00 20.08 ?  133  GLY   B O    1 
ATOM   5881 H  H    . GLY   B 1 133 ? 43.042 -32.153 5.423   1.00 20.15 ?  133  GLY   B H    1 
ATOM   5882 H  HA2  . GLY   B 1 133 ? 42.394 -33.955 6.425   1.00 20.96 ?  133  GLY   B HA2  1 
ATOM   5883 H  HA3  . GLY   B 1 133 ? 41.782 -33.097 7.579   1.00 20.96 ?  133  GLY   B HA3  1 
ATOM   5884 N  N    . ALA   B 1 134 ? 39.901 -32.577 5.240   1.00 17.03 ?  134  ALA   B N    1 
ATOM   5885 C  CA   . ALA   B 1 134 ? 38.577 -32.853 4.704   1.00 17.03 ?  134  ALA   B CA   1 
ATOM   5886 C  C    . ALA   B 1 134 ? 38.660 -33.844 3.548   1.00 17.20 ?  134  ALA   B C    1 
ATOM   5887 O  O    . ALA   B 1 134 ? 39.711 -34.032 2.932   1.00 18.13 ?  134  ALA   B O    1 
ATOM   5888 C  CB   . ALA   B 1 134 ? 37.910 -31.563 4.231   1.00 17.59 ?  134  ALA   B CB   1 
ATOM   5889 H  H    . ALA   B 1 134 ? 40.257 -31.839 4.973   1.00 20.43 ?  134  ALA   B H    1 
ATOM   5890 H  HA   . ALA   B 1 134 ? 38.025 -33.240 5.400   1.00 20.43 ?  134  ALA   B HA   1 
ATOM   5891 H  HB1  . ALA   B 1 134 ? 37.022 -31.770 3.899   1.00 21.10 ?  134  ALA   B HB1  1 
ATOM   5892 H  HB2  . ALA   B 1 134 ? 37.847 -30.947 4.978   1.00 21.10 ?  134  ALA   B HB2  1 
ATOM   5893 H  HB3  . ALA   B 1 134 ? 38.444 -31.170 3.523   1.00 21.10 ?  134  ALA   B HB3  1 
ATOM   5894 N  N    . ASP   B 1 135 ? 37.528 -34.472 3.257   1.00 17.18 ?  135  ASP   B N    1 
ATOM   5895 C  CA   . ASP   B 1 135 ? 37.431 -35.363 2.110   1.00 18.01 ?  135  ASP   B CA   1 
ATOM   5896 C  C    . ASP   B 1 135 ? 37.531 -34.524 0.844   1.00 17.03 ?  135  ASP   B C    1 
ATOM   5897 O  O    . ASP   B 1 135 ? 36.676 -33.655 0.622   1.00 16.74 ?  135  ASP   B O    1 
ATOM   5898 C  CB   . ASP   B 1 135 ? 36.088 -36.089 2.157   1.00 19.73 ?  135  ASP   B CB   1 
ATOM   5899 C  CG   . ASP   B 1 135 ? 35.909 -37.079 1.023   1.00 21.59 ?  135  ASP   B CG   1 
ATOM   5900 O  OD1  . ASP   B 1 135 ? 36.776 -37.131 0.125   1.00 21.87 ?  135  ASP   B OD1  1 
ATOM   5901 O  OD2  . ASP   B 1 135 ? 34.903 -37.825 1.044   1.00 24.59 -1 135  ASP   B OD2  1 
ATOM   5902 H  H    . ASP   B 1 135 ? 36.798 -34.391 3.703   1.00 20.61 ?  135  ASP   B H    1 
ATOM   5903 H  HA   . ASP   B 1 135 ? 38.147 -36.014 2.139   1.00 21.61 ?  135  ASP   B HA   1 
ATOM   5904 H  HB2  . ASP   B 1 135 ? 36.028 -36.578 2.991   1.00 23.67 ?  135  ASP   B HB2  1 
ATOM   5905 H  HB3  . ASP   B 1 135 ? 35.377 -35.436 2.099   1.00 23.67 ?  135  ASP   B HB3  1 
ATOM   5906 N  N    . PRO   B 1 136 ? 38.538 -34.731 -0.004  1.00 17.27 ?  136  PRO   B N    1 
ATOM   5907 C  CA   . PRO   B 1 136 ? 38.637 -33.904 -1.216  1.00 16.72 ?  136  PRO   B CA   1 
ATOM   5908 C  C    . PRO   B 1 136 ? 37.452 -34.053 -2.144  1.00 15.99 ?  136  PRO   B C    1 
ATOM   5909 O  O    . PRO   B 1 136 ? 37.132 -33.107 -2.871  1.00 15.16 ?  136  PRO   B O    1 
ATOM   5910 C  CB   . PRO   B 1 136 ? 39.949 -34.376 -1.862  1.00 17.62 ?  136  PRO   B CB   1 
ATOM   5911 C  CG   . PRO   B 1 136 ? 40.154 -35.759 -1.327  1.00 18.64 ?  136  PRO   B CG   1 
ATOM   5912 C  CD   . PRO   B 1 136 ? 39.614 -35.732 0.071   1.00 18.43 ?  136  PRO   B CD   1 
ATOM   5913 H  HA   . PRO   B 1 136 ? 38.723 -32.969 -0.979  1.00 20.06 ?  136  PRO   B HA   1 
ATOM   5914 H  HB2  . PRO   B 1 136 ? 39.858 -34.392 -2.830  1.00 21.14 ?  136  PRO   B HB2  1 
ATOM   5915 H  HB3  . PRO   B 1 136 ? 40.674 -33.791 -1.596  1.00 21.14 ?  136  PRO   B HB3  1 
ATOM   5916 H  HG2  . PRO   B 1 136 ? 39.664 -36.399 -1.868  1.00 22.37 ?  136  PRO   B HG2  1 
ATOM   5917 H  HG3  . PRO   B 1 136 ? 41.101 -35.973 -1.319  1.00 22.37 ?  136  PRO   B HG3  1 
ATOM   5918 H  HD2  . PRO   B 1 136 ? 39.251 -36.597 0.315   1.00 22.11 ?  136  PRO   B HD2  1 
ATOM   5919 H  HD3  . PRO   B 1 136 ? 40.293 -35.438 0.699   1.00 22.11 ?  136  PRO   B HD3  1 
ATOM   5920 N  N    . ILE   B 1 137 ? 36.798 -35.219 -2.154  1.00 16.07 ?  137  ILE   B N    1 
ATOM   5921 C  CA   . ILE   B 1 137 ? 35.582 -35.386 -2.945  1.00 16.89 ?  137  ILE   B CA   1 
ATOM   5922 C  C    . ILE   B 1 137 ? 34.506 -34.420 -2.468  1.00 16.56 ?  137  ILE   B C    1 
ATOM   5923 O  O    . ILE   B 1 137 ? 33.787 -33.811 -3.270  1.00 15.83 ?  137  ILE   B O    1 
ATOM   5924 C  CB   . ILE   B 1 137 ? 35.112 -36.855 -2.882  1.00 18.87 ?  137  ILE   B CB   1 
ATOM   5925 C  CG1  . ILE   B 1 137 ? 36.116 -37.761 -3.600  1.00 21.37 ?  137  ILE   B CG1  1 
ATOM   5926 C  CG2  . ILE   B 1 137 ? 33.715 -37.001 -3.477  1.00 19.60 ?  137  ILE   B CG2  1 
ATOM   5927 C  CD1  . ILE   B 1 137 ? 35.823 -39.240 -3.457  1.00 23.75 ?  137  ILE   B CD1  1 
ATOM   5928 H  H    . ILE   B 1 137 ? 37.034 -35.921 -1.722  1.00 19.27 ?  137  ILE   B H    1 
ATOM   5929 H  HA   . ILE   B 1 137 ? 35.774 -35.181 -3.878  1.00 20.26 ?  137  ILE   B HA   1 
ATOM   5930 H  HB   . ILE   B 1 137 ? 35.069 -37.121 -1.956  1.00 22.64 ?  137  ILE   B HB   1 
ATOM   5931 H  HG12 . ILE   B 1 137 ? 36.109 -37.553 -4.547  1.00 25.64 ?  137  ILE   B HG12 1 
ATOM   5932 H  HG13 . ILE   B 1 137 ? 36.997 -37.601 -3.232  1.00 25.64 ?  137  ILE   B HG13 1 
ATOM   5933 H  HG21 . ILE   B 1 137 ? 33.500 -37.942 -3.575  1.00 23.51 ?  137  ILE   B HG21 1 
ATOM   5934 H  HG22 . ILE   B 1 137 ? 33.069 -36.586 -2.884  1.00 23.51 ?  137  ILE   B HG22 1 
ATOM   5935 H  HG23 . ILE   B 1 137 ? 33.692 -36.569 -4.346  1.00 23.51 ?  137  ILE   B HG23 1 
ATOM   5936 H  HD11 . ILE   B 1 137 ? 36.567 -39.737 -3.825  1.00 28.49 ?  137  ILE   B HD11 1 
ATOM   5937 H  HD12 . ILE   B 1 137 ? 35.714 -39.454 -2.516  1.00 28.49 ?  137  ILE   B HD12 1 
ATOM   5938 H  HD13 . ILE   B 1 137 ? 35.011 -39.458 -3.942  1.00 28.49 ?  137  ILE   B HD13 1 
ATOM   5939 N  N    . HIS   B 1 138 ? 34.374 -34.275 -1.153  1.00 16.48 ?  138  HIS   B N    1 
ATOM   5940 C  CA   . HIS   B 1 138 ? 33.427 -33.311 -0.611  1.00 16.77 ?  138  HIS   B CA   1 
ATOM   5941 C  C    . HIS   B 1 138 ? 33.845 -31.885 -0.930  1.00 15.80 ?  138  HIS   B C    1 
ATOM   5942 O  O    . HIS   B 1 138 ? 32.997 -31.040 -1.235  1.00 16.00 ?  138  HIS   B O    1 
ATOM   5943 C  CB   . HIS   B 1 138 ? 33.312 -33.490 0.894   1.00 18.03 ?  138  HIS   B CB   1 
ATOM   5944 C  CG   . HIS   B 1 138 ? 32.377 -32.515 1.528   1.00 19.06 ?  138  HIS   B CG   1 
ATOM   5945 N  ND1  . HIS   B 1 138 ? 31.038 -32.459 1.207   1.00 20.51 ?  138  HIS   B ND1  1 
ATOM   5946 C  CD2  . HIS   B 1 138 ? 32.589 -31.535 2.436   1.00 19.37 ?  138  HIS   B CD2  1 
ATOM   5947 C  CE1  . HIS   B 1 138 ? 30.461 -31.497 1.904   1.00 20.36 ?  138  HIS   B CE1  1 
ATOM   5948 N  NE2  . HIS   B 1 138 ? 31.381 -30.920 2.658   1.00 19.78 ?  138  HIS   B NE2  1 
ATOM   5949 H  H    . HIS   B 1 138 ? 34.818 -34.718 -0.568  1.00 19.77 ?  138  HIS   B H    1 
ATOM   5950 H  HA   . HIS   B 1 138 ? 32.553 -33.473 -1.005  1.00 20.11 ?  138  HIS   B HA   1 
ATOM   5951 H  HB2  . HIS   B 1 138 ? 32.984 -34.384 1.081   1.00 21.63 ?  138  HIS   B HB2  1 
ATOM   5952 H  HB3  . HIS   B 1 138 ? 34.188 -33.369 1.291   1.00 21.63 ?  138  HIS   B HB3  1 
ATOM   5953 H  HD1  . HIS   B 1 138 ? 30.642 -32.978 0.642   1.00 24.61 ?  138  HIS   B HD1  1 
ATOM   5954 H  HD2  . HIS   B 1 138 ? 33.392 -31.323 2.846   1.00 23.24 ?  138  HIS   B HD2  1 
ATOM   5955 H  HE1  . HIS   B 1 138 ? 29.556 -31.273 1.868   1.00 24.43 ?  138  HIS   B HE1  1 
ATOM   5956 N  N    . SER   B 1 139 ? 35.141 -31.588 -0.852  1.00 15.11 ?  139  SER   B N    1 
ATOM   5957 C  CA   . SER   B 1 139 ? 35.579 -30.238 -1.168  1.00 14.42 ?  139  SER   B CA   1 
ATOM   5958 C  C    . SER   B 1 139 ? 35.237 -29.880 -2.605  1.00 13.60 ?  139  SER   B C    1 
ATOM   5959 O  O    . SER   B 1 139 ? 34.790 -28.761 -2.881  1.00 13.71 ?  139  SER   B O    1 
ATOM   5960 C  CB   . SER   B 1 139 ? 37.074 -30.104 -0.909  1.00 14.62 ?  139  SER   B CB   1 
ATOM   5961 O  OG   . SER   B 1 139 ? 37.487 -28.771 -1.163  1.00 15.01 ?  139  SER   B OG   1 
ATOM   5962 H  H    . SER   B 1 139 ? 35.759 -32.135 -0.629  1.00 18.13 ?  139  SER   B H    1 
ATOM   5963 H  HA   . SER   B 1 139 ? 35.114 -29.615 -0.595  1.00 17.30 ?  139  SER   B HA   1 
ATOM   5964 H  HB2  . SER   B 1 139 ? 37.257 -30.330 0.017   1.00 17.54 ?  139  SER   B HB2  1 
ATOM   5965 H  HB3  . SER   B 1 139 ? 37.559 -30.701 -1.501  1.00 17.54 ?  139  SER   B HB3  1 
ATOM   5966 H  HG   . SER   B 1 139 ? 38.312 -28.690 -1.008  1.00 18.00 ?  139  SER   B HG   1 
ATOM   5967 N  N    . LEU   B 1 140 ? 35.429 -30.821 -3.536  1.00 13.56 ?  140  LEU   B N    1 
ATOM   5968 C  CA   . LEU   B 1 140 ? 35.061 -30.567 -4.923  1.00 13.85 ?  140  LEU   B CA   1 
ATOM   5969 C  C    . LEU   B 1 140 ? 33.559 -30.347 -5.053  1.00 14.07 ?  140  LEU   B C    1 
ATOM   5970 O  O    . LEU   B 1 140 ? 33.116 -29.462 -5.789  1.00 14.27 ?  140  LEU   B O    1 
ATOM   5971 C  CB   . LEU   B 1 140 ? 35.526 -31.727 -5.805  1.00 13.83 ?  140  LEU   B CB   1 
ATOM   5972 C  CG   . LEU   B 1 140 ? 35.167 -31.621 -7.280  1.00 14.30 ?  140  LEU   B CG   1 
ATOM   5973 C  CD1  . LEU   B 1 140 ? 35.744 -30.347 -7.885  1.00 15.20 ?  140  LEU   B CD1  1 
ATOM   5974 C  CD2  . LEU   B 1 140 ? 35.649 -32.856 -8.015  1.00 15.10 ?  140  LEU   B CD2  1 
ATOM   5975 H  H    . LEU   B 1 140 ? 35.761 -31.598 -3.396  1.00 16.27 ?  140  LEU   B H    1 
ATOM   5976 H  HA   . LEU   B 1 140 ? 35.510 -29.760 -5.230  1.00 16.62 ?  140  LEU   B HA   1 
ATOM   5977 H  HB2  . LEU   B 1 140 ? 36.495 -31.785 -5.752  1.00 16.59 ?  140  LEU   B HB2  1 
ATOM   5978 H  HB3  . LEU   B 1 140 ? 35.133 -32.544 -5.474  1.00 16.59 ?  140  LEU   B HB3  1 
ATOM   5979 H  HG   . LEU   B 1 140 ? 34.202 -31.573 -7.367  1.00 17.15 ?  140  LEU   B HG   1 
ATOM   5980 H  HD11 . LEU   B 1 140 ? 35.616 -30.366 -8.845  1.00 18.23 ?  140  LEU   B HD11 1 
ATOM   5981 H  HD12 . LEU   B 1 140 ? 35.283 -29.576 -7.509  1.00 18.23 ?  140  LEU   B HD12 1 
ATOM   5982 H  HD13 . LEU   B 1 140 ? 36.690 -30.297 -7.677  1.00 18.23 ?  140  LEU   B HD13 1 
ATOM   5983 H  HD21 . LEU   B 1 140 ? 35.409 -32.771 -8.951  1.00 18.12 ?  140  LEU   B HD21 1 
ATOM   5984 H  HD22 . LEU   B 1 140 ? 36.607 -32.922 -7.917  1.00 18.12 ?  140  LEU   B HD22 1 
ATOM   5985 H  HD23 . LEU   B 1 140 ? 35.214 -33.630 -7.628  1.00 18.12 ?  140  LEU   B HD23 1 
ATOM   5986 N  N    . ARG   B 1 141 ? 32.762 -31.146 -4.338  1.00 14.18 ?  141  ARG   B N    1 
ATOM   5987 C  CA   . ARG   B 1 141 ? 31.311 -30.971 -4.310  1.00 15.19 ?  141  ARG   B CA   1 
ATOM   5988 C  C    . ARG   B 1 141 ? 30.930 -29.563 -3.878  1.00 15.01 ?  141  ARG   B C    1 
ATOM   5989 O  O    . ARG   B 1 141 ? 30.132 -28.885 -4.541  1.00 15.13 ?  141  ARG   B O    1 
ATOM   5990 C  CB   . ARG   B 1 141 ? 30.731 -31.999 -3.329  1.00 16.61 ?  141  ARG   B CB   1 
ATOM   5991 C  CG   . ARG   B 1 141 ? 29.258 -31.894 -3.007  1.00 18.96 ?  141  ARG   B CG   1 
ATOM   5992 C  CD   . ARG   B 1 141 ? 28.467 -32.525 -4.083  1.00 20.92 ?  141  ARG   B CD   1 
ATOM   5993 N  NE   . ARG   B 1 141 ? 28.196 -31.606 -5.178  1.00 21.24 ?  141  ARG   B NE   1 
ATOM   5994 C  CZ   . ARG   B 1 141 ? 28.183 -31.948 -6.459  1.00 20.64 ?  141  ARG   B CZ   1 
ATOM   5995 N  NH1  . ARG   B 1 141 ? 28.618 -33.130 -6.865  1.00 20.82 ?  141  ARG   B NH1  1 
ATOM   5996 N  NH2  . ARG   B 1 141 ? 27.708 -31.084 -7.353  1.00 21.52 ?  141  ARG   B NH2  1 
ATOM   5997 H  H    . ARG   B 1 141 ? 33.045 -31.799 -3.856  1.00 17.01 ?  141  ARG   B H    1 
ATOM   5998 H  HA   . ARG   B 1 141 ? 30.943 -31.139 -5.189  1.00 18.22 ?  141  ARG   B HA   1 
ATOM   5999 H  HB2  . ARG   B 1 141 ? 30.893 -32.889 -3.692  1.00 19.93 ?  141  ARG   B HB2  1 
ATOM   6000 H  HB3  . ARG   B 1 141 ? 31.211 -31.920 -2.490  1.00 19.93 ?  141  ARG   B HB3  1 
ATOM   6001 H  HG2  . ARG   B 1 141 ? 29.080 -32.357 -2.174  1.00 22.75 ?  141  ARG   B HG2  1 
ATOM   6002 H  HG3  . ARG   B 1 141 ? 29.000 -30.961 -2.934  1.00 22.75 ?  141  ARG   B HG3  1 
ATOM   6003 H  HD2  . ARG   B 1 141 ? 28.956 -33.292 -4.429  1.00 25.10 ?  141  ARG   B HD2  1 
ATOM   6004 H  HD3  . ARG   B 1 141 ? 27.624 -32.820 -3.716  1.00 25.10 ?  141  ARG   B HD3  1 
ATOM   6005 H  HE   . ARG   B 1 141 ? 28.028 -30.786 -4.978  1.00 25.48 ?  141  ARG   B HE   1 
ATOM   6006 H  HH11 . ARG   B 1 141 ? 28.917 -33.704 -6.300  1.00 24.98 ?  141  ARG   B HH11 1 
ATOM   6007 H  HH12 . ARG   B 1 141 ? 28.608 -33.323 -7.701  1.00 24.98 ?  141  ARG   B HH12 1 
ATOM   6008 H  HH21 . ARG   B 1 141 ? 27.429 -30.308 -7.099  1.00 25.82 ?  141  ARG   B HH21 1 
ATOM   6009 H  HH22 . ARG   B 1 141 ? 27.713 -31.282 -8.190  1.00 25.82 ?  141  ARG   B HH22 1 
ATOM   6010 N  N    . VAL   B 1 142 ? 31.479 -29.115 -2.751  1.00 14.57 ?  142  VAL   B N    1 
ATOM   6011 C  CA   . VAL   B 1 142 ? 31.145 -27.785 -2.263  1.00 14.47 ?  142  VAL   B CA   1 
ATOM   6012 C  C    . VAL   B 1 142 ? 31.620 -26.725 -3.250  1.00 14.25 ?  142  VAL   B C    1 
ATOM   6013 O  O    . VAL   B 1 142 ? 30.919 -25.744 -3.512  1.00 14.90 ?  142  VAL   B O    1 
ATOM   6014 C  CB   . VAL   B 1 142 ? 31.695 -27.559 -0.842  1.00 15.05 ?  142  VAL   B CB   1 
ATOM   6015 C  CG1  . VAL   B 1 142 ? 31.382 -26.138 -0.371  1.00 15.15 ?  142  VAL   B CG1  1 
ATOM   6016 C  CG2  . VAL   B 1 142 ? 31.129 -28.583 0.122   1.00 15.89 ?  142  VAL   B CG2  1 
ATOM   6017 H  H    . VAL   B 1 142 ? 32.042 -29.548 -2.265  1.00 17.47 ?  142  VAL   B H    1 
ATOM   6018 H  HA   . VAL   B 1 142 ? 30.186 -27.712 -2.208  1.00 17.36 ?  142  VAL   B HA   1 
ATOM   6019 H  HB   . VAL   B 1 142 ? 32.662 -27.661 -0.853  1.00 18.05 ?  142  VAL   B HB   1 
ATOM   6020 H  HG11 . VAL   B 1 142 ? 31.559 -26.073 0.580   1.00 18.17 ?  142  VAL   B HG11 1 
ATOM   6021 H  HG12 . VAL   B 1 142 ? 31.950 -25.509 -0.851  1.00 18.17 ?  142  VAL   B HG12 1 
ATOM   6022 H  HG13 . VAL   B 1 142 ? 30.451 -25.943 -0.550  1.00 18.17 ?  142  VAL   B HG13 1 
ATOM   6023 H  HG21 . VAL   B 1 142 ? 31.460 -28.393 1.013   1.00 19.07 ?  142  VAL   B HG21 1 
ATOM   6024 H  HG22 . VAL   B 1 142 ? 30.161 -28.521 0.108   1.00 19.07 ?  142  VAL   B HG22 1 
ATOM   6025 H  HG23 . VAL   B 1 142 ? 31.410 -29.466 -0.157  1.00 19.07 ?  142  VAL   B HG23 1 
ATOM   6026 N  N    . CYS   B 1 143 ? 32.804 -26.919 -3.832  1.00 13.39 ?  143  CYS   B N    1 
ATOM   6027 C  CA   . CYS   B 1 143 ? 33.296 -25.981 -4.837  1.00 13.32 ?  143  CYS   B CA   1 
ATOM   6028 C  C    . CYS   B 1 143 ? 32.292 -25.832 -5.974  1.00 13.29 ?  143  CYS   B C    1 
ATOM   6029 O  O    . CYS   B 1 143 ? 31.885 -24.721 -6.331  1.00 13.33 ?  143  CYS   B O    1 
ATOM   6030 C  CB   . CYS   B 1 143 ? 34.647 -26.469 -5.367  1.00 13.86 ?  143  CYS   B CB   1 
ATOM   6031 S  SG   . CYS   B 1 143 ? 35.393 -25.359 -6.589  1.00 14.13 ?  143  CYS   B SG   1 
ATOM   6032 H  H    . CYS   B 1 143 ? 33.336 -27.575 -3.663  1.00 16.06 ?  143  CYS   B H    1 
ATOM   6033 H  HA   . CYS   B 1 143 ? 33.424 -25.112 -4.430  1.00 15.98 ?  143  CYS   B HA   1 
ATOM   6034 H  HB2  . CYS   B 1 143 ? 35.268 -26.552 -4.626  1.00 16.63 ?  143  CYS   B HB2  1 
ATOM   6035 H  HB3  . CYS   B 1 143 ? 34.525 -27.332 -5.786  1.00 16.63 ?  143  CYS   B HB3  1 
ATOM   6036 H  HG   . CYS   B 1 143 ? 36.468 -25.789 -6.920  1.00 16.95 ?  143  CYS   B HG   1 
ATOM   6037 N  N    . VAL   B 1 144 ? 31.884 -26.953 -6.564  1.00 14.09 ?  144  VAL   B N    1 
ATOM   6038 C  CA   . VAL   B 1 144 ? 30.984 -26.890 -7.710  1.00 15.32 ?  144  VAL   B CA   1 
ATOM   6039 C  C    . VAL   B 1 144 ? 29.642 -26.281 -7.338  1.00 15.17 ?  144  VAL   B C    1 
ATOM   6040 O  O    . VAL   B 1 144 ? 29.026 -25.576 -8.146  1.00 16.34 ?  144  VAL   B O    1 
ATOM   6041 C  CB   . VAL   B 1 144 ? 30.829 -28.297 -8.299  1.00 18.09 ?  144  VAL   B CB   1 
ATOM   6042 C  CG1  . VAL   B 1 144 ? 29.545 -28.428 -9.124  1.00 20.69 ?  144  VAL   B CG1  1 
ATOM   6043 C  CG2  . VAL   B 1 144 ? 32.073 -28.677 -9.098  1.00 18.02 ?  144  VAL   B CG2  1 
ATOM   6044 H  H    . VAL   B 1 144 ? 32.110 -27.752 -6.324  1.00 16.90 ?  144  VAL   B H    1 
ATOM   6045 H  HA   . VAL   B 1 144 ? 31.381 -26.331 -8.389  1.00 18.38 ?  144  VAL   B HA   1 
ATOM   6046 H  HB   . VAL   B 1 144 ? 30.762 -28.934 -7.568  1.00 21.70 ?  144  VAL   B HB   1 
ATOM   6047 H  HG11 . VAL   B 1 144 ? 29.619 -29.212 -9.695  1.00 24.83 ?  144  VAL   B HG11 1 
ATOM   6048 H  HG12 . VAL   B 1 144 ? 28.793 -28.533 -8.522  1.00 24.83 ?  144  VAL   B HG12 1 
ATOM   6049 H  HG13 . VAL   B 1 144 ? 29.437 -27.636 -9.668  1.00 24.83 ?  144  VAL   B HG13 1 
ATOM   6050 H  HG21 . VAL   B 1 144 ? 31.957 -29.570 -9.457  1.00 21.62 ?  144  VAL   B HG21 1 
ATOM   6051 H  HG22 . VAL   B 1 144 ? 32.182 -28.041 -9.824  1.00 21.62 ?  144  VAL   B HG22 1 
ATOM   6052 H  HG23 . VAL   B 1 144 ? 32.842 -28.649 -8.512  1.00 21.62 ?  144  VAL   B HG23 1 
ATOM   6053 N  N    . ASP   B 1 145 ? 29.175 -26.525 -6.120  1.00 15.30 ?  145  ASP   B N    1 
ATOM   6054 C  CA   . ASP   B 1 145 ? 27.867 -26.054 -5.696  1.00 15.88 ?  145  ASP   B CA   1 
ATOM   6055 C  C    . ASP   B 1 145 ? 27.898 -24.635 -5.148  1.00 15.56 ?  145  ASP   B C    1 
ATOM   6056 O  O    . ASP   B 1 145 ? 26.838 -24.097 -4.812  1.00 17.55 ?  145  ASP   B O    1 
ATOM   6057 C  CB   . ASP   B 1 145 ? 27.283 -26.973 -4.615  1.00 17.81 ?  145  ASP   B CB   1 
ATOM   6058 C  CG   . ASP   B 1 145 ? 26.923 -28.349 -5.125  1.00 19.45 ?  145  ASP   B CG   1 
ATOM   6059 O  OD1  . ASP   B 1 145 ? 26.812 -28.534 -6.354  1.00 19.92 ?  145  ASP   B OD1  1 
ATOM   6060 O  OD2  . ASP   B 1 145 ? 26.744 -29.242 -4.271  1.00 21.36 -1 145  ASP   B OD2  1 
ATOM   6061 H  H    . ASP   B 1 145 ? 29.611 -26.949 -5.511  1.00 18.35 ?  145  ASP   B H    1 
ATOM   6062 H  HA   . ASP   B 1 145 ? 27.274 -26.044 -6.460  1.00 19.05 ?  145  ASP   B HA   1 
ATOM   6063 H  HB2  . ASP   B 1 145 ? 27.932 -27.085 -3.917  1.00 21.37 ?  145  ASP   B HB2  1 
ATOM   6064 H  HB3  . ASP   B 1 145 ? 26.474 -26.562 -4.271  1.00 21.37 ?  145  ASP   B HB3  1 
ATOM   6065 N  N    . THR   B 1 146 ? 29.075 -24.025 -5.032  1.00 13.99 ?  146  THR   B N    1 
ATOM   6066 C  CA   . THR   B 1 146 ? 29.209 -22.705 -4.422  1.00 13.82 ?  146  THR   B CA   1 
ATOM   6067 C  C    . THR   B 1 146 ? 29.843 -21.679 -5.341  1.00 13.56 ?  146  THR   B C    1 
ATOM   6068 O  O    . THR   B 1 146 ? 29.394 -20.522 -5.386  1.00 14.01 ?  146  THR   B O    1 
ATOM   6069 C  CB   . THR   B 1 146 ? 30.042 -22.813 -3.137  1.00 13.92 ?  146  THR   B CB   1 
ATOM   6070 O  OG1  . THR   B 1 146 ? 29.471 -23.812 -2.281  1.00 14.19 ?  146  THR   B OG1  1 
ATOM   6071 C  CG2  . THR   B 1 146 ? 30.113 -21.479 -2.412  1.00 14.21 ?  146  THR   B CG2  1 
ATOM   6072 H  H    . THR   B 1 146 ? 29.830 -24.356 -5.300  1.00 16.78 ?  146  THR   B H    1 
ATOM   6073 H  HA   . THR   B 1 146 ? 28.338 -22.382 -4.175  1.00 16.57 ?  146  THR   B HA   1 
ATOM   6074 H  HB   . THR   B 1 146 ? 30.953 -23.068 -3.364  1.00 16.70 ?  146  THR   B HB   1 
ATOM   6075 H  HG1  . THR   B 1 146 ? 29.518 -24.570 -2.661  1.00 17.03 ?  146  THR   B HG1  1 
ATOM   6076 H  HG21 . THR   B 1 146 ? 30.467 -21.604 -1.518  1.00 17.05 ?  146  THR   B HG21 1 
ATOM   6077 H  HG22 . THR   B 1 146 ? 30.694 -20.867 -2.895  1.00 17.05 ?  146  THR   B HG22 1 
ATOM   6078 H  HG23 . THR   B 1 146 ? 29.228 -21.090 -2.349  1.00 17.05 ?  146  THR   B HG23 1 
ATOM   6079 N  N    . VAL   B 1 147 ? 30.907 -22.052 -6.037  1.00 13.28 ?  147  VAL   B N    1 
ATOM   6080 C  CA   . VAL   B 1 147 ? 31.627 -21.105 -6.871  1.00 12.98 ?  147  VAL   B CA   1 
ATOM   6081 C  C    . VAL   B 1 147 ? 30.894 -20.968 -8.192  1.00 13.34 ?  147  VAL   B C    1 
ATOM   6082 O  O    . VAL   B 1 147 ? 30.524 -21.968 -8.820  1.00 14.06 ?  147  VAL   B O    1 
ATOM   6083 C  CB   . VAL   B 1 147 ? 33.079 -21.557 -7.079  1.00 13.11 ?  147  VAL   B CB   1 
ATOM   6084 C  CG1  . VAL   B 1 147 ? 33.830 -20.527 -7.903  1.00 13.19 ?  147  VAL   B CG1  1 
ATOM   6085 C  CG2  . VAL   B 1 147 ? 33.761 -21.766 -5.738  1.00 13.33 ?  147  VAL   B CG2  1 
ATOM   6086 H  H    . VAL   B 1 147 ? 31.238 -22.850 -6.045  1.00 15.94 ?  147  VAL   B H    1 
ATOM   6087 H  HA   . VAL   B 1 147 ? 31.641 -20.241 -6.438  1.00 15.57 ?  147  VAL   B HA   1 
ATOM   6088 H  HB   . VAL   B 1 147 ? 33.094 -22.401 -7.562  1.00 15.73 ?  147  VAL   B HB   1 
ATOM   6089 H  HG11 . VAL   B 1 147 ? 34.778 -20.737 -7.889  1.00 15.82 ?  147  VAL   B HG11 1 
ATOM   6090 H  HG12 . VAL   B 1 147 ? 33.504 -20.547 -8.817  1.00 15.82 ?  147  VAL   B HG12 1 
ATOM   6091 H  HG13 . VAL   B 1 147 ? 33.684 -19.647 -7.518  1.00 15.82 ?  147  VAL   B HG13 1 
ATOM   6092 H  HG21 . VAL   B 1 147 ? 34.702 -21.949 -5.885  1.00 15.99 ?  147  VAL   B HG21 1 
ATOM   6093 H  HG22 . VAL   B 1 147 ? 33.660 -20.961 -5.207  1.00 15.99 ?  147  VAL   B HG22 1 
ATOM   6094 H  HG23 . VAL   B 1 147 ? 33.345 -22.516 -5.285  1.00 15.99 ?  147  VAL   B HG23 1 
ATOM   6095 N  N    . ARG   B 1 148 ? 30.681 -19.719 -8.606  1.00 13.38 ?  148  ARG   B N    1 
ATOM   6096 C  CA   . ARG   B 1 148 ? 30.054 -19.396 -9.876  1.00 13.70 ?  148  ARG   B CA   1 
ATOM   6097 C  C    . ARG   B 1 148 ? 31.008 -18.719 -10.848 1.00 13.85 ?  148  ARG   B C    1 
ATOM   6098 O  O    . ARG   B 1 148 ? 30.723 -18.693 -12.048 1.00 15.08 ?  148  ARG   B O    1 
ATOM   6099 C  CB   . ARG   B 1 148 ? 28.822 -18.505 -9.651  1.00 14.25 ?  148  ARG   B CB   1 
ATOM   6100 C  CG   . ARG   B 1 148 ? 27.750 -19.215 -8.847  1.00 14.89 ?  148  ARG   B CG   1 
ATOM   6101 C  CD   . ARG   B 1 148 ? 26.548 -18.334 -8.547  1.00 15.74 ?  148  ARG   B CD   1 
ATOM   6102 N  NE   . ARG   B 1 148 ? 26.924 -17.134 -7.810  1.00 15.44 ?  148  ARG   B NE   1 
ATOM   6103 C  CZ   . ARG   B 1 148 ? 27.221 -17.102 -6.516  1.00 14.53 ?  148  ARG   B CZ   1 
ATOM   6104 N  NH1  . ARG   B 1 148 ? 27.159 -18.188 -5.760  1.00 14.62 ?  148  ARG   B NH1  1 
ATOM   6105 N  NH2  . ARG   B 1 148 ? 27.613 -15.955 -5.968  1.00 14.52 ?  148  ARG   B NH2  1 
ATOM   6106 H  H    . ARG   B 1 148 ? 30.904 -19.019 -8.146  1.00 16.04 ?  148  ARG   B H    1 
ATOM   6107 H  HA   . ARG   B 1 148 ? 29.753 -20.216 -10.288 1.00 16.43 ?  148  ARG   B HA   1 
ATOM   6108 H  HB2  . ARG   B 1 148 ? 29.088 -17.709 -9.162  1.00 17.10 ?  148  ARG   B HB2  1 
ATOM   6109 H  HB3  . ARG   B 1 148 ? 28.445 -18.260 -10.509 1.00 17.10 ?  148  ARG   B HB3  1 
ATOM   6110 H  HG2  . ARG   B 1 148 ? 27.436 -19.983 -9.352  1.00 17.86 ?  148  ARG   B HG2  1 
ATOM   6111 H  HG3  . ARG   B 1 148 ? 28.126 -19.505 -8.003  1.00 17.86 ?  148  ARG   B HG3  1 
ATOM   6112 H  HD2  . ARG   B 1 148 ? 26.140 -18.056 -9.381  1.00 18.89 ?  148  ARG   B HD2  1 
ATOM   6113 H  HD3  . ARG   B 1 148 ? 25.912 -18.832 -8.011  1.00 18.89 ?  148  ARG   B HD3  1 
ATOM   6114 H  HE   . ARG   B 1 148 ? 26.965 -16.394 -8.241  1.00 18.52 ?  148  ARG   B HE   1 
ATOM   6115 H  HH11 . ARG   B 1 148 ? 26.904 -18.939 -6.096  1.00 17.54 ?  148  ARG   B HH11 1 
ATOM   6116 H  HH12 . ARG   B 1 148 ? 27.348 -18.143 -4.919  1.00 17.54 ?  148  ARG   B HH12 1 
ATOM   6117 H  HH21 . ARG   B 1 148 ? 27.661 -15.244 -6.447  1.00 17.41 ?  148  ARG   B HH21 1 
ATOM   6118 H  HH22 . ARG   B 1 148 ? 27.804 -15.920 -5.129  1.00 17.41 ?  148  ARG   B HH22 1 
ATOM   6119 N  N    . THR   B 1 149 ? 32.116 -18.170 -10.360 1.00 13.67 ?  149  THR   B N    1 
ATOM   6120 C  CA   . THR   B 1 149 ? 33.153 -17.611 -11.212 1.00 13.56 ?  149  THR   B CA   1 
ATOM   6121 C  C    . THR   B 1 149 ? 34.042 -18.747 -11.721 1.00 13.29 ?  149  THR   B C    1 
ATOM   6122 O  O    . THR   B 1 149 ? 33.849 -19.917 -11.381 1.00 13.73 ?  149  THR   B O    1 
ATOM   6123 C  CB   . THR   B 1 149 ? 33.926 -16.561 -10.426 1.00 13.49 ?  149  THR   B CB   1 
ATOM   6124 O  OG1  . THR   B 1 149 ? 34.383 -17.163 -9.210  1.00 13.52 ?  149  THR   B OG1  1 
ATOM   6125 C  CG2  . THR   B 1 149 ? 33.036 -15.351 -10.131 1.00 13.97 ?  149  THR   B CG2  1 
ATOM   6126 H  H    . THR   B 1 149 ? 32.284 -18.095 -9.520  1.00 16.40 ?  149  THR   B H    1 
ATOM   6127 H  HA   . THR   B 1 149 ? 32.741 -17.173 -11.977 1.00 16.27 ?  149  THR   B HA   1 
ATOM   6128 H  HB   . THR   B 1 149 ? 34.689 -16.267 -10.942 1.00 16.18 ?  149  THR   B HB   1 
ATOM   6129 H  HG1  . THR   B 1 149 ? 34.796 -16.589 -8.747  1.00 16.22 ?  149  THR   B HG1  1 
ATOM   6130 H  HG21 . THR   B 1 149 ? 33.542 -14.678 -9.647  1.00 16.76 ?  149  THR   B HG21 1 
ATOM   6131 H  HG22 . THR   B 1 149 ? 32.718 -14.962 -10.964 1.00 16.76 ?  149  THR   B HG22 1 
ATOM   6132 H  HG23 . THR   B 1 149 ? 32.273 -15.617 -9.598  1.00 16.76 ?  149  THR   B HG23 1 
ATOM   6133 N  N    . ASN   B 1 150 ? 35.011 -18.426 -12.570 1.00 13.30 ?  150  ASN   B N    1 
ATOM   6134 C  CA   . ASN   B 1 150 ? 35.771 -19.451 -13.275 1.00 13.67 ?  150  ASN   B CA   1 
ATOM   6135 C  C    . ASN   B 1 150 ? 36.938 -19.901 -12.410 1.00 13.09 ?  150  ASN   B C    1 
ATOM   6136 O  O    . ASN   B 1 150 ? 37.872 -19.133 -12.163 1.00 13.98 ?  150  ASN   B O    1 
ATOM   6137 C  CB   . ASN   B 1 150 ? 36.245 -18.916 -14.618 1.00 15.63 ?  150  ASN   B CB   1 
ATOM   6138 C  CG   . ASN   B 1 150 ? 35.102 -18.690 -15.563 1.00 18.46 ?  150  ASN   B CG   1 
ATOM   6139 O  OD1  . ASN   B 1 150 ? 34.231 -19.542 -15.692 1.00 19.89 ?  150  ASN   B OD1  1 
ATOM   6140 N  ND2  . ASN   B 1 150 ? 35.074 -17.532 -16.201 1.00 20.07 ?  150  ASN   B ND2  1 
ATOM   6141 H  H    . ASN   B 1 150 ? 35.255 -17.617 -12.749 1.00 15.95 ?  150  ASN   B H    1 
ATOM   6142 H  HA   . ASN   B 1 150 ? 35.191 -20.215 -13.438 1.00 16.40 ?  150  ASN   B HA   1 
ATOM   6143 H  HB2  . ASN   B 1 150 ? 36.696 -18.067 -14.478 1.00 18.75 ?  150  ASN   B HB2  1 
ATOM   6144 H  HB3  . ASN   B 1 150 ? 36.851 -19.556 -15.017 1.00 18.75 ?  150  ASN   B HB3  1 
ATOM   6145 H  HD21 . ASN   B 1 150 ? 34.437 -17.355 -16.756 1.00 24.07 ?  150  ASN   B HD21 1 
ATOM   6146 H  HD22 . ASN   B 1 150 ? 35.696 -16.949 -16.071 1.00 24.07 ?  150  ASN   B HD22 1 
ATOM   6147 N  N    . VAL   B 1 151 ? 36.891 -21.146 -11.949 1.00 12.86 ?  151  VAL   B N    1 
ATOM   6148 C  CA   . VAL   B 1 151 ? 37.910 -21.676 -11.059 1.00 13.22 ?  151  VAL   B CA   1 
ATOM   6149 C  C    . VAL   B 1 151 ? 38.619 -22.839 -11.738 1.00 12.94 ?  151  VAL   B C    1 
ATOM   6150 O  O    . VAL   B 1 151 ? 37.980 -23.776 -12.241 1.00 13.91 ?  151  VAL   B O    1 
ATOM   6151 C  CB   . VAL   B 1 151 ? 37.350 -22.018 -9.662  1.00 14.57 ?  151  VAL   B CB   1 
ATOM   6152 C  CG1  . VAL   B 1 151 ? 36.197 -23.021 -9.743  1.00 15.35 ?  151  VAL   B CG1  1 
ATOM   6153 C  CG2  . VAL   B 1 151 ? 38.461 -22.511 -8.749  1.00 15.26 ?  151  VAL   B CG2  1 
ATOM   6154 H  H    . VAL   B 1 151 ? 36.270 -21.711 -12.147 1.00 15.43 ?  151  VAL   B H    1 
ATOM   6155 H  HA   . VAL   B 1 151 ? 38.577 -20.979 -10.926 1.00 15.85 ?  151  VAL   B HA   1 
ATOM   6156 H  HB   . VAL   B 1 151 ? 36.997 -21.199 -9.268  1.00 17.48 ?  151  VAL   B HB   1 
ATOM   6157 H  HG11 . VAL   B 1 151 ? 35.876 -23.210 -8.846  1.00 18.41 ?  151  VAL   B HG11 1 
ATOM   6158 H  HG12 . VAL   B 1 151 ? 35.479 -22.642 -10.276 1.00 18.41 ?  151  VAL   B HG12 1 
ATOM   6159 H  HG13 . VAL   B 1 151 ? 36.516 -23.839 -10.156 1.00 18.41 ?  151  VAL   B HG13 1 
ATOM   6160 H  HG21 . VAL   B 1 151 ? 38.113 -22.588 -7.845  1.00 18.30 ?  151  VAL   B HG21 1 
ATOM   6161 H  HG22 . VAL   B 1 151 ? 38.765 -23.377 -9.059  1.00 18.30 ?  151  VAL   B HG22 1 
ATOM   6162 H  HG23 . VAL   B 1 151 ? 39.193 -21.874 -8.765  1.00 18.30 ?  151  VAL   B HG23 1 
ATOM   6163 N  N    . TYR   B 1 152 ? 39.947 -22.753 -11.754 1.00 12.42 ?  152  TYR   B N    1 
ATOM   6164 C  CA   . TYR   B 1 152 ? 40.849 -23.736 -12.334 1.00 12.55 ?  152  TYR   B CA   1 
ATOM   6165 C  C    . TYR   B 1 152 ? 41.566 -24.416 -11.174 1.00 12.13 ?  152  TYR   B C    1 
ATOM   6166 O  O    . TYR   B 1 152 ? 42.415 -23.803 -10.519 1.00 12.75 ?  152  TYR   B O    1 
ATOM   6167 C  CB   . TYR   B 1 152 ? 41.824 -23.028 -13.276 1.00 13.50 ?  152  TYR   B CB   1 
ATOM   6168 C  CG   . TYR   B 1 152 ? 41.145 -22.565 -14.543 1.00 13.85 ?  152  TYR   B CG   1 
ATOM   6169 C  CD1  . TYR   B 1 152 ? 40.487 -21.341 -14.610 1.00 14.30 ?  152  TYR   B CD1  1 
ATOM   6170 C  CD2  . TYR   B 1 152 ? 41.144 -23.369 -15.669 1.00 15.31 ?  152  TYR   B CD2  1 
ATOM   6171 C  CE1  . TYR   B 1 152 ? 39.851 -20.936 -15.770 1.00 15.55 ?  152  TYR   B CE1  1 
ATOM   6172 C  CE2  . TYR   B 1 152 ? 40.515 -22.977 -16.828 1.00 16.09 ?  152  TYR   B CE2  1 
ATOM   6173 C  CZ   . TYR   B 1 152 ? 39.871 -21.758 -16.878 1.00 16.11 ?  152  TYR   B CZ   1 
ATOM   6174 O  OH   . TYR   B 1 152 ? 39.245 -21.377 -18.042 1.00 18.60 ?  152  TYR   B OH   1 
ATOM   6175 H  H    . TYR   B 1 152 ? 40.378 -22.085 -11.407 1.00 14.90 ?  152  TYR   B H    1 
ATOM   6176 H  HA   . TYR   B 1 152 ? 40.342 -24.398 -12.833 1.00 15.05 ?  152  TYR   B HA   1 
ATOM   6177 H  HB2  . TYR   B 1 152 ? 42.189 -22.251 -12.824 1.00 16.19 ?  152  TYR   B HB2  1 
ATOM   6178 H  HB3  . TYR   B 1 152 ? 42.536 -23.639 -13.516 1.00 16.19 ?  152  TYR   B HB3  1 
ATOM   6179 H  HD1  . TYR   B 1 152 ? 40.470 -20.788 -13.861 1.00 17.16 ?  152  TYR   B HD1  1 
ATOM   6180 H  HD2  . TYR   B 1 152 ? 41.576 -24.196 -15.640 1.00 18.36 ?  152  TYR   B HD2  1 
ATOM   6181 H  HE1  . TYR   B 1 152 ? 39.417 -20.115 -15.805 1.00 18.66 ?  152  TYR   B HE1  1 
ATOM   6182 H  HE2  . TYR   B 1 152 ? 40.530 -23.531 -17.576 1.00 19.30 ?  152  TYR   B HE2  1 
ATOM   6183 H  HH   . TYR   B 1 152 ? 39.345 -21.973 -18.628 1.00 22.32 ?  152  TYR   B HH   1 
ATOM   6184 N  N    . LEU   B 1 153 ? 41.199 -25.671 -10.907 1.00 12.38 ?  153  LEU   B N    1 
ATOM   6185 C  CA   . LEU   B 1 153 ? 41.710 -26.421 -9.769  1.00 11.82 ?  153  LEU   B CA   1 
ATOM   6186 C  C    . LEU   B 1 153 ? 42.942 -27.220 -10.168 1.00 11.89 ?  153  LEU   B C    1 
ATOM   6187 O  O    . LEU   B 1 153 ? 42.929 -27.944 -11.167 1.00 13.29 ?  153  LEU   B O    1 
ATOM   6188 C  CB   . LEU   B 1 153 ? 40.637 -27.379 -9.250  1.00 12.44 ?  153  LEU   B CB   1 
ATOM   6189 C  CG   . LEU   B 1 153 ? 39.378 -26.729 -8.677  1.00 13.09 ?  153  LEU   B CG   1 
ATOM   6190 C  CD1  . LEU   B 1 153 ? 38.275 -27.773 -8.532  1.00 13.74 ?  153  LEU   B CD1  1 
ATOM   6191 C  CD2  . LEU   B 1 153 ? 39.671 -26.070 -7.336  1.00 13.59 ?  153  LEU   B CD2  1 
ATOM   6192 H  H    . LEU   B 1 153 ? 40.625 -26.116 -11.383 1.00 14.84 ?  153  LEU   B H    1 
ATOM   6193 H  HA   . LEU   B 1 153 ? 41.938 -25.807 -9.060  1.00 14.18 ?  153  LEU   B HA   1 
ATOM   6194 H  HB2  . LEU   B 1 153 ? 40.354 -27.955 -9.978  1.00 14.93 ?  153  LEU   B HB2  1 
ATOM   6195 H  HB3  . LEU   B 1 153 ? 41.023 -27.921 -8.543  1.00 14.93 ?  153  LEU   B HB3  1 
ATOM   6196 H  HG   . LEU   B 1 153 ? 39.064 -26.040 -9.286  1.00 15.71 ?  153  LEU   B HG   1 
ATOM   6197 H  HD11 . LEU   B 1 153 ? 37.471 -27.335 -8.208  1.00 16.49 ?  153  LEU   B HD11 1 
ATOM   6198 H  HD12 . LEU   B 1 153 ? 38.110 -28.172 -9.397  1.00 16.49 ?  153  LEU   B HD12 1 
ATOM   6199 H  HD13 . LEU   B 1 153 ? 38.565 -28.444 -7.899  1.00 16.49 ?  153  LEU   B HD13 1 
ATOM   6200 H  HD21 . LEU   B 1 153 ? 38.853 -25.695 -6.977  1.00 16.30 ?  153  LEU   B HD21 1 
ATOM   6201 H  HD22 . LEU   B 1 153 ? 40.022 -26.742 -6.726  1.00 16.30 ?  153  LEU   B HD22 1 
ATOM   6202 H  HD23 . LEU   B 1 153 ? 40.330 -25.369 -7.465  1.00 16.30 ?  153  LEU   B HD23 1 
ATOM   6203 N  N    . ALA   B 1 154 ? 43.994 -27.107 -9.369  1.00 12.01 ?  154  ALA   B N    1 
ATOM   6204 C  CA   . ALA   B 1 154 ? 45.222 -27.865 -9.556  1.00 13.17 ?  154  ALA   B CA   1 
ATOM   6205 C  C    . ALA   B 1 154 ? 45.284 -28.946 -8.486  1.00 13.84 ?  154  ALA   B C    1 
ATOM   6206 O  O    . ALA   B 1 154 ? 45.214 -28.652 -7.286  1.00 15.38 ?  154  ALA   B O    1 
ATOM   6207 C  CB   . ALA   B 1 154 ? 46.442 -26.950 -9.485  1.00 14.15 ?  154  ALA   B CB   1 
ATOM   6208 H  H    . ALA   B 1 154 ? 44.017 -26.573 -8.688  1.00 14.40 ?  154  ALA   B H    1 
ATOM   6209 H  HA   . ALA   B 1 154 ? 45.208 -28.290 -10.423 1.00 15.79 ?  154  ALA   B HA   1 
ATOM   6210 H  HB1  . ALA   B 1 154 ? 47.245 -27.481 -9.611  1.00 16.98 ?  154  ALA   B HB1  1 
ATOM   6211 H  HB2  . ALA   B 1 154 ? 46.379 -26.277 -10.182 1.00 16.98 ?  154  ALA   B HB2  1 
ATOM   6212 H  HB3  . ALA   B 1 154 ? 46.468 -26.518 -8.614  1.00 16.98 ?  154  ALA   B HB3  1 
ATOM   6213 N  N    . VAL   B 1 155 ? 45.397 -30.194 -8.923  1.00 12.84 ?  155  VAL   B N    1 
ATOM   6214 C  CA   . VAL   B 1 155 ? 45.504 -31.342 -8.034  1.00 13.30 ?  155  VAL   B CA   1 
ATOM   6215 C  C    . VAL   B 1 155 ? 46.846 -32.009 -8.310  1.00 13.73 ?  155  VAL   B C    1 
ATOM   6216 O  O    . VAL   B 1 155 ? 47.087 -32.499 -9.422  1.00 15.41 ?  155  VAL   B O    1 
ATOM   6217 C  CB   . VAL   B 1 155 ? 44.345 -32.334 -8.235  1.00 14.64 ?  155  VAL   B CB   1 
ATOM   6218 C  CG1  . VAL   B 1 155 ? 44.537 -33.540 -7.335  1.00 14.58 ?  155  VAL   B CG1  1 
ATOM   6219 C  CG2  . VAL   B 1 155 ? 43.005 -31.649 -7.966  1.00 15.69 ?  155  VAL   B CG2  1 
ATOM   6220 H  H    . VAL   B 1 155 ? 45.419 -30.406 -9.757  1.00 15.40 ?  155  VAL   B H    1 
ATOM   6221 H  HA   . VAL   B 1 155 ? 45.489 -31.046 -7.114  1.00 15.96 ?  155  VAL   B HA   1 
ATOM   6222 H  HB   . VAL   B 1 155 ? 44.342 -32.641 -9.157  1.00 17.56 ?  155  VAL   B HB   1 
ATOM   6223 H  HG11 . VAL   B 1 155 ? 43.709 -34.042 -7.290  1.00 17.49 ?  155  VAL   B HG11 1 
ATOM   6224 H  HG12 . VAL   B 1 155 ? 45.241 -34.105 -7.701  1.00 17.49 ?  155  VAL   B HG12 1 
ATOM   6225 H  HG13 . VAL   B 1 155 ? 44.788 -33.239 -6.447  1.00 17.49 ?  155  VAL   B HG13 1 
ATOM   6226 H  HG21 . VAL   B 1 155 ? 42.293 -32.299 -8.061  1.00 18.82 ?  155  VAL   B HG21 1 
ATOM   6227 H  HG22 . VAL   B 1 155 ? 43.011 -31.295 -7.062  1.00 18.82 ?  155  VAL   B HG22 1 
ATOM   6228 H  HG23 . VAL   B 1 155 ? 42.885 -30.928 -8.603  1.00 18.82 ?  155  VAL   B HG23 1 
ATOM   6229 N  N    . PHE   B 1 156 ? 47.708 -32.054 -7.293  1.00 14.11 ?  156  PHE   B N    1 
ATOM   6230 C  CA   . PHE   B 1 156 ? 49.086 -32.509 -7.492  1.00 15.21 ?  156  PHE   B CA   1 
ATOM   6231 C  C    . PHE   B 1 156 ? 49.185 -34.009 -7.775  1.00 16.33 ?  156  PHE   B C    1 
ATOM   6232 O  O    . PHE   B 1 156 ? 49.923 -34.436 -8.675  1.00 18.04 ?  156  PHE   B O    1 
ATOM   6233 C  CB   . PHE   B 1 156 ? 49.912 -32.141 -6.262  1.00 15.16 ?  156  PHE   B CB   1 
ATOM   6234 C  CG   . PHE   B 1 156 ? 51.333 -32.599 -6.321  1.00 15.44 ?  156  PHE   B CG   1 
ATOM   6235 C  CD1  . PHE   B 1 156 ? 52.216 -32.061 -7.239  1.00 17.29 ?  156  PHE   B CD1  1 
ATOM   6236 C  CD2  . PHE   B 1 156 ? 51.792 -33.560 -5.443  1.00 15.56 ?  156  PHE   B CD2  1 
ATOM   6237 C  CE1  . PHE   B 1 156 ? 53.537 -32.474 -7.285  1.00 18.21 ?  156  PHE   B CE1  1 
ATOM   6238 C  CE2  . PHE   B 1 156 ? 53.109 -33.980 -5.485  1.00 17.17 ?  156  PHE   B CE2  1 
ATOM   6239 C  CZ   . PHE   B 1 156 ? 53.975 -33.437 -6.412  1.00 17.86 ?  156  PHE   B CZ   1 
ATOM   6240 H  H    . PHE   B 1 156 ? 47.518 -31.835 -6.479  1.00 16.93 ?  156  PHE   B H    1 
ATOM   6241 H  HA   . PHE   B 1 156 ? 49.456 -32.037 -8.248  1.00 18.25 ?  156  PHE   B HA   1 
ATOM   6242 H  HB2  . PHE   B 1 156 ? 49.920 -31.174 -6.172  1.00 18.19 ?  156  PHE   B HB2  1 
ATOM   6243 H  HB3  . PHE   B 1 156 ? 49.507 -32.540 -5.477  1.00 18.19 ?  156  PHE   B HB3  1 
ATOM   6244 H  HD1  . PHE   B 1 156 ? 51.922 -31.406 -7.833  1.00 20.75 ?  156  PHE   B HD1  1 
ATOM   6245 H  HD2  . PHE   B 1 156 ? 51.208 -33.932 -4.821  1.00 18.66 ?  156  PHE   B HD2  1 
ATOM   6246 H  HE1  . PHE   B 1 156 ? 54.122 -32.107 -7.909  1.00 21.84 ?  156  PHE   B HE1  1 
ATOM   6247 H  HE2  . PHE   B 1 156 ? 53.407 -34.636 -4.893  1.00 20.59 ?  156  PHE   B HE2  1 
ATOM   6248 H  HZ   . PHE   B 1 156 ? 54.863 -33.724 -6.438  1.00 21.43 ?  156  PHE   B HZ   1 
ATOM   6249 N  N    . ASP   B 1 157 ? 48.513 -34.828 -6.983  1.00 16.61 ?  157  ASP   B N    1 
ATOM   6250 C  CA   . ASP   B 1 157 ? 48.668 -36.274 -7.080  1.00 17.80 ?  157  ASP   B CA   1 
ATOM   6251 C  C    . ASP   B 1 157 ? 47.752 -36.816 -8.172  1.00 17.53 ?  157  ASP   B C    1 
ATOM   6252 O  O    . ASP   B 1 157 ? 46.526 -36.694 -8.072  1.00 16.99 ?  157  ASP   B O    1 
ATOM   6253 C  CB   . ASP   B 1 157 ? 48.313 -36.888 -5.733  1.00 18.81 ?  157  ASP   B CB   1 
ATOM   6254 C  CG   . ASP   B 1 157 ? 48.443 -38.395 -5.721  1.00 20.85 ?  157  ASP   B CG   1 
ATOM   6255 O  OD1  . ASP   B 1 157 ? 48.771 -38.998 -6.771  1.00 21.34 ?  157  ASP   B OD1  1 
ATOM   6256 O  OD2  . ASP   B 1 157 ? 48.236 -38.982 -4.641  1.00 22.76 -1 157  ASP   B OD2  1 
ATOM   6257 H  H    . ASP   B 1 157 ? 47.962 -34.575 -6.379  1.00 19.92 ?  157  ASP   B H    1 
ATOM   6258 H  HA   . ASP   B 1 157 ? 49.588 -36.500 -7.300  1.00 21.36 ?  157  ASP   B HA   1 
ATOM   6259 H  HB2  . ASP   B 1 157 ? 48.898 -36.516 -5.058  1.00 22.57 ?  157  ASP   B HB2  1 
ATOM   6260 H  HB3  . ASP   B 1 157 ? 47.390 -36.664 -5.526  1.00 22.57 ?  157  ASP   B HB3  1 
ATOM   6261 N  N    . LYS   B 1 158 ? 48.348 -37.427 -9.204  1.00 18.56 ?  158  LYS   B N    1 
ATOM   6262 C  CA   . LYS   B 1 158 ? 47.573 -38.030 -10.289 1.00 19.67 ?  158  LYS   B CA   1 
ATOM   6263 C  C    . LYS   B 1 158 ? 46.520 -39.003 -9.764  1.00 19.91 ?  158  LYS   B C    1 
ATOM   6264 O  O    . LYS   B 1 158 ? 45.419 -39.095 -10.318 1.00 19.94 ?  158  LYS   B O    1 
ATOM   6265 C  CB   . LYS   B 1 158 ? 48.520 -38.738 -11.268 1.00 21.65 ?  158  LYS   B CB   1 
ATOM   6266 C  CG   . LYS   B 1 158 ? 47.839 -39.648 -12.286 1.00 23.95 ?  158  LYS   B CG   1 
ATOM   6267 C  CD   . LYS   B 1 158 ? 46.988 -38.874 -13.269 1.00 26.18 ?  158  LYS   B CD   1 
ATOM   6268 C  CE   . LYS   B 1 158 ? 46.398 -39.801 -14.318 1.00 28.24 ?  158  LYS   B CE   1 
ATOM   6269 N  NZ   . LYS   B 1 158 ? 45.349 -39.122 -15.133 1.00 28.55 ?  158  LYS   B NZ   1 
ATOM   6270 H  H    . LYS   B 1 158 ? 49.203 -37.511 -9.298  1.00 22.27 ?  158  LYS   B H    1 
ATOM   6271 H  HA   . LYS   B 1 158 ? 47.117 -37.330 -10.781 1.00 23.59 ?  158  LYS   B HA   1 
ATOM   6272 H  HB2  . LYS   B 1 158 ? 49.009 -38.066 -11.773 1.00 25.98 ?  158  LYS   B HB2  1 
ATOM   6273 H  HB3  . LYS   B 1 158 ? 49.142 -39.283 -10.766 1.00 25.98 ?  158  LYS   B HB3  1 
ATOM   6274 H  HG2  . LYS   B 1 158 ? 48.522 -40.115 -12.794 1.00 28.73 ?  158  LYS   B HG2  1 
ATOM   6275 H  HG3  . LYS   B 1 158 ? 47.275 -40.298 -11.835 1.00 28.73 ?  158  LYS   B HG3  1 
ATOM   6276 H  HD2  . LYS   B 1 158 ? 46.259 -38.442 -12.796 1.00 31.41 ?  158  LYS   B HD2  1 
ATOM   6277 H  HD3  . LYS   B 1 158 ? 47.536 -38.214 -13.721 1.00 31.41 ?  158  LYS   B HD3  1 
ATOM   6278 H  HE2  . LYS   B 1 158 ? 47.098 -40.098 -14.918 1.00 33.89 ?  158  LYS   B HE2  1 
ATOM   6279 H  HE3  . LYS   B 1 158 ? 45.989 -40.566 -13.879 1.00 33.89 ?  158  LYS   B HE3  1 
ATOM   6280 H  HZ1  . LYS   B 1 158 ? 45.018 -39.685 -15.738 1.00 34.25 ?  158  LYS   B HZ1  1 
ATOM   6281 H  HZ2  . LYS   B 1 158 ? 44.687 -38.842 -14.606 1.00 34.25 ?  158  LYS   B HZ2  1 
ATOM   6282 H  HZ3  . LYS   B 1 158 ? 45.699 -38.419 -15.553 1.00 34.25 ?  158  LYS   B HZ3  1 
ATOM   6283 N  N    . ASN   B 1 159 ? 46.840 -39.754 -8.710  1.00 20.23 ?  159  ASN   B N    1 
ATOM   6284 C  CA   . ASN   B 1 159 ? 45.884 -40.735 -8.208  1.00 20.77 ?  159  ASN   B CA   1 
ATOM   6285 C  C    . ASN   B 1 159 ? 44.689 -40.068 -7.529  1.00 19.51 ?  159  ASN   B C    1 
ATOM   6286 O  O    . ASN   B 1 159 ? 43.554 -40.555 -7.647  1.00 19.43 ?  159  ASN   B O    1 
ATOM   6287 C  CB   . ASN   B 1 159 ? 46.592 -41.718 -7.281  1.00 22.12 ?  159  ASN   B CB   1 
ATOM   6288 C  CG   . ASN   B 1 159 ? 47.614 -42.559 -8.014  1.00 24.11 ?  159  ASN   B CG   1 
ATOM   6289 O  OD1  . ASN   B 1 159 ? 47.338 -43.088 -9.096  1.00 25.07 ?  159  ASN   B OD1  1 
ATOM   6290 N  ND2  . ASN   B 1 159 ? 48.802 -42.689 -7.434  1.00 24.83 ?  159  ASN   B ND2  1 
ATOM   6291 H  H    . ASN   B 1 159 ? 47.578 -39.701 -8.277  1.00 24.27 ?  159  ASN   B H    1 
ATOM   6292 H  HA   . ASN   B 1 159 ? 45.546 -41.240 -8.965  1.00 24.92 ?  159  ASN   B HA   1 
ATOM   6293 H  HB2  . ASN   B 1 159 ? 47.052 -41.229 -6.585  1.00 26.54 ?  159  ASN   B HB2  1 
ATOM   6294 H  HB3  . ASN   B 1 159 ? 45.937 -42.319 -6.897  1.00 26.54 ?  159  ASN   B HB3  1 
ATOM   6295 H  HD21 . ASN   B 1 159 ? 49.421 -43.156 -7.815  1.00 29.79 ?  159  ASN   B HD21 1 
ATOM   6296 H  HD22 . ASN   B 1 159 ? 48.955 -42.316 -6.676  1.00 29.79 ?  159  ASN   B HD22 1 
ATOM   6297 N  N    . LEU   B 1 160 ? 44.903 -38.940 -6.847  1.00 18.41 ?  160  LEU   B N    1 
ATOM   6298 C  CA   . LEU   B 1 160 ? 43.766 -38.212 -6.297  1.00 17.62 ?  160  LEU   B CA   1 
ATOM   6299 C  C    . LEU   B 1 160 ? 42.977 -37.537 -7.407  1.00 16.95 ?  160  LEU   B C    1 
ATOM   6300 O  O    . LEU   B 1 160 ? 41.741 -37.530 -7.386  1.00 16.60 ?  160  LEU   B O    1 
ATOM   6301 C  CB   . LEU   B 1 160 ? 44.229 -37.184 -5.265  1.00 17.30 ?  160  LEU   B CB   1 
ATOM   6302 C  CG   . LEU   B 1 160 ? 43.102 -36.287 -4.737  1.00 16.89 ?  160  LEU   B CG   1 
ATOM   6303 C  CD1  . LEU   B 1 160 ? 41.987 -37.116 -4.108  1.00 17.72 ?  160  LEU   B CD1  1 
ATOM   6304 C  CD2  . LEU   B 1 160 ? 43.649 -35.270 -3.742  1.00 17.21 ?  160  LEU   B CD2  1 
ATOM   6305 H  H    . LEU   B 1 160 ? 45.677 -38.580 -6.708  1.00 22.09 ?  160  LEU   B H    1 
ATOM   6306 H  HA   . LEU   B 1 160 ? 43.185 -38.842 -5.855  1.00 21.14 ?  160  LEU   B HA   1 
ATOM   6307 H  HB2  . LEU   B 1 160 ? 44.620 -37.658 -4.510  1.00 20.75 ?  160  LEU   B HB2  1 
ATOM   6308 H  HB3  . LEU   B 1 160 ? 44.905 -36.613 -5.671  1.00 20.75 ?  160  LEU   B HB3  1 
ATOM   6309 H  HG   . LEU   B 1 160 ? 42.725 -35.795 -5.478  1.00 20.26 ?  160  LEU   B HG   1 
ATOM   6310 H  HD11 . LEU   B 1 160 ? 41.352 -36.518 -3.690  1.00 21.26 ?  160  LEU   B HD11 1 
ATOM   6311 H  HD12 . LEU   B 1 160 ? 41.545 -37.636 -4.799  1.00 21.26 ?  160  LEU   B HD12 1 
ATOM   6312 H  HD13 . LEU   B 1 160 ? 42.369 -37.712 -3.442  1.00 21.26 ?  160  LEU   B HD13 1 
ATOM   6313 H  HD21 . LEU   B 1 160 ? 42.921 -34.701 -3.448  1.00 20.65 ?  160  LEU   B HD21 1 
ATOM   6314 H  HD22 . LEU   B 1 160 ? 44.031 -35.739 -2.985  1.00 20.65 ?  160  LEU   B HD22 1 
ATOM   6315 H  HD23 . LEU   B 1 160 ? 44.331 -34.735 -4.179  1.00 20.65 ?  160  LEU   B HD23 1 
ATOM   6316 N  N    . TYR   B 1 161 ? 43.678 -36.971 -8.391  1.00 17.00 ?  161  TYR   B N    1 
ATOM   6317 C  CA   . TYR   B 1 161 ? 43.005 -36.399 -9.551  1.00 16.74 ?  161  TYR   B CA   1 
ATOM   6318 C  C    . TYR   B 1 161 ? 42.063 -37.416 -10.175 1.00 16.47 ?  161  TYR   B C    1 
ATOM   6319 O  O    . TYR   B 1 161 ? 40.891 -37.121 -10.427 1.00 16.21 ?  161  TYR   B O    1 
ATOM   6320 C  CB   . TYR   B 1 161 ? 44.051 -35.917 -10.564 1.00 17.46 ?  161  TYR   B CB   1 
ATOM   6321 C  CG   . TYR   B 1 161 ? 43.478 -35.450 -11.878 1.00 17.95 ?  161  TYR   B CG   1 
ATOM   6322 C  CD1  . TYR   B 1 161 ? 43.092 -34.126 -12.052 1.00 17.82 ?  161  TYR   B CD1  1 
ATOM   6323 C  CD2  . TYR   B 1 161 ? 43.297 -36.329 -12.938 1.00 18.54 ?  161  TYR   B CD2  1 
ATOM   6324 C  CE1  . TYR   B 1 161 ? 42.560 -33.690 -13.243 1.00 18.84 ?  161  TYR   B CE1  1 
ATOM   6325 C  CE2  . TYR   B 1 161 ? 42.760 -35.900 -14.133 1.00 19.58 ?  161  TYR   B CE2  1 
ATOM   6326 C  CZ   . TYR   B 1 161 ? 42.396 -34.579 -14.281 1.00 19.52 ?  161  TYR   B CZ   1 
ATOM   6327 O  OH   . TYR   B 1 161 ? 41.863 -34.140 -15.467 1.00 21.53 ?  161  TYR   B OH   1 
ATOM   6328 H  H    . TYR   B 1 161 ? 44.533 -36.913 -8.416  1.00 20.40 ?  161  TYR   B H    1 
ATOM   6329 H  HA   . TYR   B 1 161 ? 42.478 -35.634 -9.273  1.00 20.09 ?  161  TYR   B HA   1 
ATOM   6330 H  HB2  . TYR   B 1 161 ? 44.538 -35.172 -10.176 1.00 20.95 ?  161  TYR   B HB2  1 
ATOM   6331 H  HB3  . TYR   B 1 161 ? 44.661 -36.643 -10.754 1.00 20.95 ?  161  TYR   B HB3  1 
ATOM   6332 H  HD1  . TYR   B 1 161 ? 43.209 -33.515 -11.358 1.00 21.38 ?  161  TYR   B HD1  1 
ATOM   6333 H  HD2  . TYR   B 1 161 ? 43.536 -37.220 -12.842 1.00 22.24 ?  161  TYR   B HD2  1 
ATOM   6334 H  HE1  . TYR   B 1 161 ? 42.319 -32.793 -13.346 1.00 22.60 ?  161  TYR   B HE1  1 
ATOM   6335 H  HE2  . TYR   B 1 161 ? 42.643 -36.498 -14.837 1.00 23.49 ?  161  TYR   B HE2  1 
ATOM   6336 H  HH   . TYR   B 1 161 ? 41.811 -34.784 -16.010 1.00 25.83 ?  161  TYR   B HH   1 
ATOM   6337 N  N    . ASP   B 1 162 ? 42.560 -38.632 -10.415 1.00 17.08 ?  162  ASP   B N    1 
ATOM   6338 C  CA   . ASP   B 1 162 ? 41.729 -39.665 -11.027 1.00 17.66 ?  162  ASP   B CA   1 
ATOM   6339 C  C    . ASP   B 1 162 ? 40.525 -40.004 -10.155 1.00 16.86 ?  162  ASP   B C    1 
ATOM   6340 O  O    . ASP   B 1 162 ? 39.420 -40.219 -10.667 1.00 17.11 ?  162  ASP   B O    1 
ATOM   6341 C  CB   . ASP   B 1 162 ? 42.561 -40.926 -11.278 1.00 19.16 ?  162  ASP   B CB   1 
ATOM   6342 C  CG   . ASP   B 1 162 ? 43.558 -40.768 -12.413 1.00 20.15 ?  162  ASP   B CG   1 
ATOM   6343 O  OD1  . ASP   B 1 162 ? 43.427 -39.820 -13.211 1.00 20.25 ?  162  ASP   B OD1  1 
ATOM   6344 O  OD2  . ASP   B 1 162 ? 44.456 -41.631 -12.524 1.00 22.20 -1 162  ASP   B OD2  1 
ATOM   6345 H  H    . ASP   B 1 162 ? 43.366 -38.873 -10.244 1.00 20.48 ?  162  ASP   B H    1 
ATOM   6346 H  HA   . ASP   B 1 162 ? 41.400 -39.347 -11.881 1.00 21.18 ?  162  ASP   B HA   1 
ATOM   6347 H  HB2  . ASP   B 1 162 ? 43.063 -41.140 -10.478 1.00 22.99 ?  162  ASP   B HB2  1 
ATOM   6348 H  HB3  . ASP   B 1 162 ? 41.969 -41.656 -11.509 1.00 22.99 ?  162  ASP   B HB3  1 
ATOM   6349 N  N    . LYS   B 1 163 ? 40.720 -40.083 -8.836  1.00 16.35 ?  163  LYS   B N    1 
ATOM   6350 C  CA   . LYS   B 1 163 ? 39.599 -40.363 -7.945  1.00 17.33 ?  163  LYS   B CA   1 
ATOM   6351 C  C    . LYS   B 1 163 ? 38.553 -39.256 -8.008  1.00 15.83 ?  163  LYS   B C    1 
ATOM   6352 O  O    . LYS   B 1 163 ? 37.342 -39.525 -8.006  1.00 16.73 ?  163  LYS   B O    1 
ATOM   6353 C  CB   . LYS   B 1 163 ? 40.094 -40.540 -6.511  1.00 20.91 ?  163  LYS   B CB   1 
ATOM   6354 C  CG   . LYS   B 1 163 ? 38.999 -41.003 -5.576  1.00 26.77 ?  163  LYS   B CG   1 
ATOM   6355 C  CD   . LYS   B 1 163 ? 39.492 -41.282 -4.170  1.00 32.04 ?  163  LYS   B CD   1 
ATOM   6356 C  CE   . LYS   B 1 163 ? 38.387 -41.937 -3.350  1.00 35.83 ?  163  LYS   B CE   1 
ATOM   6357 N  NZ   . LYS   B 1 163 ? 38.499 -41.642 -1.896  1.00 38.79 ?  163  LYS   B NZ   1 
ATOM   6358 H  H    . LYS   B 1 163 ? 41.481 -39.975 -8.443  1.00 19.61 ?  163  LYS   B H    1 
ATOM   6359 H  HA   . LYS   B 1 163 ? 39.180 -41.188 -8.224  1.00 20.79 ?  163  LYS   B HA   1 
ATOM   6360 H  HB2  . LYS   B 1 163 ? 40.800 -41.208 -6.500  1.00 25.08 ?  163  LYS   B HB2  1 
ATOM   6361 H  HB3  . LYS   B 1 163 ? 40.433 -39.694 -6.184  1.00 25.08 ?  163  LYS   B HB3  1 
ATOM   6362 H  HG2  . LYS   B 1 163 ? 38.319 -40.315 -5.521  1.00 32.12 ?  163  LYS   B HG2  1 
ATOM   6363 H  HG3  . LYS   B 1 163 ? 38.612 -41.822 -5.926  1.00 32.12 ?  163  LYS   B HG3  1 
ATOM   6364 H  HD2  . LYS   B 1 163 ? 40.250 -41.889 -4.205  1.00 38.44 ?  163  LYS   B HD2  1 
ATOM   6365 H  HD3  . LYS   B 1 163 ? 39.743 -40.449 -3.742  1.00 38.44 ?  163  LYS   B HD3  1 
ATOM   6366 H  HE2  . LYS   B 1 163 ? 37.524 -41.621 -3.663  1.00 42.99 ?  163  LYS   B HE2  1 
ATOM   6367 H  HE3  . LYS   B 1 163 ? 38.441 -42.899 -3.464  1.00 42.99 ?  163  LYS   B HE3  1 
ATOM   6368 H  HZ1  . LYS   B 1 163 ? 37.836 -42.039 -1.454  1.00 46.54 ?  163  LYS   B HZ1  1 
ATOM   6369 H  HZ2  . LYS   B 1 163 ? 39.276 -41.942 -1.586  1.00 46.54 ?  163  LYS   B HZ2  1 
ATOM   6370 H  HZ3  . LYS   B 1 163 ? 38.451 -40.764 -1.760  1.00 46.54 ?  163  LYS   B HZ3  1 
ATOM   6371 N  N    . LEU   B 1 164 ? 39.007 -38.002 -8.056  1.00 14.96 ?  164  LEU   B N    1 
ATOM   6372 C  CA   . LEU   B 1 164 ? 38.095 -36.863 -8.110  1.00 14.55 ?  164  LEU   B CA   1 
ATOM   6373 C  C    . LEU   B 1 164 ? 37.311 -36.840 -9.416  1.00 14.86 ?  164  LEU   B C    1 
ATOM   6374 O  O    . LEU   B 1 164 ? 36.087 -36.642 -9.415  1.00 15.62 ?  164  LEU   B O    1 
ATOM   6375 C  CB   . LEU   B 1 164 ? 38.897 -35.572 -7.945  1.00 14.22 ?  164  LEU   B CB   1 
ATOM   6376 C  CG   . LEU   B 1 164 ? 39.430 -35.302 -6.542  1.00 15.27 ?  164  LEU   B CG   1 
ATOM   6377 C  CD1  . LEU   B 1 164 ? 40.523 -34.246 -6.588  1.00 15.32 ?  164  LEU   B CD1  1 
ATOM   6378 C  CD2  . LEU   B 1 164 ? 38.314 -34.872 -5.605  1.00 17.07 ?  164  LEU   B CD2  1 
ATOM   6379 H  H    . LEU   B 1 164 ? 39.847 -37.781 -8.055  1.00 17.94 ?  164  LEU   B H    1 
ATOM   6380 H  HA   . LEU   B 1 164 ? 37.471 -36.923 -7.379  1.00 17.45 ?  164  LEU   B HA   1 
ATOM   6381 H  HB2  . LEU   B 1 164 ? 39.664 -35.602 -8.545  1.00 17.06 ?  164  LEU   B HB2  1 
ATOM   6382 H  HB3  . LEU   B 1 164 ? 38.331 -34.823 -8.191  1.00 17.06 ?  164  LEU   B HB3  1 
ATOM   6383 H  HG   . LEU   B 1 164 ? 39.819 -36.114 -6.193  1.00 18.32 ?  164  LEU   B HG   1 
ATOM   6384 H  HD11 . LEU   B 1 164 ? 40.845 -34.080 -5.685  1.00 18.38 ?  164  LEU   B HD11 1 
ATOM   6385 H  HD12 . LEU   B 1 164 ? 41.257 -34.568 -7.139  1.00 18.38 ?  164  LEU   B HD12 1 
ATOM   6386 H  HD13 . LEU   B 1 164 ? 40.167 -33.426 -6.964  1.00 18.38 ?  164  LEU   B HD13 1 
ATOM   6387 H  HD21 . LEU   B 1 164 ? 38.690 -34.652 -4.740  1.00 20.48 ?  164  LEU   B HD21 1 
ATOM   6388 H  HD22 . LEU   B 1 164 ? 37.865 -34.096 -5.978  1.00 20.48 ?  164  LEU   B HD22 1 
ATOM   6389 H  HD23 . LEU   B 1 164 ? 37.681 -35.604 -5.513  1.00 20.48 ?  164  LEU   B HD23 1 
ATOM   6390 N  N    . VAL   B 1 165 ? 38.000 -37.011 -10.543 1.00 16.21 ?  165  VAL   B N    1 
ATOM   6391 C  CA   . VAL   B 1 165 ? 37.344 -36.947 -11.843 1.00 17.53 ?  165  VAL   B CA   1 
ATOM   6392 C  C    . VAL   B 1 165 ? 36.425 -38.144 -12.028 1.00 19.18 ?  165  VAL   B C    1 
ATOM   6393 O  O    . VAL   B 1 165 ? 35.264 -38.006 -12.433 1.00 20.38 ?  165  VAL   B O    1 
ATOM   6394 C  CB   . VAL   B 1 165 ? 38.389 -36.858 -12.971 1.00 18.39 ?  165  VAL   B CB   1 
ATOM   6395 C  CG1  . VAL   B 1 165 ? 37.725 -36.960 -14.325 1.00 20.03 ?  165  VAL   B CG1  1 
ATOM   6396 C  CG2  . VAL   B 1 165 ? 39.177 -35.567 -12.864 1.00 18.44 ?  165  VAL   B CG2  1 
ATOM   6397 H  H    . VAL   B 1 165 ? 38.850 -37.156 -10.583 1.00 19.44 ?  165  VAL   B H    1 
ATOM   6398 H  HA   . VAL   B 1 165 ? 36.800 -36.146 -11.884 1.00 21.03 ?  165  VAL   B HA   1 
ATOM   6399 H  HB   . VAL   B 1 165 ? 39.017 -37.590 -12.885 1.00 22.06 ?  165  VAL   B HB   1 
ATOM   6400 H  HG11 . VAL   B 1 165 ? 38.343 -36.657 -15.005 1.00 24.03 ?  165  VAL   B HG11 1 
ATOM   6401 H  HG12 . VAL   B 1 165 ? 37.492 -37.890 -14.487 1.00 24.03 ?  165  VAL   B HG12 1 
ATOM   6402 H  HG13 . VAL   B 1 165 ? 36.927 -36.414 -14.329 1.00 24.03 ?  165  VAL   B HG13 1 
ATOM   6403 H  HG21 . VAL   B 1 165 ? 39.811 -35.516 -13.598 1.00 22.12 ?  165  VAL   B HG21 1 
ATOM   6404 H  HG22 . VAL   B 1 165 ? 38.564 -34.813 -12.909 1.00 22.12 ?  165  VAL   B HG22 1 
ATOM   6405 H  HG23 . VAL   B 1 165 ? 39.653 -35.551 -12.018 1.00 22.12 ?  165  VAL   B HG23 1 
ATOM   6406 N  N    . SER   B 1 166 ? 36.937 -39.342 -11.730 1.00 20.07 ?  166  SER   B N    1 
ATOM   6407 C  CA   . SER   B 1 166 ? 36.187 -40.556 -12.008 1.00 21.42 ?  166  SER   B CA   1 
ATOM   6408 C  C    . SER   B 1 166 ? 34.930 -40.643 -11.157 1.00 21.60 ?  166  SER   B C    1 
ATOM   6409 O  O    . SER   B 1 166 ? 33.958 -41.260 -11.583 1.00 22.67 ?  166  SER   B O    1 
ATOM   6410 C  CB   . SER   B 1 166 ? 37.062 -41.807 -11.839 1.00 22.55 ?  166  SER   B CB   1 
ATOM   6411 O  OG   . SER   B 1 166 ? 37.419 -42.022 -10.484 1.00 22.58 ?  166  SER   B OG   1 
ATOM   6412 H  H    . SER   B 1 166 ? 37.712 -39.471 -11.374 1.00 24.07 ?  166  SER   B H    1 
ATOM   6413 H  HA   . SER   B 1 166 ? 35.907 -40.538 -12.935 1.00 25.70 ?  166  SER   B HA   1 
ATOM   6414 H  HB2  . SER   B 1 166 ? 36.572 -42.581 -12.159 1.00 27.06 ?  166  SER   B HB2  1 
ATOM   6415 H  HB3  . SER   B 1 166 ? 37.873 -41.697 -12.366 1.00 27.06 ?  166  SER   B HB3  1 
ATOM   6416 H  HG   . SER   B 1 166 ? 37.863 -41.369 -10.198 1.00 27.09 ?  166  SER   B HG   1 
ATOM   6417 N  N    . SER   B 1 167 ? 34.913 -40.033 -9.974  1.00 20.20 ?  167  SER   B N    1 
ATOM   6418 C  CA   . SER   B 1 167 ? 33.757 -40.093 -9.086  1.00 19.92 ?  167  SER   B CA   1 
ATOM   6419 C  C    . SER   B 1 167 ? 32.839 -38.874 -9.185  1.00 19.61 ?  167  SER   B C    1 
ATOM   6420 O  O    . SER   B 1 167 ? 31.760 -38.879 -8.580  1.00 19.81 ?  167  SER   B O    1 
ATOM   6421 C  CB   . SER   B 1 167 ? 34.203 -40.275 -7.629  1.00 19.66 ?  167  SER   B CB   1 
ATOM   6422 O  OG   . SER   B 1 167 ? 34.881 -39.118 -7.166  1.00 19.43 ?  167  SER   B OG   1 
ATOM   6423 H  H    . SER   B 1 167 ? 35.569 -39.584 -9.660  1.00 24.23 ?  167  SER   B H    1 
ATOM   6424 H  HA   . SER   B 1 167 ? 33.231 -40.876 -9.320  1.00 23.90 ?  167  SER   B HA   1 
ATOM   6425 H  HB2  . SER   B 1 167 ? 33.421 -40.427 -7.074  1.00 23.58 ?  167  SER   B HB2  1 
ATOM   6426 H  HB3  . SER   B 1 167 ? 34.797 -41.047 -7.573  1.00 23.58 ?  167  SER   B HB3  1 
ATOM   6427 H  HG   . SER   B 1 167 ? 35.573 -38.991 -7.634  1.00 23.31 ?  167  SER   B HG   1 
ATOM   6428 N  N    . PHE   B 1 168 ? 33.217 -37.838 -9.935  1.00 19.43 ?  168  PHE   B N    1 
ATOM   6429 C  CA   . PHE   B 1 168 ? 32.381 -36.638 -9.995  1.00 18.98 ?  168  PHE   B CA   1 
ATOM   6430 C  C    . PHE   B 1 168 ? 31.066 -36.901 -10.726 1.00 16.65 ?  168  PHE   B C    1 
ATOM   6431 O  O    . PHE   B 1 168 ? 30.026 -36.303 -10.392 1.00 17.31 ?  168  PHE   B O    1 
ATOM   6432 C  CB   . PHE   B 1 168 ? 33.139 -35.506 -10.678 1.00 19.54 ?  168  PHE   B CB   1 
ATOM   6433 C  CG   . PHE   B 1 168 ? 32.336 -34.259 -10.813 1.00 19.55 ?  168  PHE   B CG   1 
ATOM   6434 C  CD1  . PHE   B 1 168 ? 32.010 -33.519 -9.688  1.00 20.88 ?  168  PHE   B CD1  1 
ATOM   6435 C  CD2  . PHE   B 1 168 ? 31.888 -33.834 -12.047 1.00 18.75 ?  168  PHE   B CD2  1 
ATOM   6436 C  CE1  . PHE   B 1 168 ? 31.254 -32.370 -9.791  1.00 21.30 ?  168  PHE   B CE1  1 
ATOM   6437 C  CE2  . PHE   B 1 168 ? 31.139 -32.671 -12.165 1.00 20.28 ?  168  PHE   B CE2  1 
ATOM   6438 C  CZ   . PHE   B 1 168 ? 30.816 -31.938 -11.034 1.00 20.49 ?  168  PHE   B CZ   1 
ATOM   6439 H  H    . PHE   B 1 168 ? 33.936 -37.810 -10.407 1.00 23.31 ?  168  PHE   B H    1 
ATOM   6440 H  HA   . PHE   B 1 168 ? 32.171 -36.361 -9.093  1.00 22.77 ?  168  PHE   B HA   1 
ATOM   6441 H  HB2  . PHE   B 1 168 ? 33.928 -35.296 -10.152 1.00 23.44 ?  168  PHE   B HB2  1 
ATOM   6442 H  HB3  . PHE   B 1 168 ? 33.400 -35.789 -11.566 1.00 23.44 ?  168  PHE   B HB3  1 
ATOM   6443 H  HD1  . PHE   B 1 168 ? 32.300 -33.808 -8.853  1.00 25.05 ?  168  PHE   B HD1  1 
ATOM   6444 H  HD2  . PHE   B 1 168 ? 32.103 -34.321 -12.807 1.00 22.49 ?  168  PHE   B HD2  1 
ATOM   6445 H  HE1  . PHE   B 1 168 ? 31.040 -31.879 -9.031  1.00 25.55 ?  168  PHE   B HE1  1 
ATOM   6446 H  HE2  . PHE   B 1 168 ? 30.841 -32.391 -13.003 1.00 24.34 ?  168  PHE   B HE2  1 
ATOM   6447 H  HZ   . PHE   B 1 168 ? 30.305 -31.164 -11.113 1.00 24.58 ?  168  PHE   B HZ   1 
ATOM   6448 N  N    . LEU   B 1 169 ? 31.096 -37.785 -11.719 1.00 16.82 ?  169  LEU   B N    1 
ATOM   6449 C  CA   . LEU   B 1 169 ? 29.916 -38.091 -12.514 1.00 18.81 ?  169  LEU   B CA   1 
ATOM   6450 C  C    . LEU   B 1 169 ? 29.905 -39.524 -13.016 1.00 21.43 ?  169  LEU   B C    1 
ATOM   6451 O  O    . LEU   B 1 169 ? 28.989 -39.922 -13.735 1.00 23.93 ?  169  LEU   B O    1 
ATOM   6452 C  CB   . LEU   B 1 169 ? 29.831 -37.154 -13.716 1.00 20.74 ?  169  LEU   B CB   1 
ATOM   6453 C  CG   . LEU   B 1 169 ? 28.578 -36.280 -13.798 1.00 24.04 ?  169  LEU   B CG   1 
ATOM   6454 C  CD1  . LEU   B 1 169 ? 28.539 -35.550 -15.127 1.00 25.09 ?  169  LEU   B CD1  1 
ATOM   6455 C  CD2  . LEU   B 1 169 ? 27.310 -37.089 -13.595 1.00 24.16 ?  169  LEU   B CD2  1 
ATOM   6456 O  OXT  . LEU   B 1 169 ? 30.812 -40.294 -12.728 1.00 22.33 -1 169  LEU   B OXT  1 
ATOM   6457 H  H    . LEU   B 1 169 ? 31.799 -38.214 -11.965 1.00 20.18 ?  169  LEU   B H    1 
ATOM   6458 H  HA   . LEU   B 1 169 ? 29.131 -37.959 -11.966 1.00 22.57 ?  169  LEU   B HA   1 
ATOM   6459 H  HB2  . LEU   B 1 169 ? 30.595 -36.557 -13.697 1.00 24.88 ?  169  LEU   B HB2  1 
ATOM   6460 H  HB3  . LEU   B 1 169 ? 29.859 -37.686 -14.527 1.00 24.88 ?  169  LEU   B HB3  1 
ATOM   6461 H  HG   . LEU   B 1 169 ? 28.618 -35.610 -13.097 1.00 28.84 ?  169  LEU   B HG   1 
ATOM   6462 H  HD11 . LEU   B 1 169 ? 27.752 -34.982 -15.152 1.00 30.11 ?  169  LEU   B HD11 1 
ATOM   6463 H  HD12 . LEU   B 1 169 ? 29.339 -35.010 -15.215 1.00 30.11 ?  169  LEU   B HD12 1 
ATOM   6464 H  HD13 . LEU   B 1 169 ? 28.498 -36.203 -15.844 1.00 30.11 ?  169  LEU   B HD13 1 
ATOM   6465 H  HD21 . LEU   B 1 169 ? 26.563 -36.614 -13.987 1.00 28.99 ?  169  LEU   B HD21 1 
ATOM   6466 H  HD22 . LEU   B 1 169 ? 27.417 -37.954 -14.025 1.00 28.99 ?  169  LEU   B HD22 1 
ATOM   6467 H  HD23 . LEU   B 1 169 ? 27.166 -37.211 -12.645 1.00 28.99 ?  169  LEU   B HD23 1 
HETATM 6468 N  N2   B A1BAS C 2 .   ? 15.093 1.025   6.425   0.25 16.60 ?  201  A1BAS A N2   1 
HETATM 6469 C  C3   B A1BAS C 2 .   ? 15.463 4.341   5.236   0.25 16.10 ?  201  A1BAS A C3   1 
HETATM 6470 C  C6   B A1BAS C 2 .   ? 14.973 1.050   3.618   0.25 17.79 ?  201  A1BAS A C6   1 
HETATM 6471 C  C9   B A1BAS C 2 .   ? 12.889 -0.564  -0.561  0.25 21.94 ?  201  A1BAS A C9   1 
HETATM 6472 C  C1   B A1BAS C 2 .   ? 15.353 4.392   2.739   0.25 17.10 ?  201  A1BAS A C1   1 
HETATM 6473 C  C10  B A1BAS C 2 .   ? 12.840 1.885   0.025   0.25 21.94 ?  201  A1BAS A C10  1 
HETATM 6474 C  C11  B A1BAS C 2 .   ? 15.158 2.291   4.275   0.25 16.73 ?  201  A1BAS A C11  1 
HETATM 6475 C  C2   B A1BAS C 2 .   ? 15.326 3.685   4.016   0.25 16.65 ?  201  A1BAS A C2   1 
HETATM 6476 C  C4   B A1BAS C 2 .   ? 15.207 2.175   5.699   0.25 16.32 ?  201  A1BAS A C4   1 
HETATM 6477 C  C5   B A1BAS C 2 .   ? 14.924 -0.057  5.673   0.25 16.98 ?  201  A1BAS A C5   1 
HETATM 6478 C  C7   B A1BAS C 2 .   ? 14.001 0.166   1.535   0.25 20.88 ?  201  A1BAS A C7   1 
HETATM 6479 C  C8   B A1BAS C 2 .   ? 13.671 0.571   0.092   0.25 21.84 ?  201  A1BAS A C8   1 
HETATM 6480 N  N1   B A1BAS C 2 .   ? 15.389 3.411   6.267   0.25 16.16 ?  201  A1BAS A N1   1 
HETATM 6481 N  N3   B A1BAS C 2 .   ? 14.855 -0.128  4.311   0.25 17.66 ?  201  A1BAS A N3   1 
HETATM 6482 N  N4   B A1BAS C 2 .   ? 14.909 0.992   2.259   0.25 19.33 ?  201  A1BAS A N4   1 
HETATM 6483 O  O1   B A1BAS C 2 .   ? 14.906 0.746   -0.516  0.25 22.54 ?  201  A1BAS A O1   1 
HETATM 6484 H  H4   B A1BAS C 2 .   ? 15.604 5.371   5.519   0.25 19.31 ?  201  A1BAS A H4   1 
HETATM 6485 H  H12  B A1BAS C 2 .   ? 12.663 -0.388  -1.608  0.25 26.32 ?  201  A1BAS A H12  1 
HETATM 6486 H  H10  B A1BAS C 2 .   ? 11.919 -0.750  -0.076  0.25 26.32 ?  201  A1BAS A H10  1 
HETATM 6487 H  H11  B A1BAS C 2 .   ? 13.429 -1.519  -0.506  0.25 26.32 ?  201  A1BAS A H11  1 
HETATM 6488 H  H1   B A1BAS C 2 .   ? 15.612 3.723   1.898   0.25 20.52 ?  201  A1BAS A H1   1 
HETATM 6489 H  H2   B A1BAS C 2 .   ? 16.112 5.168   2.750   0.25 20.52 ?  201  A1BAS A H2   1 
HETATM 6490 H  H3   B A1BAS C 2 .   ? 14.403 4.860   2.459   0.25 20.52 ?  201  A1BAS A H3   1 
HETATM 6491 H  H15  B A1BAS C 2 .   ? 12.292 2.001   -0.921  0.25 26.32 ?  201  A1BAS A H15  1 
HETATM 6492 H  H13  B A1BAS C 2 .   ? 13.468 2.782   0.110   0.25 26.32 ?  201  A1BAS A H13  1 
HETATM 6493 H  H14  B A1BAS C 2 .   ? 12.076 1.967   0.813   0.25 26.32 ?  201  A1BAS A H14  1 
HETATM 6494 H  H6   B A1BAS C 2 .   ? 14.830 -0.981  6.280   0.25 20.37 ?  201  A1BAS A H6   1 
HETATM 6495 H  H8   B A1BAS C 2 .   ? 14.286 -0.909  1.578   0.25 25.05 ?  201  A1BAS A H8   1 
HETATM 6496 H  H9   B A1BAS C 2 .   ? 13.074 0.242   2.108   0.25 25.05 ?  201  A1BAS A H9   1 
HETATM 6497 H  H5   B A1BAS C 2 .   ? 15.457 3.579   7.256   0.25 19.38 ?  201  A1BAS A H5   1 
HETATM 6498 H  H7   B A1BAS C 2 .   ? 15.538 1.574   1.746   0.25 23.18 ?  201  A1BAS A H7   1 
HETATM 6499 H  H16  B A1BAS C 2 .   ? 15.384 1.415   -0.032  0.25 27.04 ?  201  A1BAS A H16  1 
HETATM 6500 N  N2   C A1BAS D 2 .   ? 15.215 1.024   6.482   0.25 13.41 ?  202  A1BAS A N2   1 
HETATM 6501 C  C3   C A1BAS D 2 .   ? 15.536 4.266   5.070   0.25 12.17 ?  202  A1BAS A C3   1 
HETATM 6502 C  C6   C A1BAS D 2 .   ? 14.673 0.923   3.684   0.25 14.53 ?  202  A1BAS A C6   1 
HETATM 6503 C  C9   C A1BAS D 2 .   ? 13.445 -2.044  -0.226  0.25 18.91 ?  202  A1BAS A C9   1 
HETATM 6504 C  C1   C A1BAS D 2 .   ? 15.074 4.252   2.609   0.25 12.78 ?  202  A1BAS A C1   1 
HETATM 6505 C  C10  C A1BAS D 2 .   ? 12.931 0.395   -0.331  0.25 18.84 ?  202  A1BAS A C10  1 
HETATM 6506 C  C11  C A1BAS D 2 .   ? 15.009 2.187   4.256   0.25 12.95 ?  202  A1BAS A C11  1 
HETATM 6507 C  C2   C A1BAS D 2 .   ? 15.192 3.574   3.909   0.25 12.73 ?  202  A1BAS A C2   1 
HETATM 6508 C  C4   C A1BAS D 2 .   ? 15.258 2.126   5.666   0.25 12.63 ?  202  A1BAS A C4   1 
HETATM 6509 C  C5   C A1BAS D 2 .   ? 14.889 -0.077  5.803   0.25 14.18 ?  202  A1BAS A C5   1 
HETATM 6510 C  C7   C A1BAS D 2 .   ? 14.178 -0.556  1.724   0.25 18.04 ?  202  A1BAS A C7   1 
HETATM 6511 C  C8   C A1BAS D 2 .   ? 13.953 -0.646  0.177   0.25 18.97 ?  202  A1BAS A C8   1 
HETATM 6512 N  N1   C A1BAS D 2 .   ? 15.570 3.377   6.140   0.25 12.30 ?  202  A1BAS A N1   1 
HETATM 6513 N  N3   C A1BAS D 2 .   ? 14.616 -0.206  4.466   0.25 14.74 ?  202  A1BAS A N3   1 
HETATM 6514 N  N4   C A1BAS D 2 .   ? 14.401 0.759   2.340   0.25 16.42 ?  202  A1BAS A N4   1 
HETATM 6515 O  O1   C A1BAS D 2 .   ? 15.209 -0.402  -0.380  0.25 19.60 ?  202  A1BAS A O1   1 
HETATM 6516 H  H4   C A1BAS D 2 .   ? 15.758 5.304   5.288   0.25 14.60 ?  202  A1BAS A H4   1 
HETATM 6517 H  H12  C A1BAS D 2 .   ? 12.476 -2.297  0.217   0.25 22.69 ?  202  A1BAS A H12  1 
HETATM 6518 H  H10  C A1BAS D 2 .   ? 13.306 -2.155  -1.312  0.25 22.69 ?  202  A1BAS A H10  1 
HETATM 6519 H  H11  C A1BAS D 2 .   ? 14.141 -2.844  0.063   0.25 22.69 ?  202  A1BAS A H11  1 
HETATM 6520 H  H1   C A1BAS D 2 .   ? 14.854 5.330   2.723   0.25 15.34 ?  202  A1BAS A H1   1 
HETATM 6521 H  H2   C A1BAS D 2 .   ? 16.030 4.216   2.063   0.25 15.34 ?  202  A1BAS A H2   1 
HETATM 6522 H  H3   C A1BAS D 2 .   ? 14.298 3.859   1.952   0.25 15.34 ?  202  A1BAS A H3   1 
HETATM 6523 H  H15  C A1BAS D 2 .   ? 13.385 1.379   -0.531  0.25 22.60 ?  202  A1BAS A H15  1 
HETATM 6524 H  H13  C A1BAS D 2 .   ? 12.139 0.585   0.396   0.25 22.60 ?  202  A1BAS A H13  1 
HETATM 6525 H  H14  C A1BAS D 2 .   ? 12.441 0.107   -1.268  0.25 22.60 ?  202  A1BAS A H14  1 
HETATM 6526 H  H6   C A1BAS D 2 .   ? 14.848 -0.966  6.445   0.25 17.01 ?  202  A1BAS A H6   1 
HETATM 6527 H  H8   C A1BAS D 2 .   ? 13.385 -1.120  2.255   0.25 21.64 ?  202  A1BAS A H8   1 
HETATM 6528 H  H9   C A1BAS D 2 .   ? 15.118 -1.127  1.932   0.25 21.64 ?  202  A1BAS A H9   1 
HETATM 6529 H  H5   C A1BAS D 2 .   ? 15.782 3.580   7.102   0.25 14.76 ?  202  A1BAS A H5   1 
HETATM 6530 H  H7   C A1BAS D 2 .   ? 14.360 1.580   1.756   0.25 19.69 ?  202  A1BAS A H7   1 
HETATM 6531 H  H16  C A1BAS D 2 .   ? 15.155 -0.553  -1.324  0.25 23.51 ?  202  A1BAS A H16  1 
HETATM 6532 CL CL   B CL    E 3 .   ? 15.975 2.737   -1.202  0.50 18.68 ?  203  CL    A CL   1 
HETATM 6533 O  O    . HOH   F 4 .   ? 11.612 -10.754 -10.084 1.00 42.51 ?  1301 HOH   A O    1 
HETATM 6534 O  O    . HOH   F 4 .   ? 18.557 -2.419  -16.383 1.00 46.62 ?  1302 HOH   A O    1 
HETATM 6535 O  O    A HOH   F 4 .   ? 4.650  3.882   0.678   0.50 21.64 ?  1303 HOH   A O    1 
HETATM 6536 O  O    . HOH   F 4 .   ? 6.911  -8.232  11.846  1.00 23.77 ?  1304 HOH   A O    1 
HETATM 6537 O  O    A HOH   F 4 .   ? 15.230 -12.343 18.609  0.50 22.33 ?  1305 HOH   A O    1 
HETATM 6538 O  O    . HOH   F 4 .   ? 24.551 1.981   -6.980  1.00 20.15 ?  1306 HOH   A O    1 
HETATM 6539 O  O    . HOH   F 4 .   ? 34.372 -1.866  12.518  1.00 39.00 ?  1307 HOH   A O    1 
HETATM 6540 O  O    . HOH   F 4 .   ? 7.964  -12.631 -0.849  1.00 23.59 ?  1308 HOH   A O    1 
HETATM 6541 O  O    . HOH   F 4 .   ? 18.927 -22.001 6.922   1.00 34.87 ?  1309 HOH   A O    1 
HETATM 6542 O  O    . HOH   F 4 .   ? 28.510 -10.631 -13.998 1.00 41.83 ?  1310 HOH   A O    1 
HETATM 6543 O  O    . HOH   F 4 .   ? 14.802 3.540   17.736  1.00 39.37 ?  1311 HOH   A O    1 
HETATM 6544 O  O    . HOH   F 4 .   ? 28.888 0.458   -9.668  1.00 22.50 ?  1312 HOH   A O    1 
HETATM 6545 O  O    A HOH   F 4 .   ? 14.771 -4.666  20.456  0.50 31.45 ?  1313 HOH   A O    1 
HETATM 6546 O  O    . HOH   F 4 .   ? 15.858 2.046   24.801  1.00 45.46 ?  1314 HOH   A O    1 
HETATM 6547 O  O    . HOH   F 4 .   ? 42.367 10.520  5.170   1.00 20.62 ?  1315 HOH   A O    1 
HETATM 6548 O  O    . HOH   F 4 .   ? 28.296 -0.189  -13.342 1.00 36.54 ?  1316 HOH   A O    1 
HETATM 6549 O  O    . HOH   F 4 .   ? 30.215 -13.285 -8.494  1.00 21.92 ?  1317 HOH   A O    1 
HETATM 6550 O  O    . HOH   F 4 .   ? 19.908 -12.536 -8.901  1.00 27.87 ?  1318 HOH   A O    1 
HETATM 6551 O  O    . HOH   F 4 .   ? 36.122 -5.072  -0.521  1.00 28.62 ?  1319 HOH   A O    1 
HETATM 6552 O  O    . HOH   F 4 .   ? 14.711 -14.003 16.688  1.00 25.22 ?  1320 HOH   A O    1 
HETATM 6553 O  O    . HOH   F 4 .   ? 0.750  -4.668  0.136   1.00 34.03 ?  1321 HOH   A O    1 
HETATM 6554 O  O    A HOH   F 4 .   ? 12.265 0.195   14.915  0.50 25.86 ?  1322 HOH   A O    1 
HETATM 6555 O  O    . HOH   F 4 .   ? 8.010  -21.481 4.016   1.00 47.25 ?  1323 HOH   A O    1 
HETATM 6556 O  O    . HOH   F 4 .   ? 9.027  -10.221 19.320  1.00 45.84 ?  1324 HOH   A O    1 
HETATM 6557 O  O    . HOH   F 4 .   ? 31.026 -18.129 7.831   1.00 20.07 ?  1325 HOH   A O    1 
HETATM 6558 O  O    . HOH   F 4 .   ? 26.470 -19.318 -1.800  1.00 14.76 ?  1326 HOH   A O    1 
HETATM 6559 O  O    . HOH   F 4 .   ? 18.675 -19.385 13.543  1.00 35.53 ?  1327 HOH   A O    1 
HETATM 6560 O  O    . HOH   F 4 .   ? 27.247 13.720  2.915   1.00 28.34 ?  1328 HOH   A O    1 
HETATM 6561 O  O    . HOH   F 4 .   ? 17.016 -19.309 4.901   1.00 16.88 ?  1329 HOH   A O    1 
HETATM 6562 O  O    B HOH   F 4 .   ? 22.523 5.410   -1.665  0.50 27.10 ?  1330 HOH   A O    1 
HETATM 6563 O  O    . HOH   F 4 .   ? 20.613 -19.720 -5.055  1.00 29.89 ?  1331 HOH   A O    1 
HETATM 6564 O  O    . HOH   F 4 .   ? 37.501 2.791   10.242  1.00 29.42 ?  1332 HOH   A O    1 
HETATM 6565 O  O    B HOH   F 4 .   ? 21.244 -2.251  -2.516  0.50 17.83 ?  1333 HOH   A O    1 
HETATM 6566 O  O    . HOH   F 4 .   ? 33.957 -0.997  -8.914  1.00 27.81 ?  1334 HOH   A O    1 
HETATM 6567 O  O    . HOH   F 4 .   ? 13.942 -4.999  17.439  1.00 27.97 ?  1335 HOH   A O    1 
HETATM 6568 O  O    . HOH   F 4 .   ? 44.258 7.159   6.398   1.00 27.69 ?  1336 HOH   A O    1 
HETATM 6569 O  O    . HOH   F 4 .   ? 14.096 -4.541  -11.868 1.00 32.76 ?  1337 HOH   A O    1 
HETATM 6570 O  O    . HOH   F 4 .   ? 3.534  -9.493  9.951   1.00 37.84 ?  1338 HOH   A O    1 
HETATM 6571 O  O    . HOH   F 4 .   ? 38.508 4.975   6.997   1.00 15.72 ?  1339 HOH   A O    1 
HETATM 6572 O  O    . HOH   F 4 .   ? 38.208 10.098  7.182   1.00 43.93 ?  1340 HOH   A O    1 
HETATM 6573 O  O    . HOH   F 4 .   ? 26.786 11.367  1.687   1.00 16.58 ?  1341 HOH   A O    1 
HETATM 6574 O  O    A HOH   F 4 .   ? 14.602 -3.684  3.135   0.50 17.62 ?  1342 HOH   A O    1 
HETATM 6575 O  O    A HOH   F 4 .   ? 14.241 0.536   6.847   0.50 25.20 ?  1343 HOH   A O    1 
HETATM 6576 O  O    . HOH   F 4 .   ? 18.505 9.349   9.030   1.00 23.86 ?  1344 HOH   A O    1 
HETATM 6577 O  O    . HOH   F 4 .   ? 22.262 -19.302 11.346  1.00 36.25 ?  1345 HOH   A O    1 
HETATM 6578 O  O    . HOH   F 4 .   ? 22.272 5.236   18.991  1.00 46.93 ?  1346 HOH   A O    1 
HETATM 6579 O  O    . HOH   F 4 .   ? 28.250 -6.248  19.605  1.00 44.86 ?  1347 HOH   A O    1 
HETATM 6580 O  O    . HOH   F 4 .   ? 25.673 -0.812  -7.320  1.00 15.59 ?  1348 HOH   A O    1 
HETATM 6581 O  O    . HOH   F 4 .   ? 39.699 -1.014  -5.184  1.00 20.36 ?  1349 HOH   A O    1 
HETATM 6582 O  O    . HOH   F 4 .   ? 35.764 -12.690 6.825   1.00 16.21 ?  1350 HOH   A O    1 
HETATM 6583 O  O    . HOH   F 4 .   ? 8.798  -12.117 17.189  1.00 40.26 ?  1351 HOH   A O    1 
HETATM 6584 O  O    B HOH   F 4 .   ? 21.156 2.623   0.007   0.50 14.54 ?  1352 HOH   A O    1 
HETATM 6585 O  O    A HOH   F 4 .   ? 17.459 -1.734  0.482   0.50 18.31 ?  1353 HOH   A O    1 
HETATM 6586 O  O    . HOH   F 4 .   ? 7.650  -6.348  -6.548  1.00 42.73 ?  1354 HOH   A O    1 
HETATM 6587 O  O    . HOH   F 4 .   ? 43.293 7.806   2.718   1.00 25.43 ?  1355 HOH   A O    1 
HETATM 6588 O  O    . HOH   F 4 .   ? 24.006 -2.134  -2.072  1.00 10.86 ?  1356 HOH   A O    1 
HETATM 6589 O  O    . HOH   F 4 .   ? 31.648 8.183   14.851  1.00 23.56 ?  1357 HOH   A O    1 
HETATM 6590 O  O    . HOH   F 4 .   ? 42.467 4.269   5.307   1.00 31.76 ?  1358 HOH   A O    1 
HETATM 6591 O  O    B HOH   F 4 .   ? 15.096 -2.743  3.456   0.50 19.49 ?  1359 HOH   A O    1 
HETATM 6592 O  O    . HOH   F 4 .   ? 21.791 -13.849 -8.119  1.00 39.06 ?  1360 HOH   A O    1 
HETATM 6593 O  O    . HOH   F 4 .   ? 37.155 -2.902  9.720   1.00 42.87 ?  1361 HOH   A O    1 
HETATM 6594 O  O    . HOH   F 4 .   ? 31.791 -9.347  -6.675  1.00 23.05 ?  1362 HOH   A O    1 
HETATM 6595 O  O    . HOH   F 4 .   ? 30.764 3.048   8.291   1.00 12.09 ?  1363 HOH   A O    1 
HETATM 6596 O  O    . HOH   F 4 .   ? 14.355 -21.200 -4.294  1.00 31.18 ?  1364 HOH   A O    1 
HETATM 6597 O  O    . HOH   F 4 .   ? 23.399 11.319  4.147   1.00 12.91 ?  1365 HOH   A O    1 
HETATM 6598 O  O    . HOH   F 4 .   ? 31.058 -13.933 -2.467  1.00 14.40 ?  1366 HOH   A O    1 
HETATM 6599 O  O    . HOH   F 4 .   ? 33.648 -7.183  4.292   1.00 16.95 ?  1367 HOH   A O    1 
HETATM 6600 O  O    . HOH   F 4 .   ? 13.578 -15.242 -7.433  1.00 25.79 ?  1368 HOH   A O    1 
HETATM 6601 O  O    . HOH   F 4 .   ? 37.273 11.925  4.918   1.00 34.25 ?  1369 HOH   A O    1 
HETATM 6602 O  O    . HOH   F 4 .   ? 9.820  -21.393 5.751   1.00 19.37 ?  1370 HOH   A O    1 
HETATM 6603 O  O    . HOH   F 4 .   ? 17.161 -17.836 -5.078  1.00 28.68 ?  1371 HOH   A O    1 
HETATM 6604 O  O    . HOH   F 4 .   ? 14.401 -24.699 11.644  1.00 34.94 ?  1372 HOH   A O    1 
HETATM 6605 O  O    . HOH   F 4 .   ? 27.503 -10.658 14.064  1.00 18.16 ?  1373 HOH   A O    1 
HETATM 6606 O  O    A HOH   F 4 .   ? 18.918 -0.683  -1.585  0.50 11.06 ?  1374 HOH   A O    1 
HETATM 6607 O  O    . HOH   F 4 .   ? 14.069 -23.075 7.440   1.00 19.76 ?  1375 HOH   A O    1 
HETATM 6608 O  O    . HOH   F 4 .   ? 19.613 -11.054 24.062  1.00 65.35 ?  1376 HOH   A O    1 
HETATM 6609 O  O    . HOH   F 4 .   ? 21.859 -21.933 8.348   1.00 30.57 ?  1377 HOH   A O    1 
HETATM 6610 O  O    A HOH   F 4 .   ? 13.265 -1.446  -6.480  0.50 14.44 ?  1378 HOH   A O    1 
HETATM 6611 O  O    . HOH   F 4 .   ? 24.351 3.540   -1.780  1.00 14.71 ?  1379 HOH   A O    1 
HETATM 6612 O  O    . HOH   F 4 .   ? 43.875 8.472   -3.082  1.00 25.42 ?  1380 HOH   A O    1 
HETATM 6613 O  O    . HOH   F 4 .   ? 22.708 12.454  1.671   1.00 15.68 ?  1381 HOH   A O    1 
HETATM 6614 O  O    . HOH   F 4 .   ? 15.170 -8.024  -9.749  1.00 23.44 ?  1382 HOH   A O    1 
HETATM 6615 O  O    . HOH   F 4 .   ? 20.061 4.524   -7.461  1.00 20.16 ?  1383 HOH   A O    1 
HETATM 6616 O  O    A HOH   F 4 .   ? 21.208 -2.407  -2.016  0.50 11.34 ?  1384 HOH   A O    1 
HETATM 6617 O  O    . HOH   F 4 .   ? 27.439 -6.170  -13.988 1.00 39.29 ?  1385 HOH   A O    1 
HETATM 6618 O  O    . HOH   F 4 .   ? 31.741 -7.279  -9.830  1.00 21.72 ?  1386 HOH   A O    1 
HETATM 6619 O  O    . HOH   F 4 .   ? 24.689 -17.567 12.756  1.00 25.91 ?  1387 HOH   A O    1 
HETATM 6620 O  O    . HOH   F 4 .   ? 11.091 -0.493  2.235   1.00 47.05 ?  1388 HOH   A O    1 
HETATM 6621 O  O    . HOH   F 4 .   ? 16.481 -22.049 1.027   1.00 29.46 ?  1389 HOH   A O    1 
HETATM 6622 O  O    . HOH   F 4 .   ? 24.291 -7.845  14.467  1.00 18.47 ?  1390 HOH   A O    1 
HETATM 6623 O  O    B HOH   F 4 .   ? 12.022 6.733   10.658  0.50 31.98 ?  1391 HOH   A O    1 
HETATM 6624 O  O    . HOH   F 4 .   ? 21.192 10.181  15.099  1.00 37.22 ?  1392 HOH   A O    1 
HETATM 6625 O  O    . HOH   F 4 .   ? 6.639  -3.455  12.806  1.00 32.10 ?  1393 HOH   A O    1 
HETATM 6626 O  O    B HOH   F 4 .   ? 14.748 7.155   7.445   0.50 21.62 ?  1394 HOH   A O    1 
HETATM 6627 O  O    . HOH   F 4 .   ? 37.516 -2.091  5.780   1.00 27.47 ?  1395 HOH   A O    1 
HETATM 6628 O  O    . HOH   F 4 .   ? 23.919 -15.652 -9.161  1.00 34.82 ?  1396 HOH   A O    1 
HETATM 6629 O  O    . HOH   F 4 .   ? 16.286 -14.233 20.272  1.00 47.79 ?  1397 HOH   A O    1 
HETATM 6630 O  O    . HOH   F 4 .   ? 32.782 -9.260  5.963   1.00 20.73 ?  1398 HOH   A O    1 
HETATM 6631 O  O    . HOH   F 4 .   ? 27.859 0.824   -7.102  1.00 14.23 ?  1399 HOH   A O    1 
HETATM 6632 O  O    . HOH   F 4 .   ? 23.985 3.877   -4.791  1.00 24.90 ?  1400 HOH   A O    1 
HETATM 6633 O  O    . HOH   F 4 .   ? 30.088 -10.181 12.990  1.00 22.31 ?  1401 HOH   A O    1 
HETATM 6634 O  O    . HOH   F 4 .   ? 30.689 1.805   16.691  1.00 22.23 ?  1402 HOH   A O    1 
HETATM 6635 O  O    . HOH   F 4 .   ? 27.323 2.285   18.741  1.00 30.51 ?  1403 HOH   A O    1 
HETATM 6636 O  O    B HOH   F 4 .   ? 13.309 -1.399  -7.111  0.50 17.28 ?  1404 HOH   A O    1 
HETATM 6637 O  O    . HOH   F 4 .   ? 15.464 11.831  7.870   1.00 33.36 ?  1405 HOH   A O    1 
HETATM 6638 O  O    . HOH   F 4 .   ? 10.404 -22.106 -1.269  1.00 52.06 ?  1406 HOH   A O    1 
HETATM 6639 O  O    A HOH   F 4 .   ? 11.005 1.498   12.803  0.50 20.05 ?  1407 HOH   A O    1 
HETATM 6640 O  O    . HOH   F 4 .   ? 6.437  -5.693  11.139  1.00 23.23 ?  1408 HOH   A O    1 
HETATM 6641 O  O    . HOH   F 4 .   ? 20.560 -20.033 2.750   1.00 19.63 ?  1409 HOH   A O    1 
HETATM 6642 O  O    . HOH   F 4 .   ? 23.937 -20.259 -1.389  1.00 17.24 ?  1410 HOH   A O    1 
HETATM 6643 O  O    . HOH   F 4 .   ? 30.350 -12.992 13.453  1.00 20.95 ?  1411 HOH   A O    1 
HETATM 6644 O  O    . HOH   F 4 .   ? 41.579 1.527   4.930   1.00 36.63 ?  1412 HOH   A O    1 
HETATM 6645 O  O    . HOH   F 4 .   ? 26.889 4.116   -0.623  1.00 12.76 ?  1413 HOH   A O    1 
HETATM 6646 O  O    . HOH   F 4 .   ? 37.987 -1.305  -1.954  1.00 20.00 ?  1414 HOH   A O    1 
HETATM 6647 O  O    . HOH   F 4 .   ? 40.862 -8.274  -6.771  1.00 36.40 ?  1415 HOH   A O    1 
HETATM 6648 O  O    A HOH   F 4 .   ? 15.196 -21.652 14.161  0.50 14.29 ?  1416 HOH   A O    1 
HETATM 6649 O  O    A HOH   F 4 .   ? 21.304 3.141   -0.302  0.50 9.12  ?  1417 HOH   A O    1 
HETATM 6650 O  O    A HOH   F 4 .   ? -0.661 -8.541  2.443   0.50 31.02 ?  1418 HOH   A O    1 
HETATM 6651 O  O    A HOH   F 4 .   ? 22.727 -12.110 21.888  0.50 27.49 ?  1419 HOH   A O    1 
HETATM 6652 O  O    A HOH   F 4 .   ? -0.511 -3.138  3.151   0.50 30.15 ?  1420 HOH   A O    1 
HETATM 6653 O  O    B HOH   F 4 .   ? 18.448 -1.544  -1.456  0.50 33.24 ?  1421 HOH   A O    1 
HETATM 6654 O  O    B HOH   F 4 .   ? 11.812 -2.027  -3.566  0.50 15.53 ?  1422 HOH   A O    1 
HETATM 6655 O  O    . HOH   F 4 .   ? 32.508 -10.625 3.195   1.00 32.54 ?  1423 HOH   A O    1 
HETATM 6656 O  O    . HOH   F 4 .   ? 35.062 -5.215  -3.100  1.00 18.02 ?  1424 HOH   A O    1 
HETATM 6657 O  O    A HOH   F 4 .   ? 5.265  2.592   5.331   0.50 27.75 ?  1425 HOH   A O    1 
HETATM 6658 O  O    A HOH   F 4 .   ? 17.104 -18.150 15.069  0.50 18.52 ?  1426 HOH   A O    1 
HETATM 6659 O  O    . HOH   F 4 .   ? 14.492 -0.539  -12.111 1.00 24.23 ?  1427 HOH   A O    1 
HETATM 6660 O  O    A HOH   F 4 .   ? 15.766 -0.978  5.313   0.50 29.61 ?  1428 HOH   A O    1 
HETATM 6661 O  O    . HOH   F 4 .   ? 16.222 16.672  8.727   1.00 32.28 ?  1429 HOH   A O    1 
HETATM 6662 O  O    . HOH   F 4 .   ? 36.698 -4.985  5.403   1.00 25.50 ?  1430 HOH   A O    1 
HETATM 6663 O  O    . HOH   F 4 .   ? 30.829 6.240   -12.250 1.00 29.72 ?  1431 HOH   A O    1 
HETATM 6664 O  O    . HOH   F 4 .   ? 10.406 -13.741 -1.686  1.00 18.36 ?  1432 HOH   A O    1 
HETATM 6665 O  O    B HOH   F 4 .   ? 16.353 7.604   2.854   0.50 33.12 ?  1433 HOH   A O    1 
HETATM 6666 O  O    . HOH   F 4 .   ? 32.650 -4.314  -9.897  1.00 28.35 ?  1434 HOH   A O    1 
HETATM 6667 O  O    . HOH   F 4 .   ? 18.548 4.949   -15.063 1.00 49.95 ?  1435 HOH   A O    1 
HETATM 6668 O  O    . HOH   F 4 .   ? 27.125 -3.325  19.323  1.00 36.07 ?  1436 HOH   A O    1 
HETATM 6669 O  O    . HOH   F 4 .   ? 44.948 -0.580  2.959   1.00 43.50 ?  1437 HOH   A O    1 
HETATM 6670 O  O    B HOH   F 4 .   ? 10.934 2.289   12.290  0.50 30.71 ?  1438 HOH   A O    1 
HETATM 6671 O  O    A HOH   F 4 .   ? 18.820 2.017   -0.704  0.50 10.95 ?  1439 HOH   A O    1 
HETATM 6672 O  O    . HOH   F 4 .   ? 37.710 -8.826  -3.529  1.00 26.17 ?  1440 HOH   A O    1 
HETATM 6673 O  O    . HOH   F 4 .   ? 22.612 8.062   18.452  1.00 45.99 ?  1441 HOH   A O    1 
HETATM 6674 O  O    . HOH   F 4 .   ? 23.589 -8.081  17.042  1.00 23.22 ?  1442 HOH   A O    1 
HETATM 6675 O  O    A HOH   F 4 .   ? 11.710 -10.830 16.992  0.50 19.34 ?  1443 HOH   A O    1 
HETATM 6676 O  O    A HOH   F 4 .   ? 15.972 6.927   3.050   0.50 13.29 ?  1444 HOH   A O    1 
HETATM 6677 O  O    A HOH   F 4 .   ? 16.214 2.930   -1.390  0.50 25.07 ?  1445 HOH   A O    1 
HETATM 6678 O  O    . HOH   F 4 .   ? 23.348 -20.955 1.264   1.00 19.31 ?  1446 HOH   A O    1 
HETATM 6679 O  O    . HOH   F 4 .   ? 18.439 -16.048 16.390  1.00 37.29 ?  1447 HOH   A O    1 
HETATM 6680 O  O    . HOH   F 4 .   ? 20.543 -17.760 24.857  1.00 50.67 ?  1448 HOH   A O    1 
HETATM 6681 O  O    . HOH   F 4 .   ? 34.398 -8.084  -0.529  1.00 30.40 ?  1449 HOH   A O    1 
HETATM 6682 O  O    . HOH   F 4 .   ? 21.531 -14.817 18.066  1.00 48.76 ?  1450 HOH   A O    1 
HETATM 6683 O  O    B HOH   F 4 .   ? 7.311  1.555   7.387   0.50 34.09 ?  1451 HOH   A O    1 
HETATM 6684 O  O    . HOH   F 4 .   ? 30.538 14.728  2.829   1.00 19.35 ?  1452 HOH   A O    1 
HETATM 6685 O  O    . HOH   F 4 .   ? -1.489 -4.937  7.735   1.00 52.14 ?  1453 HOH   A O    1 
HETATM 6686 O  O    . HOH   F 4 .   ? 31.323 -12.785 0.026   1.00 19.63 ?  1454 HOH   A O    1 
HETATM 6687 O  O    . HOH   F 4 .   ? 27.671 6.957   -6.331  1.00 33.31 ?  1455 HOH   A O    1 
HETATM 6688 O  O    . HOH   F 4 .   ? 23.217 7.630   -3.199  1.00 27.55 ?  1456 HOH   A O    1 
HETATM 6689 O  O    . HOH   F 4 .   ? 9.419  -16.228 -1.990  1.00 40.89 ?  1457 HOH   A O    1 
HETATM 6690 O  O    A HOH   F 4 .   ? 13.991 -0.369  3.507   0.50 30.43 ?  1458 HOH   A O    1 
HETATM 6691 O  O    . HOH   F 4 .   ? 29.831 -16.088 10.665  1.00 36.25 ?  1459 HOH   A O    1 
HETATM 6692 O  O    . HOH   F 4 .   ? 29.837 -1.974  -12.682 1.00 50.17 ?  1460 HOH   A O    1 
HETATM 6693 O  O    . HOH   F 4 .   ? 21.498 -9.087  21.432  1.00 46.86 ?  1461 HOH   A O    1 
HETATM 6694 O  O    B HOH   F 4 .   ? 10.333 -0.022  -2.026  0.50 36.52 ?  1462 HOH   A O    1 
HETATM 6695 O  O    . HOH   F 4 .   ? 25.397 8.240   -4.775  1.00 23.59 ?  1463 HOH   A O    1 
HETATM 6696 O  O    B HOH   F 4 .   ? 18.577 1.304   -0.373  0.50 19.08 ?  1464 HOH   A O    1 
HETATM 6697 O  O    . HOH   F 4 .   ? 32.437 -15.983 10.794  1.00 38.19 ?  1465 HOH   A O    1 
HETATM 6698 O  O    . HOH   F 4 .   ? 19.905 -17.325 -5.074  1.00 24.83 ?  1466 HOH   A O    1 
HETATM 6699 O  O    . HOH   F 4 .   ? 24.909 5.582   20.776  1.00 52.39 ?  1467 HOH   A O    1 
HETATM 6700 O  O    B HOH   F 4 .   ? 11.038 0.864   14.641  0.50 35.60 ?  1468 HOH   A O    1 
HETATM 6701 O  O    . HOH   F 4 .   ? 24.586 14.483  7.833   1.00 33.95 ?  1469 HOH   A O    1 
HETATM 6702 O  O    . HOH   F 4 .   ? 23.310 -12.880 19.331  1.00 46.72 ?  1470 HOH   A O    1 
HETATM 6703 O  O    . HOH   F 4 .   ? 23.214 -22.378 -3.318  1.00 35.70 ?  1471 HOH   A O    1 
HETATM 6704 O  O    . HOH   F 4 .   ? 21.881 5.151   -5.795  1.00 31.67 ?  1472 HOH   A O    1 
HETATM 6705 O  O    B HOH   F 4 .   ? 5.482  3.798   0.587   0.50 30.05 ?  1473 HOH   A O    1 
HETATM 6706 O  O    . HOH   F 4 .   ? 27.572 -11.398 16.563  1.00 37.65 ?  1474 HOH   A O    1 
HETATM 6707 O  O    . HOH   F 4 .   ? 18.755 10.766  11.332  1.00 32.94 ?  1475 HOH   A O    1 
HETATM 6708 O  O    . HOH   F 4 .   ? 15.707 -21.508 3.681   1.00 24.35 ?  1476 HOH   A O    1 
HETATM 6709 O  O    . HOH   F 4 .   ? 26.863 11.588  -1.241  1.00 29.59 ?  1477 HOH   A O    1 
HETATM 6710 O  O    . HOH   F 4 .   ? 39.618 -7.017  -3.481  1.00 45.47 ?  1478 HOH   A O    1 
HETATM 6711 O  O    . HOH   F 4 .   ? 12.279 1.549   17.298  1.00 39.81 ?  1479 HOH   A O    1 
HETATM 6712 O  O    . HOH   F 4 .   ? 23.412 13.637  5.558   1.00 19.78 ?  1480 HOH   A O    1 
HETATM 6713 O  O    . HOH   F 4 .   ? 25.832 10.760  -3.641  1.00 24.70 ?  1481 HOH   A O    1 
HETATM 6714 O  O    B HOH   F 4 .   ? 6.480  4.192   4.526   0.50 20.70 ?  1482 HOH   A O    1 
HETATM 6715 O  O    . HOH   F 4 .   ? 11.020 -14.995 -6.091  1.00 33.52 ?  1483 HOH   A O    1 
HETATM 6716 O  O    A HOH   F 4 .   ? 11.945 -13.430 16.322  0.50 28.73 ?  1484 HOH   A O    1 
HETATM 6717 O  O    . HOH   F 4 .   ? 16.868 -20.592 16.098  1.00 29.83 ?  1485 HOH   A O    1 
HETATM 6718 O  O    . HOH   F 4 .   ? 35.109 7.405   12.252  1.00 47.91 ?  1486 HOH   A O    1 
HETATM 6719 O  O    B HOH   F 4 .   ? 10.609 -1.870  -6.015  0.50 25.74 ?  1487 HOH   A O    1 
HETATM 6720 O  O    . HOH   F 4 .   ? 8.070  -3.037  -5.706  1.00 54.73 ?  1488 HOH   A O    1 
HETATM 6721 O  O    . HOH   F 4 .   ? 28.809 8.947   17.522  1.00 36.59 ?  1489 HOH   A O    1 
HETATM 6722 O  O    . HOH   F 4 .   ? 17.350 -18.668 19.822  1.00 48.93 ?  1490 HOH   A O    1 
HETATM 6723 O  O    . HOH   F 4 .   ? 28.557 -4.687  -12.246 1.00 38.36 ?  1491 HOH   A O    1 
HETATM 6724 O  O    . HOH   F 4 .   ? 30.791 0.674   19.171  1.00 40.82 ?  1492 HOH   A O    1 
HETATM 6725 O  O    . HOH   F 4 .   ? 40.984 -3.968  -0.375  1.00 38.92 ?  1493 HOH   A O    1 
HETATM 6726 O  O    . HOH   F 4 .   ? 18.078 -16.318 -8.750  1.00 40.72 ?  1494 HOH   A O    1 
HETATM 6727 O  O    . HOH   F 4 .   ? 15.682 -17.183 -6.967  1.00 32.01 ?  1495 HOH   A O    1 
HETATM 6728 O  O    . HOH   F 4 .   ? 23.126 11.808  -4.021  1.00 20.79 ?  1496 HOH   A O    1 
HETATM 6729 O  O    . HOH   F 4 .   ? 14.017 -10.283 -10.889 1.00 32.29 ?  1497 HOH   A O    1 
HETATM 6730 O  O    . HOH   F 4 .   ? 41.645 9.359   -4.032  1.00 31.70 ?  1498 HOH   A O    1 
HETATM 6731 O  O    . HOH   F 4 .   ? 44.396 10.464  -1.623  1.00 35.52 ?  1499 HOH   A O    1 
HETATM 6732 O  O    . HOH   F 4 .   ? 16.166 -23.350 5.759   1.00 31.58 ?  1500 HOH   A O    1 
HETATM 6733 O  O    . HOH   F 4 .   ? 16.021 -6.624  -11.904 1.00 44.11 ?  1501 HOH   A O    1 
HETATM 6734 O  O    . HOH   F 4 .   ? 39.135 2.398   7.567   1.00 32.12 ?  1502 HOH   A O    1 
HETATM 6735 O  O    . HOH   F 4 .   ? 31.462 -0.578  -10.522 1.00 26.31 ?  1503 HOH   A O    1 
HETATM 6736 O  O    . HOH   F 4 .   ? 28.676 -7.933  -15.225 1.00 48.05 ?  1504 HOH   A O    1 
HETATM 6737 O  O    . HOH   F 4 .   ? 40.447 -0.263  -7.790  1.00 33.69 ?  1505 HOH   A O    1 
HETATM 6738 O  O    . HOH   F 4 .   ? 20.058 -22.365 4.116   1.00 31.74 ?  1506 HOH   A O    1 
HETATM 6739 O  O    . HOH   F 4 .   ? 18.511 -23.257 1.894   1.00 44.20 ?  1507 HOH   A O    1 
HETATM 6740 O  O    . HOH   F 4 .   ? 14.024 -25.347 8.905   1.00 32.91 ?  1508 HOH   A O    1 
HETATM 6741 O  O    B HOH   F 4 .   ? 10.361 4.446   12.167  0.50 31.89 ?  1509 HOH   A O    1 
HETATM 6742 O  O    B HOH   F 4 .   ? 14.581 7.609   4.656   0.50 30.29 ?  1510 HOH   A O    1 
HETATM 6743 O  O    . HOH   F 4 .   ? 30.701 -5.817  -11.805 1.00 52.31 ?  1511 HOH   A O    1 
HETATM 6744 O  O    . HOH   F 4 .   ? 37.395 -6.629  7.564   1.00 25.33 ?  1512 HOH   A O    1 
HETATM 6745 O  O    . HOH   F 4 .   ? 30.669 5.867   -14.630 1.00 38.82 ?  1513 HOH   A O    1 
HETATM 6746 O  O    . HOH   F 4 .   ? 23.106 -23.767 1.596   1.00 32.51 ?  1514 HOH   A O    1 
HETATM 6747 O  O    . HOH   F 4 .   ? 28.907 14.323  0.965   1.00 49.91 ?  1515 HOH   A O    1 
HETATM 6748 O  O    . HOH   F 4 .   ? 39.530 0.002   6.602   1.00 30.19 ?  1516 HOH   A O    1 
HETATM 6749 O  O    . HOH   F 4 .   ? 37.959 13.893  6.721   1.00 49.12 ?  1517 HOH   A O    1 
HETATM 6750 O  O    . HOH   F 4 .   ? 20.476 -16.044 -7.360  1.00 28.74 ?  1518 HOH   A O    1 
HETATM 6751 O  O    . HOH   F 4 .   ? 22.024 -24.011 4.515   1.00 26.84 ?  1519 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 4 .   ? 36.446 -6.550  10.146  1.00 44.83 ?  1520 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 4 .   ? 17.332 -6.778  -14.163 1.00 39.52 ?  1521 HOH   A O    1 
HETATM 6754 O  O    A HOH   F 4 .   ? 14.805 8.618   4.953   0.50 29.93 ?  1522 HOH   A O    1 
HETATM 6755 O  O    . HOH   F 4 .   ? 24.047 9.003   -7.226  1.00 34.43 ?  1523 HOH   A O    1 
HETATM 6756 O  O    B HOH   F 4 .   ? 11.844 11.924  6.900   0.50 37.43 ?  1524 HOH   A O    1 
HETATM 6757 O  O    . HOH   F 4 .   ? 15.933 -12.378 27.475  1.00 41.51 ?  1525 HOH   A O    1 
HETATM 6758 O  O    . HOH   F 4 .   ? 16.266 -21.200 18.757  1.00 40.33 ?  1526 HOH   A O    1 
HETATM 6759 O  O    . HOH   F 4 .   ? 14.625 -22.778 19.829  1.00 34.22 ?  1527 HOH   A O    1 
HETATM 6760 O  O    . HOH   G 4 .   ? 29.824 -22.432 5.437   1.00 20.77 ?  201  HOH   B O    1 
HETATM 6761 O  O    . HOH   G 4 .   ? 27.719 -29.160 -1.955  1.00 35.63 ?  202  HOH   B O    1 
HETATM 6762 O  O    . HOH   G 4 .   ? 52.941 -13.417 -20.334 1.00 37.02 ?  203  HOH   B O    1 
HETATM 6763 O  O    . HOH   G 4 .   ? 59.100 -18.700 6.780   1.00 38.60 ?  204  HOH   B O    1 
HETATM 6764 O  O    . HOH   G 4 .   ? 48.074 -6.878  15.527  1.00 35.17 ?  205  HOH   B O    1 
HETATM 6765 O  O    . HOH   G 4 .   ? 41.820 -35.908 -17.322 1.00 30.18 ?  206  HOH   B O    1 
HETATM 6766 O  O    . HOH   G 4 .   ? 37.916 -39.428 -0.194  1.00 40.05 ?  207  HOH   B O    1 
HETATM 6767 O  O    . HOH   G 4 .   ? 29.916 -26.293 4.026   1.00 27.82 ?  208  HOH   B O    1 
HETATM 6768 O  O    . HOH   G 4 .   ? 47.425 -7.399  -3.977  1.00 42.10 ?  209  HOH   B O    1 
HETATM 6769 O  O    . HOH   G 4 .   ? 27.790 -41.715 -15.172 1.00 35.74 ?  210  HOH   B O    1 
HETATM 6770 O  O    . HOH   G 4 .   ? 41.346 -7.779  5.514   1.00 39.68 ?  211  HOH   B O    1 
HETATM 6771 O  O    . HOH   G 4 .   ? 49.363 -22.703 -19.741 1.00 45.04 ?  212  HOH   B O    1 
HETATM 6772 O  O    . HOH   G 4 .   ? 58.159 -13.010 8.360   1.00 32.43 ?  213  HOH   B O    1 
HETATM 6773 O  O    . HOH   G 4 .   ? 56.320 -19.721 7.138   1.00 33.93 ?  214  HOH   B O    1 
HETATM 6774 O  O    . HOH   G 4 .   ? 54.462 -9.353  -8.732  1.00 19.62 ?  215  HOH   B O    1 
HETATM 6775 O  O    . HOH   G 4 .   ? 50.248 -3.362  7.155   1.00 34.35 ?  216  HOH   B O    1 
HETATM 6776 O  O    . HOH   G 4 .   ? 30.190 -40.965 -8.160  1.00 16.76 ?  217  HOH   B O    1 
HETATM 6777 O  O    . HOH   G 4 .   ? 57.694 -24.413 5.073   1.00 37.94 ?  218  HOH   B O    1 
HETATM 6778 O  O    . HOH   G 4 .   ? 29.751 -34.103 -0.447  1.00 33.90 ?  219  HOH   B O    1 
HETATM 6779 O  O    . HOH   G 4 .   ? 41.485 -39.123 -14.918 1.00 21.55 ?  220  HOH   B O    1 
HETATM 6780 O  O    . HOH   G 4 .   ? 56.653 -30.750 -7.827  1.00 29.78 ?  221  HOH   B O    1 
HETATM 6781 O  O    . HOH   G 4 .   ? 50.722 -6.096  0.189   1.00 27.09 ?  222  HOH   B O    1 
HETATM 6782 O  O    . HOH   G 4 .   ? 57.377 -16.227 -12.180 1.00 18.98 ?  223  HOH   B O    1 
HETATM 6783 O  O    . HOH   G 4 .   ? 57.105 -26.797 -7.605  1.00 38.90 ?  224  HOH   B O    1 
HETATM 6784 O  O    . HOH   G 4 .   ? 44.400 -7.191  2.057   1.00 33.73 ?  225  HOH   B O    1 
HETATM 6785 O  O    . HOH   G 4 .   ? 45.096 -34.874 6.785   1.00 43.97 ?  226  HOH   B O    1 
HETATM 6786 O  O    . HOH   G 4 .   ? 37.191 -19.621 -18.118 1.00 43.37 ?  227  HOH   B O    1 
HETATM 6787 O  O    . HOH   G 4 .   ? 34.512 -36.333 -7.232  1.00 18.10 ?  228  HOH   B O    1 
HETATM 6788 O  O    . HOH   G 4 .   ? 44.940 -43.481 -10.599 1.00 27.17 ?  229  HOH   B O    1 
HETATM 6789 O  O    . HOH   G 4 .   ? 35.080 -7.997  -3.070  1.00 18.64 ?  230  HOH   B O    1 
HETATM 6790 O  O    . HOH   G 4 .   ? 41.353 -9.650  13.028  1.00 22.73 ?  231  HOH   B O    1 
HETATM 6791 O  O    . HOH   G 4 .   ? 48.449 -36.482 -15.505 1.00 42.21 ?  232  HOH   B O    1 
HETATM 6792 O  O    . HOH   G 4 .   ? 30.856 -28.759 4.228   1.00 27.46 ?  233  HOH   B O    1 
HETATM 6793 O  O    . HOH   G 4 .   ? 28.401 -19.664 -13.094 1.00 25.07 ?  234  HOH   B O    1 
HETATM 6794 O  O    . HOH   G 4 .   ? 35.901 -43.187 -8.543  1.00 31.41 ?  235  HOH   B O    1 
HETATM 6795 O  O    . HOH   G 4 .   ? 39.299 -10.886 6.107   1.00 25.84 ?  236  HOH   B O    1 
HETATM 6796 O  O    . HOH   G 4 .   ? 40.595 -16.044 14.113  1.00 26.38 ?  237  HOH   B O    1 
HETATM 6797 O  O    . HOH   G 4 .   ? 51.667 -6.487  4.409   1.00 20.32 ?  238  HOH   B O    1 
HETATM 6798 O  O    . HOH   G 4 .   ? 55.352 -16.428 -14.292 1.00 34.72 ?  239  HOH   B O    1 
HETATM 6799 O  O    . HOH   G 4 .   ? 50.713 -12.958 -0.477  1.00 12.48 ?  240  HOH   B O    1 
HETATM 6800 O  O    . HOH   G 4 .   ? 32.794 -43.730 -11.380 1.00 20.48 ?  241  HOH   B O    1 
HETATM 6801 O  O    . HOH   G 4 .   ? 46.363 -1.604  13.262  1.00 27.76 ?  242  HOH   B O    1 
HETATM 6802 O  O    . HOH   G 4 .   ? 25.411 -25.922 -1.368  1.00 34.93 ?  243  HOH   B O    1 
HETATM 6803 O  O    . HOH   G 4 .   ? 44.486 -27.721 -0.729  1.00 22.45 ?  244  HOH   B O    1 
HETATM 6804 O  O    . HOH   G 4 .   ? 41.845 -23.496 9.257   1.00 17.56 ?  245  HOH   B O    1 
HETATM 6805 O  O    . HOH   G 4 .   ? 34.250 -18.524 11.383  1.00 25.14 ?  246  HOH   B O    1 
HETATM 6806 O  O    . HOH   G 4 .   ? 42.629 -22.855 3.844   1.00 12.18 ?  247  HOH   B O    1 
HETATM 6807 O  O    . HOH   G 4 .   ? 57.581 -24.356 -3.830  1.00 21.64 ?  248  HOH   B O    1 
HETATM 6808 O  O    . HOH   G 4 .   ? 43.054 -43.194 -8.287  1.00 29.14 ?  249  HOH   B O    1 
HETATM 6809 O  O    . HOH   G 4 .   ? 40.330 -12.753 -11.524 1.00 15.87 ?  250  HOH   B O    1 
HETATM 6810 O  O    . HOH   G 4 .   ? 42.556 -25.342 2.613   1.00 15.36 ?  251  HOH   B O    1 
HETATM 6811 O  O    . HOH   G 4 .   ? 39.484 -11.117 0.322   1.00 17.99 ?  252  HOH   B O    1 
HETATM 6812 O  O    . HOH   G 4 .   ? 51.521 -13.875 10.956  1.00 28.62 ?  253  HOH   B O    1 
HETATM 6813 O  O    . HOH   G 4 .   ? 38.434 -11.047 -2.255  1.00 19.50 ?  254  HOH   B O    1 
HETATM 6814 O  O    . HOH   G 4 .   ? 29.712 -25.195 -10.804 1.00 16.92 ?  255  HOH   B O    1 
HETATM 6815 O  O    . HOH   G 4 .   ? 58.150 -10.599 -4.030  1.00 20.77 ?  256  HOH   B O    1 
HETATM 6816 O  O    . HOH   G 4 .   ? 48.040 -24.489 -17.744 1.00 31.25 ?  257  HOH   B O    1 
HETATM 6817 O  O    . HOH   G 4 .   ? 34.499 -12.816 2.617   1.00 25.28 ?  258  HOH   B O    1 
HETATM 6818 O  O    . HOH   G 4 .   ? 33.518 -16.998 8.046   1.00 20.43 ?  259  HOH   B O    1 
HETATM 6819 O  O    . HOH   G 4 .   ? 27.127 -31.777 -9.995  1.00 20.82 ?  260  HOH   B O    1 
HETATM 6820 O  O    . HOH   G 4 .   ? 34.942 -24.563 13.834  1.00 31.21 ?  261  HOH   B O    1 
HETATM 6821 O  O    . HOH   G 4 .   ? 31.773 -17.933 -14.528 1.00 31.74 ?  262  HOH   B O    1 
HETATM 6822 O  O    . HOH   G 4 .   ? 43.200 -32.342 -17.145 1.00 23.25 ?  263  HOH   B O    1 
HETATM 6823 O  O    . HOH   G 4 .   ? 30.859 -15.731 2.653   1.00 14.14 ?  264  HOH   B O    1 
HETATM 6824 O  O    . HOH   G 4 .   ? 46.809 -29.542 9.739   1.00 31.63 ?  265  HOH   B O    1 
HETATM 6825 O  O    . HOH   G 4 .   ? 49.302 -28.689 -6.925  1.00 15.49 ?  266  HOH   B O    1 
HETATM 6826 O  O    . HOH   G 4 .   ? 57.461 -9.221  1.415   1.00 20.43 ?  267  HOH   B O    1 
HETATM 6827 O  O    . HOH   G 4 .   ? 38.894 -12.028 12.348  1.00 36.05 ?  268  HOH   B O    1 
HETATM 6828 O  O    . HOH   G 4 .   ? 50.971 -39.910 -8.278  1.00 30.92 ?  269  HOH   B O    1 
HETATM 6829 O  O    . HOH   G 4 .   ? 30.605 -42.208 -10.669 1.00 29.97 ?  270  HOH   B O    1 
HETATM 6830 O  O    . HOH   G 4 .   ? 42.356 -9.902  9.322   1.00 21.63 ?  271  HOH   B O    1 
HETATM 6831 O  O    . HOH   G 4 .   ? 42.854 -20.303 -20.729 1.00 36.85 ?  272  HOH   B O    1 
HETATM 6832 O  O    . HOH   G 4 .   ? 47.987 -22.762 5.827   1.00 17.22 ?  273  HOH   B O    1 
HETATM 6833 O  O    . HOH   G 4 .   ? 43.350 -15.769 -12.177 1.00 14.80 ?  274  HOH   B O    1 
HETATM 6834 O  O    . HOH   G 4 .   ? 46.573 -31.252 -4.826  1.00 20.95 ?  275  HOH   B O    1 
HETATM 6835 O  O    . HOH   G 4 .   ? 28.249 -34.311 -9.439  1.00 21.10 ?  276  HOH   B O    1 
HETATM 6836 O  O    . HOH   G 4 .   ? 56.899 -8.634  8.438   1.00 20.12 ?  277  HOH   B O    1 
HETATM 6837 O  O    . HOH   G 4 .   ? 28.444 -30.770 -14.786 1.00 30.59 ?  278  HOH   B O    1 
HETATM 6838 O  O    . HOH   G 4 .   ? 56.146 -23.499 -14.789 1.00 27.63 ?  279  HOH   B O    1 
HETATM 6839 O  O    . HOH   G 4 .   ? 27.950 -22.866 -7.989  1.00 18.62 ?  280  HOH   B O    1 
HETATM 6840 O  O    . HOH   G 4 .   ? 34.891 -33.328 -19.263 1.00 30.54 ?  281  HOH   B O    1 
HETATM 6841 O  O    . HOH   G 4 .   ? 57.115 -12.076 12.303  1.00 37.88 ?  282  HOH   B O    1 
HETATM 6842 O  O    . HOH   G 4 .   ? 48.391 -25.033 3.071   1.00 13.66 ?  283  HOH   B O    1 
HETATM 6843 O  O    . HOH   G 4 .   ? 37.394 -35.651 7.246   1.00 33.20 ?  284  HOH   B O    1 
HETATM 6844 O  O    . HOH   G 4 .   ? 49.750 -0.486  10.267  1.00 31.16 ?  285  HOH   B O    1 
HETATM 6845 O  O    . HOH   G 4 .   ? 47.059 -33.952 -4.677  1.00 17.44 ?  286  HOH   B O    1 
HETATM 6846 O  O    . HOH   G 4 .   ? 33.514 -15.284 -13.944 1.00 22.25 ?  287  HOH   B O    1 
HETATM 6847 O  O    . HOH   G 4 .   ? 48.691 -20.017 5.895   1.00 14.22 ?  288  HOH   B O    1 
HETATM 6848 O  O    . HOH   G 4 .   ? 42.393 -34.647 3.751   1.00 25.93 ?  289  HOH   B O    1 
HETATM 6849 O  O    . HOH   G 4 .   ? 52.478 -10.466 12.962  1.00 23.99 ?  290  HOH   B O    1 
HETATM 6850 O  O    . HOH   G 4 .   ? 52.561 -35.592 -8.661  1.00 30.73 ?  291  HOH   B O    1 
HETATM 6851 O  O    . HOH   G 4 .   ? 42.270 -9.951  -14.869 1.00 38.58 ?  292  HOH   B O    1 
HETATM 6852 O  O    . HOH   G 4 .   ? 36.803 -12.743 -1.529  1.00 27.96 ?  293  HOH   B O    1 
HETATM 6853 O  O    . HOH   G 4 .   ? 51.197 -37.548 -9.627  1.00 25.54 ?  294  HOH   B O    1 
HETATM 6854 O  O    . HOH   G 4 .   ? 41.148 -5.494  11.518  1.00 47.11 ?  295  HOH   B O    1 
HETATM 6855 O  O    . HOH   G 4 .   ? 42.719 -12.174 -18.456 1.00 29.03 ?  296  HOH   B O    1 
HETATM 6856 O  O    . HOH   G 4 .   ? 27.591 -26.767 -15.666 1.00 33.52 ?  297  HOH   B O    1 
HETATM 6857 O  O    . HOH   G 4 .   ? 45.373 -33.349 -15.984 1.00 23.54 ?  298  HOH   B O    1 
HETATM 6858 O  O    . HOH   G 4 .   ? 35.043 -33.582 4.478   1.00 28.98 ?  299  HOH   B O    1 
HETATM 6859 O  O    . HOH   G 4 .   ? 44.593 -27.447 1.947   1.00 15.47 ?  300  HOH   B O    1 
HETATM 6860 O  O    . HOH   G 4 .   ? 53.403 -30.181 4.479   1.00 18.81 ?  301  HOH   B O    1 
HETATM 6861 O  O    . HOH   G 4 .   ? 45.868 -40.372 -3.652  1.00 29.40 ?  302  HOH   B O    1 
HETATM 6862 O  O    . HOH   G 4 .   ? 37.515 -18.125 13.096  1.00 31.62 ?  303  HOH   B O    1 
HETATM 6863 O  O    . HOH   G 4 .   ? 43.552 -15.361 18.195  1.00 30.60 ?  304  HOH   B O    1 
HETATM 6864 O  O    . HOH   G 4 .   ? 44.009 -29.341 -4.710  1.00 24.21 ?  305  HOH   B O    1 
HETATM 6865 O  O    . HOH   G 4 .   ? 25.953 -21.479 -3.552  1.00 17.09 ?  306  HOH   B O    1 
HETATM 6866 O  O    . HOH   G 4 .   ? 41.248 -24.451 15.740  1.00 44.83 ?  307  HOH   B O    1 
HETATM 6867 O  O    . HOH   G 4 .   ? 37.801 -10.233 -10.710 1.00 17.66 ?  308  HOH   B O    1 
HETATM 6868 O  O    . HOH   G 4 .   ? 49.958 -24.630 5.826   1.00 35.66 ?  309  HOH   B O    1 
HETATM 6869 O  O    . HOH   G 4 .   ? 59.747 -15.263 8.205   1.00 33.27 ?  310  HOH   B O    1 
HETATM 6870 O  O    . HOH   G 4 .   ? 51.658 -5.902  -7.931  1.00 45.25 ?  311  HOH   B O    1 
HETATM 6871 O  O    . HOH   G 4 .   ? 53.100 -16.032 -12.745 1.00 28.05 ?  312  HOH   B O    1 
HETATM 6872 O  O    . HOH   G 4 .   ? 32.814 -34.587 -5.939  1.00 17.26 ?  313  HOH   B O    1 
HETATM 6873 O  O    . HOH   G 4 .   ? 62.669 -13.569 4.713   1.00 28.03 ?  314  HOH   B O    1 
HETATM 6874 O  O    . HOH   G 4 .   ? 48.085 -32.600 -16.633 1.00 47.71 ?  315  HOH   B O    1 
HETATM 6875 O  O    . HOH   G 4 .   ? 62.805 -20.115 -0.818  1.00 41.58 ?  316  HOH   B O    1 
HETATM 6876 O  O    . HOH   G 4 .   ? 37.095 -30.566 -21.030 1.00 31.67 ?  317  HOH   B O    1 
HETATM 6877 O  O    . HOH   G 4 .   ? 40.224 -10.830 -9.547  1.00 17.85 ?  318  HOH   B O    1 
HETATM 6878 O  O    . HOH   G 4 .   ? 41.717 -8.067  1.349   1.00 23.82 ?  319  HOH   B O    1 
HETATM 6879 O  O    . HOH   G 4 .   ? 43.192 -21.420 10.656  1.00 16.52 ?  320  HOH   B O    1 
HETATM 6880 O  O    . HOH   G 4 .   ? 53.614 -12.512 -22.272 1.00 32.07 ?  321  HOH   B O    1 
HETATM 6881 O  O    . HOH   G 4 .   ? 38.336 -12.783 7.908   1.00 19.01 ?  322  HOH   B O    1 
HETATM 6882 O  O    . HOH   G 4 .   ? 52.524 -29.182 -13.097 1.00 25.13 ?  323  HOH   B O    1 
HETATM 6883 O  O    . HOH   G 4 .   ? 26.339 -21.029 -6.247  1.00 17.46 ?  324  HOH   B O    1 
HETATM 6884 O  O    . HOH   G 4 .   ? 44.563 -24.618 9.563   1.00 19.54 ?  325  HOH   B O    1 
HETATM 6885 O  O    . HOH   G 4 .   ? 57.566 -22.012 3.211   1.00 30.63 ?  326  HOH   B O    1 
HETATM 6886 O  O    . HOH   G 4 .   ? 36.716 -12.413 4.300   1.00 18.64 ?  327  HOH   B O    1 
HETATM 6887 O  O    . HOH   G 4 .   ? 27.906 -14.741 -9.384  1.00 34.80 ?  328  HOH   B O    1 
HETATM 6888 O  O    . HOH   G 4 .   ? 33.647 -31.154 11.033  1.00 34.77 ?  329  HOH   B O    1 
HETATM 6889 O  O    . HOH   G 4 .   ? 51.379 -32.876 -10.829 1.00 41.15 ?  330  HOH   B O    1 
HETATM 6890 O  O    . HOH   G 4 .   ? 43.077 -34.593 0.041   1.00 20.41 ?  331  HOH   B O    1 
HETATM 6891 O  O    . HOH   G 4 .   ? 59.935 -17.225 -10.543 1.00 36.78 ?  332  HOH   B O    1 
HETATM 6892 O  O    . HOH   G 4 .   ? 47.130 -24.489 8.102   1.00 26.87 ?  333  HOH   B O    1 
HETATM 6893 O  O    . HOH   G 4 .   ? 44.106 -1.704  7.597   1.00 46.49 ?  334  HOH   B O    1 
HETATM 6894 O  O    . HOH   G 4 .   ? 38.349 -9.352  -13.244 1.00 28.91 ?  335  HOH   B O    1 
HETATM 6895 O  O    . HOH   G 4 .   ? 47.468 -27.414 1.995   1.00 15.30 ?  336  HOH   B O    1 
HETATM 6896 O  O    . HOH   G 4 .   ? 45.709 -36.212 -16.132 1.00 36.51 ?  337  HOH   B O    1 
HETATM 6897 O  O    . HOH   G 4 .   ? 42.807 -43.454 -14.434 1.00 46.91 ?  338  HOH   B O    1 
HETATM 6898 O  O    . HOH   G 4 .   ? 48.539 -11.916 -13.956 1.00 28.10 ?  339  HOH   B O    1 
HETATM 6899 O  O    . HOH   G 4 .   ? 46.827 -19.857 12.248  1.00 32.32 ?  340  HOH   B O    1 
HETATM 6900 O  O    . HOH   G 4 .   ? 39.500 -23.490 -20.361 1.00 39.72 ?  341  HOH   B O    1 
HETATM 6901 O  O    . HOH   G 4 .   ? 37.066 -15.049 -16.527 1.00 41.75 ?  342  HOH   B O    1 
HETATM 6902 O  O    . HOH   G 4 .   ? 28.873 -42.857 -12.416 1.00 38.06 ?  343  HOH   B O    1 
HETATM 6903 O  O    . HOH   G 4 .   ? 38.403 -12.197 -16.224 1.00 44.36 ?  344  HOH   B O    1 
HETATM 6904 O  O    . HOH   G 4 .   ? 37.046 -45.212 -9.789  1.00 39.53 ?  345  HOH   B O    1 
HETATM 6905 O  O    . HOH   G 4 .   ? 32.987 -14.679 1.039   1.00 19.71 ?  346  HOH   B O    1 
HETATM 6906 O  O    . HOH   G 4 .   ? 39.822 -44.253 -11.256 1.00 38.86 ?  347  HOH   B O    1 
HETATM 6907 O  O    . HOH   G 4 .   ? 62.483 -20.159 -4.827  1.00 45.11 ?  348  HOH   B O    1 
HETATM 6908 O  O    . HOH   G 4 .   ? 40.364 -43.436 -9.187  1.00 27.23 ?  349  HOH   B O    1 
HETATM 6909 O  O    . HOH   G 4 .   ? 55.597 -8.258  10.789  1.00 25.89 ?  350  HOH   B O    1 
HETATM 6910 O  O    . HOH   G 4 .   ? 27.796 -26.590 -0.632  1.00 30.82 ?  351  HOH   B O    1 
HETATM 6911 O  O    . HOH   G 4 .   ? 38.510 -22.352 15.035  1.00 41.79 ?  352  HOH   B O    1 
HETATM 6912 O  O    . HOH   G 4 .   ? 33.747 -9.245  -8.800  1.00 31.36 ?  353  HOH   B O    1 
HETATM 6913 O  O    . HOH   G 4 .   ? 23.222 -23.699 6.756   1.00 36.56 ?  354  HOH   B O    1 
HETATM 6914 O  O    . HOH   G 4 .   ? 44.167 -37.328 -17.833 1.00 34.73 ?  355  HOH   B O    1 
HETATM 6915 O  O    . HOH   G 4 .   ? 34.597 -10.333 7.497   1.00 24.37 ?  356  HOH   B O    1 
HETATM 6916 O  O    . HOH   G 4 .   ? 56.552 -7.311  3.150   1.00 28.22 ?  357  HOH   B O    1 
HETATM 6917 O  O    . HOH   G 4 .   ? 36.151 -8.476  -9.656  1.00 34.11 ?  358  HOH   B O    1 
HETATM 6918 O  O    . HOH   G 4 .   ? 33.950 -7.875  11.535  1.00 42.98 ?  359  HOH   B O    1 
HETATM 6919 O  O    . HOH   G 4 .   ? 43.125 -12.740 -21.232 1.00 41.63 ?  360  HOH   B O    1 
HETATM 6920 O  O    . HOH   G 4 .   ? 61.489 -19.888 1.570   1.00 34.46 ?  361  HOH   B O    1 
HETATM 6921 O  O    . HOH   G 4 .   ? 40.269 -8.771  9.947   1.00 40.88 ?  362  HOH   B O    1 
HETATM 6922 O  O    . HOH   G 4 .   ? 56.845 -21.490 -16.434 1.00 42.98 ?  363  HOH   B O    1 
HETATM 6923 O  O    . HOH   G 4 .   ? 27.135 -25.895 -11.414 1.00 33.95 ?  364  HOH   B O    1 
HETATM 6924 O  O    . HOH   G 4 .   ? 32.473 -23.589 14.010  1.00 40.28 ?  365  HOH   B O    1 
HETATM 6925 O  O    . HOH   G 4 .   ? 54.222 -5.751  3.031   1.00 37.61 ?  366  HOH   B O    1 
HETATM 6926 O  O    . HOH   G 4 .   ? 48.313 -26.532 8.810   1.00 40.57 ?  367  HOH   B O    1 
HETATM 6927 O  O    . HOH   G 4 .   ? 58.973 -10.484 9.135   1.00 39.59 ?  368  HOH   B O    1 
HETATM 6928 O  O    . HOH   G 4 .   ? 36.238 -8.759  8.947   1.00 40.72 ?  369  HOH   B O    1 
HETATM 6929 O  O    . HOH   G 4 .   ? 39.847 -7.015  7.765   1.00 43.19 ?  370  HOH   B O    1 
HETATM 6930 O  O    . HOH   G 4 .   ? 39.998 -11.356 -13.928 1.00 33.65 ?  371  HOH   B O    1 
HETATM 6931 O  O    . HOH   G 4 .   ? 51.996 -12.922 13.273  1.00 32.33 ?  372  HOH   B O    1 
HETATM 6932 O  O    . HOH   G 4 .   ? 41.733 -9.991  -17.414 1.00 53.12 ?  373  HOH   B O    1 
HETATM 6933 O  O    . HOH   G 4 .   ? 55.948 -7.789  -0.538  1.00 35.50 ?  374  HOH   B O    1 
HETATM 6934 O  O    . HOH   G 4 .   ? 62.993 -12.409 6.936   1.00 38.67 ?  375  HOH   B O    1 
HETATM 6935 O  O    . HOH   G 4 .   ? 41.836 -6.768  -4.841  1.00 48.67 ?  376  HOH   B O    1 
HETATM 6936 O  O    . HOH   G 4 .   ? 38.042 -10.585 10.040  1.00 30.08 ?  377  HOH   B O    1 
HETATM 6937 O  O    . HOH   G 4 .   ? 42.694 -17.171 -23.146 1.00 42.93 ?  378  HOH   B O    1 
HETATM 6938 O  O    . HOH   G 4 .   ? 40.162 -7.739  3.165   1.00 40.40 ?  379  HOH   B O    1 
HETATM 6939 O  O    . HOH   G 4 .   ? 36.502 -22.835 13.260  1.00 28.36 ?  380  HOH   B O    1 
HETATM 6940 O  O    . HOH   G 4 .   ? 44.049 -5.585  -3.488  1.00 42.06 ?  381  HOH   B O    1 
HETATM 6941 O  O    . HOH   G 4 .   ? 52.815 -29.896 7.137   1.00 23.75 ?  382  HOH   B O    1 
HETATM 6942 O  O    . HOH   G 4 .   ? 39.659 -14.033 15.730  1.00 52.59 ?  383  HOH   B O    1 
HETATM 6943 O  O    . HOH   G 4 .   ? 60.445 -22.347 2.800   1.00 52.84 ?  384  HOH   B O    1 
HETATM 6944 O  O    . HOH   G 4 .   ? 23.895 -20.790 -7.675  1.00 29.17 ?  385  HOH   B O    1 
HETATM 6945 O  O    . HOH   G 4 .   ? 35.349 -33.729 7.239   1.00 41.38 ?  386  HOH   B O    1 
HETATM 6946 O  O    . HOH   G 4 .   ? 46.753 -5.372  2.950   1.00 44.14 ?  387  HOH   B O    1 
HETATM 6947 O  O    . HOH   G 4 .   ? 35.273 -20.349 13.277  1.00 31.75 ?  388  HOH   B O    1 
HETATM 6948 O  O    . HOH   G 4 .   ? 25.814 -18.868 -11.961 1.00 39.76 ?  389  HOH   B O    1 
HETATM 6949 O  O    . HOH   G 4 .   ? 40.688 -6.620  -0.841  1.00 25.79 ?  390  HOH   B O    1 
HETATM 6950 O  O    . HOH   G 4 .   ? 40.865 -9.751  15.831  1.00 46.01 ?  391  HOH   B O    1 
HETATM 6951 O  O    . HOH   G 4 .   ? 44.014 -31.703 -3.824  1.00 32.20 ?  392  HOH   B O    1 
HETATM 6952 O  O    . HOH   G 4 .   ? 27.923 -27.051 2.209   1.00 32.88 ?  393  HOH   B O    1 
HETATM 6953 O  O    . HOH   G 4 .   ? 26.600 -27.937 -13.529 1.00 36.39 ?  394  HOH   B O    1 
HETATM 6954 O  O    . HOH   G 4 .   ? 50.578 -30.807 8.664   1.00 28.63 ?  395  HOH   B O    1 
HETATM 6955 O  O    . HOH   G 4 .   ? 24.593 -20.715 -10.442 1.00 38.38 ?  396  HOH   B O    1 
HETATM 6956 O  O    . HOH   G 4 .   ? 34.411 -33.481 9.581   1.00 34.43 ?  397  HOH   B O    1 
HETATM 6957 O  O    . HOH   G 4 .   ? 26.804 -30.603 -12.649 1.00 31.00 ?  398  HOH   B O    1 
HETATM 6958 O  O    . HOH   G 4 .   ? 57.533 -6.451  -2.365  1.00 33.77 ?  399  HOH   B O    1 
HETATM 6959 O  O    . HOH   G 4 .   ? 45.711 -20.181 15.220  1.00 52.36 ?  400  HOH   B O    1 
HETATM 6960 O  O    . HOH   G 4 .   ? 40.830 -11.819 -22.341 1.00 42.76 ?  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   ? 0.4918 0.4861 0.5591 -0.0286 -0.0054 0.0983  3    VAL   A N   
2    N  N   B VAL   A 3   ? 0.5482 0.5728 0.6123 0.0250  0.0037  0.0459  3    VAL   A N   
3    C  CA  A VAL   A 3   ? 0.4893 0.4847 0.5507 -0.0299 -0.0059 0.0977  3    VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.5475 0.5710 0.6057 0.0242  0.0018  0.0453  3    VAL   A CA  
5    C  C   A VAL   A 3   ? 0.4752 0.4764 0.5146 -0.0362 -0.0129 0.1011  3    VAL   A C   
6    C  C   B VAL   A 3   ? 0.5419 0.5672 0.5862 0.0190  -0.0040 0.0470  3    VAL   A C   
7    O  O   A VAL   A 3   ? 0.4779 0.4772 0.5186 -0.0327 -0.0125 0.1053  3    VAL   A O   
8    O  O   B VAL   A 3   ? 0.5425 0.5686 0.5958 0.0204  -0.0058 0.0476  3    VAL   A O   
9    C  CB  A VAL   A 3   ? 0.4982 0.4898 0.5696 -0.0268 0.0013  0.0948  3    VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.5513 0.5730 0.6151 0.0271  0.0061  0.0432  3    VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.5014 0.4916 0.5755 -0.0257 0.0039  0.0938  3    VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.5520 0.5736 0.6163 0.0280  0.0075  0.0426  3    VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.5007 0.4918 0.5744 -0.0261 0.0047  0.0939  3    VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.5537 0.5742 0.6201 0.0280  0.0076  0.0430  3    VAL   A CG2 
31   N  N   A ASN   A 4   ? 0.4551 0.4663 0.4667 -0.0461 -0.0197 0.0987  4    ASN   A N   
32   N  N   B ASN   A 4   ? 0.5339 0.5605 0.5502 0.0118  -0.0086 0.0487  4    ASN   A N   
33   C  CA  A ASN   A 4   ? 0.4331 0.4539 0.4149 -0.0575 -0.0248 0.0933  4    ASN   A CA  
34   C  CA  B ASN   A 4   ? 0.5245 0.5522 0.5113 0.0026  -0.0099 0.0479  4    ASN   A CA  
35   C  C   A ASN   A 4   ? 0.3997 0.4387 0.3660 -0.0694 -0.0156 0.0773  4    ASN   A C   
36   C  C   B ASN   A 4   ? 0.5024 0.5378 0.4728 -0.0094 -0.0002 0.0416  4    ASN   A C   
37   O  O   A ASN   A 4   ? 0.3977 0.4373 0.3462 -0.0712 -0.0195 0.0801  4    ASN   A O   
38   O  O   B ASN   A 4   ? 0.5066 0.5401 0.4702 -0.0089 -0.0012 0.0450  4    ASN   A O   
39   C  CB  A ASN   A 4   ? 0.4406 0.4555 0.4109 -0.0578 -0.0382 0.1015  4    ASN   A CB  
40   C  CB  B ASN   A 4   ? 0.5354 0.5562 0.5093 0.0040  -0.0205 0.0531  4    ASN   A CB  
41   C  CG  A ASN   A 4   ? 0.4457 0.4547 0.4043 -0.0592 -0.0485 0.1101  4    ASN   A CG  
42   C  CG  B ASN   A 4   ? 0.5432 0.5583 0.5070 0.0047  -0.0292 0.0579  4    ASN   A CG  
43   O  OD1 A ASN   A 4   ? 0.4481 0.4545 0.4006 -0.0593 -0.0516 0.1108  4    ASN   A OD1 
44   O  OD1 B ASN   A 4   ? 0.5470 0.5592 0.5069 0.0059  -0.0330 0.0596  4    ASN   A OD1 
45   N  ND2 A ASN   A 4   ? 0.4463 0.4537 0.4040 -0.0596 -0.0542 0.1170  4    ASN   A ND2 
46   N  ND2 B ASN   A 4   ? 0.5452 0.5588 0.5081 0.0049  -0.0314 0.0607  4    ASN   A ND2 
59   N  N   A SER   A 5   ? 0.3665 0.4210 0.3374 -0.0791 -0.0070 0.0577  5    SER   A N   
60   N  N   B SER   A 5   ? 0.4738 0.5188 0.4420 -0.0231 0.0099  0.0321  5    SER   A N   
61   C  CA  A SER   A 5   ? 0.3323 0.4043 0.3171 -0.0837 0.0046  0.0350  5    SER   A CA  
62   C  CA  B SER   A 5   ? 0.4433 0.4985 0.4117 -0.0360 0.0225  0.0224  5    SER   A CA  
63   C  C   A SER   A 5   ? 0.2959 0.3783 0.2809 -0.0784 0.0158  0.0205  5    SER   A C   
64   C  C   B SER   A 5   ? 0.4079 0.4688 0.3759 -0.0480 0.0358  0.0185  5    SER   A C   
65   O  O   A SER   A 5   ? 0.2997 0.3837 0.2797 -0.0706 0.0110  0.0096  5    SER   A O   
66   O  O   B SER   A 5   ? 0.4113 0.4721 0.3720 -0.0471 0.0402  0.0144  5    SER   A O   
67   C  CB  A SER   A 5   ? 0.3389 0.4133 0.3381 -0.0876 0.0031  0.0266  5    SER   A CB  
68   C  CB  B SER   A 5   ? 0.4486 0.5062 0.4201 -0.0359 0.0210  0.0176  5    SER   A CB  
69   O  OG  A SER   A 5   ? 0.3435 0.4183 0.3489 -0.0894 0.0055  0.0253  5    SER   A OG  
70   O  OG  B SER   A 5   ? 0.4525 0.5110 0.4282 -0.0349 0.0203  0.0142  5    SER   A OG  
81   N  N   A PHE   A 6   ? 0.2532 0.3424 0.2466 -0.0800 0.0319  0.0186  6    PHE   A N   
82   N  N   B PHE   A 6   ? 0.3671 0.4339 0.3461 -0.0615 0.0457  0.0208  6    PHE   A N   
83   C  CA  A PHE   A 6   ? 0.2221 0.3093 0.2104 -0.0779 0.0462  0.0279  6    PHE   A CA  
84   C  CA  B PHE   A 6   ? 0.3253 0.3980 0.3135 -0.0720 0.0513  0.0275  6    PHE   A CA  
85   C  C   A PHE   A 6   ? 0.2177 0.3146 0.2243 -0.0770 0.0564  0.0303  6    PHE   A C   
86   C  C   B PHE   A 6   ? 0.3091 0.3873 0.3196 -0.0762 0.0608  0.0269  6    PHE   A C   
87   O  O   A PHE   A 6   ? 0.2242 0.3182 0.2537 -0.0785 0.0471  0.0283  6    PHE   A O   
88   O  O   B PHE   A 6   ? 0.3111 0.3884 0.3299 -0.0755 0.0639  0.0272  6    PHE   A O   
89   C  CB  A PHE   A 6   ? 0.2054 0.2754 0.1922 -0.0692 0.0447  0.0287  6    PHE   A CB  
90   C  CB  B PHE   A 6   ? 0.3028 0.3748 0.2820 -0.0748 0.0470  0.0343  6    PHE   A CB  
91   C  CG  A PHE   A 6   ? 0.1946 0.2495 0.1874 -0.0576 0.0432  0.0259  6    PHE   A CG  
92   C  CG  B PHE   A 6   ? 0.2834 0.3554 0.2617 -0.0729 0.0399  0.0336  6    PHE   A CG  
93   C  CD1 A PHE   A 6   ? 0.1911 0.2374 0.1803 -0.0489 0.0367  0.0207  6    PHE   A CD1 
94   C  CD1 B PHE   A 6   ? 0.2771 0.3465 0.2570 -0.0691 0.0357  0.0319  6    PHE   A CD1 
95   C  CD2 A PHE   A 6   ? 0.1954 0.2431 0.1966 -0.0412 0.0481  0.0163  6    PHE   A CD2 
96   C  CD2 B PHE   A 6   ? 0.2778 0.3498 0.2629 -0.0716 0.0370  0.0333  6    PHE   A CD2 
97   C  CE1 A PHE   A 6   ? 0.1922 0.2334 0.1919 -0.0441 0.0402  0.0154  6    PHE   A CE1 
98   C  CE1 B PHE   A 6   ? 0.2737 0.3425 0.2569 -0.0668 0.0343  0.0318  6    PHE   A CE1 
99   C  CE2 A PHE   A 6   ? 0.1956 0.2366 0.2097 -0.0340 0.0480  0.0070  6    PHE   A CE2 
100  C  CE2 B PHE   A 6   ? 0.2749 0.3469 0.2685 -0.0673 0.0338  0.0291  6    PHE   A CE2 
101  C  CZ  A PHE   A 6   ? 0.1948 0.2340 0.2066 -0.0401 0.0419  0.0049  6    PHE   A CZ  
102  C  CZ  B PHE   A 6   ? 0.2734 0.3431 0.2657 -0.0673 0.0310  0.0284  6    PHE   A CZ  
121  N  N   A SER   A 7   ? 0.2085 0.3145 0.2189 -0.0727 0.0627  0.0321  7    SER   A N   
122  N  N   B SER   A 7   ? 0.2917 0.3741 0.3184 -0.0785 0.0606  0.0235  7    SER   A N   
123  C  CA  A SER   A 7   ? 0.2124 0.3217 0.2284 -0.0615 0.0543  0.0209  7    SER   A CA  
124  C  CA  B SER   A 7   ? 0.2772 0.3632 0.3213 -0.0747 0.0559  0.0172  7    SER   A CA  
125  C  C   A SER   A 7   ? 0.2071 0.3047 0.2335 -0.0589 0.0556  0.0209  7    SER   A C   
126  C  C   B SER   A 7   ? 0.2546 0.3407 0.2915 -0.0801 0.0588  0.0178  7    SER   A C   
127  O  O   A SER   A 7   ? 0.2048 0.3019 0.2415 -0.0604 0.0594  0.0225  7    SER   A O   
128  O  O   B SER   A 7   ? 0.2515 0.3374 0.2877 -0.0857 0.0704  0.0287  7    SER   A O   
129  C  CB  A SER   A 7   ? 0.2218 0.3409 0.2277 -0.0507 0.0513  0.0150  7    SER   A CB  
130  C  CB  B SER   A 7   ? 0.2870 0.3735 0.3511 -0.0656 0.0474  0.0159  7    SER   A CB  
131  O  OG  A SER   A 7   ? 0.2316 0.3527 0.2313 -0.0426 0.0506  0.0157  7    SER   A OG  
132  O  OG  B SER   A 7   ? 0.2970 0.3800 0.3792 -0.0579 0.0389  0.0141  7    SER   A OG  
143  N  N   A GLY   A 8   ? 0.2032 0.2914 0.2302 -0.0592 0.0575  0.0164  8    GLY   A N   
144  N  N   B GLY   A 8   ? 0.2354 0.3233 0.2668 -0.0770 0.0514  0.0068  8    GLY   A N   
145  C  CA  A GLY   A 8   ? 0.1953 0.2771 0.2268 -0.0509 0.0501  0.0158  8    GLY   A CA  
146  C  CA  B GLY   A 8   ? 0.2230 0.3095 0.2551 -0.0626 0.0453  0.0048  8    GLY   A CA  
147  C  C   A GLY   A 8   ? 0.1809 0.2651 0.2144 -0.0433 0.0384  0.0106  8    GLY   A C   
148  C  C   B GLY   A 8   ? 0.2077 0.2969 0.2486 -0.0492 0.0422  0.0016  8    GLY   A C   
149  O  O   A GLY   A 8   ? 0.1859 0.2669 0.2182 -0.0302 0.0308  -0.0055 8    GLY   A O   
150  O  O   B GLY   A 8   ? 0.2095 0.3025 0.2566 -0.0368 0.0393  -0.0093 8    GLY   A O   
157  N  N   A TYR   A 9   ? 0.1720 0.2505 0.2080 -0.0391 0.0278  0.0248  9    TYR   A N   
158  N  N   B TYR   A 9   ? 0.1936 0.2776 0.2332 -0.0465 0.0422  0.0108  9    TYR   A N   
159  C  CA  A TYR   A 9   ? 0.1646 0.2313 0.1961 -0.0333 0.0322  0.0339  9    TYR   A CA  
160  C  CA  B TYR   A 9   ? 0.1814 0.2587 0.2195 -0.0409 0.0417  0.0199  9    TYR   A CA  
161  C  C   A TYR   A 9   ? 0.1636 0.2123 0.1808 -0.0229 0.0426  0.0479  9    TYR   A C   
162  C  C   B TYR   A 9   ? 0.1815 0.2396 0.2097 -0.0361 0.0401  0.0273  9    TYR   A C   
163  O  O   A TYR   A 9   ? 0.1765 0.2234 0.1860 -0.0128 0.0527  0.0435  9    TYR   A O   
164  O  O   B TYR   A 9   ? 0.1902 0.2412 0.2098 -0.0292 0.0395  0.0209  9    TYR   A O   
165  C  CB  A TYR   A 9   ? 0.1619 0.2433 0.2075 -0.0271 0.0221  0.0257  9    TYR   A CB  
166  C  CB  B TYR   A 9   ? 0.1698 0.2638 0.2182 -0.0356 0.0424  0.0201  9    TYR   A CB  
167  C  CG  A TYR   A 9   ? 0.1603 0.2492 0.2031 -0.0171 0.0216  0.0190  9    TYR   A CG  
168  C  CG  B TYR   A 9   ? 0.1666 0.2660 0.2211 -0.0313 0.0461  0.0197  9    TYR   A CG  
169  C  CD1 A TYR   A 9   ? 0.1506 0.2518 0.2093 -0.0154 0.0174  0.0227  9    TYR   A CD1 
170  C  CD1 B TYR   A 9   ? 0.1640 0.2680 0.2276 -0.0406 0.0439  0.0255  9    TYR   A CD1 
171  C  CD2 A TYR   A 9   ? 0.1585 0.2473 0.2010 -0.0188 0.0187  0.0187  9    TYR   A CD2 
172  C  CD2 B TYR   A 9   ? 0.1578 0.2602 0.2181 -0.0290 0.0422  0.0264  9    TYR   A CD2 
173  C  CE1 A TYR   A 9   ? 0.1498 0.2519 0.2150 -0.0128 0.0177  0.0202  9    TYR   A CE1 
174  C  CE1 B TYR   A 9   ? 0.1575 0.2643 0.2334 -0.0363 0.0440  0.0301  9    TYR   A CE1 
175  C  CE2 A TYR   A 9   ? 0.1615 0.2502 0.2105 -0.0171 0.0217  0.0144  9    TYR   A CE2 
176  C  CE2 B TYR   A 9   ? 0.1547 0.2591 0.2251 -0.0283 0.0401  0.0279  9    TYR   A CE2 
177  C  CZ  A TYR   A 9   ? 0.1578 0.2530 0.2235 -0.0199 0.0254  0.0172  9    TYR   A CZ  
178  C  CZ  B TYR   A 9   ? 0.1431 0.2578 0.2332 -0.0324 0.0429  0.0289  9    TYR   A CZ  
179  O  OH  A TYR   A 9   ? 0.1687 0.2558 0.2451 -0.0231 0.0268  0.0172  9    TYR   A OH  
180  O  OH  B TYR   A 9   ? 0.1281 0.2552 0.2454 -0.0315 0.0357  0.0287  9    TYR   A OH  
199  N  N   A LEU   A 10  ? 0.1598 0.1988 0.1822 -0.0257 0.0309  0.0480  10   LEU   A N   
200  N  N   B LEU   A 10  ? 0.1757 0.2270 0.2158 -0.0372 0.0254  0.0379  10   LEU   A N   
201  C  CA  A LEU   A 10  ? 0.1551 0.1913 0.1918 -0.0326 0.0163  0.0427  10   LEU   A CA  
202  C  CA  B LEU   A 10  ? 0.1748 0.2182 0.2257 -0.0452 0.0186  0.0414  10   LEU   A CA  
203  C  C   A LEU   A 10  ? 0.1500 0.1752 0.1840 -0.0424 0.0088  0.0368  10   LEU   A C   
204  C  C   B LEU   A 10  ? 0.1680 0.2099 0.2313 -0.0392 0.0131  0.0489  10   LEU   A C   
205  O  O   A LEU   A 10  ? 0.1653 0.1629 0.1801 -0.0383 0.0266  0.0300  10   LEU   A O   
206  O  O   B LEU   A 10  ? 0.1757 0.1956 0.2357 -0.0374 0.0310  0.0486  10   LEU   A O   
207  C  CB  A LEU   A 10  ? 0.1627 0.1947 0.2127 -0.0308 0.0071  0.0546  10   LEU   A CB  
208  C  CB  B LEU   A 10  ? 0.1848 0.2209 0.2306 -0.0520 0.0259  0.0399  10   LEU   A CB  
209  C  CG  A LEU   A 10  ? 0.1734 0.2036 0.2443 -0.0210 -0.0067 0.0614  10   LEU   A CG  
210  C  CG  B LEU   A 10  ? 0.2009 0.2282 0.2322 -0.0468 0.0272  0.0346  10   LEU   A CG  
211  C  CD1 A LEU   A 10  ? 0.1925 0.2102 0.2665 -0.0221 -0.0146 0.0635  10   LEU   A CD1 
212  C  CD1 B LEU   A 10  ? 0.2110 0.2342 0.2447 -0.0501 0.0135  0.0303  10   LEU   A CD1 
213  C  CD2 A LEU   A 10  ? 0.1880 0.2220 0.2717 -0.0105 0.0092  0.0468  10   LEU   A CD2 
214  C  CD2 B LEU   A 10  ? 0.2069 0.2326 0.2471 -0.0410 0.0314  0.0283  10   LEU   A CD2 
237  N  N   A LYS   A 11  ? 0.1437 0.1701 0.1667 -0.0514 -0.0017 0.0559  11   LYS   A N   
238  N  N   B LYS   A 11  ? 0.1751 0.2142 0.2380 -0.0343 0.0056  0.0566  11   LYS   A N   
239  C  CA  A LYS   A 11  ? 0.1456 0.1728 0.1608 -0.0620 -0.0041 0.0452  11   LYS   A CA  
240  C  CA  B LYS   A 11  ? 0.1946 0.2247 0.2443 -0.0269 0.0004  0.0608  11   LYS   A CA  
241  C  C   A LYS   A 11  ? 0.1472 0.1849 0.1595 -0.0639 -0.0059 0.0593  11   LYS   A C   
242  C  C   B LYS   A 11  ? 0.1751 0.2148 0.2203 -0.0322 0.0054  0.0671  11   LYS   A C   
243  O  O   A LYS   A 11  ? 0.1382 0.1906 0.1769 -0.0707 -0.0091 0.0538  11   LYS   A O   
244  O  O   B LYS   A 11  ? 0.1668 0.2061 0.2489 -0.0388 -0.0020 0.0603  11   LYS   A O   
245  C  CB  A LYS   A 11  ? 0.1493 0.1615 0.1067 -0.0621 -0.0129 0.0397  11   LYS   A CB  
246  C  CB  B LYS   A 11  ? 0.2330 0.2520 0.2667 -0.0180 -0.0032 0.0494  11   LYS   A CB  
247  C  CG  A LYS   A 11  ? 0.1653 0.1417 0.1045 -0.0693 0.0032  0.0411  11   LYS   A CG  
248  C  CG  B LYS   A 11  ? 0.2675 0.2790 0.2920 -0.0182 -0.0059 0.0328  11   LYS   A CG  
249  C  CD  A LYS   A 11  ? 0.1698 0.1420 0.1185 -0.0578 0.0011  0.0357  11   LYS   A CD  
250  C  CD  B LYS   A 11  ? 0.2903 0.2906 0.3003 -0.0270 -0.0036 0.0289  11   LYS   A CD  
251  C  CE  A LYS   A 11  ? 0.1733 0.1335 0.1270 -0.0433 -0.0042 0.0352  11   LYS   A CE  
252  C  CE  B LYS   A 11  ? 0.3034 0.3004 0.3062 -0.0352 0.0011  0.0234  11   LYS   A CE  
253  N  NZ  A LYS   A 11  ? 0.1647 0.1249 0.1308 -0.0249 -0.0146 0.0322  11   LYS   A NZ  
254  N  NZ  B LYS   A 11  ? 0.3130 0.3067 0.3138 -0.0359 0.0027  0.0198  11   LYS   A NZ  
281  N  N   A LEU   A 12  ? 0.1463 0.1886 0.1646 -0.0585 -0.0262 0.0601  12   LEU   A N   
282  N  N   B LEU   A 12  ? 0.1683 0.2096 0.1805 -0.0361 0.0083  0.0735  12   LEU   A N   
283  C  CA  A LEU   A 12  ? 0.1545 0.2021 0.1817 -0.0508 -0.0243 0.0625  12   LEU   A CA  
284  C  CA  B LEU   A 12  ? 0.1706 0.2217 0.1709 -0.0351 0.0079  0.0683  12   LEU   A CA  
285  C  C   A LEU   A 12  ? 0.1537 0.1929 0.2068 -0.0544 -0.0240 0.0572  12   LEU   A C   
286  C  C   B LEU   A 12  ? 0.1606 0.2175 0.1717 -0.0406 0.0097  0.0533  12   LEU   A C   
287  O  O   A LEU   A 12  ? 0.1619 0.2014 0.2269 -0.0575 -0.0222 0.0467  12   LEU   A O   
288  O  O   B LEU   A 12  ? 0.1685 0.2234 0.1808 -0.0393 0.0070  0.0453  12   LEU   A O   
289  C  CB  A LEU   A 12  ? 0.1596 0.2107 0.1822 -0.0409 -0.0163 0.0682  12   LEU   A CB  
290  C  CB  B LEU   A 12  ? 0.1837 0.2256 0.1878 -0.0357 0.0083  0.0667  12   LEU   A CB  
291  C  CG  A LEU   A 12  ? 0.1607 0.2177 0.1701 -0.0356 -0.0079 0.0689  12   LEU   A CG  
292  C  CG  B LEU   A 12  ? 0.1967 0.2310 0.2027 -0.0340 0.0218  0.0647  12   LEU   A CG  
293  C  CD1 A LEU   A 12  ? 0.1690 0.2234 0.1751 -0.0299 0.0035  0.0603  12   LEU   A CD1 
294  C  CD1 B LEU   A 12  ? 0.2074 0.2338 0.2026 -0.0316 0.0347  0.0726  12   LEU   A CD1 
295  C  CD2 A LEU   A 12  ? 0.1587 0.2267 0.1687 -0.0284 -0.0135 0.0600  12   LEU   A CD2 
296  C  CD2 B LEU   A 12  ? 0.1962 0.2362 0.2067 -0.0305 0.0218  0.0556  12   LEU   A CD2 
319  N  N   A THR   A 13  ? 0.1517 0.1801 0.2174 -0.0518 -0.0168 0.0527  13   THR   A N   
320  N  N   B THR   A 13  ? 0.1522 0.2047 0.1750 -0.0431 0.0082  0.0401  13   THR   A N   
321  C  CA  A THR   A 13  ? 0.1614 0.1712 0.2304 -0.0484 -0.0113 0.0458  13   THR   A CA  
322  C  CA  B THR   A 13  ? 0.1624 0.1973 0.1834 -0.0466 0.0181  0.0322  13   THR   A CA  
323  C  C   A THR   A 13  ? 0.1622 0.1632 0.2307 -0.0389 -0.0190 0.0465  13   THR   A C   
324  C  C   B THR   A 13  ? 0.1706 0.1933 0.1968 -0.0485 0.0178  0.0400  13   THR   A C   
325  O  O   A THR   A 13  ? 0.1557 0.1581 0.2285 -0.0269 -0.0211 0.0406  13   THR   A O   
326  O  O   B THR   A 13  ? 0.1739 0.1897 0.2024 -0.0454 0.0146  0.0422  13   THR   A O   
327  C  CB  A THR   A 13  ? 0.1744 0.1746 0.2397 -0.0450 -0.0134 0.0440  13   THR   A CB  
328  C  CB  B THR   A 13  ? 0.1634 0.2026 0.1764 -0.0368 0.0166  0.0275  13   THR   A CB  
329  O  OG1 A THR   A 13  ? 0.1764 0.1620 0.2625 -0.0405 -0.0162 0.0346  13   THR   A OG1 
330  O  OG1 B THR   A 13  ? 0.1531 0.1997 0.1809 -0.0354 0.0174  0.0295  13   THR   A OG1 
331  C  CG2 A THR   A 13  ? 0.1883 0.1922 0.2527 -0.0371 -0.0115 0.0344  13   THR   A CG2 
332  C  CG2 B THR   A 13  ? 0.1744 0.2151 0.1972 -0.0299 0.0119  0.0149  13   THR   A CG2 
347  N  N   A ASP   A 14  ? 0.1650 0.1651 0.2355 -0.0399 -0.0168 0.0484  14   ASP   A N   
348  N  N   B ASP   A 14  ? 0.1672 0.1921 0.2000 -0.0535 0.0184  0.0452  14   ASP   A N   
349  C  CA  A ASP   A 14  ? 0.1618 0.1682 0.2362 -0.0412 -0.0139 0.0662  14   ASP   A CA  
350  C  CA  B ASP   A 14  ? 0.1766 0.1952 0.2317 -0.0433 0.0002  0.0416  14   ASP   A CA  
351  C  C   A ASP   A 14  ? 0.1645 0.1627 0.2181 -0.0339 -0.0324 0.0739  14   ASP   A C   
352  C  C   B ASP   A 14  ? 0.1739 0.1711 0.2218 -0.0398 -0.0160 0.0473  14   ASP   A C   
353  O  O   A ASP   A 14  ? 0.1776 0.1610 0.2075 -0.0321 -0.0480 0.0801  14   ASP   A O   
354  O  O   B ASP   A 14  ? 0.1899 0.1556 0.2268 -0.0430 -0.0351 0.0673  14   ASP   A O   
355  C  CB  A ASP   A 14  ? 0.1702 0.1854 0.2734 -0.0478 0.0036  0.0818  14   ASP   A CB  
356  C  CB  B ASP   A 14  ? 0.1974 0.2231 0.2931 -0.0309 -0.0104 0.0363  14   ASP   A CB  
357  C  CG  A ASP   A 14  ? 0.1883 0.2154 0.3338 -0.0529 0.0009  0.0688  14   ASP   A CG  
358  C  CG  B ASP   A 14  ? 0.2144 0.2497 0.3471 -0.0185 -0.0182 0.0277  14   ASP   A CG  
359  O  OD1 A ASP   A 14  ? 0.2011 0.2155 0.3429 -0.0501 -0.0089 0.0673  14   ASP   A OD1 
360  O  OD1 B ASP   A 14  ? 0.2272 0.2556 0.3676 -0.0063 -0.0231 0.0352  14   ASP   A OD1 
361  O  OD2 A ASP   A 14  ? 0.2033 0.2287 0.3695 -0.0574 -0.0039 0.0575  14   ASP   A OD2 
362  O  OD2 B ASP   A 14  ? 0.2206 0.2643 0.3735 -0.0209 -0.0262 0.0198  14   ASP   A OD2 
371  N  N   A ASN   A 15  ? 0.1540 0.1536 0.2170 -0.0281 -0.0156 0.0712  15   ASN   A N   
372  N  N   B ASN   A 15  ? 0.1551 0.1570 0.2098 -0.0332 0.0036  0.0296  15   ASN   A N   
373  C  CA  A ASN   A 15  ? 0.1491 0.1539 0.2056 -0.0195 -0.0054 0.0448  15   ASN   A CA  
374  C  CA  B ASN   A 15  ? 0.1472 0.1531 0.2042 -0.0269 0.0100  0.0072  15   ASN   A CA  
375  C  C   A ASN   A 15  ? 0.1444 0.1538 0.1897 -0.0221 0.0043  0.0341  15   ASN   A C   
376  C  C   B ASN   A 15  ? 0.1499 0.1496 0.2059 -0.0214 0.0174  0.0060  15   ASN   A C   
377  O  O   A ASN   A 15  ? 0.1432 0.1628 0.2003 -0.0228 0.0047  0.0192  15   ASN   A O   
378  O  O   B ASN   A 15  ? 0.1459 0.1514 0.2261 -0.0149 0.0136  0.0053  15   ASN   A O   
379  C  CB  A ASN   A 15  ? 0.1539 0.1478 0.2076 -0.0120 0.0037  0.0410  15   ASN   A CB  
380  C  CB  B ASN   A 15  ? 0.1424 0.1555 0.1907 -0.0234 0.0069  0.0000  15   ASN   A CB  
381  C  CG  A ASN   A 15  ? 0.1595 0.1519 0.2129 -0.0148 0.0077  0.0342  15   ASN   A CG  
382  C  CG  B ASN   A 15  ? 0.1449 0.1618 0.1984 -0.0232 0.0024  -0.0072 15   ASN   A CG  
383  O  OD1 A ASN   A 15  ? 0.1656 0.1450 0.2217 -0.0186 0.0128  0.0333  15   ASN   A OD1 
384  O  OD1 B ASN   A 15  ? 0.1490 0.1607 0.2172 -0.0346 0.0009  -0.0103 15   ASN   A OD1 
385  N  ND2 A ASN   A 15  ? 0.1614 0.1641 0.2086 -0.0129 0.0146  0.0285  15   ASN   A ND2 
386  N  ND2 B ASN   A 15  ? 0.1457 0.1753 0.1919 -0.0224 -0.0043 -0.0068 15   ASN   A ND2 
399  N  N   A VAL   A 16  ? 0.1450 0.1426 0.1721 -0.0154 0.0044  0.0329  16   VAL   A N   
400  N  N   B VAL   A 16  ? 0.1555 0.1428 0.1941 -0.0152 0.0205  0.0029  16   VAL   A N   
401  C  CA  A VAL   A 16  ? 0.1428 0.1404 0.1632 -0.0166 0.0090  0.0356  16   VAL   A CA  
402  C  CA  B VAL   A 16  ? 0.1547 0.1374 0.1869 -0.0164 0.0170  -0.0084 16   VAL   A CA  
403  C  C   A VAL   A 16  ? 0.1356 0.1476 0.1737 -0.0193 0.0069  0.0284  16   VAL   A C   
404  C  C   B VAL   A 16  ? 0.1474 0.1333 0.1741 -0.0157 0.0175  0.0039  16   VAL   A C   
405  O  O   A VAL   A 16  ? 0.1352 0.1451 0.1765 -0.0185 0.0179  0.0197  16   VAL   A O   
406  O  O   B VAL   A 16  ? 0.1432 0.1403 0.1908 -0.0237 0.0237  0.0022  16   VAL   A O   
407  C  CB  A VAL   A 16  ? 0.1531 0.1393 0.1435 -0.0062 0.0173  0.0305  16   VAL   A CB  
408  C  CB  B VAL   A 16  ? 0.1639 0.1432 0.1950 -0.0107 0.0260  -0.0161 16   VAL   A CB  
409  C  CG1 A VAL   A 16  ? 0.1613 0.1397 0.1349 0.0000  0.0128  0.0130  16   VAL   A CG1 
410  C  CG1 B VAL   A 16  ? 0.1768 0.1488 0.2000 -0.0074 0.0147  -0.0194 16   VAL   A CG1 
411  C  CG2 A VAL   A 16  ? 0.1600 0.1506 0.1666 0.0034  0.0309  0.0245  16   VAL   A CG2 
412  C  CG2 B VAL   A 16  ? 0.1674 0.1503 0.1943 -0.0091 0.0356  -0.0235 16   VAL   A CG2 
431  N  N   A TYR   A 17  ? 0.1354 0.1434 0.1801 -0.0234 0.0150  0.0287  17   TYR   A N   
432  N  N   B TYR   A 17  ? 0.1494 0.1362 0.1737 -0.0110 0.0256  0.0125  17   TYR   A N   
433  C  CA  A TYR   A 17  ? 0.1376 0.1451 0.1775 -0.0259 0.0142  0.0366  17   TYR   A CA  
434  C  CA  B TYR   A 17  ? 0.1468 0.1470 0.1705 -0.0107 0.0168  0.0196  17   TYR   A CA  
435  C  C   A TYR   A 17  ? 0.1415 0.1556 0.1956 -0.0280 0.0284  0.0427  17   TYR   A C   
436  C  C   B TYR   A 17  ? 0.1525 0.1470 0.1965 -0.0098 0.0147  0.0155  17   TYR   A C   
437  O  O   A TYR   A 17  ? 0.1322 0.1546 0.1916 -0.0275 0.0213  0.0459  17   TYR   A O   
438  O  O   B TYR   A 17  ? 0.1544 0.1432 0.1873 -0.0121 0.0130  0.0157  17   TYR   A O   
439  C  CB  A TYR   A 17  ? 0.1560 0.1420 0.1759 -0.0316 0.0052  0.0337  17   TYR   A CB  
440  C  CB  B TYR   A 17  ? 0.1422 0.1611 0.1679 -0.0023 0.0071  0.0149  17   TYR   A CB  
441  C  CG  A TYR   A 17  ? 0.1701 0.1512 0.1754 -0.0310 0.0011  0.0201  17   TYR   A CG  
442  C  CG  B TYR   A 17  ? 0.1478 0.1799 0.1866 -0.0028 0.0106  0.0194  17   TYR   A CG  
443  C  CD1 A TYR   A 17  ? 0.1803 0.1618 0.1739 -0.0229 0.0084  0.0187  17   TYR   A CD1 
444  C  CD1 B TYR   A 17  ? 0.1623 0.1906 0.1907 0.0071  0.0122  0.0172  17   TYR   A CD1 
445  C  CD2 A TYR   A 17  ? 0.1787 0.1546 0.1718 -0.0357 0.0057  0.0175  17   TYR   A CD2 
446  C  CD2 B TYR   A 17  ? 0.1564 0.1856 0.1986 -0.0049 0.0138  0.0263  17   TYR   A CD2 
447  C  CE1 A TYR   A 17  ? 0.1819 0.1679 0.1790 -0.0245 0.0039  0.0223  17   TYR   A CE1 
448  C  CE1 B TYR   A 17  ? 0.1726 0.1955 0.1951 0.0089  0.0125  0.0189  17   TYR   A CE1 
449  C  CE2 A TYR   A 17  ? 0.1826 0.1604 0.1719 -0.0301 -0.0003 0.0138  17   TYR   A CE2 
450  C  CE2 B TYR   A 17  ? 0.1671 0.1892 0.2020 -0.0032 0.0168  0.0255  17   TYR   A CE2 
451  C  CZ  A TYR   A 17  ? 0.1854 0.1625 0.1740 -0.0252 -0.0026 0.0206  17   TYR   A CZ  
452  C  CZ  B TYR   A 17  ? 0.1700 0.1902 0.1994 0.0062  0.0083  0.0281  17   TYR   A CZ  
453  O  OH  A TYR   A 17  ? 0.1970 0.1637 0.1851 -0.0213 -0.0060 0.0229  17   TYR   A OH  
454  O  OH  B TYR   A 17  ? 0.1710 0.1907 0.2190 0.0139  0.0118  0.0313  17   TYR   A OH  
473  N  N   A ILE   A 18  ? 0.1434 0.1624 0.2110 -0.0281 0.0401  0.0666  18   ILE   A N   
474  N  N   B ILE   A 18  ? 0.1521 0.1598 0.2124 -0.0191 0.0127  0.0268  18   ILE   A N   
475  C  CA  A ILE   A 18  ? 0.1537 0.1752 0.2254 -0.0185 0.0460  0.0681  18   ILE   A CA  
476  C  CA  B ILE   A 18  ? 0.1514 0.1723 0.2236 -0.0209 0.0067  0.0300  18   ILE   A CA  
477  C  C   A ILE   A 18  ? 0.1585 0.1871 0.2382 -0.0189 0.0549  0.0678  18   ILE   A C   
478  C  C   B ILE   A 18  ? 0.1453 0.1807 0.2371 -0.0271 0.0104  0.0288  18   ILE   A C   
479  O  O   A ILE   A 18  ? 0.1548 0.1941 0.2455 -0.0216 0.0607  0.0636  18   ILE   A O   
480  O  O   B ILE   A 18  ? 0.1484 0.1858 0.2483 -0.0369 0.0201  0.0302  18   ILE   A O   
481  C  CB  A ILE   A 18  ? 0.1667 0.1839 0.2189 -0.0093 0.0478  0.0764  18   ILE   A CB  
482  C  CB  B ILE   A 18  ? 0.1572 0.1741 0.2136 -0.0129 -0.0037 0.0506  18   ILE   A CB  
483  C  CG1 A ILE   A 18  ? 0.1878 0.1995 0.2295 -0.0090 0.0387  0.0767  18   ILE   A CG1 
484  C  CG1 B ILE   A 18  ? 0.1727 0.1886 0.2251 -0.0047 -0.0192 0.0520  18   ILE   A CG1 
485  C  CG2 A ILE   A 18  ? 0.1670 0.1931 0.2287 -0.0085 0.0467  0.0649  18   ILE   A CG2 
486  C  CG2 B ILE   A 18  ? 0.1446 0.1633 0.2208 -0.0018 -0.0035 0.0449  18   ILE   A CG2 
487  C  CD1 A ILE   A 18  ? 0.2093 0.2166 0.2456 -0.0064 0.0293  0.0749  18   ILE   A CD1 
488  C  CD1 B ILE   A 18  ? 0.1935 0.2042 0.2381 -0.0008 -0.0230 0.0542  18   ILE   A CD1 
511  N  N   A LYS   A 19  ? 0.1634 0.1929 0.2401 -0.0163 0.0751  0.0704  19   LYS   A N   
512  N  N   B LYS   A 19  ? 0.1496 0.1897 0.2535 -0.0225 0.0259  0.0294  19   LYS   A N   
513  C  CA  A LYS   A 19  ? 0.1702 0.2035 0.2513 -0.0065 0.0819  0.0678  19   LYS   A CA  
514  C  CA  B LYS   A 19  ? 0.1653 0.2101 0.2683 -0.0142 0.0413  0.0242  19   LYS   A CA  
515  C  C   A LYS   A 19  ? 0.1661 0.1968 0.2740 0.0010  0.0712  0.0709  19   LYS   A C   
516  C  C   B LYS   A 19  ? 0.1552 0.2022 0.2749 -0.0065 0.0453  0.0251  19   LYS   A C   
517  O  O   A LYS   A 19  ? 0.1654 0.1846 0.2843 -0.0005 0.0593  0.0677  19   LYS   A O   
518  O  O   B LYS   A 19  ? 0.1419 0.1828 0.2652 -0.0121 0.0430  0.0227  19   LYS   A O   
519  C  CB  A LYS   A 19  ? 0.1824 0.2207 0.2514 -0.0108 0.0836  0.0589  19   LYS   A CB  
520  C  CB  B LYS   A 19  ? 0.1867 0.2349 0.2745 -0.0174 0.0420  0.0165  19   LYS   A CB  
521  C  CG  A LYS   A 19  ? 0.2034 0.2307 0.2367 -0.0114 0.0747  0.0595  19   LYS   A CG  
522  C  CG  B LYS   A 19  ? 0.2090 0.2547 0.2697 -0.0177 0.0378  0.0117  19   LYS   A CG  
523  C  CD  A LYS   A 19  ? 0.2210 0.2374 0.2280 -0.0058 0.0679  0.0563  19   LYS   A CD  
524  C  CD  B LYS   A 19  ? 0.2281 0.2687 0.2628 -0.0165 0.0357  0.0063  19   LYS   A CD  
525  C  CE  A LYS   A 19  ? 0.2306 0.2387 0.2305 -0.0024 0.0553  0.0421  19   LYS   A CE  
526  C  CE  B LYS   A 19  ? 0.2394 0.2766 0.2536 -0.0192 0.0365  0.0043  19   LYS   A CE  
527  N  NZ  A LYS   A 19  ? 0.2343 0.2392 0.2234 -0.0014 0.0558  0.0365  19   LYS   A NZ  
528  N  NZ  B LYS   A 19  ? 0.2469 0.2814 0.2423 -0.0175 0.0380  0.0001  19   LYS   A NZ  
555  N  N   A ASN   A 20  ? 0.1672 0.2053 0.2903 0.0005  0.0696  0.0782  20   ASN   A N   
556  N  N   B ASN   A 20  ? 0.1659 0.2153 0.3043 -0.0052 0.0464  0.0272  20   ASN   A N   
557  C  CA  A ASN   A 20  ? 0.1771 0.2184 0.3047 0.0126  0.0748  0.0653  20   ASN   A CA  
558  C  CA  B ASN   A 20  ? 0.1758 0.2280 0.3212 0.0097  0.0584  0.0156  20   ASN   A CA  
559  C  C   A ASN   A 20  ? 0.1869 0.2256 0.3033 0.0092  0.0791  0.0552  20   ASN   A C   
560  C  C   B ASN   A 20  ? 0.1906 0.2369 0.3166 0.0045  0.0737  0.0186  20   ASN   A C   
561  O  O   A ASN   A 20  ? 0.1938 0.2321 0.3006 0.0031  0.0780  0.0602  20   ASN   A O   
562  O  O   B ASN   A 20  ? 0.2030 0.2506 0.3178 0.0014  0.0710  0.0248  20   ASN   A O   
563  C  CB  A ASN   A 20  ? 0.1774 0.2191 0.3238 0.0220  0.0802  0.0637  20   ASN   A CB  
564  C  CB  B ASN   A 20  ? 0.1730 0.2292 0.3478 0.0179  0.0589  0.0077  20   ASN   A CB  
565  C  CG  A ASN   A 20  ? 0.1886 0.2183 0.3504 0.0285  0.0793  0.0567  20   ASN   A CG  
566  C  CG  B ASN   A 20  ? 0.1758 0.2319 0.3753 0.0215  0.0594  -0.0001 20   ASN   A CG  
567  O  OD1 A ASN   A 20  ? 0.2090 0.2258 0.3782 0.0307  0.0818  0.0368  20   ASN   A OD1 
568  O  OD1 B ASN   A 20  ? 0.1845 0.2332 0.3996 0.0203  0.0676  -0.0123 20   ASN   A OD1 
569  N  ND2 A ASN   A 20  ? 0.1883 0.2090 0.3553 0.0351  0.0756  0.0681  20   ASN   A ND2 
570  N  ND2 B ASN   A 20  ? 0.1868 0.2325 0.3910 0.0208  0.0481  0.0065  20   ASN   A ND2 
583  N  N   A ALA   A 21  ? 0.1910 0.2210 0.3050 0.0078  0.0690  0.0421  21   ALA   A N   
584  N  N   B ALA   A 21  ? 0.1942 0.2274 0.3082 0.0009  0.0716  0.0150  21   ALA   A N   
585  C  CA  A ALA   A 21  ? 0.1921 0.2159 0.2927 0.0079  0.0645  0.0436  21   ALA   A CA  
586  C  CA  B ALA   A 21  ? 0.2019 0.2236 0.2955 -0.0038 0.0707  0.0226  21   ALA   A CA  
587  C  C   A ALA   A 21  ? 0.1912 0.2092 0.2884 0.0069  0.0520  0.0335  21   ALA   A C   
588  C  C   B ALA   A 21  ? 0.1920 0.2110 0.2750 -0.0059 0.0747  0.0263  21   ALA   A C   
589  O  O   A ALA   A 21  ? 0.1932 0.2109 0.2926 0.0078  0.0476  0.0254  21   ALA   A O   
590  O  O   B ALA   A 21  ? 0.1881 0.2000 0.2804 -0.0018 0.0781  0.0249  21   ALA   A O   
591  C  CB  A ALA   A 21  ? 0.1978 0.2193 0.2980 0.0082  0.0665  0.0471  21   ALA   A CB  
592  C  CB  B ALA   A 21  ? 0.2166 0.2321 0.3171 0.0011  0.0588  0.0183  21   ALA   A CB  
603  N  N   A ASP   A 22  ? 0.1931 0.2060 0.2815 0.0020  0.0434  0.0359  22   ASP   A N   
604  N  N   B ASP   A 22  ? 0.1910 0.2119 0.2564 -0.0030 0.0752  0.0251  22   ASP   A N   
605  C  CA  A ASP   A 22  ? 0.1947 0.1994 0.2662 0.0070  0.0339  0.0361  22   ASP   A CA  
606  C  CA  B ASP   A 22  ? 0.1962 0.2117 0.2488 0.0001  0.0659  0.0153  22   ASP   A CA  
607  C  C   A ASP   A 22  ? 0.1835 0.1958 0.2296 0.0019  0.0433  0.0395  22   ASP   A C   
608  C  C   B ASP   A 22  ? 0.1790 0.1996 0.2074 -0.0155 0.0677  0.0160  22   ASP   A C   
609  O  O   A ASP   A 22  ? 0.1923 0.1977 0.2253 -0.0039 0.0492  0.0539  22   ASP   A O   
610  O  O   B ASP   A 22  ? 0.1808 0.1974 0.2042 -0.0192 0.0631  0.0055  22   ASP   A O   
611  C  CB  A ASP   A 22  ? 0.2106 0.1985 0.2959 0.0116  0.0294  0.0250  22   ASP   A CB  
612  C  CB  B ASP   A 22  ? 0.2104 0.2200 0.2713 0.0189  0.0775  0.0030  22   ASP   A CB  
613  C  CG  A ASP   A 22  ? 0.2222 0.1951 0.3196 0.0048  0.0150  0.0299  22   ASP   A CG  
614  C  CG  B ASP   A 22  ? 0.2181 0.2205 0.2949 0.0276  0.0798  0.0059  22   ASP   A CG  
615  O  OD1 A ASP   A 22  ? 0.2204 0.1823 0.3218 -0.0160 0.0016  0.0501  22   ASP   A OD1 
616  O  OD1 B ASP   A 22  ? 0.2222 0.2129 0.2841 0.0251  0.0867  0.0132  22   ASP   A OD1 
617  O  OD2 A ASP   A 22  ? 0.2299 0.2042 0.3459 0.0222  0.0167  0.0160  22   ASP   A OD2 
618  O  OD2 B ASP   A 22  ? 0.2251 0.2385 0.3289 0.0253  0.0737  0.0080  22   ASP   A OD2 
627  N  N   A ILE   A 23  ? 0.1799 0.1923 0.2136 0.0045  0.0438  0.0274  23   ILE   A N   
628  N  N   B ILE   A 23  ? 0.1711 0.1910 0.1920 -0.0089 0.0555  0.0189  23   ILE   A N   
629  C  CA  A ILE   A 23  ? 0.1797 0.1763 0.1990 0.0019  0.0423  0.0302  23   ILE   A CA  
630  C  CA  B ILE   A 23  ? 0.1651 0.1895 0.1823 -0.0071 0.0388  0.0195  23   ILE   A CA  
631  C  C   A ILE   A 23  ? 0.1807 0.1803 0.1942 -0.0006 0.0527  0.0236  23   ILE   A C   
632  C  C   B ILE   A 23  ? 0.1694 0.1896 0.1797 -0.0157 0.0386  0.0081  23   ILE   A C   
633  O  O   A ILE   A 23  ? 0.1941 0.1767 0.1981 -0.0011 0.0485  0.0290  23   ILE   A O   
634  O  O   B ILE   A 23  ? 0.1759 0.1859 0.1718 -0.0155 0.0393  0.0062  23   ILE   A O   
635  C  CB  A ILE   A 23  ? 0.1866 0.1692 0.1759 0.0050  0.0328  0.0304  23   ILE   A CB  
636  C  CB  B ILE   A 23  ? 0.1666 0.1837 0.1650 0.0020  0.0271  0.0230  23   ILE   A CB  
637  C  CG1 A ILE   A 23  ? 0.1892 0.1705 0.1766 0.0019  0.0345  0.0214  23   ILE   A CG1 
638  C  CG1 B ILE   A 23  ? 0.1665 0.1813 0.1523 0.0072  0.0148  0.0128  23   ILE   A CG1 
639  C  CG2 A ILE   A 23  ? 0.1889 0.1671 0.1697 0.0098  0.0253  0.0370  23   ILE   A CG2 
640  C  CG2 B ILE   A 23  ? 0.1688 0.1850 0.1777 0.0095  0.0201  0.0245  23   ILE   A CG2 
641  C  CD1 A ILE   A 23  ? 0.1889 0.1692 0.1840 0.0008  0.0292  0.0174  23   ILE   A CD1 
642  C  CD1 B ILE   A 23  ? 0.1642 0.1813 0.1483 0.0111  0.0101  0.0058  23   ILE   A CD1 
665  N  N   A VAL   A 24  ? 0.1845 0.1869 0.1998 -0.0016 0.0508  0.0145  24   VAL   A N   
666  N  N   B VAL   A 24  ? 0.1779 0.2016 0.2031 -0.0234 0.0381  0.0050  24   VAL   A N   
667  C  CA  A VAL   A 24  ? 0.1950 0.1935 0.2118 -0.0076 0.0438  0.0070  24   VAL   A CA  
668  C  CA  B VAL   A 24  ? 0.1914 0.2142 0.2237 -0.0236 0.0374  0.0039  24   VAL   A CA  
669  C  C   A VAL   A 24  ? 0.2038 0.2065 0.2132 -0.0147 0.0397  0.0084  24   VAL   A C   
670  C  C   B VAL   A 24  ? 0.2034 0.2321 0.2251 -0.0249 0.0502  -0.0073 24   VAL   A C   
671  O  O   A VAL   A 24  ? 0.2112 0.2119 0.2177 -0.0142 0.0398  0.0111  24   VAL   A O   
672  O  O   B VAL   A 24  ? 0.2038 0.2379 0.2315 -0.0187 0.0459  -0.0122 24   VAL   A O   
673  C  CB  A VAL   A 24  ? 0.1969 0.1924 0.2333 -0.0058 0.0445  0.0069  24   VAL   A CB  
674  C  CB  B VAL   A 24  ? 0.1937 0.2172 0.2560 -0.0243 0.0299  0.0183  24   VAL   A CB  
675  C  CG1 A VAL   A 24  ? 0.2014 0.1948 0.2474 -0.0008 0.0359  -0.0096 24   VAL   A CG1 
676  C  CG1 B VAL   A 24  ? 0.2032 0.2225 0.2807 -0.0204 0.0125  0.0168  24   VAL   A CG1 
677  C  CG2 A VAL   A 24  ? 0.2000 0.1962 0.2382 -0.0001 0.0587  0.0150  24   VAL   A CG2 
678  C  CG2 B VAL   A 24  ? 0.1975 0.2211 0.2630 -0.0193 0.0369  0.0247  24   VAL   A CG2 
697  N  N   A GLU   A 25  ? 0.2087 0.2235 0.2195 -0.0215 0.0462  -0.0026 25   GLU   A N   
698  N  N   B GLU   A 25  ? 0.2149 0.2443 0.2232 -0.0301 0.0774  -0.0091 25   GLU   A N   
699  C  CA  A GLU   A 25  ? 0.2214 0.2411 0.2167 -0.0217 0.0524  -0.0024 25   GLU   A CA  
700  C  CA  B GLU   A 25  ? 0.2336 0.2637 0.2323 -0.0393 0.0926  -0.0101 25   GLU   A CA  
701  C  C   A GLU   A 25  ? 0.2086 0.2425 0.1973 -0.0276 0.0594  0.0006  25   GLU   A C   
702  C  C   B GLU   A 25  ? 0.2304 0.2636 0.2132 -0.0430 0.0944  -0.0115 25   GLU   A C   
703  O  O   A GLU   A 25  ? 0.2121 0.2500 0.2060 -0.0211 0.0610  0.0031  25   GLU   A O   
704  O  O   B GLU   A 25  ? 0.2365 0.2622 0.2072 -0.0352 0.0977  -0.0301 25   GLU   A O   
705  C  CB  A GLU   A 25  ? 0.2452 0.2617 0.2443 -0.0199 0.0501  0.0034  25   GLU   A CB  
706  C  CB  B GLU   A 25  ? 0.2552 0.2785 0.2567 -0.0447 0.1088  -0.0027 25   GLU   A CB  
707  C  CG  A GLU   A 25  ? 0.2704 0.2798 0.2893 -0.0232 0.0373  -0.0019 25   GLU   A CG  
708  C  CG  B GLU   A 25  ? 0.2812 0.2946 0.2942 -0.0467 0.1030  -0.0045 25   GLU   A CG  
709  C  CD  A GLU   A 25  ? 0.2903 0.2935 0.3300 -0.0311 0.0276  -0.0040 25   GLU   A CD  
710  C  CD  B GLU   A 25  ? 0.3023 0.3061 0.3355 -0.0514 0.0901  -0.0029 25   GLU   A CD  
711  O  OE1 A GLU   A 25  ? 0.2988 0.2977 0.3414 -0.0329 0.0173  -0.0131 25   GLU   A OE1 
712  O  OE1 B GLU   A 25  ? 0.3129 0.3089 0.3520 -0.0519 0.0796  -0.0068 25   GLU   A OE1 
713  O  OE2 A GLU   A 25  ? 0.2950 0.3005 0.3597 -0.0359 0.0241  -0.0086 25   GLU   A OE2 
714  O  OE2 B GLU   A 25  ? 0.3127 0.3121 0.3604 -0.0517 0.0870  -0.0003 25   GLU   A OE2 
727  N  N   A GLU   A 26  ? 0.1967 0.2395 0.2039 -0.0409 0.0643  0.0023  26   GLU   A N   
728  N  N   B GLU   A 26  ? 0.2278 0.2656 0.2130 -0.0462 0.0881  -0.0142 26   GLU   A N   
729  C  CA  A GLU   A 26  ? 0.1996 0.2454 0.2085 -0.0552 0.0648  0.0083  26   GLU   A CA  
730  C  CA  B GLU   A 26  ? 0.2337 0.2674 0.2051 -0.0488 0.0866  -0.0120 26   GLU   A CA  
731  C  C   A GLU   A 26  ? 0.1960 0.2389 0.1874 -0.0573 0.0572  0.0091  26   GLU   A C   
732  C  C   B GLU   A 26  ? 0.2372 0.2621 0.1848 -0.0437 0.0788  -0.0116 26   GLU   A C   
733  O  O   A GLU   A 26  ? 0.2012 0.2286 0.1811 -0.0614 0.0449  0.0087  26   GLU   A O   
734  O  O   B GLU   A 26  ? 0.2428 0.2622 0.1856 -0.0411 0.0725  -0.0147 26   GLU   A O   
735  C  CB  A GLU   A 26  ? 0.2114 0.2526 0.2413 -0.0641 0.0654  0.0102  26   GLU   A CB  
736  C  CB  B GLU   A 26  ? 0.2425 0.2845 0.2371 -0.0531 0.0733  -0.0215 26   GLU   A CB  
737  C  CG  A GLU   A 26  ? 0.2317 0.2653 0.2894 -0.0669 0.0659  0.0016  26   GLU   A CG  
738  C  CG  B GLU   A 26  ? 0.2484 0.3020 0.2556 -0.0629 0.0808  -0.0166 26   GLU   A CG  
739  C  CD  A GLU   A 26  ? 0.2469 0.2739 0.3149 -0.0728 0.0738  -0.0028 26   GLU   A CD  
740  C  CD  B GLU   A 26  ? 0.2568 0.3158 0.2579 -0.0748 0.0892  -0.0087 26   GLU   A CD  
741  O  OE1 A GLU   A 26  ? 0.2446 0.2898 0.3209 -0.0624 0.0970  -0.0316 26   GLU   A OE1 
742  O  OE1 B GLU   A 26  ? 0.2610 0.3367 0.2546 -0.0711 0.1052  -0.0110 26   GLU   A OE1 
743  O  OE2 A GLU   A 26  ? 0.2652 0.2788 0.3142 -0.0728 0.0629  0.0070  26   GLU   A OE2 
744  O  OE2 B GLU   A 26  ? 0.2609 0.3141 0.2363 -0.0800 0.0947  -0.0085 26   GLU   A OE2 
757  N  N   A ALA   A 27  ? 0.1846 0.2404 0.1765 -0.0608 0.0605  0.0140  27   ALA   A N   
758  N  N   B ALA   A 27  ? 0.2331 0.2546 0.1774 -0.0466 0.0691  -0.0076 27   ALA   A N   
759  C  CA  A ALA   A 27  ? 0.1955 0.2524 0.1706 -0.0605 0.0562  0.0110  27   ALA   A CA  
760  C  CA  B ALA   A 27  ? 0.2401 0.2552 0.1745 -0.0504 0.0546  -0.0086 27   ALA   A CA  
761  C  C   A ALA   A 27  ? 0.2207 0.2740 0.1809 -0.0688 0.0582  0.0027  27   ALA   A C   
762  C  C   B ALA   A 27  ? 0.2610 0.2738 0.1811 -0.0540 0.0438  -0.0219 27   ALA   A C   
763  O  O   A ALA   A 27  ? 0.2240 0.2725 0.1913 -0.0738 0.0436  -0.0002 27   ALA   A O   
764  O  O   B ALA   A 27  ? 0.2644 0.2725 0.1791 -0.0588 0.0281  -0.0227 27   ALA   A O   
765  C  CB  A ALA   A 27  ? 0.1864 0.2443 0.1686 -0.0603 0.0438  0.0037  27   ALA   A CB  
766  C  CB  B ALA   A 27  ? 0.2318 0.2424 0.1830 -0.0510 0.0528  -0.0027 27   ALA   A CB  
777  N  N   A LYS   A 28  ? 0.2529 0.3012 0.1997 -0.0662 0.0583  -0.0161 28   LYS   A N   
778  N  N   B LYS   A 28  ? 0.2847 0.2978 0.2014 -0.0524 0.0355  -0.0424 28   LYS   A N   
779  C  CA  A LYS   A 28  ? 0.2910 0.3342 0.2394 -0.0590 0.0542  -0.0293 28   LYS   A CA  
780  C  CA  B LYS   A 28  ? 0.3126 0.3312 0.2327 -0.0464 0.0291  -0.0490 28   LYS   A CA  
781  C  C   A LYS   A 28  ? 0.3093 0.3605 0.2348 -0.0650 0.0700  -0.0204 28   LYS   A C   
782  C  C   B LYS   A 28  ? 0.3316 0.3578 0.2345 -0.0529 0.0393  -0.0420 28   LYS   A C   
783  O  O   A LYS   A 28  ? 0.3144 0.3689 0.2666 -0.0618 0.0573  -0.0183 28   LYS   A O   
784  O  O   B LYS   A 28  ? 0.3359 0.3665 0.2564 -0.0508 0.0253  -0.0428 28   LYS   A O   
785  C  CB  A LYS   A 28  ? 0.3088 0.3435 0.2856 -0.0445 0.0412  -0.0392 28   LYS   A CB  
786  C  CB  B LYS   A 28  ? 0.3243 0.3384 0.2632 -0.0352 0.0174  -0.0555 28   LYS   A CB  
787  C  CG  A LYS   A 28  ? 0.3251 0.3516 0.3264 -0.0324 0.0332  -0.0442 28   LYS   A CG  
788  C  CG  B LYS   A 28  ? 0.3367 0.3484 0.3059 -0.0232 0.0101  -0.0554 28   LYS   A CG  
789  C  CD  A LYS   A 28  ? 0.3372 0.3597 0.3662 -0.0247 0.0257  -0.0468 28   LYS   A CD  
790  C  CD  B LYS   A 28  ? 0.3491 0.3600 0.3567 -0.0141 -0.0013 -0.0538 28   LYS   A CD  
791  C  CE  A LYS   A 28  ? 0.3452 0.3655 0.3920 -0.0193 0.0190  -0.0501 28   LYS   A CE  
792  C  CE  B LYS   A 28  ? 0.3604 0.3683 0.3995 -0.0098 -0.0084 -0.0533 28   LYS   A CE  
793  N  NZ  A LYS   A 28  ? 0.3496 0.3677 0.4063 -0.0159 0.0200  -0.0508 28   LYS   A NZ  
794  N  NZ  B LYS   A 28  ? 0.3660 0.3717 0.4222 -0.0082 -0.0135 -0.0529 28   LYS   A NZ  
821  N  N   A LYS   A 29  ? 0.3209 0.3769 0.2159 -0.0763 0.0958  -0.0077 29   LYS   A N   
822  N  N   B LYS   A 29  ? 0.3437 0.3755 0.2315 -0.0647 0.0643  -0.0282 29   LYS   A N   
823  C  CA  A LYS   A 29  ? 0.3397 0.3952 0.2391 -0.0823 0.1045  0.0024  29   LYS   A CA  
824  C  CA  B LYS   A 29  ? 0.3594 0.3926 0.2539 -0.0751 0.0759  -0.0179 29   LYS   A CA  
825  C  C   A LYS   A 29  ? 0.3411 0.3885 0.2224 -0.0954 0.0968  0.0091  29   LYS   A C   
826  C  C   B LYS   A 29  ? 0.3577 0.3855 0.2297 -0.0911 0.0781  -0.0072 29   LYS   A C   
827  O  O   A LYS   A 29  ? 0.3474 0.3957 0.2375 -0.0903 0.0878  0.0054  29   LYS   A O   
828  O  O   B LYS   A 29  ? 0.3605 0.3872 0.2292 -0.0925 0.0827  -0.0010 29   LYS   A O   
829  C  CB  A LYS   A 29  ? 0.3546 0.4181 0.2904 -0.0726 0.1139  0.0028  29   LYS   A CB  
830  C  CB  B LYS   A 29  ? 0.3755 0.4153 0.3088 -0.0666 0.0791  -0.0192 29   LYS   A CB  
831  C  CG  A LYS   A 29  ? 0.3704 0.4371 0.3527 -0.0627 0.1132  0.0027  29   LYS   A CG  
832  C  CG  B LYS   A 29  ? 0.3916 0.4343 0.3680 -0.0591 0.0802  -0.0194 29   LYS   A CG  
833  C  CD  A LYS   A 29  ? 0.3859 0.4536 0.4153 -0.0543 0.1058  -0.0002 29   LYS   A CD  
834  C  CD  B LYS   A 29  ? 0.4045 0.4504 0.4220 -0.0537 0.0805  -0.0203 29   LYS   A CD  
835  C  CE  A LYS   A 29  ? 0.3964 0.4642 0.4584 -0.0493 0.1011  -0.0015 29   LYS   A CE  
836  C  CE  B LYS   A 29  ? 0.4133 0.4606 0.4607 -0.0504 0.0817  -0.0201 29   LYS   A CE  
837  N  NZ  A LYS   A 29  ? 0.4006 0.4698 0.4836 -0.0462 0.0981  -0.0036 29   LYS   A NZ  
838  N  NZ  B LYS   A 29  ? 0.4166 0.4659 0.4836 -0.0487 0.0828  -0.0204 29   LYS   A NZ  
865  N  N   A VAL   A 30  ? 0.3362 0.3746 0.2073 -0.1100 0.0883  0.0154  30   VAL   A N   
866  N  N   B VAL   A 30  ? 0.3511 0.3751 0.2132 -0.1048 0.0772  -0.0001 30   VAL   A N   
867  C  CA  A VAL   A 30  ? 0.3377 0.3616 0.1962 -0.1207 0.0678  0.0244  30   VAL   A CA  
868  C  CA  B VAL   A 30  ? 0.3497 0.3653 0.2010 -0.1150 0.0633  0.0086  30   VAL   A CA  
869  C  C   A VAL   A 30  ? 0.3451 0.3544 0.1704 -0.1195 0.0549  0.0236  30   VAL   A C   
870  C  C   B VAL   A 30  ? 0.3511 0.3563 0.1719 -0.1166 0.0532  0.0161  30   VAL   A C   
871  O  O   A VAL   A 30  ? 0.3518 0.3568 0.1747 -0.1182 0.0499  0.0224  30   VAL   A O   
872  O  O   B VAL   A 30  ? 0.3572 0.3585 0.1749 -0.1155 0.0491  0.0155  30   VAL   A O   
873  C  CB  A VAL   A 30  ? 0.3330 0.3578 0.2289 -0.1286 0.0495  0.0285  30   VAL   A CB  
874  C  CB  B VAL   A 30  ? 0.3468 0.3658 0.2333 -0.1213 0.0496  0.0058  30   VAL   A CB  
875  C  CG1 A VAL   A 30  ? 0.3351 0.3581 0.2462 -0.1280 0.0361  0.0272  30   VAL   A CG1 
876  C  CG1 B VAL   A 30  ? 0.3471 0.3672 0.2402 -0.1222 0.0454  0.0084  30   VAL   A CG1 
877  C  CG2 A VAL   A 30  ? 0.3296 0.3548 0.2407 -0.1339 0.0538  0.0375  30   VAL   A CG2 
878  C  CG2 B VAL   A 30  ? 0.3457 0.3643 0.2507 -0.1238 0.0495  0.0063  30   VAL   A CG2 
897  N  N   . LYS   A 31  ? 0.3431 0.3447 0.1492 -0.1203 0.0446  0.0174  31   LYS   A N   
898  C  CA  . LYS   A 31  ? 0.3582 0.3416 0.1531 -0.1078 0.0155  0.0187  31   LYS   A CA  
899  C  C   . LYS   A 31  ? 0.3332 0.3142 0.1246 -0.0921 0.0009  0.0492  31   LYS   A C   
900  O  O   . LYS   A 31  ? 0.3400 0.3188 0.1530 -0.0858 -0.0160 0.0592  31   LYS   A O   
901  C  CB  . LYS   A 31  ? 0.4047 0.3715 0.2532 -0.1012 -0.0024 -0.0044 31   LYS   A CB  
902  C  CG  . LYS   A 31  ? 0.4491 0.4032 0.3880 -0.0877 -0.0206 -0.0193 31   LYS   A CG  
903  C  CD  . LYS   A 31  ? 0.4865 0.4309 0.4919 -0.0770 -0.0352 -0.0311 31   LYS   A CD  
904  C  CE  . LYS   A 31  ? 0.5102 0.4485 0.5549 -0.0693 -0.0480 -0.0430 31   LYS   A CE  
905  N  NZ  . LYS   A 31  ? 0.5271 0.4559 0.5877 -0.0652 -0.0542 -0.0507 31   LYS   A NZ  
920  N  N   . PRO   A 32  ? 0.2970 0.2813 0.1098 -0.0847 0.0035  0.0411  32   PRO   A N   
921  C  CA  . PRO   A 32  ? 0.2890 0.2615 0.1564 -0.0789 -0.0125 0.0525  32   PRO   A CA  
922  C  C   . PRO   A 32  ? 0.2784 0.2512 0.1617 -0.0654 -0.0193 0.0570  32   PRO   A C   
923  O  O   . PRO   A 32  ? 0.2697 0.2442 0.1579 -0.0642 -0.0341 0.0576  32   PRO   A O   
924  C  CB  . PRO   A 32  ? 0.2803 0.2660 0.1663 -0.0811 -0.0222 0.0449  32   PRO   A CB  
925  C  CG  . PRO   A 32  ? 0.2754 0.2691 0.1184 -0.0785 -0.0257 0.0319  32   PRO   A CG  
926  C  CD  . PRO   A 32  ? 0.2817 0.2667 0.1102 -0.0861 -0.0100 0.0379  32   PRO   A CD  
934  N  N   . THR   A 33  ? 0.2823 0.2495 0.1527 -0.0566 -0.0202 0.0620  33   THR   A N   
935  C  CA  . THR   A 33  ? 0.2774 0.2462 0.1575 -0.0427 -0.0369 0.0587  33   THR   A CA  
936  C  C   . THR   A 33  ? 0.2449 0.2304 0.1541 -0.0463 -0.0368 0.0491  33   THR   A C   
937  O  O   . THR   A 33  ? 0.2354 0.2325 0.1709 -0.0478 -0.0487 0.0488  33   THR   A O   
938  C  CB  . THR   A 33  ? 0.3009 0.2604 0.1696 -0.0286 -0.0415 0.0741  33   THR   A CB  
939  O  OG1 . THR   A 33  ? 0.3211 0.2682 0.2010 -0.0101 -0.0305 0.0827  33   THR   A OG1 
940  C  CG2 . THR   A 33  ? 0.3048 0.2690 0.2036 -0.0223 -0.0436 0.0740  33   THR   A CG2 
948  N  N   . VAL   A 34  ? 0.2145 0.2133 0.1399 -0.0445 -0.0292 0.0460  34   VAL   A N   
949  C  CA  . VAL   A 34  ? 0.1938 0.1943 0.1265 -0.0339 -0.0207 0.0419  34   VAL   A CA  
950  C  C   . VAL   A 34  ? 0.1781 0.1888 0.1267 -0.0305 -0.0113 0.0347  34   VAL   A C   
951  O  O   . VAL   A 34  ? 0.1824 0.1834 0.1455 -0.0401 -0.0076 0.0392  34   VAL   A O   
952  C  CB  . VAL   A 34  ? 0.1933 0.1879 0.1443 -0.0325 -0.0102 0.0322  34   VAL   A CB  
953  C  CG1 . VAL   A 34  ? 0.1976 0.1882 0.1488 -0.0298 -0.0044 0.0122  34   VAL   A CG1 
954  C  CG2 . VAL   A 34  ? 0.2015 0.2040 0.1715 -0.0217 -0.0207 0.0373  34   VAL   A CG2 
964  N  N   . VAL   A 35  ? 0.1669 0.1746 0.1297 -0.0351 -0.0086 0.0285  35   VAL   A N   
965  C  CA  . VAL   A 35  ? 0.1581 0.1715 0.1253 -0.0310 -0.0003 0.0195  35   VAL   A CA  
966  C  C   . VAL   A 35  ? 0.1520 0.1588 0.1168 -0.0228 -0.0011 0.0191  35   VAL   A C   
967  O  O   . VAL   A 35  ? 0.1449 0.1649 0.1334 -0.0247 0.0101  0.0148  35   VAL   A O   
968  C  CB  . VAL   A 35  ? 0.1620 0.1770 0.1460 -0.0198 0.0131  0.0084  35   VAL   A CB  
969  C  CG1 . VAL   A 35  ? 0.1731 0.1764 0.1501 -0.0090 0.0049  0.0062  35   VAL   A CG1 
970  C  CG2 . VAL   A 35  ? 0.1567 0.1784 0.1699 -0.0134 0.0150  0.0068  35   VAL   A CG2 
980  N  N   . VAL   A 36  ? 0.1385 0.1515 0.1173 -0.0235 0.0035  0.0228  36   VAL   A N   
981  C  CA  . VAL   A 36  ? 0.1316 0.1353 0.1290 -0.0173 -0.0038 0.0167  36   VAL   A CA  
982  C  C   . VAL   A 36  ? 0.1268 0.1400 0.1282 -0.0193 0.0018  0.0150  36   VAL   A C   
983  O  O   . VAL   A 36  ? 0.1314 0.1368 0.1519 -0.0100 0.0186  0.0142  36   VAL   A O   
984  C  CB  . VAL   A 36  ? 0.1326 0.1279 0.1405 -0.0151 -0.0035 0.0202  36   VAL   A CB  
985  C  CG1 . VAL   A 36  ? 0.1354 0.1332 0.1515 -0.0198 -0.0004 0.0098  36   VAL   A CG1 
986  C  CG2 . VAL   A 36  ? 0.1439 0.1362 0.1662 -0.0103 -0.0052 0.0150  36   VAL   A CG2 
996  N  N   . ASN   A 37  ? 0.1188 0.1329 0.1176 -0.0107 0.0010  0.0172  37   ASN   A N   
997  C  CA  . ASN   A 37  ? 0.1160 0.1256 0.1236 -0.0007 0.0014  0.0120  37   ASN   A CA  
998  C  C   . ASN   A 37  ? 0.1208 0.1229 0.1250 -0.0054 0.0055  0.0243  37   ASN   A C   
999  O  O   . ASN   A 37  ? 0.1311 0.1339 0.1090 0.0006  0.0057  0.0083  37   ASN   A O   
1000 C  CB  . ASN   A 37  ? 0.1210 0.1255 0.1311 -0.0004 0.0073  0.0072  37   ASN   A CB  
1001 C  CG  . ASN   A 37  ? 0.1240 0.1240 0.1399 0.0054  0.0114  0.0133  37   ASN   A CG  
1002 O  OD1 . ASN   A 37  ? 0.1256 0.1253 0.1501 -0.0035 0.0071  0.0140  37   ASN   A OD1 
1003 N  ND2 . ASN   A 37  ? 0.1260 0.1265 0.1385 -0.0022 -0.0015 0.0215  37   ASN   A ND2 
1010 N  N   A ALA   A 38  ? 0.1200 0.1293 0.1328 -0.0018 0.0065  0.0032  38   ALA   A N   
1011 N  N   B ALA   A 38  ? 0.1247 0.1312 0.1377 -0.0022 0.0045  0.0118  38   ALA   A N   
1012 C  CA  A ALA   A 38  ? 0.1195 0.1261 0.1215 -0.0010 -0.0038 -0.0098 38   ALA   A CA  
1013 C  CA  B ALA   A 38  ? 0.1306 0.1348 0.1349 -0.0055 -0.0067 0.0135  38   ALA   A CA  
1014 C  C   A ALA   A 38  ? 0.1220 0.1272 0.1171 -0.0004 -0.0058 -0.0203 38   ALA   A C   
1015 C  C   B ALA   A 38  ? 0.1309 0.1355 0.1286 -0.0003 -0.0153 0.0126  38   ALA   A C   
1016 O  O   A ALA   A 38  ? 0.1184 0.1177 0.1245 -0.0009 -0.0136 -0.0248 38   ALA   A O   
1017 O  O   B ALA   A 38  ? 0.1234 0.1295 0.1326 -0.0010 -0.0202 0.0113  38   ALA   A O   
1018 C  CB  A ALA   A 38  ? 0.1183 0.1400 0.1383 -0.0115 -0.0021 -0.0053 38   ALA   A CB  
1019 C  CB  B ALA   A 38  ? 0.1353 0.1391 0.1560 -0.0115 -0.0086 0.0039  38   ALA   A CB  
1030 N  N   A ALA   A 39  ? 0.1213 0.1231 0.1179 0.0012  0.0038  -0.0109 39   ALA   A N   
1031 N  N   B ALA   A 39  ? 0.1347 0.1385 0.1415 -0.0010 -0.0074 0.0208  39   ALA   A N   
1032 C  CA  A ALA   A 39  ? 0.1167 0.1168 0.1183 0.0016  0.0068  -0.0106 39   ALA   A CA  
1033 C  CA  B ALA   A 39  ? 0.1374 0.1384 0.1455 -0.0039 -0.0064 0.0160  39   ALA   A CA  
1034 C  C   A ALA   A 39  ? 0.1244 0.1219 0.1217 0.0023  0.0050  -0.0016 39   ALA   A C   
1035 C  C   B ALA   A 39  ? 0.1365 0.1310 0.1357 -0.0024 -0.0002 0.0113  39   ALA   A C   
1036 O  O   A ALA   A 39  ? 0.1352 0.1269 0.1244 -0.0049 0.0103  0.0036  39   ALA   A O   
1037 O  O   B ALA   A 39  ? 0.1493 0.1345 0.1401 -0.0062 -0.0027 0.0074  39   ALA   A O   
1038 C  CB  A ALA   A 39  ? 0.1109 0.1189 0.1280 0.0040  -0.0028 -0.0108 39   ALA   A CB  
1039 C  CB  B ALA   A 39  ? 0.1462 0.1506 0.1563 -0.0046 -0.0146 0.0093  39   ALA   A CB  
1050 N  N   A ASN   A 40  ? 0.1299 0.1273 0.1289 -0.0040 0.0084  0.0009  40   ASN   A N   
1051 N  N   B ASN   A 40  ? 0.1396 0.1272 0.1350 -0.0058 0.0182  0.0123  40   ASN   A N   
1052 C  CA  A ASN   A 40  ? 0.1400 0.1272 0.1324 -0.0025 -0.0016 -0.0014 40   ASN   A CA  
1053 C  CA  B ASN   A 40  ? 0.1455 0.1222 0.1451 -0.0032 0.0140  0.0122  40   ASN   A CA  
1054 C  C   A ASN   A 40  ? 0.1406 0.1212 0.1170 -0.0031 0.0074  0.0032  40   ASN   A C   
1055 C  C   B ASN   A 40  ? 0.1489 0.1139 0.1377 -0.0046 0.0254  0.0195  40   ASN   A C   
1056 O  O   A ASN   A 40  ? 0.1392 0.1254 0.1227 -0.0044 0.0049  0.0052  40   ASN   A O   
1057 O  O   B ASN   A 40  ? 0.1391 0.1151 0.1452 -0.0106 0.0243  0.0259  40   ASN   A O   
1058 C  CB  A ASN   A 40  ? 0.1530 0.1340 0.1375 0.0062  -0.0172 0.0030  40   ASN   A CB  
1059 C  CB  B ASN   A 40  ? 0.1555 0.1282 0.1605 -0.0032 0.0043  0.0082  40   ASN   A CB  
1060 C  CG  A ASN   A 40  ? 0.1632 0.1361 0.1621 0.0089  -0.0175 0.0147  40   ASN   A CG  
1061 C  CG  B ASN   A 40  ? 0.1569 0.1353 0.1810 -0.0090 0.0052  0.0068  40   ASN   A CG  
1062 O  OD1 A ASN   A 40  ? 0.1699 0.1330 0.1923 0.0151  -0.0250 0.0144  40   ASN   A OD1 
1063 O  OD1 B ASN   A 40  ? 0.1658 0.1441 0.1996 -0.0107 0.0111  -0.0002 40   ASN   A OD1 
1064 N  ND2 A ASN   A 40  ? 0.1640 0.1431 0.1636 0.0079  -0.0023 0.0096  40   ASN   A ND2 
1065 N  ND2 B ASN   A 40  ? 0.1487 0.1417 0.1934 -0.0146 0.0182  -0.0075 40   ASN   A ND2 
1078 N  N   A VAL   A 41  ? 0.1476 0.1226 0.1170 -0.0024 0.0113  0.0106  41   VAL   A N   
1079 N  N   B VAL   A 41  ? 0.1591 0.1170 0.1405 0.0022  0.0261  0.0210  41   VAL   A N   
1080 C  CA  A VAL   A 41  ? 0.1456 0.1311 0.1347 -0.0023 0.0174  0.0132  41   VAL   A CA  
1081 C  CA  B VAL   A 41  ? 0.1648 0.1278 0.1536 -0.0013 0.0351  0.0130  41   VAL   A CA  
1082 C  C   A VAL   A 41  ? 0.1492 0.1308 0.1573 -0.0045 0.0204  0.0130  41   VAL   A C   
1083 C  C   B VAL   A 41  ? 0.1583 0.1223 0.1538 -0.0038 0.0381  0.0110  41   VAL   A C   
1084 O  O   A VAL   A 41  ? 0.1534 0.1288 0.1797 0.0019  0.0100  0.0038  41   VAL   A O   
1085 O  O   B VAL   A 41  ? 0.1603 0.1065 0.1592 -0.0001 0.0413  -0.0005 41   VAL   A O   
1086 C  CB  A VAL   A 41  ? 0.1475 0.1355 0.1328 -0.0056 0.0276  0.0058  41   VAL   A CB  
1087 C  CB  B VAL   A 41  ? 0.1823 0.1390 0.1629 -0.0073 0.0471  0.0152  41   VAL   A CB  
1088 C  CG1 A VAL   A 41  ? 0.1639 0.1452 0.1458 -0.0034 0.0225  -0.0056 41   VAL   A CG1 
1089 C  CG1 B VAL   A 41  ? 0.1958 0.1453 0.1789 -0.0106 0.0511  0.0045  41   VAL   A CG1 
1090 C  CG2 A VAL   A 41  ? 0.1353 0.1315 0.1137 -0.0044 0.0377  0.0062  41   VAL   A CG2 
1091 C  CG2 B VAL   A 41  ? 0.1885 0.1468 0.1649 -0.0045 0.0381  0.0162  41   VAL   A CG2 
1110 N  N   . TYR   A 42  ? 0.1457 0.1243 0.1628 -0.0027 0.0299  0.0161  42   TYR   A N   
1111 C  CA  . TYR   A 42  ? 0.1467 0.1209 0.1687 -0.0044 0.0350  0.0228  42   TYR   A CA  
1112 C  C   . TYR   A 42  ? 0.1368 0.1226 0.1696 0.0001  0.0280  0.0246  42   TYR   A C   
1113 O  O   . TYR   A 42  ? 0.1338 0.1268 0.1886 -0.0126 0.0217  0.0015  42   TYR   A O   
1114 C  CB  . TYR   A 42  ? 0.1690 0.1261 0.1681 -0.0076 0.0277  0.0227  42   TYR   A CB  
1115 C  CG  . TYR   A 42  ? 0.1938 0.1418 0.1626 -0.0082 0.0254  0.0266  42   TYR   A CG  
1116 C  CD1 . TYR   A 42  ? 0.2063 0.1516 0.1710 -0.0090 0.0295  0.0272  42   TYR   A CD1 
1117 C  CD2 . TYR   A 42  ? 0.2067 0.1666 0.1791 -0.0042 0.0160  0.0232  42   TYR   A CD2 
1118 C  CE1 . TYR   A 42  ? 0.2170 0.1649 0.1656 -0.0167 0.0353  0.0241  42   TYR   A CE1 
1119 C  CE2 . TYR   A 42  ? 0.2223 0.1783 0.1908 -0.0201 0.0192  0.0208  42   TYR   A CE2 
1120 C  CZ  . TYR   A 42  ? 0.2321 0.1797 0.1649 -0.0264 0.0338  0.0277  42   TYR   A CZ  
1121 O  OH  . TYR   A 42  ? 0.2427 0.2076 0.2013 -0.0383 0.0370  0.0179  42   TYR   A OH  
1132 N  N   . LEU   A 43  ? 0.1387 0.1234 0.1505 -0.0067 0.0156  0.0086  43   LEU   A N   
1133 C  CA  . LEU   A 43  ? 0.1289 0.1213 0.1444 -0.0083 0.0115  0.0149  43   LEU   A CA  
1134 C  C   . LEU   A 43  ? 0.1271 0.1265 0.1450 -0.0034 0.0096  0.0013  43   LEU   A C   
1135 O  O   . LEU   A 43  ? 0.1446 0.1251 0.1717 0.0027  -0.0057 0.0003  43   LEU   A O   
1136 C  CB  . LEU   A 43  ? 0.1362 0.1182 0.1514 -0.0092 0.0125  0.0030  43   LEU   A CB  
1137 C  CG  . LEU   A 43  ? 0.1411 0.1237 0.1666 -0.0065 -0.0012 0.0022  43   LEU   A CG  
1138 C  CD1 . LEU   A 43  ? 0.1422 0.1320 0.1989 -0.0047 -0.0092 0.0172  43   LEU   A CD1 
1139 C  CD2 . LEU   A 43  ? 0.1494 0.1250 0.1536 -0.0049 -0.0009 0.0135  43   LEU   A CD2 
1151 N  N   A LYS   A 44  ? 0.1356 0.1277 0.1431 -0.0055 0.0053  0.0052  44   LYS   A N   
1152 N  N   B LYS   A 44  ? 0.1340 0.1265 0.1441 0.0010  0.0022  0.0067  44   LYS   A N   
1153 C  CA  A LYS   A 44  ? 0.1447 0.1290 0.1554 -0.0073 0.0128  0.0177  44   LYS   A CA  
1154 C  CA  B LYS   A 44  ? 0.1406 0.1261 0.1566 0.0049  0.0078  0.0167  44   LYS   A CA  
1155 C  C   A LYS   A 44  ? 0.1365 0.1267 0.1427 0.0007  0.0017  0.0043  44   LYS   A C   
1156 C  C   B LYS   A 44  ? 0.1322 0.1249 0.1458 0.0047  -0.0002 0.0083  44   LYS   A C   
1157 O  O   A LYS   A 44  ? 0.1475 0.1386 0.1581 0.0018  0.0028  -0.0097 44   LYS   A O   
1158 O  O   B LYS   A 44  ? 0.1392 0.1347 0.1623 -0.0011 0.0022  0.0042  44   LYS   A O   
1159 C  CB  A LYS   A 44  ? 0.1795 0.1433 0.1946 -0.0154 0.0263  0.0301  44   LYS   A CB  
1160 C  CB  B LYS   A 44  ? 0.1745 0.1394 0.2026 0.0084  0.0240  0.0214  44   LYS   A CB  
1161 C  CG  A LYS   A 44  ? 0.2117 0.1712 0.2569 -0.0220 0.0397  0.0336  44   LYS   A CG  
1162 C  CG  B LYS   A 44  ? 0.2026 0.1704 0.2705 0.0088  0.0370  0.0195  44   LYS   A CG  
1163 C  CD  A LYS   A 44  ? 0.2479 0.2166 0.3489 -0.0222 0.0316  0.0221  44   LYS   A CD  
1164 C  CD  B LYS   A 44  ? 0.2376 0.2179 0.3569 0.0010  0.0235  0.0159  44   LYS   A CD  
1165 C  CE  A LYS   A 44  ? 0.2673 0.2447 0.4098 -0.0187 0.0315  0.0167  44   LYS   A CE  
1166 C  CE  B LYS   A 44  ? 0.2527 0.2456 0.4118 -0.0023 0.0155  0.0153  44   LYS   A CE  
1167 N  NZ  A LYS   A 44  ? 0.2771 0.2655 0.4414 -0.0163 0.0294  0.0132  44   LYS   A NZ  
1168 N  NZ  B LYS   A 44  ? 0.2622 0.2644 0.4421 -0.0049 0.0125  0.0130  44   LYS   A NZ  
1195 N  N   . HIS   A 45  ? 0.1270 0.1241 0.1419 -0.0002 0.0015  0.0120  45   HIS   A N   
1196 C  CA  . HIS   A 45  ? 0.1290 0.1294 0.1462 0.0024  -0.0025 0.0078  45   HIS   A CA  
1197 C  C   . HIS   A 45  ? 0.1326 0.1385 0.1493 0.0027  -0.0045 0.0097  45   HIS   A C   
1198 O  O   . HIS   A 45  ? 0.1524 0.1535 0.1803 0.0198  -0.0047 -0.0079 45   HIS   A O   
1199 C  CB  . HIS   A 45  ? 0.1316 0.1290 0.1464 0.0029  -0.0017 -0.0026 45   HIS   A CB  
1200 C  CG  . HIS   A 45  ? 0.1265 0.1241 0.1346 -0.0043 0.0020  0.0050  45   HIS   A CG  
1201 N  ND1 . HIS   A 45  ? 0.1208 0.1262 0.1613 -0.0053 0.0029  0.0115  45   HIS   A ND1 
1202 C  CD2 . HIS   A 45  ? 0.1282 0.1288 0.1440 -0.0096 -0.0026 0.0154  45   HIS   A CD2 
1203 C  CE1 . HIS   A 45  ? 0.1191 0.1309 0.1404 -0.0106 -0.0048 0.0192  45   HIS   A CE1 
1204 N  NE2 . HIS   A 45  ? 0.1233 0.1338 0.1465 -0.0071 0.0015  0.0223  45   HIS   A NE2 
1213 N  N   . GLY   A 46  ? 0.1445 0.1428 0.1671 0.0051  -0.0149 0.0188  46   GLY   A N   
1214 C  CA  . GLY   A 46  ? 0.1503 0.1493 0.1852 0.0091  -0.0161 0.0242  46   GLY   A CA  
1215 C  C   . GLY   A 46  ? 0.1484 0.1461 0.1859 0.0178  -0.0220 0.0269  46   GLY   A C   
1216 O  O   . GLY   A 46  ? 0.1589 0.1541 0.2309 0.0213  -0.0351 0.0093  46   GLY   A O   
1220 N  N   A GLY   A 47  ? 0.1506 0.1455 0.1791 0.0205  -0.0233 0.0209  47   GLY   A N   
1221 N  N   B GLY   A 47  ? 0.1527 0.1468 0.1811 0.0160  -0.0185 0.0239  47   GLY   A N   
1222 C  CA  A GLY   A 47  ? 0.1535 0.1518 0.1786 0.0172  -0.0373 0.0120  47   GLY   A CA  
1223 C  CA  B GLY   A 47  ? 0.1574 0.1540 0.1843 0.0080  -0.0253 0.0179  47   GLY   A CA  
1224 C  C   A GLY   A 47  ? 0.1501 0.1418 0.1505 0.0216  -0.0331 0.0018  47   GLY   A C   
1225 C  C   B GLY   A 47  ? 0.1557 0.1448 0.1627 0.0073  -0.0189 0.0075  47   GLY   A C   
1226 O  O   A GLY   A 47  ? 0.1486 0.1405 0.1455 0.0346  -0.0324 -0.0026 47   GLY   A O   
1227 O  O   B GLY   A 47  ? 0.1546 0.1428 0.1634 0.0114  -0.0175 0.0263  47   GLY   A O   
1234 N  N   A GLY   A 48  ? 0.1443 0.1389 0.1350 0.0215  -0.0349 0.0037  48   GLY   A N   
1235 N  N   B GLY   A 48  ? 0.1547 0.1438 0.1553 0.0064  -0.0162 0.0002  48   GLY   A N   
1236 C  CA  A GLY   A 48  ? 0.1417 0.1344 0.1552 0.0088  -0.0242 0.0012  48   GLY   A CA  
1237 C  CA  B GLY   A 48  ? 0.1490 0.1371 0.1423 0.0049  -0.0107 -0.0111 48   GLY   A CA  
1238 C  C   A GLY   A 48  ? 0.1326 0.1282 0.1351 -0.0041 -0.0127 -0.0028 48   GLY   A C   
1239 C  C   B GLY   A 48  ? 0.1419 0.1389 0.1449 0.0029  -0.0013 -0.0032 48   GLY   A C   
1240 O  O   A GLY   A 48  ? 0.1428 0.1276 0.1440 0.0017  -0.0245 -0.0112 48   GLY   A O   
1241 O  O   B GLY   A 48  ? 0.1512 0.1390 0.1458 0.0088  0.0019  -0.0067 48   GLY   A O   
1248 N  N   A VAL   A 49  ? 0.1276 0.1255 0.1597 -0.0119 -0.0095 0.0025  49   VAL   A N   
1249 N  N   B VAL   A 49  ? 0.1288 0.1361 0.1407 -0.0005 -0.0038 -0.0033 49   VAL   A N   
1250 C  CA  A VAL   A 49  ? 0.1377 0.1212 0.1567 -0.0129 -0.0001 -0.0004 49   VAL   A CA  
1251 C  CA  B VAL   A 49  ? 0.1277 0.1406 0.1304 -0.0022 0.0077  -0.0002 49   VAL   A CA  
1252 C  C   A VAL   A 49  ? 0.1363 0.1148 0.1511 -0.0051 -0.0029 0.0101  49   VAL   A C   
1253 C  C   B VAL   A 49  ? 0.1262 0.1370 0.1156 0.0037  0.0101  -0.0185 49   VAL   A C   
1254 O  O   A VAL   A 49  ? 0.1354 0.1175 0.1663 -0.0150 -0.0013 0.0081  49   VAL   A O   
1255 O  O   B VAL   A 49  ? 0.1276 0.1400 0.1152 0.0043  0.0120  -0.0132 49   VAL   A O   
1256 C  CB  A VAL   A 49  ? 0.1457 0.1235 0.1827 -0.0154 0.0018  -0.0080 49   VAL   A CB  
1257 C  CB  B VAL   A 49  ? 0.1257 0.1421 0.1539 0.0015  -0.0016 0.0104  49   VAL   A CB  
1258 C  CG1 A VAL   A 49  ? 0.1489 0.1214 0.2005 -0.0106 0.0152  0.0027  49   VAL   A CG1 
1259 C  CG1 B VAL   A 49  ? 0.1098 0.1350 0.1492 0.0134  0.0004  0.0227  49   VAL   A CG1 
1260 C  CG2 A VAL   A 49  ? 0.1513 0.1291 0.2159 -0.0231 -0.0075 -0.0103 49   VAL   A CG2 
1261 C  CG2 B VAL   A 49  ? 0.1401 0.1502 0.1784 -0.0024 -0.0166 0.0148  49   VAL   A CG2 
1280 N  N   A ALA   A 50  ? 0.1308 0.1104 0.1516 -0.0036 -0.0179 0.0205  50   ALA   A N   
1281 N  N   B ALA   A 50  ? 0.1214 0.1327 0.1211 0.0003  -0.0012 -0.0214 50   ALA   A N   
1282 C  CA  A ALA   A 50  ? 0.1277 0.1156 0.1475 -0.0018 -0.0091 0.0249  50   ALA   A CA  
1283 C  CA  B ALA   A 50  ? 0.1177 0.1329 0.1252 -0.0055 0.0074  -0.0177 50   ALA   A CA  
1284 C  C   A ALA   A 50  ? 0.1218 0.1195 0.1455 -0.0016 -0.0061 0.0107  50   ALA   A C   
1285 C  C   B ALA   A 50  ? 0.1150 0.1353 0.1142 -0.0046 0.0091  -0.0142 50   ALA   A C   
1286 O  O   A ALA   A 50  ? 0.1240 0.1177 0.1723 -0.0006 -0.0205 0.0176  50   ALA   A O   
1287 O  O   B ALA   A 50  ? 0.1198 0.1393 0.1118 -0.0028 0.0088  -0.0116 50   ALA   A O   
1288 C  CB  A ALA   A 50  ? 0.1259 0.1204 0.1523 -0.0022 -0.0108 0.0327  50   ALA   A CB  
1289 C  CB  B ALA   A 50  ? 0.1163 0.1318 0.1384 -0.0080 0.0178  -0.0309 50   ALA   A CB  
1300 N  N   A GLY   A 51  ? 0.1269 0.1138 0.1455 0.0052  -0.0122 -0.0012 51   GLY   A N   
1301 N  N   B GLY   A 51  ? 0.1272 0.1270 0.1426 0.0001  -0.0103 -0.0112 51   GLY   A N   
1302 C  CA  A GLY   A 51  ? 0.1356 0.1157 0.1414 0.0069  -0.0042 0.0004  51   GLY   A CA  
1303 C  CA  B GLY   A 51  ? 0.1360 0.1265 0.1370 0.0036  -0.0180 -0.0122 51   GLY   A CA  
1304 C  C   A GLY   A 51  ? 0.1266 0.1192 0.1228 0.0058  0.0001  -0.0019 51   GLY   A C   
1305 C  C   B GLY   A 51  ? 0.1291 0.1317 0.1547 0.0086  -0.0107 -0.0107 51   GLY   A C   
1306 O  O   A GLY   A 51  ? 0.1259 0.1225 0.1220 0.0073  -0.0217 0.0068  51   GLY   A O   
1307 O  O   B GLY   A 51  ? 0.1343 0.1327 0.1555 0.0057  -0.0118 0.0080  51   GLY   A O   
1314 N  N   A ALA   A 52  ? 0.1242 0.1247 0.1314 -0.0002 0.0047  -0.0053 52   ALA   A N   
1315 N  N   B ALA   A 52  ? 0.1254 0.1361 0.1655 0.0020  -0.0073 -0.0128 52   ALA   A N   
1316 C  CA  A ALA   A 52  ? 0.1280 0.1318 0.1467 -0.0013 0.0076  0.0028  52   ALA   A CA  
1317 C  CA  B ALA   A 52  ? 0.1276 0.1370 0.1724 0.0010  -0.0060 -0.0068 52   ALA   A CA  
1318 C  C   A ALA   A 52  ? 0.1292 0.1331 0.1216 -0.0054 0.0069  -0.0030 52   ALA   A C   
1319 C  C   B ALA   A 52  ? 0.1250 0.1383 0.1568 -0.0011 0.0034  -0.0103 52   ALA   A C   
1320 O  O   A ALA   A 52  ? 0.1377 0.1407 0.1265 -0.0026 -0.0035 -0.0050 52   ALA   A O   
1321 O  O   B ALA   A 52  ? 0.1343 0.1289 0.1824 -0.0003 0.0093  -0.0031 52   ALA   A O   
1322 C  CB  A ALA   A 52  ? 0.1369 0.1393 0.1594 -0.0029 0.0098  0.0089  52   ALA   A CB  
1323 C  CB  B ALA   A 52  ? 0.1268 0.1423 0.1856 -0.0052 -0.0148 -0.0031 52   ALA   A CB  
1334 N  N   A LEU   A 53  ? 0.1234 0.1319 0.1223 -0.0095 0.0000  -0.0074 53   LEU   A N   
1335 N  N   B LEU   A 53  ? 0.1208 0.1453 0.1394 0.0040  0.0030  -0.0085 53   LEU   A N   
1336 C  CA  A LEU   A 53  ? 0.1296 0.1420 0.1309 -0.0053 0.0050  -0.0058 53   LEU   A CA  
1337 C  CA  B LEU   A 53  ? 0.1252 0.1524 0.1258 0.0048  -0.0001 -0.0021 53   LEU   A CA  
1338 C  C   A LEU   A 53  ? 0.1303 0.1446 0.1154 -0.0007 -0.0003 -0.0061 53   LEU   A C   
1339 C  C   B LEU   A 53  ? 0.1286 0.1537 0.1107 0.0047  0.0080  -0.0038 53   LEU   A C   
1340 O  O   A LEU   A 53  ? 0.1368 0.1477 0.1228 -0.0037 -0.0053 -0.0061 53   LEU   A O   
1341 O  O   B LEU   A 53  ? 0.1352 0.1653 0.1293 -0.0018 0.0115  -0.0026 53   LEU   A O   
1342 C  CB  A LEU   A 53  ? 0.1307 0.1462 0.1537 -0.0088 0.0039  0.0082  53   LEU   A CB  
1343 C  CB  B LEU   A 53  ? 0.1232 0.1501 0.1284 0.0010  0.0009  -0.0057 53   LEU   A CB  
1344 C  CG  A LEU   A 53  ? 0.1382 0.1487 0.1603 -0.0032 0.0064  0.0183  53   LEU   A CG  
1345 C  CG  B LEU   A 53  ? 0.1291 0.1471 0.1235 0.0044  -0.0045 -0.0107 53   LEU   A CG  
1346 C  CD1 A LEU   A 53  ? 0.1342 0.1500 0.1558 0.0081  0.0026  0.0229  53   LEU   A CD1 
1347 C  CD1 B LEU   A 53  ? 0.1336 0.1488 0.1343 0.0041  -0.0008 -0.0197 53   LEU   A CD1 
1348 C  CD2 A LEU   A 53  ? 0.1511 0.1629 0.1803 -0.0072 0.0038  0.0235  53   LEU   A CD2 
1349 C  CD2 B LEU   A 53  ? 0.1362 0.1487 0.1274 0.0043  -0.0005 -0.0137 53   LEU   A CD2 
1372 N  N   . ASN   A 54  ? 0.1269 0.1415 0.1228 -0.0010 0.0013  -0.0014 54   ASN   A N   
1373 C  CA  . ASN   A 54  ? 0.1191 0.1355 0.1332 -0.0001 -0.0044 -0.0087 54   ASN   A CA  
1374 C  C   . ASN   A 54  ? 0.1257 0.1455 0.1432 -0.0043 0.0011  -0.0056 54   ASN   A C   
1375 O  O   . ASN   A 54  ? 0.1297 0.1559 0.1492 -0.0033 -0.0053 -0.0184 54   ASN   A O   
1376 C  CB  . ASN   A 54  ? 0.1178 0.1318 0.1494 -0.0001 -0.0066 -0.0076 54   ASN   A CB  
1377 C  CG  . ASN   A 54  ? 0.1175 0.1378 0.1456 -0.0016 -0.0010 -0.0100 54   ASN   A CG  
1378 O  OD1 . ASN   A 54  ? 0.1229 0.1437 0.1493 -0.0003 -0.0046 -0.0007 54   ASN   A OD1 
1379 N  ND2 . ASN   A 54  ? 0.1310 0.1456 0.1601 -0.0085 -0.0142 0.0073  54   ASN   A ND2 
1387 N  N   . LYS   A 55  ? 0.1295 0.1481 0.1474 -0.0005 -0.0014 -0.0151 55   LYS   A N   
1388 C  CA  . LYS   A 55  ? 0.1384 0.1538 0.1540 0.0026  -0.0087 -0.0300 55   LYS   A CA  
1389 C  C   . LYS   A 55  ? 0.1365 0.1651 0.1535 -0.0051 -0.0012 -0.0363 55   LYS   A C   
1390 O  O   . LYS   A 55  ? 0.1493 0.1763 0.1551 0.0019  -0.0075 -0.0374 55   LYS   A O   
1391 C  CB  . LYS   A 55  ? 0.1460 0.1664 0.1876 0.0160  -0.0075 -0.0251 55   LYS   A CB  
1392 C  CG  . LYS   A 55  ? 0.1614 0.1972 0.1956 0.0335  -0.0192 -0.0366 55   LYS   A CG  
1393 C  CD  . LYS   A 55  ? 0.1777 0.2251 0.2066 0.0451  -0.0132 -0.0399 55   LYS   A CD  
1394 C  CE  . LYS   A 55  ? 0.2055 0.2534 0.2185 0.0607  -0.0263 -0.0359 55   LYS   A CE  
1395 N  NZ  . LYS   A 55  ? 0.2168 0.2643 0.2197 0.0673  -0.0313 -0.0353 55   LYS   A NZ  
1409 N  N   . ALA   A 56  ? 0.1394 0.1760 0.1519 -0.0077 0.0068  -0.0379 56   ALA   A N   
1410 C  CA  . ALA   A 56  ? 0.1541 0.1935 0.1621 -0.0083 0.0153  -0.0355 56   ALA   A CA  
1411 C  C   . ALA   A 56  ? 0.1588 0.2043 0.1349 -0.0083 0.0142  -0.0386 56   ALA   A C   
1412 O  O   . ALA   A 56  ? 0.1644 0.2343 0.1497 0.0005  0.0231  -0.0254 56   ALA   A O   
1413 C  CB  . ALA   A 56  ? 0.1598 0.2048 0.1744 -0.0098 0.0150  -0.0241 56   ALA   A CB  
1419 N  N   . THR   A 57  ? 0.1444 0.1811 0.1315 -0.0079 0.0137  -0.0309 57   THR   A N   
1420 C  CA  . THR   A 57  ? 0.1514 0.1729 0.1490 -0.0098 0.0059  -0.0176 57   THR   A CA  
1421 C  C   . THR   A 57  ? 0.1482 0.1771 0.1537 -0.0071 -0.0001 -0.0228 57   THR   A C   
1422 O  O   . THR   A 57  ? 0.1463 0.1797 0.1693 -0.0127 -0.0021 -0.0346 57   THR   A O   
1423 C  CB  . THR   A 57  ? 0.1433 0.1696 0.1382 -0.0048 0.0040  -0.0182 57   THR   A CB  
1424 O  OG1 . THR   A 57  ? 0.1349 0.1647 0.1342 -0.0066 0.0016  -0.0160 57   THR   A OG1 
1425 C  CG2 . THR   A 57  ? 0.1448 0.1716 0.1371 -0.0020 -0.0040 -0.0157 57   THR   A CG2 
1433 N  N   . ASN   A 58  ? 0.1513 0.1757 0.1764 -0.0093 0.0098  -0.0373 58   ASN   A N   
1434 C  CA  . ASN   A 58  ? 0.1743 0.1697 0.1938 -0.0123 0.0117  -0.0463 58   ASN   A CA  
1435 C  C   . ASN   A 58  ? 0.1516 0.1533 0.1780 0.0005  -0.0010 -0.0353 58   ASN   A C   
1436 O  O   . ASN   A 58  ? 0.1548 0.1620 0.1956 -0.0113 0.0025  -0.0347 58   ASN   A O   
1437 C  CB  . ASN   A 58  ? 0.2231 0.1854 0.2233 -0.0229 0.0443  -0.0610 58   ASN   A CB  
1438 C  CG  . ASN   A 58  ? 0.2659 0.2127 0.3047 -0.0198 0.0447  -0.0466 58   ASN   A CG  
1439 O  OD1 . ASN   A 58  ? 0.2917 0.2044 0.3527 0.0160  0.0748  -0.0327 58   ASN   A OD1 
1440 N  ND2 . ASN   A 58  ? 0.2798 0.2300 0.3300 -0.0193 0.0310  -0.0489 58   ASN   A ND2 
1447 N  N   . ASN   A 59  ? 0.1339 0.1464 0.1592 -0.0021 -0.0082 -0.0265 59   ASN   A N   
1448 C  CA  . ASN   A 59  ? 0.1372 0.1363 0.1661 -0.0025 -0.0079 -0.0149 59   ASN   A CA  
1449 C  C   . ASN   A 59  ? 0.1336 0.1386 0.1498 -0.0085 -0.0063 -0.0079 59   ASN   A C   
1450 O  O   . ASN   A 59  ? 0.1333 0.1412 0.1548 -0.0043 0.0003  -0.0041 59   ASN   A O   
1451 C  CB  . ASN   A 59  ? 0.1395 0.1283 0.1697 0.0008  -0.0161 -0.0223 59   ASN   A CB  
1452 C  CG  . ASN   A 59  ? 0.1426 0.1381 0.1743 0.0011  -0.0273 -0.0062 59   ASN   A CG  
1453 O  OD1 . ASN   A 59  ? 0.1523 0.1448 0.1634 -0.0095 -0.0255 -0.0005 59   ASN   A OD1 
1454 N  ND2 . ASN   A 59  ? 0.1487 0.1407 0.1831 -0.0108 -0.0219 -0.0019 59   ASN   A ND2 
1461 N  N   . ALA   A 60  ? 0.1271 0.1419 0.1467 -0.0029 -0.0021 -0.0047 60   ALA   A N   
1462 C  CA  . ALA   A 60  ? 0.1302 0.1438 0.1533 -0.0017 -0.0094 -0.0086 60   ALA   A CA  
1463 C  C   . ALA   A 60  ? 0.1319 0.1383 0.1584 -0.0019 -0.0014 -0.0103 60   ALA   A C   
1464 O  O   . ALA   A 60  ? 0.1254 0.1405 0.1771 -0.0031 -0.0079 -0.0127 60   ALA   A O   
1465 C  CB  . ALA   A 60  ? 0.1418 0.1584 0.1491 -0.0065 -0.0150 -0.0237 60   ALA   A CB  
1471 N  N   . MET   A 61  ? 0.1282 0.1352 0.1502 -0.0055 0.0016  -0.0065 61   MET   A N   
1472 C  CA  . MET   A 61  ? 0.1309 0.1314 0.1448 -0.0047 -0.0008 0.0003  61   MET   A CA  
1473 C  C   . MET   A 61  ? 0.1266 0.1245 0.1441 -0.0056 -0.0088 -0.0089 61   MET   A C   
1474 O  O   . MET   A 61  ? 0.1275 0.1291 0.1529 -0.0054 0.0035  0.0017  61   MET   A O   
1475 C  CB  . MET   A 61  ? 0.1296 0.1354 0.1442 -0.0118 -0.0028 -0.0053 61   MET   A CB  
1476 C  CG  . MET   A 61  ? 0.1337 0.1413 0.1538 -0.0028 -0.0010 -0.0099 61   MET   A CG  
1477 S  SD  . MET   A 61  ? 0.1331 0.1385 0.1855 -0.0143 0.0020  -0.0192 61   MET   A SD  
1478 C  CE  . MET   A 61  ? 0.1537 0.1566 0.2088 -0.0161 0.0140  -0.0200 61   MET   A CE  
1488 N  N   . GLN   A 62  ? 0.1263 0.1237 0.1427 -0.0058 -0.0001 -0.0059 62   GLN   A N   
1489 C  CA  . GLN   A 62  ? 0.1324 0.1203 0.1566 -0.0031 0.0045  -0.0017 62   GLN   A CA  
1490 C  C   . GLN   A 62  ? 0.1285 0.1133 0.1626 0.0004  0.0058  0.0001  62   GLN   A C   
1491 O  O   . GLN   A 62  ? 0.1335 0.1293 0.1668 0.0004  0.0062  -0.0039 62   GLN   A O   
1492 C  CB  . GLN   A 62  ? 0.1293 0.1170 0.1621 -0.0013 -0.0020 -0.0036 62   GLN   A CB  
1493 C  CG  . GLN   A 62  ? 0.1305 0.1195 0.1492 -0.0057 -0.0127 0.0087  62   GLN   A CG  
1494 C  CD  . GLN   A 62  ? 0.1398 0.1255 0.1550 -0.0013 0.0057  0.0067  62   GLN   A CD  
1495 O  OE1 . GLN   A 62  ? 0.1438 0.1380 0.1666 -0.0047 0.0014  -0.0045 62   GLN   A OE1 
1496 N  NE2 . GLN   A 62  ? 0.1434 0.1276 0.1668 0.0010  0.0015  -0.0062 62   GLN   A NE2 
1505 N  N   . VAL   A 63  ? 0.1260 0.1281 0.1794 -0.0067 0.0058  -0.0241 63   VAL   A N   
1506 C  CA  . VAL   A 63  ? 0.1304 0.1341 0.1909 -0.0147 0.0036  -0.0194 63   VAL   A CA  
1507 C  C   . VAL   A 63  ? 0.1203 0.1314 0.1826 -0.0152 -0.0086 -0.0211 63   VAL   A C   
1508 O  O   . VAL   A 63  ? 0.1203 0.1329 0.1942 -0.0144 -0.0034 -0.0151 63   VAL   A O   
1509 C  CB  . VAL   A 63  ? 0.1412 0.1557 0.2277 -0.0130 -0.0128 -0.0453 63   VAL   A CB  
1510 C  CG1 . VAL   A 63  ? 0.1549 0.1738 0.2635 -0.0129 -0.0130 -0.0649 63   VAL   A CG1 
1511 C  CG2 . VAL   A 63  ? 0.1510 0.1484 0.2384 -0.0113 0.0113  -0.0430 63   VAL   A CG2 
1521 N  N   . GLU   A 64  ? 0.1250 0.1376 0.1768 -0.0050 -0.0081 -0.0078 64   GLU   A N   
1522 C  CA  . GLU   A 64  ? 0.1253 0.1370 0.1708 -0.0133 -0.0194 0.0003  64   GLU   A CA  
1523 C  C   . GLU   A 64  ? 0.1203 0.1318 0.1693 -0.0143 0.0004  0.0036  64   GLU   A C   
1524 O  O   . GLU   A 64  ? 0.1279 0.1369 0.1716 -0.0041 0.0057  -0.0001 64   GLU   A O   
1525 C  CB  . GLU   A 64  ? 0.1342 0.1501 0.1704 -0.0095 -0.0040 -0.0093 64   GLU   A CB  
1526 C  CG  . GLU   A 64  ? 0.1415 0.1550 0.1676 -0.0170 -0.0091 -0.0031 64   GLU   A CG  
1527 C  CD  . GLU   A 64  ? 0.1500 0.1615 0.1782 -0.0213 0.0015  -0.0033 64   GLU   A CD  
1528 O  OE1 . GLU   A 64  ? 0.1454 0.1761 0.2023 -0.0238 0.0072  -0.0037 64   GLU   A OE1 
1529 O  OE2 . GLU   A 64  ? 0.1639 0.1644 0.1771 -0.0242 -0.0069 0.0029  64   GLU   A OE2 
1536 N  N   . SER   A 65  ? 0.1186 0.1316 0.1639 -0.0018 0.0004  -0.0005 65   SER   A N   
1537 C  CA  . SER   A 65  ? 0.1241 0.1262 0.1544 -0.0032 -0.0092 -0.0112 65   SER   A CA  
1538 C  C   . SER   A 65  ? 0.1206 0.1351 0.1611 -0.0055 -0.0020 -0.0063 65   SER   A C   
1539 O  O   . SER   A 65  ? 0.1266 0.1369 0.1812 -0.0020 0.0126  -0.0038 65   SER   A O   
1540 C  CB  . SER   A 65  ? 0.1276 0.1265 0.1570 -0.0072 0.0031  0.0013  65   SER   A CB  
1541 O  OG  . SER   A 65  ? 0.1284 0.1396 0.1649 -0.0084 -0.0055 0.0126  65   SER   A OG  
1547 N  N   . ASP   A 66  ? 0.1264 0.1262 0.1760 -0.0053 0.0141  0.0031  66   ASP   A N   
1548 C  CA  . ASP   A 66  ? 0.1354 0.1352 0.1903 -0.0034 0.0132  0.0145  66   ASP   A CA  
1549 C  C   . ASP   A 66  ? 0.1320 0.1342 0.1931 -0.0102 0.0061  0.0099  66   ASP   A C   
1550 O  O   . ASP   A 66  ? 0.1427 0.1448 0.2180 -0.0035 0.0255  0.0232  66   ASP   A O   
1551 C  CB  . ASP   A 66  ? 0.1424 0.1480 0.2211 0.0045  0.0161  0.0309  66   ASP   A CB  
1552 C  CG  . ASP   A 66  ? 0.1662 0.1572 0.2370 0.0061  0.0047  0.0463  66   ASP   A CG  
1553 O  OD1 . ASP   A 66  ? 0.1657 0.1865 0.2266 -0.0056 -0.0074 0.0475  66   ASP   A OD1 
1554 O  OD2 . ASP   A 66  ? 0.1883 0.1727 0.3231 0.0267  -0.0137 0.0220  66   ASP   A OD2 
1559 N  N   . ASP   A 67  ? 0.1244 0.1376 0.2017 -0.0040 0.0057  0.0078  67   ASP   A N   
1560 C  CA  . ASP   A 67  ? 0.1246 0.1563 0.2058 -0.0034 0.0016  0.0159  67   ASP   A CA  
1561 C  C   . ASP   A 67  ? 0.1248 0.1533 0.2007 0.0005  0.0076  0.0270  67   ASP   A C   
1562 O  O   . ASP   A 67  ? 0.1280 0.1618 0.2223 0.0026  0.0194  0.0300  67   ASP   A O   
1563 C  CB  . ASP   A 67  ? 0.1356 0.1644 0.2359 -0.0101 -0.0126 0.0189  67   ASP   A CB  
1564 C  CG  . ASP   A 67  ? 0.1398 0.1799 0.2656 -0.0139 -0.0360 0.0271  67   ASP   A CG  
1565 O  OD1 . ASP   A 67  ? 0.1427 0.1980 0.3507 -0.0144 -0.0432 0.0496  67   ASP   A OD1 
1566 O  OD2 . ASP   A 67  ? 0.1398 0.1780 0.2517 -0.0052 -0.0250 0.0241  67   ASP   A OD2 
1571 N  N   . TYR   A 68  ? 0.1308 0.1410 0.1916 0.0040  0.0189  0.0275  68   TYR   A N   
1572 C  CA  . TYR   A 68  ? 0.1435 0.1383 0.1980 0.0046  0.0260  0.0213  68   TYR   A CA  
1573 C  C   . TYR   A 68  ? 0.1365 0.1372 0.2031 -0.0013 0.0321  0.0108  68   TYR   A C   
1574 O  O   . TYR   A 68  ? 0.1402 0.1418 0.2103 0.0084  0.0319  0.0158  68   TYR   A O   
1575 C  CB  . TYR   A 68  ? 0.1480 0.1338 0.2187 0.0098  0.0422  0.0280  68   TYR   A CB  
1576 C  CG  . TYR   A 68  ? 0.1543 0.1548 0.2479 0.0076  0.0595  0.0256  68   TYR   A CG  
1577 C  CD1 . TYR   A 68  ? 0.1681 0.1637 0.2811 -0.0194 0.0474  -0.0131 68   TYR   A CD1 
1578 C  CD2 . TYR   A 68  ? 0.1766 0.1619 0.2915 0.0115  0.0625  0.0314  68   TYR   A CD2 
1579 C  CE1 . TYR   A 68  ? 0.1753 0.1752 0.3239 -0.0188 0.0529  -0.0226 68   TYR   A CE1 
1580 C  CE2 . TYR   A 68  ? 0.1677 0.1615 0.3142 -0.0004 0.0790  0.0074  68   TYR   A CE2 
1581 C  CZ  . TYR   A 68  ? 0.1718 0.1648 0.3334 -0.0216 0.0611  -0.0161 68   TYR   A CZ  
1582 O  OH  . TYR   A 68  ? 0.2039 0.1651 0.3498 -0.0161 0.0441  -0.0435 68   TYR   A OH  
1592 N  N   . ILE   A 69  ? 0.1289 0.1327 0.1936 0.0016  0.0224  0.0137  69   ILE   A N   
1593 C  CA  . ILE   A 69  ? 0.1386 0.1377 0.1902 0.0075  0.0115  -0.0009 69   ILE   A CA  
1594 C  C   . ILE   A 69  ? 0.1457 0.1423 0.1674 0.0029  0.0208  0.0197  69   ILE   A C   
1595 O  O   . ILE   A 69  ? 0.1433 0.1510 0.1741 0.0007  0.0200  0.0161  69   ILE   A O   
1596 C  CB  . ILE   A 69  ? 0.1498 0.1636 0.1884 0.0072  0.0173  -0.0078 69   ILE   A CB  
1597 C  CG1 . ILE   A 69  ? 0.1523 0.1734 0.1973 0.0077  0.0158  -0.0194 69   ILE   A CG1 
1598 C  CG2 . ILE   A 69  ? 0.1675 0.1852 0.2039 0.0137  0.0030  -0.0269 69   ILE   A CG2 
1599 C  CD1 . ILE   A 69  ? 0.1519 0.1832 0.2193 -0.0019 0.0207  -0.0277 69   ILE   A CD1 
1611 N  N   . ALA   A 70  ? 0.1480 0.1401 0.1808 -0.0062 0.0201  0.0179  70   ALA   A N   
1612 C  CA  . ALA   A 70  ? 0.1511 0.1540 0.1957 -0.0154 0.0302  0.0176  70   ALA   A CA  
1613 C  C   . ALA   A 70  ? 0.1486 0.1639 0.1997 -0.0139 0.0282  0.0135  70   ALA   A C   
1614 O  O   . ALA   A 70  ? 0.1652 0.1948 0.2301 0.0053  0.0424  0.0274  70   ALA   A O   
1615 C  CB  . ALA   A 70  ? 0.1459 0.1486 0.2298 -0.0209 0.0151  0.0129  70   ALA   A CB  
1621 N  N   . THR   A 71  ? 0.1423 0.1569 0.1946 -0.0045 0.0215  0.0232  71   THR   A N   
1622 C  CA  . THR   A 71  ? 0.1536 0.1789 0.2227 0.0052  0.0209  0.0211  71   THR   A CA  
1623 C  C   . THR   A 71  ? 0.1430 0.1730 0.2456 0.0106  0.0348  0.0130  71   THR   A C   
1624 O  O   . THR   A 71  ? 0.1458 0.1975 0.2987 0.0075  0.0452  -0.0155 71   THR   A O   
1625 C  CB  . THR   A 71  ? 0.1750 0.2041 0.2368 0.0157  -0.0153 0.0318  71   THR   A CB  
1626 O  OG1 . THR   A 71  ? 0.2028 0.2327 0.2371 0.0090  -0.0314 0.0160  71   THR   A OG1 
1627 C  CG2 . THR   A 71  ? 0.1876 0.2218 0.2710 0.0181  -0.0278 0.0414  71   THR   A CG2 
1635 N  N   . ASN   A 72  ? 0.1450 0.1590 0.2182 0.0089  0.0266  0.0218  72   ASN   A N   
1636 C  CA  . ASN   A 72  ? 0.1525 0.1596 0.2211 0.0102  0.0322  0.0155  72   ASN   A CA  
1637 C  C   . ASN   A 72  ? 0.1608 0.1552 0.2162 0.0064  0.0426  0.0078  72   ASN   A C   
1638 O  O   . ASN   A 72  ? 0.1781 0.1542 0.2446 0.0128  0.0452  -0.0064 72   ASN   A O   
1639 C  CB  . ASN   A 72  ? 0.1725 0.1674 0.2238 0.0164  0.0345  0.0227  72   ASN   A CB  
1640 C  CG  . ASN   A 72  ? 0.1923 0.1811 0.2278 0.0257  0.0344  0.0239  72   ASN   A CG  
1641 O  OD1 . ASN   A 72  ? 0.2123 0.2091 0.2497 0.0270  0.0432  0.0247  72   ASN   A OD1 
1642 N  ND2 . ASN   A 72  ? 0.2094 0.1798 0.2341 0.0473  0.0252  0.0106  72   ASN   A ND2 
1649 N  N   . GLY   A 73  ? 0.1726 0.1480 0.2009 0.0033  0.0441  0.0049  73   GLY   A N   
1650 C  CA  . GLY   A 73  ? 0.1720 0.1490 0.1827 -0.0090 0.0480  0.0056  73   GLY   A CA  
1651 C  C   . GLY   A 73  ? 0.1686 0.1413 0.1730 0.0009  0.0507  0.0222  73   GLY   A C   
1652 O  O   . GLY   A 73  ? 0.1671 0.1473 0.1973 0.0087  0.0381  0.0253  73   GLY   A O   
1656 N  N   . PRO   A 74  ? 0.1777 0.1399 0.1878 -0.0109 0.0499  0.0159  74   PRO   A N   
1657 C  CA  . PRO   A 74  ? 0.1728 0.1430 0.1908 -0.0035 0.0524  0.0161  74   PRO   A CA  
1658 C  C   . PRO   A 74  ? 0.1681 0.1298 0.1900 -0.0023 0.0294  0.0075  74   PRO   A C   
1659 O  O   . PRO   A 74  ? 0.1721 0.1374 0.2111 -0.0002 0.0358  -0.0052 74   PRO   A O   
1660 C  CB  . PRO   A 74  ? 0.1904 0.1682 0.2199 -0.0008 0.0519  0.0257  74   PRO   A CB  
1661 C  CG  . PRO   A 74  ? 0.2176 0.2036 0.2549 -0.0139 0.0397  0.0186  74   PRO   A CG  
1662 C  CD  . PRO   A 74  ? 0.1997 0.1828 0.2105 -0.0181 0.0428  0.0127  74   PRO   A CD  
1670 N  N   . LEU   A 75  ? 0.1648 0.1199 0.1706 -0.0009 0.0280  0.0036  75   LEU   A N   
1671 C  CA  . LEU   A 75  ? 0.1652 0.1243 0.1579 -0.0028 0.0113  0.0111  75   LEU   A CA  
1672 C  C   . LEU   A 75  ? 0.1722 0.1323 0.1595 -0.0008 0.0111  0.0120  75   LEU   A C   
1673 O  O   . LEU   A 75  ? 0.2086 0.1507 0.1673 0.0064  0.0046  0.0054  75   LEU   A O   
1674 C  CB  . LEU   A 75  ? 0.1715 0.1297 0.1518 -0.0087 0.0105  0.0188  75   LEU   A CB  
1675 C  CG  . LEU   A 75  ? 0.1919 0.1586 0.1686 -0.0373 0.0067  0.0135  75   LEU   A CG  
1676 C  CD1 . LEU   A 75  ? 0.2003 0.2113 0.1727 -0.0326 0.0113  0.0055  75   LEU   A CD1 
1677 C  CD2 . LEU   A 75  ? 0.2258 0.2048 0.2338 -0.0122 0.0116  0.0158  75   LEU   A CD2 
1689 N  N   . LYS   A 76  ? 0.1738 0.1334 0.1691 -0.0046 0.0066  0.0032  76   LYS   A N   
1690 C  CA  . LYS   A 76  ? 0.1694 0.1526 0.1735 -0.0073 0.0085  -0.0106 76   LYS   A CA  
1691 C  C   . LYS   A 76  ? 0.1673 0.1339 0.1440 -0.0000 0.0121  -0.0084 76   LYS   A C   
1692 O  O   . LYS   A 76  ? 0.1712 0.1301 0.1485 -0.0025 0.0181  0.0019  76   LYS   A O   
1693 C  CB  . LYS   A 76  ? 0.1703 0.1764 0.2131 -0.0004 0.0085  -0.0326 76   LYS   A CB  
1694 C  CG  . LYS   A 76  ? 0.1808 0.1630 0.2734 0.0027  0.0074  -0.0259 76   LYS   A CG  
1695 C  CD  . LYS   A 76  ? 0.1861 0.1666 0.3129 0.0068  0.0041  -0.0330 76   LYS   A CD  
1696 C  CE  . LYS   A 76  ? 0.1996 0.1923 0.3682 0.0033  0.0058  -0.0452 76   LYS   A CE  
1697 N  NZ  . LYS   A 76  ? 0.2022 0.1916 0.4129 -0.0104 -0.0028 -0.0525 76   LYS   A NZ  
1711 N  N   . VAL   A 77  ? 0.1811 0.1404 0.1423 -0.0022 0.0187  0.0044  77   VAL   A N   
1712 C  CA  . VAL   A 77  ? 0.1742 0.1445 0.1407 0.0035  0.0137  0.0052  77   VAL   A CA  
1713 C  C   . VAL   A 77  ? 0.1672 0.1388 0.1464 0.0067  0.0121  -0.0031 77   VAL   A C   
1714 O  O   . VAL   A 77  ? 0.1747 0.1430 0.1403 0.0078  0.0263  -0.0068 77   VAL   A O   
1715 C  CB  . VAL   A 77  ? 0.1864 0.1627 0.1533 0.0030  0.0165  0.0148  77   VAL   A CB  
1716 C  CG1 . VAL   A 77  ? 0.1807 0.1771 0.1825 0.0094  0.0033  0.0124  77   VAL   A CG1 
1717 C  CG2 . VAL   A 77  ? 0.2103 0.1765 0.1747 -0.0120 0.0016  0.0169  77   VAL   A CG2 
1727 N  N   . GLY   A 78  ? 0.1660 0.1362 0.1381 0.0060  0.0211  0.0046  78   GLY   A N   
1728 C  CA  . GLY   A 78  ? 0.1636 0.1354 0.1430 0.0026  0.0196  0.0072  78   GLY   A CA  
1729 C  C   . GLY   A 78  ? 0.1549 0.1319 0.1494 0.0030  0.0209  0.0059  78   GLY   A C   
1730 O  O   . GLY   A 78  ? 0.1539 0.1325 0.1787 -0.0019 0.0137  0.0239  78   GLY   A O   
1734 N  N   . GLY   A 79  ? 0.1525 0.1287 0.1542 0.0018  0.0190  0.0114  79   GLY   A N   
1735 C  CA  . GLY   A 79  ? 0.1506 0.1292 0.1644 -0.0005 0.0047  0.0106  79   GLY   A CA  
1736 C  C   . GLY   A 79  ? 0.1367 0.1220 0.1541 -0.0028 0.0131  0.0011  79   GLY   A C   
1737 O  O   . GLY   A 79  ? 0.1440 0.1318 0.1652 0.0171  0.0087  0.0041  79   GLY   A O   
1741 N  N   . SER   A 80  ? 0.1310 0.1396 0.1749 -0.0031 0.0063  0.0019  80   SER   A N   
1742 C  CA  . SER   A 80  ? 0.1323 0.1371 0.1665 -0.0030 0.0009  0.0049  80   SER   A CA  
1743 C  C   . SER   A 80  ? 0.1297 0.1358 0.1595 -0.0069 0.0031  0.0128  80   SER   A C   
1744 O  O   . SER   A 80  ? 0.1342 0.1577 0.1888 0.0052  0.0085  -0.0025 80   SER   A O   
1745 C  CB  . SER   A 80  ? 0.1414 0.1333 0.1945 -0.0126 -0.0009 0.0096  80   SER   A CB  
1746 O  OG  . SER   A 80  ? 0.1674 0.1309 0.2258 0.0013  -0.0092 0.0236  80   SER   A OG  
1752 N  N   . CYS   A 81  ? 0.1233 0.1290 0.1590 -0.0026 -0.0042 0.0119  81   CYS   A N   
1753 C  CA  . CYS   A 81  ? 0.1235 0.1376 0.1607 -0.0060 -0.0086 0.0207  81   CYS   A CA  
1754 C  C   . CYS   A 81  ? 0.1278 0.1312 0.1604 -0.0139 -0.0065 0.0266  81   CYS   A C   
1755 O  O   . CYS   A 81  ? 0.1212 0.1622 0.1817 -0.0023 0.0013  0.0319  81   CYS   A O   
1756 C  CB  . CYS   A 81  ? 0.1356 0.1445 0.1779 -0.0128 -0.0041 0.0244  81   CYS   A CB  
1757 S  SG  . CYS   A 81  ? 0.1460 0.1333 0.1750 -0.0157 -0.0027 0.0133  81   CYS   A SG  
1763 N  N   . VAL   A 82  ? 0.1299 0.1425 0.1590 -0.0039 -0.0222 0.0230  82   VAL   A N   
1764 C  CA  . VAL   A 82  ? 0.1465 0.1472 0.1550 -0.0033 -0.0104 0.0301  82   VAL   A CA  
1765 C  C   . VAL   A 82  ? 0.1405 0.1534 0.1688 -0.0040 -0.0149 0.0250  82   VAL   A C   
1766 O  O   . VAL   A 82  ? 0.1327 0.1633 0.1930 -0.0044 -0.0082 -0.0026 82   VAL   A O   
1767 C  CB  . VAL   A 82  ? 0.1728 0.1604 0.1782 -0.0012 -0.0056 0.0263  82   VAL   A CB  
1768 C  CG1 . VAL   A 82  ? 0.1943 0.1764 0.2017 0.0057  0.0001  0.0271  82   VAL   A CG1 
1769 C  CG2 . VAL   A 82  ? 0.1789 0.1650 0.2111 -0.0090 -0.0112 0.0243  82   VAL   A CG2 
1779 N  N   . LEU   A 83  ? 0.1314 0.1495 0.1612 -0.0125 -0.0130 0.0143  83   LEU   A N   
1780 C  CA  . LEU   A 83  ? 0.1318 0.1542 0.1376 -0.0116 -0.0129 0.0118  83   LEU   A CA  
1781 C  C   . LEU   A 83  ? 0.1419 0.1556 0.1371 -0.0130 -0.0180 0.0072  83   LEU   A C   
1782 O  O   . LEU   A 83  ? 0.1559 0.1564 0.1511 -0.0182 -0.0096 0.0206  83   LEU   A O   
1783 C  CB  . LEU   A 83  ? 0.1397 0.1602 0.1559 -0.0119 -0.0170 0.0177  83   LEU   A CB  
1784 C  CG  . LEU   A 83  ? 0.1531 0.1665 0.1658 -0.0154 -0.0007 0.0117  83   LEU   A CG  
1785 C  CD1 . LEU   A 83  ? 0.1675 0.1669 0.1658 -0.0202 -0.0070 0.0296  83   LEU   A CD1 
1786 C  CD2 . LEU   A 83  ? 0.1568 0.1814 0.1888 -0.0132 0.0090  0.0126  83   LEU   A CD2 
1798 N  N   . SER   A 84  ? 0.1567 0.1604 0.1325 -0.0158 -0.0122 0.0090  84   SER   A N   
1799 C  CA  . SER   A 84  ? 0.1664 0.1658 0.1298 -0.0114 -0.0090 0.0095  84   SER   A CA  
1800 C  C   . SER   A 84  ? 0.1676 0.1650 0.1321 -0.0204 0.0032  0.0172  84   SER   A C   
1801 O  O   . SER   A 84  ? 0.1670 0.1744 0.1314 -0.0163 -0.0098 0.0153  84   SER   A O   
1802 C  CB  . SER   A 84  ? 0.1758 0.1867 0.1331 -0.0148 -0.0109 0.0041  84   SER   A CB  
1803 O  OG  . SER   A 84  ? 0.1821 0.2151 0.1464 -0.0146 -0.0182 -0.0042 84   SER   A OG  
1809 N  N   . GLY   A 85  ? 0.1788 0.1828 0.1369 -0.0228 0.0095  0.0088  85   GLY   A N   
1810 C  CA  . GLY   A 85  ? 0.1828 0.1909 0.1570 -0.0289 0.0144  -0.0009 85   GLY   A CA  
1811 C  C   . GLY   A 85  ? 0.1862 0.1970 0.1397 -0.0253 0.0033  -0.0022 85   GLY   A C   
1812 O  O   . GLY   A 85  ? 0.1842 0.2044 0.1496 -0.0372 0.0158  -0.0166 85   GLY   A O   
1816 N  N   . HIS   A 86  ? 0.1880 0.1894 0.1390 -0.0204 0.0022  -0.0015 86   HIS   A N   
1817 C  CA  . HIS   A 86  ? 0.2005 0.1982 0.1249 -0.0247 0.0030  0.0006  86   HIS   A CA  
1818 C  C   . HIS   A 86  ? 0.2241 0.2106 0.1200 -0.0290 -0.0000 -0.0000 86   HIS   A C   
1819 O  O   . HIS   A 86  ? 0.2345 0.2328 0.1362 -0.0263 0.0120  0.0048  86   HIS   A O   
1820 C  CB  . HIS   A 86  ? 0.1941 0.1859 0.1321 -0.0141 0.0059  0.0039  86   HIS   A CB  
1821 C  CG  . HIS   A 86  ? 0.1825 0.1859 0.1490 -0.0101 -0.0003 0.0033  86   HIS   A CG  
1822 N  ND1 . HIS   A 86  ? 0.1902 0.1832 0.1786 -0.0175 -0.0042 0.0053  86   HIS   A ND1 
1823 C  CD2 . HIS   A 86  ? 0.1781 0.1769 0.1348 -0.0043 0.0036  0.0073  86   HIS   A CD2 
1824 C  CE1 . HIS   A 86  ? 0.1837 0.1808 0.1643 -0.0213 0.0105  0.0098  86   HIS   A CE1 
1825 N  NE2 . HIS   A 86  ? 0.1807 0.1773 0.1534 -0.0076 0.0026  0.0205  86   HIS   A NE2 
1833 N  N   . ASN   A 87  ? 0.2367 0.2188 0.1445 -0.0254 0.0200  -0.0167 87   ASN   A N   
1834 C  CA  . ASN   A 87  ? 0.2534 0.2351 0.1587 -0.0249 0.0481  -0.0229 87   ASN   A CA  
1835 C  C   . ASN   A 87  ? 0.2504 0.2468 0.1809 -0.0308 0.0671  -0.0150 87   ASN   A C   
1836 O  O   . ASN   A 87  ? 0.2713 0.2651 0.2344 -0.0456 0.0925  -0.0185 87   ASN   A O   
1837 C  CB  . ASN   A 87  ? 0.2748 0.2454 0.1722 -0.0140 0.0501  -0.0238 87   ASN   A CB  
1838 C  CG  . ASN   A 87  ? 0.2855 0.2530 0.1765 -0.0063 0.0651  -0.0098 87   ASN   A CG  
1839 O  OD1 . ASN   A 87  ? 0.3013 0.2475 0.1854 0.0121  0.0585  -0.0002 87   ASN   A OD1 
1840 N  ND2 . ASN   A 87  ? 0.2877 0.2749 0.1885 -0.0057 0.0642  -0.0074 87   ASN   A ND2 
1847 N  N   . LEU   A 88  ? 0.2317 0.2385 0.1751 -0.0327 0.0404  0.0001  88   LEU   A N   
1848 C  CA  . LEU   A 88  ? 0.2111 0.2350 0.1911 -0.0336 0.0358  0.0131  88   LEU   A CA  
1849 C  C   . LEU   A 88  ? 0.2053 0.2349 0.1850 -0.0335 0.0352  0.0314  88   LEU   A C   
1850 O  O   . LEU   A 88  ? 0.2110 0.2408 0.2183 -0.0311 0.0390  0.0475  88   LEU   A O   
1851 C  CB  . LEU   A 88  ? 0.2097 0.2444 0.2029 -0.0353 0.0056  0.0165  88   LEU   A CB  
1852 C  CG  . LEU   A 88  ? 0.2223 0.2573 0.2304 -0.0314 -0.0081 0.0125  88   LEU   A CG  
1853 C  CD1 . LEU   A 88  ? 0.2309 0.2671 0.2240 -0.0274 -0.0075 0.0020  88   LEU   A CD1 
1854 C  CD2 . LEU   A 88  ? 0.2355 0.2677 0.2701 -0.0248 -0.0030 0.0056  88   LEU   A CD2 
1866 N  N   . ALA   A 89  ? 0.2074 0.2240 0.1635 -0.0330 0.0285  0.0168  89   ALA   A N   
1867 C  CA  . ALA   A 89  ? 0.2147 0.2249 0.1366 -0.0294 0.0112  0.0152  89   ALA   A CA  
1868 C  C   . ALA   A 89  ? 0.2223 0.2261 0.1453 -0.0260 -0.0088 0.0152  89   ALA   A C   
1869 O  O   . ALA   A 89  ? 0.2186 0.2198 0.1855 -0.0342 -0.0125 -0.0077 89   ALA   A O   
1870 C  CB  . ALA   A 89  ? 0.2081 0.2234 0.1227 -0.0219 0.0032  0.0199  89   ALA   A CB  
1876 N  N   . LYS   A 90  ? 0.2317 0.2380 0.1412 -0.0394 -0.0197 0.0283  90   LYS   A N   
1877 C  CA  . LYS   A 90  ? 0.2341 0.2522 0.1498 -0.0343 -0.0256 0.0249  90   LYS   A CA  
1878 C  C   . LYS   A 90  ? 0.2069 0.2366 0.1484 -0.0328 -0.0255 0.0130  90   LYS   A C   
1879 O  O   . LYS   A 90  ? 0.2081 0.2516 0.1805 -0.0337 -0.0395 0.0018  90   LYS   A O   
1880 C  CB  . LYS   A 90  ? 0.2600 0.2836 0.1972 -0.0338 -0.0283 0.0482  90   LYS   A CB  
1881 C  CG  . LYS   A 90  ? 0.2898 0.3119 0.3025 -0.0330 -0.0264 0.0527  90   LYS   A CG  
1882 C  CD  . LYS   A 90  ? 0.3226 0.3377 0.4124 -0.0347 -0.0106 0.0608  90   LYS   A CD  
1883 C  CE  . LYS   A 90  ? 0.3462 0.3609 0.4932 -0.0337 -0.0016 0.0603  90   LYS   A CE  
1884 N  NZ  . LYS   A 90  ? 0.3626 0.3773 0.5459 -0.0322 0.0017  0.0536  90   LYS   A NZ  
1898 N  N   . HIS   A 91  ? 0.1976 0.2061 0.1154 -0.0269 -0.0369 0.0249  91   HIS   A N   
1899 C  CA  . HIS   A 91  ? 0.1860 0.1872 0.1234 -0.0232 -0.0372 0.0283  91   HIS   A CA  
1900 C  C   . HIS   A 91  ? 0.1651 0.1753 0.1137 -0.0232 -0.0240 0.0278  91   HIS   A C   
1901 O  O   . HIS   A 91  ? 0.1622 0.1892 0.1394 -0.0287 -0.0073 0.0308  91   HIS   A O   
1902 C  CB  . HIS   A 91  ? 0.2044 0.2133 0.1762 0.0058  -0.0454 0.0213  91   HIS   A CB  
1903 C  CG  . HIS   A 91  ? 0.2441 0.2589 0.2448 0.0122  -0.0671 0.0091  91   HIS   A CG  
1904 N  ND1 . HIS   A 91  ? 0.2544 0.2858 0.2816 0.0145  -0.0752 -0.0198 91   HIS   A ND1 
1905 C  CD2 . HIS   A 91  ? 0.2666 0.2783 0.2591 0.0210  -0.0782 0.0182  91   HIS   A CD2 
1906 C  CE1 . HIS   A 91  ? 0.2642 0.2930 0.2882 0.0210  -0.0756 -0.0040 91   HIS   A CE1 
1907 N  NE2 . HIS   A 91  ? 0.2761 0.2932 0.2824 0.0285  -0.0788 0.0101  91   HIS   A NE2 
1915 N  N   . CYS   A 92  ? 0.1526 0.1690 0.1190 -0.0181 -0.0203 0.0240  92   CYS   A N   
1916 C  CA  . CYS   A 92  ? 0.1438 0.1607 0.1424 -0.0139 -0.0049 0.0224  92   CYS   A CA  
1917 C  C   . CYS   A 92  ? 0.1347 0.1509 0.1353 -0.0147 -0.0053 0.0179  92   CYS   A C   
1918 O  O   . CYS   A 92  ? 0.1390 0.1563 0.1481 -0.0224 -0.0047 0.0125  92   CYS   A O   
1919 C  CB  . CYS   A 92  ? 0.1456 0.1535 0.1575 -0.0092 -0.0077 0.0174  92   CYS   A CB  
1920 S  SG  . CYS   A 92  ? 0.1431 0.1439 0.1523 -0.0134 -0.0049 0.0097  92   CYS   A SG  
1926 N  N   . LEU   A 93  ? 0.1342 0.1365 0.1419 -0.0130 0.0001  0.0193  93   LEU   A N   
1927 C  CA  . LEU   A 93  ? 0.1269 0.1353 0.1349 -0.0092 0.0021  0.0143  93   LEU   A CA  
1928 C  C   . LEU   A 93  ? 0.1260 0.1214 0.1310 -0.0083 0.0065  0.0175  93   LEU   A C   
1929 O  O   . LEU   A 93  ? 0.1203 0.1372 0.1330 -0.0062 -0.0012 0.0113  93   LEU   A O   
1930 C  CB  . LEU   A 93  ? 0.1395 0.1331 0.1522 -0.0049 -0.0113 0.0243  93   LEU   A CB  
1931 C  CG  . LEU   A 93  ? 0.1421 0.1373 0.1493 -0.0100 0.0017  0.0202  93   LEU   A CG  
1932 C  CD1 . LEU   A 93  ? 0.1488 0.1325 0.1770 -0.0077 0.0037  0.0146  93   LEU   A CD1 
1933 C  CD2 . LEU   A 93  ? 0.1587 0.1355 0.1735 -0.0105 -0.0098 0.0158  93   LEU   A CD2 
1945 N  N   . HIS   A 94  ? 0.1184 0.1206 0.1428 -0.0034 0.0039  0.0204  94   HIS   A N   
1946 C  CA  . HIS   A 94  ? 0.1137 0.1211 0.1394 -0.0051 -0.0063 0.0190  94   HIS   A CA  
1947 C  C   . HIS   A 94  ? 0.1194 0.1170 0.1458 -0.0068 -0.0021 0.0057  94   HIS   A C   
1948 O  O   . HIS   A 94  ? 0.1199 0.1352 0.1878 0.0005  0.0043  -0.0118 94   HIS   A O   
1949 C  CB  . HIS   A 94  ? 0.1201 0.1196 0.1455 -0.0031 -0.0048 0.0136  94   HIS   A CB  
1950 C  CG  . HIS   A 94  ? 0.1229 0.1212 0.1327 -0.0034 -0.0051 0.0162  94   HIS   A CG  
1951 N  ND1 . HIS   A 94  ? 0.1223 0.1212 0.1367 -0.0071 0.0007  0.0126  94   HIS   A ND1 
1952 C  CD2 . HIS   A 94  ? 0.1284 0.1359 0.1436 -0.0104 -0.0088 0.0087  94   HIS   A CD2 
1953 C  CE1 . HIS   A 94  ? 0.1282 0.1282 0.1318 -0.0103 -0.0053 0.0070  94   HIS   A CE1 
1954 N  NE2 . HIS   A 94  ? 0.1340 0.1335 0.1351 -0.0128 -0.0127 0.0032  94   HIS   A NE2 
1962 N  N   . VAL   A 95  ? 0.1168 0.1207 0.1184 -0.0019 0.0095  0.0040  95   VAL   A N   
1963 C  CA  . VAL   A 95  ? 0.1266 0.1201 0.1284 -0.0060 0.0070  0.0098  95   VAL   A CA  
1964 C  C   . VAL   A 95  ? 0.1243 0.1168 0.1263 -0.0162 0.0039  0.0035  95   VAL   A C   
1965 O  O   . VAL   A 95  ? 0.1344 0.1279 0.1276 0.0039  0.0073  0.0038  95   VAL   A O   
1966 C  CB  . VAL   A 95  ? 0.1296 0.1260 0.1431 -0.0123 0.0008  0.0057  95   VAL   A CB  
1967 C  CG1 . VAL   A 95  ? 0.1467 0.1293 0.1600 -0.0174 0.0024  -0.0053 95   VAL   A CG1 
1968 C  CG2 . VAL   A 95  ? 0.1288 0.1313 0.1368 -0.0151 0.0014  0.0146  95   VAL   A CG2 
1978 N  N   . VAL   A 96  ? 0.1302 0.1203 0.1116 -0.0056 0.0062  0.0083  96   VAL   A N   
1979 C  CA  . VAL   A 96  ? 0.1399 0.1207 0.1324 -0.0057 0.0106  0.0153  96   VAL   A CA  
1980 C  C   . VAL   A 96  ? 0.1394 0.1278 0.1441 -0.0055 0.0080  0.0119  96   VAL   A C   
1981 O  O   . VAL   A 96  ? 0.1460 0.1333 0.1626 -0.0064 0.0163  -0.0035 96   VAL   A O   
1982 C  CB  . VAL   A 96  ? 0.1419 0.1282 0.1377 -0.0036 0.0172  0.0132  96   VAL   A CB  
1983 C  CG1 . VAL   A 96  ? 0.1490 0.1394 0.1223 -0.0042 0.0084  0.0141  96   VAL   A CG1 
1984 C  CG2 . VAL   A 96  ? 0.1387 0.1371 0.1556 -0.0191 0.0077  0.0098  96   VAL   A CG2 
1994 N  N   . GLY   A 97  ? 0.1381 0.1344 0.1289 -0.0081 0.0039  0.0113  97   GLY   A N   
1995 C  CA  . GLY   A 97  ? 0.1481 0.1487 0.1272 -0.0116 -0.0067 0.0090  97   GLY   A CA  
1996 C  C   . GLY   A 97  ? 0.1508 0.1633 0.1165 -0.0124 0.0002  0.0026  97   GLY   A C   
1997 O  O   . GLY   A 97  ? 0.1624 0.1603 0.1453 -0.0181 -0.0063 0.0139  97   GLY   A O   
2001 N  N   A PRO   A 98  ? 0.1555 0.1617 0.0983 -0.0071 -0.0092 0.0030  98   PRO   A N   
2002 N  N   B PRO   A 98  ? 0.1566 0.1622 0.1232 -0.0058 -0.0001 0.0187  98   PRO   A N   
2003 C  CA  A PRO   A 98  ? 0.1593 0.1773 0.1008 -0.0075 -0.0012 -0.0054 98   PRO   A CA  
2004 C  CA  B PRO   A 98  ? 0.1641 0.1760 0.1390 -0.0026 0.0025  0.0100  98   PRO   A CA  
2005 C  C   A PRO   A 98  ? 0.1513 0.1789 0.0797 -0.0154 0.0035  0.0067  98   PRO   A C   
2006 C  C   B PRO   A 98  ? 0.1857 0.1761 0.1336 -0.0055 0.0012  0.0237  98   PRO   A C   
2007 O  O   A PRO   A 98  ? 0.1447 0.1620 0.0895 -0.0179 0.0120  0.0029  98   PRO   A O   
2008 O  O   B PRO   A 98  ? 0.1806 0.1631 0.1611 0.0015  0.0128  0.0133  98   PRO   A O   
2009 C  CB  A PRO   A 98  ? 0.1673 0.1827 0.0899 0.0062  -0.0169 -0.0110 98   PRO   A CB  
2010 C  CB  B PRO   A 98  ? 0.1658 0.1780 0.1381 0.0079  -0.0015 0.0104  98   PRO   A CB  
2011 C  CG  A PRO   A 98  ? 0.1651 0.1702 0.1110 0.0046  -0.0220 -0.0167 98   PRO   A CG  
2012 C  CG  B PRO   A 98  ? 0.1704 0.1720 0.1484 0.0059  -0.0028 0.0071  98   PRO   A CG  
2013 C  CD  A PRO   A 98  ? 0.1637 0.1597 0.1059 0.0014  -0.0156 -0.0092 98   PRO   A CD  
2014 C  CD  B PRO   A 98  ? 0.1604 0.1595 0.1318 0.0042  -0.0044 0.0168  98   PRO   A CD  
2029 N  N   A ASN   A 99  ? 0.1553 0.2017 0.0864 -0.0169 0.0080  0.0228  99   ASN   A N   
2030 N  N   B ASN   A 99  ? 0.2120 0.1832 0.1156 -0.0010 -0.0043 0.0401  99   ASN   A N   
2031 C  CA  A ASN   A 99  ? 0.1706 0.2079 0.0837 -0.0153 0.0119  0.0225  99   ASN   A CA  
2032 C  CA  B ASN   A 99  ? 0.2440 0.1858 0.1349 -0.0021 -0.0157 0.0491  99   ASN   A CA  
2033 C  C   A ASN   A 99  ? 0.1822 0.2148 0.0787 -0.0189 0.0170  0.0174  99   ASN   A C   
2034 C  C   B ASN   A 99  ? 0.2620 0.1840 0.1366 -0.0016 -0.0206 0.0529  99   ASN   A C   
2035 O  O   A ASN   A 99  ? 0.1915 0.2243 0.1012 -0.0072 0.0080  0.0132  99   ASN   A O   
2036 O  O   B ASN   A 99  ? 0.2624 0.1681 0.1485 0.0076  -0.0239 0.0432  99   ASN   A O   
2037 C  CB  A ASN   A 99  ? 0.1700 0.2027 0.0624 -0.0114 0.0105  0.0320  99   ASN   A CB  
2038 C  CB  B ASN   A 99  ? 0.2579 0.1905 0.1724 -0.0015 -0.0287 0.0484  99   ASN   A CB  
2039 C  CG  A ASN   A 99  ? 0.1708 0.1924 0.0755 -0.0015 -0.0047 0.0178  99   ASN   A CG  
2040 C  CG  B ASN   A 99  ? 0.2749 0.1976 0.2089 -0.0100 -0.0371 0.0583  99   ASN   A CG  
2041 O  OD1 A ASN   A 99  ? 0.1804 0.1955 0.0992 0.0079  0.0006  -0.0064 99   ASN   A OD1 
2042 O  OD1 B ASN   A 99  ? 0.2806 0.2021 0.2102 -0.0088 -0.0440 0.0641  99   ASN   A OD1 
2043 N  ND2 A ASN   A 99  ? 0.1749 0.1816 0.0876 -0.0051 -0.0157 0.0349  99   ASN   A ND2 
2044 N  ND2 B ASN   A 99  ? 0.2821 0.2009 0.2504 -0.0118 -0.0411 0.0506  99   ASN   A ND2 
2057 N  N   A VAL   A 100 ? 0.1940 0.2087 0.0810 -0.0290 -0.0108 -0.0007 100  VAL   A N   
2058 N  N   B VAL   A 100 ? 0.2826 0.2133 0.1548 -0.0031 -0.0274 0.0491  100  VAL   A N   
2059 C  CA  A VAL   A 100 ? 0.2136 0.2189 0.1077 -0.0291 -0.0214 0.0146  100  VAL   A CA  
2060 C  CA  B VAL   A 100 ? 0.3039 0.2325 0.1981 -0.0033 -0.0343 0.0444  100  VAL   A CA  
2061 C  C   A VAL   A 100 ? 0.2281 0.2306 0.0915 -0.0360 -0.0268 0.0373  100  VAL   A C   
2062 C  C   B VAL   A 100 ? 0.3147 0.2386 0.2186 0.0046  -0.0452 0.0455  100  VAL   A C   
2063 O  O   A VAL   A 100 ? 0.2374 0.2437 0.0931 -0.0341 -0.0147 0.0436  100  VAL   A O   
2064 O  O   B VAL   A 100 ? 0.3176 0.2374 0.2319 -0.0001 -0.0433 0.0428  100  VAL   A O   
2065 C  CB  A VAL   A 100 ? 0.2267 0.2205 0.1653 -0.0352 -0.0248 0.0105  100  VAL   A CB  
2066 C  CB  B VAL   A 100 ? 0.3108 0.2464 0.2261 -0.0046 -0.0359 0.0276  100  VAL   A CB  
2067 C  CG1 A VAL   A 100 ? 0.2259 0.2241 0.1800 -0.0400 -0.0207 0.0030  100  VAL   A CG1 
2068 C  CG1 B VAL   A 100 ? 0.3107 0.2467 0.2398 -0.0076 -0.0359 0.0264  100  VAL   A CG1 
2069 C  CG2 A VAL   A 100 ? 0.2383 0.2216 0.1824 -0.0371 -0.0222 0.0189  100  VAL   A CG2 
2070 C  CG2 B VAL   A 100 ? 0.3131 0.2544 0.2355 -0.0014 -0.0347 0.0180  100  VAL   A CG2 
2089 N  N   A ASN   A 101 ? 0.2330 0.2365 0.1192 -0.0423 -0.0310 0.0518  101  ASN   A N   
2090 N  N   B ASN   A 101 ? 0.3285 0.2510 0.2331 0.0143  -0.0561 0.0498  101  ASN   A N   
2091 C  CA  A ASN   A 101 ? 0.2550 0.2476 0.1336 -0.0523 -0.0280 0.0665  101  ASN   A CA  
2092 C  CA  B ASN   A 101 ? 0.3444 0.2663 0.2529 0.0267  -0.0556 0.0534  101  ASN   A CA  
2093 C  C   A ASN   A 101 ? 0.2771 0.2768 0.1578 -0.0638 -0.0023 0.0825  101  ASN   A C   
2094 C  C   B ASN   A 101 ? 0.3603 0.2860 0.2666 0.0245  -0.0442 0.0663  101  ASN   A C   
2095 O  O   A ASN   A 101 ? 0.2930 0.2825 0.1965 -0.0622 0.0019  0.0753  101  ASN   A O   
2096 O  O   B ASN   A 101 ? 0.3670 0.2898 0.2698 0.0241  -0.0469 0.0737  101  ASN   A O   
2097 C  CB  A ASN   A 101 ? 0.2592 0.2407 0.1252 -0.0465 -0.0459 0.0522  101  ASN   A CB  
2098 C  CB  B ASN   A 101 ? 0.3456 0.2642 0.2661 0.0336  -0.0608 0.0424  101  ASN   A CB  
2099 C  CG  A ASN   A 101 ? 0.2637 0.2349 0.1099 -0.0407 -0.0557 0.0274  101  ASN   A CG  
2100 C  CG  B ASN   A 101 ? 0.3484 0.2688 0.2830 0.0336  -0.0652 0.0281  101  ASN   A CG  
2101 O  OD1 A ASN   A 101 ? 0.2625 0.2380 0.1327 -0.0231 -0.0460 -0.0019 101  ASN   A OD1 
2102 O  OD1 B ASN   A 101 ? 0.3571 0.2745 0.2989 0.0270  -0.0581 0.0261  101  ASN   A OD1 
2103 N  ND2 A ASN   A 101 ? 0.2718 0.2329 0.1082 -0.0462 -0.0476 0.0289  101  ASN   A ND2 
2104 N  ND2 B ASN   A 101 ? 0.3457 0.2691 0.2975 0.0396  -0.0650 0.0147  101  ASN   A ND2 
2117 N  N   A LYS   A 102 ? 0.2813 0.3041 0.1877 -0.0739 0.0124  0.0889  102  LYS   A N   
2118 N  N   B LYS   A 102 ? 0.3685 0.3043 0.2853 0.0225  -0.0305 0.0644  102  LYS   A N   
2119 C  CA  A LYS   A 102 ? 0.2926 0.3299 0.2027 -0.0727 0.0100  0.0781  102  LYS   A CA  
2120 C  CA  B LYS   A 102 ? 0.3775 0.3261 0.2888 0.0128  -0.0173 0.0638  102  LYS   A CA  
2121 C  C   A LYS   A 102 ? 0.3053 0.3558 0.1943 -0.0567 0.0147  0.0647  102  LYS   A C   
2122 C  C   B LYS   A 102 ? 0.3765 0.3260 0.2653 0.0116  -0.0172 0.0778  102  LYS   A C   
2123 O  O   A LYS   A 102 ? 0.3094 0.3693 0.2102 -0.0505 0.0199  0.0569  102  LYS   A O   
2124 O  O   B LYS   A 102 ? 0.3802 0.3262 0.2727 0.0129  -0.0087 0.0846  102  LYS   A O   
2125 C  CB  A LYS   A 102 ? 0.2977 0.3296 0.2415 -0.0837 -0.0004 0.0700  102  LYS   A CB  
2126 C  CB  B LYS   A 102 ? 0.3856 0.3439 0.3195 0.0083  -0.0137 0.0461  102  LYS   A CB  
2127 C  CG  A LYS   A 102 ? 0.3036 0.3261 0.2800 -0.0910 -0.0190 0.0529  102  LYS   A CG  
2128 C  CG  B LYS   A 102 ? 0.3928 0.3609 0.3565 0.0030  -0.0113 0.0276  102  LYS   A CG  
2129 C  CD  A LYS   A 102 ? 0.3119 0.3241 0.3244 -0.0952 -0.0354 0.0311  102  LYS   A CD  
2130 C  CD  B LYS   A 102 ? 0.4009 0.3783 0.3979 -0.0011 -0.0101 0.0106  102  LYS   A CD  
2131 C  CE  A LYS   A 102 ? 0.3192 0.3217 0.3577 -0.0953 -0.0457 0.0192  102  LYS   A CE  
2132 C  CE  B LYS   A 102 ? 0.4077 0.3919 0.4307 -0.0036 -0.0135 0.0015  102  LYS   A CE  
2133 N  NZ  A LYS   A 102 ? 0.3219 0.3174 0.3765 -0.1022 -0.0472 0.0116  102  LYS   A NZ  
2134 N  NZ  B LYS   A 102 ? 0.4124 0.4005 0.4541 -0.0045 -0.0144 -0.0053 102  LYS   A NZ  
2161 N  N   A GLY   A 103 ? 0.3126 0.3700 0.2039 -0.0415 0.0116  0.0427  103  GLY   A N   
2162 N  N   B GLY   A 103 ? 0.3697 0.3292 0.2404 0.0116  -0.0301 0.0749  103  GLY   A N   
2163 C  CA  A GLY   A 103 ? 0.3212 0.3810 0.2180 -0.0299 0.0111  0.0224  103  GLY   A CA  
2164 C  CA  B GLY   A 103 ? 0.3607 0.3255 0.2304 0.0128  -0.0356 0.0803  103  GLY   A CA  
2165 C  C   A GLY   A 103 ? 0.3252 0.3932 0.2271 -0.0213 0.0161  0.0112  103  GLY   A C   
2166 C  C   B GLY   A 103 ? 0.3473 0.3186 0.2160 0.0096  -0.0343 0.0759  103  GLY   A C   
2167 O  O   A GLY   A 103 ? 0.3334 0.3979 0.2526 -0.0128 0.0131  0.0026  103  GLY   A O   
2168 O  O   B GLY   A 103 ? 0.3568 0.3227 0.2279 0.0119  -0.0353 0.0778  103  GLY   A O   
2175 N  N   A GLU   A 104 ? 0.3171 0.3975 0.2025 -0.0264 0.0283  0.0069  104  GLU   A N   
2176 N  N   B GLU   A 104 ? 0.3183 0.3038 0.1932 0.0024  -0.0348 0.0707  104  GLU   A N   
2177 C  CA  A GLU   A 104 ? 0.3062 0.3983 0.1975 -0.0355 0.0346  0.0077  104  GLU   A CA  
2178 C  CA  B GLU   A 104 ? 0.2885 0.2870 0.1661 -0.0110 -0.0326 0.0590  104  GLU   A CA  
2179 C  C   A GLU   A 104 ? 0.3079 0.4087 0.1978 -0.0373 0.0233  -0.0079 104  GLU   A C   
2180 C  C   B GLU   A 104 ? 0.2730 0.2803 0.1707 -0.0016 -0.0173 0.0448  104  GLU   A C   
2181 O  O   A GLU   A 104 ? 0.3047 0.4095 0.2031 -0.0390 0.0115  -0.0166 104  GLU   A O   
2182 O  O   B GLU   A 104 ? 0.2681 0.2687 0.1941 0.0011  -0.0218 0.0566  104  GLU   A O   
2183 C  CB  A GLU   A 104 ? 0.2918 0.3884 0.1925 -0.0428 0.0494  0.0259  104  GLU   A CB  
2184 C  CB  B GLU   A 104 ? 0.2756 0.2781 0.1563 -0.0314 -0.0367 0.0591  104  GLU   A CB  
2185 C  CG  A GLU   A 104 ? 0.2807 0.3780 0.2008 -0.0463 0.0576  0.0427  104  GLU   A CG  
2186 C  CG  B GLU   A 104 ? 0.2682 0.2765 0.1652 -0.0424 -0.0411 0.0674  104  GLU   A CG  
2187 C  CD  A GLU   A 104 ? 0.2687 0.3674 0.2005 -0.0489 0.0671  0.0576  104  GLU   A CD  
2188 C  CD  B GLU   A 104 ? 0.2535 0.2724 0.1520 -0.0514 -0.0515 0.0780  104  GLU   A CD  
2189 O  OE1 A GLU   A 104 ? 0.2564 0.3604 0.1742 -0.0489 0.0750  0.0635  104  GLU   A OE1 
2190 O  OE1 B GLU   A 104 ? 0.2408 0.2719 0.1403 -0.0507 -0.0705 0.0748  104  GLU   A OE1 
2191 O  OE2 A GLU   A 104 ? 0.2750 0.3674 0.2247 -0.0469 0.0671  0.0640  104  GLU   A OE2 
2192 O  OE2 B GLU   A 104 ? 0.2614 0.2720 0.1695 -0.0564 -0.0350 0.0752  104  GLU   A OE2 
2205 N  N   A ASP   A 105 ? 0.3123 0.4183 0.2160 -0.0324 0.0227  -0.0223 105  ASP   A N   
2206 N  N   B ASP   A 105 ? 0.2749 0.2871 0.1955 0.0025  -0.0045 0.0223  105  ASP   A N   
2207 C  CA  A ASP   A 105 ? 0.3113 0.4254 0.2427 -0.0288 0.0197  -0.0394 105  ASP   A CA  
2208 C  CA  B ASP   A 105 ? 0.2709 0.2928 0.2224 0.0101  0.0159  -0.0183 105  ASP   A CA  
2209 C  C   A ASP   A 105 ? 0.2840 0.4169 0.2286 -0.0426 0.0084  -0.0524 105  ASP   A C   
2210 C  C   B ASP   A 105 ? 0.2596 0.2859 0.1889 -0.0102 0.0223  -0.0315 105  ASP   A C   
2211 O  O   A ASP   A 105 ? 0.2725 0.4149 0.1938 -0.0442 0.0025  -0.0664 105  ASP   A O   
2212 O  O   B ASP   A 105 ? 0.2455 0.2732 0.1360 -0.0177 0.0255  -0.0434 105  ASP   A O   
2213 C  CB  A ASP   A 105 ? 0.3324 0.4376 0.2904 -0.0126 0.0239  -0.0456 105  ASP   A CB  
2214 C  CB  B ASP   A 105 ? 0.2775 0.3056 0.2824 0.0322  0.0231  -0.0421 105  ASP   A CB  
2215 C  CG  A ASP   A 105 ? 0.3499 0.4465 0.3301 0.0010  0.0219  -0.0540 105  ASP   A CG  
2216 C  CG  B ASP   A 105 ? 0.2834 0.3152 0.3316 0.0495  0.0292  -0.0658 105  ASP   A CG  
2217 O  OD1 A ASP   A 105 ? 0.3549 0.4495 0.3233 0.0050  0.0232  -0.0690 105  ASP   A OD1 
2218 O  OD1 B ASP   A 105 ? 0.2882 0.3159 0.3405 0.0500  0.0251  -0.0743 105  ASP   A OD1 
2219 O  OD2 A ASP   A 105 ? 0.3583 0.4505 0.3641 0.0075  0.0182  -0.0458 105  ASP   A OD2 
2220 O  OD2 B ASP   A 105 ? 0.2837 0.3204 0.3657 0.0575  0.0307  -0.0622 105  ASP   A OD2 
2229 N  N   A ILE   A 106 ? 0.2676 0.4068 0.2449 -0.0561 -0.0102 -0.0550 106  ILE   A N   
2230 N  N   B ILE   A 106 ? 0.2624 0.2973 0.2119 -0.0187 0.0032  -0.0358 106  ILE   A N   
2231 C  CA  A ILE   A 106 ? 0.2432 0.3901 0.2554 -0.0694 -0.0241 -0.0662 106  ILE   A CA  
2232 C  CA  B ILE   A 106 ? 0.2589 0.3104 0.2327 -0.0349 -0.0127 -0.0434 106  ILE   A CA  
2233 C  C   A ILE   A 106 ? 0.2229 0.3633 0.2635 -0.0901 -0.0178 -0.0900 106  ILE   A C   
2234 C  C   B ILE   A 106 ? 0.2585 0.3106 0.2453 -0.0495 -0.0010 -0.0475 106  ILE   A C   
2235 O  O   A ILE   A 106 ? 0.1967 0.3520 0.2655 -0.1022 -0.0089 -0.0986 106  ILE   A O   
2236 O  O   B ILE   A 106 ? 0.2508 0.3110 0.2561 -0.0543 0.0090  -0.0471 106  ILE   A O   
2237 C  CB  A ILE   A 106 ? 0.2498 0.4000 0.2878 -0.0563 -0.0328 -0.0428 106  ILE   A CB  
2238 C  CB  B ILE   A 106 ? 0.2664 0.3291 0.2713 -0.0322 -0.0329 -0.0305 106  ILE   A CB  
2239 C  CG1 A ILE   A 106 ? 0.2462 0.4013 0.3133 -0.0449 -0.0358 -0.0221 106  ILE   A CG1 
2240 C  CG1 B ILE   A 106 ? 0.2650 0.3399 0.2981 -0.0253 -0.0405 -0.0124 106  ILE   A CG1 
2241 C  CG2 A ILE   A 106 ? 0.2563 0.4036 0.2969 -0.0543 -0.0345 -0.0418 106  ILE   A CG2 
2242 C  CG2 B ILE   A 106 ? 0.2722 0.3332 0.2787 -0.0316 -0.0363 -0.0353 106  ILE   A CG2 
2243 C  CD1 A ILE   A 106 ? 0.2456 0.4000 0.3254 -0.0339 -0.0315 -0.0117 106  ILE   A CD1 
2244 C  CD1 B ILE   A 106 ? 0.2652 0.3433 0.3109 -0.0185 -0.0383 -0.0057 106  ILE   A CD1 
2267 N  N   A GLN   A 107 ? 0.2409 0.3501 0.2920 -0.0847 -0.0041 -0.1001 107  GLN   A N   
2268 N  N   B GLN   A 107 ? 0.2712 0.3078 0.2692 -0.0524 0.0075  -0.0561 107  GLN   A N   
2269 C  CA  A GLN   A 107 ? 0.2602 0.3350 0.3567 -0.0699 0.0185  -0.0941 107  GLN   A CA  
2270 C  CA  B GLN   A 107 ? 0.2843 0.3082 0.3383 -0.0535 0.0212  -0.0612 107  GLN   A CA  
2271 C  C   A GLN   A 107 ? 0.2366 0.2888 0.3348 -0.0611 0.0446  -0.0754 107  GLN   A C   
2272 C  C   B GLN   A 107 ? 0.2546 0.2748 0.3249 -0.0567 0.0396  -0.0576 107  GLN   A C   
2273 O  O   A GLN   A 107 ? 0.2339 0.2811 0.3691 -0.0487 0.0645  -0.0769 107  GLN   A O   
2274 O  O   B GLN   A 107 ? 0.2623 0.2678 0.3606 -0.0587 0.0412  -0.0573 107  GLN   A O   
2275 C  CB  A GLN   A 107 ? 0.2967 0.3618 0.4431 -0.0701 0.0091  -0.0948 107  GLN   A CB  
2276 C  CB  B GLN   A 107 ? 0.3197 0.3402 0.4183 -0.0567 0.0110  -0.0656 107  GLN   A CB  
2277 C  CG  A GLN   A 107 ? 0.3327 0.3890 0.5325 -0.0655 0.0000  -0.0867 107  GLN   A CG  
2278 C  CG  B GLN   A 107 ? 0.3535 0.3704 0.5035 -0.0574 0.0019  -0.0642 107  GLN   A CG  
2279 C  CD  A GLN   A 107 ? 0.3615 0.4093 0.6069 -0.0624 -0.0043 -0.0757 107  GLN   A CD  
2280 C  CD  B GLN   A 107 ? 0.3813 0.3959 0.5766 -0.0556 -0.0019 -0.0595 107  GLN   A CD  
2281 O  OE1 A GLN   A 107 ? 0.3746 0.4171 0.6381 -0.0607 -0.0027 -0.0726 107  GLN   A OE1 
2282 O  OE1 B GLN   A 107 ? 0.3937 0.4056 0.6070 -0.0542 0.0001  -0.0584 107  GLN   A OE1 
2283 N  NE2 A GLN   A 107 ? 0.3710 0.4169 0.6318 -0.0634 -0.0084 -0.0732 107  GLN   A NE2 
2284 N  NE2 B GLN   A 107 ? 0.3908 0.4057 0.6012 -0.0573 -0.0058 -0.0599 107  GLN   A NE2 
2301 N  N   . LEU   A 108 ? 0.2156 0.2469 0.2807 -0.0618 0.0470  -0.0645 108  LEU   A N   
2302 C  CA  . LEU   A 108 ? 0.1892 0.1936 0.2377 -0.0271 0.0448  -0.0213 108  LEU   A CA  
2303 C  C   . LEU   A 108 ? 0.1662 0.1514 0.2309 -0.0107 0.0357  0.0064  108  LEU   A C   
2304 O  O   . LEU   A 108 ? 0.1649 0.1497 0.2530 -0.0010 0.0350  0.0078  108  LEU   A O   
2305 C  CB  . LEU   A 108 ? 0.1960 0.2066 0.2170 -0.0268 0.0438  -0.0182 108  LEU   A CB  
2306 C  CG  . LEU   A 108 ? 0.2102 0.2269 0.2365 -0.0226 0.0453  -0.0175 108  LEU   A CG  
2307 C  CD1 . LEU   A 108 ? 0.2291 0.2361 0.2308 -0.0286 0.0534  -0.0098 108  LEU   A CD1 
2308 C  CD2 . LEU   A 108 ? 0.2167 0.2484 0.2818 -0.0124 0.0393  -0.0062 108  LEU   A CD2 
2321 N  N   . LEU   A 109 ? 0.1569 0.1515 0.2248 0.0008  0.0251  0.0222  109  LEU   A N   
2322 C  CA  . LEU   A 109 ? 0.1523 0.1469 0.1978 -0.0005 0.0088  0.0240  109  LEU   A CA  
2323 C  C   . LEU   A 109 ? 0.1401 0.1408 0.1764 -0.0090 0.0059  0.0081  109  LEU   A C   
2324 O  O   . LEU   A 109 ? 0.1484 0.1317 0.2008 -0.0079 -0.0071 0.0041  109  LEU   A O   
2325 C  CB  . LEU   A 109 ? 0.1609 0.1540 0.2123 0.0067  -0.0023 0.0295  109  LEU   A CB  
2326 C  CG  . LEU   A 109 ? 0.1490 0.1614 0.2212 0.0006  0.0046  0.0327  109  LEU   A CG  
2327 C  CD1 . LEU   A 109 ? 0.1593 0.1579 0.2280 0.0044  0.0133  0.0141  109  LEU   A CD1 
2328 C  CD2 . LEU   A 109 ? 0.1509 0.1757 0.2419 0.0034  0.0092  0.0370  109  LEU   A CD2 
2340 N  N   . LYS   A 110 ? 0.1459 0.1377 0.1803 -0.0098 -0.0034 0.0072  110  LYS   A N   
2341 C  CA  . LYS   A 110 ? 0.1408 0.1270 0.2017 -0.0104 -0.0077 0.0134  110  LYS   A CA  
2342 C  C   . LYS   A 110 ? 0.1464 0.1212 0.1861 -0.0090 -0.0028 0.0050  110  LYS   A C   
2343 O  O   . LYS   A 110 ? 0.1406 0.1259 0.1908 -0.0086 0.0028  -0.0041 110  LYS   A O   
2344 C  CB  . LYS   A 110 ? 0.1495 0.1374 0.2180 -0.0020 -0.0153 -0.0001 110  LYS   A CB  
2345 C  CG  . LYS   A 110 ? 0.1530 0.1325 0.2373 0.0012  -0.0197 -0.0021 110  LYS   A CG  
2346 C  CD  . LYS   A 110 ? 0.1611 0.1382 0.2482 -0.0101 -0.0239 -0.0087 110  LYS   A CD  
2347 C  CE  . LYS   A 110 ? 0.1716 0.1419 0.2564 -0.0082 -0.0026 -0.0170 110  LYS   A CE  
2348 N  NZ  . LYS   A 110 ? 0.1733 0.1426 0.2719 -0.0199 0.0078  -0.0112 110  LYS   A NZ  
2362 N  N   . SER   A 111 ? 0.1435 0.1276 0.1848 0.0009  -0.0050 0.0059  111  SER   A N   
2363 C  CA  . SER   A 111 ? 0.1372 0.1313 0.1944 -0.0035 0.0048  0.0083  111  SER   A CA  
2364 C  C   . SER   A 111 ? 0.1337 0.1244 0.1878 -0.0070 0.0072  0.0120  111  SER   A C   
2365 O  O   . SER   A 111 ? 0.1464 0.1178 0.2061 -0.0030 0.0049  0.0070  111  SER   A O   
2366 C  CB  . SER   A 111 ? 0.1544 0.1577 0.2037 -0.0039 0.0132  -0.0088 111  SER   A CB  
2367 O  OG  . SER   A 111 ? 0.2051 0.1728 0.2107 0.0043  0.0167  -0.0126 111  SER   A OG  
2373 N  N   . ALA   A 112 ? 0.1338 0.1219 0.1922 -0.0048 0.0123  0.0087  112  ALA   A N   
2374 C  CA  . ALA   A 112 ? 0.1400 0.1182 0.1804 -0.0087 0.0129  -0.0057 112  ALA   A CA  
2375 C  C   . ALA   A 112 ? 0.1350 0.1164 0.1887 -0.0061 0.0061  -0.0000 112  ALA   A C   
2376 O  O   . ALA   A 112 ? 0.1413 0.1179 0.1909 -0.0146 0.0151  0.0055  112  ALA   A O   
2377 C  CB  . ALA   A 112 ? 0.1523 0.1133 0.1967 -0.0104 0.0075  -0.0033 112  ALA   A CB  
2383 N  N   . TYR   A 113 ? 0.1277 0.1225 0.1882 -0.0045 0.0036  0.0164  113  TYR   A N   
2384 C  CA  . TYR   A 113 ? 0.1245 0.1201 0.1864 -0.0109 0.0019  0.0144  113  TYR   A CA  
2385 C  C   . TYR   A 113 ? 0.1211 0.1219 0.1655 -0.0136 -0.0013 0.0076  113  TYR   A C   
2386 O  O   . TYR   A 113 ? 0.1310 0.1260 0.1777 -0.0074 0.0115  0.0006  113  TYR   A O   
2387 C  CB  . TYR   A 113 ? 0.1240 0.1318 0.1971 -0.0075 -0.0031 0.0212  113  TYR   A CB  
2388 C  CG  . TYR   A 113 ? 0.1309 0.1426 0.1798 -0.0154 0.0052  0.0256  113  TYR   A CG  
2389 C  CD1 . TYR   A 113 ? 0.1290 0.1480 0.1802 -0.0057 0.0065  0.0353  113  TYR   A CD1 
2390 C  CD2 . TYR   A 113 ? 0.1351 0.1443 0.1830 -0.0119 -0.0006 0.0238  113  TYR   A CD2 
2391 C  CE1 . TYR   A 113 ? 0.1350 0.1610 0.1762 -0.0048 0.0072  0.0416  113  TYR   A CE1 
2392 C  CE2 . TYR   A 113 ? 0.1328 0.1545 0.1748 -0.0113 0.0046  0.0293  113  TYR   A CE2 
2393 C  CZ  . TYR   A 113 ? 0.1319 0.1561 0.1708 0.0013  0.0139  0.0410  113  TYR   A CZ  
2394 O  OH  . TYR   A 113 ? 0.1338 0.1688 0.1865 0.0069  0.0080  0.0401  113  TYR   A OH  
2404 N  N   . GLU   A 114 ? 0.1218 0.1212 0.1820 -0.0111 0.0076  0.0095  114  GLU   A N   
2405 C  CA  . GLU   A 114 ? 0.1291 0.1166 0.1999 -0.0054 0.0045  0.0107  114  GLU   A CA  
2406 C  C   . GLU   A 114 ? 0.1297 0.1199 0.1897 -0.0032 0.0102  0.0095  114  GLU   A C   
2407 O  O   . GLU   A 114 ? 0.1392 0.1221 0.1896 -0.0042 -0.0023 0.0101  114  GLU   A O   
2408 C  CB  . GLU   A 114 ? 0.1320 0.1176 0.2053 -0.0082 -0.0048 0.0109  114  GLU   A CB  
2409 C  CG  . GLU   A 114 ? 0.1375 0.1214 0.2153 -0.0021 0.0028  -0.0045 114  GLU   A CG  
2410 C  CD  . GLU   A 114 ? 0.1455 0.1281 0.2131 -0.0096 -0.0021 0.0024  114  GLU   A CD  
2411 O  OE1 . GLU   A 114 ? 0.1474 0.1244 0.2231 -0.0084 0.0069  -0.0034 114  GLU   A OE1 
2412 O  OE2 . GLU   A 114 ? 0.1637 0.1343 0.2281 -0.0129 0.0047  -0.0125 114  GLU   A OE2 
2419 N  N   . ASN   A 115 ? 0.1275 0.1249 0.1778 -0.0087 0.0031  0.0022  115  ASN   A N   
2420 C  CA  . ASN   A 115 ? 0.1269 0.1256 0.1923 -0.0129 0.0097  0.0030  115  ASN   A CA  
2421 C  C   . ASN   A 115 ? 0.1315 0.1192 0.1834 -0.0117 0.0041  0.0059  115  ASN   A C   
2422 O  O   . ASN   A 115 ? 0.1347 0.1364 0.1874 -0.0137 0.0088  0.0132  115  ASN   A O   
2423 C  CB  . ASN   A 115 ? 0.1390 0.1313 0.1829 -0.0137 0.0095  0.0061  115  ASN   A CB  
2424 C  CG  . ASN   A 115 ? 0.1384 0.1466 0.1913 -0.0170 0.0126  0.0080  115  ASN   A CG  
2425 O  OD1 . ASN   A 115 ? 0.1403 0.2381 0.2170 -0.0148 0.0196  0.0252  115  ASN   A OD1 
2426 N  ND2 . ASN   A 115 ? 0.1375 0.1288 0.1854 -0.0157 0.0186  0.0096  115  ASN   A ND2 
2433 N  N   . PHE   A 116 ? 0.1291 0.1255 0.1835 -0.0069 0.0049  0.0139  116  PHE   A N   
2434 C  CA  . PHE   A 116 ? 0.1286 0.1340 0.1728 -0.0059 0.0115  0.0176  116  PHE   A CA  
2435 C  C   . PHE   A 116 ? 0.1282 0.1419 0.1850 -0.0139 0.0083  0.0179  116  PHE   A C   
2436 O  O   . PHE   A 116 ? 0.1326 0.1499 0.1878 -0.0048 0.0062  0.0239  116  PHE   A O   
2437 C  CB  . PHE   A 116 ? 0.1298 0.1278 0.1927 -0.0045 0.0105  0.0165  116  PHE   A CB  
2438 C  CG  . PHE   A 116 ? 0.1302 0.1275 0.1821 -0.0125 0.0068  0.0079  116  PHE   A CG  
2439 C  CD1 . PHE   A 116 ? 0.1378 0.1283 0.1784 -0.0105 0.0128  0.0172  116  PHE   A CD1 
2440 C  CD2 . PHE   A 116 ? 0.1359 0.1356 0.1901 -0.0123 0.0103  0.0154  116  PHE   A CD2 
2441 C  CE1 . PHE   A 116 ? 0.1362 0.1292 0.1872 -0.0175 0.0060  0.0089  116  PHE   A CE1 
2442 C  CE2 . PHE   A 116 ? 0.1342 0.1266 0.2082 -0.0119 0.0099  0.0121  116  PHE   A CE2 
2443 C  CZ  . PHE   A 116 ? 0.1390 0.1203 0.1908 -0.0048 0.0007  0.0141  116  PHE   A CZ  
2453 N  N   . ASN   A 117 ? 0.1326 0.1357 0.1826 -0.0124 0.0065  0.0209  117  ASN   A N   
2454 C  CA  . ASN   A 117 ? 0.1352 0.1305 0.2130 -0.0069 0.0027  0.0294  117  ASN   A CA  
2455 C  C   . ASN   A 117 ? 0.1372 0.1422 0.2144 -0.0062 0.0048  0.0327  117  ASN   A C   
2456 O  O   . ASN   A 117 ? 0.1500 0.1440 0.2316 -0.0063 -0.0076 0.0417  117  ASN   A O   
2457 C  CB  . ASN   A 117 ? 0.1287 0.1329 0.2150 -0.0035 -0.0009 0.0320  117  ASN   A CB  
2458 C  CG  . ASN   A 117 ? 0.1286 0.1336 0.2120 -0.0082 0.0055  0.0297  117  ASN   A CG  
2459 O  OD1 . ASN   A 117 ? 0.1306 0.1535 0.2181 -0.0162 0.0047  0.0255  117  ASN   A OD1 
2460 N  ND2 . ASN   A 117 ? 0.1233 0.1355 0.2077 -0.0063 0.0023  0.0319  117  ASN   A ND2 
2467 N  N   . GLN   A 118 ? 0.1281 0.1412 0.2159 -0.0106 -0.0132 0.0271  118  GLN   A N   
2468 C  CA  . GLN   A 118 ? 0.1440 0.1523 0.2144 -0.0177 -0.0167 0.0232  118  GLN   A CA  
2469 C  C   . GLN   A 118 ? 0.1437 0.1545 0.2038 -0.0151 -0.0114 0.0244  118  GLN   A C   
2470 O  O   . GLN   A 118 ? 0.1468 0.1901 0.2270 -0.0087 -0.0283 0.0144  118  GLN   A O   
2471 C  CB  . GLN   A 118 ? 0.1417 0.1520 0.2187 -0.0112 -0.0093 0.0253  118  GLN   A CB  
2472 C  CG  . GLN   A 118 ? 0.1381 0.1511 0.2237 -0.0060 -0.0062 0.0229  118  GLN   A CG  
2473 C  CD  . GLN   A 118 ? 0.1328 0.1566 0.2393 -0.0036 -0.0003 0.0178  118  GLN   A CD  
2474 O  OE1 . GLN   A 118 ? 0.1322 0.1740 0.2638 0.0033  -0.0082 0.0124  118  GLN   A OE1 
2475 N  NE2 . GLN   A 118 ? 0.1404 0.1548 0.2295 -0.0019 -0.0023 0.0250  118  GLN   A NE2 
2484 N  N   . HIS   A 119 ? 0.1451 0.1482 0.1939 -0.0104 -0.0066 0.0304  119  HIS   A N   
2485 C  CA  . HIS   A 119 ? 0.1536 0.1655 0.1961 -0.0093 -0.0106 0.0362  119  HIS   A CA  
2486 C  C   . HIS   A 119 ? 0.1647 0.1771 0.1953 -0.0170 -0.0021 0.0430  119  HIS   A C   
2487 O  O   . HIS   A 119 ? 0.1649 0.1808 0.2083 -0.0307 -0.0040 0.0409  119  HIS   A O   
2488 C  CB  . HIS   A 119 ? 0.1585 0.1622 0.2048 -0.0064 0.0103  0.0377  119  HIS   A CB  
2489 C  CG  . HIS   A 119 ? 0.1594 0.1673 0.2545 -0.0041 0.0100  0.0400  119  HIS   A CG  
2490 N  ND1 . HIS   A 119 ? 0.1710 0.1815 0.3057 -0.0132 0.0154  0.0330  119  HIS   A ND1 
2491 C  CD2 . HIS   A 119 ? 0.1694 0.1727 0.2675 0.0098  0.0255  0.0568  119  HIS   A CD2 
2492 C  CE1 . HIS   A 119 ? 0.1687 0.1799 0.3226 -0.0160 0.0248  0.0571  119  HIS   A CE1 
2493 N  NE2 . HIS   A 119 ? 0.1769 0.1772 0.3063 0.0029  0.0406  0.0689  119  HIS   A NE2 
2501 N  N   . GLU   A 120 ? 0.1819 0.2058 0.1925 -0.0131 -0.0144 0.0593  120  GLU   A N   
2502 C  CA  . GLU   A 120 ? 0.2024 0.2391 0.2079 -0.0097 -0.0114 0.1011  120  GLU   A CA  
2503 C  C   . GLU   A 120 ? 0.1802 0.2235 0.1950 -0.0241 -0.0100 0.0854  120  GLU   A C   
2504 O  O   . GLU   A 120 ? 0.1786 0.2143 0.2006 -0.0222 -0.0102 0.0831  120  GLU   A O   
2505 C  CB  . GLU   A 120 ? 0.2753 0.3069 0.2759 0.0026  0.0023  0.1458  120  GLU   A CB  
2506 C  CG  . GLU   A 120 ? 0.3686 0.3821 0.3902 0.0145  0.0100  0.1473  120  GLU   A CG  
2507 C  CD  . GLU   A 120 ? 0.4351 0.4371 0.5059 0.0243  0.0202  0.1385  120  GLU   A CD  
2508 O  OE1 . GLU   A 120 ? 0.4633 0.4602 0.5306 0.0267  0.0248  0.1354  120  GLU   A OE1 
2509 O  OE2 . GLU   A 120 ? 0.4943 0.4943 0.5639 0.0276  0.0225  0.1316  120  GLU   A OE2 
2516 N  N   . VAL   A 121 ? 0.1753 0.2268 0.1709 -0.0263 -0.0002 0.0655  121  VAL   A N   
2517 C  CA  . VAL   A 121 ? 0.1826 0.2282 0.1640 -0.0278 0.0093  0.0668  121  VAL   A CA  
2518 C  C   . VAL   A 121 ? 0.1694 0.2079 0.1417 -0.0309 0.0026  0.0517  121  VAL   A C   
2519 O  O   . VAL   A 121 ? 0.1704 0.2095 0.1769 -0.0413 -0.0163 0.0429  121  VAL   A O   
2520 C  CB  . VAL   A 121 ? 0.2248 0.2654 0.2073 -0.0181 0.0263  0.0752  121  VAL   A CB  
2521 C  CG1 . VAL   A 121 ? 0.2310 0.2825 0.2123 -0.0126 0.0411  0.0728  121  VAL   A CG1 
2522 C  CG2 . VAL   A 121 ? 0.2425 0.2843 0.2527 -0.0239 0.0183  0.0561  121  VAL   A CG2 
2532 N  N   . LEU   A 122 ? 0.1613 0.1860 0.1538 -0.0314 0.0049  0.0453  122  LEU   A N   
2533 C  CA  . LEU   A 122 ? 0.1652 0.1702 0.1634 -0.0297 0.0191  0.0408  122  LEU   A CA  
2534 C  C   . LEU   A 122 ? 0.1618 0.1700 0.1698 -0.0336 0.0070  0.0343  122  LEU   A C   
2535 O  O   . LEU   A 122 ? 0.1615 0.1783 0.1951 -0.0413 0.0027  0.0380  122  LEU   A O   
2536 C  CB  . LEU   A 122 ? 0.1889 0.1747 0.1967 -0.0224 0.0124  0.0488  122  LEU   A CB  
2537 C  CG  . LEU   A 122 ? 0.1916 0.1779 0.1932 -0.0191 0.0210  0.0358  122  LEU   A CG  
2538 C  CD1 . LEU   A 122 ? 0.2040 0.1729 0.2067 -0.0317 0.0229  0.0425  122  LEU   A CD1 
2539 C  CD2 . LEU   A 122 ? 0.1843 0.1650 0.1757 -0.0160 0.0257  0.0317  122  LEU   A CD2 
2551 N  N   A LEU   A 123 ? 0.1548 0.1680 0.1570 -0.0303 0.0039  0.0357  123  LEU   A N   
2552 N  N   B LEU   A 123 ? 0.1552 0.1685 0.1579 -0.0300 -0.0024 0.0299  123  LEU   A N   
2553 C  CA  A LEU   A 123 ? 0.1529 0.1699 0.1502 -0.0271 0.0109  0.0420  123  LEU   A CA  
2554 C  CA  B LEU   A 123 ? 0.1541 0.1707 0.1553 -0.0252 -0.0005 0.0297  123  LEU   A CA  
2555 C  C   A LEU   A 123 ? 0.1460 0.1510 0.1474 -0.0212 0.0007  0.0416  123  LEU   A C   
2556 C  C   B LEU   A 123 ? 0.1504 0.1564 0.1466 -0.0190 -0.0017 0.0260  123  LEU   A C   
2557 O  O   A LEU   A 123 ? 0.1347 0.1477 0.1683 -0.0213 0.0118  0.0264  123  LEU   A O   
2558 O  O   B LEU   A 123 ? 0.1404 0.1572 0.1459 -0.0207 0.0099  0.0234  123  LEU   A O   
2559 C  CB  A LEU   A 123 ? 0.1586 0.1847 0.1483 -0.0309 0.0321  0.0372  123  LEU   A CB  
2560 C  CB  B LEU   A 123 ? 0.1593 0.1818 0.1654 -0.0282 0.0076  0.0243  123  LEU   A CB  
2561 C  CG  A LEU   A 123 ? 0.1644 0.1985 0.1619 -0.0243 0.0286  0.0212  123  LEU   A CG  
2562 C  CG  B LEU   A 123 ? 0.1629 0.1885 0.1682 -0.0250 0.0082  0.0175  123  LEU   A CG  
2563 C  CD1 A LEU   A 123 ? 0.1631 0.2049 0.1707 -0.0170 0.0176  0.0113  123  LEU   A CD1 
2564 C  CD1 B LEU   A 123 ? 0.1629 0.1905 0.1884 -0.0160 0.0051  0.0132  123  LEU   A CD1 
2565 C  CD2 A LEU   A 123 ? 0.1716 0.2073 0.1710 -0.0235 0.0226  0.0174  123  LEU   A CD2 
2566 C  CD2 B LEU   A 123 ? 0.1703 0.1974 0.1713 -0.0258 0.0021  0.0081  123  LEU   A CD2 
2589 N  N   A ALA   A 124 ? 0.1373 0.1366 0.1362 -0.0188 0.0007  0.0528  124  ALA   A N   
2590 N  N   B ALA   A 124 ? 0.1484 0.1424 0.1562 -0.0154 -0.0009 0.0163  124  ALA   A N   
2591 C  CA  A ALA   A 124 ? 0.1259 0.1321 0.1256 -0.0088 -0.0006 0.0458  124  ALA   A CA  
2592 C  CA  B ALA   A 124 ? 0.1483 0.1450 0.1732 -0.0197 -0.0002 0.0255  124  ALA   A CA  
2593 C  C   A ALA   A 124 ? 0.1224 0.1339 0.1324 -0.0105 0.0128  0.0283  124  ALA   A C   
2594 C  C   B ALA   A 124 ? 0.1402 0.1393 0.1629 -0.0190 0.0062  0.0244  124  ALA   A C   
2595 O  O   A ALA   A 124 ? 0.1274 0.1437 0.1446 -0.0132 0.0263  0.0376  124  ALA   A O   
2596 O  O   B ALA   A 124 ? 0.1393 0.1349 0.1933 -0.0101 0.0100  0.0148  124  ALA   A O   
2597 C  CB  A ALA   A 124 ? 0.1218 0.1280 0.1488 -0.0037 -0.0063 0.0364  124  ALA   A CB  
2598 C  CB  B ALA   A 124 ? 0.1582 0.1485 0.1996 -0.0191 -0.0024 0.0225  124  ALA   A CB  
2609 N  N   A PRO   A 125 ? 0.1227 0.1419 0.1639 -0.0054 0.0097  0.0211  125  PRO   A N   
2610 N  N   B PRO   A 125 ? 0.1290 0.1432 0.1412 -0.0109 0.0121  0.0400  125  PRO   A N   
2611 C  CA  A PRO   A 125 ? 0.1281 0.1399 0.1781 -0.0109 -0.0024 0.0178  125  PRO   A CA  
2612 C  CA  B PRO   A 125 ? 0.1349 0.1510 0.1456 -0.0134 0.0204  0.0338  125  PRO   A CA  
2613 C  C   A PRO   A 125 ? 0.1185 0.1343 0.1761 -0.0106 0.0036  0.0315  125  PRO   A C   
2614 C  C   B PRO   A 125 ? 0.1430 0.1632 0.1667 -0.0131 0.0194  0.0286  125  PRO   A C   
2615 O  O   A PRO   A 125 ? 0.1192 0.1297 0.1819 -0.0091 -0.0003 0.0338  125  PRO   A O   
2616 O  O   B PRO   A 125 ? 0.1486 0.1639 0.1756 -0.0144 0.0063  0.0186  125  PRO   A O   
2617 C  CB  A PRO   A 125 ? 0.1385 0.1434 0.1801 -0.0139 -0.0140 0.0044  125  PRO   A CB  
2618 C  CB  B PRO   A 125 ? 0.1248 0.1414 0.1307 -0.0158 0.0166  0.0359  125  PRO   A CB  
2619 C  CG  A PRO   A 125 ? 0.1459 0.1444 0.1878 -0.0097 -0.0055 0.0210  125  PRO   A CG  
2620 C  CG  B PRO   A 125 ? 0.1202 0.1344 0.1414 -0.0060 0.0184  0.0374  125  PRO   A CG  
2621 C  CD  A PRO   A 125 ? 0.1314 0.1454 0.1759 -0.0035 0.0087  0.0185  125  PRO   A CD  
2622 C  CD  B PRO   A 125 ? 0.1190 0.1276 0.1427 -0.0107 0.0267  0.0341  125  PRO   A CD  
2637 N  N   A LEU   A 126 ? 0.1125 0.1399 0.1692 -0.0062 0.0025  0.0355  126  LEU   A N   
2638 N  N   B LEU   A 126 ? 0.1516 0.1718 0.1867 -0.0079 0.0116  0.0251  126  LEU   A N   
2639 C  CA  A LEU   A 126 ? 0.1170 0.1451 0.1571 -0.0087 0.0011  0.0300  126  LEU   A CA  
2640 C  CA  B LEU   A 126 ? 0.1486 0.1739 0.2054 -0.0137 0.0075  0.0306  126  LEU   A CA  
2641 C  C   A LEU   A 126 ? 0.1324 0.1416 0.1466 0.0031  -0.0060 0.0323  126  LEU   A C   
2642 C  C   B LEU   A 126 ? 0.1433 0.1575 0.1816 -0.0030 0.0089  0.0239  126  LEU   A C   
2643 O  O   A LEU   A 126 ? 0.1445 0.1518 0.1790 0.0152  0.0059  0.0369  126  LEU   A O   
2644 O  O   B LEU   A 126 ? 0.1504 0.1573 0.1893 0.0078  0.0115  0.0246  126  LEU   A O   
2645 C  CB  A LEU   A 126 ? 0.1166 0.1522 0.1410 -0.0154 0.0042  0.0260  126  LEU   A CB  
2646 C  CB  B LEU   A 126 ? 0.1679 0.2050 0.2722 -0.0212 -0.0019 0.0369  126  LEU   A CB  
2647 C  CG  A LEU   A 126 ? 0.1129 0.1749 0.1422 -0.0211 0.0057  0.0266  126  LEU   A CG  
2648 C  CG  B LEU   A 126 ? 0.1901 0.2270 0.3387 -0.0212 -0.0247 0.0293  126  LEU   A CG  
2649 C  CD1 A LEU   A 126 ? 0.1205 0.1896 0.1516 -0.0193 0.0007  0.0208  126  LEU   A CD1 
2650 C  CD1 B LEU   A 126 ? 0.1848 0.2276 0.3577 -0.0237 -0.0317 0.0278  126  LEU   A CD1 
2651 C  CD2 A LEU   A 126 ? 0.1241 0.1641 0.1674 -0.0216 0.0109  0.0336  126  LEU   A CD2 
2652 C  CD2 B LEU   A 126 ? 0.1962 0.2288 0.3480 -0.0267 -0.0330 0.0249  126  LEU   A CD2 
2675 N  N   A LEU   A 127 ? 0.1350 0.1423 0.1533 0.0029  -0.0010 0.0211  127  LEU   A N   
2676 N  N   B LEU   A 127 ? 0.1370 0.1521 0.1637 -0.0009 0.0065  0.0247  127  LEU   A N   
2677 C  CA  A LEU   A 127 ? 0.1399 0.1434 0.1445 -0.0012 0.0001  0.0189  127  LEU   A CA  
2678 C  CA  B LEU   A 127 ? 0.1307 0.1477 0.1456 0.0058  -0.0004 0.0321  127  LEU   A CA  
2679 C  C   A LEU   A 127 ? 0.1389 0.1326 0.1289 -0.0023 -0.0052 0.0219  127  LEU   A C   
2680 C  C   B LEU   A 127 ? 0.1320 0.1422 0.1512 -0.0023 -0.0025 0.0138  127  LEU   A C   
2681 O  O   A LEU   A 127 ? 0.1454 0.1309 0.1475 -0.0117 -0.0111 0.0258  127  LEU   A O   
2682 O  O   B LEU   A 127 ? 0.1404 0.1455 0.1718 -0.0141 0.0122  0.0135  127  LEU   A O   
2683 C  CB  A LEU   A 127 ? 0.1414 0.1482 0.1560 0.0034  0.0041  0.0162  127  LEU   A CB  
2684 C  CB  B LEU   A 127 ? 0.1376 0.1663 0.1407 0.0095  0.0081  0.0305  127  LEU   A CB  
2685 C  CG  A LEU   A 127 ? 0.1459 0.1413 0.1654 0.0021  -0.0103 0.0152  127  LEU   A CG  
2686 C  CG  B LEU   A 127 ? 0.1419 0.1853 0.1523 0.0078  -0.0001 0.0393  127  LEU   A CG  
2687 C  CD1 A LEU   A 127 ? 0.1454 0.1321 0.1783 -0.0038 -0.0114 0.0097  127  LEU   A CD1 
2688 C  CD1 B LEU   A 127 ? 0.1488 0.1937 0.1789 0.0136  0.0058  0.0448  127  LEU   A CD1 
2689 C  CD2 A LEU   A 127 ? 0.1558 0.1331 0.1830 0.0059  -0.0149 0.0164  127  LEU   A CD2 
2690 C  CD2 B LEU   A 127 ? 0.1538 0.2033 0.1462 0.0045  -0.0123 0.0238  127  LEU   A CD2 
2713 N  N   A SER   A 128 ? 0.1457 0.1356 0.1164 -0.0082 -0.0028 0.0240  128  SER   A N   
2714 N  N   B SER   A 128 ? 0.1379 0.1425 0.1552 -0.0093 -0.0073 0.0111  128  SER   A N   
2715 C  CA  A SER   A 128 ? 0.1512 0.1399 0.1239 -0.0034 0.0094  0.0243  128  SER   A CA  
2716 C  CA  B SER   A 128 ? 0.1380 0.1379 0.1423 -0.0084 -0.0063 0.0030  128  SER   A CA  
2717 C  C   A SER   A 128 ? 0.1577 0.1502 0.1517 0.0062  0.0217  0.0216  128  SER   A C   
2718 C  C   B SER   A 128 ? 0.1404 0.1337 0.1360 -0.0078 -0.0203 0.0074  128  SER   A C   
2719 O  O   A SER   A 128 ? 0.1638 0.1689 0.1697 0.0063  0.0296  0.0153  128  SER   A O   
2720 O  O   B SER   A 128 ? 0.1353 0.1395 0.1368 -0.0073 -0.0251 0.0008  128  SER   A O   
2721 C  CB  A SER   A 128 ? 0.1445 0.1326 0.1197 -0.0059 -0.0044 0.0343  128  SER   A CB  
2722 C  CB  B SER   A 128 ? 0.1409 0.1431 0.1495 -0.0033 -0.0139 0.0037  128  SER   A CB  
2723 O  OG  A SER   A 128 ? 0.1534 0.1448 0.1362 -0.0059 0.0069  0.0218  128  SER   A OG  
2724 O  OG  B SER   A 128 ? 0.1417 0.1563 0.1690 -0.0023 -0.0055 0.0073  128  SER   A OG  
2735 N  N   A ALA   A 129 ? 0.1593 0.1584 0.1686 0.0008  0.0163  0.0292  129  ALA   A N   
2736 N  N   B ALA   A 129 ? 0.1459 0.1401 0.1421 -0.0088 -0.0261 0.0138  129  ALA   A N   
2737 C  CA  A ALA   A 129 ? 0.1539 0.1527 0.1690 -0.0025 0.0126  0.0258  129  ALA   A CA  
2738 C  CA  B ALA   A 129 ? 0.1507 0.1395 0.1527 -0.0090 -0.0102 0.0095  129  ALA   A CA  
2739 C  C   A ALA   A 129 ? 0.1536 0.1466 0.1704 -0.0065 0.0067  0.0154  129  ALA   A C   
2740 C  C   B ALA   A 129 ? 0.1577 0.1454 0.1429 -0.0058 -0.0139 0.0034  129  ALA   A C   
2741 O  O   A ALA   A 129 ? 0.1615 0.1533 0.1696 -0.0168 0.0071  0.0224  129  ALA   A O   
2742 O  O   B ALA   A 129 ? 0.1643 0.1497 0.1271 -0.0064 -0.0262 0.0188  129  ALA   A O   
2743 C  CB  A ALA   A 129 ? 0.1566 0.1577 0.1782 0.0056  0.0148  0.0206  129  ALA   A CB  
2744 C  CB  B ALA   A 129 ? 0.1484 0.1449 0.1543 -0.0110 -0.0068 0.0179  129  ALA   A CB  
2755 N  N   A GLY   A 130 ? 0.1572 0.1376 0.1903 -0.0005 0.0084  0.0001  130  GLY   A N   
2756 N  N   B GLY   A 130 ? 0.1625 0.1441 0.1488 -0.0092 -0.0096 0.0069  130  GLY   A N   
2757 C  CA  A GLY   A 130 ? 0.1713 0.1330 0.1935 0.0028  0.0032  -0.0030 130  GLY   A CA  
2758 C  CA  B GLY   A 130 ? 0.1806 0.1470 0.1588 -0.0145 -0.0245 0.0025  130  GLY   A CA  
2759 C  C   A GLY   A 130 ? 0.1728 0.1314 0.1861 0.0073  -0.0031 0.0080  130  GLY   A C   
2760 C  C   B GLY   A 130 ? 0.1858 0.1483 0.1510 -0.0137 -0.0406 0.0000  130  GLY   A C   
2761 O  O   A GLY   A 130 ? 0.1835 0.1317 0.1896 0.0031  0.0028  -0.0024 130  GLY   A O   
2762 O  O   B GLY   A 130 ? 0.1955 0.1524 0.1640 -0.0142 -0.0591 0.0013  130  GLY   A O   
2769 N  N   A ILE   A 131 ? 0.1770 0.1376 0.1722 0.0018  -0.0159 0.0249  131  ILE   A N   
2770 N  N   B ILE   A 131 ? 0.1924 0.1469 0.1528 -0.0128 -0.0195 -0.0036 131  ILE   A N   
2771 C  CA  A ILE   A 131 ? 0.1864 0.1392 0.1626 -0.0073 -0.0290 0.0277  131  ILE   A CA  
2772 C  CA  B ILE   A 131 ? 0.2071 0.1474 0.1389 -0.0165 -0.0133 -0.0069 131  ILE   A CA  
2773 C  C   A ILE   A 131 ? 0.1797 0.1464 0.1511 -0.0094 -0.0325 0.0372  131  ILE   A C   
2774 C  C   B ILE   A 131 ? 0.2009 0.1461 0.1329 -0.0166 -0.0156 0.0022  131  ILE   A C   
2775 O  O   A ILE   A 131 ? 0.1893 0.1548 0.1638 -0.0049 -0.0273 0.0420  131  ILE   A O   
2776 O  O   B ILE   A 131 ? 0.2078 0.1406 0.1527 -0.0148 -0.0192 0.0080  131  ILE   A O   
2777 C  CB  A ILE   A 131 ? 0.2039 0.1560 0.1831 -0.0230 -0.0240 0.0117  131  ILE   A CB  
2778 C  CB  B ILE   A 131 ? 0.2224 0.1648 0.1591 -0.0242 0.0009  -0.0123 131  ILE   A CB  
2779 C  CG1 A ILE   A 131 ? 0.2096 0.1778 0.1730 -0.0350 -0.0172 0.0082  131  ILE   A CG1 
2780 C  CG1 B ILE   A 131 ? 0.2275 0.1910 0.1556 -0.0339 0.0023  -0.0204 131  ILE   A CG1 
2781 C  CG2 A ILE   A 131 ? 0.2053 0.1516 0.2026 -0.0244 -0.0259 0.0029  131  ILE   A CG2 
2782 C  CG2 B ILE   A 131 ? 0.2315 0.1567 0.1907 -0.0200 0.0014  -0.0121 131  ILE   A CG2 
2783 C  CD1 A ILE   A 131 ? 0.2187 0.1921 0.1849 -0.0446 -0.0098 -0.0050 131  ILE   A CD1 
2784 C  CD1 B ILE   A 131 ? 0.2309 0.2084 0.1741 -0.0393 0.0022  -0.0230 131  ILE   A CD1 
2807 N  N   A PHE   A 132 ? 0.1691 0.1421 0.1416 -0.0052 -0.0282 0.0330  132  PHE   A N   
2808 N  N   B PHE   A 132 ? 0.1938 0.1460 0.1309 -0.0095 -0.0071 0.0095  132  PHE   A N   
2809 C  CA  A PHE   A 132 ? 0.1693 0.1473 0.1414 -0.0071 -0.0210 0.0189  132  PHE   A CA  
2810 C  CA  B PHE   A 132 ? 0.1984 0.1556 0.1353 -0.0072 -0.0073 -0.0020 132  PHE   A CA  
2811 C  C   A PHE   A 132 ? 0.1754 0.1581 0.1403 -0.0151 -0.0199 0.0205  132  PHE   A C   
2812 C  C   B PHE   A 132 ? 0.2086 0.1677 0.1453 -0.0136 -0.0129 0.0014  132  PHE   A C   
2813 O  O   A PHE   A 132 ? 0.1810 0.1681 0.1517 -0.0204 -0.0223 0.0127  132  PHE   A O   
2814 O  O   B PHE   A 132 ? 0.2246 0.1802 0.1599 -0.0188 -0.0151 -0.0087 132  PHE   A O   
2815 C  CB  A PHE   A 132 ? 0.1602 0.1438 0.1401 -0.0100 -0.0211 0.0247  132  PHE   A CB  
2816 C  CB  B PHE   A 132 ? 0.1897 0.1529 0.1264 -0.0033 -0.0047 -0.0092 132  PHE   A CB  
2817 C  CG  A PHE   A 132 ? 0.1644 0.1429 0.1463 -0.0071 -0.0216 0.0190  132  PHE   A CG  
2818 C  CG  B PHE   A 132 ? 0.1846 0.1547 0.1233 0.0012  -0.0068 -0.0096 132  PHE   A CG  
2819 C  CD1 A PHE   A 132 ? 0.1695 0.1601 0.1621 0.0028  -0.0184 0.0054  132  PHE   A CD1 
2820 C  CD1 B PHE   A 132 ? 0.1838 0.1686 0.1387 0.0014  -0.0056 -0.0088 132  PHE   A CD1 
2821 C  CD2 A PHE   A 132 ? 0.1705 0.1571 0.1682 0.0011  -0.0326 0.0129  132  PHE   A CD2 
2822 C  CD2 B PHE   A 132 ? 0.1843 0.1630 0.1340 0.0078  -0.0096 -0.0232 132  PHE   A CD2 
2823 C  CE1 A PHE   A 132 ? 0.1729 0.1644 0.1678 0.0018  -0.0280 -0.0039 132  PHE   A CE1 
2824 C  CE1 B PHE   A 132 ? 0.1797 0.1727 0.1411 0.0038  -0.0055 -0.0135 132  PHE   A CE1 
2825 C  CE2 A PHE   A 132 ? 0.1686 0.1668 0.1827 0.0037  -0.0326 0.0073  132  PHE   A CE2 
2826 C  CE2 B PHE   A 132 ? 0.1765 0.1698 0.1494 0.0173  0.0002  -0.0192 132  PHE   A CE2 
2827 C  CZ  A PHE   A 132 ? 0.1686 0.1663 0.1728 -0.0008 -0.0410 0.0000  132  PHE   A CZ  
2828 C  CZ  B PHE   A 132 ? 0.1741 0.1708 0.1390 0.0092  -0.0064 -0.0123 132  PHE   A CZ  
2847 N  N   A GLY   A 133 ? 0.1821 0.1628 0.1487 -0.0129 -0.0327 0.0206  133  GLY   A N   
2848 N  N   B GLY   A 133 ? 0.2058 0.1726 0.1524 -0.0116 -0.0297 0.0058  133  GLY   A N   
2849 C  CA  A GLY   A 133 ? 0.1884 0.1755 0.1515 -0.0152 -0.0296 0.0173  133  GLY   A CA  
2850 C  CA  B GLY   A 133 ? 0.2001 0.1853 0.1559 -0.0154 -0.0281 -0.0009 133  GLY   A CA  
2851 C  C   A GLY   A 133 ? 0.1887 0.1844 0.1500 -0.0155 -0.0382 0.0138  133  GLY   A C   
2852 C  C   B GLY   A 133 ? 0.1894 0.1969 0.1552 -0.0149 -0.0435 -0.0064 133  GLY   A C   
2853 O  O   A GLY   A 133 ? 0.1925 0.1979 0.1653 -0.0178 -0.0391 0.0026  133  GLY   A O   
2854 O  O   B GLY   A 133 ? 0.1841 0.2062 0.1784 -0.0112 -0.0485 -0.0214 133  GLY   A O   
2861 N  N   A ALA   A 134 ? 0.1835 0.1677 0.1459 -0.0145 -0.0210 0.0065  134  ALA   A N   
2862 N  N   B ALA   A 134 ? 0.1832 0.1892 0.1425 -0.0174 -0.0310 -0.0076 134  ALA   A N   
2863 C  CA  A ALA   A 134 ? 0.1816 0.1654 0.1641 -0.0081 -0.0169 -0.0046 134  ALA   A CA  
2864 C  CA  B ALA   A 134 ? 0.1803 0.1918 0.1463 -0.0235 -0.0307 -0.0068 134  ALA   A CA  
2865 C  C   A ALA   A 134 ? 0.1871 0.1694 0.1760 -0.0072 -0.0175 0.0042  134  ALA   A C   
2866 C  C   B ALA   A 134 ? 0.1791 0.1994 0.1592 -0.0258 -0.0247 0.0095  134  ALA   A C   
2867 O  O   A ALA   A 134 ? 0.2026 0.1796 0.1863 -0.0050 0.0069  0.0103  134  ALA   A O   
2868 O  O   B ALA   A 134 ? 0.1921 0.2092 0.1677 -0.0253 -0.0103 0.0113  134  ALA   A O   
2869 C  CB  A ALA   A 134 ? 0.1854 0.1615 0.1778 -0.0038 -0.0102 -0.0059 134  ALA   A CB  
2870 C  CB  B ALA   A 134 ? 0.1889 0.1876 0.1680 -0.0234 -0.0175 -0.0086 134  ALA   A CB  
2881 N  N   A ASP   A 135 ? 0.1860 0.1758 0.1875 -0.0125 -0.0191 0.0144  135  ASP   A N   
2882 N  N   B ASP   A 135 ? 0.1770 0.2033 0.1858 -0.0244 -0.0214 0.0219  135  ASP   A N   
2883 C  CA  A ASP   A 135 ? 0.1810 0.1926 0.2119 -0.0248 -0.0348 0.0323  135  ASP   A CA  
2884 C  CA  B ASP   A 135 ? 0.1736 0.2147 0.2123 -0.0316 -0.0302 0.0372  135  ASP   A CA  
2885 C  C   A ASP   A 135 ? 0.1723 0.1857 0.2128 -0.0130 -0.0313 0.0458  135  ASP   A C   
2886 C  C   B ASP   A 135 ? 0.1673 0.2043 0.2180 -0.0314 -0.0213 0.0428  135  ASP   A C   
2887 O  O   A ASP   A 135 ? 0.1721 0.1781 0.2181 -0.0057 -0.0301 0.0444  135  ASP   A O   
2888 O  O   B ASP   A 135 ? 0.1612 0.1884 0.2167 -0.0401 -0.0115 0.0411  135  ASP   A O   
2889 C  CB  A ASP   A 135 ? 0.1912 0.2253 0.2492 -0.0440 -0.0578 0.0275  135  ASP   A CB  
2890 C  CB  B ASP   A 135 ? 0.1884 0.2399 0.2574 -0.0362 -0.0409 0.0368  135  ASP   A CB  
2891 C  CG  A ASP   A 135 ? 0.2010 0.2616 0.2848 -0.0530 -0.0715 0.0253  135  ASP   A CG  
2892 C  CG  B ASP   A 135 ? 0.2024 0.2622 0.3080 -0.0335 -0.0442 0.0347  135  ASP   A CG  
2893 O  OD1 A ASP   A 135 ? 0.2006 0.2773 0.2994 -0.0515 -0.0727 0.0401  135  ASP   A OD1 
2894 O  OD1 B ASP   A 135 ? 0.2074 0.2790 0.3132 -0.0379 -0.0467 0.0389  135  ASP   A OD1 
2895 O  OD2 A ASP   A 135 ? 0.2145 0.2784 0.3125 -0.0572 -0.0746 0.0222  135  ASP   A OD2 
2896 O  OD2 B ASP   A 135 ? 0.2185 0.2724 0.3529 -0.0269 -0.0268 0.0392  135  ASP   A OD2 
2905 N  N   A PRO   A 136 ? 0.1661 0.1861 0.2230 -0.0028 -0.0249 0.0597  136  PRO   A N   
2906 N  N   B PRO   A 136 ? 0.1654 0.2063 0.2366 -0.0144 -0.0107 0.0500  136  PRO   A N   
2907 C  CA  A PRO   A 136 ? 0.1583 0.1877 0.2357 -0.0060 -0.0153 0.0572  136  PRO   A CA  
2908 C  CA  B PRO   A 136 ? 0.1569 0.2017 0.2394 -0.0107 -0.0030 0.0446  136  PRO   A CA  
2909 C  C   A PRO   A 136 ? 0.1382 0.1848 0.2296 -0.0045 -0.0122 0.0544  136  PRO   A C   
2910 C  C   B PRO   A 136 ? 0.1427 0.1911 0.2421 -0.0057 -0.0007 0.0401  136  PRO   A C   
2911 O  O   A PRO   A 136 ? 0.1330 0.1854 0.2261 -0.0061 -0.0097 0.0512  136  PRO   A O   
2912 O  O   B PRO   A 136 ? 0.1391 0.1844 0.2432 -0.0106 0.0052  0.0359  136  PRO   A O   
2913 C  CB  A PRO   A 136 ? 0.1728 0.1894 0.2528 -0.0013 -0.0187 0.0538  136  PRO   A CB  
2914 C  CB  B PRO   A 136 ? 0.1699 0.2077 0.2473 -0.0030 -0.0032 0.0429  136  PRO   A CB  
2915 C  CG  A PRO   A 136 ? 0.1830 0.1941 0.2587 0.0049  -0.0194 0.0525  136  PRO   A CG  
2916 C  CG  B PRO   A 136 ? 0.1801 0.2143 0.2598 0.0003  -0.0046 0.0420  136  PRO   A CG  
2917 C  CD  A PRO   A 136 ? 0.1715 0.1852 0.2295 0.0055  -0.0223 0.0698  136  PRO   A CD  
2918 C  CD  B PRO   A 136 ? 0.1773 0.2113 0.2504 -0.0027 -0.0040 0.0553  136  PRO   A CD  
2933 N  N   A ILE   A 137 ? 0.1393 0.1862 0.2402 -0.0083 -0.0164 0.0547  137  ILE   A N   
2934 N  N   B ILE   A 137 ? 0.1459 0.1900 0.2514 -0.0051 -0.0107 0.0395  137  ILE   A N   
2935 C  CA  A ILE   A 137 ? 0.1436 0.1960 0.2393 -0.0197 -0.0224 0.0549  137  ILE   A CA  
2936 C  CA  B ILE   A 137 ? 0.1534 0.1980 0.2499 -0.0138 -0.0252 0.0422  137  ILE   A CA  
2937 C  C   A ILE   A 137 ? 0.1486 0.1874 0.2310 -0.0229 -0.0192 0.0494  137  ILE   A C   
2938 C  C   B ILE   A 137 ? 0.1520 0.1901 0.2376 -0.0212 -0.0205 0.0402  137  ILE   A C   
2939 O  O   A ILE   A 137 ? 0.1502 0.1836 0.2332 -0.0206 -0.0134 0.0444  137  ILE   A O   
2940 O  O   B ILE   A 137 ? 0.1507 0.1888 0.2409 -0.0216 -0.0153 0.0326  137  ILE   A O   
2941 C  CB  A ILE   A 137 ? 0.1421 0.2212 0.2567 -0.0257 -0.0318 0.0555  137  ILE   A CB  
2942 C  CB  B ILE   A 137 ? 0.1623 0.2198 0.2717 -0.0147 -0.0436 0.0415  137  ILE   A CB  
2943 C  CG1 A ILE   A 137 ? 0.1534 0.2420 0.2737 -0.0194 -0.0297 0.0643  137  ILE   A CG1 
2944 C  CG1 B ILE   A 137 ? 0.1759 0.2406 0.2898 -0.0035 -0.0504 0.0485  137  ILE   A CG1 
2945 C  CG2 A ILE   A 137 ? 0.1405 0.2245 0.2676 -0.0328 -0.0355 0.0455  137  ILE   A CG2 
2946 C  CG2 B ILE   A 137 ? 0.1669 0.2204 0.2811 -0.0216 -0.0475 0.0326  137  ILE   A CG2 
2947 C  CD1 A ILE   A 137 ? 0.1680 0.2535 0.2864 -0.0131 -0.0258 0.0680  137  ILE   A CD1 
2948 C  CD1 B ILE   A 137 ? 0.1890 0.2514 0.3105 0.0051  -0.0476 0.0511  137  ILE   A CD1 
2971 N  N   . HIS   A 138 ? 0.1484 0.1975 0.2302 -0.0180 -0.0123 0.0370  138  HIS   A N   
2972 C  CA  . HIS   A 138 ? 0.1552 0.2007 0.1992 -0.0144 -0.0091 0.0320  138  HIS   A CA  
2973 C  C   . HIS   A 138 ? 0.1518 0.1922 0.1984 -0.0123 -0.0124 0.0361  138  HIS   A C   
2974 O  O   . HIS   A 138 ? 0.1585 0.1953 0.2032 -0.0140 -0.0052 0.0317  138  HIS   A O   
2975 C  CB  . HIS   A 138 ? 0.1725 0.2186 0.1999 -0.0207 -0.0210 0.0196  138  HIS   A CB  
2976 C  CG  . HIS   A 138 ? 0.1888 0.2311 0.2071 -0.0295 -0.0169 0.0157  138  HIS   A CG  
2977 N  ND1 . HIS   A 138 ? 0.1954 0.2443 0.2318 -0.0320 -0.0132 -0.0002 138  HIS   A ND1 
2978 C  CD2 . HIS   A 138 ? 0.1892 0.2413 0.2043 -0.0283 -0.0128 0.0165  138  HIS   A CD2 
2979 C  CE1 . HIS   A 138 ? 0.2004 0.2559 0.2319 -0.0205 -0.0138 -0.0004 138  HIS   A CE1 
2980 N  NE2 . HIS   A 138 ? 0.1914 0.2527 0.2158 -0.0221 -0.0071 0.0076  138  HIS   A NE2 
2989 N  N   . SER   A 139 ? 0.1415 0.1801 0.1980 -0.0149 -0.0078 0.0402  139  SER   A N   
2990 C  CA  . SER   A 139 ? 0.1345 0.1797 0.1963 -0.0100 -0.0054 0.0444  139  SER   A CA  
2991 C  C   . SER   A 139 ? 0.1322 0.1667 0.2003 -0.0126 0.0007  0.0359  139  SER   A C   
2992 O  O   . SER   A 139 ? 0.1337 0.1625 0.2076 -0.0144 0.0020  0.0343  139  SER   A O   
2993 C  CB  . SER   A 139 ? 0.1323 0.1774 0.1909 -0.0135 -0.0153 0.0461  139  SER   A CB  
2994 O  OG  . SER   A 139 ? 0.1394 0.1781 0.2043 -0.0224 -0.0114 0.0475  139  SER   A OG  
3000 N  N   . LEU   A 140 ? 0.1267 0.1734 0.1989 -0.0118 -0.0018 0.0514  140  LEU   A N   
3001 C  CA  . LEU   A 140 ? 0.1296 0.1702 0.2005 -0.0131 0.0033  0.0494  140  LEU   A CA  
3002 C  C   . LEU   A 140 ? 0.1263 0.1766 0.1946 -0.0179 -0.0018 0.0453  140  LEU   A C   
3003 O  O   . LEU   A 140 ? 0.1341 0.1778 0.2180 -0.0146 -0.0104 0.0482  140  LEU   A O   
3004 C  CB  . LEU   A 140 ? 0.1304 0.1758 0.2023 -0.0161 -0.0038 0.0508  140  LEU   A CB  
3005 C  CG  . LEU   A 140 ? 0.1340 0.1934 0.2212 -0.0223 0.0035  0.0595  140  LEU   A CG  
3006 C  CD1 . LEU   A 140 ? 0.1364 0.1978 0.2362 -0.0210 0.0051  0.0625  140  LEU   A CD1 
3007 C  CD2 . LEU   A 140 ? 0.1385 0.2116 0.2392 -0.0191 0.0079  0.0612  140  LEU   A CD2 
3019 N  N   . ARG   A 141 ? 0.1318 0.1787 0.2084 -0.0172 -0.0056 0.0400  141  ARG   A N   
3020 C  CA  . ARG   A 141 ? 0.1511 0.1927 0.2369 -0.0269 -0.0180 0.0204  141  ARG   A CA  
3021 C  C   . ARG   A 141 ? 0.1542 0.1686 0.2213 -0.0198 -0.0165 0.0198  141  ARG   A C   
3022 O  O   . ARG   A 141 ? 0.1481 0.1642 0.2368 -0.0235 -0.0041 0.0144  141  ARG   A O   
3023 C  CB  . ARG   A 141 ? 0.1636 0.2250 0.2725 -0.0399 -0.0291 -0.0065 141  ARG   A CB  
3024 C  CG  . ARG   A 141 ? 0.1994 0.2643 0.3156 -0.0452 -0.0151 -0.0110 141  ARG   A CG  
3025 C  CD  . ARG   A 141 ? 0.2273 0.2935 0.3461 -0.0547 -0.0102 -0.0098 141  ARG   A CD  
3026 N  NE  . ARG   A 141 ? 0.2164 0.3171 0.3638 -0.0561 -0.0151 -0.0040 141  ARG   A NE  
3027 C  CZ  . ARG   A 141 ? 0.2224 0.3383 0.3765 -0.0698 -0.0148 0.0016  141  ARG   A CZ  
3028 N  NH1 . ARG   A 141 ? 0.2129 0.3406 0.3650 -0.0795 0.0012  -0.0127 141  ARG   A NH1 
3029 N  NH2 . ARG   A 141 ? 0.2282 0.3519 0.3966 -0.0639 -0.0281 0.0120  141  ARG   A NH2 
3043 N  N   . VAL   A 142 ? 0.1412 0.1656 0.2071 -0.0158 -0.0053 0.0200  142  VAL   A N   
3044 C  CA  . VAL   A 142 ? 0.1410 0.1611 0.2113 -0.0135 0.0016  0.0123  142  VAL   A CA  
3045 C  C   . VAL   A 142 ? 0.1262 0.1605 0.2069 -0.0210 0.0069  0.0188  142  VAL   A C   
3046 O  O   . VAL   A 142 ? 0.1349 0.1620 0.2102 -0.0081 -0.0008 0.0221  142  VAL   A O   
3047 C  CB  . VAL   A 142 ? 0.1506 0.1688 0.2118 -0.0106 0.0041  0.0200  142  VAL   A CB  
3048 C  CG1 . VAL   A 142 ? 0.1486 0.1576 0.2121 -0.0163 0.0077  0.0080  142  VAL   A CG1 
3049 C  CG2 . VAL   A 142 ? 0.1607 0.1874 0.2203 -0.0031 0.0054  0.0202  142  VAL   A CG2 
3059 N  N   . CYS   A 143 ? 0.1311 0.1570 0.2072 -0.0157 -0.0040 0.0266  143  CYS   A N   
3060 C  CA  . CYS   A 143 ? 0.1280 0.1589 0.1996 -0.0184 -0.0016 0.0321  143  CYS   A CA  
3061 C  C   . CYS   A 143 ? 0.1322 0.1581 0.2061 -0.0201 -0.0045 0.0403  143  CYS   A C   
3062 O  O   . CYS   A 143 ? 0.1327 0.1573 0.2122 -0.0127 -0.0020 0.0427  143  CYS   A O   
3063 C  CB  . CYS   A 143 ? 0.1458 0.1614 0.2108 -0.0114 0.0118  0.0435  143  CYS   A CB  
3064 S  SG  . CYS   A 143 ? 0.1630 0.1680 0.1938 -0.0028 0.0047  0.0317  143  CYS   A SG  
3070 N  N   . VAL   A 144 ? 0.1335 0.1605 0.2390 -0.0161 -0.0024 0.0526  144  VAL   A N   
3071 C  CA  . VAL   A 144 ? 0.1397 0.1741 0.2792 -0.0245 0.0063  0.0508  144  VAL   A CA  
3072 C  C   . VAL   A 144 ? 0.1373 0.1649 0.2705 -0.0298 -0.0219 0.0471  144  VAL   A C   
3073 O  O   . VAL   A 144 ? 0.1604 0.1643 0.2703 -0.0167 -0.0221 0.0565  144  VAL   A O   
3074 C  CB  . VAL   A 144 ? 0.1619 0.1981 0.3373 -0.0169 0.0219  0.0565  144  VAL   A CB  
3075 C  CG1 . VAL   A 144 ? 0.1769 0.2116 0.3716 -0.0231 0.0110  0.0562  144  VAL   A CG1 
3076 C  CG2 . VAL   A 144 ? 0.1404 0.2053 0.3394 -0.0151 0.0351  0.0685  144  VAL   A CG2 
3086 N  N   . ASP   A 145 ? 0.1404 0.1578 0.2727 -0.0277 -0.0148 0.0294  145  ASP   A N   
3087 C  CA  . ASP   A 145 ? 0.1578 0.1613 0.2881 -0.0282 -0.0224 0.0233  145  ASP   A CA  
3088 C  C   . ASP   A 145 ? 0.1585 0.1503 0.2833 -0.0209 -0.0190 0.0123  145  ASP   A C   
3089 O  O   . ASP   A 145 ? 0.1697 0.1612 0.3338 -0.0229 -0.0271 -0.0220 145  ASP   A O   
3090 C  CB  . ASP   A 145 ? 0.1738 0.1916 0.3009 -0.0383 -0.0355 0.0176  145  ASP   A CB  
3091 C  CG  . ASP   A 145 ? 0.1917 0.2266 0.3242 -0.0539 -0.0460 0.0227  145  ASP   A CG  
3092 O  OD1 . ASP   A 145 ? 0.1922 0.2394 0.3363 -0.0668 -0.0363 0.0227  145  ASP   A OD1 
3093 O  OD2 . ASP   A 145 ? 0.2112 0.2516 0.3330 -0.0595 -0.0695 0.0239  145  ASP   A OD2 
3098 N  N   . THR   A 146 ? 0.1458 0.1401 0.2367 -0.0172 -0.0109 0.0144  146  THR   A N   
3099 C  CA  . THR   A 146 ? 0.1421 0.1379 0.2249 -0.0130 -0.0102 0.0157  146  THR   A CA  
3100 C  C   . THR   A 146 ? 0.1397 0.1358 0.2255 -0.0063 -0.0010 0.0160  146  THR   A C   
3101 O  O   . THR   A 146 ? 0.1518 0.1457 0.2413 0.0032  -0.0107 0.0080  146  THR   A O   
3102 C  CB  . THR   A 146 ? 0.1383 0.1374 0.2149 -0.0062 -0.0032 0.0133  146  THR   A CB  
3103 O  OG1 . THR   A 146 ? 0.1380 0.1588 0.2210 -0.0011 -0.0076 0.0115  146  THR   A OG1 
3104 C  CG2 . THR   A 146 ? 0.1370 0.1421 0.2282 -0.0057 0.0009  0.0100  146  THR   A CG2 
3112 N  N   . VAL   A 147 ? 0.1321 0.1404 0.2265 -0.0107 -0.0014 0.0267  147  VAL   A N   
3113 C  CA  . VAL   A 147 ? 0.1296 0.1430 0.2233 -0.0154 0.0094  0.0358  147  VAL   A CA  
3114 C  C   . VAL   A 147 ? 0.1335 0.1409 0.2356 -0.0170 0.0070  0.0351  147  VAL   A C   
3115 O  O   . VAL   A 147 ? 0.1408 0.1454 0.2530 -0.0167 -0.0030 0.0368  147  VAL   A O   
3116 C  CB  . VAL   A 147 ? 0.1422 0.1460 0.2104 -0.0148 0.0138  0.0355  147  VAL   A CB  
3117 C  CG1 . VAL   A 147 ? 0.1729 0.1597 0.2077 -0.0098 0.0084  0.0473  147  VAL   A CG1 
3118 C  CG2 . VAL   A 147 ? 0.1537 0.1441 0.2181 -0.0133 -0.0000 0.0352  147  VAL   A CG2 
3128 N  N   . ARG   A 148 ? 0.1370 0.1465 0.2319 -0.0166 0.0030  0.0507  148  ARG   A N   
3129 C  CA  . ARG   A 148 ? 0.1443 0.1453 0.2343 -0.0147 -0.0024 0.0519  148  ARG   A CA  
3130 C  C   . ARG   A 148 ? 0.1571 0.1503 0.2374 -0.0256 -0.0038 0.0658  148  ARG   A C   
3131 O  O   . ARG   A 148 ? 0.1882 0.1635 0.2622 -0.0252 0.0083  0.0640  148  ARG   A O   
3132 C  CB  . ARG   A 148 ? 0.1481 0.1463 0.2487 -0.0083 0.0104  0.0474  148  ARG   A CB  
3133 C  CG  . ARG   A 148 ? 0.1586 0.1499 0.2860 -0.0065 0.0210  0.0331  148  ARG   A CG  
3134 C  CD  . ARG   A 148 ? 0.1773 0.1498 0.3103 -0.0064 0.0348  0.0497  148  ARG   A CD  
3135 N  NE  . ARG   A 148 ? 0.1739 0.1537 0.3084 0.0038  0.0385  0.0607  148  ARG   A NE  
3136 C  CZ  . ARG   A 148 ? 0.1728 0.1404 0.2857 -0.0024 0.0364  0.0532  148  ARG   A CZ  
3137 N  NH1 . ARG   A 148 ? 0.1760 0.1413 0.2933 -0.0140 0.0353  0.0333  148  ARG   A NH1 
3138 N  NH2 . ARG   A 148 ? 0.1643 0.1633 0.2793 0.0098  0.0478  0.0514  148  ARG   A NH2 
3152 N  N   . THR   A 149 ? 0.1632 0.1584 0.2257 -0.0288 -0.0227 0.0503  149  THR   A N   
3153 C  CA  . THR   A 149 ? 0.1591 0.1700 0.2196 -0.0307 -0.0120 0.0498  149  THR   A CA  
3154 C  C   . THR   A 149 ? 0.1530 0.1652 0.2135 -0.0374 -0.0041 0.0563  149  THR   A C   
3155 O  O   . THR   A 149 ? 0.1580 0.1682 0.2299 -0.0342 -0.0090 0.0426  149  THR   A O   
3156 C  CB  . THR   A 149 ? 0.1587 0.1828 0.2183 -0.0239 -0.0065 0.0462  149  THR   A CB  
3157 O  OG1 . THR   A 149 ? 0.1656 0.1715 0.2320 -0.0310 -0.0064 0.0370  149  THR   A OG1 
3158 C  CG2 . THR   A 149 ? 0.1599 0.1941 0.2363 -0.0220 -0.0083 0.0457  149  THR   A CG2 
3166 N  N   . ASN   A 150 ? 0.1581 0.1688 0.2243 -0.0276 -0.0108 0.0629  150  ASN   A N   
3167 C  CA  . ASN   A 150 ? 0.1748 0.1863 0.2209 -0.0312 -0.0061 0.0664  150  ASN   A CA  
3168 C  C   . ASN   A 150 ? 0.1568 0.1797 0.2181 -0.0350 -0.0087 0.0539  150  ASN   A C   
3169 O  O   . ASN   A 150 ? 0.1630 0.1898 0.2401 -0.0273 -0.0127 0.0421  150  ASN   A O   
3170 C  CB  . ASN   A 150 ? 0.2229 0.2119 0.2539 -0.0348 0.0074  0.0834  150  ASN   A CB  
3171 C  CG  . ASN   A 150 ? 0.2730 0.2475 0.3220 -0.0323 -0.0047 0.0794  150  ASN   A CG  
3172 O  OD1 . ASN   A 150 ? 0.2937 0.2547 0.3398 -0.0396 -0.0025 0.0918  150  ASN   A OD1 
3173 N  ND2 . ASN   A 150 ? 0.3056 0.2749 0.3615 -0.0225 -0.0157 0.0705  150  ASN   A ND2 
3180 N  N   . VAL   A 151 ? 0.1565 0.1675 0.2195 -0.0331 -0.0105 0.0572  151  VAL   A N   
3181 C  CA  . VAL   A 151 ? 0.1655 0.1645 0.2028 -0.0358 0.0012  0.0503  151  VAL   A CA  
3182 C  C   . VAL   A 151 ? 0.1570 0.1614 0.2115 -0.0416 0.0031  0.0549  151  VAL   A C   
3183 O  O   . VAL   A 151 ? 0.1605 0.1736 0.2398 -0.0362 -0.0025 0.0534  151  VAL   A O   
3184 C  CB  . VAL   A 151 ? 0.1924 0.1809 0.2011 -0.0216 -0.0048 0.0462  151  VAL   A CB  
3185 C  CG1 . VAL   A 151 ? 0.1836 0.2022 0.2273 -0.0214 -0.0069 0.0317  151  VAL   A CG1 
3186 C  CG2 . VAL   A 151 ? 0.2019 0.1807 0.2002 -0.0163 0.0106  0.0414  151  VAL   A CG2 
3196 N  N   . TYR   A 152 ? 0.1493 0.1677 0.2017 -0.0333 -0.0043 0.0506  152  TYR   A N   
3197 C  CA  . TYR   A 152 ? 0.1499 0.1791 0.1789 -0.0340 0.0036  0.0496  152  TYR   A CA  
3198 C  C   . TYR   A 152 ? 0.1448 0.1735 0.1858 -0.0341 0.0174  0.0475  152  TYR   A C   
3199 O  O   . TYR   A 152 ? 0.1539 0.1649 0.2024 -0.0321 0.0164  0.0454  152  TYR   A O   
3200 C  CB  . TYR   A 152 ? 0.1667 0.1853 0.1767 -0.0262 0.0103  0.0444  152  TYR   A CB  
3201 C  CG  . TYR   A 152 ? 0.1860 0.2067 0.1816 -0.0331 0.0239  0.0404  152  TYR   A CG  
3202 C  CD1 . TYR   A 152 ? 0.1938 0.2242 0.1996 -0.0256 0.0265  0.0560  152  TYR   A CD1 
3203 C  CD2 . TYR   A 152 ? 0.1863 0.2134 0.1727 -0.0480 0.0261  0.0333  152  TYR   A CD2 
3204 C  CE1 . TYR   A 152 ? 0.2166 0.2350 0.2123 -0.0156 0.0097  0.0682  152  TYR   A CE1 
3205 C  CE2 . TYR   A 152 ? 0.2086 0.2280 0.1855 -0.0449 0.0274  0.0432  152  TYR   A CE2 
3206 C  CZ  . TYR   A 152 ? 0.2304 0.2306 0.2046 -0.0285 0.0200  0.0677  152  TYR   A CZ  
3207 O  OH  . TYR   A 152 ? 0.2618 0.2437 0.2493 -0.0149 0.0163  0.0801  152  TYR   A OH  
3217 N  N   . LEU   A 153 ? 0.1467 0.1710 0.1900 -0.0335 0.0164  0.0484  153  LEU   A N   
3218 C  CA  . LEU   A 153 ? 0.1425 0.1666 0.2139 -0.0186 0.0189  0.0444  153  LEU   A CA  
3219 C  C   . LEU   A 153 ? 0.1453 0.1726 0.2141 -0.0169 0.0313  0.0442  153  LEU   A C   
3220 O  O   . LEU   A 153 ? 0.1481 0.1793 0.2451 -0.0204 0.0369  0.0385  153  LEU   A O   
3221 C  CB  . LEU   A 153 ? 0.1370 0.1709 0.2323 -0.0170 0.0100  0.0423  153  LEU   A CB  
3222 C  CG  . LEU   A 153 ? 0.1440 0.1707 0.2129 -0.0185 0.0152  0.0403  153  LEU   A CG  
3223 C  CD1 . LEU   A 153 ? 0.1534 0.1761 0.2187 -0.0220 0.0017  0.0417  153  LEU   A CD1 
3224 C  CD2 . LEU   A 153 ? 0.1586 0.1666 0.2106 -0.0214 0.0225  0.0181  153  LEU   A CD2 
3236 N  N   A ALA   A 154 ? 0.1455 0.1644 0.2189 -0.0133 0.0313  0.0474  154  ALA   A N   
3237 N  N   B ALA   A 154 ? 0.1447 0.1764 0.2064 -0.0131 0.0272  0.0477  154  ALA   A N   
3238 C  CA  A ALA   A 154 ? 0.1477 0.1656 0.2351 -0.0092 0.0352  0.0436  154  ALA   A CA  
3239 C  CA  B ALA   A 154 ? 0.1456 0.1882 0.2118 -0.0108 0.0255  0.0472  154  ALA   A CA  
3240 C  C   A ALA   A 154 ? 0.1512 0.1613 0.2420 -0.0011 0.0362  0.0459  154  ALA   A C   
3241 C  C   B ALA   A 154 ? 0.1485 0.1948 0.2085 -0.0101 0.0239  0.0524  154  ALA   A C   
3242 O  O   A ALA   A 154 ? 0.1536 0.1583 0.2417 -0.0032 0.0376  0.0431  154  ALA   A O   
3243 O  O   B ALA   A 154 ? 0.1494 0.1947 0.1924 -0.0152 0.0203  0.0530  154  ALA   A O   
3244 C  CB  A ALA   A 154 ? 0.1552 0.1650 0.2416 -0.0027 0.0336  0.0350  154  ALA   A CB  
3245 C  CB  B ALA   A 154 ? 0.1530 0.1887 0.2166 -0.0032 0.0196  0.0387  154  ALA   A CB  
3256 N  N   A VAL   A 155 ? 0.1564 0.1641 0.2503 0.0120  0.0316  0.0507  155  VAL   A N   
3257 N  N   B VAL   A 155 ? 0.1556 0.2043 0.2238 -0.0065 0.0258  0.0593  155  VAL   A N   
3258 C  CA  A VAL   A 155 ? 0.1557 0.1703 0.2580 0.0127  0.0346  0.0679  155  VAL   A CA  
3259 C  CA  B VAL   A 155 ? 0.1691 0.2196 0.2442 -0.0041 0.0244  0.0689  155  VAL   A CA  
3260 C  C   A VAL   A 155 ? 0.1562 0.1764 0.2737 0.0270  0.0234  0.0768  155  VAL   A C   
3261 C  C   B VAL   A 155 ? 0.1842 0.2360 0.2745 0.0054  0.0242  0.0683  155  VAL   A C   
3262 O  O   A VAL   A 155 ? 0.1495 0.1807 0.2797 0.0347  0.0159  0.0620  155  VAL   A O   
3263 O  O   B VAL   A 155 ? 0.1811 0.2339 0.2838 0.0063  0.0316  0.0628  155  VAL   A O   
3264 C  CB  A VAL   A 155 ? 0.1536 0.1726 0.2585 0.0122  0.0251  0.0595  155  VAL   A CB  
3265 C  CB  B VAL   A 155 ? 0.1649 0.2239 0.2469 -0.0002 0.0046  0.0625  155  VAL   A CB  
3266 C  CG1 A VAL   A 155 ? 0.1649 0.1846 0.2705 0.0131  0.0087  0.0634  155  VAL   A CG1 
3267 C  CG1 B VAL   A 155 ? 0.1658 0.2336 0.2506 0.0068  -0.0096 0.0586  155  VAL   A CG1 
3268 C  CG2 A VAL   A 155 ? 0.1563 0.1770 0.2458 0.0161  0.0238  0.0622  155  VAL   A CG2 
3269 C  CG2 B VAL   A 155 ? 0.1630 0.2254 0.2423 0.0005  -0.0011 0.0608  155  VAL   A CG2 
3288 N  N   A PHE   A 156 ? 0.1655 0.1806 0.2919 0.0300  0.0245  0.0888  156  PHE   A N   
3289 N  N   B PHE   A 156 ? 0.2021 0.2559 0.2950 0.0120  0.0228  0.0644  156  PHE   A N   
3290 C  CA  A PHE   A 156 ? 0.1856 0.1891 0.3214 0.0394  0.0133  0.0859  156  PHE   A CA  
3291 C  CA  B PHE   A 156 ? 0.2304 0.2803 0.3277 0.0196  0.0218  0.0514  156  PHE   A CA  
3292 C  C   A PHE   A 156 ? 0.1832 0.1979 0.3296 0.0518  0.0166  0.0963  156  PHE   A C   
3293 C  C   B PHE   A 156 ? 0.2491 0.2993 0.3394 0.0224  0.0208  0.0684  156  PHE   A C   
3294 O  O   A PHE   A 156 ? 0.1909 0.2127 0.3498 0.0424  0.0207  0.0758  156  PHE   A O   
3295 O  O   B PHE   A 156 ? 0.2558 0.3009 0.3439 0.0191  0.0194  0.0749  156  PHE   A O   
3296 C  CB  A PHE   A 156 ? 0.2149 0.1896 0.3299 0.0337  0.0009  0.0801  156  PHE   A CB  
3297 C  CB  B PHE   A 156 ? 0.2455 0.2867 0.3398 0.0198  0.0219  0.0266  156  PHE   A CB  
3298 C  CG  A PHE   A 156 ? 0.2470 0.1979 0.3504 0.0360  -0.0110 0.0673  156  PHE   A CG  
3299 C  CG  B PHE   A 156 ? 0.2594 0.2948 0.3598 0.0206  0.0142  0.0023  156  PHE   A CG  
3300 C  CD1 A PHE   A 156 ? 0.2629 0.2035 0.3595 0.0366  -0.0143 0.0602  156  PHE   A CD1 
3301 C  CD1 B PHE   A 156 ? 0.2643 0.2960 0.3699 0.0246  0.0116  -0.0095 156  PHE   A CD1 
3302 C  CD2 A PHE   A 156 ? 0.2614 0.2056 0.3590 0.0406  -0.0153 0.0655  156  PHE   A CD2 
3303 C  CD2 B PHE   A 156 ? 0.2620 0.2982 0.3663 0.0156  0.0118  -0.0125 156  PHE   A CD2 
3304 C  CE1 A PHE   A 156 ? 0.2722 0.2119 0.3708 0.0369  -0.0121 0.0449  156  PHE   A CE1 
3305 C  CE1 B PHE   A 156 ? 0.2676 0.2975 0.3715 0.0235  0.0100  -0.0186 156  PHE   A CE1 
3306 C  CE2 A PHE   A 156 ? 0.2752 0.2153 0.3667 0.0411  -0.0161 0.0506  156  PHE   A CE2 
3307 C  CE2 B PHE   A 156 ? 0.2680 0.2992 0.3756 0.0160  0.0109  -0.0204 156  PHE   A CE2 
3308 C  CZ  A PHE   A 156 ? 0.2767 0.2168 0.3726 0.0450  -0.0140 0.0381  156  PHE   A CZ  
3309 C  CZ  B PHE   A 156 ? 0.2689 0.2990 0.3738 0.0235  0.0135  -0.0256 156  PHE   A CZ  
3328 N  N   A ASP   A 157 ? 0.1897 0.2111 0.3227 0.0552  0.0214  0.1158  157  ASP   A N   
3329 N  N   B ASP   A 157 ? 0.2539 0.3141 0.3539 0.0251  0.0146  0.0775  157  ASP   A N   
3330 C  CA  A ASP   A 157 ? 0.2056 0.2343 0.3291 0.0596  0.0121  0.1148  157  ASP   A CA  
3331 C  CA  B ASP   A 157 ? 0.2607 0.3301 0.3780 0.0194  0.0132  0.0879  157  ASP   A CA  
3332 C  C   A ASP   A 157 ? 0.1852 0.2546 0.3283 0.0625  0.0248  0.1188  157  ASP   A C   
3333 C  C   B ASP   A 157 ? 0.2516 0.3334 0.3757 0.0212  0.0102  0.0841  157  ASP   A C   
3334 O  O   A ASP   A 157 ? 0.1730 0.2467 0.3241 0.0567  0.0437  0.1334  157  ASP   A O   
3335 O  O   B ASP   A 157 ? 0.2461 0.3313 0.3777 0.0223  0.0019  0.0879  157  ASP   A O   
3336 C  CB  A ASP   A 157 ? 0.2414 0.2386 0.3453 0.0616  -0.0131 0.1132  157  ASP   A CB  
3337 C  CB  B ASP   A 157 ? 0.2708 0.3372 0.4049 0.0122  0.0168  0.1084  157  ASP   A CB  
3338 C  CG  A ASP   A 157 ? 0.2737 0.2407 0.3651 0.0599  -0.0279 0.1097  157  ASP   A CG  
3339 C  CG  B ASP   A 157 ? 0.2798 0.3432 0.4320 0.0050  0.0160  0.1280  157  ASP   A CG  
3340 O  OD1 A ASP   A 157 ? 0.2979 0.2475 0.3885 0.0509  -0.0387 0.0959  157  ASP   A OD1 
3341 O  OD1 B ASP   A 157 ? 0.2788 0.3402 0.4345 0.0050  0.0103  0.1404  157  ASP   A OD1 
3342 O  OD2 A ASP   A 157 ? 0.2776 0.2405 0.3766 0.0545  -0.0271 0.1118  157  ASP   A OD2 
3343 O  OD2 B ASP   A 157 ? 0.2855 0.3478 0.4518 0.0001  0.0139  0.1331  157  ASP   A OD2 
3352 N  N   A LYS   A 158 ? 0.1847 0.2836 0.3354 0.0640  0.0194  0.0935  158  LYS   A N   
3353 N  N   B LYS   A 158 ? 0.2486 0.3383 0.3690 0.0207  0.0121  0.0722  158  LYS   A N   
3354 C  CA  A LYS   A 158 ? 0.1770 0.3083 0.3347 0.0715  0.0259  0.0716  158  LYS   A CA  
3355 C  CA  B LYS   A 158 ? 0.2526 0.3467 0.3752 0.0187  0.0206  0.0536  158  LYS   A CA  
3356 C  C   A LYS   A 158 ? 0.1651 0.3158 0.3385 0.0704  0.0213  0.0725  158  LYS   A C   
3357 C  C   B LYS   A 158 ? 0.2354 0.3380 0.3700 0.0221  0.0191  0.0599  158  LYS   A C   
3358 O  O   A LYS   A 158 ? 0.1553 0.3301 0.3490 0.0612  0.0342  0.0726  158  LYS   A O   
3359 O  O   B LYS   A 158 ? 0.2292 0.3447 0.3678 0.0183  0.0236  0.0659  158  LYS   A O   
3360 C  CB  A LYS   A 158 ? 0.1876 0.3222 0.3310 0.0709  0.0402  0.0622  158  LYS   A CB  
3361 C  CB  B LYS   A 158 ? 0.2709 0.3636 0.3953 0.0133  0.0268  0.0283  158  LYS   A CB  
3362 C  CG  A LYS   A 158 ? 0.2009 0.3381 0.3378 0.0638  0.0475  0.0579  158  LYS   A CG  
3363 C  CG  B LYS   A 158 ? 0.2909 0.3795 0.4236 0.0073  0.0291  0.0065  158  LYS   A CG  
3364 C  CD  A LYS   A 158 ? 0.2079 0.3507 0.3426 0.0556  0.0657  0.0582  158  LYS   A CD  
3365 C  CD  B LYS   A 158 ? 0.3054 0.3924 0.4528 0.0010  0.0295  -0.0107 158  LYS   A CD  
3366 C  CE  A LYS   A 158 ? 0.2107 0.3602 0.3529 0.0466  0.0814  0.0627  158  LYS   A CE  
3367 C  CE  B LYS   A 158 ? 0.3164 0.4012 0.4778 -0.0036 0.0275  -0.0237 158  LYS   A CE  
3368 N  NZ  A LYS   A 158 ? 0.2119 0.3656 0.3581 0.0379  0.0897  0.0663  158  LYS   A NZ  
3369 N  NZ  B LYS   A 158 ? 0.3224 0.4060 0.4944 -0.0057 0.0243  -0.0316 158  LYS   A NZ  
3396 N  N   A ASN   A 159 ? 0.1691 0.3109 0.3426 0.0686  -0.0046 0.0754  159  ASN   A N   
3397 N  N   B ASN   A 159 ? 0.2271 0.3253 0.3817 0.0295  0.0114  0.0613  159  ASN   A N   
3398 C  CA  A ASN   A 159 ? 0.1805 0.3020 0.3483 0.0653  -0.0140 0.0827  159  ASN   A CA  
3399 C  CA  B ASN   A 159 ? 0.2172 0.3098 0.3871 0.0360  0.0109  0.0692  159  ASN   A CA  
3400 C  C   A ASN   A 159 ? 0.1791 0.2942 0.3399 0.0584  0.0041  0.0843  159  ASN   A C   
3401 C  C   B ASN   A 159 ? 0.1844 0.2841 0.3592 0.0384  0.0013  0.0853  159  ASN   A C   
3402 O  O   A ASN   A 159 ? 0.1733 0.2866 0.3374 0.0634  0.0036  0.0651  159  ASN   A O   
3403 O  O   B ASN   A 159 ? 0.1681 0.2778 0.3544 0.0386  -0.0166 0.0936  159  ASN   A O   
3404 C  CB  A ASN   A 159 ? 0.1879 0.3021 0.3653 0.0638  -0.0247 0.0867  159  ASN   A CB  
3405 C  CB  B ASN   A 159 ? 0.2412 0.3223 0.4238 0.0365  0.0289  0.0649  159  ASN   A CB  
3406 C  CG  A ASN   A 159 ? 0.2040 0.3095 0.3961 0.0583  -0.0128 0.0809  159  ASN   A CG  
3407 C  CG  B ASN   A 159 ? 0.2664 0.3382 0.4583 0.0322  0.0479  0.0618  159  ASN   A CG  
3408 O  OD1 A ASN   A 159 ? 0.2134 0.3187 0.4083 0.0510  -0.0066 0.0817  159  ASN   A OD1 
3409 O  OD1 B ASN   A 159 ? 0.2765 0.3456 0.4714 0.0301  0.0502  0.0607  159  ASN   A OD1 
3410 N  ND2 A ASN   A 159 ? 0.2058 0.3111 0.4111 0.0596  -0.0098 0.0749  159  ASN   A ND2 
3411 N  ND2 B ASN   A 159 ? 0.2723 0.3424 0.4733 0.0287  0.0559  0.0560  159  ASN   A ND2 
3424 N  N   A LEU   A 160 ? 0.1800 0.2867 0.3287 0.0511  0.0052  0.1071  160  LEU   A N   
3425 N  N   B LEU   A 160 ? 0.1748 0.2760 0.3470 0.0340  0.0006  0.0978  160  LEU   A N   
3426 C  CA  A LEU   A 160 ? 0.1823 0.2855 0.3093 0.0374  0.0214  0.1197  160  LEU   A CA  
3427 C  CA  B LEU   A 160 ? 0.1670 0.2737 0.3228 0.0315  0.0133  0.1101  160  LEU   A CA  
3428 C  C   A LEU   A 160 ? 0.1615 0.2838 0.2940 0.0300  0.0349  0.1282  160  LEU   A C   
3429 C  C   B LEU   A 160 ? 0.1552 0.2752 0.3051 0.0257  0.0251  0.1131  160  LEU   A C   
3430 O  O   A LEU   A 160 ? 0.1629 0.2914 0.3058 0.0208  0.0354  0.1265  160  LEU   A O   
3431 O  O   B LEU   A 160 ? 0.1519 0.2705 0.3180 0.0206  0.0251  0.1080  160  LEU   A O   
3432 C  CB  A LEU   A 160 ? 0.1981 0.2893 0.3021 0.0304  0.0242  0.1193  160  LEU   A CB  
3433 C  CB  B LEU   A 160 ? 0.1768 0.2773 0.3099 0.0264  0.0228  0.1143  160  LEU   A CB  
3434 C  CG  A LEU   A 160 ? 0.2101 0.2929 0.3047 0.0248  0.0279  0.1058  160  LEU   A CG  
3435 C  CG  B LEU   A 160 ? 0.1782 0.2829 0.3051 0.0214  0.0370  0.1058  160  LEU   A CG  
3436 C  CD1 A LEU   A 160 ? 0.2154 0.2973 0.3148 0.0237  0.0274  0.0932  160  LEU   A CD1 
3437 C  CD1 B LEU   A 160 ? 0.1803 0.2852 0.3051 0.0208  0.0355  0.1016  160  LEU   A CD1 
3438 C  CD2 A LEU   A 160 ? 0.2140 0.2930 0.3033 0.0226  0.0330  0.0998  160  LEU   A CD2 
3439 C  CD2 B LEU   A 160 ? 0.1819 0.2842 0.3021 0.0182  0.0519  0.1008  160  LEU   A CD2 
3462 N  N   A TYR   A 161 ? 0.1490 0.2746 0.2829 0.0283  0.0328  0.1339  161  TYR   A N   
3463 N  N   B TYR   A 161 ? 0.1538 0.2885 0.2959 0.0230  0.0304  0.1132  161  TYR   A N   
3464 C  CA  A TYR   A 161 ? 0.1466 0.2785 0.2817 0.0154  0.0341  0.1246  161  TYR   A CA  
3465 C  CA  B TYR   A 161 ? 0.1647 0.2980 0.2909 0.0167  0.0289  0.1154  161  TYR   A CA  
3466 C  C   A TYR   A 161 ? 0.1350 0.2947 0.2951 0.0039  0.0372  0.1133  161  TYR   A C   
3467 C  C   B TYR   A 161 ? 0.1682 0.3119 0.3038 0.0169  0.0256  0.1099  161  TYR   A C   
3468 O  O   A TYR   A 161 ? 0.1216 0.2985 0.2928 -0.0080 0.0265  0.1103  161  TYR   A O   
3469 O  O   B TYR   A 161 ? 0.1573 0.3107 0.3016 0.0142  0.0169  0.1123  161  TYR   A O   
3470 C  CB  A TYR   A 161 ? 0.1590 0.2758 0.2917 0.0069  0.0243  0.1055  161  TYR   A CB  
3471 C  CB  B TYR   A 161 ? 0.1695 0.2981 0.2921 0.0093  0.0270  0.1019  161  TYR   A CB  
3472 C  CG  A TYR   A 161 ? 0.1643 0.2759 0.2814 0.0017  0.0161  0.0887  161  TYR   A CG  
3473 C  CG  B TYR   A 161 ? 0.1717 0.3023 0.2773 0.0039  0.0270  0.0886  161  TYR   A CG  
3474 C  CD1 A TYR   A 161 ? 0.1660 0.2733 0.2735 -0.0052 0.0119  0.0877  161  TYR   A CD1 
3475 C  CD1 B TYR   A 161 ? 0.1747 0.3094 0.2812 0.0007  0.0186  0.0798  161  TYR   A CD1 
3476 C  CD2 A TYR   A 161 ? 0.1651 0.2802 0.2759 -0.0012 0.0060  0.0780  161  TYR   A CD2 
3477 C  CD2 B TYR   A 161 ? 0.1693 0.3011 0.2624 -0.0012 0.0297  0.0854  161  TYR   A CD2 
3478 C  CE1 A TYR   A 161 ? 0.1664 0.2690 0.2517 -0.0088 -0.0054 0.0916  161  TYR   A CE1 
3479 C  CE1 B TYR   A 161 ? 0.1803 0.3092 0.2828 -0.0025 0.0175  0.0825  161  TYR   A CE1 
3480 C  CE2 A TYR   A 161 ? 0.1659 0.2770 0.2640 -0.0103 -0.0016 0.0835  161  TYR   A CE2 
3481 C  CE2 B TYR   A 161 ? 0.1748 0.3025 0.2645 -0.0034 0.0240  0.0858  161  TYR   A CE2 
3482 C  CZ  A TYR   A 161 ? 0.1743 0.2715 0.2495 -0.0154 -0.0119 0.0921  161  TYR   A CZ  
3483 C  CZ  B TYR   A 161 ? 0.1887 0.3060 0.2824 -0.0038 0.0207  0.0865  161  TYR   A CZ  
3484 O  OH  A TYR   A 161 ? 0.1879 0.2686 0.2475 -0.0225 -0.0206 0.0920  161  TYR   A OH  
3485 O  OH  B TYR   A 161 ? 0.2088 0.3053 0.3059 -0.0041 0.0134  0.0831  161  TYR   A OH  
3504 N  N   A ASP   A 162 ? 0.1336 0.3061 0.3120 0.0035  0.0472  0.1081  162  ASP   A N   
3505 N  N   B ASP   A 162 ? 0.1794 0.3271 0.3258 0.0233  0.0272  0.1053  162  ASP   A N   
3506 C  CA  A ASP   A 162 ? 0.1271 0.3155 0.3129 -0.0001 0.0493  0.1070  162  ASP   A CA  
3507 C  CA  B ASP   A 162 ? 0.1861 0.3413 0.3358 0.0251  0.0283  0.1080  162  ASP   A CA  
3508 C  C   A ASP   A 162 ? 0.1198 0.3195 0.3187 -0.0093 0.0382  0.1084  162  ASP   A C   
3509 C  C   B ASP   A 162 ? 0.1843 0.3513 0.3220 0.0235  0.0191  0.1100  162  ASP   A C   
3510 O  O   A ASP   A 162 ? 0.1231 0.3220 0.3306 -0.0169 0.0414  0.1022  162  ASP   A O   
3511 O  O   B ASP   A 162 ? 0.1834 0.3560 0.3211 0.0240  0.0157  0.1116  162  ASP   A O   
3512 C  CB  A ASP   A 162 ? 0.1391 0.3196 0.3070 0.0038  0.0541  0.1048  162  ASP   A CB  
3513 C  CB  B ASP   A 162 ? 0.1913 0.3462 0.3608 0.0284  0.0342  0.1088  162  ASP   A CB  
3514 C  CG  A ASP   A 162 ? 0.1531 0.3262 0.3176 0.0123  0.0536  0.0976  162  ASP   A CG  
3515 C  CG  B ASP   A 162 ? 0.1981 0.3493 0.3815 0.0309  0.0354  0.1130  162  ASP   A CG  
3516 O  OD1 A ASP   A 162 ? 0.1670 0.3317 0.3200 0.0149  0.0527  0.0900  162  ASP   A OD1 
3517 O  OD1 B ASP   A 162 ? 0.1988 0.3475 0.3875 0.0297  0.0358  0.1204  162  ASP   A OD1 
3518 O  OD2 A ASP   A 162 ? 0.1623 0.3292 0.3288 0.0154  0.0581  0.0942  162  ASP   A OD2 
3519 O  OD2 B ASP   A 162 ? 0.2081 0.3534 0.3963 0.0370  0.0360  0.1113  162  ASP   A OD2 
3528 N  N   A LYS   A 163 ? 0.1320 0.3245 0.3210 -0.0136 0.0091  0.1155  163  LYS   A N   
3529 N  N   B LYS   A 163 ? 0.1953 0.3571 0.3192 0.0148  0.0118  0.1068  163  LYS   A N   
3530 C  CA  A LYS   A 163 ? 0.1438 0.3278 0.3136 -0.0223 -0.0013 0.1086  163  LYS   A CA  
3531 C  CA  B LYS   A 163 ? 0.2045 0.3602 0.3087 0.0023  0.0147  0.0982  163  LYS   A CA  
3532 C  C   A LYS   A 163 ? 0.1383 0.3168 0.3092 -0.0238 0.0130  0.0923  163  LYS   A C   
3533 C  C   B LYS   A 163 ? 0.1846 0.3481 0.2875 -0.0046 0.0184  0.0940  163  LYS   A C   
3534 O  O   A LYS   A 163 ? 0.1379 0.3324 0.3281 -0.0236 0.0152  0.0889  163  LYS   A O   
3535 O  O   B LYS   A 163 ? 0.1766 0.3509 0.2971 -0.0179 0.0187  0.0839  163  LYS   A O   
3536 C  CB  A LYS   A 163 ? 0.1748 0.3434 0.3353 -0.0259 -0.0119 0.1058  163  LYS   A CB  
3537 C  CB  B LYS   A 163 ? 0.2423 0.3755 0.3366 -0.0009 0.0175  0.0921  163  LYS   A CB  
3538 C  CG  A LYS   A 163 ? 0.2091 0.3587 0.3754 -0.0321 -0.0089 0.0984  163  LYS   A CG  
3539 C  CG  B LYS   A 163 ? 0.2806 0.3882 0.3740 -0.0081 0.0276  0.0882  163  LYS   A CG  
3540 C  CD  A LYS   A 163 ? 0.2432 0.3730 0.4163 -0.0361 -0.0105 0.0908  163  LYS   A CD  
3541 C  CD  B LYS   A 163 ? 0.3134 0.3993 0.4155 -0.0134 0.0328  0.0849  163  LYS   A CD  
3542 C  CE  A LYS   A 163 ? 0.2610 0.3822 0.4492 -0.0391 -0.0132 0.0847  163  LYS   A CE  
3543 C  CE  B LYS   A 163 ? 0.3378 0.4079 0.4506 -0.0178 0.0357  0.0833  163  LYS   A CE  
3544 N  NZ  A LYS   A 163 ? 0.2691 0.3875 0.4667 -0.0403 -0.0131 0.0834  163  LYS   A NZ  
3545 N  NZ  B LYS   A 163 ? 0.3490 0.4135 0.4757 -0.0200 0.0339  0.0813  163  LYS   A NZ  
3572 N  N   A LEU   A 164 ? 0.1287 0.2886 0.2884 -0.0299 0.0158  0.0835  164  LEU   A N   
3573 N  N   B LEU   A 164 ? 0.1624 0.3279 0.2625 -0.0051 0.0156  0.0906  164  LEU   A N   
3574 C  CA  A LEU   A 164 ? 0.1391 0.2620 0.2727 -0.0297 0.0291  0.0744  164  LEU   A CA  
3575 C  CA  B LEU   A 164 ? 0.1558 0.3107 0.2443 -0.0081 0.0280  0.0829  164  LEU   A CA  
3576 C  C   A LEU   A 164 ? 0.1469 0.2485 0.2753 -0.0262 0.0384  0.0631  164  LEU   A C   
3577 C  C   B LEU   A 164 ? 0.1529 0.2990 0.2495 -0.0111 0.0320  0.0749  164  LEU   A C   
3578 O  O   A LEU   A 164 ? 0.1579 0.2577 0.2812 -0.0199 0.0570  0.0451  164  LEU   A O   
3579 O  O   B LEU   A 164 ? 0.1551 0.3006 0.2483 -0.0137 0.0564  0.0600  164  LEU   A O   
3580 C  CB  A LEU   A 164 ? 0.1450 0.2552 0.2668 -0.0369 0.0278  0.0772  164  LEU   A CB  
3581 C  CB  B LEU   A 164 ? 0.1513 0.3063 0.2358 -0.0055 0.0284  0.0839  164  LEU   A CB  
3582 C  CG  A LEU   A 164 ? 0.1510 0.2516 0.2672 -0.0284 0.0296  0.0680  164  LEU   A CG  
3583 C  CG  B LEU   A 164 ? 0.1493 0.3022 0.2344 -0.0017 0.0348  0.0861  164  LEU   A CG  
3584 C  CD1 A LEU   A 164 ? 0.1415 0.2496 0.2599 -0.0170 0.0292  0.0632  164  LEU   A CD1 
3585 C  CD1 B LEU   A 164 ? 0.1358 0.2989 0.2359 0.0046  0.0301  0.0849  164  LEU   A CD1 
3586 C  CD2 A LEU   A 164 ? 0.1603 0.2500 0.2740 -0.0282 0.0253  0.0538  164  LEU   A CD2 
3587 C  CD2 B LEU   A 164 ? 0.1554 0.3009 0.2322 -0.0007 0.0401  0.0867  164  LEU   A CD2 
3610 N  N   A VAL   A 165 ? 0.1549 0.2339 0.2766 -0.0170 0.0401  0.0606  165  VAL   A N   
3611 N  N   B VAL   A 165 ? 0.1504 0.2851 0.2479 -0.0112 0.0268  0.0786  165  VAL   A N   
3612 C  CA  A VAL   A 165 ? 0.1662 0.2230 0.2620 -0.0156 0.0476  0.0543  165  VAL   A CA  
3613 C  CA  B VAL   A 165 ? 0.1568 0.2772 0.2467 -0.0082 0.0362  0.0794  165  VAL   A CA  
3614 C  C   A VAL   A 165 ? 0.1601 0.2300 0.2663 -0.0170 0.0344  0.0552  165  VAL   A C   
3615 C  C   B VAL   A 165 ? 0.1456 0.2826 0.2484 -0.0097 0.0401  0.0776  165  VAL   A C   
3616 O  O   A VAL   A 165 ? 0.1526 0.2204 0.2557 -0.0095 0.0350  0.0561  165  VAL   A O   
3617 O  O   B VAL   A 165 ? 0.1418 0.2792 0.2442 -0.0026 0.0415  0.0703  165  VAL   A O   
3618 C  CB  A VAL   A 165 ? 0.1872 0.2133 0.2642 -0.0090 0.0519  0.0415  165  VAL   A CB  
3619 C  CB  B VAL   A 165 ? 0.1772 0.2690 0.2549 -0.0013 0.0396  0.0716  165  VAL   A CB  
3620 C  CG1 A VAL   A 165 ? 0.1948 0.2115 0.2699 -0.0123 0.0622  0.0446  165  VAL   A CG1 
3621 C  CG1 B VAL   A 165 ? 0.1834 0.2682 0.2556 -0.0000 0.0494  0.0657  165  VAL   A CG1 
3622 C  CG2 A VAL   A 165 ? 0.2003 0.2091 0.2620 -0.0089 0.0477  0.0413  165  VAL   A CG2 
3623 C  CG2 B VAL   A 165 ? 0.1876 0.2693 0.2585 0.0059  0.0263  0.0697  165  VAL   A CG2 
3642 N  N   A SER   A 166 ? 0.1623 0.2471 0.2848 -0.0197 0.0229  0.0619  166  SER   A N   
3643 N  N   B SER   A 166 ? 0.1315 0.2914 0.2614 -0.0160 0.0415  0.0807  166  SER   A N   
3644 C  CA  A SER   A 166 ? 0.1614 0.2704 0.2935 -0.0249 0.0172  0.0623  166  SER   A CA  
3645 C  CA  B SER   A 166 ? 0.1423 0.3085 0.2821 -0.0142 0.0189  0.0671  166  SER   A CA  
3646 C  C   A SER   A 166 ? 0.1592 0.2980 0.2946 -0.0258 0.0074  0.0557  166  SER   A C   
3647 C  C   B SER   A 166 ? 0.1446 0.3260 0.2787 -0.0069 -0.0034 0.0644  166  SER   A C   
3648 O  O   A SER   A 166 ? 0.1609 0.2937 0.3186 -0.0274 0.0111  0.0446  166  SER   A O   
3649 O  O   B SER   A 166 ? 0.1626 0.3284 0.2992 -0.0033 -0.0053 0.0570  166  SER   A O   
3650 C  CB  A SER   A 166 ? 0.1849 0.2714 0.3115 -0.0284 0.0228  0.0722  166  SER   A CB  
3651 C  CB  B SER   A 166 ? 0.1650 0.3139 0.3173 -0.0058 0.0065  0.0453  166  SER   A CB  
3652 O  OG  A SER   A 166 ? 0.2105 0.2724 0.3324 -0.0393 0.0271  0.0806  166  SER   A OG  
3653 O  OG  B SER   A 166 ? 0.2106 0.3248 0.3544 -0.0081 0.0039  0.0348  166  SER   A OG  
3664 N  N   A SER   A 167 ? 0.1689 0.3302 0.2776 -0.0190 -0.0055 0.0524  167  SER   A N   
3665 N  N   B SER   A 167 ? 0.1450 0.3475 0.2557 0.0001  -0.0166 0.0683  167  SER   A N   
3666 C  CA  A SER   A 167 ? 0.1896 0.3606 0.2784 -0.0084 -0.0076 0.0417  167  SER   A CA  
3667 C  CA  B SER   A 167 ? 0.1718 0.3637 0.2544 0.0035  -0.0169 0.0599  167  SER   A CA  
3668 C  C   A SER   A 167 ? 0.1826 0.3723 0.2670 -0.0044 0.0006  0.0397  167  SER   A C   
3669 C  C   B SER   A 167 ? 0.1757 0.3687 0.2575 0.0030  -0.0032 0.0571  167  SER   A C   
3670 O  O   A SER   A 167 ? 0.1887 0.3735 0.2650 -0.0123 -0.0005 0.0390  167  SER   A O   
3671 O  O   B SER   A 167 ? 0.1821 0.3619 0.2634 0.0007  -0.0071 0.0623  167  SER   A O   
3672 C  CB  A SER   A 167 ? 0.2062 0.3751 0.2828 -0.0034 -0.0000 0.0422  167  SER   A CB  
3673 C  CB  B SER   A 167 ? 0.1847 0.3751 0.2541 0.0067  -0.0019 0.0644  167  SER   A CB  
3674 O  OG  A SER   A 167 ? 0.2188 0.3831 0.2882 -0.0036 0.0135  0.0468  167  SER   A OG  
3675 O  OG  B SER   A 167 ? 0.1909 0.3837 0.2528 0.0038  0.0189  0.0668  167  SER   A OG  
3686 N  N   . PHE   A 168 ? 0.1728 0.3811 0.2584 0.0116  0.0017  0.0428  168  PHE   A N   
3687 C  CA  . PHE   A 168 ? 0.1724 0.3963 0.2797 0.0113  0.0137  0.0272  168  PHE   A CA  
3688 C  C   . PHE   A 168 ? 0.2011 0.4307 0.3263 -0.0023 0.0482  0.0090  168  PHE   A C   
3689 O  O   . PHE   A 168 ? 0.2033 0.4348 0.3555 -0.0202 0.0535  0.0198  168  PHE   A O   
3690 C  CB  . PHE   A 168 ? 0.1738 0.3750 0.2628 0.0084  -0.0068 0.0361  168  PHE   A CB  
3691 C  CG  . PHE   A 168 ? 0.1704 0.3543 0.2485 -0.0033 -0.0153 0.0404  168  PHE   A CG  
3692 C  CD1 . PHE   A 168 ? 0.1745 0.3500 0.2488 -0.0047 -0.0123 0.0522  168  PHE   A CD1 
3693 C  CD2 . PHE   A 168 ? 0.1692 0.3417 0.2416 -0.0057 -0.0041 0.0348  168  PHE   A CD2 
3694 C  CE1 . PHE   A 168 ? 0.1616 0.3421 0.2334 -0.0107 -0.0066 0.0571  168  PHE   A CE1 
3695 C  CE2 . PHE   A 168 ? 0.1689 0.3303 0.2409 -0.0094 0.0056  0.0502  168  PHE   A CE2 
3696 C  CZ  . PHE   A 168 ? 0.1629 0.3327 0.2389 -0.0142 0.0032  0.0559  168  PHE   A CZ  
3707 N  N   . LEU   A 169 ? 0.2684 0.4588 0.3976 -0.0176 0.0335  -0.0140 169  LEU   A N   
3708 C  CA  . LEU   A 169 ? 0.3589 0.4884 0.5002 -0.0221 -0.0121 -0.0244 169  LEU   A CA  
3709 C  C   . LEU   A 169 ? 0.3839 0.4910 0.5322 -0.0272 -0.0285 -0.0157 169  LEU   A C   
3710 O  O   . LEU   A 169 ? 0.3926 0.4920 0.5426 -0.0289 -0.0300 -0.0147 169  LEU   A O   
3711 C  CB  . LEU   A 169 ? 0.4146 0.5098 0.5556 -0.0268 -0.0377 -0.0409 169  LEU   A CB  
3712 C  CG  . LEU   A 169 ? 0.4532 0.5251 0.5996 -0.0329 -0.0551 -0.0573 169  LEU   A CG  
3713 C  CD1 . LEU   A 169 ? 0.4672 0.5289 0.6172 -0.0331 -0.0604 -0.0625 169  LEU   A CD1 
3714 C  CD2 . LEU   A 169 ? 0.4670 0.5310 0.6125 -0.0360 -0.0577 -0.0629 169  LEU   A CD2 
3715 O  OXT . LEU   A 169 ? 0.3767 0.4887 0.5378 -0.0293 -0.0289 -0.0106 169  LEU   A OXT 
3727 N  N   A SER   B 1   ? 0.3623 0.3652 0.3832 -0.1094 -0.0768 0.0743  1    SER   B N   
3728 N  N   B SER   B 1   ? 0.3441 0.2930 0.3106 -0.1084 -0.0694 0.0225  1    SER   B N   
3729 C  CA  A SER   B 1   ? 0.3521 0.3614 0.3814 -0.1147 -0.0810 0.0756  1    SER   B CA  
3730 C  CA  B SER   B 1   ? 0.3351 0.2986 0.3121 -0.1125 -0.0778 0.0184  1    SER   B CA  
3731 C  C   A SER   B 1   ? 0.3271 0.3550 0.3662 -0.1131 -0.0904 0.0873  1    SER   B C   
3732 C  C   B SER   B 1   ? 0.3146 0.3143 0.3148 -0.1085 -0.0852 0.0448  1    SER   B C   
3733 O  O   A SER   B 1   ? 0.3337 0.3577 0.3533 -0.1059 -0.0929 0.0856  1    SER   B O   
3734 O  O   B SER   B 1   ? 0.3177 0.3168 0.3033 -0.1019 -0.0856 0.0470  1    SER   B O   
3735 C  CB  A SER   B 1   ? 0.3623 0.3613 0.3950 -0.1188 -0.0703 0.0666  1    SER   B CB  
3736 C  CB  B SER   B 1   ? 0.3444 0.2839 0.3148 -0.1144 -0.0708 -0.0111 1    SER   B CB  
3737 O  OG  A SER   B 1   ? 0.3732 0.3663 0.4245 -0.1210 -0.0567 0.0626  1    SER   B OG  
3738 O  OG  B SER   B 1   ? 0.3576 0.2825 0.3429 -0.1109 -0.0580 -0.0240 1    SER   B OG  
3753 N  N   A MET   B 2   ? 0.3008 0.3422 0.3682 -0.1153 -0.0891 0.1125  2    MET   B N   
3754 N  N   B MET   B 2   ? 0.3005 0.3241 0.3344 -0.1043 -0.0795 0.0839  2    MET   B N   
3755 C  CA  A MET   B 2   ? 0.2844 0.3361 0.3852 -0.0993 -0.0891 0.1179  2    MET   B CA  
3756 C  CA  B MET   B 2   ? 0.2958 0.3363 0.3583 -0.0831 -0.0728 0.1053  2    MET   B CA  
3757 C  C   A MET   B 2   ? 0.2457 0.3102 0.3496 -0.0886 -0.1051 0.1348  2    MET   B C   
3758 C  C   B MET   B 2   ? 0.2737 0.3226 0.3372 -0.0680 -0.0693 0.1235  2    MET   B C   
3759 O  O   A MET   B 2   ? 0.2252 0.3135 0.3426 -0.0900 -0.1218 0.1410  2    MET   B O   
3760 O  O   B MET   B 2   ? 0.2722 0.3344 0.3441 -0.0633 -0.0692 0.1214  2    MET   B O   
3761 C  CB  A MET   B 2   ? 0.3136 0.3644 0.4616 -0.0793 -0.0680 0.0909  2    MET   B CB  
3762 C  CB  B MET   B 2   ? 0.3197 0.3665 0.4232 -0.0664 -0.0668 0.0958  2    MET   B CB  
3763 C  CG  A MET   B 2   ? 0.3406 0.3873 0.5335 -0.0606 -0.0450 0.0744  2    MET   B CG  
3764 C  CG  B MET   B 2   ? 0.3402 0.3906 0.4782 -0.0517 -0.0574 0.0964  2    MET   B CG  
3765 S  SD  A MET   B 2   ? 0.3667 0.4088 0.5971 -0.0431 -0.0265 0.0620  2    MET   B SD  
3766 S  SD  B MET   B 2   ? 0.3611 0.4145 0.5251 -0.0361 -0.0502 0.0968  2    MET   B SD  
3767 C  CE  A MET   B 2   ? 0.3680 0.4112 0.5979 -0.0426 -0.0185 0.0605  2    MET   B CE  
3768 C  CE  B MET   B 2   ? 0.3605 0.4168 0.5292 -0.0361 -0.0471 0.0928  2    MET   B CE  
3787 N  N   A VAL   B 3   ? 0.2253 0.2731 0.3198 -0.0927 -0.1023 0.1390  3    VAL   B N   
3788 N  N   B VAL   B 3   ? 0.2526 0.2935 0.3104 -0.0659 -0.0660 0.1330  3    VAL   B N   
3789 C  CA  A VAL   B 3   ? 0.2165 0.2464 0.3053 -0.0854 -0.0975 0.1227  3    VAL   B CA  
3790 C  CA  B VAL   B 3   ? 0.2389 0.2692 0.2977 -0.0559 -0.0659 0.1156  3    VAL   B CA  
3791 C  C   A VAL   B 3   ? 0.1977 0.2330 0.2763 -0.0733 -0.0922 0.1118  3    VAL   B C   
3792 C  C   B VAL   B 3   ? 0.2154 0.2538 0.2676 -0.0490 -0.0637 0.1063  3    VAL   B C   
3793 O  O   A VAL   B 3   ? 0.1850 0.2243 0.2871 -0.0762 -0.0973 0.1217  3    VAL   B O   
3794 O  O   B VAL   B 3   ? 0.2118 0.2629 0.2686 -0.0302 -0.0573 0.1094  3    VAL   B O   
3795 C  CB  A VAL   B 3   ? 0.2378 0.2487 0.3455 -0.0793 -0.0862 0.1014  3    VAL   B CB  
3796 C  CB  B VAL   B 3   ? 0.2556 0.2664 0.3273 -0.0509 -0.0625 0.1031  3    VAL   B CB  
3797 C  CG1 A VAL   B 3   ? 0.2437 0.2465 0.3621 -0.0786 -0.0864 0.0925  3    VAL   B CG1 
3798 C  CG1 B VAL   B 3   ? 0.2605 0.2642 0.3409 -0.0514 -0.0652 0.0971  3    VAL   B CG1 
3799 C  CG2 A VAL   B 3   ? 0.2446 0.2539 0.3597 -0.0762 -0.0761 0.1002  3    VAL   B CG2 
3800 C  CG2 B VAL   B 3   ? 0.2620 0.2673 0.3310 -0.0478 -0.0604 0.1030  3    VAL   B CG2 
3819 N  N   . ASN   B 4   ? 0.1964 0.2274 0.2456 -0.0585 -0.0761 0.0990  4    ASN   B N   
3820 C  CA  . ASN   B 4   ? 0.1952 0.2218 0.2044 -0.0642 -0.0580 0.0525  4    ASN   B CA  
3821 C  C   . ASN   B 4   ? 0.2026 0.2371 0.1910 -0.0608 -0.0464 0.0445  4    ASN   B C   
3822 O  O   . ASN   B 4   ? 0.2053 0.2420 0.2090 -0.0592 -0.0409 0.0217  4    ASN   B O   
3823 C  CB  . ASN   B 4   ? 0.1955 0.2119 0.1881 -0.0567 -0.0599 0.0450  4    ASN   B CB  
3824 C  CG  . ASN   B 4   ? 0.1979 0.1950 0.1756 -0.0495 -0.0589 0.0380  4    ASN   B CG  
3825 O  OD1 . ASN   B 4   ? 0.2001 0.1777 0.1766 -0.0506 -0.0634 0.0285  4    ASN   B OD1 
3826 N  ND2 . ASN   B 4   ? 0.2185 0.2027 0.1808 -0.0290 -0.0416 0.0309  4    ASN   B ND2 
3834 N  N   . SER   B 5   ? 0.2153 0.2535 0.2141 -0.0599 -0.0268 0.0414  5    SER   B N   
3835 C  CA  . SER   B 5   ? 0.2418 0.2883 0.2432 -0.0453 -0.0123 0.0392  5    SER   B CA  
3836 C  C   . SER   B 5   ? 0.2630 0.2888 0.2777 -0.0642 0.0176  0.0398  5    SER   B C   
3837 O  O   . SER   B 5   ? 0.2805 0.2882 0.3382 -0.0554 0.0537  0.0351  5    SER   B O   
3838 C  CB  . SER   B 5   ? 0.2526 0.3111 0.2721 -0.0325 -0.0042 0.0492  5    SER   B CB  
3839 O  OG  . SER   B 5   ? 0.2767 0.3366 0.3251 -0.0198 -0.0023 0.0551  5    SER   B OG  
3845 N  N   . PHE   B 6   ? 0.2798 0.3000 0.2532 -0.0711 0.0299  0.0377  6    PHE   B N   
3846 C  CA  . PHE   B 6   ? 0.2909 0.3022 0.2168 -0.0889 0.0354  0.0227  6    PHE   B CA  
3847 C  C   . PHE   B 6   ? 0.3427 0.3323 0.2616 -0.0918 0.0563  -0.0038 6    PHE   B C   
3848 O  O   . PHE   B 6   ? 0.3562 0.3622 0.2896 -0.0829 0.0412  -0.0196 6    PHE   B O   
3849 C  CB  . PHE   B 6   ? 0.2593 0.2829 0.1944 -0.0834 0.0131  0.0160  6    PHE   B CB  
3850 C  CG  . PHE   B 6   ? 0.2266 0.2526 0.1806 -0.0777 -0.0043 0.0153  6    PHE   B CG  
3851 C  CD1 . PHE   B 6   ? 0.2288 0.2235 0.1666 -0.0687 -0.0229 0.0145  6    PHE   B CD1 
3852 C  CD2 . PHE   B 6   ? 0.2037 0.2505 0.1795 -0.0639 -0.0039 0.0338  6    PHE   B CD2 
3853 C  CE1 . PHE   B 6   ? 0.2259 0.2019 0.1779 -0.0569 -0.0224 0.0129  6    PHE   B CE1 
3854 C  CE2 . PHE   B 6   ? 0.2059 0.2325 0.1994 -0.0501 -0.0017 0.0381  6    PHE   B CE2 
3855 C  CZ  . PHE   B 6   ? 0.2118 0.2086 0.1843 -0.0508 -0.0114 0.0225  6    PHE   B CZ  
3865 N  N   . SER   B 7   ? 0.3795 0.3165 0.2785 -0.1123 0.0866  -0.0289 7    SER   B N   
3866 C  CA  . SER   B 7   ? 0.4163 0.3292 0.3295 -0.1107 0.1072  -0.0399 7    SER   B CA  
3867 C  C   . SER   B 7   ? 0.4134 0.3135 0.3189 -0.1146 0.1273  -0.0494 7    SER   B C   
3868 O  O   . SER   B 7   ? 0.4203 0.3115 0.3467 -0.1185 0.1294  -0.0506 7    SER   B O   
3869 C  CB  . SER   B 7   ? 0.4423 0.3459 0.3870 -0.1072 0.1182  -0.0389 7    SER   B CB  
3870 O  OG  . SER   B 7   ? 0.4596 0.3582 0.4388 -0.1047 0.1162  -0.0304 7    SER   B OG  
3876 N  N   . GLY   B 8   ? 0.4124 0.3050 0.3249 -0.0991 0.1281  -0.0577 8    GLY   B N   
3877 C  CA  . GLY   B 8   ? 0.3959 0.2875 0.3176 -0.0950 0.1343  -0.0637 8    GLY   B CA  
3878 C  C   . GLY   B 8   ? 0.3743 0.2607 0.3071 -0.0945 0.1327  -0.0600 8    GLY   B C   
3879 O  O   . GLY   B 8   ? 0.3850 0.2710 0.3459 -0.0830 0.1333  -0.0650 8    GLY   B O   
3883 N  N   . TYR   B 9   ? 0.3515 0.2415 0.2778 -0.0862 0.1037  -0.0701 9    TYR   B N   
3884 C  CA  . TYR   B 9   ? 0.3269 0.2149 0.2490 -0.0722 0.0720  -0.0532 9    TYR   B CA  
3885 C  C   . TYR   B 9   ? 0.3204 0.2166 0.2347 -0.0611 0.0355  -0.0405 9    TYR   B C   
3886 O  O   . TYR   B 9   ? 0.3323 0.2391 0.2677 -0.0612 0.0338  -0.0236 9    TYR   B O   
3887 C  CB  . TYR   B 9   ? 0.3173 0.1935 0.2545 -0.0646 0.0647  -0.0518 9    TYR   B CB  
3888 C  CG  . TYR   B 9   ? 0.3056 0.1806 0.2565 -0.0704 0.0634  -0.0501 9    TYR   B CG  
3889 C  CD1 . TYR   B 9   ? 0.3050 0.1812 0.2751 -0.0833 0.0687  -0.0459 9    TYR   B CD1 
3890 C  CD2 . TYR   B 9   ? 0.2905 0.1784 0.2470 -0.0637 0.0587  -0.0556 9    TYR   B CD2 
3891 C  CE1 . TYR   B 9   ? 0.2985 0.1923 0.2855 -0.0889 0.0720  -0.0548 9    TYR   B CE1 
3892 C  CE2 . TYR   B 9   ? 0.2907 0.1820 0.2631 -0.0634 0.0609  -0.0552 9    TYR   B CE2 
3893 C  CZ  . TYR   B 9   ? 0.2935 0.1952 0.2747 -0.0796 0.0662  -0.0681 9    TYR   B CZ  
3894 O  OH  . TYR   B 9   ? 0.2906 0.2103 0.2847 -0.0871 0.0688  -0.0839 9    TYR   B OH  
3904 N  N   . LEU   B 10  ? 0.2977 0.1912 0.2090 -0.0596 0.0106  -0.0367 10   LEU   B N   
3905 C  CA  . LEU   B 10  ? 0.2939 0.1877 0.2138 -0.0614 -0.0141 -0.0361 10   LEU   B CA  
3906 C  C   . LEU   B 10  ? 0.2752 0.1881 0.2174 -0.0584 -0.0357 -0.0301 10   LEU   B C   
3907 O  O   . LEU   B 10  ? 0.2613 0.1871 0.2153 -0.0454 -0.0271 -0.0189 10   LEU   B O   
3908 C  CB  . LEU   B 10  ? 0.3087 0.1843 0.2285 -0.0661 -0.0322 -0.0214 10   LEU   B CB  
3909 C  CG  . LEU   B 10  ? 0.3244 0.1936 0.2603 -0.0602 -0.0600 -0.0113 10   LEU   B CG  
3910 C  CD1 . LEU   B 10  ? 0.3318 0.2043 0.2816 -0.0592 -0.0599 -0.0135 10   LEU   B CD1 
3911 C  CD2 . LEU   B 10  ? 0.3346 0.2007 0.2910 -0.0605 -0.0570 0.0090  10   LEU   B CD2 
3923 N  N   . LYS   B 11  ? 0.2868 0.2172 0.2255 -0.0497 -0.0429 -0.0250 11   LYS   B N   
3924 C  CA  . LYS   B 11  ? 0.3050 0.2426 0.2517 -0.0376 -0.0518 -0.0255 11   LYS   B CA  
3925 C  C   . LYS   B 11  ? 0.2846 0.2213 0.2669 -0.0623 -0.0438 -0.0396 11   LYS   B C   
3926 O  O   . LYS   B 11  ? 0.2990 0.2414 0.3026 -0.0760 -0.0397 -0.0737 11   LYS   B O   
3927 C  CB  . LYS   B 11  ? 0.3435 0.2926 0.3039 -0.0091 -0.0569 -0.0217 11   LYS   B CB  
3928 C  CG  . LYS   B 11  ? 0.3776 0.3278 0.3746 0.0083  -0.0569 -0.0252 11   LYS   B CG  
3929 C  CD  . LYS   B 11  ? 0.4044 0.3515 0.4394 0.0182  -0.0563 -0.0329 11   LYS   B CD  
3930 C  CE  . LYS   B 11  ? 0.4232 0.3676 0.4898 0.0229  -0.0541 -0.0341 11   LYS   B CE  
3931 N  NZ  . LYS   B 11  ? 0.4351 0.3774 0.5186 0.0241  -0.0515 -0.0318 11   LYS   B NZ  
3945 N  N   . LEU   B 12  ? 0.2487 0.1992 0.2660 -0.0566 -0.0462 -0.0434 12   LEU   B N   
3946 C  CA  . LEU   B 12  ? 0.2311 0.1826 0.2772 -0.0504 -0.0406 -0.0382 12   LEU   B CA  
3947 C  C   . LEU   B 12  ? 0.2206 0.1852 0.2762 -0.0506 -0.0540 -0.0346 12   LEU   B C   
3948 O  O   . LEU   B 12  ? 0.2237 0.1870 0.2962 -0.0628 -0.0625 -0.0257 12   LEU   B O   
3949 C  CB  . LEU   B 12  ? 0.2252 0.1628 0.2802 -0.0390 -0.0315 -0.0419 12   LEU   B CB  
3950 C  CG  . LEU   B 12  ? 0.2252 0.1576 0.2806 -0.0371 -0.0213 -0.0317 12   LEU   B CG  
3951 C  CD1 . LEU   B 12  ? 0.2358 0.1634 0.2831 -0.0236 -0.0188 -0.0212 12   LEU   B CD1 
3952 C  CD2 . LEU   B 12  ? 0.2306 0.1599 0.2889 -0.0376 -0.0195 -0.0399 12   LEU   B CD2 
3964 N  N   . THR   B 13  ? 0.2117 0.1893 0.2852 -0.0484 -0.0542 -0.0387 13   THR   B N   
3965 C  CA  . THR   B 13  ? 0.2146 0.1902 0.2779 -0.0554 -0.0636 -0.0272 13   THR   B CA  
3966 C  C   . THR   B 13  ? 0.2559 0.2077 0.2945 -0.0625 -0.0747 -0.0228 13   THR   B C   
3967 O  O   . THR   B 13  ? 0.2729 0.2089 0.3125 -0.0615 -0.0412 -0.0264 13   THR   B O   
3968 C  CB  . THR   B 13  ? 0.2034 0.1912 0.2892 -0.0506 -0.0613 -0.0226 13   THR   B CB  
3969 O  OG1 . THR   B 13  ? 0.1944 0.1814 0.2964 -0.0439 -0.0506 -0.0185 13   THR   B OG1 
3970 C  CG2 . THR   B 13  ? 0.2130 0.1984 0.2887 -0.0434 -0.0575 -0.0223 13   THR   B CG2 
3978 N  N   A ASP   B 14  ? 0.2691 0.2186 0.3083 -0.0660 -0.0961 -0.0127 14   ASP   B N   
3979 N  N   B ASP   B 14  ? 0.2707 0.2202 0.3032 -0.0636 -0.0944 -0.0081 14   ASP   B N   
3980 C  CA  A ASP   B 14  ? 0.2798 0.2343 0.3336 -0.0679 -0.1003 0.0052  14   ASP   B CA  
3981 C  CA  B ASP   B 14  ? 0.2826 0.2372 0.3227 -0.0634 -0.0976 0.0131  14   ASP   B CA  
3982 C  C   A ASP   B 14  ? 0.2685 0.2196 0.2980 -0.0717 -0.0907 0.0143  14   ASP   B C   
3983 C  C   B ASP   B 14  ? 0.2694 0.2206 0.2922 -0.0687 -0.0927 0.0181  14   ASP   B C   
3984 O  O   A ASP   B 14  ? 0.2916 0.2352 0.3042 -0.0734 -0.0850 0.0240  14   ASP   B O   
3985 O  O   B ASP   B 14  ? 0.2919 0.2338 0.2990 -0.0694 -0.0925 0.0270  14   ASP   B O   
3986 C  CB  A ASP   B 14  ? 0.2995 0.2653 0.3947 -0.0638 -0.1092 0.0061  14   ASP   B CB  
3987 C  CB  B ASP   B 14  ? 0.3053 0.2709 0.3737 -0.0554 -0.1000 0.0204  14   ASP   B CB  
3988 C  CG  A ASP   B 14  ? 0.3210 0.2904 0.4559 -0.0603 -0.1024 -0.0011 14   ASP   B CG  
3989 C  CG  B ASP   B 14  ? 0.3292 0.2991 0.4260 -0.0485 -0.0874 0.0180  14   ASP   B CG  
3990 O  OD1 A ASP   B 14  ? 0.3307 0.2960 0.4684 -0.0662 -0.1017 -0.0092 14   ASP   B OD1 
3991 O  OD1 B ASP   B 14  ? 0.3391 0.3078 0.4356 -0.0487 -0.0805 0.0117  14   ASP   B OD1 
3992 O  OD2 A ASP   B 14  ? 0.3261 0.3015 0.4862 -0.0581 -0.0980 0.0007  14   ASP   B OD2 
3993 O  OD2 B ASP   B 14  ? 0.3367 0.3114 0.4519 -0.0481 -0.0833 0.0224  14   ASP   B OD2 
4002 N  N   . ASN   B 15  ? 0.2388 0.1934 0.2662 -0.0579 -0.0913 0.0133  15   ASN   B N   
4003 C  CA  . ASN   B 15  ? 0.1948 0.1703 0.2546 -0.0350 -0.0679 0.0041  15   ASN   B CA  
4004 C  C   . ASN   B 15  ? 0.1741 0.1552 0.2400 -0.0191 -0.0577 -0.0014 15   ASN   B C   
4005 O  O   . ASN   B 15  ? 0.1748 0.1518 0.2498 -0.0209 -0.0582 -0.0165 15   ASN   B O   
4006 C  CB  . ASN   B 15  ? 0.1886 0.1665 0.2701 -0.0186 -0.0638 0.0026  15   ASN   B CB  
4007 C  CG  . ASN   B 15  ? 0.1719 0.1594 0.2646 -0.0213 -0.0378 0.0091  15   ASN   B CG  
4008 O  OD1 . ASN   B 15  ? 0.1744 0.1893 0.3002 -0.0401 -0.0370 0.0124  15   ASN   B OD1 
4009 N  ND2 . ASN   B 15  ? 0.1728 0.1395 0.2557 -0.0096 -0.0094 -0.0082 15   ASN   B ND2 
4017 N  N   . VAL   B 16  ? 0.1748 0.1472 0.2456 -0.0274 -0.0580 -0.0031 16   VAL   B N   
4018 C  CA  . VAL   B 16  ? 0.1763 0.1508 0.2291 -0.0245 -0.0445 -0.0221 16   VAL   B CA  
4019 C  C   . VAL   B 16  ? 0.1730 0.1613 0.2157 -0.0332 -0.0445 -0.0182 16   VAL   B C   
4020 O  O   . VAL   B 16  ? 0.1827 0.1718 0.2383 -0.0242 -0.0398 -0.0331 16   VAL   B O   
4021 C  CB  . VAL   B 16  ? 0.1790 0.1495 0.2383 -0.0102 -0.0309 -0.0193 16   VAL   B CB  
4022 C  CG1 . VAL   B 16  ? 0.1933 0.1482 0.2335 0.0041  -0.0299 -0.0097 16   VAL   B CG1 
4023 C  CG2 . VAL   B 16  ? 0.1785 0.1554 0.2492 -0.0089 -0.0293 -0.0160 16   VAL   B CG2 
4033 N  N   . TYR   B 17  ? 0.1832 0.1680 0.2109 -0.0289 -0.0323 -0.0161 17   TYR   B N   
4034 C  CA  . TYR   B 17  ? 0.1881 0.1841 0.2040 -0.0382 -0.0345 -0.0004 17   TYR   B CA  
4035 C  C   . TYR   B 17  ? 0.1826 0.1544 0.2000 -0.0426 -0.0255 -0.0153 17   TYR   B C   
4036 O  O   . TYR   B 17  ? 0.1815 0.1626 0.2124 -0.0343 -0.0332 -0.0350 17   TYR   B O   
4037 C  CB  . TYR   B 17  ? 0.2204 0.2299 0.2300 -0.0204 -0.0310 0.0275  17   TYR   B CB  
4038 C  CG  . TYR   B 17  ? 0.2476 0.2803 0.2713 -0.0097 -0.0432 0.0348  17   TYR   B CG  
4039 C  CD1 . TYR   B 17  ? 0.2654 0.2992 0.2901 -0.0055 -0.0553 0.0427  17   TYR   B CD1 
4040 C  CD2 . TYR   B 17  ? 0.2730 0.3162 0.2936 -0.0022 -0.0482 0.0367  17   TYR   B CD2 
4041 C  CE1 . TYR   B 17  ? 0.2851 0.3295 0.3043 0.0032  -0.0621 0.0445  17   TYR   B CE1 
4042 C  CE2 . TYR   B 17  ? 0.2888 0.3393 0.3119 0.0096  -0.0604 0.0442  17   TYR   B CE2 
4043 C  CZ  . TYR   B 17  ? 0.2971 0.3435 0.3160 0.0119  -0.0663 0.0482  17   TYR   B CZ  
4044 O  OH  . TYR   B 17  ? 0.3132 0.3624 0.3279 0.0201  -0.0736 0.0482  17   TYR   B OH  
4054 N  N   . ILE   B 18  ? 0.1904 0.1572 0.1915 -0.0353 -0.0172 -0.0183 18   ILE   B N   
4055 C  CA  . ILE   B 18  ? 0.1954 0.1545 0.1828 -0.0367 -0.0153 -0.0199 18   ILE   B CA  
4056 C  C   . ILE   B 18  ? 0.2023 0.1578 0.1867 -0.0415 -0.0113 -0.0309 18   ILE   B C   
4057 O  O   . ILE   B 18  ? 0.2192 0.1778 0.2027 -0.0384 0.0028  -0.0355 18   ILE   B O   
4058 C  CB  . ILE   B 18  ? 0.1979 0.1503 0.1957 -0.0408 -0.0155 -0.0161 18   ILE   B CB  
4059 C  CG1 . ILE   B 18  ? 0.2039 0.1573 0.2161 -0.0398 -0.0101 -0.0031 18   ILE   B CG1 
4060 C  CG2 . ILE   B 18  ? 0.2061 0.1616 0.2011 -0.0421 -0.0207 -0.0130 18   ILE   B CG2 
4061 C  CD1 . ILE   B 18  ? 0.2083 0.1846 0.2318 -0.0371 -0.0289 0.0107  18   ILE   B CD1 
4073 N  N   . LYS   B 19  ? 0.2006 0.1577 0.2066 -0.0229 0.0301  -0.0407 19   LYS   B N   
4074 C  CA  . LYS   B 19  ? 0.2113 0.1574 0.2274 -0.0269 0.0265  -0.0386 19   LYS   B CA  
4075 C  C   . LYS   B 19  ? 0.2006 0.1571 0.2358 -0.0218 0.0292  -0.0465 19   LYS   B C   
4076 O  O   . LYS   B 19  ? 0.1964 0.1586 0.2180 -0.0117 0.0145  -0.0371 19   LYS   B O   
4077 C  CB  . LYS   B 19  ? 0.2341 0.1751 0.2352 -0.0324 0.0366  -0.0222 19   LYS   B CB  
4078 C  CG  . LYS   B 19  ? 0.2604 0.1921 0.2572 -0.0374 0.0485  -0.0243 19   LYS   B CG  
4079 C  CD  . LYS   B 19  ? 0.2888 0.2252 0.2708 -0.0445 0.0543  -0.0141 19   LYS   B CD  
4080 C  CE  . LYS   B 19  ? 0.3153 0.2530 0.2933 -0.0476 0.0484  -0.0163 19   LYS   B CE  
4081 N  NZ  . LYS   B 19  ? 0.3338 0.2715 0.3065 -0.0530 0.0460  -0.0169 19   LYS   B NZ  
4095 N  N   . ASN   B 20  ? 0.1948 0.1697 0.2732 -0.0161 0.0327  -0.0575 20   ASN   B N   
4096 C  CA  . ASN   B 20  ? 0.1958 0.1839 0.3011 -0.0146 0.0362  -0.0740 20   ASN   B CA  
4097 C  C   . ASN   B 20  ? 0.1870 0.2032 0.3052 -0.0203 0.0465  -0.0807 20   ASN   B C   
4098 O  O   . ASN   B 20  ? 0.2058 0.2389 0.3181 -0.0328 0.0500  -0.0792 20   ASN   B O   
4099 C  CB  . ASN   B 20  ? 0.2214 0.1864 0.3312 0.0072  0.0212  -0.0814 20   ASN   B CB  
4100 C  CG  . ASN   B 20  ? 0.2500 0.1923 0.3605 0.0332  0.0161  -0.0904 20   ASN   B CG  
4101 O  OD1 . ASN   B 20  ? 0.2785 0.2224 0.3904 0.0500  0.0162  -0.0931 20   ASN   B OD1 
4102 N  ND2 . ASN   B 20  ? 0.2445 0.1921 0.3526 0.0280  0.0027  -0.0913 20   ASN   B ND2 
4109 N  N   . ALA   B 21  ? 0.1921 0.1838 0.3026 -0.0247 0.0415  -0.0657 21   ALA   B N   
4110 C  CA  . ALA   B 21  ? 0.2023 0.1943 0.3115 -0.0258 0.0309  -0.0498 21   ALA   B CA  
4111 C  C   . ALA   B 21  ? 0.2000 0.1700 0.2972 -0.0211 0.0369  -0.0313 21   ALA   B C   
4112 O  O   . ALA   B 21  ? 0.1996 0.1594 0.2949 -0.0328 0.0342  -0.0285 21   ALA   B O   
4113 C  CB  . ALA   B 21  ? 0.2170 0.2220 0.3143 -0.0366 0.0343  -0.0325 21   ALA   B CB  
4119 N  N   . ASP   B 22  ? 0.1926 0.1602 0.2825 -0.0185 0.0292  -0.0262 22   ASP   B N   
4120 C  CA  . ASP   B 22  ? 0.1922 0.1518 0.2627 -0.0077 0.0242  -0.0222 22   ASP   B CA  
4121 C  C   . ASP   B 22  ? 0.1880 0.1546 0.2229 -0.0119 0.0174  -0.0071 22   ASP   B C   
4122 O  O   . ASP   B 22  ? 0.1892 0.1539 0.2390 -0.0095 0.0064  -0.0024 22   ASP   B O   
4123 C  CB  . ASP   B 22  ? 0.2003 0.1591 0.3030 -0.0058 0.0235  -0.0128 22   ASP   B CB  
4124 C  CG  . ASP   B 22  ? 0.2019 0.1797 0.3424 -0.0005 -0.0053 -0.0108 22   ASP   B CG  
4125 O  OD1 . ASP   B 22  ? 0.2174 0.1727 0.3468 0.0045  -0.0207 -0.0129 22   ASP   B OD1 
4126 O  OD2 . ASP   B 22  ? 0.2081 0.2093 0.3900 0.0099  -0.0242 -0.0240 22   ASP   B OD2 
4131 N  N   . ILE   B 23  ? 0.1890 0.1449 0.2116 -0.0082 0.0053  0.0147  23   ILE   B N   
4132 C  CA  . ILE   B 23  ? 0.1778 0.1475 0.1895 -0.0114 -0.0046 0.0068  23   ILE   B CA  
4133 C  C   . ILE   B 23  ? 0.1684 0.1467 0.1882 -0.0117 -0.0139 0.0024  23   ILE   B C   
4134 O  O   . ILE   B 23  ? 0.1659 0.1473 0.1846 -0.0091 -0.0118 0.0084  23   ILE   B O   
4135 C  CB  . ILE   B 23  ? 0.1734 0.1533 0.2002 -0.0200 -0.0061 0.0198  23   ILE   B CB  
4136 C  CG1 . ILE   B 23  ? 0.1754 0.1593 0.2192 -0.0143 -0.0019 0.0280  23   ILE   B CG1 
4137 C  CG2 . ILE   B 23  ? 0.1819 0.1709 0.2170 -0.0195 0.0004  0.0150  23   ILE   B CG2 
4138 C  CD1 . ILE   B 23  ? 0.1825 0.1729 0.2302 -0.0105 0.0007  0.0241  23   ILE   B CD1 
4150 N  N   . VAL   B 24  ? 0.1710 0.1459 0.2029 -0.0157 -0.0129 0.0053  24   VAL   B N   
4151 C  CA  . VAL   B 24  ? 0.1706 0.1522 0.2161 -0.0114 -0.0219 0.0057  24   VAL   B CA  
4152 C  C   . VAL   B 24  ? 0.1670 0.1537 0.2297 -0.0085 -0.0114 0.0118  24   VAL   B C   
4153 O  O   . VAL   B 24  ? 0.1653 0.1592 0.2234 -0.0158 -0.0094 0.0191  24   VAL   B O   
4154 C  CB  . VAL   B 24  ? 0.1768 0.1732 0.2153 -0.0022 -0.0259 0.0052  24   VAL   B CB  
4155 C  CG1 . VAL   B 24  ? 0.1770 0.1759 0.2367 -0.0064 -0.0229 -0.0013 24   VAL   B CG1 
4156 C  CG2 . VAL   B 24  ? 0.1875 0.2041 0.2147 0.0117  -0.0362 -0.0004 24   VAL   B CG2 
4166 N  N   . GLU   B 25  ? 0.1841 0.1674 0.2333 -0.0114 -0.0005 0.0064  25   GLU   B N   
4167 C  CA  . GLU   B 25  ? 0.1975 0.1990 0.2469 -0.0023 0.0110  0.0013  25   GLU   B CA  
4168 C  C   . GLU   B 25  ? 0.1937 0.1887 0.2136 -0.0120 0.0110  0.0044  25   GLU   B C   
4169 O  O   . GLU   B 25  ? 0.1911 0.2005 0.2280 -0.0144 0.0152  0.0088  25   GLU   B O   
4170 C  CB  . GLU   B 25  ? 0.2337 0.2513 0.3143 0.0178  0.0260  -0.0009 25   GLU   B CB  
4171 C  CG  . GLU   B 25  ? 0.2719 0.3175 0.4165 0.0279  0.0233  -0.0089 25   GLU   B CG  
4172 C  CD  . GLU   B 25  ? 0.3130 0.3757 0.5036 0.0239  0.0196  -0.0124 25   GLU   B CD  
4173 O  OE1 . GLU   B 25  ? 0.3228 0.3980 0.5337 0.0297  0.0266  -0.0132 25   GLU   B OE1 
4174 O  OE2 . GLU   B 25  ? 0.3176 0.3956 0.5404 0.0219  0.0116  -0.0182 25   GLU   B OE2 
4181 N  N   A GLU   B 26  ? 0.1933 0.1773 0.1911 -0.0273 0.0040  0.0055  26   GLU   B N   
4182 N  N   B GLU   B 26  ? 0.1915 0.1817 0.2037 -0.0241 0.0065  0.0121  26   GLU   B N   
4183 C  CA  A GLU   B 26  ? 0.1974 0.1823 0.1930 -0.0346 -0.0092 0.0013  26   GLU   B CA  
4184 C  CA  B GLU   B 26  ? 0.1925 0.1895 0.2197 -0.0293 -0.0047 0.0149  26   GLU   B CA  
4185 C  C   A GLU   B 26  ? 0.1835 0.1793 0.1923 -0.0252 -0.0020 0.0153  26   GLU   B C   
4186 C  C   B GLU   B 26  ? 0.1812 0.1832 0.2029 -0.0226 0.0008  0.0221  26   GLU   B C   
4187 O  O   A GLU   B 26  ? 0.1945 0.1934 0.1984 -0.0243 -0.0099 0.0224  26   GLU   B O   
4188 O  O   B GLU   B 26  ? 0.1924 0.1975 0.2053 -0.0214 -0.0067 0.0289  26   GLU   B O   
4189 C  CB  A GLU   B 26  ? 0.2232 0.1896 0.1977 -0.0393 -0.0083 0.0061  26   GLU   B CB  
4190 C  CB  B GLU   B 26  ? 0.2111 0.2014 0.2535 -0.0315 -0.0020 0.0293  26   GLU   B CB  
4191 C  CG  A GLU   B 26  ? 0.2519 0.2028 0.2116 -0.0358 0.0011  -0.0049 26   GLU   B CG  
4192 C  CG  B GLU   B 26  ? 0.2316 0.2197 0.2997 -0.0264 0.0090  0.0246  26   GLU   B CG  
4193 C  CD  A GLU   B 26  ? 0.2701 0.2053 0.2025 -0.0422 0.0205  -0.0210 26   GLU   B CD  
4194 C  CD  B GLU   B 26  ? 0.2354 0.2214 0.3150 -0.0310 0.0242  0.0201  26   GLU   B CD  
4195 O  OE1 A GLU   B 26  ? 0.2780 0.1975 0.1884 -0.0365 0.0458  -0.0311 26   GLU   B OE1 
4196 O  OE1 B GLU   B 26  ? 0.2390 0.2226 0.3425 -0.0388 0.0484  0.0154  26   GLU   B OE1 
4197 O  OE2 A GLU   B 26  ? 0.2779 0.2220 0.2217 -0.0462 0.0239  -0.0012 26   GLU   B OE2 
4198 O  OE2 B GLU   B 26  ? 0.2291 0.2171 0.3063 -0.0222 0.0218  0.0041  26   GLU   B OE2 
4211 N  N   . ALA   B 27  ? 0.1667 0.1651 0.1922 -0.0205 0.0065  0.0174  27   ALA   B N   
4212 C  CA  . ALA   B 27  ? 0.1671 0.1653 0.2059 -0.0167 -0.0059 0.0322  27   ALA   B CA  
4213 C  C   . ALA   B 27  ? 0.1652 0.1757 0.2338 -0.0157 0.0116  0.0457  27   ALA   B C   
4214 O  O   . ALA   B 27  ? 0.1776 0.1803 0.2478 -0.0061 0.0033  0.0500  27   ALA   B O   
4215 C  CB  . ALA   B 27  ? 0.1869 0.1515 0.2106 -0.0172 -0.0064 0.0252  27   ALA   B CB  
4222 N  N   . LYS   B 28  ? 0.1574 0.1933 0.2688 -0.0176 0.0171  0.0632  28   LYS   B N   
4223 C  CA  . LYS   B 28  ? 0.1780 0.2361 0.2865 -0.0082 0.0494  0.0890  28   LYS   B CA  
4224 C  C   . LYS   B 28  ? 0.2048 0.2543 0.2716 0.0040  0.0573  0.0829  28   LYS   B C   
4225 O  O   . LYS   B 28  ? 0.2278 0.2578 0.2883 0.0062  0.0604  0.0818  28   LYS   B O   
4226 C  CB  . LYS   B 28  ? 0.1929 0.2751 0.3409 0.0034  0.0619  0.1044  28   LYS   B CB  
4227 C  CG  . LYS   B 28  ? 0.2143 0.3253 0.3858 0.0154  0.0607  0.1092  28   LYS   B CG  
4228 C  CD  . LYS   B 28  ? 0.2474 0.3823 0.4404 0.0209  0.0786  0.1096  28   LYS   B CD  
4229 C  CE  . LYS   B 28  ? 0.2708 0.4174 0.4872 0.0308  0.0821  0.1104  28   LYS   B CE  
4230 N  NZ  . LYS   B 28  ? 0.2745 0.4333 0.5104 0.0387  0.0824  0.1147  28   LYS   B NZ  
4244 N  N   . LYS   B 29  ? 0.2222 0.2811 0.2702 0.0208  0.0520  0.0620  29   LYS   B N   
4245 C  CA  . LYS   B 29  ? 0.2655 0.3143 0.2985 0.0201  0.0466  0.0659  29   LYS   B CA  
4246 C  C   . LYS   B 29  ? 0.2598 0.3146 0.2683 0.0160  0.0303  0.0754  29   LYS   B C   
4247 O  O   . LYS   B 29  ? 0.2765 0.3360 0.2766 0.0236  0.0326  0.0725  29   LYS   B O   
4248 C  CB  . LYS   B 29  ? 0.3178 0.3512 0.3743 0.0199  0.0509  0.0500  29   LYS   B CB  
4249 C  CG  . LYS   B 29  ? 0.3646 0.3819 0.4531 0.0172  0.0560  0.0451  29   LYS   B CG  
4250 C  CD  . LYS   B 29  ? 0.4017 0.4028 0.5181 0.0127  0.0671  0.0376  29   LYS   B CD  
4251 C  CE  . LYS   B 29  ? 0.4270 0.4157 0.5640 0.0101  0.0787  0.0320  29   LYS   B CE  
4252 N  NZ  . LYS   B 29  ? 0.4377 0.4248 0.5929 0.0090  0.0837  0.0285  29   LYS   B NZ  
4266 N  N   . VAL   B 30  ? 0.2303 0.2929 0.2515 -0.0039 0.0172  0.0828  30   VAL   B N   
4267 C  CA  . VAL   B 30  ? 0.2146 0.2787 0.2868 -0.0176 -0.0127 0.0867  30   VAL   B CA  
4268 C  C   . VAL   B 30  ? 0.1899 0.2732 0.2812 -0.0180 -0.0092 0.1045  30   VAL   B C   
4269 O  O   . VAL   B 30  ? 0.2003 0.2901 0.2793 -0.0100 0.0026  0.1218  30   VAL   B O   
4270 C  CB  . VAL   B 30  ? 0.2191 0.2718 0.3290 -0.0317 -0.0404 0.0732  30   VAL   B CB  
4271 C  CG1 . VAL   B 30  ? 0.2245 0.2795 0.3345 -0.0312 -0.0399 0.0651  30   VAL   B CG1 
4272 C  CG2 . VAL   B 30  ? 0.2316 0.2707 0.3432 -0.0370 -0.0452 0.0611  30   VAL   B CG2 
4282 N  N   . LYS   B 31  ? 0.1816 0.2373 0.3132 -0.0275 -0.0187 0.1093  31   LYS   B N   
4283 C  CA  . LYS   B 31  ? 0.1736 0.2275 0.3498 -0.0382 -0.0138 0.1099  31   LYS   B CA  
4284 C  C   . LYS   B 31  ? 0.1698 0.1909 0.3048 -0.0404 -0.0421 0.0884  31   LYS   B C   
4285 O  O   . LYS   B 31  ? 0.1736 0.2088 0.3133 -0.0331 -0.0312 0.1061  31   LYS   B O   
4286 C  CB  . LYS   B 31  ? 0.1790 0.2764 0.4071 -0.0269 0.0162  0.1203  31   LYS   B CB  
4287 C  CG  . LYS   B 31  ? 0.2092 0.3252 0.4538 -0.0218 0.0311  0.1149  31   LYS   B CG  
4288 C  CD  . LYS   B 31  ? 0.2378 0.3682 0.4910 -0.0124 0.0317  0.1055  31   LYS   B CD  
4289 C  CE  . LYS   B 31  ? 0.2606 0.3957 0.5240 -0.0047 0.0229  0.0931  31   LYS   B CE  
4290 N  NZ  . LYS   B 31  ? 0.2771 0.4096 0.5367 0.0056  0.0124  0.0798  31   LYS   B NZ  
4304 N  N   . PRO   B 32  ? 0.1844 0.1620 0.2398 -0.0398 -0.0599 0.0553  32   PRO   B N   
4305 C  CA  . PRO   B 32  ? 0.1945 0.1562 0.1935 -0.0379 -0.0526 0.0375  32   PRO   B CA  
4306 C  C   . PRO   B 32  ? 0.2027 0.1456 0.1953 -0.0402 -0.0661 0.0358  32   PRO   B C   
4307 O  O   . PRO   B 32  ? 0.2145 0.1521 0.2332 -0.0438 -0.0837 0.0342  32   PRO   B O   
4308 C  CB  . PRO   B 32  ? 0.2090 0.1511 0.1997 -0.0399 -0.0415 0.0213  32   PRO   B CB  
4309 C  CG  . PRO   B 32  ? 0.2219 0.1443 0.2058 -0.0361 -0.0597 0.0278  32   PRO   B CG  
4310 C  CD  . PRO   B 32  ? 0.2094 0.1448 0.2230 -0.0293 -0.0672 0.0346  32   PRO   B CD  
4318 N  N   . THR   B 33  ? 0.2069 0.1369 0.1829 -0.0386 -0.0577 0.0350  33   THR   B N   
4319 C  CA  . THR   B 33  ? 0.2140 0.1426 0.1792 -0.0387 -0.0570 0.0339  33   THR   B CA  
4320 C  C   . THR   B 33  ? 0.2142 0.1358 0.1762 -0.0367 -0.0601 0.0182  33   THR   B C   
4321 O  O   . THR   B 33  ? 0.2356 0.1393 0.1897 -0.0509 -0.0673 0.0222  33   THR   B O   
4322 C  CB  . THR   B 33  ? 0.2211 0.1556 0.1862 -0.0242 -0.0615 0.0367  33   THR   B CB  
4323 O  OG1 . THR   B 33  ? 0.2124 0.1615 0.1776 -0.0215 -0.0587 0.0393  33   THR   B OG1 
4324 C  CG2 . THR   B 33  ? 0.2450 0.1606 0.2115 -0.0123 -0.0551 0.0285  33   THR   B CG2 
4332 N  N   . VAL   B 34  ? 0.1975 0.1349 0.1644 -0.0373 -0.0502 0.0177  34   VAL   B N   
4333 C  CA  . VAL   B 34  ? 0.1836 0.1316 0.1558 -0.0257 -0.0497 0.0076  34   VAL   B CA  
4334 C  C   . VAL   B 34  ? 0.1664 0.1270 0.1249 -0.0277 -0.0279 0.0027  34   VAL   B C   
4335 O  O   . VAL   B 34  ? 0.1836 0.1334 0.1454 -0.0281 -0.0387 0.0076  34   VAL   B O   
4336 C  CB  . VAL   B 34  ? 0.1872 0.1399 0.1916 -0.0082 -0.0404 0.0062  34   VAL   B CB  
4337 C  CG1 . VAL   B 34  ? 0.1825 0.1598 0.1950 -0.0106 -0.0170 0.0020  34   VAL   B CG1 
4338 C  CG2 . VAL   B 34  ? 0.1899 0.1475 0.2090 -0.0083 -0.0401 0.0051  34   VAL   B CG2 
4348 N  N   . VAL   B 35  ? 0.1616 0.1259 0.1256 -0.0264 -0.0203 0.0079  35   VAL   B N   
4349 C  CA  . VAL   B 35  ? 0.1515 0.1228 0.1306 -0.0216 -0.0115 0.0107  35   VAL   B CA  
4350 C  C   . VAL   B 35  ? 0.1401 0.1187 0.1384 -0.0175 -0.0132 0.0096  35   VAL   B C   
4351 O  O   . VAL   B 35  ? 0.1468 0.1239 0.1362 -0.0218 -0.0053 -0.0006 35   VAL   B O   
4352 C  CB  . VAL   B 35  ? 0.1467 0.1426 0.1461 -0.0219 -0.0037 0.0058  35   VAL   B CB  
4353 C  CG1 . VAL   B 35  ? 0.1436 0.1542 0.1637 -0.0268 -0.0076 0.0112  35   VAL   B CG1 
4354 C  CG2 . VAL   B 35  ? 0.1557 0.1453 0.1712 -0.0139 -0.0124 0.0035  35   VAL   B CG2 
4364 N  N   . VAL   B 36  ? 0.1410 0.1178 0.1360 -0.0172 -0.0180 0.0102  36   VAL   B N   
4365 C  CA  . VAL   B 36  ? 0.1350 0.1185 0.1372 -0.0157 -0.0106 0.0088  36   VAL   B CA  
4366 C  C   . VAL   B 36  ? 0.1338 0.1196 0.1307 -0.0137 -0.0121 0.0054  36   VAL   B C   
4367 O  O   . VAL   B 36  ? 0.1419 0.1278 0.1461 -0.0146 -0.0055 -0.0042 36   VAL   B O   
4368 C  CB  . VAL   B 36  ? 0.1354 0.1233 0.1504 -0.0185 -0.0066 0.0055  36   VAL   B CB  
4369 C  CG1 . VAL   B 36  ? 0.1332 0.1327 0.1693 -0.0205 -0.0150 0.0134  36   VAL   B CG1 
4370 C  CG2 . VAL   B 36  ? 0.1398 0.1295 0.1583 -0.0143 -0.0145 0.0132  36   VAL   B CG2 
4380 N  N   . ASN   B 37  ? 0.1366 0.1234 0.1317 -0.0038 -0.0114 0.0087  37   ASN   B N   
4381 C  CA  . ASN   B 37  ? 0.1370 0.1291 0.1377 -0.0010 -0.0188 0.0071  37   ASN   B CA  
4382 C  C   . ASN   B 37  ? 0.1285 0.1294 0.1363 0.0002  -0.0184 0.0055  37   ASN   B C   
4383 O  O   . ASN   B 37  ? 0.1427 0.1323 0.1437 -0.0031 -0.0040 0.0060  37   ASN   B O   
4384 C  CB  . ASN   B 37  ? 0.1343 0.1262 0.1381 -0.0024 -0.0185 0.0053  37   ASN   B CB  
4385 C  CG  . ASN   B 37  ? 0.1357 0.1291 0.1396 -0.0009 -0.0117 -0.0008 37   ASN   B CG  
4386 O  OD1 . ASN   B 37  ? 0.1467 0.1368 0.1543 0.0068  -0.0181 0.0049  37   ASN   B OD1 
4387 N  ND2 . ASN   B 37  ? 0.1459 0.1233 0.1443 -0.0005 -0.0139 0.0057  37   ASN   B ND2 
4394 N  N   . ALA   B 38  ? 0.1423 0.1276 0.1435 0.0074  -0.0039 0.0012  38   ALA   B N   
4395 C  CA  . ALA   B 38  ? 0.1478 0.1249 0.1506 -0.0010 0.0044  0.0104  38   ALA   B CA  
4396 C  C   . ALA   B 38  ? 0.1424 0.1229 0.1592 -0.0054 0.0066  0.0067  38   ALA   B C   
4397 O  O   . ALA   B 38  ? 0.1566 0.1365 0.1653 0.0048  -0.0036 0.0093  38   ALA   B O   
4398 C  CB  . ALA   B 38  ? 0.1719 0.1398 0.1656 -0.0135 0.0097  0.0157  38   ALA   B CB  
4404 N  N   . ALA   B 39  ? 0.1432 0.1291 0.1420 0.0046  -0.0037 0.0024  39   ALA   B N   
4405 C  CA  . ALA   B 39  ? 0.1518 0.1331 0.1419 0.0020  -0.0061 0.0053  39   ALA   B CA  
4406 C  C   . ALA   B 39  ? 0.1566 0.1400 0.1280 0.0073  -0.0004 0.0037  39   ALA   B C   
4407 O  O   . ALA   B 39  ? 0.1600 0.1494 0.1526 -0.0036 0.0001  0.0130  39   ALA   B O   
4408 C  CB  . ALA   B 39  ? 0.1533 0.1397 0.1619 -0.0120 -0.0030 0.0028  39   ALA   B CB  
4414 N  N   . ASN   B 40  ? 0.1641 0.1631 0.1426 -0.0088 0.0000  -0.0052 40   ASN   B N   
4415 C  CA  . ASN   B 40  ? 0.1679 0.1710 0.1514 0.0006  -0.0048 -0.0024 40   ASN   B CA  
4416 C  C   . ASN   B 40  ? 0.1715 0.1687 0.1369 0.0050  -0.0128 0.0024  40   ASN   B C   
4417 O  O   . ASN   B 40  ? 0.1680 0.1600 0.1467 0.0024  -0.0179 0.0066  40   ASN   B O   
4418 C  CB  . ASN   B 40  ? 0.1804 0.1718 0.1718 0.0107  -0.0131 0.0094  40   ASN   B CB  
4419 C  CG  . ASN   B 40  ? 0.1834 0.1742 0.2005 0.0038  -0.0232 0.0220  40   ASN   B CG  
4420 O  OD1 . ASN   B 40  ? 0.1796 0.1699 0.2733 -0.0034 -0.0332 0.0299  40   ASN   B OD1 
4421 N  ND2 . ASN   B 40  ? 0.1829 0.1736 0.2002 0.0051  -0.0165 0.0167  40   ASN   B ND2 
4428 N  N   . VAL   B 41  ? 0.1807 0.1737 0.1386 0.0111  0.0017  0.0023  41   VAL   B N   
4429 C  CA  . VAL   B 41  ? 0.1903 0.1867 0.1562 0.0033  0.0020  -0.0094 41   VAL   B CA  
4430 C  C   . VAL   B 41  ? 0.1850 0.1855 0.1435 0.0118  -0.0066 -0.0116 41   VAL   B C   
4431 O  O   . VAL   B 41  ? 0.1840 0.1785 0.1585 0.0072  -0.0097 -0.0148 41   VAL   B O   
4432 C  CB  . VAL   B 41  ? 0.1985 0.2013 0.1730 -0.0143 0.0210  -0.0189 41   VAL   B CB  
4433 C  CG1 . VAL   B 41  ? 0.1979 0.2052 0.2057 -0.0122 0.0353  -0.0221 41   VAL   B CG1 
4434 C  CG2 . VAL   B 41  ? 0.2103 0.2233 0.1710 -0.0191 0.0218  -0.0141 41   VAL   B CG2 
4444 N  N   . TYR   B 42  ? 0.1881 0.1862 0.1521 0.0140  -0.0156 0.0019  42   TYR   B N   
4445 C  CA  . TYR   B 42  ? 0.1969 0.1892 0.1510 0.0155  -0.0216 -0.0165 42   TYR   B CA  
4446 C  C   . TYR   B 42  ? 0.1758 0.1683 0.1605 0.0201  -0.0178 -0.0195 42   TYR   B C   
4447 O  O   . TYR   B 42  ? 0.1777 0.1772 0.1932 0.0090  -0.0322 -0.0214 42   TYR   B O   
4448 C  CB  . TYR   B 42  ? 0.2202 0.2183 0.1663 0.0118  -0.0198 -0.0033 42   TYR   B CB  
4449 C  CG  . TYR   B 42  ? 0.2257 0.2361 0.1559 0.0018  -0.0210 0.0146  42   TYR   B CG  
4450 C  CD1 . TYR   B 42  ? 0.2188 0.2356 0.1397 -0.0036 -0.0089 0.0158  42   TYR   B CD1 
4451 C  CD2 . TYR   B 42  ? 0.2408 0.2481 0.1988 0.0005  -0.0130 0.0214  42   TYR   B CD2 
4452 C  CE1 . TYR   B 42  ? 0.2343 0.2501 0.1523 0.0002  -0.0090 0.0056  42   TYR   B CE1 
4453 C  CE2 . TYR   B 42  ? 0.2475 0.2583 0.1964 -0.0005 0.0078  0.0313  42   TYR   B CE2 
4454 C  CZ  . TYR   B 42  ? 0.2557 0.2687 0.1875 0.0128  0.0081  0.0136  42   TYR   B CZ  
4455 O  OH  . TYR   B 42  ? 0.2923 0.2984 0.2355 0.0272  0.0161  0.0187  42   TYR   B OH  
4465 N  N   . LEU   B 43  ? 0.1655 0.1520 0.1486 0.0077  -0.0129 -0.0137 43   LEU   B N   
4466 C  CA  . LEU   B 43  ? 0.1638 0.1561 0.1319 0.0018  -0.0079 0.0014  43   LEU   B CA  
4467 C  C   . LEU   B 43  ? 0.1690 0.1590 0.1459 -0.0026 -0.0108 -0.0047 43   LEU   B C   
4468 O  O   . LEU   B 43  ? 0.1663 0.1609 0.1786 -0.0017 -0.0162 0.0056  43   LEU   B O   
4469 C  CB  . LEU   B 43  ? 0.1609 0.1518 0.1551 -0.0029 -0.0209 -0.0068 43   LEU   B CB  
4470 C  CG  . LEU   B 43  ? 0.1674 0.1483 0.1671 -0.0033 -0.0258 -0.0038 43   LEU   B CG  
4471 C  CD1 . LEU   B 43  ? 0.1774 0.1547 0.1975 -0.0049 -0.0431 -0.0029 43   LEU   B CD1 
4472 C  CD2 . LEU   B 43  ? 0.1691 0.1447 0.1777 -0.0074 -0.0337 -0.0054 43   LEU   B CD2 
4484 N  N   . LYS   B 44  ? 0.1644 0.1539 0.1569 0.0010  -0.0094 -0.0079 44   LYS   B N   
4485 C  CA  . LYS   B 44  ? 0.1806 0.1665 0.1525 0.0045  -0.0136 0.0058  44   LYS   B CA  
4486 C  C   . LYS   B 44  ? 0.1702 0.1617 0.1501 0.0095  -0.0137 0.0002  44   LYS   B C   
4487 O  O   . LYS   B 44  ? 0.1881 0.1564 0.1834 -0.0009 -0.0069 0.0059  44   LYS   B O   
4488 C  CB  . LYS   B 44  ? 0.2071 0.1922 0.1737 0.0113  -0.0251 0.0017  44   LYS   B CB  
4489 C  CG  . LYS   B 44  ? 0.2436 0.2196 0.2070 0.0114  -0.0525 0.0040  44   LYS   B CG  
4490 C  CD  . LYS   B 44  ? 0.2802 0.2421 0.2661 -0.0029 -0.0672 0.0052  44   LYS   B CD  
4491 C  CE  . LYS   B 44  ? 0.3143 0.2680 0.3166 -0.0116 -0.0684 0.0142  44   LYS   B CE  
4492 N  NZ  . LYS   B 44  ? 0.3275 0.2789 0.3474 -0.0090 -0.0790 0.0222  44   LYS   B NZ  
4506 N  N   . HIS   B 45  ? 0.1623 0.1642 0.1456 0.0051  -0.0088 0.0083  45   HIS   B N   
4507 C  CA  . HIS   B 45  ? 0.1694 0.1617 0.1511 0.0079  -0.0108 -0.0045 45   HIS   B CA  
4508 C  C   . HIS   B 45  ? 0.1926 0.1821 0.1888 0.0148  -0.0194 -0.0040 45   HIS   B C   
4509 O  O   . HIS   B 45  ? 0.2017 0.2124 0.2415 0.0408  0.0120  0.0088  45   HIS   B O   
4510 C  CB  . HIS   B 45  ? 0.1627 0.1596 0.1457 -0.0017 -0.0078 -0.0053 45   HIS   B CB  
4511 C  CG  . HIS   B 45  ? 0.1571 0.1548 0.1475 -0.0095 -0.0055 0.0026  45   HIS   B CG  
4512 N  ND1 . HIS   B 45  ? 0.1600 0.1521 0.1669 -0.0020 -0.0152 -0.0085 45   HIS   B ND1 
4513 C  CD2 . HIS   B 45  ? 0.1681 0.1601 0.1577 -0.0132 -0.0153 0.0048  45   HIS   B CD2 
4514 C  CE1 . HIS   B 45  ? 0.1710 0.1422 0.1529 -0.0053 -0.0200 -0.0056 45   HIS   B CE1 
4515 N  NE2 . HIS   B 45  ? 0.1786 0.1547 0.1588 -0.0038 -0.0224 0.0029  45   HIS   B NE2 
4523 N  N   A GLY   B 46  ? 0.2024 0.1843 0.2191 0.0183  -0.0373 0.0032  46   GLY   B N   
4524 N  N   B GLY   B 46  ? 0.2044 0.1897 0.2116 0.0181  -0.0362 0.0087  46   GLY   B N   
4525 C  CA  A GLY   B 46  ? 0.2130 0.1964 0.2599 0.0170  -0.0424 0.0043  46   GLY   B CA  
4526 C  CA  B GLY   B 46  ? 0.2163 0.2048 0.2426 0.0152  -0.0433 0.0149  46   GLY   B CA  
4527 C  C   A GLY   B 46  ? 0.2131 0.2078 0.2995 0.0250  -0.0386 -0.0000 46   GLY   B C   
4528 C  C   B GLY   B 46  ? 0.2190 0.2181 0.2761 0.0205  -0.0414 0.0172  46   GLY   B C   
4529 O  O   A GLY   B 46  ? 0.2162 0.2141 0.3654 0.0327  -0.0214 -0.0226 46   GLY   B O   
4530 O  O   B GLY   B 46  ? 0.2278 0.2340 0.3104 0.0215  -0.0346 0.0218  46   GLY   B O   
4537 N  N   . GLY   B 47  ? 0.2151 0.2165 0.2814 0.0078  -0.0266 0.0007  47   GLY   B N   
4538 C  CA  . GLY   B 47  ? 0.2007 0.1853 0.2431 -0.0010 -0.0225 0.0039  47   GLY   B CA  
4539 C  C   . GLY   B 47  ? 0.1745 0.1631 0.2019 -0.0017 -0.0059 0.0101  47   GLY   B C   
4540 O  O   . GLY   B 47  ? 0.1883 0.1442 0.2091 -0.0008 -0.0129 0.0099  47   GLY   B O   
4545 N  N   . GLY   B 48  ? 0.1523 0.1552 0.1937 0.0007  -0.0158 0.0181  48   GLY   B N   
4546 C  CA  . GLY   B 48  ? 0.1537 0.1534 0.1961 -0.0013 -0.0077 0.0122  48   GLY   B CA  
4547 C  C   . GLY   B 48  ? 0.1518 0.1444 0.1775 -0.0026 -0.0017 0.0106  48   GLY   B C   
4548 O  O   . GLY   B 48  ? 0.1484 0.1439 0.1984 0.0010  -0.0098 0.0055  48   GLY   B O   
4552 N  N   . VAL   B 49  ? 0.1542 0.1487 0.1653 0.0109  -0.0004 0.0111  49   VAL   B N   
4553 C  CA  . VAL   B 49  ? 0.1579 0.1560 0.1686 0.0069  -0.0155 -0.0001 49   VAL   B CA  
4554 C  C   . VAL   B 49  ? 0.1492 0.1491 0.1561 0.0106  -0.0072 0.0085  49   VAL   B C   
4555 O  O   . VAL   B 49  ? 0.1601 0.1505 0.1636 0.0059  0.0011  0.0130  49   VAL   B O   
4556 C  CB  . VAL   B 49  ? 0.1597 0.1661 0.1964 0.0027  -0.0304 0.0037  49   VAL   B CB  
4557 C  CG1 . VAL   B 49  ? 0.1589 0.1731 0.1979 0.0121  -0.0395 0.0008  49   VAL   B CG1 
4558 C  CG2 . VAL   B 49  ? 0.1714 0.1819 0.2275 -0.0084 -0.0399 0.0047  49   VAL   B CG2 
4568 N  N   . ALA   B 50  ? 0.1454 0.1402 0.1559 0.0052  -0.0093 0.0102  50   ALA   B N   
4569 C  CA  . ALA   B 50  ? 0.1410 0.1331 0.1580 0.0089  -0.0076 0.0094  50   ALA   B CA  
4570 C  C   . ALA   B 50  ? 0.1499 0.1421 0.1556 0.0024  -0.0051 0.0105  50   ALA   B C   
4571 O  O   . ALA   B 50  ? 0.1477 0.1424 0.1536 0.0043  -0.0050 0.0082  50   ALA   B O   
4572 C  CB  . ALA   B 50  ? 0.1514 0.1293 0.1651 -0.0018 -0.0008 0.0155  50   ALA   B CB  
4578 N  N   . GLY   B 51  ? 0.1437 0.1515 0.1795 0.0136  -0.0179 0.0128  51   GLY   B N   
4579 C  CA  . GLY   B 51  ? 0.1505 0.1570 0.1912 0.0204  -0.0149 0.0123  51   GLY   B CA  
4580 C  C   . GLY   B 51  ? 0.1480 0.1523 0.1931 0.0208  -0.0100 0.0143  51   GLY   B C   
4581 O  O   . GLY   B 51  ? 0.1510 0.1588 0.2098 0.0063  -0.0087 0.0061  51   GLY   B O   
4585 N  N   . ALA   B 52  ? 0.1489 0.1482 0.1847 0.0155  -0.0052 0.0179  52   ALA   B N   
4586 C  CA  . ALA   B 52  ? 0.1551 0.1546 0.1785 0.0140  0.0054  0.0052  52   ALA   B CA  
4587 C  C   . ALA   B 52  ? 0.1501 0.1529 0.1696 0.0089  0.0021  0.0066  52   ALA   B C   
4588 O  O   . ALA   B 52  ? 0.1528 0.1557 0.1929 0.0109  0.0074  0.0057  52   ALA   B O   
4589 C  CB  . ALA   B 52  ? 0.1692 0.1596 0.1881 0.0017  0.0113  -0.0021 52   ALA   B CB  
4595 N  N   . LEU   B 53  ? 0.1458 0.1481 0.1487 0.0155  0.0041  0.0054  53   LEU   B N   
4596 C  CA  . LEU   B 53  ? 0.1425 0.1606 0.1603 0.0140  -0.0051 0.0052  53   LEU   B CA  
4597 C  C   . LEU   B 53  ? 0.1510 0.1528 0.1572 0.0085  0.0040  0.0113  53   LEU   B C   
4598 O  O   . LEU   B 53  ? 0.1546 0.1631 0.1622 -0.0010 0.0027  0.0173  53   LEU   B O   
4599 C  CB  . LEU   B 53  ? 0.1431 0.1641 0.1826 0.0089  -0.0008 0.0179  53   LEU   B CB  
4600 C  CG  . LEU   B 53  ? 0.1408 0.1760 0.1869 0.0002  -0.0006 0.0264  53   LEU   B CG  
4601 C  CD1 . LEU   B 53  ? 0.1501 0.1940 0.1928 0.0123  -0.0051 0.0045  53   LEU   B CD1 
4602 C  CD2 . LEU   B 53  ? 0.1596 0.2059 0.2159 -0.0068 -0.0155 -0.0089 53   LEU   B CD2 
4614 N  N   . ASN   B 54  ? 0.1471 0.1401 0.1574 0.0015  -0.0004 0.0154  54   ASN   B N   
4615 C  CA  . ASN   B 54  ? 0.1472 0.1566 0.1644 -0.0014 -0.0034 0.0043  54   ASN   B CA  
4616 C  C   . ASN   B 54  ? 0.1484 0.1587 0.1849 0.0013  0.0028  0.0074  54   ASN   B C   
4617 O  O   . ASN   B 54  ? 0.1436 0.1671 0.1989 -0.0033 0.0017  0.0119  54   ASN   B O   
4618 C  CB  . ASN   B 54  ? 0.1511 0.1690 0.1735 -0.0029 0.0043  0.0083  54   ASN   B CB  
4619 C  CG  . ASN   B 54  ? 0.1485 0.1794 0.1788 -0.0038 -0.0063 0.0063  54   ASN   B CG  
4620 O  OD1 . ASN   B 54  ? 0.1465 0.1735 0.1912 -0.0058 -0.0049 -0.0098 54   ASN   B OD1 
4621 N  ND2 . ASN   B 54  ? 0.1609 0.1988 0.2120 -0.0035 -0.0293 0.0216  54   ASN   B ND2 
4628 N  N   . LYS   B 55  ? 0.1468 0.1615 0.2056 0.0155  0.0064  0.0091  55   LYS   B N   
4629 C  CA  . LYS   B 55  ? 0.1579 0.1769 0.2282 0.0190  0.0038  0.0081  55   LYS   B CA  
4630 C  C   . LYS   B 55  ? 0.1496 0.1736 0.2191 0.0101  0.0040  0.0015  55   LYS   B C   
4631 O  O   . LYS   B 55  ? 0.1476 0.1927 0.2249 0.0111  0.0056  -0.0076 55   LYS   B O   
4632 C  CB  . LYS   B 55  ? 0.1683 0.1833 0.2699 0.0261  0.0222  0.0092  55   LYS   B CB  
4633 C  CG  . LYS   B 55  ? 0.2087 0.2149 0.3548 0.0280  0.0367  0.0174  55   LYS   B CG  
4634 C  CD  . LYS   B 55  ? 0.2416 0.2398 0.4204 0.0412  0.0522  0.0241  55   LYS   B CD  
4635 C  CE  . LYS   B 55  ? 0.2661 0.2607 0.4793 0.0423  0.0648  0.0328  55   LYS   B CE  
4636 N  NZ  . LYS   B 55  ? 0.2723 0.2777 0.5101 0.0431  0.0568  0.0382  55   LYS   B NZ  
4650 N  N   . ALA   B 56  ? 0.1478 0.1768 0.1953 0.0106  -0.0042 -0.0027 56   ALA   B N   
4651 C  CA  . ALA   B 56  ? 0.1618 0.1903 0.1917 0.0052  0.0018  0.0004  56   ALA   B CA  
4652 C  C   . ALA   B 56  ? 0.1620 0.1882 0.1821 0.0066  0.0154  0.0115  56   ALA   B C   
4653 O  O   . ALA   B 56  ? 0.1767 0.2036 0.2074 0.0063  0.0344  0.0127  56   ALA   B O   
4654 C  CB  . ALA   B 56  ? 0.1758 0.2128 0.1971 -0.0089 -0.0009 0.0007  56   ALA   B CB  
4660 N  N   . THR   B 57  ? 0.1540 0.1793 0.1938 0.0073  0.0170  0.0134  57   THR   B N   
4661 C  CA  . THR   B 57  ? 0.1587 0.1806 0.1926 -0.0001 0.0264  0.0162  57   THR   B CA  
4662 C  C   . THR   B 57  ? 0.1591 0.1916 0.2101 0.0002  0.0229  0.0152  57   THR   B C   
4663 O  O   . THR   B 57  ? 0.1671 0.1914 0.2224 -0.0188 0.0129  0.0119  57   THR   B O   
4664 C  CB  . THR   B 57  ? 0.1661 0.1706 0.1819 0.0037  0.0177  0.0156  57   THR   B CB  
4665 O  OG1 . THR   B 57  ? 0.1607 0.1572 0.1953 -0.0030 0.0159  0.0116  57   THR   B OG1 
4666 C  CG2 . THR   B 57  ? 0.1685 0.1639 0.1834 0.0007  0.0142  0.0062  57   THR   B CG2 
4674 N  N   . ASN   B 58  ? 0.1496 0.2143 0.2303 -0.0089 0.0047  -0.0104 58   ASN   B N   
4675 C  CA  . ASN   B 58  ? 0.1708 0.2560 0.2797 -0.0193 0.0307  0.0024  58   ASN   B CA  
4676 C  C   . ASN   B 58  ? 0.1503 0.2326 0.2359 -0.0158 -0.0011 -0.0068 58   ASN   B C   
4677 O  O   . ASN   B 58  ? 0.1615 0.2390 0.2412 -0.0175 -0.0014 -0.0145 58   ASN   B O   
4678 C  CB  . ASN   B 58  ? 0.2491 0.3197 0.4015 -0.0302 0.0734  0.0139  58   ASN   B CB  
4679 C  CG  . ASN   B 58  ? 0.3404 0.3765 0.5440 -0.0313 0.0954  0.0418  58   ASN   B CG  
4680 O  OD1 . ASN   B 58  ? 0.3618 0.4017 0.5967 -0.0328 0.0975  0.0514  58   ASN   B OD1 
4681 N  ND2 . ASN   B 58  ? 0.4338 0.4338 0.5943 -0.0341 0.1039  0.0492  58   ASN   B ND2 
4688 N  N   . ASN   B 59  ? 0.1477 0.2147 0.2064 -0.0099 0.0039  0.0110  59   ASN   B N   
4689 C  CA  . ASN   B 59  ? 0.1506 0.2103 0.2049 -0.0131 -0.0095 0.0244  59   ASN   B CA  
4690 C  C   . ASN   B 59  ? 0.1435 0.2004 0.1986 -0.0158 -0.0096 0.0071  59   ASN   B C   
4691 O  O   . ASN   B 59  ? 0.1488 0.1965 0.2012 -0.0123 -0.0084 0.0015  59   ASN   B O   
4692 C  CB  . ASN   B 59  ? 0.1593 0.2262 0.2308 -0.0075 -0.0273 0.0204  59   ASN   B CB  
4693 C  CG  . ASN   B 59  ? 0.1702 0.2444 0.2459 -0.0051 -0.0361 0.0214  59   ASN   B CG  
4694 O  OD1 . ASN   B 59  ? 0.1727 0.2472 0.2420 -0.0029 -0.0246 0.0314  59   ASN   B OD1 
4695 N  ND2 . ASN   B 59  ? 0.1782 0.2566 0.2580 -0.0133 -0.0355 0.0188  59   ASN   B ND2 
4702 N  N   . ALA   B 60  ? 0.1468 0.1846 0.1980 -0.0123 0.0002  0.0064  60   ALA   B N   
4703 C  CA  . ALA   B 60  ? 0.1616 0.1731 0.2049 -0.0239 -0.0017 0.0103  60   ALA   B CA  
4704 C  C   . ALA   B 60  ? 0.1588 0.1626 0.1837 -0.0138 -0.0014 0.0138  60   ALA   B C   
4705 O  O   . ALA   B 60  ? 0.1618 0.1658 0.2012 -0.0181 -0.0016 -0.0038 60   ALA   B O   
4706 C  CB  . ALA   B 60  ? 0.1796 0.1740 0.2268 -0.0216 -0.0007 0.0100  60   ALA   B CB  
4712 N  N   . MET   B 61  ? 0.1486 0.1548 0.1750 -0.0116 0.0083  0.0117  61   MET   B N   
4713 C  CA  . MET   B 61  ? 0.1472 0.1540 0.1637 -0.0100 -0.0074 0.0022  61   MET   B CA  
4714 C  C   . MET   B 61  ? 0.1580 0.1531 0.1658 -0.0144 -0.0086 0.0115  61   MET   B C   
4715 O  O   . MET   B 61  ? 0.1597 0.1488 0.1680 -0.0068 -0.0025 -0.0070 61   MET   B O   
4716 C  CB  . MET   B 61  ? 0.1423 0.1562 0.1703 -0.0039 -0.0081 0.0018  61   MET   B CB  
4717 C  CG  . MET   B 61  ? 0.1412 0.1559 0.1784 -0.0036 -0.0093 0.0087  61   MET   B CG  
4718 S  SD  . MET   B 61  ? 0.1463 0.1526 0.1888 -0.0053 -0.0050 -0.0046 61   MET   B SD  
4719 C  CE  . MET   B 61  ? 0.1540 0.1684 0.1974 -0.0014 -0.0044 -0.0133 61   MET   B CE  
4729 N  N   . GLN   B 62  ? 0.1502 0.1572 0.1580 -0.0080 -0.0166 0.0159  62   GLN   B N   
4730 C  CA  . GLN   B 62  ? 0.1521 0.1628 0.1689 -0.0040 -0.0216 0.0064  62   GLN   B CA  
4731 C  C   . GLN   B 62  ? 0.1551 0.1678 0.1764 -0.0059 -0.0208 0.0023  62   GLN   B C   
4732 O  O   . GLN   B 62  ? 0.1681 0.1688 0.1756 -0.0062 -0.0255 -0.0116 62   GLN   B O   
4733 C  CB  . GLN   B 62  ? 0.1588 0.1668 0.1729 -0.0034 -0.0187 0.0066  62   GLN   B CB  
4734 C  CG  . GLN   B 62  ? 0.1548 0.1695 0.1742 -0.0034 -0.0252 -0.0043 62   GLN   B CG  
4735 C  CD  . GLN   B 62  ? 0.1550 0.1689 0.1704 0.0018  -0.0244 0.0075  62   GLN   B CD  
4736 O  OE1 . GLN   B 62  ? 0.1636 0.1642 0.1778 0.0028  -0.0276 -0.0081 62   GLN   B OE1 
4737 N  NE2 . GLN   B 62  ? 0.1560 0.1731 0.1788 -0.0055 -0.0200 -0.0067 62   GLN   B NE2 
4746 N  N   . VAL   B 63  ? 0.1537 0.1663 0.1989 -0.0125 -0.0185 -0.0079 63   VAL   B N   
4747 C  CA  . VAL   B 63  ? 0.1691 0.1745 0.2190 -0.0147 -0.0282 0.0059  63   VAL   B CA  
4748 C  C   . VAL   B 63  ? 0.1641 0.1612 0.1937 -0.0169 -0.0265 -0.0067 63   VAL   B C   
4749 O  O   . VAL   B 63  ? 0.1742 0.1624 0.2233 -0.0126 -0.0408 -0.0118 63   VAL   B O   
4750 C  CB  . VAL   B 63  ? 0.1681 0.1873 0.2569 -0.0194 -0.0258 0.0003  63   VAL   B CB  
4751 C  CG1 . VAL   B 63  ? 0.1708 0.1929 0.2711 -0.0355 -0.0201 -0.0006 63   VAL   B CG1 
4752 C  CG2 . VAL   B 63  ? 0.1618 0.2063 0.2629 -0.0158 -0.0334 -0.0076 63   VAL   B CG2 
4762 N  N   . GLU   B 64  ? 0.1644 0.1549 0.1912 -0.0145 -0.0258 -0.0039 64   GLU   B N   
4763 C  CA  . GLU   B 64  ? 0.1640 0.1489 0.1838 -0.0161 -0.0336 -0.0063 64   GLU   B CA  
4764 C  C   . GLU   B 64  ? 0.1614 0.1493 0.1760 -0.0114 -0.0303 -0.0152 64   GLU   B C   
4765 O  O   . GLU   B 64  ? 0.1706 0.1598 0.1847 -0.0153 -0.0304 -0.0140 64   GLU   B O   
4766 C  CB  . GLU   B 64  ? 0.1630 0.1579 0.1766 -0.0186 -0.0233 0.0005  64   GLU   B CB  
4767 C  CG  . GLU   B 64  ? 0.1703 0.1562 0.1724 -0.0288 -0.0253 -0.0122 64   GLU   B CG  
4768 C  CD  . GLU   B 64  ? 0.1708 0.1737 0.1919 -0.0352 -0.0273 -0.0076 64   GLU   B CD  
4769 O  OE1 . GLU   B 64  ? 0.1742 0.1924 0.2014 -0.0382 -0.0277 -0.0326 64   GLU   B OE1 
4770 O  OE2 . GLU   B 64  ? 0.1920 0.1822 0.1965 -0.0361 -0.0433 -0.0135 64   GLU   B OE2 
4777 N  N   . SER   B 65  ? 0.1584 0.1421 0.1661 -0.0091 -0.0165 -0.0100 65   SER   B N   
4778 C  CA  . SER   B 65  ? 0.1561 0.1422 0.1812 -0.0069 -0.0111 -0.0117 65   SER   B CA  
4779 C  C   . SER   B 65  ? 0.1591 0.1494 0.1747 -0.0079 -0.0222 -0.0152 65   SER   B C   
4780 O  O   . SER   B 65  ? 0.1660 0.1566 0.1823 -0.0082 -0.0181 -0.0226 65   SER   B O   
4781 C  CB  . SER   B 65  ? 0.1609 0.1497 0.1724 -0.0124 -0.0124 -0.0091 65   SER   B CB  
4782 O  OG  . SER   B 65  ? 0.1662 0.1540 0.1728 -0.0123 -0.0162 -0.0222 65   SER   B OG  
4788 N  N   . ASP   B 66  ? 0.1707 0.1567 0.1676 -0.0043 -0.0324 -0.0215 66   ASP   B N   
4789 C  CA  . ASP   B 66  ? 0.1765 0.1621 0.1617 -0.0024 -0.0336 -0.0180 66   ASP   B CA  
4790 C  C   . ASP   B 66  ? 0.1795 0.1686 0.1684 -0.0109 -0.0217 -0.0165 66   ASP   B C   
4791 O  O   . ASP   B 66  ? 0.1788 0.1740 0.1736 0.0014  -0.0292 -0.0212 66   ASP   B O   
4792 C  CB  . ASP   B 66  ? 0.1893 0.1774 0.1925 -0.0006 -0.0393 -0.0133 66   ASP   B CB  
4793 C  CG  . ASP   B 66  ? 0.2182 0.1921 0.2131 0.0095  -0.0553 0.0013  66   ASP   B CG  
4794 O  OD1 . ASP   B 66  ? 0.2453 0.1865 0.2162 0.0050  -0.0518 0.0046  66   ASP   B OD1 
4795 O  OD2 . ASP   B 66  ? 0.2372 0.2148 0.2765 0.0296  -0.0592 -0.0069 66   ASP   B OD2 
4800 N  N   . ASP   B 67  ? 0.1714 0.1601 0.1679 -0.0132 -0.0268 -0.0167 67   ASP   B N   
4801 C  CA  . ASP   B 67  ? 0.1912 0.1603 0.1712 -0.0145 -0.0246 -0.0114 67   ASP   B CA  
4802 C  C   . ASP   B 67  ? 0.1842 0.1564 0.1840 -0.0025 -0.0269 -0.0127 67   ASP   B C   
4803 O  O   . ASP   B 67  ? 0.1923 0.1666 0.1975 0.0001  -0.0207 -0.0235 67   ASP   B O   
4804 C  CB  . ASP   B 67  ? 0.2134 0.1681 0.1928 -0.0183 -0.0390 -0.0024 67   ASP   B CB  
4805 C  CG  . ASP   B 67  ? 0.2480 0.1780 0.1935 -0.0136 -0.0686 -0.0123 67   ASP   B CG  
4806 O  OD1 . ASP   B 67  ? 0.2680 0.1883 0.2097 -0.0128 -0.0685 -0.0140 67   ASP   B OD1 
4807 O  OD2 . ASP   B 67  ? 0.2641 0.1818 0.2142 0.0029  -0.0791 -0.0119 67   ASP   B OD2 
4812 N  N   . TYR   B 68  ? 0.1806 0.1557 0.1827 -0.0053 -0.0397 -0.0201 68   TYR   B N   
4813 C  CA  . TYR   B 68  ? 0.1752 0.1725 0.1961 0.0009  -0.0411 -0.0310 68   TYR   B CA  
4814 C  C   . TYR   B 68  ? 0.1697 0.1647 0.1904 -0.0015 -0.0331 -0.0353 68   TYR   B C   
4815 O  O   . TYR   B 68  ? 0.1768 0.1815 0.2070 0.0020  -0.0345 -0.0515 68   TYR   B O   
4816 C  CB  . TYR   B 68  ? 0.1813 0.1961 0.2029 0.0111  -0.0417 -0.0398 68   TYR   B CB  
4817 C  CG  . TYR   B 68  ? 0.1919 0.2190 0.2169 0.0150  -0.0324 -0.0618 68   TYR   B CG  
4818 C  CD1 . TYR   B 68  ? 0.1936 0.2210 0.2346 -0.0033 -0.0350 -0.0806 68   TYR   B CD1 
4819 C  CD2 . TYR   B 68  ? 0.1957 0.2377 0.2276 0.0153  -0.0488 -0.0617 68   TYR   B CD2 
4820 C  CE1 . TYR   B 68  ? 0.1986 0.2359 0.2624 0.0018  -0.0259 -0.0768 68   TYR   B CE1 
4821 C  CE2 . TYR   B 68  ? 0.1954 0.2433 0.2497 0.0162  -0.0352 -0.0714 68   TYR   B CE2 
4822 C  CZ  . TYR   B 68  ? 0.1897 0.2426 0.2664 0.0027  -0.0383 -0.0791 68   TYR   B CZ  
4823 O  OH  . TYR   B 68  ? 0.1850 0.2569 0.2936 0.0059  -0.0331 -0.0567 68   TYR   B OH  
4833 N  N   . ILE   B 69  ? 0.1704 0.1576 0.1980 0.0003  -0.0290 -0.0319 69   ILE   B N   
4834 C  CA  . ILE   B 69  ? 0.1758 0.1678 0.1974 -0.0059 -0.0306 -0.0397 69   ILE   B CA  
4835 C  C   . ILE   B 69  ? 0.1714 0.1650 0.1911 0.0043  -0.0398 -0.0279 69   ILE   B C   
4836 O  O   . ILE   B 69  ? 0.1815 0.1798 0.1856 0.0044  -0.0272 -0.0240 69   ILE   B O   
4837 C  CB  . ILE   B 69  ? 0.1838 0.1753 0.2227 -0.0065 -0.0105 -0.0278 69   ILE   B CB  
4838 C  CG1 . ILE   B 69  ? 0.1864 0.1802 0.2308 -0.0067 0.0022  -0.0327 69   ILE   B CG1 
4839 C  CG2 . ILE   B 69  ? 0.2001 0.1855 0.2453 -0.0042 -0.0114 -0.0181 69   ILE   B CG2 
4840 C  CD1 . ILE   B 69  ? 0.1815 0.1837 0.2405 -0.0168 0.0029  -0.0405 69   ILE   B CD1 
4852 N  N   . ALA   B 70  ? 0.1715 0.1628 0.1898 0.0038  -0.0380 -0.0288 70   ALA   B N   
4853 C  CA  . ALA   B 70  ? 0.1766 0.1673 0.1710 -0.0003 -0.0381 -0.0237 70   ALA   B CA  
4854 C  C   . ALA   B 70  ? 0.1852 0.1710 0.1709 -0.0030 -0.0419 -0.0319 70   ALA   B C   
4855 O  O   . ALA   B 70  ? 0.1986 0.1734 0.1727 0.0027  -0.0400 -0.0369 70   ALA   B O   
4856 C  CB  . ALA   B 70  ? 0.1763 0.1892 0.1856 -0.0056 -0.0363 -0.0136 70   ALA   B CB  
4862 N  N   . THR   B 71  ? 0.1908 0.1728 0.1823 -0.0012 -0.0580 -0.0292 71   THR   B N   
4863 C  CA  . THR   B 71  ? 0.2081 0.1727 0.2113 0.0033  -0.0660 -0.0246 71   THR   B CA  
4864 C  C   . THR   B 71  ? 0.2041 0.1718 0.2401 0.0242  -0.0661 -0.0428 71   THR   B C   
4865 O  O   . THR   B 71  ? 0.2162 0.1815 0.2830 0.0228  -0.0649 -0.0604 71   THR   B O   
4866 C  CB  . THR   B 71  ? 0.2283 0.1991 0.2335 -0.0022 -0.0723 -0.0070 71   THR   B CB  
4867 O  OG1 . THR   B 71  ? 0.2443 0.2273 0.2675 -0.0198 -0.0662 0.0075  71   THR   B OG1 
4868 C  CG2 . THR   B 71  ? 0.2429 0.1944 0.2527 -0.0000 -0.0653 0.0080  71   THR   B CG2 
4876 N  N   . ASN   B 72  ? 0.1875 0.1759 0.2314 0.0112  -0.0602 -0.0632 72   ASN   B N   
4877 C  CA  . ASN   B 72  ? 0.1884 0.1896 0.2278 0.0218  -0.0447 -0.0690 72   ASN   B CA  
4878 C  C   . ASN   B 72  ? 0.1870 0.2020 0.2359 0.0056  -0.0233 -0.0643 72   ASN   B C   
4879 O  O   . ASN   B 72  ? 0.1906 0.2174 0.2630 0.0111  -0.0064 -0.0651 72   ASN   B O   
4880 C  CB  . ASN   B 72  ? 0.1958 0.2029 0.2360 0.0155  -0.0687 -0.0545 72   ASN   B CB  
4881 C  CG  . ASN   B 72  ? 0.2138 0.2202 0.2450 0.0249  -0.0686 -0.0312 72   ASN   B CG  
4882 O  OD1 . ASN   B 72  ? 0.2401 0.2425 0.2483 0.0105  -0.0500 -0.0387 72   ASN   B OD1 
4883 N  ND2 . ASN   B 72  ? 0.2276 0.2298 0.2806 0.0377  -0.0559 0.0004  72   ASN   B ND2 
4890 N  N   . GLY   B 73  ? 0.1906 0.2055 0.2196 -0.0091 -0.0307 -0.0585 73   GLY   B N   
4891 C  CA  . GLY   B 73  ? 0.1867 0.2101 0.1936 -0.0143 -0.0220 -0.0490 73   GLY   B CA  
4892 C  C   . GLY   B 73  ? 0.1778 0.2109 0.1493 -0.0044 -0.0203 -0.0446 73   GLY   B C   
4893 O  O   . GLY   B 73  ? 0.1758 0.2027 0.1657 0.0027  -0.0235 -0.0330 73   GLY   B O   
4897 N  N   . PRO   B 74  ? 0.1805 0.2166 0.1560 0.0009  -0.0252 -0.0395 74   PRO   B N   
4898 C  CA  . PRO   B 74  ? 0.1729 0.2169 0.1501 0.0081  -0.0255 -0.0274 74   PRO   B CA  
4899 C  C   . PRO   B 74  ? 0.1610 0.2041 0.1538 0.0008  -0.0157 -0.0199 74   PRO   B C   
4900 O  O   . PRO   B 74  ? 0.1674 0.2087 0.1946 0.0028  -0.0148 -0.0316 74   PRO   B O   
4901 C  CB  . PRO   B 74  ? 0.1908 0.2331 0.1572 0.0026  -0.0168 -0.0159 74   PRO   B CB  
4902 C  CG  . PRO   B 74  ? 0.2115 0.2462 0.1819 0.0052  -0.0105 -0.0163 74   PRO   B CG  
4903 C  CD  . PRO   B 74  ? 0.2062 0.2369 0.1692 0.0020  -0.0101 -0.0317 74   PRO   B CD  
4911 N  N   . LEU   B 75  ? 0.1584 0.1937 0.1396 0.0084  -0.0213 -0.0257 75   LEU   B N   
4912 C  CA  . LEU   B 75  ? 0.1638 0.1910 0.1438 0.0006  -0.0196 -0.0060 75   LEU   B CA  
4913 C  C   . LEU   B 75  ? 0.1734 0.1982 0.1461 0.0018  -0.0023 -0.0023 75   LEU   B C   
4914 O  O   . LEU   B 75  ? 0.1845 0.2097 0.1582 -0.0031 -0.0048 -0.0015 75   LEU   B O   
4915 C  CB  . LEU   B 75  ? 0.1746 0.1920 0.1282 -0.0126 -0.0249 0.0013  75   LEU   B CB  
4916 C  CG  . LEU   B 75  ? 0.2067 0.2096 0.1640 -0.0349 -0.0122 0.0001  75   LEU   B CG  
4917 C  CD1 . LEU   B 75  ? 0.2387 0.2217 0.1709 -0.0442 0.0100  -0.0029 75   LEU   B CD1 
4918 C  CD2 . LEU   B 75  ? 0.2418 0.2325 0.2295 -0.0257 0.0036  -0.0009 75   LEU   B CD2 
4930 N  N   . LYS   B 76  ? 0.1735 0.2146 0.1819 -0.0015 0.0030  0.0101  76   LYS   B N   
4931 C  CA  . LYS   B 76  ? 0.1784 0.2242 0.2035 -0.0086 0.0166  0.0065  76   LYS   B CA  
4932 C  C   . LYS   B 76  ? 0.1728 0.2087 0.1611 -0.0020 0.0108  0.0200  76   LYS   B C   
4933 O  O   . LYS   B 76  ? 0.1713 0.1983 0.1650 -0.0094 0.0050  0.0230  76   LYS   B O   
4934 C  CB  . LYS   B 76  ? 0.1934 0.2381 0.2706 -0.0162 0.0432  -0.0261 76   LYS   B CB  
4935 C  CG  . LYS   B 76  ? 0.2058 0.2617 0.3295 -0.0111 0.0235  -0.0381 76   LYS   B CG  
4936 C  CD  . LYS   B 76  ? 0.2061 0.2730 0.3816 -0.0046 0.0069  -0.0457 76   LYS   B CD  
4937 C  CE  . LYS   B 76  ? 0.2139 0.2891 0.4326 0.0026  -0.0099 -0.0549 76   LYS   B CE  
4938 N  NZ  . LYS   B 76  ? 0.2099 0.2923 0.4543 -0.0014 -0.0298 -0.0714 76   LYS   B NZ  
4952 N  N   . VAL   B 77  ? 0.1839 0.2163 0.1680 0.0077  0.0078  0.0226  77   VAL   B N   
4953 C  CA  . VAL   B 77  ? 0.1846 0.2023 0.1766 0.0123  0.0111  0.0477  77   VAL   B CA  
4954 C  C   . VAL   B 77  ? 0.1674 0.1837 0.1687 0.0097  0.0169  0.0282  77   VAL   B C   
4955 O  O   . VAL   B 77  ? 0.1744 0.1844 0.1804 0.0199  0.0275  0.0239  77   VAL   B O   
4956 C  CB  . VAL   B 77  ? 0.1943 0.2100 0.2117 0.0163  0.0259  0.0562  77   VAL   B CB  
4957 C  CG1 . VAL   B 77  ? 0.1988 0.1987 0.2502 0.0029  0.0267  0.0711  77   VAL   B CG1 
4958 C  CG2 . VAL   B 77  ? 0.2067 0.2318 0.2422 0.0151  0.0042  0.0609  77   VAL   B CG2 
4968 N  N   . GLY   B 78  ? 0.1641 0.1722 0.1606 0.0066  0.0073  0.0257  78   GLY   B N   
4969 C  CA  . GLY   B 78  ? 0.1673 0.1688 0.1594 0.0091  0.0175  0.0130  78   GLY   B CA  
4970 C  C   . GLY   B 78  ? 0.1597 0.1616 0.1720 0.0100  0.0133  0.0232  78   GLY   B C   
4971 O  O   . GLY   B 78  ? 0.1587 0.1615 0.1935 0.0166  0.0075  0.0317  78   GLY   B O   
4975 N  N   . GLY   B 79  ? 0.1475 0.1665 0.1766 0.0044  0.0126  0.0154  79   GLY   B N   
4976 C  CA  . GLY   B 79  ? 0.1570 0.1557 0.1647 0.0025  0.0070  0.0092  79   GLY   B CA  
4977 C  C   . GLY   B 79  ? 0.1454 0.1475 0.1672 0.0060  0.0074  0.0013  79   GLY   B C   
4978 O  O   . GLY   B 79  ? 0.1511 0.1473 0.1848 0.0066  0.0171  0.0125  79   GLY   B O   
4982 N  N   . SER   B 80  ? 0.1465 0.1435 0.1741 0.0011  0.0146  0.0013  80   SER   B N   
4983 C  CA  . SER   B 80  ? 0.1428 0.1399 0.1782 -0.0023 -0.0033 0.0011  80   SER   B CA  
4984 C  C   . SER   B 80  ? 0.1421 0.1350 0.1678 0.0039  -0.0080 -0.0010 80   SER   B C   
4985 O  O   . SER   B 80  ? 0.1559 0.1378 0.1907 0.0034  -0.0041 -0.0011 80   SER   B O   
4986 C  CB  . SER   B 80  ? 0.1422 0.1408 0.1735 -0.0047 -0.0043 0.0070  80   SER   B CB  
4987 O  OG  . SER   B 80  ? 0.1513 0.1604 0.1919 -0.0021 -0.0113 0.0067  80   SER   B OG  
4993 N  N   . CYS   B 81  ? 0.1378 0.1299 0.1772 0.0009  -0.0099 -0.0038 81   CYS   B N   
4994 C  CA  . CYS   B 81  ? 0.1444 0.1236 0.1743 0.0017  -0.0102 -0.0043 81   CYS   B CA  
4995 C  C   . CYS   B 81  ? 0.1446 0.1252 0.1482 0.0004  -0.0137 0.0002  81   CYS   B C   
4996 O  O   . CYS   B 81  ? 0.1634 0.1293 0.1640 0.0056  -0.0022 -0.0088 81   CYS   B O   
4997 C  CB  . CYS   B 81  ? 0.1597 0.1335 0.1718 -0.0079 -0.0178 -0.0057 81   CYS   B CB  
4998 S  SG  . CYS   B 81  ? 0.1631 0.1574 0.1706 -0.0084 -0.0265 -0.0103 81   CYS   B SG  
5004 N  N   . VAL   B 82  ? 0.1460 0.1269 0.1565 0.0004  -0.0116 -0.0020 82   VAL   B N   
5005 C  CA  . VAL   B 82  ? 0.1547 0.1287 0.1569 -0.0033 -0.0140 0.0108  82   VAL   B CA  
5006 C  C   . VAL   B 82  ? 0.1636 0.1182 0.1705 -0.0036 -0.0105 0.0031  82   VAL   B C   
5007 O  O   . VAL   B 82  ? 0.1679 0.1242 0.1939 -0.0029 -0.0083 -0.0103 82   VAL   B O   
5008 C  CB  . VAL   B 82  ? 0.1625 0.1471 0.1788 -0.0026 -0.0125 0.0078  82   VAL   B CB  
5009 C  CG1 . VAL   B 82  ? 0.1812 0.1745 0.1974 0.0010  -0.0162 0.0125  82   VAL   B CG1 
5010 C  CG2 . VAL   B 82  ? 0.1723 0.1591 0.2008 -0.0060 -0.0325 0.0082  82   VAL   B CG2 
5020 N  N   . LEU   B 83  ? 0.1515 0.1224 0.1618 -0.0172 -0.0208 -0.0056 83   LEU   B N   
5021 C  CA  . LEU   B 83  ? 0.1538 0.1267 0.1529 -0.0138 -0.0235 -0.0067 83   LEU   B CA  
5022 C  C   . LEU   B 83  ? 0.1551 0.1269 0.1531 -0.0160 -0.0185 -0.0067 83   LEU   B C   
5023 O  O   . LEU   B 83  ? 0.1560 0.1356 0.1493 -0.0212 -0.0120 0.0059  83   LEU   B O   
5024 C  CB  . LEU   B 83  ? 0.1539 0.1385 0.1640 -0.0125 -0.0249 -0.0111 83   LEU   B CB  
5025 C  CG  . LEU   B 83  ? 0.1793 0.1598 0.1726 -0.0174 -0.0157 -0.0088 83   LEU   B CG  
5026 C  CD1 . LEU   B 83  ? 0.1944 0.1689 0.1732 -0.0165 -0.0254 0.0068  83   LEU   B CD1 
5027 C  CD2 . LEU   B 83  ? 0.1940 0.1590 0.1967 -0.0140 -0.0134 -0.0246 83   LEU   B CD2 
5039 N  N   . SER   B 84  ? 0.1576 0.1415 0.1787 -0.0210 -0.0192 0.0052  84   SER   B N   
5040 C  CA  . SER   B 84  ? 0.1582 0.1584 0.1709 -0.0259 -0.0172 0.0155  84   SER   B CA  
5041 C  C   . SER   B 84  ? 0.1496 0.1724 0.1223 -0.0193 -0.0142 0.0158  84   SER   B C   
5042 O  O   . SER   B 84  ? 0.1553 0.1603 0.1291 -0.0209 -0.0120 -0.0009 84   SER   B O   
5043 C  CB  . SER   B 84  ? 0.1768 0.1627 0.2154 -0.0306 0.0091  0.0206  84   SER   B CB  
5044 O  OG  . SER   B 84  ? 0.1774 0.1754 0.2584 -0.0394 0.0053  0.0316  84   SER   B OG  
5050 N  N   . GLY   B 85  ? 0.1546 0.1925 0.1455 -0.0248 -0.0171 0.0243  85   GLY   B N   
5051 C  CA  . GLY   B 85  ? 0.1569 0.1980 0.1537 -0.0356 -0.0044 -0.0005 85   GLY   B CA  
5052 C  C   . GLY   B 85  ? 0.1555 0.1808 0.1523 -0.0422 -0.0035 0.0170  85   GLY   B C   
5053 O  O   . GLY   B 85  ? 0.1685 0.1836 0.1606 -0.0526 0.0112  -0.0017 85   GLY   B O   
5057 N  N   . HIS   B 86  ? 0.1505 0.1694 0.1702 -0.0333 -0.0170 0.0166  86   HIS   B N   
5058 C  CA  . HIS   B 86  ? 0.1548 0.1673 0.1687 -0.0301 -0.0179 0.0265  86   HIS   B CA  
5059 C  C   . HIS   B 86  ? 0.1536 0.1821 0.1507 -0.0423 -0.0126 0.0400  86   HIS   B C   
5060 O  O   . HIS   B 86  ? 0.1670 0.1880 0.1576 -0.0293 -0.0006 0.0327  86   HIS   B O   
5061 C  CB  . HIS   B 86  ? 0.1634 0.1760 0.1770 -0.0187 -0.0243 0.0117  86   HIS   B CB  
5062 C  CG  . HIS   B 86  ? 0.1599 0.1754 0.1742 -0.0160 -0.0210 0.0183  86   HIS   B CG  
5063 N  ND1 . HIS   B 86  ? 0.1719 0.1994 0.1991 -0.0337 -0.0207 -0.0013 86   HIS   B ND1 
5064 C  CD2 . HIS   B 86  ? 0.1606 0.1787 0.1782 -0.0086 -0.0237 0.0173  86   HIS   B CD2 
5065 C  CE1 . HIS   B 86  ? 0.1749 0.1912 0.1819 -0.0165 -0.0053 -0.0198 86   HIS   B CE1 
5066 N  NE2 . HIS   B 86  ? 0.1699 0.1811 0.1670 -0.0001 -0.0138 -0.0025 86   HIS   B NE2 
5074 N  N   . ASN   B 87  ? 0.1595 0.1822 0.1633 -0.0395 -0.0076 0.0323  87   ASN   B N   
5075 C  CA  . ASN   B 87  ? 0.1700 0.2040 0.1765 -0.0329 0.0191  0.0178  87   ASN   B CA  
5076 C  C   . ASN   B 87  ? 0.1834 0.1861 0.1558 -0.0355 0.0246  0.0162  87   ASN   B C   
5077 O  O   . ASN   B 87  ? 0.2073 0.1933 0.1908 -0.0231 0.0514  0.0142  87   ASN   B O   
5078 C  CB  . ASN   B 87  ? 0.1702 0.2350 0.2034 -0.0311 0.0236  0.0190  87   ASN   B CB  
5079 C  CG  . ASN   B 87  ? 0.1741 0.2531 0.2140 0.0021  0.0379  0.0386  87   ASN   B CG  
5080 O  OD1 . ASN   B 87  ? 0.1695 0.2368 0.2003 0.0097  0.0456  0.0573  87   ASN   B OD1 
5081 N  ND2 . ASN   B 87  ? 0.2088 0.2674 0.2559 0.0092  0.0498  0.0259  87   ASN   B ND2 
5088 N  N   . LEU   B 88  ? 0.1694 0.1723 0.1541 -0.0402 0.0059  0.0139  88   LEU   B N   
5089 C  CA  . LEU   B 88  ? 0.1857 0.1663 0.1544 -0.0358 -0.0041 0.0055  88   LEU   B CA  
5090 C  C   . LEU   B 88  ? 0.1849 0.1586 0.1543 -0.0408 -0.0031 -0.0011 88   LEU   B C   
5091 O  O   . LEU   B 88  ? 0.2124 0.1642 0.1846 -0.0269 -0.0283 -0.0083 88   LEU   B O   
5092 C  CB  . LEU   B 88  ? 0.1936 0.1795 0.1725 -0.0469 -0.0165 0.0245  88   LEU   B CB  
5093 C  CG  . LEU   B 88  ? 0.2284 0.2064 0.1893 -0.0400 -0.0296 0.0380  88   LEU   B CG  
5094 C  CD1 . LEU   B 88  ? 0.2377 0.2396 0.1909 -0.0480 -0.0231 0.0504  88   LEU   B CD1 
5095 C  CD2 . LEU   B 88  ? 0.2637 0.2322 0.2375 -0.0007 -0.0554 0.0157  88   LEU   B CD2 
5107 N  N   . ALA   B 89  ? 0.1726 0.1550 0.1494 -0.0360 0.0217  0.0013  89   ALA   B N   
5108 C  CA  . ALA   B 89  ? 0.1665 0.1485 0.1413 -0.0355 0.0088  0.0090  89   ALA   B CA  
5109 C  C   . ALA   B 89  ? 0.1712 0.1523 0.1418 -0.0413 0.0174  0.0058  89   ALA   B C   
5110 O  O   . ALA   B 89  ? 0.1615 0.1600 0.1794 -0.0430 0.0098  -0.0229 89   ALA   B O   
5111 C  CB  . ALA   B 89  ? 0.1585 0.1480 0.1451 -0.0360 0.0021  0.0140  89   ALA   B CB  
5117 N  N   . LYS   B 90  ? 0.2118 0.1410 0.1530 -0.0453 -0.0100 0.0144  90   LYS   B N   
5118 C  CA  . LYS   B 90  ? 0.2236 0.1418 0.1570 -0.0437 -0.0081 0.0106  90   LYS   B CA  
5119 C  C   . LYS   B 90  ? 0.2082 0.1299 0.1656 -0.0405 -0.0078 -0.0002 90   LYS   B C   
5120 O  O   . LYS   B 90  ? 0.2177 0.1521 0.1901 -0.0604 0.0010  0.0031  90   LYS   B O   
5121 C  CB  . LYS   B 90  ? 0.2426 0.1483 0.1806 -0.0377 0.0040  0.0135  90   LYS   B CB  
5122 C  CG  . LYS   B 90  ? 0.2426 0.1667 0.1753 -0.0282 0.0306  0.0125  90   LYS   B CG  
5123 C  CD  . LYS   B 90  ? 0.2647 0.1936 0.2303 -0.0199 0.0490  -0.0090 90   LYS   B CD  
5124 C  CE  . LYS   B 90  ? 0.2769 0.2112 0.2866 -0.0262 0.0534  -0.0164 90   LYS   B CE  
5125 N  NZ  . LYS   B 90  ? 0.2783 0.2013 0.2885 -0.0384 0.0678  -0.0126 90   LYS   B NZ  
5139 N  N   . HIS   B 91  ? 0.1810 0.1233 0.1312 -0.0272 -0.0121 0.0076  91   HIS   B N   
5140 C  CA  . HIS   B 91  ? 0.1681 0.1306 0.1432 -0.0258 -0.0222 0.0009  91   HIS   B CA  
5141 C  C   . HIS   B 91  ? 0.1561 0.1319 0.1249 -0.0320 -0.0111 0.0101  91   HIS   B C   
5142 O  O   . HIS   B 91  ? 0.1742 0.1336 0.1274 -0.0312 -0.0257 0.0021  91   HIS   B O   
5143 C  CB  . HIS   B 91  ? 0.1838 0.1296 0.1911 -0.0095 -0.0145 0.0164  91   HIS   B CB  
5144 C  CG  . HIS   B 91  ? 0.2269 0.1495 0.2502 -0.0001 0.0202  0.0168  91   HIS   B CG  
5145 N  ND1 . HIS   B 91  ? 0.2572 0.1578 0.3025 -0.0037 0.0289  0.0042  91   HIS   B ND1 
5146 C  CD2 . HIS   B 91  ? 0.2443 0.1819 0.3056 0.0136  0.0080  0.0539  91   HIS   B CD2 
5147 C  CE1 . HIS   B 91  ? 0.2599 0.1710 0.3312 0.0160  0.0290  0.0114  91   HIS   B CE1 
5148 N  NE2 . HIS   B 91  ? 0.2554 0.1856 0.3384 0.0259  0.0225  0.0542  91   HIS   B NE2 
5156 N  N   . CYS   B 92  ? 0.1529 0.1297 0.1303 -0.0234 -0.0119 0.0068  92   CYS   B N   
5157 C  CA  . CYS   B 92  ? 0.1487 0.1318 0.1280 -0.0217 -0.0113 0.0043  92   CYS   B CA  
5158 C  C   . CYS   B 92  ? 0.1405 0.1237 0.1318 -0.0152 -0.0082 0.0003  92   CYS   B C   
5159 O  O   . CYS   B 92  ? 0.1465 0.1307 0.1552 -0.0181 -0.0038 -0.0035 92   CYS   B O   
5160 C  CB  . CYS   B 92  ? 0.1433 0.1405 0.1383 -0.0171 -0.0109 0.0023  92   CYS   B CB  
5161 S  SG  . CYS   B 92  ? 0.1427 0.1361 0.1596 -0.0126 -0.0124 0.0075  92   CYS   B SG  
5167 N  N   . LEU   B 93  ? 0.1370 0.1257 0.1349 -0.0116 -0.0044 -0.0035 93   LEU   B N   
5168 C  CA  . LEU   B 93  ? 0.1377 0.1253 0.1353 -0.0057 -0.0164 0.0083  93   LEU   B CA  
5169 C  C   . LEU   B 93  ? 0.1306 0.1252 0.1343 -0.0020 -0.0124 0.0079  93   LEU   B C   
5170 O  O   . LEU   B 93  ? 0.1375 0.1232 0.1537 -0.0086 -0.0064 0.0041  93   LEU   B O   
5171 C  CB  . LEU   B 93  ? 0.1399 0.1258 0.1518 -0.0032 -0.0128 0.0113  93   LEU   B CB  
5172 C  CG  . LEU   B 93  ? 0.1387 0.1387 0.1738 -0.0030 -0.0092 0.0170  93   LEU   B CG  
5173 C  CD1 . LEU   B 93  ? 0.1443 0.1462 0.1867 0.0045  -0.0006 -0.0064 93   LEU   B CD1 
5174 C  CD2 . LEU   B 93  ? 0.1340 0.1347 0.1828 -0.0076 -0.0216 0.0060  93   LEU   B CD2 
5186 N  N   . HIS   B 94  ? 0.1334 0.1215 0.1377 -0.0099 -0.0181 0.0090  94   HIS   B N   
5187 C  CA  . HIS   B 94  ? 0.1395 0.1210 0.1270 -0.0058 -0.0111 0.0094  94   HIS   B CA  
5188 C  C   . HIS   B 94  ? 0.1344 0.1237 0.1535 -0.0052 -0.0025 0.0080  94   HIS   B C   
5189 O  O   . HIS   B 94  ? 0.1386 0.1349 0.1881 -0.0103 0.0124  -0.0062 94   HIS   B O   
5190 C  CB  . HIS   B 94  ? 0.1366 0.1324 0.1413 -0.0019 -0.0124 0.0115  94   HIS   B CB  
5191 C  CG  . HIS   B 94  ? 0.1364 0.1283 0.1384 -0.0070 -0.0238 0.0081  94   HIS   B CG  
5192 N  ND1 . HIS   B 94  ? 0.1411 0.1307 0.1442 -0.0104 -0.0241 0.0025  94   HIS   B ND1 
5193 C  CD2 . HIS   B 94  ? 0.1420 0.1252 0.1414 -0.0037 -0.0148 0.0069  94   HIS   B CD2 
5194 C  CE1 . HIS   B 94  ? 0.1410 0.1255 0.1462 -0.0116 -0.0191 0.0054  94   HIS   B CE1 
5195 N  NE2 . HIS   B 94  ? 0.1386 0.1344 0.1466 -0.0141 -0.0107 0.0023  94   HIS   B NE2 
5203 N  N   . VAL   B 95  ? 0.1299 0.1232 0.1564 -0.0035 -0.0016 0.0069  95   VAL   B N   
5204 C  CA  . VAL   B 95  ? 0.1299 0.1345 0.1496 -0.0047 0.0045  0.0131  95   VAL   B CA  
5205 C  C   . VAL   B 95  ? 0.1366 0.1302 0.1582 -0.0034 0.0127  0.0079  95   VAL   B C   
5206 O  O   . VAL   B 95  ? 0.1434 0.1301 0.1747 -0.0014 0.0027  0.0179  95   VAL   B O   
5207 C  CB  . VAL   B 95  ? 0.1372 0.1275 0.1540 -0.0051 -0.0096 0.0094  95   VAL   B CB  
5208 C  CG1 . VAL   B 95  ? 0.1440 0.1508 0.1742 -0.0153 -0.0069 0.0151  95   VAL   B CG1 
5209 C  CG2 . VAL   B 95  ? 0.1547 0.1229 0.1473 -0.0016 -0.0209 0.0015  95   VAL   B CG2 
5219 N  N   . VAL   B 96  ? 0.1489 0.1355 0.1653 0.0026  0.0042  0.0105  96   VAL   B N   
5220 C  CA  . VAL   B 96  ? 0.1545 0.1449 0.1582 0.0009  0.0062  0.0185  96   VAL   B CA  
5221 C  C   . VAL   B 96  ? 0.1526 0.1494 0.1646 0.0047  0.0069  0.0203  96   VAL   B C   
5222 O  O   . VAL   B 96  ? 0.1522 0.1550 0.1832 0.0018  0.0167  0.0059  96   VAL   B O   
5223 C  CB  . VAL   B 96  ? 0.1554 0.1663 0.1490 -0.0008 0.0043  0.0074  96   VAL   B CB  
5224 C  CG1 . VAL   B 96  ? 0.1606 0.1763 0.1631 0.0030  0.0074  0.0034  96   VAL   B CG1 
5225 C  CG2 . VAL   B 96  ? 0.1693 0.1727 0.1530 -0.0022 0.0126  -0.0022 96   VAL   B CG2 
5235 N  N   . GLY   B 97  ? 0.1598 0.1467 0.1622 0.0012  0.0049  0.0273  97   GLY   B N   
5236 C  CA  . GLY   B 97  ? 0.1716 0.1552 0.1569 0.0012  0.0102  0.0210  97   GLY   B CA  
5237 C  C   . GLY   B 97  ? 0.1886 0.1618 0.1717 0.0048  0.0099  0.0141  97   GLY   B C   
5238 O  O   . GLY   B 97  ? 0.1977 0.1682 0.1807 0.0010  0.0069  0.0136  97   GLY   B O   
5242 N  N   . PRO   B 98  ? 0.1981 0.1628 0.1820 0.0066  0.0293  0.0291  98   PRO   B N   
5243 C  CA  . PRO   B 98  ? 0.2091 0.1776 0.1922 0.0143  0.0395  0.0235  98   PRO   B CA  
5244 C  C   . PRO   B 98  ? 0.2201 0.1762 0.1644 0.0238  0.0410  0.0453  98   PRO   B C   
5245 O  O   . PRO   B 98  ? 0.2108 0.1821 0.1758 0.0256  0.0352  0.0417  98   PRO   B O   
5246 C  CB  . PRO   B 98  ? 0.1997 0.1783 0.2043 0.0091  0.0554  0.0169  98   PRO   B CB  
5247 C  CG  . PRO   B 98  ? 0.1962 0.1733 0.2018 0.0035  0.0378  0.0334  98   PRO   B CG  
5248 C  CD  . PRO   B 98  ? 0.1821 0.1706 0.1962 0.0057  0.0310  0.0336  98   PRO   B CD  
5256 N  N   . ASN   B 99  ? 0.2338 0.1956 0.1861 0.0393  0.0361  0.0258  99   ASN   B N   
5257 C  CA  . ASN   B 99  ? 0.2545 0.2045 0.1811 0.0440  0.0236  0.0437  99   ASN   B CA  
5258 C  C   . ASN   B 99  ? 0.2796 0.2372 0.2134 0.0345  0.0384  0.0722  99   ASN   B C   
5259 O  O   . ASN   B 99  ? 0.2908 0.2433 0.2210 0.0286  0.0343  0.0678  99   ASN   B O   
5260 C  CB  . ASN   B 99  ? 0.2638 0.2008 0.1850 0.0435  0.0139  0.0401  99   ASN   B CB  
5261 C  CG  . ASN   B 99  ? 0.2688 0.2101 0.2093 0.0404  -0.0011 0.0305  99   ASN   B CG  
5262 O  OD1 . ASN   B 99  ? 0.2737 0.2071 0.2296 0.0407  -0.0019 0.0379  99   ASN   B OD1 
5263 N  ND2 . ASN   B 99  ? 0.2673 0.2130 0.2186 0.0453  -0.0206 0.0254  99   ASN   B ND2 
5270 N  N   A VAL   B 100 ? 0.2977 0.2473 0.2424 0.0254  0.0421  0.0908  100  VAL   B N   
5271 N  N   B VAL   B 100 ? 0.2969 0.2468 0.2425 0.0245  0.0423  0.0910  100  VAL   B N   
5272 C  CA  A VAL   B 100 ? 0.3247 0.2650 0.2931 0.0177  0.0440  0.0986  100  VAL   B CA  
5273 C  CA  B VAL   B 100 ? 0.3231 0.2640 0.2932 0.0162  0.0442  0.0986  100  VAL   B CA  
5274 C  C   A VAL   B 100 ? 0.3463 0.2709 0.2829 0.0239  0.0471  0.1146  100  VAL   B C   
5275 C  C   B VAL   B 100 ? 0.3453 0.2699 0.2824 0.0231  0.0466  0.1143  100  VAL   B C   
5276 O  O   A VAL   B 100 ? 0.3531 0.2820 0.2892 0.0218  0.0565  0.1079  100  VAL   B O   
5277 O  O   B VAL   B 100 ? 0.3520 0.2802 0.2874 0.0208  0.0554  0.1072  100  VAL   B O   
5278 C  CB  A VAL   B 100 ? 0.3315 0.2781 0.3508 0.0022  0.0412  0.0968  100  VAL   B CB  
5279 C  CB  B VAL   B 100 ? 0.3283 0.2766 0.3506 -0.0006 0.0425  0.0973  100  VAL   B CB  
5280 C  CG1 A VAL   B 100 ? 0.3345 0.2828 0.3736 -0.0031 0.0408  0.0954  100  VAL   B CG1 
5281 C  CG1 B VAL   B 100 ? 0.3310 0.2811 0.3735 -0.0061 0.0426  0.0963  100  VAL   B CG1 
5282 C  CG2 A VAL   B 100 ? 0.3337 0.2835 0.3661 -0.0015 0.0432  0.0993  100  VAL   B CG2 
5283 C  CG2 B VAL   B 100 ? 0.3299 0.2815 0.3661 -0.0049 0.0443  0.0998  100  VAL   B CG2 
5302 N  N   . ASN   B 101 ? 0.3601 0.2714 0.2796 0.0358  0.0361  0.1232  101  ASN   B N   
5303 C  CA  . ASN   B 101 ? 0.4033 0.2868 0.3109 0.0443  0.0151  0.1283  101  ASN   B CA  
5304 C  C   . ASN   B 101 ? 0.4482 0.3250 0.3168 0.0452  0.0062  0.1305  101  ASN   B C   
5305 O  O   . ASN   B 101 ? 0.4555 0.3395 0.3409 0.0502  0.0073  0.1050  101  ASN   B O   
5306 C  CB  . ASN   B 101 ? 0.4021 0.2730 0.3318 0.0401  0.0131  0.1136  101  ASN   B CB  
5307 C  CG  . ASN   B 101 ? 0.3992 0.2564 0.3423 0.0370  0.0128  0.1157  101  ASN   B CG  
5308 O  OD1 . ASN   B 101 ? 0.4045 0.2587 0.3792 0.0264  0.0270  0.1095  101  ASN   B OD1 
5309 N  ND2 . ASN   B 101 ? 0.3932 0.2568 0.3391 0.0340  0.0066  0.1006  101  ASN   B ND2 
5317 N  N   . LYS   B 102 ? 0.4822 0.3536 0.3226 0.0369  0.0100  0.1279  102  LYS   B N   
5318 C  CA  . LYS   B 102 ? 0.5148 0.3923 0.3433 0.0249  0.0209  0.1059  102  LYS   B CA  
5319 C  C   . LYS   B 102 ? 0.5097 0.3932 0.3371 0.0245  0.0344  0.1087  102  LYS   B C   
5320 O  O   . LYS   B 102 ? 0.5203 0.3975 0.3450 0.0263  0.0235  0.0968  102  LYS   B O   
5321 C  CB  . LYS   B 102 ? 0.5473 0.4283 0.3953 0.0146  0.0296  0.0679  102  LYS   B CB  
5322 C  CG  . LYS   B 102 ? 0.5719 0.4585 0.4594 0.0071  0.0378  0.0287  102  LYS   B CG  
5323 C  CD  . LYS   B 102 ? 0.5930 0.4832 0.5242 0.0009  0.0464  -0.0029 102  LYS   B CD  
5324 C  CE  . LYS   B 102 ? 0.6082 0.5004 0.5788 -0.0049 0.0530  -0.0236 102  LYS   B CE  
5325 N  NZ  . LYS   B 102 ? 0.6177 0.5106 0.6108 -0.0080 0.0556  -0.0353 102  LYS   B NZ  
5339 N  N   A GLY   B 103 ? 0.4993 0.3920 0.3335 0.0253  0.0492  0.1116  103  GLY   B N   
5340 N  N   B GLY   B 103 ? 0.4986 0.3880 0.3316 0.0191  0.0468  0.1107  103  GLY   B N   
5341 C  CA  A GLY   B 103 ? 0.4862 0.3889 0.3447 0.0272  0.0645  0.1032  103  GLY   B CA  
5342 C  CA  B GLY   B 103 ? 0.4847 0.3807 0.3407 0.0140  0.0599  0.1017  103  GLY   B CA  
5343 C  C   A GLY   B 103 ? 0.4685 0.3811 0.3433 0.0276  0.0795  0.0913  103  GLY   B C   
5344 C  C   B GLY   B 103 ? 0.4660 0.3683 0.3365 0.0062  0.0733  0.0896  103  GLY   B C   
5345 O  O   A GLY   B 103 ? 0.4732 0.3870 0.3542 0.0254  0.0781  0.0928  103  GLY   B O   
5346 O  O   B GLY   B 103 ? 0.4708 0.3736 0.3494 0.0064  0.0733  0.0881  103  GLY   B O   
5353 N  N   A GLU   B 104 ? 0.4428 0.3644 0.3259 0.0308  0.0956  0.0689  104  GLU   B N   
5354 N  N   B GLU   B 104 ? 0.4392 0.3472 0.3125 -0.0027 0.0865  0.0700  104  GLU   B N   
5355 C  CA  A GLU   B 104 ? 0.4161 0.3473 0.3093 0.0358  0.1051  0.0455  104  GLU   B CA  
5356 C  CA  B GLU   B 104 ? 0.4120 0.3260 0.2896 -0.0117 0.0925  0.0508  104  GLU   B CA  
5357 C  C   A GLU   B 104 ? 0.4150 0.3492 0.3242 0.0193  0.1307  0.0361  104  GLU   B C   
5358 C  C   B GLU   B 104 ? 0.4068 0.3263 0.3003 -0.0213 0.1174  0.0404  104  GLU   B C   
5359 O  O   A GLU   B 104 ? 0.4161 0.3511 0.3393 0.0142  0.1293  0.0338  104  GLU   B O   
5360 O  O   B GLU   B 104 ? 0.4075 0.3272 0.3143 -0.0250 0.1172  0.0375  104  GLU   B O   
5361 C  CB  A GLU   B 104 ? 0.3938 0.3271 0.2917 0.0587  0.0802  0.0228  104  GLU   B CB  
5362 C  CB  B GLU   B 104 ? 0.3939 0.3030 0.2716 -0.0105 0.0644  0.0329  104  GLU   B CB  
5363 C  CG  A GLU   B 104 ? 0.3747 0.3118 0.2730 0.0784  0.0470  -0.0012 104  GLU   B CG  
5364 C  CG  B GLU   B 104 ? 0.3795 0.2838 0.2519 -0.0104 0.0286  0.0120  104  GLU   B CG  
5365 C  CD  A GLU   B 104 ? 0.3566 0.2975 0.2524 0.0953  0.0209  -0.0150 104  GLU   B CD  
5366 C  CD  B GLU   B 104 ? 0.3663 0.2645 0.2302 -0.0161 0.0042  0.0033  104  GLU   B CD  
5367 O  OE1 A GLU   B 104 ? 0.3378 0.2836 0.2153 0.1085  0.0347  -0.0165 104  GLU   B OE1 
5368 O  OE1 B GLU   B 104 ? 0.3505 0.2477 0.2069 -0.0246 0.0151  0.0090  104  GLU   B OE1 
5369 O  OE2 A GLU   B 104 ? 0.3582 0.3041 0.2614 0.0956  -0.0074 -0.0257 104  GLU   B OE2 
5370 O  OE2 B GLU   B 104 ? 0.3679 0.2686 0.2240 -0.0170 -0.0239 -0.0075 104  GLU   B OE2 
5383 N  N   A ASP   B 105 ? 0.4096 0.3501 0.3279 0.0077  0.1549  0.0292  105  ASP   B N   
5384 N  N   B ASP   B 105 ? 0.3983 0.3265 0.2995 -0.0290 0.1425  0.0329  105  ASP   B N   
5385 C  CA  A ASP   B 105 ? 0.4072 0.3499 0.3492 -0.0028 0.1709  0.0149  105  ASP   B CA  
5386 C  CA  B ASP   B 105 ? 0.3934 0.3263 0.3210 -0.0354 0.1594  0.0181  105  ASP   B CA  
5387 C  C   A ASP   B 105 ? 0.3909 0.3241 0.3303 -0.0107 0.1751  0.0088  105  ASP   B C   
5388 C  C   B ASP   B 105 ? 0.3782 0.3028 0.3008 -0.0411 0.1639  0.0106  105  ASP   B C   
5389 O  O   A ASP   B 105 ? 0.3844 0.3191 0.3265 -0.0080 0.1810  0.0097  105  ASP   B O   
5390 O  O   B ASP   B 105 ? 0.3679 0.2954 0.2916 -0.0428 0.1720  0.0133  105  ASP   B O   
5391 C  CB  A ASP   B 105 ? 0.4167 0.3707 0.4003 -0.0005 0.1784  0.0012  105  ASP   B CB  
5392 C  CB  B ASP   B 105 ? 0.3995 0.3455 0.3712 -0.0324 0.1667  0.0058  105  ASP   B CB  
5393 C  CG  A ASP   B 105 ? 0.4227 0.3848 0.4492 -0.0006 0.1869  -0.0070 105  ASP   B CG  
5394 C  CG  B ASP   B 105 ? 0.4024 0.3571 0.4150 -0.0332 0.1768  0.0018  105  ASP   B CG  
5395 O  OD1 A ASP   B 105 ? 0.4217 0.3894 0.4528 -0.0050 0.1984  -0.0035 105  ASP   B OD1 
5396 O  OD1 B ASP   B 105 ? 0.4013 0.3607 0.4192 -0.0384 0.1858  0.0050  105  ASP   B OD1 
5397 O  OD2 A ASP   B 105 ? 0.4270 0.3904 0.4836 0.0031  0.1772  -0.0158 105  ASP   B OD2 
5398 O  OD2 B ASP   B 105 ? 0.4007 0.3624 0.4306 -0.0336 0.1816  0.0021  105  ASP   B OD2 
5407 N  N   A ILE   B 106 ? 0.3811 0.3030 0.3365 -0.0180 0.1609  0.0078  106  ILE   B N   
5408 N  N   B ILE   B 106 ? 0.3725 0.2875 0.3082 -0.0424 0.1477  0.0044  106  ILE   B N   
5409 C  CA  A ILE   B 106 ? 0.3646 0.2814 0.3401 -0.0272 0.1585  0.0076  106  ILE   B CA  
5410 C  CA  B ILE   B 106 ? 0.3597 0.2721 0.3178 -0.0476 0.1432  -0.0000 106  ILE   B CA  
5411 C  C   A ILE   B 106 ? 0.3366 0.2728 0.3305 -0.0248 0.1585  -0.0044 106  ILE   B C   
5412 C  C   B ILE   B 106 ? 0.3335 0.2684 0.3102 -0.0450 0.1411  -0.0191 106  ILE   B C   
5413 O  O   A ILE   B 106 ? 0.3296 0.2544 0.3321 -0.0295 0.1594  -0.0066 106  ILE   B O   
5414 O  O   B ILE   B 106 ? 0.3251 0.2501 0.3056 -0.0547 0.1365  -0.0308 106  ILE   B O   
5415 C  CB  A ILE   B 106 ? 0.3774 0.2744 0.3513 -0.0370 0.1512  0.0177  106  ILE   B CB  
5416 C  CB  B ILE   B 106 ? 0.3745 0.2677 0.3341 -0.0527 0.1368  0.0120  106  ILE   B CB  
5417 C  CG1 A ILE   B 106 ? 0.3827 0.2730 0.3558 -0.0336 0.1444  0.0115  106  ILE   B CG1 
5418 C  CG1 B ILE   B 106 ? 0.3820 0.2690 0.3452 -0.0453 0.1273  0.0072  106  ILE   B CG1 
5419 C  CG2 A ILE   B 106 ? 0.3826 0.2767 0.3676 -0.0419 0.1488  0.0238  106  ILE   B CG2 
5420 C  CG2 B ILE   B 106 ? 0.3798 0.2708 0.3505 -0.0572 0.1356  0.0182  106  ILE   B CG2 
5421 C  CD1 A ILE   B 106 ? 0.3854 0.2738 0.3541 -0.0293 0.1429  0.0098  106  ILE   B CD1 
5422 C  CD1 B ILE   B 106 ? 0.3858 0.2715 0.3474 -0.0383 0.1250  0.0058  106  ILE   B CD1 
5445 N  N   A GLN   B 107 ? 0.3193 0.2845 0.3373 -0.0247 0.1446  -0.0067 107  GLN   B N   
5446 N  N   B GLN   B 107 ? 0.3188 0.2841 0.3236 -0.0391 0.1311  -0.0201 107  GLN   B N   
5447 C  CA  A GLN   B 107 ? 0.3042 0.2968 0.3524 -0.0226 0.1194  -0.0047 107  GLN   B CA  
5448 C  CA  B GLN   B 107 ? 0.3062 0.2994 0.3443 -0.0305 0.1116  -0.0158 107  GLN   B CA  
5449 C  C   A GLN   B 107 ? 0.2737 0.2751 0.3249 -0.0126 0.0929  -0.0154 107  GLN   B C   
5450 C  C   B GLN   B 107 ? 0.2749 0.2790 0.3204 -0.0178 0.0907  -0.0220 107  GLN   B C   
5451 O  O   A GLN   B 107 ? 0.2664 0.2736 0.3484 -0.0075 0.0713  -0.0280 107  GLN   B O   
5452 O  O   B GLN   B 107 ? 0.2692 0.2831 0.3449 -0.0157 0.0704  -0.0368 107  GLN   B O   
5453 C  CB  A GLN   B 107 ? 0.3283 0.3309 0.4097 -0.0241 0.1043  0.0051  107  GLN   B CB  
5454 C  CB  B GLN   B 107 ? 0.3332 0.3344 0.4029 -0.0285 0.0958  -0.0073 107  GLN   B CB  
5455 C  CG  A GLN   B 107 ? 0.3535 0.3603 0.4706 -0.0201 0.0794  0.0111  107  GLN   B CG  
5456 C  CG  B GLN   B 107 ? 0.3609 0.3644 0.4646 -0.0221 0.0711  -0.0019 107  GLN   B CG  
5457 C  CD  A GLN   B 107 ? 0.3717 0.3817 0.5207 -0.0179 0.0612  0.0180  107  GLN   B CD  
5458 C  CD  B GLN   B 107 ? 0.3817 0.3864 0.5158 -0.0177 0.0522  0.0039  107  GLN   B CD  
5459 O  OE1 A GLN   B 107 ? 0.3790 0.3909 0.5411 -0.0133 0.0610  0.0174  107  GLN   B OE1 
5460 O  OE1 B GLN   B 107 ? 0.3903 0.3952 0.5373 -0.0139 0.0525  0.0040  107  GLN   B OE1 
5461 N  NE2 A GLN   B 107 ? 0.3797 0.3879 0.5380 -0.0174 0.0515  0.0240  107  GLN   B NE2 
5462 N  NE2 B GLN   B 107 ? 0.3907 0.3934 0.5323 -0.0162 0.0420  0.0086  107  GLN   B NE2 
5479 N  N   . LEU   B 108 ? 0.2453 0.2546 0.2829 -0.0012 0.0882  -0.0152 108  LEU   B N   
5480 C  CA  . LEU   B 108 ? 0.2247 0.2275 0.2503 0.0241  0.0605  0.0032  108  LEU   B CA  
5481 C  C   . LEU   B 108 ? 0.1902 0.1863 0.2462 0.0239  0.0343  0.0214  108  LEU   B C   
5482 O  O   . LEU   B 108 ? 0.1916 0.1755 0.2459 0.0197  0.0181  0.0206  108  LEU   B O   
5483 C  CB  . LEU   B 108 ? 0.2391 0.2479 0.2321 0.0221  0.0600  0.0068  108  LEU   B CB  
5484 C  CG  . LEU   B 108 ? 0.2535 0.2792 0.2411 0.0246  0.0510  -0.0122 108  LEU   B CG  
5485 C  CD1 . LEU   B 108 ? 0.2652 0.2957 0.2372 0.0092  0.0482  -0.0057 108  LEU   B CD1 
5486 C  CD2 . LEU   B 108 ? 0.2718 0.2947 0.2603 0.0328  0.0434  -0.0207 108  LEU   B CD2 
5499 N  N   . LEU   B 109 ? 0.1767 0.1710 0.2411 0.0141  0.0370  0.0227  109  LEU   B N   
5500 C  CA  . LEU   B 109 ? 0.1631 0.1486 0.2463 0.0081  0.0322  0.0267  109  LEU   B CA  
5501 C  C   . LEU   B 109 ? 0.1517 0.1365 0.2413 0.0021  0.0276  0.0272  109  LEU   B C   
5502 O  O   . LEU   B 109 ? 0.1474 0.1346 0.2355 0.0036  0.0218  0.0332  109  LEU   B O   
5503 C  CB  . LEU   B 109 ? 0.1772 0.1451 0.2493 0.0033  0.0215  0.0332  109  LEU   B CB  
5504 C  CG  . LEU   B 109 ? 0.1735 0.1383 0.2492 0.0056  0.0184  0.0193  109  LEU   B CG  
5505 C  CD1 . LEU   B 109 ? 0.1689 0.1488 0.2384 0.0087  0.0170  0.0212  109  LEU   B CD1 
5506 C  CD2 . LEU   B 109 ? 0.1902 0.1418 0.2554 0.0054  0.0121  0.0195  109  LEU   B CD2 
5518 N  N   . LYS   B 110 ? 0.1471 0.1377 0.2347 -0.0061 0.0256  0.0244  110  LYS   B N   
5519 C  CA  . LYS   B 110 ? 0.1439 0.1351 0.2448 -0.0015 0.0216  0.0097  110  LYS   B CA  
5520 C  C   . LYS   B 110 ? 0.1429 0.1350 0.2321 -0.0073 0.0221  0.0102  110  LYS   B C   
5521 O  O   . LYS   B 110 ? 0.1402 0.1355 0.2170 -0.0086 0.0180  0.0025  110  LYS   B O   
5522 C  CB  . LYS   B 110 ? 0.1464 0.1382 0.2645 -0.0034 0.0233  0.0079  110  LYS   B CB  
5523 C  CG  . LYS   B 110 ? 0.1474 0.1359 0.2818 -0.0084 0.0054  0.0182  110  LYS   B CG  
5524 C  CD  . LYS   B 110 ? 0.1553 0.1387 0.2854 -0.0107 -0.0003 0.0203  110  LYS   B CD  
5525 C  CE  . LYS   B 110 ? 0.1501 0.1508 0.3005 -0.0030 0.0034  0.0087  110  LYS   B CE  
5526 N  NZ  . LYS   B 110 ? 0.1517 0.1660 0.2953 -0.0053 -0.0015 0.0044  110  LYS   B NZ  
5540 N  N   . SER   B 111 ? 0.1471 0.1348 0.2417 -0.0091 0.0223  0.0126  111  SER   B N   
5541 C  CA  . SER   B 111 ? 0.1551 0.1392 0.2251 -0.0035 0.0119  0.0156  111  SER   B CA  
5542 C  C   . SER   B 111 ? 0.1453 0.1329 0.2118 -0.0010 0.0116  0.0037  111  SER   B C   
5543 O  O   . SER   B 111 ? 0.1446 0.1362 0.2177 -0.0033 0.0035  0.0046  111  SER   B O   
5544 C  CB  . SER   B 111 ? 0.1688 0.1621 0.2251 0.0003  0.0328  0.0284  111  SER   B CB  
5545 O  OG  . SER   B 111 ? 0.1852 0.1999 0.2338 0.0060  0.0369  0.0295  111  SER   B OG  
5551 N  N   . ALA   B 112 ? 0.1368 0.1372 0.2234 0.0011  0.0198  0.0170  112  ALA   B N   
5552 C  CA  . ALA   B 112 ? 0.1380 0.1421 0.2147 -0.0019 0.0041  0.0015  112  ALA   B CA  
5553 C  C   . ALA   B 112 ? 0.1347 0.1357 0.2004 -0.0030 0.0058  -0.0048 112  ALA   B C   
5554 O  O   . ALA   B 112 ? 0.1320 0.1344 0.2102 -0.0089 0.0082  -0.0005 112  ALA   B O   
5555 C  CB  . ALA   B 112 ? 0.1447 0.1469 0.2283 -0.0021 -0.0002 0.0072  112  ALA   B CB  
5561 N  N   . TYR   B 113 ? 0.1310 0.1243 0.2053 -0.0041 0.0036  0.0033  113  TYR   B N   
5562 C  CA  . TYR   B 113 ? 0.1311 0.1215 0.2000 -0.0049 0.0057  -0.0025 113  TYR   B CA  
5563 C  C   . TYR   B 113 ? 0.1280 0.1183 0.1977 -0.0061 0.0006  -0.0001 113  TYR   B C   
5564 O  O   . TYR   B 113 ? 0.1322 0.1269 0.1948 -0.0042 -0.0076 -0.0085 113  TYR   B O   
5565 C  CB  . TYR   B 113 ? 0.1378 0.1146 0.2105 -0.0020 0.0120  0.0084  113  TYR   B CB  
5566 C  CG  . TYR   B 113 ? 0.1340 0.1221 0.2230 -0.0073 0.0042  0.0113  113  TYR   B CG  
5567 C  CD1 . TYR   B 113 ? 0.1435 0.1266 0.2362 -0.0086 0.0095  0.0189  113  TYR   B CD1 
5568 C  CD2 . TYR   B 113 ? 0.1434 0.1243 0.2195 -0.0011 -0.0025 0.0081  113  TYR   B CD2 
5569 C  CE1 . TYR   B 113 ? 0.1436 0.1306 0.2202 -0.0024 0.0169  0.0121  113  TYR   B CE1 
5570 C  CE2 . TYR   B 113 ? 0.1487 0.1209 0.2247 0.0027  -0.0041 0.0140  113  TYR   B CE2 
5571 C  CZ  . TYR   B 113 ? 0.1426 0.1284 0.2353 0.0039  0.0035  0.0085  113  TYR   B CZ  
5572 O  OH  . TYR   B 113 ? 0.1474 0.1244 0.2540 0.0085  0.0081  0.0037  113  TYR   B OH  
5582 N  N   . GLU   B 114 ? 0.1280 0.1127 0.2104 -0.0055 0.0083  0.0032  114  GLU   B N   
5583 C  CA  . GLU   B 114 ? 0.1264 0.1125 0.2096 -0.0011 0.0013  0.0019  114  GLU   B CA  
5584 C  C   . GLU   B 114 ? 0.1257 0.1146 0.2013 -0.0028 0.0053  0.0025  114  GLU   B C   
5585 O  O   . GLU   B 114 ? 0.1259 0.1183 0.2233 0.0010  -0.0041 0.0096  114  GLU   B O   
5586 C  CB  . GLU   B 114 ? 0.1297 0.1247 0.2216 -0.0035 0.0027  0.0049  114  GLU   B CB  
5587 C  CG  . GLU   B 114 ? 0.1355 0.1241 0.2280 -0.0044 -0.0019 0.0069  114  GLU   B CG  
5588 C  CD  . GLU   B 114 ? 0.1296 0.1290 0.2348 -0.0071 -0.0006 0.0030  114  GLU   B CD  
5589 O  OE1 . GLU   B 114 ? 0.1279 0.1425 0.2284 -0.0102 0.0095  0.0083  114  GLU   B OE1 
5590 O  OE2 . GLU   B 114 ? 0.1302 0.1450 0.2479 -0.0158 0.0072  0.0038  114  GLU   B OE2 
5597 N  N   . ASN   B 115 ? 0.1306 0.1141 0.2001 -0.0061 -0.0033 0.0053  115  ASN   B N   
5598 C  CA  . ASN   B 115 ? 0.1308 0.1267 0.1836 -0.0063 -0.0031 0.0017  115  ASN   B CA  
5599 C  C   . ASN   B 115 ? 0.1269 0.1194 0.1923 -0.0125 -0.0033 -0.0016 115  ASN   B C   
5600 O  O   . ASN   B 115 ? 0.1343 0.1217 0.1937 -0.0113 -0.0009 0.0015  115  ASN   B O   
5601 C  CB  . ASN   B 115 ? 0.1434 0.1370 0.1880 -0.0099 0.0046  0.0046  115  ASN   B CB  
5602 C  CG  . ASN   B 115 ? 0.1494 0.1387 0.1854 0.0052  -0.0038 -0.0009 115  ASN   B CG  
5603 O  OD1 . ASN   B 115 ? 0.1854 0.1510 0.2074 -0.0006 0.0006  -0.0146 115  ASN   B OD1 
5604 N  ND2 . ASN   B 115 ? 0.1419 0.1476 0.1850 -0.0004 0.0096  0.0086  115  ASN   B ND2 
5611 N  N   . PHE   B 116 ? 0.1308 0.1184 0.1788 -0.0060 -0.0049 0.0021  116  PHE   B N   
5612 C  CA  . PHE   B 116 ? 0.1344 0.1198 0.1804 -0.0084 -0.0047 -0.0011 116  PHE   B CA  
5613 C  C   . PHE   B 116 ? 0.1338 0.1103 0.1906 -0.0112 -0.0091 0.0098  116  PHE   B C   
5614 O  O   . PHE   B 116 ? 0.1398 0.1181 0.1873 -0.0021 -0.0141 0.0014  116  PHE   B O   
5615 C  CB  . PHE   B 116 ? 0.1333 0.1192 0.1819 -0.0056 -0.0129 0.0071  116  PHE   B CB  
5616 C  CG  . PHE   B 116 ? 0.1244 0.1176 0.1941 -0.0080 -0.0106 0.0041  116  PHE   B CG  
5617 C  CD1 . PHE   B 116 ? 0.1294 0.1249 0.2158 -0.0044 -0.0044 0.0032  116  PHE   B CD1 
5618 C  CD2 . PHE   B 116 ? 0.1331 0.1298 0.1908 -0.0086 0.0007  -0.0023 116  PHE   B CD2 
5619 C  CE1 . PHE   B 116 ? 0.1381 0.1293 0.2148 -0.0098 -0.0175 0.0033  116  PHE   B CE1 
5620 C  CE2 . PHE   B 116 ? 0.1322 0.1244 0.1936 -0.0034 -0.0042 -0.0028 116  PHE   B CE2 
5621 C  CZ  . PHE   B 116 ? 0.1290 0.1276 0.1955 -0.0061 -0.0170 0.0048  116  PHE   B CZ  
5631 N  N   . ASN   B 117 ? 0.1357 0.1166 0.2006 -0.0039 -0.0188 0.0060  117  ASN   B N   
5632 C  CA  . ASN   B 117 ? 0.1410 0.1187 0.1984 -0.0024 -0.0054 -0.0048 117  ASN   B CA  
5633 C  C   . ASN   B 117 ? 0.1466 0.1178 0.2083 -0.0041 -0.0118 0.0032  117  ASN   B C   
5634 O  O   . ASN   B 117 ? 0.1506 0.1274 0.2370 -0.0076 -0.0390 0.0110  117  ASN   B O   
5635 C  CB  . ASN   B 117 ? 0.1422 0.1240 0.2025 -0.0007 -0.0105 -0.0036 117  ASN   B CB  
5636 C  CG  . ASN   B 117 ? 0.1380 0.1219 0.2133 0.0033  -0.0114 -0.0064 117  ASN   B CG  
5637 O  OD1 . ASN   B 117 ? 0.1577 0.1261 0.2459 -0.0130 -0.0004 -0.0055 117  ASN   B OD1 
5638 N  ND2 . ASN   B 117 ? 0.1404 0.1297 0.2004 -0.0041 -0.0085 -0.0046 117  ASN   B ND2 
5645 N  N   . GLN   B 118 ? 0.1415 0.1136 0.1980 -0.0067 -0.0188 -0.0003 118  GLN   B N   
5646 C  CA  . GLN   B 118 ? 0.1467 0.1184 0.2120 0.0005  -0.0197 -0.0041 118  GLN   B CA  
5647 C  C   . GLN   B 118 ? 0.1512 0.1163 0.2225 -0.0021 -0.0210 -0.0052 118  GLN   B C   
5648 O  O   . GLN   B 118 ? 0.1665 0.1188 0.2568 -0.0112 -0.0086 0.0039  118  GLN   B O   
5649 C  CB  . GLN   B 118 ? 0.1574 0.1238 0.2195 -0.0031 -0.0200 -0.0002 118  GLN   B CB  
5650 C  CG  . GLN   B 118 ? 0.1599 0.1318 0.2175 0.0011  -0.0099 -0.0119 118  GLN   B CG  
5651 C  CD  . GLN   B 118 ? 0.1611 0.1242 0.2150 0.0017  -0.0112 -0.0158 118  GLN   B CD  
5652 O  OE1 . GLN   B 118 ? 0.1727 0.1190 0.2390 0.0010  -0.0029 -0.0047 118  GLN   B OE1 
5653 N  NE2 . GLN   B 118 ? 0.1714 0.1285 0.2237 -0.0002 -0.0154 0.0046  118  GLN   B NE2 
5662 N  N   . HIS   B 119 ? 0.1547 0.1190 0.1967 -0.0101 -0.0229 0.0072  119  HIS   B N   
5663 C  CA  . HIS   B 119 ? 0.1629 0.1299 0.1929 -0.0046 -0.0231 0.0083  119  HIS   B CA  
5664 C  C   . HIS   B 119 ? 0.1694 0.1305 0.1913 -0.0023 -0.0363 0.0078  119  HIS   B C   
5665 O  O   . HIS   B 119 ? 0.1703 0.1313 0.2185 -0.0237 -0.0190 0.0057  119  HIS   B O   
5666 C  CB  . HIS   B 119 ? 0.1665 0.1433 0.1959 0.0003  -0.0197 0.0017  119  HIS   B CB  
5667 C  CG  . HIS   B 119 ? 0.1673 0.1645 0.2103 0.0088  -0.0400 -0.0136 119  HIS   B CG  
5668 N  ND1 . HIS   B 119 ? 0.1841 0.1829 0.2454 0.0048  -0.0481 -0.0320 119  HIS   B ND1 
5669 C  CD2 . HIS   B 119 ? 0.1910 0.1854 0.2131 0.0343  -0.0521 -0.0219 119  HIS   B CD2 
5670 C  CE1 . HIS   B 119 ? 0.2009 0.1956 0.2470 0.0197  -0.0549 -0.0426 119  HIS   B CE1 
5671 N  NE2 . HIS   B 119 ? 0.2090 0.2104 0.2223 0.0301  -0.0524 -0.0360 119  HIS   B NE2 
5679 N  N   . GLU   B 120 ? 0.1893 0.1309 0.1829 -0.0078 -0.0451 0.0157  120  GLU   B N   
5680 C  CA  . GLU   B 120 ? 0.2203 0.1489 0.2021 -0.0012 -0.0549 0.0218  120  GLU   B CA  
5681 C  C   . GLU   B 120 ? 0.1980 0.1376 0.1776 -0.0120 -0.0421 0.0261  120  GLU   B C   
5682 O  O   . GLU   B 120 ? 0.1885 0.1482 0.1883 -0.0140 -0.0438 0.0137  120  GLU   B O   
5683 C  CB  . GLU   B 120 ? 0.2828 0.1805 0.2581 0.0169  -0.0851 0.0474  120  GLU   B CB  
5684 C  CG  . GLU   B 120 ? 0.3415 0.2518 0.3539 0.0233  -0.0996 0.0649  120  GLU   B CG  
5685 C  CD  . GLU   B 120 ? 0.3820 0.3120 0.4486 0.0218  -0.1013 0.0805  120  GLU   B CD  
5686 O  OE1 . GLU   B 120 ? 0.4035 0.3341 0.4783 0.0149  -0.0935 0.0981  120  GLU   B OE1 
5687 O  OE2 . GLU   B 120 ? 0.4073 0.3408 0.5048 0.0205  -0.1008 0.0691  120  GLU   B OE2 
5694 N  N   . VAL   B 121 ? 0.1842 0.1376 0.1733 -0.0189 -0.0332 0.0230  121  VAL   B N   
5695 C  CA  . VAL   B 121 ? 0.1764 0.1459 0.1635 -0.0147 -0.0306 0.0187  121  VAL   B CA  
5696 C  C   . VAL   B 121 ? 0.1678 0.1424 0.1585 -0.0219 -0.0222 0.0099  121  VAL   B C   
5697 O  O   . VAL   B 121 ? 0.1765 0.1400 0.1822 -0.0285 -0.0339 0.0079  121  VAL   B O   
5698 C  CB  . VAL   B 121 ? 0.1973 0.1868 0.1773 -0.0091 -0.0336 0.0215  121  VAL   B CB  
5699 C  CG1 . VAL   B 121 ? 0.2000 0.1957 0.2089 -0.0203 -0.0172 0.0204  121  VAL   B CG1 
5700 C  CG2 . VAL   B 121 ? 0.2255 0.2095 0.1859 0.0025  -0.0178 0.0044  121  VAL   B CG2 
5710 N  N   . LEU   B 122 ? 0.1637 0.1322 0.1564 -0.0156 -0.0268 0.0063  122  LEU   B N   
5711 C  CA  . LEU   B 122 ? 0.1526 0.1428 0.1457 -0.0193 -0.0259 0.0100  122  LEU   B CA  
5712 C  C   . LEU   B 122 ? 0.1519 0.1285 0.1521 -0.0261 -0.0225 0.0114  122  LEU   B C   
5713 O  O   . LEU   B 122 ? 0.1641 0.1299 0.1853 -0.0337 -0.0274 0.0038  122  LEU   B O   
5714 C  CB  . LEU   B 122 ? 0.1708 0.1536 0.1829 -0.0013 -0.0368 0.0146  122  LEU   B CB  
5715 C  CG  . LEU   B 122 ? 0.1664 0.1624 0.1989 -0.0175 -0.0145 0.0118  122  LEU   B CG  
5716 C  CD1 . LEU   B 122 ? 0.1715 0.1865 0.2039 -0.0218 -0.0222 0.0165  122  LEU   B CD1 
5717 C  CD2 . LEU   B 122 ? 0.1697 0.1592 0.1713 -0.0140 -0.0059 0.0062  122  LEU   B CD2 
5729 N  N   . LEU   B 123 ? 0.1522 0.1227 0.1497 -0.0212 -0.0169 0.0095  123  LEU   B N   
5730 C  CA  . LEU   B 123 ? 0.1540 0.1251 0.1586 -0.0242 -0.0256 0.0027  123  LEU   B CA  
5731 C  C   . LEU   B 123 ? 0.1494 0.1209 0.1548 -0.0275 -0.0176 0.0012  123  LEU   B C   
5732 O  O   . LEU   B 123 ? 0.1628 0.1268 0.1515 -0.0343 -0.0191 0.0033  123  LEU   B O   
5733 C  CB  . LEU   B 123 ? 0.1633 0.1288 0.1680 -0.0227 -0.0126 0.0017  123  LEU   B CB  
5734 C  CG  . LEU   B 123 ? 0.1615 0.1350 0.1717 -0.0153 -0.0094 0.0055  123  LEU   B CG  
5735 C  CD1 . LEU   B 123 ? 0.1687 0.1417 0.1723 -0.0154 -0.0043 -0.0035 123  LEU   B CD1 
5736 C  CD2 . LEU   B 123 ? 0.1711 0.1399 0.1883 -0.0161 -0.0025 0.0208  123  LEU   B CD2 
5748 N  N   . ALA   B 124 ? 0.1454 0.1223 0.1522 -0.0175 -0.0092 0.0019  124  ALA   B N   
5749 C  CA  . ALA   B 124 ? 0.1391 0.1227 0.1659 -0.0151 -0.0106 -0.0068 124  ALA   B CA  
5750 C  C   . ALA   B 124 ? 0.1317 0.1267 0.1565 -0.0242 -0.0146 0.0042  124  ALA   B C   
5751 O  O   . ALA   B 124 ? 0.1451 0.1249 0.1666 -0.0145 -0.0187 0.0004  124  ALA   B O   
5752 C  CB  . ALA   B 124 ? 0.1530 0.1302 0.1746 -0.0135 0.0045  -0.0090 124  ALA   B CB  
5758 N  N   . PRO   B 125 ? 0.1455 0.1314 0.1506 -0.0156 -0.0248 0.0082  125  PRO   B N   
5759 C  CA  . PRO   B 125 ? 0.1533 0.1296 0.1732 -0.0132 -0.0193 0.0229  125  PRO   B CA  
5760 C  C   . PRO   B 125 ? 0.1453 0.1243 0.1914 -0.0160 -0.0170 0.0085  125  PRO   B C   
5761 O  O   . PRO   B 125 ? 0.1461 0.1185 0.2092 -0.0138 -0.0060 0.0134  125  PRO   B O   
5762 C  CB  . PRO   B 125 ? 0.1552 0.1497 0.1840 -0.0219 -0.0278 0.0331  125  PRO   B CB  
5763 C  CG  . PRO   B 125 ? 0.1644 0.1542 0.1701 -0.0282 -0.0257 0.0161  125  PRO   B CG  
5764 C  CD  . PRO   B 125 ? 0.1556 0.1371 0.1503 -0.0276 -0.0207 0.0112  125  PRO   B CD  
5772 N  N   . LEU   B 126 ? 0.1507 0.1172 0.2032 -0.0145 0.0056  0.0120  126  LEU   B N   
5773 C  CA  . LEU   B 126 ? 0.1568 0.1283 0.2131 -0.0144 0.0106  0.0189  126  LEU   B CA  
5774 C  C   . LEU   B 126 ? 0.1493 0.1355 0.2076 -0.0017 0.0131  0.0235  126  LEU   B C   
5775 O  O   . LEU   B 126 ? 0.1719 0.1621 0.2331 0.0189  -0.0088 -0.0045 126  LEU   B O   
5776 C  CB  . LEU   B 126 ? 0.1668 0.1323 0.2481 -0.0174 0.0154  0.0172  126  LEU   B CB  
5777 C  CG  . LEU   B 126 ? 0.1839 0.1411 0.2558 -0.0250 0.0191  -0.0033 126  LEU   B CG  
5778 C  CD1 . LEU   B 126 ? 0.1905 0.1512 0.2995 -0.0245 0.0134  -0.0154 126  LEU   B CD1 
5779 C  CD2 . LEU   B 126 ? 0.1874 0.1503 0.2513 -0.0285 0.0041  0.0009  126  LEU   B CD2 
5791 N  N   . LEU   B 127 ? 0.1483 0.1247 0.2193 0.0021  0.0124  0.0108  127  LEU   B N   
5792 C  CA  . LEU   B 127 ? 0.1438 0.1346 0.2218 -0.0080 0.0159  0.0168  127  LEU   B CA  
5793 C  C   . LEU   B 127 ? 0.1414 0.1321 0.2255 -0.0059 0.0142  0.0234  127  LEU   B C   
5794 O  O   . LEU   B 127 ? 0.1471 0.1336 0.2279 -0.0139 0.0092  0.0189  127  LEU   B O   
5795 C  CB  . LEU   B 127 ? 0.1597 0.1302 0.2301 -0.0064 0.0192  0.0220  127  LEU   B CB  
5796 C  CG  . LEU   B 127 ? 0.1731 0.1316 0.2489 0.0007  0.0174  0.0205  127  LEU   B CG  
5797 C  CD1 . LEU   B 127 ? 0.1783 0.1307 0.2590 0.0008  0.0052  0.0099  127  LEU   B CD1 
5798 C  CD2 . LEU   B 127 ? 0.1730 0.1432 0.2521 -0.0077 0.0172  0.0334  127  LEU   B CD2 
5810 N  N   . SER   B 128 ? 0.1449 0.1320 0.2241 -0.0012 -0.0080 0.0154  128  SER   B N   
5811 C  CA  . SER   B 128 ? 0.1609 0.1405 0.2132 0.0038  -0.0103 0.0162  128  SER   B CA  
5812 C  C   . SER   B 128 ? 0.1734 0.1439 0.2289 0.0046  -0.0163 0.0162  128  SER   B C   
5813 O  O   . SER   B 128 ? 0.1875 0.1459 0.2678 0.0020  -0.0191 0.0340  128  SER   B O   
5814 C  CB  . SER   B 128 ? 0.1703 0.1452 0.2137 0.0070  -0.0052 0.0295  128  SER   B CB  
5815 O  OG  . SER   B 128 ? 0.1762 0.1567 0.2179 0.0077  0.0095  0.0329  128  SER   B OG  
5821 N  N   . ALA   B 129 ? 0.1879 0.1471 0.2424 0.0240  -0.0164 0.0046  129  ALA   B N   
5822 C  CA  . ALA   B 129 ? 0.2040 0.1564 0.2640 0.0276  -0.0141 -0.0049 129  ALA   B CA  
5823 C  C   . ALA   B 129 ? 0.1898 0.1495 0.2586 0.0209  0.0089  0.0035  129  ALA   B C   
5824 O  O   . ALA   B 129 ? 0.1766 0.1529 0.2559 0.0151  -0.0068 0.0089  129  ALA   B O   
5825 C  CB  . ALA   B 129 ? 0.2272 0.1814 0.2941 0.0355  -0.0025 -0.0152 129  ALA   B CB  
5831 N  N   . GLY   B 130 ? 0.1832 0.1409 0.2658 0.0263  0.0167  0.0001  130  GLY   B N   
5832 C  CA  . GLY   B 130 ? 0.1835 0.1558 0.2765 0.0222  0.0337  0.0010  130  GLY   B CA  
5833 C  C   . GLY   B 130 ? 0.1850 0.1571 0.2719 0.0138  0.0159  0.0016  130  GLY   B C   
5834 O  O   . GLY   B 130 ? 0.1977 0.1687 0.2804 0.0140  0.0083  0.0093  130  GLY   B O   
5838 N  N   . ILE   B 131 ? 0.1758 0.1682 0.2732 0.0315  0.0143  0.0045  131  ILE   B N   
5839 C  CA  . ILE   B 131 ? 0.1982 0.1826 0.2673 0.0287  -0.0009 0.0154  131  ILE   B CA  
5840 C  C   . ILE   B 131 ? 0.2115 0.1761 0.2434 0.0209  0.0029  0.0208  131  ILE   B C   
5841 O  O   . ILE   B 131 ? 0.2366 0.1936 0.2572 0.0264  -0.0142 0.0244  131  ILE   B O   
5842 C  CB  . ILE   B 131 ? 0.2017 0.2161 0.2974 0.0260  -0.0039 0.0218  131  ILE   B CB  
5843 C  CG1 . ILE   B 131 ? 0.2118 0.2342 0.3079 0.0037  0.0029  0.0225  131  ILE   B CG1 
5844 C  CG2 . ILE   B 131 ? 0.2008 0.2340 0.3094 0.0321  -0.0068 0.0123  131  ILE   B CG2 
5845 C  CD1 . ILE   B 131 ? 0.2288 0.2551 0.3253 -0.0149 -0.0027 0.0298  131  ILE   B CD1 
5857 N  N   . PHE   B 132 ? 0.1988 0.1588 0.2271 0.0126  0.0195  0.0283  132  PHE   B N   
5858 C  CA  . PHE   B 132 ? 0.2072 0.1645 0.2259 0.0045  0.0396  0.0175  132  PHE   B CA  
5859 C  C   . PHE   B 132 ? 0.2285 0.1815 0.2453 0.0051  0.0470  0.0131  132  PHE   B C   
5860 O  O   . PHE   B 132 ? 0.2450 0.2023 0.2693 0.0028  0.0569  0.0136  132  PHE   B O   
5861 C  CB  . PHE   B 132 ? 0.1891 0.1587 0.2131 0.0126  0.0313  0.0233  132  PHE   B CB  
5862 C  CG  . PHE   B 132 ? 0.1790 0.1620 0.2188 0.0212  0.0212  0.0153  132  PHE   B CG  
5863 C  CD1 . PHE   B 132 ? 0.1906 0.1657 0.2496 0.0131  0.0245  0.0199  132  PHE   B CD1 
5864 C  CD2 . PHE   B 132 ? 0.1874 0.1650 0.1999 0.0267  0.0191  0.0329  132  PHE   B CD2 
5865 C  CE1 . PHE   B 132 ? 0.1988 0.1690 0.2611 0.0074  0.0221  0.0277  132  PHE   B CE1 
5866 C  CE2 . PHE   B 132 ? 0.1974 0.1693 0.2091 0.0154  0.0181  0.0244  132  PHE   B CE2 
5867 C  CZ  . PHE   B 132 ? 0.1991 0.1685 0.2406 0.0094  0.0128  0.0337  132  PHE   B CZ  
5877 N  N   . GLY   B 133 ? 0.2262 0.1657 0.2462 0.0020  0.0353  0.0346  133  GLY   B N   
5878 C  CA  . GLY   B 133 ? 0.2308 0.1766 0.2564 -0.0158 0.0188  0.0471  133  GLY   B CA  
5879 C  C   . GLY   B 133 ? 0.2311 0.1853 0.2612 -0.0299 0.0280  0.0478  133  GLY   B C   
5880 O  O   . GLY   B 133 ? 0.2536 0.2024 0.3070 -0.0432 0.0249  0.0608  133  GLY   B O   
5884 N  N   . ALA   B 134 ? 0.2147 0.1869 0.2454 -0.0283 0.0275  0.0237  134  ALA   B N   
5885 C  CA  . ALA   B 134 ? 0.2166 0.1806 0.2499 -0.0209 0.0383  0.0158  134  ALA   B CA  
5886 C  C   . ALA   B 134 ? 0.2283 0.1712 0.2540 -0.0129 0.0308  0.0212  134  ALA   B C   
5887 O  O   . ALA   B 134 ? 0.2287 0.1890 0.2712 -0.0052 0.0197  0.0140  134  ALA   B O   
5888 C  CB  . ALA   B 134 ? 0.2192 0.1772 0.2718 -0.0141 0.0301  0.0135  134  ALA   B CB  
5894 N  N   . ASP   B 135 ? 0.2411 0.1621 0.2498 -0.0149 0.0188  0.0203  135  ASP   B N   
5895 C  CA  . ASP   B 135 ? 0.2579 0.1596 0.2669 -0.0154 0.0029  0.0243  135  ASP   B CA  
5896 C  C   . ASP   B 135 ? 0.2373 0.1507 0.2592 -0.0065 -0.0008 0.0257  135  ASP   B C   
5897 O  O   . ASP   B 135 ? 0.2260 0.1409 0.2692 -0.0113 0.0013  0.0238  135  ASP   B O   
5898 C  CB  . ASP   B 135 ? 0.2917 0.1701 0.2878 -0.0410 0.0011  0.0253  135  ASP   B CB  
5899 C  CG  . ASP   B 135 ? 0.3215 0.1706 0.3282 -0.0589 0.0029  0.0258  135  ASP   B CG  
5900 O  OD1 . ASP   B 135 ? 0.3348 0.1632 0.3329 -0.0423 -0.0069 0.0261  135  ASP   B OD1 
5901 O  OD2 . ASP   B 135 ? 0.3426 0.2062 0.3853 -0.0703 0.0037  0.0113  135  ASP   B OD2 
5906 N  N   . PRO   B 136 ? 0.2326 0.1522 0.2713 0.0121  -0.0091 0.0239  136  PRO   B N   
5907 C  CA  . PRO   B 136 ? 0.2095 0.1458 0.2800 0.0098  -0.0078 0.0110  136  PRO   B CA  
5908 C  C   . PRO   B 136 ? 0.1893 0.1350 0.2832 0.0057  -0.0011 0.0061  136  PRO   B C   
5909 O  O   . PRO   B 136 ? 0.1687 0.1311 0.2763 0.0058  -0.0047 0.0144  136  PRO   B O   
5910 C  CB  . PRO   B 136 ? 0.2150 0.1702 0.2844 0.0274  -0.0130 -0.0037 136  PRO   B CB  
5911 C  CG  . PRO   B 136 ? 0.2360 0.1744 0.2979 0.0275  -0.0066 0.0017  136  PRO   B CG  
5912 C  CD  . PRO   B 136 ? 0.2428 0.1663 0.2912 0.0358  -0.0037 0.0162  136  PRO   B CD  
5920 N  N   . ILE   B 137 ? 0.1939 0.1283 0.2882 0.0110  -0.0050 0.0037  137  ILE   B N   
5921 C  CA  . ILE   B 137 ? 0.2026 0.1278 0.3114 -0.0068 -0.0082 -0.0007 137  ILE   B CA  
5922 C  C   . ILE   B 137 ? 0.1928 0.1344 0.3021 -0.0088 -0.0005 0.0103  137  ILE   B C   
5923 O  O   . ILE   B 137 ? 0.1807 0.1354 0.2855 -0.0121 -0.0031 0.0089  137  ILE   B O   
5924 C  CB  . ILE   B 137 ? 0.2327 0.1331 0.3514 -0.0085 -0.0122 0.0008  137  ILE   B CB  
5925 C  CG1 . ILE   B 137 ? 0.2599 0.1490 0.4033 0.0014  -0.0062 -0.0108 137  ILE   B CG1 
5926 C  CG2 . ILE   B 137 ? 0.2400 0.1390 0.3656 -0.0299 -0.0191 0.0043  137  ILE   B CG2 
5927 C  CD1 . ILE   B 137 ? 0.2815 0.1789 0.4420 0.0128  -0.0116 0.0009  137  ILE   B CD1 
5939 N  N   . HIS   B 138 ? 0.1990 0.1303 0.2967 -0.0068 0.0107  0.0097  138  HIS   B N   
5940 C  CA  . HIS   B 138 ? 0.2060 0.1435 0.2875 -0.0064 0.0288  0.0173  138  HIS   B CA  
5941 C  C   . HIS   B 138 ? 0.1872 0.1402 0.2730 -0.0093 0.0245  0.0260  138  HIS   B C   
5942 O  O   . HIS   B 138 ? 0.1785 0.1436 0.2858 -0.0053 0.0285  0.0317  138  HIS   B O   
5943 C  CB  . HIS   B 138 ? 0.2302 0.1565 0.2984 -0.0130 0.0467  0.0080  138  HIS   B CB  
5944 C  CG  . HIS   B 138 ? 0.2511 0.1697 0.3036 -0.0111 0.0585  0.0236  138  HIS   B CG  
5945 N  ND1 . HIS   B 138 ? 0.2633 0.1894 0.3267 -0.0040 0.0668  0.0212  138  HIS   B ND1 
5946 C  CD2 . HIS   B 138 ? 0.2652 0.1814 0.2893 -0.0123 0.0719  0.0132  138  HIS   B CD2 
5947 C  CE1 . HIS   B 138 ? 0.2646 0.1900 0.3190 -0.0030 0.0746  0.0228  138  HIS   B CE1 
5948 N  NE2 . HIS   B 138 ? 0.2703 0.1811 0.3001 0.0014  0.0769  0.0112  138  HIS   B NE2 
5956 N  N   . SER   B 139 ? 0.1835 0.1258 0.2649 -0.0005 0.0175  0.0130  139  SER   B N   
5957 C  CA  . SER   B 139 ? 0.1825 0.1208 0.2446 -0.0042 0.0168  0.0068  139  SER   B CA  
5958 C  C   . SER   B 139 ? 0.1568 0.1192 0.2408 -0.0092 0.0104  0.0044  139  SER   B C   
5959 O  O   . SER   B 139 ? 0.1568 0.1206 0.2434 -0.0041 0.0014  0.0132  139  SER   B O   
5960 C  CB  . SER   B 139 ? 0.1904 0.1186 0.2467 -0.0009 0.0086  0.0018  139  SER   B CB  
5961 O  OG  . SER   B 139 ? 0.1890 0.1286 0.2525 -0.0069 -0.0106 0.0198  139  SER   B OG  
5967 N  N   . LEU   B 140 ? 0.1563 0.1155 0.2436 -0.0087 0.0130  -0.0014 140  LEU   B N   
5968 C  CA  . LEU   B 140 ? 0.1562 0.1186 0.2516 -0.0060 0.0052  0.0072  140  LEU   B CA  
5969 C  C   . LEU   B 140 ? 0.1477 0.1231 0.2640 -0.0094 -0.0052 -0.0004 140  LEU   B C   
5970 O  O   . LEU   B 140 ? 0.1511 0.1254 0.2656 -0.0024 -0.0078 0.0060  140  LEU   B O   
5971 C  CB  . LEU   B 140 ? 0.1540 0.1167 0.2548 -0.0094 0.0135  0.0015  140  LEU   B CB  
5972 C  CG  . LEU   B 140 ? 0.1627 0.1238 0.2567 -0.0110 0.0013  0.0006  140  LEU   B CG  
5973 C  CD1 . LEU   B 140 ? 0.1760 0.1322 0.2693 -0.0132 0.0020  0.0058  140  LEU   B CD1 
5974 C  CD2 . LEU   B 140 ? 0.1773 0.1333 0.2632 -0.0073 0.0011  -0.0162 140  LEU   B CD2 
5986 N  N   . ARG   B 141 ? 0.1394 0.1253 0.2742 -0.0109 -0.0008 -0.0024 141  ARG   B N   
5987 C  CA  . ARG   B 141 ? 0.1468 0.1178 0.3125 -0.0170 0.0124  -0.0044 141  ARG   B CA  
5988 C  C   . ARG   B 141 ? 0.1439 0.1212 0.3053 -0.0151 0.0008  -0.0077 141  ARG   B C   
5989 O  O   . ARG   B 141 ? 0.1476 0.1250 0.3022 -0.0135 -0.0086 -0.0172 141  ARG   B O   
5990 C  CB  . ARG   B 141 ? 0.1636 0.1293 0.3382 -0.0209 0.0209  0.0011  141  ARG   B CB  
5991 C  CG  . ARG   B 141 ? 0.1970 0.1589 0.3645 -0.0269 0.0258  0.0104  141  ARG   B CG  
5992 C  CD  . ARG   B 141 ? 0.2424 0.1843 0.3683 -0.0149 0.0157  -0.0054 141  ARG   B CD  
5993 N  NE  . ARG   B 141 ? 0.2639 0.1834 0.3596 -0.0302 0.0276  -0.0132 141  ARG   B NE  
5994 C  CZ  . ARG   B 141 ? 0.2730 0.1681 0.3431 -0.0261 0.0374  -0.0244 141  ARG   B CZ  
5995 N  NH1 . ARG   B 141 ? 0.2852 0.1648 0.3412 -0.0207 0.0366  -0.0260 141  ARG   B NH1 
5996 N  NH2 . ARG   B 141 ? 0.2839 0.1833 0.3506 -0.0165 0.0275  -0.0128 141  ARG   B NH2 
6010 N  N   . VAL   B 142 ? 0.1478 0.1185 0.2872 -0.0102 0.0151  -0.0120 142  VAL   B N   
6011 C  CA  . VAL   B 142 ? 0.1436 0.1208 0.2855 -0.0089 0.0146  -0.0069 142  VAL   B CA  
6012 C  C   . VAL   B 142 ? 0.1411 0.1199 0.2802 -0.0006 0.0123  -0.0099 142  VAL   B C   
6013 O  O   . VAL   B 142 ? 0.1495 0.1178 0.2990 -0.0018 0.0078  -0.0044 142  VAL   B O   
6014 C  CB  . VAL   B 142 ? 0.1500 0.1318 0.2900 -0.0048 0.0218  0.0020  142  VAL   B CB  
6015 C  CG1 . VAL   B 142 ? 0.1603 0.1223 0.2930 0.0042  0.0223  -0.0026 142  VAL   B CG1 
6016 C  CG2 . VAL   B 142 ? 0.1732 0.1344 0.2963 0.0002  0.0178  0.0091  142  VAL   B CG2 
6026 N  N   . CYS   B 143 ? 0.1398 0.1190 0.2498 -0.0045 -0.0006 0.0039  143  CYS   B N   
6027 C  CA  . CYS   B 143 ? 0.1374 0.1190 0.2498 -0.0080 -0.0039 0.0001  143  CYS   B CA  
6028 C  C   . CYS   B 143 ? 0.1344 0.1236 0.2471 -0.0107 0.0008  -0.0036 143  CYS   B C   
6029 O  O   . CYS   B 143 ? 0.1401 0.1272 0.2393 -0.0038 -0.0119 -0.0002 143  CYS   B O   
6030 C  CB  . CYS   B 143 ? 0.1462 0.1277 0.2527 -0.0106 -0.0025 -0.0007 143  CYS   B CB  
6031 S  SG  . CYS   B 143 ? 0.1489 0.1430 0.2450 -0.0059 -0.0035 0.0039  143  CYS   B SG  
6037 N  N   . VAL   B 144 ? 0.1383 0.1274 0.2697 -0.0108 -0.0015 -0.0166 144  VAL   B N   
6038 C  CA  . VAL   B 144 ? 0.1446 0.1332 0.3043 -0.0192 -0.0161 -0.0239 144  VAL   B CA  
6039 C  C   . VAL   B 144 ? 0.1432 0.1347 0.2984 -0.0123 -0.0179 -0.0047 144  VAL   B C   
6040 O  O   . VAL   B 144 ? 0.1549 0.1566 0.3093 -0.0012 -0.0149 0.0206  144  VAL   B O   
6041 C  CB  . VAL   B 144 ? 0.1690 0.1545 0.3638 -0.0129 -0.0203 -0.0315 144  VAL   B CB  
6042 C  CG1 . VAL   B 144 ? 0.1896 0.1973 0.3993 -0.0156 -0.0314 -0.0263 144  VAL   B CG1 
6043 C  CG2 . VAL   B 144 ? 0.1814 0.1506 0.3528 -0.0057 -0.0301 -0.0491 144  VAL   B CG2 
6053 N  N   . ASP   B 145 ? 0.1435 0.1282 0.3095 -0.0109 -0.0125 -0.0138 145  ASP   B N   
6054 C  CA  . ASP   B 145 ? 0.1443 0.1341 0.3248 -0.0051 -0.0052 -0.0096 145  ASP   B CA  
6055 C  C   . ASP   B 145 ? 0.1428 0.1393 0.3091 -0.0089 -0.0018 -0.0084 145  ASP   B C   
6056 O  O   . ASP   B 145 ? 0.1465 0.1552 0.3653 -0.0119 0.0048  -0.0235 145  ASP   B O   
6057 C  CB  . ASP   B 145 ? 0.1604 0.1455 0.3709 -0.0186 0.0041  0.0002  145  ASP   B CB  
6058 C  CG  . ASP   B 145 ? 0.1729 0.1481 0.4179 -0.0248 0.0184  -0.0019 145  ASP   B CG  
6059 O  OD1 . ASP   B 145 ? 0.1706 0.1545 0.4316 -0.0262 -0.0068 -0.0190 145  ASP   B OD1 
6060 O  OD2 . ASP   B 145 ? 0.2032 0.1545 0.4540 -0.0310 0.0395  0.0078  145  ASP   B OD2 
6065 N  N   . THR   B 146 ? 0.1322 0.1265 0.2729 -0.0094 -0.0090 -0.0002 146  THR   B N   
6066 C  CA  . THR   B 146 ? 0.1420 0.1237 0.2592 -0.0059 0.0043  -0.0062 146  THR   B CA  
6067 C  C   . THR   B 146 ? 0.1434 0.1204 0.2514 -0.0085 -0.0030 -0.0053 146  THR   B C   
6068 O  O   . THR   B 146 ? 0.1512 0.1233 0.2580 -0.0035 -0.0107 -0.0049 146  THR   B O   
6069 C  CB  . THR   B 146 ? 0.1462 0.1234 0.2595 -0.0010 0.0076  0.0005  146  THR   B CB  
6070 O  OG1 . THR   B 146 ? 0.1469 0.1238 0.2686 -0.0050 0.0112  0.0079  146  THR   B OG1 
6071 C  CG2 . THR   B 146 ? 0.1591 0.1308 0.2501 -0.0038 0.0117  -0.0022 146  THR   B CG2 
6079 N  N   . VAL   B 147 ? 0.1443 0.1262 0.2343 -0.0063 0.0055  0.0052  147  VAL   B N   
6080 C  CA  . VAL   B 147 ? 0.1466 0.1235 0.2231 -0.0123 -0.0144 -0.0002 147  VAL   B CA  
6081 C  C   . VAL   B 147 ? 0.1469 0.1260 0.2341 -0.0177 -0.0159 -0.0044 147  VAL   B C   
6082 O  O   . VAL   B 147 ? 0.1532 0.1367 0.2444 -0.0200 -0.0357 -0.0105 147  VAL   B O   
6083 C  CB  . VAL   B 147 ? 0.1505 0.1375 0.2102 -0.0109 -0.0128 -0.0011 147  VAL   B CB  
6084 C  CG1 . VAL   B 147 ? 0.1510 0.1504 0.1997 -0.0121 -0.0112 0.0033  147  VAL   B CG1 
6085 C  CG2 . VAL   B 147 ? 0.1588 0.1345 0.2133 -0.0113 -0.0078 -0.0040 147  VAL   B CG2 
6095 N  N   . ARG   B 148 ? 0.1466 0.1310 0.2305 -0.0143 -0.0233 -0.0080 148  ARG   B N   
6096 C  CA  . ARG   B 148 ? 0.1569 0.1341 0.2295 -0.0045 -0.0282 -0.0139 148  ARG   B CA  
6097 C  C   . ARG   B 148 ? 0.1598 0.1449 0.2215 -0.0089 -0.0367 -0.0067 148  ARG   B C   
6098 O  O   . ARG   B 148 ? 0.1780 0.1739 0.2209 -0.0247 -0.0408 0.0007  148  ARG   B O   
6099 C  CB  . ARG   B 148 ? 0.1606 0.1434 0.2375 -0.0021 -0.0339 -0.0149 148  ARG   B CB  
6100 C  CG  . ARG   B 148 ? 0.1585 0.1536 0.2535 -0.0088 -0.0343 -0.0327 148  ARG   B CG  
6101 C  CD  . ARG   B 148 ? 0.1656 0.1730 0.2596 0.0056  -0.0360 -0.0328 148  ARG   B CD  
6102 N  NE  . ARG   B 148 ? 0.1649 0.1716 0.2500 0.0252  -0.0397 -0.0308 148  ARG   B NE  
6103 C  CZ  . ARG   B 148 ? 0.1561 0.1681 0.2278 0.0149  -0.0354 -0.0237 148  ARG   B CZ  
6104 N  NH1 . ARG   B 148 ? 0.1499 0.1725 0.2331 -0.0017 -0.0115 -0.0192 148  ARG   B NH1 
6105 N  NH2 . ARG   B 148 ? 0.1810 0.1527 0.2178 0.0146  -0.0294 -0.0125 148  ARG   B NH2 
6119 N  N   . THR   B 149 ? 0.1628 0.1377 0.2190 -0.0100 -0.0374 -0.0009 149  THR   B N   
6120 C  CA  . THR   B 149 ? 0.1677 0.1352 0.2123 -0.0128 -0.0353 0.0024  149  THR   B CA  
6121 C  C   . THR   B 149 ? 0.1695 0.1369 0.1985 -0.0137 -0.0335 0.0015  149  THR   B C   
6122 O  O   . THR   B 149 ? 0.1730 0.1367 0.2120 -0.0191 -0.0191 0.0027  149  THR   B O   
6123 C  CB  . THR   B 149 ? 0.1680 0.1331 0.2113 -0.0154 -0.0328 -0.0028 149  THR   B CB  
6124 O  OG1 . THR   B 149 ? 0.1717 0.1425 0.1995 -0.0222 -0.0415 0.0007  149  THR   B OG1 
6125 C  CG2 . THR   B 149 ? 0.1750 0.1364 0.2195 -0.0053 -0.0263 -0.0010 149  THR   B CG2 
6133 N  N   . ASN   B 150 ? 0.1771 0.1366 0.1916 -0.0161 -0.0376 -0.0019 150  ASN   B N   
6134 C  CA  . ASN   B 150 ? 0.1811 0.1516 0.1867 -0.0199 -0.0315 -0.0068 150  ASN   B CA  
6135 C  C   . ASN   B 150 ? 0.1671 0.1451 0.1853 -0.0110 -0.0322 -0.0006 150  ASN   B C   
6136 O  O   . ASN   B 150 ? 0.1764 0.1455 0.2091 -0.0272 -0.0504 -0.0039 150  ASN   B O   
6137 C  CB  . ASN   B 150 ? 0.2058 0.1866 0.2017 -0.0210 -0.0502 0.0051  150  ASN   B CB  
6138 C  CG  . ASN   B 150 ? 0.2326 0.2254 0.2434 -0.0215 -0.0537 0.0307  150  ASN   B CG  
6139 O  OD1 . ASN   B 150 ? 0.2441 0.2453 0.2662 -0.0330 -0.0695 0.0269  150  ASN   B OD1 
6140 N  ND2 . ASN   B 150 ? 0.2461 0.2458 0.2706 -0.0111 -0.0532 0.0643  150  ASN   B ND2 
6147 N  N   . VAL   B 151 ? 0.1575 0.1412 0.1900 -0.0172 -0.0326 0.0028  151  VAL   B N   
6148 C  CA  . VAL   B 151 ? 0.1565 0.1465 0.1991 -0.0248 -0.0337 0.0014  151  VAL   B CA  
6149 C  C   . VAL   B 151 ? 0.1595 0.1366 0.1955 -0.0284 -0.0354 -0.0063 151  VAL   B C   
6150 O  O   . VAL   B 151 ? 0.1706 0.1440 0.2140 -0.0272 -0.0186 -0.0113 151  VAL   B O   
6151 C  CB  . VAL   B 151 ? 0.1782 0.1589 0.2164 -0.0089 -0.0254 0.0017  151  VAL   B CB  
6152 C  CG1 . VAL   B 151 ? 0.1848 0.1617 0.2366 -0.0149 -0.0214 -0.0114 151  VAL   B CG1 
6153 C  CG2 . VAL   B 151 ? 0.1910 0.1760 0.2126 0.0051  -0.0329 0.0047  151  VAL   B CG2 
6163 N  N   . TYR   B 152 ? 0.1591 0.1290 0.1839 -0.0237 -0.0349 -0.0043 152  TYR   B N   
6164 C  CA  . TYR   B 152 ? 0.1611 0.1432 0.1723 -0.0247 -0.0164 -0.0033 152  TYR   B CA  
6165 C  C   . TYR   B 152 ? 0.1576 0.1298 0.1734 -0.0194 -0.0148 -0.0117 152  TYR   B C   
6166 O  O   . TYR   B 152 ? 0.1702 0.1319 0.1825 -0.0247 -0.0175 -0.0022 152  TYR   B O   
6167 C  CB  . TYR   B 152 ? 0.1731 0.1608 0.1790 -0.0205 -0.0221 0.0057  152  TYR   B CB  
6168 C  CG  . TYR   B 152 ? 0.1866 0.1657 0.1739 -0.0418 -0.0303 0.0049  152  TYR   B CG  
6169 C  CD1 . TYR   B 152 ? 0.1961 0.1763 0.1710 -0.0355 -0.0420 0.0067  152  TYR   B CD1 
6170 C  CD2 . TYR   B 152 ? 0.2105 0.1862 0.1850 -0.0367 -0.0230 -0.0051 152  TYR   B CD2 
6171 C  CE1 . TYR   B 152 ? 0.2154 0.1950 0.1805 -0.0285 -0.0475 0.0175  152  TYR   B CE1 
6172 C  CE2 . TYR   B 152 ? 0.2214 0.2066 0.1833 -0.0307 -0.0311 -0.0104 152  TYR   B CE2 
6173 C  CZ  . TYR   B 152 ? 0.2233 0.2161 0.1726 -0.0302 -0.0568 0.0089  152  TYR   B CZ  
6174 O  OH  . TYR   B 152 ? 0.2467 0.2526 0.2075 -0.0169 -0.0508 0.0078  152  TYR   B OH  
6184 N  N   . LEU   B 153 ? 0.1552 0.1300 0.1850 -0.0283 -0.0162 -0.0043 153  LEU   B N   
6185 C  CA  . LEU   B 153 ? 0.1553 0.1259 0.1680 -0.0215 -0.0155 -0.0053 153  LEU   B CA  
6186 C  C   . LEU   B 153 ? 0.1612 0.1260 0.1646 -0.0279 -0.0086 -0.0099 153  LEU   B C   
6187 O  O   . LEU   B 153 ? 0.1726 0.1505 0.1819 -0.0192 -0.0196 -0.0280 153  LEU   B O   
6188 C  CB  . LEU   B 153 ? 0.1626 0.1233 0.1869 -0.0258 -0.0048 -0.0081 153  LEU   B CB  
6189 C  CG  . LEU   B 153 ? 0.1563 0.1326 0.2086 -0.0244 -0.0052 -0.0014 153  LEU   B CG  
6190 C  CD1 . LEU   B 153 ? 0.1609 0.1413 0.2200 -0.0273 -0.0021 0.0118  153  LEU   B CD1 
6191 C  CD2 . LEU   B 153 ? 0.1590 0.1469 0.2104 -0.0291 0.0012  0.0036  153  LEU   B CD2 
6203 N  N   . ALA   B 154 ? 0.1577 0.1242 0.1744 -0.0074 -0.0208 -0.0102 154  ALA   B N   
6204 C  CA  . ALA   B 154 ? 0.1666 0.1343 0.1994 -0.0012 -0.0235 -0.0173 154  ALA   B CA  
6205 C  C   . ALA   B 154 ? 0.1743 0.1381 0.2135 0.0007  -0.0256 -0.0243 154  ALA   B C   
6206 O  O   . ALA   B 154 ? 0.2055 0.1407 0.2381 0.0039  -0.0146 -0.0132 154  ALA   B O   
6207 C  CB  . ALA   B 154 ? 0.1614 0.1532 0.2231 -0.0056 -0.0169 -0.0266 154  ALA   B CB  
6213 N  N   . VAL   B 155 ? 0.1463 0.1307 0.2108 -0.0052 -0.0084 -0.0144 155  VAL   B N   
6214 C  CA  . VAL   B 155 ? 0.1402 0.1319 0.2334 0.0015  -0.0143 -0.0064 155  VAL   B CA  
6215 C  C   . VAL   B 155 ? 0.1446 0.1381 0.2391 -0.0013 -0.0129 -0.0177 155  VAL   B C   
6216 O  O   . VAL   B 155 ? 0.1600 0.1559 0.2695 0.0077  -0.0152 -0.0362 155  VAL   B O   
6217 C  CB  . VAL   B 155 ? 0.1491 0.1469 0.2603 -0.0029 -0.0145 0.0022  155  VAL   B CB  
6218 C  CG1 . VAL   B 155 ? 0.1551 0.1394 0.2595 -0.0107 -0.0172 0.0041  155  VAL   B CG1 
6219 C  CG2 . VAL   B 155 ? 0.1434 0.1606 0.2919 -0.0067 -0.0103 0.0287  155  VAL   B CG2 
6229 N  N   . PHE   B 156 ? 0.1337 0.1450 0.2574 0.0030  -0.0046 -0.0095 156  PHE   B N   
6230 C  CA  . PHE   B 156 ? 0.1413 0.1509 0.2857 0.0039  -0.0087 -0.0123 156  PHE   B CA  
6231 C  C   . PHE   B 156 ? 0.1414 0.1567 0.3222 0.0106  -0.0184 -0.0345 156  PHE   B C   
6232 O  O   . PHE   B 156 ? 0.1668 0.1726 0.3461 0.0236  -0.0057 -0.0418 156  PHE   B O   
6233 C  CB  . PHE   B 156 ? 0.1478 0.1452 0.2832 0.0009  -0.0132 -0.0056 156  PHE   B CB  
6234 C  CG  . PHE   B 156 ? 0.1438 0.1562 0.2867 0.0025  -0.0153 0.0092  156  PHE   B CG  
6235 C  CD1 . PHE   B 156 ? 0.1534 0.1832 0.3205 0.0076  -0.0118 0.0376  156  PHE   B CD1 
6236 C  CD2 . PHE   B 156 ? 0.1513 0.1623 0.2775 0.0048  -0.0199 0.0118  156  PHE   B CD2 
6237 C  CE1 . PHE   B 156 ? 0.1560 0.1994 0.3363 0.0094  -0.0046 0.0423  156  PHE   B CE1 
6238 C  CE2 . PHE   B 156 ? 0.1567 0.1897 0.3059 0.0136  -0.0150 0.0181  156  PHE   B CE2 
6239 C  CZ  . PHE   B 156 ? 0.1495 0.2002 0.3291 0.0180  -0.0210 0.0278  156  PHE   B CZ  
6249 N  N   . ASP   B 157 ? 0.1434 0.1465 0.3411 0.0115  -0.0309 -0.0214 157  ASP   B N   
6250 C  CA  . ASP   B 157 ? 0.1562 0.1514 0.3689 0.0092  -0.0246 -0.0212 157  ASP   B CA  
6251 C  C   . ASP   B 157 ? 0.1553 0.1467 0.3640 0.0096  -0.0210 -0.0468 157  ASP   B C   
6252 O  O   . ASP   B 157 ? 0.1394 0.1508 0.3552 0.0091  -0.0220 -0.0375 157  ASP   B O   
6253 C  CB  . ASP   B 157 ? 0.1748 0.1666 0.3733 0.0014  -0.0419 -0.0108 157  ASP   B CB  
6254 C  CG  . ASP   B 157 ? 0.2152 0.1803 0.3965 0.0017  -0.0303 -0.0061 157  ASP   B CG  
6255 O  OD1 . ASP   B 157 ? 0.2245 0.1772 0.4090 0.0194  -0.0235 -0.0008 157  ASP   B OD1 
6256 O  OD2 . ASP   B 157 ? 0.2483 0.1950 0.4215 -0.0058 -0.0165 -0.0038 157  ASP   B OD2 
6261 N  N   . LYS   B 158 ? 0.1547 0.1807 0.3700 0.0085  -0.0161 -0.0678 158  LYS   B N   
6262 C  CA  . LYS   B 158 ? 0.1685 0.1932 0.3855 0.0078  -0.0105 -0.0842 158  LYS   B CA  
6263 C  C   . LYS   B 158 ? 0.1734 0.1772 0.4059 0.0101  -0.0119 -0.0701 158  LYS   B C   
6264 O  O   . LYS   B 158 ? 0.1739 0.1747 0.4089 0.0003  -0.0106 -0.0801 158  LYS   B O   
6265 C  CB  . LYS   B 158 ? 0.1942 0.2383 0.3902 0.0060  -0.0050 -0.1106 158  LYS   B CB  
6266 C  CG  . LYS   B 158 ? 0.2297 0.2844 0.3959 0.0129  0.0088  -0.1259 158  LYS   B CG  
6267 C  CD  . LYS   B 158 ? 0.2516 0.3290 0.4143 0.0132  0.0138  -0.1198 158  LYS   B CD  
6268 C  CE  . LYS   B 158 ? 0.2741 0.3654 0.4336 0.0161  0.0119  -0.1154 158  LYS   B CE  
6269 N  NZ  . LYS   B 158 ? 0.2696 0.3783 0.4367 0.0142  0.0088  -0.1144 158  LYS   B NZ  
6283 N  N   . ASN   B 159 ? 0.1716 0.1714 0.4259 0.0080  -0.0209 -0.0565 159  ASN   B N   
6284 C  CA  . ASN   B 159 ? 0.1871 0.1637 0.4385 0.0159  -0.0322 -0.0507 159  ASN   B CA  
6285 C  C   . ASN   B 159 ? 0.1705 0.1531 0.4178 0.0108  -0.0407 -0.0458 159  ASN   B C   
6286 O  O   . ASN   B 159 ? 0.1704 0.1429 0.4251 -0.0016 -0.0467 -0.0283 159  ASN   B O   
6287 C  CB  . ASN   B 159 ? 0.2040 0.1689 0.4676 0.0213  -0.0363 -0.0469 159  ASN   B CB  
6288 C  CG  . ASN   B 159 ? 0.2306 0.1900 0.4955 0.0278  -0.0501 -0.0571 159  ASN   B CG  
6289 O  OD1 . ASN   B 159 ? 0.2491 0.2001 0.5033 0.0314  -0.0453 -0.0725 159  ASN   B OD1 
6290 N  ND2 . ASN   B 159 ? 0.2291 0.2007 0.5137 0.0352  -0.0601 -0.0433 159  ASN   B ND2 
6297 N  N   . LEU   B 160 ? 0.1599 0.1520 0.3878 0.0121  -0.0497 -0.0379 160  LEU   B N   
6298 C  CA  . LEU   B 160 ? 0.1569 0.1543 0.3584 0.0066  -0.0391 -0.0235 160  LEU   B CA  
6299 C  C   . LEU   B 160 ? 0.1521 0.1415 0.3506 -0.0006 -0.0252 -0.0356 160  LEU   B C   
6300 O  O   . LEU   B 160 ? 0.1425 0.1430 0.3453 -0.0023 -0.0257 -0.0156 160  LEU   B O   
6301 C  CB  . LEU   B 160 ? 0.1564 0.1623 0.3385 0.0037  -0.0358 -0.0126 160  LEU   B CB  
6302 C  CG  . LEU   B 160 ? 0.1524 0.1732 0.3160 0.0031  -0.0346 0.0002  160  LEU   B CG  
6303 C  CD1 . LEU   B 160 ? 0.1640 0.1916 0.3179 -0.0049 -0.0105 0.0063  160  LEU   B CD1 
6304 C  CD2 . LEU   B 160 ? 0.1591 0.1766 0.3182 0.0156  -0.0313 -0.0101 160  LEU   B CD2 
6316 N  N   . TYR   B 161 ? 0.1480 0.1499 0.3482 -0.0044 -0.0144 -0.0425 161  TYR   B N   
6317 C  CA  . TYR   B 161 ? 0.1556 0.1471 0.3334 -0.0103 0.0045  -0.0521 161  TYR   B CA  
6318 C  C   . TYR   B 161 ? 0.1638 0.1399 0.3223 -0.0113 0.0073  -0.0358 161  TYR   B C   
6319 O  O   . TYR   B 161 ? 0.1668 0.1412 0.3077 -0.0198 0.0061  -0.0305 161  TYR   B O   
6320 C  CB  . TYR   B 161 ? 0.1679 0.1614 0.3344 -0.0192 0.0242  -0.0564 161  TYR   B CB  
6321 C  CG  . TYR   B 161 ? 0.1920 0.1628 0.3273 -0.0264 0.0310  -0.0584 161  TYR   B CG  
6322 C  CD1 . TYR   B 161 ? 0.1957 0.1597 0.3217 -0.0350 0.0302  -0.0584 161  TYR   B CD1 
6323 C  CD2 . TYR   B 161 ? 0.2127 0.1717 0.3200 -0.0260 0.0257  -0.0598 161  TYR   B CD2 
6324 C  CE1 . TYR   B 161 ? 0.2137 0.1766 0.3255 -0.0357 0.0355  -0.0610 161  TYR   B CE1 
6325 C  CE2 . TYR   B 161 ? 0.2301 0.1868 0.3271 -0.0279 0.0270  -0.0593 161  TYR   B CE2 
6326 C  CZ  . TYR   B 161 ? 0.2266 0.1886 0.3265 -0.0398 0.0281  -0.0493 161  TYR   B CZ  
6327 O  OH  . TYR   B 161 ? 0.2554 0.2135 0.3490 -0.0415 0.0324  -0.0431 161  TYR   B OH  
6337 N  N   . ASP   B 162 ? 0.1708 0.1424 0.3355 -0.0141 -0.0086 -0.0485 162  ASP   B N   
6338 C  CA  . ASP   B 162 ? 0.1803 0.1535 0.3371 -0.0105 -0.0049 -0.0489 162  ASP   B CA  
6339 C  C   . ASP   B 162 ? 0.1744 0.1433 0.3229 -0.0136 -0.0133 -0.0454 162  ASP   B C   
6340 O  O   . ASP   B 162 ? 0.1847 0.1469 0.3185 -0.0200 -0.0312 -0.0306 162  ASP   B O   
6341 C  CB  . ASP   B 162 ? 0.1981 0.1664 0.3635 0.0000  -0.0031 -0.0631 162  ASP   B CB  
6342 C  CG  . ASP   B 162 ? 0.2022 0.1879 0.3755 0.0080  -0.0092 -0.0772 162  ASP   B CG  
6343 O  OD1 . ASP   B 162 ? 0.1982 0.2110 0.3602 0.0037  -0.0006 -0.0691 162  ASP   B OD1 
6344 O  OD2 . ASP   B 162 ? 0.2188 0.2116 0.4131 0.0248  -0.0018 -0.0764 162  ASP   B OD2 
6349 N  N   . LYS   B 163 ? 0.1700 0.1356 0.3156 -0.0082 -0.0303 -0.0352 163  LYS   B N   
6350 C  CA  . LYS   B 163 ? 0.1831 0.1438 0.3317 -0.0191 -0.0268 -0.0166 163  LYS   B CA  
6351 C  C   . LYS   B 163 ? 0.1540 0.1354 0.3122 -0.0188 -0.0258 -0.0047 163  LYS   B C   
6352 O  O   . LYS   B 163 ? 0.1531 0.1469 0.3355 -0.0255 -0.0294 -0.0037 163  LYS   B O   
6353 C  CB  . LYS   B 163 ? 0.2369 0.1795 0.3779 -0.0068 -0.0332 0.0080  163  LYS   B CB  
6354 C  CG  . LYS   B 163 ? 0.3089 0.2669 0.4415 -0.0118 -0.0205 0.0148  163  LYS   B CG  
6355 C  CD  . LYS   B 163 ? 0.3720 0.3397 0.5057 -0.0230 -0.0196 0.0116  163  LYS   B CD  
6356 C  CE  . LYS   B 163 ? 0.4160 0.3961 0.5492 -0.0332 -0.0194 0.0145  163  LYS   B CE  
6357 N  NZ  . LYS   B 163 ? 0.4484 0.4484 0.5769 -0.0394 -0.0175 0.0135  163  LYS   B NZ  
6371 N  N   . LEU   B 164 ? 0.1425 0.1319 0.2939 -0.0112 -0.0175 -0.0051 164  LEU   B N   
6372 C  CA  . LEU   B 164 ? 0.1468 0.1299 0.2760 -0.0112 -0.0234 -0.0002 164  LEU   B CA  
6373 C  C   . LEU   B 164 ? 0.1515 0.1363 0.2767 -0.0170 -0.0295 0.0000  164  LEU   B C   
6374 O  O   . LEU   B 164 ? 0.1513 0.1564 0.2859 -0.0167 -0.0244 0.0008  164  LEU   B O   
6375 C  CB  . LEU   B 164 ? 0.1437 0.1313 0.2653 -0.0081 -0.0181 0.0022  164  LEU   B CB  
6376 C  CG  . LEU   B 164 ? 0.1547 0.1487 0.2767 -0.0079 -0.0164 0.0074  164  LEU   B CG  
6377 C  CD1 . LEU   B 164 ? 0.1585 0.1443 0.2795 -0.0153 -0.0270 0.0051  164  LEU   B CD1 
6378 C  CD2 . LEU   B 164 ? 0.1736 0.1865 0.2887 -0.0030 0.0036  -0.0065 164  LEU   B CD2 
6390 N  N   . VAL   B 165 ? 0.1812 0.1398 0.2947 -0.0188 -0.0326 -0.0074 165  VAL   B N   
6391 C  CA  . VAL   B 165 ? 0.2137 0.1539 0.2985 -0.0284 -0.0542 -0.0016 165  VAL   B CA  
6392 C  C   . VAL   B 165 ? 0.2445 0.1639 0.3202 -0.0410 -0.0822 -0.0057 165  VAL   B C   
6393 O  O   . VAL   B 165 ? 0.2641 0.1824 0.3279 -0.0452 -0.0850 0.0018  165  VAL   B O   
6394 C  CB  . VAL   B 165 ? 0.2339 0.1703 0.2944 -0.0138 -0.0319 -0.0134 165  VAL   B CB  
6395 C  CG1 . VAL   B 165 ? 0.2531 0.1836 0.3244 -0.0168 -0.0230 -0.0110 165  VAL   B CG1 
6396 C  CG2 . VAL   B 165 ? 0.2308 0.1768 0.2930 -0.0136 -0.0223 -0.0165 165  VAL   B CG2 
6406 N  N   . SER   B 166 ? 0.2530 0.1559 0.3535 -0.0393 -0.0915 -0.0211 166  SER   B N   
6407 C  CA  . SER   B 166 ? 0.2477 0.1595 0.4067 -0.0418 -0.0739 -0.0290 166  SER   B CA  
6408 C  C   . SER   B 166 ? 0.2327 0.1675 0.4205 -0.0408 -0.0743 -0.0084 166  SER   B C   
6409 O  O   . SER   B 166 ? 0.2310 0.1884 0.4421 -0.0473 -0.0906 -0.0294 166  SER   B O   
6410 C  CB  . SER   B 166 ? 0.2415 0.1682 0.4471 -0.0315 -0.0653 -0.0381 166  SER   B CB  
6411 O  OG  . SER   B 166 ? 0.2279 0.1643 0.4655 -0.0164 -0.0652 -0.0197 166  SER   B OG  
6417 N  N   . SER   B 167 ? 0.2158 0.1622 0.3894 -0.0380 -0.0767 0.0289  167  SER   B N   
6418 C  CA  . SER   B 167 ? 0.2064 0.1660 0.3846 -0.0316 -0.0554 0.0315  167  SER   B CA  
6419 C  C   . SER   B 167 ? 0.1976 0.1758 0.3718 -0.0413 -0.0559 0.0425  167  SER   B C   
6420 O  O   . SER   B 167 ? 0.1965 0.1877 0.3687 -0.0434 -0.0508 0.0326  167  SER   B O   
6421 C  CB  . SER   B 167 ? 0.1950 0.1710 0.3808 -0.0351 -0.0331 0.0243  167  SER   B CB  
6422 O  OG  . SER   B 167 ? 0.1880 0.1841 0.3660 -0.0209 -0.0159 0.0263  167  SER   B OG  
6428 N  N   . PHE   B 168 ? 0.1995 0.1731 0.3655 -0.0397 -0.0465 0.0484  168  PHE   B N   
6429 C  CA  . PHE   B 168 ? 0.2086 0.1693 0.3432 -0.0439 -0.0432 0.0401  168  PHE   B CA  
6430 C  C   . PHE   B 168 ? 0.1772 0.1588 0.2967 -0.0263 -0.0242 0.0201  168  PHE   B C   
6431 O  O   . PHE   B 168 ? 0.2094 0.1474 0.3011 -0.0046 -0.0211 0.0023  168  PHE   B O   
6432 C  CB  . PHE   B 168 ? 0.2212 0.1743 0.3469 -0.0572 -0.0539 0.0525  168  PHE   B CB  
6433 C  CG  . PHE   B 168 ? 0.2439 0.1623 0.3365 -0.0598 -0.0543 0.0336  168  PHE   B CG  
6434 C  CD1 . PHE   B 168 ? 0.2736 0.1725 0.3473 -0.0529 -0.0606 0.0233  168  PHE   B CD1 
6435 C  CD2 . PHE   B 168 ? 0.2318 0.1515 0.3292 -0.0564 -0.0562 0.0385  168  PHE   B CD2 
6436 C  CE1 . PHE   B 168 ? 0.2856 0.1782 0.3455 -0.0325 -0.0565 0.0260  168  PHE   B CE1 
6437 C  CE2 . PHE   B 168 ? 0.2610 0.1666 0.3432 -0.0349 -0.0630 0.0177  168  PHE   B CE2 
6438 C  CZ  . PHE   B 168 ? 0.2764 0.1584 0.3438 -0.0225 -0.0651 0.0361  168  PHE   B CZ  
6448 N  N   . LEU   B 169 ? 0.1774 0.1686 0.2932 -0.0045 -0.0078 0.0069  169  LEU   B N   
6449 C  CA  . LEU   B 169 ? 0.1992 0.1994 0.3162 -0.0093 -0.0053 -0.0287 169  LEU   B CA  
6450 C  C   . LEU   B 169 ? 0.2297 0.2214 0.3630 0.0069  -0.0034 -0.0643 169  LEU   B C   
6451 O  O   . LEU   B 169 ? 0.2521 0.2438 0.4134 0.0027  -0.0041 -0.0861 169  LEU   B O   
6452 C  CB  . LEU   B 169 ? 0.2210 0.2418 0.3252 -0.0159 -0.0180 0.0015  169  LEU   B CB  
6453 C  CG  . LEU   B 169 ? 0.2640 0.2844 0.3650 -0.0027 -0.0151 0.0152  169  LEU   B CG  
6454 C  CD1 . LEU   B 169 ? 0.2816 0.3051 0.3667 -0.0045 -0.0232 0.0336  169  LEU   B CD1 
6455 C  CD2 . LEU   B 169 ? 0.2591 0.2916 0.3673 0.0161  0.0003  0.0045  169  LEU   B CD2 
6456 O  OXT . LEU   B 169 ? 0.2514 0.2341 0.3628 0.0354  -0.0005 -0.0628 169  LEU   B OXT 
6468 N  N2  B A1BAS C .   ? 0.1959 0.2504 0.1844 0.0043  0.0040  0.0355  201  A1BAS A N2  
6469 C  C3  B A1BAS C .   ? 0.1920 0.2449 0.1748 0.0104  0.0060  0.0392  201  A1BAS A C3  
6470 C  C6  B A1BAS C .   ? 0.2124 0.2589 0.2047 -0.0007 -0.0079 0.0246  201  A1BAS A C6  
6471 C  C9  B A1BAS C .   ? 0.2610 0.3050 0.2675 -0.0187 -0.0150 -0.0133 201  A1BAS A C9  
6472 C  C1  B A1BAS C .   ? 0.2038 0.2512 0.1948 0.0135  0.0083  0.0375  201  A1BAS A C1  
6473 C  C10 B A1BAS C .   ? 0.2619 0.3054 0.2663 -0.0177 -0.0106 -0.0131 201  A1BAS A C10 
6474 C  C11 B A1BAS C .   ? 0.1999 0.2508 0.1850 0.0076  -0.0008 0.0316  201  A1BAS A C11 
6475 C  C2  B A1BAS C .   ? 0.1994 0.2490 0.1843 0.0097  0.0089  0.0366  201  A1BAS A C2  
6476 C  C4  B A1BAS C .   ? 0.1938 0.2480 0.1783 0.0094  0.0013  0.0374  201  A1BAS A C4  
6477 C  C5  B A1BAS C .   ? 0.1999 0.2551 0.1900 0.0018  -0.0026 0.0309  201  A1BAS A C5  
6478 C  C7  B A1BAS C .   ? 0.2493 0.2875 0.2565 -0.0097 -0.0174 0.0032  201  A1BAS A C7  
6479 C  C8  B A1BAS C .   ? 0.2607 0.3018 0.2673 -0.0152 -0.0144 -0.0092 201  A1BAS A C8  
6480 N  N1  B A1BAS C .   ? 0.1917 0.2450 0.1772 0.0120  0.0006  0.0404  201  A1BAS A N1  
6481 N  N3  B A1BAS C .   ? 0.2094 0.2567 0.2050 -0.0019 -0.0041 0.0251  201  A1BAS A N3  
6482 N  N4  B A1BAS C .   ? 0.2298 0.2702 0.2343 -0.0067 -0.0134 0.0134  201  A1BAS A N4  
6483 O  O1  B A1BAS C .   ? 0.2715 0.3053 0.2795 -0.0148 -0.0101 -0.0054 201  A1BAS A O1  
6500 N  N2  C A1BAS D .   ? 0.1629 0.1756 0.1712 0.0171  0.0168  0.0206  202  A1BAS A N2  
6501 C  C3  C A1BAS D .   ? 0.1445 0.1701 0.1480 0.0052  0.0059  0.0341  202  A1BAS A C3  
6502 C  C6  C A1BAS D .   ? 0.1857 0.1761 0.1903 0.0061  -0.0131 0.0021  202  A1BAS A C6  
6503 C  C9  C A1BAS D .   ? 0.2483 0.2102 0.2600 0.0027  -0.0214 -0.0279 202  A1BAS A C9  
6504 C  C1  C A1BAS D .   ? 0.1551 0.1750 0.1557 0.0010  -0.0249 0.0408  202  A1BAS A C1  
6505 C  C10 C A1BAS D .   ? 0.2460 0.2047 0.2651 0.0044  -0.0175 -0.0185 202  A1BAS A C10 
6506 C  C11 C A1BAS D .   ? 0.1608 0.1707 0.1606 0.0085  -0.0005 0.0186  202  A1BAS A C11 
6507 C  C2  C A1BAS D .   ? 0.1556 0.1729 0.1552 0.0028  -0.0030 0.0316  202  A1BAS A C2  
6508 C  C4  C A1BAS D .   ? 0.1543 0.1709 0.1549 0.0148  0.0116  0.0258  202  A1BAS A C4  
6509 C  C5  C A1BAS D .   ? 0.1731 0.1807 0.1850 0.0161  0.0028  0.0114  202  A1BAS A C5  
6510 C  C7  C A1BAS D .   ? 0.2354 0.1948 0.2552 0.0059  -0.0194 -0.0185 202  A1BAS A C7  
6511 C  C8  C A1BAS D .   ? 0.2455 0.2064 0.2687 0.0040  -0.0180 -0.0187 202  A1BAS A C8  
6512 N  N1  C A1BAS D .   ? 0.1488 0.1704 0.1482 0.0135  0.0090  0.0292  202  A1BAS A N1  
6513 N  N3  C A1BAS D .   ? 0.1871 0.1770 0.1959 0.0102  -0.0028 0.0043  202  A1BAS A N3  
6514 N  N4  C A1BAS D .   ? 0.2132 0.1844 0.2261 0.0045  -0.0192 -0.0107 202  A1BAS A N4  
6515 O  O1  C A1BAS D .   ? 0.2474 0.2087 0.2884 -0.0006 -0.0112 -0.0137 202  A1BAS A O1  
6532 CL CL  B CL    E .   ? 0.2056 0.1891 0.3150 -0.0036 -0.0418 -0.0440 203  CL    A CL  
6533 O  O   . HOH   F .   ? 0.5638 0.5859 0.4655 -0.1415 -0.1275 -0.0881 1301 HOH   A O   
6534 O  O   . HOH   F .   ? 0.7264 0.6895 0.3554 -0.1344 -0.0153 0.2364  1302 HOH   A O   
6535 O  O   A HOH   F .   ? 0.2963 0.2503 0.2757 -0.0303 -0.0600 0.0653  1303 HOH   A O   
6536 O  O   . HOH   F .   ? 0.2357 0.3360 0.3314 -0.0351 0.0324  0.1060  1304 HOH   A O   
6537 O  O   A HOH   F .   ? 0.3006 0.2692 0.2786 -0.0569 -0.0020 0.0562  1305 HOH   A O   
6538 O  O   . HOH   F .   ? 0.2186 0.2277 0.3193 0.0022  -0.0675 0.0184  1306 HOH   A O   
6539 O  O   . HOH   F .   ? 0.6610 0.4423 0.3784 0.1716  -0.1280 0.0839  1307 HOH   A O   
6540 O  O   . HOH   F .   ? 0.1577 0.4520 0.2868 -0.0144 0.0171  0.0988  1308 HOH   A O   
6541 O  O   . HOH   F .   ? 0.5415 0.2286 0.5550 0.0731  -0.0721 -0.0240 1309 HOH   A O   
6542 O  O   . HOH   F .   ? 0.5653 0.6015 0.4228 0.1978  -0.0248 -0.0495 1310 HOH   A O   
6543 O  O   . HOH   F .   ? 0.4107 0.5981 0.4871 0.1693  0.0993  -0.0643 1311 HOH   A O   
6544 O  O   . HOH   F .   ? 0.3248 0.3391 0.1910 -0.0732 0.0638  0.0314  1312 HOH   A O   
6545 O  O   A HOH   F .   ? 0.3333 0.5356 0.3260 -0.0698 0.0314  0.0712  1313 HOH   A O   
6546 O  O   . HOH   F .   ? 0.5771 0.6452 0.5048 0.0504  -0.0531 0.0926  1314 HOH   A O   
6547 O  O   . HOH   F .   ? 0.2081 0.1886 0.3869 -0.0423 0.0310  -0.0339 1315 HOH   A O   
6548 O  O   . HOH   F .   ? 0.5301 0.5423 0.3160 -0.1313 0.1603  0.0640  1316 HOH   A O   
6549 O  O   . HOH   F .   ? 0.1806 0.3345 0.3179 0.0399  -0.0226 -0.0073 1317 HOH   A O   
6550 O  O   . HOH   F .   ? 0.2051 0.3492 0.5045 -0.0485 0.0568  -0.1115 1318 HOH   A O   
6551 O  O   . HOH   F .   ? 0.4001 0.3722 0.3152 -0.0187 0.1389  0.0611  1319 HOH   A O   
6552 O  O   . HOH   F .   ? 0.3485 0.3234 0.2865 -0.1361 0.0040  0.0625  1320 HOH   A O   
6553 O  O   . HOH   F .   ? 0.2777 0.5675 0.4477 0.0110  -0.0519 0.0973  1321 HOH   A O   
6554 O  O   A HOH   F .   ? 0.3164 0.2726 0.3934 0.0039  0.1138  -0.0143 1322 HOH   A O   
6555 O  O   . HOH   F .   ? 0.9471 0.3291 0.5188 -0.0918 -0.1391 0.1015  1323 HOH   A O   
6556 O  O   . HOH   F .   ? 0.7867 0.5801 0.3748 -0.1431 0.0950  0.1804  1324 HOH   A O   
6557 O  O   . HOH   F .   ? 0.2549 0.2251 0.2825 0.0395  0.0163  0.0438  1325 HOH   A O   
6558 O  O   . HOH   F .   ? 0.1593 0.1530 0.2487 -0.0245 -0.0062 0.0065  1326 HOH   A O   
6559 O  O   . HOH   F .   ? 0.4807 0.3986 0.4708 -0.1886 -0.0597 0.1952  1327 HOH   A O   
6560 O  O   . HOH   F .   ? 0.4685 0.1945 0.4137 0.0398  -0.0928 0.0257  1328 HOH   A O   
6561 O  O   . HOH   F .   ? 0.1905 0.1890 0.2617 -0.0454 -0.0171 0.0617  1329 HOH   A O   
6562 O  O   B HOH   F .   ? 0.3515 0.4008 0.2776 0.2121  0.0935  0.1129  1330 HOH   A O   
6563 O  O   . HOH   F .   ? 0.3238 0.4016 0.4103 -0.1162 -0.0923 -0.0378 1331 HOH   A O   
6564 O  O   . HOH   F .   ? 0.2139 0.4709 0.4330 -0.0274 -0.0769 0.1983  1332 HOH   A O   
6565 O  O   B HOH   F .   ? 0.2507 0.2144 0.2125 -0.0231 -0.0046 -0.0392 1333 HOH   A O   
6566 O  O   . HOH   F .   ? 0.3522 0.4423 0.2621 -0.0127 0.0546  0.0571  1334 HOH   A O   
6567 O  O   . HOH   F .   ? 0.3001 0.3270 0.4355 -0.0876 0.1220  0.0020  1335 HOH   A O   
6568 O  O   . HOH   F .   ? 0.2421 0.4105 0.3996 0.0908  -0.0887 -0.0334 1336 HOH   A O   
6569 O  O   . HOH   F .   ? 0.5031 0.3897 0.3521 -0.1455 -0.1292 0.0211  1337 HOH   A O   
6570 O  O   . HOH   F .   ? 0.2562 0.6357 0.5457 -0.0446 0.0155  0.3060  1338 HOH   A O   
6571 O  O   . HOH   F .   ? 0.1511 0.2210 0.2253 0.0053  -0.0042 0.0568  1339 HOH   A O   
6572 O  O   . HOH   F .   ? 0.5842 0.6241 0.4610 0.0585  -0.1010 -0.0550 1340 HOH   A O   
6573 O  O   . HOH   F .   ? 0.2042 0.1761 0.2497 0.0251  -0.0434 -0.0057 1341 HOH   A O   
6574 O  O   A HOH   F .   ? 0.1369 0.3114 0.2214 0.0589  0.0459  0.0695  1342 HOH   A O   
6575 O  O   A HOH   F .   ? 0.2369 0.4755 0.2452 0.1182  0.0043  -0.0024 1343 HOH   A O   
6576 O  O   . HOH   F .   ? 0.2022 0.2746 0.4299 0.0315  0.0805  -0.0760 1344 HOH   A O   
6577 O  O   . HOH   F .   ? 0.6538 0.4045 0.3191 0.0085  0.0397  0.1061  1345 HOH   A O   
6578 O  O   . HOH   F .   ? 0.7097 0.5164 0.5569 0.1093  0.3103  -0.0789 1346 HOH   A O   
6579 O  O   . HOH   F .   ? 0.6535 0.6631 0.3880 -0.0171 -0.0335 0.1711  1347 HOH   A O   
6580 O  O   . HOH   F .   ? 0.1767 0.2220 0.1938 -0.0211 -0.0066 0.0667  1348 HOH   A O   
6581 O  O   . HOH   F .   ? 0.1880 0.2070 0.3788 0.0130  0.0814  -0.0287 1349 HOH   A O   
6582 O  O   . HOH   F .   ? 0.1494 0.1937 0.2729 0.0060  -0.0179 0.0075  1350 HOH   A O   
6583 O  O   . HOH   F .   ? 0.5655 0.3995 0.5645 -0.1369 -0.0718 0.1587  1351 HOH   A O   
6584 O  O   B HOH   F .   ? 0.1621 0.1396 0.2507 -0.0219 -0.0050 0.0057  1352 HOH   A O   
6585 O  O   A HOH   F .   ? 0.3756 0.1635 0.1565 -0.0159 0.0480  -0.0016 1353 HOH   A O   
6586 O  O   . HOH   F .   ? 0.3142 0.7678 0.5417 -0.0816 -0.0878 0.2722  1354 HOH   A O   
6587 O  O   . HOH   F .   ? 0.2087 0.3964 0.3610 -0.0165 -0.0040 0.0146  1355 HOH   A O   
6588 O  O   . HOH   F .   ? 0.1371 0.1312 0.1442 -0.0065 0.0093  0.0094  1356 HOH   A O   
6589 O  O   . HOH   F .   ? 0.2913 0.3593 0.2447 -0.0867 -0.0121 -0.0793 1357 HOH   A O   
6590 O  O   . HOH   F .   ? 0.3728 0.4283 0.4055 0.1932  0.0891  0.0661  1358 HOH   A O   
6591 O  O   B HOH   F .   ? 0.1914 0.3190 0.2302 0.0466  0.0028  0.0184  1359 HOH   A O   
6592 O  O   . HOH   F .   ? 0.2861 0.6813 0.5168 0.0468  -0.0893 0.1588  1360 HOH   A O   
6593 O  O   . HOH   F .   ? 0.4329 0.6837 0.5122 -0.0754 -0.1417 -0.0107 1361 HOH   A O   
6594 O  O   . HOH   F .   ? 0.3972 0.2094 0.2692 0.1050  0.0603  0.0251  1362 HOH   A O   
6595 O  O   . HOH   F .   ? 0.1483 0.1557 0.1555 -0.0095 -0.0065 -0.0052 1363 HOH   A O   
6596 O  O   . HOH   F .   ? 0.3162 0.3328 0.5355 -0.0758 -0.1474 -0.0699 1364 HOH   A O   
6597 O  O   . HOH   F .   ? 0.1422 0.1512 0.1969 0.0059  -0.0227 0.0004  1365 HOH   A O   
6598 O  O   . HOH   F .   ? 0.1602 0.1304 0.2564 -0.0116 0.0057  -0.0127 1366 HOH   A O   
6599 O  O   . HOH   F .   ? 0.1994 0.1907 0.2538 -0.0345 0.0184  0.0316  1367 HOH   A O   
6600 O  O   . HOH   F .   ? 0.3239 0.2899 0.3660 -0.0992 -0.0043 -0.0299 1368 HOH   A O   
6601 O  O   . HOH   F .   ? 0.5469 0.2796 0.4749 -0.1511 0.2591  -0.0982 1369 HOH   A O   
6602 O  O   . HOH   F .   ? 0.2647 0.2212 0.2500 -0.0396 0.0221  -0.0068 1370 HOH   A O   
6603 O  O   . HOH   F .   ? 0.2524 0.4596 0.3777 -0.0527 0.0239  -0.0170 1371 HOH   A O   
6604 O  O   . HOH   F .   ? 0.4588 0.3475 0.5213 0.0494  0.1552  -0.0966 1372 HOH   A O   
6605 O  O   . HOH   F .   ? 0.2138 0.2341 0.2420 -0.0336 -0.0495 0.0573  1373 HOH   A O   
6606 O  O   A HOH   F .   ? 0.1337 0.1614 0.1252 0.0238  -0.0301 -0.0146 1374 HOH   A O   
6607 O  O   . HOH   F .   ? 0.2623 0.2136 0.2751 -0.0287 0.0101  0.0326  1375 HOH   A O   
6608 O  O   . HOH   F .   ? 0.8755 0.9610 0.6465 -0.0248 -0.0877 -0.1089 1376 HOH   A O   
6609 O  O   . HOH   F .   ? 0.3952 0.2280 0.5382 -0.1130 0.0855  0.0368  1377 HOH   A O   
6610 O  O   A HOH   F .   ? 0.2135 0.1636 0.1716 -0.0197 -0.0468 0.0029  1378 HOH   A O   
6611 O  O   . HOH   F .   ? 0.1884 0.1874 0.1833 0.0040  0.0030  0.0053  1379 HOH   A O   
6612 O  O   . HOH   F .   ? 0.2656 0.3953 0.3048 0.0370  0.0644  0.1447  1380 HOH   A O   
6613 O  O   . HOH   F .   ? 0.1866 0.1783 0.2310 0.0116  -0.0249 0.0258  1381 HOH   A O   
6614 O  O   . HOH   F .   ? 0.2405 0.2902 0.3599 -0.0092 -0.0087 -0.0551 1382 HOH   A O   
6615 O  O   . HOH   F .   ? 0.2513 0.2297 0.2849 0.0048  -0.0043 0.0766  1383 HOH   A O   
6616 O  O   A HOH   F .   ? 0.1090 0.1532 0.1685 0.0073  -0.0313 -0.0271 1384 HOH   A O   
6617 O  O   . HOH   F .   ? 0.4138 0.6720 0.4071 -0.0923 -0.0148 0.1118  1385 HOH   A O   
6618 O  O   . HOH   F .   ? 0.3089 0.2950 0.2213 0.0265  0.0761  -0.0001 1386 HOH   A O   
6619 O  O   . HOH   F .   ? 0.3547 0.2596 0.3703 -0.0186 -0.0530 0.1049  1387 HOH   A O   
6620 O  O   . HOH   F .   ? 0.9854 0.3379 0.4643 -0.0544 -0.0050 0.1270  1388 HOH   A O   
6621 O  O   . HOH   F .   ? 0.3272 0.2342 0.5579 -0.0718 -0.0520 0.0292  1389 HOH   A O   
6622 O  O   . HOH   F .   ? 0.2676 0.2316 0.2027 -0.0801 0.0119  0.0365  1390 HOH   A O   
6623 O  O   B HOH   F .   ? 0.4458 0.3725 0.3969 0.0531  0.1094  -0.0820 1391 HOH   A O   
6624 O  O   . HOH   F .   ? 0.3258 0.6740 0.4144 0.1101  0.0839  -0.1094 1392 HOH   A O   
6625 O  O   . HOH   F .   ? 0.3053 0.4158 0.4983 -0.0499 0.1631  0.0031  1393 HOH   A O   
6626 O  O   B HOH   F .   ? 0.3432 0.2454 0.2327 -0.0324 -0.0045 0.0200  1394 HOH   A O   
6627 O  O   . HOH   F .   ? 0.2643 0.4011 0.3784 -0.0455 0.1045  -0.0827 1395 HOH   A O   
6628 O  O   . HOH   F .   ? 0.5507 0.2714 0.5011 0.0682  -0.0084 -0.0198 1396 HOH   A O   
6629 O  O   . HOH   F .   ? 0.5232 0.6696 0.6231 -0.0811 0.0372  -0.1337 1397 HOH   A O   
6630 O  O   . HOH   F .   ? 0.1809 0.1883 0.4184 0.0289  0.0996  0.0934  1398 HOH   A O   
6631 O  O   . HOH   F .   ? 0.2094 0.1680 0.1632 -0.0061 0.0150  0.0107  1399 HOH   A O   
6632 O  O   . HOH   F .   ? 0.2312 0.2473 0.4677 0.0250  -0.0572 -0.0754 1400 HOH   A O   
6633 O  O   . HOH   F .   ? 0.2017 0.2832 0.3627 -0.0277 -0.0201 0.0250  1401 HOH   A O   
6634 O  O   . HOH   F .   ? 0.3250 0.2824 0.2371 -0.0901 -0.0883 0.0435  1402 HOH   A O   
6635 O  O   . HOH   F .   ? 0.4909 0.4673 0.2010 -0.0150 0.0802  0.0899  1403 HOH   A O   
6636 O  O   B HOH   F .   ? 0.2516 0.2197 0.1853 0.0119  -0.0359 -0.0452 1404 HOH   A O   
6637 O  O   . HOH   F .   ? 0.3147 0.4565 0.4963 0.1007  0.0728  0.0679  1405 HOH   A O   
6638 O  O   . HOH   F .   ? 0.6750 0.6751 0.6279 -0.1100 0.1044  0.0146  1406 HOH   A O   
6639 O  O   A HOH   F .   ? 0.2359 0.2543 0.2715 -0.0391 0.0938  0.0144  1407 HOH   A O   
6640 O  O   . HOH   F .   ? 0.1796 0.3462 0.3568 -0.0321 0.0686  0.0945  1408 HOH   A O   
6641 O  O   . HOH   F .   ? 0.2289 0.1752 0.3418 0.0000  -0.0603 0.0127  1409 HOH   A O   
6642 O  O   . HOH   F .   ? 0.1618 0.1663 0.3269 0.0001  -0.0125 0.0245  1410 HOH   A O   
6643 O  O   . HOH   F .   ? 0.2239 0.2914 0.2808 -0.0123 -0.0706 0.0371  1411 HOH   A O   
6644 O  O   . HOH   F .   ? 0.4412 0.6354 0.3150 -0.0805 -0.0037 0.1170  1412 HOH   A O   
6645 O  O   . HOH   F .   ? 0.1681 0.1400 0.1767 -0.0199 0.0057  -0.0001 1413 HOH   A O   
6646 O  O   . HOH   F .   ? 0.2700 0.2094 0.2806 -0.0617 -0.0099 0.0550  1414 HOH   A O   
6647 O  O   . HOH   F .   ? 0.2599 0.3779 0.7453 -0.0263 0.0923  -0.0478 1415 HOH   A O   
6648 O  O   A HOH   F .   ? 0.1645 0.1807 0.1979 -0.0345 -0.0212 0.0776  1416 HOH   A O   
6649 O  O   A HOH   F .   ? 0.1237 0.0998 0.1230 -0.0119 -0.0157 0.0034  1417 HOH   A O   
6650 O  O   A HOH   F .   ? 0.4441 0.3144 0.4202 -0.0053 -0.0145 0.0576  1418 HOH   A O   
6651 O  O   A HOH   F .   ? 0.3211 0.3682 0.3552 -0.0635 -0.0304 0.0116  1419 HOH   A O   
6652 O  O   A HOH   F .   ? 0.2594 0.4529 0.4330 0.0600  0.0328  0.0801  1420 HOH   A O   
6653 O  O   B HOH   F .   ? 0.3524 0.4208 0.4898 0.0257  -0.1335 -0.1327 1421 HOH   A O   
6654 O  O   B HOH   F .   ? 0.1408 0.1750 0.2743 -0.0097 0.0293  0.0821  1422 HOH   A O   
6655 O  O   . HOH   F .   ? 0.4135 0.2332 0.5898 -0.0815 -0.2439 0.1116  1423 HOH   A O   
6656 O  O   . HOH   F .   ? 0.3307 0.1286 0.2254 -0.0030 -0.0575 0.0020  1424 HOH   A O   
6657 O  O   A HOH   F .   ? 0.3227 0.3088 0.4228 0.1091  0.0594  -0.0083 1425 HOH   A O   
6658 O  O   A HOH   F .   ? 0.2221 0.1994 0.2822 -0.0412 -0.0627 0.1025  1426 HOH   A O   
6659 O  O   . HOH   F .   ? 0.3304 0.3256 0.2644 -0.0660 -0.1020 0.0667  1427 HOH   A O   
6660 O  O   A HOH   F .   ? 0.3829 0.3711 0.3708 -0.0455 0.0445  0.0521  1428 HOH   A O   
6661 O  O   . HOH   F .   ? 0.4420 0.4367 0.3476 0.1877  -0.0880 -0.1447 1429 HOH   A O   
6662 O  O   . HOH   F .   ? 0.2510 0.4359 0.2821 0.1667  -0.0124 0.0117  1430 HOH   A O   
6663 O  O   . HOH   F .   ? 0.4830 0.2960 0.3503 -0.1372 0.0918  0.0278  1431 HOH   A O   
6664 O  O   . HOH   F .   ? 0.1591 0.2245 0.3140 -0.0223 -0.0207 0.0614  1432 HOH   A O   
6665 O  O   B HOH   F .   ? 0.2745 0.6214 0.3626 -0.0143 0.0213  0.0494  1433 HOH   A O   
6666 O  O   . HOH   F .   ? 0.2887 0.6129 0.1757 -0.0599 0.0492  -0.0118 1434 HOH   A O   
6667 O  O   . HOH   F .   ? 0.6643 0.8069 0.4267 0.2193  -0.1194 0.1560  1435 HOH   A O   
6668 O  O   . HOH   F .   ? 0.4718 0.5281 0.3707 0.0046  -0.1240 0.0077  1436 HOH   A O   
6669 O  O   . HOH   F .   ? 0.7125 0.3944 0.5459 0.1926  -0.0732 0.1303  1437 HOH   A O   
6670 O  O   B HOH   F .   ? 0.3107 0.5689 0.2872 -0.0673 0.1298  0.0655  1438 HOH   A O   
6671 O  O   A HOH   F .   ? 0.1786 0.1123 0.1252 -0.0069 -0.0074 -0.0174 1439 HOH   A O   
6672 O  O   . HOH   F .   ? 0.1843 0.2027 0.6074 -0.0194 -0.0915 0.0571  1440 HOH   A O   
6673 O  O   . HOH   F .   ? 0.5273 0.7690 0.4511 0.0488  0.2588  -0.0600 1441 HOH   A O   
6674 O  O   . HOH   F .   ? 0.4073 0.2759 0.1993 -0.1021 0.0375  0.0558  1442 HOH   A O   
6675 O  O   A HOH   F .   ? 0.2924 0.2444 0.1981 -0.0581 -0.0411 0.0369  1443 HOH   A O   
6676 O  O   A HOH   F .   ? 0.1330 0.1768 0.1953 0.0325  -0.0265 0.0143  1444 HOH   A O   
6677 O  O   A HOH   F .   ? 0.3530 0.2852 0.3145 -0.0072 -0.0056 -0.0619 1445 HOH   A O   
6678 O  O   . HOH   F .   ? 0.2537 0.1647 0.3154 0.0093  0.0125  0.0253  1446 HOH   A O   
6679 O  O   . HOH   F .   ? 0.4482 0.4290 0.5397 -0.0978 -0.1203 -0.1168 1447 HOH   A O   
6680 O  O   . HOH   F .   ? 0.6536 0.6627 0.6089 0.0879  -0.0852 0.0375  1448 HOH   A O   
6681 O  O   . HOH   F .   ? 0.3919 0.3418 0.4213 0.2111  -0.0411 -0.0397 1449 HOH   A O   
6682 O  O   . HOH   F .   ? 0.5607 0.5054 0.7865 0.0411  -0.1355 0.1653  1450 HOH   A O   
6683 O  O   B HOH   F .   ? 0.5709 0.3476 0.3768 -0.0407 0.0331  0.0441  1451 HOH   A O   
6684 O  O   . HOH   F .   ? 0.2337 0.2122 0.2893 0.0099  0.0443  0.0150  1452 HOH   A O   
6685 O  O   . HOH   F .   ? 0.7816 0.6474 0.5521 -0.1280 0.1146  0.2567  1453 HOH   A O   
6686 O  O   . HOH   F .   ? 0.2225 0.2634 0.2601 -0.0021 -0.0083 -0.0585 1454 HOH   A O   
6687 O  O   . HOH   F .   ? 0.4156 0.3645 0.4856 0.0658  -0.0373 0.0860  1455 HOH   A O   
6688 O  O   . HOH   F .   ? 0.2662 0.2877 0.4929 0.0316  0.0429  -0.0918 1456 HOH   A O   
6689 O  O   . HOH   F .   ? 0.4477 0.2927 0.8132 0.0277  -0.0101 -0.1222 1457 HOH   A O   
6690 O  O   A HOH   F .   ? 0.4601 0.2817 0.4144 0.1080  0.1059  0.1696  1458 HOH   A O   
6691 O  O   . HOH   F .   ? 0.5394 0.3427 0.4954 0.0760  0.0102  0.1415  1459 HOH   A O   
6692 O  O   . HOH   F .   ? 0.7285 0.6718 0.5059 -0.0945 0.1652  0.1164  1460 HOH   A O   
6693 O  O   . HOH   F .   ? 0.5726 0.5967 0.6113 -0.1295 0.1082  -0.1174 1461 HOH   A O   
6694 O  O   B HOH   F .   ? 0.6832 0.3286 0.3758 -0.0719 0.1407  -0.1159 1462 HOH   A O   
6695 O  O   . HOH   F .   ? 0.2734 0.2671 0.3559 0.0562  -0.0347 0.0060  1463 HOH   A O   
6696 O  O   B HOH   F .   ? 0.1644 0.3875 0.1732 -0.0714 -0.0230 -0.0292 1464 HOH   A O   
6697 O  O   . HOH   F .   ? 0.6099 0.3296 0.5116 0.0752  0.0678  0.0439  1465 HOH   A O   
6698 O  O   . HOH   F .   ? 0.2893 0.2630 0.3910 -0.0652 0.0120  -0.0654 1466 HOH   A O   
6699 O  O   . HOH   F .   ? 0.7338 0.7848 0.4719 0.0042  -0.0986 -0.0781 1467 HOH   A O   
6700 O  O   B HOH   F .   ? 0.3936 0.4354 0.5234 -0.0888 0.0625  0.0511  1468 HOH   A O   
6701 O  O   . HOH   F .   ? 0.3233 0.5128 0.4541 0.0731  -0.0608 0.1258  1469 HOH   A O   
6702 O  O   . HOH   F .   ? 0.6682 0.6350 0.4720 -0.0008 0.1302  0.1761  1470 HOH   A O   
6703 O  O   . HOH   F .   ? 0.3243 0.4879 0.5444 -0.1489 0.0851  -0.1750 1471 HOH   A O   
6704 O  O   . HOH   F .   ? 0.2997 0.2601 0.6437 0.0544  -0.1417 -0.0275 1472 HOH   A O   
6705 O  O   B HOH   F .   ? 0.5072 0.2680 0.3666 -0.0165 -0.0708 0.0501  1473 HOH   A O   
6706 O  O   . HOH   F .   ? 0.3692 0.6445 0.4167 -0.0788 -0.0639 0.2272  1474 HOH   A O   
6707 O  O   . HOH   F .   ? 0.2659 0.4288 0.5568 0.0562  -0.0038 -0.2023 1475 HOH   A O   
6708 O  O   . HOH   F .   ? 0.2754 0.3197 0.3300 -0.1113 0.0162  0.0082  1476 HOH   A O   
6709 O  O   . HOH   F .   ? 0.2848 0.4138 0.4258 -0.0261 -0.0221 -0.0147 1477 HOH   A O   
6710 O  O   . HOH   F .   ? 0.5860 0.3487 0.7929 0.0211  0.1329  0.2121  1478 HOH   A O   
6711 O  O   . HOH   F .   ? 0.4906 0.5497 0.4723 0.0067  0.1055  0.0779  1479 HOH   A O   
6712 O  O   . HOH   F .   ? 0.2976 0.1878 0.2659 0.0389  -0.0809 -0.0329 1480 HOH   A O   
6713 O  O   . HOH   F .   ? 0.2879 0.2564 0.3942 0.0088  0.0634  -0.0144 1481 HOH   A O   
6714 O  O   B HOH   F .   ? 0.3066 0.2098 0.2700 -0.1213 -0.0241 0.0385  1482 HOH   A O   
6715 O  O   . HOH   F .   ? 0.3783 0.5453 0.3501 0.0229  -0.0362 -0.0577 1483 HOH   A O   
6716 O  O   A HOH   F .   ? 0.4324 0.2852 0.3742 0.0655  0.1905  0.0626  1484 HOH   A O   
6717 O  O   . HOH   F .   ? 0.4699 0.2864 0.3771 -0.0662 -0.0746 0.0676  1485 HOH   A O   
6718 O  O   . HOH   F .   ? 0.4944 0.7111 0.6150 -0.1616 -0.1374 0.0622  1486 HOH   A O   
6719 O  O   B HOH   F .   ? 0.2843 0.2676 0.4261 0.0945  0.0044  0.1436  1487 HOH   A O   
6720 O  O   . HOH   F .   ? 0.7701 0.7747 0.5346 0.2122  -0.1438 -0.0567 1488 HOH   A O   
6721 O  O   . HOH   F .   ? 0.4448 0.4755 0.4698 -0.2244 -0.0183 -0.0148 1489 HOH   A O   
6722 O  O   . HOH   F .   ? 0.6188 0.5337 0.7066 -0.0753 0.0470  0.0001  1490 HOH   A O   
6723 O  O   . HOH   F .   ? 0.6337 0.4081 0.4158 -0.0643 0.1365  -0.0262 1491 HOH   A O   
6724 O  O   . HOH   F .   ? 0.8520 0.3739 0.3250 -0.0408 -0.1265 0.0139  1492 HOH   A O   
6725 O  O   . HOH   F .   ? 0.5497 0.4636 0.4655 -0.0143 0.0076  -0.1266 1493 HOH   A O   
6726 O  O   . HOH   F .   ? 0.5136 0.5352 0.4983 0.1136  -0.0600 -0.0352 1494 HOH   A O   
6727 O  O   . HOH   F .   ? 0.4518 0.4646 0.2997 -0.0064 -0.0149 0.0263  1495 HOH   A O   
6728 O  O   . HOH   F .   ? 0.2696 0.2504 0.2699 0.0432  -0.0035 -0.0091 1496 HOH   A O   
6729 O  O   . HOH   F .   ? 0.4564 0.4040 0.3667 -0.0284 -0.0457 -0.0315 1497 HOH   A O   
6730 O  O   . HOH   F .   ? 0.2776 0.5454 0.3813 0.1092  0.1025  0.2490  1498 HOH   A O   
6731 O  O   . HOH   F .   ? 0.3183 0.5301 0.5012 0.0638  0.1608  0.1989  1499 HOH   A O   
6732 O  O   . HOH   F .   ? 0.2589 0.3088 0.6321 -0.0327 0.1200  -0.1003 1500 HOH   A O   
6733 O  O   . HOH   F .   ? 0.6338 0.5212 0.5210 -0.0972 -0.0802 -0.0635 1501 HOH   A O   
6734 O  O   . HOH   F .   ? 0.2610 0.2642 0.6952 -0.0161 -0.1462 0.0483  1502 HOH   A O   
6735 O  O   . HOH   F .   ? 0.3660 0.3571 0.2767 -0.0482 0.1008  -0.0494 1503 HOH   A O   
6736 O  O   . HOH   F .   ? 0.6015 0.5870 0.6373 0.0760  0.2530  -0.1236 1504 HOH   A O   
6737 O  O   . HOH   F .   ? 0.4649 0.3141 0.5012 -0.0074 0.2510  0.0071  1505 HOH   A O   
6738 O  O   . HOH   F .   ? 0.3095 0.2073 0.6892 0.0058  0.0699  0.1102  1506 HOH   A O   
6739 O  O   . HOH   F .   ? 0.5100 0.6243 0.5453 -0.0814 -0.1248 0.0485  1507 HOH   A O   
6740 O  O   . HOH   F .   ? 0.4195 0.3368 0.4941 -0.1195 0.0762  0.0526  1508 HOH   A O   
6741 O  O   B HOH   F .   ? 0.4461 0.3538 0.4119 0.0852  0.0886  -0.0745 1509 HOH   A O   
6742 O  O   B HOH   F .   ? 0.2833 0.4667 0.4007 0.1415  0.1037  0.1254  1510 HOH   A O   
6743 O  O   . HOH   F .   ? 0.4353 0.9713 0.5808 -0.1351 -0.0424 0.2161  1511 HOH   A O   
6744 O  O   . HOH   F .   ? 0.2496 0.3428 0.3701 0.0465  -0.0223 0.0875  1512 HOH   A O   
6745 O  O   . HOH   F .   ? 0.7573 0.2520 0.4658 -0.0729 0.0985  0.0460  1513 HOH   A O   
6746 O  O   . HOH   F .   ? 0.4555 0.2901 0.4897 -0.1471 0.0001  0.0657  1514 HOH   A O   
6747 O  O   . HOH   F .   ? 0.5844 0.7267 0.5854 0.1405  0.0025  0.1204  1515 HOH   A O   
6748 O  O   . HOH   F .   ? 0.2738 0.4479 0.4255 0.0507  -0.0199 0.0318  1516 HOH   A O   
6749 O  O   . HOH   F .   ? 0.7261 0.5485 0.5918 0.1073  -0.0451 0.0707  1517 HOH   A O   
6750 O  O   . HOH   F .   ? 0.2816 0.4618 0.3485 -0.0261 -0.0466 -0.0701 1518 HOH   A O   
6751 O  O   . HOH   F .   ? 0.3102 0.2423 0.4672 0.0190  0.0554  0.0582  1519 HOH   A O   
6752 O  O   . HOH   F .   ? 0.4734 0.7208 0.5090 0.3025  -0.0184 0.1368  1520 HOH   A O   
6753 O  O   . HOH   F .   ? 0.4891 0.5910 0.4213 -0.0228 -0.0575 -0.1046 1521 HOH   A O   
6754 O  O   A HOH   F .   ? 0.3929 0.4780 0.2665 -0.0055 0.1210  -0.0806 1522 HOH   A O   
6755 O  O   . HOH   F .   ? 0.2869 0.6861 0.3353 0.0680  0.0206  0.0448  1523 HOH   A O   
6756 O  O   B HOH   F .   ? 0.5530 0.5389 0.3304 0.0663  0.0588  -0.0301 1524 HOH   A O   
6757 O  O   . HOH   F .   ? 0.4897 0.5506 0.5370 -0.0555 -0.0215 0.0170  1525 HOH   A O   
6758 O  O   . HOH   F .   ? 0.5774 0.4619 0.4929 0.1705  -0.0320 0.0679  1526 HOH   A O   
6759 O  O   . HOH   F .   ? 0.3261 0.4186 0.5557 -0.0075 -0.0782 0.2508  1527 HOH   A O   
6760 O  O   . HOH   G .   ? 0.2329 0.2267 0.3294 0.0226  0.0731  0.0357  201  HOH   B O   
6761 O  O   . HOH   G .   ? 0.3516 0.3013 0.7008 -0.0409 0.0609  -0.0241 202  HOH   B O   
6762 O  O   . HOH   G .   ? 0.3878 0.4423 0.5766 -0.1007 0.0091  -0.1323 203  HOH   B O   
6763 O  O   . HOH   G .   ? 0.3640 0.7134 0.3892 0.1298  0.0511  0.2367  204  HOH   B O   
6764 O  O   . HOH   G .   ? 0.5882 0.5089 0.2392 0.0843  -0.0869 -0.1357 205  HOH   B O   
6765 O  O   . HOH   G .   ? 0.4445 0.3047 0.3975 -0.0395 -0.0167 -0.1058 206  HOH   B O   
6766 O  O   . HOH   G .   ? 0.7067 0.3196 0.4953 0.0775  0.1245  0.0196  207  HOH   B O   
6767 O  O   . HOH   G .   ? 0.2956 0.2176 0.5439 0.0091  0.1683  0.0904  208  HOH   B O   
6768 O  O   . HOH   G .   ? 0.5602 0.4005 0.6388 0.0758  -0.0933 0.2545  209  HOH   B O   
6769 O  O   . HOH   G .   ? 0.3051 0.5573 0.4957 -0.0029 0.1622  -0.1853 210  HOH   B O   
6770 O  O   . HOH   G .   ? 0.5032 0.6023 0.4020 0.2852  -0.1305 -0.0152 211  HOH   B O   
6771 O  O   . HOH   G .   ? 0.5647 0.5927 0.5540 0.1603  0.1158  0.0718  212  HOH   B O   
6772 O  O   . HOH   G .   ? 0.4730 0.3884 0.3708 -0.0565 -0.1293 0.0868  213  HOH   B O   
6773 O  O   . HOH   G .   ? 0.2630 0.2984 0.7277 0.0490  -0.1203 0.0325  214  HOH   B O   
6774 O  O   . HOH   G .   ? 0.2003 0.2273 0.3179 -0.0015 0.0085  -0.0226 215  HOH   B O   
6775 O  O   . HOH   G .   ? 0.4104 0.4824 0.4122 0.2064  -0.0513 0.0249  216  HOH   B O   
6776 O  O   . HOH   G .   ? 0.1591 0.1916 0.2862 -0.0159 -0.0068 0.0069  217  HOH   B O   
6777 O  O   . HOH   G .   ? 0.3602 0.5960 0.4853 0.2290  0.0293  -0.1039 218  HOH   B O   
6778 O  O   . HOH   G .   ? 0.3776 0.3732 0.5373 -0.1406 -0.0022 0.0511  219  HOH   B O   
6779 O  O   . HOH   G .   ? 0.2155 0.2197 0.3837 -0.0291 -0.0117 -0.0497 220  HOH   B O   
6780 O  O   . HOH   G .   ? 0.2926 0.2846 0.5541 0.0346  -0.0466 -0.0409 221  HOH   B O   
6781 O  O   . HOH   G .   ? 0.5111 0.2091 0.3090 -0.0131 -0.0952 0.0183  222  HOH   B O   
6782 O  O   . HOH   G .   ? 0.2530 0.1802 0.2880 -0.0308 0.0980  -0.0003 223  HOH   B O   
6783 O  O   . HOH   G .   ? 0.4025 0.4017 0.6737 -0.0081 -0.1908 -0.0896 224  HOH   B O   
6784 O  O   . HOH   G .   ? 0.4196 0.4237 0.4384 -0.0022 0.0677  -0.1692 225  HOH   B O   
6785 O  O   . HOH   G .   ? 0.6943 0.6444 0.3319 0.1835  -0.0035 -0.0141 226  HOH   B O   
6786 O  O   . HOH   G .   ? 0.4772 0.8170 0.3537 0.3444  0.0276  0.0674  227  HOH   B O   
6787 O  O   . HOH   G .   ? 0.1814 0.2045 0.3018 -0.0163 -0.0045 -0.0181 228  HOH   B O   
6788 O  O   . HOH   G .   ? 0.3479 0.2446 0.4399 0.0626  -0.0575 -0.0641 229  HOH   B O   
6789 O  O   . HOH   G .   ? 0.2133 0.1333 0.3615 0.0104  -0.0558 -0.0176 230  HOH   B O   
6790 O  O   . HOH   G .   ? 0.2763 0.2597 0.3275 0.0259  0.0305  -0.0887 231  HOH   B O   
6791 O  O   . HOH   G .   ? 0.6222 0.4523 0.5292 0.1710  0.0259  -0.1031 232  HOH   B O   
6792 O  O   . HOH   G .   ? 0.3165 0.2368 0.4901 -0.0035 0.1646  0.0024  233  HOH   B O   
6793 O  O   . HOH   G .   ? 0.2411 0.3692 0.3422 -0.0372 -0.0721 -0.0601 234  HOH   B O   
6794 O  O   . HOH   G .   ? 0.3165 0.2422 0.6346 -0.0151 0.0563  0.0223  235  HOH   B O   
6795 O  O   . HOH   G .   ? 0.2814 0.3472 0.3533 -0.0782 0.0246  -0.0733 236  HOH   B O   
6796 O  O   . HOH   G .   ? 0.4286 0.3325 0.2412 0.0349  0.0909  0.0524  237  HOH   B O   
6797 O  O   . HOH   G .   ? 0.3633 0.1855 0.2233 0.0170  -0.0713 -0.0124 238  HOH   B O   
6798 O  O   . HOH   G .   ? 0.5904 0.2999 0.4288 -0.1899 0.0379  0.0130  239  HOH   B O   
6799 O  O   . HOH   G .   ? 0.1555 0.1489 0.1697 -0.0112 -0.0055 0.0013  240  HOH   B O   
6800 O  O   . HOH   G .   ? 0.2124 0.2366 0.3291 -0.0459 0.0075  -0.0378 241  HOH   B O   
6801 O  O   . HOH   G .   ? 0.3504 0.2874 0.4168 0.0305  -0.0801 -0.1191 242  HOH   B O   
6802 O  O   . HOH   G .   ? 0.5932 0.3185 0.4157 -0.2360 -0.0087 -0.0035 243  HOH   B O   
6803 O  O   . HOH   G .   ? 0.2169 0.3964 0.2397 -0.0319 -0.0241 0.0692  244  HOH   B O   
6804 O  O   . HOH   G .   ? 0.2476 0.2043 0.2154 0.0044  -0.0083 -0.0057 245  HOH   B O   
6805 O  O   . HOH   G .   ? 0.3626 0.3454 0.2471 0.0636  0.0735  0.0189  246  HOH   B O   
6806 O  O   . HOH   G .   ? 0.1528 0.1293 0.1806 -0.0033 -0.0098 0.0111  247  HOH   B O   
6807 O  O   . HOH   G .   ? 0.2822 0.2494 0.2905 0.0936  0.0684  0.0303  248  HOH   B O   
6808 O  O   . HOH   G .   ? 0.3076 0.1806 0.6192 -0.0184 -0.1383 -0.0076 249  HOH   B O   
6809 O  O   . HOH   G .   ? 0.2220 0.1509 0.2300 -0.0247 -0.0425 0.0238  250  HOH   B O   
6810 O  O   . HOH   G .   ? 0.1611 0.1465 0.2758 -0.0101 -0.0003 -0.0082 251  HOH   B O   
6811 O  O   . HOH   G .   ? 0.2304 0.2085 0.2445 -0.0327 -0.0471 0.0134  252  HOH   B O   
6812 O  O   . HOH   G .   ? 0.2817 0.4564 0.3493 -0.1064 -0.0345 -0.0637 253  HOH   B O   
6813 O  O   . HOH   G .   ? 0.2525 0.2195 0.2691 0.0754  -0.0805 -0.0690 254  HOH   B O   
6814 O  O   . HOH   G .   ? 0.1686 0.1640 0.3103 -0.0192 -0.0220 0.0122  255  HOH   B O   
6815 O  O   . HOH   G .   ? 0.2302 0.3281 0.2309 -0.0504 0.0252  0.0484  256  HOH   B O   
6816 O  O   . HOH   G .   ? 0.4441 0.3734 0.3700 -0.0785 0.0603  -0.1010 257  HOH   B O   
6817 O  O   . HOH   G .   ? 0.2568 0.2974 0.4063 -0.0591 0.0446  -0.1025 258  HOH   B O   
6818 O  O   . HOH   G .   ? 0.1869 0.2834 0.3061 0.0420  0.0471  0.1035  259  HOH   B O   
6819 O  O   . HOH   G .   ? 0.2195 0.1935 0.3781 0.0078  -0.0451 -0.0406 260  HOH   B O   
6820 O  O   . HOH   G .   ? 0.5937 0.3096 0.2827 -0.0250 0.0693  -0.0413 261  HOH   B O   
6821 O  O   . HOH   G .   ? 0.3399 0.4770 0.3890 -0.0535 -0.1231 0.1424  262  HOH   B O   
6822 O  O   . HOH   G .   ? 0.3266 0.2386 0.3179 -0.0421 0.0324  -0.0526 263  HOH   B O   
6823 O  O   . HOH   G .   ? 0.1431 0.1734 0.2205 -0.0130 0.0027  0.0146  264  HOH   B O   
6824 O  O   . HOH   G .   ? 0.3702 0.3658 0.4658 0.1166  -0.0776 -0.0999 265  HOH   B O   
6825 O  O   . HOH   G .   ? 0.2081 0.1495 0.2308 -0.0334 -0.0204 0.0159  266  HOH   B O   
6826 O  O   . HOH   G .   ? 0.2670 0.1978 0.3115 -0.0605 0.0290  -0.0109 267  HOH   B O   
6827 O  O   . HOH   G .   ? 0.2806 0.4957 0.5933 0.0100  -0.0114 -0.1214 268  HOH   B O   
6828 O  O   . HOH   G .   ? 0.2374 0.4162 0.5211 0.1073  -0.0552 -0.0661 269  HOH   B O   
6829 O  O   . HOH   G .   ? 0.4602 0.3730 0.3054 0.0825  -0.0075 -0.0962 270  HOH   B O   
6830 O  O   . HOH   G .   ? 0.2766 0.2755 0.2699 -0.0486 -0.0904 0.0177  271  HOH   B O   
6831 O  O   . HOH   G .   ? 0.4928 0.6552 0.2521 -0.0466 -0.0879 0.1468  272  HOH   B O   
6832 O  O   . HOH   G .   ? 0.2234 0.2237 0.2073 0.0009  0.0023  0.0030  273  HOH   B O   
6833 O  O   . HOH   G .   ? 0.2023 0.1783 0.1817 -0.0449 -0.0487 0.0209  274  HOH   B O   
6834 O  O   . HOH   G .   ? 0.2372 0.3327 0.2263 0.1024  -0.0217 -0.0124 275  HOH   B O   
6835 O  O   . HOH   G .   ? 0.1849 0.1391 0.4776 -0.0106 -0.0366 -0.0054 276  HOH   B O   
6836 O  O   . HOH   G .   ? 0.2465 0.2690 0.2492 -0.0525 -0.0704 -0.0295 277  HOH   B O   
6837 O  O   . HOH   G .   ? 0.2217 0.4619 0.4788 -0.0585 -0.0476 -0.1506 278  HOH   B O   
6838 O  O   . HOH   G .   ? 0.2591 0.3823 0.4085 0.0170  0.1072  0.0358  279  HOH   B O   
6839 O  O   . HOH   G .   ? 0.1672 0.1559 0.3845 -0.0159 0.0084  -0.0085 280  HOH   B O   
6840 O  O   . HOH   G .   ? 0.3014 0.2829 0.5762 0.0038  -0.0687 -0.1326 281  HOH   B O   
6841 O  O   . HOH   G .   ? 0.4078 0.5256 0.5060 0.0031  -0.1516 -0.0010 282  HOH   B O   
6842 O  O   . HOH   G .   ? 0.1640 0.1663 0.1886 -0.0055 0.0042  0.0055  283  HOH   B O   
6843 O  O   . HOH   G .   ? 0.4555 0.3272 0.4789 -0.0893 0.0139  0.0868  284  HOH   B O   
6844 O  O   . HOH   G .   ? 0.4122 0.2839 0.4877 -0.0497 -0.0993 -0.0636 285  HOH   B O   
6845 O  O   . HOH   G .   ? 0.1765 0.1882 0.2980 0.0171  -0.0119 -0.0092 286  HOH   B O   
6846 O  O   . HOH   G .   ? 0.2705 0.2668 0.3082 0.0188  -0.0804 0.0380  287  HOH   B O   
6847 O  O   . HOH   G .   ? 0.1717 0.2019 0.1665 -0.0164 -0.0194 0.0079  288  HOH   B O   
6848 O  O   . HOH   G .   ? 0.2798 0.2124 0.4929 0.0171  0.0484  0.0642  289  HOH   B O   
6849 O  O   . HOH   G .   ? 0.3847 0.3174 0.2095 0.0787  -0.0885 -0.0082 290  HOH   B O   
6850 O  O   . HOH   G .   ? 0.2072 0.2858 0.6745 0.0297  -0.0519 -0.1106 291  HOH   B O   
6851 O  O   . HOH   G .   ? 0.3772 0.7064 0.3823 0.2138  -0.0743 0.0868  292  HOH   B O   
6852 O  O   . HOH   G .   ? 0.3947 0.2165 0.4512 -0.0985 -0.2160 0.0932  293  HOH   B O   
6853 O  O   . HOH   G .   ? 0.1804 0.3288 0.4613 0.0172  -0.0036 -0.1196 294  HOH   B O   
6854 O  O   . HOH   G .   ? 0.2779 0.7279 0.7842 0.1707  -0.0508 -0.0797 295  HOH   B O   
6855 O  O   . HOH   G .   ? 0.4489 0.4038 0.2502 0.1312  -0.0827 0.0601  296  HOH   B O   
6856 O  O   . HOH   G .   ? 0.2782 0.4781 0.5172 -0.1016 -0.1208 0.1012  297  HOH   B O   
6857 O  O   . HOH   G .   ? 0.3116 0.3014 0.2813 -0.0210 0.0034  -0.1189 298  HOH   B O   
6858 O  O   . HOH   G .   ? 0.2977 0.3868 0.4167 -0.1310 0.1096  -0.0627 299  HOH   B O   
6859 O  O   . HOH   G .   ? 0.1821 0.1623 0.2434 0.0041  0.0070  0.0169  300  HOH   B O   
6860 O  O   . HOH   G .   ? 0.2066 0.1678 0.3403 0.0357  -0.0904 0.0048  301  HOH   B O   
6861 O  O   . HOH   G .   ? 0.2831 0.2810 0.5529 -0.0186 -0.0661 0.1172  302  HOH   B O   
6862 O  O   . HOH   G .   ? 0.4609 0.5042 0.2361 0.0194  0.0848  0.0808  303  HOH   B O   
6863 O  O   . HOH   G .   ? 0.4918 0.4250 0.2458 0.1248  -0.0916 -0.0279 304  HOH   B O   
6864 O  O   . HOH   G .   ? 0.3595 0.1875 0.3730 0.0725  0.1303  0.0499  305  HOH   B O   
6865 O  O   . HOH   G .   ? 0.1666 0.1564 0.3262 0.0059  -0.0064 -0.0021 306  HOH   B O   
6866 O  O   . HOH   G .   ? 0.5460 0.5818 0.5754 -0.1129 -0.0340 0.1433  307  HOH   B O   
6867 O  O   . HOH   G .   ? 0.2472 0.1532 0.2706 -0.0096 -0.0197 0.0217  308  HOH   B O   
6868 O  O   . HOH   G .   ? 0.5997 0.3819 0.3734 0.2598  0.1395  0.0738  309  HOH   B O   
6869 O  O   . HOH   G .   ? 0.2430 0.7330 0.2881 0.0738  -0.0244 -0.0742 310  HOH   B O   
6870 O  O   . HOH   G .   ? 0.6183 0.6257 0.4754 0.3045  -0.0204 -0.0101 311  HOH   B O   
6871 O  O   . HOH   G .   ? 0.5194 0.2769 0.2695 -0.1673 0.1007  -0.0193 312  HOH   B O   
6872 O  O   . HOH   G .   ? 0.1641 0.1869 0.3046 -0.0257 -0.0154 0.0096  313  HOH   B O   
6873 O  O   . HOH   G .   ? 0.2290 0.3197 0.5163 -0.0226 -0.0487 -0.0213 314  HOH   B O   
6874 O  O   . HOH   G .   ? 0.7248 0.4934 0.5945 0.2103  0.1424  0.0279  315  HOH   B O   
6875 O  O   . HOH   G .   ? 0.4657 0.4252 0.6888 0.0870  -0.0284 0.0422  316  HOH   B O   
6876 O  O   . HOH   G .   ? 0.4684 0.4716 0.2635 0.0872  -0.0636 -0.0680 317  HOH   B O   
6877 O  O   . HOH   G .   ? 0.2310 0.1622 0.2849 -0.0247 -0.0288 -0.0002 318  HOH   B O   
6878 O  O   . HOH   G .   ? 0.3957 0.2244 0.2848 0.1382  0.0927  0.0400  319  HOH   B O   
6879 O  O   . HOH   G .   ? 0.2258 0.1967 0.2053 -0.0160 0.0183  0.0204  320  HOH   B O   
6880 O  O   . HOH   G .   ? 0.2314 0.4606 0.5265 -0.0233 -0.0421 -0.0329 321  HOH   B O   
6881 O  O   . HOH   G .   ? 0.1656 0.2937 0.2630 -0.0163 -0.0214 0.0736  322  HOH   B O   
6882 O  O   . HOH   G .   ? 0.2939 0.2886 0.3721 -0.0339 0.0996  -0.0806 323  HOH   B O   
6883 O  O   . HOH   G .   ? 0.1661 0.1594 0.3381 -0.0129 -0.0223 -0.0114 324  HOH   B O   
6884 O  O   . HOH   G .   ? 0.2724 0.2273 0.2428 0.0103  -0.0179 0.0188  325  HOH   B O   
6885 O  O   . HOH   G .   ? 0.2814 0.3639 0.5186 -0.0637 -0.1779 0.1405  326  HOH   B O   
6886 O  O   . HOH   G .   ? 0.1948 0.2007 0.3129 0.0321  0.0356  0.0164  327  HOH   B O   
6887 O  O   . HOH   G .   ? 0.7922 0.2066 0.3235 0.0008  -0.0848 0.0190  328  HOH   B O   
6888 O  O   . HOH   G .   ? 0.6411 0.3388 0.3412 -0.0031 0.0767  0.0976  329  HOH   B O   
6889 O  O   . HOH   G .   ? 0.3422 0.3515 0.8698 -0.0303 -0.1000 0.1876  330  HOH   B O   
6890 O  O   . HOH   G .   ? 0.1890 0.2845 0.3019 0.0390  -0.0073 -0.0669 331  HOH   B O   
6891 O  O   . HOH   G .   ? 0.4690 0.3386 0.5897 0.1514  0.2362  0.2021  332  HOH   B O   
6892 O  O   . HOH   G .   ? 0.2620 0.2142 0.5446 0.0015  0.0067  0.0449  333  HOH   B O   
6893 O  O   . HOH   G .   ? 0.5686 0.5468 0.6510 0.0772  -0.0964 0.2289  334  HOH   B O   
6894 O  O   . HOH   G .   ? 0.5299 0.2389 0.3295 0.0486  0.0152  0.0913  335  HOH   B O   
6895 O  O   . HOH   G .   ? 0.1766 0.1550 0.2496 0.0033  -0.0171 0.0162  336  HOH   B O   
6896 O  O   . HOH   G .   ? 0.5800 0.3696 0.4375 0.0895  0.0727  -0.1502 337  HOH   B O   
6897 O  O   . HOH   G .   ? 0.6762 0.4896 0.6168 -0.1073 -0.1145 -0.1417 338  HOH   B O   
6898 O  O   . HOH   G .   ? 0.2454 0.2268 0.5953 -0.0468 -0.0054 0.1357  339  HOH   B O   
6899 O  O   . HOH   G .   ? 0.5909 0.3295 0.3076 0.0572  -0.1176 -0.0668 340  HOH   B O   
6900 O  O   . HOH   G .   ? 0.5584 0.5997 0.3509 0.0315  -0.1145 0.0542  341  HOH   B O   
6901 O  O   . HOH   G .   ? 0.4326 0.7834 0.3701 -0.0478 -0.0748 0.1873  342  HOH   B O   
6902 O  O   . HOH   G .   ? 0.2158 0.5470 0.6835 -0.0219 -0.0214 0.1103  343  HOH   B O   
6903 O  O   . HOH   G .   ? 0.6508 0.7314 0.3033 -0.0421 -0.0556 0.0572  344  HOH   B O   
6904 O  O   . HOH   G .   ? 0.4472 0.6204 0.4344 -0.1460 -0.0944 -0.0869 345  HOH   B O   
6905 O  O   . HOH   G .   ? 0.2123 0.2078 0.3288 -0.0111 0.0628  -0.0193 346  HOH   B O   
6906 O  O   . HOH   G .   ? 0.4621 0.4886 0.5259 0.0291  -0.0939 0.0081  347  HOH   B O   
6907 O  O   . HOH   G .   ? 0.4664 0.5862 0.6613 0.0417  0.0465  -0.0319 348  HOH   B O   
6908 O  O   . HOH   G .   ? 0.2965 0.2264 0.5116 -0.0337 -0.0853 -0.0591 349  HOH   B O   
6909 O  O   . HOH   G .   ? 0.3923 0.2151 0.3762 -0.0734 -0.0016 -0.0710 350  HOH   B O   
6910 O  O   . HOH   G .   ? 0.2473 0.3445 0.5793 -0.0014 -0.0080 0.0369  351  HOH   B O   
6911 O  O   . HOH   G .   ? 0.4834 0.6098 0.4946 -0.1254 0.0866  0.1054  352  HOH   B O   
6912 O  O   . HOH   G .   ? 0.2170 0.5784 0.3960 0.1338  -0.0491 -0.1192 353  HOH   B O   
6913 O  O   . HOH   G .   ? 0.4845 0.3167 0.5880 -0.1281 0.1298  0.0465  354  HOH   B O   
6914 O  O   . HOH   G .   ? 0.3155 0.5020 0.5021 -0.1625 0.0348  -0.0188 355  HOH   B O   
6915 O  O   . HOH   G .   ? 0.3002 0.1883 0.4374 0.0386  -0.1183 -0.0507 356  HOH   B O   
6916 O  O   . HOH   G .   ? 0.3752 0.2650 0.4321 -0.0907 -0.0293 -0.0503 357  HOH   B O   
6917 O  O   . HOH   G .   ? 0.5270 0.3492 0.4198 0.0415  0.1365  -0.0393 358  HOH   B O   
6918 O  O   . HOH   G .   ? 0.4886 0.6598 0.4846 0.2358  -0.1116 0.1232  359  HOH   B O   
6919 O  O   . HOH   G .   ? 0.4606 0.5125 0.6088 0.0358  0.0733  0.0376  360  HOH   B O   
6920 O  O   . HOH   G .   ? 0.4452 0.3690 0.4952 -0.0175 -0.1620 -0.0105 361  HOH   B O   
6921 O  O   . HOH   G .   ? 0.4485 0.7774 0.3272 0.2731  -0.0306 0.0140  362  HOH   B O   
6922 O  O   . HOH   G .   ? 0.5516 0.4144 0.6670 -0.0077 0.0854  0.0958  363  HOH   B O   
6923 O  O   . HOH   G .   ? 0.2286 0.3439 0.7173 -0.0533 -0.0827 -0.0796 364  HOH   B O   
6924 O  O   . HOH   G .   ? 0.6365 0.4079 0.4859 0.0807  0.0951  0.0411  365  HOH   B O   
6925 O  O   . HOH   G .   ? 0.5803 0.2996 0.5492 -0.1484 -0.0460 0.0262  366  HOH   B O   
6926 O  O   . HOH   G .   ? 0.5146 0.5952 0.4317 -0.0719 -0.0680 -0.1073 367  HOH   B O   
6927 O  O   . HOH   G .   ? 0.5835 0.5556 0.3652 0.2065  -0.1531 0.0355  368  HOH   B O   
6928 O  O   . HOH   G .   ? 0.6708 0.3243 0.5518 -0.0243 -0.1733 0.0164  369  HOH   B O   
6929 O  O   . HOH   G .   ? 0.4861 0.5653 0.5894 0.2692  0.1240  0.1327  370  HOH   B O   
6930 O  O   . HOH   G .   ? 0.6678 0.2236 0.3872 0.0009  -0.0045 0.0589  371  HOH   B O   
6931 O  O   . HOH   G .   ? 0.5058 0.3301 0.3927 0.0360  -0.1598 -0.0317 372  HOH   B O   
6932 O  O   . HOH   G .   ? 0.7798 0.7229 0.5156 0.2828  -0.1207 0.1208  373  HOH   B O   
6933 O  O   . HOH   G .   ? 0.5931 0.4414 0.3142 -0.0945 -0.1147 -0.0800 374  HOH   B O   
6934 O  O   . HOH   G .   ? 0.4364 0.5530 0.4797 -0.1174 -0.0503 0.0347  375  HOH   B O   
6935 O  O   . HOH   G .   ? 0.4661 0.7182 0.6649 0.1399  0.0669  0.3199  376  HOH   B O   
6936 O  O   . HOH   G .   ? 0.2605 0.4229 0.4595 0.0362  -0.0938 -0.0609 377  HOH   B O   
6937 O  O   . HOH   G .   ? 0.4512 0.7890 0.3910 -0.1519 0.0301  -0.1553 378  HOH   B O   
6938 O  O   . HOH   G .   ? 0.3760 0.6129 0.5462 0.1405  -0.0409 0.0912  379  HOH   B O   
6939 O  O   . HOH   G .   ? 0.3982 0.4453 0.2339 0.0564  0.0396  0.0243  380  HOH   B O   
6940 O  O   . HOH   G .   ? 0.6985 0.3600 0.5396 -0.0975 -0.0712 0.0095  381  HOH   B O   
6941 O  O   . HOH   G .   ? 0.2927 0.2629 0.3469 0.0041  0.0077  0.0384  382  HOH   B O   
6942 O  O   . HOH   G .   ? 0.6024 0.7199 0.6759 0.0282  0.2043  0.2019  383  HOH   B O   
6943 O  O   . HOH   G .   ? 0.5263 0.8545 0.6267 0.1512  0.2604  0.1271  384  HOH   B O   
6944 O  O   . HOH   G .   ? 0.2500 0.4317 0.4264 -0.0899 -0.1038 -0.0153 385  HOH   B O   
6945 O  O   . HOH   G .   ? 0.6166 0.4264 0.5293 -0.0657 -0.0296 0.0135  386  HOH   B O   
6946 O  O   . HOH   G .   ? 0.6931 0.4834 0.5008 0.0663  0.1422  -0.1166 387  HOH   B O   
6947 O  O   . HOH   G .   ? 0.4646 0.3552 0.3865 0.0383  0.0044  -0.0036 388  HOH   B O   
6948 O  O   . HOH   G .   ? 0.6018 0.4575 0.4513 -0.0176 -0.0636 -0.0404 389  HOH   B O   
6949 O  O   . HOH   G .   ? 0.4353 0.2380 0.3066 0.0916  -0.0180 0.0179  390  HOH   B O   
6950 O  O   . HOH   G .   ? 0.7300 0.5846 0.4335 0.2285  -0.0090 0.0934  391  HOH   B O   
6951 O  O   . HOH   G .   ? 0.4175 0.4224 0.3837 -0.0230 0.0280  0.0259  392  HOH   B O   
6952 O  O   . HOH   G .   ? 0.4558 0.2291 0.5642 -0.0630 0.0457  0.0763  393  HOH   B O   
6953 O  O   . HOH   G .   ? 0.2446 0.4684 0.6696 -0.1326 -0.0756 0.0177  394  HOH   B O   
6954 O  O   . HOH   G .   ? 0.3292 0.3740 0.3846 0.0400  0.0221  -0.0714 395  HOH   B O   
6955 O  O   . HOH   G .   ? 0.4449 0.6144 0.3990 0.1467  -0.0620 -0.1103 396  HOH   B O   
6956 O  O   . HOH   G .   ? 0.4213 0.4599 0.4270 0.0413  0.0978  0.0416  397  HOH   B O   
6957 O  O   . HOH   G .   ? 0.2110 0.3013 0.6655 -0.0652 -0.0719 0.0106  398  HOH   B O   
6958 O  O   . HOH   G .   ? 0.5543 0.4258 0.3029 -0.2231 -0.0571 0.1082  399  HOH   B O   
6959 O  O   . HOH   G .   ? 0.6386 0.5890 0.7619 0.0879  -0.1099 0.2824  400  HOH   B O   
6960 O  O   . HOH   G .   ? 0.6195 0.6258 0.3793 0.1568  -0.0213 0.0097  401  HOH   B O   
# 
