data_7HEW
# 
_entry.id   7HEW 
# 
_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   7HEW         pdb_00007hew 10.2210/pdb7hew/pdb 
WWPDB D_1001407386 ?            ?                   
# 
_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                        7HEW 
_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 '(2R)-2-methyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-1-ol' 220.271   1   ?                      ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                       35.453    1   ?                      ? ? ? 
4 water       nat water                                                                18.015    425 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2R)-2-methyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-1-ol' A1A99 
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 
A1A99 non-polymer         . '(2R)-2-methyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-1-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 A1A99 1   201 201  A1A99 LA1 A . 
D 3 CL    1   202 1    CL    CL  A . 
E 4 HOH   1   301 292  HOH   HOH A . 
E 4 HOH   2   302 196  HOH   HOH A . 
E 4 HOH   3   303 109  HOH   HOH A . 
E 4 HOH   4   304 1289 HOH   HOH A . 
E 4 HOH   5   305 625  HOH   HOH A . 
E 4 HOH   6   306 209  HOH   HOH A . 
E 4 HOH   7   307 86   HOH   HOH A . 
E 4 HOH   8   308 153  HOH   HOH A . 
E 4 HOH   9   309 405  HOH   HOH A . 
E 4 HOH   10  310 199  HOH   HOH A . 
E 4 HOH   11  311 337  HOH   HOH A . 
E 4 HOH   12  312 15   HOH   HOH A . 
E 4 HOH   13  313 229  HOH   HOH A . 
E 4 HOH   14  314 661  HOH   HOH A . 
E 4 HOH   15  315 76   HOH   HOH A . 
E 4 HOH   16  316 57   HOH   HOH A . 
E 4 HOH   17  317 964  HOH   HOH A . 
E 4 HOH   18  318 1275 HOH   HOH A . 
E 4 HOH   19  319 136  HOH   HOH A . 
E 4 HOH   20  320 93   HOH   HOH A . 
E 4 HOH   21  321 1295 HOH   HOH A . 
E 4 HOH   22  322 4    HOH   HOH A . 
E 4 HOH   23  323 247  HOH   HOH A . 
E 4 HOH   24  324 151  HOH   HOH A . 
E 4 HOH   25  325 124  HOH   HOH A . 
E 4 HOH   26  326 225  HOH   HOH A . 
E 4 HOH   27  327 236  HOH   HOH A . 
E 4 HOH   28  328 36   HOH   HOH A . 
E 4 HOH   29  329 15   HOH   HOH A . 
E 4 HOH   30  330 241  HOH   HOH A . 
E 4 HOH   31  331 493  HOH   HOH A . 
E 4 HOH   32  332 320  HOH   HOH A . 
E 4 HOH   33  333 1283 HOH   HOH A . 
E 4 HOH   34  334 140  HOH   HOH A . 
E 4 HOH   35  335 26   HOH   HOH A . 
E 4 HOH   36  336 21   HOH   HOH A . 
E 4 HOH   37  337 164  HOH   HOH A . 
E 4 HOH   38  338 148  HOH   HOH A . 
E 4 HOH   39  339 105  HOH   HOH A . 
E 4 HOH   40  340 192  HOH   HOH A . 
E 4 HOH   41  341 396  HOH   HOH A . 
E 4 HOH   42  342 1301 HOH   HOH A . 
E 4 HOH   43  343 68   HOH   HOH A . 
E 4 HOH   44  344 630  HOH   HOH A . 
E 4 HOH   45  345 1310 HOH   HOH A . 
E 4 HOH   46  346 42   HOH   HOH A . 
E 4 HOH   47  347 74   HOH   HOH A . 
E 4 HOH   48  348 8    HOH   HOH A . 
E 4 HOH   49  349 662  HOH   HOH A . 
E 4 HOH   50  350 33   HOH   HOH A . 
E 4 HOH   51  351 165  HOH   HOH A . 
E 4 HOH   52  352 139  HOH   HOH A . 
E 4 HOH   53  353 469  HOH   HOH A . 
E 4 HOH   54  354 393  HOH   HOH A . 
E 4 HOH   55  355 102  HOH   HOH A . 
E 4 HOH   56  356 162  HOH   HOH A . 
E 4 HOH   57  357 354  HOH   HOH A . 
E 4 HOH   58  358 66   HOH   HOH A . 
E 4 HOH   59  359 27   HOH   HOH A . 
E 4 HOH   60  360 2    HOH   HOH A . 
E 4 HOH   61  361 939  HOH   HOH A . 
E 4 HOH   62  362 92   HOH   HOH A . 
E 4 HOH   63  363 281  HOH   HOH A . 
E 4 HOH   64  364 1300 HOH   HOH A . 
E 4 HOH   65  365 155  HOH   HOH A . 
E 4 HOH   66  366 18   HOH   HOH A . 
E 4 HOH   67  367 49   HOH   HOH A . 
E 4 HOH   68  368 159  HOH   HOH A . 
E 4 HOH   69  369 169  HOH   HOH A . 
E 4 HOH   70  370 81   HOH   HOH A . 
E 4 HOH   71  371 19   HOH   HOH A . 
E 4 HOH   72  372 7    HOH   HOH A . 
E 4 HOH   73  373 45   HOH   HOH A . 
E 4 HOH   74  374 5    HOH   HOH A . 
E 4 HOH   75  375 461  HOH   HOH A . 
E 4 HOH   76  376 17   HOH   HOH A . 
E 4 HOH   77  377 46   HOH   HOH A . 
E 4 HOH   78  378 56   HOH   HOH A . 
E 4 HOH   79  379 78   HOH   HOH A . 
E 4 HOH   80  380 138  HOH   HOH A . 
E 4 HOH   81  381 218  HOH   HOH A . 
E 4 HOH   82  382 11   HOH   HOH A . 
E 4 HOH   83  383 409  HOH   HOH A . 
E 4 HOH   84  384 4    HOH   HOH A . 
E 4 HOH   85  385 3    HOH   HOH A . 
E 4 HOH   86  386 366  HOH   HOH A . 
E 4 HOH   87  387 154  HOH   HOH A . 
E 4 HOH   88  388 186  HOH   HOH A . 
E 4 HOH   89  389 134  HOH   HOH A . 
E 4 HOH   90  390 35   HOH   HOH A . 
E 4 HOH   91  391 24   HOH   HOH A . 
E 4 HOH   92  392 1313 HOH   HOH A . 
E 4 HOH   93  393 19   HOH   HOH A . 
E 4 HOH   94  394 16   HOH   HOH A . 
E 4 HOH   95  395 6    HOH   HOH A . 
E 4 HOH   96  396 8    HOH   HOH A . 
E 4 HOH   97  397 116  HOH   HOH A . 
E 4 HOH   98  398 58   HOH   HOH A . 
E 4 HOH   99  399 351  HOH   HOH A . 
E 4 HOH   100 400 132  HOH   HOH A . 
E 4 HOH   101 401 1315 HOH   HOH A . 
E 4 HOH   102 402 12   HOH   HOH A . 
E 4 HOH   103 403 83   HOH   HOH A . 
E 4 HOH   104 404 303  HOH   HOH A . 
E 4 HOH   105 405 39   HOH   HOH A . 
E 4 HOH   106 406 296  HOH   HOH A . 
E 4 HOH   107 407 1290 HOH   HOH A . 
E 4 HOH   108 408 121  HOH   HOH A . 
E 4 HOH   109 409 1308 HOH   HOH A . 
E 4 HOH   110 410 9    HOH   HOH A . 
E 4 HOH   111 411 1    HOH   HOH A . 
E 4 HOH   112 412 67   HOH   HOH A . 
E 4 HOH   113 413 1068 HOH   HOH A . 
E 4 HOH   114 414 85   HOH   HOH A . 
E 4 HOH   115 415 397  HOH   HOH A . 
E 4 HOH   116 416 278  HOH   HOH A . 
E 4 HOH   117 417 1296 HOH   HOH A . 
E 4 HOH   118 418 195  HOH   HOH A . 
E 4 HOH   119 419 156  HOH   HOH A . 
E 4 HOH   120 420 25   HOH   HOH A . 
E 4 HOH   121 421 34   HOH   HOH A . 
E 4 HOH   122 422 125  HOH   HOH A . 
E 4 HOH   123 423 53   HOH   HOH A . 
E 4 HOH   124 424 7    HOH   HOH A . 
E 4 HOH   125 425 96   HOH   HOH A . 
E 4 HOH   126 426 123  HOH   HOH A . 
E 4 HOH   127 427 1279 HOH   HOH A . 
E 4 HOH   128 428 51   HOH   HOH A . 
E 4 HOH   129 429 582  HOH   HOH A . 
E 4 HOH   130 430 95   HOH   HOH A . 
E 4 HOH   131 431 13   HOH   HOH A . 
E 4 HOH   132 432 381  HOH   HOH A . 
E 4 HOH   133 433 1309 HOH   HOH A . 
E 4 HOH   134 434 1094 HOH   HOH A . 
E 4 HOH   135 435 115  HOH   HOH A . 
E 4 HOH   136 436 212  HOH   HOH A . 
E 4 HOH   137 437 1222 HOH   HOH A . 
E 4 HOH   138 438 16   HOH   HOH A . 
E 4 HOH   139 439 122  HOH   HOH A . 
E 4 HOH   140 440 333  HOH   HOH A . 
E 4 HOH   141 441 1286 HOH   HOH A . 
E 4 HOH   142 442 40   HOH   HOH A . 
E 4 HOH   143 443 73   HOH   HOH A . 
E 4 HOH   144 444 71   HOH   HOH A . 
E 4 HOH   145 445 70   HOH   HOH A . 
E 4 HOH   146 446 1189 HOH   HOH A . 
E 4 HOH   147 447 80   HOH   HOH A . 
E 4 HOH   148 448 1238 HOH   HOH A . 
E 4 HOH   149 449 94   HOH   HOH A . 
E 4 HOH   150 450 97   HOH   HOH A . 
E 4 HOH   151 451 188  HOH   HOH A . 
E 4 HOH   152 452 944  HOH   HOH A . 
E 4 HOH   153 453 17   HOH   HOH A . 
E 4 HOH   154 454 104  HOH   HOH A . 
E 4 HOH   155 455 952  HOH   HOH A . 
E 4 HOH   156 456 1119 HOH   HOH A . 
E 4 HOH   157 457 576  HOH   HOH A . 
E 4 HOH   158 458 79   HOH   HOH A . 
E 4 HOH   159 459 14   HOH   HOH A . 
E 4 HOH   160 460 330  HOH   HOH A . 
E 4 HOH   161 461 6    HOH   HOH A . 
E 4 HOH   162 462 1134 HOH   HOH A . 
E 4 HOH   163 463 107  HOH   HOH A . 
E 4 HOH   164 464 163  HOH   HOH A . 
E 4 HOH   165 465 509  HOH   HOH A . 
E 4 HOH   166 466 726  HOH   HOH A . 
E 4 HOH   167 467 10   HOH   HOH A . 
E 4 HOH   168 468 408  HOH   HOH A . 
E 4 HOH   169 469 756  HOH   HOH A . 
E 4 HOH   170 470 361  HOH   HOH A . 
E 4 HOH   171 471 126  HOH   HOH A . 
E 4 HOH   172 472 280  HOH   HOH A . 
E 4 HOH   173 473 63   HOH   HOH A . 
E 4 HOH   174 474 556  HOH   HOH A . 
E 4 HOH   175 475 319  HOH   HOH A . 
E 4 HOH   176 476 801  HOH   HOH A . 
E 4 HOH   177 477 250  HOH   HOH A . 
E 4 HOH   178 478 1276 HOH   HOH A . 
E 4 HOH   179 479 1307 HOH   HOH A . 
E 4 HOH   180 480 135  HOH   HOH A . 
E 4 HOH   181 481 2    HOH   HOH A . 
E 4 HOH   182 482 342  HOH   HOH A . 
E 4 HOH   183 483 1306 HOH   HOH A . 
E 4 HOH   184 484 1287 HOH   HOH A . 
E 4 HOH   185 485 202  HOH   HOH A . 
E 4 HOH   186 486 370  HOH   HOH A . 
E 4 HOH   187 487 3    HOH   HOH A . 
E 4 HOH   188 488 695  HOH   HOH A . 
E 4 HOH   189 489 18   HOH   HOH A . 
E 4 HOH   190 490 224  HOH   HOH A . 
E 4 HOH   191 491 267  HOH   HOH A . 
E 4 HOH   192 492 919  HOH   HOH A . 
E 4 HOH   193 493 674  HOH   HOH A . 
E 4 HOH   194 494 521  HOH   HOH A . 
E 4 HOH   195 495 318  HOH   HOH A . 
E 4 HOH   196 496 1299 HOH   HOH A . 
E 4 HOH   197 497 326  HOH   HOH A . 
E 4 HOH   198 498 315  HOH   HOH A . 
E 4 HOH   199 499 309  HOH   HOH A . 
E 4 HOH   200 500 1314 HOH   HOH A . 
E 4 HOH   201 501 331  HOH   HOH A . 
E 4 HOH   202 502 805  HOH   HOH A . 
E 4 HOH   203 503 1284 HOH   HOH A . 
E 4 HOH   204 504 711  HOH   HOH A . 
E 4 HOH   205 505 263  HOH   HOH A . 
E 4 HOH   206 506 152  HOH   HOH A . 
E 4 HOH   207 507 941  HOH   HOH A . 
E 4 HOH   208 508 208  HOH   HOH A . 
E 4 HOH   209 509 356  HOH   HOH A . 
E 4 HOH   210 510 12   HOH   HOH A . 
E 4 HOH   211 511 1071 HOH   HOH A . 
E 4 HOH   212 512 350  HOH   HOH A . 
E 4 HOH   213 513 180  HOH   HOH A . 
E 4 HOH   214 514 363  HOH   HOH A . 
E 4 HOH   215 515 371  HOH   HOH A . 
E 4 HOH   216 516 313  HOH   HOH A . 
E 4 HOH   217 517 429  HOH   HOH A . 
E 4 HOH   218 518 376  HOH   HOH A . 
E 4 HOH   219 519 185  HOH   HOH A . 
E 4 HOH   220 520 772  HOH   HOH A . 
E 4 HOH   221 521 1074 HOH   HOH A . 
E 4 HOH   222 522 346  HOH   HOH A . 
E 4 HOH   223 523 1292 HOH   HOH A . 
E 4 HOH   224 524 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 549  HOH   HOH B . 
F 4 HOH   3   203 276  HOH   HOH B . 
F 4 HOH   4   204 240  HOH   HOH B . 
F 4 HOH   5   205 531  HOH   HOH B . 
F 4 HOH   6   206 1249 HOH   HOH B . 
F 4 HOH   7   207 232  HOH   HOH B . 
F 4 HOH   8   208 364  HOH   HOH B . 
F 4 HOH   9   209 900  HOH   HOH B . 
F 4 HOH   10  210 758  HOH   HOH B . 
F 4 HOH   11  211 398  HOH   HOH B . 
F 4 HOH   12  212 654  HOH   HOH B . 
F 4 HOH   13  213 358  HOH   HOH B . 
F 4 HOH   14  214 452  HOH   HOH B . 
F 4 HOH   15  215 264  HOH   HOH B . 
F 4 HOH   16  216 743  HOH   HOH B . 
F 4 HOH   17  217 50   HOH   HOH B . 
F 4 HOH   18  218 120  HOH   HOH B . 
F 4 HOH   19  219 343  HOH   HOH B . 
F 4 HOH   20  220 353  HOH   HOH B . 
F 4 HOH   21  221 332  HOH   HOH B . 
F 4 HOH   22  222 444  HOH   HOH B . 
F 4 HOH   23  223 131  HOH   HOH B . 
F 4 HOH   24  224 1312 HOH   HOH B . 
F 4 HOH   25  225 166  HOH   HOH B . 
F 4 HOH   26  226 128  HOH   HOH B . 
F 4 HOH   27  227 723  HOH   HOH B . 
F 4 HOH   28  228 205  HOH   HOH B . 
F 4 HOH   29  229 54   HOH   HOH B . 
F 4 HOH   30  230 75   HOH   HOH B . 
F 4 HOH   31  231 325  HOH   HOH B . 
F 4 HOH   32  232 82   HOH   HOH B . 
F 4 HOH   33  233 172  HOH   HOH B . 
F 4 HOH   34  234 127  HOH   HOH B . 
F 4 HOH   35  235 272  HOH   HOH B . 
F 4 HOH   36  236 1140 HOH   HOH B . 
F 4 HOH   37  237 1278 HOH   HOH B . 
F 4 HOH   38  238 60   HOH   HOH B . 
F 4 HOH   39  239 110  HOH   HOH B . 
F 4 HOH   40  240 181  HOH   HOH B . 
F 4 HOH   41  241 282  HOH   HOH B . 
F 4 HOH   42  242 1    HOH   HOH B . 
F 4 HOH   43  243 69   HOH   HOH B . 
F 4 HOH   44  244 72   HOH   HOH B . 
F 4 HOH   45  245 52   HOH   HOH B . 
F 4 HOH   46  246 9    HOH   HOH B . 
F 4 HOH   47  247 300  HOH   HOH B . 
F 4 HOH   48  248 14   HOH   HOH B . 
F 4 HOH   49  249 41   HOH   HOH B . 
F 4 HOH   50  250 31   HOH   HOH B . 
F 4 HOH   51  251 30   HOH   HOH B . 
F 4 HOH   52  252 129  HOH   HOH B . 
F 4 HOH   53  253 143  HOH   HOH B . 
F 4 HOH   54  254 133  HOH   HOH B . 
F 4 HOH   55  255 231  HOH   HOH B . 
F 4 HOH   56  256 144  HOH   HOH B . 
F 4 HOH   57  257 59   HOH   HOH B . 
F 4 HOH   58  258 150  HOH   HOH B . 
F 4 HOH   59  259 62   HOH   HOH B . 
F 4 HOH   60  260 47   HOH   HOH B . 
F 4 HOH   61  261 103  HOH   HOH B . 
F 4 HOH   62  262 271  HOH   HOH B . 
F 4 HOH   63  263 10   HOH   HOH B . 
F 4 HOH   64  264 347  HOH   HOH B . 
F 4 HOH   65  265 84   HOH   HOH B . 
F 4 HOH   66  266 20   HOH   HOH B . 
F 4 HOH   67  267 61   HOH   HOH B . 
F 4 HOH   68  268 391  HOH   HOH B . 
F 4 HOH   69  269 114  HOH   HOH B . 
F 4 HOH   70  270 252  HOH   HOH B . 
F 4 HOH   71  271 243  HOH   HOH B . 
F 4 HOH   72  272 387  HOH   HOH B . 
F 4 HOH   73  273 221  HOH   HOH B . 
F 4 HOH   74  274 242  HOH   HOH B . 
F 4 HOH   75  275 77   HOH   HOH B . 
F 4 HOH   76  276 11   HOH   HOH B . 
F 4 HOH   77  277 175  HOH   HOH B . 
F 4 HOH   78  278 117  HOH   HOH B . 
F 4 HOH   79  279 1277 HOH   HOH B . 
F 4 HOH   80  280 1106 HOH   HOH B . 
F 4 HOH   81  281 287  HOH   HOH B . 
F 4 HOH   82  282 43   HOH   HOH B . 
F 4 HOH   83  283 235  HOH   HOH B . 
F 4 HOH   84  284 1066 HOH   HOH B . 
F 4 HOH   85  285 88   HOH   HOH B . 
F 4 HOH   86  286 22   HOH   HOH B . 
F 4 HOH   87  287 89   HOH   HOH B . 
F 4 HOH   88  288 302  HOH   HOH B . 
F 4 HOH   89  289 13   HOH   HOH B . 
F 4 HOH   90  290 106  HOH   HOH B . 
F 4 HOH   91  291 416  HOH   HOH B . 
F 4 HOH   92  292 147  HOH   HOH B . 
F 4 HOH   93  293 316  HOH   HOH B . 
F 4 HOH   94  294 1305 HOH   HOH B . 
F 4 HOH   95  295 99   HOH   HOH B . 
F 4 HOH   96  296 704  HOH   HOH B . 
F 4 HOH   97  297 38   HOH   HOH B . 
F 4 HOH   98  298 299  HOH   HOH B . 
F 4 HOH   99  299 137  HOH   HOH B . 
F 4 HOH   100 300 1126 HOH   HOH B . 
F 4 HOH   101 301 160  HOH   HOH B . 
F 4 HOH   102 302 112  HOH   HOH B . 
F 4 HOH   103 303 216  HOH   HOH B . 
F 4 HOH   104 304 635  HOH   HOH B . 
F 4 HOH   105 305 142  HOH   HOH B . 
F 4 HOH   106 306 297  HOH   HOH B . 
F 4 HOH   107 307 311  HOH   HOH B . 
F 4 HOH   108 308 101  HOH   HOH B . 
F 4 HOH   109 309 215  HOH   HOH B . 
F 4 HOH   110 310 32   HOH   HOH B . 
F 4 HOH   111 311 1285 HOH   HOH B . 
F 4 HOH   112 312 170  HOH   HOH B . 
F 4 HOH   113 313 118  HOH   HOH B . 
F 4 HOH   114 314 220  HOH   HOH B . 
F 4 HOH   115 315 48   HOH   HOH B . 
F 4 HOH   116 316 37   HOH   HOH B . 
F 4 HOH   117 317 23   HOH   HOH B . 
F 4 HOH   118 318 341  HOH   HOH B . 
F 4 HOH   119 319 91   HOH   HOH B . 
F 4 HOH   120 320 445  HOH   HOH B . 
F 4 HOH   121 321 44   HOH   HOH B . 
F 4 HOH   122 322 1274 HOH   HOH B . 
F 4 HOH   123 323 177  HOH   HOH B . 
F 4 HOH   124 324 1291 HOH   HOH B . 
F 4 HOH   125 325 28   HOH   HOH B . 
F 4 HOH   126 326 161  HOH   HOH B . 
F 4 HOH   127 327 100  HOH   HOH B . 
F 4 HOH   128 328 141  HOH   HOH B . 
F 4 HOH   129 329 29   HOH   HOH B . 
F 4 HOH   130 330 197  HOH   HOH B . 
F 4 HOH   131 331 55   HOH   HOH B . 
F 4 HOH   132 332 98   HOH   HOH B . 
F 4 HOH   133 333 717  HOH   HOH B . 
F 4 HOH   134 334 339  HOH   HOH B . 
F 4 HOH   135 335 207  HOH   HOH B . 
F 4 HOH   136 336 182  HOH   HOH B . 
F 4 HOH   137 337 334  HOH   HOH B . 
F 4 HOH   138 338 65   HOH   HOH B . 
F 4 HOH   139 339 234  HOH   HOH B . 
F 4 HOH   140 340 1294 HOH   HOH B . 
F 4 HOH   141 341 1293 HOH   HOH B . 
F 4 HOH   142 342 362  HOH   HOH B . 
F 4 HOH   143 343 619  HOH   HOH B . 
F 4 HOH   144 344 463  HOH   HOH B . 
F 4 HOH   145 345 90   HOH   HOH B . 
F 4 HOH   146 346 178  HOH   HOH B . 
F 4 HOH   147 347 960  HOH   HOH B . 
F 4 HOH   148 348 191  HOH   HOH B . 
F 4 HOH   149 349 1046 HOH   HOH B . 
F 4 HOH   150 350 304  HOH   HOH B . 
F 4 HOH   151 351 203  HOH   HOH B . 
F 4 HOH   152 352 623  HOH   HOH B . 
F 4 HOH   153 353 1304 HOH   HOH B . 
F 4 HOH   154 354 335  HOH   HOH B . 
F 4 HOH   155 355 1280 HOH   HOH B . 
F 4 HOH   156 356 541  HOH   HOH B . 
F 4 HOH   157 357 87   HOH   HOH B . 
F 4 HOH   158 358 290  HOH   HOH B . 
F 4 HOH   159 359 1077 HOH   HOH B . 
F 4 HOH   160 360 479  HOH   HOH B . 
F 4 HOH   161 361 389  HOH   HOH B . 
F 4 HOH   162 362 718  HOH   HOH B . 
F 4 HOH   163 363 1072 HOH   HOH B . 
F 4 HOH   164 364 283  HOH   HOH B . 
F 4 HOH   165 365 898  HOH   HOH B . 
F 4 HOH   166 366 373  HOH   HOH B . 
F 4 HOH   167 367 1316 HOH   HOH B . 
F 4 HOH   168 368 615  HOH   HOH B . 
F 4 HOH   169 369 340  HOH   HOH B . 
F 4 HOH   170 370 1303 HOH   HOH B . 
F 4 HOH   171 371 667  HOH   HOH B . 
F 4 HOH   172 372 291  HOH   HOH B . 
F 4 HOH   173 373 310  HOH   HOH B . 
F 4 HOH   174 374 190  HOH   HOH B . 
F 4 HOH   175 375 431  HOH   HOH B . 
F 4 HOH   176 376 149  HOH   HOH B . 
F 4 HOH   177 377 1173 HOH   HOH B . 
F 4 HOH   178 378 183  HOH   HOH B . 
F 4 HOH   179 379 1000 HOH   HOH B . 
F 4 HOH   180 380 418  HOH   HOH B . 
F 4 HOH   181 381 1163 HOH   HOH B . 
F 4 HOH   182 382 176  HOH   HOH B . 
F 4 HOH   183 383 1311 HOH   HOH B . 
F 4 HOH   184 384 424  HOH   HOH B . 
F 4 HOH   185 385 491  HOH   HOH B . 
F 4 HOH   186 386 470  HOH   HOH B . 
F 4 HOH   187 387 248  HOH   HOH B . 
F 4 HOH   188 388 265  HOH   HOH B . 
F 4 HOH   189 389 981  HOH   HOH B . 
F 4 HOH   190 390 1298 HOH   HOH B . 
F 4 HOH   191 391 184  HOH   HOH B . 
F 4 HOH   192 392 360  HOH   HOH B . 
F 4 HOH   193 393 410  HOH   HOH B . 
F 4 HOH   194 394 355  HOH   HOH B . 
F 4 HOH   195 395 566  HOH   HOH B . 
F 4 HOH   196 396 314  HOH   HOH B . 
F 4 HOH   197 397 274  HOH   HOH B . 
F 4 HOH   198 398 157  HOH   HOH B . 
F 4 HOH   199 399 792  HOH   HOH B . 
F 4 HOH   200 400 321  HOH   HOH B . 
F 4 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HEW 
_cell.length_a           88.869 
_cell.length_b           88.869 
_cell.length_c           39.560 
_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                         7HEW 
_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          7HEW 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.85 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-24 
_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                     7HEW 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.430 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165334 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.200 
_reflns.pdbx_Rmerge_I_obs            0.041 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.500 
_reflns.B_iso_Wilson_estimate        11.810 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.045 
_reflns.pdbx_Rpim_I_all              0.018 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1050078 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 32373 7189 ? 1.410 ? ? ? 4.500 ? 0.800  ? ? ? ? ? ? 87.400 1.591 0.717 0.542 
1 2 5.480 44.430 ? 7574  1098 ? 0.024 ? ? ? 6.900 ? 59.400 ? ? ? ? ? ? 99.900 0.026 0.010 0.999 
# 
_refine.entry_id                                 7HEW 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.4300 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.1600 
_refine.ls_number_reflns_obs                     165218 
_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                          0.1425 
_refine.ls_R_factor_R_work                       0.1418 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1570 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7967 
_refine.ls_number_reflns_R_work                  157251 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.0333 
_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                            0.1100 
_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                                63.200 
_refine.B_iso_min                                8.980 
_refine.pdbx_overall_phase_error                 17.1700 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.4300 
_refine_hist.pdbx_number_atoms_ligand         33 
_refine_hist.number_atoms_solvent             425 
_refine_hist.number_atoms_total               3000 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           16.11 
_refine_hist.pdbx_B_iso_mean_solvent          30.42 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 84.0000  4407 . 0.4148 0.4052 . 224 0.0000 4631 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 94.0000  4970 . 0.3358 0.3138 . 238 0.0000 5208 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5230 . 0.2888 0.2880 . 231 0.0000 5461 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5196 . 0.2482 0.2423 . 284 0.0000 5480 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5227 . 0.2260 0.2393 . 321 0.0000 5548 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5282 . 0.2221 0.2438 . 259 0.0000 5541 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5281 . 0.1988 0.2220 . 261 0.0000 5542 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5235 . 0.1840 0.2066 . 260 0.0000 5495 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5274 . 0.1664 0.1899 . 284 0.0000 5558 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5287 . 0.1545 0.1632 . 240 0.0000 5527 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5258 . 0.1414 0.1613 . 248 0.0000 5506 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5293 . 0.1337 0.1638 . 263 0.0000 5556 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5211 . 0.1231 0.1591 . 297 0.0000 5508 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5281 . 0.1196 0.1404 . 245 0.0000 5526 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5268 . 0.1216 0.1372 . 262 0.0000 5530 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5277 . 0.1250 0.1453 . 273 0.0000 5550 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5240 . 0.1261 0.1460 . 282 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5247 . 0.1317 0.1475 . 275 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5307 . 0.1242 0.1562 . 253 0.0000 5560 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5261 . 0.1225 0.1461 . 260 0.0000 5521 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5323 . 0.1178 0.1227 . 257 0.0000 5580 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5254 . 0.1141 0.1273 . 280 0.0000 5534 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5266 . 0.1160 0.1337 . 263 0.0000 5529 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5341 . 0.1214 0.1464 . 266 0.0000 5607 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5279 . 0.1283 0.1362 . 256 0.0000 5535 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5296 . 0.1308 0.1345 . 282 0.0000 5578 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5294 . 0.1359 0.1388 . 281 0.0000 5575 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5319 . 0.1359 0.1436 . 292 0.0000 5611 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5350 . 0.1482 0.1719 . 260 0.0000 5610 . 'X-RAY DIFFRACTION' 
3.1100 44.4300 30 100.0000 5497 . 0.1468 0.1679 . 270 0.0000 5767 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEW 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003697' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEW 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HEW A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEW 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 7HEW SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEW MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEW SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEW MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O ALA A 154 ? O ALA A 154 N ALA A 124 ? N ALA A 124 
AA2 1 2 N ASN A 37  ? N ASN A 37  O LEU A 93  ? O LEU A 93  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HEW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    91 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    305 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.60 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.60   -133.28 
2 1 SER A 128 ? B 68.01   -4.43   
3 1 ASP A 157 ? B -164.35 115.46  
4 1 SER A 167 ? B -108.00 54.72   
5 1 HIS B 86  ? ? 57.46   -127.76 
# 
_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 522 ? 5.82 . 
2 1 O ? A HOH 523 ? 5.94 . 
3 1 O ? A HOH 524 ? 7.50 . 
4 1 O ? B HOH 401 ? 6.36 . 
# 
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 
A1A99 N2   N  Y N 1   
A1A99 C3   C  N R 2   
A1A99 C6   C  Y N 3   
A1A99 C9   C  Y N 4   
A1A99 C1   C  N N 5   
A1A99 C10  C  Y N 6   
A1A99 C11  C  Y N 7   
A1A99 C2   C  N N 8   
A1A99 C4   C  N N 9   
A1A99 C5   C  N N 10  
A1A99 C7   C  Y N 11  
A1A99 C8   C  Y N 12  
A1A99 N1   N  N N 13  
A1A99 N3   N  Y N 14  
A1A99 N4   N  Y N 15  
A1A99 O1   O  N N 16  
A1A99 H2   H  N N 17  
A1A99 H1   H  N N 18  
A1A99 H3   H  N N 19  
A1A99 H14  H  N N 20  
A1A99 H15  H  N N 21  
A1A99 H4   H  N N 22  
A1A99 H5   H  N N 23  
A1A99 H7   H  N N 24  
A1A99 H8   H  N N 25  
A1A99 H6   H  N N 26  
A1A99 H9   H  N N 27  
A1A99 H10  H  N N 28  
A1A99 H13  H  N N 29  
A1A99 H12  H  N N 30  
A1A99 H16  H  N N 31  
A1A99 H11  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 
A1A99 C4  C3   sing N N 1   
A1A99 C3  C5   sing N N 2   
A1A99 C3  C2   sing N N 3   
A1A99 C3  N1   sing N N 4   
A1A99 C1  C2   sing N N 5   
A1A99 C5  O1   sing N N 6   
A1A99 N1  C6   sing N N 7   
A1A99 C10 C9   sing Y N 8   
A1A99 C10 C11  doub Y N 9   
A1A99 C6  C9   doub Y N 10  
A1A99 C6  N2   sing Y N 11  
A1A99 C9  C8   sing Y N 12  
A1A99 N2  C7   doub Y N 13  
A1A99 C11 N4   sing Y N 14  
A1A99 C8  N4   sing Y N 15  
A1A99 C8  N3   doub Y N 16  
A1A99 C7  N3   sing Y N 17  
A1A99 C1  H2   sing N N 18  
A1A99 C1  H1   sing N N 19  
A1A99 C1  H3   sing N N 20  
A1A99 C10 H14  sing N N 21  
A1A99 C11 H15  sing N N 22  
A1A99 C2  H4   sing N N 23  
A1A99 C2  H5   sing N N 24  
A1A99 C4  H7   sing N N 25  
A1A99 C4  H8   sing N N 26  
A1A99 C4  H6   sing N N 27  
A1A99 C5  H9   sing N N 28  
A1A99 C5  H10  sing N N 29  
A1A99 C7  H13  sing N N 30  
A1A99 N1  H12  sing N N 31  
A1A99 N4  H16  sing N N 32  
A1A99 O1  H11  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                    7HEW 
_atom_sites.fract_transf_matrix[1][1]   0.011253 
_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]   0.011253 
_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]   0.025278 
_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   ? 19.773 -16.309 22.273  0.50 51.73 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.645 -16.273 22.411  0.50 51.87 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.797 -15.242 22.453  0.50 51.49 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.710 -15.171 22.598  0.50 51.60 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.437 -13.888 22.165  0.50 50.41 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.381 -13.843 22.264  0.50 50.48 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.564 -13.624 22.584  0.50 50.71 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.482 -13.559 22.736  0.50 50.81 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.173 -15.287 23.862  0.50 52.09 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.135 -15.161 24.030  0.50 52.20 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.141 -14.179 24.028  0.50 52.29 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.177 -13.991 24.213  0.50 52.39 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.542 -16.649 24.118  0.50 52.27 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.437 -16.480 24.331  0.50 52.39 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 18.080 -15.365 21.815  0.50 61.82 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.967 -15.284 21.989  0.50 61.95 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.869 -15.151 24.524  0.50 62.54 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.861 -15.055 24.664  0.50 62.67 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.646 -14.330 24.849  0.50 62.78 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.678 -14.118 25.035  0.50 62.90 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.597 -13.324 24.072  0.50 62.78 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.686 -13.167 24.261  0.50 62.90 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.536 -14.195 23.271  0.50 62.78 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.568 -13.962 23.459  0.50 62.90 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.092 -16.632 24.977  0.50 62.76 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.033 -16.430 25.212  0.50 62.90 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.902 -16.837 23.413  0.50 62.76 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.753 -16.634 23.661  0.50 62.90 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.238 -17.325 24.122  0.50 62.76 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.091 -17.196 24.307  0.50 62.90 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.714 -13.036 21.440  1.00 48.75 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.177 -11.696 21.101  1.00 45.05 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 18.044 -10.701 21.341  1.00 41.61 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.929 -11.076 21.717  1.00 41.46 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.725 -11.624 19.667  1.00 44.57 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.695 -11.998 18.624  1.00 44.00 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.586 -11.464 18.609  1.00 43.75 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.058 -12.924 17.742  1.00 43.88 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.932 -13.218 21.128  0.50 58.53 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.973 -13.250 21.056  0.50 58.53 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.904 -11.464 21.694  1.00 54.10 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 20.019 -10.715 19.488  1.00 53.52 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.474 -12.234 19.584  1.00 53.52 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.511 -13.171 17.126  1.00 52.69 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.842 -13.276 17.785  1.00 52.69 ?  4   ASN   A HD22 1 
ATOM   46   N  N    . SER   A 1 5   ? 18.334 -9.420  21.115  1.00 37.99 ?  5   SER   A N    1 
ATOM   47   C  CA   . SER   A 1 5   ? 17.446 -8.334  21.513  1.00 34.47 ?  5   SER   A CA   1 
ATOM   48   C  C    . SER   A 1 5   ? 16.540 -7.838  20.388  1.00 29.68 ?  5   SER   A C    1 
ATOM   49   O  O    . SER   A 1 5   ? 15.830 -6.845  20.574  1.00 30.25 ?  5   SER   A O    1 
ATOM   50   C  CB   . SER   A 1 5   ? 18.254 -7.176  22.107  1.00 35.82 ?  5   SER   A CB   1 
ATOM   51   O  OG   . SER   A 1 5   ? 19.215 -6.695  21.184  1.00 36.34 ?  5   SER   A OG   1 
ATOM   52   H  H    . SER   A 1 5   ? 19.052 -9.153  20.721  1.00 45.62 ?  5   SER   A H    1 
ATOM   53   H  HA   . SER   A 1 5   ? 16.867 -8.659  22.214  1.00 41.40 ?  5   SER   A HA   1 
ATOM   54   H  HB2  . SER   A 1 5   ? 17.651 -6.451  22.337  1.00 43.02 ?  5   SER   A HB2  1 
ATOM   55   H  HB3  . SER   A 1 5   ? 18.713 -7.486  22.907  1.00 43.02 ?  5   SER   A HB3  1 
ATOM   56   H  HG   . SER   A 1 5   ? 19.653 -6.062  21.529  1.00 43.64 ?  5   SER   A HG   1 
ATOM   57   N  N    A PHE   A 1 6   ? 16.556 -8.508  19.235  0.50 26.50 ?  6   PHE   A N    1 
ATOM   58   N  N    B PHE   A 1 6   ? 16.527 -8.497  19.234  0.50 27.21 ?  6   PHE   A N    1 
ATOM   59   C  CA   A PHE   A 1 6   ? 15.657 -8.164  18.142  0.50 23.37 ?  6   PHE   A CA   1 
ATOM   60   C  CA   B PHE   A 1 6   ? 15.619 -8.082  18.171  0.50 24.76 ?  6   PHE   A CA   1 
ATOM   61   C  C    A PHE   A 1 6   ? 14.237 -8.581  18.498  0.50 22.92 ?  6   PHE   A C    1 
ATOM   62   C  C    B PHE   A 1 6   ? 14.176 -8.358  18.586  0.50 24.69 ?  6   PHE   A C    1 
ATOM   63   O  O    A PHE   A 1 6   ? 14.008 -9.703  18.961  0.50 23.77 ?  6   PHE   A O    1 
ATOM   64   O  O    B PHE   A 1 6   ? 13.855 -9.453  19.055  0.50 25.47 ?  6   PHE   A O    1 
ATOM   65   C  CB   A PHE   A 1 6   ? 16.095 -8.877  16.865  0.50 21.23 ?  6   PHE   A CB   1 
ATOM   66   C  CB   B PHE   A 1 6   ? 15.953 -8.815  16.875  0.50 22.82 ?  6   PHE   A CB   1 
ATOM   67   C  CG   A PHE   A 1 6   ? 17.349 -8.317  16.254  0.50 19.41 ?  6   PHE   A CG   1 
ATOM   68   C  CG   B PHE   A 1 6   ? 17.280 -8.419  16.277  0.50 21.26 ?  6   PHE   A CG   1 
ATOM   69   C  CD1  A PHE   A 1 6   ? 17.323 -7.114  15.568  0.50 18.82 ?  6   PHE   A CD1  1 
ATOM   70   C  CD1  B PHE   A 1 6   ? 17.402 -7.257  15.532  0.50 20.57 ?  6   PHE   A CD1  1 
ATOM   71   C  CD2  A PHE   A 1 6   ? 18.551 -8.998  16.358  0.50 19.24 ?  6   PHE   A CD2  1 
ATOM   72   C  CD2  B PHE   A 1 6   ? 18.402 -9.211  16.458  0.50 21.09 ?  6   PHE   A CD2  1 
ATOM   73   C  CE1  A PHE   A 1 6   ? 18.475 -6.597  15.002  0.50 18.63 ?  6   PHE   A CE1  1 
ATOM   74   C  CE1  B PHE   A 1 6   ? 18.620 -6.891  14.980  0.50 20.25 ?  6   PHE   A CE1  1 
ATOM   75   C  CE2  A PHE   A 1 6   ? 19.704 -8.489  15.794  0.50 19.03 ?  6   PHE   A CE2  1 
ATOM   76   C  CE2  B PHE   A 1 6   ? 19.621 -8.849  15.909  0.50 20.70 ?  6   PHE   A CE2  1 
ATOM   77   C  CZ   A PHE   A 1 6   ? 19.666 -7.286  15.115  0.50 18.69 ?  6   PHE   A CZ   1 
ATOM   78   C  CZ   B PHE   A 1 6   ? 19.730 -7.688  15.169  0.50 20.31 ?  6   PHE   A CZ   1 
ATOM   79   H  H    A PHE   A 1 6   ? 17.076 -9.171  19.068  0.50 31.83 ?  6   PHE   A H    1 
ATOM   80   H  H    B PHE   A 1 6   ? 17.022 -9.174  19.047  0.50 32.68 ?  6   PHE   A H    1 
ATOM   81   H  HA   A PHE   A 1 6   ? 15.673 -7.209  17.992  0.50 28.08 ?  6   PHE   A HA   1 
ATOM   82   H  HA   B PHE   A 1 6   ? 15.715 -7.131  18.024  0.50 29.74 ?  6   PHE   A HA   1 
ATOM   83   H  HB2  A PHE   A 1 6   ? 16.256 -9.814  17.072  0.50 25.51 ?  6   PHE   A HB2  1 
ATOM   84   H  HB2  B PHE   A 1 6   ? 15.975 -9.769  17.054  0.50 27.42 ?  6   PHE   A HB2  1 
ATOM   85   H  HB3  A PHE   A 1 6   ? 15.385 -8.806  16.210  0.50 25.51 ?  6   PHE   A HB3  1 
ATOM   86   H  HB3  B PHE   A 1 6   ? 15.260 -8.620  16.224  0.50 27.42 ?  6   PHE   A HB3  1 
ATOM   87   H  HD1  A PHE   A 1 6   ? 16.521 -6.647  15.491  0.50 22.62 ?  6   PHE   A HD1  1 
ATOM   88   H  HD1  B PHE   A 1 6   ? 16.658 -6.715  15.402  0.50 24.72 ?  6   PHE   A HD1  1 
ATOM   89   H  HD2  A PHE   A 1 6   ? 18.580 -9.808  16.817  0.50 23.12 ?  6   PHE   A HD2  1 
ATOM   90   H  HD2  B PHE   A 1 6   ? 18.335 -9.993  16.957  0.50 25.34 ?  6   PHE   A HD2  1 
ATOM   91   H  HE1  A PHE   A 1 6   ? 18.446 -5.786  14.544  0.50 22.38 ?  6   PHE   A HE1  1 
ATOM   92   H  HE1  B PHE   A 1 6   ? 18.692 -6.109  14.482  0.50 24.34 ?  6   PHE   A HE1  1 
ATOM   93   H  HE2  A PHE   A 1 6   ? 20.506 -8.952  15.874  0.50 22.86 ?  6   PHE   A HE2  1 
ATOM   94   H  HE2  B PHE   A 1 6   ? 20.369 -9.389  16.038  0.50 24.88 ?  6   PHE   A HE2  1 
ATOM   95   H  HZ   A PHE   A 1 6   ? 20.441 -6.938  14.735  0.50 22.46 ?  6   PHE   A HZ   1 
ATOM   96   H  HZ   B PHE   A 1 6   ? 20.550 -7.445  14.799  0.50 24.41 ?  6   PHE   A HZ   1 
ATOM   97   N  N    A SER   A 1 7   ? 13.279 -7.686  18.264  0.50 21.73 ?  7   SER   A N    1 
ATOM   98   N  N    B SER   A 1 7   ? 13.302 -7.363  18.408  0.50 23.84 ?  7   SER   A N    1 
ATOM   99   C  CA   A SER   A 1 7   ? 11.912 -7.861  18.736  0.50 21.36 ?  7   SER   A CA   1 
ATOM   100  C  CA   B SER   A 1 7   ? 11.949 -7.398  18.949  0.50 23.90 ?  7   SER   A CA   1 
ATOM   101  C  C    A SER   A 1 7   ? 10.921 -7.608  17.609  0.50 19.70 ?  7   SER   A C    1 
ATOM   102  C  C    B SER   A 1 7   ? 10.934 -7.147  17.842  0.50 22.59 ?  7   SER   A C    1 
ATOM   103  O  O    A SER   A 1 7   ? 11.102 -6.693  16.799  0.50 19.87 ?  7   SER   A O    1 
ATOM   104  O  O    B SER   A 1 7   ? 11.165 -6.324  16.952  0.50 22.71 ?  7   SER   A O    1 
ATOM   105  C  CB   A SER   A 1 7   ? 11.618 -6.898  19.891  0.50 22.49 ?  7   SER   A CB   1 
ATOM   106  C  CB   B SER   A 1 7   ? 11.786 -6.344  20.062  0.50 25.00 ?  7   SER   A CB   1 
ATOM   107  O  OG   A SER   A 1 7   ? 10.257 -6.966  20.277  0.50 23.50 ?  7   SER   A OG   1 
ATOM   108  O  OG   B SER   A 1 7   ? 10.546 -6.481  20.729  0.50 26.04 ?  7   SER   A OG   1 
ATOM   109  H  H    A SER   A 1 7   ? 13.403 -6.963  17.818  0.50 26.11 ?  7   SER   A H    1 
ATOM   110  H  H    B SER   A 1 7   ? 13.469 -6.648  17.957  0.50 28.64 ?  7   SER   A H    1 
ATOM   111  H  HA   A SER   A 1 7   ? 11.792 -8.767  19.055  0.50 25.67 ?  7   SER   A HA   1 
ATOM   112  H  HA   B SER   A 1 7   ? 11.766 -8.268  19.331  0.50 28.71 ?  7   SER   A HA   1 
ATOM   113  H  HB2  A SER   A 1 7   ? 12.168 -7.140  20.652  0.50 27.02 ?  7   SER   A HB2  1 
ATOM   114  H  HB2  B SER   A 1 7   ? 12.507 -6.452  20.707  0.50 30.03 ?  7   SER   A HB2  1 
ATOM   115  H  HB3  A SER   A 1 7   ? 11.831 -5.991  19.607  0.50 27.02 ?  7   SER   A HB3  1 
ATOM   116  H  HB3  B SER   A 1 7   ? 11.823 -5.458  19.674  0.50 30.03 ?  7   SER   A HB3  1 
ATOM   117  H  HG   A SER   A 1 7   ? 10.110 -6.419  20.900  0.50 28.23 ?  7   SER   A HG   1 
ATOM   118  H  HG   B SER   A 1 7   ? 10.480 -5.913  21.347  0.50 31.29 ?  7   SER   A HG   1 
ATOM   119  N  N    A GLY   A 1 8   ? 9.871  -8.429  17.567  0.50 18.33 ?  8   GLY   A N    1 
ATOM   120  N  N    B GLY   A 1 8   ? 9.814  -7.868  17.896  0.50 21.59 ?  8   GLY   A N    1 
ATOM   121  C  CA   A GLY   A 1 8   ? 8.767  -8.199  16.656  0.50 17.58 ?  8   GLY   A CA   1 
ATOM   122  C  CA   B GLY   A 1 8   ? 8.726  -7.660  16.962  0.50 20.54 ?  8   GLY   A CA   1 
ATOM   123  C  C    A GLY   A 1 8   ? 8.966  -8.673  15.235  0.50 16.77 ?  8   GLY   A C    1 
ATOM   124  C  C    B GLY   A 1 8   ? 8.926  -8.245  15.585  0.50 19.17 ?  8   GLY   A C    1 
ATOM   125  O  O    A GLY   A 1 8   ? 8.221  -8.246  14.346  0.50 17.59 ?  8   GLY   A O    1 
ATOM   126  O  O    B GLY   A 1 8   ? 8.160  -7.909  14.675  0.50 19.95 ?  8   GLY   A O    1 
ATOM   127  H  H    A GLY   A 1 8   ? 9.779  -9.129  18.064  0.50 22.03 ?  8   GLY   A H    1 
ATOM   128  H  H    B GLY   A 1 8   ? 9.664  -8.488  18.471  0.50 25.94 ?  8   GLY   A H    1 
ATOM   129  H  HA2  A GLY   A 1 8   ? 7.978  -8.643  17.010  0.50 21.13 ?  8   GLY   A HA2  1 
ATOM   130  H  HA2  B GLY   A 1 8   ? 7.916  -8.050  17.326  0.50 24.68 ?  8   GLY   A HA2  1 
ATOM   131  H  HA3  A GLY   A 1 8   ? 8.585  -7.251  16.625  0.50 21.13 ?  8   GLY   A HA3  1 
ATOM   132  H  HA3  B GLY   A 1 8   ? 8.573  -6.705  16.858  0.50 24.68 ?  8   GLY   A HA3  1 
ATOM   133  N  N    A TYR   A 1 9   ? 9.938  -9.548  14.986  0.50 15.03 ?  9   TYR   A N    1 
ATOM   134  N  N    B TYR   A 1 9   ? 9.921  -9.106  15.394  0.50 17.28 ?  9   TYR   A N    1 
ATOM   135  C  CA   A TYR   A 1 9   ? 10.197 -10.060 13.649  0.50 13.90 ?  9   TYR   A CA   1 
ATOM   136  C  CA   B TYR   A 1 9   ? 10.181 -9.681  14.084  0.50 15.79 ?  9   TYR   A CA   1 
ATOM   137  C  C    A TYR   A 1 9   ? 9.332  -11.279 13.349  0.50 13.72 ?  9   TYR   A C    1 
ATOM   138  C  C    B TYR   A 1 9   ? 9.328  -10.923 13.848  0.50 14.88 ?  9   TYR   A C    1 
ATOM   139  O  O    A TYR   A 1 9   ? 9.051  -12.102 14.225  0.50 14.58 ?  9   TYR   A O    1 
ATOM   140  O  O    B TYR   A 1 9   ? 9.008  -11.675 14.773  0.50 16.02 ?  9   TYR   A O    1 
ATOM   141  C  CB   A TYR   A 1 9   ? 11.669 -10.457 13.503  0.50 13.62 ?  9   TYR   A CB   1 
ATOM   142  C  CB   B TYR   A 1 9   ? 11.664 -10.037 13.925  0.50 15.90 ?  9   TYR   A CB   1 
ATOM   143  C  CG   A TYR   A 1 9   ? 12.592 -9.271  13.348  0.50 13.50 ?  9   TYR   A CG   1 
ATOM   144  C  CG   B TYR   A 1 9   ? 12.562 -8.837  13.705  0.50 15.47 ?  9   TYR   A CG   1 
ATOM   145  C  CD1  A TYR   A 1 9   ? 12.945 -8.494  14.443  0.50 13.76 ?  9   TYR   A CD1  1 
ATOM   146  C  CD1  B TYR   A 1 9   ? 12.857 -7.972  14.747  0.50 15.69 ?  9   TYR   A CD1  1 
ATOM   147  C  CD2  A TYR   A 1 9   ? 13.097 -8.920  12.101  0.50 13.64 ?  9   TYR   A CD2  1 
ATOM   148  C  CD2  B TYR   A 1 9   ? 13.104 -8.564  12.453  0.50 14.97 ?  9   TYR   A CD2  1 
ATOM   149  C  CE1  A TYR   A 1 9   ? 13.774 -7.398  14.303  0.50 14.33 ?  9   TYR   A CE1  1 
ATOM   150  C  CE1  B TYR   A 1 9   ? 13.665 -6.869  14.555  0.50 15.56 ?  9   TYR   A CE1  1 
ATOM   151  C  CE2  A TYR   A 1 9   ? 13.928 -7.829  11.951  0.50 13.86 ?  9   TYR   A CE2  1 
ATOM   152  C  CE2  B TYR   A 1 9   ? 13.917 -7.458  12.250  0.50 15.01 ?  9   TYR   A CE2  1 
ATOM   153  C  CZ   A TYR   A 1 9   ? 14.264 -7.073  13.053  0.50 14.64 ?  9   TYR   A CZ   1 
ATOM   154  C  CZ   B TYR   A 1 9   ? 14.189 -6.616  13.306  0.50 15.47 ?  9   TYR   A CZ   1 
ATOM   155  O  OH   A TYR   A 1 9   ? 15.091 -5.990  12.898  0.50 15.59 ?  9   TYR   A OH   1 
ATOM   156  O  OH   B TYR   A 1 9   ? 14.987 -5.513  13.115  0.50 16.21 ?  9   TYR   A OH   1 
ATOM   157  H  H    A TYR   A 1 9   ? 10.462 -9.871  15.585  0.50 18.07 ?  9   TYR   A H    1 
ATOM   158  H  H    B TYR   A 1 9   ? 10.461 -9.373  16.012  0.50 20.76 ?  9   TYR   A H    1 
ATOM   159  H  HA   A TYR   A 1 9   ? 10.000 -9.377  12.992  0.50 16.71 ?  9   TYR   A HA   1 
ATOM   160  H  HA   B TYR   A 1 9   ? 9.958  -9.021  13.405  0.50 18.98 ?  9   TYR   A HA   1 
ATOM   161  H  HB2  A TYR   A 1 9   ? 11.944 -10.954 14.290  0.50 16.38 ?  9   TYR   A HB2  1 
ATOM   162  H  HB2  B TYR   A 1 9   ? 11.968 -10.493 14.723  0.50 19.12 ?  9   TYR   A HB2  1 
ATOM   163  H  HB3  A TYR   A 1 9   ? 11.762 -11.014 12.714  0.50 16.38 ?  9   TYR   A HB3  1 
ATOM   164  H  HB3  B TYR   A 1 9   ? 11.757 -10.619 13.156  0.50 19.12 ?  9   TYR   A HB3  1 
ATOM   165  H  HD1  A TYR   A 1 9   ? 12.612 -8.712  15.285  0.50 16.54 ?  9   TYR   A HD1  1 
ATOM   166  H  HD1  B TYR   A 1 9   ? 12.501 -8.136  15.589  0.50 18.86 ?  9   TYR   A HD1  1 
ATOM   167  H  HD2  A TYR   A 1 9   ? 12.868 -9.432  11.356  0.50 16.41 ?  9   TYR   A HD2  1 
ATOM   168  H  HD2  B TYR   A 1 9   ? 12.918 -9.130  11.739  0.50 18.00 ?  9   TYR   A HD2  1 
ATOM   169  H  HE1  A TYR   A 1 9   ? 14.006 -6.889  15.045  0.50 17.23 ?  9   TYR   A HE1  1 
ATOM   170  H  HE1  B TYR   A 1 9   ? 13.854 -6.298  15.265  0.50 18.71 ?  9   TYR   A HE1  1 
ATOM   171  H  HE2  A TYR   A 1 9   ? 14.264 -7.610  11.111  0.50 16.66 ?  9   TYR   A HE2  1 
ATOM   172  H  HE2  B TYR   A 1 9   ? 14.278 -7.285  11.406  0.50 18.05 ?  9   TYR   A HE2  1 
ATOM   173  H  HH   A TYR   A 1 9   ? 15.218 -5.619  13.641  0.50 18.74 ?  9   TYR   A HH   1 
ATOM   174  H  HH   B TYR   A 1 9   ? 15.084 -5.090  13.836  0.50 19.48 ?  9   TYR   A HH   1 
ATOM   175  N  N    A LEU   A 1 10  ? 8.938  -11.402 12.082  0.50 13.20 ?  10  LEU   A N    1 
ATOM   176  N  N    B LEU   A 1 10  ? 8.947  -11.110 12.588  0.50 14.01 ?  10  LEU   A N    1 
ATOM   177  C  CA   A LEU   A 1 10  ? 8.327  -12.621 11.576  0.50 12.90 ?  10  LEU   A CA   1 
ATOM   178  C  CA   B LEU   A 1 10  ? 8.311  -12.332 12.121  0.50 13.96 ?  10  LEU   A CA   1 
ATOM   179  C  C    A LEU   A 1 10  ? 9.439  -13.557 11.120  0.50 12.53 ?  10  LEU   A C    1 
ATOM   180  C  C    B LEU   A 1 10  ? 9.399  -13.287 11.642  0.50 13.24 ?  10  LEU   A C    1 
ATOM   181  O  O    A LEU   A 1 10  ? 10.375 -13.132 10.433  0.50 12.17 ?  10  LEU   A O    1 
ATOM   182  O  O    B LEU   A 1 10  ? 10.309 -12.882 10.912  0.50 13.16 ?  10  LEU   A O    1 
ATOM   183  C  CB   A LEU   A 1 10  ? 7.409  -12.303 10.398  0.50 13.68 ?  10  LEU   A CB   1 
ATOM   184  C  CB   B LEU   A 1 10  ? 7.368  -12.002 10.963  0.50 14.98 ?  10  LEU   A CB   1 
ATOM   185  C  CG   A LEU   A 1 10  ? 6.719  -13.509 9.757   0.50 15.60 ?  10  LEU   A CG   1 
ATOM   186  C  CG   B LEU   A 1 10  ? 6.606  -13.175 10.348  0.50 16.48 ?  10  LEU   A CG   1 
ATOM   187  C  CD1  A LEU   A 1 10  ? 5.679  -14.094 10.695  0.50 16.43 ?  10  LEU   A CD1  1 
ATOM   188  C  CD1  B LEU   A 1 10  ? 5.572  -13.715 11.322  0.50 17.47 ?  10  LEU   A CD1  1 
ATOM   189  C  CD2  A LEU   A 1 10  ? 6.092  -13.142 8.429   0.50 16.36 ?  10  LEU   A CD2  1 
ATOM   190  C  CD2  B LEU   A 1 10  ? 5.952  -12.746 9.046   0.50 18.04 ?  10  LEU   A CD2  1 
ATOM   191  H  H    A LEU   A 1 10  ? 9.030  -10.793 11.478  0.50 15.87 ?  10  LEU   A H    1 
ATOM   192  H  H    B LEU   A 1 10  ? 9.042  -10.515 11.974  0.50 16.84 ?  10  LEU   A H    1 
ATOM   193  H  HA   A LEU   A 1 10  ? 7.816  -13.059 12.275  0.50 15.51 ?  10  LEU   A HA   1 
ATOM   194  H  HA   B LEU   A 1 10  ? 7.800  -12.742 12.840  0.50 16.78 ?  10  LEU   A HA   1 
ATOM   195  H  HB2  A LEU   A 1 10  ? 6.713  -11.704 10.706  0.50 16.45 ?  10  LEU   A HB2  1 
ATOM   196  H  HB2  B LEU   A 1 10  ? 6.704  -11.363 11.274  0.50 18.01 ?  10  LEU   A HB2  1 
ATOM   197  H  HB3  A LEU   A 1 10  ? 7.931  -11.871 9.707   0.50 16.45 ?  10  LEU   A HB3  1 
ATOM   198  H  HB3  B LEU   A 1 10  ? 7.890  -11.597 10.253  0.50 18.01 ?  10  LEU   A HB3  1 
ATOM   199  H  HG   A LEU   A 1 10  ? 7.377  -14.202 9.585   0.50 18.75 ?  10  LEU   A HG   1 
ATOM   200  H  HG   B LEU   A 1 10  ? 7.229  -13.892 10.149  0.50 19.80 ?  10  LEU   A HG   1 
ATOM   201  H  HD11 A LEU   A 1 10  ? 5.314  -14.904 10.302  0.50 19.75 ?  10  LEU   A HD11 1 
ATOM   202  H  HD11 B LEU   A 1 10  ? 5.138  -14.488 10.927  0.50 21.00 ?  10  LEU   A HD11 1 
ATOM   203  H  HD12 A LEU   A 1 10  ? 6.096  -14.302 11.546  0.50 19.75 ?  10  LEU   A HD12 1 
ATOM   204  H  HD12 B LEU   A 1 10  ? 6.014  -13.969 12.146  0.50 21.00 ?  10  LEU   A HD12 1 
ATOM   205  H  HD13 A LEU   A 1 10  ? 4.970  -13.445 10.827  0.50 19.75 ?  10  LEU   A HD13 1 
ATOM   206  H  HD13 B LEU   A 1 10  ? 4.915  -13.023 11.499  0.50 21.00 ?  10  LEU   A HD13 1 
ATOM   207  H  HD21 A LEU   A 1 10  ? 5.661  -13.927 8.058   0.50 19.66 ?  10  LEU   A HD21 1 
ATOM   208  H  HD21 B LEU   A 1 10  ? 5.469  -13.500 8.672   0.50 21.68 ?  10  LEU   A HD21 1 
ATOM   209  H  HD22 A LEU   A 1 10  ? 5.437  -12.443 8.577   0.50 19.66 ?  10  LEU   A HD22 1 
ATOM   210  H  HD22 B LEU   A 1 10  ? 5.339  -12.017 9.226   0.50 21.68 ?  10  LEU   A HD22 1 
ATOM   211  H  HD23 A LEU   A 1 10  ? 6.786  -12.828 7.832   0.50 19.66 ?  10  LEU   A HD23 1 
ATOM   212  H  HD23 B LEU   A 1 10  ? 6.641  -12.456 8.429   0.50 21.68 ?  10  LEU   A HD23 1 
ATOM   213  N  N    A LYS   A 1 11  ? 9.335  -14.824 11.504  0.50 12.43 ?  11  LYS   A N    1 
ATOM   214  N  N    B LYS   A 1 11  ? 9.313  -14.545 12.059  0.50 13.59 ?  11  LYS   A N    1 
ATOM   215  C  CA   A LYS   A 1 11  ? 10.335 -15.827 11.170  0.50 12.48 ?  11  LYS   A CA   1 
ATOM   216  C  CA   B LYS   A 1 11  ? 10.279 -15.554 11.642  0.50 13.60 ?  11  LYS   A CA   1 
ATOM   217  C  C    A LYS   A 1 11  ? 9.981  -16.442 9.823   0.50 12.36 ?  11  LYS   A C    1 
ATOM   218  C  C    B LYS   A 1 11  ? 9.872  -16.089 10.272  0.50 13.11 ?  11  LYS   A C    1 
ATOM   219  O  O    A LYS   A 1 11  ? 8.928  -17.069 9.689   0.50 13.98 ?  11  LYS   A O    1 
ATOM   220  O  O    B LYS   A 1 11  ? 8.744  -16.562 10.097  0.50 13.64 ?  11  LYS   A O    1 
ATOM   221  C  CB   A LYS   A 1 11  ? 10.346 -16.890 12.267  0.50 12.73 ?  11  LYS   A CB   1 
ATOM   222  C  CB   B LYS   A 1 11  ? 10.330 -16.675 12.679  0.50 13.93 ?  11  LYS   A CB   1 
ATOM   223  C  CG   A LYS   A 1 11  ? 11.333 -18.012 12.074  0.50 13.45 ?  11  LYS   A CG   1 
ATOM   224  C  CG   B LYS   A 1 11  ? 11.383 -17.756 12.425  0.50 13.87 ?  11  LYS   A CG   1 
ATOM   225  C  CD   A LYS   A 1 11  ? 11.368 -18.876 13.326  0.50 14.53 ?  11  LYS   A CD   1 
ATOM   226  C  CD   B LYS   A 1 11  ? 11.538 -18.681 13.642  0.50 13.75 ?  11  LYS   A CD   1 
ATOM   227  C  CE   A LYS   A 1 11  ? 12.365 -20.005 13.208  0.50 14.81 ?  11  LYS   A CE   1 
ATOM   228  C  CE   B LYS   A 1 11  ? 12.543 -19.816 13.412  0.50 13.64 ?  11  LYS   A CE   1 
ATOM   229  N  NZ   A LYS   A 1 11  ? 13.738 -19.503 12.947  0.50 14.71 ?  11  LYS   A NZ   1 
ATOM   230  N  NZ   B LYS   A 1 11  ? 13.940 -19.327 13.257  0.50 13.79 ?  11  LYS   A NZ   1 
ATOM   231  H  H    A LYS   A 1 11  ? 8.674  -15.139 11.965  0.50 14.95 ?  11  LYS   A H    1 
ATOM   232  H  H    B LYS   A 1 11  ? 8.692  -14.832 12.580  0.50 16.35 ?  11  LYS   A H    1 
ATOM   233  H  HA   A LYS   A 1 11  ? 11.210 -15.420 11.115  0.50 15.01 ?  11  LYS   A HA   1 
ATOM   234  H  HA   B LYS   A 1 11  ? 11.153 -15.142 11.570  0.50 16.36 ?  11  LYS   A HA   1 
ATOM   235  H  HB2  A LYS   A 1 11  ? 10.557 -16.458 13.110  0.50 15.31 ?  11  LYS   A HB2  1 
ATOM   236  H  HB2  B LYS   A 1 11  ? 10.516 -16.275 13.544  0.50 16.75 ?  11  LYS   A HB2  1 
ATOM   237  H  HB3  A LYS   A 1 11  ? 9.461  -17.287 12.321  0.50 15.31 ?  11  LYS   A HB3  1 
ATOM   238  H  HB3  B LYS   A 1 11  ? 9.461  -17.103 12.702  0.50 16.75 ?  11  LYS   A HB3  1 
ATOM   239  H  HG2  A LYS   A 1 11  ? 11.058 -18.564 11.325  0.50 16.17 ?  11  LYS   A HG2  1 
ATOM   240  H  HG2  B LYS   A 1 11  ? 11.109 -18.290 11.665  0.50 16.67 ?  11  LYS   A HG2  1 
ATOM   241  H  HG3  A LYS   A 1 11  ? 12.217 -17.644 11.924  0.50 16.17 ?  11  LYS   A HG3  1 
ATOM   242  H  HG3  B LYS   A 1 11  ? 12.237 -17.332 12.251  0.50 16.67 ?  11  LYS   A HG3  1 
ATOM   243  H  HD2  A LYS   A 1 11  ? 11.619 -18.324 14.084  0.50 17.47 ?  11  LYS   A HD2  1 
ATOM   244  H  HD2  B LYS   A 1 11  ? 11.844 -18.159 14.399  0.50 16.53 ?  11  LYS   A HD2  1 
ATOM   245  H  HD3  A LYS   A 1 11  ? 10.487 -19.258 13.471  0.50 17.47 ?  11  LYS   A HD3  1 
ATOM   246  H  HD3  B LYS   A 1 11  ? 10.677 -19.083 13.844  0.50 16.53 ?  11  LYS   A HD3  1 
ATOM   247  H  HE2  A LYS   A 1 11  ? 12.375 -20.508 14.037  0.50 17.80 ?  11  LYS   A HE2  1 
ATOM   248  H  HE2  B LYS   A 1 11  ? 12.522 -20.420 14.172  0.50 16.40 ?  11  LYS   A HE2  1 
ATOM   249  H  HE3  A LYS   A 1 11  ? 12.105 -20.577 12.470  0.50 17.80 ?  11  LYS   A HE3  1 
ATOM   250  H  HE3  B LYS   A 1 11  ? 12.305 -20.296 12.603  0.50 16.40 ?  11  LYS   A HE3  1 
ATOM   251  H  HZ1  A LYS   A 1 11  ? 14.311 -20.182 12.935  0.50 17.69 ?  11  LYS   A HZ1  1 
ATOM   252  H  HZ1  B LYS   A 1 11  ? 14.491 -20.014 13.116  0.50 16.58 ?  11  LYS   A HZ1  1 
ATOM   253  H  HZ2  A LYS   A 1 11  ? 13.766 -19.085 12.162  0.50 17.69 ?  11  LYS   A HZ2  1 
ATOM   254  H  HZ2  B LYS   A 1 11  ? 13.993 -18.769 12.566  0.50 16.58 ?  11  LYS   A HZ2  1 
ATOM   255  H  HZ3  A LYS   A 1 11  ? 13.979 -18.932 13.587  0.50 17.69 ?  11  LYS   A HZ3  1 
ATOM   256  H  HZ3  B LYS   A 1 11  ? 14.197 -18.900 13.994  0.50 16.58 ?  11  LYS   A HZ3  1 
ATOM   257  N  N    A LEU   A 1 12  ? 10.853 -16.271 8.828   0.50 11.57 ?  12  LEU   A N    1 
ATOM   258  N  N    B LEU   A 1 12  ? 10.771 -15.990 9.293   0.50 13.00 ?  12  LEU   A N    1 
ATOM   259  C  CA   A LEU   A 1 12  ? 10.607 -16.870 7.518   0.50 11.81 ?  12  LEU   A CA   1 
ATOM   260  C  CA   B LEU   A 1 12  ? 10.498 -16.512 7.957   0.50 13.23 ?  12  LEU   A CA   1 
ATOM   261  C  C    A LEU   A 1 12  ? 11.210 -18.264 7.382   0.50 12.00 ?  12  LEU   A C    1 
ATOM   262  C  C    B LEU   A 1 12  ? 11.067 -17.907 7.733   0.50 12.55 ?  12  LEU   A C    1 
ATOM   263  O  O    A LEU   A 1 12  ? 10.584 -19.150 6.791   0.50 12.36 ?  12  LEU   A O    1 
ATOM   264  O  O    B LEU   A 1 12  ? 10.410 -18.747 7.106   0.50 12.53 ?  12  LEU   A O    1 
ATOM   265  C  CB   A LEU   A 1 12  ? 11.148 -15.970 6.401   0.50 11.76 ?  12  LEU   A CB   1 
ATOM   266  C  CB   B LEU   A 1 12  ? 11.046 -15.566 6.882   0.50 14.24 ?  12  LEU   A CB   1 
ATOM   267  C  CG   A LEU   A 1 12  ? 10.492 -14.601 6.220   0.50 13.01 ?  12  LEU   A CG   1 
ATOM   268  C  CG   B LEU   A 1 12  ? 10.380 -14.194 6.769   0.50 14.79 ?  12  LEU   A CG   1 
ATOM   269  C  CD1  A LEU   A 1 12  ? 11.208 -13.826 5.128   0.50 13.84 ?  12  LEU   A CD1  1 
ATOM   270  C  CD1  B LEU   A 1 12  ? 11.004 -13.400 5.628   0.50 15.40 ?  12  LEU   A CD1  1 
ATOM   271  C  CD2  A LEU   A 1 12  ? 9.011  -14.757 5.892   0.50 13.52 ?  12  LEU   A CD2  1 
ATOM   272  C  CD2  B LEU   A 1 12  ? 8.877  -14.342 6.571   0.50 15.26 ?  12  LEU   A CD2  1 
ATOM   273  H  H    A LEU   A 1 12  ? 11.586 -15.818 8.884   0.50 13.92 ?  12  LEU   A H    1 
ATOM   274  H  H    B LEU   A 1 12  ? 11.547 -15.610 9.376   0.50 15.64 ?  12  LEU   A H    1 
ATOM   275  H  HA   A LEU   A 1 12  ? 9.652  -16.956 7.394   0.50 14.21 ?  12  LEU   A HA   1 
ATOM   276  H  HA   B LEU   A 1 12  ? 9.539  -16.563 7.841   0.50 15.91 ?  12  LEU   A HA   1 
ATOM   277  H  HB2  A LEU   A 1 12  ? 12.089 -15.817 6.569   0.50 14.14 ?  12  LEU   A HB2  1 
ATOM   278  H  HB2  B LEU   A 1 12  ? 11.985 -15.409 7.060   0.50 17.12 ?  12  LEU   A HB2  1 
ATOM   279  H  HB3  A LEU   A 1 12  ? 11.049 -16.449 5.561   0.50 14.14 ?  12  LEU   A HB3  1 
ATOM   280  H  HB3  B LEU   A 1 12  ? 10.948 -15.997 6.020   0.50 17.12 ?  12  LEU   A HB3  1 
ATOM   281  H  HG   A LEU   A 1 12  ? 10.567 -14.103 7.047   0.50 15.65 ?  12  LEU   A HG   1 
ATOM   282  H  HG   B LEU   A 1 12  ? 10.525 -13.699 7.593   0.50 17.78 ?  12  LEU   A HG   1 
ATOM   283  H  HD11 A LEU   A 1 12  ? 10.781 -12.964 5.021   0.50 16.64 ?  12  LEU   A HD11 1 
ATOM   284  H  HD11 B LEU   A 1 12  ? 10.571 -12.533 5.573   0.50 18.52 ?  12  LEU   A HD11 1 
ATOM   285  H  HD12 A LEU   A 1 12  ? 12.137 -13.708 5.384   0.50 16.64 ?  12  LEU   A HD12 1 
ATOM   286  H  HD12 B LEU   A 1 12  ? 11.949 -13.288 5.804   0.50 18.52 ?  12  LEU   A HD12 1 
ATOM   287  H  HD13 A LEU   A 1 12  ? 11.156 -14.328 4.299   0.50 16.64 ?  12  LEU   A HD13 1 
ATOM   288  H  HD13 B LEU   A 1 12  ? 10.874 -13.888 4.800   0.50 18.52 ?  12  LEU   A HD13 1 
ATOM   289  H  HD21 A LEU   A 1 12  ? 8.644  -13.889 5.666   0.50 16.26 ?  12  LEU   A HD21 1 
ATOM   290  H  HD21 B LEU   A 1 12  ? 8.507  -13.489 6.299   0.50 18.35 ?  12  LEU   A HD21 1 
ATOM   291  H  HD22 A LEU   A 1 12  ? 8.915  -15.363 5.140   0.50 16.26 ?  12  LEU   A HD22 1 
ATOM   292  H  HD22 B LEU   A 1 12  ? 8.715  -15.010 5.887   0.50 18.35 ?  12  LEU   A HD22 1 
ATOM   293  H  HD23 A LEU   A 1 12  ? 8.549  -15.120 6.666   0.50 16.26 ?  12  LEU   A HD23 1 
ATOM   294  H  HD23 B LEU   A 1 12  ? 8.474  -14.624 7.409   0.50 18.35 ?  12  LEU   A HD23 1 
ATOM   295  N  N    A THR   A 1 13  ? 12.423 -18.462 7.894   0.50 12.70 ?  13  THR   A N    1 
ATOM   296  N  N    B THR   A 1 13  ? 12.282 -18.164 8.213   0.50 12.38 ?  13  THR   A N    1 
ATOM   297  C  CA   A THR   A 1 13  ? 13.127 -19.741 7.866   0.50 13.00 ?  13  THR   A CA   1 
ATOM   298  C  CA   B THR   A 1 13  ? 12.944 -19.450 8.037   0.50 13.11 ?  13  THR   A CA   1 
ATOM   299  C  C    A THR   A 1 13  ? 13.873 -19.892 9.187   0.50 13.58 ?  13  THR   A C    1 
ATOM   300  C  C    B THR   A 1 13  ? 13.766 -19.750 9.284   0.50 14.09 ?  13  THR   A C    1 
ATOM   301  O  O    A THR   A 1 13  ? 13.725 -19.080 10.105  0.50 13.81 ?  13  THR   A O    1 
ATOM   302  O  O    B THR   A 1 13  ? 13.738 -19.014 10.274  0.50 14.25 ?  13  THR   A O    1 
ATOM   303  C  CB   A THR   A 1 13  ? 14.121 -19.820 6.697   0.50 13.27 ?  13  THR   A CB   1 
ATOM   304  C  CB   B THR   A 1 13  ? 13.884 -19.449 6.824   0.50 13.33 ?  13  THR   A CB   1 
ATOM   305  O  OG1  A THR   A 1 13  ? 15.190 -18.893 6.918   0.50 13.37 ?  13  THR   A OG1  1 
ATOM   306  O  OG1  B THR   A 1 13  ? 14.970 -18.554 7.078   0.50 13.54 ?  13  THR   A OG1  1 
ATOM   307  C  CG2  A THR   A 1 13  ? 13.447 -19.519 5.367   0.50 13.91 ?  13  THR   A CG2  1 
ATOM   308  C  CG2  B THR   A 1 13  ? 13.162 -19.047 5.540   0.50 13.63 ?  13  THR   A CG2  1 
ATOM   309  H  H    A THR   A 1 13  ? 12.880 -17.846 8.270   0.50 15.28 ?  13  THR   A H    1 
ATOM   310  H  H    B THR   A 1 13  ? 12.754 -17.588 8.646   0.50 14.88 ?  13  THR   A H    1 
ATOM   311  H  HA   A THR   A 1 13  ? 12.488 -20.473 7.778   0.50 15.63 ?  13  THR   A HA   1 
ATOM   312  H  HA   B THR   A 1 13  ? 12.278 -20.145 7.921   0.50 15.77 ?  13  THR   A HA   1 
ATOM   313  H  HB   A THR   A 1 13  ? 14.487 -20.720 6.645   0.50 15.96 ?  13  THR   A HB   1 
ATOM   314  H  HB   B THR   A 1 13  ? 14.240 -20.341 6.699   0.50 16.03 ?  13  THR   A HB   1 
ATOM   315  H  HG1  A THR   A 1 13  ? 15.730 -18.926 6.273   0.50 16.07 ?  13  THR   A HG1  1 
ATOM   316  H  HG1  B THR   A 1 13  ? 15.485 -18.535 6.411   0.50 16.28 ?  13  THR   A HG1  1 
ATOM   317  H  HG21 A THR   A 1 13  ? 14.066 -19.685 4.636   0.50 16.73 ?  13  THR   A HG21 1 
ATOM   318  H  HG21 B THR   A 1 13  ? 13.765 -19.126 4.783   0.50 16.40 ?  13  THR   A HG21 1 
ATOM   319  H  HG22 A THR   A 1 13  ? 12.670 -20.091 5.251   0.50 16.73 ?  13  THR   A HG22 1 
ATOM   320  H  HG22 B THR   A 1 13  ? 12.400 -19.634 5.392   0.50 16.40 ?  13  THR   A HG22 1 
ATOM   321  H  HG23 A THR   A 1 13  ? 13.165 -18.594 5.339   0.50 16.73 ?  13  THR   A HG23 1 
ATOM   322  H  HG23 B THR   A 1 13  ? 12.849 -18.135 5.602   0.50 16.40 ?  13  THR   A HG23 1 
ATOM   323  N  N    A ASP   A 1 14  ? 14.706 -20.930 9.275   0.50 13.83 ?  14  ASP   A N    1 
ATOM   324  N  N    B ASP   A 1 14  ? 14.527 -20.842 9.207   0.50 14.56 ?  14  ASP   A N    1 
ATOM   325  C  CA   A ASP   A 1 14  ? 15.493 -21.150 10.482  0.50 14.12 ?  14  ASP   A CA   1 
ATOM   326  C  CA   B ASP   A 1 14  ? 15.445 -21.203 10.277  0.50 15.12 ?  14  ASP   A CA   1 
ATOM   327  C  C    A ASP   A 1 14  ? 16.272 -19.900 10.890  0.50 13.71 ?  14  ASP   A C    1 
ATOM   328  C  C    B ASP   A 1 14  ? 16.359 -20.044 10.657  0.50 13.79 ?  14  ASP   A C    1 
ATOM   329  O  O    A ASP   A 1 14  ? 16.385 -19.594 12.082  0.50 14.22 ?  14  ASP   A O    1 
ATOM   330  O  O    B ASP   A 1 14  ? 16.734 -19.916 11.828  0.50 13.99 ?  14  ASP   A O    1 
ATOM   331  C  CB   A ASP   A 1 14  ? 16.454 -22.311 10.252  0.50 15.78 ?  14  ASP   A CB   1 
ATOM   332  C  CB   B ASP   A 1 14  ? 16.285 -22.408 9.845   0.50 17.11 ?  14  ASP   A CB   1 
ATOM   333  C  CG   A ASP   A 1 14  ? 17.372 -22.531 11.419  0.50 18.71 ?  14  ASP   A CG   1 
ATOM   334  C  CG   B ASP   A 1 14  ? 17.172 -22.928 10.962  0.50 19.04 ?  14  ASP   A CG   1 
ATOM   335  O  OD1  A ASP   A 1 14  ? 16.878 -22.943 12.488  0.50 20.11 ?  14  ASP   A OD1  1 
ATOM   336  O  OD1  B ASP   A 1 14  ? 16.626 -23.349 12.006  0.50 19.52 ?  14  ASP   A OD1  1 
ATOM   337  O  OD2  A ASP   A 1 14  ? 18.582 -22.276 11.268  0.50 20.32 -1 14  ASP   A OD2  1 
ATOM   338  O  OD2  B ASP   A 1 14  ? 18.409 -22.925 10.795  0.50 20.66 -1 14  ASP   A OD2  1 
ATOM   339  H  H    A ASP   A 1 14  ? 14.846 -21.510 8.653   0.50 16.62 ?  14  ASP   A H    1 
ATOM   340  H  H    B ASP   A 1 14  ? 14.530 -21.377 8.541   0.50 17.51 ?  14  ASP   A H    1 
ATOM   341  H  HA   A ASP   A 1 14  ? 14.898 -21.386 11.212  0.50 16.97 ?  14  ASP   A HA   1 
ATOM   342  H  HA   B ASP   A 1 14  ? 14.938 -21.460 11.063  0.50 18.18 ?  14  ASP   A HA   1 
ATOM   343  H  HB2  A ASP   A 1 14  ? 15.936 -23.124 10.115  0.50 18.97 ?  14  ASP   A HB2  1 
ATOM   344  H  HB2  B ASP   A 1 14  ? 15.687 -23.132 9.578   0.50 20.56 ?  14  ASP   A HB2  1 
ATOM   345  H  HB3  A ASP   A 1 14  ? 16.994 -22.128 9.470   0.50 18.97 ?  14  ASP   A HB3  1 
ATOM   346  H  HB3  B ASP   A 1 14  ? 16.842 -22.154 9.091   0.50 20.56 ?  14  ASP   A HB3  1 
ATOM   347  N  N    A ASN   A 1 15  ? 16.814 -19.160 9.913   0.50 13.64 ?  15  ASN   A N    1 
ATOM   348  N  N    B ASN   A 1 15  ? 16.732 -19.187 9.693   0.50 12.71 ?  15  ASN   A N    1 
ATOM   349  C  CA   A ASN   A 1 15  ? 17.760 -18.082 10.182  0.50 13.81 ?  15  ASN   A CA   1 
ATOM   350  C  CA   B ASN   A 1 15  ? 17.760 -18.182 9.955   0.50 13.10 ?  15  ASN   A CA   1 
ATOM   351  C  C    A ASN   A 1 15  ? 17.354 -16.720 9.634   0.50 13.21 ?  15  ASN   A C    1 
ATOM   352  C  C    B ASN   A 1 15  ? 17.418 -16.764 9.498   0.50 13.30 ?  15  ASN   A C    1 
ATOM   353  O  O    A ASN   A 1 15  ? 18.000 -15.728 9.997   0.50 13.23 ?  15  ASN   A O    1 
ATOM   354  O  O    B ASN   A 1 15  ? 18.300 -15.897 9.543   0.50 13.49 ?  15  ASN   A O    1 
ATOM   355  C  CB   A ASN   A 1 15  ? 19.142 -18.424 9.598   0.50 13.88 ?  15  ASN   A CB   1 
ATOM   356  C  CB   B ASN   A 1 15  ? 19.124 -18.608 9.376   0.50 12.67 ?  15  ASN   A CB   1 
ATOM   357  C  CG   A ASN   A 1 15  ? 19.106 -18.599 8.093   0.50 14.06 ?  15  ASN   A CG   1 
ATOM   358  C  CG   B ASN   A 1 15  ? 19.130 -18.650 7.859   0.50 12.96 ?  15  ASN   A CG   1 
ATOM   359  O  OD1  A ASN   A 1 15  ? 18.248 -19.315 7.565   0.50 14.21 ?  15  ASN   A OD1  1 
ATOM   360  O  OD1  B ASN   A 1 15  ? 18.520 -19.533 7.248   0.50 13.25 ?  15  ASN   A OD1  1 
ATOM   361  N  ND2  A ASN   A 1 15  ? 20.021 -17.929 7.388   0.50 14.00 ?  15  ASN   A ND2  1 
ATOM   362  N  ND2  B ASN   A 1 15  ? 19.826 -17.697 7.242   0.50 12.94 ?  15  ASN   A ND2  1 
ATOM   363  H  H    A ASN   A 1 15  ? 16.651 -19.270 9.085   0.50 16.40 ?  15  ASN   A H    1 
ATOM   364  H  H    B ASN   A 1 15  ? 16.406 -19.177 8.895   0.50 15.28 ?  15  ASN   A H    1 
ATOM   365  H  HA   A ASN   A 1 15  ? 17.873 -17.993 11.148  0.50 16.61 ?  15  ASN   A HA   1 
ATOM   366  H  HA   B ASN   A 1 15  ? 17.876 -18.136 10.913  0.50 15.75 ?  15  ASN   A HA   1 
ATOM   367  H  HB2  A ASN   A 1 15  ? 19.763 -17.703 9.805   0.50 16.69 ?  15  ASN   A HB2  1 
ATOM   368  H  HB2  B ASN   A 1 15  ? 19.804 -17.969 9.661   0.50 15.24 ?  15  ASN   A HB2  1 
ATOM   369  H  HB3  A ASN   A 1 15  ? 19.459 -19.252 9.987   0.50 16.69 ?  15  ASN   A HB3  1 
ATOM   370  H  HB3  B ASN   A 1 15  ? 19.357 -19.494 9.706   0.50 15.24 ?  15  ASN   A HB3  1 
ATOM   371  H  HD21 A ASN   A 1 15  ? 20.036 -17.994 6.529   0.50 16.83 ?  15  ASN   A HD21 1 
ATOM   372  H  HD21 B ASN   A 1 15  ? 19.860 -17.684 6.385   0.50 15.56 ?  15  ASN   A HD21 1 
ATOM   373  H  HD22 A ASN   A 1 15  ? 20.603 -17.438 7.789   0.50 16.83 ?  15  ASN   A HD22 1 
ATOM   374  H  HD22 B ASN   A 1 15  ? 20.237 -17.096 7.701   0.50 15.56 ?  15  ASN   A HD22 1 
ATOM   375  N  N    A VAL   A 1 16  ? 16.340 -16.640 8.759   0.50 12.26 ?  16  VAL   A N    1 
ATOM   376  N  N    B VAL   A 1 16  ? 16.176 -16.477 9.104   0.50 13.04 ?  16  VAL   A N    1 
ATOM   377  C  CA   A VAL   A 1 16  ? 15.907 -15.387 8.136   0.50 11.88 ?  16  VAL   A CA   1 
ATOM   378  C  CA   B VAL   A 1 16  ? 15.821 -15.161 8.575   0.50 12.28 ?  16  VAL   A CA   1 
ATOM   379  C  C    A VAL   A 1 16  ? 14.628 -14.888 8.805   0.50 11.51 ?  16  VAL   A C    1 
ATOM   380  C  C    B VAL   A 1 16  ? 14.558 -14.651 9.263   0.50 12.11 ?  16  VAL   A C    1 
ATOM   381  O  O    A VAL   A 1 16  ? 13.620 -15.605 8.874   0.50 11.22 ?  16  VAL   A O    1 
ATOM   382  O  O    B VAL   A 1 16  ? 13.564 -15.378 9.381   0.50 12.33 ?  16  VAL   A O    1 
ATOM   383  C  CB   A VAL   A 1 16  ? 15.698 -15.545 6.618   0.50 12.46 ?  16  VAL   A CB   1 
ATOM   384  C  CB   B VAL   A 1 16  ? 15.657 -15.176 7.040   0.50 11.40 ?  16  VAL   A CB   1 
ATOM   385  C  CG1  A VAL   A 1 16  ? 15.200 -14.231 6.009   0.50 12.84 ?  16  VAL   A CG1  1 
ATOM   386  C  CG1  B VAL   A 1 16  ? 15.268 -13.793 6.524   0.50 10.94 ?  16  VAL   A CG1  1 
ATOM   387  C  CG2  A VAL   A 1 16  ? 16.976 -16.005 5.929   0.50 13.01 ?  16  VAL   A CG2  1 
ATOM   388  C  CG2  B VAL   A 1 16  ? 16.933 -15.655 6.359   0.50 12.71 ?  16  VAL   A CG2  1 
ATOM   389  H  H    A VAL   A 1 16  ? 15.894 -17.326 8.507   0.50 14.74 ?  16  VAL   A H    1 
ATOM   390  H  H    B VAL   A 1 16  ? 15.511 -17.023 9.147   0.50 15.68 ?  16  VAL   A H    1 
ATOM   391  H  HA   A VAL   A 1 16  ? 16.599 -14.720 8.272   0.50 14.29 ?  16  VAL   A HA   1 
ATOM   392  H  HA   B VAL   A 1 16  ? 16.536 -14.538 8.784   0.50 14.76 ?  16  VAL   A HA   1 
ATOM   393  H  HB   A VAL   A 1 16  ? 15.022 -16.229 6.467   0.50 14.99 ?  16  VAL   A HB   1 
ATOM   394  H  HB   B VAL   A 1 16  ? 14.946 -15.793 6.810   0.50 13.72 ?  16  VAL   A HB   1 
ATOM   395  H  HG11 A VAL   A 1 16  ? 15.253 -14.295 5.042   0.50 15.44 ?  16  VAL   A HG11 1 
ATOM   396  H  HG11 B VAL   A 1 16  ? 15.332 -13.790 5.558   0.50 13.17 ?  16  VAL   A HG11 1 
ATOM   397  H  HG12 A VAL   A 1 16  ? 14.279 -14.089 6.278   0.50 15.44 ?  16  VAL   A HG12 1 
ATOM   398  H  HG12 B VAL   A 1 16  ? 14.357 -13.599 6.795   0.50 13.17 ?  16  VAL   A HG12 1 
ATOM   399  H  HG13 A VAL   A 1 16  ? 15.758 -13.508 6.326   0.50 15.44 ?  16  VAL   A HG13 1 
ATOM   400  H  HG13 B VAL   A 1 16  ? 15.874 -13.136 6.899   0.50 13.17 ?  16  VAL   A HG13 1 
ATOM   401  H  HG21 A VAL   A 1 16  ? 16.883 -15.870 4.973   0.50 15.64 ?  16  VAL   A HG21 1 
ATOM   402  H  HG21 B VAL   A 1 16  ? 16.940 -15.344 5.439   0.50 15.28 ?  16  VAL   A HG21 1 
ATOM   403  H  HG22 A VAL   A 1 16  ? 17.720 -15.477 6.262   0.50 15.64 ?  16  VAL   A HG22 1 
ATOM   404  H  HG22 B VAL   A 1 16  ? 17.699 -15.300 6.835   0.50 15.28 ?  16  VAL   A HG22 1 
ATOM   405  H  HG23 A VAL   A 1 16  ? 17.126 -16.943 6.119   0.50 15.64 ?  16  VAL   A HG23 1 
ATOM   406  H  HG23 B VAL   A 1 16  ? 16.957 -16.624 6.380   0.50 15.28 ?  16  VAL   A HG23 1 
ATOM   407  N  N    A TYR   A 1 17  ? 14.658 -13.628 9.234   0.50 11.50 ?  17  TYR   A N    1 
ATOM   408  N  N    B TYR   A 1 17  ? 14.603 -13.385 9.688   0.50 11.85 ?  17  TYR   A N    1 
ATOM   409  C  CA   A TYR   A 1 17  ? 13.571 -12.948 9.919   0.50 11.44 ?  17  TYR   A CA   1 
ATOM   410  C  CA   B TYR   A 1 17  ? 13.533 -12.710 10.406  0.50 11.67 ?  17  TYR   A CA   1 
ATOM   411  C  C    A TYR   A 1 17  ? 13.307 -11.623 9.210   0.50 11.47 ?  17  TYR   A C    1 
ATOM   412  C  C    B TYR   A 1 17  ? 13.273 -11.375 9.728   0.50 11.41 ?  17  TYR   A C    1 
ATOM   413  O  O    A TYR   A 1 17  ? 14.197 -11.067 8.561   0.50 10.99 ?  17  TYR   A O    1 
ATOM   414  O  O    B TYR   A 1 17  ? 14.187 -10.795 9.139   0.50 11.12 ?  17  TYR   A O    1 
ATOM   415  C  CB   A TYR   A 1 17  ? 13.975 -12.670 11.370  0.50 12.15 ?  17  TYR   A CB   1 
ATOM   416  C  CB   B TYR   A 1 17  ? 13.953 -12.478 11.862  0.50 12.57 ?  17  TYR   A CB   1 
ATOM   417  C  CG   A TYR   A 1 17  ? 14.145 -13.916 12.214  0.50 13.43 ?  17  TYR   A CG   1 
ATOM   418  C  CG   B TYR   A 1 17  ? 14.206 -13.768 12.621  0.50 13.62 ?  17  TYR   A CG   1 
ATOM   419  C  CD1  A TYR   A 1 17  ? 15.311 -14.679 12.164  0.50 14.43 ?  17  TYR   A CD1  1 
ATOM   420  C  CD1  B TYR   A 1 17  ? 15.395 -14.478 12.468  0.50 14.71 ?  17  TYR   A CD1  1 
ATOM   421  C  CD2  A TYR   A 1 17  ? 13.133 -14.334 13.065  0.50 13.93 ?  17  TYR   A CD2  1 
ATOM   422  C  CD2  B TYR   A 1 17  ? 13.248 -14.284 13.481  0.50 14.33 ?  17  TYR   A CD2  1 
ATOM   423  C  CE1  A TYR   A 1 17  ? 15.452 -15.828 12.939  0.50 14.89 ?  17  TYR   A CE1  1 
ATOM   424  C  CE1  B TYR   A 1 17  ? 15.618 -15.668 13.155  0.50 15.63 ?  17  TYR   A CE1  1 
ATOM   425  C  CE2  A TYR   A 1 17  ? 13.265 -15.477 13.840  0.50 14.69 ?  17  TYR   A CE2  1 
ATOM   426  C  CE2  B TYR   A 1 17  ? 13.462 -15.471 14.172  0.50 15.16 ?  17  TYR   A CE2  1 
ATOM   427  C  CZ   A TYR   A 1 17  ? 14.426 -16.216 13.777  0.50 15.11 ?  17  TYR   A CZ   1 
ATOM   428  C  CZ   B TYR   A 1 17  ? 14.647 -16.157 14.008  0.50 15.55 ?  17  TYR   A CZ   1 
ATOM   429  O  OH   A TYR   A 1 17  ? 14.556 -17.346 14.552  0.50 15.96 ?  17  TYR   A OH   1 
ATOM   430  O  OH   B TYR   A 1 17  ? 14.858 -17.331 14.700  0.50 16.19 ?  17  TYR   A OH   1 
ATOM   431  H  H    A TYR   A 1 17  ? 15.342 -13.128 9.127   0.50 13.83 ?  17  TYR   A H    1 
ATOM   432  H  H    B TYR   A 1 17  ? 15.282 -12.861 9.551   0.50 14.25 ?  17  TYR   A H    1 
ATOM   433  H  HA   A TYR   A 1 17  ? 12.768 -13.504 9.909   0.50 13.76 ?  17  TYR   A HA   1 
ATOM   434  H  HA   B TYR   A 1 17  ? 12.721 -13.232 10.380  0.50 14.04 ?  17  TYR   A HA   1 
ATOM   435  H  HB2  A TYR   A 1 17  ? 14.820 -12.200 11.371  0.50 14.61 ?  17  TYR   A HB2  1 
ATOM   436  H  HB2  B TYR   A 1 17  ? 14.773 -11.961 11.868  0.50 15.12 ?  17  TYR   A HB2  1 
ATOM   437  H  HB3  A TYR   A 1 17  ? 13.291 -12.130 11.783  0.50 14.61 ?  17  TYR   A HB3  1 
ATOM   438  H  HB3  B TYR   A 1 17  ? 13.252 -11.990 12.323  0.50 15.12 ?  17  TYR   A HB3  1 
ATOM   439  H  HD1  A TYR   A 1 17  ? 16.005 -14.422 11.601  0.50 17.35 ?  17  TYR   A HD1  1 
ATOM   440  H  HD1  B TYR   A 1 17  ? 16.049 -14.152 11.891  0.50 17.68 ?  17  TYR   A HD1  1 
ATOM   441  H  HD2  A TYR   A 1 17  ? 12.345 -13.848 13.115  0.50 16.75 ?  17  TYR   A HD2  1 
ATOM   442  H  HD2  B TYR   A 1 17  ? 12.446 -13.827 13.595  0.50 17.23 ?  17  TYR   A HD2  1 
ATOM   443  H  HE1  A TYR   A 1 17  ? 16.241 -16.327 12.900  0.50 17.91 ?  17  TYR   A HE1  1 
ATOM   444  H  HE1  B TYR   A 1 17  ? 16.417 -16.133 13.041  0.50 18.79 ?  17  TYR   A HE1  1 
ATOM   445  H  HE2  A TYR   A 1 17  ? 12.576 -15.743 14.409  0.50 17.66 ?  17  TYR   A HE2  1 
ATOM   446  H  HE2  B TYR   A 1 17  ? 12.808 -15.801 14.744  0.50 18.23 ?  17  TYR   A HE2  1 
ATOM   447  H  HH   A TYR   A 1 17  ? 13.824 -17.531 14.920  0.50 19.19 ?  17  TYR   A HH   1 
ATOM   448  H  HH   B TYR   A 1 17  ? 15.620 -17.640 14.528  0.50 19.46 ?  17  TYR   A HH   1 
ATOM   449  N  N    A ILE   A 1 18  ? 12.085 -11.096 9.343   0.50 11.68 ?  18  ILE   A N    1 
ATOM   450  N  N    B ILE   A 1 18  ? 12.033 -10.875 9.803   0.50 11.74 ?  18  ILE   A N    1 
ATOM   451  C  CA   A ILE   A 1 18  ? 11.696 -9.905  8.587   0.50 11.84 ?  18  ILE   A CA   1 
ATOM   452  C  CA   B ILE   A 1 18  ? 11.658 -9.661  9.077   0.50 11.98 ?  18  ILE   A CA   1 
ATOM   453  C  C    A ILE   A 1 18  ? 10.718 -9.059  9.397   0.50 12.40 ?  18  ILE   A C    1 
ATOM   454  C  C    B ILE   A 1 18  ? 10.738 -8.784  9.919   0.50 12.15 ?  18  ILE   A C    1 
ATOM   455  O  O    A ILE   A 1 18  ? 9.899  -9.584  10.156  0.50 12.82 ?  18  ILE   A O    1 
ATOM   456  O  O    B ILE   A 1 18  ? 9.889  -9.284  10.668  0.50 12.66 ?  18  ILE   A O    1 
ATOM   457  C  CB   A ILE   A 1 18  ? 11.138 -10.305 7.200   0.50 11.72 ?  18  ILE   A CB   1 
ATOM   458  C  CB   B ILE   A 1 18  ? 11.036 -9.985  7.702   0.50 11.49 ?  18  ILE   A CB   1 
ATOM   459  C  CG1  A ILE   A 1 18  ? 11.065 -9.092  6.274   0.50 12.00 ?  18  ILE   A CG1  1 
ATOM   460  C  CG1  B ILE   A 1 18  ? 10.955 -8.732  6.827   0.50 12.35 ?  18  ILE   A CG1  1 
ATOM   461  C  CG2  A ILE   A 1 18  ? 9.784  -11.008 7.341   0.50 12.04 ?  18  ILE   A CG2  1 
ATOM   462  C  CG2  B ILE   A 1 18  ? 9.667  -10.639 7.864   0.50 12.00 ?  18  ILE   A CG2  1 
ATOM   463  C  CD1  A ILE   A 1 18  ? 10.742 -9.454  4.843   0.50 13.21 ?  18  ILE   A CD1  1 
ATOM   464  C  CD1  B ILE   A 1 18  ? 10.674 -9.041  5.377   0.50 13.61 ?  18  ILE   A CD1  1 
ATOM   465  H  H    A ILE   A 1 18  ? 11.476 -11.417 9.865   0.50 14.04 ?  18  ILE   A H    1 
ATOM   466  H  H    B ILE   A 1 18  ? 11.389 -11.224 10.261  0.50 14.13 ?  18  ILE   A H    1 
ATOM   467  H  HA   A ILE   A 1 18  ? 12.492 -9.378  8.440   0.50 14.24 ?  18  ILE   A HA   1 
ATOM   468  H  HA   B ILE   A 1 18  ? 12.463 -9.148  8.914   0.50 14.41 ?  18  ILE   A HA   1 
ATOM   469  H  HB   A ILE   A 1 18  ? 11.756 -10.943 6.806   0.50 14.09 ?  18  ILE   A HB   1 
ATOM   470  H  HB   B ILE   A 1 18  ? 11.616 -10.613 7.256   0.50 13.82 ?  18  ILE   A HB   1 
ATOM   471  H  HG12 A ILE   A 1 18  ? 10.377 -8.495  6.595   0.50 14.44 ?  18  ILE   A HG12 1 
ATOM   472  H  HG12 B ILE   A 1 18  ? 10.240 -8.159  7.151   0.50 14.85 ?  18  ILE   A HG12 1 
ATOM   473  H  HG13 A ILE   A 1 18  ? 11.926 -8.645  6.280   0.50 14.44 ?  18  ILE   A HG13 1 
ATOM   474  H  HG13 B ILE   A 1 18  ? 11.800 -8.256  6.870   0.50 14.85 ?  18  ILE   A HG13 1 
ATOM   475  H  HG21 A ILE   A 1 18  ? 9.543  -11.404 6.486   0.50 14.49 ?  18  ILE   A HG21 1 
ATOM   476  H  HG21 B ILE   A 1 18  ? 9.379  -10.985 7.002   0.50 14.44 ?  18  ILE   A HG21 1 
ATOM   477  H  HG22 A ILE   A 1 18  ? 9.855  -11.705 8.014   0.50 14.49 ?  18  ILE   A HG22 1 
ATOM   478  H  HG22 B ILE   A 1 18  ? 9.738  -11.363 8.503   0.50 14.44 ?  18  ILE   A HG22 1 
ATOM   479  H  HG23 A ILE   A 1 18  ? 9.114  -10.360 7.605   0.50 14.49 ?  18  ILE   A HG23 1 
ATOM   480  H  HG23 B ILE   A 1 18  ? 9.030  -9.978  8.181   0.50 14.44 ?  18  ILE   A HG23 1 
ATOM   481  H  HD11 A ILE   A 1 18  ? 10.780 -8.651  4.300   0.50 15.89 ?  18  ILE   A HD11 1 
ATOM   482  H  HD11 B ILE   A 1 18  ? 10.683 -8.214  4.868   0.50 16.37 ?  18  ILE   A HD11 1 
ATOM   483  H  HD12 A ILE   A 1 18  ? 11.390 -10.100 4.523   0.50 15.89 ?  18  ILE   A HD12 1 
ATOM   484  H  HD12 B ILE   A 1 18  ? 11.360 -9.640  5.044   0.50 16.37 ?  18  ILE   A HD12 1 
ATOM   485  H  HD13 A ILE   A 1 18  ? 9.850  -9.835  4.806   0.50 15.89 ?  18  ILE   A HD13 1 
ATOM   486  H  HD13 B ILE   A 1 18  ? 9.803  -9.462  5.306   0.50 16.37 ?  18  ILE   A HD13 1 
ATOM   487  N  N    A LYS   A 1 19  ? 10.788 -7.737  9.205   0.50 13.03 ?  19  LYS   A N    1 
ATOM   488  N  N    B LYS   A 1 19  ? 10.907 -7.467  9.780   0.50 12.46 ?  19  LYS   A N    1 
ATOM   489  C  CA   A LYS   A 1 19  ? 9.983  -6.792  9.973   0.50 14.06 ?  19  LYS   A CA   1 
ATOM   490  C  CA   B LYS   A 1 19  ? 10.114 -6.490  10.512  0.50 13.99 ?  19  LYS   A CA   1 
ATOM   491  C  C    A LYS   A 1 19  ? 9.777  -5.511  9.170   0.50 14.42 ?  19  LYS   A C    1 
ATOM   492  C  C    B LYS   A 1 19  ? 9.885  -5.272  9.627   0.50 14.81 ?  19  LYS   A C    1 
ATOM   493  O  O    A LYS   A 1 19  ? 10.651 -5.095  8.402   0.50 14.11 ?  19  LYS   A O    1 
ATOM   494  O  O    B LYS   A 1 19  ? 10.773 -4.876  8.869   0.50 14.65 ?  19  LYS   A O    1 
ATOM   495  C  CB   A LYS   A 1 19  ? 10.691 -6.456  11.295  0.50 14.86 ?  19  LYS   A CB   1 
ATOM   496  C  CB   B LYS   A 1 19  ? 10.829 -6.076  11.805  0.50 14.70 ?  19  LYS   A CB   1 
ATOM   497  C  CG   A LYS   A 1 19  ? 9.963  -5.505  12.252  0.50 16.12 ?  19  LYS   A CG   1 
ATOM   498  C  CG   B LYS   A 1 19  ? 10.044 -5.155  12.710  0.50 16.13 ?  19  LYS   A CG   1 
ATOM   499  C  CD   A LYS   A 1 19  ? 10.845 -5.237  13.480  0.50 16.84 ?  19  LYS   A CD   1 
ATOM   500  C  CD   B LYS   A 1 19  ? 10.888 -4.744  13.900  0.50 17.25 ?  19  LYS   A CD   1 
ATOM   501  C  CE   A LYS   A 1 19  ? 10.206 -4.291  14.493  0.50 17.41 ?  19  LYS   A CE   1 
ATOM   502  C  CE   B LYS   A 1 19  ? 10.125 -3.820  14.824  0.50 18.25 ?  19  LYS   A CE   1 
ATOM   503  N  NZ   A LYS   A 1 19  ? 11.098 -4.063  15.676  0.50 17.45 ?  19  LYS   A NZ   1 
ATOM   504  N  NZ   B LYS   A 1 19  ? 10.936 -3.463  16.011  0.50 18.77 ?  19  LYS   A NZ   1 
ATOM   505  H  H    A LYS   A 1 19  ? 11.300 -7.371  8.627   0.50 15.66 ?  19  LYS   A H    1 
ATOM   506  H  H    B LYS   A 1 19  ? 11.503 -7.105  9.266   0.50 14.98 ?  19  LYS   A H    1 
ATOM   507  H  HA   A LYS   A 1 19  ? 9.115  -7.193  10.170  0.50 16.91 ?  19  LYS   A HA   1 
ATOM   508  H  HA   B LYS   A 1 19  ? 9.258  -6.875  10.750  0.50 16.82 ?  19  LYS   A HA   1 
ATOM   509  H  HB2  A LYS   A 1 19  ? 10.835 -7.286  11.775  0.50 17.87 ?  19  LYS   A HB2  1 
ATOM   510  H  HB2  B LYS   A 1 19  ? 11.027 -6.872  12.323  0.50 17.68 ?  19  LYS   A HB2  1 
ATOM   511  H  HB3  A LYS   A 1 19  ? 11.541 -6.053  11.081  0.50 17.87 ?  19  LYS   A HB3  1 
ATOM   512  H  HB3  B LYS   A 1 19  ? 11.656 -5.621  11.579  0.50 17.68 ?  19  LYS   A HB3  1 
ATOM   513  H  HG2  A LYS   A 1 19  ? 9.788  -4.660  11.809  0.50 19.37 ?  19  LYS   A HG2  1 
ATOM   514  H  HG2  B LYS   A 1 19  ? 9.792  -4.356  12.224  0.50 19.39 ?  19  LYS   A HG2  1 
ATOM   515  H  HG3  A LYS   A 1 19  ? 9.132  -5.909  12.553  0.50 19.37 ?  19  LYS   A HG3  1 
ATOM   516  H  HG3  B LYS   A 1 19  ? 9.256  -5.617  13.039  0.50 19.39 ?  19  LYS   A HG3  1 
ATOM   517  H  HD2  A LYS   A 1 19  ? 11.021 -6.077  13.933  0.50 20.25 ?  19  LYS   A HD2  1 
ATOM   518  H  HD2  B LYS   A 1 19  ? 11.142 -5.537  14.400  0.50 20.74 ?  19  LYS   A HD2  1 
ATOM   519  H  HD3  A LYS   A 1 19  ? 11.679 -4.839  13.190  0.50 20.25 ?  19  LYS   A HD3  1 
ATOM   520  H  HD3  B LYS   A 1 19  ? 11.679 -4.279  13.584  0.50 20.74 ?  19  LYS   A HD3  1 
ATOM   521  H  HE2  A LYS   A 1 19  ? 10.042 -3.432  14.073  0.50 20.92 ?  19  LYS   A HE2  1 
ATOM   522  H  HE2  B LYS   A 1 19  ? 9.902  -3.005  14.346  0.50 21.93 ?  19  LYS   A HE2  1 
ATOM   523  H  HE3  A LYS   A 1 19  ? 9.374  -4.673  14.813  0.50 20.92 ?  19  LYS   A HE3  1 
ATOM   524  H  HE3  B LYS   A 1 19  ? 9.318  -4.265  15.125  0.50 21.93 ?  19  LYS   A HE3  1 
ATOM   525  H  HZ1  A LYS   A 1 19  ? 10.708 -3.509  16.251  0.50 20.97 ?  19  LYS   A HZ1  1 
ATOM   526  H  HZ1  B LYS   A 1 19  ? 10.469 -2.923  16.544  0.50 22.56 ?  19  LYS   A HZ1  1 
ATOM   527  H  HZ2  A LYS   A 1 19  ? 11.261 -4.838  16.086  0.50 20.97 ?  19  LYS   A HZ2  1 
ATOM   528  H  HZ2  B LYS   A 1 19  ? 11.155 -4.197  16.461  0.50 22.56 ?  19  LYS   A HZ2  1 
ATOM   529  H  HZ3  A LYS   A 1 19  ? 11.871 -3.711  15.411  0.50 20.97 ?  19  LYS   A HZ3  1 
ATOM   530  H  HZ3  B LYS   A 1 19  ? 11.679 -3.045  15.756  0.50 22.56 ?  19  LYS   A HZ3  1 
ATOM   531  N  N    A ASN   A 1 20  ? 8.615  -4.883  9.356   0.50 15.72 ?  20  ASN   A N    1 
ATOM   532  N  N    B ASN   A 1 20  ? 8.691  -4.687  9.715   0.50 16.66 ?  20  ASN   A N    1 
ATOM   533  C  CA   A ASN   A 1 20  ? 8.377  -3.540  8.831   0.50 17.16 ?  20  ASN   A CA   1 
ATOM   534  C  CA   B ASN   A 1 20  ? 8.391  -3.443  9.005   0.50 18.32 ?  20  ASN   A CA   1 
ATOM   535  C  C    A ASN   A 1 20  ? 8.994  -2.545  9.807   0.50 17.32 ?  20  ASN   A C    1 
ATOM   536  C  C    B ASN   A 1 20  ? 8.946  -2.294  9.836   0.50 18.83 ?  20  ASN   A C    1 
ATOM   537  O  O    A ASN   A 1 20  ? 8.485  -2.354  10.916  0.50 17.35 ?  20  ASN   A O    1 
ATOM   538  O  O    B ASN   A 1 20  ? 8.314  -1.841  10.793  0.50 19.42 ?  20  ASN   A O    1 
ATOM   539  C  CB   A ASN   A 1 20  ? 6.879  -3.294  8.645   0.50 18.62 ?  20  ASN   A CB   1 
ATOM   540  C  CB   B ASN   A 1 20  ? 6.888  -3.306  8.780   0.50 19.74 ?  20  ASN   A CB   1 
ATOM   541  C  CG   A ASN   A 1 20  ? 6.554  -1.846  8.299   0.50 20.47 ?  20  ASN   A CG   1 
ATOM   542  C  CG   B ASN   A 1 20  ? 6.475  -1.918  8.303   0.50 21.38 ?  20  ASN   A CG   1 
ATOM   543  O  OD1  A ASN   A 1 20  ? 5.616  -1.263  8.847   0.50 22.63 ?  20  ASN   A OD1  1 
ATOM   544  O  OD1  B ASN   A 1 20  ? 5.468  -1.372  8.764   0.50 23.14 ?  20  ASN   A OD1  1 
ATOM   545  N  ND2  A ASN   A 1 20  ? 7.323  -1.262  7.386   0.50 20.65 ?  20  ASN   A ND2  1 
ATOM   546  N  ND2  B ASN   A 1 20  ? 7.241  -1.346  7.377   0.50 21.68 ?  20  ASN   A ND2  1 
ATOM   547  H  H    A ASN   A 1 20  ? 7.947  -5.215  9.789   0.50 18.90 ?  20  ASN   A H    1 
ATOM   548  H  H    B ASN   A 1 20  ? 8.037  -4.999  10.177  0.50 20.02 ?  20  ASN   A H    1 
ATOM   549  H  HA   A ASN   A 1 20  ? 8.813  -3.450  7.971   0.50 20.63 ?  20  ASN   A HA   1 
ATOM   550  H  HA   B ASN   A 1 20  ? 8.842  -3.446  8.147   0.50 22.02 ?  20  ASN   A HA   1 
ATOM   551  H  HB2  A ASN   A 1 20  ? 6.555  -3.852  7.920   0.50 22.38 ?  20  ASN   A HB2  1 
ATOM   552  H  HB2  B ASN   A 1 20  ? 6.617  -3.946  8.107   0.50 23.72 ?  20  ASN   A HB2  1 
ATOM   553  H  HB3  A ASN   A 1 20  ? 6.417  -3.523  9.466   0.50 22.38 ?  20  ASN   A HB3  1 
ATOM   554  H  HB3  B ASN   A 1 20  ? 6.431  -3.486  9.616   0.50 23.72 ?  20  ASN   A HB3  1 
ATOM   555  H  HD21 A ASN   A 1 20  ? 7.175  -0.449  7.160   0.50 24.82 ?  20  ASN   A HD21 1 
ATOM   556  H  HD21 B ASN   A 1 20  ? 7.048  -0.562  7.083   0.50 26.05 ?  20  ASN   A HD21 1 
ATOM   557  H  HD22 A ASN   A 1 20  ? 7.970  -1.701  7.025   0.50 24.82 ?  20  ASN   A HD22 1 
ATOM   558  H  HD22 B ASN   A 1 20  ? 7.933  -1.760  7.072   0.50 26.05 ?  20  ASN   A HD22 1 
ATOM   559  N  N    A ALA   A 1 21  ? 10.104 -1.925  9.416   0.50 17.57 ?  21  ALA   A N    1 
ATOM   560  N  N    B ALA   A 1 21  ? 10.142 -1.826  9.481   0.50 18.89 ?  21  ALA   A N    1 
ATOM   561  C  CA   A ALA   A 1 21  ? 10.799 -1.030  10.328  0.50 17.14 ?  21  ALA   A CA   1 
ATOM   562  C  CA   B ALA   A 1 21  ? 10.792 -0.769  10.241  0.50 18.36 ?  21  ALA   A CA   1 
ATOM   563  C  C    A ALA   A 1 21  ? 11.749 -0.137  9.549   0.50 16.75 ?  21  ALA   A C    1 
ATOM   564  C  C    B ALA   A 1 21  ? 11.905 -0.154  9.407   0.50 17.06 ?  21  ALA   A C    1 
ATOM   565  O  O    A ALA   A 1 21  ? 12.170 -0.467  8.437   0.50 16.88 ?  21  ALA   A O    1 
ATOM   566  O  O    B ALA   A 1 21  ? 12.431 -0.777  8.480   0.50 16.95 ?  21  ALA   A O    1 
ATOM   567  C  CB   A ALA   A 1 21  ? 11.568 -1.809  11.398  0.50 17.35 ?  21  ALA   A CB   1 
ATOM   568  C  CB   B ALA   A 1 21  ? 11.345 -1.292  11.573  0.50 19.30 ?  21  ALA   A CB   1 
ATOM   569  H  H    A ALA   A 1 21  ? 10.465 -2.005  8.641   0.50 21.12 ?  21  ALA   A H    1 
ATOM   570  H  H    B ALA   A 1 21  ? 10.596 -2.105  8.807   0.50 22.70 ?  21  ALA   A H    1 
ATOM   571  H  HA   A ALA   A 1 21  ? 10.147 -0.464  10.774  0.50 20.60 ?  21  ALA   A HA   1 
ATOM   572  H  HA   B ALA   A 1 21  ? 10.145 -0.075  10.438  0.50 22.06 ?  21  ALA   A HA   1 
ATOM   573  H  HB1  A ALA   A 1 21  ? 11.990 -1.178  11.999  0.50 20.86 ?  21  ALA   A HB1  1 
ATOM   574  H  HB1  B ALA   A 1 21  ? 11.768 -0.559  12.050  0.50 23.20 ?  21  ALA   A HB1  1 
ATOM   575  H  HB2  A ALA   A 1 21  ? 10.941 -2.365  11.890  0.50 20.86 ?  21  ALA   A HB2  1 
ATOM   576  H  HB2  B ALA   A 1 21  ? 10.613 -1.650  12.103  0.50 23.20 ?  21  ALA   A HB2  1 
ATOM   577  H  HB3  A ALA   A 1 21  ? 12.234 -2.362  10.967  0.50 20.86 ?  21  ALA   A HB3  1 
ATOM   578  H  HB3  B ALA   A 1 21  ? 11.995 -1.989  11.396  0.50 23.20 ?  21  ALA   A HB3  1 
ATOM   579  N  N    A ASP   A 1 22  ? 12.064 1.007   10.157  0.50 16.72 ?  22  ASP   A N    1 
ATOM   580  N  N    B ASP   A 1 22  ? 12.228 1.095   9.739   0.50 16.46 ?  22  ASP   A N    1 
ATOM   581  C  CA   A ASP   A 1 22  ? 13.089 1.922   9.666   0.50 16.92 ?  22  ASP   A CA   1 
ATOM   582  C  CA   B ASP   A 1 22  ? 13.415 1.760   9.215   0.50 15.82 ?  22  ASP   A CA   1 
ATOM   583  C  C    A ASP   A 1 22  ? 14.429 1.446   10.215  0.50 15.84 ?  22  ASP   A C    1 
ATOM   584  C  C    B ASP   A 1 22  ? 14.650 1.137   9.858   0.50 14.43 ?  22  ASP   A C    1 
ATOM   585  O  O    A ASP   A 1 22  ? 14.652 1.470   11.429  0.50 16.17 ?  22  ASP   A O    1 
ATOM   586  O  O    B ASP   A 1 22  ? 14.739 1.043   11.085  0.50 14.31 ?  22  ASP   A O    1 
ATOM   587  C  CB   A ASP   A 1 22  ? 12.784 3.337   10.153  0.50 18.65 ?  22  ASP   A CB   1 
ATOM   588  C  CB   B ASP   A 1 22  ? 13.333 3.249   9.573   0.50 16.92 ?  22  ASP   A CB   1 
ATOM   589  C  CG   A ASP   A 1 22  ? 13.770 4.374   9.631   0.50 19.99 ?  22  ASP   A CG   1 
ATOM   590  C  CG   B ASP   A 1 22  ? 14.418 4.099   8.921   0.50 17.38 ?  22  ASP   A CG   1 
ATOM   591  O  OD1  A ASP   A 1 22  ? 14.870 4.004   9.174   0.50 20.14 ?  22  ASP   A OD1  1 
ATOM   592  O  OD1  B ASP   A 1 22  ? 15.391 3.545   8.368   0.50 16.61 ?  22  ASP   A OD1  1 
ATOM   593  O  OD2  A ASP   A 1 22  ? 13.443 5.578   9.689   0.50 21.19 -1 22  ASP   A OD2  1 
ATOM   594  O  OD2  B ASP   A 1 22  ? 14.287 5.342   8.973   0.50 18.38 -1 22  ASP   A OD2  1 
ATOM   595  H  H    A ASP   A 1 22  ? 11.676 1.287   10.875  0.50 20.10 ?  22  ASP   A H    1 
ATOM   596  H  H    B ASP   A 1 22  ? 11.758 1.587   10.266  0.50 19.79 ?  22  ASP   A H    1 
ATOM   597  H  HA   A ASP   A 1 22  ? 13.115 1.910   8.696   0.50 20.33 ?  22  ASP   A HA   1 
ATOM   598  H  HA   B ASP   A 1 22  ? 13.461 1.656   8.249   0.50 19.02 ?  22  ASP   A HA   1 
ATOM   599  H  HB2  A ASP   A 1 22  ? 11.900 3.592   9.851   0.50 22.41 ?  22  ASP   A HB2  1 
ATOM   600  H  HB2  B ASP   A 1 22  ? 12.478 3.594   9.285   0.50 20.34 ?  22  ASP   A HB2  1 
ATOM   601  H  HB3  A ASP   A 1 22  ? 12.815 3.347   11.125  0.50 22.41 ?  22  ASP   A HB3  1 
ATOM   602  H  HB3  B ASP   A 1 22  ? 13.426 3.341   10.533  0.50 20.34 ?  22  ASP   A HB3  1 
ATOM   603  N  N    A ILE   A 1 23  ? 15.322 1.018   9.320   0.50 15.06 ?  23  ILE   A N    1 
ATOM   604  N  N    B ILE   A 1 23  ? 15.602 0.695   9.030   0.50 13.53 ?  23  ILE   A N    1 
ATOM   605  C  CA   A ILE   A 1 23  ? 16.592 0.433   9.746   0.50 14.51 ?  23  ILE   A CA   1 
ATOM   606  C  CA   B ILE   A 1 23  ? 16.819 0.073   9.549   0.50 12.86 ?  23  ILE   A CA   1 
ATOM   607  C  C    A ILE   A 1 23  ? 17.389 1.404   10.606  0.50 14.32 ?  23  ILE   A C    1 
ATOM   608  C  C    B ILE   A 1 23  ? 17.556 1.026   10.481  0.50 13.16 ?  23  ILE   A C    1 
ATOM   609  O  O    A ILE   A 1 23  ? 18.129 0.986   11.505  0.50 14.62 ?  23  ILE   A O    1 
ATOM   610  O  O    B ILE   A 1 23  ? 18.210 0.593   11.436  0.50 13.35 ?  23  ILE   A O    1 
ATOM   611  C  CB   A ILE   A 1 23  ? 17.384 -0.072  8.522   0.50 14.04 ?  23  ILE   A CB   1 
ATOM   612  C  CB   B ILE   A 1 23  ? 17.718 -0.436  8.398   0.50 12.04 ?  23  ILE   A CB   1 
ATOM   613  C  CG1  A ILE   A 1 23  ? 18.571 -0.930  8.968   0.50 14.14 ?  23  ILE   A CG1  1 
ATOM   614  C  CG1  B ILE   A 1 23  ? 18.806 -1.371  8.942   0.50 12.14 ?  23  ILE   A CG1  1 
ATOM   615  C  CG2  A ILE   A 1 23  ? 17.820 1.100   7.639   0.50 14.01 ?  23  ILE   A CG2  1 
ATOM   616  C  CG2  B ILE   A 1 23  ? 18.342 0.731   7.620   0.50 11.87 ?  23  ILE   A CG2  1 
ATOM   617  C  CD1  A ILE   A 1 23  ? 19.240 -1.673  7.832   0.50 14.07 ?  23  ILE   A CD1  1 
ATOM   618  C  CD1  B ILE   A 1 23  ? 19.676 -2.011  7.866   0.50 11.98 ?  23  ILE   A CD1  1 
ATOM   619  H  H    A ILE   A 1 23  ? 15.214 1.058   8.471   0.50 18.11 ?  23  ILE   A H    1 
ATOM   620  H  H    B ILE   A 1 23  ? 15.577 0.748   8.183   0.50 16.26 ?  23  ILE   A H    1 
ATOM   621  H  HA   A ILE   A 1 23  ? 16.398 -0.338  10.296  0.50 17.45 ?  23  ILE   A HA   1 
ATOM   622  H  HA   B ILE   A 1 23  ? 16.563 -0.703  10.070  0.50 15.47 ?  23  ILE   A HA   1 
ATOM   623  H  HB   A ILE   A 1 23  ? 16.793 -0.631  7.998   0.50 16.88 ?  23  ILE   A HB   1 
ATOM   624  H  HB   B ILE   A 1 23  ? 17.169 -0.948  7.784   0.50 14.49 ?  23  ILE   A HB   1 
ATOM   625  H  HG12 A ILE   A 1 23  ? 19.237 -0.359  9.380   0.50 17.00 ?  23  ILE   A HG12 1 
ATOM   626  H  HG12 B ILE   A 1 23  ? 19.391 -0.867  9.527   0.50 14.60 ?  23  ILE   A HG12 1 
ATOM   627  H  HG13 A ILE   A 1 23  ? 18.258 -1.588  9.608   0.50 17.00 ?  23  ILE   A HG13 1 
ATOM   628  H  HG13 B ILE   A 1 23  ? 18.383 -2.089  9.439   0.50 14.60 ?  23  ILE   A HG13 1 
ATOM   629  H  HG21 A ILE   A 1 23  ? 18.190 0.753   6.812   0.50 16.85 ?  23  ILE   A HG21 1 
ATOM   630  H  HG21 B ILE   A 1 23  ? 18.740 0.388   6.800   0.50 14.28 ?  23  ILE   A HG21 1 
ATOM   631  H  HG22 A ILE   A 1 23  ? 17.044 1.654   7.443   0.50 16.85 ?  23  ILE   A HG22 1 
ATOM   632  H  HG22 B ILE   A 1 23  ? 17.650 1.371   7.407   0.50 14.28 ?  23  ILE   A HG22 1 
ATOM   633  H  HG23 A ILE   A 1 23  ? 18.487 1.624   8.107   0.50 16.85 ?  23  ILE   A HG23 1 
ATOM   634  H  HG23 B ILE   A 1 23  ? 19.027 1.147   8.166   0.50 14.28 ?  23  ILE   A HG23 1 
ATOM   635  H  HD11 A ILE   A 1 23  ? 19.942 -2.235  8.194   0.50 16.91 ?  23  ILE   A HD11 1 
ATOM   636  H  HD11 B ILE   A 1 23  ? 20.274 -2.654  8.285   0.50 14.41 ?  23  ILE   A HD11 1 
ATOM   637  H  HD12 A ILE   A 1 23  ? 18.576 -2.220  7.382   0.50 16.91 ?  23  ILE   A HD12 1 
ATOM   638  H  HD12 B ILE   A 1 23  ? 19.106 -2.462  7.225   0.50 14.41 ?  23  ILE   A HD12 1 
ATOM   639  H  HD13 A ILE   A 1 23  ? 19.614 -1.030  7.212   0.50 16.91 ?  23  ILE   A HD13 1 
ATOM   640  H  HD13 B ILE   A 1 23  ? 20.194 -1.322  7.424   0.50 14.41 ?  23  ILE   A HD13 1 
ATOM   641  N  N    A VAL   A 1 24  ? 17.246 2.708   10.363  0.50 14.71 ?  24  VAL   A N    1 
ATOM   642  N  N    B VAL   A 1 24  ? 17.449 2.331   10.231  0.50 14.15 ?  24  VAL   A N    1 
ATOM   643  C  CA   A VAL   A 1 24  ? 17.928 3.696   11.196  0.50 15.60 ?  24  VAL   A CA   1 
ATOM   644  C  CA   B VAL   A 1 24  ? 18.091 3.319   11.094  0.50 15.65 ?  24  VAL   A CA   1 
ATOM   645  C  C    A VAL   A 1 24  ? 17.433 3.608   12.632  0.50 16.24 ?  24  VAL   A C    1 
ATOM   646  C  C    B VAL   A 1 24  ? 17.511 3.254   12.501  0.50 16.56 ?  24  VAL   A C    1 
ATOM   647  O  O    A VAL   A 1 24  ? 18.224 3.533   13.581  0.50 16.52 ?  24  VAL   A O    1 
ATOM   648  O  O    B VAL   A 1 24  ? 18.245 3.314   13.495  0.50 17.08 ?  24  VAL   A O    1 
ATOM   649  C  CB   A VAL   A 1 24  ? 17.737 5.110   10.620  0.50 16.21 ?  24  VAL   A CB   1 
ATOM   650  C  CB   B VAL   A 1 24  ? 17.950 4.722   10.477  0.50 16.64 ?  24  VAL   A CB   1 
ATOM   651  C  CG1  A VAL   A 1 24  ? 18.219 6.163   11.615  0.50 16.67 ?  24  VAL   A CG1  1 
ATOM   652  C  CG1  B VAL   A 1 24  ? 18.553 5.768   11.392  0.50 17.94 ?  24  VAL   A CG1  1 
ATOM   653  C  CG2  A VAL   A 1 24  ? 18.470 5.245   9.297   0.50 16.70 ?  24  VAL   A CG2  1 
ATOM   654  C  CG2  B VAL   A 1 24  ? 18.598 4.757   9.099   0.50 16.79 ?  24  VAL   A CG2  1 
ATOM   655  H  H    A VAL   A 1 24  ? 16.766 3.042   9.734   0.50 17.69 ?  24  VAL   A H    1 
ATOM   656  H  H    B VAL   A 1 24  ? 17.016 2.663   9.574   0.50 17.02 ?  24  VAL   A H    1 
ATOM   657  H  HA   A VAL   A 1 24  ? 18.876 3.506   11.199  0.50 18.76 ?  24  VAL   A HA   1 
ATOM   658  H  HA   B VAL   A 1 24  ? 19.036 3.114   11.157  0.50 18.81 ?  24  VAL   A HA   1 
ATOM   659  H  HB   A VAL   A 1 24  ? 16.793 5.264   10.456  0.50 19.49 ?  24  VAL   A HB   1 
ATOM   660  H  HB   B VAL   A 1 24  ? 17.008 4.924   10.367  0.50 20.00 ?  24  VAL   A HB   1 
ATOM   661  H  HG11 A VAL   A 1 24  ? 18.361 6.997   11.143  0.50 20.04 ?  24  VAL   A HG11 1 
ATOM   662  H  HG11 B VAL   A 1 24  ? 18.685 6.585   10.889  0.50 21.56 ?  24  VAL   A HG11 1 
ATOM   663  H  HG12 A VAL   A 1 24  ? 17.546 6.281   12.302  0.50 20.04 ?  24  VAL   A HG12 1 
ATOM   664  H  HG12 B VAL   A 1 24  ? 17.941 5.929   12.127  0.50 21.56 ?  24  VAL   A HG12 1 
ATOM   665  H  HG13 A VAL   A 1 24  ? 19.052 5.861   12.010  0.50 20.04 ?  24  VAL   A HG13 1 
ATOM   666  H  HG13 B VAL   A 1 24  ? 19.401 5.443   11.728  0.50 21.56 ?  24  VAL   A HG13 1 
ATOM   667  H  HG21 A VAL   A 1 24  ? 18.194 6.070   8.868   0.50 20.08 ?  24  VAL   A HG21 1 
ATOM   668  H  HG21 B VAL   A 1 24  ? 18.548 5.660   8.750   0.50 20.18 ?  24  VAL   A HG21 1 
ATOM   669  H  HG22 A VAL   A 1 24  ? 19.424 5.265   9.467   0.50 20.08 ?  24  VAL   A HG22 1 
ATOM   670  H  HG22 B VAL   A 1 24  ? 19.526 4.486   9.181   0.50 20.18 ?  24  VAL   A HG22 1 
ATOM   671  H  HG23 A VAL   A 1 24  ? 18.247 4.488   8.732   0.50 20.08 ?  24  VAL   A HG23 1 
ATOM   672  H  HG23 B VAL   A 1 24  ? 18.127 4.147   8.509   0.50 20.18 ?  24  VAL   A HG23 1 
ATOM   673  N  N    A GLU   A 1 25  ? 16.111 3.622   12.812  0.50 17.01 ?  25  GLU   A N    1 
ATOM   674  N  N    B GLU   A 1 25  ? 16.186 3.119   12.607  0.50 17.25 ?  25  GLU   A N    1 
ATOM   675  C  CA   A GLU   A 1 25  ? 15.551 3.564   14.156  0.50 18.22 ?  25  GLU   A CA   1 
ATOM   676  C  CA   B GLU   A 1 25  ? 15.548 3.042   13.918  0.50 18.71 ?  25  GLU   A CA   1 
ATOM   677  C  C    A GLU   A 1 25  ? 15.783 2.204   14.796  0.50 17.56 ?  25  GLU   A C    1 
ATOM   678  C  C    B GLU   A 1 25  ? 15.835 1.708   14.600  0.50 18.43 ?  25  GLU   A C    1 
ATOM   679  O  O    A GLU   A 1 25  ? 16.007 2.123   16.008  0.50 18.03 ?  25  GLU   A O    1 
ATOM   680  O  O    B GLU   A 1 25  ? 16.068 1.667   15.814  0.50 18.89 ?  25  GLU   A O    1 
ATOM   681  C  CB   A GLU   A 1 25  ? 14.060 3.905   14.118  0.50 20.34 ?  25  GLU   A CB   1 
ATOM   682  C  CB   B GLU   A 1 25  ? 14.043 3.294   13.788  0.50 20.05 ?  25  GLU   A CB   1 
ATOM   683  C  CG   A GLU   A 1 25  ? 13.783 5.357   13.757  0.50 22.46 ?  25  GLU   A CG   1 
ATOM   684  C  CG   B GLU   A 1 25  ? 13.700 4.695   13.300  0.50 22.19 ?  25  GLU   A CG   1 
ATOM   685  C  CD   A GLU   A 1 25  ? 14.572 6.337   14.607  0.50 24.21 ?  25  GLU   A CD   1 
ATOM   686  C  CD   B GLU   A 1 25  ? 14.155 5.772   14.266  0.50 24.10 ?  25  GLU   A CD   1 
ATOM   687  O  OE1  A GLU   A 1 25  ? 14.621 6.155   15.841  0.50 24.72 ?  25  GLU   A OE1  1 
ATOM   688  O  OE1  B GLU   A 1 25  ? 14.084 5.538   15.493  0.50 24.93 ?  25  GLU   A OE1  1 
ATOM   689  O  OE2  A GLU   A 1 25  ? 15.162 7.278   14.034  0.50 25.21 -1 25  GLU   A OE2  1 
ATOM   690  O  OE2  B GLU   A 1 25  ? 14.585 6.848   13.800  0.50 25.07 -1 25  GLU   A OE2  1 
ATOM   691  H  H    A GLU   A 1 25  ? 15.527 3.663   12.182  0.50 20.44 ?  25  GLU   A H    1 
ATOM   692  H  H    B GLU   A 1 25  ? 15.644 3.065   11.942  0.50 20.73 ?  25  GLU   A H    1 
ATOM   693  H  HA   A GLU   A 1 25  ? 15.996 4.221   14.712  0.50 21.89 ?  25  GLU   A HA   1 
ATOM   694  H  HA   B GLU   A 1 25  ? 15.915 3.736   14.482  0.50 22.48 ?  25  GLU   A HA   1 
ATOM   695  H  HB2  A GLU   A 1 25  ? 13.623 3.349   13.450  0.50 24.45 ?  25  GLU   A HB2  1 
ATOM   696  H  HB2  B GLU   A 1 25  ? 13.670 2.663   13.155  0.50 24.09 ?  25  GLU   A HB2  1 
ATOM   697  H  HB3  A GLU   A 1 25  ? 13.669 3.738   14.990  0.50 24.45 ?  25  GLU   A HB3  1 
ATOM   698  H  HB3  B GLU   A 1 25  ? 13.628 3.176   14.657  0.50 24.09 ?  25  GLU   A HB3  1 
ATOM   699  H  HG2  A GLU   A 1 25  ? 14.033 5.504   12.834  0.50 26.98 ?  25  GLU   A HG2  1 
ATOM   700  H  HG2  B GLU   A 1 25  ? 14.134 4.851   12.445  0.50 26.66 ?  25  GLU   A HG2  1 
ATOM   701  H  HG3  A GLU   A 1 25  ? 12.838 5.538   13.884  0.50 26.98 ?  25  GLU   A HG3  1 
ATOM   702  H  HG3  B GLU   A 1 25  ? 12.738 4.773   13.200  0.50 26.66 ?  25  GLU   A HG3  1 
ATOM   703  N  N    A GLU   A 1 26  ? 15.748 1.134   14.000  0.50 17.36 ?  26  GLU   A N    1 
ATOM   704  N  N    B GLU   A 1 26  ? 15.832 0.607   13.844  0.50 18.42 ?  26  GLU   A N    1 
ATOM   705  C  CA   A GLU   A 1 26  ? 16.056 -0.193  14.526  0.50 17.15 ?  26  GLU   A CA   1 
ATOM   706  C  CA   B GLU   A 1 26  ? 16.219 -0.675  14.425  0.50 18.47 ?  26  GLU   A CA   1 
ATOM   707  C  C    A GLU   A 1 26  ? 17.481 -0.249  15.064  0.50 16.35 ?  26  GLU   A C    1 
ATOM   708  C  C    B GLU   A 1 26  ? 17.647 -0.623  14.949  0.50 17.72 ?  26  GLU   A C    1 
ATOM   709  O  O    A GLU   A 1 26  ? 17.718 -0.720  16.183  0.50 16.46 ?  26  GLU   A O    1 
ATOM   710  O  O    B GLU   A 1 26  ? 17.947 -1.169  16.017  0.50 17.69 ?  26  GLU   A O    1 
ATOM   711  C  CB   A GLU   A 1 26  ? 15.865 -1.249  13.435  0.50 18.17 ?  26  GLU   A CB   1 
ATOM   712  C  CB   B GLU   A 1 26  ? 16.066 -1.797  13.395  0.50 19.59 ?  26  GLU   A CB   1 
ATOM   713  C  CG   A GLU   A 1 26  ? 14.460 -1.797  13.301  0.50 20.09 ?  26  GLU   A CG   1 
ATOM   714  C  CG   B GLU   A 1 26  ? 14.632 -2.182  13.113  0.50 20.37 ?  26  GLU   A CG   1 
ATOM   715  C  CD   A GLU   A 1 26  ? 14.061 -2.676  14.474  0.50 21.44 ?  26  GLU   A CD   1 
ATOM   716  C  CD   B GLU   A 1 26  ? 13.931 -2.696  14.346  0.50 20.92 ?  26  GLU   A CD   1 
ATOM   717  O  OE1  A GLU   A 1 26  ? 14.445 -3.869  14.516  0.50 21.96 ?  26  GLU   A OE1  1 
ATOM   718  O  OE1  B GLU   A 1 26  ? 14.476 -3.608  15.009  0.50 21.21 ?  26  GLU   A OE1  1 
ATOM   719  O  OE2  A GLU   A 1 26  ? 13.367 -2.161  15.364  0.50 21.95 -1 26  GLU   A OE2  1 
ATOM   720  O  OE2  B GLU   A 1 26  ? 12.846 -2.170  14.657  0.50 20.47 -1 26  GLU   A OE2  1 
ATOM   721  H  H    A GLU   A 1 26  ? 15.553 1.158   13.162  0.50 20.86 ?  26  GLU   A H    1 
ATOM   722  H  H    B GLU   A 1 26  ? 15.620 0.575   13.013  0.50 22.14 ?  26  GLU   A H    1 
ATOM   723  H  HA   A GLU   A 1 26  ? 15.449 -0.389  15.253  0.50 20.62 ?  26  GLU   A HA   1 
ATOM   724  H  HA   B GLU   A 1 26  ? 15.640 -0.875  15.175  0.50 22.20 ?  26  GLU   A HA   1 
ATOM   725  H  HB2  A GLU   A 1 26  ? 16.109 -0.855  12.581  0.50 21.84 ?  26  GLU   A HB2  1 
ATOM   726  H  HB2  B GLU   A 1 26  ? 16.460 -1.514  12.556  0.50 23.54 ?  26  GLU   A HB2  1 
ATOM   727  H  HB3  A GLU   A 1 26  ? 16.453 -1.993  13.628  0.50 21.84 ?  26  GLU   A HB3  1 
ATOM   728  H  HB3  B GLU   A 1 26  ? 16.523 -2.592  13.719  0.50 23.54 ?  26  GLU   A HB3  1 
ATOM   729  H  HG2  A GLU   A 1 26  ? 13.840 -1.050  13.236  0.50 24.15 ?  26  GLU   A HG2  1 
ATOM   730  H  HG2  B GLU   A 1 26  ? 14.149 -1.404  12.790  0.50 24.47 ?  26  GLU   A HG2  1 
ATOM   731  H  HG3  A GLU   A 1 26  ? 14.408 -2.338  12.500  0.50 24.15 ?  26  GLU   A HG3  1 
ATOM   732  H  HG3  B GLU   A 1 26  ? 14.607 -2.889  12.452  0.50 24.47 ?  26  GLU   A HG3  1 
ATOM   733  N  N    A ALA   A 1 27  ? 18.450 0.228   14.275  0.50 15.58 ?  27  ALA   A N    1 
ATOM   734  N  N    B ALA   A 1 27  ? 18.542 0.038   14.215  0.50 17.08 ?  27  ALA   A N    1 
ATOM   735  C  CA   A ALA   A 1 27  ? 19.847 0.138   14.690  0.50 15.85 ?  27  ALA   A CA   1 
ATOM   736  C  CA   B ALA   A 1 27  ? 19.917 0.171   14.685  0.50 17.09 ?  27  ALA   A CA   1 
ATOM   737  C  C    A ALA   A 1 27  ? 20.092 0.914   15.979  0.50 17.11 ?  27  ALA   A C    1 
ATOM   738  C  C    B ALA   A 1 27  ? 19.986 1.037   15.939  0.50 18.17 ?  27  ALA   A C    1 
ATOM   739  O  O    A ALA   A 1 27  ? 20.772 0.424   16.888  0.50 17.28 ?  27  ALA   A O    1 
ATOM   740  O  O    B ALA   A 1 27  ? 20.659 0.683   16.914  0.50 18.17 ?  27  ALA   A O    1 
ATOM   741  C  CB   A ALA   A 1 27  ? 20.768 0.637   13.573  0.50 15.50 ?  27  ALA   A CB   1 
ATOM   742  C  CB   B ALA   A 1 27  ? 20.802 0.741   13.575  0.50 16.51 ?  27  ALA   A CB   1 
ATOM   743  H  H    A ALA   A 1 27  ? 18.326 0.609   13.513  0.50 18.73 ?  27  ALA   A H    1 
ATOM   744  H  H    B ALA   A 1 27  ? 18.380 0.404   13.453  0.50 20.53 ?  27  ALA   A H    1 
ATOM   745  H  HA   A ALA   A 1 27  ? 20.062 -0.790  14.857  0.50 19.06 ?  27  ALA   A HA   1 
ATOM   746  H  HA   B ALA   A 1 27  ? 20.255 -0.708  14.912  0.50 20.54 ?  27  ALA   A HA   1 
ATOM   747  H  HB1  A ALA   A 1 27  ? 21.691 0.565   13.868  0.50 18.64 ?  27  ALA   A HB1  1 
ATOM   748  H  HB1  B ALA   A 1 27  ? 21.710 0.816   13.907  0.50 19.85 ?  27  ALA   A HB1  1 
ATOM   749  H  HB2  A ALA   A 1 27  ? 20.632 0.088   12.784  0.50 18.64 ?  27  ALA   A HB2  1 
ATOM   750  H  HB2  B ALA   A 1 27  ? 20.777 0.141   12.812  0.50 19.85 ?  27  ALA   A HB2  1 
ATOM   751  H  HB3  A ALA   A 1 27  ? 20.556 1.561   13.374  0.50 18.64 ?  27  ALA   A HB3  1 
ATOM   752  H  HB3  B ALA   A 1 27  ? 20.468 1.614   13.320  0.50 19.85 ?  27  ALA   A HB3  1 
ATOM   753  N  N    A LYS   A 1 28  ? 19.536 2.122   16.082  0.50 18.91 ?  28  LYS   A N    1 
ATOM   754  N  N    B LYS   A 1 28  ? 19.280 2.172   15.941  0.50 19.50 ?  28  LYS   A N    1 
ATOM   755  C  CA   A LYS   A 1 28  ? 19.712 2.910   17.298  0.50 21.83 ?  28  LYS   A CA   1 
ATOM   756  C  CA   B LYS   A 1 28  ? 19.318 3.060   17.100  0.50 21.92 ?  28  LYS   A CA   1 
ATOM   757  C  C    A LYS   A 1 28  ? 19.154 2.179   18.511  0.50 22.83 ?  28  LYS   A C    1 
ATOM   758  C  C    B LYS   A 1 28  ? 18.790 2.384   18.359  0.50 23.26 ?  28  LYS   A C    1 
ATOM   759  O  O    A LYS   A 1 28  ? 19.753 2.208   19.592  0.50 23.30 ?  28  LYS   A O    1 
ATOM   760  O  O    B LYS   A 1 28  ? 19.193 2.750   19.470  0.50 24.04 ?  28  LYS   A O    1 
ATOM   761  C  CB   A LYS   A 1 28  ? 19.062 4.287   17.138  0.50 23.89 ?  28  LYS   A CB   1 
ATOM   762  C  CB   B LYS   A 1 28  ? 18.545 4.349   16.814  0.50 23.42 ?  28  LYS   A CB   1 
ATOM   763  C  CG   A LYS   A 1 28  ? 19.864 5.239   16.261  0.50 25.83 ?  28  LYS   A CG   1 
ATOM   764  C  CG   B LYS   A 1 28  ? 19.321 5.336   15.961  0.50 25.22 ?  28  LYS   A CG   1 
ATOM   765  C  CD   A LYS   A 1 28  ? 19.346 6.670   16.327  0.50 27.77 ?  28  LYS   A CD   1 
ATOM   766  C  CD   B LYS   A 1 28  ? 18.746 6.741   16.039  0.50 27.55 ?  28  LYS   A CD   1 
ATOM   767  C  CE   A LYS   A 1 28  ? 18.067 6.842   15.529  0.50 29.01 ?  28  LYS   A CE   1 
ATOM   768  C  CE   B LYS   A 1 28  ? 17.579 6.928   15.088  0.50 29.29 ?  28  LYS   A CE   1 
ATOM   769  N  NZ   A LYS   A 1 28  ? 17.653 8.272   15.459  0.50 29.81 ?  28  LYS   A NZ   1 
ATOM   770  N  NZ   B LYS   A 1 28  ? 17.237 8.369   14.923  0.50 30.15 ?  28  LYS   A NZ   1 
ATOM   771  H  H    A LYS   A 1 28  ? 19.062 2.496   15.477  0.50 22.72 ?  28  LYS   A H    1 
ATOM   772  H  H    B LYS   A 1 28  ? 18.784 2.447   15.293  0.50 23.43 ?  28  LYS   A H    1 
ATOM   773  H  HA   A LYS   A 1 28  ? 20.658 3.048   17.455  0.50 26.23 ?  28  LYS   A HA   1 
ATOM   774  H  HA   B LYS   A 1 28  ? 20.237 3.306   17.270  0.50 26.33 ?  28  LYS   A HA   1 
ATOM   775  H  HB2  A LYS   A 1 28  ? 18.189 4.177   16.732  0.50 28.70 ?  28  LYS   A HB2  1 
ATOM   776  H  HB2  B LYS   A 1 28  ? 17.726 4.131   16.342  0.50 28.14 ?  28  LYS   A HB2  1 
ATOM   777  H  HB3  A LYS   A 1 28  ? 18.970 4.697   18.012  0.50 28.70 ?  28  LYS   A HB3  1 
ATOM   778  H  HB3  B LYS   A 1 28  ? 18.335 4.784   17.656  0.50 28.14 ?  28  LYS   A HB3  1 
ATOM   779  H  HG2  A LYS   A 1 28  ? 20.787 5.241   16.558  0.50 31.03 ?  28  LYS   A HG2  1 
ATOM   780  H  HG2  B LYS   A 1 28  ? 20.239 5.370   16.270  0.50 30.30 ?  28  LYS   A HG2  1 
ATOM   781  H  HG3  A LYS   A 1 28  ? 19.810 4.943   15.340  0.50 31.03 ?  28  LYS   A HG3  1 
ATOM   782  H  HG3  B LYS   A 1 28  ? 19.290 5.049   15.035  0.50 30.30 ?  28  LYS   A HG3  1 
ATOM   783  H  HD2  A LYS   A 1 28  ? 19.159 6.902   17.251  0.50 33.36 ?  28  LYS   A HD2  1 
ATOM   784  H  HD2  B LYS   A 1 28  ? 18.431 6.911   16.942  0.50 33.09 ?  28  LYS   A HD2  1 
ATOM   785  H  HD3  A LYS   A 1 28  ? 20.014 7.270   15.960  0.50 33.36 ?  28  LYS   A HD3  1 
ATOM   786  H  HD3  B LYS   A 1 28  ? 19.435 7.381   15.802  0.50 33.09 ?  28  LYS   A HD3  1 
ATOM   787  H  HE2  A LYS   A 1 28  ? 18.208 6.524   14.623  0.50 34.85 ?  28  LYS   A HE2  1 
ATOM   788  H  HE2  B LYS   A 1 28  ? 17.817 6.571   14.218  0.50 35.18 ?  28  LYS   A HE2  1 
ATOM   789  H  HE3  A LYS   A 1 28  ? 17.353 6.341   15.953  0.50 34.85 ?  28  LYS   A HE3  1 
ATOM   790  H  HE3  B LYS   A 1 28  ? 16.802 6.467   15.439  0.50 35.18 ?  28  LYS   A HE3  1 
ATOM   791  H  HZ1  A LYS   A 1 28  ? 16.903 8.351   14.987  0.50 35.80 ?  28  LYS   A HZ1  1 
ATOM   792  H  HZ1  B LYS   A 1 28  ? 16.553 8.457   14.361  0.50 36.21 ?  28  LYS   A HZ1  1 
ATOM   793  H  HZ2  A LYS   A 1 28  ? 17.514 8.589   16.279  0.50 35.80 ?  28  LYS   A HZ2  1 
ATOM   794  H  HZ2  B LYS   A 1 28  ? 17.014 8.720   15.710  0.50 36.21 ?  28  LYS   A HZ2  1 
ATOM   795  H  HZ3  A LYS   A 1 28  ? 18.292 8.755   15.069  0.50 35.80 ?  28  LYS   A HZ3  1 
ATOM   796  H  HZ3  B LYS   A 1 28  ? 17.938 8.812   14.597  0.50 36.21 ?  28  LYS   A HZ3  1 
ATOM   797  N  N    A LYS   A 1 29  ? 18.017 1.499   18.347  0.50 23.67 ?  29  LYS   A N    1 
ATOM   798  N  N    B LYS   A 1 29  ? 17.902 1.401   18.215  0.50 24.21 ?  29  LYS   A N    1 
ATOM   799  C  CA   A LYS   A 1 29  ? 17.420 0.775   19.465  0.50 25.39 ?  29  LYS   A CA   1 
ATOM   800  C  CA   B LYS   A 1 29  ? 17.301 0.733   19.365  0.50 25.86 ?  29  LYS   A CA   1 
ATOM   801  C  C    A LYS   A 1 29  ? 18.257 -0.441  19.840  0.50 24.82 ?  29  LYS   A C    1 
ATOM   802  C  C    B LYS   A 1 29  ? 18.090 -0.494  19.811  0.50 24.94 ?  29  LYS   A C    1 
ATOM   803  O  O    A LYS   A 1 29  ? 18.624 -0.620  21.008  0.50 25.64 ?  29  LYS   A O    1 
ATOM   804  O  O    B LYS   A 1 29  ? 18.251 -0.725  21.016  0.50 25.27 ?  29  LYS   A O    1 
ATOM   805  C  CB   A LYS   A 1 29  ? 15.995 0.352   19.104  0.50 27.80 ?  29  LYS   A CB   1 
ATOM   806  C  CB   B LYS   A 1 29  ? 15.865 0.318   19.029  0.50 28.42 ?  29  LYS   A CB   1 
ATOM   807  C  CG   A LYS   A 1 29  ? 15.251 -0.367  20.221  0.50 30.33 ?  29  LYS   A CG   1 
ATOM   808  C  CG   B LYS   A 1 29  ? 15.117 -0.328  20.184  0.50 31.02 ?  29  LYS   A CG   1 
ATOM   809  C  CD   A LYS   A 1 29  ? 14.869 0.588   21.339  0.50 32.65 ?  29  LYS   A CD   1 
ATOM   810  C  CD   B LYS   A 1 29  ? 14.617 0.710   21.172  0.50 33.31 ?  29  LYS   A CD   1 
ATOM   811  C  CE   A LYS   A 1 29  ? 13.982 -0.091  22.372  0.50 34.26 ?  29  LYS   A CE   1 
ATOM   812  C  CE   B LYS   A 1 29  ? 14.801 0.236   22.604  0.50 34.96 ?  29  LYS   A CE   1 
ATOM   813  N  NZ   A LYS   A 1 29  ? 13.484 0.872   23.393  0.50 35.24 ?  29  LYS   A NZ   1 
ATOM   814  N  NZ   B LYS   A 1 29  ? 13.903 0.953   23.549  0.50 35.89 ?  29  LYS   A NZ   1 
ATOM   815  H  H    A LYS   A 1 29  ? 17.583 1.438   17.608  0.50 28.44 ?  29  LYS   A H    1 
ATOM   816  H  H    B LYS   A 1 29  ? 17.627 1.104   17.456  0.50 29.09 ?  29  LYS   A H    1 
ATOM   817  H  HA   A LYS   A 1 29  ? 17.373 1.360   20.237  0.50 30.50 ?  29  LYS   A HA   1 
ATOM   818  H  HA   B LYS   A 1 29  ? 17.264 1.355   20.107  0.50 31.07 ?  29  LYS   A HA   1 
ATOM   819  H  HB2  A LYS   A 1 29  ? 15.483 1.143   18.874  0.50 33.39 ?  29  LYS   A HB2  1 
ATOM   820  H  HB2  B LYS   A 1 29  ? 15.366 1.106   18.760  0.50 34.14 ?  29  LYS   A HB2  1 
ATOM   821  H  HB3  A LYS   A 1 29  ? 16.032 -0.248  18.343  0.50 33.39 ?  29  LYS   A HB3  1 
ATOM   822  H  HB3  B LYS   A 1 29  ? 15.887 -0.320  18.299  0.50 34.14 ?  29  LYS   A HB3  1 
ATOM   823  H  HG2  A LYS   A 1 29  ? 14.437 -0.754  19.863  0.50 36.43 ?  29  LYS   A HG2  1 
ATOM   824  H  HG2  B LYS   A 1 29  ? 14.350 -0.806  19.834  0.50 37.25 ?  29  LYS   A HG2  1 
ATOM   825  H  HG3  A LYS   A 1 29  ? 15.814 -1.064  20.595  0.50 36.43 ?  29  LYS   A HG3  1 
ATOM   826  H  HG3  B LYS   A 1 29  ? 15.702 -0.941  20.657  0.50 37.25 ?  29  LYS   A HG3  1 
ATOM   827  H  HD2  A LYS   A 1 29  ? 15.673 0.899   21.785  0.50 39.21 ?  29  LYS   A HD2  1 
ATOM   828  H  HD2  B LYS   A 1 29  ? 15.115 1.534   21.054  0.50 40.01 ?  29  LYS   A HD2  1 
ATOM   829  H  HD3  A LYS   A 1 29  ? 14.381 1.339   20.966  0.50 39.21 ?  29  LYS   A HD3  1 
ATOM   830  H  HD3  B LYS   A 1 29  ? 13.670 0.866   21.020  0.50 40.01 ?  29  LYS   A HD3  1 
ATOM   831  H  HE2  A LYS   A 1 29  ? 13.215 -0.484  21.926  0.50 41.14 ?  29  LYS   A HE2  1 
ATOM   832  H  HE2  B LYS   A 1 29  ? 14.602 -0.712  22.654  0.50 41.98 ?  29  LYS   A HE2  1 
ATOM   833  H  HE3  A LYS   A 1 29  ? 14.492 -0.780  22.828  0.50 41.14 ?  29  LYS   A HE3  1 
ATOM   834  H  HE3  B LYS   A 1 29  ? 15.720 0.399   22.876  0.50 41.98 ?  29  LYS   A HE3  1 
ATOM   835  H  HZ1  A LYS   A 1 29  ? 12.969 0.450   23.984  0.50 42.33 ?  29  LYS   A HZ1  1 
ATOM   836  H  HZ1  B LYS   A 1 29  ? 14.034 0.654   24.377  0.50 43.10 ?  29  LYS   A HZ1  1 
ATOM   837  H  HZ2  A LYS   A 1 29  ? 14.170 1.243   23.821  0.50 42.33 ?  29  LYS   A HZ2  1 
ATOM   838  H  HZ2  B LYS   A 1 29  ? 14.071 1.826   23.526  0.50 43.10 ?  29  LYS   A HZ2  1 
ATOM   839  H  HZ3  A LYS   A 1 29  ? 13.008 1.512   22.999  0.50 42.33 ?  29  LYS   A HZ3  1 
ATOM   840  H  HZ3  B LYS   A 1 29  ? 13.053 0.814   23.323  0.50 43.10 ?  29  LYS   A HZ3  1 
ATOM   841  N  N    . VAL   A 1 30  ? 18.570 -1.291  18.860  1.00 24.02 ?  30  VAL   A N    1 
ATOM   842  C  CA   . VAL   A 1 30  ? 19.228 -2.555  19.169  1.00 22.94 ?  30  VAL   A CA   1 
ATOM   843  C  C    . VAL   A 1 30  ? 20.732 -2.396  19.383  1.00 21.59 ?  30  VAL   A C    1 
ATOM   844  O  O    . VAL   A 1 30  ? 21.320 -3.112  20.199  1.00 22.03 ?  30  VAL   A O    1 
ATOM   845  C  CB   . VAL   A 1 30  ? 18.928 -3.557  18.038  1.00 24.03 ?  30  VAL   A CB   1 
ATOM   846  C  CG1  . VAL   A 1 30  ? 19.692 -4.856  18.246  1.00 24.43 ?  30  VAL   A CG1  1 
ATOM   847  C  CG2  . VAL   A 1 30  ? 17.431 -3.824  17.943  1.00 25.21 ?  30  VAL   A CG2  1 
ATOM   848  H  H    A VAL   A 1 30  ? 18.415 -1.162  18.026  0.50 28.85 ?  30  VAL   A H    1 
ATOM   849  H  H    B VAL   A 1 30  ? 18.525 -1.122  18.020  0.50 28.85 ?  30  VAL   A H    1 
ATOM   850  H  HA   . VAL   A 1 30  ? 18.842 -2.918  19.983  1.00 27.56 ?  30  VAL   A HA   1 
ATOM   851  H  HB   . VAL   A 1 30  ? 19.216 -3.179  17.191  1.00 28.87 ?  30  VAL   A HB   1 
ATOM   852  H  HG11 . VAL   A 1 30  ? 19.318 -5.538  17.664  1.00 29.35 ?  30  VAL   A HG11 1 
ATOM   853  H  HG12 . VAL   A 1 30  ? 20.625 -4.714  18.029  1.00 29.35 ?  30  VAL   A HG12 1 
ATOM   854  H  HG13 . VAL   A 1 30  ? 19.600 -5.128  19.172  1.00 29.35 ?  30  VAL   A HG13 1 
ATOM   855  H  HG21 . VAL   A 1 30  ? 17.271 -4.497  17.261  1.00 30.29 ?  30  VAL   A HG21 1 
ATOM   856  H  HG22 . VAL   A 1 30  ? 17.115 -4.143  18.802  1.00 30.29 ?  30  VAL   A HG22 1 
ATOM   857  H  HG23 . VAL   A 1 30  ? 16.979 -3.000  17.706  1.00 30.29 ?  30  VAL   A HG23 1 
ATOM   858  N  N    . LYS   A 1 31  ? 21.367 -1.470  18.672  1.00 21.01 ?  31  LYS   A N    1 
ATOM   859  C  CA   . LYS   A 1 31  ? 22.821 -1.358  18.628  1.00 21.81 ?  31  LYS   A CA   1 
ATOM   860  C  C    . LYS   A 1 31  ? 23.441 -2.714  18.284  1.00 19.72 ?  31  LYS   A C    1 
ATOM   861  O  O    . LYS   A 1 31  ? 24.227 -3.264  19.064  1.00 20.92 ?  31  LYS   A O    1 
ATOM   862  C  CB   . LYS   A 1 31  ? 23.396 -0.804  19.923  1.00 26.83 ?  31  LYS   A CB   1 
ATOM   863  C  CG   . LYS   A 1 31  ? 22.728 0.478   20.394  1.00 32.71 ?  31  LYS   A CG   1 
ATOM   864  C  CD   . LYS   A 1 31  ? 23.752 1.547   20.749  1.00 37.28 ?  31  LYS   A CD   1 
ATOM   865  C  CE   . LYS   A 1 31  ? 23.168 2.583   21.698  1.00 40.38 ?  31  LYS   A CE   1 
ATOM   866  N  NZ   . LYS   A 1 31  ? 21.909 3.192   21.183  1.00 41.76 ?  31  LYS   A NZ   1 
ATOM   867  H  H    . LYS   A 1 31  ? 20.965 -0.885  18.192  1.00 25.24 ?  31  LYS   A H    1 
ATOM   868  H  HA   . LYS   A 1 31  ? 23.053 -0.741  17.925  1.00 26.21 ?  31  LYS   A HA   1 
ATOM   869  H  HB2  . LYS   A 1 31  ? 23.294 -1.470  20.613  1.00 32.23 ?  31  LYS   A HB2  1 
ATOM   870  H  HB3  . LYS   A 1 31  ? 24.340 -0.617  19.785  1.00 32.23 ?  31  LYS   A HB3  1 
ATOM   871  H  HG2  . LYS   A 1 31  ? 22.162 0.824   19.686  1.00 39.29 ?  31  LYS   A HG2  1 
ATOM   872  H  HG3  . LYS   A 1 31  ? 22.199 0.291   21.185  1.00 39.29 ?  31  LYS   A HG3  1 
ATOM   873  H  HD2  . LYS   A 1 31  ? 24.513 1.132   21.183  1.00 44.77 ?  31  LYS   A HD2  1 
ATOM   874  H  HD3  . LYS   A 1 31  ? 24.034 2.001   19.938  1.00 44.77 ?  31  LYS   A HD3  1 
ATOM   875  H  HE2  . LYS   A 1 31  ? 22.970 2.157   22.546  1.00 48.49 ?  31  LYS   A HE2  1 
ATOM   876  H  HE3  . LYS   A 1 31  ? 23.815 3.294   21.827  1.00 48.49 ?  31  LYS   A HE3  1 
ATOM   877  H  HZ1  . LYS   A 1 31  ? 21.614 3.808   21.755  1.00 50.15 ?  31  LYS   A HZ1  1 
ATOM   878  H  HZ2  . LYS   A 1 31  ? 22.057 3.577   20.395  1.00 50.15 ?  31  LYS   A HZ2  1 
ATOM   879  H  HZ3  . LYS   A 1 31  ? 21.285 2.565   21.087  1.00 50.15 ?  31  LYS   A HZ3  1 
ATOM   880  N  N    . PRO   A 1 32  ? 23.105 -3.274  17.130  1.00 17.60 ?  32  PRO   A N    1 
ATOM   881  C  CA   . PRO   A 1 32  ? 23.586 -4.612  16.786  1.00 17.94 ?  32  PRO   A CA   1 
ATOM   882  C  C    . PRO   A 1 32  ? 25.087 -4.623  16.574  1.00 17.98 ?  32  PRO   A C    1 
ATOM   883  O  O    . PRO   A 1 32  ? 25.724 -3.592  16.348  1.00 17.67 ?  32  PRO   A O    1 
ATOM   884  C  CB   . PRO   A 1 32  ? 22.855 -4.912  15.474  1.00 18.13 ?  32  PRO   A CB   1 
ATOM   885  C  CG   . PRO   A 1 32  ? 22.672 -3.555  14.857  1.00 16.81 ?  32  PRO   A CG   1 
ATOM   886  C  CD   . PRO   A 1 32  ? 22.373 -2.650  16.017  1.00 16.80 ?  32  PRO   A CD   1 
ATOM   887  H  HA   . PRO   A 1 32  ? 23.342 -5.261  17.461  1.00 21.56 ?  32  PRO   A HA   1 
ATOM   888  H  HB2  . PRO   A 1 32  ? 23.402 -5.484  14.907  1.00 21.78 ?  32  PRO   A HB2  1 
ATOM   889  H  HB3  . PRO   A 1 32  ? 21.999 -5.330  15.659  1.00 21.78 ?  32  PRO   A HB3  1 
ATOM   890  H  HG2  . PRO   A 1 32  ? 23.487 -3.292  14.402  1.00 20.20 ?  32  PRO   A HG2  1 
ATOM   891  H  HG3  . PRO   A 1 32  ? 21.926 -3.583  14.231  1.00 20.20 ?  32  PRO   A HG3  1 
ATOM   892  H  HD2  . PRO   A 1 32  ? 22.714 -1.760  15.831  1.00 20.20 ?  32  PRO   A HD2  1 
ATOM   893  H  HD3  . PRO   A 1 32  ? 21.423 -2.642  16.195  1.00 20.20 ?  32  PRO   A HD3  1 
ATOM   894  N  N    . THR   A 1 33  ? 25.649 -5.830  16.620  1.00 17.68 ?  33  THR   A N    1 
ATOM   895  C  CA   . THR   A 1 33  ? 27.059 -5.990  16.289  1.00 17.78 ?  33  THR   A CA   1 
ATOM   896  C  C    . THR   A 1 33  ? 27.342 -5.532  14.865  1.00 15.90 ?  33  THR   A C    1 
ATOM   897  O  O    . THR   A 1 33  ? 28.372 -4.893  14.607  1.00 15.88 ?  33  THR   A O    1 
ATOM   898  C  CB   . THR   A 1 33  ? 27.472 -7.448  16.490  1.00 19.07 ?  33  THR   A CB   1 
ATOM   899  O  OG1  . THR   A 1 33  ? 27.180 -7.833  17.837  1.00 21.07 ?  33  THR   A OG1  1 
ATOM   900  C  CG2  . THR   A 1 33  ? 28.963 -7.637  16.226  1.00 19.87 ?  33  THR   A CG2  1 
ATOM   901  H  H    . THR   A 1 33  ? 25.246 -6.561  16.831  1.00 21.25 ?  33  THR   A H    1 
ATOM   902  H  HA   . THR   A 1 33  ? 27.592 -5.450  16.891  1.00 21.37 ?  33  THR   A HA   1 
ATOM   903  H  HB   . THR   A 1 33  ? 26.981 -8.022  15.876  1.00 22.91 ?  33  THR   A HB   1 
ATOM   904  H  HG1  . THR   A 1 33  ? 27.618 -7.355  18.374  1.00 25.32 ?  33  THR   A HG1  1 
ATOM   905  H  HG21 . THR   A 1 33  ? 29.243 -8.524  16.502  1.00 23.88 ?  33  THR   A HG21 1 
ATOM   906  H  HG22 . THR   A 1 33  ? 29.151 -7.530  15.279  1.00 23.88 ?  33  THR   A HG22 1 
ATOM   907  H  HG23 . THR   A 1 33  ? 29.471 -6.978  16.725  1.00 23.88 ?  33  THR   A HG23 1 
ATOM   908  N  N    . VAL   A 1 34  ? 26.444 -5.852  13.930  1.00 14.56 ?  34  VAL   A N    1 
ATOM   909  C  CA   . VAL   A 1 34  ? 26.622 -5.518  12.520  1.00 13.38 ?  34  VAL   A CA   1 
ATOM   910  C  C    . VAL   A 1 34  ? 25.317 -4.962  11.961  1.00 12.63 ?  34  VAL   A C    1 
ATOM   911  O  O    . VAL   A 1 34  ? 24.278 -5.634  12.011  1.00 13.38 ?  34  VAL   A O    1 
ATOM   912  C  CB   . VAL   A 1 34  ? 27.073 -6.729  11.678  1.00 14.04 ?  34  VAL   A CB   1 
ATOM   913  C  CG1  . VAL   A 1 34  ? 27.264 -6.323  10.221  1.00 14.40 ?  34  VAL   A CG1  1 
ATOM   914  C  CG2  . VAL   A 1 34  ? 28.350 -7.343  12.242  1.00 15.17 ?  34  VAL   A CG2  1 
ATOM   915  H  H    . VAL   A 1 34  ? 25.717 -6.282  14.090  1.00 17.50 ?  34  VAL   A H    1 
ATOM   916  H  HA   . VAL   A 1 34  ? 27.298 -4.827  12.435  1.00 16.09 ?  34  VAL   A HA   1 
ATOM   917  H  HB   . VAL   A 1 34  ? 26.380 -7.404  11.706  1.00 16.88 ?  34  VAL   A HB   1 
ATOM   918  H  HG11 . VAL   A 1 34  ? 27.744 -7.029  9.759   1.00 17.31 ?  34  VAL   A HG11 1 
ATOM   919  H  HG12 . VAL   A 1 34  ? 26.399 -6.187  9.810   1.00 17.31 ?  34  VAL   A HG12 1 
ATOM   920  H  HG13 . VAL   A 1 34  ? 27.783 -5.501  10.188  1.00 17.31 ?  34  VAL   A HG13 1 
ATOM   921  H  HG21 . VAL   A 1 34  ? 28.631 -8.073  11.665  1.00 18.23 ?  34  VAL   A HG21 1 
ATOM   922  H  HG22 . VAL   A 1 34  ? 29.042 -6.665  12.276  1.00 18.23 ?  34  VAL   A HG22 1 
ATOM   923  H  HG23 . VAL   A 1 34  ? 28.172 -7.680  13.134  1.00 18.23 ?  34  VAL   A HG23 1 
ATOM   924  N  N    . VAL   A 1 35  ? 25.376 -3.752  11.402  1.00 11.86 ?  35  VAL   A N    1 
ATOM   925  C  CA   . VAL   A 1 35  ? 24.334 -3.234  10.520  1.00 11.28 ?  35  VAL   A CA   1 
ATOM   926  C  C    . VAL   A 1 35  ? 24.878 -3.235  9.100   1.00 10.67 ?  35  VAL   A C    1 
ATOM   927  O  O    . VAL   A 1 35  ? 26.021 -2.829  8.864   1.00 11.32 ?  35  VAL   A O    1 
ATOM   928  C  CB   . VAL   A 1 35  ? 23.816 -1.842  10.947  1.00 12.01 ?  35  VAL   A CB   1 
ATOM   929  C  CG1  . VAL   A 1 35  ? 24.885 -0.746  10.809  1.00 12.62 ?  35  VAL   A CG1  1 
ATOM   930  C  CG2  . VAL   A 1 35  ? 22.551 -1.477  10.155  1.00 12.78 ?  35  VAL   A CG2  1 
ATOM   931  H  H    . VAL   A 1 35  ? 26.022 -3.198  11.521  1.00 14.27 ?  35  VAL   A H    1 
ATOM   932  H  HA   . VAL   A 1 35  ? 23.573 -3.842  10.546  1.00 13.57 ?  35  VAL   A HA   1 
ATOM   933  H  HB   . VAL   A 1 35  ? 23.562 -1.878  11.878  1.00 14.45 ?  35  VAL   A HB   1 
ATOM   934  H  HG11 . VAL   A 1 35  ? 24.543 0.086   11.180  1.00 15.18 ?  35  VAL   A HG11 1 
ATOM   935  H  HG12 . VAL   A 1 35  ? 25.681 -1.017  11.294  1.00 15.18 ?  35  VAL   A HG12 1 
ATOM   936  H  HG13 . VAL   A 1 35  ? 25.101 -0.619  9.870   1.00 15.18 ?  35  VAL   A HG13 1 
ATOM   937  H  HG21 . VAL   A 1 35  ? 22.218 -0.617  10.460  1.00 15.37 ?  35  VAL   A HG21 1 
ATOM   938  H  HG22 . VAL   A 1 35  ? 22.766 -1.428  9.208   1.00 15.37 ?  35  VAL   A HG22 1 
ATOM   939  H  HG23 . VAL   A 1 35  ? 21.876 -2.160  10.302  1.00 15.37 ?  35  VAL   A HG23 1 
ATOM   940  N  N    A VAL   A 1 36  ? 24.050 -3.681  8.160   0.50 10.36 ?  36  VAL   A N    1 
ATOM   941  N  N    B VAL   A 1 36  ? 24.070 -3.706  8.152   0.50 10.24 ?  36  VAL   A N    1 
ATOM   942  C  CA   A VAL   A 1 36  ? 24.398 -3.675  6.746   0.50 10.03 ?  36  VAL   A CA   1 
ATOM   943  C  CA   B VAL   A 1 36  ? 24.465 -3.731  6.747   0.50 10.05 ?  36  VAL   A CA   1 
ATOM   944  C  C    A VAL   A 1 36  ? 23.957 -2.354  6.132   0.50 9.99  ?  36  VAL   A C    1 
ATOM   945  C  C    B VAL   A 1 36  ? 23.974 -2.467  6.050   0.50 9.86  ?  36  VAL   A C    1 
ATOM   946  O  O    A VAL   A 1 36  ? 22.830 -1.894  6.359   0.50 10.54 ?  36  VAL   A O    1 
ATOM   947  O  O    B VAL   A 1 36  ? 22.789 -2.112  6.134   0.50 10.05 ?  36  VAL   A O    1 
ATOM   948  C  CB   A VAL   A 1 36  ? 23.738 -4.858  6.018   0.50 9.68  ?  36  VAL   A CB   1 
ATOM   949  C  CB   B VAL   A 1 36  ? 23.915 -4.983  6.045   0.50 10.24 ?  36  VAL   A CB   1 
ATOM   950  C  CG1  A VAL   A 1 36  ? 23.947 -4.749  4.522   0.50 9.61  ?  36  VAL   A CG1  1 
ATOM   951  C  CG1  B VAL   A 1 36  ? 24.241 -4.952  4.561   0.50 10.23 ?  36  VAL   A CG1  1 
ATOM   952  C  CG2  A VAL   A 1 36  ? 24.279 -6.178  6.540   0.50 10.62 ?  36  VAL   A CG2  1 
ATOM   953  C  CG2  B VAL   A 1 36  ? 24.470 -6.242  6.687   0.50 11.11 ?  36  VAL   A CG2  1 
ATOM   954  H  H    A VAL   A 1 36  ? 23.259 -3.993  8.318   0.50 12.46 ?  36  VAL   A H    1 
ATOM   955  H  H    B VAL   A 1 36  ? 23.282 -4.031  8.299   0.50 12.32 ?  36  VAL   A H    1 
ATOM   956  H  HA   A VAL   A 1 36  ? 25.359 -3.756  6.649   0.50 12.06 ?  36  VAL   A HA   1 
ATOM   957  H  HA   B VAL   A 1 36  ? 25.437 -3.767  6.693   0.50 12.10 ?  36  VAL   A HA   1 
ATOM   958  H  HB   A VAL   A 1 36  ? 22.782 -4.838  6.188   0.50 11.65 ?  36  VAL   A HB   1 
ATOM   959  H  HB   B VAL   A 1 36  ? 22.952 -5.005  6.137   0.50 12.32 ?  36  VAL   A HB   1 
ATOM   960  H  HG11 A VAL   A 1 36  ? 23.780 -5.615  4.121   0.50 11.56 ?  36  VAL   A HG11 1 
ATOM   961  H  HG11 B VAL   A 1 36  ? 24.112 -5.839  4.188   0.50 12.31 ?  36  VAL   A HG11 1 
ATOM   962  H  HG12 A VAL   A 1 36  ? 23.329 -4.094  4.163   0.50 11.56 ?  36  VAL   A HG12 1 
ATOM   963  H  HG12 B VAL   A 1 36  ? 23.654 -4.321  4.119   0.50 12.31 ?  36  VAL   A HG12 1 
ATOM   964  H  HG13 A VAL   A 1 36  ? 24.861 -4.476  4.354   0.50 11.56 ?  36  VAL   A HG13 1 
ATOM   965  H  HG13 B VAL   A 1 36  ? 25.167 -4.682  4.447   0.50 12.31 ?  36  VAL   A HG13 1 
ATOM   966  H  HG21 A VAL   A 1 36  ? 23.850 -6.909  6.066   0.50 12.78 ?  36  VAL   A HG21 1 
ATOM   967  H  HG21 B VAL   A 1 36  ? 24.135 -7.018  6.206   0.50 13.37 ?  36  VAL   A HG21 1 
ATOM   968  H  HG22 A VAL   A 1 36  ? 25.238 -6.209  6.392   0.50 12.78 ?  36  VAL   A HG22 1 
ATOM   969  H  HG22 B VAL   A 1 36  ? 25.438 -6.220  6.642   0.50 13.37 ?  36  VAL   A HG22 1 
ATOM   970  H  HG23 A VAL   A 1 36  ? 24.090 -6.248  7.490   0.50 12.78 ?  36  VAL   A HG23 1 
ATOM   971  H  HG23 B VAL   A 1 36  ? 24.180 -6.278  7.611   0.50 13.37 ?  36  VAL   A HG23 1 
ATOM   972  N  N    A ASN   A 1 37  ? 24.849 -1.748  5.353   0.50 9.76  ?  37  ASN   A N    1 
ATOM   973  N  N    B ASN   A 1 37  ? 24.882 -1.804  5.336   0.50 9.66  ?  37  ASN   A N    1 
ATOM   974  C  CA   A ASN   A 1 37  ? 24.525 -0.603  4.520   0.50 9.62  ?  37  ASN   A CA   1 
ATOM   975  C  CA   B ASN   A 1 37  ? 24.526 -0.697  4.462   0.50 9.32  ?  37  ASN   A CA   1 
ATOM   976  C  C    A ASN   A 1 37  ? 24.343 -1.048  3.075   0.50 9.67  ?  37  ASN   A C    1 
ATOM   977  C  C    B ASN   A 1 37  ? 24.406 -1.179  3.024   0.50 9.30  ?  37  ASN   A C    1 
ATOM   978  O  O    A ASN   A 1 37  ? 25.079 -1.908  2.578   0.50 10.64 ?  37  ASN   A O    1 
ATOM   979  O  O    B ASN   A 1 37  ? 25.226 -1.976  2.550   0.50 9.68  ?  37  ASN   A O    1 
ATOM   980  C  CB   A ASN   A 1 37  ? 25.638 0.442   4.590   0.50 9.62  ?  37  ASN   A CB   1 
ATOM   981  C  CB   B ASN   A 1 37  ? 25.574 0.414   4.533   0.50 9.70  ?  37  ASN   A CB   1 
ATOM   982  C  CG   A ASN   A 1 37  ? 25.286 1.697   3.837   0.50 9.38  ?  37  ASN   A CG   1 
ATOM   983  C  CG   B ASN   A 1 37  ? 25.250 1.578   3.604   0.50 9.89  ?  37  ASN   A CG   1 
ATOM   984  O  OD1  A ASN   A 1 37  ? 24.106 2.038   3.716   0.50 9.50  ?  37  ASN   A OD1  1 
ATOM   985  O  OD1  B ASN   A 1 37  ? 24.079 1.902   3.372   0.50 9.78  ?  37  ASN   A OD1  1 
ATOM   986  N  ND2  A ASN   A 1 37  ? 26.297 2.387   3.317   0.50 9.23  ?  37  ASN   A ND2  1 
ATOM   987  N  ND2  B ASN   A 1 37  ? 26.288 2.199   3.058   0.50 9.59  ?  37  ASN   A ND2  1 
ATOM   988  H  H    A ASN   A 1 37  ? 25.674 -1.987  5.296   0.50 11.74 ?  37  ASN   A H    1 
ATOM   989  H  H    B ASN   A 1 37  ? 25.728 -1.986  5.348   0.50 11.62 ?  37  ASN   A H    1 
ATOM   990  H  HA   A ASN   A 1 37  ? 23.701 -0.197  4.824   0.50 11.58 ?  37  ASN   A HA   1 
ATOM   991  H  HA   B ASN   A 1 37  ? 23.674 -0.339  4.744   0.50 11.22 ?  37  ASN   A HA   1 
ATOM   992  H  HB2  A ASN   A 1 37  ? 25.783 0.686   5.517   0.50 11.58 ?  37  ASN   A HB2  1 
ATOM   993  H  HB2  B ASN   A 1 37  ? 25.615 0.746   5.447   0.50 11.67 ?  37  ASN   A HB2  1 
ATOM   994  H  HB3  A ASN   A 1 37  ? 26.454 0.071   4.212   0.50 11.58 ?  37  ASN   A HB3  1 
ATOM   995  H  HB3  B ASN   A 1 37  ? 26.438 0.047   4.279   0.50 11.67 ?  37  ASN   A HB3  1 
ATOM   996  H  HD21 A ASN   A 1 37  ? 26.147 3.106   2.871   0.50 11.11 ?  37  ASN   A HD21 1 
ATOM   997  H  HD21 B ASN   A 1 37  ? 26.158 2.858   2.531   0.50 11.54 ?  37  ASN   A HD21 1 
ATOM   998  H  HD22 A ASN   A 1 37  ? 27.106 2.119   3.421   0.50 11.11 ?  37  ASN   A HD22 1 
ATOM   999  H  HD22 B ASN   A 1 37  ? 27.085 1.939   3.236   0.50 11.54 ?  37  ASN   A HD22 1 
ATOM   1000 N  N    A ALA   A 1 38  ? 23.347 -0.456  2.410   0.50 9.55  ?  38  ALA   A N    1 
ATOM   1001 N  N    B ALA   A 1 38  ? 23.373 -0.689  2.335   0.50 9.71  ?  38  ALA   A N    1 
ATOM   1002 C  CA   A ALA   A 1 38  ? 23.133 -0.614  0.971   0.50 8.98  ?  38  ALA   A CA   1 
ATOM   1003 C  CA   B ALA   A 1 38  ? 23.199 -0.903  0.898   0.50 10.42 ?  38  ALA   A CA   1 
ATOM   1004 C  C    A ALA   A 1 38  ? 24.067 0.354   0.244   0.50 9.44  ?  38  ALA   A C    1 
ATOM   1005 C  C    B ALA   A 1 38  ? 24.030 0.147   0.159   0.50 10.17 ?  38  ALA   A C    1 
ATOM   1006 O  O    A ALA   A 1 38  ? 23.693 1.466   -0.140  0.50 9.20  ?  38  ALA   A O    1 
ATOM   1007 O  O    B ALA   A 1 38  ? 23.539 1.184   -0.302  0.50 10.14 ?  38  ALA   A O    1 
ATOM   1008 C  CB   A ALA   A 1 38  ? 21.669 -0.356  0.627   0.50 9.30  ?  38  ALA   A CB   1 
ATOM   1009 C  CB   B ALA   A 1 38  ? 21.723 -0.827  0.534   0.50 11.13 ?  38  ALA   A CB   1 
ATOM   1010 H  H    A ALA   A 1 38  ? 22.771 0.060   2.782   0.50 11.50 ?  38  ALA   A H    1 
ATOM   1011 H  H    B ALA   A 1 38  ? 22.754 -0.212  2.694   0.50 11.69 ?  38  ALA   A H    1 
ATOM   1012 H  HA   A ALA   A 1 38  ? 23.356 -1.516  0.702   0.50 10.82 ?  38  ALA   A HA   1 
ATOM   1013 H  HA   B ALA   A 1 38  ? 23.534 -1.789  0.664   0.50 12.53 ?  38  ALA   A HA   1 
ATOM   1014 H  HB1  A ALA   A 1 38  ? 21.537 -0.476  -0.326  0.50 11.19 ?  38  ALA   A HB1  1 
ATOM   1015 H  HB1  B ALA   A 1 38  ? 21.633 -0.946  -0.422  0.50 13.39 ?  38  ALA   A HB1  1 
ATOM   1016 H  HB2  A ALA   A 1 38  ? 21.115 -0.984  1.119   0.50 11.19 ?  38  ALA   A HB2  1 
ATOM   1017 H  HB2  B ALA   A 1 38  ? 21.241 -1.529  1.003   0.50 13.39 ?  38  ALA   A HB2  1 
ATOM   1018 H  HB3  A ALA   A 1 38  ? 21.438 0.553   0.881   0.50 11.19 ?  38  ALA   A HB3  1 
ATOM   1019 H  HB3  B ALA   A 1 38  ? 21.382 0.041   0.796   0.50 13.39 ?  38  ALA   A HB3  1 
ATOM   1020 N  N    A ALA   A 1 39  ? 25.311 -0.085  0.055   0.50 9.48  ?  39  ALA   A N    1 
ATOM   1021 N  N    B ALA   A 1 39  ? 25.327 -0.127  0.060   0.50 10.75 ?  39  ALA   A N    1 
ATOM   1022 C  CA   A ALA   A 1 39  ? 26.406 0.758   -0.398  0.50 9.60  ?  39  ALA   A CA   1 
ATOM   1023 C  CA   B ALA   A 1 39  ? 26.292 0.826   -0.458  0.50 10.73 ?  39  ALA   A CA   1 
ATOM   1024 C  C    A ALA   A 1 39  ? 26.556 0.723   -1.914  0.50 9.81  ?  39  ALA   A C    1 
ATOM   1025 C  C    B ALA   A 1 39  ? 26.396 0.737   -1.979  0.50 10.02 ?  39  ALA   A C    1 
ATOM   1026 O  O    A ALA   A 1 39  ? 26.080 -0.190  -2.593  0.50 10.04 ?  39  ALA   A O    1 
ATOM   1027 O  O    B ALA   A 1 39  ? 25.909 -0.202  -2.613  0.50 10.62 ?  39  ALA   A O    1 
ATOM   1028 C  CB   A ALA   A 1 39  ? 27.710 0.291   0.255   0.50 9.74  ?  39  ALA   A CB   1 
ATOM   1029 C  CB   B ALA   A 1 39  ? 27.658 0.571   0.177   0.50 11.49 ?  39  ALA   A CB   1 
ATOM   1030 H  H    A ALA   A 1 39  ? 25.546 -0.903  0.184   0.50 11.41 ?  39  ALA   A H    1 
ATOM   1031 H  H    B ALA   A 1 39  ? 25.670 -0.884  0.289   0.50 12.94 ?  39  ALA   A H    1 
ATOM   1032 H  HA   A ALA   A 1 39  ? 26.236 1.674   -0.135  0.50 11.55 ?  39  ALA   A HA   1 
ATOM   1033 H  HA   B ALA   A 1 39  ? 26.004 1.721   -0.219  0.50 12.91 ?  39  ALA   A HA   1 
ATOM   1034 H  HB1  A ALA   A 1 39  ? 28.432 0.859   -0.047  0.50 11.72 ?  39  ALA   A HB1  1 
ATOM   1035 H  HB1  B ALA   A 1 39  ? 28.288 1.215   -0.177  0.50 13.82 ?  39  ALA   A HB1  1 
ATOM   1036 H  HB2  A ALA   A 1 39  ? 27.612 0.362   1.220   0.50 11.72 ?  39  ALA   A HB2  1 
ATOM   1037 H  HB2  B ALA   A 1 39  ? 27.581 0.676   1.140   0.50 13.82 ?  39  ALA   A HB2  1 
ATOM   1038 H  HB3  A ALA   A 1 39  ? 27.875 -0.628  0.005   0.50 11.72 ?  39  ALA   A HB3  1 
ATOM   1039 H  HB3  B ALA   A 1 39  ? 27.940 -0.329  -0.037  0.50 13.82 ?  39  ALA   A HB3  1 
ATOM   1040 N  N    A ASN   A 1 40  ? 27.255 1.733   -2.440  0.50 10.10 ?  40  ASN   A N    1 
ATOM   1041 N  N    B ASN   A 1 40  ? 27.039 1.747   -2.566  0.50 9.82  ?  40  ASN   A N    1 
ATOM   1042 C  CA   A ASN   A 1 40  ? 27.803 1.702   -3.790  0.50 10.08 ?  40  ASN   A CA   1 
ATOM   1043 C  CA   B ASN   A 1 40  ? 27.514 1.693   -3.941  0.50 9.96  ?  40  ASN   A CA   1 
ATOM   1044 C  C    A ASN   A 1 40  ? 29.327 1.604   -3.720  0.50 9.45  ?  40  ASN   A C    1 
ATOM   1045 C  C    B ASN   A 1 40  ? 29.038 1.589   -3.944  0.50 9.72  ?  40  ASN   A C    1 
ATOM   1046 O  O    A ASN   A 1 40  ? 29.928 1.717   -2.647  0.50 9.45  ?  40  ASN   A O    1 
ATOM   1047 O  O    B ASN   A 1 40  ? 29.690 1.692   -2.904  0.50 9.69  ?  40  ASN   A O    1 
ATOM   1048 C  CB   A ASN   A 1 40  ? 27.318 2.887   -4.646  0.50 10.93 ?  40  ASN   A CB   1 
ATOM   1049 C  CB   B ASN   A 1 40  ? 27.012 2.892   -4.764  0.50 10.87 ?  40  ASN   A CB   1 
ATOM   1050 C  CG   A ASN   A 1 40  ? 27.684 4.241   -4.066  0.50 12.13 ?  40  ASN   A CG   1 
ATOM   1051 C  CG   B ASN   A 1 40  ? 27.398 4.230   -4.166  0.50 11.10 ?  40  ASN   A CG   1 
ATOM   1052 O  OD1  A ASN   A 1 40  ? 28.833 4.482   -3.684  0.50 12.46 ?  40  ASN   A OD1  1 
ATOM   1053 O  OD1  B ASN   A 1 40  ? 28.583 4.560   -4.054  0.50 11.98 ?  40  ASN   A OD1  1 
ATOM   1054 N  ND2  A ASN   A 1 40  ? 26.703 5.144   -4.021  0.50 13.43 ?  40  ASN   A ND2  1 
ATOM   1055 N  ND2  B ASN   A 1 40  ? 26.391 5.027   -3.815  0.50 11.80 ?  40  ASN   A ND2  1 
ATOM   1056 H  H    A ASN   A 1 40  ? 27.437 2.462   -2.021  0.50 12.15 ?  40  ASN   A H    1 
ATOM   1057 H  H    B ASN   A 1 40  ? 27.210 2.489   -2.173  0.50 11.82 ?  40  ASN   A H    1 
ATOM   1058 H  HA   A ASN   A 1 40  ? 27.498 0.895   -4.228  0.50 12.13 ?  40  ASN   A HA   1 
ATOM   1059 H  HA   B ASN   A 1 40  ? 27.160 0.885   -4.355  0.50 11.98 ?  40  ASN   A HA   1 
ATOM   1060 H  HB2  A ASN   A 1 40  ? 27.713 2.817   -5.537  0.50 13.15 ?  40  ASN   A HB2  1 
ATOM   1061 H  HB2  B ASN   A 1 40  ? 27.390 2.836   -5.653  0.50 13.07 ?  40  ASN   A HB2  1 
ATOM   1062 H  HB3  A ASN   A 1 40  ? 26.352 2.845   -4.719  0.50 13.15 ?  40  ASN   A HB3  1 
ATOM   1063 H  HB3  B ASN   A 1 40  ? 26.041 2.852   -4.814  0.50 13.07 ?  40  ASN   A HB3  1 
ATOM   1064 H  HD21 A ASN   A 1 40  ? 26.856 5.933   -3.714  0.50 16.15 ?  40  ASN   A HD21 1 
ATOM   1065 H  HD21 B ASN   A 1 40  ? 26.558 5.798   -3.473  0.50 14.20 ?  40  ASN   A HD21 1 
ATOM   1066 H  HD22 A ASN   A 1 40  ? 25.914 4.934   -4.291  0.50 16.15 ?  40  ASN   A HD22 1 
ATOM   1067 H  HD22 B ASN   A 1 40  ? 25.579 4.770   -3.922  0.50 14.20 ?  40  ASN   A HD22 1 
ATOM   1068 N  N    A VAL   A 1 41  ? 29.949 1.359   -4.878  0.50 9.34  ?  41  VAL   A N    1 
ATOM   1069 N  N    B VAL   A 1 41  ? 29.609 1.368   -5.131  0.50 10.08 ?  41  VAL   A N    1 
ATOM   1070 C  CA   A VAL   A 1 41  ? 31.378 1.056   -4.905  0.50 9.49  ?  41  VAL   A CA   1 
ATOM   1071 C  CA   B VAL   A 1 41  ? 31.038 1.062   -5.225  0.50 10.62 ?  41  VAL   A CA   1 
ATOM   1072 C  C    A VAL   A 1 41  ? 32.226 2.217   -4.411  0.50 9.80  ?  41  VAL   A C    1 
ATOM   1073 C  C    B VAL   A 1 41  ? 31.915 2.211   -4.755  0.50 10.22 ?  41  VAL   A C    1 
ATOM   1074 O  O    A VAL   A 1 41  ? 33.348 2.002   -3.939  0.50 9.80  ?  41  VAL   A O    1 
ATOM   1075 O  O    B VAL   A 1 41  ? 33.077 1.991   -4.392  0.50 10.09 ?  41  VAL   A O    1 
ATOM   1076 C  CB   A VAL   A 1 41  ? 31.855 0.552   -6.293  0.50 9.54  ?  41  VAL   A CB   1 
ATOM   1077 C  CB   B VAL   A 1 41  ? 31.437 0.644   -6.656  0.50 11.81 ?  41  VAL   A CB   1 
ATOM   1078 C  CG1  A VAL   A 1 41  ? 31.146 -0.746  -6.671  0.50 10.13 ?  41  VAL   A CG1  1 
ATOM   1079 C  CG1  B VAL   A 1 41  ? 30.750 -0.654  -7.044  0.50 12.43 ?  41  VAL   A CG1  1 
ATOM   1080 C  CG2  A VAL   A 1 41  ? 31.688 1.609   -7.388  0.50 9.64  ?  41  VAL   A CG2  1 
ATOM   1081 C  CG2  B VAL   A 1 41  ? 31.123 1.753   -7.656  0.50 12.57 ?  41  VAL   A CG2  1 
ATOM   1082 H  H    A VAL   A 1 41  ? 29.577 1.356   -5.652  0.50 11.24 ?  41  VAL   A H    1 
ATOM   1083 H  H    B VAL   A 1 41  ? 29.193 1.390   -5.881  0.50 12.13 ?  41  VAL   A H    1 
ATOM   1084 H  HA   A VAL   A 1 41  ? 31.542 0.331   -4.289  0.50 11.42 ?  41  VAL   A HA   1 
ATOM   1085 H  HA   B VAL   A 1 41  ? 31.217 0.305   -4.645  0.50 12.78 ?  41  VAL   A HA   1 
ATOM   1086 H  HB   A VAL   A 1 41  ? 32.803 0.350   -6.240  0.50 11.48 ?  41  VAL   A HB   1 
ATOM   1087 H  HB   B VAL   A 1 41  ? 32.394 0.489   -6.675  0.50 14.20 ?  41  VAL   A HB   1 
ATOM   1088 H  HG11 A VAL   A 1 41  ? 31.474 -1.054  -7.531  0.50 12.19 ?  41  VAL   A HG11 1 
ATOM   1089 H  HG11 B VAL   A 1 41  ? 30.966 -0.860  -7.964  0.50 14.95 ?  41  VAL   A HG11 1 
ATOM   1090 H  HG12 A VAL   A 1 41  ? 31.323 -1.414  -5.990  0.50 12.19 ?  41  VAL   A HG12 1 
ATOM   1091 H  HG12 B VAL   A 1 41  ? 31.067 -1.364  -6.461  0.50 14.95 ?  41  VAL   A HG12 1 
ATOM   1092 H  HG13 A VAL   A 1 41  ? 30.189 -0.579  -6.726  0.50 12.19 ?  41  VAL   A HG13 1 
ATOM   1093 H  HG13 B VAL   A 1 41  ? 29.792 -0.549  -6.942  0.50 14.95 ?  41  VAL   A HG13 1 
ATOM   1094 H  HG21 A VAL   A 1 41  ? 31.941 1.220   -8.243  0.50 11.60 ?  41  VAL   A HG21 1 
ATOM   1095 H  HG21 B VAL   A 1 41  ? 31.389 1.462   -8.540  0.50 15.12 ?  41  VAL   A HG21 1 
ATOM   1096 H  HG22 A VAL   A 1 41  ? 30.764 1.891   -7.414  0.50 11.60 ?  41  VAL   A HG22 1 
ATOM   1097 H  HG22 B VAL   A 1 41  ? 30.167 1.931   -7.642  0.50 15.12 ?  41  VAL   A HG22 1 
ATOM   1098 H  HG23 A VAL   A 1 41  ? 32.265 2.362   -7.187  0.50 11.60 ?  41  VAL   A HG23 1 
ATOM   1099 H  HG23 B VAL   A 1 41  ? 31.610 2.553   -7.409  0.50 15.12 ?  41  VAL   A HG23 1 
ATOM   1100 N  N    A TYR   A 1 42  ? 31.722 3.448   -4.504  0.50 9.75  ?  42  TYR   A N    1 
ATOM   1101 N  N    B TYR   A 1 42  ? 31.401 3.442   -4.781  0.50 10.21 ?  42  TYR   A N    1 
ATOM   1102 C  CA   A TYR   A 1 42  ? 32.459 4.631   -4.073  0.50 9.99  ?  42  TYR   A CA   1 
ATOM   1103 C  CA   B TYR   A 1 42  ? 32.150 4.623   -4.368  0.50 10.48 ?  42  TYR   A CA   1 
ATOM   1104 C  C    A TYR   A 1 42  ? 32.152 5.015   -2.631  0.50 9.93  ?  42  TYR   A C    1 
ATOM   1105 C  C    B TYR   A 1 42  ? 31.927 4.994   -2.911  0.50 10.42 ?  42  TYR   A C    1 
ATOM   1106 O  O    A TYR   A 1 42  ? 32.714 5.995   -2.127  0.50 10.32 ?  42  TYR   A O    1 
ATOM   1107 O  O    B TYR   A 1 42  ? 32.488 5.995   -2.450  0.50 11.10 ?  42  TYR   A O    1 
ATOM   1108 C  CB   A TYR   A 1 42  ? 32.165 5.819   -5.009  0.50 10.62 ?  42  TYR   A CB   1 
ATOM   1109 C  CB   B TYR   A 1 42  ? 31.786 5.817   -5.260  0.50 11.15 ?  42  TYR   A CB   1 
ATOM   1110 C  CG   A TYR   A 1 42  ? 32.332 5.492   -6.484  0.50 11.35 ?  42  TYR   A CG   1 
ATOM   1111 C  CG   B TYR   A 1 42  ? 31.981 5.529   -6.727  0.50 11.70 ?  42  TYR   A CG   1 
ATOM   1112 C  CD1  A TYR   A 1 42  ? 33.591 5.296   -7.037  0.50 12.62 ?  42  TYR   A CD1  1 
ATOM   1113 C  CD1  B TYR   A 1 42  ? 33.248 5.346   -7.249  0.50 11.96 ?  42  TYR   A CD1  1 
ATOM   1114 C  CD2  A TYR   A 1 42  ? 31.229 5.367   -7.319  0.50 12.56 ?  42  TYR   A CD2  1 
ATOM   1115 C  CD2  B TYR   A 1 42  ? 30.894 5.415   -7.585  0.50 13.14 ?  42  TYR   A CD2  1 
ATOM   1116 C  CE1  A TYR   A 1 42  ? 33.748 4.985   -8.382  0.50 13.06 ?  42  TYR   A CE1  1 
ATOM   1117 C  CE1  B TYR   A 1 42  ? 33.435 5.065   -8.588  0.50 12.80 ?  42  TYR   A CE1  1 
ATOM   1118 C  CE2  A TYR   A 1 42  ? 31.378 5.063   -8.663  0.50 13.54 ?  42  TYR   A CE2  1 
ATOM   1119 C  CE2  B TYR   A 1 42  ? 31.071 5.143   -8.929  0.50 14.45 ?  42  TYR   A CE2  1 
ATOM   1120 C  CZ   A TYR   A 1 42  ? 32.640 4.873   -9.189  0.50 13.66 ?  42  TYR   A CZ   1 
ATOM   1121 C  CZ   B TYR   A 1 42  ? 32.344 4.966   -9.426  0.50 14.06 ?  42  TYR   A CZ   1 
ATOM   1122 O  OH   A TYR   A 1 42  ? 32.786 4.563   -10.523 0.50 15.41 ?  42  TYR   A OH   1 
ATOM   1123 O  OH   B TYR   A 1 42  ? 32.529 4.692   -10.761 0.50 15.63 ?  42  TYR   A OH   1 
ATOM   1124 H  H    A TYR   A 1 42  ? 30.943 3.624   -4.814  0.50 11.73 ?  42  TYR   A H    1 
ATOM   1125 H  H    B TYR   A 1 42  ? 30.600 3.622   -5.050  0.50 12.29 ?  42  TYR   A H    1 
ATOM   1126 H  HA   A TYR   A 1 42  ? 33.411 4.448   -4.134  0.50 12.02 ?  42  TYR   A HA   1 
ATOM   1127 H  HA   B TYR   A 1 42  ? 33.091 4.451   -4.483  0.50 12.61 ?  42  TYR   A HA   1 
ATOM   1128 H  HB2  A TYR   A 1 42  ? 31.252 6.109   -4.873  0.50 12.78 ?  42  TYR   A HB2  1 
ATOM   1129 H  HB2  B TYR   A 1 42  ? 30.854 6.050   -5.120  0.50 13.41 ?  42  TYR   A HB2  1 
ATOM   1130 H  HB3  A TYR   A 1 42  ? 32.776 6.546   -4.797  0.50 12.78 ?  42  TYR   A HB3  1 
ATOM   1131 H  HB3  B TYR   A 1 42  ? 32.352 6.572   -5.026  0.50 13.41 ?  42  TYR   A HB3  1 
ATOM   1132 H  HD1  A TYR   A 1 42  ? 34.348 5.372   -6.501  0.50 15.18 ?  42  TYR   A HD1  1 
ATOM   1133 H  HD1  B TYR   A 1 42  ? 33.986 5.411   -6.684  0.50 14.39 ?  42  TYR   A HD1  1 
ATOM   1134 H  HD2  A TYR   A 1 42  ? 30.378 5.497   -6.971  0.50 15.11 ?  42  TYR   A HD2  1 
ATOM   1135 H  HD2  B TYR   A 1 42  ? 30.031 5.537   -7.252  0.50 15.80 ?  42  TYR   A HD2  1 
ATOM   1136 H  HE1  A TYR   A 1 42  ? 34.599 4.860   -8.744  0.50 15.71 ?  42  TYR   A HE1  1 
ATOM   1137 H  HE1  B TYR   A 1 42  ? 34.295 4.948   -8.917  0.50 15.40 ?  42  TYR   A HE1  1 
ATOM   1138 H  HE2  A TYR   A 1 42  ? 30.625 4.986   -9.210  0.50 16.28 ?  42  TYR   A HE2  1 
ATOM   1139 H  HE2  B TYR   A 1 42  ? 30.336 5.073   -9.492  0.50 17.37 ?  42  TYR   A HE2  1 
ATOM   1140 H  HH   A TYR   A 1 42  ? 33.597 4.468   -10.714 0.50 18.52 ?  42  TYR   A HH   1 
ATOM   1141 H  HH   B TYR   A 1 42  ? 33.354 4.607   -10.914 0.50 18.79 ?  42  TYR   A HH   1 
ATOM   1142 N  N    A LEU   A 1 43  ? 31.285 4.257   -1.961  0.50 10.17 ?  43  LEU   A N    1 
ATOM   1143 N  N    B LEU   A 1 43  ? 31.123 4.218   -2.185  0.50 10.72 ?  43  LEU   A N    1 
ATOM   1144 C  CA   A LEU   A 1 43  ? 30.828 4.577   -0.609  0.50 9.87  ?  43  LEU   A CA   1 
ATOM   1145 C  CA   B LEU   A 1 43  ? 30.703 4.558   -0.826  0.50 10.41 ?  43  LEU   A CA   1 
ATOM   1146 C  C    A LEU   A 1 43  ? 30.319 6.015   -0.503  0.50 10.29 ?  43  LEU   A C    1 
ATOM   1147 C  C    B LEU   A 1 43  ? 30.246 6.011   -0.730  0.50 10.51 ?  43  LEU   A C    1 
ATOM   1148 O  O    A LEU   A 1 43  ? 30.515 6.691   0.511   0.50 10.69 ?  43  LEU   A O    1 
ATOM   1149 O  O    B LEU   A 1 43  ? 30.609 6.737   0.197   0.50 10.97 ?  43  LEU   A O    1 
ATOM   1150 C  CB   A LEU   A 1 43  ? 31.889 4.272   0.449   0.50 10.47 ?  43  LEU   A CB   1 
ATOM   1151 C  CB   B LEU   A 1 43  ? 31.776 4.248   0.218   0.50 10.48 ?  43  LEU   A CB   1 
ATOM   1152 C  CG   A LEU   A 1 43  ? 32.413 2.834   0.491   0.50 10.88 ?  43  LEU   A CG   1 
ATOM   1153 C  CG   B LEU   A 1 43  ? 32.240 2.797   0.346   0.50 10.60 ?  43  LEU   A CG   1 
ATOM   1154 C  CD1  A LEU   A 1 43  ? 33.513 2.715   1.533   0.50 11.64 ?  43  LEU   A CD1  1 
ATOM   1155 C  CD1  B LEU   A 1 43  ? 33.259 2.679   1.474   0.50 11.83 ?  43  LEU   A CD1  1 
ATOM   1156 C  CD2  A LEU   A 1 43  ? 31.302 1.831   0.771   0.50 11.12 ?  43  LEU   A CD2  1 
ATOM   1157 C  CD2  B LEU   A 1 43  ? 31.074 1.836   0.563   0.50 10.59 ?  43  LEU   A CD2  1 
ATOM   1158 H  H    A LEU   A 1 43  ? 30.940 3.531   -2.275  0.50 12.24 ?  43  LEU   A H    1 
ATOM   1159 H  H    B LEU   A 1 43  ? 30.791 3.479   -2.464  0.50 12.90 ?  43  LEU   A H    1 
ATOM   1160 H  HA   A LEU   A 1 43  ? 30.071 4.007   -0.417  0.50 11.87 ?  43  LEU   A HA   1 
ATOM   1161 H  HA   B LEU   A 1 43  ? 29.931 4.007   -0.607  0.50 12.52 ?  43  LEU   A HA   1 
ATOM   1162 H  HB2  A LEU   A 1 43  ? 32.651 4.854   0.300   0.50 12.59 ?  43  LEU   A HB2  1 
ATOM   1163 H  HB2  B LEU   A 1 43  ? 32.555 4.783   0.010   0.50 12.61 ?  43  LEU   A HB2  1 
ATOM   1164 H  HB3  A LEU   A 1 43  ? 31.504 4.460   1.320   0.50 12.59 ?  43  LEU   A HB3  1 
ATOM   1165 H  HB3  B LEU   A 1 43  ? 31.432 4.514   1.089   0.50 12.61 ?  43  LEU   A HB3  1 
ATOM   1166 H  HG   A LEU   A 1 43  ? 32.799 2.615   -0.371  0.50 13.09 ?  43  LEU   A HG   1 
ATOM   1167 H  HG   B LEU   A 1 43  ? 32.684 2.543   -0.476  0.50 12.76 ?  43  LEU   A HG   1 
ATOM   1168 H  HD11 A LEU   A 1 43  ? 33.835 1.799   1.548   0.50 14.01 ?  43  LEU   A HD11 1 
ATOM   1169 H  HD11 B LEU   A 1 43  ? 33.547 1.754   1.543   0.50 14.23 ?  43  LEU   A HD11 1 
ATOM   1170 H  HD12 A LEU   A 1 43  ? 34.235 3.316   1.299   0.50 14.01 ?  43  LEU   A HD12 1 
ATOM   1171 H  HD12 B LEU   A 1 43  ? 34.019 3.248   1.278   0.50 14.23 ?  43  LEU   A HD12 1 
ATOM   1172 H  HD13 A LEU   A 1 43  ? 33.151 2.952   2.401   0.50 14.01 ?  43  LEU   A HD13 1 
ATOM   1173 H  HD13 B LEU   A 1 43  ? 32.844 2.957   2.307   0.50 14.23 ?  43  LEU   A HD13 1 
ATOM   1174 H  HD21 A LEU   A 1 43  ? 31.693 0.950   0.872   0.50 13.38 ?  43  LEU   A HD21 1 
ATOM   1175 H  HD21 B LEU   A 1 43  ? 31.427 0.952   0.749   0.50 12.74 ?  43  LEU   A HD21 1 
ATOM   1176 H  HD22 A LEU   A 1 43  ? 30.847 2.089   1.588   0.50 13.38 ?  43  LEU   A HD22 1 
ATOM   1177 H  HD22 B LEU   A 1 43  ? 30.546 2.147   1.315   0.50 12.74 ?  43  LEU   A HD22 1 
ATOM   1178 H  HD23 A LEU   A 1 43  ? 30.681 1.837   0.028   0.50 13.38 ?  43  LEU   A HD23 1 
ATOM   1179 H  HD23 B LEU   A 1 43  ? 30.531 1.816   -0.238  0.50 12.74 ?  43  LEU   A HD23 1 
ATOM   1180 N  N    A LYS   A 1 44  ? 29.647 6.484   -1.559  0.50 10.42 ?  44  LYS   A N    1 
ATOM   1181 N  N    B LYS   A 1 44  ? 29.446 6.442   -1.708  0.50 10.21 ?  44  LYS   A N    1 
ATOM   1182 C  CA   A LYS   A 1 44  ? 28.991 7.791   -1.554  0.50 11.05 ?  44  LYS   A CA   1 
ATOM   1183 C  CA   B LYS   A 1 44  ? 28.803 7.756   -1.693  0.50 10.66 ?  44  LYS   A CA   1 
ATOM   1184 C  C    A LYS   A 1 44  ? 27.556 7.587   -1.087  0.50 10.30 ?  44  LYS   A C    1 
ATOM   1185 C  C    B LYS   A 1 44  ? 27.393 7.569   -1.138  0.50 10.13 ?  44  LYS   A C    1 
ATOM   1186 O  O    A LYS   A 1 44  ? 26.719 7.048   -1.821  0.50 11.38 ?  44  LYS   A O    1 
ATOM   1187 O  O    B LYS   A 1 44  ? 26.489 7.105   -1.839  0.50 10.82 ?  44  LYS   A O    1 
ATOM   1188 C  CB   A LYS   A 1 44  ? 29.043 8.438   -2.935  0.50 12.85 ?  44  LYS   A CB   1 
ATOM   1189 C  CB   B LYS   A 1 44  ? 28.791 8.367   -3.090  0.50 13.06 ?  44  LYS   A CB   1 
ATOM   1190 C  CG   A LYS   A 1 44  ? 30.440 8.840   -3.379  0.50 15.40 ?  44  LYS   A CG   1 
ATOM   1191 C  CG   B LYS   A 1 44  ? 30.135 8.920   -3.539  0.50 16.47 ?  44  LYS   A CG   1 
ATOM   1192 C  CD   A LYS   A 1 44  ? 31.131 9.754   -2.374  0.50 19.47 ?  44  LYS   A CD   1 
ATOM   1193 C  CD   B LYS   A 1 44  ? 30.787 9.761   -2.445  0.50 21.10 ?  44  LYS   A CD   1 
ATOM   1194 C  CE   A LYS   A 1 44  ? 32.460 10.251  -2.904  0.50 21.57 ?  44  LYS   A CE   1 
ATOM   1195 C  CE   B LYS   A 1 44  ? 31.892 10.652  -2.988  0.50 23.49 ?  44  LYS   A CE   1 
ATOM   1196 N  NZ   A LYS   A 1 44  ? 33.278 10.865  -1.831  0.50 22.42 ?  44  LYS   A NZ   1 
ATOM   1197 N  NZ   B LYS   A 1 44  ? 32.533 11.451  -1.905  0.50 25.07 ?  44  LYS   A NZ   1 
ATOM   1198 H  H    A LYS   A 1 44  ? 29.565 6.059   -2.306  0.50 12.54 ?  44  LYS   A H    1 
ATOM   1199 H  H    B LYS   A 1 44  ? 29.269 5.983   -2.418  0.50 12.28 ?  44  LYS   A H    1 
ATOM   1200 H  HA   A LYS   A 1 44  ? 29.435 8.372   -0.916  0.50 13.29 ?  44  LYS   A HA   1 
ATOM   1201 H  HA   B LYS   A 1 44  ? 29.278 8.340   -1.084  0.50 12.83 ?  44  LYS   A HA   1 
ATOM   1202 H  HB2  A LYS   A 1 44  ? 28.692 7.816   -3.588  0.50 15.46 ?  44  LYS   A HB2  1 
ATOM   1203 H  HB2  B LYS   A 1 44  ? 28.525 7.688   -3.730  0.50 15.70 ?  44  LYS   A HB2  1 
ATOM   1204 H  HB3  A LYS   A 1 44  ? 28.498 9.244   -2.922  0.50 15.46 ?  44  LYS   A HB3  1 
ATOM   1205 H  HB3  B LYS   A 1 44  ? 28.153 9.100   -3.109  0.50 15.70 ?  44  LYS   A HB3  1 
ATOM   1206 H  HG2  A LYS   A 1 44  ? 30.982 8.042   -3.482  0.50 18.52 ?  44  LYS   A HG2  1 
ATOM   1207 H  HG2  B LYS   A 1 44  ? 30.729 8.184   -3.757  0.50 19.80 ?  44  LYS   A HG2  1 
ATOM   1208 H  HG3  A LYS   A 1 44  ? 30.382 9.314   -4.225  0.50 18.52 ?  44  LYS   A HG3  1 
ATOM   1209 H  HG3  B LYS   A 1 44  ? 30.008 9.488   -4.318  0.50 19.80 ?  44  LYS   A HG3  1 
ATOM   1210 H  HD2  A LYS   A 1 44  ? 30.556 10.517  -2.195  0.50 23.39 ?  44  LYS   A HD2  1 
ATOM   1211 H  HD2  B LYS   A 1 44  ? 30.113 10.318  -2.027  0.50 25.36 ?  44  LYS   A HD2  1 
ATOM   1212 H  HD3  A LYS   A 1 44  ? 31.295 9.259   -1.555  0.50 23.39 ?  44  LYS   A HD3  1 
ATOM   1213 H  HD3  B LYS   A 1 44  ? 31.182 9.162   -1.784  0.50 25.36 ?  44  LYS   A HD3  1 
ATOM   1214 H  HE2  A LYS   A 1 44  ? 32.952 9.502   -3.274  0.50 25.92 ?  44  LYS   A HE2  1 
ATOM   1215 H  HE2  B LYS   A 1 44  ? 32.574 10.099  -3.404  0.50 28.22 ?  44  LYS   A HE2  1 
ATOM   1216 H  HE3  A LYS   A 1 44  ? 32.298 10.918  -3.588  0.50 25.92 ?  44  LYS   A HE3  1 
ATOM   1217 H  HE3  B LYS   A 1 44  ? 31.515 11.265  -3.637  0.50 28.22 ?  44  LYS   A HE3  1 
ATOM   1218 H  HZ1  A LYS   A 1 44  ? 34.061 11.128  -2.161  0.50 26.94 ?  44  LYS   A HZ1  1 
ATOM   1219 H  HZ1  B LYS   A 1 44  ? 33.175 11.964  -2.246  0.50 30.12 ?  44  LYS   A HZ1  1 
ATOM   1220 H  HZ2  A LYS   A 1 44  ? 32.855 11.574  -1.494  0.50 26.94 ?  44  LYS   A HZ2  1 
ATOM   1221 H  HZ2  B LYS   A 1 44  ? 31.928 11.968  -1.510  0.50 30.12 ?  44  LYS   A HZ2  1 
ATOM   1222 H  HZ3  A LYS   A 1 44  ? 33.420 10.277  -1.180  0.50 26.94 ?  44  LYS   A HZ3  1 
ATOM   1223 H  HZ3  B LYS   A 1 44  ? 32.891 10.907  -1.297  0.50 30.12 ?  44  LYS   A HZ3  1 
ATOM   1224 N  N    A HIS   A 1 45  ? 27.282 7.995   0.144   0.50 9.97  ?  45  HIS   A N    1 
ATOM   1225 N  N    B HIS   A 1 45  ? 27.217 7.910   0.138   0.50 10.65 ?  45  HIS   A N    1 
ATOM   1226 C  CA   A HIS   A 1 45  ? 26.053 7.606   0.828   0.50 9.96  ?  45  HIS   A CA   1 
ATOM   1227 C  CA   B HIS   A 1 45  ? 25.975 7.627   0.861   0.50 11.06 ?  45  HIS   A CA   1 
ATOM   1228 C  C    A HIS   A 1 45  ? 25.000 8.708   0.688   0.50 10.28 ?  45  HIS   A C    1 
ATOM   1229 C  C    B HIS   A 1 45  ? 24.995 8.783   0.672   0.50 11.80 ?  45  HIS   A C    1 
ATOM   1230 O  O    A HIS   A 1 45  ? 24.590 9.353   1.654   0.50 10.37 ?  45  HIS   A O    1 
ATOM   1231 O  O    B HIS   A 1 45  ? 24.849 9.661   1.524   0.50 12.70 ?  45  HIS   A O    1 
ATOM   1232 C  CB   A HIS   A 1 45  ? 26.357 7.296   2.285   0.50 9.92  ?  45  HIS   A CB   1 
ATOM   1233 C  CB   B HIS   A 1 45  ? 26.273 7.416   2.336   0.50 10.75 ?  45  HIS   A CB   1 
ATOM   1234 C  CG   A HIS   A 1 45  ? 27.472 6.314   2.472   0.50 9.10  ?  45  HIS   A CG   1 
ATOM   1235 C  CG   B HIS   A 1 45  ? 27.405 6.474   2.595   0.50 10.15 ?  45  HIS   A CG   1 
ATOM   1236 N  ND1  A HIS   A 1 45  ? 27.442 5.037   1.948   0.50 9.22  ?  45  HIS   A ND1  1 
ATOM   1237 N  ND1  B HIS   A 1 45  ? 27.418 5.177   2.129   0.50 10.84 ?  45  HIS   A ND1  1 
ATOM   1238 C  CD2  A HIS   A 1 45  ? 28.653 6.430   3.123   0.50 9.85  ?  45  HIS   A CD2  1 
ATOM   1239 C  CD2  B HIS   A 1 45  ? 28.565 6.650   3.270   0.50 9.66  ?  45  HIS   A CD2  1 
ATOM   1240 C  CE1  A HIS   A 1 45  ? 28.559 4.410   2.275   0.50 9.67  ?  45  HIS   A CE1  1 
ATOM   1241 C  CE1  B HIS   A 1 45  ? 28.542 4.594   2.508   0.50 9.76  ?  45  HIS   A CE1  1 
ATOM   1242 N  NE2  A HIS   A 1 45  ? 29.313 5.233   2.985   0.50 9.90  ?  45  HIS   A NE2  1 
ATOM   1243 N  NE2  B HIS   A 1 45  ? 29.257 5.466   3.198   0.50 9.41  ?  45  HIS   A NE2  1 
ATOM   1244 H  H    A HIS   A 1 45  ? 27.793 8.510   0.609   0.50 12.00 ?  45  HIS   A H    1 
ATOM   1245 H  H    B HIS   A 1 45  ? 27.811 8.308   0.616   0.50 12.82 ?  45  HIS   A H    1 
ATOM   1246 H  HA   A HIS   A 1 45  ? 25.703 6.802   0.417   0.50 11.99 ?  45  HIS   A HA   1 
ATOM   1247 H  HA   B HIS   A 1 45  ? 25.573 6.818   0.505   0.50 13.31 ?  45  HIS   A HA   1 
ATOM   1248 H  HB2  A HIS   A 1 45  ? 26.607 8.113   2.739   0.50 11.94 ?  45  HIS   A HB2  1 
ATOM   1249 H  HB2  B HIS   A 1 45  ? 26.498 8.271   2.734   0.50 12.93 ?  45  HIS   A HB2  1 
ATOM   1250 H  HB3  A HIS   A 1 45  ? 25.563 6.918   2.698   0.50 11.94 ?  45  HIS   A HB3  1 
ATOM   1251 H  HB3  B HIS   A 1 45  ? 25.481 7.052   2.763   0.50 12.93 ?  45  HIS   A HB3  1 
ATOM   1252 H  HD2  A HIS   A 1 45  ? 28.967 7.182   3.575   0.50 11.85 ?  45  HIS   A HD2  1 
ATOM   1253 H  HD2  B HIS   A 1 45  ? 28.847 7.430   3.696   0.50 11.62 ?  45  HIS   A HD2  1 
ATOM   1254 H  HE1  A HIS   A 1 45  ? 28.784 3.531   2.054   0.50 11.63 ?  45  HIS   A HE1  1 
ATOM   1255 H  HE1  B HIS   A 1 45  ? 28.785 3.719   2.319   0.50 11.74 ?  45  HIS   A HE1  1 
ATOM   1256 H  HE2  A HIS   A 1 45  ? 30.091 5.048   3.315   0.50 11.92 ?  45  HIS   A HE2  1 
ATOM   1257 H  HE2  B HIS   A 1 45  ? 30.026 5.313   3.549   0.50 11.33 ?  45  HIS   A HE2  1 
ATOM   1258 N  N    A GLY   A 1 46  ? 24.555 8.907   -0.552  0.50 10.99 ?  46  GLY   A N    1 
ATOM   1259 N  N    B GLY   A 1 46  ? 24.294 8.771   -0.459  0.50 11.84 ?  46  GLY   A N    1 
ATOM   1260 C  CA   A GLY   A 1 46  ? 23.760 10.075  -0.892  0.50 11.58 ?  46  GLY   A CA   1 
ATOM   1261 C  CA   B GLY   A 1 46  ? 23.454 9.907   -0.796  0.50 12.16 ?  46  GLY   A CA   1 
ATOM   1262 C  C    A GLY   A 1 46  ? 22.261 9.955   -0.681  0.50 11.27 ?  46  GLY   A C    1 
ATOM   1263 C  C    B GLY   A 1 46  ? 21.993 9.785   -0.407  0.50 11.79 ?  46  GLY   A C    1 
ATOM   1264 O  O    A GLY   A 1 46  ? 21.585 10.959  -0.432  0.50 11.59 ?  46  GLY   A O    1 
ATOM   1265 O  O    B GLY   A 1 46  ? 21.377 10.762  0.032   0.50 12.05 ?  46  GLY   A O    1 
ATOM   1266 H  H    A GLY   A 1 46  ? 24.705 8.375   -1.210  0.50 13.22 ?  46  GLY   A H    1 
ATOM   1267 H  H    B GLY   A 1 46  ? 24.293 8.131   -1.039  0.50 14.24 ?  46  GLY   A H    1 
ATOM   1268 H  HA2  A GLY   A 1 46  ? 24.082 10.827  -0.368  0.50 13.93 ?  46  GLY   A HA2  1 
ATOM   1269 H  HA2  B GLY   A 1 46  ? 23.806 10.697  -0.356  0.50 14.63 ?  46  GLY   A HA2  1 
ATOM   1270 H  HA3  A GLY   A 1 46  ? 23.911 10.283  -1.828  0.50 13.93 ?  46  GLY   A HA3  1 
ATOM   1271 H  HA3  B GLY   A 1 46  ? 23.503 10.055  -1.751  0.50 14.63 ?  46  GLY   A HA3  1 
ATOM   1272 N  N    A GLY   A 1 47  ? 21.727 8.745   -0.797  0.50 10.99 ?  47  GLY   A N    1 
ATOM   1273 N  N    B GLY   A 1 47  ? 21.419 8.596   -0.569  0.50 12.05 ?  47  GLY   A N    1 
ATOM   1274 C  CA   A GLY   A 1 47  ? 20.292 8.544   -0.751  0.50 11.34 ?  47  GLY   A CA   1 
ATOM   1275 C  CA   B GLY   A 1 47  ? 19.992 8.419   -0.378  0.50 11.80 ?  47  GLY   A CA   1 
ATOM   1276 C  C    A GLY   A 1 47  ? 19.967 7.102   -0.428  0.50 10.74 ?  47  GLY   A C    1 
ATOM   1277 C  C    B GLY   A 1 47  ? 19.671 6.982   -0.037  0.50 10.51 ?  47  GLY   A C    1 
ATOM   1278 O  O    A GLY   A 1 47  ? 20.854 6.273   -0.216  0.50 10.99 ?  47  GLY   A O    1 
ATOM   1279 O  O    B GLY   A 1 47  ? 20.561 6.142   0.112   0.50 10.42 ?  47  GLY   A O    1 
ATOM   1280 H  H    A GLY   A 1 47  ? 22.182 8.025   -0.892  0.50 13.22 ?  47  GLY   A H    1 
ATOM   1281 H  H    B GLY   A 1 47  ? 21.841 7.874   -0.778  0.50 14.49 ?  47  GLY   A H    1 
ATOM   1282 H  HA2  A GLY   A 1 47  ? 19.898 9.126   -0.079  0.50 13.64 ?  47  GLY   A HA2  1 
ATOM   1283 H  HA2  B GLY   A 1 47  ? 19.685 8.973   0.351   0.50 14.19 ?  47  GLY   A HA2  1 
ATOM   1284 H  HA3  A GLY   A 1 47  ? 19.909 8.759   -1.614  0.50 13.64 ?  47  GLY   A HA3  1 
ATOM   1285 H  HA3  B GLY   A 1 47  ? 19.519 8.674   -1.188  0.50 14.19 ?  47  GLY   A HA3  1 
ATOM   1286 N  N    A GLY   A 1 48  ? 18.673 6.797   -0.416  0.50 10.47 ?  48  GLY   A N    1 
ATOM   1287 N  N    B GLY   A 1 48  ? 18.373 6.705   0.086   0.50 10.63 ?  48  GLY   A N    1 
ATOM   1288 C  CA   A GLY   A 1 48  ? 18.259 5.461   -0.046  0.50 10.65 ?  48  GLY   A CA   1 
ATOM   1289 C  CA   B GLY   A 1 48  ? 17.944 5.382   0.490   0.50 10.19 ?  48  GLY   A CA   1 
ATOM   1290 C  C    A GLY   A 1 48  ? 18.670 5.130   1.375   0.50 10.46 ?  48  GLY   A C    1 
ATOM   1291 C  C    B GLY   A 1 48  ? 18.529 5.002   1.839   0.50 10.30 ?  48  GLY   A C    1 
ATOM   1292 O  O    A GLY   A 1 48  ? 18.836 6.013   2.228   0.50 10.67 ?  48  GLY   A O    1 
ATOM   1293 O  O    B GLY   A 1 48  ? 18.731 5.840   2.731   0.50 10.54 ?  48  GLY   A O    1 
ATOM   1294 H  H    A GLY   A 1 48  ? 18.041 7.335   -0.613  0.50 12.59 ?  48  GLY   A H    1 
ATOM   1295 H  H    B GLY   A 1 48  ? 17.724 7.265   -0.055  0.50 12.79 ?  48  GLY   A H    1 
ATOM   1296 H  HA2  A GLY   A 1 48  ? 17.300 5.383   -0.116  0.50 12.81 ?  48  GLY   A HA2  1 
ATOM   1297 H  HA2  B GLY   A 1 48  ? 16.972 5.351   0.541   0.50 12.26 ?  48  GLY   A HA2  1 
ATOM   1298 H  HA3  A GLY   A 1 48  ? 18.675 4.812   -0.633  0.50 12.81 ?  48  GLY   A HA3  1 
ATOM   1299 H  HA3  B GLY   A 1 48  ? 18.233 4.728   -0.170  0.50 12.26 ?  48  GLY   A HA3  1 
ATOM   1300 N  N    A VAL   A 1 49  ? 18.854 3.832   1.633   0.50 11.08 ?  49  VAL   A N    1 
ATOM   1301 N  N    B VAL   A 1 49  ? 18.794 3.703   1.991   0.50 10.06 ?  49  VAL   A N    1 
ATOM   1302 C  CA   A VAL   A 1 49  ? 19.284 3.389   2.957   0.50 11.20 ?  49  VAL   A CA   1 
ATOM   1303 C  CA   B VAL   A 1 49  ? 19.413 3.185   3.209   0.50 10.40 ?  49  VAL   A CA   1 
ATOM   1304 C  C    A VAL   A 1 49  ? 20.603 4.048   3.350   0.50 10.42 ?  49  VAL   A C    1 
ATOM   1305 C  C    B VAL   A 1 49  ? 20.700 3.939   3.526   0.50 9.87  ?  49  VAL   A C    1 
ATOM   1306 O  O    A VAL   A 1 49  ? 20.766 4.493   4.491   0.50 11.15 ?  49  VAL   A O    1 
ATOM   1307 O  O    B VAL   A 1 49  ? 20.934 4.345   4.670   0.50 9.63  ?  49  VAL   A O    1 
ATOM   1308 C  CB   A VAL   A 1 49  ? 19.366 1.849   3.014   0.50 12.00 ?  49  VAL   A CB   1 
ATOM   1309 C  CB   B VAL   A 1 49  ? 19.677 1.675   3.063   0.50 10.83 ?  49  VAL   A CB   1 
ATOM   1310 C  CG1  A VAL   A 1 49  ? 20.098 1.391   4.274   0.50 12.45 ?  49  VAL   A CG1  1 
ATOM   1311 C  CG1  B VAL   A 1 49  ? 20.542 1.181   4.210   0.50 10.72 ?  49  VAL   A CG1  1 
ATOM   1312 C  CG2  A VAL   A 1 49  ? 17.973 1.239   2.966   0.50 13.31 ?  49  VAL   A CG2  1 
ATOM   1313 C  CG2  B VAL   A 1 49  ? 18.367 0.898   2.986   0.50 11.77 ?  49  VAL   A CG2  1 
ATOM   1314 H  H    A VAL   A 1 49  ? 18.743 3.195   1.068   0.50 13.33 ?  49  VAL   A H    1 
ATOM   1315 H  H    B VAL   A 1 49  ? 18.619 3.104   1.401   0.50 12.11 ?  49  VAL   A H    1 
ATOM   1316 H  HA   A VAL   A 1 49  ? 18.622 3.659   3.611   0.50 13.47 ?  49  VAL   A HA   1 
ATOM   1317 H  HA   B VAL   A 1 49  ? 18.802 3.310   3.950   0.50 12.51 ?  49  VAL   A HA   1 
ATOM   1318 H  HB   A VAL   A 1 49  ? 19.864 1.522   2.249   0.50 14.43 ?  49  VAL   A HB   1 
ATOM   1319 H  HB   B VAL   A 1 49  ? 20.160 1.519   2.236   0.50 13.03 ?  49  VAL   A HB   1 
ATOM   1320 H  HG11 A VAL   A 1 49  ? 19.898 0.454   4.434   0.50 14.97 ?  49  VAL   A HG11 1 
ATOM   1321 H  HG11 B VAL   A 1 49  ? 20.453 0.217   4.278   0.50 12.90 ?  49  VAL   A HG11 1 
ATOM   1322 H  HG12 A VAL   A 1 49  ? 21.052 1.506   4.151   0.50 14.97 ?  49  VAL   A HG12 1 
ATOM   1323 H  HG12 B VAL   A 1 49  ? 21.468 1.412   4.034   0.50 12.90 ?  49  VAL   A HG12 1 
ATOM   1324 H  HG13 A VAL   A 1 49  ? 19.791 1.922   5.027   0.50 14.97 ?  49  VAL   A HG13 1 
ATOM   1325 H  HG13 B VAL   A 1 49  ? 20.245 1.597   5.033   0.50 12.90 ?  49  VAL   A HG13 1 
ATOM   1326 H  HG21 A VAL   A 1 49  ? 18.050 0.271   2.993   0.50 16.00 ?  49  VAL   A HG21 1 
ATOM   1327 H  HG21 B VAL   A 1 49  ? 18.562 -0.046  2.871   0.50 14.16 ?  49  VAL   A HG21 1 
ATOM   1328 H  HG22 A VAL   A 1 49  ? 17.468 1.551   3.733   0.50 16.00 ?  49  VAL   A HG22 1 
ATOM   1329 H  HG22 B VAL   A 1 49  ? 17.868 1.032   3.809   0.50 14.16 ?  49  VAL   A HG22 1 
ATOM   1330 H  HG23 A VAL   A 1 49  ? 17.540 1.515   2.146   0.50 16.00 ?  49  VAL   A HG23 1 
ATOM   1331 H  HG23 B VAL   A 1 49  ? 17.847 1.220   2.231   0.50 14.16 ?  49  VAL   A HG23 1 
ATOM   1332 N  N    A ALA   A 1 50  ? 21.566 4.106   2.424   0.50 9.97  ?  50  ALA   A N    1 
ATOM   1333 N  N    B ALA   A 1 50  ? 21.573 4.087   2.526   0.50 9.57  ?  50  ALA   A N    1 
ATOM   1334 C  CA   A ALA   A 1 50  ? 22.878 4.655   2.760   0.50 9.97  ?  50  ALA   A CA   1 
ATOM   1335 C  CA   B ALA   A 1 50  ? 22.891 4.664   2.771   0.50 9.73  ?  50  ALA   A CA   1 
ATOM   1336 C  C    A ALA   A 1 50  ? 22.783 6.111   3.198   0.50 10.03 ?  50  ALA   A C    1 
ATOM   1337 C  C    B ALA   A 1 50  ? 22.786 6.120   3.205   0.50 9.73  ?  50  ALA   A C    1 
ATOM   1338 O  O    A ALA   A 1 50  ? 23.426 6.519   4.174   0.50 10.55 ?  50  ALA   A O    1 
ATOM   1339 O  O    B ALA   A 1 50  ? 23.425 6.538   4.180   0.50 10.07 ?  50  ALA   A O    1 
ATOM   1340 C  CB   A ALA   A 1 50  ? 23.823 4.517   1.568   0.50 10.26 ?  50  ALA   A CB   1 
ATOM   1341 C  CB   B ALA   A 1 50  ? 23.752 4.543   1.516   0.50 10.01 ?  50  ALA   A CB   1 
ATOM   1342 H  H    A ALA   A 1 50  ? 21.481 3.846   1.610   0.50 12.00 ?  50  ALA   A H    1 
ATOM   1343 H  H    B ALA   A 1 50  ? 21.423 3.870   1.705   0.50 11.52 ?  50  ALA   A H    1 
ATOM   1344 H  HA   A ALA   A 1 50  ? 23.252 4.158   3.497   0.50 12.00 ?  50  ALA   A HA   1 
ATOM   1345 H  HA   B ALA   A 1 50  ? 23.323 4.174   3.482   0.50 11.70 ?  50  ALA   A HA   1 
ATOM   1346 H  HB1  A ALA   A 1 50  ? 24.688 4.888   1.805   0.50 12.34 ?  50  ALA   A HB1  1 
ATOM   1347 H  HB1  B ALA   A 1 50  ? 24.625 4.929   1.693   0.50 12.05 ?  50  ALA   A HB1  1 
ATOM   1348 H  HB2  A ALA   A 1 50  ? 23.915 3.578   1.345   0.50 12.34 ?  50  ALA   A HB2  1 
ATOM   1349 H  HB2  B ALA   A 1 50  ? 23.847 3.604   1.289   0.50 12.05 ?  50  ALA   A HB2  1 
ATOM   1350 H  HB3  A ALA   A 1 50  ? 23.454 5.001   0.811   0.50 12.34 ?  50  ALA   A HB3  1 
ATOM   1351 H  HB3  B ALA   A 1 50  ? 23.322 5.017   0.787   0.50 12.05 ?  50  ALA   A HB3  1 
ATOM   1352 N  N    . GLY   A 1 51  ? 21.998 6.916   2.481   1.00 10.29 ?  51  GLY   A N    1 
ATOM   1353 C  CA   . GLY   A 1 51  ? 21.847 8.306   2.865   1.00 10.73 ?  51  GLY   A CA   1 
ATOM   1354 C  C    . GLY   A 1 51  ? 21.241 8.450   4.245   1.00 10.76 ?  51  GLY   A C    1 
ATOM   1355 O  O    . GLY   A 1 51  ? 21.622 9.338   5.013   1.00 11.33 ?  51  GLY   A O    1 
ATOM   1356 H  H    A GLY   A 1 51  ? 21.553 6.685   1.780   0.50 12.39 ?  51  GLY   A H    1 
ATOM   1357 H  H    B GLY   A 1 51  ? 21.555 6.682   1.780   0.50 12.39 ?  51  GLY   A H    1 
ATOM   1358 H  HA2  . GLY   A 1 51  ? 22.708 8.744   2.867   1.00 12.91 ?  51  GLY   A HA2  1 
ATOM   1359 H  HA3  . GLY   A 1 51  ? 21.270 8.762   2.225   1.00 12.91 ?  51  GLY   A HA3  1 
ATOM   1360 N  N    . ALA   A 1 52  ? 20.282 7.579   4.575   1.00 10.80 ?  52  ALA   A N    1 
ATOM   1361 C  CA   . ALA   A 1 52  ? 19.629 7.627   5.880   1.00 11.55 ?  52  ALA   A CA   1 
ATOM   1362 C  C    . ALA   A 1 52  ? 20.583 7.214   7.001   1.00 11.03 ?  52  ALA   A C    1 
ATOM   1363 O  O    . ALA   A 1 52  ? 20.649 7.873   8.045   1.00 11.74 ?  52  ALA   A O    1 
ATOM   1364 C  CB   . ALA   A 1 52  ? 18.374 6.749   5.863   1.00 13.03 ?  52  ALA   A CB   1 
ATOM   1365 H  H    . ALA   A 1 52  ? 20.010 6.932   4.068   1.00 12.99 ?  52  ALA   A H    1 
ATOM   1366 H  HA   . ALA   A 1 52  ? 19.351 8.534   6.052   1.00 13.90 ?  52  ALA   A HA   1 
ATOM   1367 H  HB1  . ALA   A 1 52  ? 17.931 6.811   6.728   1.00 15.67 ?  52  ALA   A HB1  1 
ATOM   1368 H  HB2  . ALA   A 1 52  ? 17.774 7.068   5.169   1.00 15.67 ?  52  ALA   A HB2  1 
ATOM   1369 H  HB3  . ALA   A 1 52  ? 18.623 5.830   5.687   1.00 15.67 ?  52  ALA   A HB3  1 
ATOM   1370 N  N    A LEU   A 1 53  ? 21.323 6.117   6.806   0.50 10.97 ?  53  LEU   A N    1 
ATOM   1371 N  N    B LEU   A 1 53  ? 21.325 6.116   6.813   0.50 10.60 ?  53  LEU   A N    1 
ATOM   1372 C  CA   A LEU   A 1 53  ? 22.284 5.690   7.820   0.50 11.18 ?  53  LEU   A CA   1 
ATOM   1373 C  CA   B LEU   A 1 53  ? 22.316 5.725   7.815   0.50 10.39 ?  53  LEU   A CA   1 
ATOM   1374 C  C    A LEU   A 1 53  ? 23.363 6.742   8.015   0.50 10.81 ?  53  LEU   A C    1 
ATOM   1375 C  C    B LEU   A 1 53  ? 23.335 6.836   8.019   0.50 10.02 ?  53  LEU   A C    1 
ATOM   1376 O  O    A LEU   A 1 53  ? 23.768 7.029   9.146   0.50 11.40 ?  53  LEU   A O    1 
ATOM   1377 O  O    B LEU   A 1 53  ? 23.599 7.255   9.151   0.50 10.35 ?  53  LEU   A O    1 
ATOM   1378 C  CB   A LEU   A 1 53  ? 22.914 4.350   7.429   0.50 11.74 ?  53  LEU   A CB   1 
ATOM   1379 C  CB   B LEU   A 1 53  ? 23.021 4.422   7.415   0.50 10.40 ?  53  LEU   A CB   1 
ATOM   1380 C  CG   A LEU   A 1 53  ? 21.971 3.142   7.434   0.50 12.24 ?  53  LEU   A CG   1 
ATOM   1381 C  CG   B LEU   A 1 53  ? 22.261 3.092   7.557   0.50 10.74 ?  53  LEU   A CG   1 
ATOM   1382 C  CD1  A LEU   A 1 53  ? 22.680 1.917   6.882   0.50 12.22 ?  53  LEU   A CD1  1 
ATOM   1383 C  CD1  B LEU   A 1 53  ? 23.035 1.971   6.876   0.50 11.36 ?  53  LEU   A CD1  1 
ATOM   1384 C  CD2  A LEU   A 1 53  ? 21.442 2.876   8.836   0.50 12.83 ?  53  LEU   A CD2  1 
ATOM   1385 C  CD2  B LEU   A 1 53  ? 21.991 2.729   9.015   0.50 10.87 ?  53  LEU   A CD2  1 
ATOM   1386 H  H    A LEU   A 1 53  ? 21.288 5.612   6.108   0.50 13.20 ?  53  LEU   A H    1 
ATOM   1387 H  H    B LEU   A 1 53  ? 21.269 5.588   6.132   0.50 12.76 ?  53  LEU   A H    1 
ATOM   1388 H  HA   A LEU   A 1 53  ? 21.823 5.569   8.664   0.50 13.44 ?  53  LEU   A HA   1 
ATOM   1389 H  HA   B LEU   A 1 53  ? 21.863 5.572   8.658   0.50 12.50 ?  53  LEU   A HA   1 
ATOM   1390 H  HB2  A LEU   A 1 53  ? 23.277 4.429   6.532   0.50 14.12 ?  53  LEU   A HB2  1 
ATOM   1391 H  HB2  B LEU   A 1 53  ? 23.277 4.496   6.484   0.50 12.51 ?  53  LEU   A HB2  1 
ATOM   1392 H  HB3  A LEU   A 1 53  ? 23.634 4.154   8.050   0.50 14.12 ?  53  LEU   A HB3  1 
ATOM   1393 H  HB3  B LEU   A 1 53  ? 23.820 4.341   7.957   0.50 12.51 ?  53  LEU   A HB3  1 
ATOM   1394 H  HG   A LEU   A 1 53  ? 21.213 3.333   6.857   0.50 14.72 ?  53  LEU   A HG   1 
ATOM   1395 H  HG   B LEU   A 1 53  ? 21.406 3.170   7.107   0.50 12.92 ?  53  LEU   A HG   1 
ATOM   1396 H  HD11 A LEU   A 1 53  ? 22.067 1.167   6.893   0.50 14.70 ?  53  LEU   A HD11 1 
ATOM   1397 H  HD11 B LEU   A 1 53  ? 22.543 1.140   6.979   0.50 13.66 ?  53  LEU   A HD11 1 
ATOM   1398 H  HD12 A LEU   A 1 53  ? 22.967 2.100   5.974   0.50 14.70 ?  53  LEU   A HD12 1 
ATOM   1399 H  HD12 B LEU   A 1 53  ? 23.135 2.182   5.936   0.50 13.66 ?  53  LEU   A HD12 1 
ATOM   1400 H  HD13 A LEU   A 1 53  ? 23.451 1.724   7.440   0.50 14.70 ?  53  LEU   A HD13 1 
ATOM   1401 H  HD13 B LEU   A 1 53  ? 23.907 1.892   7.294   0.50 13.66 ?  53  LEU   A HD13 1 
ATOM   1402 H  HD21 A LEU   A 1 53  ? 20.974 2.028   8.841   0.50 15.43 ?  53  LEU   A HD21 1 
ATOM   1403 H  HD21 B LEU   A 1 53  ? 21.450 1.923   9.045   0.50 13.08 ?  53  LEU   A HD21 1 
ATOM   1404 H  HD22 A LEU   A 1 53  ? 22.189 2.848   9.454   0.50 15.43 ?  53  LEU   A HD22 1 
ATOM   1405 H  HD22 B LEU   A 1 53  ? 22.835 2.578   9.466   0.50 13.08 ?  53  LEU   A HD22 1 
ATOM   1406 H  HD23 A LEU   A 1 53  ? 20.835 3.591   9.086   0.50 15.43 ?  53  LEU   A HD23 1 
ATOM   1407 H  HD23 B LEU   A 1 53  ? 21.514 3.460   9.439   0.50 13.08 ?  53  LEU   A HD23 1 
ATOM   1408 N  N    A ASN   A 1 54  ? 23.836 7.334   6.924   0.50 10.62 ?  54  ASN   A N    1 
ATOM   1409 N  N    B ASN   A 1 54  ? 23.902 7.345   6.927   0.50 10.16 ?  54  ASN   A N    1 
ATOM   1410 C  CA   A ASN   A 1 54  ? 24.900 8.320   7.054   0.50 10.50 ?  54  ASN   A CA   1 
ATOM   1411 C  CA   B ASN   A 1 54  ? 24.942 8.357   7.065   0.50 9.94  ?  54  ASN   A CA   1 
ATOM   1412 C  C    A ASN   A 1 54  ? 24.404 9.569   7.780   0.50 10.87 ?  54  ASN   A C    1 
ATOM   1413 C  C    B ASN   A 1 54  ? 24.416 9.598   7.780   0.50 10.49 ?  54  ASN   A C    1 
ATOM   1414 O  O    A ASN   A 1 54  ? 25.099 10.108  8.650   0.50 11.43 ?  54  ASN   A O    1 
ATOM   1415 O  O    B ASN   A 1 54  ? 25.100 10.167  8.640   0.50 10.97 ?  54  ASN   A O    1 
ATOM   1416 C  CB   A ASN   A 1 54  ? 25.462 8.671   5.683   0.50 10.65 ?  54  ASN   A CB   1 
ATOM   1417 C  CB   B ASN   A 1 54  ? 25.523 8.726   5.707   0.50 10.03 ?  54  ASN   A CB   1 
ATOM   1418 C  CG   A ASN   A 1 54  ? 26.522 9.737   5.772   0.50 10.91 ?  54  ASN   A CG   1 
ATOM   1419 C  CG   B ASN   A 1 54  ? 26.492 9.876   5.813   0.50 9.98  ?  54  ASN   A CG   1 
ATOM   1420 O  OD1  A ASN   A 1 54  ? 27.514 9.570   6.484   0.50 11.05 ?  54  ASN   A OD1  1 
ATOM   1421 O  OD1  B ASN   A 1 54  ? 27.524 9.758   6.476   0.50 9.95  ?  54  ASN   A OD1  1 
ATOM   1422 N  ND2  A ASN   A 1 54  ? 26.315 10.846  5.083   0.50 11.40 ?  54  ASN   A ND2  1 
ATOM   1423 N  ND2  B ASN   A 1 54  ? 26.151 11.008  5.210   0.50 10.43 ?  54  ASN   A ND2  1 
ATOM   1424 H  H    A ASN   A 1 54  ? 23.561 7.186   6.125   0.50 12.77 ?  54  ASN   A H    1 
ATOM   1425 H  H    B ASN   A 1 54  ? 23.706 7.126   6.121   0.50 12.23 ?  54  ASN   A H    1 
ATOM   1426 H  HA   A ASN   A 1 54  ? 25.614 7.935   7.582   0.50 12.64 ?  54  ASN   A HA   1 
ATOM   1427 H  HA   B ASN   A 1 54  ? 25.656 7.991   7.606   0.50 11.97 ?  54  ASN   A HA   1 
ATOM   1428 H  HB2  A ASN   A 1 54  ? 25.857 7.869   5.292   0.50 12.81 ?  54  ASN   A HB2  1 
ATOM   1429 H  HB2  B ASN   A 1 54  ? 25.998 7.952   5.350   0.50 12.07 ?  54  ASN   A HB2  1 
ATOM   1430 H  HB3  A ASN   A 1 54  ? 24.745 8.995   5.118   0.50 12.81 ?  54  ASN   A HB3  1 
ATOM   1431 H  HB3  B ASN   A 1 54  ? 24.806 8.978   5.109   0.50 12.07 ?  54  ASN   A HB3  1 
ATOM   1432 H  HD21 A ASN   A 1 54  ? 26.896 11.476  5.113   0.50 13.71 ?  54  ASN   A HD21 1 
ATOM   1433 H  HD21 B ASN   A 1 54  ? 26.672 11.690  5.251   0.50 12.55 ?  54  ASN   A HD21 1 
ATOM   1434 H  HD22 A ASN   A 1 54  ? 25.607 10.929  4.607   0.50 13.71 ?  54  ASN   A HD22 1 
ATOM   1435 H  HD22 B ASN   A 1 54  ? 25.415 11.054  4.769   0.50 12.55 ?  54  ASN   A HD22 1 
ATOM   1436 N  N    . LYS   A 1 55  ? 23.197 10.034  7.442   1.00 11.17 ?  55  LYS   A N    1 
ATOM   1437 C  CA   . LYS   A 1 55  ? 22.617 11.190  8.120   1.00 11.68 ?  55  LYS   A CA   1 
ATOM   1438 C  C    . LYS   A 1 55  ? 22.527 10.949  9.621   1.00 11.94 ?  55  LYS   A C    1 
ATOM   1439 O  O    . LYS   A 1 55  ? 22.814 11.847  10.426  1.00 12.63 ?  55  LYS   A O    1 
ATOM   1440 C  CB   . LYS   A 1 55  ? 21.241 11.495  7.520   1.00 12.45 ?  55  LYS   A CB   1 
ATOM   1441 C  CG   . LYS   A 1 55  ? 20.508 12.660  8.168   1.00 14.14 ?  55  LYS   A CG   1 
ATOM   1442 C  CD   . LYS   A 1 55  ? 19.187 12.939  7.443   1.00 15.38 ?  55  LYS   A CD   1 
ATOM   1443 C  CE   . LYS   A 1 55  ? 18.363 14.027  8.123   1.00 17.23 ?  55  LYS   A CE   1 
ATOM   1444 N  NZ   . LYS   A 1 55  ? 17.038 14.214  7.458   1.00 18.04 ?  55  LYS   A NZ   1 
ATOM   1445 H  H    A LYS   A 1 55  ? 22.693 9.696   6.830   0.50 13.43 ?  55  LYS   A H    1 
ATOM   1446 H  H    B LYS   A 1 55  ? 22.691 9.679   6.842   0.50 13.43 ?  55  LYS   A H    1 
ATOM   1447 H  HA   . LYS   A 1 55  ? 23.185 11.962  7.974   1.00 14.04 ?  55  LYS   A HA   1 
ATOM   1448 H  HB2  . LYS   A 1 55  ? 21.352 11.710  6.580   1.00 14.97 ?  55  LYS   A HB2  1 
ATOM   1449 H  HB3  . LYS   A 1 55  ? 20.680 10.710  7.611   1.00 14.97 ?  55  LYS   A HB3  1 
ATOM   1450 H  HG2  . LYS   A 1 55  ? 20.305 12.440  9.093   1.00 17.01 ?  55  LYS   A HG2  1 
ATOM   1451 H  HG3  . LYS   A 1 55  ? 21.057 13.456  8.123   1.00 17.01 ?  55  LYS   A HG3  1 
ATOM   1452 H  HD2  . LYS   A 1 55  ? 19.381 13.229  6.539   1.00 18.49 ?  55  LYS   A HD2  1 
ATOM   1453 H  HD3  . LYS   A 1 55  ? 18.658 12.127  7.427   1.00 18.49 ?  55  LYS   A HD3  1 
ATOM   1454 H  HE2  . LYS   A 1 55  ? 18.206 13.779  9.048   1.00 20.71 ?  55  LYS   A HE2  1 
ATOM   1455 H  HE3  . LYS   A 1 55  ? 18.845 14.868  8.080   1.00 20.71 ?  55  LYS   A HE3  1 
ATOM   1456 H  HZ1  . LYS   A 1 55  ? 16.498 14.687  7.985   1.00 21.68 ?  55  LYS   A HZ1  1 
ATOM   1457 H  HZ2  . LYS   A 1 55  ? 17.142 14.648  6.689   1.00 21.68 ?  55  LYS   A HZ2  1 
ATOM   1458 H  HZ3  . LYS   A 1 55  ? 16.664 13.422  7.298   1.00 21.68 ?  55  LYS   A HZ3  1 
ATOM   1459 N  N    . ALA   A 1 56  ? 22.144 9.733   10.019  1.00 12.05 ?  56  ALA   A N    1 
ATOM   1460 C  CA   . ALA   A 1 56  ? 22.028 9.395   11.432  1.00 12.75 ?  56  ALA   A CA   1 
ATOM   1461 C  C    . ALA   A 1 56  ? 23.372 9.428   12.152  1.00 12.58 ?  56  ALA   A C    1 
ATOM   1462 O  O    . ALA   A 1 56  ? 23.394 9.607   13.371  1.00 14.18 ?  56  ALA   A O    1 
ATOM   1463 C  CB   . ALA   A 1 56  ? 21.346 8.029   11.597  1.00 13.64 ?  56  ALA   A CB   1 
ATOM   1464 H  H    . ALA   A 1 56  ? 21.959 9.089   9.483   1.00 14.49 ?  56  ALA   A H    1 
ATOM   1465 H  HA   . ALA   A 1 56  ? 21.463 10.051  11.859  1.00 15.33 ?  56  ALA   A HA   1 
ATOM   1466 H  HB1  . ALA   A 1 56  ? 21.275 7.820   12.543  1.00 16.41 ?  56  ALA   A HB1  1 
ATOM   1467 H  HB2  . ALA   A 1 56  ? 20.458 8.069   11.204  1.00 16.41 ?  56  ALA   A HB2  1 
ATOM   1468 H  HB3  . ALA   A 1 56  ? 21.873 7.349   11.149  1.00 16.41 ?  56  ALA   A HB3  1 
ATOM   1469 N  N    . THR   A 1 57  ? 24.486 9.261   11.429  1.00 11.74 ?  57  THR   A N    1 
ATOM   1470 C  CA   . THR   A 1 57  ? 25.830 9.388   11.999  1.00 11.82 ?  57  THR   A CA   1 
ATOM   1471 C  C    . THR   A 1 57  ? 26.380 10.811  11.929  1.00 12.00 ?  57  THR   A C    1 
ATOM   1472 O  O    . THR   A 1 57  ? 27.564 11.025  12.226  1.00 12.69 ?  57  THR   A O    1 
ATOM   1473 C  CB   . THR   A 1 57  ? 26.845 8.441   11.325  1.00 11.89 ?  57  THR   A CB   1 
ATOM   1474 O  OG1  . THR   A 1 57  ? 27.228 8.937   10.030  1.00 11.27 ?  57  THR   A OG1  1 
ATOM   1475 C  CG2  . THR   A 1 57  ? 26.327 7.013   11.226  1.00 11.90 ?  57  THR   A CG2  1 
ATOM   1476 H  H    . THR   A 1 57  ? 24.489 9.048   10.591  1.00 14.12 ?  57  THR   A H    1 
ATOM   1477 H  HA   . THR   A 1 57  ? 25.787 9.128   12.937  1.00 14.22 ?  57  THR   A HA   1 
ATOM   1478 H  HB   . THR   A 1 57  ? 27.646 8.406   11.884  1.00 14.30 ?  57  THR   A HB   1 
ATOM   1479 H  HG1  . THR   A 1 57  ? 26.551 8.996   9.541   1.00 13.56 ?  57  THR   A HG1  1 
ATOM   1480 H  HG21 . THR   A 1 57  ? 26.983 6.443   10.787  1.00 14.32 ?  57  THR   A HG21 1 
ATOM   1481 H  HG22 . THR   A 1 57  ? 26.152 6.653   12.113  1.00 14.32 ?  57  THR   A HG22 1 
ATOM   1482 H  HG23 . THR   A 1 57  ? 25.505 6.989   10.714  1.00 14.32 ?  57  THR   A HG23 1 
ATOM   1483 N  N    . ASN   A 1 58  ? 25.564 11.784  11.528  1.00 12.52 ?  58  ASN   A N    1 
ATOM   1484 C  CA   . ASN   A 1 58  ? 26.024 13.167  11.431  1.00 13.66 ?  58  ASN   A CA   1 
ATOM   1485 C  C    . ASN   A 1 58  ? 27.168 13.300  10.418  1.00 12.29 ?  58  ASN   A C    1 
ATOM   1486 O  O    . ASN   A 1 58  ? 28.067 14.129  10.578  1.00 13.14 ?  58  ASN   A O    1 
ATOM   1487 C  CB   . ASN   A 1 58  ? 26.405 13.704  12.825  1.00 15.99 ?  58  ASN   A CB   1 
ATOM   1488 C  CG   . ASN   A 1 58  ? 26.813 15.164  12.824  1.00 19.53 ?  58  ASN   A CG   1 
ATOM   1489 O  OD1  . ASN   A 1 58  ? 26.186 15.988  12.169  1.00 21.09 ?  58  ASN   A OD1  1 
ATOM   1490 N  ND2  . ASN   A 1 58  ? 27.862 15.493  13.579  1.00 20.67 ?  58  ASN   A ND2  1 
ATOM   1491 H  H    . ASN   A 1 58  ? 24.743 11.656  11.301  1.00 15.06 ?  58  ASN   A H    1 
ATOM   1492 H  HA   . ASN   A 1 58  ? 25.283 13.696  11.105  1.00 16.43 ?  58  ASN   A HA   1 
ATOM   1493 H  HB2  . ASN   A 1 58  ? 25.634 13.605  13.416  1.00 19.22 ?  58  ASN   A HB2  1 
ATOM   1494 H  HB3  . ASN   A 1 58  ? 27.146 13.190  13.171  1.00 19.22 ?  58  ASN   A HB3  1 
ATOM   1495 H  HD21 . ASN   A 1 58  ? 28.123 16.310  13.613  1.00 24.84 ?  58  ASN   A HD21 1 
ATOM   1496 H  HD22 . ASN   A 1 58  ? 28.267 14.887  14.029  1.00 24.84 ?  58  ASN   A HD22 1 
ATOM   1497 N  N    . ASN   A 1 59  ? 27.146 12.483  9.362   1.00 11.61 ?  59  ASN   A N    1 
ATOM   1498 C  CA   . ASN   A 1 59  ? 28.125 12.465  8.265   1.00 11.04 ?  59  ASN   A CA   1 
ATOM   1499 C  C    . ASN   A 1 59  ? 29.443 11.784  8.645   1.00 10.84 ?  59  ASN   A C    1 
ATOM   1500 O  O    . ASN   A 1 59  ? 30.362 11.750  7.814   1.00 11.22 ?  59  ASN   A O    1 
ATOM   1501 C  CB   . ASN   A 1 59  ? 28.411 13.851  7.659   1.00 11.40 ?  59  ASN   A CB   1 
ATOM   1502 C  CG   . ASN   A 1 59  ? 28.753 13.786  6.189   1.00 11.67 ?  59  ASN   A CG   1 
ATOM   1503 O  OD1  . ASN   A 1 59  ? 28.046 13.156  5.401   1.00 11.96 ?  59  ASN   A OD1  1 
ATOM   1504 N  ND2  . ASN   A 1 59  ? 29.834 14.452  5.802   1.00 12.51 ?  59  ASN   A ND2  1 
ATOM   1505 H  H    . ASN   A 1 59  ? 26.535 11.888  9.248   1.00 13.97 ?  59  ASN   A H    1 
ATOM   1506 H  HA   . ASN   A 1 59  ? 27.746 11.938  7.553   1.00 13.28 ?  59  ASN   A HA   1 
ATOM   1507 H  HB2  . ASN   A 1 59  ? 27.626 14.412  7.749   1.00 13.71 ?  59  ASN   A HB2  1 
ATOM   1508 H  HB3  . ASN   A 1 59  ? 29.164 14.257  8.116   1.00 13.71 ?  59  ASN   A HB3  1 
ATOM   1509 H  HD21 . ASN   A 1 59  ? 30.076 14.454  4.974   1.00 15.05 ?  59  ASN   A HD21 1 
ATOM   1510 H  HD22 . ASN   A 1 59  ? 30.308 14.887  6.380   1.00 15.05 ?  59  ASN   A HD22 1 
ATOM   1511 N  N    . ALA   A 1 60  ? 29.574 11.235  9.854   1.00 10.90 ?  60  ALA   A N    1 
ATOM   1512 C  CA   . ALA   A 1 60  ? 30.816 10.556  10.208  1.00 11.09 ?  60  ALA   A CA   1 
ATOM   1513 C  C    . ALA   A 1 60  ? 31.042 9.320   9.344   1.00 11.10 ?  60  ALA   A C    1 
ATOM   1514 O  O    . ALA   A 1 60  ? 32.189 9.001   9.005   1.00 11.61 ?  60  ALA   A O    1 
ATOM   1515 C  CB   . ALA   A 1 60  ? 30.816 10.200  11.695  1.00 11.92 ?  60  ALA   A CB   1 
ATOM   1516 H  H    . ALA   A 1 60  ? 28.972 11.238  10.468  1.00 13.11 ?  60  ALA   A H    1 
ATOM   1517 H  HA   . ALA   A 1 60  ? 31.556 11.163  10.051  1.00 13.34 ?  60  ALA   A HA   1 
ATOM   1518 H  HB1  . ALA   A 1 60  ? 31.646 9.753   11.916  1.00 14.34 ?  60  ALA   A HB1  1 
ATOM   1519 H  HB2  . ALA   A 1 60  ? 30.732 11.018  12.217  1.00 14.34 ?  60  ALA   A HB2  1 
ATOM   1520 H  HB3  . ALA   A 1 60  ? 30.063 9.616   11.882  1.00 14.34 ?  60  ALA   A HB3  1 
ATOM   1521 N  N    . MET   A 1 61  ? 29.968 8.626   8.960   1.00 10.69 ?  61  MET   A N    1 
ATOM   1522 C  CA   . MET   A 1 61  ? 30.111 7.489   8.053   1.00 10.54 ?  61  MET   A CA   1 
ATOM   1523 C  C    . MET   A 1 61  ? 30.739 7.916   6.727   1.00 10.28 ?  61  MET   A C    1 
ATOM   1524 O  O    . MET   A 1 61  ? 31.633 7.236   6.204   1.00 10.55 ?  61  MET   A O    1 
ATOM   1525 C  CB   . MET   A 1 61  ? 28.749 6.817   7.845   1.00 10.25 ?  61  MET   A CB   1 
ATOM   1526 C  CG   . MET   A 1 61  ? 28.757 5.656   6.863   1.00 11.15 ?  61  MET   A CG   1 
ATOM   1527 S  SD   . MET   A 1 61  ? 27.135 4.904   6.651   1.00 11.99 ?  61  MET   A SD   1 
ATOM   1528 C  CE   . MET   A 1 61  ? 27.002 3.985   8.191   1.00 13.73 ?  61  MET   A CE   1 
ATOM   1529 H  H    . MET   A 1 61  ? 29.157 8.787   9.209   1.00 12.86 ?  61  MET   A H    1 
ATOM   1530 H  HA   . MET   A 1 61  ? 30.692 6.834   8.472   1.00 12.68 ?  61  MET   A HA   1 
ATOM   1531 H  HB2  . MET   A 1 61  ? 28.439 6.475   8.697   1.00 12.34 ?  61  MET   A HB2  1 
ATOM   1532 H  HB3  . MET   A 1 61  ? 28.125 7.477   7.511   1.00 12.34 ?  61  MET   A HB3  1 
ATOM   1533 H  HG2  . MET   A 1 61  ? 29.047 5.970   5.992   1.00 13.41 ?  61  MET   A HG2  1 
ATOM   1534 H  HG3  . MET   A 1 61  ? 29.360 4.967   7.184   1.00 13.41 ?  61  MET   A HG3  1 
ATOM   1535 H  HE1  . MET   A 1 61  ? 26.159 3.501   8.201   1.00 16.51 ?  61  MET   A HE1  1 
ATOM   1536 H  HE2  . MET   A 1 61  ? 27.740 3.360   8.254   1.00 16.51 ?  61  MET   A HE2  1 
ATOM   1537 H  HE3  . MET   A 1 61  ? 27.031 4.607   8.937   1.00 16.51 ?  61  MET   A HE3  1 
ATOM   1538 N  N    . GLN   A 1 62  ? 30.287 9.044   6.171   1.00 10.44 ?  62  GLN   A N    1 
ATOM   1539 C  CA   . GLN   A 1 62  ? 30.840 9.522   4.907   1.00 10.75 ?  62  GLN   A CA   1 
ATOM   1540 C  C    . GLN   A 1 62  ? 32.311 9.903   5.043   1.00 10.64 ?  62  GLN   A C    1 
ATOM   1541 O  O    . GLN   A 1 62  ? 33.117 9.597   4.156   1.00 11.03 ?  62  GLN   A O    1 
ATOM   1542 C  CB   . GLN   A 1 62  ? 30.031 10.709  4.379   1.00 10.86 ?  62  GLN   A CB   1 
ATOM   1543 C  CG   . GLN   A 1 62  ? 30.400 11.074  2.956   1.00 10.72 ?  62  GLN   A CG   1 
ATOM   1544 C  CD   . GLN   A 1 62  ? 30.074 9.945   2.005   1.00 10.85 ?  62  GLN   A CD   1 
ATOM   1545 O  OE1  . GLN   A 1 62  ? 28.896 9.629   1.798   1.00 11.57 ?  62  GLN   A OE1  1 
ATOM   1546 N  NE2  . GLN   A 1 62  ? 31.096 9.283   1.475   1.00 11.56 ?  62  GLN   A NE2  1 
ATOM   1547 H  H    . GLN   A 1 62  ? 29.668 9.538   6.504   1.00 12.56 ?  62  GLN   A H    1 
ATOM   1548 H  HA   . GLN   A 1 62  ? 30.782 8.805   4.259   1.00 12.93 ?  62  GLN   A HA   1 
ATOM   1549 H  HB2  . GLN   A 1 62  ? 29.090 10.486  4.400   1.00 13.07 ?  62  GLN   A HB2  1 
ATOM   1550 H  HB3  . GLN   A 1 62  ? 30.205 11.483  4.940   1.00 13.07 ?  62  GLN   A HB3  1 
ATOM   1551 H  HG2  . GLN   A 1 62  ? 29.893 11.851  2.683   1.00 12.90 ?  62  GLN   A HG2  1 
ATOM   1552 H  HG3  . GLN   A 1 62  ? 31.352 11.253  2.902   1.00 12.90 ?  62  GLN   A HG3  1 
ATOM   1553 H  HE21 . GLN   A 1 62  ? 31.904 9.520   1.659   1.00 13.90 ?  62  GLN   A HE21 1 
ATOM   1554 H  HE22 . GLN   A 1 62  ? 30.954 8.626   0.941   1.00 13.90 ?  62  GLN   A HE22 1 
ATOM   1555 N  N    . VAL   A 1 63  ? 32.672 10.594  6.130   1.00 11.00 ?  63  VAL   A N    1 
ATOM   1556 C  CA   . VAL   A 1 63  ? 34.064 10.995  6.339   1.00 12.14 ?  63  VAL   A CA   1 
ATOM   1557 C  C    . VAL   A 1 63  ? 34.967 9.763   6.398   1.00 11.45 ?  63  VAL   A C    1 
ATOM   1558 O  O    . VAL   A 1 63  ? 36.018 9.700   5.742   1.00 11.88 ?  63  VAL   A O    1 
ATOM   1559 C  CB   . VAL   A 1 63  ? 34.180 11.870  7.601   1.00 13.67 ?  63  VAL   A CB   1 
ATOM   1560 C  CG1  . VAL   A 1 63  ? 35.631 12.118  7.952   1.00 15.38 ?  63  VAL   A CG1  1 
ATOM   1561 C  CG2  . VAL   A 1 63  ? 33.431 13.193  7.400   1.00 13.91 ?  63  VAL   A CG2  1 
ATOM   1562 H  H    . VAL   A 1 63  ? 32.129 10.838  6.754   1.00 13.24 ?  63  VAL   A H    1 
ATOM   1563 H  HA   . VAL   A 1 63  ? 34.343 11.528  5.582   1.00 14.60 ?  63  VAL   A HA   1 
ATOM   1564 H  HB   . VAL   A 1 63  ? 33.767 11.404  8.347   1.00 16.44 ?  63  VAL   A HB   1 
ATOM   1565 H  HG11 . VAL   A 1 63  ? 35.676 12.852  8.583   1.00 18.49 ?  63  VAL   A HG11 1 
ATOM   1566 H  HG12 . VAL   A 1 63  ? 36.002 11.316  8.346   1.00 18.49 ?  63  VAL   A HG12 1 
ATOM   1567 H  HG13 . VAL   A 1 63  ? 36.111 12.348  7.141   1.00 18.49 ?  63  VAL   A HG13 1 
ATOM   1568 H  HG21 . VAL   A 1 63  ? 33.525 13.733  8.201   1.00 16.72 ?  63  VAL   A HG21 1 
ATOM   1569 H  HG22 . VAL   A 1 63  ? 33.809 13.658  6.639   1.00 16.72 ?  63  VAL   A HG22 1 
ATOM   1570 H  HG23 . VAL   A 1 63  ? 32.491 13.004  7.240   1.00 16.72 ?  63  VAL   A HG23 1 
ATOM   1571 N  N    . GLU   A 1 64  ? 34.556 8.751   7.170   1.00 11.30 ?  64  GLU   A N    1 
ATOM   1572 C  CA   . GLU   A 1 64  ? 35.324 7.515   7.264   1.00 11.19 ?  64  GLU   A CA   1 
ATOM   1573 C  C    . GLU   A 1 64  ? 35.414 6.825   5.908   1.00 10.86 ?  64  GLU   A C    1 
ATOM   1574 O  O    . GLU   A 1 64  ? 36.465 6.283   5.529   1.00 11.34 ?  64  GLU   A O    1 
ATOM   1575 C  CB   . GLU   A 1 64  ? 34.646 6.604   8.288   1.00 11.97 ?  64  GLU   A CB   1 
ATOM   1576 C  CG   . GLU   A 1 64  ? 35.308 5.254   8.447   1.00 12.32 ?  64  GLU   A CG   1 
ATOM   1577 C  CD   . GLU   A 1 64  ? 34.431 4.253   9.168   1.00 12.85 ?  64  GLU   A CD   1 
ATOM   1578 O  OE1  . GLU   A 1 64  ? 33.190 4.333   9.024   1.00 13.85 ?  64  GLU   A OE1  1 
ATOM   1579 O  OE2  . GLU   A 1 64  ? 34.990 3.369   9.857   1.00 13.18 -1 64  GLU   A OE2  1 
ATOM   1580 H  H    . GLU   A 1 64  ? 33.825 8.748   7.628   1.00 13.59 ?  64  GLU   A H    1 
ATOM   1581 H  HA   . GLU   A 1 64  ? 36.221 7.722   7.572   1.00 13.46 ?  64  GLU   A HA   1 
ATOM   1582 H  HB2  . GLU   A 1 64  ? 34.668 7.051   9.156   1.00 14.40 ?  64  GLU   A HB2  1 
ATOM   1583 H  HB3  . GLU   A 1 64  ? 33.730 6.466   8.018   1.00 14.40 ?  64  GLU   A HB3  1 
ATOM   1584 H  HG2  . GLU   A 1 64  ? 35.517 4.890   7.573   1.00 14.82 ?  64  GLU   A HG2  1 
ATOM   1585 H  HG3  . GLU   A 1 64  ? 36.124 5.364   8.960   1.00 14.82 ?  64  GLU   A HG3  1 
ATOM   1586 N  N    . SER   A 1 65  ? 34.294 6.805   5.181   1.00 10.74 ?  65  SER   A N    1 
ATOM   1587 C  CA   . SER   A 1 65  ? 34.241 6.151   3.880   1.00 10.54 ?  65  SER   A CA   1 
ATOM   1588 C  C    . SER   A 1 65  ? 35.156 6.830   2.868   1.00 10.88 ?  65  SER   A C    1 
ATOM   1589 O  O    . SER   A 1 65  ? 35.791 6.157   2.047   1.00 11.72 ?  65  SER   A O    1 
ATOM   1590 C  CB   . SER   A 1 65  ? 32.802 6.155   3.357   1.00 10.52 ?  65  SER   A CB   1 
ATOM   1591 O  OG   . SER   A 1 65  ? 31.952 5.337   4.148   1.00 11.31 ?  65  SER   A OG   1 
ATOM   1592 H  H    . SER   A 1 65  ? 33.557 7.170   5.424   1.00 12.92 ?  65  SER   A H    1 
ATOM   1593 H  HA   . SER   A 1 65  ? 34.531 5.235   3.972   1.00 12.68 ?  65  SER   A HA   1 
ATOM   1594 H  HB2  . SER   A 1 65  ? 32.463 7.061   3.377   1.00 12.66 ?  65  SER   A HB2  1 
ATOM   1595 H  HB3  . SER   A 1 65  ? 32.805 5.821   2.449   1.00 12.66 ?  65  SER   A HB3  1 
ATOM   1596 H  HG   . SER   A 1 65  ? 31.950 5.612   4.947   1.00 13.60 ?  65  SER   A HG   1 
ATOM   1597 N  N    . ASP   A 1 66  ? 35.219 8.166   2.886   1.00 11.11 ?  66  ASP   A N    1 
ATOM   1598 C  CA   . ASP   A 1 66  ? 36.074 8.863   1.930   1.00 11.92 ?  66  ASP   A CA   1 
ATOM   1599 C  C    . ASP   A 1 66  ? 37.542 8.512   2.158   1.00 11.95 ?  66  ASP   A C    1 
ATOM   1600 O  O    . ASP   A 1 66  ? 38.308 8.339   1.200   1.00 12.79 ?  66  ASP   A O    1 
ATOM   1601 C  CB   . ASP   A 1 66  ? 35.857 10.369  2.036   1.00 13.15 ?  66  ASP   A CB   1 
ATOM   1602 C  CG   . ASP   A 1 66  ? 34.517 10.829  1.446   1.00 14.83 ?  66  ASP   A CG   1 
ATOM   1603 O  OD1  . ASP   A 1 66  ? 33.799 10.034  0.798   1.00 14.60 ?  66  ASP   A OD1  1 
ATOM   1604 O  OD2  . ASP   A 1 66  ? 34.205 12.020  1.624   1.00 17.77 -1 66  ASP   A OD2  1 
ATOM   1605 H  H    . ASP   A 1 66  ? 34.773 8.682   3.418   1.00 13.36 ?  66  ASP   A H    1 
ATOM   1606 H  HA   . ASP   A 1 66  ? 35.830 8.587   1.033   1.00 14.34 ?  66  ASP   A HA   1 
ATOM   1607 H  HB2  . ASP   A 1 66  ? 35.870 10.625  2.971   1.00 15.81 ?  66  ASP   A HB2  1 
ATOM   1608 H  HB3  . ASP   A 1 66  ? 36.569 10.821  1.558   1.00 15.81 ?  66  ASP   A HB3  1 
ATOM   1609 N  N    . ASP   A 1 67  ? 37.948 8.376   3.420   1.00 12.09 ?  67  ASP   A N    1 
ATOM   1610 C  CA   . ASP   A 1 67  ? 39.306 7.930   3.713   1.00 12.87 ?  67  ASP   A CA   1 
ATOM   1611 C  C    . ASP   A 1 67  ? 39.526 6.496   3.241   1.00 12.67 ?  67  ASP   A C    1 
ATOM   1612 O  O    . ASP   A 1 67  ? 40.585 6.173   2.693   1.00 13.63 ?  67  ASP   A O    1 
ATOM   1613 C  CB   . ASP   A 1 67  ? 39.583 8.056   5.208   1.00 14.33 ?  67  ASP   A CB   1 
ATOM   1614 C  CG   . ASP   A 1 67  ? 40.888 7.397   5.615   1.00 15.22 ?  67  ASP   A CG   1 
ATOM   1615 O  OD1  . ASP   A 1 67  ? 41.956 8.036   5.462   1.00 18.16 ?  67  ASP   A OD1  1 
ATOM   1616 O  OD2  . ASP   A 1 67  ? 40.844 6.234   6.079   1.00 14.95 -1 67  ASP   A OD2  1 
ATOM   1617 H  H    . ASP   A 1 67  ? 37.464 8.531   4.111   1.00 14.54 ?  67  ASP   A H    1 
ATOM   1618 H  HA   . ASP   A 1 67  ? 39.933 8.494   3.239   1.00 15.48 ?  67  ASP   A HA   1 
ATOM   1619 H  HB2  . ASP   A 1 67  ? 39.634 8.992   5.436   1.00 17.23 ?  67  ASP   A HB2  1 
ATOM   1620 H  HB3  . ASP   A 1 67  ? 38.861 7.628   5.698   1.00 17.23 ?  67  ASP   A HB3  1 
ATOM   1621 N  N    A TYR   A 1 68  ? 38.527 5.631   3.416   0.50 12.19 ?  68  TYR   A N    1 
ATOM   1622 N  N    B TYR   A 1 68  ? 38.533 5.614   3.448   0.50 12.29 ?  68  TYR   A N    1 
ATOM   1623 C  CA   A TYR   A 1 68  ? 38.671 4.250   2.967   0.50 12.23 ?  68  TYR   A CA   1 
ATOM   1624 C  CA   B TYR   A 1 68  ? 38.642 4.238   2.954   0.50 12.36 ?  68  TYR   A CA   1 
ATOM   1625 C  C    A TYR   A 1 68  ? 38.872 4.174   1.453   0.50 12.06 ?  68  TYR   A C    1 
ATOM   1626 C  C    B TYR   A 1 68  ? 38.909 4.216   1.453   0.50 12.05 ?  68  TYR   A C    1 
ATOM   1627 O  O    A TYR   A 1 68  ? 39.718 3.409   0.970   0.50 12.53 ?  68  TYR   A O    1 
ATOM   1628 O  O    B TYR   A 1 68  ? 39.822 3.528   0.979   0.50 12.47 ?  68  TYR   A O    1 
ATOM   1629 C  CB   A TYR   A 1 68  ? 37.457 3.421   3.410   0.50 12.56 ?  68  TYR   A CB   1 
ATOM   1630 C  CB   B TYR   A 1 68  ? 37.374 3.413   3.275   0.50 12.70 ?  68  TYR   A CB   1 
ATOM   1631 C  CG   A TYR   A 1 68  ? 37.522 2.009   2.883   0.50 13.30 ?  68  TYR   A CG   1 
ATOM   1632 C  CG   B TYR   A 1 68  ? 37.390 2.049   2.578   0.50 13.07 ?  68  TYR   A CG   1 
ATOM   1633 C  CD1  A TYR   A 1 68  ? 37.049 1.710   1.614   0.50 14.35 ?  68  TYR   A CD1  1 
ATOM   1634 C  CD1  B TYR   A 1 68  ? 36.930 1.910   1.268   0.50 13.22 ?  68  TYR   A CD1  1 
ATOM   1635 C  CD2  A TYR   A 1 68  ? 38.111 0.992   3.622   0.50 14.52 ?  68  TYR   A CD2  1 
ATOM   1636 C  CD2  B TYR   A 1 68  ? 37.912 0.918   3.207   0.50 13.76 ?  68  TYR   A CD2  1 
ATOM   1637 C  CE1  A TYR   A 1 68  ? 37.145 0.445   1.098   0.50 15.71 ?  68  TYR   A CE1  1 
ATOM   1638 C  CE1  B TYR   A 1 68  ? 36.984 0.696   0.613   0.50 12.67 ?  68  TYR   A CE1  1 
ATOM   1639 C  CE2  A TYR   A 1 68  ? 38.202 -0.295  3.113   0.50 15.33 ?  68  TYR   A CE2  1 
ATOM   1640 C  CE2  B TYR   A 1 68  ? 37.959 -0.312  2.559   0.50 12.93 ?  68  TYR   A CE2  1 
ATOM   1641 C  CZ   A TYR   A 1 68  ? 37.719 -0.554  1.852   0.50 16.27 ?  68  TYR   A CZ   1 
ATOM   1642 C  CZ   B TYR   A 1 68  ? 37.501 -0.405  1.265   0.50 12.15 ?  68  TYR   A CZ   1 
ATOM   1643 O  OH   A TYR   A 1 68  ? 37.821 -1.816  1.329   0.50 18.38 ?  68  TYR   A OH   1 
ATOM   1644 O  OH   B TYR   A 1 68  ? 37.576 -1.617  0.635   0.50 12.66 ?  68  TYR   A OH   1 
ATOM   1645 H  H    A TYR   A 1 68  ? 37.768 5.813   3.782   0.50 14.67 ?  68  TYR   A H    1 
ATOM   1646 H  H    B TYR   A 1 68  ? 37.797 5.785   3.866   0.50 14.78 ?  68  TYR   A H    1 
ATOM   1647 H  HA   A TYR   A 1 68  ? 39.454 3.868   3.387   0.50 14.71 ?  68  TYR   A HA   1 
ATOM   1648 H  HA   B TYR   A 1 68  ? 39.385 3.806   3.396   0.50 14.86 ?  68  TYR   A HA   1 
ATOM   1649 H  HB2  A TYR   A 1 68  ? 37.435 3.382   4.378   0.50 15.10 ?  68  TYR   A HB2  1 
ATOM   1650 H  HB2  B TYR   A 1 68  ? 37.320 3.259   4.231   0.50 15.27 ?  68  TYR   A HB2  1 
ATOM   1651 H  HB3  A TYR   A 1 68  ? 36.646 3.834   3.071   0.50 15.10 ?  68  TYR   A HB3  1 
ATOM   1652 H  HB3  B TYR   A 1 68  ? 36.587 3.897   2.971   0.50 15.27 ?  68  TYR   A HB3  1 
ATOM   1653 H  HD1  A TYR   A 1 68  ? 36.669 2.389   1.099   0.50 17.25 ?  68  TYR   A HD1  1 
ATOM   1654 H  HD1  B TYR   A 1 68  ? 36.584 2.648   0.820   0.50 15.90 ?  68  TYR   A HD1  1 
ATOM   1655 H  HD2  A TYR   A 1 68  ? 38.450 1.179   4.467   0.50 17.46 ?  68  TYR   A HD2  1 
ATOM   1656 H  HD2  B TYR   A 1 68  ? 38.231 0.990   4.073   0.50 16.55 ?  68  TYR   A HD2  1 
ATOM   1657 H  HE1  A TYR   A 1 68  ? 36.816 0.265   0.245   0.50 18.89 ?  68  TYR   A HE1  1 
ATOM   1658 H  HE1  B TYR   A 1 68  ? 36.668 0.610   -0.262  0.50 15.23 ?  68  TYR   A HE1  1 
ATOM   1659 H  HE2  A TYR   A 1 68  ? 38.600 -0.970  3.610   0.50 18.43 ?  68  TYR   A HE2  1 
ATOM   1660 H  HE2  B TYR   A 1 68  ? 38.315 -1.062  2.985   0.50 15.55 ?  68  TYR   A HE2  1 
ATOM   1661 H  HH   A TYR   A 1 68  ? 38.181 -2.331  1.880   0.50 22.09 ?  68  TYR   A HH   1 
ATOM   1662 H  HH   B TYR   A 1 68  ? 37.317 -1.558  -0.164  0.50 15.23 ?  68  TYR   A HH   1 
ATOM   1663 N  N    . ILE   A 1 69  ? 38.102 4.952   0.686   1.00 11.53 ?  69  ILE   A N    1 
ATOM   1664 C  CA   . ILE   A 1 69  ? 38.237 4.943   -0.769  1.00 11.83 ?  69  ILE   A CA   1 
ATOM   1665 C  C    . ILE   A 1 69  ? 39.565 5.555   -1.201  1.00 11.90 ?  69  ILE   A C    1 
ATOM   1666 O  O    . ILE   A 1 69  ? 40.209 5.066   -2.137  1.00 12.08 ?  69  ILE   A O    1 
ATOM   1667 C  CB   . ILE   A 1 69  ? 37.038 5.654   -1.427  1.00 12.70 ?  69  ILE   A CB   1 
ATOM   1668 C  CG1  . ILE   A 1 69  ? 35.728 4.914   -1.144  1.00 13.01 ?  69  ILE   A CG1  1 
ATOM   1669 C  CG2  . ILE   A 1 69  ? 37.272 5.852   -2.933  1.00 14.08 ?  69  ILE   A CG2  1 
ATOM   1670 C  CD1  . ILE   A 1 69  ? 35.560 3.624   -1.909  1.00 13.86 ?  69  ILE   A CD1  1 
ATOM   1671 H  H    A ILE   A 1 69  ? 37.504 5.493   0.986   0.50 13.87 ?  69  ILE   A H    1 
ATOM   1672 H  H    B ILE   A 1 69  ? 37.481 5.468   0.983   0.50 13.87 ?  69  ILE   A H    1 
ATOM   1673 H  HA   . ILE   A 1 69  ? 38.234 4.021   -1.069  1.00 14.23 ?  69  ILE   A HA   1 
ATOM   1674 H  HB   . ILE   A 1 69  ? 36.967 6.529   -1.028  1.00 15.27 ?  69  ILE   A HB   1 
ATOM   1675 H  HG12 . ILE   A 1 69  ? 35.693 4.698   -0.195  1.00 15.64 ?  69  ILE   A HG12 1 
ATOM   1676 H  HG13 . ILE   A 1 69  ? 34.989 5.493   -1.372  1.00 15.64 ?  69  ILE   A HG13 1 
ATOM   1677 H  HG21 . ILE   A 1 69  ? 36.423 6.061   -3.357  1.00 16.93 ?  69  ILE   A HG21 1 
ATOM   1678 H  HG22 . ILE   A 1 69  ? 37.891 6.590   -3.063  1.00 16.93 ?  69  ILE   A HG22 1 
ATOM   1679 H  HG23 . ILE   A 1 69  ? 37.637 5.040   -3.311  1.00 16.93 ?  69  ILE   A HG23 1 
ATOM   1680 H  HD11 . ILE   A 1 69  ? 34.757 3.176   -1.597  1.00 16.67 ?  69  ILE   A HD11 1 
ATOM   1681 H  HD12 . ILE   A 1 69  ? 35.476 3.826   -2.854  1.00 16.67 ?  69  ILE   A HD12 1 
ATOM   1682 H  HD13 . ILE   A 1 69  ? 36.332 3.059   -1.757  1.00 16.67 ?  69  ILE   A HD13 1 
ATOM   1683 N  N    . ALA   A 1 70  ? 39.989 6.633   -0.543  1.00 12.04 ?  70  ALA   A N    1 
ATOM   1684 C  CA   . ALA   A 1 70  ? 41.264 7.242   -0.901  1.00 12.92 ?  70  ALA   A CA   1 
ATOM   1685 C  C    . ALA   A 1 70  ? 42.412 6.258   -0.732  1.00 13.24 ?  70  ALA   A C    1 
ATOM   1686 O  O    . ALA   A 1 70  ? 43.372 6.285   -1.505  1.00 15.14 ?  70  ALA   A O    1 
ATOM   1687 C  CB   . ALA   A 1 70  ? 41.504 8.492   -0.059  1.00 13.76 ?  70  ALA   A CB   1 
ATOM   1688 H  H    . ALA   A 1 70  ? 39.568 7.021   0.095   1.00 14.48 ?  70  ALA   A H    1 
ATOM   1689 H  HA   . ALA   A 1 70  ? 41.238 7.513   -1.832  1.00 15.54 ?  70  ALA   A HA   1 
ATOM   1690 H  HB1  . ALA   A 1 70  ? 42.359 8.882   -0.309  1.00 16.54 ?  70  ALA   A HB1  1 
ATOM   1691 H  HB2  . ALA   A 1 70  ? 40.791 9.126   -0.221  1.00 16.54 ?  70  ALA   A HB2  1 
ATOM   1692 H  HB3  . ALA   A 1 70  ? 41.521 8.242   0.879   1.00 16.54 ?  70  ALA   A HB3  1 
ATOM   1693 N  N    . THR   A 1 71  ? 42.320 5.361   0.249   1.00 12.57 ?  71  THR   A N    1 
ATOM   1694 C  CA   . THR   A 1 71  ? 43.375 4.383   0.492   1.00 14.21 ?  71  THR   A CA   1 
ATOM   1695 C  C    . THR   A 1 71  ? 43.254 3.160   -0.407  1.00 14.40 ?  71  THR   A C    1 
ATOM   1696 O  O    . THR   A 1 71  ? 44.269 2.652   -0.906  1.00 16.47 ?  71  THR   A O    1 
ATOM   1697 C  CB   . THR   A 1 71  ? 43.319 3.935   1.948   1.00 16.02 ?  71  THR   A CB   1 
ATOM   1698 O  OG1  . THR   A 1 71  ? 43.583 5.060   2.791   1.00 17.54 ?  71  THR   A OG1  1 
ATOM   1699 C  CG2  . THR   A 1 71  ? 44.326 2.818   2.222   1.00 17.42 ?  71  THR   A CG2  1 
ATOM   1700 H  H    . THR   A 1 71  ? 41.650 5.289   0.781   1.00 15.12 ?  71  THR   A H    1 
ATOM   1701 H  HA   . THR   A 1 71  ? 44.238 4.788   0.325   1.00 17.08 ?  71  THR   A HA   1 
ATOM   1702 H  HB   . THR   A 1 71  ? 42.434 3.589   2.143   1.00 19.25 ?  71  THR   A HB   1 
ATOM   1703 H  HG1  . THR   A 1 71  ? 43.566 4.814   3.597   1.00 21.08 ?  71  THR   A HG1  1 
ATOM   1704 H  HG21 . THR   A 1 71  ? 44.480 2.737   3.177   1.00 20.94 ?  71  THR   A HG21 1 
ATOM   1705 H  HG22 . THR   A 1 71  ? 43.996 1.970   1.886   1.00 20.94 ?  71  THR   A HG22 1 
ATOM   1706 H  HG23 . THR   A 1 71  ? 45.174 3.019   1.788   1.00 20.94 ?  71  THR   A HG23 1 
ATOM   1707 N  N    . ASN   A 1 72  ? 42.028 2.656   -0.603  1.00 13.36 ?  72  ASN   A N    1 
ATOM   1708 C  CA   . ASN   A 1 72  ? 41.808 1.328   -1.163  1.00 13.64 ?  72  ASN   A CA   1 
ATOM   1709 C  C    . ASN   A 1 72  ? 41.173 1.311   -2.543  1.00 13.79 ?  72  ASN   A C    1 
ATOM   1710 O  O    . ASN   A 1 72  ? 41.177 0.254   -3.186  1.00 14.88 ?  72  ASN   A O    1 
ATOM   1711 C  CB   . ASN   A 1 72  ? 40.926 0.504   -0.216  1.00 14.27 ?  72  ASN   A CB   1 
ATOM   1712 C  CG   . ASN   A 1 72  ? 41.545 0.352   1.149   1.00 15.44 ?  72  ASN   A CG   1 
ATOM   1713 O  OD1  . ASN   A 1 72  ? 41.085 0.956   2.119   1.00 17.40 ?  72  ASN   A OD1  1 
ATOM   1714 N  ND2  . ASN   A 1 72  ? 42.609 -0.416  1.228   1.00 15.98 ?  72  ASN   A ND2  1 
ATOM   1715 H  H    . ASN   A 1 72  ? 41.293 3.079   -0.424  1.00 16.06 ?  72  ASN   A H    1 
ATOM   1716 H  HA   . ASN   A 1 72  ? 42.661 0.881   -1.235  1.00 16.40 ?  72  ASN   A HA   1 
ATOM   1717 H  HB2  . ASN   A 1 72  ? 40.069 0.941   -0.113  1.00 17.16 ?  72  ASN   A HB2  1 
ATOM   1718 H  HB3  . ASN   A 1 72  ? 40.807 -0.385  -0.587  1.00 17.16 ?  72  ASN   A HB3  1 
ATOM   1719 H  HD21 . ASN   A 1 72  ? 43.003 -0.524  1.987   1.00 19.20 ?  72  ASN   A HD21 1 
ATOM   1720 H  HD22 . ASN   A 1 72  ? 42.910 -0.806  0.527   1.00 19.20 ?  72  ASN   A HD22 1 
ATOM   1721 N  N    . GLY   A 1 73  ? 40.619 2.425   -3.004  1.00 13.27 ?  73  GLY   A N    1 
ATOM   1722 C  CA   . GLY   A 1 73  ? 39.872 2.450   -4.238  1.00 13.20 ?  73  GLY   A CA   1 
ATOM   1723 C  C    . GLY   A 1 73  ? 38.484 1.861   -4.066  1.00 12.47 ?  73  GLY   A C    1 
ATOM   1724 O  O    . GLY   A 1 73  ? 38.106 1.396   -2.983  1.00 13.17 ?  73  GLY   A O    1 
ATOM   1725 H  H    . GLY   A 1 73  ? 40.664 3.196   -2.616  1.00 15.96 ?  73  GLY   A H    1 
ATOM   1726 H  HA2  . GLY   A 1 73  ? 39.788 3.370   -4.549  1.00 15.88 ?  73  GLY   A HA2  1 
ATOM   1727 H  HA3  . GLY   A 1 73  ? 40.343 1.941   -4.917  1.00 15.88 ?  73  GLY   A HA3  1 
ATOM   1728 N  N    . PRO   A 1 74  ? 37.697 1.888   -5.144  1.00 13.05 ?  74  PRO   A N    1 
ATOM   1729 C  CA   . PRO   A 1 74  ? 36.302 1.446   -5.061  1.00 12.98 ?  74  PRO   A CA   1 
ATOM   1730 C  C    . PRO   A 1 74  ? 36.164 -0.039  -4.750  1.00 12.47 ?  74  PRO   A C    1 
ATOM   1731 O  O    . PRO   A 1 74  ? 37.034 -0.867  -5.043  1.00 13.41 ?  74  PRO   A O    1 
ATOM   1732 C  CB   . PRO   A 1 74  ? 35.748 1.753   -6.457  1.00 14.64 ?  74  PRO   A CB   1 
ATOM   1733 C  CG   . PRO   A 1 74  ? 36.679 2.774   -7.040  1.00 17.28 ?  74  PRO   A CG   1 
ATOM   1734 C  CD   . PRO   A 1 74  ? 38.026 2.432   -6.473  1.00 14.82 ?  74  PRO   A CD   1 
ATOM   1735 H  HA   . PRO   A 1 74  ? 35.818 1.963   -4.398  1.00 15.61 ?  74  PRO   A HA   1 
ATOM   1736 H  HB2  . PRO   A 1 74  ? 35.739 0.946   -6.994  1.00 17.60 ?  74  PRO   A HB2  1 
ATOM   1737 H  HB3  . PRO   A 1 74  ? 34.847 2.117   -6.378  1.00 17.60 ?  74  PRO   A HB3  1 
ATOM   1738 H  HG2  . PRO   A 1 74  ? 36.687 2.701   -8.008  1.00 20.77 ?  74  PRO   A HG2  1 
ATOM   1739 H  HG3  . PRO   A 1 74  ? 36.409 3.665   -6.766  1.00 20.77 ?  74  PRO   A HG3  1 
ATOM   1740 H  HD2  . PRO   A 1 74  ? 38.465 1.758   -7.018  1.00 17.82 ?  74  PRO   A HD2  1 
ATOM   1741 H  HD3  . PRO   A 1 74  ? 38.570 3.234   -6.398  1.00 17.82 ?  74  PRO   A HD3  1 
ATOM   1742 N  N    . LEU   A 1 75  ? 35.026 -0.369  -4.148  1.00 11.78 ?  75  LEU   A N    1 
ATOM   1743 C  CA   . LEU   A 1 75  ? 34.632 -1.758  -3.991  1.00 11.58 ?  75  LEU   A CA   1 
ATOM   1744 C  C    . LEU   A 1 75  ? 34.242 -2.342  -5.348  1.00 12.17 ?  75  LEU   A C    1 
ATOM   1745 O  O    . LEU   A 1 75  ? 34.103 -1.635  -6.347  1.00 13.57 ?  75  LEU   A O    1 
ATOM   1746 C  CB   . LEU   A 1 75  ? 33.447 -1.875  -3.033  1.00 11.62 ?  75  LEU   A CB   1 
ATOM   1747 C  CG   . LEU   A 1 75  ? 33.668 -1.469  -1.582  1.00 13.34 ?  75  LEU   A CG   1 
ATOM   1748 C  CD1  . LEU   A 1 75  ? 32.389 -1.671  -0.773  1.00 15.02 ?  75  LEU   A CD1  1 
ATOM   1749 C  CD2  . LEU   A 1 75  ? 34.813 -2.203  -0.949  1.00 16.72 ?  75  LEU   A CD2  1 
ATOM   1750 H  H    . LEU   A 1 75  ? 34.460 0.194   -3.830  1.00 14.17 ?  75  LEU   A H    1 
ATOM   1751 H  HA   . LEU   A 1 75  ? 35.372 -2.269  -3.638  1.00 13.93 ?  75  LEU   A HA   1 
ATOM   1752 H  HB2  . LEU   A 1 75  ? 32.726 -1.324  -3.377  1.00 13.98 ?  75  LEU   A HB2  1 
ATOM   1753 H  HB3  . LEU   A 1 75  ? 33.157 -2.803  -3.029  1.00 13.98 ?  75  LEU   A HB3  1 
ATOM   1754 H  HG   . LEU   A 1 75  ? 33.886 -0.524  -1.560  1.00 16.04 ?  75  LEU   A HG   1 
ATOM   1755 H  HD11 . LEU   A 1 75  ? 32.552 -1.403  0.144   1.00 18.05 ?  75  LEU   A HD11 1 
ATOM   1756 H  HD12 . LEU   A 1 75  ? 31.688 -1.120  -1.159  1.00 18.05 ?  75  LEU   A HD12 1 
ATOM   1757 H  HD13 . LEU   A 1 75  ? 32.137 -2.604  -0.810  1.00 18.05 ?  75  LEU   A HD13 1 
ATOM   1758 H  HD21 . LEU   A 1 75  ? 34.871 -1.957  -0.014  1.00 20.09 ?  75  LEU   A HD21 1 
ATOM   1759 H  HD22 . LEU   A 1 75  ? 34.663 -3.159  -1.032  1.00 20.09 ?  75  LEU   A HD22 1 
ATOM   1760 H  HD23 . LEU   A 1 75  ? 35.639 -1.962  -1.404  1.00 20.09 ?  75  LEU   A HD23 1 
ATOM   1761 N  N    . LYS   A 1 76  ? 34.074 -3.662  -5.368  1.00 12.66 ?  76  LYS   A N    1 
ATOM   1762 C  CA   . LYS   A 1 76  ? 33.477 -4.388  -6.485  1.00 12.88 ?  76  LYS   A CA   1 
ATOM   1763 C  C    . LYS   A 1 76  ? 31.964 -4.475  -6.287  1.00 11.85 ?  76  LYS   A C    1 
ATOM   1764 O  O    . LYS   A 1 76  ? 31.483 -4.587  -5.162  1.00 11.75 ?  76  LYS   A O    1 
ATOM   1765 C  CB   . LYS   A 1 76  ? 34.026 -5.826  -6.531  1.00 14.57 ?  76  LYS   A CB   1 
ATOM   1766 C  CG   . LYS   A 1 76  ? 35.537 -5.932  -6.718  1.00 16.02 ?  76  LYS   A CG   1 
ATOM   1767 C  CD   . LYS   A 1 76  ? 36.066 -7.330  -6.483  1.00 17.33 ?  76  LYS   A CD   1 
ATOM   1768 C  CE   . LYS   A 1 76  ? 37.553 -7.396  -6.736  1.00 19.86 ?  76  LYS   A CE   1 
ATOM   1769 N  NZ   . LYS   A 1 76  ? 38.105 -8.750  -6.545  1.00 20.68 ?  76  LYS   A NZ   1 
ATOM   1770 H  H    . LYS   A 1 76  ? 34.306 -4.182  -4.719  1.00 15.22 ?  76  LYS   A H    1 
ATOM   1771 H  HA   . LYS   A 1 76  ? 33.671 -3.941  -7.323  1.00 15.50 ?  76  LYS   A HA   1 
ATOM   1772 H  HB2  . LYS   A 1 76  ? 33.801 -6.270  -5.700  1.00 17.52 ?  76  LYS   A HB2  1 
ATOM   1773 H  HB3  . LYS   A 1 76  ? 33.607 -6.291  -7.274  1.00 17.52 ?  76  LYS   A HB3  1 
ATOM   1774 H  HG2  . LYS   A 1 76  ? 35.762 -5.675  -7.626  1.00 19.26 ?  76  LYS   A HG2  1 
ATOM   1775 H  HG3  . LYS   A 1 76  ? 35.975 -5.337  -6.088  1.00 19.26 ?  76  LYS   A HG3  1 
ATOM   1776 H  HD2  . LYS   A 1 76  ? 35.898 -7.586  -5.562  1.00 20.82 ?  76  LYS   A HD2  1 
ATOM   1777 H  HD3  . LYS   A 1 76  ? 35.623 -7.946  -7.089  1.00 20.82 ?  76  LYS   A HD3  1 
ATOM   1778 H  HE2  . LYS   A 1 76  ? 37.730 -7.127  -7.649  1.00 23.87 ?  76  LYS   A HE2  1 
ATOM   1779 H  HE3  . LYS   A 1 76  ? 38.004 -6.802  -6.118  1.00 23.87 ?  76  LYS   A HE3  1 
ATOM   1780 H  HZ1  . LYS   A 1 76  ? 38.980 -8.755  -6.702  1.00 24.85 ?  76  LYS   A HZ1  1 
ATOM   1781 H  HZ2  . LYS   A 1 76  ? 37.961 -9.030  -5.710  1.00 24.85 ?  76  LYS   A HZ2  1 
ATOM   1782 H  HZ3  . LYS   A 1 76  ? 37.711 -9.327  -7.106  1.00 24.85 ?  76  LYS   A HZ3  1 
ATOM   1783 N  N    . VAL   A 1 77  ? 31.207 -4.446  -7.389  1.00 12.18 ?  77  VAL   A N    1 
ATOM   1784 C  CA   . VAL   A 1 77  ? 29.801 -4.838  -7.297  1.00 12.11 ?  77  VAL   A CA   1 
ATOM   1785 C  C    . VAL   A 1 77  ? 29.743 -6.291  -6.848  1.00 11.90 ?  77  VAL   A C    1 
ATOM   1786 O  O    . VAL   A 1 77  ? 30.408 -7.158  -7.426  1.00 12.13 ?  77  VAL   A O    1 
ATOM   1787 C  CB   . VAL   A 1 77  ? 29.073 -4.625  -8.635  1.00 13.41 ?  77  VAL   A CB   1 
ATOM   1788 C  CG1  . VAL   A 1 77  ? 27.617 -5.069  -8.523  1.00 14.15 ?  77  VAL   A CG1  1 
ATOM   1789 C  CG2  . VAL   A 1 77  ? 29.148 -3.167  -9.071  1.00 14.74 ?  77  VAL   A CG2  1 
ATOM   1790 H  H    . VAL   A 1 77  ? 31.479 -4.206  -8.168  1.00 14.65 ?  77  VAL   A H    1 
ATOM   1791 H  HA   . VAL   A 1 77  ? 29.364 -4.292  -6.626  1.00 14.56 ?  77  VAL   A HA   1 
ATOM   1792 H  HB   . VAL   A 1 77  ? 29.504 -5.160  -9.321  1.00 16.12 ?  77  VAL   A HB   1 
ATOM   1793 H  HG11 . VAL   A 1 77  ? 27.142 -4.785  -9.319  1.00 17.01 ?  77  VAL   A HG11 1 
ATOM   1794 H  HG12 . VAL   A 1 77  ? 27.587 -6.033  -8.444  1.00 17.01 ?  77  VAL   A HG12 1 
ATOM   1795 H  HG13 . VAL   A 1 77  ? 27.225 -4.656  -7.738  1.00 17.01 ?  77  VAL   A HG13 1 
ATOM   1796 H  HG21 . VAL   A 1 77  ? 28.643 -3.059  -9.892  1.00 17.72 ?  77  VAL   A HG21 1 
ATOM   1797 H  HG22 . VAL   A 1 77  ? 28.766 -2.612  -8.372  1.00 17.72 ?  77  VAL   A HG22 1 
ATOM   1798 H  HG23 . VAL   A 1 77  ? 30.075 -2.926  -9.216  1.00 17.72 ?  77  VAL   A HG23 1 
ATOM   1799 N  N    . GLY   A 1 78  ? 28.957 -6.566  -5.803  1.00 11.47 ?  78  GLY   A N    1 
ATOM   1800 C  CA   . GLY   A 1 78  ? 28.949 -7.858  -5.148  1.00 11.79 ?  78  GLY   A CA   1 
ATOM   1801 C  C    . GLY   A 1 78  ? 29.869 -7.947  -3.951  1.00 11.41 ?  78  GLY   A C    1 
ATOM   1802 O  O    . GLY   A 1 78  ? 29.817 -8.948  -3.223  1.00 12.12 ?  78  GLY   A O    1 
ATOM   1803 H  H    . GLY   A 1 78  ? 28.405 -5.997  -5.460  1.00 13.79 ?  78  GLY   A H    1 
ATOM   1804 H  HA2  . GLY   A 1 78  ? 28.047 -8.053  -4.855  1.00 14.18 ?  78  GLY   A HA2  1 
ATOM   1805 H  HA3  . GLY   A 1 78  ? 29.213 -8.535  -5.790  1.00 14.18 ?  78  GLY   A HA3  1 
ATOM   1806 N  N    . GLY   A 1 79  ? 30.719 -6.941  -3.735  1.00 11.49 ?  79  GLY   A N    1 
ATOM   1807 C  CA   . GLY   A 1 79  ? 31.686 -6.948  -2.662  1.00 11.71 ?  79  GLY   A CA   1 
ATOM   1808 C  C    . GLY   A 1 79  ? 31.246 -6.149  -1.447  1.00 11.01 ?  79  GLY   A C    1 
ATOM   1809 O  O    . GLY   A 1 79  ? 30.123 -5.644  -1.358  1.00 11.54 ?  79  GLY   A O    1 
ATOM   1810 H  H    . GLY   A 1 79  ? 30.755 -6.226  -4.213  1.00 13.82 ?  79  GLY   A H    1 
ATOM   1811 H  HA2  . GLY   A 1 79  ? 31.835 -7.873  -2.378  1.00 14.09 ?  79  GLY   A HA2  1 
ATOM   1812 H  HA3  . GLY   A 1 79  ? 32.524 -6.593  -2.976  1.00 14.09 ?  79  GLY   A HA3  1 
ATOM   1813 N  N    . SER   A 1 80  ? 32.161 -6.048  -0.484  1.00 11.81 ?  80  SER   A N    1 
ATOM   1814 C  CA   . SER   A 1 80  ? 31.849 -5.426  0.793   1.00 10.97 ?  80  SER   A CA   1 
ATOM   1815 C  C    . SER   A 1 80  ? 33.124 -4.977  1.486   1.00 11.18 ?  80  SER   A C    1 
ATOM   1816 O  O    . SER   A 1 80  ? 34.240 -5.401  1.149   1.00 12.41 ?  80  SER   A O    1 
ATOM   1817 C  CB   . SER   A 1 80  ? 31.100 -6.400  1.715   1.00 12.06 ?  80  SER   A CB   1 
ATOM   1818 O  OG   . SER   A 1 80  ? 31.942 -7.446  2.186   1.00 13.93 ?  80  SER   A OG   1 
ATOM   1819 H  H    . SER   A 1 80  ? 32.972 -6.311  -0.559  1.00 14.21 ?  80  SER   A H    1 
ATOM   1820 H  HA   . SER   A 1 80  ? 31.291 -4.647  0.630   1.00 13.19 ?  80  SER   A HA   1 
ATOM   1821 H  HB2  . SER   A 1 80  ? 30.752 -5.907  2.472   1.00 14.51 ?  80  SER   A HB2  1 
ATOM   1822 H  HB3  . SER   A 1 80  ? 30.364 -6.795  1.215   1.00 14.51 ?  80  SER   A HB3  1 
ATOM   1823 H  HG   . SER   A 1 80  ? 32.251 -7.869  1.529   1.00 16.75 ?  80  SER   A HG   1 
ATOM   1824 N  N    . CYS   A 1 81  ? 32.934 -4.133  2.497   1.00 10.87 ?  81  CYS   A N    1 
ATOM   1825 C  CA   . CYS   A 1 81  ? 33.988 -3.842  3.456   1.00 11.03 ?  81  CYS   A CA   1 
ATOM   1826 C  C    . CYS   A 1 81  ? 33.353 -3.608  4.819   1.00 10.84 ?  81  CYS   A C    1 
ATOM   1827 O  O    . CYS   A 1 81  ? 32.187 -3.209  4.916   1.00 11.79 ?  81  CYS   A O    1 
ATOM   1828 C  CB   . CYS   A 1 81  ? 34.852 -2.651  3.025   1.00 11.77 ?  81  CYS   A CB   1 
ATOM   1829 S  SG   . CYS   A 1 81  ? 33.954 -1.070  3.054   1.00 11.69 ?  81  CYS   A SG   1 
ATOM   1830 H  H    . CYS   A 1 81  ? 32.200 -3.707  2.649   1.00 13.07 ?  81  CYS   A H    1 
ATOM   1831 H  HA   . CYS   A 1 81  ? 34.570 -4.613  3.524   1.00 13.27 ?  81  CYS   A HA   1 
ATOM   1832 H  HB2  . CYS   A 1 81  ? 35.616 -2.581  3.623   1.00 14.15 ?  81  CYS   A HB2  1 
ATOM   1833 H  HB3  . CYS   A 1 81  ? 35.170 -2.806  2.115   1.00 14.15 ?  81  CYS   A HB3  1 
ATOM   1834 H  HG   . CYS   A 1 81  ? 34.696 -0.190  2.702   1.00 14.07 ?  81  CYS   A HG   1 
ATOM   1835 N  N    . VAL   A 1 82  ? 34.131 -3.864  5.869   1.00 11.29 ?  82  VAL   A N    1 
ATOM   1836 C  CA   . VAL   A 1 82  ? 33.709 -3.627  7.244   1.00 11.95 ?  82  VAL   A CA   1 
ATOM   1837 C  C    . VAL   A 1 82  ? 34.309 -2.308  7.712   1.00 11.88 ?  82  VAL   A C    1 
ATOM   1838 O  O    . VAL   A 1 82  ? 35.533 -2.127  7.692   1.00 12.61 ?  82  VAL   A O    1 
ATOM   1839 C  CB   . VAL   A 1 82  ? 34.140 -4.765  8.182   1.00 13.29 ?  82  VAL   A CB   1 
ATOM   1840 C  CG1  . VAL   A 1 82  ? 33.697 -4.464  9.609   1.00 14.56 ?  82  VAL   A CG1  1 
ATOM   1841 C  CG2  . VAL   A 1 82  ? 33.586 -6.095  7.714   1.00 14.34 ?  82  VAL   A CG2  1 
ATOM   1842 H  H    . VAL   A 1 82  ? 34.927 -4.202  5.806   1.00 13.58 ?  82  VAL   A H    1 
ATOM   1843 H  HA   . VAL   A 1 82  ? 32.742 -3.552  7.273   1.00 14.38 ?  82  VAL   A HA   1 
ATOM   1844 H  HB   . VAL   A 1 82  ? 35.108 -4.821  8.180   1.00 15.98 ?  82  VAL   A HB   1 
ATOM   1845 H  HG11 . VAL   A 1 82  ? 33.784 -5.269  10.143  1.00 17.51 ?  82  VAL   A HG11 1 
ATOM   1846 H  HG12 . VAL   A 1 82  ? 34.255 -3.761  9.981   1.00 17.51 ?  82  VAL   A HG12 1 
ATOM   1847 H  HG13 . VAL   A 1 82  ? 32.768 -4.176  9.600   1.00 17.51 ?  82  VAL   A HG13 1 
ATOM   1848 H  HG21 . VAL   A 1 82  ? 33.843 -6.783  8.349   1.00 17.24 ?  82  VAL   A HG21 1 
ATOM   1849 H  HG22 . VAL   A 1 82  ? 32.620 -6.035  7.664   1.00 17.24 ?  82  VAL   A HG22 1 
ATOM   1850 H  HG23 . VAL   A 1 82  ? 33.953 -6.299  6.840   1.00 17.24 ?  82  VAL   A HG23 1 
ATOM   1851 N  N    . LEU   A 1 83  ? 33.455 -1.386  8.139   1.00 11.42 ?  83  LEU   A N    1 
ATOM   1852 C  CA   . LEU   A 1 83  ? 33.869 -0.115  8.715   1.00 11.51 ?  83  LEU   A CA   1 
ATOM   1853 C  C    . LEU   A 1 83  ? 33.162 0.056   10.055  1.00 11.60 ?  83  LEU   A C    1 
ATOM   1854 O  O    . LEU   A 1 83  ? 32.447 -0.838  10.523  1.00 12.07 ?  83  LEU   A O    1 
ATOM   1855 C  CB   . LEU   A 1 83  ? 33.601 1.043   7.738   1.00 11.85 ?  83  LEU   A CB   1 
ATOM   1856 C  CG   . LEU   A 1 83  ? 34.495 1.043   6.488   1.00 12.64 ?  83  LEU   A CG   1 
ATOM   1857 C  CD1  . LEU   A 1 83  ? 34.044 2.077   5.478   1.00 12.95 ?  83  LEU   A CD1  1 
ATOM   1858 C  CD2  . LEU   A 1 83  ? 35.966 1.271   6.853   1.00 13.57 ?  83  LEU   A CD2  1 
ATOM   1859 H  H    . LEU   A 1 83  ? 32.601 -1.476  8.097   1.00 13.73 ?  83  LEU   A H    1 
ATOM   1860 H  HA   . LEU   A 1 83  ? 34.822 -0.136  8.883   1.00 13.84 ?  83  LEU   A HA   1 
ATOM   1861 H  HB2  . LEU   A 1 83  ? 32.678 0.997   7.436   1.00 14.26 ?  83  LEU   A HB2  1 
ATOM   1862 H  HB3  . LEU   A 1 83  ? 33.744 1.888   8.198   1.00 14.26 ?  83  LEU   A HB3  1 
ATOM   1863 H  HG   . LEU   A 1 83  ? 34.431 0.171   6.069   1.00 15.20 ?  83  LEU   A HG   1 
ATOM   1864 H  HD11 . LEU   A 1 83  ? 34.628 2.033   4.702   1.00 15.57 ?  83  LEU   A HD11 1 
ATOM   1865 H  HD12 . LEU   A 1 83  ? 33.131 1.875   5.211   1.00 15.57 ?  83  LEU   A HD12 1 
ATOM   1866 H  HD13 . LEU   A 1 83  ? 34.087 2.954   5.879   1.00 15.57 ?  83  LEU   A HD13 1 
ATOM   1867 H  HD21 . LEU   A 1 83  ? 36.475 1.416   6.037   1.00 16.31 ?  83  LEU   A HD21 1 
ATOM   1868 H  HD22 . LEU   A 1 83  ? 36.035 2.052   7.425   1.00 16.31 ?  83  LEU   A HD22 1 
ATOM   1869 H  HD23 . LEU   A 1 83  ? 36.306 0.491   7.317   1.00 16.31 ?  83  LEU   A HD23 1 
ATOM   1870 N  N    . SER   A 1 84  ? 33.367 1.210   10.683  1.00 12.13 ?  84  SER   A N    1 
ATOM   1871 C  CA   . SER   A 1 84  ? 32.725 1.465   11.963  1.00 12.28 ?  84  SER   A CA   1 
ATOM   1872 C  C    . SER   A 1 84  ? 31.205 1.547   11.826  1.00 12.18 ?  84  SER   A C    1 
ATOM   1873 O  O    . SER   A 1 84  ? 30.670 2.014   10.821  1.00 12.31 ?  84  SER   A O    1 
ATOM   1874 C  CB   . SER   A 1 84  ? 33.231 2.782   12.546  1.00 13.43 ?  84  SER   A CB   1 
ATOM   1875 O  OG   . SER   A 1 84  ? 32.587 3.066   13.773  1.00 14.35 ?  84  SER   A OG   1 
ATOM   1876 H  H    . SER   A 1 84  ? 33.860 1.854   10.387  1.00 14.59 ?  84  SER   A H    1 
ATOM   1877 H  HA   . SER   A 1 84  ? 32.946 0.749   12.576  1.00 14.77 ?  84  SER   A HA   1 
ATOM   1878 H  HB2  . SER   A 1 84  ? 34.188 2.714   12.693  1.00 16.15 ?  84  SER   A HB2  1 
ATOM   1879 H  HB3  . SER   A 1 84  ? 33.045 3.496   11.913  1.00 16.15 ?  84  SER   A HB3  1 
ATOM   1880 H  HG   . SER   A 1 84  ? 32.873 3.793   14.082  1.00 17.25 ?  84  SER   A HG   1 
ATOM   1881 N  N    . GLY   A 1 85  ? 30.508 1.125   12.878  1.00 12.89 ?  85  GLY   A N    1 
ATOM   1882 C  CA   . GLY   A 1 85  ? 29.084 1.358   12.975  1.00 13.82 ?  85  GLY   A CA   1 
ATOM   1883 C  C    . GLY   A 1 85  ? 28.714 2.672   13.623  1.00 13.38 ?  85  GLY   A C    1 
ATOM   1884 O  O    . GLY   A 1 85  ? 27.523 2.979   13.749  1.00 13.87 ?  85  GLY   A O    1 
ATOM   1885 H  H    . GLY   A 1 85  ? 30.847 0.698   13.544  1.00 15.50 ?  85  GLY   A H    1 
ATOM   1886 H  HA2  . GLY   A 1 85  ? 28.701 1.340   12.085  1.00 16.62 ?  85  GLY   A HA2  1 
ATOM   1887 H  HA3  . GLY   A 1 85  ? 28.684 0.648   13.492  1.00 16.62 ?  85  GLY   A HA3  1 
ATOM   1888 N  N    . HIS   A 1 86  ? 29.699 3.455   14.055  1.00 13.29 ?  86  HIS   A N    1 
ATOM   1889 C  CA   . HIS   A 1 86  ? 29.469 4.790   14.621  1.00 13.59 ?  86  HIS   A CA   1 
ATOM   1890 C  C    . HIS   A 1 86  ? 28.493 4.666   15.784  1.00 14.54 ?  86  HIS   A C    1 
ATOM   1891 O  O    . HIS   A 1 86  ? 28.690 3.792   16.644  1.00 15.88 ?  86  HIS   A O    1 
ATOM   1892 C  CB   . HIS   A 1 86  ? 29.077 5.763   13.516  1.00 13.38 ?  86  HIS   A CB   1 
ATOM   1893 C  CG   . HIS   A 1 86  ? 30.127 5.869   12.472  1.00 13.26 ?  86  HIS   A CG   1 
ATOM   1894 N  ND1  . HIS   A 1 86  ? 31.217 6.704   12.605  1.00 14.54 ?  86  HIS   A ND1  1 
ATOM   1895 C  CD2  . HIS   A 1 86  ? 30.306 5.182   11.323  1.00 12.99 ?  86  HIS   A CD2  1 
ATOM   1896 C  CE1  . HIS   A 1 86  ? 32.007 6.543   11.559  1.00 14.00 ?  86  HIS   A CE1  1 
ATOM   1897 N  NE2  . HIS   A 1 86  ? 31.483 5.620   10.774  1.00 13.35 ?  86  HIS   A NE2  1 
ATOM   1898 H  H    . HIS   A 1 86  ? 30.526 3.237   14.042  1.00 15.99 ?  86  HIS   A H    1 
ATOM   1899 H  HA   . HIS   A 1 86  ? 30.304 5.113   14.990  1.00 16.34 ?  86  HIS   A HA   1 
ATOM   1900 H  HB2  . HIS   A 1 86  ? 28.256 5.461   13.094  1.00 16.08 ?  86  HIS   A HB2  1 
ATOM   1901 H  HB3  . HIS   A 1 86  ? 28.943 6.650   13.896  1.00 16.08 ?  86  HIS   A HB3  1 
ATOM   1902 H  HD2  . HIS   A 1 86  ? 29.742 4.525   10.971  1.00 15.62 ?  86  HIS   A HD2  1 
ATOM   1903 H  HE1  . HIS   A 1 86  ? 32.799 7.000   11.392  1.00 16.83 ?  86  HIS   A HE1  1 
ATOM   1904 H  HE2  . HIS   A 1 86  ? 31.815 5.348   10.020  1.00 16.05 ?  86  HIS   A HE2  1 
ATOM   1905 N  N    . ASN   A 1 87  ? 27.476 5.512   15.862  1.00 15.35 ?  87  ASN   A N    1 
ATOM   1906 C  CA   . ASN   A 1 87  ? 26.497 5.496   16.933  1.00 16.68 ?  87  ASN   A CA   1 
ATOM   1907 C  C    . ASN   A 1 87  ? 25.381 4.490   16.701  1.00 17.75 ?  87  ASN   A C    1 
ATOM   1908 O  O    . ASN   A 1 87  ? 24.464 4.417   17.523  1.00 20.02 ?  87  ASN   A O    1 
ATOM   1909 C  CB   . ASN   A 1 87  ? 25.892 6.899   17.100  1.00 17.88 ?  87  ASN   A CB   1 
ATOM   1910 C  CG   . ASN   A 1 87  ? 25.371 7.477   15.789  1.00 18.51 ?  87  ASN   A CG   1 
ATOM   1911 O  OD1  . ASN   A 1 87  ? 26.001 7.355   14.742  1.00 18.78 ?  87  ASN   A OD1  1 
ATOM   1912 N  ND2  . ASN   A 1 87  ? 24.216 8.119   15.849  1.00 19.65 ?  87  ASN   A ND2  1 
ATOM   1913 H  H    . ASN   A 1 87  ? 27.325 6.129   15.285  1.00 18.45 ?  87  ASN   A H    1 
ATOM   1914 H  HA   . ASN   A 1 87  ? 26.930 5.256   17.768  1.00 20.05 ?  87  ASN   A HA   1 
ATOM   1915 H  HB2  . ASN   A 1 87  ? 25.148 6.851   17.730  1.00 21.49 ?  87  ASN   A HB2  1 
ATOM   1916 H  HB3  . ASN   A 1 87  ? 26.573 7.494   17.446  1.00 21.49 ?  87  ASN   A HB3  1 
ATOM   1917 H  HD21 . ASN   A 1 87  ? 23.883 8.462   15.137  1.00 23.61 ?  87  ASN   A HD21 1 
ATOM   1918 H  HD22 . ASN   A 1 87  ? 23.802 8.197   16.600  1.00 23.61 ?  87  ASN   A HD22 1 
ATOM   1919 N  N    . LEU   A 1 88  ? 25.438 3.707   15.626  1.00 16.58 ?  88  LEU   A N    1 
ATOM   1920 C  CA   . LEU   A 1 88  ? 24.328 2.842   15.237  1.00 16.30 ?  88  LEU   A CA   1 
ATOM   1921 C  C    . LEU   A 1 88  ? 24.551 1.364   15.534  1.00 16.06 ?  88  LEU   A C    1 
ATOM   1922 O  O    . LEU   A 1 88  ? 23.576 0.630   15.717  1.00 17.35 ?  88  LEU   A O    1 
ATOM   1923 C  CB   . LEU   A 1 88  ? 24.053 3.002   13.738  1.00 16.89 ?  88  LEU   A CB   1 
ATOM   1924 C  CG   . LEU   A 1 88  ? 23.746 4.426   13.269  1.00 17.98 ?  88  LEU   A CG   1 
ATOM   1925 C  CD1  . LEU   A 1 88  ? 23.530 4.452   11.766  1.00 18.33 ?  88  LEU   A CD1  1 
ATOM   1926 C  CD2  . LEU   A 1 88  ? 22.536 5.001   13.994  1.00 19.83 ?  88  LEU   A CD2  1 
ATOM   1927 H  H    . LEU   A 1 88  ? 26.119 3.657   15.108  1.00 19.93 ?  88  LEU   A H    1 
ATOM   1928 H  HA   . LEU   A 1 88  ? 23.534 3.118   15.715  1.00 19.59 ?  88  LEU   A HA   1 
ATOM   1929 H  HB2  . LEU   A 1 88  ? 24.828 2.698   13.244  1.00 20.30 ?  88  LEU   A HB2  1 
ATOM   1930 H  HB3  . LEU   A 1 88  ? 23.286 2.454   13.507  1.00 20.30 ?  88  LEU   A HB3  1 
ATOM   1931 H  HG   . LEU   A 1 88  ? 24.508 4.991   13.467  1.00 21.61 ?  88  LEU   A HG   1 
ATOM   1932 H  HD11 . LEU   A 1 88  ? 23.341 5.364   11.489  1.00 22.03 ?  88  LEU   A HD11 1 
ATOM   1933 H  HD12 . LEU   A 1 88  ? 24.334 4.135   11.325  1.00 22.03 ?  88  LEU   A HD12 1 
ATOM   1934 H  HD13 . LEU   A 1 88  ? 22.781 3.877   11.542  1.00 22.03 ?  88  LEU   A HD13 1 
ATOM   1935 H  HD21 . LEU   A 1 88  ? 22.305 5.852   13.589  1.00 23.83 ?  88  LEU   A HD21 1 
ATOM   1936 H  HD22 . LEU   A 1 88  ? 21.797 4.382   13.913  1.00 23.83 ?  88  LEU   A HD22 1 
ATOM   1937 H  HD23 . LEU   A 1 88  ? 22.764 5.131   14.928  1.00 23.83 ?  88  LEU   A HD23 1 
ATOM   1938 N  N    . ALA   A 1 89  ? 25.801 0.918   15.570  1.00 15.26 ?  89  ALA   A N    1 
ATOM   1939 C  CA   . ALA   A 1 89  ? 26.153 -0.492  15.667  1.00 15.03 ?  89  ALA   A CA   1 
ATOM   1940 C  C    . ALA   A 1 89  ? 27.640 -0.547  15.975  1.00 15.16 ?  89  ALA   A C    1 
ATOM   1941 O  O    . ALA   A 1 89  ? 28.344 0.456   15.863  1.00 16.11 ?  89  ALA   A O    1 
ATOM   1942 C  CB   . ALA   A 1 89  ? 25.871 -1.213  14.349  1.00 14.60 ?  89  ALA   A CB   1 
ATOM   1943 H  H    . ALA   A 1 89  ? 26.486 1.432   15.530  1.00 18.35 ?  89  ALA   A H    1 
ATOM   1944 H  HA   . ALA   A 1 89  ? 25.656 -0.915  16.384  1.00 18.07 ?  89  ALA   A HA   1 
ATOM   1945 H  HB1  . ALA   A 1 89  ? 26.138 -2.145  14.436  1.00 17.56 ?  89  ALA   A HB1  1 
ATOM   1946 H  HB2  . ALA   A 1 89  ? 24.919 -1.165  14.156  1.00 17.56 ?  89  ALA   A HB2  1 
ATOM   1947 H  HB3  . ALA   A 1 89  ? 26.375 -0.792  13.640  1.00 17.56 ?  89  ALA   A HB3  1 
ATOM   1948 N  N    . LYS   A 1 90  ? 28.130 -1.725  16.349  1.00 15.67 ?  90  LYS   A N    1 
ATOM   1949 C  CA   . LYS   A 1 90  ? 29.575 -1.860  16.492  1.00 16.53 ?  90  LYS   A CA   1 
ATOM   1950 C  C    . LYS   A 1 90  ? 30.265 -1.674  15.143  1.00 15.37 ?  90  LYS   A C    1 
ATOM   1951 O  O    . LYS   A 1 90  ? 31.198 -0.866  15.008  1.00 16.35 ?  90  LYS   A O    1 
ATOM   1952 C  CB   . LYS   A 1 90  ? 29.926 -3.209  17.120  1.00 18.96 ?  90  LYS   A CB   1 
ATOM   1953 C  CG   . LYS   A 1 90  ? 31.404 -3.349  17.439  1.00 23.65 ?  90  LYS   A CG   1 
ATOM   1954 C  CD   . LYS   A 1 90  ? 31.659 -4.554  18.330  1.00 28.84 ?  90  LYS   A CD   1 
ATOM   1955 C  CE   . LYS   A 1 90  ? 33.076 -4.558  18.884  1.00 32.69 ?  90  LYS   A CE   1 
ATOM   1956 N  NZ   . LYS   A 1 90  ? 34.083 -4.995  17.879  1.00 34.82 ?  90  LYS   A NZ   1 
ATOM   1957 H  H    . LYS   A 1 90  ? 27.669 -2.427  16.518  1.00 18.83 ?  90  LYS   A H    1 
ATOM   1958 H  HA   . LYS   A 1 90  ? 29.897 -1.163  17.084  1.00 19.86 ?  90  LYS   A HA   1 
ATOM   1959 H  HB2  . LYS   A 1 90  ? 29.428 -3.305  17.950  1.00 22.79 ?  90  LYS   A HB2  1 
ATOM   1960 H  HB3  . LYS   A 1 90  ? 29.681 -3.916  16.506  1.00 22.79 ?  90  LYS   A HB3  1 
ATOM   1961 H  HG2  . LYS   A 1 90  ? 31.901 -3.467  16.615  1.00 28.41 ?  90  LYS   A HG2  1 
ATOM   1962 H  HG3  . LYS   A 1 90  ? 31.709 -2.554  17.906  1.00 28.41 ?  90  LYS   A HG3  1 
ATOM   1963 H  HD2  . LYS   A 1 90  ? 31.041 -4.537  19.078  1.00 34.64 ?  90  LYS   A HD2  1 
ATOM   1964 H  HD3  . LYS   A 1 90  ? 31.533 -5.366  17.812  1.00 34.64 ?  90  LYS   A HD3  1 
ATOM   1965 H  HE2  . LYS   A 1 90  ? 33.307 -3.660  19.170  1.00 39.26 ?  90  LYS   A HE2  1 
ATOM   1966 H  HE3  . LYS   A 1 90  ? 33.120 -5.167  19.637  1.00 39.26 ?  90  LYS   A HE3  1 
ATOM   1967 H  HZ1  . LYS   A 1 90  ? 33.895 -5.819  17.600  1.00 41.81 ?  90  LYS   A HZ1  1 
ATOM   1968 H  HZ2  . LYS   A 1 90  ? 34.075 -4.443  17.182  1.00 41.81 ?  90  LYS   A HZ2  1 
ATOM   1969 H  HZ3  . LYS   A 1 90  ? 34.896 -4.991  18.243  1.00 41.81 ?  90  LYS   A HZ3  1 
ATOM   1970 N  N    . HIS   A 1 91  ? 29.796 -2.399  14.129  1.00 13.58 ?  91  HIS   A N    1 
ATOM   1971 C  CA   . HIS   A 1 91  ? 30.361 -2.383  12.794  1.00 13.10 ?  91  HIS   A CA   1 
ATOM   1972 C  C    . HIS   A 1 91  ? 29.264 -2.111  11.778  1.00 11.93 ?  91  HIS   A C    1 
ATOM   1973 O  O    . HIS   A 1 91  ? 28.098 -2.478  11.977  1.00 12.46 ?  91  HIS   A O    1 
ATOM   1974 C  CB   . HIS   A 1 91  ? 30.965 -3.747  12.427  1.00 15.28 ?  91  HIS   A CB   1 
ATOM   1975 C  CG   . HIS   A 1 91  ? 31.953 -4.268  13.423  1.00 19.44 ?  91  HIS   A CG   1 
ATOM   1976 N  ND1  . HIS   A 1 91  ? 33.237 -3.780  13.522  1.00 21.36 ?  91  HIS   A ND1  1 
ATOM   1977 C  CD2  . HIS   A 1 91  ? 31.852 -5.249  14.351  1.00 21.10 ?  91  HIS   A CD2  1 
ATOM   1978 C  CE1  . HIS   A 1 91  ? 33.884 -4.432  14.473  1.00 22.22 ?  91  HIS   A CE1  1 
ATOM   1979 N  NE2  . HIS   A 1 91  ? 33.064 -5.329  14.992  1.00 22.42 ?  91  HIS   A NE2  1 
ATOM   1980 H  H    . HIS   A 1 91  ? 29.123 -2.945  14.206  1.00 16.33 ?  91  HIS   A H    1 
ATOM   1981 H  HA   . HIS   A 1 91  ? 31.042 -1.707  12.725  1.00 15.75 ?  91  HIS   A HA   1 
ATOM   1982 H  HB2  . HIS   A 1 91  ? 30.250 -4.404  12.360  1.00 18.37 ?  91  HIS   A HB2  1 
ATOM   1983 H  HB3  . HIS   A 1 91  ? 31.419 -3.672  11.575  1.00 18.37 ?  91  HIS   A HB3  1 
ATOM   1984 H  HD1  . HIS   A 1 91  ? 33.568 -3.149  13.037  1.00 25.66 ?  91  HIS   A HD1  1 
ATOM   1985 H  HD2  . HIS   A 1 91  ? 31.107 -5.770  14.526  1.00 25.36 ?  91  HIS   A HD2  1 
ATOM   1986 H  HE1  . HIS   A 1 91  ? 34.768 -4.279  14.729  1.00 26.70 ?  91  HIS   A HE1  1 
ATOM   1987 N  N    . CYS   A 1 92  ? 29.662 -1.505  10.662  1.00 11.56 ?  92  CYS   A N    1 
ATOM   1988 C  CA   . CYS   A 1 92  ? 28.825 -1.433  9.472   1.00 11.47 ?  92  CYS   A CA   1 
ATOM   1989 C  C    . CYS   A 1 92  ? 29.469 -2.257  8.364   1.00 11.00 ?  92  CYS   A C    1 
ATOM   1990 O  O    . CYS   A 1 92  ? 30.626 -2.004  7.991   1.00 11.56 ?  92  CYS   A O    1 
ATOM   1991 C  CB   . CYS   A 1 92  ? 28.617 0.009   9.008   1.00 11.59 ?  92  CYS   A CB   1 
ATOM   1992 S  SG   . CYS   A 1 92  ? 27.578 0.115   7.512   1.00 11.21 ?  92  CYS   A SG   1 
ATOM   1993 H  H    . CYS   A 1 92  ? 30.428 -1.119  10.571  1.00 13.91 ?  92  CYS   A H    1 
ATOM   1994 H  HA   . CYS   A 1 92  ? 27.957 -1.812  9.670   1.00 13.80 ?  92  CYS   A HA   1 
ATOM   1995 H  HB2  . CYS   A 1 92  ? 28.182 0.513   9.713   1.00 13.94 ?  92  CYS   A HB2  1 
ATOM   1996 H  HB3  . CYS   A 1 92  ? 29.480 0.405   8.801   1.00 13.94 ?  92  CYS   A HB3  1 
ATOM   1997 H  HG   . CYS   A 1 92  ? 27.440 1.265   7.207   1.00 13.48 ?  92  CYS   A HG   1 
ATOM   1998 N  N    . LEU   A 1 93  ? 28.730 -3.246  7.863   1.00 10.84 ?  93  LEU   A N    1 
ATOM   1999 C  CA   . LEU   A 1 93  ? 29.128 -4.004  6.682   1.00 10.51 ?  93  LEU   A CA   1 
ATOM   2000 C  C    . LEU   A 1 93  ? 28.527 -3.306  5.467   1.00 9.82  ?  93  LEU   A C    1 
ATOM   2001 O  O    . LEU   A 1 93  ? 27.311 -3.369  5.244   1.00 10.20 ?  93  LEU   A O    1 
ATOM   2002 C  CB   . LEU   A 1 93  ? 28.647 -5.449  6.792   1.00 10.97 ?  93  LEU   A CB   1 
ATOM   2003 C  CG   . LEU   A 1 93  ? 29.031 -6.345  5.618   1.00 11.05 ?  93  LEU   A CG   1 
ATOM   2004 C  CD1  . LEU   A 1 93  ? 30.541 -6.586  5.585   1.00 11.95 ?  93  LEU   A CD1  1 
ATOM   2005 C  CD2  . LEU   A 1 93  ? 28.281 -7.677  5.664   1.00 12.09 ?  93  LEU   A CD2  1 
ATOM   2006 H  H    . LEU   A 1 93  ? 27.976 -3.498  8.207   1.00 13.04 ?  93  LEU   A H    1 
ATOM   2007 H  HA   . LEU   A 1 93  ? 30.088 -3.993  6.609   1.00 12.65 ?  93  LEU   A HA   1 
ATOM   2008 H  HB2  . LEU   A 1 93  ? 29.028 -5.839  7.599   1.00 13.19 ?  93  LEU   A HB2  1 
ATOM   2009 H  HB3  . LEU   A 1 93  ? 27.680 -5.452  6.861   1.00 13.19 ?  93  LEU   A HB3  1 
ATOM   2010 H  HG   . LEU   A 1 93  ? 28.789 -5.904  4.797   1.00 13.29 ?  93  LEU   A HG   1 
ATOM   2011 H  HD11 . LEU   A 1 93  ? 30.752 -7.206  4.871   1.00 14.37 ?  93  LEU   A HD11 1 
ATOM   2012 H  HD12 . LEU   A 1 93  ? 30.997 -5.741  5.436   1.00 14.37 ?  93  LEU   A HD12 1 
ATOM   2013 H  HD13 . LEU   A 1 93  ? 30.826 -6.963  6.439   1.00 14.37 ?  93  LEU   A HD13 1 
ATOM   2014 H  HD21 . LEU   A 1 93  ? 28.556 -8.220  4.904   1.00 14.55 ?  93  LEU   A HD21 1 
ATOM   2015 H  HD22 . LEU   A 1 93  ? 28.498 -8.140  6.490   1.00 14.55 ?  93  LEU   A HD22 1 
ATOM   2016 H  HD23 . LEU   A 1 93  ? 27.329 -7.507  5.619   1.00 14.55 ?  93  LEU   A HD23 1 
ATOM   2017 N  N    . HIS   A 1 94  ? 29.369 -2.607  4.707   1.00 9.88  ?  94  HIS   A N    1 
ATOM   2018 C  CA   . HIS   A 1 94  ? 28.941 -1.935  3.483   1.00 9.95  ?  94  HIS   A CA   1 
ATOM   2019 C  C    . HIS   A 1 94  ? 28.946 -2.967  2.367   1.00 9.92  ?  94  HIS   A C    1 
ATOM   2020 O  O    . HIS   A 1 94  ? 30.011 -3.479  2.013   1.00 11.29 ?  94  HIS   A O    1 
ATOM   2021 C  CB   . HIS   A 1 94  ? 29.889 -0.786  3.150   1.00 10.13 ?  94  HIS   A CB   1 
ATOM   2022 C  CG   . HIS   A 1 94  ? 29.877 0.308   4.163   1.00 10.08 ?  94  HIS   A CG   1 
ATOM   2023 N  ND1  . HIS   A 1 94  ? 29.005 1.376   4.104   1.00 10.08 ?  94  HIS   A ND1  1 
ATOM   2024 C  CD2  . HIS   A 1 94  ? 30.619 0.480   5.279   1.00 10.72 ?  94  HIS   A CD2  1 
ATOM   2025 C  CE1  . HIS   A 1 94  ? 29.217 2.156   5.146   1.00 10.41 ?  94  HIS   A CE1  1 
ATOM   2026 N  NE2  . HIS   A 1 94  ? 30.193 1.639   5.872   1.00 10.65 ?  94  HIS   A NE2  1 
ATOM   2027 H  H    . HIS   A 1 94  ? 30.205 -2.502  4.886   1.00 11.89 ?  94  HIS   A H    1 
ATOM   2028 H  HA   . HIS   A 1 94  ? 28.038 -1.591  3.592   1.00 11.97 ?  94  HIS   A HA   1 
ATOM   2029 H  HB2  . HIS   A 1 94  ? 30.787 -1.130  3.094   1.00 12.19 ?  94  HIS   A HB2  1 
ATOM   2030 H  HB3  . HIS   A 1 94  ? 29.620 -0.402  2.300   1.00 12.19 ?  94  HIS   A HB3  1 
ATOM   2031 H  HD2  . HIS   A 1 94  ? 31.289 -0.080  5.592   1.00 12.89 ?  94  HIS   A HD2  1 
ATOM   2032 H  HE1  . HIS   A 1 94  ? 28.756 2.946   5.334   1.00 12.53 ?  94  HIS   A HE1  1 
ATOM   2033 H  HE2  . HIS   A 1 94  ? 30.506 1.982   6.597   1.00 12.81 ?  94  HIS   A HE2  1 
ATOM   2034 N  N    . VAL   A 1 95  ? 27.771 -3.287  1.819   1.00 9.44  ?  95  VAL   A N    1 
ATOM   2035 C  CA   . VAL   A 1 95  ? 27.628 -4.327  0.801   1.00 9.62  ?  95  VAL   A CA   1 
ATOM   2036 C  C    . VAL   A 1 95  ? 27.072 -3.695  -0.460  1.00 9.51  ?  95  VAL   A C    1 
ATOM   2037 O  O    . VAL   A 1 95  ? 26.067 -2.979  -0.399  1.00 10.22 ?  95  VAL   A O    1 
ATOM   2038 C  CB   . VAL   A 1 95  ? 26.703 -5.473  1.261   1.00 10.49 ?  95  VAL   A CB   1 
ATOM   2039 C  CG1  . VAL   A 1 95  ? 26.591 -6.524  0.160   1.00 11.17 ?  95  VAL   A CG1  1 
ATOM   2040 C  CG2  . VAL   A 1 95  ? 27.212 -6.081  2.547   1.00 10.85 ?  95  VAL   A CG2  1 
ATOM   2041 H  H    . VAL   A 1 95  ? 27.023 -2.905  2.026   1.00 11.36 ?  95  VAL   A H    1 
ATOM   2042 H  HA   . VAL   A 1 95  ? 28.497 -4.697  0.595   1.00 11.58 ?  95  VAL   A HA   1 
ATOM   2043 H  HB   . VAL   A 1 95  ? 25.820 -5.121  1.424   1.00 12.62 ?  95  VAL   A HB   1 
ATOM   2044 H  HG11 . VAL   A 1 95  ? 26.198 -7.334  0.529   1.00 13.44 ?  95  VAL   A HG11 1 
ATOM   2045 H  HG12 . VAL   A 1 95  ? 26.028 -6.187  -0.556  1.00 13.44 ?  95  VAL   A HG12 1 
ATOM   2046 H  HG13 . VAL   A 1 95  ? 27.478 -6.726  -0.188  1.00 13.44 ?  95  VAL   A HG13 1 
ATOM   2047 H  HG21 . VAL   A 1 95  ? 26.655 -6.842  2.772   1.00 13.06 ?  95  VAL   A HG21 1 
ATOM   2048 H  HG22 . VAL   A 1 95  ? 28.129 -6.363  2.422   1.00 13.06 ?  95  VAL   A HG22 1 
ATOM   2049 H  HG23 . VAL   A 1 95  ? 27.159 -5.412  3.246   1.00 13.06 ?  95  VAL   A HG23 1 
ATOM   2050 N  N    . VAL   A 1 96  ? 27.694 -3.981  -1.603  1.00 9.42  ?  96  VAL   A N    1 
ATOM   2051 C  CA   . VAL   A 1 96  ? 27.278 -3.427  -2.884  1.00 10.31 ?  96  VAL   A CA   1 
ATOM   2052 C  C    . VAL   A 1 96  ? 26.470 -4.474  -3.644  1.00 10.42 ?  96  VAL   A C    1 
ATOM   2053 O  O    . VAL   A 1 96  ? 27.029 -5.419  -4.211  1.00 11.31 ?  96  VAL   A O    1 
ATOM   2054 C  CB   . VAL   A 1 96  ? 28.468 -2.942  -3.714  1.00 10.76 ?  96  VAL   A CB   1 
ATOM   2055 C  CG1  . VAL   A 1 96  ? 27.953 -2.304  -4.990  1.00 11.03 ?  96  VAL   A CG1  1 
ATOM   2056 C  CG2  . VAL   A 1 96  ? 29.328 -1.965  -2.927  1.00 11.18 ?  96  VAL   A CG2  1 
ATOM   2057 H  H    . VAL   A 1 96  ? 28.380 -4.504  -1.661  1.00 11.33 ?  96  VAL   A H    1 
ATOM   2058 H  HA   . VAL   A 1 96  ? 26.700 -2.665  -2.723  1.00 12.41 ?  96  VAL   A HA   1 
ATOM   2059 H  HB   . VAL   A 1 96  ? 29.017 -3.699  -3.961  1.00 12.94 ?  96  VAL   A HB   1 
ATOM   2060 H  HG11 . VAL   A 1 96  ? 28.683 -1.821  -5.416  1.00 13.27 ?  96  VAL   A HG11 1 
ATOM   2061 H  HG12 . VAL   A 1 96  ? 27.624 -2.991  -5.586  1.00 13.27 ?  96  VAL   A HG12 1 
ATOM   2062 H  HG13 . VAL   A 1 96  ? 27.240 -1.681  -4.771  1.00 13.27 ?  96  VAL   A HG13 1 
ATOM   2063 H  HG21 . VAL   A 1 96  ? 30.031 -1.624  -3.501  1.00 13.45 ?  96  VAL   A HG21 1 
ATOM   2064 H  HG22 . VAL   A 1 96  ? 28.771 -1.228  -2.618  1.00 13.45 ?  96  VAL   A HG22 1 
ATOM   2065 H  HG23 . VAL   A 1 96  ? 29.714 -2.424  -2.165  1.00 13.45 ?  96  VAL   A HG23 1 
ATOM   2066 N  N    A GLY   A 1 97  ? 25.151 -4.316  -3.659  0.50 10.71 ?  97  GLY   A N    1 
ATOM   2067 N  N    B GLY   A 1 97  ? 25.151 -4.310  -3.675  0.50 10.47 ?  97  GLY   A N    1 
ATOM   2068 C  CA   A GLY   A 1 97  ? 24.322 -5.061  -4.570  0.50 11.36 ?  97  GLY   A CA   1 
ATOM   2069 C  CA   B GLY   A 1 97  ? 24.327 -5.083  -4.570  0.50 11.03 ?  97  GLY   A CA   1 
ATOM   2070 C  C    A GLY   A 1 97  ? 24.286 -4.367  -5.916  0.50 11.40 ?  97  GLY   A C    1 
ATOM   2071 C  C    B GLY   A 1 97  ? 24.365 -4.485  -5.963  0.50 11.36 ?  97  GLY   A C    1 
ATOM   2072 O  O    A GLY   A 1 97  ? 24.549 -3.163  -6.020  0.50 12.01 ?  97  GLY   A O    1 
ATOM   2073 O  O    B GLY   A 1 97  ? 24.689 -3.305  -6.144  0.50 12.05 ?  97  GLY   A O    1 
ATOM   2074 H  H    A GLY   A 1 97  ? 24.714 -3.775  -3.142  0.50 12.89 ?  97  GLY   A H    1 
ATOM   2075 H  H    B GLY   A 1 97  ? 24.713 -3.750  -3.182  0.50 12.60 ?  97  GLY   A H    1 
ATOM   2076 H  HA2  A GLY   A 1 97  ? 24.675 -5.959  -4.665  0.50 13.66 ?  97  GLY   A HA2  1 
ATOM   2077 H  HA2  B GLY   A 1 97  ? 24.661 -5.991  -4.608  0.50 13.27 ?  97  GLY   A HA2  1 
ATOM   2078 H  HA3  A GLY   A 1 97  ? 23.415 -5.113  -4.227  0.50 13.66 ?  97  GLY   A HA3  1 
ATOM   2079 H  HA3  B GLY   A 1 97  ? 23.411 -5.101  -4.241  0.50 13.27 ?  97  GLY   A HA3  1 
ATOM   2080 N  N    A PRO   A 1 98  ? 23.948 -5.100  -6.973  0.50 11.07 ?  98  PRO   A N    1 
ATOM   2081 N  N    B PRO   A 1 98  ? 24.029 -5.280  -6.976  0.50 12.00 ?  98  PRO   A N    1 
ATOM   2082 C  CA   A PRO   A 1 98  ? 23.819 -4.462  -8.287  0.50 11.50 ?  98  PRO   A CA   1 
ATOM   2083 C  CA   B PRO   A 1 98  ? 23.988 -4.747  -8.342  0.50 13.11 ?  98  PRO   A CA   1 
ATOM   2084 C  C    A PRO   A 1 98  ? 22.704 -3.425  -8.297  0.50 11.20 ?  98  PRO   A C    1 
ATOM   2085 C  C    B PRO   A 1 98  ? 22.895 -3.702  -8.498  0.50 13.18 ?  98  PRO   A C    1 
ATOM   2086 O  O    A PRO   A 1 98  ? 21.644 -3.613  -7.694  0.50 11.32 ?  98  PRO   A O    1 
ATOM   2087 O  O    B PRO   A 1 98  ? 21.794 -3.832  -7.956  0.50 13.52 ?  98  PRO   A O    1 
ATOM   2088 C  CB   A PRO   A 1 98  ? 23.512 -5.637  -9.224  0.50 11.80 ?  98  PRO   A CB   1 
ATOM   2089 C  CB   B PRO   A 1 98  ? 23.685 -5.984  -9.194  0.50 13.05 ?  98  PRO   A CB   1 
ATOM   2090 C  CG   A PRO   A 1 98  ? 22.961 -6.714  -8.338  0.50 12.39 ?  98  PRO   A CG   1 
ATOM   2091 C  CG   B PRO   A 1 98  ? 22.967 -6.914  -8.257  0.50 13.12 ?  98  PRO   A CG   1 
ATOM   2092 C  CD   A PRO   A 1 98  ? 23.681 -6.549  -7.026  0.50 11.68 ?  98  PRO   A CD   1 
ATOM   2093 C  CD   B PRO   A 1 98  ? 23.643 -6.702  -6.926  0.50 12.21 ?  98  PRO   A CD   1 
ATOM   2094 H  HA   A PRO   A 1 98  ? 24.654 -4.050  -8.539  0.50 13.83 ?  98  PRO   A HA   1 
ATOM   2095 H  HA   B PRO   A 1 98  ? 24.851 -4.373  -8.593  0.50 15.76 ?  98  PRO   A HA   1 
ATOM   2096 H  HB2  A PRO   A 1 98  ? 22.853 -5.372  -9.881  0.50 14.20 ?  98  PRO   A HB2  1 
ATOM   2097 H  HB2  B PRO   A 1 98  ? 23.113 -5.731  -9.935  0.50 15.70 ?  98  PRO   A HB2  1 
ATOM   2098 H  HB3  A PRO   A 1 98  ? 24.328 -5.938  -9.653  0.50 14.20 ?  98  PRO   A HB3  1 
ATOM   2099 H  HB3  B PRO   A 1 98  ? 24.511 -6.377  -9.508  0.50 15.70 ?  98  PRO   A HB3  1 
ATOM   2100 H  HG2  A PRO   A 1 98  ? 22.007 -6.590  -8.221  0.50 14.90 ?  98  PRO   A HG2  1 
ATOM   2101 H  HG2  B PRO   A 1 98  ? 22.029 -6.671  -8.209  0.50 15.78 ?  98  PRO   A HG2  1 
ATOM   2102 H  HG3  A PRO   A 1 98  ? 23.149 -7.587  -8.720  0.50 14.90 ?  98  PRO   A HG3  1 
ATOM   2103 H  HG3  B PRO   A 1 98  ? 23.076 -7.827  -8.558  0.50 15.78 ?  98  PRO   A HG3  1 
ATOM   2104 H  HD2  A PRO   A 1 98  ? 23.109 -6.826  -6.287  0.50 14.05 ?  98  PRO   A HD2  1 
ATOM   2105 H  HD2  B PRO   A 1 98  ? 23.018 -6.857  -6.198  0.50 14.69 ?  98  PRO   A HD2  1 
ATOM   2106 H  HD3  A PRO   A 1 98  ? 24.516 -7.044  -7.027  0.50 14.05 ?  98  PRO   A HD3  1 
ATOM   2107 H  HD3  B PRO   A 1 98  ? 24.426 -7.271  -6.847  0.50 14.69 ?  98  PRO   A HD3  1 
ATOM   2108 N  N    A ASN   A 1 99  ? 22.964 -2.314  -8.978  0.50 11.96 ?  99  ASN   A N    1 
ATOM   2109 N  N    B ASN   A 1 99  ? 23.203 -2.663  -9.262  0.50 13.72 ?  99  ASN   A N    1 
ATOM   2110 C  CA   A ASN   A 1 99  ? 21.985 -1.250  -9.180  0.50 12.67 ?  99  ASN   A CA   1 
ATOM   2111 C  CA   B ASN   A 1 99  ? 22.251 -1.605  -9.576  0.50 14.55 ?  99  ASN   A CA   1 
ATOM   2112 C  C    A ASN   A 1 99  ? 21.435 -1.382  -10.596 0.50 13.65 ?  99  ASN   A C    1 
ATOM   2113 C  C    B ASN   A 1 99  ? 21.658 -1.910  -10.947 0.50 15.33 ?  99  ASN   A C    1 
ATOM   2114 O  O    A ASN   A 1 99  ? 22.123 -1.055  -11.572 0.50 14.90 ?  99  ASN   A O    1 
ATOM   2115 O  O    B ASN   A 1 99  ? 22.336 -1.776  -11.971 0.50 14.98 ?  99  ASN   A O    1 
ATOM   2116 C  CB   A ASN   A 1 99  ? 22.632 0.116   -8.967  0.50 12.05 ?  99  ASN   A CB   1 
ATOM   2117 C  CB   B ASN   A 1 99  ? 22.946 -0.247  -9.565  0.50 15.67 ?  99  ASN   A CB   1 
ATOM   2118 C  CG   A ASN   A 1 99  ? 21.622 1.257   -8.973  0.50 12.29 ?  99  ASN   A CG   1 
ATOM   2119 C  CG   B ASN   A 1 99  ? 21.981 0.901   -9.761  0.50 17.07 ?  99  ASN   A CG   1 
ATOM   2120 O  OD1  A ASN   A 1 99  ? 20.628 1.222   -9.698  0.50 13.07 ?  99  ASN   A OD1  1 
ATOM   2121 O  OD1  B ASN   A 1 99  ? 20.999 0.780   -10.489 0.50 17.25 ?  99  ASN   A OD1  1 
ATOM   2122 N  ND2  A ASN   A 1 99  ? 21.882 2.277   -8.169  0.50 12.88 ?  99  ASN   A ND2  1 
ATOM   2123 N  ND2  B ASN   A 1 99  ? 22.255 2.024   -9.106  0.50 18.31 ?  99  ASN   A ND2  1 
ATOM   2124 H  H    A ASN   A 1 99  ? 23.728 -2.150  -9.327  0.50 14.38 ?  99  ASN   A H    1 
ATOM   2125 H  H    B ASN   A 1 99  ? 23.978 -2.542  -9.609  0.50 16.49 ?  99  ASN   A H    1 
ATOM   2126 H  HA   A ASN   A 1 99  ? 21.254 -1.357  -8.543  0.50 15.24 ?  99  ASN   A HA   1 
ATOM   2127 H  HA   B ASN   A 1 99  ? 21.536 -1.598  -8.914  0.50 17.49 ?  99  ASN   A HA   1 
ATOM   2128 H  HB2  A ASN   A 1 99  ? 23.089 0.121   -8.114  0.50 14.50 ?  99  ASN   A HB2  1 
ATOM   2129 H  HB2  B ASN   A 1 99  ? 23.397 -0.123  -8.714  0.50 18.83 ?  99  ASN   A HB2  1 
ATOM   2130 H  HB3  A ASN   A 1 99  ? 23.267 0.270   -9.686  0.50 14.50 ?  99  ASN   A HB3  1 
ATOM   2131 H  HB3  B ASN   A 1 99  ? 23.586 -0.228  -10.289 0.50 18.83 ?  99  ASN   A HB3  1 
ATOM   2132 H  HD21 A ASN   A 1 99  ? 21.342 2.945   -8.137  0.50 15.49 ?  99  ASN   A HD21 1 
ATOM   2133 H  HD21 B ASN   A 1 99  ? 21.737 2.705   -9.183  0.50 22.01 ?  99  ASN   A HD21 1 
ATOM   2134 H  HD22 A ASN   A 1 99  ? 22.586 2.265   -7.678  0.50 15.49 ?  99  ASN   A HD22 1 
ATOM   2135 H  HD22 B ASN   A 1 99  ? 22.952 2.069   -8.603  0.50 22.01 ?  99  ASN   A HD22 1 
ATOM   2136 N  N    A VAL   A 1 100 ? 20.193 -1.873  -10.700 0.50 14.19 ?  100 VAL   A N    1 
ATOM   2137 N  N    B VAL   A 1 100 ? 20.393 -2.334  -10.957 0.50 17.18 ?  100 VAL   A N    1 
ATOM   2138 C  CA   A VAL   A 1 100 ? 19.577 -2.111  -12.004 0.50 16.41 ?  100 VAL   A CA   1 
ATOM   2139 C  CA   B VAL   A 1 100 ? 19.735 -2.718  -12.201 0.50 19.29 ?  100 VAL   A CA   1 
ATOM   2140 C  C    A VAL   A 1 100 ? 19.465 -0.814  -12.791 0.50 16.77 ?  100 VAL   A C    1 
ATOM   2141 C  C    B VAL   A 1 100 ? 19.622 -1.533  -13.147 0.50 19.84 ?  100 VAL   A C    1 
ATOM   2142 O  O    A VAL   A 1 100 ? 19.542 -0.815  -14.025 0.50 17.13 ?  100 VAL   A O    1 
ATOM   2143 O  O    B VAL   A 1 100 ? 19.623 -1.705  -14.373 0.50 19.94 ?  100 VAL   A O    1 
ATOM   2144 C  CB   A VAL   A 1 100 ? 18.213 -2.817  -11.829 0.50 18.40 ?  100 VAL   A CB   1 
ATOM   2145 C  CB   B VAL   A 1 100 ? 18.361 -3.346  -11.895 0.50 20.83 ?  100 VAL   A CB   1 
ATOM   2146 C  CG1  A VAL   A 1 100 ? 17.512 -2.992  -13.169 0.50 19.05 ?  100 VAL   A CG1  1 
ATOM   2147 C  CG1  B VAL   A 1 100 ? 17.634 -3.701  -13.182 0.50 21.33 ?  100 VAL   A CG1  1 
ATOM   2148 C  CG2  A VAL   A 1 100 ? 18.400 -4.170  -11.157 0.50 19.05 ?  100 VAL   A CG2  1 
ATOM   2149 C  CG2  B VAL   A 1 100 ? 18.527 -4.572  -11.014 0.50 21.39 ?  100 VAL   A CG2  1 
ATOM   2150 H  H    A VAL   A 1 100 ? 19.686 -2.083  -10.025 0.50 17.06 ?  100 VAL   A H    1 
ATOM   2151 H  H    B VAL   A 1 100 ? 19.903 -2.415  -10.254 0.50 20.65 ?  100 VAL   A H    1 
ATOM   2152 H  HA   A VAL   A 1 100 ? 20.144 -2.718  -12.504 0.50 19.73 ?  100 VAL   A HA   1 
ATOM   2153 H  HA   B VAL   A 1 100 ? 20.276 -3.394  -12.639 0.50 23.18 ?  100 VAL   A HA   1 
ATOM   2154 H  HB   A VAL   A 1 100 ? 17.642 -2.282  -11.259 0.50 22.11 ?  100 VAL   A HB   1 
ATOM   2155 H  HB   B VAL   A 1 100 ? 17.822 -2.697  -11.415 0.50 25.03 ?  100 VAL   A HB   1 
ATOM   2156 H  HG11 A VAL   A 1 100 ? 16.763 -3.603  -13.058 0.50 22.89 ?  100 VAL   A HG11 1 
ATOM   2157 H  HG11 B VAL   A 1 100 ? 16.863 -4.248  -12.964 0.50 25.63 ?  100 VAL   A HG11 1 
ATOM   2158 H  HG12 A VAL   A 1 100 ? 17.189 -2.132  -13.473 0.50 22.89 ?  100 VAL   A HG12 1 
ATOM   2159 H  HG12 B VAL   A 1 100 ? 17.344 -2.885  -13.622 0.50 25.63 ?  100 VAL   A HG12 1 
ATOM   2160 H  HG13 A VAL   A 1 100 ? 18.140 -3.361  -13.809 0.50 22.89 ?  100 VAL   A HG13 1 
ATOM   2161 H  HG13 B VAL   A 1 100 ? 18.236 -4.194  -13.760 0.50 25.63 ?  100 VAL   A HG13 1 
ATOM   2162 H  HG21 A VAL   A 1 100 ? 17.542 -4.623  -11.102 0.50 22.89 ?  100 VAL   A HG21 1 
ATOM   2163 H  HG21 B VAL   A 1 100 ? 17.663 -4.996  -10.905 0.50 25.70 ?  100 VAL   A HG21 1 
ATOM   2164 H  HG22 A VAL   A 1 100 ? 19.018 -4.704  -11.683 0.50 22.89 ?  100 VAL   A HG22 1 
ATOM   2165 H  HG22 B VAL   A 1 100 ? 19.147 -5.182  -11.440 0.50 25.70 ?  100 VAL   A HG22 1 
ATOM   2166 H  HG23 A VAL   A 1 100 ? 18.758 -4.037  -10.265 0.50 22.89 ?  100 VAL   A HG23 1 
ATOM   2167 H  HG23 B VAL   A 1 100 ? 18.872 -4.295  -10.151 0.50 25.70 ?  100 VAL   A HG23 1 
ATOM   2168 N  N    A ASN   A 1 101 ? 19.290 0.310   -12.105 0.50 17.59 ?  101 ASN   A N    1 
ATOM   2169 N  N    B ASN   A 1 101 ? 19.507 -0.316  -12.605 0.50 20.40 ?  101 ASN   A N    1 
ATOM   2170 C  CA   A ASN   A 1 101 ? 19.233 1.588   -12.799 0.50 18.85 ?  101 ASN   A CA   1 
ATOM   2171 C  CA   B ASN   A 1 101 ? 19.425 0.870   -13.452 0.50 21.47 ?  101 ASN   A CA   1 
ATOM   2172 C  C    A ASN   A 1 101 ? 20.592 2.025   -13.345 0.50 20.55 ?  101 ASN   A C    1 
ATOM   2173 C  C    B ASN   A 1 101 ? 20.736 1.135   -14.183 0.50 22.48 ?  101 ASN   A C    1 
ATOM   2174 O  O    A ASN   A 1 101 ? 20.670 3.076   -13.996 0.50 21.85 ?  101 ASN   A O    1 
ATOM   2175 O  O    B ASN   A 1 101 ? 20.737 1.789   -15.233 0.50 22.73 ?  101 ASN   A O    1 
ATOM   2176 C  CB   A ASN   A 1 101 ? 18.609 2.640   -11.880 0.50 18.06 ?  101 ASN   A CB   1 
ATOM   2177 C  CB   B ASN   A 1 101 ? 19.031 2.085   -12.611 0.50 21.68 ?  101 ASN   A CB   1 
ATOM   2178 C  CG   A ASN   A 1 101 ? 17.235 2.218   -11.367 0.50 17.85 ?  101 ASN   A CG   1 
ATOM   2179 C  CG   B ASN   A 1 101 ? 17.759 1.853   -11.809 0.50 22.28 ?  101 ASN   A CG   1 
ATOM   2180 O  OD1  A ASN   A 1 101 ? 16.395 1.730   -12.126 0.50 18.05 ?  101 ASN   A OD1  1 
ATOM   2181 O  OD1  B ASN   A 1 101 ? 16.776 1.311   -12.317 0.50 23.40 ?  101 ASN   A OD1  1 
ATOM   2182 N  ND2  A ASN   A 1 101 ? 17.010 2.387   -10.072 0.50 17.77 ?  101 ASN   A ND2  1 
ATOM   2183 N  ND2  B ASN   A 1 101 ? 17.779 2.252   -10.543 0.50 22.24 ?  101 ASN   A ND2  1 
ATOM   2184 H  H    A ASN   A 1 101 ? 19.196 0.352   -11.254 0.50 21.14 ?  101 ASN   A H    1 
ATOM   2185 H  H    B ASN   A 1 101 ? 19.469 -0.155  -11.759 0.50 24.51 ?  101 ASN   A H    1 
ATOM   2186 H  HA   A ASN   A 1 101 ? 18.646 1.487   -13.561 0.50 22.65 ?  101 ASN   A HA   1 
ATOM   2187 H  HA   B ASN   A 1 101 ? 18.737 0.733   -14.116 0.50 25.79 ?  101 ASN   A HA   1 
ATOM   2188 H  HB2  A ASN   A 1 101 ? 19.189 2.779   -11.118 0.50 21.71 ?  101 ASN   A HB2  1 
ATOM   2189 H  HB2  B ASN   A 1 101 ? 19.747 2.288   -11.989 0.50 26.05 ?  101 ASN   A HB2  1 
ATOM   2190 H  HB3  A ASN   A 1 101 ? 18.506 3.467   -12.379 0.50 21.71 ?  101 ASN   A HB3  1 
ATOM   2191 H  HB3  B ASN   A 1 101 ? 18.883 2.843   -13.202 0.50 26.05 ?  101 ASN   A HB3  1 
ATOM   2192 H  HD21 A ASN   A 1 101 ? 16.251 2.162   -9.739  0.50 21.36 ?  101 ASN   A HD21 1 
ATOM   2193 H  HD21 B ASN   A 1 101 ? 17.084 2.145   -10.050 0.50 26.72 ?  101 ASN   A HD21 1 
ATOM   2194 H  HD22 A ASN   A 1 101 ? 17.616 2.731   -9.572  0.50 21.36 ?  101 ASN   A HD22 1 
ATOM   2195 H  HD22 B ASN   A 1 101 ? 18.485 2.622   -10.218 0.50 26.72 ?  101 ASN   A HD22 1 
ATOM   2196 N  N    A LYS   A 1 102 ? 21.648 1.237   -13.116 0.50 22.38 ?  102 LYS   A N    1 
ATOM   2197 N  N    B LYS   A 1 102 ? 21.854 0.654   -13.642 0.50 23.92 ?  102 LYS   A N    1 
ATOM   2198 C  CA   A LYS   A 1 102 ? 22.937 1.418   -13.771 0.50 24.17 ?  102 LYS   A CA   1 
ATOM   2199 C  CA   B LYS   A 1 102 ? 23.157 0.764   -14.285 0.50 24.87 ?  102 LYS   A CA   1 
ATOM   2200 C  C    A LYS   A 1 102 ? 23.238 0.328   -14.789 0.50 24.57 ?  102 LYS   A C    1 
ATOM   2201 C  C    B LYS   A 1 102 ? 23.456 -0.418  -15.203 0.50 24.29 ?  102 LYS   A C    1 
ATOM   2202 O  O    A LYS   A 1 102 ? 24.307 0.360   -15.408 0.50 25.26 ?  102 LYS   A O    1 
ATOM   2203 O  O    B LYS   A 1 102 ? 24.573 -0.519  -15.720 0.50 24.49 ?  102 LYS   A O    1 
ATOM   2204 C  CB   A LYS   A 1 102 ? 24.068 1.466   -12.736 0.50 25.81 ?  102 LYS   A CB   1 
ATOM   2205 C  CB   B LYS   A 1 102 ? 24.265 0.871   -13.229 0.50 26.76 ?  102 LYS   A CB   1 
ATOM   2206 C  CG   A LYS   A 1 102 ? 23.969 2.605   -11.740 0.50 27.16 ?  102 LYS   A CG   1 
ATOM   2207 C  CG   B LYS   A 1 102 ? 24.176 2.086   -12.315 0.50 28.56 ?  102 LYS   A CG   1 
ATOM   2208 C  CD   A LYS   A 1 102 ? 25.141 2.576   -10.769 0.50 28.47 ?  102 LYS   A CD   1 
ATOM   2209 C  CD   B LYS   A 1 102 ? 25.224 2.013   -11.207 0.50 30.45 ?  102 LYS   A CD   1 
ATOM   2210 C  CE   A LYS   A 1 102 ? 25.065 3.709   -9.758  0.50 29.40 ?  102 LYS   A CE   1 
ATOM   2211 C  CE   B LYS   A 1 102 ? 25.081 3.158   -10.215 0.50 31.83 ?  102 LYS   A CE   1 
ATOM   2212 N  NZ   A LYS   A 1 102 ? 26.181 3.637   -8.771  0.50 29.78 ?  102 LYS   A NZ   1 
ATOM   2213 N  NZ   B LYS   A 1 102 ? 25.351 2.717   -8.815  0.50 32.68 ?  102 LYS   A NZ   1 
ATOM   2214 H  H    A LYS   A 1 102 ? 21.641 0.568   -12.571 0.50 26.89 ?  102 LYS   A H    1 
ATOM   2215 H  H    B LYS   A 1 102 ? 21.883 0.254   -12.881 0.50 28.74 ?  102 LYS   A H    1 
ATOM   2216 H  HA   A LYS   A 1 102 ? 22.935 2.254   -14.249 0.50 29.03 ?  102 LYS   A HA   1 
ATOM   2217 H  HA   B LYS   A 1 102 ? 23.179 1.575   -14.815 0.50 29.88 ?  102 LYS   A HA   1 
ATOM   2218 H  HB2  A LYS   A 1 102 ? 24.067 0.636   -12.234 0.50 31.01 ?  102 LYS   A HB2  1 
ATOM   2219 H  HB2  B LYS   A 1 102 ? 24.234 0.082   -12.666 0.50 32.14 ?  102 LYS   A HB2  1 
ATOM   2220 H  HB3  A LYS   A 1 102 ? 24.913 1.559   -13.205 0.50 31.01 ?  102 LYS   A HB3  1 
ATOM   2221 H  HB3  B LYS   A 1 102 ? 25.123 0.912   -13.682 0.50 32.14 ?  102 LYS   A HB3  1 
ATOM   2222 H  HG2  A LYS   A 1 102 ? 23.984 3.451   -12.216 0.50 32.63 ?  102 LYS   A HG2  1 
ATOM   2223 H  HG2  B LYS   A 1 102 ? 24.335 2.892   -12.831 0.50 34.31 ?  102 LYS   A HG2  1 
ATOM   2224 H  HG3  A LYS   A 1 102 ? 23.147 2.518   -11.233 0.50 32.63 ?  102 LYS   A HG3  1 
ATOM   2225 H  HG3  B LYS   A 1 102 ? 23.298 2.117   -11.904 0.50 34.31 ?  102 LYS   A HG3  1 
ATOM   2226 H  HD2  A LYS   A 1 102 ? 25.133 1.735   -10.285 0.50 34.20 ?  102 LYS   A HD2  1 
ATOM   2227 H  HD2  B LYS   A 1 102 ? 25.128 1.178   -10.722 0.50 36.57 ?  102 LYS   A HD2  1 
ATOM   2228 H  HD3  A LYS   A 1 102 ? 25.969 2.667   -11.267 0.50 34.20 ?  102 LYS   A HD3  1 
ATOM   2229 H  HD3  B LYS   A 1 102 ? 26.108 2.065   -11.603 0.50 36.57 ?  102 LYS   A HD3  1 
ATOM   2230 H  HE2  A LYS   A 1 102 ? 25.125 4.558   -10.225 0.50 35.31 ?  102 LYS   A HE2  1 
ATOM   2231 H  HE2  B LYS   A 1 102 ? 25.718 3.855   -10.441 0.50 38.23 ?  102 LYS   A HE2  1 
ATOM   2232 H  HE3  A LYS   A 1 102 ? 24.225 3.650   -9.275  0.50 35.31 ?  102 LYS   A HE3  1 
ATOM   2233 H  HE3  B LYS   A 1 102 ? 24.177 3.505   -10.256 0.50 38.23 ?  102 LYS   A HE3  1 
ATOM   2234 H  HZ1  A LYS   A 1 102 ? 26.117 4.307   -8.190  0.50 35.77 ?  102 LYS   A HZ1  1 
ATOM   2235 H  HZ1  B LYS   A 1 102 ? 25.138 3.365   -8.244  0.50 39.25 ?  102 LYS   A HZ1  1 
ATOM   2236 H  HZ2  A LYS   A 1 102 ? 26.145 2.865   -8.328  0.50 35.77 ?  102 LYS   A HZ2  1 
ATOM   2237 H  HZ2  B LYS   A 1 102 ? 24.867 1.994   -8.625  0.50 39.25 ?  102 LYS   A HZ2  1 
ATOM   2238 H  HZ3  A LYS   A 1 102 ? 26.963 3.691   -9.192  0.50 35.77 ?  102 LYS   A HZ3  1 
ATOM   2239 H  HZ3  B LYS   A 1 102 ? 26.213 2.518   -8.719  0.50 39.25 ?  102 LYS   A HZ3  1 
ATOM   2240 N  N    A GLY   A 1 103 ? 22.334 -0.631  -14.981 0.50 24.79 ?  103 GLY   A N    1 
ATOM   2241 N  N    B GLY   A 1 103 ? 22.496 -1.318  -15.406 0.50 23.71 ?  103 GLY   A N    1 
ATOM   2242 C  CA   A GLY   A 1 103 ? 22.580 -1.728  -15.894 0.50 25.12 ?  103 GLY   A CA   1 
ATOM   2243 C  CA   B GLY   A 1 103 ? 22.722 -2.488  -16.232 0.50 23.21 ?  103 GLY   A CA   1 
ATOM   2244 C  C    A GLY   A 1 103 ? 23.465 -2.820  -15.345 0.50 25.33 ?  103 GLY   A C    1 
ATOM   2245 C  C    B GLY   A 1 103 ? 23.526 -3.592  -15.579 0.50 22.13 ?  103 GLY   A C    1 
ATOM   2246 O  O    A GLY   A 1 103 ? 24.080 -3.552  -16.127 0.50 26.08 ?  103 GLY   A O    1 
ATOM   2247 O  O    B GLY   A 1 103 ? 23.952 -4.523  -16.273 0.50 22.54 ?  103 GLY   A O    1 
ATOM   2248 H  H    A GLY   A 1 103 ? 21.571 -0.673  -14.590 0.50 29.78 ?  103 GLY   A H    1 
ATOM   2249 H  H    B GLY   A 1 103 ? 21.702 -1.261  -15.076 0.50 28.49 ?  103 GLY   A H    1 
ATOM   2250 H  HA2  A GLY   A 1 103 ? 21.729 -2.114  -16.167 0.50 30.18 ?  103 GLY   A HA2  1 
ATOM   2251 H  HA2  B GLY   A 1 103 ? 21.867 -2.863  -16.484 0.50 27.89 ?  103 GLY   A HA2  1 
ATOM   2252 H  HA3  A GLY   A 1 103 ? 23.020 -1.392  -16.688 0.50 30.18 ?  103 GLY   A HA3  1 
ATOM   2253 H  HA3  B GLY   A 1 103 ? 23.172 -2.199  -17.046 0.50 27.89 ?  103 GLY   A HA3  1 
ATOM   2254 N  N    A GLU   A 1 104 ? 23.564 -2.949  -14.024 0.50 24.31 ?  104 GLU   A N    1 
ATOM   2255 N  N    B GLU   A 1 104 ? 23.728 -3.535  -14.268 0.50 20.63 ?  104 GLU   A N    1 
ATOM   2256 C  CA   A GLU   A 1 104 ? 24.443 -3.943  -13.425 0.50 23.57 ?  104 GLU   A CA   1 
ATOM   2257 C  CA   B GLU   A 1 104 ? 24.608 -4.478  -13.595 0.50 18.84 ?  104 GLU   A CA   1 
ATOM   2258 C  C    A GLU   A 1 104 ? 23.759 -5.302  -13.331 0.50 23.94 ?  104 GLU   A C    1 
ATOM   2259 C  C    B GLU   A 1 104 ? 23.916 -5.828  -13.417 0.50 18.15 ?  104 GLU   A C    1 
ATOM   2260 O  O    A GLU   A 1 104 ? 22.550 -5.398  -13.098 0.50 24.10 ?  104 GLU   A O    1 
ATOM   2261 O  O    B GLU   A 1 104 ? 22.691 -5.915  -13.288 0.50 18.55 ?  104 GLU   A O    1 
ATOM   2262 C  CB   A GLU   A 1 104 ? 24.927 -3.462  -12.054 0.50 22.44 ?  104 GLU   A CB   1 
ATOM   2263 C  CB   B GLU   A 1 104 ? 25.073 -3.897  -12.258 0.50 18.28 ?  104 GLU   A CB   1 
ATOM   2264 C  CG   A GLU   A 1 104 ? 25.957 -2.337  -12.186 0.50 21.92 ?  104 GLU   A CG   1 
ATOM   2265 C  CG   B GLU   A 1 104 ? 25.817 -2.570  -12.436 0.50 18.60 ?  104 GLU   A CG   1 
ATOM   2266 C  CD   A GLU   A 1 104 ? 26.249 -1.577  -10.901 0.50 21.24 ?  104 GLU   A CD   1 
ATOM   2267 C  CD   B GLU   A 1 104 ? 26.227 -1.869  -11.150 0.50 18.34 ?  104 GLU   A CD   1 
ATOM   2268 O  OE1  A GLU   A 1 104 ? 25.575 -1.813  -9.882  0.50 19.81 ?  104 GLU   A OE1  1 
ATOM   2269 O  OE1  B GLU   A 1 104 ? 25.767 -2.249  -10.057 0.50 18.20 ?  104 GLU   A OE1  1 
ATOM   2270 O  OE2  A GLU   A 1 104 ? 27.161 -0.721  -10.924 0.50 22.24 -1 104 GLU   A OE2  1 
ATOM   2271 O  OE2  B GLU   A 1 104 ? 27.012 -0.900  -11.256 0.50 18.59 -1 104 GLU   A OE2  1 
ATOM   2272 H  H    A GLU   A 1 104 ? 23.144 -2.462  -13.456 0.50 29.21 ?  104 GLU   A H    1 
ATOM   2273 H  H    B GLU   A 1 104 ? 23.356 -2.959  -13.757 0.50 24.79 ?  104 GLU   A H    1 
ATOM   2274 H  HA   A GLU   A 1 104 ? 25.218 -4.050  -13.992 0.50 28.32 ?  104 GLU   A HA   1 
ATOM   2275 H  HA   B GLU   A 1 104 ? 25.393 -4.615  -14.153 0.50 22.65 ?  104 GLU   A HA   1 
ATOM   2276 H  HB2  A GLU   A 1 104 ? 24.169 -3.132  -11.548 0.50 26.97 ?  104 GLU   A HB2  1 
ATOM   2277 H  HB2  B GLU   A 1 104 ? 24.298 -3.743  -11.700 0.50 21.96 ?  104 GLU   A HB2  1 
ATOM   2278 H  HB3  A GLU   A 1 104 ? 25.342 -4.206  -11.587 0.50 26.97 ?  104 GLU   A HB3  1 
ATOM   2279 H  HB3  B GLU   A 1 104 ? 25.673 -4.531  -11.840 0.50 21.96 ?  104 GLU   A HB3  1 
ATOM   2280 H  HG2  A GLU   A 1 104 ? 26.790 -2.721  -12.491 0.50 26.33 ?  104 GLU   A HG2  1 
ATOM   2281 H  HG2  B GLU   A 1 104 ? 26.625 -2.735  -12.942 0.50 22.35 ?  104 GLU   A HG2  1 
ATOM   2282 H  HG3  A GLU   A 1 104 ? 25.627 -1.700  -12.839 0.50 26.33 ?  104 GLU   A HG3  1 
ATOM   2283 H  HG3  B GLU   A 1 104 ? 25.243 -1.957  -12.920 0.50 22.35 ?  104 GLU   A HG3  1 
ATOM   2284 N  N    A ASP   A 1 105 ? 24.554 -6.352  -13.522 0.50 24.64 ?  105 ASP   A N    1 
ATOM   2285 N  N    B ASP   A 1 105 ? 24.729 -6.885  -13.410 0.50 18.17 ?  105 ASP   A N    1 
ATOM   2286 C  CA   A ASP   A 1 105 ? 24.045 -7.714  -13.618 0.50 25.35 ?  105 ASP   A CA   1 
ATOM   2287 C  CA   B ASP   A 1 105 ? 24.248 -8.263  -13.496 0.50 18.55 ?  105 ASP   A CA   1 
ATOM   2288 C  C    A ASP   A 1 105 ? 23.352 -8.117  -12.323 0.50 23.90 ?  105 ASP   A C    1 
ATOM   2289 C  C    B ASP   A 1 105 ? 23.528 -8.664  -12.212 0.50 16.97 ?  105 ASP   A C    1 
ATOM   2290 O  O    A ASP   A 1 105 ? 23.965 -8.105  -11.253 0.50 22.69 ?  105 ASP   A O    1 
ATOM   2291 O  O    B ASP   A 1 105 ? 24.131 -8.691  -11.137 0.50 15.33 ?  105 ASP   A O    1 
ATOM   2292 C  CB   A ASP   A 1 105 ? 25.218 -8.651  -13.903 0.50 27.49 ?  105 ASP   A CB   1 
ATOM   2293 C  CB   B ASP   A 1 105 ? 25.452 -9.174  -13.741 0.50 20.78 ?  105 ASP   A CB   1 
ATOM   2294 C  CG   A ASP   A 1 105 ? 24.770 -10.052 -14.249 0.50 29.32 ?  105 ASP   A CG   1 
ATOM   2295 C  CG   B ASP   A 1 105 ? 25.096 -10.648 -13.762 0.50 22.53 ?  105 ASP   A CG   1 
ATOM   2296 O  OD1  A ASP   A 1 105 ? 23.544 -10.273 -14.336 0.50 29.71 ?  105 ASP   A OD1  1 
ATOM   2297 O  OD1  B ASP   A 1 105 ? 23.897 -10.985 -13.857 0.50 22.53 ?  105 ASP   A OD1  1 
ATOM   2298 O  OD2  A ASP   A 1 105 ? 25.641 -10.926 -14.445 0.50 30.30 -1 105 ASP   A OD2  1 
ATOM   2299 O  OD2  B ASP   A 1 105 ? 26.036 -11.474 -13.683 0.50 24.02 -1 105 ASP   A OD2  1 
ATOM   2300 H  H    A ASP   A 1 105 ? 25.407 -6.303  -13.596 0.50 29.60 ?  105 ASP   A H    1 
ATOM   2301 H  H    B ASP   A 1 105 ? 25.585 -6.823  -13.352 0.50 21.83 ?  105 ASP   A H    1 
ATOM   2302 H  HA   A ASP   A 1 105 ? 23.411 -7.789  -14.348 0.50 30.45 ?  105 ASP   A HA   1 
ATOM   2303 H  HA   B ASP   A 1 105 ? 23.632 -8.351  -14.239 0.50 22.29 ?  105 ASP   A HA   1 
ATOM   2304 H  HB2  A ASP   A 1 105 ? 25.719 -8.318  -14.666 0.50 33.02 ?  105 ASP   A HB2  1 
ATOM   2305 H  HB2  B ASP   A 1 105 ? 25.848 -8.948  -14.598 0.50 24.97 ?  105 ASP   A HB2  1 
ATOM   2306 H  HB3  A ASP   A 1 105 ? 25.800 -8.685  -13.122 0.50 33.02 ?  105 ASP   A HB3  1 
ATOM   2307 H  HB3  B ASP   A 1 105 ? 26.098 -9.040  -13.032 0.50 24.97 ?  105 ASP   A HB3  1 
ATOM   2308 N  N    A ILE   A 1 106 ? 22.074 -8.491  -12.426 0.50 23.45 ?  106 ILE   A N    1 
ATOM   2309 N  N    B ILE   A 1 106 ? 22.239 -8.997  -12.324 0.50 17.35 ?  106 ILE   A N    1 
ATOM   2310 C  CA   A ILE   A 1 106 ? 21.317 -8.895  -11.247 0.50 22.64 ?  106 ILE   A CA   1 
ATOM   2311 C  CA   B ILE   A 1 106 ? 21.465 -9.377  -11.147 0.50 17.66 ?  106 ILE   A CA   1 
ATOM   2312 C  C    A ILE   A 1 106 ? 21.852 -10.190 -10.655 0.50 21.06 ?  106 ILE   A C    1 
ATOM   2313 C  C    B ILE   A 1 106 ? 22.019 -10.629 -10.485 0.50 17.41 ?  106 ILE   A C    1 
ATOM   2314 O  O    A ILE   A 1 106 ? 21.630 -10.460 -9.470  0.50 20.11 ?  106 ILE   A O    1 
ATOM   2315 O  O    B ILE   A 1 106 ? 21.823 -10.821 -9.280  0.50 17.59 ?  106 ILE   A O    1 
ATOM   2316 C  CB   A ILE   A 1 106 ? 19.813 -8.999  -11.573 0.50 23.98 ?  106 ILE   A CB   1 
ATOM   2317 C  CB   B ILE   A 1 106 ? 19.962 -9.505  -11.487 0.50 19.71 ?  106 ILE   A CB   1 
ATOM   2318 C  CG1  A ILE   A 1 106 ? 18.982 -9.100  -10.290 0.50 24.66 ?  106 ILE   A CG1  1 
ATOM   2319 C  CG1  B ILE   A 1 106 ? 19.114 -9.538  -10.212 0.50 20.92 ?  106 ILE   A CG1  1 
ATOM   2320 C  CG2  A ILE   A 1 106 ? 19.539 -10.206 -12.457 0.50 24.31 ?  106 ILE   A CG2  1 
ATOM   2321 C  CG2  B ILE   A 1 106 ? 19.695 -10.743 -12.324 0.50 20.23 ?  106 ILE   A CG2  1 
ATOM   2322 C  CD1  A ILE   A 1 106 ? 19.199 -7.955  -9.325  0.50 25.11 ?  106 ILE   A CD1  1 
ATOM   2323 C  CD1  B ILE   A 1 106 ? 19.108 -8.228  -9.446  0.50 21.39 ?  106 ILE   A CD1  1 
ATOM   2324 H  H    A ILE   A 1 106 ? 21.633 -8.522  -13.157 0.50 28.17 ?  106 ILE   A H    1 
ATOM   2325 H  H    B ILE   A 1 106 ? 21.803 -9.008  -13.058 0.50 20.86 ?  106 ILE   A H    1 
ATOM   2326 H  HA   A ILE   A 1 106 ? 21.432 -8.211  -10.577 0.50 27.20 ?  106 ILE   A HA   1 
ATOM   2327 H  HA   B ILE   A 1 106 ? 21.554 -8.673  -10.494 0.50 21.23 ?  106 ILE   A HA   1 
ATOM   2328 H  HB   A ILE   A 1 106 ? 19.544 -8.202  -12.054 0.50 28.81 ?  106 ILE   A HB   1 
ATOM   2329 H  HB   B ILE   A 1 106 ? 19.703 -8.725  -12.002 0.50 23.68 ?  106 ILE   A HB   1 
ATOM   2330 H  HG12 A ILE   A 1 106 ? 18.041 -9.110  -10.529 0.50 29.62 ?  106 ILE   A HG12 1 
ATOM   2331 H  HG12 B ILE   A 1 106 ? 18.197 -9.739  -10.451 0.50 25.14 ?  106 ILE   A HG12 1 
ATOM   2332 H  HG13 A ILE   A 1 106 ? 19.211 -9.924  -9.833  0.50 29.62 ?  106 ILE   A HG13 1 
ATOM   2333 H  HG13 B ILE   A 1 106 ? 19.457 -10.223 -9.619  0.50 25.14 ?  106 ILE   A HG13 1 
ATOM   2334 H  HG21 A ILE   A 1 106 ? 18.646 -10.130 -12.827 0.50 29.21 ?  106 ILE   A HG21 1 
ATOM   2335 H  HG21 B ILE   A 1 106 ? 18.794 -10.689 -12.681 0.50 24.31 ?  106 ILE   A HG21 1 
ATOM   2336 H  HG22 A ILE   A 1 106 ? 20.194 -10.227 -13.171 0.50 29.21 ?  106 ILE   A HG22 1 
ATOM   2337 H  HG22 B ILE   A 1 106 ? 20.338 -10.775 -13.047 0.50 24.31 ?  106 ILE   A HG22 1 
ATOM   2338 H  HG23 A ILE   A 1 106 ? 19.607 -11.013 -11.922 0.50 29.21 ?  106 ILE   A HG23 1 
ATOM   2339 H  HG23 B ILE   A 1 106 ? 19.783 -11.528 -11.763 0.50 24.31 ?  106 ILE   A HG23 1 
ATOM   2340 H  HD11 A ILE   A 1 106 ? 18.459 -7.924  -8.702  0.50 30.17 ?  106 ILE   A HD11 1 
ATOM   2341 H  HD11 B ILE   A 1 106 ? 18.413 -8.260  -8.771  0.50 25.70 ?  106 ILE   A HD11 1 
ATOM   2342 H  HD12 A ILE   A 1 106 ? 20.030 -8.100  -8.844  0.50 30.17 ?  106 ILE   A HD12 1 
ATOM   2343 H  HD12 B ILE   A 1 106 ? 19.973 -8.102  -9.023  0.50 25.70 ?  106 ILE   A HD12 1 
ATOM   2344 H  HD13 A ILE   A 1 106 ? 19.246 -7.125  -9.826  0.50 30.17 ?  106 ILE   A HD13 1 
ATOM   2345 H  HD13 B ILE   A 1 106 ? 18.933 -7.501  -10.065 0.50 25.70 ?  106 ILE   A HD13 1 
ATOM   2346 N  N    A GLN   A 1 107 ? 22.567 -10.994 -11.449 0.50 21.44 ?  107 GLN   A N    1 
ATOM   2347 N  N    B GLN   A 1 107 ? 22.729 -11.480 -11.238 0.50 17.86 ?  107 GLN   A N    1 
ATOM   2348 C  CA   A GLN   A 1 107 ? 23.167 -12.224 -10.942 0.50 22.67 ?  107 GLN   A CA   1 
ATOM   2349 C  CA   B GLN   A 1 107 ? 23.379 -12.635 -10.623 0.50 19.67 ?  107 GLN   A CA   1 
ATOM   2350 C  C    A GLN   A 1 107 ? 24.149 -11.961 -9.809  0.50 20.55 ?  107 GLN   A C    1 
ATOM   2351 C  C    B GLN   A 1 107 ? 24.334 -12.205 -9.517  0.50 17.57 ?  107 GLN   A C    1 
ATOM   2352 O  O    A GLN   A 1 107 ? 24.395 -12.859 -8.997  0.50 22.09 ?  107 GLN   A O    1 
ATOM   2353 O  O    B GLN   A 1 107 ? 24.555 -12.951 -8.553  0.50 17.24 ?  107 GLN   A O    1 
ATOM   2354 C  CB   A GLN   A 1 107 ? 23.886 -12.964 -12.077 0.50 26.16 ?  107 GLN   A CB   1 
ATOM   2355 C  CB   B GLN   A 1 107 ? 24.112 -13.453 -11.692 0.50 23.45 ?  107 GLN   A CB   1 
ATOM   2356 C  CG   A GLN   A 1 107 ? 23.019 -13.245 -13.295 0.50 29.64 ?  107 GLN   A CG   1 
ATOM   2357 C  CG   B GLN   A 1 107 ? 23.188 -14.036 -12.750 0.50 27.12 ?  107 GLN   A CG   1 
ATOM   2358 C  CD   A GLN   A 1 107 ? 21.780 -14.045 -12.955 0.50 32.47 ?  107 GLN   A CD   1 
ATOM   2359 C  CD   B GLN   A 1 107 ? 22.165 -14.989 -12.163 0.50 30.35 ?  107 GLN   A CD   1 
ATOM   2360 O  OE1  A GLN   A 1 107 ? 21.861 -15.106 -12.337 0.50 33.76 ?  107 GLN   A OE1  1 
ATOM   2361 O  OE1  B GLN   A 1 107 ? 22.465 -15.748 -11.241 0.50 31.29 ?  107 GLN   A OE1  1 
ATOM   2362 N  NE2  A GLN   A 1 107 ? 20.621 -13.535 -13.351 0.50 33.32 ?  107 GLN   A NE2  1 
ATOM   2363 N  NE2  B GLN   A 1 107 ? 20.945 -14.946 -12.688 0.50 31.45 ?  107 GLN   A NE2  1 
ATOM   2364 H  H    A GLN   A 1 107 ? 22.727 -10.843 -12.276 0.50 25.77 ?  107 GLN   A H    1 
ATOM   2365 H  H    B GLN   A 1 107 ? 22.852 -11.410 -12.089 0.50 21.46 ?  107 GLN   A H    1 
ATOM   2366 H  HA   A GLN   A 1 107 ? 22.471 -12.806 -10.602 0.50 27.23 ?  107 GLN   A HA   1 
ATOM   2367 H  HA   B GLN   A 1 107 ? 22.703 -13.207 -10.234 0.50 23.64 ?  107 GLN   A HA   1 
ATOM   2368 H  HB2  A GLN   A 1 107 ? 24.639 -12.429 -12.372 0.50 31.43 ?  107 GLN   A HB2  1 
ATOM   2369 H  HB2  B GLN   A 1 107 ? 24.756 -12.886 -12.145 0.50 28.18 ?  107 GLN   A HB2  1 
ATOM   2370 H  HB3  A GLN   A 1 107 ? 24.204 -13.819 -11.744 0.50 31.43 ?  107 GLN   A HB3  1 
ATOM   2371 H  HB3  B GLN   A 1 107 ? 24.572 -14.196 -11.266 0.50 28.18 ?  107 GLN   A HB3  1 
ATOM   2372 H  HG2  A GLN   A 1 107 ? 22.735 -12.405 -13.685 0.50 35.60 ?  107 GLN   A HG2  1 
ATOM   2373 H  HG2  B GLN   A 1 107 ? 22.710 -13.314 -13.187 0.50 32.58 ?  107 GLN   A HG2  1 
ATOM   2374 H  HG3  A GLN   A 1 107 ? 23.537 -13.752 -13.942 0.50 35.60 ?  107 GLN   A HG3  1 
ATOM   2375 H  HG3  B GLN   A 1 107 ? 23.716 -14.526 -13.402 0.50 32.58 ?  107 GLN   A HG3  1 
ATOM   2376 H  HE21 A GLN   A 1 107 ? 20.603 -12.790 -13.780 0.50 40.02 ?  107 GLN   A HE21 1 
ATOM   2377 H  HE21 B GLN   A 1 107 ? 20.771 -14.401 -13.328 0.50 37.77 ?  107 GLN   A HE21 1 
ATOM   2378 H  HE22 A GLN   A 1 107 ? 19.889 -13.951 -13.180 0.50 40.02 ?  107 GLN   A HE22 1 
ATOM   2379 H  HE22 B GLN   A 1 107 ? 20.330 -15.467 -12.387 0.50 37.77 ?  107 GLN   A HE22 1 
ATOM   2380 N  N    A LEU   A 1 108 ? 24.708 -10.751 -9.725  0.50 16.74 ?  108 LEU   A N    1 
ATOM   2381 N  N    B LEU   A 1 108 ? 24.890 -10.997 -9.622  0.50 16.16 ?  108 LEU   A N    1 
ATOM   2382 C  CA   A LEU   A 1 108 ? 25.664 -10.428 -8.674  0.50 15.15 ?  108 LEU   A CA   1 
ATOM   2383 C  CA   B LEU   A 1 108 ? 25.749 -10.468 -8.574  0.50 15.01 ?  108 LEU   A CA   1 
ATOM   2384 C  C    A LEU   A 1 108 ? 25.000 -10.261 -7.315  0.50 13.48 ?  108 LEU   A C    1 
ATOM   2385 C  C    B LEU   A 1 108 ? 25.005 -10.257 -7.263  0.50 13.52 ?  108 LEU   A C    1 
ATOM   2386 O  O    A LEU   A 1 108 ? 25.705 -10.114 -6.313  0.50 13.59 ?  108 LEU   A O    1 
ATOM   2387 O  O    B LEU   A 1 108 ? 25.659 -10.068 -6.233  0.50 13.94 ?  108 LEU   A O    1 
ATOM   2388 C  CB   A LEU   A 1 108 ? 26.450 -9.170  -9.053  0.50 15.37 ?  108 LEU   A CB   1 
ATOM   2389 C  CB   B LEU   A 1 108 ? 26.414 -9.170  -9.041  0.50 15.40 ?  108 LEU   A CB   1 
ATOM   2390 C  CG   A LEU   A 1 108 ? 27.406 -9.374  -10.231 0.50 16.34 ?  108 LEU   A CG   1 
ATOM   2391 C  CG   B LEU   A 1 108 ? 27.460 -9.356  -10.142 0.50 16.47 ?  108 LEU   A CG   1 
ATOM   2392 C  CD1  A LEU   A 1 108 ? 27.946 -8.047  -10.741 0.50 17.03 ?  108 LEU   A CD1  1 
ATOM   2393 C  CD1  B LEU   A 1 108 ? 27.834 -8.025  -10.772 0.50 17.18 ?  108 LEU   A CD1  1 
ATOM   2394 C  CD2  A LEU   A 1 108 ? 28.552 -10.300 -9.843  0.50 17.33 ?  108 LEU   A CD2  1 
ATOM   2395 C  CD2  B LEU   A 1 108 ? 28.696 -10.042 -9.586  0.50 17.42 ?  108 LEU   A CD2  1 
ATOM   2396 H  H    A LEU   A 1 108 ? 24.541 -10.111 -10.262 0.50 20.12 ?  108 LEU   A H    1 
ATOM   2397 H  H    B LEU   A 1 108 ? 24.786 -10.478 -10.292 0.50 19.43 ?  108 LEU   A H    1 
ATOM   2398 H  HA   A LEU   A 1 108 ? 26.294 -11.161 -8.595  0.50 18.22 ?  108 LEU   A HA   1 
ATOM   2399 H  HA   B LEU   A 1 108 ? 26.451 -11.113 -8.398  0.50 18.05 ?  108 LEU   A HA   1 
ATOM   2400 H  HB2  A LEU   A 1 108 ? 25.822 -8.474  -9.300  0.50 18.48 ?  108 LEU   A HB2  1 
ATOM   2401 H  HB2  B LEU   A 1 108 ? 25.732 -8.574  -9.381  0.50 18.51 ?  108 LEU   A HB2  1 
ATOM   2402 H  HB3  A LEU   A 1 108 ? 26.974 -8.890  -8.290  0.50 18.48 ?  108 LEU   A HB3  1 
ATOM   2403 H  HB3  B LEU   A 1 108 ? 26.858 -8.763  -8.284  0.50 18.51 ?  108 LEU   A HB3  1 
ATOM   2404 H  HG   A LEU   A 1 108 ? 26.922 -9.795  -10.959 0.50 19.64 ?  108 LEU   A HG   1 
ATOM   2405 H  HG   B LEU   A 1 108 ? 27.093 -9.925  -10.838 0.50 19.79 ?  108 LEU   A HG   1 
ATOM   2406 H  HD11 A LEU   A 1 108 ? 28.540 -8.213  -11.491 0.50 20.47 ?  108 LEU   A HD11 1 
ATOM   2407 H  HD11 B LEU   A 1 108 ? 28.450 -8.184  -11.506 0.50 20.65 ?  108 LEU   A HD11 1 
ATOM   2408 H  HD12 A LEU   A 1 108 ? 27.202 -7.492  -11.026 0.50 20.47 ?  108 LEU   A HD12 1 
ATOM   2409 H  HD12 B LEU   A 1 108 ? 27.030 -7.596  -11.103 0.50 20.65 ?  108 LEU   A HD12 1 
ATOM   2410 H  HD13 A LEU   A 1 108 ? 28.431 -7.607  -10.026 0.50 20.47 ?  108 LEU   A HD13 1 
ATOM   2411 H  HD13 B LEU   A 1 108 ? 28.257 -7.466  -10.102 0.50 20.65 ?  108 LEU   A HD13 1 
ATOM   2412 H  HD21 A LEU   A 1 108 ? 29.228 -10.272 -10.536 0.50 20.83 ?  108 LEU   A HD21 1 
ATOM   2413 H  HD21 B LEU   A 1 108 ? 29.393 -10.032 -10.260 0.50 20.94 ?  108 LEU   A HD21 1 
ATOM   2414 H  HD22 A LEU   A 1 108 ? 28.927 -9.997  -9.001  0.50 20.83 ?  108 LEU   A HD22 1 
ATOM   2415 H  HD22 B LEU   A 1 108 ? 28.992 -9.565  -8.796  0.50 20.94 ?  108 LEU   A HD22 1 
ATOM   2416 H  HD23 A LEU   A 1 108 ? 28.211 -11.202 -9.747  0.50 20.83 ?  108 LEU   A HD23 1 
ATOM   2417 H  HD23 B LEU   A 1 108 ? 28.474 -10.958 -9.355  0.50 20.94 ?  108 LEU   A HD23 1 
ATOM   2418 N  N    . LEU   A 1 109 ? 23.668 -10.310 -7.257  1.00 13.15 ?  109 LEU   A N    1 
ATOM   2419 C  CA   . LEU   A 1 109 ? 22.964 -10.188 -5.988  1.00 12.53 ?  109 LEU   A CA   1 
ATOM   2420 C  C    . LEU   A 1 109 ? 23.306 -11.344 -5.054  1.00 11.65 ?  109 LEU   A C    1 
ATOM   2421 O  O    . LEU   A 1 109 ? 23.440 -11.151 -3.840  1.00 12.20 ?  109 LEU   A O    1 
ATOM   2422 C  CB   . LEU   A 1 109 ? 21.460 -10.104 -6.238  1.00 13.22 ?  109 LEU   A CB   1 
ATOM   2423 C  CG   . LEU   A 1 109 ? 20.580 -9.812  -5.025  1.00 13.78 ?  109 LEU   A CG   1 
ATOM   2424 C  CD1  . LEU   A 1 109 ? 21.040 -8.554  -4.307  1.00 14.10 ?  109 LEU   A CD1  1 
ATOM   2425 C  CD2  . LEU   A 1 109 ? 19.124 -9.680  -5.453  1.00 15.00 ?  109 LEU   A CD2  1 
ATOM   2426 H  H    A LEU   A 1 109 ? 23.152 -10.412 -7.937  0.50 15.81 ?  109 LEU   A H    1 
ATOM   2427 H  H    B LEU   A 1 109 ? 23.166 -10.416 -7.947  0.50 15.81 ?  109 LEU   A H    1 
ATOM   2428 H  HA   . LEU   A 1 109 ? 23.246 -9.366  -5.557  1.00 15.07 ?  109 LEU   A HA   1 
ATOM   2429 H  HB2  . LEU   A 1 109 ? 21.301 -9.396  -6.884  1.00 15.90 ?  109 LEU   A HB2  1 
ATOM   2430 H  HB3  . LEU   A 1 109 ? 21.167 -10.948 -6.611  1.00 15.90 ?  109 LEU   A HB3  1 
ATOM   2431 H  HG   . LEU   A 1 109 ? 20.641 -10.554 -4.406  1.00 16.57 ?  109 LEU   A HG   1 
ATOM   2432 H  HD11 . LEU   A 1 109 ? 20.350 -8.267  -3.694  1.00 16.95 ?  109 LEU   A HD11 1 
ATOM   2433 H  HD12 . LEU   A 1 109 ? 21.859 -8.747  -3.824  1.00 16.95 ?  109 LEU   A HD12 1 
ATOM   2434 H  HD13 . LEU   A 1 109 ? 21.205 -7.856  -4.967  1.00 16.95 ?  109 LEU   A HD13 1 
ATOM   2435 H  HD21 . LEU   A 1 109 ? 18.594 -9.397  -4.690  1.00 18.04 ?  109 LEU   A HD21 1 
ATOM   2436 H  HD22 . LEU   A 1 109 ? 19.057 -9.024  -6.163  1.00 18.04 ?  109 LEU   A HD22 1 
ATOM   2437 H  HD23 . LEU   A 1 109 ? 18.805 -10.543 -5.771  1.00 18.04 ?  109 LEU   A HD23 1 
ATOM   2438 N  N    . LYS   A 1 110 ? 23.459 -12.556 -5.597  1.00 11.78 ?  110 LYS   A N    1 
ATOM   2439 C  CA   . LYS   A 1 110 ? 23.845 -13.682 -4.748  1.00 11.85 ?  110 LYS   A CA   1 
ATOM   2440 C  C    . LYS   A 1 110 ? 25.229 -13.460 -4.144  1.00 11.41 ?  110 LYS   A C    1 
ATOM   2441 O  O    . LYS   A 1 110 ? 25.432 -13.661 -2.944  1.00 11.67 ?  110 LYS   A O    1 
ATOM   2442 C  CB   . LYS   A 1 110 ? 23.761 -15.004 -5.520  1.00 12.73 ?  110 LYS   A CB   1 
ATOM   2443 C  CG   . LYS   A 1 110 ? 23.952 -16.224 -4.617  1.00 12.88 ?  110 LYS   A CG   1 
ATOM   2444 C  CD   . LYS   A 1 110 ? 23.746 -17.537 -5.348  1.00 13.74 ?  110 LYS   A CD   1 
ATOM   2445 C  CE   . LYS   A 1 110 ? 23.839 -18.728 -4.408  1.00 14.74 ?  110 LYS   A CE   1 
ATOM   2446 N  NZ   . LYS   A 1 110 ? 22.663 -18.862 -3.514  1.00 15.30 ?  110 LYS   A NZ   1 
ATOM   2447 H  H    . LYS   A 1 110 ? 23.353 -12.749 -6.428  1.00 14.17 ?  110 LYS   A H    1 
ATOM   2448 H  HA   . LYS   A 1 110 ? 23.208 -13.738 -4.012  1.00 14.25 ?  110 LYS   A HA   1 
ATOM   2449 H  HB2  . LYS   A 1 110 ? 22.884 -15.072 -5.936  1.00 15.31 ?  110 LYS   A HB2  1 
ATOM   2450 H  HB3  . LYS   A 1 110 ? 24.452 -15.018 -6.194  1.00 15.31 ?  110 LYS   A HB3  1 
ATOM   2451 H  HG2  . LYS   A 1 110 ? 24.850 -16.215 -4.256  1.00 15.49 ?  110 LYS   A HG2  1 
ATOM   2452 H  HG3  . LYS   A 1 110 ? 23.304 -16.184 -3.891  1.00 15.49 ?  110 LYS   A HG3  1 
ATOM   2453 H  HD2  . LYS   A 1 110 ? 22.871 -17.540 -5.760  1.00 16.52 ?  110 LYS   A HD2  1 
ATOM   2454 H  HD3  . LYS   A 1 110 ? 24.438 -17.630 -6.023  1.00 16.52 ?  110 LYS   A HD3  1 
ATOM   2455 H  HE2  . LYS   A 1 110 ? 23.907 -19.540 -4.933  1.00 17.72 ?  110 LYS   A HE2  1 
ATOM   2456 H  HE3  . LYS   A 1 110 ? 24.624 -18.629 -3.846  1.00 17.72 ?  110 LYS   A HE3  1 
ATOM   2457 H  HZ1  . LYS   A 1 110 ? 22.755 -19.570 -2.987  1.00 18.39 ?  110 LYS   A HZ1  1 
ATOM   2458 H  HZ2  . LYS   A 1 110 ? 22.574 -18.132 -3.012  1.00 18.39 ?  110 LYS   A HZ2  1 
ATOM   2459 H  HZ3  . LYS   A 1 110 ? 21.920 -18.962 -4.003  1.00 18.39 ?  110 LYS   A HZ3  1 
ATOM   2460 N  N    . SER   A 1 111 ? 26.186 -13.013 -4.963  1.00 11.52 ?  111 SER   A N    1 
ATOM   2461 C  CA   . SER   A 1 111 ? 27.517 -12.705 -4.449  1.00 11.71 ?  111 SER   A CA   1 
ATOM   2462 C  C    . SER   A 1 111 ? 27.449 -11.666 -3.335  1.00 11.11 ?  111 SER   A C    1 
ATOM   2463 O  O    . SER   A 1 111 ? 28.147 -11.781 -2.319  1.00 11.67 ?  111 SER   A O    1 
ATOM   2464 C  CB   . SER   A 1 111 ? 28.405 -12.209 -5.591  1.00 12.89 ?  111 SER   A CB   1 
ATOM   2465 O  OG   . SER   A 1 111 ? 28.485 -13.197 -6.607  1.00 14.82 ?  111 SER   A OG   1 
ATOM   2466 H  H    . SER   A 1 111 ? 26.081 -12.881 -5.803  1.00 13.86 ?  111 SER   A H    1 
ATOM   2467 H  HA   . SER   A 1 111 ? 27.911 -13.513 -4.087  1.00 14.08 ?  111 SER   A HA   1 
ATOM   2468 H  HB2  . SER   A 1 111 ? 28.012 -11.405 -5.969  1.00 15.50 ?  111 SER   A HB2  1 
ATOM   2469 H  HB3  . SER   A 1 111 ? 29.288 -12.019 -5.244  1.00 15.50 ?  111 SER   A HB3  1 
ATOM   2470 H  HG   . SER   A 1 111 ? 28.991 -12.921 -7.231  1.00 17.81 ?  111 SER   A HG   1 
ATOM   2471 N  N    . ALA   A 1 112 ? 26.606 -10.643 -3.510  1.00 11.23 ?  112 ALA   A N    1 
ATOM   2472 C  CA   . ALA   A 1 112 ? 26.456 -9.607  -2.489  1.00 11.20 ?  112 ALA   A CA   1 
ATOM   2473 C  C    . ALA   A 1 112 ? 25.987 -10.214 -1.168  1.00 11.02 ?  112 ALA   A C    1 
ATOM   2474 O  O    . ALA   A 1 112 ? 26.543 -9.926  -0.101  1.00 11.58 ?  112 ALA   A O    1 
ATOM   2475 C  CB   . ALA   A 1 112 ? 25.494 -8.520  -2.976  1.00 11.49 ?  112 ALA   A CB   1 
ATOM   2476 H  H    . ALA   A 1 112 ? 26.120 -10.520 -4.207  1.00 13.51 ?  112 ALA   A H    1 
ATOM   2477 H  HA   . ALA   A 1 112 ? 27.315 -9.187  -2.330  1.00 13.48 ?  112 ALA   A HA   1 
ATOM   2478 H  HB1  . ALA   A 1 112 ? 25.429 -7.822  -2.295  1.00 13.82 ?  112 ALA   A HB1  1 
ATOM   2479 H  HB2  . ALA   A 1 112 ? 25.834 -8.137  -3.799  1.00 13.82 ?  112 ALA   A HB2  1 
ATOM   2480 H  HB3  . ALA   A 1 112 ? 24.618 -8.908  -3.127  1.00 13.82 ?  112 ALA   A HB3  1 
ATOM   2481 N  N    . TYR   A 1 113 ? 24.949 -11.059 -1.216  1.00 11.32 ?  113 TYR   A N    1 
ATOM   2482 C  CA   . TYR   A 1 113 ? 24.440 -11.670 0.011   1.00 10.90 ?  113 TYR   A CA   1 
ATOM   2483 C  C    . TYR   A 1 113 ? 25.448 -12.629 0.649   1.00 10.50 ?  113 TYR   A C    1 
ATOM   2484 O  O    . TYR   A 1 113 ? 25.424 -12.817 1.868   1.00 11.04 ?  113 TYR   A O    1 
ATOM   2485 C  CB   . TYR   A 1 113 ? 23.119 -12.395 -0.260  1.00 11.52 ?  113 TYR   A CB   1 
ATOM   2486 C  CG   . TYR   A 1 113 ? 21.905 -11.497 -0.172  1.00 11.60 ?  113 TYR   A CG   1 
ATOM   2487 C  CD1  . TYR   A 1 113 ? 21.549 -10.899 1.030   1.00 11.68 ?  113 TYR   A CD1  1 
ATOM   2488 C  CD2  . TYR   A 1 113 ? 21.102 -11.265 -1.280  1.00 11.59 ?  113 TYR   A CD2  1 
ATOM   2489 C  CE1  . TYR   A 1 113 ? 20.423 -10.099 1.130   1.00 12.11 ?  113 TYR   A CE1  1 
ATOM   2490 C  CE2  . TYR   A 1 113 ? 19.956 -10.455 -1.191  1.00 12.18 ?  113 TYR   A CE2  1 
ATOM   2491 C  CZ   . TYR   A 1 113 ? 19.628 -9.881  0.018   1.00 12.05 ?  113 TYR   A CZ   1 
ATOM   2492 O  OH   . TYR   A 1 113 ? 18.504 -9.088  0.141   1.00 12.93 ?  113 TYR   A OH   1 
ATOM   2493 H  H    . TYR   A 1 113 ? 24.535 -11.286 -1.935  1.00 13.62 ?  113 TYR   A H    1 
ATOM   2494 H  HA   . TYR   A 1 113 ? 24.269 -10.966 0.652   1.00 13.12 ?  113 TYR   A HA   1 
ATOM   2495 H  HB2  . TYR   A 1 113 ? 23.147 -12.765 -1.156  1.00 13.85 ?  113 TYR   A HB2  1 
ATOM   2496 H  HB3  . TYR   A 1 113 ? 23.017 -13.103 0.390   1.00 13.85 ?  113 TYR   A HB3  1 
ATOM   2497 H  HD1  . TYR   A 1 113 ? 22.076 -11.051 1.786   1.00 14.04 ?  113 TYR   A HD1  1 
ATOM   2498 H  HD2  . TYR   A 1 113 ? 21.317 -11.662 -2.090  1.00 13.94 ?  113 TYR   A HD2  1 
ATOM   2499 H  HE1  . TYR   A 1 113 ? 20.204 -9.713  1.945   1.00 14.57 ?  113 TYR   A HE1  1 
ATOM   2500 H  HE2  . TYR   A 1 113 ? 19.421 -10.310 -1.938  1.00 14.64 ?  113 TYR   A HE2  1 
ATOM   2501 H  HH   . TYR   A 1 113 ? 18.114 -9.037  -0.607  1.00 15.55 ?  113 TYR   A HH   1 
ATOM   2502 N  N    . GLU   A 1 114 ? 26.345 -13.237 -0.142  1.00 10.88 ?  114 GLU   A N    1 
ATOM   2503 C  CA   . GLU   A 1 114 ? 27.342 -14.133 0.445   1.00 11.30 ?  114 GLU   A CA   1 
ATOM   2504 C  C    . GLU   A 1 114 ? 28.200 -13.425 1.492   1.00 11.23 ?  114 GLU   A C    1 
ATOM   2505 O  O    . GLU   A 1 114 ? 28.677 -14.069 2.439   1.00 11.53 ?  114 GLU   A O    1 
ATOM   2506 C  CB   . GLU   A 1 114 ? 28.212 -14.767 -0.652  1.00 11.18 ?  114 GLU   A CB   1 
ATOM   2507 C  CG   . GLU   A 1 114 ? 27.450 -15.823 -1.435  1.00 11.91 ?  114 GLU   A CG   1 
ATOM   2508 C  CD   . GLU   A 1 114 ? 28.156 -16.352 -2.680  1.00 12.03 ?  114 GLU   A CD   1 
ATOM   2509 O  OE1  . GLU   A 1 114 ? 29.104 -15.710 -3.179  1.00 12.15 ?  114 GLU   A OE1  1 
ATOM   2510 O  OE2  . GLU   A 1 114 ? 27.717 -17.416 -3.177  1.00 13.27 -1 114 GLU   A OE2  1 
ATOM   2511 H  H    . GLU   A 1 114 ? 26.393 -13.141 -1.003  1.00 13.09 ?  114 GLU   A H    1 
ATOM   2512 H  HA   . GLU   A 1 114 ? 26.873 -14.853 0.885   1.00 13.59 ?  114 GLU   A HA   1 
ATOM   2513 H  HB2  . GLU   A 1 114 ? 28.495 -14.074 -1.278  1.00 13.45 ?  114 GLU   A HB2  1 
ATOM   2514 H  HB3  . GLU   A 1 114 ? 28.984 -15.184 -0.248  1.00 13.45 ?  114 GLU   A HB3  1 
ATOM   2515 H  HG2  . GLU   A 1 114 ? 27.293 -16.582 -0.854  1.00 14.32 ?  114 GLU   A HG2  1 
ATOM   2516 H  HG3  . GLU   A 1 114 ? 26.600 -15.450 -1.719  1.00 14.32 ?  114 GLU   A HG3  1 
ATOM   2517 N  N    . ASN   A 1 115 ? 28.385 -12.106 1.362   1.00 10.95 ?  115 ASN   A N    1 
ATOM   2518 C  CA   . ASN   A 1 115 ? 29.150 -11.377 2.368   1.00 11.18 ?  115 ASN   A CA   1 
ATOM   2519 C  C    . ASN   A 1 115 ? 28.542 -11.519 3.758   1.00 10.98 ?  115 ASN   A C    1 
ATOM   2520 O  O    . ASN   A 1 115 ? 29.263 -11.454 4.762   1.00 11.56 ?  115 ASN   A O    1 
ATOM   2521 C  CB   . ASN   A 1 115 ? 29.256 -9.899  1.995   1.00 11.37 ?  115 ASN   A CB   1 
ATOM   2522 C  CG   . ASN   A 1 115 ? 30.055 -9.680  0.734   1.00 12.20 ?  115 ASN   A CG   1 
ATOM   2523 O  OD1  . ASN   A 1 115 ? 31.274 -9.796  0.739   1.00 15.51 ?  115 ASN   A OD1  1 
ATOM   2524 N  ND2  . ASN   A 1 115 ? 29.377 -9.372  -0.354  1.00 11.89 ?  115 ASN   A ND2  1 
ATOM   2525 H  H    . ASN   A 1 115 ? 28.078 -11.622 0.717   1.00 13.17 ?  115 ASN   A H    1 
ATOM   2526 H  HA   . ASN   A 1 115 ? 30.045 -11.743 2.400   1.00 13.44 ?  115 ASN   A HA   1 
ATOM   2527 H  HB2  . ASN   A 1 115 ? 28.366 -9.540  1.865   1.00 13.68 ?  115 ASN   A HB2  1 
ATOM   2528 H  HB3  . ASN   A 1 115 ? 29.701 -9.425  2.721   1.00 13.68 ?  115 ASN   A HB3  1 
ATOM   2529 H  HD21 . ASN   A 1 115 ? 29.788 -9.238  -1.095  1.00 14.30 ?  115 ASN   A HD21 1 
ATOM   2530 H  HD22 . ASN   A 1 115 ? 28.518 -9.315  -0.321  1.00 14.30 ?  115 ASN   A HD22 1 
ATOM   2531 N  N    . PHE   A 1 116 ? 27.219 -11.690 3.843   1.00 11.11 ?  116 PHE   A N    1 
ATOM   2532 C  CA   . PHE   A 1 116 ? 26.576 -11.793 5.150   1.00 11.04 ?  116 PHE   A CA   1 
ATOM   2533 C  C    . PHE   A 1 116 ? 27.057 -13.026 5.916   1.00 11.43 ?  116 PHE   A C    1 
ATOM   2534 O  O    . PHE   A 1 116 ? 26.977 -13.051 7.145   1.00 11.89 ?  116 PHE   A O    1 
ATOM   2535 C  CB   . PHE   A 1 116 ? 25.046 -11.918 5.024   1.00 11.33 ?  116 PHE   A CB   1 
ATOM   2536 C  CG   . PHE   A 1 116 ? 24.290 -10.670 4.559   1.00 11.02 ?  116 PHE   A CG   1 
ATOM   2537 C  CD1  . PHE   A 1 116 ? 24.860 -9.644  3.811   1.00 11.02 ?  116 PHE   A CD1  1 
ATOM   2538 C  CD2  . PHE   A 1 116 ? 22.934 -10.572 4.876   1.00 12.01 ?  116 PHE   A CD2  1 
ATOM   2539 C  CE1  . PHE   A 1 116 ? 24.087 -8.563  3.395   1.00 11.57 ?  116 PHE   A CE1  1 
ATOM   2540 C  CE2  . PHE   A 1 116 ? 22.165 -9.496  4.467   1.00 12.11 ?  116 PHE   A CE2  1 
ATOM   2541 C  CZ   . PHE   A 1 116 ? 22.738 -8.491  3.726   1.00 11.37 ?  116 PHE   A CZ   1 
ATOM   2542 H  H    . PHE   A 1 116 ? 26.681 -11.741 3.171   1.00 13.37 ?  116 PHE   A H    1 
ATOM   2543 H  HA   . PHE   A 1 116 ? 26.773 -11.000 5.675   1.00 13.28 ?  116 PHE   A HA   1 
ATOM   2544 H  HB2  . PHE   A 1 116 ? 24.853 -12.627 4.388   1.00 13.63 ?  116 PHE   A HB2  1 
ATOM   2545 H  HB3  . PHE   A 1 116 ? 24.690 -12.166 5.893   1.00 13.63 ?  116 PHE   A HB3  1 
ATOM   2546 H  HD1  . PHE   A 1 116 ? 25.753 -9.696  3.580   1.00 13.26 ?  116 PHE   A HD1  1 
ATOM   2547 H  HD2  . PHE   A 1 116 ? 22.532 -11.265 5.368   1.00 14.45 ?  116 PHE   A HD2  1 
ATOM   2548 H  HE1  . PHE   A 1 116 ? 24.474 -7.883  2.901   1.00 13.92 ?  116 PHE   A HE1  1 
ATOM   2549 H  HE2  . PHE   A 1 116 ? 21.262 -9.468  4.696   1.00 14.56 ?  116 PHE   A HE2  1 
ATOM   2550 H  HZ   . PHE   A 1 116 ? 22.225 -7.766  3.459   1.00 13.68 ?  116 PHE   A HZ   1 
ATOM   2551 N  N    . ASN   A 1 117 ? 27.499 -14.075 5.211   1.00 11.47 ?  117 ASN   A N    1 
ATOM   2552 C  CA   . ASN   A 1 117 ? 27.866 -15.323 5.878   1.00 11.68 ?  117 ASN   A CA   1 
ATOM   2553 C  C    . ASN   A 1 117 ? 29.132 -15.204 6.707   1.00 12.23 ?  117 ASN   A C    1 
ATOM   2554 O  O    . ASN   A 1 117 ? 29.442 -16.125 7.466   1.00 13.20 ?  117 ASN   A O    1 
ATOM   2555 C  CB   . ASN   A 1 117 ? 27.976 -16.446 4.854   1.00 11.94 ?  117 ASN   A CB   1 
ATOM   2556 C  CG   . ASN   A 1 117 ? 26.622 -16.830 4.316   1.00 11.91 ?  117 ASN   A CG   1 
ATOM   2557 O  OD1  . ASN   A 1 117 ? 25.646 -16.865 5.069   1.00 12.74 ?  117 ASN   A OD1  1 
ATOM   2558 N  ND2  . ASN   A 1 117 ? 26.533 -17.078 3.020   1.00 11.77 ?  117 ASN   A ND2  1 
ATOM   2559 H  H    . ASN   A 1 117 ? 27.575 -14.084 4.354   1.00 13.79 ?  117 ASN   A H    1 
ATOM   2560 H  HA   . ASN   A 1 117 ? 27.144 -15.552 6.484   1.00 14.05 ?  117 ASN   A HA   1 
ATOM   2561 H  HB2  . ASN   A 1 117 ? 28.532 -16.149 4.114   1.00 14.36 ?  117 ASN   A HB2  1 
ATOM   2562 H  HB3  . ASN   A 1 117 ? 28.365 -17.221 5.279   1.00 14.36 ?  117 ASN   A HB3  1 
ATOM   2563 H  HD21 . ASN   A 1 117 ? 25.780 -17.289 2.675   1.00 14.16 ?  117 ASN   A HD21 1 
ATOM   2564 H  HD22 . ASN   A 1 117 ? 27.238 -17.021 2.524   1.00 14.16 ?  117 ASN   A HD22 1 
ATOM   2565 N  N    . GLN   A 1 118 ? 29.861 -14.095 6.589   1.00 12.05 ?  118 GLN   A N    1 
ATOM   2566 C  CA   . GLN   A 1 118 ? 31.043 -13.855 7.405   1.00 12.77 ?  118 GLN   A CA   1 
ATOM   2567 C  C    . GLN   A 1 118 ? 30.707 -13.282 8.777   1.00 12.67 ?  118 GLN   A C    1 
ATOM   2568 O  O    . GLN   A 1 118 ? 31.626 -12.989 9.550   1.00 14.45 ?  118 GLN   A O    1 
ATOM   2569 C  CB   . GLN   A 1 118 ? 32.024 -12.943 6.663   1.00 12.78 ?  118 GLN   A CB   1 
ATOM   2570 C  CG   . GLN   A 1 118 ? 32.496 -13.523 5.338   1.00 12.72 ?  118 GLN   A CG   1 
ATOM   2571 C  CD   . GLN   A 1 118 ? 33.329 -14.784 5.508   1.00 13.12 ?  118 GLN   A CD   1 
ATOM   2572 O  OE1  . GLN   A 1 118 ? 34.193 -14.859 6.393   1.00 14.06 ?  118 GLN   A OE1  1 
ATOM   2573 N  NE2  . GLN   A 1 118 ? 33.076 -15.783 4.663   1.00 13.30 ?  118 GLN   A NE2  1 
ATOM   2574 H  H    . GLN   A 1 118 ? 29.676 -13.442 6.046   1.00 14.49 ?  118 GLN   A H    1 
ATOM   2575 H  HA   . GLN   A 1 118 ? 31.478 -14.706 7.548   1.00 15.36 ?  118 GLN   A HA   1 
ATOM   2576 H  HB2  . GLN   A 1 118 ? 31.594 -12.095 6.488   1.00 15.37 ?  118 GLN   A HB2  1 
ATOM   2577 H  HB3  . GLN   A 1 118 ? 32.805 -12.809 7.226   1.00 15.37 ?  118 GLN   A HB3  1 
ATOM   2578 H  HG2  . GLN   A 1 118 ? 31.723 -13.739 4.793   1.00 15.30 ?  118 GLN   A HG2  1 
ATOM   2579 H  HG3  . GLN   A 1 118 ? 33.043 -12.860 4.885   1.00 15.30 ?  118 GLN   A HG3  1 
ATOM   2580 H  HE21 . GLN   A 1 118 ? 32.464 -15.691 4.058   1.00 15.99 ?  118 GLN   A HE21 1 
ATOM   2581 H  HE22 . GLN   A 1 118 ? 33.518 -16.515 4.713   1.00 15.99 ?  118 GLN   A HE22 1 
ATOM   2582 N  N    . HIS   A 1 119 ? 29.420 -13.129 9.096   1.00 12.28 ?  119 HIS   A N    1 
ATOM   2583 C  CA   . HIS   A 1 119 ? 28.964 -12.523 10.343  1.00 12.96 ?  119 HIS   A CA   1 
ATOM   2584 C  C    . HIS   A 1 119 ? 27.827 -13.351 10.919  1.00 13.12 ?  119 HIS   A C    1 
ATOM   2585 O  O    . HIS   A 1 119 ? 26.877 -13.683 10.205  1.00 13.74 ?  119 HIS   A O    1 
ATOM   2586 C  CB   . HIS   A 1 119 ? 28.499 -11.089 10.078  1.00 13.53 ?  119 HIS   A CB   1 
ATOM   2587 C  CG   . HIS   A 1 119 ? 29.573 -10.270 9.462   1.00 14.64 ?  119 HIS   A CG   1 
ATOM   2588 N  ND1  . HIS   A 1 119 ? 30.557 -9.671  10.214  1.00 16.85 ?  119 HIS   A ND1  1 
ATOM   2589 C  CD2  . HIS   A 1 119 ? 29.904 -10.070 8.166   1.00 15.88 ?  119 HIS   A CD2  1 
ATOM   2590 C  CE1  . HIS   A 1 119 ? 31.418 -9.082  9.403   1.00 17.42 ?  119 HIS   A CE1  1 
ATOM   2591 N  NE2  . HIS   A 1 119 ? 31.052 -9.316  8.156   1.00 17.54 ?  119 HIS   A NE2  1 
ATOM   2592 H  H    . HIS   A 1 119 ? 28.767 -13.392 8.595   1.00 14.77 ?  119 HIS   A H    1 
ATOM   2593 H  HA   . HIS   A 1 119 ? 29.692 -12.511 10.986  1.00 15.58 ?  119 HIS   A HA   1 
ATOM   2594 H  HB2  . HIS   A 1 119 ? 27.742 -11.112 9.473   1.00 16.27 ?  119 HIS   A HB2  1 
ATOM   2595 H  HB3  . HIS   A 1 119 ? 28.247 -10.681 10.920  1.00 16.27 ?  119 HIS   A HB3  1 
ATOM   2596 H  HD2  . HIS   A 1 119 ? 29.436 -10.378 7.421   1.00 19.08 ?  119 HIS   A HD2  1 
ATOM   2597 H  HE1  . HIS   A 1 119 ? 32.155 -8.581  9.663   1.00 20.93 ?  119 HIS   A HE1  1 
ATOM   2598 H  HE2  . HIS   A 1 119 ? 31.447 -9.021  7.451   1.00 21.09 ?  119 HIS   A HE2  1 
ATOM   2599 N  N    . GLU   A 1 120 ? 27.922 -13.666 12.213  1.00 14.13 ?  120 GLU   A N    1 
ATOM   2600 C  CA   . GLU   A 1 120 ? 26.976 -14.601 12.817  1.00 16.06 ?  120 GLU   A CA   1 
ATOM   2601 C  C    . GLU   A 1 120 ? 25.557 -14.042 12.884  1.00 14.77 ?  120 GLU   A C    1 
ATOM   2602 O  O    . GLU   A 1 120 ? 24.585 -14.808 12.772  1.00 15.01 ?  120 GLU   A O    1 
ATOM   2603 C  CB   . GLU   A 1 120 ? 27.455 -15.001 14.215  1.00 21.64 ?  120 GLU   A CB   1 
ATOM   2604 C  CG   . GLU   A 1 120 ? 28.662 -15.926 14.213  1.00 29.55 ?  120 GLU   A CG   1 
ATOM   2605 C  CD   . GLU   A 1 120 ? 28.836 -16.660 15.527  1.00 36.69 ?  120 GLU   A CD   1 
ATOM   2606 O  OE1  . GLU   A 1 120 ? 28.401 -16.129 16.571  1.00 38.73 ?  120 GLU   A OE1  1 
ATOM   2607 O  OE2  . GLU   A 1 120 ? 29.407 -17.771 15.513  1.00 41.50 -1 120 GLU   A OE2  1 
ATOM   2608 H  H    . GLU   A 1 120 ? 28.518 -13.358 12.757  1.00 16.99 ?  120 GLU   A H    1 
ATOM   2609 H  HA   . GLU   A 1 120 ? 26.949 -15.405 12.284  1.00 19.31 ?  120 GLU   A HA   1 
ATOM   2610 H  HB2  . GLU   A 1 120 ? 27.700 -14.204 14.710  1.00 26.00 ?  120 GLU   A HB2  1 
ATOM   2611 H  HB3  . GLU   A 1 120 ? 26.735 -15.463 14.678  1.00 26.00 ?  120 GLU   A HB3  1 
ATOM   2612 H  HG2  . GLU   A 1 120 ? 28.561 -16.583 13.507  1.00 35.50 ?  120 GLU   A HG2  1 
ATOM   2613 H  HG3  . GLU   A 1 120 ? 29.466 -15.404 14.074  1.00 35.50 ?  120 GLU   A HG3  1 
ATOM   2614 N  N    . VAL   A 1 121 ? 25.420 -12.733 13.105  1.00 14.28 ?  121 VAL   A N    1 
ATOM   2615 C  CA   . VAL   A 1 121 ? 24.126 -12.066 13.230  1.00 14.39 ?  121 VAL   A CA   1 
ATOM   2616 C  C    . VAL   A 1 121 ? 24.239 -10.681 12.603  1.00 13.07 ?  121 VAL   A C    1 
ATOM   2617 O  O    . VAL   A 1 121 ? 25.211 -9.959  12.848  1.00 13.90 ?  121 VAL   A O    1 
ATOM   2618 C  CB   . VAL   A 1 121 ? 23.686 -11.928 14.705  1.00 17.24 ?  121 VAL   A CB   1 
ATOM   2619 C  CG1  . VAL   A 1 121 ? 22.286 -11.332 14.793  1.00 17.99 ?  121 VAL   A CG1  1 
ATOM   2620 C  CG2  . VAL   A 1 121 ? 23.733 -13.259 15.437  1.00 19.69 ?  121 VAL   A CG2  1 
ATOM   2621 H  H    . VAL   A 1 121 ? 26.085 -12.191 13.190  1.00 17.17 ?  121 VAL   A H    1 
ATOM   2622 H  HA   . VAL   A 1 121 ? 23.452 -12.575 12.753  1.00 17.31 ?  121 VAL   A HA   1 
ATOM   2623 H  HB   . VAL   A 1 121 ? 24.288 -11.322 15.158  1.00 20.72 ?  121 VAL   A HB   1 
ATOM   2624 H  HG11 . VAL   A 1 121 ? 21.974 -11.382 15.713  1.00 21.63 ?  121 VAL   A HG11 1 
ATOM   2625 H  HG12 . VAL   A 1 121 ? 22.312 -10.405 14.508  1.00 21.63 ?  121 VAL   A HG12 1 
ATOM   2626 H  HG13 . VAL   A 1 121 ? 21.686 -11.836 14.218  1.00 21.63 ?  121 VAL   A HG13 1 
ATOM   2627 H  HG21 . VAL   A 1 121 ? 23.376 -13.140 16.337  1.00 23.66 ?  121 VAL   A HG21 1 
ATOM   2628 H  HG22 . VAL   A 1 121 ? 23.189 -13.907 14.958  1.00 23.66 ?  121 VAL   A HG22 1 
ATOM   2629 H  HG23 . VAL   A 1 121 ? 24.648 -13.565 15.485  1.00 23.66 ?  121 VAL   A HG23 1 
ATOM   2630 N  N    . LEU   A 1 122 ? 23.225 -10.289 11.825  1.00 12.76 ?  122 LEU   A N    1 
ATOM   2631 C  CA   . LEU   A 1 122 ? 23.227 -8.990  11.157  1.00 12.74 ?  122 LEU   A CA   1 
ATOM   2632 C  C    . LEU   A 1 122 ? 21.828 -8.399  11.111  1.00 12.35 ?  122 LEU   A C    1 
ATOM   2633 O  O    . LEU   A 1 122 ? 20.838 -9.120  10.980  1.00 13.55 ?  122 LEU   A O    1 
ATOM   2634 C  CB   . LEU   A 1 122 ? 23.644 -9.081  9.683   1.00 14.02 ?  122 LEU   A CB   1 
ATOM   2635 C  CG   . LEU   A 1 122 ? 24.851 -9.930  9.301   1.00 14.19 ?  122 LEU   A CG   1 
ATOM   2636 C  CD1  . LEU   A 1 122 ? 24.450 -11.384 9.086   1.00 14.66 ?  122 LEU   A CD1  1 
ATOM   2637 C  CD2  . LEU   A 1 122 ? 25.509 -9.361  8.050   1.00 13.40 ?  122 LEU   A CD2  1 
ATOM   2638 H  H    . LEU   A 1 122 ? 22.519 -10.761 11.666  1.00 15.34 ?  122 LEU   A H    1 
ATOM   2639 H  HA   . LEU   A 1 122 ? 23.820 -8.377  11.618  1.00 15.32 ?  122 LEU   A HA   1 
ATOM   2640 H  HB2  . LEU   A 1 122 ? 22.900 -9.439  9.185   1.00 16.85 ?  122 LEU   A HB2  1 
ATOM   2641 H  HB3  . LEU   A 1 122 ? 23.839 -8.187  9.374   1.00 16.85 ?  122 LEU   A HB3  1 
ATOM   2642 H  HG   . LEU   A 1 122 ? 25.513 -9.905  10.012  1.00 17.07 ?  122 LEU   A HG   1 
ATOM   2643 H  HD11 . LEU   A 1 122 ? 25.224 -11.894 8.795   1.00 17.62 ?  122 LEU   A HD11 1 
ATOM   2644 H  HD12 . LEU   A 1 122 ? 24.117 -11.745 9.924   1.00 17.62 ?  122 LEU   A HD12 1 
ATOM   2645 H  HD13 . LEU   A 1 122 ? 23.756 -11.426 8.411   1.00 17.62 ?  122 LEU   A HD13 1 
ATOM   2646 H  HD21 . LEU   A 1 122 ? 26.254 -9.933  7.789   1.00 16.11 ?  122 LEU   A HD21 1 
ATOM   2647 H  HD22 . LEU   A 1 122 ? 24.857 -9.329  7.334   1.00 16.11 ?  122 LEU   A HD22 1 
ATOM   2648 H  HD23 . LEU   A 1 122 ? 25.837 -8.468  8.241   1.00 16.11 ?  122 LEU   A HD23 1 
ATOM   2649 N  N    A LEU   A 1 123 ? 21.765 -7.071  11.208  0.50 11.93 ?  123 LEU   A N    1 
ATOM   2650 N  N    B LEU   A 1 123 ? 21.772 -7.071  11.208  0.50 12.11 ?  123 LEU   A N    1 
ATOM   2651 C  CA   A LEU   A 1 123 ? 20.598 -6.283  10.821  0.50 11.68 ?  123 LEU   A CA   1 
ATOM   2652 C  CA   B LEU   A 1 123 ? 20.589 -6.279  10.885  0.50 12.09 ?  123 LEU   A CA   1 
ATOM   2653 C  C    A LEU   A 1 123 ? 20.839 -5.756  9.415   0.50 10.72 ?  123 LEU   A C    1 
ATOM   2654 C  C    B LEU   A 1 123 ? 20.799 -5.718  9.483   0.50 11.62 ?  123 LEU   A C    1 
ATOM   2655 O  O    A LEU   A 1 123 ? 21.944 -5.295  9.113   0.50 10.23 ?  123 LEU   A O    1 
ATOM   2656 O  O    B LEU   A 1 123 ? 21.763 -4.976  9.259   0.50 11.82 ?  123 LEU   A O    1 
ATOM   2657 C  CB   A LEU   A 1 123 ? 20.438 -5.089  11.763  0.50 12.41 ?  123 LEU   A CB   1 
ATOM   2658 C  CB   B LEU   A 1 123 ? 20.456 -5.130  11.885  0.50 12.63 ?  123 LEU   A CB   1 
ATOM   2659 C  CG   A LEU   A 1 123 ? 19.371 -4.052  11.415  0.50 13.38 ?  123 LEU   A CG   1 
ATOM   2660 C  CG   B LEU   A 1 123 ? 19.457 -4.027  11.528  0.50 12.94 ?  123 LEU   A CG   1 
ATOM   2661 C  CD1  A LEU   A 1 123 ? 17.981 -4.676  11.439  0.50 14.01 ?  123 LEU   A CD1  1 
ATOM   2662 C  CD1  B LEU   A 1 123 ? 18.036 -4.574  11.539  0.50 13.74 ?  123 LEU   A CD1  1 
ATOM   2663 C  CD2  A LEU   A 1 123 ? 19.458 -2.884  12.387  0.50 14.12 ?  123 LEU   A CD2  1 
ATOM   2664 C  CD2  B LEU   A 1 123 ? 19.598 -2.842  12.473  0.50 13.29 ?  123 LEU   A CD2  1 
ATOM   2665 H  H    A LEU   A 1 123 ? 22.415 -6.586  11.502  0.50 14.35 ?  123 LEU   A H    1 
ATOM   2666 H  H    B LEU   A 1 123 ? 22.438 -6.583  11.460  0.50 14.56 ?  123 LEU   A H    1 
ATOM   2667 H  HA   A LEU   A 1 123 ? 19.798 -6.831  10.835  0.50 14.04 ?  123 LEU   A HA   1 
ATOM   2668 H  HA   B LEU   A 1 123 ? 19.788 -6.828  10.906  0.50 14.54 ?  123 LEU   A HA   1 
ATOM   2669 H  HB2  A LEU   A 1 123 ? 20.220 -5.429  12.643  0.50 14.92 ?  123 LEU   A HB2  1 
ATOM   2670 H  HB2  B LEU   A 1 123 ? 20.177 -5.500  12.739  0.50 15.19 ?  123 LEU   A HB2  1 
ATOM   2671 H  HB3  A LEU   A 1 123 ? 21.282 -4.619  11.799  0.50 14.92 ?  123 LEU   A HB3  1 
ATOM   2672 H  HB3  B LEU   A 1 123 ? 21.321 -4.709  11.984  0.50 15.19 ?  123 LEU   A HB3  1 
ATOM   2673 H  HG   A LEU   A 1 123 ? 19.528 -3.708  10.520  0.50 16.09 ?  123 LEU   A HG   1 
ATOM   2674 H  HG   B LEU   A 1 123 ? 19.637 -3.703  10.632  0.50 15.56 ?  123 LEU   A HG   1 
ATOM   2675 H  HD11 A LEU   A 1 123 ? 17.321 -3.989  11.259  0.50 16.84 ?  123 LEU   A HD11 1 
ATOM   2676 H  HD11 B LEU   A 1 123 ? 17.418 -3.857  11.333  0.50 16.52 ?  123 LEU   A HD11 1 
ATOM   2677 H  HD12 A LEU   A 1 123 ? 17.933 -5.368  10.761  0.50 16.84 ?  123 LEU   A HD12 1 
ATOM   2678 H  HD12 B LEU   A 1 123 ? 17.963 -5.277  10.872  0.50 16.52 ?  123 LEU   A HD12 1 
ATOM   2679 H  HD13 A LEU   A 1 123 ? 17.826 -5.062  12.317  0.50 16.84 ?  123 LEU   A HD13 1 
ATOM   2680 H  HD13 B LEU   A 1 123 ? 17.845 -4.935  12.419  0.50 16.52 ?  123 LEU   A HD13 1 
ATOM   2681 H  HD21 A LEU   A 1 123 ? 18.778 -2.232  12.163  0.50 16.97 ?  123 LEU   A HD21 1 
ATOM   2682 H  HD21 B LEU   A 1 123 ? 18.952 -2.163  12.224  0.50 15.98 ?  123 LEU   A HD21 1 
ATOM   2683 H  HD22 A LEU   A 1 123 ? 19.316 -3.215  13.289  0.50 16.97 ?  123 LEU   A HD22 1 
ATOM   2684 H  HD22 B LEU   A 1 123 ? 19.428 -3.144  13.379  0.50 15.98 ?  123 LEU   A HD22 1 
ATOM   2685 H  HD23 A LEU   A 1 123 ? 20.339 -2.484  12.318  0.50 16.97 ?  123 LEU   A HD23 1 
ATOM   2686 H  HD23 B LEU   A 1 123 ? 20.497 -2.492  12.401  0.50 15.98 ?  123 LEU   A HD23 1 
ATOM   2687 N  N    A ALA   A 1 124 ? 19.824 -5.810  8.549   0.50 10.30 ?  124 ALA   A N    1 
ATOM   2688 N  N    B ALA   A 1 124 ? 19.919 -6.064  8.542   0.50 11.40 ?  124 ALA   A N    1 
ATOM   2689 C  CA   A ALA   A 1 124 ? 20.092 -5.543  7.143   0.50 9.99  ?  124 ALA   A CA   1 
ATOM   2690 C  CA   B ALA   A 1 124 ? 20.196 -5.789  7.136   0.50 11.37 ?  124 ALA   A CA   1 
ATOM   2691 C  C    A ALA   A 1 124 ? 18.822 -5.071  6.443   0.50 10.07 ?  124 ALA   A C    1 
ATOM   2692 C  C    B ALA   A 1 124 ? 18.968 -5.306  6.373   0.50 10.74 ?  124 ALA   A C    1 
ATOM   2693 O  O    A ALA   A 1 124 ? 17.701 -5.387  6.876   0.50 10.66 ?  124 ALA   A O    1 
ATOM   2694 O  O    B ALA   A 1 124 ? 17.829 -5.647  6.723   0.50 11.14 ?  124 ALA   A O    1 
ATOM   2695 C  CB   A ALA   A 1 124 ? 20.635 -6.789  6.436   0.50 10.18 ?  124 ALA   A CB   1 
ATOM   2696 C  CB   B ALA   A 1 124 ? 20.778 -7.028  6.432   0.50 12.35 ?  124 ALA   A CB   1 
ATOM   2697 H  H    A ALA   A 1 124 ? 19.005 -5.990  8.747   0.50 12.40 ?  124 ALA   A H    1 
ATOM   2698 H  H    B ALA   A 1 124 ? 19.166 -6.457  8.684   0.50 13.71 ?  124 ALA   A H    1 
ATOM   2699 H  HA   A ALA   A 1 124 ? 20.761 -4.841  7.090   0.50 12.02 ?  124 ALA   A HA   1 
ATOM   2700 H  HA   B ALA   A 1 124 ? 20.868 -5.094  7.089   0.50 13.68 ?  124 ALA   A HA   1 
ATOM   2701 H  HB1  A ALA   A 1 124 ? 20.803 -6.570  5.508   0.50 12.25 ?  124 ALA   A HB1  1 
ATOM   2702 H  HB1  B ALA   A 1 124 ? 20.958 -6.818  5.501   0.50 14.85 ?  124 ALA   A HB1  1 
ATOM   2703 H  HB2  A ALA   A 1 124 ? 21.458 -7.058  6.870   0.50 12.25 ?  124 ALA   A HB2  1 
ATOM   2704 H  HB2  B ALA   A 1 124 ? 21.610 -7.284  6.873   0.50 14.85 ?  124 ALA   A HB2  1 
ATOM   2705 H  HB3  A ALA   A 1 124 ? 19.975 -7.493  6.502   0.50 12.25 ?  124 ALA   A HB3  1 
ATOM   2706 H  HB3  B ALA   A 1 124 ? 20.143 -7.759  6.489   0.50 14.85 ?  124 ALA   A HB3  1 
ATOM   2707 N  N    A PRO   A 1 125 ? 18.973 -4.335  5.343   0.50 10.84 ?  125 PRO   A N    1 
ATOM   2708 N  N    B PRO   A 1 125 ? 19.178 -4.529  5.312   0.50 9.94  ?  125 PRO   A N    1 
ATOM   2709 C  CA   A PRO   A 1 125 ? 17.895 -4.148  4.374   0.50 11.58 ?  125 PRO   A CA   1 
ATOM   2710 C  CA   B PRO   A 1 125 ? 18.095 -4.165  4.401   0.50 10.45 ?  125 PRO   A CA   1 
ATOM   2711 C  C    A PRO   A 1 125 ? 17.988 -5.221  3.290   0.50 11.17 ?  125 PRO   A C    1 
ATOM   2712 C  C    B PRO   A 1 125 ? 18.020 -5.192  3.275   0.50 11.25 ?  125 PRO   A C    1 
ATOM   2713 O  O    A PRO   A 1 125 ? 18.949 -5.990  3.219   0.50 11.52 ?  125 PRO   A O    1 
ATOM   2714 O  O    B PRO   A 1 125 ? 18.895 -6.047  3.118   0.50 11.72 ?  125 PRO   A O    1 
ATOM   2715 C  CB   A PRO   A 1 125 ? 18.241 -2.775  3.783   0.50 11.70 ?  125 PRO   A CB   1 
ATOM   2716 C  CB   B PRO   A 1 125 ? 18.599 -2.832  3.839   0.50 9.79  ?  125 PRO   A CB   1 
ATOM   2717 C  CG   A PRO   A 1 125 ? 19.753 -2.812  3.720   0.50 12.19 ?  125 PRO   A CG   1 
ATOM   2718 C  CG   B PRO   A 1 125 ? 20.074 -3.089  3.659   0.50 9.43  ?  125 PRO   A CG   1 
ATOM   2719 C  CD   A PRO   A 1 125 ? 20.188 -3.590  4.953   0.50 11.49 ?  125 PRO   A CD   1 
ATOM   2720 C  CD   B PRO   A 1 125 ? 20.464 -3.964  4.850   0.50 9.50  ?  125 PRO   A CD   1 
ATOM   2721 H  HA   A PRO   A 1 125 ? 17.023 -4.147  4.789   0.50 13.93 ?  125 PRO   A HA   1 
ATOM   2722 H  HA   B PRO   A 1 125 ? 17.242 -4.063  4.860   0.50 12.58 ?  125 PRO   A HA   1 
ATOM   2723 H  HB2  A PRO   A 1 125 ? 17.854 -2.680  2.899   0.50 14.07 ?  125 PRO   A HB2  1 
ATOM   2724 H  HB2  B PRO   A 1 125 ? 18.167 -2.643  2.992   0.50 11.78 ?  125 PRO   A HB2  1 
ATOM   2725 H  HB3  A PRO   A 1 125 ? 17.934 -2.071  4.378   0.50 14.07 ?  125 PRO   A HB3  1 
ATOM   2726 H  HB3  B PRO   A 1 125 ? 18.444 -2.121  4.480   0.50 11.78 ?  125 PRO   A HB3  1 
ATOM   2727 H  HG2  A PRO   A 1 125 ? 20.035 -3.269  2.911   0.50 14.66 ?  125 PRO   A HG2  1 
ATOM   2728 H  HG2  B PRO   A 1 125 ? 20.222 -3.556  2.818   0.50 11.34 ?  125 PRO   A HG2  1 
ATOM   2729 H  HG3  A PRO   A 1 125 ? 20.106 -1.908  3.741   0.50 14.66 ?  125 PRO   A HG3  1 
ATOM   2730 H  HG3  B PRO   A 1 125 ? 20.555 -2.247  3.670   0.50 11.34 ?  125 PRO   A HG3  1 
ATOM   2731 H  HD2  A PRO   A 1 125 ? 20.912 -4.197  4.733   0.50 13.83 ?  125 PRO   A HD2  1 
ATOM   2732 H  HD2  B PRO   A 1 125 ? 21.072 -4.667  4.561   0.50 11.43 ?  125 PRO   A HD2  1 
ATOM   2733 H  HD3  A PRO   A 1 125 ? 20.447 -2.977  5.663   0.50 13.83 ?  125 PRO   A HD3  1 
ATOM   2734 H  HD3  B PRO   A 1 125 ? 20.859 -3.419  5.546   0.50 11.43 ?  125 PRO   A HD3  1 
ATOM   2735 N  N    A LEU   A 1 126 ? 16.969 -5.247  2.430   0.50 11.11 ?  126 LEU   A N    1 
ATOM   2736 N  N    B LEU   A 1 126 ? 16.968 -5.073  2.468   0.50 12.14 ?  126 LEU   A N    1 
ATOM   2737 C  CA   A LEU   A 1 126 ? 17.000 -6.090  1.241   0.50 11.33 ?  126 LEU   A CA   1 
ATOM   2738 C  CA   B LEU   A 1 126 ? 16.890 -5.852  1.236   0.50 12.49 ?  126 LEU   A CA   1 
ATOM   2739 C  C    A LEU   A 1 126 ? 17.922 -5.472  0.193   0.50 11.86 ?  126 LEU   A C    1 
ATOM   2740 C  C    B LEU   A 1 126 ? 17.845 -5.266  0.202   0.50 12.12 ?  126 LEU   A C    1 
ATOM   2741 O  O    A LEU   A 1 126 ? 17.713 -4.332  -0.236  0.50 12.81 ?  126 LEU   A O    1 
ATOM   2742 O  O    B LEU   A 1 126 ? 17.593 -4.187  -0.347  0.50 12.64 ?  126 LEU   A O    1 
ATOM   2743 C  CB   A LEU   A 1 126 ? 15.591 -6.267  0.685   0.50 11.65 ?  126 LEU   A CB   1 
ATOM   2744 C  CB   B LEU   A 1 126 ? 15.466 -5.849  0.693   0.50 14.12 ?  126 LEU   A CB   1 
ATOM   2745 C  CG   A LEU   A 1 126 ? 14.712 -7.212  1.504   0.50 12.85 ?  126 LEU   A CG   1 
ATOM   2746 C  CG   B LEU   A 1 126 ? 14.513 -6.881  1.278   0.50 15.77 ?  126 LEU   A CG   1 
ATOM   2747 C  CD1  A LEU   A 1 126 ? 13.271 -7.099  1.055   0.50 13.58 ?  126 LEU   A CD1  1 
ATOM   2748 C  CD1  B LEU   A 1 126 ? 13.157 -6.711  0.631   0.50 16.30 ?  126 LEU   A CD1  1 
ATOM   2749 C  CD2  A LEU   A 1 126 ? 15.199 -8.649  1.371   0.50 12.84 ?  126 LEU   A CD2  1 
ATOM   2750 C  CD2  B LEU   A 1 126 ? 15.027 -8.300  1.069   0.50 16.40 ?  126 LEU   A CD2  1 
ATOM   2751 H  H    A LEU   A 1 126 ? 16.253 -4.776  2.501   0.50 13.36 ?  126 LEU   A H    1 
ATOM   2752 H  H    B LEU   A 1 126 ? 16.297 -4.549  2.610   0.50 14.60 ?  126 LEU   A H    1 
ATOM   2753 H  HA   A LEU   A 1 126 ? 17.352 -6.962  1.467   0.50 13.63 ?  126 LEU   A HA   1 
ATOM   2754 H  HA   B LEU   A 1 126 ? 17.153 -6.767  1.424   0.50 15.03 ?  126 LEU   A HA   1 
ATOM   2755 H  HB2  A LEU   A 1 126 ? 15.151 -5.404  0.663   0.50 14.01 ?  126 LEU   A HB2  1 
ATOM   2756 H  HB2  B LEU   A 1 126 ? 15.078 -4.973  0.858   0.50 16.97 ?  126 LEU   A HB2  1 
ATOM   2757 H  HB3  A LEU   A 1 126 ? 15.646 -6.628  -0.215  0.50 14.01 ?  126 LEU   A HB3  1 
ATOM   2758 H  HB3  B LEU   A 1 126 ? 15.508 -6.004  -0.263  0.50 16.97 ?  126 LEU   A HB3  1 
ATOM   2759 H  HG   A LEU   A 1 126 ? 14.755 -6.962  2.440   0.50 15.45 ?  126 LEU   A HG   1 
ATOM   2760 H  HG   B LEU   A 1 126 ? 14.418 -6.728  2.232   0.50 18.96 ?  126 LEU   A HG   1 
ATOM   2761 H  HD11 A LEU   A 1 126 ? 12.725 -7.704  1.583   0.50 16.33 ?  126 LEU   A HD11 1 
ATOM   2762 H  HD11 B LEU   A 1 126 ? 12.546 -7.365  1.003   0.50 19.60 ?  126 LEU   A HD11 1 
ATOM   2763 H  HD12 A LEU   A 1 126 ? 12.969 -6.186  1.185   0.50 16.33 ?  126 LEU   A HD12 1 
ATOM   2764 H  HD12 B LEU   A 1 126 ? 12.833 -5.815  0.807   0.50 19.60 ?  126 LEU   A HD12 1 
ATOM   2765 H  HD13 A LEU   A 1 126 ? 13.212 -7.336  0.116   0.50 16.33 ?  126 LEU   A HD13 1 
ATOM   2766 H  HD13 B LEU   A 1 126 ? 13.247 -6.850  -0.326  0.50 19.60 ?  126 LEU   A HD13 1 
ATOM   2767 H  HD21 A LEU   A 1 126 ? 14.542 -9.243  1.759   0.50 15.44 ?  126 LEU   A HD21 1 
ATOM   2768 H  HD21 B LEU   A 1 126 ? 14.307 -8.925  1.230   0.50 19.71 ?  126 LEU   A HD21 1 
ATOM   2769 H  HD22 A LEU   A 1 126 ? 15.316 -8.853  0.428   0.50 15.44 ?  126 LEU   A HD22 1 
ATOM   2770 H  HD22 B LEU   A 1 126 ? 15.345 -8.387  0.155   0.50 19.71 ?  126 LEU   A HD22 1 
ATOM   2771 H  HD23 A LEU   A 1 126 ? 16.046 -8.738  1.835   0.50 15.44 ?  126 LEU   A HD23 1 
ATOM   2772 H  HD23 B LEU   A 1 126 ? 15.757 -8.467  1.687   0.50 19.71 ?  126 LEU   A HD23 1 
ATOM   2773 N  N    A LEU   A 1 127 ? 18.929 -6.235  -0.227  0.50 11.85 ?  127 LEU   A N    1 
ATOM   2774 N  N    B LEU   A 1 127 ? 18.928 -5.980  -0.090  0.50 11.70 ?  127 LEU   A N    1 
ATOM   2775 C  CA   A LEU   A 1 127 ? 19.918 -5.735  -1.171  0.50 11.49 ?  127 LEU   A CA   1 
ATOM   2776 C  CA   B LEU   A 1 127 ? 19.903 -5.483  -1.050  0.50 11.67 ?  127 LEU   A CA   1 
ATOM   2777 C  C    A LEU   A 1 127 ? 19.299 -5.506  -2.541  0.50 10.85 ?  127 LEU   A C    1 
ATOM   2778 C  C    B LEU   A 1 127 ? 19.295 -5.391  -2.445  0.50 11.39 ?  127 LEU   A C    1 
ATOM   2779 O  O    A LEU   A 1 127 ? 18.488 -6.300  -3.024  0.50 11.12 ?  127 LEU   A O    1 
ATOM   2780 O  O    B LEU   A 1 127 ? 18.435 -6.186  -2.832  0.50 12.10 ?  127 LEU   A O    1 
ATOM   2781 C  CB   A LEU   A 1 127 ? 21.075 -6.726  -1.296  0.50 11.41 ?  127 LEU   A CB   1 
ATOM   2782 C  CB   B LEU   A 1 127 ? 21.128 -6.396  -1.085  0.50 12.06 ?  127 LEU   A CB   1 
ATOM   2783 C  CG   A LEU   A 1 127 ? 21.884 -6.991  -0.025  0.50 11.04 ?  127 LEU   A CG   1 
ATOM   2784 C  CG   B LEU   A 1 127 ? 21.947 -6.441  0.207   0.50 12.49 ?  127 LEU   A CG   1 
ATOM   2785 C  CD1  A LEU   A 1 127 ? 23.004 -7.968  -0.322  0.50 11.00 ?  127 LEU   A CD1  1 
ATOM   2786 C  CD1  B LEU   A 1 127 ? 23.097 -7.411  0.072   0.50 13.20 ?  127 LEU   A CD1  1 
ATOM   2787 C  CD2  A LEU   A 1 127 ? 22.440 -5.700  0.551   0.50 11.55 ?  127 LEU   A CD2  1 
ATOM   2788 C  CD2  B LEU   A 1 127 ? 22.459 -5.053  0.569   0.50 13.45 ?  127 LEU   A CD2  1 
ATOM   2789 H  H    A LEU   A 1 127 ? 19.071 -7.046  0.033   0.50 14.25 ?  127 LEU   A H    1 
ATOM   2790 H  H    B LEU   A 1 127 ? 19.126 -6.749  0.261   0.50 14.07 ?  127 LEU   A H    1 
ATOM   2791 H  HA   A LEU   A 1 127 ? 20.273 -4.895  -0.853  0.50 13.82 ?  127 LEU   A HA   1 
ATOM   2792 H  HA   B LEU   A 1 127 ? 20.192 -4.597  -0.778  0.50 14.04 ?  127 LEU   A HA   1 
ATOM   2793 H  HB2  A LEU   A 1 127 ? 20.719 -7.581  -1.588  0.50 13.73 ?  127 LEU   A HB2  1 
ATOM   2794 H  HB2  B LEU   A 1 127 ? 20.833 -7.302  -1.275  0.50 14.50 ?  127 LEU   A HB2  1 
ATOM   2795 H  HB3  A LEU   A 1 127 ? 21.697 -6.394  -1.963  0.50 13.73 ?  127 LEU   A HB3  1 
ATOM   2796 H  HB3  B LEU   A 1 127 ? 21.717 -6.093  -1.793  0.50 14.50 ?  127 LEU   A HB3  1 
ATOM   2797 H  HG   A LEU   A 1 127 ? 21.303 -7.397  0.641   0.50 13.28 ?  127 LEU   A HG   1 
ATOM   2798 H  HG   B LEU   A 1 127 ? 21.378 -6.749  0.931   0.50 15.02 ?  127 LEU   A HG   1 
ATOM   2799 H  HD11 A LEU   A 1 127 ? 23.483 -8.164  0.500   0.50 13.24 ?  127 LEU   A HD11 1 
ATOM   2800 H  HD11 B LEU   A 1 127 ? 23.628 -7.382  0.883   0.50 15.88 ?  127 LEU   A HD11 1 
ATOM   2801 H  HD12 A LEU   A 1 127 ? 22.624 -8.789  -0.682  0.50 13.24 ?  127 LEU   A HD12 1 
ATOM   2802 H  HD12 B LEU   A 1 127 ? 22.742 -8.303  -0.061  0.50 15.88 ?  127 LEU   A HD12 1 
ATOM   2803 H  HD13 A LEU   A 1 127 ? 23.605 -7.574  -0.970  0.50 13.24 ?  127 LEU   A HD13 1 
ATOM   2804 H  HD13 B LEU   A 1 127 ? 23.639 -7.151  -0.688  0.50 15.88 ?  127 LEU   A HD13 1 
ATOM   2805 H  HD21 A LEU   A 1 127 ? 23.064 -5.916  1.260   0.50 13.89 ?  127 LEU   A HD21 1 
ATOM   2806 H  HD21 B LEU   A 1 127 ? 23.122 -5.135  1.271   0.50 16.18 ?  127 LEU   A HD21 1 
ATOM   2807 H  HD22 A LEU   A 1 127 ? 22.895 -5.216  -0.157  0.50 13.89 ?  127 LEU   A HD22 1 
ATOM   2808 H  HD22 B LEU   A 1 127 ? 22.857 -4.650  -0.218  0.50 16.18 ?  127 LEU   A HD22 1 
ATOM   2809 H  HD23 A LEU   A 1 127 ? 21.708 -5.171  0.898   0.50 13.89 ?  127 LEU   A HD23 1 
ATOM   2810 H  HD23 B LEU   A 1 127 ? 21.715 -4.511  0.878   0.50 16.18 ?  127 LEU   A HD23 1 
ATOM   2811 N  N    A SER   A 1 128 ? 19.709 -4.413  -3.172  0.50 11.10 ?  128 SER   A N    1 
ATOM   2812 N  N    B SER   A 1 128 ? 19.760 -4.397  -3.198  0.50 11.35 ?  128 SER   A N    1 
ATOM   2813 C  CA   A SER   A 1 128 ? 19.280 -4.009  -4.503  0.50 11.70 ?  128 SER   A CA   1 
ATOM   2814 C  CA   B SER   A 1 128 ? 19.390 -4.100  -4.579  0.50 11.08 ?  128 SER   A CA   1 
ATOM   2815 C  C    A SER   A 1 128 ? 17.812 -3.601  -4.561  0.50 12.16 ?  128 SER   A C    1 
ATOM   2816 C  C    B SER   A 1 128 ? 17.952 -3.616  -4.750  0.50 11.03 ?  128 SER   A C    1 
ATOM   2817 O  O    A SER   A 1 128 ? 17.287 -3.375  -5.656  0.50 13.37 ?  128 SER   A O    1 
ATOM   2818 O  O    B SER   A 1 128 ? 17.583 -3.227  -5.862  0.50 11.42 ?  128 SER   A O    1 
ATOM   2819 C  CB   A SER   A 1 128 ? 19.625 -5.040  -5.587  0.50 11.87 ?  128 SER   A CB   1 
ATOM   2820 C  CB   B SER   A 1 128 ? 19.717 -5.232  -5.566  0.50 11.19 ?  128 SER   A CB   1 
ATOM   2821 O  OG   A SER   A 1 128 ? 21.030 -5.244  -5.662  0.50 12.34 ?  128 SER   A OG   1 
ATOM   2822 O  OG   B SER   A 1 128 ? 21.123 -5.417  -5.670  0.50 11.63 ?  128 SER   A OG   1 
ATOM   2823 H  H    A SER   A 1 128 ? 20.278 -3.864  -2.827  0.50 13.36 ?  128 SER   A H    1 
ATOM   2824 H  H    B SER   A 1 128 ? 20.353 -3.847  -2.904  0.50 13.66 ?  128 SER   A H    1 
ATOM   2825 H  HA   A SER   A 1 128 ? 19.793 -3.225  -4.721  0.50 14.07 ?  128 SER   A HA   1 
ATOM   2826 H  HA   B SER   A 1 128 ? 19.934 -3.354  -4.850  0.50 13.33 ?  128 SER   A HA   1 
ATOM   2827 H  HB2  A SER   A 1 128 ? 19.189 -5.881  -5.382  0.50 14.28 ?  128 SER   A HB2  1 
ATOM   2828 H  HB2  B SER   A 1 128 ? 19.307 -6.054  -5.258  0.50 13.46 ?  128 SER   A HB2  1 
ATOM   2829 H  HB3  A SER   A 1 128 ? 19.313 -4.707  -6.446  0.50 14.28 ?  128 SER   A HB3  1 
ATOM   2830 H  HB3  B SER   A 1 128 ? 19.360 -4.994  -6.442  0.50 13.46 ?  128 SER   A HB3  1 
ATOM   2831 H  HG   A SER   A 1 128 ? 21.419 -4.519  -5.829  0.50 14.84 ?  128 SER   A HG   1 
ATOM   2832 H  HG   B SER   A 1 128 ? 21.482 -4.705  -5.939  0.50 13.98 ?  128 SER   A HG   1 
ATOM   2833 N  N    A ALA   A 1 129 ? 17.142 -3.485  -3.415  0.50 12.62 ?  129 ALA   A N    1 
ATOM   2834 N  N    B ALA   A 1 129 ? 17.149 -3.590  -3.689  0.50 11.42 ?  129 ALA   A N    1 
ATOM   2835 C  CA   A ALA   A 1 129 ? 15.784 -2.966  -3.367  0.50 12.58 ?  129 ALA   A CA   1 
ATOM   2836 C  CA   B ALA   A 1 129 ? 15.785 -3.084  -3.761  0.50 12.22 ?  129 ALA   A CA   1 
ATOM   2837 C  C    A ALA   A 1 129 ? 15.822 -1.437  -3.345  0.50 12.53 ?  129 ALA   A C    1 
ATOM   2838 C  C    B ALA   A 1 129 ? 15.790 -1.555  -3.685  0.50 11.75 ?  129 ALA   A C    1 
ATOM   2839 O  O    A ALA   A 1 129 ? 16.886 -0.813  -3.416  0.50 12.63 ?  129 ALA   A O    1 
ATOM   2840 O  O    B ALA   A 1 129 ? 16.838 -0.902  -3.714  0.50 12.03 ?  129 ALA   A O    1 
ATOM   2841 C  CB   A ALA   A 1 129 ? 15.037 -3.543  -2.164  0.50 12.80 ?  129 ALA   A CB   1 
ATOM   2842 C  CB   B ALA   A 1 129 ? 14.924 -3.733  -2.677  0.50 12.93 ?  129 ALA   A CB   1 
ATOM   2843 H  H    A ALA   A 1 129 ? 17.456 -3.699  -2.640  0.50 15.18 ?  129 ALA   A H    1 
ATOM   2844 H  H    B ALA   A 1 129 ? 17.371 -3.870  -2.900  0.50 13.74 ?  129 ALA   A H    1 
ATOM   2845 H  HA   A ALA   A 1 129 ? 15.315 -3.253  -4.164  0.50 15.13 ?  129 ALA   A HA   1 
ATOM   2846 H  HA   B ALA   A 1 129 ? 15.412 -3.322  -4.619  0.50 14.69 ?  129 ALA   A HA   1 
ATOM   2847 H  HB1  A ALA   A 1 129 ? 14.130 -3.193  -2.157  0.50 15.40 ?  129 ALA   A HB1  1 
ATOM   2848 H  HB1  B ALA   A 1 129 ? 14.019 -3.389  -2.747  0.50 15.55 ?  129 ALA   A HB1  1 
ATOM   2849 H  HB2  A ALA   A 1 129 ? 15.014 -4.510  -2.244  0.50 15.40 ?  129 ALA   A HB2  1 
ATOM   2850 H  HB2  B ALA   A 1 129 ? 14.926 -4.693  -2.803  0.50 15.55 ?  129 ALA   A HB2  1 
ATOM   2851 H  HB3  A ALA   A 1 129 ? 15.496 -3.287  -1.352  0.50 15.40 ?  129 ALA   A HB3  1 
ATOM   2852 H  HB3  B ALA   A 1 129 ? 15.292 -3.512  -1.805  0.50 15.55 ?  129 ALA   A HB3  1 
ATOM   2853 N  N    A GLY   A 1 130 ? 14.652 -0.818  -3.239  0.50 13.37 ?  130 GLY   A N    1 
ATOM   2854 N  N    B GLY   A 1 130 ? 14.599 -0.973  -3.606  0.50 11.97 ?  130 GLY   A N    1 
ATOM   2855 C  CA   A GLY   A 1 130 ? 14.619 0.635   -3.214  0.50 14.07 ?  130 GLY   A CA   1 
ATOM   2856 C  CA   B GLY   A 1 130 ? 14.482 0.468   -3.500  0.50 12.84 ?  130 GLY   A CA   1 
ATOM   2857 C  C    A GLY   A 1 130 ? 15.176 1.224   -4.495  0.50 14.01 ?  130 GLY   A C    1 
ATOM   2858 C  C    B GLY   A 1 130 ? 15.145 1.149   -4.678  0.50 13.21 ?  130 GLY   A C    1 
ATOM   2859 O  O    A GLY   A 1 130 ? 14.852 0.780   -5.602  0.50 14.02 ?  130 GLY   A O    1 
ATOM   2860 O  O    B GLY   A 1 130 ? 14.999 0.735   -5.833  0.50 13.22 ?  130 GLY   A O    1 
ATOM   2861 H  H    A GLY   A 1 130 ? 13.882 -1.202  -3.174  0.50 16.08 ?  130 GLY   A H    1 
ATOM   2862 H  H    B GLY   A 1 130 ? 13.854 -1.397  -3.616  0.50 14.39 ?  130 GLY   A H    1 
ATOM   2863 H  HA2  A GLY   A 1 130 ? 13.705 0.943   -3.102  0.50 16.92 ?  130 GLY   A HA2  1 
ATOM   2864 H  HA2  B GLY   A 1 130 ? 13.540 0.714   -3.475  0.50 15.44 ?  130 GLY   A HA2  1 
ATOM   2865 H  HA3  A GLY   A 1 130 ? 15.150 0.959   -2.473  0.50 16.92 ?  130 GLY   A HA3  1 
ATOM   2866 H  HA3  B GLY   A 1 130 ? 14.901 0.777   -2.681  0.50 15.44 ?  130 GLY   A HA3  1 
ATOM   2867 N  N    A ILE   A 1 131 ? 16.035 2.239   -4.349  0.50 13.97 ?  131 ILE   A N    1 
ATOM   2868 N  N    B ILE   A 1 131 ? 15.904 2.208   -4.383  0.50 13.70 ?  131 ILE   A N    1 
ATOM   2869 C  CA   A ILE   A 1 131 ? 16.555 2.976   -5.499  0.50 13.53 ?  131 ILE   A CA   1 
ATOM   2870 C  CA   B ILE   A 1 131 ? 16.538 3.010   -5.423  0.50 13.96 ?  131 ILE   A CA   1 
ATOM   2871 C  C    A ILE   A 1 131 ? 17.583 2.200   -6.307  0.50 12.84 ?  131 ILE   A C    1 
ATOM   2872 C  C    B ILE   A 1 131 ? 17.511 2.222   -6.293  0.50 13.58 ?  131 ILE   A C    1 
ATOM   2873 O  O    A ILE   A 1 131 ? 18.012 2.692   -7.358  0.50 13.85 ?  131 ILE   A O    1 
ATOM   2874 O  O    B ILE   A 1 131 ? 17.914 2.722   -7.348  0.50 14.33 ?  131 ILE   A O    1 
ATOM   2875 C  CB   A ILE   A 1 131 ? 17.108 4.367   -5.111  0.50 14.30 ?  131 ILE   A CB   1 
ATOM   2876 C  CB   B ILE   A 1 131 ? 17.211 4.275   -4.835  0.50 15.14 ?  131 ILE   A CB   1 
ATOM   2877 C  CG1  A ILE   A 1 131 ? 18.364 4.242   -4.236  0.50 14.95 ?  131 ILE   A CG1  1 
ATOM   2878 C  CG1  B ILE   A 1 131 ? 18.409 3.910   -3.951  0.50 15.70 ?  131 ILE   A CG1  1 
ATOM   2879 C  CG2  A ILE   A 1 131 ? 16.026 5.195   -4.422  0.50 14.56 ?  131 ILE   A CG2  1 
ATOM   2880 C  CG2  B ILE   A 1 131 ? 16.197 5.111   -4.059  0.50 15.86 ?  131 ILE   A CG2  1 
ATOM   2881 C  CD1  A ILE   A 1 131 ? 19.006 5.581   -3.877  0.50 15.51 ?  131 ILE   A CD1  1 
ATOM   2882 C  CD1  B ILE   A 1 131 ? 19.127 5.124   -3.361  0.50 16.49 ?  131 ILE   A CD1  1 
ATOM   2883 H  H    A ILE   A 1 131 ? 16.326 2.522   -3.597  0.50 16.80 ?  131 ILE   A H    1 
ATOM   2884 H  H    B ILE   A 1 131 ? 16.048 2.488   -3.584  0.50 16.48 ?  131 ILE   A H    1 
ATOM   2885 H  HA   A ILE   A 1 131 ? 15.820 3.135   -6.104  0.50 16.27 ?  131 ILE   A HA   1 
ATOM   2886 H  HA   B ILE   A 1 131 ? 15.837 3.322   -6.014  0.50 16.78 ?  131 ILE   A HA   1 
ATOM   2887 H  HB   A ILE   A 1 131 ? 17.359 4.827   -5.928  0.50 17.19 ?  131 ILE   A HB   1 
ATOM   2888 H  HB   B ILE   A 1 131 ? 17.532 4.811   -5.576  0.50 18.21 ?  131 ILE   A HB   1 
ATOM   2889 H  HG12 A ILE   A 1 131 ? 18.126 3.795   -3.410  0.50 17.98 ?  131 ILE   A HG12 1 
ATOM   2890 H  HG12 B ILE   A 1 131 ? 18.100 3.361   -3.216  0.50 18.88 ?  131 ILE   A HG12 1 
ATOM   2891 H  HG13 A ILE   A 1 131 ? 19.030 3.719   -4.712  0.50 17.98 ?  131 ILE   A HG13 1 
ATOM   2892 H  HG13 B ILE   A 1 131 ? 19.054 3.420   -4.484  0.50 18.88 ?  131 ILE   A HG13 1 
ATOM   2893 H  HG21 A ILE   A 1 131 ? 16.346 6.101   -4.306  0.50 17.50 ?  131 ILE   A HG21 1 
ATOM   2894 H  HG21 B ILE   A 1 131 ? 16.582 5.980   -3.870  0.50 19.06 ?  131 ILE   A HG21 1 
ATOM   2895 H  HG22 A ILE   A 1 131 ? 15.230 5.192   -4.975  0.50 17.50 ?  131 ILE   A HG22 1 
ATOM   2896 H  HG22 B ILE   A 1 131 ? 15.397 5.214   -4.598  0.50 19.06 ?  131 ILE   A HG22 1 
ATOM   2897 H  HG23 A ILE   A 1 131 ? 15.829 4.797   -3.559  0.50 17.50 ?  131 ILE   A HG23 1 
ATOM   2898 H  HG23 B ILE   A 1 131 ? 15.980 4.654   -3.232  0.50 19.06 ?  131 ILE   A HG23 1 
ATOM   2899 H  HD11 A ILE   A 1 131 ? 19.850 5.414   -3.427  0.50 18.64 ?  131 ILE   A HD11 1 
ATOM   2900 H  HD11 B ILE   A 1 131 ? 19.946 4.830   -2.934  0.50 19.83 ?  131 ILE   A HD11 1 
ATOM   2901 H  HD12 A ILE   A 1 131 ? 19.161 6.085   -4.691  0.50 18.64 ?  131 ILE   A HD12 1 
ATOM   2902 H  HD12 B ILE   A 1 131 ? 19.333 5.749   -4.075  0.50 19.83 ?  131 ILE   A HD12 1 
ATOM   2903 H  HD13 A ILE   A 1 131 ? 18.409 6.070   -3.291  0.50 18.64 ?  131 ILE   A HD13 1 
ATOM   2904 H  HD13 B ILE   A 1 131 ? 18.549 5.550   -2.708  0.50 19.83 ?  131 ILE   A HD13 1 
ATOM   2905 N  N    A PHE   A 1 132 ? 17.992 1.007   -5.856  0.50 12.42 ?  132 PHE   A N    1 
ATOM   2906 N  N    B PHE   A 1 132 ? 17.894 1.003   -5.889  0.50 13.44 ?  132 PHE   A N    1 
ATOM   2907 C  CA   A PHE   A 1 132 ? 18.802 0.136   -6.700  0.50 12.42 ?  132 PHE   A CA   1 
ATOM   2908 C  CA   B PHE   A 1 132 ? 18.821 0.203   -6.685  0.50 13.79 ?  132 PHE   A CA   1 
ATOM   2909 C  C    A PHE   A 1 132 ? 17.964 -0.609  -7.740  0.50 12.56 ?  132 PHE   A C    1 
ATOM   2910 C  C    B PHE   A 1 132 ? 18.154 -0.523  -7.854  0.50 14.67 ?  132 PHE   A C    1 
ATOM   2911 O  O    A PHE   A 1 132 ? 18.533 -1.252  -8.627  0.50 12.71 ?  132 PHE   A O    1 
ATOM   2912 O  O    B PHE   A 1 132 ? 18.867 -1.082  -8.695  0.50 16.03 ?  132 PHE   A O    1 
ATOM   2913 C  CB   A PHE   A 1 132 ? 19.623 -0.845  -5.850  0.50 12.38 ?  132 PHE   A CB   1 
ATOM   2914 C  CB   B PHE   A 1 132 ? 19.575 -0.798  -5.802  0.50 13.26 ?  132 PHE   A CB   1 
ATOM   2915 C  CG   A PHE   A 1 132 ? 20.862 -0.238  -5.212  0.50 12.73 ?  132 PHE   A CG   1 
ATOM   2916 C  CG   B PHE   A 1 132 ? 20.765 -0.211  -5.078  0.50 12.97 ?  132 PHE   A CG   1 
ATOM   2917 C  CD1  A PHE   A 1 132 ? 20.774 0.848   -4.352  0.50 13.08 ?  132 PHE   A CD1  1 
ATOM   2918 C  CD1  B PHE   A 1 132 ? 20.596 0.679   -4.028  0.50 13.18 ?  132 PHE   A CD1  1 
ATOM   2919 C  CD2  A PHE   A 1 132 ? 22.114 -0.793  -5.447  0.50 13.29 ?  132 PHE   A CD2  1 
ATOM   2920 C  CD2  B PHE   A 1 132 ? 22.054 -0.580  -5.431  0.50 12.91 ?  132 PHE   A CD2  1 
ATOM   2921 C  CE1  A PHE   A 1 132 ? 21.915 1.382   -3.760  0.50 12.97 ?  132 PHE   A CE1  1 
ATOM   2922 C  CE1  B PHE   A 1 132 ? 21.692 1.202   -3.362  0.50 12.82 ?  132 PHE   A CE1  1 
ATOM   2923 C  CE2  A PHE   A 1 132 ? 23.253 -0.268  -4.856  0.50 13.58 ?  132 PHE   A CE2  1 
ATOM   2924 C  CE2  B PHE   A 1 132 ? 23.152 -0.063  -4.763  0.50 13.40 ?  132 PHE   A CE2  1 
ATOM   2925 C  CZ   A PHE   A 1 132 ? 23.152 0.823   -4.013  0.50 13.30 ?  132 PHE   A CZ   1 
ATOM   2926 C  CZ   B PHE   A 1 132 ? 22.968 0.832   -3.729  0.50 12.93 ?  132 PHE   A CZ   1 
ATOM   2927 H  H    A PHE   A 1 132 ? 17.816 0.685   -5.073  0.50 14.93 ?  132 PHE   A H    1 
ATOM   2928 H  H    B PHE   A 1 132 ? 17.634 0.625   -5.155  0.50 16.16 ?  132 PHE   A H    1 
ATOM   2929 H  HA   A PHE   A 1 132 ? 19.434 0.685   -7.179  0.50 14.94 ?  132 PHE   A HA   1 
ATOM   2930 H  HA   B PHE   A 1 132 ? 19.479 0.805   -7.057  0.50 16.58 ?  132 PHE   A HA   1 
ATOM   2931 H  HB2  A PHE   A 1 132 ? 19.064 -1.180  -5.131  0.50 14.89 ?  132 PHE   A HB2  1 
ATOM   2932 H  HB2  B PHE   A 1 132 ? 18.968 -1.145  -5.131  0.50 15.94 ?  132 PHE   A HB2  1 
ATOM   2933 H  HB3  A PHE   A 1 132 ? 19.913 -1.585  -6.410  0.50 14.89 ?  132 PHE   A HB3  1 
ATOM   2934 H  HB3  B PHE   A 1 132 ? 19.898 -1.523  -6.360  0.50 15.94 ?  132 PHE   A HB3  1 
ATOM   2935 H  HD1  A PHE   A 1 132 ? 19.947 1.227   -4.174  0.50 15.73 ?  132 PHE   A HD1  1 
ATOM   2936 H  HD1  B PHE   A 1 132 ? 19.738 0.934   -3.775  0.50 15.85 ?  132 PHE   A HD1  1 
ATOM   2937 H  HD2  A PHE   A 1 132 ? 22.195 -1.528  -6.013  0.50 15.98 ?  132 PHE   A HD2  1 
ATOM   2938 H  HD2  B PHE   A 1 132 ? 22.186 -1.184  -6.130  0.50 15.52 ?  132 PHE   A HD2  1 
ATOM   2939 H  HE1  A PHE   A 1 132 ? 21.846 2.117   -3.189  0.50 15.60 ?  132 PHE   A HE1  1 
ATOM   2940 H  HE1  B PHE   A 1 132 ? 21.566 1.804   -2.665  0.50 15.41 ?  132 PHE   A HE1  1 
ATOM   2941 H  HE2  A PHE   A 1 132 ? 24.087 -0.643  -5.033  0.50 16.33 ?  132 PHE   A HE2  1 
ATOM   2942 H  HE2  B PHE   A 1 132 ? 24.011 -0.313  -5.019  0.50 16.11 ?  132 PHE   A HE2  1 
ATOM   2943 H  HZ   A PHE   A 1 132 ? 23.917 1.183   -3.619  0.50 16.00 ?  132 PHE   A HZ   1 
ATOM   2944 H  HZ   B PHE   A 1 132 ? 23.701 1.184   -3.283  0.50 15.55 ?  132 PHE   A HZ   1 
ATOM   2945 N  N    A GLY   A 1 133 ? 16.635 -0.556  -7.641  0.50 12.51 ?  133 GLY   A N    1 
ATOM   2946 N  N    B GLY   A 1 133 ? 16.820 -0.555  -7.925  0.50 14.20 ?  133 GLY   A N    1 
ATOM   2947 C  CA   A GLY   A 1 133 ? 15.768 -0.912  -8.751  0.50 13.05 ?  133 GLY   A CA   1 
ATOM   2948 C  CA   B GLY   A 1 133 ? 16.118 -0.953  -9.129  0.50 14.26 ?  133 GLY   A CA   1 
ATOM   2949 C  C    A GLY   A 1 133 ? 15.563 -2.383  -9.032  0.50 13.76 ?  133 GLY   A C    1 
ATOM   2950 C  C    B GLY   A 1 133 ? 15.558 -2.364  -9.143  0.50 14.31 ?  133 GLY   A C    1 
ATOM   2951 O  O    A GLY   A 1 133 ? 15.115 -2.723  -10.133 0.50 14.85 ?  133 GLY   A O    1 
ATOM   2952 O  O    B GLY   A 1 133 ? 14.622 -2.628  -9.909  0.50 14.80 ?  133 GLY   A O    1 
ATOM   2953 H  H    A GLY   A 1 133 ? 16.209 -0.321  -6.935  0.50 15.04 ?  133 GLY   A H    1 
ATOM   2954 H  H    B GLY   A 1 133 ? 16.297 -0.342  -7.273  0.50 17.08 ?  133 GLY   A H    1 
ATOM   2955 H  HA2  A GLY   A 1 133 ? 14.892 -0.525  -8.595  0.50 15.69 ?  133 GLY   A HA2  1 
ATOM   2956 H  HA2  B GLY   A 1 133 ? 15.377 -0.349  -9.272  0.50 17.15 ?  133 GLY   A HA2  1 
ATOM   2957 H  HA3  A GLY   A 1 133 ? 16.123 -0.520  -9.561  0.50 15.69 ?  133 GLY   A HA3  1 
ATOM   2958 H  HA3  B GLY   A 1 133 ? 16.723 -0.865  -9.882  0.50 17.15 ?  133 GLY   A HA3  1 
ATOM   2959 N  N    A ALA   A 1 134 ? 15.874 -3.272  -8.093  0.50 13.33 ?  134 ALA   A N    1 
ATOM   2960 N  N    B ALA   A 1 134 ? 16.101 -3.279  -8.343  0.50 14.03 ?  134 ALA   A N    1 
ATOM   2961 C  CA   A ALA   A 1 134 ? 15.589 -4.686  -8.289  0.50 14.33 ?  134 ALA   A CA   1 
ATOM   2962 C  CA   B ALA   A 1 134 ? 15.685 -4.669  -8.456  0.50 14.62 ?  134 ALA   A CA   1 
ATOM   2963 C  C    A ALA   A 1 134 ? 14.251 -5.054  -7.657  0.50 15.12 ?  134 ALA   A C    1 
ATOM   2964 C  C    B ALA   A 1 134 ? 14.351 -4.903  -7.747  0.50 15.07 ?  134 ALA   A C    1 
ATOM   2965 O  O    A ALA   A 1 134 ? 13.695 -4.317  -6.838  0.50 15.67 ?  134 ALA   A O    1 
ATOM   2966 O  O    B ALA   A 1 134 ? 13.873 -4.084  -6.956  0.50 15.76 ?  134 ALA   A O    1 
ATOM   2967 C  CB   A ALA   A 1 134 ? 16.700 -5.568  -7.713  0.50 15.05 ?  134 ALA   A CB   1 
ATOM   2968 C  CB   B ALA   A 1 134 ? 16.761 -5.607  -7.908  0.50 15.28 ?  134 ALA   A CB   1 
ATOM   2969 H  H    A ALA   A 1 134 ? 16.258 -3.084  -7.337  0.50 16.03 ?  134 ALA   A H    1 
ATOM   2970 H  H    B ALA   A 1 134 ? 16.702 -3.125  -7.742  0.50 16.87 ?  134 ALA   A H    1 
ATOM   2971 H  HA   A ALA   A 1 134 ? 15.533 -4.864  -9.240  0.50 17.22 ?  134 ALA   A HA   1 
ATOM   2972 H  HA   B ALA   A 1 134 ? 15.561 -4.879  -9.393  0.50 17.58 ?  134 ALA   A HA   1 
ATOM   2973 H  HB1  A ALA   A 1 134 ? 16.486 -6.496  -7.895  0.50 18.09 ?  134 ALA   A HB1  1 
ATOM   2974 H  HB1  B ALA   A 1 134 ? 16.460 -6.524  -8.007  0.50 18.37 ?  134 ALA   A HB1  1 
ATOM   2975 H  HB2  A ALA   A 1 134 ? 17.539 -5.333  -8.140  0.50 18.09 ?  134 ALA   A HB2  1 
ATOM   2976 H  HB2  B ALA   A 1 134 ? 17.581 -5.473  -8.411  0.50 18.37 ?  134 ALA   A HB2  1 
ATOM   2977 H  HB3  A ALA   A 1 134 ? 16.758 -5.419  -6.759  0.50 18.09 ?  134 ALA   A HB3  1 
ATOM   2978 H  HB3  B ALA   A 1 134 ? 16.911 -5.406  -6.972  0.50 18.37 ?  134 ALA   A HB3  1 
ATOM   2979 N  N    A ASP   A 1 135 ? 13.741 -6.214  -8.053  0.50 16.12 ?  135 ASP   A N    1 
ATOM   2980 N  N    B ASP   A 1 135 ? 13.753 -6.054  -8.044  0.50 16.19 ?  135 ASP   A N    1 
ATOM   2981 C  CA   A ASP   A 1 135 ? 12.499 -6.735  -7.494  0.50 17.07 ?  135 ASP   A CA   1 
ATOM   2982 C  CA   B ASP   A 1 135 ? 12.480 -6.434  -7.446  0.50 17.38 ?  135 ASP   A CA   1 
ATOM   2983 C  C    A ASP   A 1 135 ? 12.743 -7.164  -6.053  0.50 16.78 ?  135 ASP   A C    1 
ATOM   2984 C  C    B ASP   A 1 135 ? 12.708 -6.920  -6.019  0.50 16.74 ?  135 ASP   A C    1 
ATOM   2985 O  O    A ASP   A 1 135 ? 13.547 -8.074  -5.818  0.50 16.72 ?  135 ASP   A O    1 
ATOM   2986 O  O    B ASP   A 1 135 ? 13.435 -7.899  -5.819  0.50 16.33 ?  135 ASP   A O    1 
ATOM   2987 C  CB   A ASP   A 1 135 ? 12.045 -7.936  -8.318  0.50 18.82 ?  135 ASP   A CB   1 
ATOM   2988 C  CB   B ASP   A 1 135 ? 11.838 -7.540  -8.269  0.50 19.75 ?  135 ASP   A CB   1 
ATOM   2989 C  CG   A ASP   A 1 135 ? 10.682 -8.464  -7.893  0.50 20.55 ?  135 ASP   A CG   1 
ATOM   2990 C  CG   B ASP   A 1 135 ? 10.775 -8.291  -7.497  0.50 21.72 ?  135 ASP   A CG   1 
ATOM   2991 O  OD1  A ASP   A 1 135 ? 10.255 -8.201  -6.749  0.50 20.76 ?  135 ASP   A OD1  1 
ATOM   2992 O  OD1  B ASP   A 1 135 ? 9.972  -7.630  -6.804  0.50 21.77 ?  135 ASP   A OD1  1 
ATOM   2993 O  OD2  A ASP   A 1 135 ? 10.034 -9.150  -8.710  0.50 22.14 -1 135 ASP   A OD2  1 
ATOM   2994 O  OD2  B ASP   A 1 135 ? 10.749 -9.537  -7.581  0.50 23.22 -1 135 ASP   A OD2  1 
ATOM   2995 H  H    A ASP   A 1 135 ? 14.097 -6.724  -8.646  0.50 19.38 ?  135 ASP   A H    1 
ATOM   2996 H  H    B ASP   A 1 135 ? 14.063 -6.638  -8.590  0.50 19.46 ?  135 ASP   A H    1 
ATOM   2997 H  HA   A ASP   A 1 135 ? 11.811 -6.053  -7.531  0.50 20.51 ?  135 ASP   A HA   1 
ATOM   2998 H  HA   B ASP   A 1 135 ? 11.880 -5.674  -7.447  0.50 20.89 ?  135 ASP   A HA   1 
ATOM   2999 H  HB2  A ASP   A 1 135 ? 11.973 -7.674  -9.248  0.50 22.62 ?  135 ASP   A HB2  1 
ATOM   3000 H  HB2  B ASP   A 1 135 ? 11.427 -7.150  -9.059  0.50 23.73 ?  135 ASP   A HB2  1 
ATOM   3001 H  HB3  A ASP   A 1 135 ? 12.696 -8.649  -8.223  0.50 22.62 ?  135 ASP   A HB3  1 
ATOM   3002 H  HB3  B ASP   A 1 135 ? 12.520 -8.177  -8.535  0.50 23.73 ?  135 ASP   A HB3  1 
ATOM   3003 N  N    A PRO   A 1 136 ? 12.085 -6.552  -5.065  0.50 16.56 ?  136 PRO   A N    1 
ATOM   3004 N  N    B PRO   A 1 136 ? 12.114 -6.278  -5.009  0.50 16.61 ?  136 PRO   A N    1 
ATOM   3005 C  CA   A PRO   A 1 136 ? 12.328 -6.954  -3.668  0.50 16.50 ?  136 PRO   A CA   1 
ATOM   3006 C  CA   B PRO   A 1 136 ? 12.361 -6.701  -3.619  0.50 16.62 ?  136 PRO   A CA   1 
ATOM   3007 C  C    A PRO   A 1 136 ? 11.911 -8.381  -3.355  0.50 15.58 ?  136 PRO   A C    1 
ATOM   3008 C  C    B PRO   A 1 136 ? 11.911 -8.122  -3.312  0.50 15.95 ?  136 PRO   A C    1 
ATOM   3009 O  O    A PRO   A 1 136 ? 12.539 -9.024  -2.505  0.50 15.12 ?  136 PRO   A O    1 
ATOM   3010 O  O    B PRO   A 1 136 ? 12.473 -8.760  -2.412  0.50 15.25 ?  136 PRO   A O    1 
ATOM   3011 C  CB   A PRO   A 1 136 ? 11.518 -5.931  -2.859  0.50 17.41 ?  136 PRO   A CB   1 
ATOM   3012 C  CB   B PRO   A 1 136 ? 11.597 -5.653  -2.793  0.50 17.32 ?  136 PRO   A CB   1 
ATOM   3013 C  CG   A PRO   A 1 136 ? 10.485 -5.419  -3.806  0.50 18.13 ?  136 PRO   A CG   1 
ATOM   3014 C  CG   B PRO   A 1 136 ? 10.598 -5.075  -3.741  0.50 18.13 ?  136 PRO   A CG   1 
ATOM   3015 C  CD   A PRO   A 1 136 ? 11.110 -5.453  -5.166  0.50 17.16 ?  136 PRO   A CD   1 
ATOM   3016 C  CD   B PRO   A 1 136 ? 11.228 -5.105  -5.082  0.50 17.37 ?  136 PRO   A CD   1 
ATOM   3017 H  HA   A PRO   A 1 136 ? 13.272 -6.851  -3.453  0.50 19.84 ?  136 PRO   A HA   1 
ATOM   3018 H  HA   B PRO   A 1 136 ? 13.305 -6.622  -3.411  0.50 19.98 ?  136 PRO   A HA   1 
ATOM   3019 H  HB2  A PRO   A 1 136 ? 11.104 -6.375  -2.102  0.50 20.93 ?  136 PRO   A HB2  1 
ATOM   3020 H  HB2  B PRO   A 1 136 ? 11.153 -6.077  -2.042  0.50 20.82 ?  136 PRO   A HB2  1 
ATOM   3021 H  HB3  A PRO   A 1 136 ? 12.104 -5.218  -2.560  0.50 20.93 ?  136 PRO   A HB3  1 
ATOM   3022 H  HB3  B PRO   A 1 136 ? 12.209 -4.962  -2.483  0.50 20.82 ?  136 PRO   A HB3  1 
ATOM   3023 H  HG2  A PRO   A 1 136 ? 9.708  -5.992  -3.777  0.50 21.79 ?  136 PRO   A HG2  1 
ATOM   3024 H  HG2  B PRO   A 1 136 ? 9.791  -5.618  -3.732  0.50 21.78 ?  136 PRO   A HG2  1 
ATOM   3025 H  HG3  A PRO   A 1 136 ? 10.254 -4.510  -3.565  0.50 21.79 ?  136 PRO   A HG3  1 
ATOM   3026 H  HG3  B PRO   A 1 136 ? 10.402 -4.162  -3.488  0.50 21.78 ?  136 PRO   A HG3  1 
ATOM   3027 H  HD2  A PRO   A 1 136 ? 10.442 -5.662  -5.839  0.50 20.63 ?  136 PRO   A HD2  1 
ATOM   3028 H  HD2  B PRO   A 1 136 ? 10.551 -5.232  -5.768  0.50 20.88 ?  136 PRO   A HD2  1 
ATOM   3029 H  HD3  A PRO   A 1 136 ? 11.559 -4.614  -5.361  0.50 20.63 ?  136 PRO   A HD3  1 
ATOM   3030 H  HD3  B PRO   A 1 136 ? 11.744 -4.298  -5.236  0.50 20.88 ?  136 PRO   A HD3  1 
ATOM   3031 N  N    A ILE   A 1 137 ? 10.856 -8.894  -3.992  0.50 15.64 ?  137 ILE   A N    1 
ATOM   3032 N  N    B ILE   A 1 137 ? 10.907 -8.638  -4.022  0.50 16.38 ?  137 ILE   A N    1 
ATOM   3033 C  CA   A ILE   A 1 137 ? 10.510 -10.301 -3.811  0.50 15.87 ?  137 ILE   A CA   1 
ATOM   3034 C  CA   B ILE   A 1 137 ? 10.492 -10.026 -3.822  0.50 16.85 ?  137 ILE   A CA   1 
ATOM   3035 C  C    A ILE   A 1 137 ? 11.679 -11.184 -4.227  0.50 15.46 ?  137 ILE   A C    1 
ATOM   3036 C  C    B ILE   A 1 137 ? 11.636 -10.970 -4.175  0.50 16.92 ?  137 ILE   A C    1 
ATOM   3037 O  O    A ILE   A 1 137 ? 12.013 -12.166 -3.550  0.50 15.13 ?  137 ILE   A O    1 
ATOM   3038 O  O    B ILE   A 1 137 ? 11.927 -11.933 -3.455  0.50 17.17 ?  137 ILE   A O    1 
ATOM   3039 C  CB   A ILE   A 1 137 ? 9.216  -10.643 -4.576  0.50 16.90 ?  137 ILE   A CB   1 
ATOM   3040 C  CB   B ILE   A 1 137 ? 9.235  -10.332 -4.656  0.50 18.00 ?  137 ILE   A CB   1 
ATOM   3041 C  CG1  A ILE   A 1 137 ? 8.033  -9.847  -4.012  0.50 17.80 ?  137 ILE   A CG1  1 
ATOM   3042 C  CG1  B ILE   A 1 137 ? 8.101  -9.357  -4.315  0.50 19.22 ?  137 ILE   A CG1  1 
ATOM   3043 C  CG2  A ILE   A 1 137 ? 8.938  -12.143 -4.519  0.50 17.33 ?  137 ILE   A CG2  1 
ATOM   3044 C  CG2  B ILE   A 1 137 ? 8.806  -11.777 -4.448  0.50 18.28 ?  137 ILE   A CG2  1 
ATOM   3045 C  CD1  A ILE   A 1 137 ? 6.735  -10.046 -4.771  0.50 18.74 ?  137 ILE   A CD1  1 
ATOM   3046 C  CD1  B ILE   A 1 137 ? 6.882  -9.507  -5.205  0.50 20.25 ?  137 ILE   A CD1  1 
ATOM   3047 H  H    A ILE   A 1 137 ? 10.342 -8.465  -4.525  0.50 18.80 ?  137 ILE   A H    1 
ATOM   3048 H  H    B ILE   A 1 137 ? 10.464 -8.208  -4.616  0.50 19.69 ?  137 ILE   A H    1 
ATOM   3049 H  HA   A ILE   A 1 137 ? 10.350 -10.469 -2.873  0.50 19.08 ?  137 ILE   A HA   1 
ATOM   3050 H  HA   B ILE   A 1 137 ? 10.274 -10.157 -2.887  0.50 20.25 ?  137 ILE   A HA   1 
ATOM   3051 H  HB   A ILE   A 1 137 ? 9.332  -10.392 -5.503  0.50 20.31 ?  137 ILE   A HB   1 
ATOM   3052 H  HB   B ILE   A 1 137 ? 9.462  -10.215 -5.590  0.50 21.63 ?  137 ILE   A HB   1 
ATOM   3053 H  HG12 A ILE   A 1 137 ? 7.884  -10.115 -3.091  0.50 21.39 ?  137 ILE   A HG12 1 
ATOM   3054 H  HG12 B ILE   A 1 137 ? 7.823  -9.510  -3.400  0.50 23.10 ?  137 ILE   A HG12 1 
ATOM   3055 H  HG13 A ILE   A 1 137 ? 8.252  -8.899  -4.043  0.50 21.39 ?  137 ILE   A HG13 1 
ATOM   3056 H  HG13 B ILE   A 1 137 ? 8.424  -8.447  -4.414  0.50 23.10 ?  137 ILE   A HG13 1 
ATOM   3057 H  HG21 A ILE   A 1 137 ? 8.161  -12.349 -5.062  0.50 20.83 ?  137 ILE   A HG21 1 
ATOM   3058 H  HG21 B ILE   A 1 137 ? 7.953  -11.920 -4.886  0.50 21.97 ?  137 ILE   A HG21 1 
ATOM   3059 H  HG22 A ILE   A 1 137 ? 9.696  -12.628 -4.866  0.50 20.83 ?  137 ILE   A HG22 1 
ATOM   3060 H  HG22 B ILE   A 1 137 ? 9.473  -12.365 -4.834  0.50 21.97 ?  137 ILE   A HG22 1 
ATOM   3061 H  HG23 A ILE   A 1 137 ? 8.772  -12.394 -3.599  0.50 20.83 ?  137 ILE   A HG23 1 
ATOM   3062 H  HG23 B ILE   A 1 137 ? 8.722  -11.947 -3.498  0.50 21.97 ?  137 ILE   A HG23 1 
ATOM   3063 H  HD11 A ILE   A 1 137 ? 6.005  -9.857  -4.170  0.50 22.52 ?  137 ILE   A HD11 1 
ATOM   3064 H  HD11 B ILE   A 1 137 ? 6.580  -8.629  -5.483  0.50 24.33 ?  137 ILE   A HD11 1 
ATOM   3065 H  HD12 A ILE   A 1 137 ? 6.718  -9.435  -5.524  0.50 22.52 ?  137 ILE   A HD12 1 
ATOM   3066 H  HD12 B ILE   A 1 137 ? 7.122  -10.034 -5.985  0.50 24.33 ?  137 ILE   A HD12 1 
ATOM   3067 H  HD13 A ILE   A 1 137 ? 6.665  -10.958 -5.087  0.50 22.52 ?  137 ILE   A HD13 1 
ATOM   3068 H  HD13 B ILE   A 1 137 ? 6.181  -9.959  -4.708  0.50 24.33 ?  137 ILE   A HD13 1 
ATOM   3069 N  N    A HIS   A 1 138 ? 12.317 -10.849 -5.349  0.50 15.49 ?  138 HIS   A N    1 
ATOM   3070 N  N    B HIS   A 1 138 ? 12.292 -10.708 -5.306  0.50 16.91 ?  138 HIS   A N    1 
ATOM   3071 C  CA   A HIS   A 1 138 ? 13.505 -11.580 -5.770  0.50 15.38 ?  138 HIS   A CA   1 
ATOM   3072 C  CA   B HIS   A 1 138 ? 13.424 -11.525 -5.729  0.50 16.34 ?  138 HIS   A CA   1 
ATOM   3073 C  C    A HIS   A 1 138 ? 14.638 -11.420 -4.763  0.50 14.65 ?  138 HIS   A C    1 
ATOM   3074 C  C    B HIS   A 1 138 ? 14.585 -11.412 -4.748  0.50 15.18 ?  138 HIS   A C    1 
ATOM   3075 O  O    A HIS   A 1 138 ? 15.318 -12.398 -4.426  0.50 14.82 ?  138 HIS   A O    1 
ATOM   3076 O  O    B HIS   A 1 138 ? 15.233 -12.414 -4.421  0.50 15.55 ?  138 HIS   A O    1 
ATOM   3077 C  CB   A HIS   A 1 138 ? 13.934 -11.120 -7.161  0.50 16.27 ?  138 HIS   A CB   1 
ATOM   3078 C  CB   B HIS   A 1 138 ? 13.847 -11.101 -7.135  0.50 16.79 ?  138 HIS   A CB   1 
ATOM   3079 C  CG   A HIS   A 1 138 ? 15.182 -11.785 -7.649  0.50 17.12 ?  138 HIS   A CG   1 
ATOM   3080 C  CG   B HIS   A 1 138 ? 15.131 -11.717 -7.589  0.50 17.38 ?  138 HIS   A CG   1 
ATOM   3081 N  ND1  A HIS   A 1 138 ? 15.272 -13.146 -7.846  0.50 18.17 ?  138 HIS   A ND1  1 
ATOM   3082 N  ND1  B HIS   A 1 138 ? 15.242 -13.051 -7.919  0.50 18.41 ?  138 HIS   A ND1  1 
ATOM   3083 C  CD2  A HIS   A 1 138 ? 16.397 -11.277 -7.961  0.50 17.59 ?  138 HIS   A CD2  1 
ATOM   3084 C  CD2  B HIS   A 1 138 ? 16.362 -11.181 -7.764  0.50 17.53 ?  138 HIS   A CD2  1 
ATOM   3085 C  CE1  A HIS   A 1 138 ? 16.487 -13.447 -8.269  0.50 18.46 ?  138 HIS   A CE1  1 
ATOM   3086 C  CE1  B HIS   A 1 138 ? 16.486 -13.309 -8.281  0.50 18.44 ?  138 HIS   A CE1  1 
ATOM   3087 N  NE2  A HIS   A 1 138 ? 17.189 -12.331 -8.347  0.50 18.12 ?  138 HIS   A NE2  1 
ATOM   3088 N  NE2  B HIS   A 1 138 ? 17.186 -12.192 -8.194  0.50 18.02 ?  138 HIS   A NE2  1 
ATOM   3089 H  H    A HIS   A 1 138 ? 12.083 -10.207 -5.880  0.50 18.62 ?  138 HIS   A H    1 
ATOM   3090 H  H    B HIS   A 1 138 ? 12.097 -10.065 -5.845  0.50 20.33 ?  138 HIS   A H    1 
ATOM   3091 H  HA   A HIS   A 1 138 ? 13.287 -12.521 -5.830  0.50 18.49 ?  138 HIS   A HA   1 
ATOM   3092 H  HA   B HIS   A 1 138 ? 13.149 -12.451 -5.766  0.50 19.64 ?  138 HIS   A HA   1 
ATOM   3093 H  HB2  A HIS   A 1 138 ? 13.224 -11.323 -7.795  0.50 19.55 ?  138 HIS   A HB2  1 
ATOM   3094 H  HB2  B HIS   A 1 138 ? 13.153 -11.363 -7.763  0.50 20.18 ?  138 HIS   A HB2  1 
ATOM   3095 H  HB3  A HIS   A 1 138 ? 14.095 -10.165 -7.145  0.50 19.55 ?  138 HIS   A HB3  1 
ATOM   3096 H  HB3  B HIS   A 1 138 ? 13.957 -10.137 -7.155  0.50 20.18 ?  138 HIS   A HB3  1 
ATOM   3097 H  HD1  A HIS   A 1 138 ? 14.635 -13.711 -7.720  0.50 21.84 ?  138 HIS   A HD1  1 
ATOM   3098 H  HD1  B HIS   A 1 138 ? 14.600 -13.624 -7.896  0.50 22.12 ?  138 HIS   A HD1  1 
ATOM   3099 H  HD2  A HIS   A 1 138 ? 16.645 -10.383 -7.926  0.50 21.15 ?  138 HIS   A HD2  1 
ATOM   3100 H  HD2  B HIS   A 1 138 ? 16.603 -10.295 -7.621  0.50 21.07 ?  138 HIS   A HD2  1 
ATOM   3101 H  HE1  A HIS   A 1 138 ? 16.794 -14.300 -8.475  0.50 22.19 ?  138 HIS   A HE1  1 
ATOM   3102 H  HE1  B HIS   A 1 138 ? 16.813 -14.138 -8.549  0.50 22.16 ?  138 HIS   A HE1  1 
ATOM   3103 N  N    . SER   A 1 139 ? 14.860 -10.199 -4.267  1.00 14.61 ?  139 SER   A N    1 
ATOM   3104 C  CA   . SER   A 1 139 ? 15.936 -10.003 -3.303  1.00 14.11 ?  139 SER   A CA   1 
ATOM   3105 C  C    . SER   A 1 139 ? 15.724 -10.849 -2.051  1.00 13.40 ?  139 SER   A C    1 
ATOM   3106 O  O    . SER   A 1 139 ? 16.675 -11.439 -1.524  1.00 13.56 ?  139 SER   A O    1 
ATOM   3107 C  CB   . SER   A 1 139 ? 16.065 -8.524  -2.950  1.00 14.26 ?  139 SER   A CB   1 
ATOM   3108 O  OG   . SER   A 1 139 ? 17.150 -8.352  -2.060  1.00 14.04 ?  139 SER   A OG   1 
ATOM   3109 H  H    A SER   A 1 139 ? 14.415 -9.490  -4.468  0.50 17.57 ?  139 SER   A H    1 
ATOM   3110 H  H    B SER   A 1 139 ? 14.435 -9.480  -4.478  0.50 17.57 ?  139 SER   A H    1 
ATOM   3111 H  HA   . SER   A 1 139 ? 16.773 -10.279 -3.709  1.00 16.97 ?  139 SER   A HA   1 
ATOM   3112 H  HB2  . SER   A 1 139 ? 16.222 -8.007  -3.758  1.00 17.14 ?  139 SER   A HB2  1 
ATOM   3113 H  HB3  . SER   A 1 139 ? 15.252 -8.222  -2.513  1.00 17.14 ?  139 SER   A HB3  1 
ATOM   3114 H  HG   . SER   A 1 139 ? 17.244 -7.540  -1.862  1.00 16.88 ?  139 SER   A HG   1 
ATOM   3115 N  N    A LEU   A 1 140 ? 14.469 -11.008 -1.629  0.50 13.48 ?  140 LEU   A N    1 
ATOM   3116 N  N    B LEU   A 1 140 ? 14.505 -10.822 -1.492  0.50 13.11 ?  140 LEU   A N    1 
ATOM   3117 C  CA   A LEU   A 1 140 ? 14.194 -11.876 -0.491  0.50 12.81 ?  140 LEU   A CA   1 
ATOM   3118 C  CA   B LEU   A 1 140 ? 14.235 -11.590 -0.276  0.50 12.26 ?  140 LEU   A CA   1 
ATOM   3119 C  C    A LEU   A 1 140 ? 14.477 -13.337 -0.826  0.50 12.59 ?  140 LEU   A C    1 
ATOM   3120 C  C    B LEU   A 1 140 ? 14.484 -13.077 -0.505  0.50 12.03 ?  140 LEU   A C    1 
ATOM   3121 O  O    A LEU   A 1 140 ? 15.085 -14.057 -0.024  0.50 12.14 ?  140 LEU   A O    1 
ATOM   3122 O  O    B LEU   A 1 140 ? 14.993 -13.780 0.380   0.50 12.48 ?  140 LEU   A O    1 
ATOM   3123 C  CB   A LEU   A 1 140 ? 12.750 -11.693 -0.035  0.50 13.13 ?  140 LEU   A CB   1 
ATOM   3124 C  CB   B LEU   A 1 140 ? 12.800 -11.333 0.205   0.50 12.23 ?  140 LEU   A CB   1 
ATOM   3125 C  CG   A LEU   A 1 140 ? 12.339 -12.592 1.129   0.50 13.27 ?  140 LEU   A CG   1 
ATOM   3126 C  CG   B LEU   A 1 140 ? 12.298 -12.172 1.388   0.50 12.36 ?  140 LEU   A CG   1 
ATOM   3127 C  CD1  A LEU   A 1 140 ? 13.258 -12.384 2.323   0.50 14.01 ?  140 LEU   A CD1  1 
ATOM   3128 C  CD1  B LEU   A 1 140 ? 13.174 -11.980 2.618   0.50 12.47 ?  140 LEU   A CD1  1 
ATOM   3129 C  CD2  A LEU   A 1 140 ? 10.886 -12.339 1.509   0.50 13.58 ?  140 LEU   A CD2  1 
ATOM   3130 C  CD2  B LEU   A 1 140 ? 10.840 -11.848 1.715   0.50 12.73 ?  140 LEU   A CD2  1 
ATOM   3131 H  H    A LEU   A 1 140 ? 13.779 -10.636 -1.982  0.50 16.21 ?  140 LEU   A H    1 
ATOM   3132 H  H    B LEU   A 1 140 ? 13.838 -10.362 -1.787  0.50 15.76 ?  140 LEU   A H    1 
ATOM   3133 H  HA   A LEU   A 1 140 ? 14.778 -11.623 0.235   0.50 15.40 ?  140 LEU   A HA   1 
ATOM   3134 H  HA   B LEU   A 1 140 ? 14.833 -11.284 0.427   0.50 14.75 ?  140 LEU   A HA   1 
ATOM   3135 H  HB2  A LEU   A 1 140 ? 12.633 -10.775 0.245   0.50 15.79 ?  140 LEU   A HB2  1 
ATOM   3136 H  HB2  B LEU   A 1 140 ? 12.727 -10.400 0.472   0.50 14.71 ?  140 LEU   A HB2  1 
ATOM   3137 H  HB3  A LEU   A 1 140 ? 12.164 -11.888 -0.782  0.50 15.79 ?  140 LEU   A HB3  1 
ATOM   3138 H  HB3  B LEU   A 1 140 ? 12.198 -11.498 -0.534  0.50 14.71 ?  140 LEU   A HB3  1 
ATOM   3139 H  HG   A LEU   A 1 140 ? 12.413 -13.521 0.853   0.50 15.96 ?  140 LEU   A HG   1 
ATOM   3140 H  HG   B LEU   A 1 140 ? 12.332 -13.107 1.144   0.50 14.86 ?  140 LEU   A HG   1 
ATOM   3141 H  HD11 A LEU   A 1 140 ? 12.878 -12.834 3.092   0.50 16.85 ?  140 LEU   A HD11 1 
ATOM   3142 H  HD11 B LEU   A 1 140 ? 12.797 -12.488 3.356   0.50 14.99 ?  140 LEU   A HD11 1 
ATOM   3143 H  HD12 A LEU   A 1 140 ? 14.131 -12.756 2.119   0.50 16.85 ?  140 LEU   A HD12 1 
ATOM   3144 H  HD12 B LEU   A 1 140 ? 14.066 -12.303 2.418   0.50 14.99 ?  140 LEU   A HD12 1 
ATOM   3145 H  HD13 A LEU   A 1 140 ? 13.334 -11.433 2.498   0.50 16.85 ?  140 LEU   A HD13 1 
ATOM   3146 H  HD13 B LEU   A 1 140 ? 13.202 -11.039 2.844   0.50 14.99 ?  140 LEU   A HD13 1 
ATOM   3147 H  HD21 A LEU   A 1 140 ? 10.647 -12.923 2.246   0.50 16.33 ?  140 LEU   A HD21 1 
ATOM   3148 H  HD21 B LEU   A 1 140 ? 10.525 -12.460 2.401   0.50 15.31 ?  140 LEU   A HD21 1 
ATOM   3149 H  HD22 A LEU   A 1 140 ? 10.786 -11.412 1.774   0.50 16.33 ?  140 LEU   A HD22 1 
ATOM   3150 H  HD22 B LEU   A 1 140 ? 10.783 -10.935 2.038   0.50 15.31 ?  140 LEU   A HD22 1 
ATOM   3151 H  HD23 A LEU   A 1 140 ? 10.321 -12.527 0.742   0.50 16.33 ?  140 LEU   A HD23 1 
ATOM   3152 H  HD23 B LEU   A 1 140 ? 10.303 -11.950 0.913   0.50 15.31 ?  140 LEU   A HD23 1 
ATOM   3153 N  N    A ARG   A 1 141 ? 14.044 -13.793 -2.006  0.50 13.05 ?  141 ARG   A N    1 
ATOM   3154 N  N    B ARG   A 1 141 ? 14.143 -13.572 -1.697  0.50 12.55 ?  141 ARG   A N    1 
ATOM   3155 C  CA   A ARG   A 1 141 ? 14.311 -15.168 -2.416  0.50 14.21 ?  141 ARG   A CA   1 
ATOM   3156 C  CA   B ARG   A 1 141 ? 14.356 -14.985 -1.992  0.50 13.23 ?  141 ARG   A CA   1 
ATOM   3157 C  C    A ARG   A 1 141 ? 15.802 -15.459 -2.386  0.50 13.84 ?  141 ARG   A C    1 
ATOM   3158 C  C    B ARG   A 1 141 ? 15.845 -15.313 -2.097  0.50 12.78 ?  141 ARG   A C    1 
ATOM   3159 O  O    A ARG   A 1 141 ? 16.228 -16.524 -1.928  0.50 13.52 ?  141 ARG   A O    1 
ATOM   3160 O  O    B ARG   A 1 141 ? 16.311 -16.296 -1.507  0.50 11.93 ?  141 ARG   A O    1 
ATOM   3161 C  CB   A ARG   A 1 141 ? 13.755 -15.390 -3.824  0.50 15.82 ?  141 ARG   A CB   1 
ATOM   3162 C  CB   B ARG   A 1 141 ? 13.600 -15.387 -3.260  0.50 14.11 ?  141 ARG   A CB   1 
ATOM   3163 C  CG   A ARG   A 1 141 ? 13.684 -16.841 -4.265  0.50 18.07 ?  141 ARG   A CG   1 
ATOM   3164 C  CG   B ARG   A 1 141 ? 13.755 -16.869 -3.635  0.50 15.50 ?  141 ARG   A CG   1 
ATOM   3165 C  CD   A ARG   A 1 141 ? 12.667 -17.596 -3.444  0.50 19.18 ?  141 ARG   A CD   1 
ATOM   3166 C  CD   B ARG   A 1 141 ? 13.159 -17.814 -2.590  0.50 16.76 ?  141 ARG   A CD   1 
ATOM   3167 N  NE   A ARG   A 1 141 ? 13.295 -18.390 -2.397  0.50 20.01 ?  141 ARG   A NE   1 
ATOM   3168 N  NE   B ARG   A 1 141 ? 11.726 -17.600 -2.438  0.50 17.65 ?  141 ARG   A NE   1 
ATOM   3169 C  CZ   A ARG   A 1 141 ? 12.630 -18.971 -1.408  0.50 20.47 ?  141 ARG   A CZ   1 
ATOM   3170 C  CZ   B ARG   A 1 141 ? 10.968 -18.186 -1.522  0.50 18.14 ?  141 ARG   A CZ   1 
ATOM   3171 N  NH1  A ARG   A 1 141 ? 11.327 -18.801 -1.259  0.50 21.21 ?  141 ARG   A NH1  1 
ATOM   3172 N  NH1  B ARG   A 1 141 ? 11.474 -19.046 -0.651  0.50 18.48 ?  141 ARG   A NH1  1 
ATOM   3173 N  NH2  A ARG   A 1 141 ? 13.290 -19.736 -0.545  0.50 20.34 ?  141 ARG   A NH2  1 
ATOM   3174 N  NH2  B ARG   A 1 141 ? 9.669  -17.903 -1.479  0.50 18.94 ?  141 ARG   A NH2  1 
ATOM   3175 H  H    A ARG   A 1 141 ? 13.609 -13.336 -2.585  0.50 15.70 ?  141 ARG   A H    1 
ATOM   3176 H  H    B ARG   A 1 141 ? 13.788 -13.112 -2.332  0.50 15.09 ?  141 ARG   A H    1 
ATOM   3177 H  HA   A ARG   A 1 141 ? 13.879 -15.786 -1.809  0.50 17.09 ?  141 ARG   A HA   1 
ATOM   3178 H  HA   B ARG   A 1 141 ? 13.994 -15.499 -1.261  0.50 15.91 ?  141 ARG   A HA   1 
ATOM   3179 H  HB2  A ARG   A 1 141 ? 12.856 -15.033 -3.860  0.50 19.01 ?  141 ARG   A HB2  1 
ATOM   3180 H  HB2  B ARG   A 1 141 ? 12.651 -15.212 -3.127  0.50 16.97 ?  141 ARG   A HB2  1 
ATOM   3181 H  HB3  A ARG   A 1 141 ? 14.318 -14.926 -4.460  0.50 19.01 ?  141 ARG   A HB3  1 
ATOM   3182 H  HB3  B ARG   A 1 141 ? 13.924 -14.853 -4.003  0.50 16.97 ?  141 ARG   A HB3  1 
ATOM   3183 H  HG2  A ARG   A 1 141 ? 13.419 -16.888 -5.199  0.50 21.71 ?  141 ARG   A HG2  1 
ATOM   3184 H  HG2  B ARG   A 1 141 ? 13.301 -17.028 -4.477  0.50 18.63 ?  141 ARG   A HG2  1 
ATOM   3185 H  HG3  A ARG   A 1 141 ? 14.551 -17.265 -4.142  0.50 21.71 ?  141 ARG   A HG3  1 
ATOM   3186 H  HG3  B ARG   A 1 141 ? 14.699 -17.076 -3.728  0.50 18.63 ?  141 ARG   A HG3  1 
ATOM   3187 H  HD2  A ARG   A 1 141 ? 12.068 -16.963 -3.019  0.50 23.04 ?  141 ARG   A HD2  1 
ATOM   3188 H  HD2  B ARG   A 1 141 ? 13.302 -18.731 -2.873  0.50 20.15 ?  141 ARG   A HD2  1 
ATOM   3189 H  HD3  A ARG   A 1 141 ? 12.165 -18.192 -4.025  0.50 23.04 ?  141 ARG   A HD3  1 
ATOM   3190 H  HD3  B ARG   A 1 141 ? 13.584 -17.658 -1.733  0.50 20.15 ?  141 ARG   A HD3  1 
ATOM   3191 H  HE   A ARG   A 1 141 ? 14.132 -18.571 -2.480  0.50 24.04 ?  141 ARG   A HE   1 
ATOM   3192 H  HE   B ARG   A 1 141 ? 11.344 -17.055 -2.984  0.50 21.21 ?  141 ARG   A HE   1 
ATOM   3193 H  HH11 A ARG   A 1 141 ? 10.886 -18.319 -1.817  0.50 25.49 ?  141 ARG   A HH11 1 
ATOM   3194 H  HH11 B ARG   A 1 141 ? 12.310 -19.240 -0.673  0.50 22.21 ?  141 ARG   A HH11 1 
ATOM   3195 H  HH12 A ARG   A 1 141 ? 10.917 -19.189 -0.609  0.50 25.49 ?  141 ARG   A HH12 1 
ATOM   3196 H  HH12 B ARG   A 1 141 ? 10.960 -19.418 -0.070  0.50 22.21 ?  141 ARG   A HH12 1 
ATOM   3197 H  HH21 A ARG   A 1 141 ? 14.140 -19.848 -0.633  0.50 24.44 ?  141 ARG   A HH21 1 
ATOM   3198 H  HH21 B ARG   A 1 141 ? 9.331  -17.347 -2.042  0.50 22.76 ?  141 ARG   A HH21 1 
ATOM   3199 H  HH22 A ARG   A 1 141 ? 12.873 -20.110 0.106   0.50 24.44 ?  141 ARG   A HH22 1 
ATOM   3200 H  HH22 B ARG   A 1 141 ? 9.166  -18.280 -0.892  0.50 22.76 ?  141 ARG   A HH22 1 
ATOM   3201 N  N    . VAL   A 1 142 ? 16.613 -14.511 -2.851  1.00 13.41 ?  142 VAL   A N    1 
ATOM   3202 C  CA   . VAL   A 1 142 ? 18.059 -14.723 -2.899  1.00 13.38 ?  142 VAL   A CA   1 
ATOM   3203 C  C    . VAL   A 1 142 ? 18.639 -14.705 -1.493  1.00 12.84 ?  142 VAL   A C    1 
ATOM   3204 O  O    . VAL   A 1 142 ? 19.497 -15.524 -1.150  1.00 13.30 ?  142 VAL   A O    1 
ATOM   3205 C  CB   . VAL   A 1 142 ? 18.752 -13.698 -3.818  1.00 13.72 ?  142 VAL   A CB   1 
ATOM   3206 C  CG1  . VAL   A 1 142 ? 20.268 -13.902 -3.786  1.00 13.25 ?  142 VAL   A CG1  1 
ATOM   3207 C  CG2  . VAL   A 1 142 ? 18.240 -13.821 -5.242  1.00 14.91 ?  142 VAL   A CG2  1 
ATOM   3208 H  H    A VAL   A 1 142 ? 16.355 -13.736 -3.135  0.50 16.13 ?  142 VAL   A H    1 
ATOM   3209 H  H    B VAL   A 1 142 ? 16.331 -13.849 -3.330  0.50 16.13 ?  142 VAL   A H    1 
ATOM   3210 H  HA   . VAL   A 1 142 ? 18.229 -15.595 -3.272  1.00 16.09 ?  142 VAL   A HA   1 
ATOM   3211 H  HB   . VAL   A 1 142 ? 18.565 -12.795 -3.503  1.00 16.50 ?  142 VAL   A HB   1 
ATOM   3212 H  HG11 . VAL   A 1 142 ? 20.670 -13.407 -4.518  1.00 15.94 ?  142 VAL   A HG11 1 
ATOM   3213 H  HG12 . VAL   A 1 142 ? 20.618 -13.569 -2.940  1.00 15.94 ?  142 VAL   A HG12 1 
ATOM   3214 H  HG13 . VAL   A 1 142 ? 20.461 -14.844 -3.876  1.00 15.94 ?  142 VAL   A HG13 1 
ATOM   3215 H  HG21 . VAL   A 1 142 ? 18.705 -13.178 -5.801  1.00 17.93 ?  142 VAL   A HG21 1 
ATOM   3216 H  HG22 . VAL   A 1 142 ? 18.417 -14.721 -5.557  1.00 17.93 ?  142 VAL   A HG22 1 
ATOM   3217 H  HG23 . VAL   A 1 142 ? 17.291 -13.644 -5.250  1.00 17.93 ?  142 VAL   A HG23 1 
ATOM   3218 N  N    . CYS   A 1 143 ? 18.174 -13.781 -0.653  1.00 12.60 ?  143 CYS   A N    1 
ATOM   3219 C  CA   . CYS   A 1 143 ? 18.637 -13.732 0.729   1.00 12.71 ?  143 CYS   A CA   1 
ATOM   3220 C  C    . CYS   A 1 143 ? 18.407 -15.071 1.423   1.00 12.84 ?  143 CYS   A C    1 
ATOM   3221 O  O    . CYS   A 1 143 ? 19.326 -15.663 1.999   1.00 12.66 ?  143 CYS   A O    1 
ATOM   3222 C  CB   . CYS   A 1 143 ? 17.908 -12.613 1.471   1.00 13.28 ?  143 CYS   A CB   1 
ATOM   3223 S  SG   . CYS   A 1 143 ? 18.399 -12.445 3.196   1.00 13.55 ?  143 CYS   A SG   1 
ATOM   3224 H  H    . CYS   A 1 143 ? 17.594 -13.182 -0.857  1.00 15.15 ?  143 CYS   A H    1 
ATOM   3225 H  HA   . CYS   A 1 143 ? 19.585 -13.547 0.744   1.00 15.28 ?  143 CYS   A HA   1 
ATOM   3226 H  HB2  . CYS   A 1 143 ? 18.086 -11.774 1.024   1.00 15.97 ?  143 CYS   A HB2  1 
ATOM   3227 H  HB3  . CYS   A 1 143 ? 16.957 -12.797 1.454   1.00 15.97 ?  143 CYS   A HB3  1 
ATOM   3228 H  HG   . CYS   A 1 143 ? 17.822 -11.504 3.662   1.00 16.30 ?  143 CYS   A HG   1 
ATOM   3229 N  N    . VAL   A 1 144 ? 17.178 -15.577 1.358   1.00 13.07 ?  144 VAL   A N    1 
ATOM   3230 C  CA   . VAL   A 1 144 ? 16.837 -16.813 2.053   1.00 14.52 ?  144 VAL   A CA   1 
ATOM   3231 C  C    . VAL   A 1 144 ? 17.653 -17.985 1.526   1.00 14.39 ?  144 VAL   A C    1 
ATOM   3232 O  O    . VAL   A 1 144 ? 18.024 -18.892 2.283   1.00 15.00 ?  144 VAL   A O    1 
ATOM   3233 C  CB   . VAL   A 1 144 ? 15.320 -17.054 1.941   1.00 17.47 ?  144 VAL   A CB   1 
ATOM   3234 C  CG1  . VAL   A 1 144 ? 14.963 -18.485 2.283   1.00 19.22 ?  144 VAL   A CG1  1 
ATOM   3235 C  CG2  . VAL   A 1 144 ? 14.573 -16.055 2.828   1.00 17.33 ?  144 VAL   A CG2  1 
ATOM   3236 H  H    . VAL   A 1 144 ? 16.521 -15.218 0.924   1.00 15.72 ?  144 VAL   A H    1 
ATOM   3237 H  HA   . VAL   A 1 144 ? 17.042 -16.712 2.988   1.00 17.45 ?  144 VAL   A HA   1 
ATOM   3238 H  HB   . VAL   A 1 144 ? 15.039 -16.893 1.022   1.00 21.00 ?  144 VAL   A HB   1 
ATOM   3239 H  HG11 . VAL   A 1 144 ? 14.010 -18.536 2.475   1.00 23.10 ?  144 VAL   A HG11 1 
ATOM   3240 H  HG12 . VAL   A 1 144 ? 15.173 -19.056 1.529   1.00 23.10 ?  144 VAL   A HG12 1 
ATOM   3241 H  HG13 . VAL   A 1 144 ? 15.467 -18.757 3.063   1.00 23.10 ?  144 VAL   A HG13 1 
ATOM   3242 H  HG21 . VAL   A 1 144 ? 13.615 -16.194 2.739   1.00 20.83 ?  144 VAL   A HG21 1 
ATOM   3243 H  HG22 . VAL   A 1 144 ? 14.840 -16.185 3.751   1.00 20.83 ?  144 VAL   A HG22 1 
ATOM   3244 H  HG23 . VAL   A 1 144 ? 14.796 -15.149 2.547   1.00 20.83 ?  144 VAL   A HG23 1 
ATOM   3245 N  N    . ASP   A 1 145 ? 17.918 -18.007 0.224   1.00 14.52 ?  145 ASP   A N    1 
ATOM   3246 C  CA   . ASP   A 1 145 ? 18.629 -19.111 -0.410  1.00 14.98 ?  145 ASP   A CA   1 
ATOM   3247 C  C    . ASP   A 1 145 ? 20.151 -18.963 -0.374  1.00 14.70 ?  145 ASP   A C    1 
ATOM   3248 O  O    . ASP   A 1 145 ? 20.856 -19.856 -0.863  1.00 16.78 ?  145 ASP   A O    1 
ATOM   3249 C  CB   . ASP   A 1 145 ? 18.173 -19.246 -1.865  1.00 16.65 ?  145 ASP   A CB   1 
ATOM   3250 C  CG   . ASP   A 1 145 ? 16.728 -19.691 -1.989  1.00 18.60 ?  145 ASP   A CG   1 
ATOM   3251 O  OD1  . ASP   A 1 145 ? 16.167 -20.228 -1.008  1.00 19.38 ?  145 ASP   A OD1  1 
ATOM   3252 O  OD2  . ASP   A 1 145 ? 16.155 -19.496 -3.078  1.00 20.04 -1 145 ASP   A OD2  1 
ATOM   3253 H  H    . ASP   A 1 145 ? 17.678 -17.390 -0.325  1.00 17.46 ?  145 ASP   A H    1 
ATOM   3254 H  HA   . ASP   A 1 145 ? 18.397 -19.934 0.047   1.00 18.01 ?  145 ASP   A HA   1 
ATOM   3255 H  HB2  . ASP   A 1 145 ? 18.259 -18.386 -2.307  1.00 20.02 ?  145 ASP   A HB2  1 
ATOM   3256 H  HB3  . ASP   A 1 145 ? 18.722 -19.906 -2.311  1.00 20.02 ?  145 ASP   A HB3  1 
ATOM   3257 N  N    . THR   A 1 146 ? 20.675 -17.877 0.186   1.00 13.07 ?  146 THR   A N    1 
ATOM   3258 C  CA   . THR   A 1 146 ? 22.113 -17.616 0.195   1.00 12.44 ?  146 THR   A CA   1 
ATOM   3259 C  C    . THR   A 1 146 ? 22.681 -17.424 1.588   1.00 12.39 ?  146 THR   A C    1 
ATOM   3260 O  O    . THR   A 1 146 ? 23.759 -17.952 1.892   1.00 13.31 ?  146 THR   A O    1 
ATOM   3261 C  CB   . THR   A 1 146 ? 22.434 -16.362 -0.644  1.00 12.56 ?  146 THR   A CB   1 
ATOM   3262 O  OG1  . THR   A 1 146 ? 21.902 -16.522 -1.960  1.00 13.11 ?  146 THR   A OG1  1 
ATOM   3263 C  CG2  . THR   A 1 146 ? 23.940 -16.124 -0.730  1.00 13.38 ?  146 THR   A CG2  1 
ATOM   3264 H  H    . THR   A 1 146 ? 20.208 -17.260 0.565   1.00 15.72 ?  146 THR   A H    1 
ATOM   3265 H  HA   . THR   A 1 146 ? 22.572 -18.361 -0.208  1.00 14.96 ?  146 THR   A HA   1 
ATOM   3266 H  HB   . THR   A 1 146 ? 22.031 -15.579 -0.233  1.00 15.10 ?  146 THR   A HB   1 
ATOM   3267 H  HG1  . THR   A 1 146 ? 21.067 -16.606 -1.930  1.00 15.77 ?  146 THR   A HG1  1 
ATOM   3268 H  HG21 . THR   A 1 146 ? 24.133 -15.464 -1.413  1.00 16.09 ?  146 THR   A HG21 1 
ATOM   3269 H  HG22 . THR   A 1 146 ? 24.275 -15.801 0.122   1.00 16.09 ?  146 THR   A HG22 1 
ATOM   3270 H  HG23 . THR   A 1 146 ? 24.391 -16.952 -0.955  1.00 16.09 ?  146 THR   A HG23 1 
ATOM   3271 N  N    . VAL   A 1 147 ? 21.999 -16.657 2.429   1.00 12.49 ?  147 VAL   A N    1 
ATOM   3272 C  CA   . VAL   A 1 147 ? 22.492 -16.365 3.765   1.00 12.43 ?  147 VAL   A CA   1 
ATOM   3273 C  C    . VAL   A 1 147 ? 22.176 -17.536 4.683   1.00 12.83 ?  147 VAL   A C    1 
ATOM   3274 O  O    . VAL   A 1 147 ? 21.033 -18.006 4.741   1.00 13.31 ?  147 VAL   A O    1 
ATOM   3275 C  CB   . VAL   A 1 147 ? 21.875 -15.061 4.290   1.00 12.47 ?  147 VAL   A CB   1 
ATOM   3276 C  CG1  . VAL   A 1 147 ? 22.426 -14.754 5.656   1.00 13.69 ?  147 VAL   A CG1  1 
ATOM   3277 C  CG2  . VAL   A 1 147 ? 22.124 -13.909 3.322   1.00 12.69 ?  147 VAL   A CG2  1 
ATOM   3278 H  H    . VAL   A 1 147 ? 21.235 -16.297 2.251   1.00 15.02 ?  147 VAL   A H    1 
ATOM   3279 H  HA   . VAL   A 1 147 ? 23.453 -16.253 3.730   1.00 14.95 ?  147 VAL   A HA   1 
ATOM   3280 H  HB   . VAL   A 1 147 ? 20.918 -15.176 4.380   1.00 15.00 ?  147 VAL   A HB   1 
ATOM   3281 H  HG11 . VAL   A 1 147 ? 22.197 -13.846 5.892   1.00 16.47 ?  147 VAL   A HG11 1 
ATOM   3282 H  HG12 . VAL   A 1 147 ? 22.035 -15.372 6.298   1.00 16.47 ?  147 VAL   A HG12 1 
ATOM   3283 H  HG13 . VAL   A 1 147 ? 23.389 -14.864 5.638   1.00 16.47 ?  147 VAL   A HG13 1 
ATOM   3284 H  HG21 . VAL   A 1 147 ? 21.793 -13.086 3.720   1.00 15.27 ?  147 VAL   A HG21 1 
ATOM   3285 H  HG22 . VAL   A 1 147 ? 23.072 -13.837 3.151   1.00 15.27 ?  147 VAL   A HG22 1 
ATOM   3286 H  HG23 . VAL   A 1 147 ? 21.647 -14.087 2.495   1.00 15.27 ?  147 VAL   A HG23 1 
ATOM   3287 N  N    . ARG   A 1 148 ? 23.200 -18.010 5.394   1.00 13.18 ?  148 ARG   A N    1 
ATOM   3288 C  CA   . ARG   A 1 148 ? 23.072 -19.091 6.358   1.00 13.07 ?  148 ARG   A CA   1 
ATOM   3289 C  C    . ARG   A 1 148 ? 23.211 -18.626 7.796   1.00 13.54 ?  148 ARG   A C    1 
ATOM   3290 O  O    . ARG   A 1 148 ? 22.807 -19.354 8.714   1.00 15.31 ?  148 ARG   A O    1 
ATOM   3291 C  CB   . ARG   A 1 148 ? 24.099 -20.194 6.069   1.00 13.66 ?  148 ARG   A CB   1 
ATOM   3292 C  CG   . ARG   A 1 148 ? 23.938 -20.819 4.697   1.00 14.85 ?  148 ARG   A CG   1 
ATOM   3293 C  CD   . ARG   A 1 148 ? 25.026 -21.852 4.399   1.00 15.76 ?  148 ARG   A CD   1 
ATOM   3294 N  NE   . ARG   A 1 148 ? 26.363 -21.271 4.413   1.00 15.97 ?  148 ARG   A NE   1 
ATOM   3295 C  CZ   . ARG   A 1 148 ? 26.871 -20.535 3.434   1.00 14.86 ?  148 ARG   A CZ   1 
ATOM   3296 N  NH1  . ARG   A 1 148 ? 26.190 -20.298 2.326   1.00 15.32 ?  148 ARG   A NH1  1 
ATOM   3297 N  NH2  . ARG   A 1 148 ? 28.092 -20.022 3.572   1.00 15.33 ?  148 ARG   A NH2  1 
ATOM   3298 H  H    . ARG   A 1 148 ? 24.008 -17.710 5.318   1.00 15.85 ?  148 ARG   A H    1 
ATOM   3299 H  HA   . ARG   A 1 148 ? 22.192 -19.480 6.263   1.00 15.72 ?  148 ARG   A HA   1 
ATOM   3300 H  HB2  . ARG   A 1 148 ? 24.989 -19.829 6.128   1.00 16.43 ?  148 ARG   A HB2  1 
ATOM   3301 H  HB3  . ARG   A 1 148 ? 23.986 -20.905 6.727   1.00 16.43 ?  148 ARG   A HB3  1 
ATOM   3302 H  HG2  . ARG   A 1 148 ? 23.075 -21.259 4.649   1.00 17.85 ?  148 ARG   A HG2  1 
ATOM   3303 H  HG3  . ARG   A 1 148 ? 23.992 -20.118 4.029   1.00 17.85 ?  148 ARG   A HG3  1 
ATOM   3304 H  HD2  . ARG   A 1 148 ? 24.996 -22.549 5.075   1.00 18.95 ?  148 ARG   A HD2  1 
ATOM   3305 H  HD3  . ARG   A 1 148 ? 24.867 -22.236 3.522   1.00 18.95 ?  148 ARG   A HD3  1 
ATOM   3306 H  HE   . ARG   A 1 148 ? 26.858 -21.419 5.095   1.00 19.19 ?  148 ARG   A HE   1 
ATOM   3307 H  HH11 . ARG   A 1 148 ? 25.401 -20.618 2.226   1.00 18.42 ?  148 ARG   A HH11 1 
ATOM   3308 H  HH12 . ARG   A 1 148 ? 26.538 -19.813 1.704   1.00 18.42 ?  148 ARG   A HH12 1 
ATOM   3309 H  HH21 . ARG   A 1 148 ? 28.542 -20.169 4.287   1.00 18.43 ?  148 ARG   A HH21 1 
ATOM   3310 H  HH22 . ARG   A 1 148 ? 28.432 -19.540 2.942   1.00 18.43 ?  148 ARG   A HH22 1 
ATOM   3311 N  N    . THR   A 1 149 ? 23.761 -17.434 8.008   1.00 13.77 ?  149 THR   A N    1 
ATOM   3312 C  CA   . THR   A 1 149 ? 23.842 -16.841 9.326   1.00 13.98 ?  149 THR   A CA   1 
ATOM   3313 C  C    . THR   A 1 149 ? 22.516 -16.148 9.642   1.00 13.38 ?  149 THR   A C    1 
ATOM   3314 O  O    . THR   A 1 149 ? 21.574 -16.148 8.840   1.00 14.23 ?  149 THR   A O    1 
ATOM   3315 C  CB   . THR   A 1 149 ? 25.044 -15.904 9.381   1.00 14.13 ?  149 THR   A CB   1 
ATOM   3316 O  OG1  . THR   A 1 149 ? 24.913 -14.962 8.315   1.00 14.15 ?  149 THR   A OG1  1 
ATOM   3317 C  CG2  . THR   A 1 149 ? 26.356 -16.689 9.236   1.00 14.60 ?  149 THR   A CG2  1 
ATOM   3318 H  H    . THR   A 1 149 ? 24.105 -16.941 7.386   1.00 16.56 ?  149 THR   A H    1 
ATOM   3319 H  HA   . THR   A 1 149 ? 23.976 -17.545 9.978   1.00 16.81 ?  149 THR   A HA   1 
ATOM   3320 H  HB   . THR   A 1 149 ? 25.050 -15.442 10.231  1.00 16.99 ?  149 THR   A HB   1 
ATOM   3321 H  HG1  . THR   A 1 149 ? 25.565 -14.429 8.322   1.00 17.01 ?  149 THR   A HG1  1 
ATOM   3322 H  HG21 . THR   A 1 149 ? 27.112 -16.085 9.291   1.00 17.55 ?  149 THR   A HG21 1 
ATOM   3323 H  HG22 . THR   A 1 149 ? 26.431 -17.351 9.943   1.00 17.55 ?  149 THR   A HG22 1 
ATOM   3324 H  HG23 . THR   A 1 149 ? 26.382 -17.146 8.378   1.00 17.55 ?  149 THR   A HG23 1 
ATOM   3325 N  N    . ASN   A 1 150 ? 22.402 -15.602 10.846  1.00 13.72 ?  150 ASN   A N    1 
ATOM   3326 C  CA   . ASN   A 1 150 ? 21.123 -15.093 11.342  1.00 14.08 ?  150 ASN   A CA   1 
ATOM   3327 C  C    . ASN   A 1 150 ? 20.939 -13.651 10.887  1.00 13.40 ?  150 ASN   A C    1 
ATOM   3328 O  O    . ASN   A 1 150 ? 21.684 -12.757 11.306  1.00 14.87 ?  150 ASN   A O    1 
ATOM   3329 C  CB   . ASN   A 1 150 ? 21.075 -15.208 12.861  1.00 16.64 ?  150 ASN   A CB   1 
ATOM   3330 C  CG   . ASN   A 1 150 ? 20.932 -16.639 13.318  1.00 20.74 ?  150 ASN   A CG   1 
ATOM   3331 O  OD1  . ASN   A 1 150 ? 20.330 -17.458 12.626  1.00 22.05 ?  150 ASN   A OD1  1 
ATOM   3332 N  ND2  . ASN   A 1 150 ? 21.500 -16.956 14.475  1.00 23.16 ?  150 ASN   A ND2  1 
ATOM   3333 H  H    . ASN   A 1 150 ? 23.052 -15.510 11.399  1.00 16.50 ?  150 ASN   A H    1 
ATOM   3334 H  HA   . ASN   A 1 150 ? 20.399 -15.625 10.974  1.00 16.93 ?  150 ASN   A HA   1 
ATOM   3335 H  HB2  . ASN   A 1 150 ? 21.894 -14.854 13.237  1.00 20.00 ?  150 ASN   A HB2  1 
ATOM   3336 H  HB3  . ASN   A 1 150 ? 20.311 -14.709 13.196  1.00 20.00 ?  150 ASN   A HB3  1 
ATOM   3337 H  HD21 . ASN   A 1 150 ? 21.445 -17.763 14.779  1.00 27.83 ?  150 ASN   A HD21 1 
ATOM   3338 H  HD22 . ASN   A 1 150 ? 21.918 -16.359 14.931  1.00 27.83 ?  150 ASN   A HD22 1 
ATOM   3339 N  N    . VAL   A 1 151 ? 19.944 -13.420 10.036  1.00 13.25 ?  151 VAL   A N    1 
ATOM   3340 C  CA   . VAL   A 1 151 ? 19.723 -12.110 9.442   1.00 13.04 ?  151 VAL   A CA   1 
ATOM   3341 C  C    . VAL   A 1 151 ? 18.334 -11.595 9.809   1.00 12.81 ?  151 VAL   A C    1 
ATOM   3342 O  O    . VAL   A 1 151 ? 17.324 -12.303 9.662   1.00 14.29 ?  151 VAL   A O    1 
ATOM   3343 C  CB   . VAL   A 1 151 ? 20.012 -12.096 7.924   1.00 14.42 ?  151 VAL   A CB   1 
ATOM   3344 C  CG1  . VAL   A 1 151 ? 19.176 -13.102 7.167   1.00 15.71 ?  151 VAL   A CG1  1 
ATOM   3345 C  CG2  . VAL   A 1 151 ? 19.827 -10.687 7.355   1.00 14.81 ?  151 VAL   A CG2  1 
ATOM   3346 H  H    . VAL   A 1 151 ? 19.378 -14.017 9.779   1.00 15.94 ?  151 VAL   A H    1 
ATOM   3347 H  HA   . VAL   A 1 151 ? 20.361 -11.496 9.837   1.00 15.69 ?  151 VAL   A HA   1 
ATOM   3348 H  HB   . VAL   A 1 151 ? 20.945 -12.335 7.784   1.00 17.34 ?  151 VAL   A HB   1 
ATOM   3349 H  HG11 . VAL   A 1 151 ? 19.349 -13.017 6.215   1.00 18.88 ?  151 VAL   A HG11 1 
ATOM   3350 H  HG12 . VAL   A 1 151 ? 19.415 -13.997 7.464   1.00 18.88 ?  151 VAL   A HG12 1 
ATOM   3351 H  HG13 . VAL   A 1 151 ? 18.236 -12.936 7.346   1.00 18.88 ?  151 VAL   A HG13 1 
ATOM   3352 H  HG21 . VAL   A 1 151 ? 20.148 -10.672 6.437   1.00 17.81 ?  151 VAL   A HG21 1 
ATOM   3353 H  HG22 . VAL   A 1 151 ? 18.887 -10.457 7.378   1.00 17.81 ?  151 VAL   A HG22 1 
ATOM   3354 H  HG23 . VAL   A 1 151 ? 20.339 -10.060 7.890   1.00 17.81 ?  151 VAL   A HG23 1 
ATOM   3355 N  N    . TYR   A 1 152 ? 18.318 -10.355 10.301  1.00 12.94 ?  152 TYR   A N    1 
ATOM   3356 C  CA   . TYR   A 1 152 ? 17.127 -9.614  10.679  1.00 12.83 ?  152 TYR   A CA   1 
ATOM   3357 C  C    . TYR   A 1 152 ? 16.938 -8.515  9.644   1.00 12.48 ?  152 TYR   A C    1 
ATOM   3358 O  O    . TYR   A 1 152 ? 17.713 -7.550  9.600   1.00 12.87 ?  152 TYR   A O    1 
ATOM   3359 C  CB   . TYR   A 1 152 ? 17.307 -9.072  12.094  1.00 13.26 ?  152 TYR   A CB   1 
ATOM   3360 C  CG   . TYR   A 1 152 ? 17.266 -10.202 13.095  1.00 14.59 ?  152 TYR   A CG   1 
ATOM   3361 C  CD1  . TYR   A 1 152 ? 18.397 -10.962 13.375  1.00 15.96 ?  152 TYR   A CD1  1 
ATOM   3362 C  CD2  . TYR   A 1 152 ? 16.083 -10.550 13.721  1.00 14.80 ?  152 TYR   A CD2  1 
ATOM   3363 C  CE1  . TYR   A 1 152 ? 18.356 -12.024 14.263  1.00 17.36 ?  152 TYR   A CE1  1 
ATOM   3364 C  CE2  . TYR   A 1 152 ? 16.025 -11.619 14.610  1.00 16.35 ?  152 TYR   A CE2  1 
ATOM   3365 C  CZ   . TYR   A 1 152 ? 17.167 -12.346 14.877  1.00 17.38 ?  152 TYR   A CZ   1 
ATOM   3366 O  OH   . TYR   A 1 152 ? 17.117 -13.407 15.760  1.00 19.62 ?  152 TYR   A OH   1 
ATOM   3367 H  H    . TYR   A 1 152 ? 19.041 -9.892  10.412  1.00 15.57 ?  152 TYR   A H    1 
ATOM   3368 H  HA   . TYR   A 1 152 ? 16.359 -10.208 10.659  1.00 15.43 ?  152 TYR   A HA   1 
ATOM   3369 H  HB2  . TYR   A 1 152 ? 18.167 -8.637  12.164  1.00 15.95 ?  152 TYR   A HB2  1 
ATOM   3370 H  HB3  . TYR   A 1 152 ? 16.590 -8.458  12.297  1.00 15.95 ?  152 TYR   A HB3  1 
ATOM   3371 H  HD1  . TYR   A 1 152 ? 19.199 -10.748 12.953  1.00 19.18 ?  152 TYR   A HD1  1 
ATOM   3372 H  HD2  . TYR   A 1 152 ? 15.306 -10.070 13.537  1.00 17.80 ?  152 TYR   A HD2  1 
ATOM   3373 H  HE1  . TYR   A 1 152 ? 19.127 -12.514 14.443  1.00 20.87 ?  152 TYR   A HE1  1 
ATOM   3374 H  HE2  . TYR   A 1 152 ? 15.223 -11.836 15.030  1.00 19.65 ?  152 TYR   A HE2  1 
ATOM   3375 H  HH   . TYR   A 1 152 ? 16.336 -13.486 16.069  1.00 23.58 ?  152 TYR   A HH   1 
ATOM   3376 N  N    A LEU   A 1 153 ? 15.956 -8.726  8.760   0.50 12.17 ?  153 LEU   A N    1 
ATOM   3377 N  N    B LEU   A 1 153 ? 15.880 -8.620  8.856   0.50 12.61 ?  153 LEU   A N    1 
ATOM   3378 C  CA   A LEU   A 1 153 ? 15.691 -7.869  7.610   0.50 12.16 ?  153 LEU   A CA   1 
ATOM   3379 C  CA   B LEU   A 1 153 ? 15.612 -7.653  7.806   0.50 12.29 ?  153 LEU   A CA   1 
ATOM   3380 C  C    A LEU   A 1 153 ? 14.677 -6.791  7.971   0.50 12.24 ?  153 LEU   A C    1 
ATOM   3381 C  C    B LEU   A 1 153 ? 14.647 -6.581  8.297   0.50 12.33 ?  153 LEU   A C    1 
ATOM   3382 O  O    A LEU   A 1 153 ? 13.571 -7.096  8.432   0.50 13.01 ?  153 LEU   A O    1 
ATOM   3383 O  O    B LEU   A 1 153 ? 13.574 -6.896  8.827   0.50 13.02 ?  153 LEU   A O    1 
ATOM   3384 C  CB   A LEU   A 1 153 ? 15.135 -8.695  6.446   0.50 11.98 ?  153 LEU   A CB   1 
ATOM   3385 C  CB   B LEU   A 1 153 ? 15.034 -8.353  6.582   0.50 12.24 ?  153 LEU   A CB   1 
ATOM   3386 C  CG   A LEU   A 1 153 ? 16.079 -9.662  5.727   0.50 12.01 ?  153 LEU   A CG   1 
ATOM   3387 C  CG   B LEU   A 1 153 ? 15.944 -9.410  5.960   0.50 12.21 ?  153 LEU   A CG   1 
ATOM   3388 C  CD1  A LEU   A 1 153 ? 15.293 -10.572 4.784   0.50 12.45 ?  153 LEU   A CD1  1 
ATOM   3389 C  CD1  B LEU   A 1 153 ? 15.147 -10.241 4.974   0.50 12.49 ?  153 LEU   A CD1  1 
ATOM   3390 C  CD2  A LEU   A 1 153 ? 17.136 -8.889  4.956   0.50 12.48 ?  153 LEU   A CD2  1 
ATOM   3391 C  CD2  B LEU   A 1 153 ? 17.145 -8.756  5.285   0.50 12.99 ?  153 LEU   A CD2  1 
ATOM   3392 H  H    A LEU   A 1 153 ? 15.407 -9.395  8.815   0.50 14.64 ?  153 LEU   A H    1 
ATOM   3393 H  H    B LEU   A 1 153 ? 15.286 -9.248  8.915   0.50 15.17 ?  153 LEU   A H    1 
ATOM   3394 H  HA   A LEU   A 1 153 ? 16.513 -7.446  7.326   0.50 14.63 ?  153 LEU   A HA   1 
ATOM   3395 H  HA   B LEU   A 1 153 ? 16.444 -7.225  7.562   0.50 14.78 ?  153 LEU   A HA   1 
ATOM   3396 H  HB2  A LEU   A 1 153 ? 14.393 -9.226  6.779   0.50 14.41 ?  153 LEU   A HB2  1 
ATOM   3397 H  HB2  B LEU   A 1 153 ? 14.208 -8.786  6.843   0.50 14.72 ?  153 LEU   A HB2  1 
ATOM   3398 H  HB3  A LEU   A 1 153 ? 14.805 -8.081  5.772   0.50 14.41 ?  153 LEU   A HB3  1 
ATOM   3399 H  HB3  B LEU   A 1 153 ? 14.854 -7.680  5.909   0.50 14.72 ?  153 LEU   A HB3  1 
ATOM   3400 H  HG   A LEU   A 1 153 ? 16.526 -10.225 6.381   0.50 14.45 ?  153 LEU   A HG   1 
ATOM   3401 H  HG   B LEU   A 1 153 ? 16.272 -9.997  6.659   0.50 14.68 ?  153 LEU   A HG   1 
ATOM   3402 H  HD11 A LEU   A 1 153 ? 15.835 -11.346 4.564   0.50 14.97 ?  153 LEU   A HD11 1 
ATOM   3403 H  HD11 B LEU   A 1 153 ? 15.731 -10.906 4.581   0.50 15.02 ?  153 LEU   A HD11 1 
ATOM   3404 H  HD12 A LEU   A 1 153 ? 14.479 -10.856 5.224   0.50 14.97 ?  153 LEU   A HD12 1 
ATOM   3405 H  HD12 B LEU   A 1 153 ? 14.419 -10.675 5.446   0.50 15.02 ?  153 LEU   A HD12 1 
ATOM   3406 H  HD13 A LEU   A 1 153 ? 15.079 -10.077 3.977   0.50 14.97 ?  153 LEU   A HD13 1 
ATOM   3407 H  HD13 B LEU   A 1 153 ? 14.794 -9.658  4.285   0.50 15.02 ?  153 LEU   A HD13 1 
ATOM   3408 H  HD21 A LEU   A 1 153 ? 17.759 -9.517  4.561   0.50 15.01 ?  153 LEU   A HD21 1 
ATOM   3409 H  HD21 B LEU   A 1 153 ? 17.673 -9.445  4.852   0.50 15.62 ?  153 LEU   A HD21 1 
ATOM   3410 H  HD22 A LEU   A 1 153 ? 16.699 -8.373  4.262   0.50 15.01 ?  153 LEU   A HD22 1 
ATOM   3411 H  HD22 B LEU   A 1 153 ? 16.828 -8.118  4.628   0.50 15.62 ?  153 LEU   A HD22 1 
ATOM   3412 H  HD23 A LEU   A 1 153 ? 17.601 -8.303  5.569   0.50 15.01 ?  153 LEU   A HD23 1 
ATOM   3413 H  HD23 B LEU   A 1 153 ? 17.679 -8.304  5.957   0.50 15.62 ?  153 LEU   A HD23 1 
ATOM   3414 N  N    A ALA   A 1 154 ? 15.043 -5.538  7.720   0.50 11.76 ?  154 ALA   A N    1 
ATOM   3415 N  N    B ALA   A 1 154 ? 15.036 -5.319  8.115   0.50 12.11 ?  154 ALA   A N    1 
ATOM   3416 C  CA   A ALA   A 1 154 ? 14.190 -4.390  7.990   0.50 12.69 ?  154 ALA   A CA   1 
ATOM   3417 C  CA   B ALA   A 1 154 ? 14.163 -4.173  8.335   0.50 13.19 ?  154 ALA   A CA   1 
ATOM   3418 C  C    A ALA   A 1 154 ? 13.665 -3.839  6.674   0.50 13.14 ?  154 ALA   A C    1 
ATOM   3419 C  C    B ALA   A 1 154 ? 13.734 -3.653  6.968   0.50 13.79 ?  154 ALA   A C    1 
ATOM   3420 O  O    A ALA   A 1 154 ? 14.450 -3.464  5.794   0.50 13.87 ?  154 ALA   A O    1 
ATOM   3421 O  O    B ALA   A 1 154 ? 14.584 -3.295  6.145   0.50 13.74 ?  154 ALA   A O    1 
ATOM   3422 C  CB   A ALA   A 1 154 ? 14.966 -3.301  8.727   0.50 13.30 ?  154 ALA   A CB   1 
ATOM   3423 C  CB   B ALA   A 1 154 ? 14.891 -3.074  9.113   0.50 13.18 ?  154 ALA   A CB   1 
ATOM   3424 H  H    A ALA   A 1 154 ? 15.804 -5.334  7.384   0.50 14.15 ?  154 ALA   A H    1 
ATOM   3425 H  H    B ALA   A 1 154 ? 15.828 -5.090  7.856   0.50 14.56 ?  154 ALA   A H    1 
ATOM   3426 H  HA   A ALA   A 1 154 ? 13.437 -4.666  8.535   0.50 15.26 ?  154 ALA   A HA   1 
ATOM   3427 H  HA   B ALA   A 1 154 ? 13.378 -4.435  8.839   0.50 15.87 ?  154 ALA   A HA   1 
ATOM   3428 H  HB1  A ALA   A 1 154 ? 14.373 -2.553  8.888   0.50 15.99 ?  154 ALA   A HB1  1 
ATOM   3429 H  HB1  B ALA   A 1 154 ? 14.289 -2.322  9.250   0.50 15.85 ?  154 ALA   A HB1  1 
ATOM   3430 H  HB2  A ALA   A 1 154 ? 15.289 -3.660  9.566   0.50 15.99 ?  154 ALA   A HB2  1 
ATOM   3431 H  HB2  B ALA   A 1 154 ? 15.178 -3.423  9.972   0.50 15.85 ?  154 ALA   A HB2  1 
ATOM   3432 H  HB3  A ALA   A 1 154 ? 15.713 -3.022  8.174   0.50 15.99 ?  154 ALA   A HB3  1 
ATOM   3433 H  HB3  B ALA   A 1 154 ? 15.666 -2.780  8.603   0.50 15.85 ?  154 ALA   A HB3  1 
ATOM   3434 N  N    A VAL   A 1 155 ? 12.343 -3.772  6.556   0.50 13.82 ?  155 VAL   A N    1 
ATOM   3435 N  N    B VAL   A 1 155 ? 12.423 -3.617  6.726   0.50 15.00 ?  155 VAL   A N    1 
ATOM   3436 C  CA   A VAL   A 1 155 ? 11.661 -3.250  5.378   0.50 14.48 ?  155 VAL   A CA   1 
ATOM   3437 C  CA   B VAL   A 1 155 ? 11.856 -3.193  5.445   0.50 16.44 ?  155 VAL   A CA   1 
ATOM   3438 C  C    A VAL   A 1 155 ? 10.949 -1.965  5.774   0.50 14.86 ?  155 VAL   A C    1 
ATOM   3439 C  C    B VAL   A 1 155 ? 10.973 -1.978  5.699   0.50 18.32 ?  155 VAL   A C    1 
ATOM   3440 O  O    A VAL   A 1 155 ? 10.054 -1.982  6.629   0.50 15.05 ?  155 VAL   A O    1 
ATOM   3441 O  O    B VAL   A 1 155 ? 9.875  -2.106  6.257   0.50 18.36 ?  155 VAL   A O    1 
ATOM   3442 C  CB   A VAL   A 1 155 ? 10.674 -4.274  4.799   0.50 15.10 ?  155 VAL   A CB   1 
ATOM   3443 C  CB   B VAL   A 1 155 ? 11.066 -4.316  4.756   0.50 16.23 ?  155 VAL   A CB   1 
ATOM   3444 C  CG1  A VAL   A 1 155 ? 9.934  -3.672  3.619   0.50 16.01 ?  155 VAL   A CG1  1 
ATOM   3445 C  CG1  B VAL   A 1 155 ? 10.351 -3.789  3.512   0.50 16.56 ?  155 VAL   A CG1  1 
ATOM   3446 C  CG2  A VAL   A 1 155 ? 11.411 -5.538  4.386   0.50 15.26 ?  155 VAL   A CG2  1 
ATOM   3447 C  CG2  B VAL   A 1 155 ? 11.992 -5.461  4.385   0.50 16.09 ?  155 VAL   A CG2  1 
ATOM   3448 H  H    A VAL   A 1 155 ? 11.800 -4.043  7.171   0.50 16.61 ?  155 VAL   A H    1 
ATOM   3449 H  H    B VAL   A 1 155 ? 11.827 -3.840  7.308   0.50 18.04 ?  155 VAL   A H    1 
ATOM   3450 H  HA   A VAL   A 1 155 ? 12.312 -3.039  4.700   0.50 17.41 ?  155 VAL   A HA   1 
ATOM   3451 H  HA   B VAL   A 1 155 ? 12.573 -2.922  4.855   0.50 19.76 ?  155 VAL   A HA   1 
ATOM   3452 H  HB   A VAL   A 1 155 ? 10.018 -4.510  5.479   0.50 18.16 ?  155 VAL   A HB   1 
ATOM   3453 H  HB   B VAL   A 1 155 ? 10.396 -4.656  5.371   0.50 19.52 ?  155 VAL   A HB   1 
ATOM   3454 H  HG11 A VAL   A 1 155 ? 9.474  -4.379  3.144   0.50 19.25 ?  155 VAL   A HG11 1 
ATOM   3455 H  HG11 B VAL   A 1 155 ? 10.068 -4.543  2.970   0.50 19.90 ?  155 VAL   A HG11 1 
ATOM   3456 H  HG12 A VAL   A 1 155 ? 9.293  -3.020  3.944   0.50 19.25 ?  155 VAL   A HG12 1 
ATOM   3457 H  HG12 B VAL   A 1 155 ? 9.575  -3.272  3.783   0.50 19.90 ?  155 VAL   A HG12 1 
ATOM   3458 H  HG13 A VAL   A 1 155 ? 10.578 -3.243  3.034   0.50 19.25 ?  155 VAL   A HG13 1 
ATOM   3459 H  HG13 B VAL   A 1 155 ? 10.962 -3.232  3.006   0.50 19.90 ?  155 VAL   A HG13 1 
ATOM   3460 H  HG21 A VAL   A 1 155 ? 10.779 -6.152  3.981   0.50 18.34 ?  155 VAL   A HG21 1 
ATOM   3461 H  HG21 B VAL   A 1 155 ? 11.474 -6.156  3.950   0.50 19.34 ?  155 VAL   A HG21 1 
ATOM   3462 H  HG22 A VAL   A 1 155 ? 12.101 -5.303  3.748   0.50 18.34 ?  155 VAL   A HG22 1 
ATOM   3463 H  HG22 B VAL   A 1 155 ? 12.675 -5.129  3.781   0.50 19.34 ?  155 VAL   A HG22 1 
ATOM   3464 H  HG23 A VAL   A 1 155 ? 11.809 -5.943  5.173   0.50 18.34 ?  155 VAL   A HG23 1 
ATOM   3465 H  HG23 B VAL   A 1 155 ? 12.403 -5.809  5.191   0.50 19.34 ?  155 VAL   A HG23 1 
ATOM   3466 N  N    A PHE   A 1 156 ? 11.323 -0.857  5.131   0.50 15.51 ?  156 PHE   A N    1 
ATOM   3467 N  N    B PHE   A 1 156 ? 11.435 -0.805  5.264   0.50 20.49 ?  156 PHE   A N    1 
ATOM   3468 C  CA   A PHE   A 1 156 ? 10.795 0.449   5.522   0.50 16.81 ?  156 PHE   A CA   1 
ATOM   3469 C  CA   B PHE   A 1 156 ? 10.781 0.471   5.565   0.50 23.09 ?  156 PHE   A CA   1 
ATOM   3470 C  C    A PHE   A 1 156 ? 9.328  0.601   5.139   0.50 17.08 ?  156 PHE   A C    1 
ATOM   3471 C  C    B PHE   A 1 156 ? 9.691  0.788   4.534   0.50 24.37 ?  156 PHE   A C    1 
ATOM   3472 O  O    A PHE   A 1 156 ? 8.522  1.113   5.927   0.50 17.68 ?  156 PHE   A O    1 
ATOM   3473 O  O    B PHE   A 1 156 ? 9.705  1.819   3.860   0.50 24.88 ?  156 PHE   A O    1 
ATOM   3474 C  CB   A PHE   A 1 156 ? 11.634 1.547   4.866   0.50 17.67 ?  156 PHE   A CB   1 
ATOM   3475 C  CB   B PHE   A 1 156 ? 11.833 1.577   5.629   0.50 24.27 ?  156 PHE   A CB   1 
ATOM   3476 C  CG   A PHE   A 1 156 ? 11.158 2.941   5.169   0.50 18.90 ?  156 PHE   A CG   1 
ATOM   3477 C  CG   B PHE   A 1 156 ? 11.336 2.882   6.194   0.50 25.63 ?  156 PHE   A CG   1 
ATOM   3478 C  CD1  A PHE   A 1 156 ? 11.092 3.387   6.478   0.50 19.55 ?  156 PHE   A CD1  1 
ATOM   3479 C  CD1  B PHE   A 1 156 ? 10.234 2.931   7.031   0.50 26.29 ?  156 PHE   A CD1  1 
ATOM   3480 C  CD2  A PHE   A 1 156 ? 10.788 3.804   4.148   0.50 20.06 ?  156 PHE   A CD2  1 
ATOM   3481 C  CD2  B PHE   A 1 156 ? 11.989 4.065   5.885   0.50 26.16 ?  156 PHE   A CD2  1 
ATOM   3482 C  CE1  A PHE   A 1 156 ? 10.657 4.664   6.767   0.50 20.51 ?  156 PHE   A CE1  1 
ATOM   3483 C  CE1  B PHE   A 1 156 ? 9.791  4.133   7.547   0.50 26.59 ?  156 PHE   A CE1  1 
ATOM   3484 C  CE2  A PHE   A 1 156 ? 10.352 5.086   4.430   0.50 20.99 ?  156 PHE   A CE2  1 
ATOM   3485 C  CE2  B PHE   A 1 156 ? 11.550 5.271   6.396   0.50 26.50 ?  156 PHE   A CE2  1 
ATOM   3486 C  CZ   A PHE   A 1 156 ? 10.291 5.518   5.741   0.50 21.04 ?  156 PHE   A CZ   1 
ATOM   3487 C  CZ   B PHE   A 1 156 ? 10.449 5.305   7.228   0.50 26.59 ?  156 PHE   A CZ   1 
ATOM   3488 H  H    A PHE   A 1 156 ? 11.862 -0.844  4.464   0.50 18.65 ?  156 PHE   A H    1 
ATOM   3489 H  H    B PHE   A 1 156 ? 12.144 -0.718  4.786   0.50 24.63 ?  156 PHE   A H    1 
ATOM   3490 H  HA   A PHE   A 1 156 ? 10.870 0.547   6.481   0.50 20.21 ?  156 PHE   A HA   1 
ATOM   3491 H  HA   B PHE   A 1 156 ? 10.357 0.395   6.430   0.50 27.74 ?  156 PHE   A HA   1 
ATOM   3492 H  HB2  A PHE   A 1 156 ? 12.551 1.469   5.178   0.50 21.24 ?  156 PHE   A HB2  1 
ATOM   3493 H  HB2  B PHE   A 1 156 ? 12.566 1.278   6.190   0.50 29.15 ?  156 PHE   A HB2  1 
ATOM   3494 H  HB3  A PHE   A 1 156 ? 11.608 1.427   3.902   0.50 21.24 ?  156 PHE   A HB3  1 
ATOM   3495 H  HB3  B PHE   A 1 156 ? 12.161 1.755   4.733   0.50 29.15 ?  156 PHE   A HB3  1 
ATOM   3496 H  HD1  A PHE   A 1 156 ? 11.341 2.816   7.171   0.50 23.49 ?  156 PHE   A HD1  1 
ATOM   3497 H  HD1  B PHE   A 1 156 ? 9.789  2.144   7.251   0.50 31.58 ?  156 PHE   A HD1  1 
ATOM   3498 H  HD2  A PHE   A 1 156 ? 10.830 3.512   3.265   0.50 24.10 ?  156 PHE   A HD2  1 
ATOM   3499 H  HD2  B PHE   A 1 156 ? 12.732 4.049   5.325   0.50 31.42 ?  156 PHE   A HD2  1 
ATOM   3500 H  HE1  A PHE   A 1 156 ? 10.617 4.955   7.649   0.50 24.64 ?  156 PHE   A HE1  1 
ATOM   3501 H  HE1  B PHE   A 1 156 ? 9.050  4.152   8.107   0.50 31.94 ?  156 PHE   A HE1  1 
ATOM   3502 H  HE2  A PHE   A 1 156 ? 10.106 5.654   3.739   0.50 25.22 ?  156 PHE   A HE2  1 
ATOM   3503 H  HE2  B PHE   A 1 156 ? 11.995 6.061   6.180   0.50 31.83 ?  156 PHE   A HE2  1 
ATOM   3504 H  HZ   A PHE   A 1 156 ? 9.998  6.378   5.934   0.50 25.28 ?  156 PHE   A HZ   1 
ATOM   3505 H  HZ   B PHE   A 1 156 ? 10.150 6.115   7.574   0.50 31.94 ?  156 PHE   A HZ   1 
ATOM   3506 N  N    A ASP   A 1 157 ? 8.973  0.181   3.930   0.50 17.91 ?  157 ASP   A N    1 
ATOM   3507 N  N    B ASP   A 1 157 ? 8.722  -0.120  4.433   0.50 25.19 ?  157 ASP   A N    1 
ATOM   3508 C  CA   A ASP   A 1 157 ? 7.640  0.404   3.384   0.50 19.29 ?  157 ASP   A CA   1 
ATOM   3509 C  CA   B ASP   A 1 157 ? 7.613  0.041   3.493   0.50 26.18 ?  157 ASP   A CA   1 
ATOM   3510 C  C    A ASP   A 1 157 ? 6.680  -0.673  3.891   0.50 19.42 ?  157 ASP   A C    1 
ATOM   3511 C  C    B ASP   A 1 157 ? 6.505  -0.925  3.882   0.50 26.26 ?  157 ASP   A C    1 
ATOM   3512 O  O    A ASP   A 1 157 ? 6.871  -1.863  3.611   0.50 18.49 ?  157 ASP   A O    1 
ATOM   3513 O  O    B ASP   A 1 157 ? 6.694  -2.144  3.810   0.50 26.17 ?  157 ASP   A O    1 
ATOM   3514 C  CB   A ASP   A 1 157 ? 7.736  0.358   1.863   0.50 20.62 ?  157 ASP   A CB   1 
ATOM   3515 C  CB   B ASP   A 1 157 ? 8.078  -0.220  2.060   0.50 27.01 ?  157 ASP   A CB   1 
ATOM   3516 C  CG   A ASP   A 1 157 ? 6.504  0.896   1.184   0.50 22.29 ?  157 ASP   A CG   1 
ATOM   3517 C  CG   B ASP   A 1 157 ? 7.016  0.130   1.027   0.50 27.96 ?  157 ASP   A CG   1 
ATOM   3518 O  OD1  A ASP   A 1 157 ? 6.317  2.127   1.185   0.50 23.92 ?  157 ASP   A OD1  1 
ATOM   3519 O  OD1  B ASP   A 1 157 ? 5.815  0.113   1.371   0.50 27.84 ?  157 ASP   A OD1  1 
ATOM   3520 O  OD2  A ASP   A 1 157 ? 5.724  0.082   0.646   0.50 22.66 -1 157 ASP   A OD2  1 
ATOM   3521 O  OD2  B ASP   A 1 157 ? 7.383  0.414   -0.132  0.50 28.78 -1 157 ASP   A OD2  1 
ATOM   3522 H  H    A ASP   A 1 157 ? 9.501  -0.235  3.392   0.50 21.52 ?  157 ASP   A H    1 
ATOM   3523 H  H    B ASP   A 1 157 ? 8.681  -0.837  4.898   0.50 30.27 ?  157 ASP   A H    1 
ATOM   3524 H  HA   A ASP   A 1 157 ? 7.313  1.281   3.654   0.50 23.18 ?  157 ASP   A HA   1 
ATOM   3525 H  HA   B ASP   A 1 157 ? 7.264  0.941   3.545   0.50 31.45 ?  157 ASP   A HA   1 
ATOM   3526 H  HB2  A ASP   A 1 157 ? 8.508  0.872   1.574   0.50 24.77 ?  157 ASP   A HB2  1 
ATOM   3527 H  HB2  B ASP   A 1 157 ? 8.870  0.314   1.889   0.50 32.45 ?  157 ASP   A HB2  1 
ATOM   3528 H  HB3  A ASP   A 1 157 ? 7.825  -0.558  1.577   0.50 24.77 ?  157 ASP   A HB3  1 
ATOM   3529 H  HB3  B ASP   A 1 157 ? 8.290  -1.160  1.960   0.50 32.45 ?  157 ASP   A HB3  1 
ATOM   3530 N  N    A LYS   A 1 158 ? 5.643  -0.256  4.628   0.50 20.62 ?  158 LYS   A N    1 
ATOM   3531 N  N    B LYS   A 1 158 ? 5.352  -0.383  4.282   0.50 26.40 ?  158 LYS   A N    1 
ATOM   3532 C  CA   A LYS   A 1 158 ? 4.712  -1.218  5.219   0.50 21.12 ?  158 LYS   A CA   1 
ATOM   3533 C  CA   B LYS   A 1 158 ? 4.228  -1.215  4.698   0.50 26.68 ?  158 LYS   A CA   1 
ATOM   3534 C  C    A LYS   A 1 158 ? 3.957  -1.992  4.146   0.50 21.00 ?  158 LYS   A C    1 
ATOM   3535 C  C    B LYS   A 1 158 ? 3.737  -2.095  3.552   0.50 25.86 ?  158 LYS   A C    1 
ATOM   3536 O  O    A LYS   A 1 158 ? 3.740  -3.203  4.279   0.50 21.21 ?  158 LYS   A O    1 
ATOM   3537 O  O    B LYS   A 1 158 ? 3.678  -3.325  3.670   0.50 25.42 ?  158 LYS   A O    1 
ATOM   3538 C  CB   A LYS   A 1 158 ? 3.736  -0.502  6.158   0.50 21.57 ?  158 LYS   A CB   1 
ATOM   3539 C  CB   B LYS   A 1 158 ? 3.095  -0.320  5.203   0.50 27.86 ?  158 LYS   A CB   1 
ATOM   3540 C  CG   A LYS   A 1 158 ? 2.508  -1.326  6.569   0.50 22.28 ?  158 LYS   A CG   1 
ATOM   3541 C  CG   B LYS   A 1 158 ? 2.719  -0.521  6.670   0.50 29.20 ?  158 LYS   A CG   1 
ATOM   3542 C  CD   A LYS   A 1 158 ? 2.876  -2.577  7.366   0.50 22.54 ?  158 LYS   A CD   1 
ATOM   3543 C  CD   B LYS   A 1 158 ? 1.215  -0.690  6.845   0.50 30.11 ?  158 LYS   A CD   1 
ATOM   3544 C  CE   A LYS   A 1 158 ? 1.624  -3.301  7.859   0.50 22.90 ?  158 LYS   A CE   1 
ATOM   3545 C  CE   B LYS   A 1 158 ? 0.433  0.269   5.953   0.50 30.71 ?  158 LYS   A CE   1 
ATOM   3546 N  NZ   A LYS   A 1 158 ? 1.929  -4.622  8.477   0.50 22.99 ?  158 LYS   A NZ   1 
ATOM   3547 N  NZ   B LYS   A 1 158 ? -0.761 0.823   6.626   0.50 31.00 ?  158 LYS   A NZ   1 
ATOM   3548 H  H    A LYS   A 1 158 ? 5.471  0.568   4.798   0.50 24.77 ?  158 LYS   A H    1 
ATOM   3549 H  H    B LYS   A 1 158 ? 5.198  0.461   4.330   0.50 31.71 ?  158 LYS   A H    1 
ATOM   3550 H  HA   A LYS   A 1 158 ? 5.221  -1.855  5.746   0.50 25.38 ?  158 LYS   A HA   1 
ATOM   3551 H  HA   B LYS   A 1 158 ? 4.500  -1.791  5.426   0.50 32.05 ?  158 LYS   A HA   1 
ATOM   3552 H  HB2  A LYS   A 1 158 ? 4.215  -0.259  6.969   0.50 25.91 ?  158 LYS   A HB2  1 
ATOM   3553 H  HB2  B LYS   A 1 158 ? 3.339  0.617   5.101   0.50 33.47 ?  158 LYS   A HB2  1 
ATOM   3554 H  HB3  A LYS   A 1 158 ? 3.423  0.303   5.717   0.50 25.91 ?  158 LYS   A HB3  1 
ATOM   3555 H  HB3  B LYS   A 1 158 ? 2.318  -0.511  4.658   0.50 33.47 ?  158 LYS   A HB3  1 
ATOM   3556 H  HG2  A LYS   A 1 158 ? 1.946  -0.773  7.127   0.50 26.77 ?  158 LYS   A HG2  1 
ATOM   3557 H  HG2  B LYS   A 1 158 ? 3.154  -1.317  7.013   0.50 35.07 ?  158 LYS   A HG2  1 
ATOM   3558 H  HG3  A LYS   A 1 158 ? 2.019  -1.598  5.777   0.50 26.77 ?  158 LYS   A HG3  1 
ATOM   3559 H  HG3  B LYS   A 1 158 ? 2.996  0.256   7.186   0.50 35.07 ?  158 LYS   A HG3  1 
ATOM   3560 H  HD2  A LYS   A 1 158 ? 3.380  -3.182  6.800   0.50 27.08 ?  158 LYS   A HD2  1 
ATOM   3561 H  HD2  B LYS   A 1 158 ? 0.970  -1.601  6.612   0.50 36.17 ?  158 LYS   A HD2  1 
ATOM   3562 H  HD3  A LYS   A 1 158 ? 3.406  -2.318  8.138   0.50 27.08 ?  158 LYS   A HD3  1 
ATOM   3563 H  HD3  B LYS   A 1 158 ? 0.977  -0.506  7.768   0.50 36.17 ?  158 LYS   A HD3  1 
ATOM   3564 H  HE2  A LYS   A 1 158 ? 1.186  -2.749  8.525   0.50 27.51 ?  158 LYS   A HE2  1 
ATOM   3565 H  HE2  B LYS   A 1 158 ? 1.003  1.014   5.705   0.50 36.89 ?  158 LYS   A HE2  1 
ATOM   3566 H  HE3  A LYS   A 1 158 ? 1.031  -3.447  7.106   0.50 27.51 ?  158 LYS   A HE3  1 
ATOM   3567 H  HE3  B LYS   A 1 158 ? 0.149  -0.212  5.154   0.50 36.89 ?  158 LYS   A HE3  1 
ATOM   3568 H  HZ1  A LYS   A 1 158 ? 1.177  -5.010  8.749   0.50 27.62 ?  158 LYS   A HZ1  1 
ATOM   3569 H  HZ1  B LYS   A 1 158 ? -1.186 1.375   6.074   0.50 37.24 ?  158 LYS   A HZ1  1 
ATOM   3570 H  HZ2  A LYS   A 1 158 ? 2.329  -5.151  7.882   0.50 27.62 ?  158 LYS   A HZ2  1 
ATOM   3571 H  HZ2  B LYS   A 1 158 ? -1.308 0.166   6.863   0.50 37.24 ?  158 LYS   A HZ2  1 
ATOM   3572 H  HZ3  A LYS   A 1 158 ? 2.469  -4.514  9.176   0.50 27.62 ?  158 LYS   A HZ3  1 
ATOM   3573 H  HZ3  B LYS   A 1 158 ? -0.513 1.273   7.353   0.50 37.24 ?  158 LYS   A HZ3  1 
ATOM   3574 N  N    A ASN   A 1 159 ? 3.520  -1.307  3.089   0.50 21.52 ?  159 ASN   A N    1 
ATOM   3575 N  N    B ASN   A 1 159 ? 3.357  -1.469  2.434   0.50 25.89 ?  159 ASN   A N    1 
ATOM   3576 C  CA   A ASN   A 1 159 ? 2.835  -2.004  2.007   0.50 22.02 ?  159 ASN   A CA   1 
ATOM   3577 C  CA   B ASN   A 1 159 ? 2.837  -2.216  1.292   0.50 25.94 ?  159 ASN   A CA   1 
ATOM   3578 C  C    A ASN   A 1 159 ? 3.736  -3.068  1.391   0.50 21.07 ?  159 ASN   A C    1 
ATOM   3579 C  C    B ASN   A 1 159 ? 3.801  -3.315  0.871   0.50 24.32 ?  159 ASN   A C    1 
ATOM   3580 O  O    A ASN   A 1 159 ? 3.311  -4.208  1.172   0.50 20.41 ?  159 ASN   A O    1 
ATOM   3581 O  O    B ASN   A 1 159 ? 3.381  -4.421  0.509   0.50 24.19 ?  159 ASN   A O    1 
ATOM   3582 C  CB   A ASN   A 1 159 ? 2.353  -0.998  0.960   0.50 23.43 ?  159 ASN   A CB   1 
ATOM   3583 C  CB   B ASN   A 1 159 ? 2.584  -1.252  0.129   0.50 27.68 ?  159 ASN   A CB   1 
ATOM   3584 C  CG   A ASN   A 1 159 ? 1.173  -0.179  1.444   0.50 25.13 ?  159 ASN   A CG   1 
ATOM   3585 C  CG   B ASN   A 1 159 ? 1.619  -0.136  0.494   0.50 29.44 ?  159 ASN   A CG   1 
ATOM   3586 O  OD1  A ASN   A 1 159 ? 0.318  -0.683  2.168   0.50 25.78 ?  159 ASN   A OD1  1 
ATOM   3587 O  OD1  B ASN   A 1 159 ? 0.578  -0.376  1.109   0.50 30.28 ?  159 ASN   A OD1  1 
ATOM   3588 N  ND2  A ASN   A 1 159 ? 1.120  1.090   1.048   0.50 25.81 ?  159 ASN   A ND2  1 
ATOM   3589 N  ND2  B ASN   A 1 159 ? 1.964  1.094   0.119   0.50 30.17 ?  159 ASN   A ND2  1 
ATOM   3590 H  H    A ASN   A 1 159 ? 3.611  -0.459  2.976   0.50 25.86 ?  159 ASN   A H    1 
ATOM   3591 H  H    B ASN   A 1 159 ? 3.395  -0.621  2.315   0.50 31.10 ?  159 ASN   A H    1 
ATOM   3592 H  HA   A ASN   A 1 159 ? 2.055  -2.452  2.368   0.50 26.46 ?  159 ASN   A HA   1 
ATOM   3593 H  HA   B ASN   A 1 159 ? 1.992  -2.629  1.527   0.50 31.17 ?  159 ASN   A HA   1 
ATOM   3594 H  HB2  A ASN   A 1 159 ? 3.070  -0.384  0.749   0.50 28.15 ?  159 ASN   A HB2  1 
ATOM   3595 H  HB2  B ASN   A 1 159 ? 3.425  -0.845  -0.137  0.50 33.25 ?  159 ASN   A HB2  1 
ATOM   3596 H  HB3  A ASN   A 1 159 ? 2.074  -1.476  0.163   0.50 28.15 ?  159 ASN   A HB3  1 
ATOM   3597 H  HB3  B ASN   A 1 159 ? 2.204  -1.742  -0.617  0.50 33.25 ?  159 ASN   A HB3  1 
ATOM   3598 H  HD21 A ASN   A 1 159 ? 0.468  1.594   1.297   0.50 31.01 ?  159 ASN   A HD21 1 
ATOM   3599 H  HD21 B ASN   A 1 159 ? 1.450  1.760   0.304   0.50 36.24 ?  159 ASN   A HD21 1 
ATOM   3600 H  HD22 A ASN   A 1 159 ? 1.740  1.407   0.546   0.50 31.01 ?  159 ASN   A HD22 1 
ATOM   3601 H  HD22 B ASN   A 1 159 ? 2.699  1.227   -0.308  0.50 36.24 ?  159 ASN   A HD22 1 
ATOM   3602 N  N    A LEU   A 1 160 ? 4.996  -2.717  1.119   0.50 20.42 ?  160 LEU   A N    1 
ATOM   3603 N  N    B LEU   A 1 160 ? 5.102  -3.031  0.928   0.50 23.05 ?  160 LEU   A N    1 
ATOM   3604 C  CA   A LEU   A 1 160 ? 5.928  -3.704  0.584   0.50 19.89 ?  160 LEU   A CA   1 
ATOM   3605 C  CA   B LEU   A 1 160 ? 6.093  -4.000  0.479   0.50 21.78 ?  160 LEU   A CA   1 
ATOM   3606 C  C    A LEU   A 1 160 ? 6.170  -4.826  1.583   0.50 18.86 ?  160 LEU   A C    1 
ATOM   3607 C  C    B LEU   A 1 160 ? 6.218  -5.155  1.463   0.50 20.71 ?  160 LEU   A C    1 
ATOM   3608 O  O    A LEU   A 1 160 ? 6.265  -5.997  1.199   0.50 19.42 ?  160 LEU   A O    1 
ATOM   3609 O  O    B LEU   A 1 160 ? 6.191  -6.327  1.069   0.50 21.02 ?  160 LEU   A O    1 
ATOM   3610 C  CB   A LEU   A 1 160 ? 7.248  -3.039  0.198   0.50 19.80 ?  160 LEU   A CB   1 
ATOM   3611 C  CB   B LEU   A 1 160 ? 7.445  -3.309  0.306   0.50 21.82 ?  160 LEU   A CB   1 
ATOM   3612 C  CG   A LEU   A 1 160 ? 8.381  -4.008  -0.149  0.50 19.87 ?  160 LEU   A CG   1 
ATOM   3613 C  CG   B LEU   A 1 160 ? 8.449  -4.195  -0.417  0.50 22.13 ?  160 LEU   A CG   1 
ATOM   3614 C  CD1  A LEU   A 1 160 ? 7.997  -4.898  -1.322  0.50 19.64 ?  160 LEU   A CD1  1 
ATOM   3615 C  CD1  B LEU   A 1 160 ? 7.891  -4.487  -1.794  0.50 22.61 ?  160 LEU   A CD1  1 
ATOM   3616 C  CD2  A LEU   A 1 160 ? 9.655  -3.244  -0.443  0.50 19.99 ?  160 LEU   A CD2  1 
ATOM   3617 C  CD2  B LEU   A 1 160 ? 9.807  -3.526  -0.495  0.50 21.92 ?  160 LEU   A CD2  1 
ATOM   3618 H  H    A LEU   A 1 160 ? 5.326  -1.929  1.238   0.50 24.53 ?  160 LEU   A H    1 
ATOM   3619 H  H    B LEU   A 1 160 ? 5.432  -2.294  1.220   0.50 27.70 ?  160 LEU   A H    1 
ATOM   3620 H  HA   A LEU   A 1 160 ? 5.544  -4.092  -0.215  0.50 23.90 ?  160 LEU   A HA   1 
ATOM   3621 H  HA   B LEU   A 1 160 ? 5.805  -4.361  -0.372  0.50 26.17 ?  160 LEU   A HA   1 
ATOM   3622 H  HB2  A LEU   A 1 160 ? 7.097  -2.464  -0.572  0.50 23.79 ?  160 LEU   A HB2  1 
ATOM   3623 H  HB2  B LEU   A 1 160 ? 7.334  -2.490  -0.207  0.50 26.22 ?  160 LEU   A HB2  1 
ATOM   3624 H  HB3  A LEU   A 1 160 ? 7.548  -2.508  0.948   0.50 23.79 ?  160 LEU   A HB3  1 
ATOM   3625 H  HB3  B LEU   A 1 160 ? 7.809  -3.104  1.183   0.50 26.22 ?  160 LEU   A HB3  1 
ATOM   3626 H  HG   A LEU   A 1 160 ? 8.555  -4.577  0.613   0.50 23.87 ?  160 LEU   A HG   1 
ATOM   3627 H  HG   B LEU   A 1 160 ? 8.547  -5.034  0.063   0.50 26.59 ?  160 LEU   A HG   1 
ATOM   3628 H  HD11 A LEU   A 1 160 ? 8.760  -5.441  -1.566  0.50 23.60 ?  160 LEU   A HD11 1 
ATOM   3629 H  HD11 B LEU   A 1 160 ? 8.568  -4.303  -2.445  0.50 27.17 ?  160 LEU   A HD11 1 
ATOM   3630 H  HD12 A LEU   A 1 160 ? 7.255  -5.465  -1.060  0.50 23.60 ?  160 LEU   A HD12 1 
ATOM   3631 H  HD12 B LEU   A 1 160 ? 7.619  -5.417  -1.835  0.50 27.17 ?  160 LEU   A HD12 1 
ATOM   3632 H  HD13 A LEU   A 1 160 ? 7.735  -4.337  -2.071  0.50 23.60 ?  160 LEU   A HD13 1 
ATOM   3633 H  HD13 B LEU   A 1 160 ? 7.129  -3.909  -1.960  0.50 27.17 ?  160 LEU   A HD13 1 
ATOM   3634 H  HD21 A LEU   A 1 160 ? 10.358 -3.876  -0.659  0.50 24.02 ?  160 LEU   A HD21 1 
ATOM   3635 H  HD21 B LEU   A 1 160 ? 10.452 -4.160  -0.842  0.50 26.34 ?  160 LEU   A HD21 1 
ATOM   3636 H  HD22 A LEU   A 1 160 ? 9.503  -2.649  -1.194  0.50 24.02 ?  160 LEU   A HD22 1 
ATOM   3637 H  HD22 B LEU   A 1 160 ? 9.746  -2.758  -1.085  0.50 26.34 ?  160 LEU   A HD22 1 
ATOM   3638 H  HD23 A LEU   A 1 160 ? 9.904  -2.728  0.341   0.50 24.02 ?  160 LEU   A HD23 1 
ATOM   3639 H  HD23 B LEU   A 1 160 ? 10.070 -3.240  0.394   0.50 26.34 ?  160 LEU   A HD23 1 
ATOM   3640 N  N    A TYR   A 1 161 ? 6.277  -4.489  2.870   0.50 18.07 ?  161 TYR   A N    1 
ATOM   3641 N  N    B TYR   A 1 161 ? 6.380  -4.839  2.748   0.50 20.33 ?  161 TYR   A N    1 
ATOM   3642 C  CA   A TYR   A 1 161 ? 6.458  -5.523  3.881   0.50 17.91 ?  161 TYR   A CA   1 
ATOM   3643 C  CA   B TYR   A 1 161 ? 6.451  -5.875  3.771   0.50 20.46 ?  161 TYR   A CA   1 
ATOM   3644 C  C    A TYR   A 1 161 ? 5.337  -6.558  3.820   0.50 18.29 ?  161 TYR   A C    1 
ATOM   3645 C  C    B TYR   A 1 161 ? 5.266  -6.829  3.654   0.50 21.06 ?  161 TYR   A C    1 
ATOM   3646 O  O    A TYR   A 1 161 ? 5.592  -7.766  3.838   0.50 18.14 ?  161 TYR   A O    1 
ATOM   3647 O  O    B TYR   A 1 161 ? 5.436  -8.053  3.638   0.50 20.88 ?  161 TYR   A O    1 
ATOM   3648 C  CB   A TYR   A 1 161 ? 6.561  -4.907  5.277   0.50 17.70 ?  161 TYR   A CB   1 
ATOM   3649 C  CB   B TYR   A 1 161 ? 6.502  -5.215  5.154   0.50 20.34 ?  161 TYR   A CB   1 
ATOM   3650 C  CG   A TYR   A 1 161 ? 6.453  -5.958  6.347   0.50 17.28 ?  161 TYR   A CG   1 
ATOM   3651 C  CG   B TYR   A 1 161 ? 6.449  -6.172  6.329   0.50 20.17 ?  161 TYR   A CG   1 
ATOM   3652 C  CD1  A TYR   A 1 161 ? 7.520  -6.804  6.616   0.50 17.09 ?  161 TYR   A CD1  1 
ATOM   3653 C  CD1  B TYR   A 1 161 ? 5.233  -6.659  6.798   0.50 20.31 ?  161 TYR   A CD1  1 
ATOM   3654 C  CD2  A TYR   A 1 161 ? 5.276  -6.128  7.066   0.50 17.08 ?  161 TYR   A CD2  1 
ATOM   3655 C  CD2  B TYR   A 1 161 ? 7.611  -6.574  6.982   0.50 19.77 ?  161 TYR   A CD2  1 
ATOM   3656 C  CE1  A TYR   A 1 161 ? 7.428  -7.783  7.579   0.50 17.00 ?  161 TYR   A CE1  1 
ATOM   3657 C  CE1  B TYR   A 1 161 ? 5.175  -7.525  7.869   0.50 20.57 ?  161 TYR   A CE1  1 
ATOM   3658 C  CE2  A TYR   A 1 161 ? 5.172  -7.106  8.035   0.50 17.13 ?  161 TYR   A CE2  1 
ATOM   3659 C  CE2  B TYR   A 1 161 ? 7.562  -7.445  8.058   0.50 19.98 ?  161 TYR   A CE2  1 
ATOM   3660 C  CZ   A TYR   A 1 161 ? 6.252  -7.933  8.285   0.50 17.69 ?  161 TYR   A CZ   1 
ATOM   3661 C  CZ   B TYR   A 1 161 ? 6.339  -7.915  8.496   0.50 20.95 ?  161 TYR   A CZ   1 
ATOM   3662 O  OH   A TYR   A 1 161 ? 6.164  -8.911  9.247   0.50 18.59 ?  161 TYR   A OH   1 
ATOM   3663 O  OH   B TYR   A 1 161 ? 6.277  -8.779  9.565   0.50 22.00 ?  161 TYR   A OH   1 
ATOM   3664 H  H    A TYR   A 1 161 ? 6.241  -3.685  3.177   0.50 21.72 ?  161 TYR   A H    1 
ATOM   3665 H  H    B TYR   A 1 161 ? 6.442  -4.038  3.045   0.50 24.42 ?  161 TYR   A H    1 
ATOM   3666 H  HA   A TYR   A 1 161 ? 7.283  -5.987  3.707   0.50 21.52 ?  161 TYR   A HA   1 
ATOM   3667 H  HA   B TYR   A 1 161 ? 7.264  -6.388  3.649   0.50 24.58 ?  161 TYR   A HA   1 
ATOM   3668 H  HB2  A TYR   A 1 161 ? 7.421  -4.464  5.369   0.50 21.28 ?  161 TYR   A HB2  1 
ATOM   3669 H  HB2  B TYR   A 1 161 ? 7.329  -4.713  5.222   0.50 24.44 ?  161 TYR   A HB2  1 
ATOM   3670 H  HB3  A TYR   A 1 161 ? 5.842  -4.264  5.405   0.50 21.28 ?  161 TYR   A HB3  1 
ATOM   3671 H  HB3  B TYR   A 1 161 ? 5.748  -4.611  5.234   0.50 24.44 ?  161 TYR   A HB3  1 
ATOM   3672 H  HD1  A TYR   A 1 161 ? 8.310  -6.708  6.138   0.50 20.54 ?  161 TYR   A HD1  1 
ATOM   3673 H  HD1  B TYR   A 1 161 ? 4.444  -6.402  6.379   0.50 24.41 ?  161 TYR   A HD1  1 
ATOM   3674 H  HD2  A TYR   A 1 161 ? 4.546  -5.571  6.901   0.50 20.53 ?  161 TYR   A HD2  1 
ATOM   3675 H  HD2  B TYR   A 1 161 ? 8.435  -6.258  6.689   0.50 23.76 ?  161 TYR   A HD2  1 
ATOM   3676 H  HE1  A TYR   A 1 161 ? 8.150  -8.347  7.748   0.50 20.44 ?  161 TYR   A HE1  1 
ATOM   3677 H  HE1  B TYR   A 1 161 ? 4.352  -7.845  8.168   0.50 24.72 ?  161 TYR   A HE1  1 
ATOM   3678 H  HE2  A TYR   A 1 161 ? 4.378  -7.211  8.515   0.50 20.59 ?  161 TYR   A HE2  1 
ATOM   3679 H  HE2  B TYR   A 1 161 ? 8.347  -7.707  8.487   0.50 24.01 ?  161 TYR   A HE2  1 
ATOM   3680 H  HH   A TYR   A 1 161 ? 6.879  -9.345  9.292   0.50 22.34 ?  161 TYR   A HH   1 
ATOM   3681 H  HH   B TYR   A 1 161 ? 7.044  -8.936  9.860   0.50 26.43 ?  161 TYR   A HH   1 
ATOM   3682 N  N    A ASP   A 1 162 ? 4.084  -6.103  3.731   0.50 19.07 ?  162 ASP   A N    1 
ATOM   3683 N  N    B ASP   A 1 162 ? 4.054  -6.275  3.554   0.50 22.22 ?  162 ASP   A N    1 
ATOM   3684 C  CA   A ASP   A 1 162 ? 2.961  -7.043  3.723   0.50 19.46 ?  162 ASP   A CA   1 
ATOM   3685 C  CA   B ASP   A 1 162 ? 2.855  -7.095  3.378   0.50 23.17 ?  162 ASP   A CA   1 
ATOM   3686 C  C    A ASP   A 1 162 ? 2.978  -7.918  2.476   0.50 19.78 ?  162 ASP   A C    1 
ATOM   3687 C  C    B ASP   A 1 162 ? 2.978  -7.998  2.156   0.50 23.27 ?  162 ASP   A C    1 
ATOM   3688 O  O    A ASP   A 1 162 ? 2.646  -9.109  2.541   0.50 20.30 ?  162 ASP   A O    1 
ATOM   3689 O  O    B ASP   A 1 162 ? 2.598  -9.175  2.199   0.50 23.28 ?  162 ASP   A O    1 
ATOM   3690 C  CB   A ASP   A 1 162 ? 1.628  -6.294  3.825   0.50 19.80 ?  162 ASP   A CB   1 
ATOM   3691 C  CB   B ASP   A 1 162 ? 1.627  -6.189  3.230   0.50 24.18 ?  162 ASP   A CB   1 
ATOM   3692 C  CG   A ASP   A 1 162 ? 1.349  -5.773  5.221   0.50 20.69 ?  162 ASP   A CG   1 
ATOM   3693 C  CG   B ASP   A 1 162 ? 1.303  -5.422  4.502   0.50 25.07 ?  162 ASP   A CG   1 
ATOM   3694 O  OD1  A ASP   A 1 162 ? 2.047  -6.192  6.171   0.50 21.34 ?  162 ASP   A OD1  1 
ATOM   3695 O  OD1  B ASP   A 1 162 ? 1.756  -5.841  5.587   0.50 25.41 ?  162 ASP   A OD1  1 
ATOM   3696 O  OD2  A ASP   A 1 162 ? 0.415  -4.955  5.366   0.50 21.22 -1 162 ASP   A OD2  1 
ATOM   3697 O  OD2  B ASP   A 1 162 ? 0.572  -4.410  4.418   0.50 25.62 -1 162 ASP   A OD2  1 
ATOM   3698 H  H    A ASP   A 1 162 ? 3.854  -5.274  3.661   0.50 22.92 ?  162 ASP   A H    1 
ATOM   3699 H  H    B ASP   A 1 162 ? 3.901  -5.433  3.586   0.50 26.69 ?  162 ASP   A H    1 
ATOM   3700 H  HA   A ASP   A 1 162 ? 3.028  -7.627  4.490   0.50 23.39 ?  162 ASP   A HA   1 
ATOM   3701 H  HA   B ASP   A 1 162 ? 2.723  -7.652  4.160   0.50 27.84 ?  162 ASP   A HA   1 
ATOM   3702 H  HB2  A ASP   A 1 162 ? 1.629  -5.548  3.204   0.50 23.79 ?  162 ASP   A HB2  1 
ATOM   3703 H  HB2  B ASP   A 1 162 ? 1.792  -5.542  2.521   0.50 29.05 ?  162 ASP   A HB2  1 
ATOM   3704 H  HB3  A ASP   A 1 162 ? 0.900  -6.899  3.612   0.50 23.79 ?  162 ASP   A HB3  1 
ATOM   3705 H  HB3  B ASP   A 1 162 ? 0.852  -6.727  3.010   0.50 29.05 ?  162 ASP   A HB3  1 
ATOM   3706 N  N    A LYS   A 1 163 ? 3.346  -7.344  1.327   0.50 20.58 ?  163 LYS   A N    1 
ATOM   3707 N  N    B LYS   A 1 163 ? 3.497  -7.457  1.053   0.50 23.78 ?  163 LYS   A N    1 
ATOM   3708 C  CA   A LYS   A 1 163 ? 3.430  -8.134  0.102   0.50 21.08 ?  163 LYS   A CA   1 
ATOM   3709 C  CA   B LYS   A 1 163 ? 3.633  -8.226  -0.179  0.50 24.16 ?  163 LYS   A CA   1 
ATOM   3710 C  C    A LYS   A 1 163 ? 4.565  -9.146  0.180   0.50 20.40 ?  163 LYS   A C    1 
ATOM   3711 C  C    B LYS   A 1 163 ? 4.656  -9.347  -0.022  0.50 22.79 ?  163 LYS   A C    1 
ATOM   3712 O  O    A LYS   A 1 163 ? 4.450  -10.257 -0.350  0.50 20.95 ?  163 LYS   A O    1 
ATOM   3713 O  O    B LYS   A 1 163 ? 4.416  -10.480 -0.455  0.50 23.36 ?  163 LYS   A O    1 
ATOM   3714 C  CB   A LYS   A 1 163 ? 3.611  -7.210  -1.104  0.50 23.02 ?  163 LYS   A CB   1 
ATOM   3715 C  CB   B LYS   A 1 163 ? 4.049  -7.275  -1.300  0.50 26.51 ?  163 LYS   A CB   1 
ATOM   3716 C  CG   A LYS   A 1 163 ? 3.671  -7.928  -2.446  0.50 25.38 ?  163 LYS   A CG   1 
ATOM   3717 C  CG   B LYS   A 1 163 ? 3.863  -7.794  -2.710  0.50 28.96 ?  163 LYS   A CG   1 
ATOM   3718 C  CD   A LYS   A 1 163 ? 4.054  -6.974  -3.568  0.50 27.60 ?  163 LYS   A CD   1 
ATOM   3719 C  CD   B LYS   A 1 163 ? 4.692  -6.959  -3.677  0.50 31.31 ?  163 LYS   A CD   1 
ATOM   3720 C  CE   A LYS   A 1 163 ? 4.034  -7.670  -4.921  0.50 29.36 ?  163 LYS   A CE   1 
ATOM   3721 C  CE   B LYS   A 1 163 ? 3.924  -6.607  -4.939  0.50 33.08 ?  163 LYS   A CE   1 
ATOM   3722 N  NZ   A LYS   A 1 163 ? 4.676  -6.847  -5.985  0.50 30.09 ?  163 LYS   A NZ   1 
ATOM   3723 N  NZ   B LYS   A 1 163 ? 4.806  -5.936  -5.936  0.50 34.10 ?  163 LYS   A NZ   1 
ATOM   3724 H  H    A LYS   A 1 163 ? 3.543  -6.512  1.233   0.50 24.73 ?  163 LYS   A H    1 
ATOM   3725 H  H    B LYS   A 1 163 ? 3.770  -6.645  0.995   0.50 28.57 ?  163 LYS   A H    1 
ATOM   3726 H  HA   A LYS   A 1 163 ? 2.600  -8.623  -0.019  0.50 25.33 ?  163 LYS   A HA   1 
ATOM   3727 H  HA   B LYS   A 1 163 ? 2.776  -8.619  -0.413  0.50 29.02 ?  163 LYS   A HA   1 
ATOM   3728 H  HB2  A LYS   A 1 163 ? 2.860  -6.590  -1.139  0.50 27.66 ?  163 LYS   A HB2  1 
ATOM   3729 H  HB2  B LYS   A 1 163 ? 3.527  -6.461  -1.221  0.50 31.84 ?  163 LYS   A HB2  1 
ATOM   3730 H  HB3  A LYS   A 1 163 ? 4.435  -6.714  -0.998  0.50 27.66 ?  163 LYS   A HB3  1 
ATOM   3731 H  HB3  B LYS   A 1 163 ? 4.989  -7.068  -1.189  0.50 31.84 ?  163 LYS   A HB3  1 
ATOM   3732 H  HG2  A LYS   A 1 163 ? 4.337  -8.631  -2.410  0.50 30.49 ?  163 LYS   A HG2  1 
ATOM   3733 H  HG2  B LYS   A 1 163 ? 4.161  -8.715  -2.760  0.50 34.78 ?  163 LYS   A HG2  1 
ATOM   3734 H  HG3  A LYS   A 1 163 ? 2.799  -8.302  -2.650  0.50 30.49 ?  163 LYS   A HG3  1 
ATOM   3735 H  HG3  B LYS   A 1 163 ? 2.928  -7.724  -2.963  0.50 34.78 ?  163 LYS   A HG3  1 
ATOM   3736 H  HD2  A LYS   A 1 163 ? 3.420  -6.239  -3.596  0.50 33.15 ?  163 LYS   A HD2  1 
ATOM   3737 H  HD2  B LYS   A 1 163 ? 4.949  -6.131  -3.241  0.50 37.60 ?  163 LYS   A HD2  1 
ATOM   3738 H  HD3  A LYS   A 1 163 ? 4.951  -6.638  -3.412  0.50 33.15 ?  163 LYS   A HD3  1 
ATOM   3739 H  HD3  B LYS   A 1 163 ? 5.482  -7.460  -3.931  0.50 37.60 ?  163 LYS   A HD3  1 
ATOM   3740 H  HE2  A LYS   A 1 163 ? 4.511  -8.510  -4.858  0.50 35.26 ?  163 LYS   A HE2  1 
ATOM   3741 H  HE2  B LYS   A 1 163 ? 3.572  -7.417  -5.338  0.50 39.72 ?  163 LYS   A HE2  1 
ATOM   3742 H  HE3  A LYS   A 1 163 ? 3.114  -7.830  -5.180  0.50 35.26 ?  163 LYS   A HE3  1 
ATOM   3743 H  HE3  B LYS   A 1 163 ? 3.201  -5.999  -4.715  0.50 39.72 ?  163 LYS   A HE3  1 
ATOM   3744 H  HZ1  A LYS   A 1 163 ? 4.650  -7.279  -6.762  0.50 36.14 ?  163 LYS   A HZ1  1 
ATOM   3745 H  HZ1  B LYS   A 1 163 ? 4.342  -5.736  -6.668  0.50 40.95 ?  163 LYS   A HZ1  1 
ATOM   3746 H  HZ2  A LYS   A 1 163 ? 4.246  -6.072  -6.071  0.50 36.14 ?  163 LYS   A HZ2  1 
ATOM   3747 H  HZ2  B LYS   A 1 163 ? 5.140  -5.186  -5.592  0.50 40.95 ?  163 LYS   A HZ2  1 
ATOM   3748 H  HZ3  A LYS   A 1 163 ? 5.525  -6.683  -5.773  0.50 36.14 ?  163 LYS   A HZ3  1 
ATOM   3749 H  HZ3  B LYS   A 1 163 ? 5.479  -6.476  -6.158  0.50 40.95 ?  163 LYS   A HZ3  1 
ATOM   3750 N  N    A LEU   A 1 164 ? 5.673  -8.774  0.827   0.50 18.96 ?  164 LEU   A N    1 
ATOM   3751 N  N    B LEU   A 1 164 ? 5.803  -9.046  0.592   0.50 20.91 ?  164 LEU   A N    1 
ATOM   3752 C  CA   A LEU   A 1 164 ? 6.797  -9.696  0.972   0.50 18.17 ?  164 LEU   A CA   1 
ATOM   3753 C  CA   B LEU   A 1 164 ? 6.850  -10.050 0.770   0.50 19.70 ?  164 LEU   A CA   1 
ATOM   3754 C  C    A LEU   A 1 164 ? 6.402  -10.922 1.784   0.50 18.52 ?  164 LEU   A C    1 
ATOM   3755 C  C    B LEU   A 1 164 ? 6.379  -11.166 1.691   0.50 19.78 ?  164 LEU   A C    1 
ATOM   3756 O  O    A LEU   A 1 164 ? 6.800  -12.047 1.462   0.50 18.82 ?  164 LEU   A O    1 
ATOM   3757 O  O    B LEU   A 1 164 ? 6.593  -12.351 1.409   0.50 20.18 ?  164 LEU   A O    1 
ATOM   3758 C  CB   A LEU   A 1 164 ? 7.967  -8.972  1.635   0.50 17.49 ?  164 LEU   A CB   1 
ATOM   3759 C  CB   B LEU   A 1 164 ? 8.103  -9.396  1.354   0.50 19.13 ?  164 LEU   A CB   1 
ATOM   3760 C  CG   A LEU   A 1 164 ? 8.742  -8.014  0.724   0.50 17.77 ?  164 LEU   A CG   1 
ATOM   3761 C  CG   B LEU   A 1 164 ? 8.791  -8.280  0.567   0.50 19.16 ?  164 LEU   A CG   1 
ATOM   3762 C  CD1  A LEU   A 1 164 ? 9.655  -7.098  1.527   0.50 17.58 ?  164 LEU   A CD1  1 
ATOM   3763 C  CD1  B LEU   A 1 164 ? 9.722  -7.480  1.471   0.50 19.17 ?  164 LEU   A CD1  1 
ATOM   3764 C  CD2  A LEU   A 1 164 ? 9.543  -8.790  -0.312  0.50 17.96 ?  164 LEU   A CD2  1 
ATOM   3765 C  CD2  B LEU   A 1 164 ? 9.559  -8.863  -0.596  0.50 19.51 ?  164 LEU   A CD2  1 
ATOM   3766 H  H    A LEU   A 1 164 ? 5.795  -7.998  1.185   0.50 22.79 ?  164 LEU   A H    1 
ATOM   3767 H  H    B LEU   A 1 164 ? 5.994  -8.279  0.922   0.50 25.13 ?  164 LEU   A H    1 
ATOM   3768 H  HA   A LEU   A 1 164 ? 7.078  -9.990  0.095   0.50 21.84 ?  164 LEU   A HA   1 
ATOM   3769 H  HA   B LEU   A 1 164 ? 7.075  -10.443 -0.087  0.50 23.67 ?  164 LEU   A HA   1 
ATOM   3770 H  HB2  A LEU   A 1 164 ? 7.627  -8.450  2.381   0.50 21.02 ?  164 LEU   A HB2  1 
ATOM   3771 H  HB2  B LEU   A 1 164 ? 7.867  -9.027  2.216   0.50 22.99 ?  164 LEU   A HB2  1 
ATOM   3772 H  HB3  A LEU   A 1 164 ? 8.594  -9.634  1.961   0.50 21.02 ?  164 LEU   A HB3  1 
ATOM   3773 H  HB3  B LEU   A 1 164 ? 8.765  -10.094 1.480   0.50 22.99 ?  164 LEU   A HB3  1 
ATOM   3774 H  HG   A LEU   A 1 164 ? 8.108  -7.453  0.249   0.50 21.36 ?  164 LEU   A HG   1 
ATOM   3775 H  HG   B LEU   A 1 164 ? 8.119  -7.676  0.216   0.50 23.02 ?  164 LEU   A HG   1 
ATOM   3776 H  HD11 A LEU   A 1 164 ? 10.125 -6.507  0.919   0.50 21.13 ?  164 LEU   A HD11 1 
ATOM   3777 H  HD11 B LEU   A 1 164 ? 10.150 -6.786  0.948   0.50 23.04 ?  164 LEU   A HD11 1 
ATOM   3778 H  HD12 A LEU   A 1 164 ? 9.115  -6.576  2.143   0.50 21.13 ?  164 LEU   A HD12 1 
ATOM   3779 H  HD12 B LEU   A 1 164 ? 9.202  -7.082  2.188   0.50 23.04 ?  164 LEU   A HD12 1 
ATOM   3780 H  HD13 A LEU   A 1 164 ? 10.289 -7.639  2.022   0.50 21.13 ?  164 LEU   A HD13 1 
ATOM   3781 H  HD13 B LEU   A 1 164 ? 10.392 -8.077  1.841   0.50 23.04 ?  164 LEU   A HD13 1 
ATOM   3782 H  HD21 A LEU   A 1 164 ? 10.112 -8.173  -0.798  0.50 21.59 ?  164 LEU   A HD21 1 
ATOM   3783 H  HD21 B LEU   A 1 164 ? 9.980  -8.141  -1.087  0.50 23.45 ?  164 LEU   A HD21 1 
ATOM   3784 H  HD22 A LEU   A 1 164 ? 10.084 -9.454  0.141   0.50 21.59 ?  164 LEU   A HD22 1 
ATOM   3785 H  HD22 B LEU   A 1 164 ? 10.233 -9.470  -0.254  0.50 23.45 ?  164 LEU   A HD22 1 
ATOM   3786 H  HD23 A LEU   A 1 164 ? 8.929  -9.225  -0.925  0.50 21.59 ?  164 LEU   A HD23 1 
ATOM   3787 H  HD23 B LEU   A 1 164 ? 8.941  -9.340  -1.170  0.50 23.45 ?  164 LEU   A HD23 1 
ATOM   3788 N  N    A VAL   A 1 165 ? 5.617  -10.720 2.841   0.50 18.39 ?  165 VAL   A N    1 
ATOM   3789 N  N    B VAL   A 1 165 ? 5.758  -10.801 2.813   0.50 19.80 ?  165 VAL   A N    1 
ATOM   3790 C  CA   A VAL   A 1 165 ? 5.201  -11.829 3.692   0.50 18.34 ?  165 VAL   A CA   1 
ATOM   3791 C  CA   B VAL   A 1 165 ? 5.220  -11.802 3.730   0.50 20.10 ?  165 VAL   A CA   1 
ATOM   3792 C  C    A VAL   A 1 165 ? 4.197  -12.717 2.966   0.50 18.18 ?  165 VAL   A C    1 
ATOM   3793 C  C    B VAL   A 1 165 ? 4.123  -12.604 3.046   0.50 20.44 ?  165 VAL   A C    1 
ATOM   3794 O  O    A VAL   A 1 165 ? 4.339  -13.945 2.929   0.50 18.12 ?  165 VAL   A O    1 
ATOM   3795 O  O    B VAL   A 1 165 ? 4.150  -13.840 3.029   0.50 20.24 ?  165 VAL   A O    1 
ATOM   3796 C  CB   A VAL   A 1 165 ? 4.631  -11.284 5.014   0.50 18.91 ?  165 VAL   A CB   1 
ATOM   3797 C  CB   B VAL   A 1 165 ? 4.714  -11.131 5.021   0.50 20.49 ?  165 VAL   A CB   1 
ATOM   3798 C  CG1  A VAL   A 1 165 ? 3.918  -12.381 5.789   0.50 19.07 ?  165 VAL   A CG1  1 
ATOM   3799 C  CG1  B VAL   A 1 165 ? 3.936  -12.126 5.875   0.50 20.63 ?  165 VAL   A CG1  1 
ATOM   3800 C  CG2  A VAL   A 1 165 ? 5.738  -10.647 5.847   0.50 19.44 ?  165 VAL   A CG2  1 
ATOM   3801 C  CG2  B VAL   A 1 165 ? 5.876  -10.544 5.807   0.50 20.99 ?  165 VAL   A CG2  1 
ATOM   3802 H  H    A VAL   A 1 165 ? 5.307  -9.956  3.085   0.50 22.10 ?  165 VAL   A H    1 
ATOM   3803 H  H    B VAL   A 1 165 ? 5.631  -9.991  3.061   0.50 23.80 ?  165 VAL   A H    1 
ATOM   3804 H  HA   A VAL   A 1 165 ? 5.973  -12.373 3.904   0.50 22.04 ?  165 VAL   A HA   1 
ATOM   3805 H  HA   B VAL   A 1 165 ? 5.925  -12.418 3.978   0.50 24.15 ?  165 VAL   A HA   1 
ATOM   3806 H  HB   A VAL   A 1 165 ? 3.979  -10.595 4.813   0.50 22.73 ?  165 VAL   A HB   1 
ATOM   3807 H  HB   B VAL   A 1 165 ? 4.114  -10.405 4.789   0.50 24.63 ?  165 VAL   A HB   1 
ATOM   3808 H  HG11 A VAL   A 1 165 ? 3.818  -12.100 6.711   0.50 22.91 ?  165 VAL   A HG11 1 
ATOM   3809 H  HG11 B VAL   A 1 165 ? 3.863  -11.777 6.778   0.50 24.79 ?  165 VAL   A HG11 1 
ATOM   3810 H  HG12 A VAL   A 1 165 ? 3.041  -12.529 5.395   0.50 22.91 ?  165 VAL   A HG12 1 
ATOM   3811 H  HG12 B VAL   A 1 165 ? 3.049  -12.245 5.498   0.50 24.79 ?  165 VAL   A HG12 1 
ATOM   3812 H  HG13 A VAL   A 1 165 ? 4.444  -13.192 5.744   0.50 22.91 ?  165 VAL   A HG13 1 
ATOM   3813 H  HG13 B VAL   A 1 165 ? 4.409  -12.972 5.886   0.50 24.79 ?  165 VAL   A HG13 1 
ATOM   3814 H  HG21 A VAL   A 1 165 ? 5.362  -10.313 6.676   0.50 23.36 ?  165 VAL   A HG21 1 
ATOM   3815 H  HG21 B VAL   A 1 165 ? 5.535  -10.131 6.617   0.50 25.22 ?  165 VAL   A HG21 1 
ATOM   3816 H  HG22 A VAL   A 1 165 ? 6.417  -11.315 6.036   0.50 23.36 ?  165 VAL   A HG22 1 
ATOM   3817 H  HG22 B VAL   A 1 165 ? 6.495  -11.256 6.035   0.50 25.22 ?  165 VAL   A HG22 1 
ATOM   3818 H  HG23 A VAL   A 1 165 ? 6.129  -9.914  5.344   0.50 23.36 ?  165 VAL   A HG23 1 
ATOM   3819 H  HG23 B VAL   A 1 165 ? 6.322  -9.879  5.260   0.50 25.22 ?  165 VAL   A HG23 1 
ATOM   3820 N  N    A SER   A 1 166 ? 3.165  -12.107 2.381   0.50 18.71 ?  166 SER   A N    1 
ATOM   3821 N  N    B SER   A 1 166 ? 3.143  -11.908 2.463   0.50 21.29 ?  166 SER   A N    1 
ATOM   3822 C  CA   A SER   A 1 166 ? 2.056  -12.866 1.812   0.50 19.38 ?  166 SER   A CA   1 
ATOM   3823 C  CA   B SER   A 1 166 ? 1.992  -12.593 1.882   0.50 22.24 ?  166 SER   A CA   1 
ATOM   3824 C  C    A SER   A 1 166 ? 2.444  -13.604 0.544   0.50 19.91 ?  166 SER   A C    1 
ATOM   3825 C  C    B SER   A 1 166 ? 2.425  -13.647 0.872   0.50 22.51 ?  166 SER   A C    1 
ATOM   3826 O  O    A SER   A 1 166 ? 1.751  -14.555 0.163   0.50 20.73 ?  166 SER   A O    1 
ATOM   3827 O  O    B SER   A 1 166 ? 1.890  -14.764 0.861   0.50 22.21 ?  166 SER   A O    1 
ATOM   3828 C  CB   A SER   A 1 166 ? 0.892  -11.932 1.472   0.50 20.71 ?  166 SER   A CB   1 
ATOM   3829 C  CB   B SER   A 1 166 ? 1.042  -11.577 1.236   0.50 23.49 ?  166 SER   A CB   1 
ATOM   3830 O  OG   A SER   A 1 166 ? 0.383  -11.278 2.620   0.50 22.57 ?  166 SER   A OG   1 
ATOM   3831 O  OG   B SER   A 1 166 ? 0.654  -10.579 2.164   0.50 25.19 ?  166 SER   A OG   1 
ATOM   3832 H  H    A SER   A 1 166 ? 3.073  -11.265 2.311   0.50 22.49 ?  166 SER   A H    1 
ATOM   3833 H  H    B SER   A 1 166 ? 3.117  -11.053 2.401   0.50 25.58 ?  166 SER   A H    1 
ATOM   3834 H  HA   A SER   A 1 166 ? 1.739  -13.526 2.455   0.50 23.29 ?  166 SER   A HA   1 
ATOM   3835 H  HA   B SER   A 1 166 ? 1.496  -13.043 2.582   0.50 26.72 ?  166 SER   A HA   1 
ATOM   3836 H  HB2  A SER   A 1 166 ? 1.204  -11.263 0.845   0.50 24.88 ?  166 SER   A HB2  1 
ATOM   3837 H  HB2  B SER   A 1 166 ? 1.480  -11.153 0.485   0.50 28.23 ?  166 SER   A HB2  1 
ATOM   3838 H  HB3  A SER   A 1 166 ? 0.176  -12.452 1.067   0.50 24.88 ?  166 SER   A HB3  1 
ATOM   3839 H  HB3  B SER   A 1 166 ? 0.237  -12.034 0.930   0.50 28.23 ?  166 SER   A HB3  1 
ATOM   3840 H  HG   A SER   A 1 166 ? 0.996  -10.831 2.984   0.50 27.12 ?  166 SER   A HG   1 
ATOM   3841 H  HG   B SER   A 1 166 ? 1.329  -10.194 2.483   0.50 30.27 ?  166 SER   A HG   1 
ATOM   3842 N  N    A SER   A 1 167 ? 3.500  -13.166 -0.139  0.50 19.43 ?  167 SER   A N    1 
ATOM   3843 N  N    B SER   A 1 167 ? 3.410  -13.323 0.031   0.50 23.05 ?  167 SER   A N    1 
ATOM   3844 C  CA   A SER   A 1 167 ? 3.985  -13.868 -1.314  0.50 19.61 ?  167 SER   A CA   1 
ATOM   3845 C  CA   B SER   A 1 167 ? 3.800  -14.221 -1.051  0.50 23.45 ?  167 SER   A CA   1 
ATOM   3846 C  C    A SER   A 1 167 ? 5.129  -14.816 -0.999  0.50 19.41 ?  167 SER   A C    1 
ATOM   3847 C  C    B SER   A 1 167 ? 5.146  -14.890 -0.804  0.50 23.28 ?  167 SER   A C    1 
ATOM   3848 O  O    A SER   A 1 167 ? 5.564  -15.553 -1.890  0.50 19.24 ?  167 SER   A O    1 
ATOM   3849 O  O    B SER   A 1 167 ? 6.031  -14.829 -1.663  0.50 24.04 ?  167 SER   A O    1 
ATOM   3850 C  CB   A SER   A 1 167 ? 4.432  -12.870 -2.386  0.50 19.62 ?  167 SER   A CB   1 
ATOM   3851 C  CB   B SER   A 1 167 ? 3.836  -13.462 -2.381  0.50 24.50 ?  167 SER   A CB   1 
ATOM   3852 O  OG   A SER   A 1 167 ? 5.496  -12.061 -1.911  0.50 19.00 ?  167 SER   A OG   1 
ATOM   3853 O  OG   B SER   A 1 167 ? 4.821  -12.440 -2.356  0.50 25.34 ?  167 SER   A OG   1 
ATOM   3854 H  H    A SER   A 1 167 ? 3.937  -12.453 0.055   0.50 23.35 ?  167 SER   A H    1 
ATOM   3855 H  H    B SER   A 1 167 ? 3.856  -12.582 0.067   0.50 27.69 ?  167 SER   A H    1 
ATOM   3856 H  HA   A SER   A 1 167 ? 3.263  -14.391 -1.691  0.50 23.56 ?  167 SER   A HA   1 
ATOM   3857 H  HA   B SER   A 1 167 ? 3.150  -14.925 -1.128  0.50 28.17 ?  167 SER   A HA   1 
ATOM   3858 H  HB2  A SER   A 1 167 ? 4.743  -13.359 -3.166  0.50 23.57 ?  167 SER   A HB2  1 
ATOM   3859 H  HB2  B SER   A 1 167 ? 4.048  -14.088 -3.092  0.50 29.43 ?  167 SER   A HB2  1 
ATOM   3860 H  HB3  A SER   A 1 167 ? 3.687  -12.300 -2.627  0.50 23.57 ?  167 SER   A HB3  1 
ATOM   3861 H  HB3  B SER   A 1 167 ? 2.958  -13.070 -2.545  0.50 29.43 ?  167 SER   A HB3  1 
ATOM   3862 H  HG   A SER   A 1 167 ? 5.245  -11.617 -1.239  0.50 22.83 ?  167 SER   A HG   1 
ATOM   3863 H  HG   B SER   A 1 167 ? 4.626  -11.876 -1.764  0.50 30.44 ?  167 SER   A HG   1 
ATOM   3864 N  N    A PHE   A 1 168 ? 5.618  -14.829 0.238   0.50 18.96 ?  168 PHE   A N    1 
ATOM   3865 N  N    B PHE   A 1 168 ? 5.302  -15.562 0.337   0.50 22.13 ?  168 PHE   A N    1 
ATOM   3866 C  CA   A PHE   A 1 168 ? 6.783  -15.644 0.539   0.50 19.37 ?  168 PHE   A CA   1 
ATOM   3867 C  CA   B PHE   A 1 168 ? 6.573  -16.182 0.701   0.50 21.50 ?  168 PHE   A CA   1 
ATOM   3868 C  C    A PHE   A 1 168 ? 6.432  -17.118 0.437   0.50 21.01 ?  168 PHE   A C    1 
ATOM   3869 C  C    B PHE   A 1 168 ? 6.545  -17.703 0.607   0.50 22.46 ?  168 PHE   A C    1 
ATOM   3870 O  O    A PHE   A 1 168 ? 5.414  -17.570 0.974   0.50 21.78 ?  168 PHE   A O    1 
ATOM   3871 O  O    B PHE   A 1 168 ? 7.403  -18.290 -0.057  0.50 22.21 ?  168 PHE   A O    1 
ATOM   3872 C  CB   A PHE   A 1 168 ? 7.343  -15.349 1.927   0.50 18.37 ?  168 PHE   A CB   1 
ATOM   3873 C  CB   B PHE   A 1 168 ? 7.028  -15.750 2.101   0.50 20.95 ?  168 PHE   A CB   1 
ATOM   3874 C  CG   A PHE   A 1 168 ? 8.572  -16.155 2.244   0.50 17.65 ?  168 PHE   A CG   1 
ATOM   3875 C  CG   B PHE   A 1 168 ? 8.385  -16.277 2.478   0.50 20.47 ?  168 PHE   A CG   1 
ATOM   3876 C  CD1  A PHE   A 1 168 ? 9.768  -15.875 1.608   0.50 17.36 ?  168 PHE   A CD1  1 
ATOM   3877 C  CD1  B PHE   A 1 168 ? 9.529  -15.735 1.919   0.50 20.23 ?  168 PHE   A CD1  1 
ATOM   3878 C  CD2  A PHE   A 1 168 ? 8.531  -17.213 3.140   0.50 17.22 ?  168 PHE   A CD2  1 
ATOM   3879 C  CD2  B PHE   A 1 168 ? 8.519  -17.321 3.378   0.50 20.27 ?  168 PHE   A CD2  1 
ATOM   3880 C  CE1  A PHE   A 1 168 ? 10.902 -16.617 1.872   0.50 16.72 ?  168 PHE   A CE1  1 
ATOM   3881 C  CE1  B PHE   A 1 168 ? 10.780 -16.220 2.256   0.50 19.98 ?  168 PHE   A CE1  1 
ATOM   3882 C  CE2  A PHE   A 1 168 ? 9.670  -17.957 3.409   0.50 17.09 ?  168 PHE   A CE2  1 
ATOM   3883 C  CE2  B PHE   A 1 168 ? 9.768  -17.806 3.719   0.50 20.24 ?  168 PHE   A CE2  1 
ATOM   3884 C  CZ   A PHE   A 1 168 ? 10.856 -17.656 2.774   0.50 16.87 ?  168 PHE   A CZ   1 
ATOM   3885 C  CZ   B PHE   A 1 168 ? 10.897 -17.256 3.157   0.50 20.09 ?  168 PHE   A CZ   1 
ATOM   3886 H  H    A PHE   A 1 168 ? 5.298  -14.389 0.903   0.50 22.79 ?  168 PHE   A H    1 
ATOM   3887 H  H    B PHE   A 1 168 ? 4.675  -15.680 0.910   0.50 26.59 ?  168 PHE   A H    1 
ATOM   3888 H  HA   A PHE   A 1 168 ? 7.479  -15.455 -0.111  0.50 23.28 ?  168 PHE   A HA   1 
ATOM   3889 H  HA   B PHE   A 1 168 ? 7.249  -15.869 0.079   0.50 25.83 ?  168 PHE   A HA   1 
ATOM   3890 H  HB2  A PHE   A 1 168 ? 7.579  -14.409 1.978   0.50 22.08 ?  168 PHE   A HB2  1 
ATOM   3891 H  HB2  B PHE   A 1 168 ? 7.068  -14.783 2.135   0.50 25.18 ?  168 PHE   A HB2  1 
ATOM   3892 H  HB3  A PHE   A 1 168 ? 6.667  -15.557 2.591   0.50 22.08 ?  168 PHE   A HB3  1 
ATOM   3893 H  HB3  B PHE   A 1 168 ? 6.392  -16.081 2.752   0.50 25.18 ?  168 PHE   A HB3  1 
ATOM   3894 H  HD1  A PHE   A 1 168 ? 9.812  -15.174 1.000   0.50 20.87 ?  168 PHE   A HD1  1 
ATOM   3895 H  HD1  B PHE   A 1 168 ? 9.458  -15.036 1.310   0.50 24.31 ?  168 PHE   A HD1  1 
ATOM   3896 H  HD2  A PHE   A 1 168 ? 7.731  -17.419 3.571   0.50 20.70 ?  168 PHE   A HD2  1 
ATOM   3897 H  HD2  B PHE   A 1 168 ? 7.758  -17.698 3.759   0.50 24.36 ?  168 PHE   A HD2  1 
ATOM   3898 H  HE1  A PHE   A 1 168 ? 11.704 -16.413 1.444   0.50 20.09 ?  168 PHE   A HE1  1 
ATOM   3899 H  HE1  B PHE   A 1 168 ? 11.544 -15.846 1.877   0.50 24.01 ?  168 PHE   A HE1  1 
ATOM   3900 H  HE2  A PHE   A 1 168 ? 9.632  -18.664 4.016   0.50 20.54 ?  168 PHE   A HE2  1 
ATOM   3901 H  HE2  B PHE   A 1 168 ? 9.842  -18.507 4.327   0.50 24.32 ?  168 PHE   A HE2  1 
ATOM   3902 H  HZ   A PHE   A 1 168 ? 11.622 -18.159 2.951   0.50 20.28 ?  168 PHE   A HZ   1 
ATOM   3903 H  HZ   B PHE   A 1 168 ? 11.737 -17.582 3.387   0.50 24.15 ?  168 PHE   A HZ   1 
ATOM   3904 N  N    A LEU   A 1 169 ? 7.289  -17.866 -0.248  0.50 22.37 ?  169 LEU   A N    1 
ATOM   3905 N  N    B LEU   A 1 169 ? 5.622  -18.367 1.294   0.50 24.17 ?  169 LEU   A N    1 
ATOM   3906 C  CA   A LEU   A 1 169 ? 7.101  -19.297 -0.399  0.50 23.41 ?  169 LEU   A CA   1 
ATOM   3907 C  CA   B LEU   A 1 169 ? 5.553  -19.826 1.233   0.50 26.24 ?  169 LEU   A CA   1 
ATOM   3908 C  C    A LEU   A 1 169 ? 7.943  -20.033 0.633   0.50 23.09 ?  169 LEU   A C    1 
ATOM   3909 C  C    B LEU   A 1 169 ? 5.030  -20.292 -0.120  0.50 27.61 ?  169 LEU   A C    1 
ATOM   3910 O  O    A LEU   A 1 169 ? 7.408  -20.476 1.650   0.50 23.24 ?  169 LEU   A O    1 
ATOM   3911 O  O    B LEU   A 1 169 ? 3.832  -20.263 -0.382  0.50 27.71 ?  169 LEU   A O    1 
ATOM   3912 C  CB   A LEU   A 1 169 ? 7.449  -19.730 -1.829  0.50 24.34 ?  169 LEU   A CB   1 
ATOM   3913 C  CB   B LEU   A 1 169 ? 4.678  -20.373 2.365   0.50 26.62 ?  169 LEU   A CB   1 
ATOM   3914 C  CG   A LEU   A 1 169 ? 7.136  -21.179 -2.211  0.50 25.11 ?  169 LEU   A CG   1 
ATOM   3915 C  CG   B LEU   A 1 169 ? 5.081  -21.718 2.983   0.50 26.86 ?  169 LEU   A CG   1 
ATOM   3916 C  CD1  A LEU   A 1 169 ? 5.722  -21.555 -1.804  0.50 25.45 ?  169 LEU   A CD1  1 
ATOM   3917 C  CD1  B LEU   A 1 169 ? 4.099  -22.119 4.077   0.50 26.88 ?  169 LEU   A CD1  1 
ATOM   3918 C  CD2  A LEU   A 1 169 ? 7.331  -21.392 -3.707  0.50 25.12 ?  169 LEU   A CD2  1 
ATOM   3919 C  CD2  B LEU   A 1 169 ? 5.203  -22.823 1.938   0.50 27.43 ?  169 LEU   A CD2  1 
ATOM   3920 O  OXT  A LEU   A 1 169 ? 9.158  -20.180 0.496   0.50 22.50 -1 169 LEU   A OXT  1 
ATOM   3921 O  OXT  B LEU   A 1 169 ? 5.805  -20.709 -0.982  0.50 28.80 -1 169 LEU   A OXT  1 
ATOM   3922 H  H    A LEU   A 1 169 ? 7.998  -17.567 -0.638  0.50 26.88 ?  169 LEU   A H    1 
ATOM   3923 H  H    B LEU   A 1 169 ? 5.050  -17.999 1.817   0.50 29.04 ?  169 LEU   A H    1 
ATOM   3924 H  HA   A LEU   A 1 169 ? 6.182  -19.522 -0.224  0.50 28.13 ?  169 LEU   A HA   1 
ATOM   3925 H  HA   B LEU   A 1 169 ? 6.442  -20.189 1.322   0.50 31.52 ?  169 LEU   A HA   1 
ATOM   3926 H  HB2  A LEU   A 1 169 ? 6.951  -19.163 -2.441  0.50 29.24 ?  169 LEU   A HB2  1 
ATOM   3927 H  HB2  B LEU   A 1 169 ? 4.684  -19.721 3.081   0.50 31.98 ?  169 LEU   A HB2  1 
ATOM   3928 H  HB3  A LEU   A 1 169 ? 8.397  -19.597 -1.971  0.50 29.24 ?  169 LEU   A HB3  1 
ATOM   3929 H  HB3  B LEU   A 1 169 ? 3.773  -20.470 2.033   0.50 31.98 ?  169 LEU   A HB3  1 
ATOM   3930 H  HG   A LEU   A 1 169 ? 7.750  -21.769 -1.746  0.50 30.16 ?  169 LEU   A HG   1 
ATOM   3931 H  HG   B LEU   A 1 169 ? 5.949  -21.615 3.398   0.50 32.27 ?  169 LEU   A HG   1 
ATOM   3932 H  HD11 A LEU   A 1 169 ? 5.482  -22.393 -2.229  0.50 30.57 ?  169 LEU   A HD11 1 
ATOM   3933 H  HD11 B LEU   A 1 169 ? 4.376  -22.969 4.452   0.50 32.29 ?  169 LEU   A HD11 1 
ATOM   3934 H  HD12 A LEU   A 1 169 ? 5.685  -21.652 -0.840  0.50 30.57 ?  169 LEU   A HD12 1 
ATOM   3935 H  HD12 B LEU   A 1 169 ? 4.102  -21.436 4.767   0.50 32.29 ?  169 LEU   A HD12 1 
ATOM   3936 H  HD13 A LEU   A 1 169 ? 5.114  -20.855 -2.091  0.50 30.57 ?  169 LEU   A HD13 1 
ATOM   3937 H  HD13 B LEU   A 1 169 ? 3.213  -22.197 3.692   0.50 32.29 ?  169 LEU   A HD13 1 
ATOM   3938 H  HD21 A LEU   A 1 169 ? 7.135  -22.317 -3.924  0.50 30.18 ?  169 LEU   A HD21 1 
ATOM   3939 H  HD21 B LEU   A 1 169 ? 5.472  -23.644 2.381   0.50 32.95 ?  169 LEU   A HD21 1 
ATOM   3940 H  HD22 A LEU   A 1 169 ? 6.727  -20.805 -4.190  0.50 30.18 ?  169 LEU   A HD22 1 
ATOM   3941 H  HD22 B LEU   A 1 169 ? 4.345  -22.949 1.507   0.50 32.95 ?  169 LEU   A HD22 1 
ATOM   3942 H  HD23 A LEU   A 1 169 ? 8.249  -21.185 -3.940  0.50 30.18 ?  169 LEU   A HD23 1 
ATOM   3943 H  HD23 B LEU   A 1 169 ? 5.870  -22.568 1.283   0.50 32.95 ?  169 LEU   A HD23 1 
ATOM   3944 N  N    A SER   B 1 1   ? 50.782 -9.182  -23.727 0.50 30.62 ?  1   SER   B N    1 
ATOM   3945 N  N    B SER   B 1 1   ? 50.916 -9.335  -23.847 0.50 26.96 ?  1   SER   B N    1 
ATOM   3946 C  CA   A SER   B 1 1   ? 51.325 -10.253 -22.869 0.50 30.30 ?  1   SER   B CA   1 
ATOM   3947 C  CA   B SER   B 1 1   ? 51.335 -10.280 -22.790 0.50 27.05 ?  1   SER   B CA   1 
ATOM   3948 C  C    A SER   B 1 1   ? 50.275 -11.323 -22.629 0.50 28.98 ?  1   SER   B C    1 
ATOM   3949 C  C    B SER   B 1 1   ? 50.247 -11.314 -22.521 0.50 26.52 ?  1   SER   B C    1 
ATOM   3950 O  O    A SER   B 1 1   ? 49.084 -11.130 -22.901 0.50 28.68 ?  1   SER   B O    1 
ATOM   3951 O  O    B SER   B 1 1   ? 49.076 -11.129 -22.874 0.50 26.21 ?  1   SER   B O    1 
ATOM   3952 C  CB   A SER   B 1 1   ? 51.807 -9.685  -21.537 0.50 31.03 ?  1   SER   B CB   1 
ATOM   3953 C  CB   B SER   B 1 1   ? 51.685 -9.535  -21.504 0.50 27.44 ?  1   SER   B CB   1 
ATOM   3954 O  OG   A SER   B 1 1   ? 50.713 -9.276  -20.737 0.50 32.15 ?  1   SER   B OG   1 
ATOM   3955 O  OG   B SER   B 1 1   ? 50.683 -9.725  -20.522 0.50 28.34 ?  1   SER   B OG   1 
ATOM   3956 H  H1   A SER   B 1 1   ? 50.540 -9.532  -24.506 0.50 36.77 ?  1   SER   B H1   1 
ATOM   3957 H  H1   B SER   B 1 1   ? 51.567 -8.744  -23.979 0.50 32.38 ?  1   SER   B H1   1 
ATOM   3958 H  H2   A SER   B 1 1   ? 50.081 -8.818  -23.326 0.50 36.77 ?  1   SER   B H2   1 
ATOM   3959 H  H2   B SER   B 1 1   ? 50.764 -9.787  -24.596 0.50 32.38 ?  1   SER   B H2   1 
ATOM   3960 H  H3   A SER   B 1 1   ? 51.413 -8.571  -23.852 0.50 36.77 ?  1   SER   B H3   1 
ATOM   3961 H  H3   B SER   B 1 1   ? 50.178 -8.919  -23.588 0.50 32.38 ?  1   SER   B H3   1 
ATOM   3962 H  HA   A SER   B 1 1   ? 52.073 -10.660 -23.320 0.50 36.40 ?  1   SER   B HA   1 
ATOM   3963 H  HA   B SER   B 1 1   ? 52.126 -10.741 -23.098 0.50 32.49 ?  1   SER   B HA   1 
ATOM   3964 H  HB2  A SER   B 1 1   ? 52.310 -10.372 -21.073 0.50 37.27 ?  1   SER   B HB2  1 
ATOM   3965 H  HB2  B SER   B 1 1   ? 52.527 -9.877  -21.168 0.50 32.96 ?  1   SER   B HB2  1 
ATOM   3966 H  HB3  A SER   B 1 1   ? 52.372 -8.916  -21.707 0.50 37.27 ?  1   SER   B HB3  1 
ATOM   3967 H  HB3  B SER   B 1 1   ? 51.766 -8.587  -21.699 0.50 32.96 ?  1   SER   B HB3  1 
ATOM   3968 H  HG   A SER   B 1 1   ? 50.988 -8.795  -20.107 0.50 38.62 ?  1   SER   B HG   1 
ATOM   3969 H  HG   B SER   B 1 1   ? 50.675 -9.069  -19.998 0.50 34.04 ?  1   SER   B HG   1 
ATOM   3970 N  N    A MET   B 1 2   ? 50.734 -12.452 -22.106 0.50 27.76 ?  2   MET   B N    1 
ATOM   3971 N  N    B MET   B 1 2   ? 50.655 -12.403 -21.879 0.50 26.09 ?  2   MET   B N    1 
ATOM   3972 C  CA   A MET   B 1 2   ? 49.913 -13.638 -21.926 0.50 27.06 ?  2   MET   B CA   1 
ATOM   3973 C  CA   B MET   B 1 2   ? 49.840 -13.605 -21.731 0.50 26.06 ?  2   MET   B CA   1 
ATOM   3974 C  C    A MET   B 1 2   ? 49.686 -13.832 -20.435 0.50 23.83 ?  2   MET   B C    1 
ATOM   3975 C  C    B MET   B 1 2   ? 49.559 -13.827 -20.249 0.50 24.14 ?  2   MET   B C    1 
ATOM   3976 O  O    A MET   B 1 2   ? 50.642 -14.028 -19.678 0.50 22.97 ?  2   MET   B O    1 
ATOM   3977 O  O    B MET   B 1 2   ? 50.433 -14.287 -19.507 0.50 24.70 ?  2   MET   B O    1 
ATOM   3978 C  CB   A MET   B 1 2   ? 50.622 -14.844 -22.537 0.50 30.32 ?  2   MET   B CB   1 
ATOM   3979 C  CB   B MET   B 1 2   ? 50.595 -14.781 -22.325 0.50 28.68 ?  2   MET   B CB   1 
ATOM   3980 C  CG   A MET   B 1 2   ? 49.759 -16.085 -22.680 0.50 33.28 ?  2   MET   B CG   1 
ATOM   3981 C  CG   B MET   B 1 2   ? 49.737 -15.951 -22.779 0.50 30.77 ?  2   MET   B CG   1 
ATOM   3982 S  SD   A MET   B 1 2   ? 50.583 -17.359 -23.653 0.50 35.94 ?  2   MET   B SD   1 
ATOM   3983 S  SD   B MET   B 1 2   ? 50.642 -17.015 -23.911 0.50 32.61 ?  2   MET   B SD   1 
ATOM   3984 C  CE   A MET   B 1 2   ? 51.159 -16.363 -25.025 0.50 36.14 ?  2   MET   B CE   1 
ATOM   3985 C  CE   B MET   B 1 2   ? 51.471 -15.786 -24.899 0.50 32.98 ?  2   MET   B CE   1 
ATOM   3986 H  H    A MET   B 1 2   ? 51.543 -12.561 -21.831 0.50 33.34 ?  2   MET   B H    1 
ATOM   3987 H  H    B MET   B 1 2   ? 51.434 -12.480 -21.521 0.50 31.34 ?  2   MET   B H    1 
ATOM   3988 H  HA   A MET   B 1 2   ? 49.063 -13.532 -22.375 0.50 32.50 ?  2   MET   B HA   1 
ATOM   3989 H  HA   B MET   B 1 2   ? 49.009 -13.502 -22.221 0.50 31.31 ?  2   MET   B HA   1 
ATOM   3990 H  HB2  A MET   B 1 2   ? 50.924 -14.568 -23.416 0.50 36.42 ?  2   MET   B HB2  1 
ATOM   3991 H  HB2  B MET   B 1 2   ? 51.095 -14.420 -23.067 0.50 34.45 ?  2   MET   B HB2  1 
ATOM   3992 H  HB3  A MET   B 1 2   ? 51.384 -15.086 -21.993 0.50 36.42 ?  2   MET   B HB3  1 
ATOM   3993 H  HB3  B MET   B 1 2   ? 51.211 -15.136 -21.674 0.50 34.45 ?  2   MET   B HB3  1 
ATOM   3994 H  HG2  A MET   B 1 2   ? 49.574 -16.444 -21.797 0.50 39.97 ?  2   MET   B HG2  1 
ATOM   3995 H  HG2  B MET   B 1 2   ? 49.475 -16.478 -22.002 0.50 36.96 ?  2   MET   B HG2  1 
ATOM   3996 H  HG3  A MET   B 1 2   ? 48.933 -15.857 -23.132 0.50 39.97 ?  2   MET   B HG3  1 
ATOM   3997 H  HG3  B MET   B 1 2   ? 48.954 -15.634 -23.245 0.50 36.96 ?  2   MET   B HG3  1 
ATOM   3998 H  HE1  A MET   B 1 2   ? 51.328 -16.939 -25.775 0.50 43.40 ?  2   MET   B HE1  1 
ATOM   3999 H  HE1  B MET   B 1 2   ? 51.678 -16.188 -25.734 0.50 39.61 ?  2   MET   B HE1  1 
ATOM   4000 H  HE2  A MET   B 1 2   ? 50.467 -15.715 -25.248 0.50 43.40 ?  2   MET   B HE2  1 
ATOM   4001 H  HE2  B MET   B 1 2   ? 50.869 -15.033 -25.033 0.50 39.61 ?  2   MET   B HE2  1 
ATOM   4002 H  HE3  A MET   B 1 2   ? 51.974 -15.894 -24.771 0.50 43.40 ?  2   MET   B HE3  1 
ATOM   4003 H  HE3  B MET   B 1 2   ? 52.286 -15.489 -24.449 0.50 39.61 ?  2   MET   B HE3  1 
ATOM   4004 N  N    A VAL   B 1 3   ? 48.427 -13.730 -20.013 0.50 21.47 ?  3   VAL   B N    1 
ATOM   4005 N  N    B VAL   B 1 3   ? 48.343 -13.503 -19.822 0.50 21.79 ?  3   VAL   B N    1 
ATOM   4006 C  CA   A VAL   B 1 3   ? 48.025 -13.980 -18.637 0.50 20.08 ?  3   VAL   B CA   1 
ATOM   4007 C  CA   B VAL   B 1 3   ? 47.895 -13.764 -18.460 0.50 20.49 ?  3   VAL   B CA   1 
ATOM   4008 C  C    A VAL   B 1 3   ? 46.796 -14.880 -18.659 0.50 18.07 ?  3   VAL   B C    1 
ATOM   4009 C  C    B VAL   B 1 3   ? 46.646 -14.631 -18.511 0.50 18.62 ?  3   VAL   B C    1 
ATOM   4010 O  O    A VAL   B 1 3   ? 46.114 -15.016 -19.678 0.50 17.89 ?  3   VAL   B O    1 
ATOM   4011 O  O    B VAL   B 1 3   ? 45.824 -14.529 -19.427 0.50 18.98 ?  3   VAL   B O    1 
ATOM   4012 C  CB   A VAL   B 1 3   ? 47.732 -12.672 -17.867 0.50 21.40 ?  3   VAL   B CB   1 
ATOM   4013 C  CB   B VAL   B 1 3   ? 47.643 -12.474 -17.645 0.50 21.35 ?  3   VAL   B CB   1 
ATOM   4014 C  CG1  A VAL   B 1 3   ? 48.986 -11.804 -17.785 0.50 21.80 ?  3   VAL   B CG1  1 
ATOM   4015 C  CG1  B VAL   B 1 3   ? 48.919 -11.646 -17.538 0.50 21.66 ?  3   VAL   B CG1  1 
ATOM   4016 C  CG2  A VAL   B 1 3   ? 46.589 -11.910 -18.527 0.50 22.12 ?  3   VAL   B CG2  1 
ATOM   4017 C  CG2  B VAL   B 1 3   ? 46.509 -11.661 -18.253 0.50 21.71 ?  3   VAL   B CG2  1 
ATOM   4018 H  H    A VAL   B 1 3   ? 47.774 -13.498 -20.521 0.50 25.80 ?  3   VAL   B H    1 
ATOM   4019 H  H    B VAL   B 1 3   ? 47.749 -13.132 -20.319 0.50 26.18 ?  3   VAL   B H    1 
ATOM   4020 H  HA   A VAL   B 1 3   ? 48.739 -14.449 -18.173 0.50 24.13 ?  3   VAL   B HA   1 
ATOM   4021 H  HA   B VAL   B 1 3   ? 48.577 -14.270 -17.999 0.50 24.63 ?  3   VAL   B HA   1 
ATOM   4022 H  HB   A VAL   B 1 3   ? 47.462 -12.893 -16.961 0.50 25.72 ?  3   VAL   B HB   1 
ATOM   4023 H  HB   B VAL   B 1 3   ? 47.380 -12.722 -16.745 0.50 25.65 ?  3   VAL   B HB   1 
ATOM   4024 H  HG11 A VAL   B 1 3   ? 48.780 -10.999 -17.285 0.50 26.20 ?  3   VAL   B HG11 1 
ATOM   4025 H  HG11 B VAL   B 1 3   ? 48.737 -10.853 -17.009 0.50 26.03 ?  3   VAL   B HG11 1 
ATOM   4026 H  HG12 A VAL   B 1 3   ? 49.686 -12.304 -17.334 0.50 26.20 ?  3   VAL   B HG12 1 
ATOM   4027 H  HG12 B VAL   B 1 3   ? 49.606 -12.180 -17.108 0.50 26.03 ?  3   VAL   B HG12 1 
ATOM   4028 H  HG13 A VAL   B 1 3   ? 49.269 -11.574 -18.682 0.50 26.20 ?  3   VAL   B HG13 1 
ATOM   4029 H  HG13 B VAL   B 1 3   ? 49.206 -11.392 -18.428 0.50 26.03 ?  3   VAL   B HG13 1 
ATOM   4030 H  HG21 A VAL   B 1 3   ? 46.515 -11.036 -18.115 0.50 26.58 ?  3   VAL   B HG21 1 
ATOM   4031 H  HG21 B VAL   B 1 3   ? 46.485 -10.788 -17.832 0.50 26.08 ?  3   VAL   B HG21 1 
ATOM   4032 H  HG22 A VAL   B 1 3   ? 46.778 -11.814 -19.473 0.50 26.58 ?  3   VAL   B HG22 1 
ATOM   4033 H  HG22 B VAL   B 1 3   ? 46.663 -11.567 -19.205 0.50 26.08 ?  3   VAL   B HG22 1 
ATOM   4034 H  HG23 A VAL   B 1 3   ? 45.764 -12.405 -18.403 0.50 26.58 ?  3   VAL   B HG23 1 
ATOM   4035 H  HG23 B VAL   B 1 3   ? 45.670 -12.125 -18.098 0.50 26.08 ?  3   VAL   B HG23 1 
ATOM   4036 N  N    . ASN   B 1 4   ? 46.516 -15.499 -17.512 1.00 17.00 ?  4   ASN   B N    1 
ATOM   4037 C  CA   . ASN   B 1 4   ? 45.385 -16.421 -17.399 1.00 16.09 ?  4   ASN   B CA   1 
ATOM   4038 C  C    . ASN   B 1 4   ? 45.335 -17.386 -18.584 1.00 16.22 ?  4   ASN   B C    1 
ATOM   4039 O  O    . ASN   B 1 4   ? 44.274 -17.654 -19.146 1.00 17.00 ?  4   ASN   B O    1 
ATOM   4040 C  CB   . ASN   B 1 4   ? 44.054 -15.681 -17.230 1.00 15.58 ?  4   ASN   B CB   1 
ATOM   4041 C  CG   . ASN   B 1 4   ? 44.010 -14.852 -15.959 1.00 14.75 ?  4   ASN   B CG   1 
ATOM   4042 O  OD1  . ASN   B 1 4   ? 44.296 -15.352 -14.875 1.00 14.34 ?  4   ASN   B OD1  1 
ATOM   4043 N  ND2  . ASN   B 1 4   ? 43.652 -13.581 -16.088 1.00 15.64 ?  4   ASN   B ND2  1 
ATOM   4044 H  H    A ASN   B 1 4   ? 46.960 -15.396 -16.784 0.50 20.43 ?  4   ASN   B H    1 
ATOM   4045 H  H    B ASN   B 1 4   ? 47.087 -15.579 -16.876 0.50 20.43 ?  4   ASN   B H    1 
ATOM   4046 H  HA   . ASN   B 1 4   ? 45.519 -16.955 -16.599 1.00 19.34 ?  4   ASN   B HA   1 
ATOM   4047 H  HB2  . ASN   B 1 4   ? 43.918 -15.091 -17.982 1.00 18.73 ?  4   ASN   B HB2  1 
ATOM   4048 H  HB3  . ASN   B 1 4   ? 43.335 -16.337 -17.188 1.00 18.73 ?  4   ASN   B HB3  1 
ATOM   4049 H  HD21 . ASN   B 1 4   ? 43.611 -13.070 -15.395 1.00 18.81 ?  4   ASN   B HD21 1 
ATOM   4050 H  HD22 . ASN   B 1 4   ? 43.456 -13.263 -16.864 1.00 18.81 ?  4   ASN   B HD22 1 
ATOM   4051 N  N    . SER   B 1 5   ? 46.497 -17.915 -18.966 1.00 16.90 ?  5   SER   B N    1 
ATOM   4052 C  CA   . SER   B 1 5   ? 46.599 -18.827 -20.107 1.00 19.17 ?  5   SER   B CA   1 
ATOM   4053 C  C    . SER   B 1 5   ? 46.577 -20.265 -19.600 1.00 20.54 ?  5   SER   B C    1 
ATOM   4054 O  O    . SER   B 1 5   ? 47.573 -20.982 -19.608 1.00 23.00 ?  5   SER   B O    1 
ATOM   4055 C  CB   . SER   B 1 5   ? 47.858 -18.531 -20.919 1.00 20.57 ?  5   SER   B CB   1 
ATOM   4056 O  OG   . SER   B 1 5   ? 49.033 -18.737 -20.153 1.00 23.43 ?  5   SER   B OG   1 
ATOM   4057 H  H    . SER   B 1 5   ? 47.254 -17.758 -18.580 1.00 20.32 ?  5   SER   B H    1 
ATOM   4058 H  HA   . SER   B 1 5   ? 45.832 -18.701 -20.682 1.00 23.04 ?  5   SER   B HA   1 
ATOM   4059 H  HB2  . SER   B 1 5   ? 47.875 -19.116 -21.695 1.00 24.72 ?  5   SER   B HB2  1 
ATOM   4060 H  HB3  . SER   B 1 5   ? 47.818 -17.607 -21.208 1.00 24.72 ?  5   SER   B HB3  1 
ATOM   4061 H  HG   . SER   B 1 5   ? 49.082 -19.541 -19.918 1.00 28.15 ?  5   SER   B HG   1 
ATOM   4062 N  N    . PHE   B 1 6   ? 45.400 -20.664 -19.132 1.00 20.56 ?  6   PHE   B N    1 
ATOM   4063 C  CA   . PHE   B 1 6   ? 45.190 -22.014 -18.631 1.00 20.10 ?  6   PHE   B CA   1 
ATOM   4064 C  C    . PHE   B 1 6   ? 45.104 -22.985 -19.797 1.00 23.19 ?  6   PHE   B C    1 
ATOM   4065 O  O    . PHE   B 1 6   ? 44.451 -22.702 -20.805 1.00 25.16 ?  6   PHE   B O    1 
ATOM   4066 C  CB   . PHE   B 1 6   ? 43.896 -22.065 -17.820 1.00 18.44 ?  6   PHE   B CB   1 
ATOM   4067 C  CG   . PHE   B 1 6   ? 43.918 -21.205 -16.586 1.00 16.81 ?  6   PHE   B CG   1 
ATOM   4068 C  CD1  . PHE   B 1 6   ? 44.432 -21.699 -15.403 1.00 15.60 ?  6   PHE   B CD1  1 
ATOM   4069 C  CD2  . PHE   B 1 6   ? 43.424 -19.909 -16.612 1.00 16.34 ?  6   PHE   B CD2  1 
ATOM   4070 C  CE1  . PHE   B 1 6   ? 44.447 -20.915 -14.258 1.00 15.12 ?  6   PHE   B CE1  1 
ATOM   4071 C  CE2  . PHE   B 1 6   ? 43.442 -19.116 -15.477 1.00 16.63 ?  6   PHE   B CE2  1 
ATOM   4072 C  CZ   . PHE   B 1 6   ? 43.961 -19.613 -14.301 1.00 15.66 ?  6   PHE   B CZ   1 
ATOM   4073 H  H    . PHE   B 1 6   ? 44.698 -20.169 -19.098 1.00 24.71 ?  6   PHE   B H    1 
ATOM   4074 H  HA   . PHE   B 1 6   ? 45.927 -22.274 -18.059 1.00 24.15 ?  6   PHE   B HA   1 
ATOM   4075 H  HB2  . PHE   B 1 6   ? 43.162 -21.762 -18.379 1.00 22.16 ?  6   PHE   B HB2  1 
ATOM   4076 H  HB3  . PHE   B 1 6   ? 43.736 -22.981 -17.541 1.00 22.16 ?  6   PHE   B HB3  1 
ATOM   4077 H  HD1  . PHE   B 1 6   ? 44.770 -22.566 -15.369 1.00 18.76 ?  6   PHE   B HD1  1 
ATOM   4078 H  HD2  . PHE   B 1 6   ? 43.071 -19.570 -17.402 1.00 19.64 ?  6   PHE   B HD2  1 
ATOM   4079 H  HE1  . PHE   B 1 6   ? 44.807 -21.248 -13.465 1.00 18.18 ?  6   PHE   B HE1  1 
ATOM   4080 H  HE2  . PHE   B 1 6   ? 43.104 -18.249 -15.507 1.00 19.99 ?  6   PHE   B HE2  1 
ATOM   4081 H  HZ   . PHE   B 1 6   ? 43.972 -19.087 -13.536 1.00 18.83 ?  6   PHE   B HZ   1 
ATOM   4082 N  N    . SER   B 1 7   ? 45.780 -24.127 -19.662 1.00 24.03 ?  7   SER   B N    1 
ATOM   4083 C  CA   . SER   B 1 7   ? 45.861 -25.108 -20.734 1.00 26.65 ?  7   SER   B CA   1 
ATOM   4084 C  C    . SER   B 1 7   ? 45.803 -26.518 -20.165 1.00 26.00 ?  7   SER   B C    1 
ATOM   4085 O  O    . SER   B 1 7   ? 46.398 -26.806 -19.123 1.00 27.14 ?  7   SER   B O    1 
ATOM   4086 C  CB   . SER   B 1 7   ? 47.159 -24.935 -21.534 1.00 29.40 ?  7   SER   B CB   1 
ATOM   4087 O  OG   . SER   B 1 7   ? 47.146 -25.730 -22.705 1.00 31.64 ?  7   SER   B OG   1 
ATOM   4088 H  H    . SER   B 1 7   ? 46.211 -24.353 -18.949 1.00 28.87 ?  7   SER   B H    1 
ATOM   4089 H  HA   . SER   B 1 7   ? 45.113 -24.993 -21.336 1.00 32.01 ?  7   SER   B HA   1 
ATOM   4090 H  HB2  . SER   B 1 7   ? 47.252 -24.002 -21.786 1.00 35.31 ?  7   SER   B HB2  1 
ATOM   4091 H  HB3  . SER   B 1 7   ? 47.911 -25.202 -20.981 1.00 35.31 ?  7   SER   B HB3  1 
ATOM   4092 H  HG   . SER   B 1 7   ? 47.862 -25.623 -23.134 1.00 38.00 ?  7   SER   B HG   1 
ATOM   4093 N  N    . GLY   B 1 8   ? 45.086 -27.396 -20.864 1.00 25.94 ?  8   GLY   B N    1 
ATOM   4094 C  CA   . GLY   B 1 8   ? 45.044 -28.794 -20.496 1.00 25.32 ?  8   GLY   B CA   1 
ATOM   4095 C  C    . GLY   B 1 8   ? 44.116 -29.127 -19.356 1.00 23.83 ?  8   GLY   B C    1 
ATOM   4096 O  O    . GLY   B 1 8   ? 44.265 -30.193 -18.744 1.00 25.20 ?  8   GLY   B O    1 
ATOM   4097 H  H    . GLY   B 1 8   ? 44.620 -27.196 -21.556 1.00 31.16 ?  8   GLY   B H    1 
ATOM   4098 H  HA2  . GLY   B 1 8   ? 44.761 -29.310 -21.266 1.00 30.42 ?  8   GLY   B HA2  1 
ATOM   4099 H  HA3  . GLY   B 1 8   ? 45.931 -29.083 -20.245 1.00 30.42 ?  8   GLY   B HA3  1 
ATOM   4100 N  N    . TYR   B 1 9   ? 43.143 -28.269 -19.062 1.00 21.78 ?  9   TYR   B N    1 
ATOM   4101 C  CA   . TYR   B 1 9   ? 42.194 -28.546 -17.997 1.00 19.68 ?  9   TYR   B CA   1 
ATOM   4102 C  C    . TYR   B 1 9   ? 41.008 -29.336 -18.516 1.00 19.20 ?  9   TYR   B C    1 
ATOM   4103 O  O    . TYR   B 1 9   ? 40.589 -29.194 -19.668 1.00 21.17 ?  9   TYR   B O    1 
ATOM   4104 C  CB   . TYR   B 1 9   ? 41.693 -27.257 -17.348 1.00 19.12 ?  9   TYR   B CB   1 
ATOM   4105 C  CG   . TYR   B 1 9   ? 42.722 -26.634 -16.432 1.00 18.65 ?  9   TYR   B CG   1 
ATOM   4106 C  CD1  . TYR   B 1 9   ? 43.825 -25.973 -16.949 1.00 19.19 ?  9   TYR   B CD1  1 
ATOM   4107 C  CD2  . TYR   B 1 9   ? 42.603 -26.728 -15.054 1.00 17.61 ?  9   TYR   B CD2  1 
ATOM   4108 C  CE1  . TYR   B 1 9   ? 44.779 -25.421 -16.119 1.00 19.41 ?  9   TYR   B CE1  1 
ATOM   4109 C  CE2  . TYR   B 1 9   ? 43.551 -26.181 -14.215 1.00 17.87 ?  9   TYR   B CE2  1 
ATOM   4110 C  CZ   . TYR   B 1 9   ? 44.639 -25.523 -14.753 1.00 19.10 ?  9   TYR   B CZ   1 
ATOM   4111 O  OH   . TYR   B 1 9   ? 45.592 -24.978 -13.927 1.00 19.82 ?  9   TYR   B OH   1 
ATOM   4112 H  H    . TYR   B 1 9   ? 42.996 -27.530 -19.478 1.00 26.17 ?  9   TYR   B H    1 
ATOM   4113 H  HA   . TYR   B 1 9   ? 42.623 -29.073 -17.313 1.00 23.65 ?  9   TYR   B HA   1 
ATOM   4114 H  HB2  . TYR   B 1 9   ? 41.468 -26.607 -18.035 1.00 22.98 ?  9   TYR   B HB2  1 
ATOM   4115 H  HB3  . TYR   B 1 9   ? 40.911 -27.464 -16.817 1.00 22.98 ?  9   TYR   B HB3  1 
ATOM   4116 H  HD1  . TYR   B 1 9   ? 43.922 -25.905 -17.872 1.00 23.06 ?  9   TYR   B HD1  1 
ATOM   4117 H  HD2  . TYR   B 1 9   ? 41.867 -27.177 -14.688 1.00 21.16 ?  9   TYR   B HD2  1 
ATOM   4118 H  HE1  . TYR   B 1 9   ? 45.508 -24.981 -16.481 1.00 23.33 ?  9   TYR   B HE1  1 
ATOM   4119 H  HE2  . TYR   B 1 9   ? 43.448 -26.256 -13.292 1.00 21.48 ?  9   TYR   B HE2  1 
ATOM   4120 H  HH   . TYR   B 1 9   ? 46.184 -24.612 -14.390 1.00 23.82 ?  9   TYR   B HH   1 
ATOM   4121 N  N    . LEU   B 1 10  ? 40.481 -30.190 -17.644 1.00 17.44 ?  10  LEU   B N    1 
ATOM   4122 C  CA   . LEU   B 1 10  ? 39.271 -30.945 -17.907 1.00 17.43 ?  10  LEU   B CA   1 
ATOM   4123 C  C    . LEU   B 1 10  ? 38.089 -30.173 -17.338 1.00 16.99 ?  10  LEU   B C    1 
ATOM   4124 O  O    . LEU   B 1 10  ? 38.105 -29.766 -16.173 1.00 16.50 ?  10  LEU   B O    1 
ATOM   4125 C  CB   . LEU   B 1 10  ? 39.377 -32.313 -17.235 1.00 18.34 ?  10  LEU   B CB   1 
ATOM   4126 C  CG   . LEU   B 1 10  ? 38.241 -33.274 -17.564 1.00 20.01 ?  10  LEU   B CG   1 
ATOM   4127 C  CD1  . LEU   B 1 10  ? 38.394 -33.815 -18.981 1.00 21.31 ?  10  LEU   B CD1  1 
ATOM   4128 C  CD2  . LEU   B 1 10  ? 38.168 -34.401 -16.547 1.00 21.41 ?  10  LEU   B CD2  1 
ATOM   4129 H  H    . LEU   B 1 10  ? 40.815 -30.348 -16.863 1.00 20.96 ?  10  LEU   B H    1 
ATOM   4130 H  HA   . LEU   B 1 10  ? 39.146 -31.068 -18.857 1.00 20.95 ?  10  LEU   B HA   1 
ATOM   4131 H  HB2  . LEU   B 1 10  ? 40.207 -32.734 -17.512 1.00 22.04 ?  10  LEU   B HB2  1 
ATOM   4132 H  HB3  . LEU   B 1 10  ? 39.386 -32.191 -16.269 1.00 22.04 ?  10  LEU   B HB3  1 
ATOM   4133 H  HG   . LEU   B 1 10  ? 37.402 -32.791 -17.523 1.00 24.05 ?  10  LEU   B HG   1 
ATOM   4134 H  HD11 . LEU   B 1 10  ? 37.684 -34.453 -19.151 1.00 25.60 ?  10  LEU   B HD11 1 
ATOM   4135 H  HD12 . LEU   B 1 10  ? 38.332 -33.076 -19.606 1.00 25.60 ?  10  LEU   B HD12 1 
ATOM   4136 H  HD13 . LEU   B 1 10  ? 39.257 -34.248 -19.060 1.00 25.60 ?  10  LEU   B HD13 1 
ATOM   4137 H  HD21 . LEU   B 1 10  ? 37.440 -34.993 -16.790 1.00 25.73 ?  10  LEU   B HD21 1 
ATOM   4138 H  HD22 . LEU   B 1 10  ? 39.007 -34.881 -16.550 1.00 25.73 ?  10  LEU   B HD22 1 
ATOM   4139 H  HD23 . LEU   B 1 10  ? 38.005 -34.017 -15.670 1.00 25.73 ?  10  LEU   B HD23 1 
ATOM   4140 N  N    . LYS   B 1 11  ? 37.061 -29.991 -18.158 1.00 18.17 ?  11  LYS   B N    1 
ATOM   4141 C  CA   . LYS   B 1 11  ? 35.869 -29.268 -17.744 1.00 19.95 ?  11  LYS   B CA   1 
ATOM   4142 C  C    . LYS   B 1 11  ? 34.977 -30.195 -16.922 1.00 19.26 ?  11  LYS   B C    1 
ATOM   4143 O  O    . LYS   B 1 11  ? 34.576 -31.264 -17.396 1.00 21.02 ?  11  LYS   B O    1 
ATOM   4144 C  CB   . LYS   B 1 11  ? 35.139 -28.773 -18.991 1.00 23.74 ?  11  LYS   B CB   1 
ATOM   4145 C  CG   . LYS   B 1 11  ? 33.988 -27.818 -18.738 1.00 27.29 ?  11  LYS   B CG   1 
ATOM   4146 C  CD   . LYS   B 1 11  ? 33.264 -27.503 -20.045 1.00 30.32 ?  11  LYS   B CD   1 
ATOM   4147 C  CE   . LYS   B 1 11  ? 32.219 -26.416 -19.869 1.00 32.60 ?  11  LYS   B CE   1 
ATOM   4148 N  NZ   . LYS   B 1 11  ? 32.842 -25.088 -19.630 1.00 33.97 ?  11  LYS   B NZ   1 
ATOM   4149 H  H    . LYS   B 1 11  ? 37.021 -30.295 -18.962 1.00 21.84 ?  11  LYS   B H    1 
ATOM   4150 H  HA   . LYS   B 1 11  ? 36.117 -28.507 -17.199 1.00 23.97 ?  11  LYS   B HA   1 
ATOM   4151 H  HB2  . LYS   B 1 11  ? 35.779 -28.310 -19.557 1.00 28.52 ?  11  LYS   B HB2  1 
ATOM   4152 H  HB3  . LYS   B 1 11  ? 34.783 -29.539 -19.467 1.00 28.52 ?  11  LYS   B HB3  1 
ATOM   4153 H  HG2  . LYS   B 1 11  ? 33.354 -28.228 -18.130 1.00 32.78 ?  11  LYS   B HG2  1 
ATOM   4154 H  HG3  . LYS   B 1 11  ? 34.328 -26.989 -18.369 1.00 32.78 ?  11  LYS   B HG3  1 
ATOM   4155 H  HD2  . LYS   B 1 11  ? 33.911 -27.199 -20.702 1.00 36.42 ?  11  LYS   B HD2  1 
ATOM   4156 H  HD3  . LYS   B 1 11  ? 32.818 -28.304 -20.364 1.00 36.42 ?  11  LYS   B HD3  1 
ATOM   4157 H  HE2  . LYS   B 1 11  ? 31.680 -26.358 -20.673 1.00 39.16 ?  11  LYS   B HE2  1 
ATOM   4158 H  HE3  . LYS   B 1 11  ? 31.661 -26.634 -19.107 1.00 39.16 ?  11  LYS   B HE3  1 
ATOM   4159 H  HZ1  . LYS   B 1 11  ? 32.210 -24.466 -19.548 1.00 40.80 ?  11  LYS   B HZ1  1 
ATOM   4160 H  HZ2  . LYS   B 1 11  ? 33.326 -25.108 -18.884 1.00 40.80 ?  11  LYS   B HZ2  1 
ATOM   4161 H  HZ3  . LYS   B 1 11  ? 33.371 -24.872 -20.313 1.00 40.80 ?  11  LYS   B HZ3  1 
ATOM   4162 N  N    . LEU   B 1 12  ? 34.662 -29.786 -15.694 1.00 17.67 ?  12  LEU   B N    1 
ATOM   4163 C  CA   . LEU   B 1 12  ? 33.698 -30.490 -14.855 1.00 17.38 ?  12  LEU   B CA   1 
ATOM   4164 C  C    . LEU   B 1 12  ? 32.306 -29.882 -14.951 1.00 17.47 ?  12  LEU   B C    1 
ATOM   4165 O  O    . LEU   B 1 12  ? 31.321 -30.596 -15.131 1.00 17.95 ?  12  LEU   B O    1 
ATOM   4166 C  CB   . LEU   B 1 12  ? 34.163 -30.505 -13.395 1.00 16.86 ?  12  LEU   B CB   1 
ATOM   4167 C  CG   . LEU   B 1 12  ? 35.500 -31.196 -13.135 1.00 16.81 ?  12  LEU   B CG   1 
ATOM   4168 C  CD1  . LEU   B 1 12  ? 35.846 -31.166 -11.656 1.00 17.06 ?  12  LEU   B CD1  1 
ATOM   4169 C  CD2  . LEU   B 1 12  ? 35.490 -32.625 -13.660 1.00 17.67 ?  12  LEU   B CD2  1 
ATOM   4170 H  H    . LEU   B 1 12  ? 35.002 -29.092 -15.320 1.00 21.24 ?  12  LEU   B H    1 
ATOM   4171 H  HA   . LEU   B 1 12  ? 33.632 -31.408 -15.158 1.00 20.89 ?  12  LEU   B HA   1 
ATOM   4172 H  HB2  . LEU   B 1 12  ? 34.244 -29.588 -13.090 1.00 20.26 ?  12  LEU   B HB2  1 
ATOM   4173 H  HB3  . LEU   B 1 12  ? 33.492 -30.964 -12.865 1.00 20.26 ?  12  LEU   B HB3  1 
ATOM   4174 H  HG   . LEU   B 1 12  ? 36.195 -30.711 -13.609 1.00 20.21 ?  12  LEU   B HG   1 
ATOM   4175 H  HD11 . LEU   B 1 12  ? 36.703 -31.607 -11.523 1.00 20.51 ?  12  LEU   B HD11 1 
ATOM   4176 H  HD12 . LEU   B 1 12  ? 35.903 -30.244 -11.360 1.00 20.51 ?  12  LEU   B HD12 1 
ATOM   4177 H  HD13 . LEU   B 1 12  ? 35.157 -31.632 -11.158 1.00 20.51 ?  12  LEU   B HD13 1 
ATOM   4178 H  HD21 . LEU   B 1 12  ? 36.279 -33.085 -13.337 1.00 21.23 ?  12  LEU   B HD21 1 
ATOM   4179 H  HD22 . LEU   B 1 12  ? 34.690 -33.071 -13.344 1.00 21.23 ?  12  LEU   B HD22 1 
ATOM   4180 H  HD23 . LEU   B 1 12  ? 35.495 -32.604 -14.632 1.00 21.23 ?  12  LEU   B HD23 1 
ATOM   4181 N  N    . THR   B 1 13  ? 32.216 -28.565 -14.834 1.00 17.40 ?  13  THR   B N    1 
ATOM   4182 C  CA   . THR   B 1 13  ? 30.989 -27.812 -15.028 1.00 17.46 ?  13  THR   B CA   1 
ATOM   4183 C  C    . THR   B 1 13  ? 31.324 -26.609 -15.902 1.00 19.37 ?  13  THR   B C    1 
ATOM   4184 O  O    . THR   B 1 13  ? 32.470 -26.416 -16.324 1.00 19.86 ?  13  THR   B O    1 
ATOM   4185 C  CB   . THR   B 1 13  ? 30.397 -27.347 -13.693 1.00 17.30 ?  13  THR   B CB   1 
ATOM   4186 O  OG1  . THR   B 1 13  ? 31.241 -26.327 -13.143 1.00 16.78 ?  13  THR   B OG1  1 
ATOM   4187 C  CG2  . THR   B 1 13  ? 30.291 -28.504 -12.709 1.00 17.82 ?  13  THR   B CG2  1 
ATOM   4188 H  H    . THR   B 1 13  ? 32.885 -28.062 -14.636 1.00 20.92 ?  13  THR   B H    1 
ATOM   4189 H  HA   . THR   B 1 13  ? 30.331 -28.364 -15.480 1.00 20.98 ?  13  THR   B HA   1 
ATOM   4190 H  HB   . THR   B 1 13  ? 29.503 -26.986 -13.838 1.00 20.79 ?  13  THR   B HB   1 
ATOM   4191 H  HG1  . THR   B 1 13  ? 30.937 -25.565 -13.347 1.00 20.17 ?  13  THR   B HG1  1 
ATOM   4192 H  HG21 . THR   B 1 13  ? 29.789 -28.231 -11.924 1.00 21.42 ?  13  THR   B HG21 1 
ATOM   4193 H  HG22 . THR   B 1 13  ? 29.834 -29.253 -13.126 1.00 21.42 ?  13  THR   B HG22 1 
ATOM   4194 H  HG23 . THR   B 1 13  ? 31.175 -28.789 -12.434 1.00 21.42 ?  13  THR   B HG23 1 
ATOM   4195 N  N    A ASP   B 1 14  ? 30.312 -25.782 -16.164 0.50 20.31 ?  14  ASP   B N    1 
ATOM   4196 N  N    B ASP   B 1 14  ? 30.317 -25.774 -16.164 0.50 20.21 ?  14  ASP   B N    1 
ATOM   4197 C  CA   A ASP   B 1 14  ? 30.528 -24.617 -17.013 0.50 21.45 ?  14  ASP   B CA   1 
ATOM   4198 C  CA   B ASP   B 1 14  ? 30.529 -24.614 -17.024 0.50 21.22 ?  14  ASP   B CA   1 
ATOM   4199 C  C    A ASP   B 1 14  ? 31.640 -23.725 -16.478 0.50 19.72 ?  14  ASP   B C    1 
ATOM   4200 C  C    B ASP   B 1 14  ? 31.543 -23.631 -16.457 0.50 19.59 ?  14  ASP   B C    1 
ATOM   4201 O  O    A ASP   B 1 14  ? 32.337 -23.070 -17.264 0.50 20.65 ?  14  ASP   B O    1 
ATOM   4202 O  O    B ASP   B 1 14  ? 32.032 -22.776 -17.203 0.50 20.42 ?  14  ASP   B O    1 
ATOM   4203 C  CB   A ASP   B 1 14  ? 29.224 -23.832 -17.172 0.50 24.56 ?  14  ASP   B CB   1 
ATOM   4204 C  CB   B ASP   B 1 14  ? 29.212 -23.882 -17.273 0.50 24.18 ?  14  ASP   B CB   1 
ATOM   4205 C  CG   A ASP   B 1 14  ? 28.228 -24.524 -18.075 0.50 27.40 ?  14  ASP   B CG   1 
ATOM   4206 C  CG   B ASP   B 1 14  ? 28.345 -24.588 -18.295 0.50 26.91 ?  14  ASP   B CG   1 
ATOM   4207 O  OD1  A ASP   B 1 14  ? 28.543 -25.609 -18.612 0.50 28.18 ?  14  ASP   B OD1  1 
ATOM   4208 O  OD1  B ASP   B 1 14  ? 28.911 -25.230 -19.206 0.50 27.65 ?  14  ASP   B OD1  1 
ATOM   4209 O  OD2  A ASP   B 1 14  ? 27.120 -23.973 -18.244 0.50 28.64 -1 14  ASP   B OD2  1 
ATOM   4210 O  OD2  B ASP   B 1 14  ? 27.104 -24.507 -18.191 0.50 28.07 -1 14  ASP   B OD2  1 
ATOM   4211 H  H    A ASP   B 1 14  ? 29.512 -25.864 -15.857 0.50 24.41 ?  14  ASP   B H    1 
ATOM   4212 H  H    B ASP   B 1 14  ? 29.515 -25.856 -15.861 0.50 24.29 ?  14  ASP   B H    1 
ATOM   4213 H  HA   A ASP   B 1 14  ? 30.801 -24.912 -17.890 0.50 25.77 ?  14  ASP   B HA   1 
ATOM   4214 H  HA   B ASP   B 1 14  ? 30.858 -24.923 -17.881 0.50 25.49 ?  14  ASP   B HA   1 
ATOM   4215 H  HB2  A ASP   B 1 14  ? 28.794 -23.738 -16.312 0.50 29.50 ?  14  ASP   B HB2  1 
ATOM   4216 H  HB2  B ASP   B 1 14  ? 28.722 -23.819 -16.437 0.50 29.05 ?  14  ASP   B HB2  1 
ATOM   4217 H  HB3  A ASP   B 1 14  ? 29.414 -22.962 -17.553 0.50 29.50 ?  14  ASP   B HB3  1 
ATOM   4218 H  HB3  B ASP   B 1 14  ? 29.409 -22.987 -17.605 0.50 29.05 ?  14  ASP   B HB3  1 
ATOM   4219 N  N    . ASN   B 1 15  ? 31.846 -23.704 -15.159 1.00 17.44 ?  15  ASN   B N    1 
ATOM   4220 C  CA   . ASN   B 1 15  ? 32.810 -22.789 -14.553 1.00 15.08 ?  15  ASN   B CA   1 
ATOM   4221 C  C    . ASN   B 1 15  ? 33.907 -23.448 -13.724 1.00 13.91 ?  15  ASN   B C    1 
ATOM   4222 O  O    . ASN   B 1 15  ? 34.760 -22.724 -13.201 1.00 14.39 ?  15  ASN   B O    1 
ATOM   4223 C  CB   . ASN   B 1 15  ? 32.100 -21.735 -13.686 1.00 15.35 ?  15  ASN   B CB   1 
ATOM   4224 C  CG   . ASN   B 1 15  ? 31.473 -22.337 -12.449 1.00 15.05 ?  15  ASN   B CG   1 
ATOM   4225 O  OD1  . ASN   B 1 15  ? 30.530 -23.131 -12.542 1.00 16.81 ?  15  ASN   B OD1  1 
ATOM   4226 N  ND2  . ASN   B 1 15  ? 31.992 -21.987 -11.285 1.00 14.40 ?  15  ASN   B ND2  1 
ATOM   4227 H  H    A ASN   B 1 15  ? 31.442 -24.216 -14.596 0.50 20.96 ?  15  ASN   B H    1 
ATOM   4228 H  H    B ASN   B 1 15  ? 31.478 -24.249 -14.604 0.50 20.96 ?  15  ASN   B H    1 
ATOM   4229 H  HA   . ASN   B 1 15  ? 33.254 -22.303 -15.257 1.00 18.13 ?  15  ASN   B HA   1 
ATOM   4230 H  HB2  . ASN   B 1 15  ? 32.748 -21.064 -13.403 1.00 18.45 ?  15  ASN   B HB2  1 
ATOM   4231 H  HB3  . ASN   B 1 15  ? 31.396 -21.308 -14.203 1.00 18.45 ?  15  ASN   B HB3  1 
ATOM   4232 H  HD21 . ASN   B 1 15  ? 31.669 -22.301 -10.550 1.00 17.31 ?  15  ASN   B HD21 1 
ATOM   4233 H  HD22 . ASN   B 1 15  ? 32.655 -21.432 -11.251 1.00 17.31 ?  15  ASN   B HD22 1 
ATOM   4234 N  N    . VAL   B 1 16  ? 33.917 -24.771 -13.576 1.00 13.99 ?  16  VAL   B N    1 
ATOM   4235 C  CA   . VAL   B 1 16  ? 34.917 -25.462 -12.767 1.00 13.87 ?  16  VAL   B CA   1 
ATOM   4236 C  C    . VAL   B 1 16  ? 35.711 -26.402 -13.661 1.00 13.85 ?  16  VAL   B C    1 
ATOM   4237 O  O    . VAL   B 1 16  ? 35.133 -27.284 -14.320 1.00 15.02 ?  16  VAL   B O    1 
ATOM   4238 C  CB   . VAL   B 1 16  ? 34.291 -26.229 -11.592 1.00 14.23 ?  16  VAL   B CB   1 
ATOM   4239 C  CG1  . VAL   B 1 16  ? 35.375 -26.963 -10.795 1.00 14.36 ?  16  VAL   B CG1  1 
ATOM   4240 C  CG2  . VAL   B 1 16  ? 33.496 -25.291 -10.695 1.00 14.97 ?  16  VAL   B CG2  1 
ATOM   4241 H  H    . VAL   B 1 16  ? 33.336 -25.300 -13.932 1.00 16.82 ?  16  VAL   B H    1 
ATOM   4242 H  HA   . VAL   B 1 16  ? 35.530 -24.806 -12.398 1.00 16.68 ?  16  VAL   B HA   1 
ATOM   4243 H  HB   . VAL   B 1 16  ? 33.680 -26.897 -11.941 1.00 17.11 ?  16  VAL   B HB   1 
ATOM   4244 H  HG11 . VAL   B 1 16  ? 34.996 -27.264 -9.953  1.00 17.26 ?  16  VAL   B HG11 1 
ATOM   4245 H  HG12 . VAL   B 1 16  ? 35.690 -27.722 -11.306 1.00 17.26 ?  16  VAL   B HG12 1 
ATOM   4246 H  HG13 . VAL   B 1 16  ? 36.107 -26.348 -10.622 1.00 17.26 ?  16  VAL   B HG13 1 
ATOM   4247 H  HG21 . VAL   B 1 16  ? 33.157 -25.790 -9.935  1.00 18.00 ?  16  VAL   B HG21 1 
ATOM   4248 H  HG22 . VAL   B 1 16  ? 34.077 -24.578 -10.390 1.00 18.00 ?  16  VAL   B HG22 1 
ATOM   4249 H  HG23 . VAL   B 1 16  ? 32.757 -24.921 -11.203 1.00 18.00 ?  16  VAL   B HG23 1 
ATOM   4250 N  N    . TYR   B 1 17  ? 37.037 -26.232 -13.641 1.00 14.32 ?  17  TYR   B N    1 
ATOM   4251 C  CA   . TYR   B 1 17  ? 37.982 -26.982 -14.452 1.00 14.54 ?  17  TYR   B CA   1 
ATOM   4252 C  C    . TYR   B 1 17  ? 39.031 -27.603 -13.538 1.00 13.37 ?  17  TYR   B C    1 
ATOM   4253 O  O    . TYR   B 1 17  ? 39.312 -27.077 -12.457 1.00 14.14 ?  17  TYR   B O    1 
ATOM   4254 C  CB   . TYR   B 1 17  ? 38.691 -26.057 -15.450 1.00 16.78 ?  17  TYR   B CB   1 
ATOM   4255 C  CG   . TYR   B 1 17  ? 37.770 -25.286 -16.358 1.00 19.54 ?  17  TYR   B CG   1 
ATOM   4256 C  CD1  . TYR   B 1 17  ? 37.187 -24.093 -15.947 1.00 20.72 ?  17  TYR   B CD1  1 
ATOM   4257 C  CD2  . TYR   B 1 17  ? 37.481 -25.752 -17.632 1.00 21.36 ?  17  TYR   B CD2  1 
ATOM   4258 C  CE1  . TYR   B 1 17  ? 36.342 -23.385 -16.781 1.00 22.35 ?  17  TYR   B CE1  1 
ATOM   4259 C  CE2  . TYR   B 1 17  ? 36.639 -25.052 -18.473 1.00 22.90 ?  17  TYR   B CE2  1 
ATOM   4260 C  CZ   . TYR   B 1 17  ? 36.070 -23.872 -18.042 1.00 23.45 ?  17  TYR   B CZ   1 
ATOM   4261 O  OH   . TYR   B 1 17  ? 35.231 -23.174 -18.877 1.00 25.08 ?  17  TYR   B OH   1 
ATOM   4262 H  H    . TYR   B 1 17  ? 37.432 -25.651 -13.132 1.00 17.22 ?  17  TYR   B H    1 
ATOM   4263 H  HA   . TYR   B 1 17  ? 37.523 -27.690 -14.932 1.00 17.48 ?  17  TYR   B HA   1 
ATOM   4264 H  HB2  . TYR   B 1 17  ? 39.230 -25.418 -14.962 1.00 20.17 ?  17  TYR   B HB2  1 
ATOM   4265 H  HB3  . TYR   B 1 17  ? 39.256 -26.599 -16.018 1.00 20.17 ?  17  TYR   B HB3  1 
ATOM   4266 H  HD1  . TYR   B 1 17  ? 37.371 -23.764 -15.099 1.00 24.90 ?  17  TYR   B HD1  1 
ATOM   4267 H  HD2  . TYR   B 1 17  ? 37.855 -26.547 -17.929 1.00 25.66 ?  17  TYR   B HD2  1 
ATOM   4268 H  HE1  . TYR   B 1 17  ? 35.957 -22.584 -16.496 1.00 26.86 ?  17  TYR   B HE1  1 
ATOM   4269 H  HE2  . TYR   B 1 17  ? 36.445 -25.375 -19.327 1.00 27.52 ?  17  TYR   B HE2  1 
ATOM   4270 H  HH   . TYR   B 1 17  ? 35.144 -23.573 -19.613 1.00 30.13 ?  17  TYR   B HH   1 
ATOM   4271 N  N    . ILE   B 1 18  ? 39.650 -28.701 -13.979 1.00 13.41 ?  18  ILE   B N    1 
ATOM   4272 C  CA   . ILE   B 1 18  ? 40.579 -29.430 -13.118 1.00 13.66 ?  18  ILE   B CA   1 
ATOM   4273 C  C    . ILE   B 1 18  ? 41.745 -29.976 -13.936 1.00 13.99 ?  18  ILE   B C    1 
ATOM   4274 O  O    . ILE   B 1 18  ? 41.586 -30.379 -15.092 1.00 15.17 ?  18  ILE   B O    1 
ATOM   4275 C  CB   . ILE   B 1 18  ? 39.829 -30.532 -12.322 1.00 14.17 ?  18  ILE   B CB   1 
ATOM   4276 C  CG1  . ILE   B 1 18  ? 40.685 -31.079 -11.175 1.00 14.72 ?  18  ILE   B CG1  1 
ATOM   4277 C  CG2  . ILE   B 1 18  ? 39.326 -31.643 -13.252 1.00 14.69 ?  18  ILE   B CG2  1 
ATOM   4278 C  CD1  . ILE   B 1 18  ? 39.874 -31.891 -10.172 1.00 16.36 ?  18  ILE   B CD1  1 
ATOM   4279 H  H    . ILE   B 1 18  ? 39.555 -29.040 -14.762 1.00 16.13 ?  18  ILE   B H    1 
ATOM   4280 H  HA   . ILE   B 1 18  ? 40.944 -28.813 -12.464 1.00 16.42 ?  18  ILE   B HA   1 
ATOM   4281 H  HB   . ILE   B 1 18  ? 39.046 -30.125 -11.918 1.00 17.04 ?  18  ILE   B HB   1 
ATOM   4282 H  HG12 . ILE   B 1 18  ? 41.374 -31.651 -11.535 1.00 17.70 ?  18  ILE   B HG12 1 
ATOM   4283 H  HG13 . ILE   B 1 18  ? 41.082 -30.333 -10.697 1.00 17.70 ?  18  ILE   B HG13 1 
ATOM   4284 H  HG21 . ILE   B 1 18  ? 38.739 -32.236 -12.750 1.00 17.66 ?  18  ILE   B HG21 1 
ATOM   4285 H  HG22 . ILE   B 1 18  ? 38.834 -31.240 -13.983 1.00 17.66 ?  18  ILE   B HG22 1 
ATOM   4286 H  HG23 . ILE   B 1 18  ? 40.082 -32.142 -13.592 1.00 17.66 ?  18  ILE   B HG23 1 
ATOM   4287 H  HD11 . ILE   B 1 18  ? 40.453 -32.165 -9.443  1.00 19.66 ?  18  ILE   B HD11 1 
ATOM   4288 H  HD12 . ILE   B 1 18  ? 39.149 -31.344 -9.828  1.00 19.66 ?  18  ILE   B HD12 1 
ATOM   4289 H  HD13 . ILE   B 1 18  ? 39.512 -32.675 -10.617 1.00 19.66 ?  18  ILE   B HD13 1 
ATOM   4290 N  N    . LYS   B 1 19  ? 42.927 -30.011 -13.313 1.00 14.23 ?  19  LYS   B N    1 
ATOM   4291 C  CA   . LYS   B 1 19  ? 44.138 -30.490 -13.967 1.00 15.12 ?  19  LYS   B CA   1 
ATOM   4292 C  C    . LYS   B 1 19  ? 45.039 -31.168 -12.945 1.00 15.02 ?  19  LYS   B C    1 
ATOM   4293 O  O    . LYS   B 1 19  ? 45.126 -30.729 -11.796 1.00 14.76 ?  19  LYS   B O    1 
ATOM   4294 C  CB   . LYS   B 1 19  ? 44.913 -29.329 -14.603 1.00 16.37 ?  19  LYS   B CB   1 
ATOM   4295 C  CG   . LYS   B 1 19  ? 46.116 -29.734 -15.441 1.00 18.33 ?  19  LYS   B CG   1 
ATOM   4296 C  CD   . LYS   B 1 19  ? 46.817 -28.492 -15.985 1.00 20.44 ?  19  LYS   B CD   1 
ATOM   4297 C  CE   . LYS   B 1 19  ? 47.994 -28.853 -16.868 1.00 22.39 ?  19  LYS   B CE   1 
ATOM   4298 N  NZ   . LYS   B 1 19  ? 48.715 -27.649 -17.358 1.00 23.61 ?  19  LYS   B NZ   1 
ATOM   4299 H  H    . LYS   B 1 19  ? 43.046 -29.755 -12.496 1.00 17.11 ?  19  LYS   B H    1 
ATOM   4300 H  HA   . LYS   B 1 19  ? 43.900 -31.133 -14.656 1.00 18.17 ?  19  LYS   B HA   1 
ATOM   4301 H  HB2  . LYS   B 1 19  ? 44.307 -28.839 -15.178 1.00 19.68 ?  19  LYS   B HB2  1 
ATOM   4302 H  HB3  . LYS   B 1 19  ? 45.228 -28.748 -13.891 1.00 19.68 ?  19  LYS   B HB3  1 
ATOM   4303 H  HG2  . LYS   B 1 19  ? 46.743 -30.229 -14.893 1.00 22.03 ?  19  LYS   B HG2  1 
ATOM   4304 H  HG3  . LYS   B 1 19  ? 45.818 -30.275 -16.191 1.00 22.03 ?  19  LYS   B HG3  1 
ATOM   4305 H  HD2  . LYS   B 1 19  ? 46.187 -27.974 -16.512 1.00 24.56 ?  19  LYS   B HD2  1 
ATOM   4306 H  HD3  . LYS   B 1 19  ? 47.145 -27.961 -15.242 1.00 24.56 ?  19  LYS   B HD3  1 
ATOM   4307 H  HE2  . LYS   B 1 19  ? 48.616 -29.396 -16.360 1.00 26.90 ?  19  LYS   B HE2  1 
ATOM   4308 H  HE3  . LYS   B 1 19  ? 47.671 -29.348 -17.639 1.00 26.90 ?  19  LYS   B HE3  1 
ATOM   4309 H  HZ1  . LYS   B 1 19  ? 49.351 -27.889 -17.932 1.00 28.36 ?  19  LYS   B HZ1  1 
ATOM   4310 H  HZ2  . LYS   B 1 19  ? 48.147 -27.100 -17.768 1.00 28.36 ?  19  LYS   B HZ2  1 
ATOM   4311 H  HZ3  . LYS   B 1 19  ? 49.089 -27.220 -16.675 1.00 28.36 ?  19  LYS   B HZ3  1 
ATOM   4312 N  N    . ASN   B 1 20  ? 45.724 -32.224 -13.379 1.00 16.22 ?  20  ASN   B N    1 
ATOM   4313 C  CA   . ASN   B 1 20  ? 46.760 -32.852 -12.569 1.00 17.00 ?  20  ASN   B CA   1 
ATOM   4314 C  C    . ASN   B 1 20  ? 48.032 -32.034 -12.753 1.00 17.47 ?  20  ASN   B C    1 
ATOM   4315 O  O    . ASN   B 1 20  ? 48.675 -32.109 -13.807 1.00 19.47 ?  20  ASN   B O    1 
ATOM   4316 C  CB   . ASN   B 1 20  ? 46.938 -34.303 -13.016 1.00 18.49 ?  20  ASN   B CB   1 
ATOM   4317 C  CG   . ASN   B 1 20  ? 48.099 -35.007 -12.337 1.00 19.72 ?  20  ASN   B CG   1 
ATOM   4318 O  OD1  . ASN   B 1 20  ? 48.767 -35.843 -12.954 1.00 22.13 ?  20  ASN   B OD1  1 
ATOM   4319 N  ND2  . ASN   B 1 20  ? 48.337 -34.696 -11.070 1.00 19.40 ?  20  ASN   B ND2  1 
ATOM   4320 H  H    . ASN   B 1 20  ? 45.607 -32.592 -14.145 1.00 19.50 ?  20  ASN   B H    1 
ATOM   4321 H  HA   . ASN   B 1 20  ? 46.497 -32.842 -11.634 1.00 20.43 ?  20  ASN   B HA   1 
ATOM   4322 H  HB2  . ASN   B 1 20  ? 46.131 -34.800 -12.808 1.00 22.22 ?  20  ASN   B HB2  1 
ATOM   4323 H  HB3  . ASN   B 1 20  ? 47.099 -34.318 -13.970 1.00 22.22 ?  20  ASN   B HB3  1 
ATOM   4324 H  HD21 . ASN   B 1 20  ? 48.990 -35.063 -10.650 1.00 23.31 ?  20  ASN   B HD21 1 
ATOM   4325 H  HD22 . ASN   B 1 20  ? 47.847 -34.110 -10.666 1.00 23.31 ?  20  ASN   B HD22 1 
ATOM   4326 N  N    . ALA   B 1 21  ? 48.390 -31.238 -11.744 1.00 16.96 ?  21  ALA   B N    1 
ATOM   4327 C  CA   . ALA   B 1 21  ? 49.489 -30.298 -11.896 1.00 17.87 ?  21  ALA   B CA   1 
ATOM   4328 C  C    . ALA   B 1 21  ? 49.951 -29.808 -10.532 1.00 16.71 ?  21  ALA   B C    1 
ATOM   4329 O  O    . ALA   B 1 21  ? 49.207 -29.838 -9.548  1.00 16.53 ?  21  ALA   B O    1 
ATOM   4330 C  CB   . ALA   B 1 21  ? 49.069 -29.121 -12.776 1.00 19.07 ?  21  ALA   B CB   1 
ATOM   4331 H  H    . ALA   B 1 21  ? 48.017 -31.239 -10.965 1.00 20.38 ?  21  ALA   B H    1 
ATOM   4332 H  HA   . ALA   B 1 21  ? 50.232 -30.753 -12.319 1.00 21.47 ?  21  ALA   B HA   1 
ATOM   4333 H  HB1  . ALA   B 1 21  ? 49.849 -28.585 -12.950 1.00 22.92 ?  21  ALA   B HB1  1 
ATOM   4334 H  HB2  . ALA   B 1 21  ? 48.711 -29.476 -13.605 1.00 22.92 ?  21  ALA   B HB2  1 
ATOM   4335 H  HB3  . ALA   B 1 21  ? 48.391 -28.612 -12.311 1.00 22.92 ?  21  ALA   B HB3  1 
ATOM   4336 N  N    . ASP   B 1 22  ? 51.210 -29.370 -10.507 1.00 15.95 ?  22  ASP   B N    1 
ATOM   4337 C  CA   . ASP   B 1 22  ? 51.824 -28.673 -9.380  1.00 15.17 ?  22  ASP   B CA   1 
ATOM   4338 C  C    . ASP   B 1 22  ? 51.419 -27.200 -9.460  1.00 13.95 ?  22  ASP   B C    1 
ATOM   4339 O  O    . ASP   B 1 22  ? 51.731 -26.521 -10.444 1.00 14.49 ?  22  ASP   B O    1 
ATOM   4340 C  CB   . ASP   B 1 22  ? 53.342 -28.857 -9.534  1.00 16.77 ?  22  ASP   B CB   1 
ATOM   4341 C  CG   . ASP   B 1 22  ? 54.174 -28.100 -8.502  1.00 18.51 ?  22  ASP   B CG   1 
ATOM   4342 O  OD1  . ASP   B 1 22  ? 53.806 -26.990 -8.093  1.00 18.84 ?  22  ASP   B OD1  1 
ATOM   4343 O  OD2  . ASP   B 1 22  ? 55.256 -28.612 -8.129  1.00 20.95 -1 22  ASP   B OD2  1 
ATOM   4344 H  H    . ASP   B 1 22  ? 51.757 -29.473 -11.168 1.00 19.17 ?  22  ASP   B H    1 
ATOM   4345 H  HA   . ASP   B 1 22  ? 51.533 -29.060 -8.535  1.00 18.24 ?  22  ASP   B HA   1 
ATOM   4346 H  HB2  . ASP   B 1 22  ? 53.560 -29.794 -9.456  1.00 20.15 ?  22  ASP   B HB2  1 
ATOM   4347 H  HB3  . ASP   B 1 22  ? 53.606 -28.523 -10.405 1.00 20.15 ?  22  ASP   B HB3  1 
ATOM   4348 N  N    . ILE   B 1 23  ? 50.717 -26.707 -8.432  1.00 13.63 ?  23  ILE   B N    1 
ATOM   4349 C  CA   . ILE   B 1 23  ? 50.123 -25.370 -8.496  1.00 12.91 ?  23  ILE   B CA   1 
ATOM   4350 C  C    . ILE   B 1 23  ? 51.177 -24.281 -8.637  1.00 12.54 ?  23  ILE   B C    1 
ATOM   4351 O  O    . ILE   B 1 23  ? 50.903 -23.237 -9.235  1.00 12.47 ?  23  ILE   B O    1 
ATOM   4352 C  CB   . ILE   B 1 23  ? 49.178 -25.130 -7.301  1.00 13.28 ?  23  ILE   B CB   1 
ATOM   4353 C  CG1  . ILE   B 1 23  ? 48.355 -23.854 -7.499  1.00 13.98 ?  23  ILE   B CG1  1 
ATOM   4354 C  CG2  . ILE   B 1 23  ? 49.939 -25.093 -5.994  1.00 14.46 ?  23  ILE   B CG2  1 
ATOM   4355 C  CD1  . ILE   B 1 23  ? 47.221 -23.684 -6.493  1.00 14.51 ?  23  ILE   B CD1  1 
ATOM   4356 H  H    . ILE   B 1 23  ? 50.577 -27.129 -7.695  1.00 16.39 ?  23  ILE   B H    1 
ATOM   4357 H  HA   . ILE   B 1 23  ? 49.579 -25.333 -9.293  1.00 15.52 ?  23  ILE   B HA   1 
ATOM   4358 H  HB   . ILE   B 1 23  ? 48.556 -25.875 -7.262  1.00 15.97 ?  23  ILE   B HB   1 
ATOM   4359 H  HG12 . ILE   B 1 23  ? 48.947 -23.086 -7.412  1.00 16.81 ?  23  ILE   B HG12 1 
ATOM   4360 H  HG13 . ILE   B 1 23  ? 47.968 -23.864 -8.389  1.00 16.81 ?  23  ILE   B HG13 1 
ATOM   4361 H  HG21 . ILE   B 1 23  ? 49.306 -25.086 -5.259  1.00 17.39 ?  23  ILE   B HG21 1 
ATOM   4362 H  HG22 . ILE   B 1 23  ? 50.504 -25.879 -5.936  1.00 17.39 ?  23  ILE   B HG22 1 
ATOM   4363 H  HG23 . ILE   B 1 23  ? 50.485 -24.292 -5.968  1.00 17.39 ?  23  ILE   B HG23 1 
ATOM   4364 H  HD11 . ILE   B 1 23  ? 46.707 -22.897 -6.728  1.00 17.45 ?  23  ILE   B HD11 1 
ATOM   4365 H  HD12 . ILE   B 1 23  ? 46.655 -24.472 -6.527  1.00 17.45 ?  23  ILE   B HD12 1 
ATOM   4366 H  HD13 . ILE   B 1 23  ? 47.598 -23.584 -5.607  1.00 17.45 ?  23  ILE   B HD13 1 
ATOM   4367 N  N    . VAL   B 1 24  ? 52.375 -24.482 -8.080  1.00 13.01 ?  24  VAL   B N    1 
ATOM   4368 C  CA   . VAL   B 1 24  ? 53.451 -23.502 -8.249  1.00 13.70 ?  24  VAL   B CA   1 
ATOM   4369 C  C    . VAL   B 1 24  ? 53.904 -23.452 -9.702  1.00 13.84 ?  24  VAL   B C    1 
ATOM   4370 O  O    . VAL   B 1 24  ? 54.041 -22.373 -10.295 1.00 14.34 ?  24  VAL   B O    1 
ATOM   4371 C  CB   . VAL   B 1 24  ? 54.628 -23.815 -7.303  1.00 14.62 ?  24  VAL   B CB   1 
ATOM   4372 C  CG1  . VAL   B 1 24  ? 55.834 -22.937 -7.634  1.00 14.95 ?  24  VAL   B CG1  1 
ATOM   4373 C  CG2  . VAL   B 1 24  ? 54.207 -23.635 -5.868  1.00 15.78 ?  24  VAL   B CG2  1 
ATOM   4374 H  H    . VAL   B 1 24  ? 52.586 -25.168 -7.607  1.00 15.64 ?  24  VAL   B H    1 
ATOM   4375 H  HA   . VAL   B 1 24  ? 53.111 -22.626 -8.015  1.00 16.47 ?  24  VAL   B HA   1 
ATOM   4376 H  HB   . VAL   B 1 24  ? 54.892 -24.741 -7.419  1.00 17.58 ?  24  VAL   B HB   1 
ATOM   4377 H  HG11 . VAL   B 1 24  ? 56.424 -22.914 -6.867  1.00 17.98 ?  24  VAL   B HG11 1 
ATOM   4378 H  HG12 . VAL   B 1 24  ? 56.295 -23.314 -8.397  1.00 17.98 ?  24  VAL   B HG12 1 
ATOM   4379 H  HG13 . VAL   B 1 24  ? 55.522 -22.041 -7.839  1.00 17.98 ?  24  VAL   B HG13 1 
ATOM   4380 H  HG21 . VAL   B 1 24  ? 54.930 -23.914 -5.287  1.00 18.96 ?  24  VAL   B HG21 1 
ATOM   4381 H  HG22 . VAL   B 1 24  ? 54.003 -22.698 -5.715  1.00 18.96 ?  24  VAL   B HG22 1 
ATOM   4382 H  HG23 . VAL   B 1 24  ? 53.418 -24.176 -5.698  1.00 18.96 ?  24  VAL   B HG23 1 
ATOM   4383 N  N    . GLU   B 1 25  ? 54.165 -24.622 -10.292 1.00 14.57 ?  25  GLU   B N    1 
ATOM   4384 C  CA   . GLU   B 1 25  ? 54.553 -24.659 -11.697 1.00 16.02 ?  25  GLU   B CA   1 
ATOM   4385 C  C    . GLU   B 1 25  ? 53.445 -24.106 -12.582 1.00 14.81 ?  25  GLU   B C    1 
ATOM   4386 O  O    . GLU   B 1 25  ? 53.712 -23.395 -13.560 1.00 15.79 ?  25  GLU   B O    1 
ATOM   4387 C  CB   . GLU   B 1 25  ? 54.941 -26.083 -12.092 1.00 20.23 ?  25  GLU   B CB   1 
ATOM   4388 C  CG   . GLU   B 1 25  ? 56.228 -26.542 -11.424 1.00 25.91 ?  25  GLU   B CG   1 
ATOM   4389 C  CD   . GLU   B 1 25  ? 57.349 -25.519 -11.538 1.00 30.94 ?  25  GLU   B CD   1 
ATOM   4390 O  OE1  . GLU   B 1 25  ? 57.697 -25.140 -12.678 1.00 32.78 ?  25  GLU   B OE1  1 
ATOM   4391 O  OE2  . GLU   B 1 25  ? 57.868 -25.073 -10.488 1.00 32.80 -1 25  GLU   B OE2  1 
ATOM   4392 H  H    . GLU   B 1 25  ? 54.126 -25.390 -9.904  1.00 17.51 ?  25  GLU   B H    1 
ATOM   4393 H  HA   . GLU   B 1 25  ? 55.314 -24.081 -11.821 1.00 19.26 ?  25  GLU   B HA   1 
ATOM   4394 H  HB2  . GLU   B 1 25  ? 54.234 -26.694 -11.825 1.00 24.31 ?  25  GLU   B HB2  1 
ATOM   4395 H  HB3  . GLU   B 1 25  ? 55.068 -26.122 -13.052 1.00 24.31 ?  25  GLU   B HB3  1 
ATOM   4396 H  HG2  . GLU   B 1 25  ? 56.064 -26.687 -10.483 1.00 31.12 ?  25  GLU   B HG2  1 
ATOM   4397 H  HG3  . GLU   B 1 25  ? 56.528 -27.362 -11.846 1.00 31.12 ?  25  GLU   B HG3  1 
ATOM   4398 N  N    A GLU   B 1 26  ? 52.192 -24.415 -12.250 0.50 13.84 ?  26  GLU   B N    1 
ATOM   4399 N  N    B GLU   B 1 26  ? 52.191 -24.421 -12.251 0.50 14.30 ?  26  GLU   B N    1 
ATOM   4400 C  CA   A GLU   B 1 26  ? 51.071 -23.884 -13.016 0.50 14.25 ?  26  GLU   B CA   1 
ATOM   4401 C  CA   B GLU   B 1 26  ? 51.061 -23.892 -13.009 0.50 15.09 ?  26  GLU   B CA   1 
ATOM   4402 C  C    A GLU   B 1 26  ? 51.026 -22.367 -12.932 0.50 13.94 ?  26  GLU   B C    1 
ATOM   4403 C  C    B GLU   B 1 26  ? 51.016 -22.372 -12.930 0.50 14.29 ?  26  GLU   B C    1 
ATOM   4404 O  O    A GLU   B 1 26  ? 50.848 -21.684 -13.946 0.50 14.98 ?  26  GLU   B O    1 
ATOM   4405 O  O    B GLU   B 1 26  ? 50.827 -21.695 -13.945 0.50 15.22 ?  26  GLU   B O    1 
ATOM   4406 C  CB   A GLU   B 1 26  ? 49.758 -24.473 -12.501 0.50 15.42 ?  26  GLU   B CB   1 
ATOM   4407 C  CB   B GLU   B 1 26  ? 49.747 -24.478 -12.481 0.50 17.06 ?  26  GLU   B CB   1 
ATOM   4408 C  CG   A GLU   B 1 26  ? 49.451 -25.847 -13.038 0.50 17.16 ?  26  GLU   B CG   1 
ATOM   4409 C  CG   B GLU   B 1 26  ? 49.224 -25.686 -13.241 0.50 19.52 ?  26  GLU   B CG   1 
ATOM   4410 C  CD   A GLU   B 1 26  ? 49.271 -25.871 -14.544 0.50 17.77 ?  26  GLU   B CD   1 
ATOM   4411 C  CD   B GLU   B 1 26  ? 48.897 -25.381 -14.699 0.50 20.40 ?  26  GLU   B CD   1 
ATOM   4412 O  OE1  A GLU   B 1 26  ? 48.432 -25.100 -15.058 0.50 17.14 ?  26  GLU   B OE1  1 
ATOM   4413 O  OE1  B GLU   B 1 26  ? 47.832 -24.787 -14.992 0.50 21.21 ?  26  GLU   B OE1  1 
ATOM   4414 O  OE2  A GLU   B 1 26  ? 49.972 -26.657 -15.209 0.50 19.07 -1 26  GLU   B OE2  1 
ATOM   4415 O  OE2  B GLU   B 1 26  ? 49.718 -25.746 -15.557 0.50 20.08 -1 26  GLU   B OE2  1 
ATOM   4416 H  H    A GLU   B 1 26  ? 51.963 -24.926 -11.591 0.50 16.64 ?  26  GLU   B H    1 
ATOM   4417 H  H    B GLU   B 1 26  ? 51.967 -24.937 -11.595 0.50 17.19 ?  26  GLU   B H    1 
ATOM   4418 H  HA   A GLU   B 1 26  ? 51.173 -24.133 -13.945 0.50 17.13 ?  26  GLU   B HA   1 
ATOM   4419 H  HA   B GLU   B 1 26  ? 51.156 -24.144 -13.938 0.50 18.14 ?  26  GLU   B HA   1 
ATOM   4420 H  HB2  A GLU   B 1 26  ? 49.801 -24.539 -11.531 0.50 18.53 ?  26  GLU   B HB2  1 
ATOM   4421 H  HB2  B GLU   B 1 26  ? 49.875 -24.747 -11.558 0.50 20.51 ?  26  GLU   B HB2  1 
ATOM   4422 H  HB3  A GLU   B 1 26  ? 49.028 -23.882 -12.753 0.50 18.53 ?  26  GLU   B HB3  1 
ATOM   4423 H  HB3  B GLU   B 1 26  ? 49.063 -23.791 -12.526 0.50 20.51 ?  26  GLU   B HB3  1 
ATOM   4424 H  HG2  A GLU   B 1 26  ? 50.190 -26.423 -12.830 0.50 20.63 ?  26  GLU   B HG2  1 
ATOM   4425 H  HG2  B GLU   B 1 26  ? 49.897 -26.385 -13.207 0.50 23.46 ?  26  GLU   B HG2  1 
ATOM   4426 H  HG3  A GLU   B 1 26  ? 48.636 -26.164 -12.621 0.50 20.63 ?  26  GLU   B HG3  1 
ATOM   4427 H  HG3  B GLU   B 1 26  ? 48.407 -25.993 -12.819 0.50 23.46 ?  26  GLU   B HG3  1 
ATOM   4428 N  N    . ALA   B 1 27  ? 51.159 -21.820 -11.723 1.00 13.28 ?  27  ALA   B N    1 
ATOM   4429 C  CA   . ALA   B 1 27  ? 51.132 -20.370 -11.570 1.00 13.78 ?  27  ALA   B CA   1 
ATOM   4430 C  C    . ALA   B 1 27  ? 52.206 -19.707 -12.422 1.00 14.71 ?  27  ALA   B C    1 
ATOM   4431 O  O    . ALA   B 1 27  ? 51.948 -18.698 -13.092 1.00 15.26 ?  27  ALA   B O    1 
ATOM   4432 C  CB   . ALA   B 1 27  ? 51.291 -19.998 -10.098 1.00 13.72 ?  27  ALA   B CB   1 
ATOM   4433 H  H    A ALA   B 1 27  ? 51.260 -22.259 -10.990 0.50 15.97 ?  27  ALA   B H    1 
ATOM   4434 H  H    B ALA   B 1 27  ? 51.265 -22.258 -10.990 0.50 15.97 ?  27  ALA   B H    1 
ATOM   4435 H  HA   . ALA   B 1 27  ? 50.275 -20.036 -11.865 1.00 16.56 ?  27  ALA   B HA   1 
ATOM   4436 H  HB1  . ALA   B 1 27  ? 51.269 -19.032 -10.011 1.00 16.50 ?  27  ALA   B HB1  1 
ATOM   4437 H  HB2  . ALA   B 1 27  ? 50.558 -20.390 -9.594  1.00 16.50 ?  27  ALA   B HB2  1 
ATOM   4438 H  HB3  . ALA   B 1 27  ? 52.136 -20.342 -9.771  1.00 16.50 ?  27  ALA   B HB3  1 
ATOM   4439 N  N    . LYS   B 1 28  ? 53.420 -20.259 -12.414 1.00 16.26 ?  28  LYS   B N    1 
ATOM   4440 C  CA   . LYS   B 1 28  ? 54.499 -19.637 -13.171 1.00 18.22 ?  28  LYS   B CA   1 
ATOM   4441 C  C    . LYS   B 1 28  ? 54.248 -19.705 -14.673 1.00 19.04 ?  28  LYS   B C    1 
ATOM   4442 O  O    . LYS   B 1 28  ? 54.670 -18.804 -15.409 1.00 20.15 ?  28  LYS   B O    1 
ATOM   4443 C  CB   . LYS   B 1 28  ? 55.853 -20.233 -12.774 1.00 20.79 ?  28  LYS   B CB   1 
ATOM   4444 C  CG   . LYS   B 1 28  ? 56.246 -19.895 -11.338 1.00 23.41 ?  28  LYS   B CG   1 
ATOM   4445 C  CD   . LYS   B 1 28  ? 57.686 -20.257 -11.011 1.00 27.42 ?  28  LYS   B CD   1 
ATOM   4446 C  CE   . LYS   B 1 28  ? 57.815 -21.688 -10.543 1.00 30.40 ?  28  LYS   B CE   1 
ATOM   4447 N  NZ   . LYS   B 1 28  ? 59.167 -21.954 -9.976  1.00 31.17 ?  28  LYS   B NZ   1 
ATOM   4448 H  H    . LYS   B 1 28  ? 53.639 -20.973 -11.986 1.00 19.54 ?  28  LYS   B H    1 
ATOM   4449 H  HA   . LYS   B 1 28  ? 54.527 -18.698 -12.938 1.00 21.89 ?  28  LYS   B HA   1 
ATOM   4450 H  HB2  . LYS   B 1 28  ? 55.817 -21.197 -12.851 1.00 24.98 ?  28  LYS   B HB2  1 
ATOM   4451 H  HB3  . LYS   B 1 28  ? 56.542 -19.877 -13.359 1.00 24.98 ?  28  LYS   B HB3  1 
ATOM   4452 H  HG2  . LYS   B 1 28  ? 56.136 -18.939 -11.201 1.00 28.12 ?  28  LYS   B HG2  1 
ATOM   4453 H  HG3  . LYS   B 1 28  ? 55.666 -20.382 -10.733 1.00 28.12 ?  28  LYS   B HG3  1 
ATOM   4454 H  HD2  . LYS   B 1 28  ? 58.229 -20.143 -11.806 1.00 32.94 ?  28  LYS   B HD2  1 
ATOM   4455 H  HD3  . LYS   B 1 28  ? 58.003 -19.673 -10.304 1.00 32.94 ?  28  LYS   B HD3  1 
ATOM   4456 H  HE2  . LYS   B 1 28  ? 57.155 -21.860 -9.852  1.00 36.52 ?  28  LYS   B HE2  1 
ATOM   4457 H  HE3  . LYS   B 1 28  ? 57.675 -22.286 -11.295 1.00 36.52 ?  28  LYS   B HE3  1 
ATOM   4458 H  HZ1  . LYS   B 1 28  ? 59.223 -22.800 -9.706  1.00 37.44 ?  28  LYS   B HZ1  1 
ATOM   4459 H  HZ2  . LYS   B 1 28  ? 59.790 -21.805 -10.593 1.00 37.44 ?  28  LYS   B HZ2  1 
ATOM   4460 H  HZ3  . LYS   B 1 28  ? 59.315 -21.419 -9.279  1.00 37.44 ?  28  LYS   B HZ3  1 
ATOM   4461 N  N    A LYS   B 1 29  ? 53.546 -20.739 -15.142 0.50 20.15 ?  29  LYS   B N    1 
ATOM   4462 N  N    B LYS   B 1 29  ? 53.549 -20.737 -15.141 0.50 20.10 ?  29  LYS   B N    1 
ATOM   4463 C  CA   A LYS   B 1 29  ? 53.263 -20.886 -16.567 0.50 22.29 ?  29  LYS   B CA   1 
ATOM   4464 C  CA   B LYS   B 1 29  ? 53.268 -20.865 -16.566 0.50 22.20 ?  29  LYS   B CA   1 
ATOM   4465 C  C    A LYS   B 1 29  ? 52.004 -20.144 -17.006 0.50 21.22 ?  29  LYS   B C    1 
ATOM   4466 C  C    B LYS   B 1 29  ? 52.016 -20.102 -16.988 0.50 21.12 ?  29  LYS   B C    1 
ATOM   4467 O  O    A LYS   B 1 29  ? 51.989 -19.545 -18.087 0.50 22.10 ?  29  LYS   B O    1 
ATOM   4468 O  O    B LYS   B 1 29  ? 52.023 -19.436 -18.029 0.50 21.98 ?  29  LYS   B O    1 
ATOM   4469 C  CB   A LYS   B 1 29  ? 53.141 -22.369 -16.934 0.50 25.93 ?  29  LYS   B CB   1 
ATOM   4470 C  CB   B LYS   B 1 29  ? 53.138 -22.343 -16.940 0.50 25.80 ?  29  LYS   B CB   1 
ATOM   4471 C  CG   A LYS   B 1 29  ? 52.878 -22.616 -18.415 0.50 29.25 ?  29  LYS   B CG   1 
ATOM   4472 C  CG   B LYS   B 1 29  ? 53.000 -22.600 -18.431 0.50 29.07 ?  29  LYS   B CG   1 
ATOM   4473 C  CD   A LYS   B 1 29  ? 53.063 -24.080 -18.790 0.50 31.88 ?  29  LYS   B CD   1 
ATOM   4474 C  CD   B LYS   B 1 29  ? 53.220 -24.068 -18.770 0.50 31.65 ?  29  LYS   B CD   1 
ATOM   4475 C  CE   A LYS   B 1 29  ? 51.983 -24.960 -18.182 0.50 33.71 ?  29  LYS   B CE   1 
ATOM   4476 C  CE   B LYS   B 1 29  ? 52.160 -24.961 -18.143 0.50 33.43 ?  29  LYS   B CE   1 
ATOM   4477 N  NZ   A LYS   B 1 29  ? 52.164 -26.390 -18.561 0.50 34.81 ?  29  LYS   B NZ   1 
ATOM   4478 N  NZ   B LYS   B 1 29  ? 52.376 -26.398 -18.477 0.50 34.51 ?  29  LYS   B NZ   1 
ATOM   4479 H  H    A LYS   B 1 29  ? 53.227 -21.371 -14.650 0.50 24.22 ?  29  LYS   B H    1 
ATOM   4480 H  H    B LYS   B 1 29  ? 53.228 -21.374 -14.653 0.50 24.15 ?  29  LYS   B H    1 
ATOM   4481 H  HA   A LYS   B 1 29  ? 54.006 -20.522 -17.066 0.50 26.79 ?  29  LYS   B HA   1 
ATOM   4482 H  HA   B LYS   B 1 29  ? 54.014 -20.501 -17.062 0.50 26.67 ?  29  LYS   B HA   1 
ATOM   4483 H  HB2  A LYS   B 1 29  ? 53.970 -22.819 -16.704 0.50 31.14 ?  29  LYS   B HB2  1 
ATOM   4484 H  HB2  B LYS   B 1 29  ? 53.932 -22.810 -16.634 0.50 31.00 ?  29  LYS   B HB2  1 
ATOM   4485 H  HB3  A LYS   B 1 29  ? 52.408 -22.759 -16.435 0.50 31.14 ?  29  LYS   B HB3  1 
ATOM   4486 H  HB3  B LYS   B 1 29  ? 52.355 -22.706 -16.503 0.50 31.00 ?  29  LYS   B HB3  1 
ATOM   4487 H  HG2  A LYS   B 1 29  ? 51.964 -22.366 -18.624 0.50 35.14 ?  29  LYS   B HG2  1 
ATOM   4488 H  HG2  B LYS   B 1 29  ? 52.106 -22.354 -18.716 0.50 34.92 ?  29  LYS   B HG2  1 
ATOM   4489 H  HG3  A LYS   B 1 29  ? 53.498 -22.089 -18.943 0.50 35.14 ?  29  LYS   B HG3  1 
ATOM   4490 H  HG3  B LYS   B 1 29  ? 53.661 -22.076 -18.910 0.50 34.92 ?  29  LYS   B HG3  1 
ATOM   4491 H  HD2  A LYS   B 1 29  ? 53.020 -24.170 -19.755 0.50 38.29 ?  29  LYS   B HD2  1 
ATOM   4492 H  HD2  B LYS   B 1 29  ? 53.181 -24.182 -19.732 0.50 38.02 ?  29  LYS   B HD2  1 
ATOM   4493 H  HD3  A LYS   B 1 29  ? 53.923 -24.387 -18.463 0.50 38.29 ?  29  LYS   B HD3  1 
ATOM   4494 H  HD3  B LYS   B 1 29  ? 54.087 -24.346 -18.435 0.50 38.02 ?  29  LYS   B HD3  1 
ATOM   4495 H  HE2  A LYS   B 1 29  ? 52.022 -24.896 -17.215 0.50 40.48 ?  29  LYS   B HE2  1 
ATOM   4496 H  HE2  B LYS   B 1 29  ? 52.191 -24.869 -17.178 0.50 40.15 ?  29  LYS   B HE2  1 
ATOM   4497 H  HE3  A LYS   B 1 29  ? 51.114 -24.669 -18.503 0.50 40.48 ?  29  LYS   B HE3  1 
ATOM   4498 H  HE3  B LYS   B 1 29  ? 51.286 -24.700 -18.476 0.50 40.15 ?  29  LYS   B HE3  1 
ATOM   4499 H  HZ1  A LYS   B 1 29  ? 51.522 -26.886 -18.195 0.50 41.81 ?  29  LYS   B HZ1  1 
ATOM   4500 H  HZ1  B LYS   B 1 29  ? 51.743 -26.897 -18.099 0.50 41.44 ?  29  LYS   B HZ1  1 
ATOM   4501 H  HZ2  A LYS   B 1 29  ? 52.128 -26.478 -19.446 0.50 41.81 ?  29  LYS   B HZ2  1 
ATOM   4502 H  HZ2  B LYS   B 1 29  ? 52.346 -26.513 -19.359 0.50 41.44 ?  29  LYS   B HZ2  1 
ATOM   4503 H  HZ3  A LYS   B 1 29  ? 52.954 -26.683 -18.274 0.50 41.81 ?  29  LYS   B HZ3  1 
ATOM   4504 H  HZ3  B LYS   B 1 29  ? 53.171 -26.663 -18.177 0.50 41.44 ?  29  LYS   B HZ3  1 
ATOM   4505 N  N    . VAL   B 1 30  ? 50.944 -20.184 -16.194 1.00 19.84 ?  30  VAL   B N    1 
ATOM   4506 C  CA   . VAL   B 1 30  ? 49.660 -19.583 -16.574 1.00 19.87 ?  30  VAL   B CA   1 
ATOM   4507 C  C    . VAL   B 1 30  ? 49.653 -18.070 -16.404 1.00 18.87 ?  30  VAL   B C    1 
ATOM   4508 O  O    . VAL   B 1 30  ? 48.899 -17.361 -17.091 1.00 19.64 ?  30  VAL   B O    1 
ATOM   4509 C  CB   . VAL   B 1 30  ? 48.551 -20.216 -15.710 1.00 21.08 ?  30  VAL   B CB   1 
ATOM   4510 C  CG1  . VAL   B 1 30  ? 47.259 -19.401 -15.768 1.00 21.23 ?  30  VAL   B CG1  1 
ATOM   4511 C  CG2  . VAL   B 1 30  ? 48.314 -21.660 -16.123 1.00 21.92 ?  30  VAL   B CG2  1 
ATOM   4512 H  H    A VAL   B 1 30  ? 50.937 -20.563 -15.416 0.50 23.85 ?  30  VAL   B H    1 
ATOM   4513 H  H    B VAL   B 1 30  ? 50.927 -20.599 -15.435 0.50 23.85 ?  30  VAL   B H    1 
ATOM   4514 H  HA   . VAL   B 1 30  ? 49.473 -19.803 -17.502 1.00 23.88 ?  30  VAL   B HA   1 
ATOM   4515 H  HB   . VAL   B 1 30  ? 48.845 -20.233 -14.787 1.00 25.33 ?  30  VAL   B HB   1 
ATOM   4516 H  HG11 . VAL   B 1 30  ? 46.518 -19.980 -15.525 1.00 25.51 ?  30  VAL   B HG11 1 
ATOM   4517 H  HG12 . VAL   B 1 30  ? 47.318 -18.667 -15.140 1.00 25.51 ?  30  VAL   B HG12 1 
ATOM   4518 H  HG13 . VAL   B 1 30  ? 47.129 -19.073 -16.667 1.00 25.51 ?  30  VAL   B HG13 1 
ATOM   4519 H  HG21 . VAL   B 1 30  ? 47.617 -22.043 -15.562 1.00 26.33 ?  30  VAL   B HG21 1 
ATOM   4520 H  HG22 . VAL   B 1 30  ? 48.033 -21.683 -17.052 1.00 26.33 ?  30  VAL   B HG22 1 
ATOM   4521 H  HG23 . VAL   B 1 30  ? 49.135 -22.162 -16.013 1.00 26.33 ?  30  VAL   B HG23 1 
ATOM   4522 N  N    . LYS   B 1 31  ? 50.433 -17.566 -15.462 1.00 18.55 ?  31  LYS   B N    1 
ATOM   4523 C  CA   . LYS   B 1 31  ? 50.446 -16.156 -15.098 1.00 18.90 ?  31  LYS   B CA   1 
ATOM   4524 C  C    . LYS   B 1 31  ? 49.043 -15.690 -14.708 1.00 16.58 ?  31  LYS   B C    1 
ATOM   4525 O  O    . LYS   B 1 31  ? 48.496 -14.768 -15.326 1.00 17.73 ?  31  LYS   B O    1 
ATOM   4526 C  CB   . LYS   B 1 31  ? 51.070 -15.332 -16.232 1.00 22.24 ?  31  LYS   B CB   1 
ATOM   4527 C  CG   . LYS   B 1 31  ? 52.496 -15.779 -16.573 1.00 25.57 ?  31  LYS   B CG   1 
ATOM   4528 C  CD   . LYS   B 1 31  ? 53.088 -14.988 -17.730 1.00 28.56 ?  31  LYS   B CD   1 
ATOM   4529 C  CE   . LYS   B 1 31  ? 54.568 -15.272 -17.900 1.00 30.83 ?  31  LYS   B CE   1 
ATOM   4530 N  NZ   . LYS   B 1 31  ? 55.318 -14.895 -16.670 1.00 32.11 ?  31  LYS   B NZ   1 
ATOM   4531 H  H    . LYS   B 1 31  ? 50.983 -18.056 -15.011 1.00 22.29 ?  31  LYS   B H    1 
ATOM   4532 H  HA   . LYS   B 1 31  ? 51.002 -16.069 -14.322 1.00 22.71 ?  31  LYS   B HA   1 
ATOM   4533 H  HB2  . LYS   B 1 31  ? 50.528 -15.424 -17.034 1.00 26.72 ?  31  LYS   B HB2  1 
ATOM   4534 H  HB3  . LYS   B 1 31  ? 51.102 -14.406 -15.956 1.00 26.72 ?  31  LYS   B HB3  1 
ATOM   4535 H  HG2  . LYS   B 1 31  ? 53.054 -15.653 -15.790 1.00 30.71 ?  31  LYS   B HG2  1 
ATOM   4536 H  HG3  . LYS   B 1 31  ? 52.481 -16.719 -16.821 1.00 30.71 ?  31  LYS   B HG3  1 
ATOM   4537 H  HD2  . LYS   B 1 31  ? 52.633 -15.237 -18.549 1.00 34.30 ?  31  LYS   B HD2  1 
ATOM   4538 H  HD3  . LYS   B 1 31  ? 52.976 -14.042 -17.556 1.00 34.30 ?  31  LYS   B HD3  1 
ATOM   4539 H  HE2  . LYS   B 1 31  ? 54.706 -16.220 -18.062 1.00 37.03 ?  31  LYS   B HE2  1 
ATOM   4540 H  HE3  . LYS   B 1 31  ? 54.918 -14.751 -18.642 1.00 37.03 ?  31  LYS   B HE3  1 
ATOM   4541 H  HZ1  . LYS   B 1 31  ? 56.193 -14.934 -16.821 1.00 38.56 ?  31  LYS   B HZ1  1 
ATOM   4542 H  HZ2  . LYS   B 1 31  ? 55.102 -14.066 -16.428 1.00 38.56 ?  31  LYS   B HZ2  1 
ATOM   4543 H  HZ3  . LYS   B 1 31  ? 55.113 -15.452 -16.007 1.00 38.56 ?  31  LYS   B HZ3  1 
ATOM   4544 N  N    . PRO   B 1 32  ? 48.434 -16.293 -13.679 1.00 14.53 ?  32  PRO   B N    1 
ATOM   4545 C  CA   . PRO   B 1 32  ? 47.052 -15.939 -13.328 1.00 13.54 ?  32  PRO   B CA   1 
ATOM   4546 C  C    . PRO   B 1 32  ? 46.965 -14.594 -12.626 1.00 13.76 ?  32  PRO   B C    1 
ATOM   4547 O  O    . PRO   B 1 32  ? 47.891 -14.169 -11.927 1.00 15.11 ?  32  PRO   B O    1 
ATOM   4548 C  CB   . PRO   B 1 32  ? 46.655 -17.057 -12.360 1.00 13.75 ?  32  PRO   B CB   1 
ATOM   4549 C  CG   . PRO   B 1 32  ? 47.954 -17.385 -11.673 1.00 14.24 ?  32  PRO   B CG   1 
ATOM   4550 C  CD   . PRO   B 1 32  ? 49.010 -17.277 -12.737 1.00 14.48 ?  32  PRO   B CD   1 
ATOM   4551 H  HA   . PRO   B 1 32  ? 46.469 -15.954 -14.113 1.00 16.28 ?  32  PRO   B HA   1 
ATOM   4552 H  HB2  . PRO   B 1 32  ? 45.994 -16.731 -11.728 1.00 16.54 ?  32  PRO   B HB2  1 
ATOM   4553 H  HB3  . PRO   B 1 32  ? 46.318 -17.824 -12.852 1.00 16.54 ?  32  PRO   B HB3  1 
ATOM   4554 H  HG2  . PRO   B 1 32  ? 48.120 -16.737 -10.964 1.00 17.13 ?  32  PRO   B HG2  1 
ATOM   4555 H  HG3  . PRO   B 1 32  ? 47.924 -18.281 -11.314 1.00 17.13 ?  32  PRO   B HG3  1 
ATOM   4556 H  HD2  . PRO   B 1 32  ? 49.836 -16.932 -12.363 1.00 17.41 ?  32  PRO   B HD2  1 
ATOM   4557 H  HD3  . PRO   B 1 32  ? 49.138 -18.129 -13.172 1.00 17.41 ?  32  PRO   B HD3  1 
ATOM   4558 N  N    . THR   B 1 33  ? 45.811 -13.939 -12.790 1.00 13.22 ?  33  THR   B N    1 
ATOM   4559 C  CA   . THR   B 1 33  ? 45.513 -12.764 -11.980 1.00 13.67 ?  33  THR   B CA   1 
ATOM   4560 C  C    . THR   B 1 33  ? 45.464 -13.117 -10.500 1.00 13.13 ?  33  THR   B C    1 
ATOM   4561 O  O    . THR   B 1 33  ? 45.932 -12.340 -9.658  1.00 14.15 ?  33  THR   B O    1 
ATOM   4562 C  CB   . THR   B 1 33  ? 44.194 -12.129 -12.433 1.00 14.16 ?  33  THR   B CB   1 
ATOM   4563 O  OG1  . THR   B 1 33  ? 44.239 -11.873 -13.838 1.00 14.10 ?  33  THR   B OG1  1 
ATOM   4564 C  CG2  . THR   B 1 33  ? 43.939 -10.826 -11.690 1.00 15.51 ?  33  THR   B CG2  1 
ATOM   4565 H  H    . THR   B 1 33  ? 45.189 -14.163 -13.349 1.00 15.90 ?  33  THR   B H    1 
ATOM   4566 H  HA   . THR   B 1 33  ? 46.213 -12.113 -12.111 1.00 16.44 ?  33  THR   B HA   1 
ATOM   4567 H  HB   . THR   B 1 33  ? 43.458 -12.736 -12.240 1.00 17.03 ?  33  THR   B HB   1 
ATOM   4568 H  HG1  . THR   B 1 33  ? 43.511 -11.513 -14.089 1.00 16.95 ?  33  THR   B HG1  1 
ATOM   4569 H  HG21 . THR   B 1 33  ? 43.181 -10.367 -12.077 1.00 18.64 ?  33  THR   B HG21 1 
ATOM   4570 H  HG22 . THR   B 1 33  ? 43.755 -11.007 -10.754 1.00 18.64 ?  33  THR   B HG22 1 
ATOM   4571 H  HG23 . THR   B 1 33  ? 44.722 -10.256 -11.752 1.00 18.64 ?  33  THR   B HG23 1 
ATOM   4572 N  N    . VAL   B 1 34  ? 44.909 -14.285 -10.160 1.00 12.45 ?  34  VAL   B N    1 
ATOM   4573 C  CA   . VAL   B 1 34  ? 44.722 -14.688 -8.768  1.00 12.06 ?  34  VAL   B CA   1 
ATOM   4574 C  C    . VAL   B 1 34  ? 45.154 -16.138 -8.603  1.00 10.86 ?  34  VAL   B C    1 
ATOM   4575 O  O    . VAL   B 1 34  ? 44.637 -17.023 -9.291  1.00 11.73 ?  34  VAL   B O    1 
ATOM   4576 C  CB   . VAL   B 1 34  ? 43.254 -14.541 -8.312  1.00 13.15 ?  34  VAL   B CB   1 
ATOM   4577 C  CG1  . VAL   B 1 34  ? 43.103 -14.991 -6.865  1.00 13.57 ?  34  VAL   B CG1  1 
ATOM   4578 C  CG2  . VAL   B 1 34  ? 42.759 -13.120 -8.496  1.00 14.22 ?  34  VAL   B CG2  1 
ATOM   4579 H  H    . VAL   B 1 34  ? 44.638 -14.873 -10.726 1.00 14.98 ?  34  VAL   B H    1 
ATOM   4580 H  HA   . VAL   B 1 34  ? 45.272 -14.137 -8.191  1.00 14.51 ?  34  VAL   B HA   1 
ATOM   4581 H  HB   . VAL   B 1 34  ? 42.697 -15.121 -8.857  1.00 15.82 ?  34  VAL   B HB   1 
ATOM   4582 H  HG11 . VAL   B 1 34  ? 42.246 -14.681 -6.526  1.00 16.32 ?  34  VAL   B HG11 1 
ATOM   4583 H  HG12 . VAL   B 1 34  ? 43.136 -15.960 -6.825  1.00 16.32 ?  34  VAL   B HG12 1 
ATOM   4584 H  HG13 . VAL   B 1 34  ? 43.821 -14.610 -6.338  1.00 16.32 ?  34  VAL   B HG13 1 
ATOM   4585 H  HG21 . VAL   B 1 34  ? 41.845 -13.062 -8.174  1.00 17.10 ?  34  VAL   B HG21 1 
ATOM   4586 H  HG22 . VAL   B 1 34  ? 43.329 -12.523 -7.991  1.00 17.10 ?  34  VAL   B HG22 1 
ATOM   4587 H  HG23 . VAL   B 1 34  ? 42.792 -12.899 -9.439  1.00 17.10 ?  34  VAL   B HG23 1 
ATOM   4588 N  N    . VAL   B 1 35  ? 46.070 -16.388 -7.666  1.00 10.58 ?  35  VAL   B N    1 
ATOM   4589 C  CA   . VAL   B 1 35  ? 46.309 -17.729 -7.148  1.00 10.51 ?  35  VAL   B CA   1 
ATOM   4590 C  C    . VAL   B 1 35  ? 45.771 -17.785 -5.727  1.00 9.95  ?  35  VAL   B C    1 
ATOM   4591 O  O    . VAL   B 1 35  ? 45.994 -16.862 -4.935  1.00 10.46 ?  35  VAL   B O    1 
ATOM   4592 C  CB   . VAL   B 1 35  ? 47.794 -18.154 -7.229  1.00 10.96 ?  35  VAL   B CB   1 
ATOM   4593 C  CG1  . VAL   B 1 35  ? 48.686 -17.309 -6.318  1.00 11.99 ?  35  VAL   B CG1  1 
ATOM   4594 C  CG2  . VAL   B 1 35  ? 47.942 -19.642 -6.899  1.00 11.70 ?  35  VAL   B CG2  1 
ATOM   4595 H  H    . VAL   B 1 35  ? 46.575 -15.788 -7.318  1.00 12.73 ?  35  VAL   B H    1 
ATOM   4596 H  HA   . VAL   B 1 35  ? 45.795 -18.364 -7.678  1.00 12.64 ?  35  VAL   B HA   1 
ATOM   4597 H  HB   . VAL   B 1 35  ? 48.102 -18.034 -8.143  1.00 13.18 ?  35  VAL   B HB   1 
ATOM   4598 H  HG11 . VAL   B 1 35  ? 49.612 -17.529 -6.495  1.00 14.42 ?  35  VAL   B HG11 1 
ATOM   4599 H  HG12 . VAL   B 1 35  ? 48.519 -16.376 -6.497  1.00 14.42 ?  35  VAL   B HG12 1 
ATOM   4600 H  HG13 . VAL   B 1 35  ? 48.469 -17.516 -5.392  1.00 14.42 ?  35  VAL   B HG13 1 
ATOM   4601 H  HG21 . VAL   B 1 35  ? 48.866 -19.909 -7.012  1.00 14.07 ?  35  VAL   B HG21 1 
ATOM   4602 H  HG22 . VAL   B 1 35  ? 47.666 -19.795 -5.977  1.00 14.07 ?  35  VAL   B HG22 1 
ATOM   4603 H  HG23 . VAL   B 1 35  ? 47.374 -20.165 -7.495  1.00 14.07 ?  35  VAL   B HG23 1 
ATOM   4604 N  N    . VAL   B 1 36  ? 45.053 -18.867 -5.410  1.00 10.33 ?  36  VAL   B N    1 
ATOM   4605 C  CA   . VAL   B 1 36  ? 44.506 -19.079 -4.079  1.00 9.92  ?  36  VAL   B CA   1 
ATOM   4606 C  C    . VAL   B 1 36  ? 45.516 -19.838 -3.227  1.00 9.77  ?  36  VAL   B C    1 
ATOM   4607 O  O    . VAL   B 1 36  ? 46.062 -20.866 -3.650  1.00 10.93 ?  36  VAL   B O    1 
ATOM   4608 C  CB   . VAL   B 1 36  ? 43.168 -19.836 -4.153  1.00 10.47 ?  36  VAL   B CB   1 
ATOM   4609 C  CG1  . VAL   B 1 36  ? 42.669 -20.195 -2.760  1.00 11.17 ?  36  VAL   B CG1  1 
ATOM   4610 C  CG2  . VAL   B 1 36  ? 42.140 -19.003 -4.903  1.00 11.15 ?  36  VAL   B CG2  1 
ATOM   4611 H  H    . VAL   B 1 36  ? 44.879 -19.506 -5.964  1.00 12.43 ?  36  VAL   B H    1 
ATOM   4612 H  HA   . VAL   B 1 36  ? 44.344 -18.219 -3.665  1.00 11.94 ?  36  VAL   B HA   1 
ATOM   4613 H  HB   . VAL   B 1 36  ? 43.298 -20.661 -4.647  1.00 12.59 ?  36  VAL   B HB   1 
ATOM   4614 H  HG11 . VAL   B 1 36  ? 41.731 -20.431 -2.813  1.00 13.44 ?  36  VAL   B HG11 1 
ATOM   4615 H  HG12 . VAL   B 1 36  ? 43.181 -20.941 -2.420  1.00 13.44 ?  36  VAL   B HG12 1 
ATOM   4616 H  HG13 . VAL   B 1 36  ? 42.780 -19.421 -2.180  1.00 13.44 ?  36  VAL   B HG13 1 
ATOM   4617 H  HG21 . VAL   B 1 36  ? 41.298 -19.480 -4.922  1.00 13.42 ?  36  VAL   B HG21 1 
ATOM   4618 H  HG22 . VAL   B 1 36  ? 42.033 -18.152 -4.453  1.00 13.42 ?  36  VAL   B HG22 1 
ATOM   4619 H  HG23 . VAL   B 1 36  ? 42.456 -18.855 -5.813  1.00 13.42 ?  36  VAL   B HG23 1 
ATOM   4620 N  N    . ASN   B 1 37  ? 45.736 -19.345 -2.010  1.00 10.15 ?  37  ASN   B N    1 
ATOM   4621 C  CA   . ASN   B 1 37  ? 46.496 -20.066 -1.005  1.00 10.40 ?  37  ASN   B CA   1 
ATOM   4622 C  C    . ASN   B 1 37  ? 45.551 -20.743 -0.020  1.00 10.34 ?  37  ASN   B C    1 
ATOM   4623 O  O    . ASN   B 1 37  ? 44.544 -20.166 0.397   1.00 10.64 ?  37  ASN   B O    1 
ATOM   4624 C  CB   . ASN   B 1 37  ? 47.425 -19.122 -0.246  1.00 10.63 ?  37  ASN   B CB   1 
ATOM   4625 C  CG   . ASN   B 1 37  ? 48.278 -19.842 0.767   1.00 10.63 ?  37  ASN   B CG   1 
ATOM   4626 O  OD1  . ASN   B 1 37  ? 48.621 -21.018 0.593   1.00 11.25 ?  37  ASN   B OD1  1 
ATOM   4627 N  ND2  . ASN   B 1 37  ? 48.626 -19.144 1.839   1.00 10.84 ?  37  ASN   B ND2  1 
ATOM   4628 H  H    . ASN   B 1 37  ? 45.450 -18.581 -1.737  1.00 12.21 ?  37  ASN   B H    1 
ATOM   4629 H  HA   . ASN   B 1 37  ? 47.030 -20.757 -1.426  1.00 12.51 ?  37  ASN   B HA   1 
ATOM   4630 H  HB2  . ASN   B 1 37  ? 48.015 -18.691 -0.881  1.00 12.78 ?  37  ASN   B HB2  1 
ATOM   4631 H  HB3  . ASN   B 1 37  ? 46.897 -18.465 0.226   1.00 12.78 ?  37  ASN   B HB3  1 
ATOM   4632 H  HD21 . ASN   B 1 37  ? 49.108 -19.510 2.451   1.00 13.04 ?  37  ASN   B HD21 1 
ATOM   4633 H  HD22 . ASN   B 1 37  ? 48.359 -18.339 1.932   1.00 13.04 ?  37  ASN   B HD22 1 
ATOM   4634 N  N    . ALA   B 1 38  ? 45.900 -21.977 0.355   1.00 10.41 ?  38  ALA   B N    1 
ATOM   4635 C  CA   . ALA   B 1 38  ? 45.249 -22.727 1.433   1.00 10.85 ?  38  ALA   B CA   1 
ATOM   4636 C  C    . ALA   B 1 38  ? 45.833 -22.242 2.760   1.00 10.68 ?  38  ALA   B C    1 
ATOM   4637 O  O    . ALA   B 1 38  ? 46.738 -22.848 3.343   1.00 11.65 ?  38  ALA   B O    1 
ATOM   4638 C  CB   . ALA   B 1 38  ? 45.478 -24.221 1.241   1.00 11.96 ?  38  ALA   B CB   1 
ATOM   4639 H  H    . ALA   B 1 38  ? 46.546 -22.412 -0.003  1.00 12.53 ?  38  ALA   B H    1 
ATOM   4640 H  HA   . ALA   B 1 38  ? 44.293 -22.549 1.430   1.00 13.05 ?  38  ALA   B HA   1 
ATOM   4641 H  HB1  . ALA   B 1 38  ? 45.033 -24.703 1.966   1.00 14.39 ?  38  ALA   B HB1  1 
ATOM   4642 H  HB2  . ALA   B 1 38  ? 45.098 -24.491 0.392   1.00 14.39 ?  38  ALA   B HB2  1 
ATOM   4643 H  HB3  . ALA   B 1 38  ? 46.425 -24.403 1.261   1.00 14.39 ?  38  ALA   B HB3  1 
ATOM   4644 N  N    . ALA   B 1 39  ? 45.317 -21.100 3.223   1.00 10.64 ?  39  ALA   B N    1 
ATOM   4645 C  CA   . ALA   B 1 39  ? 45.868 -20.367 4.351   1.00 10.94 ?  39  ALA   B CA   1 
ATOM   4646 C  C    . ALA   B 1 39  ? 45.250 -20.818 5.674   1.00 11.07 ?  39  ALA   B C    1 
ATOM   4647 O  O    . ALA   B 1 39  ? 44.222 -21.497 5.722   1.00 11.90 ?  39  ALA   B O    1 
ATOM   4648 C  CB   . ALA   B 1 39  ? 45.622 -18.868 4.160   1.00 11.75 ?  39  ALA   B CB   1 
ATOM   4649 H  H    . ALA   B 1 39  ? 44.619 -20.723 2.883   1.00 12.80 ?  39  ALA   B H    1 
ATOM   4650 H  HA   . ALA   B 1 39  ? 46.822 -20.514 4.393   1.00 13.16 ?  39  ALA   B HA   1 
ATOM   4651 H  HB1  . ALA   B 1 39  ? 45.995 -18.387 4.916   1.00 14.13 ?  39  ALA   B HB1  1 
ATOM   4652 H  HB2  . ALA   B 1 39  ? 46.056 -18.577 3.340   1.00 14.13 ?  39  ALA   B HB2  1 
ATOM   4653 H  HB3  . ALA   B 1 39  ? 44.668 -18.704 4.103   1.00 14.13 ?  39  ALA   B HB3  1 
ATOM   4654 N  N    . ASN   B 1 40  ? 45.890 -20.394 6.762   1.00 12.08 ?  40  ASN   B N    1 
ATOM   4655 C  CA   . ASN   B 1 40  ? 45.335 -20.447 8.104   1.00 12.49 ?  40  ASN   B CA   1 
ATOM   4656 C  C    . ASN   B 1 40  ? 45.153 -19.021 8.631   1.00 11.88 ?  40  ASN   B C    1 
ATOM   4657 O  O    . ASN   B 1 40  ? 45.564 -18.038 8.001   1.00 12.02 ?  40  ASN   B O    1 
ATOM   4658 C  CB   . ASN   B 1 40  ? 46.194 -21.326 9.031   1.00 13.36 ?  40  ASN   B CB   1 
ATOM   4659 C  CG   . ASN   B 1 40  ? 47.650 -20.919 9.053   1.00 14.34 ?  40  ASN   B CG   1 
ATOM   4660 O  OD1  . ASN   B 1 40  ? 47.965 -19.736 9.119   1.00 16.24 ?  40  ASN   B OD1  1 
ATOM   4661 N  ND2  . ASN   B 1 40  ? 48.547 -21.895 9.006   1.00 14.32 ?  40  ASN   B ND2  1 
ATOM   4662 H  H    . ASN   B 1 40  ? 46.687 -20.069 6.740   1.00 14.53 ?  40  ASN   B H    1 
ATOM   4663 H  HA   . ASN   B 1 40  ? 44.456 -20.851 8.062   1.00 15.02 ?  40  ASN   B HA   1 
ATOM   4664 H  HB2  . ASN   B 1 40  ? 45.855 -21.260 9.937   1.00 16.07 ?  40  ASN   B HB2  1 
ATOM   4665 H  HB3  . ASN   B 1 40  ? 46.148 -22.247 8.726   1.00 16.07 ?  40  ASN   B HB3  1 
ATOM   4666 H  HD21 . ASN   B 1 40  ? 49.390 -21.709 9.014   1.00 17.22 ?  40  ASN   B HD21 1 
ATOM   4667 H  HD22 . ASN   B 1 40  ? 48.291 -22.714 8.961   1.00 17.22 ?  40  ASN   B HD22 1 
ATOM   4668 N  N    . VAL   B 1 41  ? 44.497 -18.899 9.787   1.00 12.40 ?  41  VAL   B N    1 
ATOM   4669 C  CA   . VAL   B 1 41  ? 44.039 -17.578 10.233  1.00 13.25 ?  41  VAL   B CA   1 
ATOM   4670 C  C    . VAL   B 1 41  ? 45.192 -16.625 10.530  1.00 12.95 ?  41  VAL   B C    1 
ATOM   4671 O  O    . VAL   B 1 41  ? 45.014 -15.404 10.457  1.00 13.21 ?  41  VAL   B O    1 
ATOM   4672 C  CB   . VAL   B 1 41  ? 43.064 -17.654 11.424  1.00 14.65 ?  41  VAL   B CB   1 
ATOM   4673 C  CG1  . VAL   B 1 41  ? 41.757 -18.319 11.017  1.00 15.21 ?  41  VAL   B CG1  1 
ATOM   4674 C  CG2  . VAL   B 1 41  ? 43.708 -18.357 12.609  1.00 15.80 ?  41  VAL   B CG2  1 
ATOM   4675 H  H    . VAL   B 1 41  ? 44.311 -19.544 10.319  1.00 14.91 ?  41  VAL   B H    1 
ATOM   4676 H  HA   . VAL   B 1 41  ? 43.544 -17.182 9.502   1.00 15.94 ?  41  VAL   B HA   1 
ATOM   4677 H  HB   . VAL   B 1 41  ? 42.850 -16.750 11.706  1.00 17.61 ?  41  VAL   B HB   1 
ATOM   4678 H  HG11 . VAL   B 1 41  ? 41.155 -18.328 11.780  1.00 18.29 ?  41  VAL   B HG11 1 
ATOM   4679 H  HG12 . VAL   B 1 41  ? 41.360 -17.818 10.289  1.00 18.29 ?  41  VAL   B HG12 1 
ATOM   4680 H  HG13 . VAL   B 1 41  ? 41.941 -19.228 10.733  1.00 18.29 ?  41  VAL   B HG13 1 
ATOM   4681 H  HG21 . VAL   B 1 41  ? 43.079 -18.373 13.347  1.00 18.99 ?  41  VAL   B HG21 1 
ATOM   4682 H  HG22 . VAL   B 1 41  ? 43.936 -19.266 12.351  1.00 18.99 ?  41  VAL   B HG22 1 
ATOM   4683 H  HG23 . VAL   B 1 41  ? 44.509 -17.876 12.866  1.00 18.99 ?  41  VAL   B HG23 1 
ATOM   4684 N  N    . TYR   B 1 42  ? 46.361 -17.138 10.912  1.00 13.32 ?  42  TYR   B N    1 
ATOM   4685 C  CA   . TYR   B 1 42  ? 47.516 -16.287 11.183  1.00 13.99 ?  42  TYR   B CA   1 
ATOM   4686 C  C    . TYR   B 1 42  ? 48.484 -16.211 10.007  1.00 13.03 ?  42  TYR   B C    1 
ATOM   4687 O  O    . TYR   B 1 42  ? 49.576 -15.646 10.146  1.00 14.21 ?  42  TYR   B O    1 
ATOM   4688 C  CB   . TYR   B 1 42  ? 48.215 -16.694 12.488  1.00 16.19 ?  42  TYR   B CB   1 
ATOM   4689 C  CG   . TYR   B 1 42  ? 47.620 -16.003 13.712  1.00 16.44 ?  42  TYR   B CG   1 
ATOM   4690 C  CD1  . TYR   B 1 42  ? 47.845 -14.648 13.945  1.00 15.60 ?  42  TYR   B CD1  1 
ATOM   4691 C  CD2  . TYR   B 1 42  ? 46.830 -16.695 14.617  1.00 18.42 ?  42  TYR   B CD2  1 
ATOM   4692 C  CE1  . TYR   B 1 42  ? 47.307 -14.003 15.045  1.00 16.91 ?  42  TYR   B CE1  1 
ATOM   4693 C  CE2  . TYR   B 1 42  ? 46.285 -16.059 15.724  1.00 18.45 ?  42  TYR   B CE2  1 
ATOM   4694 C  CZ   . TYR   B 1 42  ? 46.528 -14.709 15.933  1.00 18.57 ?  42  TYR   B CZ   1 
ATOM   4695 O  OH   . TYR   B 1 42  ? 45.997 -14.065 17.033  1.00 21.34 ?  42  TYR   B OH   1 
ATOM   4696 H  H    . TYR   B 1 42  ? 46.508 -17.983 11.015  1.00 16.02 ?  42  TYR   B H    1 
ATOM   4697 H  HA   . TYR   B 1 42  ? 47.186 -15.388 11.319  1.00 16.82 ?  42  TYR   B HA   1 
ATOM   4698 H  HB2  . TYR   B 1 42  ? 48.126 -17.650 12.611  1.00 19.47 ?  42  TYR   B HB2  1 
ATOM   4699 H  HB3  . TYR   B 1 42  ? 49.152 -16.450 12.430  1.00 19.47 ?  42  TYR   B HB3  1 
ATOM   4700 H  HD1  . TYR   B 1 42  ? 48.376 -14.165 13.342  1.00 18.76 ?  42  TYR   B HD1  1 
ATOM   4701 H  HD2  . TYR   B 1 42  ? 46.662 -17.598 14.476  1.00 22.13 ?  42  TYR   B HD2  1 
ATOM   4702 H  HE1  . TYR   B 1 42  ? 47.477 -13.097 15.183  1.00 20.32 ?  42  TYR   B HE1  1 
ATOM   4703 H  HE2  . TYR   B 1 42  ? 45.757 -16.536 16.321  1.00 22.17 ?  42  TYR   B HE2  1 
ATOM   4704 H  HH   . TYR   B 1 42  ? 46.228 -13.261 17.029  1.00 25.64 ?  42  TYR   B HH   1 
ATOM   4705 N  N    . LEU   B 1 43  ? 48.087 -16.722 8.846   1.00 11.97 ?  43  LEU   B N    1 
ATOM   4706 C  CA   . LEU   B 1 43  ? 48.901 -16.655 7.637   1.00 11.90 ?  43  LEU   B CA   1 
ATOM   4707 C  C    . LEU   B 1 43  ? 50.316 -17.163 7.893   1.00 12.41 ?  43  LEU   B C    1 
ATOM   4708 O  O    . LEU   B 1 43  ? 51.297 -16.566 7.443   1.00 13.03 ?  43  LEU   B O    1 
ATOM   4709 C  CB   . LEU   B 1 43  ? 48.920 -15.250 7.028   1.00 12.30 ?  43  LEU   B CB   1 
ATOM   4710 C  CG   . LEU   B 1 43  ? 47.564 -14.633 6.656   1.00 12.40 ?  43  LEU   B CG   1 
ATOM   4711 C  CD1  . LEU   B 1 43  ? 47.775 -13.235 6.085   1.00 13.51 ?  43  LEU   B CD1  1 
ATOM   4712 C  CD2  . LEU   B 1 43  ? 46.799 -15.523 5.682   1.00 12.52 ?  43  LEU   B CD2  1 
ATOM   4713 H  H    . LEU   B 1 43  ? 47.339 -17.133 8.729   1.00 14.40 ?  43  LEU   B H    1 
ATOM   4714 H  HA   . LEU   B 1 43  ? 48.504 -17.246 6.973   1.00 14.31 ?  43  LEU   B HA   1 
ATOM   4715 H  HB2  . LEU   B 1 43  ? 49.341 -14.653 7.663   1.00 14.80 ?  43  LEU   B HB2  1 
ATOM   4716 H  HB3  . LEU   B 1 43  ? 49.450 -15.283 6.216   1.00 14.80 ?  43  LEU   B HB3  1 
ATOM   4717 H  HG   . LEU   B 1 43  ? 47.031 -14.548 7.457   1.00 14.92 ?  43  LEU   B HG   1 
ATOM   4718 H  HD11 . LEU   B 1 43  ? 46.913 -12.853 5.853   1.00 16.25 ?  43  LEU   B HD11 1 
ATOM   4719 H  HD12 . LEU   B 1 43  ? 48.208 -12.682 6.758   1.00 16.25 ?  43  LEU   B HD12 1 
ATOM   4720 H  HD13 . LEU   B 1 43  ? 48.335 -13.291 5.296   1.00 16.25 ?  43  LEU   B HD13 1 
ATOM   4721 H  HD21 . LEU   B 1 43  ? 45.991 -15.059 5.397   1.00 15.05 ?  43  LEU   B HD21 1 
ATOM   4722 H  HD22 . LEU   B 1 43  ? 47.356 -15.713 4.912   1.00 15.05 ?  43  LEU   B HD22 1 
ATOM   4723 H  HD23 . LEU   B 1 43  ? 46.557 -16.351 6.128   1.00 15.05 ?  43  LEU   B HD23 1 
ATOM   4724 N  N    . LYS   B 1 44  ? 50.418 -18.294 8.598   1.00 12.29 ?  44  LYS   B N    1 
ATOM   4725 C  CA   . LYS   B 1 44  ? 51.689 -18.966 8.834   1.00 13.00 ?  44  LYS   B CA   1 
ATOM   4726 C  C    . LYS   B 1 44  ? 51.808 -20.081 7.803   1.00 12.22 ?  44  LYS   B C    1 
ATOM   4727 O  O    . LYS   B 1 44  ? 51.111 -21.096 7.888   1.00 13.71 ?  44  LYS   B O    1 
ATOM   4728 C  CB   . LYS   B 1 44  ? 51.751 -19.482 10.269  1.00 14.74 ?  44  LYS   B CB   1 
ATOM   4729 C  CG   . LYS   B 1 44  ? 51.924 -18.370 11.297  1.00 17.34 ?  44  LYS   B CG   1 
ATOM   4730 C  CD   . LYS   B 1 44  ? 53.134 -17.510 10.932  1.00 20.31 ?  44  LYS   B CD   1 
ATOM   4731 C  CE   . LYS   B 1 44  ? 53.595 -16.618 12.054  1.00 23.09 ?  44  LYS   B CE   1 
ATOM   4732 N  NZ   . LYS   B 1 44  ? 54.784 -15.817 11.670  1.00 24.51 ?  44  LYS   B NZ   1 
ATOM   4733 H  H    . LYS   B 1 44  ? 49.743 -18.689 8.961   1.00 14.78 ?  44  LYS   B H    1 
ATOM   4734 H  HA   . LYS   B 1 44  ? 52.414 -18.342 8.675   1.00 15.63 ?  44  LYS   B HA   1 
ATOM   4735 H  HB2  . LYS   B 1 44  ? 50.919 -19.946 10.470  1.00 17.72 ?  44  LYS   B HB2  1 
ATOM   4736 H  HB3  . LYS   B 1 44  ? 52.497 -20.088 10.352  1.00 17.72 ?  44  LYS   B HB3  1 
ATOM   4737 H  HG2  . LYS   B 1 44  ? 51.134 -17.812 11.310  1.00 20.84 ?  44  LYS   B HG2  1 
ATOM   4738 H  HG3  . LYS   B 1 44  ? 52.078 -18.766 12.172  1.00 20.84 ?  44  LYS   B HG3  1 
ATOM   4739 H  HD2  . LYS   B 1 44  ? 53.867 -18.098 10.675  1.00 24.40 ?  44  LYS   B HD2  1 
ATOM   4740 H  HD3  . LYS   B 1 44  ? 52.893 -16.940 10.185  1.00 24.40 ?  44  LYS   B HD3  1 
ATOM   4741 H  HE2  . LYS   B 1 44  ? 52.887 -15.995 12.249  1.00 27.74 ?  44  LYS   B HE2  1 
ATOM   4742 H  HE3  . LYS   B 1 44  ? 53.813 -17.157 12.832  1.00 27.74 ?  44  LYS   B HE3  1 
ATOM   4743 H  HZ1  . LYS   B 1 44  ? 55.032 -15.299 12.349  1.00 29.45 ?  44  LYS   B HZ1  1 
ATOM   4744 H  HZ2  . LYS   B 1 44  ? 55.458 -16.352 11.450  1.00 29.45 ?  44  LYS   B HZ2  1 
ATOM   4745 H  HZ3  . LYS   B 1 44  ? 54.587 -15.299 10.970  1.00 29.45 ?  44  LYS   B HZ3  1 
ATOM   4746 N  N    . HIS   B 1 45  ? 52.659 -19.864 6.803   1.00 12.14 ?  45  HIS   B N    1 
ATOM   4747 C  CA   . HIS   B 1 45  ? 52.669 -20.693 5.601   1.00 12.61 ?  45  HIS   B CA   1 
ATOM   4748 C  C    . HIS   B 1 45  ? 53.689 -21.815 5.760   1.00 14.56 ?  45  HIS   B C    1 
ATOM   4749 O  O    . HIS   B 1 45  ? 54.759 -21.817 5.161   1.00 16.87 ?  45  HIS   B O    1 
ATOM   4750 C  CB   . HIS   B 1 45  ? 52.977 -19.838 4.383   1.00 12.15 ?  45  HIS   B CB   1 
ATOM   4751 C  CG   . HIS   B 1 45  ? 52.113 -18.630 4.281   1.00 12.01 ?  45  HIS   B CG   1 
ATOM   4752 N  ND1  . HIS   B 1 45  ? 50.735 -18.701 4.245   1.00 12.28 ?  45  HIS   B ND1  1 
ATOM   4753 C  CD2  . HIS   B 1 45  ? 52.433 -17.317 4.209   1.00 12.86 ?  45  HIS   B CD2  1 
ATOM   4754 C  CE1  . HIS   B 1 45  ? 50.251 -17.476 4.143   1.00 11.84 ?  45  HIS   B CE1  1 
ATOM   4755 N  NE2  . HIS   B 1 45  ? 51.256 -16.619 4.121   1.00 12.50 ?  45  HIS   B NE2  1 
ATOM   4756 H  H    . HIS   B 1 45  ? 53.238 -19.226 6.790   1.00 14.60 ?  45  HIS   B H    1 
ATOM   4757 H  HA   . HIS   B 1 45  ? 51.788 -21.091 5.478   1.00 15.17 ?  45  HIS   B HA   1 
ATOM   4758 H  HB2  . HIS   B 1 45  ? 53.898 -19.551 4.425   1.00 14.61 ?  45  HIS   B HB2  1 
ATOM   4759 H  HB3  . HIS   B 1 45  ? 52.839 -20.379 3.580   1.00 14.61 ?  45  HIS   B HB3  1 
ATOM   4760 H  HD2  . HIS   B 1 45  ? 53.291 -16.957 4.214   1.00 15.47 ?  45  HIS   B HD2  1 
ATOM   4761 H  HE1  . HIS   B 1 45  ? 49.348 -17.258 4.091   1.00 14.24 ?  45  HIS   B HE1  1 
ATOM   4762 H  HE2  . HIS   B 1 45  ? 51.181 -15.765 4.066   1.00 15.03 ?  45  HIS   B HE2  1 
ATOM   4763 N  N    A GLY   B 1 46  ? 53.318 -22.798 6.577   0.50 15.51 ?  46  GLY   B N    1 
ATOM   4764 N  N    B GLY   B 1 46  ? 53.331 -22.783 6.596   0.50 15.39 ?  46  GLY   B N    1 
ATOM   4765 C  CA   A GLY   B 1 46  ? 54.244 -23.847 6.962   0.50 17.26 ?  46  GLY   B CA   1 
ATOM   4766 C  CA   B GLY   B 1 46  ? 54.255 -23.846 6.930   0.50 16.99 ?  46  GLY   B CA   1 
ATOM   4767 C  C    A GLY   B 1 46  ? 54.291 -25.080 6.082   0.50 18.67 ?  46  GLY   B C    1 
ATOM   4768 C  C    B GLY   B 1 46  ? 54.278 -24.996 5.944   0.50 18.47 ?  46  GLY   B C    1 
ATOM   4769 O  O    A GLY   B 1 46  ? 55.377 -25.541 5.717   0.50 20.62 ?  46  GLY   B O    1 
ATOM   4770 O  O    B GLY   B 1 46  ? 55.314 -25.291 5.338   0.50 19.87 ?  46  GLY   B O    1 
ATOM   4771 H  H    A GLY   B 1 46  ? 52.536 -22.863 6.938   0.50 18.65 ?  46  GLY   B H    1 
ATOM   4772 H  H    B GLY   B 1 46  ? 52.564 -22.834 6.989   0.50 18.50 ?  46  GLY   B H    1 
ATOM   4773 H  HA2  A GLY   B 1 46  ? 55.136 -23.470 6.995   0.50 20.74 ?  46  GLY   B HA2  1 
ATOM   4774 H  HA2  B GLY   B 1 46  ? 55.150 -23.477 6.982   0.50 20.43 ?  46  GLY   B HA2  1 
ATOM   4775 H  HA3  A GLY   B 1 46  ? 54.014 -24.147 7.854   0.50 20.74 ?  46  GLY   B HA3  1 
ATOM   4776 H  HA3  B GLY   B 1 46  ? 54.024 -24.194 7.807   0.50 20.43 ?  46  GLY   B HA3  1 
ATOM   4777 N  N    . GLY   B 1 47  ? 53.132 -25.648 5.755   1.00 18.39 ?  47  GLY   B N    1 
ATOM   4778 C  CA   . GLY   B 1 47  ? 53.069 -26.920 5.064   1.00 16.18 ?  47  GLY   B CA   1 
ATOM   4779 C  C    . GLY   B 1 47  ? 52.165 -26.897 3.847   1.00 14.06 ?  47  GLY   B C    1 
ATOM   4780 O  O    . GLY   B 1 47  ? 51.516 -25.894 3.549   1.00 14.06 ?  47  GLY   B O    1 
ATOM   4781 H  H    A GLY   B 1 47  ? 52.361 -25.323 5.954   0.50 22.10 ?  47  GLY   B H    1 
ATOM   4782 H  H    B GLY   B 1 47  ? 52.366 -25.364 6.027   0.50 22.10 ?  47  GLY   B H    1 
ATOM   4783 H  HA2  . GLY   B 1 47  ? 53.957 -27.179 4.774   1.00 19.45 ?  47  GLY   B HA2  1 
ATOM   4784 H  HA3  . GLY   B 1 47  ? 52.743 -27.600 5.677   1.00 19.45 ?  47  GLY   B HA3  1 
ATOM   4785 N  N    . GLY   B 1 48  ? 52.121 -28.039 3.160   1.00 13.09 ?  48  GLY   B N    1 
ATOM   4786 C  CA   . GLY   B 1 48  ? 51.195 -28.188 2.055   1.00 12.88 ?  48  GLY   B CA   1 
ATOM   4787 C  C    . GLY   B 1 48  ? 51.332 -27.074 1.040   1.00 12.26 ?  48  GLY   B C    1 
ATOM   4788 O  O    . GLY   B 1 48  ? 52.436 -26.608 0.730   1.00 12.97 ?  48  GLY   B O    1 
ATOM   4789 H  H    . GLY   B 1 48  ? 52.617 -28.719 3.307   1.00 15.74 ?  48  GLY   B H    1 
ATOM   4790 H  HA2  . GLY   B 1 48  ? 51.357 -29.030 1.607   1.00 15.49 ?  48  GLY   B HA2  1 
ATOM   4791 H  HA3  . GLY   B 1 48  ? 50.284 -28.185 2.390   1.00 15.49 ?  48  GLY   B HA3  1 
ATOM   4792 N  N    . VAL   B 1 49  ? 50.183 -26.635 0.515   1.00 12.15 ?  49  VAL   B N    1 
ATOM   4793 C  CA   . VAL   B 1 49  ? 50.167 -25.610 -0.526  1.00 12.19 ?  49  VAL   B CA   1 
ATOM   4794 C  C    . VAL   B 1 49  ? 50.827 -24.320 -0.039  1.00 11.48 ?  49  VAL   B C    1 
ATOM   4795 O  O    . VAL   B 1 49  ? 51.615 -23.699 -0.762  1.00 11.97 ?  49  VAL   B O    1 
ATOM   4796 C  CB   . VAL   B 1 49  ? 48.725 -25.360 -1.013  1.00 13.53 ?  49  VAL   B CB   1 
ATOM   4797 C  CG1  . VAL   B 1 49  ? 48.660 -24.102 -1.880  1.00 13.40 ?  49  VAL   B CG1  1 
ATOM   4798 C  CG2  . VAL   B 1 49  ? 48.187 -26.566 -1.769  1.00 14.82 ?  49  VAL   B CG2  1 
ATOM   4799 H  H    . VAL   B 1 49  ? 49.396 -26.916 0.741   1.00 14.61 ?  49  VAL   B H    1 
ATOM   4800 H  HA   . VAL   B 1 49  ? 50.674 -25.929 -1.286  1.00 14.66 ?  49  VAL   B HA   1 
ATOM   4801 H  HB   . VAL   B 1 49  ? 48.153 -25.213 -0.245  1.00 16.27 ?  49  VAL   B HB   1 
ATOM   4802 H  HG11 . VAL   B 1 49  ? 47.834 -24.114 -2.395  1.00 16.11 ?  49  VAL   B HG11 1 
ATOM   4803 H  HG12 . VAL   B 1 49  ? 48.676 -23.316 -1.311  1.00 16.11 ?  49  VAL   B HG12 1 
ATOM   4804 H  HG13 . VAL   B 1 49  ? 49.419 -24.090 -2.484  1.00 16.11 ?  49  VAL   B HG13 1 
ATOM   4805 H  HG21 . VAL   B 1 49  ? 47.280 -26.379 -2.061  1.00 17.82 ?  49  VAL   B HG21 1 
ATOM   4806 H  HG22 . VAL   B 1 49  ? 48.753 -26.732 -2.542  1.00 17.82 ?  49  VAL   B HG22 1 
ATOM   4807 H  HG23 . VAL   B 1 49  ? 48.195 -27.335 -1.182  1.00 17.82 ?  49  VAL   B HG23 1 
ATOM   4808 N  N    . ALA   B 1 50  ? 50.485 -23.876 1.174   1.00 11.38 ?  50  ALA   B N    1 
ATOM   4809 C  CA   . ALA   B 1 50  ? 51.006 -22.600 1.656   1.00 11.29 ?  50  ALA   B CA   1 
ATOM   4810 C  C    . ALA   B 1 50  ? 52.525 -22.635 1.762   1.00 11.56 ?  50  ALA   B C    1 
ATOM   4811 O  O    . ALA   B 1 50  ? 53.206 -21.666 1.397   1.00 11.42 ?  50  ALA   B O    1 
ATOM   4812 C  CB   . ALA   B 1 50  ? 50.380 -22.249 3.003   1.00 11.49 ?  50  ALA   B CB   1 
ATOM   4813 H  H    . ALA   B 1 50  ? 49.977 -24.295 1.730   1.00 13.69 ?  50  ALA   B H    1 
ATOM   4814 H  HA   . ALA   B 1 50  ? 50.776 -21.909 1.026   1.00 13.58 ?  50  ALA   B HA   1 
ATOM   4815 H  HB1  . ALA   B 1 50  ? 50.737 -21.396 3.303   1.00 13.83 ?  50  ALA   B HB1  1 
ATOM   4816 H  HB2  . ALA   B 1 50  ? 49.419 -22.184 2.895   1.00 13.83 ?  50  ALA   B HB2  1 
ATOM   4817 H  HB3  . ALA   B 1 50  ? 50.596 -22.941 3.647   1.00 13.83 ?  50  ALA   B HB3  1 
ATOM   4818 N  N    . GLY   B 1 51  ? 53.077 -23.733 2.274   1.00 12.09 ?  51  GLY   B N    1 
ATOM   4819 C  CA   . GLY   B 1 51  ? 54.522 -23.835 2.345   1.00 12.78 ?  51  GLY   B CA   1 
ATOM   4820 C  C    . GLY   B 1 51  ? 55.170 -23.776 0.977   1.00 12.52 ?  51  GLY   B C    1 
ATOM   4821 O  O    . GLY   B 1 51  ? 56.208 -23.132 0.797   1.00 13.66 ?  51  GLY   B O    1 
ATOM   4822 H  H    . GLY   B 1 51  ? 52.651 -24.419 2.571   1.00 14.54 ?  51  GLY   B H    1 
ATOM   4823 H  HA2  . GLY   B 1 51  ? 54.874 -23.108 2.885   1.00 15.37 ?  51  GLY   B HA2  1 
ATOM   4824 H  HA3  . GLY   B 1 51  ? 54.770 -24.676 2.769   1.00 15.37 ?  51  GLY   B HA3  1 
ATOM   4825 N  N    . ALA   B 1 52  ? 54.566 -24.438 -0.007  1.00 12.24 ?  52  ALA   B N    1 
ATOM   4826 C  CA   . ALA   B 1 52  ? 55.128 -24.440 -1.351  1.00 12.64 ?  52  ALA   B CA   1 
ATOM   4827 C  C    . ALA   B 1 52  ? 55.048 -23.062 -2.000  1.00 11.82 ?  52  ALA   B C    1 
ATOM   4828 O  O    . ALA   B 1 52  ? 56.018 -22.614 -2.631  1.00 12.58 ?  52  ALA   B O    1 
ATOM   4829 C  CB   . ALA   B 1 52  ? 54.421 -25.478 -2.212  1.00 13.36 ?  52  ALA   B CB   1 
ATOM   4830 H  H    . ALA   B 1 52  ? 53.830 -24.881 0.079   1.00 14.72 ?  52  ALA   B H    1 
ATOM   4831 H  HA   . ALA   B 1 52  ? 56.063 -24.686 -1.289  1.00 15.20 ?  52  ALA   B HA   1 
ATOM   4832 H  HB1  . ALA   B 1 52  ? 54.816 -25.464 -3.099  1.00 16.06 ?  52  ALA   B HB1  1 
ATOM   4833 H  HB2  . ALA   B 1 52  ? 54.543 -26.354 -1.811  1.00 16.06 ?  52  ALA   B HB2  1 
ATOM   4834 H  HB3  . ALA   B 1 52  ? 53.481 -25.261 -2.261  1.00 16.06 ?  52  ALA   B HB3  1 
ATOM   4835 N  N    . LEU   B 1 53  ? 53.902 -22.386 -1.881  1.00 11.32 ?  53  LEU   B N    1 
ATOM   4836 C  CA   . LEU   B 1 53  ? 53.788 -21.046 -2.449  1.00 11.67 ?  53  LEU   B CA   1 
ATOM   4837 C  C    . LEU   B 1 53  ? 54.791 -20.102 -1.799  1.00 11.56 ?  53  LEU   B C    1 
ATOM   4838 O  O    . LEU   B 1 53  ? 55.499 -19.355 -2.485  1.00 12.49 ?  53  LEU   B O    1 
ATOM   4839 C  CB   . LEU   B 1 53  ? 52.362 -20.513 -2.280  1.00 12.41 ?  53  LEU   B CB   1 
ATOM   4840 C  CG   . LEU   B 1 53  ? 51.228 -21.233 -3.022  1.00 12.79 ?  53  LEU   B CG   1 
ATOM   4841 C  CD1  . LEU   B 1 53  ? 49.875 -20.640 -2.666  1.00 14.44 ?  53  LEU   B CD1  1 
ATOM   4842 C  CD2  . LEU   B 1 53  ? 51.442 -21.194 -4.526  1.00 14.41 ?  53  LEU   B CD2  1 
ATOM   4843 H  H    . LEU   B 1 53  ? 53.195 -22.674 -1.484  1.00 13.62 ?  53  LEU   B H    1 
ATOM   4844 H  HA   . LEU   B 1 53  ? 53.986 -21.093 -3.402  1.00 14.04 ?  53  LEU   B HA   1 
ATOM   4845 H  HB2  . LEU   B 1 53  ? 52.148 -20.549 -1.338  1.00 14.93 ?  53  LEU   B HB2  1 
ATOM   4846 H  HB3  . LEU   B 1 53  ? 52.355 -19.596 -2.580  1.00 14.93 ?  53  LEU   B HB3  1 
ATOM   4847 H  HG   . LEU   B 1 53  ? 51.213 -22.162 -2.747  1.00 15.39 ?  53  LEU   B HG   1 
ATOM   4848 H  HD11 . LEU   B 1 53  ? 49.179 -21.120 -3.148  1.00 17.36 ?  53  LEU   B HD11 1 
ATOM   4849 H  HD12 . LEU   B 1 53  ? 49.726 -20.732 -1.708  1.00 17.36 ?  53  LEU   B HD12 1 
ATOM   4850 H  HD13 . LEU   B 1 53  ? 49.859 -19.704 -2.912  1.00 17.36 ?  53  LEU   B HD13 1 
ATOM   4851 H  HD21 . LEU   B 1 53  ? 50.707 -21.646 -4.966  1.00 17.33 ?  53  LEU   B HD21 1 
ATOM   4852 H  HD22 . LEU   B 1 53  ? 51.484 -20.270 -4.818  1.00 17.33 ?  53  LEU   B HD22 1 
ATOM   4853 H  HD23 . LEU   B 1 53  ? 52.278 -21.643 -4.737  1.00 17.33 ?  53  LEU   B HD23 1 
ATOM   4854 N  N    . ASN   B 1 54  ? 54.887 -20.137 -0.473  1.00 11.43 ?  54  ASN   B N    1 
ATOM   4855 C  CA   . ASN   B 1 54  ? 55.803 -19.226 0.198   1.00 12.29 ?  54  ASN   B CA   1 
ATOM   4856 C  C    . ASN   B 1 54  ? 57.247 -19.500 -0.202  1.00 12.42 ?  54  ASN   B C    1 
ATOM   4857 O  O    . ASN   B 1 54  ? 58.022 -18.561 -0.433  1.00 13.03 ?  54  ASN   B O    1 
ATOM   4858 C  CB   . ASN   B 1 54  ? 55.635 -19.298 1.708   1.00 12.96 ?  54  ASN   B CB   1 
ATOM   4859 C  CG   . ASN   B 1 54  ? 56.614 -18.388 2.419   1.00 12.93 ?  54  ASN   B CG   1 
ATOM   4860 O  OD1  . ASN   B 1 54  ? 56.630 -17.179 2.180   1.00 13.04 ?  54  ASN   B OD1  1 
ATOM   4861 N  ND2  . ASN   B 1 54  ? 57.463 -18.969 3.264   1.00 14.75 ?  54  ASN   B ND2  1 
ATOM   4862 H  H    . ASN   B 1 54  ? 54.444 -20.664 0.044   1.00 13.75 ?  54  ASN   B H    1 
ATOM   4863 H  HA   . ASN   B 1 54  ? 55.589 -18.323 -0.080  1.00 14.78 ?  54  ASN   B HA   1 
ATOM   4864 H  HB2  . ASN   B 1 54  ? 54.736 -19.016 1.941   1.00 15.58 ?  54  ASN   B HB2  1 
ATOM   4865 H  HB3  . ASN   B 1 54  ? 55.790 -20.207 2.004   1.00 15.58 ?  54  ASN   B HB3  1 
ATOM   4866 H  HD21 . ASN   B 1 54  ? 58.049 -18.498 3.680   1.00 17.74 ?  54  ASN   B HD21 1 
ATOM   4867 H  HD22 . ASN   B 1 54  ? 57.435 -19.822 3.387   1.00 17.74 ?  54  ASN   B HD22 1 
ATOM   4868 N  N    . LYS   B 1 55  ? 57.633 -20.777 -0.278  1.00 13.06 ?  55  LYS   B N    1 
ATOM   4869 C  CA   . LYS   B 1 55  ? 58.990 -21.113 -0.698  1.00 14.43 ?  55  LYS   B CA   1 
ATOM   4870 C  C    . LYS   B 1 55  ? 59.285 -20.569 -2.091  1.00 13.78 ?  55  LYS   B C    1 
ATOM   4871 O  O    . LYS   B 1 55  ? 60.384 -20.063 -2.345  1.00 14.66 ?  55  LYS   B O    1 
ATOM   4872 C  CB   . LYS   B 1 55  ? 59.192 -22.628 -0.643  1.00 16.01 ?  55  LYS   B CB   1 
ATOM   4873 C  CG   . LYS   B 1 55  ? 60.582 -23.087 -1.039  1.00 19.89 ?  55  LYS   B CG   1 
ATOM   4874 C  CD   . LYS   B 1 55  ? 60.748 -24.591 -0.881  1.00 23.31 ?  55  LYS   B CD   1 
ATOM   4875 C  CE   . LYS   B 1 55  ? 60.686 -25.023 0.584   1.00 26.23 ?  55  LYS   B CE   1 
ATOM   4876 N  NZ   . LYS   B 1 55  ? 61.103 -26.435 0.773   1.00 27.71 ?  55  LYS   B NZ   1 
ATOM   4877 H  H    . LYS   B 1 55  ? 57.134 -21.451 -0.096  1.00 15.70 ?  55  LYS   B H    1 
ATOM   4878 H  HA   . LYS   B 1 55  ? 59.619 -20.705 -0.084  1.00 17.35 ?  55  LYS   B HA   1 
ATOM   4879 H  HB2  . LYS   B 1 55  ? 59.028 -22.923 0.265   1.00 19.24 ?  55  LYS   B HB2  1 
ATOM   4880 H  HB3  . LYS   B 1 55  ? 58.561 -23.049 -1.245  1.00 19.24 ?  55  LYS   B HB3  1 
ATOM   4881 H  HG2  . LYS   B 1 55  ? 60.742 -22.861 -1.969  1.00 23.91 ?  55  LYS   B HG2  1 
ATOM   4882 H  HG3  . LYS   B 1 55  ? 61.237 -22.647 -0.472  1.00 23.91 ?  55  LYS   B HG3  1 
ATOM   4883 H  HD2  . LYS   B 1 55  ? 60.035 -25.044 -1.359  1.00 28.01 ?  55  LYS   B HD2  1 
ATOM   4884 H  HD3  . LYS   B 1 55  ? 61.611 -24.858 -1.236  1.00 28.01 ?  55  LYS   B HD3  1 
ATOM   4885 H  HE2  . LYS   B 1 55  ? 61.276 -24.451 1.104   1.00 31.50 ?  55  LYS   B HE2  1 
ATOM   4886 H  HE3  . LYS   B 1 55  ? 59.771 -24.925 0.902   1.00 31.50 ?  55  LYS   B HE3  1 
ATOM   4887 H  HZ1  . LYS   B 1 55  ? 61.042 -26.652 1.633   1.00 33.28 ?  55  LYS   B HZ1  1 
ATOM   4888 H  HZ2  . LYS   B 1 55  ? 60.572 -26.969 0.300   1.00 33.28 ?  55  LYS   B HZ2  1 
ATOM   4889 H  HZ3  . LYS   B 1 55  ? 61.941 -26.539 0.502   1.00 33.28 ?  55  LYS   B HZ3  1 
ATOM   4890 N  N    . ALA   B 1 56  ? 58.313 -20.652 -3.006  1.00 13.42 ?  56  ALA   B N    1 
ATOM   4891 C  CA   . ALA   B 1 56  ? 58.532 -20.145 -4.355  1.00 14.08 ?  56  ALA   B CA   1 
ATOM   4892 C  C    . ALA   B 1 56  ? 58.807 -18.647 -4.348  1.00 13.74 ?  56  ALA   B C    1 
ATOM   4893 O  O    . ALA   B 1 56  ? 59.538 -18.144 -5.213  1.00 15.05 ?  56  ALA   B O    1 
ATOM   4894 C  CB   . ALA   B 1 56  ? 57.336 -20.480 -5.248  1.00 15.33 ?  56  ALA   B CB   1 
ATOM   4895 H  H    . ALA   B 1 56  ? 57.531 -20.983 -2.866  1.00 16.14 ?  56  ALA   B H    1 
ATOM   4896 H  HA   . ALA   B 1 56  ? 59.311 -20.579 -4.725  1.00 16.93 ?  56  ALA   B HA   1 
ATOM   4897 H  HB1  . ALA   B 1 56  ? 57.507 -20.141 -6.142  1.00 18.43 ?  56  ALA   B HB1  1 
ATOM   4898 H  HB2  . ALA   B 1 56  ? 57.230 -21.444 -5.276  1.00 18.43 ?  56  ALA   B HB2  1 
ATOM   4899 H  HB3  . ALA   B 1 56  ? 56.540 -20.068 -4.883  1.00 18.43 ?  56  ALA   B HB3  1 
ATOM   4900 N  N    . THR   B 1 57  ? 58.239 -17.921 -3.382  1.00 13.60 ?  57  THR   B N    1 
ATOM   4901 C  CA   . THR   B 1 57  ? 58.479 -16.485 -3.245  1.00 13.58 ?  57  THR   B CA   1 
ATOM   4902 C  C    . THR   B 1 57  ? 59.733 -16.161 -2.439  1.00 14.53 ?  57  THR   B C    1 
ATOM   4903 O  O    . THR   B 1 57  ? 59.968 -14.987 -2.128  1.00 15.06 ?  57  THR   B O    1 
ATOM   4904 C  CB   . THR   B 1 57  ? 57.278 -15.758 -2.604  1.00 13.05 ?  57  THR   B CB   1 
ATOM   4905 O  OG1  . THR   B 1 57  ? 57.255 -15.980 -1.185  1.00 13.36 ?  57  THR   B OG1  1 
ATOM   4906 C  CG2  . THR   B 1 57  ? 55.961 -16.174 -3.244  1.00 13.17 ?  57  THR   B CG2  1 
ATOM   4907 H  H    . THR   B 1 57  ? 57.694 -18.234 -2.794  1.00 16.35 ?  57  THR   B H    1 
ATOM   4908 H  HA   . THR   B 1 57  ? 58.599 -16.109 -4.132  1.00 16.33 ?  57  THR   B HA   1 
ATOM   4909 H  HB   . THR   B 1 57  ? 57.383 -14.805 -2.765  1.00 15.70 ?  57  THR   B HB   1 
ATOM   4910 H  HG1  . THR   B 1 57  ? 57.184 -16.801 -1.028  1.00 16.07 ?  57  THR   B HG1  1 
ATOM   4911 H  HG21 . THR   B 1 57  ? 55.235 -15.637 -2.894  1.00 15.83 ?  57  THR   B HG21 1 
ATOM   4912 H  HG22 . THR   B 1 57  ? 56.004 -16.054 -4.208  1.00 15.83 ?  57  THR   B HG22 1 
ATOM   4913 H  HG23 . THR   B 1 57  ? 55.780 -17.108 -3.057  1.00 15.83 ?  57  THR   B HG23 1 
ATOM   4914 N  N    . ASN   B 1 58  ? 60.528 -17.164 -2.078  1.00 15.16 ?  58  ASN   B N    1 
ATOM   4915 C  CA   . ASN   B 1 58  ? 61.726 -16.941 -1.272  1.00 17.81 ?  58  ASN   B CA   1 
ATOM   4916 C  C    . ASN   B 1 58  ? 61.385 -16.235 0.039   1.00 15.32 ?  58  ASN   B C    1 
ATOM   4917 O  O    . ASN   B 1 58  ? 62.120 -15.361 0.508   1.00 16.02 ?  58  ASN   B O    1 
ATOM   4918 C  CB   . ASN   B 1 58  ? 62.803 -16.178 -2.048  1.00 25.31 ?  58  ASN   B CB   1 
ATOM   4919 C  CG   . ASN   B 1 58  ? 64.180 -16.324 -1.427  1.00 33.97 ?  58  ASN   B CG   1 
ATOM   4920 O  OD1  . ASN   B 1 58  ? 64.486 -17.338 -0.799  1.00 36.60 ?  58  ASN   B OD1  1 
ATOM   4921 N  ND2  . ASN   B 1 58  ? 65.017 -15.309 -1.598  1.00 39.95 ?  58  ASN   B ND2  1 
ATOM   4922 H  H    . ASN   B 1 58  ? 60.396 -17.990 -2.285  1.00 18.22 ?  58  ASN   B H    1 
ATOM   4923 H  HA   . ASN   B 1 58  ? 62.101 -17.806 -1.045  1.00 21.40 ?  58  ASN   B HA   1 
ATOM   4924 H  HB2  . ASN   B 1 58  ? 62.844 -16.520 -2.956  1.00 30.40 ?  58  ASN   B HB2  1 
ATOM   4925 H  HB3  . ASN   B 1 58  ? 62.581 -15.234 -2.059  1.00 30.40 ?  58  ASN   B HB3  1 
ATOM   4926 H  HD21 . ASN   B 1 58  ? 65.809 -15.347 -1.266  1.00 47.97 ?  58  ASN   B HD21 1 
ATOM   4927 H  HD22 . ASN   B 1 58  ? 64.768 -14.616 -2.040  1.00 47.97 ?  58  ASN   B HD22 1 
ATOM   4928 N  N    . ASN   B 1 59  ? 60.264 -16.629 0.643   1.00 14.78 ?  59  ASN   B N    1 
ATOM   4929 C  CA   . ASN   B 1 59  ? 59.787 -16.163 1.944   1.00 15.01 ?  59  ASN   B CA   1 
ATOM   4930 C  C    . ASN   B 1 59  ? 59.184 -14.759 1.889   1.00 14.28 ?  59  ASN   B C    1 
ATOM   4931 O  O    . ASN   B 1 59  ? 58.758 -14.257 2.934   1.00 14.29 ?  59  ASN   B O    1 
ATOM   4932 C  CB   . ASN   B 1 59  ? 60.860 -16.213 3.047   1.00 16.26 ?  59  ASN   B CB   1 
ATOM   4933 C  CG   . ASN   B 1 59  ? 60.272 -16.402 4.425   1.00 17.13 ?  59  ASN   B CG   1 
ATOM   4934 O  OD1  . ASN   B 1 59  ? 59.443 -17.285 4.641   1.00 17.43 ?  59  ASN   B OD1  1 
ATOM   4935 N  ND2  . ASN   B 1 59  ? 60.690 -15.570 5.369   1.00 17.73 ?  59  ASN   B ND2  1 
ATOM   4936 H  H    . ASN   B 1 59  ? 59.732 -17.209 0.300   1.00 17.77 ?  59  ASN   B H    1 
ATOM   4937 H  HA   . ASN   B 1 59  ? 59.083 -16.762 2.229   1.00 18.05 ?  59  ASN   B HA   1 
ATOM   4938 H  HB2  . ASN   B 1 59  ? 61.459 -16.959 2.885   1.00 19.54 ?  59  ASN   B HB2  1 
ATOM   4939 H  HB3  . ASN   B 1 59  ? 61.358 -15.382 3.055   1.00 19.54 ?  59  ASN   B HB3  1 
ATOM   4940 H  HD21 . ASN   B 1 59  ? 60.383 -15.634 6.173   1.00 21.31 ?  59  ASN   B HD21 1 
ATOM   4941 H  HD22 . ASN   B 1 59  ? 61.270 -14.963 5.182   1.00 21.31 ?  59  ASN   B HD22 1 
ATOM   4942 N  N    . ALA   B 1 60  ? 59.119 -14.111 0.721   1.00 13.94 ?  60  ALA   B N    1 
ATOM   4943 C  CA   . ALA   B 1 60  ? 58.524 -12.778 0.658   1.00 14.11 ?  60  ALA   B CA   1 
ATOM   4944 C  C    . ALA   B 1 60  ? 57.056 -12.802 1.053   1.00 13.10 ?  60  ALA   B C    1 
ATOM   4945 O  O    . ALA   B 1 60  ? 56.554 -11.847 1.663   1.00 13.83 ?  60  ALA   B O    1 
ATOM   4946 C  CB   . ALA   B 1 60  ? 58.691 -12.191 -0.745  1.00 15.23 ?  60  ALA   B CB   1 
ATOM   4947 H  H    . ALA   B 1 60  ? 59.409 -14.419 -0.026  1.00 16.76 ?  60  ALA   B H    1 
ATOM   4948 H  HA   . ALA   B 1 60  ? 58.989 -12.200 1.280   1.00 16.97 ?  60  ALA   B HA   1 
ATOM   4949 H  HB1  . ALA   B 1 60  ? 58.295 -11.309 -0.766  1.00 18.32 ?  60  ALA   B HB1  1 
ATOM   4950 H  HB2  . ALA   B 1 60  ? 59.641 -12.132 -0.950  1.00 18.32 ?  60  ALA   B HB2  1 
ATOM   4951 H  HB3  . ALA   B 1 60  ? 58.253 -12.771 -1.386  1.00 18.32 ?  60  ALA   B HB3  1 
ATOM   4952 N  N    . MET   B 1 61  ? 56.348 -13.877 0.710   1.00 12.62 ?  61  MET   B N    1 
ATOM   4953 C  CA   . MET   B 1 61  ? 54.954 -14.000 1.108   1.00 12.18 ?  61  MET   B CA   1 
ATOM   4954 C  C    . MET   B 1 61  ? 54.821 -14.011 2.628   1.00 12.29 ?  61  MET   B C    1 
ATOM   4955 O  O    . MET   B 1 61  ? 53.918 -13.369 3.183   1.00 12.18 ?  61  MET   B O    1 
ATOM   4956 C  CB   . MET   B 1 61  ? 54.375 -15.269 0.480   1.00 12.10 ?  61  MET   B CB   1 
ATOM   4957 C  CG   . MET   B 1 61  ? 52.931 -15.564 0.887   1.00 11.99 ?  61  MET   B CG   1 
ATOM   4958 S  SD   . MET   B 1 61  ? 52.287 -17.063 0.124   1.00 12.58 ?  61  MET   B SD   1 
ATOM   4959 C  CE   . MET   B 1 61  ? 52.044 -16.497 -1.557  1.00 14.17 ?  61  MET   B CE   1 
ATOM   4960 H  H    . MET   B 1 61  ? 56.653 -14.548 0.256   1.00 15.18 ?  61  MET   B H    1 
ATOM   4961 H  HA   . MET   B 1 61  ? 54.461 -13.247 0.751   1.00 14.65 ?  61  MET   B HA   1 
ATOM   4962 H  HB2  . MET   B 1 61  ? 54.392 -15.180 -0.487  1.00 14.55 ?  61  MET   B HB2  1 
ATOM   4963 H  HB3  . MET   B 1 61  ? 54.915 -16.029 0.747   1.00 14.55 ?  61  MET   B HB3  1 
ATOM   4964 H  HG2  . MET   B 1 61  ? 52.888 -15.681 1.849   1.00 14.43 ?  61  MET   B HG2  1 
ATOM   4965 H  HG3  . MET   B 1 61  ? 52.367 -14.825 0.615   1.00 14.43 ?  61  MET   B HG3  1 
ATOM   4966 H  HE1  . MET   B 1 61  ? 51.668 -17.220 -2.084  1.00 17.04 ?  61  MET   B HE1  1 
ATOM   4967 H  HE2  . MET   B 1 61  ? 51.440 -15.740 -1.553  1.00 17.04 ?  61  MET   B HE2  1 
ATOM   4968 H  HE3  . MET   B 1 61  ? 52.903 -16.232 -1.929  1.00 17.04 ?  61  MET   B HE3  1 
ATOM   4969 N  N    . GLN   B 1 62  ? 55.704 -14.731 3.324   1.00 12.13 ?  62  GLN   B N    1 
ATOM   4970 C  CA   . GLN   B 1 62  ? 55.599 -14.793 4.779   1.00 12.51 ?  62  GLN   B CA   1 
ATOM   4971 C  C    . GLN   B 1 62  ? 55.887 -13.442 5.417   1.00 12.88 ?  62  GLN   B C    1 
ATOM   4972 O  O    . GLN   B 1 62  ? 55.204 -13.043 6.367   1.00 13.31 ?  62  GLN   B O    1 
ATOM   4973 C  CB   . GLN   B 1 62  ? 56.541 -15.855 5.340   1.00 12.78 ?  62  GLN   B CB   1 
ATOM   4974 C  CG   . GLN   B 1 62  ? 56.331 -16.123 6.821   1.00 13.18 ?  62  GLN   B CG   1 
ATOM   4975 C  CD   . GLN   B 1 62  ? 54.959 -16.709 7.071   1.00 12.80 ?  62  GLN   B CD   1 
ATOM   4976 O  OE1  . GLN   B 1 62  ? 54.703 -17.858 6.713   1.00 13.09 ?  62  GLN   B OE1  1 
ATOM   4977 N  NE2  . GLN   B 1 62  ? 54.053 -15.918 7.636   1.00 13.33 ?  62  GLN   B NE2  1 
ATOM   4978 H  H    . GLN   B 1 62  ? 56.352 -15.187 2.982   1.00 14.58 ?  62  GLN   B H    1 
ATOM   4979 H  HA   . GLN   B 1 62  ? 54.693 -15.045 5.011   1.00 15.05 ?  62  GLN   B HA   1 
ATOM   4980 H  HB2  . GLN   B 1 62  ? 56.404 -16.687 4.861   1.00 15.37 ?  62  GLN   B HB2  1 
ATOM   4981 H  HB3  . GLN   B 1 62  ? 57.460 -15.556 5.219   1.00 15.37 ?  62  GLN   B HB3  1 
ATOM   4982 H  HG2  . GLN   B 1 62  ? 56.997 -16.764 7.125   1.00 15.85 ?  62  GLN   B HG2  1 
ATOM   4983 H  HG3  . GLN   B 1 62  ? 56.410 -15.297 7.315   1.00 15.85 ?  62  GLN   B HG3  1 
ATOM   4984 H  HE21 . GLN   B 1 62  ? 54.265 -15.115 7.860   1.00 16.03 ?  62  GLN   B HE21 1 
ATOM   4985 H  HE22 . GLN   B 1 62  ? 53.262 -16.214 7.789   1.00 16.03 ?  62  GLN   B HE22 1 
ATOM   4986 N  N    . VAL   B 1 63  ? 56.898 -12.725 4.922   1.00 13.61 ?  63  VAL   B N    1 
ATOM   4987 C  CA   . VAL   B 1 63  ? 57.204 -11.409 5.480   1.00 14.31 ?  63  VAL   B CA   1 
ATOM   4988 C  C    . VAL   B 1 63  ? 56.011 -10.473 5.304   1.00 13.80 ?  63  VAL   B C    1 
ATOM   4989 O  O    . VAL   B 1 63  ? 55.600 -9.770  6.238   1.00 14.34 ?  63  VAL   B O    1 
ATOM   4990 C  CB   . VAL   B 1 63  ? 58.491 -10.847 4.853   1.00 15.70 ?  63  VAL   B CB   1 
ATOM   4991 C  CG1  . VAL   B 1 63  ? 58.720 -9.409  5.303   1.00 16.29 ?  63  VAL   B CG1  1 
ATOM   4992 C  CG2  . VAL   B 1 63  ? 59.677 -11.723 5.234   1.00 16.35 ?  63  VAL   B CG2  1 
ATOM   4993 H  H    . VAL   B 1 63  ? 57.408 -12.972 4.271   1.00 16.36 ?  63  VAL   B H    1 
ATOM   4994 H  HA   . VAL   B 1 63  ? 57.364 -11.511 6.429   1.00 17.20 ?  63  VAL   B HA   1 
ATOM   4995 H  HB   . VAL   B 1 63  ? 58.414 -10.857 3.888   1.00 18.87 ?  63  VAL   B HB   1 
ATOM   4996 H  HG11 . VAL   B 1 63  ? 59.636 -9.161  5.117   1.00 19.58 ?  63  VAL   B HG11 1 
ATOM   4997 H  HG12 . VAL   B 1 63  ? 58.112 -8.828  4.821   1.00 19.58 ?  63  VAL   B HG12 1 
ATOM   4998 H  HG13 . VAL   B 1 63  ? 58.549 -9.350  6.258   1.00 19.58 ?  63  VAL   B HG13 1 
ATOM   4999 H  HG21 . VAL   B 1 63  ? 60.489 -11.344 4.854   1.00 19.66 ?  63  VAL   B HG21 1 
ATOM   5000 H  HG22 . VAL   B 1 63  ? 59.755 -11.747 6.204   1.00 19.66 ?  63  VAL   B HG22 1 
ATOM   5001 H  HG23 . VAL   B 1 63  ? 59.540 -12.617 4.892   1.00 19.66 ?  63  VAL   B HG23 1 
ATOM   5002 N  N    . GLU   B 1 64  ? 55.442 -10.451 4.097   1.00 13.18 ?  64  GLU   B N    1 
ATOM   5003 C  CA   . GLU   B 1 64  ? 54.268 -9.621  3.828   1.00 12.92 ?  64  GLU   B CA   1 
ATOM   5004 C  C    . GLU   B 1 64  ? 53.090 -10.027 4.708   1.00 12.44 ?  64  GLU   B C    1 
ATOM   5005 O  O    . GLU   B 1 64  ? 52.345 -9.170  5.214   1.00 12.94 ?  64  GLU   B O    1 
ATOM   5006 C  CB   . GLU   B 1 64  ? 53.907 -9.764  2.348   1.00 13.00 ?  64  GLU   B CB   1 
ATOM   5007 C  CG   . GLU   B 1 64  ? 52.637 -9.032  1.918   1.00 13.33 ?  64  GLU   B CG   1 
ATOM   5008 C  CD   . GLU   B 1 64  ? 52.092 -9.527  0.585   1.00 13.93 ?  64  GLU   B CD   1 
ATOM   5009 O  OE1  . GLU   B 1 64  ? 52.280 -10.728 0.257   1.00 14.65 ?  64  GLU   B OE1  1 
ATOM   5010 O  OE2  . GLU   B 1 64  ? 51.458 -8.712  -0.127  1.00 14.71 -1 64  GLU   B OE2  1 
ATOM   5011 H  H    . GLU   B 1 64  ? 55.726 -10.902 3.416   1.00 15.85 ?  64  GLU   B H    1 
ATOM   5012 H  HA   . GLU   B 1 64  ? 54.484 -8.692  4.004   1.00 15.53 ?  64  GLU   B HA   1 
ATOM   5013 H  HB2  . GLU   B 1 64  ? 54.637 -9.404  1.811   1.00 15.63 ?  64  GLU   B HB2  1 
ATOM   5014 H  HB3  . GLU   B 1 64  ? 53.788 -10.701 2.145   1.00 15.63 ?  64  GLU   B HB3  1 
ATOM   5015 H  HG2  . GLU   B 1 64  ? 51.942 -9.163  2.587   1.00 16.03 ?  64  GLU   B HG2  1 
ATOM   5016 H  HG3  . GLU   B 1 64  ? 52.829 -8.085  1.833   1.00 16.03 ?  64  GLU   B HG3  1 
ATOM   5017 N  N    . SER   B 1 65  ? 52.908 -11.335 4.892   1.00 12.22 ?  65  SER   B N    1 
ATOM   5018 C  CA   . SER   B 1 65  ? 51.802 -11.842 5.694   1.00 12.10 ?  65  SER   B CA   1 
ATOM   5019 C  C    . SER   B 1 65  ? 51.939 -11.444 7.156   1.00 12.29 ?  65  SER   B C    1 
ATOM   5020 O  O    . SER   B 1 65  ? 50.942 -11.079 7.794   1.00 12.75 ?  65  SER   B O    1 
ATOM   5021 C  CB   . SER   B 1 65  ? 51.711 -13.364 5.561   1.00 12.57 ?  65  SER   B CB   1 
ATOM   5022 O  OG   . SER   B 1 65  ? 51.368 -13.761 4.240   1.00 12.58 ?  65  SER   B OG   1 
ATOM   5023 H  H    . SER   B 1 65  ? 53.414 -11.956 4.559   1.00 14.70 ?  65  SER   B H    1 
ATOM   5024 H  HA   . SER   B 1 65  ? 50.971 -11.471 5.356   1.00 14.55 ?  65  SER   B HA   1 
ATOM   5025 H  HB2  . SER   B 1 65  ? 52.566 -13.757 5.788   1.00 15.12 ?  65  SER   B HB2  1 
ATOM   5026 H  HB3  . SER   B 1 65  ? 51.026 -13.695 6.167   1.00 15.12 ?  65  SER   B HB3  1 
ATOM   5027 H  HG   . SER   B 1 65  ? 51.950 -13.478 3.694   1.00 15.14 ?  65  SER   B HG   1 
ATOM   5028 N  N    . ASP   B 1 66  ? 53.150 -11.539 7.717   1.00 12.78 ?  66  ASP   B N    1 
ATOM   5029 C  CA   . ASP   B 1 66  ? 53.338 -11.155 9.115   1.00 13.08 ?  66  ASP   B CA   1 
ATOM   5030 C  C    . ASP   B 1 66  ? 53.022 -9.678  9.323   1.00 13.33 ?  66  ASP   B C    1 
ATOM   5031 O  O    . ASP   B 1 66  ? 52.441 -9.293  10.345  1.00 13.91 ?  66  ASP   B O    1 
ATOM   5032 C  CB   . ASP   B 1 66  ? 54.770 -11.458 9.560   1.00 14.35 ?  66  ASP   B CB   1 
ATOM   5033 C  CG   . ASP   B 1 66  ? 55.048 -12.947 9.720   1.00 16.14 ?  66  ASP   B CG   1 
ATOM   5034 O  OD1  . ASP   B 1 66  ? 54.098 -13.760 9.643   1.00 16.87 ?  66  ASP   B OD1  1 
ATOM   5035 O  OD2  . ASP   B 1 66  ? 56.233 -13.304 9.939   1.00 18.97 -1 66  ASP   B OD2  1 
ATOM   5036 H  H    . ASP   B 1 66  ? 53.854 -11.827 7.321   1.00 15.37 ?  66  ASP   B H    1 
ATOM   5037 H  HA   . ASP   B 1 66  ? 52.733 -11.668 9.673   1.00 15.73 ?  66  ASP   B HA   1 
ATOM   5038 H  HB2  . ASP   B 1 66  ? 55.385 -11.115 8.895   1.00 17.25 ?  66  ASP   B HB2  1 
ATOM   5039 H  HB3  . ASP   B 1 66  ? 54.930 -11.025 10.415  1.00 17.25 ?  66  ASP   B HB3  1 
ATOM   5040 N  N    . ASP   B 1 67  ? 53.394 -8.830  8.363   1.00 12.90 ?  67  ASP   B N    1 
ATOM   5041 C  CA   . ASP   B 1 67  ? 53.045 -7.419  8.456   1.00 13.43 ?  67  ASP   B CA   1 
ATOM   5042 C  C    . ASP   B 1 67  ? 51.533 -7.214  8.373   1.00 13.62 ?  67  ASP   B C    1 
ATOM   5043 O  O    . ASP   B 1 67  ? 50.970 -6.405  9.120   1.00 14.25 ?  67  ASP   B O    1 
ATOM   5044 C  CB   . ASP   B 1 67  ? 53.769 -6.644  7.363   1.00 14.87 ?  67  ASP   B CB   1 
ATOM   5045 C  CG   . ASP   B 1 67  ? 53.347 -5.200  7.321   1.00 16.09 ?  67  ASP   B CG   1 
ATOM   5046 O  OD1  . ASP   B 1 67  ? 53.853 -4.392  8.135   1.00 17.32 ?  67  ASP   B OD1  1 
ATOM   5047 O  OD2  . ASP   B 1 67  ? 52.478 -4.891  6.488   1.00 17.17 -1 67  ASP   B OD2  1 
ATOM   5048 H  H    . ASP   B 1 67  ? 53.851 -9.046  7.664   1.00 15.51 ?  67  ASP   B H    1 
ATOM   5049 H  HA   . ASP   B 1 67  ? 53.349 -7.077  9.311   1.00 16.15 ?  67  ASP   B HA   1 
ATOM   5050 H  HB2  . ASP   B 1 67  ? 54.727 -6.671  7.531   1.00 17.88 ?  67  ASP   B HB2  1 
ATOM   5051 H  HB3  . ASP   B 1 67  ? 53.576 -7.052  6.502   1.00 17.88 ?  67  ASP   B HB3  1 
ATOM   5052 N  N    . TYR   B 1 68  ? 50.855 -7.949  7.481   1.00 13.44 ?  68  TYR   B N    1 
ATOM   5053 C  CA   . TYR   B 1 68  ? 49.398 -7.875  7.408   1.00 14.18 ?  68  TYR   B CA   1 
ATOM   5054 C  C    . TYR   B 1 68  ? 48.765 -8.222  8.752   1.00 13.68 ?  68  TYR   B C    1 
ATOM   5055 O  O    . TYR   B 1 68  ? 47.831 -7.548  9.206   1.00 14.00 ?  68  TYR   B O    1 
ATOM   5056 C  CB   . TYR   B 1 68  ? 48.866 -8.810  6.312   1.00 14.67 ?  68  TYR   B CB   1 
ATOM   5057 C  CG   . TYR   B 1 68  ? 47.356 -8.959  6.365   1.00 15.41 ?  68  TYR   B CG   1 
ATOM   5058 C  CD1  . TYR   B 1 68  ? 46.760 -9.909  7.190   1.00 16.43 ?  68  TYR   B CD1  1 
ATOM   5059 C  CD2  . TYR   B 1 68  ? 46.530 -8.121  5.637   1.00 16.30 ?  68  TYR   B CD2  1 
ATOM   5060 C  CE1  . TYR   B 1 68  ? 45.390 -10.027 7.279   1.00 17.63 ?  68  TYR   B CE1  1 
ATOM   5061 C  CE2  . TYR   B 1 68  ? 45.145 -8.243  5.711   1.00 16.89 ?  68  TYR   B CE2  1 
ATOM   5062 C  CZ   . TYR   B 1 68  ? 44.593 -9.195  6.539   1.00 17.26 ?  68  TYR   B CZ   1 
ATOM   5063 O  OH   . TYR   B 1 68  ? 43.225 -9.314  6.636   1.00 17.98 ?  68  TYR   B OH   1 
ATOM   5064 H  H    . TYR   B 1 68  ? 51.218 -8.499  6.918   1.00 16.16 ?  68  TYR   B H    1 
ATOM   5065 H  HA   . TYR   B 1 68  ? 49.146 -6.971  7.180   1.00 17.05 ?  68  TYR   B HA   1 
ATOM   5066 H  HB2  . TYR   B 1 68  ? 49.100 -8.450  5.446   1.00 17.64 ?  68  TYR   B HB2  1 
ATOM   5067 H  HB3  . TYR   B 1 68  ? 49.260 -9.691  6.427   1.00 17.64 ?  68  TYR   B HB3  1 
ATOM   5068 H  HD1  . TYR   B 1 68  ? 47.297 -10.479 7.698   1.00 19.75 ?  68  TYR   B HD1  1 
ATOM   5069 H  HD2  . TYR   B 1 68  ? 46.910 -7.474  5.092   1.00 19.59 ?  68  TYR   B HD2  1 
ATOM   5070 H  HE1  . TYR   B 1 68  ? 45.008 -10.680 7.825   1.00 21.19 ?  68  TYR   B HE1  1 
ATOM   5071 H  HE2  . TYR   B 1 68  ? 44.598 -7.678  5.220   1.00 20.30 ?  68  TYR   B HE2  1 
ATOM   5072 H  HH   . TYR   B 1 68  ? 42.840 -8.763  6.127   1.00 21.61 ?  68  TYR   B HH   1 
ATOM   5073 N  N    . ILE   B 1 69  ? 49.256 -9.283  9.398   1.00 13.43 ?  69  ILE   B N    1 
ATOM   5074 C  CA   . ILE   B 1 69  ? 48.695 -9.713  10.676  1.00 13.98 ?  69  ILE   B CA   1 
ATOM   5075 C  C    . ILE   B 1 69  ? 48.950 -8.669  11.756  1.00 13.34 ?  69  ILE   B C    1 
ATOM   5076 O  O    . ILE   B 1 69  ? 48.081 -8.402  12.594  1.00 13.96 ?  69  ILE   B O    1 
ATOM   5077 C  CB   . ILE   B 1 69  ? 49.263 -11.090 11.069  1.00 14.69 ?  69  ILE   B CB   1 
ATOM   5078 C  CG1  . ILE   B 1 69  ? 48.739 -12.192 10.140  1.00 15.04 ?  69  ILE   B CG1  1 
ATOM   5079 C  CG2  . ILE   B 1 69  ? 48.962 -11.412 12.526  1.00 16.11 ?  69  ILE   B CG2  1 
ATOM   5080 C  CD1  . ILE   B 1 69  ? 47.259 -12.505 10.299  1.00 15.10 ?  69  ILE   B CD1  1 
ATOM   5081 H  H    . ILE   B 1 69  ? 49.915 -9.760  9.124   1.00 16.15 ?  69  ILE   B H    1 
ATOM   5082 H  HA   . ILE   B 1 69  ? 47.739 -9.803  10.579  1.00 16.81 ?  69  ILE   B HA   1 
ATOM   5083 H  HB   . ILE   B 1 69  ? 50.230 -11.051 10.969  1.00 17.66 ?  69  ILE   B HB   1 
ATOM   5084 H  HG12 . ILE   B 1 69  ? 48.887 -11.916 9.222   1.00 18.08 ?  69  ILE   B HG12 1 
ATOM   5085 H  HG13 . ILE   B 1 69  ? 49.236 -13.006 10.319  1.00 18.08 ?  69  ILE   B HG13 1 
ATOM   5086 H  HG21 . ILE   B 1 69  ? 49.106 -12.362 12.669  1.00 19.37 ?  69  ILE   B HG21 1 
ATOM   5087 H  HG22 . ILE   B 1 69  ? 49.556 -10.902 13.097  1.00 19.37 ?  69  ILE   B HG22 1 
ATOM   5088 H  HG23 . ILE   B 1 69  ? 48.039 -11.188 12.714  1.00 19.37 ?  69  ILE   B HG23 1 
ATOM   5089 H  HD11 . ILE   B 1 69  ? 47.019 -13.199 9.667   1.00 18.15 ?  69  ILE   B HD11 1 
ATOM   5090 H  HD12 . ILE   B 1 69  ? 47.094 -12.814 11.204  1.00 18.15 ?  69  ILE   B HD12 1 
ATOM   5091 H  HD13 . ILE   B 1 69  ? 46.742 -11.705 10.123  1.00 18.15 ?  69  ILE   B HD13 1 
ATOM   5092 N  N    . ALA   B 1 70  ? 50.145 -8.079  11.776  1.00 13.55 ?  70  ALA   B N    1 
ATOM   5093 C  CA   . ALA   B 1 70  ? 50.422 -7.041  12.763  1.00 13.70 ?  70  ALA   B CA   1 
ATOM   5094 C  C    . ALA   B 1 70  ? 49.422 -5.896  12.652  1.00 13.93 ?  70  ALA   B C    1 
ATOM   5095 O  O    . ALA   B 1 70  ? 48.981 -5.346  13.666  1.00 14.23 ?  70  ALA   B O    1 
ATOM   5096 C  CB   . ALA   B 1 70  ? 51.852 -6.527  12.603  1.00 14.45 ?  70  ALA   B CB   1 
ATOM   5097 H  H    . ALA   B 1 70  ? 50.792 -8.257  11.245  1.00 16.29 ?  70  ALA   B H    1 
ATOM   5098 H  HA   . ALA   B 1 70  ? 50.348 -7.420  13.655  1.00 16.47 ?  70  ALA   B HA   1 
ATOM   5099 H  HB1  . ALA   B 1 70  ? 52.034 -5.864  13.292  1.00 17.37 ?  70  ALA   B HB1  1 
ATOM   5100 H  HB2  . ALA   B 1 70  ? 52.473 -7.270  12.695  1.00 17.37 ?  70  ALA   B HB2  1 
ATOM   5101 H  HB3  . ALA   B 1 70  ? 51.952 -6.125  11.726  1.00 17.37 ?  70  ALA   B HB3  1 
ATOM   5102 N  N    . THR   B 1 71  ? 49.048 -5.529  11.430  1.00 14.31 ?  71  THR   B N    1 
ATOM   5103 C  CA   . THR   B 1 71  ? 48.152 -4.395  11.225  1.00 15.08 ?  71  THR   B CA   1 
ATOM   5104 C  C    . THR   B 1 71  ? 46.685 -4.759  11.433  1.00 15.46 ?  71  THR   B C    1 
ATOM   5105 O  O    . THR   B 1 71  ? 45.905 -3.938  11.937  1.00 17.09 ?  71  THR   B O    1 
ATOM   5106 C  CB   . THR   B 1 71  ? 48.371 -3.825  9.824   1.00 17.08 ?  71  THR   B CB   1 
ATOM   5107 O  OG1  . THR   B 1 71  ? 49.701 -3.303  9.729   1.00 19.11 ?  71  THR   B OG1  1 
ATOM   5108 C  CG2  . THR   B 1 71  ? 47.361 -2.727  9.512   1.00 18.18 ?  71  THR   B CG2  1 
ATOM   5109 H  H    . THR   B 1 71  ? 49.306 -5.919  10.708  1.00 17.20 ?  71  THR   B H    1 
ATOM   5110 H  HA   . THR   B 1 71  ? 48.381 -3.702  11.864  1.00 18.13 ?  71  THR   B HA   1 
ATOM   5111 H  HB   . THR   B 1 71  ? 48.272 -4.529  9.168   1.00 20.53 ?  71  THR   B HB   1 
ATOM   5112 H  HG1  . THR   B 1 71  ? 49.831 -2.967  8.966   1.00 22.97 ?  71  THR   B HG1  1 
ATOM   5113 H  HG21 . THR   B 1 71  ? 47.667 -2.201  8.755   1.00 21.84 ?  71  THR   B HG21 1 
ATOM   5114 H  HG22 . THR   B 1 71  ? 46.502 -3.116  9.299   1.00 21.84 ?  71  THR   B HG22 1 
ATOM   5115 H  HG23 . THR   B 1 71  ? 47.264 -2.139  10.279  1.00 21.84 ?  71  THR   B HG23 1 
ATOM   5116 N  N    . ASN   B 1 72  ? 46.287 -5.976  11.043  1.00 15.01 ?  72  ASN   B N    1 
ATOM   5117 C  CA   . ASN   B 1 72  ? 44.883 -6.334  10.911  1.00 15.62 ?  72  ASN   B CA   1 
ATOM   5118 C  C    . ASN   B 1 72  ? 44.409 -7.435  11.847  1.00 16.20 ?  72  ASN   B C    1 
ATOM   5119 O  O    . ASN   B 1 72  ? 43.195 -7.595  12.010  1.00 17.37 ?  72  ASN   B O    1 
ATOM   5120 C  CB   . ASN   B 1 72  ? 44.581 -6.758  9.464   1.00 16.63 ?  72  ASN   B CB   1 
ATOM   5121 C  CG   . ASN   B 1 72  ? 44.853 -5.652  8.473   1.00 17.68 ?  72  ASN   B CG   1 
ATOM   5122 O  OD1  . ASN   B 1 72  ? 45.867 -5.655  7.771   1.00 18.76 ?  72  ASN   B OD1  1 
ATOM   5123 N  ND2  . ASN   B 1 72  ? 43.966 -4.679  8.434   1.00 19.38 ?  72  ASN   B ND2  1 
ATOM   5124 H  H    . ASN   B 1 72  ? 46.830 -6.619  10.839  1.00 18.05 ?  72  ASN   B H    1 
ATOM   5125 H  HA   . ASN   B 1 72  ? 44.355 -5.543  11.093  1.00 18.77 ?  72  ASN   B HA   1 
ATOM   5126 H  HB2  . ASN   B 1 72  ? 45.144 -7.514  9.230   1.00 19.99 ?  72  ASN   B HB2  1 
ATOM   5127 H  HB3  . ASN   B 1 72  ? 43.648 -7.001  9.394   1.00 19.99 ?  72  ASN   B HB3  1 
ATOM   5128 H  HD21 . ASN   B 1 72  ? 44.065 -4.021  7.886   1.00 23.29 ?  72  ASN   B HD21 1 
ATOM   5129 H  HD22 . ASN   B 1 72  ? 43.266 -4.711  8.937   1.00 23.29 ?  72  ASN   B HD22 1 
ATOM   5130 N  N    . GLY   B 1 73  ? 45.307 -8.189  12.466  1.00 15.81 ?  73  GLY   B N    1 
ATOM   5131 C  CA   . GLY   B 1 73  ? 44.904 -9.324  13.257  1.00 15.12 ?  73  GLY   B CA   1 
ATOM   5132 C  C    . GLY   B 1 73  ? 44.550 -10.510 12.385  1.00 13.98 ?  73  GLY   B C    1 
ATOM   5133 O  O    . GLY   B 1 73  ? 44.545 -10.428 11.155  1.00 13.96 ?  73  GLY   B O    1 
ATOM   5134 H  H    . GLY   B 1 73  ? 46.157 -8.054  12.442  1.00 19.01 ?  73  GLY   B H    1 
ATOM   5135 H  HA2  . GLY   B 1 73  ? 45.626 -9.575  13.852  1.00 18.17 ?  73  GLY   B HA2  1 
ATOM   5136 H  HA3  . GLY   B 1 73  ? 44.129 -9.088  13.793  1.00 18.17 ?  73  GLY   B HA3  1 
ATOM   5137 N  N    . PRO   B 1 74  ? 44.243 -11.638 13.019  1.00 14.42 ?  74  PRO   B N    1 
ATOM   5138 C  CA   . PRO   B 1 74  ? 43.996 -12.871 12.270  1.00 13.81 ?  74  PRO   B CA   1 
ATOM   5139 C  C    . PRO   B 1 74  ? 42.694 -12.819 11.485  1.00 13.11 ?  74  PRO   B C    1 
ATOM   5140 O  O    . PRO   B 1 74  ? 41.752 -12.086 11.809  1.00 14.64 ?  74  PRO   B O    1 
ATOM   5141 C  CB   . PRO   B 1 74  ? 43.924 -13.936 13.370  1.00 14.84 ?  74  PRO   B CB   1 
ATOM   5142 C  CG   . PRO   B 1 74  ? 43.472 -13.192 14.577  1.00 16.35 ?  74  PRO   B CG   1 
ATOM   5143 C  CD   . PRO   B 1 74  ? 44.146 -11.850 14.472  1.00 15.76 ?  74  PRO   B CD   1 
ATOM   5144 H  HA   . PRO   B 1 74  ? 44.738 -13.057 11.671  1.00 16.61 ?  74  PRO   B HA   1 
ATOM   5145 H  HB2  . PRO   B 1 74  ? 43.278 -14.615 13.118  1.00 17.85 ?  74  PRO   B HB2  1 
ATOM   5146 H  HB3  . PRO   B 1 74  ? 44.801 -14.322 13.506  1.00 17.85 ?  74  PRO   B HB3  1 
ATOM   5147 H  HG2  . PRO   B 1 74  ? 42.507 -13.093 14.561  1.00 19.65 ?  74  PRO   B HG2  1 
ATOM   5148 H  HG3  . PRO   B 1 74  ? 43.759 -13.659 15.375  1.00 19.65 ?  74  PRO   B HG3  1 
ATOM   5149 H  HD2  . PRO   B 1 74  ? 43.598 -11.159 14.886  1.00 18.94 ?  74  PRO   B HD2  1 
ATOM   5150 H  HD3  . PRO   B 1 74  ? 45.032 -11.879 14.867  1.00 18.94 ?  74  PRO   B HD3  1 
ATOM   5151 N  N    . LEU   B 1 75  ? 42.660 -13.633 10.432  1.00 12.60 ?  75  LEU   B N    1 
ATOM   5152 C  CA   . LEU   B 1 75  ? 41.444 -13.853 9.671   1.00 12.68 ?  75  LEU   B CA   1 
ATOM   5153 C  C    . LEU   B 1 75  ? 40.479 -14.718 10.478  1.00 13.14 ?  75  LEU   B C    1 
ATOM   5154 O  O    . LEU   B 1 75  ? 40.829 -15.277 11.519  1.00 14.09 ?  75  LEU   B O    1 
ATOM   5155 C  CB   . LEU   B 1 75  ? 41.766 -14.571 8.360   1.00 12.52 ?  75  LEU   B CB   1 
ATOM   5156 C  CG   . LEU   B 1 75  ? 42.620 -13.822 7.328   1.00 14.72 ?  75  LEU   B CG   1 
ATOM   5157 C  CD1  . LEU   B 1 75  ? 42.806 -14.672 6.074   1.00 16.43 ?  75  LEU   B CD1  1 
ATOM   5158 C  CD2  . LEU   B 1 75  ? 42.036 -12.486 6.970   1.00 17.85 ?  75  LEU   B CD2  1 
ATOM   5159 H  H    . LEU   B 1 75  ? 43.336 -14.071 10.133  1.00 15.15 ?  75  LEU   B H    1 
ATOM   5160 H  HA   . LEU   B 1 75  ? 41.014 -13.007 9.469   1.00 15.24 ?  75  LEU   B HA   1 
ATOM   5161 H  HB2  . LEU   B 1 75  ? 42.235 -15.394 8.573   1.00 15.05 ?  75  LEU   B HB2  1 
ATOM   5162 H  HB3  . LEU   B 1 75  ? 40.927 -14.795 7.921   1.00 15.05 ?  75  LEU   B HB3  1 
ATOM   5163 H  HG   . LEU   B 1 75  ? 43.498 -13.672 7.708   1.00 17.70 ?  75  LEU   B HG   1 
ATOM   5164 H  HD11 . LEU   B 1 75  ? 43.354 -14.181 5.438   1.00 19.75 ?  75  LEU   B HD11 1 
ATOM   5165 H  HD12 . LEU   B 1 75  ? 43.248 -15.503 6.313   1.00 19.75 ?  75  LEU   B HD12 1 
ATOM   5166 H  HD13 . LEU   B 1 75  ? 41.939 -14.860 5.683   1.00 19.75 ?  75  LEU   B HD13 1 
ATOM   5167 H  HD21 . LEU   B 1 75  ? 42.560 -12.093 6.258   1.00 21.45 ?  75  LEU   B HD21 1 
ATOM   5168 H  HD22 . LEU   B 1 75  ? 41.118 -12.611 6.680   1.00 21.45 ?  75  LEU   B HD22 1 
ATOM   5169 H  HD23 . LEU   B 1 75  ? 42.059 -11.914 7.754   1.00 21.45 ?  75  LEU   B HD23 1 
ATOM   5170 N  N    . LYS   B 1 76  ? 39.242 -14.813 9.982   1.00 14.37 ?  76  LYS   B N    1 
ATOM   5171 C  CA   . LYS   B 1 76  ? 38.264 -15.790 10.448  1.00 15.78 ?  76  LYS   B CA   1 
ATOM   5172 C  C    . LYS   B 1 76  ? 38.357 -17.056 9.600   1.00 14.51 ?  76  LYS   B C    1 
ATOM   5173 O  O    . LYS   B 1 76  ? 38.630 -16.991 8.403   1.00 14.07 ?  76  LYS   B O    1 
ATOM   5174 C  CB   . LYS   B 1 76  ? 36.840 -15.228 10.283  1.00 18.55 ?  76  LYS   B CB   1 
ATOM   5175 C  CG   . LYS   B 1 76  ? 36.569 -13.831 10.879  1.00 20.85 ?  76  LYS   B CG   1 
ATOM   5176 C  CD   . LYS   B 1 76  ? 35.165 -13.296 10.516  1.00 22.40 ?  76  LYS   B CD   1 
ATOM   5177 C  CE   . LYS   B 1 76  ? 34.889 -11.946 11.162  1.00 24.48 ?  76  LYS   B CE   1 
ATOM   5178 N  NZ   . LYS   B 1 76  ? 33.603 -11.345 10.708  1.00 25.23 ?  76  LYS   B NZ   1 
ATOM   5179 H  H    . LYS   B 1 76  ? 38.939 -14.309 9.357   1.00 17.28 ?  76  LYS   B H    1 
ATOM   5180 H  HA   . LYS   B 1 76  ? 38.414 -16.015 11.380  1.00 18.97 ?  76  LYS   B HA   1 
ATOM   5181 H  HB2  . LYS   B 1 76  ? 36.640 -15.176 9.336   1.00 22.29 ?  76  LYS   B HB2  1 
ATOM   5182 H  HB3  . LYS   B 1 76  ? 36.217 -15.840 10.707  1.00 22.29 ?  76  LYS   B HB3  1 
ATOM   5183 H  HG2  . LYS   B 1 76  ? 36.633 -13.877 11.846  1.00 25.05 ?  76  LYS   B HG2  1 
ATOM   5184 H  HG3  . LYS   B 1 76  ? 37.227 -13.204 10.533  1.00 25.05 ?  76  LYS   B HG3  1 
ATOM   5185 H  HD2  . LYS   B 1 76  ? 35.102 -13.187 9.553   1.00 26.92 ?  76  LYS   B HD2  1 
ATOM   5186 H  HD3  . LYS   B 1 76  ? 34.493 -13.922 10.826  1.00 26.92 ?  76  LYS   B HD3  1 
ATOM   5187 H  HE2  . LYS   B 1 76  ? 34.844 -12.059 12.124  1.00 29.41 ?  76  LYS   B HE2  1 
ATOM   5188 H  HE3  . LYS   B 1 76  ? 35.605 -11.332 10.932  1.00 29.41 ?  76  LYS   B HE3  1 
ATOM   5189 H  HZ1  . LYS   B 1 76  ? 33.475 -10.558 11.105  1.00 30.31 ?  76  LYS   B HZ1  1 
ATOM   5190 H  HZ2  . LYS   B 1 76  ? 33.617 -11.222 9.826   1.00 30.31 ?  76  LYS   B HZ2  1 
ATOM   5191 H  HZ3  . LYS   B 1 76  ? 32.924 -11.884 10.912  1.00 30.31 ?  76  LYS   B HZ3  1 
ATOM   5192 N  N    . VAL   B 1 77  ? 38.110 -18.218 10.220  1.00 14.57 ?  77  VAL   B N    1 
ATOM   5193 C  CA   . VAL   B 1 77  ? 37.895 -19.423 9.425   1.00 14.67 ?  77  VAL   B CA   1 
ATOM   5194 C  C    . VAL   B 1 77  ? 36.698 -19.181 8.514   1.00 13.43 ?  77  VAL   B C    1 
ATOM   5195 O  O    . VAL   B 1 77  ? 35.634 -18.738 8.967   1.00 13.96 ?  77  VAL   B O    1 
ATOM   5196 C  CB   . VAL   B 1 77  ? 37.699 -20.652 10.329  1.00 16.12 ?  77  VAL   B CB   1 
ATOM   5197 C  CG1  . VAL   B 1 77  ? 37.413 -21.885 9.477   1.00 17.00 ?  77  VAL   B CG1  1 
ATOM   5198 C  CG2  . VAL   B 1 77  ? 38.934 -20.883 11.208  1.00 17.87 ?  77  VAL   B CG2  1 
ATOM   5199 H  H    . VAL   B 1 77  ? 38.071 -18.329 11.067  1.00 17.52 ?  77  VAL   B H    1 
ATOM   5200 H  HA   . VAL   B 1 77  ? 38.668 -19.582 8.863   1.00 17.63 ?  77  VAL   B HA   1 
ATOM   5201 H  HB   . VAL   B 1 77  ? 36.935 -20.502 10.908  1.00 19.38 ?  77  VAL   B HB   1 
ATOM   5202 H  HG11 . VAL   B 1 77  ? 37.466 -22.673 10.042  1.00 20.43 ?  77  VAL   B HG11 1 
ATOM   5203 H  HG12 . VAL   B 1 77  ? 36.521 -21.812 9.100   1.00 20.43 ?  77  VAL   B HG12 1 
ATOM   5204 H  HG13 . VAL   B 1 77  ? 38.071 -21.940 8.771   1.00 20.43 ?  77  VAL   B HG13 1 
ATOM   5205 H  HG21 . VAL   B 1 77  ? 38.797 -21.685 11.732  1.00 21.48 ?  77  VAL   B HG21 1 
ATOM   5206 H  HG22 . VAL   B 1 77  ? 39.708 -20.983 10.636  1.00 21.48 ?  77  VAL   B HG22 1 
ATOM   5207 H  HG23 . VAL   B 1 77  ? 39.047 -20.117 11.792  1.00 21.48 ?  77  VAL   B HG23 1 
ATOM   5208 N  N    . GLY   B 1 78  ? 36.875 -19.458 7.223   1.00 13.35 ?  78  GLY   B N    1 
ATOM   5209 C  CA   . GLY   B 1 78  ? 35.898 -19.134 6.209   1.00 12.91 ?  78  GLY   B CA   1 
ATOM   5210 C  C    . GLY   B 1 78  ? 36.141 -17.813 5.515   1.00 12.56 ?  78  GLY   B C    1 
ATOM   5211 O  O    . GLY   B 1 78  ? 35.464 -17.523 4.526   1.00 12.88 ?  78  GLY   B O    1 
ATOM   5212 H  H    . GLY   B 1 78  ? 37.578 -19.842 6.907   1.00 16.05 ?  78  GLY   B H    1 
ATOM   5213 H  HA2  . GLY   B 1 78  ? 35.894 -19.830 5.536   1.00 15.53 ?  78  GLY   B HA2  1 
ATOM   5214 H  HA3  . GLY   B 1 78  ? 35.018 -19.099 6.615   1.00 15.53 ?  78  GLY   B HA3  1 
ATOM   5215 N  N    . GLY   B 1 79  ? 37.095 -17.013 5.999   1.00 12.48 ?  79  GLY   B N    1 
ATOM   5216 C  CA   . GLY   B 1 79  ? 37.394 -15.715 5.431   1.00 12.20 ?  79  GLY   B CA   1 
ATOM   5217 C  C    . GLY   B 1 79  ? 38.631 -15.726 4.544   1.00 11.59 ?  79  GLY   B C    1 
ATOM   5218 O  O    . GLY   B 1 79  ? 39.242 -16.761 4.283   1.00 12.20 ?  79  GLY   B O    1 
ATOM   5219 H  H    . GLY   B 1 79  ? 37.599 -17.216 6.662   1.00 15.01 ?  79  GLY   B H    1 
ATOM   5220 H  HA2  . GLY   B 1 79  ? 36.640 -15.412 4.900   1.00 14.67 ?  79  GLY   B HA2  1 
ATOM   5221 H  HA3  . GLY   B 1 79  ? 37.537 -15.078 6.148   1.00 14.67 ?  79  GLY   B HA3  1 
ATOM   5222 N  N    . SER   B 1 80  ? 38.989 -14.526 4.072   1.00 11.94 ?  80  SER   B N    1 
ATOM   5223 C  CA   . SER   B 1 80  ? 40.098 -14.392 3.137   1.00 11.62 ?  80  SER   B CA   1 
ATOM   5224 C  C    . SER   B 1 80  ? 40.683 -12.984 3.195   1.00 11.52 ?  80  SER   B C    1 
ATOM   5225 O  O    . SER   B 1 80  ? 40.060 -12.051 3.709   1.00 12.82 ?  80  SER   B O    1 
ATOM   5226 C  CB   . SER   B 1 80  ? 39.656 -14.687 1.700   1.00 12.07 ?  80  SER   B CB   1 
ATOM   5227 O  OG   . SER   B 1 80  ? 38.821 -13.660 1.190   1.00 13.09 ?  80  SER   B OG   1 
ATOM   5228 H  H    . SER   B 1 80  ? 38.611 -13.782 4.281   1.00 14.36 ?  80  SER   B H    1 
ATOM   5229 H  HA   . SER   B 1 80  ? 40.789 -15.020 3.381   1.00 13.97 ?  80  SER   B HA   1 
ATOM   5230 H  HB2  . SER   B 1 80  ? 40.437 -14.756 1.132   1.00 14.52 ?  80  SER   B HB2  1 
ATOM   5231 H  HB3  . SER   B 1 80  ? 39.163 -15.524 1.686   1.00 14.52 ?  80  SER   B HB3  1 
ATOM   5232 H  HG   . SER   B 1 80  ? 38.126 -13.592 1.665   1.00 15.74 ?  80  SER   B HG   1 
ATOM   5233 N  N    . CYS   B 1 81  ? 41.877 -12.834 2.615   1.00 11.38 ?  81  CYS   B N    1 
ATOM   5234 C  CA   . CYS   B 1 81  ? 42.410 -11.519 2.301   1.00 11.75 ?  81  CYS   B CA   1 
ATOM   5235 C  C    . CYS   B 1 81  ? 43.181 -11.605 0.994   1.00 10.88 ?  81  CYS   B C    1 
ATOM   5236 O  O    . CYS   B 1 81  ? 43.702 -12.664 0.622   1.00 11.89 ?  81  CYS   B O    1 
ATOM   5237 C  CB   . CYS   B 1 81  ? 43.301 -10.969 3.423   1.00 12.50 ?  81  CYS   B CB   1 
ATOM   5238 S  SG   . CYS   B 1 81  ? 44.825 -11.902 3.668   1.00 12.57 ?  81  CYS   B SG   1 
ATOM   5239 H  H    . CYS   B 1 81  ? 42.396 -13.486 2.390   1.00 13.69 ?  81  CYS   B H    1 
ATOM   5240 H  HA   . CYS   B 1 81  ? 41.674 -10.900 2.175   1.00 14.13 ?  81  CYS   B HA   1 
ATOM   5241 H  HB2  . CYS   B 1 81  ? 43.545 -10.053 3.216   1.00 15.03 ?  81  CYS   B HB2  1 
ATOM   5242 H  HB3  . CYS   B 1 81  ? 42.801 -10.988 4.260   1.00 15.03 ?  81  CYS   B HB3  1 
ATOM   5243 H  HG   . CYS   B 1 81  ? 45.453 -11.409 4.565   1.00 15.12 ?  81  CYS   B HG   1 
ATOM   5244 N  N    . VAL   B 1 82  ? 43.283 -10.459 0.320   1.00 11.38 ?  82  VAL   B N    1 
ATOM   5245 C  CA   . VAL   B 1 82  ? 44.044 -10.323 -0.919  1.00 11.39 ?  82  VAL   B CA   1 
ATOM   5246 C  C    . VAL   B 1 82  ? 45.387 -9.684  -0.601  1.00 11.67 ?  82  VAL   B C    1 
ATOM   5247 O  O    . VAL   B 1 82  ? 45.442 -8.566  -0.069  1.00 12.71 ?  82  VAL   B O    1 
ATOM   5248 C  CB   . VAL   B 1 82  ? 43.292 -9.480  -1.960  1.00 12.54 ?  82  VAL   B CB   1 
ATOM   5249 C  CG1  . VAL   B 1 82  ? 44.137 -9.325  -3.221  1.00 14.00 ?  82  VAL   B CG1  1 
ATOM   5250 C  CG2  . VAL   B 1 82  ? 41.935 -10.084 -2.277  1.00 13.54 ?  82  VAL   B CG2  1 
ATOM   5251 H  H    . VAL   B 1 82  ? 42.906 -9.719  0.565   1.00 13.69 ?  82  VAL   B H    1 
ATOM   5252 H  HA   . VAL   B 1 82  ? 44.202 -11.202 -1.297  1.00 13.70 ?  82  VAL   B HA   1 
ATOM   5253 H  HB   . VAL   B 1 82  ? 43.141 -8.595  -1.595  1.00 15.09 ?  82  VAL   B HB   1 
ATOM   5254 H  HG11 . VAL   B 1 82  ? 43.570 -9.009  -3.943  1.00 16.83 ?  82  VAL   B HG11 1 
ATOM   5255 H  HG12 . VAL   B 1 82  ? 44.842 -8.677  -3.053  1.00 16.83 ?  82  VAL   B HG12 1 
ATOM   5256 H  HG13 . VAL   B 1 82  ? 44.520 -10.182 -3.453  1.00 16.83 ?  82  VAL   B HG13 1 
ATOM   5257 H  HG21 . VAL   B 1 82  ? 41.497 -9.552  -2.962  1.00 16.28 ?  82  VAL   B HG21 1 
ATOM   5258 H  HG22 . VAL   B 1 82  ? 42.056 -10.994 -2.598  1.00 16.28 ?  82  VAL   B HG22 1 
ATOM   5259 H  HG23 . VAL   B 1 82  ? 41.391 -10.092 -1.471  1.00 16.28 ?  82  VAL   B HG23 1 
ATOM   5260 N  N    . LEU   B 1 83  ? 46.466 -10.371 -0.969  1.00 11.30 ?  83  LEU   B N    1 
ATOM   5261 C  CA   . LEU   B 1 83  ? 47.821 -9.856  -0.848  1.00 11.34 ?  83  LEU   B CA   1 
ATOM   5262 C  C    . LEU   B 1 83  ? 48.525 -9.995  -2.197  1.00 11.26 ?  83  LEU   B C    1 
ATOM   5263 O  O    . LEU   B 1 83  ? 47.922 -10.405 -3.194  1.00 11.43 ?  83  LEU   B O    1 
ATOM   5264 C  CB   . LEU   B 1 83  ? 48.574 -10.537 0.302   1.00 12.06 ?  83  LEU   B CB   1 
ATOM   5265 C  CG   . LEU   B 1 83  ? 48.073 -10.168 1.703   1.00 13.11 ?  83  LEU   B CG   1 
ATOM   5266 C  CD1  . LEU   B 1 83  ? 48.710 -11.030 2.770   1.00 13.72 ?  83  LEU   B CD1  1 
ATOM   5267 C  CD2  . LEU   B 1 83  ? 48.283 -8.685  2.020   1.00 14.01 ?  83  LEU   B CD2  1 
ATOM   5268 H  H    . LEU   B 1 83  ? 46.431 -11.168 -1.300  1.00 13.59 ?  83  LEU   B H    1 
ATOM   5269 H  HA   . LEU   B 1 83  ? 47.770 -8.911  -0.646  1.00 13.64 ?  83  LEU   B HA   1 
ATOM   5270 H  HB2  . LEU   B 1 83  ? 48.494 -11.496 0.203   1.00 14.50 ?  83  LEU   B HB2  1 
ATOM   5271 H  HB3  . LEU   B 1 83  ? 49.511 -10.282 0.248   1.00 14.50 ?  83  LEU   B HB3  1 
ATOM   5272 H  HG   . LEU   B 1 83  ? 47.121 -10.332 1.731   1.00 15.77 ?  83  LEU   B HG   1 
ATOM   5273 H  HD11 . LEU   B 1 83  ? 48.356 -10.773 3.637   1.00 16.50 ?  83  LEU   B HD11 1 
ATOM   5274 H  HD12 . LEU   B 1 83  ? 48.494 -11.962 2.593   1.00 16.50 ?  83  LEU   B HD12 1 
ATOM   5275 H  HD13 . LEU   B 1 83  ? 49.669 -10.906 2.754   1.00 16.50 ?  83  LEU   B HD13 1 
ATOM   5276 H  HD21 . LEU   B 1 83  ? 48.092 -8.533  2.958   1.00 16.84 ?  83  LEU   B HD21 1 
ATOM   5277 H  HD22 . LEU   B 1 83  ? 49.203 -8.446  1.826   1.00 16.84 ?  83  LEU   B HD22 1 
ATOM   5278 H  HD23 . LEU   B 1 83  ? 47.683 -8.156  1.470   1.00 16.84 ?  83  LEU   B HD23 1 
ATOM   5279 N  N    . SER   B 1 84  ? 49.801 -9.614  -2.251  1.00 12.52 ?  84  SER   B N    1 
ATOM   5280 C  CA   . SER   B 1 84  ? 50.542 -9.730  -3.501  1.00 12.81 ?  84  SER   B CA   1 
ATOM   5281 C  C    . SER   B 1 84  ? 50.696 -11.190 -3.923  1.00 11.89 ?  84  SER   B C    1 
ATOM   5282 O  O    . SER   B 1 84  ? 50.813 -12.092 -3.096  1.00 11.70 ?  84  SER   B O    1 
ATOM   5283 C  CB   . SER   B 1 84  ? 51.938 -9.123  -3.349  1.00 14.39 ?  84  SER   B CB   1 
ATOM   5284 O  OG   . SER   B 1 84  ? 52.682 -9.328  -4.535  1.00 16.19 ?  84  SER   B OG   1 
ATOM   5285 H  H    . SER   B 1 84  ? 50.243 -9.274  -1.594  1.00 15.05 ?  84  SER   B H    1 
ATOM   5286 H  HA   . SER   B 1 84  ? 50.076 -9.257  -4.205  1.00 15.41 ?  84  SER   B HA   1 
ATOM   5287 H  HB2  . SER   B 1 84  ? 51.856 -8.167  -3.180  1.00 17.30 ?  84  SER   B HB2  1 
ATOM   5288 H  HB3  . SER   B 1 84  ? 52.399 -9.549  -2.611  1.00 17.30 ?  84  SER   B HB3  1 
ATOM   5289 H  HG   . SER   B 1 84  ? 53.450 -8.980  -4.459  1.00 19.46 ?  84  SER   B HG   1 
ATOM   5290 N  N    . GLY   B 1 85  ? 50.763 -11.408 -5.229  1.00 12.90 ?  85  GLY   B N    1 
ATOM   5291 C  CA   . GLY   B 1 85  ? 51.109 -12.697 -5.777  1.00 13.43 ?  85  GLY   B CA   1 
ATOM   5292 C  C    . GLY   B 1 85  ? 52.579 -12.884 -6.085  1.00 12.82 ?  85  GLY   B C    1 
ATOM   5293 O  O    . GLY   B 1 85  ? 52.957 -13.962 -6.548  1.00 13.14 ?  85  GLY   B O    1 
ATOM   5294 H  H    . GLY   B 1 85  ? 50.614 -10.813 -5.821  1.00 15.52 ?  85  GLY   B H    1 
ATOM   5295 H  HA2  . GLY   B 1 85  ? 50.848 -13.391 -5.148  1.00 16.14 ?  85  GLY   B HA2  1 
ATOM   5296 H  HA3  . GLY   B 1 85  ? 50.616 -12.835 -6.595  1.00 16.14 ?  85  GLY   B HA3  1 
ATOM   5297 N  N    . HIS   B 1 86  ? 53.429 -11.884 -5.858  1.00 12.80 ?  86  HIS   B N    1 
ATOM   5298 C  CA   . HIS   B 1 86  ? 54.892 -12.052 -5.942  1.00 12.91 ?  86  HIS   B CA   1 
ATOM   5299 C  C    . HIS   B 1 86  ? 55.266 -12.560 -7.332  1.00 13.02 ?  86  HIS   B C    1 
ATOM   5300 O  O    . HIS   B 1 86  ? 54.882 -11.937 -8.333  1.00 13.62 ?  86  HIS   B O    1 
ATOM   5301 C  CB   . HIS   B 1 86  ? 55.383 -12.902 -4.770  1.00 13.16 ?  86  HIS   B CB   1 
ATOM   5302 C  CG   . HIS   B 1 86  ? 55.070 -12.302 -3.442  1.00 13.08 ?  86  HIS   B CG   1 
ATOM   5303 N  ND1  . HIS   B 1 86  ? 55.891 -11.381 -2.829  1.00 14.68 ?  86  HIS   B ND1  1 
ATOM   5304 C  CD2  . HIS   B 1 86  ? 53.997 -12.457 -2.629  1.00 13.56 ?  86  HIS   B CD2  1 
ATOM   5305 C  CE1  . HIS   B 1 86  ? 55.337 -10.998 -1.694  1.00 14.34 ?  86  HIS   B CE1  1 
ATOM   5306 N  NE2  . HIS   B 1 86  ? 54.186 -11.631 -1.550  1.00 13.58 ?  86  HIS   B NE2  1 
ATOM   5307 H  H    . HIS   B 1 86  ? 53.186 -11.088 -5.662  1.00 15.40 ?  86  HIS   B H    1 
ATOM   5308 H  HA   . HIS   B 1 86  ? 55.298 -11.183 -5.842  1.00 15.53 ?  86  HIS   B HA   1 
ATOM   5309 H  HB2  . HIS   B 1 86  ? 54.973 -13.779 -4.814  1.00 15.82 ?  86  HIS   B HB2  1 
ATOM   5310 H  HB3  . HIS   B 1 86  ? 56.354 -12.994 -4.834  1.00 15.82 ?  86  HIS   B HB3  1 
ATOM   5311 H  HD2  . HIS   B 1 86  ? 53.264 -13.013 -2.784  1.00 16.31 ?  86  HIS   B HD2  1 
ATOM   5312 H  HE1  . HIS   B 1 86  ? 55.700 -10.396 -1.089  1.00 17.24 ?  86  HIS   B HE1  1 
ATOM   5313 H  HE2  . HIS   B 1 86  ? 53.651 -11.560 -0.881  1.00 16.33 ?  86  HIS   B HE2  1 
ATOM   5314 N  N    . ASN   B 1 87  ? 56.031 -13.647 -7.445  1.00 13.30 ?  87  ASN   B N    1 
ATOM   5315 C  CA   . ASN   B 1 87  ? 56.424 -14.215 -8.725  1.00 14.12 ?  87  ASN   B CA   1 
ATOM   5316 C  C    . ASN   B 1 87  ? 55.445 -15.262 -9.225  1.00 13.80 ?  87  ASN   B C    1 
ATOM   5317 O  O    . ASN   B 1 87  ? 55.761 -15.978 -10.178 1.00 15.38 ?  87  ASN   B O    1 
ATOM   5318 C  CB   . ASN   B 1 87  ? 57.823 -14.837 -8.612  1.00 15.85 ?  87  ASN   B CB   1 
ATOM   5319 C  CG   . ASN   B 1 87  ? 57.883 -15.959 -7.579  1.00 16.68 ?  87  ASN   B CG   1 
ATOM   5320 O  OD1  . ASN   B 1 87  ? 57.244 -15.888 -6.521  1.00 15.52 ?  87  ASN   B OD1  1 
ATOM   5321 N  ND2  . ASN   B 1 87  ? 58.626 -17.020 -7.901  1.00 19.12 ?  87  ASN   B ND2  1 
ATOM   5322 H  H    . ASN   B 1 87  ? 56.333 -14.090 -6.772  1.00 16.00 ?  87  ASN   B H    1 
ATOM   5323 H  HA   . ASN   B 1 87  ? 56.465 -13.506 -9.382  1.00 16.98 ?  87  ASN   B HA   1 
ATOM   5324 H  HB2  . ASN   B 1 87  ? 58.075 -15.204 -9.477  1.00 19.05 ?  87  ASN   B HB2  1 
ATOM   5325 H  HB3  . ASN   B 1 87  ? 58.453 -14.149 -8.349  1.00 19.05 ?  87  ASN   B HB3  1 
ATOM   5326 H  HD21 . ASN   B 1 87  ? 58.694 -17.676 -7.355  1.00 22.97 ?  87  ASN   B HD21 1 
ATOM   5327 H  HD22 . ASN   B 1 87  ? 59.049 -17.039 -8.654  1.00 22.97 ?  87  ASN   B HD22 1 
ATOM   5328 N  N    . LEU   B 1 88  ? 54.267 -15.360 -8.609  1.00 12.82 ?  88  LEU   B N    1 
ATOM   5329 C  CA   . LEU   B 1 88  ? 53.288 -16.390 -8.933  1.00 13.09 ?  88  LEU   B CA   1 
ATOM   5330 C  C    . LEU   B 1 88  ? 52.053 -15.872 -9.653  1.00 12.74 ?  88  LEU   B C    1 
ATOM   5331 O  O    . LEU   B 1 88  ? 51.442 -16.621 -10.430 1.00 14.29 ?  88  LEU   B O    1 
ATOM   5332 C  CB   . LEU   B 1 88  ? 52.820 -17.072 -7.642  1.00 13.76 ?  88  LEU   B CB   1 
ATOM   5333 C  CG   . LEU   B 1 88  ? 53.936 -17.731 -6.842  1.00 15.91 ?  88  LEU   B CG   1 
ATOM   5334 C  CD1  . LEU   B 1 88  ? 53.447 -18.047 -5.439  1.00 17.23 ?  88  LEU   B CD1  1 
ATOM   5335 C  CD2  . LEU   B 1 88  ? 54.396 -18.983 -7.555  1.00 18.86 ?  88  LEU   B CD2  1 
ATOM   5336 H  H    . LEU   B 1 88  ? 54.009 -14.830 -7.977  1.00 15.42 ?  88  LEU   B H    1 
ATOM   5337 H  HA   . LEU   B 1 88  ? 53.702 -17.056 -9.494  1.00 15.74 ?  88  LEU   B HA   1 
ATOM   5338 H  HB2  . LEU   B 1 88  ? 52.399 -16.408 -7.073  1.00 16.54 ?  88  LEU   B HB2  1 
ATOM   5339 H  HB3  . LEU   B 1 88  ? 52.176 -17.760 -7.873  1.00 16.54 ?  88  LEU   B HB3  1 
ATOM   5340 H  HG   . LEU   B 1 88  ? 54.689 -17.119 -6.777  1.00 19.12 ?  88  LEU   B HG   1 
ATOM   5341 H  HD11 . LEU   B 1 88  ? 54.088 -18.629 -5.009  1.00 20.71 ?  88  LEU   B HD11 1 
ATOM   5342 H  HD12 . LEU   B 1 88  ? 53.363 -17.217 -4.943  1.00 20.71 ?  88  LEU   B HD12 1 
ATOM   5343 H  HD13 . LEU   B 1 88  ? 52.585 -18.483 -5.503  1.00 20.71 ?  88  LEU   B HD13 1 
ATOM   5344 H  HD21 . LEU   B 1 88  ? 55.062 -19.427 -7.008  1.00 22.66 ?  88  LEU   B HD21 1 
ATOM   5345 H  HD22 . LEU   B 1 88  ? 53.634 -19.567 -7.688  1.00 22.66 ?  88  LEU   B HD22 1 
ATOM   5346 H  HD23 . LEU   B 1 88  ? 54.780 -18.739 -8.412  1.00 22.66 ?  88  LEU   B HD23 1 
ATOM   5347 N  N    . ALA   B 1 89  ? 51.649 -14.635 -9.388  1.00 12.26 ?  89  ALA   B N    1 
ATOM   5348 C  CA   . ALA   B 1 89  ? 50.351 -14.147 -9.832  1.00 11.64 ?  89  ALA   B CA   1 
ATOM   5349 C  C    . ALA   B 1 89  ? 50.320 -12.655 -9.553  1.00 11.96 ?  89  ALA   B C    1 
ATOM   5350 O  O    . ALA   B 1 89  ? 51.161 -12.132 -8.821  1.00 12.76 ?  89  ALA   B O    1 
ATOM   5351 C  CB   . ALA   B 1 89  ? 49.218 -14.829 -9.070  1.00 11.94 ?  89  ALA   B CB   1 
ATOM   5352 H  H    . ALA   B 1 89  ? 52.098 -14.053 -8.936  1.00 14.74 ?  89  ALA   B H    1 
ATOM   5353 H  HA   . ALA   B 1 89  ? 50.240 -14.299 -10.786 1.00 14.01 ?  89  ALA   B HA   1 
ATOM   5354 H  HB1  . ALA   B 1 89  ? 48.369 -14.498 -9.407  1.00 14.36 ?  89  ALA   B HB1  1 
ATOM   5355 H  HB2  . ALA   B 1 89  ? 49.278 -15.788 -9.216  1.00 14.36 ?  89  ALA   B HB2  1 
ATOM   5356 H  HB3  . ALA   B 1 89  ? 49.306 -14.629 -8.130  1.00 14.36 ?  89  ALA   B HB3  1 
ATOM   5357 N  N    . LYS   B 1 90  ? 49.321 -11.969 -10.108 1.00 12.96 ?  90  LYS   B N    1 
ATOM   5358 C  CA   . LYS   B 1 90  ? 49.124 -10.582 -9.702  1.00 13.05 ?  90  LYS   B CA   1 
ATOM   5359 C  C    . LYS   B 1 90  ? 48.815 -10.508 -8.212  1.00 12.98 ?  90  LYS   B C    1 
ATOM   5360 O  O    . LYS   B 1 90  ? 49.456 -9.750  -7.467  1.00 14.22 ?  90  LYS   B O    1 
ATOM   5361 C  CB   . LYS   B 1 90  ? 48.038 -9.920  -10.552 1.00 14.64 ?  90  LYS   B CB   1 
ATOM   5362 C  CG   . LYS   B 1 90  ? 47.748 -8.476  -10.165 1.00 15.33 ?  90  LYS   B CG   1 
ATOM   5363 C  CD   . LYS   B 1 90  ? 48.954 -7.580  -10.270 1.00 18.29 ?  90  LYS   B CD   1 
ATOM   5364 C  CE   . LYS   B 1 90  ? 48.511 -6.149  -10.060 1.00 20.39 ?  90  LYS   B CE   1 
ATOM   5365 N  NZ   . LYS   B 1 90  ? 49.658 -5.228  -9.913  1.00 20.22 ?  90  LYS   B NZ   1 
ATOM   5366 H  H    . LYS   B 1 90  ? 48.762 -12.274 -10.689 1.00 15.58 ?  90  LYS   B H    1 
ATOM   5367 H  HA   . LYS   B 1 90  ? 49.947 -10.102 -9.856  1.00 15.70 ?  90  LYS   B HA   1 
ATOM   5368 H  HB2  . LYS   B 1 90  ? 48.325 -9.924  -11.482 1.00 17.61 ?  90  LYS   B HB2  1 
ATOM   5369 H  HB3  . LYS   B 1 90  ? 47.215 -10.427 -10.465 1.00 17.61 ?  90  LYS   B HB3  1 
ATOM   5370 H  HG2  . LYS   B 1 90  ? 47.060 -8.127  -10.753 1.00 18.43 ?  90  LYS   B HG2  1 
ATOM   5371 H  HG3  . LYS   B 1 90  ? 47.430 -8.453  -9.245  1.00 18.43 ?  90  LYS   B HG3  1 
ATOM   5372 H  HD2  . LYS   B 1 90  ? 49.597 -7.814  -9.581  1.00 21.99 ?  90  LYS   B HD2  1 
ATOM   5373 H  HD3  . LYS   B 1 90  ? 49.347 -7.665  -11.152 1.00 21.99 ?  90  LYS   B HD3  1 
ATOM   5374 H  HE2  . LYS   B 1 90  ? 47.991 -5.858  -10.828 1.00 24.50 ?  90  LYS   B HE2  1 
ATOM   5375 H  HE3  . LYS   B 1 90  ? 47.976 -6.090  -9.254  1.00 24.50 ?  90  LYS   B HE3  1 
ATOM   5376 H  HZ1  . LYS   B 1 90  ? 49.370 -4.392  -9.794  1.00 24.29 ?  90  LYS   B HZ1  1 
ATOM   5377 H  HZ2  . LYS   B 1 90  ? 50.154 -5.462  -9.212  1.00 24.29 ?  90  LYS   B HZ2  1 
ATOM   5378 H  HZ3  . LYS   B 1 90  ? 50.167 -5.251  -10.645 1.00 24.29 ?  90  LYS   B HZ3  1 
ATOM   5379 N  N    . HIS   B 1 91  ? 47.856 -11.323 -7.760  1.00 11.41 ?  91  HIS   B N    1 
ATOM   5380 C  CA   . HIS   B 1 91  ? 47.394 -11.352 -6.386  1.00 11.44 ?  91  HIS   B CA   1 
ATOM   5381 C  C    . HIS   B 1 91  ? 47.397 -12.781 -5.871  1.00 10.85 ?  91  HIS   B C    1 
ATOM   5382 O  O    . HIS   B 1 91  ? 47.163 -13.732 -6.627  1.00 11.46 ?  91  HIS   B O    1 
ATOM   5383 C  CB   . HIS   B 1 91  ? 45.939 -10.878 -6.270  1.00 13.23 ?  91  HIS   B CB   1 
ATOM   5384 C  CG   . HIS   B 1 91  ? 45.719 -9.471  -6.709  1.00 16.31 ?  91  HIS   B CG   1 
ATOM   5385 N  ND1  . HIS   B 1 91  ? 46.308 -8.393  -6.084  1.00 19.20 ?  91  HIS   B ND1  1 
ATOM   5386 C  CD2  . HIS   B 1 91  ? 44.940 -8.959  -7.688  1.00 18.76 ?  91  HIS   B CD2  1 
ATOM   5387 C  CE1  . HIS   B 1 91  ? 45.923 -7.276  -6.676  1.00 19.98 ?  91  HIS   B CE1  1 
ATOM   5388 N  NE2  . HIS   B 1 91  ? 45.087 -7.593  -7.650  1.00 20.12 ?  91  HIS   B NE2  1 
ATOM   5389 H  H    . HIS   B 1 91  ? 47.441 -11.886 -8.258  1.00 13.73 ?  91  HIS   B H    1 
ATOM   5390 H  HA   . HIS   B 1 91  ? 47.961 -10.792 -5.821  1.00 13.76 ?  91  HIS   B HA   1 
ATOM   5391 H  HB2  . HIS   B 1 91  ? 45.380 -11.445 -6.820  1.00 15.91 ?  91  HIS   B HB2  1 
ATOM   5392 H  HB3  . HIS   B 1 91  ? 45.659 -10.942 -5.341  1.00 15.91 ?  91  HIS   B HB3  1 
ATOM   5393 H  HD1  . HIS   B 1 91  ? 46.850 -8.438  -5.416  1.00 23.08 ?  91  HIS   B HD1  1 
ATOM   5394 H  HD2  . HIS   B 1 91  ? 44.416 -9.431  -8.288  1.00 22.55 ?  91  HIS   B HD2  1 
ATOM   5395 H  HE1  . HIS   B 1 91  ? 46.190 -6.411  -6.439  1.00 24.01 ?  91  HIS   B HE1  1 
ATOM   5396 N  N    . CYS   B 1 92  ? 47.592 -12.919 -4.568  1.00 10.55 ?  92  CYS   B N    1 
ATOM   5397 C  CA   . CYS   B 1 92  ? 47.295 -14.156 -3.860  1.00 10.58 ?  92  CYS   B CA   1 
ATOM   5398 C  C    . CYS   B 1 92  ? 46.076 -13.925 -2.974  1.00 10.20 ?  92  CYS   B C    1 
ATOM   5399 O  O    . CYS   B 1 92  ? 46.077 -13.022 -2.125  1.00 11.13 ?  92  CYS   B O    1 
ATOM   5400 C  CB   . CYS   B 1 92  ? 48.476 -14.619 -3.014  1.00 11.06 ?  92  CYS   B CB   1 
ATOM   5401 S  SG   . CYS   B 1 92  ? 48.122 -16.152 -2.114  1.00 11.12 ?  92  CYS   B SG   1 
ATOM   5402 H  H    . CYS   B 1 92  ? 47.912 -12.297 -4.058  1.00 12.69 ?  92  CYS   B H    1 
ATOM   5403 H  HA   . CYS   B 1 92  ? 47.091 -14.849 -4.507  1.00 12.73 ?  92  CYS   B HA   1 
ATOM   5404 H  HB2  . CYS   B 1 92  ? 49.237 -14.772 -3.590  1.00 13.31 ?  92  CYS   B HB2  1 
ATOM   5405 H  HB3  . CYS   B 1 92  ? 48.680 -13.930 -2.362  1.00 13.31 ?  92  CYS   B HB3  1 
ATOM   5406 H  HG   . CYS   B 1 92  ? 49.098 -16.464 -1.494  1.00 13.38 ?  92  CYS   B HG   1 
ATOM   5407 N  N    . LEU   B 1 93  ? 45.037 -14.734 -3.186  1.00 10.07 ?  93  LEU   B N    1 
ATOM   5408 C  CA   . LEU   B 1 93  ? 43.862 -14.746 -2.324  1.00 10.32 ?  93  LEU   B CA   1 
ATOM   5409 C  C    . LEU   B 1 93  ? 44.092 -15.812 -1.261  1.00 10.01 ?  93  LEU   B C    1 
ATOM   5410 O  O    . LEU   B 1 93  ? 44.051 -17.013 -1.556  1.00 10.39 ?  93  LEU   B O    1 
ATOM   5411 C  CB   . LEU   B 1 93  ? 42.599 -15.039 -3.130  1.00 10.58 ?  93  LEU   B CB   1 
ATOM   5412 C  CG   . LEU   B 1 93  ? 41.301 -15.055 -2.318  1.00 11.36 ?  93  LEU   B CG   1 
ATOM   5413 C  CD1  . LEU   B 1 93  ? 40.941 -13.671 -1.821  1.00 11.81 ?  93  LEU   B CD1  1 
ATOM   5414 C  CD2  . LEU   B 1 93  ? 40.176 -15.645 -3.152  1.00 11.70 ?  93  LEU   B CD2  1 
ATOM   5415 H  H    . LEU   B 1 93  ? 44.993 -15.301 -3.843  1.00 12.11 ?  93  LEU   B H    1 
ATOM   5416 H  HA   . LEU   B 1 93  ? 43.770 -13.886 -1.894  1.00 12.41 ?  93  LEU   B HA   1 
ATOM   5417 H  HB2  . LEU   B 1 93  ? 42.506 -14.359 -3.813  1.00 12.73 ?  93  LEU   B HB2  1 
ATOM   5418 H  HB3  . LEU   B 1 93  ? 42.691 -15.909 -3.545  1.00 12.73 ?  93  LEU   B HB3  1 
ATOM   5419 H  HG   . LEU   B 1 93  ? 41.420 -15.624 -1.543  1.00 13.66 ?  93  LEU   B HG   1 
ATOM   5420 H  HD11 . LEU   B 1 93  ? 40.090 -13.713 -1.358  1.00 14.20 ?  93  LEU   B HD11 1 
ATOM   5421 H  HD12 . LEU   B 1 93  ? 41.633 -13.363 -1.214  1.00 14.20 ?  93  LEU   B HD12 1 
ATOM   5422 H  HD13 . LEU   B 1 93  ? 40.875 -13.069 -2.580  1.00 14.20 ?  93  LEU   B HD13 1 
ATOM   5423 H  HD21 . LEU   B 1 93  ? 39.357 -15.644 -2.630  1.00 14.07 ?  93  LEU   B HD21 1 
ATOM   5424 H  HD22 . LEU   B 1 93  ? 40.057 -15.111 -3.953  1.00 14.07 ?  93  LEU   B HD22 1 
ATOM   5425 H  HD23 . LEU   B 1 93  ? 40.406 -16.558 -3.397  1.00 14.07 ?  93  LEU   B HD23 1 
ATOM   5426 N  N    . HIS   B 1 94  ? 44.365 -15.377 -0.037  1.00 9.85  ?  94  HIS   B N    1 
ATOM   5427 C  CA   . HIS   B 1 94  ? 44.584 -16.286 1.083   1.00 10.08 ?  94  HIS   B CA   1 
ATOM   5428 C  C    . HIS   B 1 94  ? 43.223 -16.644 1.664   1.00 10.35 ?  94  HIS   B C    1 
ATOM   5429 O  O    . HIS   B 1 94  ? 42.550 -15.776 2.226   1.00 11.93 ?  94  HIS   B O    1 
ATOM   5430 C  CB   . HIS   B 1 94  ? 45.462 -15.610 2.137   1.00 10.46 ?  94  HIS   B CB   1 
ATOM   5431 C  CG   . HIS   B 1 94  ? 46.847 -15.305 1.667   1.00 10.51 ?  94  HIS   B CG   1 
ATOM   5432 N  ND1  . HIS   B 1 94  ? 47.875 -16.223 1.742   1.00 10.75 ?  94  HIS   B ND1  1 
ATOM   5433 C  CD2  . HIS   B 1 94  ? 47.353 -14.197 1.072   1.00 10.53 ?  94  HIS   B CD2  1 
ATOM   5434 C  CE1  . HIS   B 1 94  ? 48.964 -15.670 1.236   1.00 10.71 ?  94  HIS   B CE1  1 
ATOM   5435 N  NE2  . HIS   B 1 94  ? 48.675 -14.445 0.821   1.00 10.74 ?  94  HIS   B NE2  1 
ATOM   5436 H  H    . HIS   B 1 94  ? 44.424 -14.541 0.173   1.00 11.85 ?  94  HIS   B H    1 
ATOM   5437 H  HA   . HIS   B 1 94  ? 45.022 -17.091 0.772   1.00 12.13 ?  94  HIS   B HA   1 
ATOM   5438 H  HB2  . HIS   B 1 94  ? 45.050 -14.774 2.400   1.00 12.58 ?  94  HIS   B HB2  1 
ATOM   5439 H  HB3  . HIS   B 1 94  ? 45.534 -16.199 2.904   1.00 12.58 ?  94  HIS   B HB3  1 
ATOM   5440 H  HD2  . HIS   B 1 94  ? 46.900 -13.411 0.886   1.00 12.67 ?  94  HIS   B HD2  1 
ATOM   5441 H  HE1  . HIS   B 1 94  ? 49.798 -16.088 1.176   1.00 12.88 ?  94  HIS   B HE1  1 
ATOM   5442 H  HE2  . HIS   B 1 94  ? 49.236 -13.904 0.459   1.00 12.92 ?  94  HIS   B HE2  1 
ATOM   5443 N  N    . VAL   B 1 95  ? 42.797 -17.900 1.506   1.00 10.50 ?  95  VAL   B N    1 
ATOM   5444 C  CA   . VAL   B 1 95  ? 41.470 -18.343 1.939   1.00 10.60 ?  95  VAL   B CA   1 
ATOM   5445 C  C    . VAL   B 1 95  ? 41.641 -19.385 3.032   1.00 10.56 ?  95  VAL   B C    1 
ATOM   5446 O  O    . VAL   B 1 95  ? 42.410 -20.338 2.866   1.00 11.16 ?  95  VAL   B O    1 
ATOM   5447 C  CB   . VAL   B 1 95  ? 40.652 -18.944 0.780   1.00 10.72 ?  95  VAL   B CB   1 
ATOM   5448 C  CG1  . VAL   B 1 95  ? 39.274 -19.397 1.261   1.00 11.87 ?  95  VAL   B CG1  1 
ATOM   5449 C  CG2  . VAL   B 1 95  ? 40.527 -17.954 -0.356  1.00 11.30 ?  95  VAL   B CG2  1 
ATOM   5450 H  H    . VAL   B 1 95  ? 43.261 -18.523 1.138   1.00 12.64 ?  95  VAL   B H    1 
ATOM   5451 H  HA   . VAL   B 1 95  ? 40.975 -17.594 2.306   1.00 12.75 ?  95  VAL   B HA   1 
ATOM   5452 H  HB   . VAL   B 1 95  ? 41.112 -19.724 0.440   1.00 12.89 ?  95  VAL   B HB   1 
ATOM   5453 H  HG11 . VAL   B 1 95  ? 38.715 -19.595 0.488   1.00 14.28 ?  95  VAL   B HG11 1 
ATOM   5454 H  HG12 . VAL   B 1 95  ? 39.368 -20.197 1.804   1.00 14.28 ?  95  VAL   B HG12 1 
ATOM   5455 H  HG13 . VAL   B 1 95  ? 38.865 -18.689 1.783   1.00 14.28 ?  95  VAL   B HG13 1 
ATOM   5456 H  HG21 . VAL   B 1 95  ? 39.948 -18.329 -1.037  1.00 13.59 ?  95  VAL   B HG21 1 
ATOM   5457 H  HG22 . VAL   B 1 95  ? 40.144 -17.131 -0.012  1.00 13.59 ?  95  VAL   B HG22 1 
ATOM   5458 H  HG23 . VAL   B 1 95  ? 41.407 -17.787 -0.720  1.00 13.59 ?  95  VAL   B HG23 1 
ATOM   5459 N  N    . VAL   B 1 96  ? 40.915 -19.216 4.132   1.00 11.07 ?  96  VAL   B N    1 
ATOM   5460 C  CA   . VAL   B 1 96  ? 40.996 -20.138 5.265   1.00 11.57 ?  96  VAL   B CA   1 
ATOM   5461 C  C    . VAL   B 1 96  ? 39.807 -21.100 5.219   1.00 11.78 ?  96  VAL   B C    1 
ATOM   5462 O  O    . VAL   B 1 96  ? 38.685 -20.741 5.595   1.00 12.81 ?  96  VAL   B O    1 
ATOM   5463 C  CB   . VAL   B 1 96  ? 41.052 -19.397 6.603   1.00 12.49 ?  96  VAL   B CB   1 
ATOM   5464 C  CG1  . VAL   B 1 96  ? 41.228 -20.385 7.738   1.00 13.17 ?  96  VAL   B CG1  1 
ATOM   5465 C  CG2  . VAL   B 1 96  ? 42.171 -18.363 6.611   1.00 13.21 ?  96  VAL   B CG2  1 
ATOM   5466 H  H    . VAL   B 1 96  ? 40.355 -18.575 4.249   1.00 13.32 ?  96  VAL   B H    1 
ATOM   5467 H  HA   . VAL   B 1 96  ? 41.812 -20.665 5.185   1.00 13.92 ?  96  VAL   B HA   1 
ATOM   5468 H  HB   . VAL   B 1 96  ? 40.212 -18.934 6.740   1.00 15.02 ?  96  VAL   B HB   1 
ATOM   5469 H  HG11 . VAL   B 1 96  ? 41.421 -19.897 8.556   1.00 15.83 ?  96  VAL   B HG11 1 
ATOM   5470 H  HG12 . VAL   B 1 96  ? 40.413 -20.899 7.848   1.00 15.83 ?  96  VAL   B HG12 1 
ATOM   5471 H  HG13 . VAL   B 1 96  ? 41.969 -20.980 7.531   1.00 15.83 ?  96  VAL   B HG13 1 
ATOM   5472 H  HG21 . VAL   B 1 96  ? 42.221 -17.956 7.493   1.00 15.89 ?  96  VAL   B HG21 1 
ATOM   5473 H  HG22 . VAL   B 1 96  ? 43.010 -18.797 6.400   1.00 15.89 ?  96  VAL   B HG22 1 
ATOM   5474 H  HG23 . VAL   B 1 96  ? 41.976 -17.679 5.948   1.00 15.89 ?  96  VAL   B HG23 1 
ATOM   5475 N  N    . GLY   B 1 97  ? 40.045 -22.335 4.783   1.00 11.95 ?  97  GLY   B N    1 
ATOM   5476 C  CA   . GLY   B 1 97  ? 39.070 -23.390 4.943   1.00 12.54 ?  97  GLY   B CA   1 
ATOM   5477 C  C    . GLY   B 1 97  ? 39.189 -24.001 6.321   1.00 13.13 ?  97  GLY   B C    1 
ATOM   5478 O  O    . GLY   B 1 97  ? 40.229 -23.880 6.978   1.00 13.80 ?  97  GLY   B O    1 
ATOM   5479 H  H    . GLY   B 1 97  ? 40.774 -22.580 4.384   1.00 14.37 ?  97  GLY   B H    1 
ATOM   5480 H  HA2  . GLY   B 1 97  ? 38.179 -23.019 4.826   1.00 15.08 ?  97  GLY   B HA2  1 
ATOM   5481 H  HA3  . GLY   B 1 97  ? 39.215 -24.075 4.272   1.00 15.08 ?  97  GLY   B HA3  1 
ATOM   5482 N  N    . PRO   B 1 98  ? 38.139 -24.684 6.781   1.00 14.00 ?  98  PRO   B N    1 
ATOM   5483 C  CA   . PRO   B 1 98  ? 38.224 -25.380 8.069   1.00 14.89 ?  98  PRO   B CA   1 
ATOM   5484 C  C    . PRO   B 1 98  ? 39.253 -26.500 8.026   1.00 14.73 ?  98  PRO   B C    1 
ATOM   5485 O  O    . PRO   B 1 98  ? 39.359 -27.236 7.045   1.00 14.73 ?  98  PRO   B O    1 
ATOM   5486 C  CB   . PRO   B 1 98  ? 36.804 -25.924 8.266   1.00 14.81 ?  98  PRO   B CB   1 
ATOM   5487 C  CG   . PRO   B 1 98  ? 36.253 -26.055 6.889   1.00 14.77 ?  98  PRO   B CG   1 
ATOM   5488 C  CD   . PRO   B 1 98  ? 36.825 -24.877 6.141   1.00 14.27 ?  98  PRO   B CD   1 
ATOM   5489 H  HA   . PRO   B 1 98  ? 38.443 -24.760 8.778   1.00 17.90 ?  98  PRO   B HA   1 
ATOM   5490 H  HB2  . PRO   B 1 98  ? 36.842 -26.790 8.702   1.00 17.81 ?  98  PRO   B HB2  1 
ATOM   5491 H  HB3  . PRO   B 1 98  ? 36.281 -25.297 8.785   1.00 17.81 ?  98  PRO   B HB3  1 
ATOM   5492 H  HG2  . PRO   B 1 98  ? 36.548 -26.892 6.493   1.00 17.76 ?  98  PRO   B HG2  1 
ATOM   5493 H  HG3  . PRO   B 1 98  ? 35.286 -26.009 6.914   1.00 17.76 ?  98  PRO   B HG3  1 
ATOM   5494 H  HD2  . PRO   B 1 98  ? 36.933 -25.092 5.195   1.00 17.15 ?  98  PRO   B HD2  1 
ATOM   5495 H  HD3  . PRO   B 1 98  ? 36.275 -24.090 6.262   1.00 17.15 ?  98  PRO   B HD3  1 
ATOM   5496 N  N    . ASN   B 1 99  ? 39.999 -26.634 9.113   1.00 15.63 ?  99  ASN   B N    1 
ATOM   5497 C  CA   . ASN   B 1 99  ? 40.977 -27.707 9.270   1.00 16.57 ?  99  ASN   B CA   1 
ATOM   5498 C  C    . ASN   B 1 99  ? 40.349 -28.797 10.138  1.00 18.77 ?  99  ASN   B C    1 
ATOM   5499 O  O    . ASN   B 1 99  ? 40.261 -28.657 11.360  1.00 19.46 ?  99  ASN   B O    1 
ATOM   5500 C  CB   . ASN   B 1 99  ? 42.250 -27.152 9.894   1.00 16.80 ?  99  ASN   B CB   1 
ATOM   5501 C  CG   . ASN   B 1 99  ? 43.381 -28.158 9.903   1.00 17.84 ?  99  ASN   B CG   1 
ATOM   5502 O  OD1  . ASN   B 1 99  ? 43.159 -29.351 10.066  1.00 18.84 ?  99  ASN   B OD1  1 
ATOM   5503 N  ND2  . ASN   B 1 99  ? 44.601 -27.678 9.727   1.00 18.01 ?  99  ASN   B ND2  1 
ATOM   5504 H  H    . ASN   B 1 99  ? 39.951 -26.107 9.788   1.00 18.79 ?  99  ASN   B H    1 
ATOM   5505 H  HA   . ASN   B 1 99  ? 41.191 -28.089 8.405   1.00 19.91 ?  99  ASN   B HA   1 
ATOM   5506 H  HB2  . ASN   B 1 99  ? 42.534 -26.379 9.393   1.00 20.19 ?  99  ASN   B HB2  1 
ATOM   5507 H  HB3  . ASN   B 1 99  ? 42.059 -26.901 10.816  1.00 20.19 ?  99  ASN   B HB3  1 
ATOM   5508 H  HD21 . ASN   B 1 99  ? 45.274 -28.210 9.726   1.00 21.65 ?  99  ASN   B HD21 1 
ATOM   5509 H  HD22 . ASN   B 1 99  ? 44.714 -26.834 9.617   1.00 21.65 ?  99  ASN   B HD22 1 
ATOM   5510 N  N    A VAL   B 1 100 ? 39.895 -29.877 9.498   0.50 20.74 ?  100 VAL   B N    1 
ATOM   5511 N  N    B VAL   B 1 100 ? 39.905 -29.878 9.492   0.50 20.69 ?  100 VAL   B N    1 
ATOM   5512 C  CA   A VAL   B 1 100 ? 39.283 -30.975 10.244  0.50 23.30 ?  100 VAL   B CA   1 
ATOM   5513 C  CA   B VAL   B 1 100 ? 39.289 -30.991 10.211  0.50 23.18 ?  100 VAL   B CA   1 
ATOM   5514 C  C    A VAL   B 1 100 ? 40.291 -31.631 11.179  0.50 23.83 ?  100 VAL   B C    1 
ATOM   5515 C  C    B VAL   B 1 100 ? 40.284 -31.655 11.153  0.50 23.70 ?  100 VAL   B C    1 
ATOM   5516 O  O    A VAL   B 1 100 ? 39.921 -32.134 12.247  0.50 24.32 ?  100 VAL   B O    1 
ATOM   5517 O  O    B VAL   B 1 100 ? 39.898 -32.188 12.201  0.50 24.05 ?  100 VAL   B O    1 
ATOM   5518 C  CB   A VAL   B 1 100 ? 38.632 -31.990 9.283   0.50 25.57 ?  100 VAL   B CB   1 
ATOM   5519 C  CB   B VAL   B 1 100 ? 38.680 -31.993 9.208   0.50 25.37 ?  100 VAL   B CB   1 
ATOM   5520 C  CG1  A VAL   B 1 100 ? 38.148 -33.216 10.045  0.50 26.49 ?  100 VAL   B CG1  1 
ATOM   5521 C  CG1  B VAL   B 1 100 ? 38.217 -33.259 9.916   0.50 26.26 ?  100 VAL   B CG1  1 
ATOM   5522 C  CG2  A VAL   B 1 100 ? 37.477 -31.342 8.535   0.50 26.11 ?  100 VAL   B CG2  1 
ATOM   5523 C  CG2  B VAL   B 1 100 ? 37.525 -31.346 8.459   0.50 25.89 ?  100 VAL   B CG2  1 
ATOM   5524 H  H    A VAL   B 1 100 ? 39.918 -29.993 8.646   0.50 24.93 ?  100 VAL   B H    1 
ATOM   5525 H  H    B VAL   B 1 100 ? 39.941 -29.985 8.640   0.50 24.86 ?  100 VAL   B H    1 
ATOM   5526 H  HA   A VAL   B 1 100 ? 38.573 -30.610 10.794  0.50 27.99 ?  100 VAL   B HA   1 
ATOM   5527 H  HA   B VAL   B 1 100 ? 38.561 -30.647 10.750  0.50 27.85 ?  100 VAL   B HA   1 
ATOM   5528 H  HB   A VAL   B 1 100 ? 39.289 -32.282 8.634   0.50 30.72 ?  100 VAL   B HB   1 
ATOM   5529 H  HB   B VAL   B 1 100 ? 39.356 -32.246 8.561   0.50 30.48 ?  100 VAL   B HB   1 
ATOM   5530 H  HG11 A VAL   B 1 100 ? 37.556 -33.729 9.471   0.50 31.82 ?  100 VAL   B HG11 1 
ATOM   5531 H  HG11 B VAL   B 1 100 ? 37.645 -33.764 9.315   0.50 31.54 ?  100 VAL   B HG11 1 
ATOM   5532 H  HG12 A VAL   B 1 100 ? 38.911 -33.760 10.296  0.50 31.82 ?  100 VAL   B HG12 1 
ATOM   5533 H  HG12 B VAL   B 1 100 ? 38.990 -33.793 10.157  0.50 31.54 ?  100 VAL   B HG12 1 
ATOM   5534 H  HG13 A VAL   B 1 100 ? 37.668 -32.929 10.838  0.50 31.82 ?  100 VAL   B HG13 1 
ATOM   5535 H  HG13 B VAL   B 1 100 ? 37.720 -33.014 10.712  0.50 31.54 ?  100 VAL   B HG13 1 
ATOM   5536 H  HG21 A VAL   B 1 100 ? 37.083 -31.996 7.936   0.50 31.36 ?  100 VAL   B HG21 1 
ATOM   5537 H  HG21 B VAL   B 1 100 ? 37.150 -31.991 7.840   0.50 31.11 ?  100 VAL   B HG21 1 
ATOM   5538 H  HG22 A VAL   B 1 100 ? 36.814 -31.041 9.177   0.50 31.36 ?  100 VAL   B HG22 1 
ATOM   5539 H  HG22 B VAL   B 1 100 ? 36.849 -31.071 9.099   0.50 31.11 ?  100 VAL   B HG22 1 
ATOM   5540 H  HG23 A VAL   B 1 100 ? 37.814 -30.589 8.028   0.50 31.36 ?  100 VAL   B HG23 1 
ATOM   5541 H  HG23 B VAL   B 1 100 ? 37.857 -30.575 7.975   0.50 31.11 ?  100 VAL   B HG23 1 
ATOM   5542 N  N    . ASN   B 1 101 ? 41.571 -31.655 10.795  1.00 24.16 ?  101 ASN   B N    1 
ATOM   5543 C  CA   . ASN   B 1 101 ? 42.602 -32.185 11.688  1.00 26.62 ?  101 ASN   B CA   1 
ATOM   5544 C  C    . ASN   B 1 101 ? 42.763 -31.345 12.951  1.00 29.17 ?  101 ASN   B C    1 
ATOM   5545 O  O    . ASN   B 1 101 ? 43.368 -31.819 13.922  1.00 30.07 ?  101 ASN   B O    1 
ATOM   5546 C  CB   . ASN   B 1 101 ? 43.935 -32.322 10.946  1.00 26.44 ?  101 ASN   B CB   1 
ATOM   5547 C  CG   . ASN   B 1 101 ? 43.919 -33.451 9.928   1.00 25.97 ?  101 ASN   B CG   1 
ATOM   5548 O  OD1  . ASN   B 1 101 ? 43.244 -34.459 10.119  1.00 27.04 ?  101 ASN   B OD1  1 
ATOM   5549 N  ND2  . ASN   B 1 101 ? 44.656 -33.279 8.837   1.00 25.72 ?  101 ASN   B ND2  1 
ATOM   5550 H  H    A ASN   B 1 101 ? 41.856 -31.394 10.027  0.50 29.03 ?  101 ASN   B H    1 
ATOM   5551 H  H    B ASN   B 1 101 ? 41.865 -31.370 10.038  0.50 29.03 ?  101 ASN   B H    1 
ATOM   5552 H  HA   . ASN   B 1 101 ? 42.338 -33.066 11.969  1.00 31.97 ?  101 ASN   B HA   1 
ATOM   5553 H  HB2  . ASN   B 1 101 ? 44.131 -31.496 10.473  1.00 31.76 ?  101 ASN   B HB2  1 
ATOM   5554 H  HB3  . ASN   B 1 101 ? 44.637 -32.508 11.588  1.00 31.76 ?  101 ASN   B HB3  1 
ATOM   5555 H  HD21 . ASN   B 1 101 ? 44.676 -33.891 8.232   1.00 30.90 ?  101 ASN   B HD21 1 
ATOM   5556 H  HD22 . ASN   B 1 101 ? 45.114 -32.559 8.734   1.00 30.90 ?  101 ASN   B HD22 1 
ATOM   5557 N  N    A LYS   B 1 102 ? 42.243 -30.116 12.959  0.50 30.63 ?  102 LYS   B N    1 
ATOM   5558 N  N    B LYS   B 1 102 ? 42.240 -30.118 12.960  0.50 30.63 ?  102 LYS   B N    1 
ATOM   5559 C  CA   A LYS   B 1 102 ? 42.223 -29.266 14.142  0.50 32.39 ?  102 LYS   B CA   1 
ATOM   5560 C  CA   B LYS   B 1 102 ? 42.223 -29.270 14.145  0.50 32.39 ?  102 LYS   B CA   1 
ATOM   5561 C  C    A LYS   B 1 102 ? 40.853 -29.231 14.807  0.50 31.82 ?  102 LYS   B C    1 
ATOM   5562 C  C    B LYS   B 1 102 ? 40.854 -29.236 14.812  0.50 31.83 ?  102 LYS   B C    1 
ATOM   5563 O  O    A LYS   B 1 102 ? 40.646 -28.443 15.735  0.50 32.20 ?  102 LYS   B O    1 
ATOM   5564 O  O    B LYS   B 1 102 ? 40.650 -28.455 15.747  0.50 32.23 ?  102 LYS   B O    1 
ATOM   5565 C  CB   A LYS   B 1 102 ? 42.641 -27.837 13.782  0.50 34.83 ?  102 LYS   B CB   1 
ATOM   5566 C  CB   B LYS   B 1 102 ? 42.641 -27.842 13.786  0.50 34.82 ?  102 LYS   B CB   1 
ATOM   5567 C  CG   A LYS   B 1 102 ? 44.108 -27.657 13.430  0.50 37.13 ?  102 LYS   B CG   1 
ATOM   5568 C  CG   B LYS   B 1 102 ? 44.102 -27.669 13.411  0.50 37.11 ?  102 LYS   B CG   1 
ATOM   5569 C  CD   A LYS   B 1 102 ? 44.382 -26.203 13.070  0.50 39.20 ?  102 LYS   B CD   1 
ATOM   5570 C  CD   B LYS   B 1 102 ? 44.353 -26.247 12.933  0.50 39.16 ?  102 LYS   B CD   1 
ATOM   5571 C  CE   A LYS   B 1 102 ? 45.851 -25.950 12.781  0.50 40.77 ?  102 LYS   B CE   1 
ATOM   5572 C  CE   B LYS   B 1 102 ? 45.831 -25.958 12.746  0.50 40.72 ?  102 LYS   B CE   1 
ATOM   5573 N  NZ   A LYS   B 1 102 ? 46.094 -24.528 12.402  0.50 41.67 ?  102 LYS   B NZ   1 
ATOM   5574 N  NZ   B LYS   B 1 102 ? 46.053 -24.565 12.263  0.50 41.61 ?  102 LYS   B NZ   1 
ATOM   5575 H  H    A LYS   B 1 102 ? 41.878 -29.746 12.273  0.50 36.79 ?  102 LYS   B H    1 
ATOM   5576 H  H    B LYS   B 1 102 ? 41.869 -29.748 12.276  0.50 36.79 ?  102 LYS   B H    1 
ATOM   5577 H  HA   A LYS   B 1 102 ? 42.864 -29.606 14.785  0.50 38.91 ?  102 LYS   B HA   1 
ATOM   5578 H  HA   B LYS   B 1 102 ? 42.866 -29.612 14.785  0.50 38.90 ?  102 LYS   B HA   1 
ATOM   5579 H  HB2  A LYS   B 1 102 ? 42.121 -27.546 13.018  0.50 41.83 ?  102 LYS   B HB2  1 
ATOM   5580 H  HB2  B LYS   B 1 102 ? 42.110 -27.543 13.033  0.50 41.82 ?  102 LYS   B HB2  1 
ATOM   5581 H  HB3  A LYS   B 1 102 ? 42.454 -27.260 14.541  0.50 41.83 ?  102 LYS   B HB3  1 
ATOM   5582 H  HB3  B LYS   B 1 102 ? 42.469 -27.268 14.551  0.50 41.82 ?  102 LYS   B HB3  1 
ATOM   5583 H  HG2  A LYS   B 1 102 ? 44.660 -27.893 14.193  0.50 44.59 ?  102 LYS   B HG2  1 
ATOM   5584 H  HG2  B LYS   B 1 102 ? 44.661 -27.836 14.187  0.50 44.57 ?  102 LYS   B HG2  1 
ATOM   5585 H  HG3  A LYS   B 1 102 ? 44.331 -28.210 12.665  0.50 44.59 ?  102 LYS   B HG3  1 
ATOM   5586 H  HG3  B LYS   B 1 102 ? 44.329 -28.280 12.692  0.50 44.57 ?  102 LYS   B HG3  1 
ATOM   5587 H  HD2  A LYS   B 1 102 ? 43.874 -25.971 12.277  0.50 47.07 ?  102 LYS   B HD2  1 
ATOM   5588 H  HD2  B LYS   B 1 102 ? 43.909 -26.116 12.080  0.50 47.03 ?  102 LYS   B HD2  1 
ATOM   5589 H  HD3  A LYS   B 1 102 ? 44.118 -25.637 13.812  0.50 47.07 ?  102 LYS   B HD3  1 
ATOM   5590 H  HD3  B LYS   B 1 102 ? 44.004 -25.625 13.590  0.50 47.03 ?  102 LYS   B HD3  1 
ATOM   5591 H  HE2  A LYS   B 1 102 ? 46.372 -26.147 13.575  0.50 48.96 ?  102 LYS   B HE2  1 
ATOM   5592 H  HE2  B LYS   B 1 102 ? 46.288 -26.062 13.595  0.50 48.90 ?  102 LYS   B HE2  1 
ATOM   5593 H  HE3  A LYS   B 1 102 ? 46.134 -26.514 12.044  0.50 48.96 ?  102 LYS   B HE3  1 
ATOM   5594 H  HE3  B LYS   B 1 102 ? 46.197 -26.570 12.089  0.50 48.90 ?  102 LYS   B HE3  1 
ATOM   5595 H  HZ1  A LYS   B 1 102 ? 46.959 -24.400 12.237  0.50 50.04 ?  102 LYS   B HZ1  1 
ATOM   5596 H  HZ1  B LYS   B 1 102 ? 46.923 -24.414 12.159  0.50 49.96 ?  102 LYS   B HZ1  1 
ATOM   5597 H  HZ2  A LYS   B 1 102 ? 45.627 -24.323 11.672  0.50 50.04 ?  102 LYS   B HZ2  1 
ATOM   5598 H  HZ2  B LYS   B 1 102 ? 45.643 -24.446 11.482  0.50 49.96 ?  102 LYS   B HZ2  1 
ATOM   5599 H  HZ3  A LYS   B 1 102 ? 45.844 -23.989 13.065  0.50 50.04 ?  102 LYS   B HZ3  1 
ATOM   5600 H  HZ3  B LYS   B 1 102 ? 45.726 -23.984 12.852  0.50 49.96 ?  102 LYS   B HZ3  1 
ATOM   5601 N  N    . GLY   B 1 103 ? 39.910 -30.049 14.344  1.00 31.01 ?  103 GLY   B N    1 
ATOM   5602 C  CA   . GLY   B 1 103 ? 38.581 -30.091 14.923  1.00 30.23 ?  103 GLY   B CA   1 
ATOM   5603 C  C    . GLY   B 1 103 ? 37.633 -29.010 14.454  1.00 28.78 ?  103 GLY   B C    1 
ATOM   5604 O  O    . GLY   B 1 103 ? 36.541 -28.880 15.019  1.00 29.71 ?  103 GLY   B O    1 
ATOM   5605 H  H    A GLY   B 1 103 ? 40.022 -30.592 13.689  0.50 37.24 ?  103 GLY   B H    1 
ATOM   5606 H  H    B GLY   B 1 103 ? 40.021 -30.587 13.685  0.50 37.24 ?  103 GLY   B H    1 
ATOM   5607 H  HA2  . GLY   B 1 103 ? 38.181 -30.950 14.715  1.00 36.31 ?  103 GLY   B HA2  1 
ATOM   5608 H  HA3  . GLY   B 1 103 ? 38.659 -30.024 15.888  1.00 36.31 ?  103 GLY   B HA3  1 
ATOM   5609 N  N    A GLU   B 1 104 ? 38.023 -28.219 13.457  0.50 27.88 ?  104 GLU   B N    1 
ATOM   5610 N  N    B GLU   B 1 104 ? 37.993 -28.247 13.426  0.50 27.46 ?  104 GLU   B N    1 
ATOM   5611 C  CA   A GLU   B 1 104 ? 37.192 -27.114 13.004  0.50 26.88 ?  104 GLU   B CA   1 
ATOM   5612 C  CA   B GLU   B 1 104 ? 37.134 -27.173 12.949  0.50 26.06 ?  104 GLU   B CA   1 
ATOM   5613 C  C    A GLU   B 1 104 ? 36.010 -27.628 12.186  0.50 27.64 ?  104 GLU   B C    1 
ATOM   5614 C  C    B GLU   B 1 104 ? 35.982 -27.724 12.111  0.50 26.43 ?  104 GLU   B C    1 
ATOM   5615 O  O    A GLU   B 1 104 ? 36.056 -28.708 11.589  0.50 28.36 ?  104 GLU   B O    1 
ATOM   5616 O  O    B GLU   B 1 104 ? 36.077 -28.797 11.507  0.50 27.09 ?  104 GLU   B O    1 
ATOM   5617 C  CB   A GLU   B 1 104 ? 38.036 -26.126 12.197  0.50 25.67 ?  104 GLU   B CB   1 
ATOM   5618 C  CB   B GLU   B 1 104 ? 37.960 -26.158 12.160  0.50 24.82 ?  104 GLU   B CB   1 
ATOM   5619 C  CG   A GLU   B 1 104 ? 39.165 -25.513 13.020  0.50 24.51 ?  104 GLU   B CG   1 
ATOM   5620 C  CG   B GLU   B 1 104 ? 39.047 -25.531 13.018  0.50 23.65 ?  104 GLU   B CG   1 
ATOM   5621 C  CD   A GLU   B 1 104 ? 40.083 -24.614 12.223  0.50 23.45 ?  104 GLU   B CD   1 
ATOM   5622 C  CD   B GLU   B 1 104 ? 40.023 -24.672 12.250  0.50 22.54 ?  104 GLU   B CD   1 
ATOM   5623 O  OE1  A GLU   B 1 104 ? 40.076 -24.679 10.976  0.50 21.91 ?  104 GLU   B OE1  1 
ATOM   5624 O  OE1  B GLU   B 1 104 ? 39.992 -24.668 11.001  0.50 21.39 ?  104 GLU   B OE1  1 
ATOM   5625 O  OE2  A GLU   B 1 104 ? 40.820 -23.834 12.861  0.50 23.92 -1 104 GLU   B OE2  1 
ATOM   5626 O  OE2  B GLU   B 1 104 ? 40.832 -23.998 12.917  0.50 22.52 -1 104 GLU   B OE2  1 
ATOM   5627 H  H    A GLU   B 1 104 ? 38.769 -28.297 13.038  0.50 33.49 ?  104 GLU   B H    1 
ATOM   5628 H  H    B GLU   B 1 104 ? 38.734 -28.325 12.999  0.50 32.99 ?  104 GLU   B H    1 
ATOM   5629 H  HA   A GLU   B 1 104 ? 36.844 -26.642 13.778  0.50 32.29 ?  104 GLU   B HA   1 
ATOM   5630 H  HA   B GLU   B 1 104 ? 36.754 -26.715 13.714  0.50 31.30 ?  104 GLU   B HA   1 
ATOM   5631 H  HB2  A GLU   B 1 104 ? 38.434 -26.588 11.443  0.50 30.84 ?  104 GLU   B HB2  1 
ATOM   5632 H  HB2  B GLU   B 1 104 ? 38.384 -26.602 11.411  0.50 29.82 ?  104 GLU   B HB2  1 
ATOM   5633 H  HB3  A GLU   B 1 104 ? 37.469 -25.404 11.885  0.50 30.84 ?  104 GLU   B HB3  1 
ATOM   5634 H  HB3  B GLU   B 1 104 ? 37.377 -25.449 11.845  0.50 29.82 ?  104 GLU   B HB3  1 
ATOM   5635 H  HG2  A GLU   B 1 104 ? 38.785 -24.972 13.730  0.50 29.44 ?  104 GLU   B HG2  1 
ATOM   5636 H  HG2  B GLU   B 1 104 ? 38.631 -24.966 13.688  0.50 28.42 ?  104 GLU   B HG2  1 
ATOM   5637 H  HG3  A GLU   B 1 104 ? 39.706 -26.222 13.400  0.50 29.44 ?  104 GLU   B HG3  1 
ATOM   5638 H  HG3  B GLU   B 1 104 ? 39.555 -26.234 13.449  0.50 28.42 ?  104 GLU   B HG3  1 
ATOM   5639 N  N    A ASP   B 1 105 ? 34.940 -26.837 12.169  0.50 27.89 ?  105 ASP   B N    1 
ATOM   5640 N  N    B ASP   B 1 105 ? 34.882 -26.972 12.087  0.50 26.26 ?  105 ASP   B N    1 
ATOM   5641 C  CA   A ASP   B 1 105 ? 33.667 -27.286 11.617  0.50 28.55 ?  105 ASP   B CA   1 
ATOM   5642 C  CA   B ASP   B 1 105 ? 33.622 -27.459 11.533  0.50 26.58 ?  105 ASP   B CA   1 
ATOM   5643 C  C    A ASP   B 1 105 ? 33.735 -27.348 10.095  0.50 27.03 ?  105 ASP   B C    1 
ATOM   5644 C  C    B ASP   B 1 105 ? 33.676 -27.467 10.010  0.50 25.23 ?  105 ASP   B C    1 
ATOM   5645 O  O    A ASP   B 1 105 ? 33.909 -26.321 9.430   0.50 26.59 ?  105 ASP   B O    1 
ATOM   5646 O  O    B ASP   B 1 105 ? 33.849 -26.417 9.381   0.50 24.58 ?  105 ASP   B O    1 
ATOM   5647 C  CB   A ASP   B 1 105 ? 32.557 -26.337 12.058  0.50 31.06 ?  105 ASP   B CB   1 
ATOM   5648 C  CB   B ASP   B 1 105 ? 32.467 -26.585 12.020  0.50 28.59 ?  105 ASP   B CB   1 
ATOM   5649 C  CG   A ASP   B 1 105 ? 31.183 -26.800 11.618  0.50 33.16 ?  105 ASP   B CG   1 
ATOM   5650 C  CG   B ASP   B 1 105 ? 31.107 -27.177 11.685  0.50 30.10 ?  105 ASP   B CG   1 
ATOM   5651 O  OD1  A ASP   B 1 105 ? 31.063 -27.937 11.115  0.50 33.53 ?  105 ASP   B OD1  1 
ATOM   5652 O  OD1  B ASP   B 1 105 ? 31.054 -28.152 10.905  0.50 30.43 ?  105 ASP   B OD1  1 
ATOM   5653 O  OD2  A ASP   B 1 105 ? 30.220 -26.016 11.767  0.50 34.38 -1 105 ASP   B OD2  1 
ATOM   5654 O  OD2  B ASP   B 1 105 ? 30.089 -26.680 12.214  0.50 30.46 -1 105 ASP   B OD2  1 
ATOM   5655 H  H    A ASP   B 1 105 ? 34.927 -26.033 12.477  0.50 33.50 ?  105 ASP   B H    1 
ATOM   5656 H  H    B ASP   B 1 105 ? 34.841 -26.168 12.392  0.50 31.55 ?  105 ASP   B H    1 
ATOM   5657 H  HA   A ASP   B 1 105 ? 33.469 -28.174 11.952  0.50 34.30 ?  105 ASP   B HA   1 
ATOM   5658 H  HA   B ASP   B 1 105 ? 33.466 -28.365 11.838  0.50 31.93 ?  105 ASP   B HA   1 
ATOM   5659 H  HB2  A ASP   B 1 105 ? 32.578 -26.260 13.027  0.50 37.30 ?  105 ASP   B HB2  1 
ATOM   5660 H  HB2  B ASP   B 1 105 ? 32.522 -26.494 12.984  0.50 34.34 ?  105 ASP   B HB2  1 
ATOM   5661 H  HB3  A ASP   B 1 105 ? 32.701 -25.472 11.652  0.50 37.30 ?  105 ASP   B HB3  1 
ATOM   5662 H  HB3  B ASP   B 1 105 ? 32.539 -25.708 11.603  0.50 34.34 ?  105 ASP   B HB3  1 
ATOM   5663 N  N    A ILE   B 1 106 ? 33.567 -28.553 9.546   0.50 26.46 ?  106 ILE   B N    1 
ATOM   5664 N  N    B ILE   B 1 106 ? 33.495 -28.652 9.419   0.50 24.90 ?  106 ILE   B N    1 
ATOM   5665 C  CA   A ILE   B 1 106 ? 33.574 -28.743 8.100   0.50 25.59 ?  106 ILE   B CA   1 
ATOM   5666 C  CA   B ILE   B 1 106 ? 33.500 -28.794 7.968   0.50 24.38 ?  106 ILE   B CA   1 
ATOM   5667 C  C    A ILE   B 1 106 ? 32.475 -27.937 7.418   0.50 24.55 ?  106 ILE   B C    1 
ATOM   5668 C  C    B ILE   B 1 106 ? 32.414 -27.950 7.314   0.50 23.55 ?  106 ILE   B C    1 
ATOM   5669 O  O    A ILE   B 1 106 ? 32.576 -27.639 6.223   0.50 23.96 ?  106 ILE   B O    1 
ATOM   5670 O  O    B ILE   B 1 106 ? 32.514 -27.622 6.126   0.50 22.75 ?  106 ILE   B O    1 
ATOM   5671 C  CB   A ILE   B 1 106 ? 33.477 -30.252 7.777   0.50 26.10 ?  106 ILE   B CB   1 
ATOM   5672 C  CB   B ILE   B 1 106 ? 33.384 -30.291 7.593   0.50 25.13 ?  106 ILE   B CB   1 
ATOM   5673 C  CG1  A ILE   B 1 106 ? 33.716 -30.512 6.288   0.50 26.31 ?  106 ILE   B CG1  1 
ATOM   5674 C  CG1  B ILE   B 1 106 ? 33.692 -30.511 6.111   0.50 25.66 ?  106 ILE   B CG1  1 
ATOM   5675 C  CG2  A ILE   B 1 106 ? 32.126 -30.808 8.210   0.50 26.66 ?  106 ILE   B CG2  1 
ATOM   5676 C  CG2  B ILE   B 1 106 ? 31.998 -30.825 7.932   0.50 25.69 ?  106 ILE   B CG2  1 
ATOM   5677 C  CD1  A ILE   B 1 106 ? 35.073 -30.053 5.803   0.50 26.29 ?  106 ILE   B CD1  1 
ATOM   5678 C  CD1  B ILE   B 1 106 ? 35.079 -30.063 5.710   0.50 25.84 ?  106 ILE   B CD1  1 
ATOM   5679 H  H    A ILE   B 1 106 ? 33.450 -29.275 9.994   0.50 31.79 ?  106 ILE   B H    1 
ATOM   5680 H  H    B ILE   B 1 106 ? 33.369 -29.387 9.842   0.50 29.92 ?  106 ILE   B H    1 
ATOM   5681 H  HA   A ILE   B 1 106 ? 34.421 -28.421 7.761   0.50 30.74 ?  106 ILE   B HA   1 
ATOM   5682 H  HA   B ILE   B 1 106 ? 34.349 -28.472 7.637   0.50 29.29 ?  106 ILE   B HA   1 
ATOM   5683 H  HB   A ILE   B 1 106 ? 34.167 -30.712 8.278   0.50 31.35 ?  106 ILE   B HB   1 
ATOM   5684 H  HB   B ILE   B 1 106 ? 34.034 -30.787 8.115   0.50 30.19 ?  106 ILE   B HB   1 
ATOM   5685 H  HG12 A ILE   B 1 106 ? 33.657 -31.468 6.124   0.50 31.61 ?  106 ILE   B HG12 1 
ATOM   5686 H  HG12 B ILE   B 1 106 ? 33.622 -31.460 5.914   0.50 30.83 ?  106 ILE   B HG12 1 
ATOM   5687 H  HG13 A ILE   B 1 106 ? 33.043 -30.048 5.770   0.50 31.61 ?  106 ILE   B HG13 1 
ATOM   5688 H  HG13 B ILE   B 1 106 ? 33.054 -30.017 5.577   0.50 30.83 ?  106 ILE   B HG13 1 
ATOM   5689 H  HG21 A ILE   B 1 106 ? 32.138 -31.773 8.111   0.50 32.02 ?  106 ILE   B HG21 1 
ATOM   5690 H  HG21 B ILE   B 1 106 ? 32.006 -31.792 7.861   0.50 30.87 ?  106 ILE   B HG21 1 
ATOM   5691 H  HG22 A ILE   B 1 106 ? 31.971 -30.574 9.138   0.50 32.02 ?  106 ILE   B HG22 1 
ATOM   5692 H  HG22 B ILE   B 1 106 ? 31.773 -30.563 8.839   0.50 30.87 ?  106 ILE   B HG22 1 
ATOM   5693 H  HG23 A ILE   B 1 106 ? 31.432 -30.427 7.651   0.50 32.02 ?  106 ILE   B HG23 1 
ATOM   5694 H  HG23 B ILE   B 1 106 ? 31.353 -30.453 7.312   0.50 30.87 ?  106 ILE   B HG23 1 
ATOM   5695 H  HD11 A ILE   B 1 106 ? 35.252 -30.455 4.940   0.50 31.58 ?  106 ILE   B HD11 1 
ATOM   5696 H  HD11 B ILE   B 1 106 ? 35.308 -30.470 4.861   0.50 31.05 ?  106 ILE   B HD11 1 
ATOM   5697 H  HD12 A ILE   B 1 106 ? 35.069 -29.086 5.722   0.50 31.58 ?  106 ILE   B HD12 1 
ATOM   5698 H  HD12 B ILE   B 1 106 ? 35.087 -29.096 5.626   0.50 31.05 ?  106 ILE   B HD12 1 
ATOM   5699 H  HD13 A ILE   B 1 106 ? 35.748 -30.329 6.444   0.50 31.58 ?  106 ILE   B HD13 1 
ATOM   5700 H  HD13 B ILE   B 1 106 ? 35.711 -30.342 6.392   0.50 31.05 ?  106 ILE   B HD13 1 
ATOM   5701 N  N    A GLN   B 1 107 ? 31.426 -27.561 8.154   0.50 24.76 ?  107 GLN   B N    1 
ATOM   5702 N  N    B GLN   B 1 107 ? 31.377 -27.575 8.067   0.50 24.15 ?  107 GLN   B N    1 
ATOM   5703 C  CA   A GLN   B 1 107 ? 30.343 -26.779 7.568   0.50 24.84 ?  107 GLN   B CA   1 
ATOM   5704 C  CA   B GLN   B 1 107 ? 30.306 -26.756 7.510   0.50 24.62 ?  107 GLN   B CA   1 
ATOM   5705 C  C    A GLN   B 1 107 ? 30.825 -25.435 7.036   0.50 22.82 ?  107 GLN   B C    1 
ATOM   5706 C  C    B GLN   B 1 107 ? 30.801 -25.392 7.043   0.50 22.78 ?  107 GLN   B C    1 
ATOM   5707 O  O    A GLN   B 1 107 ? 30.189 -24.872 6.141   0.50 23.34 ?  107 GLN   B O    1 
ATOM   5708 O  O    B GLN   B 1 107 ? 30.148 -24.769 6.201   0.50 23.48 ?  107 GLN   B O    1 
ATOM   5709 C  CB   A GLN   B 1 107 ? 29.238 -26.569 8.608   0.50 27.89 ?  107 GLN   B CB   1 
ATOM   5710 C  CB   B GLN   B 1 107 ? 29.189 -26.592 8.546   0.50 27.81 ?  107 GLN   B CB   1 
ATOM   5711 C  CG   A GLN   B 1 107 ? 27.913 -26.060 8.048   0.50 30.98 ?  107 GLN   B CG   1 
ATOM   5712 C  CG   B GLN   B 1 107 ? 27.842 -26.169 7.971   0.50 31.02 ?  107 GLN   B CG   1 
ATOM   5713 C  CD   A GLN   B 1 107 ? 27.864 -24.547 7.917   0.50 33.33 ?  107 GLN   B CD   1 
ATOM   5714 C  CD   B GLN   B 1 107 ? 27.692 -24.663 7.856   0.50 33.53 ?  107 GLN   B CD   1 
ATOM   5715 O  OE1  A GLN   B 1 107 ? 28.700 -23.834 8.475   0.50 34.22 ?  107 GLN   B OE1  1 
ATOM   5716 O  OE1  B GLN   B 1 107 ? 28.484 -23.902 8.415   0.50 34.51 ?  107 GLN   B OE1  1 
ATOM   5717 N  NE2  A GLN   B 1 107 ? 26.875 -24.049 7.176   0.50 34.15 ?  107 GLN   B NE2  1 
ATOM   5718 N  NE2  B GLN   B 1 107 ? 26.667 -24.224 7.132   0.50 34.40 ?  107 GLN   B NE2  1 
ATOM   5719 H  H    A GLN   B 1 107 ? 31.326 -27.735 8.987   0.50 29.74 ?  107 GLN   B H    1 
ATOM   5720 H  H    B GLN   B 1 107 ? 31.273 -27.777 8.893   0.50 29.01 ?  107 GLN   B H    1 
ATOM   5721 H  HA   A GLN   B 1 107 ? 29.964 -27.275 6.826   0.50 29.84 ?  107 GLN   B HA   1 
ATOM   5722 H  HA   B GLN   B 1 107 ? 29.931 -27.214 6.742   0.50 29.58 ?  107 GLN   B HA   1 
ATOM   5723 H  HB2  A GLN   B 1 107 ? 29.064 -27.415 9.041   0.50 33.50 ?  107 GLN   B HB2  1 
ATOM   5724 H  HB2  B GLN   B 1 107 ? 29.060 -27.440 8.993   0.50 33.40 ?  107 GLN   B HB2  1 
ATOM   5725 H  HB3  A GLN   B 1 107 ? 29.549 -25.924 9.262   0.50 33.50 ?  107 GLN   B HB3  1 
ATOM   5726 H  HB3  B GLN   B 1 107 ? 29.460 -25.921 9.191   0.50 33.40 ?  107 GLN   B HB3  1 
ATOM   5727 H  HG2  A GLN   B 1 107 ? 27.773 -26.438 7.167   0.50 37.20 ?  107 GLN   B HG2  1 
ATOM   5728 H  HG2  B GLN   B 1 107 ? 27.742 -26.545 7.083   0.50 37.26 ?  107 GLN   B HG2  1 
ATOM   5729 H  HG3  A GLN   B 1 107 ? 27.194 -26.335 8.643   0.50 37.20 ?  107 GLN   B HG3  1 
ATOM   5730 H  HG3  B GLN   B 1 107 ? 27.134 -26.500 8.550   0.50 37.26 ?  107 GLN   B HG3  1 
ATOM   5731 H  HE21 A GLN   B 1 107 ? 26.310 -24.579 6.799   0.50 41.01 ?  107 GLN   B HE21 1 
ATOM   5732 H  HE21 B GLN   B 1 107 ? 26.134 -24.785 6.755   0.50 41.31 ?  107 GLN   B HE21 1 
ATOM   5733 H  HE22 A GLN   B 1 107 ? 26.798 -23.198 7.074   0.50 41.01 ?  107 GLN   B HE22 1 
ATOM   5734 H  HE22 B GLN   B 1 107 ? 26.535 -23.379 7.040   0.50 41.31 ?  107 GLN   B HE22 1 
ATOM   5735 N  N    . LEU   B 1 108 ? 31.942 -24.919 7.554   1.00 20.69 ?  108 LEU   B N    1 
ATOM   5736 C  CA   . LEU   B 1 108 ? 32.487 -23.623 7.144   1.00 18.21 ?  108 LEU   B CA   1 
ATOM   5737 C  C    . LEU   B 1 108 ? 33.126 -23.646 5.764   1.00 15.95 ?  108 LEU   B C    1 
ATOM   5738 O  O    . LEU   B 1 108 ? 33.550 -22.592 5.272   1.00 15.84 ?  108 LEU   B O    1 
ATOM   5739 C  CB   . LEU   B 1 108 ? 33.501 -23.139 8.180   1.00 18.67 ?  108 LEU   B CB   1 
ATOM   5740 C  CG   . LEU   B 1 108 ? 32.882 -22.655 9.490   1.00 20.10 ?  108 LEU   B CG   1 
ATOM   5741 C  CD1  . LEU   B 1 108 ? 33.904 -22.639 10.615  1.00 20.50 ?  108 LEU   B CD1  1 
ATOM   5742 C  CD2  . LEU   B 1 108 ? 32.289 -21.269 9.293   1.00 21.25 ?  108 LEU   B CD2  1 
ATOM   5743 H  H    A LEU   B 1 108 ? 32.401 -25.307 8.165   0.50 24.87 ?  108 LEU   B H    1 
ATOM   5744 H  H    B LEU   B 1 108 ? 32.410 -25.328 8.144   0.50 24.87 ?  108 LEU   B H    1 
ATOM   5745 H  HA   . LEU   B 1 108 ? 31.764 -22.982 7.120   1.00 21.89 ?  108 LEU   B HA   1 
ATOM   5746 H  HB2  . LEU   B 1 108 ? 34.100 -23.871 8.395   1.00 22.44 ?  108 LEU   B HB2  1 
ATOM   5747 H  HB3  . LEU   B 1 108 ? 34.001 -22.403 7.803   1.00 22.44 ?  108 LEU   B HB3  1 
ATOM   5748 H  HG   . LEU   B 1 108 ? 32.162 -23.254 9.748   1.00 24.16 ?  108 LEU   B HG   1 
ATOM   5749 H  HD11 . LEU   B 1 108 ? 33.468 -22.355 11.436  1.00 24.64 ?  108 LEU   B HD11 1 
ATOM   5750 H  HD12 . LEU   B 1 108 ? 34.267 -23.531 10.726  1.00 24.64 ?  108 LEU   B HD12 1 
ATOM   5751 H  HD13 . LEU   B 1 108 ? 34.614 -22.018 10.388  1.00 24.64 ?  108 LEU   B HD13 1 
ATOM   5752 H  HD21 . LEU   B 1 108 ? 31.944 -20.949 10.141  1.00 25.53 ?  108 LEU   B HD21 1 
ATOM   5753 H  HD22 . LEU   B 1 108 ? 32.985 -20.673 8.974   1.00 25.53 ?  108 LEU   B HD22 1 
ATOM   5754 H  HD23 . LEU   B 1 108 ? 31.573 -21.321 8.642   1.00 25.53 ?  108 LEU   B HD23 1 
ATOM   5755 N  N    . LEU   B 1 109 ? 33.196 -24.816 5.134   1.00 14.99 ?  109 LEU   B N    1 
ATOM   5756 C  CA   . LEU   B 1 109 ? 33.823 -24.920 3.826   1.00 14.26 ?  109 LEU   B CA   1 
ATOM   5757 C  C    . LEU   B 1 109 ? 33.058 -24.129 2.772   1.00 13.80 ?  109 LEU   B C    1 
ATOM   5758 O  O    . LEU   B 1 109 ? 33.672 -23.530 1.884   1.00 13.39 ?  109 LEU   B O    1 
ATOM   5759 C  CB   . LEU   B 1 109 ? 33.934 -26.392 3.441   1.00 14.37 ?  109 LEU   B CB   1 
ATOM   5760 C  CG   . LEU   B 1 109 ? 34.717 -26.725 2.174   1.00 13.96 ?  109 LEU   B CG   1 
ATOM   5761 C  CD1  . LEU   B 1 109 ? 36.092 -26.057 2.182   1.00 13.95 ?  109 LEU   B CD1  1 
ATOM   5762 C  CD2  . LEU   B 1 109 ? 34.849 -28.241 2.029   1.00 15.04 ?  109 LEU   B CD2  1 
ATOM   5763 H  H    . LEU   B 1 109 ? 32.891 -25.558 5.437   1.00 18.02 ?  109 LEU   B H    1 
ATOM   5764 H  HA   . LEU   B 1 109 ? 34.717 -24.557 3.873   1.00 17.15 ?  109 LEU   B HA   1 
ATOM   5765 H  HB2  . LEU   B 1 109 ? 34.369 -26.866 4.168   1.00 17.27 ?  109 LEU   B HB2  1 
ATOM   5766 H  HB3  . LEU   B 1 109 ? 33.040 -26.750 3.320   1.00 17.27 ?  109 LEU   B HB3  1 
ATOM   5767 H  HG   . LEU   B 1 109 ? 34.227 -26.402 1.399   1.00 16.78 ?  109 LEU   B HG   1 
ATOM   5768 H  HD11 . LEU   B 1 109 ? 36.628 -26.422 1.462   1.00 16.77 ?  109 LEU   B HD11 1 
ATOM   5769 H  HD12 . LEU   B 1 109 ? 35.976 -25.102 2.056   1.00 16.77 ?  109 LEU   B HD12 1 
ATOM   5770 H  HD13 . LEU   B 1 109 ? 36.520 -26.231 3.035   1.00 16.77 ?  109 LEU   B HD13 1 
ATOM   5771 H  HD21 . LEU   B 1 109 ? 35.418 -28.439 1.266   1.00 18.08 ?  109 LEU   B HD21 1 
ATOM   5772 H  HD22 . LEU   B 1 109 ? 35.244 -28.602 2.836   1.00 18.08 ?  109 LEU   B HD22 1 
ATOM   5773 H  HD23 . LEU   B 1 109 ? 33.968 -28.626 1.889   1.00 18.08 ?  109 LEU   B HD23 1 
ATOM   5774 N  N    . LYS   B 1 110 ? 31.723 -24.099 2.855   1.00 13.40 ?  110 LYS   B N    1 
ATOM   5775 C  CA   . LYS   B 1 110 ? 30.964 -23.332 1.870   1.00 13.14 ?  110 LYS   B CA   1 
ATOM   5776 C  C    . LYS   B 1 110 ? 31.305 -21.843 1.958   1.00 12.80 ?  110 LYS   B C    1 
ATOM   5777 O  O    . LYS   B 1 110 ? 31.560 -21.194 0.939   1.00 12.68 ?  110 LYS   B O    1 
ATOM   5778 C  CB   . LYS   B 1 110 ? 29.458 -23.573 2.017   1.00 13.97 ?  110 LYS   B CB   1 
ATOM   5779 C  CG   . LYS   B 1 110 ? 28.654 -22.950 0.877   1.00 14.21 ?  110 LYS   B CG   1 
ATOM   5780 C  CD   . LYS   B 1 110 ? 27.184 -23.379 0.899   1.00 14.69 ?  110 LYS   B CD   1 
ATOM   5781 C  CE   . LYS   B 1 110 ? 26.409 -22.845 -0.315  1.00 15.19 ?  110 LYS   B CE   1 
ATOM   5782 N  NZ   . LYS   B 1 110 ? 26.741 -23.554 -1.581  1.00 15.28 ?  110 LYS   B NZ   1 
ATOM   5783 H  H    . LYS   B 1 110 ? 31.252 -24.507 3.447   1.00 16.12 ?  110 LYS   B H    1 
ATOM   5784 H  HA   . LYS   B 1 110 ? 31.219 -23.633 0.984   1.00 15.80 ?  110 LYS   B HA   1 
ATOM   5785 H  HB2  . LYS   B 1 110 ? 29.287 -24.529 2.016   1.00 16.80 ?  110 LYS   B HB2  1 
ATOM   5786 H  HB3  . LYS   B 1 110 ? 29.151 -23.182 2.848   1.00 16.80 ?  110 LYS   B HB3  1 
ATOM   5787 H  HG2  . LYS   B 1 110 ? 28.680 -21.986 0.954   1.00 17.09 ?  110 LYS   B HG2  1 
ATOM   5788 H  HG3  . LYS   B 1 110 ? 29.029 -23.230 0.028   1.00 17.09 ?  110 LYS   B HG3  1 
ATOM   5789 H  HD2  . LYS   B 1 110 ? 27.129 -24.351 0.886   1.00 17.67 ?  110 LYS   B HD2  1 
ATOM   5790 H  HD3  . LYS   B 1 110 ? 26.758 -23.036 1.701   1.00 17.67 ?  110 LYS   B HD3  1 
ATOM   5791 H  HE2  . LYS   B 1 110 ? 25.459 -22.947 -0.158  1.00 18.26 ?  110 LYS   B HE2  1 
ATOM   5792 H  HE3  . LYS   B 1 110 ? 26.626 -21.907 -0.437  1.00 18.26 ?  110 LYS   B HE3  1 
ATOM   5793 H  HZ1  . LYS   B 1 110 ? 26.273 -23.210 -2.254  1.00 18.36 ?  110 LYS   B HZ1  1 
ATOM   5794 H  HZ2  . LYS   B 1 110 ? 27.609 -23.471 -1.758  1.00 18.36 ?  110 LYS   B HZ2  1 
ATOM   5795 H  HZ3  . LYS   B 1 110 ? 26.544 -24.420 -1.503  1.00 18.36 ?  110 LYS   B HZ3  1 
ATOM   5796 N  N    . SER   B 1 111 ? 31.330 -21.293 3.176   1.00 13.12 ?  111 SER   B N    1 
ATOM   5797 C  CA   . SER   B 1 111 ? 31.718 -19.894 3.353   1.00 13.00 ?  111 SER   B CA   1 
ATOM   5798 C  C    . SER   B 1 111 ? 33.099 -19.628 2.766   1.00 12.62 ?  111 SER   B C    1 
ATOM   5799 O  O    . SER   B 1 111 ? 33.326 -18.593 2.121   1.00 12.88 ?  111 SER   B O    1 
ATOM   5800 C  CB   . SER   B 1 111 ? 31.711 -19.536 4.840   1.00 14.03 ?  111 SER   B CB   1 
ATOM   5801 O  OG   . SER   B 1 111 ? 30.402 -19.549 5.374   1.00 16.01 ?  111 SER   B OG   1 
ATOM   5802 H  H    . SER   B 1 111 ? 31.131 -21.707 3.906   1.00 15.78 ?  111 SER   B H    1 
ATOM   5803 H  HA   . SER   B 1 111 ? 31.080 -19.325 2.900   1.00 15.63 ?  111 SER   B HA   1 
ATOM   5804 H  HB2  . SER   B 1 111 ? 32.243 -20.183 5.326   1.00 16.87 ?  111 SER   B HB2  1 
ATOM   5805 H  HB3  . SER   B 1 111 ? 32.085 -18.649 4.954   1.00 16.87 ?  111 SER   B HB3  1 
ATOM   5806 H  HG   . SER   B 1 111 ? 30.418 -19.340 6.195   1.00 19.25 ?  111 SER   B HG   1 
ATOM   5807 N  N    . ALA   B 1 112 ? 34.039 -20.547 2.986   1.00 12.67 ?  112 ALA   B N    1 
ATOM   5808 C  CA   . ALA   B 1 112 ? 35.382 -20.377 2.442   1.00 12.49 ?  112 ALA   B CA   1 
ATOM   5809 C  C    . ALA   B 1 112 ? 35.349 -20.284 0.919   1.00 11.72 ?  112 ALA   B C    1 
ATOM   5810 O  O    . ALA   B 1 112 ? 35.967 -19.390 0.327   1.00 12.08 ?  112 ALA   B O    1 
ATOM   5811 C  CB   . ALA   B 1 112 ? 36.284 -21.520 2.914   1.00 13.00 ?  112 ALA   B CB   1 
ATOM   5812 H  H    . ALA   B 1 112 ? 33.925 -21.271 3.443   1.00 15.24 ?  112 ALA   B H    1 
ATOM   5813 H  HA   . ALA   B 1 112 ? 35.751 -19.548 2.782   1.00 15.03 ?  112 ALA   B HA   1 
ATOM   5814 H  HB1  . ALA   B 1 112 ? 37.175 -21.386 2.551   1.00 15.63 ?  112 ALA   B HB1  1 
ATOM   5815 H  HB2  . ALA   B 1 112 ? 36.324 -21.508 3.886   1.00 15.63 ?  112 ALA   B HB2  1 
ATOM   5816 H  HB3  . ALA   B 1 112 ? 35.922 -22.360 2.607   1.00 15.63 ?  112 ALA   B HB3  1 
ATOM   5817 N  N    . TYR   B 1 113 ? 34.616 -21.187 0.261   1.00 11.83 ?  113 TYR   B N    1 
ATOM   5818 C  CA   . TYR   B 1 113 ? 34.537 -21.135 -1.195  1.00 11.59 ?  113 TYR   B CA   1 
ATOM   5819 C  C    . TYR   B 1 113 ? 33.829 -19.881 -1.704  1.00 11.09 ?  113 TYR   B C    1 
ATOM   5820 O  O    . TYR   B 1 113 ? 34.102 -19.444 -2.827  1.00 11.52 ?  113 TYR   B O    1 
ATOM   5821 C  CB   . TYR   B 1 113 ? 33.863 -22.391 -1.753  1.00 11.67 ?  113 TYR   B CB   1 
ATOM   5822 C  CG   . TYR   B 1 113 ? 34.824 -23.544 -2.017  1.00 12.09 ?  113 TYR   B CG   1 
ATOM   5823 C  CD1  . TYR   B 1 113 ? 35.817 -23.442 -2.988  1.00 12.53 ?  113 TYR   B CD1  1 
ATOM   5824 C  CD2  . TYR   B 1 113 ? 34.736 -24.733 -1.305  1.00 12.31 ?  113 TYR   B CD2  1 
ATOM   5825 C  CE1  . TYR   B 1 113 ? 36.698 -24.475 -3.236  1.00 12.83 ?  113 TYR   B CE1  1 
ATOM   5826 C  CE2  . TYR   B 1 113 ? 35.606 -25.786 -1.553  1.00 12.48 ?  113 TYR   B CE2  1 
ATOM   5827 C  CZ   . TYR   B 1 113 ? 36.580 -25.654 -2.525  1.00 12.93 ?  113 TYR   B CZ   1 
ATOM   5828 O  OH   . TYR   B 1 113 ? 37.459 -26.670 -2.795  1.00 13.42 ?  113 TYR   B OH   1 
ATOM   5829 H  H    . TYR   B 1 113 ? 34.158 -21.821 0.631   1.00 14.22 ?  113 TYR   B H    1 
ATOM   5830 H  HA   . TYR   B 1 113 ? 35.438 -21.115 -1.535  1.00 13.94 ?  113 TYR   B HA   1 
ATOM   5831 H  HB2  . TYR   B 1 113 ? 33.200 -22.706 -1.117  1.00 14.04 ?  113 TYR   B HB2  1 
ATOM   5832 H  HB3  . TYR   B 1 113 ? 33.432 -22.167 -2.591  1.00 14.04 ?  113 TYR   B HB3  1 
ATOM   5833 H  HD1  . TYR   B 1 113 ? 35.897 -22.649 -3.477  1.00 15.07 ?  113 TYR   B HD1  1 
ATOM   5834 H  HD2  . TYR   B 1 113 ? 34.077 -24.827 -0.660  1.00 14.80 ?  113 TYR   B HD2  1 
ATOM   5835 H  HE1  . TYR   B 1 113 ? 37.353 -24.386 -3.900  1.00 15.42 ?  113 TYR   B HE1  1 
ATOM   5836 H  HE2  . TYR   B 1 113 ? 35.530 -26.576 -1.076  1.00 15.01 ?  113 TYR   B HE2  1 
ATOM   5837 H  HH   . TYR   B 1 113 ? 37.278 -27.334 -2.311  1.00 16.14 ?  113 TYR   B HH   1 
ATOM   5838 N  N    . GLU   B 1 114 ? 32.909 -19.304 -0.923  1.00 11.33 ?  114 GLU   B N    1 
ATOM   5839 C  CA   . GLU   B 1 114 ? 32.224 -18.097 -1.377  1.00 11.26 ?  114 GLU   B CA   1 
ATOM   5840 C  C    . GLU   B 1 114 ? 33.205 -16.972 -1.674  1.00 11.34 ?  114 GLU   B C    1 
ATOM   5841 O  O    . GLU   B 1 114 ? 32.919 -16.106 -2.507  1.00 11.77 ?  114 GLU   B O    1 
ATOM   5842 C  CB   . GLU   B 1 114 ? 31.167 -17.667 -0.356  1.00 11.66 ?  114 GLU   B CB   1 
ATOM   5843 C  CG   . GLU   B 1 114 ? 29.942 -18.583 -0.433  1.00 12.05 ?  114 GLU   B CG   1 
ATOM   5844 C  CD   . GLU   B 1 114 ? 28.922 -18.408 0.683   1.00 12.37 ?  114 GLU   B CD   1 
ATOM   5845 O  OE1  . GLU   B 1 114 ? 29.220 -17.799 1.732   1.00 12.59 ?  114 GLU   B OE1  1 
ATOM   5846 O  OE2  . GLU   B 1 114 ? 27.794 -18.939 0.519   1.00 13.21 -1 114 GLU   B OE2  1 
ATOM   5847 H  H    . GLU   B 1 114 ? 32.670 -19.590 -0.144  1.00 13.63 ?  114 GLU   B H    1 
ATOM   5848 H  HA   . GLU   B 1 114 ? 31.765 -18.300 -2.197  1.00 13.54 ?  114 GLU   B HA   1 
ATOM   5849 H  HB2  . GLU   B 1 114 ? 31.536 -17.728 0.543   1.00 14.03 ?  114 GLU   B HB2  1 
ATOM   5850 H  HB3  . GLU   B 1 114 ? 30.884 -16.762 -0.543  1.00 14.03 ?  114 GLU   B HB3  1 
ATOM   5851 H  HG2  . GLU   B 1 114 ? 29.488 -18.415 -1.270  1.00 14.49 ?  114 GLU   B HG2  1 
ATOM   5852 H  HG3  . GLU   B 1 114 ? 30.247 -19.505 -0.407  1.00 14.49 ?  114 GLU   B HG3  1 
ATOM   5853 N  N    . ASN   B 1 115 ? 34.375 -16.970 -1.026  1.00 11.06 ?  115 ASN   B N    1 
ATOM   5854 C  CA   . ASN   B 1 115 ? 35.366 -15.938 -1.322  1.00 11.05 ?  115 ASN   B CA   1 
ATOM   5855 C  C    . ASN   B 1 115 ? 35.771 -15.953 -2.789  1.00 10.74 ?  115 ASN   B C    1 
ATOM   5856 O  O    . ASN   B 1 115 ? 36.157 -14.909 -3.342  1.00 11.42 ?  115 ASN   B O    1 
ATOM   5857 C  CB   . ASN   B 1 115 ? 36.608 -16.112 -0.441  1.00 11.58 ?  115 ASN   B CB   1 
ATOM   5858 C  CG   . ASN   B 1 115 ? 36.338 -15.851 1.026   1.00 12.10 ?  115 ASN   B CG   1 
ATOM   5859 O  OD1  . ASN   B 1 115 ? 36.337 -14.705 1.467   1.00 14.09 ?  115 ASN   B OD1  1 
ATOM   5860 N  ND2  . ASN   B 1 115 ? 36.170 -16.919 1.805   1.00 12.27 ?  115 ASN   B ND2  1 
ATOM   5861 H  H    . ASN   B 1 115 ? 34.610 -17.534 -0.415  1.00 13.30 ?  115 ASN   B H    1 
ATOM   5862 H  HA   . ASN   B 1 115 ? 34.987 -15.067 -1.125  1.00 13.29 ?  115 ASN   B HA   1 
ATOM   5863 H  HB2  . ASN   B 1 115 ? 36.936 -17.021 -0.530  1.00 13.93 ?  115 ASN   B HB2  1 
ATOM   5864 H  HB3  . ASN   B 1 115 ? 37.293 -15.486 -0.734  1.00 13.93 ?  115 ASN   B HB3  1 
ATOM   5865 H  HD21 . ASN   B 1 115 ? 36.027 -16.812 2.650   1.00 14.75 ?  115 ASN   B HD21 1 
ATOM   5866 H  HD22 . ASN   B 1 115 ? 36.190 -17.705 1.469   1.00 14.75 ?  115 ASN   B HD22 1 
ATOM   5867 N  N    . PHE   B 1 116 ? 35.746 -17.131 -3.426  1.00 10.59 ?  116 PHE   B N    1 
ATOM   5868 C  CA   . PHE   B 1 116 ? 36.173 -17.219 -4.818  1.00 11.04 ?  116 PHE   B CA   1 
ATOM   5869 C  C    . PHE   B 1 116 ? 35.267 -16.394 -5.728  1.00 10.76 ?  116 PHE   B C    1 
ATOM   5870 O  O    . PHE   B 1 116 ? 35.699 -15.964 -6.802  1.00 11.36 ?  116 PHE   B O    1 
ATOM   5871 C  CB   . PHE   B 1 116 ? 36.147 -18.666 -5.343  1.00 10.84 ?  116 PHE   B CB   1 
ATOM   5872 C  CG   . PHE   B 1 116 ? 37.218 -19.620 -4.792  1.00 10.85 ?  116 PHE   B CG   1 
ATOM   5873 C  CD1  . PHE   B 1 116 ? 37.873 -19.432 -3.585  1.00 11.63 ?  116 PHE   B CD1  1 
ATOM   5874 C  CD2  . PHE   B 1 116 ? 37.521 -20.758 -5.529  1.00 11.16 ?  116 PHE   B CD2  1 
ATOM   5875 C  CE1  . PHE   B 1 116 ? 38.803 -20.373 -3.131  1.00 11.74 ?  116 PHE   B CE1  1 
ATOM   5876 C  CE2  . PHE   B 1 116 ? 38.449 -21.694 -5.082  1.00 11.03 ?  116 PHE   B CE2  1 
ATOM   5877 C  CZ   . PHE   B 1 116 ? 39.087 -21.504 -3.888  1.00 11.19 ?  116 PHE   B CZ   1 
ATOM   5878 H  H    . PHE   B 1 116 ? 35.485 -17.879 -3.080  1.00 12.74 ?  116 PHE   B H    1 
ATOM   5879 H  HA   . PHE   B 1 116 ? 37.078 -16.884 -4.898  1.00 13.28 ?  116 PHE   B HA   1 
ATOM   5880 H  HB2  . PHE   B 1 116 ? 35.276 -19.050 -5.126  1.00 13.04 ?  116 PHE   B HB2  1 
ATOM   5881 H  HB3  . PHE   B 1 116 ? 36.247 -18.641 -6.307  1.00 13.04 ?  116 PHE   B HB3  1 
ATOM   5882 H  HD1  . PHE   B 1 116 ? 37.671 -18.682 -3.067  1.00 13.99 ?  116 PHE   B HD1  1 
ATOM   5883 H  HD2  . PHE   B 1 116 ? 37.083 -20.909 -6.336  1.00 13.42 ?  116 PHE   B HD2  1 
ATOM   5884 H  HE1  . PHE   B 1 116 ? 39.241 -20.233 -2.324  1.00 14.12 ?  116 PHE   B HE1  1 
ATOM   5885 H  HE2  . PHE   B 1 116 ? 38.642 -22.444 -5.594  1.00 13.27 ?  116 PHE   B HE2  1 
ATOM   5886 H  HZ   . PHE   B 1 116 ? 39.721 -22.112 -3.593  1.00 13.46 ?  116 PHE   B HZ   1 
ATOM   5887 N  N    . ASN   B 1 117 ? 34.000 -16.191 -5.340  1.00 11.59 ?  117 ASN   B N    1 
ATOM   5888 C  CA   . ASN   B 1 117 ? 33.052 -15.486 -6.202  1.00 11.62 ?  117 ASN   B CA   1 
ATOM   5889 C  C    . ASN   B 1 117 ? 33.368 -14.006 -6.354  1.00 11.87 ?  117 ASN   B C    1 
ATOM   5890 O  O    . ASN   B 1 117 ? 32.770 -13.348 -7.210  1.00 12.87 ?  117 ASN   B O    1 
ATOM   5891 C  CB   . ASN   B 1 117 ? 31.625 -15.708 -5.714  1.00 11.81 ?  117 ASN   B CB   1 
ATOM   5892 C  CG   . ASN   B 1 117 ? 31.178 -17.119 -5.962  1.00 12.16 ?  117 ASN   B CG   1 
ATOM   5893 O  OD1  . ASN   B 1 117 ? 31.536 -17.712 -6.980  1.00 12.84 ?  117 ASN   B OD1  1 
ATOM   5894 N  ND2  . ASN   B 1 117 ? 30.437 -17.688 -5.025  1.00 11.92 ?  117 ASN   B ND2  1 
ATOM   5895 H  H    . ASN   B 1 117 ? 33.678 -16.446 -4.580  1.00 13.95 ?  117 ASN   B H    1 
ATOM   5896 H  HA   . ASN   B 1 117 ? 33.114 -15.880 -7.079  1.00 13.98 ?  117 ASN   B HA   1 
ATOM   5897 H  HB2  . ASN   B 1 117 ? 31.578 -15.539 -4.757  1.00 14.20 ?  117 ASN   B HB2  1 
ATOM   5898 H  HB3  . ASN   B 1 117 ? 31.030 -15.104 -6.187  1.00 14.20 ?  117 ASN   B HB3  1 
ATOM   5899 H  HD21 . ASN   B 1 117 ? 30.160 -18.493 -5.125  1.00 14.34 ?  117 ASN   B HD21 1 
ATOM   5900 H  HD22 . ASN   B 1 117 ? 30.216 -17.239 -4.323  1.00 14.34 ?  117 ASN   B HD22 1 
ATOM   5901 N  N    . GLN   B 1 118 ? 34.301 -13.480 -5.574  1.00 11.61 ?  118 GLN   B N    1 
ATOM   5902 C  CA   . GLN   B 1 118 ? 34.734 -12.093 -5.707  1.00 11.91 ?  118 GLN   B CA   1 
ATOM   5903 C  C    . GLN   B 1 118 ? 35.799 -11.899 -6.779  1.00 12.02 ?  118 GLN   B C    1 
ATOM   5904 O  O    . GLN   B 1 118 ? 36.273 -10.770 -6.960  1.00 13.55 ?  118 GLN   B O    1 
ATOM   5905 C  CB   . GLN   B 1 118 ? 35.208 -11.564 -4.351  1.00 12.60 ?  118 GLN   B CB   1 
ATOM   5906 C  CG   . GLN   B 1 118 ? 34.122 -11.608 -3.283  1.00 12.88 ?  118 GLN   B CG   1 
ATOM   5907 C  CD   . GLN   B 1 118 ? 32.952 -10.702 -3.611  1.00 12.67 ?  118 GLN   B CD   1 
ATOM   5908 O  OE1  . GLN   B 1 118 ? 33.139 -9.557  -4.052  1.00 13.52 ?  118 GLN   B OE1  1 
ATOM   5909 N  NE2  . GLN   B 1 118 ? 31.737 -11.197 -3.403  1.00 13.13 ?  118 GLN   B NE2  1 
ATOM   5910 H  H    . GLN   B 1 118 ? 34.715 -13.906 -4.944  1.00 13.96 ?  118 GLN   B H    1 
ATOM   5911 H  HA   . GLN   B 1 118 ? 33.967 -11.563 -5.971  1.00 14.33 ?  118 GLN   B HA   1 
ATOM   5912 H  HB2  . GLN   B 1 118 ? 35.955 -12.092 -4.040  1.00 15.16 ?  118 GLN   B HB2  1 
ATOM   5913 H  HB3  . GLN   B 1 118 ? 35.481 -10.632 -4.451  1.00 15.16 ?  118 GLN   B HB3  1 
ATOM   5914 H  HG2  . GLN   B 1 118 ? 33.789 -12.518 -3.209  1.00 15.49 ?  118 GLN   B HG2  1 
ATOM   5915 H  HG3  . GLN   B 1 118 ? 34.495 -11.323 -2.434  1.00 15.49 ?  118 GLN   B HG3  1 
ATOM   5916 H  HE21 . GLN   B 1 118 ? 31.644 -11.994 -3.094  1.00 15.79 ?  118 GLN   B HE21 1 
ATOM   5917 H  HE22 . GLN   B 1 118 ? 31.048 -10.718 -3.578  1.00 15.79 ?  118 GLN   B HE22 1 
ATOM   5918 N  N    . HIS   B 1 119 ? 36.160 -12.959 -7.506  1.00 11.46 ?  119 HIS   B N    1 
ATOM   5919 C  CA   . HIS   B 1 119 ? 37.197 -12.910 -8.530  1.00 12.12 ?  119 HIS   B CA   1 
ATOM   5920 C  C    . HIS   B 1 119 ? 36.715 -13.643 -9.770  1.00 11.92 ?  119 HIS   B C    1 
ATOM   5921 O  O    . HIS   B 1 119 ? 36.202 -14.758 -9.671  1.00 12.48 ?  119 HIS   B O    1 
ATOM   5922 C  CB   . HIS   B 1 119 ? 38.486 -13.531 -7.990  1.00 12.47 ?  119 HIS   B CB   1 
ATOM   5923 C  CG   . HIS   B 1 119 ? 38.968 -12.835 -6.763  1.00 13.71 ?  119 HIS   B CG   1 
ATOM   5924 N  ND1  . HIS   B 1 119 ? 39.761 -11.707 -6.814  1.00 15.25 ?  119 HIS   B ND1  1 
ATOM   5925 C  CD2  . HIS   B 1 119 ? 38.680 -13.038 -5.457  1.00 14.99 ?  119 HIS   B CD2  1 
ATOM   5926 C  CE1  . HIS   B 1 119 ? 39.970 -11.271 -5.585  1.00 16.21 ?  119 HIS   B CE1  1 
ATOM   5927 N  NE2  . HIS   B 1 119 ? 39.319 -12.055 -4.745  1.00 16.21 ?  119 HIS   B NE2  1 
ATOM   5928 H  H    . HIS   B 1 119 ? 35.802 -13.740 -7.426  1.00 13.79 ?  119 HIS   B H    1 
ATOM   5929 H  HA   . HIS   B 1 119 ? 37.374 -11.984 -8.766  1.00 14.57 ?  119 HIS   B HA   1 
ATOM   5930 H  HB2  . HIS   B 1 119 ? 38.327 -14.458 -7.773  1.00 15.00 ?  119 HIS   B HB2  1 
ATOM   5931 H  HB3  . HIS   B 1 119 ? 39.179 -13.458 -8.670  1.00 15.00 ?  119 HIS   B HB3  1 
ATOM   5932 H  HD2  . HIS   B 1 119 ? 38.152 -13.722 -5.110  1.00 18.02 ?  119 HIS   B HD2  1 
ATOM   5933 H  HE1  . HIS   B 1 119 ? 40.499 -10.543 -5.343  1.00 19.49 ?  119 HIS   B HE1  1 
ATOM   5934 H  HE2  . HIS   B 1 119 ? 39.325 -11.987 -3.884  1.00 19.49 ?  119 HIS   B HE2  1 
ATOM   5935 N  N    . GLU   B 1 120 ? 36.873 -13.022 -10.940 1.00 12.42 ?  120 GLU   B N    1 
ATOM   5936 C  CA   . GLU   B 1 120 ? 36.285 -13.598 -12.145 1.00 13.75 ?  120 GLU   B CA   1 
ATOM   5937 C  C    . GLU   B 1 120 ? 36.955 -14.901 -12.565 1.00 12.64 ?  120 GLU   B C    1 
ATOM   5938 O  O    . GLU   B 1 120 ? 36.290 -15.775 -13.138 1.00 12.96 ?  120 GLU   B O    1 
ATOM   5939 C  CB   . GLU   B 1 120 ? 36.305 -12.580 -13.283 1.00 18.16 ?  120 GLU   B CB   1 
ATOM   5940 C  CG   . GLU   B 1 120 ? 35.323 -11.441 -13.069 1.00 24.37 ?  120 GLU   B CG   1 
ATOM   5941 C  CD   . GLU   B 1 120 ? 35.103 -10.607 -14.313 1.00 30.31 ?  120 GLU   B CD   1 
ATOM   5942 O  OE1  . GLU   B 1 120 ? 36.079 -10.375 -15.057 1.00 32.54 ?  120 GLU   B OE1  1 
ATOM   5943 O  OE2  . GLU   B 1 120 ? 33.949 -10.189 -14.544 1.00 33.11 -1 120 GLU   B OE2  1 
ATOM   5944 H  H    . GLU   B 1 120 ? 37.303 -12.283 -11.061 1.00 14.94 ?  120 GLU   B H    1 
ATOM   5945 H  HA   . GLU   B 1 120 ? 35.360 -13.802 -11.961 1.00 16.54 ?  120 GLU   B HA   1 
ATOM   5946 H  HB2  . GLU   B 1 120 ? 37.192 -12.195 -13.356 1.00 21.82 ?  120 GLU   B HB2  1 
ATOM   5947 H  HB3  . GLU   B 1 120 ? 36.067 -13.023 -14.113 1.00 21.82 ?  120 GLU   B HB3  1 
ATOM   5948 H  HG2  . GLU   B 1 120 ? 34.463 -11.807 -12.812 1.00 29.27 ?  120 GLU   B HG2  1 
ATOM   5949 H  HG3  . GLU   B 1 120 ? 35.659 -10.860 -12.369 1.00 29.27 ?  120 GLU   B HG3  1 
ATOM   5950 N  N    . VAL   B 1 121 ? 38.254 -15.046 -12.302 1.00 12.13 ?  121 VAL   B N    1 
ATOM   5951 C  CA   . VAL   B 1 121 ? 39.004 -16.251 -12.652 1.00 12.06 ?  121 VAL   B CA   1 
ATOM   5952 C  C    . VAL   B 1 121 ? 40.119 -16.459 -11.633 1.00 11.68 ?  121 VAL   B C    1 
ATOM   5953 O  O    . VAL   B 1 121 ? 40.791 -15.504 -11.231 1.00 12.57 ?  121 VAL   B O    1 
ATOM   5954 C  CB   . VAL   B 1 121 ? 39.510 -16.202 -14.112 1.00 13.94 ?  121 VAL   B CB   1 
ATOM   5955 C  CG1  . VAL   B 1 121 ? 40.373 -14.968 -14.375 1.00 15.23 ?  121 VAL   B CG1  1 
ATOM   5956 C  CG2  . VAL   B 1 121 ? 40.243 -17.479 -14.473 1.00 15.36 ?  121 VAL   B CG2  1 
ATOM   5957 H  H    . VAL   B 1 121 ? 38.736 -14.443 -11.914 1.00 14.59 ?  121 VAL   B H    1 
ATOM   5958 H  HA   . VAL   B 1 121 ? 38.397 -17.004 -12.586 1.00 14.51 ?  121 VAL   B HA   1 
ATOM   5959 H  HB   . VAL   B 1 121 ? 38.737 -16.139 -14.701 1.00 16.76 ?  121 VAL   B HB   1 
ATOM   5960 H  HG11 . VAL   B 1 121 ? 40.676 -14.983 -15.296 1.00 18.31 ?  121 VAL   B HG11 1 
ATOM   5961 H  HG12 . VAL   B 1 121 ? 39.842 -14.170 -14.216 1.00 18.31 ?  121 VAL   B HG12 1 
ATOM   5962 H  HG13 . VAL   B 1 121 ? 41.134 -14.982 -13.775 1.00 18.31 ?  121 VAL   B HG13 1 
ATOM   5963 H  HG21 . VAL   B 1 121 ? 40.440 -17.469 -15.425 1.00 18.46 ?  121 VAL   B HG21 1 
ATOM   5964 H  HG22 . VAL   B 1 121 ? 41.070 -17.522 -13.968 1.00 18.46 ?  121 VAL   B HG22 1 
ATOM   5965 H  HG23 . VAL   B 1 121 ? 39.681 -18.237 -14.260 1.00 18.46 ?  121 VAL   B HG23 1 
ATOM   5966 N  N    . LEU   B 1 122 ? 40.302 -17.713 -11.206 1.00 11.27 ?  122 LEU   B N    1 
ATOM   5967 C  CA   . LEU   B 1 122 ? 41.283 -18.066 -10.181 1.00 11.00 ?  122 LEU   B CA   1 
ATOM   5968 C  C    . LEU   B 1 122 ? 41.944 -19.395 -10.509 1.00 10.95 ?  122 LEU   B C    1 
ATOM   5969 O  O    . LEU   B 1 122 ? 41.284 -20.317 -11.009 1.00 12.22 ?  122 LEU   B O    1 
ATOM   5970 C  CB   . LEU   B 1 122 ? 40.627 -18.302 -8.805  1.00 12.95 ?  122 LEU   B CB   1 
ATOM   5971 C  CG   . LEU   B 1 122 ? 39.597 -17.280 -8.311  1.00 12.88 ?  122 LEU   B CG   1 
ATOM   5972 C  CD1  . LEU   B 1 122 ? 38.189 -17.638 -8.773  1.00 13.92 ?  122 LEU   B CD1  1 
ATOM   5973 C  CD2  . LEU   B 1 122 ? 39.662 -17.176 -6.804  1.00 12.36 ?  122 LEU   B CD2  1 
ATOM   5974 H  H    . LEU   B 1 122 ? 39.864 -18.391 -11.503 1.00 13.55 ?  122 LEU   B H    1 
ATOM   5975 H  HA   . LEU   B 1 122 ? 41.957 -17.367 -10.098 1.00 13.24 ?  122 LEU   B HA   1 
ATOM   5976 H  HB2  . LEU   B 1 122 ? 40.177 -19.156 -8.834  1.00 15.58 ?  122 LEU   B HB2  1 
ATOM   5977 H  HB3  . LEU   B 1 122 ? 41.330 -18.331 -8.139  1.00 15.58 ?  122 LEU   B HB3  1 
ATOM   5978 H  HG   . LEU   B 1 122 ? 39.816 -16.407 -8.675  1.00 15.49 ?  122 LEU   B HG   1 
ATOM   5979 H  HD11 . LEU   B 1 122 ? 37.566 -16.983 -8.421  1.00 16.74 ?  122 LEU   B HD11 1 
ATOM   5980 H  HD12 . LEU   B 1 122 ? 38.165 -17.629 -9.742  1.00 16.74 ?  122 LEU   B HD12 1 
ATOM   5981 H  HD13 . LEU   B 1 122 ? 37.964 -18.521 -8.443  1.00 16.74 ?  122 LEU   B HD13 1 
ATOM   5982 H  HD21 . LEU   B 1 122 ? 38.981 -16.561 -6.495  1.00 14.86 ?  122 LEU   B HD21 1 
ATOM   5983 H  HD22 . LEU   B 1 122 ? 39.517 -18.055 -6.418  1.00 14.86 ?  122 LEU   B HD22 1 
ATOM   5984 H  HD23 . LEU   B 1 122 ? 40.543 -16.848 -6.547  1.00 14.86 ?  122 LEU   B HD23 1 
ATOM   5985 N  N    . LEU   B 1 123 ? 43.235 -19.499 -10.160 1.00 10.73 ?  123 LEU   B N    1 
ATOM   5986 C  CA   . LEU   B 1 123 ? 43.944 -20.772 -10.038 1.00 10.87 ?  123 LEU   B CA   1 
ATOM   5987 C  C    . LEU   B 1 123 ? 43.918 -21.170 -8.567  1.00 10.76 ?  123 LEU   B C    1 
ATOM   5988 O  O    . LEU   B 1 123 ? 44.267 -20.343 -7.714  1.00 11.20 ?  123 LEU   B O    1 
ATOM   5989 C  CB   . LEU   B 1 123 ? 45.393 -20.597 -10.506 1.00 11.26 ?  123 LEU   B CB   1 
ATOM   5990 C  CG   . LEU   B 1 123 ? 46.337 -21.775 -10.261 1.00 11.73 ?  123 LEU   B CG   1 
ATOM   5991 C  CD1  . LEU   B 1 123 ? 45.913 -23.019 -11.036 1.00 12.19 ?  123 LEU   B CD1  1 
ATOM   5992 C  CD2  . LEU   B 1 123 ? 47.757 -21.372 -10.623 1.00 12.75 ?  123 LEU   B CD2  1 
ATOM   5993 H  H    . LEU   B 1 123 ? 43.734 -18.816 -9.970  1.00 12.91 ?  123 LEU   B H    1 
ATOM   5994 H  HA   . LEU   B 1 123 ? 43.500 -21.454 -10.566 1.00 13.08 ?  123 LEU   B HA   1 
ATOM   5995 H  HB2  . LEU   B 1 123 ? 45.378 -20.432 -11.462 1.00 13.54 ?  123 LEU   B HB2  1 
ATOM   5996 H  HB3  . LEU   B 1 123 ? 45.765 -19.830 -10.051 1.00 13.54 ?  123 LEU   B HB3  1 
ATOM   5997 H  HG   . LEU   B 1 123 ? 46.326 -22.002 -9.318  1.00 14.11 ?  123 LEU   B HG   1 
ATOM   5998 H  HD11 . LEU   B 1 123 ? 46.545 -23.731 -10.861 1.00 14.66 ?  123 LEU   B HD11 1 
ATOM   5999 H  HD12 . LEU   B 1 123 ? 45.025 -23.286 -10.742 1.00 14.66 ?  123 LEU   B HD12 1 
ATOM   6000 H  HD13 . LEU   B 1 123 ? 45.897 -22.811 -11.982 1.00 14.66 ?  123 LEU   B HD13 1 
ATOM   6001 H  HD21 . LEU   B 1 123 ? 48.349 -22.124 -10.469 1.00 15.33 ?  123 LEU   B HD21 1 
ATOM   6002 H  HD22 . LEU   B 1 123 ? 47.784 -21.117 -11.559 1.00 15.33 ?  123 LEU   B HD22 1 
ATOM   6003 H  HD23 . LEU   B 1 123 ? 48.021 -20.622 -10.068 1.00 15.33 ?  123 LEU   B HD23 1 
ATOM   6004 N  N    . ALA   B 1 124 ? 43.490 -22.400 -8.255  1.00 10.72 ?  124 ALA   B N    1 
ATOM   6005 C  CA   . ALA   B 1 124 ? 43.230 -22.721 -6.859  1.00 10.91 ?  124 ALA   B CA   1 
ATOM   6006 C  C    . ALA   B 1 124 ? 43.507 -24.182 -6.541  1.00 10.81 ?  124 ALA   B C    1 
ATOM   6007 O  O    . ALA   B 1 124 ? 43.374 -25.058 -7.410  1.00 11.26 ?  124 ALA   B O    1 
ATOM   6008 C  CB   . ALA   B 1 124 ? 41.776 -22.409 -6.486  1.00 11.51 ?  124 ALA   B CB   1 
ATOM   6009 H  H    . ALA   B 1 124 ? 43.334 -23.039 -8.819  1.00 12.90 ?  124 ALA   B H    1 
ATOM   6010 H  HA   . ALA   B 1 124 ? 43.806 -22.174 -6.315  1.00 13.12 ?  124 ALA   B HA   1 
ATOM   6011 H  HB1  . ALA   B 1 124 ? 41.628 -22.631 -5.555  1.00 13.85 ?  124 ALA   B HB1  1 
ATOM   6012 H  HB2  . ALA   B 1 124 ? 41.612 -21.460 -6.628  1.00 13.85 ?  124 ALA   B HB2  1 
ATOM   6013 H  HB3  . ALA   B 1 124 ? 41.180 -22.929 -7.049  1.00 13.85 ?  124 ALA   B HB3  1 
ATOM   6014 N  N    . PRO   B 1 125 ? 43.796 -24.482 -5.275  1.00 10.71 ?  125 PRO   B N    1 
ATOM   6015 C  CA   . PRO   B 1 125 ? 43.735 -25.849 -4.759  1.00 11.68 ?  125 PRO   B CA   1 
ATOM   6016 C  C    . PRO   B 1 125 ? 42.337 -26.125 -4.208  1.00 11.69 ?  125 PRO   B C    1 
ATOM   6017 O  O    . PRO   B 1 125 ? 41.538 -25.209 -4.000  1.00 12.23 ?  125 PRO   B O    1 
ATOM   6018 C  CB   . PRO   B 1 125 ? 44.731 -25.783 -3.593  1.00 12.71 ?  125 PRO   B CB   1 
ATOM   6019 C  CG   . PRO   B 1 125 ? 44.490 -24.394 -3.015  1.00 12.65 ?  125 PRO   B CG   1 
ATOM   6020 C  CD   . PRO   B 1 125 ? 44.130 -23.519 -4.211  1.00 11.47 ?  125 PRO   B CD   1 
ATOM   6021 H  HA   . PRO   B 1 125 ? 44.008 -26.513 -5.413  1.00 14.05 ?  125 PRO   B HA   1 
ATOM   6022 H  HB2  . PRO   B 1 125 ? 44.526 -26.471 -2.936  1.00 15.29 ?  125 PRO   B HB2  1 
ATOM   6023 H  HB3  . PRO   B 1 125 ? 45.639 -25.873 -3.918  1.00 15.29 ?  125 PRO   B HB3  1 
ATOM   6024 H  HG2  . PRO   B 1 125 ? 43.755 -24.417 -2.380  1.00 15.21 ?  125 PRO   B HG2  1 
ATOM   6025 H  HG3  . PRO   B 1 125 ? 45.300 -24.068 -2.581  1.00 15.21 ?  125 PRO   B HG3  1 
ATOM   6026 H  HD2  . PRO   B 1 125 ? 43.369 -22.954 -4.009  1.00 13.80 ?  125 PRO   B HD2  1 
ATOM   6027 H  HD3  . PRO   B 1 125 ? 44.903 -22.977 -4.476  1.00 13.80 ?  125 PRO   B HD3  1 
ATOM   6028 N  N    . LEU   B 1 126 ? 42.068 -27.407 -3.930  1.00 12.11 ?  126 LEU   B N    1 
ATOM   6029 C  CA   . LEU   B 1 126 ? 40.841 -27.770 -3.228  1.00 12.71 ?  126 LEU   B CA   1 
ATOM   6030 C  C    . LEU   B 1 126 ? 40.955 -27.373 -1.764  1.00 12.77 ?  126 LEU   B C    1 
ATOM   6031 O  O    . LEU   B 1 126 ? 41.850 -27.833 -1.049  1.00 14.25 ?  126 LEU   B O    1 
ATOM   6032 C  CB   . LEU   B 1 126 ? 40.590 -29.266 -3.344  1.00 14.10 ?  126 LEU   B CB   1 
ATOM   6033 C  CG   . LEU   B 1 126 ? 40.062 -29.757 -4.692  1.00 14.83 ?  126 LEU   B CG   1 
ATOM   6034 C  CD1  . LEU   B 1 126 ? 40.108 -31.271 -4.761  1.00 16.48 ?  126 LEU   B CD1  1 
ATOM   6035 C  CD2  . LEU   B 1 126 ? 38.645 -29.255 -4.945  1.00 15.13 ?  126 LEU   B CD2  1 
ATOM   6036 H  H    . LEU   B 1 126 ? 42.577 -28.072 -4.127  1.00 14.57 ?  126 LEU   B H    1 
ATOM   6037 H  HA   . LEU   B 1 126 ? 40.094 -27.292 -3.622  1.00 15.29 ?  126 LEU   B HA   1 
ATOM   6038 H  HB2  . LEU   B 1 126 ? 41.424 -29.726 -3.175  1.00 16.95 ?  126 LEU   B HB2  1 
ATOM   6039 H  HB3  . LEU   B 1 126 ? 39.938 -29.514 -2.672  1.00 16.95 ?  126 LEU   B HB3  1 
ATOM   6040 H  HG   . LEU   B 1 126 ? 40.631 -29.409 -5.399  1.00 17.83 ?  126 LEU   B HG   1 
ATOM   6041 H  HD11 . LEU   B 1 126 ? 39.767 -31.562 -5.622  1.00 19.81 ?  126 LEU   B HD11 1 
ATOM   6042 H  HD12 . LEU   B 1 126 ? 41.024 -31.568 -4.650  1.00 19.81 ?  126 LEU   B HD12 1 
ATOM   6043 H  HD13 . LEU   B 1 126 ? 39.554 -31.637 -4.049  1.00 19.81 ?  126 LEU   B HD13 1 
ATOM   6044 H  HD21 . LEU   B 1 126 ? 38.299 -29.671 -5.749  1.00 18.19 ?  126 LEU   B HD21 1 
ATOM   6045 H  HD22 . LEU   B 1 126 ? 38.089 -29.482 -4.186  1.00 18.19 ?  126 LEU   B HD22 1 
ATOM   6046 H  HD23 . LEU   B 1 126 ? 38.666 -28.288 -5.059  1.00 18.19 ?  126 LEU   B HD23 1 
ATOM   6047 N  N    . LEU   B 1 127 ? 40.028 -26.541 -1.305  1.00 12.42 ?  127 LEU   B N    1 
ATOM   6048 C  CA   . LEU   B 1 127 ? 40.082 -26.051 0.063   1.00 12.75 ?  127 LEU   B CA   1 
ATOM   6049 C  C    . LEU   B 1 127 ? 39.818 -27.174 1.057   1.00 12.66 ?  127 LEU   B C    1 
ATOM   6050 O  O    . LEU   B 1 127 ? 38.994 -28.066 0.832   1.00 12.95 ?  127 LEU   B O    1 
ATOM   6051 C  CB   . LEU   B 1 127 ? 39.067 -24.925 0.275   1.00 13.42 ?  127 LEU   B CB   1 
ATOM   6052 C  CG   . LEU   B 1 127 ? 39.245 -23.657 -0.559  1.00 14.16 ?  127 LEU   B CG   1 
ATOM   6053 C  CD1  . LEU   B 1 127 ? 38.122 -22.689 -0.222  1.00 14.12 ?  127 LEU   B CD1  1 
ATOM   6054 C  CD2  . LEU   B 1 127 ? 40.614 -23.022 -0.329  1.00 14.82 ?  127 LEU   B CD2  1 
ATOM   6055 H  H    . LEU   B 1 127 ? 39.359 -26.238 -1.763  1.00 14.94 ?  127 LEU   B H    1 
ATOM   6056 H  HA   . LEU   B 1 127 ? 40.967 -25.692 0.235   1.00 15.33 ?  127 LEU   B HA   1 
ATOM   6057 H  HB2  . LEU   B 1 127 ? 38.182 -25.273 0.077   1.00 16.13 ?  127 LEU   B HB2  1 
ATOM   6058 H  HB3  . LEU   B 1 127 ? 39.100 -24.658 1.208   1.00 16.13 ?  127 LEU   B HB3  1 
ATOM   6059 H  HG   . LEU   B 1 127 ? 39.165 -23.877 -1.498  1.00 17.03 ?  127 LEU   B HG   1 
ATOM   6060 H  HD11 . LEU   B 1 127 ? 38.235 -21.875 -0.745  1.00 16.98 ?  127 LEU   B HD11 1 
ATOM   6061 H  HD12 . LEU   B 1 127 ? 37.270 -23.098 -0.432  1.00 16.98 ?  127 LEU   B HD12 1 
ATOM   6062 H  HD13 . LEU   B 1 127 ? 38.161 -22.472 0.725   1.00 16.98 ?  127 LEU   B HD13 1 
ATOM   6063 H  HD21 . LEU   B 1 127 ? 40.651 -22.169 -0.790  1.00 17.82 ?  127 LEU   B HD21 1 
ATOM   6064 H  HD22 . LEU   B 1 127 ? 40.744 -22.888 0.624   1.00 17.82 ?  127 LEU   B HD22 1 
ATOM   6065 H  HD23 . LEU   B 1 127 ? 41.297 -23.616 -0.676  1.00 17.82 ?  127 LEU   B HD23 1 
ATOM   6066 N  N    . SER   B 1 128 ? 40.503 -27.092 2.187   1.00 12.67 ?  128 SER   B N    1 
ATOM   6067 C  CA   . SER   B 1 128 ? 40.397 -28.011 3.311   1.00 13.08 ?  128 SER   B CA   1 
ATOM   6068 C  C    . SER   B 1 128 ? 40.891 -29.418 2.988   1.00 14.22 ?  128 SER   B C    1 
ATOM   6069 O  O    . SER   B 1 128 ? 40.806 -30.300 3.844   1.00 15.55 ?  128 SER   B O    1 
ATOM   6070 C  CB   . SER   B 1 128 ? 38.999 -28.016 3.949   1.00 13.45 ?  128 SER   B CB   1 
ATOM   6071 O  OG   . SER   B 1 128 ? 38.687 -26.740 4.500   1.00 14.21 ?  128 SER   B OG   1 
ATOM   6072 H  H    . SER   B 1 128 ? 41.069 -26.458 2.333   1.00 15.24 ?  128 SER   B H    1 
ATOM   6073 H  HA   . SER   B 1 128 ? 40.987 -27.671 3.993   1.00 15.73 ?  128 SER   B HA   1 
ATOM   6074 H  HB2  . SER   B 1 128 ? 38.336 -28.251 3.278   1.00 16.17 ?  128 SER   B HB2  1 
ATOM   6075 H  HB3  . SER   B 1 128 ? 38.983 -28.690 4.663   1.00 16.17 ?  128 SER   B HB3  1 
ATOM   6076 H  HG   . SER   B 1 128 ? 39.258 -26.545 5.086   1.00 17.09 ?  128 SER   B HG   1 
ATOM   6077 N  N    . ALA   B 1 129 ? 41.462 -29.635 1.801   1.00 15.05 ?  129 ALA   B N    1 
ATOM   6078 C  CA   . ALA   B 1 129 ? 42.005 -30.933 1.437   1.00 16.07 ?  129 ALA   B CA   1 
ATOM   6079 C  C    . ALA   B 1 129 ? 43.394 -31.118 2.036   1.00 15.05 ?  129 ALA   B C    1 
ATOM   6080 O  O    . ALA   B 1 129 ? 43.959 -30.225 2.681   1.00 14.97 ?  129 ALA   B O    1 
ATOM   6081 C  CB   . ALA   B 1 129 ? 42.054 -31.084 -0.082  1.00 18.00 ?  129 ALA   B CB   1 
ATOM   6082 H  H    . ALA   B 1 129 ? 41.540 -29.039 1.181   1.00 18.10 ?  129 ALA   B H    1 
ATOM   6083 H  HA   . ALA   B 1 129 ? 41.428 -31.625 1.786   1.00 19.31 ?  129 ALA   B HA   1 
ATOM   6084 H  HB1  . ALA   B 1 129 ? 42.413 -31.960 -0.299  1.00 21.64 ?  129 ALA   B HB1  1 
ATOM   6085 H  HB2  . ALA   B 1 129 ? 41.156 -30.998 -0.437  1.00 21.64 ?  129 ALA   B HB2  1 
ATOM   6086 H  HB3  . ALA   B 1 129 ? 42.625 -30.393 -0.451  1.00 21.64 ?  129 ALA   B HB3  1 
ATOM   6087 N  N    . GLY   B 1 130 ? 43.948 -32.306 1.814   1.00 15.30 ?  130 GLY   B N    1 
ATOM   6088 C  CA   . GLY   B 1 130 ? 45.333 -32.548 2.162   1.00 16.01 ?  130 GLY   B CA   1 
ATOM   6089 C  C    . GLY   B 1 130 ? 45.554 -32.449 3.652   1.00 15.85 ?  130 GLY   B C    1 
ATOM   6090 O  O    . GLY   B 1 130 ? 44.863 -33.093 4.455   1.00 16.76 ?  130 GLY   B O    1 
ATOM   6091 H  H    . GLY   B 1 130 ? 43.548 -32.980 1.460   1.00 18.39 ?  130 GLY   B H    1 
ATOM   6092 H  HA2  . GLY   B 1 130 ? 45.595 -33.438 1.867   1.00 19.25 ?  130 GLY   B HA2  1 
ATOM   6093 H  HA3  . GLY   B 1 130 ? 45.903 -31.900 1.719   1.00 19.25 ?  130 GLY   B HA3  1 
ATOM   6094 N  N    . ILE   B 1 131 ? 46.531 -31.620 4.033   1.00 16.12 ?  131 ILE   B N    1 
ATOM   6095 C  CA   . ILE   B 1 131 ? 46.892 -31.487 5.437   1.00 16.94 ?  131 ILE   B CA   1 
ATOM   6096 C  C    . ILE   B 1 131 ? 45.778 -30.887 6.274   1.00 16.28 ?  131 ILE   B C    1 
ATOM   6097 O  O    . ILE   B 1 131 ? 45.852 -30.962 7.504   1.00 17.61 ?  131 ILE   B O    1 
ATOM   6098 C  CB   . ILE   B 1 131 ? 48.215 -30.712 5.631   1.00 18.83 ?  131 ILE   B CB   1 
ATOM   6099 C  CG1  . ILE   B 1 131 ? 48.054 -29.235 5.238   1.00 19.47 ?  131 ILE   B CG1  1 
ATOM   6100 C  CG2  . ILE   B 1 131 ? 49.337 -31.366 4.830   1.00 19.93 ?  131 ILE   B CG2  1 
ATOM   6101 C  CD1  . ILE   B 1 131 ? 49.261 -28.371 5.577   1.00 20.43 ?  131 ILE   B CD1  1 
ATOM   6102 H  H    . ILE   B 1 131 ? 46.995 -31.131 3.498   1.00 19.37 ?  131 ILE   B H    1 
ATOM   6103 H  HA   . ILE   B 1 131 ? 47.037 -32.377 5.786   1.00 20.37 ?  131 ILE   B HA   1 
ATOM   6104 H  HB   . ILE   B 1 131 ? 48.446 -30.749 6.573   1.00 22.63 ?  131 ILE   B HB   1 
ATOM   6105 H  HG12 . ILE   B 1 131 ? 47.907 -29.186 4.280   1.00 23.40 ?  131 ILE   B HG12 1 
ATOM   6106 H  HG13 . ILE   B 1 131 ? 47.285 -28.861 5.702   1.00 23.40 ?  131 ILE   B HG13 1 
ATOM   6107 H  HG21 . ILE   B 1 131 ? 50.176 -30.954 5.079   1.00 23.94 ?  131 ILE   B HG21 1 
ATOM   6108 H  HG22 . ILE   B 1 131 ? 49.352 -32.311 5.032   1.00 23.94 ?  131 ILE   B HG22 1 
ATOM   6109 H  HG23 . ILE   B 1 131 ? 49.163 -31.228 3.885   1.00 23.94 ?  131 ILE   B HG23 1 
ATOM   6110 H  HD11 . ILE   B 1 131 ? 49.045 -27.446 5.382   1.00 24.55 ?  131 ILE   B HD11 1 
ATOM   6111 H  HD12 . ILE   B 1 131 ? 49.460 -28.472 6.521   1.00 24.55 ?  131 ILE   B HD12 1 
ATOM   6112 H  HD13 . ILE   B 1 131 ? 50.012 -28.659 5.043   1.00 24.55 ?  131 ILE   B HD13 1 
ATOM   6113 N  N    . PHE   B 1 132 ? 44.750 -30.302 5.646   1.00 15.17 ?  132 PHE   B N    1 
ATOM   6114 C  CA   . PHE   B 1 132 ? 43.590 -29.801 6.377   1.00 15.36 ?  132 PHE   B CA   1 
ATOM   6115 C  C    . PHE   B 1 132 ? 42.566 -30.891 6.700   1.00 16.59 ?  132 PHE   B C    1 
ATOM   6116 O  O    . PHE   B 1 132 ? 41.659 -30.643 7.500   1.00 18.24 ?  132 PHE   B O    1 
ATOM   6117 C  CB   . PHE   B 1 132 ? 42.914 -28.661 5.602   1.00 14.60 ?  132 PHE   B CB   1 
ATOM   6118 C  CG   . PHE   B 1 132 ? 43.615 -27.321 5.719   1.00 14.66 ?  132 PHE   B CG   1 
ATOM   6119 C  CD1  . PHE   B 1 132 ? 44.915 -27.140 5.263   1.00 15.71 ?  132 PHE   B CD1  1 
ATOM   6120 C  CD2  . PHE   B 1 132 ? 42.938 -26.225 6.234   1.00 14.11 ?  132 PHE   B CD2  1 
ATOM   6121 C  CE1  . PHE   B 1 132 ? 45.536 -25.898 5.358   1.00 16.02 ?  132 PHE   B CE1  1 
ATOM   6122 C  CE2  . PHE   B 1 132 ? 43.549 -24.982 6.329   1.00 14.34 ?  132 PHE   B CE2  1 
ATOM   6123 C  CZ   . PHE   B 1 132 ? 44.848 -24.820 5.887   1.00 15.39 ?  132 PHE   B CZ   1 
ATOM   6124 H  H    . PHE   B 1 132 ? 44.702 -30.185 4.790   1.00 18.24 ?  132 PHE   B H    1 
ATOM   6125 H  HA   . PHE   B 1 132 ? 43.900 -29.430 7.215   1.00 18.46 ?  132 PHE   B HA   1 
ATOM   6126 H  HB2  . PHE   B 1 132 ? 42.893 -28.895 4.663   1.00 17.56 ?  132 PHE   B HB2  1 
ATOM   6127 H  HB3  . PHE   B 1 132 ? 42.009 -28.551 5.935   1.00 17.56 ?  132 PHE   B HB3  1 
ATOM   6128 H  HD1  . PHE   B 1 132 ? 45.382 -27.864 4.912   1.00 18.89 ?  132 PHE   B HD1  1 
ATOM   6129 H  HD2  . PHE   B 1 132 ? 42.059 -26.327 6.530   1.00 16.96 ?  132 PHE   B HD2  1 
ATOM   6130 H  HE1  . PHE   B 1 132 ? 46.413 -25.795 5.064   1.00 19.26 ?  132 PHE   B HE1  1 
ATOM   6131 H  HE2  . PHE   B 1 132 ? 43.082 -24.256 6.685   1.00 17.25 ?  132 PHE   B HE2  1 
ATOM   6132 H  HZ   . PHE   B 1 132 ? 45.264 -23.987 5.954   1.00 18.51 ?  132 PHE   B HZ   1 
ATOM   6133 N  N    . GLY   B 1 133 ? 42.669 -32.083 6.099   1.00 16.07 ?  133 GLY   B N    1 
ATOM   6134 C  CA   . GLY   B 1 133 ? 41.954 -33.248 6.593   1.00 16.74 ?  133 GLY   B CA   1 
ATOM   6135 C  C    . GLY   B 1 133 ? 40.557 -33.511 6.057   1.00 17.19 ?  133 GLY   B C    1 
ATOM   6136 O  O    . GLY   B 1 133 ? 39.967 -34.532 6.429   1.00 19.41 ?  133 GLY   B O    1 
ATOM   6137 H  H    . GLY   B 1 133 ? 43.151 -32.227 5.402   1.00 19.32 ?  133 GLY   B H    1 
ATOM   6138 H  HA2  . GLY   B 1 133 ? 42.489 -34.028 6.398   1.00 20.12 ?  133 GLY   B HA2  1 
ATOM   6139 H  HA3  . GLY   B 1 133 ? 41.884 -33.168 7.556   1.00 20.12 ?  133 GLY   B HA3  1 
ATOM   6140 N  N    . ALA   B 1 134 ? 39.996 -32.647 5.218   1.00 16.42 ?  134 ALA   B N    1 
ATOM   6141 C  CA   . ALA   B 1 134 ? 38.669 -32.922 4.685   1.00 16.69 ?  134 ALA   B CA   1 
ATOM   6142 C  C    . ALA   B 1 134 ? 38.752 -33.919 3.530   1.00 16.77 ?  134 ALA   B C    1 
ATOM   6143 O  O    . ALA   B 1 134 ? 39.804 -34.111 2.916   1.00 17.77 ?  134 ALA   B O    1 
ATOM   6144 C  CB   . ALA   B 1 134 ? 37.994 -31.631 4.220   1.00 17.08 ?  134 ALA   B CB   1 
ATOM   6145 H  H    . ALA   B 1 134 ? 40.351 -31.906 4.948   1.00 19.73 ?  134 ALA   B H    1 
ATOM   6146 H  HA   . ALA   B 1 134 ? 38.122 -33.313 5.383   1.00 20.06 ?  134 ALA   B HA   1 
ATOM   6147 H  HB1  . ALA   B 1 134 ? 37.108 -31.844 3.884   1.00 20.53 ?  134 ALA   B HB1  1 
ATOM   6148 H  HB2  . ALA   B 1 134 ? 37.925 -31.023 4.972   1.00 20.53 ?  134 ALA   B HB2  1 
ATOM   6149 H  HB3  . ALA   B 1 134 ? 38.527 -31.231 3.517   1.00 20.53 ?  134 ALA   B HB3  1 
ATOM   6150 N  N    . ASP   B 1 135 ? 37.621 -34.546 3.239   1.00 16.83 ?  135 ASP   B N    1 
ATOM   6151 C  CA   . ASP   B 1 135 ? 37.520 -35.442 2.093   1.00 17.53 ?  135 ASP   B CA   1 
ATOM   6152 C  C    . ASP   B 1 135 ? 37.617 -34.607 0.822   1.00 16.57 ?  135 ASP   B C    1 
ATOM   6153 O  O    . ASP   B 1 135 ? 36.767 -33.733 0.604   1.00 16.67 ?  135 ASP   B O    1 
ATOM   6154 C  CB   . ASP   B 1 135 ? 36.174 -36.165 2.154   1.00 19.08 ?  135 ASP   B CB   1 
ATOM   6155 C  CG   . ASP   B 1 135 ? 35.979 -37.161 1.025   1.00 20.97 ?  135 ASP   B CG   1 
ATOM   6156 O  OD1  . ASP   B 1 135 ? 36.841 -37.234 0.125   1.00 21.03 ?  135 ASP   B OD1  1 
ATOM   6157 O  OD2  . ASP   B 1 135 ? 34.962 -37.893 1.053   1.00 23.91 -1 135 ASP   B OD2  1 
ATOM   6158 H  H    . ASP   B 1 135 ? 36.893 -34.467 3.687   1.00 20.23 ?  135 ASP   B H    1 
ATOM   6159 H  HA   . ASP   B 1 135 ? 38.236 -36.096 2.121   1.00 21.07 ?  135 ASP   B HA   1 
ATOM   6160 H  HB2  . ASP   B 1 135 ? 36.122 -36.651 2.988   1.00 22.93 ?  135 ASP   B HB2  1 
ATOM   6161 H  HB3  . ASP   B 1 135 ? 35.467 -35.505 2.104   1.00 22.93 ?  135 ASP   B HB3  1 
ATOM   6162 N  N    . PRO   B 1 136 ? 38.624 -34.814 -0.029  1.00 16.68 ?  136 PRO   B N    1 
ATOM   6163 C  CA   . PRO   B 1 136 ? 38.720 -33.987 -1.244  1.00 15.98 ?  136 PRO   B CA   1 
ATOM   6164 C  C    . PRO   B 1 136 ? 37.532 -34.143 -2.171  1.00 15.60 ?  136 PRO   B C    1 
ATOM   6165 O  O    . PRO   B 1 136 ? 37.208 -33.196 -2.899  1.00 14.60 ?  136 PRO   B O    1 
ATOM   6166 C  CB   . PRO   B 1 136 ? 40.033 -34.454 -1.890  1.00 17.16 ?  136 PRO   B CB   1 
ATOM   6167 C  CG   . PRO   B 1 136 ? 40.240 -35.839 -1.355  1.00 18.03 ?  136 PRO   B CG   1 
ATOM   6168 C  CD   . PRO   B 1 136 ? 39.709 -35.805 0.047   1.00 17.67 ?  136 PRO   B CD   1 
ATOM   6169 H  HA   . PRO   B 1 136 ? 38.804 -33.050 -1.006  1.00 19.21 ?  136 PRO   B HA   1 
ATOM   6170 H  HB2  . PRO   B 1 136 ? 39.939 -34.466 -2.858  1.00 20.62 ?  136 PRO   B HB2  1 
ATOM   6171 H  HB3  . PRO   B 1 136 ? 40.756 -33.864 -1.625  1.00 20.62 ?  136 PRO   B HB3  1 
ATOM   6172 H  HG2  . PRO   B 1 136 ? 39.746 -36.476 -1.892  1.00 21.67 ?  136 PRO   B HG2  1 
ATOM   6173 H  HG3  . PRO   B 1 136 ? 41.188 -36.051 -1.355  1.00 21.67 ?  136 PRO   B HG3  1 
ATOM   6174 H  HD2  . PRO   B 1 136 ? 39.356 -36.672 0.298   1.00 21.24 ?  136 PRO   B HD2  1 
ATOM   6175 H  HD3  . PRO   B 1 136 ? 40.394 -35.505 0.667   1.00 21.24 ?  136 PRO   B HD3  1 
ATOM   6176 N  N    . ILE   B 1 137 ? 36.873 -35.306 -2.171  1.00 15.62 ?  137 ILE   B N    1 
ATOM   6177 C  CA   . ILE   B 1 137 ? 35.655 -35.475 -2.957  1.00 16.21 ?  137 ILE   B CA   1 
ATOM   6178 C  C    . ILE   B 1 137 ? 34.584 -34.504 -2.479  1.00 15.95 ?  137 ILE   B C    1 
ATOM   6179 O  O    . ILE   B 1 137 ? 33.868 -33.890 -3.281  1.00 15.49 ?  137 ILE   B O    1 
ATOM   6180 C  CB   . ILE   B 1 137 ? 35.178 -36.941 -2.893  1.00 18.29 ?  137 ILE   B CB   1 
ATOM   6181 C  CG1  . ILE   B 1 137 ? 36.141 -37.844 -3.662  1.00 21.02 ?  137 ILE   B CG1  1 
ATOM   6182 C  CG2  . ILE   B 1 137 ? 33.768 -37.069 -3.456  1.00 18.88 ?  137 ILE   B CG2  1 
ATOM   6183 C  CD1  . ILE   B 1 137 ? 35.819 -39.324 -3.547  1.00 23.51 ?  137 ILE   B CD1  1 
ATOM   6184 H  H    . ILE   B 1 137 ? 37.110 -36.005 -1.734  1.00 18.78 ?  137 ILE   B H    1 
ATOM   6185 H  HA   . ILE   B 1 137 ? 35.843 -35.270 -3.888  1.00 19.48 ?  137 ILE   B HA   1 
ATOM   6186 H  HB   . ILE   B 1 137 ? 35.160 -37.221 -1.968  1.00 21.98 ?  137 ILE   B HB   1 
ATOM   6187 H  HG12 . ILE   B 1 137 ? 36.108 -37.610 -4.603  1.00 25.26 ?  137 ILE   B HG12 1 
ATOM   6188 H  HG13 . ILE   B 1 137 ? 37.034 -37.710 -3.318  1.00 25.26 ?  137 ILE   B HG13 1 
ATOM   6189 H  HG21 . ILE   B 1 137 ? 33.515 -38.005 -3.498  1.00 22.69 ?  137 ILE   B HG21 1 
ATOM   6190 H  HG22 . ILE   B 1 137 ? 33.144 -36.603 -2.879  1.00 22.69 ?  137 ILE   B HG22 1 
ATOM   6191 H  HG23 . ILE   B 1 137 ? 33.745 -36.685 -4.347  1.00 22.69 ?  137 ILE   B HG23 1 
ATOM   6192 H  HD11 . ILE   B 1 137 ? 36.480 -39.815 -4.050  1.00 28.24 ?  137 ILE   B HD11 1 
ATOM   6193 H  HD12 . ILE   B 1 137 ? 35.844 -39.583 -2.612  1.00 28.24 ?  137 ILE   B HD12 1 
ATOM   6194 H  HD13 . ILE   B 1 137 ? 34.938 -39.498 -3.915  1.00 28.24 ?  137 ILE   B HD13 1 
ATOM   6195 N  N    A HIS   B 1 138 ? 34.460 -34.352 -1.161  0.50 15.91 ?  138 HIS   B N    1 
ATOM   6196 N  N    B HIS   B 1 138 ? 34.451 -34.351 -1.163  0.50 15.93 ?  138 HIS   B N    1 
ATOM   6197 C  CA   A HIS   B 1 138 ? 33.514 -33.391 -0.607  0.50 16.11 ?  138 HIS   B CA   1 
ATOM   6198 C  CA   B HIS   B 1 138 ? 33.494 -33.381 -0.643  0.50 16.15 ?  138 HIS   B CA   1 
ATOM   6199 C  C    A HIS   B 1 138 ? 33.921 -31.959 -0.934  0.50 15.48 ?  138 HIS   B C    1 
ATOM   6200 C  C    B HIS   B 1 138 ? 33.920 -31.954 -0.966  0.50 15.39 ?  138 HIS   B C    1 
ATOM   6201 O  O    A HIS   B 1 138 ? 33.065 -31.119 -1.235  0.50 15.77 ?  138 HIS   B O    1 
ATOM   6202 O  O    B HIS   B 1 138 ? 33.079 -31.113 -1.300  0.50 15.42 ?  138 HIS   B O    1 
ATOM   6203 C  CB   A HIS   B 1 138 ? 33.424 -33.587 0.902   0.50 17.05 ?  138 HIS   B CB   1 
ATOM   6204 C  CB   B HIS   B 1 138 ? 33.316 -33.557 0.860   0.50 17.23 ?  138 HIS   B CB   1 
ATOM   6205 C  CG   A HIS   B 1 138 ? 32.555 -32.582 1.584   0.50 17.73 ?  138 HIS   B CG   1 
ATOM   6206 C  CG   B HIS   B 1 138 ? 32.343 -32.591 1.456   0.50 17.72 ?  138 HIS   B CG   1 
ATOM   6207 N  ND1  A HIS   B 1 138 ? 31.205 -32.473 1.334   0.50 18.82 ?  138 HIS   B ND1  1 
ATOM   6208 N  ND1  B HIS   B 1 138 ? 31.012 -32.562 1.100   0.50 18.52 ?  138 HIS   B ND1  1 
ATOM   6209 C  CD2  A HIS   B 1 138 ? 32.846 -31.630 2.501   0.50 17.69 ?  138 HIS   B CD2  1 
ATOM   6210 C  CD2  B HIS   B 1 138 ? 32.513 -31.599 2.362   0.50 17.93 ?  138 HIS   B CD2  1 
ATOM   6211 C  CE1  A HIS   B 1 138 ? 30.699 -31.501 2.070   0.50 18.44 ?  138 HIS   B CE1  1 
ATOM   6212 C  CE1  B HIS   B 1 138 ? 30.400 -31.603 1.771   0.50 18.27 ?  138 HIS   B CE1  1 
ATOM   6213 N  NE2  A HIS   B 1 138 ? 31.674 -30.974 2.790   0.50 18.09 ?  138 HIS   B NE2  1 
ATOM   6214 N  NE2  B HIS   B 1 138 ? 31.287 -31.004 2.545   0.50 18.00 ?  138 HIS   B NE2  1 
ATOM   6215 H  H    A HIS   B 1 138 ? 34.916 -34.786 -0.576  0.50 19.12 ?  138 HIS   B H    1 
ATOM   6216 H  H    B HIS   B 1 138 ? 34.897 -34.783 -0.568  0.50 19.15 ?  138 HIS   B H    1 
ATOM   6217 H  HA   A HIS   B 1 138 ? 32.638 -33.556 -0.989  0.50 19.37 ?  138 HIS   B HA   1 
ATOM   6218 H  HA   B HIS   B 1 138 ? 32.635 -33.541 -1.064  0.50 19.41 ?  138 HIS   B HA   1 
ATOM   6219 H  HB2  A HIS   B 1 138 ? 33.053 -34.469 1.080   0.50 20.50 ?  138 HIS   B HB2  1 
ATOM   6220 H  HB2  B HIS   B 1 138 ? 32.988 -34.456 1.035   0.50 20.71 ?  138 HIS   B HB2  1 
ATOM   6221 H  HB3  A HIS   B 1 138 ? 34.311 -33.522 1.282   0.50 20.50 ?  138 HIS   B HB3  1 
ATOM   6222 H  HB3  B HIS   B 1 138 ? 34.173 -33.430 1.296   0.50 20.71 ?  138 HIS   B HB3  1 
ATOM   6223 H  HD1  B HIS   B 1 138 ? 30.638 -33.089 0.534   0.50 22.26 ?  138 HIS   B HD1  1 
ATOM   6224 H  HD2  A HIS   B 1 138 ? 33.679 -31.458 2.870   0.50 21.27 ?  138 HIS   B HD2  1 
ATOM   6225 H  HD2  B HIS   B 1 138 ? 33.309 -31.370 2.788   0.50 21.55 ?  138 HIS   B HD2  1 
ATOM   6226 H  HE1  A HIS   B 1 138 ? 29.805 -31.240 2.084   0.50 22.16 ?  138 HIS   B HE1  1 
ATOM   6227 H  HE1  B HIS   B 1 138 ? 29.498 -31.387 1.712   0.50 21.95 ?  138 HIS   B HE1  1 
ATOM   6228 H  HE2  A HIS   B 1 138 ? 31.584 -30.329 3.348   0.50 21.74 ?  138 HIS   B HE2  1 
ATOM   6229 N  N    . SER   B 1 139 ? 35.217 -31.655 -0.876  1.00 14.97 ?  139 SER   B N    1 
ATOM   6230 C  CA   . SER   B 1 139 ? 35.660 -30.305 -1.192  1.00 14.28 ?  139 SER   B CA   1 
ATOM   6231 C  C    . SER   B 1 139 ? 35.315 -29.948 -2.628  1.00 13.30 ?  139 SER   B C    1 
ATOM   6232 O  O    . SER   B 1 139 ? 34.869 -28.830 -2.904  1.00 13.59 ?  139 SER   B O    1 
ATOM   6233 C  CB   . SER   B 1 139 ? 37.155 -30.172 -0.941  1.00 14.70 ?  139 SER   B CB   1 
ATOM   6234 O  OG   . SER   B 1 139 ? 37.559 -28.836 -1.182  1.00 14.52 ?  139 SER   B OG   1 
ATOM   6235 H  H    A SER   B 1 139 ? 35.843 -32.203 -0.668  0.50 17.99 ?  139 SER   B H    1 
ATOM   6236 H  H    B SER   B 1 139 ? 35.838 -32.200 -0.648  0.50 17.99 ?  139 SER   B H    1 
ATOM   6237 H  HA   . SER   B 1 139 ? 35.197 -29.679 -0.615  1.00 17.17 ?  139 SER   B HA   1 
ATOM   6238 H  HB2  . SER   B 1 139 ? 37.346 -30.407 -0.021  1.00 17.67 ?  139 SER   B HB2  1 
ATOM   6239 H  HB3  . SER   B 1 139 ? 37.636 -30.760 -1.545  1.00 17.67 ?  139 SER   B HB3  1 
ATOM   6240 H  HG   . SER   B 1 139 ? 38.385 -28.754 -1.037  1.00 17.46 ?  139 SER   B HG   1 
ATOM   6241 N  N    . LEU   B 1 140 ? 35.510 -30.887 -3.557  1.00 13.48 ?  140 LEU   B N    1 
ATOM   6242 C  CA   . LEU   B 1 140 ? 35.142 -30.643 -4.945  1.00 13.43 ?  140 LEU   B CA   1 
ATOM   6243 C  C    . LEU   B 1 140 ? 33.639 -30.411 -5.074  1.00 13.65 ?  140 LEU   B C    1 
ATOM   6244 O  O    . LEU   B 1 140 ? 33.202 -29.521 -5.808  1.00 13.75 ?  140 LEU   B O    1 
ATOM   6245 C  CB   . LEU   B 1 140 ? 35.611 -31.808 -5.822  1.00 13.36 ?  140 LEU   B CB   1 
ATOM   6246 C  CG   . LEU   B 1 140 ? 35.252 -31.700 -7.295  1.00 13.69 ?  140 LEU   B CG   1 
ATOM   6247 C  CD1  . LEU   B 1 140 ? 35.810 -30.411 -7.878  1.00 14.92 ?  140 LEU   B CD1  1 
ATOM   6248 C  CD2  . LEU   B 1 140 ? 35.733 -32.918 -8.059  1.00 14.87 ?  140 LEU   B CD2  1 
ATOM   6249 H  H    . LEU   B 1 140 ? 35.843 -31.663 -3.410  1.00 16.20 ?  140 LEU   B H    1 
ATOM   6250 H  HA   . LEU   B 1 140 ? 35.593 -29.840 -5.250  1.00 16.15 ?  140 LEU   B HA   1 
ATOM   6251 H  HB2  . LEU   B 1 140 ? 36.580 -31.867 -5.765  1.00 16.06 ?  140 LEU   B HB2  1 
ATOM   6252 H  HB3  . LEU   B 1 140 ? 35.217 -32.626 -5.490  1.00 16.06 ?  140 LEU   B HB3  1 
ATOM   6253 H  HG   . LEU   B 1 140 ? 34.287 -31.655 -7.374  1.00 16.46 ?  140 LEU   B HG   1 
ATOM   6254 H  HD11 . LEU   B 1 140 ? 35.718 -30.435 -8.840  1.00 17.93 ?  140 LEU   B HD11 1 
ATOM   6255 H  HD12 . LEU   B 1 140 ? 35.311 -29.654 -7.519  1.00 17.93 ?  140 LEU   B HD12 1 
ATOM   6256 H  HD13 . LEU   B 1 140 ? 36.745 -30.331 -7.634  1.00 17.93 ?  140 LEU   B HD13 1 
ATOM   6257 H  HD21 . LEU   B 1 140 ? 35.484 -32.811 -8.991  1.00 17.88 ?  140 LEU   B HD21 1 
ATOM   6258 H  HD22 . LEU   B 1 140 ? 36.692 -32.980 -7.974  1.00 17.88 ?  140 LEU   B HD22 1 
ATOM   6259 H  HD23 . LEU   B 1 140 ? 35.305 -33.700 -7.687  1.00 17.88 ?  140 LEU   B HD23 1 
ATOM   6260 N  N    . ARG   B 1 141 ? 32.836 -31.204 -4.358  1.00 13.76 ?  141 ARG   B N    1 
ATOM   6261 C  CA   . ARG   B 1 141 ? 31.383 -31.033 -4.340  1.00 14.85 ?  141 ARG   B CA   1 
ATOM   6262 C  C    . ARG   B 1 141 ? 31.000 -29.623 -3.905  1.00 14.20 ?  141 ARG   B C    1 
ATOM   6263 O  O    . ARG   B 1 141 ? 30.207 -28.938 -4.568  1.00 14.34 ?  141 ARG   B O    1 
ATOM   6264 C  CB   . ARG   B 1 141 ? 30.805 -32.067 -3.364  1.00 16.59 ?  141 ARG   B CB   1 
ATOM   6265 C  CG   . ARG   B 1 141 ? 29.338 -31.950 -3.032  1.00 18.96 ?  141 ARG   B CG   1 
ATOM   6266 C  CD   . ARG   B 1 141 ? 28.543 -32.580 -4.099  1.00 20.99 ?  141 ARG   B CD   1 
ATOM   6267 N  NE   . ARG   B 1 141 ? 28.265 -31.663 -5.192  1.00 21.41 ?  141 ARG   B NE   1 
ATOM   6268 C  CZ   . ARG   B 1 141 ? 28.244 -32.003 -6.474  1.00 20.74 ?  141 ARG   B CZ   1 
ATOM   6269 N  NH1  . ARG   B 1 141 ? 28.687 -33.181 -6.886  1.00 20.89 ?  141 ARG   B NH1  1 
ATOM   6270 N  NH2  . ARG   B 1 141 ? 27.769 -31.134 -7.364  1.00 21.53 ?  141 ARG   B NH2  1 
ATOM   6271 H  H    . ARG   B 1 141 ? 33.119 -31.854 -3.869  1.00 16.55 ?  141 ARG   B H    1 
ATOM   6272 H  HA   . ARG   B 1 141 ? 31.025 -31.200 -5.223  1.00 17.85 ?  141 ARG   B HA   1 
ATOM   6273 H  HB2  . ARG   B 1 141 ? 30.960 -32.952 -3.735  1.00 19.94 ?  141 ARG   B HB2  1 
ATOM   6274 H  HB3  . ARG   B 1 141 ? 31.291 -31.997 -2.528  1.00 19.94 ?  141 ARG   B HB3  1 
ATOM   6275 H  HG2  . ARG   B 1 141 ? 29.166 -32.408 -2.197  1.00 22.78 ?  141 ARG   B HG2  1 
ATOM   6276 H  HG3  . ARG   B 1 141 ? 29.087 -31.014 -2.959  1.00 22.78 ?  141 ARG   B HG3  1 
ATOM   6277 H  HD2  . ARG   B 1 141 ? 29.029 -33.347 -4.450  1.00 25.22 ?  141 ARG   B HD2  1 
ATOM   6278 H  HD3  . ARG   B 1 141 ? 27.704 -32.874 -3.727  1.00 25.22 ?  141 ARG   B HD3  1 
ATOM   6279 H  HE   . ARG   B 1 141 ? 28.081 -30.846 -4.990  1.00 25.72 ?  141 ARG   B HE   1 
ATOM   6280 H  HH11 . ARG   B 1 141 ? 28.987 -33.753 -6.323  1.00 25.10 ?  141 ARG   B HH11 1 
ATOM   6281 H  HH12 . ARG   B 1 141 ? 28.670 -33.369 -7.721  1.00 25.10 ?  141 ARG   B HH12 1 
ATOM   6282 H  HH21 . ARG   B 1 141 ? 27.483 -30.361 -7.107  1.00 25.87 ?  141 ARG   B HH21 1 
ATOM   6283 H  HH22 . ARG   B 1 141 ? 27.767 -31.332 -8.201  1.00 25.87 ?  141 ARG   B HH22 1 
ATOM   6284 N  N    . VAL   B 1 142 ? 31.548 -29.178 -2.777  1.00 13.85 ?  142 VAL   B N    1 
ATOM   6285 C  CA   . VAL   B 1 142 ? 31.222 -27.843 -2.289  1.00 13.91 ?  142 VAL   B CA   1 
ATOM   6286 C  C    . VAL   B 1 142 ? 31.693 -26.784 -3.278  1.00 13.90 ?  142 VAL   B C    1 
ATOM   6287 O  O    . VAL   B 1 142 ? 30.999 -25.791 -3.525  1.00 14.16 ?  142 VAL   B O    1 
ATOM   6288 C  CB   . VAL   B 1 142 ? 31.772 -27.616 -0.868  1.00 14.62 ?  142 VAL   B CB   1 
ATOM   6289 C  CG1  . VAL   B 1 142 ? 31.455 -26.192 -0.390  1.00 14.50 ?  142 VAL   B CG1  1 
ATOM   6290 C  CG2  . VAL   B 1 142 ? 31.198 -28.646 0.093   1.00 15.52 ?  142 VAL   B CG2  1 
ATOM   6291 H  H    . VAL   B 1 142 ? 32.105 -29.615 -2.291  1.00 16.65 ?  142 VAL   B H    1 
ATOM   6292 H  HA   . VAL   B 1 142 ? 30.262 -27.768 -2.234  1.00 16.72 ?  142 VAL   B HA   1 
ATOM   6293 H  HB   . VAL   B 1 142 ? 32.737 -27.723 -0.878  1.00 17.58 ?  142 VAL   B HB   1 
ATOM   6294 H  HG11 . VAL   B 1 142 ? 31.636 -26.133 0.559   1.00 17.43 ?  142 VAL   B HG11 1 
ATOM   6295 H  HG12 . VAL   B 1 142 ? 32.018 -25.565 -0.873  1.00 17.43 ?  142 VAL   B HG12 1 
ATOM   6296 H  HG13 . VAL   B 1 142 ? 30.521 -26.004 -0.564  1.00 17.43 ?  142 VAL   B HG13 1 
ATOM   6297 H  HG21 . VAL   B 1 142 ? 31.533 -28.464 0.983   1.00 18.66 ?  142 VAL   B HG21 1 
ATOM   6298 H  HG22 . VAL   B 1 142 ? 30.231 -28.578 0.079   1.00 18.66 ?  142 VAL   B HG22 1 
ATOM   6299 H  HG23 . VAL   B 1 142 ? 31.473 -29.530 -0.193  1.00 18.66 ?  142 VAL   B HG23 1 
ATOM   6300 N  N    . CYS   B 1 143 ? 32.872 -26.985 -3.869  1.00 13.08 ?  143 CYS   B N    1 
ATOM   6301 C  CA   . CYS   B 1 143 ? 33.367 -26.042 -4.866  1.00 13.22 ?  143 CYS   B CA   1 
ATOM   6302 C  C    . CYS   B 1 143 ? 32.364 -25.888 -6.004  1.00 13.31 ?  143 CYS   B C    1 
ATOM   6303 O  O    . CYS   B 1 143 ? 31.957 -24.775 -6.353  1.00 13.45 ?  143 CYS   B O    1 
ATOM   6304 C  CB   . CYS   B 1 143 ? 34.723 -26.522 -5.396  1.00 13.22 ?  143 CYS   B CB   1 
ATOM   6305 S  SG   . CYS   B 1 143 ? 35.477 -25.415 -6.606  1.00 13.56 ?  143 CYS   B SG   1 
ATOM   6306 H  H    . CYS   B 1 143 ? 33.400 -27.645 -3.707  1.00 15.73 ?  143 CYS   B H    1 
ATOM   6307 H  HA   . CYS   B 1 143 ? 33.495 -25.171 -4.454  1.00 15.90 ?  143 CYS   B HA   1 
ATOM   6308 H  HB2  . CYS   B 1 143 ? 35.342 -26.604 -4.653  1.00 15.89 ?  143 CYS   B HB2  1 
ATOM   6309 H  HB3  . CYS   B 1 143 ? 34.604 -27.381 -5.817  1.00 15.89 ?  143 CYS   B HB3  1 
ATOM   6310 H  HG   . CYS   B 1 143 ? 36.547 -25.852 -6.929  1.00 16.30 ?  143 CYS   B HG   1 
ATOM   6311 N  N    . VAL   B 1 144 ? 31.954 -27.008 -6.598  1.00 13.53 ?  144 VAL   B N    1 
ATOM   6312 C  CA   . VAL   B 1 144 ? 31.050 -26.941 -7.741  1.00 14.50 ?  144 VAL   B CA   1 
ATOM   6313 C  C    . VAL   B 1 144 ? 29.708 -26.335 -7.363  1.00 14.75 ?  144 VAL   B C    1 
ATOM   6314 O  O    . VAL   B 1 144 ? 29.091 -25.625 -8.170  1.00 16.02 ?  144 VAL   B O    1 
ATOM   6315 C  CB   . VAL   B 1 144 ? 30.901 -28.350 -8.328  1.00 17.35 ?  144 VAL   B CB   1 
ATOM   6316 C  CG1  . VAL   B 1 144 ? 29.631 -28.480 -9.163  1.00 19.94 ?  144 VAL   B CG1  1 
ATOM   6317 C  CG2  . VAL   B 1 144 ? 32.152 -28.735 -9.119  1.00 17.36 ?  144 VAL   B CG2  1 
ATOM   6318 H  H    . VAL   B 1 144 ? 32.193 -27.803 -6.369  1.00 16.26 ?  144 VAL   B H    1 
ATOM   6319 H  HA   . VAL   B 1 144 ? 31.444 -26.379 -8.422  1.00 17.44 ?  144 VAL   B HA   1 
ATOM   6320 H  HB   . VAL   B 1 144 ? 30.827 -28.982 -7.594  1.00 20.86 ?  144 VAL   B HB   1 
ATOM   6321 H  HG11 . VAL   B 1 144 ? 29.712 -29.265 -9.729  1.00 23.96 ?  144 VAL   B HG11 1 
ATOM   6322 H  HG12 . VAL   B 1 144 ? 28.873 -28.580 -8.570  1.00 23.96 ?  144 VAL   B HG12 1 
ATOM   6323 H  HG13 . VAL   B 1 144 ? 29.533 -27.689 -9.711  1.00 23.96 ?  144 VAL   B HG13 1 
ATOM   6324 H  HG21 . VAL   B 1 144 ? 32.039 -29.630 -9.476  1.00 20.87 ?  144 VAL   B HG21 1 
ATOM   6325 H  HG22 . VAL   B 1 144 ? 32.270 -28.103 -9.847  1.00 20.87 ?  144 VAL   B HG22 1 
ATOM   6326 H  HG23 . VAL   B 1 144 ? 32.921 -28.708 -8.530  1.00 20.87 ?  144 VAL   B HG23 1 
ATOM   6327 N  N    . ASP   B 1 145 ? 29.242 -26.579 -6.140  1.00 15.01 ?  145 ASP   B N    1 
ATOM   6328 C  CA   . ASP   B 1 145 ? 27.932 -26.111 -5.704  1.00 15.64 ?  145 ASP   B CA   1 
ATOM   6329 C  C    . ASP   B 1 145 ? 27.958 -24.687 -5.156  1.00 15.05 ?  145 ASP   B C    1 
ATOM   6330 O  O    . ASP   B 1 145 ? 26.896 -24.144 -4.833  1.00 17.03 ?  145 ASP   B O    1 
ATOM   6331 C  CB   . ASP   B 1 145 ? 27.353 -27.040 -4.628  1.00 17.44 ?  145 ASP   B CB   1 
ATOM   6332 C  CG   . ASP   B 1 145 ? 26.988 -28.416 -5.147  1.00 19.07 ?  145 ASP   B CG   1 
ATOM   6333 O  OD1  . ASP   B 1 145 ? 26.878 -28.599 -6.376  1.00 19.62 ?  145 ASP   B OD1  1 
ATOM   6334 O  OD2  . ASP   B 1 145 ? 26.798 -29.306 -4.296  1.00 21.36 -1 145 ASP   B OD2  1 
ATOM   6335 H  H    . ASP   B 1 145 ? 29.685 -26.993 -5.533  1.00 18.05 ?  145 ASP   B H    1 
ATOM   6336 H  HA   . ASP   B 1 145 ? 27.338 -26.102 -6.462  1.00 18.80 ?  145 ASP   B HA   1 
ATOM   6337 H  HB2  . ASP   B 1 145 ? 28.005 -27.160 -3.932  1.00 20.97 ?  145 ASP   B HB2  1 
ATOM   6338 H  HB3  . ASP   B 1 145 ? 26.546 -26.633 -4.274  1.00 20.97 ?  145 ASP   B HB3  1 
ATOM   6339 N  N    . THR   B 1 146 ? 29.137 -24.078 -5.035  1.00 13.40 ?  146 THR   B N    1 
ATOM   6340 C  CA   . THR   B 1 146 ? 29.278 -22.758 -4.426  1.00 13.09 ?  146 THR   B CA   1 
ATOM   6341 C  C    . THR   B 1 146 ? 29.909 -21.727 -5.345  1.00 12.91 ?  146 THR   B C    1 
ATOM   6342 O  O    . THR   B 1 146 ? 29.450 -20.570 -5.392  1.00 13.22 ?  146 THR   B O    1 
ATOM   6343 C  CB   . THR   B 1 146 ? 30.109 -22.867 -3.141  1.00 13.34 ?  146 THR   B CB   1 
ATOM   6344 O  OG1  . THR   B 1 146 ? 29.538 -23.861 -2.283  1.00 13.47 ?  146 THR   B OG1  1 
ATOM   6345 C  CG2  . THR   B 1 146 ? 30.176 -21.525 -2.417  1.00 13.34 ?  146 THR   B CG2  1 
ATOM   6346 H  H    . THR   B 1 146 ? 29.888 -24.410 -5.304  1.00 16.11 ?  146 THR   B H    1 
ATOM   6347 H  HA   . THR   B 1 146 ? 28.409 -22.430 -4.179  1.00 15.74 ?  146 THR   B HA   1 
ATOM   6348 H  HB   . THR   B 1 146 ? 31.020 -23.122 -3.364  1.00 16.04 ?  146 THR   B HB   1 
ATOM   6349 H  HG1  . THR   B 1 146 ? 29.577 -24.619 -2.661  1.00 16.20 ?  146 THR   B HG1  1 
ATOM   6350 H  HG21 . THR   B 1 146 ? 30.528 -21.644 -1.521  1.00 16.04 ?  146 THR   B HG21 1 
ATOM   6351 H  HG22 . THR   B 1 146 ? 30.760 -20.913 -2.900  1.00 16.04 ?  146 THR   B HG22 1 
ATOM   6352 H  HG23 . THR   B 1 146 ? 29.292 -21.135 -2.359  1.00 16.04 ?  146 THR   B HG23 1 
ATOM   6353 N  N    . VAL   B 1 147 ? 30.976 -22.098 -6.047  1.00 12.78 ?  147 VAL   B N    1 
ATOM   6354 C  CA   . VAL   B 1 147 ? 31.695 -21.155 -6.889  1.00 12.58 ?  147 VAL   B CA   1 
ATOM   6355 C  C    . VAL   B 1 147 ? 30.959 -21.018 -8.211  1.00 12.99 ?  147 VAL   B C    1 
ATOM   6356 O  O    . VAL   B 1 147 ? 30.594 -22.020 -8.841  1.00 13.51 ?  147 VAL   B O    1 
ATOM   6357 C  CB   . VAL   B 1 147 ? 33.152 -21.602 -7.096  1.00 12.39 ?  147 VAL   B CB   1 
ATOM   6358 C  CG1  . VAL   B 1 147 ? 33.913 -20.570 -7.906  1.00 12.61 ?  147 VAL   B CG1  1 
ATOM   6359 C  CG2  . VAL   B 1 147 ? 33.834 -21.822 -5.757  1.00 12.54 ?  147 VAL   B CG2  1 
ATOM   6360 H  H    . VAL   B 1 147 ? 31.308 -22.896 -6.057  1.00 15.37 ?  147 VAL   B H    1 
ATOM   6361 H  HA   . VAL   B 1 147 ? 31.711 -20.287 -6.456  1.00 15.14 ?  147 VAL   B HA   1 
ATOM   6362 H  HB   . VAL   B 1 147 ? 33.168 -22.439 -7.587  1.00 14.91 ?  147 VAL   B HB   1 
ATOM   6363 H  HG11 . VAL   B 1 147 ? 34.856 -20.795 -7.902  1.00 15.16 ?  147 VAL   B HG11 1 
ATOM   6364 H  HG12 . VAL   B 1 147 ? 33.578 -20.568 -8.816  1.00 15.16 ?  147 VAL   B HG12 1 
ATOM   6365 H  HG13 . VAL   B 1 147 ? 33.782 -19.695 -7.504  1.00 15.16 ?  147 VAL   B HG13 1 
ATOM   6366 H  HG21 . VAL   B 1 147 ? 34.775 -22.006 -5.908  1.00 15.08 ?  147 VAL   B HG21 1 
ATOM   6367 H  HG22 . VAL   B 1 147 ? 33.736 -21.020 -5.220  1.00 15.08 ?  147 VAL   B HG22 1 
ATOM   6368 H  HG23 . VAL   B 1 147 ? 33.418 -22.574 -5.311  1.00 15.08 ?  147 VAL   B HG23 1 
ATOM   6369 N  N    . ARG   B 1 148 ? 30.747 -19.767 -8.628  1.00 12.78 ?  148 ARG   B N    1 
ATOM   6370 C  CA   . ARG   B 1 148 ? 30.121 -19.437 -9.898  1.00 12.95 ?  148 ARG   B CA   1 
ATOM   6371 C  C    . ARG   B 1 148 ? 31.078 -18.763 -10.870 1.00 12.90 ?  148 ARG   B C    1 
ATOM   6372 O  O    . ARG   B 1 148 ? 30.791 -18.734 -12.069 1.00 14.30 ?  148 ARG   B O    1 
ATOM   6373 C  CB   . ARG   B 1 148 ? 28.890 -18.549 -9.666  1.00 13.56 ?  148 ARG   B CB   1 
ATOM   6374 C  CG   . ARG   B 1 148 ? 27.812 -19.263 -8.871  1.00 14.28 ?  148 ARG   B CG   1 
ATOM   6375 C  CD   . ARG   B 1 148 ? 26.601 -18.383 -8.560  1.00 15.30 ?  148 ARG   B CD   1 
ATOM   6376 N  NE   . ARG   B 1 148 ? 26.977 -17.182 -7.824  1.00 14.84 ?  148 ARG   B NE   1 
ATOM   6377 C  CZ   . ARG   B 1 148 ? 27.279 -17.147 -6.532  1.00 13.79 ?  148 ARG   B CZ   1 
ATOM   6378 N  NH1  . ARG   B 1 148 ? 27.217 -18.232 -5.774  1.00 13.91 ?  148 ARG   B NH1  1 
ATOM   6379 N  NH2  . ARG   B 1 148 ? 27.675 -15.999 -5.991  1.00 14.00 ?  148 ARG   B NH2  1 
ATOM   6380 H  H    . ARG   B 1 148 ? 30.974 -19.067 -8.166  1.00 15.37 ?  148 ARG   B H    1 
ATOM   6381 H  HA   . ARG   B 1 148 ? 29.817 -20.258 -10.307 1.00 15.58 ?  148 ARG   B HA   1 
ATOM   6382 H  HB2  . ARG   B 1 148 ? 29.161 -17.757 -9.168  1.00 16.30 ?  148 ARG   B HB2  1 
ATOM   6383 H  HB3  . ARG   B 1 148 ? 28.522 -18.291 -10.523 1.00 16.30 ?  148 ARG   B HB3  1 
ATOM   6384 H  HG2  . ARG   B 1 148 ? 27.497 -20.025 -9.384  1.00 17.17 ?  148 ARG   B HG2  1 
ATOM   6385 H  HG3  . ARG   B 1 148 ? 28.182 -19.562 -8.028  1.00 17.17 ?  148 ARG   B HG3  1 
ATOM   6386 H  HD2  . ARG   B 1 148 ? 26.183 -18.107 -9.392  1.00 18.40 ?  148 ARG   B HD2  1 
ATOM   6387 H  HD3  . ARG   B 1 148 ? 25.968 -18.886 -8.021  1.00 18.40 ?  148 ARG   B HD3  1 
ATOM   6388 H  HE   . ARG   B 1 148 ? 27.008 -16.443 -8.257  1.00 17.84 ?  148 ARG   B HE   1 
ATOM   6389 H  HH11 . ARG   B 1 148 ? 26.957 -18.983 -6.107  1.00 16.72 ?  148 ARG   B HH11 1 
ATOM   6390 H  HH12 . ARG   B 1 148 ? 27.410 -18.185 -4.934  1.00 16.72 ?  148 ARG   B HH12 1 
ATOM   6391 H  HH21 . ARG   B 1 148 ? 27.726 -15.291 -6.476  1.00 16.83 ?  148 ARG   B HH21 1 
ATOM   6392 H  HH22 . ARG   B 1 148 ? 27.874 -15.961 -5.155  1.00 16.83 ?  148 ARG   B HH22 1 
ATOM   6393 N  N    . THR   B 1 149 ? 32.190 -18.216 -10.383 1.00 12.77 ?  149 THR   B N    1 
ATOM   6394 C  CA   . THR   B 1 149 ? 33.230 -17.654 -11.232 1.00 12.83 ?  149 THR   B CA   1 
ATOM   6395 C  C    . THR   B 1 149 ? 34.116 -18.789 -11.746 1.00 12.50 ?  149 THR   B C    1 
ATOM   6396 O  O    . THR   B 1 149 ? 33.923 -19.959 -11.409 1.00 12.91 ?  149 THR   B O    1 
ATOM   6397 C  CB   . THR   B 1 149 ? 33.999 -16.598 -10.449 1.00 12.81 ?  149 THR   B CB   1 
ATOM   6398 O  OG1  . THR   B 1 149 ? 34.458 -17.196 -9.238  1.00 12.76 ?  149 THR   B OG1  1 
ATOM   6399 C  CG2  . THR   B 1 149 ? 33.100 -15.396 -10.150 1.00 13.51 ?  149 THR   B CG2  1 
ATOM   6400 H  H    . THR   B 1 149 ? 32.354 -18.143 -9.543  1.00 15.36 ?  149 THR   B H    1 
ATOM   6401 H  HA   . THR   B 1 149 ? 32.815 -17.222 -11.996 1.00 15.43 ?  149 THR   B HA   1 
ATOM   6402 H  HB   . THR   B 1 149 ? 34.758 -16.302 -10.967 1.00 15.41 ?  149 THR   B HB   1 
ATOM   6403 H  HG1  . THR   B 1 149 ? 34.869 -16.620 -8.775  1.00 15.34 ?  149 THR   B HG1  1 
ATOM   6404 H  HG21 . THR   B 1 149 ? 33.602 -14.721 -9.670  1.00 16.24 ?  149 THR   B HG21 1 
ATOM   6405 H  HG22 . THR   B 1 149 ? 32.771 -15.014 -10.980 1.00 16.24 ?  149 THR   B HG22 1 
ATOM   6406 H  HG23 . THR   B 1 149 ? 32.343 -15.670 -9.609  1.00 16.24 ?  149 THR   B HG23 1 
ATOM   6407 N  N    . ASN   B 1 150 ? 35.083 -18.465 -12.590 1.00 12.49 ?  150 ASN   B N    1 
ATOM   6408 C  CA   . ASN   B 1 150 ? 35.849 -19.488 -13.292 1.00 13.10 ?  150 ASN   B CA   1 
ATOM   6409 C  C    . ASN   B 1 150 ? 37.013 -19.944 -12.423 1.00 12.96 ?  150 ASN   B C    1 
ATOM   6410 O  O    . ASN   B 1 150 ? 37.941 -19.176 -12.160 1.00 13.55 ?  150 ASN   B O    1 
ATOM   6411 C  CB   . ASN   B 1 150 ? 36.322 -18.953 -14.635 1.00 14.83 ?  150 ASN   B CB   1 
ATOM   6412 C  CG   . ASN   B 1 150 ? 35.178 -18.739 -15.589 1.00 17.51 ?  150 ASN   B CG   1 
ATOM   6413 O  OD1  . ASN   B 1 150 ? 34.294 -19.581 -15.699 1.00 18.48 ?  150 ASN   B OD1  1 
ATOM   6414 N  ND2  . ASN   B 1 150 ? 35.166 -17.600 -16.259 1.00 19.10 ?  150 ASN   B ND2  1 
ATOM   6415 H  H    . ASN   B 1 150 ? 35.323 -17.656 -12.768 1.00 15.02 ?  150 ASN   B H    1 
ATOM   6416 H  HA   . ASN   B 1 150 ? 35.269 -20.253 -13.457 1.00 15.76 ?  150 ASN   B HA   1 
ATOM   6417 H  HB2  . ASN   B 1 150 ? 36.763 -18.098 -14.496 1.00 17.83 ?  150 ASN   B HB2  1 
ATOM   6418 H  HB3  . ASN   B 1 150 ? 36.933 -19.587 -15.032 1.00 17.83 ?  150 ASN   B HB3  1 
ATOM   6419 H  HD21 . ASN   B 1 150 ? 34.530 -17.431 -16.818 1.00 22.96 ?  150 ASN   B HD21 1 
ATOM   6420 H  HD22 . ASN   B 1 150 ? 35.797 -17.024 -16.148 1.00 22.96 ?  150 ASN   B HD22 1 
ATOM   6421 N  N    . VAL   B 1 151 ? 36.975 -21.196 -11.981 1.00 12.41 ?  151 VAL   B N    1 
ATOM   6422 C  CA   . VAL   B 1 151 ? 37.993 -21.731 -11.092 1.00 12.26 ?  151 VAL   B CA   1 
ATOM   6423 C  C    . VAL   B 1 151 ? 38.702 -22.901 -11.766 1.00 12.18 ?  151 VAL   B C    1 
ATOM   6424 O  O    . VAL   B 1 151 ? 38.062 -23.831 -12.277 1.00 13.34 ?  151 VAL   B O    1 
ATOM   6425 C  CB   . VAL   B 1 151 ? 37.434 -22.068 -9.694  1.00 13.64 ?  151 VAL   B CB   1 
ATOM   6426 C  CG1  . VAL   B 1 151 ? 36.271 -23.067 -9.768  1.00 14.38 ?  151 VAL   B CG1  1 
ATOM   6427 C  CG2  . VAL   B 1 151 ? 38.541 -22.562 -8.778  1.00 14.31 ?  151 VAL   B CG2  1 
ATOM   6428 H  H    . VAL   B 1 151 ? 36.357 -21.761 -12.187 1.00 14.92 ?  151 VAL   B H    1 
ATOM   6429 H  HA   . VAL   B 1 151 ? 38.661 -21.036 -10.958 1.00 14.75 ?  151 VAL   B HA   1 
ATOM   6430 H  HB   . VAL   B 1 151 ? 37.085 -21.251 -9.303  1.00 16.40 ?  151 VAL   B HB   1 
ATOM   6431 H  HG11 . VAL   B 1 151 ? 35.957 -23.257 -8.870  1.00 17.29 ?  151 VAL   B HG11 1 
ATOM   6432 H  HG12 . VAL   B 1 151 ? 35.552 -22.682 -10.295 1.00 17.29 ?  151 VAL   B HG12 1 
ATOM   6433 H  HG13 . VAL   B 1 151 ? 36.582 -23.887 -10.187 1.00 17.29 ?  151 VAL   B HG13 1 
ATOM   6434 H  HG21 . VAL   B 1 151 ? 38.190 -22.645 -7.876  1.00 17.21 ?  151 VAL   B HG21 1 
ATOM   6435 H  HG22 . VAL   B 1 151 ? 38.851 -23.427 -9.089  1.00 17.21 ?  151 VAL   B HG22 1 
ATOM   6436 H  HG23 . VAL   B 1 151 ? 39.272 -21.925 -8.788  1.00 17.21 ?  151 VAL   B HG23 1 
ATOM   6437 N  N    . TYR   B 1 152 ? 40.034 -22.805 -11.791 1.00 11.76 ?  152 TYR   B N    1 
ATOM   6438 C  CA   . TYR   B 1 152 ? 40.943 -23.782 -12.372 1.00 11.93 ?  152 TYR   B CA   1 
ATOM   6439 C  C    . TYR   B 1 152 ? 41.666 -24.462 -11.214 1.00 11.47 ?  152 TYR   B C    1 
ATOM   6440 O  O    . TYR   B 1 152 ? 42.507 -23.845 -10.554 1.00 11.90 ?  152 TYR   B O    1 
ATOM   6441 C  CB   . TYR   B 1 152 ? 41.913 -23.071 -13.320 1.00 12.70 ?  152 TYR   B CB   1 
ATOM   6442 C  CG   . TYR   B 1 152 ? 41.233 -22.611 -14.585 1.00 13.34 ?  152 TYR   B CG   1 
ATOM   6443 C  CD1  . TYR   B 1 152 ? 40.558 -21.394 -14.647 1.00 13.90 ?  152 TYR   B CD1  1 
ATOM   6444 C  CD2  . TYR   B 1 152 ? 41.244 -23.409 -15.715 1.00 14.28 ?  152 TYR   B CD2  1 
ATOM   6445 C  CE1  . TYR   B 1 152 ? 39.916 -20.995 -15.806 1.00 15.24 ?  152 TYR   B CE1  1 
ATOM   6446 C  CE2  . TYR   B 1 152 ? 40.612 -23.020 -16.875 1.00 15.40 ?  152 TYR   B CE2  1 
ATOM   6447 C  CZ   . TYR   B 1 152 ? 39.948 -21.809 -16.921 1.00 15.56 ?  152 TYR   B CZ   1 
ATOM   6448 O  OH   . TYR   B 1 152 ? 39.316 -21.430 -18.082 1.00 17.97 ?  152 TYR   B OH   1 
ATOM   6449 H  H    . TYR   B 1 152 ? 40.462 -22.130 -11.454 1.00 14.15 ?  152 TYR   B H    1 
ATOM   6450 H  HA   . TYR   B 1 152 ? 40.439 -24.446 -12.869 1.00 14.34 ?  152 TYR   B HA   1 
ATOM   6451 H  HB2  . TYR   B 1 152 ? 42.277 -22.290 -12.868 1.00 15.27 ?  152 TYR   B HB2  1 
ATOM   6452 H  HB3  . TYR   B 1 152 ? 42.628 -23.678 -13.558 1.00 15.27 ?  152 TYR   B HB3  1 
ATOM   6453 H  HD1  . TYR   B 1 152 ? 40.528 -20.847 -13.894 1.00 16.71 ?  152 TYR   B HD1  1 
ATOM   6454 H  HD2  . TYR   B 1 152 ? 41.688 -24.228 -15.687 1.00 17.17 ?  152 TYR   B HD2  1 
ATOM   6455 H  HE1  . TYR   B 1 152 ? 39.467 -20.182 -15.836 1.00 18.33 ?  152 TYR   B HE1  1 
ATOM   6456 H  HE2  . TYR   B 1 152 ? 40.636 -23.573 -17.621 1.00 18.52 ?  152 TYR   B HE2  1 
ATOM   6457 H  HH   . TYR   B 1 152 ? 39.423 -22.025 -18.667 1.00 21.60 ?  152 TYR   B HH   1 
ATOM   6458 N  N    . LEU   B 1 153 ? 41.301 -25.719 -10.945 1.00 11.63 ?  153 LEU   B N    1 
ATOM   6459 C  CA   . LEU   B 1 153 ? 41.802 -26.471 -9.803  1.00 11.42 ?  153 LEU   B CA   1 
ATOM   6460 C  C    . LEU   B 1 153 ? 43.033 -27.273 -10.194 1.00 11.81 ?  153 LEU   B C    1 
ATOM   6461 O  O    . LEU   B 1 153 ? 43.013 -28.002 -11.188 1.00 12.92 ?  153 LEU   B O    1 
ATOM   6462 C  CB   . LEU   B 1 153 ? 40.719 -27.427 -9.298  1.00 12.02 ?  153 LEU   B CB   1 
ATOM   6463 C  CG   . LEU   B 1 153 ? 39.467 -26.778 -8.715  1.00 12.79 ?  153 LEU   B CG   1 
ATOM   6464 C  CD1  . LEU   B 1 153 ? 38.363 -27.821 -8.563  1.00 13.70 ?  153 LEU   B CD1  1 
ATOM   6465 C  CD2  . LEU   B 1 153 ? 39.767 -26.129 -7.376  1.00 12.91 ?  153 LEU   B CD2  1 
ATOM   6466 H  H    . LEU   B 1 153 ? 40.735 -26.168 -11.427 1.00 13.98 ?  153 LEU   B H    1 
ATOM   6467 H  HA   . LEU   B 1 153 ? 42.028 -25.856 -9.092  1.00 13.74 ?  153 LEU   B HA   1 
ATOM   6468 H  HB2  . LEU   B 1 153 ? 40.432 -27.986 -10.034 1.00 14.46 ?  153 LEU   B HB2  1 
ATOM   6469 H  HB3  . LEU   B 1 153 ? 41.100 -27.980 -8.599  1.00 14.46 ?  153 LEU   B HB3  1 
ATOM   6470 H  HG   . LEU   B 1 153 ? 39.147 -26.085 -9.320  1.00 15.38 ?  153 LEU   B HG   1 
ATOM   6471 H  HD11 . LEU   B 1 153 ? 37.563 -27.383 -8.232  1.00 16.47 ?  153 LEU   B HD11 1 
ATOM   6472 H  HD12 . LEU   B 1 153 ? 38.191 -28.218 -9.427  1.00 16.47 ?  153 LEU   B HD12 1 
ATOM   6473 H  HD13 . LEU   B 1 153 ? 38.659 -28.493 -7.934  1.00 16.47 ?  153 LEU   B HD13 1 
ATOM   6474 H  HD21 . LEU   B 1 153 ? 38.951 -25.763 -7.007  1.00 15.53 ?  153 LEU   B HD21 1 
ATOM   6475 H  HD22 . LEU   B 1 153 ? 40.131 -26.802 -6.778  1.00 15.53 ?  153 LEU   B HD22 1 
ATOM   6476 H  HD23 . LEU   B 1 153 ? 40.419 -25.421 -7.508  1.00 15.53 ?  153 LEU   B HD23 1 
ATOM   6477 N  N    . ALA   B 1 154 ? 44.086 -27.166 -9.389  1.00 11.85 ?  154 ALA   B N    1 
ATOM   6478 C  CA   . ALA   B 1 154 ? 45.312 -27.929 -9.577  1.00 13.06 ?  154 ALA   B CA   1 
ATOM   6479 C  C    . ALA   B 1 154 ? 45.379 -29.012 -8.506  1.00 13.53 ?  154 ALA   B C    1 
ATOM   6480 O  O    . ALA   B 1 154 ? 45.297 -28.718 -7.305  1.00 14.73 ?  154 ALA   B O    1 
ATOM   6481 C  CB   . ALA   B 1 154 ? 46.538 -27.021 -9.513  1.00 13.72 ?  154 ALA   B CB   1 
ATOM   6482 H  H    . ALA   B 1 154 ? 44.104 -26.641 -8.702  1.00 14.26 ?  154 ALA   B H    1 
ATOM   6483 H  HA   . ALA   B 1 154 ? 45.293 -28.356 -10.440 1.00 15.71 ?  154 ALA   B HA   1 
ATOM   6484 H  HB1  . ALA   B 1 154 ? 47.335 -27.557 -9.639  1.00 16.49 ?  154 ALA   B HB1  1 
ATOM   6485 H  HB2  . ALA   B 1 154 ? 46.474 -26.353 -10.215 1.00 16.49 ?  154 ALA   B HB2  1 
ATOM   6486 H  HB3  . ALA   B 1 154 ? 46.568 -26.583 -8.646  1.00 16.49 ?  154 ALA   B HB3  1 
ATOM   6487 N  N    . VAL   B 1 155 ? 45.508 -30.260 -8.942  1.00 12.60 ?  155 VAL   B N    1 
ATOM   6488 C  CA   . VAL   B 1 155 ? 45.615 -31.411 -8.055  1.00 12.78 ?  155 VAL   B CA   1 
ATOM   6489 C  C    . VAL   B 1 155 ? 46.957 -32.079 -8.335  1.00 13.20 ?  155 VAL   B C    1 
ATOM   6490 O  O    . VAL   B 1 155 ? 47.194 -32.566 -9.448  1.00 14.97 ?  155 VAL   B O    1 
ATOM   6491 C  CB   . VAL   B 1 155 ? 44.453 -32.400 -8.251  1.00 14.48 ?  155 VAL   B CB   1 
ATOM   6492 C  CG1  . VAL   B 1 155 ? 44.639 -33.606 -7.347  1.00 14.42 ?  155 VAL   B CG1  1 
ATOM   6493 C  CG2  . VAL   B 1 155 ? 43.113 -31.712 -7.976  1.00 15.69 ?  155 VAL   B CG2  1 
ATOM   6494 H  H    . VAL   B 1 155 ? 45.541 -30.468 -9.777  1.00 15.15 ?  155 VAL   B H    1 
ATOM   6495 H  HA   . VAL   B 1 155 ? 45.606 -31.116 -7.134  1.00 15.37 ?  155 VAL   B HA   1 
ATOM   6496 H  HB   . VAL   B 1 155 ? 44.448 -32.709 -9.172  1.00 17.41 ?  155 VAL   B HB   1 
ATOM   6497 H  HG11 . VAL   B 1 155 ? 43.810 -34.111 -7.314  1.00 17.34 ?  155 VAL   B HG11 1 
ATOM   6498 H  HG12 . VAL   B 1 155 ? 45.349 -34.169 -7.701  1.00 17.34 ?  155 VAL   B HG12 1 
ATOM   6499 H  HG13 . VAL   B 1 155 ? 44.873 -33.303 -6.455  1.00 17.34 ?  155 VAL   B HG13 1 
ATOM   6500 H  HG21 . VAL   B 1 155 ? 42.399 -32.360 -8.073  1.00 18.86 ?  155 VAL   B HG21 1 
ATOM   6501 H  HG22 . VAL   B 1 155 ? 43.122 -31.359 -7.072  1.00 18.86 ?  155 VAL   B HG22 1 
ATOM   6502 H  HG23 . VAL   B 1 155 ? 42.993 -30.988 -8.612  1.00 18.86 ?  155 VAL   B HG23 1 
ATOM   6503 N  N    . PHE   B 1 156 ? 47.823 -32.120 -7.318  1.00 13.49 ?  156 PHE   B N    1 
ATOM   6504 C  CA   . PHE   B 1 156 ? 49.204 -32.572 -7.511  1.00 14.59 ?  156 PHE   B CA   1 
ATOM   6505 C  C    . PHE   B 1 156 ? 49.309 -34.069 -7.810  1.00 15.49 ?  156 PHE   B C    1 
ATOM   6506 O  O    . PHE   B 1 156 ? 50.046 -34.484 -8.716  1.00 17.25 ?  156 PHE   B O    1 
ATOM   6507 C  CB   . PHE   B 1 156 ? 50.024 -32.212 -6.274  1.00 14.87 ?  156 PHE   B CB   1 
ATOM   6508 C  CG   . PHE   B 1 156 ? 51.452 -32.672 -6.333  1.00 15.39 ?  156 PHE   B CG   1 
ATOM   6509 C  CD1  . PHE   B 1 156 ? 52.331 -32.135 -7.255  1.00 17.15 ?  156 PHE   B CD1  1 
ATOM   6510 C  CD2  . PHE   B 1 156 ? 51.914 -33.634 -5.457  1.00 15.61 ?  156 PHE   B CD2  1 
ATOM   6511 C  CE1  . PHE   B 1 156 ? 53.654 -32.552 -7.305  1.00 17.99 ?  156 PHE   B CE1  1 
ATOM   6512 C  CE2  . PHE   B 1 156 ? 53.233 -34.057 -5.505  1.00 16.84 ?  156 PHE   B CE2  1 
ATOM   6513 C  CZ   . PHE   B 1 156 ? 54.093 -33.513 -6.433  1.00 17.48 ?  156 PHE   B CZ   1 
ATOM   6514 H  H    . PHE   B 1 156 ? 47.631 -31.895 -6.504  1.00 16.22 ?  156 PHE   B H    1 
ATOM   6515 H  HA   . PHE   B 1 156 ? 49.577 -32.091 -8.260  1.00 17.55 ?  156 PHE   B HA   1 
ATOM   6516 H  HB2  . PHE   B 1 156 ? 50.030 -31.248 -6.173  1.00 17.88 ?  156 PHE   B HB2  1 
ATOM   6517 H  HB3  . PHE   B 1 156 ? 49.614 -32.621 -5.494  1.00 17.88 ?  156 PHE   B HB3  1 
ATOM   6518 H  HD1  . PHE   B 1 156 ? 52.030 -31.480 -7.848  1.00 20.62 ?  156 PHE   B HD1  1 
ATOM   6519 H  HD2  . PHE   B 1 156 ? 51.331 -34.008 -4.832  1.00 18.77 ?  156 PHE   B HD2  1 
ATOM   6520 H  HE1  . PHE   B 1 156 ? 54.232 -32.182 -7.933  1.00 21.62 ?  156 PHE   B HE1  1 
ATOM   6521 H  HE2  . PHE   B 1 156 ? 53.531 -34.712 -4.915  1.00 20.24 ?  156 PHE   B HE2  1 
ATOM   6522 H  HZ   . PHE   B 1 156 ? 54.977 -33.798 -6.466  1.00 21.01 ?  156 PHE   B HZ   1 
ATOM   6523 N  N    . ASP   B 1 157 ? 48.634 -34.898 -7.028  1.00 16.14 ?  157 ASP   B N    1 
ATOM   6524 C  CA   . ASP   B 1 157 ? 48.784 -36.345 -7.124  1.00 17.27 ?  157 ASP   B CA   1 
ATOM   6525 C  C    . ASP   B 1 157 ? 47.862 -36.892 -8.211  1.00 17.14 ?  157 ASP   B C    1 
ATOM   6526 O  O    . ASP   B 1 157 ? 46.635 -36.769 -8.110  1.00 16.55 ?  157 ASP   B O    1 
ATOM   6527 C  CB   . ASP   B 1 157 ? 48.446 -36.962 -5.772  1.00 18.32 ?  157 ASP   B CB   1 
ATOM   6528 C  CG   . ASP   B 1 157 ? 48.562 -38.475 -5.764  1.00 20.37 ?  157 ASP   B CG   1 
ATOM   6529 O  OD1  . ASP   B 1 157 ? 48.892 -39.081 -6.811  1.00 20.82 ?  157 ASP   B OD1  1 
ATOM   6530 O  OD2  . ASP   B 1 157 ? 48.331 -39.066 -4.691  1.00 22.61 -1 157 ASP   B OD2  1 
ATOM   6531 H  H    . ASP   B 1 157 ? 48.076 -34.648 -6.428  1.00 19.40 ?  157 ASP   B H    1 
ATOM   6532 H  HA   . ASP   B 1 157 ? 49.704 -36.568 -7.352  1.00 20.76 ?  157 ASP   B HA   1 
ATOM   6533 H  HB2  . ASP   B 1 157 ? 49.045 -36.594 -5.104  1.00 22.01 ?  157 ASP   B HB2  1 
ATOM   6534 H  HB3  . ASP   B 1 157 ? 47.530 -36.737 -5.551  1.00 22.01 ?  157 ASP   B HB3  1 
ATOM   6535 N  N    A LYS   B 1 158 ? 48.459 -37.513 -9.236  0.50 17.84 ?  158 LYS   B N    1 
ATOM   6536 N  N    B LYS   B 1 158 ? 48.458 -37.516 -9.235  0.50 17.85 ?  158 LYS   B N    1 
ATOM   6537 C  CA   A LYS   B 1 158 ? 47.683 -38.110 -10.323 0.50 18.85 ?  158 LYS   B CA   1 
ATOM   6538 C  CA   B LYS   B 1 158 ? 47.681 -38.107 -10.324 0.50 18.84 ?  158 LYS   B CA   1 
ATOM   6539 C  C    A LYS   B 1 158 ? 46.623 -39.077 -9.799  0.50 18.94 ?  158 LYS   B C    1 
ATOM   6540 C  C    B LYS   B 1 158 ? 46.625 -39.082 -9.803  0.50 18.94 ?  158 LYS   B C    1 
ATOM   6541 O  O    A LYS   B 1 158 ? 45.516 -39.160 -10.347 0.50 18.96 ?  158 LYS   B O    1 
ATOM   6542 O  O    B LYS   B 1 158 ? 45.521 -39.173 -10.357 0.50 18.96 ?  158 LYS   B O    1 
ATOM   6543 C  CB   A LYS   B 1 158 ? 48.635 -38.816 -11.297 0.50 20.29 ?  158 LYS   B CB   1 
ATOM   6544 C  CB   B LYS   B 1 158 ? 48.631 -38.802 -11.308 0.50 20.25 ?  158 LYS   B CB   1 
ATOM   6545 C  CG   A LYS   B 1 158 ? 47.966 -39.735 -12.311 0.50 21.98 ?  158 LYS   B CG   1 
ATOM   6546 C  CG   B LYS   B 1 158 ? 47.960 -39.686 -12.353 0.50 21.92 ?  158 LYS   B CG   1 
ATOM   6547 C  CD   A LYS   B 1 158 ? 47.076 -38.973 -13.270 0.50 23.58 ?  158 LYS   B CD   1 
ATOM   6548 C  CD   B LYS   B 1 158 ? 47.096 -38.887 -13.307 0.50 23.58 ?  158 LYS   B CD   1 
ATOM   6549 C  CE   A LYS   B 1 158 ? 46.500 -39.898 -14.327 0.50 24.84 ?  158 LYS   B CE   1 
ATOM   6550 C  CE   B LYS   B 1 158 ? 46.522 -39.780 -14.394 0.50 24.88 ?  158 LYS   B CE   1 
ATOM   6551 N  NZ   A LYS   B 1 158 ? 45.432 -39.238 -15.127 0.50 24.94 ?  158 LYS   B NZ   1 
ATOM   6552 N  NZ   B LYS   B 1 158 ? 45.481 -39.088 -15.204 0.50 25.19 ?  158 LYS   B NZ   1 
ATOM   6553 H  H    A LYS   B 1 158 ? 49.313 -37.609 -9.323  0.50 21.44 ?  158 LYS   B H    1 
ATOM   6554 H  H    B LYS   B 1 158 ? 49.312 -37.616 -9.320  0.50 21.45 ?  158 LYS   B H    1 
ATOM   6555 H  HA   A LYS   B 1 158 ? 47.233 -37.406 -10.814 0.50 22.65 ?  158 LYS   B HA   1 
ATOM   6556 H  HA   B LYS   B 1 158 ? 47.227 -37.400 -10.808 0.50 22.65 ?  158 LYS   B HA   1 
ATOM   6557 H  HB2  A LYS   B 1 158 ? 49.122 -38.142 -11.803 0.50 24.38 ?  158 LYS   B HB2  1 
ATOM   6558 H  HB2  B LYS   B 1 158 ? 49.133 -38.122 -11.791 0.50 24.34 ?  158 LYS   B HB2  1 
ATOM   6559 H  HB3  A LYS   B 1 158 ? 49.263 -39.352 -10.790 0.50 24.38 ?  158 LYS   B HB3  1 
ATOM   6560 H  HB3  B LYS   B 1 158 ? 49.246 -39.360 -10.809 0.50 24.34 ?  158 LYS   B HB3  1 
ATOM   6561 H  HG2  A LYS   B 1 158 ? 48.653 -40.179 -12.834 0.50 26.41 ?  158 LYS   B HG2  1 
ATOM   6562 H  HG2  B LYS   B 1 158 ? 48.647 -40.131 -12.877 0.50 26.34 ?  158 LYS   B HG2  1 
ATOM   6563 H  HG3  A LYS   B 1 158 ? 47.428 -40.402 -11.853 0.50 26.41 ?  158 LYS   B HG3  1 
ATOM   6564 H  HG3  B LYS   B 1 158 ? 47.403 -40.352 -11.918 0.50 26.34 ?  158 LYS   B HG3  1 
ATOM   6565 H  HD2  A LYS   B 1 158 ? 46.341 -38.572 -12.779 0.50 28.33 ?  158 LYS   B HD2  1 
ATOM   6566 H  HD2  B LYS   B 1 158 ? 46.360 -38.487 -12.819 0.50 28.33 ?  158 LYS   B HD2  1 
ATOM   6567 H  HD3  A LYS   B 1 158 ? 47.598 -38.286 -13.716 0.50 28.33 ?  158 LYS   B HD3  1 
ATOM   6568 H  HD3  B LYS   B 1 158 ? 47.635 -38.200 -13.730 0.50 28.33 ?  158 LYS   B HD3  1 
ATOM   6569 H  HE2  A LYS   B 1 158 ? 47.207 -40.168 -14.933 0.50 29.84 ?  158 LYS   B HE2  1 
ATOM   6570 H  HE2  B LYS   B 1 158 ? 47.235 -40.054 -14.991 0.50 29.89 ?  158 LYS   B HE2  1 
ATOM   6571 H  HE3  A LYS   B 1 158 ? 46.117 -40.678 -13.895 0.50 29.84 ?  158 LYS   B HE3  1 
ATOM   6572 H  HE3  B LYS   B 1 158 ? 46.114 -40.559 -13.983 0.50 29.89 ?  158 LYS   B HE3  1 
ATOM   6573 H  HZ1  A LYS   B 1 158 ? 45.113 -39.802 -15.736 0.50 29.96 ?  158 LYS   B HZ1  1 
ATOM   6574 H  HZ1  B LYS   B 1 158 ? 45.165 -39.638 -15.829 0.50 30.26 ?  158 LYS   B HZ1  1 
ATOM   6575 H  HZ2  A LYS   B 1 158 ? 44.766 -38.982 -14.594 0.50 29.96 ?  158 LYS   B HZ2  1 
ATOM   6576 H  HZ2  B LYS   B 1 158 ? 44.808 -38.831 -14.680 0.50 30.26 ?  158 LYS   B HZ2  1 
ATOM   6577 H  HZ3  A LYS   B 1 158 ? 45.761 -38.521 -15.541 0.50 29.96 ?  158 LYS   B HZ3  1 
ATOM   6578 H  HZ3  B LYS   B 1 158 ? 45.830 -38.371 -15.599 0.50 30.26 ?  158 LYS   B HZ3  1 
ATOM   6579 N  N    . ASN   B 1 159 ? 46.946 -39.833 -8.747  1.00 19.10 ?  159 ASN   B N    1 
ATOM   6580 C  CA   . ASN   B 1 159 ? 45.993 -40.817 -8.235  1.00 19.98 ?  159 ASN   B CA   1 
ATOM   6581 C  C    . ASN   B 1 159 ? 44.793 -40.147 -7.561  1.00 18.92 ?  159 ASN   B C    1 
ATOM   6582 O  O    . ASN   B 1 159 ? 43.660 -40.637 -7.672  1.00 19.06 ?  159 ASN   B O    1 
ATOM   6583 C  CB   . ASN   B 1 159 ? 46.700 -41.796 -7.304  1.00 21.74 ?  159 ASN   B CB   1 
ATOM   6584 C  CG   . ASN   B 1 159 ? 47.727 -42.636 -8.029  1.00 23.95 ?  159 ASN   B CG   1 
ATOM   6585 O  OD1  . ASN   B 1 159 ? 47.475 -43.130 -9.136  1.00 25.13 ?  159 ASN   B OD1  1 
ATOM   6586 N  ND2  . ASN   B 1 159 ? 48.894 -42.807 -7.412  1.00 24.74 ?  159 ASN   B ND2  1 
ATOM   6587 H  H    A ASN   B 1 159 ? 47.693 -39.792 -8.326  0.50 22.95 ?  159 ASN   B H    1 
ATOM   6588 H  H    B ASN   B 1 159 ? 47.691 -39.789 -8.324  0.50 22.95 ?  159 ASN   B H    1 
ATOM   6589 H  HA   . ASN   B 1 159 ? 45.653 -41.324 -8.990  1.00 24.01 ?  159 ASN   B HA   1 
ATOM   6590 H  HB2  . ASN   B 1 159 ? 47.153 -41.303 -6.606  1.00 26.12 ?  159 ASN   B HB2  1 
ATOM   6591 H  HB3  . ASN   B 1 159 ? 46.044 -42.398 -6.924  1.00 26.12 ?  159 ASN   B HB3  1 
ATOM   6592 H  HD21 . ASN   B 1 159 ? 49.518 -43.277 -7.782  1.00 29.72 ?  159 ASN   B HD21 1 
ATOM   6593 H  HD22 . ASN   B 1 159 ? 49.028 -42.461 -6.636  1.00 29.72 ?  159 ASN   B HD22 1 
ATOM   6594 N  N    . LEU   B 1 160 ? 45.007 -39.014 -6.880  1.00 17.88 ?  160 LEU   B N    1 
ATOM   6595 C  CA   . LEU   B 1 160 ? 43.873 -38.280 -6.330  1.00 16.77 ?  160 LEU   B CA   1 
ATOM   6596 C  C    . LEU   B 1 160 ? 43.077 -37.615 -7.441  1.00 16.16 ?  160 LEU   B C    1 
ATOM   6597 O  O    . LEU   B 1 160 ? 41.839 -37.615 -7.416  1.00 15.65 ?  160 LEU   B O    1 
ATOM   6598 C  CB   . LEU   B 1 160 ? 44.329 -37.247 -5.301  1.00 16.34 ?  160 LEU   B CB   1 
ATOM   6599 C  CG   . LEU   B 1 160 ? 43.198 -36.366 -4.753  1.00 16.20 ?  160 LEU   B CG   1 
ATOM   6600 C  CD1  . LEU   B 1 160 ? 42.089 -37.205 -4.122  1.00 17.27 ?  160 LEU   B CD1  1 
ATOM   6601 C  CD2  . LEU   B 1 160 ? 43.738 -35.352 -3.755  1.00 16.47 ?  160 LEU   B CD2  1 
ATOM   6602 H  H    . LEU   B 1 160 ? 45.780 -38.653 -6.743  1.00 21.49 ?  160 LEU   B H    1 
ATOM   6603 H  HA   . LEU   B 1 160 ? 43.290 -38.910 -5.887  1.00 20.16 ?  160 LEU   B HA   1 
ATOM   6604 H  HB2  . LEU   B 1 160 ? 44.736 -37.717 -4.554  1.00 19.65 ?  160 LEU   B HB2  1 
ATOM   6605 H  HB3  . LEU   B 1 160 ? 44.990 -36.666 -5.715  1.00 19.65 ?  160 LEU   B HB3  1 
ATOM   6606 H  HG   . LEU   B 1 160 ? 42.810 -35.873 -5.489  1.00 19.48 ?  160 LEU   B HG   1 
ATOM   6607 H  HD11 . LEU   B 1 160 ? 41.450 -36.612 -3.702  1.00 20.76 ?  160 LEU   B HD11 1 
ATOM   6608 H  HD12 . LEU   B 1 160 ? 41.650 -37.729 -4.813  1.00 20.76 ?  160 LEU   B HD12 1 
ATOM   6609 H  HD13 . LEU   B 1 160 ? 42.477 -37.798 -3.457  1.00 20.76 ?  160 LEU   B HD13 1 
ATOM   6610 H  HD21 . LEU   B 1 160 ? 43.003 -34.797 -3.450  1.00 19.79 ?  160 LEU   B HD21 1 
ATOM   6611 H  HD22 . LEU   B 1 160 ? 44.133 -35.822 -3.008  1.00 19.79 ?  160 LEU   B HD22 1 
ATOM   6612 H  HD23 . LEU   B 1 160 ? 44.406 -34.803 -4.196  1.00 19.79 ?  160 LEU   B HD23 1 
ATOM   6613 N  N    . TYR   B 1 161 ? 43.773 -37.039 -8.424  1.00 16.33 ?  161 TYR   B N    1 
ATOM   6614 C  CA   . TYR   B 1 161 ? 43.096 -36.474 -9.585  1.00 16.17 ?  161 TYR   B CA   1 
ATOM   6615 C  C    . TYR   B 1 161 ? 42.153 -37.498 -10.208 1.00 15.88 ?  161 TYR   B C    1 
ATOM   6616 O  O    . TYR   B 1 161 ? 40.981 -37.201 -10.475 1.00 15.75 ?  161 TYR   B O    1 
ATOM   6617 C  CB   . TYR   B 1 161 ? 44.141 -35.991 -10.599 1.00 16.90 ?  161 TYR   B CB   1 
ATOM   6618 C  CG   . TYR   B 1 161 ? 43.566 -35.523 -11.913 1.00 17.44 ?  161 TYR   B CG   1 
ATOM   6619 C  CD1  . TYR   B 1 161 ? 43.165 -34.203 -12.082 1.00 17.38 ?  161 TYR   B CD1  1 
ATOM   6620 C  CD2  . TYR   B 1 161 ? 43.403 -36.400 -12.981 1.00 18.12 ?  161 TYR   B CD2  1 
ATOM   6621 C  CE1  . TYR   B 1 161 ? 42.636 -33.768 -13.271 1.00 18.12 ?  161 TYR   B CE1  1 
ATOM   6622 C  CE2  . TYR   B 1 161 ? 42.865 -35.972 -14.174 1.00 19.00 ?  161 TYR   B CE2  1 
ATOM   6623 C  CZ   . TYR   B 1 161 ? 42.487 -34.653 -14.314 1.00 18.81 ?  161 TYR   B CZ   1 
ATOM   6624 O  OH   . TYR   B 1 161 ? 41.950 -34.211 -15.499 1.00 20.67 ?  161 TYR   B OH   1 
ATOM   6625 H  H    . TYR   B 1 161 ? 44.626 -36.974 -8.446  1.00 19.63 ?  161 TYR   B H    1 
ATOM   6626 H  HA   . TYR   B 1 161 ? 42.568 -35.708 -9.307  1.00 19.44 ?  161 TYR   B HA   1 
ATOM   6627 H  HB2  . TYR   B 1 161 ? 44.630 -35.247 -10.211 1.00 20.32 ?  161 TYR   B HB2  1 
ATOM   6628 H  HB3  . TYR   B 1 161 ? 44.751 -36.719 -10.789 1.00 20.32 ?  161 TYR   B HB3  1 
ATOM   6629 H  HD1  . TYR   B 1 161 ? 43.268 -33.596 -11.381 1.00 20.89 ?  161 TYR   B HD1  1 
ATOM   6630 H  HD2  . TYR   B 1 161 ? 43.657 -37.287 -12.889 1.00 21.78 ?  161 TYR   B HD2  1 
ATOM   6631 H  HE1  . TYR   B 1 161 ? 42.379 -32.875 -13.367 1.00 21.77 ?  161 TYR   B HE1  1 
ATOM   6632 H  HE2  . TYR   B 1 161 ? 42.763 -36.561 -14.883 1.00 22.83 ?  161 TYR   B HE2  1 
ATOM   6633 H  HH   . TYR   B 1 161 ? 41.917 -34.849 -16.048 1.00 24.84 ?  161 TYR   B HH   1 
ATOM   6634 N  N    . ASP   B 1 162 ? 42.651 -38.718 -10.435 1.00 16.63 ?  162 ASP   B N    1 
ATOM   6635 C  CA   . ASP   B 1 162 ? 41.827 -39.752 -11.051 1.00 16.79 ?  162 ASP   B CA   1 
ATOM   6636 C  C    . ASP   B 1 162 ? 40.620 -40.090 -10.183 1.00 16.26 ?  162 ASP   B C    1 
ATOM   6637 O  O    . ASP   B 1 162 ? 39.518 -40.311 -10.699 1.00 16.74 ?  162 ASP   B O    1 
ATOM   6638 C  CB   . ASP   B 1 162 ? 42.663 -41.010 -11.300 1.00 18.38 ?  162 ASP   B CB   1 
ATOM   6639 C  CG   . ASP   B 1 162 ? 43.657 -40.850 -12.440 1.00 19.77 ?  162 ASP   B CG   1 
ATOM   6640 O  OD1  . ASP   B 1 162 ? 43.524 -39.907 -13.243 1.00 19.95 ?  162 ASP   B OD1  1 
ATOM   6641 O  OD2  . ASP   B 1 162 ? 44.566 -41.702 -12.545 1.00 21.80 -1 162 ASP   B OD2  1 
ATOM   6642 H  H    . ASP   B 1 162 ? 43.454 -38.961 -10.242 1.00 19.99 ?  162 ASP   B H    1 
ATOM   6643 H  HA   . ASP   B 1 162 ? 41.503 -39.430 -11.904 1.00 20.19 ?  162 ASP   B HA   1 
ATOM   6644 H  HB2  . ASP   B 1 162 ? 43.169 -41.218 -10.500 1.00 22.09 ?  162 ASP   B HB2  1 
ATOM   6645 H  HB3  . ASP   B 1 162 ? 42.073 -41.742 -11.524 1.00 22.09 ?  162 ASP   B HB3  1 
ATOM   6646 N  N    A LYS   B 1 163 ? 40.807 -40.153 -8.863  0.50 16.11 ?  163 LYS   B N    1 
ATOM   6647 N  N    B LYS   B 1 163 ? 40.811 -40.163 -8.866  0.50 15.98 ?  163 LYS   B N    1 
ATOM   6648 C  CA   A LYS   B 1 163 ? 39.684 -40.447 -7.979  0.50 16.81 ?  163 LYS   B CA   1 
ATOM   6649 C  CA   B LYS   B 1 163 ? 39.685 -40.446 -7.981  0.50 16.58 ?  163 LYS   B CA   1 
ATOM   6650 C  C    A LYS   B 1 163 ? 38.643 -39.336 -8.022  0.50 15.61 ?  163 LYS   B C    1 
ATOM   6651 C  C    B LYS   B 1 163 ? 38.643 -39.337 -8.049  0.50 15.43 ?  163 LYS   B C    1 
ATOM   6652 O  O    A LYS   B 1 163 ? 37.435 -39.606 -7.998  0.50 16.41 ?  163 LYS   B O    1 
ATOM   6653 O  O    B LYS   B 1 163 ? 37.436 -39.608 -8.078  0.50 16.07 ?  163 LYS   B O    1 
ATOM   6654 C  CB   A LYS   B 1 163 ? 40.172 -40.657 -6.548  0.50 19.59 ?  163 LYS   B CB   1 
ATOM   6655 C  CB   B LYS   B 1 163 ? 40.174 -40.631 -6.547  0.50 19.27 ?  163 LYS   B CB   1 
ATOM   6656 C  CG   A LYS   B 1 163 ? 39.090 -41.195 -5.627  0.50 23.82 ?  163 LYS   B CG   1 
ATOM   6657 C  CG   B LYS   B 1 163 ? 39.082 -41.091 -5.603  0.50 23.47 ?  163 LYS   B CG   1 
ATOM   6658 C  CD   A LYS   B 1 163 ? 39.495 -41.159 -4.166  0.50 27.55 ?  163 LYS   B CD   1 
ATOM   6659 C  CD   B LYS   B 1 163 ? 39.597 -41.351 -4.201  0.50 27.34 ?  163 LYS   B CD   1 
ATOM   6660 C  CE   A LYS   B 1 163 ? 38.427 -41.818 -3.302  0.50 30.02 ?  163 LYS   B CE   1 
ATOM   6661 C  CE   B LYS   B 1 163 ? 38.530 -42.045 -3.367  0.50 29.88 ?  163 LYS   B CE   1 
ATOM   6662 N  NZ   A LYS   B 1 163 ? 38.549 -41.454 -1.864  0.50 31.40 ?  163 LYS   B NZ   1 
ATOM   6663 N  NZ   B LYS   B 1 163 ? 38.606 -41.681 -1.926  0.50 31.22 ?  163 LYS   B NZ   1 
ATOM   6664 H  H    A LYS   B 1 163 ? 41.560 -40.028 -8.465  0.50 19.37 ?  163 LYS   B H    1 
ATOM   6665 H  H    B LYS   B 1 163 ? 41.567 -40.054 -8.469  0.50 19.21 ?  163 LYS   B H    1 
ATOM   6666 H  HA   A LYS   B 1 163 ? 39.256 -41.263 -8.275  0.50 20.20 ?  163 LYS   B HA   1 
ATOM   6667 H  HA   B LYS   B 1 163 ? 39.263 -41.268 -8.265  0.50 19.94 ?  163 LYS   B HA   1 
ATOM   6668 H  HB2  A LYS   B 1 163 ? 40.903 -41.297 -6.556  0.50 23.55 ?  163 LYS   B HB2  1 
ATOM   6669 H  HB2  B LYS   B 1 163 ? 40.877 -41.299 -6.540  0.50 23.16 ?  163 LYS   B HB2  1 
ATOM   6670 H  HB3  A LYS   B 1 163 ? 40.478 -39.810 -6.188  0.50 23.55 ?  163 LYS   B HB3  1 
ATOM   6671 H  HB3  B LYS   B 1 163 ? 40.517 -39.786 -6.218  0.50 23.16 ?  163 LYS   B HB3  1 
ATOM   6672 H  HG2  A LYS   B 1 163 ? 38.289 -40.658 -5.728  0.50 28.61 ?  163 LYS   B HG2  1 
ATOM   6673 H  HG2  B LYS   B 1 163 ? 38.398 -40.406 -5.549  0.50 28.20 ?  163 LYS   B HG2  1 
ATOM   6674 H  HG3  A LYS   B 1 163 ? 38.903 -42.117 -5.866  0.50 28.61 ?  163 LYS   B HG3  1 
ATOM   6675 H  HG3  B LYS   B 1 163 ? 38.699 -41.917 -5.941  0.50 28.20 ?  163 LYS   B HG3  1 
ATOM   6676 H  HD2  A LYS   B 1 163 ? 40.327 -41.646 -4.049  0.50 33.10 ?  163 LYS   B HD2  1 
ATOM   6677 H  HD2  B LYS   B 1 163 ? 40.378 -41.928 -4.244  0.50 32.84 ?  163 LYS   B HD2  1 
ATOM   6678 H  HD3  A LYS   B 1 163 ? 39.598 -40.239 -3.880  0.50 33.10 ?  163 LYS   B HD3  1 
ATOM   6679 H  HD3  B LYS   B 1 163 ? 39.821 -40.509 -3.776  0.50 32.84 ?  163 LYS   B HD3  1 
ATOM   6680 H  HE2  A LYS   B 1 163 ? 37.549 -41.551 -3.615  0.50 36.05 ?  163 LYS   B HE2  1 
ATOM   6681 H  HE2  B LYS   B 1 163 ? 37.655 -41.790 -3.698  0.50 35.89 ?  163 LYS   B HE2  1 
ATOM   6682 H  HE3  A LYS   B 1 163 ? 38.519 -42.780 -3.374  0.50 36.05 ?  163 LYS   B HE3  1 
ATOM   6683 H  HE3  B LYS   B 1 163 ? 38.646 -43.006 -3.441  0.50 35.89 ?  163 LYS   B HE3  1 
ATOM   6684 H  HZ1  A LYS   B 1 163 ? 37.908 -41.856 -1.394  0.50 37.72 ?  163 LYS   B HZ1  1 
ATOM   6685 H  HZ1  B LYS   B 1 163 ? 37.967 -42.104 -1.473  0.50 37.49 ?  163 LYS   B HZ1  1 
ATOM   6686 H  HZ2  A LYS   B 1 163 ? 39.341 -41.711 -1.552  0.50 37.72 ?  163 LYS   B HZ2  1 
ATOM   6687 H  HZ2  B LYS   B 1 163 ? 39.398 -41.912 -1.596  0.50 37.49 ?  163 LYS   B HZ2  1 
ATOM   6688 H  HZ3  A LYS   B 1 163 ? 38.470 -40.573 -1.765  0.50 37.72 ?  163 LYS   B HZ3  1 
ATOM   6689 H  HZ3  B LYS   B 1 163 ? 38.495 -40.803 -1.830  0.50 37.49 ?  163 LYS   B HZ3  1 
ATOM   6690 N  N    . LEU   B 1 164 ? 39.095 -38.081 -8.077  1.00 14.56 ?  164 LEU   B N    1 
ATOM   6691 C  CA   . LEU   B 1 164 ? 38.182 -36.945 -8.133  1.00 14.06 ?  164 LEU   B CA   1 
ATOM   6692 C  C    . LEU   B 1 164 ? 37.400 -36.922 -9.440  1.00 14.16 ?  164 LEU   B C    1 
ATOM   6693 O  O    . LEU   B 1 164 ? 36.177 -36.718 -9.441  1.00 15.16 ?  164 LEU   B O    1 
ATOM   6694 C  CB   . LEU   B 1 164 ? 38.982 -35.649 -7.971  1.00 13.67 ?  164 LEU   B CB   1 
ATOM   6695 C  CG   . LEU   B 1 164 ? 39.515 -35.371 -6.569  1.00 14.77 ?  164 LEU   B CG   1 
ATOM   6696 C  CD1  . LEU   B 1 164 ? 40.608 -34.318 -6.618  1.00 14.69 ?  164 LEU   B CD1  1 
ATOM   6697 C  CD2  . LEU   B 1 164 ? 38.401 -34.923 -5.644  1.00 16.75 ?  164 LEU   B CD2  1 
ATOM   6698 H  H    A LEU   B 1 164 ? 39.931 -37.861 -8.081  0.50 17.51 ?  164 LEU   B H    1 
ATOM   6699 H  H    B LEU   B 1 164 ? 39.931 -37.860 -8.058  0.50 17.51 ?  164 LEU   B H    1 
ATOM   6700 H  HA   . LEU   B 1 164 ? 37.555 -37.001 -7.405  1.00 16.91 ?  164 LEU   B HA   1 
ATOM   6701 H  HB2  . LEU   B 1 164 ? 39.752 -35.679 -8.570  1.00 16.44 ?  164 LEU   B HB2  1 
ATOM   6702 H  HB3  . LEU   B 1 164 ? 38.419 -34.900 -8.219  1.00 16.44 ?  164 LEU   B HB3  1 
ATOM   6703 H  HG   . LEU   B 1 164 ? 39.905 -36.179 -6.212  1.00 17.76 ?  164 LEU   B HG   1 
ATOM   6704 H  HD11 . LEU   B 1 164 ? 40.933 -34.146 -5.716  1.00 17.66 ?  164 LEU   B HD11 1 
ATOM   6705 H  HD12 . LEU   B 1 164 ? 41.345 -34.639 -7.169  1.00 17.66 ?  164 LEU   B HD12 1 
ATOM   6706 H  HD13 . LEU   B 1 164 ? 40.255 -33.496 -6.998  1.00 17.66 ?  164 LEU   B HD13 1 
ATOM   6707 H  HD21 . LEU   B 1 164 ? 38.775 -34.705 -4.777  1.00 20.14 ?  164 LEU   B HD21 1 
ATOM   6708 H  HD22 . LEU   B 1 164 ? 37.966 -34.144 -6.023  1.00 20.14 ?  164 LEU   B HD22 1 
ATOM   6709 H  HD23 . LEU   B 1 164 ? 37.761 -35.648 -5.555  1.00 20.14 ?  164 LEU   B HD23 1 
ATOM   6710 N  N    . VAL   B 1 165 ? 38.090 -37.092 -10.570 1.00 15.69 ?  165 VAL   B N    1 
ATOM   6711 C  CA   . VAL   B 1 165 ? 37.431 -37.027 -11.871 1.00 16.84 ?  165 VAL   B CA   1 
ATOM   6712 C  C    . VAL   B 1 165 ? 36.514 -38.228 -12.058 1.00 18.67 ?  165 VAL   B C    1 
ATOM   6713 O  O    . VAL   B 1 165 ? 35.356 -38.094 -12.476 1.00 19.66 ?  165 VAL   B O    1 
ATOM   6714 C  CB   . VAL   B 1 165 ? 38.477 -36.937 -12.997 1.00 17.78 ?  165 VAL   B CB   1 
ATOM   6715 C  CG1  . VAL   B 1 165 ? 37.815 -37.044 -14.354 1.00 19.12 ?  165 VAL   B CG1  1 
ATOM   6716 C  CG2  . VAL   B 1 165 ? 39.257 -35.649 -12.891 1.00 17.87 ?  165 VAL   B CG2  1 
ATOM   6717 H  H    . VAL   B 1 165 ? 38.938 -37.233 -10.610 1.00 18.86 ?  165 VAL   B H    1 
ATOM   6718 H  HA   . VAL   B 1 165 ? 36.885 -36.226 -11.911 1.00 20.24 ?  165 VAL   B HA   1 
ATOM   6719 H  HB   . VAL   B 1 165 ? 39.107 -37.667 -12.907 1.00 21.37 ?  165 VAL   B HB   1 
ATOM   6720 H  HG11 . VAL   B 1 165 ? 38.431 -36.730 -15.032 1.00 22.98 ?  165 VAL   B HG11 1 
ATOM   6721 H  HG12 . VAL   B 1 165 ? 37.595 -37.975 -14.517 1.00 22.98 ?  165 VAL   B HG12 1 
ATOM   6722 H  HG13 . VAL   B 1 165 ? 37.011 -36.507 -14.357 1.00 22.98 ?  165 VAL   B HG13 1 
ATOM   6723 H  HG21 . VAL   B 1 165 ? 39.896 -35.598 -13.620 1.00 21.48 ?  165 VAL   B HG21 1 
ATOM   6724 H  HG22 . VAL   B 1 165 ? 38.642 -34.897 -12.943 1.00 21.48 ?  165 VAL   B HG22 1 
ATOM   6725 H  HG23 . VAL   B 1 165 ? 39.727 -35.626 -12.041 1.00 21.48 ?  165 VAL   B HG23 1 
ATOM   6726 N  N    . SER   B 1 166 ? 37.028 -39.427 -11.762 1.00 19.70 ?  166 SER   B N    1 
ATOM   6727 C  CA   . SER   B 1 166 ? 36.276 -40.640 -12.048 1.00 20.83 ?  166 SER   B CA   1 
ATOM   6728 C  C    . SER   B 1 166 ? 35.015 -40.729 -11.203 1.00 20.99 ?  166 SER   B C    1 
ATOM   6729 O  O    . SER   B 1 166 ? 34.047 -41.359 -11.627 1.00 22.19 ?  166 SER   B O    1 
ATOM   6730 C  CB   . SER   B 1 166 ? 37.143 -41.898 -11.883 1.00 21.99 ?  166 SER   B CB   1 
ATOM   6731 O  OG   . SER   B 1 166 ? 37.511 -42.119 -10.531 1.00 22.12 ?  166 SER   B OG   1 
ATOM   6732 H  H    . SER   B 1 166 ? 37.804 -39.555 -11.406 1.00 23.67 ?  166 SER   B H    1 
ATOM   6733 H  HA   . SER   B 1 166 ? 36.001 -40.610 -12.975 1.00 25.03 ?  166 SER   B HA   1 
ATOM   6734 H  HB2  . SER   B 1 166 ? 36.640 -42.664 -12.202 1.00 26.42 ?  166 SER   B HB2  1 
ATOM   6735 H  HB3  . SER   B 1 166 ? 37.950 -41.794 -12.413 1.00 26.42 ?  166 SER   B HB3  1 
ATOM   6736 H  HG   . SER   B 1 166 ? 37.950 -41.468 -10.245 1.00 26.58 ?  166 SER   B HG   1 
ATOM   6737 N  N    . SER   B 1 167 ? 34.992 -40.114 -10.021 1.00 19.67 ?  167 SER   B N    1 
ATOM   6738 C  CA   . SER   B 1 167 ? 33.836 -40.178 -9.135  1.00 19.02 ?  167 SER   B CA   1 
ATOM   6739 C  C    . SER   B 1 167 ? 32.918 -38.961 -9.233  1.00 18.69 ?  167 SER   B C    1 
ATOM   6740 O  O    . SER   B 1 167 ? 31.841 -38.966 -8.623  1.00 19.02 ?  167 SER   B O    1 
ATOM   6741 C  CB   . SER   B 1 167 ? 34.282 -40.356 -7.678  1.00 18.78 ?  167 SER   B CB   1 
ATOM   6742 O  OG   . SER   B 1 167 ? 34.949 -39.192 -7.201  1.00 18.86 ?  167 SER   B OG   1 
ATOM   6743 H  H    . SER   B 1 167 ? 35.640 -39.649 -9.709  1.00 23.63 ?  167 SER   B H    1 
ATOM   6744 H  HA   . SER   B 1 167 ? 33.308 -40.958 -9.378  1.00 22.85 ?  167 SER   B HA   1 
ATOM   6745 H  HB2  . SER   B 1 167 ? 33.496 -40.526 -7.131  1.00 22.56 ?  167 SER   B HB2  1 
ATOM   6746 H  HB3  . SER   B 1 167 ? 34.882 -41.121 -7.629  1.00 22.56 ?  167 SER   B HB3  1 
ATOM   6747 H  HG   . SER   B 1 167 ? 35.626 -39.054 -7.674  1.00 22.66 ?  167 SER   B HG   1 
ATOM   6748 N  N    . PHE   B 1 168 ? 33.297 -37.922 -9.981  1.00 18.48 ?  168 PHE   B N    1 
ATOM   6749 C  CA   . PHE   B 1 168 ? 32.465 -36.719 -10.034 1.00 17.95 ?  168 PHE   B CA   1 
ATOM   6750 C  C    . PHE   B 1 168 ? 31.143 -36.974 -10.753 1.00 15.83 ?  168 PHE   B C    1 
ATOM   6751 O  O    . PHE   B 1 168 ? 30.111 -36.369 -10.407 1.00 16.57 ?  168 PHE   B O    1 
ATOM   6752 C  CB   . PHE   B 1 168 ? 33.221 -35.581 -10.712 1.00 18.71 ?  168 PHE   B CB   1 
ATOM   6753 C  CG   . PHE   B 1 168 ? 32.414 -34.330 -10.840 1.00 18.71 ?  168 PHE   B CG   1 
ATOM   6754 C  CD1  . PHE   B 1 168 ? 32.103 -33.581 -9.713  1.00 20.11 ?  168 PHE   B CD1  1 
ATOM   6755 C  CD2  . PHE   B 1 168 ? 31.952 -33.908 -12.068 1.00 18.03 ?  168 PHE   B CD2  1 
ATOM   6756 C  CE1  . PHE   B 1 168 ? 31.344 -32.432 -9.809  1.00 20.55 ?  168 PHE   B CE1  1 
ATOM   6757 C  CE2  . PHE   B 1 168 ? 31.204 -32.739 -12.181 1.00 19.45 ?  168 PHE   B CE2  1 
ATOM   6758 C  CZ   . PHE   B 1 168 ? 30.893 -32.001 -11.046 1.00 19.74 ?  168 PHE   B CZ   1 
ATOM   6759 H  H    . PHE   B 1 168 ? 34.016 -37.885 -10.453 1.00 22.20 ?  168 PHE   B H    1 
ATOM   6760 H  HA   . PHE   B 1 168 ? 32.256 -36.441 -9.133  1.00 21.57 ?  168 PHE   B HA   1 
ATOM   6761 H  HB2  . PHE   B 1 168 ? 34.010 -35.370 -10.187 1.00 22.48 ?  168 PHE   B HB2  1 
ATOM   6762 H  HB3  . PHE   B 1 168 ? 33.480 -35.853 -11.604 1.00 22.48 ?  168 PHE   B HB3  1 
ATOM   6763 H  HD1  . PHE   B 1 168 ? 32.400 -33.867 -8.880  1.00 24.16 ?  168 PHE   B HD1  1 
ATOM   6764 H  HD2  . PHE   B 1 168 ? 32.159 -34.392 -12.831 1.00 21.67 ?  168 PHE   B HD2  1 
ATOM   6765 H  HE1  . PHE   B 1 168 ? 31.142 -31.941 -9.045  1.00 24.69 ?  168 PHE   B HE1  1 
ATOM   6766 H  HE2  . PHE   B 1 168 ? 30.895 -32.460 -13.016 1.00 23.38 ?  168 PHE   B HE2  1 
ATOM   6767 H  HZ   . PHE   B 1 168 ? 30.381 -31.225 -11.119 1.00 23.72 ?  168 PHE   B HZ   1 
ATOM   6768 N  N    . LEU   B 1 169 ? 31.160 -37.857 -11.749 1.00 16.18 ?  169 LEU   B N    1 
ATOM   6769 C  CA   . LEU   B 1 169 ? 29.976 -38.175 -12.537 1.00 18.37 ?  169 LEU   B CA   1 
ATOM   6770 C  C    . LEU   B 1 169 ? 29.970 -39.611 -13.036 1.00 21.20 ?  169 LEU   B C    1 
ATOM   6771 O  O    . LEU   B 1 169 ? 29.059 -40.023 -13.752 1.00 23.89 ?  169 LEU   B O    1 
ATOM   6772 C  CB   . LEU   B 1 169 ? 29.893 -37.251 -13.746 1.00 19.95 ?  169 LEU   B CB   1 
ATOM   6773 C  CG   . LEU   B 1 169 ? 28.654 -36.364 -13.836 1.00 23.32 ?  169 LEU   B CG   1 
ATOM   6774 C  CD1  . LEU   B 1 169 ? 28.619 -35.671 -15.183 1.00 24.45 ?  169 LEU   B CD1  1 
ATOM   6775 C  CD2  . LEU   B 1 169 ? 27.382 -37.158 -13.603 1.00 23.54 ?  169 LEU   B CD2  1 
ATOM   6776 O  OXT  . LEU   B 1 169 ? 30.883 -40.374 -12.754 1.00 22.20 -1 169 LEU   B OXT  1 
ATOM   6777 H  H    . LEU   B 1 169 ? 31.863 -38.292 -11.997 1.00 19.45 ?  169 LEU   B H    1 
ATOM   6778 H  HA   . LEU   B 1 169 ? 29.194 -38.039 -11.983 1.00 22.07 ?  169 LEU   B HA   1 
ATOM   6779 H  HB2  . LEU   B 1 169 ? 30.666 -36.668 -13.737 1.00 23.97 ?  169 LEU   B HB2  1 
ATOM   6780 H  HB3  . LEU   B 1 169 ? 29.912 -37.798 -14.548 1.00 23.97 ?  169 LEU   B HB3  1 
ATOM   6781 H  HG   . LEU   B 1 169 ? 28.708 -35.679 -13.151 1.00 28.02 ?  169 LEU   B HG   1 
ATOM   6782 H  HD11 . LEU   B 1 169 ? 27.840 -35.093 -15.219 1.00 29.37 ?  169 LEU   B HD11 1 
ATOM   6783 H  HD12 . LEU   B 1 169 ? 29.427 -35.146 -15.288 1.00 29.37 ?  169 LEU   B HD12 1 
ATOM   6784 H  HD13 . LEU   B 1 169 ? 28.565 -36.342 -15.881 1.00 29.37 ?  169 LEU   B HD13 1 
ATOM   6785 H  HD21 . LEU   B 1 169 ? 26.637 -36.696 -14.014 1.00 28.29 ?  169 LEU   B HD21 1 
ATOM   6786 H  HD22 . LEU   B 1 169 ? 27.484 -38.040 -14.000 1.00 28.29 ?  169 LEU   B HD22 1 
ATOM   6787 H  HD23 . LEU   B 1 169 ? 27.235 -37.243 -12.649 1.00 28.29 ?  169 LEU   B HD23 1 
HETATM 6788 N  N2   B A1A99 C 2 .   ? 14.698 -0.544  4.276   0.50 12.86 ?  201 A1A99 A N2   1 
HETATM 6789 C  C3   B A1A99 C 2 .   ? 14.371 -1.032  1.422   0.50 15.02 ?  201 A1A99 A C3   1 
HETATM 6790 C  C6   B A1A99 C 2 .   ? 14.823 0.516   3.401   0.50 12.94 ?  201 A1A99 A C6   1 
HETATM 6791 C  C9   B A1A99 C 2 .   ? 15.127 1.816   3.900   0.50 12.84 ?  201 A1A99 A C9   1 
HETATM 6792 C  C1   B A1A99 C 2 .   ? 11.833 -0.639  1.492   0.50 16.36 ?  201 A1A99 A C1   1 
HETATM 6793 C  C10  B A1A99 C 2 .   ? 15.345 3.132   3.372   0.50 13.64 ?  201 A1A99 A C10  1 
HETATM 6794 C  C11  B A1A99 C 2 .   ? 15.619 3.971   4.441   0.50 14.08 ?  201 A1A99 A C11  1 
HETATM 6795 C  C2   B A1A99 C 2 .   ? 12.967 -1.597  1.806   0.50 15.44 ?  201 A1A99 A C2   1 
HETATM 6796 C  C4   B A1A99 C 2 .   ? 14.436 -0.813  -0.090  0.50 15.84 ?  201 A1A99 A C4   1 
HETATM 6797 C  C5   B A1A99 C 2 .   ? 15.497 -2.092  1.716   0.50 14.55 ?  201 A1A99 A C5   1 
HETATM 6798 C  C7   B A1A99 C 2 .   ? 14.883 -0.275  5.590   0.50 12.60 ?  201 A1A99 A C7   1 
HETATM 6799 C  C8   B A1A99 C 2 .   ? 15.288 1.909   5.294   0.50 12.82 ?  201 A1A99 A C8   1 
HETATM 6800 N  N1   B A1A99 C 2 .   ? 14.652 0.292   2.055   0.50 14.17 ?  201 A1A99 A N1   1 
HETATM 6801 N  N3   B A1A99 C 2 .   ? 15.173 0.876   6.173   0.50 12.39 ?  201 A1A99 A N3   1 
HETATM 6802 N  N4   B A1A99 C 2 .   ? 15.582 3.223   5.637   0.50 13.61 ?  201 A1A99 A N4   1 
HETATM 6803 O  O1   B A1A99 C 2 .   ? 15.150 -2.874  2.847   0.50 14.31 ?  201 A1A99 A O1   1 
HETATM 6804 H  H2   B A1A99 C 2 .   ? 11.095 -0.565  2.306   0.50 19.67 ?  201 A1A99 A H2   1 
HETATM 6805 H  H1   B A1A99 C 2 .   ? 11.261 -0.964  0.614   0.50 19.67 ?  201 A1A99 A H1   1 
HETATM 6806 H  H3   B A1A99 C 2 .   ? 12.173 0.380   1.278   0.50 19.67 ?  201 A1A99 A H3   1 
HETATM 6807 H  H14  B A1A99 C 2 .   ? 15.310 3.435   2.338   0.50 16.40 ?  201 A1A99 A H14  1 
HETATM 6808 H  H15  B A1A99 C 2 .   ? 15.832 5.036   4.459   0.50 16.93 ?  201 A1A99 A H15  1 
HETATM 6809 H  H4   B A1A99 C 2 .   ? 12.927 -1.889  2.873   0.50 18.56 ?  201 A1A99 A H4   1 
HETATM 6810 H  H5   B A1A99 C 2 .   ? 12.791 -2.551  1.263   0.50 18.56 ?  201 A1A99 A H5   1 
HETATM 6811 H  H7   B A1A99 C 2 .   ? 14.206 -1.705  -0.686  0.50 19.04 ?  201 A1A99 A H7   1 
HETATM 6812 H  H8   B A1A99 C 2 .   ? 15.442 -0.490  -0.389  0.50 19.04 ?  201 A1A99 A H8   1 
HETATM 6813 H  H6   B A1A99 C 2 .   ? 13.750 -0.031  -0.445  0.50 19.04 ?  201 A1A99 A H6   1 
HETATM 6814 H  H9   B A1A99 C 2 .   ? 16.500 -1.637  1.843   0.50 17.50 ?  201 A1A99 A H9   1 
HETATM 6815 H  H10  B A1A99 C 2 .   ? 15.624 -2.736  0.810   0.50 17.50 ?  201 A1A99 A H10  1 
HETATM 6816 H  H13  B A1A99 C 2 .   ? 14.776 -1.128  6.275   0.50 15.15 ?  201 A1A99 A H13  1 
HETATM 6817 H  H12  B A1A99 C 2 .   ? 14.728 1.088   1.444   0.50 17.03 ?  201 A1A99 A H12  1 
HETATM 6818 H  H16  B A1A99 C 2 .   ? 15.743 3.578   6.568   0.50 16.36 ?  201 A1A99 A H16  1 
HETATM 6819 H  H11  B A1A99 C 2 .   ? 15.896 -2.857  3.439   0.50 17.21 ?  201 A1A99 A H11  1 
HETATM 6820 CL CL   B CL    D 3 .   ? 15.889 2.815   -1.048  0.50 20.95 ?  202 CL    A CL   1 
HETATM 6821 O  O    . HOH   E 4 .   ? 14.779 -4.737  20.564  1.00 44.22 ?  301 HOH   A O    1 
HETATM 6822 O  O    A HOH   E 4 .   ? 4.726  3.844   0.678   0.50 20.78 ?  302 HOH   A O    1 
HETATM 6823 O  O    . HOH   E 4 .   ? 28.887 0.447   -9.726  1.00 21.66 ?  303 HOH   A O    1 
HETATM 6824 O  O    . HOH   E 4 .   ? 18.589 -2.482  -16.407 1.00 43.63 ?  304 HOH   A O    1 
HETATM 6825 O  O    . HOH   E 4 .   ? 34.412 -1.895  12.526  1.00 38.63 ?  305 HOH   A O    1 
HETATM 6826 O  O    . HOH   E 4 .   ? 15.231 -12.259 18.770  1.00 39.59 ?  306 HOH   A O    1 
HETATM 6827 O  O    . HOH   E 4 .   ? 6.986  -8.227  11.908  1.00 22.88 ?  307 HOH   A O    1 
HETATM 6828 O  O    . HOH   E 4 .   ? 17.224 -18.125 15.071  1.00 27.64 ?  308 HOH   A O    1 
HETATM 6829 O  O    . HOH   E 4 .   ? 8.858  -12.017 17.283  1.00 45.94 ?  309 HOH   A O    1 
HETATM 6830 O  O    . HOH   E 4 .   ? 23.956 -15.753 -9.161  1.00 36.06 ?  310 HOH   A O    1 
HETATM 6831 O  O    . HOH   E 4 .   ? 18.990 -22.026 6.907   1.00 31.42 ?  311 HOH   A O    1 
HETATM 6832 O  O    B HOH   E 4 .   ? 14.789 3.384   17.234  0.50 30.70 ?  312 HOH   A O    1 
HETATM 6833 O  O    A HOH   E 4 .   ? 12.357 0.169   14.910  0.50 25.26 ?  313 HOH   A O    1 
HETATM 6834 O  O    . HOH   E 4 .   ? 9.126  -10.203 19.286  1.00 46.16 ?  314 HOH   A O    1 
HETATM 6835 O  O    . HOH   E 4 .   ? 42.470 10.553  5.168   1.00 20.48 ?  315 HOH   A O    1 
HETATM 6836 O  O    . HOH   E 4 .   ? 9.905  -21.425 5.754   1.00 18.71 ?  316 HOH   A O    1 
HETATM 6837 O  O    . HOH   E 4 .   ? 28.313 -0.211  -13.390 1.00 34.79 ?  317 HOH   A O    1 
HETATM 6838 O  O    . HOH   E 4 .   ? 14.465 -24.732 11.598  1.00 31.63 ?  318 HOH   A O    1 
HETATM 6839 O  O    . HOH   E 4 .   ? 14.797 -14.019 16.758  1.00 26.19 ?  319 HOH   A O    1 
HETATM 6840 O  O    . HOH   E 4 .   ? 26.806 11.366  1.693   1.00 16.09 ?  320 HOH   A O    1 
HETATM 6841 O  O    . HOH   E 4 .   ? 28.386 -6.313  19.582  1.00 44.16 ?  321 HOH   A O    1 
HETATM 6842 O  O    B HOH   E 4 .   ? 13.434 -1.090  -6.868  0.50 23.31 ?  322 HOH   A O    1 
HETATM 6843 O  O    . HOH   E 4 .   ? 0.794  -4.716  0.232   1.00 34.11 ?  323 HOH   A O    1 
HETATM 6844 O  O    . HOH   E 4 .   ? 19.926 -12.589 -8.889  1.00 27.58 ?  324 HOH   A O    1 
HETATM 6845 O  O    . HOH   E 4 .   ? 30.296 -13.321 -8.518  1.00 20.36 ?  325 HOH   A O    1 
HETATM 6846 O  O    . HOH   E 4 .   ? 34.012 -1.068  -8.934  1.00 27.21 ?  326 HOH   A O    1 
HETATM 6847 O  O    . HOH   E 4 .   ? 36.276 -5.077  -0.527  1.00 27.77 ?  327 HOH   A O    1 
HETATM 6848 O  O    A HOH   E 4 .   ? 17.536 -1.769  0.472   0.50 20.06 ?  328 HOH   A O    1 
HETATM 6849 O  O    . HOH   E 4 .   ? 26.524 -19.365 -1.805  1.00 14.23 ?  329 HOH   A O    1 
HETATM 6850 O  O    . HOH   E 4 .   ? 27.264 13.743  2.913   1.00 28.61 ?  330 HOH   A O    1 
HETATM 6851 O  O    . HOH   E 4 .   ? 7.652  -6.319  -6.561  1.00 42.13 ?  331 HOH   A O    1 
HETATM 6852 O  O    . HOH   E 4 .   ? 20.650 -19.724 -5.054  1.00 28.01 ?  332 HOH   A O    1 
HETATM 6853 O  O    A HOH   E 4 .   ? 15.251 3.898   17.864  0.50 31.46 ?  333 HOH   A O    1 
HETATM 6854 O  O    . HOH   E 4 .   ? 31.121 -18.185 7.814   1.00 20.36 ?  334 HOH   A O    1 
HETATM 6855 O  O    . HOH   E 4 .   ? 25.711 -0.858  -7.381  1.00 16.32 ?  335 HOH   A O    1 
HETATM 6856 O  O    A HOH   E 4 .   ? 14.683 -3.717  3.130   0.50 18.91 ?  336 HOH   A O    1 
HETATM 6857 O  O    . HOH   E 4 .   ? 37.591 2.794   10.206  1.00 28.64 ?  337 HOH   A O    1 
HETATM 6858 O  O    . HOH   E 4 .   ? 14.036 -4.954  17.470  1.00 27.17 ?  338 HOH   A O    1 
HETATM 6859 O  O    . HOH   E 4 .   ? 8.004  -12.713 -0.851  1.00 24.28 ?  339 HOH   A O    1 
HETATM 6860 O  O    . HOH   E 4 .   ? 14.089 -4.515  -11.864 1.00 36.94 ?  340 HOH   A O    1 
HETATM 6861 O  O    . HOH   E 4 .   ? 22.305 -19.346 11.366  1.00 33.62 ?  341 HOH   A O    1 
HETATM 6862 O  O    . HOH   E 4 .   ? 11.691 -10.838 -10.013 1.00 43.84 ?  342 HOH   A O    1 
HETATM 6863 O  O    . HOH   E 4 .   ? 38.111 -1.327  -1.999  1.00 18.90 ?  343 HOH   A O    1 
HETATM 6864 O  O    . HOH   E 4 .   ? 18.754 -19.415 13.631  1.00 32.96 ?  344 HOH   A O    1 
HETATM 6865 O  O    . HOH   E 4 .   ? 28.589 -10.655 -14.054 1.00 40.87 ?  345 HOH   A O    1 
HETATM 6866 O  O    . HOH   E 4 .   ? 38.591 4.979   6.928   1.00 15.78 ?  346 HOH   A O    1 
HETATM 6867 O  O    . HOH   E 4 .   ? 15.280 -21.640 14.256  1.00 18.53 ?  347 HOH   A O    1 
HETATM 6868 O  O    . HOH   E 4 .   ? 27.893 0.816   -7.164  1.00 14.46 ?  348 HOH   A O    1 
HETATM 6869 O  O    . HOH   E 4 .   ? 8.190  -21.514 4.037   1.00 51.19 ?  349 HOH   A O    1 
HETATM 6870 O  O    A HOH   E 4 .   ? 14.324 0.505   6.839   0.50 24.62 ?  350 HOH   A O    1 
HETATM 6871 O  O    . HOH   E 4 .   ? 44.334 7.125   6.427   1.00 27.43 ?  351 HOH   A O    1 
HETATM 6872 O  O    . HOH   E 4 .   ? 17.206 -17.864 -4.993  1.00 28.31 ?  352 HOH   A O    1 
HETATM 6873 O  O    . HOH   E 4 .   ? 38.322 10.148  7.131   1.00 44.29 ?  353 HOH   A O    1 
HETATM 6874 O  O    . HOH   E 4 .   ? 3.623  -9.636  9.924   1.00 38.93 ?  354 HOH   A O    1 
HETATM 6875 O  O    . HOH   E 4 .   ? 31.721 8.223   14.816  1.00 24.47 ?  355 HOH   A O    1 
HETATM 6876 O  O    . HOH   E 4 .   ? 37.374 11.936  4.956   1.00 31.56 ?  356 HOH   A O    1 
HETATM 6877 O  O    . HOH   E 4 .   ? 42.546 4.252   5.280   1.00 31.26 ?  357 HOH   A O    1 
HETATM 6878 O  O    . HOH   E 4 .   ? 35.862 -12.730 6.792   1.00 15.77 ?  358 HOH   A O    1 
HETATM 6879 O  O    . HOH   E 4 .   ? 24.402 3.537   -1.786  1.00 14.61 ?  359 HOH   A O    1 
HETATM 6880 O  O    . HOH   E 4 .   ? 24.063 -2.156  -2.084  1.00 10.88 ?  360 HOH   A O    1 
HETATM 6881 O  O    . HOH   E 4 .   ? 37.277 -2.935  9.648   1.00 40.80 ?  361 HOH   A O    1 
HETATM 6882 O  O    . HOH   E 4 .   ? 39.768 -1.012  -5.221  1.00 20.05 ?  362 HOH   A O    1 
HETATM 6883 O  O    . HOH   E 4 .   ? 30.899 6.269   -12.312 1.00 28.61 ?  363 HOH   A O    1 
HETATM 6884 O  O    . HOH   E 4 .   ? 22.356 5.349   19.025  1.00 46.61 ?  364 HOH   A O    1 
HETATM 6885 O  O    . HOH   E 4 .   ? 13.581 -15.278 -7.419  1.00 27.45 ?  365 HOH   A O    1 
HETATM 6886 O  O    . HOH   E 4 .   ? 22.755 12.502  1.664   1.00 14.58 ?  366 HOH   A O    1 
HETATM 6887 O  O    . HOH   E 4 .   ? 17.057 -19.342 4.921   1.00 15.69 ?  367 HOH   A O    1 
HETATM 6888 O  O    . HOH   E 4 .   ? 43.914 8.437   -3.141  1.00 26.10 ?  368 HOH   A O    1 
HETATM 6889 O  O    . HOH   E 4 .   ? 14.401 -21.273 -4.249  1.00 29.39 ?  369 HOH   A O    1 
HETATM 6890 O  O    . HOH   E 4 .   ? 31.866 -9.369  -6.654  1.00 22.15 ?  370 HOH   A O    1 
HETATM 6891 O  O    . HOH   E 4 .   ? 31.129 -13.977 -2.465  1.00 13.63 ?  371 HOH   A O    1 
HETATM 6892 O  O    B HOH   E 4 .   ? 21.189 2.605   -0.009  0.50 20.17 ?  372 HOH   A O    1 
HETATM 6893 O  O    . HOH   E 4 .   ? 33.735 -7.189  4.271   1.00 16.72 ?  373 HOH   A O    1 
HETATM 6894 O  O    . HOH   E 4 .   ? 30.839 3.069   8.274   1.00 12.31 ?  374 HOH   A O    1 
HETATM 6895 O  O    . HOH   E 4 .   ? 22.688 -11.984 21.919  1.00 44.68 ?  375 HOH   A O    1 
HETATM 6896 O  O    A HOH   E 4 .   ? 21.283 -2.443  -2.029  0.50 11.29 ?  376 HOH   A O    1 
HETATM 6897 O  O    . HOH   E 4 .   ? 27.590 -10.676 14.077  1.00 17.73 ?  377 HOH   A O    1 
HETATM 6898 O  O    . HOH   E 4 .   ? 18.516 9.373   8.990   1.00 22.47 ?  378 HOH   A O    1 
HETATM 6899 O  O    A HOH   E 4 .   ? 20.115 4.502   -7.512  0.50 16.53 ?  379 HOH   A O    1 
HETATM 6900 O  O    . HOH   E 4 .   ? 21.963 -21.987 8.411   1.00 27.84 ?  380 HOH   A O    1 
HETATM 6901 O  O    . HOH   E 4 .   ? 43.377 7.831   2.657   1.00 25.10 ?  381 HOH   A O    1 
HETATM 6902 O  O    B HOH   E 4 .   ? 12.268 6.665   10.358  0.50 32.63 ?  382 HOH   A O    1 
HETATM 6903 O  O    A HOH   E 4 .   ? -0.430 -3.176  3.161   0.50 31.37 ?  383 HOH   A O    1 
HETATM 6904 O  O    A HOH   E 4 .   ? 18.994 -0.719  -1.597  0.50 12.39 ?  384 HOH   A O    1 
HETATM 6905 O  O    . HOH   E 4 .   ? 26.951 4.123   -0.638  1.00 12.45 ?  385 HOH   A O    1 
HETATM 6906 O  O    . HOH   E 4 .   ? 21.232 10.245  15.027  1.00 35.31 ?  386 HOH   A O    1 
HETATM 6907 O  O    . HOH   E 4 .   ? 24.781 -17.603 12.767  1.00 24.45 ?  387 HOH   A O    1 
HETATM 6908 O  O    . HOH   E 4 .   ? 16.541 -22.108 1.044   1.00 30.43 ?  388 HOH   A O    1 
HETATM 6909 O  O    . HOH   E 4 .   ? 31.801 -7.302  -9.861  1.00 21.32 ?  389 HOH   A O    1 
HETATM 6910 O  O    . HOH   E 4 .   ? 24.369 -7.829  14.492  1.00 17.49 ?  390 HOH   A O    1 
HETATM 6911 O  O    . HOH   E 4 .   ? 6.503  -5.650  11.215  1.00 21.21 ?  391 HOH   A O    1 
HETATM 6912 O  O    . HOH   E 4 .   ? 16.015 2.200   24.946  1.00 47.56 ?  392 HOH   A O    1 
HETATM 6913 O  O    B HOH   E 4 .   ? 7.243  1.485   7.398   0.50 37.59 ?  393 HOH   A O    1 
HETATM 6914 O  O    B HOH   E 4 .   ? 22.744 5.782   -1.666  0.50 20.54 ?  394 HOH   A O    1 
HETATM 6915 O  O    A HOH   E 4 .   ? 21.380 3.107   -0.319  0.50 9.50  ?  395 HOH   A O    1 
HETATM 6916 O  O    B HOH   E 4 .   ? 21.282 -2.099  -2.506  0.50 17.00 ?  396 HOH   A O    1 
HETATM 6917 O  O    . HOH   E 4 .   ? 37.582 -2.005  5.726   1.00 26.57 ?  397 HOH   A O    1 
HETATM 6918 O  O    . HOH   E 4 .   ? 32.851 -9.280  5.951   1.00 20.10 ?  398 HOH   A O    1 
HETATM 6919 O  O    . HOH   E 4 .   ? 6.729  -3.389  12.905  1.00 32.26 ?  399 HOH   A O    1 
HETATM 6920 O  O    A HOH   E 4 .   ? 11.094 1.470   12.798  0.50 19.22 ?  400 HOH   A O    1 
HETATM 6921 O  O    . HOH   E 4 .   ? 27.440 2.331   18.758  1.00 32.43 ?  401 HOH   A O    1 
HETATM 6922 O  O    . HOH   E 4 .   ? 23.452 11.353  4.135   1.00 12.48 ?  402 HOH   A O    1 
HETATM 6923 O  O    . HOH   E 4 .   ? 30.781 1.841   16.708  1.00 21.96 ?  403 HOH   A O    1 
HETATM 6924 O  O    A HOH   E 4 .   ? 15.849 -1.010  5.305   0.50 29.94 ?  404 HOH   A O    1 
HETATM 6925 O  O    A HOH   E 4 .   ? 13.336 -1.488  -6.485  0.50 14.57 ?  405 HOH   A O    1 
HETATM 6926 O  O    . HOH   E 4 .   ? 15.504 11.825  7.864   1.00 30.94 ?  406 HOH   A O    1 
HETATM 6927 O  O    A HOH   E 4 .   ? -0.579 -8.580  2.457   0.50 32.46 ?  407 HOH   A O    1 
HETATM 6928 O  O    . HOH   E 4 .   ? 30.177 -10.168 13.015  1.00 21.68 ?  408 HOH   A O    1 
HETATM 6929 O  O    . HOH   E 4 .   ? 27.428 -6.153  -14.088 1.00 37.22 ?  409 HOH   A O    1 
HETATM 6930 O  O    B HOH   E 4 .   ? 18.495 -1.577  -1.166  0.50 32.36 ?  410 HOH   A O    1 
HETATM 6931 O  O    B HOH   E 4 .   ? 11.847 -1.725  -3.206  0.50 16.88 ?  411 HOH   A O    1 
HETATM 6932 O  O    . HOH   E 4 .   ? 20.628 -20.068 2.764   1.00 18.14 ?  412 HOH   A O    1 
HETATM 6933 O  O    . HOH   E 4 .   ? 40.947 -8.250  -6.800  1.00 36.65 ?  413 HOH   A O    1 
HETATM 6934 O  O    A HOH   E 4 .   ? 24.604 2.005   -6.965  0.50 14.45 ?  414 HOH   A O    1 
HETATM 6935 O  O    . HOH   E 4 .   ? 41.657 1.548   4.902   1.00 39.10 ?  415 HOH   A O    1 
HETATM 6936 O  O    . HOH   E 4 .   ? 16.256 16.691  8.755   1.00 30.43 ?  416 HOH   A O    1 
HETATM 6937 O  O    . HOH   E 4 .   ? 19.595 -11.159 24.111  1.00 63.20 ?  417 HOH   A O    1 
HETATM 6938 O  O    . HOH   E 4 .   ? 14.483 -0.462  -12.061 1.00 29.10 ?  418 HOH   A O    1 
HETATM 6939 O  O    . HOH   E 4 .   ? 32.606 -10.672 3.175   1.00 30.90 ?  419 HOH   A O    1 
HETATM 6940 O  O    . HOH   E 4 .   ? 23.975 -20.309 -1.352  1.00 16.39 ?  420 HOH   A O    1 
HETATM 6941 O  O    . HOH   E 4 .   ? 14.136 -23.140 7.457   1.00 19.17 ?  421 HOH   A O    1 
HETATM 6942 O  O    . HOH   E 4 .   ? 32.683 -4.332  -9.905  1.00 27.73 ?  422 HOH   A O    1 
HETATM 6943 O  O    . HOH   E 4 .   ? 35.100 -5.230  -3.129  1.00 18.09 ?  423 HOH   A O    1 
HETATM 6944 O  O    . HOH   E 4 .   ? 16.072 7.031   2.968   1.00 20.13 ?  424 HOH   A O    1 
HETATM 6945 O  O    . HOH   E 4 .   ? 15.196 -8.091  -9.758  1.00 24.26 ?  425 HOH   A O    1 
HETATM 6946 O  O    . HOH   E 4 .   ? 30.458 -12.992 13.512  1.00 20.05 ?  426 HOH   A O    1 
HETATM 6947 O  O    . HOH   E 4 .   ? 44.971 -0.608  2.951   1.00 41.09 ?  427 HOH   A O    1 
HETATM 6948 O  O    . HOH   E 4 .   ? 10.447 -13.792 -1.674  1.00 18.36 ?  428 HOH   A O    1 
HETATM 6949 O  O    . HOH   E 4 .   ? 16.278 -14.225 20.310  1.00 43.73 ?  429 HOH   A O    1 
HETATM 6950 O  O    . HOH   E 4 .   ? 36.808 -4.968  5.367   1.00 25.77 ?  430 HOH   A O    1 
HETATM 6951 O  O    B HOH   E 4 .   ? 10.965 2.341   12.090  0.50 27.53 ?  431 HOH   A O    1 
HETATM 6952 O  O    . HOH   E 4 .   ? 5.230  2.594   5.266   1.00 36.53 ?  432 HOH   A O    1 
HETATM 6953 O  O    . HOH   E 4 .   ? 10.408 -22.163 -1.297  1.00 49.65 ?  433 HOH   A O    1 
HETATM 6954 O  O    . HOH   E 4 .   ? -1.379 -5.110  7.714   1.00 46.18 ?  434 HOH   A O    1 
HETATM 6955 O  O    A HOH   E 4 .   ? 11.108 -0.446  1.978   0.50 30.09 ?  435 HOH   A O    1 
HETATM 6956 O  O    . HOH   E 4 .   ? 27.182 -3.181  19.396  1.00 35.38 ?  436 HOH   A O    1 
HETATM 6957 O  O    . HOH   E 4 .   ? 22.649 8.019   18.386  1.00 48.74 ?  437 HOH   A O    1 
HETATM 6958 O  O    A HOH   E 4 .   ? 18.896 1.982   -0.718  0.50 11.48 ?  438 HOH   A O    1 
HETATM 6959 O  O    A HOH   E 4 .   ? 24.114 3.920   -4.890  0.50 17.34 ?  439 HOH   A O    1 
HETATM 6960 O  O    . HOH   E 4 .   ? 21.722 -13.922 -8.158  1.00 44.19 ?  440 HOH   A O    1 
HETATM 6961 O  O    . HOH   E 4 .   ? 21.337 -9.286  21.343  1.00 44.16 ?  441 HOH   A O    1 
HETATM 6962 O  O    A HOH   E 4 .   ? 16.289 2.893   -1.402  0.50 18.42 ?  442 HOH   A O    1 
HETATM 6963 O  O    . HOH   E 4 .   ? 37.796 -8.849  -3.532  1.00 25.67 ?  443 HOH   A O    1 
HETATM 6964 O  O    . HOH   E 4 .   ? 23.657 -8.075  17.095  1.00 22.06 ?  444 HOH   A O    1 
HETATM 6965 O  O    . HOH   E 4 .   ? 11.810 -10.822 17.079  1.00 26.93 ?  445 HOH   A O    1 
HETATM 6966 O  O    . HOH   E 4 .   ? 20.638 -17.827 24.852  1.00 52.87 ?  446 HOH   A O    1 
HETATM 6967 O  O    . HOH   E 4 .   ? 23.387 -21.005 1.299   1.00 18.30 ?  447 HOH   A O    1 
HETATM 6968 O  O    . HOH   E 4 .   ? 18.486 4.935   -15.115 1.00 50.45 ?  448 HOH   A O    1 
HETATM 6969 O  O    . HOH   E 4 .   ? 34.479 -8.092  -0.544  1.00 30.78 ?  449 HOH   A O    1 
HETATM 6970 O  O    . HOH   E 4 .   ? 30.611 14.778  2.822   1.00 18.94 ?  450 HOH   A O    1 
HETATM 6971 O  O    A HOH   E 4 .   ? 23.221 7.470   -3.203  0.50 22.78 ?  451 HOH   A O    1 
HETATM 6972 O  O    . HOH   E 4 .   ? 18.487 -16.109 16.450  1.00 36.92 ?  452 HOH   A O    1 
HETATM 6973 O  O    B HOH   E 4 .   ? 23.309 8.013   -3.317  0.50 31.03 ?  453 HOH   A O    1 
HETATM 6974 O  O    . HOH   E 4 .   ? 31.379 -12.827 0.017   1.00 19.40 ?  454 HOH   A O    1 
HETATM 6975 O  O    A HOH   E 4 .   ? 9.443  -16.389 -1.958  0.50 32.13 ?  455 HOH   A O    1 
HETATM 6976 O  O    . HOH   E 4 .   ? 27.734 6.918   -6.385  1.00 33.29 ?  456 HOH   A O    1 
HETATM 6977 O  O    . HOH   E 4 .   ? 21.666 -14.778 17.957  1.00 51.82 ?  457 HOH   A O    1 
HETATM 6978 O  O    A HOH   E 4 .   ? 14.072 -0.403  3.500   0.50 29.90 ?  458 HOH   A O    1 
HETATM 6979 O  O    B HOH   E 4 .   ? 11.302 0.665   14.608  0.50 33.04 ?  459 HOH   A O    1 
HETATM 6980 O  O    . HOH   E 4 .   ? 29.932 -16.104 10.672  1.00 36.95 ?  460 HOH   A O    1 
HETATM 6981 O  O    B HOH   E 4 .   ? 18.583 1.400   -0.345  0.50 19.20 ?  461 HOH   A O    1 
HETATM 6982 O  O    . HOH   E 4 .   ? 29.761 -2.046  -12.747 1.00 46.19 ?  462 HOH   A O    1 
HETATM 6983 O  O    . HOH   E 4 .   ? 25.454 8.285   -4.825  1.00 21.73 ?  463 HOH   A O    1 
HETATM 6984 O  O    . HOH   E 4 .   ? 19.984 -17.394 -5.049  1.00 25.62 ?  464 HOH   A O    1 
HETATM 6985 O  O    . HOH   E 4 .   ? 32.484 -16.020 10.892  1.00 35.32 ?  465 HOH   A O    1 
HETATM 6986 O  O    . HOH   E 4 .   ? 24.896 5.626   20.750  1.00 52.86 ?  466 HOH   A O    1 
HETATM 6987 O  O    B HOH   E 4 .   ? 13.016 2.444   -0.248  0.50 25.41 ?  467 HOH   A O    1 
HETATM 6988 O  O    . HOH   E 4 .   ? 23.297 -22.381 -3.344  1.00 34.73 ?  468 HOH   A O    1 
HETATM 6989 O  O    . HOH   E 4 .   ? 24.599 14.539  7.863   1.00 35.93 ?  469 HOH   A O    1 
HETATM 6990 O  O    . HOH   E 4 .   ? 26.911 11.577  -1.244  1.00 27.86 ?  470 HOH   A O    1 
HETATM 6991 O  O    . HOH   E 4 .   ? 15.748 -21.541 3.706   1.00 22.75 ?  471 HOH   A O    1 
HETATM 6992 O  O    A HOH   E 4 .   ? 21.984 5.226   -5.804  0.50 22.17 ?  472 HOH   A O    1 
HETATM 6993 O  O    . HOH   E 4 .   ? 23.498 13.697  5.542   1.00 19.14 ?  473 HOH   A O    1 
HETATM 6994 O  O    . HOH   E 4 .   ? 39.722 -7.098  -3.537  1.00 47.63 ?  474 HOH   A O    1 
HETATM 6995 O  O    . HOH   E 4 .   ? 18.742 10.739  11.371  1.00 32.89 ?  475 HOH   A O    1 
HETATM 6996 O  O    . HOH   E 4 .   ? 27.564 -11.397 16.575  1.00 37.12 ?  476 HOH   A O    1 
HETATM 6997 O  O    . HOH   E 4 .   ? 25.883 10.790  -3.632  1.00 22.90 ?  477 HOH   A O    1 
HETATM 6998 O  O    . HOH   E 4 .   ? 12.011 -13.494 16.366  1.00 48.88 ?  478 HOH   A O    1 
HETATM 6999 O  O    . HOH   E 4 .   ? 12.360 1.534   17.269  1.00 39.96 ?  479 HOH   A O    1 
HETATM 7000 O  O    . HOH   E 4 .   ? 23.185 11.858  -3.997  1.00 20.16 ?  480 HOH   A O    1 
HETATM 7001 O  O    B HOH   E 4 .   ? 11.261 0.500   -1.912  0.50 27.41 ?  481 HOH   A O    1 
HETATM 7002 O  O    . HOH   E 4 .   ? 11.122 -15.143 -6.108  1.00 32.78 ?  482 HOH   A O    1 
HETATM 7003 O  O    . HOH   E 4 .   ? 35.181 7.451   12.247  1.00 49.66 ?  483 HOH   A O    1 
HETATM 7004 O  O    . HOH   E 4 .   ? 28.943 8.923   17.503  1.00 37.93 ?  484 HOH   A O    1 
HETATM 7005 O  O    . HOH   E 4 .   ? 16.842 -20.614 16.223  1.00 28.70 ?  485 HOH   A O    1 
HETATM 7006 O  O    . HOH   E 4 .   ? 18.205 -16.331 -8.792  1.00 44.92 ?  486 HOH   A O    1 
HETATM 7007 O  O    B HOH   E 4 .   ? 10.774 -1.541  -5.797  0.50 22.73 ?  487 HOH   A O    1 
HETATM 7008 O  O    . HOH   E 4 .   ? 17.471 -18.746 19.785  1.00 47.53 ?  488 HOH   A O    1 
HETATM 7009 O  O    B HOH   E 4 .   ? 5.269  4.208   0.746   0.50 33.43 ?  489 HOH   A O    1 
HETATM 7010 O  O    . HOH   E 4 .   ? 15.710 -17.210 -6.955  1.00 31.90 ?  490 HOH   A O    1 
HETATM 7011 O  O    . HOH   E 4 .   ? 14.106 -10.335 -10.895 1.00 35.06 ?  491 HOH   A O    1 
HETATM 7012 O  O    . HOH   E 4 .   ? 30.976 0.735   19.129  1.00 41.40 ?  492 HOH   A O    1 
HETATM 7013 O  O    . HOH   E 4 .   ? 41.032 -3.997  -0.321  1.00 37.08 ?  493 HOH   A O    1 
HETATM 7014 O  O    . HOH   E 4 .   ? 28.575 -4.711  -12.313 1.00 39.09 ?  494 HOH   A O    1 
HETATM 7015 O  O    . HOH   E 4 .   ? 44.483 10.432  -1.680  1.00 33.48 ?  495 HOH   A O    1 
HETATM 7016 O  O    . HOH   E 4 .   ? 23.312 -12.893 19.360  1.00 44.48 ?  496 HOH   A O    1 
HETATM 7017 O  O    . HOH   E 4 .   ? 20.546 -15.960 -7.397  1.00 30.02 ?  497 HOH   A O    1 
HETATM 7018 O  O    . HOH   E 4 .   ? 31.458 -0.594  -10.589 1.00 29.15 ?  498 HOH   A O    1 
HETATM 7019 O  O    . HOH   E 4 .   ? 41.700 9.368   -4.034  1.00 32.89 ?  499 HOH   A O    1 
HETATM 7020 O  O    . HOH   E 4 .   ? 28.725 -7.960  -15.262 1.00 48.34 ?  500 HOH   A O    1 
HETATM 7021 O  O    . HOH   E 4 .   ? 39.227 2.396   7.525   1.00 31.74 ?  501 HOH   A O    1 
HETATM 7022 O  O    . HOH   E 4 .   ? 18.624 -23.255 1.923   1.00 43.44 ?  502 HOH   A O    1 
HETATM 7023 O  O    . HOH   E 4 .   ? 8.126  -2.997  -5.700  1.00 49.47 ?  503 HOH   A O    1 
HETATM 7024 O  O    . HOH   E 4 .   ? 16.022 -6.797  -11.819 1.00 44.88 ?  504 HOH   A O    1 
HETATM 7025 O  O    . HOH   E 4 .   ? 40.511 -0.258  -7.844  1.00 33.59 ?  505 HOH   A O    1 
HETATM 7026 O  O    . HOH   E 4 .   ? 20.089 -22.406 4.204   1.00 29.81 ?  506 HOH   A O    1 
HETATM 7027 O  O    . HOH   E 4 .   ? 14.092 -25.407 8.936   1.00 31.92 ?  507 HOH   A O    1 
HETATM 7028 O  O    . HOH   E 4 .   ? 16.207 -23.419 5.790   1.00 30.36 ?  508 HOH   A O    1 
HETATM 7029 O  O    . HOH   E 4 .   ? 30.699 5.833   -14.808 1.00 36.51 ?  509 HOH   A O    1 
HETATM 7030 O  O    B HOH   E 4 .   ? 10.443 4.857   11.708  0.50 37.11 ?  510 HOH   A O    1 
HETATM 7031 O  O    . HOH   E 4 .   ? 30.740 -5.805  -11.858 1.00 48.99 ?  511 HOH   A O    1 
HETATM 7032 O  O    . HOH   E 4 .   ? 23.199 -23.827 1.678   1.00 30.54 ?  512 HOH   A O    1 
HETATM 7033 O  O    . HOH   E 4 .   ? 37.472 -6.701  7.502   1.00 24.07 ?  513 HOH   A O    1 
HETATM 7034 O  O    . HOH   E 4 .   ? 39.619 -0.018  6.532   1.00 30.18 ?  514 HOH   A O    1 
HETATM 7035 O  O    . HOH   E 4 .   ? 29.006 14.346  0.909   1.00 48.78 ?  515 HOH   A O    1 
HETATM 7036 O  O    . HOH   E 4 .   ? 38.072 13.925  6.704   1.00 51.73 ?  516 HOH   A O    1 
HETATM 7037 O  O    . HOH   E 4 .   ? 36.584 -6.465  10.140  1.00 42.10 ?  517 HOH   A O    1 
HETATM 7038 O  O    . HOH   E 4 .   ? 14.905 8.430   4.971   1.00 36.66 ?  518 HOH   A O    1 
HETATM 7039 O  O    . HOH   E 4 .   ? 22.083 -24.080 4.505   1.00 25.60 ?  519 HOH   A O    1 
HETATM 7040 O  O    . HOH   E 4 .   ? 17.451 -6.796  -14.220 1.00 41.95 ?  520 HOH   A O    1 
HETATM 7041 O  O    . HOH   E 4 .   ? 24.091 9.096   -7.202  1.00 35.14 ?  521 HOH   A O    1 
HETATM 7042 O  O    . HOH   E 4 .   ? 16.329 -21.210 18.787  1.00 36.28 ?  522 HOH   A O    1 
HETATM 7043 O  O    . HOH   E 4 .   ? 16.015 -12.405 27.432  1.00 42.96 ?  523 HOH   A O    1 
HETATM 7044 O  O    . HOH   E 4 .   ? 14.684 -22.800 19.858  1.00 34.48 ?  524 HOH   A O    1 
HETATM 7045 O  O    . HOH   F 4 .   ? 29.906 -22.473 5.478   1.00 20.36 ?  201 HOH   B O    1 
HETATM 7046 O  O    . HOH   F 4 .   ? 41.768 -35.968 -17.317 1.00 30.86 ?  202 HOH   B O    1 
HETATM 7047 O  O    . HOH   F 4 .   ? 29.799 -34.150 -0.463  1.00 33.67 ?  203 HOH   B O    1 
HETATM 7048 O  O    . HOH   F 4 .   ? 27.779 -29.206 -1.942  1.00 35.48 ?  204 HOH   B O    1 
HETATM 7049 O  O    . HOH   F 4 .   ? 53.027 -13.401 -20.379 1.00 35.82 ?  205 HOH   B O    1 
HETATM 7050 O  O    . HOH   F 4 .   ? 38.008 -39.510 -0.281  1.00 42.51 ?  206 HOH   B O    1 
HETATM 7051 O  O    . HOH   F 4 .   ? 29.964 -26.340 4.035   1.00 27.53 ?  207 HOH   B O    1 
HETATM 7052 O  O    . HOH   F 4 .   ? 59.247 -18.721 6.775   1.00 37.72 ?  208 HOH   B O    1 
HETATM 7053 O  O    . HOH   F 4 .   ? 49.456 -22.753 -19.778 1.00 49.80 ?  209 HOH   B O    1 
HETATM 7054 O  O    . HOH   F 4 .   ? 41.480 -7.790  5.473   1.00 37.17 ?  210 HOH   B O    1 
HETATM 7055 O  O    . HOH   F 4 .   ? 27.883 -41.866 -15.148 1.00 36.19 ?  211 HOH   B O    1 
HETATM 7056 O  O    . HOH   F 4 .   ? 47.481 -7.418  -3.979  1.00 42.40 ?  212 HOH   B O    1 
HETATM 7057 O  O    . HOH   F 4 .   ? 48.121 -6.980  15.520  1.00 41.01 ?  213 HOH   B O    1 
HETATM 7058 O  O    . HOH   F 4 .   ? 57.794 -24.509 4.996   1.00 37.97 ?  214 HOH   B O    1 
HETATM 7059 O  O    . HOH   F 4 .   ? 58.321 -12.895 8.389   1.00 33.35 ?  215 HOH   B O    1 
HETATM 7060 O  O    . HOH   F 4 .   ? 56.492 -19.749 7.133   1.00 32.53 ?  216 HOH   B O    1 
HETATM 7061 O  O    . HOH   F 4 .   ? 30.272 -41.048 -8.212  1.00 16.71 ?  217 HOH   B O    1 
HETATM 7062 O  O    . HOH   F 4 .   ? 54.559 -9.358  -8.833  1.00 18.68 ?  218 HOH   B O    1 
HETATM 7063 O  O    . HOH   F 4 .   ? 55.504 -16.500 -14.362 1.00 34.69 ?  219 HOH   B O    1 
HETATM 7064 O  O    . HOH   F 4 .   ? 50.326 -3.342  7.129   1.00 35.77 ?  220 HOH   B O    1 
HETATM 7065 O  O    . HOH   F 4 .   ? 56.790 -30.781 -7.792  1.00 31.43 ?  221 HOH   B O    1 
HETATM 7066 O  O    . HOH   F 4 .   ? 44.519 -7.235  2.065   1.00 33.73 ?  222 HOH   B O    1 
HETATM 7067 O  O    . HOH   F 4 .   ? 50.841 -6.116  0.142   1.00 26.85 ?  223 HOH   B O    1 
HETATM 7068 O  O    . HOH   F 4 .   ? 48.580 -36.536 -15.539 1.00 42.82 ?  224 HOH   B O    1 
HETATM 7069 O  O    . HOH   F 4 .   ? 45.070 -43.545 -10.657 1.00 27.58 ?  225 HOH   B O    1 
HETATM 7070 O  O    . HOH   F 4 .   ? 40.664 -16.061 14.093  1.00 24.17 ?  226 HOH   B O    1 
HETATM 7071 O  O    . HOH   F 4 .   ? 45.231 -34.969 6.814   1.00 39.34 ?  227 HOH   B O    1 
HETATM 7072 O  O    . HOH   F 4 .   ? 30.920 -28.815 4.229   1.00 27.24 ?  228 HOH   B O    1 
HETATM 7073 O  O    . HOH   F 4 .   ? 57.508 -16.260 -12.225 1.00 19.11 ?  229 HOH   B O    1 
HETATM 7074 O  O    . HOH   F 4 .   ? 34.607 -36.417 -7.253  1.00 18.02 ?  230 HOH   B O    1 
HETATM 7075 O  O    . HOH   F 4 .   ? 46.446 -1.605  13.225  1.00 30.06 ?  231 HOH   B O    1 
HETATM 7076 O  O    . HOH   F 4 .   ? 41.568 -39.171 -14.983 1.00 21.63 ?  232 HOH   B O    1 
HETATM 7077 O  O    . HOH   F 4 .   ? 34.970 -24.675 13.820  1.00 29.06 ?  233 HOH   B O    1 
HETATM 7078 O  O    . HOH   F 4 .   ? 41.469 -9.667  13.029  1.00 21.62 ?  234 HOH   B O    1 
HETATM 7079 O  O    . HOH   F 4 .   ? 39.399 -10.907 6.096   1.00 26.10 ?  235 HOH   B O    1 
HETATM 7080 O  O    . HOH   F 4 .   ? 57.273 -26.832 -7.663  1.00 40.74 ?  236 HOH   B O    1 
HETATM 7081 O  O    . HOH   F 4 .   ? 37.149 -19.768 -18.137 1.00 37.54 ?  237 HOH   B O    1 
HETATM 7082 O  O    . HOH   F 4 .   ? 51.751 -6.530  4.423   1.00 20.00 ?  238 HOH   B O    1 
HETATM 7083 O  O    . HOH   F 4 .   ? 35.162 -8.004  -3.061  1.00 18.68 ?  239 HOH   B O    1 
HETATM 7084 O  O    . HOH   F 4 .   ? 28.453 -19.663 -13.152 1.00 23.88 ?  240 HOH   B O    1 
HETATM 7085 O  O    . HOH   F 4 .   ? 36.044 -43.318 -8.544  1.00 32.88 ?  241 HOH   B O    1 
HETATM 7086 O  O    . HOH   F 4 .   ? 50.818 -12.994 -0.500  1.00 12.06 ?  242 HOH   B O    1 
HETATM 7087 O  O    . HOH   F 4 .   ? 32.861 -43.829 -11.400 1.00 19.61 ?  243 HOH   B O    1 
HETATM 7088 O  O    . HOH   F 4 .   ? 41.929 -23.587 9.259   1.00 17.03 ?  244 HOH   B O    1 
HETATM 7089 O  O    . HOH   F 4 .   ? 57.719 -24.397 -3.857  1.00 22.46 ?  245 HOH   B O    1 
HETATM 7090 O  O    . HOH   F 4 .   ? 42.722 -22.904 3.817   1.00 11.84 ?  246 HOH   B O    1 
HETATM 7091 O  O    . HOH   F 4 .   ? 25.448 -25.977 -1.353  1.00 32.15 ?  247 HOH   B O    1 
HETATM 7092 O  O    . HOH   F 4 .   ? 42.652 -25.410 2.600   1.00 15.12 ?  248 HOH   B O    1 
HETATM 7093 O  O    . HOH   F 4 .   ? 38.542 -11.040 -2.294  1.00 18.61 ?  249 HOH   B O    1 
HETATM 7094 O  O    . HOH   F 4 .   ? 40.400 -12.784 -11.552 1.00 15.30 ?  250 HOH   B O    1 
HETATM 7095 O  O    . HOH   F 4 .   ? 39.575 -11.151 0.295   1.00 16.97 ?  251 HOH   B O    1 
HETATM 7096 O  O    . HOH   F 4 .   ? 43.187 -43.289 -8.329  1.00 28.38 ?  252 HOH   B O    1 
HETATM 7097 O  O    . HOH   F 4 .   ? 43.286 -32.405 -17.133 1.00 22.60 ?  253 HOH   B O    1 
HETATM 7098 O  O    . HOH   F 4 .   ? 44.616 -27.837 -0.767  1.00 21.51 ?  254 HOH   B O    1 
HETATM 7099 O  O    . HOH   F 4 .   ? 51.630 -13.859 10.923  1.00 28.30 ?  255 HOH   B O    1 
HETATM 7100 O  O    . HOH   F 4 .   ? 34.273 -18.599 11.395  1.00 23.60 ?  256 HOH   B O    1 
HETATM 7101 O  O    . HOH   F 4 .   ? 48.085 -22.841 5.788   1.00 16.66 ?  257 HOH   B O    1 
HETATM 7102 O  O    . HOH   F 4 .   ? 58.263 -10.611 -4.087  1.00 20.41 ?  258 HOH   B O    1 
HETATM 7103 O  O    . HOH   F 4 .   ? 33.599 -17.046 8.066   1.00 19.57 ?  259 HOH   B O    1 
HETATM 7104 O  O    . HOH   F 4 .   ? 29.775 -25.240 -10.854 1.00 17.00 ?  260 HOH   B O    1 
HETATM 7105 O  O    . HOH   F 4 .   ? 27.173 -31.855 -10.000 1.00 21.38 ?  261 HOH   B O    1 
HETATM 7106 O  O    . HOH   F 4 .   ? 31.859 -17.986 -14.546 1.00 31.56 ?  262 HOH   B O    1 
HETATM 7107 O  O    . HOH   F 4 .   ? 30.928 -15.772 2.648   1.00 13.69 ?  263 HOH   B O    1 
HETATM 7108 O  O    . HOH   F 4 .   ? 38.993 -12.057 12.312  1.00 35.07 ?  264 HOH   B O    1 
HETATM 7109 O  O    . HOH   F 4 .   ? 57.053 -8.660  8.371   1.00 20.03 ?  265 HOH   B O    1 
HETATM 7110 O  O    . HOH   F 4 .   ? 49.419 -28.742 -6.967  1.00 15.71 ?  266 HOH   B O    1 
HETATM 7111 O  O    . HOH   F 4 .   ? 57.589 -9.248  1.377   1.00 19.88 ?  267 HOH   B O    1 
HETATM 7112 O  O    . HOH   F 4 .   ? 51.085 -39.999 -8.322  1.00 32.17 ?  268 HOH   B O    1 
HETATM 7113 O  O    . HOH   F 4 .   ? 46.690 -31.320 -4.865  1.00 18.97 ?  269 HOH   B O    1 
HETATM 7114 O  O    . HOH   F 4 .   ? 48.084 -24.544 -17.799 1.00 30.23 ?  270 HOH   B O    1 
HETATM 7115 O  O    . HOH   F 4 .   ? 28.532 -30.860 -14.802 1.00 29.25 ?  271 HOH   B O    1 
HETATM 7116 O  O    . HOH   F 4 .   ? 42.343 -10.118 -14.974 1.00 36.08 ?  272 HOH   B O    1 
HETATM 7117 O  O    . HOH   F 4 .   ? 30.627 -42.272 -10.670 1.00 28.42 ?  273 HOH   B O    1 
HETATM 7118 O  O    . HOH   F 4 .   ? 56.268 -23.492 -14.774 1.00 26.49 ?  274 HOH   B O    1 
HETATM 7119 O  O    . HOH   F 4 .   ? 28.318 -34.384 -9.477  1.00 20.94 ?  275 HOH   B O    1 
HETATM 7120 O  O    . HOH   F 4 .   ? 43.449 -15.815 -12.210 1.00 14.26 ?  276 HOH   B O    1 
HETATM 7121 O  O    . HOH   F 4 .   ? 34.544 -12.840 2.633   1.00 23.47 ?  277 HOH   B O    1 
HETATM 7122 O  O    . HOH   F 4 .   ? 42.423 -9.921  9.340   1.00 21.19 ?  278 HOH   B O    1 
HETATM 7123 O  O    . HOH   F 4 .   ? 34.956 -33.345 -19.291 1.00 31.87 ?  279 HOH   B O    1 
HETATM 7124 O  O    . HOH   F 4 .   ? 57.246 -12.045 12.278  1.00 34.79 ?  280 HOH   B O    1 
HETATM 7125 O  O    . HOH   F 4 .   ? 46.941 -29.634 9.774   1.00 31.92 ?  281 HOH   B O    1 
HETATM 7126 O  O    . HOH   F 4 .   ? 28.010 -22.904 -8.016  1.00 17.27 ?  282 HOH   B O    1 
HETATM 7127 O  O    . HOH   F 4 .   ? 27.663 -26.800 -15.746 1.00 34.01 ?  283 HOH   B O    1 
HETATM 7128 O  O    . HOH   F 4 .   ? 36.907 -12.799 -1.547  1.00 26.25 ?  284 HOH   B O    1 
HETATM 7129 O  O    . HOH   F 4 .   ? 52.662 -10.441 12.973  1.00 22.76 ?  285 HOH   B O    1 
HETATM 7130 O  O    . HOH   F 4 .   ? 48.513 -25.092 3.046   1.00 13.10 ?  286 HOH   B O    1 
HETATM 7131 O  O    . HOH   F 4 .   ? 47.165 -34.026 -4.709  1.00 17.10 ?  287 HOH   B O    1 
HETATM 7132 O  O    . HOH   F 4 .   ? 49.846 -0.472  10.253  1.00 31.11 ?  288 HOH   B O    1 
HETATM 7133 O  O    . HOH   F 4 .   ? 48.804 -20.067 5.899   1.00 13.92 ?  289 HOH   B O    1 
HETATM 7134 O  O    . HOH   F 4 .   ? 33.576 -15.317 -14.013 1.00 21.16 ?  290 HOH   B O    1 
HETATM 7135 O  O    . HOH   F 4 .   ? 42.895 -20.268 -20.762 1.00 36.65 ?  291 HOH   B O    1 
HETATM 7136 O  O    . HOH   F 4 .   ? 42.500 -34.751 3.754   1.00 26.22 ?  292 HOH   B O    1 
HETATM 7137 O  O    . HOH   F 4 .   ? 52.678 -35.689 -8.663  1.00 30.21 ?  293 HOH   B O    1 
HETATM 7138 O  O    . HOH   F 4 .   ? 41.206 -5.539  11.539  1.00 41.60 ?  294 HOH   B O    1 
HETATM 7139 O  O    . HOH   F 4 .   ? 45.419 -33.416 -16.006 1.00 22.75 ?  295 HOH   B O    1 
HETATM 7140 O  O    . HOH   F 4 .   ? 62.906 -20.209 -0.915  1.00 37.74 ?  296 HOH   B O    1 
HETATM 7141 O  O    . HOH   F 4 .   ? 26.006 -21.522 -3.520  1.00 16.77 ?  297 HOH   B O    1 
HETATM 7142 O  O    . HOH   F 4 .   ? 46.002 -40.467 -3.665  1.00 28.44 ?  298 HOH   B O    1 
HETATM 7143 O  O    . HOH   F 4 .   ? 51.331 -37.644 -9.661  1.00 24.67 ?  299 HOH   B O    1 
HETATM 7144 O  O    . HOH   F 4 .   ? 41.259 -24.438 15.759  1.00 44.33 ?  300 HOH   B O    1 
HETATM 7145 O  O    . HOH   F 4 .   ? 42.793 -12.286 -18.547 1.00 27.92 ?  301 HOH   B O    1 
HETATM 7146 O  O    . HOH   F 4 .   ? 44.698 -27.504 1.953   1.00 14.94 ?  302 HOH   B O    1 
HETATM 7147 O  O    . HOH   F 4 .   ? 59.873 -15.353 8.161   1.00 31.78 ?  303 HOH   B O    1 
HETATM 7148 O  O    . HOH   F 4 .   ? 37.424 -35.751 7.177   1.00 33.30 ?  304 HOH   B O    1 
HETATM 7149 O  O    . HOH   F 4 .   ? 44.098 -29.392 -4.727  1.00 22.81 ?  305 HOH   B O    1 
HETATM 7150 O  O    . HOH   F 4 .   ? 35.123 -33.638 4.456   1.00 28.55 ?  306 HOH   B O    1 
HETATM 7151 O  O    . HOH   F 4 .   ? 37.597 -18.261 13.105  1.00 28.90 ?  307 HOH   B O    1 
HETATM 7152 O  O    . HOH   F 4 .   ? 53.532 -30.250 4.468   1.00 18.90 ?  308 HOH   B O    1 
HETATM 7153 O  O    . HOH   F 4 .   ? 53.209 -16.067 -12.802 1.00 27.54 ?  309 HOH   B O    1 
HETATM 7154 O  O    . HOH   F 4 .   ? 40.326 -10.850 -9.562  1.00 16.80 ?  310 HOH   B O    1 
HETATM 7155 O  O    . HOH   F 4 .   ? 51.762 -5.938  -7.993  1.00 47.34 ?  311 HOH   B O    1 
HETATM 7156 O  O    . HOH   F 4 .   ? 62.774 -13.574 4.810   1.00 28.75 ?  312 HOH   B O    1 
HETATM 7157 O  O    . HOH   F 4 .   ? 52.655 -29.264 -13.072 1.00 24.24 ?  313 HOH   B O    1 
HETATM 7158 O  O    . HOH   F 4 .   ? 50.047 -24.716 5.819   1.00 34.25 ?  314 HOH   B O    1 
HETATM 7159 O  O    . HOH   F 4 .   ? 32.872 -34.655 -5.952  1.00 17.03 ?  315 HOH   B O    1 
HETATM 7160 O  O    . HOH   F 4 .   ? 37.895 -10.255 -10.758 1.00 16.96 ?  316 HOH   B O    1 
HETATM 7161 O  O    . HOH   F 4 .   ? 43.305 -21.470 10.651  1.00 15.57 ?  317 HOH   B O    1 
HETATM 7162 O  O    . HOH   F 4 .   ? 43.598 -15.379 18.191  1.00 30.53 ?  318 HOH   B O    1 
HETATM 7163 O  O    . HOH   F 4 .   ? 41.796 -8.100  1.344   1.00 24.56 ?  319 HOH   B O    1 
HETATM 7164 O  O    . HOH   F 4 .   ? 45.828 -36.297 -16.172 1.00 36.04 ?  320 HOH   B O    1 
HETATM 7165 O  O    . HOH   F 4 .   ? 38.430 -12.820 7.917   1.00 18.65 ?  321 HOH   B O    1 
HETATM 7166 O  O    . HOH   F 4 .   ? 51.493 -32.979 -10.861 1.00 38.90 ?  322 HOH   B O    1 
HETATM 7167 O  O    . HOH   F 4 .   ? 37.198 -30.588 -21.092 1.00 30.00 ?  323 HOH   B O    1 
HETATM 7168 O  O    . HOH   F 4 .   ? 48.201 -32.662 -16.720 1.00 45.25 ?  324 HOH   B O    1 
HETATM 7169 O  O    . HOH   F 4 .   ? 26.384 -21.076 -6.260  1.00 16.56 ?  325 HOH   B O    1 
HETATM 7170 O  O    . HOH   F 4 .   ? 60.011 -17.258 -10.566 1.00 35.29 ?  326 HOH   B O    1 
HETATM 7171 O  O    . HOH   F 4 .   ? 44.708 -24.669 9.535   1.00 19.27 ?  327 HOH   B O    1 
HETATM 7172 O  O    . HOH   F 4 .   ? 57.692 -22.069 3.201   1.00 29.60 ?  328 HOH   B O    1 
HETATM 7173 O  O    . HOH   F 4 .   ? 36.797 -12.445 4.271   1.00 18.56 ?  329 HOH   B O    1 
HETATM 7174 O  O    . HOH   F 4 .   ? 53.763 -12.453 -22.310 1.00 36.32 ?  330 HOH   B O    1 
HETATM 7175 O  O    . HOH   F 4 .   ? 43.189 -34.652 0.020   1.00 21.09 ?  331 HOH   B O    1 
HETATM 7176 O  O    . HOH   F 4 .   ? 47.279 -24.535 8.105   1.00 26.85 ?  332 HOH   B O    1 
HETATM 7177 O  O    . HOH   F 4 .   ? 33.729 -31.232 11.062  1.00 35.24 ?  333 HOH   B O    1 
HETATM 7178 O  O    . HOH   F 4 .   ? 39.572 -23.501 -20.372 1.00 38.19 ?  334 HOH   B O    1 
HETATM 7179 O  O    . HOH   F 4 .   ? 48.674 -11.914 -13.904 1.00 27.73 ?  335 HOH   B O    1 
HETATM 7180 O  O    . HOH   F 4 .   ? 38.426 -9.377  -13.282 1.00 27.58 ?  336 HOH   B O    1 
HETATM 7181 O  O    . HOH   F 4 .   ? 27.932 -14.747 -9.503  1.00 34.62 ?  337 HOH   B O    1 
HETATM 7182 O  O    . HOH   F 4 .   ? 47.564 -27.479 1.975   1.00 14.86 ?  338 HOH   B O    1 
HETATM 7183 O  O    . HOH   F 4 .   ? 42.917 -43.520 -14.471 1.00 44.97 ?  339 HOH   B O    1 
HETATM 7184 O  O    . HOH   F 4 .   ? 44.238 -1.679  7.558   1.00 44.68 ?  340 HOH   B O    1 
HETATM 7185 O  O    . HOH   F 4 .   ? 37.074 -15.052 -16.517 1.00 38.64 ?  341 HOH   B O    1 
HETATM 7186 O  O    . HOH   F 4 .   ? 28.912 -42.929 -12.428 1.00 40.25 ?  342 HOH   B O    1 
HETATM 7187 O  O    . HOH   F 4 .   ? 46.914 -19.960 12.322  1.00 32.46 ?  343 HOH   B O    1 
HETATM 7188 O  O    . HOH   F 4 .   ? 39.856 -44.296 -11.297 1.00 36.97 ?  344 HOH   B O    1 
HETATM 7189 O  O    . HOH   F 4 .   ? 33.063 -14.718 1.038   1.00 18.39 ?  345 HOH   B O    1 
HETATM 7190 O  O    . HOH   F 4 .   ? 37.101 -45.310 -9.757  1.00 36.30 ?  346 HOH   B O    1 
HETATM 7191 O  O    . HOH   F 4 .   ? 38.511 -12.295 -16.240 1.00 39.39 ?  347 HOH   B O    1 
HETATM 7192 O  O    . HOH   F 4 .   ? 40.482 -43.514 -9.190  1.00 27.15 ?  348 HOH   B O    1 
HETATM 7193 O  O    . HOH   F 4 .   ? 62.593 -20.105 -4.916  1.00 46.71 ?  349 HOH   B O    1 
HETATM 7194 O  O    . HOH   F 4 .   ? 55.721 -8.270  10.777  1.00 24.09 ?  350 HOH   B O    1 
HETATM 7195 O  O    . HOH   F 4 .   ? 23.302 -23.745 6.773   1.00 37.64 ?  351 HOH   B O    1 
HETATM 7196 O  O    . HOH   F 4 .   ? 33.796 -9.349  -8.843  1.00 30.53 ?  352 HOH   B O    1 
HETATM 7197 O  O    . HOH   F 4 .   ? 38.612 -22.380 15.034  1.00 40.15 ?  353 HOH   B O    1 
HETATM 7198 O  O    . HOH   F 4 .   ? 27.839 -26.655 -0.625  1.00 29.55 ?  354 HOH   B O    1 
HETATM 7199 O  O    . HOH   F 4 .   ? 44.256 -37.412 -17.936 1.00 32.40 ?  355 HOH   B O    1 
HETATM 7200 O  O    . HOH   F 4 .   ? 36.185 -8.558  -9.666  1.00 33.80 ?  356 HOH   B O    1 
HETATM 7201 O  O    . HOH   F 4 .   ? 34.721 -10.351 7.479   1.00 24.42 ?  357 HOH   B O    1 
HETATM 7202 O  O    . HOH   F 4 .   ? 56.658 -7.273  3.053   1.00 28.59 ?  358 HOH   B O    1 
HETATM 7203 O  O    . HOH   F 4 .   ? 34.081 -7.862  11.493  1.00 41.82 ?  359 HOH   B O    1 
HETATM 7204 O  O    . HOH   F 4 .   ? 43.215 -12.742 -21.256 1.00 37.08 ?  360 HOH   B O    1 
HETATM 7205 O  O    . HOH   F 4 .   ? 61.594 -19.901 1.603   1.00 33.68 ?  361 HOH   B O    1 
HETATM 7206 O  O    . HOH   F 4 .   ? 57.002 -21.533 -16.390 1.00 40.84 ?  362 HOH   B O    1 
HETATM 7207 O  O    . HOH   F 4 .   ? 27.216 -25.981 -11.416 1.00 33.29 ?  363 HOH   B O    1 
HETATM 7208 O  O    . HOH   F 4 .   ? 40.330 -8.818  9.882   1.00 38.78 ?  364 HOH   B O    1 
HETATM 7209 O  O    . HOH   F 4 .   ? 32.589 -23.672 14.049  1.00 40.72 ?  365 HOH   B O    1 
HETATM 7210 O  O    . HOH   F 4 .   ? 59.109 -10.557 9.092   1.00 38.92 ?  366 HOH   B O    1 
HETATM 7211 O  O    . HOH   F 4 .   ? 54.330 -5.817  2.926   1.00 37.93 ?  367 HOH   B O    1 
HETATM 7212 O  O    . HOH   F 4 .   ? 48.454 -26.545 8.781   1.00 39.88 ?  368 HOH   B O    1 
HETATM 7213 O  O    . HOH   F 4 .   ? 36.300 -8.749  8.929   1.00 36.85 ?  369 HOH   B O    1 
HETATM 7214 O  O    . HOH   F 4 .   ? 41.862 -10.081 -17.455 1.00 53.44 ?  370 HOH   B O    1 
HETATM 7215 O  O    . HOH   F 4 .   ? 39.893 -7.106  7.819   1.00 44.08 ?  371 HOH   B O    1 
HETATM 7216 O  O    . HOH   F 4 .   ? 40.088 -11.398 -14.016 1.00 31.98 ?  372 HOH   B O    1 
HETATM 7217 O  O    . HOH   F 4 .   ? 52.156 -12.893 13.287  1.00 31.24 ?  373 HOH   B O    1 
HETATM 7218 O  O    . HOH   F 4 .   ? 56.020 -7.768  -0.587  1.00 34.71 ?  374 HOH   B O    1 
HETATM 7219 O  O    . HOH   F 4 .   ? 63.119 -12.411 6.919   1.00 36.49 ?  375 HOH   B O    1 
HETATM 7220 O  O    . HOH   F 4 .   ? 38.125 -10.640 10.027  1.00 29.05 ?  376 HOH   B O    1 
HETATM 7221 O  O    . HOH   F 4 .   ? 41.934 -6.833  -4.831  1.00 47.91 ?  377 HOH   B O    1 
HETATM 7222 O  O    . HOH   F 4 .   ? 36.604 -22.909 13.288  1.00 24.05 ?  378 HOH   B O    1 
HETATM 7223 O  O    . HOH   F 4 .   ? 42.770 -17.213 -23.226 1.00 41.87 ?  379 HOH   B O    1 
HETATM 7224 O  O    . HOH   F 4 .   ? 40.245 -7.701  3.183   1.00 38.33 ?  380 HOH   B O    1 
HETATM 7225 O  O    . HOH   F 4 .   ? 44.080 -5.609  -3.497  1.00 43.22 ?  381 HOH   B O    1 
HETATM 7226 O  O    . HOH   F 4 .   ? 52.941 -29.938 7.139   1.00 23.68 ?  382 HOH   B O    1 
HETATM 7227 O  O    . HOH   F 4 .   ? 39.747 -14.074 15.736  1.00 48.94 ?  383 HOH   B O    1 
HETATM 7228 O  O    . HOH   F 4 .   ? 60.548 -22.356 2.799   1.00 45.94 ?  384 HOH   B O    1 
HETATM 7229 O  O    . HOH   F 4 .   ? 46.819 -5.403  2.939   1.00 41.79 ?  385 HOH   B O    1 
HETATM 7230 O  O    . HOH   F 4 .   ? 35.455 -33.739 7.232   1.00 41.67 ?  386 HOH   B O    1 
HETATM 7231 O  O    . HOH   F 4 .   ? 23.987 -20.912 -7.711  1.00 27.27 ?  387 HOH   B O    1 
HETATM 7232 O  O    . HOH   F 4 .   ? 35.323 -20.383 13.309  1.00 31.33 ?  388 HOH   B O    1 
HETATM 7233 O  O    . HOH   F 4 .   ? 25.833 -18.947 -11.986 1.00 36.84 ?  389 HOH   B O    1 
HETATM 7234 O  O    . HOH   F 4 .   ? 40.992 -9.813  15.830  1.00 45.17 ?  390 HOH   B O    1 
HETATM 7235 O  O    . HOH   F 4 .   ? 40.771 -6.649  -0.873  1.00 25.84 ?  391 HOH   B O    1 
HETATM 7236 O  O    . HOH   F 4 .   ? 44.163 -31.733 -3.832  1.00 33.68 ?  392 HOH   B O    1 
HETATM 7237 O  O    . HOH   F 4 .   ? 28.051 -27.111 2.228   1.00 34.25 ?  393 HOH   B O    1 
HETATM 7238 O  O    . HOH   F 4 .   ? 26.638 -27.945 -13.479 1.00 34.37 ?  394 HOH   B O    1 
HETATM 7239 O  O    . HOH   F 4 .   ? 34.516 -33.520 9.613   1.00 33.90 ?  395 HOH   B O    1 
HETATM 7240 O  O    . HOH   F 4 .   ? 50.710 -30.865 8.652   1.00 27.30 ?  396 HOH   B O    1 
HETATM 7241 O  O    . HOH   F 4 .   ? 24.660 -20.723 -10.486 1.00 36.03 ?  397 HOH   B O    1 
HETATM 7242 O  O    . HOH   F 4 .   ? 26.870 -30.667 -12.676 1.00 29.54 ?  398 HOH   B O    1 
HETATM 7243 O  O    . HOH   F 4 .   ? 45.775 -20.181 15.221  1.00 51.41 ?  399 HOH   B O    1 
HETATM 7244 O  O    . HOH   F 4 .   ? 57.694 -6.441  -2.313  1.00 33.71 ?  400 HOH   B O    1 
HETATM 7245 O  O    . HOH   F 4 .   ? 40.895 -11.833 -22.398 1.00 44.94 ?  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   ? 0.6503 0.6379 0.6772 0.0036  -0.0186 0.0832  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6524 0.6386 0.6797 0.0025  -0.0199 0.0821  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6480 0.6362 0.6721 0.0026  -0.0180 0.0836  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6499 0.6367 0.6739 0.0019  -0.0195 0.0827  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6365 0.6286 0.6502 -0.0005 -0.0204 0.0899  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6376 0.6290 0.6515 -0.0010 -0.0214 0.0893  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6387 0.6303 0.6577 0.0009  -0.0218 0.0916  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6401 0.6308 0.6596 0.0002  -0.0228 0.0909  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6551 0.6408 0.6832 0.0040  -0.0140 0.0787  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6575 0.6413 0.6845 0.0032  -0.0162 0.0776  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6577 0.6426 0.6863 0.0044  -0.0127 0.0771  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6602 0.6430 0.6873 0.0035  -0.0151 0.0757  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6574 0.6424 0.6863 0.0046  -0.0122 0.0772  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6600 0.6428 0.6876 0.0039  -0.0146 0.0761  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6202 0.6175 0.6145 -0.0054 -0.0202 0.0945  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5841 0.5923 0.5354 -0.0152 -0.0168 0.1011  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5363 0.5593 0.4855 -0.0289 -0.0012 0.0850  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5391 0.5621 0.4741 -0.0301 -0.0021 0.0916  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5932 0.5972 0.5030 -0.0118 -0.0278 0.1207  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.5998 0.6001 0.4718 -0.0091 -0.0373 0.1401  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.6034 0.6006 0.4582 -0.0082 -0.0405 0.1463  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.6007 0.6007 0.4659 -0.0076 -0.0412 0.1497  4   ASN   A ND2 
46   N  N   . SER   A 5   ? 0.4827 0.5184 0.4424 -0.0426 0.0129  0.0620  5   SER   A N   
47   C  CA  . SER   A 5   ? 0.4279 0.4800 0.4019 -0.0542 0.0300  0.0374  5   SER   A CA  
48   C  C   . SER   A 5   ? 0.3662 0.4213 0.3403 -0.0591 0.0503  0.0196  5   SER   A C   
49   O  O   . SER   A 5   ? 0.3760 0.4349 0.3385 -0.0462 0.0523  0.0055  5   SER   A O   
50   C  CB  . SER   A 5   ? 0.4358 0.4964 0.4288 -0.0588 0.0271  0.0293  5   SER   A CB  
51   O  OG  . SER   A 5   ? 0.4404 0.4978 0.4424 -0.0612 0.0272  0.0242  5   SER   A OG  
57   N  N   A PHE   A 6   ? 0.3230 0.3794 0.3044 -0.0696 0.0626  0.0250  6   PHE   A N   
58   N  N   B PHE   A 6   ? 0.3325 0.3893 0.3120 -0.0671 0.0630  0.0171  6   PHE   A N   
59   C  CA  A PHE   A 6   ? 0.2840 0.3360 0.2679 -0.0783 0.0684  0.0367  6   PHE   A CA  
60   C  CA  B PHE   A 6   ? 0.3017 0.3557 0.2833 -0.0735 0.0702  0.0208  6   PHE   A CA  
61   C  C   A PHE   A 6   ? 0.2718 0.3285 0.2706 -0.0781 0.0795  0.0298  6   PHE   A C   
62   C  C   B PHE   A 6   ? 0.2991 0.3491 0.2897 -0.0732 0.0857  0.0224  6   PHE   A C   
63   O  O   A PHE   A 6   ? 0.2739 0.3356 0.2936 -0.0790 0.0748  0.0319  6   PHE   A O   
64   O  O   B PHE   A 6   ? 0.3028 0.3539 0.3113 -0.0738 0.0806  0.0286  6   PHE   A O   
65   C  CB  A PHE   A 6   ? 0.2646 0.3014 0.2405 -0.0785 0.0532  0.0507  6   PHE   A CB  
66   C  CB  B PHE   A 6   ? 0.2786 0.3296 0.2591 -0.0733 0.0555  0.0187  6   PHE   A CB  
67   C  CG  A PHE   A 6   ? 0.2496 0.2743 0.2137 -0.0755 0.0407  0.0631  6   PHE   A CG  
68   C  CG  B PHE   A 6   ? 0.2594 0.3087 0.2396 -0.0702 0.0412  0.0135  6   PHE   A CG  
69   C  CD1 A PHE   A 6   ? 0.2452 0.2643 0.2057 -0.0690 0.0308  0.0636  6   PHE   A CD1 
70   C  CD1 B PHE   A 6   ? 0.2520 0.3005 0.2291 -0.0643 0.0352  0.0098  6   PHE   A CD1 
71   C  CD2 A PHE   A 6   ? 0.2495 0.2663 0.2150 -0.0668 0.0361  0.0684  6   PHE   A CD2 
72   C  CD2 B PHE   A 6   ? 0.2548 0.3007 0.2456 -0.0663 0.0372  0.0108  6   PHE   A CD2 
73   C  CE1 A PHE   A 6   ? 0.2423 0.2576 0.2078 -0.0674 0.0273  0.0652  6   PHE   A CE1 
74   C  CE1 B PHE   A 6   ? 0.2469 0.2944 0.2283 -0.0633 0.0361  0.0096  6   PHE   A CE1 
75   C  CE2 A PHE   A 6   ? 0.2467 0.2587 0.2175 -0.0642 0.0305  0.0679  6   PHE   A CE2 
76   C  CE2 B PHE   A 6   ? 0.2497 0.2931 0.2438 -0.0647 0.0344  0.0093  6   PHE   A CE2 
77   C  CZ  A PHE   A 6   ? 0.2441 0.2543 0.2117 -0.0663 0.0260  0.0651  6   PHE   A CZ  
78   C  CZ  B PHE   A 6   ? 0.2468 0.2922 0.2329 -0.0629 0.0356  0.0078  6   PHE   A CZ  
97   N  N   A SER   A 7   ? 0.2579 0.3117 0.2561 -0.0759 0.0880  0.0219  7   SER   A N   
98   N  N   B SER   A 7   ? 0.2919 0.3349 0.2790 -0.0701 0.0986  0.0159  7   SER   A N   
99   C  CA  A SER   A 7   ? 0.2513 0.2985 0.2619 -0.0705 0.0832  -0.0025 7   SER   A CA  
100  C  CA  B SER   A 7   ? 0.2922 0.3252 0.2906 -0.0620 0.0889  -0.0058 7   SER   A CA  
101  C  C   A SER   A 7   ? 0.2332 0.2638 0.2513 -0.0710 0.0906  -0.0051 7   SER   A C   
102  C  C   B SER   A 7   ? 0.2801 0.3040 0.2742 -0.0588 0.0912  -0.0013 7   SER   A C   
103  O  O   A SER   A 7   ? 0.2410 0.2576 0.2563 -0.0730 0.0936  -0.0016 7   SER   A O   
104  O  O   B SER   A 7   ? 0.2881 0.3007 0.2741 -0.0631 0.0898  0.0095  7   SER   A O   
105  C  CB  A SER   A 7   ? 0.2636 0.3162 0.2747 -0.0638 0.0739  -0.0149 7   SER   A CB  
106  C  CB  B SER   A 7   ? 0.3005 0.3339 0.3153 -0.0603 0.0807  -0.0213 7   SER   A CB  
107  O  OG  A SER   A 7   ? 0.2761 0.3279 0.2889 -0.0585 0.0631  -0.0220 7   SER   A OG  
108  O  OG  B SER   A 7   ? 0.3077 0.3407 0.3412 -0.0575 0.0705  -0.0322 7   SER   A OG  
119  N  N   A GLY   A 8   ? 0.2162 0.2400 0.2403 -0.0667 0.0851  -0.0186 8   GLY   A N   
120  N  N   B GLY   A 8   ? 0.2649 0.2888 0.2664 -0.0489 0.0889  -0.0077 8   GLY   A N   
121  C  CA  A GLY   A 8   ? 0.2028 0.2247 0.2404 -0.0527 0.0821  -0.0235 8   GLY   A CA  
122  C  CA  B GLY   A 8   ? 0.2482 0.2698 0.2625 -0.0400 0.0799  -0.0087 8   GLY   A CA  
123  C  C   A GLY   A 8   ? 0.1899 0.2132 0.2339 -0.0373 0.0697  -0.0288 8   GLY   A C   
124  C  C   B GLY   A 8   ? 0.2283 0.2519 0.2481 -0.0306 0.0665  -0.0096 8   GLY   A C   
125  O  O   A GLY   A 8   ? 0.1933 0.2208 0.2541 -0.0199 0.0682  -0.0549 8   GLY   A O   
126  O  O   B GLY   A 8   ? 0.2314 0.2585 0.2681 -0.0222 0.0618  -0.0244 8   GLY   A O   
133  N  N   A TYR   A 9   ? 0.1731 0.1945 0.2035 -0.0340 0.0602  -0.0111 9   TYR   A N   
134  N  N   B TYR   A 9   ? 0.2059 0.2278 0.2227 -0.0290 0.0555  0.0061  9   TYR   A N   
135  C  CA  A TYR   A 9   ? 0.1642 0.1783 0.1857 -0.0299 0.0463  -0.0035 9   TYR   A CA  
136  C  CA  B TYR   A 9   ? 0.1896 0.2054 0.2049 -0.0285 0.0520  0.0105  9   TYR   A CA  
137  C  C   A TYR   A 9   ? 0.1776 0.1663 0.1775 -0.0320 0.0448  0.0123  9   TYR   A C   
138  C  C   B TYR   A 9   ? 0.1901 0.1901 0.1853 -0.0241 0.0561  0.0190  9   TYR   A C   
139  O  O   A TYR   A 9   ? 0.2020 0.1725 0.1795 -0.0397 0.0442  0.0001  9   TYR   A O   
140  O  O   B TYR   A 9   ? 0.2052 0.2037 0.1997 -0.0283 0.0544  0.0134  9   TYR   A O   
141  C  CB  A TYR   A 9   ? 0.1576 0.1760 0.1839 -0.0132 0.0362  -0.0118 9   TYR   A CB  
142  C  CB  B TYR   A 9   ? 0.1873 0.2071 0.2098 -0.0226 0.0387  -0.0025 9   TYR   A CB  
143  C  CG  A TYR   A 9   ? 0.1547 0.1710 0.1874 -0.0023 0.0488  -0.0198 9   TYR   A CG  
144  C  CG  B TYR   A 9   ? 0.1820 0.2038 0.2020 -0.0206 0.0429  -0.0121 9   TYR   A CG  
145  C  CD1 A TYR   A 9   ? 0.1539 0.1727 0.1961 -0.0044 0.0544  -0.0165 9   TYR   A CD1 
146  C  CD1 B TYR   A 9   ? 0.1850 0.2035 0.2077 -0.0197 0.0480  -0.0231 9   TYR   A CD1 
147  C  CD2 A TYR   A 9   ? 0.1577 0.1654 0.1953 -0.0025 0.0414  -0.0038 9   TYR   A CD2 
148  C  CD2 B TYR   A 9   ? 0.1784 0.1973 0.1932 -0.0192 0.0380  -0.0094 9   TYR   A CD2 
149  C  CE1 A TYR   A 9   ? 0.1551 0.1770 0.2123 -0.0022 0.0484  -0.0231 9   TYR   A CE1 
150  C  CE1 B TYR   A 9   ? 0.1817 0.1978 0.2117 -0.0187 0.0525  -0.0297 9   TYR   A CE1 
151  C  CE2 A TYR   A 9   ? 0.1553 0.1677 0.2035 -0.0033 0.0513  -0.0183 9   TYR   A CE2 
152  C  CE2 B TYR   A 9   ? 0.1736 0.1967 0.2001 -0.0162 0.0468  -0.0126 9   TYR   A CE2 
153  C  CZ  A TYR   A 9   ? 0.1573 0.1791 0.2199 -0.0125 0.0556  -0.0248 9   TYR   A CZ  
154  C  CZ  B TYR   A 9   ? 0.1759 0.1957 0.2160 -0.0180 0.0592  -0.0206 9   TYR   A CZ  
155  O  OH  A TYR   A 9   ? 0.1670 0.1859 0.2395 -0.0269 0.0540  -0.0373 9   TYR   A OH  
156  O  OH  B TYR   A 9   ? 0.1796 0.1979 0.2382 -0.0215 0.0716  -0.0139 9   TYR   A OH  
175  N  N   A LEU   A 10  ? 0.1634 0.1567 0.1814 -0.0300 0.0367  0.0223  10  LEU   A N   
176  N  N   B LEU   A 10  ? 0.1755 0.1771 0.1796 -0.0181 0.0520  0.0216  10  LEU   A N   
177  C  CA  A LEU   A 10  ? 0.1540 0.1567 0.1793 -0.0301 0.0263  0.0289  10  LEU   A CA  
178  C  CA  B LEU   A 10  ? 0.1673 0.1809 0.1820 -0.0209 0.0466  0.0171  10  LEU   A CA  
179  C  C   A LEU   A 10  ? 0.1447 0.1494 0.1821 -0.0305 0.0248  0.0253  10  LEU   A C   
180  C  C   B LEU   A 10  ? 0.1644 0.1718 0.1668 -0.0273 0.0296  0.0236  10  LEU   A C   
181  O  O   A LEU   A 10  ? 0.1455 0.1473 0.1698 -0.0273 0.0319  0.0238  10  LEU   A O   
182  O  O   B LEU   A 10  ? 0.1686 0.1639 0.1673 -0.0273 0.0353  0.0230  10  LEU   A O   
183  C  CB  A LEU   A 10  ? 0.1609 0.1678 0.1912 -0.0254 0.0143  0.0320  10  LEU   A CB  
184  C  CB  B LEU   A 10  ? 0.1681 0.1890 0.2121 -0.0270 0.0343  0.0206  10  LEU   A CB  
185  C  CG  A LEU   A 10  ? 0.1783 0.1811 0.2332 -0.0229 0.0005  0.0246  10  LEU   A CG  
186  C  CG  B LEU   A 10  ? 0.1790 0.2016 0.2455 -0.0227 0.0228  0.0094  10  LEU   A CG  
187  C  CD1 A LEU   A 10  ? 0.1860 0.1846 0.2538 -0.0278 0.0086  0.0214  10  LEU   A CD1 
188  C  CD1 B LEU   A 10  ? 0.1879 0.2085 0.2676 -0.0291 0.0176  0.0058  10  LEU   A CD1 
189  C  CD2 A LEU   A 10  ? 0.1905 0.1908 0.2402 -0.0150 0.0041  0.0070  10  LEU   A CD2 
190  C  CD2 B LEU   A 10  ? 0.1967 0.2170 0.2716 -0.0187 0.0133  0.0040  10  LEU   A CD2 
213  N  N   A LYS   A 11  ? 0.1426 0.1464 0.1835 -0.0262 0.0303  0.0233  11  LYS   A N   
214  N  N   B LYS   A 11  ? 0.1699 0.1678 0.1788 -0.0335 0.0181  0.0165  11  LYS   A N   
215  C  CA  A LYS   A 11  ? 0.1433 0.1401 0.1908 -0.0342 0.0265  0.0192  11  LYS   A CA  
216  C  CA  B LYS   A 11  ? 0.1700 0.1630 0.1838 -0.0345 0.0153  0.0214  11  LYS   A CA  
217  C  C   A LYS   A 11  ? 0.1403 0.1445 0.1849 -0.0292 0.0350  0.0102  11  LYS   A C   
218  C  C   B LYS   A 11  ? 0.1589 0.1543 0.1849 -0.0392 0.0166  0.0093  11  LYS   A C   
219  O  O   A LYS   A 11  ? 0.1497 0.1635 0.2181 -0.0460 0.0407  -0.0045 11  LYS   A O   
220  O  O   B LYS   A 11  ? 0.1588 0.1579 0.2015 -0.0471 0.0301  -0.0161 11  LYS   A O   
221  C  CB  A LYS   A 11  ? 0.1551 0.1415 0.1871 -0.0357 0.0177  0.0093  11  LYS   A CB  
222  C  CB  B LYS   A 11  ? 0.1825 0.1605 0.1862 -0.0328 0.0051  0.0184  11  LYS   A CB  
223  C  CG  A LYS   A 11  ? 0.1723 0.1409 0.1978 -0.0442 0.0187  0.0212  11  LYS   A CG  
224  C  CG  B LYS   A 11  ? 0.1906 0.1615 0.1747 -0.0324 0.0061  0.0214  11  LYS   A CG  
225  C  CD  A LYS   A 11  ? 0.1922 0.1498 0.2100 -0.0372 0.0112  0.0238  11  LYS   A CD  
226  C  CD  B LYS   A 11  ? 0.1949 0.1645 0.1631 -0.0333 0.0003  0.0280  11  LYS   A CD  
227  C  CE  A LYS   A 11  ? 0.2005 0.1458 0.2163 -0.0355 0.0064  0.0265  11  LYS   A CE  
228  C  CE  B LYS   A 11  ? 0.2008 0.1604 0.1571 -0.0280 -0.0004 0.0334  11  LYS   A CE  
229  N  NZ  A LYS   A 11  ? 0.1973 0.1421 0.2196 -0.0299 -0.0111 0.0143  11  LYS   A NZ  
230  N  NZ  B LYS   A 11  ? 0.1996 0.1638 0.1605 -0.0179 -0.0032 0.0399  11  LYS   A NZ  
257  N  N   A LEU   A 12  ? 0.1331 0.1408 0.1659 -0.0328 0.0332  -0.0042 12  LEU   A N   
258  N  N   B LEU   A 12  ? 0.1486 0.1609 0.1845 -0.0279 0.0083  0.0047  12  LEU   A N   
259  C  CA  A LEU   A 12  ? 0.1364 0.1378 0.1747 -0.0266 0.0197  0.0071  12  LEU   A CA  
260  C  CA  B LEU   A 12  ? 0.1435 0.1733 0.1860 -0.0207 0.0089  0.0047  12  LEU   A CA  
261  C  C   A LEU   A 12  ? 0.1410 0.1302 0.1846 -0.0309 0.0175  0.0138  12  LEU   A C   
262  C  C   B LEU   A 12  ? 0.1387 0.1682 0.1698 -0.0220 0.0176  0.0164  12  LEU   A C   
263  O  O   A LEU   A 12  ? 0.1452 0.1290 0.1953 -0.0285 0.0142  0.0046  12  LEU   A O   
264  O  O   B LEU   A 12  ? 0.1483 0.1634 0.1644 -0.0106 0.0103  0.0113  12  LEU   A O   
265  C  CB  A LEU   A 12  ? 0.1413 0.1301 0.1753 -0.0195 0.0121  0.0125  12  LEU   A CB  
266  C  CB  B LEU   A 12  ? 0.1503 0.1852 0.2054 -0.0149 0.0071  -0.0016 12  LEU   A CB  
267  C  CG  A LEU   A 12  ? 0.1559 0.1387 0.1999 -0.0092 0.0200  0.0151  12  LEU   A CG  
268  C  CG  B LEU   A 12  ? 0.1534 0.1910 0.2175 -0.0108 0.0170  -0.0031 12  LEU   A CG  
269  C  CD1 A LEU   A 12  ? 0.1686 0.1465 0.2108 0.0033  0.0257  0.0283  12  LEU   A CD1 
270  C  CD1 B LEU   A 12  ? 0.1632 0.1957 0.2263 0.0017  0.0289  -0.0079 12  LEU   A CD1 
271  C  CD2 A LEU   A 12  ? 0.1544 0.1432 0.2162 -0.0008 0.0154  0.0147  12  LEU   A CD2 
272  C  CD2 B LEU   A 12  ? 0.1483 0.1962 0.2354 -0.0108 0.0071  -0.0167 12  LEU   A CD2 
295  N  N   A THR   A 13  ? 0.1407 0.1374 0.2045 -0.0291 0.0137  0.0148  13  THR   A N   
296  N  N   B THR   A 13  ? 0.1317 0.1666 0.1718 -0.0198 0.0164  0.0059  13  THR   A N   
297  C  CA  A THR   A 13  ? 0.1460 0.1404 0.2076 -0.0265 0.0147  0.0212  13  THR   A CA  
298  C  CA  B THR   A 13  ? 0.1383 0.1660 0.1940 -0.0255 0.0179  0.0148  13  THR   A CA  
299  C  C   A THR   A 13  ? 0.1528 0.1425 0.2205 -0.0242 0.0043  0.0376  13  THR   A C   
300  C  C   B THR   A 13  ? 0.1435 0.1812 0.2107 -0.0367 0.0129  0.0296  13  THR   A C   
301  O  O   A THR   A 13  ? 0.1587 0.1425 0.2233 -0.0193 0.0058  0.0320  13  THR   A O   
302  O  O   B THR   A 13  ? 0.1459 0.1858 0.2097 -0.0388 0.0007  0.0414  13  THR   A O   
303  C  CB  A THR   A 13  ? 0.1503 0.1441 0.2099 -0.0171 0.0166  0.0211  13  THR   A CB  
304  C  CB  B THR   A 13  ? 0.1407 0.1643 0.2015 -0.0118 0.0229  0.0253  13  THR   A CB  
305  O  OG1 A THR   A 13  ? 0.1575 0.1350 0.2154 -0.0185 0.0050  0.0212  13  THR   A OG1 
306  O  OG1 B THR   A 13  ? 0.1384 0.1651 0.2109 -0.0128 0.0321  0.0307  13  THR   A OG1 
307  C  CG2 A THR   A 13  ? 0.1560 0.1522 0.2204 -0.0079 0.0177  0.0065  13  THR   A CG2 
308  C  CG2 B THR   A 13  ? 0.1371 0.1711 0.2099 -0.0034 0.0224  0.0155  13  THR   A CG2 
323  N  N   A ASP   A 14  ? 0.1555 0.1469 0.2230 -0.0235 -0.0039 0.0541  14  ASP   A N   
324  N  N   B ASP   A 14  ? 0.1450 0.1882 0.2202 -0.0408 0.0156  0.0336  14  ASP   A N   
325  C  CA  A ASP   A 14  ? 0.1627 0.1520 0.2216 -0.0231 -0.0038 0.0601  14  ASP   A CA  
326  C  CA  B ASP   A 14  ? 0.1602 0.1934 0.2208 -0.0351 0.0079  0.0388  14  ASP   A CA  
327  C  C   A ASP   A 14  ? 0.1570 0.1567 0.2074 -0.0208 0.0017  0.0558  14  ASP   A C   
328  C  C   B ASP   A 14  ? 0.1548 0.1777 0.1913 -0.0264 -0.0010 0.0457  14  ASP   A C   
329  O  O   A ASP   A 14  ? 0.1590 0.1649 0.2163 -0.0265 0.0116  0.0485  14  ASP   A O   
330  O  O   B ASP   A 14  ? 0.1585 0.1812 0.1918 -0.0229 0.0001  0.0415  14  ASP   A O   
331  C  CB  A ASP   A 14  ? 0.1784 0.1598 0.2615 -0.0292 -0.0134 0.0572  14  ASP   A CB  
332  C  CB  B ASP   A 14  ? 0.1777 0.2191 0.2531 -0.0362 -0.0001 0.0395  14  ASP   A CB  
333  C  CG  A ASP   A 14  ? 0.1979 0.1901 0.3227 -0.0339 -0.0178 0.0400  14  ASP   A CG  
334  C  CG  B ASP   A 14  ? 0.1864 0.2443 0.2928 -0.0489 -0.0061 0.0295  14  ASP   A CG  
335  O  OD1 A ASP   A 14  ? 0.2061 0.2117 0.3463 -0.0230 -0.0347 0.0346  14  ASP   A OD1 
336  O  OD1 B ASP   A 14  ? 0.1952 0.2495 0.2971 -0.0467 -0.0089 0.0306  14  ASP   A OD1 
337  O  OD2 A ASP   A 14  ? 0.2133 0.2032 0.3556 -0.0440 -0.0224 0.0199  14  ASP   A OD2 
338  O  OD2 B ASP   A 14  ? 0.1980 0.2625 0.3243 -0.0444 -0.0102 0.0203  14  ASP   A OD2 
347  N  N   A ASN   A 15  ? 0.1541 0.1547 0.2094 -0.0275 0.0040  0.0533  15  ASN   A N   
348  N  N   B ASN   A 15  ? 0.1427 0.1610 0.1792 -0.0335 0.0023  0.0514  15  ASN   A N   
349  C  CA  A ASN   A 15  ? 0.1538 0.1579 0.2132 -0.0238 -0.0025 0.0440  15  ASN   A CA  
350  C  CA  B ASN   A 15  ? 0.1403 0.1567 0.2007 -0.0277 -0.0005 0.0333  15  ASN   A CA  
351  C  C   A ASN   A 15  ? 0.1485 0.1487 0.2047 -0.0238 0.0073  0.0392  15  ASN   A C   
352  C  C   B ASN   A 15  ? 0.1334 0.1533 0.2186 -0.0204 0.0080  0.0324  15  ASN   A C   
353  O  O   A ASN   A 15  ? 0.1412 0.1510 0.2104 -0.0138 0.0126  0.0336  15  ASN   A O   
354  O  O   B ASN   A 15  ? 0.1182 0.1532 0.2411 -0.0091 0.0148  0.0221  15  ASN   A O   
355  C  CB  A ASN   A 15  ? 0.1521 0.1609 0.2145 -0.0178 -0.0052 0.0501  15  ASN   A CB  
356  C  CB  B ASN   A 15  ? 0.1367 0.1488 0.1961 -0.0298 -0.0015 0.0295  15  ASN   A CB  
357  C  CG  A ASN   A 15  ? 0.1475 0.1687 0.2179 -0.0126 0.0069  0.0479  15  ASN   A CG  
358  C  CG  B ASN   A 15  ? 0.1314 0.1540 0.2068 -0.0213 0.0049  0.0255  15  ASN   A CG  
359  O  OD1 A ASN   A 15  ? 0.1473 0.1653 0.2272 -0.0171 0.0311  0.0549  15  ASN   A OD1 
360  O  OD1 B ASN   A 15  ? 0.1316 0.1577 0.2141 -0.0227 0.0144  0.0087  15  ASN   A OD1 
361  N  ND2 A ASN   A 15  ? 0.1459 0.1774 0.2086 -0.0111 0.0039  0.0443  15  ASN   A ND2 
362  N  ND2 B ASN   A 15  ? 0.1305 0.1551 0.2059 -0.0130 0.0062  0.0396  15  ASN   A ND2 
375  N  N   A VAL   A 16  ? 0.1470 0.1385 0.1803 -0.0194 0.0146  0.0304  16  VAL   A N   
376  N  N   B VAL   A 16  ? 0.1373 0.1516 0.2066 -0.0116 0.0062  0.0369  16  VAL   A N   
377  C  CA  A VAL   A 16  ? 0.1429 0.1364 0.1721 -0.0188 0.0176  0.0081  16  VAL   A CA  
378  C  CA  B VAL   A 16  ? 0.1372 0.1470 0.1822 -0.0123 0.0081  0.0376  16  VAL   A CA  
379  C  C   A VAL   A 16  ? 0.1398 0.1367 0.1608 -0.0182 0.0143  0.0098  16  VAL   A C   
380  C  C   B VAL   A 16  ? 0.1356 0.1507 0.1738 -0.0173 0.0151  0.0354  16  VAL   A C   
381  O  O   A VAL   A 16  ? 0.1342 0.1384 0.1535 -0.0236 0.0242  0.0056  16  VAL   A O   
382  O  O   B VAL   A 16  ? 0.1364 0.1523 0.1798 -0.0207 0.0193  0.0183  16  VAL   A O   
383  C  CB  A VAL   A 16  ? 0.1500 0.1394 0.1840 -0.0094 0.0238  -0.0019 16  VAL   A CB  
384  C  CB  B VAL   A 16  ? 0.1411 0.1330 0.1592 -0.0020 0.0200  0.0260  16  VAL   A CB  
385  C  CG1 A VAL   A 16  ? 0.1591 0.1429 0.1859 -0.0082 0.0097  -0.0171 16  VAL   A CG1 
386  C  CG1 B VAL   A 16  ? 0.1486 0.1285 0.1387 0.0045  0.0141  0.0112  16  VAL   A CG1 
387  C  CG2 A VAL   A 16  ? 0.1592 0.1498 0.1851 -0.0060 0.0288  -0.0122 16  VAL   A CG2 
388  C  CG2 B VAL   A 16  ? 0.1548 0.1465 0.1816 0.0091  0.0264  0.0254  16  VAL   A CG2 
407  N  N   A TYR   A 17  ? 0.1399 0.1328 0.1641 -0.0184 0.0226  0.0093  17  TYR   A N   
408  N  N   B TYR   A 17  ? 0.1377 0.1434 0.1691 -0.0209 0.0186  0.0293  17  TYR   A N   
409  C  CA  A TYR   A 17  ? 0.1433 0.1402 0.1510 -0.0198 0.0247  0.0137  17  TYR   A CA  
410  C  CA  B TYR   A 17  ? 0.1449 0.1463 0.1523 -0.0232 0.0093  0.0302  17  TYR   A CA  
411  C  C   A TYR   A 17  ? 0.1479 0.1302 0.1578 -0.0179 0.0224  0.0005  17  TYR   A C   
412  C  C   B TYR   A 17  ? 0.1385 0.1485 0.1463 -0.0206 0.0100  0.0306  17  TYR   A C   
413  O  O   A TYR   A 17  ? 0.1414 0.1247 0.1514 -0.0218 0.0240  0.0083  17  TYR   A O   
414  O  O   B TYR   A 17  ? 0.1327 0.1456 0.1443 -0.0188 0.0105  0.0296  17  TYR   A O   
415  C  CB  A TYR   A 17  ? 0.1542 0.1528 0.1547 -0.0260 0.0131  0.0211  17  TYR   A CB  
416  C  CB  B TYR   A 17  ? 0.1702 0.1491 0.1584 -0.0246 -0.0024 0.0266  17  TYR   A CB  
417  C  CG  A TYR   A 17  ? 0.1703 0.1634 0.1764 -0.0358 -0.0007 0.0290  17  TYR   A CG  
418  C  CG  B TYR   A 17  ? 0.1949 0.1597 0.1629 -0.0265 -0.0170 0.0200  17  TYR   A CG  
419  C  CD1 A TYR   A 17  ? 0.1820 0.1719 0.1943 -0.0314 -0.0079 0.0235  17  TYR   A CD1 
420  C  CD1 B TYR   A 17  ? 0.2090 0.1723 0.1774 -0.0171 -0.0167 0.0294  17  TYR   A CD1 
421  C  CD2 A TYR   A 17  ? 0.1801 0.1705 0.1788 -0.0479 -0.0020 0.0392  17  TYR   A CD2 
422  C  CD2 B TYR   A 17  ? 0.2063 0.1747 0.1633 -0.0319 -0.0157 0.0123  17  TYR   A CD2 
423  C  CE1 A TYR   A 17  ? 0.1885 0.1692 0.2083 -0.0400 -0.0162 0.0261  17  TYR   A CE1 
424  C  CE1 B TYR   A 17  ? 0.2223 0.1806 0.1911 -0.0145 -0.0173 0.0342  17  TYR   A CE1 
425  C  CE2 A TYR   A 17  ? 0.1903 0.1710 0.1969 -0.0513 -0.0146 0.0288  17  TYR   A CE2 
426  C  CE2 B TYR   A 17  ? 0.2206 0.1823 0.1732 -0.0253 -0.0163 0.0142  17  TYR   A CE2 
427  C  CZ  A TYR   A 17  ? 0.1939 0.1682 0.2120 -0.0487 -0.0218 0.0349  17  TYR   A CZ  
428  C  CZ  B TYR   A 17  ? 0.2250 0.1836 0.1820 -0.0178 -0.0215 0.0334  17  TYR   A CZ  
429  O  OH  A TYR   A 17  ? 0.2039 0.1709 0.2317 -0.0473 -0.0250 0.0361  17  TYR   A OH  
430  O  OH  B TYR   A 17  ? 0.2295 0.1889 0.1969 -0.0130 -0.0199 0.0415  17  TYR   A OH  
449  N  N   A ILE   A 18  ? 0.1546 0.1357 0.1533 -0.0124 0.0254  0.0117  18  ILE   A N   
450  N  N   B ILE   A 18  ? 0.1342 0.1557 0.1564 -0.0206 0.0190  0.0294  18  ILE   A N   
451  C  CA  A ILE   A 18  ? 0.1580 0.1386 0.1532 -0.0136 0.0290  0.0047  18  ILE   A CA  
452  C  CA  B ILE   A 18  ? 0.1416 0.1537 0.1599 -0.0137 0.0209  0.0186  18  ILE   A CA  
453  C  C   A ILE   A 18  ? 0.1583 0.1438 0.1692 -0.0239 0.0307  0.0076  18  ILE   A C   
454  C  C   B ILE   A 18  ? 0.1391 0.1598 0.1629 -0.0177 0.0160  0.0146  18  ILE   A C   
455  O  O   A ILE   A 18  ? 0.1614 0.1496 0.1762 -0.0334 0.0395  0.0140  18  ILE   A O   
456  O  O   B ILE   A 18  ? 0.1361 0.1707 0.1742 -0.0174 0.0327  0.0180  18  ILE   A O   
457  C  CB  A ILE   A 18  ? 0.1643 0.1413 0.1396 -0.0019 0.0287  0.0132  18  ILE   A CB  
458  C  CB  B ILE   A 18  ? 0.1529 0.1441 0.1395 -0.0096 0.0234  0.0267  18  ILE   A CB  
459  C  CG1 A ILE   A 18  ? 0.1697 0.1462 0.1401 0.0137  0.0163  0.0117  18  ILE   A CG1 
460  C  CG1 B ILE   A 18  ? 0.1684 0.1526 0.1483 -0.0045 0.0244  0.0258  18  ILE   A CG1 
461  C  CG2 A ILE   A 18  ? 0.1626 0.1421 0.1529 0.0017  0.0277  -0.0076 18  ILE   A CG2 
462  C  CG2 B ILE   A 18  ? 0.1616 0.1519 0.1426 -0.0132 0.0243  0.0208  18  ILE   A CG2 
463  C  CD1 A ILE   A 18  ? 0.1890 0.1536 0.1594 0.0178  0.0159  0.0043  18  ILE   A CD1 
464  C  CD1 B ILE   A 18  ? 0.1874 0.1644 0.1654 -0.0034 0.0183  0.0182  18  ILE   A CD1 
487  N  N   A LYS   A 19  ? 0.1581 0.1490 0.1878 -0.0247 0.0393  0.0058  19  LYS   A N   
488  N  N   B LYS   A 19  ? 0.1436 0.1621 0.1676 -0.0181 0.0287  0.0093  19  LYS   A N   
489  C  CA  A LYS   A 19  ? 0.1637 0.1601 0.2106 -0.0178 0.0426  0.0119  19  LYS   A CA  
490  C  CA  B LYS   A 19  ? 0.1643 0.1744 0.1929 -0.0078 0.0448  0.0125  19  LYS   A CA  
491  C  C   A LYS   A 19  ? 0.1510 0.1612 0.2356 -0.0101 0.0441  0.0346  19  LYS   A C   
492  C  C   B LYS   A 19  ? 0.1619 0.1764 0.2245 0.0055  0.0486  0.0223  19  LYS   A C   
493  O  O   A LYS   A 19  ? 0.1412 0.1586 0.2362 -0.0102 0.0294  0.0339  19  LYS   A O   
494  O  O   B LYS   A 19  ? 0.1604 0.1676 0.2287 0.0038  0.0395  0.0187  19  LYS   A O   
495  C  CB  A LYS   A 19  ? 0.1730 0.1677 0.2240 -0.0248 0.0473  0.0032  19  LYS   A CB  
496  C  CB  B LYS   A 19  ? 0.1768 0.1821 0.1998 -0.0056 0.0549  -0.0072 19  LYS   A CB  
497  C  CG  A LYS   A 19  ? 0.2031 0.1786 0.2307 -0.0174 0.0483  -0.0104 19  LYS   A CG  
498  C  CG  B LYS   A 19  ? 0.2093 0.1959 0.2079 0.0002  0.0625  -0.0191 19  LYS   A CG  
499  C  CD  A LYS   A 19  ? 0.2203 0.1880 0.2317 -0.0144 0.0606  -0.0173 19  LYS   A CD  
500  C  CD  B LYS   A 19  ? 0.2345 0.2042 0.2169 -0.0043 0.0734  -0.0252 19  LYS   A CD  
501  C  CE  A LYS   A 19  ? 0.2342 0.1898 0.2374 -0.0077 0.0664  -0.0278 19  LYS   A CE  
502  C  CE  B LYS   A 19  ? 0.2536 0.2147 0.2252 -0.0087 0.0772  -0.0251 19  LYS   A CE  
503  N  NZ  A LYS   A 19  ? 0.2404 0.1894 0.2331 -0.0042 0.0817  -0.0338 19  LYS   A NZ  
504  N  NZ  B LYS   A 19  ? 0.2642 0.2208 0.2281 -0.0179 0.0858  -0.0254 19  LYS   A NZ  
531  N  N   A ASN   A 20  ? 0.1584 0.1632 0.2758 -0.0076 0.0502  0.0497  20  ASN   A N   
532  N  N   B ASN   A 20  ? 0.1746 0.1916 0.2668 0.0119  0.0576  0.0276  20  ASN   A N   
533  C  CA  A ASN   A 20  ? 0.1724 0.1770 0.3027 0.0117  0.0643  0.0504  20  ASN   A CA  
534  C  CA  B ASN   A 20  ? 0.1868 0.2100 0.2993 0.0217  0.0669  0.0330  20  ASN   A CA  
535  C  C   A ASN   A 20  ? 0.1831 0.1761 0.2989 0.0123  0.0654  0.0426  20  ASN   A C   
536  C  C   B ASN   A 20  ? 0.2055 0.2104 0.2994 0.0093  0.0744  0.0316  20  ASN   A C   
537  O  O   A ASN   A 20  ? 0.1914 0.1734 0.2944 0.0149  0.0722  0.0414  20  ASN   A O   
538  O  O   B ASN   A 20  ? 0.2208 0.2094 0.3077 0.0072  0.0769  0.0268  20  ASN   A O   
539  C  CB  A ASN   A 20  ? 0.1825 0.1889 0.3363 0.0191  0.0716  0.0700  20  ASN   A CB  
540  C  CB  B ASN   A 20  ? 0.1877 0.2260 0.3363 0.0374  0.0668  0.0454  20  ASN   A CB  
541  C  CG  A ASN   A 20  ? 0.1961 0.2007 0.3808 0.0273  0.0740  0.0823  20  ASN   A CG  
542  C  CG  B ASN   A 20  ? 0.1927 0.2382 0.3814 0.0517  0.0622  0.0560  20  ASN   A CG  
543  O  OD1 A ASN   A 20  ? 0.2212 0.2183 0.4203 0.0358  0.0795  0.0747  20  ASN   A OD1 
544  O  OD1 B ASN   A 20  ? 0.2080 0.2500 0.4211 0.0582  0.0719  0.0509  20  ASN   A OD1 
545  N  ND2 A ASN   A 20  ? 0.1997 0.1969 0.3880 0.0192  0.0649  0.0912  20  ASN   A ND2 
546  N  ND2 B ASN   A 20  ? 0.1983 0.2375 0.3879 0.0496  0.0485  0.0642  20  ASN   A ND2 
559  N  N   A ALA   A 21  ? 0.1848 0.1815 0.3015 0.0085  0.0512  0.0270  21  ALA   A N   
560  N  N   B ALA   A 21  ? 0.2092 0.2109 0.2974 0.0048  0.0649  0.0260  21  ALA   A N   
561  C  CA  A ALA   A 21  ? 0.1831 0.1801 0.2879 0.0039  0.0415  0.0238  21  ALA   A CA  
562  C  CA  B ALA   A 21  ? 0.2090 0.2062 0.2823 0.0004  0.0606  0.0316  21  ALA   A CA  
563  C  C   A ALA   A 21  ? 0.1745 0.1829 0.2789 -0.0070 0.0375  0.0215  21  ALA   A C   
564  C  C   B ALA   A 21  ? 0.1957 0.1945 0.2581 0.0024  0.0661  0.0328  21  ALA   A C   
565  O  O   A ALA   A 21  ? 0.1693 0.1853 0.2868 -0.0074 0.0302  0.0198  21  ALA   A O   
566  O  O   B ALA   A 21  ? 0.1949 0.1827 0.2666 0.0135  0.0659  0.0254  21  ALA   A O   
567  C  CB  A ALA   A 21  ? 0.1903 0.1763 0.2928 0.0071  0.0371  0.0234  21  ALA   A CB  
568  C  CB  B ALA   A 21  ? 0.2195 0.2094 0.3045 -0.0005 0.0468  0.0280  21  ALA   A CB  
579  N  N   A ASP   A 22  ? 0.1801 0.1852 0.2700 -0.0141 0.0405  0.0254  22  ASP   A N   
580  N  N   B ASP   A 22  ? 0.1923 0.1925 0.2406 -0.0033 0.0598  0.0336  22  ASP   A N   
581  C  CA  A ASP   A 22  ? 0.1919 0.1925 0.2584 -0.0104 0.0280  0.0235  22  ASP   A CA  
582  C  CA  B ASP   A 22  ? 0.1901 0.1868 0.2242 -0.0060 0.0467  0.0250  22  ASP   A CA  
583  C  C   A ASP   A 22  ? 0.1863 0.1949 0.2207 -0.0086 0.0296  0.0229  22  ASP   A C   
584  C  C   B ASP   A 22  ? 0.1739 0.1781 0.1965 -0.0158 0.0496  0.0193  22  ASP   A C   
585  O  O   A ASP   A 22  ? 0.1914 0.1999 0.2230 -0.0104 0.0304  0.0196  22  ASP   A O   
586  O  O   B ASP   A 22  ? 0.1714 0.1833 0.1890 -0.0257 0.0483  0.0090  22  ASP   A O   
587  C  CB  A ASP   A 22  ? 0.2117 0.1979 0.2989 -0.0098 0.0196  0.0168  22  ASP   A CB  
588  C  CB  B ASP   A 22  ? 0.2049 0.1911 0.2471 0.0057  0.0410  0.0108  22  ASP   A CB  
589  C  CG  A ASP   A 22  ? 0.2240 0.2015 0.3342 -0.0101 -0.0017 0.0204  22  ASP   A CG  
590  C  CG  B ASP   A 22  ? 0.2124 0.1869 0.2610 0.0088  0.0314  0.0156  22  ASP   A CG  
591  O  OD1 A ASP   A 22  ? 0.2207 0.1950 0.3495 -0.0234 -0.0179 0.0261  22  ASP   A OD1 
592  O  OD1 B ASP   A 22  ? 0.2108 0.1781 0.2423 0.0088  0.0316  0.0209  22  ASP   A OD1 
593  O  OD2 A ASP   A 22  ? 0.2375 0.2089 0.3585 0.0002  0.0010  0.0191  22  ASP   A OD2 
594  O  OD2 B ASP   A 22  ? 0.2165 0.2008 0.2811 0.0057  0.0343  0.0088  22  ASP   A OD2 
603  N  N   A ILE   A 23  ? 0.1834 0.1925 0.1963 -0.0076 0.0310  0.0172  23  ILE   A N   
604  N  N   B ILE   A 23  ? 0.1633 0.1689 0.1817 -0.0116 0.0448  0.0164  23  ILE   A N   
605  C  CA  A ILE   A 23  ? 0.1850 0.1812 0.1852 -0.0019 0.0307  0.0184  23  ILE   A CA  
606  C  CA  B ILE   A 23  ? 0.1539 0.1696 0.1653 -0.0099 0.0304  0.0206  23  ILE   A CA  
607  C  C   A ILE   A 23  ? 0.1898 0.1832 0.1709 -0.0020 0.0425  0.0129  23  ILE   A C   
608  C  C   B ILE   A 23  ? 0.1581 0.1743 0.1677 -0.0198 0.0332  0.0169  23  ILE   A C   
609  O  O   A ILE   A 23  ? 0.1959 0.1824 0.1772 -0.0014 0.0420  0.0142  23  ILE   A O   
610  O  O   B ILE   A 23  ? 0.1616 0.1739 0.1718 -0.0145 0.0281  0.0100  23  ILE   A O   
611  C  CB  A ILE   A 23  ? 0.1893 0.1710 0.1732 0.0049  0.0269  0.0185  23  ILE   A CB  
612  C  CB  B ILE   A 23  ? 0.1521 0.1630 0.1426 -0.0045 0.0188  0.0248  23  ILE   A CB  
613  C  CG1 A ILE   A 23  ? 0.1945 0.1714 0.1713 0.0076  0.0275  0.0155  23  ILE   A CG1 
614  C  CG1 B ILE   A 23  ? 0.1593 0.1608 0.1412 -0.0051 0.0043  0.0118  23  ILE   A CG1 
615  C  CG2 A ILE   A 23  ? 0.1883 0.1664 0.1777 0.0067  0.0235  0.0187  23  ILE   A CG2 
616  C  CG2 B ILE   A 23  ? 0.1498 0.1629 0.1384 0.0036  0.0122  0.0227  23  ILE   A CG2 
617  C  CD1 A ILE   A 23  ? 0.1935 0.1741 0.1668 0.0025  0.0193  0.0134  23  ILE   A CD1 
618  C  CD1 B ILE   A 23  ? 0.1591 0.1580 0.1381 -0.0012 -0.0039 -0.0001 23  ILE   A CD1 
641  N  N   A VAL   A 24  ? 0.1933 0.1885 0.1770 -0.0060 0.0392  0.0089  24  VAL   A N   
642  N  N   B VAL   A 24  ? 0.1694 0.1844 0.1839 -0.0308 0.0302  0.0052  24  VAL   A N   
643  C  CA  A VAL   A 24  ? 0.2047 0.1942 0.1939 -0.0143 0.0373  0.0029  24  VAL   A CA  
644  C  CA  B VAL   A 24  ? 0.1884 0.1985 0.2078 -0.0330 0.0315  -0.0014 24  VAL   A CA  
645  C  C   A VAL   A 24  ? 0.2131 0.2056 0.1984 -0.0213 0.0338  -0.0008 24  VAL   A C   
646  C  C   B VAL   A 24  ? 0.1973 0.2213 0.2105 -0.0331 0.0480  -0.0133 24  VAL   A C   
647  O  O   A VAL   A 24  ? 0.2222 0.2083 0.1973 -0.0140 0.0310  0.0004  24  VAL   A O   
648  O  O   B VAL   A 24  ? 0.2029 0.2277 0.2184 -0.0243 0.0452  -0.0114 24  VAL   A O   
649  C  CB  A VAL   A 24  ? 0.2077 0.1947 0.2137 -0.0128 0.0456  0.0037  24  VAL   A CB  
650  C  CB  B VAL   A 24  ? 0.1955 0.1999 0.2369 -0.0346 0.0255  0.0085  24  VAL   A CB  
651  C  CG1 A VAL   A 24  ? 0.2111 0.1999 0.2224 -0.0070 0.0532  -0.0066 24  VAL   A CG1 
652  C  CG1 B VAL   A 24  ? 0.2089 0.2096 0.2630 -0.0345 0.0174  0.0067  24  VAL   A CG1 
653  C  CG2 A VAL   A 24  ? 0.2118 0.1970 0.2259 -0.0131 0.0569  0.0159  24  VAL   A CG2 
654  C  CG2 B VAL   A 24  ? 0.1987 0.1989 0.2404 -0.0345 0.0347  0.0074  24  VAL   A CG2 
673  N  N   A GLU   A 25  ? 0.2166 0.2231 0.2065 -0.0275 0.0380  -0.0153 25  GLU   A N   
674  N  N   B GLU   A 25  ? 0.2028 0.2402 0.2125 -0.0344 0.0707  -0.0307 25  GLU   A N   
675  C  CA  A GLU   A 25  ? 0.2290 0.2454 0.2177 -0.0255 0.0479  -0.0197 25  GLU   A CA  
676  C  CA  B GLU   A 25  ? 0.2196 0.2643 0.2269 -0.0428 0.0769  -0.0350 25  GLU   A CA  
677  C  C   A GLU   A 25  ? 0.2189 0.2467 0.2014 -0.0341 0.0605  -0.0117 25  GLU   A C   
678  C  C   B GLU   A 25  ? 0.2140 0.2755 0.2107 -0.0450 0.0794  -0.0390 25  GLU   A C   
679  O  O   A GLU   A 25  ? 0.2237 0.2536 0.2079 -0.0280 0.0586  -0.0161 25  GLU   A O   
680  O  O   B GLU   A 25  ? 0.2209 0.2837 0.2130 -0.0395 0.0835  -0.0498 25  GLU   A O   
681  C  CB  A GLU   A 25  ? 0.2509 0.2677 0.2543 -0.0210 0.0447  -0.0219 25  GLU   A CB  
682  C  CB  B GLU   A 25  ? 0.2406 0.2741 0.2471 -0.0470 0.0845  -0.0302 25  GLU   A CB  
683  C  CG  A GLU   A 25  ? 0.2707 0.2856 0.2969 -0.0230 0.0308  -0.0251 25  GLU   A CG  
684  C  CG  B GLU   A 25  ? 0.2647 0.2867 0.2915 -0.0514 0.0739  -0.0253 25  GLU   A CG  
685  C  CD  A GLU   A 25  ? 0.2840 0.3002 0.3356 -0.0289 0.0221  -0.0215 25  GLU   A CD  
686  C  CD  B GLU   A 25  ? 0.2828 0.2989 0.3341 -0.0533 0.0626  -0.0209 25  GLU   A CD  
687  O  OE1 A GLU   A 25  ? 0.2912 0.3057 0.3422 -0.0304 0.0100  -0.0265 25  GLU   A OE1 
688  O  OE1 B GLU   A 25  ? 0.2896 0.3030 0.3549 -0.0514 0.0594  -0.0170 25  GLU   A OE1 
689  O  OE2 A GLU   A 25  ? 0.2853 0.3083 0.3642 -0.0315 0.0246  -0.0202 25  GLU   A OE2 
690  O  OE2 B GLU   A 25  ? 0.2943 0.3038 0.3544 -0.0526 0.0542  -0.0217 25  GLU   A OE2 
703  N  N   A GLU   A 26  ? 0.2110 0.2419 0.2066 -0.0513 0.0679  -0.0098 26  GLU   A N   
704  N  N   B GLU   A 26  ? 0.2117 0.2750 0.2132 -0.0511 0.0739  -0.0369 26  GLU   A N   
705  C  CA  A GLU   A 26  ? 0.2189 0.2417 0.1911 -0.0638 0.0655  -0.0057 26  GLU   A CA  
706  C  CA  B GLU   A 26  ? 0.2187 0.2758 0.2073 -0.0491 0.0661  -0.0290 26  GLU   A CA  
707  C  C   A GLU   A 26  ? 0.2128 0.2391 0.1692 -0.0659 0.0561  -0.0031 26  GLU   A C   
708  C  C   B GLU   A 26  ? 0.2186 0.2686 0.1863 -0.0416 0.0613  -0.0229 26  GLU   A C   
709  O  O   A GLU   A 26  ? 0.2208 0.2375 0.1670 -0.0668 0.0530  -0.0020 26  GLU   A O   
710  O  O   B GLU   A 26  ? 0.2215 0.2664 0.1841 -0.0380 0.0669  -0.0208 26  GLU   A O   
711  C  CB  A GLU   A 26  ? 0.2353 0.2385 0.2165 -0.0731 0.0645  0.0005  26  GLU   A CB  
712  C  CB  B GLU   A 26  ? 0.2282 0.2877 0.2284 -0.0529 0.0531  -0.0274 26  GLU   A CB  
713  C  CG  A GLU   A 26  ? 0.2516 0.2447 0.2672 -0.0748 0.0703  -0.0070 26  GLU   A CG  
714  C  CG  B GLU   A 26  ? 0.2337 0.2984 0.2416 -0.0583 0.0611  -0.0217 26  GLU   A CG  
715  C  CD  A GLU   A 26  ? 0.2655 0.2500 0.2990 -0.0751 0.0917  -0.0075 26  GLU   A CD  
716  C  CD  B GLU   A 26  ? 0.2439 0.3082 0.2429 -0.0661 0.0714  -0.0145 26  GLU   A CD  
717  O  OE1 A GLU   A 26  ? 0.2655 0.2622 0.3067 -0.0656 0.1144  -0.0393 26  GLU   A OE1 
718  O  OE1 B GLU   A 26  ? 0.2474 0.3267 0.2320 -0.0599 0.0883  -0.0231 26  GLU   A OE1 
719  O  OE2 A GLU   A 26  ? 0.2760 0.2548 0.3034 -0.0723 0.0908  0.0068  26  GLU   A OE2 
720  O  OE2 B GLU   A 26  ? 0.2470 0.3043 0.2263 -0.0735 0.0759  -0.0128 26  GLU   A OE2 
733  N  N   A ALA   A 27  ? 0.1965 0.2338 0.1617 -0.0749 0.0558  0.0008  27  ALA   A N   
734  N  N   B ALA   A 27  ? 0.2129 0.2638 0.1725 -0.0367 0.0526  -0.0174 27  ALA   A N   
735  C  CA  A ALA   A 27  ? 0.2017 0.2398 0.1607 -0.0779 0.0540  0.0024  27  ALA   A CA  
736  C  CA  B ALA   A 27  ? 0.2207 0.2670 0.1615 -0.0264 0.0413  -0.0166 27  ALA   A CA  
737  C  C   A ALA   A 27  ? 0.2202 0.2595 0.1706 -0.0817 0.0560  -0.0110 27  ALA   A C   
738  C  C   B ALA   A 27  ? 0.2400 0.2824 0.1680 -0.0202 0.0348  -0.0241 27  ALA   A C   
739  O  O   A ALA   A 27  ? 0.2256 0.2598 0.1713 -0.0857 0.0448  -0.0152 27  ALA   A O   
740  O  O   B ALA   A 27  ? 0.2439 0.2812 0.1652 -0.0196 0.0250  -0.0276 27  ALA   A O   
741  C  CB  A ALA   A 27  ? 0.1922 0.2317 0.1651 -0.0767 0.0386  0.0035  27  ALA   A CB  
742  C  CB  B ALA   A 27  ? 0.2122 0.2587 0.1566 -0.0251 0.0343  -0.0160 27  ALA   A CB  
753  N  N   A LYS   A 28  ? 0.2461 0.2849 0.1875 -0.0713 0.0552  -0.0309 28  LYS   A N   
754  N  N   B LYS   A 28  ? 0.2613 0.3009 0.1785 -0.0125 0.0291  -0.0367 28  LYS   A N   
755  C  CA  A LYS   A 28  ? 0.2827 0.3187 0.2280 -0.0543 0.0488  -0.0409 28  LYS   A CA  
756  C  CA  B LYS   A 28  ? 0.2904 0.3284 0.2138 -0.0027 0.0232  -0.0414 28  LYS   A CA  
757  C  C   A LYS   A 28  ? 0.3006 0.3448 0.2221 -0.0521 0.0674  -0.0296 28  LYS   A C   
758  C  C   B LYS   A 28  ? 0.3122 0.3537 0.2179 -0.0121 0.0413  -0.0279 28  LYS   A C   
759  O  O   A LYS   A 28  ? 0.3006 0.3472 0.2373 -0.0469 0.0533  -0.0285 28  LYS   A O   
760  O  O   B LYS   A 28  ? 0.3176 0.3570 0.2390 -0.0091 0.0300  -0.0275 28  LYS   A O   
761  C  CB  A LYS   A 28  ? 0.2994 0.3303 0.2780 -0.0376 0.0312  -0.0517 28  LYS   A CB  
762  C  CB  B LYS   A 28  ? 0.3014 0.3341 0.2545 0.0145  0.0043  -0.0529 28  LYS   A CB  
763  C  CG  A LYS   A 28  ? 0.3138 0.3400 0.3277 -0.0237 0.0185  -0.0553 28  LYS   A CG  
764  C  CG  B LYS   A 28  ? 0.3129 0.3418 0.3036 0.0268  -0.0098 -0.0570 28  LYS   A CG  
765  C  CD  A LYS   A 28  ? 0.3238 0.3510 0.3802 -0.0135 0.0034  -0.0554 28  LYS   A CD  
766  C  CD  B LYS   A 28  ? 0.3268 0.3543 0.3655 0.0355  -0.0237 -0.0560 28  LYS   A CD  
767  C  CE  A LYS   A 28  ? 0.3297 0.3587 0.4140 -0.0075 -0.0111 -0.0587 28  LYS   A CE  
768  C  CE  B LYS   A 28  ? 0.3387 0.3639 0.4102 0.0391  -0.0339 -0.0564 28  LYS   A CE  
769  N  NZ  A LYS   A 28  ? 0.3341 0.3628 0.4357 -0.0034 -0.0153 -0.0591 28  LYS   A NZ  
770  N  NZ  B LYS   A 28  ? 0.3443 0.3686 0.4326 0.0417  -0.0411 -0.0577 28  LYS   A NZ  
797  N  N   A LYS   A 29  ? 0.3159 0.3673 0.2161 -0.0580 0.0943  -0.0131 29  LYS   A N   
798  N  N   B LYS   A 29  ? 0.3263 0.3749 0.2188 -0.0269 0.0699  -0.0097 29  LYS   A N   
799  C  CA  A LYS   A 29  ? 0.3356 0.3910 0.2382 -0.0621 0.1063  -0.0013 29  LYS   A CA  
800  C  CA  B LYS   A 29  ? 0.3437 0.3963 0.2425 -0.0412 0.0860  0.0002  29  LYS   A CA  
801  C  C   A LYS   A 29  ? 0.3355 0.3921 0.2154 -0.0709 0.1044  0.0045  29  LYS   A C   
802  C  C   B LYS   A 29  ? 0.3394 0.3944 0.2136 -0.0625 0.0951  0.0069  29  LYS   A C   
803  O  O   A LYS   A 29  ? 0.3406 0.3998 0.2336 -0.0661 0.0957  0.0024  29  LYS   A O   
804  O  O   B LYS   A 29  ? 0.3427 0.4006 0.2169 -0.0632 0.0961  0.0120  29  LYS   A O   
805  C  CB  A LYS   A 29  ? 0.3513 0.4114 0.2934 -0.0551 0.1134  0.0020  29  LYS   A CB  
806  C  CB  B LYS   A 29  ? 0.3626 0.4180 0.2993 -0.0325 0.0866  0.0007  29  LYS   A CB  
807  C  CG  A LYS   A 29  ? 0.3670 0.4282 0.3570 -0.0490 0.1126  0.0031  29  LYS   A CG  
808  C  CG  B LYS   A 29  ? 0.3810 0.4365 0.3610 -0.0248 0.0815  -0.0000 29  LYS   A CG  
809  C  CD  A LYS   A 29  ? 0.3811 0.4424 0.4170 -0.0439 0.1090  0.0011  29  LYS   A CD  
810  C  CD  B LYS   A 29  ? 0.3959 0.4521 0.4177 -0.0180 0.0765  -0.0021 29  LYS   A CD  
811  C  CE  A LYS   A 29  ? 0.3900 0.4517 0.4600 -0.0418 0.1066  -0.0006 29  LYS   A CE  
812  C  CE  B LYS   A 29  ? 0.4060 0.4625 0.4598 -0.0138 0.0735  -0.0046 29  LYS   A CE  
813  N  NZ  A LYS   A 29  ? 0.3942 0.4571 0.4879 -0.0403 0.1044  -0.0025 29  LYS   A NZ  
814  N  NZ  B LYS   A 29  ? 0.4116 0.4680 0.4840 -0.0114 0.0723  -0.0084 29  LYS   A NZ  
841  N  N   . VAL   A 30  ? 0.3303 0.3847 0.1976 -0.0814 0.0966  0.0065  30  VAL   A N   
842  C  CA  . VAL   A 30  ? 0.3303 0.3708 0.1705 -0.0997 0.0676  0.0242  30  VAL   A CA  
843  C  C   . VAL   A 30  ? 0.3350 0.3537 0.1316 -0.1016 0.0434  0.0277  30  VAL   A C   
844  O  O   . VAL   A 30  ? 0.3428 0.3558 0.1385 -0.1059 0.0333  0.0327  30  VAL   A O   
845  C  CB  . VAL   A 30  ? 0.3267 0.3671 0.2193 -0.1098 0.0438  0.0314  30  VAL   A CB  
846  C  CG1 . VAL   A 30  ? 0.3290 0.3651 0.2339 -0.1121 0.0277  0.0343  30  VAL   A CG1 
847  C  CG2 . VAL   A 30  ? 0.3271 0.3692 0.2617 -0.1138 0.0441  0.0334  30  VAL   A CG2 
858  N  N   . LYS   A 31  ? 0.3310 0.3378 0.1294 -0.1070 0.0289  0.0211  31  LYS   A N   
859  C  CA  . LYS   A 31  ? 0.3488 0.3367 0.1432 -0.0942 0.0041  0.0177  31  LYS   A CA  
860  C  C   . LYS   A 31  ? 0.3221 0.3116 0.1154 -0.0756 -0.0003 0.0545  31  LYS   A C   
861  O  O   . LYS   A 31  ? 0.3293 0.3228 0.1428 -0.0670 -0.0147 0.0652  31  LYS   A O   
862  C  CB  . LYS   A 31  ? 0.3969 0.3663 0.2564 -0.0897 -0.0152 -0.0054 31  LYS   A CB  
863  C  CG  . LYS   A 31  ? 0.4428 0.3978 0.4022 -0.0760 -0.0312 -0.0213 31  LYS   A CG  
864  C  CD  . LYS   A 31  ? 0.4841 0.4228 0.5096 -0.0657 -0.0452 -0.0348 31  LYS   A CD  
865  C  CE  . LYS   A 31  ? 0.5139 0.4429 0.5773 -0.0578 -0.0576 -0.0467 31  LYS   A CE  
866  N  NZ  . LYS   A 31  ? 0.5245 0.4495 0.6127 -0.0540 -0.0640 -0.0531 31  LYS   A NZ  
880  N  N   . PRO   A 32  ? 0.2843 0.2781 0.1065 -0.0691 0.0049  0.0465  32  PRO   A N   
881  C  CA  . PRO   A 32  ? 0.2736 0.2592 0.1489 -0.0649 -0.0106 0.0580  32  PRO   A CA  
882  C  C   . PRO   A 32  ? 0.2677 0.2523 0.1631 -0.0553 -0.0191 0.0668  32  PRO   A C   
883  O  O   . PRO   A 32  ? 0.2608 0.2454 0.1651 -0.0583 -0.0374 0.0683  32  PRO   A O   
884  C  CB  . PRO   A 32  ? 0.2669 0.2613 0.1605 -0.0643 -0.0196 0.0444  32  PRO   A CB  
885  C  CG  . PRO   A 32  ? 0.2637 0.2646 0.1103 -0.0596 -0.0230 0.0391  32  PRO   A CG  
886  C  CD  . PRO   A 32  ? 0.2678 0.2655 0.1052 -0.0628 -0.0070 0.0379  32  PRO   A CD  
894  N  N   . THR   A 33  ? 0.2676 0.2489 0.1552 -0.0514 -0.0152 0.0700  33  THR   A N   
895  C  CA  . THR   A 33  ? 0.2637 0.2460 0.1659 -0.0381 -0.0316 0.0641  33  THR   A CA  
896  C  C   . THR   A 33  ? 0.2305 0.2252 0.1485 -0.0422 -0.0290 0.0471  33  THR   A C   
897  O  O   . THR   A 33  ? 0.2222 0.2245 0.1566 -0.0401 -0.0473 0.0471  33  THR   A O   
898  C  CB  . THR   A 33  ? 0.2868 0.2637 0.1739 -0.0255 -0.0366 0.0834  33  THR   A CB  
899  O  OG1 . THR   A 33  ? 0.3106 0.2792 0.2108 -0.0114 -0.0226 0.0900  33  THR   A OG1 
900  C  CG2 . THR   A 33  ? 0.2901 0.2705 0.1943 -0.0216 -0.0385 0.0830  33  THR   A CG2 
908  N  N   . VAL   A 34  ? 0.2048 0.2054 0.1428 -0.0433 -0.0171 0.0446  34  VAL   A N   
909  C  CA  . VAL   A 34  ? 0.1941 0.1866 0.1278 -0.0310 -0.0068 0.0452  34  VAL   A CA  
910  C  C   . VAL   A 34  ? 0.1785 0.1777 0.1236 -0.0287 -0.0065 0.0342  34  VAL   A C   
911  O  O   . VAL   A 34  ? 0.1772 0.1799 0.1513 -0.0383 -0.0037 0.0414  34  VAL   A O   
912  C  CB  . VAL   A 34  ? 0.1959 0.1815 0.1560 -0.0253 -0.0081 0.0316  34  VAL   A CB  
913  C  CG1 . VAL   A 34  ? 0.1996 0.1806 0.1669 -0.0229 -0.0023 0.0232  34  VAL   A CG1 
914  C  CG2 . VAL   A 34  ? 0.1965 0.1975 0.1823 -0.0167 -0.0209 0.0297  34  VAL   A CG2 
924  N  N   . VAL   A 35  ? 0.1621 0.1644 0.1241 -0.0286 -0.0073 0.0314  35  VAL   A N   
925  C  CA  . VAL   A 35  ? 0.1521 0.1597 0.1167 -0.0266 0.0017  0.0258  35  VAL   A CA  
926  C  C   . VAL   A 35  ? 0.1409 0.1428 0.1216 -0.0219 0.0032  0.0202  35  VAL   A C   
927  O  O   . VAL   A 35  ? 0.1357 0.1525 0.1418 -0.0223 0.0084  0.0158  35  VAL   A O   
928  C  CB  . VAL   A 35  ? 0.1612 0.1705 0.1248 -0.0188 0.0120  0.0132  35  VAL   A CB  
929  C  CG1 . VAL   A 35  ? 0.1733 0.1697 0.1366 -0.0113 0.0076  0.0011  35  VAL   A CG1 
930  C  CG2 . VAL   A 35  ? 0.1577 0.1711 0.1569 -0.0171 0.0143  0.0041  35  VAL   A CG2 
940  N  N   A VAL   A 36  ? 0.1334 0.1414 0.1187 -0.0206 0.0046  0.0228  36  VAL   A N   
941  N  N   B VAL   A 36  ? 0.1314 0.1383 0.1194 -0.0232 0.0060  0.0241  36  VAL   A N   
942  C  CA  A VAL   A 36  ? 0.1263 0.1351 0.1195 -0.0115 0.0005  0.0137  36  VAL   A CA  
943  C  CA  B VAL   A 36  ? 0.1249 0.1302 0.1268 -0.0176 0.0018  0.0146  36  VAL   A CA  
944  C  C   A VAL   A 36  ? 0.1299 0.1342 0.1154 -0.0045 0.0064  0.0099  36  VAL   A C   
945  C  C   B VAL   A 36  ? 0.1181 0.1276 0.1288 -0.0228 0.0072  0.0152  36  VAL   A C   
946  O  O   A VAL   A 36  ? 0.1413 0.1355 0.1236 0.0033  0.0060  -0.0071 36  VAL   A O   
947  O  O   B VAL   A 36  ? 0.1222 0.1167 0.1431 -0.0147 0.0199  0.0101  36  VAL   A O   
948  C  CB  A VAL   A 36  ? 0.1159 0.1237 0.1284 -0.0104 -0.0040 0.0231  36  VAL   A CB  
949  C  CB  B VAL   A 36  ? 0.1258 0.1186 0.1446 -0.0108 0.0023  0.0118  36  VAL   A CB  
950  C  CG1 A VAL   A 36  ? 0.1034 0.1259 0.1357 -0.0020 -0.0051 -0.0015 36  VAL   A CG1 
951  C  CG1 B VAL   A 36  ? 0.1330 0.1086 0.1473 -0.0037 -0.0055 0.0121  36  VAL   A CG1 
952  C  CG2 A VAL   A 36  ? 0.1281 0.1305 0.1448 -0.0077 -0.0074 0.0281  36  VAL   A CG2 
953  C  CG2 B VAL   A 36  ? 0.1355 0.1198 0.1669 -0.0031 0.0050  0.0070  36  VAL   A CG2 
972  N  N   A ASN   A 37  ? 0.1255 0.1286 0.1166 0.0057  0.0057  0.0131  37  ASN   A N   
973  N  N   B ASN   A 37  ? 0.1106 0.1218 0.1345 -0.0173 0.0021  0.0119  37  ASN   A N   
974  C  CA  A ASN   A 37  ? 0.1266 0.1278 0.1113 0.0050  0.0007  0.0213  37  ASN   A CA  
975  C  CA  B ASN   A 37  ? 0.1109 0.1170 0.1262 -0.0079 0.0021  0.0159  37  ASN   A CA  
976  C  C   A ASN   A 37  ? 0.1287 0.1287 0.1101 -0.0021 0.0150  0.0222  37  ASN   A C   
977  C  C   B ASN   A 37  ? 0.1079 0.1127 0.1327 0.0016  0.0130  0.0176  37  ASN   A C   
978  O  O   A ASN   A 37  ? 0.1362 0.1407 0.1275 0.0001  0.0070  0.0123  37  ASN   A O   
979  O  O   B ASN   A 37  ? 0.1076 0.1230 0.1371 0.0130  0.0089  0.0062  37  ASN   A O   
980  C  CB  A ASN   A 37  ? 0.1256 0.1278 0.1123 0.0064  -0.0029 0.0151  37  ASN   A CB  
981  C  CB  B ASN   A 37  ? 0.1186 0.1151 0.1349 -0.0046 0.0069  0.0065  37  ASN   A CB  
982  C  CG  A ASN   A 37  ? 0.1241 0.1260 0.1061 0.0082  -0.0009 0.0058  37  ASN   A CG  
983  C  CG  B ASN   A 37  ? 0.1206 0.1124 0.1426 -0.0056 0.0105  -0.0003 37  ASN   A CG  
984  O  OD1 A ASN   A 37  ? 0.1280 0.1253 0.1075 0.0078  -0.0033 0.0035  37  ASN   A OD1 
985  O  OD1 B ASN   A 37  ? 0.1195 0.1186 0.1335 -0.0090 0.0053  0.0028  37  ASN   A OD1 
986  N  ND2 A ASN   A 37  ? 0.1226 0.1255 0.1025 0.0066  -0.0059 0.0139  37  ASN   A ND2 
987  N  ND2 B ASN   A 37  ? 0.1226 0.1067 0.1350 -0.0088 0.0083  0.0070  37  ASN   A ND2 
1000 N  N   A ALA   A 38  ? 0.1263 0.1286 0.1081 -0.0008 0.0100  0.0115  38  ALA   A N   
1001 N  N   B ALA   A 38  ? 0.1141 0.1145 0.1404 0.0026  0.0046  0.0053  38  ALA   A N   
1002 C  CA  A ALA   A 38  ? 0.1255 0.1160 0.0999 0.0019  0.0085  0.0017  38  ALA   A CA  
1003 C  CA  B ALA   A 38  ? 0.1238 0.1210 0.1510 -0.0019 -0.0013 0.0049  38  ALA   A CA  
1004 C  C   A ALA   A 38  ? 0.1281 0.1250 0.1053 0.0030  0.0017  0.0020  38  ALA   A C   
1005 C  C   B ALA   A 38  ? 0.1204 0.1216 0.1446 0.0042  -0.0072 -0.0037 38  ALA   A C   
1006 O  O   A ALA   A 38  ? 0.1285 0.1169 0.1041 -0.0035 -0.0116 -0.0091 38  ALA   A O   
1007 O  O   B ALA   A 38  ? 0.1126 0.1151 0.1577 0.0005  -0.0168 -0.0033 38  ALA   A O   
1008 C  CB  A ALA   A 38  ? 0.1225 0.1237 0.1071 -0.0093 0.0018  -0.0037 38  ALA   A CB  
1009 C  CB  B ALA   A 38  ? 0.1317 0.1252 0.1659 -0.0029 -0.0100 -0.0069 38  ALA   A CB  
1020 N  N   A ALA   A 39  ? 0.1266 0.1195 0.1142 0.0056  0.0167  0.0085  39  ALA   A N   
1021 N  N   B ALA   A 39  ? 0.1285 0.1314 0.1486 0.0013  -0.0023 0.0066  39  ALA   A N   
1022 C  CA  A ALA   A 39  ? 0.1203 0.1185 0.1260 0.0093  0.0153  0.0070  39  ALA   A CA  
1023 C  CA  B ALA   A 39  ? 0.1307 0.1379 0.1390 -0.0010 -0.0107 0.0114  39  ALA   A CA  
1024 C  C   A ALA   A 39  ? 0.1229 0.1252 0.1247 0.0023  0.0012  0.0058  39  ALA   A C   
1025 C  C   B ALA   A 39  ? 0.1199 0.1282 0.1327 -0.0036 -0.0103 0.0085  39  ALA   A C   
1026 O  O   A ALA   A 39  ? 0.1309 0.1298 0.1208 -0.0078 0.0082  0.0160  39  ALA   A O   
1027 O  O   B ALA   A 39  ? 0.1381 0.1254 0.1400 -0.0025 -0.0062 0.0017  39  ALA   A O   
1028 C  CB  A ALA   A 39  ? 0.1114 0.1163 0.1425 0.0077  0.0056  0.0126  39  ALA   A CB  
1029 C  CB  B ALA   A 39  ? 0.1402 0.1516 0.1447 -0.0029 -0.0226 0.0108  39  ALA   A CB  
1040 N  N   A ASN   A 40  ? 0.1238 0.1272 0.1326 -0.0015 0.0078  -0.0046 40  ASN   A N   
1041 N  N   B ASN   A 40  ? 0.1221 0.1231 0.1280 -0.0061 0.0054  0.0123  40  ASN   A N   
1042 C  CA  A ASN   A 40  ? 0.1315 0.1217 0.1300 0.0008  -0.0037 -0.0014 40  ASN   A CA  
1043 C  CA  B ASN   A 40  ? 0.1239 0.1162 0.1382 -0.0022 -0.0091 0.0194  40  ASN   A CA  
1044 C  C   A ASN   A 40  ? 0.1316 0.1173 0.1103 -0.0041 -0.0007 0.0030  40  ASN   A C   
1045 C  C   B ASN   A 40  ? 0.1285 0.1143 0.1267 -0.0059 0.0012  0.0235  40  ASN   A C   
1046 O  O   A ASN   A 40  ? 0.1306 0.1217 0.1069 -0.0108 0.0033  0.0087  40  ASN   A O   
1047 O  O   B ASN   A 40  ? 0.1197 0.1205 0.1281 -0.0050 0.0023  0.0246  40  ASN   A O   
1048 C  CB  A ASN   A 40  ? 0.1400 0.1362 0.1392 0.0038  -0.0135 -0.0055 40  ASN   A CB  
1049 C  CB  B ASN   A 40  ? 0.1363 0.1247 0.1519 0.0016  -0.0100 0.0155  40  ASN   A CB  
1050 C  CG  A ASN   A 40  ? 0.1555 0.1424 0.1628 0.0023  -0.0105 0.0060  40  ASN   A CG  
1051 C  CG  B ASN   A 40  ? 0.1394 0.1278 0.1546 -0.0001 -0.0143 0.0166  40  ASN   A CG  
1052 O  OD1 A ASN   A 40  ? 0.1640 0.1425 0.1670 0.0058  -0.0298 0.0071  40  ASN   A OD1 
1053 O  OD1 B ASN   A 40  ? 0.1504 0.1375 0.1673 -0.0020 -0.0037 0.0040  40  ASN   A OD1 
1054 N  ND2 A ASN   A 40  ? 0.1642 0.1583 0.1880 0.0050  0.0057  -0.0019 40  ASN   A ND2 
1055 N  ND2 B ASN   A 40  ? 0.1360 0.1351 0.1773 -0.0062 0.0062  -0.0045 40  ASN   A ND2 
1068 N  N   A VAL   A 41  ? 0.1336 0.1195 0.1017 -0.0017 0.0009  -0.0004 41  VAL   A N   
1069 N  N   B VAL   A 41  ? 0.1315 0.1203 0.1313 -0.0025 -0.0011 0.0245  41  VAL   A N   
1070 C  CA  A VAL   A 41  ? 0.1237 0.1248 0.1120 -0.0001 0.0078  0.0038  41  VAL   A CA  
1071 C  CA  B VAL   A 41  ? 0.1377 0.1288 0.1370 -0.0074 -0.0017 0.0212  41  VAL   A CA  
1072 C  C   A VAL   A 41  ? 0.1241 0.1261 0.1220 0.0017  0.0073  0.0081  41  VAL   A C   
1073 C  C   B VAL   A 41  ? 0.1332 0.1242 0.1308 -0.0059 0.0072  0.0160  41  VAL   A C   
1074 O  O   A VAL   A 41  ? 0.1336 0.1233 0.1155 0.0031  -0.0053 0.0026  41  VAL   A O   
1075 O  O   B VAL   A 41  ? 0.1466 0.1173 0.1195 -0.0001 0.0011  0.0120  41  VAL   A O   
1076 C  CB  A VAL   A 41  ? 0.1230 0.1311 0.1084 -0.0006 0.0081  0.0058  41  VAL   A CB  
1077 C  CB  B VAL   A 41  ? 0.1527 0.1479 0.1480 -0.0067 0.0102  0.0200  41  VAL   A CB  
1078 C  CG1 A VAL   A 41  ? 0.1292 0.1380 0.1178 0.0064  0.0003  -0.0058 41  VAL   A CG1 
1079 C  CG1 B VAL   A 41  ? 0.1680 0.1587 0.1456 -0.0098 0.0179  0.0088  41  VAL   A CG1 
1080 C  CG2 A VAL   A 41  ? 0.1274 0.1342 0.1048 -0.0006 0.0132  0.0013  41  VAL   A CG2 
1081 C  CG2 B VAL   A 41  ? 0.1562 0.1546 0.1667 -0.0093 0.0000  0.0160  41  VAL   A CG2 
1100 N  N   A TYR   A 42  ? 0.1102 0.1236 0.1365 -0.0075 0.0100  0.0100  42  TYR   A N   
1101 N  N   B TYR   A 42  ? 0.1207 0.1235 0.1438 -0.0045 0.0127  0.0279  42  TYR   A N   
1102 C  CA  A TYR   A 42  ? 0.1178 0.1212 0.1405 -0.0124 0.0047  0.0149  42  TYR   A CA  
1103 C  CA  B TYR   A 42  ? 0.1261 0.1221 0.1499 -0.0021 0.0170  0.0282  42  TYR   A CA  
1104 C  C   A TYR   A 42  ? 0.1154 0.1116 0.1504 -0.0110 0.0073  0.0078  42  TYR   A C   
1105 C  C   B TYR   A 42  ? 0.1302 0.1246 0.1413 -0.0012 0.0144  0.0311  42  TYR   A C   
1106 O  O   A TYR   A 42  ? 0.1152 0.1131 0.1640 -0.0172 0.0043  0.0035  42  TYR   A O   
1107 O  O   B TYR   A 42  ? 0.1316 0.1330 0.1571 -0.0126 0.0090  0.0162  42  TYR   A O   
1108 C  CB  A TYR   A 42  ? 0.1376 0.1365 0.1296 -0.0091 0.0044  0.0245  42  TYR   A CB  
1109 C  CB  B TYR   A 42  ? 0.1387 0.1213 0.1636 0.0006  0.0070  0.0268  42  TYR   A CB  
1110 C  CG  A TYR   A 42  ? 0.1554 0.1480 0.1276 -0.0122 0.0046  0.0340  42  TYR   A CG  
1111 C  CG  B TYR   A 42  ? 0.1515 0.1370 0.1560 0.0025  0.0050  0.0259  42  TYR   A CG  
1112 C  CD1 A TYR   A 42  ? 0.1686 0.1657 0.1452 -0.0180 0.0127  0.0236  42  TYR   A CD1 
1113 C  CD1 B TYR   A 42  ? 0.1563 0.1508 0.1475 0.0020  0.0149  0.0320  42  TYR   A CD1 
1114 C  CD2 A TYR   A 42  ? 0.1682 0.1653 0.1439 -0.0055 -0.0061 0.0272  42  TYR   A CD2 
1115 C  CD2 B TYR   A 42  ? 0.1671 0.1607 0.1714 0.0082  0.0032  0.0167  42  TYR   A CD2 
1116 C  CE1 A TYR   A 42  ? 0.1811 0.1740 0.1412 -0.0197 0.0158  0.0234  42  TYR   A CE1 
1117 C  CE1 B TYR   A 42  ? 0.1681 0.1638 0.1545 -0.0040 0.0270  0.0247  42  TYR   A CE1 
1118 C  CE2 A TYR   A 42  ? 0.1811 0.1777 0.1556 -0.0155 -0.0080 0.0271  42  TYR   A CE2 
1119 C  CE2 B TYR   A 42  ? 0.1864 0.1779 0.1847 0.0002  0.0120  0.0202  42  TYR   A CE2 
1120 C  CZ  A TYR   A 42  ? 0.1927 0.1823 0.1440 -0.0220 0.0035  0.0275  42  TYR   A CZ  
1121 C  CZ  B TYR   A 42  ? 0.1905 0.1790 0.1649 -0.0075 0.0239  0.0173  42  TYR   A CZ  
1122 O  OH  A TYR   A 42  ? 0.2118 0.1990 0.1745 -0.0262 0.0047  0.0256  42  TYR   A OH  
1123 O  OH  B TYR   A 42  ? 0.2042 0.2023 0.1873 -0.0185 0.0318  0.0086  42  TYR   A OH  
1142 N  N   A LEU   A 43  ? 0.1228 0.1115 0.1522 -0.0132 0.0062  -0.0082 43  LEU   A N   
1143 N  N   B LEU   A 43  ? 0.1315 0.1304 0.1454 -0.0019 0.0131  0.0244  43  LEU   A N   
1144 C  CA  A LEU   A 43  ? 0.1214 0.1070 0.1465 -0.0092 0.0049  -0.0085 43  LEU   A CA  
1145 C  CA  B LEU   A 43  ? 0.1263 0.1292 0.1401 -0.0005 0.0120  0.0238  43  LEU   A CA  
1146 C  C   A LEU   A 43  ? 0.1275 0.1156 0.1480 -0.0067 0.0060  -0.0077 43  LEU   A C   
1147 C  C   B LEU   A 43  ? 0.1291 0.1357 0.1347 0.0005  0.0038  0.0142  43  LEU   A C   
1148 O  O   A LEU   A 43  ? 0.1428 0.1151 0.1482 -0.0036 0.0058  -0.0029 43  LEU   A O   
1149 O  O   B LEU   A 43  ? 0.1413 0.1403 0.1354 0.0087  0.0019  0.0198  43  LEU   A O   
1150 C  CB  A LEU   A 43  ? 0.1291 0.1150 0.1535 -0.0051 -0.0022 -0.0113 43  LEU   A CB  
1151 C  CB  B LEU   A 43  ? 0.1243 0.1281 0.1456 -0.0064 0.0110  0.0304  43  LEU   A CB  
1152 C  CG  A LEU   A 43  ? 0.1321 0.1189 0.1624 -0.0081 -0.0036 -0.0100 43  LEU   A CG  
1153 C  CG  B LEU   A 43  ? 0.1196 0.1271 0.1561 -0.0024 0.0088  0.0276  43  LEU   A CG  
1154 C  CD1 A LEU   A 43  ? 0.1304 0.1257 0.1863 -0.0074 -0.0137 -0.0018 43  LEU   A CD1 
1155 C  CD1 B LEU   A 43  ? 0.1265 0.1321 0.1910 -0.0032 0.0036  0.0305  43  LEU   A CD1 
1156 C  CD2 A LEU   A 43  ? 0.1407 0.1251 0.1567 -0.0067 -0.0078 -0.0062 43  LEU   A CD2 
1157 C  CD2 B LEU   A 43  ? 0.1264 0.1280 0.1478 -0.0018 -0.0008 0.0350  43  LEU   A CD2 
1180 N  N   A LYS   A 44  ? 0.1274 0.1177 0.1508 -0.0081 0.0084  -0.0037 44  LYS   A N   
1181 N  N   B LYS   A 44  ? 0.1232 0.1308 0.1339 0.0010  -0.0054 0.0190  44  LYS   A N   
1182 C  CA  A LYS   A 44  ? 0.1311 0.1229 0.1660 -0.0117 0.0182  0.0073  44  LYS   A CA  
1183 C  CA  B LYS   A 44  ? 0.1338 0.1309 0.1405 0.0015  -0.0057 0.0295  44  LYS   A CA  
1184 C  C   A LYS   A 44  ? 0.1219 0.1220 0.1474 -0.0005 0.0125  0.0049  44  LYS   A C   
1185 C  C   B LYS   A 44  ? 0.1254 0.1265 0.1330 0.0025  -0.0086 0.0143  44  LYS   A C   
1186 O  O   A LYS   A 44  ? 0.1279 0.1399 0.1648 0.0032  0.0012  -0.0008 44  LYS   A O   
1187 O  O   B LYS   A 44  ? 0.1291 0.1375 0.1447 -0.0033 -0.0011 -0.0018 44  LYS   A O   
1188 C  CB  A LYS   A 44  ? 0.1501 0.1379 0.2004 -0.0136 0.0194  0.0153  44  LYS   A CB  
1189 C  CB  B LYS   A 44  ? 0.1582 0.1454 0.1926 0.0144  0.0085  0.0404  44  LYS   A CB  
1190 C  CG  A LYS   A 44  ? 0.1768 0.1578 0.2506 -0.0170 0.0374  0.0259  44  LYS   A CG  
1191 C  CG  B LYS   A 44  ? 0.1808 0.1712 0.2738 0.0201  0.0256  0.0424  44  LYS   A CG  
1192 C  CD  A LYS   A 44  ? 0.2045 0.1980 0.3371 -0.0156 0.0368  0.0197  44  LYS   A CD  
1193 C  CD  B LYS   A 44  ? 0.2109 0.2151 0.3759 0.0146  0.0107  0.0372  44  LYS   A CD  
1194 C  CE  A LYS   A 44  ? 0.2144 0.2187 0.3865 0.0015  0.0408  0.0182  44  LYS   A CE  
1195 C  CE  B LYS   A 44  ? 0.2201 0.2323 0.4401 0.0150  0.0023  0.0406  44  LYS   A CE  
1196 N  NZ  A LYS   A 44  ? 0.2165 0.2302 0.4051 0.0104  0.0439  0.0138  44  LYS   A NZ  
1197 N  NZ  B LYS   A 44  ? 0.2269 0.2447 0.4810 0.0132  -0.0029 0.0470  44  LYS   A NZ  
1224 N  N   A HIS   A 45  ? 0.1201 0.1161 0.1425 0.0031  0.0150  0.0063  45  HIS   A N   
1225 N  N   B HIS   A 45  ? 0.1363 0.1258 0.1427 -0.0023 -0.0148 0.0088  45  HIS   A N   
1226 C  CA  A HIS   A 45  ? 0.1159 0.1204 0.1423 0.0068  0.0115  0.0085  45  HIS   A CA  
1227 C  CA  B HIS   A 45  ? 0.1383 0.1324 0.1496 -0.0030 -0.0177 0.0136  45  HIS   A CA  
1228 C  C   A HIS   A 45  ? 0.1155 0.1288 0.1463 0.0056  0.0112  0.0093  45  HIS   A C   
1229 C  C   B HIS   A 45  ? 0.1453 0.1408 0.1623 -0.0014 -0.0155 0.0167  45  HIS   A C   
1230 O  O   A HIS   A 45  ? 0.1174 0.1165 0.1601 0.0066  0.0059  -0.0053 45  HIS   A O   
1231 O  O   B HIS   A 45  ? 0.1536 0.1443 0.1845 0.0106  -0.0150 0.0114  45  HIS   A O   
1232 C  CB  A HIS   A 45  ? 0.1223 0.1149 0.1397 0.0055  0.0127  0.0085  45  HIS   A CB  
1233 C  CB  B HIS   A 45  ? 0.1311 0.1271 0.1502 -0.0021 -0.0155 0.0031  45  HIS   A CB  
1234 C  CG  A HIS   A 45  ? 0.1247 0.1063 0.1147 0.0030  0.0101  0.0101  45  HIS   A CG  
1235 C  CG  B HIS   A 45  ? 0.1210 0.1274 0.1373 -0.0082 0.0041  -0.0023 45  HIS   A CG  
1236 N  ND1 A HIS   A 45  ? 0.1224 0.1129 0.1149 0.0030  0.0054  0.0099  45  HIS   A ND1 
1237 N  ND1 B HIS   A 45  ? 0.1130 0.1353 0.1635 -0.0061 0.0060  0.0068  45  HIS   A ND1 
1238 C  CD2 A HIS   A 45  ? 0.1293 0.1160 0.1288 0.0016  0.0016  0.0183  45  HIS   A CD2 
1239 C  CD2 B HIS   A 45  ? 0.1149 0.1256 0.1265 -0.0075 0.0006  -0.0076 45  HIS   A CD2 
1240 C  CE1 A HIS   A 45  ? 0.1280 0.1222 0.1171 -0.0014 0.0007  0.0270  45  HIS   A CE1 
1241 C  CE1 B HIS   A 45  ? 0.1108 0.1270 0.1329 -0.0092 0.0046  -0.0033 45  HIS   A CE1 
1242 N  NE2 A HIS   A 45  ? 0.1304 0.1194 0.1266 0.0065  0.0029  0.0318  45  HIS   A NE2 
1243 N  NE2 B HIS   A 45  ? 0.1135 0.1235 0.1206 -0.0061 -0.0025 -0.0121 45  HIS   A NE2 
1258 N  N   A GLY   A 46  ? 0.1178 0.1426 0.1569 0.0128  -0.0006 0.0192  46  GLY   A N   
1259 N  N   B GLY   A 46  ? 0.1456 0.1394 0.1647 -0.0067 -0.0190 0.0194  46  GLY   A N   
1260 C  CA  A GLY   A 46  ? 0.1202 0.1433 0.1766 0.0103  -0.0061 0.0325  46  GLY   A CA  
1261 C  CA  B GLY   A 46  ? 0.1391 0.1468 0.1762 -0.0067 -0.0107 0.0222  46  GLY   A CA  
1262 C  C   A GLY   A 46  ? 0.1280 0.1390 0.1613 0.0133  -0.0097 0.0446  46  GLY   A C   
1263 C  C   B GLY   A 46  ? 0.1386 0.1475 0.1620 0.0035  -0.0018 0.0267  46  GLY   A C   
1264 O  O   A GLY   A 46  ? 0.1404 0.1337 0.1663 0.0163  -0.0124 0.0498  46  GLY   A O   
1265 O  O   B GLY   A 46  ? 0.1483 0.1522 0.1574 0.0099  -0.0009 0.0219  46  GLY   A O   
1272 N  N   A GLY   A 47  ? 0.1275 0.1368 0.1531 0.0123  -0.0132 0.0381  47  GLY   A N   
1273 N  N   B GLY   A 47  ? 0.1410 0.1482 0.1687 0.0069  -0.0018 0.0213  47  GLY   A N   
1274 C  CA  A GLY   A 47  ? 0.1361 0.1441 0.1507 0.0162  -0.0134 0.0258  47  GLY   A CA  
1275 C  CA  B GLY   A 47  ? 0.1357 0.1518 0.1608 0.0061  -0.0124 0.0276  47  GLY   A CA  
1276 C  C   A GLY   A 47  ? 0.1328 0.1352 0.1399 0.0185  -0.0009 0.0143  47  GLY   A C   
1277 C  C   B GLY   A 47  ? 0.1285 0.1413 0.1295 0.0070  -0.0111 0.0122  47  GLY   A C   
1278 O  O   A GLY   A 47  ? 0.1339 0.1264 0.1575 0.0258  0.0050  0.0175  47  GLY   A O   
1279 O  O   B GLY   A 47  ? 0.1249 0.1382 0.1328 0.0062  -0.0091 0.0227  47  GLY   A O   
1286 N  N   A GLY   A 48  ? 0.1301 0.1398 0.1277 0.0161  -0.0014 0.0063  48  GLY   A N   
1287 N  N   B GLY   A 48  ? 0.1260 0.1406 0.1374 0.0089  -0.0061 0.0120  48  GLY   A N   
1288 C  CA  A GLY   A 48  ? 0.1232 0.1398 0.1416 0.0061  0.0094  0.0007  48  GLY   A CA  
1289 C  CA  B GLY   A 48  ? 0.1320 0.1295 0.1257 0.0019  -0.0026 -0.0003 48  GLY   A CA  
1290 C  C   A GLY   A 48  ? 0.1218 0.1387 0.1368 0.0001  0.0079  0.0002  48  GLY   A C   
1291 C  C   B GLY   A 48  ? 0.1338 0.1284 0.1291 -0.0071 0.0040  0.0081  48  GLY   A C   
1292 O  O   A GLY   A 48  ? 0.1366 0.1393 0.1294 -0.0007 -0.0032 0.0066  48  GLY   A O   
1293 O  O   B GLY   A 48  ? 0.1421 0.1301 0.1284 -0.0020 0.0085  -0.0044 48  GLY   A O   
1300 N  N   A VAL   A 49  ? 0.1249 0.1404 0.1556 -0.0049 -0.0037 0.0057  49  VAL   A N   
1301 N  N   B VAL   A 49  ? 0.1245 0.1224 0.1354 -0.0090 -0.0074 0.0029  49  VAL   A N   
1302 C  CA  A VAL   A 49  ? 0.1359 0.1345 0.1551 -0.0014 0.0005  0.0084  49  VAL   A CA  
1303 C  CA  B VAL   A 49  ? 0.1243 0.1266 0.1442 -0.0052 -0.0022 0.0048  49  VAL   A CA  
1304 C  C   A VAL   A 49  ? 0.1329 0.1280 0.1351 -0.0022 0.0005  0.0127  49  VAL   A C   
1305 C  C   B VAL   A 49  ? 0.1230 0.1207 0.1314 0.0031  0.0007  -0.0058 49  VAL   A C   
1306 O  O   A VAL   A 49  ? 0.1339 0.1390 0.1509 -0.0129 -0.0003 0.0009  49  VAL   A O   
1307 O  O   B VAL   A 49  ? 0.1208 0.1232 0.1218 0.0096  0.0065  0.0036  49  VAL   A O   
1308 C  CB  A VAL   A 49  ? 0.1489 0.1326 0.1743 -0.0020 0.0034  0.0061  49  VAL   A CB  
1309 C  CB  B VAL   A 49  ? 0.1232 0.1225 0.1659 -0.0032 -0.0065 0.0133  49  VAL   A CB  
1310 C  CG1 A VAL   A 49  ? 0.1519 0.1327 0.1884 0.0055  0.0119  0.0049  49  VAL   A CG1 
1311 C  CG1 B VAL   A 49  ? 0.1134 0.1234 0.1704 0.0136  -0.0058 0.0206  49  VAL   A CG1 
1312 C  CG2 A VAL   A 49  ? 0.1581 0.1383 0.2093 -0.0102 -0.0016 -0.0025 49  VAL   A CG2 
1313 C  CG2 B VAL   A 49  ? 0.1303 0.1263 0.1907 -0.0069 -0.0107 0.0163  49  VAL   A CG2 
1332 N  N   A ALA   A 50  ? 0.1268 0.1225 0.1296 0.0012  -0.0056 0.0237  50  ALA   A N   
1333 N  N   B ALA   A 50  ? 0.1197 0.1182 0.1257 -0.0014 -0.0062 -0.0047 50  ALA   A N   
1334 C  CA  A ALA   A 50  ? 0.1264 0.1217 0.1309 0.0004  -0.0055 0.0222  50  ALA   A CA  
1335 C  CA  B ALA   A 50  ? 0.1195 0.1189 0.1312 -0.0081 0.0004  -0.0059 50  ALA   A CA  
1336 C  C   A ALA   A 50  ? 0.1207 0.1259 0.1343 -0.0013 -0.0034 0.0079  50  ALA   A C   
1337 C  C   B ALA   A 50  ? 0.1167 0.1241 0.1290 -0.0089 0.0030  -0.0025 50  ALA   A C   
1338 O  O   A ALA   A 50  ? 0.1209 0.1290 0.1509 0.0065  -0.0100 0.0069  50  ALA   A O   
1339 O  O   B ALA   A 50  ? 0.1173 0.1260 0.1395 -0.0086 0.0014  0.0001  50  ALA   A O   
1340 C  CB  A ALA   A 50  ? 0.1271 0.1252 0.1374 0.0074  0.0045  0.0192  50  ALA   A CB  
1341 C  CB  B ALA   A 50  ? 0.1182 0.1235 0.1386 -0.0067 0.0094  -0.0207 50  ALA   A CB  
1352 N  N   . GLY   A 51  ? 0.1220 0.1187 0.1504 0.0048  -0.0080 0.0038  51  GLY   A N   
1353 C  CA  . GLY   A 51  ? 0.1363 0.1147 0.1565 0.0098  -0.0191 -0.0043 51  GLY   A CA  
1354 C  C   . GLY   A 51  ? 0.1217 0.1281 0.1589 0.0045  -0.0107 -0.0115 51  GLY   A C   
1355 O  O   . GLY   A 51  ? 0.1330 0.1343 0.1631 0.0029  -0.0119 -0.0108 51  GLY   A O   
1360 N  N   . ALA   A 52  ? 0.1223 0.1376 0.1504 0.0082  0.0025  -0.0207 52  ALA   A N   
1361 C  CA  . ALA   A 52  ? 0.1256 0.1491 0.1643 0.0028  0.0007  -0.0185 52  ALA   A CA  
1362 C  C   . ALA   A 52  ? 0.1242 0.1513 0.1437 -0.0069 0.0054  -0.0132 52  ALA   A C   
1363 O  O   . ALA   A 52  ? 0.1334 0.1582 0.1545 -0.0028 0.0047  -0.0113 52  ALA   A O   
1364 C  CB  . ALA   A 52  ? 0.1398 0.1797 0.1756 -0.0040 -0.0029 -0.0178 52  ALA   A CB  
1370 N  N   A LEU   A 53  ? 0.1251 0.1481 0.1436 -0.0124 0.0055  -0.0085 53  LEU   A N   
1371 N  N   B LEU   A 53  ? 0.1200 0.1437 0.1391 -0.0090 0.0010  -0.0114 53  LEU   A N   
1372 C  CA  A LEU   A 53  ? 0.1344 0.1532 0.1370 -0.0114 0.0104  0.0010  53  LEU   A CA  
1373 C  CA  B LEU   A 53  ? 0.1268 0.1442 0.1237 -0.0058 -0.0001 -0.0015 53  LEU   A CA  
1374 C  C   A LEU   A 53  ? 0.1297 0.1480 0.1328 -0.0013 0.0012  -0.0036 53  LEU   A C   
1375 C  C   B LEU   A 53  ? 0.1227 0.1408 0.1170 0.0036  -0.0053 -0.0005 53  LEU   A C   
1376 O  O   A LEU   A 53  ? 0.1368 0.1504 0.1459 -0.0083 0.0051  -0.0028 53  LEU   A O   
1377 O  O   B LEU   A 53  ? 0.1356 0.1384 0.1193 -0.0040 -0.0047 -0.0016 53  LEU   A O   
1378 C  CB  A LEU   A 53  ? 0.1435 0.1562 0.1462 -0.0131 0.0137  0.0095  53  LEU   A CB  
1379 C  CB  B LEU   A 53  ? 0.1317 0.1412 0.1222 -0.0065 -0.0102 0.0033  53  LEU   A CB  
1380 C  CG  A LEU   A 53  ? 0.1452 0.1592 0.1606 -0.0124 0.0124  0.0106  53  LEU   A CG  
1381 C  CG  B LEU   A 53  ? 0.1365 0.1440 0.1276 -0.0041 -0.0158 -0.0020 53  LEU   A CG  
1382 C  CD1 A LEU   A 53  ? 0.1434 0.1604 0.1605 -0.0060 0.0087  0.0148  53  LEU   A CD1 
1383 C  CD1 B LEU   A 53  ? 0.1478 0.1473 0.1365 -0.0082 -0.0061 -0.0101 53  LEU   A CD1 
1384 C  CD2 A LEU   A 53  ? 0.1511 0.1679 0.1686 -0.0216 0.0112  0.0140  53  LEU   A CD2 
1385 C  CD2 B LEU   A 53  ? 0.1321 0.1495 0.1316 -0.0053 -0.0108 0.0005  53  LEU   A CD2 
1408 N  N   A ASN   A 54  ? 0.1280 0.1389 0.1366 -0.0036 -0.0031 0.0028  54  ASN   A N   
1409 N  N   B ASN   A 54  ? 0.1228 0.1387 0.1245 0.0045  0.0009  0.0071  54  ASN   A N   
1410 C  CA  A ASN   A 54  ? 0.1234 0.1319 0.1438 -0.0062 -0.0081 -0.0010 54  ASN   A CA  
1411 C  CA  B ASN   A 54  ? 0.1164 0.1363 0.1251 0.0018  -0.0012 0.0039  54  ASN   A CA  
1412 C  C   A ASN   A 54  ? 0.1339 0.1392 0.1399 -0.0067 -0.0009 -0.0039 54  ASN   A C   
1413 C  C   B ASN   A 54  ? 0.1305 0.1405 0.1276 -0.0018 0.0021  -0.0022 54  ASN   A C   
1414 O  O   A ASN   A 54  ? 0.1341 0.1508 0.1493 -0.0072 -0.0062 -0.0118 54  ASN   A O   
1415 O  O   B ASN   A 54  ? 0.1308 0.1486 0.1375 -0.0007 -0.0064 -0.0106 54  ASN   A O   
1416 C  CB  A ASN   A 54  ? 0.1210 0.1252 0.1583 -0.0128 -0.0134 -0.0044 54  ASN   A CB  
1417 C  CB  B ASN   A 54  ? 0.1190 0.1350 0.1272 0.0049  0.0022  0.0017  54  ASN   A CB  
1418 C  CG  A ASN   A 54  ? 0.1232 0.1231 0.1682 -0.0100 -0.0092 -0.0016 54  ASN   A CG  
1419 C  CG  B ASN   A 54  ? 0.1206 0.1345 0.1241 0.0144  0.0038  0.0016  54  ASN   A CG  
1420 O  OD1 A ASN   A 54  ? 0.1253 0.1188 0.1758 -0.0123 -0.0117 0.0045  54  ASN   A OD1 
1421 O  OD1 B ASN   A 54  ? 0.1221 0.1377 0.1180 0.0165  -0.0018 -0.0033 54  ASN   A OD1 
1422 N  ND2 A ASN   A 54  ? 0.1245 0.1304 0.1782 -0.0083 -0.0179 -0.0042 54  ASN   A ND2 
1423 N  ND2 B ASN   A 54  ? 0.1289 0.1362 0.1312 0.0091  -0.0012 0.0052  54  ASN   A ND2 
1436 N  N   . LYS   A 55  ? 0.1316 0.1377 0.1550 0.0006  -0.0036 -0.0114 55  LYS   A N   
1437 C  CA  . LYS   A 55  ? 0.1364 0.1482 0.1591 0.0060  -0.0058 -0.0157 55  LYS   A CA  
1438 C  C   . LYS   A 55  ? 0.1340 0.1613 0.1585 -0.0036 -0.0044 -0.0159 55  LYS   A C   
1439 O  O   . LYS   A 55  ? 0.1455 0.1711 0.1632 0.0034  -0.0106 -0.0240 55  LYS   A O   
1440 C  CB  . LYS   A 55  ? 0.1444 0.1577 0.1708 0.0205  -0.0061 -0.0231 55  LYS   A CB  
1441 C  CG  . LYS   A 55  ? 0.1561 0.1879 0.1934 0.0237  -0.0260 -0.0271 55  LYS   A CG  
1442 C  CD  . LYS   A 55  ? 0.1709 0.2068 0.2067 0.0376  -0.0166 -0.0304 55  LYS   A CD  
1443 C  CE  . LYS   A 55  ? 0.1885 0.2364 0.2297 0.0475  -0.0247 -0.0283 55  LYS   A CE  
1444 N  NZ  . LYS   A 55  ? 0.1985 0.2449 0.2421 0.0516  -0.0250 -0.0269 55  LYS   A NZ  
1459 N  N   . ALA   A 56  ? 0.1362 0.1717 0.1498 -0.0054 0.0024  -0.0174 56  ALA   A N   
1460 C  CA  . ALA   A 56  ? 0.1497 0.1855 0.1491 -0.0080 0.0125  -0.0125 56  ALA   A CA  
1461 C  C   . ALA   A 56  ? 0.1547 0.1942 0.1290 -0.0080 0.0105  -0.0201 56  ALA   A C   
1462 O  O   . ALA   A 56  ? 0.1634 0.2276 0.1477 0.0047  0.0152  -0.0127 56  ALA   A O   
1463 C  CB  . ALA   A 56  ? 0.1580 0.1980 0.1625 -0.0149 0.0187  -0.0089 56  ALA   A CB  
1469 N  N   . THR   A 57  ? 0.1411 0.1739 0.1309 -0.0071 0.0074  -0.0177 57  THR   A N   
1470 C  CA  . THR   A 57  ? 0.1453 0.1688 0.1350 -0.0083 0.0004  -0.0130 57  THR   A CA  
1471 C  C   . THR   A 57  ? 0.1435 0.1728 0.1395 -0.0025 -0.0031 -0.0192 57  THR   A C   
1472 O  O   . THR   A 57  ? 0.1417 0.1792 0.1612 -0.0122 -0.0081 -0.0274 57  THR   A O   
1473 C  CB  . THR   A 57  ? 0.1442 0.1694 0.1383 -0.0058 0.0033  -0.0117 57  THR   A CB  
1474 O  OG1 . THR   A 57  ? 0.1327 0.1608 0.1347 -0.0029 0.0054  -0.0116 57  THR   A OG1 
1475 C  CG2 . THR   A 57  ? 0.1490 0.1697 0.1335 -0.0056 -0.0003 -0.0061 57  THR   A CG2 
1483 N  N   . ASN   A 58  ? 0.1450 0.1669 0.1638 -0.0056 0.0080  -0.0331 58  ASN   A N   
1484 C  CA  . ASN   A 58  ? 0.1675 0.1631 0.1886 -0.0091 0.0032  -0.0356 58  ASN   A CA  
1485 C  C   . ASN   A 58  ? 0.1486 0.1469 0.1715 -0.0000 -0.0038 -0.0205 58  ASN   A C   
1486 O  O   . ASN   A 58  ? 0.1515 0.1601 0.1875 -0.0138 -0.0036 -0.0289 58  ASN   A O   
1487 C  CB  . ASN   A 58  ? 0.2110 0.1814 0.2151 -0.0178 0.0250  -0.0499 58  ASN   A CB  
1488 C  CG  . ASN   A 58  ? 0.2532 0.2048 0.2841 -0.0127 0.0300  -0.0427 58  ASN   A CG  
1489 O  OD1 . ASN   A 58  ? 0.2801 0.2005 0.3205 0.0228  0.0628  -0.0380 58  ASN   A OD1 
1490 N  ND2 . ASN   A 58  ? 0.2641 0.2160 0.3053 -0.0124 0.0133  -0.0493 58  ASN   A ND2 
1497 N  N   . ASN   A 59  ? 0.1345 0.1475 0.1592 -0.0052 -0.0132 -0.0150 59  ASN   A N   
1498 C  CA  . ASN   A 59  ? 0.1375 0.1336 0.1483 -0.0021 -0.0081 -0.0085 59  ASN   A CA  
1499 C  C   . ASN   A 59  ? 0.1366 0.1350 0.1403 -0.0033 -0.0145 -0.0071 59  ASN   A C   
1500 O  O   . ASN   A 59  ? 0.1333 0.1409 0.1522 -0.0037 -0.0008 -0.0003 59  ASN   A O   
1501 C  CB  . ASN   A 59  ? 0.1368 0.1303 0.1660 0.0032  -0.0148 -0.0167 59  ASN   A CB  
1502 C  CG  . ASN   A 59  ? 0.1413 0.1326 0.1696 -0.0023 -0.0275 -0.0032 59  ASN   A CG  
1503 O  OD1 . ASN   A 59  ? 0.1511 0.1392 0.1640 -0.0086 -0.0292 0.0034  59  ASN   A OD1 
1504 N  ND2 . ASN   A 59  ? 0.1514 0.1394 0.1846 -0.0137 -0.0267 0.0035  59  ASN   A ND2 
1511 N  N   . ALA   A 60  ? 0.1317 0.1396 0.1427 -0.0019 -0.0095 -0.0052 60  ALA   A N   
1512 C  CA  . ALA   A 60  ? 0.1301 0.1400 0.1511 0.0006  -0.0044 -0.0009 60  ALA   A CA  
1513 C  C   . ALA   A 60  ? 0.1318 0.1319 0.1580 0.0011  -0.0001 -0.0014 60  ALA   A C   
1514 O  O   . ALA   A 60  ? 0.1244 0.1386 0.1781 -0.0029 -0.0076 -0.0070 60  ALA   A O   
1515 C  CB  . ALA   A 60  ? 0.1372 0.1540 0.1617 -0.0053 -0.0073 -0.0181 60  ALA   A CB  
1521 N  N   . MET   A 61  ? 0.1283 0.1305 0.1472 -0.0071 -0.0061 -0.0073 61  MET   A N   
1522 C  CA  . MET   A 61  ? 0.1276 0.1261 0.1467 -0.0100 -0.0018 0.0036  61  MET   A CA  
1523 C  C   . MET   A 61  ? 0.1179 0.1204 0.1521 -0.0080 -0.0070 -0.0030 61  MET   A C   
1524 O  O   . MET   A 61  ? 0.1286 0.1236 0.1487 -0.0022 0.0035  0.0023  61  MET   A O   
1525 C  CB  . MET   A 61  ? 0.1289 0.1280 0.1326 -0.0050 -0.0031 -0.0001 61  MET   A CB  
1526 C  CG  . MET   A 61  ? 0.1337 0.1330 0.1568 -0.0005 -0.0013 -0.0027 61  MET   A CG  
1527 S  SD  . MET   A 61  ? 0.1345 0.1386 0.1824 -0.0096 0.0009  -0.0174 61  MET   A SD  
1528 C  CE  . MET   A 61  ? 0.1589 0.1545 0.2083 -0.0177 0.0151  -0.0149 61  MET   A CE  
1538 N  N   . GLN   A 62  ? 0.1227 0.1230 0.1511 -0.0085 -0.0022 0.0010  62  GLN   A N   
1539 C  CA  . GLN   A 62  ? 0.1300 0.1190 0.1592 -0.0048 0.0027  0.0030  62  GLN   A CA  
1540 C  C   . GLN   A 62  ? 0.1269 0.1144 0.1629 -0.0013 0.0045  0.0063  62  GLN   A C   
1541 O  O   . GLN   A 62  ? 0.1300 0.1259 0.1630 -0.0016 0.0046  -0.0007 62  GLN   A O   
1542 C  CB  . GLN   A 62  ? 0.1259 0.1207 0.1662 -0.0008 0.0042  0.0007  62  GLN   A CB  
1543 C  CG  . GLN   A 62  ? 0.1296 0.1181 0.1598 -0.0030 -0.0077 0.0136  62  GLN   A CG  
1544 C  CD  . GLN   A 62  ? 0.1360 0.1204 0.1560 -0.0023 -0.0003 0.0130  62  GLN   A CD  
1545 O  OE1 . GLN   A 62  ? 0.1403 0.1367 0.1626 -0.0044 -0.0021 0.0029  62  GLN   A OE1 
1546 N  NE2 . GLN   A 62  ? 0.1455 0.1264 0.1673 0.0053  0.0024  -0.0061 62  GLN   A NE2 
1555 N  N   . VAL   A 63  ? 0.1224 0.1279 0.1678 -0.0054 0.0033  -0.0191 63  VAL   A N   
1556 C  CA  . VAL   A 63  ? 0.1314 0.1348 0.1950 -0.0166 -0.0021 -0.0143 63  VAL   A CA  
1557 C  C   . VAL   A 63  ? 0.1165 0.1335 0.1850 -0.0164 -0.0108 -0.0165 63  VAL   A C   
1558 O  O   . VAL   A 63  ? 0.1191 0.1363 0.1961 -0.0178 -0.0037 -0.0114 63  VAL   A O   
1559 C  CB  . VAL   A 63  ? 0.1453 0.1572 0.2171 -0.0143 -0.0076 -0.0434 63  VAL   A CB  
1560 C  CG1 . VAL   A 63  ? 0.1568 0.1698 0.2577 -0.0235 -0.0098 -0.0592 63  VAL   A CG1 
1561 C  CG2 . VAL   A 63  ? 0.1496 0.1444 0.2345 -0.0151 0.0138  -0.0391 63  VAL   A CG2 
1571 N  N   . GLU   A 64  ? 0.1198 0.1423 0.1672 -0.0047 -0.0043 -0.0047 64  GLU   A N   
1572 C  CA  . GLU   A 64  ? 0.1166 0.1382 0.1704 -0.0064 -0.0036 -0.0028 64  GLU   A CA  
1573 C  C   . GLU   A 64  ? 0.1157 0.1289 0.1681 -0.0072 0.0004  0.0012  64  GLU   A C   
1574 O  O   . GLU   A 64  ? 0.1277 0.1332 0.1701 -0.0008 -0.0039 0.0007  64  GLU   A O   
1575 C  CB  . GLU   A 64  ? 0.1298 0.1527 0.1725 -0.0086 -0.0030 -0.0042 64  GLU   A CB  
1576 C  CG  . GLU   A 64  ? 0.1397 0.1541 0.1743 -0.0120 0.0039  -0.0058 64  GLU   A CG  
1577 C  CD  . GLU   A 64  ? 0.1471 0.1598 0.1814 -0.0145 0.0097  -0.0018 64  GLU   A CD  
1578 O  OE1 . GLU   A 64  ? 0.1492 0.1688 0.2083 -0.0214 0.0158  -0.0032 64  GLU   A OE1 
1579 O  OE2 . GLU   A 64  ? 0.1667 0.1620 0.1719 -0.0192 -0.0064 0.0051  64  GLU   A OE2 
1586 N  N   . SER   A 65  ? 0.1109 0.1339 0.1633 0.0004  0.0050  -0.0023 65  SER   A N   
1587 C  CA  . SER   A 65  ? 0.1206 0.1236 0.1561 -0.0008 -0.0019 -0.0075 65  SER   A CA  
1588 C  C   . SER   A 65  ? 0.1223 0.1315 0.1596 -0.0016 0.0039  -0.0020 65  SER   A C   
1589 O  O   . SER   A 65  ? 0.1281 0.1349 0.1824 0.0006  0.0068  -0.0040 65  SER   A O   
1590 C  CB  . SER   A 65  ? 0.1228 0.1218 0.1551 -0.0071 0.0052  0.0003  65  SER   A CB  
1591 O  OG  . SER   A 65  ? 0.1207 0.1393 0.1696 -0.0073 -0.0063 0.0171  65  SER   A OG  
1597 N  N   . ASP   A 66  ? 0.1262 0.1248 0.1710 -0.0067 0.0140  0.0033  66  ASP   A N   
1598 C  CA  . ASP   A 66  ? 0.1351 0.1358 0.1820 -0.0010 0.0078  0.0140  66  ASP   A CA  
1599 C  C   . ASP   A 66  ? 0.1328 0.1348 0.1866 -0.0080 0.0115  0.0200  66  ASP   A C   
1600 O  O   . ASP   A 66  ? 0.1383 0.1461 0.2017 -0.0069 0.0216  0.0252  66  ASP   A O   
1601 C  CB  . ASP   A 66  ? 0.1392 0.1462 0.2143 0.0057  0.0105  0.0280  66  ASP   A CB  
1602 C  CG  . ASP   A 66  ? 0.1625 0.1558 0.2450 0.0043  -0.0017 0.0372  66  ASP   A CG  
1603 O  OD1 . ASP   A 66  ? 0.1606 0.1879 0.2062 -0.0045 -0.0041 0.0490  66  ASP   A OD1 
1604 O  OD2 . ASP   A 66  ? 0.1844 0.1660 0.3249 0.0251  -0.0249 0.0143  66  ASP   A OD2 
1609 N  N   . ASP   A 67  ? 0.1274 0.1351 0.1969 -0.0031 0.0082  0.0160  67  ASP   A N   
1610 C  CA  . ASP   A 67  ? 0.1282 0.1510 0.2099 -0.0019 0.0073  0.0238  67  ASP   A CA  
1611 C  C   . ASP   A 67  ? 0.1269 0.1535 0.2010 0.0020  0.0142  0.0235  67  ASP   A C   
1612 O  O   . ASP   A 67  ? 0.1274 0.1605 0.2300 0.0048  0.0306  0.0339  67  ASP   A O   
1613 C  CB  . ASP   A 67  ? 0.1365 0.1661 0.2421 -0.0049 -0.0133 0.0267  67  ASP   A CB  
1614 C  CG  . ASP   A 67  ? 0.1349 0.1708 0.2726 -0.0098 -0.0322 0.0313  67  ASP   A CG  
1615 O  OD1 . ASP   A 67  ? 0.1407 0.1932 0.3559 -0.0105 -0.0417 0.0496  67  ASP   A OD1 
1616 O  OD2 . ASP   A 67  ? 0.1383 0.1757 0.2541 0.0001  -0.0199 0.0243  67  ASP   A OD2 
1621 N  N   A TYR   A 68  ? 0.1279 0.1390 0.1964 0.0014  0.0200  0.0229  68  TYR   A N   
1622 N  N   B TYR   A 68  ? 0.1297 0.1437 0.1936 0.0061  0.0116  0.0294  68  TYR   A N   
1623 C  CA  A TYR   A 68  ? 0.1383 0.1344 0.1921 -0.0033 0.0317  0.0210  68  TYR   A CA  
1624 C  CA  B TYR   A 68  ? 0.1419 0.1422 0.1854 0.0056  0.0139  0.0311  68  TYR   A CA  
1625 C  C   A TYR   A 68  ? 0.1326 0.1362 0.1896 -0.0006 0.0264  0.0195  68  TYR   A C   
1626 C  C   B TYR   A 68  ? 0.1322 0.1403 0.1855 0.0058  0.0184  0.0229  68  TYR   A C   
1627 O  O   A TYR   A 68  ? 0.1374 0.1368 0.2018 0.0012  0.0314  0.0192  68  TYR   A O   
1628 O  O   B TYR   A 68  ? 0.1347 0.1430 0.1960 0.0136  0.0254  0.0223  68  TYR   A O   
1629 C  CB  A TYR   A 68  ? 0.1443 0.1299 0.2028 0.0033  0.0498  0.0171  68  TYR   A CB  
1630 C  CB  B TYR   A 68  ? 0.1513 0.1425 0.1888 0.0148  0.0171  0.0341  68  TYR   A CB  
1631 C  CG  A TYR   A 68  ? 0.1445 0.1372 0.2238 -0.0010 0.0655  0.0172  68  TYR   A CG  
1632 C  CG  B TYR   A 68  ? 0.1545 0.1502 0.1919 0.0150  0.0145  0.0286  68  TYR   A CG  
1633 C  CD1 A TYR   A 68  ? 0.1478 0.1446 0.2527 -0.0250 0.0573  0.0010  68  TYR   A CD1 
1634 C  CD1 B TYR   A 68  ? 0.1636 0.1505 0.1883 0.0075  0.0062  0.0256  68  TYR   A CD1 
1635 C  CD2 A TYR   A 68  ? 0.1621 0.1449 0.2449 0.0044  0.0675  0.0233  68  TYR   A CD2 
1636 C  CD2 B TYR   A 68  ? 0.1678 0.1536 0.2015 0.0155  0.0064  0.0241  68  TYR   A CD2 
1637 C  CE1 A TYR   A 68  ? 0.1503 0.1588 0.2878 -0.0274 0.0527  -0.0166 68  TYR   A CE1 
1638 C  CE1 B TYR   A 68  ? 0.1684 0.1433 0.1696 0.0099  0.0108  0.0494  68  TYR   A CE1 
1639 C  CE2 A TYR   A 68  ? 0.1625 0.1526 0.2675 0.0035  0.0752  0.0064  68  TYR   A CE2 
1640 C  CE2 B TYR   A 68  ? 0.1665 0.1494 0.1753 0.0114  0.0094  0.0189  68  TYR   A CE2 
1641 C  CZ  A TYR   A 68  ? 0.1532 0.1575 0.3074 -0.0175 0.0567  -0.0315 68  TYR   A CZ  
1642 C  CZ  B TYR   A 68  ? 0.1702 0.1387 0.1528 0.0144  0.0188  0.0364  68  TYR   A CZ  
1643 O  OH  A TYR   A 68  ? 0.1666 0.1742 0.3575 -0.0177 0.0357  -0.0673 68  TYR   A OH  
1644 O  OH  B TYR   A 68  ? 0.1932 0.1339 0.1540 0.0129  0.0019  0.0291  68  TYR   A OH  
1663 N  N   . ILE   A 69  ? 0.1278 0.1306 0.1796 0.0002  0.0216  0.0269  69  ILE   A N   
1664 C  CA  . ILE   A 69  ? 0.1405 0.1344 0.1747 0.0009  0.0127  0.0089  69  ILE   A CA  
1665 C  C   . ILE   A 69  ? 0.1405 0.1400 0.1717 0.0028  0.0186  0.0206  69  ILE   A C   
1666 O  O   . ILE   A 69  ? 0.1411 0.1451 0.1728 0.0012  0.0221  0.0206  69  ILE   A O   
1667 C  CB  . ILE   A 69  ? 0.1460 0.1570 0.1795 0.0027  0.0099  -0.0073 69  ILE   A CB  
1668 C  CG1 . ILE   A 69  ? 0.1417 0.1651 0.1874 0.0086  0.0176  -0.0182 69  ILE   A CG1 
1669 C  CG2 . ILE   A 69  ? 0.1596 0.1799 0.1956 0.0108  0.0005  -0.0115 69  ILE   A CG2 
1670 C  CD1 . ILE   A 69  ? 0.1483 0.1724 0.2061 -0.0028 0.0121  -0.0219 69  ILE   A CD1 
1683 N  N   . ALA   A 70  ? 0.1434 0.1365 0.1774 -0.0062 0.0210  0.0178  70  ALA   A N   
1684 C  CA  . ALA   A 70  ? 0.1446 0.1458 0.2006 -0.0143 0.0258  0.0264  70  ALA   A CA  
1685 C  C   . ALA   A 70  ? 0.1424 0.1645 0.1963 -0.0070 0.0278  0.0230  70  ALA   A C   
1686 O  O   . ALA   A 70  ? 0.1609 0.1987 0.2156 0.0074  0.0438  0.0384  70  ALA   A O   
1687 C  CB  . ALA   A 70  ? 0.1496 0.1450 0.2280 -0.0200 0.0145  0.0199  70  ALA   A CB  
1693 N  N   . THR   A 71  ? 0.1343 0.1559 0.1874 -0.0029 0.0172  0.0226  71  THR   A N   
1694 C  CA  . THR   A 71  ? 0.1445 0.1753 0.2200 0.0089  0.0201  0.0254  71  THR   A CA  
1695 C  C   . THR   A 71  ? 0.1360 0.1697 0.2417 0.0150  0.0307  0.0190  71  THR   A C   
1696 O  O   . THR   A 71  ? 0.1439 0.1956 0.2862 0.0089  0.0421  -0.0074 71  THR   A O   
1697 C  CB  . THR   A 71  ? 0.1690 0.2046 0.2349 0.0165  -0.0096 0.0361  71  THR   A CB  
1698 O  OG1 . THR   A 71  ? 0.1965 0.2297 0.2403 0.0086  -0.0327 0.0216  71  THR   A OG1 
1699 C  CG2 . THR   A 71  ? 0.1828 0.2242 0.2551 0.0226  -0.0099 0.0480  71  THR   A CG2 
1707 N  N   . ASN   A 72  ? 0.1384 0.1559 0.2132 0.0142  0.0246  0.0223  72  ASN   A N   
1708 C  CA  . ASN   A 72  ? 0.1502 0.1529 0.2150 0.0153  0.0299  0.0218  72  ASN   A CA  
1709 C  C   . ASN   A 72  ? 0.1640 0.1545 0.2052 0.0130  0.0460  0.0108  72  ASN   A C   
1710 O  O   . ASN   A 72  ? 0.1798 0.1573 0.2282 0.0198  0.0438  -0.0060 72  ASN   A O   
1711 C  CB  . ASN   A 72  ? 0.1623 0.1616 0.2183 0.0143  0.0318  0.0280  72  ASN   A CB  
1712 C  CG  . ASN   A 72  ? 0.1907 0.1692 0.2270 0.0262  0.0315  0.0283  72  ASN   A CG  
1713 O  OD1 . ASN   A 72  ? 0.2124 0.2033 0.2454 0.0252  0.0417  0.0267  72  ASN   A OD1 
1714 N  ND2 . ASN   A 72  ? 0.2069 0.1702 0.2299 0.0509  0.0138  0.0189  72  ASN   A ND2 
1721 N  N   . GLY   A 73  ? 0.1674 0.1491 0.1879 0.0039  0.0465  0.0057  73  GLY   A N   
1722 C  CA  . GLY   A 73  ? 0.1734 0.1456 0.1827 -0.0082 0.0406  0.0030  73  GLY   A CA  
1723 C  C   . GLY   A 73  ? 0.1658 0.1386 0.1694 0.0017  0.0553  0.0235  73  GLY   A C   
1724 O  O   . GLY   A 73  ? 0.1644 0.1482 0.1877 0.0092  0.0381  0.0273  73  GLY   A O   
1728 N  N   . PRO   A 74  ? 0.1794 0.1402 0.1763 -0.0101 0.0466  0.0142  74  PRO   A N   
1729 C  CA  . PRO   A 74  ? 0.1698 0.1360 0.1876 -0.0052 0.0403  0.0144  74  PRO   A CA  
1730 C  C   . PRO   A 74  ? 0.1618 0.1300 0.1819 -0.0007 0.0277  0.0048  74  PRO   A C   
1731 O  O   . PRO   A 74  ? 0.1697 0.1335 0.2062 0.0070  0.0345  0.0008  74  PRO   A O   
1732 C  CB  . PRO   A 74  ? 0.1799 0.1664 0.2099 -0.0030 0.0396  0.0242  74  PRO   A CB  
1733 C  CG  . PRO   A 74  ? 0.2072 0.2000 0.2495 -0.0159 0.0317  0.0089  74  PRO   A CG  
1734 C  CD  . PRO   A 74  ? 0.1923 0.1763 0.1946 -0.0214 0.0357  0.0044  74  PRO   A CD  
1742 N  N   . LEU   A 75  ? 0.1588 0.1256 0.1632 -0.0015 0.0274  0.0062  75  LEU   A N   
1743 C  CA  . LEU   A 75  ? 0.1624 0.1220 0.1555 -0.0012 0.0125  0.0133  75  LEU   A CA  
1744 C  C   . LEU   A 75  ? 0.1741 0.1347 0.1537 0.0018  0.0157  0.0179  75  LEU   A C   
1745 O  O   . LEU   A 75  ? 0.2135 0.1487 0.1534 0.0057  0.0055  0.0035  75  LEU   A O   
1746 C  CB  . LEU   A 75  ? 0.1673 0.1292 0.1450 -0.0080 0.0094  0.0201  75  LEU   A CB  
1747 C  CG  . LEU   A 75  ? 0.1879 0.1638 0.1551 -0.0338 0.0028  0.0141  75  LEU   A CG  
1748 C  CD1 . LEU   A 75  ? 0.1980 0.2097 0.1629 -0.0380 0.0071  0.0014  75  LEU   A CD1 
1749 C  CD2 . LEU   A 75  ? 0.2175 0.2072 0.2104 -0.0097 0.0086  0.0173  75  LEU   A CD2 
1761 N  N   . LYS   A 76  ? 0.1740 0.1371 0.1699 -0.0093 0.0196  0.0052  76  LYS   A N   
1762 C  CA  . LYS   A 76  ? 0.1678 0.1543 0.1674 -0.0118 0.0120  -0.0094 76  LYS   A CA  
1763 C  C   . LYS   A 76  ? 0.1693 0.1385 0.1424 -0.0070 0.0127  0.0040  76  LYS   A C   
1764 O  O   . LYS   A 76  ? 0.1729 0.1298 0.1436 -0.0049 0.0167  0.0085  76  LYS   A O   
1765 C  CB  . LYS   A 76  ? 0.1663 0.1802 0.2070 -0.0002 0.0168  -0.0330 76  LYS   A CB  
1766 C  CG  . LYS   A 76  ? 0.1737 0.1715 0.2636 0.0005  0.0151  -0.0288 76  LYS   A CG  
1767 C  CD  . LYS   A 76  ? 0.1827 0.1665 0.3091 0.0093  0.0062  -0.0320 76  LYS   A CD  
1768 C  CE  . LYS   A 76  ? 0.1980 0.1897 0.3671 0.0007  0.0107  -0.0422 76  LYS   A CE  
1769 N  NZ  . LYS   A 76  ? 0.1937 0.1856 0.4063 -0.0141 0.0057  -0.0502 76  LYS   A NZ  
1783 N  N   . VAL   A 77  ? 0.1788 0.1433 0.1408 -0.0046 0.0277  0.0113  77  VAL   A N   
1784 C  CA  . VAL   A 77  ? 0.1714 0.1436 0.1450 0.0046  0.0137  0.0118  77  VAL   A CA  
1785 C  C   . VAL   A 77  ? 0.1649 0.1410 0.1462 0.0074  0.0155  0.0051  77  VAL   A C   
1786 O  O   . VAL   A 77  ? 0.1722 0.1445 0.1442 0.0130  0.0255  0.0003  77  VAL   A O   
1787 C  CB  . VAL   A 77  ? 0.1925 0.1575 0.1594 0.0032  0.0102  0.0156  77  VAL   A CB  
1788 C  CG1 . VAL   A 77  ? 0.1878 0.1667 0.1831 0.0104  0.0036  0.0094  77  VAL   A CG1 
1789 C  CG2 . VAL   A 77  ? 0.2164 0.1664 0.1773 -0.0022 -0.0012 0.0262  77  VAL   A CG2 
1799 N  N   . GLY   A 78  ? 0.1603 0.1346 0.1406 0.0050  0.0228  0.0084  78  GLY   A N   
1800 C  CA  . GLY   A 78  ? 0.1575 0.1312 0.1594 0.0061  0.0252  0.0169  78  GLY   A CA  
1801 C  C   . GLY   A 78  ? 0.1516 0.1295 0.1526 0.0046  0.0192  0.0120  78  GLY   A C   
1802 O  O   . GLY   A 78  ? 0.1500 0.1356 0.1749 0.0038  0.0219  0.0272  78  GLY   A O   
1806 N  N   . GLY   A 79  ? 0.1546 0.1314 0.1505 0.0044  0.0187  0.0169  79  GLY   A N   
1807 C  CA  . GLY   A 79  ? 0.1484 0.1294 0.1671 0.0007  0.0211  0.0089  79  GLY   A CA  
1808 C  C   . GLY   A 79  ? 0.1370 0.1215 0.1597 0.0006  0.0158  0.0066  79  GLY   A C   
1809 O  O   . GLY   A 79  ? 0.1413 0.1356 0.1616 0.0223  0.0104  0.0044  79  GLY   A O   
1813 N  N   . SER   A 80  ? 0.1280 0.1364 0.1845 -0.0012 0.0150  0.0008  80  SER   A N   
1814 C  CA  . SER   A 80  ? 0.1271 0.1333 0.1563 -0.0001 0.0036  0.0016  80  SER   A CA  
1815 C  C   . SER   A 80  ? 0.1294 0.1303 0.1653 -0.0024 0.0032  0.0121  80  SER   A C   
1816 O  O   . SER   A 80  ? 0.1265 0.1527 0.1924 0.0087  0.0110  0.0022  80  SER   A O   
1817 C  CB  . SER   A 80  ? 0.1355 0.1335 0.1893 -0.0122 0.0026  0.0087  80  SER   A CB  
1818 O  OG  . SER   A 80  ? 0.1632 0.1338 0.2324 0.0051  -0.0055 0.0262  80  SER   A OG  
1824 N  N   . CYS   A 81  ? 0.1228 0.1256 0.1645 -0.0017 -0.0010 0.0112  81  CYS   A N   
1825 C  CA  . CYS   A 81  ? 0.1211 0.1378 0.1601 -0.0054 -0.0052 0.0215  81  CYS   A CA  
1826 C  C   . CYS   A 81  ? 0.1212 0.1339 0.1569 -0.0083 -0.0040 0.0291  81  CYS   A C   
1827 O  O   . CYS   A 81  ? 0.1206 0.1636 0.1637 0.0003  0.0036  0.0295  81  CYS   A O   
1828 C  CB  . CYS   A 81  ? 0.1312 0.1458 0.1701 -0.0177 -0.0049 0.0246  81  CYS   A CB  
1829 S  SG  . CYS   A 81  ? 0.1442 0.1365 0.1636 -0.0154 0.0016  0.0155  81  CYS   A SG  
1835 N  N   . VAL   A 82  ? 0.1265 0.1391 0.1633 -0.0003 -0.0126 0.0178  82  VAL   A N   
1836 C  CA  . VAL   A 82  ? 0.1389 0.1465 0.1688 -0.0050 -0.0051 0.0231  82  VAL   A CA  
1837 C  C   . VAL   A 82  ? 0.1344 0.1500 0.1671 -0.0010 -0.0163 0.0245  82  VAL   A C   
1838 O  O   . VAL   A 82  ? 0.1307 0.1600 0.1886 -0.0031 -0.0103 0.0041  82  VAL   A O   
1839 C  CB  . VAL   A 82  ? 0.1660 0.1596 0.1793 0.0023  -0.0010 0.0270  82  VAL   A CB  
1840 C  CG1 . VAL   A 82  ? 0.1889 0.1751 0.1892 0.0104  -0.0001 0.0264  82  VAL   A CG1 
1841 C  CG2 . VAL   A 82  ? 0.1746 0.1610 0.2091 0.0016  -0.0041 0.0387  82  VAL   A CG2 
1851 N  N   . LEU   A 83  ? 0.1302 0.1456 0.1579 -0.0073 -0.0131 0.0165  83  LEU   A N   
1852 C  CA  . LEU   A 83  ? 0.1337 0.1509 0.1525 -0.0121 -0.0171 0.0094  83  LEU   A CA  
1853 C  C   . LEU   A 83  ? 0.1389 0.1534 0.1483 -0.0101 -0.0203 0.0138  83  LEU   A C   
1854 O  O   . LEU   A 83  ? 0.1488 0.1567 0.1531 -0.0137 -0.0102 0.0211  83  LEU   A O   
1855 C  CB  . LEU   A 83  ? 0.1431 0.1502 0.1570 -0.0086 -0.0133 0.0141  83  LEU   A CB  
1856 C  CG  . LEU   A 83  ? 0.1538 0.1617 0.1647 -0.0106 0.0021  0.0085  83  LEU   A CG  
1857 C  CD1 . LEU   A 83  ? 0.1614 0.1607 0.1700 -0.0223 -0.0029 0.0208  83  LEU   A CD1 
1858 C  CD2 . LEU   A 83  ? 0.1573 0.1792 0.1789 -0.0125 0.0153  0.0202  83  LEU   A CD2 
1870 N  N   . SER   A 84  ? 0.1495 0.1621 0.1495 -0.0140 -0.0149 0.0240  84  SER   A N   
1871 C  CA  . SER   A 84  ? 0.1618 0.1652 0.1396 -0.0147 -0.0105 0.0230  84  SER   A CA  
1872 C  C   . SER   A 84  ? 0.1699 0.1578 0.1350 -0.0164 -0.0038 0.0217  84  SER   A C   
1873 O  O   . SER   A 84  ? 0.1624 0.1733 0.1320 -0.0109 -0.0084 0.0147  84  SER   A O   
1874 C  CB  . SER   A 84  ? 0.1673 0.1924 0.1506 -0.0175 -0.0053 0.0110  84  SER   A CB  
1875 O  OG  . SER   A 84  ? 0.1757 0.2144 0.1552 -0.0136 -0.0212 0.0002  84  SER   A OG  
1881 N  N   . GLY   A 85  ? 0.1789 0.1720 0.1389 -0.0229 0.0066  0.0107  85  GLY   A N   
1882 C  CA  . GLY   A 85  ? 0.1847 0.1822 0.1582 -0.0286 0.0127  0.0032  85  GLY   A CA  
1883 C  C   . GLY   A 85  ? 0.1836 0.1905 0.1343 -0.0208 -0.0060 0.0067  85  GLY   A C   
1884 O  O   . GLY   A 85  ? 0.1809 0.2017 0.1443 -0.0274 0.0119  -0.0039 85  GLY   A O   
1888 N  N   . HIS   A 86  ? 0.1862 0.1814 0.1375 -0.0142 -0.0065 0.0089  86  HIS   A N   
1889 C  CA  . HIS   A 86  ? 0.1985 0.1913 0.1264 -0.0179 -0.0020 0.0020  86  HIS   A CA  
1890 C  C   . HIS   A 86  ? 0.2200 0.2073 0.1251 -0.0193 -0.0145 0.0038  86  HIS   A C   
1891 O  O   . HIS   A 86  ? 0.2355 0.2277 0.1404 -0.0115 0.0032  0.0063  86  HIS   A O   
1892 C  CB  . HIS   A 86  ? 0.1930 0.1772 0.1381 -0.0126 0.0008  -0.0001 86  HIS   A CB  
1893 C  CG  . HIS   A 86  ? 0.1889 0.1758 0.1391 -0.0090 0.0059  0.0074  86  HIS   A CG  
1894 N  ND1 . HIS   A 86  ? 0.1962 0.1787 0.1776 -0.0230 0.0034  0.0110  86  HIS   A ND1 
1895 C  CD2 . HIS   A 86  ? 0.1892 0.1762 0.1280 -0.0040 0.0065  0.0129  86  HIS   A CD2 
1896 C  CE1 . HIS   A 86  ? 0.1878 0.1794 0.1647 -0.0201 0.0197  0.0181  86  HIS   A CE1 
1897 N  NE2 . HIS   A 86  ? 0.1829 0.1752 0.1489 -0.0025 0.0098  0.0271  86  HIS   A NE2 
1905 N  N   . ASN   A 87  ? 0.2302 0.2164 0.1365 -0.0120 0.0136  -0.0071 87  ASN   A N   
1906 C  CA  . ASN   A 87  ? 0.2527 0.2313 0.1498 -0.0145 0.0439  -0.0088 87  ASN   A CA  
1907 C  C   . ASN   A 87  ? 0.2523 0.2454 0.1768 -0.0210 0.0620  0.0008  87  ASN   A C   
1908 O  O   . ASN   A 87  ? 0.2764 0.2610 0.2232 -0.0344 0.0897  -0.0083 87  ASN   A O   
1909 C  CB  . ASN   A 87  ? 0.2704 0.2372 0.1718 -0.0027 0.0483  -0.0108 87  ASN   A CB  
1910 C  CG  . ASN   A 87  ? 0.2822 0.2440 0.1770 0.0054  0.0604  0.0006  87  ASN   A CG  
1911 O  OD1 . ASN   A 87  ? 0.2975 0.2407 0.1755 0.0227  0.0531  0.0048  87  ASN   A OD1 
1912 N  ND2 . ASN   A 87  ? 0.2870 0.2659 0.1937 0.0031  0.0638  -0.0003 87  ASN   A ND2 
1919 N  N   . LEU   A 88  ? 0.2218 0.2377 0.1704 -0.0235 0.0348  0.0153  88  LEU   A N   
1920 C  CA  . LEU   A 88  ? 0.2017 0.2344 0.1832 -0.0257 0.0369  0.0258  88  LEU   A CA  
1921 C  C   . LEU   A 88  ? 0.2001 0.2331 0.1771 -0.0250 0.0296  0.0379  88  LEU   A C   
1922 O  O   . LEU   A 88  ? 0.2055 0.2415 0.2123 -0.0234 0.0330  0.0578  88  LEU   A O   
1923 C  CB  . LEU   A 88  ? 0.2009 0.2408 0.2002 -0.0340 0.0091  0.0320  88  LEU   A CB  
1924 C  CG  . LEU   A 88  ? 0.2133 0.2503 0.2197 -0.0304 -0.0090 0.0317  88  LEU   A CG  
1925 C  CD1 . LEU   A 88  ? 0.2266 0.2556 0.2143 -0.0312 -0.0141 0.0143  88  LEU   A CD1 
1926 C  CD2 . LEU   A 88  ? 0.2281 0.2647 0.2606 -0.0223 -0.0088 0.0258  88  LEU   A CD2 
1938 N  N   . ALA   A 89  ? 0.2022 0.2193 0.1583 -0.0267 0.0220  0.0191  89  ALA   A N   
1939 C  CA  . ALA   A 89  ? 0.2084 0.2167 0.1459 -0.0226 0.0052  0.0204  89  ALA   A CA  
1940 C  C   . ALA   A 89  ? 0.2119 0.2182 0.1460 -0.0199 -0.0084 0.0190  89  ALA   A C   
1941 O  O   . ALA   A 89  ? 0.2151 0.2126 0.1844 -0.0293 -0.0193 -0.0065 89  ALA   A O   
1942 C  CB  . ALA   A 89  ? 0.2011 0.2156 0.1382 -0.0197 -0.0020 0.0253  89  ALA   A CB  
1948 N  N   . LYS   A 90  ? 0.2175 0.2333 0.1445 -0.0288 -0.0225 0.0297  90  LYS   A N   
1949 C  CA  . LYS   A 90  ? 0.2280 0.2491 0.1508 -0.0220 -0.0378 0.0334  90  LYS   A CA  
1950 C  C   . LYS   A 90  ? 0.2000 0.2285 0.1554 -0.0217 -0.0338 0.0204  90  LYS   A C   
1951 O  O   . LYS   A 90  ? 0.1984 0.2418 0.1812 -0.0281 -0.0387 0.0109  90  LYS   A O   
1952 C  CB  . LYS   A 90  ? 0.2578 0.2859 0.1768 -0.0145 -0.0497 0.0573  90  LYS   A CB  
1953 C  CG  . LYS   A 90  ? 0.3002 0.3208 0.2775 -0.0127 -0.0492 0.0633  90  LYS   A CG  
1954 C  CD  . LYS   A 90  ? 0.3470 0.3602 0.3885 -0.0128 -0.0333 0.0668  90  LYS   A CD  
1955 C  CE  . LYS   A 90  ? 0.3775 0.3918 0.4726 -0.0140 -0.0207 0.0600  90  LYS   A CE  
1956 N  NZ  . LYS   A 90  ? 0.3949 0.4019 0.5261 -0.0147 -0.0139 0.0520  90  LYS   A NZ  
1970 N  N   . HIS   A 91  ? 0.1890 0.1964 0.1304 -0.0191 -0.0389 0.0258  91  HIS   A N   
1971 C  CA  . HIS   A 91  ? 0.1764 0.1818 0.1395 -0.0175 -0.0278 0.0265  91  HIS   A CA  
1972 C  C   . HIS   A 91  ? 0.1576 0.1698 0.1257 -0.0171 -0.0197 0.0233  91  HIS   A C   
1973 O  O   . HIS   A 91  ? 0.1539 0.1814 0.1382 -0.0176 -0.0043 0.0267  91  HIS   A O   
1974 C  CB  . HIS   A 91  ? 0.1908 0.2076 0.1822 0.0069  -0.0452 0.0267  91  HIS   A CB  
1975 C  CG  . HIS   A 91  ? 0.2303 0.2587 0.2496 0.0153  -0.0657 0.0162  91  HIS   A CG  
1976 N  ND1 . HIS   A 91  ? 0.2373 0.2850 0.2892 0.0210  -0.0743 -0.0058 91  HIS   A ND1 
1977 C  CD2 . HIS   A 91  ? 0.2549 0.2803 0.2665 0.0200  -0.0747 0.0219  91  HIS   A CD2 
1978 C  CE1 . HIS   A 91  ? 0.2515 0.2929 0.3000 0.0241  -0.0714 0.0065  91  HIS   A CE1 
1979 N  NE2 . HIS   A 91  ? 0.2645 0.2937 0.2936 0.0275  -0.0764 0.0140  91  HIS   A NE2 
1987 N  N   . CYS   A 92  ? 0.1497 0.1596 0.1301 -0.0194 -0.0125 0.0172  92  CYS   A N   
1988 C  CA  . CYS   A 92  ? 0.1413 0.1550 0.1395 -0.0151 -0.0050 0.0161  92  CYS   A CA  
1989 C  C   . CYS   A 92  ? 0.1332 0.1523 0.1326 -0.0153 0.0005  0.0248  92  CYS   A C   
1990 O  O   . CYS   A 92  ? 0.1348 0.1545 0.1501 -0.0210 -0.0026 0.0177  92  CYS   A O   
1991 C  CB  . CYS   A 92  ? 0.1451 0.1526 0.1426 -0.0084 -0.0050 0.0132  92  CYS   A CB  
1992 S  SG  . CYS   A 92  ? 0.1398 0.1410 0.1449 -0.0128 -0.0045 0.0128  92  CYS   A SG  
1998 N  N   . LEU   A 93  ? 0.1306 0.1365 0.1447 -0.0138 0.0058  0.0177  93  LEU   A N   
1999 C  CA  . LEU   A 93  ? 0.1204 0.1370 0.1420 -0.0062 0.0038  0.0148  93  LEU   A CA  
2000 C  C   . LEU   A 93  ? 0.1222 0.1206 0.1302 -0.0061 0.0052  0.0105  93  LEU   A C   
2001 O  O   . LEU   A 93  ? 0.1219 0.1318 0.1338 -0.0049 -0.0015 0.0143  93  LEU   A O   
2002 C  CB  . LEU   A 93  ? 0.1311 0.1315 0.1541 -0.0029 -0.0027 0.0279  93  LEU   A CB  
2003 C  CG  . LEU   A 93  ? 0.1363 0.1349 0.1487 -0.0031 -0.0001 0.0253  93  LEU   A CG  
2004 C  CD1 . LEU   A 93  ? 0.1451 0.1346 0.1742 -0.0010 0.0086  0.0195  93  LEU   A CD1 
2005 C  CD2 . LEU   A 93  ? 0.1519 0.1341 0.1736 -0.0101 -0.0004 0.0194  93  LEU   A CD2 
2017 N  N   . HIS   A 94  ? 0.1157 0.1187 0.1410 -0.0008 0.0043  0.0145  94  HIS   A N   
2018 C  CA  . HIS   A 94  ? 0.1169 0.1229 0.1381 -0.0059 -0.0039 0.0196  94  HIS   A CA  
2019 C  C   . HIS   A 94  ? 0.1165 0.1178 0.1425 -0.0077 0.0032  0.0099  94  HIS   A C   
2020 O  O   . HIS   A 94  ? 0.1162 0.1361 0.1768 0.0011  0.0031  -0.0093 94  HIS   A O   
2021 C  CB  . HIS   A 94  ? 0.1177 0.1239 0.1433 -0.0036 -0.0060 0.0179  94  HIS   A CB  
2022 C  CG  . HIS   A 94  ? 0.1222 0.1243 0.1366 -0.0072 -0.0082 0.0155  94  HIS   A CG  
2023 N  ND1 . HIS   A 94  ? 0.1204 0.1210 0.1417 -0.0032 0.0040  0.0141  94  HIS   A ND1 
2024 C  CD2 . HIS   A 94  ? 0.1308 0.1320 0.1444 -0.0062 -0.0050 0.0084  94  HIS   A CD2 
2025 C  CE1 . HIS   A 94  ? 0.1309 0.1290 0.1358 -0.0054 -0.0080 0.0062  94  HIS   A CE1 
2026 N  NE2 . HIS   A 94  ? 0.1326 0.1266 0.1455 -0.0092 -0.0073 0.0071  94  HIS   A NE2 
2034 N  N   . VAL   A 95  ? 0.1156 0.1146 0.1284 -0.0032 0.0096  0.0055  95  VAL   A N   
2035 C  CA  . VAL   A 95  ? 0.1196 0.1203 0.1257 -0.0039 0.0091  0.0141  95  VAL   A CA  
2036 C  C   . VAL   A 95  ? 0.1215 0.1180 0.1220 -0.0122 0.0022  0.0056  95  VAL   A C   
2037 O  O   . VAL   A 95  ? 0.1313 0.1283 0.1289 0.0060  0.0065  0.0064  95  VAL   A O   
2038 C  CB  . VAL   A 95  ? 0.1253 0.1231 0.1501 -0.0120 0.0012  0.0127  95  VAL   A CB  
2039 C  CG1 . VAL   A 95  ? 0.1421 0.1207 0.1616 -0.0152 0.0012  -0.0016 95  VAL   A CG1 
2040 C  CG2 . VAL   A 95  ? 0.1300 0.1254 0.1570 -0.0147 0.0023  0.0242  95  VAL   A CG2 
2050 N  N   . VAL   A 96  ? 0.1261 0.1207 0.1110 -0.0032 0.0062  0.0115  96  VAL   A N   
2051 C  CA  . VAL   A 96  ? 0.1345 0.1202 0.1370 -0.0006 0.0034  0.0203  96  VAL   A CA  
2052 C  C   . VAL   A 96  ? 0.1364 0.1281 0.1315 -0.0012 0.0035  0.0164  96  VAL   A C   
2053 O  O   . VAL   A 96  ? 0.1426 0.1379 0.1494 -0.0070 0.0172  -0.0018 96  VAL   A O   
2054 C  CB  . VAL   A 96  ? 0.1396 0.1258 0.1434 -0.0045 0.0183  0.0210  96  VAL   A CB  
2055 C  CG1 . VAL   A 96  ? 0.1508 0.1342 0.1342 0.0033  0.0202  0.0127  96  VAL   A CG1 
2056 C  CG2 . VAL   A 96  ? 0.1416 0.1297 0.1536 -0.0157 0.0156  0.0177  96  VAL   A CG2 
2066 N  N   A GLY   A 97  ? 0.1382 0.1327 0.1360 -0.0077 0.0039  0.0106  97  GLY   A N   
2067 N  N   B GLY   A 97  ? 0.1403 0.1323 0.1253 -0.0055 0.0024  0.0119  97  GLY   A N   
2068 C  CA  A GLY   A 97  ? 0.1469 0.1416 0.1431 -0.0056 -0.0004 0.0149  97  GLY   A CA  
2069 C  CA  B GLY   A 97  ? 0.1511 0.1381 0.1299 -0.0017 -0.0028 0.0213  97  GLY   A CA  
2070 C  C   A GLY   A 97  ? 0.1489 0.1524 0.1317 -0.0095 0.0013  0.0094  97  GLY   A C   
2071 C  C   B GLY   A 97  ? 0.1554 0.1485 0.1277 -0.0041 -0.0036 0.0221  97  GLY   A C   
2072 O  O   A GLY   A 97  ? 0.1539 0.1510 0.1515 -0.0114 0.0018  0.0085  97  GLY   A O   
2073 O  O   B GLY   A 97  ? 0.1632 0.1510 0.1437 -0.0041 0.0011  0.0222  97  GLY   A O   
2080 N  N   A PRO   A 98  ? 0.1556 0.1533 0.1116 0.0001  -0.0014 0.0108  98  PRO   A N   
2081 N  N   B PRO   A 98  ? 0.1664 0.1508 0.1389 -0.0013 -0.0076 0.0278  98  PRO   A N   
2082 C  CA  A PRO   A 98  ? 0.1631 0.1649 0.1088 0.0011  0.0032  -0.0015 98  PRO   A CA  
2083 C  CA  B PRO   A 98  ? 0.1787 0.1599 0.1594 -0.0032 -0.0083 0.0126  98  PRO   A CA  
2084 C  C   A PRO   A 98  ? 0.1592 0.1726 0.0936 -0.0049 0.0008  0.0062  98  PRO   A C   
2085 C  C   B PRO   A 98  ? 0.1967 0.1550 0.1492 -0.0059 -0.0067 0.0217  98  PRO   A C   
2086 O  O   A PRO   A 98  ? 0.1499 0.1664 0.1139 -0.0049 0.0010  0.0092  98  PRO   A O   
2087 O  O   B PRO   A 98  ? 0.1862 0.1471 0.1804 0.0035  -0.0035 0.0206  98  PRO   A O   
2088 C  CB  A PRO   A 98  ? 0.1733 0.1721 0.1031 0.0058  -0.0031 -0.0011 98  PRO   A CB  
2089 C  CB  B PRO   A 98  ? 0.1833 0.1582 0.1545 0.0008  -0.0136 0.0136  98  PRO   A CB  
2090 C  CG  A PRO   A 98  ? 0.1742 0.1698 0.1268 0.0037  -0.0038 -0.0079 98  PRO   A CG  
2091 C  CG  B PRO   A 98  ? 0.1846 0.1547 0.1594 -0.0028 -0.0156 0.0136  98  PRO   A CG  
2092 C  CD  A PRO   A 98  ? 0.1628 0.1593 0.1215 -0.0004 -0.0021 0.0016  98  PRO   A CD  
2093 C  CD  B PRO   A 98  ? 0.1731 0.1475 0.1434 -0.0042 -0.0133 0.0258  98  PRO   A CD  
2108 N  N   A ASN   A 99  ? 0.1628 0.1893 0.1023 -0.0029 0.0018  0.0235  99  ASN   A N   
2109 N  N   B ASN   A 99  ? 0.2291 0.1586 0.1335 -0.0021 -0.0049 0.0348  99  ASN   A N   
2110 C  CA  A ASN   A 99  ? 0.1785 0.1992 0.1038 -0.0083 0.0117  0.0250  99  ASN   A CA  
2111 C  CA  B ASN   A 99  ? 0.2607 0.1620 0.1301 0.0053  -0.0120 0.0489  99  ASN   A CA  
2112 C  C   A ASN   A 99  ? 0.2001 0.2173 0.1011 -0.0214 0.0154  0.0260  99  ASN   A C   
2113 C  C   B ASN   A 99  ? 0.2776 0.1717 0.1334 0.0074  -0.0229 0.0461  99  ASN   A C   
2114 O  O   A ASN   A 99  ? 0.2117 0.2346 0.1197 -0.0083 -0.0000 0.0137  99  ASN   A O   
2115 O  O   B ASN   A 99  ? 0.2788 0.1568 0.1334 0.0157  -0.0244 0.0294  99  ASN   A O   
2116 C  CB  A ASN   A 99  ? 0.1690 0.1931 0.0959 -0.0069 0.0118  0.0303  99  ASN   A CB  
2117 C  CB  B ASN   A 99  ? 0.2744 0.1602 0.1606 0.0081  -0.0226 0.0383  99  ASN   A CB  
2118 C  CG  A ASN   A 99  ? 0.1689 0.1880 0.1102 -0.0011 0.0058  0.0196  99  ASN   A CG  
2119 C  CG  B ASN   A 99  ? 0.2884 0.1689 0.1913 0.0080  -0.0292 0.0370  99  ASN   A CG  
2120 O  OD1 A ASN   A 99  ? 0.1772 0.1987 0.1206 0.0113  0.0008  0.0031  99  ASN   A OD1 
2121 O  OD1 B ASN   A 99  ? 0.2943 0.1752 0.1858 0.0091  -0.0309 0.0347  99  ASN   A OD1 
2122 N  ND2 A ASN   A 99  ? 0.1734 0.1842 0.1320 -0.0029 -0.0117 0.0284  99  ASN   A ND2 
2123 N  ND2 B ASN   A 99  ? 0.2915 0.1757 0.2286 0.0157  -0.0416 0.0267  99  ASN   A ND2 
2136 N  N   A VAL   A 100 ? 0.2179 0.2222 0.0992 -0.0380 -0.0135 0.0119  100 VAL   A N   
2137 N  N   B VAL   A 100 ? 0.2937 0.2022 0.1570 0.0035  -0.0370 0.0415  100 VAL   A N   
2138 C  CA  A VAL   A 100 ? 0.2458 0.2381 0.1398 -0.0404 -0.0282 0.0177  100 VAL   A CA  
2139 C  CA  B VAL   A 100 ? 0.3110 0.2252 0.1967 0.0036  -0.0477 0.0319  100 VAL   A CA  
2140 C  C   A VAL   A 100 ? 0.2577 0.2483 0.1313 -0.0432 -0.0308 0.0357  100 VAL   A C   
2141 C  C   B VAL   A 100 ? 0.3189 0.2316 0.2033 0.0119  -0.0572 0.0334  100 VAL   A C   
2142 O  O   A VAL   A 100 ? 0.2636 0.2546 0.1326 -0.0406 -0.0147 0.0441  100 VAL   A O   
2143 O  O   B VAL   A 100 ? 0.3220 0.2286 0.2071 0.0082  -0.0517 0.0182  100 VAL   A O   
2144 C  CB  A VAL   A 100 ? 0.2648 0.2432 0.1911 -0.0452 -0.0336 0.0164  100 VAL   A CB  
2145 C  CB  B VAL   A 100 ? 0.3200 0.2435 0.2278 0.0005  -0.0517 0.0183  100 VAL   A CB  
2146 C  CG1 A VAL   A 100 ? 0.2662 0.2442 0.2134 -0.0490 -0.0303 0.0153  100 VAL   A CG1 
2147 C  CG1 B VAL   A 100 ? 0.3205 0.2449 0.2449 0.0006  -0.0507 0.0212  100 VAL   A CG1 
2148 C  CG2 A VAL   A 100 ? 0.2753 0.2474 0.2010 -0.0472 -0.0366 0.0178  100 VAL   A CG2 
2149 C  CG2 B VAL   A 100 ? 0.3243 0.2538 0.2346 -0.0004 -0.0504 0.0109  100 VAL   A CG2 
2168 N  N   A ASN   A 101 ? 0.2660 0.2531 0.1493 -0.0433 -0.0375 0.0607  101 ASN   A N   
2169 N  N   B ASN   A 101 ? 0.3249 0.2446 0.2054 0.0210  -0.0672 0.0490  101 ASN   A N   
2170 C  CA  A ASN   A 101 ? 0.2856 0.2620 0.1686 -0.0421 -0.0379 0.0776  101 ASN   A CA  
2171 C  CA  B ASN   A 101 ? 0.3356 0.2582 0.2219 0.0264  -0.0639 0.0561  101 ASN   A CA  
2172 C  C   A ASN   A 101 ? 0.3095 0.2887 0.1827 -0.0480 -0.0160 0.0980  101 ASN   A C   
2173 C  C   B ASN   A 101 ? 0.3517 0.2763 0.2262 0.0255  -0.0467 0.0755  101 ASN   A C   
2174 O  O   A ASN   A 101 ? 0.3225 0.2938 0.2139 -0.0454 -0.0148 0.0952  101 ASN   A O   
2175 O  O   B ASN   A 101 ? 0.3586 0.2818 0.2234 0.0231  -0.0437 0.0809  101 ASN   A O   
2176 C  CB  A ASN   A 101 ? 0.2838 0.2450 0.1575 -0.0334 -0.0586 0.0699  101 ASN   A CB  
2177 C  CB  B ASN   A 101 ? 0.3308 0.2553 0.2376 0.0277  -0.0699 0.0452  101 ASN   A CB  
2178 C  CG  A ASN   A 101 ? 0.2840 0.2308 0.1635 -0.0255 -0.0691 0.0351  101 ASN   A CG  
2179 C  CG  B ASN   A 101 ? 0.3279 0.2588 0.2597 0.0250  -0.0729 0.0305  101 ASN   A CG  
2180 O  OD1 A ASN   A 101 ? 0.2793 0.2340 0.1723 -0.0074 -0.0724 -0.0024 101 ASN   A OD1 
2181 O  OD1 B ASN   A 101 ? 0.3357 0.2679 0.2855 0.0161  -0.0648 0.0228  101 ASN   A OD1 
2182 N  ND2 A ASN   A 101 ? 0.2884 0.2188 0.1682 -0.0317 -0.0628 0.0416  101 ASN   A ND2 
2183 N  ND2 B ASN   A 101 ? 0.3223 0.2534 0.2693 0.0294  -0.0735 0.0215  101 ASN   A ND2 
2196 N  N   A LYS   A 102 ? 0.3189 0.3171 0.2144 -0.0536 -0.0069 0.0918  102 LYS   A N   
2197 N  N   B LYS   A 102 ? 0.3610 0.2922 0.2558 0.0237  -0.0281 0.0743  102 LYS   A N   
2198 C  CA  A LYS   A 102 ? 0.3328 0.3427 0.2428 -0.0529 -0.0138 0.0754  102 LYS   A CA  
2199 C  CA  B LYS   A 102 ? 0.3727 0.3090 0.2634 0.0143  -0.0131 0.0724  102 LYS   A CA  
2200 C  C   A LYS   A 102 ? 0.3409 0.3616 0.2312 -0.0426 -0.0171 0.0657  102 LYS   A C   
2201 C  C   B LYS   A 102 ? 0.3745 0.3069 0.2414 0.0111  -0.0139 0.0882  102 LYS   A C   
2202 O  O   A LYS   A 102 ? 0.3449 0.3707 0.2441 -0.0376 -0.0169 0.0615  102 LYS   A O   
2203 O  O   B LYS   A 102 ? 0.3773 0.3065 0.2466 0.0098  -0.0085 0.0978  102 LYS   A O   
2204 C  CB  A LYS   A 102 ? 0.3415 0.3493 0.2899 -0.0600 -0.0225 0.0572  102 LYS   A CB  
2205 C  CB  B LYS   A 102 ? 0.3833 0.3280 0.3053 0.0103  -0.0104 0.0461  102 LYS   A CB  
2206 C  CG  A LYS   A 102 ? 0.3495 0.3528 0.3296 -0.0659 -0.0344 0.0364  102 LYS   A CG  
2207 C  CG  B LYS   A 102 ? 0.3924 0.3446 0.3482 0.0067  -0.0089 0.0210  102 LYS   A CG  
2208 C  CD  A LYS   A 102 ? 0.3584 0.3573 0.3659 -0.0687 -0.0466 0.0151  102 LYS   A CD  
2209 C  CD  B LYS   A 102 ? 0.4025 0.3611 0.3934 0.0042  -0.0100 -0.0020 102 LYS   A CD  
2210 C  CE  A LYS   A 102 ? 0.3653 0.3589 0.3928 -0.0703 -0.0537 0.0041  102 LYS   A CE  
2211 C  CE  B LYS   A 102 ? 0.4095 0.3730 0.4270 0.0029  -0.0142 -0.0150 102 LYS   A CE  
2212 N  NZ  A LYS   A 102 ? 0.3677 0.3582 0.4056 -0.0755 -0.0555 -0.0043 102 LYS   A NZ  
2213 N  NZ  B LYS   A 102 ? 0.4134 0.3795 0.4489 0.0027  -0.0162 -0.0248 102 LYS   A NZ  
2240 N  N   A GLY   A 103 ? 0.3425 0.3713 0.2281 -0.0347 -0.0168 0.0464  103 GLY   A N   
2241 N  N   B GLY   A 103 ? 0.3716 0.3087 0.2206 0.0091  -0.0254 0.0822  103 GLY   A N   
2242 C  CA  A GLY   A 103 ? 0.3464 0.3781 0.2299 -0.0285 -0.0116 0.0308  103 GLY   A CA  
2243 C  CA  B GLY   A 103 ? 0.3672 0.3045 0.2101 0.0048  -0.0289 0.0767  103 GLY   A CA  
2244 C  C   A GLY   A 103 ? 0.3449 0.3844 0.2332 -0.0265 -0.0009 0.0190  103 GLY   A C   
2245 C  C   B GLY   A 103 ? 0.3564 0.2929 0.1915 -0.0028 -0.0259 0.0685  103 GLY   A C   
2246 O  O   A GLY   A 103 ? 0.3517 0.3869 0.2525 -0.0249 0.0029  0.0110  103 GLY   A O   
2247 O  O   B GLY   A 103 ? 0.3645 0.2971 0.1947 -0.0024 -0.0251 0.0697  103 GLY   A O   
2254 N  N   A GLU   A 104 ? 0.3320 0.3849 0.2070 -0.0299 0.0118  0.0121  104 GLU   A N   
2255 N  N   B GLU   A 104 ? 0.3342 0.2751 0.1746 -0.0088 -0.0321 0.0615  104 GLU   A N   
2256 C  CA  A GLU   A 104 ? 0.3157 0.3817 0.1983 -0.0375 0.0191  0.0099  104 GLU   A CA  
2257 C  CA  B GLU   A 104 ? 0.3093 0.2542 0.1525 -0.0180 -0.0353 0.0496  104 GLU   A CA  
2258 C  C   A GLU   A 104 ? 0.3166 0.3917 0.2013 -0.0345 0.0157  -0.0018 104 GLU   A C   
2259 C  C   B GLU   A 104 ? 0.2916 0.2409 0.1571 -0.0110 -0.0268 0.0307  104 GLU   A C   
2260 O  O   A GLU   A 104 ? 0.3145 0.3921 0.2092 -0.0364 0.0105  -0.0138 104 GLU   A O   
2261 O  O   B GLU   A 104 ? 0.2851 0.2297 0.1899 -0.0090 -0.0308 0.0267  104 GLU   A O   
2262 C  CB  A GLU   A 104 ? 0.2957 0.3683 0.1887 -0.0490 0.0304  0.0238  104 GLU   A CB  
2263 C  CB  B GLU   A 104 ? 0.3008 0.2469 0.1467 -0.0312 -0.0349 0.0601  104 GLU   A CB  
2264 C  CG  A GLU   A 104 ? 0.2798 0.3556 0.1973 -0.0581 0.0349  0.0348  104 GLU   A CG  
2265 C  CG  B GLU   A 104 ? 0.2991 0.2491 0.1585 -0.0420 -0.0373 0.0700  104 GLU   A CG  
2266 C  CD  A GLU   A 104 ? 0.2641 0.3434 0.1994 -0.0667 0.0442  0.0442  104 GLU   A CD  
2267 C  CD  B GLU   A 104 ? 0.2940 0.2509 0.1518 -0.0492 -0.0436 0.0834  104 GLU   A CD  
2268 O  OE1 A GLU   A 104 ? 0.2507 0.3357 0.1663 -0.0686 0.0494  0.0440  104 GLU   A OE1 
2269 O  OE1 B GLU   A 104 ? 0.2897 0.2542 0.1478 -0.0478 -0.0554 0.0734  104 GLU   A OE1 
2270 O  OE2 A GLU   A 104 ? 0.2694 0.3432 0.2324 -0.0683 0.0429  0.0453  104 GLU   A OE2 
2271 O  OE2 B GLU   A 104 ? 0.2992 0.2516 0.1554 -0.0584 -0.0370 0.0896  104 GLU   A OE2 
2284 N  N   A ASP   A 105 ? 0.3188 0.4013 0.2161 -0.0279 0.0157  -0.0053 105 ASP   A N   
2285 N  N   B ASP   A 105 ? 0.2868 0.2381 0.1654 -0.0095 -0.0140 0.0242  105 ASP   A N   
2286 C  CA  A ASP   A 105 ? 0.3162 0.4078 0.2391 -0.0245 0.0151  -0.0168 105 ASP   A CA  
2287 C  CA  B ASP   A 105 ? 0.2789 0.2366 0.1893 -0.0025 -0.0003 -0.0056 105 ASP   A CA  
2288 C  C   A ASP   A 105 ? 0.2876 0.3976 0.2228 -0.0339 0.0010  -0.0320 105 ASP   A C   
2289 C  C   B ASP   A 105 ? 0.2584 0.2177 0.1687 -0.0108 0.0057  -0.0095 105 ASP   A C   
2290 O  O   A ASP   A 105 ? 0.2759 0.3958 0.1903 -0.0349 -0.0014 -0.0446 105 ASP   A O   
2291 O  O   B ASP   A 105 ? 0.2402 0.2099 0.1322 -0.0140 0.0076  -0.0137 105 ASP   A O   
2292 C  CB  A ASP   A 105 ? 0.3383 0.4211 0.2850 -0.0129 0.0237  -0.0129 105 ASP   A CB  
2293 C  CB  B ASP   A 105 ? 0.2912 0.2571 0.2412 0.0099  0.0046  -0.0228 105 ASP   A CB  
2294 C  CG  A ASP   A 105 ? 0.3559 0.4315 0.3268 -0.0038 0.0245  -0.0120 105 ASP   A CG  
2295 C  CG  B ASP   A 105 ? 0.3025 0.2725 0.2811 0.0220  0.0056  -0.0433 105 ASP   A CG  
2296 O  OD1 A ASP   A 105 ? 0.3615 0.4361 0.3312 -0.0012 0.0243  -0.0191 105 ASP   A OD1 
2297 O  OD1 B ASP   A 105 ? 0.3090 0.2736 0.2734 0.0184  -0.0006 -0.0589 105 ASP   A OD1 
2298 O  OD2 A ASP   A 105 ? 0.3636 0.4354 0.3522 -0.0002 0.0248  -0.0043 105 ASP   A OD2 
2299 O  OD2 B ASP   A 105 ? 0.3077 0.2835 0.3214 0.0273  -0.0021 -0.0387 105 ASP   A OD2 
2308 N  N   A ILE   A 106 ? 0.2681 0.3852 0.2377 -0.0445 -0.0231 -0.0402 106 ILE   A N   
2309 N  N   B ILE   A 106 ? 0.2547 0.2178 0.1868 -0.0080 -0.0107 -0.0030 106 ILE   A N   
2310 C  CA  A ILE   A 106 ? 0.2406 0.3679 0.2516 -0.0560 -0.0409 -0.0550 106 ILE   A CA  
2311 C  CA  B ILE   A 106 ? 0.2490 0.2238 0.1982 -0.0172 -0.0216 -0.0020 106 ILE   A CA  
2312 C  C   A ILE   A 106 ? 0.2111 0.3400 0.2490 -0.0760 -0.0384 -0.0803 106 ILE   A C   
2313 C  C   B ILE   A 106 ? 0.2478 0.2179 0.1958 -0.0224 -0.0138 0.0202  106 ILE   A C   
2314 O  O   A ILE   A 106 ? 0.1833 0.3287 0.2522 -0.0825 -0.0230 -0.0864 106 ILE   A O   
2315 O  O   B ILE   A 106 ? 0.2386 0.2231 0.2068 -0.0244 -0.0027 0.0227  106 ILE   A O   
2316 C  CB  A ILE   A 106 ? 0.2484 0.3764 0.2863 -0.0434 -0.0505 -0.0333 106 ILE   A CB  
2317 C  CB  B ILE   A 106 ? 0.2534 0.2476 0.2478 -0.0163 -0.0374 0.0001  106 ILE   A CB  
2318 C  CG1 A ILE   A 106 ? 0.2481 0.3782 0.3105 -0.0327 -0.0544 -0.0184 106 ILE   A CG1 
2319 C  CG1 B ILE   A 106 ? 0.2531 0.2641 0.2777 -0.0097 -0.0426 0.0053  106 ILE   A CG1 
2320 C  CG2 A ILE   A 106 ? 0.2515 0.3787 0.2935 -0.0419 -0.0553 -0.0296 106 ILE   A CG2 
2321 C  CG2 B ILE   A 106 ? 0.2551 0.2535 0.2599 -0.0189 -0.0410 -0.0051 106 ILE   A CG2 
2322 C  CD1 A ILE   A 106 ? 0.2505 0.3781 0.3256 -0.0241 -0.0484 -0.0111 106 ILE   A CD1 
2323 C  CD1 B ILE   A 106 ? 0.2517 0.2696 0.2914 -0.0051 -0.0400 0.0078  106 ILE   A CD1 
2346 N  N   A GLN   A 107 ? 0.2245 0.3250 0.2653 -0.0756 -0.0276 -0.0922 107 GLN   A N   
2347 N  N   B GLN   A 107 ? 0.2588 0.2059 0.2139 -0.0178 -0.0107 0.0278  107 GLN   A N   
2348 C  CA  A GLN   A 107 ? 0.2424 0.3068 0.3120 -0.0610 -0.0060 -0.0897 107 GLN   A CA  
2349 C  CA  B GLN   A 107 ? 0.2739 0.2090 0.2646 -0.0150 -0.0095 0.0273  107 GLN   A CA  
2350 C  C   A GLN   A 107 ? 0.2187 0.2660 0.2962 -0.0501 0.0224  -0.0765 107 GLN   A C   
2351 C  C   B GLN   A 107 ? 0.2479 0.1810 0.2389 -0.0089 -0.0044 0.0396  107 GLN   A C   
2352 O  O   A GLN   A 107 ? 0.2284 0.2667 0.3442 -0.0396 0.0372  -0.0654 107 GLN   A O   
2353 O  O   B GLN   A 107 ? 0.2503 0.1691 0.2355 -0.0067 -0.0152 0.0334  107 GLN   A O   
2354 C  CB  A GLN   A 107 ? 0.2789 0.3300 0.3851 -0.0607 -0.0129 -0.0823 107 GLN   A CB  
2355 C  CB  B GLN   A 107 ? 0.3093 0.2491 0.3327 -0.0256 -0.0208 0.0208  107 GLN   A CB  
2356 C  CG  A GLN   A 107 ? 0.3103 0.3523 0.4635 -0.0587 -0.0204 -0.0689 107 GLN   A CG  
2357 C  CG  B GLN   A 107 ? 0.3394 0.2867 0.4045 -0.0326 -0.0361 0.0269  107 GLN   A CG  
2358 C  CD  A GLN   A 107 ? 0.3352 0.3688 0.5297 -0.0583 -0.0264 -0.0546 107 GLN   A CD  
2359 C  CD  B GLN   A 107 ? 0.3643 0.3212 0.4678 -0.0354 -0.0460 0.0342  107 GLN   A CD  
2360 O  OE1 A GLN   A 107 ? 0.3448 0.3769 0.5610 -0.0571 -0.0303 -0.0508 107 GLN   A OE1 
2361 O  OE1 B GLN   A 107 ? 0.3730 0.3315 0.4842 -0.0362 -0.0468 0.0429  107 GLN   A OE1 
2362 N  NE2 A GLN   A 107 ? 0.3434 0.3736 0.5492 -0.0604 -0.0279 -0.0520 107 GLN   A NE2 
2363 N  NE2 B GLN   A 107 ? 0.3720 0.3330 0.4899 -0.0361 -0.0534 0.0337  107 GLN   A NE2 
2380 N  N   A LEU   A 108 ? 0.1853 0.2195 0.2312 -0.0446 0.0340  -0.0819 108 LEU   A N   
2381 N  N   B LEU   A 108 ? 0.2196 0.1753 0.2191 -0.0216 0.0120  0.0255  108 LEU   A N   
2382 C  CA  A LEU   A 108 ? 0.1755 0.1902 0.2100 -0.0186 0.0297  -0.0352 108 LEU   A CA  
2383 C  CA  B LEU   A 108 ? 0.1976 0.1667 0.2061 -0.0156 0.0158  0.0158  108 LEU   A CA  
2384 C  C   A LEU   A 108 ? 0.1601 0.1572 0.1949 -0.0053 0.0235  -0.0009 108 LEU   A C   
2385 C  C   B LEU   A 108 ? 0.1718 0.1468 0.1950 -0.0036 0.0168  0.0230  108 LEU   A C   
2386 O  O   A LEU   A 108 ? 0.1543 0.1570 0.2049 -0.0033 0.0227  0.0023  108 LEU   A O   
2387 O  O   B LEU   A 108 ? 0.1675 0.1508 0.2115 0.0009  0.0185  0.0229  108 LEU   A O   
2388 C  CB  A LEU   A 108 ? 0.1831 0.2005 0.2004 -0.0165 0.0325  -0.0210 108 LEU   A CB  
2389 C  CB  B LEU   A 108 ? 0.2039 0.1845 0.1966 -0.0262 0.0215  0.0038  108 LEU   A CB  
2390 C  CG  A LEU   A 108 ? 0.1944 0.2166 0.2098 -0.0102 0.0365  -0.0144 108 LEU   A CG  
2391 C  CG  B LEU   A 108 ? 0.2124 0.2066 0.2066 -0.0300 0.0225  -0.0111 108 LEU   A CG  
2392 C  CD1 A LEU   A 108 ? 0.2105 0.2240 0.2124 -0.0131 0.0424  -0.0121 108 LEU   A CD1 
2393 C  CD1 B LEU   A 108 ? 0.2252 0.2166 0.2108 -0.0326 0.0318  -0.0158 108 LEU   A CD1 
2394 C  CD2 A LEU   A 108 ? 0.1928 0.2281 0.2376 -0.0032 0.0350  -0.0127 108 LEU   A CD2 
2395 C  CD2 B LEU   A 108 ? 0.2087 0.2226 0.2305 -0.0344 0.0150  -0.0168 108 LEU   A CD2 
2418 N  N   . LEU   A 109 ? 0.1516 0.1485 0.1994 0.0027  0.0175  0.0216  109 LEU   A N   
2419 C  CA  . LEU   A 109 ? 0.1491 0.1389 0.1883 0.0015  0.0005  0.0181  109 LEU   A CA  
2420 C  C   . LEU   A 109 ? 0.1314 0.1352 0.1759 -0.0064 0.0027  0.0071  109 LEU   A C   
2421 O  O   . LEU   A 109 ? 0.1445 0.1266 0.1925 -0.0064 -0.0059 0.0034  109 LEU   A O   
2422 C  CB  . LEU   A 109 ? 0.1554 0.1490 0.1979 0.0065  -0.0085 0.0352  109 LEU   A CB  
2423 C  CG  . LEU   A 109 ? 0.1487 0.1611 0.2138 0.0027  0.0005  0.0371  109 LEU   A CG  
2424 C  CD1 . LEU   A 109 ? 0.1547 0.1544 0.2266 -0.0020 0.0085  0.0175  109 LEU   A CD1 
2425 C  CD2 . LEU   A 109 ? 0.1509 0.1779 0.2413 0.0033  0.0030  0.0367  109 LEU   A CD2 
2438 N  N   . LYS   A 110 ? 0.1336 0.1331 0.1807 -0.0078 0.0015  0.0093  110 LYS   A N   
2439 C  CA  . LYS   A 110 ? 0.1349 0.1268 0.1884 -0.0102 0.0018  0.0146  110 LYS   A CA  
2440 C  C   . LYS   A 110 ? 0.1384 0.1214 0.1740 -0.0109 0.0013  0.0077  110 LYS   A C   
2441 O  O   . LYS   A 110 ? 0.1346 0.1255 0.1830 -0.0092 0.0068  0.0013  110 LYS   A O   
2442 C  CB  . LYS   A 110 ? 0.1441 0.1337 0.2057 -0.0064 -0.0077 0.0007  110 LYS   A CB  
2443 C  CG  . LYS   A 110 ? 0.1418 0.1324 0.2153 -0.0070 -0.0088 -0.0006 110 LYS   A CG  
2444 C  CD  . LYS   A 110 ? 0.1489 0.1378 0.2354 -0.0109 -0.0079 -0.0025 110 LYS   A CD  
2445 C  CE  . LYS   A 110 ? 0.1610 0.1459 0.2531 -0.0137 0.0085  -0.0065 110 LYS   A CE  
2446 N  NZ  . LYS   A 110 ? 0.1655 0.1475 0.2684 -0.0221 0.0170  0.0004  110 LYS   A NZ  
2460 N  N   . SER   A 111 ? 0.1400 0.1259 0.1718 -0.0039 -0.0002 0.0103  111 SER   A N   
2461 C  CA  . SER   A 111 ? 0.1353 0.1309 0.1786 -0.0064 0.0090  -0.0000 111 SER   A CA  
2462 C  C   . SER   A 111 ? 0.1306 0.1264 0.1653 -0.0118 0.0073  0.0141  111 SER   A C   
2463 O  O   . SER   A 111 ? 0.1448 0.1208 0.1777 -0.0076 0.0068  0.0076  111 SER   A O   
2464 C  CB  . SER   A 111 ? 0.1467 0.1482 0.1947 -0.0053 0.0143  -0.0043 111 SER   A CB  
2465 O  OG  . SER   A 111 ? 0.1967 0.1712 0.1950 0.0001  0.0245  -0.0109 111 SER   A OG  
2471 N  N   . ALA   A 112 ? 0.1319 0.1163 0.1786 -0.0032 0.0124  0.0100  112 ALA   A N   
2472 C  CA  . ALA   A 112 ? 0.1346 0.1196 0.1715 -0.0043 0.0199  0.0023  112 ALA   A CA  
2473 C  C   . ALA   A 112 ? 0.1314 0.1128 0.1746 -0.0010 0.0079  0.0038  112 ALA   A C   
2474 O  O   . ALA   A 112 ? 0.1351 0.1173 0.1877 -0.0111 0.0137  0.0129  112 ALA   A O   
2475 C  CB  . ALA   A 112 ? 0.1439 0.1186 0.1740 -0.0086 0.0106  0.0088  112 ALA   A CB  
2481 N  N   . TYR   A 113 ? 0.1242 0.1201 0.1858 -0.0062 0.0112  0.0121  113 TYR   A N   
2482 C  CA  . TYR   A 113 ? 0.1223 0.1141 0.1780 -0.0061 0.0146  0.0148  113 TYR   A CA  
2483 C  C   . TYR   A 113 ? 0.1208 0.1174 0.1610 -0.0122 0.0084  0.0101  113 TYR   A C   
2484 O  O   . TYR   A 113 ? 0.1214 0.1247 0.1733 -0.0064 0.0131  0.0105  113 TYR   A O   
2485 C  CB  . TYR   A 113 ? 0.1243 0.1275 0.1857 -0.0027 0.0003  0.0247  113 TYR   A CB  
2486 C  CG  . TYR   A 113 ? 0.1290 0.1339 0.1778 -0.0122 0.0086  0.0271  113 TYR   A CG  
2487 C  CD1 . TYR   A 113 ? 0.1293 0.1417 0.1725 -0.0021 0.0135  0.0313  113 TYR   A CD1 
2488 C  CD2 . TYR   A 113 ? 0.1287 0.1408 0.1707 -0.0114 0.0019  0.0243  113 TYR   A CD2 
2489 C  CE1 . TYR   A 113 ? 0.1404 0.1495 0.1704 -0.0018 0.0068  0.0382  113 TYR   A CE1 
2490 C  CE2 . TYR   A 113 ? 0.1363 0.1493 0.1770 -0.0095 0.0037  0.0287  113 TYR   A CE2 
2491 C  CZ  . TYR   A 113 ? 0.1334 0.1500 0.1744 0.0044  0.0117  0.0367  113 TYR   A CZ  
2492 O  OH  . TYR   A 113 ? 0.1339 0.1581 0.1992 0.0173  0.0110  0.0351  113 TYR   A OH  
2502 N  N   . GLU   A 114 ? 0.1187 0.1185 0.1763 -0.0051 0.0096  0.0124  114 GLU   A N   
2503 C  CA  . GLU   A 114 ? 0.1202 0.1139 0.1952 0.0021  0.0056  0.0182  114 GLU   A CA  
2504 C  C   . GLU   A 114 ? 0.1191 0.1170 0.1905 0.0005  0.0165  0.0154  114 GLU   A C   
2505 O  O   . GLU   A 114 ? 0.1316 0.1174 0.1892 -0.0007 0.0057  0.0135  114 GLU   A O   
2506 C  CB  . GLU   A 114 ? 0.1219 0.1194 0.1836 -0.0065 0.0021  0.0180  114 GLU   A CB  
2507 C  CG  . GLU   A 114 ? 0.1296 0.1288 0.1940 -0.0016 0.0060  0.0063  114 GLU   A CG  
2508 C  CD  . GLU   A 114 ? 0.1447 0.1165 0.1959 -0.0068 0.0008  0.0119  114 GLU   A CD  
2509 O  OE1 . GLU   A 114 ? 0.1439 0.1209 0.1969 -0.0085 0.0109  -0.0019 114 GLU   A OE1 
2510 O  OE2 . GLU   A 114 ? 0.1611 0.1236 0.2194 -0.0103 0.0066  -0.0054 114 GLU   A OE2 
2517 N  N   . ASN   A 115 ? 0.1249 0.1211 0.1699 -0.0086 0.0118  0.0090  115 ASN   A N   
2518 C  CA  . ASN   A 115 ? 0.1237 0.1245 0.1764 -0.0065 0.0098  0.0159  115 ASN   A CA  
2519 C  C   . ASN   A 115 ? 0.1260 0.1233 0.1680 -0.0088 0.0033  0.0097  115 ASN   A C   
2520 O  O   . ASN   A 115 ? 0.1318 0.1378 0.1698 -0.0115 0.0095  0.0186  115 ASN   A O   
2521 C  CB  . ASN   A 115 ? 0.1352 0.1275 0.1694 -0.0109 0.0136  0.0125  115 ASN   A CB  
2522 C  CG  . ASN   A 115 ? 0.1326 0.1512 0.1796 -0.0175 0.0155  0.0101  115 ASN   A CG  
2523 O  OD1 . ASN   A 115 ? 0.1368 0.2483 0.2044 -0.0153 0.0222  0.0225  115 ASN   A OD1 
2524 N  ND2 . ASN   A 115 ? 0.1376 0.1319 0.1822 -0.0160 0.0211  0.0140  115 ASN   A ND2 
2531 N  N   . PHE   A 116 ? 0.1227 0.1217 0.1779 -0.0022 0.0102  0.0180  116 PHE   A N   
2532 C  CA  . PHE   A 116 ? 0.1226 0.1310 0.1658 -0.0049 0.0161  0.0173  116 PHE   A CA  
2533 C  C   . PHE   A 116 ? 0.1197 0.1386 0.1760 -0.0075 0.0183  0.0259  116 PHE   A C   
2534 O  O   . PHE   A 116 ? 0.1281 0.1442 0.1794 0.0008  0.0129  0.0275  116 PHE   A O   
2535 C  CB  . PHE   A 116 ? 0.1275 0.1252 0.1779 -0.0085 0.0184  0.0169  116 PHE   A CB  
2536 C  CG  . PHE   A 116 ? 0.1266 0.1224 0.1695 -0.0054 0.0126  0.0080  116 PHE   A CG  
2537 C  CD1 . PHE   A 116 ? 0.1275 0.1235 0.1679 -0.0117 0.0143  0.0152  116 PHE   A CD1 
2538 C  CD2 . PHE   A 116 ? 0.1330 0.1352 0.1882 -0.0065 0.0153  0.0165  116 PHE   A CD2 
2539 C  CE1 . PHE   A 116 ? 0.1319 0.1226 0.1853 -0.0150 0.0102  0.0121  116 PHE   A CE1 
2540 C  CE2 . PHE   A 116 ? 0.1310 0.1325 0.1965 -0.0054 0.0126  0.0140  116 PHE   A CE2 
2541 C  CZ  . PHE   A 116 ? 0.1350 0.1185 0.1785 -0.0021 0.0128  0.0135  116 PHE   A CZ  
2551 N  N   . ASN   A 117 ? 0.1227 0.1332 0.1796 -0.0048 0.0138  0.0222  117 ASN   A N   
2552 C  CA  . ASN   A 117 ? 0.1298 0.1254 0.1888 -0.0073 0.0128  0.0291  117 ASN   A CA  
2553 C  C   . ASN   A 117 ? 0.1307 0.1383 0.1956 -0.0038 0.0118  0.0304  117 ASN   A C   
2554 O  O   . ASN   A 117 ? 0.1436 0.1436 0.2145 -0.0067 -0.0069 0.0447  117 ASN   A O   
2555 C  CB  . ASN   A 117 ? 0.1267 0.1303 0.1964 -0.0024 0.0098  0.0276  117 ASN   A CB  
2556 C  CG  . ASN   A 117 ? 0.1282 0.1331 0.1913 -0.0031 0.0112  0.0292  117 ASN   A CG  
2557 O  OD1 . ASN   A 117 ? 0.1292 0.1521 0.2029 -0.0125 0.0120  0.0248  117 ASN   A OD1 
2558 N  ND2 . ASN   A 117 ? 0.1233 0.1316 0.1923 -0.0023 0.0097  0.0284  117 ASN   A ND2 
2565 N  N   . GLN   A 118 ? 0.1243 0.1347 0.1988 -0.0086 0.0009  0.0335  118 GLN   A N   
2566 C  CA  . GLN   A 118 ? 0.1365 0.1445 0.2043 -0.0074 -0.0070 0.0232  118 GLN   A CA  
2567 C  C   . GLN   A 118 ? 0.1325 0.1542 0.1946 -0.0130 0.0005  0.0261  118 GLN   A C   
2568 O  O   . GLN   A 118 ? 0.1352 0.1881 0.2257 -0.0033 -0.0104 0.0182  118 GLN   A O   
2569 C  CB  . GLN   A 118 ? 0.1284 0.1477 0.2095 -0.0075 -0.0002 0.0252  118 GLN   A CB  
2570 C  CG  . GLN   A 118 ? 0.1243 0.1498 0.2094 -0.0016 0.0091  0.0235  118 GLN   A CG  
2571 C  CD  . GLN   A 118 ? 0.1272 0.1520 0.2194 -0.0001 0.0129  0.0198  118 GLN   A CD  
2572 O  OE1 . GLN   A 118 ? 0.1339 0.1651 0.2352 0.0053  -0.0041 0.0167  118 GLN   A OE1 
2573 N  NE2 . GLN   A 118 ? 0.1425 0.1462 0.2167 0.0047  0.0036  0.0195  118 GLN   A NE2 
2582 N  N   . HIS   A 119 ? 0.1400 0.1486 0.1779 -0.0086 -0.0044 0.0274  119 HIS   A N   
2583 C  CA  . HIS   A 119 ? 0.1519 0.1607 0.1797 -0.0092 -0.0024 0.0294  119 HIS   A CA  
2584 C  C   . HIS   A 119 ? 0.1602 0.1669 0.1713 -0.0133 0.0024  0.0333  119 HIS   A C   
2585 O  O   . HIS   A 119 ? 0.1612 0.1782 0.1828 -0.0289 0.0034  0.0332  119 HIS   A O   
2586 C  CB  . HIS   A 119 ? 0.1520 0.1591 0.2030 -0.0023 0.0188  0.0331  119 HIS   A CB  
2587 C  CG  . HIS   A 119 ? 0.1493 0.1630 0.2440 0.0055  0.0179  0.0474  119 HIS   A CG  
2588 N  ND1 . HIS   A 119 ? 0.1612 0.1799 0.2991 -0.0060 0.0118  0.0350  119 HIS   A ND1 
2589 C  CD2 . HIS   A 119 ? 0.1643 0.1733 0.2656 0.0142  0.0350  0.0646  119 HIS   A CD2 
2590 C  CE1 . HIS   A 119 ? 0.1600 0.1796 0.3221 -0.0125 0.0278  0.0464  119 HIS   A CE1 
2591 N  NE2 . HIS   A 119 ? 0.1738 0.1773 0.3155 0.0029  0.0481  0.0609  119 HIS   A NE2 
2599 N  N   . GLU   A 120 ? 0.1692 0.1915 0.1763 -0.0060 -0.0036 0.0546  120 GLU   A N   
2600 C  CA  . GLU   A 120 ? 0.1900 0.2222 0.1982 0.0019  -0.0001 0.0959  120 GLU   A CA  
2601 C  C   . GLU   A 120 ? 0.1722 0.2031 0.1858 -0.0147 -0.0015 0.0855  120 GLU   A C   
2602 O  O   . GLU   A 120 ? 0.1715 0.1969 0.2017 -0.0119 0.0035  0.0785  120 GLU   A O   
2603 C  CB  . GLU   A 120 ? 0.2618 0.2943 0.2661 0.0263  0.0005  0.1481  120 GLU   A CB  
2604 C  CG  . GLU   A 120 ? 0.3613 0.3767 0.3848 0.0403  -0.0012 0.1564  120 GLU   A CG  
2605 C  CD  . GLU   A 120 ? 0.4407 0.4428 0.5105 0.0495  0.0080  0.1463  120 GLU   A CD  
2606 O  OE1 . GLU   A 120 ? 0.4656 0.4656 0.5405 0.0515  0.0113  0.1421  120 GLU   A OE1 
2607 O  OE2 . GLU   A 120 ? 0.5040 0.5040 0.5687 0.0528  0.0131  0.1416  120 GLU   A OE2 
2614 N  N   . VAL   A 121 ? 0.1681 0.2068 0.1678 -0.0147 0.0055  0.0617  121 VAL   A N   
2615 C  CA  . VAL   A 121 ? 0.1763 0.2138 0.1568 -0.0127 0.0104  0.0630  121 VAL   A CA  
2616 C  C   . VAL   A 121 ? 0.1635 0.1949 0.1383 -0.0243 0.0013  0.0467  121 VAL   A C   
2617 O  O   . VAL   A 121 ? 0.1643 0.2005 0.1631 -0.0331 -0.0069 0.0357  121 VAL   A O   
2618 C  CB  . VAL   A 121 ? 0.2117 0.2497 0.1938 -0.0001 0.0252  0.0716  121 VAL   A CB  
2619 C  CG1 . VAL   A 121 ? 0.2163 0.2664 0.2010 0.0068  0.0311  0.0748  121 VAL   A CG1 
2620 C  CG2 . VAL   A 121 ? 0.2358 0.2665 0.2458 -0.0080 0.0189  0.0595  121 VAL   A CG2 
2630 N  N   . LEU   A 122 ? 0.1585 0.1751 0.1511 -0.0233 0.0096  0.0463  122 LEU   A N   
2631 C  CA  . LEU   A 122 ? 0.1618 0.1628 0.1593 -0.0210 0.0275  0.0385  122 LEU   A CA  
2632 C  C   . LEU   A 122 ? 0.1513 0.1612 0.1569 -0.0240 0.0089  0.0337  122 LEU   A C   
2633 O  O   . LEU   A 122 ? 0.1514 0.1719 0.1914 -0.0334 0.0052  0.0424  122 LEU   A O   
2634 C  CB  . LEU   A 122 ? 0.1793 0.1620 0.1913 -0.0103 0.0146  0.0447  122 LEU   A CB  
2635 C  CG  . LEU   A 122 ? 0.1817 0.1733 0.1843 -0.0121 0.0221  0.0373  122 LEU   A CG  
2636 C  CD1 . LEU   A 122 ? 0.1971 0.1664 0.1934 -0.0161 0.0193  0.0389  122 LEU   A CD1 
2637 C  CD2 . LEU   A 122 ? 0.1726 0.1616 0.1747 -0.0121 0.0292  0.0299  122 LEU   A CD2 
2649 N  N   A LEU   A 123 ? 0.1471 0.1574 0.1489 -0.0206 0.0084  0.0321  123 LEU   A N   
2650 N  N   B LEU   A 123 ? 0.1458 0.1601 0.1540 -0.0203 0.0011  0.0258  123 LEU   A N   
2651 C  CA  A LEU   A 123 ? 0.1503 0.1552 0.1381 -0.0247 0.0183  0.0368  123 LEU   A CA  
2652 C  CA  B LEU   A 123 ? 0.1479 0.1607 0.1508 -0.0224 0.0041  0.0229  123 LEU   A CA  
2653 C  C   A LEU   A 123 ? 0.1415 0.1381 0.1277 -0.0206 0.0176  0.0347  123 LEU   A C   
2654 C  C   B LEU   A 123 ? 0.1446 0.1495 0.1475 -0.0171 0.0060  0.0151  123 LEU   A C   
2655 O  O   A LEU   A 123 ? 0.1270 0.1272 0.1345 -0.0207 0.0166  0.0329  123 LEU   A O   
2656 O  O   B LEU   A 123 ? 0.1393 0.1519 0.1578 -0.0113 0.0026  0.0071  123 LEU   A O   
2657 C  CB  A LEU   A 123 ? 0.1636 0.1686 0.1392 -0.0294 0.0305  0.0348  123 LEU   A CB  
2658 C  CB  B LEU   A 123 ? 0.1553 0.1716 0.1532 -0.0261 0.0071  0.0236  123 LEU   A CB  
2659 C  CG  A LEU   A 123 ? 0.1724 0.1794 0.1564 -0.0228 0.0286  0.0232  123 LEU   A CG  
2660 C  CG  B LEU   A 123 ? 0.1576 0.1783 0.1556 -0.0242 0.0074  0.0249  123 LEU   A CG  
2661 C  CD1 A LEU   A 123 ? 0.1749 0.1839 0.1735 -0.0117 0.0188  0.0121  123 LEU   A CD1 
2662 C  CD1 B LEU   A 123 ? 0.1612 0.1810 0.1799 -0.0134 0.0009  0.0190  123 LEU   A CD1 
2663 C  CD2 A LEU   A 123 ? 0.1827 0.1906 0.1631 -0.0177 0.0214  0.0146  123 LEU   A CD2 
2664 C  CD2 B LEU   A 123 ? 0.1657 0.1880 0.1512 -0.0187 0.0024  0.0199  123 LEU   A CD2 
2687 N  N   A ALA   A 124 ? 0.1379 0.1322 0.1213 -0.0170 0.0173  0.0295  124 ALA   A N   
2688 N  N   B ALA   A 124 ? 0.1462 0.1369 0.1499 -0.0189 0.0034  0.0107  124 ALA   A N   
2689 C  CA  A ALA   A 124 ? 0.1217 0.1336 0.1244 -0.0010 0.0065  0.0211  124 ALA   A CA  
2690 C  CA  B ALA   A 124 ? 0.1391 0.1328 0.1603 -0.0215 0.0022  0.0185  124 ALA   A CA  
2691 C  C   A ALA   A 124 ? 0.1185 0.1292 0.1348 -0.0059 0.0105  0.0175  124 ALA   A C   
2692 C  C   B ALA   A 124 ? 0.1318 0.1248 0.1515 -0.0166 0.0115  0.0199  124 ALA   A C   
2693 O  O   A ALA   A 124 ? 0.1223 0.1348 0.1480 -0.0069 0.0171  0.0217  124 ALA   A O   
2694 O  O   B ALA   A 124 ? 0.1329 0.1222 0.1682 -0.0073 0.0257  0.0157  124 ALA   A O   
2695 C  CB  A ALA   A 124 ? 0.1119 0.1351 0.1396 0.0051  -0.0011 0.0191  124 ALA   A CB  
2696 C  CB  B ALA   A 124 ? 0.1490 0.1334 0.1869 -0.0277 0.0042  0.0214  124 ALA   A CB  
2707 N  N   A PRO   A 125 ? 0.1182 0.1377 0.1561 -0.0017 0.0153  0.0280  125 PRO   A N   
2708 N  N   B PRO   A 125 ? 0.1211 0.1240 0.1326 -0.0070 0.0043  0.0319  125 PRO   A N   
2709 C  CA  A PRO   A 125 ? 0.1266 0.1450 0.1684 -0.0035 0.0043  0.0221  125 PRO   A CA  
2710 C  CA  B PRO   A 125 ? 0.1261 0.1336 0.1374 -0.0149 0.0101  0.0264  125 PRO   A CA  
2711 C  C   A PRO   A 125 ? 0.1191 0.1467 0.1588 -0.0114 0.0039  0.0229  125 PRO   A C   
2712 C  C   B PRO   A 125 ? 0.1298 0.1465 0.1512 -0.0164 0.0050  0.0188  125 PRO   A C   
2713 O  O   A PRO   A 125 ? 0.1253 0.1443 0.1679 -0.0064 -0.0053 0.0195  125 PRO   A O   
2714 O  O   B PRO   A 125 ? 0.1345 0.1450 0.1658 -0.0080 -0.0001 0.0150  125 PRO   A O   
2715 C  CB  A PRO   A 125 ? 0.1320 0.1465 0.1660 -0.0042 0.0025  0.0164  125 PRO   A CB  
2716 C  CB  B PRO   A 125 ? 0.1186 0.1271 0.1261 -0.0163 0.0090  0.0271  125 PRO   A CB  
2717 C  CG  A PRO   A 125 ? 0.1420 0.1440 0.1771 0.0006  0.0041  0.0223  125 PRO   A CG  
2718 C  CG  B PRO   A 125 ? 0.1075 0.1195 0.1311 -0.0044 0.0110  0.0194  125 PRO   A CG  
2719 C  CD  A PRO   A 125 ? 0.1279 0.1394 0.1694 0.0024  0.0153  0.0151  125 PRO   A CD  
2720 C  CD  B PRO   A 125 ? 0.1124 0.1125 0.1359 -0.0087 0.0087  0.0250  125 PRO   A CD  
2735 N  N   A LEU   A 126 ? 0.1199 0.1490 0.1531 -0.0049 0.0055  0.0268  126 LEU   A N   
2736 N  N   B LEU   A 126 ? 0.1388 0.1586 0.1639 -0.0093 -0.0032 0.0152  126 LEU   A N   
2737 C  CA  A LEU   A 126 ? 0.1255 0.1447 0.1604 -0.0029 0.0035  0.0269  126 LEU   A CA  
2738 C  CA  B LEU   A 126 ? 0.1405 0.1535 0.1807 -0.0098 -0.0092 0.0254  126 LEU   A CA  
2739 C  C   A LEU   A 126 ? 0.1409 0.1437 0.1661 0.0086  -0.0004 0.0233  126 LEU   A C   
2740 C  C   B LEU   A 126 ? 0.1460 0.1424 0.1720 0.0033  -0.0035 0.0197  126 LEU   A C   
2741 O  O   A LEU   A 126 ? 0.1486 0.1505 0.1875 0.0160  0.0217  0.0253  126 LEU   A O   
2742 O  O   B LEU   A 126 ? 0.1549 0.1449 0.1804 0.0095  -0.0001 0.0261  126 LEU   A O   
2743 C  CB  A LEU   A 126 ? 0.1268 0.1408 0.1750 -0.0033 -0.0042 0.0262  126 LEU   A CB  
2744 C  CB  B LEU   A 126 ? 0.1510 0.1663 0.2191 -0.0137 -0.0145 0.0345  126 LEU   A CB  
2745 C  CG  A LEU   A 126 ? 0.1243 0.1634 0.2006 -0.0018 0.0044  0.0376  126 LEU   A CG  
2746 C  CG  B LEU   A 126 ? 0.1584 0.1768 0.2641 -0.0130 -0.0201 0.0486  126 LEU   A CG  
2747 C  CD1 A LEU   A 126 ? 0.1261 0.1754 0.2146 -0.0047 0.0067  0.0455  126 LEU   A CD1 
2748 C  CD1 B LEU   A 126 ? 0.1594 0.1803 0.2798 -0.0142 -0.0310 0.0512  126 LEU   A CD1 
2749 C  CD2 A LEU   A 126 ? 0.1338 0.1546 0.1993 -0.0139 0.0145  0.0589  126 LEU   A CD2 
2750 C  CD2 B LEU   A 126 ? 0.1623 0.1808 0.2800 -0.0151 -0.0246 0.0512  126 LEU   A CD2 
2773 N  N   A LEU   A 127 ? 0.1451 0.1394 0.1658 0.0092  -0.0031 0.0133  127 LEU   A N   
2774 N  N   B LEU   A 127 ? 0.1413 0.1356 0.1675 0.0018  0.0045  0.0232  127 LEU   A N   
2775 C  CA  A LEU   A 127 ? 0.1496 0.1342 0.1528 0.0038  -0.0080 0.0038  127 LEU   A CA  
2776 C  CA  B LEU   A 127 ? 0.1367 0.1434 0.1634 0.0012  -0.0031 0.0284  127 LEU   A CA  
2777 C  C   A LEU   A 127 ? 0.1443 0.1314 0.1365 0.0012  -0.0066 0.0023  127 LEU   A C   
2778 C  C   B LEU   A 127 ? 0.1354 0.1409 0.1567 -0.0015 -0.0039 0.0184  127 LEU   A C   
2779 O  O   A LEU   A 127 ? 0.1490 0.1328 0.1408 -0.0092 -0.0077 0.0126  127 LEU   A O   
2780 O  O   B LEU   A 127 ? 0.1456 0.1441 0.1702 -0.0057 0.0061  0.0193  127 LEU   A O   
2781 C  CB  A LEU   A 127 ? 0.1546 0.1359 0.1431 0.0038  -0.0041 0.0055  127 LEU   A CB  
2782 C  CB  B LEU   A 127 ? 0.1367 0.1595 0.1618 0.0072  0.0008  0.0240  127 LEU   A CB  
2783 C  CG  A LEU   A 127 ? 0.1562 0.1251 0.1383 0.0067  -0.0083 0.0120  127 LEU   A CG  
2784 C  CG  B LEU   A 127 ? 0.1358 0.1735 0.1651 0.0113  -0.0030 0.0270  127 LEU   A CG  
2785 C  CD1 A LEU   A 127 ? 0.1575 0.1143 0.1463 -0.0002 -0.0130 0.0025  127 LEU   A CD1 
2786 C  CD1 B LEU   A 127 ? 0.1341 0.1799 0.1876 0.0233  0.0070  0.0297  127 LEU   A CD1 
2787 C  CD2 A LEU   A 127 ? 0.1661 0.1142 0.1583 0.0101  -0.0157 0.0205  127 LEU   A CD2 
2788 C  CD2 B LEU   A 127 ? 0.1542 0.1897 0.1673 0.0076  -0.0188 0.0139  127 LEU   A CD2 
2811 N  N   A SER   A 128 ? 0.1514 0.1353 0.1351 -0.0012 -0.0021 0.0113  128 SER   A N   
2812 N  N   B SER   A 128 ? 0.1407 0.1362 0.1545 -0.0075 -0.0087 0.0184  128 SER   A N   
2813 C  CA  A SER   A 128 ? 0.1617 0.1427 0.1400 0.0027  0.0008  0.0158  128 SER   A CA  
2814 C  CA  B SER   A 128 ? 0.1430 0.1334 0.1446 -0.0054 -0.0121 0.0146  128 SER   A CA  
2815 C  C   A SER   A 128 ? 0.1669 0.1499 0.1451 0.0085  0.0071  0.0287  128 SER   A C   
2816 C  C   B SER   A 128 ? 0.1436 0.1316 0.1438 -0.0027 -0.0234 0.0267  128 SER   A C   
2817 O  O   A SER   A 128 ? 0.1783 0.1661 0.1637 0.0064  0.0123  0.0215  128 SER   A O   
2818 O  O   B SER   A 128 ? 0.1388 0.1374 0.1576 -0.0110 -0.0239 0.0178  128 SER   A O   
2819 C  CB  A SER   A 128 ? 0.1595 0.1497 0.1419 -0.0016 0.0030  0.0219  128 SER   A CB  
2820 C  CB  B SER   A 128 ? 0.1399 0.1448 0.1406 -0.0056 -0.0103 0.0186  128 SER   A CB  
2821 O  OG  A SER   A 128 ? 0.1616 0.1569 0.1501 -0.0004 0.0028  0.0118  128 SER   A OG  
2822 O  OG  B SER   A 128 ? 0.1390 0.1550 0.1477 -0.0084 -0.0043 0.0185  128 SER   A OG  
2833 N  N   A ALA   A 129 ? 0.1615 0.1558 0.1622 0.0023  0.0071  0.0280  129 ALA   A N   
2834 N  N   B ALA   A 129 ? 0.1442 0.1392 0.1505 -0.0040 -0.0305 0.0225  129 ALA   A N   
2835 C  CA  A ALA   A 129 ? 0.1538 0.1563 0.1677 0.0027  0.0041  0.0223  129 ALA   A CA  
2836 C  CA  B ALA   A 129 ? 0.1491 0.1490 0.1661 -0.0014 -0.0281 0.0146  129 ALA   A CA  
2837 C  C   A ALA   A 129 ? 0.1537 0.1461 0.1762 -0.0062 0.0007  0.0044  129 ALA   A C   
2838 C  C   B ALA   A 129 ? 0.1524 0.1486 0.1454 0.0066  -0.0332 0.0002  129 ALA   A C   
2839 O  O   A ALA   A 129 ? 0.1569 0.1499 0.1730 -0.0153 0.0043  0.0055  129 ALA   A O   
2840 O  O   B ALA   A 129 ? 0.1551 0.1569 0.1450 0.0019  -0.0356 0.0106  129 ALA   A O   
2841 C  CB  A ALA   A 129 ? 0.1513 0.1659 0.1692 0.0168  -0.0006 0.0272  129 ALA   A CB  
2842 C  CB  B ALA   A 129 ? 0.1539 0.1618 0.1755 -0.0051 -0.0283 0.0109  129 ALA   A CB  
2853 N  N   A GLY   A 130 ? 0.1588 0.1427 0.2065 -0.0126 0.0045  -0.0129 130 GLY   A N   
2854 N  N   B GLY   A 130 ? 0.1588 0.1480 0.1478 0.0070  -0.0291 -0.0044 130 GLY   A N   
2855 C  CA  A GLY   A 130 ? 0.1801 0.1460 0.2084 -0.0064 0.0026  -0.0135 130 GLY   A CA  
2856 C  CA  B GLY   A 130 ? 0.1792 0.1501 0.1586 0.0110  -0.0348 -0.0060 130 GLY   A CA  
2857 C  C   A GLY   A 130 ? 0.1876 0.1408 0.2041 -0.0083 0.0002  -0.0074 130 GLY   A C   
2858 C  C   B GLY   A 130 ? 0.1869 0.1434 0.1717 0.0180  -0.0375 -0.0000 130 GLY   A C   
2859 O  O   A GLY   A 130 ? 0.1902 0.1415 0.2008 -0.0125 0.0064  -0.0101 130 GLY   A O   
2860 O  O   B GLY   A 130 ? 0.1916 0.1374 0.1733 0.0222  -0.0428 -0.0000 130 GLY   A O   
2867 N  N   A ILE   A 131 ? 0.1961 0.1414 0.1933 -0.0196 -0.0140 0.0077  131 ILE   A N   
2868 N  N   B ILE   A 131 ? 0.1945 0.1471 0.1791 0.0106  -0.0316 0.0061  131 ILE   A N   
2869 C  CA  A ILE   A 131 ? 0.2013 0.1413 0.1714 -0.0254 -0.0294 0.0117  131 ILE   A CA  
2870 C  CA  B ILE   A 131 ? 0.2065 0.1475 0.1764 0.0082  -0.0365 0.0069  131 ILE   A CA  
2871 C  C   A ILE   A 131 ? 0.1881 0.1473 0.1523 -0.0239 -0.0284 0.0201  131 ILE   A C   
2872 C  C   B ILE   A 131 ? 0.1998 0.1541 0.1620 0.0067  -0.0374 0.0158  131 ILE   A C   
2873 O  O   A ILE   A 131 ? 0.1957 0.1523 0.1781 -0.0254 -0.0238 0.0184  131 ILE   A O   
2874 O  O   B ILE   A 131 ? 0.2015 0.1586 0.1844 0.0073  -0.0348 0.0197  131 ILE   A O   
2875 C  CB  A ILE   A 131 ? 0.2236 0.1521 0.1677 -0.0317 -0.0357 0.0087  131 ILE   A CB  
2876 C  CB  B ILE   A 131 ? 0.2287 0.1588 0.1879 0.0015  -0.0335 -0.0006 131 ILE   A CB  
2877 C  CG1 A ILE   A 131 ? 0.2302 0.1670 0.1710 -0.0420 -0.0391 0.0147  131 ILE   A CG1 
2878 C  CG1 B ILE   A 131 ? 0.2376 0.1712 0.1878 0.0003  -0.0442 0.0043  131 ILE   A CG1 
2879 C  CG2 A ILE   A 131 ? 0.2329 0.1430 0.1771 -0.0238 -0.0417 0.0039  131 ILE   A CG2 
2880 C  CG2 B ILE   A 131 ? 0.2378 0.1599 0.2048 0.0011  -0.0306 -0.0129 131 ILE   A CG2 
2881 C  CD1 A ILE   A 131 ? 0.2313 0.1724 0.1855 -0.0484 -0.0424 0.0186  131 ILE   A CD1 
2882 C  CD1 B ILE   A 131 ? 0.2462 0.1784 0.2021 -0.0055 -0.0446 0.0048  131 ILE   A CD1 
2905 N  N   A PHE   A 132 ? 0.1746 0.1470 0.1502 -0.0144 -0.0284 0.0221  132 PHE   A N   
2906 N  N   B PHE   A 132 ? 0.1935 0.1537 0.1634 0.0086  -0.0365 0.0170  132 PHE   A N   
2907 C  CA  A PHE   A 132 ? 0.1780 0.1569 0.1370 -0.0121 -0.0157 0.0168  132 PHE   A CA  
2908 C  CA  B PHE   A 132 ? 0.1987 0.1631 0.1623 0.0051  -0.0287 0.0071  132 PHE   A CA  
2909 C  C   A PHE   A 132 ? 0.1791 0.1701 0.1282 -0.0129 -0.0085 0.0164  132 PHE   A C   
2910 C  C   B PHE   A 132 ? 0.2049 0.1720 0.1804 0.0024  -0.0344 0.0107  132 PHE   A C   
2911 O  O   A PHE   A 132 ? 0.1770 0.1808 0.1253 -0.0192 -0.0104 0.0071  132 PHE   A O   
2912 O  O   B PHE   A 132 ? 0.2181 0.1876 0.2035 -0.0057 -0.0284 0.0092  132 PHE   A O   
2913 C  CB  A PHE   A 132 ? 0.1742 0.1494 0.1469 -0.0071 -0.0200 0.0250  132 PHE   A CB  
2914 C  CB  B PHE   A 132 ? 0.1943 0.1584 0.1511 0.0100  -0.0206 0.0019  132 PHE   A CB  
2915 C  CG  A PHE   A 132 ? 0.1782 0.1481 0.1575 0.0026  -0.0240 0.0251  132 PHE   A CG  
2916 C  CG  B PHE   A 132 ? 0.1919 0.1599 0.1411 0.0148  -0.0145 -0.0031 132 PHE   A CG  
2917 C  CD1 A PHE   A 132 ? 0.1765 0.1585 0.1619 0.0055  -0.0226 0.0055  132 PHE   A CD1 
2918 C  CD1 B PHE   A 132 ? 0.1861 0.1707 0.1440 0.0169  -0.0125 -0.0106 132 PHE   A CD1 
2919 C  CD2 A PHE   A 132 ? 0.1790 0.1581 0.1679 0.0110  -0.0307 0.0219  132 PHE   A CD2 
2920 C  CD2 B PHE   A 132 ? 0.1926 0.1646 0.1332 0.0176  -0.0127 -0.0235 132 PHE   A CD2 
2921 C  CE1 A PHE   A 132 ? 0.1757 0.1625 0.1547 0.0087  -0.0254 -0.0041 132 PHE   A CE1 
2922 C  CE1 B PHE   A 132 ? 0.1837 0.1737 0.1295 0.0193  -0.0105 -0.0140 132 PHE   A CE1 
2923 C  CE2 A PHE   A 132 ? 0.1777 0.1670 0.1715 0.0167  -0.0322 0.0116  132 PHE   A CE2 
2924 C  CE2 B PHE   A 132 ? 0.1903 0.1750 0.1438 0.0237  -0.0112 -0.0191 132 PHE   A CE2 
2925 C  CZ  A PHE   A 132 ? 0.1746 0.1689 0.1619 0.0101  -0.0313 0.0020  132 PHE   A CZ  
2926 C  CZ  B PHE   A 132 ? 0.1853 0.1760 0.1301 0.0181  -0.0100 -0.0091 132 PHE   A CZ  
2945 N  N   A GLY   A 133 ? 0.1818 0.1699 0.1235 -0.0086 -0.0132 0.0149  133 GLY   A N   
2946 N  N   B GLY   A 133 ? 0.2002 0.1669 0.1725 0.0057  -0.0429 0.0084  133 GLY   A N   
2947 C  CA  A GLY   A 133 ? 0.1868 0.1821 0.1269 -0.0068 -0.0162 0.0054  133 GLY   A CA  
2948 C  CA  B GLY   A 133 ? 0.1977 0.1757 0.1684 0.0053  -0.0455 -0.0004 133 GLY   A CA  
2949 C  C   A GLY   A 133 ? 0.1920 0.1913 0.1396 -0.0123 -0.0310 0.0011  133 GLY   A C   
2950 C  C   B GLY   A 133 ? 0.1904 0.1854 0.1678 0.0045  -0.0565 -0.0093 133 GLY   A C   
2951 O  O   A GLY   A 133 ? 0.1979 0.2011 0.1653 -0.0096 -0.0346 -0.0086 133 GLY   A O   
2952 O  O   B GLY   A 133 ? 0.1819 0.1993 0.1812 0.0044  -0.0534 -0.0226 133 GLY   A O   
2959 N  N   A ALA   A 134 ? 0.1876 0.1801 0.1389 -0.0223 -0.0208 0.0063  134 ALA   A N   
2960 N  N   B ALA   A 134 ? 0.1871 0.1716 0.1745 0.0032  -0.0395 -0.0019 134 ALA   A N   
2961 C  CA  A ALA   A 134 ? 0.1869 0.1849 0.1726 -0.0259 -0.0256 0.0012  134 ALA   A CA  
2962 C  CA  B ALA   A 134 ? 0.1886 0.1695 0.1975 -0.0012 -0.0343 0.0021  134 ALA   A CA  
2963 C  C   A ALA   A 134 ? 0.1866 0.2004 0.1874 -0.0298 -0.0284 0.0139  134 ALA   A C   
2964 C  C   B ALA   A 134 ? 0.1903 0.1744 0.2080 -0.0092 -0.0286 0.0207  134 ALA   A C   
2965 O  O   A ALA   A 134 ? 0.1923 0.2019 0.2014 -0.0305 -0.0059 0.0178  134 ALA   A O   
2966 O  O   B ALA   A 134 ? 0.1941 0.1710 0.2339 -0.0170 -0.0135 0.0217  134 ALA   A O   
2967 C  CB  A ALA   A 134 ? 0.1953 0.1826 0.1938 -0.0231 -0.0204 -0.0059 134 ALA   A CB  
2968 C  CB  B ALA   A 134 ? 0.1964 0.1661 0.2181 0.0025  -0.0274 -0.0126 134 ALA   A CB  
2979 N  N   A ASP   A 135 ? 0.1902 0.2111 0.2113 -0.0334 -0.0386 0.0277  135 ASP   A N   
2980 N  N   B ASP   A 135 ? 0.1979 0.1860 0.2311 -0.0125 -0.0343 0.0310  135 ASP   A N   
2981 C  CA  A ASP   A 135 ? 0.1863 0.2195 0.2427 -0.0404 -0.0524 0.0511  135 ASP   A CA  
2982 C  CA  B ASP   A 135 ? 0.1972 0.1951 0.2680 -0.0179 -0.0432 0.0457  135 ASP   A CA  
2983 C  C   A ASP   A 135 ? 0.1761 0.2115 0.2502 -0.0247 -0.0429 0.0689  135 ASP   A C   
2984 C  C   B ASP   A 135 ? 0.1837 0.1855 0.2667 -0.0146 -0.0412 0.0518  135 ASP   A C   
2985 O  O   A ASP   A 135 ? 0.1738 0.2063 0.2553 -0.0213 -0.0435 0.0654  135 ASP   A O   
2986 O  O   B ASP   A 135 ? 0.1806 0.1742 0.2656 -0.0137 -0.0399 0.0557  135 ASP   A O   
2987 C  CB  A ASP   A 135 ? 0.1981 0.2423 0.2748 -0.0549 -0.0726 0.0466  135 ASP   A CB  
2988 C  CB  B ASP   A 135 ? 0.2140 0.2198 0.3166 -0.0212 -0.0494 0.0506  135 ASP   A CB  
2989 C  CG  A ASP   A 135 ? 0.2095 0.2672 0.3039 -0.0666 -0.0814 0.0429  135 ASP   A CG  
2990 C  CG  B ASP   A 135 ? 0.2228 0.2424 0.3600 -0.0187 -0.0500 0.0579  135 ASP   A CG  
2991 O  OD1 A ASP   A 135 ? 0.2079 0.2776 0.3035 -0.0662 -0.0847 0.0476  135 ASP   A OD1 
2992 O  OD1 B ASP   A 135 ? 0.2156 0.2425 0.3690 -0.0133 -0.0640 0.0699  135 ASP   A OD1 
2993 O  OD2 A ASP   A 135 ? 0.2217 0.2816 0.3380 -0.0719 -0.0773 0.0392  135 ASP   A OD2 
2994 O  OD2 B ASP   A 135 ? 0.2343 0.2561 0.3920 -0.0175 -0.0434 0.0565  135 ASP   A OD2 
3003 N  N   A PRO   A 136 ? 0.1659 0.2058 0.2576 -0.0080 -0.0259 0.0885  136 PRO   A N   
3004 N  N   B PRO   A 136 ? 0.1737 0.1837 0.2738 -0.0084 -0.0339 0.0546  136 PRO   A N   
3005 C  CA  A PRO   A 136 ? 0.1567 0.2007 0.2696 -0.0025 -0.0116 0.0820  136 PRO   A CA  
3006 C  CA  B PRO   A 136 ? 0.1682 0.1876 0.2758 -0.0115 -0.0216 0.0419  136 PRO   A CA  
3007 C  C   A PRO   A 136 ? 0.1323 0.1927 0.2671 0.0019  -0.0030 0.0785  136 PRO   A C   
3008 C  C   B PRO   A 136 ? 0.1527 0.1904 0.2628 -0.0105 -0.0203 0.0287  136 PRO   A C   
3009 O  O   A PRO   A 136 ? 0.1234 0.1843 0.2667 -0.0013 0.0003  0.0800  136 PRO   A O   
3010 O  O   B PRO   A 136 ? 0.1520 0.1823 0.2452 -0.0099 -0.0172 0.0201  136 PRO   A O   
3011 C  CB  A PRO   A 136 ? 0.1727 0.2023 0.2866 -0.0030 -0.0089 0.0825  136 PRO   A CB  
3012 C  CB  B PRO   A 136 ? 0.1820 0.1864 0.2897 -0.0069 -0.0230 0.0426  136 PRO   A CB  
3013 C  CG  A PRO   A 136 ? 0.1850 0.2112 0.2928 -0.0038 -0.0096 0.0816  136 PRO   A CG  
3014 C  CG  B PRO   A 136 ? 0.1954 0.1902 0.3031 -0.0013 -0.0258 0.0434  136 PRO   A CG  
3015 C  CD  A PRO   A 136 ? 0.1756 0.2078 0.2686 -0.0018 -0.0128 0.0985  136 PRO   A CD  
3016 C  CD  B PRO   A 136 ? 0.1807 0.1852 0.2942 -0.0030 -0.0250 0.0561  136 PRO   A CD  
3031 N  N   A ILE   A 137 ? 0.1331 0.1949 0.2661 -0.0020 -0.0130 0.0831  137 ILE   A N   
3032 N  N   B ILE   A 137 ? 0.1541 0.1938 0.2744 -0.0213 -0.0262 0.0298  137 ILE   A N   
3033 C  CA  A ILE   A 137 ? 0.1333 0.2019 0.2677 -0.0109 -0.0253 0.0721  137 ILE   A CA  
3034 C  CA  B ILE   A 137 ? 0.1557 0.2100 0.2744 -0.0219 -0.0332 0.0302  137 ILE   A CA  
3035 C  C   A ILE   A 137 ? 0.1386 0.1982 0.2505 -0.0145 -0.0346 0.0590  137 ILE   A C   
3036 C  C   B ILE   A 137 ? 0.1584 0.2159 0.2686 -0.0256 -0.0261 0.0304  137 ILE   A C   
3037 O  O   A ILE   A 137 ? 0.1355 0.1871 0.2522 -0.0145 -0.0212 0.0447  137 ILE   A O   
3038 O  O   B ILE   A 137 ? 0.1562 0.2175 0.2787 -0.0252 -0.0162 0.0290  137 ILE   A O   
3039 C  CB  A ILE   A 137 ? 0.1360 0.2148 0.2914 -0.0147 -0.0310 0.0758  137 ILE   A CB  
3040 C  CB  B ILE   A 137 ? 0.1668 0.2203 0.2966 -0.0178 -0.0456 0.0329  137 ILE   A CB  
3041 C  CG1 A ILE   A 137 ? 0.1420 0.2264 0.3077 -0.0138 -0.0212 0.0824  137 ILE   A CG1 
3042 C  CG1 B ILE   A 137 ? 0.1797 0.2339 0.3167 -0.0097 -0.0530 0.0467  137 ILE   A CG1 
3043 C  CG2 A ILE   A 137 ? 0.1415 0.2163 0.3007 -0.0156 -0.0380 0.0677  137 ILE   A CG2 
3044 C  CG2 B ILE   A 137 ? 0.1716 0.2189 0.3041 -0.0160 -0.0483 0.0254  137 ILE   A CG2 
3045 C  CD1 A ILE   A 137 ? 0.1561 0.2333 0.3226 -0.0085 -0.0100 0.0833  137 ILE   A CD1 
3046 C  CD1 B ILE   A 137 ? 0.1944 0.2406 0.3343 -0.0093 -0.0467 0.0568  137 ILE   A CD1 
3069 N  N   A HIS   A 138 ? 0.1403 0.2108 0.2374 -0.0063 -0.0292 0.0543  138 HIS   A N   
3070 N  N   B HIS   A 138 ? 0.1581 0.2288 0.2557 -0.0198 -0.0125 0.0263  138 HIS   A N   
3071 C  CA  A HIS   A 138 ? 0.1481 0.2146 0.2218 -0.0120 -0.0251 0.0458  138 HIS   A CA  
3072 C  CA  B HIS   A 138 ? 0.1587 0.2265 0.2356 -0.0226 -0.0093 0.0289  138 HIS   A CA  
3073 C  C   A HIS   A 138 ? 0.1392 0.2071 0.2105 -0.0128 -0.0172 0.0469  138 HIS   A C   
3074 C  C   B HIS   A 138 ? 0.1441 0.2133 0.2195 -0.0195 -0.0051 0.0401  138 HIS   A C   
3075 O  O   A HIS   A 138 ? 0.1498 0.2086 0.2049 -0.0079 -0.0136 0.0430  138 HIS   A O   
3076 O  O   B HIS   A 138 ? 0.1538 0.2167 0.2203 -0.0174 -0.0011 0.0370  138 HIS   A O   
3077 C  CB  A HIS   A 138 ? 0.1716 0.2277 0.2187 -0.0175 -0.0257 0.0359  138 HIS   A CB  
3078 C  CB  B HIS   A 138 ? 0.1721 0.2367 0.2292 -0.0259 -0.0095 0.0177  138 HIS   A CB  
3079 C  CG  A HIS   A 138 ? 0.1917 0.2373 0.2215 -0.0227 -0.0257 0.0273  138 HIS   A CG  
3080 C  CG  B HIS   A 138 ? 0.1859 0.2445 0.2299 -0.0309 -0.0166 0.0065  138 HIS   A CG  
3081 N  ND1 A HIS   A 138 ? 0.2022 0.2466 0.2418 -0.0238 -0.0213 0.0172  138 HIS   A ND1 
3082 N  ND1 B HIS   A 138 ? 0.1946 0.2532 0.2516 -0.0316 -0.0161 -0.0025 138 HIS   A ND1 
3083 C  CD2 A HIS   A 138 ? 0.1977 0.2458 0.2250 -0.0212 -0.0216 0.0248  138 HIS   A CD2 
3084 C  CD2 B HIS   A 138 ? 0.1877 0.2498 0.2287 -0.0292 -0.0156 0.0037  138 HIS   A CD2 
3085 C  CE1 A HIS   A 138 ? 0.2063 0.2523 0.2429 -0.0194 -0.0232 0.0119  138 HIS   A CE1 
3086 C  CE1 B HIS   A 138 ? 0.1961 0.2562 0.2484 -0.0284 -0.0205 -0.0063 138 HIS   A CE1 
3087 N  NE2 A HIS   A 138 ? 0.2041 0.2523 0.2321 -0.0195 -0.0188 0.0164  138 HIS   A NE2 
3088 N  NE2 B HIS   A 138 ? 0.1925 0.2552 0.2370 -0.0285 -0.0152 -0.0036 138 HIS   A NE2 
3103 N  N   . SER   A 139 ? 0.1354 0.1996 0.2201 -0.0117 -0.0060 0.0493  139 SER   A N   
3104 C  CA  . SER   A 139 ? 0.1336 0.1895 0.2131 -0.0088 -0.0016 0.0528  139 SER   A CA  
3105 C  C   . SER   A 139 ? 0.1322 0.1693 0.2076 -0.0083 0.0046  0.0417  139 SER   A C   
3106 O  O   . SER   A 139 ? 0.1292 0.1677 0.2183 -0.0091 -0.0007 0.0438  139 SER   A O   
3107 C  CB  . SER   A 139 ? 0.1296 0.1855 0.2266 -0.0129 -0.0067 0.0533  139 SER   A CB  
3108 O  OG  . SER   A 139 ? 0.1349 0.1832 0.2154 -0.0162 -0.0127 0.0653  139 SER   A OG  
3115 N  N   A LEU   A 140 ? 0.1272 0.1718 0.2133 -0.0050 -0.0008 0.0395  140 LEU   A N   
3116 N  N   B LEU   A 140 ? 0.1324 0.1646 0.2010 -0.0123 0.0029  0.0490  140 LEU   A N   
3117 C  CA  A LEU   A 140 ? 0.1191 0.1608 0.2067 -0.0068 -0.0021 0.0304  140 LEU   A CA  
3118 C  CA  B LEU   A 140 ? 0.1265 0.1479 0.1915 -0.0184 0.0053  0.0378  140 LEU   A CA  
3119 C  C   A LEU   A 140 ? 0.1191 0.1676 0.1916 -0.0034 -0.0024 0.0184  140 LEU   A C   
3120 C  C   B LEU   A 140 ? 0.1231 0.1533 0.1806 -0.0196 0.0046  0.0272  140 LEU   A C   
3121 O  O   A LEU   A 140 ? 0.1165 0.1599 0.1848 0.0032  0.0016  0.0148  140 LEU   A O   
3122 O  O   B LEU   A 140 ? 0.1300 0.1523 0.1921 -0.0074 0.0055  0.0195  140 LEU   A O   
3123 C  CB  A LEU   A 140 ? 0.1244 0.1519 0.2227 -0.0072 -0.0061 0.0190  140 LEU   A CB  
3124 C  CB  B LEU   A 140 ? 0.1249 0.1438 0.1960 -0.0220 -0.0005 0.0302  140 LEU   A CB  
3125 C  CG  A LEU   A 140 ? 0.1286 0.1457 0.2299 -0.0146 0.0042  0.0099  140 LEU   A CG  
3126 C  CG  B LEU   A 140 ? 0.1241 0.1487 0.1967 -0.0208 0.0077  0.0349  140 LEU   A CG  
3127 C  CD1 A LEU   A 140 ? 0.1343 0.1520 0.2462 -0.0020 -0.0009 0.0041  140 LEU   A CD1 
3128 C  CD1 B LEU   A 140 ? 0.1271 0.1487 0.1979 -0.0179 0.0100  0.0299  140 LEU   A CD1 
3129 C  CD2 A LEU   A 140 ? 0.1398 0.1427 0.2337 -0.0147 0.0145  0.0103  140 LEU   A CD2 
3130 C  CD2 B LEU   A 140 ? 0.1253 0.1530 0.2053 -0.0190 0.0111  0.0411  140 LEU   A CD2 
3153 N  N   A ARG   A 141 ? 0.1251 0.1761 0.1947 -0.0145 -0.0187 0.0120  141 ARG   A N   
3154 N  N   B ARG   A 141 ? 0.1256 0.1640 0.1872 -0.0278 -0.0066 0.0313  141 ARG   A N   
3155 C  CA  A ARG   A 141 ? 0.1432 0.1941 0.2027 -0.0263 -0.0198 -0.0025 141 ARG   A CA  
3156 C  CA  B ARG   A 141 ? 0.1338 0.1824 0.1865 -0.0359 -0.0098 0.0147  141 ARG   A CA  
3157 C  C   A ARG   A 141 ? 0.1439 0.1801 0.2017 -0.0224 -0.0155 0.0041  141 ARG   A C   
3158 C  C   B ARG   A 141 ? 0.1357 0.1702 0.1799 -0.0289 -0.0140 0.0176  141 ARG   A C   
3159 O  O   A ARG   A 141 ? 0.1405 0.1714 0.2016 -0.0236 -0.0117 -0.0143 141 ARG   A O   
3160 O  O   B ARG   A 141 ? 0.1308 0.1570 0.1655 -0.0352 -0.0070 0.0044  141 ARG   A O   
3161 C  CB  A ARG   A 141 ? 0.1593 0.2261 0.2155 -0.0312 -0.0210 -0.0109 141 ARG   A CB  
3162 C  CB  B ARG   A 141 ? 0.1431 0.2097 0.1834 -0.0406 0.0018  0.0076  141 ARG   A CB  
3163 C  CG  A ARG   A 141 ? 0.1872 0.2518 0.2474 -0.0332 -0.0296 -0.0114 141 ARG   A CG  
3164 C  CG  B ARG   A 141 ? 0.1661 0.2318 0.1910 -0.0398 0.0087  0.0026  141 ARG   A CG  
3165 C  CD  A ARG   A 141 ? 0.1980 0.2655 0.2651 -0.0447 -0.0319 -0.0080 141 ARG   A CD  
3166 C  CD  B ARG   A 141 ? 0.1805 0.2395 0.2169 -0.0409 0.0091  0.0092  141 ARG   A CD  
3167 N  NE  A ARG   A 141 ? 0.1970 0.2770 0.2862 -0.0534 -0.0274 -0.0030 141 ARG   A NE  
3168 N  NE  B ARG   A 141 ? 0.1908 0.2580 0.2217 -0.0336 0.0211  0.0172  141 ARG   A NE  
3169 C  CZ  A ARG   A 141 ? 0.1888 0.2924 0.2965 -0.0633 -0.0287 -0.0006 141 ARG   A CZ  
3170 C  CZ  B ARG   A 141 ? 0.1959 0.2659 0.2276 -0.0394 0.0266  0.0258  141 ARG   A CZ  
3171 N  NH1 A ARG   A 141 ? 0.1927 0.3040 0.3093 -0.0591 -0.0320 0.0009  141 ARG   A NH1 
3172 N  NH1 B ARG   A 141 ? 0.2009 0.2773 0.2240 -0.0431 0.0211  0.0171  141 ARG   A NH1 
3173 N  NH2 A ARG   A 141 ? 0.1803 0.2970 0.2954 -0.0662 -0.0289 -0.0021 141 ARG   A NH2 
3174 N  NH2 B ARG   A 141 ? 0.1987 0.2724 0.2485 -0.0326 0.0292  0.0274  141 ARG   A NH2 
3201 N  N   . VAL   A 142 ? 0.1369 0.1740 0.1987 -0.0197 -0.0074 0.0180  142 VAL   A N   
3202 C  CA  . VAL   A 142 ? 0.1402 0.1649 0.2033 -0.0172 0.0089  0.0135  142 VAL   A CA  
3203 C  C   . VAL   A 142 ? 0.1272 0.1571 0.2034 -0.0175 0.0024  0.0234  142 VAL   A C   
3204 O  O   . VAL   A 142 ? 0.1292 0.1619 0.2142 -0.0072 0.0040  0.0231  142 VAL   A O   
3205 C  CB  . VAL   A 142 ? 0.1496 0.1730 0.1988 -0.0157 0.0076  0.0200  142 VAL   A CB  
3206 C  CG1 . VAL   A 142 ? 0.1409 0.1651 0.1976 -0.0199 0.0101  0.0136  142 VAL   A CG1 
3207 C  CG2 . VAL   A 142 ? 0.1642 0.1911 0.2112 -0.0100 -0.0001 0.0277  142 VAL   A CG2 
3218 N  N   . CYS   A 143 ? 0.1277 0.1558 0.1953 -0.0151 -0.0020 0.0214  143 CYS   A N   
3219 C  CA  . CYS   A 143 ? 0.1272 0.1535 0.2021 -0.0126 0.0050  0.0300  143 CYS   A CA  
3220 C  C   . CYS   A 143 ? 0.1284 0.1519 0.2077 -0.0144 0.0082  0.0332  143 CYS   A C   
3221 O  O   . CYS   A 143 ? 0.1260 0.1539 0.2009 -0.0074 0.0040  0.0395  143 CYS   A O   
3222 C  CB  . CYS   A 143 ? 0.1439 0.1558 0.2048 -0.0069 0.0177  0.0372  143 CYS   A CB  
3223 S  SG  . CYS   A 143 ? 0.1555 0.1626 0.1968 0.0017  0.0138  0.0277  143 CYS   A SG  
3229 N  N   . VAL   A 144 ? 0.1281 0.1545 0.2140 -0.0156 0.0086  0.0375  144 VAL   A N   
3230 C  CA  . VAL   A 144 ? 0.1344 0.1656 0.2515 -0.0218 0.0156  0.0394  144 VAL   A CA  
3231 C  C   . VAL   A 144 ? 0.1382 0.1561 0.2524 -0.0262 -0.0127 0.0319  144 VAL   A C   
3232 O  O   . VAL   A 144 ? 0.1527 0.1635 0.2538 -0.0120 -0.0084 0.0377  144 VAL   A O   
3233 C  CB  . VAL   A 144 ? 0.1589 0.1862 0.3187 -0.0076 0.0331  0.0396  144 VAL   A CB  
3234 C  CG1 . VAL   A 144 ? 0.1695 0.2019 0.3590 -0.0097 0.0177  0.0359  144 VAL   A CG1 
3235 C  CG2 . VAL   A 144 ? 0.1434 0.1871 0.3281 -0.0114 0.0445  0.0495  144 VAL   A CG2 
3245 N  N   . ASP   A 145 ? 0.1403 0.1509 0.2605 -0.0220 -0.0033 0.0267  145 ASP   A N   
3246 C  CA  . ASP   A 145 ? 0.1494 0.1564 0.2635 -0.0254 -0.0096 0.0184  145 ASP   A CA  
3247 C  C   . ASP   A 145 ? 0.1500 0.1543 0.2543 -0.0184 -0.0003 0.0082  145 ASP   A C   
3248 O  O   . ASP   A 145 ? 0.1637 0.1616 0.3124 -0.0235 -0.0074 -0.0244 145 ASP   A O   
3249 C  CB  . ASP   A 145 ? 0.1651 0.1890 0.2787 -0.0307 -0.0192 0.0113  145 ASP   A CB  
3250 C  CG  . ASP   A 145 ? 0.1752 0.2311 0.3002 -0.0500 -0.0258 0.0203  145 ASP   A CG  
3251 O  OD1 . ASP   A 145 ? 0.1713 0.2455 0.3195 -0.0642 -0.0157 0.0265  145 ASP   A OD1 
3252 O  OD2 . ASP   A 145 ? 0.1967 0.2617 0.3030 -0.0573 -0.0412 0.0150  145 ASP   A OD2 
3257 N  N   . THR   A 146 ? 0.1364 0.1388 0.2215 -0.0179 0.0019  0.0167  146 THR   A N   
3258 C  CA  . THR   A 146 ? 0.1324 0.1383 0.2019 -0.0115 0.0032  0.0154  146 THR   A CA  
3259 C  C   . THR   A 146 ? 0.1237 0.1354 0.2115 -0.0047 0.0063  0.0207  146 THR   A C   
3260 O  O   . THR   A 146 ? 0.1415 0.1472 0.2168 -0.0010 0.0023  0.0138  146 THR   A O   
3261 C  CB  . THR   A 146 ? 0.1338 0.1429 0.2005 -0.0089 0.0044  0.0174  146 THR   A CB  
3262 O  OG1 . THR   A 146 ? 0.1311 0.1583 0.2089 -0.0025 0.0029  0.0112  146 THR   A OG1 
3263 C  CG2 . THR   A 146 ? 0.1356 0.1514 0.2214 -0.0152 0.0046  0.0144  146 THR   A CG2 
3271 N  N   . VAL   A 147 ? 0.1226 0.1376 0.2142 -0.0084 0.0091  0.0228  147 VAL   A N   
3272 C  CA  . VAL   A 147 ? 0.1271 0.1435 0.2019 -0.0126 0.0181  0.0266  147 VAL   A CA  
3273 C  C   . VAL   A 147 ? 0.1289 0.1393 0.2192 -0.0140 0.0182  0.0328  147 VAL   A C   
3274 O  O   . VAL   A 147 ? 0.1352 0.1383 0.2322 -0.0142 0.0096  0.0358  147 VAL   A O   
3275 C  CB  . VAL   A 147 ? 0.1403 0.1379 0.1955 -0.0115 0.0206  0.0303  147 VAL   A CB  
3276 C  CG1 . VAL   A 147 ? 0.1743 0.1549 0.1911 -0.0090 0.0155  0.0422  147 VAL   A CG1 
3277 C  CG2 . VAL   A 147 ? 0.1518 0.1368 0.1937 -0.0091 0.0062  0.0282  147 VAL   A CG2 
3287 N  N   . ARG   A 148 ? 0.1312 0.1455 0.2240 -0.0165 0.0140  0.0494  148 ARG   A N   
3288 C  CA  . ARG   A 148 ? 0.1378 0.1409 0.2179 -0.0135 0.0087  0.0472  148 ARG   A CA  
3289 C  C   . ARG   A 148 ? 0.1495 0.1489 0.2161 -0.0167 0.0111  0.0619  148 ARG   A C   
3290 O  O   . ARG   A 148 ? 0.1806 0.1642 0.2370 -0.0218 0.0161  0.0579  148 ARG   A O   
3291 C  CB  . ARG   A 148 ? 0.1427 0.1474 0.2290 -0.0068 0.0193  0.0421  148 ARG   A CB  
3292 C  CG  . ARG   A 148 ? 0.1611 0.1448 0.2583 -0.0082 0.0319  0.0273  148 ARG   A CG  
3293 C  CD  . ARG   A 148 ? 0.1743 0.1433 0.2814 -0.0105 0.0396  0.0498  148 ARG   A CD  
3294 N  NE  . ARG   A 148 ? 0.1673 0.1507 0.2887 -0.0000 0.0372  0.0519  148 ARG   A NE  
3295 C  CZ  . ARG   A 148 ? 0.1699 0.1326 0.2621 -0.0031 0.0438  0.0400  148 ARG   A CZ  
3296 N  NH1 . ARG   A 148 ? 0.1827 0.1377 0.2618 -0.0112 0.0374  0.0208  148 ARG   A NH1 
3297 N  NH2 . ARG   A 148 ? 0.1605 0.1571 0.2648 0.0117  0.0416  0.0417  148 ARG   A NH2 
3311 N  N   . THR   A 149 ? 0.1510 0.1589 0.2132 -0.0193 0.0008  0.0585  149 THR   A N   
3312 C  CA  . THR   A 149 ? 0.1547 0.1657 0.2108 -0.0179 0.0032  0.0559  149 THR   A CA  
3313 C  C   . THR   A 149 ? 0.1494 0.1624 0.1965 -0.0252 0.0062  0.0587  149 THR   A C   
3314 O  O   . THR   A 149 ? 0.1528 0.1696 0.2184 -0.0267 -0.0004 0.0484  149 THR   A O   
3315 C  CB  . THR   A 149 ? 0.1519 0.1695 0.2154 -0.0172 0.0059  0.0414  149 THR   A CB  
3316 O  OG1 . THR   A 149 ? 0.1612 0.1556 0.2208 -0.0261 0.0016  0.0391  149 THR   A OG1 
3317 C  CG2 . THR   A 149 ? 0.1502 0.1868 0.2177 -0.0081 -0.0033 0.0345  149 THR   A CG2 
3325 N  N   . ASN   A 150 ? 0.1536 0.1654 0.2023 -0.0154 -0.0033 0.0558  150 ASN   A N   
3326 C  CA  . ASN   A 150 ? 0.1623 0.1764 0.1964 -0.0176 0.0128  0.0507  150 ASN   A CA  
3327 C  C   . ASN   A 150 ? 0.1455 0.1639 0.1996 -0.0179 0.0057  0.0500  150 ASN   A C   
3328 O  O   . ASN   A 150 ? 0.1569 0.1778 0.2304 -0.0185 -0.0049 0.0400  150 ASN   A O   
3329 C  CB  . ASN   A 150 ? 0.2024 0.2037 0.2261 -0.0205 0.0318  0.0758  150 ASN   A CB  
3330 C  CG  . ASN   A 150 ? 0.2581 0.2355 0.2943 -0.0168 0.0132  0.0805  150 ASN   A CG  
3331 O  OD1 . ASN   A 150 ? 0.2830 0.2471 0.3078 -0.0224 0.0128  0.0938  150 ASN   A OD1 
3332 N  ND2 . ASN   A 150 ? 0.2880 0.2574 0.3347 -0.0103 0.0003  0.0748  150 ASN   A ND2 
3339 N  N   . VAL   A 151 ? 0.1497 0.1508 0.2030 -0.0199 0.0031  0.0518  151 VAL   A N   
3340 C  CA  . VAL   A 151 ? 0.1528 0.1555 0.1872 -0.0246 0.0079  0.0418  151 VAL   A CA  
3341 C  C   . VAL   A 151 ? 0.1443 0.1491 0.1932 -0.0291 0.0096  0.0497  151 VAL   A C   
3342 O  O   . VAL   A 151 ? 0.1517 0.1566 0.2347 -0.0258 0.0085  0.0444  151 VAL   A O   
3343 C  CB  . VAL   A 151 ? 0.1763 0.1743 0.1973 -0.0171 0.0098  0.0446  151 VAL   A CB  
3344 C  CG1 . VAL   A 151 ? 0.1701 0.1940 0.2328 -0.0194 0.0022  0.0368  151 VAL   A CG1 
3345 C  CG2 . VAL   A 151 ? 0.1898 0.1723 0.2008 -0.0117 0.0285  0.0348  151 VAL   A CG2 
3355 N  N   . TYR   A 152 ? 0.1427 0.1531 0.1960 -0.0254 0.0116  0.0452  152 TYR   A N   
3356 C  CA  . TYR   A 152 ? 0.1445 0.1577 0.1853 -0.0212 0.0167  0.0403  152 TYR   A CA  
3357 C  C   . TYR   A 152 ? 0.1429 0.1518 0.1796 -0.0247 0.0226  0.0368  152 TYR   A C   
3358 O  O   . TYR   A 152 ? 0.1509 0.1521 0.1859 -0.0269 0.0211  0.0346  152 TYR   A O   
3359 C  CB  . TYR   A 152 ? 0.1559 0.1637 0.1844 -0.0145 0.0222  0.0406  152 TYR   A CB  
3360 C  CG  . TYR   A 152 ? 0.1764 0.1860 0.1920 -0.0220 0.0302  0.0430  152 TYR   A CG  
3361 C  CD1 . TYR   A 152 ? 0.1866 0.2100 0.2098 -0.0115 0.0307  0.0560  152 TYR   A CD1 
3362 C  CD2 . TYR   A 152 ? 0.1814 0.1977 0.1833 -0.0377 0.0368  0.0431  152 TYR   A CD2 
3363 C  CE1 . TYR   A 152 ? 0.2145 0.2252 0.2200 -0.0089 0.0131  0.0710  152 TYR   A CE1 
3364 C  CE2 . TYR   A 152 ? 0.2078 0.2147 0.1987 -0.0380 0.0308  0.0492  152 TYR   A CE2 
3365 C  CZ  . TYR   A 152 ? 0.2305 0.2242 0.2055 -0.0250 0.0232  0.0737  152 TYR   A CZ  
3366 O  OH  . TYR   A 152 ? 0.2616 0.2424 0.2414 -0.0159 0.0209  0.0872  152 TYR   A OH  
3376 N  N   A LEU   A 153 ? 0.1341 0.1439 0.1844 -0.0236 0.0224  0.0384  153 LEU   A N   
3377 N  N   B LEU   A 153 ? 0.1433 0.1558 0.1801 -0.0248 0.0178  0.0366  153 LEU   A N   
3378 C  CA  A LEU   A 153 ? 0.1271 0.1369 0.1982 -0.0165 0.0121  0.0379  153 LEU   A CA  
3379 C  CA  B LEU   A 153 ? 0.1404 0.1534 0.1732 -0.0064 0.0125  0.0309  153 LEU   A CA  
3380 C  C   A LEU   A 153 ? 0.1315 0.1365 0.1968 -0.0227 0.0273  0.0271  153 LEU   A C   
3381 C  C   B LEU   A 153 ? 0.1426 0.1619 0.1640 0.0011  0.0164  0.0214  153 LEU   A C   
3382 O  O   A LEU   A 153 ? 0.1390 0.1418 0.2134 -0.0309 0.0375  0.0139  153 LEU   A O   
3383 O  O   B LEU   A 153 ? 0.1438 0.1708 0.1802 0.0022  0.0312  0.0185  153 LEU   A O   
3384 C  CB  A LEU   A 153 ? 0.1211 0.1298 0.2044 -0.0169 0.0094  0.0316  153 LEU   A CB  
3385 C  CB  B LEU   A 153 ? 0.1398 0.1477 0.1774 0.0015  0.0044  0.0310  153 LEU   A CB  
3386 C  CG  A LEU   A 153 ? 0.1223 0.1353 0.1988 -0.0212 0.0184  0.0185  153 LEU   A CG  
3387 C  CG  B LEU   A 153 ? 0.1457 0.1486 0.1696 0.0009  0.0100  0.0258  153 LEU   A CG  
3388 C  CD1 A LEU   A 153 ? 0.1267 0.1381 0.2082 -0.0136 0.0162  0.0127  153 LEU   A CD1 
3389 C  CD1 B LEU   A 153 ? 0.1486 0.1458 0.1802 0.0060  0.0072  0.0281  153 LEU   A CD1 
3390 C  CD2 A LEU   A 153 ? 0.1341 0.1474 0.1926 -0.0288 0.0258  -0.0001 153 LEU   A CD2 
3391 C  CD2 B LEU   A 153 ? 0.1566 0.1587 0.1783 -0.0010 0.0115  0.0123  153 LEU   A CD2 
3414 N  N   A ALA   A 154 ? 0.1268 0.1294 0.1908 -0.0225 0.0360  0.0258  154 ALA   A N   
3415 N  N   B ALA   A 154 ? 0.1437 0.1588 0.1576 0.0073  0.0217  0.0216  154 ALA   A N   
3416 C  CA  A ALA   A 154 ? 0.1375 0.1375 0.2070 -0.0202 0.0431  0.0252  154 ALA   A CA  
3417 C  CA  B ALA   A 154 ? 0.1510 0.1649 0.1853 0.0108  0.0216  0.0236  154 ALA   A CA  
3418 C  C   A ALA   A 154 ? 0.1440 0.1368 0.2183 -0.0127 0.0383  0.0364  154 ALA   A C   
3419 C  C   B ALA   A 154 ? 0.1560 0.1728 0.1954 0.0055  0.0095  0.0381  154 ALA   A C   
3420 O  O   A ALA   A 154 ? 0.1555 0.1448 0.2268 -0.0171 0.0339  0.0352  154 ALA   A O   
3421 O  O   B ALA   A 154 ? 0.1616 0.1724 0.1879 -0.0058 0.0047  0.0417  154 ALA   A O   
3422 C  CB  A ALA   A 154 ? 0.1536 0.1452 0.2063 -0.0094 0.0410  0.0128  154 ALA   A CB  
3423 C  CB  B ALA   A 154 ? 0.1558 0.1574 0.1877 0.0190  0.0115  0.0118  154 ALA   A CB  
3434 N  N   A VAL   A 155 ? 0.1457 0.1451 0.2342 -0.0080 0.0384  0.0546  155 VAL   A N   
3435 N  N   B VAL   A 155 ? 0.1627 0.1880 0.2194 0.0051  0.0063  0.0500  155 VAL   A N   
3436 C  CA  A VAL   A 155 ? 0.1471 0.1540 0.2491 -0.0033 0.0283  0.0729  155 VAL   A CA  
3437 C  CA  B VAL   A 155 ? 0.1710 0.2058 0.2479 0.0087  0.0013  0.0494  155 VAL   A CA  
3438 C  C   A VAL   A 155 ? 0.1421 0.1560 0.2667 0.0050  0.0152  0.0754  155 VAL   A C   
3439 C  C   B VAL   A 155 ? 0.1872 0.2220 0.2870 0.0167  0.0095  0.0460  155 VAL   A C   
3440 O  O   A VAL   A 155 ? 0.1368 0.1607 0.2742 0.0130  0.0087  0.0645  155 VAL   A O   
3441 O  O   B VAL   A 155 ? 0.1795 0.2160 0.3019 0.0159  0.0223  0.0482  155 VAL   A O   
3442 C  CB  A VAL   A 155 ? 0.1490 0.1678 0.2571 0.0089  0.0031  0.0679  155 VAL   A CB  
3443 C  CB  B VAL   A 155 ? 0.1629 0.2113 0.2427 0.0063  -0.0082 0.0448  155 VAL   A CB  
3444 C  CG1 A VAL   A 155 ? 0.1530 0.1816 0.2737 0.0142  -0.0070 0.0685  155 VAL   A CG1 
3445 C  CG1 B VAL   A 155 ? 0.1655 0.2197 0.2440 0.0133  -0.0116 0.0402  155 VAL   A CG1 
3446 C  CG2 A VAL   A 155 ? 0.1481 0.1770 0.2547 0.0184  -0.0052 0.0672  155 VAL   A CG2 
3447 C  CG2 B VAL   A 155 ? 0.1586 0.2124 0.2402 0.0009  -0.0193 0.0394  155 VAL   A CG2 
3466 N  N   A PHE   A 156 ? 0.1538 0.1587 0.2770 0.0047  0.0153  0.0840  156 PHE   A N   
3467 N  N   B PHE   A 156 ? 0.2181 0.2473 0.3133 0.0227  0.0071  0.0407  156 PHE   A N   
3468 C  CA  A PHE   A 156 ? 0.1724 0.1631 0.3034 0.0176  0.0144  0.0798  156 PHE   A CA  
3469 C  CA  B PHE   A 156 ? 0.2548 0.2733 0.3492 0.0293  0.0113  0.0316  156 PHE   A CA  
3470 C  C   A PHE   A 156 ? 0.1717 0.1700 0.3073 0.0366  0.0089  0.0817  156 PHE   A C   
3471 C  C   B PHE   A 156 ? 0.2751 0.2911 0.3597 0.0310  0.0097  0.0465  156 PHE   A C   
3472 O  O   A PHE   A 156 ? 0.1760 0.1782 0.3174 0.0303  0.0180  0.0620  156 PHE   A O   
3473 O  O   B PHE   A 156 ? 0.2837 0.2925 0.3690 0.0283  0.0047  0.0495  156 PHE   A O   
3474 C  CB  A PHE   A 156 ? 0.1976 0.1598 0.3140 0.0152  0.0033  0.0881  156 PHE   A CB  
3475 C  CB  B PHE   A 156 ? 0.2719 0.2809 0.3692 0.0333  0.0138  0.0128  156 PHE   A CB  
3476 C  CG  A PHE   A 156 ? 0.2250 0.1645 0.3287 0.0193  -0.0034 0.0860  156 PHE   A CG  
3477 C  CG  B PHE   A 156 ? 0.2891 0.2902 0.3946 0.0354  0.0129  -0.0078 156 PHE   A CG  
3478 C  CD1 A PHE   A 156 ? 0.2357 0.1708 0.3363 0.0180  -0.0002 0.0717  156 PHE   A CD1 
3479 C  CD1 B PHE   A 156 ? 0.2985 0.2932 0.4073 0.0389  0.0139  -0.0168 156 PHE   A CD1 
3480 C  CD2 A PHE   A 156 ? 0.2450 0.1771 0.3399 0.0268  -0.0082 0.0870  156 PHE   A CD2 
3481 C  CD2 B PHE   A 156 ? 0.2947 0.2946 0.4046 0.0318  0.0167  -0.0178 156 PHE   A CD2 
3482 C  CE1 A PHE   A 156 ? 0.2497 0.1816 0.3480 0.0207  0.0072  0.0595  156 PHE   A CE1 
3483 C  CE1 B PHE   A 156 ? 0.3010 0.2955 0.4137 0.0386  0.0134  -0.0241 156 PHE   A CE1 
3484 C  CE2 A PHE   A 156 ? 0.2585 0.1898 0.3492 0.0293  -0.0045 0.0685  156 PHE   A CE2 
3485 C  CE2 B PHE   A 156 ? 0.2990 0.2958 0.4121 0.0327  0.0174  -0.0241 156 PHE   A CE2 
3486 C  CZ  A PHE   A 156 ? 0.2583 0.1899 0.3511 0.0312  0.0025  0.0536  156 PHE   A CZ  
3487 C  CZ  B PHE   A 156 ? 0.3004 0.2966 0.4134 0.0382  0.0168  -0.0279 156 PHE   A CZ  
3506 N  N   A ASP   A 157 ? 0.1854 0.1890 0.3060 0.0439  -0.0021 0.0958  157 ASP   A N   
3507 N  N   B ASP   A 157 ? 0.2840 0.3095 0.3638 0.0318  0.0087  0.0602  157 ASP   A N   
3508 C  CA  A ASP   A 157 ? 0.2015 0.2184 0.3130 0.0469  -0.0089 0.0958  157 ASP   A CA  
3509 C  CA  B ASP   A 157 ? 0.2903 0.3266 0.3779 0.0274  0.0120  0.0719  157 ASP   A CA  
3510 C  C   A ASP   A 157 ? 0.1850 0.2370 0.3157 0.0556  0.0090  0.0998  157 ASP   A C   
3511 C  C   B ASP   A 157 ? 0.2856 0.3316 0.3806 0.0260  0.0093  0.0608  157 ASP   A C   
3512 O  O   A ASP   A 157 ? 0.1742 0.2298 0.2984 0.0544  0.0240  0.1198  157 ASP   A O   
3513 O  O   B ASP   A 157 ? 0.2828 0.3300 0.3815 0.0229  0.0089  0.0590  157 ASP   A O   
3514 C  CB  A ASP   A 157 ? 0.2315 0.2260 0.3258 0.0451  -0.0295 0.0973  157 ASP   A CB  
3515 C  CB  B ASP   A 157 ? 0.2978 0.3346 0.3940 0.0255  0.0200  0.0999  157 ASP   A CB  
3516 C  CG  A ASP   A 157 ? 0.2586 0.2357 0.3524 0.0418  -0.0392 0.0949  157 ASP   A CG  
3517 C  CG  B ASP   A 157 ? 0.3066 0.3407 0.4150 0.0240  0.0256  0.1243  157 ASP   A CG  
3518 O  OD1 A ASP   A 157 ? 0.2811 0.2442 0.3837 0.0356  -0.0491 0.0839  157 ASP   A OD1 
3519 O  OD1 B ASP   A 157 ? 0.3088 0.3388 0.4101 0.0254  0.0209  0.1450  157 ASP   A OD1 
3520 O  OD2 A ASP   A 157 ? 0.2621 0.2354 0.3634 0.0382  -0.0396 0.0940  157 ASP   A OD2 
3521 O  OD2 B ASP   A 157 ? 0.3097 0.3470 0.4368 0.0211  0.0284  0.1243  157 ASP   A OD2 
3530 N  N   A LYS   A 158 ? 0.1869 0.2645 0.3319 0.0598  0.0093  0.0781  158 LYS   A N   
3531 N  N   B LYS   A 158 ? 0.2853 0.3374 0.3803 0.0281  0.0038  0.0512  158 LYS   A N   
3532 C  CA  A LYS   A 158 ? 0.1795 0.2903 0.3326 0.0674  0.0118  0.0645  158 LYS   A CA  
3533 C  CA  B LYS   A 158 ? 0.2880 0.3465 0.3793 0.0305  0.0048  0.0417  158 LYS   A CA  
3534 C  C   A LYS   A 158 ? 0.1681 0.3068 0.3231 0.0772  0.0098  0.0720  158 LYS   A C   
3535 C  C   B LYS   A 158 ? 0.2737 0.3461 0.3627 0.0341  0.0100  0.0523  158 LYS   A C   
3536 O  O   A LYS   A 158 ? 0.1601 0.3184 0.3274 0.0686  0.0242  0.0648  158 LYS   A O   
3537 O  O   B LYS   A 158 ? 0.2672 0.3496 0.3490 0.0334  0.0063  0.0555  158 LYS   A O   
3538 C  CB  A LYS   A 158 ? 0.1859 0.2968 0.3367 0.0639  0.0272  0.0530  158 LYS   A CB  
3539 C  CB  B LYS   A 158 ? 0.3032 0.3573 0.3982 0.0300  0.0006  0.0229  158 LYS   A CB  
3540 C  CG  A LYS   A 158 ? 0.1957 0.3050 0.3458 0.0570  0.0383  0.0469  158 LYS   A CG  
3541 C  CG  B LYS   A 158 ? 0.3174 0.3677 0.4242 0.0284  -0.0056 0.0087  158 LYS   A CG  
3542 C  CD  A LYS   A 158 ? 0.1939 0.3152 0.3473 0.0480  0.0588  0.0481  158 LYS   A CD  
3543 C  CD  B LYS   A 158 ? 0.3245 0.3751 0.4445 0.0275  -0.0104 -0.0036 158 LYS   A CD  
3544 C  CE  A LYS   A 158 ? 0.1934 0.3233 0.3533 0.0356  0.0761  0.0506  158 LYS   A CE  
3545 C  CE  B LYS   A 158 ? 0.3277 0.3794 0.4597 0.0258  -0.0146 -0.0116 158 LYS   A CE  
3546 N  NZ  A LYS   A 158 ? 0.1935 0.3273 0.3528 0.0238  0.0840  0.0552  158 LYS   A NZ  
3547 N  NZ  B LYS   A 158 ? 0.3286 0.3813 0.4682 0.0253  -0.0182 -0.0156 158 LYS   A NZ  
3574 N  N   A ASN   A 159 ? 0.1747 0.3161 0.3269 0.0778  -0.0082 0.0851  159 ASN   A N   
3575 N  N   B ASN   A 159 ? 0.2698 0.3449 0.3690 0.0392  0.0158  0.0598  159 ASN   A N   
3576 C  CA  A ASN   A 159 ? 0.1826 0.3223 0.3318 0.0736  -0.0128 0.0976  159 ASN   A CA  
3577 C  CA  B ASN   A 159 ? 0.2681 0.3427 0.3750 0.0399  0.0289  0.0683  159 ASN   A CA  
3578 C  C   A ASN   A 159 ? 0.1715 0.3192 0.3099 0.0623  -0.0089 0.1028  159 ASN   A C   
3579 C  C   B ASN   A 159 ? 0.2460 0.3321 0.3460 0.0336  0.0230  0.0680  159 ASN   A C   
3580 O  O   A ASN   A 159 ? 0.1546 0.3297 0.2913 0.0601  -0.0172 0.0961  159 ASN   A O   
3581 O  O   B ASN   A 159 ? 0.2405 0.3432 0.3352 0.0315  0.0133  0.0648  159 ASN   A O   
3582 C  CB  A ASN   A 159 ? 0.1985 0.3304 0.3615 0.0762  -0.0111 0.1026  159 ASN   A CB  
3583 C  CB  B ASN   A 159 ? 0.2842 0.3503 0.4173 0.0448  0.0499  0.0763  159 ASN   A CB  
3584 C  CG  A ASN   A 159 ? 0.2200 0.3409 0.3938 0.0667  0.0008  0.1000  159 ASN   A CG  
3585 C  CG  B ASN   A 159 ? 0.2984 0.3586 0.4615 0.0411  0.0706  0.0785  159 ASN   A CG  
3586 O  OD1 A ASN   A 159 ? 0.2329 0.3455 0.4012 0.0594  0.0136  0.1037  159 ASN   A OD1 
3587 O  OD1 B ASN   A 159 ? 0.3027 0.3618 0.4858 0.0392  0.0731  0.0797  159 ASN   A OD1 
3588 N  ND2 A ASN   A 159 ? 0.2256 0.3454 0.4098 0.0605  0.0096  0.0939  159 ASN   A ND2 
3589 N  ND2 B ASN   A 159 ? 0.3059 0.3637 0.4769 0.0380  0.0796  0.0784  159 ASN   A ND2 
3602 N  N   A LEU   A 160 ? 0.1677 0.3020 0.3060 0.0520  -0.0162 0.1140  160 LEU   A N   
3603 N  N   B LEU   A 160 ? 0.2259 0.3134 0.3367 0.0267  0.0169  0.0756  160 LEU   A N   
3604 C  CA  A LEU   A 160 ? 0.1691 0.2884 0.2981 0.0327  -0.0004 0.1150  160 LEU   A CA  
3605 C  CA  B LEU   A 160 ? 0.2076 0.2984 0.3216 0.0203  0.0140  0.0825  160 LEU   A CA  
3606 C  C   A LEU   A 160 ? 0.1478 0.2826 0.2862 0.0222  0.0178  0.1146  160 LEU   A C   
3607 C  C   B LEU   A 160 ? 0.1872 0.2902 0.3096 0.0128  0.0169  0.0874  160 LEU   A C   
3608 O  O   A LEU   A 160 ? 0.1481 0.2921 0.2978 0.0154  0.0143  0.1079  160 LEU   A O   
3609 O  O   B LEU   A 160 ? 0.1857 0.2899 0.3229 0.0066  0.0160  0.0785  160 LEU   A O   
3610 C  CB  A LEU   A 160 ? 0.1842 0.2816 0.2864 0.0212  0.0032  0.1163  160 LEU   A CB  
3611 C  CB  B LEU   A 160 ? 0.2165 0.2939 0.3188 0.0129  0.0145  0.0797  160 LEU   A CB  
3612 C  CG  A LEU   A 160 ? 0.1929 0.2787 0.2833 0.0038  0.0169  0.1036  160 LEU   A CG  
3613 C  CG  B LEU   A 160 ? 0.2239 0.2940 0.3231 0.0015  0.0173  0.0658  160 LEU   A CG  
3614 C  CD1 A LEU   A 160 ? 0.2027 0.2740 0.2694 -0.0025 0.0215  0.1103  160 LEU   A CD1 
3615 C  CD1 B LEU   A 160 ? 0.2321 0.2986 0.3284 0.0008  0.0185  0.0562  160 LEU   A CD1 
3616 C  CD2 A LEU   A 160 ? 0.1923 0.2790 0.2882 0.0004  0.0238  0.0890  160 LEU   A CD2 
3617 C  CD2 B LEU   A 160 ? 0.2249 0.2886 0.3194 -0.0049 0.0208  0.0635  160 LEU   A CD2 
3640 N  N   A TYR   A 161 ? 0.1385 0.2675 0.2805 0.0222  0.0214  0.1185  161 TYR   A N   
3641 N  N   B TYR   A 161 ? 0.1785 0.2902 0.3036 0.0098  0.0122  0.0922  161 TYR   A N   
3642 C  CA  A TYR   A 161 ? 0.1392 0.2609 0.2802 0.0193  0.0245  0.1095  161 TYR   A CA  
3643 C  CA  B TYR   A 161 ? 0.1818 0.2943 0.3013 0.0003  0.0086  0.0932  161 TYR   A CA  
3644 C  C   A TYR   A 161 ? 0.1247 0.2802 0.2901 0.0125  0.0230  0.1008  161 TYR   A C   
3645 C  C   B TYR   A 161 ? 0.1804 0.3066 0.3130 -0.0030 0.0113  0.0891  161 TYR   A C   
3646 O  O   A TYR   A 161 ? 0.1151 0.2812 0.2928 0.0055  0.0142  0.1010  161 TYR   A O   
3647 O  O   B TYR   A 161 ? 0.1750 0.3054 0.3131 -0.0044 0.0078  0.0879  161 TYR   A O   
3648 C  CB  A TYR   A 161 ? 0.1483 0.2437 0.2807 0.0200  0.0263  0.0933  161 TYR   A CB  
3649 C  CB  B TYR   A 161 ? 0.1825 0.2919 0.2982 -0.0036 0.0041  0.0800  161 TYR   A CB  
3650 C  CG  A TYR   A 161 ? 0.1531 0.2319 0.2717 0.0193  0.0306  0.0709  161 TYR   A CG  
3651 C  CG  B TYR   A 161 ? 0.1822 0.2943 0.2899 -0.0092 0.0000  0.0660  161 TYR   A CG  
3652 C  CD1 A TYR   A 161 ? 0.1521 0.2259 0.2715 0.0148  0.0319  0.0610  161 TYR   A CD1 
3653 C  CD1 B TYR   A 161 ? 0.1836 0.3009 0.2873 -0.0129 -0.0076 0.0563  161 TYR   A CD1 
3654 C  CD2 A TYR   A 161 ? 0.1548 0.2314 0.2629 0.0206  0.0261  0.0632  161 TYR   A CD2 
3655 C  CD2 B TYR   A 161 ? 0.1750 0.2922 0.2841 -0.0141 0.0013  0.0611  161 TYR   A CD2 
3656 C  CE1 A TYR   A 161 ? 0.1575 0.2215 0.2670 0.0103  0.0245  0.0661  161 TYR   A CE1 
3657 C  CE1 B TYR   A 161 ? 0.1869 0.3045 0.2903 -0.0158 -0.0035 0.0591  161 TYR   A CE1 
3658 C  CE2 A TYR   A 161 ? 0.1583 0.2289 0.2635 0.0136  0.0266  0.0677  161 TYR   A CE2 
3659 C  CE2 B TYR   A 161 ? 0.1764 0.2978 0.2850 -0.0159 -0.0024 0.0615  161 TYR   A CE2 
3660 C  CZ  A TYR   A 161 ? 0.1685 0.2318 0.2717 0.0062  0.0186  0.0704  161 TYR   A CZ  
3661 C  CZ  B TYR   A 161 ? 0.1897 0.3061 0.3002 -0.0163 -0.0044 0.0675  161 TYR   A CZ  
3662 O  OH  A TYR   A 161 ? 0.1812 0.2415 0.2835 -0.0080 0.0136  0.0717  161 TYR   A OH  
3663 O  OH  B TYR   A 161 ? 0.1996 0.3128 0.3235 -0.0180 -0.0087 0.0769  161 TYR   A OH  
3682 N  N   A ASP   A 162 ? 0.1229 0.2990 0.3026 0.0129  0.0264  0.0929  162 ASP   A N   
3683 N  N   B ASP   A 162 ? 0.1868 0.3226 0.3347 -0.0021 0.0171  0.0866  162 ASP   A N   
3684 C  CA  A ASP   A 162 ? 0.1199 0.3179 0.3016 0.0073  0.0277  0.0896  162 ASP   A CA  
3685 C  CA  B ASP   A 162 ? 0.1935 0.3416 0.3453 -0.0056 0.0177  0.0858  162 ASP   A CA  
3686 C  C   A ASP   A 162 ? 0.1140 0.3274 0.3102 0.0035  0.0290  0.0896  162 ASP   A C   
3687 C  C   B ASP   A 162 ? 0.1949 0.3484 0.3409 -0.0147 0.0171  0.0859  162 ASP   A C   
3688 O  O   A ASP   A 162 ? 0.1165 0.3286 0.3264 0.0011  0.0285  0.0825  162 ASP   A O   
3689 O  O   B ASP   A 162 ? 0.1913 0.3474 0.3460 -0.0209 0.0131  0.0849  162 ASP   A O   
3690 C  CB  A ASP   A 162 ? 0.1361 0.3263 0.2898 0.0089  0.0390  0.0862  162 ASP   A CB  
3691 C  CB  B ASP   A 162 ? 0.2027 0.3537 0.3624 0.0041  0.0154  0.0858  162 ASP   A CB  
3692 C  CG  A ASP   A 162 ? 0.1542 0.3371 0.2950 0.0135  0.0390  0.0803  162 ASP   A CG  
3693 C  CG  B ASP   A 162 ? 0.2126 0.3642 0.3758 0.0156  0.0094  0.0907  162 ASP   A CG  
3694 O  OD1 A ASP   A 162 ? 0.1665 0.3435 0.3006 0.0144  0.0265  0.0727  162 ASP   A OD1 
3695 O  OD1 B ASP   A 162 ? 0.2135 0.3681 0.3839 0.0178  0.0044  0.0946  162 ASP   A OD1 
3696 O  OD2 A ASP   A 162 ? 0.1614 0.3395 0.3055 0.0152  0.0621  0.0794  162 ASP   A OD2 
3697 O  OD2 B ASP   A 162 ? 0.2228 0.3672 0.3833 0.0224  0.0156  0.0921  162 ASP   A OD2 
3706 N  N   A LYS   A 163 ? 0.1269 0.3382 0.3169 0.0042  0.0055  0.0912  163 LYS   A N   
3707 N  N   B LYS   A 163 ? 0.2073 0.3565 0.3397 -0.0155 0.0119  0.0827  163 LYS   A N   
3708 C  CA  A LYS   A 163 ? 0.1408 0.3473 0.3128 0.0005  -0.0036 0.0874  163 LYS   A CA  
3709 C  CA  B LYS   A 163 ? 0.2206 0.3614 0.3358 -0.0171 0.0096  0.0770  163 LYS   A CA  
3710 C  C   A LYS   A 163 ? 0.1291 0.3417 0.3045 -0.0022 0.0123  0.0824  163 LYS   A C   
3711 C  C   B LYS   A 163 ? 0.2081 0.3421 0.3155 -0.0200 0.0142  0.0703  163 LYS   A C   
3712 O  O   A LYS   A 163 ? 0.1197 0.3544 0.3218 -0.0118 0.0125  0.0723  163 LYS   A O   
3713 O  O   B LYS   A 163 ? 0.2102 0.3507 0.3266 -0.0226 0.0085  0.0654  163 LYS   A O   
3714 C  CB  A LYS   A 163 ? 0.1741 0.3612 0.3393 0.0015  -0.0135 0.0867  163 LYS   A CB  
3715 C  CB  B LYS   A 163 ? 0.2543 0.3840 0.3689 -0.0148 0.0062  0.0758  163 LYS   A CB  
3716 C  CG  A LYS   A 163 ? 0.2108 0.3755 0.3781 0.0012  -0.0095 0.0855  163 LYS   A CG  
3717 C  CG  B LYS   A 163 ? 0.2868 0.4030 0.4105 -0.0178 0.0082  0.0770  163 LYS   A CG  
3718 C  CD  A LYS   A 163 ? 0.2451 0.3864 0.4171 0.0009  -0.0107 0.0827  163 LYS   A CD  
3719 C  CD  B LYS   A 163 ? 0.3160 0.4182 0.4552 -0.0196 0.0072  0.0774  163 LYS   A CD  
3720 C  CE  A LYS   A 163 ? 0.2733 0.3930 0.4491 -0.0002 -0.0100 0.0808  163 LYS   A CE  
3721 C  CE  B LYS   A 163 ? 0.3384 0.4276 0.4907 -0.0205 0.0077  0.0791  163 LYS   A CE  
3722 N  NZ  A LYS   A 163 ? 0.2786 0.3966 0.4680 -0.0016 -0.0081 0.0818  163 LYS   A NZ  
3723 N  NZ  B LYS   A 163 ? 0.3489 0.4331 0.5136 -0.0223 0.0059  0.0788  163 LYS   A NZ  
3750 N  N   A LEU   A 164 ? 0.1177 0.3203 0.2824 -0.0082 0.0099  0.0782  164 LEU   A N   
3751 N  N   B LEU   A 164 ? 0.1871 0.3155 0.2920 -0.0256 0.0140  0.0662  164 LEU   A N   
3752 C  CA  A LEU   A 164 ? 0.1183 0.2987 0.2734 -0.0194 0.0163  0.0732  164 LEU   A CA  
3753 C  CA  B LEU   A 164 ? 0.1750 0.2914 0.2821 -0.0336 0.0197  0.0655  164 LEU   A CA  
3754 C  C   A LEU   A 164 ? 0.1232 0.2955 0.2851 -0.0260 0.0212  0.0726  164 LEU   A C   
3755 C  C   B LEU   A 164 ? 0.1741 0.2925 0.2851 -0.0313 0.0255  0.0663  164 LEU   A C   
3756 O  O   A LEU   A 164 ? 0.1239 0.2990 0.2921 -0.0431 0.0364  0.0596  164 LEU   A O   
3757 O  O   B LEU   A 164 ? 0.1751 0.2940 0.2975 -0.0324 0.0400  0.0490  164 LEU   A O   
3758 C  CB  A LEU   A 164 ? 0.1237 0.2834 0.2574 -0.0215 0.0198  0.0678  164 LEU   A CB  
3759 C  CB  B LEU   A 164 ? 0.1742 0.2763 0.2765 -0.0461 0.0186  0.0672  164 LEU   A CB  
3760 C  CG  A LEU   A 164 ? 0.1434 0.2756 0.2564 -0.0187 0.0162  0.0619  164 LEU   A CG  
3761 C  CG  B LEU   A 164 ? 0.1787 0.2712 0.2781 -0.0453 0.0163  0.0613  164 LEU   A CG  
3762 C  CD1 A LEU   A 164 ? 0.1446 0.2697 0.2536 -0.0110 0.0099  0.0612  164 LEU   A CD1 
3763 C  CD1 B LEU   A 164 ? 0.1777 0.2697 0.2811 -0.0444 0.0124  0.0537  164 LEU   A CD1 
3764 C  CD2 A LEU   A 164 ? 0.1569 0.2775 0.2482 -0.0214 0.0233  0.0591  164 LEU   A CD2 
3765 C  CD2 B LEU   A 164 ? 0.1886 0.2746 0.2781 -0.0407 0.0142  0.0583  164 LEU   A CD2 
3788 N  N   A VAL   A 165 ? 0.1224 0.2888 0.2876 -0.0244 0.0213  0.0773  165 VAL   A N   
3789 N  N   B VAL   A 165 ? 0.1729 0.2987 0.2808 -0.0281 0.0204  0.0712  165 VAL   A N   
3790 C  CA  A VAL   A 165 ? 0.1301 0.2826 0.2841 -0.0283 0.0314  0.0806  165 VAL   A CA  
3791 C  CA  B VAL   A 165 ? 0.1785 0.3062 0.2790 -0.0250 0.0209  0.0710  165 VAL   A CA  
3792 C  C   A VAL   A 165 ? 0.1228 0.2914 0.2767 -0.0238 0.0388  0.0830  165 VAL   A C   
3793 C  C   B VAL   A 165 ? 0.1749 0.3206 0.2810 -0.0231 0.0186  0.0674  165 VAL   A C   
3794 O  O   A VAL   A 165 ? 0.1265 0.2936 0.2684 -0.0208 0.0406  0.0854  165 VAL   A O   
3795 O  O   B VAL   A 165 ? 0.1719 0.3226 0.2746 -0.0199 0.0219  0.0627  165 VAL   A O   
3796 C  CB  A VAL   A 165 ? 0.1479 0.2740 0.2967 -0.0277 0.0386  0.0732  165 VAL   A CB  
3797 C  CB  B VAL   A 165 ? 0.1914 0.3029 0.2843 -0.0191 0.0248  0.0660  165 VAL   A CB  
3798 C  CG1 A VAL   A 165 ? 0.1487 0.2738 0.3019 -0.0279 0.0399  0.0716  165 VAL   A CG1 
3799 C  CG1 B VAL   A 165 ? 0.1919 0.3051 0.2869 -0.0188 0.0255  0.0603  165 VAL   A CG1 
3800 C  CG2 A VAL   A 165 ? 0.1621 0.2701 0.3065 -0.0293 0.0390  0.0752  165 VAL   A CG2 
3801 C  CG2 B VAL   A 165 ? 0.2028 0.3019 0.2928 -0.0169 0.0221  0.0644  165 VAL   A CG2 
3820 N  N   A SER   A 166 ? 0.1187 0.3020 0.2904 -0.0211 0.0324  0.0798  166 SER   A N   
3821 N  N   B SER   A 166 ? 0.1763 0.3332 0.2995 -0.0242 0.0129  0.0638  166 SER   A N   
3822 C  CA  A SER   A 166 ? 0.1259 0.3161 0.2944 -0.0275 0.0287  0.0765  166 SER   A CA  
3823 C  CA  B SER   A 166 ? 0.1831 0.3474 0.3145 -0.0321 0.0056  0.0557  166 SER   A CA  
3824 C  C   A SER   A 166 ? 0.1352 0.3375 0.2836 -0.0292 0.0043  0.0605  166 SER   A C   
3825 C  C   B SER   A 166 ? 0.1919 0.3527 0.3106 -0.0431 0.0057  0.0589  166 SER   A C   
3826 O  O   A SER   A 166 ? 0.1453 0.3491 0.2931 -0.0376 -0.0030 0.0494  166 SER   A O   
3827 O  O   B SER   A 166 ? 0.1878 0.3548 0.3012 -0.0541 0.0001  0.0586  166 SER   A O   
3828 C  CB  A SER   A 166 ? 0.1519 0.3130 0.3218 -0.0303 0.0321  0.0823  166 SER   A CB  
3829 C  CB  B SER   A 166 ? 0.1903 0.3572 0.3451 -0.0258 -0.0111 0.0407  166 SER   A CB  
3830 O  OG  A SER   A 166 ? 0.1864 0.3155 0.3556 -0.0377 0.0345  0.0795  166 SER   A OG  
3831 O  OG  B SER   A 166 ? 0.2189 0.3665 0.3719 -0.0258 -0.0135 0.0412  166 SER   A OG  
3842 N  N   A SER   A 167 ? 0.1382 0.3421 0.2578 -0.0155 -0.0063 0.0528  167 SER   A N   
3843 N  N   B SER   A 167 ? 0.2075 0.3545 0.3137 -0.0349 0.0092  0.0605  167 SER   A N   
3844 C  CA  A SER   A 167 ? 0.1507 0.3450 0.2493 -0.0127 -0.0169 0.0358  167 SER   A CA  
3845 C  CA  B SER   A 167 ? 0.2203 0.3556 0.3151 -0.0289 0.0160  0.0584  167 SER   A CA  
3846 C  C   A SER   A 167 ? 0.1536 0.3337 0.2502 -0.0105 -0.0101 0.0295  167 SER   A C   
3847 C  C   B SER   A 167 ? 0.2084 0.3564 0.3198 -0.0189 0.0258  0.0528  167 SER   A C   
3848 O  O   A SER   A 167 ? 0.1512 0.3361 0.2439 -0.0169 -0.0089 0.0196  167 SER   A O   
3849 O  O   B SER   A 167 ? 0.2212 0.3581 0.3341 -0.0156 0.0205  0.0578  167 SER   A O   
3850 C  CB  A SER   A 167 ? 0.1466 0.3563 0.2424 -0.0186 -0.0080 0.0344  167 SER   A CB  
3851 C  CB  B SER   A 167 ? 0.2444 0.3579 0.3285 -0.0290 0.0067  0.0513  167 SER   A CB  
3852 O  OG  A SER   A 167 ? 0.1335 0.3641 0.2242 -0.0230 0.0021  0.0399  167 SER   A OG  
3853 O  OG  B SER   A 167 ? 0.2622 0.3596 0.3409 -0.0291 -0.0011 0.0477  167 SER   A OG  
3864 N  N   A PHE   A 168 ? 0.1535 0.3189 0.2481 -0.0063 -0.0096 0.0346  168 PHE   A N   
3865 N  N   B PHE   A 168 ? 0.1838 0.3544 0.3027 -0.0124 0.0399  0.0420  168 PHE   A N   
3866 C  CA  A PHE   A 168 ? 0.1622 0.3088 0.2650 -0.0075 0.0020  0.0289  168 PHE   A CA  
3867 C  CA  B PHE   A 168 ? 0.1732 0.3568 0.2869 -0.0077 0.0504  0.0310  168 PHE   A CA  
3868 C  C   A PHE   A 168 ? 0.1797 0.3165 0.3021 -0.0107 0.0276  0.0158  168 PHE   A C   
3869 C  C   B PHE   A 168 ? 0.1799 0.3712 0.3022 -0.0145 0.0612  0.0135  168 PHE   A C   
3870 O  O   A PHE   A 168 ? 0.1813 0.3185 0.3277 -0.0152 0.0369  0.0216  168 PHE   A O   
3871 O  O   B PHE   A 168 ? 0.1709 0.3745 0.2986 -0.0191 0.0848  0.0060  168 PHE   A O   
3872 C  CB  A PHE   A 168 ? 0.1572 0.2920 0.2488 -0.0150 -0.0152 0.0298  168 PHE   A CB  
3873 C  CB  B PHE   A 168 ? 0.1695 0.3497 0.2769 -0.0076 0.0391  0.0423  168 PHE   A CB  
3874 C  CG  A PHE   A 168 ? 0.1558 0.2770 0.2377 -0.0188 -0.0222 0.0239  168 PHE   A CG  
3875 C  CG  B PHE   A 168 ? 0.1678 0.3409 0.2690 -0.0070 0.0286  0.0559  168 PHE   A CG  
3876 C  CD1 A PHE   A 168 ? 0.1513 0.2707 0.2377 -0.0203 -0.0256 0.0256  168 PHE   A CD1 
3877 C  CD1 B PHE   A 168 ? 0.1647 0.3380 0.2658 -0.0064 0.0268  0.0646  168 PHE   A CD1 
3878 C  CD2 A PHE   A 168 ? 0.1593 0.2701 0.2248 -0.0184 -0.0135 0.0167  168 PHE   A CD2 
3879 C  CD2 B PHE   A 168 ? 0.1690 0.3355 0.2657 -0.0069 0.0295  0.0614  168 PHE   A CD2 
3880 C  CE1 A PHE   A 168 ? 0.1424 0.2654 0.2273 -0.0213 -0.0310 0.0217  168 PHE   A CE1 
3881 C  CE1 B PHE   A 168 ? 0.1610 0.3348 0.2634 -0.0082 0.0258  0.0702  168 PHE   A CE1 
3882 C  CE2 A PHE   A 168 ? 0.1620 0.2637 0.2235 -0.0203 -0.0131 0.0202  168 PHE   A CE2 
3883 C  CE2 B PHE   A 168 ? 0.1692 0.3318 0.2681 -0.0084 0.0253  0.0691  168 PHE   A CE2 
3884 C  CZ  A PHE   A 168 ? 0.1533 0.2634 0.2245 -0.0217 -0.0214 0.0237  168 PHE   A CZ  
3885 C  CZ  B PHE   A 168 ? 0.1657 0.3310 0.2669 -0.0120 0.0246  0.0713  168 PHE   A CZ  
3904 N  N   A LEU   A 169 ? 0.2071 0.3185 0.3244 -0.0074 0.0376  -0.0057 169 LEU   A N   
3905 N  N   B LEU   A 169 ? 0.2058 0.3849 0.3277 -0.0089 0.0477  0.0023  169 LEU   A N   
3906 C  CA  A LEU   A 169 ? 0.2332 0.3179 0.3384 -0.0023 0.0386  -0.0111 169 LEU   A CA  
3907 C  CA  B LEU   A 169 ? 0.2389 0.4011 0.3571 -0.0045 0.0337  -0.0144 169 LEU   A CA  
3908 C  C   A LEU   A 169 ? 0.2258 0.3129 0.3385 -0.0029 0.0532  0.0007  169 LEU   A C   
3909 C  C   B LEU   A 169 ? 0.2563 0.4111 0.3816 0.0015  0.0320  -0.0304 169 LEU   A C   
3910 O  O   A LEU   A 169 ? 0.2309 0.3127 0.3393 0.0010  0.0484  -0.0002 169 LEU   A O   
3911 O  O   B LEU   A 169 ? 0.2571 0.4133 0.3822 0.0029  0.0277  -0.0301 169 LEU   A O   
3912 C  CB  A LEU   A 169 ? 0.2574 0.3230 0.3443 0.0015  0.0283  -0.0258 169 LEU   A CB  
3913 C  CB  B LEU   A 169 ? 0.2524 0.4049 0.3542 -0.0069 0.0262  -0.0118 169 LEU   A CB  
3914 C  CG  A LEU   A 169 ? 0.2770 0.3265 0.3505 0.0001  0.0187  -0.0423 169 LEU   A CG  
3915 C  CG  B LEU   A 169 ? 0.2640 0.4080 0.3486 -0.0101 0.0195  -0.0090 169 LEU   A CG  
3916 C  CD1 A LEU   A 169 ? 0.2855 0.3267 0.3546 0.0010  0.0131  -0.0490 169 LEU   A CD1 
3917 C  CD1 B LEU   A 169 ? 0.2692 0.4092 0.3430 -0.0137 0.0202  -0.0087 169 LEU   A CD1 
3918 C  CD2 A LEU   A 169 ? 0.2814 0.3269 0.3463 -0.0020 0.0223  -0.0470 169 LEU   A CD2 
3919 C  CD2 B LEU   A 169 ? 0.2714 0.4101 0.3609 -0.0114 0.0115  -0.0068 169 LEU   A CD2 
3920 O  OXT A LEU   A 169 ? 0.2136 0.3136 0.3278 -0.0053 0.0798  0.0054  169 LEU   A OXT 
3921 O  OXT B LEU   A 169 ? 0.2738 0.4180 0.4027 0.0035  0.0272  -0.0386 169 LEU   A OXT 
3944 N  N   A SER   B 1   ? 0.3912 0.3795 0.3926 -0.0950 -0.0826 0.0528  1   SER   B N   
3945 N  N   B SER   B 1   ? 0.3684 0.3313 0.3247 -0.1018 -0.0683 0.0337  1   SER   B N   
3946 C  CA  A SER   B 1   ? 0.3819 0.3779 0.3916 -0.0984 -0.0850 0.0544  1   SER   B CA  
3947 C  CA  B SER   B 1   ? 0.3596 0.3363 0.3319 -0.1049 -0.0717 0.0335  1   SER   B CA  
3948 C  C   A SER   B 1   ? 0.3562 0.3712 0.3736 -0.0988 -0.0893 0.0663  1   SER   B C   
3949 C  C   B SER   B 1   ? 0.3367 0.3428 0.3282 -0.1038 -0.0732 0.0538  1   SER   B C   
3950 O  O   A SER   B 1   ? 0.3602 0.3716 0.3577 -0.0970 -0.0898 0.0629  1   SER   B O   
3951 O  O   B SER   B 1   ? 0.3399 0.3424 0.3137 -0.1020 -0.0715 0.0531  1   SER   B O   
3952 C  CB  A SER   B 1   ? 0.3936 0.3796 0.4057 -0.0989 -0.0777 0.0465  1   SER   B CB  
3953 C  CB  B SER   B 1   ? 0.3706 0.3313 0.3407 -0.1044 -0.0658 0.0154  1   SER   B CB  
3954 O  OG  A SER   B 1   ? 0.4036 0.3851 0.4329 -0.0992 -0.0695 0.0440  1   SER   B OG  
3955 O  OG  B SER   B 1   ? 0.3803 0.3324 0.3642 -0.1027 -0.0604 0.0054  1   SER   B OG  
3970 N  N   A MET   B 2   ? 0.3274 0.3603 0.3670 -0.0984 -0.0892 0.0924  2   MET   B N   
3971 N  N   B MET   B 2   ? 0.3145 0.3463 0.3305 -0.0998 -0.0699 0.0883  2   MET   B N   
3972 C  CA  A MET   B 2   ? 0.3051 0.3511 0.3717 -0.0849 -0.0873 0.1088  2   MET   B CA  
3973 C  CA  B MET   B 2   ? 0.3000 0.3502 0.3401 -0.0815 -0.0655 0.1098  2   MET   B CA  
3974 C  C   A MET   B 2   ? 0.2599 0.3203 0.3253 -0.0768 -0.1006 0.1322  2   MET   B C   
3975 C  C   B MET   B 2   ? 0.2723 0.3334 0.3115 -0.0672 -0.0571 0.1217  2   MET   B C   
3976 O  O   A MET   B 2   ? 0.2413 0.3232 0.3084 -0.0728 -0.1210 0.1445  2   MET   B O   
3977 O  O   B MET   B 2   ? 0.2711 0.3466 0.3209 -0.0586 -0.0533 0.1159  2   MET   B O   
3978 C  CB  A MET   B 2   ? 0.3336 0.3777 0.4407 -0.0684 -0.0679 0.0886  2   MET   B CB  
3979 C  CB  B MET   B 2   ? 0.3202 0.3754 0.3939 -0.0671 -0.0681 0.1062  2   MET   B CB  
3980 C  CG  A MET   B 2   ? 0.3590 0.4000 0.5054 -0.0525 -0.0480 0.0767  2   MET   B CG  
3981 C  CG  B MET   B 2   ? 0.3370 0.3963 0.4359 -0.0536 -0.0672 0.1135  2   MET   B CG  
3982 S  SD  A MET   B 2   ? 0.3804 0.4192 0.5660 -0.0396 -0.0336 0.0673  2   MET   B SD  
3983 S  SD  B MET   B 2   ? 0.3527 0.4158 0.4706 -0.0417 -0.0691 0.1203  2   MET   B SD  
3984 C  CE  A MET   B 2   ? 0.3834 0.4235 0.5662 -0.0379 -0.0266 0.0685  2   MET   B CE  
3985 C  CE  B MET   B 2   ? 0.3538 0.4195 0.4798 -0.0412 -0.0669 0.1131  2   MET   B CE  
4004 N  N   A VAL   B 3   ? 0.2318 0.2800 0.3040 -0.0819 -0.0887 0.1384  3   VAL   B N   
4005 N  N   B VAL   B 3   ? 0.2448 0.2989 0.2842 -0.0686 -0.0495 0.1307  3   VAL   B N   
4006 C  CA  A VAL   B 3   ? 0.2195 0.2459 0.2976 -0.0743 -0.0773 0.1234  3   VAL   B CA  
4007 C  CA  B VAL   B 3   ? 0.2298 0.2701 0.2788 -0.0583 -0.0461 0.1111  3   VAL   B CA  
4008 C  C   A VAL   B 3   ? 0.1970 0.2290 0.2606 -0.0652 -0.0741 0.1088  3   VAL   B C   
4009 C  C   B VAL   B 3   ? 0.2059 0.2502 0.2515 -0.0509 -0.0502 0.0996  3   VAL   B C   
4010 O  O   A VAL   B 3   ? 0.1954 0.2224 0.2618 -0.0595 -0.0743 0.1174  3   VAL   B O   
4011 O  O   B VAL   B 3   ? 0.2068 0.2598 0.2545 -0.0341 -0.0510 0.0984  3   VAL   B O   
4012 C  CB  A VAL   B 3   ? 0.2349 0.2446 0.3337 -0.0713 -0.0663 0.1064  3   VAL   B CB  
4013 C  CB  B VAL   B 3   ? 0.2429 0.2645 0.3038 -0.0567 -0.0373 0.1007  3   VAL   B CB  
4014 C  CG1 A VAL   B 3   ? 0.2403 0.2396 0.3485 -0.0734 -0.0636 0.1019  3   VAL   B CG1 
4015 C  CG1 B VAL   B 3   ? 0.2469 0.2585 0.3177 -0.0611 -0.0363 0.0951  3   VAL   B CG1 
4016 C  CG2 A VAL   B 3   ? 0.2386 0.2518 0.3502 -0.0697 -0.0584 0.1014  3   VAL   B CG2 
4017 C  CG2 B VAL   B 3   ? 0.2473 0.2686 0.3088 -0.0550 -0.0323 0.0993  3   VAL   B CG2 
4036 N  N   . ASN   B 4   ? 0.1874 0.2206 0.2379 -0.0570 -0.0601 0.0898  4   ASN   B N   
4037 C  CA  . ASN   B 4   ? 0.1918 0.2197 0.1996 -0.0558 -0.0496 0.0528  4   ASN   B CA  
4038 C  C   . ASN   B 4   ? 0.2001 0.2313 0.1847 -0.0560 -0.0396 0.0366  4   ASN   B C   
4039 O  O   . ASN   B 4   ? 0.2037 0.2383 0.2039 -0.0556 -0.0317 0.0168  4   ASN   B O   
4040 C  CB  . ASN   B 4   ? 0.1922 0.2108 0.1890 -0.0526 -0.0614 0.0420  4   ASN   B CB  
4041 C  CG  . ASN   B 4   ? 0.1924 0.1875 0.1805 -0.0507 -0.0516 0.0362  4   ASN   B CG  
4042 O  OD1 . ASN   B 4   ? 0.1883 0.1776 0.1790 -0.0465 -0.0557 0.0353  4   ASN   B OD1 
4043 N  ND2 . ASN   B 4   ? 0.2162 0.1936 0.1846 -0.0256 -0.0373 0.0287  4   ASN   B ND2 
4051 N  N   . SER   B 5   ? 0.2125 0.2411 0.1887 -0.0538 -0.0278 0.0362  5   SER   B N   
4052 C  CA  . SER   B 5   ? 0.2375 0.2752 0.2156 -0.0393 -0.0113 0.0347  5   SER   B CA  
4053 C  C   . SER   B 5   ? 0.2549 0.2777 0.2478 -0.0573 0.0211  0.0386  5   SER   B C   
4054 O  O   . SER   B 5   ? 0.2723 0.2764 0.3253 -0.0502 0.0536  0.0384  5   SER   B O   
4055 C  CB  . SER   B 5   ? 0.2489 0.2958 0.2370 -0.0291 -0.0073 0.0424  5   SER   B CB  
4056 O  OG  . SER   B 5   ? 0.2708 0.3233 0.2963 -0.0182 -0.0090 0.0470  5   SER   B OG  
4062 N  N   . PHE   B 6   ? 0.2715 0.2923 0.2173 -0.0624 0.0388  0.0375  6   PHE   B N   
4063 C  CA  . PHE   B 6   ? 0.2825 0.2916 0.1895 -0.0791 0.0410  0.0191  6   PHE   B CA  
4064 C  C   . PHE   B 6   ? 0.3341 0.3171 0.2300 -0.0858 0.0619  -0.0096 6   PHE   B C   
4065 O  O   . PHE   B 6   ? 0.3489 0.3461 0.2610 -0.0796 0.0431  -0.0265 6   PHE   B O   
4066 C  CB  . PHE   B 6   ? 0.2513 0.2730 0.1763 -0.0725 0.0119  0.0133  6   PHE   B CB  
4067 C  CG  . PHE   B 6   ? 0.2167 0.2448 0.1775 -0.0671 0.0030  0.0110  6   PHE   B CG  
4068 C  CD1 . PHE   B 6   ? 0.2138 0.2161 0.1629 -0.0640 -0.0090 0.0028  6   PHE   B CD1 
4069 C  CD2 . PHE   B 6   ? 0.1965 0.2417 0.1825 -0.0535 0.0052  0.0336  6   PHE   B CD2 
4070 C  CE1 . PHE   B 6   ? 0.2099 0.1932 0.1714 -0.0497 -0.0084 0.0002  6   PHE   B CE1 
4071 C  CE2 . PHE   B 6   ? 0.1964 0.2239 0.2115 -0.0402 0.0059  0.0319  6   PHE   B CE2 
4072 C  CZ  . PHE   B 6   ? 0.1983 0.1998 0.1970 -0.0428 0.0015  0.0069  6   PHE   B CZ  
4082 N  N   . SER   B 7   ? 0.3678 0.2974 0.2479 -0.1096 0.0881  -0.0366 7   SER   B N   
4083 C  CA  . SER   B 7   ? 0.4014 0.3120 0.2992 -0.1066 0.1076  -0.0432 7   SER   B CA  
4084 C  C   . SER   B 7   ? 0.3983 0.2977 0.2917 -0.1087 0.1248  -0.0545 7   SER   B C   
4085 O  O   . SER   B 7   ? 0.4054 0.3006 0.3252 -0.1116 0.1213  -0.0538 7   SER   B O   
4086 C  CB  . SER   B 7   ? 0.4254 0.3319 0.3598 -0.1044 0.1221  -0.0379 7   SER   B CB  
4087 O  OG  . SER   B 7   ? 0.4407 0.3457 0.4158 -0.1011 0.1238  -0.0297 7   SER   B OG  
4093 N  N   . GLY   B 8   ? 0.3934 0.2884 0.3038 -0.0938 0.1293  -0.0645 8   GLY   B N   
4094 C  CA  . GLY   B 8   ? 0.3762 0.2736 0.3123 -0.0898 0.1296  -0.0644 8   GLY   B CA  
4095 C  C   . GLY   B 8   ? 0.3543 0.2489 0.3022 -0.0882 0.1306  -0.0584 8   GLY   B C   
4096 O  O   . GLY   B 8   ? 0.3650 0.2598 0.3325 -0.0751 0.1337  -0.0651 8   GLY   B O   
4100 N  N   . TYR   B 9   ? 0.3298 0.2255 0.2723 -0.0806 0.1084  -0.0638 9   TYR   B N   
4101 C  CA  . TYR   B 9   ? 0.3078 0.1996 0.2403 -0.0690 0.0727  -0.0495 9   TYR   B CA  
4102 C  C   . TYR   B 9   ? 0.3035 0.2041 0.2221 -0.0622 0.0320  -0.0378 9   TYR   B C   
4103 O  O   . TYR   B 9   ? 0.3175 0.2289 0.2577 -0.0646 0.0296  -0.0210 9   TYR   B O   
4104 C  CB  . TYR   B 9   ? 0.3008 0.1879 0.2380 -0.0588 0.0620  -0.0389 9   TYR   B CB  
4105 C  CG  . TYR   B 9   ? 0.2909 0.1756 0.2420 -0.0599 0.0592  -0.0432 9   TYR   B CG  
4106 C  CD1 . TYR   B 9   ? 0.2929 0.1726 0.2635 -0.0761 0.0640  -0.0369 9   TYR   B CD1 
4107 C  CD2 . TYR   B 9   ? 0.2738 0.1723 0.2229 -0.0559 0.0602  -0.0514 9   TYR   B CD2 
4108 C  CE1 . TYR   B 9   ? 0.2848 0.1829 0.2698 -0.0784 0.0712  -0.0450 9   TYR   B CE1 
4109 C  CE2 . TYR   B 9   ? 0.2725 0.1725 0.2340 -0.0515 0.0571  -0.0502 9   TYR   B CE2 
4110 C  CZ  . TYR   B 9   ? 0.2755 0.1864 0.2637 -0.0683 0.0622  -0.0595 9   TYR   B CZ  
4111 O  OH  . TYR   B 9   ? 0.2755 0.1980 0.2796 -0.0792 0.0655  -0.0769 9   TYR   B OH  
4121 N  N   . LEU   B 10  ? 0.2824 0.1851 0.1952 -0.0580 0.0076  -0.0351 10  LEU   B N   
4122 C  CA  . LEU   B 10  ? 0.2801 0.1843 0.1979 -0.0646 -0.0148 -0.0297 10  LEU   B CA  
4123 C  C   . LEU   B 10  ? 0.2609 0.1798 0.2050 -0.0578 -0.0250 -0.0296 10  LEU   B C   
4124 O  O   . LEU   B 10  ? 0.2432 0.1786 0.2051 -0.0405 -0.0182 -0.0231 10  LEU   B O   
4125 C  CB  . LEU   B 10  ? 0.2990 0.1880 0.2097 -0.0694 -0.0356 -0.0154 10  LEU   B CB  
4126 C  CG  . LEU   B 10  ? 0.3172 0.2000 0.2431 -0.0630 -0.0640 0.0000  10  LEU   B CG  
4127 C  CD1 . LEU   B 10  ? 0.3285 0.2084 0.2727 -0.0632 -0.0600 0.0019  10  LEU   B CD1 
4128 C  CD2 . LEU   B 10  ? 0.3276 0.2136 0.2723 -0.0588 -0.0584 0.0100  10  LEU   B CD2 
4140 N  N   . LYS   B 11  ? 0.2738 0.2067 0.2099 -0.0491 -0.0360 -0.0222 11  LYS   B N   
4141 C  CA  . LYS   B 11  ? 0.2922 0.2345 0.2313 -0.0379 -0.0521 -0.0272 11  LYS   B CA  
4142 C  C   . LYS   B 11  ? 0.2715 0.2185 0.2418 -0.0592 -0.0424 -0.0389 11  LYS   B C   
4143 O  O   . LYS   B 11  ? 0.2832 0.2401 0.2754 -0.0739 -0.0413 -0.0707 11  LYS   B O   
4144 C  CB  . LYS   B 11  ? 0.3309 0.2855 0.2856 -0.0125 -0.0581 -0.0188 11  LYS   B CB  
4145 C  CG  . LYS   B 11  ? 0.3630 0.3200 0.3537 0.0021  -0.0595 -0.0202 11  LYS   B CG  
4146 C  CD  . LYS   B 11  ? 0.3883 0.3442 0.4195 0.0130  -0.0567 -0.0224 11  LYS   B CD  
4147 C  CE  . LYS   B 11  ? 0.4086 0.3605 0.4697 0.0155  -0.0532 -0.0254 11  LYS   B CE  
4148 N  NZ  . LYS   B 11  ? 0.4203 0.3708 0.4996 0.0152  -0.0524 -0.0251 11  LYS   B NZ  
4162 N  N   . LEU   B 12  ? 0.2384 0.1961 0.2371 -0.0540 -0.0338 -0.0391 12  LEU   B N   
4163 C  CA  . LEU   B 12  ? 0.2258 0.1790 0.2557 -0.0520 -0.0327 -0.0348 12  LEU   B CA  
4164 C  C   . LEU   B 12  ? 0.2174 0.1771 0.2691 -0.0521 -0.0459 -0.0263 12  LEU   B C   
4165 O  O   . LEU   B 12  ? 0.2152 0.1772 0.2897 -0.0620 -0.0579 -0.0214 12  LEU   B O   
4166 C  CB  . LEU   B 12  ? 0.2233 0.1663 0.2509 -0.0369 -0.0188 -0.0411 12  LEU   B CB  
4167 C  CG  . LEU   B 12  ? 0.2268 0.1575 0.2545 -0.0393 -0.0086 -0.0297 12  LEU   B CG  
4168 C  CD1 . LEU   B 12  ? 0.2413 0.1660 0.2411 -0.0262 -0.0118 -0.0183 12  LEU   B CD1 
4169 C  CD2 . LEU   B 12  ? 0.2363 0.1584 0.2766 -0.0391 -0.0076 -0.0424 12  LEU   B CD2 
4181 N  N   . THR   B 13  ? 0.2088 0.1821 0.2703 -0.0501 -0.0546 -0.0367 13  THR   B N   
4182 C  CA  . THR   B 13  ? 0.2077 0.1907 0.2650 -0.0577 -0.0628 -0.0230 13  THR   B CA  
4183 C  C   . THR   B 13  ? 0.2460 0.2090 0.2810 -0.0653 -0.0742 -0.0193 13  THR   B C   
4184 O  O   . THR   B 13  ? 0.2630 0.2060 0.2856 -0.0627 -0.0402 -0.0235 13  THR   B O   
4185 C  CB  . THR   B 13  ? 0.1954 0.1927 0.2692 -0.0548 -0.0539 -0.0151 13  THR   B CB  
4186 O  OG1 . THR   B 13  ? 0.1857 0.1859 0.2661 -0.0493 -0.0372 -0.0183 13  THR   B OG1 
4187 C  CG2 . THR   B 13  ? 0.2109 0.1960 0.2702 -0.0494 -0.0425 -0.0124 13  THR   B CG2 
4195 N  N   A ASP   B 14  ? 0.2559 0.2210 0.2950 -0.0684 -0.0959 -0.0089 14  ASP   B N   
4196 N  N   B ASP   B 14  ? 0.2572 0.2224 0.2883 -0.0660 -0.0947 -0.0056 14  ASP   B N   
4197 C  CA  A ASP   B 14  ? 0.2659 0.2356 0.3134 -0.0674 -0.1008 0.0075  14  ASP   B CA  
4198 C  CA  B ASP   B 14  ? 0.2680 0.2373 0.3008 -0.0626 -0.0990 0.0121  14  ASP   B CA  
4199 C  C   A ASP   B 14  ? 0.2543 0.2185 0.2765 -0.0674 -0.0845 0.0151  14  ASP   B C   
4200 C  C   B ASP   B 14  ? 0.2552 0.2188 0.2702 -0.0641 -0.0862 0.0131  14  ASP   B C   
4201 O  O   A ASP   B 14  ? 0.2759 0.2298 0.2789 -0.0647 -0.0784 0.0285  14  ASP   B O   
4202 O  O   B ASP   B 14  ? 0.2766 0.2248 0.2746 -0.0602 -0.0845 0.0177  14  ASP   B O   
4203 C  CB  A ASP   B 14  ? 0.2855 0.2660 0.3816 -0.0641 -0.1073 0.0104  14  ASP   B CB  
4204 C  CB  B ASP   B 14  ? 0.2892 0.2692 0.3602 -0.0556 -0.1003 0.0210  14  ASP   B CB  
4205 C  CG  A ASP   B 14  ? 0.3060 0.2904 0.4445 -0.0626 -0.1012 0.0039  14  ASP   B CG  
4206 C  CG  B ASP   B 14  ? 0.3108 0.2955 0.4163 -0.0513 -0.0908 0.0167  14  ASP   B CG  
4207 O  OD1 A ASP   B 14  ? 0.3162 0.2968 0.4577 -0.0689 -0.0995 -0.0049 14  ASP   B OD1 
4208 O  OD1 B ASP   B 14  ? 0.3181 0.3063 0.4263 -0.0527 -0.0843 0.0108  14  ASP   B OD1 
4209 O  OD2 A ASP   B 14  ? 0.3106 0.3002 0.4775 -0.0616 -0.0947 0.0055  14  ASP   B OD2 
4210 O  OD2 B ASP   B 14  ? 0.3185 0.3043 0.4436 -0.0535 -0.0878 0.0163  14  ASP   B OD2 
4219 N  N   . ASN   B 15  ? 0.2240 0.1948 0.2437 -0.0568 -0.0792 0.0175  15  ASN   B N   
4220 C  CA  . ASN   B 15  ? 0.1835 0.1691 0.2206 -0.0352 -0.0475 0.0088  15  ASN   B CA  
4221 C  C   . ASN   B 15  ? 0.1663 0.1538 0.2085 -0.0203 -0.0428 -0.0044 15  ASN   B C   
4222 O  O   . ASN   B 15  ? 0.1651 0.1462 0.2356 -0.0230 -0.0469 -0.0154 15  ASN   B O   
4223 C  CB  . ASN   B 15  ? 0.1777 0.1680 0.2376 -0.0186 -0.0518 0.0122  15  ASN   B CB  
4224 C  CG  . ASN   B 15  ? 0.1615 0.1626 0.2479 -0.0252 -0.0271 0.0074  15  ASN   B CG  
4225 O  OD1 . ASN   B 15  ? 0.1686 0.1959 0.2741 -0.0419 -0.0276 0.0089  15  ASN   B OD1 
4226 N  ND2 . ASN   B 15  ? 0.1655 0.1438 0.2378 -0.0139 -0.0037 -0.0123 15  ASN   B ND2 
4234 N  N   . VAL   B 16  ? 0.1711 0.1414 0.2191 -0.0285 -0.0501 -0.0073 16  VAL   B N   
4235 C  CA  . VAL   B 16  ? 0.1682 0.1439 0.2149 -0.0257 -0.0367 -0.0189 16  VAL   B CA  
4236 C  C   . VAL   B 16  ? 0.1656 0.1495 0.2112 -0.0349 -0.0403 -0.0108 16  VAL   B C   
4237 O  O   . VAL   B 16  ? 0.1698 0.1628 0.2382 -0.0279 -0.0372 -0.0246 16  VAL   B O   
4238 C  CB  . VAL   B 16  ? 0.1757 0.1433 0.2217 -0.0122 -0.0270 -0.0168 16  VAL   B CB  
4239 C  CG1 . VAL   B 16  ? 0.1846 0.1463 0.2146 0.0023  -0.0180 -0.0146 16  VAL   B CG1 
4240 C  CG2 . VAL   B 16  ? 0.1808 0.1516 0.2364 -0.0077 -0.0197 -0.0232 16  VAL   B CG2 
4250 N  N   . TYR   B 17  ? 0.1744 0.1638 0.2059 -0.0338 -0.0285 -0.0203 17  TYR   B N   
4251 C  CA  . TYR   B 17  ? 0.1837 0.1769 0.1919 -0.0372 -0.0274 -0.0025 17  TYR   B CA  
4252 C  C   . TYR   B 17  ? 0.1727 0.1494 0.1859 -0.0362 -0.0187 -0.0097 17  TYR   B C   
4253 O  O   . TYR   B 17  ? 0.1756 0.1583 0.2033 -0.0317 -0.0362 -0.0277 17  TYR   B O   
4254 C  CB  . TYR   B 17  ? 0.2106 0.2191 0.2079 -0.0269 -0.0274 0.0268  17  TYR   B CB  
4255 C  CG  . TYR   B 17  ? 0.2375 0.2637 0.2412 -0.0208 -0.0381 0.0360  17  TYR   B CG  
4256 C  CD1 . TYR   B 17  ? 0.2546 0.2767 0.2558 -0.0142 -0.0510 0.0474  17  TYR   B CD1 
4257 C  CD2 . TYR   B 17  ? 0.2623 0.2931 0.2561 -0.0101 -0.0459 0.0358  17  TYR   B CD2 
4258 C  CE1 . TYR   B 17  ? 0.2755 0.3023 0.2714 -0.0020 -0.0591 0.0421  17  TYR   B CE1 
4259 C  CE2 . TYR   B 17  ? 0.2812 0.3135 0.2756 0.0036  -0.0592 0.0415  17  TYR   B CE2 
4260 C  CZ  . TYR   B 17  ? 0.2905 0.3209 0.2797 0.0093  -0.0678 0.0449  17  TYR   B CZ  
4261 O  OH  . TYR   B 17  ? 0.3073 0.3412 0.3043 0.0211  -0.0721 0.0454  17  TYR   B OH  
4271 N  N   . ILE   B 18  ? 0.1805 0.1536 0.1754 -0.0284 -0.0119 -0.0192 18  ILE   B N   
4272 C  CA  . ILE   B 18  ? 0.1801 0.1532 0.1856 -0.0336 -0.0093 -0.0221 18  ILE   B CA  
4273 C  C   . ILE   B 18  ? 0.1971 0.1546 0.1800 -0.0382 -0.0060 -0.0305 18  ILE   B C   
4274 O  O   . ILE   B 18  ? 0.2222 0.1689 0.1853 -0.0338 0.0057  -0.0311 18  ILE   B O   
4275 C  CB  . ILE   B 18  ? 0.1866 0.1565 0.1955 -0.0441 -0.0097 -0.0156 18  ILE   B CB  
4276 C  CG1 . ILE   B 18  ? 0.1944 0.1591 0.2059 -0.0413 -0.0003 -0.0074 18  ILE   B CG1 
4277 C  CG2 . ILE   B 18  ? 0.1948 0.1639 0.1996 -0.0492 -0.0138 -0.0173 18  ILE   B CG2 
4278 C  CD1 . ILE   B 18  ? 0.2080 0.1847 0.2288 -0.0392 -0.0213 0.0170  18  ILE   B CD1 
4290 N  N   . LYS   B 19  ? 0.1914 0.1536 0.1956 -0.0208 0.0314  -0.0309 19  LYS   B N   
4291 C  CA  . LYS   B 19  ? 0.2007 0.1546 0.2190 -0.0242 0.0264  -0.0410 19  LYS   B CA  
4292 C  C   . LYS   B 19  ? 0.1883 0.1521 0.2303 -0.0203 0.0368  -0.0442 19  LYS   B C   
4293 O  O   . LYS   B 19  ? 0.1899 0.1605 0.2104 -0.0134 0.0197  -0.0386 19  LYS   B O   
4294 C  CB  . LYS   B 19  ? 0.2270 0.1790 0.2161 -0.0278 0.0350  -0.0308 19  LYS   B CB  
4295 C  CG  . LYS   B 19  ? 0.2562 0.1981 0.2423 -0.0335 0.0460  -0.0353 19  LYS   B CG  
4296 C  CD  . LYS   B 19  ? 0.2867 0.2329 0.2571 -0.0367 0.0560  -0.0269 19  LYS   B CD  
4297 C  CE  . LYS   B 19  ? 0.3156 0.2614 0.2738 -0.0387 0.0528  -0.0309 19  LYS   B CE  
4298 N  NZ  . LYS   B 19  ? 0.3332 0.2781 0.2856 -0.0451 0.0541  -0.0269 19  LYS   B NZ  
4312 N  N   . ASN   B 20  ? 0.1857 0.1636 0.2671 -0.0104 0.0355  -0.0568 20  ASN   B N   
4313 C  CA  . ASN   B 20  ? 0.1861 0.1765 0.2832 -0.0098 0.0375  -0.0668 20  ASN   B CA  
4314 C  C   . ASN   B 20  ? 0.1834 0.1936 0.2870 -0.0184 0.0446  -0.0770 20  ASN   B C   
4315 O  O   . ASN   B 20  ? 0.2058 0.2289 0.3051 -0.0309 0.0501  -0.0760 20  ASN   B O   
4316 C  CB  . ASN   B 20  ? 0.2185 0.1782 0.3059 0.0100  0.0270  -0.0676 20  ASN   B CB  
4317 C  CG  . ASN   B 20  ? 0.2454 0.1855 0.3183 0.0351  0.0255  -0.0745 20  ASN   B CG  
4318 O  OD1 . ASN   B 20  ? 0.2750 0.2229 0.3427 0.0522  0.0219  -0.0771 20  ASN   B OD1 
4319 N  ND2 . ASN   B 20  ? 0.2387 0.1876 0.3109 0.0369  0.0155  -0.0694 20  ASN   B ND2 
4326 N  N   . ALA   B 21  ? 0.1900 0.1789 0.2754 -0.0263 0.0464  -0.0640 21  ALA   B N   
4327 C  CA  . ALA   B 21  ? 0.1996 0.1871 0.2922 -0.0280 0.0323  -0.0452 21  ALA   B CA  
4328 C  C   . ALA   B 21  ? 0.1981 0.1634 0.2735 -0.0236 0.0379  -0.0316 21  ALA   B C   
4329 O  O   . ALA   B 21  ? 0.2024 0.1550 0.2706 -0.0318 0.0377  -0.0243 21  ALA   B O   
4330 C  CB  . ALA   B 21  ? 0.2110 0.2166 0.2970 -0.0387 0.0269  -0.0350 21  ALA   B CB  
4336 N  N   . ASP   B 22  ? 0.1912 0.1571 0.2577 -0.0206 0.0314  -0.0246 22  ASP   B N   
4337 C  CA  . ASP   B 22  ? 0.1853 0.1450 0.2462 -0.0107 0.0196  -0.0201 22  ASP   B CA  
4338 C  C   . ASP   B 22  ? 0.1762 0.1468 0.2072 -0.0153 0.0183  -0.0066 22  ASP   B C   
4339 O  O   . ASP   B 22  ? 0.1799 0.1482 0.2224 -0.0106 0.0119  -0.0029 22  ASP   B O   
4340 C  CB  . ASP   B 22  ? 0.1948 0.1519 0.2904 -0.0087 0.0265  -0.0080 22  ASP   B CB  
4341 C  CG  . ASP   B 22  ? 0.1927 0.1737 0.3368 -0.0003 -0.0006 -0.0084 22  ASP   B CG  
4342 O  OD1 . ASP   B 22  ? 0.2127 0.1709 0.3321 0.0029  -0.0266 -0.0050 22  ASP   B OD1 
4343 O  OD2 . ASP   B 22  ? 0.1979 0.2023 0.3957 0.0086  -0.0194 -0.0234 22  ASP   B OD2 
4348 N  N   . ILE   B 23  ? 0.1830 0.1441 0.1909 -0.0098 0.0046  0.0087  23  ILE   B N   
4349 C  CA  . ILE   B 23  ? 0.1679 0.1428 0.1796 -0.0084 -0.0051 0.0036  23  ILE   B CA  
4350 C  C   . ILE   B 23  ? 0.1598 0.1433 0.1734 -0.0017 -0.0086 0.0020  23  ILE   B C   
4351 O  O   . ILE   B 23  ? 0.1578 0.1436 0.1722 -0.0065 -0.0102 0.0054  23  ILE   B O   
4352 C  CB  . ILE   B 23  ? 0.1639 0.1482 0.1926 -0.0176 -0.0021 0.0142  23  ILE   B CB  
4353 C  CG1 . ILE   B 23  ? 0.1677 0.1575 0.2061 -0.0124 0.0035  0.0227  23  ILE   B CG1 
4354 C  CG2 . ILE   B 23  ? 0.1745 0.1703 0.2048 -0.0250 -0.0040 0.0064  23  ILE   B CG2 
4355 C  CD1 . ILE   B 23  ? 0.1742 0.1682 0.2091 -0.0076 0.0071  0.0144  23  ILE   B CD1 
4367 N  N   . VAL   B 24  ? 0.1632 0.1490 0.1819 -0.0091 -0.0030 0.0003  24  VAL   B N   
4368 C  CA  . VAL   B 24  ? 0.1610 0.1498 0.2098 -0.0052 -0.0117 -0.0008 24  VAL   B CA  
4369 C  C   . VAL   B 24  ? 0.1568 0.1492 0.2197 -0.0142 -0.0093 -0.0002 24  VAL   B C   
4370 O  O   . VAL   B 24  ? 0.1583 0.1572 0.2292 -0.0197 -0.0084 0.0061  24  VAL   B O   
4371 C  CB  . VAL   B 24  ? 0.1721 0.1676 0.2158 0.0034  -0.0224 -0.0041 24  VAL   B CB  
4372 C  CG1 . VAL   B 24  ? 0.1728 0.1698 0.2257 -0.0065 -0.0237 -0.0083 24  VAL   B CG1 
4373 C  CG2 . VAL   B 24  ? 0.1785 0.1994 0.2215 0.0050  -0.0248 -0.0085 24  VAL   B CG2 
4383 N  N   . GLU   B 25  ? 0.1793 0.1583 0.2158 -0.0138 -0.0026 0.0074  25  GLU   B N   
4384 C  CA  . GLU   B 25  ? 0.1932 0.1912 0.2243 0.0012  0.0083  0.0042  25  GLU   B CA  
4385 C  C   . GLU   B 25  ? 0.1869 0.1852 0.1907 -0.0132 0.0122  0.0100  25  GLU   B C   
4386 O  O   . GLU   B 25  ? 0.1886 0.2035 0.2079 -0.0092 0.0206  0.0119  25  GLU   B O   
4387 C  CB  . GLU   B 25  ? 0.2319 0.2398 0.2971 0.0261  0.0187  0.0064  25  GLU   B CB  
4388 C  CG  . GLU   B 25  ? 0.2705 0.3107 0.4032 0.0381  0.0154  -0.0060 25  GLU   B CG  
4389 C  CD  . GLU   B 25  ? 0.3092 0.3706 0.4957 0.0363  0.0103  -0.0147 25  GLU   B CD  
4390 O  OE1 . GLU   B 25  ? 0.3254 0.3928 0.5275 0.0402  0.0146  -0.0158 25  GLU   B OE1 
4391 O  OE2 . GLU   B 25  ? 0.3233 0.3889 0.5340 0.0329  0.0059  -0.0240 25  GLU   B OE2 
4398 N  N   A GLU   B 26  ? 0.1839 0.1738 0.1682 -0.0281 0.0085  0.0009  26  GLU   B N   
4399 N  N   B GLU   B 26  ? 0.1827 0.1797 0.1808 -0.0234 0.0101  0.0104  26  GLU   B N   
4400 C  CA  A GLU   B 26  ? 0.1834 0.1800 0.1779 -0.0348 -0.0055 -0.0035 26  GLU   B CA  
4401 C  CA  B GLU   B 26  ? 0.1802 0.1895 0.2037 -0.0273 -0.0008 0.0131  26  GLU   B CA  
4402 C  C   A GLU   B 26  ? 0.1690 0.1809 0.1797 -0.0276 0.0009  0.0110  26  GLU   B C   
4403 C  C   B GLU   B 26  ? 0.1677 0.1857 0.1896 -0.0236 0.0037  0.0195  26  GLU   B C   
4404 O  O   A GLU   B 26  ? 0.1868 0.1960 0.1863 -0.0248 -0.0047 0.0181  26  GLU   B O   
4405 O  O   B GLU   B 26  ? 0.1858 0.2003 0.1922 -0.0207 -0.0011 0.0271  26  GLU   B O   
4406 C  CB  A GLU   B 26  ? 0.2080 0.1906 0.1872 -0.0426 -0.0063 -0.0019 26  GLU   B CB  
4407 C  CB  B GLU   B 26  ? 0.1996 0.2071 0.2416 -0.0310 0.0014  0.0265  26  GLU   B CB  
4408 C  CG  A GLU   B 26  ? 0.2393 0.2006 0.2122 -0.0426 0.0000  -0.0108 26  GLU   B CG  
4409 C  CG  B GLU   B 26  ? 0.2230 0.2268 0.2920 -0.0274 0.0101  0.0256  26  GLU   B CG  
4410 C  CD  A GLU   B 26  ? 0.2587 0.2033 0.2133 -0.0494 0.0184  -0.0213 26  GLU   B CD  
4411 C  CD  B GLU   B 26  ? 0.2280 0.2312 0.3159 -0.0316 0.0247  0.0228  26  GLU   B CD  
4412 O  OE1 A GLU   B 26  ? 0.2629 0.1932 0.1950 -0.0448 0.0462  -0.0239 26  GLU   B OE1 
4413 O  OE1 B GLU   B 26  ? 0.2311 0.2311 0.3438 -0.0435 0.0467  0.0124  26  GLU   B OE1 
4414 O  OE2 A GLU   B 26  ? 0.2681 0.2218 0.2347 -0.0531 0.0220  0.0025  26  GLU   B OE2 
4415 O  OE2 B GLU   B 26  ? 0.2227 0.2301 0.3102 -0.0208 0.0275  0.0131  26  GLU   B OE2 
4428 N  N   . ALA   B 27  ? 0.1485 0.1693 0.1868 -0.0216 0.0064  0.0165  27  ALA   B N   
4429 C  CA  . ALA   B 27  ? 0.1552 0.1631 0.2051 -0.0147 -0.0056 0.0274  27  ALA   B CA  
4430 C  C   . ALA   B 27  ? 0.1606 0.1708 0.2275 -0.0135 0.0102  0.0357  27  ALA   B C   
4431 O  O   . ALA   B 27  ? 0.1706 0.1784 0.2310 -0.0051 0.0068  0.0476  27  ALA   B O   
4432 C  CB  . ALA   B 27  ? 0.1732 0.1510 0.1972 -0.0165 -0.0047 0.0198  27  ALA   B CB  
4439 N  N   . LYS   B 28  ? 0.1595 0.1918 0.2663 -0.0201 0.0242  0.0577  28  LYS   B N   
4440 C  CA  . LYS   B 28  ? 0.1704 0.2356 0.2862 -0.0134 0.0509  0.0840  28  LYS   B CA  
4441 C  C   . LYS   B 28  ? 0.2006 0.2596 0.2634 -0.0015 0.0623  0.0790  28  LYS   B C   
4442 O  O   . LYS   B 28  ? 0.2235 0.2639 0.2783 -0.0024 0.0632  0.0747  28  LYS   B O   
4443 C  CB  . LYS   B 28  ? 0.1856 0.2691 0.3352 -0.0043 0.0597  0.1028  28  LYS   B CB  
4444 C  CG  . LYS   B 28  ? 0.2067 0.3103 0.3723 0.0117  0.0514  0.1130  28  LYS   B CG  
4445 C  CD  . LYS   B 28  ? 0.2438 0.3668 0.4311 0.0231  0.0602  0.1086  28  LYS   B CD  
4446 C  CE  . LYS   B 28  ? 0.2742 0.4056 0.4754 0.0357  0.0628  0.1107  28  LYS   B CE  
4447 N  NZ  . LYS   B 28  ? 0.2776 0.4139 0.4929 0.0453  0.0610  0.1176  28  LYS   B NZ  
4461 N  N   A LYS   B 29  ? 0.2216 0.2787 0.2654 0.0124  0.0566  0.0690  29  LYS   B N   
4462 N  N   B LYS   B 29  ? 0.2210 0.2786 0.2641 0.0114  0.0564  0.0696  29  LYS   B N   
4463 C  CA  A LYS   B 29  ? 0.2557 0.3037 0.2877 0.0142  0.0530  0.0625  29  LYS   B CA  
4464 C  CA  B LYS   B 29  ? 0.2544 0.3036 0.2855 0.0123  0.0527  0.0637  29  LYS   B CA  
4465 C  C   A LYS   B 29  ? 0.2508 0.3039 0.2515 0.0151  0.0468  0.0733  29  LYS   B C   
4466 C  C   B LYS   B 29  ? 0.2491 0.3043 0.2489 0.0129  0.0453  0.0739  29  LYS   B C   
4467 O  O   A LYS   B 29  ? 0.2660 0.3168 0.2570 0.0210  0.0421  0.0754  29  LYS   B O   
4468 O  O   B LYS   B 29  ? 0.2626 0.3185 0.2540 0.0170  0.0376  0.0749  29  LYS   B O   
4469 C  CB  A LYS   B 29  ? 0.2975 0.3308 0.3567 0.0115  0.0494  0.0456  29  LYS   B CB  
4470 C  CB  B LYS   B 29  ? 0.2960 0.3303 0.3540 0.0092  0.0499  0.0482  29  LYS   B CB  
4471 C  CG  A LYS   B 29  ? 0.3308 0.3536 0.4270 0.0071  0.0503  0.0357  29  LYS   B CG  
4472 C  CG  B LYS   B 29  ? 0.3292 0.3524 0.4230 0.0044  0.0524  0.0400  29  LYS   B CG  
4473 C  CD  A LYS   B 29  ? 0.3573 0.3695 0.4845 0.0023  0.0550  0.0256  29  LYS   B CD  
4474 C  CD  B LYS   B 29  ? 0.3552 0.3679 0.4796 -0.0004 0.0564  0.0308  29  LYS   B CD  
4475 C  CE  A LYS   B 29  ? 0.3758 0.3797 0.5252 -0.0010 0.0592  0.0185  29  LYS   B CE  
4476 C  CE  B LYS   B 29  ? 0.3734 0.3778 0.5191 -0.0038 0.0612  0.0248  29  LYS   B CE  
4477 N  NZ  A LYS   B 29  ? 0.3862 0.3852 0.5512 -0.0026 0.0607  0.0147  29  LYS   B NZ  
4478 N  NZ  B LYS   B 29  ? 0.3833 0.3833 0.5445 -0.0047 0.0627  0.0215  29  LYS   B NZ  
4505 N  N   . VAL   B 30  ? 0.2294 0.2915 0.2331 0.0057  0.0425  0.0749  30  VAL   B N   
4506 C  CA  . VAL   B 30  ? 0.2128 0.2749 0.2673 -0.0072 -0.0005 0.0804  30  VAL   B CA  
4507 C  C   . VAL   B 30  ? 0.1902 0.2641 0.2627 -0.0081 0.0049  0.0984  30  VAL   B C   
4508 O  O   . VAL   B 30  ? 0.1987 0.2827 0.2650 -0.0011 0.0131  0.1086  30  VAL   B O   
4509 C  CB  . VAL   B 30  ? 0.2181 0.2685 0.3145 -0.0241 -0.0376 0.0691  30  VAL   B CB  
4510 C  CG1 . VAL   B 30  ? 0.2205 0.2740 0.3122 -0.0280 -0.0313 0.0619  30  VAL   B CG1 
4511 C  CG2 . VAL   B 30  ? 0.2273 0.2707 0.3346 -0.0288 -0.0518 0.0557  30  VAL   B CG2 
4522 N  N   . LYS   B 31  ? 0.1772 0.2254 0.3021 -0.0236 0.0038  0.1023  31  LYS   B N   
4523 C  CA  . LYS   B 31  ? 0.1643 0.2173 0.3364 -0.0332 -0.0050 0.1078  31  LYS   B CA  
4524 C  C   . LYS   B 31  ? 0.1558 0.1810 0.2933 -0.0340 -0.0251 0.0867  31  LYS   B C   
4525 O  O   . LYS   B 31  ? 0.1650 0.2011 0.3074 -0.0233 -0.0200 0.1068  31  LYS   B O   
4526 C  CB  . LYS   B 31  ? 0.1787 0.2664 0.3998 -0.0288 0.0195  0.1204  31  LYS   B CB  
4527 C  CG  . LYS   B 31  ? 0.2106 0.3129 0.4479 -0.0280 0.0372  0.1193  31  LYS   B CG  
4528 C  CD  . LYS   B 31  ? 0.2423 0.3590 0.4838 -0.0206 0.0364  0.1107  31  LYS   B CD  
4529 C  CE  . LYS   B 31  ? 0.2638 0.3856 0.5218 -0.0169 0.0275  0.0969  31  LYS   B CE  
4530 N  NZ  . LYS   B 31  ? 0.2787 0.4040 0.5372 -0.0072 0.0127  0.0828  31  LYS   B NZ  
4544 N  N   . PRO   B 32  ? 0.1672 0.1578 0.2271 -0.0327 -0.0401 0.0467  32  PRO   B N   
4545 C  CA  . PRO   B 32  ? 0.1767 0.1542 0.1835 -0.0355 -0.0407 0.0341  32  PRO   B CA  
4546 C  C   . PRO   B 32  ? 0.1893 0.1416 0.1918 -0.0382 -0.0499 0.0308  32  PRO   B C   
4547 O  O   . PRO   B 32  ? 0.2052 0.1480 0.2208 -0.0381 -0.0720 0.0343  32  PRO   B O   
4548 C  CB  . PRO   B 32  ? 0.1968 0.1549 0.1708 -0.0411 -0.0337 0.0130  32  PRO   B CB  
4549 C  CG  . PRO   B 32  ? 0.2129 0.1461 0.1823 -0.0307 -0.0533 0.0231  32  PRO   B CG  
4550 C  CD  . PRO   B 32  ? 0.1973 0.1441 0.2088 -0.0207 -0.0539 0.0315  32  PRO   B CD  
4558 N  N   . THR   B 33  ? 0.1914 0.1378 0.1731 -0.0302 -0.0459 0.0216  33  THR   B N   
4559 C  CA  . THR   B 33  ? 0.2009 0.1440 0.1746 -0.0324 -0.0464 0.0254  33  THR   B CA  
4560 C  C   . THR   B 33  ? 0.2010 0.1356 0.1624 -0.0358 -0.0482 0.0193  33  THR   B C   
4561 O  O   . THR   B 33  ? 0.2236 0.1404 0.1737 -0.0439 -0.0562 0.0196  33  THR   B O   
4562 C  CB  . THR   B 33  ? 0.2104 0.1505 0.1771 -0.0163 -0.0551 0.0364  33  THR   B CB  
4563 O  OG1 . THR   B 33  ? 0.1984 0.1583 0.1788 -0.0197 -0.0519 0.0379  33  THR   B OG1 
4564 C  CG2 . THR   B 33  ? 0.2357 0.1614 0.1921 -0.0070 -0.0510 0.0273  33  THR   B CG2 
4572 N  N   . VAL   B 34  ? 0.1868 0.1311 0.1553 -0.0370 -0.0400 0.0139  34  VAL   B N   
4573 C  CA  . VAL   B 34  ? 0.1721 0.1289 0.1574 -0.0284 -0.0344 0.0096  34  VAL   B CA  
4574 C  C   . VAL   B 34  ? 0.1552 0.1263 0.1312 -0.0286 -0.0232 0.0061  34  VAL   B C   
4575 O  O   . VAL   B 34  ? 0.1747 0.1292 0.1419 -0.0240 -0.0348 0.0057  34  VAL   B O   
4576 C  CB  . VAL   B 34  ? 0.1706 0.1392 0.1899 -0.0111 -0.0324 -0.0009 34  VAL   B CB  
4577 C  CG1 . VAL   B 34  ? 0.1649 0.1600 0.1908 -0.0101 -0.0147 -0.0070 34  VAL   B CG1 
4578 C  CG2 . VAL   B 34  ? 0.1774 0.1440 0.2190 -0.0101 -0.0352 -0.0026 34  VAL   B CG2 
4588 N  N   . VAL   B 35  ? 0.1476 0.1211 0.1332 -0.0260 -0.0136 0.0055  35  VAL   B N   
4589 C  CA  . VAL   B 35  ? 0.1454 0.1194 0.1343 -0.0221 -0.0107 0.0045  35  VAL   B CA  
4590 C  C   . VAL   B 35  ? 0.1336 0.1170 0.1275 -0.0184 -0.0092 0.0101  35  VAL   B C   
4591 O  O   . VAL   B 35  ? 0.1367 0.1250 0.1360 -0.0242 -0.0022 -0.0044 35  VAL   B O   
4592 C  CB  . VAL   B 35  ? 0.1374 0.1377 0.1413 -0.0174 0.0002  0.0078  35  VAL   B CB  
4593 C  CG1 . VAL   B 35  ? 0.1333 0.1575 0.1646 -0.0256 0.0011  0.0008  35  VAL   B CG1 
4594 C  CG2 . VAL   B 35  ? 0.1375 0.1438 0.1631 -0.0075 -0.0043 0.0046  35  VAL   B CG2 
4604 N  N   . VAL   B 36  ? 0.1385 0.1197 0.1343 -0.0168 -0.0161 0.0076  36  VAL   B N   
4605 C  CA  . VAL   B 36  ? 0.1316 0.1153 0.1300 -0.0096 -0.0026 0.0071  36  VAL   B CA  
4606 C  C   . VAL   B 36  ? 0.1253 0.1204 0.1256 -0.0086 -0.0013 -0.0004 36  VAL   B C   
4607 O  O   . VAL   B 36  ? 0.1337 0.1288 0.1527 -0.0117 -0.0029 -0.0062 36  VAL   B O   
4608 C  CB  . VAL   B 36  ? 0.1301 0.1209 0.1467 -0.0156 -0.0030 0.0022  36  VAL   B CB  
4609 C  CG1 . VAL   B 36  ? 0.1309 0.1321 0.1614 -0.0171 0.0010  0.0022  36  VAL   B CG1 
4610 C  CG2 . VAL   B 36  ? 0.1339 0.1267 0.1632 -0.0144 -0.0142 0.0096  36  VAL   B CG2 
4620 N  N   . ASN   B 37  ? 0.1341 0.1226 0.1290 -0.0000 -0.0069 0.0058  37  ASN   B N   
4621 C  CA  . ASN   B 37  ? 0.1307 0.1240 0.1402 0.0025  -0.0113 0.0059  37  ASN   B CA  
4622 C  C   . ASN   B 37  ? 0.1301 0.1243 0.1386 0.0036  -0.0105 0.0001  37  ASN   B C   
4623 O  O   . ASN   B 37  ? 0.1389 0.1301 0.1353 -0.0004 -0.0003 0.0074  37  ASN   B O   
4624 C  CB  . ASN   B 37  ? 0.1312 0.1321 0.1405 0.0056  -0.0111 0.0028  37  ASN   B CB  
4625 C  CG  . ASN   B 37  ? 0.1313 0.1293 0.1433 0.0015  -0.0119 0.0009  37  ASN   B CG  
4626 O  OD1 . ASN   B 37  ? 0.1369 0.1370 0.1536 0.0075  -0.0051 0.0012  37  ASN   B OD1 
4627 N  ND2 . ASN   B 37  ? 0.1379 0.1246 0.1494 -0.0011 -0.0157 0.0056  37  ASN   B ND2 
4634 N  N   . ALA   B 38  ? 0.1393 0.1230 0.1333 0.0059  0.0002  0.0014  38  ALA   B N   
4635 C  CA  . ALA   B 38  ? 0.1509 0.1248 0.1364 0.0010  0.0073  0.0094  38  ALA   B CA  
4636 C  C   . ALA   B 38  ? 0.1431 0.1228 0.1399 -0.0015 0.0067  0.0097  38  ALA   B C   
4637 O  O   . ALA   B 38  ? 0.1527 0.1319 0.1582 0.0068  0.0038  0.0104  38  ALA   B O   
4638 C  CB  . ALA   B 38  ? 0.1725 0.1319 0.1500 -0.0077 0.0150  0.0040  38  ALA   B CB  
4644 N  N   . ALA   B 39  ? 0.1424 0.1276 0.1341 0.0049  -0.0022 0.0027  39  ALA   B N   
4645 C  CA  . ALA   B 39  ? 0.1553 0.1316 0.1288 0.0080  -0.0096 0.0081  39  ALA   B CA  
4646 C  C   . ALA   B 39  ? 0.1553 0.1374 0.1280 0.0058  -0.0057 0.0073  39  ALA   B C   
4647 O  O   . ALA   B 39  ? 0.1585 0.1440 0.1498 0.0013  -0.0000 0.0122  39  ALA   B O   
4648 C  CB  . ALA   B 39  ? 0.1558 0.1386 0.1521 -0.0042 0.0015  0.0048  39  ALA   B CB  
4654 N  N   . ASN   B 40  ? 0.1620 0.1571 0.1399 -0.0045 0.0005  -0.0017 40  ASN   B N   
4655 C  CA  . ASN   B 40  ? 0.1633 0.1646 0.1466 -0.0011 -0.0034 -0.0007 40  ASN   B CA  
4656 C  C   . ASN   B 40  ? 0.1660 0.1635 0.1217 0.0049  -0.0067 0.0035  40  ASN   B C   
4657 O  O   . ASN   B 40  ? 0.1664 0.1571 0.1330 0.0078  -0.0116 0.0063  40  ASN   B O   
4658 C  CB  . ASN   B 40  ? 0.1770 0.1660 0.1647 0.0061  -0.0108 0.0141  40  ASN   B CB  
4659 C  CG  . ASN   B 40  ? 0.1781 0.1726 0.1941 0.0021  -0.0224 0.0136  40  ASN   B CG  
4660 O  OD1 . ASN   B 40  ? 0.1772 0.1701 0.2696 -0.0007 -0.0355 0.0182  40  ASN   B OD1 
4661 N  ND2 . ASN   B 40  ? 0.1860 0.1727 0.1854 0.0049  -0.0205 0.0147  40  ASN   B ND2 
4668 N  N   . VAL   B 41  ? 0.1752 0.1686 0.1272 0.0089  0.0032  0.0010  41  VAL   B N   
4669 C  CA  . VAL   B 41  ? 0.1823 0.1818 0.1394 0.0095  0.0001  -0.0080 41  VAL   B CA  
4670 C  C   . VAL   B 41  ? 0.1771 0.1796 0.1352 0.0196  -0.0062 -0.0095 41  VAL   B C   
4671 O  O   . VAL   B 41  ? 0.1767 0.1744 0.1508 0.0130  -0.0091 -0.0110 41  VAL   B O   
4672 C  CB  . VAL   B 41  ? 0.1967 0.1977 0.1621 -0.0050 0.0220  -0.0196 41  VAL   B CB  
4673 C  CG1 . VAL   B 41  ? 0.1923 0.1999 0.1858 -0.0127 0.0334  -0.0234 41  VAL   B CG1 
4674 C  CG2 . VAL   B 41  ? 0.2085 0.2192 0.1727 -0.0110 0.0268  -0.0253 41  VAL   B CG2 
4684 N  N   . TYR   B 42  ? 0.1862 0.1809 0.1390 0.0191  -0.0127 0.0016  42  TYR   B N   
4685 C  CA  . TYR   B 42  ? 0.1921 0.1882 0.1512 0.0180  -0.0272 -0.0119 42  TYR   B CA  
4686 C  C   . TYR   B 42  ? 0.1722 0.1634 0.1593 0.0223  -0.0269 -0.0162 42  TYR   B C   
4687 O  O   . TYR   B 42  ? 0.1764 0.1707 0.1929 0.0137  -0.0307 -0.0219 42  TYR   B O   
4688 C  CB  . TYR   B 42  ? 0.2151 0.2222 0.1780 0.0111  -0.0289 -0.0011 42  TYR   B CB  
4689 C  CG  . TYR   B 42  ? 0.2149 0.2414 0.1682 0.0013  -0.0297 0.0112  42  TYR   B CG  
4690 C  CD1 . TYR   B 42  ? 0.2062 0.2427 0.1440 -0.0025 -0.0156 0.0027  42  TYR   B CD1 
4691 C  CD2 . TYR   B 42  ? 0.2303 0.2579 0.2115 0.0012  -0.0189 0.0141  42  TYR   B CD2 
4692 C  CE1 . TYR   B 42  ? 0.2206 0.2614 0.1604 0.0010  -0.0115 0.0005  42  TYR   B CE1 
4693 C  CE2 . TYR   B 42  ? 0.2329 0.2651 0.2028 0.0047  0.0116  0.0297  42  TYR   B CE2 
4694 C  CZ  . TYR   B 42  ? 0.2421 0.2758 0.1877 0.0150  0.0106  0.0144  42  TYR   B CZ  
4695 O  OH  . TYR   B 42  ? 0.2783 0.2987 0.2337 0.0300  0.0212  0.0211  42  TYR   B OH  
4705 N  N   . LEU   B 43  ? 0.1599 0.1534 0.1414 0.0111  -0.0187 -0.0138 43  LEU   B N   
4706 C  CA  . LEU   B 43  ? 0.1596 0.1576 0.1350 0.0121  -0.0155 -0.0040 43  LEU   B CA  
4707 C  C   . LEU   B 43  ? 0.1674 0.1579 0.1463 0.0086  -0.0133 -0.0001 43  LEU   B C   
4708 O  O   . LEU   B 43  ? 0.1618 0.1624 0.1707 0.0058  -0.0200 0.0074  43  LEU   B O   
4709 C  CB  . LEU   B 43  ? 0.1594 0.1493 0.1587 0.0025  -0.0274 -0.0083 43  LEU   B CB  
4710 C  CG  . LEU   B 43  ? 0.1647 0.1455 0.1611 0.0012  -0.0297 -0.0100 43  LEU   B CG  
4711 C  CD1 . LEU   B 43  ? 0.1755 0.1487 0.1891 0.0014  -0.0451 -0.0026 43  LEU   B CD1 
4712 C  CD2 . LEU   B 43  ? 0.1616 0.1473 0.1668 -0.0047 -0.0309 -0.0064 43  LEU   B CD2 
4724 N  N   . LYS   B 44  ? 0.1663 0.1517 0.1488 0.0111  -0.0100 -0.0075 44  LYS   B N   
4725 C  CA  . LYS   B 44  ? 0.1796 0.1626 0.1517 0.0134  -0.0169 0.0069  44  LYS   B CA  
4726 C  C   . LYS   B 44  ? 0.1636 0.1558 0.1450 0.0154  -0.0131 0.0016  44  LYS   B C   
4727 O  O   . LYS   B 44  ? 0.1857 0.1570 0.1780 0.0061  -0.0072 0.0040  44  LYS   B O   
4728 C  CB  . LYS   B 44  ? 0.2059 0.1865 0.1674 0.0153  -0.0295 0.0024  44  LYS   B CB  
4729 C  CG  . LYS   B 44  ? 0.2417 0.2145 0.2025 0.0118  -0.0557 0.0033  44  LYS   B CG  
4730 C  CD  . LYS   B 44  ? 0.2767 0.2342 0.2607 -0.0021 -0.0685 0.0022  44  LYS   B CD  
4731 C  CE  . LYS   B 44  ? 0.3111 0.2586 0.3075 -0.0086 -0.0735 0.0117  44  LYS   B CE  
4732 N  NZ  . LYS   B 44  ? 0.3252 0.2712 0.3349 -0.0047 -0.0830 0.0258  44  LYS   B NZ  
4746 N  N   . HIS   B 45  ? 0.1596 0.1600 0.1417 0.0080  -0.0135 0.0049  45  HIS   B N   
4747 C  CA  . HIS   B 45  ? 0.1699 0.1600 0.1493 0.0075  -0.0103 -0.0004 45  HIS   B CA  
4748 C  C   . HIS   B 45  ? 0.1952 0.1786 0.1795 0.0180  -0.0205 -0.0037 45  HIS   B C   
4749 O  O   . HIS   B 45  ? 0.2061 0.2076 0.2274 0.0455  0.0126  -0.0041 45  HIS   B O   
4750 C  CB  . HIS   B 45  ? 0.1557 0.1593 0.1466 -0.0005 -0.0078 0.0000  45  HIS   B CB  
4751 C  CG  . HIS   B 45  ? 0.1533 0.1522 0.1509 -0.0068 -0.0098 -0.0015 45  HIS   B CG  
4752 N  ND1 . HIS   B 45  ? 0.1620 0.1495 0.1551 -0.0007 -0.0243 -0.0048 45  HIS   B ND1 
4753 C  CD2 . HIS   B 45  ? 0.1652 0.1531 0.1705 -0.0096 -0.0197 -0.0037 45  HIS   B CD2 
4754 C  CE1 . HIS   B 45  ? 0.1688 0.1366 0.1446 -0.0037 -0.0292 -0.0095 45  HIS   B CE1 
4755 N  NE2 . HIS   B 45  ? 0.1717 0.1443 0.1588 0.0024  -0.0228 -0.0061 45  HIS   B NE2 
4763 N  N   A GLY   B 46  ? 0.2032 0.1790 0.2072 0.0201  -0.0398 0.0054  46  GLY   B N   
4764 N  N   B GLY   B 46  ? 0.2042 0.1829 0.1975 0.0214  -0.0412 0.0120  46  GLY   B N   
4765 C  CA  A GLY   B 46  ? 0.2133 0.1901 0.2524 0.0172  -0.0440 0.0087  46  GLY   B CA  
4766 C  CA  B GLY   B 46  ? 0.2155 0.1967 0.2335 0.0178  -0.0461 0.0191  46  GLY   B CA  
4767 C  C   A GLY   B 46  ? 0.2128 0.2017 0.2948 0.0240  -0.0380 0.0015  46  GLY   B C   
4768 C  C   B GLY   B 46  ? 0.2180 0.2116 0.2721 0.0222  -0.0396 0.0166  46  GLY   B C   
4769 O  O   A GLY   B 46  ? 0.2149 0.2069 0.3615 0.0321  -0.0263 -0.0137 46  GLY   B O   
4770 O  O   B GLY   B 46  ? 0.2250 0.2263 0.3037 0.0261  -0.0343 0.0268  46  GLY   B O   
4777 N  N   . GLY   B 47  ? 0.2154 0.2099 0.2734 0.0102  -0.0218 -0.0028 47  GLY   B N   
4778 C  CA  . GLY   B 47  ? 0.2049 0.1808 0.2291 0.0042  -0.0182 -0.0012 47  GLY   B CA  
4779 C  C   . GLY   B 47  ? 0.1815 0.1591 0.1934 0.0033  0.0016  -0.0011 47  GLY   B C   
4780 O  O   . GLY   B 47  ? 0.1879 0.1457 0.2007 0.0065  -0.0084 0.0048  47  GLY   B O   
4785 N  N   . GLY   B 48  ? 0.1660 0.1512 0.1803 0.0061  -0.0115 0.0138  48  GLY   B N   
4786 C  CA  . GLY   B 48  ? 0.1664 0.1470 0.1761 -0.0011 -0.0012 0.0099  48  GLY   B CA  
4787 C  C   . GLY   B 48  ? 0.1548 0.1414 0.1695 -0.0019 0.0026  -0.0009 48  GLY   B C   
4788 O  O   . GLY   B 48  ? 0.1455 0.1467 0.2007 0.0025  -0.0032 0.0079  48  GLY   B O   
4792 N  N   . VAL   B 49  ? 0.1536 0.1462 0.1618 0.0104  -0.0032 0.0061  49  VAL   B N   
4793 C  CA  . VAL   B 49  ? 0.1558 0.1508 0.1567 0.0090  -0.0146 -0.0083 49  VAL   B CA  
4794 C  C   . VAL   B 49  ? 0.1451 0.1444 0.1469 0.0113  -0.0018 0.0060  49  VAL   B C   
4795 O  O   . VAL   B 49  ? 0.1517 0.1499 0.1532 0.0075  -0.0023 0.0057  49  VAL   B O   
4796 C  CB  . VAL   B 49  ? 0.1560 0.1715 0.1866 -0.0002 -0.0215 -0.0046 49  VAL   B CB  
4797 C  CG1 . VAL   B 49  ? 0.1549 0.1732 0.1810 0.0122  -0.0257 0.0010  49  VAL   B CG1 
4798 C  CG2 . VAL   B 49  ? 0.1748 0.1861 0.2022 -0.0086 -0.0328 -0.0029 49  VAL   B CG2 
4808 N  N   . ALA   B 50  ? 0.1379 0.1384 0.1562 0.0008  -0.0006 0.0082  50  ALA   B N   
4809 C  CA  . ALA   B 50  ? 0.1401 0.1320 0.1569 0.0069  -0.0025 0.0076  50  ALA   B CA  
4810 C  C   . ALA   B 50  ? 0.1470 0.1406 0.1516 0.0041  -0.0058 0.0078  50  ALA   B C   
4811 O  O   . ALA   B 50  ? 0.1438 0.1427 0.1475 0.0065  -0.0018 0.0005  50  ALA   B O   
4812 C  CB  . ALA   B 50  ? 0.1464 0.1334 0.1569 -0.0027 -0.0015 0.0097  50  ALA   B CB  
4818 N  N   . GLY   B 51  ? 0.1446 0.1504 0.1643 0.0157  -0.0093 0.0134  51  GLY   B N   
4819 C  CA  . GLY   B 51  ? 0.1519 0.1553 0.1784 0.0186  -0.0086 0.0121  51  GLY   B CA  
4820 C  C   . GLY   B 51  ? 0.1503 0.1447 0.1807 0.0226  -0.0092 0.0095  51  GLY   B C   
4821 O  O   . GLY   B 51  ? 0.1549 0.1624 0.2015 0.0115  -0.0108 0.0057  51  GLY   B O   
4825 N  N   . ALA   B 52  ? 0.1469 0.1450 0.1730 0.0166  -0.0080 0.0185  52  ALA   B N   
4826 C  CA  . ALA   B 52  ? 0.1559 0.1497 0.1747 0.0162  -0.0018 0.0012  52  ALA   B CA  
4827 C  C   . ALA   B 52  ? 0.1453 0.1466 0.1573 0.0089  0.0027  -0.0016 52  ALA   B C   
4828 O  O   . ALA   B 52  ? 0.1496 0.1534 0.1750 0.0101  0.0033  0.0054  52  ALA   B O   
4829 C  CB  . ALA   B 52  ? 0.1720 0.1493 0.1863 0.0076  0.0032  0.0045  52  ALA   B CB  
4835 N  N   . LEU   B 53  ? 0.1363 0.1469 0.1468 0.0157  0.0021  0.0023  53  LEU   B N   
4836 C  CA  . LEU   B 53  ? 0.1371 0.1575 0.1488 0.0153  -0.0019 0.0061  53  LEU   B CA  
4837 C  C   . LEU   B 53  ? 0.1420 0.1445 0.1525 0.0143  0.0014  0.0095  53  LEU   B C   
4838 O  O   . LEU   B 53  ? 0.1512 0.1562 0.1670 0.0014  0.0052  0.0192  53  LEU   B O   
4839 C  CB  . LEU   B 53  ? 0.1425 0.1621 0.1669 0.0103  0.0069  0.0153  53  LEU   B CB  
4840 C  CG  . LEU   B 53  ? 0.1375 0.1768 0.1717 0.0052  0.0026  0.0210  53  LEU   B CG  
4841 C  CD1 . LEU   B 53  ? 0.1469 0.2001 0.2016 0.0164  -0.0007 0.0112  53  LEU   B CD1 
4842 C  CD2 . LEU   B 53  ? 0.1490 0.2051 0.1935 -0.0096 -0.0087 -0.0139 53  LEU   B CD2 
4854 N  N   . ASN   B 54  ? 0.1426 0.1399 0.1518 0.0058  -0.0002 0.0076  54  ASN   B N   
4855 C  CA  . ASN   B 54  ? 0.1454 0.1532 0.1683 0.0030  -0.0073 0.0012  54  ASN   B CA  
4856 C  C   . ASN   B 54  ? 0.1396 0.1535 0.1788 0.0019  -0.0007 0.0043  54  ASN   B C   
4857 O  O   . ASN   B 54  ? 0.1397 0.1615 0.1938 -0.0028 0.0059  0.0000  54  ASN   B O   
4858 C  CB  . ASN   B 54  ? 0.1541 0.1623 0.1759 0.0066  0.0069  0.0064  54  ASN   B CB  
4859 C  CG  . ASN   B 54  ? 0.1472 0.1713 0.1727 0.0042  -0.0033 0.0087  54  ASN   B CG  
4860 O  OD1 . ASN   B 54  ? 0.1455 0.1710 0.1789 0.0012  -0.0092 -0.0104 54  ASN   B OD1 
4861 N  ND2 . ASN   B 54  ? 0.1622 0.1946 0.2037 0.0052  -0.0176 0.0156  54  ASN   B ND2 
4868 N  N   . LYS   B 55  ? 0.1397 0.1575 0.1988 0.0102  0.0037  0.0030  55  LYS   B N   
4869 C  CA  . LYS   B 55  ? 0.1551 0.1760 0.2170 0.0218  0.0046  0.0040  55  LYS   B CA  
4870 C  C   . LYS   B 55  ? 0.1448 0.1691 0.2097 0.0169  0.0073  -0.0015 55  LYS   B C   
4871 O  O   . LYS   B 55  ? 0.1426 0.1880 0.2263 0.0143  0.0102  -0.0029 55  LYS   B O   
4872 C  CB  . LYS   B 55  ? 0.1675 0.1893 0.2514 0.0319  0.0171  0.0107  55  LYS   B CB  
4873 C  CG  . LYS   B 55  ? 0.2059 0.2162 0.3337 0.0390  0.0373  0.0240  55  LYS   B CG  
4874 C  CD  . LYS   B 55  ? 0.2404 0.2412 0.4042 0.0472  0.0521  0.0382  55  LYS   B CD  
4875 C  CE  . LYS   B 55  ? 0.2667 0.2592 0.4706 0.0462  0.0622  0.0463  55  LYS   B CE  
4876 N  NZ  . LYS   B 55  ? 0.2757 0.2725 0.5046 0.0428  0.0490  0.0544  55  LYS   B NZ  
4890 N  N   . ALA   B 56  ? 0.1412 0.1724 0.1964 0.0125  0.0011  -0.0097 56  ALA   B N   
4891 C  CA  . ALA   B 56  ? 0.1578 0.1934 0.1837 0.0047  0.0029  -0.0036 56  ALA   B CA  
4892 C  C   . ALA   B 56  ? 0.1607 0.1884 0.1730 0.0032  0.0186  0.0076  56  ALA   B C   
4893 O  O   . ALA   B 56  ? 0.1789 0.1943 0.1986 0.0072  0.0371  0.0118  56  ALA   B O   
4894 C  CB  . ALA   B 56  ? 0.1712 0.2184 0.1930 -0.0123 0.0042  -0.0053 56  ALA   B CB  
4900 N  N   . THR   B 57  ? 0.1550 0.1800 0.1818 0.0081  0.0194  0.0063  57  THR   B N   
4901 C  CA  . THR   B 57  ? 0.1571 0.1758 0.1830 0.0012  0.0268  0.0130  57  THR   B CA  
4902 C  C   . THR   B 57  ? 0.1566 0.1864 0.2092 -0.0023 0.0225  0.0102  57  THR   B C   
4903 O  O   . THR   B 57  ? 0.1634 0.1868 0.2219 -0.0156 0.0168  0.0093  57  THR   B O   
4904 C  CB  . THR   B 57  ? 0.1624 0.1613 0.1722 0.0015  0.0184  0.0173  57  THR   B CB  
4905 O  OG1 . THR   B 57  ? 0.1589 0.1576 0.1912 -0.0000 0.0192  0.0141  57  THR   B OG1 
4906 C  CG2 . THR   B 57  ? 0.1594 0.1661 0.1747 0.0037  0.0202  0.0114  57  THR   B CG2 
4914 N  N   . ASN   B 58  ? 0.1426 0.2063 0.2271 -0.0111 0.0052  -0.0095 58  ASN   B N   
4915 C  CA  . ASN   B 58  ? 0.1592 0.2501 0.2673 -0.0196 0.0333  -0.0022 58  ASN   B CA  
4916 C  C   . ASN   B 58  ? 0.1390 0.2247 0.2183 -0.0110 0.0031  -0.0052 58  ASN   B C   
4917 O  O   . ASN   B 58  ? 0.1508 0.2314 0.2266 -0.0166 0.0066  -0.0130 58  ASN   B O   
4918 C  CB  . ASN   B 58  ? 0.2453 0.3238 0.3925 -0.0370 0.0744  0.0093  58  ASN   B CB  
4919 C  CG  . ASN   B 58  ? 0.3511 0.3942 0.5454 -0.0428 0.0913  0.0392  58  ASN   B CG  
4920 O  OD1 . ASN   B 58  ? 0.3720 0.4180 0.6007 -0.0445 0.0936  0.0489  58  ASN   B OD1 
4921 N  ND2 . ASN   B 58  ? 0.4598 0.4598 0.5982 -0.0476 0.0980  0.0479  58  ASN   B ND2 
4928 N  N   . ASN   B 59  ? 0.1420 0.2121 0.2074 -0.0057 0.0017  0.0060  59  ASN   B N   
4929 C  CA  . ASN   B 59  ? 0.1438 0.2153 0.2113 -0.0062 -0.0111 0.0111  59  ASN   B CA  
4930 C  C   . ASN   B 59  ? 0.1400 0.2041 0.1983 -0.0120 -0.0147 -0.0028 59  ASN   B C   
4931 O  O   . ASN   B 59  ? 0.1481 0.1959 0.1990 -0.0183 -0.0113 -0.0047 59  ASN   B O   
4932 C  CB  . ASN   B 59  ? 0.1549 0.2350 0.2278 -0.0015 -0.0238 0.0102  59  ASN   B CB  
4933 C  CG  . ASN   B 59  ? 0.1633 0.2476 0.2401 0.0005  -0.0337 0.0049  59  ASN   B CG  
4934 O  OD1 . ASN   B 59  ? 0.1675 0.2526 0.2421 0.0026  -0.0214 0.0197  59  ASN   B OD1 
4935 N  ND2 . ASN   B 59  ? 0.1739 0.2556 0.2442 -0.0108 -0.0388 0.0004  59  ASN   B ND2 
4942 N  N   . ALA   B 60  ? 0.1431 0.1870 0.1994 -0.0128 0.0030  -0.0009 60  ALA   B N   
4943 C  CA  . ALA   B 60  ? 0.1571 0.1742 0.2049 -0.0209 0.0009  0.0073  60  ALA   B CA  
4944 C  C   . ALA   B 60  ? 0.1547 0.1593 0.1837 -0.0141 -0.0046 0.0113  60  ALA   B C   
4945 O  O   . ALA   B 60  ? 0.1573 0.1678 0.2004 -0.0172 -0.0033 -0.0042 60  ALA   B O   
4946 C  CB  . ALA   B 60  ? 0.1695 0.1780 0.2314 -0.0181 0.0097  0.0066  60  ALA   B CB  
4952 N  N   . MET   B 61  ? 0.1423 0.1561 0.1811 -0.0077 -0.0015 0.0124  61  MET   B N   
4953 C  CA  . MET   B 61  ? 0.1416 0.1460 0.1753 -0.0102 -0.0034 0.0045  61  MET   B CA  
4954 C  C   . MET   B 61  ? 0.1468 0.1456 0.1747 -0.0087 -0.0059 0.0065  61  MET   B C   
4955 O  O   . MET   B 61  ? 0.1457 0.1490 0.1683 -0.0016 -0.0067 -0.0095 61  MET   B O   
4956 C  CB  . MET   B 61  ? 0.1387 0.1535 0.1674 0.0004  0.0004  0.0007  61  MET   B CB  
4957 C  CG  . MET   B 61  ? 0.1410 0.1511 0.1636 -0.0004 -0.0036 -0.0008 61  MET   B CG  
4958 S  SD  . MET   B 61  ? 0.1388 0.1542 0.1850 -0.0032 -0.0036 -0.0061 61  MET   B SD  
4959 C  CE  . MET   B 61  ? 0.1490 0.1792 0.2101 -0.0049 -0.0028 -0.0170 61  MET   B CE  
4969 N  N   . GLN   B 62  ? 0.1463 0.1506 0.1639 -0.0056 -0.0155 0.0083  62  GLN   B N   
4970 C  CA  . GLN   B 62  ? 0.1491 0.1580 0.1683 -0.0043 -0.0175 0.0019  62  GLN   B CA  
4971 C  C   . GLN   B 62  ? 0.1472 0.1648 0.1774 -0.0012 -0.0296 -0.0076 62  GLN   B C   
4972 O  O   . GLN   B 62  ? 0.1636 0.1620 0.1803 -0.0005 -0.0280 -0.0168 62  GLN   B O   
4973 C  CB  . GLN   B 62  ? 0.1509 0.1628 0.1720 0.0018  -0.0141 0.0042  62  GLN   B CB  
4974 C  CG  . GLN   B 62  ? 0.1520 0.1672 0.1815 0.0033  -0.0240 -0.0032 62  GLN   B CG  
4975 C  CD  . GLN   B 62  ? 0.1566 0.1610 0.1688 0.0068  -0.0264 0.0109  62  GLN   B CD  
4976 O  OE1 . GLN   B 62  ? 0.1598 0.1618 0.1759 0.0061  -0.0304 -0.0010 62  GLN   B OE1 
4977 N  NE2 . GLN   B 62  ? 0.1563 0.1691 0.1812 0.0003  -0.0189 -0.0095 62  GLN   B NE2 
4986 N  N   . VAL   B 63  ? 0.1507 0.1677 0.1987 -0.0116 -0.0195 -0.0116 63  VAL   B N   
4987 C  CA  . VAL   B 63  ? 0.1587 0.1718 0.2131 -0.0135 -0.0287 -0.0089 63  VAL   B CA  
4988 C  C   . VAL   B 63  ? 0.1624 0.1604 0.2014 -0.0146 -0.0264 -0.0169 63  VAL   B C   
4989 O  O   . VAL   B 63  ? 0.1692 0.1565 0.2190 -0.0115 -0.0392 -0.0092 63  VAL   B O   
4990 C  CB  . VAL   B 63  ? 0.1582 0.1873 0.2508 -0.0171 -0.0247 -0.0090 63  VAL   B CB  
4991 C  CG1 . VAL   B 63  ? 0.1643 0.1895 0.2652 -0.0249 -0.0216 -0.0087 63  VAL   B CG1 
4992 C  CG2 . VAL   B 63  ? 0.1558 0.2057 0.2599 -0.0111 -0.0277 -0.0184 63  VAL   B CG2 
5002 N  N   . GLU   B 64  ? 0.1601 0.1515 0.1892 -0.0093 -0.0201 -0.0128 64  GLU   B N   
5003 C  CA  . GLU   B 64  ? 0.1602 0.1447 0.1858 -0.0123 -0.0249 -0.0082 64  GLU   B CA  
5004 C  C   . GLU   B 64  ? 0.1527 0.1457 0.1744 -0.0032 -0.0293 -0.0160 64  GLU   B C   
5005 O  O   . GLU   B 64  ? 0.1647 0.1576 0.1695 -0.0099 -0.0219 -0.0135 64  GLU   B O   
5006 C  CB  . GLU   B 64  ? 0.1579 0.1538 0.1823 -0.0165 -0.0162 0.0002  64  GLU   B CB  
5007 C  CG  . GLU   B 64  ? 0.1670 0.1592 0.1802 -0.0257 -0.0186 -0.0088 64  GLU   B CG  
5008 C  CD  . GLU   B 64  ? 0.1683 0.1746 0.1864 -0.0308 -0.0257 -0.0107 64  GLU   B CD  
5009 O  OE1 . GLU   B 64  ? 0.1693 0.1986 0.1887 -0.0377 -0.0198 -0.0316 64  GLU   B OE1 
5010 O  OE2 . GLU   B 64  ? 0.1835 0.1806 0.1950 -0.0322 -0.0406 -0.0135 64  GLU   B OE2 
5017 N  N   . SER   B 65  ? 0.1525 0.1419 0.1699 -0.0102 -0.0143 -0.0152 65  SER   B N   
5018 C  CA  . SER   B 65  ? 0.1530 0.1408 0.1659 -0.0060 -0.0142 -0.0209 65  SER   B CA  
5019 C  C   . SER   B 65  ? 0.1526 0.1435 0.1710 0.0023  -0.0256 -0.0171 65  SER   B C   
5020 O  O   . SER   B 65  ? 0.1603 0.1566 0.1675 0.0027  -0.0253 -0.0279 65  SER   B O   
5021 C  CB  . SER   B 65  ? 0.1575 0.1508 0.1693 -0.0104 -0.0188 -0.0117 65  SER   B CB  
5022 O  OG  . SER   B 65  ? 0.1583 0.1528 0.1670 -0.0079 -0.0140 -0.0231 65  SER   B OG  
5028 N  N   . ASP   B 66  ? 0.1663 0.1487 0.1705 -0.0010 -0.0327 -0.0196 66  ASP   B N   
5029 C  CA  . ASP   B 66  ? 0.1742 0.1588 0.1642 0.0001  -0.0338 -0.0159 66  ASP   B CA  
5030 C  C   . ASP   B 66  ? 0.1780 0.1669 0.1614 -0.0073 -0.0277 -0.0157 66  ASP   B C   
5031 O  O   . ASP   B 66  ? 0.1827 0.1727 0.1730 0.0043  -0.0332 -0.0192 66  ASP   B O   
5032 C  CB  . ASP   B 66  ? 0.1878 0.1704 0.1869 0.0064  -0.0435 -0.0229 66  ASP   B CB  
5033 C  CG  . ASP   B 66  ? 0.2158 0.1818 0.2156 0.0219  -0.0536 -0.0055 66  ASP   B CG  
5034 O  OD1 . ASP   B 66  ? 0.2428 0.1771 0.2212 0.0111  -0.0515 -0.0026 66  ASP   B OD1 
5035 O  OD2 . ASP   B 66  ? 0.2333 0.2135 0.2739 0.0404  -0.0525 -0.0110 66  ASP   B OD2 
5040 N  N   . ASP   B 67  ? 0.1709 0.1572 0.1620 -0.0103 -0.0277 -0.0176 67  ASP   B N   
5041 C  CA  . ASP   B 67  ? 0.1871 0.1532 0.1699 -0.0138 -0.0266 -0.0141 67  ASP   B CA  
5042 C  C   . ASP   B 67  ? 0.1859 0.1517 0.1799 -0.0001 -0.0261 -0.0146 67  ASP   B C   
5043 O  O   . ASP   B 67  ? 0.1925 0.1608 0.1880 -0.0019 -0.0223 -0.0246 67  ASP   B O   
5044 C  CB  . ASP   B 67  ? 0.2070 0.1646 0.1935 -0.0181 -0.0401 -0.0080 67  ASP   B CB  
5045 C  CG  . ASP   B 67  ? 0.2440 0.1736 0.1939 -0.0124 -0.0679 -0.0133 67  ASP   B CG  
5046 O  OD1 . ASP   B 67  ? 0.2685 0.1779 0.2117 -0.0142 -0.0688 -0.0117 67  ASP   B OD1 
5047 O  OD2 . ASP   B 67  ? 0.2606 0.1818 0.2101 0.0056  -0.0708 -0.0167 67  ASP   B OD2 
5052 N  N   . TYR   B 68  ? 0.1814 0.1526 0.1768 -0.0009 -0.0417 -0.0258 68  TYR   B N   
5053 C  CA  . TYR   B 68  ? 0.1738 0.1689 0.1961 0.0034  -0.0409 -0.0293 68  TYR   B CA  
5054 C  C   . TYR   B 68  ? 0.1657 0.1661 0.1880 -0.0007 -0.0302 -0.0340 68  TYR   B C   
5055 O  O   . TYR   B 68  ? 0.1737 0.1800 0.1783 0.0027  -0.0324 -0.0459 68  TYR   B O   
5056 C  CB  . TYR   B 68  ? 0.1747 0.1869 0.1959 0.0050  -0.0425 -0.0408 68  TYR   B CB  
5057 C  CG  . TYR   B 68  ? 0.1887 0.2016 0.1952 0.0137  -0.0322 -0.0603 68  TYR   B CG  
5058 C  CD1 . TYR   B 68  ? 0.1918 0.2041 0.2284 -0.0017 -0.0258 -0.0709 68  TYR   B CD1 
5059 C  CD2 . TYR   B 68  ? 0.1951 0.2191 0.2052 0.0191  -0.0346 -0.0499 68  TYR   B CD2 
5060 C  CE1 . TYR   B 68  ? 0.1980 0.2211 0.2508 0.0001  -0.0189 -0.0652 68  TYR   B CE1 
5061 C  CE2 . TYR   B 68  ? 0.1986 0.2223 0.2208 0.0181  -0.0254 -0.0618 68  TYR   B CE2 
5062 C  CZ  . TYR   B 68  ? 0.1940 0.2219 0.2399 0.0058  -0.0257 -0.0639 68  TYR   B CZ  
5063 O  OH  . TYR   B 68  ? 0.1900 0.2344 0.2590 0.0040  -0.0278 -0.0356 68  TYR   B OH  
5073 N  N   . ILE   B 69  ? 0.1659 0.1559 0.1885 0.0021  -0.0251 -0.0314 69  ILE   B N   
5074 C  CA  . ILE   B 69  ? 0.1739 0.1611 0.1963 -0.0050 -0.0195 -0.0347 69  ILE   B CA  
5075 C  C   . ILE   B 69  ? 0.1707 0.1574 0.1789 0.0100  -0.0318 -0.0299 69  ILE   B C   
5076 O  O   . ILE   B 69  ? 0.1781 0.1731 0.1790 0.0084  -0.0224 -0.0322 69  ILE   B O   
5077 C  CB  . ILE   B 69  ? 0.1809 0.1670 0.2103 -0.0027 -0.0013 -0.0301 69  ILE   B CB  
5078 C  CG1 . ILE   B 69  ? 0.1839 0.1737 0.2139 -0.0073 0.0072  -0.0315 69  ILE   B CG1 
5079 C  CG2 . ILE   B 69  ? 0.1973 0.1800 0.2349 -0.0020 -0.0005 -0.0261 69  ILE   B CG2 
5080 C  CD1 . ILE   B 69  ? 0.1791 0.1789 0.2156 -0.0181 0.0053  -0.0399 69  ILE   B CD1 
5092 N  N   . ALA   B 70  ? 0.1738 0.1608 0.1801 0.0074  -0.0399 -0.0306 70  ALA   B N   
5093 C  CA  . ALA   B 70  ? 0.1782 0.1671 0.1752 0.0031  -0.0422 -0.0221 70  ALA   B CA  
5094 C  C   . ALA   B 70  ? 0.1850 0.1664 0.1780 -0.0022 -0.0415 -0.0342 70  ALA   B C   
5095 O  O   . ALA   B 70  ? 0.1912 0.1709 0.1785 0.0002  -0.0388 -0.0378 70  ALA   B O   
5096 C  CB  . ALA   B 70  ? 0.1807 0.1835 0.1847 0.0049  -0.0396 -0.0260 70  ALA   B CB  
5102 N  N   . THR   B 71  ? 0.1905 0.1685 0.1846 0.0028  -0.0507 -0.0295 71  THR   B N   
5103 C  CA  . THR   B 71  ? 0.2024 0.1691 0.2015 0.0079  -0.0641 -0.0321 71  THR   B CA  
5104 C  C   . THR   B 71  ? 0.1989 0.1717 0.2168 0.0253  -0.0632 -0.0418 71  THR   B C   
5105 O  O   . THR   B 71  ? 0.2116 0.1766 0.2612 0.0242  -0.0567 -0.0635 71  THR   B O   
5106 C  CB  . THR   B 71  ? 0.2210 0.1971 0.2310 0.0007  -0.0682 -0.0117 71  THR   B CB  
5107 O  OG1 . THR   B 71  ? 0.2380 0.2274 0.2608 -0.0189 -0.0640 0.0096  71  THR   B OG1 
5108 C  CG2 . THR   B 71  ? 0.2388 0.1970 0.2549 0.0032  -0.0591 0.0002  71  THR   B CG2 
5116 N  N   . ASN   B 72  ? 0.1863 0.1792 0.2048 0.0130  -0.0590 -0.0593 72  ASN   B N   
5117 C  CA  . ASN   B 72  ? 0.1857 0.1895 0.2182 0.0223  -0.0446 -0.0686 72  ASN   B CA  
5118 C  C   . ASN   B 72  ? 0.1860 0.2023 0.2273 0.0068  -0.0196 -0.0686 72  ASN   B C   
5119 O  O   . ASN   B 72  ? 0.1872 0.2201 0.2528 0.0091  -0.0103 -0.0672 72  ASN   B O   
5120 C  CB  . ASN   B 72  ? 0.1978 0.2045 0.2295 0.0220  -0.0644 -0.0596 72  ASN   B CB  
5121 C  CG  . ASN   B 72  ? 0.2188 0.2188 0.2340 0.0356  -0.0649 -0.0396 72  ASN   B CG  
5122 O  OD1 . ASN   B 72  ? 0.2423 0.2347 0.2358 0.0197  -0.0445 -0.0467 72  ASN   B OD1 
5123 N  ND2 . ASN   B 72  ? 0.2312 0.2279 0.2773 0.0538  -0.0538 -0.0040 72  ASN   B ND2 
5130 N  N   . GLY   B 73  ? 0.1923 0.2007 0.2077 -0.0018 -0.0253 -0.0651 73  GLY   B N   
5131 C  CA  . GLY   B 73  ? 0.1832 0.2108 0.1803 -0.0054 -0.0191 -0.0530 73  GLY   B CA  
5132 C  C   . GLY   B 73  ? 0.1759 0.2077 0.1477 0.0010  -0.0133 -0.0442 73  GLY   B C   
5133 O  O   . GLY   B 73  ? 0.1713 0.1933 0.1658 0.0066  -0.0147 -0.0301 73  GLY   B O   
5137 N  N   . PRO   B 74  ? 0.1814 0.2160 0.1503 0.0047  -0.0242 -0.0330 74  PRO   B N   
5138 C  CA  . PRO   B 74  ? 0.1748 0.2154 0.1346 0.0073  -0.0235 -0.0253 74  PRO   B CA  
5139 C  C   . PRO   B 74  ? 0.1622 0.1977 0.1382 0.0050  -0.0120 -0.0209 74  PRO   B C   
5140 O  O   . PRO   B 74  ? 0.1671 0.2020 0.1873 0.0085  -0.0112 -0.0350 74  PRO   B O   
5141 C  CB  . PRO   B 74  ? 0.1899 0.2369 0.1372 0.0013  -0.0209 -0.0182 74  PRO   B CB  
5142 C  CG  . PRO   B 74  ? 0.2115 0.2452 0.1643 0.0033  -0.0138 -0.0111 74  PRO   B CG  
5143 C  CD  . PRO   B 74  ? 0.2037 0.2352 0.1599 0.0056  -0.0123 -0.0288 74  PRO   B CD  
5151 N  N   . LEU   B 75  ? 0.1583 0.1864 0.1339 0.0086  -0.0203 -0.0236 75  LEU   B N   
5152 C  CA  . LEU   B 75  ? 0.1561 0.1840 0.1415 0.0072  -0.0134 -0.0093 75  LEU   B CA  
5153 C  C   . LEU   B 75  ? 0.1643 0.1883 0.1468 0.0086  -0.0090 -0.0103 75  LEU   B C   
5154 O  O   . LEU   B 75  ? 0.1795 0.1974 0.1583 0.0020  -0.0114 -0.0016 75  LEU   B O   
5155 C  CB  . LEU   B 75  ? 0.1650 0.1806 0.1300 0.0002  -0.0197 0.0052  75  LEU   B CB  
5156 C  CG  . LEU   B 75  ? 0.1988 0.2011 0.1595 -0.0273 -0.0145 -0.0067 75  LEU   B CG  
5157 C  CD1 . LEU   B 75  ? 0.2321 0.2198 0.1724 -0.0401 0.0102  -0.0094 75  LEU   B CD1 
5158 C  CD2 . LEU   B 75  ? 0.2366 0.2212 0.2203 -0.0175 -0.0032 -0.0048 75  LEU   B CD2 
5170 N  N   . LYS   B 76  ? 0.1648 0.2109 0.1704 0.0040  0.0023  -0.0018 76  LYS   B N   
5171 C  CA  . LYS   B 76  ? 0.1774 0.2237 0.1985 -0.0018 0.0222  -0.0041 76  LYS   B CA  
5172 C  C   . LYS   B 76  ? 0.1738 0.2093 0.1683 0.0051  0.0073  0.0155  76  LYS   B C   
5173 O  O   . LYS   B 76  ? 0.1717 0.1918 0.1711 0.0026  0.0045  0.0202  76  LYS   B O   
5174 C  CB  . LYS   B 76  ? 0.1922 0.2366 0.2759 -0.0068 0.0436  -0.0363 76  LYS   B CB  
5175 C  CG  . LYS   B 76  ? 0.2025 0.2558 0.3339 -0.0024 0.0357  -0.0474 76  LYS   B CG  
5176 C  CD  . LYS   B 76  ? 0.2048 0.2631 0.3833 0.0035  0.0203  -0.0679 76  LYS   B CD  
5177 C  CE  . LYS   B 76  ? 0.2108 0.2806 0.4388 0.0059  0.0054  -0.0804 76  LYS   B CE  
5178 N  NZ  . LYS   B 76  ? 0.2071 0.2880 0.4637 0.0007  -0.0132 -0.0970 76  LYS   B NZ  
5192 N  N   . VAL   B 77  ? 0.1761 0.2189 0.1587 0.0164  0.0153  0.0171  77  VAL   B N   
5193 C  CA  . VAL   B 77  ? 0.1791 0.2109 0.1672 0.0229  0.0246  0.0399  77  VAL   B CA  
5194 C  C   . VAL   B 77  ? 0.1611 0.1838 0.1652 0.0199  0.0188  0.0365  77  VAL   B C   
5195 O  O   . VAL   B 77  ? 0.1705 0.1817 0.1783 0.0262  0.0266  0.0253  77  VAL   B O   
5196 C  CB  . VAL   B 77  ? 0.1894 0.2236 0.1996 0.0260  0.0315  0.0563  77  VAL   B CB  
5197 C  CG1 . VAL   B 77  ? 0.1926 0.2178 0.2353 0.0146  0.0331  0.0678  77  VAL   B CG1 
5198 C  CG2 . VAL   B 77  ? 0.2045 0.2465 0.2281 0.0210  0.0126  0.0582  77  VAL   B CG2 
5208 N  N   . GLY   B 78  ? 0.1602 0.1739 0.1730 0.0153  0.0118  0.0261  78  GLY   B N   
5209 C  CA  . GLY   B 78  ? 0.1597 0.1692 0.1616 0.0143  0.0200  0.0173  78  GLY   B CA  
5210 C  C   . GLY   B 78  ? 0.1555 0.1623 0.1596 0.0106  0.0153  0.0219  78  GLY   B C   
5211 O  O   . GLY   B 78  ? 0.1614 0.1594 0.1684 0.0149  0.0165  0.0280  78  GLY   B O   
5215 N  N   . GLY   B 79  ? 0.1440 0.1663 0.1639 0.0111  0.0155  0.0145  79  GLY   B N   
5216 C  CA  . GLY   B 79  ? 0.1452 0.1614 0.1568 0.0084  0.0014  0.0068  79  GLY   B CA  
5217 C  C   . GLY   B 79  ? 0.1356 0.1496 0.1553 0.0112  0.0052  0.0034  79  GLY   B C   
5218 O  O   . GLY   B 79  ? 0.1480 0.1487 0.1666 0.0117  0.0161  0.0166  79  GLY   B O   
5222 N  N   . SER   B 80  ? 0.1380 0.1443 0.1712 0.0053  0.0155  0.0007  80  SER   B N   
5223 C  CA  . SER   B 80  ? 0.1318 0.1403 0.1692 0.0015  0.0029  -0.0026 80  SER   B CA  
5224 C  C   . SER   B 80  ? 0.1399 0.1399 0.1580 0.0092  -0.0032 -0.0031 80  SER   B C   
5225 O  O   . SER   B 80  ? 0.1498 0.1444 0.1928 0.0115  -0.0005 -0.0089 80  SER   B O   
5226 C  CB  . SER   B 80  ? 0.1443 0.1407 0.1737 -0.0036 -0.0013 0.0066  80  SER   B CB  
5227 O  OG  . SER   B 80  ? 0.1489 0.1566 0.1917 -0.0021 -0.0121 0.0116  80  SER   B OG  
5233 N  N   . CYS   B 81  ? 0.1398 0.1283 0.1643 0.0017  -0.0070 -0.0067 81  CYS   B N   
5234 C  CA  . CYS   B 81  ? 0.1445 0.1256 0.1763 -0.0008 -0.0092 -0.0045 81  CYS   B CA  
5235 C  C   . CYS   B 81  ? 0.1418 0.1244 0.1472 -0.0000 -0.0148 -0.0013 81  CYS   B C   
5236 O  O   . CYS   B 81  ? 0.1674 0.1259 0.1585 0.0059  -0.0030 -0.0086 81  CYS   B O   
5237 C  CB  . CYS   B 81  ? 0.1613 0.1408 0.1729 -0.0084 -0.0152 -0.0033 81  CYS   B CB  
5238 S  SG  . CYS   B 81  ? 0.1568 0.1586 0.1624 -0.0055 -0.0246 -0.0096 81  CYS   B SG  
5244 N  N   . VAL   B 82  ? 0.1429 0.1229 0.1667 -0.0005 -0.0135 -0.0093 82  VAL   B N   
5245 C  CA  . VAL   B 82  ? 0.1516 0.1233 0.1577 -0.0060 -0.0091 0.0028  82  VAL   B CA  
5246 C  C   . VAL   B 82  ? 0.1587 0.1179 0.1669 -0.0024 -0.0060 -0.0031 82  VAL   B C   
5247 O  O   . VAL   B 82  ? 0.1650 0.1224 0.1955 -0.0081 -0.0083 -0.0198 82  VAL   B O   
5248 C  CB  . VAL   B 82  ? 0.1593 0.1488 0.1685 0.0010  -0.0132 0.0102  82  VAL   B CB  
5249 C  CG1 . VAL   B 82  ? 0.1825 0.1681 0.1813 0.0072  -0.0227 0.0240  82  VAL   B CG1 
5250 C  CG2 . VAL   B 82  ? 0.1670 0.1587 0.1888 -0.0036 -0.0266 0.0143  82  VAL   B CG2 
5260 N  N   . LEU   B 83  ? 0.1459 0.1264 0.1569 -0.0160 -0.0172 -0.0049 83  LEU   B N   
5261 C  CA  . LEU   B 83  ? 0.1469 0.1256 0.1584 -0.0104 -0.0174 -0.0049 83  LEU   B CA  
5262 C  C   . LEU   B 83  ? 0.1461 0.1286 0.1531 -0.0178 -0.0186 -0.0045 83  LEU   B C   
5263 O  O   . LEU   B 83  ? 0.1534 0.1380 0.1429 -0.0193 -0.0141 0.0051  83  LEU   B O   
5264 C  CB  . LEU   B 83  ? 0.1506 0.1382 0.1693 -0.0125 -0.0197 -0.0111 83  LEU   B CB  
5265 C  CG  . LEU   B 83  ? 0.1637 0.1572 0.1774 -0.0130 -0.0056 -0.0097 83  LEU   B CG  
5266 C  CD1 . LEU   B 83  ? 0.1775 0.1602 0.1836 -0.0142 -0.0245 0.0031  83  LEU   B CD1 
5267 C  CD2 . LEU   B 83  ? 0.1809 0.1611 0.1902 -0.0068 0.0009  -0.0273 83  LEU   B CD2 
5279 N  N   . SER   B 84  ? 0.1557 0.1396 0.1803 -0.0226 -0.0118 -0.0028 84  SER   B N   
5280 C  CA  . SER   B 84  ? 0.1613 0.1563 0.1693 -0.0304 -0.0139 0.0171  84  SER   B CA  
5281 C  C   . SER   B 84  ? 0.1460 0.1737 0.1321 -0.0225 -0.0205 0.0169  84  SER   B C   
5282 O  O   . SER   B 84  ? 0.1521 0.1560 0.1365 -0.0190 -0.0158 0.0023  84  SER   B O   
5283 C  CB  . SER   B 84  ? 0.1750 0.1583 0.2134 -0.0311 0.0084  0.0099  84  SER   B CB  
5284 O  OG  . SER   B 84  ? 0.1746 0.1795 0.2612 -0.0372 0.0048  0.0186  84  SER   B OG  
5290 N  N   . GLY   B 85  ? 0.1488 0.1973 0.1441 -0.0226 -0.0104 0.0216  85  GLY   B N   
5291 C  CA  . GLY   B 85  ? 0.1490 0.2016 0.1595 -0.0324 0.0002  -0.0077 85  GLY   B CA  
5292 C  C   . GLY   B 85  ? 0.1509 0.1811 0.1551 -0.0424 -0.0028 0.0085  85  GLY   B C   
5293 O  O   . GLY   B 85  ? 0.1668 0.1777 0.1548 -0.0542 0.0148  -0.0045 85  GLY   B O   
5297 N  N   . HIS   B 86  ? 0.1475 0.1668 0.1722 -0.0318 -0.0181 0.0174  86  HIS   B N   
5298 C  CA  . HIS   B 86  ? 0.1494 0.1655 0.1757 -0.0323 -0.0175 0.0196  86  HIS   B CA  
5299 C  C   . HIS   B 86  ? 0.1500 0.1785 0.1662 -0.0400 -0.0123 0.0357  86  HIS   B C   
5300 O  O   . HIS   B 86  ? 0.1657 0.1867 0.1651 -0.0322 0.0018  0.0290  86  HIS   B O   
5301 C  CB  . HIS   B 86  ? 0.1581 0.1663 0.1755 -0.0238 -0.0219 0.0038  86  HIS   B CB  
5302 C  CG  . HIS   B 86  ? 0.1584 0.1709 0.1679 -0.0137 -0.0232 0.0061  86  HIS   B CG  
5303 N  ND1 . HIS   B 86  ? 0.1713 0.1952 0.1914 -0.0244 -0.0226 -0.0114 86  HIS   B ND1 
5304 C  CD2 . HIS   B 86  ? 0.1604 0.1768 0.1782 -0.0096 -0.0235 0.0073  86  HIS   B CD2 
5305 C  CE1 . HIS   B 86  ? 0.1771 0.1943 0.1735 -0.0144 -0.0049 -0.0251 86  HIS   B CE1 
5306 N  NE2 . HIS   B 86  ? 0.1697 0.1857 0.1605 -0.0021 -0.0099 -0.0057 86  HIS   B NE2 
5314 N  N   . ASN   B 87  ? 0.1556 0.1795 0.1703 -0.0368 -0.0047 0.0315  87  ASN   B N   
5315 C  CA  . ASN   B 87  ? 0.1643 0.2040 0.1682 -0.0328 0.0170  0.0171  87  ASN   B CA  
5316 C  C   . ASN   B 87  ? 0.1760 0.1867 0.1617 -0.0311 0.0314  0.0150  87  ASN   B C   
5317 O  O   . ASN   B 87  ? 0.2026 0.1933 0.1884 -0.0221 0.0523  0.0105  87  ASN   B O   
5318 C  CB  . ASN   B 87  ? 0.1676 0.2357 0.1989 -0.0307 0.0131  0.0145  87  ASN   B CB  
5319 C  CG  . ASN   B 87  ? 0.1722 0.2514 0.2102 0.0034  0.0277  0.0278  87  ASN   B CG  
5320 O  OD1 . ASN   B 87  ? 0.1673 0.2317 0.1907 0.0095  0.0357  0.0430  87  ASN   B OD1 
5321 N  ND2 . ASN   B 87  ? 0.2075 0.2669 0.2519 0.0072  0.0436  0.0231  87  ASN   B ND2 
5328 N  N   . LEU   B 88  ? 0.1609 0.1749 0.1514 -0.0360 0.0077  0.0133  88  LEU   B N   
5329 C  CA  . LEU   B 88  ? 0.1756 0.1638 0.1580 -0.0320 -0.0006 0.0057  88  LEU   B CA  
5330 C  C   . LEU   B 88  ? 0.1743 0.1513 0.1583 -0.0371 -0.0007 0.0016  88  LEU   B C   
5331 O  O   . LEU   B 88  ? 0.1931 0.1641 0.1859 -0.0195 -0.0222 -0.0074 88  LEU   B O   
5332 C  CB  . LEU   B 88  ? 0.1834 0.1659 0.1734 -0.0390 -0.0125 0.0231  88  LEU   B CB  
5333 C  CG  . LEU   B 88  ? 0.2197 0.1912 0.1935 -0.0292 -0.0292 0.0414  88  LEU   B CG  
5334 C  CD1 . LEU   B 88  ? 0.2270 0.2280 0.1998 -0.0418 -0.0209 0.0555  88  LEU   B CD1 
5335 C  CD2 . LEU   B 88  ? 0.2541 0.2118 0.2506 0.0136  -0.0510 0.0180  88  LEU   B CD2 
5347 N  N   . ALA   B 89  ? 0.1629 0.1520 0.1509 -0.0371 0.0146  0.0058  89  ALA   B N   
5348 C  CA  . ALA   B 89  ? 0.1578 0.1484 0.1362 -0.0342 0.0006  0.0069  89  ALA   B CA  
5349 C  C   . ALA   B 89  ? 0.1696 0.1519 0.1328 -0.0374 0.0126  0.0040  89  ALA   B C   
5350 O  O   . ALA   B 89  ? 0.1567 0.1561 0.1722 -0.0407 0.0101  -0.0254 89  ALA   B O   
5351 C  CB  . ALA   B 89  ? 0.1486 0.1476 0.1574 -0.0354 0.0054  0.0131  89  ALA   B CB  
5357 N  N   . LYS   B 90  ? 0.2021 0.1423 0.1478 -0.0437 -0.0114 0.0088  90  LYS   B N   
5358 C  CA  . LYS   B 90  ? 0.2144 0.1399 0.1417 -0.0461 -0.0116 0.0082  90  LYS   B CA  
5359 C  C   . LYS   B 90  ? 0.2044 0.1286 0.1602 -0.0451 -0.0091 0.0013  90  LYS   B C   
5360 O  O   . LYS   B 90  ? 0.2161 0.1478 0.1765 -0.0602 -0.0029 0.0026  90  LYS   B O   
5361 C  CB  . LYS   B 90  ? 0.2348 0.1517 0.1700 -0.0344 -0.0019 0.0185  90  LYS   B CB  
5362 C  CG  . LYS   B 90  ? 0.2392 0.1614 0.1821 -0.0234 0.0218  0.0168  90  LYS   B CG  
5363 C  CD  . LYS   B 90  ? 0.2705 0.1910 0.2335 -0.0174 0.0474  0.0031  90  LYS   B CD  
5364 C  CE  . LYS   B 90  ? 0.2810 0.2086 0.2850 -0.0267 0.0634  -0.0057 90  LYS   B CE  
5365 N  NZ  . LYS   B 90  ? 0.2890 0.1985 0.2807 -0.0413 0.0843  -0.0008 90  LYS   B NZ  
5379 N  N   . HIS   B 91  ? 0.1764 0.1223 0.1349 -0.0334 -0.0135 0.0019  91  HIS   B N   
5380 C  CA  . HIS   B 91  ? 0.1608 0.1277 0.1461 -0.0258 -0.0094 0.0015  91  HIS   B CA  
5381 C  C   . HIS   B 91  ? 0.1486 0.1323 0.1316 -0.0307 -0.0125 0.0028  91  HIS   B C   
5382 O  O   . HIS   B 91  ? 0.1676 0.1366 0.1311 -0.0275 -0.0209 0.0023  91  HIS   B O   
5383 C  CB  . HIS   B 91  ? 0.1833 0.1283 0.1912 -0.0057 -0.0053 0.0120  91  HIS   B CB  
5384 C  CG  . HIS   B 91  ? 0.2220 0.1485 0.2491 0.0052  0.0288  0.0186  91  HIS   B CG  
5385 N  ND1 . HIS   B 91  ? 0.2552 0.1590 0.3154 -0.0027 0.0344  0.0008  91  HIS   B ND1 
5386 C  CD2 . HIS   B 91  ? 0.2391 0.1779 0.2959 0.0182  0.0193  0.0559  91  HIS   B CD2 
5387 C  CE1 . HIS   B 91  ? 0.2575 0.1714 0.3301 0.0184  0.0358  0.0137  91  HIS   B CE1 
5388 N  NE2 . HIS   B 91  ? 0.2486 0.1865 0.3295 0.0290  0.0352  0.0578  91  HIS   B NE2 
5396 N  N   . CYS   B 92  ? 0.1447 0.1278 0.1283 -0.0246 -0.0144 0.0020  92  CYS   B N   
5397 C  CA  . CYS   B 92  ? 0.1397 0.1274 0.1348 -0.0213 -0.0061 0.0054  92  CYS   B CA  
5398 C  C   . CYS   B 92  ? 0.1420 0.1209 0.1247 -0.0101 -0.0098 0.0006  92  CYS   B C   
5399 O  O   . CYS   B 92  ? 0.1480 0.1293 0.1456 -0.0183 -0.0020 -0.0014 92  CYS   B O   
5400 C  CB  . CYS   B 92  ? 0.1413 0.1347 0.1444 -0.0154 -0.0066 0.0037  92  CYS   B CB  
5401 S  SG  . CYS   B 92  ? 0.1400 0.1370 0.1455 -0.0103 -0.0092 0.0053  92  CYS   B SG  
5407 N  N   . LEU   B 93  ? 0.1301 0.1218 0.1306 -0.0180 -0.0095 0.0014  93  LEU   B N   
5408 C  CA  . LEU   B 93  ? 0.1318 0.1212 0.1390 -0.0089 -0.0104 0.0048  93  LEU   B CA  
5409 C  C   . LEU   B 93  ? 0.1311 0.1219 0.1272 -0.0060 -0.0082 0.0030  93  LEU   B C   
5410 O  O   . LEU   B 93  ? 0.1345 0.1217 0.1384 -0.0044 -0.0016 0.0004  93  LEU   B O   
5411 C  CB  . LEU   B 93  ? 0.1342 0.1227 0.1452 -0.0040 -0.0115 0.0058  93  LEU   B CB  
5412 C  CG  . LEU   B 93  ? 0.1316 0.1379 0.1621 -0.0034 -0.0029 0.0126  93  LEU   B CG  
5413 C  CD1 . LEU   B 93  ? 0.1379 0.1470 0.1638 0.0079  0.0041  -0.0030 93  LEU   B CD1 
5414 C  CD2 . LEU   B 93  ? 0.1390 0.1316 0.1739 -0.0071 -0.0055 0.0065  93  LEU   B CD2 
5426 N  N   . HIS   B 94  ? 0.1325 0.1147 0.1270 -0.0071 -0.0111 0.0051  94  HIS   B N   
5427 C  CA  . HIS   B 94  ? 0.1343 0.1129 0.1357 -0.0043 -0.0044 0.0084  94  HIS   B CA  
5428 C  C   . HIS   B 94  ? 0.1273 0.1200 0.1457 -0.0014 -0.0041 0.0099  94  HIS   B C   
5429 O  O   . HIS   B 94  ? 0.1337 0.1342 0.1853 -0.0013 0.0148  -0.0078 94  HIS   B O   
5430 C  CB  . HIS   B 94  ? 0.1321 0.1289 0.1362 -0.0009 -0.0060 0.0081  94  HIS   B CB  
5431 C  CG  . HIS   B 94  ? 0.1357 0.1257 0.1377 -0.0071 -0.0209 0.0060  94  HIS   B CG  
5432 N  ND1 . HIS   B 94  ? 0.1427 0.1296 0.1362 -0.0065 -0.0208 0.0030  94  HIS   B ND1 
5433 C  CD2 . HIS   B 94  ? 0.1372 0.1216 0.1412 -0.0042 -0.0168 0.0090  94  HIS   B CD2 
5434 C  CE1 . HIS   B 94  ? 0.1446 0.1297 0.1324 -0.0127 -0.0214 0.0013  94  HIS   B CE1 
5435 N  NE2 . HIS   B 94  ? 0.1383 0.1314 0.1384 -0.0166 -0.0163 0.0045  94  HIS   B NE2 
5443 N  N   . VAL   B 95  ? 0.1255 0.1221 0.1515 -0.0002 -0.0023 0.0068  95  VAL   B N   
5444 C  CA  . VAL   B 95  ? 0.1257 0.1293 0.1476 -0.0031 0.0019  0.0172  95  VAL   B CA  
5445 C  C   . VAL   B 95  ? 0.1307 0.1314 0.1391 -0.0011 0.0129  0.0077  95  VAL   B C   
5446 O  O   . VAL   B 95  ? 0.1334 0.1298 0.1608 0.0043  0.0063  0.0160  95  VAL   B O   
5447 C  CB  . VAL   B 95  ? 0.1350 0.1232 0.1491 -0.0047 -0.0057 0.0093  95  VAL   B CB  
5448 C  CG1 . VAL   B 95  ? 0.1459 0.1376 0.1675 -0.0048 -0.0001 0.0134  95  VAL   B CG1 
5449 C  CG2 . VAL   B 95  ? 0.1460 0.1248 0.1584 -0.0003 -0.0142 0.0026  95  VAL   B CG2 
5459 N  N   . VAL   B 96  ? 0.1437 0.1353 0.1418 0.0071  0.0087  0.0152  96  VAL   B N   
5460 C  CA  . VAL   B 96  ? 0.1537 0.1456 0.1405 0.0108  0.0048  0.0184  96  VAL   B CA  
5461 C  C   . VAL   B 96  ? 0.1500 0.1464 0.1511 0.0108  0.0125  0.0202  96  VAL   B C   
5462 O  O   . VAL   B 96  ? 0.1483 0.1560 0.1822 0.0061  0.0145  0.0097  96  VAL   B O   
5463 C  CB  . VAL   B 96  ? 0.1575 0.1683 0.1487 0.0120  0.0050  0.0072  96  VAL   B CB  
5464 C  CG1 . VAL   B 96  ? 0.1582 0.1838 0.1583 0.0170  0.0085  0.0052  96  VAL   B CG1 
5465 C  CG2 . VAL   B 96  ? 0.1662 0.1781 0.1577 0.0061  0.0111  0.0015  96  VAL   B CG2 
5475 N  N   . GLY   B 97  ? 0.1627 0.1430 0.1483 0.0056  0.0126  0.0220  97  GLY   B N   
5476 C  CA  . GLY   B 97  ? 0.1753 0.1480 0.1532 0.0041  0.0159  0.0151  97  GLY   B CA  
5477 C  C   . GLY   B 97  ? 0.1830 0.1569 0.1588 0.0080  0.0071  0.0157  97  GLY   B C   
5478 O  O   . GLY   B 97  ? 0.1913 0.1688 0.1640 0.0022  0.0038  0.0081  97  GLY   B O   
5482 N  N   . PRO   B 98  ? 0.1945 0.1632 0.1743 0.0081  0.0303  0.0307  98  PRO   B N   
5483 C  CA  . PRO   B 98  ? 0.2080 0.1754 0.1823 0.0183  0.0419  0.0279  98  PRO   B CA  
5484 C  C   . PRO   B 98  ? 0.2212 0.1831 0.1554 0.0293  0.0363  0.0437  98  PRO   B C   
5485 O  O   . PRO   B 98  ? 0.2068 0.1742 0.1786 0.0252  0.0439  0.0408  98  PRO   B O   
5486 C  CB  . PRO   B 98  ? 0.1927 0.1745 0.1957 0.0139  0.0538  0.0211  98  PRO   B CB  
5487 C  CG  . PRO   B 98  ? 0.1896 0.1725 0.1991 0.0118  0.0448  0.0370  98  PRO   B CG  
5488 C  CD  . PRO   B 98  ? 0.1778 0.1693 0.1949 0.0129  0.0332  0.0352  98  PRO   B CD  
5496 N  N   . ASN   B 99  ? 0.2307 0.1988 0.1645 0.0494  0.0352  0.0256  99  ASN   B N   
5497 C  CA  . ASN   B 99  ? 0.2530 0.2070 0.1695 0.0539  0.0265  0.0414  99  ASN   B CA  
5498 C  C   . ASN   B 99  ? 0.2810 0.2412 0.1908 0.0450  0.0501  0.0728  99  ASN   B C   
5499 O  O   . ASN   B 99  ? 0.2945 0.2418 0.2030 0.0445  0.0399  0.0613  99  ASN   B O   
5500 C  CB  . ASN   B 99  ? 0.2606 0.2021 0.1757 0.0555  0.0190  0.0367  99  ASN   B CB  
5501 C  CG  . ASN   B 99  ? 0.2632 0.2076 0.2070 0.0520  0.0077  0.0324  99  ASN   B CG  
5502 O  OD1 . ASN   B 99  ? 0.2679 0.2094 0.2385 0.0573  0.0077  0.0400  99  ASN   B OD1 
5503 N  ND2 . ASN   B 99  ? 0.2601 0.2059 0.2184 0.0560  -0.0162 0.0295  99  ASN   B ND2 
5510 N  N   A VAL   B 100 ? 0.3009 0.2592 0.2281 0.0354  0.0525  0.0915  100 VAL   B N   
5511 N  N   B VAL   B 100 ? 0.2998 0.2587 0.2277 0.0341  0.0527  0.0917  100 VAL   B N   
5512 C  CA  A VAL   B 100 ? 0.3279 0.2761 0.2814 0.0273  0.0543  0.1046  100 VAL   B CA  
5513 C  CA  B VAL   B 100 ? 0.3258 0.2749 0.2800 0.0249  0.0548  0.1049  100 VAL   B CA  
5514 C  C   A VAL   B 100 ? 0.3492 0.2796 0.2765 0.0325  0.0551  0.1197  100 VAL   B C   
5515 C  C   B VAL   B 100 ? 0.3479 0.2783 0.2741 0.0306  0.0551  0.1194  100 VAL   B C   
5516 O  O   A VAL   B 100 ? 0.3543 0.2865 0.2833 0.0310  0.0627  0.1165  100 VAL   B O   
5517 O  O   B VAL   B 100 ? 0.3525 0.2836 0.2777 0.0280  0.0625  0.1156  100 VAL   B O   
5518 C  CB  A VAL   B 100 ? 0.3365 0.2905 0.3446 0.0118  0.0493  0.1069  100 VAL   B CB  
5519 C  CB  B VAL   B 100 ? 0.3328 0.2889 0.3423 0.0080  0.0514  0.1083  100 VAL   B CB  
5520 C  CG1 A VAL   B 100 ? 0.3411 0.2967 0.3686 0.0084  0.0478  0.1074  100 VAL   B CG1 
5521 C  CG1 B VAL   B 100 ? 0.3368 0.2948 0.3661 0.0040  0.0510  0.1096  100 VAL   B CG1 
5522 C  CG2 A VAL   B 100 ? 0.3386 0.2943 0.3592 0.0069  0.0514  0.1111  100 VAL   B CG2 
5523 C  CG2 B VAL   B 100 ? 0.3346 0.2922 0.3570 0.0027  0.0533  0.1128  100 VAL   B CG2 
5542 N  N   . ASN   B 101 ? 0.3648 0.2822 0.2711 0.0413  0.0412  0.1276  101 ASN   B N   
5543 C  CA  . ASN   B 101 ? 0.4102 0.3015 0.2996 0.0473  0.0117  0.1293  101 ASN   B CA  
5544 C  C   . ASN   B 101 ? 0.4597 0.3462 0.3023 0.0435  -0.0018 0.1277  101 ASN   B C   
5545 O  O   . ASN   B 101 ? 0.4659 0.3577 0.3188 0.0499  -0.0039 0.1093  101 ASN   B O   
5546 C  CB  . ASN   B 101 ? 0.4080 0.2832 0.3134 0.0438  0.0096  0.1194  101 ASN   B CB  
5547 C  CG  . ASN   B 101 ? 0.4026 0.2628 0.3213 0.0416  0.0111  0.1242  101 ASN   B CG  
5548 O  OD1 . ASN   B 101 ? 0.4065 0.2636 0.3573 0.0333  0.0272  0.1130  101 ASN   B OD1 
5549 N  ND2 . ASN   B 101 ? 0.3988 0.2609 0.3176 0.0402  0.0041  0.1086  101 ASN   B ND2 
5557 N  N   A LYS   B 102 ? 0.4801 0.3663 0.3175 0.0345  0.0022  0.1151  102 LYS   B N   
5558 N  N   B LYS   B 102 ? 0.4799 0.3663 0.3176 0.0346  0.0021  0.1153  102 LYS   B N   
5559 C  CA  A LYS   B 102 ? 0.4994 0.3916 0.3398 0.0242  0.0092  0.0923  102 LYS   B CA  
5560 C  CA  B LYS   B 102 ? 0.4992 0.3915 0.3400 0.0243  0.0090  0.0926  102 LYS   B CA  
5561 C  C   A LYS   B 102 ? 0.4994 0.3919 0.3176 0.0253  0.0172  0.0966  102 LYS   B C   
5562 C  C   B LYS   B 102 ? 0.4993 0.3918 0.3181 0.0254  0.0172  0.0965  102 LYS   B C   
5563 O  O   A LYS   B 102 ? 0.5070 0.3956 0.3208 0.0265  0.0096  0.0937  102 LYS   B O   
5564 O  O   B LYS   B 102 ? 0.5069 0.3956 0.3220 0.0267  0.0097  0.0931  102 LYS   B O   
5565 C  CB  A LYS   B 102 ? 0.5160 0.4147 0.3928 0.0139  0.0156  0.0583  102 LYS   B CB  
5566 C  CB  B LYS   B 102 ? 0.5155 0.4146 0.3930 0.0142  0.0152  0.0589  102 LYS   B CB  
5567 C  CG  A LYS   B 102 ? 0.5296 0.4344 0.4469 0.0064  0.0226  0.0249  102 LYS   B CG  
5568 C  CG  B LYS   B 102 ? 0.5289 0.4344 0.4469 0.0068  0.0221  0.0257  102 LYS   B CG  
5569 C  CD  A LYS   B 102 ? 0.5409 0.4504 0.4981 0.0007  0.0294  -0.0010 102 LYS   B CD  
5570 C  CD  B LYS   B 102 ? 0.5400 0.4504 0.4976 0.0012  0.0287  0.0001  102 LYS   B CD  
5571 C  CE  A LYS   B 102 ? 0.5485 0.4617 0.5388 -0.0038 0.0347  -0.0198 102 LYS   B CE  
5572 C  CE  B LYS   B 102 ? 0.5476 0.4617 0.5379 -0.0033 0.0337  -0.0183 102 LYS   B CE  
5573 N  NZ  A LYS   B 102 ? 0.5527 0.4687 0.5620 -0.0062 0.0368  -0.0304 102 LYS   B NZ  
5574 N  NZ  B LYS   B 102 ? 0.5517 0.4687 0.5604 -0.0057 0.0356  -0.0287 102 LYS   B NZ  
5601 N  N   . GLY   B 103 ? 0.4883 0.3854 0.3044 0.0245  0.0361  0.0973  103 GLY   B N   
5602 C  CA  . GLY   B 103 ? 0.4654 0.3738 0.3095 0.0233  0.0698  0.0794  103 GLY   B CA  
5603 C  C   . GLY   B 103 ? 0.4380 0.3566 0.2989 0.0162  0.0984  0.0652  103 GLY   B C   
5604 O  O   . GLY   B 103 ? 0.4457 0.3658 0.3173 0.0168  0.0998  0.0645  103 GLY   B O   
5609 N  N   A GLU   B 104 ? 0.4209 0.3463 0.2923 0.0189  0.1083  0.0511  104 GLU   B N   
5610 N  N   B GLU   B 104 ? 0.4186 0.3382 0.2866 0.0066  0.1057  0.0520  104 GLU   B N   
5611 C  CA  A GLU   B 104 ? 0.4036 0.3362 0.2815 0.0227  0.1105  0.0354  104 GLU   B CA  
5612 C  CA  B GLU   B 104 ? 0.3993 0.3202 0.2706 -0.0023 0.1044  0.0375  104 GLU   B CA  
5613 C  C   A GLU   B 104 ? 0.4071 0.3416 0.3014 0.0083  0.1308  0.0322  104 GLU   B C   
5614 C  C   B GLU   B 104 ? 0.3974 0.3201 0.2867 -0.0138 0.1236  0.0320  104 GLU   B C   
5615 O  O   A GLU   B 104 ? 0.4094 0.3455 0.3226 0.0048  0.1273  0.0288  104 GLU   B O   
5616 O  O   B GLU   B 104 ? 0.3998 0.3218 0.3077 -0.0164 0.1209  0.0253  104 GLU   B O   
5617 C  CB  A GLU   B 104 ? 0.3869 0.3208 0.2676 0.0413  0.0822  0.0150  104 GLU   B CB  
5618 C  CB  B GLU   B 104 ? 0.3860 0.3016 0.2555 0.0002  0.0733  0.0193  104 GLU   B CB  
5619 C  CG  A GLU   B 104 ? 0.3717 0.3080 0.2515 0.0600  0.0475  -0.0088 104 GLU   B CG  
5620 C  CG  B GLU   B 104 ? 0.3754 0.2855 0.2378 0.0038  0.0351  -0.0047 104 GLU   B CG  
5621 C  CD  A GLU   B 104 ? 0.3580 0.2959 0.2369 0.0764  0.0190  -0.0198 104 GLU   B CD  
5622 C  CD  B GLU   B 104 ? 0.3664 0.2693 0.2207 0.0032  0.0071  -0.0137 104 GLU   B CD  
5623 O  OE1 A GLU   B 104 ? 0.3424 0.2826 0.2074 0.0891  0.0287  -0.0192 104 GLU   B OE1 
5624 O  OE1 B GLU   B 104 ? 0.3544 0.2556 0.2025 0.0014  0.0114  -0.0103 104 GLU   B OE1 
5625 O  OE2 A GLU   B 104 ? 0.3601 0.3017 0.2470 0.0761  -0.0067 -0.0294 104 GLU   B OE2 
5626 O  OE2 B GLU   B 104 ? 0.3686 0.2708 0.2163 0.0007  -0.0169 -0.0232 104 GLU   B OE2 
5639 N  N   A ASP   B 105 ? 0.4053 0.3450 0.3094 -0.0031 0.1516  0.0344  105 ASP   B N   
5640 N  N   B ASP   B 105 ? 0.3904 0.3205 0.2868 -0.0243 0.1443  0.0348  105 ASP   B N   
5641 C  CA  A ASP   B 105 ? 0.4061 0.3475 0.3312 -0.0104 0.1673  0.0249  105 ASP   B CA  
5642 C  CA  B ASP   B 105 ? 0.3862 0.3197 0.3039 -0.0302 0.1609  0.0266  105 ASP   B CA  
5643 C  C   A ASP   B 105 ? 0.3923 0.3250 0.3096 -0.0140 0.1697  0.0212  105 ASP   B C   
5644 C  C   B ASP   B 105 ? 0.3738 0.2978 0.2871 -0.0366 0.1592  0.0164  105 ASP   B C   
5645 O  O   A ASP   B 105 ? 0.3862 0.3197 0.3044 -0.0116 0.1767  0.0224  105 ASP   B O   
5646 O  O   B ASP   B 105 ? 0.3642 0.2895 0.2804 -0.0379 0.1665  0.0159  105 ASP   B O   
5647 C  CB  A ASP   B 105 ? 0.4186 0.3675 0.3939 -0.0094 0.1699  0.0116  105 ASP   B CB  
5648 C  CB  B ASP   B 105 ? 0.3933 0.3366 0.3563 -0.0256 0.1665  0.0198  105 ASP   B CB  
5649 C  CG  A ASP   B 105 ? 0.4269 0.3814 0.4518 -0.0108 0.1748  0.0037  105 ASP   B CG  
5650 C  CG  B ASP   B 105 ? 0.3966 0.3466 0.4005 -0.0255 0.1762  0.0208  105 ASP   B CG  
5651 O  OD1 A ASP   B 105 ? 0.4277 0.3863 0.4599 -0.0158 0.1824  0.0066  105 ASP   B OD1 
5652 O  OD1 B ASP   B 105 ? 0.3966 0.3506 0.4093 -0.0317 0.1795  0.0262  105 ASP   B OD1 
5653 O  OD2 A ASP   B 105 ? 0.4317 0.3869 0.4876 -0.0075 0.1676  -0.0036 105 ASP   B OD2 
5654 O  OD2 B ASP   B 105 ? 0.3949 0.3504 0.4121 -0.0244 0.1864  0.0223  105 ASP   B OD2 
5663 N  N   A ILE   B 106 ? 0.3823 0.3050 0.3183 -0.0175 0.1548  0.0218  106 ILE   B N   
5664 N  N   B ILE   B 106 ? 0.3674 0.2827 0.2960 -0.0393 0.1420  0.0109  106 ILE   B N   
5665 C  CA  A ILE   B 106 ? 0.3643 0.2826 0.3255 -0.0240 0.1535  0.0205  106 ILE   B CA  
5666 C  CA  B ILE   B 106 ? 0.3530 0.2676 0.3058 -0.0455 0.1399  0.0065  106 ILE   B CA  
5667 C  C   A ILE   B 106 ? 0.3366 0.2739 0.3221 -0.0194 0.1537  0.0102  106 ILE   B C   
5668 C  C   B ILE   B 106 ? 0.3276 0.2639 0.3031 -0.0413 0.1393  -0.0068 106 ILE   B C   
5669 O  O   A ILE   B 106 ? 0.3298 0.2571 0.3233 -0.0193 0.1500  0.0078  106 ILE   B O   
5670 O  O   B ILE   B 106 ? 0.3191 0.2465 0.2987 -0.0475 0.1322  -0.0146 106 ILE   B O   
5671 C  CB  A ILE   B 106 ? 0.3764 0.2759 0.3392 -0.0318 0.1436  0.0262  106 ILE   B CB  
5672 C  CB  B ILE   B 106 ? 0.3673 0.2659 0.3215 -0.0505 0.1314  0.0131  106 ILE   B CB  
5673 C  CG1 A ILE   B 106 ? 0.3823 0.2756 0.3419 -0.0266 0.1352  0.0219  106 ILE   B CG1 
5674 C  CG1 B ILE   B 106 ? 0.3756 0.2701 0.3294 -0.0407 0.1214  0.0092  106 ILE   B CG1 
5675 C  CG2 A ILE   B 106 ? 0.3817 0.2772 0.3540 -0.0380 0.1415  0.0306  106 ILE   B CG2 
5676 C  CG2 B ILE   B 106 ? 0.3728 0.2677 0.3358 -0.0577 0.1306  0.0168  106 ILE   B CG2 
5677 C  CD1 A ILE   B 106 ? 0.3845 0.2765 0.3380 -0.0222 0.1324  0.0225  106 ILE   B CD1 
5678 C  CD1 B ILE   B 106 ? 0.3789 0.2733 0.3298 -0.0339 0.1187  0.0105  106 ILE   B CD1 
5701 N  N   A GLN   B 107 ? 0.3204 0.2857 0.3346 -0.0191 0.1443  0.0090  107 GLN   B N   
5702 N  N   B GLN   B 107 ? 0.3158 0.2807 0.3209 -0.0341 0.1324  -0.0066 107 GLN   B N   
5703 C  CA  A GLN   B 107 ? 0.3018 0.2950 0.3471 -0.0176 0.1292  0.0087  107 GLN   B CA  
5704 C  CA  B GLN   B 107 ? 0.3016 0.2948 0.3392 -0.0258 0.1217  -0.0028 107 GLN   B CA  
5705 C  C   A GLN   B 107 ? 0.2706 0.2739 0.3228 -0.0091 0.1060  -0.0003 107 GLN   B C   
5706 C  C   B GLN   B 107 ? 0.2713 0.2761 0.3180 -0.0148 0.1031  -0.0066 107 GLN   B C   
5707 O  O   A GLN   B 107 ? 0.2634 0.2733 0.3500 -0.0020 0.0846  -0.0152 107 GLN   B O   
5708 O  O   B GLN   B 107 ? 0.2664 0.2803 0.3454 -0.0111 0.0816  -0.0229 107 GLN   B O   
5709 C  CB  A GLN   B 107 ? 0.3248 0.3280 0.4068 -0.0173 0.1124  0.0125  107 GLN   B CB  
5710 C  CB  B GLN   B 107 ? 0.3276 0.3291 0.3999 -0.0215 0.1056  0.0015  107 GLN   B CB  
5711 C  CG  A GLN   B 107 ? 0.3501 0.3572 0.4696 -0.0123 0.0825  0.0128  107 GLN   B CG  
5712 C  CG  B GLN   B 107 ? 0.3558 0.3594 0.4635 -0.0136 0.0770  0.0028  107 GLN   B CG  
5713 C  CD  A GLN   B 107 ? 0.3681 0.3789 0.5195 -0.0110 0.0615  0.0172  107 GLN   B CD  
5714 C  CD  B GLN   B 107 ? 0.3769 0.3824 0.5147 -0.0097 0.0556  0.0072  107 GLN   B CD  
5715 O  OE1 A GLN   B 107 ? 0.3747 0.3874 0.5383 -0.0086 0.0590  0.0161  107 GLN   B OE1 
5716 O  OE1 B GLN   B 107 ? 0.3851 0.3917 0.5345 -0.0075 0.0538  0.0070  107 GLN   B OE1 
5717 N  NE2 A GLN   B 107 ? 0.3755 0.3854 0.5364 -0.0097 0.0519  0.0226  107 GLN   B NE2 
5718 N  NE2 B GLN   B 107 ? 0.3858 0.3901 0.5310 -0.0072 0.0454  0.0113  107 GLN   B NE2 
5735 N  N   . LEU   B 108 ? 0.2458 0.2521 0.2884 0.0031  0.0935  -0.0009 108 LEU   B N   
5736 C  CA  . LEU   B 108 ? 0.2216 0.2279 0.2425 0.0228  0.0658  0.0148  108 LEU   B CA  
5737 C  C   . LEU   B 108 ? 0.1901 0.1866 0.2292 0.0246  0.0370  0.0305  108 LEU   B C   
5738 O  O   . LEU   B 108 ? 0.1926 0.1782 0.2310 0.0213  0.0236  0.0219  108 LEU   B O   
5739 C  CB  . LEU   B 108 ? 0.2385 0.2499 0.2211 0.0189  0.0670  0.0153  108 LEU   B CB  
5740 C  CG  . LEU   B 108 ? 0.2536 0.2834 0.2268 0.0241  0.0539  -0.0030 108 LEU   B CG  
5741 C  CD1 . LEU   B 108 ? 0.2611 0.2991 0.2189 0.0154  0.0541  -0.0010 108 LEU   B CD1 
5742 C  CD2 . LEU   B 108 ? 0.2675 0.2964 0.2434 0.0320  0.0469  -0.0141 108 LEU   B CD2 
5755 N  N   . LEU   B 109 ? 0.1790 0.1678 0.2226 0.0186  0.0385  0.0250  109 LEU   B N   
5756 C  CA  . LEU   B 109 ? 0.1595 0.1479 0.2344 0.0138  0.0345  0.0272  109 LEU   B CA  
5757 C  C   . LEU   B 109 ? 0.1518 0.1381 0.2345 0.0079  0.0323  0.0212  109 LEU   B C   
5758 O  O   . LEU   B 109 ? 0.1445 0.1347 0.2294 0.0084  0.0290  0.0326  109 LEU   B O   
5759 C  CB  . LEU   B 109 ? 0.1718 0.1406 0.2334 0.0127  0.0242  0.0310  109 LEU   B CB  
5760 C  CG  . LEU   B 109 ? 0.1674 0.1378 0.2252 0.0119  0.0179  0.0225  109 LEU   B CG  
5761 C  CD1 . LEU   B 109 ? 0.1639 0.1495 0.2165 0.0110  0.0294  0.0181  109 LEU   B CD1 
5762 C  CD2 . LEU   B 109 ? 0.1870 0.1451 0.2394 0.0118  0.0101  0.0147  109 LEU   B CD2 
5774 N  N   . LYS   B 110 ? 0.1434 0.1391 0.2268 -0.0008 0.0278  0.0254  110 LYS   B N   
5775 C  CA  . LYS   B 110 ? 0.1430 0.1344 0.2217 0.0004  0.0266  0.0170  110 LYS   B CA  
5776 C  C   . LYS   B 110 ? 0.1411 0.1326 0.2127 0.0026  0.0280  0.0168  110 LYS   B C   
5777 O  O   . LYS   B 110 ? 0.1398 0.1312 0.2109 -0.0056 0.0196  0.0097  110 LYS   B O   
5778 C  CB  . LYS   B 110 ? 0.1453 0.1371 0.2484 -0.0058 0.0238  0.0153  110 LYS   B CB  
5779 C  CG  . LYS   B 110 ? 0.1476 0.1343 0.2581 -0.0078 0.0178  0.0211  110 LYS   B CG  
5780 C  CD  . LYS   B 110 ? 0.1509 0.1349 0.2725 -0.0062 0.0107  0.0213  110 LYS   B CD  
5781 C  CE  . LYS   B 110 ? 0.1503 0.1494 0.2773 -0.0014 0.0112  0.0042  110 LYS   B CE  
5782 N  NZ  . LYS   B 110 ? 0.1477 0.1644 0.2683 0.0010  0.0069  0.0010  110 LYS   B NZ  
5796 N  N   . SER   B 111 ? 0.1479 0.1329 0.2176 -0.0025 0.0249  0.0212  111 SER   B N   
5797 C  CA  . SER   B 111 ? 0.1457 0.1394 0.2088 -0.0009 0.0154  0.0232  111 SER   B CA  
5798 C  C   . SER   B 111 ? 0.1402 0.1355 0.2037 -0.0023 0.0106  0.0075  111 SER   B C   
5799 O  O   . SER   B 111 ? 0.1445 0.1368 0.2081 -0.0057 0.0031  0.0105  111 SER   B O   
5800 C  CB  . SER   B 111 ? 0.1621 0.1588 0.2122 0.0016  0.0305  0.0269  111 SER   B CB  
5801 O  OG  . SER   B 111 ? 0.1834 0.1974 0.2275 0.0047  0.0385  0.0308  111 SER   B OG  
5807 N  N   . ALA   B 112 ? 0.1292 0.1365 0.2158 0.0043  0.0232  0.0189  112 ALA   B N   
5808 C  CA  . ALA   B 112 ? 0.1341 0.1392 0.2014 -0.0006 0.0069  0.0089  112 ALA   B CA  
5809 C  C   . ALA   B 112 ? 0.1253 0.1292 0.1907 -0.0031 0.0072  0.0093  112 ALA   B C   
5810 O  O   . ALA   B 112 ? 0.1274 0.1309 0.2006 -0.0034 0.0061  0.0031  112 ALA   B O   
5811 C  CB  . ALA   B 112 ? 0.1436 0.1418 0.2084 0.0031  0.0097  0.0154  112 ALA   B CB  
5817 N  N   . TYR   B 113 ? 0.1261 0.1208 0.2024 -0.0001 0.0075  0.0090  113 TYR   B N   
5818 C  CA  . TYR   B 113 ? 0.1251 0.1213 0.1939 -0.0043 0.0095  -0.0043 113 TYR   B CA  
5819 C  C   . TYR   B 113 ? 0.1221 0.1094 0.1897 -0.0058 0.0024  0.0044  113 TYR   B C   
5820 O  O   . TYR   B 113 ? 0.1294 0.1179 0.1904 -0.0038 0.0022  0.0009  113 TYR   B O   
5821 C  CB  . TYR   B 113 ? 0.1290 0.1143 0.2000 -0.0044 0.0165  0.0111  113 TYR   B CB  
5822 C  CG  . TYR   B 113 ? 0.1291 0.1198 0.2104 -0.0073 0.0067  0.0123  113 TYR   B CG  
5823 C  CD1 . TYR   B 113 ? 0.1346 0.1193 0.2223 -0.0030 0.0102  0.0174  113 TYR   B CD1 
5824 C  CD2 . TYR   B 113 ? 0.1364 0.1147 0.2166 -0.0043 0.0039  0.0087  113 TYR   B CD2 
5825 C  CE1 . TYR   B 113 ? 0.1371 0.1282 0.2220 -0.0016 0.0188  0.0108  113 TYR   B CE1 
5826 C  CE2 . TYR   B 113 ? 0.1425 0.1104 0.2213 0.0017  0.0044  0.0143  113 TYR   B CE2 
5827 C  CZ  . TYR   B 113 ? 0.1359 0.1227 0.2327 0.0073  0.0093  0.0057  113 TYR   B CZ  
5828 O  OH  . TYR   B 113 ? 0.1409 0.1218 0.2474 0.0136  0.0164  0.0103  113 TYR   B OH  
5838 N  N   . GLU   B 114 ? 0.1228 0.1107 0.1969 -0.0037 0.0092  0.0097  114 GLU   B N   
5839 C  CA  . GLU   B 114 ? 0.1198 0.1098 0.1981 -0.0029 0.0088  0.0002  114 GLU   B CA  
5840 C  C   . GLU   B 114 ? 0.1198 0.1197 0.1914 -0.0007 0.0056  0.0012  114 GLU   B C   
5841 O  O   . GLU   B 114 ? 0.1213 0.1202 0.2056 0.0007  0.0022  0.0094  114 GLU   B O   
5842 C  CB  . GLU   B 114 ? 0.1226 0.1169 0.2036 -0.0028 0.0082  0.0058  114 GLU   B CB  
5843 C  CG  . GLU   B 114 ? 0.1313 0.1188 0.2076 -0.0022 0.0064  0.0080  114 GLU   B CG  
5844 C  CD  . GLU   B 114 ? 0.1303 0.1267 0.2129 -0.0077 0.0056  0.0089  114 GLU   B CD  
5845 O  OE1 . GLU   B 114 ? 0.1294 0.1397 0.2092 -0.0061 0.0162  0.0122  114 GLU   B OE1 
5846 O  OE2 . GLU   B 114 ? 0.1269 0.1406 0.2344 -0.0163 0.0075  0.0103  114 GLU   B OE2 
5853 N  N   . ASN   B 115 ? 0.1274 0.1145 0.1782 -0.0065 0.0047  0.0045  115 ASN   B N   
5854 C  CA  . ASN   B 115 ? 0.1275 0.1186 0.1735 -0.0071 0.0024  0.0067  115 ASN   B CA  
5855 C  C   . ASN   B 115 ? 0.1215 0.1175 0.1689 -0.0139 0.0004  0.0012  115 ASN   B C   
5856 O  O   . ASN   B 115 ? 0.1301 0.1196 0.1841 -0.0129 0.0023  0.0049  115 ASN   B O   
5857 C  CB  . ASN   B 115 ? 0.1372 0.1269 0.1760 -0.0115 0.0047  0.0045  115 ASN   B CB  
5858 C  CG  . ASN   B 115 ? 0.1460 0.1316 0.1820 0.0050  0.0052  -0.0025 115 ASN   B CG  
5859 O  OD1 . ASN   B 115 ? 0.1908 0.1492 0.1956 0.0017  0.0078  -0.0086 115 ASN   B OD1 
5860 N  ND2 . ASN   B 115 ? 0.1415 0.1429 0.1817 -0.0027 0.0039  0.0089  115 ASN   B ND2 
5867 N  N   . PHE   B 116 ? 0.1258 0.1174 0.1589 -0.0039 0.0028  -0.0023 116 PHE   B N   
5868 C  CA  . PHE   B 116 ? 0.1270 0.1223 0.1702 -0.0095 -0.0013 -0.0018 116 PHE   B CA  
5869 C  C   . PHE   B 116 ? 0.1281 0.1111 0.1697 -0.0097 -0.0056 0.0078  116 PHE   B C   
5870 O  O   . PHE   B 116 ? 0.1321 0.1222 0.1776 -0.0038 -0.0077 0.0050  116 PHE   B O   
5871 C  CB  . PHE   B 116 ? 0.1236 0.1152 0.1730 -0.0035 -0.0080 0.0059  116 PHE   B CB  
5872 C  CG  . PHE   B 116 ? 0.1198 0.1210 0.1714 -0.0042 -0.0034 -0.0035 116 PHE   B CG  
5873 C  CD1 . PHE   B 116 ? 0.1296 0.1253 0.1871 -0.0015 0.0015  0.0042  116 PHE   B CD1 
5874 C  CD2 . PHE   B 116 ? 0.1249 0.1303 0.1687 -0.0033 -0.0005 -0.0038 116 PHE   B CD2 
5875 C  CE1 . PHE   B 116 ? 0.1337 0.1242 0.1881 -0.0065 -0.0068 0.0087  116 PHE   B CE1 
5876 C  CE2 . PHE   B 116 ? 0.1262 0.1252 0.1676 -0.0008 0.0007  0.0023  116 PHE   B CE2 
5877 C  CZ  . PHE   B 116 ? 0.1211 0.1285 0.1754 -0.0019 -0.0097 0.0152  116 PHE   B CZ  
5887 N  N   . ASN   B 117 ? 0.1316 0.1150 0.1939 -0.0053 -0.0074 0.0068  117 ASN   B N   
5888 C  CA  . ASN   B 117 ? 0.1349 0.1165 0.1900 -0.0006 -0.0096 0.0060  117 ASN   B CA  
5889 C  C   . ASN   B 117 ? 0.1366 0.1111 0.2033 -0.0010 -0.0065 0.0029  117 ASN   B C   
5890 O  O   . ASN   B 117 ? 0.1421 0.1229 0.2238 -0.0036 -0.0270 0.0097  117 ASN   B O   
5891 C  CB  . ASN   B 117 ? 0.1351 0.1231 0.1905 -0.0034 -0.0078 0.0001  117 ASN   B CB  
5892 C  CG  . ASN   B 117 ? 0.1252 0.1280 0.2087 0.0023  -0.0032 -0.0078 117 ASN   B CG  
5893 O  OD1 . ASN   B 117 ? 0.1489 0.1273 0.2117 -0.0168 0.0021  -0.0029 117 ASN   B OD1 
5894 N  ND2 . ASN   B 117 ? 0.1311 0.1271 0.1948 -0.0019 -0.0022 -0.0046 117 ASN   B ND2 
5901 N  N   . GLN   B 118 ? 0.1392 0.1105 0.1913 -0.0089 -0.0220 -0.0012 118 GLN   B N   
5902 C  CA  . GLN   B 118 ? 0.1393 0.1176 0.1956 0.0010  -0.0134 0.0062  118 GLN   B CA  
5903 C  C   . GLN   B 118 ? 0.1412 0.1163 0.1993 0.0013  -0.0072 0.0010  118 GLN   B C   
5904 O  O   . GLN   B 118 ? 0.1588 0.1154 0.2405 -0.0089 0.0056  0.0014  118 GLN   B O   
5905 C  CB  . GLN   B 118 ? 0.1465 0.1251 0.2072 -0.0024 -0.0128 0.0029  118 GLN   B CB  
5906 C  CG  . GLN   B 118 ? 0.1580 0.1260 0.2055 0.0083  -0.0014 -0.0094 118 GLN   B CG  
5907 C  CD  . GLN   B 118 ? 0.1625 0.1217 0.1974 0.0005  -0.0006 -0.0088 118 GLN   B CD  
5908 O  OE1 . GLN   B 118 ? 0.1642 0.1250 0.2245 0.0014  0.0102  0.0045  118 GLN   B OE1 
5909 N  NE2 . GLN   B 118 ? 0.1691 0.1239 0.2058 0.0056  -0.0114 0.0062  118 GLN   B NE2 
5918 N  N   . HIS   B 119 ? 0.1428 0.1183 0.1744 -0.0050 -0.0115 0.0050  119 HIS   B N   
5919 C  CA  . HIS   B 119 ? 0.1546 0.1307 0.1751 -0.0037 -0.0130 0.0041  119 HIS   B CA  
5920 C  C   . HIS   B 119 ? 0.1573 0.1316 0.1642 -0.0044 -0.0265 0.0075  119 HIS   B C   
5921 O  O   . HIS   B 119 ? 0.1624 0.1308 0.1810 -0.0280 -0.0167 0.0089  119 HIS   B O   
5922 C  CB  . HIS   B 119 ? 0.1552 0.1421 0.1764 0.0029  -0.0196 -0.0025 119 HIS   B CB  
5923 C  CG  . HIS   B 119 ? 0.1646 0.1649 0.1916 0.0138  -0.0348 -0.0215 119 HIS   B CG  
5924 N  ND1 . HIS   B 119 ? 0.1807 0.1801 0.2186 0.0072  -0.0451 -0.0418 119 HIS   B ND1 
5925 C  CD2 . HIS   B 119 ? 0.1825 0.1866 0.2003 0.0361  -0.0425 -0.0233 119 HIS   B CD2 
5926 C  CE1 . HIS   B 119 ? 0.1976 0.1985 0.2198 0.0215  -0.0530 -0.0479 119 HIS   B CE1 
5927 N  NE2 . HIS   B 119 ? 0.2019 0.2114 0.2026 0.0328  -0.0443 -0.0380 119 HIS   B NE2 
5935 N  N   . GLU   B 120 ? 0.1698 0.1364 0.1658 -0.0127 -0.0328 0.0155  120 GLU   B N   
5936 C  CA  . GLU   B 120 ? 0.1970 0.1491 0.1764 -0.0012 -0.0441 0.0246  120 GLU   B CA  
5937 C  C   . GLU   B 120 ? 0.1755 0.1350 0.1698 -0.0116 -0.0329 0.0259  120 GLU   B C   
5938 O  O   . GLU   B 120 ? 0.1759 0.1490 0.1674 -0.0140 -0.0327 0.0162  120 GLU   B O   
5939 C  CB  . GLU   B 120 ? 0.2610 0.1890 0.2400 0.0202  -0.0720 0.0452  120 GLU   B CB  
5940 C  CG  . GLU   B 120 ? 0.3181 0.2612 0.3465 0.0286  -0.0975 0.0706  120 GLU   B CG  
5941 C  CD  . GLU   B 120 ? 0.3631 0.3269 0.4617 0.0259  -0.1027 0.0869  120 GLU   B CD  
5942 O  OE1 . GLU   B 120 ? 0.3836 0.3500 0.5029 0.0180  -0.0940 0.1013  120 GLU   B OE1 
5943 O  OE2 . GLU   B 120 ? 0.3846 0.3546 0.5188 0.0256  -0.1059 0.0805  120 GLU   B OE2 
5950 N  N   . VAL   B 121 ? 0.1621 0.1353 0.1635 -0.0152 -0.0219 0.0175  121 VAL   B N   
5951 C  CA  . VAL   B 121 ? 0.1641 0.1434 0.1509 -0.0189 -0.0187 0.0149  121 VAL   B CA  
5952 C  C   . VAL   B 121 ? 0.1548 0.1374 0.1516 -0.0226 -0.0180 0.0176  121 VAL   B C   
5953 O  O   . VAL   B 121 ? 0.1647 0.1330 0.1800 -0.0283 -0.0256 0.0044  121 VAL   B O   
5954 C  CB  . VAL   B 121 ? 0.1856 0.1816 0.1624 -0.0023 -0.0275 0.0192  121 VAL   B CB  
5955 C  CG1 . VAL   B 121 ? 0.1931 0.1911 0.1946 -0.0171 -0.0151 0.0184  121 VAL   B CG1 
5956 C  CG2 . VAL   B 121 ? 0.2084 0.2083 0.1668 0.0066  -0.0218 0.0086  121 VAL   B CG2 
5966 N  N   . LEU   B 122 ? 0.1475 0.1297 0.1509 -0.0153 -0.0227 0.0104  122 LEU   B N   
5967 C  CA  . LEU   B 122 ? 0.1405 0.1397 0.1379 -0.0209 -0.0193 0.0098  122 LEU   B CA  
5968 C  C   . LEU   B 122 ? 0.1405 0.1267 0.1488 -0.0271 -0.0187 0.0101  122 LEU   B C   
5969 O  O   . LEU   B 122 ? 0.1531 0.1301 0.1809 -0.0267 -0.0279 0.0053  122 LEU   B O   
5970 C  CB  . LEU   B 122 ? 0.1602 0.1541 0.1777 -0.0006 -0.0204 0.0137  122 LEU   B CB  
5971 C  CG  . LEU   B 122 ? 0.1505 0.1583 0.1808 -0.0166 -0.0128 0.0070  122 LEU   B CG  
5972 C  CD1 . LEU   B 122 ? 0.1586 0.1785 0.1918 -0.0186 -0.0116 0.0040  122 LEU   B CD1 
5973 C  CD2 . LEU   B 122 ? 0.1552 0.1570 0.1573 -0.0134 -0.0077 -0.0024 122 LEU   B CD2 
5985 N  N   . LEU   B 123 ? 0.1410 0.1207 0.1460 -0.0231 -0.0127 0.0076  123 LEU   B N   
5986 C  CA  . LEU   B 123 ? 0.1449 0.1253 0.1429 -0.0221 -0.0185 0.0049  123 LEU   B CA  
5987 C  C   . LEU   B 123 ? 0.1387 0.1204 0.1496 -0.0263 -0.0146 0.0024  123 LEU   B C   
5988 O  O   . LEU   B 123 ? 0.1515 0.1233 0.1509 -0.0303 -0.0150 0.0067  123 LEU   B O   
5989 C  CB  . LEU   B 123 ? 0.1500 0.1280 0.1497 -0.0217 -0.0131 -0.0013 123 LEU   B CB  
5990 C  CG  . LEU   B 123 ? 0.1479 0.1337 0.1640 -0.0152 -0.0048 0.0110  123 LEU   B CG  
5991 C  CD1 . LEU   B 123 ? 0.1587 0.1347 0.1698 -0.0184 0.0011  -0.0104 123 LEU   B CD1 
5992 C  CD2 . LEU   B 123 ? 0.1597 0.1406 0.1840 -0.0157 0.0010  0.0164  123 LEU   B CD2 
6004 N  N   . ALA   B 124 ? 0.1361 0.1201 0.1511 -0.0177 -0.0014 0.0001  124 ALA   B N   
6005 C  CA  . ALA   B 124 ? 0.1318 0.1214 0.1612 -0.0165 -0.0054 -0.0104 124 ALA   B CA  
6006 C  C   . ALA   B 124 ? 0.1297 0.1177 0.1633 -0.0156 -0.0101 0.0027  124 ALA   B C   
6007 O  O   . ALA   B 124 ? 0.1420 0.1250 0.1608 -0.0144 -0.0082 -0.0006 124 ALA   B O   
6008 C  CB  . ALA   B 124 ? 0.1400 0.1275 0.1700 -0.0092 -0.0004 0.0004  124 ALA   B CB  
6014 N  N   . PRO   B 125 ? 0.1395 0.1200 0.1474 -0.0138 -0.0147 0.0108  125 PRO   B N   
6015 C  CA  . PRO   B 125 ? 0.1480 0.1253 0.1704 -0.0115 -0.0143 0.0202  125 PRO   B CA  
6016 C  C   . PRO   B 125 ? 0.1394 0.1188 0.1861 -0.0153 -0.0111 0.0085  125 PRO   B C   
6017 O  O   . PRO   B 125 ? 0.1417 0.1167 0.2064 -0.0115 -0.0022 0.0168  125 PRO   B O   
6018 C  CB  . PRO   B 125 ? 0.1497 0.1473 0.1860 -0.0170 -0.0211 0.0307  125 PRO   B CB  
6019 C  CG  . PRO   B 125 ? 0.1587 0.1521 0.1698 -0.0249 -0.0175 0.0175  125 PRO   B CG  
6020 C  CD  . PRO   B 125 ? 0.1527 0.1321 0.1512 -0.0304 -0.0096 0.0119  125 PRO   B CD  
6028 N  N   . LEU   B 126 ? 0.1458 0.1151 0.1992 -0.0134 0.0097  0.0124  126 LEU   B N   
6029 C  CA  . LEU   B 126 ? 0.1564 0.1223 0.2042 -0.0114 0.0190  0.0114  126 LEU   B CA  
6030 C  C   . LEU   B 126 ? 0.1502 0.1319 0.2032 -0.0004 0.0208  0.0165  126 LEU   B C   
6031 O  O   . LEU   B 126 ? 0.1680 0.1598 0.2138 0.0150  -0.0020 -0.0051 126 LEU   B O   
6032 C  CB  . LEU   B 126 ? 0.1704 0.1292 0.2361 -0.0186 0.0198  0.0103  126 LEU   B CB  
6033 C  CG  . LEU   B 126 ? 0.1843 0.1385 0.2407 -0.0273 0.0238  -0.0045 126 LEU   B CG  
6034 C  CD1 . LEU   B 126 ? 0.1971 0.1452 0.2839 -0.0228 0.0196  -0.0093 126 LEU   B CD1 
6035 C  CD2 . LEU   B 126 ? 0.1877 0.1494 0.2377 -0.0364 0.0122  -0.0027 126 LEU   B CD2 
6047 N  N   . LEU   B 127 ? 0.1466 0.1218 0.2035 0.0014  0.0242  0.0129  127 LEU   B N   
6048 C  CA  . LEU   B 127 ? 0.1413 0.1307 0.2124 -0.0048 0.0232  0.0173  127 LEU   B CA  
6049 C  C   . LEU   B 127 ? 0.1382 0.1304 0.2124 -0.0023 0.0187  0.0165  127 LEU   B C   
6050 O  O   . LEU   B 127 ? 0.1429 0.1320 0.2171 -0.0136 0.0113  0.0205  127 LEU   B O   
6051 C  CB  . LEU   B 127 ? 0.1568 0.1277 0.2252 -0.0015 0.0148  0.0237  127 LEU   B CB  
6052 C  CG  . LEU   B 127 ? 0.1709 0.1315 0.2358 0.0003  0.0157  0.0232  127 LEU   B CG  
6053 C  CD1 . LEU   B 127 ? 0.1697 0.1291 0.2378 0.0038  0.0096  0.0199  127 LEU   B CD1 
6054 C  CD2 . LEU   B 127 ? 0.1743 0.1455 0.2433 -0.0073 0.0204  0.0307  127 LEU   B CD2 
6066 N  N   . SER   B 128 ? 0.1466 0.1287 0.2061 -0.0003 0.0032  0.0139  128 SER   B N   
6067 C  CA  . SER   B 128 ? 0.1568 0.1387 0.2015 0.0079  0.0022  0.0192  128 SER   B CA  
6068 C  C   . SER   B 128 ? 0.1757 0.1374 0.2274 0.0089  -0.0142 0.0179  128 SER   B C   
6069 O  O   . SER   B 128 ? 0.1889 0.1422 0.2598 0.0084  -0.0084 0.0335  128 SER   B O   
6070 C  CB  . SER   B 128 ? 0.1661 0.1414 0.2034 0.0084  0.0057  0.0318  128 SER   B CB  
6071 O  OG  . SER   B 128 ? 0.1759 0.1527 0.2114 0.0136  0.0124  0.0351  128 SER   B OG  
6077 N  N   . ALA   B 129 ? 0.1883 0.1390 0.2447 0.0267  -0.0140 0.0074  129 ALA   B N   
6078 C  CA  . ALA   B 129 ? 0.2015 0.1519 0.2571 0.0294  -0.0146 -0.0027 129 ALA   B CA  
6079 C  C   . ALA   B 129 ? 0.1879 0.1447 0.2391 0.0236  0.0049  0.0067  129 ALA   B C   
6080 O  O   . ALA   B 129 ? 0.1734 0.1490 0.2465 0.0172  -0.0050 0.0114  129 ALA   B O   
6081 C  CB  . ALA   B 129 ? 0.2240 0.1736 0.2864 0.0358  -0.0070 -0.0124 129 ALA   B CB  
6087 N  N   . GLY   B 130 ? 0.1859 0.1418 0.2536 0.0269  0.0120  -0.0004 130 GLY   B N   
6088 C  CA  . GLY   B 130 ? 0.1908 0.1538 0.2638 0.0257  0.0313  -0.0035 130 GLY   B CA  
6089 C  C   . GLY   B 130 ? 0.1912 0.1539 0.2572 0.0215  0.0187  0.0060  130 GLY   B C   
6090 O  O   . GLY   B 130 ? 0.2064 0.1705 0.2597 0.0153  0.0045  0.0122  130 GLY   B O   
6094 N  N   . ILE   B 131 ? 0.1801 0.1729 0.2594 0.0363  0.0237  0.0100  131 ILE   B N   
6095 C  CA  . ILE   B 131 ? 0.2034 0.1885 0.2520 0.0325  0.0078  0.0219  131 ILE   B CA  
6096 C  C   . ILE   B 131 ? 0.2168 0.1770 0.2248 0.0256  0.0077  0.0298  131 ILE   B C   
6097 O  O   . ILE   B 131 ? 0.2433 0.1919 0.2339 0.0299  -0.0095 0.0244  131 ILE   B O   
6098 C  CB  . ILE   B 131 ? 0.2086 0.2261 0.2808 0.0348  -0.0014 0.0280  131 ILE   B CB  
6099 C  CG1 . ILE   B 131 ? 0.2083 0.2460 0.2854 0.0108  0.0091  0.0265  131 ILE   B CG1 
6100 C  CG2 . ILE   B 131 ? 0.2114 0.2452 0.3005 0.0376  -0.0064 0.0215  131 ILE   B CG2 
6101 C  CD1 . ILE   B 131 ? 0.2164 0.2666 0.2932 -0.0075 -0.0013 0.0347  131 ILE   B CD1 
6113 N  N   . PHE   B 132 ? 0.2010 0.1564 0.2191 0.0204  0.0199  0.0279  132 PHE   B N   
6114 C  CA  . PHE   B 132 ? 0.2084 0.1569 0.2182 0.0088  0.0327  0.0177  132 PHE   B CA  
6115 C  C   . PHE   B 132 ? 0.2265 0.1745 0.2294 0.0087  0.0399  0.0178  132 PHE   B C   
6116 O  O   . PHE   B 132 ? 0.2440 0.1965 0.2526 0.0033  0.0485  0.0229  132 PHE   B O   
6117 C  CB  . PHE   B 132 ? 0.1882 0.1610 0.2057 0.0118  0.0322  0.0187  132 PHE   B CB  
6118 C  CG  . PHE   B 132 ? 0.1804 0.1658 0.2108 0.0161  0.0227  0.0109  132 PHE   B CG  
6119 C  CD1 . PHE   B 132 ? 0.1892 0.1675 0.2402 0.0097  0.0267  0.0195  132 PHE   B CD1 
6120 C  CD2 . PHE   B 132 ? 0.1870 0.1629 0.1860 0.0243  0.0233  0.0243  132 PHE   B CD2 
6121 C  CE1 . PHE   B 132 ? 0.1946 0.1691 0.2451 0.0126  0.0294  0.0195  132 PHE   B CE1 
6122 C  CE2 . PHE   B 132 ? 0.1925 0.1678 0.1848 0.0228  0.0154  0.0170  132 PHE   B CE2 
6123 C  CZ  . PHE   B 132 ? 0.1966 0.1680 0.2203 0.0151  0.0080  0.0254  132 PHE   B CZ  
6133 N  N   . GLY   B 133 ? 0.2236 0.1679 0.2190 0.0095  0.0343  0.0292  133 GLY   B N   
6134 C  CA  . GLY   B 133 ? 0.2334 0.1776 0.2250 -0.0148 0.0256  0.0398  133 GLY   B CA  
6135 C  C   . GLY   B 133 ? 0.2367 0.1830 0.2336 -0.0290 0.0316  0.0426  133 GLY   B C   
6136 O  O   . GLY   B 133 ? 0.2538 0.1962 0.2875 -0.0421 0.0299  0.0536  133 GLY   B O   
6140 N  N   . ALA   B 134 ? 0.2207 0.1839 0.2192 -0.0272 0.0302  0.0208  134 ALA   B N   
6141 C  CA  . ALA   B 134 ? 0.2174 0.1801 0.2367 -0.0233 0.0348  0.0043  134 ALA   B CA  
6142 C  C   . ALA   B 134 ? 0.2251 0.1706 0.2415 -0.0134 0.0347  0.0191  134 ALA   B C   
6143 O  O   . ALA   B 134 ? 0.2259 0.1915 0.2578 -0.0012 0.0256  0.0083  134 ALA   B O   
6144 C  CB  . ALA   B 134 ? 0.2153 0.1782 0.2554 -0.0104 0.0271  -0.0019 134 ALA   B CB  
6150 N  N   . ASP   B 135 ? 0.2427 0.1623 0.2344 -0.0134 0.0191  0.0227  135 ASP   B N   
6151 C  CA  . ASP   B 135 ? 0.2588 0.1574 0.2500 -0.0126 0.0041  0.0309  135 ASP   B CA  
6152 C  C   . ASP   B 135 ? 0.2394 0.1500 0.2400 -0.0032 0.0100  0.0280  135 ASP   B C   
6153 O  O   . ASP   B 135 ? 0.2294 0.1484 0.2555 -0.0011 0.0183  0.0352  135 ASP   B O   
6154 C  CB  . ASP   B 135 ? 0.2877 0.1666 0.2706 -0.0353 -0.0003 0.0398  135 ASP   B CB  
6155 C  CG  . ASP   B 135 ? 0.3135 0.1716 0.3114 -0.0557 0.0013  0.0324  135 ASP   B CG  
6156 O  OD1 . ASP   B 135 ? 0.3238 0.1635 0.3115 -0.0388 -0.0050 0.0277  135 ASP   B OD1 
6157 O  OD2 . ASP   B 135 ? 0.3328 0.2111 0.3646 -0.0684 0.0012  0.0121  135 ASP   B OD2 
6162 N  N   . PRO   B 136 ? 0.2308 0.1541 0.2489 0.0150  -0.0037 0.0206  136 PRO   B N   
6163 C  CA  . PRO   B 136 ? 0.2063 0.1481 0.2527 0.0178  -0.0041 0.0110  136 PRO   B CA  
6164 C  C   . PRO   B 136 ? 0.1888 0.1421 0.2617 0.0127  -0.0013 0.0060  136 PRO   B C   
6165 O  O   . PRO   B 136 ? 0.1689 0.1335 0.2525 0.0115  -0.0041 0.0083  136 PRO   B O   
6166 C  CB  . PRO   B 136 ? 0.2103 0.1684 0.2734 0.0309  -0.0027 -0.0004 136 PRO   B CB  
6167 C  CG  . PRO   B 136 ? 0.2295 0.1715 0.2840 0.0344  -0.0038 0.0054  136 PRO   B CG  
6168 C  CD  . PRO   B 136 ? 0.2342 0.1636 0.2736 0.0385  -0.0009 0.0132  136 PRO   B CD  
6176 N  N   . ILE   B 137 ? 0.1976 0.1294 0.2666 0.0087  -0.0085 0.0085  137 ILE   B N   
6177 C  CA  . ILE   B 137 ? 0.2047 0.1214 0.2897 -0.0046 0.0020  -0.0013 137 ILE   B CA  
6178 C  C   . ILE   B 137 ? 0.1969 0.1279 0.2812 -0.0104 0.0078  0.0154  137 ILE   B C   
6179 O  O   . ILE   B 137 ? 0.1775 0.1336 0.2774 -0.0117 0.0079  0.0165  137 ILE   B O   
6180 C  CB  . ILE   B 137 ? 0.2351 0.1306 0.3293 -0.0052 0.0005  0.0028  137 ILE   B CB  
6181 C  CG1 . ILE   B 137 ? 0.2644 0.1501 0.3841 0.0014  0.0071  -0.0159 137 ILE   B CG1 
6182 C  CG2 . ILE   B 137 ? 0.2394 0.1354 0.3426 -0.0319 0.0003  0.0063  137 ILE   B CG2 
6183 C  CD1 . ILE   B 137 ? 0.2859 0.1807 0.4266 0.0171  0.0035  -0.0073 137 ILE   B CD1 
6195 N  N   A HIS   B 138 ? 0.1997 0.1276 0.2771 -0.0101 0.0198  0.0196  138 HIS   B N   
6196 N  N   B HIS   B 138 ? 0.1970 0.1329 0.2756 -0.0107 0.0097  0.0153  138 HIS   B N   
6197 C  CA  A HIS   B 138 ? 0.2034 0.1319 0.2769 -0.0030 0.0365  0.0195  138 HIS   B CA  
6198 C  CA  B HIS   B 138 ? 0.1986 0.1432 0.2719 -0.0045 0.0141  0.0116  138 HIS   B CA  
6199 C  C   A HIS   B 138 ? 0.1858 0.1356 0.2669 -0.0038 0.0367  0.0235  138 HIS   B C   
6200 C  C   B HIS   B 138 ? 0.1820 0.1412 0.2614 -0.0035 0.0274  0.0212  138 HIS   B C   
6201 O  O   A HIS   B 138 ? 0.1795 0.1400 0.2799 -0.0000 0.0347  0.0355  138 HIS   B O   
6202 O  O   B HIS   B 138 ? 0.1728 0.1468 0.2665 0.0019  0.0277  0.0350  138 HIS   B O   
6203 C  CB  A HIS   B 138 ? 0.2243 0.1396 0.2840 -0.0014 0.0609  0.0176  138 HIS   B CB  
6204 C  CB  B HIS   B 138 ? 0.2170 0.1623 0.2755 -0.0069 0.0102  0.0008  138 HIS   B CB  
6205 C  CG  A HIS   B 138 ? 0.2383 0.1556 0.2799 -0.0015 0.0850  0.0363  138 HIS   B CG  
6206 C  CG  B HIS   B 138 ? 0.2261 0.1837 0.2634 -0.0091 0.0021  0.0064  138 HIS   B CG  
6207 N  ND1 A HIS   B 138 ? 0.2460 0.1706 0.2984 0.0015  0.0949  0.0329  138 HIS   B ND1 
6208 N  ND1 B HIS   B 138 ? 0.2308 0.1989 0.2741 -0.0049 0.0051  0.0028  138 HIS   B ND1 
6209 C  CD2 A HIS   B 138 ? 0.2441 0.1629 0.2653 -0.0016 0.1003  0.0301  138 HIS   B CD2 
6210 C  CD2 B HIS   B 138 ? 0.2315 0.1935 0.2564 -0.0084 -0.0007 -0.0015 138 HIS   B CD2 
6211 C  CE1 A HIS   B 138 ? 0.2450 0.1678 0.2877 -0.0007 0.1007  0.0347  138 HIS   B CE1 
6212 C  CE1 B HIS   B 138 ? 0.2316 0.1980 0.2645 -0.0030 0.0033  0.0029  138 HIS   B CE1 
6213 N  NE2 A HIS   B 138 ? 0.2484 0.1634 0.2755 0.0030  0.1029  0.0252  138 HIS   B NE2 
6214 N  NE2 B HIS   B 138 ? 0.2322 0.1943 0.2576 -0.0043 -0.0035 -0.0055 138 HIS   B NE2 
6229 N  N   . SER   B 139 ? 0.1769 0.1309 0.2609 -0.0002 0.0300  0.0154  139 SER   B N   
6230 C  CA  . SER   B 139 ? 0.1730 0.1230 0.2466 -0.0085 0.0204  0.0026  139 SER   B CA  
6231 C  C   . SER   B 139 ? 0.1492 0.1149 0.2414 -0.0017 0.0150  0.0067  139 SER   B C   
6232 O  O   . SER   B 139 ? 0.1522 0.1163 0.2478 -0.0012 0.0048  0.0090  139 SER   B O   
6233 C  CB  . SER   B 139 ? 0.1833 0.1239 0.2512 0.0017  0.0073  0.0096  139 SER   B CB  
6234 O  OG  . SER   B 139 ? 0.1858 0.1238 0.2420 -0.0046 -0.0040 0.0209  139 SER   B OG  
6241 N  N   . LEU   B 140 ? 0.1535 0.1131 0.2455 -0.0063 0.0169  -0.0081 140 LEU   B N   
6242 C  CA  . LEU   B 140 ? 0.1496 0.1184 0.2422 -0.0057 0.0149  0.0035  140 LEU   B CA  
6243 C  C   . LEU   B 140 ? 0.1449 0.1164 0.2573 -0.0081 0.0033  0.0004  140 LEU   B C   
6244 O  O   . LEU   B 140 ? 0.1446 0.1206 0.2572 -0.0027 0.0007  0.0071  140 LEU   B O   
6245 C  CB  . LEU   B 140 ? 0.1478 0.1164 0.2434 -0.0103 0.0153  -0.0039 140 LEU   B CB  
6246 C  CG  . LEU   B 140 ? 0.1577 0.1227 0.2398 -0.0110 0.0066  0.0045  140 LEU   B CG  
6247 C  CD1 . LEU   B 140 ? 0.1660 0.1360 0.2648 -0.0133 0.0147  0.0045  140 LEU   B CD1 
6248 C  CD2 . LEU   B 140 ? 0.1764 0.1330 0.2558 -0.0041 -0.0040 -0.0104 140 LEU   B CD2 
6260 N  N   . ARG   B 141 ? 0.1393 0.1178 0.2659 -0.0092 0.0030  -0.0039 141 ARG   B N   
6261 C  CA  . ARG   B 141 ? 0.1379 0.1214 0.3049 -0.0142 0.0255  -0.0032 141 ARG   B CA  
6262 C  C   . ARG   B 141 ? 0.1333 0.1223 0.2839 -0.0122 0.0142  -0.0013 141 ARG   B C   
6263 O  O   . ARG   B 141 ? 0.1449 0.1263 0.2737 -0.0129 0.0014  -0.0147 141 ARG   B O   
6264 C  CB  . ARG   B 141 ? 0.1613 0.1316 0.3373 -0.0277 0.0252  -0.0036 141 ARG   B CB  
6265 C  CG  . ARG   B 141 ? 0.1987 0.1585 0.3630 -0.0277 0.0245  0.0030  141 ARG   B CG  
6266 C  CD  . ARG   B 141 ? 0.2475 0.1834 0.3665 -0.0169 0.0084  -0.0102 141 ARG   B CD  
6267 N  NE  . ARG   B 141 ? 0.2732 0.1850 0.3552 -0.0366 0.0149  -0.0135 141 ARG   B NE  
6268 C  CZ  . ARG   B 141 ? 0.2871 0.1657 0.3351 -0.0351 0.0210  -0.0324 141 ARG   B CZ  
6269 N  NH1 . ARG   B 141 ? 0.2988 0.1636 0.3312 -0.0316 0.0227  -0.0269 141 ARG   B NH1 
6270 N  NH2 . ARG   B 141 ? 0.2963 0.1850 0.3368 -0.0180 0.0100  -0.0205 141 ARG   B NH2 
6284 N  N   . VAL   B 142 ? 0.1413 0.1200 0.2650 -0.0071 0.0171  -0.0058 142 VAL   B N   
6285 C  CA  . VAL   B 142 ? 0.1385 0.1257 0.2642 -0.0047 0.0193  0.0006  142 VAL   B CA  
6286 C  C   . VAL   B 142 ? 0.1352 0.1221 0.2710 -0.0031 0.0152  -0.0018 142 VAL   B C   
6287 O  O   . VAL   B 142 ? 0.1419 0.1167 0.2793 -0.0022 0.0167  -0.0006 142 VAL   B O   
6288 C  CB  . VAL   B 142 ? 0.1514 0.1365 0.2677 -0.0001 0.0297  0.0084  142 VAL   B CB  
6289 C  CG1 . VAL   B 142 ? 0.1558 0.1310 0.2640 0.0075  0.0304  0.0085  142 VAL   B CG1 
6290 C  CG2 . VAL   B 142 ? 0.1773 0.1362 0.2762 -0.0000 0.0194  0.0145  142 VAL   B CG2 
6300 N  N   . CYS   B 143 ? 0.1329 0.1202 0.2440 -0.0023 0.0070  0.0094  143 CYS   B N   
6301 C  CA  . CYS   B 143 ? 0.1361 0.1234 0.2428 -0.0080 0.0054  0.0022  143 CYS   B CA  
6302 C  C   . CYS   B 143 ? 0.1310 0.1239 0.2510 -0.0085 0.0055  -0.0015 143 CYS   B C   
6303 O  O   . CYS   B 143 ? 0.1329 0.1187 0.2597 -0.0074 -0.0024 -0.0025 143 CYS   B O   
6304 C  CB  . CYS   B 143 ? 0.1433 0.1255 0.2333 -0.0072 0.0021  0.0005  143 CYS   B CB  
6305 S  SG  . CYS   B 143 ? 0.1445 0.1407 0.2299 -0.0049 0.0071  0.0076  143 CYS   B SG  
6311 N  N   . VAL   B 144 ? 0.1366 0.1259 0.2514 -0.0092 -0.0018 -0.0118 144 VAL   B N   
6312 C  CA  . VAL   B 144 ? 0.1399 0.1294 0.2817 -0.0197 -0.0082 -0.0172 144 VAL   B CA  
6313 C  C   . VAL   B 144 ? 0.1362 0.1328 0.2913 -0.0147 -0.0101 0.0013  144 VAL   B C   
6314 O  O   . VAL   B 144 ? 0.1486 0.1503 0.3099 0.0027  -0.0089 0.0200  144 VAL   B O   
6315 C  CB  . VAL   B 144 ? 0.1665 0.1491 0.3437 -0.0143 -0.0190 -0.0305 144 VAL   B CB  
6316 C  CG1 . VAL   B 144 ? 0.1936 0.1877 0.3764 -0.0099 -0.0268 -0.0292 144 VAL   B CG1 
6317 C  CG2 . VAL   B 144 ? 0.1797 0.1433 0.3367 -0.0019 -0.0277 -0.0391 144 VAL   B CG2 
6327 N  N   . ASP   B 145 ? 0.1419 0.1250 0.3036 -0.0141 0.0017  -0.0135 145 ASP   B N   
6328 C  CA  . ASP   B 145 ? 0.1389 0.1322 0.3233 -0.0105 0.0060  -0.0058 145 ASP   B CA  
6329 C  C   . ASP   B 145 ? 0.1353 0.1317 0.3046 -0.0073 0.0105  -0.0025 145 ASP   B C   
6330 O  O   . ASP   B 145 ? 0.1385 0.1494 0.3592 -0.0087 0.0118  -0.0263 145 ASP   B O   
6331 C  CB  . ASP   B 145 ? 0.1565 0.1414 0.3649 -0.0171 0.0207  -0.0011 145 ASP   B CB  
6332 C  CG  . ASP   B 145 ? 0.1670 0.1487 0.4087 -0.0306 0.0296  -0.0025 145 ASP   B CG  
6333 O  OD1 . ASP   B 145 ? 0.1723 0.1522 0.4209 -0.0266 0.0046  -0.0221 145 ASP   B OD1 
6334 O  OD2 . ASP   B 145 ? 0.2000 0.1593 0.4522 -0.0361 0.0468  0.0079  145 ASP   B OD2 
6339 N  N   . THR   B 146 ? 0.1284 0.1237 0.2570 -0.0103 0.0012  0.0010  146 THR   B N   
6340 C  CA  . THR   B 146 ? 0.1365 0.1199 0.2410 -0.0097 0.0018  -0.0005 146 THR   B CA  
6341 C  C   . THR   B 146 ? 0.1382 0.1218 0.2306 -0.0071 0.0010  -0.0004 146 THR   B C   
6342 O  O   . THR   B 146 ? 0.1458 0.1242 0.2324 -0.0033 -0.0032 0.0037  146 THR   B O   
6343 C  CB  . THR   B 146 ? 0.1406 0.1255 0.2408 -0.0044 0.0131  0.0078  146 THR   B CB  
6344 O  OG1 . THR   B 146 ? 0.1430 0.1240 0.2448 -0.0060 0.0159  0.0133  146 THR   B OG1 
6345 C  CG2 . THR   B 146 ? 0.1562 0.1309 0.2196 -0.0023 0.0099  0.0061  146 THR   B CG2 
6353 N  N   . VAL   B 147 ? 0.1395 0.1270 0.2191 -0.0053 0.0120  -0.0013 147 VAL   B N   
6354 C  CA  . VAL   B 147 ? 0.1409 0.1194 0.2179 -0.0148 -0.0034 -0.0064 147 VAL   B CA  
6355 C  C   . VAL   B 147 ? 0.1350 0.1250 0.2337 -0.0179 -0.0121 0.0001  147 VAL   B C   
6356 O  O   . VAL   B 147 ? 0.1452 0.1352 0.2328 -0.0221 -0.0289 -0.0079 147 VAL   B O   
6357 C  CB  . VAL   B 147 ? 0.1414 0.1312 0.1983 -0.0090 -0.0046 0.0024  147 VAL   B CB  
6358 C  CG1 . VAL   B 147 ? 0.1427 0.1437 0.1927 -0.0097 -0.0086 0.0029  147 VAL   B CG1 
6359 C  CG2 . VAL   B 147 ? 0.1534 0.1272 0.1958 -0.0108 0.0005  0.0018  147 VAL   B CG2 
6369 N  N   . ARG   B 148 ? 0.1337 0.1263 0.2256 -0.0105 -0.0196 -0.0023 148 ARG   B N   
6370 C  CA  . ARG   B 148 ? 0.1428 0.1350 0.2143 -0.0048 -0.0274 -0.0107 148 ARG   B CA  
6371 C  C   . ARG   B 148 ? 0.1513 0.1401 0.1987 -0.0069 -0.0273 -0.0088 148 ARG   B C   
6372 O  O   . ARG   B 148 ? 0.1666 0.1767 0.1999 -0.0230 -0.0358 0.0016  148 ARG   B O   
6373 C  CB  . ARG   B 148 ? 0.1492 0.1420 0.2240 -0.0031 -0.0307 -0.0176 148 ARG   B CB  
6374 C  CG  . ARG   B 148 ? 0.1515 0.1572 0.2340 -0.0110 -0.0241 -0.0393 148 ARG   B CG  
6375 C  CD  . ARG   B 148 ? 0.1611 0.1763 0.2441 0.0027  -0.0277 -0.0367 148 ARG   B CD  
6376 N  NE  . ARG   B 148 ? 0.1587 0.1724 0.2327 0.0180  -0.0271 -0.0384 148 ARG   B NE  
6377 C  CZ  . ARG   B 148 ? 0.1492 0.1628 0.2119 0.0064  -0.0194 -0.0221 148 ARG   B CZ  
6378 N  NH1 . ARG   B 148 ? 0.1476 0.1666 0.2142 -0.0061 -0.0070 -0.0150 148 ARG   B NH1 
6379 N  NH2 . ARG   B 148 ? 0.1699 0.1480 0.2140 0.0148  -0.0219 -0.0051 148 ARG   B NH2 
6393 N  N   . THR   B 149 ? 0.1525 0.1359 0.1968 -0.0117 -0.0297 0.0017  149 THR   B N   
6394 C  CA  . THR   B 149 ? 0.1535 0.1411 0.1931 -0.0149 -0.0300 0.0091  149 THR   B CA  
6395 C  C   . THR   B 149 ? 0.1499 0.1363 0.1888 -0.0135 -0.0271 0.0055  149 THR   B C   
6396 O  O   . THR   B 149 ? 0.1620 0.1345 0.1941 -0.0192 -0.0139 0.0011  149 THR   B O   
6397 C  CB  . THR   B 149 ? 0.1543 0.1379 0.1946 -0.0186 -0.0259 -0.0022 149 THR   B CB  
6398 O  OG1 . THR   B 149 ? 0.1604 0.1427 0.1817 -0.0232 -0.0316 -0.0010 149 THR   B OG1 
6399 C  CG2 . THR   B 149 ? 0.1622 0.1406 0.2103 -0.0052 -0.0181 -0.0050 149 THR   B CG2 
6407 N  N   . ASN   B 150 ? 0.1605 0.1329 0.1811 -0.0133 -0.0281 -0.0026 150 ASN   B N   
6408 C  CA  . ASN   B 150 ? 0.1665 0.1464 0.1850 -0.0212 -0.0207 -0.0032 150 ASN   B CA  
6409 C  C   . ASN   B 150 ? 0.1576 0.1424 0.1925 -0.0143 -0.0270 -0.0025 150 ASN   B C   
6410 O  O   . ASN   B 150 ? 0.1618 0.1401 0.2130 -0.0280 -0.0393 -0.0006 150 ASN   B O   
6411 C  CB  . ASN   B 150 ? 0.1847 0.1802 0.1988 -0.0278 -0.0398 0.0090  150 ASN   B CB  
6412 C  CG  . ASN   B 150 ? 0.2134 0.2229 0.2291 -0.0259 -0.0388 0.0253  150 ASN   B CG  
6413 O  OD1 . ASN   B 150 ? 0.2202 0.2456 0.2365 -0.0328 -0.0518 0.0227  150 ASN   B OD1 
6414 N  ND2 . ASN   B 150 ? 0.2288 0.2429 0.2542 -0.0120 -0.0500 0.0593  150 ASN   B ND2 
6421 N  N   . VAL   B 151 ? 0.1502 0.1389 0.1823 -0.0183 -0.0264 -0.0019 151 VAL   B N   
6422 C  CA  . VAL   B 151 ? 0.1446 0.1404 0.1810 -0.0216 -0.0254 0.0024  151 VAL   B CA  
6423 C  C   . VAL   B 151 ? 0.1506 0.1303 0.1818 -0.0296 -0.0227 -0.0003 151 VAL   B C   
6424 O  O   . VAL   B 151 ? 0.1573 0.1454 0.2042 -0.0317 -0.0172 -0.0110 151 VAL   B O   
6425 C  CB  . VAL   B 151 ? 0.1651 0.1564 0.1968 -0.0062 -0.0138 -0.0023 151 VAL   B CB  
6426 C  CG1 . VAL   B 151 ? 0.1767 0.1568 0.2130 -0.0154 -0.0019 -0.0202 151 VAL   B CG1 
6427 C  CG2 . VAL   B 151 ? 0.1797 0.1759 0.1881 0.0039  -0.0158 0.0128  151 VAL   B CG2 
6437 N  N   . TYR   B 152 ? 0.1471 0.1243 0.1755 -0.0220 -0.0198 -0.0019 152 TYR   B N   
6438 C  CA  . TYR   B 152 ? 0.1469 0.1415 0.1647 -0.0222 -0.0154 -0.0096 152 TYR   B CA  
6439 C  C   . TYR   B 152 ? 0.1476 0.1287 0.1596 -0.0190 -0.0109 -0.0082 152 TYR   B C   
6440 O  O   . TYR   B 152 ? 0.1579 0.1268 0.1676 -0.0241 -0.0149 -0.0032 152 TYR   B O   
6441 C  CB  . TYR   B 152 ? 0.1580 0.1542 0.1704 -0.0224 -0.0141 0.0031  152 TYR   B CB  
6442 C  CG  . TYR   B 152 ? 0.1740 0.1628 0.1701 -0.0372 -0.0148 0.0039  152 TYR   B CG  
6443 C  CD1 . TYR   B 152 ? 0.1843 0.1762 0.1677 -0.0271 -0.0302 0.0120  152 TYR   B CD1 
6444 C  CD2 . TYR   B 152 ? 0.1974 0.1752 0.1699 -0.0291 -0.0112 0.0001  152 TYR   B CD2 
6445 C  CE1 . TYR   B 152 ? 0.2057 0.1923 0.1812 -0.0220 -0.0300 0.0245  152 TYR   B CE1 
6446 C  CE2 . TYR   B 152 ? 0.2126 0.2010 0.1716 -0.0297 -0.0192 0.0001  152 TYR   B CE2 
6447 C  CZ  . TYR   B 152 ? 0.2142 0.2137 0.1632 -0.0268 -0.0454 0.0202  152 TYR   B CZ  
6448 O  OH  . TYR   B 152 ? 0.2361 0.2526 0.1941 -0.0151 -0.0437 0.0154  152 TYR   B OH  
6458 N  N   . LEU   B 153 ? 0.1467 0.1238 0.1712 -0.0251 -0.0153 -0.0108 153 LEU   B N   
6459 C  CA  . LEU   B 153 ? 0.1518 0.1246 0.1575 -0.0183 -0.0099 -0.0089 153 LEU   B CA  
6460 C  C   . LEU   B 153 ? 0.1527 0.1257 0.1702 -0.0226 -0.0047 -0.0138 153 LEU   B C   
6461 O  O   . LEU   B 153 ? 0.1614 0.1486 0.1810 -0.0146 -0.0078 -0.0267 153 LEU   B O   
6462 C  CB  . LEU   B 153 ? 0.1552 0.1243 0.1774 -0.0268 -0.0017 -0.0019 153 LEU   B CB  
6463 C  CG  . LEU   B 153 ? 0.1489 0.1336 0.2035 -0.0215 -0.0024 -0.0020 153 LEU   B CG  
6464 C  CD1 . LEU   B 153 ? 0.1554 0.1489 0.2162 -0.0281 0.0024  0.0057  153 LEU   B CD1 
6465 C  CD2 . LEU   B 153 ? 0.1428 0.1416 0.2062 -0.0293 0.0077  0.0028  153 LEU   B CD2 
6477 N  N   . ALA   B 154 ? 0.1469 0.1245 0.1790 -0.0044 -0.0158 -0.0053 154 ALA   B N   
6478 C  CA  . ALA   B 154 ? 0.1604 0.1395 0.1964 0.0003  -0.0122 -0.0178 154 ALA   B CA  
6479 C  C   . ALA   B 154 ? 0.1697 0.1438 0.2007 0.0037  -0.0210 -0.0191 154 ALA   B C   
6480 O  O   . ALA   B 154 ? 0.1984 0.1422 0.2191 0.0072  -0.0097 -0.0081 154 ALA   B O   
6481 C  CB  . ALA   B 154 ? 0.1564 0.1493 0.2156 -0.0047 -0.0192 -0.0287 154 ALA   B CB  
6487 N  N   . VAL   B 155 ? 0.1405 0.1291 0.2091 0.0005  -0.0091 -0.0149 155 VAL   B N   
6488 C  CA  . VAL   B 155 ? 0.1357 0.1277 0.2221 -0.0014 -0.0166 -0.0057 155 VAL   B CA  
6489 C  C   . VAL   B 155 ? 0.1412 0.1320 0.2285 -0.0045 -0.0074 -0.0206 155 VAL   B C   
6490 O  O   . VAL   B 155 ? 0.1605 0.1501 0.2582 0.0058  -0.0081 -0.0355 155 VAL   B O   
6491 C  CB  . VAL   B 155 ? 0.1443 0.1457 0.2600 -0.0070 -0.0154 0.0066  155 VAL   B CB  
6492 C  CG1 . VAL   B 155 ? 0.1484 0.1416 0.2579 -0.0112 -0.0128 0.0076  155 VAL   B CG1 
6493 C  CG2 . VAL   B 155 ? 0.1386 0.1616 0.2957 -0.0077 -0.0046 0.0307  155 VAL   B CG2 
6503 N  N   . PHE   B 156 ? 0.1317 0.1382 0.2428 0.0018  -0.0007 -0.0152 156 PHE   B N   
6504 C  CA  . PHE   B 156 ? 0.1417 0.1454 0.2675 0.0045  -0.0011 -0.0141 156 PHE   B CA  
6505 C  C   . PHE   B 156 ? 0.1386 0.1545 0.2956 0.0119  -0.0108 -0.0345 156 PHE   B C   
6506 O  O   . PHE   B 156 ? 0.1617 0.1751 0.3186 0.0243  0.0020  -0.0380 156 PHE   B O   
6507 C  CB  . PHE   B 156 ? 0.1489 0.1461 0.2699 0.0012  -0.0134 -0.0110 156 PHE   B CB  
6508 C  CG  . PHE   B 156 ? 0.1471 0.1545 0.2830 0.0008  -0.0173 0.0078  156 PHE   B CG  
6509 C  CD1 . PHE   B 156 ? 0.1500 0.1800 0.3217 0.0050  -0.0090 0.0362  156 PHE   B CD1 
6510 C  CD2 . PHE   B 156 ? 0.1515 0.1624 0.2794 0.0080  -0.0271 0.0114  156 PHE   B CD2 
6511 C  CE1 . PHE   B 156 ? 0.1547 0.1971 0.3316 0.0063  -0.0069 0.0394  156 PHE   B CE1 
6512 C  CE2 . PHE   B 156 ? 0.1559 0.1811 0.3029 0.0116  -0.0212 0.0185  156 PHE   B CE2 
6513 C  CZ  . PHE   B 156 ? 0.1486 0.1936 0.3221 0.0133  -0.0202 0.0244  156 PHE   B CZ  
6523 N  N   . ASP   B 157 ? 0.1471 0.1451 0.3208 0.0117  -0.0237 -0.0258 157 ASP   B N   
6524 C  CA  . ASP   B 157 ? 0.1580 0.1516 0.3465 0.0092  -0.0272 -0.0295 157 ASP   B CA  
6525 C  C   . ASP   B 157 ? 0.1548 0.1485 0.3479 0.0077  -0.0190 -0.0449 157 ASP   B C   
6526 O  O   . ASP   B 157 ? 0.1424 0.1490 0.3374 0.0067  -0.0157 -0.0302 157 ASP   B O   
6527 C  CB  . ASP   B 157 ? 0.1709 0.1751 0.3500 0.0018  -0.0474 -0.0168 157 ASP   B CB  
6528 C  CG  . ASP   B 157 ? 0.2089 0.1879 0.3771 0.0017  -0.0292 -0.0146 157 ASP   B CG  
6529 O  OD1 . ASP   B 157 ? 0.2197 0.1761 0.3955 0.0145  -0.0215 -0.0123 157 ASP   B OD1 
6530 O  OD2 . ASP   B 157 ? 0.2443 0.2051 0.4097 -0.0013 -0.0124 -0.0063 157 ASP   B OD2 
6535 N  N   A LYS   B 158 ? 0.1541 0.1713 0.3526 0.0039  -0.0086 -0.0632 158 LYS   B N   
6536 N  N   B LYS   B 158 ? 0.1542 0.1715 0.3524 0.0067  -0.0081 -0.0632 158 LYS   B N   
6537 C  CA  A LYS   B 158 ? 0.1685 0.1881 0.3596 0.0042  -0.0082 -0.0738 158 LYS   B CA  
6538 C  CA  B LYS   B 158 ? 0.1687 0.1884 0.3588 0.0093  -0.0073 -0.0735 158 LYS   B CA  
6539 C  C   A LYS   B 158 ? 0.1672 0.1800 0.3724 0.0044  -0.0126 -0.0724 158 LYS   B C   
6540 C  C   B LYS   B 158 ? 0.1677 0.1798 0.3721 0.0071  -0.0126 -0.0717 158 LYS   B C   
6541 O  O   A LYS   B 158 ? 0.1702 0.1763 0.3740 -0.0044 -0.0120 -0.0799 158 LYS   B O   
6542 O  O   B LYS   B 158 ? 0.1714 0.1751 0.3738 -0.0017 -0.0126 -0.0785 158 LYS   B O   
6543 C  CB  A LYS   B 158 ? 0.1938 0.2203 0.3568 0.0058  -0.0009 -0.0831 158 LYS   B CB  
6544 C  CB  B LYS   B 158 ? 0.1939 0.2211 0.3546 0.0148  0.0009  -0.0831 158 LYS   B CB  
6545 C  CG  A LYS   B 158 ? 0.2235 0.2511 0.3605 0.0047  0.0059  -0.0859 158 LYS   B CG  
6546 C  CG  B LYS   B 158 ? 0.2239 0.2524 0.3566 0.0162  0.0083  -0.0866 158 LYS   B CG  
6547 C  CD  A LYS   B 158 ? 0.2441 0.2815 0.3704 0.0031  0.0083  -0.0806 158 LYS   B CD  
6548 C  CD  B LYS   B 158 ? 0.2459 0.2845 0.3655 0.0162  0.0107  -0.0812 158 LYS   B CD  
6549 C  CE  A LYS   B 158 ? 0.2593 0.3036 0.3809 0.0038  0.0033  -0.0763 158 LYS   B CE  
6550 C  CE  B LYS   B 158 ? 0.2623 0.3068 0.3764 0.0186  0.0061  -0.0757 158 LYS   B CE  
6551 N  NZ  A LYS   B 158 ? 0.2576 0.3115 0.3785 -0.0009 -0.0004 -0.0777 158 LYS   B NZ  
6552 N  NZ  B LYS   B 158 ? 0.2641 0.3166 0.3764 0.0179  0.0050  -0.0739 158 LYS   B NZ  
6579 N  N   . ASN   B 159 ? 0.1668 0.1735 0.3854 0.0069  -0.0210 -0.0663 159 ASN   B N   
6580 C  CA  . ASN   B 159 ? 0.1835 0.1621 0.4137 0.0197  -0.0343 -0.0581 159 ASN   B CA  
6581 C  C   . ASN   B 159 ? 0.1677 0.1505 0.4006 0.0168  -0.0433 -0.0425 159 ASN   B C   
6582 O  O   . ASN   B 159 ? 0.1704 0.1446 0.4093 -0.0008 -0.0489 -0.0282 159 ASN   B O   
6583 C  CB  . ASN   B 159 ? 0.2046 0.1745 0.4467 0.0294  -0.0395 -0.0507 159 ASN   B CB  
6584 C  CG  . ASN   B 159 ? 0.2351 0.1974 0.4775 0.0329  -0.0532 -0.0631 159 ASN   B CG  
6585 O  OD1 . ASN   B 159 ? 0.2533 0.2112 0.4903 0.0393  -0.0532 -0.0675 159 ASN   B OD1 
6586 N  ND2 . ASN   B 159 ? 0.2380 0.2081 0.4938 0.0380  -0.0580 -0.0543 159 ASN   B ND2 
6594 N  N   . LEU   B 160 ? 0.1527 0.1507 0.3758 0.0089  -0.0425 -0.0340 160 LEU   B N   
6595 C  CA  . LEU   B 160 ? 0.1523 0.1506 0.3343 0.0078  -0.0335 -0.0191 160 LEU   B CA  
6596 C  C   . LEU   B 160 ? 0.1484 0.1421 0.3234 0.0004  -0.0222 -0.0289 160 LEU   B C   
6597 O  O   . LEU   B 160 ? 0.1414 0.1450 0.3083 -0.0022 -0.0256 -0.0188 160 LEU   B O   
6598 C  CB  . LEU   B 160 ? 0.1557 0.1553 0.3100 0.0046  -0.0339 -0.0095 160 LEU   B CB  
6599 C  CG  . LEU   B 160 ? 0.1546 0.1670 0.2941 0.0103  -0.0311 0.0002  160 LEU   B CG  
6600 C  CD1 . LEU   B 160 ? 0.1687 0.1902 0.2973 0.0002  -0.0181 0.0046  160 LEU   B CD1 
6601 C  CD2 . LEU   B 160 ? 0.1580 0.1723 0.2954 0.0207  -0.0309 -0.0117 160 LEU   B CD2 
6613 N  N   . TYR   B 161 ? 0.1438 0.1501 0.3267 -0.0027 -0.0074 -0.0367 161 TYR   B N   
6614 C  CA  . TYR   B 161 ? 0.1490 0.1495 0.3160 -0.0108 0.0058  -0.0419 161 TYR   B CA  
6615 C  C   . TYR   B 161 ? 0.1581 0.1461 0.2993 -0.0096 0.0138  -0.0373 161 TYR   B C   
6616 O  O   . TYR   B 161 ? 0.1638 0.1464 0.2884 -0.0159 0.0039  -0.0341 161 TYR   B O   
6617 C  CB  . TYR   B 161 ? 0.1636 0.1587 0.3199 -0.0193 0.0248  -0.0437 161 TYR   B CB  
6618 C  CG  . TYR   B 161 ? 0.1881 0.1590 0.3156 -0.0273 0.0331  -0.0511 161 TYR   B CG  
6619 C  CD1 . TYR   B 161 ? 0.1971 0.1587 0.3045 -0.0360 0.0253  -0.0541 161 TYR   B CD1 
6620 C  CD2 . TYR   B 161 ? 0.2136 0.1686 0.3063 -0.0276 0.0289  -0.0545 161 TYR   B CD2 
6621 C  CE1 . TYR   B 161 ? 0.2117 0.1744 0.3022 -0.0427 0.0292  -0.0483 161 TYR   B CE1 
6622 C  CE2 . TYR   B 161 ? 0.2282 0.1845 0.3091 -0.0348 0.0310  -0.0444 161 TYR   B CE2 
6623 C  CZ  . TYR   B 161 ? 0.2271 0.1879 0.2998 -0.0500 0.0279  -0.0365 161 TYR   B CZ  
6624 O  OH  . TYR   B 161 ? 0.2554 0.2136 0.3164 -0.0519 0.0298  -0.0328 161 TYR   B OH  
6634 N  N   . ASP   B 162 ? 0.1651 0.1469 0.3198 -0.0081 0.0040  -0.0473 162 ASP   B N   
6635 C  CA  . ASP   B 162 ? 0.1725 0.1537 0.3120 -0.0155 -0.0003 -0.0512 162 ASP   B CA  
6636 C  C   . ASP   B 162 ? 0.1705 0.1459 0.3014 -0.0196 -0.0033 -0.0495 162 ASP   B C   
6637 O  O   . ASP   B 162 ? 0.1806 0.1519 0.3036 -0.0248 -0.0147 -0.0312 162 ASP   B O   
6638 C  CB  . ASP   B 162 ? 0.1960 0.1691 0.3334 -0.0013 -0.0021 -0.0600 162 ASP   B CB  
6639 C  CG  . ASP   B 162 ? 0.2016 0.1951 0.3546 0.0090  -0.0031 -0.0714 162 ASP   B CG  
6640 O  OD1 . ASP   B 162 ? 0.2040 0.2126 0.3414 0.0030  0.0056  -0.0715 162 ASP   B OD1 
6641 O  OD2 . ASP   B 162 ? 0.2165 0.2191 0.3927 0.0222  0.0007  -0.0725 162 ASP   B OD2 
6646 N  N   A LYS   B 163 ? 0.1719 0.1421 0.2981 -0.0153 -0.0111 -0.0366 163 LYS   B N   
6647 N  N   B LYS   B 163 ? 0.1716 0.1393 0.2962 -0.0164 -0.0105 -0.0372 163 LYS   B N   
6648 C  CA  A LYS   B 163 ? 0.1831 0.1477 0.3079 -0.0188 -0.0155 -0.0160 163 LYS   B CA  
6649 C  CA  B LYS   B 163 ? 0.1824 0.1432 0.3045 -0.0215 -0.0148 -0.0160 163 LYS   B CA  
6650 C  C   A LYS   B 163 ? 0.1536 0.1393 0.3002 -0.0181 -0.0206 -0.0066 163 LYS   B C   
6651 C  C   B LYS   B 163 ? 0.1538 0.1370 0.2953 -0.0203 -0.0186 -0.0075 163 LYS   B C   
6652 O  O   A LYS   B 163 ? 0.1536 0.1477 0.3222 -0.0212 -0.0208 -0.0010 163 LYS   B O   
6653 O  O   B LYS   B 163 ? 0.1549 0.1450 0.3107 -0.0247 -0.0150 -0.0023 163 LYS   B O   
6654 C  CB  A LYS   B 163 ? 0.2248 0.1773 0.3424 -0.0188 -0.0151 -0.0055 163 LYS   B CB  
6655 C  CB  B LYS   B 163 ? 0.2232 0.1703 0.3386 -0.0223 -0.0154 -0.0037 163 LYS   B CB  
6656 C  CG  A LYS   B 163 ? 0.2795 0.2392 0.3862 -0.0207 -0.0074 -0.0035 163 LYS   B CG  
6657 C  CG  B LYS   B 163 ? 0.2776 0.2322 0.3820 -0.0249 -0.0087 -0.0005 163 LYS   B CG  
6658 C  CD  A LYS   B 163 ? 0.3265 0.2891 0.4313 -0.0282 -0.0077 -0.0098 163 LYS   B CD  
6659 C  CD  B LYS   B 163 ? 0.3244 0.2860 0.4283 -0.0333 -0.0100 -0.0040 163 LYS   B CD  
6660 C  CE  A LYS   B 163 ? 0.3563 0.3216 0.4626 -0.0345 -0.0063 -0.0101 163 LYS   B CE  
6661 C  CE  B LYS   B 163 ? 0.3548 0.3194 0.4611 -0.0414 -0.0091 -0.0052 163 LYS   B CE  
6662 N  NZ  A LYS   B 163 ? 0.3734 0.3340 0.4857 -0.0374 -0.0052 -0.0127 163 LYS   B NZ  
6663 N  NZ  B LYS   B 163 ? 0.3719 0.3299 0.4843 -0.0451 -0.0072 -0.0080 163 LYS   B NZ  
6690 N  N   . LEU   B 164 ? 0.1387 0.1344 0.2802 -0.0169 -0.0190 -0.0048 164 LEU   B N   
6691 C  CA  . LEU   B 164 ? 0.1404 0.1323 0.2617 -0.0115 -0.0226 0.0006  164 LEU   B CA  
6692 C  C   . LEU   B 164 ? 0.1453 0.1340 0.2587 -0.0144 -0.0282 -0.0076 164 LEU   B C   
6693 O  O   . LEU   B 164 ? 0.1486 0.1545 0.2729 -0.0134 -0.0288 -0.0025 164 LEU   B O   
6694 C  CB  . LEU   B 164 ? 0.1399 0.1297 0.2499 -0.0065 -0.0160 0.0036  164 LEU   B CB  
6695 C  CG  . LEU   B 164 ? 0.1527 0.1500 0.2585 -0.0118 -0.0073 0.0054  164 LEU   B CG  
6696 C  CD1 . LEU   B 164 ? 0.1528 0.1480 0.2573 -0.0111 -0.0222 -0.0035 164 LEU   B CD1 
6697 C  CD2 . LEU   B 164 ? 0.1691 0.1895 0.2780 -0.0089 0.0088  -0.0159 164 LEU   B CD2 
6710 N  N   . VAL   B 165 ? 0.1742 0.1404 0.2814 -0.0191 -0.0295 -0.0126 165 VAL   B N   
6711 C  CA  . VAL   B 165 ? 0.2077 0.1515 0.2806 -0.0293 -0.0497 -0.0086 165 VAL   B CA  
6712 C  C   . VAL   B 165 ? 0.2377 0.1649 0.3068 -0.0451 -0.0727 0.0004  165 VAL   B C   
6713 O  O   . VAL   B 165 ? 0.2534 0.1791 0.3145 -0.0465 -0.0747 -0.0006 165 VAL   B O   
6714 C  CB  . VAL   B 165 ? 0.2318 0.1670 0.2770 -0.0128 -0.0209 -0.0185 165 VAL   B CB  
6715 C  CG1 . VAL   B 165 ? 0.2471 0.1743 0.3052 -0.0123 -0.0117 -0.0184 165 VAL   B CG1 
6716 C  CG2 . VAL   B 165 ? 0.2316 0.1742 0.2733 -0.0107 -0.0075 -0.0153 165 VAL   B CG2 
6726 N  N   . SER   B 166 ? 0.2518 0.1573 0.3394 -0.0421 -0.0790 -0.0195 166 SER   B N   
6727 C  CA  . SER   B 166 ? 0.2416 0.1551 0.3947 -0.0445 -0.0720 -0.0282 166 SER   B CA  
6728 C  C   . SER   B 166 ? 0.2247 0.1669 0.4061 -0.0417 -0.0747 -0.0050 166 SER   B C   
6729 O  O   . SER   B 166 ? 0.2257 0.1903 0.4273 -0.0465 -0.0933 -0.0267 166 SER   B O   
6730 C  CB  . SER   B 166 ? 0.2428 0.1642 0.4286 -0.0270 -0.0642 -0.0359 166 SER   B CB  
6731 O  OG  . SER   B 166 ? 0.2328 0.1595 0.4481 -0.0184 -0.0676 -0.0250 166 SER   B OG  
6737 N  N   . SER   B 167 ? 0.2073 0.1626 0.3772 -0.0403 -0.0744 0.0288  167 SER   B N   
6738 C  CA  . SER   B 167 ? 0.1981 0.1688 0.3557 -0.0416 -0.0541 0.0325  167 SER   B CA  
6739 C  C   . SER   B 167 ? 0.1925 0.1780 0.3397 -0.0519 -0.0507 0.0433  167 SER   B C   
6740 O  O   . SER   B 167 ? 0.1989 0.1866 0.3371 -0.0527 -0.0456 0.0372  167 SER   B O   
6741 C  CB  . SER   B 167 ? 0.1867 0.1751 0.3516 -0.0393 -0.0232 0.0371  167 SER   B CB  
6742 O  OG  . SER   B 167 ? 0.1830 0.1887 0.3447 -0.0294 -0.0135 0.0333  167 SER   B OG  
6748 N  N   . PHE   B 168 ? 0.1905 0.1796 0.3319 -0.0468 -0.0305 0.0479  168 PHE   B N   
6749 C  CA  . PHE   B 168 ? 0.2004 0.1709 0.3107 -0.0492 -0.0260 0.0300  168 PHE   B CA  
6750 C  C   . PHE   B 168 ? 0.1757 0.1620 0.2639 -0.0275 -0.0118 0.0158  168 PHE   B C   
6751 O  O   . PHE   B 168 ? 0.2109 0.1520 0.2667 -0.0039 -0.0111 0.0004  168 PHE   B O   
6752 C  CB  . PHE   B 168 ? 0.2161 0.1757 0.3190 -0.0541 -0.0443 0.0426  168 PHE   B CB  
6753 C  CG  . PHE   B 168 ? 0.2415 0.1546 0.3149 -0.0560 -0.0535 0.0209  168 PHE   B CG  
6754 C  CD1 . PHE   B 168 ? 0.2764 0.1631 0.3246 -0.0490 -0.0644 0.0186  168 PHE   B CD1 
6755 C  CD2 . PHE   B 168 ? 0.2252 0.1499 0.3101 -0.0475 -0.0519 0.0300  168 PHE   B CD2 
6756 C  CE1 . PHE   B 168 ? 0.2881 0.1717 0.3211 -0.0337 -0.0597 0.0244  168 PHE   B CE1 
6757 C  CE2 . PHE   B 168 ? 0.2585 0.1596 0.3211 -0.0311 -0.0591 0.0184  168 PHE   B CE2 
6758 C  CZ  . PHE   B 168 ? 0.2755 0.1546 0.3197 -0.0200 -0.0653 0.0340  168 PHE   B CZ  
6768 N  N   . LEU   B 169 ? 0.1719 0.1748 0.2681 -0.0031 -0.0035 0.0037  169 LEU   B N   
6769 C  CA  . LEU   B 169 ? 0.1983 0.1998 0.2997 -0.0087 -0.0040 -0.0224 169 LEU   B CA  
6770 C  C   . LEU   B 169 ? 0.2287 0.2220 0.3546 0.0078  -0.0065 -0.0555 169 LEU   B C   
6771 O  O   . LEU   B 169 ? 0.2516 0.2440 0.4121 0.0040  -0.0091 -0.0783 169 LEU   B O   
6772 C  CB  . LEU   B 169 ? 0.2160 0.2406 0.3013 -0.0150 -0.0203 0.0043  169 LEU   B CB  
6773 C  CG  . LEU   B 169 ? 0.2620 0.2799 0.3443 -0.0009 -0.0135 0.0113  169 LEU   B CG  
6774 C  CD1 . LEU   B 169 ? 0.2792 0.3002 0.3495 0.0029  -0.0213 0.0265  169 LEU   B CD1 
6775 C  CD2 . LEU   B 169 ? 0.2586 0.2854 0.3506 0.0165  0.0036  0.0013  169 LEU   B CD2 
6776 O  OXT . LEU   B 169 ? 0.2521 0.2418 0.3497 0.0357  -0.0043 -0.0554 169 LEU   B OXT 
6788 N  N2  B A1A99 C .   ? 0.1722 0.1488 0.1677 -0.0037 0.0167  0.0208  201 A1A99 A N2  
6789 C  C3  B A1A99 C .   ? 0.1806 0.1673 0.2228 0.0164  0.0029  0.0112  201 A1A99 A C3  
6790 C  C6  B A1A99 C .   ? 0.1606 0.1542 0.1771 0.0076  0.0146  0.0198  201 A1A99 A C6  
6791 C  C9  B A1A99 C .   ? 0.1555 0.1509 0.1813 0.0205  0.0179  0.0340  201 A1A99 A C9  
6792 C  C1  B A1A99 C .   ? 0.1768 0.1915 0.2533 0.0034  0.0248  0.0173  201 A1A99 A C1  
6793 C  C10 B A1A99 C .   ? 0.1610 0.1578 0.1993 0.0249  0.0189  0.0291  201 A1A99 A C10 
6794 C  C11 B A1A99 C .   ? 0.1614 0.1598 0.2140 0.0170  0.0153  0.0350  201 A1A99 A C11 
6795 C  C2  B A1A99 C .   ? 0.1729 0.1751 0.2386 0.0085  0.0199  0.0299  201 A1A99 A C2  
6796 C  C4  B A1A99 C .   ? 0.1946 0.1753 0.2318 0.0185  0.0048  0.0025  201 A1A99 A C4  
6797 C  C5  B A1A99 C .   ? 0.1773 0.1531 0.2225 0.0180  -0.0094 0.0142  201 A1A99 A C5  
6798 C  C7  B A1A99 C .   ? 0.1577 0.1458 0.1751 0.0013  0.0230  0.0154  201 A1A99 A C7  
6799 C  C8  B A1A99 C .   ? 0.1523 0.1482 0.1868 0.0133  0.0177  0.0268  201 A1A99 A C8  
6800 N  N1  B A1A99 C .   ? 0.1697 0.1645 0.2041 0.0097  0.0152  0.0100  201 A1A99 A N1  
6801 N  N3  B A1A99 C .   ? 0.1548 0.1476 0.1684 -0.0012 0.0252  0.0223  201 A1A99 A N3  
6802 N  N4  B A1A99 C .   ? 0.1564 0.1510 0.2095 0.0204  0.0093  0.0294  201 A1A99 A N4  
6803 O  O1  B A1A99 C .   ? 0.1755 0.1520 0.2163 0.0186  -0.0195 0.0266  201 A1A99 A O1  
6820 CL CL  B CL    D .   ? 0.2335 0.1850 0.3773 0.0204  -0.0703 -0.0676 202 CL    A CL  
6821 O  O   . HOH   E .   ? 0.4245 0.8103 0.4453 -0.1140 0.0752  0.0197  301 HOH   A O   
6822 O  O   A HOH   E .   ? 0.3119 0.1862 0.2913 -0.0264 -0.0874 0.0672  302 HOH   A O   
6823 O  O   . HOH   E .   ? 0.3292 0.3158 0.1780 -0.0603 0.0512  0.0435  303 HOH   A O   
6824 O  O   . HOH   E .   ? 0.6749 0.6368 0.3460 -0.1450 -0.0193 0.2023  304 HOH   A O   
6825 O  O   . HOH   E .   ? 0.6251 0.4876 0.3550 0.2194  -0.1214 0.0532  305 HOH   A O   
6826 O  O   . HOH   E .   ? 0.5054 0.4293 0.5695 -0.0525 0.1398  0.1618  306 HOH   A O   
6827 O  O   . HOH   E .   ? 0.2563 0.2728 0.3402 -0.0283 0.0672  0.0681  307 HOH   A O   
6828 O  O   . HOH   E .   ? 0.2806 0.2645 0.5051 -0.0376 -0.1060 0.1371  308 HOH   A O   
6829 O  O   . HOH   E .   ? 0.6206 0.5338 0.5913 -0.1370 0.0393  0.1775  309 HOH   A O   
6830 O  O   . HOH   E .   ? 0.5577 0.3291 0.4834 0.1334  -0.0798 -0.0197 310 HOH   A O   
6831 O  O   . HOH   E .   ? 0.5232 0.2065 0.4641 0.0521  -0.0005 0.0063  311 HOH   A O   
6832 O  O   B HOH   E .   ? 0.3342 0.5135 0.3190 0.0139  -0.0081 -0.0362 312 HOH   A O   
6833 O  O   A HOH   E .   ? 0.2779 0.2892 0.3927 0.0104  0.1171  -0.0425 313 HOH   A O   
6834 O  O   . HOH   E .   ? 0.7538 0.5055 0.4945 -0.1106 0.1516  0.1753  314 HOH   A O   
6835 O  O   . HOH   E .   ? 0.2206 0.1954 0.3622 -0.0552 0.0060  -0.0218 315 HOH   A O   
6836 O  O   . HOH   E .   ? 0.2440 0.2134 0.2534 -0.0374 0.0205  0.0049  316 HOH   A O   
6837 O  O   . HOH   E .   ? 0.5026 0.5173 0.3021 -0.1474 0.1445  0.0732  317 HOH   A O   
6838 O  O   . HOH   E .   ? 0.3365 0.3790 0.4861 0.0840  0.0664  -0.1151 318 HOH   A O   
6839 O  O   . HOH   E .   ? 0.3770 0.3269 0.2911 -0.1557 0.0210  0.0538  319 HOH   A O   
6840 O  O   . HOH   E .   ? 0.2035 0.1671 0.2405 0.0147  -0.0311 0.0028  320 HOH   A O   
6841 O  O   . HOH   E .   ? 0.6670 0.6400 0.3708 -0.0394 -0.0568 0.1622  321 HOH   A O   
6842 O  O   B HOH   E .   ? 0.2526 0.3707 0.2625 -0.0126 -0.0374 -0.0207 322 HOH   A O   
6843 O  O   . HOH   E .   ? 0.2894 0.5718 0.4346 -0.0123 -0.0823 0.0900  323 HOH   A O   
6844 O  O   . HOH   E .   ? 0.2030 0.3626 0.4823 -0.0459 0.0453  -0.1210 324 HOH   A O   
6845 O  O   . HOH   E .   ? 0.1832 0.2977 0.2926 0.0323  -0.0172 -0.0144 325 HOH   A O   
6846 O  O   . HOH   E .   ? 0.3285 0.4565 0.2487 -0.0302 0.0490  0.0582  326 HOH   A O   
6847 O  O   . HOH   E .   ? 0.3233 0.3760 0.3559 -0.0621 0.1282  0.0302  327 HOH   A O   
6848 O  O   A HOH   E .   ? 0.4184 0.1679 0.1759 0.0173  0.0292  0.0028  328 HOH   A O   
6849 O  O   . HOH   E .   ? 0.1499 0.1512 0.2397 -0.0209 0.0051  0.0041  329 HOH   A O   
6850 O  O   . HOH   E .   ? 0.4514 0.2100 0.4258 0.0363  -0.1434 0.0596  330 HOH   A O   
6851 O  O   . HOH   E .   ? 0.3246 0.7692 0.5070 -0.0930 -0.0795 0.2349  331 HOH   A O   
6852 O  O   . HOH   E .   ? 0.2980 0.4052 0.3611 -0.1129 -0.0747 -0.0471 332 HOH   A O   
6853 O  O   A HOH   E .   ? 0.4064 0.3879 0.4009 0.1010  0.0400  -0.1137 333 HOH   A O   
6854 O  O   . HOH   E .   ? 0.2496 0.2351 0.2888 0.0454  0.0281  0.0474  334 HOH   A O   
6855 O  O   . HOH   E .   ? 0.1888 0.2230 0.2085 -0.0266 -0.0049 0.0743  335 HOH   A O   
6856 O  O   A HOH   E .   ? 0.1809 0.2852 0.2523 0.0602  0.0585  0.1243  336 HOH   A O   
6857 O  O   . HOH   E .   ? 0.2273 0.4394 0.4217 -0.0224 -0.0576 0.1906  337 HOH   A O   
6858 O  O   . HOH   E .   ? 0.3134 0.3240 0.3950 -0.0821 0.1366  0.0025  338 HOH   A O   
6859 O  O   . HOH   E .   ? 0.1569 0.4744 0.2911 -0.0239 0.0190  0.0812  339 HOH   A O   
6860 O  O   . HOH   E .   ? 0.5365 0.5052 0.3619 -0.1382 -0.0516 0.0067  340 HOH   A O   
6861 O  O   . HOH   E .   ? 0.6022 0.3864 0.2889 0.0397  0.0544  0.1089  341 HOH   A O   
6862 O  O   . HOH   E .   ? 0.5827 0.5928 0.4902 -0.1274 -0.1238 -0.0965 342 HOH   A O   
6863 O  O   . HOH   E .   ? 0.2623 0.2077 0.2479 -0.0590 -0.0028 0.0563  343 HOH   A O   
6864 O  O   . HOH   E .   ? 0.3546 0.4151 0.4827 -0.1528 -0.0388 0.2103  344 HOH   A O   
6865 O  O   . HOH   E .   ? 0.5781 0.6116 0.3632 0.2256  -0.0583 -0.0578 345 HOH   A O   
6866 O  O   . HOH   E .   ? 0.1516 0.2262 0.2217 0.0057  -0.0072 0.0602  346 HOH   A O   
6867 O  O   . HOH   E .   ? 0.1991 0.2300 0.2750 -0.0223 -0.0180 0.0884  347 HOH   A O   
6868 O  O   . HOH   E .   ? 0.2188 0.1684 0.1623 -0.0107 0.0147  0.0148  348 HOH   A O   
6869 O  O   . HOH   E .   ? 0.8553 0.4589 0.6308 -0.0453 -0.1321 0.0417  349 HOH   A O   
6870 O  O   A HOH   E .   ? 0.2628 0.4281 0.2445 0.1023  -0.0076 -0.0388 350 HOH   A O   
6871 O  O   . HOH   E .   ? 0.2500 0.4048 0.3874 0.0923  -0.0845 -0.0193 351 HOH   A O   
6872 O  O   . HOH   E .   ? 0.2788 0.4599 0.3371 -0.0591 0.0559  -0.0277 352 HOH   A O   
6873 O  O   . HOH   E .   ? 0.6810 0.5364 0.4654 -0.0507 -0.1465 -0.1094 353 HOH   A O   
6874 O  O   . HOH   E .   ? 0.2684 0.6352 0.5756 -0.0318 0.0868  0.2480  354 HOH   A O   
6875 O  O   . HOH   E .   ? 0.3310 0.3665 0.2324 -0.0899 -0.0337 -0.0671 355 HOH   A O   
6876 O  O   . HOH   E .   ? 0.5159 0.2723 0.4110 -0.1663 0.1981  -0.0775 356 HOH   A O   
6877 O  O   . HOH   E .   ? 0.3707 0.4598 0.3574 0.2040  0.0857  0.0720  357 HOH   A O   
6878 O  O   . HOH   E .   ? 0.1439 0.1875 0.2677 0.0088  -0.0145 0.0054  358 HOH   A O   
6879 O  O   . HOH   E .   ? 0.1919 0.1799 0.1835 0.0048  0.0087  0.0144  359 HOH   A O   
6880 O  O   . HOH   E .   ? 0.1334 0.1296 0.1503 -0.0035 0.0070  0.0094  360 HOH   A O   
6881 O  O   . HOH   E .   ? 0.3897 0.6707 0.4896 -0.0384 -0.1168 0.0073  361 HOH   A O   
6882 O  O   . HOH   E .   ? 0.1884 0.2137 0.3596 0.0119  0.0808  -0.0180 362 HOH   A O   
6883 O  O   . HOH   E .   ? 0.4669 0.3263 0.2940 -0.1113 0.0323  0.0640  363 HOH   A O   
6884 O  O   . HOH   E .   ? 0.6394 0.5349 0.5966 -0.0067 0.2587  -0.1075 364 HOH   A O   
6885 O  O   . HOH   E .   ? 0.3427 0.3371 0.3629 -0.1267 -0.0245 -0.0042 365 HOH   A O   
6886 O  O   . HOH   E .   ? 0.1721 0.1679 0.2139 0.0147  -0.0231 0.0210  366 HOH   A O   
6887 O  O   . HOH   E .   ? 0.1715 0.1873 0.2375 -0.0249 0.0041  0.0435  367 HOH   A O   
6888 O  O   . HOH   E .   ? 0.2668 0.4249 0.2999 0.0426  0.0713  0.1663  368 HOH   A O   
6889 O  O   . HOH   E .   ? 0.2967 0.3422 0.4777 -0.0730 -0.1018 -0.0785 369 HOH   A O   
6890 O  O   . HOH   E .   ? 0.3976 0.2078 0.2361 0.1163  0.0491  0.0274  370 HOH   A O   
6891 O  O   . HOH   E .   ? 0.1588 0.1331 0.2257 -0.0104 0.0159  -0.0077 371 HOH   A O   
6892 O  O   B HOH   E .   ? 0.1754 0.2791 0.3119 -0.0627 0.0223  -0.0809 372 HOH   A O   
6893 O  O   . HOH   E .   ? 0.1927 0.1980 0.2444 -0.0351 0.0121  0.0361  373 HOH   A O   
6894 O  O   . HOH   E .   ? 0.1500 0.1561 0.1617 -0.0030 -0.0121 0.0009  374 HOH   A O   
6895 O  O   . HOH   E .   ? 0.5079 0.5075 0.6823 -0.0650 -0.0722 0.1389  375 HOH   A O   
6896 O  O   A HOH   E .   ? 0.1129 0.1372 0.1789 0.0109  -0.0269 -0.0127 376 HOH   A O   
6897 O  O   . HOH   E .   ? 0.2178 0.2316 0.2241 -0.0355 -0.0486 0.0459  377 HOH   A O   
6898 O  O   . HOH   E .   ? 0.2044 0.2809 0.3685 0.0440  0.0835  -0.0414 378 HOH   A O   
6899 O  O   A HOH   E .   ? 0.1954 0.1979 0.2349 0.0157  0.0201  0.0875  379 HOH   A O   
6900 O  O   . HOH   E .   ? 0.3983 0.2191 0.4406 -0.1037 0.1098  0.0198  380 HOH   A O   
6901 O  O   . HOH   E .   ? 0.2235 0.3901 0.3402 -0.0250 -0.0073 0.0683  381 HOH   A O   
6902 O  O   B HOH   E .   ? 0.4838 0.3276 0.4284 0.1075  0.0635  -0.0818 382 HOH   A O   
6903 O  O   A HOH   E .   ? 0.2652 0.4923 0.4347 0.0636  0.0212  0.0494  383 HOH   A O   
6904 O  O   A HOH   E .   ? 0.1305 0.1746 0.1657 0.0213  -0.0459 -0.0357 384 HOH   A O   
6905 O  O   . HOH   E .   ? 0.1712 0.1388 0.1630 -0.0220 0.0061  -0.0009 385 HOH   A O   
6906 O  O   . HOH   E .   ? 0.3001 0.6132 0.4283 0.1038  0.0901  -0.0794 386 HOH   A O   
6907 O  O   . HOH   E .   ? 0.3290 0.2592 0.3408 0.0003  -0.0332 0.0789  387 HOH   A O   
6908 O  O   . HOH   E .   ? 0.3308 0.2357 0.5897 -0.0789 -0.0359 0.0114  388 HOH   A O   
6909 O  O   . HOH   E .   ? 0.3024 0.2891 0.2185 0.0375  0.0740  0.0108  389 HOH   A O   
6910 O  O   . HOH   E .   ? 0.2571 0.2126 0.1947 -0.0602 0.0126  0.0319  390 HOH   A O   
6911 O  O   . HOH   E .   ? 0.1786 0.2773 0.3500 -0.0230 0.0638  0.0755  391 HOH   A O   
6912 O  O   . HOH   E .   ? 0.5701 0.6740 0.5629 0.1583  -0.0366 -0.0050 392 HOH   A O   
6913 O  O   B HOH   E .   ? 0.6564 0.3479 0.4240 -0.0552 0.0641  0.0451  393 HOH   A O   
6914 O  O   B HOH   E .   ? 0.2540 0.3163 0.2102 0.1442  0.0444  0.0931  394 HOH   A O   
6915 O  O   A HOH   E .   ? 0.1044 0.1267 0.1297 0.0037  -0.0197 -0.0225 395 HOH   A O   
6916 O  O   B HOH   E .   ? 0.2510 0.1941 0.2009 -0.0126 -0.0495 -0.0038 396 HOH   A O   
6917 O  O   . HOH   E .   ? 0.2631 0.4219 0.3245 -0.0409 0.0953  -0.0700 397 HOH   A O   
6918 O  O   . HOH   E .   ? 0.1839 0.1933 0.3864 0.0399  0.1020  0.1041  398 HOH   A O   
6919 O  O   . HOH   E .   ? 0.3193 0.3663 0.5399 -0.0325 0.1580  -0.0144 399 HOH   A O   
6920 O  O   A HOH   E .   ? 0.2202 0.2552 0.2546 0.0055  0.0733  0.0046  400 HOH   A O   
6921 O  O   . HOH   E .   ? 0.4915 0.5188 0.2220 0.0364  0.1026  0.1076  401 HOH   A O   
6922 O  O   . HOH   E .   ? 0.1403 0.1443 0.1896 0.0005  -0.0187 0.0014  402 HOH   A O   
6923 O  O   . HOH   E .   ? 0.3232 0.2752 0.2361 -0.0766 -0.0994 0.0331  403 HOH   A O   
6924 O  O   A HOH   E .   ? 0.3311 0.4373 0.3694 -0.0246 0.0141  0.0010  404 HOH   A O   
6925 O  O   A HOH   E .   ? 0.1969 0.1272 0.2296 -0.0101 -0.0497 -0.0095 405 HOH   A O   
6926 O  O   . HOH   E .   ? 0.2782 0.4194 0.4780 0.0774  0.0096  0.0778  406 HOH   A O   
6927 O  O   A HOH   E .   ? 0.4735 0.3180 0.4417 -0.0465 -0.0346 0.0785  407 HOH   A O   
6928 O  O   . HOH   E .   ? 0.2019 0.2615 0.3602 -0.0251 -0.0175 0.0155  408 HOH   A O   
6929 O  O   . HOH   E .   ? 0.3733 0.5926 0.4483 -0.0759 -0.0096 0.1388  409 HOH   A O   
6930 O  O   B HOH   E .   ? 0.2781 0.4792 0.4721 -0.0613 -0.0984 -0.1320 410 HOH   A O   
6931 O  O   B HOH   E .   ? 0.1539 0.2119 0.2757 -0.0405 0.0163  0.0362  411 HOH   A O   
6932 O  O   . HOH   E .   ? 0.2172 0.1760 0.2960 0.0055  -0.0350 0.0153  412 HOH   A O   
6933 O  O   . HOH   E .   ? 0.2850 0.3542 0.7533 -0.0147 0.0601  -0.0501 413 HOH   A O   
6934 O  O   A HOH   E .   ? 0.1670 0.1573 0.2246 0.0143  -0.0579 0.0171  414 HOH   A O   
6935 O  O   . HOH   E .   ? 0.5274 0.6469 0.3115 -0.1097 -0.0096 0.1405  415 HOH   A O   
6936 O  O   . HOH   E .   ? 0.3759 0.4365 0.3436 0.1713  -0.0775 -0.1471 416 HOH   A O   
6937 O  O   . HOH   E .   ? 0.8125 0.8503 0.7383 -0.0688 0.0092  -0.0734 417 HOH   A O   
6938 O  O   . HOH   E .   ? 0.4018 0.4508 0.2530 -0.0603 -0.1271 0.0218  418 HOH   A O   
6939 O  O   . HOH   E .   ? 0.4131 0.2264 0.5347 -0.0705 -0.2224 0.1010  419 HOH   A O   
6940 O  O   . HOH   E .   ? 0.1550 0.1675 0.3004 -0.0045 0.0027  0.0212  420 HOH   A O   
6941 O  O   . HOH   E .   ? 0.2599 0.1990 0.2695 -0.0154 0.0135  0.0321  421 HOH   A O   
6942 O  O   . HOH   E .   ? 0.2906 0.5873 0.1758 -0.0591 0.0436  -0.0002 422 HOH   A O   
6943 O  O   . HOH   E .   ? 0.3428 0.1270 0.2176 0.0059  -0.0462 0.0035  423 HOH   A O   
6944 O  O   . HOH   E .   ? 0.2112 0.2173 0.3362 0.0319  -0.0438 0.0406  424 HOH   A O   
6945 O  O   . HOH   E .   ? 0.2534 0.3102 0.3580 -0.0019 -0.0205 -0.0691 425 HOH   A O   
6946 O  O   . HOH   E .   ? 0.2251 0.2713 0.2655 -0.0147 -0.0642 0.0495  426 HOH   A O   
6947 O  O   . HOH   E .   ? 0.6666 0.3685 0.5262 0.1720  -0.0777 0.1265  427 HOH   A O   
6948 O  O   . HOH   E .   ? 0.1677 0.2278 0.3019 -0.0279 -0.0093 0.0596  428 HOH   A O   
6949 O  O   . HOH   E .   ? 0.5582 0.5238 0.5796 -0.0323 -0.0795 -0.0968 429 HOH   A O   
6950 O  O   . HOH   E .   ? 0.2344 0.4568 0.2878 0.1683  -0.0020 0.0329  430 HOH   A O   
6951 O  O   B HOH   E .   ? 0.2799 0.5310 0.2353 -0.0505 0.0730  0.0057  431 HOH   A O   
6952 O  O   . HOH   E .   ? 0.3931 0.3594 0.6356 0.1225  0.1082  0.0383  432 HOH   A O   
6953 O  O   . HOH   E .   ? 0.6508 0.6229 0.6129 -0.1333 0.0071  0.0274  433 HOH   A O   
6954 O  O   . HOH   E .   ? 0.5931 0.6097 0.5517 -0.0656 0.0539  0.2645  434 HOH   A O   
6955 O  O   A HOH   E .   ? 0.4984 0.3082 0.3367 0.1111  0.1903  0.0952  435 HOH   A O   
6956 O  O   . HOH   E .   ? 0.4943 0.4910 0.3591 -0.0513 -0.1618 0.0192  436 HOH   A O   
6957 O  O   . HOH   E .   ? 0.6476 0.7398 0.4645 0.0707  0.3112  -0.0331 437 HOH   A O   
6958 O  O   A HOH   E .   ? 0.1659 0.1312 0.1391 -0.0168 -0.0076 -0.0085 438 HOH   A O   
6959 O  O   A HOH   E .   ? 0.1915 0.1847 0.2825 0.0201  -0.0310 -0.0468 439 HOH   A O   
6960 O  O   . HOH   E .   ? 0.4232 0.7285 0.5272 0.1398  0.0263  0.1557  440 HOH   A O   
6961 O  O   . HOH   E .   ? 0.5117 0.5633 0.6031 -0.1639 0.0006  -0.1213 441 HOH   A O   
6962 O  O   A HOH   E .   ? 0.2406 0.2149 0.2444 0.0209  -0.0990 -0.0325 442 HOH   A O   
6963 O  O   . HOH   E .   ? 0.1838 0.2134 0.5782 -0.0260 -0.0939 0.0598  443 HOH   A O   
6964 O  O   . HOH   E .   ? 0.3790 0.2728 0.1864 -0.0840 0.0340  0.0481  444 HOH   A O   
6965 O  O   . HOH   E .   ? 0.4150 0.3138 0.2942 -0.0562 0.0186  0.0428  445 HOH   A O   
6966 O  O   . HOH   E .   ? 0.6858 0.7003 0.6226 0.1184  -0.0690 0.0658  446 HOH   A O   
6967 O  O   . HOH   E .   ? 0.2430 0.1651 0.2873 0.0018  0.0027  0.0149  447 HOH   A O   
6968 O  O   . HOH   E .   ? 0.6831 0.8029 0.4308 0.2176  -0.1130 0.1960  448 HOH   A O   
6969 O  O   . HOH   E .   ? 0.4207 0.3836 0.3650 0.2382  -0.0452 -0.0346 449 HOH   A O   
6970 O  O   . HOH   E .   ? 0.2432 0.2211 0.2552 0.0287  0.0405  0.0315  450 HOH   A O   
6971 O  O   A HOH   E .   ? 0.2501 0.2338 0.3815 0.0232  0.1141  -0.0326 451 HOH   A O   
6972 O  O   . HOH   E .   ? 0.4783 0.4392 0.4852 -0.1044 -0.1084 -0.1036 452 HOH   A O   
6973 O  O   B HOH   E .   ? 0.3318 0.4281 0.4192 0.0663  0.0040  -0.0013 453 HOH   A O   
6974 O  O   . HOH   E .   ? 0.2124 0.2740 0.2507 0.0000  -0.0123 -0.0550 454 HOH   A O   
6975 O  O   A HOH   E .   ? 0.4813 0.2492 0.4902 0.0098  0.0518  -0.0546 455 HOH   A O   
6976 O  O   . HOH   E .   ? 0.4581 0.3943 0.4125 0.0201  -0.0412 0.0674  456 HOH   A O   
6977 O  O   . HOH   E .   ? 0.5696 0.6065 0.7928 0.0261  -0.1302 0.2320  457 HOH   A O   
6978 O  O   A HOH   E .   ? 0.5105 0.2366 0.3889 0.0720  0.1894  0.1152  458 HOH   A O   
6979 O  O   B HOH   E .   ? 0.3855 0.3805 0.4893 -0.0559 0.0853  -0.0048 459 HOH   A O   
6980 O  O   . HOH   E .   ? 0.6395 0.3172 0.4472 0.0966  0.0105  0.1351  460 HOH   A O   
6981 O  O   B HOH   E .   ? 0.1907 0.3126 0.2261 -0.0622 -0.0230 -0.0029 461 HOH   A O   
6982 O  O   . HOH   E .   ? 0.6589 0.5904 0.5058 -0.0493 0.1057  0.1194  462 HOH   A O   
6983 O  O   . HOH   E .   ? 0.2461 0.2463 0.3333 0.0353  -0.0444 0.0115  463 HOH   A O   
6984 O  O   . HOH   E .   ? 0.3173 0.2984 0.3576 -0.0710 0.0323  -0.0731 464 HOH   A O   
6985 O  O   . HOH   E .   ? 0.4979 0.3578 0.4861 0.0496  0.1071  0.0408  465 HOH   A O   
6986 O  O   . HOH   E .   ? 0.7295 0.7958 0.4832 0.0710  -0.1203 -0.0539 466 HOH   A O   
6987 O  O   B HOH   E .   ? 0.4242 0.1844 0.3568 0.0755  0.0968  0.0480  467 HOH   A O   
6988 O  O   . HOH   E .   ? 0.3211 0.4838 0.5145 -0.1374 0.1042  -0.1391 468 HOH   A O   
6989 O  O   . HOH   E .   ? 0.4315 0.4817 0.4520 0.1061  -0.0539 0.1363  469 HOH   A O   
6990 O  O   . HOH   E .   ? 0.3053 0.3792 0.3741 -0.0478 -0.0323 0.0219  470 HOH   A O   
6991 O  O   . HOH   E .   ? 0.2568 0.2867 0.3210 -0.0849 0.0430  -0.0195 471 HOH   A O   
6992 O  O   A HOH   E .   ? 0.2528 0.1742 0.4156 0.0548  -0.1336 -0.0125 472 HOH   A O   
6993 O  O   . HOH   E .   ? 0.2967 0.1765 0.2541 0.0404  -0.0898 -0.0228 473 HOH   A O   
6994 O  O   . HOH   E .   ? 0.6264 0.3642 0.8192 0.0764  0.1149  0.2575  474 HOH   A O   
6995 O  O   . HOH   E .   ? 0.2950 0.4008 0.5538 0.0402  0.0445  -0.1894 475 HOH   A O   
6996 O  O   . HOH   E .   ? 0.3980 0.6055 0.4070 -0.0928 -0.0592 0.2056  476 HOH   A O   
6997 O  O   . HOH   E .   ? 0.2908 0.2358 0.3436 0.0097  0.0293  -0.0107 477 HOH   A O   
6998 O  O   . HOH   E .   ? 0.6189 0.6153 0.6230 0.2141  0.2949  0.2457  478 HOH   A O   
6999 O  O   . HOH   E .   ? 0.5064 0.5324 0.4793 -0.0016 0.1098  0.0901  479 HOH   A O   
7000 O  O   . HOH   E .   ? 0.2605 0.2538 0.2518 0.0424  0.0001  0.0268  480 HOH   A O   
7001 O  O   B HOH   E .   ? 0.3344 0.3703 0.3368 0.0633  0.0744  -0.1023 481 HOH   A O   
7002 O  O   . HOH   E .   ? 0.4068 0.5124 0.3264 0.0057  -0.0622 -0.0148 482 HOH   A O   
7003 O  O   . HOH   E .   ? 0.5211 0.7079 0.6579 -0.1476 -0.1415 0.0572  483 HOH   A O   
7004 O  O   . HOH   E .   ? 0.4407 0.4850 0.5153 -0.2304 -0.0379 0.0232  484 HOH   A O   
7005 O  O   . HOH   E .   ? 0.4437 0.2827 0.3640 -0.0565 -0.1119 0.0632  485 HOH   A O   
7006 O  O   . HOH   E .   ? 0.5924 0.5599 0.5543 0.1008  -0.0393 -0.0634 486 HOH   A O   
7007 O  O   B HOH   E .   ? 0.2146 0.1995 0.4496 0.0508  0.0203  0.0763  487 HOH   A O   
7008 O  O   . HOH   E .   ? 0.6251 0.5109 0.6701 -0.0523 0.0617  -0.0131 488 HOH   A O   
7009 O  O   B HOH   E .   ? 0.4731 0.4267 0.3703 -0.0826 -0.0717 0.0804  489 HOH   A O   
7010 O  O   . HOH   E .   ? 0.4332 0.4820 0.2969 -0.0170 -0.0128 0.0251  490 HOH   A O   
7011 O  O   . HOH   E .   ? 0.4997 0.4553 0.3771 -0.0656 -0.0570 -0.0031 491 HOH   A O   
7012 O  O   . HOH   E .   ? 0.8460 0.4047 0.3223 -0.0877 -0.1133 -0.0250 492 HOH   A O   
7013 O  O   . HOH   E .   ? 0.5549 0.4426 0.4112 -0.0003 0.0106  -0.1283 493 HOH   A O   
7014 O  O   . HOH   E .   ? 0.6183 0.3906 0.4763 -0.0339 0.1658  0.0019  494 HOH   A O   
7015 O  O   . HOH   E .   ? 0.3105 0.4846 0.4770 0.0216  0.1364  0.1643  495 HOH   A O   
7016 O  O   . HOH   E .   ? 0.6023 0.6299 0.4578 -0.0432 0.1363  0.1057  496 HOH   A O   
7017 O  O   . HOH   E .   ? 0.3267 0.4875 0.3265 -0.0350 -0.0092 -0.0423 497 HOH   A O   
7018 O  O   . HOH   E .   ? 0.5085 0.3529 0.2463 -0.0906 0.1437  -0.0381 498 HOH   A O   
7019 O  O   . HOH   E .   ? 0.3001 0.5432 0.4065 0.1365  0.1221  0.2589  499 HOH   A O   
7020 O  O   . HOH   E .   ? 0.5717 0.5779 0.6871 0.0651  0.2547  -0.1182 500 HOH   A O   
7021 O  O   . HOH   E .   ? 0.2599 0.2456 0.7004 -0.0055 -0.1261 0.0205  501 HOH   A O   
7022 O  O   . HOH   E .   ? 0.5551 0.5893 0.5062 -0.0897 -0.1207 0.0570  502 HOH   A O   
7023 O  O   . HOH   E .   ? 0.6862 0.6457 0.5476 0.1757  -0.1505 -0.0658 503 HOH   A O   
7024 O  O   . HOH   E .   ? 0.6258 0.5363 0.5430 -0.0564 -0.1112 -0.0877 504 HOH   A O   
7025 O  O   . HOH   E .   ? 0.5047 0.3247 0.4469 0.0036  0.2468  0.0087  505 HOH   A O   
7026 O  O   . HOH   E .   ? 0.2960 0.2079 0.6286 0.0037  0.0771  0.0917  506 HOH   A O   
7027 O  O   . HOH   E .   ? 0.4088 0.3369 0.4672 -0.0815 0.0971  0.0819  507 HOH   A O   
7028 O  O   . HOH   E .   ? 0.2524 0.3650 0.5362 -0.0294 0.1041  -0.0837 508 HOH   A O   
7029 O  O   . HOH   E .   ? 0.6107 0.2664 0.5103 -0.0624 0.0661  0.0807  509 HOH   A O   
7030 O  O   B HOH   E .   ? 0.4870 0.5044 0.4186 0.1834  0.1145  -0.0925 510 HOH   A O   
7031 O  O   . HOH   E .   ? 0.4131 0.8523 0.5961 -0.1123 -0.0658 0.1924  511 HOH   A O   
7032 O  O   . HOH   E .   ? 0.4597 0.2832 0.4175 -0.1560 0.0202  0.0253  512 HOH   A O   
7033 O  O   . HOH   E .   ? 0.2350 0.2960 0.3835 0.0371  -0.0664 0.0526  513 HOH   A O   
7034 O  O   . HOH   E .   ? 0.2938 0.4837 0.3692 0.0957  -0.0119 0.0577  514 HOH   A O   
7035 O  O   . HOH   E .   ? 0.5516 0.7418 0.5600 0.1413  -0.0070 0.1496  515 HOH   A O   
7036 O  O   . HOH   E .   ? 0.7970 0.5726 0.5960 0.0039  0.0482  -0.0318 516 HOH   A O   
7037 O  O   . HOH   E .   ? 0.4882 0.6950 0.4162 0.3122  -0.0077 0.0993  517 HOH   A O   
7038 O  O   . HOH   E .   ? 0.3159 0.8165 0.2607 0.1254  0.0525  0.0727  518 HOH   A O   
7039 O  O   . HOH   E .   ? 0.2959 0.2227 0.4542 0.0088  0.0421  0.0598  519 HOH   A O   
7040 O  O   . HOH   E .   ? 0.5280 0.6291 0.4366 -0.0063 -0.1088 -0.1216 520 HOH   A O   
7041 O  O   . HOH   E .   ? 0.2684 0.7374 0.3296 0.0727  0.0036  0.0784  521 HOH   A O   
7042 O  O   . HOH   E .   ? 0.4933 0.4631 0.4221 0.1243  0.0584  0.1306  522 HOH   A O   
7043 O  O   . HOH   E .   ? 0.5204 0.5932 0.5187 -0.0885 -0.0237 0.0516  523 HOH   A O   
7044 O  O   . HOH   E .   ? 0.3745 0.4038 0.5318 -0.0337 -0.0844 0.2293  524 HOH   A O   
7045 O  O   . HOH   F .   ? 0.2260 0.2261 0.3214 0.0227  0.0704  0.0289  201 HOH   B O   
7046 O  O   . HOH   F .   ? 0.4658 0.3161 0.3907 -0.0470 -0.0277 -0.1115 202 HOH   B O   
7047 O  O   . HOH   F .   ? 0.3953 0.3818 0.5020 -0.1417 -0.0105 0.0781  203 HOH   B O   
7048 O  O   . HOH   F .   ? 0.3654 0.2735 0.7091 -0.0415 0.1300  -0.0043 204 HOH   B O   
7049 O  O   . HOH   F .   ? 0.4087 0.4290 0.5232 -0.1352 0.0343  -0.1723 205 HOH   B O   
7050 O  O   . HOH   F .   ? 0.7478 0.3431 0.5245 0.1000  0.1719  -0.0065 206 HOH   B O   
7051 O  O   . HOH   F .   ? 0.3262 0.2048 0.5149 0.0074  0.1978  0.0715  207 HOH   B O   
7052 O  O   . HOH   F .   ? 0.3237 0.7091 0.4003 0.1449  0.0414  0.2188  208 HOH   B O   
7053 O  O   . HOH   F .   ? 0.6125 0.6818 0.5979 0.1178  -0.0239 0.0476  209 HOH   B O   
7054 O  O   . HOH   F .   ? 0.4740 0.5892 0.3491 0.2834  -0.1057 -0.0264 210 HOH   B O   
7055 O  O   . HOH   F .   ? 0.2858 0.6091 0.4801 -0.0128 0.1434  -0.1910 211 HOH   B O   
7056 O  O   . HOH   F .   ? 0.6044 0.4362 0.5703 0.0988  -0.0893 0.2590  212 HOH   B O   
7057 O  O   . HOH   F .   ? 0.6402 0.6709 0.2472 0.1544  -0.0545 -0.1299 213 HOH   B O   
7058 O  O   . HOH   F .   ? 0.3690 0.6014 0.4722 0.2517  0.0098  -0.0937 214 HOH   B O   
7059 O  O   . HOH   F .   ? 0.4599 0.4486 0.3586 -0.0085 -0.1122 0.0923  215 HOH   B O   
7060 O  O   . HOH   F .   ? 0.2872 0.2952 0.6538 0.0717  -0.1067 0.0310  216 HOH   B O   
7061 O  O   . HOH   F .   ? 0.1578 0.2044 0.2726 -0.0205 -0.0116 0.0080  217 HOH   B O   
7062 O  O   . HOH   F .   ? 0.1960 0.2346 0.2793 -0.0048 0.0128  -0.0142 218 HOH   B O   
7063 O  O   . HOH   F .   ? 0.6043 0.3131 0.4007 -0.1907 0.0601  -0.0133 219 HOH   B O   
7064 O  O   . HOH   F .   ? 0.3733 0.5369 0.4488 0.2081  -0.0427 -0.0224 220 HOH   B O   
7065 O  O   . HOH   F .   ? 0.3553 0.2948 0.5439 0.0581  -0.0621 -0.0150 221 HOH   B O   
7066 O  O   . HOH   F .   ? 0.4382 0.4163 0.4271 0.0206  0.0960  -0.1646 222 HOH   B O   
7067 O  O   . HOH   F .   ? 0.5150 0.1980 0.3073 -0.0085 -0.0990 0.0150  223 HOH   B O   
7068 O  O   . HOH   F .   ? 0.6893 0.4327 0.5050 0.2092  0.0171  -0.1182 224 HOH   B O   
7069 O  O   . HOH   F .   ? 0.4073 0.2663 0.3745 0.1009  -0.0317 -0.0485 225 HOH   B O   
7070 O  O   . HOH   F .   ? 0.3609 0.3415 0.2160 0.0280  0.0580  0.0399  226 HOH   B O   
7071 O  O   . HOH   F .   ? 0.5758 0.6102 0.3086 0.0714  -0.0130 0.0149  227 HOH   B O   
7072 O  O   . HOH   F .   ? 0.3264 0.2285 0.4801 -0.0035 0.1756  -0.0028 228 HOH   B O   
7073 O  O   . HOH   F .   ? 0.2564 0.1815 0.2883 -0.0274 0.1039  -0.0001 229 HOH   B O   
7074 O  O   . HOH   F .   ? 0.1754 0.2107 0.2984 -0.0172 0.0071  -0.0141 230 HOH   B O   
7075 O  O   . HOH   F .   ? 0.3560 0.3927 0.3933 0.0831  -0.0907 -0.1788 231 HOH   B O   
7076 O  O   . HOH   F .   ? 0.2226 0.2224 0.3767 -0.0384 -0.0169 -0.0549 232 HOH   B O   
7077 O  O   . HOH   F .   ? 0.5319 0.3037 0.2685 0.0114  0.1059  -0.0328 233 HOH   B O   
7078 O  O   . HOH   F .   ? 0.2629 0.2599 0.2986 0.0249  0.0261  -0.0743 234 HOH   B O   
7079 O  O   . HOH   F .   ? 0.2627 0.4049 0.3241 -0.0673 0.0579  -0.0957 235 HOH   B O   
7080 O  O   . HOH   F .   ? 0.4082 0.4189 0.7209 -0.0292 -0.1708 -0.1063 236 HOH   B O   
7081 O  O   . HOH   F .   ? 0.4568 0.6285 0.3412 0.2559  0.0311  0.0190  237 HOH   B O   
7082 O  O   . HOH   F .   ? 0.3695 0.1825 0.2081 0.0256  -0.0780 -0.0202 238 HOH   B O   
7083 O  O   . HOH   F .   ? 0.2168 0.1322 0.3609 0.0119  -0.0665 -0.0186 239 HOH   B O   
7084 O  O   . HOH   F .   ? 0.2185 0.3770 0.3118 -0.0305 -0.0535 -0.0668 240 HOH   B O   
7085 O  O   . HOH   F .   ? 0.3181 0.3327 0.5986 0.0327  0.0622  0.0564  241 HOH   B O   
7086 O  O   . HOH   F .   ? 0.1441 0.1473 0.1669 -0.0128 -0.0057 -0.0010 242 HOH   B O   
7087 O  O   . HOH   F .   ? 0.2157 0.2372 0.2922 -0.0520 -0.0015 -0.0154 243 HOH   B O   
7088 O  O   . HOH   F .   ? 0.2419 0.2142 0.1910 0.0125  -0.0021 0.0119  244 HOH   B O   
7089 O  O   . HOH   F .   ? 0.3060 0.2439 0.3034 0.1017  0.0908  0.0093  245 HOH   B O   
7090 O  O   . HOH   F .   ? 0.1491 0.1315 0.1692 -0.0043 -0.0038 0.0080  246 HOH   B O   
7091 O  O   . HOH   F .   ? 0.4739 0.3162 0.4316 -0.2209 0.0424  -0.0076 247 HOH   B O   
7092 O  O   . HOH   F .   ? 0.1553 0.1540 0.2652 -0.0095 0.0042  -0.0131 248 HOH   B O   
7093 O  O   . HOH   F .   ? 0.2356 0.2062 0.2652 0.0681  -0.0711 -0.0642 249 HOH   B O   
7094 O  O   . HOH   F .   ? 0.2111 0.1456 0.2245 -0.0256 -0.0335 0.0219  250 HOH   B O   
7095 O  O   . HOH   F .   ? 0.2221 0.2020 0.2205 -0.0285 -0.0409 0.0120  251 HOH   B O   
7096 O  O   . HOH   F .   ? 0.3042 0.1788 0.5953 -0.0137 -0.1320 -0.0336 252 HOH   B O   
7097 O  O   . HOH   F .   ? 0.3067 0.2443 0.3077 -0.0391 0.0286  -0.0399 253 HOH   B O   
7098 O  O   . HOH   F .   ? 0.2073 0.3699 0.2403 -0.0304 -0.0184 0.0494  254 HOH   B O   
7099 O  O   . HOH   F .   ? 0.2830 0.4332 0.3590 -0.1006 -0.0319 -0.0863 255 HOH   B O   
7100 O  O   . HOH   F .   ? 0.3434 0.3212 0.2319 0.0535  0.0787  0.0308  256 HOH   B O   
7101 O  O   . HOH   F .   ? 0.2278 0.2193 0.1858 0.0040  -0.0018 0.0033  257 HOH   B O   
7102 O  O   . HOH   F .   ? 0.2303 0.3116 0.2336 -0.0506 0.0301  0.0552  258 HOH   B O   
7103 O  O   . HOH   F .   ? 0.1795 0.2758 0.2882 0.0434  0.0380  0.0986  259 HOH   B O   
7104 O  O   . HOH   F .   ? 0.1633 0.1652 0.3173 -0.0175 -0.0198 0.0153  260 HOH   B O   
7105 O  O   . HOH   F .   ? 0.2257 0.1991 0.3874 0.0135  -0.0538 -0.0514 261 HOH   B O   
7106 O  O   . HOH   F .   ? 0.2959 0.5284 0.3748 -0.0336 -0.0949 0.1750  262 HOH   B O   
7107 O  O   . HOH   F .   ? 0.1425 0.1680 0.2096 -0.0069 0.0046  0.0179  263 HOH   B O   
7108 O  O   . HOH   F .   ? 0.3377 0.4992 0.4958 0.0247  0.0245  -0.0829 264 HOH   B O   
7109 O  O   . HOH   F .   ? 0.2461 0.2785 0.2363 -0.0515 -0.0631 -0.0359 265 HOH   B O   
7110 O  O   . HOH   F .   ? 0.2032 0.1564 0.2372 -0.0302 -0.0202 0.0172  266 HOH   B O   
7111 O  O   . HOH   F .   ? 0.2576 0.2003 0.2975 -0.0581 0.0253  -0.0094 267 HOH   B O   
7112 O  O   . HOH   F .   ? 0.2631 0.4699 0.4892 0.1495  -0.0439 -0.0471 268 HOH   B O   
7113 O  O   . HOH   F .   ? 0.2211 0.2478 0.2518 0.0680  -0.0206 -0.0165 269 HOH   B O   
7114 O  O   . HOH   F .   ? 0.4176 0.3656 0.3654 -0.0701 0.0972  -0.0936 270 HOH   B O   
7115 O  O   . HOH   F .   ? 0.2113 0.4431 0.4570 -0.0455 -0.0485 -0.1328 271 HOH   B O   
7116 O  O   . HOH   F .   ? 0.3307 0.7023 0.3381 0.2062  -0.0196 0.0522  272 HOH   B O   
7117 O  O   . HOH   F .   ? 0.4626 0.3351 0.2823 0.0668  -0.0254 -0.1081 273 HOH   B O   
7118 O  O   . HOH   F .   ? 0.2574 0.3984 0.3508 0.0177  0.0944  0.0195  274 HOH   B O   
7119 O  O   . HOH   F .   ? 0.1749 0.1493 0.4716 -0.0125 -0.0239 -0.0087 275 HOH   B O   
7120 O  O   . HOH   F .   ? 0.1919 0.1806 0.1692 -0.0432 -0.0397 0.0119  276 HOH   B O   
7121 O  O   . HOH   F .   ? 0.2333 0.3142 0.3442 -0.0439 0.0453  -0.1036 277 HOH   B O   
7122 O  O   . HOH   F .   ? 0.2765 0.2693 0.2593 -0.0307 -0.0899 0.0130  278 HOH   B O   
7123 O  O   . HOH   F .   ? 0.4359 0.2532 0.5217 0.0007  0.0474  -0.0751 279 HOH   B O   
7124 O  O   . HOH   F .   ? 0.3820 0.5235 0.4165 -0.0064 -0.1189 0.0200  280 HOH   B O   
7125 O  O   . HOH   F .   ? 0.3627 0.3740 0.4760 0.1288  -0.0823 -0.1046 281 HOH   B O   
7126 O  O   . HOH   F .   ? 0.1650 0.1547 0.3366 -0.0143 0.0033  -0.0071 282 HOH   B O   
7127 O  O   . HOH   F .   ? 0.2719 0.4885 0.5318 -0.0967 -0.1209 0.1296  283 HOH   B O   
7128 O  O   . HOH   F .   ? 0.3917 0.2088 0.3967 -0.0850 -0.2002 0.0689  284 HOH   B O   
7129 O  O   . HOH   F .   ? 0.3694 0.2790 0.2164 0.0472  -0.0811 -0.0202 285 HOH   B O   
7130 O  O   . HOH   F .   ? 0.1616 0.1609 0.1753 0.0022  0.0039  0.0054  286 HOH   B O   
7131 O  O   . HOH   F .   ? 0.1728 0.1945 0.2826 0.0228  -0.0113 0.0008  287 HOH   B O   
7132 O  O   . HOH   F .   ? 0.4119 0.2946 0.4757 -0.0367 -0.1203 -0.0764 288 HOH   B O   
7133 O  O   . HOH   F .   ? 0.1679 0.2044 0.1567 -0.0159 -0.0173 0.0015  289 HOH   B O   
7134 O  O   . HOH   F .   ? 0.2506 0.2648 0.2885 0.0253  -0.0655 0.0242  290 HOH   B O   
7135 O  O   . HOH   F .   ? 0.5171 0.6025 0.2729 0.0229  -0.0916 0.0936  291 HOH   B O   
7136 O  O   . HOH   F .   ? 0.3069 0.2074 0.4819 0.0256  0.0560  0.0573  292 HOH   B O   
7137 O  O   . HOH   F .   ? 0.2061 0.2692 0.6726 0.0454  -0.0429 -0.1194 293 HOH   B O   
7138 O  O   . HOH   F .   ? 0.2648 0.6108 0.7052 0.0714  -0.0527 -0.1068 294 HOH   B O   
7139 O  O   . HOH   F .   ? 0.3042 0.2845 0.2757 -0.0133 0.0001  -0.1143 295 HOH   B O   
7140 O  O   . HOH   F .   ? 0.4341 0.3877 0.6124 0.0482  -0.0156 0.0030  296 HOH   B O   
7141 O  O   . HOH   F .   ? 0.1641 0.1516 0.3215 0.0040  0.0060  -0.0005 297 HOH   B O   
7142 O  O   . HOH   F .   ? 0.2945 0.2850 0.5011 -0.0156 -0.0662 0.1058  298 HOH   B O   
7143 O  O   . HOH   F .   ? 0.1740 0.2981 0.4650 0.0098  -0.0027 -0.1203 299 HOH   B O   
7144 O  O   . HOH   F .   ? 0.6126 0.5226 0.5492 -0.1233 -0.0399 0.1361  300 HOH   B O   
7145 O  O   . HOH   F .   ? 0.4508 0.3665 0.2435 0.1034  -0.0632 0.0598  301 HOH   B O   
7146 O  O   . HOH   F .   ? 0.1774 0.1583 0.2320 0.0085  0.0068  0.0197  302 HOH   B O   
7147 O  O   . HOH   F .   ? 0.2607 0.6815 0.2651 0.0511  -0.0311 -0.0469 303 HOH   B O   
7148 O  O   . HOH   F .   ? 0.4513 0.3543 0.4596 -0.0710 0.0555  0.1214  304 HOH   B O   
7149 O  O   . HOH   F .   ? 0.3274 0.1879 0.3512 0.0697  0.1232  0.0490  305 HOH   B O   
7150 O  O   . HOH   F .   ? 0.3328 0.3576 0.3944 -0.1195 0.1186  -0.0520 306 HOH   B O   
7151 O  O   . HOH   F .   ? 0.4061 0.4870 0.2049 0.0051  0.0566  0.0532  307 HOH   B O   
7152 O  O   . HOH   F .   ? 0.2150 0.1585 0.3446 0.0332  -0.1022 -0.0107 308 HOH   B O   
7153 O  O   . HOH   F .   ? 0.4852 0.3004 0.2607 -0.1815 0.0877  -0.0254 309 HOH   B O   
7154 O  O   . HOH   F .   ? 0.2142 0.1596 0.2644 -0.0276 -0.0280 0.0015  310 HOH   B O   
7155 O  O   . HOH   F .   ? 0.6422 0.6034 0.5529 0.2824  -0.0178 -0.0350 311 HOH   B O   
7156 O  O   . HOH   F .   ? 0.2273 0.3313 0.5336 -0.0180 -0.0672 -0.0242 312 HOH   B O   
7157 O  O   . HOH   F .   ? 0.2690 0.3159 0.3361 -0.0393 0.0921  -0.0820 313 HOH   B O   
7158 O  O   . HOH   F .   ? 0.5806 0.3846 0.3361 0.2652  0.0931  0.0760  314 HOH   B O   
7159 O  O   . HOH   F .   ? 0.1624 0.2004 0.2840 -0.0306 -0.0156 0.0131  315 HOH   B O   
7160 O  O   . HOH   F .   ? 0.2455 0.1541 0.2447 -0.0145 -0.0139 0.0329  316 HOH   B O   
7161 O  O   . HOH   F .   ? 0.2134 0.1956 0.1825 -0.0067 0.0137  0.0199  317 HOH   B O   
7162 O  O   . HOH   F .   ? 0.5295 0.3794 0.2510 0.1165  -0.0868 -0.0239 318 HOH   B O   
7163 O  O   . HOH   F .   ? 0.4321 0.2282 0.2727 0.1550  0.1060  0.0386  319 HOH   B O   
7164 O  O   . HOH   F .   ? 0.5879 0.3325 0.4490 0.0049  0.1400  -0.1568 320 HOH   B O   
7165 O  O   . HOH   F .   ? 0.1628 0.3004 0.2454 -0.0119 -0.0276 0.0731  321 HOH   B O   
7166 O  O   . HOH   F .   ? 0.3387 0.3846 0.7548 -0.0262 -0.0929 0.1976  322 HOH   B O   
7167 O  O   . HOH   F .   ? 0.4667 0.4172 0.2562 0.0427  -0.0357 -0.0535 323 HOH   B O   
7168 O  O   . HOH   F .   ? 0.6878 0.4595 0.5718 0.1973  0.1279  0.0030  324 HOH   B O   
7169 O  O   . HOH   F .   ? 0.1641 0.1641 0.3011 -0.0148 -0.0124 -0.0064 325 HOH   B O   
7170 O  O   . HOH   F .   ? 0.4523 0.3430 0.5453 0.1375  0.2172  0.1921  326 HOH   B O   
7171 O  O   . HOH   F .   ? 0.2837 0.2267 0.2217 0.0261  -0.0232 0.0216  327 HOH   B O   
7172 O  O   . HOH   F .   ? 0.2701 0.3198 0.5347 -0.0451 -0.1755 0.1491  328 HOH   B O   
7173 O  O   . HOH   F .   ? 0.1922 0.2099 0.3029 0.0322  0.0373  0.0154  329 HOH   B O   
7174 O  O   . HOH   F .   ? 0.2471 0.5931 0.5397 -0.0613 -0.0054 -0.0293 330 HOH   B O   
7175 O  O   . HOH   F .   ? 0.1909 0.3037 0.3066 0.0358  -0.0068 -0.0673 331 HOH   B O   
7176 O  O   . HOH   F .   ? 0.2738 0.2018 0.5444 0.0078  -0.0155 0.0375  332 HOH   B O   
7177 O  O   . HOH   F .   ? 0.6583 0.3393 0.3413 0.0106  0.1335  0.1097  333 HOH   B O   
7178 O  O   . HOH   F .   ? 0.5089 0.6097 0.3327 0.0436  -0.0931 0.0564  334 HOH   B O   
7179 O  O   . HOH   F .   ? 0.2291 0.2440 0.5804 -0.0465 -0.0071 0.1531  335 HOH   B O   
7180 O  O   . HOH   F .   ? 0.4930 0.2480 0.3071 0.0566  0.0587  0.0888  336 HOH   B O   
7181 O  O   . HOH   F .   ? 0.7742 0.2252 0.3161 0.0220  -0.0909 -0.0105 337 HOH   B O   
7182 O  O   . HOH   F .   ? 0.1773 0.1543 0.2329 0.0103  -0.0141 0.0074  338 HOH   B O   
7183 O  O   . HOH   F .   ? 0.6371 0.4614 0.6100 -0.0721 -0.1159 -0.1450 339 HOH   B O   
7184 O  O   . HOH   F .   ? 0.5238 0.5320 0.6418 0.0736  -0.0490 0.2356  340 HOH   B O   
7185 O  O   . HOH   F .   ? 0.4382 0.7089 0.3210 0.0434  -0.0430 0.1239  341 HOH   B O   
7186 O  O   . HOH   F .   ? 0.2545 0.5666 0.7081 -0.0526 -0.0031 0.1530  342 HOH   B O   
7187 O  O   . HOH   F .   ? 0.5763 0.3420 0.3149 0.0924  -0.1301 -0.0621 343 HOH   B O   
7188 O  O   . HOH   F .   ? 0.4429 0.4863 0.4755 0.0036  -0.0873 0.0250  344 HOH   B O   
7189 O  O   . HOH   F .   ? 0.2070 0.2016 0.2902 -0.0074 0.0565  -0.0012 345 HOH   B O   
7190 O  O   . HOH   F .   ? 0.4171 0.5574 0.4049 -0.0747 -0.0976 -0.0642 346 HOH   B O   
7191 O  O   . HOH   F .   ? 0.5802 0.6366 0.2800 0.0367  -0.0290 0.1217  347 HOH   B O   
7192 O  O   . HOH   F .   ? 0.2809 0.2299 0.5209 -0.0322 -0.0899 -0.0514 348 HOH   B O   
7193 O  O   . HOH   F .   ? 0.4560 0.5993 0.7196 0.0339  0.0642  -0.0943 349 HOH   B O   
7194 O  O   . HOH   F .   ? 0.3424 0.2264 0.3467 -0.0541 -0.0172 -0.0651 350 HOH   B O   
7195 O  O   . HOH   F .   ? 0.4848 0.3537 0.5917 -0.1161 0.1841  0.0629  351 HOH   B O   
7196 O  O   . HOH   F .   ? 0.2250 0.5944 0.3406 0.1430  -0.0508 -0.1399 352 HOH   B O   
7197 O  O   . HOH   F .   ? 0.4562 0.5553 0.5140 -0.1184 0.0886  0.0393  353 HOH   B O   
7198 O  O   . HOH   F .   ? 0.2308 0.3821 0.5097 0.0150  0.0277  0.0516  354 HOH   B O   
7199 O  O   . HOH   F .   ? 0.3485 0.4086 0.4742 -0.1513 0.0529  -0.0252 355 HOH   B O   
7200 O  O   . HOH   F .   ? 0.4699 0.3863 0.4280 0.0502  0.1228  -0.0389 356 HOH   B O   
7201 O  O   . HOH   F .   ? 0.3257 0.2008 0.4015 0.0528  -0.1251 -0.0560 357 HOH   B O   
7202 O  O   . HOH   F .   ? 0.3736 0.2956 0.4171 -0.1026 -0.0413 -0.0547 358 HOH   B O   
7203 O  O   . HOH   F .   ? 0.4690 0.6047 0.5153 0.2116  -0.1159 0.1508  359 HOH   B O   
7204 O  O   . HOH   F .   ? 0.3906 0.4891 0.5290 -0.0189 -0.0442 -0.0212 360 HOH   B O   
7205 O  O   . HOH   F .   ? 0.4339 0.3583 0.4874 0.0234  -0.1590 -0.0418 361 HOH   B O   
7206 O  O   . HOH   F .   ? 0.5815 0.4143 0.5560 -0.0011 0.0650  0.1073  362 HOH   B O   
7207 O  O   . HOH   F .   ? 0.2150 0.3633 0.6866 -0.0665 -0.0535 -0.0801 363 HOH   B O   
7208 O  O   . HOH   F .   ? 0.4767 0.6706 0.3262 0.2430  -0.0452 0.0189  364 HOH   B O   
7209 O  O   . HOH   F .   ? 0.6257 0.4877 0.4339 0.1765  0.1039  0.0648  365 HOH   B O   
7210 O  O   . HOH   F .   ? 0.6092 0.5397 0.3298 0.1211  -0.1606 0.0278  366 HOH   B O   
7211 O  O   . HOH   F .   ? 0.5289 0.3160 0.5962 -0.1356 -0.0664 0.0230  367 HOH   B O   
7212 O  O   . HOH   F .   ? 0.5193 0.5638 0.4320 -0.0835 -0.0732 -0.1078 368 HOH   B O   
7213 O  O   . HOH   F .   ? 0.5121 0.3691 0.5188 0.0668  -0.1730 -0.0074 369 HOH   B O   
7214 O  O   . HOH   F .   ? 0.7536 0.7709 0.5058 0.2822  -0.1273 0.1606  370 HOH   B O   
7215 O  O   . HOH   F .   ? 0.4532 0.6541 0.5677 0.2848  0.0437  0.1353  371 HOH   B O   
7216 O  O   . HOH   F .   ? 0.6051 0.2386 0.3712 0.0357  0.0421  0.0784  372 HOH   B O   
7217 O  O   . HOH   F .   ? 0.4601 0.3422 0.3848 0.0750  -0.1555 -0.0547 373 HOH   B O   
7218 O  O   . HOH   F .   ? 0.6095 0.4110 0.2982 -0.0838 -0.0936 -0.0558 374 HOH   B O   
7219 O  O   . HOH   F .   ? 0.4402 0.4490 0.4973 -0.0760 -0.0580 0.0395  375 HOH   B O   
7220 O  O   . HOH   F .   ? 0.2376 0.4387 0.4275 0.0349  -0.0689 -0.0736 376 HOH   B O   
7221 O  O   . HOH   F .   ? 0.4666 0.7552 0.5986 0.1514  0.0975  0.3285  377 HOH   B O   
7222 O  O   . HOH   F .   ? 0.3120 0.3810 0.2207 0.0462  0.0059  -0.0016 378 HOH   B O   
7223 O  O   . HOH   F .   ? 0.4735 0.7469 0.3705 -0.1361 0.0634  -0.1531 379 HOH   B O   
7224 O  O   . HOH   F .   ? 0.3585 0.5187 0.5793 0.1235  -0.0751 0.0481  380 HOH   B O   
7225 O  O   . HOH   F .   ? 0.7682 0.3617 0.5124 -0.1160 -0.0654 -0.0182 381 HOH   B O   
7226 O  O   . HOH   F .   ? 0.2942 0.2719 0.3337 0.0034  0.0205  0.0419  382 HOH   B O   
7227 O  O   . HOH   F .   ? 0.5780 0.6722 0.6091 0.0491  0.2398  0.1705  383 HOH   B O   
7228 O  O   . HOH   F .   ? 0.4188 0.7580 0.5685 0.1064  0.1720  0.1109  384 HOH   B O   
7229 O  O   . HOH   F .   ? 0.6985 0.3941 0.4952 0.1262  0.0827  -0.0720 385 HOH   B O   
7230 O  O   . HOH   F .   ? 0.6167 0.4633 0.5033 -0.0925 -0.0050 0.0174  386 HOH   B O   
7231 O  O   . HOH   F .   ? 0.2407 0.4252 0.3702 -0.0722 -0.0935 -0.0300 387 HOH   B O   
7232 O  O   . HOH   F .   ? 0.4663 0.3928 0.3313 0.0542  0.0633  0.0194  388 HOH   B O   
7233 O  O   . HOH   F .   ? 0.5178 0.4898 0.3920 -0.0168 -0.0745 -0.0505 389 HOH   B O   
7234 O  O   . HOH   F .   ? 0.7466 0.5544 0.4153 0.1906  -0.0159 0.0650  390 HOH   B O   
7235 O  O   . HOH   F .   ? 0.4433 0.2334 0.3051 0.1134  -0.0368 0.0151  391 HOH   B O   
7236 O  O   . HOH   F .   ? 0.4948 0.4208 0.3641 0.0216  -0.0041 0.0793  392 HOH   B O   
7237 O  O   . HOH   F .   ? 0.5707 0.2320 0.4986 -0.0961 0.0659  0.0595  393 HOH   B O   
7238 O  O   . HOH   F .   ? 0.2389 0.4185 0.6486 -0.1269 -0.0711 0.0177  394 HOH   B O   
7239 O  O   . HOH   F .   ? 0.4285 0.4288 0.4306 0.0159  0.0998  0.0735  395 HOH   B O   
7240 O  O   . HOH   F .   ? 0.3341 0.3621 0.3412 0.0354  0.0371  -0.0708 396 HOH   B O   
7241 O  O   . HOH   F .   ? 0.4301 0.6074 0.3313 0.1259  -0.0353 -0.0878 397 HOH   B O   
7242 O  O   . HOH   F .   ? 0.2184 0.2831 0.6210 -0.0539 -0.0797 0.0291  398 HOH   B O   
7243 O  O   . HOH   F .   ? 0.6263 0.6337 0.6936 0.1237  -0.1230 0.2651  399 HOH   B O   
7244 O  O   . HOH   F .   ? 0.5384 0.4287 0.3136 -0.1899 -0.0206 0.1195  400 HOH   B O   
7245 O  O   . HOH   F .   ? 0.6322 0.7013 0.3741 0.1241  -0.0198 0.0183  401 HOH   B O   
# 
