data_7HES
# 
_entry.id   7HES 
# 
_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   7HES         pdb_00007hes 10.2210/pdb7hes/pdb 
WWPDB D_1001407382 ?            ?                   
# 
_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                        7HES 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                        18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 
'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                            114.023   1   ?                      ? ? ? 
3 non-polymer syn '{1-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclopentyl}methanol' 232.282   1   ?                      ? ? ? 
4 water       nat water                                                             18.015    409 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                            TFA   
3 '{1-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclopentyl}methanol' A1A98 
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 
A1A98 non-polymer         . '{1-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclopentyl}methanol' ? 'C12 H16 N4 O'   232.282 
ALA   'L-peptide linking' y ALANINE                                                           ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                          ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                        ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                   ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                          ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                         ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                   ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                           ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                         ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                             ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                           ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                            ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                        ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                     ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                           ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                            ? 'C3 H7 N O3'     105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                            ? 'C2 H F3 O2'     114.023 
THR   'L-peptide linking' y THREONINE                                                         ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                          ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                            ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1A98 1   202 201  A1A98 LA1 A . 
E 4 HOH   1   301 196  HOH   HOH A . 
E 4 HOH   2   302 292  HOH   HOH A . 
E 4 HOH   3   303 229  HOH   HOH A . 
E 4 HOH   4   304 209  HOH   HOH A . 
E 4 HOH   5   305 93   HOH   HOH A . 
E 4 HOH   6   306 153  HOH   HOH A . 
E 4 HOH   7   307 36   HOH   HOH A . 
E 4 HOH   8   308 49   HOH   HOH A . 
E 4 HOH   9   309 409  HOH   HOH A . 
E 4 HOH   10  310 625  HOH   HOH A . 
E 4 HOH   11  311 18   HOH   HOH A . 
E 4 HOH   12  312 1310 HOH   HOH A . 
E 4 HOH   13  313 1289 HOH   HOH A . 
E 4 HOH   14  314 1295 HOH   HOH A . 
E 4 HOH   15  315 1309 HOH   HOH A . 
E 4 HOH   16  316 337  HOH   HOH A . 
E 4 HOH   17  317 57   HOH   HOH A . 
E 4 HOH   18  318 136  HOH   HOH A . 
E 4 HOH   19  319 124  HOH   HOH A . 
E 4 HOH   20  320 1296 HOH   HOH A . 
E 4 HOH   21  321 661  HOH   HOH A . 
E 4 HOH   22  322 34   HOH   HOH A . 
E 4 HOH   23  323 86   HOH   HOH A . 
E 4 HOH   24  324 109  HOH   HOH A . 
E 4 HOH   25  325 247  HOH   HOH A . 
E 4 HOH   26  326 1301 HOH   HOH A . 
E 4 HOH   27  327 76   HOH   HOH A . 
E 4 HOH   28  328 469  HOH   HOH A . 
E 4 HOH   29  329 195  HOH   HOH A . 
E 4 HOH   30  330 151  HOH   HOH A . 
E 4 HOH   31  331 236  HOH   HOH A . 
E 4 HOH   32  332 192  HOH   HOH A . 
E 4 HOH   33  333 33   HOH   HOH A . 
E 4 HOH   34  334 96   HOH   HOH A . 
E 4 HOH   35  335 21   HOH   HOH A . 
E 4 HOH   36  336 1300 HOH   HOH A . 
E 4 HOH   37  337 164  HOH   HOH A . 
E 4 HOH   38  338 1308 HOH   HOH A . 
E 4 HOH   39  339 165  HOH   HOH A . 
E 4 HOH   40  340 964  HOH   HOH A . 
E 4 HOH   41  341 393  HOH   HOH A . 
E 4 HOH   42  342 105  HOH   HOH A . 
E 4 HOH   43  343 320  HOH   HOH A . 
E 4 HOH   44  344 1283 HOH   HOH A . 
E 4 HOH   45  345 1290 HOH   HOH A . 
E 4 HOH   46  346 140  HOH   HOH A . 
E 4 HOH   47  347 6    HOH   HOH A . 
E 4 HOH   48  348 354  HOH   HOH A . 
E 4 HOH   49  349 169  HOH   HOH A . 
E 4 HOH   50  350 241  HOH   HOH A . 
E 4 HOH   51  351 39   HOH   HOH A . 
E 4 HOH   52  352 42   HOH   HOH A . 
E 4 HOH   53  353 92   HOH   HOH A . 
E 4 HOH   54  354 218  HOH   HOH A . 
E 4 HOH   55  355 155  HOH   HOH A . 
E 4 HOH   56  356 225  HOH   HOH A . 
E 4 HOH   57  357 2    HOH   HOH A . 
E 4 HOH   58  358 630  HOH   HOH A . 
E 4 HOH   59  359 85   HOH   HOH A . 
E 4 HOH   60  360 17   HOH   HOH A . 
E 4 HOH   61  361 19   HOH   HOH A . 
E 4 HOH   62  362 939  HOH   HOH A . 
E 4 HOH   63  363 662  HOH   HOH A . 
E 4 HOH   64  364 102  HOH   HOH A . 
E 4 HOH   65  365 62   HOH   HOH A . 
E 4 HOH   66  366 139  HOH   HOH A . 
E 4 HOH   67  367 66   HOH   HOH A . 
E 4 HOH   68  368 81   HOH   HOH A . 
E 4 HOH   69  369 396  HOH   HOH A . 
E 4 HOH   70  370 296  HOH   HOH A . 
E 4 HOH   71  371 5    HOH   HOH A . 
E 4 HOH   72  372 46   HOH   HOH A . 
E 4 HOH   73  373 162  HOH   HOH A . 
E 4 HOH   74  374 35   HOH   HOH A . 
E 4 HOH   75  375 366  HOH   HOH A . 
E 4 HOH   76  376 45   HOH   HOH A . 
E 4 HOH   77  377 56   HOH   HOH A . 
E 4 HOH   78  378 154  HOH   HOH A . 
E 4 HOH   79  379 159  HOH   HOH A . 
E 4 HOH   80  380 186  HOH   HOH A . 
E 4 HOH   81  381 115  HOH   HOH A . 
E 4 HOH   82  382 140  HOH   HOH A . 
E 4 HOH   83  383 27   HOH   HOH A . 
E 4 HOH   84  384 26   HOH   HOH A . 
E 4 HOH   85  385 138  HOH   HOH A . 
E 4 HOH   86  386 24   HOH   HOH A . 
E 4 HOH   87  387 116  HOH   HOH A . 
E 4 HOH   88  388 134  HOH   HOH A . 
E 4 HOH   89  389 461  HOH   HOH A . 
E 4 HOH   90  390 132  HOH   HOH A . 
E 4 HOH   91  391 405  HOH   HOH A . 
E 4 HOH   92  392 58   HOH   HOH A . 
E 4 HOH   93  393 199  HOH   HOH A . 
E 4 HOH   94  394 1313 HOH   HOH A . 
E 4 HOH   95  395 303  HOH   HOH A . 
E 4 HOH   96  396 74   HOH   HOH A . 
E 4 HOH   97  397 12   HOH   HOH A . 
E 4 HOH   98  398 78   HOH   HOH A . 
E 4 HOH   99  399 278  HOH   HOH A . 
E 4 HOH   100 400 148  HOH   HOH A . 
E 4 HOH   101 401 281  HOH   HOH A . 
E 4 HOH   102 402 67   HOH   HOH A . 
E 4 HOH   103 403 333  HOH   HOH A . 
E 4 HOH   104 404 83   HOH   HOH A . 
E 4 HOH   105 405 25   HOH   HOH A . 
E 4 HOH   106 406 351  HOH   HOH A . 
E 4 HOH   107 407 70   HOH   HOH A . 
E 4 HOH   108 408 3    HOH   HOH A . 
E 4 HOH   109 409 122  HOH   HOH A . 
E 4 HOH   110 410 4    HOH   HOH A . 
E 4 HOH   111 411 493  HOH   HOH A . 
E 4 HOH   112 412 123  HOH   HOH A . 
E 4 HOH   113 413 1315 HOH   HOH A . 
E 4 HOH   114 414 68   HOH   HOH A . 
E 4 HOH   115 415 1068 HOH   HOH A . 
E 4 HOH   116 416 125  HOH   HOH A . 
E 4 HOH   117 417 8    HOH   HOH A . 
E 4 HOH   118 418 1279 HOH   HOH A . 
E 4 HOH   119 419 121  HOH   HOH A . 
E 4 HOH   120 420 53   HOH   HOH A . 
E 4 HOH   121 421 1275 HOH   HOH A . 
E 4 HOH   122 422 51   HOH   HOH A . 
E 4 HOH   123 423 95   HOH   HOH A . 
E 4 HOH   124 424 381  HOH   HOH A . 
E 4 HOH   125 425 397  HOH   HOH A . 
E 4 HOH   126 426 156  HOH   HOH A . 
E 4 HOH   127 427 1222 HOH   HOH A . 
E 4 HOH   128 428 952  HOH   HOH A . 
E 4 HOH   129 429 7    HOH   HOH A . 
E 4 HOH   130 430 582  HOH   HOH A . 
E 4 HOH   131 431 80   HOH   HOH A . 
E 4 HOH   132 432 71   HOH   HOH A . 
E 4 HOH   133 433 40   HOH   HOH A . 
E 4 HOH   134 434 212  HOH   HOH A . 
E 4 HOH   135 435 1238 HOH   HOH A . 
E 4 HOH   136 436 79   HOH   HOH A . 
E 4 HOH   137 437 16   HOH   HOH A . 
E 4 HOH   138 438 104  HOH   HOH A . 
E 4 HOH   139 439 576  HOH   HOH A . 
E 4 HOH   140 440 94   HOH   HOH A . 
E 4 HOH   141 441 944  HOH   HOH A . 
E 4 HOH   142 442 188  HOH   HOH A . 
E 4 HOH   143 443 73   HOH   HOH A . 
E 4 HOH   144 444 1189 HOH   HOH A . 
E 4 HOH   145 445 97   HOH   HOH A . 
E 4 HOH   146 446 1094 HOH   HOH A . 
E 4 HOH   147 447 1286 HOH   HOH A . 
E 4 HOH   148 448 509  HOH   HOH A . 
E 4 HOH   149 449 107  HOH   HOH A . 
E 4 HOH   150 450 330  HOH   HOH A . 
E 4 HOH   151 451 1134 HOH   HOH A . 
E 4 HOH   152 452 726  HOH   HOH A . 
E 4 HOH   153 453 1119 HOH   HOH A . 
E 4 HOH   154 454 163  HOH   HOH A . 
E 4 HOH   155 455 342  HOH   HOH A . 
E 4 HOH   156 456 408  HOH   HOH A . 
E 4 HOH   157 457 280  HOH   HOH A . 
E 4 HOH   158 458 756  HOH   HOH A . 
E 4 HOH   159 459 361  HOH   HOH A . 
E 4 HOH   160 460 319  HOH   HOH A . 
E 4 HOH   161 461 801  HOH   HOH A . 
E 4 HOH   162 462 126  HOH   HOH A . 
E 4 HOH   163 463 370  HOH   HOH A . 
E 4 HOH   164 464 1307 HOH   HOH A . 
E 4 HOH   165 465 556  HOH   HOH A . 
E 4 HOH   166 466 63   HOH   HOH A . 
E 4 HOH   167 467 1284 HOH   HOH A . 
E 4 HOH   168 468 1276 HOH   HOH A . 
E 4 HOH   169 469 250  HOH   HOH A . 
E 4 HOH   170 470 224  HOH   HOH A . 
E 4 HOH   171 471 1287 HOH   HOH A . 
E 4 HOH   172 472 711  HOH   HOH A . 
E 4 HOH   173 473 202  HOH   HOH A . 
E 4 HOH   174 474 208  HOH   HOH A . 
E 4 HOH   175 475 1306 HOH   HOH A . 
E 4 HOH   176 476 152  HOH   HOH A . 
E 4 HOH   177 477 695  HOH   HOH A . 
E 4 HOH   178 478 674  HOH   HOH A . 
E 4 HOH   179 479 919  HOH   HOH A . 
E 4 HOH   180 480 135  HOH   HOH A . 
E 4 HOH   181 481 267  HOH   HOH A . 
E 4 HOH   182 482 318  HOH   HOH A . 
E 4 HOH   183 483 1314 HOH   HOH A . 
E 4 HOH   184 484 941  HOH   HOH A . 
E 4 HOH   185 485 521  HOH   HOH A . 
E 4 HOH   186 486 331  HOH   HOH A . 
E 4 HOH   187 487 805  HOH   HOH A . 
E 4 HOH   188 488 1299 HOH   HOH A . 
E 4 HOH   189 489 309  HOH   HOH A . 
E 4 HOH   190 490 315  HOH   HOH A . 
E 4 HOH   191 491 263  HOH   HOH A . 
E 4 HOH   192 492 1071 HOH   HOH A . 
E 4 HOH   193 493 180  HOH   HOH A . 
E 4 HOH   194 494 363  HOH   HOH A . 
E 4 HOH   195 495 326  HOH   HOH A . 
E 4 HOH   196 496 356  HOH   HOH A . 
E 4 HOH   197 497 371  HOH   HOH A . 
E 4 HOH   198 498 313  HOH   HOH A . 
E 4 HOH   199 499 376  HOH   HOH A . 
E 4 HOH   200 500 429  HOH   HOH A . 
E 4 HOH   201 501 185  HOH   HOH A . 
E 4 HOH   202 502 70   HOH   HOH A . 
E 4 HOH   203 503 1074 HOH   HOH A . 
E 4 HOH   204 504 772  HOH   HOH A . 
E 4 HOH   205 505 1292 HOH   HOH A . 
E 4 HOH   206 506 346  HOH   HOH A . 
E 4 HOH   207 507 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 205  HOH   HOH B . 
F 4 HOH   3   203 240  HOH   HOH B . 
F 4 HOH   4   204 549  HOH   HOH B . 
F 4 HOH   5   205 531  HOH   HOH B . 
F 4 HOH   6   206 232  HOH   HOH B . 
F 4 HOH   7   207 900  HOH   HOH B . 
F 4 HOH   8   208 358  HOH   HOH B . 
F 4 HOH   9   209 50   HOH   HOH B . 
F 4 HOH   10  210 120  HOH   HOH B . 
F 4 HOH   11  211 398  HOH   HOH B . 
F 4 HOH   12  212 364  HOH   HOH B . 
F 4 HOH   13  213 353  HOH   HOH B . 
F 4 HOH   14  214 1249 HOH   HOH B . 
F 4 HOH   15  215 452  HOH   HOH B . 
F 4 HOH   16  216 1278 HOH   HOH B . 
F 4 HOH   17  217 1140 HOH   HOH B . 
F 4 HOH   18  218 758  HOH   HOH B . 
F 4 HOH   19  219 743  HOH   HOH B . 
F 4 HOH   20  220 332  HOH   HOH B . 
F 4 HOH   21  221 264  HOH   HOH B . 
F 4 HOH   22  222 82   HOH   HOH B . 
F 4 HOH   23  223 15   HOH   HOH B . 
F 4 HOH   24  224 75   HOH   HOH B . 
F 4 HOH   25  225 172  HOH   HOH B . 
F 4 HOH   26  226 69   HOH   HOH B . 
F 4 HOH   27  227 343  HOH   HOH B . 
F 4 HOH   28  228 131  HOH   HOH B . 
F 4 HOH   29  229 300  HOH   HOH B . 
F 4 HOH   30  230 444  HOH   HOH B . 
F 4 HOH   31  231 54   HOH   HOH B . 
F 4 HOH   32  232 391  HOH   HOH B . 
F 4 HOH   33  233 654  HOH   HOH B . 
F 4 HOH   34  234 1312 HOH   HOH B . 
F 4 HOH   35  235 325  HOH   HOH B . 
F 4 HOH   36  236 60   HOH   HOH B . 
F 4 HOH   37  237 52   HOH   HOH B . 
F 4 HOH   38  238 272  HOH   HOH B . 
F 4 HOH   39  239 1    HOH   HOH B . 
F 4 HOH   40  240 110  HOH   HOH B . 
F 4 HOH   41  241 127  HOH   HOH B . 
F 4 HOH   42  242 128  HOH   HOH B . 
F 4 HOH   43  243 144  HOH   HOH B . 
F 4 HOH   44  244 133  HOH   HOH B . 
F 4 HOH   45  245 129  HOH   HOH B . 
F 4 HOH   46  246 14   HOH   HOH B . 
F 4 HOH   47  247 30   HOH   HOH B . 
F 4 HOH   48  248 9    HOH   HOH B . 
F 4 HOH   49  249 41   HOH   HOH B . 
F 4 HOH   50  250 723  HOH   HOH B . 
F 4 HOH   51  251 150  HOH   HOH B . 
F 4 HOH   52  252 143  HOH   HOH B . 
F 4 HOH   53  253 287  HOH   HOH B . 
F 4 HOH   54  254 181  HOH   HOH B . 
F 4 HOH   55  255 243  HOH   HOH B . 
F 4 HOH   56  256 276  HOH   HOH B . 
F 4 HOH   57  257 416  HOH   HOH B . 
F 4 HOH   58  258 31   HOH   HOH B . 
F 4 HOH   59  259 166  HOH   HOH B . 
F 4 HOH   60  260 47   HOH   HOH B . 
F 4 HOH   61  261 271  HOH   HOH B . 
F 4 HOH   62  262 10   HOH   HOH B . 
F 4 HOH   63  263 221  HOH   HOH B . 
F 4 HOH   64  264 231  HOH   HOH B . 
F 4 HOH   65  265 1277 HOH   HOH B . 
F 4 HOH   66  266 252  HOH   HOH B . 
F 4 HOH   67  267 242  HOH   HOH B . 
F 4 HOH   68  268 20   HOH   HOH B . 
F 4 HOH   69  269 117  HOH   HOH B . 
F 4 HOH   70  270 347  HOH   HOH B . 
F 4 HOH   71  271 72   HOH   HOH B . 
F 4 HOH   72  272 59   HOH   HOH B . 
F 4 HOH   73  273 103  HOH   HOH B . 
F 4 HOH   74  274 77   HOH   HOH B . 
F 4 HOH   75  275 11   HOH   HOH B . 
F 4 HOH   76  276 1305 HOH   HOH B . 
F 4 HOH   77  277 282  HOH   HOH B . 
F 4 HOH   78  278 175  HOH   HOH B . 
F 4 HOH   79  279 84   HOH   HOH B . 
F 4 HOH   80  280 220  HOH   HOH B . 
F 4 HOH   81  281 22   HOH   HOH B . 
F 4 HOH   82  282 43   HOH   HOH B . 
F 4 HOH   83  283 114  HOH   HOH B . 
F 4 HOH   84  284 61   HOH   HOH B . 
F 4 HOH   85  285 207  HOH   HOH B . 
F 4 HOH   86  286 302  HOH   HOH B . 
F 4 HOH   87  287 147  HOH   HOH B . 
F 4 HOH   88  288 88   HOH   HOH B . 
F 4 HOH   89  289 235  HOH   HOH B . 
F 4 HOH   90  290 106  HOH   HOH B . 
F 4 HOH   91  291 1106 HOH   HOH B . 
F 4 HOH   92  292 89   HOH   HOH B . 
F 4 HOH   93  293 13   HOH   HOH B . 
F 4 HOH   94  294 99   HOH   HOH B . 
F 4 HOH   95  295 1066 HOH   HOH B . 
F 4 HOH   96  296 216  HOH   HOH B . 
F 4 HOH   97  297 1285 HOH   HOH B . 
F 4 HOH   98  298 160  HOH   HOH B . 
F 4 HOH   99  299 137  HOH   HOH B . 
F 4 HOH   100 300 311  HOH   HOH B . 
F 4 HOH   101 301 170  HOH   HOH B . 
F 4 HOH   102 302 299  HOH   HOH B . 
F 4 HOH   103 303 215  HOH   HOH B . 
F 4 HOH   104 304 112  HOH   HOH B . 
F 4 HOH   105 305 316  HOH   HOH B . 
F 4 HOH   106 306 635  HOH   HOH B . 
F 4 HOH   107 307 37   HOH   HOH B . 
F 4 HOH   108 308 142  HOH   HOH B . 
F 4 HOH   109 309 118  HOH   HOH B . 
F 4 HOH   110 310 32   HOH   HOH B . 
F 4 HOH   111 311 387  HOH   HOH B . 
F 4 HOH   112 312 23   HOH   HOH B . 
F 4 HOH   113 313 197  HOH   HOH B . 
F 4 HOH   114 314 38   HOH   HOH B . 
F 4 HOH   115 315 101  HOH   HOH B . 
F 4 HOH   116 316 1274 HOH   HOH B . 
F 4 HOH   117 317 177  HOH   HOH B . 
F 4 HOH   118 318 297  HOH   HOH B . 
F 4 HOH   119 319 1294 HOH   HOH B . 
F 4 HOH   120 320 960  HOH   HOH B . 
F 4 HOH   121 321 28   HOH   HOH B . 
F 4 HOH   122 322 44   HOH   HOH B . 
F 4 HOH   123 323 182  HOH   HOH B . 
F 4 HOH   124 324 48   HOH   HOH B . 
F 4 HOH   125 325 100  HOH   HOH B . 
F 4 HOH   126 326 91   HOH   HOH B . 
F 4 HOH   127 327 29   HOH   HOH B . 
F 4 HOH   128 328 98   HOH   HOH B . 
F 4 HOH   129 329 161  HOH   HOH B . 
F 4 HOH   130 330 55   HOH   HOH B . 
F 4 HOH   131 331 341  HOH   HOH B . 
F 4 HOH   132 332 1291 HOH   HOH B . 
F 4 HOH   133 333 334  HOH   HOH B . 
F 4 HOH   134 334 717  HOH   HOH B . 
F 4 HOH   135 335 141  HOH   HOH B . 
F 4 HOH   136 336 704  HOH   HOH B . 
F 4 HOH   137 337 65   HOH   HOH B . 
F 4 HOH   138 338 445  HOH   HOH B . 
F 4 HOH   139 339 178  HOH   HOH B . 
F 4 HOH   140 340 234  HOH   HOH B . 
F 4 HOH   141 341 1293 HOH   HOH B . 
F 4 HOH   142 342 1126 HOH   HOH B . 
F 4 HOH   143 343 619  HOH   HOH B . 
F 4 HOH   144 344 87   HOH   HOH B . 
F 4 HOH   145 345 362  HOH   HOH B . 
F 4 HOH   146 346 90   HOH   HOH B . 
F 4 HOH   147 347 1304 HOH   HOH B . 
F 4 HOH   148 348 1280 HOH   HOH B . 
F 4 HOH   149 349 191  HOH   HOH B . 
F 4 HOH   150 350 463  HOH   HOH B . 
F 4 HOH   151 351 339  HOH   HOH B . 
F 4 HOH   152 352 623  HOH   HOH B . 
F 4 HOH   153 353 335  HOH   HOH B . 
F 4 HOH   154 354 1046 HOH   HOH B . 
F 4 HOH   155 355 1077 HOH   HOH B . 
F 4 HOH   156 356 304  HOH   HOH B . 
F 4 HOH   157 357 203  HOH   HOH B . 
F 4 HOH   158 358 290  HOH   HOH B . 
F 4 HOH   159 359 541  HOH   HOH B . 
F 4 HOH   160 360 718  HOH   HOH B . 
F 4 HOH   161 361 389  HOH   HOH B . 
F 4 HOH   162 362 283  HOH   HOH B . 
F 4 HOH   163 363 1072 HOH   HOH B . 
F 4 HOH   164 364 291  HOH   HOH B . 
F 4 HOH   165 365 479  HOH   HOH B . 
F 4 HOH   166 366 615  HOH   HOH B . 
F 4 HOH   167 367 340  HOH   HOH B . 
F 4 HOH   168 368 1316 HOH   HOH B . 
F 4 HOH   169 369 898  HOH   HOH B . 
F 4 HOH   170 370 373  HOH   HOH B . 
F 4 HOH   171 371 1303 HOH   HOH B . 
F 4 HOH   172 372 667  HOH   HOH B . 
F 4 HOH   173 373 310  HOH   HOH B . 
F 4 HOH   174 374 431  HOH   HOH B . 
F 4 HOH   175 375 190  HOH   HOH B . 
F 4 HOH   176 376 1173 HOH   HOH B . 
F 4 HOH   177 377 183  HOH   HOH B . 
F 4 HOH   178 378 1000 HOH   HOH B . 
F 4 HOH   179 379 418  HOH   HOH B . 
F 4 HOH   180 380 149  HOH   HOH B . 
F 4 HOH   181 381 1163 HOH   HOH B . 
F 4 HOH   182 382 1311 HOH   HOH B . 
F 4 HOH   183 383 424  HOH   HOH B . 
F 4 HOH   184 384 176  HOH   HOH B . 
F 4 HOH   185 385 491  HOH   HOH B . 
F 4 HOH   186 386 981  HOH   HOH B . 
F 4 HOH   187 387 1298 HOH   HOH B . 
F 4 HOH   188 388 248  HOH   HOH B . 
F 4 HOH   189 389 470  HOH   HOH B . 
F 4 HOH   190 390 265  HOH   HOH B . 
F 4 HOH   191 391 350  HOH   HOH B . 
F 4 HOH   192 392 184  HOH   HOH B . 
F 4 HOH   193 393 360  HOH   HOH B . 
F 4 HOH   194 394 410  HOH   HOH B . 
F 4 HOH   195 395 355  HOH   HOH B . 
F 4 HOH   196 396 274  HOH   HOH B . 
F 4 HOH   197 397 566  HOH   HOH B . 
F 4 HOH   198 398 157  HOH   HOH B . 
F 4 HOH   199 399 314  HOH   HOH B . 
F 4 HOH   200 400 792  HOH   HOH B . 
F 4 HOH   201 401 321  HOH   HOH B . 
F 4 HOH   202 402 558  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           7HES 
_cell.length_a           88.779 
_cell.length_b           88.779 
_cell.length_c           39.423 
_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                         7HES 
_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          7HES 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.53 
_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                     7HES 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.390 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   155708 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.053 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.300 
_reflns.B_iso_Wilson_estimate        13.350 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.058 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     996569 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.020 1.040  ? 40310 7290 ? 2.465 ? ? ? 5.500 ? 0.500  ? ? ? ? ? ? 94.900 2.723 1.133 0.314 
1 2 5.590 44.390 ? 7099  1035 ? 0.026 ? ? ? 6.900 ? 47.800 ? ? ? ? ? ? 99.800 0.028 0.011 0.999 
# 
_refine.entry_id                                 7HES 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.3900 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4500 
_refine.ls_number_reflns_obs                     155267 
_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                          0.1536 
_refine.ls_R_factor_R_work                       0.1528 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1699 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  7506 
_refine.ls_number_reflns_R_work                  147761 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.7429 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1500 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                82.540 
_refine.B_iso_min                                9.510 
_refine.pdbx_overall_phase_error                 21.7200 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0200 
_refine_hist.d_res_low                        44.3900 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             409 
_refine_hist.number_atoms_total               2991 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           15.70 
_refine_hist.pdbx_B_iso_mean_solvent          32.55 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0200 1.0300  30 87.0000  4321 . 0.4866 0.4784 . 179 0.0000 4500 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 99.0000  4855 . 0.4244 0.3994 . 285 0.0000 5140 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4890 . 0.3759 0.3967 . 288 0.0000 5178 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4903 . 0.3419 0.3634 . 275 0.0000 5178 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4932 . 0.3241 0.3474 . 231 0.0000 5163 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4934 . 0.3080 0.3112 . 235 0.0000 5169 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4915 . 0.2779 0.3028 . 265 0.0000 5180 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 4944 . 0.2517 0.2822 . 224 0.0000 5168 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4900 . 0.2334 0.2560 . 238 0.0000 5138 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4945 . 0.2099 0.2388 . 256 0.0000 5201 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4925 . 0.1897 0.2227 . 253 0.0000 5178 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4911 . 0.1690 0.2047 . 266 0.0000 5177 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5025 . 0.1547 0.1878 . 213 0.0000 5238 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4885 . 0.1538 0.1719 . 243 0.0000 5128 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4917 . 0.1445 0.1622 . 257 0.0000 5174 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4932 . 0.1423 0.1557 . 270 0.0000 5202 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4945 . 0.1423 0.1750 . 247 0.0000 5192 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4928 . 0.1368 0.1558 . 258 0.0000 5186 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4953 . 0.1354 0.1820 . 239 0.0000 5192 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4975 . 0.1310 0.1456 . 244 0.0000 5219 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4947 . 0.1237 0.1358 . 244 0.0000 5191 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 4934 . 0.1211 0.1433 . 256 0.0000 5190 . 'X-RAY DIFFRACTION' 
1.5900 1.6600  30 100.0000 4934 . 0.1229 0.1421 . 268 0.0000 5202 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5022 . 0.1326 0.1549 . 200 0.0000 5222 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4955 . 0.1324 0.1518 . 290 0.0000 5245 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4950 . 0.1367 0.1360 . 242 0.0000 5192 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4944 . 0.1358 0.1459 . 289 0.0000 5233 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 4978 . 0.1361 0.1437 . 252 0.0000 5230 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5006 . 0.1494 0.1668 . 249 0.0000 5255 . 'X-RAY DIFFRACTION' 
3.1700 44.3900 30 100.0000 5156 . 0.1506 0.1751 . 250 0.0000 5406 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HES 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003692' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HES 
_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 7HES A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HES 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 7HES SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HES MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HES SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HES MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O 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                   7HES 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    205 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    313 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86 ? ? 56.13 -132.45 
2 1 HIS B 86 ? ? 56.30 -126.97 
# 
_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 505 ? 5.82 . 
2 1 O ? A HOH 506 ? 6.10 . 
3 1 O ? A HOH 507 ? 7.69 . 
4 1 O ? B HOH 402 ? 6.54 . 
# 
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 
A1A98 N2   N Y N 1   
A1A98 C3   C Y N 2   
A1A98 C6   C Y N 3   
A1A98 C9   C N N 4   
A1A98 C12  C N N 5   
A1A98 C1   C N N 6   
A1A98 C10  C N N 7   
A1A98 C11  C N N 8   
A1A98 C2   C N N 9   
A1A98 C4   C Y N 10  
A1A98 C5   C Y N 11  
A1A98 C7   C Y N 12  
A1A98 C8   C Y N 13  
A1A98 N1   N N N 14  
A1A98 N3   N Y N 15  
A1A98 N4   N Y N 16  
A1A98 O1   O N N 17  
A1A98 H10  H N N 18  
A1A98 H9   H N N 19  
A1A98 H16  H N N 20  
A1A98 H15  H N N 21  
A1A98 H2   H N N 22  
A1A98 H3   H N N 23  
A1A98 H11  H N N 24  
A1A98 H12  H N N 25  
A1A98 H13  H N N 26  
A1A98 H14  H N N 27  
A1A98 H5   H N N 28  
A1A98 H6   H N N 29  
A1A98 H7   H N N 30  
A1A98 H4   H N N 31  
A1A98 H8   H N N 32  
A1A98 H1   H N N 33  
ALA   N    N N N 34  
ALA   CA   C N S 35  
ALA   C    C N N 36  
ALA   O    O N N 37  
ALA   CB   C N N 38  
ALA   OXT  O N N 39  
ALA   H    H N N 40  
ALA   H2   H N N 41  
ALA   HA   H N N 42  
ALA   HB1  H N N 43  
ALA   HB2  H N N 44  
ALA   HB3  H N N 45  
ALA   HXT  H N N 46  
ARG   N    N N N 47  
ARG   CA   C N S 48  
ARG   C    C N N 49  
ARG   O    O N N 50  
ARG   CB   C N N 51  
ARG   CG   C N N 52  
ARG   CD   C N N 53  
ARG   NE   N N N 54  
ARG   CZ   C N N 55  
ARG   NH1  N N N 56  
ARG   NH2  N N N 57  
ARG   OXT  O N N 58  
ARG   H    H N N 59  
ARG   H2   H N N 60  
ARG   HA   H N N 61  
ARG   HB2  H N N 62  
ARG   HB3  H N N 63  
ARG   HG2  H N N 64  
ARG   HG3  H N N 65  
ARG   HD2  H N N 66  
ARG   HD3  H N N 67  
ARG   HE   H N N 68  
ARG   HH11 H N N 69  
ARG   HH12 H N N 70  
ARG   HH21 H N N 71  
ARG   HH22 H N N 72  
ARG   HXT  H N N 73  
ASN   N    N N N 74  
ASN   CA   C N S 75  
ASN   C    C N N 76  
ASN   O    O N N 77  
ASN   CB   C N N 78  
ASN   CG   C N N 79  
ASN   OD1  O N N 80  
ASN   ND2  N N N 81  
ASN   OXT  O N N 82  
ASN   H    H N N 83  
ASN   H2   H N N 84  
ASN   HA   H N N 85  
ASN   HB2  H N N 86  
ASN   HB3  H N N 87  
ASN   HD21 H N N 88  
ASN   HD22 H N N 89  
ASN   HXT  H N N 90  
ASP   N    N N N 91  
ASP   CA   C N S 92  
ASP   C    C N N 93  
ASP   O    O N N 94  
ASP   CB   C N N 95  
ASP   CG   C N N 96  
ASP   OD1  O N N 97  
ASP   OD2  O N N 98  
ASP   OXT  O N N 99  
ASP   H    H N N 100 
ASP   H2   H N N 101 
ASP   HA   H N N 102 
ASP   HB2  H N N 103 
ASP   HB3  H N N 104 
ASP   HD2  H N N 105 
ASP   HXT  H 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 
TFA   C1   C N N 337 
TFA   C2   C N N 338 
TFA   O    O N N 339 
TFA   F1   F N N 340 
TFA   F2   F N N 341 
TFA   F3   F N N 342 
TFA   OXT  O N N 343 
TFA   HXT  H N N 344 
THR   N    N N N 345 
THR   CA   C N S 346 
THR   C    C N N 347 
THR   O    O N N 348 
THR   CB   C N R 349 
THR   OG1  O N N 350 
THR   CG2  C N N 351 
THR   OXT  O N N 352 
THR   H    H N N 353 
THR   H2   H N N 354 
THR   HA   H N N 355 
THR   HB   H N N 356 
THR   HG1  H N N 357 
THR   HG21 H N N 358 
THR   HG22 H N N 359 
THR   HG23 H N N 360 
THR   HXT  H N N 361 
TYR   N    N N N 362 
TYR   CA   C N S 363 
TYR   C    C N N 364 
TYR   O    O N N 365 
TYR   CB   C N N 366 
TYR   CG   C Y N 367 
TYR   CD1  C Y N 368 
TYR   CD2  C Y N 369 
TYR   CE1  C Y N 370 
TYR   CE2  C Y N 371 
TYR   CZ   C Y N 372 
TYR   OH   O N N 373 
TYR   OXT  O N N 374 
TYR   H    H N N 375 
TYR   H2   H N N 376 
TYR   HA   H N N 377 
TYR   HB2  H N N 378 
TYR   HB3  H N N 379 
TYR   HD1  H N N 380 
TYR   HD2  H N N 381 
TYR   HE1  H N N 382 
TYR   HE2  H N N 383 
TYR   HH   H N N 384 
TYR   HXT  H N N 385 
VAL   N    N N N 386 
VAL   CA   C N S 387 
VAL   C    C N N 388 
VAL   O    O N N 389 
VAL   CB   C N N 390 
VAL   CG1  C N N 391 
VAL   CG2  C N N 392 
VAL   OXT  O N N 393 
VAL   H    H N N 394 
VAL   H2   H N N 395 
VAL   HA   H N N 396 
VAL   HB   H N N 397 
VAL   HG11 H N N 398 
VAL   HG12 H N N 399 
VAL   HG13 H N N 400 
VAL   HG21 H N N 401 
VAL   HG22 H N N 402 
VAL   HG23 H N N 403 
VAL   HXT  H N N 404 
# 
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 
A1A98 C10 C9   sing N N 1   
A1A98 C10 C11  sing N N 2   
A1A98 C9  C2   sing N N 3   
A1A98 C11 C12  sing N N 4   
A1A98 C2  C1   sing N N 5   
A1A98 C2  C12  sing N N 6   
A1A98 C2  N1   sing N N 7   
A1A98 C1  O1   sing N N 8   
A1A98 N1  C3   sing N N 9   
A1A98 C3  C6   doub Y N 10  
A1A98 C3  N2   sing Y N 11  
A1A98 C7  C6   sing Y N 12  
A1A98 C7  C8   doub Y N 13  
A1A98 C6  C5   sing Y N 14  
A1A98 N2  C4   doub Y N 15  
A1A98 C8  N4   sing Y N 16  
A1A98 C5  N4   sing Y N 17  
A1A98 C5  N3   doub Y N 18  
A1A98 C4  N3   sing Y N 19  
A1A98 C9  H10  sing N N 20  
A1A98 C9  H9   sing N N 21  
A1A98 C12 H16  sing N N 22  
A1A98 C12 H15  sing N N 23  
A1A98 C1  H2   sing N N 24  
A1A98 C1  H3   sing N N 25  
A1A98 C10 H11  sing N N 26  
A1A98 C10 H12  sing N N 27  
A1A98 C11 H13  sing N N 28  
A1A98 C11 H14  sing N N 29  
A1A98 C4  H5   sing N N 30  
A1A98 C7  H6   sing N N 31  
A1A98 C8  H7   sing N N 32  
A1A98 N1  H4   sing N N 33  
A1A98 N4  H8   sing N N 34  
A1A98 O1  H1   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
GLN   N   CA   sing N N 118 
GLN   N   H    sing N N 119 
GLN   N   H2   sing N N 120 
GLN   CA  C    sing N N 121 
GLN   CA  CB   sing N N 122 
GLN   CA  HA   sing N N 123 
GLN   C   O    doub N N 124 
GLN   C   OXT  sing N N 125 
GLN   CB  CG   sing N N 126 
GLN   CB  HB2  sing N N 127 
GLN   CB  HB3  sing N N 128 
GLN   CG  CD   sing N N 129 
GLN   CG  HG2  sing N N 130 
GLN   CG  HG3  sing N N 131 
GLN   CD  OE1  doub N N 132 
GLN   CD  NE2  sing N N 133 
GLN   NE2 HE21 sing N N 134 
GLN   NE2 HE22 sing N N 135 
GLN   OXT HXT  sing N N 136 
GLU   N   CA   sing N N 137 
GLU   N   H    sing N N 138 
GLU   N   H2   sing N N 139 
GLU   CA  C    sing N N 140 
GLU   CA  CB   sing N N 141 
GLU   CA  HA   sing N N 142 
GLU   C   O    doub N N 143 
GLU   C   OXT  sing N N 144 
GLU   CB  CG   sing N N 145 
GLU   CB  HB2  sing N N 146 
GLU   CB  HB3  sing N N 147 
GLU   CG  CD   sing N N 148 
GLU   CG  HG2  sing N N 149 
GLU   CG  HG3  sing N N 150 
GLU   CD  OE1  doub N N 151 
GLU   CD  OE2  sing N N 152 
GLU   OE2 HE2  sing N N 153 
GLU   OXT HXT  sing N N 154 
GLY   N   CA   sing N N 155 
GLY   N   H    sing N N 156 
GLY   N   H2   sing N N 157 
GLY   CA  C    sing N N 158 
GLY   CA  HA2  sing N N 159 
GLY   CA  HA3  sing N N 160 
GLY   C   O    doub N N 161 
GLY   C   OXT  sing N N 162 
GLY   OXT HXT  sing N N 163 
HIS   N   CA   sing N N 164 
HIS   N   H    sing N N 165 
HIS   N   H2   sing N N 166 
HIS   CA  C    sing N N 167 
HIS   CA  CB   sing N N 168 
HIS   CA  HA   sing N N 169 
HIS   C   O    doub N N 170 
HIS   C   OXT  sing N N 171 
HIS   CB  CG   sing N N 172 
HIS   CB  HB2  sing N N 173 
HIS   CB  HB3  sing N N 174 
HIS   CG  ND1  sing Y N 175 
HIS   CG  CD2  doub Y N 176 
HIS   ND1 CE1  doub Y N 177 
HIS   ND1 HD1  sing N N 178 
HIS   CD2 NE2  sing Y N 179 
HIS   CD2 HD2  sing N N 180 
HIS   CE1 NE2  sing Y N 181 
HIS   CE1 HE1  sing N N 182 
HIS   NE2 HE2  sing N N 183 
HIS   OXT HXT  sing N N 184 
HOH   O   H1   sing N N 185 
HOH   O   H2   sing N N 186 
ILE   N   CA   sing N N 187 
ILE   N   H    sing N N 188 
ILE   N   H2   sing N N 189 
ILE   CA  C    sing N N 190 
ILE   CA  CB   sing N N 191 
ILE   CA  HA   sing N N 192 
ILE   C   O    doub N N 193 
ILE   C   OXT  sing N N 194 
ILE   CB  CG1  sing N N 195 
ILE   CB  CG2  sing N N 196 
ILE   CB  HB   sing N N 197 
ILE   CG1 CD1  sing N N 198 
ILE   CG1 HG12 sing N N 199 
ILE   CG1 HG13 sing N N 200 
ILE   CG2 HG21 sing N N 201 
ILE   CG2 HG22 sing N N 202 
ILE   CG2 HG23 sing N N 203 
ILE   CD1 HD11 sing N N 204 
ILE   CD1 HD12 sing N N 205 
ILE   CD1 HD13 sing N N 206 
ILE   OXT HXT  sing N N 207 
LEU   N   CA   sing N N 208 
LEU   N   H    sing N N 209 
LEU   N   H2   sing N N 210 
LEU   CA  C    sing N N 211 
LEU   CA  CB   sing N N 212 
LEU   CA  HA   sing N N 213 
LEU   C   O    doub N N 214 
LEU   C   OXT  sing N N 215 
LEU   CB  CG   sing N N 216 
LEU   CB  HB2  sing N N 217 
LEU   CB  HB3  sing N N 218 
LEU   CG  CD1  sing N N 219 
LEU   CG  CD2  sing N N 220 
LEU   CG  HG   sing N N 221 
LEU   CD1 HD11 sing N N 222 
LEU   CD1 HD12 sing N N 223 
LEU   CD1 HD13 sing N N 224 
LEU   CD2 HD21 sing N N 225 
LEU   CD2 HD22 sing N N 226 
LEU   CD2 HD23 sing N N 227 
LEU   OXT HXT  sing N N 228 
LYS   N   CA   sing N N 229 
LYS   N   H    sing N N 230 
LYS   N   H2   sing N N 231 
LYS   CA  C    sing N N 232 
LYS   CA  CB   sing N N 233 
LYS   CA  HA   sing N N 234 
LYS   C   O    doub N N 235 
LYS   C   OXT  sing N N 236 
LYS   CB  CG   sing N N 237 
LYS   CB  HB2  sing N N 238 
LYS   CB  HB3  sing N N 239 
LYS   CG  CD   sing N N 240 
LYS   CG  HG2  sing N N 241 
LYS   CG  HG3  sing N N 242 
LYS   CD  CE   sing N N 243 
LYS   CD  HD2  sing N N 244 
LYS   CD  HD3  sing N N 245 
LYS   CE  NZ   sing N N 246 
LYS   CE  HE2  sing N N 247 
LYS   CE  HE3  sing N N 248 
LYS   NZ  HZ1  sing N N 249 
LYS   NZ  HZ2  sing N N 250 
LYS   NZ  HZ3  sing N N 251 
LYS   OXT HXT  sing N N 252 
MET   N   CA   sing N N 253 
MET   N   H    sing N N 254 
MET   N   H2   sing N N 255 
MET   CA  C    sing N N 256 
MET   CA  CB   sing N N 257 
MET   CA  HA   sing N N 258 
MET   C   O    doub N N 259 
MET   C   OXT  sing N N 260 
MET   CB  CG   sing N N 261 
MET   CB  HB2  sing N N 262 
MET   CB  HB3  sing N N 263 
MET   CG  SD   sing N N 264 
MET   CG  HG2  sing N N 265 
MET   CG  HG3  sing N N 266 
MET   SD  CE   sing N N 267 
MET   CE  HE1  sing N N 268 
MET   CE  HE2  sing N N 269 
MET   CE  HE3  sing N N 270 
MET   OXT HXT  sing N N 271 
PHE   N   CA   sing N N 272 
PHE   N   H    sing N N 273 
PHE   N   H2   sing N N 274 
PHE   CA  C    sing N N 275 
PHE   CA  CB   sing N N 276 
PHE   CA  HA   sing N N 277 
PHE   C   O    doub N N 278 
PHE   C   OXT  sing N N 279 
PHE   CB  CG   sing N N 280 
PHE   CB  HB2  sing N N 281 
PHE   CB  HB3  sing N N 282 
PHE   CG  CD1  doub Y N 283 
PHE   CG  CD2  sing Y N 284 
PHE   CD1 CE1  sing Y N 285 
PHE   CD1 HD1  sing N N 286 
PHE   CD2 CE2  doub Y N 287 
PHE   CD2 HD2  sing N N 288 
PHE   CE1 CZ   doub Y N 289 
PHE   CE1 HE1  sing N N 290 
PHE   CE2 CZ   sing Y N 291 
PHE   CE2 HE2  sing N N 292 
PHE   CZ  HZ   sing N N 293 
PHE   OXT HXT  sing N N 294 
PRO   N   CA   sing N N 295 
PRO   N   CD   sing N N 296 
PRO   N   H    sing N N 297 
PRO   CA  C    sing N N 298 
PRO   CA  CB   sing N N 299 
PRO   CA  HA   sing N N 300 
PRO   C   O    doub N N 301 
PRO   C   OXT  sing N N 302 
PRO   CB  CG   sing N N 303 
PRO   CB  HB2  sing N N 304 
PRO   CB  HB3  sing N N 305 
PRO   CG  CD   sing N N 306 
PRO   CG  HG2  sing N N 307 
PRO   CG  HG3  sing N N 308 
PRO   CD  HD2  sing N N 309 
PRO   CD  HD3  sing N N 310 
PRO   OXT HXT  sing N N 311 
SER   N   CA   sing N N 312 
SER   N   H    sing N N 313 
SER   N   H2   sing N N 314 
SER   CA  C    sing N N 315 
SER   CA  CB   sing N N 316 
SER   CA  HA   sing N N 317 
SER   C   O    doub N N 318 
SER   C   OXT  sing N N 319 
SER   CB  OG   sing N N 320 
SER   CB  HB2  sing N N 321 
SER   CB  HB3  sing N N 322 
SER   OG  HG   sing N N 323 
SER   OXT HXT  sing N N 324 
TFA   C1  C2   sing N N 325 
TFA   C1  O    doub N N 326 
TFA   C1  OXT  sing N N 327 
TFA   C2  F1   sing N N 328 
TFA   C2  F2   sing N N 329 
TFA   C2  F3   sing N N 330 
TFA   OXT HXT  sing N N 331 
THR   N   CA   sing N N 332 
THR   N   H    sing N N 333 
THR   N   H2   sing N N 334 
THR   CA  C    sing N N 335 
THR   CA  CB   sing N N 336 
THR   CA  HA   sing N N 337 
THR   C   O    doub N N 338 
THR   C   OXT  sing N N 339 
THR   CB  OG1  sing N N 340 
THR   CB  CG2  sing N N 341 
THR   CB  HB   sing N N 342 
THR   OG1 HG1  sing N N 343 
THR   CG2 HG21 sing N N 344 
THR   CG2 HG22 sing N N 345 
THR   CG2 HG23 sing N N 346 
THR   OXT HXT  sing N N 347 
TYR   N   CA   sing N N 348 
TYR   N   H    sing N N 349 
TYR   N   H2   sing N N 350 
TYR   CA  C    sing N N 351 
TYR   CA  CB   sing N N 352 
TYR   CA  HA   sing N N 353 
TYR   C   O    doub N N 354 
TYR   C   OXT  sing N N 355 
TYR   CB  CG   sing N N 356 
TYR   CB  HB2  sing N N 357 
TYR   CB  HB3  sing N N 358 
TYR   CG  CD1  doub Y N 359 
TYR   CG  CD2  sing Y N 360 
TYR   CD1 CE1  sing Y N 361 
TYR   CD1 HD1  sing N N 362 
TYR   CD2 CE2  doub Y N 363 
TYR   CD2 HD2  sing N N 364 
TYR   CE1 CZ   doub Y N 365 
TYR   CE1 HE1  sing N N 366 
TYR   CE2 CZ   sing Y N 367 
TYR   CE2 HE2  sing N N 368 
TYR   CZ  OH   sing N N 369 
TYR   OH  HH   sing N N 370 
TYR   OXT HXT  sing N N 371 
VAL   N   CA   sing N N 372 
VAL   N   H    sing N N 373 
VAL   N   H2   sing N N 374 
VAL   CA  C    sing N N 375 
VAL   CA  CB   sing N N 376 
VAL   CA  HA   sing N N 377 
VAL   C   O    doub N N 378 
VAL   C   OXT  sing N N 379 
VAL   CB  CG1  sing N N 380 
VAL   CB  CG2  sing N N 381 
VAL   CB  HB   sing N N 382 
VAL   CG1 HG11 sing N N 383 
VAL   CG1 HG12 sing N N 384 
VAL   CG1 HG13 sing N N 385 
VAL   CG2 HG21 sing N N 386 
VAL   CG2 HG22 sing N N 387 
VAL   CG2 HG23 sing N N 388 
VAL   OXT HXT  sing N N 389 
# 
_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                    7HES 
_atom_sites.fract_transf_matrix[1][1]   0.011264 
_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]   0.011264 
_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]   0.025366 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
F 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.636 -16.123 22.253  0.80 62.97 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.558 -15.855 22.420  0.20 58.61 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.658 -15.054 22.417  0.80 62.49 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.543 -14.821 22.579  0.20 58.17 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.306 -13.700 22.135  0.80 60.49 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.153 -13.445 22.335  0.20 56.17 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.416 -13.428 22.591  0.80 61.33 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.167 -13.094 22.937  0.20 56.64 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.016 -15.092 23.822  0.80 63.55 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.882 -14.897 23.969  0.20 59.32 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.993 -13.974 23.974  0.80 63.79 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.798 -13.837 24.099  0.20 59.64 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.369 -16.448 24.080  0.80 63.86 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.311 -16.288 24.214  0.20 59.69 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.949 -15.183 21.771  0.80 74.99 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.850 -14.959 21.919  0.20 69.80 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.705 -14.960 24.492  0.80 76.26 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.552 -14.728 24.649  0.20 71.18 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.481 -14.123 24.785  0.80 76.55 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.285 -14.009 24.904  0.20 71.56 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.457 -13.125 24.029  0.80 76.55 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.214 -12.963 24.153  0.20 71.56 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.402 -13.982 23.205  0.80 76.55 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.218 -13.883 23.323  0.20 71.56 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.916 -16.424 24.939  0.80 76.63 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.825 -16.285 25.054  0.20 71.63 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.729 -16.631 23.375  0.80 76.63 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.712 -16.515 23.486  0.20 71.63 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.057 -17.131 24.089  0.80 76.63 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.039 -16.927 24.255  0.20 71.63 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.609 -12.858 21.372  0.80 57.10 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.533 -12.670 21.450  0.20 53.36 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.046 -11.495 21.087  0.80 53.20 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 18.979 -11.318 21.133  0.20 50.25 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.886 -10.532 21.329  0.80 49.69 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.854 -10.322 21.409  0.20 47.38 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.793 -10.931 21.744  0.80 49.54 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.770 -10.684 21.872  0.20 47.45 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.635 -11.363 19.675  0.80 52.41 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.498 -11.221 19.694  0.20 49.82 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.673 -11.799 18.592  0.80 51.52 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.487 -11.692 18.672  0.20 49.36 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.516 -11.379 18.565  0.80 51.24 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.306 -11.354 18.744  0.20 49.25 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.149 -12.650 17.689  0.80 51.30 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.951 -12.479 17.707  0.20 49.24 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.862 -13.064 21.003  0.80 68.52 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.830 -12.914 21.016  0.20 64.03 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.747 -11.264 21.708  0.80 63.84 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.717 -11.099 21.712  0.20 60.30 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.869 -10.434 19.513  0.80 62.89 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.719 -10.294 19.499  0.20 59.78 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.428 -11.918 19.611  0.80 62.89 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.290 -11.772 19.605  0.20 59.78 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.646 -12.929 17.051  0.80 61.55 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.420 -12.770 17.098  0.20 59.09 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.965 -12.922 17.744  0.80 61.55 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.784 -12.696 17.693  0.20 59.09 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.131 -9.248  21.062  0.80 46.12 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.126 -9.050  21.117  0.20 44.33 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.231 -8.174  21.461  0.80 42.48 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.227 -7.957  21.465  0.20 41.17 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.392 -7.629  20.305  0.80 37.78 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.319 -7.535  20.316  0.20 37.49 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.807 -6.547  20.430  0.80 37.79 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.613 -6.529  20.440  0.20 37.42 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.017 -7.047  22.135  0.80 43.82 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 18.019 -6.756  21.988  0.20 41.75 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 18.975 -6.487  21.253  0.80 44.46 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.894 -6.247  20.999  0.20 42.00 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.825 -8.976  20.636  0.80 55.35 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.835 -8.796  20.704  0.20 53.19 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.619 -8.525  22.125  0.80 50.98 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.653 -8.254  22.185  0.20 49.40 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.401 -6.351  22.409  0.80 52.59 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.395 -6.060  22.252  0.20 50.10 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.476 -7.405  22.913  0.80 52.59 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.544 -7.035  22.755  0.20 50.10 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.401 -5.873  21.643  0.80 53.35 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.313 -5.584  21.302  0.20 50.40 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.315 -8.350  19.190  0.80 32.74 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.319 -8.268  19.207  0.20 33.83 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.427 -7.961  18.100  0.80 27.87 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.324 -8.029  18.174  0.20 30.16 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 13.988 -8.322  18.449  0.80 27.18 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 13.954 -8.459  18.685  0.20 28.55 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.714 -9.421  18.934  0.80 28.43 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.828 -9.413  19.457  0.20 28.96 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 15.833 -8.666  16.808  0.80 25.08 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.659 -8.821  16.911  0.20 28.36 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.121 -8.154  16.219  0.80 23.02 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 16.962 -8.430  16.269  0.20 26.83 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.145 -6.982  15.485  0.80 21.96 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.035 -7.343  15.413  0.20 26.06 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.301 -8.851  16.396  0.80 23.20 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.111 -9.162  16.509  0.20 26.26 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.327 -6.507  14.939  0.80 21.76 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.232 -6.989  14.817  0.20 25.70 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.484 -8.387  15.852  0.80 23.03 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.310 -8.815  15.918  0.20 25.87 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.499 -7.209  15.123  0.80 22.18 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.371 -7.727  15.071  0.20 25.64 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 16.761 -9.070  19.046  0.80 39.29 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.870 -8.904  19.032  0.20 40.59 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.472 -7.011  17.969  0.80 33.44 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.293 -7.086  17.957  0.20 36.19 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 15.942 -9.616  16.992  0.80 30.10 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.713 -9.761  17.139  0.20 34.03 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.130 -8.542  16.153  0.80 30.10 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 14.953 -8.686  16.261  0.20 34.03 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.357 -6.503  15.359  0.80 26.35 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.271 -6.843  15.238  0.20 31.28 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.300 -9.642  16.887  0.80 27.85 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.074 -9.894  17.078  0.20 31.51 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.333 -5.714  14.448  0.80 26.11 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.271 -6.256  14.246  0.20 30.84 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.276 -8.860  15.980  0.80 27.63 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.076 -9.315  16.091  0.20 31.04 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.294 -6.892  14.758  0.80 26.61 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.178 -7.493  14.672  0.20 30.77 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.065 -7.394  18.192  0.80 25.46 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 12.919 -7.741  18.257  0.20 26.57 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.686 -7.511  18.656  0.80 25.27 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.572 -8.052  18.711  0.20 24.54 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.699 -7.273  17.520  0.80 22.57 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.570 -7.577  17.672  0.20 22.35 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 10.931 -6.435  16.646  0.80 22.68 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.700 -6.477  17.130  0.20 22.25 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.420 -6.496  19.776  0.80 27.51 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.280 -7.401  20.068  0.20 24.73 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.079 -6.572  20.222  0.80 29.42 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.380 -8.187  20.829  0.20 25.07 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.221 -6.683  17.741  0.80 30.55 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 12.969 -7.079  17.704  0.20 31.89 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.536 -8.401  19.009  0.80 30.32 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.478 -9.011  18.805  0.20 29.44 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.015 -6.687  20.520  0.80 33.01 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.112 -7.310  20.558  0.20 29.67 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.590 -5.604  19.438  0.80 33.01 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 10.882 -6.529  19.923  0.20 29.67 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 9.951  -6.015  20.837  0.80 35.30 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 9.658  -8.285  20.414  0.20 30.09 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.588  -8.009  17.543  0.80 20.56 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.574  -8.415  17.402  0.20 20.33 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.509  -7.776  16.605  0.80 19.39 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.559  -8.106  16.420  0.20 18.60 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.736  -8.279  15.199  0.80 17.57 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.810  -8.662  15.037  0.20 16.93 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.015  -7.866  14.285  0.80 17.94 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.134  -8.240  14.091  0.20 17.04 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.443  -8.642  18.101  0.80 24.67 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.465  -9.182  17.784  0.20 24.39 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.709  -8.199  16.951  0.80 23.27 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.711  -8.444  16.738  0.20 22.32 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.343  -6.821  16.556  0.80 23.27 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.481  -7.144  16.341  0.20 22.32 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.712  -9.157  14.988  0.80 16.92 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.747  -9.595  14.887  0.20 15.41 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 9.987  -9.690  13.663  0.80 15.81 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.129 -10.102 13.577  0.20 14.31 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.145  -10.930 13.403  0.80 14.55 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.303  -11.322 13.194  0.20 13.50 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.902  -11.738 14.302  0.80 16.20 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 8.990  -12.169 14.035  0.20 12.75 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.470 -10.055 13.513  0.80 16.32 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.619 -10.453 13.546  0.20 13.93 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.381 -8.859  13.332  0.80 16.38 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.513 -9.241  13.406  0.20 13.56 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.691 -8.044  14.406  0.80 17.57 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.835 -8.460  14.507  0.20 13.73 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 12.895 -8.534  12.087  0.80 16.44 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 13.027 -8.873  12.170  0.20 13.69 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.494 -6.936  14.250  0.80 18.48 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.645 -7.345  14.381  0.20 14.12 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.702 -7.426  11.918  0.80 16.87 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.834 -7.763  12.034  0.20 13.82 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.003 -6.633  13.002  0.80 18.22 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 14.144 -7.005  13.141  0.20 14.35 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 14.795 -5.527  12.830  0.80 19.22 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.951 -5.901  13.000  0.20 14.99 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.235 -9.454  15.602  0.80 20.30 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.183 -9.948  15.538  0.20 18.49 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.765  -9.021  12.995  0.80 18.98 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.970  -9.416  12.917  0.20 17.18 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.750 -10.544 14.303  0.80 19.59 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 11.857 -10.910 14.368  0.20 16.71 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.551 -10.620 12.729  0.80 19.59 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.782 -11.034 12.788  0.20 16.71 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.338 -8.253  15.249  0.80 21.08 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.496 -8.686  15.345  0.20 16.48 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.687 -9.069  11.353  0.80 19.73 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.824 -9.383  11.420  0.20 16.42 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.695 -6.406  14.984  0.80 22.18 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.853 -6.828  15.127  0.20 16.94 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.046 -7.220  11.080  0.80 20.25 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.177 -7.531  11.200  0.20 16.58 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 14.907 -5.141  13.568  0.80 23.06 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 15.184 -5.813  12.196  0.20 17.99 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.688  -11.055 12.164  0.80 14.04 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.960  -11.401 11.911  0.20 13.71 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.100  -12.289 11.676  0.80 14.12 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.277  -12.557 11.346  0.20 13.57 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.227  -13.228 11.254  0.80 13.62 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.322  -13.537 10.826  0.20 12.89 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.180 -12.812 10.589  0.80 13.06 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.268 -13.138 10.140  0.20 12.80 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.192  -11.975 10.487  0.80 15.09 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.376  -12.105 10.198  0.20 14.84 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.557  -13.165 9.765   0.80 17.13 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.017  -12.785 10.045  0.20 16.27 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.509  -13.803 10.651  0.80 19.15 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.148  -11.971 9.106   0.20 16.70 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 5.956  -12.735 8.429   0.80 19.30 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 6.169  -14.201 9.528   0.20 16.87 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.709  -10.423 11.575  0.80 16.85 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 9.115  -10.782 11.335  0.20 16.45 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.566  -12.705 12.383  0.80 16.94 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.737  -12.993 12.023  0.20 16.29 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.464  -11.407 10.799  0.80 18.11 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 7.209  -11.158 10.307  0.20 17.81 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.714  -11.487 9.834   0.80 18.11 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.855  -12.251 9.368   0.20 17.81 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.240  -13.826 9.589   0.80 20.56 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 5.575  -12.819 10.909  0.20 19.53 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.146  -14.583 10.200  0.80 22.97 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 4.256  -12.350 9.090   0.20 20.05 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 5.916  -14.068 11.491  0.80 22.97 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 5.113  -11.055 9.423   0.20 20.05 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.799  -13.161 10.819  0.80 22.97 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 5.536  -11.997 8.218   0.20 20.05 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.564  -13.513 8.001   0.80 23.15 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 5.289  -14.593 9.418   0.20 20.24 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.276  -12.065 8.590   0.80 23.15 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 6.628  -14.174 8.673   0.20 20.24 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.660  -12.370 7.873   0.80 23.15 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 6.686  -14.714 10.166  0.20 20.24 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.129  -14.488 11.662  0.80 13.81 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.147  -14.815 11.154  0.20 12.50 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.120 -15.491 11.302  0.80 13.92 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.119 -15.851 10.821  0.20 13.08 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.761  -16.057 9.936   0.80 13.85 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.797  -16.419 9.443   0.20 13.40 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.646  -16.557 9.745   0.80 15.67 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.790  -17.111 9.272   0.20 13.98 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.144 -16.596 12.355  0.80 13.75 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.061 -16.950 11.876  0.20 13.66 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.201 -17.681 12.160  0.80 14.30 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.107 -18.026 11.735  0.20 13.97 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.272 -18.569 13.402  0.80 14.70 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.098 -18.905 12.972  0.20 14.44 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.249 -19.733 13.250  0.80 15.52 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.142 -19.990 12.884  0.20 14.75 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.654 -19.274 13.051  0.80 15.91 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.491 -19.423 12.623  0.20 14.63 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.485  -14.789 12.149  0.80 16.57 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.464  -15.112 11.588  0.20 15.00 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 10.996 -15.076 11.254  0.80 16.70 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.012 -15.471 10.806  0.20 15.70 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.304 -16.191 13.220  0.80 16.50 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.172 -16.549 12.750  0.20 16.39 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.280  -17.035 12.356  0.80 16.50 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.192  -17.381 11.824  0.20 16.39 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 10.967 -18.235 11.399  0.80 17.17 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 10.909 -18.579 10.960  0.20 16.77 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.071 -17.271 12.029  0.80 17.17 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 11.981 -17.617 11.646  0.20 16.77 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.557 -18.039 14.162  0.80 17.64 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.287 -18.361 13.753  0.20 17.33 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.390 -18.945 13.577  0.80 17.64 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.227 -19.324 13.059  0.20 17.33 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.225 -20.285 14.051  0.80 18.62 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.171 -20.479 13.721  0.20 17.70 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 11.997 -20.267 12.478  0.80 18.62 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 11.914 -20.582 12.153  0.20 17.70 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.178 -19.969 12.846  0.80 19.10 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.103 -20.065 12.671  0.20 17.56 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.693 -18.683 12.389  0.80 19.10 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.517 -19.058 11.811  0.20 17.56 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 13.962 -18.898 13.796  0.80 19.10 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.679 -18.797 13.228  0.20 17.56 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.691 -15.974 8.984   0.80 13.52 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.661 -16.148 8.463   0.20 13.08 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.466 -16.540 7.658   0.80 13.76 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.438 -16.674 7.120   0.20 13.05 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.043 -17.939 7.515   0.80 13.59 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.028 -18.067 6.926   0.20 12.77 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.408 -18.813 6.917   0.80 14.32 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.386 -18.928 6.314   0.20 12.22 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.062 -15.640 6.570   0.80 15.38 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.007 -15.716 6.071   0.20 13.27 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.404 -14.277 6.343   0.80 16.24 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.303 -14.356 6.016   0.20 13.76 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.091 -13.552 5.197   0.80 17.28 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.067 -13.360 5.160   0.20 13.87 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 8.910  -14.434 6.069   0.80 17.07 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 8.876  -14.518 5.505   0.20 14.28 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.476 -15.611 9.083   0.80 16.23 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.374 -15.666 8.551   0.20 15.69 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.514  -16.602 7.505   0.80 16.51 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.482  -16.735 6.975   0.20 15.66 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 11.993 -15.468 6.795   0.80 18.46 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 11.944 -15.559 6.269   0.20 15.93 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.025 -16.118 5.727   0.80 18.46 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 10.923 -16.133 5.198   0.20 15.93 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.504 -13.741 7.144   0.80 19.49 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.255 -13.998 6.914   0.20 16.51 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.664 -12.690 5.065   0.80 20.74 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.594 -12.512 5.166   0.20 16.64 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.028 -13.423 5.421   0.80 20.74 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 11.957 -13.244 5.528   0.20 16.64 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.016 -14.085 4.390   0.80 20.74 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 11.125 -13.700 4.254   0.20 16.64 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.555  -13.586 5.759   0.80 20.49 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.506  -13.641 5.325   0.20 17.14 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 8.783  -15.114 5.387   0.80 20.49 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.889  -15.046 4.692   0.20 17.14 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.462  -14.701 6.887   0.80 20.49 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.346  -14.968 6.183   0.20 17.14 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.241 -18.156 8.046   0.80 13.10 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.242 -18.301 7.420   0.20 13.04 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 12.942 -19.426 7.957   0.80 13.46 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 12.889 -19.606 7.343   0.20 13.18 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.685 -19.637 9.265   0.80 14.05 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.650 -19.830 8.646   0.20 12.89 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.570 -18.850 10.211  0.80 14.41 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.474 -19.100 9.626   0.20 12.87 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 13.930 -19.454 6.784   0.80 14.41 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 13.833 -19.693 6.136   0.20 13.35 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 14.972 -18.514 7.038   0.80 14.23 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 14.928 -18.787 6.323   0.20 13.61 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.262 -19.112 5.458   0.80 15.56 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.110 -19.350 4.846   0.20 13.34 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.696 -17.550 8.463   0.80 15.72 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.721 -17.705 7.812   0.20 15.65 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.305 -20.144 7.844   0.80 16.15 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.211 -20.300 7.253   0.20 15.82 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.322 -20.337 6.712   0.80 17.29 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.170 -20.600 6.064   0.20 16.02 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.629 -18.885 7.408   0.80 17.07 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.457 -18.834 5.673   0.20 16.33 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 13.901 -19.210 4.729   0.80 18.67 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 13.601 -19.710 4.091   0.20 16.01 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.518 -19.713 5.301   0.80 18.67 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.221 -19.733 4.855   0.20 16.01 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 12.938 -18.201 5.469   0.80 18.67 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 13.040 -18.387 4.751   0.20 16.01 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.484 -20.702 9.299   0.80 14.77 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.522 -20.842 8.651   0.20 13.34 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.326 -20.970 10.451  0.80 15.88 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.289 -21.150 9.855   0.20 13.19 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.130 -19.739 10.862  0.80 14.78 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.232 -20.015 10.242  0.20 11.58 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.324 -19.486 12.057  0.80 15.82 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.575 -19.874 11.423  0.20 12.12 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.277 -22.118 10.120  0.80 19.04 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.068 -22.452 9.653   0.20 15.53 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.228 -22.407 11.247  0.80 23.23 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.098 -22.687 10.733  0.20 17.47 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 16.762 -22.886 12.306  0.80 24.88 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 16.731 -22.626 11.925  0.20 18.28 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.429 -22.139 11.073  0.80 25.27 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.269 -22.948 10.392  0.20 18.38 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.566 -21.264 8.662   0.80 17.73 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.679 -21.362 7.983   0.20 16.01 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 14.772 -21.243 11.201  0.80 19.06 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 14.677 -21.291 10.593  0.20 15.82 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.751 -22.919 9.931   0.80 22.84 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 15.454 -23.201 9.686   0.20 18.64 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 16.797 -21.883 9.331   0.80 22.84 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 16.517 -22.425 8.795   0.20 18.64 ?  14  ASP   A HB3  1 
ATOM   371  N N    A ASN   A 1 15  ? 16.620 -18.963 9.891   0.80 13.76 ?  15  ASN   A N    1 
ATOM   372  N N    B ASN   A 1 15  ? 16.661 -19.192 9.277   0.20 10.47 ?  15  ASN   A N    1 
ATOM   373  C CA   A ASN   A 1 15  ? 17.597 -17.920 10.176  0.80 13.98 ?  15  ASN   A CA   1 
ATOM   374  C CA   B ASN   A 1 15  ? 17.659 -18.162 9.543   0.20 10.50 ?  15  ASN   A CA   1 
ATOM   375  C C    A ASN   A 1 15  ? 17.236 -16.532 9.663   0.80 13.80 ?  15  ASN   A C    1 
ATOM   376  C C    B ASN   A 1 15  ? 17.303 -16.776 9.011   0.20 10.70 ?  15  ASN   A C    1 
ATOM   377  O O    A ASN   A 1 15  ? 17.994 -15.599 9.929   0.80 14.55 ?  15  ASN   A O    1 
ATOM   378  O O    B ASN   A 1 15  ? 18.128 -15.865 9.132   0.20 11.22 ?  15  ASN   A O    1 
ATOM   379  C CB   A ASN   A 1 15  ? 18.977 -18.310 9.614   0.80 13.97 ?  15  ASN   A CB   1 
ATOM   380  C CB   B ASN   A 1 15  ? 19.032 -18.583 8.986   0.20 9.92  ?  15  ASN   A CB   1 
ATOM   381  C CG   A ASN   A 1 15  ? 18.976 -18.439 8.103   0.80 14.37 ?  15  ASN   A CG   1 
ATOM   382  C CG   B ASN   A 1 15  ? 19.050 -18.647 7.469   0.20 10.42 ?  15  ASN   A CG   1 
ATOM   383  O OD1  A ASN   A 1 15  ? 18.262 -19.267 7.537   0.80 15.39 ?  15  ASN   A OD1  1 
ATOM   384  O OD1  B ASN   A 1 15  ? 18.367 -19.471 6.862   0.20 10.36 ?  15  ASN   A OD1  1 
ATOM   385  N ND2  A ASN   A 1 15  ? 19.766 -17.600 7.439   0.80 14.38 ?  15  ASN   A ND2  1 
ATOM   386  N ND2  B ASN   A 1 15  ? 19.843 -17.780 6.850   0.20 11.07 ?  15  ASN   A ND2  1 
ATOM   387  H H    A ASN   A 1 15  ? 16.398 -19.019 9.075   0.80 16.51 ?  15  ASN   A H    1 
ATOM   388  H H    B ASN   A 1 15  ? 16.386 -19.219 8.462   0.20 12.56 ?  15  ASN   A H    1 
ATOM   389  H HA   A ASN   A 1 15  ? 17.698 -17.844 11.142  0.80 16.77 ?  15  ASN   A HA   1 
ATOM   390  H HA   B ASN   A 1 15  ? 17.766 -18.087 10.501  0.20 12.60 ?  15  ASN   A HA   1 
ATOM   391  H HB2  A ASN   A 1 15  ? 19.625 -17.619 9.865   0.80 16.76 ?  15  ASN   A HB2  1 
ATOM   392  H HB2  B ASN   A 1 15  ? 19.703 -17.935 9.268   0.20 11.91 ?  15  ASN   A HB2  1 
ATOM   393  H HB3  A ASN   A 1 15  ? 19.246 -19.158 9.996   0.80 16.76 ?  15  ASN   A HB3  1 
ATOM   394  H HB3  B ASN   A 1 15  ? 19.266 -19.463 9.329   0.20 11.91 ?  15  ASN   A HB3  1 
ATOM   395  H HD21 A ASN   A 1 15  ? 19.803 -17.630 6.579   0.80 17.25 ?  15  ASN   A HD21 1 
ATOM   396  H HD21 B ASN   A 1 15  ? 19.890 -17.781 5.990   0.20 13.28 ?  15  ASN   A HD21 1 
ATOM   397  H HD22 A ASN   A 1 15  ? 20.251 -17.021 7.863   0.80 17.25 ?  15  ASN   A HD22 1 
ATOM   398  H HD22 B ASN   A 1 15  ? 20.309 -17.215 7.303   0.20 13.28 ?  15  ASN   A HD22 1 
ATOM   399  N N    A VAL   A 1 16  ? 16.122 -16.358 8.954   0.80 13.89 ?  16  VAL   A N    1 
ATOM   400  N N    B VAL   A 1 16  ? 16.116 -16.585 8.439   0.20 10.64 ?  16  VAL   A N    1 
ATOM   401  C CA   A VAL   A 1 16  ? 15.746 -15.070 8.380   0.80 14.10 ?  16  VAL   A CA   1 
ATOM   402  C CA   B VAL   A 1 16  ? 15.714 -15.311 7.849   0.20 10.68 ?  16  VAL   A CA   1 
ATOM   403  C C    A VAL   A 1 16  ? 14.460 -14.574 9.031   0.80 14.22 ?  16  VAL   A C    1 
ATOM   404  C C    B VAL   A 1 16  ? 14.470 -14.790 8.567   0.20 10.81 ?  16  VAL   A C    1 
ATOM   405  O O    A VAL   A 1 16  ? 13.464 -15.308 9.109   0.80 14.20 ?  16  VAL   A O    1 
ATOM   406  O O    B VAL   A 1 16  ? 13.474 -15.511 8.702   0.20 10.65 ?  16  VAL   A O    1 
ATOM   407  C CB   A VAL   A 1 16  ? 15.596 -15.136 6.850   0.80 14.35 ?  16  VAL   A CB   1 
ATOM   408  C CB   B VAL   A 1 16  ? 15.456 -15.449 6.337   0.20 10.66 ?  16  VAL   A CB   1 
ATOM   409  C CG1  A VAL   A 1 16  ? 15.199 -13.760 6.297   0.80 15.05 ?  16  VAL   A CG1  1 
ATOM   410  C CG1  B VAL   A 1 16  ? 15.000 -14.121 5.757   0.20 10.86 ?  16  VAL   A CG1  1 
ATOM   411  C CG2  A VAL   A 1 16  ? 16.878 -15.633 6.205   0.80 15.36 ?  16  VAL   A CG2  1 
ATOM   412  C CG2  B VAL   A 1 16  ? 16.705 -15.945 5.622   0.20 10.30 ?  16  VAL   A CG2  1 
ATOM   413  H H    A VAL   A 1 16  ? 15.561 -16.984 8.790   0.80 16.67 ?  16  VAL   A H    1 
ATOM   414  H H    B VAL   A 1 16  ? 15.525 -17.202 8.373   0.20 12.77 ?  16  VAL   A H    1 
ATOM   415  H HA   A VAL   A 1 16  ? 16.440 -14.423 8.579   0.80 16.92 ?  16  VAL   A HA   1 
ATOM   416  H HA   B VAL   A 1 16  ? 16.430 -14.667 7.971   0.20 12.82 ?  16  VAL   A HA   1 
ATOM   417  H HB   A VAL   A 1 16  ? 14.886 -15.759 6.637   0.80 17.22 ?  16  VAL   A HB   1 
ATOM   418  H HB   B VAL   A 1 16  ? 14.753 -16.104 6.194   0.20 12.79 ?  16  VAL   A HB   1 
ATOM   419  H HG11 A VAL   A 1 16  ? 15.278 -13.777 5.332   0.80 18.05 ?  16  VAL   A HG11 1 
ATOM   420  H HG11 B VAL   A 1 16  ? 14.999 -14.182 4.791   0.20 13.03 ?  16  VAL   A HG11 1 
ATOM   421  H HG12 A VAL   A 1 16  ? 14.280 -13.568 6.547   0.80 18.05 ?  16  VAL   A HG12 1 
ATOM   422  H HG12 B VAL   A 1 16  ? 14.107 -13.928 6.077   0.20 13.03 ?  16  VAL   A HG12 1 
ATOM   423  H HG13 A VAL   A 1 16  ? 15.790 -13.087 6.667   0.80 18.05 ?  16  VAL   A HG13 1 
ATOM   424  H HG13 B VAL   A 1 16  ? 15.616 -13.429 6.045   0.20 13.03 ?  16  VAL   A HG13 1 
ATOM   425  H HG21 A VAL   A 1 16  ? 16.874 -15.388 5.268   0.80 18.43 ?  16  VAL   A HG21 1 
ATOM   426  H HG21 B VAL   A 1 16  ? 16.773 -15.504 4.763   0.20 12.36 ?  16  VAL   A HG21 1 
ATOM   427  H HG22 A VAL   A 1 16  ? 17.634 -15.229 6.654   0.80 18.43 ?  16  VAL   A HG22 1 
ATOM   428  H HG22 B VAL   A 1 16  ? 17.481 -15.734 6.163   0.20 12.36 ?  16  VAL   A HG22 1 
ATOM   429  H HG23 A VAL   A 1 16  ? 16.918 -16.598 6.298   0.80 18.43 ?  16  VAL   A HG23 1 
ATOM   430  H HG23 B VAL   A 1 16  ? 16.641 -16.907 5.502   0.20 12.36 ?  16  VAL   A HG23 1 
ATOM   431  N N    A TYR   A 1 17  ? 14.485 -13.310 9.451   0.80 13.60 ?  17  TYR   A N    1 
ATOM   432  N N    B TYR   A 1 17  ? 14.526 -13.526 8.996   0.20 11.15 ?  17  TYR   A N    1 
ATOM   433  C CA   A TYR   A 1 17  ? 13.393 -12.625 10.124  0.80 13.42 ?  17  TYR   A CA   1 
ATOM   434  C CA   B TYR   A 1 17  ? 13.457 -12.836 9.714   0.20 11.80 ?  17  TYR   A CA   1 
ATOM   435  C C    A TYR   A 1 17  ? 13.126 -11.319 9.389   0.80 13.79 ?  17  TYR   A C    1 
ATOM   436  C C    B TYR   A 1 17  ? 13.190 -11.482 9.049   0.20 12.31 ?  17  TYR   A C    1 
ATOM   437  O O    A TYR   A 1 17  ? 14.048 -10.736 8.813   0.80 13.07 ?  17  TYR   A O    1 
ATOM   438  O O    B TYR   A 1 17  ? 13.952 -11.041 8.184   0.20 11.97 ?  17  TYR   A O    1 
ATOM   439  C CB   A TYR   A 1 17  ? 13.788 -12.338 11.573  0.80 14.45 ?  17  TYR   A CB   1 
ATOM   440  C CB   B TYR   A 1 17  ? 13.841 -12.635 11.188  0.20 12.06 ?  17  TYR   A CB   1 
ATOM   441  C CG   A TYR   A 1 17  ? 13.963 -13.603 12.381  0.80 15.40 ?  17  TYR   A CG   1 
ATOM   442  C CG   B TYR   A 1 17  ? 14.095 -13.917 11.962  0.20 12.76 ?  17  TYR   A CG   1 
ATOM   443  C CD1  A TYR   A 1 17  ? 15.132 -14.355 12.301  0.80 16.79 ?  17  TYR   A CD1  1 
ATOM   444  C CD1  B TYR   A 1 17  ? 15.304 -14.596 11.851  0.20 13.35 ?  17  TYR   A CD1  1 
ATOM   445  C CD2  A TYR   A 1 17  ? 12.948 -14.060 13.208  0.80 15.46 ?  17  TYR   A CD2  1 
ATOM   446  C CD2  B TYR   A 1 17  ? 13.132 -14.441 12.817  0.20 12.88 ?  17  TYR   A CD2  1 
ATOM   447  C CE1  A TYR   A 1 17  ? 15.285 -15.530 13.033  0.80 17.27 ?  17  TYR   A CE1  1 
ATOM   448  C CE1  B TYR   A 1 17  ? 15.540 -15.765 12.560  0.20 13.43 ?  17  TYR   A CE1  1 
ATOM   449  C CE2  A TYR   A 1 17  ? 13.087 -15.236 13.942  0.80 16.78 ?  17  TYR   A CE2  1 
ATOM   450  C CE2  B TYR   A 1 17  ? 13.360 -15.610 13.530  0.20 13.03 ?  17  TYR   A CE2  1 
ATOM   451  C CZ   A TYR   A 1 17  ? 14.259 -15.964 13.855  0.80 16.83 ?  17  TYR   A CZ   1 
ATOM   452  C CZ   B TYR   A 1 17  ? 14.568 -16.265 13.398  0.20 13.25 ?  17  TYR   A CZ   1 
ATOM   453  O OH   A TYR   A 1 17  ? 14.400 -17.129 14.585  0.80 18.01 ?  17  TYR   A OH   1 
ATOM   454  O OH   B TYR   A 1 17  ? 14.805 -17.426 14.103  0.20 13.33 ?  17  TYR   A OH   1 
ATOM   455  H H    A TYR   A 1 17  ? 15.171 -12.786 9.335   0.80 16.33 ?  17  TYR   A H    1 
ATOM   456  H H    B TYR   A 1 17  ? 15.218 -13.035 8.877   0.20 13.38 ?  17  TYR   A H    1 
ATOM   457  H HA   A TYR   A 1 17  ? 12.593 -13.169 10.106  0.80 16.11 ?  17  TYR   A HA   1 
ATOM   458  H HA   B TYR   A 1 17  ? 12.649 -13.372 9.675   0.20 14.16 ?  17  TYR   A HA   1 
ATOM   459  H HB2  A TYR   A 1 17  ? 14.627 -11.851 11.580  0.80 17.34 ?  17  TYR   A HB2  1 
ATOM   460  H HB2  B TYR   A 1 17  ? 14.651 -12.106 11.229  0.20 14.47 ?  17  TYR   A HB2  1 
ATOM   461  H HB3  A TYR   A 1 17  ? 13.094 -11.807 11.989  0.80 17.34 ?  17  TYR   A HB3  1 
ATOM   462  H HB3  B TYR   A 1 17  ? 13.120 -12.169 11.629  0.20 14.47 ?  17  TYR   A HB3  1 
ATOM   463  H HD1  A TYR   A 1 17  ? 15.825 -14.067 11.745  0.80 20.15 ?  17  TYR   A HD1  1 
ATOM   464  H HD1  B TYR   A 1 17  ? 15.965 -14.266 11.289  0.20 16.02 ?  17  TYR   A HD1  1 
ATOM   465  H HD2  A TYR   A 1 17  ? 12.156 -13.574 13.269  0.80 18.55 ?  17  TYR   A HD2  1 
ATOM   466  H HD2  B TYR   A 1 17  ? 12.315 -14.005 12.909  0.20 15.45 ?  17  TYR   A HD2  1 
ATOM   467  H HE1  A TYR   A 1 17  ? 16.076 -16.022 12.969  0.80 20.73 ?  17  TYR   A HE1  1 
ATOM   468  H HE1  B TYR   A 1 17  ? 16.353 -16.211 12.474  0.20 16.11 ?  17  TYR   A HE1  1 
ATOM   469  H HE2  A TYR   A 1 17  ? 12.396 -15.522 14.494  0.80 20.14 ?  17  TYR   A HE2  1 
ATOM   470  H HE2  B TYR   A 1 17  ? 12.701 -15.951 14.097  0.20 15.64 ?  17  TYR   A HE2  1 
ATOM   471  H HH   A TYR   A 1 17  ? 13.654 -17.378 14.873  0.80 21.61 ?  17  TYR   A HH   1 
ATOM   472  H HH   B TYR   A 1 17  ? 15.574 -17.717 13.926  0.20 15.99 ?  17  TYR   A HH   1 
ATOM   473  N N    A ILE   A 1 18  ? 11.867 -10.853 9.395   0.80 14.10 ?  18  ILE   A N    1 
ATOM   474  N N    B ILE   A 1 18  ? 12.112 -10.801 9.456   0.20 13.10 ?  18  ILE   A N    1 
ATOM   475  C CA   A ILE   A 1 18  ? 11.490 -9.676  8.617   0.80 13.77 ?  18  ILE   A CA   1 
ATOM   476  C CA   B ILE   A 1 18  ? 11.695 -9.563  8.786   0.20 13.12 ?  18  ILE   A CA   1 
ATOM   477  C C    A ILE   A 1 18  ? 10.516 -8.802  9.398   0.80 14.30 ?  18  ILE   A C    1 
ATOM   478  C C    B ILE   A 1 18  ? 10.802 -8.729  9.702   0.20 13.08 ?  18  ILE   A C    1 
ATOM   479  O O    A ILE   A 1 18  ? 9.680  -9.298  10.156  0.80 14.09 ?  18  ILE   A O    1 
ATOM   480  O O    B ILE   A 1 18  ? 10.081 -9.265  10.545  0.20 13.55 ?  18  ILE   A O    1 
ATOM   481  C CB   A ILE   A 1 18  ? 10.952 -10.085 7.225   0.80 13.78 ?  18  ILE   A CB   1 
ATOM   482  C CB   B ILE   A 1 18  ? 10.991 -9.879  7.441   0.20 12.93 ?  18  ILE   A CB   1 
ATOM   483  C CG1  A ILE   A 1 18  ? 10.939 -8.895  6.266   0.80 14.50 ?  18  ILE   A CG1  1 
ATOM   484  C CG1  B ILE   A 1 18  ? 10.816 -8.606  6.608   0.20 13.45 ?  18  ILE   A CG1  1 
ATOM   485  C CG2  A ILE   A 1 18  ? 9.597  -10.778 7.335   0.80 14.53 ?  18  ILE   A CG2  1 
ATOM   486  C CG2  B ILE   A 1 18  ? 9.647  -10.555 7.683   0.20 13.32 ?  18  ILE   A CG2  1 
ATOM   487  C CD1  A ILE   A 1 18  ? 10.712 -9.294  4.840   0.80 15.59 ?  18  ILE   A CD1  1 
ATOM   488  C CD1  B ILE   A 1 18  ? 10.307 -8.868  5.210   0.20 14.09 ?  18  ILE   A CD1  1 
ATOM   489  H H    A ILE   A 1 18  ? 11.222 -11.209 9.835   0.80 16.92 ?  18  ILE   A H    1 
ATOM   490  H H    B ILE   A 1 18  ? 11.615 -11.041 10.112  0.20 15.72 ?  18  ILE   A H    1 
ATOM   491  H HA   A ILE   A 1 18  ? 12.293 -9.147  8.462   0.80 16.52 ?  18  ILE   A HA   1 
ATOM   492  H HA   B ILE   A 1 18  ? 12.486 -9.040  8.589   0.20 15.74 ?  18  ILE   A HA   1 
ATOM   493  H HB   A ILE   A 1 18  ? 11.577 -10.733 6.860   0.80 16.54 ?  18  ILE   A HB   1 
ATOM   494  H HB   B ILE   A 1 18  ? 11.553 -10.490 6.946   0.20 15.51 ?  18  ILE   A HB   1 
ATOM   495  H HG12 A ILE   A 1 18  ? 10.237 -8.286  6.521   0.80 17.40 ?  18  ILE   A HG12 1 
ATOM   496  H HG12 B ILE   A 1 18  ? 10.182 -8.022  7.050   0.20 16.14 ?  18  ILE   A HG12 1 
ATOM   497  H HG13 A ILE   A 1 18  ? 11.803 -8.444  6.307   0.80 17.40 ?  18  ILE   A HG13 1 
ATOM   498  H HG13 B ILE   A 1 18  ? 11.676 -8.160  6.531   0.20 16.14 ?  18  ILE   A HG13 1 
ATOM   499  H HG21 A ILE   A 1 18  ? 9.368  -11.159 6.471   0.80 17.44 ?  18  ILE   A HG21 1 
ATOM   500  H HG21 B ILE   A 1 18  ? 9.325  -10.923 6.845   0.20 15.98 ?  18  ILE   A HG21 1 
ATOM   501  H HG22 A ILE   A 1 18  ? 9.657  -11.480 8.000   0.80 17.44 ?  18  ILE   A HG22 1 
ATOM   502  H HG22 B ILE   A 1 18  ? 9.763  -11.266 8.332   0.20 15.98 ?  18  ILE   A HG22 1 
ATOM   503  H HG23 A ILE   A 1 18  ? 8.929  -10.127 7.597   0.80 17.44 ?  18  ILE   A HG23 1 
ATOM   504  H HG23 B ILE   A 1 18  ? 9.015  -9.900  8.021   0.20 15.98 ?  18  ILE   A HG23 1 
ATOM   505  H HD11 A ILE   A 1 18  ? 10.786 -8.507  4.276   0.80 18.70 ?  18  ILE   A HD11 1 
ATOM   506  H HD11 B ILE   A 1 18  ? 10.306 -8.036  4.712   0.20 16.91 ?  18  ILE   A HD11 1 
ATOM   507  H HD12 A ILE   A 1 18  ? 11.377 -9.950  4.583   0.80 18.70 ?  18  ILE   A HD12 1 
ATOM   508  H HD12 B ILE   A 1 18  ? 10.890 -9.513  4.778   0.20 16.91 ?  18  ILE   A HD12 1 
ATOM   509  H HD13 A ILE   A 1 18  ? 9.823  -9.674  4.760   0.80 18.70 ?  18  ILE   A HD13 1 
ATOM   510  H HD13 B ILE   A 1 18  ? 9.406  -9.223  5.264   0.20 16.91 ?  18  ILE   A HD13 1 
ATOM   511  N N    A LYS   A 1 19  ? 10.637 -7.484  9.210   0.80 14.95 ?  19  LYS   A N    1 
ATOM   512  N N    B LYS   A 1 19  ? 10.833 -7.402  9.502   0.20 12.86 ?  19  LYS   A N    1 
ATOM   513  C CA   A LYS   A 1 19  ? 9.825  -6.511  9.929   0.80 15.56 ?  19  LYS   A CA   1 
ATOM   514  C CA   B LYS   A 1 19  ? 10.001 -6.449  10.237  0.20 13.89 ?  19  LYS   A CA   1 
ATOM   515  C C    A LYS   A 1 19  ? 9.646  -5.271  9.067   0.80 15.01 ?  19  LYS   A C    1 
ATOM   516  C C    B LYS   A 1 19  ? 9.795  -5.186  9.400   0.20 13.50 ?  19  LYS   A C    1 
ATOM   517  O O    A LYS   A 1 19  ? 10.541 -4.899  8.306   0.80 14.91 ?  19  LYS   A O    1 
ATOM   518  O O    B LYS   A 1 19  ? 10.718 -4.733  8.721   0.20 13.13 ?  19  LYS   A O    1 
ATOM   519  C CB   A LYS   A 1 19  ? 10.535 -6.110  11.229  0.80 16.47 ?  19  LYS   A CB   1 
ATOM   520  C CB   B LYS   A 1 19  ? 10.639 -6.083  11.588  0.20 14.75 ?  19  LYS   A CB   1 
ATOM   521  C CG   A LYS   A 1 19  ? 9.772  -5.194  12.172  0.80 18.40 ?  19  LYS   A CG   1 
ATOM   522  C CG   B LYS   A 1 19  ? 9.827  -5.111  12.437  0.20 15.62 ?  19  LYS   A CG   1 
ATOM   523  C CD   A LYS   A 1 19  ? 10.635 -4.943  13.403  0.80 20.46 ?  19  LYS   A CD   1 
ATOM   524  C CD   B LYS   A 1 19  ? 10.593 -4.690  13.684  0.20 16.49 ?  19  LYS   A CD   1 
ATOM   525  C CE   A LYS   A 1 19  ? 9.998  -4.007  14.412  0.80 22.09 ?  19  LYS   A CE   1 
ATOM   526  C CE   B LYS   A 1 19  ? 9.787  -3.718  14.533  0.20 17.08 ?  19  LYS   A CE   1 
ATOM   527  N NZ   A LYS   A 1 19  ? 10.929 -3.785  15.558  0.80 22.41 ?  19  LYS   A NZ   1 
ATOM   528  N NZ   B LYS   A 1 19  ? 10.555 -3.248  15.718  0.20 17.31 ?  19  LYS   A NZ   1 
ATOM   529  H H    A LYS   A 1 19  ? 11.205 -7.124  8.665   0.80 17.94 ?  19  LYS   A H    1 
ATOM   530  H H    B LYS   A 1 19  ? 11.350 -7.021  8.930   0.20 15.44 ?  19  LYS   A H    1 
ATOM   531  H HA   A LYS   A 1 19  ? 8.962  -6.897  10.139  0.80 18.67 ?  19  LYS   A HA   1 
ATOM   532  H HA   B LYS   A 1 19  ? 9.136  -6.837  10.409  0.20 16.66 ?  19  LYS   A HA   1 
ATOM   533  H HB2  A LYS   A 1 19  ? 10.735 -6.919  11.726  0.80 19.76 ?  19  LYS   A HB2  1 
ATOM   534  H HB2  B LYS   A 1 19  ? 10.751 -6.897  12.108  0.20 17.70 ?  19  LYS   A HB2  1 
ATOM   535  H HB3  A LYS   A 1 19  ? 11.362 -5.662  10.999  0.80 19.76 ?  19  LYS   A HB3  1 
ATOM   536  H HB3  B LYS   A 1 19  ? 11.506 -5.678  11.431  0.20 17.70 ?  19  LYS   A HB3  1 
ATOM   537  H HG2  A LYS   A 1 19  ? 9.593  -4.345  11.735  0.80 22.08 ?  19  LYS   A HG2  1 
ATOM   538  H HG2  B LYS   A 1 19  ? 9.632  -4.312  11.923  0.20 18.74 ?  19  LYS   A HG2  1 
ATOM   539  H HG3  A LYS   A 1 19  ? 8.944  -5.619  12.450  0.80 22.08 ?  19  LYS   A HG3  1 
ATOM   540  H HG3  B LYS   A 1 19  ? 9.003  -5.539  12.719  0.20 18.74 ?  19  LYS   A HG3  1 
ATOM   541  H HD2  A LYS   A 1 19  ? 10.799 -5.790  13.847  0.80 24.55 ?  19  LYS   A HD2  1 
ATOM   542  H HD2  B LYS   A 1 19  ? 10.788 -5.474  14.221  0.20 19.79 ?  19  LYS   A HD2  1 
ATOM   543  H HD3  A LYS   A 1 19  ? 11.475 -4.550  13.121  0.80 24.55 ?  19  LYS   A HD3  1 
ATOM   544  H HD3  B LYS   A 1 19  ? 11.418 -4.252  13.420  0.20 19.79 ?  19  LYS   A HD3  1 
ATOM   545  H HE2  A LYS   A 1 19  ? 9.817  -3.150  13.993  0.80 26.51 ?  19  LYS   A HE2  1 
ATOM   546  H HE2  B LYS   A 1 19  ? 9.553  -2.944  13.997  0.20 20.49 ?  19  LYS   A HE2  1 
ATOM   547  H HE3  A LYS   A 1 19  ? 9.179  -4.399  14.752  0.80 26.51 ?  19  LYS   A HE3  1 
ATOM   548  H HE3  B LYS   A 1 19  ? 8.984  -4.161  14.849  0.20 20.49 ?  19  LYS   A HE3  1 
ATOM   549  H HZ1  A LYS   A 1 19  ? 10.543 -3.266  16.168  0.80 26.89 ?  19  LYS   A HZ1  1 
ATOM   550  H HZ1  B LYS   A 1 19  ? 10.061 -2.685  16.198  0.20 20.77 ?  19  LYS   A HZ1  1 
ATOM   551  H HZ2  A LYS   A 1 19  ? 11.140 -4.564  15.931  0.80 26.89 ?  19  LYS   A HZ2  1 
ATOM   552  H HZ2  B LYS   A 1 19  ? 10.782 -3.941  16.228  0.20 20.77 ?  19  LYS   A HZ2  1 
ATOM   553  H HZ3  A LYS   A 1 19  ? 11.673 -3.391  15.272  0.80 26.89 ?  19  LYS   A HZ3  1 
ATOM   554  H HZ3  B LYS   A 1 19  ? 11.296 -2.830  15.454  0.20 20.77 ?  19  LYS   A HZ3  1 
ATOM   555  N N    A ASN   A 1 20  ? 8.488  -4.622  9.200   0.80 16.07 ?  20  ASN   A N    1 
ATOM   556  N N    B ASN   A 1 20  ? 8.581  -4.619  9.457   0.20 13.42 ?  20  ASN   A N    1 
ATOM   557  C CA   A ASN   A 1 20  ? 8.289  -3.289  8.632   0.80 16.94 ?  20  ASN   A CA   1 
ATOM   558  C CA   B ASN   A 1 20  ? 8.241  -3.372  8.756   0.20 13.37 ?  20  ASN   A CA   1 
ATOM   559  C C    A ASN   A 1 20  ? 8.920  -2.289  9.594   0.80 17.74 ?  20  ASN   A C    1 
ATOM   560  C C    B ASN   A 1 20  ? 8.743  -2.191  9.580   0.20 13.85 ?  20  ASN   A C    1 
ATOM   561  O O    A ASN   A 1 20  ? 8.413  -2.074  10.700  0.80 18.90 ?  20  ASN   A O    1 
ATOM   562  O O    B ASN   A 1 20  ? 8.043  -1.667  10.451  0.20 13.98 ?  20  ASN   A O    1 
ATOM   563  C CB   A ASN   A 1 20  ? 6.799  -3.024  8.420   0.80 17.62 ?  20  ASN   A CB   1 
ATOM   564  C CB   B ASN   A 1 20  ? 6.732  -3.278  8.512   0.20 13.06 ?  20  ASN   A CB   1 
ATOM   565  C CG   A ASN   A 1 20  ? 6.491  -1.583  8.011   0.80 18.98 ?  20  ASN   A CG   1 
ATOM   566  C CG   B ASN   A 1 20  ? 6.320  -2.016  7.731   0.20 13.10 ?  20  ASN   A CG   1 
ATOM   567  O OD1  A ASN   A 1 20  ? 5.479  -1.024  8.428   0.80 22.38 ?  20  ASN   A OD1  1 
ATOM   568  O OD1  B ASN   A 1 20  ? 5.179  -1.544  7.844   0.20 12.76 ?  20  ASN   A OD1  1 
ATOM   569  N ND2  A ASN   A 1 20  ? 7.354  -0.985  7.195   0.80 18.61 ?  20  ASN   A ND2  1 
ATOM   570  N ND2  B ASN   A 1 20  ? 7.240  -1.476  6.935   0.20 14.24 ?  20  ASN   A ND2  1 
ATOM   571  H H    A ASN   A 1 20  ? 7.804  -4.938  9.621   0.80 19.28 ?  20  ASN   A H    1 
ATOM   572  H H    B ASN   A 1 20  ? 7.921  -4.955  9.888   0.20 16.10 ?  20  ASN   A H    1 
ATOM   573  H HA   A ASN   A 1 20  ? 8.743  -3.236  7.779   0.80 20.33 ?  20  ASN   A HA   1 
ATOM   574  H HA   B ASN   A 1 20  ? 8.691  -3.360  7.901   0.20 16.05 ?  20  ASN   A HA   1 
ATOM   575  H HB2  A ASN   A 1 20  ? 6.473  -3.608  7.718   0.80 21.14 ?  20  ASN   A HB2  1 
ATOM   576  H HB2  B ASN   A 1 20  ? 6.438  -4.051  8.012   0.20 15.67 ?  20  ASN   A HB2  1 
ATOM   577  H HB3  A ASN   A 1 20  ? 6.328  -3.209  9.248   0.80 21.14 ?  20  ASN   A HB3  1 
ATOM   578  H HB3  B ASN   A 1 20  ? 6.272  -3.252  9.362   0.20 15.67 ?  20  ASN   A HB3  1 
ATOM   579  H HD21 A ASN   A 1 20  ? 7.216  -0.177  6.946   0.80 22.33 ?  20  ASN   A HD21 1 
ATOM   580  H HD21 B ASN   A 1 20  ? 7.053  -0.771  6.481   0.20 17.09 ?  20  ASN   A HD21 1 
ATOM   581  H HD22 A ASN   A 1 20  ? 8.053  -1.408  6.918   0.80 22.33 ?  20  ASN   A HD22 1 
ATOM   582  H HD22 B ASN   A 1 20  ? 8.022  -1.825  6.873   0.20 17.09 ?  20  ASN   A HD22 1 
ATOM   583  N N    A ALA   A 1 21  ? 10.058 -1.720  9.206   0.80 17.95 ?  21  ALA   A N    1 
ATOM   584  N N    B ALA   A 1 21  ? 9.965  -1.747  9.286   0.20 14.47 ?  21  ALA   A N    1 
ATOM   585  C CA   A ALA   A 1 21  ? 10.764 -0.836  10.117  0.80 17.79 ?  21  ALA   A CA   1 
ATOM   586  C CA   B ALA   A 1 21  ? 10.587 -0.693  10.076  0.20 14.70 ?  21  ALA   A CA   1 
ATOM   587  C C    A ALA   A 1 21  ? 11.720 0.045   9.337   0.80 17.21 ?  21  ALA   A C    1 
ATOM   588  C C    B ALA   A 1 21  ? 11.746 -0.075  9.307   0.20 13.94 ?  21  ALA   A C    1 
ATOM   589  O O    A ALA   A 1 21  ? 12.182 -0.316  8.251   0.80 17.44 ?  21  ALA   A O    1 
ATOM   590  O O    B ALA   A 1 21  ? 12.276 -0.663  8.361   0.20 13.55 ?  21  ALA   A O    1 
ATOM   591  C CB   A ALA   A 1 21  ? 11.523 -1.626  11.188  0.80 18.46 ?  21  ALA   A CB   1 
ATOM   592  C CB   B ALA   A 1 21  ? 11.080 -1.229  11.424  0.20 15.36 ?  21  ALA   A CB   1 
ATOM   593  H H    A ALA   A 1 21  ? 10.431 -1.834  8.442   0.80 21.54 ?  21  ALA   A H    1 
ATOM   594  H H    B ALA   A 1 21  ? 10.440 -2.036  8.632   0.20 17.37 ?  21  ALA   A H    1 
ATOM   595  H HA   A ALA   A 1 21  ? 10.116 -0.268  10.564  0.80 21.35 ?  21  ALA   A HA   1 
ATOM   596  H HA   B ALA   A 1 21  ? 9.932  -0.000  10.247  0.20 17.64 ?  21  ALA   A HA   1 
ATOM   597  H HB1  A ALA   A 1 21  ? 11.934 -1.001  11.802  0.80 22.15 ?  21  ALA   A HB1  1 
ATOM   598  H HB1  B ALA   A 1 21  ? 11.509 -0.507  11.910  0.20 18.44 ?  21  ALA   A HB1  1 
ATOM   599  H HB2  A ALA   A 1 21  ? 10.893 -2.192  11.671  0.80 22.15 ?  21  ALA   A HB2  1 
ATOM   600  H HB2  B ALA   A 1 21  ? 10.322 -1.563  11.927  0.20 18.44 ?  21  ALA   A HB2  1 
ATOM   601  H HB3  A ALA   A 1 21  ? 12.196 -2.175  10.763  0.80 22.15 ?  21  ALA   A HB3  1 
ATOM   602  H HB3  B ALA   A 1 21  ? 11.716 -1.944  11.265  0.20 18.44 ?  21  ALA   A HB3  1 
ATOM   603  N N    A ASP   A 1 22  ? 11.986 1.215   9.911   0.80 17.55 ?  22  ASP   A N    1 
ATOM   604  N N    B ASP   A 1 22  ? 12.125 1.128   9.738   0.20 14.10 ?  22  ASP   A N    1 
ATOM   605  C CA   A ASP   A 1 22  ? 13.048 2.103   9.460   0.80 17.36 ?  22  ASP   A CA   1 
ATOM   606  C CA   B ASP   A 1 22  ? 13.306 1.811   9.225   0.20 14.26 ?  22  ASP   A CA   1 
ATOM   607  C C    A ASP   A 1 22  ? 14.362 1.593   10.042  0.80 15.75 ?  22  ASP   A C    1 
ATOM   608  C C    B ASP   A 1 22  ? 14.549 1.211   9.875   0.20 13.30 ?  22  ASP   A C    1 
ATOM   609  O O    A ASP   A 1 22  ? 14.548 1.601   11.263  0.80 16.92 ?  22  ASP   A O    1 
ATOM   610  O O    B ASP   A 1 22  ? 14.645 1.138   11.104  0.20 13.31 ?  22  ASP   A O    1 
ATOM   611  C CB   A ASP   A 1 22  ? 12.733 3.510   9.956   0.80 19.98 ?  22  ASP   A CB   1 
ATOM   612  C CB   B ASP   A 1 22  ? 13.204 3.302   9.562   0.20 15.32 ?  22  ASP   A CB   1 
ATOM   613  C CG   A ASP   A 1 22  ? 13.744 4.539   9.492   0.80 22.30 ?  22  ASP   A CG   1 
ATOM   614  C CG   B ASP   A 1 22  ? 14.331 4.129   8.968   0.20 15.58 ?  22  ASP   A CG   1 
ATOM   615  O OD1  A ASP   A 1 22  ? 14.870 4.173   9.106   0.80 22.95 ?  22  ASP   A OD1  1 
ATOM   616  O OD1  B ASP   A 1 22  ? 15.257 3.550   8.367   0.20 15.22 ?  22  ASP   A OD1  1 
ATOM   617  O OD2  A ASP   A 1 22  ? 13.407 5.738   9.517   0.80 24.32 -1 22  ASP   A OD2  1 
ATOM   618  O OD2  B ASP   A 1 22  ? 14.292 5.370   9.112   0.20 15.82 -1 22  ASP   A OD2  1 
ATOM   619  H H    A ASP   A 1 22  ? 11.532 1.525   10.573  0.80 21.07 ?  22  ASP   A H    1 
ATOM   620  H H    B ASP   A 1 22  ? 11.698 1.576   10.335  0.20 16.92 ?  22  ASP   A H    1 
ATOM   621  H HA   A ASP   A 1 22  ? 13.098 2.098   8.490   0.80 20.83 ?  22  ASP   A HA   1 
ATOM   622  H HA   B ASP   A 1 22  ? 13.357 1.705   8.259   0.20 17.11 ?  22  ASP   A HA   1 
ATOM   623  H HB2  A ASP   A 1 22  ? 11.856 3.768   9.625   0.80 23.98 ?  22  ASP   A HB2  1 
ATOM   624  H HB2  B ASP   A 1 22  ? 12.361 3.647   9.227   0.20 18.38 ?  22  ASP   A HB2  1 
ATOM   625  H HB3  A ASP   A 1 22  ? 12.722 3.498   10.929  0.80 23.98 ?  22  ASP   A HB3  1 
ATOM   626  H HB3  B ASP   A 1 22  ? 13.250 3.412   10.521  0.20 18.38 ?  22  ASP   A HB3  1 
ATOM   627  N N    A ILE   A 1 23  ? 15.273 1.149   9.171   0.80 15.46 ?  23  ILE   A N    1 
ATOM   628  N N    B ILE   A 1 23  ? 15.497 0.766   9.044   0.20 13.15 ?  23  ILE   A N    1 
ATOM   629  C CA   A ILE   A 1 23  ? 16.522 0.538   9.625   0.80 14.77 ?  23  ILE   A CA   1 
ATOM   630  C CA   B ILE   A 1 23  ? 16.720 0.154   9.554   0.20 13.09 ?  23  ILE   A CA   1 
ATOM   631  C C    A ILE   A 1 23  ? 17.316 1.487   10.517  0.80 14.67 ?  23  ILE   A C    1 
ATOM   632  C C    B ILE   A 1 23  ? 17.480 1.129   10.439  0.20 13.88 ?  23  ILE   A C    1 
ATOM   633  O O    A ILE   A 1 23  ? 18.022 1.042   11.431  0.80 15.33 ?  23  ILE   A O    1 
ATOM   634  O O    B ILE   A 1 23  ? 18.183 0.718   11.371  0.20 13.68 ?  23  ILE   A O    1 
ATOM   635  C CB   A ILE   A 1 23  ? 17.340 0.018   8.421   0.80 14.17 ?  23  ILE   A CB   1 
ATOM   636  C CB   B ILE   A 1 23  ? 17.587 -0.385  8.394   0.20 12.52 ?  23  ILE   A CB   1 
ATOM   637  C CG1  A ILE   A 1 23  ? 18.457 -0.927  8.885   0.80 14.51 ?  23  ILE   A CG1  1 
ATOM   638  C CG1  B ILE   A 1 23  ? 18.682 -1.312  8.932   0.20 12.28 ?  23  ILE   A CG1  1 
ATOM   639  C CG2  A ILE   A 1 23  ? 17.876 1.183   7.593   0.80 15.00 ?  23  ILE   A CG2  1 
ATOM   640  C CG2  B ILE   A 1 23  ? 18.201 0.757   7.586   0.20 12.36 ?  23  ILE   A CG2  1 
ATOM   641  C CD1  A ILE   A 1 23  ? 19.215 -1.597  7.747   0.80 15.23 ?  23  ILE   A CD1  1 
ATOM   642  C CD1  B ILE   A 1 23  ? 19.569 -1.908  7.854   0.20 12.16 ?  23  ILE   A CD1  1 
ATOM   643  H H    A ILE   A 1 23  ? 15.184 1.183   8.321   0.80 18.55 ?  23  ILE   A H    1 
ATOM   644  H H    B ILE   A 1 23  ? 15.460 0.802   8.198   0.20 15.77 ?  23  ILE   A H    1 
ATOM   645  H HA   A ILE   A 1 23  ? 16.299 -0.234  10.168  0.80 17.72 ?  23  ILE   A HA   1 
ATOM   646  H HA   B ILE   A 1 23  ? 16.467 -0.603  10.096  0.20 15.71 ?  23  ILE   A HA   1 
ATOM   647  H HB   A ILE   A 1 23  ? 16.739 -0.492  7.855   0.80 17.00 ?  23  ILE   A HB   1 
ATOM   648  H HB   B ILE   A 1 23  ? 17.020 -0.903  7.801   0.20 15.02 ?  23  ILE   A HB   1 
ATOM   649  H HG12 A ILE   A 1 23  ? 19.094 -0.424  9.410   0.80 17.41 ?  23  ILE   A HG12 1 
ATOM   650  H HG12 B ILE   A 1 23  ? 19.249 -0.812  9.538   0.20 14.74 ?  23  ILE   A HG12 1 
ATOM   651  H HG13 A ILE   A 1 23  ? 18.063 -1.629  9.429   0.80 17.41 ?  23  ILE   A HG13 1 
ATOM   652  H HG13 B ILE   A 1 23  ? 18.261 -2.047  9.407   0.20 14.74 ?  23  ILE   A HG13 1 
ATOM   653  H HG21 A ILE   A 1 23  ? 18.228 0.840   6.756   0.80 18.00 ?  23  ILE   A HG21 1 
ATOM   654  H HG21 B ILE   A 1 23  ? 18.551 0.402   6.750   0.20 14.83 ?  23  ILE   A HG21 1 
ATOM   655  H HG22 A ILE   A 1 23  ? 17.148 1.802   7.413   0.80 18.00 ?  23  ILE   A HG22 1 
ATOM   656  H HG22 B ILE   A 1 23  ? 17.515 1.416   7.400   0.20 14.83 ?  23  ILE   A HG22 1 
ATOM   657  H HG23 A ILE   A 1 23  ? 18.576 1.631   8.089   0.80 18.00 ?  23  ILE   A HG23 1 
ATOM   658  H HG23 B ILE   A 1 23  ? 18.918 1.160   8.098   0.20 14.83 ?  23  ILE   A HG23 1 
ATOM   659  H HD11 A ILE   A 1 23  ? 19.854 -2.224  8.121   0.80 18.27 ?  23  ILE   A HD11 1 
ATOM   660  H HD11 B ILE   A 1 23  ? 20.142 -2.582  8.253   0.20 14.60 ?  23  ILE   A HD11 1 
ATOM   661  H HD12 A ILE   A 1 23  ? 18.584 -2.066  7.179   0.80 18.27 ?  23  ILE   A HD12 1 
ATOM   662  H HD12 B ILE   A 1 23  ? 19.009 -2.311  7.172   0.20 14.60 ?  23  ILE   A HD12 1 
ATOM   663  H HD13 A ILE   A 1 23  ? 19.679 -0.917  7.234   0.80 18.27 ?  23  ILE   A HD13 1 
ATOM   664  H HD13 B ILE   A 1 23  ? 20.110 -1.203  7.464   0.20 14.60 ?  23  ILE   A HD13 1 
ATOM   665  N N    A VAL   A 1 24  ? 17.207 2.798   10.286  0.80 15.65 ?  24  VAL   A N    1 
ATOM   666  N N    B VAL   A 1 24  ? 17.348 2.429   10.173  0.20 15.29 ?  24  VAL   A N    1 
ATOM   667  C CA   A VAL   A 1 24  ? 17.889 3.761   11.149  0.80 17.46 ?  24  VAL   A CA   1 
ATOM   668  C CA   B VAL   A 1 24  ? 17.993 3.435   11.011  0.20 16.69 ?  24  VAL   A CA   1 
ATOM   669  C C    A VAL   A 1 24  ? 17.336 3.685   12.566  0.80 18.01 ?  24  VAL   A C    1 
ATOM   670  C C    B VAL   A 1 24  ? 17.401 3.407   12.415  0.20 17.73 ?  24  VAL   A C    1 
ATOM   671  O O    A VAL   A 1 24  ? 18.087 3.633   13.549  0.80 18.89 ?  24  VAL   A O    1 
ATOM   672  O O    B VAL   A 1 24  ? 18.127 3.386   13.415  0.20 18.32 ?  24  VAL   A O    1 
ATOM   673  C CB   A VAL   A 1 24  ? 17.761 5.182   10.572  0.80 18.67 ?  24  VAL   A CB   1 
ATOM   674  C CB   B VAL   A 1 24  ? 17.872 4.826   10.361  0.20 17.20 ?  24  VAL   A CB   1 
ATOM   675  C CG1  A VAL   A 1 24  ? 18.240 6.221   11.587  0.80 19.78 ?  24  VAL   A CG1  1 
ATOM   676  C CG1  B VAL   A 1 24  ? 18.568 5.870   11.211  0.20 17.88 ?  24  VAL   A CG1  1 
ATOM   677  C CG2  A VAL   A 1 24  ? 18.520 5.295   9.265   0.80 19.82 ?  24  VAL   A CG2  1 
ATOM   678  C CG2  B VAL   A 1 24  ? 18.441 4.807   8.947   0.20 17.13 ?  24  VAL   A CG2  1 
ATOM   679  H H    A VAL   A 1 24  ? 16.747 3.146   9.650   0.80 18.77 ?  24  VAL   A H    1 
ATOM   680  H H    B VAL   A 1 24  ? 16.889 2.751   9.524   0.20 18.35 ?  24  VAL   A H    1 
ATOM   681  H HA   A VAL   A 1 24  ? 18.831 3.539   11.185  0.80 20.95 ?  24  VAL   A HA   1 
ATOM   682  H HA   B VAL   A 1 24  ? 18.936 3.226   11.085  0.20 20.03 ?  24  VAL   A HA   1 
ATOM   683  H HB   A VAL   A 1 24  ? 16.828 5.361   10.384  0.80 22.41 ?  24  VAL   A HB   1 
ATOM   684  H HB   B VAL   A 1 24  ? 16.935 5.067   10.298  0.20 20.64 ?  24  VAL   A HB   1 
ATOM   685  H HG11 A VAL   A 1 24  ? 18.417 7.053   11.123  0.80 23.73 ?  24  VAL   A HG11 1 
ATOM   686  H HG11 B VAL   A 1 24  ? 18.643 6.691   10.701  0.20 21.45 ?  24  VAL   A HG11 1 
ATOM   687  H HG12 A VAL   A 1 24  ? 17.549 6.355   12.253  0.80 23.73 ?  24  VAL   A HG12 1 
ATOM   688  H HG12 B VAL   A 1 24  ? 18.043 6.025   12.011  0.20 21.45 ?  24  VAL   A HG12 1 
ATOM   689  H HG13 A VAL   A 1 24  ? 19.053 5.899   12.007  0.80 23.73 ?  24  VAL   A HG13 1 
ATOM   690  H HG13 B VAL   A 1 24  ? 19.450 5.545   11.447  0.20 21.45 ?  24  VAL   A HG13 1 
ATOM   691  H HG21 A VAL   A 1 24  ? 18.356 6.169   8.875   0.80 23.78 ?  24  VAL   A HG21 1 
ATOM   692  H HG21 B VAL   A 1 24  ? 18.459 5.713   8.600   0.20 20.56 ?  24  VAL   A HG21 1 
ATOM   693  H HG22 A VAL   A 1 24  ? 19.470 5.187   9.438   0.80 23.78 ?  24  VAL   A HG22 1 
ATOM   694  H HG22 B VAL   A 1 24  ? 19.342 4.447   8.974   0.20 20.56 ?  24  VAL   A HG22 1 
ATOM   695  H HG23 A VAL   A 1 24  ? 18.216 4.602   8.657   0.80 23.78 ?  24  VAL   A HG23 1 
ATOM   696  H HG23 B VAL   A 1 24  ? 17.880 4.250   8.385   0.20 20.56 ?  24  VAL   A HG23 1 
ATOM   697  N N    A GLU   A 1 25  ? 16.008 3.699   12.692  0.80 18.61 ?  25  GLU   A N    1 
ATOM   698  N N    B GLU   A 1 25  ? 16.069 3.391   12.508  0.20 18.47 ?  25  GLU   A N    1 
ATOM   699  C CA   A GLU   A 1 25  ? 15.397 3.647   14.015  0.80 20.14 ?  25  GLU   A CA   1 
ATOM   700  C CA   B GLU   A 1 25  ? 15.422 3.359   13.817  0.20 19.48 ?  25  GLU   A CA   1 
ATOM   701  C C    A GLU   A 1 25  ? 15.630 2.295   14.677  0.80 18.83 ?  25  GLU   A C    1 
ATOM   702  C C    B GLU   A 1 25  ? 15.635 2.015   14.505  0.20 19.07 ?  25  GLU   A C    1 
ATOM   703  O O    A GLU   A 1 25  ? 15.863 2.225   15.890  0.80 19.82 ?  25  GLU   A O    1 
ATOM   704  O O    B GLU   A 1 25  ? 15.803 1.958   15.729  0.20 19.49 ?  25  GLU   A O    1 
ATOM   705  C CB   A GLU   A 1 25  ? 13.909 3.994   13.920  0.80 22.98 ?  25  GLU   A CB   1 
ATOM   706  C CB   B GLU   A 1 25  ? 13.934 3.683   13.677  0.20 20.94 ?  25  GLU   A CB   1 
ATOM   707  C CG   A GLU   A 1 25  ? 13.661 5.465   13.576  0.80 27.21 ?  25  GLU   A CG   1 
ATOM   708  C CG   B GLU   A 1 25  ? 13.663 5.092   13.167  0.20 22.99 ?  25  GLU   A CG   1 
ATOM   709  C CD   A GLU   A 1 25  ? 14.445 6.423   14.464  0.80 30.88 ?  25  GLU   A CD   1 
ATOM   710  C CD   B GLU   A 1 25  ? 14.227 6.162   14.078  0.20 24.81 ?  25  GLU   A CD   1 
ATOM   711  O OE1  A GLU   A 1 25  ? 14.462 6.222   15.699  0.80 32.18 ?  25  GLU   A OE1  1 
ATOM   712  O OE1  B GLU   A 1 25  ? 14.203 5.964   15.311  0.20 25.68 ?  25  GLU   A OE1  1 
ATOM   713  O OE2  A GLU   A 1 25  ? 15.064 7.364   13.925  0.80 32.39 -1 25  GLU   A OE2  1 
ATOM   714  O OE2  B GLU   A 1 25  ? 14.695 7.197   13.560  0.20 25.56 -1 25  GLU   A OE2  1 
ATOM   715  H H    A GLU   A 1 25  ? 15.451 3.752   12.036  0.80 22.33 ?  25  GLU   A H    1 
ATOM   716  H H    B GLU   A 1 25  ? 15.529 3.398   11.840  0.20 22.16 ?  25  GLU   A H    1 
ATOM   717  H HA   A GLU   A 1 25  ? 15.821 4.311   14.576  0.80 24.17 ?  25  GLU   A HA   1 
ATOM   718  H HA   B GLU   A 1 25  ? 15.821 4.039   14.377  0.20 23.38 ?  25  GLU   A HA   1 
ATOM   719  H HB2  A GLU   A 1 25  ? 13.495 3.457   13.222  0.80 27.58 ?  25  GLU   A HB2  1 
ATOM   720  H HB2  B GLU   A 1 25  ? 13.531 3.062   13.051  0.20 25.13 ?  25  GLU   A HB2  1 
ATOM   721  H HB3  A GLU   A 1 25  ? 13.480 3.814   14.771  0.80 27.58 ?  25  GLU   A HB3  1 
ATOM   722  H HB3  B GLU   A 1 25  ? 13.510 3.597   14.546  0.20 25.13 ?  25  GLU   A HB3  1 
ATOM   723  H HG2  A GLU   A 1 25  ? 13.934 5.624   12.661  0.80 32.65 ?  25  GLU   A HG2  1 
ATOM   724  H HG2  B GLU   A 1 25  ? 14.067 5.197   12.292  0.20 27.59 ?  25  GLU   A HG2  1 
ATOM   725  H HG3  A GLU   A 1 25  ? 12.715 5.658   13.681  0.80 32.65 ?  25  GLU   A HG3  1 
ATOM   726  H HG3  B GLU   A 1 25  ? 12.707 5.236   13.114  0.20 27.59 ?  25  GLU   A HG3  1 
ATOM   727  N N    A GLU   A 1 26  ? 15.600 1.215   13.894  0.80 18.33 ?  26  GLU   A N    1 
ATOM   728  N N    B GLU   A 1 26  ? 15.636 0.923   13.738  0.20 18.56 ?  26  GLU   A N    1 
ATOM   729  C CA   A GLU   A 1 26  ? 15.915 -0.103  14.438  0.80 18.23 ?  26  GLU   A CA   1 
ATOM   730  C CA   B GLU   A 1 26  ? 15.972 -0.374  14.315  0.20 18.25 ?  26  GLU   A CA   1 
ATOM   731  C C    A GLU   A 1 26  ? 17.341 -0.146  14.977  0.80 17.30 ?  26  GLU   A C    1 
ATOM   732  C C    B GLU   A 1 26  ? 17.405 -0.401  14.826  0.20 17.45 ?  26  GLU   A C    1 
ATOM   733  O O    A GLU   A 1 26  ? 17.587 -0.652  16.078  0.80 17.77 ?  26  GLU   A O    1 
ATOM   734  O O    B GLU   A 1 26  ? 17.707 -1.112  15.790  0.20 17.38 ?  26  GLU   A O    1 
ATOM   735  C CB   A GLU   A 1 26  ? 15.735 -1.171  13.359  0.80 20.26 ?  26  GLU   A CB   1 
ATOM   736  C CB   B GLU   A 1 26  ? 15.769 -1.480  13.281  0.20 18.71 ?  26  GLU   A CB   1 
ATOM   737  C CG   A GLU   A 1 26  ? 14.333 -1.690  13.176  0.80 23.84 ?  26  GLU   A CG   1 
ATOM   738  C CG   B GLU   A 1 26  ? 14.316 -1.793  12.996  0.20 19.23 ?  26  GLU   A CG   1 
ATOM   739  C CD   A GLU   A 1 26  ? 13.837 -2.476  14.366  0.80 25.43 ?  26  GLU   A CD   1 
ATOM   740  C CD   B GLU   A 1 26  ? 13.586 -2.337  14.204  0.20 19.15 ?  26  GLU   A CD   1 
ATOM   741  O OE1  A GLU   A 1 26  ? 14.335 -3.598  14.623  0.80 25.56 ?  26  GLU   A OE1  1 
ATOM   742  O OE1  B GLU   A 1 26  ? 14.164 -3.172  14.929  0.20 19.69 ?  26  GLU   A OE1  1 
ATOM   743  O OE2  A GLU   A 1 26  ? 12.940 -1.953  15.043  0.80 26.58 -1 26  GLU   A OE2  1 
ATOM   744  O OE2  B GLU   A 1 26  ? 12.437 -1.909  14.433  0.20 18.15 -1 26  GLU   A OE2  1 
ATOM   745  H H    A GLU   A 1 26  ? 15.402 1.226   13.056  0.80 22.00 ?  26  GLU   A H    1 
ATOM   746  H H    B GLU   A 1 26  ? 15.444 0.905   12.901  0.20 22.27 ?  26  GLU   A H    1 
ATOM   747  H HA   A GLU   A 1 26  ? 15.307 -0.295  15.166  0.80 21.88 ?  26  GLU   A HA   1 
ATOM   748  H HA   B GLU   A 1 26  ? 15.386 -0.549  15.066  0.20 21.90 ?  26  GLU   A HA   1 
ATOM   749  H HB2  A GLU   A 1 26  ? 16.018 -0.795  12.509  0.80 24.32 ?  26  GLU   A HB2  1 
ATOM   750  H HB2  B GLU   A 1 26  ? 16.181 -1.205  12.445  0.20 22.46 ?  26  GLU   A HB2  1 
ATOM   751  H HB3  A GLU   A 1 26  ? 16.302 -1.922  13.585  0.80 24.32 ?  26  GLU   A HB3  1 
ATOM   752  H HB3  B GLU   A 1 26  ? 16.194 -2.291  13.603  0.20 22.46 ?  26  GLU   A HB3  1 
ATOM   753  H HG2  A GLU   A 1 26  ? 13.735 -0.940  13.045  0.80 28.61 ?  26  GLU   A HG2  1 
ATOM   754  H HG2  B GLU   A 1 26  ? 13.860 -0.980  12.745  0.20 23.08 ?  26  GLU   A HG2  1 
ATOM   755  H HG3  A GLU   A 1 26  ? 14.306 -2.277  12.408  0.80 28.61 ?  26  GLU   A HG3  1 
ATOM   756  H HG3  B GLU   A 1 26  ? 14.269 -2.445  12.280  0.20 23.08 ?  26  GLU   A HG3  1 
ATOM   757  N N    . ALA   A 1 27  ? 18.302 0.361   14.199  1.00 16.60 ?  27  ALA   A N    1 
ATOM   758  C CA   . ALA   A 1 27  ? 19.689 0.366   14.649  1.00 17.09 ?  27  ALA   A CA   1 
ATOM   759  C C    . ALA   A 1 27  ? 19.849 1.171   15.933  1.00 18.79 ?  27  ALA   A C    1 
ATOM   760  O O    . ALA   A 1 27  ? 20.514 0.724   16.875  1.00 19.29 ?  27  ALA   A O    1 
ATOM   761  C CB   . ALA   A 1 27  ? 20.606 0.898   13.545  1.00 16.42 ?  27  ALA   A CB   1 
ATOM   762  H H    A ALA   A 1 27  ? 18.174 0.704   13.418  0.80 19.92 ?  27  ALA   A H    1 
ATOM   763  H H    B ALA   A 1 27  ? 18.134 0.875   13.526  0.20 19.92 ?  27  ALA   A H    1 
ATOM   764  H HA   . ALA   A 1 27  ? 19.954 -0.544  14.835  1.00 20.50 ?  27  ALA   A HA   1 
ATOM   765  H HB1  . ALA   A 1 27  ? 21.523 0.887   13.865  1.00 19.70 ?  27  ALA   A HB1  1 
ATOM   766  H HB2  . ALA   A 1 27  ? 20.524 0.329   12.763  1.00 19.70 ?  27  ALA   A HB2  1 
ATOM   767  H HB3  . ALA   A 1 27  ? 20.346 1.805   13.323  1.00 19.70 ?  27  ALA   A HB3  1 
ATOM   768  N N    A LYS   A 1 28  ? 19.228 2.350   16.007  0.80 20.68 ?  28  LYS   A N    1 
ATOM   769  N N    B LYS   A 1 28  ? 19.236 2.360   15.988  0.20 20.78 ?  28  LYS   A N    1 
ATOM   770  C CA   A LYS   A 1 28  ? 19.376 3.169   17.205  0.80 23.43 ?  28  LYS   A CA   1 
ATOM   771  C CA   B LYS   A 1 28  ? 19.330 3.200   17.179  0.20 22.94 ?  28  LYS   A CA   1 
ATOM   772  C C    A LYS   A 1 28  ? 18.809 2.479   18.438  0.80 24.86 ?  28  LYS   A C    1 
ATOM   773  C C    B LYS   A 1 28  ? 18.779 2.489   18.408  0.20 24.86 ?  28  LYS   A C    1 
ATOM   774  O O    A LYS   A 1 28  ? 19.284 2.720   19.552  0.80 26.59 ?  28  LYS   A O    1 
ATOM   775  O O    B LYS   A 1 28  ? 19.289 2.679   19.518  0.20 25.35 ?  28  LYS   A O    1 
ATOM   776  C CB   A LYS   A 1 28  ? 18.748 4.547   16.997  0.80 25.75 ?  28  LYS   A CB   1 
ATOM   777  C CB   B LYS   A 1 28  ? 18.574 4.516   16.963  0.20 23.35 ?  28  LYS   A CB   1 
ATOM   778  C CG   A LYS   A 1 28  ? 19.596 5.445   16.115  0.80 27.86 ?  28  LYS   A CG   1 
ATOM   779  C CG   B LYS   A 1 28  ? 19.084 5.380   15.821  0.20 23.73 ?  28  LYS   A CG   1 
ATOM   780  C CD   A LYS   A 1 28  ? 19.140 6.889   16.153  0.80 30.81 ?  28  LYS   A CD   1 
ATOM   781  C CD   B LYS   A 1 28  ? 18.522 6.794   15.917  0.20 24.49 ?  28  LYS   A CD   1 
ATOM   782  C CE   A LYS   A 1 28  ? 17.818 7.062   15.444  0.80 32.70 ?  28  LYS   A CE   1 
ATOM   783  C CE   B LYS   A 1 28  ? 18.267 7.390   14.541  0.20 25.10 ?  28  LYS   A CE   1 
ATOM   784  N NZ   A LYS   A 1 28  ? 17.459 8.501   15.322  0.80 34.10 ?  28  LYS   A NZ   1 
ATOM   785  N NZ   B LYS   A 1 28  ? 18.378 8.879   14.540  0.20 25.44 ?  28  LYS   A NZ   1 
ATOM   786  H H    A LYS   A 1 28  ? 18.733 2.689   15.391  0.80 24.82 ?  28  LYS   A H    1 
ATOM   787  H H    B LYS   A 1 28  ? 18.761 2.695   15.355  0.20 24.93 ?  28  LYS   A H    1 
ATOM   788  H HA   A LYS   A 1 28  ? 20.320 3.306   17.366  0.80 28.12 ?  28  LYS   A HA   1 
ATOM   789  H HA   B LYS   A 1 28  ? 20.258 3.416   17.349  0.20 27.53 ?  28  LYS   A HA   1 
ATOM   790  H HB2  A LYS   A 1 28  ? 17.883 4.443   16.573  0.80 30.90 ?  28  LYS   A HB2  1 
ATOM   791  H HB2  B LYS   A 1 28  ? 17.644 4.316   16.772  0.20 28.01 ?  28  LYS   A HB2  1 
ATOM   792  H HB3  A LYS   A 1 28  ? 18.647 4.984   17.858  0.80 30.90 ?  28  LYS   A HB3  1 
ATOM   793  H HB3  B LYS   A 1 28  ? 18.634 5.050   17.769  0.20 28.01 ?  28  LYS   A HB3  1 
ATOM   794  H HG2  A LYS   A 1 28  ? 20.516 5.413   16.421  0.80 33.43 ?  28  LYS   A HG2  1 
ATOM   795  H HG2  B LYS   A 1 28  ? 20.052 5.433   15.861  0.20 28.47 ?  28  LYS   A HG2  1 
ATOM   796  H HG3  A LYS   A 1 28  ? 19.538 5.134   15.199  0.80 33.43 ?  28  LYS   A HG3  1 
ATOM   797  H HG3  B LYS   A 1 28  ? 18.803 5.002   14.974  0.20 28.47 ?  28  LYS   A HG3  1 
ATOM   798  H HD2  A LYS   A 1 28  ? 19.030 7.168   17.075  0.80 36.97 ?  28  LYS   A HD2  1 
ATOM   799  H HD2  B LYS   A 1 28  ? 17.681 6.772   16.401  0.20 29.39 ?  28  LYS   A HD2  1 
ATOM   800  H HD3  A LYS   A 1 28  ? 19.799 7.445   15.709  0.80 36.97 ?  28  LYS   A HD3  1 
ATOM   801  H HD3  B LYS   A 1 28  ? 19.160 7.362   16.380  0.20 29.39 ?  28  LYS   A HD3  1 
ATOM   802  H HE2  A LYS   A 1 28  ? 17.882 6.685   14.552  0.80 39.24 ?  28  LYS   A HE2  1 
ATOM   803  H HE2  B LYS   A 1 28  ? 18.918 7.037   13.917  0.20 30.12 ?  28  LYS   A HE2  1 
ATOM   804  H HE3  A LYS   A 1 28  ? 17.122 6.615   15.950  0.80 39.24 ?  28  LYS   A HE3  1 
ATOM   805  H HE3  B LYS   A 1 28  ? 17.368 7.154   14.256  0.20 30.12 ?  28  LYS   A HE3  1 
ATOM   806  H HZ1  A LYS   A 1 28  ? 16.680 8.585   14.902  0.80 40.92 ?  28  LYS   A HZ1  1 
ATOM   807  H HZ1  B LYS   A 1 28  ? 18.222 9.195   13.722  0.20 30.52 ?  28  LYS   A HZ1  1 
ATOM   808  H HZ2  A LYS   A 1 28  ? 17.395 8.868   16.130  0.80 40.92 ?  28  LYS   A HZ2  1 
ATOM   809  H HZ2  B LYS   A 1 28  ? 17.785 9.230   15.103  0.20 30.52 ?  28  LYS   A HZ2  1 
ATOM   810  H HZ3  A LYS   A 1 28  ? 18.086 8.932   14.859  0.80 40.92 ?  28  LYS   A HZ3  1 
ATOM   811  H HZ3  B LYS   A 1 28  ? 19.196 9.122   14.793  0.20 30.52 ?  28  LYS   A HZ3  1 
ATOM   812  N N    A LYS   A 1 29  ? 17.811 1.612   18.263  0.80 25.23 ?  29  LYS   A N    1 
ATOM   813  N N    B LYS   A 1 29  ? 17.744 1.667   18.229  0.20 26.32 ?  29  LYS   A N    1 
ATOM   814  C CA   A LYS   A 1 29  ? 17.214 0.912   19.398  0.80 27.09 ?  29  LYS   A CA   1 
ATOM   815  C CA   B LYS   A 1 29  ? 17.094 1.003   19.353  0.20 27.94 ?  29  LYS   A CA   1 
ATOM   816  C C    A LYS   A 1 29  ? 18.031 -0.313  19.795  0.80 27.48 ?  29  LYS   A C    1 
ATOM   817  C C    B LYS   A 1 29  ? 17.835 -0.262  19.765  0.20 27.64 ?  29  LYS   A C    1 
ATOM   818  O O    A LYS   A 1 29  ? 18.332 -0.511  20.978  0.80 29.29 ?  29  LYS   A O    1 
ATOM   819  O O    B LYS   A 1 29  ? 18.024 -0.513  20.961  0.20 27.86 ?  29  LYS   A O    1 
ATOM   820  C CB   A LYS   A 1 29  ? 15.784 0.493   19.053  0.80 29.49 ?  29  LYS   A CB   1 
ATOM   821  C CB   B LYS   A 1 29  ? 15.652 0.657   18.980  0.20 29.83 ?  29  LYS   A CB   1 
ATOM   822  C CG   A LYS   A 1 29  ? 15.042 -0.184  20.196  0.80 32.85 ?  29  LYS   A CG   1 
ATOM   823  C CG   B LYS   A 1 29  ? 14.848 0.013   20.098  0.20 31.67 ?  29  LYS   A CG   1 
ATOM   824  C CD   A LYS   A 1 29  ? 14.738 0.803   21.312  0.80 35.88 ?  29  LYS   A CD   1 
ATOM   825  C CD   B LYS   A 1 29  ? 14.592 0.990   21.232  0.20 33.24 ?  29  LYS   A CD   1 
ATOM   826  C CE   A LYS   A 1 29  ? 13.862 0.178   22.385  0.80 37.87 ?  29  LYS   A CE   1 
ATOM   827  C CE   B LYS   A 1 29  ? 13.696 0.376   22.296  0.20 34.36 ?  29  LYS   A CE   1 
ATOM   828  N NZ   A LYS   A 1 29  ? 13.476 1.170   23.426  0.80 39.11 ?  29  LYS   A NZ   1 
ATOM   829  N NZ   B LYS   A 1 29  ? 13.430 1.325   23.411  0.20 35.01 ?  29  LYS   A NZ   1 
ATOM   830  H H    A LYS   A 1 29  ? 17.458 1.420   17.503  0.80 30.27 ?  29  LYS   A H    1 
ATOM   831  H H    B LYS   A 1 29  ? 17.405 1.481   17.467  0.20 31.59 ?  29  LYS   A H    1 
ATOM   832  H HA   A LYS   A 1 29  ? 17.180 1.512   20.158  0.80 32.51 ?  29  LYS   A HA   1 
ATOM   833  H HA   B LYS   A 1 29  ? 17.076 1.604   20.112  0.20 33.53 ?  29  LYS   A HA   1 
ATOM   834  H HB2  A LYS   A 1 29  ? 15.280 1.281   18.803  0.80 35.39 ?  29  LYS   A HB2  1 
ATOM   835  H HB2  B LYS   A 1 29  ? 15.195 1.471   18.721  0.20 35.79 ?  29  LYS   A HB2  1 
ATOM   836  H HB3  A LYS   A 1 29  ? 15.812 -0.130  18.311  0.80 35.39 ?  29  LYS   A HB3  1 
ATOM   837  H HB3  B LYS   A 1 29  ? 15.666 0.037   18.233  0.20 35.79 ?  29  LYS   A HB3  1 
ATOM   838  H HG2  A LYS   A 1 29  ? 14.201 -0.536  19.867  0.80 39.41 ?  29  LYS   A HG2  1 
ATOM   839  H HG2  B LYS   A 1 29  ? 13.991 -0.275  19.747  0.20 38.00 ?  29  LYS   A HG2  1 
ATOM   840  H HG3  A LYS   A 1 29  ? 15.584 -0.902  20.562  0.80 39.41 ?  29  LYS   A HG3  1 
ATOM   841  H HG3  B LYS   A 1 29  ? 15.334 -0.748  20.455  0.20 38.00 ?  29  LYS   A HG3  1 
ATOM   842  H HD2  A LYS   A 1 29  ? 15.569 1.085   21.726  0.80 43.06 ?  29  LYS   A HD2  1 
ATOM   843  H HD2  B LYS   A 1 29  ? 15.435 1.230   21.647  0.20 39.89 ?  29  LYS   A HD2  1 
ATOM   844  H HD3  A LYS   A 1 29  ? 14.270 1.568   20.943  0.80 43.06 ?  29  LYS   A HD3  1 
ATOM   845  H HD3  B LYS   A 1 29  ? 14.152 1.780   20.881  0.20 39.89 ?  29  LYS   A HD3  1 
ATOM   846  H HE2  A LYS   A 1 29  ? 13.052 -0.165  21.976  0.80 45.45 ?  29  LYS   A HE2  1 
ATOM   847  H HE2  B LYS   A 1 29  ? 12.847 0.132   21.895  0.20 41.23 ?  29  LYS   A HE2  1 
ATOM   848  H HE3  A LYS   A 1 29  ? 14.349 -0.542  22.817  0.80 45.45 ?  29  LYS   A HE3  1 
ATOM   849  H HE3  B LYS   A 1 29  ? 14.130 -0.410  22.663  0.20 41.23 ?  29  LYS   A HE3  1 
ATOM   850  H HZ1  A LYS   A 1 29  ? 12.964 0.781   24.042  0.80 46.94 ?  29  LYS   A HZ1  1 
ATOM   851  H HZ1  B LYS   A 1 29  ? 12.904 0.941   24.017  0.20 42.01 ?  29  LYS   A HZ1  1 
ATOM   852  H HZ2  A LYS   A 1 29  ? 14.204 1.497   23.819  0.80 46.94 ?  29  LYS   A HZ2  1 
ATOM   853  H HZ2  B LYS   A 1 29  ? 14.196 1.561   23.798  0.20 42.01 ?  29  LYS   A HZ2  1 
ATOM   854  H HZ3  A LYS   A 1 29  ? 13.023 1.840   23.054  0.80 46.94 ?  29  LYS   A HZ3  1 
ATOM   855  H HZ3  B LYS   A 1 29  ? 13.027 2.055   23.098  0.20 42.01 ?  29  LYS   A HZ3  1 
ATOM   856  N N    A VAL   A 1 30  ? 18.376 -1.156  18.822  0.80 25.78 ?  30  VAL   A N    1 
ATOM   857  N N    B VAL   A 1 30  ? 18.252 -1.071  18.794  0.20 27.14 ?  30  VAL   A N    1 
ATOM   858  C CA   A VAL   A 1 30  ? 19.022 -2.430  19.118  0.80 24.62 ?  30  VAL   A CA   1 
ATOM   859  C CA   B VAL   A 1 30  ? 18.896 -2.342  19.102  0.20 26.71 ?  30  VAL   A CA   1 
ATOM   860  C C    A VAL   A 1 30  ? 20.519 -2.261  19.352  0.80 23.26 ?  30  VAL   A C    1 
ATOM   861  C C    B VAL   A 1 30  ? 20.395 -2.176  19.323  0.20 26.30 ?  30  VAL   A C    1 
ATOM   862  O O    A VAL   A 1 30  ? 21.107 -2.984  20.162  0.80 23.93 ?  30  VAL   A O    1 
ATOM   863  O O    B VAL   A 1 30  ? 20.982 -2.892  20.141  0.20 26.20 ?  30  VAL   A O    1 
ATOM   864  C CB   A VAL   A 1 30  ? 18.740 -3.431  17.982  0.80 25.63 ?  30  VAL   A CB   1 
ATOM   865  C CB   B VAL   A 1 30  ? 18.615 -3.354  17.976  0.20 26.76 ?  30  VAL   A CB   1 
ATOM   866  C CG1  A VAL   A 1 30  ? 19.528 -4.720  18.183  0.80 26.52 ?  30  VAL   A CG1  1 
ATOM   867  C CG1  B VAL   A 1 30  ? 19.371 -4.652  18.217  0.20 26.89 ?  30  VAL   A CG1  1 
ATOM   868  C CG2  A VAL   A 1 30  ? 17.251 -3.726  17.888  0.80 26.50 ?  30  VAL   A CG2  1 
ATOM   869  C CG2  B VAL   A 1 30  ? 17.124 -3.614  17.853  0.20 26.93 ?  30  VAL   A CG2  1 
ATOM   870  H H    A VAL   A 1 30  ? 18.239 -1.019  17.986  0.80 30.93 ?  30  VAL   A H    1 
ATOM   871  H H    B VAL   A 1 30  ? 18.182 -0.905  17.952  0.20 32.57 ?  30  VAL   A H    1 
ATOM   872  H HA   A VAL   A 1 30  ? 18.634 -2.795  19.927  0.80 29.54 ?  30  VAL   A HA   1 
ATOM   873  H HA   B VAL   A 1 30  ? 18.506 -2.693  19.919  0.20 32.05 ?  30  VAL   A HA   1 
ATOM   874  H HB   A VAL   A 1 30  ? 19.022 -3.042  17.138  0.80 30.76 ?  30  VAL   A HB   1 
ATOM   875  H HB   B VAL   A 1 30  ? 18.928 -2.984  17.136  0.20 32.12 ?  30  VAL   A HB   1 
ATOM   876  H HG11 A VAL   A 1 30  ? 19.164 -5.405  17.599  0.80 31.83 ?  30  VAL   A HG11 1 
ATOM   877  H HG11 B VAL   A 1 30  ? 18.950 -5.362  17.706  0.20 32.26 ?  30  VAL   A HG11 1 
ATOM   878  H HG12 A VAL   A 1 30  ? 20.460 -4.562  17.963  0.80 31.83 ?  30  VAL   A HG12 1 
ATOM   879  H HG12 B VAL   A 1 30  ? 20.292 -4.542  17.932  0.20 32.26 ?  30  VAL   A HG12 1 
ATOM   880  H HG13 A VAL   A 1 30  ? 19.446 -4.998  19.108  0.80 31.83 ?  30  VAL   A HG13 1 
ATOM   881  H HG13 B VAL   A 1 30  ? 19.339 -4.862  19.162  0.20 32.26 ?  30  VAL   A HG13 1 
ATOM   882  H HG21 A VAL   A 1 30  ? 17.102 -4.380  17.186  0.80 31.80 ?  30  VAL   A HG21 1 
ATOM   883  H HG21 B VAL   A 1 30  ? 16.977 -4.276  17.160  0.20 32.32 ?  30  VAL   A HG21 1 
ATOM   884  H HG22 A VAL   A 1 30  ? 16.947 -4.082  18.738  0.80 31.80 ?  30  VAL   A HG22 1 
ATOM   885  H HG22 B VAL   A 1 30  ? 16.791 -3.943  18.702  0.20 32.32 ?  30  VAL   A HG22 1 
ATOM   886  H HG23 A VAL   A 1 30  ? 16.780 -2.906  17.683  0.80 31.80 ?  30  VAL   A HG23 1 
ATOM   887  H HG23 B VAL   A 1 30  ? 16.680 -2.785  17.620  0.20 32.32 ?  30  VAL   A HG23 1 
ATOM   888  N N    A LYS   A 1 31  ? 21.155 -1.320  18.661  0.80 21.91 ?  31  LYS   A N    1 
ATOM   889  N N    B LYS   A 1 31  ? 21.020 -1.240  18.618  0.20 26.19 ?  31  LYS   A N    1 
ATOM   890  C CA   A LYS   A 1 31  ? 22.609 -1.213  18.615  0.80 22.66 ?  31  LYS   A CA   1 
ATOM   891  C CA   B LYS   A 1 31  ? 22.471 -1.108  18.578  0.20 26.47 ?  31  LYS   A CA   1 
ATOM   892  C C    A LYS   A 1 31  ? 23.224 -2.574  18.276  0.80 20.60 ?  31  LYS   A C    1 
ATOM   893  C C    B LYS   A 1 31  ? 23.114 -2.468  18.290  0.20 24.55 ?  31  LYS   A C    1 
ATOM   894  O O    A LYS   A 1 31  ? 24.006 -3.123  19.057  0.80 22.29 ?  31  LYS   A O    1 
ATOM   895  O O    B LYS   A 1 31  ? 23.867 -2.993  19.116  0.20 24.78 ?  31  LYS   A O    1 
ATOM   896  C CB   A LYS   A 1 31  ? 23.183 -0.664  19.912  0.80 27.64 ?  31  LYS   A CB   1 
ATOM   897  C CB   B LYS   A 1 31  ? 23.027 -0.501  19.858  0.20 28.88 ?  31  LYS   A CB   1 
ATOM   898  C CG   A LYS   A 1 31  ? 22.502 0.601   20.400  0.80 33.49 ?  31  LYS   A CG   1 
ATOM   899  C CG   B LYS   A 1 31  ? 22.321 0.768   20.302  0.20 31.42 ?  31  LYS   A CG   1 
ATOM   900  C CD   A LYS   A 1 31  ? 23.512 1.673   20.773  0.80 37.88 ?  31  LYS   A CD   1 
ATOM   901  C CD   B LYS   A 1 31  ? 23.280 1.710   21.007  0.20 33.54 ?  31  LYS   A CD   1 
ATOM   902  C CE   A LYS   A 1 31  ? 22.890 2.725   21.680  0.80 40.84 ?  31  LYS   A CE   1 
ATOM   903  C CE   B LYS   A 1 31  ? 22.535 2.752   21.823  0.20 34.99 ?  31  LYS   A CE   1 
ATOM   904  N NZ   A LYS   A 1 31  ? 21.661 3.333   21.100  0.80 42.23 ?  31  LYS   A NZ   1 
ATOM   905  N NZ   B LYS   A 1 31  ? 21.448 3.408   21.046  0.20 35.86 ?  31  LYS   A NZ   1 
ATOM   906  H H    A LYS   A 1 31  ? 20.752 -0.720  18.197  0.80 26.29 ?  31  LYS   A H    1 
ATOM   907  H H    B LYS   A 1 31  ? 20.609 -0.662  18.139  0.20 31.43 ?  31  LYS   A H    1 
ATOM   908  H HA   A LYS   A 1 31  ? 22.844 -0.598  17.905  0.80 27.19 ?  31  LYS   A HA   1 
ATOM   909  H HA   B LYS   A 1 31  ? 22.696 -0.512  17.853  0.20 31.77 ?  31  LYS   A HA   1 
ATOM   910  H HB2  A LYS   A 1 31  ? 23.091 -1.341  20.595  0.80 33.17 ?  31  LYS   A HB2  1 
ATOM   911  H HB2  B LYS   A 1 31  ? 22.950 -1.147  20.574  0.20 34.65 ?  31  LYS   A HB2  1 
ATOM   912  H HB3  A LYS   A 1 31  ? 24.123 -0.462  19.772  0.80 33.17 ?  31  LYS   A HB3  1 
ATOM   913  H HB3  B LYS   A 1 31  ? 23.963 -0.280  19.715  0.20 34.65 ?  31  LYS   A HB3  1 
ATOM   914  H HG2  A LYS   A 1 31  ? 21.934 0.951   19.695  0.80 40.19 ?  31  LYS   A HG2  1 
ATOM   915  H HG2  B LYS   A 1 31  ? 21.959 1.225   19.526  0.20 37.71 ?  31  LYS   A HG2  1 
ATOM   916  H HG3  A LYS   A 1 31  ? 21.973 0.394   21.186  0.80 40.19 ?  31  LYS   A HG3  1 
ATOM   917  H HG3  B LYS   A 1 31  ? 21.608 0.540   20.920  0.20 37.71 ?  31  LYS   A HG3  1 
ATOM   918  H HD2  A LYS   A 1 31  ? 24.256 1.265   21.244  0.80 45.46 ?  31  LYS   A HD2  1 
ATOM   919  H HD2  B LYS   A 1 31  ? 23.847 1.200   21.607  0.20 40.24 ?  31  LYS   A HD2  1 
ATOM   920  H HD3  A LYS   A 1 31  ? 23.827 2.113   19.966  0.80 45.46 ?  31  LYS   A HD3  1 
ATOM   921  H HD3  B LYS   A 1 31  ? 23.821 2.171   20.345  0.20 40.24 ?  31  LYS   A HD3  1 
ATOM   922  H HE2  A LYS   A 1 31  ? 22.650 2.310   22.524  0.80 49.01 ?  31  LYS   A HE2  1 
ATOM   923  H HE2  B LYS   A 1 31  ? 22.138 2.322   22.596  0.20 41.99 ?  31  LYS   A HE2  1 
ATOM   924  H HE3  A LYS   A 1 31  ? 23.534 3.434   21.830  0.80 49.01 ?  31  LYS   A HE3  1 
ATOM   925  H HE3  B LYS   A 1 31  ? 23.160 3.438   22.106  0.20 41.99 ?  31  LYS   A HE3  1 
ATOM   926  H HZ1  A LYS   A 1 31  ? 21.341 3.956   21.650  0.80 50.68 ?  31  LYS   A HZ1  1 
ATOM   927  H HZ1  B LYS   A 1 31  ? 21.078 4.056   21.530  0.20 43.03 ?  31  LYS   A HZ1  1 
ATOM   928  H HZ2  A LYS   A 1 31  ? 21.848 3.708   20.315  0.80 50.68 ?  31  LYS   A HZ2  1 
ATOM   929  H HZ2  B LYS   A 1 31  ? 21.776 3.757   20.297  0.20 43.03 ?  31  LYS   A HZ2  1 
ATOM   930  H HZ3  A LYS   A 1 31  ? 21.038 2.708   20.980  0.80 50.68 ?  31  LYS   A HZ3  1 
ATOM   931  H HZ3  B LYS   A 1 31  ? 20.821 2.811   20.836  0.20 43.03 ?  31  LYS   A HZ3  1 
ATOM   932  N N    A PRO   A 1 32  ? 22.885 -3.137  17.120  0.80 18.25 ?  32  PRO   A N    1 
ATOM   933  N N    B PRO   A 1 32  ? 22.835 -3.057  17.131  0.20 22.52 ?  32  PRO   A N    1 
ATOM   934  C CA   A PRO   A 1 32  ? 23.362 -4.478  16.782  0.80 18.31 ?  32  PRO   A CA   1 
ATOM   935  C CA   B PRO   A 1 32  ? 23.317 -4.413  16.855  0.20 21.44 ?  32  PRO   A CA   1 
ATOM   936  C C    A PRO   A 1 32  ? 24.865 -4.491  16.576  0.80 18.25 ?  32  PRO   A C    1 
ATOM   937  C C    B PRO   A 1 32  ? 24.822 -4.430  16.644  0.20 20.42 ?  32  PRO   A C    1 
ATOM   938  O O    A PRO   A 1 32  ? 25.504 -3.460  16.352  0.80 18.68 ?  32  PRO   A O    1 
ATOM   939  O O    B PRO   A 1 32  ? 25.482 -3.397  16.519  0.20 20.46 ?  32  PRO   A O    1 
ATOM   940  C CB   A PRO   A 1 32  ? 22.647 -4.772  15.460  0.80 18.27 ?  32  PRO   A CB   1 
ATOM   941  C CB   B PRO   A 1 32  ? 22.580 -4.784  15.567  0.20 21.46 ?  32  PRO   A CB   1 
ATOM   942  C CG   A PRO   A 1 32  ? 22.501 -3.418  14.833  0.80 17.23 ?  32  PRO   A CG   1 
ATOM   943  C CG   B PRO   A 1 32  ? 22.403 -3.478  14.870  0.20 21.62 ?  32  PRO   A CG   1 
ATOM   944  C CD   A PRO   A 1 32  ? 22.176 -2.512  15.992  0.80 17.31 ?  32  PRO   A CD   1 
ATOM   945  C CD   B PRO   A 1 32  ? 22.150 -2.471  15.965  0.20 21.94 ?  32  PRO   A CD   1 
ATOM   946  H HA   A PRO   A 1 32  ? 23.101 -5.126  17.454  0.80 21.97 ?  32  PRO   A HA   1 
ATOM   947  H HA   B PRO   A 1 32  ? 23.068 -5.023  17.567  0.20 25.73 ?  32  PRO   A HA   1 
ATOM   948  H HB2  A PRO   A 1 32  ? 23.193 -5.356  14.905  0.80 21.93 ?  32  PRO   A HB2  1 
ATOM   949  H HB2  B PRO   A 1 32  ? 23.122 -5.389  15.037  0.20 25.76 ?  32  PRO   A HB2  1 
ATOM   950  H HB3  A PRO   A 1 32  ? 21.778 -5.173  15.629  0.80 21.93 ?  32  PRO   A HB3  1 
ATOM   951  H HB3  B PRO   A 1 32  ? 21.720 -5.182  15.778  0.20 25.76 ?  32  PRO   A HB3  1 
ATOM   952  H HG2  A PRO   A 1 32  ? 23.335 -3.166  14.411  0.80 20.67 ?  32  PRO   A HG2  1 
ATOM   953  H HG2  B PRO   A 1 32  ? 23.213 -3.258  14.383  0.20 25.94 ?  32  PRO   A HG2  1 
ATOM   954  H HG3  A PRO   A 1 32  ? 21.776 -3.437  14.186  0.80 20.67 ?  32  PRO   A HG3  1 
ATOM   955  H HG3  B PRO   A 1 32  ? 21.645 -3.530  14.268  0.20 25.94 ?  32  PRO   A HG3  1 
ATOM   956  H HD2  A PRO   A 1 32  ? 22.518 -1.624  15.814  0.80 20.78 ?  32  PRO   A HD2  1 
ATOM   957  H HD2  B PRO   A 1 32  ? 22.543 -1.616  15.729  0.20 26.32 ?  32  PRO   A HD2  1 
ATOM   958  H HD3  A PRO   A 1 32  ? 21.220 -2.507  16.147  0.80 20.78 ?  32  PRO   A HD3  1 
ATOM   959  H HD3  B PRO   A 1 32  ? 21.198 -2.392  16.131  0.20 26.32 ?  32  PRO   A HD3  1 
ATOM   960  N N    A THR   A 1 33  ? 25.422 -5.700  16.616  0.80 18.66 ?  33  THR   A N    1 
ATOM   961  N N    B THR   A 1 33  ? 25.365 -5.647  16.603  0.20 19.70 ?  33  THR   A N    1 
ATOM   962  C CA   A THR   A 1 33  ? 26.835 -5.862  16.302  0.80 18.90 ?  33  THR   A CA   1 
ATOM   963  C CA   B THR   A 1 33  ? 26.786 -5.806  16.314  0.20 19.02 ?  33  THR   A CA   1 
ATOM   964  C C    A THR   A 1 33  ? 27.135 -5.400  14.883  0.80 17.18 ?  33  THR   A C    1 
ATOM   965  C C    B THR   A 1 33  ? 27.107 -5.368  14.891  0.20 17.41 ?  33  THR   A C    1 
ATOM   966  O O    A THR   A 1 33  ? 28.161 -4.747  14.639  0.80 17.41 ?  33  THR   A O    1 
ATOM   967  O O    B THR   A 1 33  ? 28.130 -4.713  14.653  0.20 17.42 ?  33  THR   A O    1 
ATOM   968  C CB   A THR   A 1 33  ? 27.250 -7.319  16.493  0.80 21.11 ?  33  THR   A CB   1 
ATOM   969  C CB   B THR   A 1 33  ? 27.203 -7.259  16.535  0.20 20.08 ?  33  THR   A CB   1 
ATOM   970  O OG1  A THR   A 1 33  ? 26.966 -7.722  17.837  0.80 23.05 ?  33  THR   A OG1  1 
ATOM   971  O OG1  B THR   A 1 33  ? 26.903 -7.646  17.881  0.20 20.94 ?  33  THR   A OG1  1 
ATOM   972  C CG2  A THR   A 1 33  ? 28.736 -7.490  16.221  0.80 21.75 ?  33  THR   A CG2  1 
ATOM   973  C CG2  B THR   A 1 33  ? 28.694 -7.431  16.284  0.20 20.33 ?  33  THR   A CG2  1 
ATOM   974  H H    A THR   A 1 33  ? 25.009 -6.430  16.813  0.80 22.39 ?  33  THR   A H    1 
ATOM   975  H H    B THR   A 1 33  ? 24.940 -6.382  16.739  0.20 23.63 ?  33  THR   A H    1 
ATOM   976  H HA   A THR   A 1 33  ? 27.357 -5.318  16.911  0.80 22.67 ?  33  THR   A HA   1 
ATOM   977  H HA   B THR   A 1 33  ? 27.295 -5.250  16.922  0.20 22.83 ?  33  THR   A HA   1 
ATOM   978  H HB   A THR   A 1 33  ? 26.757 -7.883  15.874  0.80 25.33 ?  33  THR   A HB   1 
ATOM   979  H HB   B THR   A 1 33  ? 26.720 -7.832  15.917  0.20 24.09 ?  33  THR   A HB   1 
ATOM   980  H HG1  A THR   A 1 33  ? 27.402 -7.247  18.377  0.80 27.66 ?  33  THR   A HG1  1 
ATOM   981  H HG1  B THR   A 1 33  ? 27.324 -7.156  18.418  0.20 25.12 ?  33  THR   A HG1  1 
ATOM   982  H HG21 A THR   A 1 33  ? 29.028 -8.364  16.520  0.80 26.10 ?  33  THR   A HG21 1 
ATOM   983  H HG21 B THR   A 1 33  ? 28.983 -8.301  16.597  0.20 24.39 ?  33  THR   A HG21 1 
ATOM   984  H HG22 A THR   A 1 33  ? 28.913 -7.408  15.270  0.80 26.10 ?  33  THR   A HG22 1 
ATOM   985  H HG22 B THR   A 1 33  ? 28.884 -7.360  15.335  0.20 24.39 ?  33  THR   A HG22 1 
ATOM   986  H HG23 A THR   A 1 33  ? 29.238 -6.810  16.696  0.80 26.10 ?  33  THR   A HG23 1 
ATOM   987  H HG23 B THR   A 1 33  ? 29.190 -6.745  16.758  0.20 24.39 ?  33  THR   A HG23 1 
ATOM   988  N N    . VAL   A 1 34  ? 26.247 -5.715  13.936  1.00 15.92 ?  34  VAL   A N    1 
ATOM   989  C CA   . VAL   A 1 34  ? 26.441 -5.383  12.527  1.00 14.06 ?  34  VAL   A CA   1 
ATOM   990  C C    . VAL   A 1 34  ? 25.145 -4.829  11.958  1.00 13.45 ?  34  VAL   A C    1 
ATOM   991  O O    . VAL   A 1 34  ? 24.106 -5.500  12.003  1.00 14.58 ?  34  VAL   A O    1 
ATOM   992  C CB   . VAL   A 1 34  ? 26.887 -6.596  11.690  1.00 14.69 ?  34  VAL   A CB   1 
ATOM   993  C CG1  . VAL   A 1 34  ? 27.048 -6.202  10.227  1.00 14.93 ?  34  VAL   A CG1  1 
ATOM   994  C CG2  . VAL   A 1 34  ? 28.165 -7.208  12.245  1.00 16.46 ?  34  VAL   A CG2  1 
ATOM   995  H H    A VAL   A 1 34  ? 25.506 -6.126  14.094  0.80 19.11 ?  34  VAL   A H    1 
ATOM   996  H H    B VAL   A 1 34  ? 25.522 -6.157  14.086  0.20 19.11 ?  34  VAL   A H    1 
ATOM   997  H HA   . VAL   A 1 34  ? 27.118 -4.696  12.445  1.00 16.87 ?  34  VAL   A HA   1 
ATOM   998  H HB   . VAL   A 1 34  ? 26.190 -7.275  11.742  1.00 17.63 ?  34  VAL   A HB   1 
ATOM   999  H HG11 . VAL   A 1 34  ? 27.548 -6.898  9.771   1.00 17.92 ?  34  VAL   A HG11 1 
ATOM   1000 H HG12 . VAL   A 1 34  ? 26.170 -6.112  9.823   1.00 17.92 ?  34  VAL   A HG12 1 
ATOM   1001 H HG13 . VAL   A 1 34  ? 27.527 -5.364  10.178  1.00 17.92 ?  34  VAL   A HG13 1 
ATOM   1002 H HG21 . VAL   A 1 34  ? 28.435 -7.942  11.670  1.00 19.75 ?  34  VAL   A HG21 1 
ATOM   1003 H HG22 . VAL   A 1 34  ? 28.854 -6.530  12.265  1.00 19.75 ?  34  VAL   A HG22 1 
ATOM   1004 H HG23 . VAL   A 1 34  ? 27.996 -7.538  13.142  1.00 19.75 ?  34  VAL   A HG23 1 
ATOM   1005 N N    . VAL   A 1 35  ? 25.214 -3.625  11.395  1.00 12.76 ?  35  VAL   A N    1 
ATOM   1006 C CA   . VAL   A 1 35  ? 24.185 -3.109  10.500  1.00 11.98 ?  35  VAL   A CA   1 
ATOM   1007 C C    . VAL   A 1 35  ? 24.741 -3.116  9.081   1.00 11.58 ?  35  VAL   A C    1 
ATOM   1008 O O    . VAL   A 1 35  ? 25.889 -2.713  8.856   1.00 12.58 ?  35  VAL   A O    1 
ATOM   1009 C CB   . VAL   A 1 35  ? 23.670 -1.709  10.912  1.00 12.87 ?  35  VAL   A CB   1 
ATOM   1010 C CG1  . VAL   A 1 35  ? 24.734 -0.627  10.782  1.00 13.48 ?  35  VAL   A CG1  1 
ATOM   1011 C CG2  . VAL   A 1 35  ? 22.439 -1.341  10.092  1.00 13.77 ?  35  VAL   A CG2  1 
ATOM   1012 H H    . VAL   A 1 35  ? 25.855 -3.069  11.525  1.00 15.31 ?  35  VAL   A H    1 
ATOM   1013 H HA   . VAL   A 1 35  ? 23.422 -3.713  10.522  1.00 14.38 ?  35  VAL   A HA   1 
ATOM   1014 H HB   . VAL   A 1 35  ? 23.392 -1.742  11.841  1.00 15.44 ?  35  VAL   A HB   1 
ATOM   1015 H HG11 . VAL   A 1 35  ? 24.387 0.202   11.150  1.00 16.18 ?  35  VAL   A HG11 1 
ATOM   1016 H HG12 . VAL   A 1 35  ? 25.521 -0.903  11.274  1.00 16.18 ?  35  VAL   A HG12 1 
ATOM   1017 H HG13 . VAL   A 1 35  ? 24.951 -0.506  9.845   1.00 16.18 ?  35  VAL   A HG13 1 
ATOM   1018 H HG21 . VAL   A 1 35  ? 22.095 -0.493  10.403  1.00 16.52 ?  35  VAL   A HG21 1 
ATOM   1019 H HG22 . VAL   A 1 35  ? 22.693 -1.275  9.157   1.00 16.52 ?  35  VAL   A HG22 1 
ATOM   1020 H HG23 . VAL   A 1 35  ? 21.768 -2.035  10.203  1.00 16.52 ?  35  VAL   A HG23 1 
ATOM   1021 N N    . VAL   A 1 36  ? 23.935 -3.586  8.128   1.00 10.92 ?  36  VAL   A N    1 
ATOM   1022 C CA   . VAL   A 1 36  ? 24.318 -3.602  6.719   1.00 10.94 ?  36  VAL   A CA   1 
ATOM   1023 C C    . VAL   A 1 36  ? 23.869 -2.304  6.055   1.00 11.19 ?  36  VAL   A C    1 
ATOM   1024 O O    . VAL   A 1 36  ? 22.709 -1.897  6.190   1.00 11.73 ?  36  VAL   A O    1 
ATOM   1025 C CB   . VAL   A 1 36  ? 23.718 -4.823  5.996   1.00 11.04 ?  36  VAL   A CB   1 
ATOM   1026 C CG1  . VAL   A 1 36  ? 23.988 -4.747  4.513   1.00 11.31 ?  36  VAL   A CG1  1 
ATOM   1027 C CG2  . VAL   A 1 36  ? 24.271 -6.120  6.577   1.00 11.97 ?  36  VAL   A CG2  1 
ATOM   1028 H H    . VAL   A 1 36  ? 23.142 -3.899  8.272   1.00 13.10 ?  36  VAL   A H    1 
ATOM   1029 H HA   . VAL   A 1 36  ? 25.287 -3.661  6.656   1.00 13.13 ?  36  VAL   A HA   1 
ATOM   1030 H HB   . VAL   A 1 36  ? 22.757 -4.820  6.126   1.00 13.25 ?  36  VAL   A HB   1 
ATOM   1031 H HG11 . VAL   A 1 36  ? 23.841 -5.621  4.122   1.00 13.57 ?  36  VAL   A HG11 1 
ATOM   1032 H HG12 . VAL   A 1 36  ? 23.384 -4.100  4.111   1.00 13.57 ?  36  VAL   A HG12 1 
ATOM   1033 H HG13 . VAL   A 1 36  ? 24.907 -4.472  4.374   1.00 13.57 ?  36  VAL   A HG13 1 
ATOM   1034 H HG21 . VAL   A 1 36  ? 23.877 -6.875  6.103   1.00 14.37 ?  36  VAL   A HG21 1 
ATOM   1035 H HG22 . VAL   A 1 36  ? 25.236 -6.134  6.465   1.00 14.37 ?  36  VAL   A HG22 1 
ATOM   1036 H HG23 . VAL   A 1 36  ? 24.047 -6.176  7.519   1.00 14.37 ?  36  VAL   A HG23 1 
ATOM   1037 N N    . ASN   A 1 37  ? 24.786 -1.665  5.331   1.00 10.32 ?  37  ASN   A N    1 
ATOM   1038 C CA   . ASN   A 1 37  ? 24.455 -0.554  4.457   1.00 10.27 ?  37  ASN   A CA   1 
ATOM   1039 C C    . ASN   A 1 37  ? 24.326 -1.037  3.021   1.00 10.33 ?  37  ASN   A C    1 
ATOM   1040 O O    . ASN   A 1 37  ? 25.123 -1.858  2.550   1.00 10.82 ?  37  ASN   A O    1 
ATOM   1041 C CB   . ASN   A 1 37  ? 25.535 0.522   4.531   1.00 10.62 ?  37  ASN   A CB   1 
ATOM   1042 C CG   . ASN   A 1 37  ? 25.211 1.712   3.676   1.00 10.86 ?  37  ASN   A CG   1 
ATOM   1043 O OD1  . ASN   A 1 37  ? 24.033 2.054   3.492   1.00 11.53 ?  37  ASN   A OD1  1 
ATOM   1044 N ND2  . ASN   A 1 37  ? 26.242 2.363   3.149   1.00 11.12 ?  37  ASN   A ND2  1 
ATOM   1045 H H    . ASN   A 1 37  ? 25.622 -1.856  5.341   1.00 12.38 ?  37  ASN   A H    1 
ATOM   1046 H HA   . ASN   A 1 37  ? 23.612 -0.154  4.733   1.00 12.32 ?  37  ASN   A HA   1 
ATOM   1047 H HB2  . ASN   A 1 37  ? 25.629 0.821   5.446   1.00 12.75 ?  37  ASN   A HB2  1 
ATOM   1048 H HB3  . ASN   A 1 37  ? 26.378 0.141   4.218   1.00 12.75 ?  37  ASN   A HB3  1 
ATOM   1049 H HD21 . ASN   A 1 37  ? 26.103 3.051   2.649   1.00 13.34 ?  37  ASN   A HD21 1 
ATOM   1050 H HD22 . ASN   A 1 37  ? 27.041 2.100   3.294   1.00 13.34 ?  37  ASN   A HD22 1 
ATOM   1051 N N    A ALA   A 1 38  ? 23.321 -0.500  2.325   0.80 10.61 ?  38  ALA   A N    1 
ATOM   1052 N N    B ALA   A 1 38  ? 23.311 -0.530  2.320   0.20 10.56 ?  38  ALA   A N    1 
ATOM   1053 C CA   A ALA   A 1 38  ? 23.143 -0.663  0.884   0.80 10.53 ?  38  ALA   A CA   1 
ATOM   1054 C CA   B ALA   A 1 38  ? 23.145 -0.804  0.893   0.20 11.01 ?  38  ALA   A CA   1 
ATOM   1055 C C    A ALA   A 1 38  ? 24.051 0.339   0.173   0.80 10.63 ?  38  ALA   A C    1 
ATOM   1056 C C    B ALA   A 1 38  ? 23.905 0.270   0.118   0.20 11.25 ?  38  ALA   A C    1 
ATOM   1057 O O    A ALA   A 1 38  ? 23.639 1.425   -0.241  0.80 10.68 ?  38  ALA   A O    1 
ATOM   1058 O O    B ALA   A 1 38  ? 23.352 1.273   -0.337  0.20 11.23 ?  38  ALA   A O    1 
ATOM   1059 C CB   A ALA   A 1 38  ? 21.675 -0.454  0.513   0.80 11.84 ?  38  ALA   A CB   1 
ATOM   1060 C CB   B ALA   A 1 38  ? 21.667 -0.842  0.522   0.20 11.39 ?  38  ALA   A CB   1 
ATOM   1061 H H    A ALA   A 1 38  ? 22.714 -0.005  2.683   0.80 12.73 ?  38  ALA   A H    1 
ATOM   1062 H H    B ALA   A 1 38  ? 22.701 -0.020  2.655   0.20 12.67 ?  38  ALA   A H    1 
ATOM   1063 H HA   A ALA   A 1 38  ? 23.402 -1.563  0.623   0.80 12.64 ?  38  ALA   A HA   1 
ATOM   1064 H HA   B ALA   A 1 38  ? 23.533 -1.672  0.687   0.20 13.21 ?  38  ALA   A HA   1 
ATOM   1065 H HB1  A ALA   A 1 38  ? 21.568 -0.572  -0.444  0.80 14.20 ?  38  ALA   A HB1  1 
ATOM   1066 H HB1  B ALA   A 1 38  ? 21.590 -0.984  -0.434  0.20 13.67 ?  38  ALA   A HB1  1 
ATOM   1067 H HB2  A ALA   A 1 38  ? 21.131 -1.107  0.986   0.80 14.20 ?  38  ALA   A HB2  1 
ATOM   1068 H HB2  B ALA   A 1 38  ? 21.234 -1.566  1.001   0.20 13.67 ?  38  ALA   A HB2  1 
ATOM   1069 H HB3  A ALA   A 1 38  ? 21.408 0.442   0.768   0.80 14.20 ?  38  ALA   A HB3  1 
ATOM   1070 H HB3  B ALA   A 1 38  ? 21.262 0.006   0.763   0.20 13.67 ?  38  ALA   A HB3  1 
ATOM   1071 N N    A ALA   A 1 39  ? 25.319 -0.034  0.051   0.80 10.43 ?  39  ALA   A N    1 
ATOM   1072 N N    B ALA   A 1 39  ? 25.205 0.044   -0.033  0.20 11.59 ?  39  ALA   A N    1 
ATOM   1073 C CA   A ALA   A 1 39  ? 26.357 0.848   -0.451  0.80 10.30 ?  39  ALA   A CA   1 
ATOM   1074 C CA   B ALA   A 1 39  ? 26.121 1.054   -0.538  0.20 11.95 ?  39  ALA   A CA   1 
ATOM   1075 C C    A ALA   A 1 39  ? 26.468 0.793   -1.972  0.80 10.23 ?  39  ALA   A C    1 
ATOM   1076 C C    B ALA   A 1 39  ? 26.412 0.849   -2.020  0.20 11.64 ?  39  ALA   A C    1 
ATOM   1077 O O    A ALA   A 1 39  ? 25.960 -0.120  -2.634  0.80 10.79 ?  39  ALA   A O    1 
ATOM   1078 O O    B ALA   A 1 39  ? 26.043 -0.160  -2.629  0.20 11.70 ?  39  ALA   A O    1 
ATOM   1079 C CB   A ALA   A 1 39  ? 27.696 0.472   0.186   0.80 10.54 ?  39  ALA   A CB   1 
ATOM   1080 C CB   B ALA   A 1 39  ? 27.431 1.016   0.253   0.20 12.64 ?  39  ALA   A CB   1 
ATOM   1081 H H    A ALA   A 1 39  ? 25.604 -0.823  0.261   0.80 12.51 ?  39  ALA   A H    1 
ATOM   1082 H H    B ALA   A 1 39  ? 25.587 -0.707  0.147   0.20 13.91 ?  39  ALA   A H    1 
ATOM   1083 H HA   A ALA   A 1 39  ? 26.141 1.757   -0.191  0.80 12.36 ?  39  ALA   A HA   1 
ATOM   1084 H HA   B ALA   A 1 39  ? 25.722 1.928   -0.422  0.20 14.34 ?  39  ALA   A HA   1 
ATOM   1085 H HB1  A ALA   A 1 39  ? 28.381 1.072   -0.150  0.80 12.65 ?  39  ALA   A HB1  1 
ATOM   1086 H HB1  B ALA   A 1 39  ? 28.009 1.728   -0.063  0.20 15.17 ?  39  ALA   A HB1  1 
ATOM   1087 H HB2  A ALA   A 1 39  ? 27.625 0.566   1.153   0.80 12.65 ?  39  ALA   A HB2  1 
ATOM   1088 H HB2  B ALA   A 1 39  ? 27.237 1.139   1.194   0.20 15.17 ?  39  ALA   A HB2  1 
ATOM   1089 H HB3  A ALA   A 1 39  ? 27.912 -0.442  -0.041  0.80 12.65 ?  39  ALA   A HB3  1 
ATOM   1090 H HB3  B ALA   A 1 39  ? 27.858 0.156   0.116   0.20 15.17 ?  39  ALA   A HB3  1 
ATOM   1091 N N    A ASN   A 1 40  ? 27.139 1.804   -2.523  0.80 11.02 ?  40  ASN   A N    1 
ATOM   1092 N N    B ASN   A 1 40  ? 27.086 1.838   -2.598  0.20 11.62 ?  40  ASN   A N    1 
ATOM   1093 C CA   A ASN   A 1 40  ? 27.679 1.762   -3.877  0.80 11.43 ?  40  ASN   A CA   1 
ATOM   1094 C CA   B ASN   A 1 40  ? 27.666 1.742   -3.928  0.20 11.62 ?  40  ASN   A CA   1 
ATOM   1095 C C    A ASN   A 1 40  ? 29.202 1.632   -3.810  0.80 10.82 ?  40  ASN   A C    1 
ATOM   1096 C C    B ASN   A 1 40  ? 29.181 1.598   -3.816  0.20 11.30 ?  40  ASN   A C    1 
ATOM   1097 O O    A ASN   A 1 40  ? 29.803 1.726   -2.739  0.80 11.14 ?  40  ASN   A O    1 
ATOM   1098 O O    B ASN   A 1 40  ? 29.762 1.690   -2.731  0.20 11.19 ?  40  ASN   A O    1 
ATOM   1099 C CB   A ASN   A 1 40  ? 27.201 2.956   -4.726  0.80 12.06 ?  40  ASN   A CB   1 
ATOM   1100 C CB   B ASN   A 1 40  ? 27.286 2.952   -4.795  0.20 11.80 ?  40  ASN   A CB   1 
ATOM   1101 C CG   A ASN   A 1 40  ? 27.603 4.298   -4.156  0.80 13.02 ?  40  ASN   A CG   1 
ATOM   1102 C CG   B ASN   A 1 40  ? 27.554 4.277   -4.109  0.20 12.17 ?  40  ASN   A CG   1 
ATOM   1103 O OD1  A ASN   A 1 40  ? 28.776 4.533   -3.849  0.80 13.32 ?  40  ASN   A OD1  1 
ATOM   1104 O OD1  B ASN   A 1 40  ? 28.704 4.644   -3.867  0.20 12.20 ?  40  ASN   A OD1  1 
ATOM   1105 N ND2  A ASN   A 1 40  ? 26.623 5.188   -4.009  0.80 13.93 ?  40  ASN   A ND2  1 
ATOM   1106 N ND2  B ASN   A 1 40  ? 26.488 5.010   -3.806  0.20 12.45 ?  40  ASN   A ND2  1 
ATOM   1107 H H    A ASN   A 1 40  ? 27.306 2.541   -2.114  0.80 13.22 ?  40  ASN   A H    1 
ATOM   1108 H H    B ASN   A 1 40  ? 27.226 2.596   -2.220  0.20 13.95 ?  40  ASN   A H    1 
ATOM   1109 H HA   A ASN   A 1 40  ? 27.349 0.955   -4.305  0.80 13.72 ?  40  ASN   A HA   1 
ATOM   1110 H HA   B ASN   A 1 40  ? 27.322 0.944   -4.361  0.20 13.95 ?  40  ASN   A HA   1 
ATOM   1111 H HB2  A ASN   A 1 40  ? 27.578 2.874   -5.615  0.80 14.47 ?  40  ASN   A HB2  1 
ATOM   1112 H HB2  B ASN   A 1 40  ? 27.805 2.926   -5.613  0.20 14.16 ?  40  ASN   A HB2  1 
ATOM   1113 H HB3  A ASN   A 1 40  ? 26.230 2.927   -4.778  0.80 14.47 ?  40  ASN   A HB3  1 
ATOM   1114 H HB3  B ASN   A 1 40  ? 26.339 2.904   -5.000  0.20 14.16 ?  40  ASN   A HB3  1 
ATOM   1115 H HD21 A ASN   A 1 40  ? 26.796 5.969   -3.691  0.80 16.71 ?  40  ASN   A HD21 1 
ATOM   1116 H HD21 B ASN   A 1 40  ? 26.588 5.771   -3.419  0.20 14.94 ?  40  ASN   A HD21 1 
ATOM   1117 H HD22 A ASN   A 1 40  ? 25.818 4.982   -4.227  0.80 16.71 ?  40  ASN   A HD22 1 
ATOM   1118 H HD22 B ASN   A 1 40  ? 25.700 4.723   -3.997  0.20 14.94 ?  40  ASN   A HD22 1 
ATOM   1119 N N    . VAL   A 1 41  ? 29.817 1.357   -4.964  1.00 11.61 ?  41  VAL   A N    1 
ATOM   1120 C CA   . VAL   A 1 41  ? 31.248 1.054   -4.989  1.00 11.76 ?  41  VAL   A CA   1 
ATOM   1121 C C    . VAL   A 1 41  ? 32.111 2.205   -4.506  1.00 11.84 ?  41  VAL   A C    1 
ATOM   1122 O O    . VAL   A 1 41  ? 33.252 1.976   -4.091  1.00 12.43 ?  41  VAL   A O    1 
ATOM   1123 C CB   . VAL   A 1 41  ? 31.740 0.570   -6.374  1.00 12.77 ?  41  VAL   A CB   1 
ATOM   1124 C CG1  . VAL   A 1 41  ? 31.040 -0.722  -6.788  1.00 13.96 ?  41  VAL   A CG1  1 
ATOM   1125 C CG2  . VAL   A 1 41  ? 31.605 1.651   -7.441  1.00 13.75 ?  41  VAL   A CG2  1 
ATOM   1126 H H    A VAL   A 1 41  ? 29.428 1.316   -5.728  0.80 13.93 ?  41  VAL   A H    1 
ATOM   1127 H H    B VAL   A 1 41  ? 29.439 1.347   -5.733  0.20 13.93 ?  41  VAL   A H    1 
ATOM   1128 H HA   . VAL   A 1 41  ? 31.407 0.316   -4.377  1.00 14.11 ?  41  VAL   A HA   1 
ATOM   1129 H HB   . VAL   A 1 41  ? 32.686 0.359   -6.306  1.00 15.32 ?  41  VAL   A HB   1 
ATOM   1130 H HG11 . VAL   A 1 41  ? 31.377 -1.008  -7.655  1.00 16.75 ?  41  VAL   A HG11 1 
ATOM   1131 H HG12 . VAL   A 1 41  ? 31.217 -1.407  -6.125  1.00 16.75 ?  41  VAL   A HG12 1 
ATOM   1132 H HG13 . VAL   A 1 41  ? 30.084 -0.560  -6.848  1.00 16.75 ?  41  VAL   A HG13 1 
ATOM   1133 H HG21 . VAL   A 1 41  ? 31.831 1.274   -8.310  1.00 16.50 ?  41  VAL   A HG21 1 
ATOM   1134 H HG22 . VAL   A 1 41  ? 30.695 1.978   -7.451  1.00 16.50 ?  41  VAL   A HG22 1 
ATOM   1135 H HG23 . VAL   A 1 41  ? 32.218 2.377   -7.235  1.00 16.50 ?  41  VAL   A HG23 1 
ATOM   1136 N N    . TYR   A 1 42  ? 31.609 3.442   -4.572  1.00 11.68 ?  42  TYR   A N    1 
ATOM   1137 C CA   . TYR   A 1 42  ? 32.345 4.630   -4.158  1.00 11.80 ?  42  TYR   A CA   1 
ATOM   1138 C C    . TYR   A 1 42  ? 32.090 5.000   -2.706  1.00 11.09 ?  42  TYR   A C    1 
ATOM   1139 O O    . TYR   A 1 42  ? 32.658 5.986   -2.220  1.00 12.05 ?  42  TYR   A O    1 
ATOM   1140 C CB   . TYR   A 1 42  ? 31.985 5.817   -5.070  1.00 12.36 ?  42  TYR   A CB   1 
ATOM   1141 C CG   . TYR   A 1 42  ? 32.167 5.500   -6.539  1.00 12.83 ?  42  TYR   A CG   1 
ATOM   1142 C CD1  . TYR   A 1 42  ? 33.430 5.297   -7.072  1.00 13.62 ?  42  TYR   A CD1  1 
ATOM   1143 C CD2  . TYR   A 1 42  ? 31.073 5.376   -7.390  1.00 14.60 ?  42  TYR   A CD2  1 
ATOM   1144 C CE1  . TYR   A 1 42  ? 33.601 4.983   -8.409  1.00 14.58 ?  42  TYR   A CE1  1 
ATOM   1145 C CE2  . TYR   A 1 42  ? 31.240 5.082   -8.734  1.00 15.92 ?  42  TYR   A CE2  1 
ATOM   1146 C CZ   . TYR   A 1 42  ? 32.506 4.879   -9.236  1.00 15.66 ?  42  TYR   A CZ   1 
ATOM   1147 O OH   . TYR   A 1 42  ? 32.671 4.578   -10.565 1.00 17.31 ?  42  TYR   A OH   1 
ATOM   1148 H H    . TYR   A 1 42  ? 30.813 3.612   -4.860  1.00 14.02 ?  42  TYR   A H    1 
ATOM   1149 H HA   . TYR   A 1 42  ? 33.289 4.460   -4.261  1.00 14.16 ?  42  TYR   A HA   1 
ATOM   1150 H HB2  . TYR   A 1 42  ? 31.049 6.057   -4.922  1.00 14.83 ?  42  TYR   A HB2  1 
ATOM   1151 H HB3  . TYR   A 1 42  ? 32.552 6.570   -4.848  1.00 14.83 ?  42  TYR   A HB3  1 
ATOM   1152 H HD1  . TYR   A 1 42  ? 34.171 5.359   -6.514  1.00 16.35 ?  42  TYR   A HD1  1 
ATOM   1153 H HD2  . TYR   A 1 42  ? 30.212 5.516   -7.054  1.00 17.53 ?  42  TYR   A HD2  1 
ATOM   1154 H HE1  . TYR   A 1 42  ? 34.453 4.851   -8.748  1.00 17.49 ?  42  TYR   A HE1  1 
ATOM   1155 H HE2  . TYR   A 1 42  ? 30.495 5.008   -9.291  1.00 19.10 ?  42  TYR   A HE2  1 
ATOM   1156 H HH   . TYR   A 1 42  ? 33.489 4.473   -10.736 1.00 20.77 ?  42  TYR   A HH   1 
ATOM   1157 N N    . LEU   A 1 43  ? 31.235 4.248   -2.020  1.00 10.80 ?  43  LEU   A N    1 
ATOM   1158 C CA   . LEU   A 1 43  ? 30.784 4.590   -0.677  1.00 10.51 ?  43  LEU   A CA   1 
ATOM   1159 C C    . LEU   A 1 43  ? 30.305 6.040   -0.589  1.00 10.88 ?  43  LEU   A C    1 
ATOM   1160 O O    . LEU   A 1 43  ? 30.566 6.747   0.390   1.00 12.35 ?  43  LEU   A O    1 
ATOM   1161 C CB   . LEU   A 1 43  ? 31.826 4.275   0.391   1.00 11.58 ?  43  LEU   A CB   1 
ATOM   1162 C CG   . LEU   A 1 43  ? 32.334 2.827   0.471   1.00 11.93 ?  43  LEU   A CG   1 
ATOM   1163 C CD1  . LEU   A 1 43  ? 33.359 2.722   1.580   1.00 12.88 ?  43  LEU   A CD1  1 
ATOM   1164 C CD2  . LEU   A 1 43  ? 31.188 1.853   0.713   1.00 12.47 ?  43  LEU   A CD2  1 
ATOM   1165 H H    . LEU   A 1 43  ? 30.895 3.507   -2.316  1.00 12.96 ?  43  LEU   A H    1 
ATOM   1166 H HA   . LEU   A 1 43  ? 30.009 4.032   -0.480  1.00 12.62 ?  43  LEU   A HA   1 
ATOM   1167 H HB2  . LEU   A 1 43  ? 32.592 4.845   0.242   1.00 13.90 ?  43  LEU   A HB2  1 
ATOM   1168 H HB3  . LEU   A 1 43  ? 31.436 4.482   1.258   1.00 13.90 ?  43  LEU   A HB3  1 
ATOM   1169 H HG   . LEU   A 1 43  ? 32.769 2.598   -0.368  1.00 14.32 ?  43  LEU   A HG   1 
ATOM   1170 H HD11 . LEU   A 1 43  ? 33.683 1.809   1.625   1.00 15.45 ?  43  LEU   A HD11 1 
ATOM   1171 H HD12 . LEU   A 1 43  ? 34.096 3.326   1.392   1.00 15.45 ?  43  LEU   A HD12 1 
ATOM   1172 H HD13 . LEU   A 1 43  ? 32.939 2.966   2.421   1.00 15.45 ?  43  LEU   A HD13 1 
ATOM   1173 H HD21 . LEU   A 1 43  ? 31.557 0.967   0.853   1.00 14.97 ?  43  LEU   A HD21 1 
ATOM   1174 H HD22 . LEU   A 1 43  ? 30.696 2.137   1.496   1.00 14.97 ?  43  LEU   A HD22 1 
ATOM   1175 H HD23 . LEU   A 1 43  ? 30.609 1.852   -0.064  1.00 14.97 ?  43  LEU   A HD23 1 
ATOM   1176 N N    A LYS   A 1 44  ? 29.592 6.481   -1.622  0.80 11.16 ?  44  LYS   A N    1 
ATOM   1177 N N    B LYS   A 1 44  ? 29.574 6.478   -1.614  0.20 12.24 ?  44  LYS   A N    1 
ATOM   1178 C CA   A LYS   A 1 44  ? 28.957 7.792   -1.622  0.80 11.29 ?  44  LYS   A CA   1 
ATOM   1179 C CA   B LYS   A 1 44  ? 28.922 7.786   -1.609  0.20 13.65 ?  44  LYS   A CA   1 
ATOM   1180 C C    A LYS   A 1 44  ? 27.525 7.612   -1.133  0.80 9.93  ?  44  LYS   A C    1 
ATOM   1181 C C    B LYS   A 1 44  ? 27.494 7.583   -1.123  0.20 12.99 ?  44  LYS   A C    1 
ATOM   1182 O O    A LYS   A 1 44  ? 26.671 7.082   -1.854  0.80 11.86 ?  44  LYS   A O    1 
ATOM   1183 O O    B LYS   A 1 44  ? 26.632 7.102   -1.862  0.20 13.31 ?  44  LYS   A O    1 
ATOM   1184 C CB   A LYS   A 1 44  ? 29.007 8.411   -3.012  0.80 13.73 ?  44  LYS   A CB   1 
ATOM   1185 C CB   B LYS   A 1 44  ? 28.963 8.426   -2.993  0.20 15.90 ?  44  LYS   A CB   1 
ATOM   1186 C CG   A LYS   A 1 44  ? 30.387 8.879   -3.432  0.80 17.41 ?  44  LYS   A CG   1 
ATOM   1187 C CG   B LYS   A 1 44  ? 30.336 8.935   -3.401  0.20 18.25 ?  44  LYS   A CG   1 
ATOM   1188 C CD   A LYS   A 1 44  ? 31.040 9.783   -2.392  0.80 22.76 ?  44  LYS   A CD   1 
ATOM   1189 C CD   B LYS   A 1 44  ? 30.911 9.889   -2.362  0.20 20.81 ?  44  LYS   A CD   1 
ATOM   1190 C CE   A LYS   A 1 44  ? 32.362 10.336  -2.892  0.80 26.25 ?  44  LYS   A CE   1 
ATOM   1191 C CE   B LYS   A 1 44  ? 32.255 10.438  -2.797  0.20 22.61 ?  44  LYS   A CE   1 
ATOM   1192 N NZ   A LYS   A 1 44  ? 33.198 10.838  -1.769  0.80 27.92 ?  44  LYS   A NZ   1 
ATOM   1193 N NZ   B LYS   A 1 44  ? 33.020 11.007  -1.654  0.20 23.61 ?  44  LYS   A NZ   1 
ATOM   1194 H H    A LYS   A 1 44  ? 29.460 6.028   -2.344  0.80 13.39 ?  44  LYS   A H    1 
ATOM   1195 H H    B LYS   A 1 44  ? 29.432 6.029   -2.333  0.20 14.69 ?  44  LYS   A H    1 
ATOM   1196 H HA   A LYS   A 1 44  ? 29.407 8.369   -0.988  0.80 13.55 ?  44  LYS   A HA   1 
ATOM   1197 H HA   B LYS   A 1 44  ? 29.359 8.367   -0.971  0.20 16.38 ?  44  LYS   A HA   1 
ATOM   1198 H HB2  A LYS   A 1 44  ? 28.705 7.758   -3.658  0.80 16.48 ?  44  LYS   A HB2  1 
ATOM   1199 H HB2  B LYS   A 1 44  ? 28.683 7.771   -3.651  0.20 19.08 ?  44  LYS   A HB2  1 
ATOM   1200 H HB3  A LYS   A 1 44  ? 28.417 9.185   -3.027  0.80 16.48 ?  44  LYS   A HB3  1 
ATOM   1201 H HB3  B LYS   A 1 44  ? 28.354 9.184   -3.008  0.20 19.08 ?  44  LYS   A HB3  1 
ATOM   1202 H HG2  A LYS   A 1 44  ? 30.960 8.107   -3.561  0.80 20.90 ?  44  LYS   A HG2  1 
ATOM   1203 H HG2  B LYS   A 1 44  ? 30.940 8.182   -3.493  0.20 21.90 ?  44  LYS   A HG2  1 
ATOM   1204 H HG3  A LYS   A 1 44  ? 30.317 9.383   -4.260  0.80 20.90 ?  44  LYS   A HG3  1 
ATOM   1205 H HG3  B LYS   A 1 44  ? 30.263 9.411   -4.245  0.20 21.90 ?  44  LYS   A HG3  1 
ATOM   1206 H HD2  A LYS   A 1 44  ? 30.445 10.523  -2.192  0.80 27.31 ?  44  LYS   A HD2  1 
ATOM   1207 H HD2  B LYS   A 1 44  ? 30.294 10.628  -2.232  0.20 24.98 ?  44  LYS   A HD2  1 
ATOM   1208 H HD3  A LYS   A 1 44  ? 31.220 9.269   -1.587  0.80 27.31 ?  44  LYS   A HD3  1 
ATOM   1209 H HD3  B LYS   A 1 44  ? 31.048 9.415   -1.527  0.20 24.98 ?  44  LYS   A HD3  1 
ATOM   1210 H HE2  A LYS   A 1 44  ? 32.853 9.631   -3.343  0.80 31.51 ?  44  LYS   A HE2  1 
ATOM   1211 H HE2  B LYS   A 1 44  ? 32.779 9.720   -3.185  0.20 27.13 ?  44  LYS   A HE2  1 
ATOM   1212 H HE3  A LYS   A 1 44  ? 32.192 11.071  -3.499  0.80 31.51 ?  44  LYS   A HE3  1 
ATOM   1213 H HE3  B LYS   A 1 44  ? 32.114 11.141  -3.448  0.20 27.13 ?  44  LYS   A HE3  1 
ATOM   1214 H HZ1  A LYS   A 1 44  ? 33.966 11.158  -2.081  0.80 33.51 ?  44  LYS   A HZ1  1 
ATOM   1215 H HZ1  B LYS   A 1 44  ? 33.803 11.320  -1.938  0.20 28.33 ?  44  LYS   A HZ1  1 
ATOM   1216 H HZ2  A LYS   A 1 44  ? 32.766 11.488  -1.338  0.80 33.51 ?  44  LYS   A HZ2  1 
ATOM   1217 H HZ2  B LYS   A 1 44  ? 32.561 11.671  -1.280  0.20 28.33 ?  44  LYS   A HZ2  1 
ATOM   1218 H HZ3  A LYS   A 1 44  ? 33.368 10.178  -1.197  0.80 33.51 ?  44  LYS   A HZ3  1 
ATOM   1219 H HZ3  B LYS   A 1 44  ? 33.166 10.377  -1.041  0.20 28.33 ?  44  LYS   A HZ3  1 
ATOM   1220 N N    A HIS   A 1 45  ? 27.275 8.016   0.110   0.80 10.24 ?  45  HIS   A N    1 
ATOM   1221 N N    B HIS   A 1 45  ? 27.248 7.947   0.133   0.20 12.58 ?  45  HIS   A N    1 
ATOM   1222 C CA   A HIS   A 1 45  ? 26.040 7.666   0.810   0.80 10.57 ?  45  HIS   A CA   1 
ATOM   1223 C CA   B HIS   A 1 45  ? 25.960 7.711   0.778   0.20 12.20 ?  45  HIS   A CA   1 
ATOM   1224 C C    A HIS   A 1 45  ? 25.001 8.778   0.642   0.80 11.44 ?  45  HIS   A C    1 
ATOM   1225 C C    B HIS   A 1 45  ? 25.098 8.943   0.547   0.20 12.23 ?  45  HIS   A C    1 
ATOM   1226 O O    A HIS   A 1 45  ? 24.679 9.531   1.565   0.80 12.86 ?  45  HIS   A O    1 
ATOM   1227 O O    B HIS   A 1 45  ? 25.127 9.904   1.319   0.20 12.13 ?  45  HIS   A O    1 
ATOM   1228 C CB   A HIS   A 1 45  ? 26.343 7.401   2.276   0.80 10.45 ?  45  HIS   A CB   1 
ATOM   1229 C CB   B HIS   A 1 45  ? 26.168 7.436   2.259   0.20 11.92 ?  45  HIS   A CB   1 
ATOM   1230 C CG   A HIS   A 1 45  ? 27.459 6.432   2.497   0.80 10.40 ?  45  HIS   A CG   1 
ATOM   1231 C CG   B HIS   A 1 45  ? 27.305 6.507   2.537   0.20 11.09 ?  45  HIS   A CG   1 
ATOM   1232 N ND1  A HIS   A 1 45  ? 27.453 5.146   1.992   0.80 11.30 ?  45  HIS   A ND1  1 
ATOM   1233 N ND1  B HIS   A 1 45  ? 27.356 5.224   2.036   0.20 10.90 ?  45  HIS   A ND1  1 
ATOM   1234 C CD2  A HIS   A 1 45  ? 28.626 6.573   3.169   0.80 10.78 ?  45  HIS   A CD2  1 
ATOM   1235 C CD2  B HIS   A 1 45  ? 28.442 6.681   3.251   0.20 10.91 ?  45  HIS   A CD2  1 
ATOM   1236 C CE1  A HIS   A 1 45  ? 28.573 4.543   2.353   0.80 11.11 ?  45  HIS   A CE1  1 
ATOM   1237 C CE1  B HIS   A 1 45  ? 28.475 4.646   2.438   0.20 10.33 ?  45  HIS   A CE1  1 
ATOM   1238 N NE2  A HIS   A 1 45  ? 29.299 5.383   3.069   0.80 11.06 ?  45  HIS   A NE2  1 
ATOM   1239 N NE2  B HIS   A 1 45  ? 29.150 5.507   3.178   0.20 10.55 ?  45  HIS   A NE2  1 
ATOM   1240 H H    A HIS   A 1 45  ? 27.802 8.516   0.570   0.80 12.28 ?  45  HIS   A H    1 
ATOM   1241 H H    B HIS   A 1 45  ? 27.818 8.350   0.639   0.20 15.10 ?  45  HIS   A H    1 
ATOM   1242 H HA   A HIS   A 1 45  ? 25.675 6.856   0.424   0.80 12.68 ?  45  HIS   A HA   1 
ATOM   1243 H HA   B HIS   A 1 45  ? 25.527 6.938   0.376   0.20 14.64 ?  45  HIS   A HA   1 
ATOM   1244 H HB2  A HIS   A 1 45  ? 26.581 8.237   2.704   0.80 12.54 ?  45  HIS   A HB2  1 
ATOM   1245 H HB2  B HIS   A 1 45  ? 26.353 8.274   2.710   0.20 14.31 ?  45  HIS   A HB2  1 
ATOM   1246 H HB3  A HIS   A 1 45  ? 25.544 7.036   2.697   0.80 12.54 ?  45  HIS   A HB3  1 
ATOM   1247 H HB3  B HIS   A 1 45  ? 25.364 7.036   2.623   0.20 14.31 ?  45  HIS   A HB3  1 
ATOM   1248 H HD2  A HIS   A 1 45  ? 28.917 7.337   3.614   0.80 12.94 ?  45  HIS   A HD2  1 
ATOM   1249 H HD2  B HIS   A 1 45  ? 28.694 7.452   3.709   0.20 13.09 ?  45  HIS   A HD2  1 
ATOM   1250 H HE1  A HIS   A 1 45  ? 28.806 3.666   2.146   0.80 13.34 ?  45  HIS   A HE1  1 
ATOM   1251 H HE1  B HIS   A 1 45  ? 28.740 3.778   2.236   0.20 12.40 ?  45  HIS   A HE1  1 
ATOM   1252 H HE2  A HIS   A 1 45  ? 30.071 5.214   3.409   0.80 13.27 ?  45  HIS   A HE2  1 
ATOM   1253 H HE2  B HIS   A 1 45  ? 29.911 5.359   3.548   0.20 12.66 ?  45  HIS   A HE2  1 
ATOM   1254 N N    A GLY   A 1 46  ? 24.437 8.842   -0.564  0.80 13.12 ?  46  GLY   A N    1 
ATOM   1255 N N    B GLY   A 1 46  ? 24.334 8.923   -0.541  0.20 12.79 ?  46  GLY   A N    1 
ATOM   1256 C CA   A GLY   A 1 46  ? 23.600 9.974   -0.921  0.80 13.94 ?  46  GLY   A CA   1 
ATOM   1257 C CA   B GLY   A 1 46  ? 23.493 10.054  -0.879  0.20 12.86 ?  46  GLY   A CA   1 
ATOM   1258 C C    A GLY   A 1 46  ? 22.116 9.820   -0.664  0.80 14.08 ?  46  GLY   A C    1 
ATOM   1259 C C    B GLY   A 1 46  ? 22.051 9.912   -0.429  0.20 12.67 ?  46  GLY   A C    1 
ATOM   1260 O O    A GLY   A 1 46  ? 21.441 10.798  -0.329  0.80 15.24 ?  46  GLY   A O    1 
ATOM   1261 O O    B GLY   A 1 46  ? 21.470 10.859  0.110   0.20 13.08 ?  46  GLY   A O    1 
ATOM   1262 H H    A GLY   A 1 46  ? 24.513 8.242   -1.175  0.80 15.74 ?  46  GLY   A H    1 
ATOM   1263 H H    B GLY   A 1 46  ? 24.300 8.269   -1.104  0.20 15.35 ?  46  GLY   A H    1 
ATOM   1264 H HA2  A GLY   A 1 46  ? 23.900 10.752  -0.426  0.80 16.72 ?  46  GLY   A HA2  1 
ATOM   1265 H HA2  B GLY   A 1 46  ? 23.861 10.854  -0.468  0.20 15.43 ?  46  GLY   A HA2  1 
ATOM   1266 H HA3  A GLY   A 1 46  ? 23.703 10.155  -1.861  0.80 16.72 ?  46  GLY   A HA3  1 
ATOM   1267 H HA3  B GLY   A 1 46  ? 23.506 10.178  -1.839  0.20 15.43 ?  46  GLY   A HA3  1 
ATOM   1268 N N    A GLY   A 1 47  ? 21.587 8.616   -0.839  0.80 13.78 ?  47  GLY   A N    1 
ATOM   1269 N N    B GLY   A 1 47  ? 21.461 8.738   -0.640  0.20 12.38 ?  47  GLY   A N    1 
ATOM   1270 C CA   A GLY   A 1 47  ? 20.156 8.414   -0.797  0.80 13.89 ?  47  GLY   A CA   1 
ATOM   1271 C CA   B GLY   A 1 47  ? 20.058 8.530   -0.347  0.20 12.46 ?  47  GLY   A CA   1 
ATOM   1272 C C    A GLY   A 1 47  ? 19.824 6.995   -0.394  0.80 13.33 ?  47  GLY   A C    1 
ATOM   1273 C C    B GLY   A 1 47  ? 19.768 7.090   0.024   0.20 11.87 ?  47  GLY   A C    1 
ATOM   1274 O O    A GLY   A 1 47  ? 20.706 6.171   -0.145  0.80 13.64 ?  47  GLY   A O    1 
ATOM   1275 O O    B GLY   A 1 47  ? 20.672 6.259   0.138   0.20 11.43 ?  47  GLY   A O    1 
ATOM   1276 H H    A GLY   A 1 47  ? 22.034 7.894   -0.969  0.80 16.53 ?  47  GLY   A H    1 
ATOM   1277 H H    B GLY   A 1 47  ? 21.864 8.048   -0.949  0.20 14.85 ?  47  GLY   A H    1 
ATOM   1278 H HA2  A GLY   A 1 47  ? 19.743 9.029   -0.164  0.80 16.66 ?  47  GLY   A HA2  1 
ATOM   1279 H HA2  B GLY   A 1 47  ? 19.791 9.099   0.392   0.20 14.95 ?  47  GLY   A HA2  1 
ATOM   1280 H HA3  A GLY   A 1 47  ? 19.775 8.581   -1.677  0.80 16.66 ?  47  GLY   A HA3  1 
ATOM   1281 H HA3  B GLY   A 1 47  ? 19.527 8.769   -1.125  0.20 14.95 ?  47  GLY   A HA3  1 
ATOM   1282 N N    A GLY   A 1 48  ? 18.528 6.711   -0.334  0.80 13.35 ?  48  GLY   A N    1 
ATOM   1283 N N    B GLY   A 1 48  ? 18.482 6.800   0.215   0.20 11.82 ?  48  GLY   A N    1 
ATOM   1284 C CA   A GLY   A 1 48  ? 18.126 5.392   0.081   0.80 13.34 ?  48  GLY   A CA   1 
ATOM   1285 C CA   B GLY   A 1 48  ? 18.061 5.467   0.601   0.20 11.34 ?  48  GLY   A CA   1 
ATOM   1286 C C    A GLY   A 1 48  ? 18.594 5.099   1.493   0.80 12.49 ?  48  GLY   A C    1 
ATOM   1287 C C    B GLY   A 1 48  ? 18.630 5.070   1.951   0.20 11.18 ?  48  GLY   A C    1 
ATOM   1288 O O    A GLY   A 1 48  ? 18.771 5.998   2.327   0.80 12.69 ?  48  GLY   A O    1 
ATOM   1289 O O    B GLY   A 1 48  ? 18.797 5.893   2.860   0.20 11.10 ?  48  GLY   A O    1 
ATOM   1290 H H    A GLY   A 1 48  ? 17.877 7.251   -0.512  0.80 16.03 ?  48  GLY   A H    1 
ATOM   1291 H H    B GLY   A 1 48  ? 17.836 7.361   0.124   0.20 14.19 ?  48  GLY   A H    1 
ATOM   1292 H HA2  A GLY   A 1 48  ? 17.163 5.305   0.050   0.80 16.01 ?  48  GLY   A HA2  1 
ATOM   1293 H HA2  B GLY   A 1 48  ? 17.090 5.431   0.644   0.20 13.61 ?  48  GLY   A HA2  1 
ATOM   1294 H HA3  A GLY   A 1 48  ? 18.519 4.729   -0.513  0.80 16.01 ?  48  GLY   A HA3  1 
ATOM   1295 H HA3  B GLY   A 1 48  ? 18.360 4.823   -0.064  0.20 13.61 ?  48  GLY   A HA3  1 
ATOM   1296 N N    A VAL   A 1 49  ? 18.817 3.812   1.760   0.80 12.22 ?  49  VAL   A N    1 
ATOM   1297 N N    B VAL   A 1 49  ? 18.923 3.775   2.087   0.20 10.51 ?  49  VAL   A N    1 
ATOM   1298 C CA   A VAL   A 1 49  ? 19.315 3.387   3.064   0.80 12.36 ?  49  VAL   A CA   1 
ATOM   1299 C CA   B VAL   A 1 49  ? 19.551 3.273   3.307   0.20 10.42 ?  49  VAL   A CA   1 
ATOM   1300 C C    A VAL   A 1 49  ? 20.627 4.082   3.404   0.80 11.22 ?  49  VAL   A C    1 
ATOM   1301 C C    B VAL   A 1 49  ? 20.860 4.003   3.579   0.20 9.93  ?  49  VAL   A C    1 
ATOM   1302 O O    A VAL   A 1 49  ? 20.827 4.514   4.543   0.80 11.46 ?  49  VAL   A O    1 
ATOM   1303 O O    B VAL   A 1 49  ? 21.149 4.385   4.720   0.20 10.27 ?  49  VAL   A O    1 
ATOM   1304 C CB   A VAL   A 1 49  ? 19.465 1.855   3.089   0.80 13.83 ?  49  VAL   A CB   1 
ATOM   1305 C CB   B VAL   A 1 49  ? 19.759 1.750   3.206   0.20 10.77 ?  49  VAL   A CB   1 
ATOM   1306 C CG1  A VAL   A 1 49  ? 20.277 1.402   4.301   0.80 13.55 ?  49  VAL   A CG1  1 
ATOM   1307 C CG1  B VAL   A 1 49  ? 20.714 1.270   4.284   0.20 10.62 ?  49  VAL   A CG1  1 
ATOM   1308 C CG2  A VAL   A 1 49  ? 18.098 1.186   3.082   0.80 16.52 ?  49  VAL   A CG2  1 
ATOM   1309 C CG2  B VAL   A 1 49  ? 18.434 1.018   3.314   0.20 11.30 ?  49  VAL   A CG2  1 
ATOM   1310 H H    A VAL   A 1 49  ? 18.687 3.163   1.206   0.80 14.66 ?  49  VAL   A H    1 
ATOM   1311 H H    B VAL   A 1 49  ? 18.765 3.170   1.495   0.20 12.61 ?  49  VAL   A H    1 
ATOM   1312 H HA   A VAL   A 1 49  ? 18.668 3.628   3.743   0.80 14.83 ?  49  VAL   A HA   1 
ATOM   1313 H HA   B VAL   A 1 49  ? 18.959 3.437   4.057   0.20 12.50 ?  49  VAL   A HA   1 
ATOM   1314 H HB   A VAL   A 1 49  ? 19.943 1.569   2.295   0.80 16.59 ?  49  VAL   A HB   1 
ATOM   1315 H HB   B VAL   A 1 49  ? 20.149 1.535   2.343   0.20 12.92 ?  49  VAL   A HB   1 
ATOM   1316 H HG11 A VAL   A 1 49  ? 20.122 0.459   4.448   0.80 16.26 ?  49  VAL   A HG11 1 
ATOM   1317 H HG11 B VAL   A 1 49  ? 20.607 0.312   4.394   0.20 12.74 ?  49  VAL   A HG11 1 
ATOM   1318 H HG12 A VAL   A 1 49  ? 21.219 1.561   4.129   0.80 16.26 ?  49  VAL   A HG12 1 
ATOM   1319 H HG12 B VAL   A 1 49  ? 21.624 1.470   4.014   0.20 12.74 ?  49  VAL   A HG12 1 
ATOM   1320 H HG13 A VAL   A 1 49  ? 19.990 1.911   5.077   0.80 16.26 ?  49  VAL   A HG13 1 
ATOM   1321 H HG13 B VAL   A 1 49  ? 20.504 1.722   5.115   0.20 12.74 ?  49  VAL   A HG13 1 
ATOM   1322 H HG21 A VAL   A 1 49  ? 18.217 0.223   3.093   0.80 19.82 ?  49  VAL   A HG21 1 
ATOM   1323 H HG21 B VAL   A 1 49  ? 18.588 0.066   3.208   0.20 13.56 ?  49  VAL   A HG21 1 
ATOM   1324 H HG22 A VAL   A 1 49  ? 17.607 1.468   3.869   0.80 19.82 ?  49  VAL   A HG22 1 
ATOM   1325 H HG22 B VAL   A 1 49  ? 18.047 1.196   4.187   0.20 13.56 ?  49  VAL   A HG22 1 
ATOM   1326 H HG23 A VAL   A 1 49  ? 17.625 1.453   2.281   0.80 19.82 ?  49  VAL   A HG23 1 
ATOM   1327 H HG23 B VAL   A 1 49  ? 17.840 1.337   2.618   0.20 13.56 ?  49  VAL   A HG23 1 
ATOM   1328 N N    A ALA   A 1 50  ? 21.551 4.159   2.441   0.80 10.68 ?  50  ALA   A N    1 
ATOM   1329 N N    B ALA   A 1 50  ? 21.679 4.191   2.542   0.20 9.71  ?  50  ALA   A N    1 
ATOM   1330 C CA   A ALA   A 1 50  ? 22.872 4.714   2.722   0.80 10.72 ?  50  ALA   A CA   1 
ATOM   1331 C CA   B ALA   A 1 50  ? 22.979 4.827   2.731   0.20 9.75  ?  50  ALA   A CA   1 
ATOM   1332 C C    A ALA   A 1 50  ? 22.784 6.176   3.135   0.80 10.39 ?  50  ALA   A C    1 
ATOM   1333 C C    B ALA   A 1 50  ? 22.821 6.275   3.171   0.20 9.60  ?  50  ALA   A C    1 
ATOM   1334 O O    A ALA   A 1 50  ? 23.422 6.594   4.106   0.80 11.30 ?  50  ALA   A O    1 
ATOM   1335 O O    B ALA   A 1 50  ? 23.395 6.695   4.182   0.20 9.51  ?  50  ALA   A O    1 
ATOM   1336 C CB   A ALA   A 1 50  ? 23.763 4.550   1.494   0.80 11.06 ?  50  ALA   A CB   1 
ATOM   1337 C CB   B ALA   A 1 50  ? 23.788 4.743   1.437   0.20 9.78  ?  50  ALA   A CB   1 
ATOM   1338 H H    A ALA   A 1 50  ? 21.438 3.899   1.627   0.80 12.81 ?  50  ALA   A H    1 
ATOM   1339 H H    B ALA   A 1 50  ? 21.502 3.966   1.730   0.20 11.65 ?  50  ALA   A H    1 
ATOM   1340 H HA   A ALA   A 1 50  ? 23.271 4.224   3.457   0.80 12.87 ?  50  ALA   A HA   1 
ATOM   1341 H HA   B ALA   A 1 50  ? 23.465 4.355   3.423   0.20 11.70 ?  50  ALA   A HA   1 
ATOM   1342 H HB1  A ALA   A 1 50  ? 24.638 4.921   1.690   0.80 13.28 ?  50  ALA   A HB1  1 
ATOM   1343 H HB1  B ALA   A 1 50  ? 24.660 5.141   1.584   0.20 11.74 ?  50  ALA   A HB1  1 
ATOM   1344 H HB2  A ALA   A 1 50  ? 23.842 3.607   1.285   0.80 13.28 ?  50  ALA   A HB2  1 
ATOM   1345 H HB2  B ALA   A 1 50  ? 23.888 3.811   1.188   0.20 11.74 ?  50  ALA   A HB2  1 
ATOM   1346 H HB3  A ALA   A 1 50  ? 23.362 5.024   0.749   0.80 13.28 ?  50  ALA   A HB3  1 
ATOM   1347 H HB3  B ALA   A 1 50  ? 23.317 5.223   0.738   0.20 11.74 ?  50  ALA   A HB3  1 
ATOM   1348 N N    A GLY   A 1 51  ? 22.000 6.968   2.406   0.80 11.03 ?  51  GLY   A N    1 
ATOM   1349 N N    B GLY   A 1 51  ? 22.043 7.054   2.419   0.20 10.32 ?  51  GLY   A N    1 
ATOM   1350 C CA   A GLY   A 1 51  ? 21.841 8.365   2.782   0.80 11.26 ?  51  GLY   A CA   1 
ATOM   1351 C CA   B GLY   A 1 51  ? 21.826 8.440   2.796   0.20 10.74 ?  51  GLY   A CA   1 
ATOM   1352 C C    A GLY   A 1 51  ? 21.242 8.518   4.166   0.80 11.13 ?  51  GLY   A C    1 
ATOM   1353 C C    B GLY   A 1 51  ? 21.194 8.571   4.167   0.20 10.98 ?  51  GLY   A C    1 
ATOM   1354 O O    A GLY   A 1 51  ? 21.644 9.396   4.935   0.80 12.09 ?  51  GLY   A O    1 
ATOM   1355 O O    B GLY   A 1 51  ? 21.533 9.477   4.934   0.20 11.01 ?  51  GLY   A O    1 
ATOM   1356 H H    A GLY   A 1 51  ? 21.571 6.727   1.698   0.80 13.24 ?  51  GLY   A H    1 
ATOM   1357 H H    B GLY   A 1 51  ? 21.639 6.803   1.702   0.20 12.38 ?  51  GLY   A H    1 
ATOM   1358 H HA2  A GLY   A 1 51  ? 22.707 8.805   2.766   0.80 13.52 ?  51  GLY   A HA2  1 
ATOM   1359 H HA2  B GLY   A 1 51  ? 22.677 8.907   2.800   0.20 12.89 ?  51  GLY   A HA2  1 
ATOM   1360 H HA3  A GLY   A 1 51  ? 21.263 8.808   2.137   0.80 13.52 ?  51  GLY   A HA3  1 
ATOM   1361 H HA3  B GLY   A 1 51  ? 21.248 8.863   2.141   0.20 12.89 ?  51  GLY   A HA3  1 
ATOM   1362 N N    . ALA   A 1 52  ? 20.268 7.665   4.499   1.00 11.56 ?  52  ALA   A N    1 
ATOM   1363 C CA   . ALA   A 1 52  ? 19.621 7.728   5.807   1.00 12.20 ?  52  ALA   A CA   1 
ATOM   1364 C C    . ALA   A 1 52  ? 20.571 7.313   6.933   1.00 11.34 ?  52  ALA   A C    1 
ATOM   1365 O O    . ALA   A 1 52  ? 20.637 7.980   7.975   1.00 12.56 ?  52  ALA   A O    1 
ATOM   1366 C CB   . ALA   A 1 52  ? 18.350 6.873   5.802   1.00 13.33 ?  52  ALA   A CB   1 
ATOM   1367 H H    A ALA   A 1 52  ? 19.975 7.039   3.983   0.80 13.87 ?  52  ALA   A H    1 
ATOM   1368 H H    B ALA   A 1 52  ? 20.013 7.014   3.993   0.20 13.87 ?  52  ALA   A H    1 
ATOM   1369 H HA   . ALA   A 1 52  ? 19.360 8.641   5.970   1.00 14.64 ?  52  ALA   A HA   1 
ATOM   1370 H HB1  . ALA   A 1 52  ? 17.929 6.936   6.676   1.00 16.00 ?  52  ALA   A HB1  1 
ATOM   1371 H HB2  . ALA   A 1 52  ? 17.745 7.213   5.122   1.00 16.00 ?  52  ALA   A HB2  1 
ATOM   1372 H HB3  . ALA   A 1 52  ? 18.582 5.953   5.611   1.00 16.00 ?  52  ALA   A HB3  1 
ATOM   1373 N N    A LEU   A 1 53  ? 21.312 6.217   6.752   0.80 10.96 ?  53  LEU   A N    1 
ATOM   1374 N N    B LEU   A 1 53  ? 21.317 6.218   6.741   0.20 11.03 ?  53  LEU   A N    1 
ATOM   1375 C CA   A LEU   A 1 53  ? 22.276 5.817   7.775   0.80 11.76 ?  53  LEU   A CA   1 
ATOM   1376 C CA   B LEU   A 1 53  ? 22.279 5.792   7.756   0.20 11.12 ?  53  LEU   A CA   1 
ATOM   1377 C C    A LEU   A 1 53  ? 23.321 6.905   7.975   0.80 10.83 ?  53  LEU   A C    1 
ATOM   1378 C C    B LEU   A 1 53  ? 23.357 6.847   7.965   0.20 10.89 ?  53  LEU   A C    1 
ATOM   1379 O O    A LEU   A 1 53  ? 23.633 7.285   9.108   0.80 12.07 ?  53  LEU   A O    1 
ATOM   1380 O O    B LEU   A 1 53  ? 23.746 7.132   9.104   0.20 11.23 ?  53  LEU   A O    1 
ATOM   1381 C CB   A LEU   A 1 53  ? 22.948 4.485   7.409   0.80 12.02 ?  53  LEU   A CB   1 
ATOM   1382 C CB   B LEU   A 1 53  ? 22.926 4.459   7.363   0.20 10.98 ?  53  LEU   A CB   1 
ATOM   1383 C CG   A LEU   A 1 53  ? 22.074 3.220   7.438   0.80 13.04 ?  53  LEU   A CG   1 
ATOM   1384 C CG   B LEU   A 1 53  ? 22.173 3.142   7.590   0.20 10.82 ?  53  LEU   A CG   1 
ATOM   1385 C CD1  A LEU   A 1 53  ? 22.815 2.041   6.828   0.80 13.66 ?  53  LEU   A CD1  1 
ATOM   1386 C CD1  B LEU   A 1 53  ? 22.969 1.986   7.006   0.20 11.10 ?  53  LEU   A CD1  1 
ATOM   1387 C CD2  A LEU   A 1 53  ? 21.625 2.894   8.852   0.80 14.39 ?  53  LEU   A CD2  1 
ATOM   1388 C CD2  B LEU   A 1 53  ? 21.911 2.896   9.064   0.20 11.04 ?  53  LEU   A CD2  1 
ATOM   1389 H H    A LEU   A 1 53  ? 21.278 5.699   6.060   0.80 13.15 ?  53  LEU   A H    1 
ATOM   1390 H H    B LEU   A 1 53  ? 21.287 5.714   6.041   0.20 13.24 ?  53  LEU   A H    1 
ATOM   1391 H HA   A LEU   A 1 53  ? 21.811 5.689   8.610   0.80 14.11 ?  53  LEU   A HA   1 
ATOM   1392 H HA   B LEU   A 1 53  ? 21.815 5.666   8.595   0.20 13.34 ?  53  LEU   A HA   1 
ATOM   1393 H HB2  A LEU   A 1 53  ? 23.305 4.559   6.506   0.80 14.42 ?  53  LEU   A HB2  1 
ATOM   1394 H HB2  B LEU   A 1 53  ? 23.126 4.497   6.415   0.20 13.17 ?  53  LEU   A HB2  1 
ATOM   1395 H HB3  A LEU   A 1 53  ? 23.682 4.333   8.024   0.80 14.42 ?  53  LEU   A HB3  1 
ATOM   1396 H HB3  B LEU   A 1 53  ? 23.758 4.382   7.854   0.20 13.17 ?  53  LEU   A HB3  1 
ATOM   1397 H HG   A LEU   A 1 53  ? 21.280 3.376   6.901   0.80 15.65 ?  53  LEU   A HG   1 
ATOM   1398 H HG   B LEU   A 1 53  ? 21.320 3.178   7.130   0.20 12.98 ?  53  LEU   A HG   1 
ATOM   1399 H HD11 A LEU   A 1 53  ? 22.240 1.258   6.861   0.80 16.39 ?  53  LEU   A HD11 1 
ATOM   1400 H HD11 B LEU   A 1 53  ? 22.482 1.160   7.157   0.20 13.32 ?  53  LEU   A HD11 1 
ATOM   1401 H HD12 A LEU   A 1 53  ? 23.038 2.248   5.909   0.80 16.39 ?  53  LEU   A HD12 1 
ATOM   1402 H HD12 B LEU   A 1 53  ? 23.085 2.131   6.054   0.20 13.32 ?  53  LEU   A HD12 1 
ATOM   1403 H HD13 A LEU   A 1 53  ? 23.622 1.879   7.339   0.80 16.39 ?  53  LEU   A HD13 1 
ATOM   1404 H HD13 B LEU   A 1 53  ? 23.833 1.945   7.444   0.20 13.32 ?  53  LEU   A HD13 1 
ATOM   1405 H HD21 A LEU   A 1 53  ? 21.107 2.071   8.840   0.80 17.26 ?  53  LEU   A HD21 1 
ATOM   1406 H HD21 B LEU   A 1 53  ? 21.419 2.065   9.162   0.20 13.25 ?  53  LEU   A HD21 1 
ATOM   1407 H HD22 A LEU   A 1 53  ? 22.406 2.783   9.416   0.80 17.26 ?  53  LEU   A HD22 1 
ATOM   1408 H HD22 B LEU   A 1 53  ? 22.757 2.837   9.529   0.20 13.25 ?  53  LEU   A HD22 1 
ATOM   1409 H HD23 A LEU   A 1 53  ? 21.076 3.621   9.187   0.80 17.26 ?  53  LEU   A HD23 1 
ATOM   1410 H HD23 B LEU   A 1 53  ? 21.387 3.631   9.418   0.20 13.25 ?  53  LEU   A HD23 1 
ATOM   1411 N N    . ASN   A 1 54  ? 23.858 7.434   6.877   1.00 10.62 ?  54  ASN   A N    1 
ATOM   1412 C CA   . ASN   A 1 54  ? 24.905 8.433   7.005   1.00 10.67 ?  54  ASN   A CA   1 
ATOM   1413 C C    . ASN   A 1 54  ? 24.399 9.676   7.729   1.00 10.92 ?  54  ASN   A C    1 
ATOM   1414 O O    . ASN   A 1 54  ? 25.085 10.225  8.598   1.00 11.77 ?  54  ASN   A O    1 
ATOM   1415 C CB   . ASN   A 1 54  ? 25.468 8.795   5.643   1.00 10.79 ?  54  ASN   A CB   1 
ATOM   1416 C CG   . ASN   A 1 54  ? 26.487 9.891   5.750   1.00 11.50 ?  54  ASN   A CG   1 
ATOM   1417 O OD1  . ASN   A 1 54  ? 27.494 9.742   6.457   1.00 11.43 ?  54  ASN   A OD1  1 
ATOM   1418 N ND2  . ASN   A 1 54  ? 26.239 11.006  5.088   1.00 12.47 ?  54  ASN   A ND2  1 
ATOM   1419 H H    A ASN   A 1 54  ? 23.630 7.238   6.068   0.80 12.75 ?  54  ASN   A H    1 
ATOM   1420 H H    B ASN   A 1 54  ? 23.600 7.276   6.069   0.20 12.75 ?  54  ASN   A H    1 
ATOM   1421 H HA   . ASN   A 1 54  ? 25.620 8.060   7.533   1.00 12.80 ?  54  ASN   A HA   1 
ATOM   1422 H HB2  . ASN   A 1 54  ? 25.899 8.010   5.257   1.00 12.95 ?  54  ASN   A HB2  1 
ATOM   1423 H HB3  . ASN   A 1 54  ? 24.755 9.101   5.064   1.00 12.95 ?  54  ASN   A HB3  1 
ATOM   1424 H HD21 . ASN   A 1 54  ? 26.799 11.662  5.124   1.00 14.97 ?  54  ASN   A HD21 1 
ATOM   1425 H HD22 . ASN   A 1 54  ? 25.528 11.077  4.615   1.00 14.97 ?  54  ASN   A HD22 1 
ATOM   1426 N N    . LYS   A 1 55  ? 23.194 10.137  7.384   1.00 11.44 ?  55  LYS   A N    1 
ATOM   1427 C CA   . LYS   A 1 55  ? 22.605 11.294  8.051   1.00 12.64 ?  55  LYS   A CA   1 
ATOM   1428 C C    . LYS   A 1 55  ? 22.508 11.063  9.553   1.00 12.45 ?  55  LYS   A C    1 
ATOM   1429 O O    . LYS   A 1 55  ? 22.798 11.962  10.356  1.00 13.48 ?  55  LYS   A O    1 
ATOM   1430 C CB   . LYS   A 1 55  ? 21.228 11.574  7.443   1.00 13.23 ?  55  LYS   A CB   1 
ATOM   1431 C CG   . LYS   A 1 55  ? 20.480 12.744  8.048   1.00 15.62 ?  55  LYS   A CG   1 
ATOM   1432 C CD   . LYS   A 1 55  ? 19.137 12.933  7.336   1.00 17.58 ?  55  LYS   A CD   1 
ATOM   1433 C CE   . LYS   A 1 55  ? 18.299 14.037  7.954   1.00 20.24 ?  55  LYS   A CE   1 
ATOM   1434 N NZ   . LYS   A 1 55  ? 16.938 14.118  7.337   1.00 21.60 ?  55  LYS   A NZ   1 
ATOM   1435 H H    . LYS   A 1 55  ? 22.687 9.784   6.777   1.00 13.73 ?  55  LYS   A H    1 
ATOM   1436 H HA   . LYS   A 1 55  ? 23.165 12.065  7.898   1.00 15.17 ?  55  LYS   A HA   1 
ATOM   1437 H HB2  . LYS   A 1 55  ? 21.337 11.758  6.499   1.00 15.88 ?  55  LYS   A HB2  1 
ATOM   1438 H HB3  . LYS   A 1 55  ? 20.671 10.785  7.558   1.00 15.88 ?  55  LYS   A HB3  1 
ATOM   1439 H HG2  . LYS   A 1 55  ? 20.301 12.572  8.988   1.00 18.74 ?  55  LYS   A HG2  1 
ATOM   1440 H HG3  . LYS   A 1 55  ? 20.998 13.555  7.943   1.00 18.74 ?  55  LYS   A HG3  1 
ATOM   1441 H HD2  . LYS   A 1 55  ? 19.304 13.158  6.405   1.00 21.10 ?  55  LYS   A HD2  1 
ATOM   1442 H HD3  . LYS   A 1 55  ? 18.633 12.103  7.387   1.00 21.10 ?  55  LYS   A HD3  1 
ATOM   1443 H HE2  . LYS   A 1 55  ? 18.191 13.867  8.901   1.00 24.29 ?  55  LYS   A HE2  1 
ATOM   1444 H HE3  . LYS   A 1 55  ? 18.743 14.890  7.815   1.00 24.29 ?  55  LYS   A HE3  1 
ATOM   1445 H HZ1  . LYS   A 1 55  ? 16.369 14.510  7.901   1.00 25.92 ?  55  LYS   A HZ1  1 
ATOM   1446 H HZ2  . LYS   A 1 55  ? 16.966 14.599  6.586   1.00 25.92 ?  55  LYS   A HZ2  1 
ATOM   1447 H HZ3  . LYS   A 1 55  ? 16.635 13.303  7.147   1.00 25.92 ?  55  LYS   A HZ3  1 
ATOM   1448 N N    . ALA   A 1 56  ? 22.119 9.852   9.955   1.00 12.81 ?  56  ALA   A N    1 
ATOM   1449 C CA   . ALA   A 1 56  ? 21.995 9.536   11.373  1.00 13.60 ?  56  ALA   A CA   1 
ATOM   1450 C C    . ALA   A 1 56  ? 23.338 9.566   12.098  1.00 13.34 ?  56  ALA   A C    1 
ATOM   1451 O O    . ALA   A 1 56  ? 23.355 9.749   13.316  1.00 14.57 ?  56  ALA   A O    1 
ATOM   1452 C CB   . ALA   A 1 56  ? 21.291 8.190   11.565  1.00 14.99 ?  56  ALA   A CB   1 
ATOM   1453 H H    . ALA   A 1 56  ? 21.922 9.203   9.427   1.00 15.37 ?  56  ALA   A H    1 
ATOM   1454 H HA   . ALA   A 1 56  ? 21.446 10.205  11.789  1.00 16.33 ?  56  ALA   A HA   1 
ATOM   1455 H HB1  . ALA   A 1 56  ? 21.221 8.000   12.516  1.00 17.99 ?  56  ALA   A HB1  1 
ATOM   1456 H HB2  . ALA   A 1 56  ? 20.400 8.245   11.178  1.00 17.99 ?  56  ALA   A HB2  1 
ATOM   1457 H HB3  . ALA   A 1 56  ? 21.798 7.492   11.126  1.00 17.99 ?  56  ALA   A HB3  1 
ATOM   1458 N N    . THR   A 1 57  ? 24.453 9.371   11.386  1.00 12.95 ?  57  THR   A N    1 
ATOM   1459 C CA   . THR   A 1 57  ? 25.792 9.504   11.964  1.00 12.55 ?  57  THR   A CA   1 
ATOM   1460 C C    . THR   A 1 57  ? 26.344 10.923  11.880  1.00 12.76 ?  57  THR   A C    1 
ATOM   1461 O O    . THR   A 1 57  ? 27.530 11.129  12.167  1.00 13.43 ?  57  THR   A O    1 
ATOM   1462 C CB   . THR   A 1 57  ? 26.801 8.550   11.295  1.00 12.03 ?  57  THR   A CB   1 
ATOM   1463 O OG1  . THR   A 1 57  ? 27.177 9.037   9.993   1.00 12.01 ?  57  THR   A OG1  1 
ATOM   1464 C CG2  . THR   A 1 57  ? 26.275 7.129   11.214  1.00 12.48 ?  57  THR   A CG2  1 
ATOM   1465 H H    . THR   A 1 57  ? 24.461 9.139   10.557  1.00 15.54 ?  57  THR   A H    1 
ATOM   1466 H HA   . THR   A 1 57  ? 25.752 9.256   12.905  1.00 15.05 ?  57  THR   A HA   1 
ATOM   1467 H HB   . THR   A 1 57  ? 27.602 8.519   11.846  1.00 14.43 ?  57  THR   A HB   1 
ATOM   1468 H HG1  . THR   A 1 57  ? 26.492 9.096   9.505   1.00 14.42 ?  57  THR   A HG1  1 
ATOM   1469 H HG21 . THR   A 1 57  ? 26.929 6.552   10.782  1.00 14.97 ?  57  THR   A HG21 1 
ATOM   1470 H HG22 . THR   A 1 57  ? 26.098 6.783   12.104  1.00 14.97 ?  57  THR   A HG22 1 
ATOM   1471 H HG23 . THR   A 1 57  ? 25.453 7.101   10.701  1.00 14.97 ?  57  THR   A HG23 1 
ATOM   1472 N N    . ASN   A 1 58  ? 25.535 11.897  11.467  1.00 13.28 ?  58  ASN   A N    1 
ATOM   1473 C CA   . ASN   A 1 58  ? 26.004 13.276  11.381  1.00 13.84 ?  58  ASN   A CA   1 
ATOM   1474 C C    . ASN   A 1 58  ? 27.148 13.400  10.370  1.00 12.79 ?  58  ASN   A C    1 
ATOM   1475 O O    . ASN   A 1 58  ? 28.042 14.228  10.526  1.00 13.74 ?  58  ASN   A O    1 
ATOM   1476 C CB   . ASN   A 1 58  ? 26.392 13.794  12.782  1.00 16.49 ?  58  ASN   A CB   1 
ATOM   1477 C CG   . ASN   A 1 58  ? 26.829 15.247  12.799  1.00 20.58 ?  58  ASN   A CG   1 
ATOM   1478 O OD1  . ASN   A 1 58  ? 26.198 16.098  12.180  1.00 22.29 ?  58  ASN   A OD1  1 
ATOM   1479 N ND2  . ASN   A 1 58  ? 27.908 15.542  13.547  1.00 21.39 ?  58  ASN   A ND2  1 
ATOM   1480 H H    . ASN   A 1 58  ? 24.719 11.781  11.218  1.00 15.93 ?  58  ASN   A H    1 
ATOM   1481 H HA   . ASN   A 1 58  ? 25.277 13.822  11.065  1.00 16.61 ?  58  ASN   A HA   1 
ATOM   1482 H HB2  . ASN   A 1 58  ? 25.619 13.712  13.373  1.00 19.78 ?  58  ASN   A HB2  1 
ATOM   1483 H HB3  . ASN   A 1 58  ? 27.122 13.265  13.136  1.00 19.78 ?  58  ASN   A HB3  1 
ATOM   1484 H HD21 . ASN   A 1 58  ? 28.199 16.354  13.598  1.00 25.67 ?  58  ASN   A HD21 1 
ATOM   1485 H HD22 . ASN   A 1 58  ? 28.321 14.918  13.973  1.00 25.67 ?  58  ASN   A HD22 1 
ATOM   1486 N N    . ASN   A 1 59  ? 27.127 12.574  9.321   1.00 12.10 ?  59  ASN   A N    1 
ATOM   1487 C CA   . ASN   A 1 59  ? 28.104 12.531  8.225   1.00 11.69 ?  59  ASN   A CA   1 
ATOM   1488 C C    . ASN   A 1 59  ? 29.419 11.847  8.621   1.00 11.64 ?  59  ASN   A C    1 
ATOM   1489 O O    . ASN   A 1 59  ? 30.346 11.802  7.796   1.00 11.82 ?  59  ASN   A O    1 
ATOM   1490 C CB   . ASN   A 1 59  ? 28.409 13.914  7.609   1.00 12.11 ?  59  ASN   A CB   1 
ATOM   1491 C CG   . ASN   A 1 59  ? 28.768 13.834  6.141   1.00 12.24 ?  59  ASN   A CG   1 
ATOM   1492 O OD1  . ASN   A 1 59  ? 28.052 13.214  5.346   1.00 12.34 ?  59  ASN   A OD1  1 
ATOM   1493 N ND2  . ASN   A 1 59  ? 29.867 14.488  5.761   1.00 12.98 ?  59  ASN   A ND2  1 
ATOM   1494 H H    . ASN   A 1 59  ? 26.508 11.987  9.213   1.00 14.51 ?  59  ASN   A H    1 
ATOM   1495 H HA   . ASN   A 1 59  ? 27.721 11.997  7.516   1.00 14.03 ?  59  ASN   A HA   1 
ATOM   1496 H HB2  . ASN   A 1 59  ? 27.627 14.482  7.685   1.00 14.53 ?  59  ASN   A HB2  1 
ATOM   1497 H HB3  . ASN   A 1 59  ? 29.160 14.317  8.069   1.00 14.53 ?  59  ASN   A HB3  1 
ATOM   1498 H HD21 . ASN   A 1 59  ? 30.113 14.479  4.933   1.00 15.57 ?  59  ASN   A HD21 1 
ATOM   1499 H HD22 . ASN   A 1 59  ? 30.339 14.916  6.338   1.00 15.57 ?  59  ASN   A HD22 1 
ATOM   1500 N N    . ALA   A 1 60  ? 29.538 11.304  9.831   1.00 11.68 ?  60  ALA   A N    1 
ATOM   1501 C CA   . ALA   A 1 60  ? 30.778 10.628  10.194  1.00 11.97 ?  60  ALA   A CA   1 
ATOM   1502 C C    . ALA   A 1 60  ? 31.005 9.387   9.337   1.00 12.08 ?  60  ALA   A C    1 
ATOM   1503 O O    . ALA   A 1 60  ? 32.150 9.051   9.009   1.00 12.39 ?  60  ALA   A O    1 
ATOM   1504 C CB   . ALA   A 1 60  ? 30.767 10.274  11.678  1.00 12.36 ?  60  ALA   A CB   1 
ATOM   1505 H H    . ALA   A 1 60  ? 28.935 11.309  10.443  1.00 14.01 ?  60  ALA   A H    1 
ATOM   1506 H HA   . ALA   A 1 60  ? 31.520 11.235  10.042  1.00 14.37 ?  60  ALA   A HA   1 
ATOM   1507 H HB1  . ALA   A 1 60  ? 31.592 9.828   11.907  1.00 14.83 ?  60  ALA   A HB1  1 
ATOM   1508 H HB2  . ALA   A 1 60  ? 30.674 11.092  12.197  1.00 14.83 ?  60  ALA   A HB2  1 
ATOM   1509 H HB3  . ALA   A 1 60  ? 30.010 9.689   11.857  1.00 14.83 ?  60  ALA   A HB3  1 
ATOM   1510 N N    . MET   A 1 61  ? 29.932 8.693   8.955   1.00 11.20 ?  61  MET   A N    1 
ATOM   1511 C CA   . MET   A 1 61  ? 30.072 7.552   8.057   1.00 10.90 ?  61  MET   A CA   1 
ATOM   1512 C C    . MET   A 1 61  ? 30.712 7.972   6.737   1.00 10.65 ?  61  MET   A C    1 
ATOM   1513 O O    . MET   A 1 61  ? 31.604 7.288   6.225   1.00 11.52 ?  61  MET   A O    1 
ATOM   1514 C CB   . MET   A 1 61  ? 28.707 6.891   7.843   1.00 10.97 ?  61  MET   A CB   1 
ATOM   1515 C CG   . MET   A 1 61  ? 28.719 5.724   6.876   1.00 11.41 ?  61  MET   A CG   1 
ATOM   1516 S SD   . MET   A 1 61  ? 27.098 4.980   6.665   1.00 12.63 ?  61  MET   A SD   1 
ATOM   1517 C CE   . MET   A 1 61  ? 26.954 4.126   8.237   1.00 14.36 ?  61  MET   A CE   1 
ATOM   1518 H H    . MET   A 1 61  ? 29.130 8.865   9.194   1.00 13.45 ?  61  MET   A H    1 
ATOM   1519 H HA   . MET   A 1 61  ? 30.646 6.895   8.476   1.00 13.08 ?  61  MET   A HA   1 
ATOM   1520 H HB2  . MET   A 1 61  ? 28.382 6.565   8.694   1.00 13.17 ?  61  MET   A HB2  1 
ATOM   1521 H HB3  . MET   A 1 61  ? 28.090 7.555   7.490   1.00 13.17 ?  61  MET   A HB3  1 
ATOM   1522 H HG2  . MET   A 1 61  ? 29.011 6.025   6.001   1.00 13.70 ?  61  MET   A HG2  1 
ATOM   1523 H HG3  . MET   A 1 61  ? 29.317 5.036   7.207   1.00 13.70 ?  61  MET   A HG3  1 
ATOM   1524 H HE1  . MET   A 1 61  ? 26.121 3.630   8.255   1.00 17.23 ?  61  MET   A HE1  1 
ATOM   1525 H HE2  . MET   A 1 61  ? 27.704 3.524   8.339   1.00 17.23 ?  61  MET   A HE2  1 
ATOM   1526 H HE3  . MET   A 1 61  ? 26.958 4.782   8.958   1.00 17.23 ?  61  MET   A HE3  1 
ATOM   1527 N N    . GLN   A 1 62  ? 30.273 9.095   6.171   1.00 10.91 ?  62  GLN   A N    1 
ATOM   1528 C CA   . GLN   A 1 62  ? 30.839 9.564   4.908   1.00 11.14 ?  62  GLN   A CA   1 
ATOM   1529 C C    . GLN   A 1 62  ? 32.312 9.943   5.051   1.00 10.96 ?  62  GLN   A C    1 
ATOM   1530 O O    . GLN   A 1 62  ? 33.122 9.621   4.174   1.00 11.66 ?  62  GLN   A O    1 
ATOM   1531 C CB   . GLN   A 1 62  ? 30.044 10.747  4.366   1.00 11.38 ?  62  GLN   A CB   1 
ATOM   1532 C CG   . GLN   A 1 62  ? 30.443 11.110  2.945   1.00 11.55 ?  62  GLN   A CG   1 
ATOM   1533 C CD   . GLN   A 1 62  ? 30.101 9.982   1.993   1.00 11.50 ?  62  GLN   A CD   1 
ATOM   1534 O OE1  . GLN   A 1 62  ? 28.918 9.675   1.779   1.00 12.12 ?  62  GLN   A OE1  1 
ATOM   1535 N NE2  . GLN   A 1 62  ? 31.120 9.303   1.479   1.00 12.19 ?  62  GLN   A NE2  1 
ATOM   1536 H H    . GLN   A 1 62  ? 29.654 9.593   6.494   1.00 13.09 ?  62  GLN   A H    1 
ATOM   1537 H HA   . GLN   A 1 62  ? 30.786 8.845   4.261   1.00 13.37 ?  62  GLN   A HA   1 
ATOM   1538 H HB2  . GLN   A 1 62  ? 29.103 10.527  4.370   1.00 13.65 ?  62  GLN   A HB2  1 
ATOM   1539 H HB3  . GLN   A 1 62  ? 30.210 11.524  4.925   1.00 13.65 ?  62  GLN   A HB3  1 
ATOM   1540 H HG2  . GLN   A 1 62  ? 29.946 11.892  2.663   1.00 13.86 ?  62  GLN   A HG2  1 
ATOM   1541 H HG3  . GLN   A 1 62  ? 31.393 11.272  2.900   1.00 13.86 ?  62  GLN   A HG3  1 
ATOM   1542 H HE21 . GLN   A 1 62  ? 31.930 9.536   1.667   1.00 14.62 ?  62  GLN   A HE21 1 
ATOM   1543 H HE22 . GLN   A 1 62  ? 30.979 8.649   0.941   1.00 14.62 ?  62  GLN   A HE22 1 
ATOM   1544 N N    . VAL   A 1 63  ? 32.679 10.617  6.146   1.00 11.68 ?  63  VAL   A N    1 
ATOM   1545 C CA   . VAL   A 1 63  ? 34.072 11.013  6.363   1.00 12.62 ?  63  VAL   A CA   1 
ATOM   1546 C C    . VAL   A 1 63  ? 34.964 9.777   6.435   1.00 12.10 ?  63  VAL   A C    1 
ATOM   1547 O O    . VAL   A 1 63  ? 36.016 9.697   5.782   1.00 12.57 ?  63  VAL   A O    1 
ATOM   1548 C CB   . VAL   A 1 63  ? 34.178 11.889  7.626   1.00 14.55 ?  63  VAL   A CB   1 
ATOM   1549 C CG1  . VAL   A 1 63  ? 35.628 12.119  8.006   1.00 16.77 ?  63  VAL   A CG1  1 
ATOM   1550 C CG2  . VAL   A 1 63  ? 33.461 13.230  7.410   1.00 14.58 ?  63  VAL   A CG2  1 
ATOM   1551 H H    . VAL   A 1 63  ? 32.141 10.856  6.775   1.00 14.01 ?  63  VAL   A H    1 
ATOM   1552 H HA   . VAL   A 1 63  ? 34.367 11.546  5.611   1.00 15.14 ?  63  VAL   A HA   1 
ATOM   1553 H HB   . VAL   A 1 63  ? 33.745 11.430  8.367   1.00 17.45 ?  63  VAL   A HB   1 
ATOM   1554 H HG11 . VAL   A 1 63  ? 35.670 12.854  8.636   1.00 20.12 ?  63  VAL   A HG11 1 
ATOM   1555 H HG12 . VAL   A 1 63  ? 35.980 11.313  8.414   1.00 20.12 ?  63  VAL   A HG12 1 
ATOM   1556 H HG13 . VAL   A 1 63  ? 36.127 12.337  7.206   1.00 20.12 ?  63  VAL   A HG13 1 
ATOM   1557 H HG21 . VAL   A 1 63  ? 33.544 13.764  8.214   1.00 17.49 ?  63  VAL   A HG21 1 
ATOM   1558 H HG22 . VAL   A 1 63  ? 33.874 13.687  6.662   1.00 17.49 ?  63  VAL   A HG22 1 
ATOM   1559 H HG23 . VAL   A 1 63  ? 32.526 13.058  7.220   1.00 17.49 ?  63  VAL   A HG23 1 
ATOM   1560 N N    . GLU   A 1 64  ? 34.531 8.775   7.207   1.00 12.07 ?  64  GLU   A N    1 
ATOM   1561 C CA   . GLU   A 1 64  ? 35.293 7.533   7.306   1.00 11.91 ?  64  GLU   A CA   1 
ATOM   1562 C C    . GLU   A 1 64  ? 35.386 6.846   5.950   1.00 11.41 ?  64  GLU   A C    1 
ATOM   1563 O O    . GLU   A 1 64  ? 36.433 6.291   5.582   1.00 12.22 ?  64  GLU   A O    1 
ATOM   1564 C CB   . GLU   A 1 64  ? 34.608 6.620   8.324   1.00 12.43 ?  64  GLU   A CB   1 
ATOM   1565 C CG   . GLU   A 1 64  ? 35.255 5.271   8.481   1.00 13.17 ?  64  GLU   A CG   1 
ATOM   1566 C CD   . GLU   A 1 64  ? 34.377 4.286   9.222   1.00 14.16 ?  64  GLU   A CD   1 
ATOM   1567 O OE1  . GLU   A 1 64  ? 33.135 4.378   9.099   1.00 14.81 ?  64  GLU   A OE1  1 
ATOM   1568 O OE2  . GLU   A 1 64  ? 34.922 3.392   9.909   1.00 14.12 -1 64  GLU   A OE2  1 
ATOM   1569 H H    . GLU   A 1 64  ? 33.806 8.789   7.670   1.00 14.48 ?  64  GLU   A H    1 
ATOM   1570 H HA   . GLU   A 1 64  ? 36.190 7.732   7.627   1.00 14.29 ?  64  GLU   A HA   1 
ATOM   1571 H HB2  . GLU   A 1 64  ? 34.625 7.059   9.197   1.00 14.91 ?  64  GLU   A HB2  1 
ATOM   1572 H HB3  . GLU   A 1 64  ? 33.688 6.490   8.049   1.00 14.91 ?  64  GLU   A HB3  1 
ATOM   1573 H HG2  . GLU   A 1 64  ? 35.439 4.901   7.600   1.00 15.81 ?  64  GLU   A HG2  1 
ATOM   1574 H HG3  . GLU   A 1 64  ? 36.078 5.374   8.974   1.00 15.81 ?  64  GLU   A HG3  1 
ATOM   1575 N N    . SER   A 1 65  ? 34.272 6.837   5.215   1.00 11.24 ?  65  SER   A N    1 
ATOM   1576 C CA   . SER   A 1 65  ? 34.216 6.174   3.918   1.00 11.21 ?  65  SER   A CA   1 
ATOM   1577 C C    . SER   A 1 65  ? 35.145 6.828   2.908   1.00 11.29 ?  65  SER   A C    1 
ATOM   1578 O O    . SER   A 1 65  ? 35.792 6.141   2.111   1.00 12.68 ?  65  SER   A O    1 
ATOM   1579 C CB   . SER   A 1 65  ? 32.778 6.177   3.389   1.00 11.60 ?  65  SER   A CB   1 
ATOM   1580 O OG   . SER   A 1 65  ? 31.936 5.374   4.194   1.00 11.73 ?  65  SER   A OG   1 
ATOM   1581 H H    . SER   A 1 65  ? 33.535 7.216   5.449   1.00 13.49 ?  65  SER   A H    1 
ATOM   1582 H HA   . SER   A 1 65  ? 34.499 5.253   4.026   1.00 13.45 ?  65  SER   A HA   1 
ATOM   1583 H HB2  . SER   A 1 65  ? 32.445 7.086   3.388   1.00 13.93 ?  65  SER   A HB2  1 
ATOM   1584 H HB3  . SER   A 1 65  ? 32.780 5.823   2.485   1.00 13.93 ?  65  SER   A HB3  1 
ATOM   1585 H HG   . SER   A 1 65  ? 31.932 5.669   4.988   1.00 14.08 ?  65  SER   A HG   1 
ATOM   1586 N N    . ASP   A 1 66  ? 35.227 8.163   2.922   1.00 11.23 ?  66  ASP   A N    1 
ATOM   1587 C CA   . ASP   A 1 66  ? 36.095 8.858   1.980   1.00 12.33 ?  66  ASP   A CA   1 
ATOM   1588 C C    . ASP   A 1 66  ? 37.556 8.511   2.229   1.00 12.15 ?  66  ASP   A C    1 
ATOM   1589 O O    . ASP   A 1 66  ? 38.328 8.327   1.283   1.00 13.19 ?  66  ASP   A O    1 
ATOM   1590 C CB   . ASP   A 1 66  ? 35.871 10.368  2.063   1.00 14.08 ?  66  ASP   A CB   1 
ATOM   1591 C CG   . ASP   A 1 66  ? 34.539 10.816  1.453   1.00 15.82 ?  66  ASP   A CG   1 
ATOM   1592 O OD1  . ASP   A 1 66  ? 33.843 10.013  0.794   1.00 15.81 ?  66  ASP   A OD1  1 
ATOM   1593 O OD2  . ASP   A 1 66  ? 34.222 12.012  1.607   1.00 18.64 -1 66  ASP   A OD2  1 
ATOM   1594 H H    . ASP   A 1 66  ? 34.791 8.680   3.458   1.00 13.48 ?  66  ASP   A H    1 
ATOM   1595 H HA   . ASP   A 1 66  ? 35.868 8.577   1.080   1.00 14.79 ?  66  ASP   A HA   1 
ATOM   1596 H HB2  . ASP   A 1 66  ? 35.874 10.637  2.992   1.00 16.90 ?  66  ASP   A HB2  1 
ATOM   1597 H HB3  . ASP   A 1 66  ? 36.584 10.818  1.582   1.00 16.90 ?  66  ASP   A HB3  1 
ATOM   1598 N N    . ASP   A 1 67  ? 37.946 8.386   3.496   1.00 12.32 ?  67  ASP   A N    1 
ATOM   1599 C CA   . ASP   A 1 67  ? 39.301 7.941   3.804   1.00 13.06 ?  67  ASP   A CA   1 
ATOM   1600 C C    . ASP   A 1 67  ? 39.529 6.501   3.343   1.00 12.91 ?  67  ASP   A C    1 
ATOM   1601 O O    . ASP   A 1 67  ? 40.590 6.179   2.791   1.00 13.99 ?  67  ASP   A O    1 
ATOM   1602 C CB   . ASP   A 1 67  ? 39.569 8.087   5.300   1.00 14.16 ?  67  ASP   A CB   1 
ATOM   1603 C CG   . ASP   A 1 67  ? 40.861 7.424   5.724   1.00 16.07 ?  67  ASP   A CG   1 
ATOM   1604 O OD1  . ASP   A 1 67  ? 41.928 8.074   5.607   1.00 18.82 ?  67  ASP   A OD1  1 
ATOM   1605 O OD2  . ASP   A 1 67  ? 40.804 6.251   6.164   1.00 16.17 -1 67  ASP   A OD2  1 
ATOM   1606 H H    . ASP   A 1 67  ? 37.457 8.553   4.180   1.00 14.79 ?  67  ASP   A H    1 
ATOM   1607 H HA   . ASP   A 1 67  ? 39.935 8.509   3.332   1.00 15.67 ?  67  ASP   A HA   1 
ATOM   1608 H HB2  . ASP   A 1 67  ? 39.628 9.027   5.517   1.00 17.00 ?  67  ASP   A HB2  1 
ATOM   1609 H HB3  . ASP   A 1 67  ? 38.839 7.674   5.787   1.00 17.00 ?  67  ASP   A HB3  1 
ATOM   1610 N N    . TYR   A 1 68  ? 38.538 5.625   3.542   1.00 13.02 ?  68  TYR   A N    1 
ATOM   1611 C CA   . TYR   A 1 68  ? 38.652 4.244   3.067   1.00 13.21 ?  68  TYR   A CA   1 
ATOM   1612 C C    . TYR   A 1 68  ? 38.896 4.197   1.558   1.00 12.79 ?  68  TYR   A C    1 
ATOM   1613 O O    . TYR   A 1 68  ? 39.783 3.473   1.085   1.00 13.64 ?  68  TYR   A O    1 
ATOM   1614 C CB   . TYR   A 1 68  ? 37.400 3.430   3.443   1.00 13.40 ?  68  TYR   A CB   1 
ATOM   1615 C CG   . TYR   A 1 68  ? 37.427 2.031   2.815   1.00 14.79 ?  68  TYR   A CG   1 
ATOM   1616 C CD1  . TYR   A 1 68  ? 36.979 1.838   1.513   1.00 16.54 ?  68  TYR   A CD1  1 
ATOM   1617 C CD2  . TYR   A 1 68  ? 37.966 0.943   3.485   1.00 16.83 ?  68  TYR   A CD2  1 
ATOM   1618 C CE1  . TYR   A 1 68  ? 37.039 0.619   0.898   1.00 18.07 ?  68  TYR   A CE1  1 
ATOM   1619 C CE2  . TYR   A 1 68  ? 38.036 -0.322  2.861   1.00 17.85 ?  68  TYR   A CE2  1 
ATOM   1620 C CZ   . TYR   A 1 68  ? 37.579 -0.457  1.569   1.00 18.99 ?  68  TYR   A CZ   1 
ATOM   1621 O OH   . TYR   A 1 68  ? 37.653 -1.677  0.937   1.00 21.11 ?  68  TYR   A OH   1 
ATOM   1622 H H    . TYR   A 1 68  ? 37.799 5.806   3.945   1.00 15.63 ?  68  TYR   A H    1 
ATOM   1623 H HA   . TYR   A 1 68  ? 39.411 3.833   3.500   1.00 15.86 ?  68  TYR   A HA   1 
ATOM   1624 H HB2  . TYR   A 1 68  ? 37.366 3.322   4.409   1.00 16.08 ?  68  TYR   A HB2  1 
ATOM   1625 H HB3  . TYR   A 1 68  ? 36.607 3.887   3.129   1.00 16.08 ?  68  TYR   A HB3  1 
ATOM   1626 H HD1  . TYR   A 1 68  ? 36.628 2.564   1.046   1.00 19.85 ?  68  TYR   A HD1  1 
ATOM   1627 H HD2  . TYR   A 1 68  ? 38.297 1.040   4.343   1.00 20.19 ?  68  TYR   A HD2  1 
ATOM   1628 H HE1  . TYR   A 1 68  ? 36.726 0.520   0.025   1.00 21.68 ?  68  TYR   A HE1  1 
ATOM   1629 H HE2  . TYR   A 1 68  ? 38.398 -1.055  3.300   1.00 21.42 ?  68  TYR   A HE2  1 
ATOM   1630 H HH   . TYR   A 1 68  ? 37.986 -2.248  1.447   1.00 25.34 ?  68  TYR   A HH   1 
ATOM   1631 N N    . ILE   A 1 69  ? 38.107 4.950   0.783   1.00 12.21 ?  69  ILE   A N    1 
ATOM   1632 C CA   . ILE   A 1 69  ? 38.252 4.933   -0.672  1.00 12.26 ?  69  ILE   A CA   1 
ATOM   1633 C C    . ILE   A 1 69  ? 39.584 5.544   -1.101  1.00 12.27 ?  69  ILE   A C    1 
ATOM   1634 O O    . ILE   A 1 69  ? 40.230 5.064   -2.041  1.00 12.77 ?  69  ILE   A O    1 
ATOM   1635 C CB   . ILE   A 1 69  ? 37.051 5.632   -1.339  1.00 13.49 ?  69  ILE   A CB   1 
ATOM   1636 C CG1  . ILE   A 1 69  ? 35.737 4.896   -1.049  1.00 13.81 ?  69  ILE   A CG1  1 
ATOM   1637 C CG2  . ILE   A 1 69  ? 37.298 5.806   -2.848  1.00 15.13 ?  69  ILE   A CG2  1 
ATOM   1638 C CD1  . ILE   A 1 69  ? 35.569 3.625   -1.836  1.00 14.60 ?  69  ILE   A CD1  1 
ATOM   1639 H H    . ILE   A 1 69  ? 37.490 5.475   1.073   1.00 14.66 ?  69  ILE   A H    1 
ATOM   1640 H HA   . ILE   A 1 69  ? 38.250 4.008   -0.965  1.00 14.71 ?  69  ILE   A HA   1 
ATOM   1641 H HB   . ILE   A 1 69  ? 36.976 6.513   -0.955  1.00 16.19 ?  69  ILE   A HB   1 
ATOM   1642 H HG12 . ILE   A 1 69  ? 35.708 4.664   -0.104  1.00 16.57 ?  69  ILE   A HG12 1 
ATOM   1643 H HG13 . ILE   A 1 69  ? 34.995 5.482   -1.263  1.00 16.57 ?  69  ILE   A HG13 1 
ATOM   1644 H HG21 . ILE   A 1 69  ? 36.451 5.999   -3.287  1.00 18.16 ?  69  ILE   A HG21 1 
ATOM   1645 H HG22 . ILE   A 1 69  ? 37.909 6.548   -2.986  1.00 18.16 ?  69  ILE   A HG22 1 
ATOM   1646 H HG23 . ILE   A 1 69  ? 37.675 4.991   -3.209  1.00 18.16 ?  69  ILE   A HG23 1 
ATOM   1647 H HD11 . ILE   A 1 69  ? 34.795 3.149   -1.496  1.00 17.52 ?  69  ILE   A HD11 1 
ATOM   1648 H HD12 . ILE   A 1 69  ? 35.429 3.853   -2.770  1.00 17.52 ?  69  ILE   A HD12 1 
ATOM   1649 H HD13 . ILE   A 1 69  ? 36.362 3.084   -1.738  1.00 17.52 ?  69  ILE   A HD13 1 
ATOM   1650 N N    . ALA   A 1 70  ? 40.001 6.623   -0.447  1.00 12.97 ?  70  ALA   A N    1 
ATOM   1651 C CA   . ALA   A 1 70  ? 41.283 7.230   -0.791  1.00 14.15 ?  70  ALA   A CA   1 
ATOM   1652 C C    . ALA   A 1 70  ? 42.433 6.249   -0.607  1.00 14.76 ?  70  ALA   A C    1 
ATOM   1653 O O    . ALA   A 1 70  ? 43.419 6.304   -1.347  1.00 16.58 ?  70  ALA   A O    1 
ATOM   1654 C CB   . ALA   A 1 70  ? 41.504 8.488   0.054   1.00 14.69 ?  70  ALA   A CB   1 
ATOM   1655 H H    . ALA   A 1 70  ? 39.564 7.019   0.179   1.00 15.56 ?  70  ALA   A H    1 
ATOM   1656 H HA   . ALA   A 1 70  ? 41.257 7.509   -1.724  1.00 16.98 ?  70  ALA   A HA   1 
ATOM   1657 H HB1  . ALA   A 1 70  ? 42.363 8.880   -0.184  1.00 17.63 ?  70  ALA   A HB1  1 
ATOM   1658 H HB2  . ALA   A 1 70  ? 40.795 9.125   -0.119  1.00 17.63 ?  70  ALA   A HB2  1 
ATOM   1659 H HB3  . ALA   A 1 70  ? 41.508 8.242   0.992   1.00 17.63 ?  70  ALA   A HB3  1 
ATOM   1660 N N    . THR   A 1 71  ? 42.321 5.350   0.364   1.00 13.98 ?  71  THR   A N    1 
ATOM   1661 C CA   . THR   A 1 71  ? 43.373 4.370   0.617   1.00 15.87 ?  71  THR   A CA   1 
ATOM   1662 C C    . THR   A 1 71  ? 43.257 3.140   -0.279  1.00 16.10 ?  71  THR   A C    1 
ATOM   1663 O O    . THR   A 1 71  ? 44.275 2.618   -0.761  1.00 18.31 ?  71  THR   A O    1 
ATOM   1664 C CB   . THR   A 1 71  ? 43.296 3.929   2.074   1.00 18.31 ?  71  THR   A CB   1 
ATOM   1665 O OG1  . THR   A 1 71  ? 43.515 5.058   2.925   1.00 19.87 ?  71  THR   A OG1  1 
ATOM   1666 C CG2  . THR   A 1 71  ? 44.320 2.837   2.376   1.00 20.26 ?  71  THR   A CG2  1 
ATOM   1667 H H    . THR   A 1 71  ? 41.640 5.283   0.883   1.00 16.78 ?  71  THR   A H    1 
ATOM   1668 H HA   . THR   A 1 71  ? 44.235 4.782   0.460   1.00 19.04 ?  71  THR   A HA   1 
ATOM   1669 H HB   . THR   A 1 71  ? 42.409 3.564   2.242   1.00 21.98 ?  71  THR   A HB   1 
ATOM   1670 H HG1  . THR   A 1 71  ? 42.916 5.634   2.784   1.00 23.84 ?  71  THR   A HG1  1 
ATOM   1671 H HG21 . THR   A 1 71  ? 44.438 2.754   3.334   1.00 24.31 ?  71  THR   A HG21 1 
ATOM   1672 H HG22 . THR   A 1 71  ? 44.019 1.984   2.022   1.00 24.31 ?  71  THR   A HG22 1 
ATOM   1673 H HG23 . THR   A 1 71  ? 45.173 3.063   1.973   1.00 24.31 ?  71  THR   A HG23 1 
ATOM   1674 N N    . ASN   A 1 72  ? 42.034 2.638   -0.486  1.00 15.04 ?  72  ASN   A N    1 
ATOM   1675 C CA   . ASN   A 1 72  ? 41.818 1.309   -1.048  1.00 15.17 ?  72  ASN   A CA   1 
ATOM   1676 C C    . ASN   A 1 72  ? 41.205 1.299   -2.436  1.00 15.30 ?  72  ASN   A C    1 
ATOM   1677 O O    . ASN   A 1 72  ? 41.209 0.240   -3.080  1.00 16.22 ?  72  ASN   A O    1 
ATOM   1678 C CB   . ASN   A 1 72  ? 40.916 0.504   -0.111  1.00 16.16 ?  72  ASN   A CB   1 
ATOM   1679 C CG   . ASN   A 1 72  ? 41.527 0.337   1.253   1.00 17.31 ?  72  ASN   A CG   1 
ATOM   1680 O OD1  . ASN   A 1 72  ? 41.082 0.926   2.233   1.00 19.21 ?  72  ASN   A OD1  1 
ATOM   1681 N ND2  . ASN   A 1 72  ? 42.575 -0.443  1.318   1.00 17.77 ?  72  ASN   A ND2  1 
ATOM   1682 H H    . ASN   A 1 72  ? 41.307 3.058   -0.307  1.00 18.05 ?  72  ASN   A H    1 
ATOM   1683 H HA   . ASN   A 1 72  ? 42.671 0.855   -1.108  1.00 18.21 ?  72  ASN   A HA   1 
ATOM   1684 H HB2  . ASN   A 1 72  ? 40.069 0.963   -0.016  1.00 19.39 ?  72  ASN   A HB2  1 
ATOM   1685 H HB3  . ASN   A 1 72  ? 40.779 -0.379  -0.490  1.00 19.39 ?  72  ASN   A HB3  1 
ATOM   1686 H HD21 . ASN   A 1 72  ? 42.969 -0.566  2.074   1.00 21.32 ?  72  ASN   A HD21 1 
ATOM   1687 H HD22 . ASN   A 1 72  ? 42.870 -0.834  0.612   1.00 21.32 ?  72  ASN   A HD22 1 
ATOM   1688 N N    . GLY   A 1 73  ? 40.655 2.416   -2.902  1.00 14.39 ?  73  GLY   A N    1 
ATOM   1689 C CA   . GLY   A 1 73  ? 39.921 2.424   -4.141  1.00 14.19 ?  73  GLY   A CA   1 
ATOM   1690 C C    . GLY   A 1 73  ? 38.532 1.848   -3.967  1.00 13.51 ?  73  GLY   A C    1 
ATOM   1691 O O    . GLY   A 1 73  ? 38.143 1.399   -2.880  1.00 14.01 ?  73  GLY   A O    1 
ATOM   1692 H H    . GLY   A 1 73  ? 40.704 3.193   -2.519  1.00 17.27 ?  73  GLY   A H    1 
ATOM   1693 H HA2  . GLY   A 1 73  ? 39.844 3.342   -4.464  1.00 17.03 ?  73  GLY   A HA2  1 
ATOM   1694 H HA3  . GLY   A 1 73  ? 40.396 1.906   -4.807  1.00 17.03 ?  73  GLY   A HA3  1 
ATOM   1695 N N    . PRO   A 1 74  ? 37.760 1.848   -5.048  1.00 13.79 ?  74  PRO   A N    1 
ATOM   1696 C CA   . PRO   A 1 74  ? 36.356 1.430   -4.963  1.00 13.92 ?  74  PRO   A CA   1 
ATOM   1697 C C    . PRO   A 1 74  ? 36.203 -0.053  -4.647  1.00 13.28 ?  74  PRO   A C    1 
ATOM   1698 O O    . PRO   A 1 74  ? 37.070 -0.885  -4.930  1.00 14.29 ?  74  PRO   A O    1 
ATOM   1699 C CB   . PRO   A 1 74  ? 35.813 1.738   -6.365  1.00 15.74 ?  74  PRO   A CB   1 
ATOM   1700 C CG   . PRO   A 1 74  ? 36.781 2.681   -6.982  1.00 19.17 ?  74  PRO   A CG   1 
ATOM   1701 C CD   . PRO   A 1 74  ? 38.110 2.361   -6.381  1.00 15.99 ?  74  PRO   A CD   1 
ATOM   1702 H HA   . PRO   A 1 74  ? 35.881 1.962   -4.301  1.00 16.71 ?  74  PRO   A HA   1 
ATOM   1703 H HB2  . PRO   A 1 74  ? 35.761 0.914   -6.875  1.00 18.88 ?  74  PRO   A HB2  1 
ATOM   1704 H HB3  . PRO   A 1 74  ? 34.937 2.147   -6.288  1.00 18.88 ?  74  PRO   A HB3  1 
ATOM   1705 H HG2  . PRO   A 1 74  ? 36.804 2.543   -7.941  1.00 23.00 ?  74  PRO   A HG2  1 
ATOM   1706 H HG3  . PRO   A 1 74  ? 36.527 3.592   -6.773  1.00 23.00 ?  74  PRO   A HG3  1 
ATOM   1707 H HD2  . PRO   A 1 74  ? 38.568 1.677   -6.897  1.00 19.19 ?  74  PRO   A HD2  1 
ATOM   1708 H HD3  . PRO   A 1 74  ? 38.650 3.169   -6.314  1.00 19.19 ?  74  PRO   A HD3  1 
ATOM   1709 N N    . LEU   A 1 75  ? 35.048 -0.376  -4.066  1.00 12.86 ?  75  LEU   A N    1 
ATOM   1710 C CA   . LEU   A 1 75  ? 34.649 -1.767  -3.923  1.00 12.01 ?  75  LEU   A CA   1 
ATOM   1711 C C    . LEU   A 1 75  ? 34.265 -2.337  -5.285  1.00 12.44 ?  75  LEU   A C    1 
ATOM   1712 O O    . LEU   A 1 75  ? 34.146 -1.617  -6.279  1.00 14.06 ?  75  LEU   A O    1 
ATOM   1713 C CB   . LEU   A 1 75  ? 33.455 -1.891  -2.972  1.00 12.46 ?  75  LEU   A CB   1 
ATOM   1714 C CG   . LEU   A 1 75  ? 33.655 -1.467  -1.521  1.00 13.85 ?  75  LEU   A CG   1 
ATOM   1715 C CD1  . LEU   A 1 75  ? 32.379 -1.702  -0.725  1.00 15.92 ?  75  LEU   A CD1  1 
ATOM   1716 C CD2  . LEU   A 1 75  ? 34.805 -2.168  -0.871  1.00 17.43 ?  75  LEU   A CD2  1 
ATOM   1717 H H    . LEU   A 1 75  ? 34.476 0.197   -3.760  1.00 15.44 ?  75  LEU   A H    1 
ATOM   1718 H HA   . LEU   A 1 75  ? 35.389 -2.276  -3.577  1.00 14.41 ?  75  LEU   A HA   1 
ATOM   1719 H HB2  . LEU   A 1 75  ? 32.731 -1.361  -3.327  1.00 14.96 ?  75  LEU   A HB2  1 
ATOM   1720 H HB3  . LEU   A 1 75  ? 33.192 -2.826  -2.956  1.00 14.96 ?  75  LEU   A HB3  1 
ATOM   1721 H HG   . LEU   A 1 75  ? 33.849 -0.512  -1.503  1.00 16.62 ?  75  LEU   A HG   1 
ATOM   1722 H HD11 . LEU   A 1 75  ? 32.522 -1.419  0.192   1.00 19.10 ?  75  LEU   A HD11 1 
ATOM   1723 H HD12 . LEU   A 1 75  ? 31.661 -1.182  -1.122  1.00 19.10 ?  75  LEU   A HD12 1 
ATOM   1724 H HD13 . LEU   A 1 75  ? 32.160 -2.645  -0.752  1.00 19.10 ?  75  LEU   A HD13 1 
ATOM   1725 H HD21 . LEU   A 1 75  ? 34.848 -1.904  0.061   1.00 20.91 ?  75  LEU   A HD21 1 
ATOM   1726 H HD22 . LEU   A 1 75  ? 34.673 -3.123  -0.943  1.00 20.91 ?  75  LEU   A HD22 1 
ATOM   1727 H HD23 . LEU   A 1 75  ? 35.629 -1.912  -1.321  1.00 20.91 ?  75  LEU   A HD23 1 
ATOM   1728 N N    . LYS   A 1 76  ? 34.071 -3.658  -5.312  1.00 13.10 ?  76  LYS   A N    1 
ATOM   1729 C CA   . LYS   A 1 76  ? 33.477 -4.375  -6.434  1.00 13.62 ?  76  LYS   A CA   1 
ATOM   1730 C C    . LYS   A 1 76  ? 31.963 -4.450  -6.247  1.00 12.34 ?  76  LYS   A C    1 
ATOM   1731 O O    . LYS   A 1 76  ? 31.475 -4.571  -5.124  1.00 12.52 ?  76  LYS   A O    1 
ATOM   1732 C CB   . LYS   A 1 76  ? 34.010 -5.817  -6.480  1.00 15.45 ?  76  LYS   A CB   1 
ATOM   1733 C CG   . LYS   A 1 76  ? 35.521 -5.928  -6.650  1.00 17.29 ?  76  LYS   A CG   1 
ATOM   1734 C CD   . LYS   A 1 76  ? 36.027 -7.346  -6.465  1.00 18.94 ?  76  LYS   A CD   1 
ATOM   1735 C CE   . LYS   A 1 76  ? 37.533 -7.414  -6.664  1.00 20.92 ?  76  LYS   A CE   1 
ATOM   1736 N NZ   . LYS   A 1 76  ? 38.073 -8.770  -6.431  1.00 21.65 ?  76  LYS   A NZ   1 
ATOM   1737 H H    . LYS   A 1 76  ? 34.296 -4.179  -4.661  1.00 15.72 ?  76  LYS   A H    1 
ATOM   1738 H HA   . LYS   A 1 76  ? 33.682 -3.927  -7.271  1.00 16.35 ?  76  LYS   A HA   1 
ATOM   1739 H HB2  . LYS   A 1 76  ? 33.770 -6.259  -5.650  1.00 18.54 ?  76  LYS   A HB2  1 
ATOM   1740 H HB3  . LYS   A 1 76  ? 33.592 -6.275  -7.226  1.00 18.54 ?  76  LYS   A HB3  1 
ATOM   1741 H HG2  . LYS   A 1 76  ? 35.763 -5.638  -7.542  1.00 20.75 ?  76  LYS   A HG2  1 
ATOM   1742 H HG3  . LYS   A 1 76  ? 35.958 -5.369  -5.988  1.00 20.75 ?  76  LYS   A HG3  1 
ATOM   1743 H HD2  . LYS   A 1 76  ? 35.823 -7.653  -5.567  1.00 22.73 ?  76  LYS   A HD2  1 
ATOM   1744 H HD3  . LYS   A 1 76  ? 35.607 -7.930  -7.121  1.00 22.73 ?  76  LYS   A HD3  1 
ATOM   1745 H HE2  . LYS   A 1 76  ? 37.745 -7.158  -7.575  1.00 25.11 ?  76  LYS   A HE2  1 
ATOM   1746 H HE3  . LYS   A 1 76  ? 37.962 -6.810  -6.039  1.00 25.11 ?  76  LYS   A HE3  1 
ATOM   1747 H HZ1  . LYS   A 1 76  ? 38.954 -8.778  -6.556  1.00 25.98 ?  76  LYS   A HZ1  1 
ATOM   1748 H HZ2  . LYS   A 1 76  ? 37.897 -9.035  -5.599  1.00 25.98 ?  76  LYS   A HZ2  1 
ATOM   1749 H HZ3  . LYS   A 1 76  ? 37.700 -9.352  -6.999  1.00 25.98 ?  76  LYS   A HZ3  1 
ATOM   1750 N N    . VAL   A 1 77  ? 31.216 -4.414  -7.355  1.00 12.85 ?  77  VAL   A N    1 
ATOM   1751 C CA   . VAL   A 1 77  ? 29.806 -4.796  -7.268  1.00 12.64 ?  77  VAL   A CA   1 
ATOM   1752 C C    . VAL   A 1 77  ? 29.742 -6.252  -6.829  1.00 12.38 ?  77  VAL   A C    1 
ATOM   1753 O O    . VAL   A 1 77  ? 30.394 -7.121  -7.416  1.00 13.07 ?  77  VAL   A O    1 
ATOM   1754 C CB   . VAL   A 1 77  ? 29.086 -4.574  -8.606  1.00 14.12 ?  77  VAL   A CB   1 
ATOM   1755 C CG1  . VAL   A 1 77  ? 27.620 -4.995  -8.493  1.00 15.09 ?  77  VAL   A CG1  1 
ATOM   1756 C CG2  . VAL   A 1 77  ? 29.195 -3.124  -9.037  1.00 15.52 ?  77  VAL   A CG2  1 
ATOM   1757 H H    . VAL   A 1 77  ? 31.490 -4.176  -8.133  1.00 15.43 ?  77  VAL   A H    1 
ATOM   1758 H HA   . VAL   A 1 77  ? 29.370 -4.252  -6.592  1.00 15.17 ?  77  VAL   A HA   1 
ATOM   1759 H HB   . VAL   A 1 77  ? 29.508 -5.123  -9.284  1.00 16.94 ?  77  VAL   A HB   1 
ATOM   1760 H HG11 . VAL   A 1 77  ? 27.146 -4.692  -9.282  1.00 18.11 ?  77  VAL   A HG11 1 
ATOM   1761 H HG12 . VAL   A 1 77  ? 27.571 -5.963  -8.431  1.00 18.11 ?  77  VAL   A HG12 1 
ATOM   1762 H HG13 . VAL   A 1 77  ? 27.236 -4.591  -7.700  1.00 18.11 ?  77  VAL   A HG13 1 
ATOM   1763 H HG21 . VAL   A 1 77  ? 28.675 -2.996  -9.843  1.00 18.63 ?  77  VAL   A HG21 1 
ATOM   1764 H HG22 . VAL   A 1 77  ? 28.855 -2.558  -8.327  1.00 18.63 ?  77  VAL   A HG22 1 
ATOM   1765 H HG23 . VAL   A 1 77  ? 30.128 -2.913  -9.207  1.00 18.63 ?  77  VAL   A HG23 1 
ATOM   1766 N N    . GLY   A 1 78  ? 28.970 -6.521  -5.779  1.00 11.82 ?  78  GLY   A N    1 
ATOM   1767 C CA   . GLY   A 1 78  ? 28.946 -7.813  -5.130  1.00 12.49 ?  78  GLY   A CA   1 
ATOM   1768 C C    . GLY   A 1 78  ? 29.851 -7.896  -3.922  1.00 12.25 ?  78  GLY   A C    1 
ATOM   1769 O O    . GLY   A 1 78  ? 29.794 -8.893  -3.187  1.00 12.93 ?  78  GLY   A O    1 
ATOM   1770 H H    . GLY   A 1 78  ? 28.429 -5.947  -5.427  1.00 14.19 ?  78  GLY   A H    1 
ATOM   1771 H HA2  . GLY   A 1 78  ? 28.041 -8.011  -4.851  1.00 14.99 ?  78  GLY   A HA2  1 
ATOM   1772 H HA3  . GLY   A 1 78  ? 29.224 -8.491  -5.768  1.00 14.99 ?  78  GLY   A HA3  1 
ATOM   1773 N N    . GLY   A 1 79  ? 30.702 -6.890  -3.703  1.00 11.96 ?  79  GLY   A N    1 
ATOM   1774 C CA   . GLY   A 1 79  ? 31.656 -6.907  -2.617  1.00 11.98 ?  79  GLY   A CA   1 
ATOM   1775 C C    . GLY   A 1 79  ? 31.204 -6.117  -1.402  1.00 11.11 ?  79  GLY   A C    1 
ATOM   1776 O O    . GLY   A 1 79  ? 30.085 -5.606  -1.325  1.00 12.39 ?  79  GLY   A O    1 
ATOM   1777 H H    . GLY   A 1 79  ? 30.745 -6.172  -4.184  1.00 14.35 ?  79  GLY   A H    1 
ATOM   1778 H HA2  . GLY   A 1 79  ? 31.814 -7.829  -2.349  1.00 14.38 ?  79  GLY   A HA2  1 
ATOM   1779 H HA3  . GLY   A 1 79  ? 32.501 -6.539  -2.928  1.00 14.38 ?  79  GLY   A HA3  1 
ATOM   1780 N N    . SER   A 1 80  ? 32.112 -6.018  -0.431  1.00 12.24 ?  80  SER   A N    1 
ATOM   1781 C CA   . SER   A 1 80  ? 31.781 -5.393  0.839   1.00 11.80 ?  80  SER   A CA   1 
ATOM   1782 C C    . SER   A 1 80  ? 33.053 -4.938  1.541   1.00 11.89 ?  80  SER   A C    1 
ATOM   1783 O O    . SER   A 1 80  ? 34.162 -5.383  1.223   1.00 13.45 ?  80  SER   A O    1 
ATOM   1784 C CB   . SER   A 1 80  ? 31.009 -6.354  1.748   1.00 12.75 ?  80  SER   A CB   1 
ATOM   1785 O OG   . SER   A 1 80  ? 31.833 -7.399  2.234   1.00 14.55 ?  80  SER   A OG   1 
ATOM   1786 H H    . SER   A 1 80  ? 32.925 -6.297  -0.491  1.00 14.69 ?  80  SER   A H    1 
ATOM   1787 H HA   . SER   A 1 80  ? 31.226 -4.616  0.662   1.00 14.16 ?  80  SER   A HA   1 
ATOM   1788 H HB2  . SER   A 1 80  ? 30.656 -5.854  2.499   1.00 15.30 ?  80  SER   A HB2  1 
ATOM   1789 H HB3  . SER   A 1 80  ? 30.278 -6.744  1.240   1.00 15.30 ?  80  SER   A HB3  1 
ATOM   1790 H HG   . SER   A 1 80  ? 32.148 -7.836  1.590   1.00 17.46 ?  80  SER   A HG   1 
ATOM   1791 N N    . CYS   A 1 81  ? 32.862 -4.099  2.553   1.00 11.68 ?  81  CYS   A N    1 
ATOM   1792 C CA   . CYS   A 1 81  ? 33.910 -3.807  3.516   1.00 11.94 ?  81  CYS   A CA   1 
ATOM   1793 C C    . CYS   A 1 81  ? 33.266 -3.561  4.874   1.00 11.46 ?  81  CYS   A C    1 
ATOM   1794 O O    . CYS   A 1 81  ? 32.101 -3.155  4.959   1.00 12.94 ?  81  CYS   A O    1 
ATOM   1795 C CB   . CYS   A 1 81  ? 34.776 -2.616  3.093   1.00 12.42 ?  81  CYS   A CB   1 
ATOM   1796 S SG   . CYS   A 1 81  ? 33.895 -1.038  3.114   1.00 12.47 ?  81  CYS   A SG   1 
ATOM   1797 H H    . CYS   A 1 81  ? 32.120 -3.682  2.706   1.00 14.02 ?  81  CYS   A H    1 
ATOM   1798 H HA   . CYS   A 1 81  ? 34.488 -4.580  3.593   1.00 14.32 ?  81  CYS   A HA   1 
ATOM   1799 H HB2  . CYS   A 1 81  ? 35.533 -2.548  3.702   1.00 14.90 ?  81  CYS   A HB2  1 
ATOM   1800 H HB3  . CYS   A 1 81  ? 35.102 -2.769  2.189   1.00 14.90 ?  81  CYS   A HB3  1 
ATOM   1801 H HG   . CYS   A 1 81  ? 34.639 -0.166  2.775   1.00 14.97 ?  81  CYS   A HG   1 
ATOM   1802 N N    . VAL   A 1 82  ? 34.028 -3.833  5.932   1.00 11.76 ?  82  VAL   A N    1 
ATOM   1803 C CA   . VAL   A 1 82  ? 33.605 -3.587  7.305   1.00 12.55 ?  82  VAL   A CA   1 
ATOM   1804 C C    . VAL   A 1 82  ? 34.199 -2.271  7.775   1.00 12.72 ?  82  VAL   A C    1 
ATOM   1805 O O    . VAL   A 1 82  ? 35.425 -2.098  7.766   1.00 13.26 ?  82  VAL   A O    1 
ATOM   1806 C CB   . VAL   A 1 82  ? 34.027 -4.727  8.243   1.00 14.40 ?  82  VAL   A CB   1 
ATOM   1807 C CG1  . VAL   A 1 82  ? 33.564 -4.440  9.663   1.00 16.16 ?  82  VAL   A CG1  1 
ATOM   1808 C CG2  . VAL   A 1 82  ? 33.480 -6.059  7.753   1.00 15.14 ?  82  VAL   A CG2  1 
ATOM   1809 H H    . VAL   A 1 82  ? 34.814 -4.192  5.874   1.00 14.12 ?  82  VAL   A H    1 
ATOM   1810 H HA   . VAL   A 1 82  ? 32.636 -3.506  7.324   1.00 15.05 ?  82  VAL   A HA   1 
ATOM   1811 H HB   . VAL   A 1 82  ? 34.993 -4.775  8.249   1.00 17.28 ?  82  VAL   A HB   1 
ATOM   1812 H HG11 . VAL   A 1 82  ? 33.672 -5.242  10.193  1.00 19.39 ?  82  VAL   A HG11 1 
ATOM   1813 H HG12 . VAL   A 1 82  ? 34.098 -3.721  10.037  1.00 19.39 ?  82  VAL   A HG12 1 
ATOM   1814 H HG13 . VAL   A 1 82  ? 32.627 -4.179  9.645   1.00 19.39 ?  82  VAL   A HG13 1 
ATOM   1815 H HG21 . VAL   A 1 82  ? 33.713 -6.746  8.394   1.00 18.17 ?  82  VAL   A HG21 1 
ATOM   1816 H HG22 . VAL   A 1 82  ? 32.515 -5.993  7.671   1.00 18.17 ?  82  VAL   A HG22 1 
ATOM   1817 H HG23 . VAL   A 1 82  ? 33.871 -6.263  6.889   1.00 18.17 ?  82  VAL   A HG23 1 
ATOM   1818 N N    . LEU   A 1 83  ? 33.342 -1.346  8.191   1.00 12.28 ?  83  LEU   A N    1 
ATOM   1819 C CA   . LEU   A 1 83  ? 33.771 -0.082  8.771   1.00 11.95 ?  83  LEU   A CA   1 
ATOM   1820 C C    . LEU   A 1 83  ? 33.042 0.107   10.097  1.00 12.07 ?  83  LEU   A C    1 
ATOM   1821 O O    . LEU   A 1 83  ? 32.317 -0.783  10.565  1.00 12.85 ?  83  LEU   A O    1 
ATOM   1822 C CB   . LEU   A 1 83  ? 33.531 1.081   7.798   1.00 12.60 ?  83  LEU   A CB   1 
ATOM   1823 C CG   . LEU   A 1 83  ? 34.417 1.069   6.550   1.00 13.21 ?  83  LEU   A CG   1 
ATOM   1824 C CD1  . LEU   A 1 83  ? 33.994 2.138   5.561   1.00 13.63 ?  83  LEU   A CD1  1 
ATOM   1825 C CD2  . LEU   A 1 83  ? 35.901 1.240   6.912   1.00 14.18 ?  83  LEU   A CD2  1 
ATOM   1826 H H    . LEU   A 1 83  ? 32.487 -1.427  8.149   1.00 14.74 ?  83  LEU   A H    1 
ATOM   1827 H HA   . LEU   A 1 83  ? 34.722 -0.117  8.956   1.00 14.34 ?  83  LEU   A HA   1 
ATOM   1828 H HB2  . LEU   A 1 83  ? 32.606 1.053   7.497   1.00 15.12 ?  83  LEU   A HB2  1 
ATOM   1829 H HB3  . LEU   A 1 83  ? 33.691 1.919   8.260   1.00 15.12 ?  83  LEU   A HB3  1 
ATOM   1830 H HG   . LEU   A 1 83  ? 34.320 0.211   6.112   1.00 15.85 ?  83  LEU   A HG   1 
ATOM   1831 H HD11 . LEU   A 1 83  ? 34.576 2.094   4.782   1.00 16.36 ?  83  LEU   A HD11 1 
ATOM   1832 H HD12 . LEU   A 1 83  ? 33.077 1.977   5.294   1.00 16.36 ?  83  LEU   A HD12 1 
ATOM   1833 H HD13 . LEU   A 1 83  ? 34.071 3.008   5.980   1.00 16.36 ?  83  LEU   A HD13 1 
ATOM   1834 H HD21 . LEU   A 1 83  ? 36.413 1.375   6.095   1.00 17.02 ?  83  LEU   A HD21 1 
ATOM   1835 H HD22 . LEU   A 1 83  ? 36.003 2.010   7.492   1.00 17.02 ?  83  LEU   A HD22 1 
ATOM   1836 H HD23 . LEU   A 1 83  ? 36.214 0.441   7.364   1.00 17.02 ?  83  LEU   A HD23 1 
ATOM   1837 N N    . SER   A 1 84  ? 33.263 1.257   10.728  1.00 13.09 ?  84  SER   A N    1 
ATOM   1838 C CA   . SER   A 1 84  ? 32.615 1.527   12.001  1.00 12.88 ?  84  SER   A CA   1 
ATOM   1839 C C    . SER   A 1 84  ? 31.095 1.619   11.847  1.00 12.74 ?  84  SER   A C    1 
ATOM   1840 O O    . SER   A 1 84  ? 30.574 2.082   10.830  1.00 13.28 ?  84  SER   A O    1 
ATOM   1841 C CB   . SER   A 1 84  ? 33.119 2.849   12.573  1.00 13.75 ?  84  SER   A CB   1 
ATOM   1842 O OG   . SER   A 1 84  ? 32.492 3.125   13.806  1.00 15.13 ?  84  SER   A OG   1 
ATOM   1843 H H    . SER   A 1 84  ? 33.774 1.889   10.442  1.00 15.71 ?  84  SER   A H    1 
ATOM   1844 H HA   . SER   A 1 84  ? 32.826 0.818   12.628  1.00 15.46 ?  84  SER   A HA   1 
ATOM   1845 H HB2  . SER   A 1 84  ? 34.078 2.792   12.709  1.00 16.50 ?  84  SER   A HB2  1 
ATOM   1846 H HB3  . SER   A 1 84  ? 32.913 3.564   11.950  1.00 16.50 ?  84  SER   A HB3  1 
ATOM   1847 H HG   . SER   A 1 84  ? 32.777 3.856   14.120  1.00 18.16 ?  84  SER   A HG   1 
ATOM   1848 N N    . GLY   A 1 85  ? 30.379 1.223   12.899  1.00 13.99 ?  85  GLY   A N    1 
ATOM   1849 C CA   . GLY   A 1 85  ? 28.951 1.456   12.976  1.00 14.47 ?  85  GLY   A CA   1 
ATOM   1850 C C    . GLY   A 1 85  ? 28.580 2.772   13.621  1.00 14.23 ?  85  GLY   A C    1 
ATOM   1851 O O    . GLY   A 1 85  ? 27.388 3.086   13.725  1.00 15.25 ?  85  GLY   A O    1 
ATOM   1852 H H    . GLY   A 1 85  ? 30.702 0.813   13.585  1.00 16.79 ?  85  GLY   A H    1 
ATOM   1853 H HA2  . GLY   A 1 85  ? 28.580 1.446   12.080  1.00 17.36 ?  85  GLY   A HA2  1 
ATOM   1854 H HA3  . GLY   A 1 85  ? 28.538 0.747   13.484  1.00 17.36 ?  85  GLY   A HA3  1 
ATOM   1855 N N    . HIS   A 1 86  ? 29.566 3.547   14.071  1.00 13.92 ?  86  HIS   A N    1 
ATOM   1856 C CA   . HIS   A 1 86  ? 29.344 4.889   14.629  1.00 14.39 ?  86  HIS   A CA   1 
ATOM   1857 C C    . HIS   A 1 86  ? 28.354 4.777   15.782  1.00 15.04 ?  86  HIS   A C    1 
ATOM   1858 O O    . HIS   A 1 86  ? 28.542 3.914   16.655  1.00 16.68 ?  86  HIS   A O    1 
ATOM   1859 C CB   . HIS   A 1 86  ? 28.977 5.864   13.517  1.00 14.42 ?  86  HIS   A CB   1 
ATOM   1860 C CG   . HIS   A 1 86  ? 30.039 5.958   12.482  1.00 14.18 ?  86  HIS   A CG   1 
ATOM   1861 N ND1  . HIS   A 1 86  ? 31.136 6.779   12.625  1.00 15.74 ?  86  HIS   A ND1  1 
ATOM   1862 C CD2  . HIS   A 1 86  ? 30.225 5.270   11.334  1.00 14.34 ?  86  HIS   A CD2  1 
ATOM   1863 C CE1  . HIS   A 1 86  ? 31.940 6.609   11.591  1.00 14.72 ?  86  HIS   A CE1  1 
ATOM   1864 N NE2  . HIS   A 1 86  ? 31.412 5.698   10.796  1.00 14.70 ?  86  HIS   A NE2  1 
ATOM   1865 H H    . HIS   A 1 86  ? 30.386 3.315   14.076  1.00 16.70 ?  86  HIS   A H    1 
ATOM   1866 H HA   . HIS   A 1 86  ? 30.176 5.202   15.004  1.00 17.27 ?  86  HIS   A HA   1 
ATOM   1867 H HB2  . HIS   A 1 86  ? 28.156 5.571   13.084  1.00 17.30 ?  86  HIS   A HB2  1 
ATOM   1868 H HB3  . HIS   A 1 86  ? 28.846 6.753   13.894  1.00 17.30 ?  86  HIS   A HB3  1 
ATOM   1869 H HD2  . HIS   A 1 86  ? 29.654 4.624   10.976  1.00 17.21 ?  86  HIS   A HD2  1 
ATOM   1870 H HE1  . HIS   A 1 86  ? 32.737 7.058   11.438  1.00 17.67 ?  86  HIS   A HE1  1 
ATOM   1871 H HE2  . HIS   A 1 86  ? 31.749 5.422   10.049  1.00 17.64 ?  86  HIS   A HE2  1 
ATOM   1872 N N    . ASN   A 1 87  ? 27.334 5.621   15.839  1.00 16.07 ?  87  ASN   A N    1 
ATOM   1873 C CA   . ASN   A 1 87  ? 26.353 5.618   16.908  1.00 17.17 ?  87  ASN   A CA   1 
ATOM   1874 C C    . ASN   A 1 87  ? 25.222 4.628   16.678  1.00 18.42 ?  87  ASN   A C    1 
ATOM   1875 O O    . ASN   A 1 87  ? 24.298 4.574   17.492  1.00 20.93 ?  87  ASN   A O    1 
ATOM   1876 C CB   . ASN   A 1 87  ? 25.764 7.029   17.055  1.00 18.27 ?  87  ASN   A CB   1 
ATOM   1877 C CG   . ASN   A 1 87  ? 25.249 7.587   15.736  1.00 18.93 ?  87  ASN   A CG   1 
ATOM   1878 O OD1  . ASN   A 1 87  ? 25.894 7.457   14.697  1.00 19.24 ?  87  ASN   A OD1  1 
ATOM   1879 N ND2  . ASN   A 1 87  ? 24.082 8.204   15.773  1.00 20.04 ?  87  ASN   A ND2  1 
ATOM   1880 H H    . ASN   A 1 87  ? 27.182 6.224   15.246  1.00 19.28 ?  87  ASN   A H    1 
ATOM   1881 H HA   . ASN   A 1 87  ? 26.783 5.384   17.747  1.00 20.61 ?  87  ASN   A HA   1 
ATOM   1882 H HB2  . ASN   A 1 87  ? 25.022 6.999   17.684  1.00 21.93 ?  87  ASN   A HB2  1 
ATOM   1883 H HB3  . ASN   A 1 87  ? 26.453 7.625   17.387  1.00 21.93 ?  87  ASN   A HB3  1 
ATOM   1884 H HD21 . ASN   A 1 87  ? 23.750 8.530   15.052  1.00 24.05 ?  87  ASN   A HD21 1 
ATOM   1885 H HD22 . ASN   A 1 87  ? 23.661 8.285   16.519  1.00 24.05 ?  87  ASN   A HD22 1 
ATOM   1886 N N    A LEU   A 1 88  ? 25.278 3.844   15.606  0.80 17.08 ?  88  LEU   A N    1 
ATOM   1887 N N    B LEU   A 1 88  ? 25.274 3.833   15.609  0.20 18.09 ?  88  LEU   A N    1 
ATOM   1888 C CA   A LEU   A 1 88  ? 24.169 2.979   15.213  0.80 17.01 ?  88  LEU   A CA   1 
ATOM   1889 C CA   B LEU   A 1 88  ? 24.157 2.979   15.225  0.20 17.96 ?  88  LEU   A CA   1 
ATOM   1890 C C    A LEU   A 1 88  ? 24.388 1.503   15.501  0.80 16.47 ?  88  LEU   A C    1 
ATOM   1891 C C    B LEU   A 1 88  ? 24.388 1.496   15.479  0.20 17.24 ?  88  LEU   A C    1 
ATOM   1892 O O    A LEU   A 1 88  ? 23.410 0.773   15.682  0.80 17.79 ?  88  LEU   A O    1 
ATOM   1893 O O    B LEU   A 1 88  ? 23.412 0.755   15.629  0.20 17.61 ?  88  LEU   A O    1 
ATOM   1894 C CB   A LEU   A 1 88  ? 23.903 3.133   13.713  0.80 17.56 ?  88  LEU   A CB   1 
ATOM   1895 C CB   B LEU   A 1 88  ? 23.840 3.171   13.735  0.20 18.53 ?  88  LEU   A CB   1 
ATOM   1896 C CG   A LEU   A 1 88  ? 23.605 4.547   13.208  0.80 18.51 ?  88  LEU   A CG   1 
ATOM   1897 C CG   B LEU   A 1 88  ? 23.560 4.613   13.303  0.20 18.95 ?  88  LEU   A CG   1 
ATOM   1898 C CD1  A LEU   A 1 88  ? 23.466 4.533   11.699  0.80 19.24 ?  88  LEU   A CD1  1 
ATOM   1899 C CD1  B LEU   A 1 88  ? 23.467 4.721   11.789  0.20 19.08 ?  88  LEU   A CD1  1 
ATOM   1900 C CD2  A LEU   A 1 88  ? 22.349 5.113   13.859  0.80 20.28 ?  88  LEU   A CD2  1 
ATOM   1901 C CD2  B LEU   A 1 88  ? 22.289 5.132   13.958  0.20 19.39 ?  88  LEU   A CD2  1 
ATOM   1902 H H    A LEU   A 1 88  ? 25.965 3.787   15.094  0.80 20.49 ?  88  LEU   A H    1 
ATOM   1903 H H    B LEU   A 1 88  ? 25.958 3.769   15.096  0.20 21.71 ?  88  LEU   A H    1 
ATOM   1904 H HA   A LEU   A 1 88  ? 23.375 3.259   15.688  0.80 20.42 ?  88  LEU   A HA   1 
ATOM   1905 H HA   B LEU   A 1 88  ? 23.373 3.245   15.727  0.20 21.55 ?  88  LEU   A HA   1 
ATOM   1906 H HB2  A LEU   A 1 88  ? 24.678 2.819   13.229  0.80 21.07 ?  88  LEU   A HB2  1 
ATOM   1907 H HB2  B LEU   A 1 88  ? 24.595 2.853   13.217  0.20 22.23 ?  88  LEU   A HB2  1 
ATOM   1908 H HB3  A LEU   A 1 88  ? 23.135 2.586   13.487  0.80 21.07 ?  88  LEU   A HB3  1 
ATOM   1909 H HB3  B LEU   A 1 88  ? 23.055 2.644   13.520  0.20 22.23 ?  88  LEU   A HB3  1 
ATOM   1910 H HG   A LEU   A 1 88  ? 24.345 5.131   13.434  0.80 22.21 ?  88  LEU   A HG   1 
ATOM   1911 H HG   B LEU   A 1 88  ? 24.293 5.175   13.594  0.20 22.75 ?  88  LEU   A HG   1 
ATOM   1912 H HD11 A LEU   A 1 88  ? 23.279 5.434   11.389  0.80 23.09 ?  88  LEU   A HD11 1 
ATOM   1913 H HD11 B LEU   A 1 88  ? 23.302 5.647   11.549  0.20 22.89 ?  88  LEU   A HD11 1 
ATOM   1914 H HD12 A LEU   A 1 88  ? 24.294 4.215   11.309  0.80 23.09 ?  88  LEU   A HD12 1 
ATOM   1915 H HD12 B LEU   A 1 88  ? 24.304 4.424   11.399  0.20 22.89 ?  88  LEU   A HD12 1 
ATOM   1916 H HD13 A LEU   A 1 88  ? 22.736 3.943   11.454  0.80 23.09 ?  88  LEU   A HD13 1 
ATOM   1917 H HD13 B LEU   A 1 88  ? 22.738 4.163   11.475  0.20 22.89 ?  88  LEU   A HD13 1 
ATOM   1918 H HD21 A LEU   A 1 88  ? 22.151 5.977   13.465  0.80 24.34 ?  88  LEU   A HD21 1 
ATOM   1919 H HD21 B LEU   A 1 88  ? 22.093 6.015   13.609  0.20 23.26 ?  88  LEU   A HD21 1 
ATOM   1920 H HD22 A LEU   A 1 88  ? 21.612 4.502   13.703  0.80 24.34 ?  88  LEU   A HD22 1 
ATOM   1921 H HD22 B LEU   A 1 88  ? 21.559 4.526   13.756  0.20 23.26 ?  88  LEU   A HD22 1 
ATOM   1922 H HD23 A LEU   A 1 88  ? 22.504 5.210   14.810  0.80 24.34 ?  88  LEU   A HD23 1 
ATOM   1923 H HD23 B LEU   A 1 88  ? 22.424 5.178   14.917  0.20 23.26 ?  88  LEU   A HD23 1 
ATOM   1924 N N    . ALA   A 1 89  ? 25.639 1.050   15.524  1.00 16.30 ?  89  ALA   A N    1 
ATOM   1925 C CA   . ALA   A 1 89  ? 25.975 -0.360  15.654  1.00 15.93 ?  89  ALA   A CA   1 
ATOM   1926 C C    . ALA   A 1 89  ? 27.459 -0.427  15.981  1.00 16.14 ?  89  ALA   A C    1 
ATOM   1927 O O    . ALA   A 1 89  ? 28.178 0.565   15.852  1.00 17.11 ?  89  ALA   A O    1 
ATOM   1928 C CB   . ALA   A 1 89  ? 25.720 -1.086  14.337  1.00 15.58 ?  89  ALA   A CB   1 
ATOM   1929 H H    A ALA   A 1 89  ? 26.330 1.560   15.460  0.80 19.56 ?  89  ALA   A H    1 
ATOM   1930 H H    B ALA   A 1 89  ? 26.329 1.563   15.471  0.20 19.56 ?  89  ALA   A H    1 
ATOM   1931 H HA   . ALA   A 1 89  ? 25.456 -0.770  16.365  1.00 19.12 ?  89  ALA   A HA   1 
ATOM   1932 H HB1  . ALA   A 1 89  ? 25.967 -2.018  14.437  1.00 18.70 ?  89  ALA   A HB1  1 
ATOM   1933 H HB2  . ALA   A 1 89  ? 24.781 -1.013  14.108  1.00 18.70 ?  89  ALA   A HB2  1 
ATOM   1934 H HB3  . ALA   A 1 89  ? 26.262 -0.675  13.642  1.00 18.70 ?  89  ALA   A HB3  1 
ATOM   1935 N N    . LYS   A 1 90  ? 27.930 -1.604  16.388  1.00 16.66 ?  90  LYS   A N    1 
ATOM   1936 C CA   . LYS   A 1 90  ? 29.374 -1.766  16.530  1.00 17.72 ?  90  LYS   A CA   1 
ATOM   1937 C C    . LYS   A 1 90  ? 30.071 -1.575  15.186  1.00 16.53 ?  90  LYS   A C    1 
ATOM   1938 O O    . LYS   A 1 90  ? 31.000 -0.761  15.057  1.00 17.73 ?  90  LYS   A O    1 
ATOM   1939 C CB   . LYS   A 1 90  ? 29.705 -3.132  17.127  1.00 20.63 ?  90  LYS   A CB   1 
ATOM   1940 C CG   . LYS   A 1 90  ? 31.188 -3.298  17.447  1.00 26.93 ?  90  LYS   A CG   1 
ATOM   1941 C CD   . LYS   A 1 90  ? 31.430 -4.493  18.358  1.00 33.64 ?  90  LYS   A CD   1 
ATOM   1942 C CE   . LYS   A 1 90  ? 32.850 -4.502  18.910  1.00 39.36 ?  90  LYS   A CE   1 
ATOM   1943 N NZ   . LYS   A 1 90  ? 33.842 -5.040  17.936  1.00 42.52 ?  90  LYS   A NZ   1 
ATOM   1944 H H    . LYS   A 1 90  ? 27.449 -2.288  16.584  1.00 19.99 ?  90  LYS   A H    1 
ATOM   1945 H HA   . LYS   A 1 90  ? 29.702 -1.086  17.133  1.00 21.27 ?  90  LYS   A HA   1 
ATOM   1946 H HB2  . LYS   A 1 90  ? 29.203 -3.246  17.953  1.00 24.75 ?  90  LYS   A HB2  1 
ATOM   1947 H HB3  . LYS   A 1 90  ? 29.454 -3.826  16.496  1.00 24.75 ?  90  LYS   A HB3  1 
ATOM   1948 H HG2  . LYS   A 1 90  ? 31.680 -3.437  16.623  1.00 32.31 ?  90  LYS   A HG2  1 
ATOM   1949 H HG3  . LYS   A 1 90  ? 31.508 -2.501  17.899  1.00 32.31 ?  90  LYS   A HG3  1 
ATOM   1950 H HD2  . LYS   A 1 90  ? 30.814 -4.456  19.107  1.00 40.36 ?  90  LYS   A HD2  1 
ATOM   1951 H HD3  . LYS   A 1 90  ? 31.295 -5.312  17.854  1.00 40.36 ?  90  LYS   A HD3  1 
ATOM   1952 H HE2  . LYS   A 1 90  ? 33.110 -3.594  19.132  1.00 47.24 ?  90  LYS   A HE2  1 
ATOM   1953 H HE3  . LYS   A 1 90  ? 32.878 -5.058  19.704  1.00 47.24 ?  90  LYS   A HE3  1 
ATOM   1954 H HZ1  . LYS   A 1 90  ? 34.652 -5.058  18.307  1.00 51.02 ?  90  LYS   A HZ1  1 
ATOM   1955 H HZ2  . LYS   A 1 90  ? 33.616 -5.867  17.697  1.00 51.02 ?  90  LYS   A HZ2  1 
ATOM   1956 H HZ3  . LYS   A 1 90  ? 33.867 -4.525  17.212  1.00 51.02 ?  90  LYS   A HZ3  1 
ATOM   1957 N N    . HIS   A 1 91  ? 29.606 -2.294  14.167  1.00 14.31 ?  91  HIS   A N    1 
ATOM   1958 C CA   . HIS   A 1 91  ? 30.187 -2.292  12.837  1.00 13.52 ?  91  HIS   A CA   1 
ATOM   1959 C C    . HIS   A 1 91  ? 29.111 -2.010  11.802  1.00 12.16 ?  91  HIS   A C    1 
ATOM   1960 O O    . HIS   A 1 91  ? 27.941 -2.372  11.982  1.00 13.47 ?  91  HIS   A O    1 
ATOM   1961 C CB   . HIS   A 1 91  ? 30.772 -3.662  12.477  1.00 16.08 ?  91  HIS   A CB   1 
ATOM   1962 C CG   . HIS   A 1 91  ? 31.777 -4.172  13.457  1.00 20.57 ?  91  HIS   A CG   1 
ATOM   1963 N ND1  . HIS   A 1 91  ? 33.060 -3.674  13.535  1.00 22.75 ?  91  HIS   A ND1  1 
ATOM   1964 C CD2  . HIS   A 1 91  ? 31.696 -5.147  14.393  1.00 22.79 ?  91  HIS   A CD2  1 
ATOM   1965 C CE1  . HIS   A 1 91  ? 33.724 -4.316  14.480  1.00 23.98 ?  91  HIS   A CE1  1 
ATOM   1966 N NE2  . HIS   A 1 91  ? 32.920 -5.219  15.014  1.00 24.21 ?  91  HIS   A NE2  1 
ATOM   1967 H H    . HIS   A 1 91  ? 28.917 -2.819  14.228  1.00 17.17 ?  91  HIS   A H    1 
ATOM   1968 H HA   . HIS   A 1 91  ? 30.885 -1.621  12.772  1.00 16.23 ?  91  HIS   A HA   1 
ATOM   1969 H HB2  . HIS   A 1 91  ? 30.049 -4.309  12.436  1.00 19.29 ?  91  HIS   A HB2  1 
ATOM   1970 H HB3  . HIS   A 1 91  ? 31.205 -3.601  11.611  1.00 19.29 ?  91  HIS   A HB3  1 
ATOM   1971 H HD1  . HIS   A 1 91  ? 33.380 -3.043  13.040  1.00 27.30 ?  91  HIS   A HD1  1 
ATOM   1972 H HD2  . HIS   A 1 91  ? 30.956 -5.670  14.584  1.00 27.35 ?  91  HIS   A HD2  1 
ATOM   1973 H HE1  . HIS   A 1 91  ? 34.611 -4.157  14.722  1.00 28.78 ?  91  HIS   A HE1  1 
ATOM   1974 N N    . CYS   A 1 92  ? 29.525 -1.415  10.686  1.00 12.25 ?  92  CYS   A N    1 
ATOM   1975 C CA   . CYS   A 1 92  ? 28.697 -1.344  9.491   1.00 11.73 ?  92  CYS   A CA   1 
ATOM   1976 C C    . CYS   A 1 92  ? 29.348 -2.166  8.390   1.00 11.86 ?  92  CYS   A C    1 
ATOM   1977 O O    . CYS   A 1 92  ? 30.503 -1.917  8.025   1.00 12.58 ?  92  CYS   A O    1 
ATOM   1978 C CB   . CYS   A 1 92  ? 28.482 0.097   9.029   1.00 12.43 ?  92  CYS   A CB   1 
ATOM   1979 S SG   . CYS   A 1 92  ? 27.494 0.202   7.516   1.00 12.08 ?  92  CYS   A SG   1 
ATOM   1980 H H    . CYS   A 1 92  ? 30.298 -1.031  10.601  1.00 14.70 ?  92  CYS   A H    1 
ATOM   1981 H HA   . CYS   A 1 92  ? 27.832 -1.732  9.689   1.00 14.08 ?  92  CYS   A HA   1 
ATOM   1982 H HB2  . CYS   A 1 92  ? 28.011 0.589   9.725   1.00 14.91 ?  92  CYS   A HB2  1 
ATOM   1983 H HB3  . CYS   A 1 92  ? 29.339 0.511   8.857   1.00 14.91 ?  92  CYS   A HB3  1 
ATOM   1984 H HG   . CYS   A 1 92  ? 27.358 1.356   7.221   1.00 14.50 ?  92  CYS   A HG   1 
ATOM   1985 N N    . LEU   A 1 93  ? 28.616 -3.152  7.886   1.00 11.48 ?  93  LEU   A N    1 
ATOM   1986 C CA   . LEU   A 1 93  ? 29.023 -3.907  6.707   1.00 10.58 ?  93  LEU   A CA   1 
ATOM   1987 C C    . LEU   A 1 93  ? 28.433 -3.222  5.480   1.00 10.75 ?  93  LEU   A C    1 
ATOM   1988 O O    . LEU   A 1 93  ? 27.218 -3.275  5.252   1.00 10.96 ?  93  LEU   A O    1 
ATOM   1989 C CB   . LEU   A 1 93  ? 28.545 -5.355  6.821   1.00 11.91 ?  93  LEU   A CB   1 
ATOM   1990 C CG   . LEU   A 1 93  ? 28.935 -6.248  5.645   1.00 12.36 ?  93  LEU   A CG   1 
ATOM   1991 C CD1  . LEU   A 1 93  ? 30.442 -6.527  5.631   1.00 13.22 ?  93  LEU   A CD1  1 
ATOM   1992 C CD2  . LEU   A 1 93  ? 28.160 -7.562  5.696   1.00 13.06 ?  93  LEU   A CD2  1 
ATOM   1993 H H    . LEU   A 1 93  ? 27.863 -3.405  8.221   1.00 13.78 ?  93  LEU   A H    1 
ATOM   1994 H HA   . LEU   A 1 93  ? 29.987 -3.894  6.635   1.00 12.69 ?  93  LEU   A HA   1 
ATOM   1995 H HB2  . LEU   A 1 93  ? 28.929 -5.741  7.626   1.00 14.29 ?  93  LEU   A HB2  1 
ATOM   1996 H HB3  . LEU   A 1 93  ? 27.579 -5.359  6.887   1.00 14.29 ?  93  LEU   A HB3  1 
ATOM   1997 H HG   . LEU   A 1 93  ? 28.713 -5.797  4.819   1.00 14.83 ?  93  LEU   A HG   1 
ATOM   1998 H HD11 . LEU   A 1 93  ? 30.649 -7.122  4.897   1.00 15.86 ?  93  LEU   A HD11 1 
ATOM   1999 H HD12 . LEU   A 1 93  ? 30.923 -5.689  5.524   1.00 15.86 ?  93  LEU   A HD12 1 
ATOM   2000 H HD13 . LEU   A 1 93  ? 30.696 -6.941  6.475   1.00 15.86 ?  93  LEU   A HD13 1 
ATOM   2001 H HD21 . LEU   A 1 93  ? 28.426 -8.110  4.941   1.00 15.67 ?  93  LEU   A HD21 1 
ATOM   2002 H HD22 . LEU   A 1 93  ? 28.361 -8.016  6.526   1.00 15.67 ?  93  LEU   A HD22 1 
ATOM   2003 H HD23 . LEU   A 1 93  ? 27.211 -7.365  5.644   1.00 15.67 ?  93  LEU   A HD23 1 
ATOM   2004 N N    . HIS   A 1 94  ? 29.279 -2.532  4.720   1.00 10.59 ?  94  HIS   A N    1 
ATOM   2005 C CA   . HIS   A 1 94  ? 28.858 -1.860  3.494   1.00 10.36 ?  94  HIS   A CA   1 
ATOM   2006 C C    . HIS   A 1 94  ? 28.876 -2.896  2.383   1.00 10.63 ?  94  HIS   A C    1 
ATOM   2007 O O    . HIS   A 1 94  ? 29.942 -3.432  2.056   1.00 12.20 ?  94  HIS   A O    1 
ATOM   2008 C CB   . HIS   A 1 94  ? 29.825 -0.721  3.168   1.00 10.62 ?  94  HIS   A CB   1 
ATOM   2009 C CG   . HIS   A 1 94  ? 29.816 0.376   4.181   1.00 10.59 ?  94  HIS   A CG   1 
ATOM   2010 N ND1  . HIS   A 1 94  ? 28.944 1.444   4.118   1.00 10.52 ?  94  HIS   A ND1  1 
ATOM   2011 C CD2  . HIS   A 1 94  ? 30.543 0.543   5.307   1.00 11.31 ?  94  HIS   A CD2  1 
ATOM   2012 C CE1  . HIS   A 1 94  ? 29.159 2.233   5.156   1.00 11.00 ?  94  HIS   A CE1  1 
ATOM   2013 N NE2  . HIS   A 1 94  ? 30.118 1.705   5.894   1.00 11.30 ?  94  HIS   A NE2  1 
ATOM   2014 H H    . HIS   A 1 94  ? 30.116 -2.431  4.888   1.00 12.71 ?  94  HIS   A H    1 
ATOM   2015 H HA   . HIS   A 1 94  ? 27.957 -1.499  3.589   1.00 12.43 ?  94  HIS   A HA   1 
ATOM   2016 H HB2  . HIS   A 1 94  ? 30.721 -1.073  3.120   1.00 12.74 ?  94  HIS   A HB2  1 
ATOM   2017 H HB3  . HIS   A 1 94  ? 29.575 -0.330  2.310   1.00 12.74 ?  94  HIS   A HB3  1 
ATOM   2018 H HD2  . HIS   A 1 94  ? 31.212 -0.015  5.618   1.00 13.57 ?  94  HIS   A HD2  1 
ATOM   2019 H HE1  . HIS   A 1 94  ? 28.696 3.024   5.333   1.00 13.20 ?  94  HIS   A HE1  1 
ATOM   2020 H HE2  . HIS   A 1 94  ? 30.428 2.051   6.615   1.00 13.56 ?  94  HIS   A HE2  1 
ATOM   2021 N N    . VAL   A 1 95  ? 27.707 -3.227  1.837   1.00 10.09 ?  95  VAL   A N    1 
ATOM   2022 C CA   . VAL   A 1 95  ? 27.571 -4.261  0.816   1.00 10.23 ?  95  VAL   A CA   1 
ATOM   2023 C C    . VAL   A 1 95  ? 27.028 -3.627  -0.452  1.00 9.76  ?  95  VAL   A C    1 
ATOM   2024 O O    . VAL   A 1 95  ? 26.025 -2.905  -0.401  1.00 10.99 ?  95  VAL   A O    1 
ATOM   2025 C CB   . VAL   A 1 95  ? 26.645 -5.403  1.270   1.00 10.74 ?  95  VAL   A CB   1 
ATOM   2026 C CG1  . VAL   A 1 95  ? 26.537 -6.449  0.164   1.00 11.63 ?  95  VAL   A CG1  1 
ATOM   2027 C CG2  . VAL   A 1 95  ? 27.146 -6.021  2.558   1.00 10.88 ?  95  VAL   A CG2  1 
ATOM   2028 H H    . VAL   A 1 95  ? 26.957 -2.871  2.054   1.00 12.11 ?  95  VAL   A H    1 
ATOM   2029 H HA   . VAL   A 1 95  ? 28.439 -4.642  0.617   1.00 12.28 ?  95  VAL   A HA   1 
ATOM   2030 H HB   . VAL   A 1 95  ? 25.759 -5.055  1.432   1.00 12.88 ?  95  VAL   A HB   1 
ATOM   2031 H HG11 . VAL   A 1 95  ? 26.153 -7.265  0.529   1.00 13.95 ?  95  VAL   A HG11 1 
ATOM   2032 H HG12 . VAL   A 1 95  ? 25.963 -6.110  -0.544  1.00 13.95 ?  95  VAL   A HG12 1 
ATOM   2033 H HG13 . VAL   A 1 95  ? 27.421 -6.636  -0.190  1.00 13.95 ?  95  VAL   A HG13 1 
ATOM   2034 H HG21 . VAL   A 1 95  ? 26.591 -6.789  2.779   1.00 13.05 ?  95  VAL   A HG21 1 
ATOM   2035 H HG22 . VAL   A 1 95  ? 28.065 -6.303  2.439   1.00 13.05 ?  95  VAL   A HG22 1 
ATOM   2036 H HG23 . VAL   A 1 95  ? 27.087 -5.360  3.263   1.00 13.05 ?  95  VAL   A HG23 1 
ATOM   2037 N N    . VAL   A 1 96  ? 27.660 -3.925  -1.589  1.00 10.15 ?  96  VAL   A N    1 
ATOM   2038 C CA   . VAL   A 1 96  ? 27.253 -3.379  -2.877  1.00 10.44 ?  96  VAL   A CA   1 
ATOM   2039 C C    . VAL   A 1 96  ? 26.454 -4.434  -3.633  1.00 11.13 ?  96  VAL   A C    1 
ATOM   2040 O O    . VAL   A 1 96  ? 27.017 -5.376  -4.193  1.00 11.96 ?  96  VAL   A O    1 
ATOM   2041 C CB   . VAL   A 1 96  ? 28.448 -2.893  -3.694  1.00 10.84 ?  96  VAL   A CB   1 
ATOM   2042 C CG1  . VAL   A 1 96  ? 27.953 -2.265  -4.970  1.00 11.30 ?  96  VAL   A CG1  1 
ATOM   2043 C CG2  . VAL   A 1 96  ? 29.296 -1.926  -2.888  1.00 11.63 ?  96  VAL   A CG2  1 
ATOM   2044 H H    . VAL   A 1 96  ? 28.350 -4.453  -1.634  1.00 12.18 ?  96  VAL   A H    1 
ATOM   2045 H HA   . VAL   A 1 96  ? 26.671 -2.624  -2.719  1.00 12.52 ?  96  VAL   A HA   1 
ATOM   2046 H HB   . VAL   A 1 96  ? 29.000 -3.650  -3.930  1.00 13.00 ?  96  VAL   A HB   1 
ATOM   2047 H HG11 . VAL   A 1 96  ? 28.684 -1.782  -5.384  1.00 13.56 ?  96  VAL   A HG11 1 
ATOM   2048 H HG12 . VAL   A 1 96  ? 27.634 -2.959  -5.563  1.00 13.56 ?  96  VAL   A HG12 1 
ATOM   2049 H HG13 . VAL   A 1 96  ? 27.231 -1.649  -4.758  1.00 13.56 ?  96  VAL   A HG13 1 
ATOM   2050 H HG21 . VAL   A 1 96  ? 29.991 -1.565  -3.454  1.00 13.96 ?  96  VAL   A HG21 1 
ATOM   2051 H HG22 . VAL   A 1 96  ? 28.731 -1.208  -2.555  1.00 13.96 ?  96  VAL   A HG22 1 
ATOM   2052 H HG23 . VAL   A 1 96  ? 29.692 -2.403  -2.139  1.00 13.96 ?  96  VAL   A HG23 1 
ATOM   2053 N N    . GLY   A 1 97  ? 25.137 -4.270  -3.672  1.00 11.26 ?  97  GLY   A N    1 
ATOM   2054 C CA   . GLY   A 1 97  ? 24.327 -5.030  -4.585  1.00 11.88 ?  97  GLY   A CA   1 
ATOM   2055 C C    . GLY   A 1 97  ? 24.337 -4.384  -5.955  1.00 12.14 ?  97  GLY   A C    1 
ATOM   2056 O O    . GLY   A 1 97  ? 24.627 -3.192  -6.096  1.00 12.97 ?  97  GLY   A O    1 
ATOM   2057 H H    . GLY   A 1 97  ? 24.695 -3.726  -3.168  1.00 13.51 ?  97  GLY   A H    1 
ATOM   2058 H HA2  . GLY   A 1 97  ? 24.682 -5.929  -4.647  1.00 14.25 ?  97  GLY   A HA2  1 
ATOM   2059 H HA3  . GLY   A 1 97  ? 23.414 -5.074  -4.258  1.00 14.25 ?  97  GLY   A HA3  1 
ATOM   2060 N N    A PRO   A 1 98  ? 24.011 -5.134  -7.005  0.80 12.04 ?  98  PRO   A N    1 
ATOM   2061 N N    B PRO   A 1 98  ? 24.028 -5.173  -6.980  0.20 12.54 ?  98  PRO   A N    1 
ATOM   2062 C CA   A PRO   A 1 98  ? 23.888 -4.511  -8.330  0.80 13.63 ?  98  PRO   A CA   1 
ATOM   2063 C CA   B PRO   A 1 98  ? 23.990 -4.638  -8.342  0.20 13.24 ?  98  PRO   A CA   1 
ATOM   2064 C C    A PRO   A 1 98  ? 22.782 -3.461  -8.367  0.80 13.83 ?  98  PRO   A C    1 
ATOM   2065 C C    B PRO   A 1 98  ? 22.851 -3.651  -8.509  0.20 13.50 ?  98  PRO   A C    1 
ATOM   2066 O O    A PRO   A 1 98  ? 21.711 -3.637  -7.785  0.80 13.01 ?  98  PRO   A O    1 
ATOM   2067 O O    B PRO   A 1 98  ? 21.723 -3.888  -8.070  0.20 13.84 ?  98  PRO   A O    1 
ATOM   2068 C CB   A PRO   A 1 98  ? 23.573 -5.693  -9.253  0.80 14.58 ?  98  PRO   A CB   1 
ATOM   2069 C CB   B PRO   A 1 98  ? 23.760 -5.886  -9.201  0.20 13.43 ?  98  PRO   A CB   1 
ATOM   2070 C CG   A PRO   A 1 98  ? 22.981 -6.738  -8.352  0.80 13.84 ?  98  PRO   A CG   1 
ATOM   2071 C CG   B PRO   A 1 98  ? 23.040 -6.828  -8.290  0.20 13.21 ?  98  PRO   A CG   1 
ATOM   2072 C CD   A PRO   A 1 98  ? 23.721 -6.579  -7.039  0.80 12.57 ?  98  PRO   A CD   1 
ATOM   2073 C CD   B PRO   A 1 98  ? 23.633 -6.592  -6.929  0.20 12.64 ?  98  PRO   A CD   1 
ATOM   2074 H HA   A PRO   A 1 98  ? 24.728 -4.108  -8.586  0.80 16.35 ?  98  PRO   A HA   1 
ATOM   2075 H HA   B PRO   A 1 98  ? 24.831 -4.218  -8.576  0.20 15.88 ?  98  PRO   A HA   1 
ATOM   2076 H HB2  A PRO   A 1 98  ? 22.933 -5.418  -9.926  0.80 17.50 ?  98  PRO   A HB2  1 
ATOM   2077 H HB2  B PRO   A 1 98  ? 23.209 -5.658  -9.968  0.20 16.12 ?  98  PRO   A HB2  1 
ATOM   2078 H HB3  A PRO   A 1 98  ? 24.390 -6.015  -9.660  0.80 17.50 ?  98  PRO   A HB3  1 
ATOM   2079 H HB3  B PRO   A 1 98  ? 24.610 -6.253  -9.479  0.20 16.12 ?  98  PRO   A HB3  1 
ATOM   2080 H HG2  A PRO   A 1 98  ? 22.032 -6.571  -8.234  0.80 16.61 ?  98  PRO   A HG2  1 
ATOM   2081 H HG2  B PRO   A 1 98  ? 22.091 -6.623  -8.289  0.20 15.85 ?  98  PRO   A HG2  1 
ATOM   2082 H HG3  A PRO   A 1 98  ? 23.131 -7.619  -8.728  0.80 16.61 ?  98  PRO   A HG3  1 
ATOM   2083 H HG3  B PRO   A 1 98  ? 23.194 -7.740  -8.575  0.20 15.85 ?  98  PRO   A HG3  1 
ATOM   2084 H HD2  A PRO   A 1 98  ? 23.153 -6.839  -6.294  0.80 15.08 ?  98  PRO   A HD2  1 
ATOM   2085 H HD2  B PRO   A 1 98  ? 22.966 -6.735  -6.237  0.20 15.17 ?  98  PRO   A HD2  1 
ATOM   2086 H HD3  A PRO   A 1 98  ? 24.548 -7.087  -7.050  0.80 15.08 ?  98  PRO   A HD3  1 
ATOM   2087 H HD3  B PRO   A 1 98  ? 24.413 -7.152  -6.793  0.20 15.17 ?  98  PRO   A HD3  1 
ATOM   2088 N N    A ASN   A 1 99  ? 23.057 -2.350  -9.052  0.80 15.19 ?  99  ASN   A N    1 
ATOM   2089 N N    B ASN   A 1 99  ? 23.156 -2.534  -9.154  0.20 13.68 ?  99  ASN   A N    1 
ATOM   2090 C CA   A ASN   A 1 99  ? 22.079 -1.282  -9.263  0.80 16.60 ?  99  ASN   A CA   1 
ATOM   2091 C CA   B ASN   A 1 99  ? 22.152 -1.533  -9.480  0.20 14.42 ?  99  ASN   A CA   1 
ATOM   2092 C C    A ASN   A 1 99  ? 21.507 -1.426  -10.672 0.80 18.17 ?  99  ASN   A C    1 
ATOM   2093 C C    B ASN   A 1 99  ? 21.632 -1.850  -10.878 0.20 15.21 ?  99  ASN   A C    1 
ATOM   2094 O O    A ASN   A 1 99  ? 22.169 -1.092  -11.663 0.80 19.86 ?  99  ASN   A O    1 
ATOM   2095 O O    B ASN   A 1 99  ? 22.377 -1.778  -11.862 0.20 14.34 ?  99  ASN   A O    1 
ATOM   2096 C CB   A ASN   A 1 99  ? 22.714 0.095   -9.063  0.80 17.49 ?  99  ASN   A CB   1 
ATOM   2097 C CB   B ASN   A 1 99  ? 22.754 -0.133  -9.397  0.20 15.15 ?  99  ASN   A CB   1 
ATOM   2098 C CG   A ASN   A 1 99  ? 21.681 1.229   -9.045  0.80 18.56 ?  99  ASN   A CG   1 
ATOM   2099 C CG   B ASN   A 1 99  ? 21.704 0.956   -9.452  0.20 15.99 ?  99  ASN   A CG   1 
ATOM   2100 O OD1  A ASN   A 1 99  ? 20.679 1.181   -9.758  0.80 19.26 ?  99  ASN   A OD1  1 
ATOM   2101 O OD1  B ASN   A 1 99  ? 20.840 0.951   -10.329 0.20 15.80 ?  99  ASN   A OD1  1 
ATOM   2102 N ND2  A ASN   A 1 99  ? 21.942 2.264   -8.239  0.80 18.98 ?  99  ASN   A ND2  1 
ATOM   2103 N ND2  B ASN   A 1 99  ? 21.764 1.890   -8.504  0.20 15.98 ?  99  ASN   A ND2  1 
ATOM   2104 H H    A ASN   A 1 99  ? 23.827 -2.178  -9.382  0.80 18.23 ?  99  ASN   A H    1 
ATOM   2105 H H    B ASN   A 1 99  ? 23.947 -2.328  -9.416  0.20 16.41 ?  99  ASN   A H    1 
ATOM   2106 H HA   A ASN   A 1 99  ? 21.350 -1.380  -8.619  0.80 19.92 ?  99  ASN   A HA   1 
ATOM   2107 H HA   B ASN   A 1 99  ? 21.413 -1.588  -8.850  0.20 17.30 ?  99  ASN   A HA   1 
ATOM   2108 H HB2  A ASN   A 1 99  ? 23.190 0.109   -8.220  0.80 20.99 ?  99  ASN   A HB2  1 
ATOM   2109 H HB2  B ASN   A 1 99  ? 23.235 -0.044  -8.557  0.20 18.18 ?  99  ASN   A HB2  1 
ATOM   2110 H HB3  A ASN   A 1 99  ? 23.325 0.263   -9.796  0.80 20.99 ?  99  ASN   A HB3  1 
ATOM   2111 H HB3  B ASN   A 1 99  ? 23.358 -0.002  -10.140 0.20 18.18 ?  99  ASN   A HB3  1 
ATOM   2112 H HD21 A ASN   A 1 99  ? 21.391 2.923   -8.188  0.80 22.78 ?  99  ASN   A HD21 1 
ATOM   2113 H HD21 B ASN   A 1 99  ? 21.188 2.526   -8.485  0.20 19.18 ?  99  ASN   A HD21 1 
ATOM   2114 H HD22 A ASN   A 1 99  ? 22.654 2.262   -7.756  0.80 22.78 ?  99  ASN   A HD22 1 
ATOM   2115 H HD22 B ASN   A 1 99  ? 22.383 1.855   -7.902  0.20 19.18 ?  99  ASN   A HD22 1 
ATOM   2116 N N    A VAL   A 1 100 ? 20.267 -1.918  -10.749 0.80 19.23 ?  100 VAL   A N    1 
ATOM   2117 N N    B VAL   A 1 100 ? 20.359 -2.246  -10.955 0.20 17.09 ?  100 VAL   A N    1 
ATOM   2118 C CA   A VAL   A 1 100 ? 19.622 -2.150  -12.040 0.80 21.17 ?  100 VAL   A CA   1 
ATOM   2119 C CA   B VAL   A 1 100 ? 19.754 -2.580  -12.241 0.20 19.43 ?  100 VAL   A CA   1 
ATOM   2120 C C    A VAL   A 1 100 ? 19.490 -0.852  -12.823 0.80 21.29 ?  100 VAL   A C    1 
ATOM   2121 C C    B VAL   A 1 100 ? 19.685 -1.358  -13.141 0.20 20.74 ?  100 VAL   A C    1 
ATOM   2122 O O    A VAL   A 1 100 ? 19.553 -0.853  -14.058 0.80 22.88 ?  100 VAL   A O    1 
ATOM   2123 O O    B VAL   A 1 100 ? 19.801 -1.474  -14.367 0.20 21.17 ?  100 VAL   A O    1 
ATOM   2124 C CB   A VAL   A 1 100 ? 18.266 -2.863  -11.842 0.80 22.60 ?  100 VAL   A CB   1 
ATOM   2125 C CB   B VAL   A 1 100 ? 18.363 -3.205  -12.019 0.20 20.42 ?  100 VAL   A CB   1 
ATOM   2126 C CG1  A VAL   A 1 100 ? 17.512 -2.989  -13.162 0.80 23.51 ?  100 VAL   A CG1  1 
ATOM   2127 C CG1  B VAL   A 1 100 ? 17.682 -3.488  -13.350 0.20 20.91 ?  100 VAL   A CG1  1 
ATOM   2128 C CG2  A VAL   A 1 100 ? 18.490 -4.235  -11.226 0.80 23.29 ?  100 VAL   A CG2  1 
ATOM   2129 C CG2  B VAL   A 1 100 ? 18.493 -4.472  -11.203 0.20 20.79 ?  100 VAL   A CG2  1 
ATOM   2130 H H    A VAL   A 1 100 ? 19.771 -2.117  -10.068 0.80 23.08 ?  100 VAL   A H    1 
ATOM   2131 H H    B VAL   A 1 100 ? 19.832 -2.341  -10.281 0.20 20.50 ?  100 VAL   A H    1 
ATOM   2132 H HA   A VAL   A 1 100 ? 20.181 -2.743  -12.559 0.80 25.40 ?  100 VAL   A HA   1 
ATOM   2133 H HA   B VAL   A 1 100 ? 20.309 -3.237  -12.684 0.20 23.32 ?  100 VAL   A HA   1 
ATOM   2134 H HB   A VAL   A 1 100 ? 17.717 -2.347  -11.232 0.80 27.12 ?  100 VAL   A HB   1 
ATOM   2135 H HB   B VAL   A 1 100 ? 17.810 -2.579  -11.525 0.20 24.50 ?  100 VAL   A HB   1 
ATOM   2136 H HG11 A VAL   A 1 100 ? 16.774 -3.609  -13.047 0.80 28.22 ?  100 VAL   A HG11 1 
ATOM   2137 H HG11 B VAL   A 1 100 ? 16.909 -4.051  -13.192 0.20 25.10 ?  100 VAL   A HG11 1 
ATOM   2138 H HG12 A VAL   A 1 100 ? 17.173 -2.118  -13.420 0.80 28.22 ?  100 VAL   A HG12 1 
ATOM   2139 H HG12 B VAL   A 1 100 ? 17.402 -2.649  -13.751 0.20 25.10 ?  100 VAL   A HG12 1 
ATOM   2140 H HG13 A VAL   A 1 100 ? 18.119 -3.325  -13.841 0.80 28.22 ?  100 VAL   A HG13 1 
ATOM   2141 H HG13 B VAL   A 1 100 ? 18.308 -3.943  -13.934 0.20 25.10 ?  100 VAL   A HG13 1 
ATOM   2142 H HG21 A VAL   A 1 100 ? 17.636 -4.690  -11.144 0.80 27.94 ?  100 VAL   A HG21 1 
ATOM   2143 H HG21 B VAL   A 1 100 ? 17.623 -4.891  -11.135 0.20 24.95 ?  100 VAL   A HG21 1 
ATOM   2144 H HG22 A VAL   A 1 100 ? 19.081 -4.747  -11.802 0.80 27.94 ?  100 VAL   A HG22 1 
ATOM   2145 H HG22 B VAL   A 1 100 ? 19.116 -5.067  -11.648 0.20 24.95 ?  100 VAL   A HG22 1 
ATOM   2146 H HG23 A VAL   A 1 100 ? 18.893 -4.128  -10.351 0.80 27.94 ?  100 VAL   A HG23 1 
ATOM   2147 H HG23 B VAL   A 1 100 ? 18.824 -4.246  -10.320 0.20 24.95 ?  100 VAL   A HG23 1 
ATOM   2148 N N    A ASN   A 1 101 ? 19.292 0.269   -12.134 0.80 22.37 ?  101 ASN   A N    1 
ATOM   2149 N N    B ASN   A 1 101 ? 19.482 -0.175  -12.557 0.20 21.77 ?  101 ASN   A N    1 
ATOM   2150 C CA   A ASN   A 1 101 ? 19.228 1.550   -12.824 0.80 24.00 ?  101 ASN   A CA   1 
ATOM   2151 C CA   B ASN   A 1 101 ? 19.397 1.047   -13.347 0.20 22.92 ?  101 ASN   A CA   1 
ATOM   2152 C C    A ASN   A 1 101 ? 20.587 1.997   -13.371 0.80 26.35 ?  101 ASN   A C    1 
ATOM   2153 C C    B ASN   A 1 101 ? 20.753 1.497   -13.871 0.20 24.50 ?  101 ASN   A C    1 
ATOM   2154 O O    A ASN   A 1 101 ? 20.665 3.080   -13.966 0.80 28.39 ?  101 ASN   A O    1 
ATOM   2155 O O    B ASN   A 1 101 ? 20.801 2.300   -14.809 0.20 24.23 ?  101 ASN   A O    1 
ATOM   2156 C CB   A ASN   A 1 101 ? 18.593 2.592   -11.901 0.80 23.14 ?  101 ASN   A CB   1 
ATOM   2157 C CB   B ASN   A 1 101 ? 18.735 2.155   -12.525 0.20 22.53 ?  101 ASN   A CB   1 
ATOM   2158 C CG   A ASN   A 1 101 ? 17.210 2.165   -11.412 0.80 22.03 ?  101 ASN   A CG   1 
ATOM   2159 C CG   B ASN   A 1 101 ? 17.383 1.741   -11.979 0.20 22.43 ?  101 ASN   A CG   1 
ATOM   2160 O OD1  A ASN   A 1 101 ? 16.399 1.639   -12.181 0.80 21.67 ?  101 ASN   A OD1  1 
ATOM   2161 O OD1  B ASN   A 1 101 ? 16.727 0.850   -12.521 0.20 22.61 ?  101 ASN   A OD1  1 
ATOM   2162 N ND2  A ASN   A 1 101 ? 16.944 2.369   -10.128 0.80 22.08 ?  101 ASN   A ND2  1 
ATOM   2163 N ND2  B ASN   A 1 101 ? 16.957 2.385   -10.900 0.20 22.30 ?  101 ASN   A ND2  1 
ATOM   2164 H H    A ASN   A 1 101 ? 19.168 0.309   -11.282 0.80 26.84 ?  101 ASN   A H    1 
ATOM   2165 H H    B ASN   A 1 101 ? 19.378 -0.056  -11.711 0.20 26.12 ?  101 ASN   A H    1 
ATOM   2166 H HA   A ASN   A 1 101 ? 18.637 1.452   -13.583 0.80 28.80 ?  101 ASN   A HA   1 
ATOM   2167 H HA   B ASN   A 1 101 ? 18.842 0.884   -14.117 0.20 27.51 ?  101 ASN   A HA   1 
ATOM   2168 H HB2  A ASN   A 1 101 ? 19.160 2.724   -11.126 0.80 27.76 ?  101 ASN   A HB2  1 
ATOM   2169 H HB2  B ASN   A 1 101 ? 19.303 2.384   -11.772 0.20 27.03 ?  101 ASN   A HB2  1 
ATOM   2170 H HB3  A ASN   A 1 101 ? 18.498 3.430   -12.388 0.80 27.76 ?  101 ASN   A HB3  1 
ATOM   2171 H HB3  B ASN   A 1 101 ? 18.601 2.934   -13.088 0.20 27.03 ?  101 ASN   A HB3  1 
ATOM   2172 H HD21 A ASN   A 1 101 ? 16.176 2.146   -9.812  0.80 26.49 ?  101 ASN   A HD21 1 
ATOM   2173 H HD21 B ASN   A 1 101 ? 16.196 2.186   -10.552 0.20 26.76 ?  101 ASN   A HD21 1 
ATOM   2174 H HD22 A ASN   A 1 101 ? 17.531 2.733   -9.618  0.80 26.49 ?  101 ASN   A HD22 1 
ATOM   2175 H HD22 B ASN   A 1 101 ? 17.442 3.002   -10.549 0.20 26.76 ?  101 ASN   A HD22 1 
ATOM   2176 N N    A LYS   A 1 102 ? 21.639 1.183   -13.197 0.80 28.59 ?  102 LYS   A N    1 
ATOM   2177 N N    B LYS   A 1 102 ? 21.849 0.993   -13.304 0.20 26.22 ?  102 LYS   A N    1 
ATOM   2178 C CA   A LYS   A 1 102 ? 22.931 1.375   -13.848 0.80 30.11 ?  102 LYS   A CA   1 
ATOM   2179 C CA   B LYS   A 1 102 ? 23.186 1.302   -13.789 0.20 27.55 ?  102 LYS   A CA   1 
ATOM   2180 C C    A LYS   A 1 102 ? 23.269 0.263   -14.837 0.80 30.76 ?  102 LYS   A C    1 
ATOM   2181 C C    B LYS   A 1 102 ? 23.725 0.235   -14.732 0.20 28.22 ?  102 LYS   A C    1 
ATOM   2182 O O    A LYS   A 1 102 ? 24.369 0.270   -15.397 0.80 31.74 ?  102 LYS   A O    1 
ATOM   2183 O O    B LYS   A 1 102 ? 24.871 0.344   -15.180 0.20 28.73 ?  102 LYS   A O    1 
ATOM   2184 C CB   A LYS   A 1 102 ? 24.059 1.439   -12.808 0.80 32.13 ?  102 LYS   A CB   1 
ATOM   2185 C CB   B LYS   A 1 102 ? 24.155 1.502   -12.616 0.20 28.28 ?  102 LYS   A CB   1 
ATOM   2186 C CG   A LYS   A 1 102 ? 23.961 2.564   -11.803 0.80 34.03 ?  102 LYS   A CG   1 
ATOM   2187 C CG   B LYS   A 1 102 ? 23.825 2.697   -11.730 0.20 28.88 ?  102 LYS   A CG   1 
ATOM   2188 C CD   A LYS   A 1 102 ? 25.158 2.537   -10.856 0.80 35.95 ?  102 LYS   A CD   1 
ATOM   2189 C CD   B LYS   A 1 102 ? 24.839 2.862   -10.604 0.20 29.40 ?  102 LYS   A CD   1 
ATOM   2190 C CE   A LYS   A 1 102 ? 25.074 3.637   -9.810  0.80 37.53 ?  102 LYS   A CE   1 
ATOM   2191 C CE   B LYS   A 1 102 ? 24.465 4.018   -9.687  0.20 29.83 ?  102 LYS   A CE   1 
ATOM   2192 N NZ   A LYS   A 1 102 ? 26.174 3.528   -8.805  0.80 38.41 ?  102 LYS   A NZ   1 
ATOM   2193 N NZ   B LYS   A 1 102 ? 25.360 4.114   -8.498  0.20 30.03 ?  102 LYS   A NZ   1 
ATOM   2194 H H    A LYS   A 1 102 ? 21.624 0.487   -12.685 0.80 34.31 ?  102 LYS   A H    1 
ATOM   2195 H H    B LYS   A 1 102 ? 21.840 0.450   -12.637 0.20 31.46 ?  102 LYS   A H    1 
ATOM   2196 H HA   A LYS   A 1 102 ? 22.918 2.217   -14.325 0.80 36.13 ?  102 LYS   A HA   1 
ATOM   2197 H HA   B LYS   A 1 102 ? 23.150 2.139   -14.276 0.20 33.06 ?  102 LYS   A HA   1 
ATOM   2198 H HB2  A LYS   A 1 102 ? 24.066 0.606   -12.311 0.80 38.55 ?  102 LYS   A HB2  1 
ATOM   2199 H HB2  B LYS   A 1 102 ? 24.143 0.708   -12.061 0.20 33.93 ?  102 LYS   A HB2  1 
ATOM   2200 H HB3  A LYS   A 1 102 ? 24.902 1.543   -13.277 0.80 38.55 ?  102 LYS   A HB3  1 
ATOM   2201 H HB3  B LYS   A 1 102 ? 25.047 1.639   -12.971 0.20 33.93 ?  102 LYS   A HB3  1 
ATOM   2202 H HG2  A LYS   A 1 102 ? 23.956 3.413   -12.270 0.80 40.84 ?  102 LYS   A HG2  1 
ATOM   2203 H HG2  B LYS   A 1 102 ? 23.835 3.506   -12.266 0.20 34.65 ?  102 LYS   A HG2  1 
ATOM   2204 H HG3  A LYS   A 1 102 ? 23.152 2.457   -11.279 0.80 40.84 ?  102 LYS   A HG3  1 
ATOM   2205 H HG3  B LYS   A 1 102 ? 22.949 2.570   -11.333 0.20 34.65 ?  102 LYS   A HG3  1 
ATOM   2206 H HD2  A LYS   A 1 102 ? 25.184 1.681   -10.397 0.80 43.14 ?  102 LYS   A HD2  1 
ATOM   2207 H HD2  B LYS   A 1 102 ? 24.866 2.050   -10.073 0.20 35.28 ?  102 LYS   A HD2  1 
ATOM   2208 H HD3  A LYS   A 1 102 ? 25.973 2.664   -11.368 0.80 43.14 ?  102 LYS   A HD3  1 
ATOM   2209 H HD3  B LYS   A 1 102 ? 25.714 3.044   -10.983 0.20 35.28 ?  102 LYS   A HD3  1 
ATOM   2210 H HE2  A LYS   A 1 102 ? 25.146 4.500   -10.249 0.80 45.04 ?  102 LYS   A HE2  1 
ATOM   2211 H HE2  B LYS   A 1 102 ? 24.532 4.850   -10.182 0.20 35.80 ?  102 LYS   A HE2  1 
ATOM   2212 H HE3  A LYS   A 1 102 ? 24.226 3.568   -9.343  0.80 45.04 ?  102 LYS   A HE3  1 
ATOM   2213 H HE3  B LYS   A 1 102 ? 23.557 3.892   -9.371  0.20 35.80 ?  102 LYS   A HE3  1 
ATOM   2214 H HZ1  A LYS   A 1 102 ? 26.103 4.181   -8.205  0.80 46.09 ?  102 LYS   A HZ1  1 
ATOM   2215 H HZ1  B LYS   A 1 102 ? 25.113 4.799   -7.986  0.20 36.04 ?  102 LYS   A HZ1  1 
ATOM   2216 H HZ2  A LYS   A 1 102 ? 26.127 2.744   -8.386  0.80 46.09 ?  102 LYS   A HZ2  1 
ATOM   2217 H HZ2  B LYS   A 1 102 ? 25.312 3.364   -8.021  0.20 36.04 ?  102 LYS   A HZ2  1 
ATOM   2218 H HZ3  A LYS   A 1 102 ? 26.964 3.592   -9.211  0.80 46.09 ?  102 LYS   A HZ3  1 
ATOM   2219 H HZ3  B LYS   A 1 102 ? 26.202 4.237   -8.760  0.20 36.04 ?  102 LYS   A HZ3  1 
ATOM   2220 N N    A GLY   A 1 103 ? 22.376 -0.703  -15.048 0.80 31.21 ?  103 GLY   A N    1 
ATOM   2221 N N    B GLY   A 1 103 ? 22.932 -0.790  -15.039 0.20 28.30 ?  103 GLY   A N    1 
ATOM   2222 C CA   A GLY   A 1 103 ? 22.640 -1.808  -15.954 0.80 31.00 ?  103 GLY   A CA   1 
ATOM   2223 C CA   B GLY   A 1 103 ? 23.328 -1.809  -15.991 0.20 27.96 ?  103 GLY   A CA   1 
ATOM   2224 C C    A GLY   A 1 103 ? 23.491 -2.929  -15.394 0.80 30.48 ?  103 GLY   A C    1 
ATOM   2225 C C    B GLY   A 1 103 ? 24.267 -2.845  -15.411 0.20 27.55 ?  103 GLY   A C    1 
ATOM   2226 O O    A GLY   A 1 103 ? 24.017 -3.736  -16.167 0.80 31.32 ?  103 GLY   A O    1 
ATOM   2227 O O    B GLY   A 1 103 ? 25.296 -3.160  -16.015 0.20 28.07 ?  103 GLY   A O    1 
ATOM   2228 H H    A GLY   A 1 103 ? 21.606 -0.734  -14.683 0.80 37.45 ?  103 GLY   A H    1 
ATOM   2229 H H    B GLY   A 1 103 ? 22.152 -0.919  -14.700 0.20 33.96 ?  103 GLY   A H    1 
ATOM   2230 H HA2  A GLY   A 1 103 ? 21.791 -2.183  -16.251 0.80 37.20 ?  103 GLY   A HA2  1 
ATOM   2231 H HA2  B GLY   A 1 103 ? 22.537 -2.262  -16.322 0.20 33.55 ?  103 GLY   A HA2  1 
ATOM   2232 H HA3  A GLY   A 1 103 ? 23.098 -1.466  -16.737 0.80 37.20 ?  103 GLY   A HA3  1 
ATOM   2233 H HA3  B GLY   A 1 103 ? 23.773 -1.387  -16.742 0.20 33.55 ?  103 GLY   A HA3  1 
ATOM   2234 N N    A GLU   A 1 104 ? 23.641 -3.016  -14.077 0.80 28.03 ?  104 GLU   A N    1 
ATOM   2235 N N    B GLU   A 1 104 ? 23.922 -3.393  -14.247 0.20 26.30 ?  104 GLU   A N    1 
ATOM   2236 C CA   A GLU   A 1 104 ? 24.512 -4.016  -13.472 0.80 26.28 ?  104 GLU   A CA   1 
ATOM   2237 C CA   B GLU   A 1 104 ? 24.787 -4.325  -13.536 0.20 25.31 ?  104 GLU   A CA   1 
ATOM   2238 C C    A GLU   A 1 104 ? 23.818 -5.376  -13.375 0.80 26.35 ?  104 GLU   A C    1 
ATOM   2239 C C    B GLU   A 1 104 ? 24.122 -5.691  -13.410 0.20 25.05 ?  104 GLU   A C    1 
ATOM   2240 O O    A GLU   A 1 104 ? 22.592 -5.471  -13.256 0.80 26.80 ?  104 GLU   A O    1 
ATOM   2241 O O    B GLU   A 1 104 ? 22.919 -5.793  -13.148 0.20 24.63 ?  104 GLU   A O    1 
ATOM   2242 C CB   A GLU   A 1 104 ? 25.005 -3.520  -12.108 0.80 24.48 ?  104 GLU   A CB   1 
ATOM   2243 C CB   B GLU   A 1 104 ? 25.193 -3.757  -12.169 0.20 24.92 ?  104 GLU   A CB   1 
ATOM   2244 C CG   A GLU   A 1 104 ? 25.871 -2.259  -12.265 0.80 23.75 ?  104 GLU   A CG   1 
ATOM   2245 C CG   B GLU   A 1 104 ? 26.018 -2.478  -12.291 0.20 24.98 ?  104 GLU   A CG   1 
ATOM   2246 C CD   A GLU   A 1 104 ? 26.252 -1.544  -10.970 0.80 22.27 ?  104 GLU   A CD   1 
ATOM   2247 C CD   B GLU   A 1 104 ? 26.166 -1.738  -10.974 0.20 25.03 ?  104 GLU   A CD   1 
ATOM   2248 O OE1  A GLU   A 1 104 ? 25.670 -1.832  -9.899  0.80 20.40 ?  104 GLU   A OE1  1 
ATOM   2249 O OE1  B GLU   A 1 104 ? 25.852 -2.323  -9.917  0.20 25.07 ?  104 GLU   A OE1  1 
ATOM   2250 O OE2  A GLU   A 1 104 ? 27.137 -0.656  -11.052 0.80 23.02 -1 104 GLU   A OE2  1 
ATOM   2251 O OE2  B GLU   A 1 104 ? 26.592 -0.564  -10.998 0.20 25.20 -1 104 GLU   A OE2  1 
ATOM   2252 H H    A GLU   A 1 104 ? 23.251 -2.500  -13.514 0.80 33.63 ?  104 GLU   A H    1 
ATOM   2253 H H    B GLU   A 1 104 ? 23.180 -3.230  -13.843 0.20 31.56 ?  104 GLU   A H    1 
ATOM   2254 H HA   A GLU   A 1 104 ? 25.288 -4.126  -14.041 0.80 31.54 ?  104 GLU   A HA   1 
ATOM   2255 H HA   B GLU   A 1 104 ? 25.599 -4.446  -14.045 0.20 30.38 ?  104 GLU   A HA   1 
ATOM   2256 H HB2  A GLU   A 1 104 ? 24.241 -3.304  -11.551 0.80 29.38 ?  104 GLU   A HB2  1 
ATOM   2257 H HB2  B GLU   A 1 104 ? 24.399 -3.549  -11.655 0.20 29.90 ?  104 GLU   A HB2  1 
ATOM   2258 H HB3  A GLU   A 1 104 ? 25.541 -4.213  -11.693 0.80 29.38 ?  104 GLU   A HB3  1 
ATOM   2259 H HB3  B GLU   A 1 104 ? 25.734 -4.412  -11.697 0.20 29.90 ?  104 GLU   A HB3  1 
ATOM   2260 H HG2  A GLU   A 1 104 ? 26.693 -2.510  -12.709 0.80 28.50 ?  104 GLU   A HG2  1 
ATOM   2261 H HG2  B GLU   A 1 104 ? 26.908 -2.702  -12.612 0.20 29.98 ?  104 GLU   A HG2  1 
ATOM   2262 H HG3  A GLU   A 1 104 ? 25.385 -1.623  -12.813 0.80 28.50 ?  104 GLU   A HG3  1 
ATOM   2263 H HG3  B GLU   A 1 104 ? 25.587 -1.882  -12.927 0.20 29.98 ?  104 GLU   A HG3  1 
ATOM   2264 N N    A ASP   A 1 105 ? 24.628 -6.433  -13.420 0.80 26.75 ?  105 ASP   A N    1 
ATOM   2265 N N    B ASP   A 1 105 ? 24.928 -6.732  -13.608 0.20 25.66 ?  105 ASP   A N    1 
ATOM   2266 C CA   A ASP   A 1 105 ? 24.128 -7.798  -13.573 0.80 28.01 ?  105 ASP   A CA   1 
ATOM   2267 C CA   B ASP   A 1 105 ? 24.455 -8.110  -13.647 0.20 26.56 ?  105 ASP   A CA   1 
ATOM   2268 C C    A ASP   A 1 105 ? 23.469 -8.282  -12.283 0.80 25.31 ?  105 ASP   A C    1 
ATOM   2269 C C    B ASP   A 1 105 ? 23.685 -8.457  -12.380 0.20 26.50 ?  105 ASP   A C    1 
ATOM   2270 O O    A ASP   A 1 105 ? 24.123 -8.380  -11.242 0.80 23.49 ?  105 ASP   A O    1 
ATOM   2271 O O    B ASP   A 1 105 ? 24.225 -8.378  -11.272 0.20 26.23 ?  105 ASP   A O    1 
ATOM   2272 C CB   A ASP   A 1 105 ? 25.298 -8.706  -13.947 0.80 31.55 ?  105 ASP   A CB   1 
ATOM   2273 C CB   B ASP   A 1 105 ? 25.672 -9.024  -13.797 0.20 27.49 ?  105 ASP   A CB   1 
ATOM   2274 C CG   A ASP   A 1 105 ? 24.897 -10.154 -14.104 0.80 34.66 ?  105 ASP   A CG   1 
ATOM   2275 C CG   B ASP   A 1 105 ? 25.297 -10.480 -13.994 0.20 28.35 ?  105 ASP   A CG   1 
ATOM   2276 O OD1  A ASP   A 1 105 ? 23.685 -10.432 -14.193 0.80 35.34 ?  105 ASP   A OD1  1 
ATOM   2277 O OD1  B ASP   A 1 105 ? 24.089 -10.788 -14.065 0.20 28.38 ?  105 ASP   A OD1  1 
ATOM   2278 O OD2  A ASP   A 1 105 ? 25.805 -11.015 -14.138 0.80 36.56 -1 105 ASP   A OD2  1 
ATOM   2279 O OD2  B ASP   A 1 105 ? 26.220 -11.320 -14.076 0.20 28.65 -1 105 ASP   A OD2  1 
ATOM   2280 H H    A ASP   A 1 105 ? 25.485 -6.383  -13.363 0.80 32.10 ?  105 ASP   A H    1 
ATOM   2281 H H    B ASP   A 1 105 ? 25.770 -6.660  -13.728 0.20 30.79 ?  105 ASP   A H    1 
ATOM   2282 H HA   A ASP   A 1 105 ? 23.472 -7.827  -14.286 0.80 33.61 ?  105 ASP   A HA   1 
ATOM   2283 H HA   B ASP   A 1 105 ? 23.869 -8.238  -14.409 0.20 31.87 ?  105 ASP   A HA   1 
ATOM   2284 H HB2  A ASP   A 1 105 ? 25.674 -8.406  -14.791 0.80 37.86 ?  105 ASP   A HB2  1 
ATOM   2285 H HB2  B ASP   A 1 105 ? 26.193 -8.726  -14.563 0.20 32.99 ?  105 ASP   A HB2  1 
ATOM   2286 H HB3  A ASP   A 1 105 ? 25.969 -8.664  -13.251 0.80 37.86 ?  105 ASP   A HB3  1 
ATOM   2287 H HB3  B ASP   A 1 105 ? 26.211 -8.967  -12.993 0.20 32.99 ?  105 ASP   A HB3  1 
ATOM   2288 N N    A ILE   A 1 106 ? 22.178 -8.622  -12.366 0.80 24.63 ?  106 ILE   A N    1 
ATOM   2289 N N    B ILE   A 1 106 ? 22.419 -8.852  -12.546 0.20 26.61 ?  106 ILE   A N    1 
ATOM   2290 C CA   A ILE   A 1 106 ? 21.423 -9.043  -11.189 0.80 23.77 ?  106 ILE   A CA   1 
ATOM   2291 C CA   B ILE   A 1 106 ? 21.604 -9.221  -11.394 0.20 26.81 ?  106 ILE   A CA   1 
ATOM   2292 C C    A ILE   A 1 106 ? 21.962 -10.334 -10.590 0.80 23.14 ?  106 ILE   A C    1 
ATOM   2293 C C    B ILE   A 1 106 ? 22.102 -10.501 -10.742 0.20 26.63 ?  106 ILE   A C    1 
ATOM   2294 O O    A ILE   A 1 106 ? 21.747 -10.593 -9.403  0.80 22.45 ?  106 ILE   A O    1 
ATOM   2295 O O    B ILE   A 1 106 ? 21.820 -10.739 -9.562  0.20 26.35 ?  106 ILE   A O    1 
ATOM   2296 C CB   A ILE   A 1 106 ? 19.915 -9.140  -11.519 0.80 25.82 ?  106 ILE   A CB   1 
ATOM   2297 C CB   B ILE   A 1 106 ? 20.111 -9.323  -11.762 0.20 27.45 ?  106 ILE   A CB   1 
ATOM   2298 C CG1  A ILE   A 1 106 ? 19.076 -9.200  -10.239 0.80 26.66 ?  106 ILE   A CG1  1 
ATOM   2299 C CG1  B ILE   A 1 106 ? 19.238 -9.068  -10.533 0.20 27.79 ?  106 ILE   A CG1  1 
ATOM   2300 C CG2  A ILE   A 1 106 ? 19.632 -10.364 -12.360 0.80 27.10 ?  106 ILE   A CG2  1 
ATOM   2301 C CG2  B ILE   A 1 106 ? 19.787 -10.701 -12.298 0.20 27.65 ?  106 ILE   A CG2  1 
ATOM   2302 C CD1  A ILE   A 1 106 ? 19.157 -7.948  -9.394  0.80 27.15 ?  106 ILE   A CD1  1 
ATOM   2303 C CD1  B ILE   A 1 106 ? 19.442 -7.713  -9.904  0.20 27.99 ?  106 ILE   A CD1  1 
ATOM   2304 H H    A ILE   A 1 106 ? 21.722 -8.609  -13.090 0.80 29.55 ?  106 ILE   A H    1 
ATOM   2305 H H    B ILE   A 1 106 ? 22.018 -8.906  -13.302 0.20 31.93 ?  106 ILE   A H    1 
ATOM   2306 H HA   A ILE   A 1 106 ? 21.533 -8.366  -10.509 0.80 28.52 ?  106 ILE   A HA   1 
ATOM   2307 H HA   B ILE   A 1 106 ? 21.702 -8.522  -10.738 0.20 32.17 ?  106 ILE   A HA   1 
ATOM   2308 H HB   A ILE   A 1 106 ? 19.662 -8.349  -12.019 0.80 30.98 ?  106 ILE   A HB   1 
ATOM   2309 H HB   B ILE   A 1 106 ? 19.902 -8.661  -12.442 0.20 32.95 ?  106 ILE   A HB   1 
ATOM   2310 H HG12 A ILE   A 1 106 ? 18.147 -9.329  -10.482 0.80 31.99 ?  106 ILE   A HG12 1 
ATOM   2311 H HG12 B ILE   A 1 106 ? 18.305 -9.135  -10.791 0.20 33.34 ?  106 ILE   A HG12 1 
ATOM   2312 H HG13 A ILE   A 1 106 ? 19.381 -9.942  -9.696  0.80 31.99 ?  106 ILE   A HG13 1 
ATOM   2313 H HG13 B ILE   A 1 106 ? 19.442 -9.739  -9.863  0.20 33.34 ?  106 ILE   A HG13 1 
ATOM   2314 H HG21 A ILE   A 1 106 ? 18.756 -10.268 -12.760 0.80 32.52 ?  106 ILE   A HG21 1 
ATOM   2315 H HG21 B ILE   A 1 106 ? 18.948 -10.658 -12.781 0.20 33.17 ?  106 ILE   A HG21 1 
ATOM   2316 H HG22 A ILE   A 1 106 ? 20.311 -10.432 -13.045 0.80 32.52 ?  106 ILE   A HG22 1 
ATOM   2317 H HG22 B ILE   A 1 106 ? 20.498 -10.983 -12.890 0.20 33.17 ?  106 ILE   A HG22 1 
ATOM   2318 H HG23 A ILE   A 1 106 ? 19.655 -11.147 -11.788 0.80 32.52 ?  106 ILE   A HG23 1 
ATOM   2319 H HG23 B ILE   A 1 106 ? 19.706 -11.319 -11.553 0.20 33.17 ?  106 ILE   A HG23 1 
ATOM   2320 H HD11 A ILE   A 1 106 ? 18.438 -7.959  -8.745  0.80 32.58 ?  106 ILE   A HD11 1 
ATOM   2321 H HD11 B ILE   A 1 106 ? 18.640 -7.468  -9.422  0.20 33.58 ?  106 ILE   A HD11 1 
ATOM   2322 H HD12 A ILE   A 1 106 ? 20.014 -7.927  -8.937  0.80 32.58 ?  106 ILE   A HD12 1 
ATOM   2323 H HD12 B ILE   A 1 106 ? 20.195 -7.759  -9.293  0.20 33.58 ?  106 ILE   A HD12 1 
ATOM   2324 H HD13 A ILE   A 1 106 ? 19.071 -7.172  -9.970  0.80 32.58 ?  106 ILE   A HD13 1 
ATOM   2325 H HD13 B ILE   A 1 106 ? 19.621 -7.066  -10.604 0.20 33.58 ?  106 ILE   A HD13 1 
ATOM   2326 N N    A GLN   A 1 107 ? 22.677 -11.146 -11.381 0.80 24.41 ?  107 GLN   A N    1 
ATOM   2327 N N    B GLN   A 1 107 ? 22.838 -11.337 -11.479 0.20 26.69 ?  107 GLN   A N    1 
ATOM   2328 C CA   A GLN   A 1 107 ? 23.294 -12.360 -10.851 0.80 27.28 ?  107 GLN   A CA   1 
ATOM   2329 C CA   B GLN   A 1 107 ? 23.460 -12.503 -10.869 0.20 27.13 ?  107 GLN   A CA   1 
ATOM   2330 C C    A GLN   A 1 107 ? 24.270 -12.050 -9.718  0.80 24.58 ?  107 GLN   A C    1 
ATOM   2331 C C    B GLN   A 1 107 ? 24.417 -12.110 -9.755  0.20 24.11 ?  107 GLN   A C    1 
ATOM   2332 O O    A GLN   A 1 107 ? 24.492 -12.890 -8.838  0.80 25.93 ?  107 GLN   A O    1 
ATOM   2333 O O    B GLN   A 1 107 ? 24.777 -12.961 -8.934  0.20 24.64 ?  107 GLN   A O    1 
ATOM   2334 C CB   A GLN   A 1 107 ? 23.989 -13.122 -11.986 0.80 32.60 ?  107 GLN   A CB   1 
ATOM   2335 C CB   B GLN   A 1 107 ? 24.205 -13.320 -11.929 0.20 30.27 ?  107 GLN   A CB   1 
ATOM   2336 C CG   A GLN   A 1 107 ? 23.093 -13.365 -13.202 0.80 38.56 ?  107 GLN   A CG   1 
ATOM   2337 C CG   B GLN   A 1 107 ? 23.328 -13.801 -13.077 0.20 33.28 ?  107 GLN   A CG   1 
ATOM   2338 C CD   A GLN   A 1 107 ? 21.821 -14.113 -12.851 0.80 43.54 ?  107 GLN   A CD   1 
ATOM   2339 C CD   B GLN   A 1 107 ? 22.306 -14.831 -12.641 0.20 35.78 ?  107 GLN   A CD   1 
ATOM   2340 O OE1  A GLN   A 1 107 ? 21.859 -15.151 -12.188 0.80 45.26 ?  107 GLN   A OE1  1 
ATOM   2341 O OE1  B GLN   A 1 107 ? 22.536 -15.596 -11.704 0.20 36.57 ?  107 GLN   A OE1  1 
ATOM   2342 N NE2  A GLN   A 1 107 ? 20.683 -13.583 -13.287 0.80 45.06 ?  107 GLN   A NE2  1 
ATOM   2343 N NE2  B GLN   A 1 107 ? 21.165 -14.856 -13.323 0.20 36.48 ?  107 GLN   A NE2  1 
ATOM   2344 H H    A GLN   A 1 107 ? 22.823 -11.012 -12.216 0.80 29.29 ?  107 GLN   A H    1 
ATOM   2345 H H    B GLN   A 1 107 ? 22.993 -11.248 -12.317 0.20 32.02 ?  107 GLN   A H    1 
ATOM   2346 H HA   A GLN   A 1 107 ? 22.609 -12.937 -10.492 0.80 32.74 ?  107 GLN   A HA   1 
ATOM   2347 H HA   B GLN   A 1 107 ? 22.773 -13.069 -10.487 0.20 32.55 ?  107 GLN   A HA   1 
ATOM   2348 H HB2  A GLN   A 1 107 ? 24.760 -12.617 -12.290 0.80 39.12 ?  107 GLN   A HB2  1 
ATOM   2349 H HB2  B GLN   A 1 107 ? 24.910 -12.773 -12.307 0.20 36.33 ?  107 GLN   A HB2  1 
ATOM   2350 H HB3  A GLN   A 1 107 ? 24.275 -13.992 -11.663 0.80 39.12 ?  107 GLN   A HB3  1 
ATOM   2351 H HB3  B GLN   A 1 107 ? 24.591 -14.105 -11.507 0.20 36.33 ?  107 GLN   A HB3  1 
ATOM   2352 H HG2  A GLN   A 1 107 ? 22.841 -12.513 -13.593 0.80 46.27 ?  107 GLN   A HG2  1 
ATOM   2353 H HG2  B GLN   A 1 107 ? 22.851 -13.044 -13.451 0.20 39.94 ?  107 GLN   A HG2  1 
ATOM   2354 H HG3  A GLN   A 1 107 ? 23.581 -13.891 -13.857 0.80 46.27 ?  107 GLN   A HG3  1 
ATOM   2355 H HG3  B GLN   A 1 107 ? 23.891 -14.205 -13.756 0.20 39.94 ?  107 GLN   A HG3  1 
ATOM   2356 H HE21 A GLN   A 1 107 ? 20.694 -12.856 -13.746 0.80 54.07 ?  107 GLN   A HE21 1 
ATOM   2357 H HE21 B GLN   A 1 107 ? 21.040 -14.305 -13.971 0.20 43.77 ?  107 GLN   A HE21 1 
ATOM   2358 H HE22 A GLN   A 1 107 ? 19.935 -13.970 -13.112 0.80 54.07 ?  107 GLN   A HE22 1 
ATOM   2359 H HE22 B GLN   A 1 107 ? 20.552 -15.423 -13.116 0.20 43.77 ?  107 GLN   A HE22 1 
ATOM   2360 N N    . LEU   A 1 108 ? 24.835 -10.843 -9.701  1.00 20.88 ?  108 LEU   A N    1 
ATOM   2361 C CA   . LEU   A 1 108 ? 25.733 -10.417 -8.640  1.00 17.13 ?  108 LEU   A CA   1 
ATOM   2362 C C    . LEU   A 1 108 ? 25.016 -10.234 -7.311  1.00 14.69 ?  108 LEU   A C    1 
ATOM   2363 O O    . LEU   A 1 108 ? 25.687 -10.060 -6.293  1.00 15.24 ?  108 LEU   A O    1 
ATOM   2364 C CB   . LEU   A 1 108 ? 26.463 -9.123  -9.035  1.00 17.06 ?  108 LEU   A CB   1 
ATOM   2365 C CG   . LEU   A 1 108 ? 27.467 -9.318  -10.175 1.00 18.76 ?  108 LEU   A CG   1 
ATOM   2366 C CD1  . LEU   A 1 108 ? 27.945 -7.981  -10.730 1.00 19.79 ?  108 LEU   A CD1  1 
ATOM   2367 C CD2  . LEU   A 1 108 ? 28.655 -10.150 -9.718  1.00 20.98 ?  108 LEU   A CD2  1 
ATOM   2368 H H    A LEU   A 1 108 ? 24.703 -10.246 -10.296 0.80 25.05 ?  108 LEU   A H    1 
ATOM   2369 H H    B LEU   A 1 108 ? 24.627 -10.234 -10.261 0.20 25.05 ?  108 LEU   A H    1 
ATOM   2370 H HA   . LEU   A 1 108 ? 26.406 -11.102 -8.506  1.00 20.55 ?  108 LEU   A HA   1 
ATOM   2371 H HB2  . LEU   A 1 108 ? 25.808 -8.471  -9.328  1.00 20.47 ?  108 LEU   A HB2  1 
ATOM   2372 H HB3  . LEU   A 1 108 ? 26.946 -8.786  -8.267  1.00 20.47 ?  108 LEU   A HB3  1 
ATOM   2373 H HG   . LEU   A 1 108 ? 27.035 -9.800  -10.896 1.00 22.51 ?  108 LEU   A HG   1 
ATOM   2374 H HD11 . LEU   A 1 108 ? 28.566 -8.146  -11.462 1.00 23.75 ?  108 LEU   A HD11 1 
ATOM   2375 H HD12 . LEU   A 1 108 ? 27.181 -7.482  -11.055 1.00 23.75 ?  108 LEU   A HD12 1 
ATOM   2376 H HD13 . LEU   A 1 108 ? 28.393 -7.486  -10.027 1.00 23.75 ?  108 LEU   A HD13 1 
ATOM   2377 H HD21 . LEU   A 1 108 ? 29.345 -10.115 -10.398 1.00 25.18 ?  108 LEU   A HD21 1 
ATOM   2378 H HD22 . LEU   A 1 108 ? 28.993 -9.783  -8.885  1.00 25.18 ?  108 LEU   A HD22 1 
ATOM   2379 H HD23 . LEU   A 1 108 ? 28.368 -11.066 -9.583  1.00 25.18 ?  108 LEU   A HD23 1 
ATOM   2380 N N    . LEU   A 1 109 ? 23.679 -10.298 -7.286  1.00 13.98 ?  109 LEU   A N    1 
ATOM   2381 C CA   . LEU   A 1 109 ? 22.963 -10.164 -6.023  1.00 13.42 ?  109 LEU   A CA   1 
ATOM   2382 C C    . LEU   A 1 109 ? 23.300 -11.310 -5.074  1.00 12.85 ?  109 LEU   A C    1 
ATOM   2383 O O    . LEU   A 1 109 ? 23.444 -11.105 -3.866  1.00 13.53 ?  109 LEU   A O    1 
ATOM   2384 C CB   . LEU   A 1 109 ? 21.458 -10.095 -6.285  1.00 14.56 ?  109 LEU   A CB   1 
ATOM   2385 C CG   . LEU   A 1 109 ? 20.559 -9.778  -5.088  1.00 14.77 ?  109 LEU   A CG   1 
ATOM   2386 C CD1  . LEU   A 1 109 ? 21.006 -8.507  -4.386  1.00 14.63 ?  109 LEU   A CD1  1 
ATOM   2387 C CD2  . LEU   A 1 109 ? 19.095 -9.665  -5.529  1.00 15.66 ?  109 LEU   A CD2  1 
ATOM   2388 H H    . LEU   A 1 109 ? 23.177 -10.416 -7.972  1.00 16.78 ?  109 LEU   A H    1 
ATOM   2389 H HA   . LEU   A 1 109 ? 23.236 -9.334  -5.598  1.00 16.11 ?  109 LEU   A HA   1 
ATOM   2390 H HB2  . LEU   A 1 109 ? 21.298 -9.405  -6.946  1.00 17.48 ?  109 LEU   A HB2  1 
ATOM   2391 H HB3  . LEU   A 1 109 ? 21.171 -10.950 -6.631  1.00 17.48 ?  109 LEU   A HB3  1 
ATOM   2392 H HG   . LEU   A 1 109 ? 20.616 -10.501 -4.446  1.00 17.72 ?  109 LEU   A HG   1 
ATOM   2393 H HD11 . LEU   A 1 109 ? 20.323 -8.229  -3.755  1.00 17.56 ?  109 LEU   A HD11 1 
ATOM   2394 H HD12 . LEU   A 1 109 ? 21.839 -8.672  -3.923  1.00 17.56 ?  109 LEU   A HD12 1 
ATOM   2395 H HD13 . LEU   A 1 109 ? 21.134 -7.805  -5.054  1.00 17.56 ?  109 LEU   A HD13 1 
ATOM   2396 H HD21 . LEU   A 1 109 ? 18.557 -9.350  -4.782  1.00 18.79 ?  109 LEU   A HD21 1 
ATOM   2397 H HD22 . LEU   A 1 109 ? 19.027 -9.041  -6.267  1.00 18.79 ?  109 LEU   A HD22 1 
ATOM   2398 H HD23 . LEU   A 1 109 ? 18.778 -10.542 -5.809  1.00 18.79 ?  109 LEU   A HD23 1 
ATOM   2399 N N    . LYS   A 1 110 ? 23.424 -12.533 -5.596  1.00 13.21 ?  110 LYS   A N    1 
ATOM   2400 C CA   . LYS   A 1 110 ? 23.798 -13.646 -4.730  1.00 13.40 ?  110 LYS   A CA   1 
ATOM   2401 C C    . LYS   A 1 110 ? 25.184 -13.424 -4.129  1.00 12.50 ?  110 LYS   A C    1 
ATOM   2402 O O    . LYS   A 1 110 ? 25.382 -13.623 -2.931  1.00 12.84 ?  110 LYS   A O    1 
ATOM   2403 C CB   . LYS   A 1 110 ? 23.716 -14.979 -5.482  1.00 14.61 ?  110 LYS   A CB   1 
ATOM   2404 C CG   . LYS   A 1 110 ? 23.922 -16.192 -4.571  1.00 14.64 ?  110 LYS   A CG   1 
ATOM   2405 C CD   . LYS   A 1 110 ? 23.703 -17.524 -5.288  1.00 15.16 ?  110 LYS   A CD   1 
ATOM   2406 C CE   . LYS   A 1 110 ? 23.806 -18.709 -4.333  1.00 15.80 ?  110 LYS   A CE   1 
ATOM   2407 N NZ   . LYS   A 1 110 ? 22.626 -18.819 -3.430  1.00 16.13 ?  110 LYS   A NZ   1 
ATOM   2408 H H    . LYS   A 1 110 ? 23.296 -12.739 -6.413  1.00 15.85 ?  110 LYS   A H    1 
ATOM   2409 H HA   . LYS   A 1 110 ? 23.170 -13.694 -3.988  1.00 16.08 ?  110 LYS   A HA   1 
ATOM   2410 H HB2  . LYS   A 1 110 ? 22.836 -15.058 -5.885  1.00 17.54 ?  110 LYS   A HB2  1 
ATOM   2411 H HB3  . LYS   A 1 110 ? 24.400 -15.000 -6.165  1.00 17.54 ?  110 LYS   A HB3  1 
ATOM   2412 H HG2  . LYS   A 1 110 ? 24.830 -16.179 -4.228  1.00 17.57 ?  110 LYS   A HG2  1 
ATOM   2413 H HG3  . LYS   A 1 110 ? 23.293 -16.143 -3.833  1.00 17.57 ?  110 LYS   A HG3  1 
ATOM   2414 H HD2  . LYS   A 1 110 ? 22.822 -17.535 -5.684  1.00 18.19 ?  110 LYS   A HD2  1 
ATOM   2415 H HD3  . LYS   A 1 110 ? 24.384 -17.631 -5.974  1.00 18.19 ?  110 LYS   A HD3  1 
ATOM   2416 H HE2  . LYS   A 1 110 ? 23.875 -19.530 -4.845  1.00 18.96 ?  110 LYS   A HE2  1 
ATOM   2417 H HE3  . LYS   A 1 110 ? 24.601 -18.602 -3.777  1.00 18.96 ?  110 LYS   A HE3  1 
ATOM   2418 H HZ1  . LYS   A 1 110 ? 22.717 -19.514 -2.886  1.00 19.35 ?  110 LYS   A HZ1  1 
ATOM   2419 H HZ2  . LYS   A 1 110 ? 22.548 -18.077 -2.941  1.00 19.35 ?  110 LYS   A HZ2  1 
ATOM   2420 H HZ3  . LYS   A 1 110 ? 21.885 -18.922 -3.914  1.00 19.35 ?  110 LYS   A HZ3  1 
ATOM   2421 N N    . SER   A 1 111 ? 26.143 -12.980 -4.946  1.00 12.99 ?  111 SER   A N    1 
ATOM   2422 C CA   . SER   A 1 111 ? 27.475 -12.662 -4.437  1.00 13.09 ?  111 SER   A CA   1 
ATOM   2423 C C    . SER   A 1 111 ? 27.412 -11.611 -3.333  1.00 12.65 ?  111 SER   A C    1 
ATOM   2424 O O    . SER   A 1 111 ? 28.099 -11.723 -2.313  1.00 13.42 ?  111 SER   A O    1 
ATOM   2425 C CB   . SER   A 1 111 ? 28.347 -12.165 -5.589  1.00 14.34 ?  111 SER   A CB   1 
ATOM   2426 O OG   . SER   A 1 111 ? 28.461 -13.166 -6.590  1.00 16.04 ?  111 SER   A OG   1 
ATOM   2427 H H    . SER   A 1 111 ? 26.042 -12.862 -5.789  1.00 15.59 ?  111 SER   A H    1 
ATOM   2428 H HA   . SER   A 1 111 ? 27.885 -13.465 -4.076  1.00 15.71 ?  111 SER   A HA   1 
ATOM   2429 H HB2  . SER   A 1 111 ? 27.935 -11.381 -5.985  1.00 17.21 ?  111 SER   A HB2  1 
ATOM   2430 H HB3  . SER   A 1 111 ? 29.228 -11.944 -5.252  1.00 17.21 ?  111 SER   A HB3  1 
ATOM   2431 H HG   . SER   A 1 111 ? 28.956 -12.887 -7.219  1.00 19.25 ?  111 SER   A HG   1 
ATOM   2432 N N    . ALA   A 1 112 ? 26.571 -10.593 -3.510  1.00 12.51 ?  112 ALA   A N    1 
ATOM   2433 C CA   . ALA   A 1 112 ? 26.430 -9.561  -2.486  1.00 12.04 ?  112 ALA   A CA   1 
ATOM   2434 C C    . ALA   A 1 112 ? 25.941 -10.159 -1.170  1.00 11.65 ?  112 ALA   A C    1 
ATOM   2435 O O    . ALA   A 1 112 ? 26.481 -9.860  -0.098  1.00 12.47 ?  112 ALA   A O    1 
ATOM   2436 C CB   . ALA   A 1 112 ? 25.477 -8.467  -2.973  1.00 12.81 ?  112 ALA   A CB   1 
ATOM   2437 H H    . ALA   A 1 112 ? 26.081 -10.475 -4.207  1.00 15.01 ?  112 ALA   A H    1 
ATOM   2438 H HA   . ALA   A 1 112 ? 27.295 -9.147  -2.330  1.00 14.44 ?  112 ALA   A HA   1 
ATOM   2439 H HB1  . ALA   A 1 112 ? 25.404 -7.777  -2.286  1.00 15.37 ?  112 ALA   A HB1  1 
ATOM   2440 H HB2  . ALA   A 1 112 ? 25.825 -8.073  -3.789  1.00 15.37 ?  112 ALA   A HB2  1 
ATOM   2441 H HB3  . ALA   A 1 112 ? 24.603 -8.853  -3.139  1.00 15.37 ?  112 ALA   A HB3  1 
ATOM   2442 N N    . TYR   A 1 113 ? 24.896 -10.991 -1.226  1.00 12.17 ?  113 TYR   A N    1 
ATOM   2443 C CA   . TYR   A 1 113 ? 24.379 -11.600 -0.004  1.00 12.11 ?  113 TYR   A CA   1 
ATOM   2444 C C    . TYR   A 1 113 ? 25.377 -12.551 0.653   1.00 11.81 ?  113 TYR   A C    1 
ATOM   2445 O O    . TYR   A 1 113 ? 25.330 -12.738 1.875   1.00 12.73 ?  113 TYR   A O    1 
ATOM   2446 C CB   . TYR   A 1 113 ? 23.059 -12.323 -0.279  1.00 12.47 ?  113 TYR   A CB   1 
ATOM   2447 C CG   . TYR   A 1 113 ? 21.837 -11.427 -0.210  1.00 11.74 ?  113 TYR   A CG   1 
ATOM   2448 C CD1  . TYR   A 1 113 ? 21.460 -10.820 0.986   1.00 12.49 ?  113 TYR   A CD1  1 
ATOM   2449 C CD2  . TYR   A 1 113 ? 21.043 -11.207 -1.330  1.00 12.39 ?  113 TYR   A CD2  1 
ATOM   2450 C CE1  . TYR   A 1 113 ? 20.340 -10.035 1.066   1.00 12.70 ?  113 TYR   A CE1  1 
ATOM   2451 C CE2  . TYR   A 1 113 ? 19.893 -10.412 -1.255  1.00 12.83 ?  113 TYR   A CE2  1 
ATOM   2452 C CZ   . TYR   A 1 113 ? 19.560 -9.825  -0.050  1.00 12.44 ?  113 TYR   A CZ   1 
ATOM   2453 O OH   . TYR   A 1 113 ? 18.434 -9.036  0.070   1.00 13.09 ?  113 TYR   A OH   1 
ATOM   2454 H H    . TYR   A 1 113 ? 24.487 -11.212 -1.951  1.00 14.60 ?  113 TYR   A H    1 
ATOM   2455 H HA   . TYR   A 1 113 ? 24.202 -10.895 0.630   1.00 14.53 ?  113 TYR   A HA   1 
ATOM   2456 H HB2  . TYR   A 1 113 ? 23.087 -12.707 -1.167  1.00 14.96 ?  113 TYR   A HB2  1 
ATOM   2457 H HB3  . TYR   A 1 113 ? 22.946 -13.025 0.380   1.00 14.96 ?  113 TYR   A HB3  1 
ATOM   2458 H HD1  . TYR   A 1 113 ? 21.975 -10.960 1.750   1.00 14.99 ?  113 TYR   A HD1  1 
ATOM   2459 H HD2  . TYR   A 1 113 ? 21.265 -11.614 -2.136  1.00 14.87 ?  113 TYR   A HD2  1 
ATOM   2460 H HE1  . TYR   A 1 113 ? 20.108 -9.636  1.875   1.00 15.24 ?  113 TYR   A HE1  1 
ATOM   2461 H HE2  . TYR   A 1 113 ? 19.365 -10.266 -2.005  1.00 15.39 ?  113 TYR   A HE2  1 
ATOM   2462 H HH   . TYR   A 1 113 ? 18.053 -8.985  -0.676  1.00 15.70 ?  113 TYR   A HH   1 
ATOM   2463 N N    . GLU   A 1 114 ? 26.281 -13.163 -0.123  1.00 11.81 ?  114 GLU   A N    1 
ATOM   2464 C CA   . GLU   A 1 114 ? 27.271 -14.057 0.479   1.00 12.00 ?  114 GLU   A CA   1 
ATOM   2465 C C    . GLU   A 1 114 ? 28.115 -13.347 1.532   1.00 11.98 ?  114 GLU   A C    1 
ATOM   2466 O O    . GLU   A 1 114 ? 28.600 -13.981 2.478   1.00 12.80 ?  114 GLU   A O    1 
ATOM   2467 C CB   . GLU   A 1 114 ? 28.142 -14.713 -0.605  1.00 12.52 ?  114 GLU   A CB   1 
ATOM   2468 C CG   . GLU   A 1 114 ? 27.396 -15.773 -1.381  1.00 13.22 ?  114 GLU   A CG   1 
ATOM   2469 C CD   . GLU   A 1 114 ? 28.113 -16.303 -2.615  1.00 13.84 ?  114 GLU   A CD   1 
ATOM   2470 O OE1  . GLU   A 1 114 ? 29.067 -15.666 -3.109  1.00 14.13 ?  114 GLU   A OE1  1 
ATOM   2471 O OE2  . GLU   A 1 114 ? 27.680 -17.364 -3.108  1.00 15.17 -1 114 GLU   A OE2  1 
ATOM   2472 H H    . GLU   A 1 114 ? 26.347 -13.068 -0.985  1.00 14.18 ?  114 GLU   A H    1 
ATOM   2473 H HA   . GLU   A 1 114 ? 26.796 -14.768 0.922   1.00 14.40 ?  114 GLU   A HA   1 
ATOM   2474 H HB2  . GLU   A 1 114 ? 28.435 -14.035 -1.240  1.00 15.02 ?  114 GLU   A HB2  1 
ATOM   2475 H HB3  . GLU   A 1 114 ? 28.908 -15.132 -0.192  1.00 15.02 ?  114 GLU   A HB3  1 
ATOM   2476 H HG2  . GLU   A 1 114 ? 27.243 -16.530 -0.800  1.00 15.87 ?  114 GLU   A HG2  1 
ATOM   2477 H HG3  . GLU   A 1 114 ? 26.547 -15.406 -1.673  1.00 15.87 ?  114 GLU   A HG3  1 
ATOM   2478 N N    . ASN   A 1 115 ? 28.306 -12.034 1.394   1.00 12.11 ?  115 ASN   A N    1 
ATOM   2479 C CA   . ASN   A 1 115 ? 29.071 -11.305 2.399   1.00 12.85 ?  115 ASN   A CA   1 
ATOM   2480 C C    . ASN   A 1 115 ? 28.446 -11.432 3.784   1.00 12.59 ?  115 ASN   A C    1 
ATOM   2481 O O    . ASN   A 1 115 ? 29.152 -11.360 4.794   1.00 13.19 ?  115 ASN   A O    1 
ATOM   2482 C CB   . ASN   A 1 115 ? 29.200 -9.829  2.021   1.00 12.82 ?  115 ASN   A CB   1 
ATOM   2483 C CG   . ASN   A 1 115 ? 29.994 -9.623  0.752   1.00 13.41 ?  115 ASN   A CG   1 
ATOM   2484 O OD1  . ASN   A 1 115 ? 31.211 -9.767  0.757   1.00 16.54 ?  115 ASN   A OD1  1 
ATOM   2485 N ND2  . ASN   A 1 115 ? 29.324 -9.299  -0.335  1.00 12.84 ?  115 ASN   A ND2  1 
ATOM   2486 H H    . ASN   A 1 115 ? 28.005 -11.550 0.746   1.00 14.53 ?  115 ASN   A H    1 
ATOM   2487 H HA   . ASN   A 1 115 ? 29.962 -11.683 2.443   1.00 15.42 ?  115 ASN   A HA   1 
ATOM   2488 H HB2  . ASN   A 1 115 ? 28.313 -9.458  1.898   1.00 15.38 ?  115 ASN   A HB2  1 
ATOM   2489 H HB3  . ASN   A 1 115 ? 29.656 -9.363  2.742   1.00 15.38 ?  115 ASN   A HB3  1 
ATOM   2490 H HD21 . ASN   A 1 115 ? 29.737 -9.176  -1.076  1.00 15.40 ?  115 ASN   A HD21 1 
ATOM   2491 H HD22 . ASN   A 1 115 ? 28.463 -9.229  -0.305  1.00 15.40 ?  115 ASN   A HD22 1 
ATOM   2492 N N    . PHE   A 1 116 ? 27.118 -11.607 3.856   1.00 12.64 ?  116 PHE   A N    1 
ATOM   2493 C CA   . PHE   A 1 116 ? 26.454 -11.699 5.157   1.00 12.56 ?  116 PHE   A CA   1 
ATOM   2494 C C    . PHE   A 1 116 ? 26.921 -12.926 5.935   1.00 12.78 ?  116 PHE   A C    1 
ATOM   2495 O O    . PHE   A 1 116 ? 26.855 -12.947 7.168   1.00 13.36 ?  116 PHE   A O    1 
ATOM   2496 C CB   . PHE   A 1 116 ? 24.927 -11.826 5.010   1.00 12.87 ?  116 PHE   A CB   1 
ATOM   2497 C CG   . PHE   A 1 116 ? 24.182 -10.580 4.539   1.00 12.40 ?  116 PHE   A CG   1 
ATOM   2498 C CD1  . PHE   A 1 116 ? 24.765 -9.561  3.799   1.00 12.04 ?  116 PHE   A CD1  1 
ATOM   2499 C CD2  . PHE   A 1 116 ? 22.830 -10.472 4.844   1.00 12.89 ?  116 PHE   A CD2  1 
ATOM   2500 C CE1  . PHE   A 1 116 ? 24.001 -8.487  3.373   1.00 12.34 ?  116 PHE   A CE1  1 
ATOM   2501 C CE2  . PHE   A 1 116 ? 22.071 -9.400  4.436   1.00 13.12 ?  116 PHE   A CE2  1 
ATOM   2502 C CZ   . PHE   A 1 116 ? 22.643 -8.406  3.697   1.00 12.59 ?  116 PHE   A CZ   1 
ATOM   2503 H H    . PHE   A 1 116 ? 26.587 -11.659 3.178   1.00 15.17 ?  116 PHE   A H    1 
ATOM   2504 H HA   . PHE   A 1 116 ? 26.648 -10.907 5.682   1.00 15.07 ?  116 PHE   A HA   1 
ATOM   2505 H HB2  . PHE   A 1 116 ? 24.742 -12.532 4.371   1.00 15.44 ?  116 PHE   A HB2  1 
ATOM   2506 H HB3  . PHE   A 1 116 ? 24.561 -12.076 5.875   1.00 15.44 ?  116 PHE   A HB3  1 
ATOM   2507 H HD1  . PHE   A 1 116 ? 25.663 -9.621  3.570   1.00 14.45 ?  116 PHE   A HD1  1 
ATOM   2508 H HD2  . PHE   A 1 116 ? 22.420 -11.156 5.342   1.00 15.47 ?  116 PHE   A HD2  1 
ATOM   2509 H HE1  . PHE   A 1 116 ? 24.405 -7.806  2.880   1.00 14.81 ?  116 PHE   A HE1  1 
ATOM   2510 H HE2  . PHE   A 1 116 ? 21.164 -9.356  4.660   1.00 15.74 ?  116 PHE   A HE2  1 
ATOM   2511 H HZ   . PHE   A 1 116 ? 22.140 -7.669  3.427   1.00 15.10 ?  116 PHE   A HZ   1 
ATOM   2512 N N    . ASN   A 1 117 ? 27.379 -13.964 5.233   1.00 13.00 ?  117 ASN   A N    1 
ATOM   2513 C CA   . ASN   A 1 117 ? 27.740 -15.208 5.908   1.00 13.62 ?  117 ASN   A CA   1 
ATOM   2514 C C    . ASN   A 1 117 ? 28.999 -15.089 6.749   1.00 13.79 ?  117 ASN   A C    1 
ATOM   2515 O O    . ASN   A 1 117 ? 29.282 -16.005 7.529   1.00 14.54 ?  117 ASN   A O    1 
ATOM   2516 C CB   . ASN   A 1 117 ? 27.868 -16.346 4.895   1.00 13.93 ?  117 ASN   A CB   1 
ATOM   2517 C CG   . ASN   A 1 117 ? 26.520 -16.743 4.350   1.00 13.96 ?  117 ASN   A CG   1 
ATOM   2518 O OD1  . ASN   A 1 117 ? 25.539 -16.758 5.085   1.00 14.51 ?  117 ASN   A OD1  1 
ATOM   2519 N ND2  . ASN   A 1 117 ? 26.452 -17.002 3.062   1.00 13.28 ?  117 ASN   A ND2  1 
ATOM   2520 H H    . ASN   A 1 117 ? 27.462 -13.983 4.373   1.00 15.60 ?  117 ASN   A H    1 
ATOM   2521 H HA   . ASN   A 1 117 ? 27.018 -15.446 6.509   1.00 16.34 ?  117 ASN   A HA   1 
ATOM   2522 H HB2  . ASN   A 1 117 ? 28.423 -16.052 4.154   1.00 16.71 ?  117 ASN   A HB2  1 
ATOM   2523 H HB3  . ASN   A 1 117 ? 28.259 -17.117 5.327   1.00 16.71 ?  117 ASN   A HB3  1 
ATOM   2524 H HD21 . ASN   A 1 117 ? 25.706 -17.228 2.714   1.00 15.93 ?  117 ASN   A HD21 1 
ATOM   2525 H HD22 . ASN   A 1 117 ? 27.168 -16.972 2.584   1.00 15.93 ?  117 ASN   A HD22 1 
ATOM   2526 N N    . GLN   A 1 118 ? 29.739 -13.990 6.630   1.00 13.71 ?  118 GLN   A N    1 
ATOM   2527 C CA   . GLN   A 1 118 ? 30.908 -13.757 7.467   1.00 14.26 ?  118 GLN   A CA   1 
ATOM   2528 C C    . GLN   A 1 118 ? 30.552 -13.190 8.837   1.00 14.28 ?  118 GLN   A C    1 
ATOM   2529 O O    . GLN   A 1 118 ? 31.466 -12.903 9.623   1.00 15.60 ?  118 GLN   A O    1 
ATOM   2530 C CB   . GLN   A 1 118 ? 31.908 -12.857 6.736   1.00 14.71 ?  118 GLN   A CB   1 
ATOM   2531 C CG   . GLN   A 1 118 ? 32.380 -13.431 5.414   1.00 14.05 ?  118 GLN   A CG   1 
ATOM   2532 C CD   . GLN   A 1 118 ? 33.229 -14.679 5.587   1.00 14.69 ?  118 GLN   A CD   1 
ATOM   2533 O OE1  . GLN   A 1 118 ? 34.084 -14.750 6.479   1.00 15.68 ?  118 GLN   A OE1  1 
ATOM   2534 N NE2  . GLN   A 1 118 ? 32.987 -15.682 4.735   1.00 14.65 ?  118 GLN   A NE2  1 
ATOM   2535 H H    . GLN   A 1 118 ? 29.577 -13.353 6.071   1.00 16.45 ?  118 GLN   A H    1 
ATOM   2536 H HA   . GLN   A 1 118 ? 31.339 -14.614 7.618   1.00 17.11 ?  118 GLN   A HA   1 
ATOM   2537 H HB2  . GLN   A 1 118 ? 31.487 -12.003 6.562   1.00 17.66 ?  118 GLN   A HB2  1 
ATOM   2538 H HB3  . GLN   A 1 118 ? 32.685 -12.736 7.304   1.00 17.66 ?  118 GLN   A HB3  1 
ATOM   2539 H HG2  . GLN   A 1 118 ? 31.607 -13.661 4.869   1.00 16.86 ?  118 GLN   A HG2  1 
ATOM   2540 H HG3  . GLN   A 1 118 ? 32.918 -12.767 4.954   1.00 16.86 ?  118 GLN   A HG3  1 
ATOM   2541 H HE21 . GLN   A 1 118 ? 32.371 -15.595 4.128   1.00 17.58 ?  118 GLN   A HE21 1 
ATOM   2542 H HE22 . GLN   A 1 118 ? 33.429 -16.413 4.784   1.00 17.58 ?  118 GLN   A HE22 1 
ATOM   2543 N N    . HIS   A 1 119 ? 29.260 -13.020 9.140   1.00 13.85 ?  119 HIS   A N    1 
ATOM   2544 C CA   . HIS   A 1 119 ? 28.800 -12.408 10.383  1.00 14.41 ?  119 HIS   A CA   1 
ATOM   2545 C C    . HIS   A 1 119 ? 27.655 -13.220 10.960  1.00 15.54 ?  119 HIS   A C    1 
ATOM   2546 O O    . HIS   A 1 119 ? 26.714 -13.568 10.242  1.00 15.39 ?  119 HIS   A O    1 
ATOM   2547 C CB   . HIS   A 1 119 ? 28.355 -10.971 10.114  1.00 14.54 ?  119 HIS   A CB   1 
ATOM   2548 C CG   . HIS   A 1 119 ? 29.437 -10.172 9.479   1.00 15.70 ?  119 HIS   A CG   1 
ATOM   2549 N ND1  . HIS   A 1 119 ? 30.410 -9.534  10.215  1.00 18.39 ?  119 HIS   A ND1  1 
ATOM   2550 C CD2  . HIS   A 1 119 ? 29.767 -9.998  8.178   1.00 16.49 ?  119 HIS   A CD2  1 
ATOM   2551 C CE1  . HIS   A 1 119 ? 31.273 -8.966  9.391   1.00 18.60 ?  119 HIS   A CE1  1 
ATOM   2552 N NE2  . HIS   A 1 119 ? 30.917 -9.246  8.151   1.00 18.12 ?  119 HIS   A NE2  1 
ATOM   2553 H H    . HIS   A 1 119 ? 28.608 -13.259 8.624   1.00 16.62 ?  119 HIS   A H    1 
ATOM   2554 H HA   . HIS   A 1 119 ? 29.525 -12.396 11.024  1.00 17.29 ?  119 HIS   A HA   1 
ATOM   2555 H HB2  . HIS   A 1 119 ? 27.587 -10.983 9.518   1.00 17.45 ?  119 HIS   A HB2  1 
ATOM   2556 H HB3  . HIS   A 1 119 ? 28.117 -10.552 10.956  1.00 17.45 ?  119 HIS   A HB3  1 
ATOM   2557 H HD2  . HIS   A 1 119 ? 29.307 -10.335 7.439   1.00 19.78 ?  119 HIS   A HD2  1 
ATOM   2558 H HE1  . HIS   A 1 119 ? 32.007 -8.458  9.641   1.00 22.32 ?  119 HIS   A HE1  1 
ATOM   2559 H HE2  . HIS   A 1 119 ? 31.314 -8.969  7.441   1.00 21.75 ?  119 HIS   A HE2  1 
ATOM   2560 N N    A GLU   A 1 120 ? 27.743 -13.520 12.258  0.80 15.88 ?  120 GLU   A N    1 
ATOM   2561 N N    B GLU   A 1 120 ? 27.724 -13.501 12.264  0.20 18.25 ?  120 GLU   A N    1 
ATOM   2562 C CA   A GLU   A 1 120 ? 26.787 -14.440 12.868  0.80 18.06 ?  120 GLU   A CA   1 
ATOM   2563 C CA   B GLU   A 1 120 ? 26.754 -14.406 12.878  0.20 21.19 ?  120 GLU   A CA   1 
ATOM   2564 C C    A GLU   A 1 120 ? 25.371 -13.874 12.915  0.80 16.39 ?  120 GLU   A C    1 
ATOM   2565 C C    B GLU   A 1 120 ? 25.347 -13.813 12.893  0.20 19.90 ?  120 GLU   A C    1 
ATOM   2566 O O    A GLU   A 1 120 ? 24.399 -14.637 12.799  0.80 16.66 ?  120 GLU   A O    1 
ATOM   2567 O O    B GLU   A 1 120 ? 24.368 -14.527 12.641  0.20 19.85 ?  120 GLU   A O    1 
ATOM   2568 C CB   A GLU   A 1 120 ? 27.255 -14.824 14.272  0.80 22.45 ?  120 GLU   A CB   1 
ATOM   2569 C CB   B GLU   A 1 120 ? 27.205 -14.789 14.288  0.20 25.41 ?  120 GLU   A CB   1 
ATOM   2570 C CG   A GLU   A 1 120 ? 28.452 -15.761 14.281  0.80 28.77 ?  120 GLU   A CG   1 
ATOM   2571 C CG   B GLU   A 1 120 ? 28.423 -15.703 14.317  0.20 29.82 ?  120 GLU   A CG   1 
ATOM   2572 C CD   A GLU   A 1 120 ? 28.601 -16.501 15.593  0.80 34.70 ?  120 GLU   A CD   1 
ATOM   2573 C CD   B GLU   A 1 120 ? 28.593 -16.406 15.650  0.20 33.46 ?  120 GLU   A CD   1 
ATOM   2574 O OE1  A GLU   A 1 120 ? 28.166 -15.961 16.633  0.80 36.29 ?  120 GLU   A OE1  1 
ATOM   2575 O OE1  B GLU   A 1 120 ? 28.106 -15.875 16.670  0.20 34.40 ?  120 GLU   A OE1  1 
ATOM   2576 O OE2  A GLU   A 1 120 ? 29.148 -17.625 15.584  0.80 37.10 -1 120 GLU   A OE2  1 
ATOM   2577 O OE2  B GLU   A 1 120 ? 29.211 -17.491 15.675  0.20 34.74 -1 120 GLU   A OE2  1 
ATOM   2578 H H    A GLU   A 1 120 ? 28.345 -13.214 12.794  0.80 19.06 ?  120 GLU   A H    1 
ATOM   2579 H H    B GLU   A 1 120 ? 28.318 -13.189 12.804  0.20 21.90 ?  120 GLU   A H    1 
ATOM   2580 H HA   A GLU   A 1 120 ? 26.764 -15.255 12.345  0.80 21.68 ?  120 GLU   A HA   1 
ATOM   2581 H HA   B GLU   A 1 120 ? 26.721 -15.220 12.355  0.20 25.43 ?  120 GLU   A HA   1 
ATOM   2582 H HB2  A GLU   A 1 120 ? 27.509 -14.024 14.758  0.80 26.94 ?  120 GLU   A HB2  1 
ATOM   2583 H HB2  B GLU   A 1 120 ? 27.432 -13.983 14.778  0.20 30.49 ?  120 GLU   A HB2  1 
ATOM   2584 H HB3  A GLU   A 1 120 ? 26.529 -15.274 14.740  0.80 26.94 ?  120 GLU   A HB3  1 
ATOM   2585 H HB3  B GLU   A 1 120 ? 26.479 -15.252 14.735  0.20 30.49 ?  120 GLU   A HB3  1 
ATOM   2586 H HG2  A GLU   A 1 120 ? 28.353 -16.411 13.567  0.80 34.52 ?  120 GLU   A HG2  1 
ATOM   2587 H HG2  B GLU   A 1 120 ? 28.333 -16.373 13.621  0.20 35.79 ?  120 GLU   A HG2  1 
ATOM   2588 H HG3  A GLU   A 1 120 ? 29.262 -15.247 14.154  0.80 34.52 ?  120 GLU   A HG3  1 
ATOM   2589 H HG3  B GLU   A 1 120 ? 29.221 -15.174 14.168  0.20 35.79 ?  120 GLU   A HG3  1 
ATOM   2590 N N    A VAL   A 1 121 ? 25.236 -12.561 13.112  0.80 15.64 ?  121 VAL   A N    1 
ATOM   2591 N N    B VAL   A 1 121 ? 25.220 -12.521 13.188  0.20 18.76 ?  121 VAL   A N    1 
ATOM   2592 C CA   A VAL   A 1 121 ? 23.940 -11.894 13.220  0.80 15.97 ?  121 VAL   A CA   1 
ATOM   2593 C CA   B VAL   A 1 121 ? 23.923 -11.853 13.271  0.20 17.82 ?  121 VAL   A CA   1 
ATOM   2594 C C    A VAL   A 1 121 ? 24.053 -10.520 12.571  0.80 14.73 ?  121 VAL   A C    1 
ATOM   2595 C C    B VAL   A 1 121 ? 24.040 -10.493 12.599  0.20 15.92 ?  121 VAL   A C    1 
ATOM   2596 O O    A VAL   A 1 121 ? 25.026 -9.799  12.809  0.80 14.99 ?  121 VAL   A O    1 
ATOM   2597 O O    B VAL   A 1 121 ? 25.017 -9.769  12.816  0.20 16.05 ?  121 VAL   A O    1 
ATOM   2598 C CB   A VAL   A 1 121 ? 23.502 -11.729 14.693  0.80 18.98 ?  121 VAL   A CB   1 
ATOM   2599 C CB   B VAL   A 1 121 ? 23.457 -11.691 14.736  0.20 19.00 ?  121 VAL   A CB   1 
ATOM   2600 C CG1  A VAL   A 1 121 ? 22.116 -11.099 14.769  0.80 19.56 ?  121 VAL   A CG1  1 
ATOM   2601 C CG1  B VAL   A 1 121 ? 22.092 -11.018 14.792  0.20 19.30 ?  121 VAL   A CG1  1 
ATOM   2602 C CG2  A VAL   A 1 121 ? 23.516 -13.053 15.434  0.80 21.00 ?  121 VAL   A CG2  1 
ATOM   2603 C CG2  B VAL   A 1 121 ? 23.418 -13.035 15.451  0.20 19.63 ?  121 VAL   A CG2  1 
ATOM   2604 H H    A VAL   A 1 121 ? 25.905 -12.022 13.193  0.80 18.77 ?  121 VAL   A H    1 
ATOM   2605 H H    B VAL   A 1 121 ? 25.885 -11.998 13.343  0.20 22.52 ?  121 VAL   A H    1 
ATOM   2606 H HA   A VAL   A 1 121 ? 23.270 -12.414 12.752  0.80 19.17 ?  121 VAL   A HA   1 
ATOM   2607 H HA   B VAL   A 1 121 ? 23.259 -12.376 12.798  0.20 21.39 ?  121 VAL   A HA   1 
ATOM   2608 H HB   A VAL   A 1 121 ? 24.121 -11.134 15.142  0.80 22.77 ?  121 VAL   A HB   1 
ATOM   2609 H HB   B VAL   A 1 121 ? 24.087 -11.124 15.206  0.20 22.80 ?  121 VAL   A HB   1 
ATOM   2610 H HG11 A VAL   A 1 121 ? 21.794 -11.149 15.684  0.80 23.47 ?  121 VAL   A HG11 1 
ATOM   2611 H HG11 B VAL   A 1 121 ? 21.745 -11.085 15.697  0.20 23.16 ?  121 VAL   A HG11 1 
ATOM   2612 H HG12 A VAL   A 1 121 ? 22.171 -10.172 14.490  0.80 23.47 ?  121 VAL   A HG12 1 
ATOM   2613 H HG12 B VAL   A 1 121 ? 22.186 -10.085 14.545  0.20 23.16 ?  121 VAL   A HG12 1 
ATOM   2614 H HG13 A VAL   A 1 121 ? 21.514 -11.587 14.183  0.80 23.47 ?  121 VAL   A HG13 1 
ATOM   2615 H HG13 B VAL   A 1 121 ? 21.492 -11.467 14.176  0.20 23.16 ?  121 VAL   A HG13 1 
ATOM   2616 H HG21 A VAL   A 1 121 ? 23.161 -12.917 16.332  0.80 25.20 ?  121 VAL   A HG21 1 
ATOM   2617 H HG21 B VAL   A 1 121 ? 23.072 -12.904 16.350  0.20 23.55 ?  121 VAL   A HG21 1 
ATOM   2618 H HG22 A VAL   A 1 121 ? 22.956 -13.689 14.959  0.80 25.20 ?  121 VAL   A HG22 1 
ATOM   2619 H HG22 B VAL   A 1 121 ? 22.838 -13.638 14.961  0.20 23.55 ?  121 VAL   A HG22 1 
ATOM   2620 H HG23 A VAL   A 1 121 ? 24.423 -13.382 15.486  0.80 25.20 ?  121 VAL   A HG23 1 
ATOM   2621 H HG23 B VAL   A 1 121 ? 24.316 -13.398 15.494  0.20 23.55 ?  121 VAL   A HG23 1 
ATOM   2622 N N    . LEU   A 1 122 ? 23.041 -10.137 11.788  1.00 14.01 ?  122 LEU   A N    1 
ATOM   2623 C CA   . LEU   A 1 122 ? 23.045 -8.845  11.108  1.00 13.35 ?  122 LEU   A CA   1 
ATOM   2624 C C    . LEU   A 1 122 ? 21.651 -8.236  11.064  1.00 13.33 ?  122 LEU   A C    1 
ATOM   2625 O O    . LEU   A 1 122 ? 20.655 -8.950  10.922  1.00 14.30 ?  122 LEU   A O    1 
ATOM   2626 C CB   . LEU   A 1 122 ? 23.500 -8.954  9.651   1.00 14.86 ?  122 LEU   A CB   1 
ATOM   2627 C CG   . LEU   A 1 122 ? 24.708 -9.804  9.293   1.00 14.65 ?  122 LEU   A CG   1 
ATOM   2628 C CD1  . LEU   A 1 122 ? 24.302 -11.254 9.066   1.00 15.42 ?  122 LEU   A CD1  1 
ATOM   2629 C CD2  . LEU   A 1 122 ? 25.394 -9.230  8.061   1.00 13.79 ?  122 LEU   A CD2  1 
ATOM   2630 H H    A LEU   A 1 122 ? 22.334 -10.608 11.640  0.80 16.81 ?  122 LEU   A H    1 
ATOM   2631 H H    B LEU   A 1 122 ? 22.351 -10.626 11.617  0.20 16.81 ?  122 LEU   A H    1 
ATOM   2632 H HA   . LEU   A 1 122 ? 23.639 -8.231  11.578  1.00 16.02 ?  122 LEU   A HA   1 
ATOM   2633 H HB2  . LEU   A 1 122 ? 22.765 -9.306  9.142   1.00 17.83 ?  122 LEU   A HB2  1 
ATOM   2634 H HB3  . LEU   A 1 122 ? 23.705 -8.059  9.344   1.00 17.83 ?  122 LEU   A HB3  1 
ATOM   2635 H HG   . LEU   A 1 122 ? 25.355 -9.787  10.017  1.00 17.58 ?  122 LEU   A HG   1 
ATOM   2636 H HD11 . LEU   A 1 122 ? 25.081 -11.773 8.803   1.00 18.51 ?  122 LEU   A HD11 1 
ATOM   2637 H HD12 . LEU   A 1 122 ? 23.935 -11.612 9.890   1.00 18.51 ?  122 LEU   A HD12 1 
ATOM   2638 H HD13 . LEU   A 1 122 ? 23.633 -11.291 8.363   1.00 18.51 ?  122 LEU   A HD13 1 
ATOM   2639 H HD21 . LEU   A 1 122 ? 26.143 -9.804  7.804   1.00 16.55 ?  122 LEU   A HD21 1 
ATOM   2640 H HD22 . LEU   A 1 122 ? 24.760 -9.184  7.328   1.00 16.55 ?  122 LEU   A HD22 1 
ATOM   2641 H HD23 . LEU   A 1 122 ? 25.730 -8.340  8.262   1.00 16.55 ?  122 LEU   A HD23 1 
ATOM   2642 N N    A LEU   A 1 123 ? 21.592 -6.907  11.172  0.80 13.03 ?  123 LEU   A N    1 
ATOM   2643 N N    B LEU   A 1 123 ? 21.611 -6.906  11.184  0.20 12.96 ?  123 LEU   A N    1 
ATOM   2644 C CA   A LEU   A 1 123 ? 20.429 -6.111  10.778  0.80 12.76 ?  123 LEU   A CA   1 
ATOM   2645 C CA   B LEU   A 1 123 ? 20.432 -6.102  10.881  0.20 12.62 ?  123 LEU   A CA   1 
ATOM   2646 C C    A LEU   A 1 123 ? 20.683 -5.604  9.365   0.80 12.28 ?  123 LEU   A C    1 
ATOM   2647 C C    B LEU   A 1 123 ? 20.653 -5.530  9.486   0.20 11.81 ?  123 LEU   A C    1 
ATOM   2648 O O    A LEU   A 1 123 ? 21.761 -5.068  9.093   0.80 12.23 ?  123 LEU   A O    1 
ATOM   2649 O O    B LEU   A 1 123 ? 21.505 -4.656  9.300   0.20 11.46 ?  123 LEU   A O    1 
ATOM   2650 C CB   A LEU   A 1 123 ? 20.269 -4.921  11.725  0.80 13.39 ?  123 LEU   A CB   1 
ATOM   2651 C CB   B LEU   A 1 123 ? 20.268 -4.985  11.909  0.20 13.28 ?  123 LEU   A CB   1 
ATOM   2652 C CG   A LEU   A 1 123 ? 19.226 -3.851  11.387  0.80 14.31 ?  123 LEU   A CG   1 
ATOM   2653 C CG   B LEU   A 1 123 ? 19.212 -3.931  11.565  0.20 13.82 ?  123 LEU   A CG   1 
ATOM   2654 C CD1  A LEU   A 1 123 ? 17.811 -4.427  11.378  0.80 15.25 ?  123 LEU   A CD1  1 
ATOM   2655 C CD1  B LEU   A 1 123 ? 17.841 -4.576  11.418  0.20 14.02 ?  123 LEU   A CD1  1 
ATOM   2656 C CD2  A LEU   A 1 123 ? 19.326 -2.680  12.373  0.80 14.95 ?  123 LEU   A CD2  1 
ATOM   2657 C CD2  B LEU   A 1 123 ? 19.176 -2.811  12.600  0.20 14.50 ?  123 LEU   A CD2  1 
ATOM   2658 H H    A LEU   A 1 123 ? 22.242 -6.426  11.483  0.80 15.64 ?  123 LEU   A H    1 
ATOM   2659 H H    B LEU   A 1 123 ? 22.286 -6.428  11.438  0.20 15.55 ?  123 LEU   A H    1 
ATOM   2660 H HA   A LEU   A 1 123 ? 19.627 -6.655  10.796  0.80 15.31 ?  123 LEU   A HA   1 
ATOM   2661 H HA   B LEU   A 1 123 ? 19.643 -6.657  10.876  0.20 15.14 ?  123 LEU   A HA   1 
ATOM   2662 H HB2  A LEU   A 1 123 ? 20.033 -5.264  12.600  0.80 16.07 ?  123 LEU   A HB2  1 
ATOM   2663 H HB2  B LEU   A 1 123 ? 20.016 -5.383  12.757  0.20 15.93 ?  123 LEU   A HB2  1 
ATOM   2664 H HB3  A LEU   A 1 123 ? 21.121 -4.467  11.781  0.80 16.07 ?  123 LEU   A HB3  1 
ATOM   2665 H HB3  B LEU   A 1 123 ? 21.117 -4.523  12.008  0.20 15.93 ?  123 LEU   A HB3  1 
ATOM   2666 H HG   A LEU   A 1 123 ? 19.405 -3.492  10.502  0.80 17.17 ?  123 LEU   A HG   1 
ATOM   2667 H HG   B LEU   A 1 123 ? 19.439 -3.526  10.714  0.20 16.59 ?  123 LEU   A HG   1 
ATOM   2668 H HD11 A LEU   A 1 123 ? 17.176 -3.721  11.170  0.80 18.30 ?  123 LEU   A HD11 1 
ATOM   2669 H HD11 B LEU   A 1 123 ? 17.170 -3.878  11.359  0.20 16.82 ?  123 LEU   A HD11 1 
ATOM   2670 H HD12 A LEU   A 1 123 ? 17.759 -5.125  10.707  0.80 18.30 ?  123 LEU   A HD12 1 
ATOM   2671 H HD12 B LEU   A 1 123 ? 17.831 -5.112  10.609  0.20 16.82 ?  123 LEU   A HD12 1 
ATOM   2672 H HD13 A LEU   A 1 123 ? 17.614 -4.796  12.255  0.80 18.30 ?  123 LEU   A HD13 1 
ATOM   2673 H HD13 B LEU   A 1 123 ? 17.670 -5.136  12.191  0.20 16.82 ?  123 LEU   A HD13 1 
ATOM   2674 H HD21 A LEU   A 1 123 ? 18.659 -2.012  12.149  0.80 17.94 ?  123 LEU   A HD21 1 
ATOM   2675 H HD21 B LEU   A 1 123 ? 18.498 -2.165  12.343  0.20 17.39 ?  123 LEU   A HD21 1 
ATOM   2676 H HD22 A LEU   A 1 123 ? 19.163 -3.014  13.274  0.80 17.94 ?  123 LEU   A HD22 1 
ATOM   2677 H HD22 B LEU   A 1 123 ? 18.961 -3.188  13.467  0.20 17.39 ?  123 LEU   A HD22 1 
ATOM   2678 H HD23 A LEU   A 1 123 ? 20.213 -2.295  12.323  0.80 17.94 ?  123 LEU   A HD23 1 
ATOM   2679 H HD23 B LEU   A 1 123 ? 20.046 -2.382  12.631  0.20 17.39 ?  123 LEU   A HD23 1 
ATOM   2680 N N    A ALA   A 1 124 ? 19.705 -5.748  8.467   0.80 11.63 ?  124 ALA   A N    1 
ATOM   2681 N N    B ALA   A 1 124 ? 19.904 -6.027  8.507   0.20 11.32 ?  124 ALA   A N    1 
ATOM   2682 C CA   A ALA   A 1 124 ? 19.985 -5.485  7.063   0.80 11.16 ?  124 ALA   A CA   1 
ATOM   2683 C CA   B ALA   A 1 124 ? 20.179 -5.740  7.110   0.20 11.43 ?  124 ALA   A CA   1 
ATOM   2684 C C    A ALA   A 1 124 ? 18.747 -5.055  6.285   0.80 11.59 ?  124 ALA   A C    1 
ATOM   2685 C C    B ALA   A 1 124 ? 18.968 -5.150  6.402   0.20 11.08 ?  124 ALA   A C    1 
ATOM   2686 O O    A ALA   A 1 124 ? 17.619 -5.449  6.625   0.80 12.23 ?  124 ALA   A O    1 
ATOM   2687 O O    B ALA   A 1 124 ? 17.825 -5.330  6.842   0.20 11.18 ?  124 ALA   A O    1 
ATOM   2688 C CB   A ALA   A 1 124 ? 20.593 -6.719  6.386   0.80 11.41 ?  124 ALA   A CB   1 
ATOM   2689 C CB   B ALA   A 1 124 ? 20.624 -7.011  6.372   0.20 12.13 ?  124 ALA   A CB   1 
ATOM   2690 H H    A ALA   A 1 124 ? 18.892 -5.971  8.643   0.80 13.96 ?  124 ALA   A H    1 
ATOM   2691 H H    B ALA   A 1 124 ? 19.217 -6.539  8.629   0.20 13.58 ?  124 ALA   A H    1 
ATOM   2692 H HA   A ALA   A 1 124 ? 20.653 -4.777  7.020   0.80 13.39 ?  124 ALA   A HA   1 
ATOM   2693 H HA   B ALA   A 1 124 ? 20.899 -5.096  7.065   0.20 13.71 ?  124 ALA   A HA   1 
ATOM   2694 H HB1  A ALA   A 1 124 ? 20.780 -6.511  5.456   0.80 13.69 ?  124 ALA   A HB1  1 
ATOM   2695 H HB1  B ALA   A 1 124 ? 20.809 -6.792  5.443   0.20 14.55 ?  124 ALA   A HB1  1 
ATOM   2696 H HB2  A ALA   A 1 124 ? 21.423 -6.958  6.838   0.80 13.69 ?  124 ALA   A HB2  1 
ATOM   2697 H HB2  B ALA   A 1 124 ? 21.427 -7.360  6.793   0.20 14.55 ?  124 ALA   A HB2  1 
ATOM   2698 H HB3  A ALA   A 1 124 ? 19.966 -7.453  6.444   0.80 13.69 ?  124 ALA   A HB3  1 
ATOM   2699 H HB3  B ALA   A 1 124 ? 19.915 -7.671  6.419   0.20 14.55 ?  124 ALA   A HB3  1 
ATOM   2700 N N    A PRO   A 1 125 ? 18.941 -4.313  5.200   0.80 11.54 ?  125 PRO   A N    1 
ATOM   2701 N N    B PRO   A 1 125 ? 19.189 -4.431  5.295   0.20 10.12 ?  125 PRO   A N    1 
ATOM   2702 C CA   A PRO   A 1 125 ? 17.888 -4.086  4.213   0.80 12.10 ?  125 PRO   A CA   1 
ATOM   2703 C CA   B PRO   A 1 125 ? 18.076 -3.996  4.449   0.20 10.38 ?  125 PRO   A CA   1 
ATOM   2704 C C    A PRO   A 1 125 ? 17.950 -5.163  3.136   0.80 11.87 ?  125 PRO   A C    1 
ATOM   2705 C C    B PRO   A 1 125 ? 17.912 -4.960  3.288   0.20 11.22 ?  125 PRO   A C    1 
ATOM   2706 O O    A PRO   A 1 125 ? 18.914 -5.925  3.038   0.80 12.20 ?  125 PRO   A O    1 
ATOM   2707 O O    B PRO   A 1 125 ? 18.738 -5.862  3.124   0.20 11.20 ?  125 PRO   A O    1 
ATOM   2708 C CB   A PRO   A 1 125 ? 18.320 -2.746  3.603   0.80 12.19 ?  125 PRO   A CB   1 
ATOM   2709 C CB   B PRO   A 1 125 ? 18.554 -2.628  3.956   0.20 10.04 ?  125 PRO   A CB   1 
ATOM   2710 C CG   A PRO   A 1 125 ? 19.817 -2.906  3.514   0.80 12.29 ?  125 PRO   A CG   1 
ATOM   2711 C CG   B PRO   A 1 125 ? 20.048 -2.825  3.795   0.20 10.06 ?  125 PRO   A CG   1 
ATOM   2712 C CD   A PRO   A 1 125 ? 20.189 -3.616  4.819   0.80 11.90 ?  125 PRO   A CD   1 
ATOM   2713 C CD   B PRO   A 1 125 ? 20.471 -3.891  4.807   0.20 9.69  ?  125 PRO   A CD   1 
ATOM   2714 H HA   A PRO   A 1 125 ? 17.004 -4.039  4.618   0.80 14.51 ?  125 PRO   A HA   1 
ATOM   2715 H HA   B PRO   A 1 125 ? 17.250 -3.913  4.956   0.20 12.46 ?  125 PRO   A HA   1 
ATOM   2716 H HB2  A PRO   A 1 125 ? 17.917 -2.636  2.727   0.80 14.62 ?  125 PRO   A HB2  1 
ATOM   2717 H HB2  B PRO   A 1 125 ? 18.134 -2.420  3.105   0.20 12.05 ?  125 PRO   A HB2  1 
ATOM   2718 H HB3  A PRO   A 1 125 ? 18.074 -2.020  4.198   0.80 14.62 ?  125 PRO   A HB3  1 
ATOM   2719 H HB3  B PRO   A 1 125 ? 18.357 -1.948  4.618   0.20 12.05 ?  125 PRO   A HB3  1 
ATOM   2720 H HG2  A PRO   A 1 125 ? 20.050 -3.458  2.745   0.80 14.75 ?  125 PRO   A HG2  1 
ATOM   2721 H HG2  B PRO   A 1 125 ? 20.238 -3.123  2.892   0.20 12.08 ?  125 PRO   A HG2  1 
ATOM   2722 H HG3  A PRO   A 1 125 ? 20.242 -2.037  3.454   0.80 14.75 ?  125 PRO   A HG3  1 
ATOM   2723 H HG3  B PRO   A 1 125 ? 20.503 -1.988  3.977   0.20 12.08 ?  125 PRO   A HG3  1 
ATOM   2724 H HD2  A PRO   A 1 125 ? 20.910 -4.244  4.675   0.80 14.28 ?  125 PRO   A HD2  1 
ATOM   2725 H HD2  B PRO   A 1 125 ? 20.990 -4.587  4.370   0.20 11.63 ?  125 PRO   A HD2  1 
ATOM   2726 H HD3  A PRO   A 1 125 ? 20.423 -2.958  5.501   0.80 14.28 ?  125 PRO   A HD3  1 
ATOM   2727 H HD3  B PRO   A 1 125 ? 20.967 -3.484  5.535   0.20 11.63 ?  125 PRO   A HD3  1 
ATOM   2728 N N    A LEU   A 1 126 ? 16.915 -5.181  2.299   0.80 12.02 ?  126 LEU   A N    1 
ATOM   2729 N N    B LEU   A 1 126 ? 16.879 -4.782  2.468   0.20 11.98 ?  126 LEU   A N    1 
ATOM   2730 C CA   A LEU   A 1 126 ? 16.935 -6.003  1.098   0.80 12.06 ?  126 LEU   A CA   1 
ATOM   2731 C CA   B LEU   A 1 126 ? 16.699 -5.621  1.287   0.20 12.43 ?  126 LEU   A CA   1 
ATOM   2732 C C    A LEU   A 1 126 ? 17.873 -5.392  0.064   0.80 11.94 ?  126 LEU   A C    1 
ATOM   2733 C C    B LEU   A 1 126 ? 17.609 -5.104  0.177   0.20 12.23 ?  126 LEU   A C    1 
ATOM   2734 O O    A LEU   A 1 126 ? 17.656 -4.275  -0.414  0.80 12.98 ?  126 LEU   A O    1 
ATOM   2735 O O    B LEU   A 1 126 ? 17.329 -4.063  -0.426  0.20 12.93 ?  126 LEU   A O    1 
ATOM   2736 C CB   A LEU   A 1 126 ? 15.526 -6.149  0.533   0.80 12.68 ?  126 LEU   A CB   1 
ATOM   2737 C CB   B LEU   A 1 126 ? 15.240 -5.597  0.843   0.20 13.90 ?  126 LEU   A CB   1 
ATOM   2738 C CG   A LEU   A 1 126 ? 14.598 -7.057  1.333   0.80 13.24 ?  126 LEU   A CG   1 
ATOM   2739 C CG   B LEU   A 1 126 ? 14.808 -6.704  -0.120  0.20 15.05 ?  126 LEU   A CG   1 
ATOM   2740 C CD1  A LEU   A 1 126 ? 13.171 -6.917  0.818   0.80 15.03 ?  126 LEU   A CD1  1 
ATOM   2741 C CD1  B LEU   A 1 126 ? 14.969 -8.070  0.521   0.20 15.33 ?  126 LEU   A CD1  1 
ATOM   2742 C CD2  A LEU   A 1 126 ? 15.074 -8.509  1.247   0.80 13.55 ?  126 LEU   A CD2  1 
ATOM   2743 C CD2  B LEU   A 1 126 ? 13.369 -6.488  -0.555  0.20 15.73 ?  126 LEU   A CD2  1 
ATOM   2744 H H    A LEU   A 1 126 ? 16.199 -4.717  2.396   0.80 14.42 ?  126 LEU   A H    1 
ATOM   2745 H H    B LEU   A 1 126 ? 16.266 -4.184  2.581   0.20 14.37 ?  126 LEU   A H    1 
ATOM   2746 H HA   A LEU   A 1 126 ? 17.268 -6.884  1.318   0.80 14.48 ?  126 LEU   A HA   1 
ATOM   2747 H HA   B LEU   A 1 126 ? 16.952 -6.532  1.504   0.20 14.92 ?  126 LEU   A HA   1 
ATOM   2748 H HB2  A LEU   A 1 126 ? 15.112 -5.276  0.500   0.80 15.22 ?  126 LEU   A HB2  1 
ATOM   2749 H HB2  B LEU   A 1 126 ? 14.675 -5.655  1.628   0.20 16.68 ?  126 LEU   A HB2  1 
ATOM   2750 H HB3  A LEU   A 1 126 ? 15.586 -6.517  -0.363  0.80 15.22 ?  126 LEU   A HB3  1 
ATOM   2751 H HB3  B LEU   A 1 126 ? 15.080 -4.755  0.391   0.20 16.68 ?  126 LEU   A HB3  1 
ATOM   2752 H HG   A LEU   A 1 126 ? 14.613 -6.794  2.268   0.80 15.88 ?  126 LEU   A HG   1 
ATOM   2753 H HG   B LEU   A 1 126 ? 15.368 -6.671  -0.912  0.20 18.06 ?  126 LEU   A HG   1 
ATOM   2754 H HD11 A LEU   A 1 126 ? 12.593 -7.504  1.328   0.80 18.04 ?  126 LEU   A HD11 1 
ATOM   2755 H HD11 B LEU   A 1 126 ? 14.509 -8.727  -0.022  0.20 18.39 ?  126 LEU   A HD11 1 
ATOM   2756 H HD12 A LEU   A 1 126 ? 12.893 -5.997  0.923   0.80 18.04 ?  126 LEU   A HD12 1 
ATOM   2757 H HD12 B LEU   A 1 126 ? 15.913 -8.285  0.573   0.20 18.39 ?  126 LEU   A HD12 1 
ATOM   2758 H HD13 A LEU   A 1 126 ? 13.154 -7.167  -0.120  0.80 18.04 ?  126 LEU   A HD13 1 
ATOM   2759 H HD13 B LEU   A 1 126 ? 14.583 -8.046  1.411   0.20 18.39 ?  126 LEU   A HD13 1 
ATOM   2760 H HD21 A LEU   A 1 126 ? 14.393 -9.090  1.622   0.80 16.26 ?  126 LEU   A HD21 1 
ATOM   2761 H HD21 B LEU   A 1 126 ? 13.116 -7.195  -1.170  0.20 18.87 ?  126 LEU   A HD21 1 
ATOM   2762 H HD22 A LEU   A 1 126 ? 15.225 -8.737  0.316   0.80 16.26 ?  126 LEU   A HD22 1 
ATOM   2763 H HD22 B LEU   A 1 126 ? 12.796 -6.510  0.228   0.20 18.87 ?  126 LEU   A HD22 1 
ATOM   2764 H HD23 A LEU   A 1 126 ? 15.900 -8.605  1.748   0.80 16.26 ?  126 LEU   A HD23 1 
ATOM   2765 H HD23 B LEU   A 1 126 ? 13.295 -5.626  -0.994  0.20 18.87 ?  126 LEU   A HD23 1 
ATOM   2766 N N    A LEU   A 1 127 ? 18.915 -6.130  -0.289  0.80 11.36 ?  127 LEU   A N    1 
ATOM   2767 N N    B LEU   A 1 127 ? 18.693 -5.827  -0.103  0.20 11.55 ?  127 LEU   A N    1 
ATOM   2768 C CA   A LEU   A 1 127 ? 19.910 -5.625  -1.221  0.80 11.54 ?  127 LEU   A CA   1 
ATOM   2769 C CA   B LEU   A 1 127 ? 19.668 -5.349  -1.076  0.20 11.58 ?  127 LEU   A CA   1 
ATOM   2770 C C    A LEU   A 1 127 ? 19.303 -5.445  -2.604  0.80 10.87 ?  127 LEU   A C    1 
ATOM   2771 C C    B LEU   A 1 127 ? 19.060 -5.249  -2.475  0.20 11.58 ?  127 LEU   A C    1 
ATOM   2772 O O    A LEU   A 1 127 ? 18.486 -6.250  -3.058  0.80 10.90 ?  127 LEU   A O    1 
ATOM   2773 O O    B LEU   A 1 127 ? 18.180 -6.025  -2.861  0.20 12.00 ?  127 LEU   A O    1 
ATOM   2774 C CB   A LEU   A 1 127 ? 21.097 -6.587  -1.308  0.80 13.07 ?  127 LEU   A CB   1 
ATOM   2775 C CB   B LEU   A 1 127 ? 20.901 -6.259  -1.104  0.20 11.71 ?  127 LEU   A CB   1 
ATOM   2776 C CG   A LEU   A 1 127 ? 21.862 -6.849  -0.013  0.80 13.61 ?  127 LEU   A CG   1 
ATOM   2777 C CG   B LEU   A 1 127 ? 21.793 -6.261  0.146   0.20 11.19 ?  127 LEU   A CG   1 
ATOM   2778 C CD1  A LEU   A 1 127 ? 22.944 -7.877  -0.263  0.80 14.80 ?  127 LEU   A CD1  1 
ATOM   2779 C CD1  B LEU   A 1 127 ? 22.977 -7.212  -0.015  0.20 11.51 ?  127 LEU   A CD1  1 
ATOM   2780 C CD2  A LEU   A 1 127 ? 22.480 -5.576  0.509   0.80 14.62 ?  127 LEU   A CD2  1 
ATOM   2781 C CD2  B LEU   A 1 127 ? 22.279 -4.854  0.483   0.20 10.92 ?  127 LEU   A CD2  1 
ATOM   2782 H H    A LEU   A 1 127 ? 19.071 -6.927  -0.002  0.80 13.63 ?  127 LEU   A H    1 
ATOM   2783 H H    B LEU   A 1 127 ? 18.889 -6.583  0.264   0.20 13.86 ?  127 LEU   A H    1 
ATOM   2784 H HA   A LEU   A 1 127 ? 20.229 -4.764  -0.912  0.80 13.85 ?  127 LEU   A HA   1 
ATOM   2785 H HA   B LEU   A 1 127 ? 19.961 -4.461  -0.810  0.20 13.89 ?  127 LEU   A HA   1 
ATOM   2786 H HB2  A LEU   A 1 127 ? 20.774 -7.437  -1.634  0.80 15.69 ?  127 LEU   A HB2  1 
ATOM   2787 H HB2  B LEU   A 1 127 ? 20.603 -7.170  -1.244  0.20 14.05 ?  127 LEU   A HB2  1 
ATOM   2788 H HB3  A LEU   A 1 127 ? 21.732 -6.218  -1.945  0.80 15.69 ?  127 LEU   A HB3  1 
ATOM   2789 H HB3  B LEU   A 1 127 ? 21.458 -5.986  -1.852  0.20 14.05 ?  127 LEU   A HB3  1 
ATOM   2790 H HG   A LEU   A 1 127 ? 21.252 -7.199  0.659   0.80 16.34 ?  127 LEU   A HG   1 
ATOM   2791 H HG   B LEU   A 1 127 ? 21.270 -6.575  0.897   0.20 13.43 ?  127 LEU   A HG   1 
ATOM   2792 H HD11 A LEU   A 1 127 ? 23.396 -8.070  0.574   0.80 17.76 ?  127 LEU   A HD11 1 
ATOM   2793 H HD11 B LEU   A 1 127 ? 23.513 -7.189  0.795   0.20 13.81 ?  127 LEU   A HD11 1 
ATOM   2794 H HD12 A LEU   A 1 127 ? 22.538 -8.686  -0.614  0.80 17.76 ?  127 LEU   A HD12 1 
ATOM   2795 H HD12 B LEU   A 1 127 ? 22.642 -8.111  -0.162  0.20 13.81 ?  127 LEU   A HD12 1 
ATOM   2796 H HD13 A LEU   A 1 127 ? 23.575 -7.519  -0.906  0.80 17.76 ?  127 LEU   A HD13 1 
ATOM   2797 H HD13 B LEU   A 1 127 ? 23.511 -6.929  -0.773  0.20 13.81 ?  127 LEU   A HD13 1 
ATOM   2798 H HD21 A LEU   A 1 127 ? 23.039 -5.790  1.271   0.80 17.55 ?  127 LEU   A HD21 1 
ATOM   2799 H HD21 B LEU   A 1 127 ? 22.965 -4.912  1.166   0.20 13.10 ?  127 LEU   A HD21 1 
ATOM   2800 H HD22 A LEU   A 1 127 ? 23.019 -5.182  -0.196  0.80 17.55 ?  127 LEU   A HD22 1 
ATOM   2801 H HD22 B LEU   A 1 127 ? 22.641 -4.445  -0.318  0.20 13.10 ?  127 LEU   A HD22 1 
ATOM   2802 H HD23 A LEU   A 1 127 ? 21.776 -4.967  0.769   0.80 17.55 ?  127 LEU   A HD23 1 
ATOM   2803 H HD23 B LEU   A 1 127 ? 21.529 -4.333  0.811   0.20 13.10 ?  127 LEU   A HD23 1 
ATOM   2804 N N    A SER   A 1 128 ? 19.745 -4.396  -3.289  0.80 11.26 ?  128 SER   A N    1 
ATOM   2805 N N    B SER   A 1 128 ? 19.549 -4.263  -3.228  0.20 11.88 ?  128 SER   A N    1 
ATOM   2806 C CA   A SER   A 1 128 ? 19.347 -4.033  -4.640  0.80 11.56 ?  128 SER   A CA   1 
ATOM   2807 C CA   B SER   A 1 128 ? 19.184 -3.977  -4.617  0.20 12.09 ?  128 SER   A CA   1 
ATOM   2808 C C    A SER   A 1 128 ? 17.889 -3.591  -4.747  0.80 11.27 ?  128 SER   A C    1 
ATOM   2809 C C    B SER   A 1 128 ? 17.724 -3.591  -4.839  0.20 12.09 ?  128 SER   A C    1 
ATOM   2810 O O    A SER   A 1 128 ? 17.455 -3.270  -5.849  0.80 12.67 ?  128 SER   A O    1 
ATOM   2811 O O    B SER   A 1 128 ? 17.319 -3.374  -5.985  0.20 12.85 ?  128 SER   A O    1 
ATOM   2812 C CB   A SER   A 1 128 ? 19.693 -5.111  -5.682  0.80 11.95 ?  128 SER   A CB   1 
ATOM   2813 C CB   B SER   A 1 128 ? 19.584 -5.107  -5.575  0.20 12.16 ?  128 SER   A CB   1 
ATOM   2814 O OG   A SER   A 1 128 ? 21.104 -5.335  -5.714  0.80 12.83 ?  128 SER   A OG   1 
ATOM   2815 O OG   B SER   A 1 128 ? 20.996 -5.228  -5.646  0.20 12.25 ?  128 SER   A OG   1 
ATOM   2816 H H    A SER   A 1 128 ? 20.333 -3.851  -2.971  0.80 13.51 ?  128 SER   A H    1 
ATOM   2817 H H    B SER   A 1 128 ? 20.135 -3.716  -2.927  0.20 14.26 ?  128 SER   A H    1 
ATOM   2818 H HA   A SER   A 1 128 ? 19.869 -3.260  -4.884  0.80 13.87 ?  128 SER   A HA   1 
ATOM   2819 H HA   B SER   A 1 128 ? 19.719 -3.215  -4.874  0.20 14.51 ?  128 SER   A HA   1 
ATOM   2820 H HB2  A SER   A 1 128 ? 19.236 -5.935  -5.452  0.80 14.34 ?  128 SER   A HB2  1 
ATOM   2821 H HB2  B SER   A 1 128 ? 19.206 -5.943  -5.273  0.20 14.59 ?  128 SER   A HB2  1 
ATOM   2822 H HB3  A SER   A 1 128 ? 19.394 -4.804  -6.559  0.80 14.34 ?  128 SER   A HB3  1 
ATOM   2823 H HB3  B SER   A 1 128 ? 19.235 -4.893  -6.467  0.20 14.59 ?  128 SER   A HB3  1 
ATOM   2824 H HG   A SER   A 1 128 ? 21.494 -4.618  -5.909  0.80 15.39 ?  128 SER   A HG   1 
ATOM   2825 H HG   B SER   A 1 128 ? 21.331 -4.511  -5.932  0.20 14.71 ?  128 SER   A HG   1 
ATOM   2826 N N    A ALA   A 1 129 ? 17.148 -3.520  -3.638  0.80 12.42 ?  129 ALA   A N    1 
ATOM   2827 N N    B ALA   A 1 129 ? 16.927 -3.489  -3.777  0.20 12.24 ?  129 ALA   A N    1 
ATOM   2828 C CA   A ALA   A 1 129 ? 15.771 -3.038  -3.635  0.80 13.26 ?  129 ALA   A CA   1 
ATOM   2829 C CA   B ALA   A 1 129 ? 15.565 -3.004  -3.920  0.20 12.50 ?  129 ALA   A CA   1 
ATOM   2830 C C    A ALA   A 1 129 ? 15.755 -1.508  -3.593  0.80 12.83 ?  129 ALA   A C    1 
ATOM   2831 C C    B ALA   A 1 129 ? 15.547 -1.477  -3.858  0.20 13.06 ?  129 ALA   A C    1 
ATOM   2832 O O    A ALA   A 1 129 ? 16.795 -0.844  -3.671  0.80 13.37 ?  129 ALA   A O    1 
ATOM   2833 O O    B ALA   A 1 129 ? 16.587 -0.817  -3.773  0.20 12.97 ?  129 ALA   A O    1 
ATOM   2834 C CB   A ALA   A 1 129 ? 14.993 -3.654  -2.470  0.80 14.40 ?  129 ALA   A CB   1 
ATOM   2835 C CB   B ALA   A 1 129 ? 14.659 -3.617  -2.853  0.20 12.51 ?  129 ALA   A CB   1 
ATOM   2836 H H    A ALA   A 1 129 ? 17.427 -3.763  -2.858  0.80 14.90 ?  129 ALA   A H    1 
ATOM   2837 H H    B ALA   A 1 129 ? 17.142 -3.697  -2.971  0.20 14.69 ?  129 ALA   A H    1 
ATOM   2838 H HA   A ALA   A 1 129 ? 15.343 -3.312  -4.456  0.80 15.91 ?  129 ALA   A HA   1 
ATOM   2839 H HA   B ALA   A 1 129 ? 15.227 -3.273  -4.789  0.20 15.00 ?  129 ALA   A HA   1 
ATOM   2840 H HB1  A ALA   A 1 129 ? 14.078 -3.326  -2.495  0.80 17.28 ?  129 ALA   A HB1  1 
ATOM   2841 H HB1  B ALA   A 1 129 ? 13.754 -3.287  -2.982  0.20 15.01 ?  129 ALA   A HB1  1 
ATOM   2842 H HB2  A ALA   A 1 129 ? 15.004 -4.615  -2.553  0.80 17.28 ?  129 ALA   A HB2  1 
ATOM   2843 H HB2  B ALA   A 1 129 ? 14.675 -4.581  -2.942  0.20 15.01 ?  129 ALA   A HB2  1 
ATOM   2844 H HB3  A ALA   A 1 129 ? 15.412 -3.386  -1.633  0.80 17.28 ?  129 ALA   A HB3  1 
ATOM   2845 H HB3  B ALA   A 1 129 ? 14.983 -3.357  -1.977  0.20 15.01 ?  129 ALA   A HB3  1 
ATOM   2846 N N    A GLY   A 1 130 ? 14.557 -0.940  -3.475  0.80 13.30 ?  130 GLY   A N    1 
ATOM   2847 N N    B GLY   A 1 130 ? 14.347 -0.906  -3.911  0.20 13.67 ?  130 GLY   A N    1 
ATOM   2848 C CA   A GLY   A 1 130 ? 14.427 0.506   -3.431  0.80 13.57 ?  130 GLY   A CA   1 
ATOM   2849 C CA   B GLY   A 1 130 ? 14.223 0.541   -3.846  0.20 14.22 ?  130 GLY   A CA   1 
ATOM   2850 C C    A GLY   A 1 130 ? 15.040 1.138   -4.663  0.80 13.03 ?  130 GLY   A C    1 
ATOM   2851 C C    B GLY   A 1 130 ? 14.852 1.206   -5.057  0.20 14.61 ?  130 GLY   A C    1 
ATOM   2852 O O    A GLY   A 1 130 ? 14.809 0.691   -5.792  0.80 13.56 ?  130 GLY   A O    1 
ATOM   2853 O O    B GLY   A 1 130 ? 14.716 0.739   -6.194  0.20 14.68 ?  130 GLY   A O    1 
ATOM   2854 H H    A GLY   A 1 130 ? 13.812 -1.377  -3.419  0.80 15.96 ?  130 GLY   A H    1 
ATOM   2855 H H    B GLY   A 1 130 ? 13.603 -1.330  -3.984  0.20 16.41 ?  130 GLY   A H    1 
ATOM   2856 H HA2  A GLY   A 1 130 ? 13.486 0.746   -3.389  0.80 16.29 ?  130 GLY   A HA2  1 
ATOM   2857 H HA2  B GLY   A 1 130 ? 13.283 0.782   -3.799  0.20 17.06 ?  130 GLY   A HA2  1 
ATOM   2858 H HA3  A GLY   A 1 130 ? 14.875 0.852   -2.650  0.80 16.29 ?  130 GLY   A HA3  1 
ATOM   2859 H HA3  B GLY   A 1 130 ? 14.667 0.870   -3.053  0.20 17.06 ?  130 GLY   A HA3  1 
ATOM   2860 N N    A ILE   A 1 131 ? 15.837 2.191   -4.446  0.80 13.74 ?  131 ILE   A N    1 
ATOM   2861 N N    B ILE   A 1 131 ? 15.562 2.311   -4.811  0.20 14.70 ?  131 ILE   A N    1 
ATOM   2862 C CA   A ILE   A 1 131 ? 16.418 2.954   -5.548  0.80 13.96 ?  131 ILE   A CA   1 
ATOM   2863 C CA   B ILE   A 1 131 ? 16.165 3.080   -5.895  0.20 15.29 ?  131 ILE   A CA   1 
ATOM   2864 C C    A ILE   A 1 131 ? 17.463 2.189   -6.349  0.80 13.29 ?  131 ILE   A C    1 
ATOM   2865 C C    B ILE   A 1 131 ? 17.247 2.311   -6.638  0.20 15.04 ?  131 ILE   A C    1 
ATOM   2866 O O    A ILE   A 1 131 ? 17.898 2.696   -7.391  0.80 14.32 ?  131 ILE   A O    1 
ATOM   2867 O O    B ILE   A 1 131 ? 17.748 2.795   -7.657  0.20 14.78 ?  131 ILE   A O    1 
ATOM   2868 C CB   A ILE   A 1 131 ? 16.959 4.330   -5.097  0.80 16.25 ?  131 ILE   A CB   1 
ATOM   2869 C CB   B ILE   A 1 131 ? 16.688 4.457   -5.417  0.20 16.05 ?  131 ILE   A CB   1 
ATOM   2870 C CG1  A ILE   A 1 131 ? 18.209 4.192   -4.216  0.80 17.92 ?  131 ILE   A CG1  1 
ATOM   2871 C CG1  B ILE   A 1 131 ? 17.905 4.298   -4.497  0.20 17.14 ?  131 ILE   A CG1  1 
ATOM   2872 C CG2  A ILE   A 1 131 ? 15.874 5.099   -4.370  0.80 17.58 ?  131 ILE   A CG2  1 
ATOM   2873 C CG2  B ILE   A 1 131 ? 15.570 5.237   -4.731  0.20 15.65 ?  131 ILE   A CG2  1 
ATOM   2874 C CD1  A ILE   A 1 131 ? 18.778 5.542   -3.761  0.80 19.35 ?  131 ILE   A CD1  1 
ATOM   2875 C CD1  B ILE   A 1 131 ? 18.863 5.477   -4.540  0.20 17.65 ?  131 ILE   A CD1  1 
ATOM   2876 H H    A ILE   A 1 131 ? 16.038 2.488   -3.667  0.80 16.48 ?  131 ILE   A H    1 
ATOM   2877 H H    B ILE   A 1 131 ? 15.699 2.632   -4.023  0.20 17.64 ?  131 ILE   A H    1 
ATOM   2878 H HA   A ILE   A 1 131 ? 15.701 3.137   -6.172  0.80 16.75 ?  131 ILE   A HA   1 
ATOM   2879 H HA   B ILE   A 1 131 ? 15.480 3.263   -6.545  0.20 18.34 ?  131 ILE   A HA   1 
ATOM   2880 H HB   A ILE   A 1 131 ? 17.200 4.826   -5.893  0.80 19.51 ?  131 ILE   A HB   1 
ATOM   2881 H HB   B ILE   A 1 131 ? 16.964 4.962   -6.198  0.20 19.27 ?  131 ILE   A HB   1 
ATOM   2882 H HG12 A ILE   A 1 131 ? 17.980 3.678   -3.427  0.80 21.50 ?  131 ILE   A HG12 1 
ATOM   2883 H HG12 B ILE   A 1 131 ? 17.591 4.209   -3.586  0.20 20.57 ?  131 ILE   A HG12 1 
ATOM   2884 H HG13 A ILE   A 1 131 ? 18.900 3.732   -4.720  0.80 21.50 ?  131 ILE   A HG13 1 
ATOM   2885 H HG13 B ILE   A 1 131 ? 18.408 3.508   -4.745  0.20 20.57 ?  131 ILE   A HG13 1 
ATOM   2886 H HG21 A ILE   A 1 131 ? 16.147 6.024   -4.285  0.80 21.10 ?  131 ILE   A HG21 1 
ATOM   2887 H HG21 B ILE   A 1 131 ? 15.909 6.108   -4.468  0.20 18.78 ?  131 ILE   A HG21 1 
ATOM   2888 H HG22 A ILE   A 1 131 ? 15.052 5.042   -4.882  0.80 21.10 ?  131 ILE   A HG22 1 
ATOM   2889 H HG22 B ILE   A 1 131 ? 14.833 5.345   -5.352  0.20 18.78 ?  131 ILE   A HG22 1 
ATOM   2890 H HG23 A ILE   A 1 131 ? 15.743 4.705   -3.493  0.80 21.10 ?  131 ILE   A HG23 1 
ATOM   2891 H HG23 B ILE   A 1 131 ? 15.275 4.748   -3.948  0.20 18.78 ?  131 ILE   A HG23 1 
ATOM   2892 H HD11 A ILE   A 1 131 ? 19.639 5.397   -3.339  0.80 23.22 ?  131 ILE   A HD11 1 
ATOM   2893 H HD11 B ILE   A 1 131 ? 19.608 5.297   -3.944  0.20 21.18 ?  131 ILE   A HD11 1 
ATOM   2894 H HD12 A ILE   A 1 131 ? 18.883 6.119   -4.535  0.80 23.22 ?  131 ILE   A HD12 1 
ATOM   2895 H HD12 B ILE   A 1 131 ? 19.186 5.590   -5.448  0.20 21.18 ?  131 ILE   A HD12 1 
ATOM   2896 H HD13 A ILE   A 1 131 ? 18.165 5.949   -3.128  0.80 23.22 ?  131 ILE   A HD13 1 
ATOM   2897 H HD13 B ILE   A 1 131 ? 18.394 6.275   -4.253  0.20 21.18 ?  131 ILE   A HD13 1 
ATOM   2898 N N    A PHE   A 1 132 ? 17.885 0.990   -5.910  0.80 12.89 ?  132 PHE   A N    1 
ATOM   2899 N N    B PHE   A 1 132 ? 17.625 1.126   -6.155  0.20 15.29 ?  132 PHE   A N    1 
ATOM   2900 C CA   A PHE   A 1 132 ? 18.750 0.160   -6.746  0.80 13.12 ?  132 PHE   A CA   1 
ATOM   2901 C CA   B PHE   A 1 132 ? 18.612 0.324   -6.863  0.20 15.16 ?  132 PHE   A CA   1 
ATOM   2902 C C    A PHE   A 1 132 ? 17.978 -0.589  -7.834  0.80 13.87 ?  132 PHE   A C    1 
ATOM   2903 C C    B PHE   A 1 132 ? 18.033 -0.372  -8.091  0.20 15.45 ?  132 PHE   A C    1 
ATOM   2904 O O    A PHE   A 1 132 ? 18.602 -1.221  -8.694  0.80 14.11 ?  132 PHE   A O    1 
ATOM   2905 O O    B PHE   A 1 132 ? 18.795 -0.732  -8.994  0.20 15.83 ?  132 PHE   A O    1 
ATOM   2906 C CB   A PHE   A 1 132 ? 19.582 -0.816  -5.900  0.80 12.30 ?  132 PHE   A CB   1 
ATOM   2907 C CB   B PHE   A 1 132 ? 19.243 -0.697  -5.916  0.20 14.70 ?  132 PHE   A CB   1 
ATOM   2908 C CG   A PHE   A 1 132 ? 20.802 -0.198  -5.227  0.80 11.84 ?  132 PHE   A CG   1 
ATOM   2909 C CG   B PHE   A 1 132 ? 20.445 -0.180  -5.173  0.20 14.41 ?  132 PHE   A CG   1 
ATOM   2910 C CD1  A PHE   A 1 132 ? 20.682 0.852   -4.334  0.80 13.20 ?  132 PHE   A CD1  1 
ATOM   2911 C CD1  B PHE   A 1 132 ? 20.306 0.748   -4.154  0.20 14.39 ?  132 PHE   A CD1  1 
ATOM   2912 C CD2  A PHE   A 1 132 ? 22.061 -0.740  -5.444  0.80 12.54 ?  132 PHE   A CD2  1 
ATOM   2913 C CD2  B PHE   A 1 132 ? 21.712 -0.644  -5.482  0.20 14.21 ?  132 PHE   A CD2  1 
ATOM   2914 C CE1  A PHE   A 1 132 ? 21.810 1.381   -3.707  0.80 13.60 ?  132 PHE   A CE1  1 
ATOM   2915 C CE1  B PHE   A 1 132 ? 21.414 1.213   -3.466  0.20 14.45 ?  132 PHE   A CE1  1 
ATOM   2916 C CE2  A PHE   A 1 132 ? 23.182 -0.224  -4.821  0.80 13.55 ?  132 PHE   A CE2  1 
ATOM   2917 C CE2  B PHE   A 1 132 ? 22.821 -0.186  -4.798  0.20 14.32 ?  132 PHE   A CE2  1 
ATOM   2918 C CZ   A PHE   A 1 132 ? 23.055 0.837   -3.950  0.80 13.62 ?  132 PHE   A CZ   1 
ATOM   2919 C CZ   B PHE   A 1 132 ? 22.671 0.746   -3.789  0.20 14.23 ?  132 PHE   A CZ   1 
ATOM   2920 H H    A PHE   A 1 132 ? 17.689 0.643   -5.142  0.80 15.47 ?  132 PHE   A H    1 
ATOM   2921 H H    B PHE   A 1 132 ? 17.330 0.774   -5.425  0.20 18.34 ?  132 PHE   A H    1 
ATOM   2922 H HA   A PHE   A 1 132 ? 19.378 0.743   -7.191  0.80 15.74 ?  132 PHE   A HA   1 
ATOM   2923 H HA   B PHE   A 1 132 ? 19.318 0.915   -7.166  0.20 18.20 ?  132 PHE   A HA   1 
ATOM   2924 H HB2  A PHE   A 1 132 ? 19.019 -1.183  -5.200  0.80 14.77 ?  132 PHE   A HB2  1 
ATOM   2925 H HB2  B PHE   A 1 132 ? 18.583 -0.964  -5.259  0.20 17.64 ?  132 PHE   A HB2  1 
ATOM   2926 H HB3  A PHE   A 1 132 ? 19.895 -1.540  -6.473  0.80 14.77 ?  132 PHE   A HB3  1 
ATOM   2927 H HB3  B PHE   A 1 132 ? 19.524 -1.464  -6.434  0.20 17.64 ?  132 PHE   A HB3  1 
ATOM   2928 H HD1  A PHE   A 1 132 ? 19.845 1.213   -4.166  0.80 15.84 ?  132 PHE   A HD1  1 
ATOM   2929 H HD1  B PHE   A 1 132 ? 19.461 1.068   -3.933  0.20 17.27 ?  132 PHE   A HD1  1 
ATOM   2930 H HD2  A PHE   A 1 132 ? 22.157 -1.465  -6.032  0.80 15.05 ?  132 PHE   A HD2  1 
ATOM   2931 H HD2  B PHE   A 1 132 ? 21.818 -1.271  -6.161  0.20 17.05 ?  132 PHE   A HD2  1 
ATOM   2932 H HE1  A PHE   A 1 132 ? 21.719 2.096   -3.117  0.80 16.32 ?  132 PHE   A HE1  1 
ATOM   2933 H HE1  B PHE   A 1 132 ? 21.310 1.840   -2.785  0.20 17.35 ?  132 PHE   A HE1  1 
ATOM   2934 H HE2  A PHE   A 1 132 ? 24.023 -0.594  -4.992  0.80 16.26 ?  132 PHE   A HE2  1 
ATOM   2935 H HE2  B PHE   A 1 132 ? 23.666 -0.504  -5.019  0.20 17.18 ?  132 PHE   A HE2  1 
ATOM   2936 H HZ   A PHE   A 1 132 ? 23.810 1.194   -3.532  0.80 16.34 ?  132 PHE   A HZ   1 
ATOM   2937 H HZ   B PHE   A 1 132 ? 23.415 1.056   -3.326  0.20 17.08 ?  132 PHE   A HZ   1 
ATOM   2938 N N    A GLY   A 1 133 ? 16.644 -0.543  -7.819  0.80 13.89 ?  133 GLY   A N    1 
ATOM   2939 N N    B GLY   A 1 133 ? 16.715 -0.581  -8.142  0.20 15.12 ?  133 GLY   A N    1 
ATOM   2940 C CA   A GLY   A 1 133 ? 15.844 -0.912  -8.976  0.80 14.35 ?  133 GLY   A CA   1 
ATOM   2941 C CA   B GLY   A 1 133 ? 16.027 -0.943  -9.365  0.20 14.92 ?  133 GLY   A CA   1 
ATOM   2942 C C    A GLY   A 1 133 ? 15.554 -2.383  -9.194  0.80 14.95 ?  133 GLY   A C    1 
ATOM   2943 C C    B GLY   A 1 133 ? 15.518 -2.370  -9.437  0.20 15.14 ?  133 GLY   A C    1 
ATOM   2944 O O    A GLY   A 1 133 ? 14.959 -2.715  -10.225 0.80 16.54 ?  133 GLY   A O    1 
ATOM   2945 O O    B GLY   A 1 133 ? 14.612 -2.643  -10.238 0.20 15.16 ?  133 GLY   A O    1 
ATOM   2946 H H    A GLY   A 1 133 ? 16.174 -0.292  -7.142  0.80 16.67 ?  133 GLY   A H    1 
ATOM   2947 H H    B GLY   A 1 133 ? 16.193 -0.513  -7.460  0.20 18.15 ?  133 GLY   A H    1 
ATOM   2948 H HA2  A GLY   A 1 133 ? 14.982 -0.461  -8.911  0.80 17.22 ?  133 GLY   A HA2  1 
ATOM   2949 H HA2  B GLY   A 1 133 ? 15.263 -0.361  -9.476  0.20 17.91 ?  133 GLY   A HA2  1 
ATOM   2950 H HA3  A GLY   A 1 133 ? 16.281 -0.583  -9.775  0.80 17.22 ?  133 GLY   A HA3  1 
ATOM   2951 H HA3  B GLY   A 1 133 ? 16.624 -0.790  -10.115 0.20 17.91 ?  133 GLY   A HA3  1 
ATOM   2952 N N    A ALA   A 1 134 ? 15.940 -3.275  -8.283  0.80 14.40 ?  134 ALA   A N    1 
ATOM   2953 N N    B ALA   A 1 134 ? 16.051 -3.282  -8.630  0.20 15.29 ?  134 ALA   A N    1 
ATOM   2954 C CA   A ALA   A 1 134 ? 15.603 -4.684  -8.435  0.80 14.43 ?  134 ALA   A CA   1 
ATOM   2955 C CA   B ALA   A 1 134 ? 15.742 -4.694  -8.801  0.20 15.50 ?  134 ALA   A CA   1 
ATOM   2956 C C    A ALA   A 1 134 ? 14.254 -4.988  -7.788  0.80 15.09 ?  134 ALA   A C    1 
ATOM   2957 C C    B ALA   A 1 134 ? 14.377 -5.037  -8.208  0.20 15.37 ?  134 ALA   A C    1 
ATOM   2958 O O    A ALA   A 1 134 ? 13.737 -4.216  -6.975  0.80 16.29 ?  134 ALA   A O    1 
ATOM   2959 O O    B ALA   A 1 134 ? 13.763 -4.251  -7.481  0.20 15.38 ?  134 ALA   A O    1 
ATOM   2960 C CB   A ALA   A 1 134 ? 16.679 -5.574  -7.815  0.80 15.43 ?  134 ALA   A CB   1 
ATOM   2961 C CB   B ALA   A 1 134 ? 16.828 -5.561  -8.167  0.20 15.92 ?  134 ALA   A CB   1 
ATOM   2962 H H    A ALA   A 1 134 ? 16.402 -3.083  -7.580  0.80 17.28 ?  134 ALA   A H    1 
ATOM   2963 H H    B ALA   A 1 134 ? 16.584 -3.107  -7.979  0.20 18.34 ?  134 ALA   A H    1 
ATOM   2964 H HA   A ALA   A 1 134 ? 15.549 -4.891  -9.382  0.80 17.31 ?  134 ALA   A HA   1 
ATOM   2965 H HA   B ALA   A 1 134 ? 15.712 -4.895  -9.747  0.20 18.61 ?  134 ALA   A HA   1 
ATOM   2966 H HB1  A ALA   A 1 134 ? 16.441 -6.499  -7.965  0.80 18.51 ?  134 ALA   A HB1  1 
ATOM   2967 H HB1  B ALA   A 1 134 ? 16.613 -6.494  -8.321  0.20 19.10 ?  134 ALA   A HB1  1 
ATOM   2968 H HB2  A ALA   A 1 134 ? 17.532 -5.378  -8.239  0.80 18.51 ?  134 ALA   A HB2  1 
ATOM   2969 H HB2  B ALA   A 1 134 ? 17.680 -5.344  -8.577  0.20 19.10 ?  134 ALA   A HB2  1 
ATOM   2970 H HB3  A ALA   A 1 134 ? 16.732 -5.389  -6.867  0.80 18.51 ?  134 ALA   A HB3  1 
ATOM   2971 H HB3  B ALA   A 1 134 ? 16.862 -5.380  -7.216  0.20 19.10 ?  134 ALA   A HB3  1 
ATOM   2972 N N    A ASP   A 1 135 ? 13.690 -6.134  -8.164  0.80 15.59 ?  135 ASP   A N    1 
ATOM   2973 N N    B ASP   A 1 135 ? 13.907 -6.240  -8.532  0.20 15.46 ?  135 ASP   A N    1 
ATOM   2974 C CA   A ASP   A 1 135 ? 12.427 -6.603  -7.597  0.80 16.15 ?  135 ASP   A CA   1 
ATOM   2975 C CA   B ASP   A 1 135 ? 12.620 -6.715  -8.037  0.20 15.79 ?  135 ASP   A CA   1 
ATOM   2976 C C    A ASP   A 1 135 ? 12.661 -7.052  -6.159  0.80 15.09 ?  135 ASP   A C    1 
ATOM   2977 C C    B ASP   A 1 135 ? 12.763 -7.158  -6.587  0.20 14.86 ?  135 ASP   A C    1 
ATOM   2978 O O    A ASP   A 1 135 ? 13.448 -7.983  -5.931  0.80 15.02 ?  135 ASP   A O    1 
ATOM   2979 O O    B ASP   A 1 135 ? 13.563 -8.056  -6.300  0.20 14.71 ?  135 ASP   A O    1 
ATOM   2980 C CB   A ASP   A 1 135 ? 11.924 -7.770  -8.444  0.80 18.86 ?  135 ASP   A CB   1 
ATOM   2981 C CB   B ASP   A 1 135 ? 12.124 -7.879  -8.886  0.20 17.34 ?  135 ASP   A CB   1 
ATOM   2982 C CG   A ASP   A 1 135 ? 10.600 -8.356  -7.952  0.80 21.63 ?  135 ASP   A CG   1 
ATOM   2983 C CG   B ASP   A 1 135 ? 10.860 -8.516  -8.332  0.20 18.53 ?  135 ASP   A CG   1 
ATOM   2984 O OD1  A ASP   A 1 135 ? 10.082 -7.930  -6.899  0.80 21.62 ?  135 ASP   A OD1  1 
ATOM   2985 O OD1  B ASP   A 1 135 ? 9.831  -7.816  -8.212  0.20 18.98 ?  135 ASP   A OD1  1 
ATOM   2986 O OD2  A ASP   A 1 135 ? 10.071 -9.248  -8.652  0.80 24.87 -1 135 ASP   A OD2  1 
ATOM   2987 O OD2  B ASP   A 1 135 ? 10.896 -9.725  -8.023  0.20 18.89 -1 135 ASP   A OD2  1 
ATOM   2988 H H    A ASP   A 1 135 ? 14.031 -6.667  -8.748  0.80 18.71 ?  135 ASP   A H    1 
ATOM   2989 H H    B ASP   A 1 135 ? 14.319 -6.801  -9.037  0.20 18.55 ?  135 ASP   A H    1 
ATOM   2990 H HA   A ASP   A 1 135 ? 11.775 -5.884  -7.626  0.80 19.39 ?  135 ASP   A HA   1 
ATOM   2991 H HA   B ASP   A 1 135 ? 11.977 -5.997  -8.098  0.20 18.95 ?  135 ASP   A HA   1 
ATOM   2992 H HB2  A ASP   A 1 135 ? 11.781 -7.458  -9.350  0.80 22.64 ?  135 ASP   A HB2  1 
ATOM   2993 H HB2  B ASP   A 1 135 ? 11.944 -7.555  -9.783  0.20 20.81 ?  135 ASP   A HB2  1 
ATOM   2994 H HB3  A ASP   A 1 135 ? 12.593 -8.470  -8.435  0.80 22.64 ?  135 ASP   A HB3  1 
ATOM   2995 H HB3  B ASP   A 1 135 ? 12.801 -8.568  -8.907  0.20 20.81 ?  135 ASP   A HB3  1 
ATOM   2996 N N    A PRO   A 1 136 ? 12.036 -6.414  -5.163  0.80 15.17 ?  136 PRO   A N    1 
ATOM   2997 N N    B PRO   A 1 136 ? 12.017 -6.567  -5.651  0.20 14.35 ?  136 PRO   A N    1 
ATOM   2998 C CA   A PRO   A 1 136 ? 12.280 -6.821  -3.768  0.80 14.88 ?  136 PRO   A CA   1 
ATOM   2999 C CA   B PRO   A 1 136 ? 12.205 -6.932  -4.237  0.20 14.12 ?  136 PRO   A CA   1 
ATOM   3000 C C    A PRO   A 1 136 ? 11.855 -8.245  -3.452  0.80 14.18 ?  136 PRO   A C    1 
ATOM   3001 C C    B PRO   A 1 136 ? 11.829 -8.370  -3.927  0.20 13.78 ?  136 PRO   A C    1 
ATOM   3002 O O    A PRO   A 1 136 ? 12.439 -8.860  -2.551  0.80 13.51 ?  136 PRO   A O    1 
ATOM   3003 O O    B PRO   A 1 136 ? 12.487 -9.006  -3.095  0.20 13.67 ?  136 PRO   A O    1 
ATOM   3004 C CB   A PRO   A 1 136 ? 11.493 -5.782  -2.954  0.80 15.87 ?  136 PRO   A CB   1 
ATOM   3005 C CB   B PRO   A 1 136 ? 11.326 -5.914  -3.496  0.20 14.29 ?  136 PRO   A CB   1 
ATOM   3006 C CG   A PRO   A 1 136 ? 10.465 -5.260  -3.905  0.80 17.26 ?  136 PRO   A CG   1 
ATOM   3007 C CG   B PRO   A 1 136 ? 10.291 -5.512  -4.502  0.20 14.27 ?  136 PRO   A CG   1 
ATOM   3008 C CD   A PRO   A 1 136 ? 11.117 -5.265  -5.251  0.80 16.38 ?  136 PRO   A CD   1 
ATOM   3009 C CD   B PRO   A 1 136 ? 10.977 -5.541  -5.832  0.20 14.24 ?  136 PRO   A CD   1 
ATOM   3010 H HA   A PRO   A 1 136 ? 13.225 -6.727  -3.554  0.80 17.85 ?  136 PRO   A HA   1 
ATOM   3011 H HA   B PRO   A 1 136 ? 13.131 -6.793  -3.973  0.20 16.95 ?  136 PRO   A HA   1 
ATOM   3012 H HB2  A PRO   A 1 136 ? 11.072 -6.215  -2.194  0.80 19.04 ?  136 PRO   A HB2  1 
ATOM   3013 H HB2  B PRO   A 1 136 ? 10.914 -6.332  -2.725  0.20 17.15 ?  136 PRO   A HB2  1 
ATOM   3014 H HB3  A PRO   A 1 136 ? 12.087 -5.074  -2.661  0.80 19.04 ?  136 PRO   A HB3  1 
ATOM   3015 H HB3  B PRO   A 1 136 ? 11.862 -5.148  -3.228  0.20 17.15 ?  136 PRO   A HB3  1 
ATOM   3016 H HG2  A PRO   A 1 136 ? 9.691  -5.845  -3.902  0.80 20.71 ?  136 PRO   A HG2  1 
ATOM   3017 H HG2  B PRO   A 1 136 ? 9.560  -6.147  -4.485  0.20 17.13 ?  136 PRO   A HG2  1 
ATOM   3018 H HG3  A PRO   A 1 136 ? 10.216 -4.359  -3.653  0.80 20.71 ?  136 PRO   A HG3  1 
ATOM   3019 H HG3  B PRO   A 1 136 ? 9.976  -4.618  -4.306  0.20 17.13 ?  136 PRO   A HG3  1 
ATOM   3020 H HD2  A PRO   A 1 136 ? 10.456 -5.420  -5.946  0.80 19.66 ?  136 PRO   A HD2  1 
ATOM   3021 H HD2  B PRO   A 1 136 ? 10.363 -5.816  -6.531  0.20 17.09 ?  136 PRO   A HD2  1 
ATOM   3022 H HD3  A PRO   A 1 136 ? 11.605 -4.439  -5.401  0.80 19.66 ?  136 PRO   A HD3  1 
ATOM   3023 H HD3  B PRO   A 1 136 ? 11.386 -4.684  -6.032  0.20 17.09 ?  136 PRO   A HD3  1 
ATOM   3024 N N    A ILE   A 1 137 ? 10.842 -8.779  -4.140  0.80 14.46 ?  137 ILE   A N    1 
ATOM   3025 N N    B ILE   A 1 137 ? 10.787 -8.905  -4.571  0.20 13.85 ?  137 ILE   A N    1 
ATOM   3026 C CA   A ILE   A 1 137 ? 10.459 -10.173 -3.925  0.80 14.63 ?  137 ILE   A CA   1 
ATOM   3027 C CA   B ILE   A 1 137 ? 10.445 -10.312 -4.380  0.20 14.25 ?  137 ILE   A CA   1 
ATOM   3028 C C    A ILE   A 1 137 ? 11.609 -11.092 -4.314  0.80 14.38 ?  137 ILE   A C    1 
ATOM   3029 C C    B ILE   A 1 137 ? 11.645 -11.191 -4.702  0.20 14.47 ?  137 ILE   A C    1 
ATOM   3030 O O    A ILE   A 1 137 ? 11.925 -12.059 -3.607  0.80 14.41 ?  137 ILE   A O    1 
ATOM   3031 O O    B ILE   A 1 137 ? 11.888 -12.208 -4.041  0.20 14.67 ?  137 ILE   A O    1 
ATOM   3032 C CB   A ILE   A 1 137 ? 9.165  -10.498 -4.698  0.80 16.57 ?  137 ILE   A CB   1 
ATOM   3033 C CB   B ILE   A 1 137 ? 9.210  -10.684 -5.223  0.20 14.52 ?  137 ILE   A CB   1 
ATOM   3034 C CG1  A ILE   A 1 137 ? 8.005  -9.602  -4.238  0.80 18.53 ?  137 ILE   A CG1  1 
ATOM   3035 C CG1  B ILE   A 1 137 ? 7.969  -9.964  -4.689  0.20 14.96 ?  137 ILE   A CG1  1 
ATOM   3036 C CG2  A ILE   A 1 137 ? 8.804  -11.974 -4.537  0.80 17.12 ?  137 ILE   A CG2  1 
ATOM   3037 C CG2  B ILE   A 1 137 ? 8.990  -12.193 -5.227  0.20 14.13 ?  137 ILE   A CG2  1 
ATOM   3038 C CD1  A ILE   A 1 137 ? 6.725  -9.783  -5.047  0.80 20.22 ?  137 ILE   A CD1  1 
ATOM   3039 C CD1  B ILE   A 1 137 ? 6.695  -10.293 -5.438  0.20 15.45 ?  137 ILE   A CD1  1 
ATOM   3040 H H    A ILE   A 1 137 ? 10.371 -8.362  -4.733  0.80 17.35 ?  137 ILE   A H    1 
ATOM   3041 H H    B ILE   A 1 137 ? 10.275 -8.483  -5.116  0.20 16.62 ?  137 ILE   A H    1 
ATOM   3042 H HA   A ILE   A 1 137 ? 10.282 -10.304 -2.986  0.80 17.56 ?  137 ILE   A HA   1 
ATOM   3043 H HA   B ILE   A 1 137 ? 10.220 -10.456 -3.450  0.20 17.10 ?  137 ILE   A HA   1 
ATOM   3044 H HB   A ILE   A 1 137 ? 9.316  -10.328 -5.639  0.80 19.88 ?  137 ILE   A HB   1 
ATOM   3045 H HB   B ILE   A 1 137 ? 9.362  -10.395 -6.135  0.20 17.43 ?  137 ILE   A HB   1 
ATOM   3046 H HG12 A ILE   A 1 137 ? 7.802  -9.800  -3.311  0.80 22.23 ?  137 ILE   A HG12 1 
ATOM   3047 H HG12 B ILE   A 1 137 ? 7.841  -10.213 -3.760  0.20 17.95 ?  137 ILE   A HG12 1 
ATOM   3048 H HG13 A ILE   A 1 137 ? 8.275  -8.672  -4.323  0.80 22.23 ?  137 ILE   A HG13 1 
ATOM   3049 H HG13 B ILE   A 1 137 ? 8.114  -9.007  -4.754  0.20 17.95 ?  137 ILE   A HG13 1 
ATOM   3050 H HG21 A ILE   A 1 137 ? 7.926  -12.142 -4.916  0.80 20.55 ?  137 ILE   A HG21 1 
ATOM   3051 H HG21 B ILE   A 1 137 ? 8.171  -12.398 -5.703  0.20 16.96 ?  137 ILE   A HG21 1 
ATOM   3052 H HG22 A ILE   A 1 137 ? 9.462  -12.511 -5.000  0.80 20.55 ?  137 ILE   A HG22 1 
ATOM   3053 H HG22 B ILE   A 1 137 ? 9.733  -12.624 -5.672  0.20 16.96 ?  137 ILE   A HG22 1 
ATOM   3054 H HG23 A ILE   A 1 137 ? 8.798  -12.193 -3.593  0.80 20.55 ?  137 ILE   A HG23 1 
ATOM   3055 H HG23 B ILE   A 1 137 ? 8.925  -12.502 -4.311  0.20 16.96 ?  137 ILE   A HG23 1 
ATOM   3056 H HD11 A ILE   A 1 137 ? 6.004  -10.036 -4.448  0.80 24.26 ?  137 ILE   A HD11 1 
ATOM   3057 H HD11 B ILE   A 1 137 ? 6.026  -9.626  -5.226  0.20 18.54 ?  137 ILE   A HD11 1 
ATOM   3058 H HD12 A ILE   A 1 137 ? 6.518  -8.949  -5.488  0.80 24.26 ?  137 ILE   A HD12 1 
ATOM   3059 H HD12 B ILE   A 1 137 ? 6.881  -10.286 -6.390  0.20 18.54 ?  137 ILE   A HD12 1 
ATOM   3060 H HD13 A ILE   A 1 137 ? 6.859  -10.477 -5.714  0.80 24.26 ?  137 ILE   A HD13 1 
ATOM   3061 H HD13 B ILE   A 1 137 ? 6.387  -11.171 -5.167  0.20 18.54 ?  137 ILE   A HD13 1 
ATOM   3062 N N    A HIS   A 1 138 ? 12.257 -10.794 -5.441  0.80 14.94 ?  138 HIS   A N    1 
ATOM   3063 N N    B HIS   A 1 138 ? 12.414 -10.811 -5.723  0.20 14.75 ?  138 HIS   A N    1 
ATOM   3064 C CA   A HIS   A 1 138 ? 13.427 -11.557 -5.860  0.80 15.05 ?  138 HIS   A CA   1 
ATOM   3065 C CA   B HIS   A 1 138 ? 13.622 -11.557 -6.049  0.20 14.95 ?  138 HIS   A CA   1 
ATOM   3066 C C    A HIS   A 1 138 ? 14.570 -11.416 -4.860  0.80 14.39 ?  138 HIS   A C    1 
ATOM   3067 C C    B HIS   A 1 138 ? 14.684 -11.397 -4.968  0.20 14.34 ?  138 HIS   A C    1 
ATOM   3068 O O    A HIS   A 1 138 ? 15.220 -12.403 -4.493  0.80 15.22 ?  138 HIS   A O    1 
ATOM   3069 O O    B HIS   A 1 138 ? 15.371 -12.366 -4.621  0.20 14.21 ?  138 HIS   A O    1 
ATOM   3070 C CB   A HIS   A 1 138 ? 13.849 -11.103 -7.255  0.80 15.94 ?  138 HIS   A CB   1 
ATOM   3071 C CB   B HIS   A 1 138 ? 14.161 -11.120 -7.409  0.20 15.97 ?  138 HIS   A CB   1 
ATOM   3072 C CG   A HIS   A 1 138 ? 15.127 -11.724 -7.720  0.80 17.06 ?  138 HIS   A CG   1 
ATOM   3073 C CG   B HIS   A 1 138 ? 15.380 -11.872 -7.839  0.20 16.63 ?  138 HIS   A CG   1 
ATOM   3074 N ND1  A HIS   A 1 138 ? 15.258 -13.077 -7.950  0.80 18.52 ?  138 HIS   A ND1  1 
ATOM   3075 N ND1  B HIS   A 1 138 ? 15.396 -13.243 -7.980  0.20 17.21 ?  138 HIS   A ND1  1 
ATOM   3076 C CD2  A HIS   A 1 138 ? 16.341 -11.181 -7.973  0.80 17.02 ?  138 HIS   A CD2  1 
ATOM   3077 C CD2  B HIS   A 1 138 ? 16.627 -11.447 -8.148  0.20 16.79 ?  138 HIS   A CD2  1 
ATOM   3078 C CE1  A HIS   A 1 138 ? 16.493 -13.337 -8.340  0.80 19.01 ?  138 HIS   A CE1  1 
ATOM   3079 C CE1  B HIS   A 1 138 ? 16.599 -13.629 -8.364  0.20 17.52 ?  138 HIS   A CE1  1 
ATOM   3080 N NE2  A HIS   A 1 138 ? 17.172 -12.204 -8.359  0.80 17.96 ?  138 HIS   A NE2  1 
ATOM   3081 N NE2  B HIS   A 1 138 ? 17.366 -12.559 -8.472  0.20 17.17 ?  138 HIS   A NE2  1 
ATOM   3082 H H    A HIS   A 1 138 ? 12.035 -10.156 -5.982  0.80 17.93 ?  138 HIS   A H    1 
ATOM   3083 H H    B HIS   A 1 138 ? 12.252 -10.141 -6.240  0.20 17.70 ?  138 HIS   A H    1 
ATOM   3084 H HA   A HIS   A 1 138 ? 13.189 -12.490 -5.917  0.80 18.06 ?  138 HIS   A HA   1 
ATOM   3085 H HA   B HIS   A 1 138 ? 13.399 -12.497 -6.108  0.20 17.94 ?  138 HIS   A HA   1 
ATOM   3086 H HB2  A HIS   A 1 138 ? 13.154 -11.341 -7.892  0.80 19.13 ?  138 HIS   A HB2  1 
ATOM   3087 H HB2  B HIS   A 1 138 ? 13.472 -11.262 -8.079  0.20 19.17 ?  138 HIS   A HB2  1 
ATOM   3088 H HB3  A HIS   A 1 138 ? 13.972 -10.139 -7.254  0.80 19.13 ?  138 HIS   A HB3  1 
ATOM   3089 H HB3  B HIS   A 1 138 ? 14.391 -10.179 -7.369  0.20 19.17 ?  138 HIS   A HB3  1 
ATOM   3090 H HD1  A HIS   A 1 138 ? 14.630 -13.661 -7.862  0.80 22.22 ?  138 HIS   A HD1  1 
ATOM   3091 H HD2  A HIS   A 1 138 ? 16.568 -10.283 -7.905  0.80 20.42 ?  138 HIS   A HD2  1 
ATOM   3092 H HD2  B HIS   A 1 138 ? 16.926 -10.567 -8.143  0.20 20.15 ?  138 HIS   A HD2  1 
ATOM   3093 H HE1  A HIS   A 1 138 ? 16.828 -14.179 -8.556  0.80 22.81 ?  138 HIS   A HE1  1 
ATOM   3094 H HE1  B HIS   A 1 138 ? 16.861 -14.504 -8.528  0.20 21.03 ?  138 HIS   A HE1  1 
ATOM   3095 H HE2  B HIS   A 1 138 ? 18.192 -12.558 -8.707  0.20 20.60 ?  138 HIS   A HE2  1 
ATOM   3096 N N    . SER   A 1 139 ? 14.840 -10.188 -4.419  1.00 13.93 ?  139 SER   A N    1 
ATOM   3097 C CA   . SER   A 1 139 ? 15.895 -9.982  -3.436  1.00 13.74 ?  139 SER   A CA   1 
ATOM   3098 C C    . SER   A 1 139 ? 15.659 -10.806 -2.177  1.00 13.67 ?  139 SER   A C    1 
ATOM   3099 O O    . SER   A 1 139 ? 16.600 -11.394 -1.628  1.00 13.74 ?  139 SER   A O    1 
ATOM   3100 C CB   . SER   A 1 139 ? 16.031 -8.497  -3.101  1.00 13.41 ?  139 SER   A CB   1 
ATOM   3101 O OG   . SER   A 1 139 ? 17.095 -8.314  -2.183  1.00 14.15 ?  139 SER   A OG   1 
ATOM   3102 H H    A SER   A 1 139 ? 14.435 -9.471  -4.665  0.80 16.71 ?  139 SER   A H    1 
ATOM   3103 H H    B SER   A 1 139 ? 14.365 -9.493  -4.595  0.20 16.71 ?  139 SER   A H    1 
ATOM   3104 H HA   . SER   A 1 139 ? 16.741 -10.267 -3.817  1.00 16.49 ?  139 SER   A HA   1 
ATOM   3105 H HB2  . SER   A 1 139 ? 16.220 -7.994  -3.909  1.00 16.09 ?  139 SER   A HB2  1 
ATOM   3106 H HB3  . SER   A 1 139 ? 15.208 -8.179  -2.694  1.00 16.09 ?  139 SER   A HB3  1 
ATOM   3107 H HG   . SER   A 1 139 ? 17.183 -7.496  -1.987  1.00 16.99 ?  139 SER   A HG   1 
ATOM   3108 N N    . LEU   A 1 140 ? 14.411 -10.869 -1.706  1.00 13.09 ?  140 LEU   A N    1 
ATOM   3109 C CA   . LEU   A 1 140 ? 14.120 -11.672 -0.521  1.00 13.10 ?  140 LEU   A CA   1 
ATOM   3110 C C    . LEU   A 1 140 ? 14.396 -13.151 -0.776  1.00 13.50 ?  140 LEU   A C    1 
ATOM   3111 O O    . LEU   A 1 140 ? 14.939 -13.855 0.089   1.00 14.55 ?  140 LEU   A O    1 
ATOM   3112 C CB   . LEU   A 1 140 ? 12.677 -11.439 -0.080  1.00 13.86 ?  140 LEU   A CB   1 
ATOM   3113 C CG   . LEU   A 1 140 ? 12.215 -12.256 1.127   1.00 14.49 ?  140 LEU   A CG   1 
ATOM   3114 C CD1  . LEU   A 1 140 ? 13.118 -12.077 2.346   1.00 15.15 ?  140 LEU   A CD1  1 
ATOM   3115 C CD2  . LEU   A 1 140 ? 10.749 -11.919 1.460   1.00 15.17 ?  140 LEU   A CD2  1 
ATOM   3116 H H    . LEU   A 1 140 ? 13.736 -10.454 -2.042  1.00 15.71 ?  140 LEU   A H    1 
ATOM   3117 H HA   . LEU   A 1 140 ? 14.697 -11.381 0.201   1.00 15.72 ?  140 LEU   A HA   1 
ATOM   3118 H HB2  . LEU   A 1 140 ? 12.571 -10.502 0.148   1.00 16.63 ?  140 LEU   A HB2  1 
ATOM   3119 H HB3  . LEU   A 1 140 ? 12.091 -11.659 -0.820  1.00 16.63 ?  140 LEU   A HB3  1 
ATOM   3120 H HG   . LEU   A 1 140 ? 12.236 -13.193 0.883   1.00 17.39 ?  140 LEU   A HG   1 
ATOM   3121 H HD11 . LEU   A 1 140 ? 12.735 -12.573 3.092   1.00 18.18 ?  140 LEU   A HD11 1 
ATOM   3122 H HD12 . LEU   A 1 140 ? 13.996 -12.436 2.138   1.00 18.18 ?  140 LEU   A HD12 1 
ATOM   3123 H HD13 . LEU   A 1 140 ? 13.178 -11.142 2.565   1.00 18.18 ?  140 LEU   A HD13 1 
ATOM   3124 H HD21 . LEU   A 1 140 ? 10.469 -12.448 2.227   1.00 18.21 ?  140 LEU   A HD21 1 
ATOM   3125 H HD22 . LEU   A 1 140 ? 10.676 -10.976 1.667   1.00 18.21 ?  140 LEU   A HD22 1 
ATOM   3126 H HD23 . LEU   A 1 140 ? 10.190 -12.135 0.695   1.00 18.21 ?  140 LEU   A HD23 1 
ATOM   3127 N N    . ARG   A 1 141 ? 14.028 -13.637 -1.962  1.00 14.07 ?  141 ARG   A N    1 
ATOM   3128 C CA   . ARG   A 1 141 ? 14.273 -15.034 -2.305  1.00 15.42 ?  141 ARG   A CA   1 
ATOM   3129 C C    . ARG   A 1 141 ? 15.769 -15.334 -2.313  1.00 14.66 ?  141 ARG   A C    1 
ATOM   3130 O O    . ARG   A 1 141 ? 16.219 -16.342 -1.755  1.00 14.89 ?  141 ARG   A O    1 
ATOM   3131 C CB   . ARG   A 1 141 ? 13.664 -15.317 -3.677  1.00 16.88 ?  141 ARG   A CB   1 
ATOM   3132 C CG   . ARG   A 1 141 ? 13.658 -16.768 -4.096  1.00 20.02 ?  141 ARG   A CG   1 
ATOM   3133 C CD   . ARG   A 1 141 ? 12.610 -17.522 -3.338  1.00 23.14 ?  141 ARG   A CD   1 
ATOM   3134 N NE   . ARG   A 1 141 ? 13.205 -18.320 -2.280  1.00 24.42 ?  141 ARG   A NE   1 
ATOM   3135 C CZ   . ARG   A 1 141 ? 12.516 -18.867 -1.286  1.00 24.73 ?  141 ARG   A CZ   1 
ATOM   3136 N NH1  . ARG   A 1 141 ? 11.235 -18.595 -1.101  1.00 23.94 ?  141 ARG   A NH1  1 
ATOM   3137 N NH2  . ARG   A 1 141 ? 13.131 -19.700 -0.452  1.00 25.61 ?  141 ARG   A NH2  1 
ATOM   3138 H H    . ARG   A 1 141 ? 13.638 -13.179 -2.582  1.00 16.89 ?  141 ARG   A H    1 
ATOM   3139 H HA   . ARG   A 1 141 ? 13.847 -15.605 -1.651  1.00 18.51 ?  141 ARG   A HA   1 
ATOM   3140 H HB2  . ARG   A 1 141 ? 12.745 -15.003 -3.678  1.00 20.25 ?  141 ARG   A HB2  1 
ATOM   3141 H HB3  . ARG   A 1 141 ? 14.169 -14.823 -4.342  1.00 20.25 ?  141 ARG   A HB3  1 
ATOM   3142 H HG2  . ARG   A 1 141 ? 13.462 -16.829 -5.045  1.00 24.03 ?  141 ARG   A HG2  1 
ATOM   3143 H HG3  . ARG   A 1 141 ? 14.526 -17.164 -3.907  1.00 24.03 ?  141 ARG   A HG3  1 
ATOM   3144 H HD2  . ARG   A 1 141 ? 11.993 -16.897 -2.924  1.00 27.77 ?  141 ARG   A HD2  1 
ATOM   3145 H HD3  . ARG   A 1 141 ? 12.130 -18.108 -3.947  1.00 27.77 ?  141 ARG   A HD3  1 
ATOM   3146 H HE   . ARG   A 1 141 ? 14.025 -18.554 -2.368  1.00 29.31 ?  141 ARG   A HE   1 
ATOM   3147 H HH11 . ARG   A 1 141 ? 10.817 -18.071 -1.640  1.00 28.72 ?  141 ARG   A HH11 1 
ATOM   3148 H HH12 . ARG   A 1 141 ? 10.806 -18.959 -0.446  1.00 28.72 ?  141 ARG   A HH12 1 
ATOM   3149 H HH21 . ARG   A 1 141 ? 13.963 -19.883 -0.563  1.00 30.73 ?  141 ARG   A HH21 1 
ATOM   3150 H HH22 . ARG   A 1 141 ? 12.697 -20.050 0.205   1.00 30.73 ?  141 ARG   A HH22 1 
ATOM   3151 N N    . VAL   A 1 142 ? 16.560 -14.469 -2.952  1.00 13.96 ?  142 VAL   A N    1 
ATOM   3152 C CA   . VAL   A 1 142 ? 18.009 -14.676 -2.968  1.00 14.12 ?  142 VAL   A CA   1 
ATOM   3153 C C    . VAL   A 1 142 ? 18.568 -14.652 -1.551  1.00 13.23 ?  142 VAL   A C    1 
ATOM   3154 O O    . VAL   A 1 142 ? 19.435 -15.458 -1.197  1.00 13.90 ?  142 VAL   A O    1 
ATOM   3155 C CB   . VAL   A 1 142 ? 18.711 -13.663 -3.889  1.00 14.38 ?  142 VAL   A CB   1 
ATOM   3156 C CG1  . VAL   A 1 142 ? 20.229 -13.859 -3.834  1.00 14.12 ?  142 VAL   A CG1  1 
ATOM   3157 C CG2  . VAL   A 1 142 ? 18.232 -13.814 -5.318  1.00 15.74 ?  142 VAL   A CG2  1 
ATOM   3158 H H    . VAL   A 1 142 ? 16.290 -13.767 -3.380  1.00 16.76 ?  142 VAL   A H    1 
ATOM   3159 H HA   . VAL   A 1 142 ? 18.185 -15.550 -3.329  1.00 16.94 ?  142 VAL   A HA   1 
ATOM   3160 H HB   . VAL   A 1 142 ? 18.518 -12.756 -3.596  1.00 17.25 ?  142 VAL   A HB   1 
ATOM   3161 H HG11 . VAL   A 1 142 ? 20.641 -13.367 -4.563  1.00 16.95 ?  142 VAL   A HG11 1 
ATOM   3162 H HG12 . VAL   A 1 142 ? 20.565 -13.526 -2.985  1.00 16.95 ?  142 VAL   A HG12 1 
ATOM   3163 H HG13 . VAL   A 1 142 ? 20.429 -14.804 -3.921  1.00 16.95 ?  142 VAL   A HG13 1 
ATOM   3164 H HG21 . VAL   A 1 142 ? 18.684 -13.152 -5.871  1.00 18.88 ?  142 VAL   A HG21 1 
ATOM   3165 H HG22 . VAL   A 1 142 ? 18.457 -14.705 -5.626  1.00 18.88 ?  142 VAL   A HG22 1 
ATOM   3166 H HG23 . VAL   A 1 142 ? 17.280 -13.676 -5.345  1.00 18.88 ?  142 VAL   A HG23 1 
ATOM   3167 N N    . CYS   A 1 143 ? 18.088 -13.727 -0.720  1.00 13.10 ?  143 CYS   A N    1 
ATOM   3168 C CA   . CYS   A 1 143 ? 18.545 -13.670 0.663   1.00 13.51 ?  143 CYS   A CA   1 
ATOM   3169 C C    . CYS   A 1 143 ? 18.317 -15.006 1.361   1.00 13.80 ?  143 CYS   A C    1 
ATOM   3170 O O    . CYS   A 1 143 ? 19.233 -15.575 1.959   1.00 13.83 ?  143 CYS   A O    1 
ATOM   3171 C CB   . CYS   A 1 143 ? 17.806 -12.552 1.398   1.00 13.89 ?  143 CYS   A CB   1 
ATOM   3172 S SG   . CYS   A 1 143 ? 18.294 -12.349 3.117   1.00 14.27 ?  143 CYS   A SG   1 
ATOM   3173 H H    . CYS   A 1 143 ? 17.500 -13.133 -0.927  1.00 15.72 ?  143 CYS   A H    1 
ATOM   3174 H HA   . CYS   A 1 143 ? 19.494 -13.479 0.683   1.00 16.21 ?  143 CYS   A HA   1 
ATOM   3175 H HB2  . CYS   A 1 143 ? 17.975 -11.716 0.945   1.00 16.67 ?  143 CYS   A HB2  1 
ATOM   3176 H HB3  . CYS   A 1 143 ? 16.859 -12.749 1.386   1.00 16.67 ?  143 CYS   A HB3  1 
ATOM   3177 H HG   . CYS   A 1 143 ? 17.706 -11.409 3.569   1.00 17.12 ?  143 CYS   A HG   1 
ATOM   3178 N N    . VAL   A 1 144 ? 17.083 -15.509 1.302   1.00 14.29 ?  144 VAL   A N    1 
ATOM   3179 C CA   . VAL   A 1 144 ? 16.727 -16.746 1.986   1.00 16.38 ?  144 VAL   A CA   1 
ATOM   3180 C C    . VAL   A 1 144 ? 17.548 -17.915 1.469   1.00 15.82 ?  144 VAL   A C    1 
ATOM   3181 O O    . VAL   A 1 144 ? 17.916 -18.817 2.235   1.00 16.35 ?  144 VAL   A O    1 
ATOM   3182 C CB   . VAL   A 1 144 ? 15.213 -16.977 1.822   1.00 19.06 ?  144 VAL   A CB   1 
ATOM   3183 C CG1  . VAL   A 1 144 ? 14.852 -18.432 2.050   1.00 21.21 ?  144 VAL   A CG1  1 
ATOM   3184 C CG2  . VAL   A 1 144 ? 14.449 -16.012 2.738   1.00 19.27 ?  144 VAL   A CG2  1 
ATOM   3185 H H    . VAL   A 1 144 ? 16.429 -15.144 0.868   1.00 17.15 ?  144 VAL   A H    1 
ATOM   3186 H HA   . VAL   A 1 144 ? 16.908 -16.648 2.927   1.00 19.66 ?  144 VAL   A HA   1 
ATOM   3187 H HB   . VAL   A 1 144 ? 14.962 -16.754 0.907   1.00 22.87 ?  144 VAL   A HB   1 
ATOM   3188 H HG11 . VAL   A 1 144 ? 13.894 -18.496 2.185   1.00 25.46 ?  144 VAL   A HG11 1 
ATOM   3189 H HG12 . VAL   A 1 144 ? 15.106 -18.945 1.266   1.00 25.46 ?  144 VAL   A HG12 1 
ATOM   3190 H HG13 . VAL   A 1 144 ? 15.321 -18.752 2.830   1.00 25.46 ?  144 VAL   A HG13 1 
ATOM   3191 H HG21 . VAL   A 1 144 ? 13.490 -16.158 2.630   1.00 23.12 ?  144 VAL   A HG21 1 
ATOM   3192 H HG22 . VAL   A 1 144 ? 14.699 -16.178 3.658   1.00 23.12 ?  144 VAL   A HG22 1 
ATOM   3193 H HG23 . VAL   A 1 144 ? 14.663 -15.096 2.496   1.00 23.12 ?  144 VAL   A HG23 1 
ATOM   3194 N N    . ASP   A 1 145 ? 17.824 -17.939 0.169   1.00 16.49 ?  145 ASP   A N    1 
ATOM   3195 C CA   . ASP   A 1 145 ? 18.549 -19.045 -0.447  1.00 16.81 ?  145 ASP   A CA   1 
ATOM   3196 C C    . ASP   A 1 145 ? 20.069 -18.903 -0.375  1.00 16.50 ?  145 ASP   A C    1 
ATOM   3197 O O    . ASP   A 1 145 ? 20.778 -19.804 -0.836  1.00 18.25 ?  145 ASP   A O    1 
ATOM   3198 C CB   . ASP   A 1 145 ? 18.128 -19.200 -1.912  1.00 18.33 ?  145 ASP   A CB   1 
ATOM   3199 C CG   . ASP   A 1 145 ? 16.683 -19.642 -2.066  1.00 20.66 ?  145 ASP   A CG   1 
ATOM   3200 O OD1  . ASP   A 1 145 ? 16.085 -20.157 -1.094  1.00 21.50 ?  145 ASP   A OD1  1 
ATOM   3201 O OD2  . ASP   A 1 145 ? 16.142 -19.469 -3.174  1.00 22.41 -1 145 ASP   A OD2  1 
ATOM   3202 H H    . ASP   A 1 145 ? 17.580 -17.327 -0.391  1.00 19.79 ?  145 ASP   A H    1 
ATOM   3203 H HA   . ASP   A 1 145 ? 18.304 -19.863 0.008   1.00 20.17 ?  145 ASP   A HA   1 
ATOM   3204 H HB2  . ASP   A 1 145 ? 18.239 -18.347 -2.367  1.00 22.00 ?  145 ASP   A HB2  1 
ATOM   3205 H HB3  . ASP   A 1 145 ? 18.687 -19.872 -2.333  1.00 22.00 ?  145 ASP   A HB3  1 
ATOM   3206 N N    . THR   A 1 146 ? 20.592 -17.805 0.167   1.00 14.44 ?  146 THR   A N    1 
ATOM   3207 C CA   . THR   A 1 146 ? 22.033 -17.563 0.192   1.00 14.16 ?  146 THR   A CA   1 
ATOM   3208 C C    . THR   A 1 146 ? 22.587 -17.371 1.593   1.00 14.13 ?  146 THR   A C    1 
ATOM   3209 O O    . THR   A 1 146 ? 23.652 -17.919 1.913   1.00 15.10 ?  146 THR   A O    1 
ATOM   3210 C CB   . THR   A 1 146 ? 22.366 -16.320 -0.653  1.00 14.41 ?  146 THR   A CB   1 
ATOM   3211 O OG1  . THR   A 1 146 ? 21.841 -16.486 -1.974  1.00 15.17 ?  146 THR   A OG1  1 
ATOM   3212 C CG2  . THR   A 1 146 ? 23.872 -16.101 -0.728  1.00 14.86 ?  146 THR   A CG2  1 
ATOM   3213 H H    . THR   A 1 146 ? 20.125 -17.173 0.529   1.00 17.32 ?  146 THR   A H    1 
ATOM   3214 H HA   . THR   A 1 146 ? 22.487 -18.316 -0.198  1.00 17.00 ?  146 THR   A HA   1 
ATOM   3215 H HB   . THR   A 1 146 ? 21.970 -15.532 -0.241  1.00 17.29 ?  146 THR   A HB   1 
ATOM   3216 H HG1  . THR   A 1 146 ? 21.006 -16.554 -1.937  1.00 18.21 ?  146 THR   A HG1  1 
ATOM   3217 H HG21 . THR   A 1 146 ? 24.076 -15.442 -1.410  1.00 17.83 ?  146 THR   A HG21 1 
ATOM   3218 H HG22 . THR   A 1 146 ? 24.210 -15.782 0.125   1.00 17.83 ?  146 THR   A HG22 1 
ATOM   3219 H HG23 . THR   A 1 146 ? 24.316 -16.933 -0.952  1.00 17.83 ?  146 THR   A HG23 1 
ATOM   3220 N N    . VAL   A 1 147 ? 21.910 -16.591 2.425   1.00 13.83 ?  147 VAL   A N    1 
ATOM   3221 C CA   . VAL   A 1 147 ? 22.395 -16.285 3.762   1.00 14.12 ?  147 VAL   A CA   1 
ATOM   3222 C C    . VAL   A 1 147 ? 22.072 -17.451 4.685   1.00 14.17 ?  147 VAL   A C    1 
ATOM   3223 O O    . VAL   A 1 147 ? 20.932 -17.937 4.727   1.00 15.10 ?  147 VAL   A O    1 
ATOM   3224 C CB   . VAL   A 1 147 ? 21.776 -14.975 4.274   1.00 14.36 ?  147 VAL   A CB   1 
ATOM   3225 C CG1  . VAL   A 1 147 ? 22.321 -14.638 5.638   1.00 15.35 ?  147 VAL   A CG1  1 
ATOM   3226 C CG2  . VAL   A 1 147 ? 22.035 -13.836 3.289   1.00 15.03 ?  147 VAL   A CG2  1 
ATOM   3227 H H    . VAL   A 1 147 ? 21.154 -16.220 2.241   1.00 16.59 ?  147 VAL   A H    1 
ATOM   3228 H HA   . VAL   A 1 147 ? 23.357 -16.178 3.738   1.00 16.95 ?  147 VAL   A HA   1 
ATOM   3229 H HB   . VAL   A 1 147 ? 20.818 -15.092 4.358   1.00 17.24 ?  147 VAL   A HB   1 
ATOM   3230 H HG11 . VAL   A 1 147 ? 22.054 -13.740 5.871   1.00 18.43 ?  147 VAL   A HG11 1 
ATOM   3231 H HG12 . VAL   A 1 147 ? 21.962 -15.269 6.287   1.00 18.43 ?  147 VAL   A HG12 1 
ATOM   3232 H HG13 . VAL   A 1 147 ? 23.289 -14.705 5.617   1.00 18.43 ?  147 VAL   A HG13 1 
ATOM   3233 H HG21 . VAL   A 1 147 ? 21.713 -13.009 3.679   1.00 18.03 ?  147 VAL   A HG21 1 
ATOM   3234 H HG22 . VAL   A 1 147 ? 22.985 -13.779 3.118   1.00 18.03 ?  147 VAL   A HG22 1 
ATOM   3235 H HG23 . VAL   A 1 147 ? 21.557 -14.022 2.465   1.00 18.03 ?  147 VAL   A HG23 1 
ATOM   3236 N N    . ARG   A 1 148 ? 23.085 -17.907 5.416   1.00 14.67 ?  148 ARG   A N    1 
ATOM   3237 C CA   . ARG   A 1 148 ? 22.953 -18.973 6.392   1.00 15.24 ?  148 ARG   A CA   1 
ATOM   3238 C C    . ARG   A 1 148 ? 23.074 -18.493 7.826   1.00 15.57 ?  148 ARG   A C    1 
ATOM   3239 O O    . ARG   A 1 148 ? 22.661 -19.215 8.741   1.00 16.93 ?  148 ARG   A O    1 
ATOM   3240 C CB   . ARG   A 1 148 ? 24.001 -20.065 6.128   1.00 15.66 ?  148 ARG   A CB   1 
ATOM   3241 C CG   . ARG   A 1 148 ? 23.867 -20.712 4.765   1.00 16.97 ?  148 ARG   A CG   1 
ATOM   3242 C CD   . ARG   A 1 148 ? 24.975 -21.729 4.506   1.00 17.86 ?  148 ARG   A CD   1 
ATOM   3243 N NE   . ARG   A 1 148 ? 26.311 -21.138 4.549   1.00 17.87 ?  148 ARG   A NE   1 
ATOM   3244 C CZ   . ARG   A 1 148 ? 26.840 -20.427 3.563   1.00 16.98 ?  148 ARG   A CZ   1 
ATOM   3245 N NH1  . ARG   A 1 148 ? 26.183 -20.220 2.432   1.00 17.55 ?  148 ARG   A NH1  1 
ATOM   3246 N NH2  . ARG   A 1 148 ? 28.047 -19.878 3.726   1.00 17.29 ?  148 ARG   A NH2  1 
ATOM   3247 H H    . ARG   A 1 148 ? 23.882 -17.592 5.361   1.00 17.60 ?  148 ARG   A H    1 
ATOM   3248 H HA   . ARG   A 1 148 ? 22.080 -19.380 6.297   1.00 18.29 ?  148 ARG   A HA   1 
ATOM   3249 H HB2  . ARG   A 1 148 ? 24.887 -19.679 6.185   1.00 18.80 ?  148 ARG   A HB2  1 
ATOM   3250 H HB3  . ARG   A 1 148 ? 23.903 -20.768 6.792   1.00 18.80 ?  148 ARG   A HB3  1 
ATOM   3251 H HG2  . ARG   A 1 148 ? 23.009 -21.163 4.714   1.00 20.36 ?  148 ARG   A HG2  1 
ATOM   3252 H HG3  . ARG   A 1 148 ? 23.916 -20.016 4.085   1.00 20.36 ?  148 ARG   A HG3  1 
ATOM   3253 H HD2  . ARG   A 1 148 ? 24.928 -22.415 5.185   1.00 21.43 ?  148 ARG   A HD2  1 
ATOM   3254 H HD3  . ARG   A 1 148 ? 24.843 -22.113 3.627   1.00 21.43 ?  148 ARG   A HD3  1 
ATOM   3255 H HE   . ARG   A 1 148 ? 26.794 -21.289 5.240   1.00 21.44 ?  148 ARG   A HE   1 
ATOM   3256 H HH11 . ARG   A 1 148 ? 25.404 -20.553 2.316   1.00 21.06 ?  148 ARG   A HH11 1 
ATOM   3257 H HH12 . ARG   A 1 148 ? 26.547 -19.747 1.808   1.00 21.06 ?  148 ARG   A HH12 1 
ATOM   3258 H HH21 . ARG   A 1 148 ? 28.475 -19.991 4.464   1.00 20.74 ?  148 ARG   A HH21 1 
ATOM   3259 H HH22 . ARG   A 1 148 ? 28.397 -19.405 3.096   1.00 20.74 ?  148 ARG   A HH22 1 
ATOM   3260 N N    . THR   A 1 149 ? 23.620 -17.298 8.039   1.00 15.51 ?  149 THR   A N    1 
ATOM   3261 C CA   . THR   A 1 149 ? 23.680 -16.680 9.352   1.00 15.75 ?  149 THR   A CA   1 
ATOM   3262 C C    . THR   A 1 149 ? 22.348 -15.988 9.650   1.00 15.17 ?  149 THR   A C    1 
ATOM   3263 O O    . THR   A 1 149 ? 21.424 -15.978 8.826   1.00 15.87 ?  149 THR   A O    1 
ATOM   3264 C CB   . THR   A 1 149 ? 24.877 -15.737 9.409   1.00 16.24 ?  149 THR   A CB   1 
ATOM   3265 O OG1  . THR   A 1 149 ? 24.753 -14.814 8.327   1.00 15.93 ?  149 THR   A OG1  1 
ATOM   3266 C CG2  . THR   A 1 149 ? 26.195 -16.539 9.296   1.00 16.25 ?  149 THR   A CG2  1 
ATOM   3267 H H    . THR   A 1 149 ? 23.968 -16.812 7.418   1.00 18.61 ?  149 THR   A H    1 
ATOM   3268 H HA   . THR   A 1 149 ? 23.805 -17.377 10.017  1.00 18.90 ?  149 THR   A HA   1 
ATOM   3269 H HB   . THR   A 1 149 ? 24.871 -15.262 10.250  1.00 19.48 ?  149 THR   A HB   1 
ATOM   3270 H HG1  . THR   A 1 149 ? 25.413 -14.285 8.326   1.00 19.12 ?  149 THR   A HG1  1 
ATOM   3271 H HG21 . THR   A 1 149 ? 26.954 -15.936 9.348   1.00 19.51 ?  149 THR   A HG21 1 
ATOM   3272 H HG22 . THR   A 1 149 ? 26.259 -17.186 10.017  1.00 19.51 ?  149 THR   A HG22 1 
ATOM   3273 H HG23 . THR   A 1 149 ? 26.230 -17.012 8.448   1.00 19.51 ?  149 THR   A HG23 1 
ATOM   3274 N N    . ASN   A 1 150 ? 22.219 -15.442 10.855  1.00 15.10 ?  150 ASN   A N    1 
ATOM   3275 C CA   . ASN   A 1 150 ? 20.934 -14.919 11.323  1.00 16.25 ?  150 ASN   A CA   1 
ATOM   3276 C C    . ASN   A 1 150 ? 20.760 -13.481 10.848  1.00 15.37 ?  150 ASN   A C    1 
ATOM   3277 O O    . ASN   A 1 150 ? 21.518 -12.585 11.242  1.00 16.63 ?  150 ASN   A O    1 
ATOM   3278 C CB   . ASN   A 1 150 ? 20.843 -15.034 12.840  1.00 19.39 ?  150 ASN   A CB   1 
ATOM   3279 C CG   . ASN   A 1 150 ? 20.753 -16.470 13.297  1.00 23.25 ?  150 ASN   A CG   1 
ATOM   3280 O OD1  . ASN   A 1 150 ? 20.175 -17.307 12.606  1.00 24.64 ?  150 ASN   A OD1  1 
ATOM   3281 N ND2  . ASN   A 1 150 ? 21.338 -16.771 14.453  1.00 25.97 ?  150 ASN   A ND2  1 
ATOM   3282 H H    . ASN   A 1 150 ? 22.860 -15.365 11.426  1.00 18.12 ?  150 ASN   A H    1 
ATOM   3283 H HA   . ASN   A 1 150 ? 20.220 -15.461 10.941  1.00 19.50 ?  150 ASN   A HA   1 
ATOM   3284 H HB2  . ASN   A 1 150 ? 21.633 -14.646 13.243  1.00 23.27 ?  150 ASN   A HB2  1 
ATOM   3285 H HB3  . ASN   A 1 150 ? 20.047 -14.579 13.153  1.00 23.27 ?  150 ASN   A HB3  1 
ATOM   3286 H HD21 . ASN   A 1 150 ? 21.319 -17.582 14.759  1.00 31.16 ?  150 ASN   A HD21 1 
ATOM   3287 H HD22 . ASN   A 1 150 ? 21.736 -16.160 14.908  1.00 31.16 ?  150 ASN   A HD22 1 
ATOM   3288 N N    . VAL   A 1 151 ? 19.771 -13.259 9.992   1.00 14.74 ?  151 VAL   A N    1 
ATOM   3289 C CA   . VAL   A 1 151 ? 19.563 -11.959 9.378   1.00 14.69 ?  151 VAL   A CA   1 
ATOM   3290 C C    . VAL   A 1 151 ? 18.180 -11.429 9.737   1.00 14.23 ?  151 VAL   A C    1 
ATOM   3291 O O    . VAL   A 1 151 ? 17.168 -12.136 9.604   1.00 16.04 ?  151 VAL   A O    1 
ATOM   3292 C CB   . VAL   A 1 151 ? 19.852 -11.976 7.861   1.00 16.23 ?  151 VAL   A CB   1 
ATOM   3293 C CG1  . VAL   A 1 151 ? 19.034 -13.018 7.134   1.00 17.48 ?  151 VAL   A CG1  1 
ATOM   3294 C CG2  . VAL   A 1 151 ? 19.684 -10.575 7.255   1.00 16.27 ?  151 VAL   A CG2  1 
ATOM   3295 H H    . VAL   A 1 151 ? 19.198 -13.855 9.755   1.00 17.68 ?  151 VAL   A H    1 
ATOM   3296 H HA   . VAL   A 1 151 ? 20.211 -11.344 9.766   1.00 17.63 ?  151 VAL   A HA   1 
ATOM   3297 H HB   . VAL   A 1 151 ? 20.786 -12.224 7.740   1.00 19.48 ?  151 VAL   A HB   1 
ATOM   3298 H HG11 . VAL   A 1 151 ? 19.213 -12.961 6.183   1.00 20.97 ?  151 VAL   A HG11 1 
ATOM   3299 H HG12 . VAL   A 1 151 ? 19.286 -13.903 7.459   1.00 20.97 ?  151 VAL   A HG12 1 
ATOM   3300 H HG13 . VAL   A 1 151 ? 18.093 -12.864 7.306   1.00 20.97 ?  151 VAL   A HG13 1 
ATOM   3301 H HG21 . VAL   A 1 151 ? 19.981 -10.597 6.328   1.00 19.52 ?  151 VAL   A HG21 1 
ATOM   3302 H HG22 . VAL   A 1 151 ? 18.752 -10.321 7.295   1.00 19.52 ?  151 VAL   A HG22 1 
ATOM   3303 H HG23 . VAL   A 1 151 ? 20.226 -9.947  7.756   1.00 19.52 ?  151 VAL   A HG23 1 
ATOM   3304 N N    A TYR   A 1 152 ? 18.162 -10.189 10.223  0.80 14.23 ?  152 TYR   A N    1 
ATOM   3305 N N    B TYR   A 1 152 ? 18.149 -10.168 10.167  0.20 14.36 ?  152 TYR   A N    1 
ATOM   3306 C CA   A TYR   A 1 152 ? 16.965 -9.449  10.595  0.80 14.06 ?  152 TYR   A CA   1 
ATOM   3307 C CA   B TYR   A 1 152 ? 16.933 -9.469  10.567  0.20 14.38 ?  152 TYR   A CA   1 
ATOM   3308 C C    A TYR   A 1 152 ? 16.779 -8.358  9.554   0.80 13.14 ?  152 TYR   A C    1 
ATOM   3309 C C    B TYR   A 1 152 ? 16.705 -8.336  9.575   0.20 13.56 ?  152 TYR   A C    1 
ATOM   3310 O O    A TYR   A 1 152 ? 17.569 -7.408  9.491   0.80 13.04 ?  152 TYR   A O    1 
ATOM   3311 O O    B TYR   A 1 152 ? 17.344 -7.283  9.662   0.20 13.67 ?  152 TYR   A O    1 
ATOM   3312 C CB   A TYR   A 1 152 ? 17.136 -8.892  12.005  0.80 15.32 ?  152 TYR   A CB   1 
ATOM   3313 C CB   B TYR   A 1 152 ? 17.075 -8.956  11.993  0.20 15.41 ?  152 TYR   A CB   1 
ATOM   3314 C CG   A TYR   A 1 152 ? 17.091 -10.007 13.019  0.80 16.15 ?  152 TYR   A CG   1 
ATOM   3315 C CG   B TYR   A 1 152 ? 17.031 -10.069 13.010  0.20 16.36 ?  152 TYR   A CG   1 
ATOM   3316 C CD1  A TYR   A 1 152 ? 18.226 -10.752 13.319  0.80 17.93 ?  152 TYR   A CD1  1 
ATOM   3317 C CD1  B TYR   A 1 152 ? 18.168 -10.808 13.305  0.20 17.16 ?  152 TYR   A CD1  1 
ATOM   3318 C CD2  A TYR   A 1 152 ? 15.900 -10.361 13.633  0.80 16.82 ?  152 TYR   A CD2  1 
ATOM   3319 C CD2  B TYR   A 1 152 ? 15.849 -10.397 13.657  0.20 16.86 ?  152 TYR   A CD2  1 
ATOM   3320 C CE1  A TYR   A 1 152 ? 18.185 -11.795 14.221  0.80 19.57 ?  152 TYR   A CE1  1 
ATOM   3321 C CE1  B TYR   A 1 152 ? 18.132 -11.837 14.226  0.20 17.98 ?  152 TYR   A CE1  1 
ATOM   3322 C CE2  A TYR   A 1 152 ? 15.846 -11.415 14.542  0.80 18.63 ?  152 TYR   A CE2  1 
ATOM   3323 C CE2  B TYR   A 1 152 ? 15.802 -11.426 14.580  0.20 17.66 ?  152 TYR   A CE2  1 
ATOM   3324 C CZ   A TYR   A 1 152 ? 16.996 -12.125 14.834  0.80 19.96 ?  152 TYR   A CZ   1 
ATOM   3325 C CZ   B TYR   A 1 152 ? 16.947 -12.142 14.861  0.20 18.31 ?  152 TYR   A CZ   1 
ATOM   3326 O OH   A TYR   A 1 152 ? 16.967 -13.175 15.731  0.80 22.94 ?  152 TYR   A OH   1 
ATOM   3327 O OH   B TYR   A 1 152 ? 16.908 -13.168 15.778  0.20 19.62 ?  152 TYR   A OH   1 
ATOM   3328 H H    A TYR   A 1 152 ? 18.887 -9.724  10.335  0.80 17.07 ?  152 TYR   A H    1 
ATOM   3329 H H    B TYR   A 1 152 ? 18.859 -9.674  10.233  0.20 17.24 ?  152 TYR   A H    1 
ATOM   3330 H HA   A TYR   A 1 152 ? 16.203 -10.041 10.576  0.80 16.87 ?  152 TYR   A HA   1 
ATOM   3331 H HA   B TYR   A 1 152 ? 16.184 -10.075 10.522  0.20 17.26 ?  152 TYR   A HA   1 
ATOM   3332 H HB2  A TYR   A 1 152 ? 17.999 -8.449  12.073  0.80 18.38 ?  152 TYR   A HB2  1 
ATOM   3333 H HB2  B TYR   A 1 152 ? 17.928 -8.504  12.078  0.20 18.50 ?  152 TYR   A HB2  1 
ATOM   3334 H HB3  A TYR   A 1 152 ? 16.420 -8.272  12.192  0.80 18.38 ?  152 TYR   A HB3  1 
ATOM   3335 H HB3  B TYR   A 1 152 ? 16.358 -8.335  12.182  0.20 18.50 ?  152 TYR   A HB3  1 
ATOM   3336 H HD1  A TYR   A 1 152 ? 19.033 -10.535 12.908  0.80 21.52 ?  152 TYR   A HD1  1 
ATOM   3337 H HD1  B TYR   A 1 152 ? 18.969 -10.604 12.876  0.20 20.59 ?  152 TYR   A HD1  1 
ATOM   3338 H HD2  A TYR   A 1 152 ? 15.122 -9.883  13.438  0.80 20.19 ?  152 TYR   A HD2  1 
ATOM   3339 H HD2  B TYR   A 1 152 ? 15.075 -9.915  13.467  0.20 20.23 ?  152 TYR   A HD2  1 
ATOM   3340 H HE1  A TYR   A 1 152 ? 18.957 -12.277 14.417  0.80 23.49 ?  152 TYR   A HE1  1 
ATOM   3341 H HE1  B TYR   A 1 152 ? 18.902 -12.320 14.416  0.20 21.57 ?  152 TYR   A HE1  1 
ATOM   3342 H HE2  A TYR   A 1 152 ? 15.041 -11.637 14.957  0.80 22.35 ?  152 TYR   A HE2  1 
ATOM   3343 H HE2  B TYR   A 1 152 ? 15.003 -11.631 15.009  0.20 21.20 ?  152 TYR   A HE2  1 
ATOM   3344 H HH   A TYR   A 1 152 ? 16.191 -13.276 16.036  0.80 27.53 ?  152 TYR   A HH   1 
ATOM   3345 H HH   B TYR   A 1 152 ? 16.134 -13.238 16.095  0.20 23.54 ?  152 TYR   A HH   1 
ATOM   3346 N N    A LEU   A 1 153 ? 15.761 -8.523  8.712   0.80 13.61 ?  153 LEU   A N    1 
ATOM   3347 N N    B LEU   A 1 153 ? 15.792 -8.560  8.633   0.20 12.88 ?  153 LEU   A N    1 
ATOM   3348 C CA   A LEU   A 1 153 ? 15.525 -7.647  7.572   0.80 13.09 ?  153 LEU   A CA   1 
ATOM   3349 C CA   B LEU   A 1 153 ? 15.514 -7.581  7.593   0.20 12.14 ?  153 LEU   A CA   1 
ATOM   3350 C C    A LEU   A 1 153 ? 14.523 -6.562  7.937   0.80 13.72 ?  153 LEU   A C    1 
ATOM   3351 C C    B LEU   A 1 153 ? 14.559 -6.517  8.115   0.20 11.94 ?  153 LEU   A C    1 
ATOM   3352 O O    A LEU   A 1 153 ? 13.400 -6.859  8.357   0.80 14.81 ?  153 LEU   A O    1 
ATOM   3353 O O    B LEU   A 1 153 ? 13.552 -6.833  8.757   0.20 11.91 ?  153 LEU   A O    1 
ATOM   3354 C CB   A LEU   A 1 153 ? 14.983 -8.441  6.385   0.80 13.35 ?  153 LEU   A CB   1 
ATOM   3355 C CB   B LEU   A 1 153 ? 14.900 -8.272  6.376   0.20 12.14 ?  153 LEU   A CB   1 
ATOM   3356 C CG   A LEU   A 1 153 ? 15.914 -9.466  5.749   0.80 13.66 ?  153 LEU   A CG   1 
ATOM   3357 C CG   B LEU   A 1 153 ? 15.818 -9.258  5.655   0.20 12.32 ?  153 LEU   A CG   1 
ATOM   3358 C CD1  A LEU   A 1 153 ? 15.124 -10.331 4.787   0.80 13.61 ?  153 LEU   A CD1  1 
ATOM   3359 C CD1  B LEU   A 1 153 ? 15.034 -10.100 4.668   0.20 12.79 ?  153 LEU   A CD1  1 
ATOM   3360 C CD2  A LEU   A 1 153 ? 17.056 -8.775  5.031   0.80 13.89 ?  153 LEU   A CD2  1 
ATOM   3361 C CD2  B LEU   A 1 153 ? 16.920 -8.503  4.946   0.20 12.61 ?  153 LEU   A CD2  1 
ATOM   3362 H H    A LEU   A 1 153 ? 15.177 -9.156  8.786   0.80 16.34 ?  153 LEU   A H    1 
ATOM   3363 H H    B LEU   A 1 153 ? 15.314 -9.274  8.578   0.20 15.45 ?  153 LEU   A H    1 
ATOM   3364 H HA   A LEU   A 1 153 ? 16.361 -7.230  7.315   0.80 15.70 ?  153 LEU   A HA   1 
ATOM   3365 H HA   B LEU   A 1 153 ? 16.336 -7.151  7.322   0.20 14.57 ?  153 LEU   A HA   1 
ATOM   3366 H HB2  A LEU   A 1 153 ? 14.192 -8.913  6.677   0.80 16.02 ?  153 LEU   A HB2  1 
ATOM   3367 H HB2  B LEU   A 1 153 ? 14.114 -8.760  6.661   0.20 14.57 ?  153 LEU   A HB2  1 
ATOM   3368 H HB3  A LEU   A 1 153 ? 14.743 -7.806  5.691   0.80 16.02 ?  153 LEU   A HB3  1 
ATOM   3369 H HB3  B LEU   A 1 153 ? 14.644 -7.592  5.731   0.20 14.57 ?  153 LEU   A HB3  1 
ATOM   3370 H HG   A LEU   A 1 153 ? 16.293 -10.036 6.443   0.80 16.40 ?  153 LEU   A HG   1 
ATOM   3371 H HG   B LEU   A 1 153 ? 16.224 -9.852  6.308   0.20 14.78 ?  153 LEU   A HG   1 
ATOM   3372 H HD11 A LEU   A 1 153 ? 15.694 -11.033 4.450   0.80 16.33 ?  153 LEU   A HD11 1 
ATOM   3373 H HD11 B LEU   A 1 153 ? 15.637 -10.730 4.244   0.20 15.34 ?  153 LEU   A HD11 1 
ATOM   3374 H HD12 A LEU   A 1 153 ? 14.366 -10.707 5.258   0.80 16.33 ?  153 LEU   A HD12 1 
ATOM   3375 H HD12 B LEU   A 1 153 ? 14.337 -10.576 5.144   0.20 15.34 ?  153 LEU   A HD12 1 
ATOM   3376 H HD13 A LEU   A 1 153 ? 14.813 -9.771  4.055   0.80 16.33 ?  153 LEU   A HD13 1 
ATOM   3377 H HD13 B LEU   A 1 153 ? 14.641 -9.516  4.001   0.20 15.34 ?  153 LEU   A HD13 1 
ATOM   3378 H HD21 A LEU   A 1 153 ? 17.639 -9.445  4.644   0.80 16.67 ?  153 LEU   A HD21 1 
ATOM   3379 H HD21 B LEU   A 1 153 ? 17.437 -9.129  4.419   0.20 15.13 ?  153 LEU   A HD21 1 
ATOM   3380 H HD22 A LEU   A 1 153 ? 16.691 -8.208  4.337   0.80 16.67 ?  153 LEU   A HD22 1 
ATOM   3381 H HD22 B LEU   A 1 153 ? 16.518 -7.834  4.371   0.20 15.13 ?  153 LEU   A HD22 1 
ATOM   3382 H HD23 A LEU   A 1 153 ? 17.554 -8.237  5.670   0.80 16.67 ?  153 LEU   A HD23 1 
ATOM   3383 H HD23 B LEU   A 1 153 ? 17.485 -8.077  5.608   0.20 15.13 ?  153 LEU   A HD23 1 
ATOM   3384 N N    A ALA   A 1 154 ? 14.920 -5.311  7.737   0.80 13.97 ?  154 ALA   A N    1 
ATOM   3385 N N    B ALA   A 1 154 ? 14.884 -5.255  7.843   0.20 12.08 ?  154 ALA   A N    1 
ATOM   3386 C CA   A ALA   A 1 154 ? 14.059 -4.156  7.931   0.80 14.07 ?  154 ALA   A CA   1 
ATOM   3387 C CA   B ALA   A 1 154 ? 14.030 -4.119  8.165   0.20 12.42 ?  154 ALA   A CA   1 
ATOM   3388 C C    A ALA   A 1 154 ? 13.576 -3.674  6.568   0.80 13.32 ?  154 ALA   A C    1 
ATOM   3389 C C    B ALA   A 1 154 ? 13.608 -3.483  6.848   0.20 12.32 ?  154 ALA   A C    1 
ATOM   3390 O O    A ALA   A 1 154 ? 14.386 -3.323  5.707   0.80 13.98 ?  154 ALA   A O    1 
ATOM   3391 O O    B ALA   A 1 154 ? 14.442 -2.922  6.132   0.20 12.08 ?  154 ALA   A O    1 
ATOM   3392 C CB   A ALA   A 1 154 ? 14.819 -3.048  8.656   0.80 14.93 ?  154 ALA   A CB   1 
ATOM   3393 C CB   B ALA   A 1 154 ? 14.777 -3.119  9.046   0.20 12.78 ?  154 ALA   A CB   1 
ATOM   3394 H H    A ALA   A 1 154 ? 15.721 -5.103  7.478   0.80 16.76 ?  154 ALA   A H    1 
ATOM   3395 H H    B ALA   A 1 154 ? 15.623 -5.023  7.460   0.20 14.50 ?  154 ALA   A H    1 
ATOM   3396 H HA   A ALA   A 1 154 ? 13.291 -4.413  8.461   0.80 16.88 ?  154 ALA   A HA   1 
ATOM   3397 H HA   B ALA   A 1 154 ? 13.239 -4.420  8.635   0.20 14.91 ?  154 ALA   A HA   1 
ATOM   3398 H HB1  A ALA   A 1 154 ? 14.225 -2.290  8.773   0.80 17.92 ?  154 ALA   A HB1  1 
ATOM   3399 H HB1  B ALA   A 1 154 ? 14.189 -2.373  9.247   0.20 15.34 ?  154 ALA   A HB1  1 
ATOM   3400 H HB2  A ALA   A 1 154 ? 15.111 -3.379  9.519   0.80 17.92 ?  154 ALA   A HB2  1 
ATOM   3401 H HB2  B ALA   A 1 154 ? 15.044 -3.561  9.867   0.20 15.34 ?  154 ALA   A HB2  1 
ATOM   3402 H HB3  A ALA   A 1 154 ? 15.586 -2.790  8.122   0.80 17.92 ?  154 ALA   A HB3  1 
ATOM   3403 H HB3  B ALA   A 1 154 ? 15.561 -2.802  8.570   0.20 15.34 ?  154 ALA   A HB3  1 
ATOM   3404 N N    A VAL   A 1 155 ? 12.258 -3.670  6.378   0.50 11.66 ?  155 VAL   A N    1 
ATOM   3405 N N    B VAL   A 1 155 ? 12.320 -3.578  6.524   0.20 12.26 ?  155 VAL   A N    1 
ATOM   3406 C CA   A VAL   A 1 155 ? 11.612 -3.201  5.155   0.50 14.32 ?  155 VAL   A CA   1 
ATOM   3407 C CA   B VAL   A 1 155 ? 11.776 -3.061  5.273   0.20 13.71 ?  155 VAL   A CA   1 
ATOM   3408 C CA   T VAL   A 1 155 ? 11.605 -3.260  5.242   0.30 14.63 ?  155 VAL   A CA   1 
ATOM   3409 C C    A VAL   A 1 155 ? 10.900 -1.896  5.491   0.50 15.94 ?  155 VAL   A C    1 
ATOM   3410 C C    B VAL   A 1 155 ? 10.921 -1.847  5.609   0.20 14.77 ?  155 VAL   A C    1 
ATOM   3411 C C    T VAL   A 1 155 ? 10.995 -1.888  5.553   0.30 14.31 ?  155 VAL   A C    1 
ATOM   3412 O O    A VAL   A 1 155 ? 9.923  -1.895  6.247   0.50 16.56 ?  155 VAL   A O    1 
ATOM   3413 O O    B VAL   A 1 155 ? 9.861  -1.974  6.235   0.20 15.43 ?  155 VAL   A O    1 
ATOM   3414 O O    T VAL   A 1 155 ? 10.166 -1.758  6.450   0.30 13.72 ?  155 VAL   A O    1 
ATOM   3415 C CB   A VAL   A 1 155 ? 10.626 -4.242  4.609   0.50 14.91 ?  155 VAL   A CB   1 
ATOM   3416 C CB   B VAL   A 1 155 ? 10.975 -4.126  4.512   0.20 13.64 ?  155 VAL   A CB   1 
ATOM   3417 C CB   T VAL   A 1 155 ? 10.570 -4.257  4.676   0.30 14.99 ?  155 VAL   A CB   1 
ATOM   3418 C CG1  A VAL   A 1 155 ? 9.950  -3.747  3.340   0.50 15.20 ?  155 VAL   A CG1  1 
ATOM   3419 C CG1  B VAL   A 1 155 ? 10.372 -3.537  3.247   0.20 13.74 ?  155 VAL   A CG1  1 
ATOM   3420 C CG1  T VAL   A 1 155 ? 9.899  -3.691  3.437   0.30 15.12 ?  155 VAL   A CG1  1 
ATOM   3421 C CG2  A VAL   A 1 155 ? 11.346 -5.565  4.355   0.50 15.76 ?  155 VAL   A CG2  1 
ATOM   3422 C CG2  B VAL   A 1 155 ? 11.871 -5.309  4.172   0.20 13.51 ?  155 VAL   A CG2  1 
ATOM   3423 C CG2  T VAL   A 1 155 ? 11.242 -5.597  4.359   0.30 15.40 ?  155 VAL   A CG2  1 
ATOM   3424 H H    A VAL   A 1 155 ? 11.700 -3.968  6.959   0.50 13.99 ?  155 VAL   A H    1 
ATOM   3425 H H    B VAL   A 1 155 ? 11.725 -3.940  7.030   0.20 14.71 ?  155 VAL   A H    1 
ATOM   3426 H HA   A VAL   A 1 155 ? 12.283 -3.020  4.479   0.50 17.19 ?  155 VAL   A HA   1 
ATOM   3427 H HA   B VAL   A 1 155 ? 12.502 -2.770  4.701   0.20 16.45 ?  155 VAL   A HA   1 
ATOM   3428 H HB   A VAL   A 1 155 ? 9.935  -4.400  5.273   0.50 17.89 ?  155 VAL   A HB   1 
ATOM   3429 H HB   B VAL   A 1 155 ? 10.252 -4.447  5.071   0.20 16.37 ?  155 VAL   A HB   1 
ATOM   3430 H HB   T VAL   A 1 155 ? 9.883  -4.419  5.343   0.30 17.99 ?  155 VAL   A HB   1 
ATOM   3431 H HG11 A VAL   A 1 155 ? 9.428  -4.470  2.959   0.50 18.24 ?  155 VAL   A HG11 1 
ATOM   3432 H HG11 B VAL   A 1 155 ? 9.978  -4.252  2.725   0.20 16.49 ?  155 VAL   A HG11 1 
ATOM   3433 H HG11 T VAL   A 1 155 ? 9.381  -4.391  3.011   0.30 18.14 ?  155 VAL   A HG11 1 
ATOM   3434 H HG12 A VAL   A 1 155 ? 9.368  -3.001  3.559   0.50 18.24 ?  155 VAL   A HG12 1 
ATOM   3435 H HG12 B VAL   A 1 155 ? 9.690  -2.891  3.488   0.20 16.49 ?  155 VAL   A HG12 1 
ATOM   3436 H HG12 T VAL   A 1 155 ? 9.316  -2.961  3.698   0.30 18.14 ?  155 VAL   A HG12 1 
ATOM   3437 H HG13 A VAL   A 1 155 ? 10.630 -3.462  2.710   0.50 18.24 ?  155 VAL   A HG13 1 
ATOM   3438 H HG13 B VAL   A 1 155 ? 11.073 -3.106  2.735   0.20 16.49 ?  155 VAL   A HG13 1 
ATOM   3439 H HG13 T VAL   A 1 155 ? 10.583 -3.369  2.828   0.30 18.14 ?  155 VAL   A HG13 1 
ATOM   3440 H HG21 A VAL   A 1 155 ? 10.733 -6.184  3.932   0.50 18.91 ?  155 VAL   A HG21 1 
ATOM   3441 H HG21 B VAL   A 1 155 ? 11.360 -5.956  3.660   0.20 16.21 ?  155 VAL   A HG21 1 
ATOM   3442 H HG21 T VAL   A 1 155 ? 10.579 -6.211  4.006   0.30 18.48 ?  155 VAL   A HG21 1 
ATOM   3443 H HG22 A VAL   A 1 155 ? 12.107 -5.404  3.774   0.50 18.91 ?  155 VAL   A HG22 1 
ATOM   3444 H HG22 B VAL   A 1 155 ? 12.625 -4.995  3.650   0.20 16.21 ?  155 VAL   A HG22 1 
ATOM   3445 H HG22 T VAL   A 1 155 ? 11.941 -5.452  3.699   0.30 18.48 ?  155 VAL   A HG22 1 
ATOM   3446 H HG23 A VAL   A 1 155 ? 11.651 -5.929  5.203   0.50 18.91 ?  155 VAL   A HG23 1 
ATOM   3447 H HG23 B VAL   A 1 155 ? 12.185 -5.715  4.996   0.20 16.21 ?  155 VAL   A HG23 1 
ATOM   3448 H HG23 T VAL   A 1 155 ? 11.628 -5.960  5.172   0.30 18.48 ?  155 VAL   A HG23 1 
ATOM   3449 N N    A PHE   A 1 156 ? 11.370 -0.782  4.917   0.50 17.23 ?  156 PHE   A N    1 
ATOM   3450 N N    B PHE   A 1 156 ? 11.378 -0.667  5.182   0.20 15.29 ?  156 PHE   A N    1 
ATOM   3451 N N    T PHE   A 1 156 ? 11.424 -0.866  4.806   0.30 14.94 ?  156 PHE   A N    1 
ATOM   3452 C CA   A PHE   A 1 156 ? 10.842 0.535   5.287   0.50 18.97 ?  156 PHE   A CA   1 
ATOM   3453 C CA   B PHE   A 1 156 ? 10.723 0.581   5.564   0.20 16.39 ?  156 PHE   A CA   1 
ATOM   3454 C CA   T PHE   A 1 156 ? 10.985 0.504   5.072   0.30 15.41 ?  156 PHE   A CA   1 
ATOM   3455 C C    A PHE   A 1 156 ? 9.377  0.700   4.891   0.50 19.21 ?  156 PHE   A C    1 
ATOM   3456 C C    B PHE   A 1 156 ? 9.319  0.690   4.976   0.20 16.73 ?  156 PHE   A C    1 
ATOM   3457 C C    T PHE   A 1 156 ? 9.521  0.704   4.698   0.30 16.23 ?  156 PHE   A C    1 
ATOM   3458 O O    A PHE   A 1 156 ? 8.580  1.260   5.656   0.50 19.77 ?  156 PHE   A O    1 
ATOM   3459 O O    B PHE   A 1 156 ? 8.371  1.064   5.677   0.20 17.18 ?  156 PHE   A O    1 
ATOM   3460 O O    T PHE   A 1 156 ? 8.750  1.311   5.453   0.30 17.01 ?  156 PHE   A O    1 
ATOM   3461 C CB   A PHE   A 1 156 ? 11.688 1.637   4.643   0.50 20.39 ?  156 PHE   A CB   1 
ATOM   3462 C CB   B PHE   A 1 156 ? 11.591 1.763   5.127   0.20 17.31 ?  156 PHE   A CB   1 
ATOM   3463 C CB   T PHE   A 1 156 ? 11.869 1.478   4.287   0.30 14.51 ?  156 PHE   A CB   1 
ATOM   3464 C CG   A PHE   A 1 156 ? 11.221 3.032   4.980   0.50 21.96 ?  156 PHE   A CG   1 
ATOM   3465 C CG   B PHE   A 1 156 ? 10.966 3.103   5.379   0.20 18.22 ?  156 PHE   A CG   1 
ATOM   3466 C CG   T PHE   A 1 156 ? 11.522 2.937   4.493   0.30 14.28 ?  156 PHE   A CG   1 
ATOM   3467 C CD1  A PHE   A 1 156 ? 11.171 3.451   6.300   0.50 22.54 ?  156 PHE   A CD1  1 
ATOM   3468 C CD1  B PHE   A 1 156 ? 10.953 3.644   6.653   0.20 18.70 ?  156 PHE   A CD1  1 
ATOM   3469 C CD1  T PHE   A 1 156 ? 11.931 3.601   5.644   0.30 15.36 ?  156 PHE   A CD1  1 
ATOM   3470 C CD2  A PHE   A 1 156 ? 10.842 3.924   3.985   0.50 22.89 ?  156 PHE   A CD2  1 
ATOM   3471 C CD2  B PHE   A 1 156 ? 10.400 3.825   4.341   0.20 18.79 ?  156 PHE   A CD2  1 
ATOM   3472 C CD2  T PHE   A 1 156 ? 10.819 3.647   3.530   0.30 14.72 ?  156 PHE   A CD2  1 
ATOM   3473 C CE1  A PHE   A 1 156 ? 10.743 4.726   6.625   0.50 23.05 ?  156 PHE   A CE1  1 
ATOM   3474 C CE1  B PHE   A 1 156 ? 10.382 4.878   6.888   0.20 19.12 ?  156 PHE   A CE1  1 
ATOM   3475 C CE1  T PHE   A 1 156 ? 11.628 4.939   5.841   0.30 15.97 ?  156 PHE   A CE1  1 
ATOM   3476 C CE2  A PHE   A 1 156 ? 10.413 5.206   4.306   0.50 23.43 ?  156 PHE   A CE2  1 
ATOM   3477 C CE2  B PHE   A 1 156 ? 9.829  5.060   4.570   0.20 18.89 ?  156 PHE   A CE2  1 
ATOM   3478 C CE2  T PHE   A 1 156 ? 10.513 4.986   3.720   0.30 15.63 ?  156 PHE   A CE2  1 
ATOM   3479 C CZ   A PHE   A 1 156 ? 10.371 5.607   5.628   0.50 23.39 ?  156 PHE   A CZ   1 
ATOM   3480 C CZ   B PHE   A 1 156 ? 9.820  5.586   5.844   0.20 19.42 ?  156 PHE   A CZ   1 
ATOM   3481 C CZ   T PHE   A 1 156 ? 10.919 5.633   4.880   0.30 16.17 ?  156 PHE   A CZ   1 
ATOM   3482 H H    A PHE   A 1 156 ? 11.992 -0.766  4.321   0.50 20.67 ?  156 PHE   A H    1 
ATOM   3483 H H    B PHE   A 1 156 ? 12.072 -0.566  4.681   0.20 18.34 ?  156 PHE   A H    1 
ATOM   3484 H H    T PHE   A 1 156 ? 11.974 -0.942  4.149   0.30 17.93 ?  156 PHE   A H    1 
ATOM   3485 H HA   A PHE   A 1 156 ? 10.911 0.643   6.248   0.50 22.77 ?  156 PHE   A HA   1 
ATOM   3486 H HA   B PHE   A 1 156 ? 10.644 0.608   6.528   0.20 19.66 ?  156 PHE   A HA   1 
ATOM   3487 H HA   T PHE   A 1 156 ? 11.089 0.697   6.017   0.30 18.49 ?  156 PHE   A HA   1 
ATOM   3488 H HB2  A PHE   A 1 156 ? 12.608 1.553   4.946   0.50 24.47 ?  156 PHE   A HB2  1 
ATOM   3489 H HB2  B PHE   A 1 156 ? 12.431 1.731   5.615   0.20 20.77 ?  156 PHE   A HB2  1 
ATOM   3490 H HB2  T PHE   A 1 156 ? 12.792 1.350   4.561   0.30 17.42 ?  156 PHE   A HB2  1 
ATOM   3491 H HB3  A PHE   A 1 156 ? 11.653 1.539   3.678   0.50 24.47 ?  156 PHE   A HB3  1 
ATOM   3492 H HB3  B PHE   A 1 156 ? 11.766 1.691   4.175   0.20 20.77 ?  156 PHE   A HB3  1 
ATOM   3493 H HB3  T PHE   A 1 156 ? 11.780 1.285   3.341   0.30 17.42 ?  156 PHE   A HB3  1 
ATOM   3494 H HD1  A PHE   A 1 156 ? 11.424 2.864   6.976   0.50 27.05 ?  156 PHE   A HD1  1 
ATOM   3495 H HD1  B PHE   A 1 156 ? 11.333 3.170   7.358   0.20 22.44 ?  156 PHE   A HD1  1 
ATOM   3496 H HD1  T PHE   A 1 156 ? 12.406 3.135   6.299   0.30 18.43 ?  156 PHE   A HD1  1 
ATOM   3497 H HD2  A PHE   A 1 156 ? 10.871 3.661   3.094   0.50 27.47 ?  156 PHE   A HD2  1 
ATOM   3498 H HD2  B PHE   A 1 156 ? 10.404 3.473   3.480   0.20 22.55 ?  156 PHE   A HD2  1 
ATOM   3499 H HD2  T PHE   A 1 156 ? 10.544 3.215   2.755   0.30 17.67 ?  156 PHE   A HD2  1 
ATOM   3500 H HE1  A PHE   A 1 156 ? 10.715 4.993   7.518   0.50 27.67 ?  156 PHE   A HE1  1 
ATOM   3501 H HE1  B PHE   A 1 156 ? 10.380 5.233   7.749   0.20 22.95 ?  156 PHE   A HE1  1 
ATOM   3502 H HE1  T PHE   A 1 156 ? 11.901 5.366   6.622   0.30 19.17 ?  156 PHE   A HE1  1 
ATOM   3503 H HE2  A PHE   A 1 156 ? 10.160 5.796   3.633   0.50 28.11 ?  156 PHE   A HE2  1 
ATOM   3504 H HE2  B PHE   A 1 156 ? 9.450  5.537   3.867   0.20 22.67 ?  156 PHE   A HE2  1 
ATOM   3505 H HE2  T PHE   A 1 156 ? 10.036 5.448   3.074   0.30 18.75 ?  156 PHE   A HE2  1 
ATOM   3506 H HZ   A PHE   A 1 156 ? 10.082 6.464   5.849   0.50 28.07 ?  156 PHE   A HZ   1 
ATOM   3507 H HZ   B PHE   A 1 156 ? 9.438  6.417   5.998   0.20 23.31 ?  156 PHE   A HZ   1 
ATOM   3508 H HZ   T PHE   A 1 156 ? 10.714 6.529   5.011   0.30 19.41 ?  156 PHE   A HZ   1 
ATOM   3509 N N    A ASP   A 1 157 ? 9.008  0.243   3.700   0.50 19.27 ?  157 ASP   A N    1 
ATOM   3510 N N    B ASP   A 1 157 ? 9.167  0.382   3.691   0.20 16.56 ?  157 ASP   A N    1 
ATOM   3511 N N    T ASP   A 1 157 ? 9.123  0.212   3.531   0.30 16.75 ?  157 ASP   A N    1 
ATOM   3512 C CA   A ASP   A 1 157 ? 7.702  0.534   3.118   0.50 20.35 ?  157 ASP   A CA   1 
ATOM   3513 C CA   B ASP   A 1 157 ? 7.894  0.590   3.013   0.20 16.63 ?  157 ASP   A CA   1 
ATOM   3514 C CA   T ASP   A 1 157 ? 7.822  0.514   2.952   0.30 17.36 ?  157 ASP   A CA   1 
ATOM   3515 C C    A ASP   A 1 157 ? 6.697  -0.500  3.615   0.50 20.64 ?  157 ASP   A C    1 
ATOM   3516 C C    B ASP   A 1 157 ? 6.849  -0.410  3.500   0.20 16.56 ?  157 ASP   A C    1 
ATOM   3517 C C    T ASP   A 1 157 ? 6.784  -0.455  3.505   0.30 18.13 ?  157 ASP   A C    1 
ATOM   3518 O O    A ASP   A 1 157 ? 6.814  -1.690  3.299   0.50 19.87 ?  157 ASP   A O    1 
ATOM   3519 O O    B ASP   A 1 157 ? 7.119  -1.609  3.617   0.20 16.53 ?  157 ASP   A O    1 
ATOM   3520 O O    T ASP   A 1 157 ? 6.870  -1.665  3.264   0.30 17.67 ?  157 ASP   A O    1 
ATOM   3521 C CB   A ASP   A 1 157 ? 7.815  0.505   1.598   0.50 21.52 ?  157 ASP   A CB   1 
ATOM   3522 C CB   B ASP   A 1 157 ? 8.092  0.450   1.504   0.20 16.76 ?  157 ASP   A CB   1 
ATOM   3523 C CB   T ASP   A 1 157 ? 7.917  0.380   1.435   0.30 17.28 ?  157 ASP   A CB   1 
ATOM   3524 C CG   A ASP   A 1 157 ? 6.552  0.968   0.906   0.50 22.96 ?  157 ASP   A CG   1 
ATOM   3525 C CG   B ASP   A 1 157 ? 6.878  0.883   0.716   0.20 16.82 ?  157 ASP   A CG   1 
ATOM   3526 C CG   T ASP   A 1 157 ? 6.760  1.035   0.718   0.30 16.80 ?  157 ASP   A CG   1 
ATOM   3527 O OD1  A ASP   A 1 157 ? 6.222  2.167   0.996   0.50 24.43 ?  157 ASP   A OD1  1 
ATOM   3528 O OD1  B ASP   A 1 157 ? 5.818  0.241   0.864   0.20 16.74 ?  157 ASP   A OD1  1 
ATOM   3529 O OD1  T ASP   A 1 157 ? 5.670  0.427   0.689   0.30 17.26 ?  157 ASP   A OD1  1 
ATOM   3530 O OD2  A ASP   A 1 157 ? 5.883  0.121   0.272   0.50 22.84 -1 157 ASP   A OD2  1 
ATOM   3531 O OD2  B ASP   A 1 157 ? 6.978  1.873   -0.038  0.20 16.97 -1 157 ASP   A OD2  1 
ATOM   3532 O OD2  T ASP   A 1 157 ? 6.927  2.161   0.204   0.30 15.95 -1 157 ASP   A OD2  1 
ATOM   3533 H H    A ASP   A 1 157 ? 9.516  -0.249  3.202   0.50 23.13 ?  157 ASP   A H    1 
ATOM   3534 H H    B ASP   A 1 157 ? 9.786  0.057   3.188   0.20 19.87 ?  157 ASP   A H    1 
ATOM   3535 H H    T ASP   A 1 157 ? 9.604  -0.310  3.047   0.30 20.10 ?  157 ASP   A H    1 
ATOM   3536 H HA   A ASP   A 1 157 ? 7.420  1.418   3.404   0.50 24.42 ?  157 ASP   A HA   1 
ATOM   3537 H HA   B ASP   A 1 157 ? 7.574  1.488   3.198   0.20 19.95 ?  157 ASP   A HA   1 
ATOM   3538 H HA   T ASP   A 1 157 ? 7.565  1.425   3.175   0.30 20.84 ?  157 ASP   A HA   1 
ATOM   3539 H HB2  A ASP   A 1 157 ? 8.577  1.052   1.332   0.50 25.82 ?  157 ASP   A HB2  1 
ATOM   3540 H HB2  B ASP   A 1 157 ? 8.841  1.000   1.228   0.20 20.11 ?  157 ASP   A HB2  1 
ATOM   3541 H HB2  T ASP   A 1 157 ? 8.745  0.783   1.136   0.30 20.74 ?  157 ASP   A HB2  1 
ATOM   3542 H HB3  A ASP   A 1 157 ? 7.954  -0.408  1.314   0.50 25.82 ?  157 ASP   A HB3  1 
ATOM   3543 H HB3  B ASP   A 1 157 ? 8.271  -0.480  1.291   0.20 20.11 ?  157 ASP   A HB3  1 
ATOM   3544 H HB3  T ASP   A 1 157 ? 7.916  -0.566  1.211   0.30 20.74 ?  157 ASP   A HB3  1 
ATOM   3545 N N    A LYS   A 1 158 ? 5.704  -0.043  4.388   0.50 21.90 ?  158 LYS   A N    1 
ATOM   3546 N N    B LYS   A 1 158 ? 5.639  0.088   3.771   0.20 16.40 ?  158 LYS   A N    1 
ATOM   3547 N N    T LYS   A 1 158 ? 5.799  0.077   4.235   0.30 19.18 ?  158 LYS   A N    1 
ATOM   3548 C CA   A LYS   A 1 158 ? 4.727  -0.970  4.954   0.50 22.98 ?  158 LYS   A CA   1 
ATOM   3549 C CA   B LYS   A 1 158 ? 4.591  -0.769  4.319   0.20 16.40 ?  158 LYS   A CA   1 
ATOM   3550 C CA   T LYS   A 1 158 ? 4.805  -0.790  4.862   0.30 20.45 ?  158 LYS   A CA   1 
ATOM   3551 C C    A LYS   A 1 158 ? 3.971  -1.705  3.858   0.50 21.57 ?  158 LYS   A C    1 
ATOM   3552 C C    B LYS   A 1 158 ? 3.956  -1.634  3.237   0.20 16.68 ?  158 LYS   A C    1 
ATOM   3553 C C    T LYS   A 1 158 ? 4.035  -1.591  3.821   0.30 20.05 ?  158 LYS   A C    1 
ATOM   3554 O O    A LYS   A 1 158 ? 3.731  -2.914  3.961   0.50 21.70 ?  158 LYS   A O    1 
ATOM   3555 O O    B LYS   A 1 158 ? 3.796  -2.846  3.415   0.20 16.27 ?  158 LYS   A O    1 
ATOM   3556 O O    T LYS   A 1 158 ? 3.785  -2.787  4.009   0.30 20.13 ?  158 LYS   A O    1 
ATOM   3557 C CB   A LYS   A 1 158 ? 3.753  -0.231  5.876   0.50 25.53 ?  158 LYS   A CB   1 
ATOM   3558 C CB   B LYS   A 1 158 ? 3.520  0.071   5.021   0.20 16.57 ?  158 LYS   A CB   1 
ATOM   3559 C CB   T LYS   A 1 158 ? 3.845  0.027   5.729   0.30 22.67 ?  158 LYS   A CB   1 
ATOM   3560 C CG   A LYS   A 1 158 ? 2.512  -1.043  6.291   0.50 27.73 ?  158 LYS   A CG   1 
ATOM   3561 C CG   B LYS   A 1 158 ? 2.343  -0.760  5.520   0.20 16.93 ?  158 LYS   A CG   1 
ATOM   3562 C CG   T LYS   A 1 158 ? 2.623  -0.758  6.215   0.30 24.84 ?  158 LYS   A CG   1 
ATOM   3563 C CD   A LYS   A 1 158 ? 2.847  -2.333  7.056   0.50 29.36 ?  158 LYS   A CD   1 
ATOM   3564 C CD   B LYS   A 1 158 ? 1.242  0.094   6.114   0.20 17.48 ?  158 LYS   A CD   1 
ATOM   3565 C CD   T LYS   A 1 158 ? 3.009  -1.979  7.051   0.30 26.86 ?  158 LYS   A CD   1 
ATOM   3566 C CE   A LYS   A 1 158 ? 1.578  -2.972  7.633   0.50 30.03 ?  158 LYS   A CE   1 
ATOM   3567 C CE   B LYS   A 1 158 ? 0.131  -0.771  6.692   0.20 17.57 ?  158 LYS   A CE   1 
ATOM   3568 C CE   T LYS   A 1 158 ? 1.775  -2.777  7.472   0.30 28.25 ?  158 LYS   A CE   1 
ATOM   3569 N NZ   A LYS   A 1 158 ? 1.793  -4.338  8.200   0.50 30.20 ?  158 LYS   A NZ   1 
ATOM   3570 N NZ   B LYS   A 1 158 ? -0.386 -1.761  5.708   0.20 17.76 ?  158 LYS   A NZ   1 
ATOM   3571 N NZ   T LYS   A 1 158 ? 2.109  -3.985  8.284   0.30 29.05 ?  158 LYS   A NZ   1 
ATOM   3572 H H    A LYS   A 1 158 ? 5.583  0.783   4.593   0.50 26.28 ?  158 LYS   A H    1 
ATOM   3573 H H    B LYS   A 1 158 ? 5.401  0.904   3.638   0.20 19.68 ?  158 LYS   A H    1 
ATOM   3574 H H    T LYS   A 1 158 ? 5.686  0.919   4.375   0.30 23.02 ?  158 LYS   A H    1 
ATOM   3575 H HA   A LYS   A 1 158 ? 5.195  -1.630  5.486   0.50 27.57 ?  158 LYS   A HA   1 
ATOM   3576 H HA   B LYS   A 1 158 ? 4.980  -1.360  4.980   0.20 19.68 ?  158 LYS   A HA   1 
ATOM   3577 H HA   T LYS   A 1 158 ? 5.263  -1.418  5.440   0.30 24.54 ?  158 LYS   A HA   1 
ATOM   3578 H HB2  A LYS   A 1 158 ? 4.222  0.023   6.687   0.50 30.64 ?  158 LYS   A HB2  1 
ATOM   3579 H HB2  B LYS   A 1 158 ? 3.919  0.513   5.789   0.20 19.89 ?  158 LYS   A HB2  1 
ATOM   3580 H HB2  T LYS   A 1 158 ? 4.322  0.340   6.516   0.30 27.20 ?  158 LYS   A HB2  1 
ATOM   3581 H HB3  A LYS   A 1 158 ? 3.441  0.567   5.421   0.50 30.64 ?  158 LYS   A HB3  1 
ATOM   3582 H HB3  B LYS   A 1 158 ? 3.177  0.733   4.401   0.20 19.89 ?  158 LYS   A HB3  1 
ATOM   3583 H HB3  T LYS   A 1 158 ? 3.524  0.785   5.218   0.30 27.20 ?  158 LYS   A HB3  1 
ATOM   3584 H HG2  A LYS   A 1 158 ? 1.964  -0.493  6.872   0.50 33.27 ?  158 LYS   A HG2  1 
ATOM   3585 H HG2  B LYS   A 1 158 ? 1.960  -1.257  4.780   0.20 20.32 ?  158 LYS   A HG2  1 
ATOM   3586 H HG2  T LYS   A 1 158 ? 2.080  -0.180  6.770   0.30 29.81 ?  158 LYS   A HG2  1 
ATOM   3587 H HG3  A LYS   A 1 158 ? 2.001  -1.284  5.501   0.50 33.27 ?  158 LYS   A HG3  1 
ATOM   3588 H HG3  B LYS   A 1 158 ? 2.657  -1.373  6.204   0.20 20.32 ?  158 LYS   A HG3  1 
ATOM   3589 H HG3  T LYS   A 1 158 ? 2.103  -1.062  5.453   0.30 29.81 ?  158 LYS   A HG3  1 
ATOM   3590 H HD2  A LYS   A 1 158 ? 3.263  -2.969  6.453   0.50 35.23 ?  158 LYS   A HD2  1 
ATOM   3591 H HD2  B LYS   A 1 158 ? 1.608  0.640   6.826   0.20 20.98 ?  158 LYS   A HD2  1 
ATOM   3592 H HD2  T LYS   A 1 158 ? 3.580  -2.565  6.531   0.30 32.24 ?  158 LYS   A HD2  1 
ATOM   3593 H HD3  A LYS   A 1 158 ? 3.445  -2.125  7.792   0.50 35.23 ?  158 LYS   A HD3  1 
ATOM   3594 H HD3  B LYS   A 1 158 ? 0.861  0.655   5.420   0.20 20.98 ?  158 LYS   A HD3  1 
ATOM   3595 H HD3  T LYS   A 1 158 ? 3.469  -1.688  7.854   0.30 32.24 ?  158 LYS   A HD3  1 
ATOM   3596 H HE2  A LYS   A 1 158 ? 1.235  -2.407  8.344   0.50 36.03 ?  158 LYS   A HE2  1 
ATOM   3597 H HE2  B LYS   A 1 158 ? 0.476  -1.263  7.451   0.20 21.09 ?  158 LYS   A HE2  1 
ATOM   3598 H HE2  T LYS   A 1 158 ? 1.195  -2.210  8.004   0.30 33.90 ?  158 LYS   A HE2  1 
ATOM   3599 H HE3  A LYS   A 1 158 ? 0.918  -3.046  6.929   0.50 36.03 ?  158 LYS   A HE3  1 
ATOM   3600 H HE3  B LYS   A 1 158 ? -0.606 -0.204  6.968   0.20 21.09 ?  158 LYS   A HE3  1 
ATOM   3601 H HE3  T LYS   A 1 158 ? 1.306  -3.076  6.678   0.30 33.90 ?  158 LYS   A HE3  1 
ATOM   3602 H HZ1  A LYS   A 1 158 ? 1.027  -4.660  8.520   0.50 36.24 ?  158 LYS   A HZ1  1 
ATOM   3603 H HZ1  B LYS   A 1 158 ? -1.077 -2.202  6.054   0.20 21.31 ?  158 LYS   A HZ1  1 
ATOM   3604 H HZ1  T LYS   A 1 158 ? 1.364  -4.419  8.508   0.30 34.86 ?  158 LYS   A HZ1  1 
ATOM   3605 H HZ2  A LYS   A 1 158 ? 2.093  -4.886  7.565   0.50 36.24 ?  158 LYS   A HZ2  1 
ATOM   3606 H HZ2  B LYS   A 1 158 ? -0.649 -1.345  4.967   0.20 21.31 ?  158 LYS   A HZ2  1 
ATOM   3607 H HZ2  T LYS   A 1 158 ? 2.632  -4.532  7.815   0.30 34.86 ?  158 LYS   A HZ2  1 
ATOM   3608 H HZ3  A LYS   A 1 158 ? 2.390  -4.305  8.859   0.50 36.24 ?  158 LYS   A HZ3  1 
ATOM   3609 H HZ3  B LYS   A 1 158 ? 0.254  -2.345  5.499   0.20 21.31 ?  158 LYS   A HZ3  1 
ATOM   3610 H HZ3  T LYS   A 1 158 ? 2.536  -3.744  9.027   0.30 34.86 ?  158 LYS   A HZ3  1 
ATOM   3611 N N    A ASN   A 1 159 ? 3.582  -0.997  2.799   0.50 21.13 ?  159 ASN   A N    1 
ATOM   3612 N N    B ASN   A 1 159 ? 3.569  -1.025  2.114   0.20 17.28 ?  159 ASN   A N    1 
ATOM   3613 N N    T ASN   A 1 159 ? 3.639  -0.954  2.726   0.30 20.29 ?  159 ASN   A N    1 
ATOM   3614 C CA   A ASN   A 1 159 ? 2.885  -1.670  1.712   0.50 20.49 ?  159 ASN   A CA   1 
ATOM   3615 C CA   B ASN   A 1 159 ? 2.960  -1.797  1.038   0.20 18.51 ?  159 ASN   A CA   1 
ATOM   3616 C CA   T ASN   A 1 159 ? 2.899  -1.658  1.687   0.30 20.34 ?  159 ASN   A CA   1 
ATOM   3617 C C    A ASN   A 1 159 ? 3.756  -2.755  1.089   0.50 19.32 ?  159 ASN   A C    1 
ATOM   3618 C C    B ASN   A 1 159 ? 3.909  -2.870  0.525   0.20 18.49 ?  159 ASN   A C    1 
ATOM   3619 C C    T ASN   A 1 159 ? 3.727  -2.774  1.057   0.30 20.26 ?  159 ASN   A C    1 
ATOM   3620 O O    A ASN   A 1 159 ? 3.282  -3.866  0.821   0.50 17.85 ?  159 ASN   A O    1 
ATOM   3621 O O    B ASN   A 1 159 ? 3.467  -3.947  0.109   0.20 18.31 ?  159 ASN   A O    1 
ATOM   3622 O O    T ASN   A 1 159 ? 3.194  -3.826  0.712   0.30 19.73 ?  159 ASN   A O    1 
ATOM   3623 C CB   A ASN   A 1 159 ? 2.391  -0.650  0.682   0.50 22.08 ?  159 ASN   A CB   1 
ATOM   3624 C CB   B ASN   A 1 159 ? 2.521  -0.864  -0.092  0.20 19.38 ?  159 ASN   A CB   1 
ATOM   3625 C CB   T ASN   A 1 159 ? 2.388  -0.683  0.623   0.30 21.19 ?  159 ASN   A CB   1 
ATOM   3626 C CG   A ASN   A 1 159 ? 1.131  0.071   1.140   0.50 23.93 ?  159 ASN   A CG   1 
ATOM   3627 C CG   B ASN   A 1 159 ? 1.425  0.099   0.338   0.20 20.35 ?  159 ASN   A CG   1 
ATOM   3628 C CG   T ASN   A 1 159 ? 1.168  0.095   1.087   0.30 22.22 ?  159 ASN   A CG   1 
ATOM   3629 O OD1  A ASN   A 1 159 ? 0.299  -0.507  1.840   0.50 25.44 ?  159 ASN   A OD1  1 
ATOM   3630 O OD1  B ASN   A 1 159 ? 0.521  -0.268  1.087   0.20 21.06 ?  159 ASN   A OD1  1 
ATOM   3631 O OD1  T ASN   A 1 159 ? 0.361  -0.408  1.868   0.30 23.19 ?  159 ASN   A OD1  1 
ATOM   3632 N ND2  A ASN   A 1 159 ? 0.983  1.334   0.746   0.50 24.68 ?  159 ASN   A ND2  1 
ATOM   3633 N ND2  B ASN   A 1 159 ? 1.501  1.337   -0.137  0.20 20.59 ?  159 ASN   A ND2  1 
ATOM   3634 N ND2  T ASN   A 1 159 ? 1.027  1.325   0.607   0.30 22.60 ?  159 ASN   A ND2  1 
ATOM   3635 H H    A ASN   A 1 159 ? 3.713  -0.151  2.691   0.50 25.36 ?  159 ASN   A H    1 
ATOM   3636 H H    B ASN   A 1 159 ? 3.653  -0.186  1.953   0.20 20.74 ?  159 ASN   A H    1 
ATOM   3637 H H    T ASN   A 1 159 ? 3.779  -0.121  2.566   0.30 24.34 ?  159 ASN   A H    1 
ATOM   3638 H HA   A ASN   A 1 159 ? 2.109  -2.107  2.079   0.50 24.58 ?  159 ASN   A HA   1 
ATOM   3639 H HA   B ASN   A 1 159 ? 2.168  -2.241  1.375   0.20 22.21 ?  159 ASN   A HA   1 
ATOM   3640 H HA   T ASN   A 1 159 ? 2.131  -2.077  2.093   0.30 24.41 ?  159 ASN   A HA   1 
ATOM   3641 H HB2  A ASN   A 1 159 ? 3.075  0.019   0.535   0.50 26.49 ?  159 ASN   A HB2  1 
ATOM   3642 H HB2  B ASN   A 1 159 ? 3.279  -0.336  -0.385  0.20 23.26 ?  159 ASN   A HB2  1 
ATOM   3643 H HB2  T ASN   A 1 159 ? 3.086  -0.047  0.410   0.30 25.43 ?  159 ASN   A HB2  1 
ATOM   3644 H HB3  A ASN   A 1 159 ? 2.187  -1.110  -0.146  0.50 26.49 ?  159 ASN   A HB3  1 
ATOM   3645 H HB3  B ASN   A 1 159 ? 2.181  -1.395  -0.831  0.20 23.26 ?  159 ASN   A HB3  1 
ATOM   3646 H HB3  T ASN   A 1 159 ? 2.142  -1.186  -0.172  0.30 25.43 ?  159 ASN   A HB3  1 
ATOM   3647 H HD21 A ASN   A 1 159 ? 0.284  1.780   0.980   0.50 29.62 ?  159 ASN   A HD21 1 
ATOM   3648 H HD21 B ASN   A 1 159 ? 0.901  1.915   0.075   0.20 24.70 ?  159 ASN   A HD21 1 
ATOM   3649 H HD21 T ASN   A 1 159 ? 0.349  1.800   0.841   0.30 27.12 ?  159 ASN   A HD21 1 
ATOM   3650 H HD22 A ASN   A 1 159 ? 1.585  1.704   0.261   0.50 29.62 ?  159 ASN   A HD22 1 
ATOM   3651 H HD22 B ASN   A 1 159 ? 2.147  1.557   -0.659  0.20 24.70 ?  159 ASN   A HD22 1 
ATOM   3652 H HD22 T ASN   A 1 159 ? 1.612  1.642   0.067   0.30 27.12 ?  159 ASN   A HD22 1 
ATOM   3653 N N    A LEU   A 1 160 ? 5.045  -2.479  0.898   0.50 18.55 ?  160 LEU   A N    1 
ATOM   3654 N N    B LEU   A 1 160 ? 5.214  -2.603  0.562   0.20 17.99 ?  160 LEU   A N    1 
ATOM   3655 N N    T LEU   A 1 160 ? 5.029  -2.559  0.921   0.30 20.18 ?  160 LEU   A N    1 
ATOM   3656 C CA   A LEU   A 1 160 ? 5.917  -3.516  0.356   0.50 17.74 ?  160 LEU   A CA   1 
ATOM   3657 C CA   B LEU   A 1 160 ? 6.188  -3.608  0.154   0.20 17.67 ?  160 LEU   A CA   1 
ATOM   3658 C CA   T LEU   A 1 160 ? 5.898  -3.591  0.370   0.30 19.97 ?  160 LEU   A CA   1 
ATOM   3659 C C    A LEU   A 1 160 ? 6.086  -4.666  1.343   0.50 16.36 ?  160 LEU   A C    1 
ATOM   3660 C C    B LEU   A 1 160 ? 6.269  -4.737  1.175   0.20 16.70 ?  160 LEU   A C    1 
ATOM   3661 O O    A LEU   A 1 160 ? 6.089  -5.838  0.947   0.50 15.92 ?  160 LEU   A O    1 
ATOM   3662 O O    B LEU   A 1 160 ? 6.226  -5.920  0.816   0.20 16.35 ?  160 LEU   A O    1 
ATOM   3663 C CB   A LEU   A 1 160 ? 7.270  -2.927  -0.025  0.50 17.87 ?  160 LEU   A CB   1 
ATOM   3664 C CB   B LEU   A 1 160 ? 7.554  -2.951  -0.030  0.20 18.30 ?  160 LEU   A CB   1 
ATOM   3665 C CB   T LEU   A 1 160 ? 7.266  -3.014  0.015   0.30 19.68 ?  160 LEU   A CB   1 
ATOM   3666 C CG   A LEU   A 1 160 ? 8.304  -3.965  -0.459  0.50 18.87 ?  160 LEU   A CG   1 
ATOM   3667 C CG   B LEU   A 1 160 ? 8.691  -3.871  -0.470  0.20 18.90 ?  160 LEU   A CG   1 
ATOM   3668 C CG   T LEU   A 1 160 ? 8.312  -4.040  -0.413  0.30 19.85 ?  160 LEU   A CG   1 
ATOM   3669 C CD1  A LEU   A 1 160 ? 7.812  -4.742  -1.661  0.50 19.95 ?  160 LEU   A CD1  1 
ATOM   3670 C CD1  B LEU   A 1 160 ? 8.275  -4.670  -1.684  0.20 18.86 ?  160 LEU   A CD1  1 
ATOM   3671 C CD1  T LEU   A 1 160 ? 7.860  -4.789  -1.649  0.30 20.25 ?  160 LEU   A CD1  1 
ATOM   3672 C CD2  A LEU   A 1 160 ? 9.612  -3.282  -0.764  0.50 19.02 ?  160 LEU   A CD2  1 
ATOM   3673 C CD2  B LEU   A 1 160 ? 9.942  -3.062  -0.763  0.20 19.45 ?  160 LEU   A CD2  1 
ATOM   3674 C CD2  T LEU   A 1 160 ? 9.637  -3.352  -0.660  0.30 19.65 ?  160 LEU   A CD2  1 
ATOM   3675 H H    A LEU   A 1 160 ? 5.437  -1.726  1.083   0.50 22.26 ?  160 LEU   A H    1 
ATOM   3676 H H    B LEU   A 1 160 ? 5.554  -1.854  0.815   0.20 21.59 ?  160 LEU   A H    1 
ATOM   3677 H H    T LEU   A 1 160 ? 5.438  -1.832  1.143   0.30 24.22 ?  160 LEU   A H    1 
ATOM   3678 H HA   A LEU   A 1 160 ? 5.513  -3.864  -0.447  0.50 21.28 ?  160 LEU   A HA   1 
ATOM   3679 H HA   B LEU   A 1 160 ? 5.909  -3.981  -0.697  0.20 21.20 ?  160 LEU   A HA   1 
ATOM   3680 H HB2  A LEU   A 1 160 ? 7.153  -2.304  -0.764  0.50 21.44 ?  160 LEU   A HB2  1 
ATOM   3681 H HB2  B LEU   A 1 160 ? 7.471  -2.252  -0.697  0.20 21.96 ?  160 LEU   A HB2  1 
ATOM   3682 H HB2  T LEU   A 1 160 ? 7.161  -2.376  -0.712  0.30 23.61 ?  160 LEU   A HB2  1 
ATOM   3683 H HB3  A LEU   A 1 160 ? 7.639  -2.458  0.740   0.50 21.44 ?  160 LEU   A HB3  1 
ATOM   3684 H HB3  B LEU   A 1 160 ? 7.816  -2.560  0.818   0.20 21.96 ?  160 LEU   A HB3  1 
ATOM   3685 H HB3  T LEU   A 1 160 ? 7.621  -2.564  0.796   0.30 23.61 ?  160 LEU   A HB3  1 
ATOM   3686 H HG   A LEU   A 1 160 ? 8.461  -4.591  0.266   0.50 22.65 ?  160 LEU   A HG   1 
ATOM   3687 H HG   B LEU   A 1 160 ? 8.896  -4.491  0.250   0.20 22.69 ?  160 LEU   A HG   1 
ATOM   3688 H HG   T LEU   A 1 160 ? 8.438  -4.682  0.304   0.30 23.82 ?  160 LEU   A HG   1 
ATOM   3689 H HD11 A LEU   A 1 160 ? 8.519  -5.326  -1.967  0.50 23.94 ?  160 LEU   A HD11 1 
ATOM   3690 H HD11 B LEU   A 1 160 ? 9.046  -5.138  -2.033  0.20 22.63 ?  160 LEU   A HD11 1 
ATOM   3691 H HD11 T LEU   A 1 160 ? 8.575  -5.372  -1.943  0.30 24.29 ?  160 LEU   A HD11 1 
ATOM   3692 H HD12 A LEU   A 1 160 ? 7.037  -5.266  -1.404  0.50 23.94 ?  160 LEU   A HD12 1 
ATOM   3693 H HD12 B LEU   A 1 160 ? 7.592  -5.307  -1.423  0.20 22.63 ?  160 LEU   A HD12 1 
ATOM   3694 H HD12 T LEU   A 1 160 ? 7.073  -5.311  -1.430  0.30 24.29 ?  160 LEU   A HD12 1 
ATOM   3695 H HD13 A LEU   A 1 160 ? 7.571  -4.115  -2.362  0.50 23.94 ?  160 LEU   A HD13 1 
ATOM   3696 H HD13 B LEU   A 1 160 ? 7.923  -4.061  -2.353  0.20 22.63 ?  160 LEU   A HD13 1 
ATOM   3697 H HD13 T LEU   A 1 160 ? 7.649  -4.146  -2.345  0.30 24.29 ?  160 LEU   A HD13 1 
ATOM   3698 H HD21 A LEU   A 1 160 ? 10.263 -3.949  -1.036  0.50 22.82 ?  160 LEU   A HD21 1 
ATOM   3699 H HD21 B LEU   A 1 160 ? 10.450 -3.502  -1.461  0.20 23.34 ?  160 LEU   A HD21 1 
ATOM   3700 H HD21 T LEU   A 1 160 ? 10.292 -4.014  -0.929  0.30 23.58 ?  160 LEU   A HD21 1 
ATOM   3701 H HD22 A LEU   A 1 160 ? 9.476  -2.643  -1.481  0.50 22.82 ?  160 LEU   A HD22 1 
ATOM   3702 H HD22 B LEU   A 1 160 ? 9.685  -2.172  -1.053  0.20 23.34 ?  160 LEU   A HD22 1 
ATOM   3703 H HD22 T LEU   A 1 160 ? 9.522  -2.695  -1.366  0.30 23.58 ?  160 LEU   A HD22 1 
ATOM   3704 H HD23 A LEU   A 1 160 ? 9.924  -2.822  0.032   0.50 22.82 ?  160 LEU   A HD23 1 
ATOM   3705 H HD23 B LEU   A 1 160 ? 10.473 -3.005  0.046   0.20 23.34 ?  160 LEU   A HD23 1 
ATOM   3706 H HD23 T LEU   A 1 160 ? 9.924  -2.913  0.156   0.30 23.58 ?  160 LEU   A HD23 1 
ATOM   3707 N N    A TYR   A 1 161 ? 6.243  -4.349  2.628   0.80 17.13 ?  161 TYR   A N    1 
ATOM   3708 N N    B TYR   A 1 161 ? 6.397  -4.388  2.457   0.20 16.16 ?  161 TYR   A N    1 
ATOM   3709 C CA   A TYR   A 1 161 ? 6.351  -5.388  3.645   0.80 17.04 ?  161 TYR   A CA   1 
ATOM   3710 C CA   B TYR   A 1 161 ? 6.421  -5.401  3.508   0.20 16.01 ?  161 TYR   A CA   1 
ATOM   3711 C C    A TYR   A 1 161 ? 5.199  -6.381  3.552   0.80 18.12 ?  161 TYR   A C    1 
ATOM   3712 C C    B TYR   A 1 161 ? 5.179  -6.279  3.444   0.20 16.50 ?  161 TYR   A C    1 
ATOM   3713 O O    A TYR   A 1 161 ? 5.410  -7.600  3.534   0.80 17.43 ?  161 TYR   A O    1 
ATOM   3714 O O    B TYR   A 1 161 ? 5.269  -7.511  3.502   0.20 16.33 ?  161 TYR   A O    1 
ATOM   3715 C CB   A TYR   A 1 161 ? 6.400  -4.761  5.038   0.80 17.10 ?  161 TYR   A CB   1 
ATOM   3716 C CB   B TYR   A 1 161 ? 6.535  -4.726  4.877   0.20 15.57 ?  161 TYR   A CB   1 
ATOM   3717 C CG   A TYR   A 1 161 ? 6.319  -5.805  6.122   0.80 16.44 ?  161 TYR   A CG   1 
ATOM   3718 C CG   B TYR   A 1 161 ? 6.399  -5.675  6.051   0.20 15.06 ?  161 TYR   A CG   1 
ATOM   3719 C CD1  A TYR   A 1 161 ? 7.443  -6.528  6.493   0.80 16.24 ?  161 TYR   A CD1  1 
ATOM   3720 C CD1  B TYR   A 1 161 ? 7.508  -6.325  6.577   0.20 14.94 ?  161 TYR   A CD1  1 
ATOM   3721 C CD2  A TYR   A 1 161 ? 5.116  -6.090  6.754   0.80 16.64 ?  161 TYR   A CD2  1 
ATOM   3722 C CD2  B TYR   A 1 161 ? 5.163  -5.906  6.648   0.20 15.14 ?  161 TYR   A CD2  1 
ATOM   3723 C CE1  A TYR   A 1 161 ? 7.377  -7.498  7.461   0.80 15.79 ?  161 TYR   A CE1  1 
ATOM   3724 C CE1  B TYR   A 1 161 ? 7.391  -7.188  7.653   0.20 15.01 ?  161 TYR   A CE1  1 
ATOM   3725 C CE2  A TYR   A 1 161 ? 5.041  -7.061  7.730   0.80 16.24 ?  161 TYR   A CE2  1 
ATOM   3726 C CE2  B TYR   A 1 161 ? 5.037  -6.767  7.726   0.20 15.12 ?  161 TYR   A CE2  1 
ATOM   3727 C CZ   A TYR   A 1 161 ? 6.173  -7.761  8.078   0.80 15.78 ?  161 TYR   A CZ   1 
ATOM   3728 C CZ   B TYR   A 1 161 ? 6.154  -7.405  8.224   0.20 15.24 ?  161 TYR   A CZ   1 
ATOM   3729 O OH   A TYR   A 1 161 ? 6.120  -8.728  9.049   0.80 16.24 ?  161 TYR   A OH   1 
ATOM   3730 O OH   B TYR   A 1 161 ? 6.039  -8.265  9.295   0.20 16.11 ?  161 TYR   A OH   1 
ATOM   3731 H H    A TYR   A 1 161 ? 6.292  -3.545  2.930   0.80 20.55 ?  161 TYR   A H    1 
ATOM   3732 H H    B TYR   A 1 161 ? 6.468  -3.581  2.737   0.20 19.39 ?  161 TYR   A H    1 
ATOM   3733 H HA   A TYR   A 1 161 ? 7.172  -5.878  3.510   0.80 20.45 ?  161 TYR   A HA   1 
ATOM   3734 H HA   B TYR   A 1 161 ? 7.197  -5.967  3.385   0.20 19.21 ?  161 TYR   A HA   1 
ATOM   3735 H HB2  A TYR   A 1 161 ? 7.238  -4.277  5.139   0.80 20.53 ?  161 TYR   A HB2  1 
ATOM   3736 H HB2  B TYR   A 1 161 ? 7.404  -4.300  4.940   0.20 18.69 ?  161 TYR   A HB2  1 
ATOM   3737 H HB3  A TYR   A 1 161 ? 5.651  -4.150  5.142   0.80 20.53 ?  161 TYR   A HB3  1 
ATOM   3738 H HB3  B TYR   A 1 161 ? 5.836  -4.057  4.954   0.20 18.69 ?  161 TYR   A HB3  1 
ATOM   3739 H HD1  A TYR   A 1 161 ? 8.257  -6.352  6.074   0.80 19.48 ?  161 TYR   A HD1  1 
ATOM   3740 H HD1  B TYR   A 1 161 ? 8.344  -6.182  6.197   0.20 17.93 ?  161 TYR   A HD1  1 
ATOM   3741 H HD2  A TYR   A 1 161 ? 4.345  -5.621  6.517   0.80 19.97 ?  161 TYR   A HD2  1 
ATOM   3742 H HD2  B TYR   A 1 161 ? 4.406  -5.477  6.318   0.20 18.17 ?  161 TYR   A HD2  1 
ATOM   3743 H HE1  A TYR   A 1 161 ? 8.142  -7.972  7.700   0.80 18.95 ?  161 TYR   A HE1  1 
ATOM   3744 H HE1  B TYR   A 1 161 ? 8.144  -7.617  7.992   0.20 18.01 ?  161 TYR   A HE1  1 
ATOM   3745 H HE2  A TYR   A 1 161 ? 4.223  -7.244  8.148   0.80 19.48 ?  161 TYR   A HE2  1 
ATOM   3746 H HE2  B TYR   A 1 161 ? 4.203  -6.912  8.114   0.20 18.14 ?  161 TYR   A HE2  1 
ATOM   3747 H HH   A TYR   A 1 161 ? 6.871  -9.076  9.158   0.80 19.49 ?  161 TYR   A HH   1 
ATOM   3748 H HH   B TYR   A 1 161 ? 5.237  -8.304  9.548   0.20 19.33 ?  161 TYR   A HH   1 
ATOM   3749 N N    A ASP   A 1 162 ? 3.962  -5.873  3.518   0.80 18.99 ?  162 ASP   A N    1 
ATOM   3750 N N    B ASP   A 1 162 ? 4.003  -5.657  3.331   0.20 16.91 ?  162 ASP   A N    1 
ATOM   3751 C CA   A ASP   A 1 162 ? 2.801  -6.761  3.454   0.80 19.99 ?  162 ASP   A CA   1 
ATOM   3752 C CA   B ASP   A 1 162 ? 2.776  -6.427  3.159   0.20 17.33 ?  162 ASP   A CA   1 
ATOM   3753 C C    A ASP   A 1 162 ? 2.849  -7.629  2.205   0.80 19.75 ?  162 ASP   A C    1 
ATOM   3754 C C    B ASP   A 1 162 ? 2.855  -7.304  1.916   0.20 18.19 ?  162 ASP   A C    1 
ATOM   3755 O O    A ASP   A 1 162 ? 2.500  -8.817  2.245   0.80 19.87 ?  162 ASP   A O    1 
ATOM   3756 O O    B ASP   A 1 162 ? 2.435  -8.467  1.937   0.20 17.93 ?  162 ASP   A O    1 
ATOM   3757 C CB   A ASP   A 1 162 ? 1.506  -5.947  3.483   0.80 21.18 ?  162 ASP   A CB   1 
ATOM   3758 C CB   B ASP   A 1 162 ? 1.573  -5.482  3.073   0.20 16.81 ?  162 ASP   A CB   1 
ATOM   3759 C CG   A ASP   A 1 162 ? 1.213  -5.356  4.843   0.80 22.78 ?  162 ASP   A CG   1 
ATOM   3760 C CG   B ASP   A 1 162 ? 1.289  -4.763  4.385   0.20 16.45 ?  162 ASP   A CG   1 
ATOM   3761 O OD1  A ASP   A 1 162 ? 1.842  -5.775  5.835   0.80 23.24 ?  162 ASP   A OD1  1 
ATOM   3762 O OD1  B ASP   A 1 162 ? 1.861  -5.156  5.423   0.20 16.30 ?  162 ASP   A OD1  1 
ATOM   3763 O OD2  A ASP   A 1 162 ? 0.337  -4.469  4.915   0.80 23.71 -1 162 ASP   A OD2  1 
ATOM   3764 O OD2  B ASP   A 1 162 ? 0.495  -3.797  4.379   0.20 16.09 -1 162 ASP   A OD2  1 
ATOM   3765 H H    A ASP   A 1 162 ? 3.768  -5.024  3.535   0.80 22.79 ?  162 ASP   A H    1 
ATOM   3766 H H    B ASP   A 1 162 ? 3.894  -4.804  3.351   0.20 20.30 ?  162 ASP   A H    1 
ATOM   3767 H HA   A ASP   A 1 162 ? 2.805  -7.338  4.229   0.80 23.99 ?  162 ASP   A HA   1 
ATOM   3768 H HA   B ASP   A 1 162 ? 2.652  -7.003  3.927   0.20 20.79 ?  162 ASP   A HA   1 
ATOM   3769 H HB2  A ASP   A 1 162 ? 1.568  -5.215  2.850   0.80 25.42 ?  162 ASP   A HB2  1 
ATOM   3770 H HB2  B ASP   A 1 162 ? 1.748  -4.805  2.404   0.20 20.17 ?  162 ASP   A HB2  1 
ATOM   3771 H HB3  A ASP   A 1 162 ? 0.761  -6.524  3.251   0.80 25.42 ?  162 ASP   A HB3  1 
ATOM   3772 H HB3  B ASP   A 1 162 ? 0.786  -5.996  2.831   0.20 20.17 ?  162 ASP   A HB3  1 
ATOM   3773 N N    A LYS   A 1 163 ? 3.274  -7.050  1.081   0.80 20.50 ?  163 LYS   A N    1 
ATOM   3774 N N    B LYS   A 1 163 ? 3.402  -6.767  0.823   0.20 19.27 ?  163 LYS   A N    1 
ATOM   3775 C CA   A LYS   A 1 163 ? 3.368  -7.826  -0.150  0.80 21.24 ?  163 LYS   A CA   1 
ATOM   3776 C CA   B LYS   A 1 163 ? 3.525  -7.545  -0.405  0.20 20.11 ?  163 LYS   A CA   1 
ATOM   3777 C C    A LYS   A 1 163 ? 4.452  -8.896  -0.052  0.80 20.31 ?  163 LYS   A C    1 
ATOM   3778 C C    B LYS   A 1 163 ? 4.482  -8.717  -0.220  0.20 19.48 ?  163 LYS   A C    1 
ATOM   3779 O O    A LYS   A 1 163 ? 4.290  -10.003 -0.574  0.80 20.53 ?  163 LYS   A O    1 
ATOM   3780 O O    B LYS   A 1 163 ? 4.168  -9.852  -0.592  0.20 19.30 ?  163 LYS   A O    1 
ATOM   3781 C CB   A LYS   A 1 163 ? 3.626  -6.895  -1.335  0.80 24.28 ?  163 LYS   A CB   1 
ATOM   3782 C CB   B LYS   A 1 163 ? 4.001  -6.643  -1.545  0.20 21.71 ?  163 LYS   A CB   1 
ATOM   3783 C CG   A LYS   A 1 163 ? 3.713  -7.620  -2.665  0.80 27.31 ?  163 LYS   A CG   1 
ATOM   3784 C CG   B LYS   A 1 163 ? 4.095  -7.341  -2.895  0.20 23.49 ?  163 LYS   A CG   1 
ATOM   3785 C CD   A LYS   A 1 163 ? 4.112  -6.678  -3.786  0.80 31.02 ?  163 LYS   A CD   1 
ATOM   3786 C CD   B LYS   A 1 163 ? 5.105  -6.656  -3.799  0.20 25.22 ?  163 LYS   A CD   1 
ATOM   3787 C CE   A LYS   A 1 163 ? 4.074  -7.380  -5.134  0.80 33.93 ?  163 LYS   A CE   1 
ATOM   3788 C CE   B LYS   A 1 163 ? 4.799  -6.913  -5.266  0.20 26.35 ?  163 LYS   A CE   1 
ATOM   3789 N NZ   A LYS   A 1 163 ? 4.693  -6.557  -6.210  0.80 35.33 ?  163 LYS   A NZ   1 
ATOM   3790 N NZ   B LYS   A 1 163 ? 5.936  -6.527  -6.147  0.20 27.09 ?  163 LYS   A NZ   1 
ATOM   3791 H H    A LYS   A 1 163 ? 3.502  -6.215  1.010   0.80 24.60 ?  163 LYS   A H    1 
ATOM   3792 H H    B LYS   A 1 163 ? 3.703  -5.964  0.768   0.20 23.12 ?  163 LYS   A H    1 
ATOM   3793 H HA   A LYS   A 1 163 ? 2.515  -8.262  -0.298  0.80 25.49 ?  163 LYS   A HA   1 
ATOM   3794 H HA   B LYS   A 1 163 ? 2.655  -7.901  -0.647  0.20 24.13 ?  163 LYS   A HA   1 
ATOM   3795 H HB2  A LYS   A 1 163 ? 2.894  -6.249  -1.398  0.80 29.13 ?  163 LYS   A HB2  1 
ATOM   3796 H HB2  B LYS   A 1 163 ? 3.377  -5.905  -1.642  0.20 26.05 ?  163 LYS   A HB2  1 
ATOM   3797 H HB3  A LYS   A 1 163 ? 4.459  -6.424  -1.193  0.80 29.13 ?  163 LYS   A HB3  1 
ATOM   3798 H HB3  B LYS   A 1 163 ? 4.881  -6.302  -1.329  0.20 26.05 ?  163 LYS   A HB3  1 
ATOM   3799 H HG2  A LYS   A 1 163 ? 4.382  -8.319  -2.608  0.80 32.77 ?  163 LYS   A HG2  1 
ATOM   3800 H HG2  B LYS   A 1 163 ? 4.375  -8.262  -2.773  0.20 28.18 ?  163 LYS   A HG2  1 
ATOM   3801 H HG3  A LYS   A 1 163 ? 2.847  -8.002  -2.880  0.80 32.77 ?  163 LYS   A HG3  1 
ATOM   3802 H HG3  B LYS   A 1 163 ? 3.229  -7.311  -3.330  0.20 28.18 ?  163 LYS   A HG3  1 
ATOM   3803 H HD2  A LYS   A 1 163 ? 3.493  -5.933  -3.814  0.80 37.23 ?  163 LYS   A HD2  1 
ATOM   3804 H HD2  B LYS   A 1 163 ? 5.078  -5.700  -3.642  0.20 30.26 ?  163 LYS   A HD2  1 
ATOM   3805 H HD3  A LYS   A 1 163 ? 5.015  -6.361  -3.631  0.80 37.23 ?  163 LYS   A HD3  1 
ATOM   3806 H HD3  B LYS   A 1 163 ? 5.992  -7.003  -3.607  0.20 30.26 ?  163 LYS   A HD3  1 
ATOM   3807 H HE2  A LYS   A 1 163 ? 4.554  -8.220  -5.071  0.80 40.72 ?  163 LYS   A HE2  1 
ATOM   3808 H HE2  B LYS   A 1 163 ? 4.618  -7.857  -5.394  0.20 31.62 ?  163 LYS   A HE2  1 
ATOM   3809 H HE3  A LYS   A 1 163 ? 3.152  -7.547  -5.378  0.80 40.72 ?  163 LYS   A HE3  1 
ATOM   3810 H HE3  B LYS   A 1 163 ? 4.023  -6.388  -5.524  0.20 31.62 ?  163 LYS   A HE3  1 
ATOM   3811 H HZ1  A LYS   A 1 163 ? 4.658  -6.993  -6.985  0.80 42.39 ?  163 LYS   A HZ1  1 
ATOM   3812 H HZ1  B LYS   A 1 163 ? 5.729  -6.687  -6.998  0.20 32.51 ?  163 LYS   A HZ1  1 
ATOM   3813 H HZ2  A LYS   A 1 163 ? 4.255  -5.786  -6.291  0.80 42.39 ?  163 LYS   A HZ2  1 
ATOM   3814 H HZ2  B LYS   A 1 163 ? 6.115  -5.661  -6.050  0.20 32.51 ?  163 LYS   A HZ2  1 
ATOM   3815 H HZ3  A LYS   A 1 163 ? 5.544  -6.387  -6.012  0.80 42.39 ?  163 LYS   A HZ3  1 
ATOM   3816 H HZ3  B LYS   A 1 163 ? 6.660  -6.998  -5.932  0.20 32.51 ?  163 LYS   A HZ3  1 
ATOM   3817 N N    A LEU   A 1 164 ? 5.569  -8.584  0.605   0.80 17.89 ?  164 LEU   A N    1 
ATOM   3818 N N    B LEU   A 1 164 ? 5.659  -8.459  0.353   0.20 18.64 ?  164 LEU   A N    1 
ATOM   3819 C CA   A LEU   A 1 164 ? 6.644  -9.565  0.731   0.80 17.48 ?  164 LEU   A CA   1 
ATOM   3820 C CA   B LEU   A 1 164 ? 6.662  -9.512  0.491   0.20 18.41 ?  164 LEU   A CA   1 
ATOM   3821 C C    A LEU   A 1 164 ? 6.209  -10.753 1.578   0.80 17.89 ?  164 LEU   A C    1 
ATOM   3822 C C    B LEU   A 1 164 ? 6.168  -10.617 1.413   0.20 18.13 ?  164 LEU   A C    1 
ATOM   3823 O O    A LEU   A 1 164 ? 6.529  -11.905 1.261   0.80 18.03 ?  164 LEU   A O    1 
ATOM   3824 O O    B LEU   A 1 164 ? 6.263  -11.806 1.085   0.20 18.34 ?  164 LEU   A O    1 
ATOM   3825 C CB   A LEU   A 1 164 ? 7.864  -8.897  1.355   0.80 16.87 ?  164 LEU   A CB   1 
ATOM   3826 C CB   B LEU   A 1 164 ? 7.965  -8.921  1.028   0.20 18.34 ?  164 LEU   A CB   1 
ATOM   3827 C CG   A LEU   A 1 164 ? 8.645  -7.933  0.461   0.80 16.61 ?  164 LEU   A CG   1 
ATOM   3828 C CG   B LEU   A 1 164 ? 8.777  -8.039  0.081   0.20 18.23 ?  164 LEU   A CG   1 
ATOM   3829 C CD1  A LEU   A 1 164 ? 9.567  -7.061  1.302   0.80 15.78 ?  164 LEU   A CD1  1 
ATOM   3830 C CD1  B LEU   A 1 164 ? 9.882  -7.335  0.848   0.20 17.97 ?  164 LEU   A CD1  1 
ATOM   3831 C CD2  A LEU   A 1 164 ? 9.446  -8.698  -0.576  0.80 16.84 ?  164 LEU   A CD2  1 
ATOM   3832 C CD2  B LEU   A 1 164 ? 9.358  -8.866  -1.053  0.20 18.56 ?  164 LEU   A CD2  1 
ATOM   3833 H H    A LEU   A 1 164 ? 5.726  -7.818  0.981   0.80 21.46 ?  164 LEU   A H    1 
ATOM   3834 H H    B LEU   A 1 164 ? 5.891  -7.699  0.677   0.20 22.36 ?  164 LEU   A H    1 
ATOM   3835 H HA   A LEU   A 1 164 ? 6.887  -9.877  -0.155  0.80 20.97 ?  164 LEU   A HA   1 
ATOM   3836 H HA   B LEU   A 1 164 ? 6.839  -9.900  -0.379  0.20 22.10 ?  164 LEU   A HA   1 
ATOM   3837 H HB2  A LEU   A 1 164 ? 7.573  -8.391  2.130   0.80 20.25 ?  164 LEU   A HB2  1 
ATOM   3838 H HB2  B LEU   A 1 164 ? 7.756  -8.384  1.806   0.20 22.01 ?  164 LEU   A HB2  1 
ATOM   3839 H HB3  A LEU   A 1 164 ? 8.480  -9.588  1.631   0.80 20.25 ?  164 LEU   A HB3  1 
ATOM   3840 H HB3  B LEU   A 1 164 ? 8.542  -9.655  1.292   0.20 22.01 ?  164 LEU   A HB3  1 
ATOM   3841 H HG   A LEU   A 1 164 ? 8.026  -7.346  -0.004  0.80 19.94 ?  164 LEU   A HG   1 
ATOM   3842 H HG   B LEU   A 1 164 ? 8.197  -7.362  -0.302  0.20 21.87 ?  164 LEU   A HG   1 
ATOM   3843 H HD11 A LEU   A 1 164 ? 10.056 -6.459  0.722   0.80 18.94 ?  164 LEU   A HD11 1 
ATOM   3844 H HD11 B LEU   A 1 164 ? 10.391 -6.783  0.234   0.20 21.56 ?  164 LEU   A HD11 1 
ATOM   3845 H HD12 A LEU   A 1 164 ? 9.031  -6.550  1.932   0.80 18.94 ?  164 LEU   A HD12 1 
ATOM   3846 H HD12 B LEU   A 1 164 ? 9.485  -6.782  1.540   0.20 21.56 ?  164 LEU   A HD12 1 
ATOM   3847 H HD13 A LEU   A 1 164 ? 10.186 -7.631  1.786   0.80 18.94 ?  164 LEU   A HD13 1 
ATOM   3848 H HD13 B LEU   A 1 164 ? 10.461 -8.002  1.251   0.20 21.56 ?  164 LEU   A HD13 1 
ATOM   3849 H HD21 A LEU   A 1 164 ? 9.965  -8.069  -1.106  0.80 20.20 ?  164 LEU   A HD21 1 
ATOM   3850 H HD21 B LEU   A 1 164 ? 9.935  -8.302  -1.591  0.20 22.27 ?  164 LEU   A HD21 1 
ATOM   3851 H HD22 A LEU   A 1 164 ? 10.043 -9.314  -0.123  0.80 20.20 ?  164 LEU   A HD22 1 
ATOM   3852 H HD22 B LEU   A 1 164 ? 9.869  -9.600  -0.677  0.20 22.27 ?  164 LEU   A HD22 1 
ATOM   3853 H HD23 A LEU   A 1 164 ? 8.837  -9.186  -1.149  0.80 20.20 ?  164 LEU   A HD23 1 
ATOM   3854 H HD23 B LEU   A 1 164 ? 8.632  -9.212  -1.595  0.20 22.27 ?  164 LEU   A HD23 1 
ATOM   3855 N N    A VAL   A 1 165 ? 5.510  -10.485 2.675   0.80 17.45 ?  165 VAL   A N    1 
ATOM   3856 N N    B VAL   A 1 165 ? 5.641  -10.242 2.578   0.20 17.38 ?  165 VAL   A N    1 
ATOM   3857 C CA   A VAL   A 1 165 ? 5.026  -11.557 3.535   0.80 17.13 ?  165 VAL   A CA   1 
ATOM   3858 C CA   B VAL   A 1 165 ? 5.197  -11.241 3.544   0.20 17.00 ?  165 VAL   A CA   1 
ATOM   3859 C C    A VAL   A 1 165 ? 3.996  -12.409 2.801   0.80 17.93 ?  165 VAL   A C    1 
ATOM   3860 C C    B VAL   A 1 165 ? 4.068  -12.082 2.967   0.20 16.89 ?  165 VAL   A C    1 
ATOM   3861 O O    A VAL   A 1 165 ? 4.103  -13.641 2.752   0.80 17.78 ?  165 VAL   A O    1 
ATOM   3862 O O    B VAL   A 1 165 ? 4.063  -13.312 3.099   0.20 17.01 ?  165 VAL   A O    1 
ATOM   3863 C CB   A VAL   A 1 165 ? 4.456  -10.957 4.832   0.80 17.73 ?  165 VAL   A CB   1 
ATOM   3864 C CB   B VAL   A 1 165 ? 4.804  -10.571 4.872   0.20 17.00 ?  165 VAL   A CB   1 
ATOM   3865 C CG1  A VAL   A 1 165 ? 3.719  -12.016 5.644   0.80 18.34 ?  165 VAL   A CG1  1 
ATOM   3866 C CG1  B VAL   A 1 165 ? 4.020  -11.538 5.747   0.20 17.12 ?  165 VAL   A CG1  1 
ATOM   3867 C CG2  A VAL   A 1 165 ? 5.563  -10.299 5.648   0.80 18.32 ?  165 VAL   A CG2  1 
ATOM   3868 C CG2  B VAL   A 1 165 ? 6.047  -10.082 5.596   0.20 17.03 ?  165 VAL   A CG2  1 
ATOM   3869 H H    A VAL   A 1 165 ? 5.300  -9.696  2.938   0.80 20.94 ?  165 VAL   A H    1 
ATOM   3870 H H    B VAL   A 1 165 ? 5.533  -9.427  2.829   0.20 20.85 ?  165 VAL   A H    1 
ATOM   3871 H HA   A VAL   A 1 165 ? 5.771  -12.131 3.772   0.80 20.55 ?  165 VAL   A HA   1 
ATOM   3872 H HA   B VAL   A 1 165 ? 5.933  -11.839 3.728   0.20 20.41 ?  165 VAL   A HA   1 
ATOM   3873 H HB   A VAL   A 1 165 ? 3.815  -10.270 4.597   0.80 21.28 ?  165 VAL   A HB   1 
ATOM   3874 H HB   B VAL   A 1 165 ? 4.237  -9.804  4.689   0.20 20.40 ?  165 VAL   A HB   1 
ATOM   3875 H HG11 A VAL   A 1 165 ? 3.598  -11.689 6.551   0.80 22.01 ?  165 VAL   A HG11 1 
ATOM   3876 H HG11 B VAL   A 1 165 ? 4.010  -11.200 6.656   0.20 20.54 ?  165 VAL   A HG11 1 
ATOM   3877 H HG12 A VAL   A 1 165 ? 2.850  -12.182 5.240   0.80 22.01 ?  165 VAL   A HG12 1 
ATOM   3878 H HG12 B VAL   A 1 165 ? 3.111  -11.607 5.414   0.20 20.54 ?  165 VAL   A HG12 1 
ATOM   3879 H HG13 A VAL   A 1 165 ? 4.241  -12.831 5.655   0.80 22.01 ?  165 VAL   A HG13 1 
ATOM   3880 H HG13 B VAL   A 1 165 ? 4.451  -12.406 5.723   0.20 20.54 ?  165 VAL   A HG13 1 
ATOM   3881 H HG21 A VAL   A 1 165 ? 5.186  -9.943  6.467   0.80 21.98 ?  165 VAL   A HG21 1 
ATOM   3882 H HG21 B VAL   A 1 165 ? 5.783  -9.658  6.426   0.20 20.43 ?  165 VAL   A HG21 1 
ATOM   3883 H HG22 A VAL   A 1 165 ? 6.243  -10.958 5.854   0.80 21.98 ?  165 VAL   A HG22 1 
ATOM   3884 H HG22 B VAL   A 1 165 ? 6.622  -10.842 5.779   0.20 20.43 ?  165 VAL   A HG22 1 
ATOM   3885 H HG23 A VAL   A 1 165 ? 5.953  -9.576  5.125   0.80 21.98 ?  165 VAL   A HG23 1 
ATOM   3886 H HG23 B VAL   A 1 165 ? 6.510  -9.446  5.029   0.20 20.43 ?  165 VAL   A HG23 1 
ATOM   3887 N N    A SER   A 1 166 ? 2.999  -11.763 2.196   0.80 18.50 ?  166 SER   A N    1 
ATOM   3888 N N    B SER   A 1 166 ? 3.104  -11.445 2.306   0.20 16.83 ?  166 SER   A N    1 
ATOM   3889 C CA   A SER   A 1 166 ? 1.891  -12.503 1.600   0.80 19.40 ?  166 SER   A CA   1 
ATOM   3890 C CA   B SER   A 1 166 ? 1.932  -12.176 1.849   0.20 17.09 ?  166 SER   A CA   1 
ATOM   3891 C C    A SER   A 1 166 ? 2.344  -13.349 0.423   0.80 20.39 ?  166 SER   A C    1 
ATOM   3892 C C    B SER   A 1 166 ? 2.205  -13.038 0.626   0.20 17.43 ?  166 SER   A C    1 
ATOM   3893 O O    A SER   A 1 166 ? 1.712  -14.370 0.119   0.80 22.30 ?  166 SER   A O    1 
ATOM   3894 O O    B SER   A 1 166 ? 1.374  -13.889 0.297   0.20 17.24 ?  166 SER   A O    1 
ATOM   3895 C CB   A SER   A 1 166 ? 0.792  -11.538 1.149   0.80 20.58 ?  166 SER   A CB   1 
ATOM   3896 C CB   B SER   A 1 166 ? 0.801  -11.210 1.508   0.20 17.10 ?  166 SER   A CB   1 
ATOM   3897 O OG   A SER   A 1 166 ? 0.153  -10.919 2.256   0.80 22.37 ?  166 SER   A OG   1 
ATOM   3898 O OG   B SER   A 1 166 ? 1.022  -10.627 0.238   0.20 17.16 ?  166 SER   A OG   1 
ATOM   3899 H H    A SER   A 1 166 ? 2.936  -10.913 2.125   0.80 22.20 ?  166 SER   A H    1 
ATOM   3900 H H    B SER   A 1 166 ? 3.106  -10.604 2.104   0.20 20.20 ?  166 SER   A H    1 
ATOM   3901 H HA   A SER   A 1 166 ? 1.507  -13.098 2.262   0.80 23.28 ?  166 SER   A HA   1 
ATOM   3902 H HA   B SER   A 1 166 ? 1.628  -12.753 2.565   0.20 20.51 ?  166 SER   A HA   1 
ATOM   3903 H HB2  A SER   A 1 166 ? 1.182  -10.861 0.572   0.80 24.70 ?  166 SER   A HB2  1 
ATOM   3904 H HB2  B SER   A 1 166 ? -0.039 -11.699 1.496   0.20 20.52 ?  166 SER   A HB2  1 
ATOM   3905 H HB3  A SER   A 1 166 ? 0.114  -12.033 0.660   0.80 24.70 ?  166 SER   A HB3  1 
ATOM   3906 H HB3  B SER   A 1 166 ? 0.769  -10.511 2.179   0.20 20.52 ?  166 SER   A HB3  1 
ATOM   3907 H HG   A SER   A 1 166 ? -0.423 -10.368 1.988   0.80 26.84 ?  166 SER   A HG   1 
ATOM   3908 H HG   B SER   A 1 166 ? 1.751  -10.213 0.238   0.20 20.60 ?  166 SER   A HG   1 
ATOM   3909 N N    A SER   A 1 167 ? 3.418  -12.941 -0.256  0.80 19.22 ?  167 SER   A N    1 
ATOM   3910 N N    B SER   A 1 167 ? 3.327  -12.838 -0.062  0.20 18.40 ?  167 SER   A N    1 
ATOM   3911 C CA   A SER   A 1 167 ? 3.921  -13.657 -1.419  0.80 19.82 ?  167 SER   A CA   1 
ATOM   3912 C CA   B SER   A 1 167 ? 3.610  -13.572 -1.287  0.20 19.59 ?  167 SER   A CA   1 
ATOM   3913 C C    A SER   A 1 167 ? 5.060  -14.613 -1.085  0.80 19.46 ?  167 SER   A C    1 
ATOM   3914 C C    B SER   A 1 167 ? 4.806  -14.505 -1.168  0.20 20.53 ?  167 SER   A C    1 
ATOM   3915 O O    A SER   A 1 167 ? 5.571  -15.284 -1.989  0.80 20.38 ?  167 SER   A O    1 
ATOM   3916 O O    B SER   A 1 167 ? 5.189  -15.125 -2.166  0.20 20.60 ?  167 SER   A O    1 
ATOM   3917 C CB   A SER   A 1 167 ? 4.372  -12.667 -2.507  0.80 20.28 ?  167 SER   A CB   1 
ATOM   3918 C CB   B SER   A 1 167 ? 3.825  -12.601 -2.455  0.20 19.97 ?  167 SER   A CB   1 
ATOM   3919 O OG   A SER   A 1 167 ? 5.422  -11.834 -2.043  0.80 21.08 ?  167 SER   A OG   1 
ATOM   3920 O OG   B SER   A 1 167 ? 5.022  -11.861 -2.293  0.20 20.31 ?  167 SER   A OG   1 
ATOM   3921 H H    A SER   A 1 167 ? 3.866  -12.228 -0.064  0.80 23.06 ?  167 SER   A H    1 
ATOM   3922 H H    B SER   A 1 167 ? 3.939  -12.275 0.164   0.20 22.08 ?  167 SER   A H    1 
ATOM   3923 H HA   A SER   A 1 167 ? 3.199  -14.176 -1.794  0.80 23.78 ?  167 SER   A HA   1 
ATOM   3924 H HA   B SER   A 1 167 ? 2.835  -14.111 -1.502  0.20 23.51 ?  167 SER   A HA   1 
ATOM   3925 H HB2  A SER   A 1 167 ? 4.690  -13.164 -3.277  0.80 24.34 ?  167 SER   A HB2  1 
ATOM   3926 H HB2  B SER   A 1 167 ? 3.877  -13.112 -3.277  0.20 23.97 ?  167 SER   A HB2  1 
ATOM   3927 H HB3  A SER   A 1 167 ? 3.613  -12.115 -2.771  0.80 24.34 ?  167 SER   A HB3  1 
ATOM   3928 H HB3  B SER   A 1 167 ? 3.072  -11.989 -2.495  0.20 23.97 ?  167 SER   A HB3  1 
ATOM   3929 H HG   A SER   A 1 167 ? 5.148  -11.366 -1.395  0.80 25.30 ?  167 SER   A HG   1 
ATOM   3930 H HG   B SER   A 1 167 ? 4.984  -11.407 -1.587  0.20 24.38 ?  167 SER   A HG   1 
ATOM   3931 N N    A PHE   A 1 168 ? 5.475  -14.696 0.179   0.80 19.10 ?  168 PHE   A N    1 
ATOM   3932 N N    B PHE   A 1 168 ? 5.400  -14.630 0.016   0.20 21.71 ?  168 PHE   A N    1 
ATOM   3933 C CA   A PHE   A 1 168 ? 6.657  -15.484 0.511   0.80 19.60 ?  168 PHE   A CA   1 
ATOM   3934 C CA   B PHE   A 1 168 ? 6.580  -15.468 0.172   0.20 23.00 ?  168 PHE   A CA   1 
ATOM   3935 C C    A PHE   A 1 168 ? 6.358  -16.973 0.428   0.80 21.04 ?  168 PHE   A C    1 
ATOM   3936 C C    B PHE   A 1 168 ? 6.233  -16.932 -0.068  0.20 25.18 ?  168 PHE   A C    1 
ATOM   3937 O O    A PHE   A 1 168 ? 5.388  -17.459 1.018   0.80 23.38 ?  168 PHE   A O    1 
ATOM   3938 O O    B PHE   A 1 168 ? 5.189  -17.422 0.373   0.20 25.53 ?  168 PHE   A O    1 
ATOM   3939 C CB   A PHE   A 1 168 ? 7.163  -15.164 1.914   0.80 18.84 ?  168 PHE   A CB   1 
ATOM   3940 C CB   B PHE   A 1 168 ? 7.161  -15.292 1.574   0.20 22.14 ?  168 PHE   A CB   1 
ATOM   3941 C CG   A PHE   A 1 168 ? 8.422  -15.908 2.259   0.80 18.35 ?  168 PHE   A CG   1 
ATOM   3942 C CG   B PHE   A 1 168 ? 8.467  -16.002 1.782   0.20 21.26 ?  168 PHE   A CG   1 
ATOM   3943 C CD1  A PHE   A 1 168 ? 9.618  -15.552 1.669   0.80 18.68 ?  168 PHE   A CD1  1 
ATOM   3944 C CD1  B PHE   A 1 168 ? 9.656  -15.425 1.368   0.20 20.93 ?  168 PHE   A CD1  1 
ATOM   3945 C CD2  A PHE   A 1 168 ? 8.410  -16.983 3.130   0.80 17.79 ?  168 PHE   A CD2  1 
ATOM   3946 C CD2  B PHE   A 1 168 ? 8.507  -17.244 2.393   0.20 20.72 ?  168 PHE   A CD2  1 
ATOM   3947 C CE1  A PHE   A 1 168 ? 10.780 -16.235 1.958   0.80 18.12 ?  168 PHE   A CE1  1 
ATOM   3948 C CE1  B PHE   A 1 168 ? 10.860 -16.075 1.558   0.20 20.65 ?  168 PHE   A CE1  1 
ATOM   3949 C CE2  A PHE   A 1 168 ? 9.579  -17.671 3.426   0.80 17.93 ?  168 PHE   A CE2  1 
ATOM   3950 C CE2  B PHE   A 1 168 ? 9.708  -17.898 2.586   0.20 20.49 ?  168 PHE   A CE2  1 
ATOM   3951 C CZ   A PHE   A 1 168 ? 10.761 -17.294 2.836   0.80 17.99 ?  168 PHE   A CZ   1 
ATOM   3952 C CZ   B PHE   A 1 168 ? 10.885 -17.312 2.169   0.20 20.41 ?  168 PHE   A CZ   1 
ATOM   3953 H H    A PHE   A 1 168 ? 5.102  -14.303 0.847   0.80 22.91 ?  168 PHE   A H    1 
ATOM   3954 H H    B PHE   A 1 168 ? 5.145  -14.239 0.740   0.20 26.05 ?  168 PHE   A H    1 
ATOM   3955 H HA   A PHE   A 1 168 ? 7.364  -15.277 -0.122  0.80 23.52 ?  168 PHE   A HA   1 
ATOM   3956 H HA   B PHE   A 1 168 ? 7.250  -15.204 -0.475  0.20 27.59 ?  168 PHE   A HA   1 
ATOM   3957 H HB2  A PHE   A 1 168 ? 7.350  -14.214 1.974   0.80 22.61 ?  168 PHE   A HB2  1 
ATOM   3958 H HB2  B PHE   A 1 168 ? 7.310  -14.347 1.732   0.20 26.57 ?  168 PHE   A HB2  1 
ATOM   3959 H HB3  A PHE   A 1 168 ? 6.483  -15.411 2.558   0.80 22.61 ?  168 PHE   A HB3  1 
ATOM   3960 H HB3  B PHE   A 1 168 ? 6.529  -15.639 2.222   0.20 26.57 ?  168 PHE   A HB3  1 
ATOM   3961 H HD1  A PHE   A 1 168 ? 9.646  -14.837 1.074   0.80 22.42 ?  168 PHE   A HD1  1 
ATOM   3962 H HD1  B PHE   A 1 168 ? 9.644  -14.591 0.956   0.20 25.11 ?  168 PHE   A HD1  1 
ATOM   3963 H HD2  A PHE   A 1 168 ? 7.612  -17.242 3.532   0.80 21.34 ?  168 PHE   A HD2  1 
ATOM   3964 H HD2  B PHE   A 1 168 ? 7.716  -17.642 2.676   0.20 24.86 ?  168 PHE   A HD2  1 
ATOM   3965 H HE1  A PHE   A 1 168 ? 11.587 -15.981 1.559   0.80 21.74 ?  168 PHE   A HE1  1 
ATOM   3966 H HE1  B PHE   A 1 168 ? 11.653 -15.679 1.277   0.20 24.78 ?  168 PHE   A HE1  1 
ATOM   3967 H HE2  A PHE   A 1 168 ? 9.560  -18.390 4.018   0.80 21.52 ?  168 PHE   A HE2  1 
ATOM   3968 H HE2  B PHE   A 1 168 ? 9.723  -18.732 2.998   0.20 24.58 ?  168 PHE   A HE2  1 
ATOM   3969 H HZ   A PHE   A 1 168 ? 11.549 -17.755 3.030   0.80 21.59 ?  168 PHE   A HZ   1 
ATOM   3970 H HZ   B PHE   A 1 168 ? 11.695 -17.751 2.298   0.20 24.49 ?  168 PHE   A HZ   1 
ATOM   3971 N N    A LEU   A 1 169 ? 7.227  -17.706 -0.261  0.80 23.06 ?  169 LEU   A N    1 
ATOM   3972 N N    B LEU   A 1 169 ? 7.117  -17.630 -0.776  0.20 27.13 ?  169 LEU   A N    1 
ATOM   3973 C CA   A LEU   A 1 169 ? 7.034  -19.138 -0.412  0.80 27.35 ?  169 LEU   A CA   1 
ATOM   3974 C CA   B LEU   A 1 169 ? 6.921  -19.043 -1.075  0.20 29.06 ?  169 LEU   A CA   1 
ATOM   3975 C C    A LEU   A 1 169 ? 7.866  -19.888 0.615   0.80 28.02 ?  169 LEU   A C    1 
ATOM   3976 C C    B LEU   A 1 169 ? 7.994  -19.870 -0.380  0.20 29.90 ?  169 LEU   A C    1 
ATOM   3977 O O    A LEU   A 1 169 ? 7.315  -20.397 1.596   0.80 28.19 ?  169 LEU   A O    1 
ATOM   3978 O O    B LEU   A 1 169 ? 7.828  -20.283 0.768   0.20 30.44 ?  169 LEU   A O    1 
ATOM   3979 C CB   A LEU   A 1 169 ? 7.373  -19.586 -1.839  0.80 29.89 ?  169 LEU   A CB   1 
ATOM   3980 C CB   B LEU   A 1 169 ? 6.978  -19.282 -2.584  0.20 29.92 ?  169 LEU   A CB   1 
ATOM   3981 C CG   A LEU   A 1 169 ? 7.061  -21.047 -2.181  0.80 32.43 ?  169 LEU   A CG   1 
ATOM   3982 C CG   B LEU   A 1 169 ? 6.731  -20.715 -3.064  0.20 30.60 ?  169 LEU   A CG   1 
ATOM   3983 C CD1  A LEU   A 1 169 ? 5.641  -21.417 -1.774  0.80 33.32 ?  169 LEU   A CD1  1 
ATOM   3984 C CD1  B LEU   A 1 169 ? 5.261  -21.089 -2.934  0.20 30.71 ?  169 LEU   A CD1  1 
ATOM   3985 C CD2  A LEU   A 1 169 ? 7.268  -21.308 -3.666  0.80 33.31 ?  169 LEU   A CD2  1 
ATOM   3986 C CD2  B LEU   A 1 169 ? 7.211  -20.892 -4.497  0.20 30.78 ?  169 LEU   A CD2  1 
ATOM   3987 O OXT  A LEU   A 1 169 ? 9.090  -19.985 0.499   0.80 27.08 -1 169 LEU   A OXT  1 
ATOM   3988 O OXT  B LEU   A 1 169 ? 9.052  -20.136 -0.949  0.20 29.97 -1 169 LEU   A OXT  1 
ATOM   3989 H H    A LEU   A 1 169 ? 7.935  -17.397 -0.642  0.80 27.67 ?  169 LEU   A H    1 
ATOM   3990 H H    B LEU   A 1 169 ? 7.848  -17.305 -1.094  0.20 32.55 ?  169 LEU   A H    1 
ATOM   3991 H HA   A LEU   A 1 169 ? 6.109  -19.350 -0.237  0.80 32.82 ?  169 LEU   A HA   1 
ATOM   3992 H HA   B LEU   A 1 169 ? 6.052  -19.327 -0.754  0.20 34.87 ?  169 LEU   A HA   1 
ATOM   3993 H HB2  A LEU   A 1 169 ? 6.870  -19.034 -2.459  0.80 35.87 ?  169 LEU   A HB2  1 
ATOM   3994 H HB2  B LEU   A 1 169 ? 6.307  -18.722 -3.002  0.20 35.91 ?  169 LEU   A HB2  1 
ATOM   3995 H HB3  A LEU   A 1 169 ? 8.321  -19.454 -1.988  0.80 35.87 ?  169 LEU   A HB3  1 
ATOM   3996 H HB3  B LEU   A 1 169 ? 7.856  -19.023 -2.899  0.20 35.91 ?  169 LEU   A HB3  1 
ATOM   3997 H HG   A LEU   A 1 169 ? 7.669  -21.623 -1.693  0.80 38.92 ?  169 LEU   A HG   1 
ATOM   3998 H HG   B LEU   A 1 169 ? 7.239  -21.326 -2.510  0.20 36.73 ?  169 LEU   A HG   1 
ATOM   3999 H HD11 A LEU   A 1 169 ? 5.409  -22.268 -2.177  0.80 39.99 ?  169 LEU   A HD11 1 
ATOM   4000 H HD11 B LEU   A 1 169 ? 5.137  -21.996 -3.254  0.20 36.86 ?  169 LEU   A HD11 1 
ATOM   4001 H HD12 A LEU   A 1 169 ? 5.597  -21.487 -0.808  0.80 39.99 ?  169 LEU   A HD12 1 
ATOM   4002 H HD12 B LEU   A 1 169 ? 5.002  -21.029 -2.001  0.20 36.86 ?  169 LEU   A HD12 1 
ATOM   4003 H HD13 A LEU   A 1 169 ? 5.034  -20.728 -2.086  0.80 39.99 ?  169 LEU   A HD13 1 
ATOM   4004 H HD13 B LEU   A 1 169 ? 4.731  -20.475 -3.465  0.20 36.86 ?  169 LEU   A HD13 1 
ATOM   4005 H HD21 A LEU   A 1 169 ? 7.071  -22.240 -3.854  0.80 39.97 ?  169 LEU   A HD21 1 
ATOM   4006 H HD21 B LEU   A 1 169 ? 7.038  -21.804 -4.778  0.20 36.94 ?  169 LEU   A HD21 1 
ATOM   4007 H HD22 A LEU   A 1 169 ? 6.670  -20.737 -4.174  0.80 39.97 ?  169 LEU   A HD22 1 
ATOM   4008 H HD22 B LEU   A 1 169 ? 6.733  -20.272 -5.069  0.20 36.94 ?  169 LEU   A HD22 1 
ATOM   4009 H HD23 A LEU   A 1 169 ? 8.189  -21.112 -3.896  0.80 39.97 ?  169 LEU   A HD23 1 
ATOM   4010 H HD23 B LEU   A 1 169 ? 8.164  -20.710 -4.535  0.20 36.94 ?  169 LEU   A HD23 1 
ATOM   4011 N N    A SER   B 1 1   ? 50.865 -9.300  -23.736 0.80 26.40 ?  1   SER   B N    1 
ATOM   4012 N N    B SER   B 1 1   ? 50.734 -9.262  -23.677 0.20 26.99 ?  1   SER   B N    1 
ATOM   4013 C CA   A SER   B 1 1   ? 51.323 -10.317 -22.769 0.80 27.36 ?  1   SER   B CA   1 
ATOM   4014 C CA   B SER   B 1 1   ? 51.262 -10.255 -22.719 0.20 27.13 ?  1   SER   B CA   1 
ATOM   4015 C C    A SER   B 1 1   ? 50.237 -11.357 -22.500 0.80 26.57 ?  1   SER   B C    1 
ATOM   4016 C C    B SER   B 1 1   ? 50.234 -11.347 -22.485 0.20 26.64 ?  1   SER   B C    1 
ATOM   4017 O O    A SER   B 1 1   ? 49.035 -11.146 -22.746 0.80 26.60 ?  1   SER   B O    1 
ATOM   4018 O O    B SER   B 1 1   ? 49.041 -11.167 -22.739 0.20 26.57 ?  1   SER   B O    1 
ATOM   4019 C CB   A SER   B 1 1   ? 51.752 -9.668  -21.455 0.80 27.99 ?  1   SER   B CB   1 
ATOM   4020 C CB   B SER   B 1 1   ? 51.613 -9.589  -21.392 0.20 27.35 ?  1   SER   B CB   1 
ATOM   4021 O OG   A SER   B 1 1   ? 50.639 -9.480  -20.603 0.80 30.62 ?  1   SER   B OG   1 
ATOM   4022 O OG   B SER   B 1 1   ? 50.482 -9.533  -20.543 0.20 28.10 ?  1   SER   B OG   1 
ATOM   4023 H H1   A SER   B 1 1   ? 50.732 -9.686  -24.523 0.80 31.68 ?  1   SER   B H1   1 
ATOM   4024 H H1   B SER   B 1 1   ? 50.617 -9.654  -24.465 0.20 32.39 ?  1   SER   B H1   1 
ATOM   4025 H H2   A SER   B 1 1   ? 50.113 -8.940  -23.441 0.80 31.68 ?  1   SER   B H2   1 
ATOM   4026 H H2   B SER   B 1 1   ? 49.961 -8.951  -23.375 0.20 32.39 ?  1   SER   B H2   1 
ATOM   4027 H H3   A SER   B 1 1   ? 51.492 -8.672  -23.812 0.80 31.68 ?  1   SER   B H3   1 
ATOM   4028 H H3   B SER   B 1 1   ? 51.320 -8.600  -23.753 0.20 32.39 ?  1   SER   B H3   1 
ATOM   4029 H HA   A SER   B 1 1   ? 52.095 -10.763 -23.150 0.80 32.83 ?  1   SER   B HA   1 
ATOM   4030 H HA   B SER   B 1 1   ? 52.059 -10.651 -23.092 0.20 32.55 ?  1   SER   B HA   1 
ATOM   4031 H HB2  A SER   B 1 1   ? 52.383 -10.253 -21.011 0.80 33.59 ?  1   SER   B HB2  1 
ATOM   4032 H HB2  B SER   B 1 1   ? 52.314 -10.104 -20.966 0.20 32.82 ?  1   SER   B HB2  1 
ATOM   4033 H HB3  A SER   B 1 1   ? 52.169 -8.810  -21.643 0.80 33.59 ?  1   SER   B HB3  1 
ATOM   4034 H HB3  B SER   B 1 1   ? 51.919 -8.686  -21.564 0.20 32.82 ?  1   SER   B HB3  1 
ATOM   4035 H HG   A SER   B 1 1   ? 50.872 -9.027  -19.931 0.80 36.75 ?  1   SER   B HG   1 
ATOM   4036 H HG   B SER   B 1 1   ? 50.660 -9.071  -19.865 0.20 33.72 ?  1   SER   B HG   1 
ATOM   4037 N N    A MET   B 1 2   ? 50.687 -12.489 -21.980 0.80 25.92 ?  2   MET   B N    1 
ATOM   4038 N N    B MET   B 1 2   ? 50.708 -12.483 -21.990 0.20 26.22 ?  2   MET   B N    1 
ATOM   4039 C CA   A MET   B 1 2   ? 49.869 -13.683 -21.827 0.80 26.58 ?  2   MET   B CA   1 
ATOM   4040 C CA   B MET   B 1 2   ? 49.885 -13.665 -21.798 0.20 25.91 ?  2   MET   B CA   1 
ATOM   4041 C C    A MET   B 1 2   ? 49.612 -13.900 -20.342 0.80 25.03 ?  2   MET   B C    1 
ATOM   4042 C C    B MET   B 1 2   ? 49.625 -13.839 -20.313 0.20 24.31 ?  2   MET   B C    1 
ATOM   4043 O O    A MET   B 1 2   ? 50.537 -14.203 -19.584 0.80 25.53 ?  2   MET   B O    1 
ATOM   4044 O O    B MET   B 1 2   ? 50.559 -14.058 -19.535 0.20 24.31 ?  2   MET   B O    1 
ATOM   4045 C CB   A MET   B 1 2   ? 50.611 -14.864 -22.438 0.80 30.57 ?  2   MET   B CB   1 
ATOM   4046 C CB   B MET   B 1 2   ? 50.605 -14.880 -22.357 0.20 27.57 ?  2   MET   B CB   1 
ATOM   4047 C CG   A MET   B 1 2   ? 49.796 -16.138 -22.571 0.80 34.60 ?  2   MET   B CG   1 
ATOM   4048 C CG   B MET   B 1 2   ? 49.701 -16.052 -22.718 0.20 29.04 ?  2   MET   B CG   1 
ATOM   4049 S SD   A MET   B 1 2   ? 50.655 -17.331 -23.618 0.80 38.91 ?  2   MET   B SD   1 
ATOM   4050 S SD   B MET   B 1 2   ? 50.557 -17.210 -23.790 0.20 30.37 ?  2   MET   B SD   1 
ATOM   4051 C CE   A MET   B 1 2   ? 51.130 -16.265 -24.966 0.80 39.04 ?  2   MET   B CE   1 
ATOM   4052 C CE   B MET   B 1 2   ? 51.615 -16.079 -24.677 0.20 30.68 ?  2   MET   B CE   1 
ATOM   4053 H H    A MET   B 1 2   ? 51.499 -12.600 -21.706 0.80 31.10 ?  2   MET   B H    1 
ATOM   4054 H H    B MET   B 1 2   ? 51.530 -12.601 -21.755 0.20 31.47 ?  2   MET   B H    1 
ATOM   4055 H HA   A MET   B 1 2   ? 49.033 -13.575 -22.302 0.80 31.90 ?  2   MET   B HA   1 
ATOM   4056 H HA   B MET   B 1 2   ? 49.051 -13.577 -22.283 0.20 31.09 ?  2   MET   B HA   1 
ATOM   4057 H HB2  A MET   B 1 2   ? 50.904 -14.576 -23.313 0.80 36.69 ?  2   MET   B HB2  1 
ATOM   4058 H HB2  B MET   B 1 2   ? 51.039 -14.525 -23.140 0.20 33.08 ?  2   MET   B HB2  1 
ATOM   4059 H HB3  A MET   B 1 2   ? 51.382 -15.081 -21.896 0.80 36.69 ?  2   MET   B HB3  1 
ATOM   4060 H HB3  B MET   B 1 2   ? 51.269 -15.214 -21.737 0.20 33.08 ?  2   MET   B HB3  1 
ATOM   4061 H HG2  A MET   B 1 2   ? 49.666 -16.532 -21.689 0.80 41.52 ?  2   MET   B HG2  1 
ATOM   4062 H HG2  B MET   B 1 2   ? 49.438 -16.524 -21.907 0.20 34.84 ?  2   MET   B HG2  1 
ATOM   4063 H HG3  A MET   B 1 2   ? 48.940 -15.940 -22.981 0.80 41.52 ?  2   MET   B HG3  1 
ATOM   4064 H HG3  B MET   B 1 2   ? 48.918 -15.735 -23.191 0.20 34.84 ?  2   MET   B HG3  1 
ATOM   4065 H HE1  A MET   B 1 2   ? 51.281 -16.805 -25.742 0.80 46.84 ?  2   MET   B HE1  1 
ATOM   4066 H HE1  B MET   B 1 2   ? 51.970 -16.549 -25.412 0.20 36.82 ?  2   MET   B HE1  1 
ATOM   4067 H HE2  A MET   B 1 2   ? 50.407 -15.633 -25.128 0.80 46.84 ?  2   MET   B HE2  1 
ATOM   4068 H HE2  B MET   B 1 2   ? 51.084 -15.320 -24.991 0.20 36.82 ?  2   MET   B HE2  1 
ATOM   4069 H HE3  A MET   B 1 2   ? 51.941 -15.783 -24.726 0.80 46.84 ?  2   MET   B HE3  1 
ATOM   4070 H HE3  B MET   B 1 2   ? 52.341 -15.772 -24.096 0.20 36.82 ?  2   MET   B HE3  1 
ATOM   4071 N N    . VAL   B 1 3   ? 48.361 -13.720 -19.925 1.00 22.54 ?  3   VAL   B N    1 
ATOM   4072 C CA   . VAL   B 1 3   ? 47.944 -13.960 -18.553 1.00 21.35 ?  3   VAL   B CA   1 
ATOM   4073 C C    . VAL   B 1 3   ? 46.711 -14.852 -18.572 1.00 19.65 ?  3   VAL   B C    1 
ATOM   4074 O O    . VAL   B 1 3   ? 45.984 -14.938 -19.565 1.00 20.08 ?  3   VAL   B O    1 
ATOM   4075 C CB   . VAL   B 1 3   ? 47.666 -12.650 -17.782 1.00 22.66 ?  3   VAL   B CB   1 
ATOM   4076 C CG1  . VAL   B 1 3   ? 48.947 -11.805 -17.660 1.00 23.41 ?  3   VAL   B CG1  1 
ATOM   4077 C CG2  . VAL   B 1 3   ? 46.557 -11.860 -18.455 1.00 23.41 ?  3   VAL   B CG2  1 
ATOM   4078 H H    A VAL   B 1 3   ? 47.723 -13.457 -20.441 0.80 27.05 ?  3   VAL   B H    1 
ATOM   4079 H H    B VAL   B 1 3   ? 47.718 -13.494 -20.453 0.20 27.05 ?  3   VAL   B H    1 
ATOM   4080 H HA   . VAL   B 1 3   ? 48.651 -14.432 -18.087 1.00 25.61 ?  3   VAL   B HA   1 
ATOM   4081 H HB   . VAL   B 1 3   ? 47.373 -12.876 -16.886 1.00 27.19 ?  3   VAL   B HB   1 
ATOM   4082 H HG11 . VAL   B 1 3   ? 48.741 -10.997 -17.165 1.00 28.09 ?  3   VAL   B HG11 1 
ATOM   4083 H HG12 . VAL   B 1 3   ? 49.619 -12.322 -17.188 1.00 28.09 ?  3   VAL   B HG12 1 
ATOM   4084 H HG13 . VAL   B 1 3   ? 49.261 -11.582 -18.548 1.00 28.09 ?  3   VAL   B HG13 1 
ATOM   4085 H HG21 . VAL   B 1 3   ? 46.483 -10.995 -18.028 1.00 28.09 ?  3   VAL   B HG21 1 
ATOM   4086 H HG22 . VAL   B 1 3   ? 46.771 -11.751 -19.394 1.00 28.09 ?  3   VAL   B HG22 1 
ATOM   4087 H HG23 . VAL   B 1 3   ? 45.721 -12.347 -18.362 1.00 28.09 ?  3   VAL   B HG23 1 
ATOM   4088 N N    . ASN   B 1 4   ? 46.484 -15.530 -17.451 1.00 17.79 ?  4   ASN   B N    1 
ATOM   4089 C CA   . ASN   B 1 4   ? 45.340 -16.432 -17.321 1.00 16.92 ?  4   ASN   B CA   1 
ATOM   4090 C C    . ASN   B 1 4   ? 45.273 -17.404 -18.496 1.00 17.41 ?  4   ASN   B C    1 
ATOM   4091 O O    . ASN   B 1 4   ? 44.212 -17.649 -19.069 1.00 17.72 ?  4   ASN   B O    1 
ATOM   4092 C CB   . ASN   B 1 4   ? 44.030 -15.650 -17.176 1.00 16.43 ?  4   ASN   B CB   1 
ATOM   4093 C CG   . ASN   B 1 4   ? 43.978 -14.841 -15.896 1.00 15.36 ?  4   ASN   B CG   1 
ATOM   4094 O OD1  . ASN   B 1 4   ? 44.263 -15.349 -14.814 1.00 15.71 ?  4   ASN   B OD1  1 
ATOM   4095 N ND2  . ASN   B 1 4   ? 43.651 -13.559 -16.021 1.00 16.79 ?  4   ASN   B ND2  1 
ATOM   4096 H H    . ASN   B 1 4   ? 46.987 -15.492 -16.755 1.00 21.35 ?  4   ASN   B H    1 
ATOM   4097 H HA   . ASN   B 1 4   ? 45.464 -16.962 -16.517 1.00 20.30 ?  4   ASN   B HA   1 
ATOM   4098 H HB2  . ASN   B 1 4   ? 43.946 -15.040 -17.923 1.00 19.71 ?  4   ASN   B HB2  1 
ATOM   4099 H HB3  . ASN   B 1 4   ? 43.293 -16.277 -17.168 1.00 19.71 ?  4   ASN   B HB3  1 
ATOM   4100 H HD21 . ASN   B 1 4   ? 43.614 -13.055 -15.322 1.00 20.14 ?  4   ASN   B HD21 1 
ATOM   4101 H HD22 . ASN   B 1 4   ? 43.472 -13.232 -16.794 1.00 20.14 ?  4   ASN   B HD22 1 
ATOM   4102 N N    . SER   B 1 5   ? 46.427 -17.958 -18.865 1.00 18.40 ?  5   SER   B N    1 
ATOM   4103 C CA   . SER   B 1 5   ? 46.519 -18.867 -20.006 1.00 20.55 ?  5   SER   B CA   1 
ATOM   4104 C C    . SER   B 1 5   ? 46.491 -20.302 -19.492 1.00 22.29 ?  5   SER   B C    1 
ATOM   4105 O O    . SER   B 1 5   ? 47.496 -21.006 -19.458 1.00 25.29 ?  5   SER   B O    1 
ATOM   4106 C CB   . SER   B 1 5   ? 47.780 -18.574 -20.820 1.00 22.19 ?  5   SER   B CB   1 
ATOM   4107 O OG   . SER   B 1 5   ? 48.947 -18.670 -20.019 1.00 25.26 ?  5   SER   B OG   1 
ATOM   4108 H H    . SER   B 1 5   ? 47.179 -17.838 -18.462 1.00 22.08 ?  5   SER   B H    1 
ATOM   4109 H HA   . SER   B 1 5   ? 45.753 -18.739 -20.583 1.00 24.66 ?  5   SER   B HA   1 
ATOM   4110 H HB2  . SER   B 1 5   ? 47.840 -19.213 -21.553 1.00 26.63 ?  5   SER   B HB2  1 
ATOM   4111 H HB3  . SER   B 1 5   ? 47.711 -17.674 -21.182 1.00 26.63 ?  5   SER   B HB3  1 
ATOM   4112 H HG   . SER   B 1 5   ? 49.016 -19.446 -19.712 1.00 30.32 ?  5   SER   B HG   1 
ATOM   4113 N N    . PHE   B 1 6   ? 45.305 -20.706 -19.049 1.00 22.75 ?  6   PHE   B N    1 
ATOM   4114 C CA   . PHE   B 1 6   ? 45.089 -22.054 -18.548 1.00 22.06 ?  6   PHE   B CA   1 
ATOM   4115 C C    . PHE   B 1 6   ? 44.971 -23.003 -19.729 1.00 26.13 ?  6   PHE   B C    1 
ATOM   4116 O O    . PHE   B 1 6   ? 44.269 -22.706 -20.700 1.00 28.58 ?  6   PHE   B O    1 
ATOM   4117 C CB   . PHE   B 1 6   ? 43.807 -22.101 -17.719 1.00 20.40 ?  6   PHE   B CB   1 
ATOM   4118 C CG   . PHE   B 1 6   ? 43.842 -21.241 -16.490 1.00 18.59 ?  6   PHE   B CG   1 
ATOM   4119 C CD1  . PHE   B 1 6   ? 44.339 -21.733 -15.295 1.00 17.85 ?  6   PHE   B CD1  1 
ATOM   4120 C CD2  . PHE   B 1 6   ? 43.381 -19.935 -16.531 1.00 17.66 ?  6   PHE   B CD2  1 
ATOM   4121 C CE1  . PHE   B 1 6   ? 44.368 -20.938 -14.159 1.00 17.36 ?  6   PHE   B CE1  1 
ATOM   4122 C CE2  . PHE   B 1 6   ? 43.408 -19.135 -15.404 1.00 18.57 ?  6   PHE   B CE2  1 
ATOM   4123 C CZ   . PHE   B 1 6   ? 43.905 -19.629 -14.219 1.00 17.80 ?  6   PHE   B CZ   1 
ATOM   4124 H H    . PHE   B 1 6   ? 44.602 -20.213 -19.036 1.00 27.30 ?  6   PHE   B H    1 
ATOM   4125 H HA   . PHE   B 1 6   ? 45.835 -22.332 -17.997 1.00 26.47 ?  6   PHE   B HA   1 
ATOM   4126 H HB2  . PHE   B 1 6   ? 43.067 -21.798 -18.271 1.00 24.48 ?  6   PHE   B HB2  1 
ATOM   4127 H HB3  . PHE   B 1 6   ? 43.649 -23.015 -17.435 1.00 24.48 ?  6   PHE   B HB3  1 
ATOM   4128 H HD1  . PHE   B 1 6   ? 44.662 -22.604 -15.255 1.00 21.42 ?  6   PHE   B HD1  1 
ATOM   4129 H HD2  . PHE   B 1 6   ? 43.041 -19.598 -17.325 1.00 21.19 ?  6   PHE   B HD2  1 
ATOM   4130 H HE1  . PHE   B 1 6   ? 44.715 -21.271 -13.363 1.00 20.83 ?  6   PHE   B HE1  1 
ATOM   4131 H HE2  . PHE   B 1 6   ? 43.089 -18.262 -15.448 1.00 22.29 ?  6   PHE   B HE2  1 
ATOM   4132 H HZ   . PHE   B 1 6   ? 43.927 -19.095 -13.458 1.00 21.36 ?  6   PHE   B HZ   1 
ATOM   4133 N N    A SER   B 1 7   ? 45.666 -24.137 -19.643 0.80 27.03 ?  7   SER   B N    1 
ATOM   4134 N N    B SER   B 1 7   ? 45.660 -24.140 -19.655 0.20 26.81 ?  7   SER   B N    1 
ATOM   4135 C CA   A SER   B 1 7   ? 45.736 -25.105 -20.726 0.80 30.19 ?  7   SER   B CA   1 
ATOM   4136 C CA   B SER   B 1 7   ? 45.645 -25.105 -20.743 0.20 27.85 ?  7   SER   B CA   1 
ATOM   4137 C C    A SER   B 1 7   ? 45.660 -26.512 -20.153 0.80 29.39 ?  7   SER   B C    1 
ATOM   4138 C C    B SER   B 1 7   ? 45.640 -26.518 -20.181 0.20 27.96 ?  7   SER   B C    1 
ATOM   4139 O O    A SER   B 1 7   ? 46.282 -26.810 -19.131 0.80 30.12 ?  7   SER   B O    1 
ATOM   4140 O O    B SER   B 1 7   ? 46.302 -26.799 -19.178 0.20 28.40 ?  7   SER   B O    1 
ATOM   4141 C CB   A SER   B 1 7   ? 47.044 -24.941 -21.514 0.80 33.52 ?  7   SER   B CB   1 
ATOM   4142 C CB   B SER   B 1 7   ? 46.855 -24.919 -21.667 0.20 28.47 ?  7   SER   B CB   1 
ATOM   4143 O OG   A SER   B 1 7   ? 47.122 -25.863 -22.586 0.80 35.53 ?  7   SER   B OG   1 
ATOM   4144 O OG   B SER   B 1 7   ? 46.599 -25.455 -22.953 0.20 28.87 ?  7   SER   B OG   1 
ATOM   4145 H H    A SER   B 1 7   ? 46.125 -24.366 -18.950 0.80 32.43 ?  7   SER   B H    1 
ATOM   4146 H H    B SER   B 1 7   ? 46.151 -24.373 -18.984 0.20 32.17 ?  7   SER   B H    1 
ATOM   4147 H HA   A SER   B 1 7   ? 44.993 -24.978 -21.331 0.80 36.23 ?  7   SER   B HA   1 
ATOM   4148 H HA   B SER   B 1 7   ? 44.841 -24.987 -21.268 0.20 33.42 ?  7   SER   B HA   1 
ATOM   4149 H HB2  A SER   B 1 7   ? 47.083 -24.041 -21.876 0.80 40.23 ?  7   SER   B HB2  1 
ATOM   4150 H HB2  B SER   B 1 7   ? 47.045 -23.970 -21.749 0.20 34.16 ?  7   SER   B HB2  1 
ATOM   4151 H HB3  A SER   B 1 7   ? 47.796 -25.085 -20.915 0.80 40.23 ?  7   SER   B HB3  1 
ATOM   4152 H HB3  B SER   B 1 7   ? 47.620 -25.377 -21.284 0.20 34.16 ?  7   SER   B HB3  1 
ATOM   4153 H HG   A SER   B 1 7   ? 47.848 -25.761 -23.000 0.80 42.63 ?  7   SER   B HG   1 
ATOM   4154 H HG   B SER   B 1 7   ? 47.267 -25.339 -23.451 0.20 34.64 ?  7   SER   B HG   1 
ATOM   4155 N N    A GLY   B 1 8   ? 44.893 -27.373 -20.820 0.80 29.00 ?  8   GLY   B N    1 
ATOM   4156 N N    B GLY   B 1 8   ? 44.889 -27.400 -20.836 0.20 27.75 ?  8   GLY   B N    1 
ATOM   4157 C CA   A GLY   B 1 8   ? 44.847 -28.771 -20.452 0.80 28.29 ?  8   GLY   B CA   1 
ATOM   4158 C CA   B GLY   B 1 8   ? 44.851 -28.792 -20.443 0.20 27.29 ?  8   GLY   B CA   1 
ATOM   4159 C C    A GLY   B 1 8   ? 43.952 -29.102 -19.286 0.80 27.01 ?  8   GLY   B C    1 
ATOM   4160 C C    B GLY   B 1 8   ? 43.945 -29.109 -19.278 0.20 26.48 ?  8   GLY   B C    1 
ATOM   4161 O O    A GLY   B 1 8   ? 44.133 -30.158 -18.668 0.80 28.66 ?  8   GLY   B O    1 
ATOM   4162 O O    B GLY   B 1 8   ? 44.125 -30.152 -18.641 0.20 27.10 ?  8   GLY   B O    1 
ATOM   4163 H H    A GLY   B 1 8   ? 44.398 -27.165 -21.489 0.80 34.79 ?  8   GLY   B H    1 
ATOM   4164 H H    B GLY   B 1 8   ? 44.398 -27.213 -21.517 0.20 33.30 ?  8   GLY   B H    1 
ATOM   4165 H HA2  A GLY   B 1 8   ? 44.532 -29.285 -21.208 0.80 33.95 ?  8   GLY   B HA2  1 
ATOM   4166 H HA2  B GLY   B 1 8   ? 44.557 -29.325 -21.198 0.20 32.74 ?  8   GLY   B HA2  1 
ATOM   4167 H HA3  A GLY   B 1 8   ? 45.742 -29.070 -20.233 0.80 33.95 ?  8   GLY   B HA3  1 
ATOM   4168 H HA3  B GLY   B 1 8   ? 45.745 -29.077 -20.204 0.20 32.74 ?  8   GLY   B HA3  1 
ATOM   4169 N N    . TYR   B 1 9   ? 42.970 -28.255 -18.980 1.00 25.28 ?  9   TYR   B N    1 
ATOM   4170 C CA   . TYR   B 1 9   ? 42.039 -28.528 -17.896 1.00 22.52 ?  9   TYR   B CA   1 
ATOM   4171 C C    . TYR   B 1 9   ? 40.846 -29.326 -18.389 1.00 22.19 ?  9   TYR   B C    1 
ATOM   4172 O O    . TYR   B 1 9   ? 40.409 -29.195 -19.537 1.00 24.09 ?  9   TYR   B O    1 
ATOM   4173 C CB   . TYR   B 1 9   ? 41.543 -27.241 -17.243 1.00 21.61 ?  9   TYR   B CB   1 
ATOM   4174 C CG   . TYR   B 1 9   ? 42.582 -26.625 -16.337 1.00 20.86 ?  9   TYR   B CG   1 
ATOM   4175 C CD1  . TYR   B 1 9   ? 43.666 -25.942 -16.865 1.00 21.77 ?  9   TYR   B CD1  1 
ATOM   4176 C CD2  . TYR   B 1 9   ? 42.495 -26.750 -14.957 1.00 20.25 ?  9   TYR   B CD2  1 
ATOM   4177 C CE1  . TYR   B 1 9   ? 44.633 -25.388 -16.047 1.00 21.65 ?  9   TYR   B CE1  1 
ATOM   4178 C CE2  . TYR   B 1 9   ? 43.462 -26.199 -14.126 1.00 20.31 ?  9   TYR   B CE2  1 
ATOM   4179 C CZ   . TYR   B 1 9   ? 44.530 -25.515 -14.679 1.00 21.14 ?  9   TYR   B CZ   1 
ATOM   4180 O OH   . TYR   B 1 9   ? 45.497 -24.969 -13.869 1.00 21.80 ?  9   TYR   B OH   1 
ATOM   4181 H H    A TYR   B 1 9   ? 42.809 -27.522 -19.403 0.80 30.34 ?  9   TYR   B H    1 
ATOM   4182 H H    B TYR   B 1 9   ? 42.819 -27.517 -19.396 0.20 30.34 ?  9   TYR   B H    1 
ATOM   4183 H HA   . TYR   B 1 9   ? 42.484 -29.050 -17.216 1.00 27.02 ?  9   TYR   B HA   1 
ATOM   4184 H HB2  . TYR   B 1 9   ? 41.305 -26.594 -17.929 1.00 25.93 ?  9   TYR   B HB2  1 
ATOM   4185 H HB3  . TYR   B 1 9   ? 40.764 -27.458 -16.707 1.00 25.93 ?  9   TYR   B HB3  1 
ATOM   4186 H HD1  . TYR   B 1 9   ? 43.737 -25.853 -17.789 1.00 26.13 ?  9   TYR   B HD1  1 
ATOM   4187 H HD2  . TYR   B 1 9   ? 41.770 -27.217 -14.586 1.00 24.31 ?  9   TYR   B HD2  1 
ATOM   4188 H HE1  . TYR   B 1 9   ? 45.343 -24.934 -16.420 1.00 25.98 ?  9   TYR   B HE1  1 
ATOM   4189 H HE2  . TYR   B 1 9   ? 43.380 -26.296 -13.204 1.00 24.38 ?  9   TYR   B HE2  1 
ATOM   4190 H HH   . TYR   B 1 9   ? 46.069 -24.585 -14.341 1.00 26.16 ?  9   TYR   B HH   1 
ATOM   4191 N N    . LEU   B 1 10  ? 40.340 -30.179 -17.504 1.00 20.31 ?  10  LEU   B N    1 
ATOM   4192 C CA   . LEU   B 1 10  ? 39.130 -30.944 -17.748 1.00 20.26 ?  10  LEU   B CA   1 
ATOM   4193 C C    . LEU   B 1 10  ? 37.948 -30.160 -17.201 1.00 20.59 ?  10  LEU   B C    1 
ATOM   4194 O O    . LEU   B 1 10  ? 37.965 -29.723 -16.047 1.00 20.18 ?  10  LEU   B O    1 
ATOM   4195 C CB   . LEU   B 1 10  ? 39.222 -32.295 -17.038 1.00 21.88 ?  10  LEU   B CB   1 
ATOM   4196 C CG   . LEU   B 1 10  ? 38.088 -33.270 -17.341 1.00 23.83 ?  10  LEU   B CG   1 
ATOM   4197 C CD1  . LEU   B 1 10  ? 38.201 -33.783 -18.770 1.00 25.49 ?  10  LEU   B CD1  1 
ATOM   4198 C CD2  . LEU   B 1 10  ? 38.074 -34.424 -16.346 1.00 25.08 ?  10  LEU   B CD2  1 
ATOM   4199 H H    . LEU   B 1 10  ? 40.685 -30.329 -16.726 1.00 24.37 ?  10  LEU   B H    1 
ATOM   4200 H HA   . LEU   B 1 10  ? 39.007 -31.088 -18.696 1.00 24.31 ?  10  LEU   B HA   1 
ATOM   4201 H HB2  . LEU   B 1 10  ? 40.052 -32.724 -17.299 1.00 26.25 ?  10  LEU   B HB2  1 
ATOM   4202 H HB3  . LEU   B 1 10  ? 39.225 -32.143 -16.078 1.00 26.25 ?  10  LEU   B HB3  1 
ATOM   4203 H HG   . LEU   B 1 10  ? 37.241 -32.804 -17.260 1.00 28.59 ?  10  LEU   B HG   1 
ATOM   4204 H HD11 . LEU   B 1 10  ? 37.523 -34.458 -18.917 1.00 30.59 ?  10  LEU   B HD11 1 
ATOM   4205 H HD12 . LEU   B 1 10  ? 38.069 -33.040 -19.381 1.00 30.59 ?  10  LEU   B HD12 1 
ATOM   4206 H HD13 . LEU   B 1 10  ? 39.084 -34.163 -18.898 1.00 30.59 ?  10  LEU   B HD13 1 
ATOM   4207 H HD21 . LEU   B 1 10  ? 37.344 -35.022 -16.569 1.00 30.09 ?  10  LEU   B HD21 1 
ATOM   4208 H HD22 . LEU   B 1 10  ? 38.918 -34.895 -16.400 1.00 30.09 ?  10  LEU   B HD22 1 
ATOM   4209 H HD23 . LEU   B 1 10  ? 37.948 -34.066 -15.453 1.00 30.09 ?  10  LEU   B HD23 1 
ATOM   4210 N N    A LYS   B 1 11  ? 36.933 -29.975 -18.036 0.80 21.60 ?  11  LYS   B N    1 
ATOM   4211 N N    B LYS   B 1 11  ? 36.922 -29.997 -18.029 0.20 21.96 ?  11  LYS   B N    1 
ATOM   4212 C CA   A LYS   B 1 11  ? 35.727 -29.270 -17.632 0.80 24.27 ?  11  LYS   B CA   1 
ATOM   4213 C CA   B LYS   B 1 11  ? 35.722 -29.271 -17.636 0.20 23.62 ?  11  LYS   B CA   1 
ATOM   4214 C C    A LYS   B 1 11  ? 34.880 -30.196 -16.763 0.80 23.19 ?  11  LYS   B C    1 
ATOM   4215 C C    B LYS   B 1 11  ? 34.840 -30.176 -16.782 0.20 22.59 ?  11  LYS   B C    1 
ATOM   4216 O O    A LYS   B 1 11  ? 34.550 -31.314 -17.178 0.80 24.79 ?  11  LYS   B O    1 
ATOM   4217 O O    B LYS   B 1 11  ? 34.433 -31.254 -17.230 0.20 23.09 ?  11  LYS   B O    1 
ATOM   4218 C CB   A LYS   B 1 11  ? 34.962 -28.846 -18.886 0.80 28.43 ?  11  LYS   B CB   1 
ATOM   4219 C CB   B LYS   B 1 11  ? 34.973 -28.828 -18.891 0.20 26.36 ?  11  LYS   B CB   1 
ATOM   4220 C CG   A LYS   B 1 11  ? 33.854 -27.835 -18.662 0.80 32.14 ?  11  LYS   B CG   1 
ATOM   4221 C CG   B LYS   B 1 11  ? 33.824 -27.875 -18.636 0.20 28.78 ?  11  LYS   B CG   1 
ATOM   4222 C CD   A LYS   B 1 11  ? 33.161 -27.504 -19.981 0.80 35.01 ?  11  LYS   B CD   1 
ATOM   4223 C CD   B LYS   B 1 11  ? 33.064 -27.580 -19.920 0.20 30.74 ?  11  LYS   B CD   1 
ATOM   4224 C CE   A LYS   B 1 11  ? 32.146 -26.384 -19.824 0.80 37.02 ?  11  LYS   B CE   1 
ATOM   4225 C CE   B LYS   B 1 11  ? 32.068 -26.449 -19.727 0.20 32.08 ?  11  LYS   B CE   1 
ATOM   4226 N NZ   A LYS   B 1 11  ? 32.795 -25.075 -19.551 0.80 38.03 ?  11  LYS   B NZ   1 
ATOM   4227 N NZ   B LYS   B 1 11  ? 32.748 -25.155 -19.438 0.20 32.75 ?  11  LYS   B NZ   1 
ATOM   4228 H H    A LYS   B 1 11  ? 36.918 -30.250 -18.852 0.80 25.91 ?  11  LYS   B H    1 
ATOM   4229 H H    B LYS   B 1 11  ? 36.899 -30.298 -18.836 0.20 26.35 ?  11  LYS   B H    1 
ATOM   4230 H HA   A LYS   B 1 11  ? 35.958 -28.477 -17.124 0.80 29.13 ?  11  LYS   B HA   1 
ATOM   4231 H HA   B LYS   B 1 11  ? 35.964 -28.486 -17.121 0.20 28.34 ?  11  LYS   B HA   1 
ATOM   4232 H HB2  A LYS   B 1 11  ? 35.592 -28.450 -19.512 0.80 34.12 ?  11  LYS   B HB2  1 
ATOM   4233 H HB2  B LYS   B 1 11  ? 35.598 -28.381 -19.484 0.20 31.64 ?  11  LYS   B HB2  1 
ATOM   4234 H HB3  A LYS   B 1 11  ? 34.562 -29.632 -19.286 0.80 34.12 ?  11  LYS   B HB3  1 
ATOM   4235 H HB3  B LYS   B 1 11  ? 34.611 -29.613 -19.330 0.20 31.64 ?  11  LYS   B HB3  1 
ATOM   4236 H HG2  A LYS   B 1 11  ? 33.196 -28.207 -18.056 0.80 38.57 ?  11  LYS   B HG2  1 
ATOM   4237 H HG2  B LYS   B 1 11  ? 33.209 -28.275 -18.003 0.20 34.54 ?  11  LYS   B HG2  1 
ATOM   4238 H HG3  A LYS   B 1 11  ? 34.229 -27.018 -18.300 0.80 38.57 ?  11  LYS   B HG3  1 
ATOM   4239 H HG3  B LYS   B 1 11  ? 34.173 -27.040 -18.288 0.20 34.54 ?  11  LYS   B HG3  1 
ATOM   4240 H HD2  A LYS   B 1 11  ? 33.827 -27.221 -20.629 0.80 42.01 ?  11  LYS   B HD2  1 
ATOM   4241 H HD2  B LYS   B 1 11  ? 33.692 -27.318 -20.612 0.20 36.88 ?  11  LYS   B HD2  1 
ATOM   4242 H HD3  A LYS   B 1 11  ? 32.697 -28.293 -20.304 0.80 42.01 ?  11  LYS   B HD3  1 
ATOM   4243 H HD3  B LYS   B 1 11  ? 32.575 -28.373 -20.192 0.20 36.88 ?  11  LYS   B HD3  1 
ATOM   4244 H HE2  A LYS   B 1 11  ? 31.632 -26.303 -20.643 0.80 44.43 ?  11  LYS   B HE2  1 
ATOM   4245 H HE2  B LYS   B 1 11  ? 31.546 -26.342 -20.537 0.20 38.49 ?  11  LYS   B HE2  1 
ATOM   4246 H HE3  A LYS   B 1 11  ? 31.558 -26.593 -19.081 0.80 44.43 ?  11  LYS   B HE3  1 
ATOM   4247 H HE3  B LYS   B 1 11  ? 31.487 -26.662 -18.980 0.20 38.49 ?  11  LYS   B HE3  1 
ATOM   4248 H HZ1  A LYS   B 1 11  ? 32.177 -24.440 -19.472 0.80 45.64 ?  11  LYS   B HZ1  1 
ATOM   4249 H HZ1  B LYS   B 1 11  ? 32.148 -24.499 -19.401 0.20 39.30 ?  11  LYS   B HZ1  1 
ATOM   4250 H HZ2  A LYS   B 1 11  ? 33.264 -25.119 -18.797 0.80 45.64 ?  11  LYS   B HZ2  1 
ATOM   4251 H HZ2  B LYS   B 1 11  ? 33.174 -25.202 -18.658 0.20 39.30 ?  11  LYS   B HZ2  1 
ATOM   4252 H HZ3  A LYS   B 1 11  ? 33.343 -24.863 -20.221 0.80 45.64 ?  11  LYS   B HZ3  1 
ATOM   4253 H HZ3  B LYS   B 1 11  ? 33.337 -24.971 -20.079 0.20 39.30 ?  11  LYS   B HZ3  1 
ATOM   4254 N N    . LEU   B 1 12  ? 34.544 -29.742 -15.555 1.00 21.27 ?  12  LEU   B N    1 
ATOM   4255 C CA   . LEU   B 1 12  ? 33.606 -30.449 -14.686 1.00 20.07 ?  12  LEU   B CA   1 
ATOM   4256 C C    . LEU   B 1 12  ? 32.217 -29.841 -14.758 1.00 19.67 ?  12  LEU   B C    1 
ATOM   4257 O O    . LEU   B 1 12  ? 31.229 -30.560 -14.917 1.00 20.47 ?  12  LEU   B O    1 
ATOM   4258 C CB   . LEU   B 1 12  ? 34.081 -30.459 -13.227 1.00 19.26 ?  12  LEU   B CB   1 
ATOM   4259 C CG   . LEU   B 1 12  ? 35.410 -31.161 -12.954 1.00 18.82 ?  12  LEU   B CG   1 
ATOM   4260 C CD1  . LEU   B 1 12  ? 35.784 -31.087 -11.478 1.00 19.04 ?  12  LEU   B CD1  1 
ATOM   4261 C CD2  . LEU   B 1 12  ? 35.407 -32.610 -13.440 1.00 19.06 ?  12  LEU   B CD2  1 
ATOM   4262 H H    A LEU   B 1 12  ? 34.850 -29.013 -15.211 0.80 25.53 ?  12  LEU   B H    1 
ATOM   4263 H H    B LEU   B 1 12  ? 34.868 -29.024 -15.204 0.20 25.53 ?  12  LEU   B H    1 
ATOM   4264 H HA   . LEU   B 1 12  ? 33.529 -31.362 -14.986 1.00 24.08 ?  12  LEU   B HA   1 
ATOM   4265 H HB2  . LEU   B 1 12  ? 34.162 -29.543 -12.927 1.00 23.11 ?  12  LEU   B HB2  1 
ATOM   4266 H HB3  . LEU   B 1 12  ? 33.399 -30.910 -12.697 1.00 23.11 ?  12  LEU   B HB3  1 
ATOM   4267 H HG   . LEU   B 1 12  ? 36.098 -30.691 -13.445 1.00 22.58 ?  12  LEU   B HG   1 
ATOM   4268 H HD11 . LEU   B 1 12  ? 36.636 -31.537 -11.346 1.00 22.85 ?  12  LEU   B HD11 1 
ATOM   4269 H HD12 . LEU   B 1 12  ? 35.861 -30.156 -11.213 1.00 22.85 ?  12  LEU   B HD12 1 
ATOM   4270 H HD13 . LEU   B 1 12  ? 35.097 -31.524 -10.951 1.00 22.85 ?  12  LEU   B HD13 1 
ATOM   4271 H HD21 . LEU   B 1 12  ? 36.228 -33.037 -13.148 1.00 22.87 ?  12  LEU   B HD21 1 
ATOM   4272 H HD22 . LEU   B 1 12  ? 34.641 -33.068 -13.063 1.00 22.87 ?  12  LEU   B HD22 1 
ATOM   4273 H HD23 . LEU   B 1 12  ? 35.356 -32.616 -14.408 1.00 22.87 ?  12  LEU   B HD23 1 
ATOM   4274 N N    . THR   B 1 13  ? 32.126 -28.524 -14.632 1.00 19.70 ?  13  THR   B N    1 
ATOM   4275 C CA   . THR   B 1 13  ? 30.899 -27.781 -14.852 1.00 19.68 ?  13  THR   B CA   1 
ATOM   4276 C C    . THR   B 1 13  ? 31.242 -26.603 -15.755 1.00 22.19 ?  13  THR   B C    1 
ATOM   4277 O O    . THR   B 1 13  ? 32.387 -26.439 -16.188 1.00 23.06 ?  13  THR   B O    1 
ATOM   4278 C CB   . THR   B 1 13  ? 30.306 -27.276 -13.532 1.00 18.58 ?  13  THR   B CB   1 
ATOM   4279 O OG1  . THR   B 1 13  ? 31.157 -26.255 -13.003 1.00 18.33 ?  13  THR   B OG1  1 
ATOM   4280 C CG2  . THR   B 1 13  ? 30.183 -28.409 -12.517 1.00 19.06 ?  13  THR   B CG2  1 
ATOM   4281 H H    . THR   B 1 13  ? 32.788 -28.018 -14.405 1.00 23.65 ?  13  THR   B H    1 
ATOM   4282 H HA   . THR   B 1 13  ? 30.245 -28.343 -15.287 1.00 23.62 ?  13  THR   B HA   1 
ATOM   4283 H HB   . THR   B 1 13  ? 29.415 -26.909 -13.691 1.00 22.30 ?  13  THR   B HB   1 
ATOM   4284 H HG1  . THR   B 1 13  ? 30.817 -25.485 -13.155 1.00 21.99 ?  13  THR   B HG1  1 
ATOM   4285 H HG21 . THR   B 1 13  ? 29.704 -28.104 -11.729 1.00 22.88 ?  13  THR   B HG21 1 
ATOM   4286 H HG22 . THR   B 1 13  ? 29.700 -29.153 -12.908 1.00 22.88 ?  13  THR   B HG22 1 
ATOM   4287 H HG23 . THR   B 1 13  ? 31.065 -28.711 -12.250 1.00 22.88 ?  13  THR   B HG23 1 
ATOM   4288 N N    A ASP   B 1 14  ? 30.245 -25.766 -16.032 0.80 23.32 ?  14  ASP   B N    1 
ATOM   4289 N N    B ASP   B 1 14  ? 30.246 -25.756 -16.022 0.20 22.97 ?  14  ASP   B N    1 
ATOM   4290 C CA   A ASP   B 1 14  ? 30.489 -24.623 -16.902 0.80 24.99 ?  14  ASP   B CA   1 
ATOM   4291 C CA   B ASP   B 1 14  ? 30.467 -24.613 -16.900 0.20 23.82 ?  14  ASP   B CA   1 
ATOM   4292 C C    A ASP   B 1 14  ? 31.582 -23.714 -16.356 0.80 23.05 ?  14  ASP   B C    1 
ATOM   4293 C C    B ASP   B 1 14  ? 31.470 -23.619 -16.333 0.20 22.04 ?  14  ASP   B C    1 
ATOM   4294 O O    A ASP   B 1 14  ? 32.249 -23.022 -17.135 0.80 25.01 ?  14  ASP   B O    1 
ATOM   4295 O O    B ASP   B 1 14  ? 31.950 -22.758 -17.078 0.20 22.29 ?  14  ASP   B O    1 
ATOM   4296 C CB   A ASP   B 1 14  ? 29.201 -23.828 -17.114 0.80 28.64 ?  14  ASP   B CB   1 
ATOM   4297 C CB   B ASP   B 1 14  ? 29.151 -23.889 -17.183 0.20 26.37 ?  14  ASP   B CB   1 
ATOM   4298 C CG   A ASP   B 1 14  ? 28.228 -24.528 -18.036 0.80 32.67 ?  14  ASP   B CG   1 
ATOM   4299 C CG   B ASP   B 1 14  ? 28.255 -24.657 -18.137 0.20 28.75 ?  14  ASP   B CG   1 
ATOM   4300 O OD1  A ASP   B 1 14  ? 28.656 -25.379 -18.849 0.80 34.03 ?  14  ASP   B OD1  1 
ATOM   4301 O OD1  B ASP   B 1 14  ? 28.786 -25.371 -19.014 0.20 29.59 ?  14  ASP   B OD1  1 
ATOM   4302 O OD2  A ASP   B 1 14  ? 27.022 -24.225 -17.950 0.80 34.29 -1 14  ASP   B OD2  1 
ATOM   4303 O OD2  B ASP   B 1 14  ? 27.018 -24.549 -18.009 0.20 29.53 -1 14  ASP   B OD2  1 
ATOM   4304 H H    A ASP   B 1 14  ? 29.441 -25.830 -15.732 0.80 27.98 ?  14  ASP   B H    1 
ATOM   4305 H H    B ASP   B 1 14  ? 29.446 -25.820 -15.714 0.20 27.56 ?  14  ASP   B H    1 
ATOM   4306 H HA   A ASP   B 1 14  ? 30.785 -24.941 -17.765 0.80 29.99 ?  14  ASP   B HA   1 
ATOM   4307 H HA   B ASP   B 1 14  ? 30.815 -24.932 -17.745 0.20 28.58 ?  14  ASP   B HA   1 
ATOM   4308 H HB2  A ASP   B 1 14  ? 28.756 -23.705 -16.262 0.80 34.37 ?  14  ASP   B HB2  1 
ATOM   4309 H HB2  B ASP   B 1 14  ? 28.671 -23.772 -16.349 0.20 31.64 ?  14  ASP   B HB2  1 
ATOM   4310 H HB3  A ASP   B 1 14  ? 29.418 -22.965 -17.502 0.80 34.37 ?  14  ASP   B HB3  1 
ATOM   4311 H HB3  B ASP   B 1 14  ? 29.350 -23.019 -17.573 0.20 31.64 ?  14  ASP   B HB3  1 
ATOM   4312 N N    . ASN   B 1 15  ? 31.782 -23.693 -15.036 1.00 20.32 ?  15  ASN   B N    1 
ATOM   4313 C CA   . ASN   B 1 15  ? 32.747 -22.775 -14.430 1.00 17.75 ?  15  ASN   B CA   1 
ATOM   4314 C C    . ASN   B 1 15  ? 33.844 -23.428 -13.597 1.00 16.10 ?  15  ASN   B C    1 
ATOM   4315 O O    . ASN   B 1 15  ? 34.714 -22.709 -13.094 1.00 16.10 ?  15  ASN   B O    1 
ATOM   4316 C CB   . ASN   B 1 15  ? 32.037 -21.721 -13.565 1.00 17.51 ?  15  ASN   B CB   1 
ATOM   4317 C CG   . ASN   B 1 15  ? 31.418 -22.323 -12.321 1.00 17.18 ?  15  ASN   B CG   1 
ATOM   4318 O OD1  . ASN   B 1 15  ? 30.465 -23.105 -12.406 1.00 19.68 ?  15  ASN   B OD1  1 
ATOM   4319 N ND2  . ASN   B 1 15  ? 31.962 -21.991 -11.166 1.00 16.26 ?  15  ASN   B ND2  1 
ATOM   4320 H H    A ASN   B 1 15  ? 31.364 -24.191 -14.469 0.80 24.38 ?  15  ASN   B H    1 
ATOM   4321 H H    B ASN   B 1 15  ? 31.425 -24.246 -14.480 0.20 24.38 ?  15  ASN   B H    1 
ATOM   4322 H HA   . ASN   B 1 15  ? 33.194 -22.290 -15.132 1.00 21.30 ?  15  ASN   B HA   1 
ATOM   4323 H HB2  . ASN   B 1 15  ? 32.686 -21.043 -13.289 1.00 21.02 ?  15  ASN   B HB2  1 
ATOM   4324 H HB3  . ASN   B 1 15  ? 31.332 -21.294 -14.084 1.00 21.02 ?  15  ASN   B HB3  1 
ATOM   4325 H HD21 . ASN   B 1 15  ? 31.641 -22.299 -10.432 1.00 19.51 ?  15  ASN   B HD21 1 
ATOM   4326 H HD22 . ASN   B 1 15  ? 32.644 -21.453 -11.137 1.00 19.51 ?  15  ASN   B HD22 1 
ATOM   4327 N N    . VAL   B 1 16  ? 33.828 -24.747 -13.413 1.00 15.99 ?  16  VAL   B N    1 
ATOM   4328 C CA   . VAL   B 1 16  ? 34.834 -25.440 -12.609 1.00 15.58 ?  16  VAL   B CA   1 
ATOM   4329 C C    . VAL   B 1 16  ? 35.617 -26.378 -13.511 1.00 15.65 ?  16  VAL   B C    1 
ATOM   4330 O O    . VAL   B 1 16  ? 35.033 -27.260 -14.163 1.00 16.71 ?  16  VAL   B O    1 
ATOM   4331 C CB   . VAL   B 1 16  ? 34.213 -26.207 -11.432 1.00 15.52 ?  16  VAL   B CB   1 
ATOM   4332 C CG1  . VAL   B 1 16  ? 35.300 -26.962 -10.651 1.00 15.34 ?  16  VAL   B CG1  1 
ATOM   4333 C CG2  . VAL   B 1 16  ? 33.428 -25.258 -10.536 1.00 16.28 ?  16  VAL   B CG2  1 
ATOM   4334 H H    . VAL   B 1 16  ? 33.221 -25.274 -13.741 1.00 19.18 ?  16  VAL   B H    1 
ATOM   4335 H HA   . VAL   B 1 16  ? 35.443 -24.789 -12.246 1.00 18.69 ?  16  VAL   B HA   1 
ATOM   4336 H HB   . VAL   B 1 16  ? 33.589 -26.870 -11.779 1.00 18.62 ?  16  VAL   B HB   1 
ATOM   4337 H HG11 . VAL   B 1 16  ? 34.925 -27.270 -9.809  1.00 18.40 ?  16  VAL   B HG11 1 
ATOM   4338 H HG12 . VAL   B 1 16  ? 35.603 -27.719 -11.173 1.00 18.40 ?  16  VAL   B HG12 1 
ATOM   4339 H HG13 . VAL   B 1 16  ? 36.038 -26.356 -10.478 1.00 18.40 ?  16  VAL   B HG13 1 
ATOM   4340 H HG21 . VAL   B 1 16  ? 33.103 -25.748 -9.764  1.00 19.54 ?  16  VAL   B HG21 1 
ATOM   4341 H HG22 . VAL   B 1 16  ? 34.012 -24.540 -10.253 1.00 19.54 ?  16  VAL   B HG22 1 
ATOM   4342 H HG23 . VAL   B 1 16  ? 32.679 -24.898 -11.038 1.00 19.54 ?  16  VAL   B HG23 1 
ATOM   4343 N N    . TYR   B 1 17  ? 36.938 -26.211 -13.498 1.00 16.21 ?  17  TYR   B N    1 
ATOM   4344 C CA   . TYR   B 1 17  ? 37.882 -26.962 -14.311 1.00 16.57 ?  17  TYR   B CA   1 
ATOM   4345 C C    . TYR   B 1 17  ? 38.938 -27.577 -13.401 1.00 15.42 ?  17  TYR   B C    1 
ATOM   4346 O O    . TYR   B 1 17  ? 39.231 -27.049 -12.324 1.00 15.52 ?  17  TYR   B O    1 
ATOM   4347 C CB   . TYR   B 1 17  ? 38.579 -26.037 -15.324 1.00 20.01 ?  17  TYR   B CB   1 
ATOM   4348 C CG   . TYR   B 1 17  ? 37.648 -25.280 -16.244 1.00 24.08 ?  17  TYR   B CG   1 
ATOM   4349 C CD1  . TYR   B 1 17  ? 37.062 -24.087 -15.848 1.00 26.38 ?  17  TYR   B CD1  1 
ATOM   4350 C CD2  . TYR   B 1 17  ? 37.361 -25.761 -17.517 1.00 26.89 ?  17  TYR   B CD2  1 
ATOM   4351 C CE1  . TYR   B 1 17  ? 36.211 -23.391 -16.692 1.00 28.63 ?  17  TYR   B CE1  1 
ATOM   4352 C CE2  . TYR   B 1 17  ? 36.516 -25.074 -18.368 1.00 28.93 ?  17  TYR   B CE2  1 
ATOM   4353 C CZ   . TYR   B 1 17  ? 35.939 -23.891 -17.949 1.00 29.99 ?  17  TYR   B CZ   1 
ATOM   4354 O OH   . TYR   B 1 17  ? 35.099 -23.206 -18.794 1.00 31.17 ?  17  TYR   B OH   1 
ATOM   4355 H H    . TYR   B 1 17  ? 37.333 -25.626 -12.995 1.00 19.46 ?  17  TYR   B H    1 
ATOM   4356 H HA   . TYR   B 1 17  ? 37.413 -27.665 -14.790 1.00 19.88 ?  17  TYR   B HA   1 
ATOM   4357 H HB2  . TYR   B 1 17  ? 39.112 -25.389 -14.842 1.00 24.01 ?  17  TYR   B HB2  1 
ATOM   4358 H HB3  . TYR   B 1 17  ? 39.147 -26.581 -15.883 1.00 24.01 ?  17  TYR   B HB3  1 
ATOM   4359 H HD1  . TYR   B 1 17  ? 37.239 -23.748 -15.002 1.00 31.65 ?  17  TYR   B HD1  1 
ATOM   4360 H HD2  . TYR   B 1 17  ? 37.745 -26.557 -17.803 1.00 32.27 ?  17  TYR   B HD2  1 
ATOM   4361 H HE1  . TYR   B 1 17  ? 35.822 -22.593 -16.414 1.00 34.36 ?  17  TYR   B HE1  1 
ATOM   4362 H HE2  . TYR   B 1 17  ? 36.330 -25.408 -19.218 1.00 34.71 ?  17  TYR   B HE2  1 
ATOM   4363 H HH   . TYR   B 1 17  ? 35.024 -23.619 -19.522 1.00 37.40 ?  17  TYR   B HH   1 
ATOM   4364 N N    . ILE   B 1 18  ? 39.542 -28.682 -13.840 1.00 15.86 ?  18  ILE   B N    1 
ATOM   4365 C CA   . ILE   B 1 18  ? 40.474 -29.412 -12.987 1.00 15.93 ?  18  ILE   B CA   1 
ATOM   4366 C C    . ILE   B 1 18  ? 41.627 -29.965 -13.816 1.00 16.34 ?  18  ILE   B C    1 
ATOM   4367 O O    . ILE   B 1 18  ? 41.461 -30.350 -14.977 1.00 17.40 ?  18  ILE   B O    1 
ATOM   4368 C CB   . ILE   B 1 18  ? 39.736 -30.519 -12.184 1.00 15.99 ?  18  ILE   B CB   1 
ATOM   4369 C CG1  . ILE   B 1 18  ? 40.611 -31.062 -11.049 1.00 16.20 ?  18  ILE   B CG1  1 
ATOM   4370 C CG2  . ILE   B 1 18  ? 39.246 -31.643 -13.110 1.00 16.16 ?  18  ILE   B CG2  1 
ATOM   4371 C CD1  . ILE   B 1 18  ? 39.832 -31.905 -10.045 1.00 17.68 ?  18  ILE   B CD1  1 
ATOM   4372 H H    . ILE   B 1 18  ? 39.428 -29.018 -14.615 1.00 19.03 ?  18  ILE   B H    1 
ATOM   4373 H HA   . ILE   B 1 18  ? 40.840 -28.790 -12.334 1.00 19.12 ?  18  ILE   B HA   1 
ATOM   4374 H HB   . ILE   B 1 18  ? 38.951 -30.124 -11.772 1.00 19.19 ?  18  ILE   B HB   1 
ATOM   4375 H HG12 . ILE   B 1 18  ? 41.311 -31.615 -11.424 1.00 19.44 ?  18  ILE   B HG12 1 
ATOM   4376 H HG13 . ILE   B 1 18  ? 41.000 -30.313 -10.567 1.00 19.44 ?  18  ILE   B HG13 1 
ATOM   4377 H HG21 . ILE   B 1 18  ? 38.656 -32.235 -12.611 1.00 19.39 ?  18  ILE   B HG21 1 
ATOM   4378 H HG22 . ILE   B 1 18  ? 38.761 -31.250 -13.853 1.00 19.39 ?  18  ILE   B HG22 1 
ATOM   4379 H HG23 . ILE   B 1 18  ? 40.008 -32.143 -13.440 1.00 19.39 ?  18  ILE   B HG23 1 
ATOM   4380 H HD11 . ILE   B 1 18  ? 40.429 -32.177 -9.328  1.00 21.21 ?  18  ILE   B HD11 1 
ATOM   4381 H HD12 . ILE   B 1 18  ? 39.103 -31.378 -9.683  1.00 21.21 ?  18  ILE   B HD12 1 
ATOM   4382 H HD13 . ILE   B 1 18  ? 39.481 -32.690 -10.495 1.00 21.21 ?  18  ILE   B HD13 1 
ATOM   4383 N N    . LYS   B 1 19  ? 42.808 -30.015 -13.199 1.00 16.82 ?  19  LYS   B N    1 
ATOM   4384 C CA   . LYS   B 1 19  ? 44.017 -30.482 -13.857 1.00 17.73 ?  19  LYS   B CA   1 
ATOM   4385 C C    . LYS   B 1 19  ? 44.911 -31.176 -12.839 1.00 17.31 ?  19  LYS   B C    1 
ATOM   4386 O O    . LYS   B 1 19  ? 44.996 -30.753 -11.683 1.00 16.37 ?  19  LYS   B O    1 
ATOM   4387 C CB   . LYS   B 1 19  ? 44.789 -29.308 -14.468 1.00 19.13 ?  19  LYS   B CB   1 
ATOM   4388 C CG   . LYS   B 1 19  ? 45.951 -29.715 -15.346 1.00 21.44 ?  19  LYS   B CG   1 
ATOM   4389 C CD   . LYS   B 1 19  ? 46.653 -28.486 -15.902 1.00 23.86 ?  19  LYS   B CD   1 
ATOM   4390 C CE   . LYS   B 1 19  ? 47.814 -28.855 -16.801 1.00 26.11 ?  19  LYS   B CE   1 
ATOM   4391 N NZ   . LYS   B 1 19  ? 48.495 -27.644 -17.331 1.00 27.34 ?  19  LYS   B NZ   1 
ATOM   4392 H H    . LYS   B 1 19  ? 42.916 -29.780 -12.381 1.00 20.18 ?  19  LYS   B H    1 
ATOM   4393 H HA   . LYS   B 1 19  ? 43.777 -31.106 -14.563 1.00 21.27 ?  19  LYS   B HA   1 
ATOM   4394 H HB2  . LYS   B 1 19  ? 44.179 -28.787 -15.012 1.00 22.95 ?  19  LYS   B HB2  1 
ATOM   4395 H HB3  . LYS   B 1 19  ? 45.132 -28.756 -13.743 1.00 22.95 ?  19  LYS   B HB3  1 
ATOM   4396 H HG2  . LYS   B 1 19  ? 46.584 -30.227 -14.821 1.00 25.73 ?  19  LYS   B HG2  1 
ATOM   4397 H HG3  . LYS   B 1 19  ? 45.616 -30.246 -16.087 1.00 25.73 ?  19  LYS   B HG3  1 
ATOM   4398 H HD2  . LYS   B 1 19  ? 46.017 -27.965 -16.419 1.00 28.63 ?  19  LYS   B HD2  1 
ATOM   4399 H HD3  . LYS   B 1 19  ? 46.993 -27.955 -15.163 1.00 28.63 ?  19  LYS   B HD3  1 
ATOM   4400 H HE2  . LYS   B 1 19  ? 48.460 -29.371 -16.293 1.00 31.34 ?  19  LYS   B HE2  1 
ATOM   4401 H HE3  . LYS   B 1 19  ? 47.485 -29.375 -17.551 1.00 31.34 ?  19  LYS   B HE3  1 
ATOM   4402 H HZ1  . LYS   B 1 19  ? 49.143 -27.879 -17.894 1.00 32.81 ?  19  LYS   B HZ1  1 
ATOM   4403 H HZ2  . LYS   B 1 19  ? 47.910 -27.130 -17.765 1.00 32.81 ?  19  LYS   B HZ2  1 
ATOM   4404 H HZ3  . LYS   B 1 19  ? 48.849 -27.175 -16.663 1.00 32.81 ?  19  LYS   B HZ3  1 
ATOM   4405 N N    . ASN   B 1 20  ? 45.601 -32.222 -13.280 1.00 19.16 ?  20  ASN   B N    1 
ATOM   4406 C CA   . ASN   B 1 20  ? 46.619 -32.869 -12.453 1.00 20.38 ?  20  ASN   B CA   1 
ATOM   4407 C C    . ASN   B 1 20  ? 47.902 -32.064 -12.627 1.00 20.86 ?  20  ASN   B C    1 
ATOM   4408 O O    . ASN   B 1 20  ? 48.547 -32.137 -13.677 1.00 23.02 ?  20  ASN   B O    1 
ATOM   4409 C CB   . ASN   B 1 20  ? 46.775 -34.327 -12.886 1.00 22.43 ?  20  ASN   B CB   1 
ATOM   4410 C CG   . ASN   B 1 20  ? 47.929 -35.049 -12.197 1.00 24.07 ?  20  ASN   B CG   1 
ATOM   4411 O OD1  . ASN   B 1 20  ? 48.582 -35.906 -12.806 1.00 26.50 ?  20  ASN   B OD1  1 
ATOM   4412 N ND2  . ASN   B 1 20  ? 48.171 -34.738 -10.930 1.00 23.64 ?  20  ASN   B ND2  1 
ATOM   4413 H H    . ASN   B 1 20  ? 45.496 -32.573 -14.061 1.00 22.99 ?  20  ASN   B H    1 
ATOM   4414 H HA   . ASN   B 1 20  ? 46.334 -32.842 -11.524 1.00 24.46 ?  20  ASN   B HA   1 
ATOM   4415 H HB2  . ASN   B 1 20  ? 45.950 -34.804 -12.679 1.00 26.91 ?  20  ASN   B HB2  1 
ATOM   4416 H HB3  . ASN   B 1 20  ? 46.931 -34.350 -13.842 1.00 26.91 ?  20  ASN   B HB3  1 
ATOM   4417 H HD21 . ASN   B 1 20  ? 48.812 -35.124 -10.507 1.00 28.36 ?  20  ASN   B HD21 1 
ATOM   4418 H HD22 . ASN   B 1 20  ? 47.695 -34.140 -10.528 1.00 28.36 ?  20  ASN   B HD22 1 
ATOM   4419 N N    . ALA   B 1 21  ? 48.265 -31.268 -11.616 1.00 20.09 ?  21  ALA   B N    1 
ATOM   4420 C CA   . ALA   B 1 21  ? 49.384 -30.354 -11.770 1.00 20.60 ?  21  ALA   B CA   1 
ATOM   4421 C C    . ALA   B 1 21  ? 49.848 -29.837 -10.417 1.00 19.35 ?  21  ALA   B C    1 
ATOM   4422 O O    . ALA   B 1 21  ? 49.108 -29.856 -9.428  1.00 19.15 ?  21  ALA   B O    1 
ATOM   4423 C CB   . ALA   B 1 21  ? 49.011 -29.191 -12.688 1.00 22.49 ?  21  ALA   B CB   1 
ATOM   4424 H H    . ALA   B 1 21  ? 47.873 -31.246 -10.839 1.00 24.10 ?  21  ALA   B H    1 
ATOM   4425 H HA   . ALA   B 1 21  ? 50.117 -30.837 -12.172 1.00 24.72 ?  21  ALA   B HA   1 
ATOM   4426 H HB1  . ALA   B 1 21  ? 49.807 -28.670 -12.852 1.00 26.98 ?  21  ALA   B HB1  1 
ATOM   4427 H HB2  . ALA   B 1 21  ? 48.671 -29.554 -13.520 1.00 26.98 ?  21  ALA   B HB2  1 
ATOM   4428 H HB3  . ALA   B 1 21  ? 48.331 -28.654 -12.256 1.00 26.98 ?  21  ALA   B HB3  1 
ATOM   4429 N N    . ASP   B 1 22  ? 51.104 -29.380 -10.411 1.00 18.19 ?  22  ASP   B N    1 
ATOM   4430 C CA   . ASP   B 1 22  ? 51.735 -28.690 -9.290  1.00 17.51 ?  22  ASP   B CA   1 
ATOM   4431 C C    . ASP   B 1 22  ? 51.327 -27.221 -9.363  1.00 15.58 ?  22  ASP   B C    1 
ATOM   4432 O O    . ASP   B 1 22  ? 51.629 -26.544 -10.351 1.00 16.26 ?  22  ASP   B O    1 
ATOM   4433 C CB   . ASP   B 1 22  ? 53.253 -28.853 -9.465  1.00 18.93 ?  22  ASP   B CB   1 
ATOM   4434 C CG   . ASP   B 1 22  ? 54.087 -28.106 -8.432  1.00 20.50 ?  22  ASP   B CG   1 
ATOM   4435 O OD1  . ASP   B 1 22  ? 53.728 -26.989 -8.027  1.00 20.02 ?  22  ASP   B OD1  1 
ATOM   4436 O OD2  . ASP   B 1 22  ? 55.153 -28.638 -8.053  1.00 23.36 -1 22  ASP   B OD2  1 
ATOM   4437 H H    . ASP   B 1 22  ? 51.638 -29.466 -11.084 1.00 21.83 ?  22  ASP   B H    1 
ATOM   4438 H HA   . ASP   B 1 22  ? 51.458 -29.073 -8.442  1.00 21.02 ?  22  ASP   B HA   1 
ATOM   4439 H HB2  . ASP   B 1 22  ? 53.481 -29.789 -9.402  1.00 22.72 ?  22  ASP   B HB2  1 
ATOM   4440 H HB3  . ASP   B 1 22  ? 53.507 -28.504 -10.333 1.00 22.72 ?  22  ASP   B HB3  1 
ATOM   4441 N N    . ILE   B 1 23  ? 50.618 -26.732 -8.335  1.00 14.78 ?  23  ILE   B N    1 
ATOM   4442 C CA   . ILE   B 1 23  ? 50.034 -25.387 -8.401  1.00 13.96 ?  23  ILE   B CA   1 
ATOM   4443 C C    . ILE   B 1 23  ? 51.098 -24.307 -8.547  1.00 13.72 ?  23  ILE   B C    1 
ATOM   4444 O O    . ILE   B 1 23  ? 50.838 -23.264 -9.158  1.00 13.28 ?  23  ILE   B O    1 
ATOM   4445 C CB   . ILE   B 1 23  ? 49.103 -25.122 -7.203  1.00 14.27 ?  23  ILE   B CB   1 
ATOM   4446 C CG1  . ILE   B 1 23  ? 48.293 -23.842 -7.409  1.00 15.01 ?  23  ILE   B CG1  1 
ATOM   4447 C CG2  . ILE   B 1 23  ? 49.872 -25.087 -5.903  1.00 15.07 ?  23  ILE   B CG2  1 
ATOM   4448 C CD1  . ILE   B 1 23  ? 47.160 -23.664 -6.399  1.00 15.66 ?  23  ILE   B CD1  1 
ATOM   4449 H H    . ILE   B 1 23  ? 50.466 -27.153 -7.604  1.00 17.73 ?  23  ILE   B H    1 
ATOM   4450 H HA   . ILE   B 1 23  ? 49.486 -25.340 -9.195  1.00 16.75 ?  23  ILE   B HA   1 
ATOM   4451 H HB   . ILE   B 1 23  ? 48.474 -25.859 -7.154  1.00 17.13 ?  23  ILE   B HB   1 
ATOM   4452 H HG12 . ILE   B 1 23  ? 48.894 -23.078 -7.322  1.00 18.01 ?  23  ILE   B HG12 1 
ATOM   4453 H HG13 . ILE   B 1 23  ? 47.909 -23.852 -8.298  1.00 18.01 ?  23  ILE   B HG13 1 
ATOM   4454 H HG21 . ILE   B 1 23  ? 49.244 -25.078 -5.165  1.00 18.09 ?  23  ILE   B HG21 1 
ATOM   4455 H HG22 . ILE   B 1 23  ? 50.436 -25.873 -5.849  1.00 18.09 ?  23  ILE   B HG22 1 
ATOM   4456 H HG23 . ILE   B 1 23  ? 50.420 -24.286 -5.882  1.00 18.09 ?  23  ILE   B HG23 1 
ATOM   4457 H HD11 . ILE   B 1 23  ? 46.655 -22.872 -6.636  1.00 18.80 ?  23  ILE   B HD11 1 
ATOM   4458 H HD12 . ILE   B 1 23  ? 46.591 -24.446 -6.435  1.00 18.80 ?  23  ILE   B HD12 1 
ATOM   4459 H HD13 . ILE   B 1 23  ? 47.541 -23.566 -5.515  1.00 18.80 ?  23  ILE   B HD13 1 
ATOM   4460 N N    . VAL   B 1 24  ? 52.293 -24.514 -7.985  1.00 14.31 ?  24  VAL   B N    1 
ATOM   4461 C CA   . VAL   B 1 24  ? 53.365 -23.532 -8.144  1.00 14.88 ?  24  VAL   B CA   1 
ATOM   4462 C C    . VAL   B 1 24  ? 53.822 -23.483 -9.593  1.00 15.14 ?  24  VAL   B C    1 
ATOM   4463 O O    . VAL   B 1 24  ? 53.957 -22.405 -10.186 1.00 15.59 ?  24  VAL   B O    1 
ATOM   4464 C CB   . VAL   B 1 24  ? 54.539 -23.856 -7.200  1.00 15.30 ?  24  VAL   B CB   1 
ATOM   4465 C CG1  . VAL   B 1 24  ? 55.755 -22.977 -7.530  1.00 16.67 ?  24  VAL   B CG1  1 
ATOM   4466 C CG2  . VAL   B 1 24  ? 54.125 -23.677 -5.755  1.00 16.12 ?  24  VAL   B CG2  1 
ATOM   4467 H H    . VAL   B 1 24  ? 52.511 -25.203 -7.520  1.00 17.17 ?  24  VAL   B H    1 
ATOM   4468 H HA   . VAL   B 1 24  ? 53.034 -22.655 -7.905  1.00 17.85 ?  24  VAL   B HA   1 
ATOM   4469 H HB   . VAL   B 1 24  ? 54.804 -24.783 -7.321  1.00 18.36 ?  24  VAL   B HB   1 
ATOM   4470 H HG11 . VAL   B 1 24  ? 56.363 -22.980 -6.771  1.00 20.00 ?  24  VAL   B HG11 1 
ATOM   4471 H HG12 . VAL   B 1 24  ? 56.206 -23.333 -8.310  1.00 20.00 ?  24  VAL   B HG12 1 
ATOM   4472 H HG13 . VAL   B 1 24  ? 55.452 -22.072 -7.702  1.00 20.00 ?  24  VAL   B HG13 1 
ATOM   4473 H HG21 . VAL   B 1 24  ? 54.856 -23.953 -5.179  1.00 19.34 ?  24  VAL   B HG21 1 
ATOM   4474 H HG22 . VAL   B 1 24  ? 53.922 -22.741 -5.602  1.00 19.34 ?  24  VAL   B HG22 1 
ATOM   4475 H HG23 . VAL   B 1 24  ? 53.343 -24.220 -5.582  1.00 19.34 ?  24  VAL   B HG23 1 
ATOM   4476 N N    A GLU   B 1 25  ? 54.099 -24.651 -10.178 0.80 15.94 ?  25  GLU   B N    1 
ATOM   4477 N N    B GLU   B 1 25  ? 54.072 -24.651 -10.188 0.20 16.77 ?  25  GLU   B N    1 
ATOM   4478 C CA   A GLU   B 1 25  ? 54.489 -24.684 -11.582 0.80 17.54 ?  25  GLU   B CA   1 
ATOM   4479 C CA   B GLU   B 1 25  ? 54.467 -24.689 -11.592 0.20 18.61 ?  25  GLU   B CA   1 
ATOM   4480 C C    A GLU   B 1 25  ? 53.375 -24.154 -12.470 0.80 15.75 ?  25  GLU   B C    1 
ATOM   4481 C C    B GLU   B 1 25  ? 53.346 -24.192 -12.495 0.20 17.95 ?  25  GLU   B C    1 
ATOM   4482 O O    A GLU   B 1 25  ? 53.638 -23.425 -13.436 0.80 16.92 ?  25  GLU   B O    1 
ATOM   4483 O O    B GLU   B 1 25  ? 53.604 -23.543 -13.516 0.20 18.27 ?  25  GLU   B O    1 
ATOM   4484 C CB   A GLU   B 1 25  ? 54.905 -26.097 -11.982 0.80 21.81 ?  25  GLU   B CB   1 
ATOM   4485 C CB   B GLU   B 1 25  ? 54.900 -26.104 -11.977 0.20 21.30 ?  25  GLU   B CB   1 
ATOM   4486 C CG   A GLU   B 1 25  ? 56.197 -26.543 -11.307 0.80 27.31 ?  25  GLU   B CG   1 
ATOM   4487 C CG   B GLU   B 1 25  ? 56.178 -26.555 -11.284 0.20 24.15 ?  25  GLU   B CG   1 
ATOM   4488 C CD   A GLU   B 1 25  ? 57.305 -25.497 -11.374 0.80 32.09 ?  25  GLU   B CD   1 
ATOM   4489 C CD   B GLU   B 1 25  ? 57.344 -25.613 -11.519 0.20 26.67 ?  25  GLU   B CD   1 
ATOM   4490 O OE1  A GLU   B 1 25  ? 57.722 -25.134 -12.496 0.80 33.90 ?  25  GLU   B OE1  1 
ATOM   4491 O OE1  B GLU   B 1 25  ? 57.689 -25.381 -12.697 0.20 27.63 ?  25  GLU   B OE1  1 
ATOM   4492 O OE2  A GLU   B 1 25  ? 57.753 -25.019 -10.305 0.80 33.51 -1 25  GLU   B OE2  1 
ATOM   4493 O OE2  B GLU   B 1 25  ? 57.912 -25.098 -10.530 0.20 27.45 -1 25  GLU   B OE2  1 
ATOM   4494 H H    A GLU   B 1 25  ? 54.069 -25.417 -9.791  0.80 19.13 ?  25  GLU   B H    1 
ATOM   4495 H H    B GLU   B 1 25  ? 54.028 -25.418 -9.805  0.20 20.12 ?  25  GLU   B H    1 
ATOM   4496 H HA   A GLU   B 1 25  ? 55.240 -24.088 -11.708 0.80 21.05 ?  25  GLU   B HA   1 
ATOM   4497 H HA   B GLU   B 1 25  ? 55.221 -24.096 -11.721 0.20 22.33 ?  25  GLU   B HA   1 
ATOM   4498 H HB2  A GLU   B 1 25  ? 54.204 -26.718 -11.727 0.80 26.17 ?  25  GLU   B HB2  1 
ATOM   4499 H HB2  B GLU   B 1 25  ? 54.195 -26.726 -11.733 0.20 25.56 ?  25  GLU   B HB2  1 
ATOM   4500 H HB3  A GLU   B 1 25  ? 55.039 -26.127 -12.943 0.80 26.17 ?  25  GLU   B HB3  1 
ATOM   4501 H HB3  B GLU   B 1 25  ? 55.051 -26.137 -12.934 0.20 25.56 ?  25  GLU   B HB3  1 
ATOM   4502 H HG2  A GLU   B 1 25  ? 56.022 -26.718 -10.374 0.80 32.77 ?  25  GLU   B HG2  1 
ATOM   4503 H HG2  B GLU   B 1 25  ? 56.016 -26.612 -10.331 0.20 28.98 ?  25  GLU   B HG2  1 
ATOM   4504 H HG3  A GLU   B 1 25  ? 56.520 -27.345 -11.748 0.80 32.77 ?  25  GLU   B HG3  1 
ATOM   4505 H HG3  B GLU   B 1 25  ? 56.439 -27.418 -11.635 0.20 28.98 ?  25  GLU   B HG3  1 
ATOM   4506 N N    A GLU   B 1 26  ? 52.122 -24.489 -12.144 0.80 14.95 ?  26  GLU   B N    1 
ATOM   4507 N N    B GLU   B 1 26  ? 52.092 -24.481 -12.137 0.20 17.44 ?  26  GLU   B N    1 
ATOM   4508 C CA   A GLU   B 1 26  ? 50.991 -23.961 -12.902 0.80 16.58 ?  26  GLU   B CA   1 
ATOM   4509 C CA   B GLU   B 1 26  ? 50.971 -23.953 -12.908 0.20 17.27 ?  26  GLU   B CA   1 
ATOM   4510 C C    A GLU   B 1 26  ? 50.948 -22.442 -12.834 0.80 15.27 ?  26  GLU   B C    1 
ATOM   4511 C C    B GLU   B 1 26  ? 50.928 -22.435 -12.835 0.20 15.69 ?  26  GLU   B C    1 
ATOM   4512 O O    A GLU   B 1 26  ? 50.756 -21.772 -13.852 0.80 16.48 ?  26  GLU   B O    1 
ATOM   4513 O O    B GLU   B 1 26  ? 50.730 -21.758 -13.850 0.20 15.94 ?  26  GLU   B O    1 
ATOM   4514 C CB   A GLU   B 1 26  ? 49.675 -24.542 -12.378 0.80 18.51 ?  26  GLU   B CB   1 
ATOM   4515 C CB   B GLU   B 1 26  ? 49.652 -24.541 -12.405 0.20 18.42 ?  26  GLU   B CB   1 
ATOM   4516 C CG   A GLU   B 1 26  ? 49.222 -25.809 -13.075 0.80 22.48 ?  26  GLU   B CG   1 
ATOM   4517 C CG   B GLU   B 1 26  ? 49.254 -25.830 -13.088 0.20 20.02 ?  26  GLU   B CG   1 
ATOM   4518 C CD   A GLU   B 1 26  ? 48.946 -25.596 -14.568 0.80 24.18 ?  26  GLU   B CD   1 
ATOM   4519 C CD   B GLU   B 1 26  ? 49.028 -25.684 -14.583 0.20 20.79 ?  26  GLU   B CD   1 
ATOM   4520 O OE1  A GLU   B 1 26  ? 47.936 -24.956 -14.934 0.80 24.89 ?  26  GLU   B OE1  1 
ATOM   4521 O OE1  B GLU   B 1 26  ? 48.159 -24.888 -14.993 0.20 20.87 ?  26  GLU   B OE1  1 
ATOM   4522 O OE2  A GLU   B 1 26  ? 49.745 -26.080 -15.379 0.80 26.50 -1 26  GLU   B OE2  1 
ATOM   4523 O OE2  B GLU   B 1 26  ? 49.720 -26.383 -15.350 0.20 21.89 -1 26  GLU   B OE2  1 
ATOM   4524 H H    A GLU   B 1 26  ? 51.902 -25.019 -11.498 0.80 17.94 ?  26  GLU   B H    1 
ATOM   4525 H H    B GLU   B 1 26  ? 51.870 -24.972 -11.466 0.20 20.93 ?  26  GLU   B H    1 
ATOM   4526 H HA   A GLU   B 1 26  ? 51.087 -24.219 -13.830 0.80 19.89 ?  26  GLU   B HA   1 
ATOM   4527 H HA   B GLU   B 1 26  ? 51.082 -24.205 -13.836 0.20 20.73 ?  26  GLU   B HA   1 
ATOM   4528 H HB2  A GLU   B 1 26  ? 49.774 -24.741 -11.433 0.80 22.22 ?  26  GLU   B HB2  1 
ATOM   4529 H HB2  B GLU   B 1 26  ? 49.733 -24.723 -11.453 0.20 22.11 ?  26  GLU   B HB2  1 
ATOM   4530 H HB3  A GLU   B 1 26  ? 48.973 -23.879 -12.495 0.80 22.22 ?  26  GLU   B HB3  1 
ATOM   4531 H HB3  B GLU   B 1 26  ? 48.944 -23.893 -12.552 0.20 22.11 ?  26  GLU   B HB3  1 
ATOM   4532 H HG2  A GLU   B 1 26  ? 49.915 -26.480 -12.962 0.80 26.98 ?  26  GLU   B HG2  1 
ATOM   4533 H HG2  B GLU   B 1 26  ? 49.963 -26.471 -12.961 0.20 24.03 ?  26  GLU   B HG2  1 
ATOM   4534 H HG3  A GLU   B 1 26  ? 48.397 -26.114 -12.666 0.80 26.98 ?  26  GLU   B HG3  1 
ATOM   4535 H HG3  B GLU   B 1 26  ? 48.429 -26.146 -12.697 0.20 24.03 ?  26  GLU   B HG3  1 
ATOM   4536 N N    . ALA   B 1 27  ? 51.100 -21.880 -11.635 1.00 14.35 ?  27  ALA   B N    1 
ATOM   4537 C CA   . ALA   B 1 27  ? 51.059 -20.430 -11.492 1.00 14.39 ?  27  ALA   B CA   1 
ATOM   4538 C C    . ALA   B 1 27  ? 52.132 -19.767 -12.346 1.00 15.32 ?  27  ALA   B C    1 
ATOM   4539 O O    . ALA   B 1 27  ? 51.867 -18.762 -13.022 1.00 16.09 ?  27  ALA   B O    1 
ATOM   4540 C CB   . ALA   B 1 27  ? 51.192 -20.038 -10.022 1.00 14.58 ?  27  ALA   B CB   1 
ATOM   4541 H H    A ALA   B 1 27  ? 51.226 -22.312 -10.901 0.80 17.22 ?  27  ALA   B H    1 
ATOM   4542 H H    B ALA   B 1 27  ? 51.240 -22.314 -10.905 0.20 17.22 ?  27  ALA   B H    1 
ATOM   4543 H HA   . ALA   B 1 27  ? 50.201 -20.110 -11.806 1.00 17.26 ?  27  ALA   B HA   1 
ATOM   4544 H HB1  . ALA   B 1 27  ? 51.154 -19.071 -9.950  1.00 17.50 ?  27  ALA   B HB1  1 
ATOM   4545 H HB2  . ALA   B 1 27  ? 50.456 -20.433 -9.525  1.00 17.50 ?  27  ALA   B HB2  1 
ATOM   4546 H HB3  . ALA   B 1 27  ? 52.036 -20.364 -9.681  1.00 17.50 ?  27  ALA   B HB3  1 
ATOM   4547 N N    . LYS   B 1 28  ? 53.350 -20.321 -12.342 1.00 16.90 ?  28  LYS   B N    1 
ATOM   4548 C CA   . LYS   B 1 28  ? 54.417 -19.713 -13.126 1.00 18.99 ?  28  LYS   B CA   1 
ATOM   4549 C C    . LYS   B 1 28  ? 54.145 -19.800 -14.623 1.00 20.38 ?  28  LYS   B C    1 
ATOM   4550 O O    . LYS   B 1 28  ? 54.556 -18.908 -15.376 1.00 21.43 ?  28  LYS   B O    1 
ATOM   4551 C CB   . LYS   B 1 28  ? 55.776 -20.306 -12.739 1.00 22.00 ?  28  LYS   B CB   1 
ATOM   4552 C CG   . LYS   B 1 28  ? 56.175 -19.954 -11.308 1.00 25.22 ?  28  LYS   B CG   1 
ATOM   4553 C CD   . LYS   B 1 28  ? 57.607 -20.337 -10.965 1.00 30.35 ?  28  LYS   B CD   1 
ATOM   4554 C CE   . LYS   B 1 28  ? 57.740 -21.814 -10.685 1.00 34.43 ?  28  LYS   B CE   1 
ATOM   4555 N NZ   . LYS   B 1 28  ? 59.096 -22.149 -10.162 1.00 36.45 ?  28  LYS   B NZ   1 
ATOM   4556 H H    . LYS   B 1 28  ? 53.573 -21.031 -11.908 1.00 20.28 ?  28  LYS   B H    1 
ATOM   4557 H HA   . LYS   B 1 28  ? 54.450 -18.772 -12.908 1.00 22.79 ?  28  LYS   B HA   1 
ATOM   4558 H HB2  . LYS   B 1 28  ? 55.740 -21.270 -12.812 1.00 26.40 ?  28  LYS   B HB2  1 
ATOM   4559 H HB3  . LYS   B 1 28  ? 56.459 -19.952 -13.335 1.00 26.40 ?  28  LYS   B HB3  1 
ATOM   4560 H HG2  . LYS   B 1 28  ? 56.080 -18.995 -11.188 1.00 30.26 ?  28  LYS   B HG2  1 
ATOM   4561 H HG3  . LYS   B 1 28  ? 55.583 -20.422 -10.700 1.00 30.26 ?  28  LYS   B HG3  1 
ATOM   4562 H HD2  . LYS   B 1 28  ? 58.183 -20.112 -11.713 1.00 36.42 ?  28  LYS   B HD2  1 
ATOM   4563 H HD3  . LYS   B 1 28  ? 57.882 -19.848 -10.173 1.00 36.42 ?  28  LYS   B HD3  1 
ATOM   4564 H HE2  . LYS   B 1 28  ? 57.084 -22.074 -10.019 1.00 41.31 ?  28  LYS   B HE2  1 
ATOM   4565 H HE3  . LYS   B 1 28  ? 57.599 -22.310 -11.507 1.00 41.31 ?  28  LYS   B HE3  1 
ATOM   4566 H HZ1  . LYS   B 1 28  ? 59.154 -23.022 -10.003 1.00 43.74 ?  28  LYS   B HZ1  1 
ATOM   4567 H HZ2  . LYS   B 1 28  ? 59.716 -21.920 -10.758 1.00 43.74 ?  28  LYS   B HZ2  1 
ATOM   4568 H HZ3  . LYS   B 1 28  ? 59.247 -21.706 -9.404  1.00 43.74 ?  28  LYS   B HZ3  1 
ATOM   4569 N N    A LYS   B 1 29  ? 53.440 -20.840 -15.071 0.80 21.56 ?  29  LYS   B N    1 
ATOM   4570 N N    B LYS   B 1 29  ? 53.433 -20.839 -15.069 0.20 21.96 ?  29  LYS   B N    1 
ATOM   4571 C CA   A LYS   B 1 29  ? 53.164 -20.990 -16.494 0.80 23.58 ?  29  LYS   B CA   1 
ATOM   4572 C CA   B LYS   B 1 29  ? 53.155 -21.005 -16.492 0.20 23.72 ?  29  LYS   B CA   1 
ATOM   4573 C C    A LYS   B 1 29  ? 51.907 -20.245 -16.933 0.80 22.60 ?  29  LYS   B C    1 
ATOM   4574 C C    B LYS   B 1 29  ? 51.899 -20.264 -16.939 0.20 22.67 ?  29  LYS   B C    1 
ATOM   4575 O O    A LYS   B 1 29  ? 51.899 -19.630 -18.005 0.80 24.45 ?  29  LYS   B O    1 
ATOM   4576 O O    B LYS   B 1 29  ? 51.886 -19.666 -18.021 0.20 23.37 ?  29  LYS   B O    1 
ATOM   4577 C CB   A LYS   B 1 29  ? 53.046 -22.472 -16.858 0.80 28.18 ?  29  LYS   B CB   1 
ATOM   4578 C CB   B LYS   B 1 29  ? 53.028 -22.492 -16.838 0.20 26.88 ?  29  LYS   B CB   1 
ATOM   4579 C CG   A LYS   B 1 29  ? 52.847 -22.731 -18.342 0.80 32.37 ?  29  LYS   B CG   1 
ATOM   4580 C CG   B LYS   B 1 29  ? 52.887 -22.773 -18.327 0.20 29.73 ?  29  LYS   B CG   1 
ATOM   4581 C CD   A LYS   B 1 29  ? 53.058 -24.200 -18.678 0.80 35.40 ?  29  LYS   B CD   1 
ATOM   4582 C CD   B LYS   B 1 29  ? 53.014 -24.261 -18.629 0.20 31.92 ?  29  LYS   B CD   1 
ATOM   4583 C CE   A LYS   B 1 29  ? 51.985 -25.079 -18.059 0.80 37.57 ?  29  LYS   B CE   1 
ATOM   4584 C CE   B LYS   B 1 29  ? 51.820 -25.049 -18.115 0.20 33.47 ?  29  LYS   B CE   1 
ATOM   4585 N NZ   A LYS   B 1 29  ? 52.214 -26.520 -18.363 0.80 38.70 ?  29  LYS   B NZ   1 
ATOM   4586 N NZ   B LYS   B 1 29  ? 51.957 -26.507 -18.402 0.20 34.31 ?  29  LYS   B NZ   1 
ATOM   4587 H H    A LYS   B 1 29  ? 53.112 -21.467 -14.573 0.80 25.88 ?  29  LYS   B H    1 
ATOM   4588 H H    B LYS   B 1 29  ? 53.103 -21.461 -14.566 0.20 26.35 ?  29  LYS   B H    1 
ATOM   4589 H HA   A LYS   B 1 29  ? 53.910 -20.624 -16.988 0.80 28.30 ?  29  LYS   B HA   1 
ATOM   4590 H HA   B LYS   B 1 29  ? 53.899 -20.649 -16.991 0.20 28.46 ?  29  LYS   B HA   1 
ATOM   4591 H HB2  A LYS   B 1 29  ? 53.862 -22.923 -16.590 0.80 33.82 ?  29  LYS   B HB2  1 
ATOM   4592 H HB2  B LYS   B 1 29  ? 53.822 -22.953 -16.527 0.20 32.25 ?  29  LYS   B HB2  1 
ATOM   4593 H HB3  A LYS   B 1 29  ? 52.290 -22.850 -16.389 0.80 33.82 ?  29  LYS   B HB3  1 
ATOM   4594 H HB3  B LYS   B 1 29  ? 52.244 -22.851 -16.396 0.20 32.25 ?  29  LYS   B HB3  1 
ATOM   4595 H HG2  A LYS   B 1 29  ? 51.941 -22.487 -18.590 0.80 38.84 ?  29  LYS   B HG2  1 
ATOM   4596 H HG2  B LYS   B 1 29  ? 52.014 -22.475 -18.629 0.20 35.67 ?  29  LYS   B HG2  1 
ATOM   4597 H HG3  A LYS   B 1 29  ? 53.487 -22.205 -18.849 0.80 38.84 ?  29  LYS   B HG3  1 
ATOM   4598 H HG3  B LYS   B 1 29  ? 53.586 -22.303 -18.810 0.20 35.67 ?  29  LYS   B HG3  1 
ATOM   4599 H HD2  A LYS   B 1 29  ? 53.029 -24.317 -19.640 0.80 42.49 ?  29  LYS   B HD2  1 
ATOM   4600 H HD2  B LYS   B 1 29  ? 53.072 -24.389 -19.588 0.20 38.31 ?  29  LYS   B HD2  1 
ATOM   4601 H HD3  A LYS   B 1 29  ? 53.919 -24.487 -18.332 0.80 42.49 ?  29  LYS   B HD3  1 
ATOM   4602 H HD3  B LYS   B 1 29  ? 53.812 -24.606 -18.197 0.20 38.31 ?  29  LYS   B HD3  1 
ATOM   4603 H HE2  A LYS   B 1 29  ? 51.992 -24.969 -17.095 0.80 45.09 ?  29  LYS   B HE2  1 
ATOM   4604 H HE2  B LYS   B 1 29  ? 51.748 -24.936 -17.154 0.20 40.17 ?  29  LYS   B HE2  1 
ATOM   4605 H HE3  A LYS   B 1 29  ? 51.119 -24.826 -18.418 0.80 45.09 ?  29  LYS   B HE3  1 
ATOM   4606 H HE3  B LYS   B 1 29  ? 51.014 -24.729 -18.551 0.20 40.17 ?  29  LYS   B HE3  1 
ATOM   4607 H HZ1  A LYS   B 1 29  ? 51.574 -27.015 -17.992 0.80 46.45 ?  29  LYS   B HZ1  1 
ATOM   4608 H HZ1  B LYS   B 1 29  ? 51.248 -26.947 -18.093 0.20 41.18 ?  29  LYS   B HZ1  1 
ATOM   4609 H HZ2  A LYS   B 1 29  ? 52.207 -26.650 -19.243 0.80 46.45 ?  29  LYS   B HZ2  1 
ATOM   4610 H HZ2  B LYS   B 1 29  ? 52.021 -26.639 -19.280 0.20 41.18 ?  29  LYS   B HZ2  1 
ATOM   4611 H HZ3  A LYS   B 1 29  ? 53.002 -26.777 -18.039 0.80 46.45 ?  29  LYS   B HZ3  1 
ATOM   4612 H HZ3  B LYS   B 1 29  ? 52.690 -26.826 -18.008 0.20 41.18 ?  29  LYS   B HZ3  1 
ATOM   4613 N N    . VAL   B 1 30  ? 50.843 -20.297 -16.127 1.00 21.21 ?  30  VAL   B N    1 
ATOM   4614 C CA   . VAL   B 1 30  ? 49.565 -19.686 -16.507 1.00 20.84 ?  30  VAL   B CA   1 
ATOM   4615 C C    . VAL   B 1 30  ? 49.576 -18.176 -16.340 1.00 19.28 ?  30  VAL   B C    1 
ATOM   4616 O O    . VAL   B 1 30  ? 48.846 -17.458 -17.043 1.00 20.08 ?  30  VAL   B O    1 
ATOM   4617 C CB   . VAL   B 1 30  ? 48.468 -20.296 -15.617 1.00 22.03 ?  30  VAL   B CB   1 
ATOM   4618 C CG1  . VAL   B 1 30  ? 47.182 -19.491 -15.697 1.00 23.05 ?  30  VAL   B CG1  1 
ATOM   4619 C CG2  . VAL   B 1 30  ? 48.231 -21.748 -15.990 1.00 23.11 ?  30  VAL   B CG2  1 
ATOM   4620 H H    A VAL   B 1 30  ? 50.829 -20.697 -15.362 0.80 25.45 ?  30  VAL   B H    1 
ATOM   4621 H H    B VAL   B 1 30  ? 50.835 -20.674 -15.350 0.20 25.45 ?  30  VAL   B H    1 
ATOM   4622 H HA   . VAL   B 1 30  ? 49.365 -19.907 -17.429 1.00 25.01 ?  30  VAL   B HA   1 
ATOM   4623 H HB   . VAL   B 1 30  ? 48.766 -20.283 -14.693 1.00 26.44 ?  30  VAL   B HB   1 
ATOM   4624 H HG11 . VAL   B 1 30  ? 46.444 -20.075 -15.458 1.00 27.66 ?  30  VAL   B HG11 1 
ATOM   4625 H HG12 . VAL   B 1 30  ? 47.230 -18.754 -15.074 1.00 27.66 ?  30  VAL   B HG12 1 
ATOM   4626 H HG13 . VAL   B 1 30  ? 47.063 -19.175 -16.600 1.00 27.66 ?  30  VAL   B HG13 1 
ATOM   4627 H HG21 . VAL   B 1 30  ? 47.542 -22.119 -15.412 1.00 27.73 ?  30  VAL   B HG21 1 
ATOM   4628 H HG22 . VAL   B 1 30  ? 47.937 -21.793 -16.916 1.00 27.73 ?  30  VAL   B HG22 1 
ATOM   4629 H HG23 . VAL   B 1 30  ? 49.054 -22.245 -15.880 1.00 27.73 ?  30  VAL   B HG23 1 
ATOM   4630 N N    A LYS   B 1 31  ? 50.358 -17.672 -15.396 0.80 18.62 ?  31  LYS   B N    1 
ATOM   4631 N N    B LYS   B 1 31  ? 50.381 -17.679 -15.411 0.20 19.31 ?  31  LYS   B N    1 
ATOM   4632 C CA   A LYS   B 1 31  ? 50.400 -16.254 -15.063 0.80 19.23 ?  31  LYS   B CA   1 
ATOM   4633 C CA   B LYS   B 1 31  ? 50.400 -16.269 -15.046 0.20 19.76 ?  31  LYS   B CA   1 
ATOM   4634 C C    A LYS   B 1 31  ? 49.009 -15.756 -14.669 0.80 17.21 ?  31  LYS   B C    1 
ATOM   4635 C C    B LYS   B 1 31  ? 48.999 -15.774 -14.678 0.20 17.50 ?  31  LYS   B C    1 
ATOM   4636 O O    A LYS   B 1 31  ? 48.478 -14.832 -15.297 0.80 17.86 ?  31  LYS   B O    1 
ATOM   4637 O O    B LYS   B 1 31  ? 48.455 -14.882 -15.336 0.20 17.54 ?  31  LYS   B O    1 
ATOM   4638 C CB   A LYS   B 1 31  ? 51.017 -15.464 -16.222 0.80 22.56 ?  31  LYS   B CB   1 
ATOM   4639 C CB   B LYS   B 1 31  ? 51.018 -15.424 -16.151 0.20 22.44 ?  31  LYS   B CB   1 
ATOM   4640 C CG   A LYS   B 1 31  ? 52.477 -15.849 -16.494 0.80 25.86 ?  31  LYS   B CG   1 
ATOM   4641 C CG   B LYS   B 1 31  ? 52.421 -15.898 -16.505 0.20 24.80 ?  31  LYS   B CG   1 
ATOM   4642 C CD   A LYS   B 1 31  ? 53.054 -15.087 -17.674 0.80 29.69 ?  31  LYS   B CD   1 
ATOM   4643 C CD   B LYS   B 1 31  ? 53.006 -15.148 -17.681 0.20 26.99 ?  31  LYS   B CD   1 
ATOM   4644 C CE   A LYS   B 1 31  ? 54.541 -15.329 -17.804 0.80 32.79 ?  31  LYS   B CE   1 
ATOM   4645 C CE   B LYS   B 1 31  ? 54.489 -15.437 -17.828 0.20 28.70 ?  31  LYS   B CE   1 
ATOM   4646 N NZ   A LYS   B 1 31  ? 55.254 -14.896 -16.571 0.80 34.09 ?  31  LYS   B NZ   1 
ATOM   4647 N NZ   B LYS   B 1 31  ? 55.239 -15.059 -16.597 0.20 29.44 ?  31  LYS   B NZ   1 
ATOM   4648 H H    A LYS   B 1 31  ? 50.891 -18.157 -14.923 0.80 22.34 ?  31  LYS   B H    1 
ATOM   4649 H H    B LYS   B 1 31  ? 50.944 -18.156 -14.970 0.20 23.17 ?  31  LYS   B H    1 
ATOM   4650 H HA   A LYS   B 1 31  ? 50.971 -16.152 -14.299 0.80 23.08 ?  31  LYS   B HA   1 
ATOM   4651 H HA   B LYS   B 1 31  ? 50.955 -16.175 -14.268 0.20 23.71 ?  31  LYS   B HA   1 
ATOM   4652 H HB2  A LYS   B 1 31  ? 50.513 -15.631 -17.034 0.80 27.07 ?  31  LYS   B HB2  1 
ATOM   4653 H HB2  B LYS   B 1 31  ? 50.470 -15.477 -16.948 0.20 26.93 ?  31  LYS   B HB2  1 
ATOM   4654 H HB3  A LYS   B 1 31  ? 50.995 -14.524 -16.002 0.80 27.07 ?  31  LYS   B HB3  1 
ATOM   4655 H HB3  B LYS   B 1 31  ? 51.079 -14.504 -15.846 0.20 26.93 ?  31  LYS   B HB3  1 
ATOM   4656 H HG2  A LYS   B 1 31  ? 53.008 -15.647 -15.706 0.80 31.03 ?  31  LYS   B HG2  1 
ATOM   4657 H HG2  B LYS   B 1 31  ? 52.998 -15.766 -15.736 0.20 29.77 ?  31  LYS   B HG2  1 
ATOM   4658 H HG3  A LYS   B 1 31  ? 52.529 -16.800 -16.692 0.80 31.03 ?  31  LYS   B HG3  1 
ATOM   4659 H HG3  B LYS   B 1 31  ? 52.391 -16.841 -16.737 0.20 29.77 ?  31  LYS   B HG3  1 
ATOM   4660 H HD2  A LYS   B 1 31  ? 52.621 -15.388 -18.487 0.80 35.63 ?  31  LYS   B HD2  1 
ATOM   4661 H HD2  B LYS   B 1 31  ? 52.557 -15.430 -18.493 0.20 32.38 ?  31  LYS   B HD2  1 
ATOM   4662 H HD3  A LYS   B 1 31  ? 52.907 -14.140 -17.541 0.80 35.63 ?  31  LYS   B HD3  1 
ATOM   4663 H HD3  B LYS   B 1 31  ? 52.891 -14.198 -17.541 0.20 32.38 ?  31  LYS   B HD3  1 
ATOM   4664 H HE2  A LYS   B 1 31  ? 54.706 -16.276 -17.938 0.80 39.34 ?  31  LYS   B HE2  1 
ATOM   4665 H HE2  B LYS   B 1 31  ? 54.620 -16.387 -17.984 0.20 34.44 ?  31  LYS   B HE2  1 
ATOM   4666 H HE3  A LYS   B 1 31  ? 54.885 -14.817 -18.554 0.80 39.34 ?  31  LYS   B HE3  1 
ATOM   4667 H HE3  B LYS   B 1 31  ? 54.844 -14.923 -18.570 0.20 34.44 ?  31  LYS   B HE3  1 
ATOM   4668 H HZ1  A LYS   B 1 31  ? 56.132 -14.897 -16.711 0.80 40.90 ?  31  LYS   B HZ1  1 
ATOM   4669 H HZ1  B LYS   B 1 31  ? 56.113 -15.074 -16.756 0.20 35.33 ?  31  LYS   B HZ1  1 
ATOM   4670 H HZ2  A LYS   B 1 31  ? 54.997 -14.074 -16.346 0.80 40.90 ?  31  LYS   B HZ2  1 
ATOM   4671 H HZ2  B LYS   B 1 31  ? 55.005 -14.239 -16.340 0.20 35.33 ?  31  LYS   B HZ2  1 
ATOM   4672 H HZ3  A LYS   B 1 31  ? 55.067 -15.450 -15.900 0.80 40.90 ?  31  LYS   B HZ3  1 
ATOM   4673 H HZ3  B LYS   B 1 31  ? 55.054 -15.630 -15.939 0.20 35.33 ?  31  LYS   B HZ3  1 
ATOM   4674 N N    . PRO   B 1 32  ? 48.395 -16.335 -13.632 1.00 15.32 ?  32  PRO   B N    1 
ATOM   4675 C CA   . PRO   B 1 32  ? 47.023 -15.959 -13.273 1.00 14.35 ?  32  PRO   B CA   1 
ATOM   4676 C C    . PRO   B 1 32  ? 46.949 -14.612 -12.572 1.00 14.26 ?  32  PRO   B C    1 
ATOM   4677 O O    . PRO   B 1 32  ? 47.876 -14.192 -11.875 1.00 15.68 ?  32  PRO   B O    1 
ATOM   4678 C CB   . PRO   B 1 32  ? 46.617 -17.069 -12.295 1.00 14.68 ?  32  PRO   B CB   1 
ATOM   4679 C CG   . PRO   B 1 32  ? 47.926 -17.426 -11.616 1.00 14.70 ?  32  PRO   B CG   1 
ATOM   4680 C CD   . PRO   B 1 32  ? 48.972 -17.313 -12.685 1.00 15.41 ?  32  PRO   B CD   1 
ATOM   4681 H HA   . PRO   B 1 32  ? 46.443 -15.973 -14.051 1.00 17.22 ?  32  PRO   B HA   1 
ATOM   4682 H HB2  . PRO   B 1 32  ? 45.976 -16.728 -11.650 1.00 17.62 ?  32  PRO   B HB2  1 
ATOM   4683 H HB3  . PRO   B 1 32  ? 46.258 -17.829 -12.777 1.00 17.62 ?  32  PRO   B HB3  1 
ATOM   4684 H HG2  . PRO   B 1 32  ? 48.109 -16.802 -10.894 1.00 17.64 ?  32  PRO   B HG2  1 
ATOM   4685 H HG3  . PRO   B 1 32  ? 47.888 -18.336 -11.275 1.00 17.64 ?  32  PRO   B HG3  1 
ATOM   4686 H HD2  . PRO   B 1 32  ? 49.800 -16.974 -12.309 1.00 18.49 ?  32  PRO   B HD2  1 
ATOM   4687 H HD3  . PRO   B 1 32  ? 49.100 -18.168 -13.117 1.00 18.49 ?  32  PRO   B HD3  1 
ATOM   4688 N N    . THR   B 1 33  ? 45.800 -13.953 -12.734 1.00 14.17 ?  33  THR   B N    1 
ATOM   4689 C CA   . THR   B 1 33  ? 45.516 -12.773 -11.923 1.00 14.49 ?  33  THR   B CA   1 
ATOM   4690 C C    . THR   B 1 33  ? 45.473 -13.125 -10.440 1.00 13.89 ?  33  THR   B C    1 
ATOM   4691 O O    . THR   B 1 33  ? 45.949 -12.349 -9.597  1.00 14.86 ?  33  THR   B O    1 
ATOM   4692 C CB   . THR   B 1 33  ? 44.192 -12.143 -12.362 1.00 15.07 ?  33  THR   B CB   1 
ATOM   4693 O OG1  . THR   B 1 33  ? 44.219 -11.882 -13.768 1.00 15.18 ?  33  THR   B OG1  1 
ATOM   4694 C CG2  . THR   B 1 33  ? 43.949 -10.850 -11.604 1.00 16.65 ?  33  THR   B CG2  1 
ATOM   4695 H H    . THR   B 1 33  ? 45.183 -14.168 -13.304 1.00 17.01 ?  33  THR   B H    1 
ATOM   4696 H HA   . THR   B 1 33  ? 46.215 -12.122 -12.067 1.00 17.38 ?  33  THR   B HA   1 
ATOM   4697 H HB   . THR   B 1 33  ? 43.461 -12.760 -12.167 1.00 18.08 ?  33  THR   B HB   1 
ATOM   4698 H HG1  . THR   B 1 33  ? 43.493 -11.523 -14.008 1.00 18.22 ?  33  THR   B HG1  1 
ATOM   4699 H HG21 . THR   B 1 33  ? 43.207 -10.372 -11.994 1.00 19.98 ?  33  THR   B HG21 1 
ATOM   4700 H HG22 . THR   B 1 33  ? 43.749 -11.043 -10.673 1.00 19.98 ?  33  THR   B HG22 1 
ATOM   4701 H HG23 . THR   B 1 33  ? 44.744 -10.294 -11.645 1.00 19.98 ?  33  THR   B HG23 1 
ATOM   4702 N N    . VAL   B 1 34  ? 44.915 -14.291 -10.102 1.00 13.07 ?  34  VAL   B N    1 
ATOM   4703 C CA   . VAL   B 1 34  ? 44.712 -14.674 -8.709  1.00 12.32 ?  34  VAL   B CA   1 
ATOM   4704 C C    . VAL   B 1 34  ? 45.126 -16.126 -8.532  1.00 11.48 ?  34  VAL   B C    1 
ATOM   4705 O O    . VAL   B 1 34  ? 44.590 -17.015 -9.207  1.00 12.57 ?  34  VAL   B O    1 
ATOM   4706 C CB   . VAL   B 1 34  ? 43.244 -14.511 -8.263  1.00 13.72 ?  34  VAL   B CB   1 
ATOM   4707 C CG1  . VAL   B 1 34  ? 43.076 -14.965 -6.822  1.00 13.92 ?  34  VAL   B CG1  1 
ATOM   4708 C CG2  . VAL   B 1 34  ? 42.761 -13.081 -8.455  1.00 14.65 ?  34  VAL   B CG2  1 
ATOM   4709 H H    . VAL   B 1 34  ? 44.647 -14.886 -10.669 1.00 15.68 ?  34  VAL   B H    1 
ATOM   4710 H HA   . VAL   B 1 34  ? 45.272 -14.126 -8.139  1.00 14.78 ?  34  VAL   B HA   1 
ATOM   4711 H HB   . VAL   B 1 34  ? 42.689 -15.076 -8.819  1.00 16.46 ?  34  VAL   B HB   1 
ATOM   4712 H HG11 . VAL   B 1 34  ? 42.232 -14.625 -6.479  1.00 16.71 ?  34  VAL   B HG11 1 
ATOM   4713 H HG12 . VAL   B 1 34  ? 43.073 -15.935 -6.791  1.00 16.71 ?  34  VAL   B HG12 1 
ATOM   4714 H HG13 . VAL   B 1 34  ? 43.808 -14.617 -6.289  1.00 16.71 ?  34  VAL   B HG13 1 
ATOM   4715 H HG21 . VAL   B 1 34  ? 41.842 -13.011 -8.149  1.00 17.58 ?  34  VAL   B HG21 1 
ATOM   4716 H HG22 . VAL   B 1 34  ? 43.326 -12.479 -7.947  1.00 17.58 ?  34  VAL   B HG22 1 
ATOM   4717 H HG23 . VAL   B 1 34  ? 42.807 -12.852 -9.401  1.00 17.58 ?  34  VAL   B HG23 1 
ATOM   4718 N N    . VAL   B 1 35  ? 46.033 -16.378 -7.596  1.00 10.87 ?  35  VAL   B N    1 
ATOM   4719 C CA   . VAL   B 1 35  ? 46.255 -17.722 -7.072  1.00 10.84 ?  35  VAL   B CA   1 
ATOM   4720 C C    . VAL   B 1 35  ? 45.704 -17.772 -5.654  1.00 10.43 ?  35  VAL   B C    1 
ATOM   4721 O O    . VAL   B 1 35  ? 45.938 -16.860 -4.856  1.00 11.06 ?  35  VAL   B O    1 
ATOM   4722 C CB   . VAL   B 1 35  ? 47.738 -18.158 -7.142  1.00 11.62 ?  35  VAL   B CB   1 
ATOM   4723 C CG1  . VAL   B 1 35  ? 48.643 -17.309 -6.228  1.00 13.02 ?  35  VAL   B CG1  1 
ATOM   4724 C CG2  . VAL   B 1 35  ? 47.867 -19.653 -6.816  1.00 12.64 ?  35  VAL   B CG2  1 
ATOM   4725 H H    . VAL   B 1 35  ? 46.542 -15.778 -7.245  1.00 13.04 ?  35  VAL   B H    1 
ATOM   4726 H HA   . VAL   B 1 35  ? 45.744 -18.350 -7.599  1.00 13.01 ?  35  VAL   B HA   1 
ATOM   4727 H HB   . VAL   B 1 35  ? 48.048 -18.036 -8.053  1.00 13.95 ?  35  VAL   B HB   1 
ATOM   4728 H HG11 . VAL   B 1 35  ? 49.566 -17.554 -6.393  1.00 15.62 ?  35  VAL   B HG11 1 
ATOM   4729 H HG12 . VAL   B 1 35  ? 48.499 -16.377 -6.427  1.00 15.62 ?  35  VAL   B HG12 1 
ATOM   4730 H HG13 . VAL   B 1 35  ? 48.412 -17.496 -5.303  1.00 15.62 ?  35  VAL   B HG13 1 
ATOM   4731 H HG21 . VAL   B 1 35  ? 48.790 -19.927 -6.917  1.00 15.17 ?  35  VAL   B HG21 1 
ATOM   4732 H HG22 . VAL   B 1 35  ? 47.576 -19.808 -5.900  1.00 15.17 ?  35  VAL   B HG22 1 
ATOM   4733 H HG23 . VAL   B 1 35  ? 47.303 -20.164 -7.424  1.00 15.17 ?  35  VAL   B HG23 1 
ATOM   4734 N N    . VAL   B 1 36  ? 44.987 -18.854 -5.335  1.00 10.83 ?  36  VAL   B N    1 
ATOM   4735 C CA   . VAL   B 1 36  ? 44.445 -19.053 -4.000  1.00 10.33 ?  36  VAL   B CA   1 
ATOM   4736 C C    . VAL   B 1 36  ? 45.454 -19.814 -3.147  1.00 10.07 ?  36  VAL   B C    1 
ATOM   4737 O O    . VAL   B 1 36  ? 46.002 -20.846 -3.569  1.00 11.39 ?  36  VAL   B O    1 
ATOM   4738 C CB   . VAL   B 1 36  ? 43.104 -19.809 -4.069  1.00 10.80 ?  36  VAL   B CB   1 
ATOM   4739 C CG1  . VAL   B 1 36  ? 42.614 -20.164 -2.681  1.00 11.37 ?  36  VAL   B CG1  1 
ATOM   4740 C CG2  . VAL   B 1 36  ? 42.081 -18.984 -4.826  1.00 11.60 ?  36  VAL   B CG2  1 
ATOM   4741 H H    . VAL   B 1 36  ? 44.817 -19.501 -5.877  1.00 12.99 ?  36  VAL   B H    1 
ATOM   4742 H HA   . VAL   B 1 36  ? 44.285 -18.192 -3.586  1.00 12.40 ?  36  VAL   B HA   1 
ATOM   4743 H HB   . VAL   B 1 36  ? 43.235 -20.636 -4.556  1.00 12.96 ?  36  VAL   B HB   1 
ATOM   4744 H HG11 . VAL   B 1 36  ? 41.671 -20.378 -2.722  1.00 13.64 ?  36  VAL   B HG11 1 
ATOM   4745 H HG12 . VAL   B 1 36  ? 43.114 -20.926 -2.350  1.00 13.64 ?  36  VAL   B HG12 1 
ATOM   4746 H HG13 . VAL   B 1 36  ? 42.750 -19.399 -2.093  1.00 13.64 ?  36  VAL   B HG13 1 
ATOM   4747 H HG21 . VAL   B 1 36  ? 41.237 -19.464 -4.839  1.00 13.92 ?  36  VAL   B HG21 1 
ATOM   4748 H HG22 . VAL   B 1 36  ? 41.971 -18.131 -4.383  1.00 13.92 ?  36  VAL   B HG22 1 
ATOM   4749 H HG23 . VAL   B 1 36  ? 42.396 -18.850 -5.735  1.00 13.92 ?  36  VAL   B HG23 1 
ATOM   4750 N N    . ASN   B 1 37  ? 45.674 -19.321 -1.930  1.00 10.52 ?  37  ASN   B N    1 
ATOM   4751 C CA   . ASN   B 1 37  ? 46.421 -20.042 -0.914  1.00 10.55 ?  37  ASN   B CA   1 
ATOM   4752 C C    . ASN   B 1 37  ? 45.470 -20.714 0.068   1.00 11.17 ?  37  ASN   B C    1 
ATOM   4753 O O    . ASN   B 1 37  ? 44.459 -20.130 0.472   1.00 11.66 ?  37  ASN   B O    1 
ATOM   4754 C CB   . ASN   B 1 37  ? 47.355 -19.098 -0.159  1.00 10.45 ?  37  ASN   B CB   1 
ATOM   4755 C CG   . ASN   B 1 37  ? 48.201 -19.807 0.857   1.00 11.33 ?  37  ASN   B CG   1 
ATOM   4756 O OD1  . ASN   B 1 37  ? 48.536 -20.988 0.683   1.00 11.93 ?  37  ASN   B OD1  1 
ATOM   4757 N ND2  . ASN   B 1 37  ? 48.548 -19.109 1.936   1.00 11.06 ?  37  ASN   B ND2  1 
ATOM   4758 H H    . ASN   B 1 37  ? 45.392 -18.549 -1.661  1.00 12.63 ?  37  ASN   B H    1 
ATOM   4759 H HA   . ASN   B 1 37  ? 46.959 -20.728 -1.332  1.00 12.66 ?  37  ASN   B HA   1 
ATOM   4760 H HB2  . ASN   B 1 37  ? 47.956 -18.674 -0.791  1.00 12.54 ?  37  ASN   B HB2  1 
ATOM   4761 H HB3  . ASN   B 1 37  ? 46.834 -18.428 0.306   1.00 12.54 ?  37  ASN   B HB3  1 
ATOM   4762 H HD21 . ASN   B 1 37  ? 49.047 -19.466 2.544   1.00 13.27 ?  37  ASN   B HD21 1 
ATOM   4763 H HD22 . ASN   B 1 37  ? 48.314 -18.289 2.017   1.00 13.27 ?  37  ASN   B HD22 1 
ATOM   4764 N N    . ALA   B 1 38  ? 45.816 -21.946 0.447   1.00 11.31 ?  38  ALA   B N    1 
ATOM   4765 C CA   . ALA   B 1 38  ? 45.164 -22.680 1.533   1.00 11.52 ?  38  ALA   B CA   1 
ATOM   4766 C C    . ALA   B 1 38  ? 45.757 -22.192 2.851   1.00 11.62 ?  38  ALA   B C    1 
ATOM   4767 O O    . ALA   B 1 38  ? 46.659 -22.801 3.436   1.00 12.64 ?  38  ALA   B O    1 
ATOM   4768 C CB   . ALA   B 1 38  ? 45.386 -24.173 1.358   1.00 12.68 ?  38  ALA   B CB   1 
ATOM   4769 H H    . ALA   B 1 38  ? 46.466 -22.389 0.087   1.00 13.57 ?  38  ALA   B H    1 
ATOM   4770 H HA   . ALA   B 1 38  ? 44.214 -22.500 1.532   1.00 13.82 ?  38  ALA   B HA   1 
ATOM   4771 H HB1  . ALA   B 1 38  ? 44.942 -24.648 2.086   1.00 15.22 ?  38  ALA   B HB1  1 
ATOM   4772 H HB2  . ALA   B 1 38  ? 45.004 -24.451 0.511   1.00 15.22 ?  38  ALA   B HB2  1 
ATOM   4773 H HB3  . ALA   B 1 38  ? 46.334 -24.362 1.375   1.00 15.22 ?  38  ALA   B HB3  1 
ATOM   4774 N N    . ALA   B 1 39  ? 45.235 -21.054 3.305   1.00 11.19 ?  39  ALA   B N    1 
ATOM   4775 C CA   . ALA   B 1 39  ? 45.784 -20.319 4.434   1.00 11.53 ?  39  ALA   B CA   1 
ATOM   4776 C C    . ALA   B 1 39  ? 45.170 -20.761 5.763   1.00 11.50 ?  39  ALA   B C    1 
ATOM   4777 O O    . ALA   B 1 39  ? 44.131 -21.421 5.816   1.00 13.06 ?  39  ALA   B O    1 
ATOM   4778 C CB   . ALA   B 1 39  ? 45.547 -18.816 4.239   1.00 11.95 ?  39  ALA   B CB   1 
ATOM   4779 H H    . ALA   B 1 39  ? 44.540 -20.682 2.969   1.00 13.43 ?  39  ALA   B H    1 
ATOM   4780 H HA   . ALA   B 1 39  ? 46.740 -20.469 4.483   1.00 13.83 ?  39  ALA   B HA   1 
ATOM   4781 H HB1  . ALA   B 1 39  ? 45.917 -18.335 4.998   1.00 14.34 ?  39  ALA   B HB1  1 
ATOM   4782 H HB2  . ALA   B 1 39  ? 45.988 -18.531 3.423   1.00 14.34 ?  39  ALA   B HB2  1 
ATOM   4783 H HB3  . ALA   B 1 39  ? 44.594 -18.650 4.177   1.00 14.34 ?  39  ALA   B HB3  1 
ATOM   4784 N N    . ASN   B 1 40  ? 45.820 -20.349 6.849   1.00 12.17 ?  40  ASN   B N    1 
ATOM   4785 C CA   . ASN   B 1 40  ? 45.250 -20.383 8.187   1.00 12.92 ?  40  ASN   B CA   1 
ATOM   4786 C C    . ASN   B 1 40  ? 45.057 -18.953 8.700   1.00 12.79 ?  40  ASN   B C    1 
ATOM   4787 O O    . ASN   B 1 40  ? 45.477 -17.981 8.071   1.00 12.69 ?  40  ASN   B O    1 
ATOM   4788 C CB   . ASN   B 1 40  ? 46.092 -21.248 9.137   1.00 13.89 ?  40  ASN   B CB   1 
ATOM   4789 C CG   . ASN   B 1 40  ? 47.546 -20.831 9.178   1.00 14.74 ?  40  ASN   B CG   1 
ATOM   4790 O OD1  . ASN   B 1 40  ? 47.863 -19.643 9.266   1.00 17.10 ?  40  ASN   B OD1  1 
ATOM   4791 N ND2  . ASN   B 1 40  ? 48.442 -21.805 9.122   1.00 14.94 ?  40  ASN   B ND2  1 
ATOM   4792 H H    . ASN   B 1 40  ? 46.621 -20.037 6.831   1.00 14.60 ?  40  ASN   B H    1 
ATOM   4793 H HA   . ASN   B 1 40  ? 44.365 -20.779 8.136   1.00 15.50 ?  40  ASN   B HA   1 
ATOM   4794 H HB2  . ASN   B 1 40  ? 45.725 -21.174 10.033  1.00 16.67 ?  40  ASN   B HB2  1 
ATOM   4795 H HB3  . ASN   B 1 40  ? 46.046 -22.170 8.838   1.00 16.67 ?  40  ASN   B HB3  1 
ATOM   4796 H HD21 . ASN   B 1 40  ? 49.280 -21.623 9.150   1.00 17.93 ?  40  ASN   B HD21 1 
ATOM   4797 H HD22 . ASN   B 1 40  ? 48.183 -22.627 9.067   1.00 17.93 ?  40  ASN   B HD22 1 
ATOM   4798 N N    . VAL   B 1 41  ? 44.417 -18.825 9.863   1.00 13.29 ?  41  VAL   B N    1 
ATOM   4799 C CA   . VAL   B 1 41  ? 43.951 -17.509 10.311  1.00 14.21 ?  41  VAL   B CA   1 
ATOM   4800 C C    . VAL   B 1 41  ? 45.103 -16.554 10.603  1.00 13.73 ?  41  VAL   B C    1 
ATOM   4801 O O    . VAL   B 1 41  ? 44.927 -15.332 10.513  1.00 14.13 ?  41  VAL   B O    1 
ATOM   4802 C CB   . VAL   B 1 41  ? 42.982 -17.588 11.507  1.00 15.83 ?  41  VAL   B CB   1 
ATOM   4803 C CG1  . VAL   B 1 41  ? 41.676 -18.273 11.110  1.00 16.34 ?  41  VAL   B CG1  1 
ATOM   4804 C CG2  . VAL   B 1 41  ? 43.645 -18.259 12.703  1.00 16.24 ?  41  VAL   B CG2  1 
ATOM   4805 H H    . VAL   B 1 41  ? 44.242 -19.468 10.395  1.00 15.95 ?  41  VAL   B H    1 
ATOM   4806 H HA   . VAL   B 1 41  ? 43.450 -17.112 9.583   1.00 17.05 ?  41  VAL   B HA   1 
ATOM   4807 H HB   . VAL   B 1 41  ? 42.755 -16.685 11.776  1.00 18.99 ?  41  VAL   B HB   1 
ATOM   4808 H HG11 . VAL   B 1 41  ? 41.075 -18.282 11.872  1.00 19.60 ?  41  VAL   B HG11 1 
ATOM   4809 H HG12 . VAL   B 1 41  ? 41.271 -17.786 10.376  1.00 19.60 ?  41  VAL   B HG12 1 
ATOM   4810 H HG13 . VAL   B 1 41  ? 41.868 -19.185 10.833  1.00 19.60 ?  41  VAL   B HG13 1 
ATOM   4811 H HG21 . VAL   B 1 41  ? 43.005 -18.315 13.430  1.00 19.48 ?  41  VAL   B HG21 1 
ATOM   4812 H HG22 . VAL   B 1 41  ? 43.933 -19.151 12.450  1.00 19.48 ?  41  VAL   B HG22 1 
ATOM   4813 H HG23 . VAL   B 1 41  ? 44.411 -17.731 12.978  1.00 19.48 ?  41  VAL   B HG23 1 
ATOM   4814 N N    . TYR   B 1 42  ? 46.277 -17.070 10.970  1.00 13.92 ?  42  TYR   B N    1 
ATOM   4815 C CA   . TYR   B 1 42  ? 47.432 -16.224 11.240  1.00 14.24 ?  42  TYR   B CA   1 
ATOM   4816 C C    . TYR   B 1 42  ? 48.399 -16.152 10.056  1.00 13.20 ?  42  TYR   B C    1 
ATOM   4817 O O    . TYR   B 1 42  ? 49.484 -15.572 10.186  1.00 15.06 ?  42  TYR   B O    1 
ATOM   4818 C CB   . TYR   B 1 42  ? 48.115 -16.623 12.556  1.00 16.46 ?  42  TYR   B CB   1 
ATOM   4819 C CG   . TYR   B 1 42  ? 47.526 -15.917 13.779  1.00 16.45 ?  42  TYR   B CG   1 
ATOM   4820 C CD1  . TYR   B 1 42  ? 47.738 -14.557 13.981  1.00 15.69 ?  42  TYR   B CD1  1 
ATOM   4821 C CD2  . TYR   B 1 42  ? 46.758 -16.596 14.714  1.00 18.00 ?  42  TYR   B CD2  1 
ATOM   4822 C CE1  . TYR   B 1 42  ? 47.212 -13.897 15.079  1.00 16.50 ?  42  TYR   B CE1  1 
ATOM   4823 C CE2  . TYR   B 1 42  ? 46.228 -15.941 15.823  1.00 18.37 ?  42  TYR   B CE2  1 
ATOM   4824 C CZ   . TYR   B 1 42  ? 46.460 -14.586 15.997  1.00 18.36 ?  42  TYR   B CZ   1 
ATOM   4825 O OH   . TYR   B 1 42  ? 45.953 -13.906 17.089  1.00 20.68 ?  42  TYR   B OH   1 
ATOM   4826 H H    . TYR   B 1 42  ? 46.427 -17.919 11.059  1.00 16.70 ?  42  TYR   B H    1 
ATOM   4827 H HA   . TYR   B 1 42  ? 47.101 -15.329 11.366  1.00 17.09 ?  42  TYR   B HA   1 
ATOM   4828 H HB2  . TYR   B 1 42  ? 48.019 -17.580 12.684  1.00 19.75 ?  42  TYR   B HB2  1 
ATOM   4829 H HB3  . TYR   B 1 42  ? 49.056 -16.392 12.497  1.00 19.75 ?  42  TYR   B HB3  1 
ATOM   4830 H HD1  . TYR   B 1 42  ? 48.251 -14.079 13.362  1.00 18.82 ?  42  TYR   B HD1  1 
ATOM   4831 H HD2  . TYR   B 1 42  ? 46.597 -17.508 14.596  1.00 21.60 ?  42  TYR   B HD2  1 
ATOM   4832 H HE1  . TYR   B 1 42  ? 47.372 -12.989 15.192  1.00 19.80 ?  42  TYR   B HE1  1 
ATOM   4833 H HE2  . TYR   B 1 42  ? 45.712 -16.413 16.437  1.00 22.04 ?  42  TYR   B HE2  1 
ATOM   4834 H HH   . TYR   B 1 42  ? 46.178 -13.097 17.044  1.00 24.82 ?  42  TYR   B HH   1 
ATOM   4835 N N    . LEU   B 1 43  ? 47.999 -16.661 8.893   1.00 12.29 ?  43  LEU   B N    1 
ATOM   4836 C CA   . LEU   B 1 43  ? 48.814 -16.592 7.682   1.00 12.10 ?  43  LEU   B CA   1 
ATOM   4837 C C    . LEU   B 1 43  ? 50.228 -17.098 7.941   1.00 12.80 ?  43  LEU   B C    1 
ATOM   4838 O O    . LEU   B 1 43  ? 51.210 -16.511 7.487   1.00 13.74 ?  43  LEU   B O    1 
ATOM   4839 C CB   . LEU   B 1 43  ? 48.830 -15.184 7.075   1.00 12.72 ?  43  LEU   B CB   1 
ATOM   4840 C CG   . LEU   B 1 43  ? 47.468 -14.586 6.704   1.00 13.03 ?  43  LEU   B CG   1 
ATOM   4841 C CD1  . LEU   B 1 43  ? 47.672 -13.178 6.129   1.00 14.40 ?  43  LEU   B CD1  1 
ATOM   4842 C CD2  . LEU   B 1 43  ? 46.699 -15.468 5.731   1.00 13.55 ?  43  LEU   B CD2  1 
ATOM   4843 H H    . LEU   B 1 43  ? 47.251 -17.072 8.774   1.00 14.74 ?  43  LEU   B H    1 
ATOM   4844 H HA   . LEU   B 1 43  ? 48.417 -17.180 7.016   1.00 14.53 ?  43  LEU   B HA   1 
ATOM   4845 H HB2  . LEU   B 1 43  ? 49.249 -14.584 7.710   1.00 15.27 ?  43  LEU   B HB2  1 
ATOM   4846 H HB3  . LEU   B 1 43  ? 49.363 -15.211 6.261   1.00 15.27 ?  43  LEU   B HB3  1 
ATOM   4847 H HG   . LEU   B 1 43  ? 46.940 -14.499 7.509   1.00 15.64 ?  43  LEU   B HG   1 
ATOM   4848 H HD11 . LEU   B 1 43  ? 46.803 -12.806 5.901   1.00 17.28 ?  43  LEU   B HD11 1 
ATOM   4849 H HD12 . LEU   B 1 43  ? 48.100 -12.624 6.800   1.00 17.28 ?  43  LEU   B HD12 1 
ATOM   4850 H HD13 . LEU   B 1 43  ? 48.226 -13.235 5.339   1.00 17.28 ?  43  LEU   B HD13 1 
ATOM   4851 H HD21 . LEU   B 1 43  ? 45.890 -15.004 5.455   1.00 16.26 ?  43  LEU   B HD21 1 
ATOM   4852 H HD22 . LEU   B 1 43  ? 47.253 -15.650 4.957   1.00 16.26 ?  43  LEU   B HD22 1 
ATOM   4853 H HD23 . LEU   B 1 43  ? 46.465 -16.299 6.174   1.00 16.26 ?  43  LEU   B HD23 1 
ATOM   4854 N N    . LYS   B 1 44  ? 50.328 -18.217 8.661   1.00 13.19 ?  44  LYS   B N    1 
ATOM   4855 C CA   . LYS   B 1 44  ? 51.596 -18.895 8.916   1.00 13.58 ?  44  LYS   B CA   1 
ATOM   4856 C C    . LYS   B 1 44  ? 51.710 -20.015 7.892   1.00 13.11 ?  44  LYS   B C    1 
ATOM   4857 O O    . LYS   B 1 44  ? 51.017 -21.031 7.981   1.00 14.26 ?  44  LYS   B O    1 
ATOM   4858 C CB   . LYS   B 1 44  ? 51.638 -19.400 10.354  1.00 15.37 ?  44  LYS   B CB   1 
ATOM   4859 C CG   . LYS   B 1 44  ? 51.844 -18.289 11.372  1.00 18.00 ?  44  LYS   B CG   1 
ATOM   4860 C CD   . LYS   B 1 44  ? 53.072 -17.462 10.968  1.00 21.66 ?  44  LYS   B CD   1 
ATOM   4861 C CE   . LYS   B 1 44  ? 53.550 -16.517 12.034  1.00 24.74 ?  44  LYS   B CE   1 
ATOM   4862 N NZ   . LYS   B 1 44  ? 54.762 -15.764 11.628  1.00 25.67 ?  44  LYS   B NZ   1 
ATOM   4863 H H    . LYS   B 1 44  ? 49.654 -18.609 9.023   1.00 15.83 ?  44  LYS   B H    1 
ATOM   4864 H HA   . LYS   B 1 44  ? 52.330 -18.285 8.749   1.00 16.29 ?  44  LYS   B HA   1 
ATOM   4865 H HB2  . LYS   B 1 44  ? 50.788 -19.833 10.558  1.00 18.44 ?  44  LYS   B HB2  1 
ATOM   4866 H HB3  . LYS   B 1 44  ? 52.361 -20.032 10.449  1.00 18.44 ?  44  LYS   B HB3  1 
ATOM   4867 H HG2  . LYS   B 1 44  ? 51.066 -17.713 11.395  1.00 21.60 ?  44  LYS   B HG2  1 
ATOM   4868 H HG3  . LYS   B 1 44  ? 52.007 -18.680 12.250  1.00 21.60 ?  44  LYS   B HG3  1 
ATOM   4869 H HD2  . LYS   B 1 44  ? 53.793 -18.076 10.732  1.00 25.99 ?  44  LYS   B HD2  1 
ATOM   4870 H HD3  . LYS   B 1 44  ? 52.836 -16.924 10.194  1.00 25.99 ?  44  LYS   B HD3  1 
ATOM   4871 H HE2  . LYS   B 1 44  ? 52.849 -15.877 12.206  1.00 29.69 ?  44  LYS   B HE2  1 
ATOM   4872 H HE3  . LYS   B 1 44  ? 53.761 -17.026 12.828  1.00 29.69 ?  44  LYS   B HE3  1 
ATOM   4873 H HZ1  . LYS   B 1 44  ? 55.006 -15.212 12.282  1.00 30.81 ?  44  LYS   B HZ1  1 
ATOM   4874 H HZ2  . LYS   B 1 44  ? 55.431 -16.324 11.456  1.00 30.81 ?  44  LYS   B HZ2  1 
ATOM   4875 H HZ3  . LYS   B 1 44  ? 54.593 -15.284 10.895  1.00 30.81 ?  44  LYS   B HZ3  1 
ATOM   4876 N N    . HIS   B 1 45  ? 52.555 -19.798 6.886   1.00 12.73 ?  45  HIS   B N    1 
ATOM   4877 C CA   . HIS   B 1 45  ? 52.581 -20.640 5.690   1.00 12.82 ?  45  HIS   B CA   1 
ATOM   4878 C C    . HIS   B 1 45  ? 53.602 -21.763 5.854   1.00 14.98 ?  45  HIS   B C    1 
ATOM   4879 O O    . HIS   B 1 45  ? 54.662 -21.783 5.234   1.00 17.81 ?  45  HIS   B O    1 
ATOM   4880 C CB   . HIS   B 1 45  ? 52.893 -19.793 4.469   1.00 12.98 ?  45  HIS   B CB   1 
ATOM   4881 C CG   . HIS   B 1 45  ? 52.027 -18.585 4.354   1.00 12.57 ?  45  HIS   B CG   1 
ATOM   4882 N ND1  . HIS   B 1 45  ? 50.647 -18.658 4.329   1.00 12.95 ?  45  HIS   B ND1  1 
ATOM   4883 C CD2  . HIS   B 1 45  ? 52.345 -17.274 4.263   1.00 13.65 ?  45  HIS   B CD2  1 
ATOM   4884 C CE1  . HIS   B 1 45  ? 50.161 -17.436 4.218   1.00 12.70 ?  45  HIS   B CE1  1 
ATOM   4885 N NE2  . HIS   B 1 45  ? 51.167 -16.581 4.178   1.00 13.38 ?  45  HIS   B NE2  1 
ATOM   4886 H H    . HIS   B 1 45  ? 53.122 -19.149 6.869   1.00 15.28 ?  45  HIS   B H    1 
ATOM   4887 H HA   . HIS   B 1 45  ? 51.699 -21.035 5.566   1.00 15.38 ?  45  HIS   B HA   1 
ATOM   4888 H HB2  . HIS   B 1 45  ? 53.813 -19.500 4.520   1.00 15.57 ?  45  HIS   B HB2  1 
ATOM   4889 H HB3  . HIS   B 1 45  ? 52.762 -20.337 3.673   1.00 15.57 ?  45  HIS   B HB3  1 
ATOM   4890 H HD2  . HIS   B 1 45  ? 53.204 -16.915 4.261   1.00 16.38 ?  45  HIS   B HD2  1 
ATOM   4891 H HE1  . HIS   B 1 45  ? 49.261 -17.217 4.170   1.00 15.24 ?  45  HIS   B HE1  1 
ATOM   4892 H HE2  . HIS   B 1 45  ? 51.095 -15.730 4.113   1.00 16.06 ?  45  HIS   B HE2  1 
ATOM   4893 N N    A GLY   B 1 46  ? 53.241 -22.729 6.693   0.80 16.04 ?  46  GLY   B N    1 
ATOM   4894 N N    B GLY   B 1 46  ? 53.253 -22.711 6.716   0.20 16.09 ?  46  GLY   B N    1 
ATOM   4895 C CA   A GLY   B 1 46  ? 54.175 -23.773 7.076   0.80 18.14 ?  46  GLY   B CA   1 
ATOM   4896 C CA   B GLY   B 1 46  ? 54.178 -23.771 7.059   0.20 17.36 ?  46  GLY   B CA   1 
ATOM   4897 C C    A GLY   B 1 46  ? 54.221 -24.998 6.181   0.80 20.21 ?  46  GLY   B C    1 
ATOM   4898 C C    B GLY   B 1 46  ? 54.207 -24.924 6.076   0.20 18.67 ?  46  GLY   B C    1 
ATOM   4899 O O    A GLY   B 1 46  ? 55.300 -25.434 5.768   0.80 23.91 ?  46  GLY   B O    1 
ATOM   4900 O O    B GLY   B 1 46  ? 55.246 -25.211 5.474   0.20 19.37 ?  46  GLY   B O    1 
ATOM   4901 H H    A GLY   B 1 46  ? 52.465 -22.783 7.072   0.80 19.25 ?  46  GLY   B H    1 
ATOM   4902 H H    B GLY   B 1 46  ? 52.490 -22.753 7.119   0.20 19.31 ?  46  GLY   B H    1 
ATOM   4903 H HA2  A GLY   B 1 46  ? 55.065 -23.391 7.112   0.80 21.76 ?  46  GLY   B HA2  1 
ATOM   4904 H HA2  B GLY   B 1 46  ? 55.071 -23.398 7.114   0.20 20.84 ?  46  GLY   B HA2  1 
ATOM   4905 H HA3  A GLY   B 1 46  ? 53.947 -24.078 7.969   0.80 21.76 ?  46  GLY   B HA3  1 
ATOM   4906 H HA3  B GLY   B 1 46  ? 53.943 -24.118 7.934   0.20 20.84 ?  46  GLY   B HA3  1 
ATOM   4907 N N    . GLY   B 1 47  ? 53.066 -25.586 5.886   1.00 19.45 ?  47  GLY   B N    1 
ATOM   4908 C CA   . GLY   B 1 47  ? 53.008 -26.856 5.190   1.00 17.21 ?  47  GLY   B CA   1 
ATOM   4909 C C    . GLY   B 1 47  ? 52.078 -26.838 3.991   1.00 14.96 ?  47  GLY   B C    1 
ATOM   4910 O O    . GLY   B 1 47  ? 51.408 -25.845 3.712   1.00 14.86 ?  47  GLY   B O    1 
ATOM   4911 H H    A GLY   B 1 47  ? 52.294 -25.268 6.097   0.80 23.34 ?  47  GLY   B H    1 
ATOM   4912 H H    B GLY   B 1 47  ? 52.298 -25.304 6.157   0.20 23.34 ?  47  GLY   B H    1 
ATOM   4913 H HA2  . GLY   B 1 47  ? 53.895 -27.099 4.881   1.00 20.65 ?  47  GLY   B HA2  1 
ATOM   4914 H HA3  . GLY   B 1 47  ? 52.705 -27.540 5.807   1.00 20.65 ?  47  GLY   B HA3  1 
ATOM   4915 N N    . GLY   B 1 48  ? 52.021 -27.982 3.310   1.00 14.47 ?  48  GLY   B N    1 
ATOM   4916 C CA   . GLY   B 1 48  ? 51.096 -28.134 2.202   1.00 14.20 ?  48  GLY   B CA   1 
ATOM   4917 C C    . GLY   B 1 48  ? 51.241 -27.032 1.177   1.00 13.15 ?  48  GLY   B C    1 
ATOM   4918 O O    . GLY   B 1 48  ? 52.344 -26.578 0.864   1.00 13.53 ?  48  GLY   B O    1 
ATOM   4919 H H    . GLY   B 1 48  ? 52.508 -28.665 3.470   1.00 17.36 ?  48  GLY   B H    1 
ATOM   4920 H HA2  . GLY   B 1 48  ? 51.254 -28.987 1.767   1.00 17.04 ?  48  GLY   B HA2  1 
ATOM   4921 H HA3  . GLY   B 1 48  ? 50.184 -28.124 2.534   1.00 17.04 ?  48  GLY   B HA3  1 
ATOM   4922 N N    . VAL   B 1 49  ? 50.099 -26.600 0.641   1.00 13.16 ?  49  VAL   B N    1 
ATOM   4923 C CA   . VAL   B 1 49  ? 50.089 -25.584 -0.407  1.00 12.58 ?  49  VAL   B CA   1 
ATOM   4924 C C    . VAL   B 1 49  ? 50.747 -24.299 0.076   1.00 11.66 ?  49  VAL   B C    1 
ATOM   4925 O O    . VAL   B 1 49  ? 51.538 -23.683 -0.645  1.00 12.70 ?  49  VAL   B O    1 
ATOM   4926 C CB   . VAL   B 1 49  ? 48.646 -25.324 -0.884  1.00 13.79 ?  49  VAL   B CB   1 
ATOM   4927 C CG1  . VAL   B 1 49  ? 48.562 -24.065 -1.747  1.00 13.75 ?  49  VAL   B CG1  1 
ATOM   4928 C CG2  . VAL   B 1 49  ? 48.110 -26.530 -1.646  1.00 16.15 ?  49  VAL   B CG2  1 
ATOM   4929 H H    . VAL   B 1 49  ? 49.313 -26.879 0.866   1.00 15.79 ?  49  VAL   B H    1 
ATOM   4930 H HA   . VAL   B 1 49  ? 50.591 -25.909 -1.169  1.00 15.10 ?  49  VAL   B HA   1 
ATOM   4931 H HB   . VAL   B 1 49  ? 48.074 -25.189 -0.111  1.00 16.55 ?  49  VAL   B HB   1 
ATOM   4932 H HG11 . VAL   B 1 49  ? 47.730 -24.072 -2.244  1.00 16.50 ?  49  VAL   B HG11 1 
ATOM   4933 H HG12 . VAL   B 1 49  ? 48.590 -23.281 -1.169  1.00 16.50 ?  49  VAL   B HG12 1 
ATOM   4934 H HG13 . VAL   B 1 49  ? 49.313 -24.050 -2.359  1.00 16.50 ?  49  VAL   B HG13 1 
ATOM   4935 H HG21 . VAL   B 1 49  ? 47.199 -26.347 -1.933  1.00 19.38 ?  49  VAL   B HG21 1 
ATOM   4936 H HG22 . VAL   B 1 49  ? 48.672 -26.690 -2.420  1.00 19.38 ?  49  VAL   B HG22 1 
ATOM   4937 H HG23 . VAL   B 1 49  ? 48.122 -27.303 -1.061  1.00 19.38 ?  49  VAL   B HG23 1 
ATOM   4938 N N    . ALA   B 1 50  ? 50.393 -23.848 1.281   1.00 11.72 ?  50  ALA   B N    1 
ATOM   4939 C CA   . ALA   B 1 50  ? 50.916 -22.568 1.754   1.00 11.68 ?  50  ALA   B CA   1 
ATOM   4940 C C    . ALA   B 1 50  ? 52.438 -22.598 1.866   1.00 11.78 ?  50  ALA   B C    1 
ATOM   4941 O O    . ALA   B 1 50  ? 53.120 -21.635 1.496   1.00 12.34 ?  50  ALA   B O    1 
ATOM   4942 C CB   . ALA   B 1 50  ? 50.293 -22.209 3.099   1.00 12.49 ?  50  ALA   B CB   1 
ATOM   4943 H H    . ALA   B 1 50  ? 49.861 -24.247 1.825   1.00 14.07 ?  50  ALA   B H    1 
ATOM   4944 H HA   . ALA   B 1 50  ? 50.681 -21.876 1.120   1.00 14.02 ?  50  ALA   B HA   1 
ATOM   4945 H HB1  . ALA   B 1 50  ? 50.653 -21.353 3.393   1.00 14.99 ?  50  ALA   B HB1  1 
ATOM   4946 H HB2  . ALA   B 1 50  ? 49.331 -22.138 2.993   1.00 14.99 ?  50  ALA   B HB2  1 
ATOM   4947 H HB3  . ALA   B 1 50  ? 50.508 -22.896 3.744   1.00 14.99 ?  50  ALA   B HB3  1 
ATOM   4948 N N    . GLY   B 1 51  ? 52.987 -23.689 2.387   1.00 12.54 ?  51  GLY   B N    1 
ATOM   4949 C CA   . GLY   B 1 51  ? 54.431 -23.795 2.460   1.00 13.03 ?  51  GLY   B CA   1 
ATOM   4950 C C    . GLY   B 1 51  ? 55.080 -23.754 1.093   1.00 12.89 ?  51  GLY   B C    1 
ATOM   4951 O O    . GLY   B 1 51  ? 56.130 -23.128 0.915   1.00 13.83 ?  51  GLY   B O    1 
ATOM   4952 H H    . GLY   B 1 51  ? 52.557 -24.366 2.694   1.00 15.05 ?  51  GLY   B H    1 
ATOM   4953 H HA2  . GLY   B 1 51  ? 54.786 -23.061 2.985   1.00 15.63 ?  51  GLY   B HA2  1 
ATOM   4954 H HA3  . GLY   B 1 51  ? 54.676 -24.629 2.890   1.00 15.63 ?  51  GLY   B HA3  1 
ATOM   4955 N N    . ALA   B 1 52  ? 54.481 -24.433 0.112   1.00 12.62 ?  52  ALA   B N    1 
ATOM   4956 C CA   . ALA   B 1 52  ? 55.048 -24.436 -1.232  1.00 13.31 ?  52  ALA   B CA   1 
ATOM   4957 C C    . ALA   B 1 52  ? 54.964 -23.057 -1.881  1.00 12.21 ?  52  ALA   B C    1 
ATOM   4958 O O    . ALA   B 1 52  ? 55.929 -22.601 -2.512  1.00 13.44 ?  52  ALA   B O    1 
ATOM   4959 C CB   . ALA   B 1 52  ? 54.350 -25.473 -2.103  1.00 14.09 ?  52  ALA   B CB   1 
ATOM   4960 H H    . ALA   B 1 52  ? 53.755 -24.893 0.197   1.00 15.14 ?  52  ALA   B H    1 
ATOM   4961 H HA   . ALA   B 1 52  ? 55.984 -24.677 -1.174  1.00 15.98 ?  52  ALA   B HA   1 
ATOM   4962 H HB1  . ALA   B 1 52  ? 54.746 -25.455 -2.992  1.00 16.91 ?  52  ALA   B HB1  1 
ATOM   4963 H HB2  . ALA   B 1 52  ? 54.472 -26.351 -1.708  1.00 16.91 ?  52  ALA   B HB2  1 
ATOM   4964 H HB3  . ALA   B 1 52  ? 53.407 -25.261 -2.159  1.00 16.91 ?  52  ALA   B HB3  1 
ATOM   4965 N N    . LEU   B 1 53  ? 53.819 -22.379 -1.764  1.00 11.94 ?  53  LEU   B N    1 
ATOM   4966 C CA   . LEU   B 1 53  ? 53.710 -21.040 -2.336  1.00 11.99 ?  53  LEU   B CA   1 
ATOM   4967 C C    . LEU   B 1 53  ? 54.721 -20.100 -1.694  1.00 12.06 ?  53  LEU   B C    1 
ATOM   4968 O O    . LEU   B 1 53  ? 55.424 -19.353 -2.387  1.00 12.98 ?  53  LEU   B O    1 
ATOM   4969 C CB   . LEU   B 1 53  ? 52.285 -20.496 -2.174  1.00 13.01 ?  53  LEU   B CB   1 
ATOM   4970 C CG   . LEU   B 1 53  ? 51.145 -21.226 -2.895  1.00 13.27 ?  53  LEU   B CG   1 
ATOM   4971 C CD1  . LEU   B 1 53  ? 49.814 -20.588 -2.557  1.00 14.68 ?  53  LEU   B CD1  1 
ATOM   4972 C CD2  . LEU   B 1 53  ? 51.357 -21.250 -4.400  1.00 15.38 ?  53  LEU   B CD2  1 
ATOM   4973 H H    . LEU   B 1 53  ? 53.116 -22.662 -1.362  1.00 14.32 ?  53  LEU   B H    1 
ATOM   4974 H HA   . LEU   B 1 53  ? 53.910 -21.087 -3.286  1.00 14.39 ?  53  LEU   B HA   1 
ATOM   4975 H HB2  . LEU   B 1 53  ? 52.070 -20.501 -1.231  1.00 15.61 ?  53  LEU   B HB2  1 
ATOM   4976 H HB3  . LEU   B 1 53  ? 52.277 -19.581 -2.497  1.00 15.61 ?  53  LEU   B HB3  1 
ATOM   4977 H HG   . LEU   B 1 53  ? 51.111 -22.142 -2.583  1.00 15.92 ?  53  LEU   B HG   1 
ATOM   4978 H HD11 . LEU   B 1 53  ? 49.105 -21.069 -3.019  1.00 17.62 ?  53  LEU   B HD11 1 
ATOM   4979 H HD12 . LEU   B 1 53  ? 49.669 -20.642 -1.597  1.00 17.62 ?  53  LEU   B HD12 1 
ATOM   4980 H HD13 . LEU   B 1 53  ? 49.821 -19.662 -2.838  1.00 17.62 ?  53  LEU   B HD13 1 
ATOM   4981 H HD21 . LEU   B 1 53  ? 50.642 -21.760 -4.813  1.00 18.46 ?  53  LEU   B HD21 1 
ATOM   4982 H HD22 . LEU   B 1 53  ? 51.348 -20.341 -4.736  1.00 18.46 ?  53  LEU   B HD22 1 
ATOM   4983 H HD23 . LEU   B 1 53  ? 52.211 -21.667 -4.592  1.00 18.46 ?  53  LEU   B HD23 1 
ATOM   4984 N N    . ASN   B 1 54  ? 54.808 -20.120 -0.366  1.00 12.02 ?  54  ASN   B N    1 
ATOM   4985 C CA   . ASN   B 1 54  ? 55.727 -19.214 0.304   1.00 12.55 ?  54  ASN   B CA   1 
ATOM   4986 C C    . ASN   B 1 54  ? 57.168 -19.499 -0.094  1.00 13.18 ?  54  ASN   B C    1 
ATOM   4987 O O    . ASN   B 1 54  ? 57.944 -18.567 -0.338  1.00 13.62 ?  54  ASN   B O    1 
ATOM   4988 C CB   . ASN   B 1 54  ? 55.569 -19.284 1.815   1.00 13.48 ?  54  ASN   B CB   1 
ATOM   4989 C CG   . ASN   B 1 54  ? 56.546 -18.367 2.523   1.00 13.53 ?  54  ASN   B CG   1 
ATOM   4990 O OD1  . ASN   B 1 54  ? 56.571 -17.157 2.277   1.00 14.04 ?  54  ASN   B OD1  1 
ATOM   4991 N ND2  . ASN   B 1 54  ? 57.371 -18.936 3.389   1.00 15.19 ?  54  ASN   B ND2  1 
ATOM   4992 H H    . ASN   B 1 54  ? 54.359 -20.636 0.153   1.00 14.43 ?  54  ASN   B H    1 
ATOM   4993 H HA   . ASN   B 1 54  ? 55.520 -18.306 0.028   1.00 15.06 ?  54  ASN   B HA   1 
ATOM   4994 H HB2  . ASN   B 1 54  ? 54.669 -19.012 2.057   1.00 16.18 ?  54  ASN   B HB2  1 
ATOM   4995 H HB3  . ASN   B 1 54  ? 55.737 -20.191 2.112   1.00 16.18 ?  54  ASN   B HB3  1 
ATOM   4996 H HD21 . ASN   B 1 54  ? 57.952 -18.457 3.811   1.00 18.23 ?  54  ASN   B HD21 1 
ATOM   4997 H HD22 . ASN   B 1 54  ? 57.334 -19.782 3.529   1.00 18.23 ?  54  ASN   B HD22 1 
ATOM   4998 N N    . LYS   B 1 55  ? 57.549 -20.779 -0.154  1.00 13.84 ?  55  LYS   B N    1 
ATOM   4999 C CA   . LYS   B 1 55  ? 58.904 -21.123 -0.570  1.00 14.66 ?  55  LYS   B CA   1 
ATOM   5000 C C    . LYS   B 1 55  ? 59.202 -20.582 -1.964  1.00 14.42 ?  55  LYS   B C    1 
ATOM   5001 O O    . LYS   B 1 55  ? 60.301 -20.070 -2.217  1.00 15.30 ?  55  LYS   B O    1 
ATOM   5002 C CB   . LYS   B 1 55  ? 59.100 -22.638 -0.517  1.00 16.67 ?  55  LYS   B CB   1 
ATOM   5003 C CG   . LYS   B 1 55  ? 60.467 -23.100 -0.973  1.00 21.21 ?  55  LYS   B CG   1 
ATOM   5004 C CD   . LYS   B 1 55  ? 60.635 -24.600 -0.802  1.00 24.79 ?  55  LYS   B CD   1 
ATOM   5005 C CE   . LYS   B 1 55  ? 60.688 -24.996 0.670   1.00 27.80 ?  55  LYS   B CE   1 
ATOM   5006 N NZ   . LYS   B 1 55  ? 61.094 -26.409 0.850   1.00 29.68 ?  55  LYS   B NZ   1 
ATOM   5007 H H    . LYS   B 1 55  ? 57.046 -21.450 0.039   1.00 16.60 ?  55  LYS   B H    1 
ATOM   5008 H HA   . LYS   B 1 55  ? 59.532 -20.721 0.047   1.00 17.59 ?  55  LYS   B HA   1 
ATOM   5009 H HB2  . LYS   B 1 55  ? 58.973 -22.931 0.402   1.00 20.00 ?  55  LYS   B HB2  1 
ATOM   5010 H HB3  . LYS   B 1 55  ? 58.437 -23.061 -1.086  1.00 20.00 ?  55  LYS   B HB3  1 
ATOM   5011 H HG2  . LYS   B 1 55  ? 60.580 -22.888 -1.913  1.00 25.45 ?  55  LYS   B HG2  1 
ATOM   5012 H HG3  . LYS   B 1 55  ? 61.148 -22.653 -0.444  1.00 25.45 ?  55  LYS   B HG3  1 
ATOM   5013 H HD2  . LYS   B 1 55  ? 59.884 -25.059 -1.212  1.00 29.75 ?  55  LYS   B HD2  1 
ATOM   5014 H HD3  . LYS   B 1 55  ? 61.466 -24.882 -1.220  1.00 29.75 ?  55  LYS   B HD3  1 
ATOM   5015 H HE2  . LYS   B 1 55  ? 61.331 -24.427 1.126   1.00 33.36 ?  55  LYS   B HE2  1 
ATOM   5016 H HE3  . LYS   B 1 55  ? 59.806 -24.877 1.061   1.00 33.36 ?  55  LYS   B HE3  1 
ATOM   5017 H HZ1  . LYS   B 1 55  ? 61.104 -26.611 1.717   1.00 35.61 ?  55  LYS   B HZ1  1 
ATOM   5018 H HZ2  . LYS   B 1 55  ? 60.518 -26.944 0.435   1.00 35.61 ?  55  LYS   B HZ2  1 
ATOM   5019 H HZ3  . LYS   B 1 55  ? 61.906 -26.536 0.512   1.00 35.61 ?  55  LYS   B HZ3  1 
ATOM   5020 N N    . ALA   B 1 56  ? 58.234 -20.678 -2.882  1.00 14.07 ?  56  ALA   B N    1 
ATOM   5021 C CA   . ALA   B 1 56  ? 58.455 -20.177 -4.232  1.00 14.85 ?  56  ALA   B CA   1 
ATOM   5022 C C    . ALA   B 1 56  ? 58.740 -18.682 -4.234  1.00 14.26 ?  56  ALA   B C    1 
ATOM   5023 O O    . ALA   B 1 56  ? 59.471 -18.195 -5.104  1.00 15.27 ?  56  ALA   B O    1 
ATOM   5024 C CB   . ALA   B 1 56  ? 57.252 -20.505 -5.122  1.00 16.02 ?  56  ALA   B CB   1 
ATOM   5025 H H    . ALA   B 1 56  ? 57.447 -21.003 -2.745  1.00 16.89 ?  56  ALA   B H    1 
ATOM   5026 H HA   . ALA   B 1 56  ? 59.231 -20.619 -4.605  1.00 17.82 ?  56  ALA   B HA   1 
ATOM   5027 H HB1  . ALA   B 1 56  ? 57.423 -20.172 -6.019  1.00 19.22 ?  56  ALA   B HB1  1 
ATOM   5028 H HB2  . ALA   B 1 56  ? 57.138 -21.470 -5.149  1.00 19.22 ?  56  ALA   B HB2  1 
ATOM   5029 H HB3  . ALA   B 1 56  ? 56.461 -20.086 -4.757  1.00 19.22 ?  56  ALA   B HB3  1 
ATOM   5030 N N    . THR   B 1 57  ? 58.171 -17.937 -3.282  1.00 14.37 ?  57  THR   B N    1 
ATOM   5031 C CA   . THR   B 1 57  ? 58.409 -16.502 -3.174  1.00 14.44 ?  57  THR   B CA   1 
ATOM   5032 C C    . THR   B 1 57  ? 59.661 -16.171 -2.367  1.00 15.53 ?  57  THR   B C    1 
ATOM   5033 O O    . THR   B 1 57  ? 59.912 -14.992 -2.079  1.00 15.96 ?  57  THR   B O    1 
ATOM   5034 C CB   . THR   B 1 57  ? 57.206 -15.772 -2.546  1.00 13.28 ?  57  THR   B CB   1 
ATOM   5035 O OG1  . THR   B 1 57  ? 57.185 -15.981 -1.126  1.00 13.91 ?  57  THR   B OG1  1 
ATOM   5036 C CG2  . THR   B 1 57  ? 55.880 -16.196 -3.189  1.00 13.42 ?  57  THR   B CG2  1 
ATOM   5037 H H    . THR   B 1 57  ? 57.623 -18.247 -2.689  1.00 17.24 ?  57  THR   B H    1 
ATOM   5038 H HA   . THR   B 1 57  ? 58.525 -16.146 -4.070  1.00 17.33 ?  57  THR   B HA   1 
ATOM   5039 H HB   . THR   B 1 57  ? 57.310 -14.821 -2.716  1.00 15.94 ?  57  THR   B HB   1 
ATOM   5040 H HG1  . THR   B 1 57  ? 57.113 -16.800 -0.960  1.00 16.69 ?  57  THR   B HG1  1 
ATOM   5041 H HG21 . THR   B 1 57  ? 55.151 -15.669 -2.833  1.00 16.10 ?  57  THR   B HG21 1 
ATOM   5042 H HG22 . THR   B 1 57  ? 55.919 -16.073 -4.152  1.00 16.10 ?  57  THR   B HG22 1 
ATOM   5043 H HG23 . THR   B 1 57  ? 55.707 -17.135 -3.005  1.00 16.10 ?  57  THR   B HG23 1 
ATOM   5044 N N    . ASN   B 1 58  ? 60.446 -17.175 -1.995  1.00 15.95 ?  58  ASN   B N    1 
ATOM   5045 C CA   . ASN   B 1 58  ? 61.645 -16.960 -1.187  1.00 19.54 ?  58  ASN   B CA   1 
ATOM   5046 C C    . ASN   B 1 58  ? 61.312 -16.241 0.123   1.00 16.57 ?  58  ASN   B C    1 
ATOM   5047 O O    . ASN   B 1 58  ? 62.046 -15.361 0.580   1.00 17.28 ?  58  ASN   B O    1 
ATOM   5048 C CB   . ASN   B 1 58  ? 62.738 -16.224 -1.971  1.00 30.16 ?  58  ASN   B CB   1 
ATOM   5049 C CG   . ASN   B 1 58  ? 64.118 -16.426 -1.373  1.00 41.99 ?  58  ASN   B CG   1 
ATOM   5050 O OD1  . ASN   B 1 58  ? 64.394 -17.455 -0.757  1.00 44.74 ?  58  ASN   B OD1  1 
ATOM   5051 N ND2  . ASN   B 1 58  ? 64.992 -15.443 -1.551  1.00 50.21 ?  58  ASN   B ND2  1 
ATOM   5052 H H    . ASN   B 1 58  ? 60.313 -18.003 -2.209  1.00 19.15 ?  58  ASN   B H    1 
ATOM   5053 H HA   . ASN   B 1 58  ? 62.004 -17.833 -0.962  1.00 23.45 ?  58  ASN   B HA   1 
ATOM   5054 H HB2  . ASN   B 1 58  ? 62.758 -16.553 -2.886  1.00 36.20 ?  58  ASN   B HB2  1 
ATOM   5055 H HB3  . ASN   B 1 58  ? 62.550 -15.274 -1.965  1.00 36.20 ?  58  ASN   B HB3  1 
ATOM   5056 H HD21 . ASN   B 1 58  ? 65.788 -15.512 -1.231  1.00 60.25 ?  58  ASN   B HD21 1 
ATOM   5057 H HD22 . ASN   B 1 58  ? 64.763 -14.738 -1.985  1.00 60.25 ?  58  ASN   B HD22 1 
ATOM   5058 N N    . ASN   B 1 59  ? 60.185 -16.621 0.729   1.00 15.31 ?  59  ASN   B N    1 
ATOM   5059 C CA   . ASN   B 1 59  ? 59.710 -16.139 2.027   1.00 15.12 ?  59  ASN   B CA   1 
ATOM   5060 C C    . ASN   B 1 59  ? 59.121 -14.733 1.963   1.00 14.54 ?  59  ASN   B C    1 
ATOM   5061 O O    . ASN   B 1 59  ? 58.693 -14.219 3.009   1.00 14.84 ?  59  ASN   B O    1 
ATOM   5062 C CB   . ASN   B 1 59  ? 60.786 -16.176 3.127   1.00 16.23 ?  59  ASN   B CB   1 
ATOM   5063 C CG   . ASN   B 1 59  ? 60.203 -16.353 4.511   1.00 17.84 ?  59  ASN   B CG   1 
ATOM   5064 O OD1  . ASN   B 1 59  ? 59.384 -17.246 4.748   1.00 17.41 ?  59  ASN   B OD1  1 
ATOM   5065 N ND2  . ASN   B 1 59  ? 60.624 -15.504 5.438   1.00 18.83 ?  59  ASN   B ND2  1 
ATOM   5066 H H    . ASN   B 1 59  ? 59.641 -17.202 0.383   1.00 18.37 ?  59  ASN   B H    1 
ATOM   5067 H HA   . ASN   B 1 59  ? 59.002 -16.733 2.317   1.00 18.14 ?  59  ASN   B HA   1 
ATOM   5068 H HB2  . ASN   B 1 59  ? 61.388 -16.918 2.964   1.00 19.48 ?  59  ASN   B HB2  1 
ATOM   5069 H HB3  . ASN   B 1 59  ? 61.278 -15.340 3.118   1.00 19.48 ?  59  ASN   B HB3  1 
ATOM   5070 H HD21 . ASN   B 1 59  ? 60.323 -15.560 6.243   1.00 22.60 ?  59  ASN   B HD21 1 
ATOM   5071 H HD22 . ASN   B 1 59  ? 61.194 -14.891 5.238   1.00 22.60 ?  59  ASN   B HD22 1 
ATOM   5072 N N    . ALA   B 1 60  ? 59.053 -14.100 0.787   1.00 14.47 ?  60  ALA   B N    1 
ATOM   5073 C CA   . ALA   B 1 60  ? 58.456 -12.769 0.709   1.00 14.45 ?  60  ALA   B CA   1 
ATOM   5074 C C    . ALA   B 1 60  ? 56.987 -12.798 1.113   1.00 13.78 ?  60  ALA   B C    1 
ATOM   5075 O O    . ALA   B 1 60  ? 56.485 -11.856 1.736   1.00 14.06 ?  60  ALA   B O    1 
ATOM   5076 C CB   . ALA   B 1 60  ? 58.617 -12.199 -0.697  1.00 15.39 ?  60  ALA   B CB   1 
ATOM   5077 H H    . ALA   B 1 60  ? 59.345 -14.420 0.040   1.00 17.37 ?  60  ALA   B H    1 
ATOM   5078 H HA   . ALA   B 1 60  ? 58.923 -12.190 1.326   1.00 17.34 ?  60  ALA   B HA   1 
ATOM   5079 H HB1  . ALA   B 1 60  ? 58.215 -11.320 -0.721  1.00 18.47 ?  60  ALA   B HB1  1 
ATOM   5080 H HB2  . ALA   B 1 60  ? 59.563 -12.141 -0.906  1.00 18.47 ?  60  ALA   B HB2  1 
ATOM   5081 H HB3  . ALA   B 1 60  ? 58.174 -12.788 -1.328  1.00 18.47 ?  60  ALA   B HB3  1 
ATOM   5082 N N    . MET   B 1 61  ? 56.279 -13.875 0.770   1.00 12.85 ?  61  MET   B N    1 
ATOM   5083 C CA   . MET   B 1 61  ? 54.880 -13.996 1.165   1.00 12.55 ?  61  MET   B CA   1 
ATOM   5084 C C    . MET   B 1 61  ? 54.738 -13.989 2.687   1.00 12.50 ?  61  MET   B C    1 
ATOM   5085 O O    . MET   B 1 61  ? 53.832 -13.344 3.230   1.00 12.55 ?  61  MET   B O    1 
ATOM   5086 C CB   . MET   B 1 61  ? 54.294 -15.266 0.544   1.00 12.69 ?  61  MET   B CB   1 
ATOM   5087 C CG   . MET   B 1 61  ? 52.841 -15.541 0.940   1.00 12.10 ?  61  MET   B CG   1 
ATOM   5088 S SD   . MET   B 1 61  ? 52.216 -17.056 0.185   1.00 13.01 ?  61  MET   B SD   1 
ATOM   5089 C CE   . MET   B 1 61  ? 51.955 -16.483 -1.486  1.00 14.04 ?  61  MET   B CE   1 
ATOM   5090 H H    . MET   B 1 61  ? 56.582 -14.549 0.315   1.00 15.42 ?  61  MET   B H    1 
ATOM   5091 H HA   . MET   B 1 61  ? 54.391 -13.247 0.801   1.00 15.06 ?  61  MET   B HA   1 
ATOM   5092 H HB2  . MET   B 1 61  ? 54.329 -15.190 -0.424  1.00 15.23 ?  61  MET   B HB2  1 
ATOM   5093 H HB3  . MET   B 1 61  ? 54.826 -16.030 0.827   1.00 15.23 ?  61  MET   B HB3  1 
ATOM   5094 H HG2  . MET   B 1 61  ? 52.780 -15.641 1.904   1.00 14.52 ?  61  MET   B HG2  1 
ATOM   5095 H HG3  . MET   B 1 61  ? 52.285 -14.799 0.647   1.00 14.52 ?  61  MET   B HG3  1 
ATOM   5096 H HE1  . MET   B 1 61  ? 51.585 -17.206 -2.015  1.00 16.85 ?  61  MET   B HE1  1 
ATOM   5097 H HE2  . MET   B 1 61  ? 51.331 -15.734 -1.473  1.00 16.85 ?  61  MET   B HE2  1 
ATOM   5098 H HE3  . MET   B 1 61  ? 52.801 -16.195 -1.862  1.00 16.85 ?  61  MET   B HE3  1 
ATOM   5099 N N    . GLN   B 1 62  ? 55.622 -14.696 3.397   1.00 12.31 ?  62  GLN   B N    1 
ATOM   5100 C CA   . GLN   B 1 62  ? 55.518 -14.745 4.852   1.00 12.99 ?  62  GLN   B CA   1 
ATOM   5101 C C    . GLN   B 1 62  ? 55.796 -13.384 5.472   1.00 13.24 ?  62  GLN   B C    1 
ATOM   5102 O O    . GLN   B 1 62  ? 55.110 -12.974 6.416   1.00 13.87 ?  62  GLN   B O    1 
ATOM   5103 C CB   . GLN   B 1 62  ? 56.476 -15.789 5.429   1.00 13.64 ?  62  GLN   B CB   1 
ATOM   5104 C CG   . GLN   B 1 62  ? 56.243 -16.062 6.909   1.00 14.11 ?  62  GLN   B CG   1 
ATOM   5105 C CD   . GLN   B 1 62  ? 54.867 -16.657 7.149   1.00 13.71 ?  62  GLN   B CD   1 
ATOM   5106 O OE1  . GLN   B 1 62  ? 54.607 -17.806 6.786   1.00 14.33 ?  62  GLN   B OE1  1 
ATOM   5107 N NE2  . GLN   B 1 62  ? 53.959 -15.864 7.715   1.00 13.66 ?  62  GLN   B NE2  1 
ATOM   5108 H H    . GLN   B 1 62  ? 56.279 -15.143 3.066   1.00 14.78 ?  62  GLN   B H    1 
ATOM   5109 H HA   . GLN   B 1 62  ? 54.612 -15.004 5.090   1.00 15.59 ?  62  GLN   B HA   1 
ATOM   5110 H HB2  . GLN   B 1 62  ? 56.359 -16.627 4.953   1.00 16.37 ?  62  GLN   B HB2  1 
ATOM   5111 H HB3  . GLN   B 1 62  ? 57.387 -15.474 5.325   1.00 16.37 ?  62  GLN   B HB3  1 
ATOM   5112 H HG2  . GLN   B 1 62  ? 56.905 -16.691 7.227   1.00 16.93 ?  62  GLN   B HG2  1 
ATOM   5113 H HG3  . GLN   B 1 62  ? 56.305 -15.228 7.402   1.00 16.93 ?  62  GLN   B HG3  1 
ATOM   5114 H HE21 . GLN   B 1 62  ? 54.173 -15.063 7.945   1.00 16.40 ?  62  GLN   B HE21 1 
ATOM   5115 H HE22 . GLN   B 1 62  ? 53.168 -16.160 7.861   1.00 16.40 ?  62  GLN   B HE22 1 
ATOM   5116 N N    . VAL   B 1 63  ? 56.815 -12.679 4.980   1.00 14.03 ?  63  VAL   B N    1 
ATOM   5117 C CA   . VAL   B 1 63  ? 57.119 -11.353 5.522   1.00 15.02 ?  63  VAL   B CA   1 
ATOM   5118 C C    . VAL   B 1 63  ? 55.925 -10.421 5.336   1.00 14.37 ?  63  VAL   B C    1 
ATOM   5119 O O    . VAL   B 1 63  ? 55.507 -9.715  6.265   1.00 14.87 ?  63  VAL   B O    1 
ATOM   5120 C CB   . VAL   B 1 63  ? 58.411 -10.801 4.896   1.00 16.33 ?  63  VAL   B CB   1 
ATOM   5121 C CG1  . VAL   B 1 63  ? 58.647 -9.357  5.335   1.00 16.87 ?  63  VAL   B CG1  1 
ATOM   5122 C CG2  . VAL   B 1 63  ? 59.602 -11.674 5.293   1.00 17.24 ?  63  VAL   B CG2  1 
ATOM   5123 H H    . VAL   B 1 63  ? 57.326 -12.941 4.338   1.00 16.83 ?  63  VAL   B H    1 
ATOM   5124 H HA   . VAL   B 1 63  ? 57.276 -11.446 6.471   1.00 18.02 ?  63  VAL   B HA   1 
ATOM   5125 H HB   . VAL   B 1 63  ? 58.342 -10.822 3.928   1.00 19.60 ?  63  VAL   B HB   1 
ATOM   5126 H HG11 . VAL   B 1 63  ? 59.564 -9.111  5.132   1.00 20.25 ?  63  VAL   B HG11 1 
ATOM   5127 H HG12 . VAL   B 1 63  ? 58.036 -8.779  4.855   1.00 20.25 ?  63  VAL   B HG12 1 
ATOM   5128 H HG13 . VAL   B 1 63  ? 58.492 -9.291  6.290   1.00 20.25 ?  63  VAL   B HG13 1 
ATOM   5129 H HG21 . VAL   B 1 63  ? 60.413 -11.303 4.908   1.00 20.68 ?  63  VAL   B HG21 1 
ATOM   5130 H HG22 . VAL   B 1 63  ? 59.676 -11.683 6.263   1.00 20.68 ?  63  VAL   B HG22 1 
ATOM   5131 H HG23 . VAL   B 1 63  ? 59.463 -12.575 4.966   1.00 20.68 ?  63  VAL   B HG23 1 
ATOM   5132 N N    . GLU   B 1 64  ? 55.356 -10.414 4.132   1.00 13.74 ?  64  GLU   B N    1 
ATOM   5133 C CA   . GLU   B 1 64  ? 54.192 -9.580  3.854   1.00 13.31 ?  64  GLU   B CA   1 
ATOM   5134 C C    . GLU   B 1 64  ? 53.009 -9.980  4.729   1.00 13.04 ?  64  GLU   B C    1 
ATOM   5135 O O    . GLU   B 1 64  ? 52.259 -9.123  5.226   1.00 13.42 ?  64  GLU   B O    1 
ATOM   5136 C CB   . GLU   B 1 64  ? 53.830 -9.752  2.382   1.00 13.68 ?  64  GLU   B CB   1 
ATOM   5137 C CG   . GLU   B 1 64  ? 52.564 -9.015  1.949   1.00 13.86 ?  64  GLU   B CG   1 
ATOM   5138 C CD   . GLU   B 1 64  ? 52.044 -9.495  0.606   1.00 14.85 ?  64  GLU   B CD   1 
ATOM   5139 O OE1  . GLU   B 1 64  ? 52.213 -10.701 0.295   1.00 15.86 ?  64  GLU   B OE1  1 
ATOM   5140 O OE2  . GLU   B 1 64  ? 51.425 -8.683  -0.125  1.00 15.11 -1 64  GLU   B OE2  1 
ATOM   5141 H H    . GLU   B 1 64  ? 55.627 -10.884 3.457   1.00 16.49 ?  64  GLU   B H    1 
ATOM   5142 H HA   . GLU   B 1 64  ? 54.408 -8.649  4.017   1.00 15.97 ?  64  GLU   B HA   1 
ATOM   5143 H HB2  . GLU   B 1 64  ? 54.558 -9.413  1.836   1.00 16.42 ?  64  GLU   B HB2  1 
ATOM   5144 H HB3  . GLU   B 1 64  ? 53.698 -10.695 2.202   1.00 16.42 ?  64  GLU   B HB3  1 
ATOM   5145 H HG2  . GLU   B 1 64  ? 51.862 -9.164  2.608   1.00 16.64 ?  64  GLU   B HG2  1 
ATOM   5146 H HG3  . GLU   B 1 64  ? 52.758 -8.072  1.881   1.00 16.64 ?  64  GLU   B HG3  1 
ATOM   5147 N N    . SER   B 1 65  ? 52.829 -11.287 4.918   1.00 12.67 ?  65  SER   B N    1 
ATOM   5148 C CA   . SER   B 1 65  ? 51.720 -11.797 5.714   1.00 12.75 ?  65  SER   B CA   1 
ATOM   5149 C C    . SER   B 1 65  ? 51.841 -11.391 7.177   1.00 13.03 ?  65  SER   B C    1 
ATOM   5150 O O    . SER   B 1 65  ? 50.840 -11.007 7.803   1.00 13.26 ?  65  SER   B O    1 
ATOM   5151 C CB   . SER   B 1 65  ? 51.649 -13.317 5.584   1.00 13.01 ?  65  SER   B CB   1 
ATOM   5152 O OG   . SER   B 1 65  ? 51.275 -13.723 4.276   1.00 13.10 ?  65  SER   B OG   1 
ATOM   5153 H H    . SER   B 1 65  ? 53.340 -11.904 4.593   1.00 15.21 ?  65  SER   B H    1 
ATOM   5154 H HA   . SER   B 1 65  ? 50.892 -11.429 5.373   1.00 15.30 ?  65  SER   B HA   1 
ATOM   5155 H HB2  . SER   B 1 65  ? 52.517 -13.692 5.786   1.00 15.62 ?  65  SER   B HB2  1 
ATOM   5156 H HB3  . SER   B 1 65  ? 50.989 -13.651 6.217   1.00 15.62 ?  65  SER   B HB3  1 
ATOM   5157 H HG   . SER   B 1 65  ? 51.826 -13.428 3.712   1.00 15.72 ?  65  SER   B HG   1 
ATOM   5158 N N    . ASP   B 1 66  ? 53.049 -11.485 7.750   1.00 13.22 ?  66  ASP   B N    1 
ATOM   5159 C CA   . ASP   B 1 66  ? 53.231 -11.089 9.145   1.00 13.33 ?  66  ASP   B CA   1 
ATOM   5160 C C    . ASP   B 1 66  ? 52.919 -9.610  9.341   1.00 13.87 ?  66  ASP   B C    1 
ATOM   5161 O O    . ASP   B 1 66  ? 52.339 -9.218  10.360  1.00 14.34 ?  66  ASP   B O    1 
ATOM   5162 C CB   . ASP   B 1 66  ? 54.657 -11.397 9.604   1.00 14.94 ?  66  ASP   B CB   1 
ATOM   5163 C CG   . ASP   B 1 66  ? 54.921 -12.892 9.765   1.00 16.87 ?  66  ASP   B CG   1 
ATOM   5164 O OD1  . ASP   B 1 66  ? 53.971 -13.704 9.696   1.00 17.74 ?  66  ASP   B OD1  1 
ATOM   5165 O OD2  . ASP   B 1 66  ? 56.098 -13.260 9.975   1.00 19.77 -1 66  ASP   B OD2  1 
ATOM   5166 H H    . ASP   B 1 66  ? 53.761 -11.778 7.363   1.00 15.87 ?  66  ASP   B H    1 
ATOM   5167 H HA   . ASP   B 1 66  ? 52.628 -11.597 9.706   1.00 16.00 ?  66  ASP   B HA   1 
ATOM   5168 H HB2  . ASP   B 1 66  ? 55.289 -11.053 8.953   1.00 17.92 ?  66  ASP   B HB2  1 
ATOM   5169 H HB3  . ASP   B 1 66  ? 54.817 -10.972 10.469  1.00 17.92 ?  66  ASP   B HB3  1 
ATOM   5170 N N    . ASP   B 1 67  ? 53.303 -8.772  8.379   1.00 13.13 ?  67  ASP   B N    1 
ATOM   5171 C CA   . ASP   B 1 67  ? 52.952 -7.360  8.458   1.00 14.25 ?  67  ASP   B CA   1 
ATOM   5172 C C    . ASP   B 1 67  ? 51.439 -7.154  8.373   1.00 14.42 ?  67  ASP   B C    1 
ATOM   5173 O O    . ASP   B 1 67  ? 50.874 -6.340  9.114   1.00 14.87 ?  67  ASP   B O    1 
ATOM   5174 C CB   . ASP   B 1 67  ? 53.662 -6.596  7.349   1.00 15.93 ?  67  ASP   B CB   1 
ATOM   5175 C CG   . ASP   B 1 67  ? 53.237 -5.152  7.294   1.00 16.96 ?  67  ASP   B CG   1 
ATOM   5176 O OD1  . ASP   B 1 67  ? 53.726 -4.333  8.110   1.00 18.30 ?  67  ASP   B OD1  1 
ATOM   5177 O OD2  . ASP   B 1 67  ? 52.385 -4.844  6.450   1.00 18.12 -1 67  ASP   B OD2  1 
ATOM   5178 H H    . ASP   B 1 67  ? 53.758 -8.995  7.683   1.00 15.76 ?  67  ASP   B H    1 
ATOM   5179 H HA   . ASP   B 1 67  ? 53.256 -7.006  9.308   1.00 17.09 ?  67  ASP   B HA   1 
ATOM   5180 H HB2  . ASP   B 1 67  ? 54.620 -6.627  7.503   1.00 19.12 ?  67  ASP   B HB2  1 
ATOM   5181 H HB3  . ASP   B 1 67  ? 53.452 -7.010  6.494   1.00 19.12 ?  67  ASP   B HB3  1 
ATOM   5182 N N    . TYR   B 1 68  ? 50.762 -7.887  7.479   1.00 13.97 ?  68  TYR   B N    1 
ATOM   5183 C CA   . TYR   B 1 68  ? 49.305 -7.805  7.398   1.00 14.54 ?  68  TYR   B CA   1 
ATOM   5184 C C    . TYR   B 1 68  ? 48.671 -8.151  8.742   1.00 14.57 ?  68  TYR   B C    1 
ATOM   5185 O O    . TYR   B 1 68  ? 47.741 -7.469  9.191   1.00 15.35 ?  68  TYR   B O    1 
ATOM   5186 C CB   . TYR   B 1 68  ? 48.771 -8.734  6.296   1.00 15.34 ?  68  TYR   B CB   1 
ATOM   5187 C CG   . TYR   B 1 68  ? 47.265 -8.880  6.348   1.00 16.67 ?  68  TYR   B CG   1 
ATOM   5188 C CD1  . TYR   B 1 68  ? 46.670 -9.834  7.167   1.00 17.57 ?  68  TYR   B CD1  1 
ATOM   5189 C CD2  . TYR   B 1 68  ? 46.436 -8.040  5.617   1.00 18.02 ?  68  TYR   B CD2  1 
ATOM   5190 C CE1  . TYR   B 1 68  ? 45.307 -9.952  7.255   1.00 19.08 ?  68  TYR   B CE1  1 
ATOM   5191 C CE2  . TYR   B 1 68  ? 45.051 -8.161  5.695   1.00 18.74 ?  68  TYR   B CE2  1 
ATOM   5192 C CZ   . TYR   B 1 68  ? 44.512 -9.122  6.517   1.00 19.15 ?  68  TYR   B CZ   1 
ATOM   5193 O OH   . TYR   B 1 68  ? 43.147 -9.250  6.626   1.00 20.96 ?  68  TYR   B OH   1 
ATOM   5194 H H    . TYR   B 1 68  ? 51.119 -8.442  6.923   1.00 16.77 ?  68  TYR   B H    1 
ATOM   5195 H HA   . TYR   B 1 68  ? 49.056 -6.899  7.176   1.00 17.45 ?  68  TYR   B HA   1 
ATOM   5196 H HB2  . TYR   B 1 68  ? 49.003 -8.363  5.431   1.00 18.41 ?  68  TYR   B HB2  1 
ATOM   5197 H HB3  . TYR   B 1 68  ? 49.161 -9.614  6.400   1.00 18.41 ?  68  TYR   B HB3  1 
ATOM   5198 H HD1  . TYR   B 1 68  ? 47.208 -10.405 7.669   1.00 21.09 ?  68  TYR   B HD1  1 
ATOM   5199 H HD2  . TYR   B 1 68  ? 46.809 -7.384  5.076   1.00 21.63 ?  68  TYR   B HD2  1 
ATOM   5200 H HE1  . TYR   B 1 68  ? 44.924 -10.607 7.799   1.00 22.89 ?  68  TYR   B HE1  1 
ATOM   5201 H HE2  . TYR   B 1 68  ? 44.489 -7.595  5.211   1.00 22.49 ?  68  TYR   B HE2  1 
ATOM   5202 H HH   . TYR   B 1 68  ? 42.747 -8.700  6.128   1.00 25.15 ?  68  TYR   B HH   1 
ATOM   5203 N N    . ILE   B 1 69  ? 49.157 -9.213  9.395   1.00 14.01 ?  69  ILE   B N    1 
ATOM   5204 C CA   . ILE   B 1 69  ? 48.590 -9.634  10.674  1.00 14.69 ?  69  ILE   B CA   1 
ATOM   5205 C C    . ILE   B 1 69  ? 48.847 -8.588  11.750  1.00 14.54 ?  69  ILE   B C    1 
ATOM   5206 O O    . ILE   B 1 69  ? 47.979 -8.309  12.586  1.00 14.63 ?  69  ILE   B O    1 
ATOM   5207 C CB   . ILE   B 1 69  ? 49.164 -11.008 11.074  1.00 15.58 ?  69  ILE   B CB   1 
ATOM   5208 C CG1  . ILE   B 1 69  ? 48.642 -12.117 10.153  1.00 16.11 ?  69  ILE   B CG1  1 
ATOM   5209 C CG2  . ILE   B 1 69  ? 48.881 -11.322 12.546  1.00 16.46 ?  69  ILE   B CG2  1 
ATOM   5210 C CD1  . ILE   B 1 69  ? 47.166 -12.433 10.309  1.00 16.79 ?  69  ILE   B CD1  1 
ATOM   5211 H H    . ILE   B 1 69  ? 49.800 -9.708  9.116   1.00 16.82 ?  69  ILE   B H    1 
ATOM   5212 H HA   . ILE   B 1 69  ? 47.629 -9.731  10.578  1.00 17.63 ?  69  ILE   B HA   1 
ATOM   5213 H HB   . ILE   B 1 69  ? 50.125 -10.969 10.965  1.00 18.69 ?  69  ILE   B HB   1 
ATOM   5214 H HG12 . ILE   B 1 69  ? 48.789 -11.851 9.232   1.00 19.33 ?  69  ILE   B HG12 1 
ATOM   5215 H HG13 . ILE   B 1 69  ? 49.137 -12.934 10.336  1.00 19.33 ?  69  ILE   B HG13 1 
ATOM   5216 H HG21 . ILE   B 1 69  ? 49.029 -12.269 12.700  1.00 19.75 ?  69  ILE   B HG21 1 
ATOM   5217 H HG22 . ILE   B 1 69  ? 49.486 -10.805 13.104  1.00 19.75 ?  69  ILE   B HG22 1 
ATOM   5218 H HG23 . ILE   B 1 69  ? 47.962 -11.094 12.750  1.00 19.75 ?  69  ILE   B HG23 1 
ATOM   5219 H HD11 . ILE   B 1 69  ? 46.935 -13.154 9.699   1.00 20.15 ?  69  ILE   B HD11 1 
ATOM   5220 H HD12 . ILE   B 1 69  ? 46.994 -12.710 11.222  1.00 20.15 ?  69  ILE   B HD12 1 
ATOM   5221 H HD13 . ILE   B 1 69  ? 46.648 -11.644 10.096  1.00 20.15 ?  69  ILE   B HD13 1 
ATOM   5222 N N    . ALA   B 1 70  ? 50.040 -7.996  11.761  1.00 14.30 ?  70  ALA   B N    1 
ATOM   5223 C CA   . ALA   B 1 70  ? 50.325 -6.968  12.755  1.00 14.43 ?  70  ALA   B CA   1 
ATOM   5224 C C    . ALA   B 1 70  ? 49.323 -5.827  12.653  1.00 15.21 ?  70  ALA   B C    1 
ATOM   5225 O O    . ALA   B 1 70  ? 48.881 -5.279  13.669  1.00 15.36 ?  70  ALA   B O    1 
ATOM   5226 C CB   . ALA   B 1 70  ? 51.752 -6.448  12.584  1.00 14.91 ?  70  ALA   B CB   1 
ATOM   5227 H H    . ALA   B 1 70  ? 50.679 -8.170  11.219  1.00 17.16 ?  70  ALA   B H    1 
ATOM   5228 H HA   . ALA   B 1 70  ? 50.252 -7.355  13.643  1.00 17.31 ?  70  ALA   B HA   1 
ATOM   5229 H HB1  . ALA   B 1 70  ? 51.938 -5.797  13.283  1.00 17.90 ?  70  ALA   B HB1  1 
ATOM   5230 H HB2  . ALA   B 1 70  ? 52.374 -7.191  12.660  1.00 17.90 ?  70  ALA   B HB2  1 
ATOM   5231 H HB3  . ALA   B 1 70  ? 51.840 -6.033  11.714  1.00 17.90 ?  70  ALA   B HB3  1 
ATOM   5232 N N    . THR   B 1 71  ? 48.946 -5.462  11.431  1.00 15.38 ?  71  THR   B N    1 
ATOM   5233 C CA   . THR   B 1 71  ? 48.051 -4.331  11.213  1.00 16.18 ?  71  THR   B CA   1 
ATOM   5234 C C    . THR   B 1 71  ? 46.582 -4.698  11.418  1.00 16.73 ?  71  THR   B C    1 
ATOM   5235 O O    . THR   B 1 71  ? 45.802 -3.887  11.937  1.00 18.11 ?  71  THR   B O    1 
ATOM   5236 C CB   . THR   B 1 71  ? 48.278 -3.773  9.805   1.00 18.03 ?  71  THR   B CB   1 
ATOM   5237 O OG1  . THR   B 1 71  ? 49.609 -3.253  9.708   1.00 20.36 ?  71  THR   B OG1  1 
ATOM   5238 C CG2  . THR   B 1 71  ? 47.271 -2.684  9.469   1.00 19.06 ?  71  THR   B CG2  1 
ATOM   5239 H H    . THR   B 1 71  ? 49.197 -5.857  10.708  1.00 18.45 ?  71  THR   B H    1 
ATOM   5240 H HA   . THR   B 1 71  ? 48.273 -3.633  11.846  1.00 19.42 ?  71  THR   B HA   1 
ATOM   5241 H HB   . THR   B 1 71  ? 48.186 -4.482  9.154   1.00 21.64 ?  71  THR   B HB   1 
ATOM   5242 H HG1  . THR   B 1 71  ? 49.743 -2.918  8.945   1.00 24.43 ?  71  THR   B HG1  1 
ATOM   5243 H HG21 . THR   B 1 71  ? 47.577 -2.174  8.699   1.00 22.87 ?  71  THR   B HG21 1 
ATOM   5244 H HG22 . THR   B 1 71  ? 46.412 -3.077  9.262   1.00 22.87 ?  71  THR   B HG22 1 
ATOM   5245 H HG23 . THR   B 1 71  ? 47.173 -2.078  10.221  1.00 22.87 ?  71  THR   B HG23 1 
ATOM   5246 N N    . ASN   B 1 72  ? 46.187 -5.908  11.023  1.00 16.41 ?  72  ASN   B N    1 
ATOM   5247 C CA   . ASN   B 1 72  ? 44.784 -6.270  10.901  1.00 16.83 ?  72  ASN   B CA   1 
ATOM   5248 C C    . ASN   B 1 72  ? 44.316 -7.357  11.856  1.00 17.31 ?  72  ASN   B C    1 
ATOM   5249 O O    . ASN   B 1 72  ? 43.101 -7.515  12.026  1.00 18.90 ?  72  ASN   B O    1 
ATOM   5250 C CB   . ASN   B 1 72  ? 44.477 -6.706  9.461   1.00 17.58 ?  72  ASN   B CB   1 
ATOM   5251 C CG   . ASN   B 1 72  ? 44.749 -5.604  8.457   1.00 18.83 ?  72  ASN   B CG   1 
ATOM   5252 O OD1  . ASN   B 1 72  ? 45.770 -5.608  7.759   1.00 20.06 ?  72  ASN   B OD1  1 
ATOM   5253 N ND2  . ASN   B 1 72  ? 43.855 -4.639  8.401   1.00 20.50 ?  72  ASN   B ND2  1 
ATOM   5254 H H    . ASN   B 1 72  ? 46.727 -6.556  10.820  1.00 19.69 ?  72  ASN   B H    1 
ATOM   5255 H HA   . ASN   B 1 72  ? 44.252 -5.483  11.082  1.00 20.20 ?  72  ASN   B HA   1 
ATOM   5256 H HB2  . ASN   B 1 72  ? 45.037 -7.467  9.234   1.00 21.10 ?  72  ASN   B HB2  1 
ATOM   5257 H HB3  . ASN   B 1 72  ? 43.542 -6.950  9.396   1.00 21.10 ?  72  ASN   B HB3  1 
ATOM   5258 H HD21 . ASN   B 1 72  ? 43.960 -3.988  7.848   1.00 24.61 ?  72  ASN   B HD21 1 
ATOM   5259 H HD22 . ASN   B 1 72  ? 43.157 -4.664  8.905   1.00 24.61 ?  72  ASN   B HD22 1 
ATOM   5260 N N    . GLY   B 1 73  ? 45.220 -8.098  12.485  1.00 16.68 ?  73  GLY   B N    1 
ATOM   5261 C CA   . GLY   B 1 73  ? 44.833 -9.238  13.277  1.00 16.32 ?  73  GLY   B CA   1 
ATOM   5262 C C    . GLY   B 1 73  ? 44.482 -10.432 12.414  1.00 14.86 ?  73  GLY   B C    1 
ATOM   5263 O O    . GLY   B 1 73  ? 44.473 -10.361 11.181  1.00 14.55 ?  73  GLY   B O    1 
ATOM   5264 H H    . GLY   B 1 73  ? 46.068 -7.948  12.474  1.00 20.01 ?  73  GLY   B H    1 
ATOM   5265 H HA2  . GLY   B 1 73  ? 45.563 -9.483  13.868  1.00 19.58 ?  73  GLY   B HA2  1 
ATOM   5266 H HA3  . GLY   B 1 73  ? 44.061 -9.010  13.819  1.00 19.58 ?  73  GLY   B HA3  1 
ATOM   5267 N N    . PRO   B 1 74  ? 44.174 -11.555 13.060  1.00 15.32 ?  74  PRO   B N    1 
ATOM   5268 C CA   . PRO   B 1 74  ? 43.907 -12.792 12.323  1.00 14.63 ?  74  PRO   B CA   1 
ATOM   5269 C C    . PRO   B 1 74  ? 42.616 -12.732 11.524  1.00 14.02 ?  74  PRO   B C    1 
ATOM   5270 O O    . PRO   B 1 74  ? 41.678 -11.998 11.848  1.00 15.35 ?  74  PRO   B O    1 
ATOM   5271 C CB   . PRO   B 1 74  ? 43.805 -13.843 13.435  1.00 15.97 ?  74  PRO   B CB   1 
ATOM   5272 C CG   . PRO   B 1 74  ? 43.384 -13.075 14.640  1.00 17.33 ?  74  PRO   B CG   1 
ATOM   5273 C CD   . PRO   B 1 74  ? 44.074 -11.748 14.516  1.00 16.62 ?  74  PRO   B CD   1 
ATOM   5274 H HA   . PRO   B 1 74  ? 44.653 -13.002 11.737  1.00 17.55 ?  74  PRO   B HA   1 
ATOM   5275 H HB2  . PRO   B 1 74  ? 43.135 -14.502 13.195  1.00 19.16 ?  74  PRO   B HB2  1 
ATOM   5276 H HB3  . PRO   B 1 74  ? 44.668 -14.259 13.574  1.00 19.16 ?  74  PRO   B HB3  1 
ATOM   5277 H HG2  . PRO   B 1 74  ? 42.420 -12.961 14.637  1.00 20.80 ?  74  PRO   B HG2  1 
ATOM   5278 H HG3  . PRO   B 1 74  ? 43.674 -13.538 15.440  1.00 20.80 ?  74  PRO   B HG3  1 
ATOM   5279 H HD2  . PRO   B 1 74  ? 43.531 -11.047 14.921  1.00 19.94 ?  74  PRO   B HD2  1 
ATOM   5280 H HD3  . PRO   B 1 74  ? 44.956 -11.784 14.917  1.00 19.94 ?  74  PRO   B HD3  1 
ATOM   5281 N N    . LEU   B 1 75  ? 42.583 -13.538 10.469  1.00 13.65 ?  75  LEU   B N    1 
ATOM   5282 C CA   . LEU   B 1 75  ? 41.376 -13.756 9.695   1.00 13.12 ?  75  LEU   B CA   1 
ATOM   5283 C C    . LEU   B 1 75  ? 40.394 -14.609 10.494  1.00 13.73 ?  75  LEU   B C    1 
ATOM   5284 O O    . LEU   B 1 75  ? 40.731 -15.195 11.522  1.00 14.62 ?  75  LEU   B O    1 
ATOM   5285 C CB   . LEU   B 1 75  ? 41.709 -14.480 8.392   1.00 13.33 ?  75  LEU   B CB   1 
ATOM   5286 C CG   . LEU   B 1 75  ? 42.525 -13.709 7.352   1.00 15.43 ?  75  LEU   B CG   1 
ATOM   5287 C CD1  . LEU   B 1 75  ? 42.697 -14.521 6.071   1.00 16.72 ?  75  LEU   B CD1  1 
ATOM   5288 C CD2  . LEU   B 1 75  ? 41.902 -12.376 7.052   1.00 19.68 ?  75  LEU   B CD2  1 
ATOM   5289 H H    . LEU   B 1 75  ? 43.265 -13.982 10.180  1.00 16.37 ?  75  LEU   B H    1 
ATOM   5290 H HA   . LEU   B 1 75  ? 40.958 -12.907 9.491   1.00 15.74 ?  75  LEU   B HA   1 
ATOM   5291 H HB2  . LEU   B 1 75  ? 42.216 -15.282 8.612   1.00 16.00 ?  75  LEU   B HB2  1 
ATOM   5292 H HB3  . LEU   B 1 75  ? 40.878 -14.739 7.966   1.00 16.00 ?  75  LEU   B HB3  1 
ATOM   5293 H HG   . LEU   B 1 75  ? 43.411 -13.544 7.714   1.00 18.51 ?  75  LEU   B HG   1 
ATOM   5294 H HD11 . LEU   B 1 75  ? 43.226 -14.006 5.437   1.00 20.06 ?  75  LEU   B HD11 1 
ATOM   5295 H HD12 . LEU   B 1 75  ? 43.154 -15.352 6.279   1.00 20.06 ?  75  LEU   B HD12 1 
ATOM   5296 H HD13 . LEU   B 1 75  ? 41.824 -14.708 5.694   1.00 20.06 ?  75  LEU   B HD13 1 
ATOM   5297 H HD21 . LEU   B 1 75  ? 42.340 -11.988 6.279   1.00 23.61 ?  75  LEU   B HD21 1 
ATOM   5298 H HD22 . LEU   B 1 75  ? 40.960 -12.504 6.871   1.00 23.61 ?  75  LEU   B HD22 1 
ATOM   5299 H HD23 . LEU   B 1 75  ? 42.015 -11.792 7.821   1.00 23.61 ?  75  LEU   B HD23 1 
ATOM   5300 N N    . LYS   B 1 76  ? 39.159 -14.673 9.998   1.00 15.30 ?  76  LYS   B N    1 
ATOM   5301 C CA   . LYS   B 1 76  ? 38.166 -15.619 10.485  1.00 16.61 ?  76  LYS   B CA   1 
ATOM   5302 C C    . LYS   B 1 76  ? 38.257 -16.900 9.665   1.00 15.31 ?  76  LYS   B C    1 
ATOM   5303 O O    . LYS   B 1 76  ? 38.538 -16.862 8.468   1.00 14.87 ?  76  LYS   B O    1 
ATOM   5304 C CB   . LYS   B 1 76  ? 36.750 -15.052 10.293  1.00 18.32 ?  76  LYS   B CB   1 
ATOM   5305 C CG   . LYS   B 1 76  ? 36.457 -13.681 10.924  1.00 19.94 ?  76  LYS   B CG   1 
ATOM   5306 C CD   . LYS   B 1 76  ? 35.052 -13.177 10.545  1.00 21.36 ?  76  LYS   B CD   1 
ATOM   5307 C CE   . LYS   B 1 76  ? 34.773 -11.796 11.128  1.00 23.59 ?  76  LYS   B CE   1 
ATOM   5308 N NZ   . LYS   B 1 76  ? 33.503 -11.186 10.639  1.00 24.05 ?  76  LYS   B NZ   1 
ATOM   5309 H H    . LYS   B 1 76  ? 38.877 -14.176 9.358   1.00 18.36 ?  76  LYS   B H    1 
ATOM   5310 H HA   . LYS   B 1 76  ? 38.319 -15.828 11.420  1.00 19.93 ?  76  LYS   B HA   1 
ATOM   5311 H HB2  . LYS   B 1 76  ? 36.589 -14.973 9.340   1.00 21.99 ?  76  LYS   B HB2  1 
ATOM   5312 H HB3  . LYS   B 1 76  ? 36.123 -15.685 10.673  1.00 21.99 ?  76  LYS   B HB3  1 
ATOM   5313 H HG2  . LYS   B 1 76  ? 36.508 -13.758 11.889  1.00 23.93 ?  76  LYS   B HG2  1 
ATOM   5314 H HG3  . LYS   B 1 76  ? 37.112 -13.038 10.604  1.00 23.93 ?  76  LYS   B HG3  1 
ATOM   5315 H HD2  . LYS   B 1 76  ? 34.984 -13.122 9.577   1.00 25.63 ?  76  LYS   B HD2  1 
ATOM   5316 H HD3  . LYS   B 1 76  ? 34.389 -13.797 10.890  1.00 25.63 ?  76  LYS   B HD3  1 
ATOM   5317 H HE2  . LYS   B 1 76  ? 34.713 -11.872 12.091  1.00 28.30 ?  76  LYS   B HE2  1 
ATOM   5318 H HE3  . LYS   B 1 76  ? 35.499 -11.203 10.885  1.00 28.30 ?  76  LYS   B HE3  1 
ATOM   5319 H HZ1  . LYS   B 1 76  ? 33.386 -10.382 11.009  1.00 28.86 ?  76  LYS   B HZ1  1 
ATOM   5320 H HZ2  . LYS   B 1 76  ? 33.525 -11.091 9.753   1.00 28.86 ?  76  LYS   B HZ2  1 
ATOM   5321 H HZ3  . LYS   B 1 76  ? 32.808 -11.701 10.854  1.00 28.86 ?  76  LYS   B HZ3  1 
ATOM   5322 N N    . VAL   B 1 77  ? 38.016 -18.045 10.310  1.00 16.24 ?  77  VAL   B N    1 
ATOM   5323 C CA   . VAL   B 1 77  ? 37.809 -19.267 9.541   1.00 16.19 ?  77  VAL   B CA   1 
ATOM   5324 C C    . VAL   B 1 77  ? 36.624 -19.042 8.616   1.00 14.84 ?  77  VAL   B C    1 
ATOM   5325 O O    . VAL   B 1 77  ? 35.557 -18.599 9.056   1.00 14.89 ?  77  VAL   B O    1 
ATOM   5326 C CB   . VAL   B 1 77  ? 37.587 -20.467 10.471  1.00 18.34 ?  77  VAL   B CB   1 
ATOM   5327 C CG1  . VAL   B 1 77  ? 37.289 -21.715 9.646   1.00 19.02 ?  77  VAL   B CG1  1 
ATOM   5328 C CG2  . VAL   B 1 77  ? 38.800 -20.687 11.378  1.00 19.62 ?  77  VAL   B CG2  1 
ATOM   5329 H H    . VAL   B 1 77  ? 37.977 -18.138 11.157  1.00 19.48 ?  77  VAL   B H    1 
ATOM   5330 H HA   . VAL   B 1 77  ? 38.588 -19.445 8.993   1.00 19.43 ?  77  VAL   B HA   1 
ATOM   5331 H HB   . VAL   B 1 77  ? 36.812 -20.290 11.031  1.00 22.01 ?  77  VAL   B HB   1 
ATOM   5332 H HG11 . VAL   B 1 77  ? 37.312 -22.489 10.231  1.00 22.82 ?  77  VAL   B HG11 1 
ATOM   5333 H HG12 . VAL   B 1 77  ? 36.405 -21.636 9.247   1.00 22.82 ?  77  VAL   B HG12 1 
ATOM   5334 H HG13 . VAL   B 1 77  ? 37.958 -21.804 8.953   1.00 22.82 ?  77  VAL   B HG13 1 
ATOM   5335 H HG21 . VAL   B 1 77  ? 38.647 -21.478 11.915  1.00 23.54 ?  77  VAL   B HG21 1 
ATOM   5336 H HG22 . VAL   B 1 77  ? 39.584 -20.803 10.825  1.00 23.54 ?  77  VAL   B HG22 1 
ATOM   5337 H HG23 . VAL   B 1 77  ? 38.904 -19.910 11.949  1.00 23.54 ?  77  VAL   B HG23 1 
ATOM   5338 N N    . GLY   B 1 78  ? 36.810 -19.330 7.325   1.00 14.31 ?  78  GLY   B N    1 
ATOM   5339 C CA   . GLY   B 1 78  ? 35.844 -19.022 6.297   1.00 13.97 ?  78  GLY   B CA   1 
ATOM   5340 C C    . GLY   B 1 78  ? 36.093 -17.712 5.583   1.00 13.46 ?  78  GLY   B C    1 
ATOM   5341 O O    . GLY   B 1 78  ? 35.405 -17.423 4.596   1.00 13.70 ?  78  GLY   B O    1 
ATOM   5342 H H    . GLY   B 1 78  ? 37.515 -19.726 7.019   1.00 17.17 ?  78  GLY   B H    1 
ATOM   5343 H HA2  . GLY   B 1 78  ? 35.850 -19.724 5.632   1.00 16.76 ?  78  GLY   B HA2  1 
ATOM   5344 H HA3  . GLY   B 1 78  ? 34.962 -18.984 6.695   1.00 16.76 ?  78  GLY   B HA3  1 
ATOM   5345 N N    . GLY   B 1 79  ? 37.026 -16.896 6.074   1.00 13.69 ?  79  GLY   B N    1 
ATOM   5346 C CA   . GLY   B 1 79  ? 37.320 -15.606 5.487   1.00 13.31 ?  79  GLY   B CA   1 
ATOM   5347 C C    . GLY   B 1 79  ? 38.551 -15.632 4.597   1.00 12.61 ?  79  GLY   B C    1 
ATOM   5348 O O    . GLY   B 1 79  ? 39.174 -16.671 4.368   1.00 12.87 ?  79  GLY   B O    1 
ATOM   5349 H H    . GLY   B 1 79  ? 37.517 -17.076 6.758   1.00 16.43 ?  79  GLY   B H    1 
ATOM   5350 H HA2  . GLY   B 1 79  ? 36.563 -15.312 4.954   1.00 15.97 ?  79  GLY   B HA2  1 
ATOM   5351 H HA3  . GLY   B 1 79  ? 37.470 -14.955 6.189   1.00 15.97 ?  79  GLY   B HA3  1 
ATOM   5352 N N    . SER   B 1 80  ? 38.927 -14.444 4.119   1.00 12.57 ?  80  SER   B N    1 
ATOM   5353 C CA   . SER   B 1 80  ? 40.040 -14.317 3.185   1.00 12.28 ?  80  SER   B CA   1 
ATOM   5354 C C    . SER   B 1 80  ? 40.617 -12.908 3.228   1.00 12.22 ?  80  SER   B C    1 
ATOM   5355 O O    . SER   B 1 80  ? 40.003 -11.970 3.739   1.00 13.41 ?  80  SER   B O    1 
ATOM   5356 C CB   . SER   B 1 80  ? 39.607 -14.621 1.747   1.00 12.42 ?  80  SER   B CB   1 
ATOM   5357 O OG   . SER   B 1 80  ? 38.768 -13.598 1.234   1.00 13.49 ?  80  SER   B OG   1 
ATOM   5358 H H    . SER   B 1 80  ? 38.560 -13.699 4.324   1.00 15.09 ?  80  SER   B H    1 
ATOM   5359 H HA   . SER   B 1 80  ? 40.734 -14.949 3.438   1.00 14.74 ?  80  SER   B HA   1 
ATOM   5360 H HB2  . SER   B 1 80  ? 40.397 -14.684 1.184   1.00 14.90 ?  80  SER   B HB2  1 
ATOM   5361 H HB3  . SER   B 1 80  ? 39.123 -15.460 1.730   1.00 14.90 ?  80  SER   B HB3  1 
ATOM   5362 H HG   . SER   B 1 80  ? 38.077 -13.525 1.716   1.00 16.18 ?  80  SER   B HG   1 
ATOM   5363 N N    . CYS   B 1 81  ? 41.800 -12.773 2.638   1.00 11.95 ?  81  CYS   B N    1 
ATOM   5364 C CA   . CYS   B 1 81  ? 42.358 -11.466 2.324   1.00 12.13 ?  81  CYS   B CA   1 
ATOM   5365 C C    . CYS   B 1 81  ? 43.136 -11.560 1.018   1.00 11.46 ?  81  CYS   B C    1 
ATOM   5366 O O    . CYS   B 1 81  ? 43.640 -12.627 0.645   1.00 12.50 ?  81  CYS   B O    1 
ATOM   5367 C CB   . CYS   B 1 81  ? 43.245 -10.927 3.451   1.00 13.09 ?  81  CYS   B CB   1 
ATOM   5368 S SG   . CYS   B 1 81  ? 44.771 -11.861 3.702   1.00 13.34 ?  81  CYS   B SG   1 
ATOM   5369 H H    . CYS   B 1 81  ? 42.313 -13.433 2.408   1.00 14.34 ?  81  CYS   B H    1 
ATOM   5370 H HA   . CYS   B 1 81  ? 41.626 -10.838 2.195   1.00 14.56 ?  81  CYS   B HA   1 
ATOM   5371 H HB2  . CYS   B 1 81  ? 43.490 -10.009 3.244   1.00 15.71 ?  81  CYS   B HB2  1 
ATOM   5372 H HB3  . CYS   B 1 81  ? 42.738 -10.944 4.282   1.00 15.71 ?  81  CYS   B HB3  1 
ATOM   5373 H HG   . CYS   B 1 81  ? 45.386 -11.363 4.609   1.00 16.01 ?  81  CYS   B HG   1 
ATOM   5374 N N    . VAL   B 1 82  ? 43.249 -10.419 0.339   1.00 11.77 ?  82  VAL   B N    1 
ATOM   5375 C CA   . VAL   B 1 82  ? 44.005 -10.293 -0.905  1.00 11.94 ?  82  VAL   B CA   1 
ATOM   5376 C C    . VAL   B 1 82  ? 45.346 -9.649  -0.588  1.00 12.26 ?  82  VAL   B C    1 
ATOM   5377 O O    . VAL   B 1 82  ? 45.394 -8.532  -0.053  1.00 13.57 ?  82  VAL   B O    1 
ATOM   5378 C CB   . VAL   B 1 82  ? 43.254 -9.453  -1.949  1.00 12.81 ?  82  VAL   B CB   1 
ATOM   5379 C CG1  . VAL   B 1 82  ? 44.083 -9.317  -3.225  1.00 14.60 ?  82  VAL   B CG1  1 
ATOM   5380 C CG2  . VAL   B 1 82  ? 41.878 -10.048 -2.235  1.00 13.91 ?  82  VAL   B CG2  1 
ATOM   5381 H H    . VAL   B 1 82  ? 42.877 -9.675  0.583   1.00 14.12 ?  82  VAL   B H    1 
ATOM   5382 H HA   . VAL   B 1 82  ? 44.164 -11.174 -1.274  1.00 14.33 ?  82  VAL   B HA   1 
ATOM   5383 H HB   . VAL   B 1 82  ? 43.121 -8.563  -1.596  1.00 15.37 ?  82  VAL   B HB   1 
ATOM   5384 H HG11 . VAL   B 1 82  ? 43.521 -8.976  -3.938  1.00 17.51 ?  82  VAL   B HG11 1 
ATOM   5385 H HG12 . VAL   B 1 82  ? 44.820 -8.701  -3.066  1.00 17.51 ?  82  VAL   B HG12 1 
ATOM   5386 H HG13 . VAL   B 1 82  ? 44.435 -10.189 -3.473  1.00 17.51 ?  82  VAL   B HG13 1 
ATOM   5387 H HG21 . VAL   B 1 82  ? 41.445 -9.528  -2.934  1.00 16.70 ?  82  VAL   B HG21 1 
ATOM   5388 H HG22 . VAL   B 1 82  ? 41.980 -10.967 -2.528  1.00 16.70 ?  82  VAL   B HG22 1 
ATOM   5389 H HG23 . VAL   B 1 82  ? 41.343 -10.016 -1.426  1.00 16.70 ?  82  VAL   B HG23 1 
ATOM   5390 N N    . LEU   B 1 83  ? 46.430 -10.332 -0.950  1.00 11.88 ?  83  LEU   B N    1 
ATOM   5391 C CA   . LEU   B 1 83  ? 47.791 -9.815  -0.830  1.00 11.79 ?  83  LEU   B CA   1 
ATOM   5392 C C    . LEU   B 1 83  ? 48.490 -9.972  -2.181  1.00 11.55 ?  83  LEU   B C    1 
ATOM   5393 O O    . LEU   B 1 83  ? 47.893 -10.413 -3.168  1.00 11.49 ?  83  LEU   B O    1 
ATOM   5394 C CB   . LEU   B 1 83  ? 48.535 -10.502 0.321   1.00 12.55 ?  83  LEU   B CB   1 
ATOM   5395 C CG   . LEU   B 1 83  ? 48.047 -10.150 1.729   1.00 13.47 ?  83  LEU   B CG   1 
ATOM   5396 C CD1  . LEU   B 1 83  ? 48.674 -11.033 2.795   1.00 14.41 ?  83  LEU   B CD1  1 
ATOM   5397 C CD2  . LEU   B 1 83  ? 48.275 -8.668  2.046   1.00 14.05 ?  83  LEU   B CD2  1 
ATOM   5398 H H    . LEU   B 1 83  ? 46.394 -11.128 -1.289  1.00 14.26 ?  83  LEU   B H    1 
ATOM   5399 H HA   . LEU   B 1 83  ? 47.742 -8.872  -0.642  1.00 14.15 ?  83  LEU   B HA   1 
ATOM   5400 H HB2  . LEU   B 1 83  ? 48.453 -11.460 0.209   1.00 15.07 ?  83  LEU   B HB2  1 
ATOM   5401 H HB3  . LEU   B 1 83  ? 49.471 -10.249 0.262   1.00 15.07 ?  83  LEU   B HB3  1 
ATOM   5402 H HG   . LEU   B 1 83  ? 47.094 -10.305 1.755   1.00 16.16 ?  83  LEU   B HG   1 
ATOM   5403 H HD11 . LEU   B 1 83  ? 48.327 -10.775 3.662   1.00 17.29 ?  83  LEU   B HD11 1 
ATOM   5404 H HD12 . LEU   B 1 83  ? 48.445 -11.962 2.613   1.00 17.29 ?  83  LEU   B HD12 1 
ATOM   5405 H HD13 . LEU   B 1 83  ? 49.637 -10.925 2.776   1.00 17.29 ?  83  LEU   B HD13 1 
ATOM   5406 H HD21 . LEU   B 1 83  ? 48.073 -8.515  2.983   1.00 16.86 ?  83  LEU   B HD21 1 
ATOM   5407 H HD22 . LEU   B 1 83  ? 49.201 -8.443  1.867   1.00 16.86 ?  83  LEU   B HD22 1 
ATOM   5408 H HD23 . LEU   B 1 83  ? 47.690 -8.131  1.491   1.00 16.86 ?  83  LEU   B HD23 1 
ATOM   5409 N N    . SER   B 1 84  ? 49.767 -9.598  -2.239  1.00 12.69 ?  84  SER   B N    1 
ATOM   5410 C CA   . SER   B 1 84  ? 50.502 -9.734  -3.488  1.00 13.30 ?  84  SER   B CA   1 
ATOM   5411 C C    . SER   B 1 84  ? 50.665 -11.203 -3.876  1.00 11.90 ?  84  SER   B C    1 
ATOM   5412 O O    . SER   B 1 84  ? 50.775 -12.088 -3.027  1.00 11.87 ?  84  SER   B O    1 
ATOM   5413 C CB   . SER   B 1 84  ? 51.895 -9.123  -3.354  1.00 14.96 ?  84  SER   B CB   1 
ATOM   5414 O OG   . SER   B 1 84  ? 52.637 -9.376  -4.531  1.00 16.62 ?  84  SER   B OG   1 
ATOM   5415 H H    . SER   B 1 84  ? 50.204 -9.252  -1.592  1.00 15.22 ?  84  SER   B H    1 
ATOM   5416 H HA   . SER   B 1 84  ? 50.031 -9.282  -4.202  1.00 15.96 ?  84  SER   B HA   1 
ATOM   5417 H HB2  . SER   B 1 84  ? 51.809 -8.164  -3.221  1.00 17.95 ?  84  SER   B HB2  1 
ATOM   5418 H HB3  . SER   B 1 84  ? 52.350 -9.523  -2.596  1.00 17.95 ?  84  SER   B HB3  1 
ATOM   5419 H HG   . SER   B 1 84  ? 53.410 -9.028  -4.461  1.00 19.95 ?  84  SER   B HG   1 
ATOM   5420 N N    . GLY   B 1 85  ? 50.728 -11.442 -5.179  1.00 13.14 ?  85  GLY   B N    1 
ATOM   5421 C CA   . GLY   B 1 85  ? 51.073 -12.744 -5.698  1.00 14.17 ?  85  GLY   B CA   1 
ATOM   5422 C C    . GLY   B 1 85  ? 52.545 -12.934 -6.006  1.00 13.31 ?  85  GLY   B C    1 
ATOM   5423 O O    . GLY   B 1 85  ? 52.928 -14.010 -6.459  1.00 13.56 ?  85  GLY   B O    1 
ATOM   5424 H H    . GLY   B 1 85  ? 50.567 -10.863 -5.786  1.00 15.77 ?  85  GLY   B H    1 
ATOM   5425 H HA2  . GLY   B 1 85  ? 50.814 -13.426 -5.052  1.00 17.00 ?  85  GLY   B HA2  1 
ATOM   5426 H HA3  . GLY   B 1 85  ? 50.577 -12.908 -6.512  1.00 17.00 ?  85  GLY   B HA3  1 
ATOM   5427 N N    . HIS   B 1 86  ? 53.397 -11.937 -5.781  1.00 13.07 ?  86  HIS   B N    1 
ATOM   5428 C CA   . HIS   B 1 86  ? 54.865 -12.096 -5.878  1.00 12.96 ?  86  HIS   B CA   1 
ATOM   5429 C C    . HIS   B 1 86  ? 55.233 -12.620 -7.264  1.00 13.15 ?  86  HIS   B C    1 
ATOM   5430 O O    . HIS   B 1 86  ? 54.839 -12.016 -8.275  1.00 14.23 ?  86  HIS   B O    1 
ATOM   5431 C CB   . HIS   B 1 86  ? 55.359 -12.925 -4.692  1.00 13.55 ?  86  HIS   B CB   1 
ATOM   5432 C CG   . HIS   B 1 86  ? 55.035 -12.308 -3.374  1.00 13.69 ?  86  HIS   B CG   1 
ATOM   5433 N ND1  . HIS   B 1 86  ? 55.864 -11.401 -2.753  1.00 15.48 ?  86  HIS   B ND1  1 
ATOM   5434 C CD2  . HIS   B 1 86  ? 53.950 -12.438 -2.574  1.00 14.22 ?  86  HIS   B CD2  1 
ATOM   5435 C CE1  . HIS   B 1 86  ? 55.300 -10.994 -1.629  1.00 15.56 ?  86  HIS   B CE1  1 
ATOM   5436 N NE2  . HIS   B 1 86  ? 54.138 -11.607 -1.497  1.00 14.83 ?  86  HIS   B NE2  1 
ATOM   5437 H H    . HIS   B 1 86  ? 53.152 -11.143 -5.567  1.00 15.68 ?  86  HIS   B H    1 
ATOM   5438 H HA   . HIS   B 1 86  ? 55.266 -11.221 -5.787  1.00 15.56 ?  86  HIS   B HA   1 
ATOM   5439 H HB2  . HIS   B 1 86  ? 54.948 -13.803 -4.719  1.00 16.26 ?  86  HIS   B HB2  1 
ATOM   5440 H HB3  . HIS   B 1 86  ? 56.325 -13.012 -4.744  1.00 16.26 ?  86  HIS   B HB3  1 
ATOM   5441 H HD2  . HIS   B 1 86  ? 53.200 -12.971 -2.734  1.00 17.06 ?  86  HIS   B HD2  1 
ATOM   5442 H HE1  . HIS   B 1 86  ? 55.667 -10.397 -1.015  1.00 18.67 ?  86  HIS   B HE1  1 
ATOM   5443 H HE2  . HIS   B 1 86  ? 53.589 -11.514 -0.833  1.00 17.79 ?  86  HIS   B HE2  1 
ATOM   5444 N N    . ASN   B 1 87  ? 55.992 -13.710 -7.368  1.00 13.69 ?  87  ASN   B N    1 
ATOM   5445 C CA   . ASN   B 1 87  ? 56.382 -14.287 -8.644  1.00 14.80 ?  87  ASN   B CA   1 
ATOM   5446 C C    . ASN   B 1 87  ? 55.392 -15.323 -9.150  1.00 14.58 ?  87  ASN   B C    1 
ATOM   5447 O O    . ASN   B 1 87  ? 55.701 -16.024 -10.119 1.00 16.49 ?  87  ASN   B O    1 
ATOM   5448 C CB   . ASN   B 1 87  ? 57.771 -14.928 -8.534  1.00 16.75 ?  87  ASN   B CB   1 
ATOM   5449 C CG   . ASN   B 1 87  ? 57.824 -16.048 -7.497  1.00 17.36 ?  87  ASN   B CG   1 
ATOM   5450 O OD1  . ASN   B 1 87  ? 57.207 -15.956 -6.430  1.00 16.69 ?  87  ASN   B OD1  1 
ATOM   5451 N ND2  . ASN   B 1 87  ? 58.562 -17.121 -7.813  1.00 20.20 ?  87  ASN   B ND2  1 
ATOM   5452 H H    . ASN   B 1 87  ? 56.291 -14.146 -6.689  1.00 16.43 ?  87  ASN   B H    1 
ATOM   5453 H HA   . ASN   B 1 87  ? 56.426 -13.581 -9.302  1.00 17.76 ?  87  ASN   B HA   1 
ATOM   5454 H HB2  . ASN   B 1 87  ? 58.011 -15.302 -9.399  1.00 20.10 ?  87  ASN   B HB2  1 
ATOM   5455 H HB3  . ASN   B 1 87  ? 58.409 -14.247 -8.279  1.00 20.10 ?  87  ASN   B HB3  1 
ATOM   5456 H HD21 . ASN   B 1 87  ? 58.625 -17.776 -7.262  1.00 24.24 ?  87  ASN   B HD21 1 
ATOM   5457 H HD22 . ASN   B 1 87  ? 58.974 -17.155 -8.571  1.00 24.24 ?  87  ASN   B HD22 1 
ATOM   5458 N N    . LEU   B 1 88  ? 54.212 -15.428 -8.530  1.00 13.03 ?  88  LEU   B N    1 
ATOM   5459 C CA   . LEU   B 1 88  ? 53.228 -16.453 -8.858  1.00 13.37 ?  88  LEU   B CA   1 
ATOM   5460 C C    . LEU   B 1 88  ? 51.997 -15.932 -9.574  1.00 13.47 ?  88  LEU   B C    1 
ATOM   5461 O O    . LEU   B 1 88  ? 51.393 -16.673 -10.354 1.00 15.16 ?  88  LEU   B O    1 
ATOM   5462 C CB   . LEU   B 1 88  ? 52.758 -17.143 -7.575  1.00 14.60 ?  88  LEU   B CB   1 
ATOM   5463 C CG   . LEU   B 1 88  ? 53.877 -17.800 -6.785  1.00 16.85 ?  88  LEU   B CG   1 
ATOM   5464 C CD1  . LEU   B 1 88  ? 53.387 -18.195 -5.403  1.00 18.49 ?  88  LEU   B CD1  1 
ATOM   5465 C CD2  . LEU   B 1 88  ? 54.382 -19.002 -7.549  1.00 20.69 ?  88  LEU   B CD2  1 
ATOM   5466 H H    . LEU   B 1 88  ? 53.953 -14.904 -7.884  1.00 15.63 ?  88  LEU   B H    1 
ATOM   5467 H HA   . LEU   B 1 88  ? 53.639 -17.115 -9.419  1.00 16.04 ?  88  LEU   B HA   1 
ATOM   5468 H HB2  . LEU   B 1 88  ? 52.326 -16.494 -6.995  1.00 17.52 ?  88  LEU   B HB2  1 
ATOM   5469 H HB3  . LEU   B 1 88  ? 52.114 -17.841 -7.809  1.00 17.52 ?  88  LEU   B HB3  1 
ATOM   5470 H HG   . LEU   B 1 88  ? 54.605 -17.169 -6.684  1.00 20.22 ?  88  LEU   B HG   1 
ATOM   5471 H HD11 . LEU   B 1 88  ? 54.057 -18.754 -4.982  1.00 22.19 ?  88  LEU   B HD11 1 
ATOM   5472 H HD12 . LEU   B 1 88  ? 53.245 -17.392 -4.879  1.00 22.19 ?  88  LEU   B HD12 1 
ATOM   5473 H HD13 . LEU   B 1 88  ? 52.555 -18.683 -5.495  1.00 22.19 ?  88  LEU   B HD13 1 
ATOM   5474 H HD21 . LEU   B 1 88  ? 55.009 -19.484 -6.990  1.00 24.83 ?  88  LEU   B HD21 1 
ATOM   5475 H HD22 . LEU   B 1 88  ? 53.631 -19.570 -7.776  1.00 24.83 ?  88  LEU   B HD22 1 
ATOM   5476 H HD23 . LEU   B 1 88  ? 54.825 -18.698 -8.357  1.00 24.83 ?  88  LEU   B HD23 1 
ATOM   5477 N N    . ALA   B 1 89  ? 51.596 -14.698 -9.300  1.00 12.61 ?  89  ALA   B N    1 
ATOM   5478 C CA   . ALA   B 1 89  ? 50.315 -14.189 -9.757  1.00 11.90 ?  89  ALA   B CA   1 
ATOM   5479 C C    . ALA   B 1 89  ? 50.304 -12.701 -9.468  1.00 12.64 ?  89  ALA   B C    1 
ATOM   5480 O O    . ALA   B 1 89  ? 51.125 -12.199 -8.703  1.00 13.32 ?  89  ALA   B O    1 
ATOM   5481 C CB   . ALA   B 1 89  ? 49.169 -14.857 -9.007  1.00 12.37 ?  89  ALA   B CB   1 
ATOM   5482 H H    . ALA   B 1 89  ? 52.050 -14.123 -8.846  1.00 15.13 ?  89  ALA   B H    1 
ATOM   5483 H HA   . ALA   B 1 89  ? 50.209 -14.332 -10.716 1.00 14.27 ?  89  ALA   B HA   1 
ATOM   5484 H HB1  . ALA   B 1 89  ? 48.327 -14.514 -9.352  1.00 14.84 ?  89  ALA   B HB1  1 
ATOM   5485 H HB2  . ALA   B 1 89  ? 49.220 -15.814 -9.152  1.00 14.84 ?  89  ALA   B HB2  1 
ATOM   5486 H HB3  . ALA   B 1 89  ? 49.253 -14.654 -8.068  1.00 14.84 ?  89  ALA   B HB3  1 
ATOM   5487 N N    . LYS   B 1 90  ? 49.330 -12.000 -10.040 1.00 13.21 ?  90  LYS   B N    1 
ATOM   5488 C CA   . LYS   B 1 90  ? 49.150 -10.609 -9.636  1.00 13.17 ?  90  LYS   B CA   1 
ATOM   5489 C C    . LYS   B 1 90  ? 48.819 -10.530 -8.150  1.00 12.82 ?  90  LYS   B C    1 
ATOM   5490 O O    . LYS   B 1 90  ? 49.472 -9.796  -7.395  1.00 13.50 ?  90  LYS   B O    1 
ATOM   5491 C CB   . LYS   B 1 90  ? 48.086 -9.934  -10.501 1.00 14.62 ?  90  LYS   B CB   1 
ATOM   5492 C CG   . LYS   B 1 90  ? 47.776 -8.504  -10.102 1.00 15.04 ?  90  LYS   B CG   1 
ATOM   5493 C CD   . LYS   B 1 90  ? 48.981 -7.611  -10.142 1.00 17.79 ?  90  LYS   B CD   1 
ATOM   5494 C CE   . LYS   B 1 90  ? 48.508 -6.207  -9.846  1.00 19.69 ?  90  LYS   B CE   1 
ATOM   5495 N NZ   . LYS   B 1 90  ? 49.631 -5.254  -9.776  1.00 19.08 ?  90  LYS   B NZ   1 
ATOM   5496 H H    . LYS   B 1 90  ? 48.782 -12.293 -10.638 1.00 15.85 ?  90  LYS   B H    1 
ATOM   5497 H HA   . LYS   B 1 90  ? 49.982 -10.140 -9.779  1.00 15.80 ?  90  LYS   B HA   1 
ATOM   5498 H HB2  . LYS   B 1 90  ? 48.395 -9.919  -11.423 1.00 17.54 ?  90  LYS   B HB2  1 
ATOM   5499 H HB3  . LYS   B 1 90  ? 47.262 -10.443 -10.444 1.00 17.54 ?  90  LYS   B HB3  1 
ATOM   5500 H HG2  . LYS   B 1 90  ? 47.115 -8.142  -10.716 1.00 18.05 ?  90  LYS   B HG2  1 
ATOM   5501 H HG3  . LYS   B 1 90  ? 47.419 -8.494  -9.198  1.00 18.05 ?  90  LYS   B HG3  1 
ATOM   5502 H HD2  . LYS   B 1 90  ? 49.618 -7.879  -9.459  1.00 21.34 ?  90  LYS   B HD2  1 
ATOM   5503 H HD3  . LYS   B 1 90  ? 49.384 -7.633  -11.024 1.00 21.34 ?  90  LYS   B HD3  1 
ATOM   5504 H HE2  . LYS   B 1 90  ? 47.906 -5.914  -10.552 1.00 23.63 ?  90  LYS   B HE2  1 
ATOM   5505 H HE3  . LYS   B 1 90  ? 48.045 -6.194  -8.992  1.00 23.63 ?  90  LYS   B HE3  1 
ATOM   5506 H HZ1  . LYS   B 1 90  ? 49.328 -4.435  -9.602  1.00 22.90 ?  90  LYS   B HZ1  1 
ATOM   5507 H HZ2  . LYS   B 1 90  ? 50.194 -5.496  -9.131  1.00 22.90 ?  90  LYS   B HZ2  1 
ATOM   5508 H HZ3  . LYS   B 1 90  ? 50.067 -5.241  -10.552 1.00 22.90 ?  90  LYS   B HZ3  1 
ATOM   5509 N N    . HIS   B 1 91  ? 47.844 -11.324 -7.705  1.00 11.62 ?  91  HIS   B N    1 
ATOM   5510 C CA   . HIS   B 1 91  ? 47.385 -11.346 -6.326  1.00 11.77 ?  91  HIS   B CA   1 
ATOM   5511 C C    . HIS   B 1 91  ? 47.372 -12.776 -5.809  1.00 10.97 ?  91  HIS   B C    1 
ATOM   5512 O O    . HIS   B 1 91  ? 47.131 -13.719 -6.571  1.00 11.63 ?  91  HIS   B O    1 
ATOM   5513 C CB   . HIS   B 1 91  ? 45.936 -10.869 -6.210  1.00 13.07 ?  91  HIS   B CB   1 
ATOM   5514 C CG   . HIS   B 1 91  ? 45.729 -9.461  -6.645  1.00 16.50 ?  91  HIS   B CG   1 
ATOM   5515 N ND1  . HIS   B 1 91  ? 46.337 -8.388  -6.028  1.00 19.46 ?  91  HIS   B ND1  1 
ATOM   5516 C CD2  . HIS   B 1 91  ? 44.958 -8.945  -7.626  1.00 19.20 ?  91  HIS   B CD2  1 
ATOM   5517 C CE1  . HIS   B 1 91  ? 45.959 -7.268  -6.622  1.00 20.59 ?  91  HIS   B CE1  1 
ATOM   5518 N NE2  . HIS   B 1 91  ? 45.118 -7.580  -7.592  1.00 20.71 ?  91  HIS   B NE2  1 
ATOM   5519 H H    . HIS   B 1 91  ? 47.418 -11.880 -8.205  1.00 13.95 ?  91  HIS   B H    1 
ATOM   5520 H HA   . HIS   B 1 91  ? 47.959 -10.791 -5.763  1.00 14.12 ?  91  HIS   B HA   1 
ATOM   5521 H HB2  . HIS   B 1 91  ? 45.376 -11.431 -6.758  1.00 15.68 ?  91  HIS   B HB2  1 
ATOM   5522 H HB3  . HIS   B 1 91  ? 45.660 -10.931 -5.279  1.00 15.68 ?  91  HIS   B HB3  1 
ATOM   5523 H HD2  . HIS   B 1 91  ? 44.423 -9.414  -8.219  1.00 23.04 ?  91  HIS   B HD2  1 
ATOM   5524 H HE1  . HIS   B 1 91  ? 46.232 -6.404  -6.391  1.00 24.71 ?  91  HIS   B HE1  1 
ATOM   5525 H HE2  . HIS   B 1 91  ? 44.740 -7.011  -8.123  1.00 24.85 ?  91  HIS   B HE2  1 
ATOM   5526 N N    . CYS   B 1 92  ? 47.573 -12.919 -4.504  1.00 11.04 ?  92  CYS   B N    1 
ATOM   5527 C CA   . CYS   B 1 92  ? 47.249 -14.154 -3.796  1.00 10.74 ?  92  CYS   B CA   1 
ATOM   5528 C C    . CYS   B 1 92  ? 46.025 -13.904 -2.922  1.00 10.43 ?  92  CYS   B C    1 
ATOM   5529 O O    . CYS   B 1 92  ? 46.031 -12.998 -2.075  1.00 11.52 ?  92  CYS   B O    1 
ATOM   5530 C CB   . CYS   B 1 92  ? 48.417 -14.601 -2.928  1.00 11.27 ?  92  CYS   B CB   1 
ATOM   5531 S SG   . CYS   B 1 92  ? 48.058 -16.148 -2.035  1.00 11.58 ?  92  CYS   B SG   1 
ATOM   5532 H H    . CYS   B 1 92  ? 47.922 -12.315 -3.999  1.00 13.24 ?  92  CYS   B H    1 
ATOM   5533 H HA   . CYS   B 1 92  ? 47.050 -14.856 -4.436  1.00 12.89 ?  92  CYS   B HA   1 
ATOM   5534 H HB2  . CYS   B 1 92  ? 49.192 -14.754 -3.485  1.00 13.53 ?  92  CYS   B HB2  1 
ATOM   5535 H HB3  . CYS   B 1 92  ? 48.603 -13.917 -2.269  1.00 13.53 ?  92  CYS   B HB3  1 
ATOM   5536 H HG   . CYS   B 1 92  ? 49.025 -16.460 -1.399  1.00 13.90 ?  92  CYS   B HG   1 
ATOM   5537 N N    . LEU   B 1 93  ? 44.986 -14.715 -3.120  1.00 10.74 ?  93  LEU   B N    1 
ATOM   5538 C CA   . LEU   B 1 93  ? 43.808 -14.712 -2.260  1.00 10.87 ?  93  LEU   B CA   1 
ATOM   5539 C C    . LEU   B 1 93  ? 44.035 -15.771 -1.191  1.00 10.24 ?  93  LEU   B C    1 
ATOM   5540 O O    . LEU   B 1 93  ? 43.990 -16.973 -1.478  1.00 11.24 ?  93  LEU   B O    1 
ATOM   5541 C CB   . LEU   B 1 93  ? 42.540 -15.007 -3.062  1.00 11.23 ?  93  LEU   B CB   1 
ATOM   5542 C CG   . LEU   B 1 93  ? 41.233 -15.019 -2.259  1.00 11.99 ?  93  LEU   B CG   1 
ATOM   5543 C CD1  . LEU   B 1 93  ? 40.872 -13.636 -1.771  1.00 12.39 ?  93  LEU   B CD1  1 
ATOM   5544 C CD2  . LEU   B 1 93  ? 40.096 -15.620 -3.077  1.00 12.22 ?  93  LEU   B CD2  1 
ATOM   5545 H H    . LEU   B 1 93  ? 44.940 -15.292 -3.764  1.00 12.89 ?  93  LEU   B H    1 
ATOM   5546 H HA   . LEU   B 1 93  ? 43.717 -13.843 -1.837  1.00 13.04 ?  93  LEU   B HA   1 
ATOM   5547 H HB2  . LEU   B 1 93  ? 42.448 -14.327 -3.750  1.00 13.48 ?  93  LEU   B HB2  1 
ATOM   5548 H HB3  . LEU   B 1 93  ? 42.634 -15.875 -3.476  1.00 13.48 ?  93  LEU   B HB3  1 
ATOM   5549 H HG   . LEU   B 1 93  ? 41.355 -15.577 -1.477  1.00 14.38 ?  93  LEU   B HG   1 
ATOM   5550 H HD11 . LEU   B 1 93  ? 40.023 -13.672 -1.304  1.00 14.87 ?  93  LEU   B HD11 1 
ATOM   5551 H HD12 . LEU   B 1 93  ? 41.565 -13.314 -1.174  1.00 14.87 ?  93  LEU   B HD12 1 
ATOM   5552 H HD13 . LEU   B 1 93  ? 40.798 -13.037 -2.537  1.00 14.87 ?  93  LEU   B HD13 1 
ATOM   5553 H HD21 . LEU   B 1 93  ? 39.286 -15.609 -2.546  1.00 14.66 ?  93  LEU   B HD21 1 
ATOM   5554 H HD22 . LEU   B 1 93  ? 39.975 -15.094 -3.882  1.00 14.66 ?  93  LEU   B HD22 1 
ATOM   5555 H HD23 . LEU   B 1 93  ? 40.328 -16.534 -3.310  1.00 14.66 ?  93  LEU   B HD23 1 
ATOM   5556 N N    . HIS   B 1 94  ? 44.312 -15.340 0.030   1.00 10.44 ?  94  HIS   B N    1 
ATOM   5557 C CA   . HIS   B 1 94  ? 44.528 -16.251 1.147   1.00 10.74 ?  94  HIS   B CA   1 
ATOM   5558 C C    . HIS   B 1 94  ? 43.163 -16.598 1.726   1.00 11.18 ?  94  HIS   B C    1 
ATOM   5559 O O    . HIS   B 1 94  ? 42.498 -15.720 2.280   1.00 12.32 ?  94  HIS   B O    1 
ATOM   5560 C CB   . HIS   B 1 94  ? 45.398 -15.580 2.208   1.00 11.31 ?  94  HIS   B CB   1 
ATOM   5561 C CG   . HIS   B 1 94  ? 46.782 -15.270 1.738   1.00 11.24 ?  94  HIS   B CG   1 
ATOM   5562 N ND1  . HIS   B 1 94  ? 47.809 -16.187 1.816   1.00 11.41 ?  94  HIS   B ND1  1 
ATOM   5563 C CD2  . HIS   B 1 94  ? 47.287 -14.164 1.141   1.00 11.32 ?  94  HIS   B CD2  1 
ATOM   5564 C CE1  . HIS   B 1 94  ? 48.897 -15.636 1.309   1.00 12.27 ?  94  HIS   B CE1  1 
ATOM   5565 N NE2  . HIS   B 1 94  ? 48.608 -14.416 0.886   1.00 11.86 ?  94  HIS   B NE2  1 
ATOM   5566 H H    . HIS   B 1 94  ? 44.409 -14.501 0.234   1.00 12.52 ?  94  HIS   B H    1 
ATOM   5567 H HA   . HIS   B 1 94  ? 44.963 -17.059 0.835   1.00 12.88 ?  94  HIS   B HA   1 
ATOM   5568 H HB2  . HIS   B 1 94  ? 44.984 -14.750 2.474   1.00 13.57 ?  94  HIS   B HB2  1 
ATOM   5569 H HB3  . HIS   B 1 94  ? 45.474 -16.178 2.965   1.00 13.57 ?  94  HIS   B HB3  1 
ATOM   5570 H HD2  . HIS   B 1 94  ? 46.828 -13.379 0.946   1.00 13.59 ?  94  HIS   B HD2  1 
ATOM   5571 H HE1  . HIS   B 1 94  ? 49.727 -16.054 1.240   1.00 14.72 ?  94  HIS   B HE1  1 
ATOM   5572 H HE2  . HIS   B 1 94  ? 49.165 -13.873 0.520   1.00 14.23 ?  94  HIS   B HE2  1 
ATOM   5573 N N    . VAL   B 1 95  ? 42.728 -17.850 1.583   1.00 11.13 ?  95  VAL   B N    1 
ATOM   5574 C CA   . VAL   B 1 95  ? 41.398 -18.288 2.015   1.00 11.14 ?  95  VAL   B CA   1 
ATOM   5575 C C    . VAL   B 1 95  ? 41.558 -19.324 3.114   1.00 11.41 ?  95  VAL   B C    1 
ATOM   5576 O O    . VAL   B 1 95  ? 42.341 -20.267 2.967   1.00 12.18 ?  95  VAL   B O    1 
ATOM   5577 C CB   . VAL   B 1 95  ? 40.586 -18.887 0.852   1.00 11.30 ?  95  VAL   B CB   1 
ATOM   5578 C CG1  . VAL   B 1 95  ? 39.205 -19.360 1.325   1.00 12.96 ?  95  VAL   B CG1  1 
ATOM   5579 C CG2  . VAL   B 1 95  ? 40.454 -17.895 -0.282  1.00 11.50 ?  95  VAL   B CG2  1 
ATOM   5580 H H    . VAL   B 1 95  ? 43.192 -18.478 1.222   1.00 13.35 ?  95  VAL   B H    1 
ATOM   5581 H HA   . VAL   B 1 95  ? 40.905 -17.532 2.371   1.00 13.37 ?  95  VAL   B HA   1 
ATOM   5582 H HB   . VAL   B 1 95  ? 41.059 -19.657 0.506   1.00 13.56 ?  95  VAL   B HB   1 
ATOM   5583 H HG11 . VAL   B 1 95  ? 38.656 -19.561 0.545   1.00 15.55 ?  95  VAL   B HG11 1 
ATOM   5584 H HG12 . VAL   B 1 95  ? 39.308 -20.161 1.862   1.00 15.55 ?  95  VAL   B HG12 1 
ATOM   5585 H HG13 . VAL   B 1 95  ? 38.787 -18.660 1.846   1.00 15.55 ?  95  VAL   B HG13 1 
ATOM   5586 H HG21 . VAL   B 1 95  ? 39.874 -18.268 -0.961  1.00 13.80 ?  95  VAL   B HG21 1 
ATOM   5587 H HG22 . VAL   B 1 95  ? 40.065 -17.073 0.069   1.00 13.80 ?  95  VAL   B HG22 1 
ATOM   5588 H HG23 . VAL   B 1 95  ? 41.330 -17.716 -0.646  1.00 13.80 ?  95  VAL   B HG23 1 
ATOM   5589 N N    . VAL   B 1 96  ? 40.826 -19.146 4.211   1.00 11.99 ?  96  VAL   B N    1 
ATOM   5590 C CA   . VAL   B 1 96  ? 40.912 -20.050 5.357   1.00 12.25 ?  96  VAL   B CA   1 
ATOM   5591 C C    . VAL   B 1 96  ? 39.726 -21.012 5.317   1.00 12.89 ?  96  VAL   B C    1 
ATOM   5592 O O    . VAL   B 1 96  ? 38.608 -20.659 5.705   1.00 13.91 ?  96  VAL   B O    1 
ATOM   5593 C CB   . VAL   B 1 96  ? 40.954 -19.294 6.687   1.00 13.08 ?  96  VAL   B CB   1 
ATOM   5594 C CG1  . VAL   B 1 96  ? 41.112 -20.286 7.839   1.00 13.97 ?  96  VAL   B CG1  1 
ATOM   5595 C CG2  . VAL   B 1 96  ? 42.075 -18.271 6.699   1.00 13.44 ?  96  VAL   B CG2  1 
ATOM   5596 H H    . VAL   B 1 96  ? 40.267 -18.501 4.318   1.00 14.39 ?  96  VAL   B H    1 
ATOM   5597 H HA   . VAL   B 1 96  ? 41.728 -20.573 5.287   1.00 14.70 ?  96  VAL   B HA   1 
ATOM   5598 H HB   . VAL   B 1 96  ? 40.115 -18.827 6.813   1.00 15.69 ?  96  VAL   B HB   1 
ATOM   5599 H HG11 . VAL   B 1 96  ? 41.316 -19.799 8.654   1.00 16.76 ?  96  VAL   B HG11 1 
ATOM   5600 H HG12 . VAL   B 1 96  ? 40.288 -20.785 7.953   1.00 16.76 ?  96  VAL   B HG12 1 
ATOM   5601 H HG13 . VAL   B 1 96  ? 41.842 -20.898 7.635   1.00 16.76 ?  96  VAL   B HG13 1 
ATOM   5602 H HG21 . VAL   B 1 96  ? 42.114 -17.854 7.576   1.00 16.13 ?  96  VAL   B HG21 1 
ATOM   5603 H HG22 . VAL   B 1 96  ? 42.912 -18.712 6.503   1.00 16.13 ?  96  VAL   B HG22 1 
ATOM   5604 H HG23 . VAL   B 1 96  ? 41.890 -17.594 6.025   1.00 16.13 ?  96  VAL   B HG23 1 
ATOM   5605 N N    . GLY   B 1 97  ? 39.965 -22.241 4.873   1.00 12.78 ?  97  GLY   B N    1 
ATOM   5606 C CA   . GLY   B 1 97  ? 39.000 -23.303 5.036   1.00 14.18 ?  97  GLY   B CA   1 
ATOM   5607 C C    . GLY   B 1 97  ? 39.134 -23.902 6.417   1.00 15.51 ?  97  GLY   B C    1 
ATOM   5608 O O    . GLY   B 1 97  ? 40.175 -23.767 7.072   1.00 15.53 ?  97  GLY   B O    1 
ATOM   5609 H H    . GLY   B 1 97  ? 40.692 -22.477 4.464   1.00 15.34 ?  97  GLY   B H    1 
ATOM   5610 H HA2  . GLY   B 1 97  ? 38.107 -22.939 4.920   1.00 17.02 ?  97  GLY   B HA2  1 
ATOM   5611 H HA3  . GLY   B 1 97  ? 39.151 -23.988 4.368   1.00 17.02 ?  97  GLY   B HA3  1 
ATOM   5612 N N    . PRO   B 1 98  ? 38.088 -24.576 6.890   1.00 16.65 ?  98  PRO   B N    1 
ATOM   5613 C CA   . PRO   B 1 98  ? 38.189 -25.268 8.178   1.00 18.14 ?  98  PRO   B CA   1 
ATOM   5614 C C    . PRO   B 1 98  ? 39.212 -26.398 8.134   1.00 17.65 ?  98  PRO   B C    1 
ATOM   5615 O O    . PRO   B 1 98  ? 39.320 -27.131 7.153   1.00 17.56 ?  98  PRO   B O    1 
ATOM   5616 C CB   . PRO   B 1 98  ? 36.766 -25.794 8.406   1.00 18.53 ?  98  PRO   B CB   1 
ATOM   5617 C CG   . PRO   B 1 98  ? 36.182 -25.917 7.048   1.00 18.35 ?  98  PRO   B CG   1 
ATOM   5618 C CD   . PRO   B 1 98  ? 36.767 -24.769 6.263   1.00 17.48 ?  98  PRO   B CD   1 
ATOM   5619 H HA   . PRO   B 1 98  ? 38.424 -24.642 8.880   1.00 21.77 ?  98  PRO   B HA   1 
ATOM   5620 H HB2  . PRO   B 1 98  ? 36.809 -26.661 8.841   1.00 22.24 ?  98  PRO   B HB2  1 
ATOM   5621 H HB3  . PRO   B 1 98  ? 36.267 -25.163 8.941   1.00 22.24 ?  98  PRO   B HB3  1 
ATOM   5622 H HG2  . PRO   B 1 98  ? 36.439 -26.768 6.655   1.00 22.02 ?  98  PRO   B HG2  1 
ATOM   5623 H HG3  . PRO   B 1 98  ? 35.218 -25.841 7.100   1.00 22.02 ?  98  PRO   B HG3  1 
ATOM   5624 H HD2  . PRO   B 1 98  ? 36.864 -25.012 5.324   1.00 20.98 ?  98  PRO   B HD2  1 
ATOM   5625 H HD3  . PRO   B 1 98  ? 36.225 -23.972 6.365   1.00 20.98 ?  98  PRO   B HD3  1 
ATOM   5626 N N    . ASN   B 1 99  ? 39.979 -26.519 9.211   1.00 19.02 ?  99  ASN   B N    1 
ATOM   5627 C CA   . ASN   B 1 99  ? 40.967 -27.588 9.370   1.00 20.31 ?  99  ASN   B CA   1 
ATOM   5628 C C    . ASN   B 1 99  ? 40.363 -28.658 10.274  1.00 22.87 ?  99  ASN   B C    1 
ATOM   5629 O O    . ASN   B 1 99  ? 40.343 -28.507 11.497  1.00 24.18 ?  99  ASN   B O    1 
ATOM   5630 C CB   . ASN   B 1 99  ? 42.247 -27.020 9.970   1.00 20.57 ?  99  ASN   B CB   1 
ATOM   5631 C CG   . ASN   B 1 99  ? 43.381 -28.028 10.005  1.00 21.13 ?  99  ASN   B CG   1 
ATOM   5632 O OD1  . ASN   B 1 99  ? 43.168 -29.211 10.225  1.00 21.98 ?  99  ASN   B OD1  1 
ATOM   5633 N ND2  . ASN   B 1 99  ? 44.592 -27.557 9.780   1.00 20.83 ?  99  ASN   B ND2  1 
ATOM   5634 H H    . ASN   B 1 99  ? 39.944 -25.978 9.876   1.00 22.83 ?  99  ASN   B H    1 
ATOM   5635 H HA   . ASN   B 1 99  ? 41.161 -27.987 8.509   1.00 24.38 ?  99  ASN   B HA   1 
ATOM   5636 H HB2  . ASN   B 1 99  ? 42.522 -26.262 9.441   1.00 24.68 ?  99  ASN   B HB2  1 
ATOM   5637 H HB3  . ASN   B 1 99  ? 42.059 -26.743 10.883  1.00 24.68 ?  99  ASN   B HB3  1 
ATOM   5638 H HD21 . ASN   B 1 99  ? 45.263 -28.087 9.784   1.00 25.00 ?  99  ASN   B HD21 1 
ATOM   5639 H HD22 . ASN   B 1 99  ? 44.698 -26.717 9.629   1.00 25.00 ?  99  ASN   B HD22 1 
ATOM   5640 N N    . VAL   B 1 100 ? 39.853 -29.734 9.663   1.00 25.71 ?  100 VAL   B N    1 
ATOM   5641 C CA   . VAL   B 1 100 ? 39.238 -30.817 10.430  1.00 29.20 ?  100 VAL   B CA   1 
ATOM   5642 C C    . VAL   B 1 100 ? 40.257 -31.491 11.340  1.00 29.94 ?  100 VAL   B C    1 
ATOM   5643 O O    . VAL   B 1 100 ? 39.904 -31.991 12.415  1.00 30.87 ?  100 VAL   B O    1 
ATOM   5644 C CB   . VAL   B 1 100 ? 38.542 -31.814 9.479   1.00 31.63 ?  100 VAL   B CB   1 
ATOM   5645 C CG1  . VAL   B 1 100 ? 38.041 -33.032 10.242  1.00 32.97 ?  100 VAL   B CG1  1 
ATOM   5646 C CG2  . VAL   B 1 100 ? 37.386 -31.129 8.761   1.00 32.16 ?  100 VAL   B CG2  1 
ATOM   5647 H H    . VAL   B 1 100 ? 39.832 -29.848 8.805   1.00 30.86 ?  100 VAL   B H    1 
ATOM   5648 H HA   . VAL   B 1 100 ? 38.540 -30.441 10.990  1.00 35.04 ?  100 VAL   B HA   1 
ATOM   5649 H HB   . VAL   B 1 100 ? 39.174 -32.119 8.808   1.00 37.95 ?  100 VAL   B HB   1 
ATOM   5650 H HG11 . VAL   B 1 100 ? 37.431 -33.533 9.675   1.00 39.57 ?  100 VAL   B HG11 1 
ATOM   5651 H HG12 . VAL   B 1 100 ? 38.797 -33.591 10.482  1.00 39.57 ?  100 VAL   B HG12 1 
ATOM   5652 H HG13 . VAL   B 1 100 ? 37.577 -32.736 11.040  1.00 39.57 ?  100 VAL   B HG13 1 
ATOM   5653 H HG21 . VAL   B 1 100 ? 36.936 -31.774 8.192   1.00 38.60 ?  100 VAL   B HG21 1 
ATOM   5654 H HG22 . VAL   B 1 100 ? 36.766 -30.783 9.422   1.00 38.60 ?  100 VAL   B HG22 1 
ATOM   5655 H HG23 . VAL   B 1 100 ? 37.736 -30.402 8.224   1.00 38.60 ?  100 VAL   B HG23 1 
ATOM   5656 N N    . ASN   B 1 101 ? 41.528 -31.529 10.932  1.00 30.90 ?  101 ASN   B N    1 
ATOM   5657 C CA   . ASN   B 1 101 ? 42.566 -32.072 11.806  1.00 32.13 ?  101 ASN   B CA   1 
ATOM   5658 C C    . ASN   B 1 101 ? 42.759 -31.230 13.061  1.00 35.52 ?  101 ASN   B C    1 
ATOM   5659 O O    . ASN   B 1 101 ? 43.377 -31.704 14.023  1.00 36.41 ?  101 ASN   B O    1 
ATOM   5660 C CB   . ASN   B 1 101 ? 43.886 -32.226 11.048  1.00 31.39 ?  101 ASN   B CB   1 
ATOM   5661 C CG   . ASN   B 1 101 ? 43.868 -33.401 10.085  1.00 30.43 ?  101 ASN   B CG   1 
ATOM   5662 O OD1  . ASN   B 1 101 ? 43.190 -34.395 10.321  1.00 30.96 ?  101 ASN   B OD1  1 
ATOM   5663 N ND2  . ASN   B 1 101 ? 44.605 -33.282 8.988   1.00 29.22 ?  101 ASN   B ND2  1 
ATOM   5664 H H    . ASN   B 1 101 ? 41.803 -31.267 10.161  1.00 37.08 ?  101 ASN   B H    1 
ATOM   5665 H HA   . ASN   B 1 101 ? 42.290 -32.955 12.090  1.00 38.55 ?  101 ASN   B HA   1 
ATOM   5666 H HB2  . ASN   B 1 101 ? 44.059 -31.422 10.537  1.00 37.67 ?  101 ASN   B HB2  1 
ATOM   5667 H HB3  . ASN   B 1 101 ? 44.600 -32.374 11.689  1.00 37.67 ?  101 ASN   B HB3  1 
ATOM   5668 H HD21 . ASN   B 1 101 ? 44.622 -33.921 8.414   1.00 35.07 ?  101 ASN   B HD21 1 
ATOM   5669 H HD22 . ASN   B 1 101 ? 45.060 -32.566 8.851   1.00 35.07 ?  101 ASN   B HD22 1 
ATOM   5670 N N    A LYS   B 1 102 ? 42.260 -29.993 13.067  0.80 37.56 ?  102 LYS   B N    1 
ATOM   5671 N N    B LYS   B 1 102 ? 42.256 -29.996 13.070  0.20 37.65 ?  102 LYS   B N    1 
ATOM   5672 C CA   A LYS   B 1 102 ? 42.205 -29.158 14.259  0.80 39.77 ?  102 LYS   B CA   1 
ATOM   5673 C CA   B LYS   B 1 102 ? 42.209 -29.168 14.266  0.20 39.66 ?  102 LYS   B CA   1 
ATOM   5674 C C    A LYS   B 1 102 ? 40.816 -29.131 14.884  0.80 39.11 ?  102 LYS   B C    1 
ATOM   5675 C C    B LYS   B 1 102 ? 40.826 -29.151 14.904  0.20 39.43 ?  102 LYS   B C    1 
ATOM   5676 O O    A LYS   B 1 102 ? 40.567 -28.323 15.784  0.80 39.45 ?  102 LYS   B O    1 
ATOM   5677 O O    B LYS   B 1 102 ? 40.595 -28.380 15.841  0.20 39.79 ?  102 LYS   B O    1 
ATOM   5678 C CB   A LYS   B 1 102 ? 42.631 -27.726 13.931  0.80 42.86 ?  102 LYS   B CB   1 
ATOM   5679 C CB   B LYS   B 1 102 ? 42.649 -27.738 13.942  0.20 41.84 ?  102 LYS   B CB   1 
ATOM   5680 C CG   A LYS   B 1 102 ? 44.094 -27.542 13.572  0.80 45.68 ?  102 LYS   B CG   1 
ATOM   5681 C CG   B LYS   B 1 102 ? 44.110 -27.599 13.547  0.20 43.64 ?  102 LYS   B CG   1 
ATOM   5682 C CD   A LYS   B 1 102 ? 44.341 -26.097 13.165  0.80 48.52 ?  102 LYS   B CD   1 
ATOM   5683 C CD   B LYS   B 1 102 ? 44.406 -26.179 13.087  0.20 45.31 ?  102 LYS   B CD   1 
ATOM   5684 C CE   A LYS   B 1 102 ? 45.806 -25.811 12.895  0.80 50.51 ?  102 LYS   B CE   1 
ATOM   5685 C CE   B LYS   B 1 102 ? 45.891 -25.954 12.861  0.20 46.44 ?  102 LYS   B CE   1 
ATOM   5686 N NZ   A LYS   B 1 102 ? 46.006 -24.391 12.480  0.80 51.73 ?  102 LYS   B NZ   1 
ATOM   5687 N NZ   B LYS   B 1 102 ? 46.166 -24.565 12.397  0.20 47.11 ?  102 LYS   B NZ   1 
ATOM   5688 H H    A LYS   B 1 102 ? 41.941 -29.606 12.369  0.80 45.07 ?  102 LYS   B H    1 
ATOM   5689 H H    B LYS   B 1 102 ? 41.929 -29.608 12.375  0.20 45.18 ?  102 LYS   B H    1 
ATOM   5690 H HA   A LYS   B 1 102 ? 42.824 -29.507 14.917  0.80 47.73 ?  102 LYS   B HA   1 
ATOM   5691 H HA   B LYS   B 1 102 ? 42.829 -29.525 14.919  0.20 47.60 ?  102 LYS   B HA   1 
ATOM   5692 H HB2  A LYS   B 1 102 ? 42.107 -27.413 13.178  0.80 51.43 ?  102 LYS   B HB2  1 
ATOM   5693 H HB2  B LYS   B 1 102 ? 42.113 -27.407 13.206  0.20 50.21 ?  102 LYS   B HB2  1 
ATOM   5694 H HB3  A LYS   B 1 102 ? 42.452 -27.167 14.704  0.80 51.43 ?  102 LYS   B HB3  1 
ATOM   5695 H HB3  B LYS   B 1 102 ? 42.505 -27.184 14.726  0.20 50.21 ?  102 LYS   B HB3  1 
ATOM   5696 H HG2  A LYS   B 1 102 ? 44.648 -27.745 14.343  0.80 54.82 ?  102 LYS   B HG2  1 
ATOM   5697 H HG2  B LYS   B 1 102 ? 44.674 -27.797 14.312  0.20 52.36 ?  102 LYS   B HG2  1 
ATOM   5698 H HG3  A LYS   B 1 102 ? 44.323 -28.118 12.826  0.80 54.82 ?  102 LYS   B HG3  1 
ATOM   5699 H HG3  B LYS   B 1 102 ? 44.307 -28.206 12.816  0.20 52.36 ?  102 LYS   B HG3  1 
ATOM   5700 H HD2  A LYS   B 1 102 ? 43.842 -25.907 12.354  0.80 58.23 ?  102 LYS   B HD2  1 
ATOM   5701 H HD2  B LYS   B 1 102 ? 43.944 -26.013 12.249  0.20 54.38 ?  102 LYS   B HD2  1 
ATOM   5702 H HD3  A LYS   B 1 102 ? 44.046 -25.511 13.880  0.80 58.23 ?  102 LYS   B HD3  1 
ATOM   5703 H HD3  B LYS   B 1 102 ? 44.104 -25.554 13.764  0.20 54.38 ?  102 LYS   B HD3  1 
ATOM   5704 H HE2  A LYS   B 1 102 ? 46.319 -25.968 13.703  0.80 60.61 ?  102 LYS   B HE2  1 
ATOM   5705 H HE2  B LYS   B 1 102 ? 46.368 -26.096 13.694  0.20 55.72 ?  102 LYS   B HE2  1 
ATOM   5706 H HE3  A LYS   B 1 102 ? 46.119 -26.386 12.179  0.80 60.61 ?  102 LYS   B HE3  1 
ATOM   5707 H HE3  B LYS   B 1 102 ? 46.210 -26.570 12.183  0.20 55.72 ?  102 LYS   B HE3  1 
ATOM   5708 H HZ1  A LYS   B 1 102 ? 46.868 -24.238 12.325  0.80 62.08 ?  102 LYS   B HZ1  1 
ATOM   5709 H HZ1  B LYS   B 1 102 ? 47.040 -24.453 12.271  0.20 56.53 ?  102 LYS   B HZ1  1 
ATOM   5710 H HZ2  A LYS   B 1 102 ? 45.544 -24.224 11.738  0.80 62.08 ?  102 LYS   B HZ2  1 
ATOM   5711 H HZ2  B LYS   B 1 102 ? 45.741 -24.411 11.630  0.20 56.53 ?  102 LYS   B HZ2  1 
ATOM   5712 H HZ3  A LYS   B 1 102 ? 45.725 -23.844 13.124  0.80 62.08 ?  102 LYS   B HZ3  1 
ATOM   5713 H HZ3  B LYS   B 1 102 ? 45.884 -23.980 13.006  0.20 56.53 ?  102 LYS   B HZ3  1 
ATOM   5714 N N    . GLY   B 1 103 ? 39.902 -29.977 14.416  1.00 38.93 ?  103 GLY   B N    1 
ATOM   5715 C CA   . GLY   B 1 103 ? 38.569 -30.047 14.980  1.00 38.50 ?  103 GLY   B CA   1 
ATOM   5716 C C    . GLY   B 1 103 ? 37.616 -28.962 14.535  1.00 37.55 ?  103 GLY   B C    1 
ATOM   5717 O O    . GLY   B 1 103 ? 36.528 -28.846 15.110  1.00 37.95 ?  103 GLY   B O    1 
ATOM   5718 H H    A GLY   B 1 103 ? 40.032 -30.521 13.765  0.80 46.72 ?  103 GLY   B H    1 
ATOM   5719 H H    B GLY   B 1 103 ? 40.027 -30.510 13.754  0.20 46.72 ?  103 GLY   B H    1 
ATOM   5720 H HA2  . GLY   B 1 103 ? 38.177 -30.904 14.751  1.00 46.20 ?  103 GLY   B HA2  1 
ATOM   5721 H HA3  . GLY   B 1 103 ? 38.633 -29.997 15.946  1.00 46.20 ?  103 GLY   B HA3  1 
ATOM   5722 N N    A GLU   B 1 104 ? 37.990 -28.155 13.545  0.80 36.17 ?  104 GLU   B N    1 
ATOM   5723 N N    B GLU   B 1 104 ? 37.971 -28.179 13.521  0.20 37.13 ?  104 GLU   B N    1 
ATOM   5724 C CA   A GLU   B 1 104 ? 37.140 -27.062 13.103  0.80 34.81 ?  104 GLU   B CA   1 
ATOM   5725 C CA   B GLU   B 1 104 ? 37.105 -27.104 13.066  0.20 36.51 ?  104 GLU   B CA   1 
ATOM   5726 C C    A GLU   B 1 104 ? 35.947 -27.591 12.307  0.80 35.35 ?  104 GLU   B C    1 
ATOM   5727 C C    B GLU   B 1 104 ? 35.935 -27.653 12.251  0.20 36.83 ?  104 GLU   B C    1 
ATOM   5728 O O    A GLU   B 1 104 ? 35.973 -28.690 11.743  0.80 36.04 ?  104 GLU   B O    1 
ATOM   5729 O O    B GLU   B 1 104 ? 35.995 -28.744 11.677  0.20 37.01 ?  104 GLU   B O    1 
ATOM   5730 C CB   A GLU   B 1 104 ? 37.953 -26.059 12.282  0.80 33.59 ?  104 GLU   B CB   1 
ATOM   5731 C CB   B GLU   B 1 104 ? 37.909 -26.081 12.263  0.20 35.67 ?  104 GLU   B CB   1 
ATOM   5732 C CG   A GLU   B 1 104 ? 39.051 -25.397 13.104  0.80 32.34 ?  104 GLU   B CG   1 
ATOM   5733 C CG   B GLU   B 1 104 ? 39.007 -25.422 13.085  0.20 34.99 ?  104 GLU   B CG   1 
ATOM   5734 C CD   A GLU   B 1 104 ? 39.981 -24.513 12.295  0.80 31.21 ?  104 GLU   B CD   1 
ATOM   5735 C CD   B GLU   B 1 104 ? 39.918 -24.539 12.257  0.20 34.49 ?  104 GLU   B CD   1 
ATOM   5736 O OE1  A GLU   B 1 104 ? 39.980 -24.592 11.049  0.80 29.17 ?  104 GLU   B OE1  1 
ATOM   5737 O OE1  B GLU   B 1 104 ? 39.814 -24.567 11.013  0.20 34.03 ?  104 GLU   B OE1  1 
ATOM   5738 O OE2  A GLU   B 1 104 ? 40.732 -23.738 12.923  0.80 31.21 -1 104 GLU   B OE2  1 
ATOM   5739 O OE2  B GLU   B 1 104 ? 40.742 -23.814 12.854  0.20 34.40 -1 104 GLU   B OE2  1 
ATOM   5740 H H    A GLU   B 1 104 ? 38.736 -28.214 13.122  0.80 43.41 ?  104 GLU   B H    1 
ATOM   5741 H H    B GLU   B 1 104 ? 38.711 -28.246 13.086  0.20 44.55 ?  104 GLU   B H    1 
ATOM   5742 H HA   A GLU   B 1 104 ? 36.797 -26.598 13.882  0.80 41.78 ?  104 GLU   B HA   1 
ATOM   5743 H HA   B GLU   B 1 104 ? 36.737 -26.650 13.838  0.20 43.81 ?  104 GLU   B HA   1 
ATOM   5744 H HB2  A GLU   B 1 104 ? 38.367 -26.518 11.536  0.80 40.31 ?  104 GLU   B HB2  1 
ATOM   5745 H HB2  B GLU   B 1 104 ? 38.325 -26.525 11.508  0.20 42.81 ?  104 GLU   B HB2  1 
ATOM   5746 H HB3  A GLU   B 1 104 ? 37.359 -25.362 11.956  0.80 40.31 ?  104 GLU   B HB3  1 
ATOM   5747 H HB3  B GLU   B 1 104 ? 37.312 -25.383 11.948  0.20 42.81 ?  104 GLU   B HB3  1 
ATOM   5748 H HG2  A GLU   B 1 104 ? 38.642 -24.847 13.791  0.80 38.81 ?  104 GLU   B HG2  1 
ATOM   5749 H HG2  B GLU   B 1 104 ? 38.599 -24.871 13.772  0.20 41.99 ?  104 GLU   B HG2  1 
ATOM   5750 H HG3  A GLU   B 1 104 ? 39.594 -26.085 13.515  0.80 38.81 ?  104 GLU   B HG3  1 
ATOM   5751 H HG3  B GLU   B 1 104 ? 39.549 -26.114 13.499  0.20 41.99 ?  104 GLU   B HG3  1 
ATOM   5752 N N    A ASP   B 1 105 ? 34.888 -26.784 12.271  0.80 34.37 ?  105 ASP   B N    1 
ATOM   5753 N N    B ASP   B 1 105 ? 34.857 -26.871 12.209  0.20 36.61 ?  105 ASP   B N    1 
ATOM   5754 C CA   A ASP   B 1 105 ? 33.613 -27.222 11.718  0.80 34.93 ?  105 ASP   B CA   1 
ATOM   5755 C CA   B ASP   B 1 105 ? 33.598 -27.323 11.631  0.20 36.70 ?  105 ASP   B CA   1 
ATOM   5756 C C    A ASP   B 1 105 ? 33.686 -27.274 10.198  0.80 32.94 ?  105 ASP   B C    1 
ATOM   5757 C C    B ASP   B 1 105 ? 33.695 -27.341 10.110  0.20 35.53 ?  105 ASP   B C    1 
ATOM   5758 O O    A ASP   B 1 105 ? 33.884 -26.246 9.542   0.80 32.01 ?  105 ASP   B O    1 
ATOM   5759 O O    B ASP   B 1 105 ? 33.931 -26.305 9.480   0.20 35.32 ?  105 ASP   B O    1 
ATOM   5760 C CB   A ASP   B 1 105 ? 32.505 -26.269 12.162  0.80 37.87 ?  105 ASP   B CB   1 
ATOM   5761 C CB   B ASP   B 1 105 ? 32.465 -26.403 12.083  0.20 37.77 ?  105 ASP   B CB   1 
ATOM   5762 C CG   A ASP   B 1 105 ? 31.133 -26.727 11.718  0.80 40.76 ?  105 ASP   B CG   1 
ATOM   5763 C CG   B ASP   B 1 105 ? 31.096 -26.937 11.706  0.20 38.87 ?  105 ASP   B CG   1 
ATOM   5764 O OD1  A ASP   B 1 105 ? 31.027 -27.846 11.173  0.80 40.86 ?  105 ASP   B OD1  1 
ATOM   5765 O OD1  B ASP   B 1 105 ? 31.028 -28.009 11.069  0.20 39.18 ?  105 ASP   B OD1  1 
ATOM   5766 O OD2  A ASP   B 1 105 ? 30.159 -25.966 11.910  0.80 42.66 -1 105 ASP   B OD2  1 
ATOM   5767 O OD2  B ASP   B 1 105 ? 30.087 -26.286 12.051  0.20 39.29 -1 105 ASP   B OD2  1 
ATOM   5768 H H    A ASP   B 1 105 ? 34.885 -25.974 12.556  0.80 41.25 ?  105 ASP   B H    1 
ATOM   5769 H H    B ASP   B 1 105 ? 34.832 -26.068 12.506  0.20 43.94 ?  105 ASP   B H    1 
ATOM   5770 H HA   A ASP   B 1 105 ? 33.401 -28.109 12.048  0.80 41.92 ?  105 ASP   B HA   1 
ATOM   5771 H HA   B ASP   B 1 105 ? 33.399 -28.222 11.936  0.20 44.04 ?  105 ASP   B HA   1 
ATOM   5772 H HB2  A ASP   B 1 105 ? 32.513 -26.198 13.131  0.80 45.44 ?  105 ASP   B HB2  1 
ATOM   5773 H HB2  B ASP   B 1 105 ? 32.495 -26.310 13.050  0.20 45.33 ?  105 ASP   B HB2  1 
ATOM   5774 H HB3  A ASP   B 1 105 ? 32.651 -25.398 11.765  0.80 45.44 ?  105 ASP   B HB3  1 
ATOM   5775 H HB3  B ASP   B 1 105 ? 32.571 -25.533 11.665  0.20 45.33 ?  105 ASP   B HB3  1 
ATOM   5776 N N    A ILE   B 1 106 ? 33.498 -28.473 9.640   0.80 32.21 ?  106 ILE   B N    1 
ATOM   5777 N N    B ILE   B 1 106 ? 33.506 -28.525 9.521   0.20 34.44 ?  106 ILE   B N    1 
ATOM   5778 C CA   A ILE   B 1 106 ? 33.494 -28.655 8.194   0.80 31.02 ?  106 ILE   B CA   1 
ATOM   5779 C CA   B ILE   B 1 106 ? 33.513 -28.669 8.070   0.20 33.50 ?  106 ILE   B CA   1 
ATOM   5780 C C    A ILE   B 1 106 ? 32.406 -27.824 7.523   0.80 29.28 ?  106 ILE   B C    1 
ATOM   5781 C C    B ILE   B 1 106 ? 32.411 -27.845 7.417   0.20 32.48 ?  106 ILE   B C    1 
ATOM   5782 O O    A ILE   B 1 106 ? 32.510 -27.515 6.332   0.80 28.26 ?  106 ILE   B O    1 
ATOM   5783 O O    B ILE   B 1 106 ? 32.480 -27.560 6.217   0.20 32.32 ?  106 ILE   B O    1 
ATOM   5784 C CB   A ILE   B 1 106 ? 33.372 -30.162 7.863   0.80 31.68 ?  106 ILE   B CB   1 
ATOM   5785 C CB   B ILE   B 1 106 ? 33.412 -30.166 7.697   0.20 33.58 ?  106 ILE   B CB   1 
ATOM   5786 C CG1  A ILE   B 1 106 ? 33.620 -30.424 6.379   0.80 31.95 ?  106 ILE   B CG1  1 
ATOM   5787 C CG1  B ILE   B 1 106 ? 33.687 -30.383 6.207   0.20 33.48 ?  106 ILE   B CG1  1 
ATOM   5788 C CG2  A ILE   B 1 106 ? 32.003 -30.695 8.275   0.80 32.60 ?  106 ILE   B CG2  1 
ATOM   5789 C CG2  B ILE   B 1 106 ? 32.043 -30.722 8.068   0.20 33.81 ?  106 ILE   B CG2  1 
ATOM   5790 C CD1  A ILE   B 1 106 ? 34.994 -30.011 5.917   0.80 31.76 ?  106 ILE   B CD1  1 
ATOM   5791 C CD1  B ILE   B 1 106 ? 35.044 -29.895 5.762   0.20 33.41 ?  106 ILE   B CD1  1 
ATOM   5792 H H    A ILE   B 1 106 ? 33.366 -29.196 10.086  0.80 38.66 ?  106 ILE   B H    1 
ATOM   5793 H H    B ILE   B 1 106 ? 33.384 -29.261 9.944   0.20 41.33 ?  106 ILE   B H    1 
ATOM   5794 H HA   A ILE   B 1 106 ? 34.342 -28.348 7.852   0.80 37.23 ?  106 ILE   B HA   1 
ATOM   5795 H HA   B ILE   B 1 106 ? 34.357 -28.335 7.738   0.20 40.20 ?  106 ILE   B HA   1 
ATOM   5796 H HB   A ILE   B 1 106 ? 34.042 -30.640 8.373   0.80 38.01 ?  106 ILE   B HB   1 
ATOM   5797 H HB   B ILE   B 1 106 ? 34.081 -30.651 8.203   0.20 40.29 ?  106 ILE   B HB   1 
ATOM   5798 H HG12 A ILE   B 1 106 ? 33.528 -31.375 6.208   0.80 38.34 ?  106 ILE   B HG12 1 
ATOM   5799 H HG12 B ILE   B 1 106 ? 33.641 -31.335 6.017   0.20 40.18 ?  106 ILE   B HG12 1 
ATOM   5800 H HG13 A ILE   B 1 106 ? 32.971 -29.933 5.855   0.80 38.34 ?  106 ILE   B HG13 1 
ATOM   5801 H HG13 B ILE   B 1 106 ? 33.017 -29.913 5.689   0.20 40.18 ?  106 ILE   B HG13 1 
ATOM   5802 H HG21 A ILE   B 1 106 ? 32.002 -31.661 8.192   0.80 39.12 ?  106 ILE   B HG21 1 
ATOM   5803 H HG21 B ILE   B 1 106 ? 32.061 -31.688 7.982   0.20 40.57 ?  106 ILE   B HG21 1 
ATOM   5804 H HG22 A ILE   B 1 106 ? 31.828 -30.443 9.195   0.80 39.12 ?  106 ILE   B HG22 1 
ATOM   5805 H HG22 B ILE   B 1 106 ? 31.841 -30.476 8.984   0.20 40.57 ?  106 ILE   B HG22 1 
ATOM   5806 H HG23 A ILE   B 1 106 ? 31.325 -30.314 7.695   0.80 39.12 ?  106 ILE   B HG23 1 
ATOM   5807 H HG23 B ILE   B 1 106 ? 31.376 -30.350 7.470   0.20 40.57 ?  106 ILE   B HG23 1 
ATOM   5808 H HD11 A ILE   B 1 106 ? 35.172 -30.416 5.054   0.80 38.11 ?  106 ILE   B HD11 1 
ATOM   5809 H HD11 B ILE   B 1 106 ? 35.253 -30.290 4.903   0.20 40.09 ?  106 ILE   B HD11 1 
ATOM   5810 H HD12 A ILE   B 1 106 ? 35.026 -29.044 5.839   0.80 38.11 ?  106 ILE   B HD12 1 
ATOM   5811 H HD12 B ILE   B 1 106 ? 35.022 -28.928 5.687   0.20 40.09 ?  106 ILE   B HD12 1 
ATOM   5812 H HD13 A ILE   B 1 106 ? 35.650 -30.313 6.565   0.80 38.11 ?  106 ILE   B HD13 1 
ATOM   5813 H HD13 B ILE   B 1 106 ? 35.705 -30.163 6.420   0.20 40.09 ?  106 ILE   B HD13 1 
ATOM   5814 N N    A GLN   B 1 107 ? 31.365 -27.437 8.263   0.80 29.74 ?  107 GLN   B N    1 
ATOM   5815 N N    B GLN   B 1 107 ? 31.390 -27.452 8.181   0.20 31.91 ?  107 GLN   B N    1 
ATOM   5816 C CA   A GLN   B 1 107 ? 30.288 -26.646 7.675   0.80 29.73 ?  107 GLN   B CA   1 
ATOM   5817 C CA   B GLN   B 1 107 ? 30.301 -26.656 7.627   0.20 31.12 ?  107 GLN   B CA   1 
ATOM   5818 C C    A GLN   B 1 107 ? 30.770 -25.294 7.165   0.80 26.96 ?  107 GLN   B C    1 
ATOM   5819 C C    B GLN   B 1 107 ? 30.766 -25.281 7.161   0.20 28.04 ?  107 GLN   B C    1 
ATOM   5820 O O    A GLN   B 1 107 ? 30.124 -24.716 6.287   0.80 27.22 ?  107 GLN   B O    1 
ATOM   5821 O O    B GLN   B 1 107 ? 30.097 -24.667 6.324   0.20 28.19 ?  107 GLN   B O    1 
ATOM   5822 C CB   A GLN   B 1 107 ? 29.163 -26.451 8.696   0.80 34.08 ?  107 GLN   B CB   1 
ATOM   5823 C CB   B GLN   B 1 107 ? 29.184 -26.519 8.667   0.20 33.71 ?  107 GLN   B CB   1 
ATOM   5824 C CG   A GLN   B 1 107 ? 27.835 -25.980 8.103   0.80 38.06 ?  107 GLN   B CG   1 
ATOM   5825 C CG   B GLN   B 1 107 ? 27.841 -26.070 8.105   0.20 35.90 ?  107 GLN   B CG   1 
ATOM   5826 C CD   A GLN   B 1 107 ? 27.739 -24.467 7.987   0.80 41.12 ?  107 GLN   B CD   1 
ATOM   5827 C CD   B GLN   B 1 107 ? 27.690 -24.561 8.068   0.20 37.64 ?  107 GLN   B CD   1 
ATOM   5828 O OE1  A GLN   B 1 107 ? 28.552 -23.736 8.555   0.80 42.18 ?  107 GLN   B OE1  1 
ATOM   5829 O OE1  B GLN   B 1 107 ? 28.481 -23.830 8.665   0.20 38.19 ?  107 GLN   B OE1  1 
ATOM   5830 N NE2  A GLN   B 1 107 ? 26.738 -23.991 7.251   0.80 42.17 ?  107 GLN   B NE2  1 
ATOM   5831 N NE2  B GLN   B 1 107 ? 26.666 -24.086 7.368   0.20 38.29 ?  107 GLN   B NE2  1 
ATOM   5832 H H    A GLN   B 1 107 ? 31.263 -27.611 9.093   0.80 35.69 ?  107 GLN   B H    1 
ATOM   5833 H H    B GLN   B 1 107 ? 31.302 -27.638 9.014   0.20 38.29 ?  107 GLN   B H    1 
ATOM   5834 H HA   A GLN   B 1 107 ? 29.921 -27.133 6.919   0.80 35.67 ?  107 GLN   B HA   1 
ATOM   5835 H HA   B GLN   B 1 107 ? 29.932 -27.121 6.860   0.20 37.34 ?  107 GLN   B HA   1 
ATOM   5836 H HB2  A GLN   B 1 107 ? 29.000 -27.296 9.136   0.80 40.90 ?  107 GLN   B HB2  1 
ATOM   5837 H HB2  B GLN   B 1 107 ? 29.048 -27.381 9.087   0.20 40.45 ?  107 GLN   B HB2  1 
ATOM   5838 H HB3  A GLN   B 1 107 ? 29.447 -25.791 9.347   0.80 40.90 ?  107 GLN   B HB3  1 
ATOM   5839 H HB3  B GLN   B 1 107 ? 29.457 -25.872 9.335   0.20 40.45 ?  107 GLN   B HB3  1 
ATOM   5840 H HG2  A GLN   B 1 107 ? 27.733 -26.352 7.214   0.80 45.67 ?  107 GLN   B HG2  1 
ATOM   5841 H HG2  B GLN   B 1 107 ? 27.749 -26.402 7.199   0.20 43.08 ?  107 GLN   B HG2  1 
ATOM   5842 H HG3  A GLN   B 1 107 ? 27.110 -26.285 8.674   0.80 45.67 ?  107 GLN   B HG3  1 
ATOM   5843 H HG3  B GLN   B 1 107 ? 27.130 -26.431 8.662   0.20 43.08 ?  107 GLN   B HG3  1 
ATOM   5844 H HE21 A GLN   B 1 107 ? 26.188 -24.532 6.869   0.80 50.60 ?  107 GLN   B HE21 1 
ATOM   5845 H HE21 B GLN   B 1 107 ? 26.133 -24.627 6.963   0.20 45.94 ?  107 GLN   B HE21 1 
ATOM   5846 H HE22 A GLN   B 1 107 ? 26.636 -23.141 7.157   0.80 50.60 ?  107 GLN   B HE22 1 
ATOM   5847 H HE22 B GLN   B 1 107 ? 26.536 -23.238 7.319   0.20 45.94 ?  107 GLN   B HE22 1 
ATOM   5848 N N    . LEU   B 1 108 ? 31.893 -24.785 7.676   1.00 24.97 ?  108 LEU   B N    1 
ATOM   5849 C CA   . LEU   B 1 108 ? 32.421 -23.485 7.257   1.00 21.55 ?  108 LEU   B CA   1 
ATOM   5850 C C    . LEU   B 1 108 ? 33.079 -23.517 5.886   1.00 18.36 ?  108 LEU   B C    1 
ATOM   5851 O O    . LEU   B 1 108 ? 33.502 -22.467 5.387   1.00 17.05 ?  108 LEU   B O    1 
ATOM   5852 C CB   . LEU   B 1 108 ? 33.398 -22.948 8.303   1.00 22.03 ?  108 LEU   B CB   1 
ATOM   5853 C CG   . LEU   B 1 108 ? 32.759 -22.429 9.590   1.00 23.58 ?  108 LEU   B CG   1 
ATOM   5854 C CD1  . LEU   B 1 108 ? 33.773 -22.411 10.709  1.00 24.02 ?  108 LEU   B CD1  1 
ATOM   5855 C CD2  . LEU   B 1 108 ? 32.198 -21.030 9.372   1.00 24.29 ?  108 LEU   B CD2  1 
ATOM   5856 H H    A LEU   B 1 108 ? 32.359 -25.170 8.285   0.80 29.96 ?  108 LEU   B H    1 
ATOM   5857 H H    B LEU   B 1 108 ? 32.361 -25.177 8.279   0.20 29.96 ?  108 LEU   B H    1 
ATOM   5858 H HA   . LEU   B 1 108 ? 31.682 -22.862 7.206   1.00 25.86 ?  108 LEU   B HA   1 
ATOM   5859 H HB2  . LEU   B 1 108 ? 34.004 -23.659 8.552   1.00 26.43 ?  108 LEU   B HB2  1 
ATOM   5860 H HB3  . LEU   B 1 108 ? 33.892 -22.214 7.912   1.00 26.43 ?  108 LEU   B HB3  1 
ATOM   5861 H HG   . LEU   B 1 108 ? 32.025 -23.011 9.851   1.00 28.29 ?  108 LEU   B HG   1 
ATOM   5862 H HD11 . LEU   B 1 108 ? 33.340 -22.110 11.524  1.00 28.83 ?  108 LEU   B HD11 1 
ATOM   5863 H HD12 . LEU   B 1 108 ? 34.122 -23.306 10.831  1.00 28.83 ?  108 LEU   B HD12 1 
ATOM   5864 H HD13 . LEU   B 1 108 ? 34.490 -21.803 10.472  1.00 28.83 ?  108 LEU   B HD13 1 
ATOM   5865 H HD21 . LEU   B 1 108 ? 31.799 -20.714 10.199  1.00 29.15 ?  108 LEU   B HD21 1 
ATOM   5866 H HD22 . LEU   B 1 108 ? 32.920 -20.439 9.107   1.00 29.15 ?  108 LEU   B HD22 1 
ATOM   5867 H HD23 . LEU   B 1 108 ? 31.525 -21.064 8.674   1.00 29.15 ?  108 LEU   B HD23 1 
ATOM   5868 N N    . LEU   B 1 109 ? 33.152 -24.685 5.260   1.00 16.72 ?  109 LEU   B N    1 
ATOM   5869 C CA   . LEU   B 1 109 ? 33.782 -24.799 3.952   1.00 15.66 ?  109 LEU   B CA   1 
ATOM   5870 C C    . LEU   B 1 109 ? 33.005 -24.044 2.882   1.00 14.88 ?  109 LEU   B C    1 
ATOM   5871 O O    . LEU   B 1 109 ? 33.618 -23.459 1.981   1.00 14.50 ?  109 LEU   B O    1 
ATOM   5872 C CB   . LEU   B 1 109 ? 33.931 -26.283 3.596   1.00 16.04 ?  109 LEU   B CB   1 
ATOM   5873 C CG   . LEU   B 1 109 ? 34.673 -26.651 2.315   1.00 15.46 ?  109 LEU   B CG   1 
ATOM   5874 C CD1  . LEU   B 1 109 ? 36.040 -25.986 2.282   1.00 15.13 ?  109 LEU   B CD1  1 
ATOM   5875 C CD2  . LEU   B 1 109 ? 34.823 -28.166 2.203   1.00 16.25 ?  109 LEU   B CD2  1 
ATOM   5876 H H    . LEU   B 1 109 ? 32.863 -25.430 5.572   1.00 20.06 ?  109 LEU   B H    1 
ATOM   5877 H HA   . LEU   B 1 109 ? 34.673 -24.413 3.992   1.00 18.79 ?  109 LEU   B HA   1 
ATOM   5878 H HB2  . LEU   B 1 109 ? 34.405 -26.717 4.320   1.00 19.25 ?  109 LEU   B HB2  1 
ATOM   5879 H HB3  . LEU   B 1 109 ? 33.043 -26.663 3.523   1.00 19.25 ?  109 LEU   B HB3  1 
ATOM   5880 H HG   . LEU   B 1 109 ? 34.159 -26.355 1.545   1.00 18.55 ?  109 LEU   B HG   1 
ATOM   5881 H HD11 . LEU   B 1 109 ? 36.547 -26.346 1.537   1.00 18.16 ?  109 LEU   B HD11 1 
ATOM   5882 H HD12 . LEU   B 1 109 ? 35.915 -25.033 2.169   1.00 18.16 ?  109 LEU   B HD12 1 
ATOM   5883 H HD13 . LEU   B 1 109 ? 36.496 -26.171 3.114   1.00 18.16 ?  109 LEU   B HD13 1 
ATOM   5884 H HD21 . LEU   B 1 109 ? 35.375 -28.375 1.429   1.00 19.50 ?  109 LEU   B HD21 1 
ATOM   5885 H HD22 . LEU   B 1 109 ? 35.251 -28.502 3.007   1.00 19.50 ?  109 LEU   B HD22 1 
ATOM   5886 H HD23 . LEU   B 1 109 ? 33.948 -28.573 2.101   1.00 19.50 ?  109 LEU   B HD23 1 
ATOM   5887 N N    . LYS   B 1 110 ? 31.669 -24.003 2.972   1.00 14.56 ?  110 LYS   B N    1 
ATOM   5888 C CA   . LYS   B 1 110 ? 30.908 -23.249 1.981   1.00 14.47 ?  110 LYS   B CA   1 
ATOM   5889 C C    . LYS   B 1 110 ? 31.245 -21.761 2.058   1.00 14.06 ?  110 LYS   B C    1 
ATOM   5890 O O    . LYS   B 1 110 ? 31.510 -21.123 1.035   1.00 13.96 ?  110 LYS   B O    1 
ATOM   5891 C CB   . LYS   B 1 110 ? 29.404 -23.491 2.139   1.00 15.49 ?  110 LYS   B CB   1 
ATOM   5892 C CG   . LYS   B 1 110 ? 28.597 -22.891 0.991   1.00 16.01 ?  110 LYS   B CG   1 
ATOM   5893 C CD   . LYS   B 1 110 ? 27.130 -23.311 1.031   1.00 16.15 ?  110 LYS   B CD   1 
ATOM   5894 C CE   . LYS   B 1 110 ? 26.366 -22.778 -0.179  1.00 17.37 ?  110 LYS   B CE   1 
ATOM   5895 N NZ   . LYS   B 1 110 ? 26.691 -23.507 -1.431  1.00 17.52 ?  110 LYS   B NZ   1 
ATOM   5896 H H    . LYS   B 1 110 ? 31.203 -24.393 3.576   1.00 17.47 ?  110 LYS   B H    1 
ATOM   5897 H HA   . LYS   B 1 110 ? 31.158 -23.559 1.096   1.00 17.37 ?  110 LYS   B HA   1 
ATOM   5898 H HB2  . LYS   B 1 110 ? 29.237 -24.447 2.156   1.00 18.59 ?  110 LYS   B HB2  1 
ATOM   5899 H HB3  . LYS   B 1 110 ? 29.102 -23.086 2.967   1.00 18.59 ?  110 LYS   B HB3  1 
ATOM   5900 H HG2  . LYS   B 1 110 ? 28.636 -21.921 1.051   1.00 19.21 ?  110 LYS   B HG2  1 
ATOM   5901 H HG3  . LYS   B 1 110 ? 28.975 -23.186 0.149   1.00 19.21 ?  110 LYS   B HG3  1 
ATOM   5902 H HD2  . LYS   B 1 110 ? 27.073 -24.280 1.029   1.00 19.38 ?  110 LYS   B HD2  1 
ATOM   5903 H HD3  . LYS   B 1 110 ? 26.715 -22.955 1.836   1.00 19.38 ?  110 LYS   B HD3  1 
ATOM   5904 H HE2  . LYS   B 1 110 ? 25.416 -22.868 -0.018  1.00 20.85 ?  110 LYS   B HE2  1 
ATOM   5905 H HE3  . LYS   B 1 110 ? 26.596 -21.845 -0.309  1.00 20.85 ?  110 LYS   B HE3  1 
ATOM   5906 H HZ1  . LYS   B 1 110 ? 26.229 -23.168 -2.109  1.00 21.02 ?  110 LYS   B HZ1  1 
ATOM   5907 H HZ2  . LYS   B 1 110 ? 27.561 -23.437 -1.607  1.00 21.02 ?  110 LYS   B HZ2  1 
ATOM   5908 H HZ3  . LYS   B 1 110 ? 26.485 -24.370 -1.342  1.00 21.02 ?  110 LYS   B HZ3  1 
ATOM   5909 N N    . SER   B 1 111 ? 31.279 -21.204 3.274   1.00 14.89 ?  111 SER   B N    1 
ATOM   5910 C CA   . SER   B 1 111 ? 31.670 -19.807 3.446   1.00 15.02 ?  111 SER   B CA   1 
ATOM   5911 C C    . SER   B 1 111 ? 33.050 -19.551 2.848   1.00 14.02 ?  111 SER   B C    1 
ATOM   5912 O O    . SER   B 1 111 ? 33.273 -18.522 2.193   1.00 14.10 ?  111 SER   B O    1 
ATOM   5913 C CB   . SER   B 1 111 ? 31.679 -19.447 4.931   1.00 16.36 ?  111 SER   B CB   1 
ATOM   5914 O OG   . SER   B 1 111 ? 30.379 -19.449 5.487   1.00 17.44 ?  111 SER   B OG   1 
ATOM   5915 H H    . SER   B 1 111 ? 31.095 -21.621 4.002   1.00 17.87 ?  111 SER   B H    1 
ATOM   5916 H HA   . SER   B 1 111 ? 31.031 -19.240 2.992   1.00 18.03 ?  111 SER   B HA   1 
ATOM   5917 H HB2  . SER   B 1 111 ? 32.213 -20.104 5.406   1.00 19.63 ?  111 SER   B HB2  1 
ATOM   5918 H HB3  . SER   B 1 111 ? 32.070 -18.569 5.034   1.00 19.63 ?  111 SER   B HB3  1 
ATOM   5919 H HG   . SER   B 1 111 ? 30.416 -19.235 6.304   1.00 20.93 ?  111 SER   B HG   1 
ATOM   5920 N N    . ALA   B 1 112 ? 33.989 -20.475 3.067   1.00 13.87 ?  112 ALA   B N    1 
ATOM   5921 C CA   . ALA   B 1 112 ? 35.334 -20.305 2.524   1.00 13.68 ?  112 ALA   B CA   1 
ATOM   5922 C C    . ALA   B 1 112 ? 35.306 -20.218 1.000   1.00 13.19 ?  112 ALA   B C    1 
ATOM   5923 O O    . ALA   B 1 112 ? 35.922 -19.324 0.405   1.00 13.55 ?  112 ALA   B O    1 
ATOM   5924 C CB   . ALA   B 1 112 ? 36.241 -21.437 3.013   1.00 14.03 ?  112 ALA   B CB   1 
ATOM   5925 H H    . ALA   B 1 112 ? 33.875 -21.194 3.529   1.00 16.65 ?  112 ALA   B H    1 
ATOM   5926 H HA   . ALA   B 1 112 ? 35.697 -19.469 2.858   1.00 16.42 ?  112 ALA   B HA   1 
ATOM   5927 H HB1  . ALA   B 1 112 ? 37.132 -21.300 2.648   1.00 16.83 ?  112 ALA   B HB1  1 
ATOM   5928 H HB2  . ALA   B 1 112 ? 36.280 -21.412 3.984   1.00 16.83 ?  112 ALA   B HB2  1 
ATOM   5929 H HB3  . ALA   B 1 112 ? 35.884 -22.281 2.715   1.00 16.83 ?  112 ALA   B HB3  1 
ATOM   5930 N N    . TYR   B 1 113 ? 34.563 -21.121 0.348   1.00 13.08 ?  113 TYR   B N    1 
ATOM   5931 C CA   . TYR   B 1 113 ? 34.491 -21.082 -1.109  1.00 13.03 ?  113 TYR   B CA   1 
ATOM   5932 C C    . TYR   B 1 113 ? 33.777 -19.836 -1.630  1.00 12.41 ?  113 TYR   B C    1 
ATOM   5933 O O    . TYR   B 1 113 ? 34.053 -19.397 -2.753  1.00 12.65 ?  113 TYR   B O    1 
ATOM   5934 C CB   . TYR   B 1 113 ? 33.822 -22.344 -1.659  1.00 13.12 ?  113 TYR   B CB   1 
ATOM   5935 C CG   . TYR   B 1 113 ? 34.778 -23.494 -1.905  1.00 13.54 ?  113 TYR   B CG   1 
ATOM   5936 C CD1  . TYR   B 1 113 ? 35.772 -23.397 -2.867  1.00 14.10 ?  113 TYR   B CD1  1 
ATOM   5937 C CD2  . TYR   B 1 113 ? 34.680 -24.679 -1.184  1.00 13.62 ?  113 TYR   B CD2  1 
ATOM   5938 C CE1  . TYR   B 1 113 ? 36.656 -24.436 -3.096  1.00 14.08 ?  113 TYR   B CE1  1 
ATOM   5939 C CE2  . TYR   B 1 113 ? 35.555 -25.732 -1.409  1.00 13.92 ?  113 TYR   B CE2  1 
ATOM   5940 C CZ   . TYR   B 1 113 ? 36.537 -25.612 -2.372  1.00 13.93 ?  113 TYR   B CZ   1 
ATOM   5941 O OH   . TYR   B 1 113 ? 37.426 -26.628 -2.631  1.00 14.80 ?  113 TYR   B OH   1 
ATOM   5942 H H    . TYR   B 1 113 ? 34.095 -21.748 0.723   1.00 15.70 ?  113 TYR   B H    1 
ATOM   5943 H HA   . TYR   B 1 113 ? 35.390 -21.061 -1.446  1.00 15.64 ?  113 TYR   B HA   1 
ATOM   5944 H HB2  . TYR   B 1 113 ? 33.150 -22.651 -1.023  1.00 15.74 ?  113 TYR   B HB2  1 
ATOM   5945 H HB3  . TYR   B 1 113 ? 33.391 -22.128 -2.502  1.00 15.74 ?  113 TYR   B HB3  1 
ATOM   5946 H HD1  . TYR   B 1 113 ? 35.856 -22.607 -3.358  1.00 16.92 ?  113 TYR   B HD1  1 
ATOM   5947 H HD2  . TYR   B 1 113 ? 34.012 -24.765 -0.541  1.00 16.35 ?  113 TYR   B HD2  1 
ATOM   5948 H HE1  . TYR   B 1 113 ? 37.315 -24.345 -3.747  1.00 16.89 ?  113 TYR   B HE1  1 
ATOM   5949 H HE2  . TYR   B 1 113 ? 35.470 -26.520 -0.923  1.00 16.70 ?  113 TYR   B HE2  1 
ATOM   5950 H HH   . TYR   B 1 113 ? 37.253 -27.286 -2.139  1.00 17.76 ?  113 TYR   B HH   1 
ATOM   5951 N N    . GLU   B 1 114 ? 32.858 -19.260 -0.848  1.00 12.99 ?  114 GLU   B N    1 
ATOM   5952 C CA   . GLU   B 1 114 ? 32.174 -18.051 -1.298  1.00 12.79 ?  114 GLU   B CA   1 
ATOM   5953 C C    . GLU   B 1 114 ? 33.153 -16.928 -1.604  1.00 12.50 ?  114 GLU   B C    1 
ATOM   5954 O O    . GLU   B 1 114 ? 32.871 -16.077 -2.449  1.00 13.02 ?  114 GLU   B O    1 
ATOM   5955 C CB   . GLU   B 1 114 ? 31.131 -17.626 -0.262  1.00 13.23 ?  114 GLU   B CB   1 
ATOM   5956 C CG   . GLU   B 1 114 ? 29.871 -18.509 -0.365  1.00 13.31 ?  114 GLU   B CG   1 
ATOM   5957 C CD   . GLU   B 1 114 ? 28.862 -18.337 0.762   1.00 13.61 ?  114 GLU   B CD   1 
ATOM   5958 O OE1  . GLU   B 1 114 ? 29.165 -17.726 1.805   1.00 13.61 ?  114 GLU   B OE1  1 
ATOM   5959 O OE2  . GLU   B 1 114 ? 27.740 -18.878 0.605   1.00 14.76 -1 114 GLU   B OE2  1 
ATOM   5960 H H    . GLU   B 1 114 ? 32.606 -19.554 -0.075  1.00 15.59 ?  114 GLU   B H    1 
ATOM   5961 H HA   . GLU   B 1 114 ? 31.698 -18.250 -2.114  1.00 15.35 ?  114 GLU   B HA   1 
ATOM   5962 H HB2  . GLU   B 1 114 ? 31.503 -17.724 0.633   1.00 15.88 ?  114 GLU   B HB2  1 
ATOM   5963 H HB3  . GLU   B 1 114 ? 30.876 -16.704 -0.419  1.00 15.88 ?  114 GLU   B HB3  1 
ATOM   5964 H HG2  . GLU   B 1 114 ? 29.419 -18.299 -1.193  1.00 15.97 ?  114 GLU   B HG2  1 
ATOM   5965 H HG3  . GLU   B 1 114 ? 30.148 -19.436 -0.365  1.00 15.97 ?  114 GLU   B HG3  1 
ATOM   5966 N N    . ASN   B 1 115 ? 34.324 -16.921 -0.957  1.00 12.04 ?  115 ASN   B N    1 
ATOM   5967 C CA   . ASN   B 1 115 ? 35.311 -15.889 -1.260  1.00 11.62 ?  115 ASN   B CA   1 
ATOM   5968 C C    . ASN   B 1 115 ? 35.723 -15.912 -2.728  1.00 12.05 ?  115 ASN   B C    1 
ATOM   5969 O O    . ASN   B 1 115 ? 36.115 -14.877 -3.285  1.00 12.51 ?  115 ASN   B O    1 
ATOM   5970 C CB   . ASN   B 1 115 ? 36.553 -16.070 -0.373  1.00 13.04 ?  115 ASN   B CB   1 
ATOM   5971 C CG   . ASN   B 1 115 ? 36.285 -15.790 1.086   1.00 13.36 ?  115 ASN   B CG   1 
ATOM   5972 O OD1  . ASN   B 1 115 ? 36.268 -14.633 1.516   1.00 15.35 ?  115 ASN   B OD1  1 
ATOM   5973 N ND2  . ASN   B 1 115 ? 36.121 -16.848 1.873   1.00 13.47 ?  115 ASN   B ND2  1 
ATOM   5974 H H    . ASN   B 1 115 ? 34.565 -17.485 -0.347  1.00 14.45 ?  115 ASN   B H    1 
ATOM   5975 H HA   . ASN   B 1 115 ? 34.932 -15.018 -1.068  1.00 13.94 ?  115 ASN   B HA   1 
ATOM   5976 H HB2  . ASN   B 1 115 ? 36.869 -16.981 -0.453  1.00 15.65 ?  115 ASN   B HB2  1 
ATOM   5977 H HB3  . ASN   B 1 115 ? 37.240 -15.451 -0.664  1.00 15.65 ?  115 ASN   B HB3  1 
ATOM   5978 H HD21 . ASN   B 1 115 ? 35.972 -16.745 2.716   1.00 16.17 ?  115 ASN   B HD21 1 
ATOM   5979 H HD22 . ASN   B 1 115 ? 36.154 -17.644 1.542   1.00 16.17 ?  115 ASN   B HD22 1 
ATOM   5980 N N    . PHE   B 1 116 ? 35.702 -17.093 -3.359  1.00 11.97 ?  116 PHE   B N    1 
ATOM   5981 C CA   . PHE   B 1 116 ? 36.128 -17.188 -4.748  1.00 12.40 ?  116 PHE   B CA   1 
ATOM   5982 C C    . PHE   B 1 116 ? 35.230 -16.368 -5.663  1.00 11.82 ?  116 PHE   B C    1 
ATOM   5983 O O    . PHE   B 1 116 ? 35.668 -15.929 -6.731  1.00 12.53 ?  116 PHE   B O    1 
ATOM   5984 C CB   . PHE   B 1 116 ? 36.091 -18.640 -5.258  1.00 11.80 ?  116 PHE   B CB   1 
ATOM   5985 C CG   . PHE   B 1 116 ? 37.158 -19.587 -4.711  1.00 11.82 ?  116 PHE   B CG   1 
ATOM   5986 C CD1  . PHE   B 1 116 ? 37.807 -19.401 -3.504  1.00 12.40 ?  116 PHE   B CD1  1 
ATOM   5987 C CD2  . PHE   B 1 116 ? 37.466 -20.726 -5.447  1.00 11.92 ?  116 PHE   B CD2  1 
ATOM   5988 C CE1  . PHE   B 1 116 ? 38.733 -20.335 -3.050  1.00 12.56 ?  116 PHE   B CE1  1 
ATOM   5989 C CE2  . PHE   B 1 116 ? 38.403 -21.657 -5.004  1.00 12.11 ?  116 PHE   B CE2  1 
ATOM   5990 C CZ   . PHE   B 1 116 ? 39.025 -21.462 -3.806  1.00 12.38 ?  116 PHE   B CZ   1 
ATOM   5991 H H    . PHE   B 1 116 ? 35.442 -17.838 -3.009  1.00 14.37 ?  116 PHE   B H    1 
ATOM   5992 H HA   . PHE   B 1 116 ? 37.035 -16.863 -4.833  1.00 14.88 ?  116 PHE   B HA   1 
ATOM   5993 H HB2  . PHE   B 1 116 ? 35.221 -19.020 -5.032  1.00 14.16 ?  116 PHE   B HB2  1 
ATOM   5994 H HB3  . PHE   B 1 116 ? 36.182 -18.626 -6.226  1.00 14.16 ?  116 PHE   B HB3  1 
ATOM   5995 H HD1  . PHE   B 1 116 ? 37.605 -18.660 -2.984  1.00 14.87 ?  116 PHE   B HD1  1 
ATOM   5996 H HD2  . PHE   B 1 116 ? 37.031 -20.871 -6.261  1.00 14.30 ?  116 PHE   B HD2  1 
ATOM   5997 H HE1  . PHE   B 1 116 ? 39.173 -20.201 -2.240  1.00 15.07 ?  116 PHE   B HE1  1 
ATOM   5998 H HE2  . PHE   B 1 116 ? 38.594 -22.406 -5.522  1.00 14.53 ?  116 PHE   B HE2  1 
ATOM   5999 H HZ   . PHE   B 1 116 ? 39.665 -22.073 -3.512  1.00 14.86 ?  116 PHE   B HZ   1 
ATOM   6000 N N    . ASN   B 1 117 ? 33.960 -16.160 -5.277  1.00 12.52 ?  117 ASN   B N    1 
ATOM   6001 C CA   . ASN   B 1 117 ? 33.011 -15.457 -6.139  1.00 12.97 ?  117 ASN   B CA   1 
ATOM   6002 C C    . ASN   B 1 117 ? 33.324 -13.977 -6.297  1.00 13.14 ?  117 ASN   B C    1 
ATOM   6003 O O    . ASN   B 1 117 ? 32.737 -13.328 -7.161  1.00 14.42 ?  117 ASN   B O    1 
ATOM   6004 C CB   . ASN   B 1 117 ? 31.587 -15.677 -5.633  1.00 13.26 ?  117 ASN   B CB   1 
ATOM   6005 C CG   . ASN   B 1 117 ? 31.127 -17.081 -5.886  1.00 13.19 ?  117 ASN   B CG   1 
ATOM   6006 O OD1  . ASN   B 1 117 ? 31.473 -17.670 -6.913  1.00 14.01 ?  117 ASN   B OD1  1 
ATOM   6007 N ND2  . ASN   B 1 117 ? 30.397 -17.655 -4.941  1.00 13.25 ?  117 ASN   B ND2  1 
ATOM   6008 H H    . ASN   B 1 117 ? 33.636 -16.422 -4.518  1.00 15.03 ?  117 ASN   B H    1 
ATOM   6009 H HA   . ASN   B 1 117 ? 33.063 -15.858 -7.016  1.00 15.57 ?  117 ASN   B HA   1 
ATOM   6010 H HB2  . ASN   B 1 117 ? 31.552 -15.515 -4.676  1.00 15.91 ?  117 ASN   B HB2  1 
ATOM   6011 H HB3  . ASN   B 1 117 ? 30.987 -15.071 -6.097  1.00 15.91 ?  117 ASN   B HB3  1 
ATOM   6012 H HD21 . ASN   B 1 117 ? 30.110 -18.461 -5.046  1.00 15.91 ?  117 ASN   B HD21 1 
ATOM   6013 H HD22 . ASN   B 1 117 ? 30.184 -17.215 -4.232  1.00 15.91 ?  117 ASN   B HD22 1 
ATOM   6014 N N    . GLN   B 1 118 ? 34.252 -13.446 -5.523  1.00 12.57 ?  118 GLN   B N    1 
ATOM   6015 C CA   . GLN   B 1 118 ? 34.684 -12.063 -5.663  1.00 13.90 ?  118 GLN   B CA   1 
ATOM   6016 C C    . GLN   B 1 118 ? 35.758 -11.880 -6.730  1.00 14.06 ?  118 GLN   B C    1 
ATOM   6017 O O    . GLN   B 1 118 ? 36.240 -10.758 -6.902  1.00 15.18 ?  118 GLN   B O    1 
ATOM   6018 C CB   . GLN   B 1 118 ? 35.161 -11.535 -4.307  1.00 14.30 ?  118 GLN   B CB   1 
ATOM   6019 C CG   . GLN   B 1 118 ? 34.079 -11.569 -3.233  1.00 14.54 ?  118 GLN   B CG   1 
ATOM   6020 C CD   . GLN   B 1 118 ? 32.908 -10.667 -3.572  1.00 14.18 ?  118 GLN   B CD   1 
ATOM   6021 O OE1  . GLN   B 1 118 ? 33.100 -9.529  -4.012  1.00 15.07 ?  118 GLN   B OE1  1 
ATOM   6022 N NE2  . GLN   B 1 118 ? 31.691 -11.161 -3.372  1.00 14.45 ?  118 GLN   B NE2  1 
ATOM   6023 H H    . GLN   B 1 118 ? 34.676 -13.870 -4.902  1.00 15.08 ?  118 GLN   B H    1 
ATOM   6024 H HA   . GLN   B 1 118 ? 33.924 -11.531 -5.937  1.00 16.68 ?  118 GLN   B HA   1 
ATOM   6025 H HB2  . GLN   B 1 118 ? 35.907 -12.067 -4.001  1.00 17.16 ?  118 GLN   B HB2  1 
ATOM   6026 H HB3  . GLN   B 1 118 ? 35.439 -10.606 -4.410  1.00 17.16 ?  118 GLN   B HB3  1 
ATOM   6027 H HG2  . GLN   B 1 118 ? 33.753 -12.482 -3.147  1.00 17.45 ?  118 GLN   B HG2  1 
ATOM   6028 H HG3  . GLN   B 1 118 ? 34.460 -11.274 -2.391  1.00 17.45 ?  118 GLN   B HG3  1 
ATOM   6029 H HE21 . GLN   B 1 118 ? 31.599 -11.963 -3.057  1.00 17.34 ?  118 GLN   B HE21 1 
ATOM   6030 H HE22 . GLN   B 1 118 ? 31.003 -10.689 -3.548  1.00 17.34 ?  118 GLN   B HE22 1 
ATOM   6031 N N    . HIS   B 1 119 ? 36.119 -12.936 -7.464  1.00 13.14 ?  119 HIS   B N    1 
ATOM   6032 C CA   . HIS   B 1 119 ? 37.162 -12.884 -8.481  1.00 13.34 ?  119 HIS   B CA   1 
ATOM   6033 C C    . HIS   B 1 119 ? 36.676 -13.615 -9.718  1.00 13.31 ?  119 HIS   B C    1 
ATOM   6034 O O    . HIS   B 1 119 ? 36.161 -14.728 -9.613  1.00 13.89 ?  119 HIS   B O    1 
ATOM   6035 C CB   . HIS   B 1 119 ? 38.438 -13.525 -7.930  1.00 13.26 ?  119 HIS   B CB   1 
ATOM   6036 C CG   . HIS   B 1 119 ? 38.910 -12.844 -6.693  1.00 14.56 ?  119 HIS   B CG   1 
ATOM   6037 N ND1  . HIS   B 1 119 ? 39.716 -11.726 -6.731  1.00 16.07 ?  119 HIS   B ND1  1 
ATOM   6038 C CD2  . HIS   B 1 119 ? 38.603 -13.048 -5.391  1.00 15.67 ?  119 HIS   B CD2  1 
ATOM   6039 C CE1  . HIS   B 1 119 ? 39.918 -11.298 -5.499  1.00 17.33 ?  119 HIS   B CE1  1 
ATOM   6040 N NE2  . HIS   B 1 119 ? 39.241 -12.070 -4.668  1.00 17.47 ?  119 HIS   B NE2  1 
ATOM   6041 H H    . HIS   B 1 119 ? 35.759 -13.714 -7.392  1.00 15.76 ?  119 HIS   B H    1 
ATOM   6042 H HA   . HIS   B 1 119 ? 37.353 -11.957 -8.716  1.00 16.01 ?  119 HIS   B HA   1 
ATOM   6043 H HB2  . HIS   B 1 119 ? 38.260 -14.454 -7.721  1.00 15.92 ?  119 HIS   B HB2  1 
ATOM   6044 H HB3  . HIS   B 1 119 ? 39.140 -13.463 -8.601  1.00 15.92 ?  119 HIS   B HB3  1 
ATOM   6045 H HD2  . HIS   B 1 119 ? 38.057 -13.721 -5.053  1.00 18.80 ?  119 HIS   B HD2  1 
ATOM   6046 H HE1  . HIS   B 1 119 ? 40.454 -10.579 -5.253  1.00 20.80 ?  119 HIS   B HE1  1 
ATOM   6047 H HE2  . HIS   B 1 119 ? 39.240 -12.003 -3.810  1.00 20.96 ?  119 HIS   B HE2  1 
ATOM   6048 N N    A GLU   B 1 120 ? 36.837 -12.999 -10.888 0.80 13.87 ?  120 GLU   B N    1 
ATOM   6049 N N    B GLU   B 1 120 ? 36.851 -12.998 -10.889 0.20 15.13 ?  120 GLU   B N    1 
ATOM   6050 C CA   A GLU   B 1 120 ? 36.260 -13.579 -12.093 0.80 15.29 ?  120 GLU   B CA   1 
ATOM   6051 C CA   B GLU   B 1 120 ? 36.278 -13.562 -12.107 0.20 17.02 ?  120 GLU   B CA   1 
ATOM   6052 C C    A GLU   B 1 120 ? 36.936 -14.885 -12.494 0.80 14.14 ?  120 GLU   B C    1 
ATOM   6053 C C    B GLU   B 1 120 ? 36.945 -14.872 -12.510 0.20 15.35 ?  120 GLU   B C    1 
ATOM   6054 O O    A GLU   B 1 120 ? 36.273 -15.761 -13.061 0.80 14.52 ?  120 GLU   B O    1 
ATOM   6055 O O    B GLU   B 1 120 ? 36.285 -15.745 -13.085 0.20 15.41 ?  120 GLU   B O    1 
ATOM   6056 C CB   A GLU   B 1 120 ? 36.282 -12.568 -13.236 0.80 20.42 ?  120 GLU   B CB   1 
ATOM   6057 C CB   B GLU   B 1 120 ? 36.343 -12.541 -13.243 0.20 21.05 ?  120 GLU   B CB   1 
ATOM   6058 C CG   A GLU   B 1 120 ? 35.285 -11.432 -13.051 0.80 27.08 ?  120 GLU   B CG   1 
ATOM   6059 C CG   B GLU   B 1 120 ? 35.438 -11.333 -13.034 0.20 25.10 ?  120 GLU   B CG   1 
ATOM   6060 C CD   A GLU   B 1 120 ? 35.191 -10.527 -14.262 0.80 32.77 ?  120 GLU   B CD   1 
ATOM   6061 C CD   B GLU   B 1 120 ? 35.382 -10.431 -14.252 0.20 28.50 ?  120 GLU   B CD   1 
ATOM   6062 O OE1  A GLU   B 1 120 ? 36.206 -10.373 -14.977 0.80 34.86 ?  120 GLU   B OE1  1 
ATOM   6063 O OE1  B GLU   B 1 120 ? 36.304 -10.504 -15.092 0.20 29.70 ?  120 GLU   B OE1  1 
ATOM   6064 O OE2  A GLU   B 1 120 ? 34.099 -9.972  -14.500 0.80 35.37 -1 120 GLU   B OE2  1 
ATOM   6065 O OE2  B GLU   B 1 120 ? 34.417 -9.646  -14.370 0.20 29.71 -1 120 GLU   B OE2  1 
ATOM   6066 H H    A GLU   B 1 120 ? 37.270 -12.262 -11.009 0.80 16.64 ?  120 GLU   B H    1 
ATOM   6067 H H    B GLU   B 1 120 ? 37.291 -12.267 -11.001 0.20 18.15 ?  120 GLU   B H    1 
ATOM   6068 H HA   A GLU   B 1 120 ? 35.337 -13.788 -11.911 0.80 18.34 ?  120 GLU   B HA   1 
ATOM   6069 H HA   B GLU   B 1 120 ? 35.347 -13.757 -11.943 0.20 20.42 ?  120 GLU   B HA   1 
ATOM   6070 H HB2  A GLU   B 1 120 ? 37.165 -12.175 -13.299 0.80 24.50 ?  120 GLU   B HB2  1 
ATOM   6071 H HB2  B GLU   B 1 120 ? 37.253 -12.217 -13.325 0.20 25.26 ?  120 GLU   B HB2  1 
ATOM   6072 H HB3  A GLU   B 1 120 ? 36.061 -13.022 -14.063 0.80 24.50 ?  120 GLU   B HB3  1 
ATOM   6073 H HB3  B GLU   B 1 120 ? 36.072 -12.974 -14.068 0.20 25.26 ?  120 GLU   B HB3  1 
ATOM   6074 H HG2  A GLU   B 1 120 ? 34.401 -11.806 -12.891 0.80 32.50 ?  120 GLU   B HG2  1 
ATOM   6075 H HG2  B GLU   B 1 120 ? 34.539 -11.642 -12.831 0.20 30.13 ?  120 GLU   B HG2  1 
ATOM   6076 H HG3  A GLU   B 1 120 ? 35.554 -10.889 -12.294 0.80 32.50 ?  120 GLU   B HG3  1 
ATOM   6077 H HG3  B GLU   B 1 120 ? 35.779 -10.804 -12.297 0.20 30.13 ?  120 GLU   B HG3  1 
ATOM   6078 N N    . VAL   B 1 121 ? 38.237 -15.028 -12.230 1.00 13.87 ?  121 VAL   B N    1 
ATOM   6079 C CA   . VAL   B 1 121 ? 38.978 -16.240 -12.578 1.00 13.09 ?  121 VAL   B CA   1 
ATOM   6080 C C    . VAL   B 1 121 ? 40.091 -16.449 -11.560 1.00 12.85 ?  121 VAL   B C    1 
ATOM   6081 O O    . VAL   B 1 121 ? 40.765 -15.494 -11.160 1.00 13.48 ?  121 VAL   B O    1 
ATOM   6082 C CB   . VAL   B 1 121 ? 39.491 -16.197 -14.036 1.00 15.50 ?  121 VAL   B CB   1 
ATOM   6083 C CG1  . VAL   B 1 121 ? 40.353 -14.962 -14.281 1.00 17.54 ?  121 VAL   B CG1  1 
ATOM   6084 C CG2  . VAL   B 1 121 ? 40.240 -17.479 -14.398 1.00 17.11 ?  121 VAL   B CG2  1 
ATOM   6085 H H    A VAL   B 1 121 ? 38.726 -14.428 -11.850 0.80 16.65 ?  121 VAL   B H    1 
ATOM   6086 H H    B VAL   B 1 121 ? 38.724 -14.434 -11.839 0.20 16.65 ?  121 VAL   B H    1 
ATOM   6087 H HA   . VAL   B 1 121 ? 38.367 -16.993 -12.512 1.00 15.70 ?  121 VAL   B HA   1 
ATOM   6088 H HB   . VAL   B 1 121 ? 38.723 -16.135 -14.630 1.00 18.60 ?  121 VAL   B HB   1 
ATOM   6089 H HG11 . VAL   B 1 121 ? 40.672 -14.975 -15.198 1.00 21.05 ?  121 VAL   B HG11 1 
ATOM   6090 H HG12 . VAL   B 1 121 ? 39.818 -14.166 -14.131 1.00 21.05 ?  121 VAL   B HG12 1 
ATOM   6091 H HG13 . VAL   B 1 121 ? 41.106 -14.976 -13.670 1.00 21.05 ?  121 VAL   B HG13 1 
ATOM   6092 H HG21 . VAL   B 1 121 ? 40.448 -17.466 -15.347 1.00 20.53 ?  121 VAL   B HG21 1 
ATOM   6093 H HG22 . VAL   B 1 121 ? 41.059 -17.525 -13.883 1.00 20.53 ?  121 VAL   B HG22 1 
ATOM   6094 H HG23 . VAL   B 1 121 ? 39.677 -18.243 -14.196 1.00 20.53 ?  121 VAL   B HG23 1 
ATOM   6095 N N    . LEU   B 1 122 ? 40.261 -17.703 -11.122 1.00 12.37 ?  122 LEU   B N    1 
ATOM   6096 C CA   . LEU   B 1 122 ? 41.238 -18.068 -10.098 1.00 11.86 ?  122 LEU   B CA   1 
ATOM   6097 C C    . LEU   B 1 122 ? 41.890 -19.399 -10.429 1.00 11.91 ?  122 LEU   B C    1 
ATOM   6098 O O    . LEU   B 1 122 ? 41.230 -20.314 -10.935 1.00 12.92 ?  122 LEU   B O    1 
ATOM   6099 C CB   . LEU   B 1 122 ? 40.584 -18.295 -8.720  1.00 14.15 ?  122 LEU   B CB   1 
ATOM   6100 C CG   . LEU   B 1 122 ? 39.553 -17.269 -8.251  1.00 14.45 ?  122 LEU   B CG   1 
ATOM   6101 C CD1  . LEU   B 1 122 ? 38.160 -17.642 -8.729  1.00 14.58 ?  122 LEU   B CD1  1 
ATOM   6102 C CD2  . LEU   B 1 122 ? 39.587 -17.136 -6.746  1.00 13.99 ?  122 LEU   B CD2  1 
ATOM   6103 H H    . LEU   B 1 122 ? 39.809 -18.379 -11.406 1.00 14.84 ?  122 LEU   B H    1 
ATOM   6104 H HA   . LEU   B 1 122 ? 41.918 -17.382 -10.013 1.00 14.23 ?  122 LEU   B HA   1 
ATOM   6105 H HB2  . LEU   B 1 122 ? 40.135 -19.155 -8.734  1.00 16.98 ?  122 LEU   B HB2  1 
ATOM   6106 H HB3  . LEU   B 1 122 ? 41.283 -18.313 -8.048  1.00 16.98 ?  122 LEU   B HB3  1 
ATOM   6107 H HG   . LEU   B 1 122 ? 39.776 -16.404 -8.630  1.00 17.35 ?  122 LEU   B HG   1 
ATOM   6108 H HD11 . LEU   B 1 122 ? 37.524 -16.996 -8.381  1.00 17.50 ?  122 LEU   B HD11 1 
ATOM   6109 H HD12 . LEU   B 1 122 ? 38.144 -17.623 -9.701  1.00 17.50 ?  122 LEU   B HD12 1 
ATOM   6110 H HD13 . LEU   B 1 122 ? 37.941 -18.528 -8.411  1.00 17.50 ?  122 LEU   B HD13 1 
ATOM   6111 H HD21 . LEU   B 1 122 ? 38.903 -16.503 -6.469  1.00 16.79 ?  122 LEU   B HD21 1 
ATOM   6112 H HD22 . LEU   B 1 122 ? 39.416 -18.002 -6.347  1.00 16.79 ?  122 LEU   B HD22 1 
ATOM   6113 H HD23 . LEU   B 1 122 ? 40.461 -16.813 -6.477  1.00 16.79 ?  122 LEU   B HD23 1 
ATOM   6114 N N    . LEU   B 1 123 ? 43.176 -19.510 -10.075 1.00 11.60 ?  123 LEU   B N    1 
ATOM   6115 C CA   . LEU   B 1 123 ? 43.888 -20.775 -9.956  1.00 12.09 ?  123 LEU   B CA   1 
ATOM   6116 C C    . LEU   B 1 123 ? 43.858 -21.162 -8.483  1.00 11.52 ?  123 LEU   B C    1 
ATOM   6117 O O    . LEU   B 1 123 ? 44.209 -20.343 -7.629  1.00 11.82 ?  123 LEU   B O    1 
ATOM   6118 C CB   . LEU   B 1 123 ? 45.340 -20.588 -10.405 1.00 12.69 ?  123 LEU   B CB   1 
ATOM   6119 C CG   . LEU   B 1 123 ? 46.279 -21.773 -10.165 1.00 12.91 ?  123 LEU   B CG   1 
ATOM   6120 C CD1  . LEU   B 1 123 ? 45.852 -23.031 -10.929 1.00 13.85 ?  123 LEU   B CD1  1 
ATOM   6121 C CD2  . LEU   B 1 123 ? 47.691 -21.379 -10.549 1.00 13.82 ?  123 LEU   B CD2  1 
ATOM   6122 H H    . LEU   B 1 123 ? 43.672 -18.832 -9.877  1.00 13.92 ?  123 LEU   B H    1 
ATOM   6123 H HA   . LEU   B 1 123 ? 43.455 -21.464 -10.483 1.00 14.50 ?  123 LEU   B HA   1 
ATOM   6124 H HB2  . LEU   B 1 123 ? 45.335 -20.406 -11.355 1.00 15.23 ?  123 LEU   B HB2  1 
ATOM   6125 H HB3  . LEU   B 1 123 ? 45.705 -19.826 -9.929  1.00 15.23 ?  123 LEU   B HB3  1 
ATOM   6126 H HG   . LEU   B 1 123 ? 46.280 -21.987 -9.219  1.00 15.49 ?  123 LEU   B HG   1 
ATOM   6127 H HD11 . LEU   B 1 123 ? 46.491 -23.738 -10.750 1.00 16.62 ?  123 LEU   B HD11 1 
ATOM   6128 H HD12 . LEU   B 1 123 ? 44.969 -23.300 -10.628 1.00 16.62 ?  123 LEU   B HD12 1 
ATOM   6129 H HD13 . LEU   B 1 123 ? 45.832 -22.833 -11.877 1.00 16.62 ?  123 LEU   B HD13 1 
ATOM   6130 H HD21 . LEU   B 1 123 ? 48.279 -22.133 -10.395 1.00 16.59 ?  123 LEU   B HD21 1 
ATOM   6131 H HD22 . LEU   B 1 123 ? 47.705 -21.130 -11.486 1.00 16.59 ?  123 LEU   B HD22 1 
ATOM   6132 H HD23 . LEU   B 1 123 ? 47.967 -20.626 -10.002 1.00 16.59 ?  123 LEU   B HD23 1 
ATOM   6133 N N    . ALA   B 1 124 ? 43.421 -22.391 -8.174  1.00 11.47 ?  124 ALA   B N    1 
ATOM   6134 C CA   . ALA   B 1 124 ? 43.165 -22.716 -6.776  1.00 11.56 ?  124 ALA   B CA   1 
ATOM   6135 C C    . ALA   B 1 124 ? 43.437 -24.177 -6.439  1.00 10.71 ?  124 ALA   B C    1 
ATOM   6136 O O    . ALA   B 1 124 ? 43.307 -25.056 -7.303  1.00 12.01 ?  124 ALA   B O    1 
ATOM   6137 C CB   . ALA   B 1 124 ? 41.712 -22.390 -6.398  1.00 12.15 ?  124 ALA   B CB   1 
ATOM   6138 H H    . ALA   B 1 124 ? 43.261 -23.030 -8.734  1.00 13.76 ?  124 ALA   B H    1 
ATOM   6139 H HA   . ALA   B 1 124 ? 43.741 -22.163 -6.230  1.00 13.87 ?  124 ALA   B HA   1 
ATOM   6140 H HB1  . ALA   B 1 124 ? 41.564 -22.611 -5.466  1.00 14.58 ?  124 ALA   B HB1  1 
ATOM   6141 H HB2  . ALA   B 1 124 ? 41.552 -21.441 -6.542  1.00 14.58 ?  124 ALA   B HB2  1 
ATOM   6142 H HB3  . ALA   B 1 124 ? 41.113 -22.910 -6.960  1.00 14.58 ?  124 ALA   B HB3  1 
ATOM   6143 N N    . PRO   B 1 125 ? 43.741 -24.464 -5.178  1.00 11.21 ?  125 PRO   B N    1 
ATOM   6144 C CA   . PRO   B 1 125 ? 43.677 -25.832 -4.655  1.00 12.29 ?  125 PRO   B CA   1 
ATOM   6145 C C    . PRO   B 1 125 ? 42.275 -26.101 -4.109  1.00 12.82 ?  125 PRO   B C    1 
ATOM   6146 O O    . PRO   B 1 125 ? 41.487 -25.184 -3.900  1.00 13.07 ?  125 PRO   B O    1 
ATOM   6147 C CB   . PRO   B 1 125 ? 44.666 -25.761 -3.482  1.00 13.24 ?  125 PRO   B CB   1 
ATOM   6148 C CG   . PRO   B 1 125 ? 44.427 -24.356 -2.924  1.00 13.04 ?  125 PRO   B CG   1 
ATOM   6149 C CD   . PRO   B 1 125 ? 44.076 -23.495 -4.123  1.00 12.12 ?  125 PRO   B CD   1 
ATOM   6150 H HA   . PRO   B 1 125 ? 43.951 -26.505 -5.303  1.00 14.74 ?  125 PRO   B HA   1 
ATOM   6151 H HB2  . PRO   B 1 125 ? 44.450 -26.438 -2.819  1.00 15.89 ?  125 PRO   B HB2  1 
ATOM   6152 H HB3  . PRO   B 1 125 ? 45.575 -25.859 -3.798  1.00 15.89 ?  125 PRO   B HB3  1 
ATOM   6153 H HG2  . PRO   B 1 125 ? 43.686 -24.372 -2.294  1.00 15.65 ?  125 PRO   B HG2  1 
ATOM   6154 H HG3  . PRO   B 1 125 ? 45.233 -24.032 -2.489  1.00 15.65 ?  125 PRO   B HG3  1 
ATOM   6155 H HD2  . PRO   B 1 125 ? 43.315 -22.931 -3.934  1.00 14.54 ?  125 PRO   B HD2  1 
ATOM   6156 H HD3  . PRO   B 1 125 ? 44.852 -22.959 -4.389  1.00 14.54 ?  125 PRO   B HD3  1 
ATOM   6157 N N    . LEU   B 1 126 ? 42.012 -27.375 -3.799  1.00 13.24 ?  126 LEU   B N    1 
ATOM   6158 C CA   . LEU   B 1 126 ? 40.795 -27.735 -3.073  1.00 13.84 ?  126 LEU   B CA   1 
ATOM   6159 C C    . LEU   B 1 126 ? 40.918 -27.330 -1.610  1.00 13.64 ?  126 LEU   B C    1 
ATOM   6160 O O    . LEU   B 1 126 ? 41.798 -27.812 -0.894  1.00 15.75 ?  126 LEU   B O    1 
ATOM   6161 C CB   . LEU   B 1 126 ? 40.539 -29.235 -3.170  1.00 14.96 ?  126 LEU   B CB   1 
ATOM   6162 C CG   . LEU   B 1 126 ? 40.002 -29.724 -4.515  1.00 16.66 ?  126 LEU   B CG   1 
ATOM   6163 C CD1  . LEU   B 1 126 ? 40.039 -31.236 -4.582  1.00 18.97 ?  126 LEU   B CD1  1 
ATOM   6164 C CD2  . LEU   B 1 126 ? 38.587 -29.226 -4.772  1.00 16.96 ?  126 LEU   B CD2  1 
ATOM   6165 H H    . LEU   B 1 126 ? 42.524 -28.043 -3.984  1.00 15.89 ?  126 LEU   B H    1 
ATOM   6166 H HA   . LEU   B 1 126 ? 40.041 -27.267 -3.457  1.00 16.60 ?  126 LEU   B HA   1 
ATOM   6167 H HB2  . LEU   B 1 126 ? 41.370 -29.701 -3.000  1.00 17.96 ?  126 LEU   B HB2  1 
ATOM   6168 H HB3  . LEU   B 1 126 ? 39.886 -29.479 -2.492  1.00 17.96 ?  126 LEU   B HB3  1 
ATOM   6169 H HG   . LEU   B 1 126 ? 40.573 -29.372 -5.220  1.00 20.00 ?  126 LEU   B HG   1 
ATOM   6170 H HD11 . LEU   B 1 126 ? 39.697 -31.517 -5.445  1.00 22.76 ?  126 LEU   B HD11 1 
ATOM   6171 H HD12 . LEU   B 1 126 ? 40.953 -31.533 -4.471  1.00 22.76 ?  126 LEU   B HD12 1 
ATOM   6172 H HD13 . LEU   B 1 126 ? 39.482 -31.592 -3.872  1.00 22.76 ?  126 LEU   B HD13 1 
ATOM   6173 H HD21 . LEU   B 1 126 ? 38.249 -29.642 -5.582  1.00 20.35 ?  126 LEU   B HD21 1 
ATOM   6174 H HD22 . LEU   B 1 126 ? 38.025 -29.471 -4.018  1.00 20.35 ?  126 LEU   B HD22 1 
ATOM   6175 H HD23 . LEU   B 1 126 ? 38.595 -28.262 -4.876  1.00 20.35 ?  126 LEU   B HD23 1 
ATOM   6176 N N    . LEU   B 1 127 ? 39.994 -26.498 -1.146  1.00 13.46 ?  127 LEU   B N    1 
ATOM   6177 C CA   . LEU   B 1 127 ? 40.055 -26.005 0.216   1.00 13.78 ?  127 LEU   B CA   1 
ATOM   6178 C C    . LEU   B 1 127 ? 39.764 -27.121 1.212   1.00 13.88 ?  127 LEU   B C    1 
ATOM   6179 O O    . LEU   B 1 127 ? 38.938 -28.010 0.982   1.00 14.45 ?  127 LEU   B O    1 
ATOM   6180 C CB   . LEU   B 1 127 ? 39.038 -24.883 0.422   1.00 14.93 ?  127 LEU   B CB   1 
ATOM   6181 C CG   . LEU   B 1 127 ? 39.212 -23.615 -0.418  1.00 15.14 ?  127 LEU   B CG   1 
ATOM   6182 C CD1  . LEU   B 1 127 ? 38.086 -22.643 -0.111  1.00 15.77 ?  127 LEU   B CD1  1 
ATOM   6183 C CD2  . LEU   B 1 127 ? 40.566 -22.957 -0.178  1.00 16.33 ?  127 LEU   B CD2  1 
ATOM   6184 H H    . LEU   B 1 127 ? 39.331 -26.188 -1.605  1.00 16.15 ?  127 LEU   B H    1 
ATOM   6185 H HA   . LEU   B 1 127 ? 40.943 -25.644 0.391   1.00 16.54 ?  127 LEU   B HA   1 
ATOM   6186 H HB2  . LEU   B 1 127 ? 38.157 -25.238 0.223   1.00 17.91 ?  127 LEU   B HB2  1 
ATOM   6187 H HB3  . LEU   B 1 127 ? 39.070 -24.616 1.355   1.00 17.91 ?  127 LEU   B HB3  1 
ATOM   6188 H HG   . LEU   B 1 127 ? 39.147 -23.840 -1.354  1.00 18.17 ?  127 LEU   B HG   1 
ATOM   6189 H HD11 . LEU   B 1 127 ? 38.202 -21.835 -0.643  1.00 18.92 ?  127 LEU   B HD11 1 
ATOM   6190 H HD12 . LEU   B 1 127 ? 37.234 -23.055 -0.331  1.00 18.92 ?  127 LEU   B HD12 1 
ATOM   6191 H HD13 . LEU   B 1 127 ? 38.103 -22.413 0.834   1.00 18.92 ?  127 LEU   B HD13 1 
ATOM   6192 H HD21 . LEU   B 1 127 ? 40.601 -22.112 -0.658  1.00 19.60 ?  127 LEU   B HD21 1 
ATOM   6193 H HD22 . LEU   B 1 127 ? 40.680 -22.795 0.773   1.00 19.60 ?  127 LEU   B HD22 1 
ATOM   6194 H HD23 . LEU   B 1 127 ? 41.263 -23.547 -0.499  1.00 19.60 ?  127 LEU   B HD23 1 
ATOM   6195 N N    . SER   B 1 128 ? 40.449 -27.040 2.345   1.00 14.04 ?  128 SER   B N    1 
ATOM   6196 C CA   . SER   B 1 128 ? 40.312 -27.944 3.474   1.00 14.67 ?  128 SER   B CA   1 
ATOM   6197 C C    . SER   B 1 128 ? 40.804 -29.356 3.175   1.00 16.26 ?  128 SER   B C    1 
ATOM   6198 O O    . SER   B 1 128 ? 40.684 -30.222 4.033   1.00 18.12 ?  128 SER   B O    1 
ATOM   6199 C CB   . SER   B 1 128 ? 38.893 -27.941 4.065   1.00 14.82 ?  128 SER   B CB   1 
ATOM   6200 O OG   . SER   B 1 128 ? 38.603 -26.661 4.636   1.00 15.35 ?  128 SER   B OG   1 
ATOM   6201 H H    . SER   B 1 128 ? 41.035 -26.424 2.489   1.00 16.85 ?  128 SER   B H    1 
ATOM   6202 H HA   . SER   B 1 128 ? 40.881 -27.604 4.170   1.00 17.61 ?  128 SER   B HA   1 
ATOM   6203 H HB2  . SER   B 1 128 ? 38.244 -28.136 3.364   1.00 17.78 ?  128 SER   B HB2  1 
ATOM   6204 H HB3  . SER   B 1 128 ? 38.834 -28.625 4.759   1.00 17.78 ?  128 SER   B HB3  1 
ATOM   6205 H HG   . SER   B 1 128 ? 39.162 -26.495 5.239   1.00 18.41 ?  128 SER   B HG   1 
ATOM   6206 N N    . ALA   B 1 129 ? 41.392 -29.595 2.002   1.00 17.79 ?  129 ALA   B N    1 
ATOM   6207 C CA   . ALA   B 1 129 ? 41.929 -30.899 1.652   1.00 18.43 ?  129 ALA   B CA   1 
ATOM   6208 C C    . ALA   B 1 129 ? 43.325 -31.072 2.231   1.00 17.37 ?  129 ALA   B C    1 
ATOM   6209 O O    . ALA   B 1 129 ? 43.871 -30.182 2.892   1.00 17.02 ?  129 ALA   B O    1 
ATOM   6210 C CB   . ALA   B 1 129 ? 41.973 -31.064 0.136   1.00 20.38 ?  129 ALA   B CB   1 
ATOM   6211 H H    . ALA   B 1 129 ? 41.496 -29.003 1.383   1.00 21.35 ?  129 ALA   B H    1 
ATOM   6212 H HA   . ALA   B 1 129 ? 41.364 -31.590 2.019   1.00 22.12 ?  129 ALA   B HA   1 
ATOM   6213 H HB1  . ALA   B 1 129 ? 42.316 -31.946 -0.077  1.00 24.46 ?  129 ALA   B HB1  1 
ATOM   6214 H HB2  . ALA   B 1 129 ? 41.078 -30.961 -0.216  1.00 24.46 ?  129 ALA   B HB2  1 
ATOM   6215 H HB3  . ALA   B 1 129 ? 42.557 -30.384 -0.240  1.00 24.46 ?  129 ALA   B HB3  1 
ATOM   6216 N N    . GLY   B 1 130 ? 43.914 -32.234 1.952   1.00 17.33 ?  130 GLY   B N    1 
ATOM   6217 C CA   . GLY   B 1 130 ? 45.304 -32.464 2.305   1.00 17.80 ?  130 GLY   B CA   1 
ATOM   6218 C C    . GLY   B 1 130 ? 45.511 -32.370 3.797   1.00 17.80 ?  130 GLY   B C    1 
ATOM   6219 O O    . GLY   B 1 130 ? 44.801 -33.008 4.588   1.00 18.54 ?  130 GLY   B O    1 
ATOM   6220 H H    . GLY   B 1 130 ? 43.544 -32.892 1.545   1.00 20.79 ?  130 GLY   B H    1 
ATOM   6221 H HA2  . GLY   B 1 130 ? 45.578 -33.349 2.009   1.00 21.36 ?  130 GLY   B HA2  1 
ATOM   6222 H HA3  . GLY   B 1 130 ? 45.874 -31.808 1.873   1.00 21.36 ?  130 GLY   B HA3  1 
ATOM   6223 N N    . ILE   B 1 131 ? 46.495 -31.556 4.192   1.00 18.18 ?  131 ILE   B N    1 
ATOM   6224 C CA   . ILE   B 1 131 ? 46.862 -31.436 5.592   1.00 19.31 ?  131 ILE   B CA   1 
ATOM   6225 C C    . ILE   B 1 131 ? 45.749 -30.837 6.433   1.00 18.13 ?  131 ILE   B C    1 
ATOM   6226 O O    . ILE   B 1 131 ? 45.821 -30.906 7.661   1.00 20.20 ?  131 ILE   B O    1 
ATOM   6227 C CB   . ILE   B 1 131 ? 48.192 -30.661 5.781   1.00 21.27 ?  131 ILE   B CB   1 
ATOM   6228 C CG1  . ILE   B 1 131 ? 48.017 -29.169 5.454   1.00 22.27 ?  131 ILE   B CG1  1 
ATOM   6229 C CG2  . ILE   B 1 131 ? 49.299 -31.279 4.924   1.00 22.80 ?  131 ILE   B CG2  1 
ATOM   6230 C CD1  . ILE   B 1 131 ? 49.214 -28.301 5.811   1.00 23.13 ?  131 ILE   B CD1  1 
ATOM   6231 H H    . ILE   B 1 131 ? 46.965 -31.065 3.666   1.00 21.82 ?  131 ILE   B H    1 
ATOM   6232 H HA   . ILE   B 1 131 ? 47.012 -32.324 5.941   1.00 23.17 ?  131 ILE   B HA   1 
ATOM   6233 H HB   . ILE   B 1 131 ? 48.455 -30.736 6.713   1.00 25.52 ?  131 ILE   B HB   1 
ATOM   6234 H HG12 . ILE   B 1 131 ? 47.859 -29.081 4.503   1.00 26.73 ?  131 ILE   B HG12 1 
ATOM   6235 H HG13 . ILE   B 1 131 ? 47.255 -28.822 5.945   1.00 26.73 ?  131 ILE   B HG13 1 
ATOM   6236 H HG21 . ILE   B 1 131 ? 50.142 -30.870 5.161   1.00 27.36 ?  131 ILE   B HG21 1 
ATOM   6237 H HG22 . ILE   B 1 131 ? 49.327 -32.231 5.091   1.00 27.36 ?  131 ILE   B HG22 1 
ATOM   6238 H HG23 . ILE   B 1 131 ? 49.097 -31.110 3.989   1.00 27.36 ?  131 ILE   B HG23 1 
ATOM   6239 H HD11 . ILE   B 1 131 ? 48.992 -27.373 5.633   1.00 27.75 ?  131 ILE   B HD11 1 
ATOM   6240 H HD12 . ILE   B 1 131 ? 49.418 -28.416 6.753   1.00 27.75 ?  131 ILE   B HD12 1 
ATOM   6241 H HD13 . ILE   B 1 131 ? 49.972 -28.570 5.272   1.00 27.75 ?  131 ILE   B HD13 1 
ATOM   6242 N N    . PHE   B 1 132 ? 44.720 -30.249 5.806   1.00 17.09 ?  132 PHE   B N    1 
ATOM   6243 C CA   . PHE   B 1 132 ? 43.567 -29.738 6.541   1.00 17.86 ?  132 PHE   B CA   1 
ATOM   6244 C C    . PHE   B 1 132 ? 42.545 -30.819 6.896   1.00 19.53 ?  132 PHE   B C    1 
ATOM   6245 O O    . PHE   B 1 132 ? 41.667 -30.559 7.726   1.00 21.12 ?  132 PHE   B O    1 
ATOM   6246 C CB   . PHE   B 1 132 ? 42.877 -28.619 5.751   1.00 17.01 ?  132 PHE   B CB   1 
ATOM   6247 C CG   . PHE   B 1 132 ? 43.567 -27.274 5.846   1.00 16.61 ?  132 PHE   B CG   1 
ATOM   6248 C CD1  . PHE   B 1 132 ? 44.852 -27.095 5.365   1.00 17.77 ?  132 PHE   B CD1  1 
ATOM   6249 C CD2  . PHE   B 1 132 ? 42.898 -26.172 6.375   1.00 15.79 ?  132 PHE   B CD2  1 
ATOM   6250 C CE1  . PHE   B 1 132 ? 45.475 -25.854 5.442   1.00 18.38 ?  132 PHE   B CE1  1 
ATOM   6251 C CE2  . PHE   B 1 132 ? 43.512 -24.928 6.447   1.00 16.87 ?  132 PHE   B CE2  1 
ATOM   6252 C CZ   . PHE   B 1 132 ? 44.797 -24.775 5.982   1.00 18.17 ?  132 PHE   B CZ   1 
ATOM   6253 H H    . PHE   B 1 132 ? 44.673 -30.136 4.952   1.00 20.51 ?  132 PHE   B H    1 
ATOM   6254 H HA   . PHE   B 1 132 ? 43.883 -29.356 7.370   1.00 21.44 ?  132 PHE   B HA   1 
ATOM   6255 H HB2  . PHE   B 1 132 ? 42.854 -28.865 4.817   1.00 20.41 ?  132 PHE   B HB2  1 
ATOM   6256 H HB3  . PHE   B 1 132 ? 41.972 -28.511 6.088   1.00 20.41 ?  132 PHE   B HB3  1 
ATOM   6257 H HD1  . PHE   B 1 132 ? 45.313 -27.818 5.007   1.00 21.32 ?  132 PHE   B HD1  1 
ATOM   6258 H HD2  . PHE   B 1 132 ? 42.030 -26.271 6.698   1.00 18.95 ?  132 PHE   B HD2  1 
ATOM   6259 H HE1  . PHE   B 1 132 ? 46.344 -25.748 5.129   1.00 22.05 ?  132 PHE   B HE1  1 
ATOM   6260 H HE2  . PHE   B 1 132 ? 43.059 -24.200 6.819   1.00 20.24 ?  132 PHE   B HE2  1 
ATOM   6261 H HZ   . PHE   B 1 132 ? 45.215 -23.940 6.037   1.00 21.80 ?  132 PHE   B HZ   1 
ATOM   6262 N N    . GLY   B 1 133 ? 42.616 -32.013 6.288   1.00 19.05 ?  133 GLY   B N    1 
ATOM   6263 C CA   . GLY   B 1 133 ? 41.900 -33.172 6.793   1.00 20.11 ?  133 GLY   B CA   1 
ATOM   6264 C C    . GLY   B 1 133 ? 40.505 -33.436 6.252   1.00 20.57 ?  133 GLY   B C    1 
ATOM   6265 O O    . GLY   B 1 133 ? 39.923 -34.461 6.610   1.00 22.30 ?  133 GLY   B O    1 
ATOM   6266 H H    . GLY   B 1 133 ? 43.086 -32.171 5.578   1.00 22.85 ?  133 GLY   B H    1 
ATOM   6267 H HA2  . GLY   B 1 133 ? 42.434 -33.961 6.618   1.00 24.13 ?  133 GLY   B HA2  1 
ATOM   6268 H HA3  . GLY   B 1 133 ? 41.818 -33.079 7.753   1.00 24.13 ?  133 GLY   B HA3  1 
ATOM   6269 N N    . ALA   B 1 134 ? 39.936 -32.562 5.428   1.00 19.71 ?  134 ALA   B N    1 
ATOM   6270 C CA   . ALA   B 1 134 ? 38.617 -32.853 4.884   1.00 19.78 ?  134 ALA   B CA   1 
ATOM   6271 C C    . ALA   B 1 134 ? 38.718 -33.838 3.723   1.00 19.60 ?  134 ALA   B C    1 
ATOM   6272 O O    . ALA   B 1 134 ? 39.777 -34.020 3.113   1.00 20.19 ?  134 ALA   B O    1 
ATOM   6273 C CB   . ALA   B 1 134 ? 37.932 -31.573 4.411   1.00 19.80 ?  134 ALA   B CB   1 
ATOM   6274 H H    . ALA   B 1 134 ? 40.277 -31.810 5.188   1.00 23.65 ?  134 ALA   B H    1 
ATOM   6275 H HA   . ALA   B 1 134 ? 38.068 -33.252 5.578   1.00 23.74 ?  134 ALA   B HA   1 
ATOM   6276 H HB1  . ALA   B 1 134 ? 37.045 -31.794 4.084   1.00 23.76 ?  134 ALA   B HB1  1 
ATOM   6277 H HB2  . ALA   B 1 134 ? 37.864 -30.955 5.156   1.00 23.76 ?  134 ALA   B HB2  1 
ATOM   6278 H HB3  . ALA   B 1 134 ? 38.457 -31.177 3.699   1.00 23.76 ?  134 ALA   B HB3  1 
ATOM   6279 N N    . ASP   B 1 135 ? 37.593 -34.476 3.426   1.00 20.05 ?  135 ASP   B N    1 
ATOM   6280 C CA   . ASP   B 1 135 ? 37.504 -35.358 2.275   1.00 21.06 ?  135 ASP   B CA   1 
ATOM   6281 C C    . ASP   B 1 135 ? 37.597 -34.517 1.008   1.00 19.49 ?  135 ASP   B C    1 
ATOM   6282 O O    . ASP   B 1 135 ? 36.733 -33.655 0.783   1.00 19.18 ?  135 ASP   B O    1 
ATOM   6283 C CB   . ASP   B 1 135 ? 36.169 -36.099 2.323   1.00 23.14 ?  135 ASP   B CB   1 
ATOM   6284 C CG   . ASP   B 1 135 ? 36.006 -37.109 1.202   1.00 24.93 ?  135 ASP   B CG   1 
ATOM   6285 O OD1  . ASP   B 1 135 ? 36.865 -37.150 0.296   1.00 25.02 ?  135 ASP   B OD1  1 
ATOM   6286 O OD2  . ASP   B 1 135 ? 35.019 -37.881 1.243   1.00 28.07 -1 135 ASP   B OD2  1 
ATOM   6287 H H    . ASP   B 1 135 ? 36.864 -34.410 3.878   1.00 24.06 ?  135 ASP   B H    1 
ATOM   6288 H HA   . ASP   B 1 135 ? 38.227 -36.006 2.307   1.00 25.27 ?  135 ASP   B HA   1 
ATOM   6289 H HB2  . ASP   B 1 135 ? 36.107 -36.577 3.160   1.00 27.77 ?  135 ASP   B HB2  1 
ATOM   6290 H HB3  . ASP   B 1 135 ? 35.453 -35.454 2.246   1.00 27.77 ?  135 ASP   B HB3  1 
ATOM   6291 N N    . PRO   B 1 136 ? 38.609 -34.717 0.162   1.00 19.47 ?  136 PRO   B N    1 
ATOM   6292 C CA   . PRO   B 1 136 ? 38.694 -33.913 -1.068  1.00 18.22 ?  136 PRO   B CA   1 
ATOM   6293 C C    . PRO   B 1 136 ? 37.487 -34.075 -1.975  1.00 17.49 ?  136 PRO   B C    1 
ATOM   6294 O O    . PRO   B 1 136 ? 37.155 -33.142 -2.713  1.00 16.85 ?  136 PRO   B O    1 
ATOM   6295 C CB   . PRO   B 1 136 ? 39.995 -34.403 -1.724  1.00 19.09 ?  136 PRO   B CB   1 
ATOM   6296 C CG   . PRO   B 1 136 ? 40.197 -35.797 -1.162  1.00 20.93 ?  136 PRO   B CG   1 
ATOM   6297 C CD   . PRO   B 1 136 ? 39.686 -35.719 0.248   1.00 20.44 ?  136 PRO   B CD   1 
ATOM   6298 H HA   . PRO   B 1 136 ? 38.787 -32.976 -0.850  1.00 21.86 ?  136 PRO   B HA   1 
ATOM   6299 H HB2  . PRO   B 1 136 ? 39.893 -34.433 -2.689  1.00 22.91 ?  136 PRO   B HB2  1 
ATOM   6300 H HB3  . PRO   B 1 136 ? 40.727 -33.821 -1.472  1.00 22.91 ?  136 PRO   B HB3  1 
ATOM   6301 H HG2  . PRO   B 1 136 ? 39.681 -36.442 -1.673  1.00 25.11 ?  136 PRO   B HG2  1 
ATOM   6302 H HG3  . PRO   B 1 136 ? 41.139 -36.028 -1.170  1.00 25.11 ?  136 PRO   B HG3  1 
ATOM   6303 H HD2  . PRO   B 1 136 ? 39.333 -36.578 0.529   1.00 24.52 ?  136 PRO   B HD2  1 
ATOM   6304 H HD3  . PRO   B 1 136 ? 40.384 -35.409 0.849   1.00 24.52 ?  136 PRO   B HD3  1 
ATOM   6305 N N    . ILE   B 1 137 ? 36.821 -35.236 -1.945  1.00 17.91 ?  137 ILE   B N    1 
ATOM   6306 C CA   . ILE   B 1 137 ? 35.599 -35.419 -2.729  1.00 18.03 ?  137 ILE   B CA   1 
ATOM   6307 C C    . ILE   B 1 137 ? 34.524 -34.447 -2.262  1.00 17.28 ?  137 ILE   B C    1 
ATOM   6308 O O    . ILE   B 1 137 ? 33.819 -33.828 -3.073  1.00 16.87 ?  137 ILE   B O    1 
ATOM   6309 C CB   . ILE   B 1 137 ? 35.129 -36.891 -2.657  1.00 19.98 ?  137 ILE   B CB   1 
ATOM   6310 C CG1  . ILE   B 1 137 ? 36.138 -37.798 -3.361  1.00 22.39 ?  137 ILE   B CG1  1 
ATOM   6311 C CG2  . ILE   B 1 137 ? 33.728 -37.047 -3.257  1.00 20.65 ?  137 ILE   B CG2  1 
ATOM   6312 C CD1  . ILE   B 1 137 ? 35.832 -39.280 -3.243  1.00 24.84 ?  137 ILE   B CD1  1 
ATOM   6313 H H    . ILE   B 1 137 ? 37.053 -35.928 -1.487  1.00 21.49 ?  137 ILE   B H    1 
ATOM   6314 H HA   . ILE   B 1 137 ? 35.789 -35.218 -3.658  1.00 21.63 ?  137 ILE   B HA   1 
ATOM   6315 H HB   . ILE   B 1 137 ? 35.086 -37.149 -1.728  1.00 23.98 ?  137 ILE   B HB   1 
ATOM   6316 H HG12 . ILE   B 1 137 ? 36.159 -37.579 -4.305  1.00 26.87 ?  137 ILE   B HG12 1 
ATOM   6317 H HG13 . ILE   B 1 137 ? 37.016 -37.650 -2.972  1.00 26.87 ?  137 ILE   B HG13 1 
ATOM   6318 H HG21 . ILE   B 1 137 ? 33.465 -37.982 -3.230  1.00 24.77 ?  137 ILE   B HG21 1 
ATOM   6319 H HG22 . ILE   B 1 137 ? 33.093 -36.530 -2.738  1.00 24.77 ?  137 ILE   B HG22 1 
ATOM   6320 H HG23 . ILE   B 1 137 ? 33.737 -36.737 -4.175  1.00 24.77 ?  137 ILE   B HG23 1 
ATOM   6321 H HD11 . ILE   B 1 137 ? 36.439 -39.760 -3.825  1.00 29.81 ?  137 ILE   B HD11 1 
ATOM   6322 H HD12 . ILE   B 1 137 ? 35.961 -39.561 -2.322  1.00 29.81 ?  137 ILE   B HD12 1 
ATOM   6323 H HD13 . ILE   B 1 137 ? 34.921 -39.453 -3.519  1.00 29.81 ?  137 ILE   B HD13 1 
ATOM   6324 N N    . HIS   B 1 138 ? 34.391 -34.287 -0.948  1.00 17.93 ?  138 HIS   B N    1 
ATOM   6325 C CA   . HIS   B 1 138 ? 33.448 -33.311 -0.416  1.00 18.37 ?  138 HIS   B CA   1 
ATOM   6326 C C    . HIS   B 1 138 ? 33.864 -31.884 -0.758  1.00 17.49 ?  138 HIS   B C    1 
ATOM   6327 O O    . HIS   B 1 138 ? 33.016 -31.037 -1.058  1.00 18.27 ?  138 HIS   B O    1 
ATOM   6328 C CB   . HIS   B 1 138 ? 33.353 -33.475 1.092   1.00 20.27 ?  138 HIS   B CB   1 
ATOM   6329 C CG   . HIS   B 1 138 ? 32.418 -32.502 1.727   1.00 21.76 ?  138 HIS   B CG   1 
ATOM   6330 N ND1  . HIS   B 1 138 ? 31.082 -32.438 1.396   1.00 23.27 ?  138 HIS   B ND1  1 
ATOM   6331 C CD2  . HIS   B 1 138 ? 32.627 -31.527 2.644   1.00 22.52 ?  138 HIS   B CD2  1 
ATOM   6332 C CE1  . HIS   B 1 138 ? 30.505 -31.475 2.091   1.00 23.15 ?  138 HIS   B CE1  1 
ATOM   6333 N NE2  . HIS   B 1 138 ? 31.417 -30.914 2.864   1.00 22.63 ?  138 HIS   B NE2  1 
ATOM   6334 H H    . HIS   B 1 138 ? 34.838 -34.719 -0.351  1.00 21.52 ?  138 HIS   B H    1 
ATOM   6335 H HA   . HIS   B 1 138 ? 32.571 -33.480 -0.795  1.00 22.05 ?  138 HIS   B HA   1 
ATOM   6336 H HB2  . HIS   B 1 138 ? 33.032 -34.368 1.296   1.00 24.33 ?  138 HIS   B HB2  1 
ATOM   6337 H HB3  . HIS   B 1 138 ? 34.230 -33.342 1.482   1.00 24.33 ?  138 HIS   B HB3  1 
ATOM   6338 H HD2  . HIS   B 1 138 ? 33.427 -31.325 3.066   1.00 27.02 ?  138 HIS   B HD2  1 
ATOM   6339 H HE1  . HIS   B 1 138 ? 29.602 -31.241 2.052   1.00 27.78 ?  138 HIS   B HE1  1 
ATOM   6340 H HE2  . HIS   B 1 138 ? 31.272 -30.263 3.412   1.00 27.15 ?  138 HIS   B HE2  1 
ATOM   6341 N N    . SER   B 1 139 ? 35.160 -31.589 -0.695  1.00 16.47 ?  139 SER   B N    1 
ATOM   6342 C CA   . SER   B 1 139 ? 35.603 -30.242 -1.017  1.00 15.78 ?  139 SER   B CA   1 
ATOM   6343 C C    . SER   B 1 139 ? 35.264 -29.895 -2.455  1.00 15.33 ?  139 SER   B C    1 
ATOM   6344 O O    . SER   B 1 139 ? 34.809 -28.784 -2.737  1.00 15.45 ?  139 SER   B O    1 
ATOM   6345 C CB   . SER   B 1 139 ? 37.099 -30.108 -0.754  1.00 16.30 ?  139 SER   B CB   1 
ATOM   6346 O OG   . SER   B 1 139 ? 37.501 -28.764 -0.977  1.00 16.52 ?  139 SER   B OG   1 
ATOM   6347 H H    . SER   B 1 139 ? 35.781 -32.136 -0.472  1.00 19.76 ?  139 SER   B H    1 
ATOM   6348 H HA   . SER   B 1 139 ? 35.135 -29.612 -0.447  1.00 18.94 ?  139 SER   B HA   1 
ATOM   6349 H HB2  . SER   B 1 139 ? 37.280 -30.357 0.168   1.00 19.56 ?  139 SER   B HB2  1 
ATOM   6350 H HB3  . SER   B 1 139 ? 37.584 -30.685 -1.359  1.00 19.56 ?  139 SER   B HB3  1 
ATOM   6351 H HG   . SER   B 1 139 ? 38.325 -28.681 -0.813  1.00 19.82 ?  139 SER   B HG   1 
ATOM   6352 N N    . LEU   B 1 140 ? 35.455 -30.843 -3.379  1.00 15.09 ?  140 LEU   B N    1 
ATOM   6353 C CA   . LEU   B 1 140 ? 35.080 -30.604 -4.766  1.00 15.13 ?  140 LEU   B CA   1 
ATOM   6354 C C    . LEU   B 1 140 ? 33.576 -30.376 -4.894  1.00 15.22 ?  140 LEU   B C    1 
ATOM   6355 O O    . LEU   B 1 140 ? 33.137 -29.496 -5.638  1.00 15.47 ?  140 LEU   B O    1 
ATOM   6356 C CB   . LEU   B 1 140 ? 35.555 -31.765 -5.643  1.00 15.58 ?  140 LEU   B CB   1 
ATOM   6357 C CG   . LEU   B 1 140 ? 35.185 -31.670 -7.116  1.00 15.44 ?  140 LEU   B CG   1 
ATOM   6358 C CD1  . LEU   B 1 140 ? 35.763 -30.405 -7.724  1.00 16.67 ?  140 LEU   B CD1  1 
ATOM   6359 C CD2  . LEU   B 1 140 ? 35.668 -32.912 -7.843  1.00 16.75 ?  140 LEU   B CD2  1 
ATOM   6360 H H    . LEU   B 1 140 ? 35.784 -31.620 -3.230  1.00 18.10 ?  140 LEU   B H    1 
ATOM   6361 H HA   . LEU   B 1 140 ? 35.531 -29.805 -5.078  1.00 18.16 ?  140 LEU   B HA   1 
ATOM   6362 H HB2  . LEU   B 1 140 ? 36.522 -31.820 -5.597  1.00 18.70 ?  140 LEU   B HB2  1 
ATOM   6363 H HB3  . LEU   B 1 140 ? 35.169 -32.591 -5.306  1.00 18.70 ?  140 LEU   B HB3  1 
ATOM   6364 H HG   . LEU   B 1 140 ? 34.218 -31.628 -7.199  1.00 18.52 ?  140 LEU   B HG   1 
ATOM   6365 H HD11 . LEU   B 1 140 ? 35.642 -30.434 -8.684  1.00 20.00 ?  140 LEU   B HD11 1 
ATOM   6366 H HD12 . LEU   B 1 140 ? 35.301 -29.635 -7.355  1.00 20.00 ?  140 LEU   B HD12 1 
ATOM   6367 H HD13 . LEU   B 1 140 ? 36.708 -30.358 -7.509  1.00 20.00 ?  140 LEU   B HD13 1 
ATOM   6368 H HD21 . LEU   B 1 140 ? 35.423 -32.842 -8.779  1.00 20.10 ?  140 LEU   B HD21 1 
ATOM   6369 H HD22 . LEU   B 1 140 ? 36.626 -32.978 -7.751  1.00 20.10 ?  140 LEU   B HD22 1 
ATOM   6370 H HD23 . LEU   B 1 140 ? 35.239 -33.691 -7.449  1.00 20.10 ?  140 LEU   B HD23 1 
ATOM   6371 N N    . ARG   B 1 141 ? 32.774 -31.167 -4.179  1.00 15.49 ?  141 ARG   B N    1 
ATOM   6372 C CA   . ARG   B 1 141 ? 31.325 -30.988 -4.153  1.00 16.38 ?  141 ARG   B CA   1 
ATOM   6373 C C    . ARG   B 1 141 ? 30.950 -29.573 -3.735  1.00 15.79 ?  141 ARG   B C    1 
ATOM   6374 O O    . ARG   B 1 141 ? 30.145 -28.902 -4.400  1.00 16.42 ?  141 ARG   B O    1 
ATOM   6375 C CB   . ARG   B 1 141 ? 30.750 -32.006 -3.163  1.00 18.03 ?  141 ARG   B CB   1 
ATOM   6376 C CG   . ARG   B 1 141 ? 29.278 -31.890 -2.841  1.00 20.02 ?  141 ARG   B CG   1 
ATOM   6377 C CD   . ARG   B 1 141 ? 28.485 -32.522 -3.909  1.00 21.22 ?  141 ARG   B CD   1 
ATOM   6378 N NE   . ARG   B 1 141 ? 28.226 -31.615 -5.015  1.00 21.69 ?  141 ARG   B NE   1 
ATOM   6379 C CZ   . ARG   B 1 141 ? 28.210 -31.976 -6.290  1.00 21.34 ?  141 ARG   B CZ   1 
ATOM   6380 N NH1  . ARG   B 1 141 ? 28.640 -33.167 -6.680  1.00 21.32 ?  141 ARG   B NH1  1 
ATOM   6381 N NH2  . ARG   B 1 141 ? 27.742 -31.125 -7.196  1.00 21.99 ?  141 ARG   B NH2  1 
ATOM   6382 H H    . ARG   B 1 141 ? 33.054 -31.815 -3.693  1.00 18.59 ?  141 ARG   B H    1 
ATOM   6383 H HA   . ARG   B 1 141 ? 30.956 -31.149 -5.027  1.00 19.65 ?  141 ARG   B HA   1 
ATOM   6384 H HB2  . ARG   B 1 141 ? 30.906 -32.890 -3.522  1.00 21.63 ?  141 ARG   B HB2  1 
ATOM   6385 H HB3  . ARG   B 1 141 ? 31.228 -31.916 -2.325  1.00 21.63 ?  141 ARG   B HB3  1 
ATOM   6386 H HG2  . ARG   B 1 141 ? 29.099 -32.340 -2.004  1.00 24.02 ?  141 ARG   B HG2  1 
ATOM   6387 H HG3  . ARG   B 1 141 ? 29.020 -30.950 -2.775  1.00 24.02 ?  141 ARG   B HG3  1 
ATOM   6388 H HD2  . ARG   B 1 141 ? 28.969 -33.298 -4.242  1.00 25.47 ?  141 ARG   B HD2  1 
ATOM   6389 H HD3  . ARG   B 1 141 ? 27.638 -32.805 -3.541  1.00 25.47 ?  141 ARG   B HD3  1 
ATOM   6390 H HE   . ARG   B 1 141 ? 28.092 -30.786 -4.828  1.00 26.03 ?  141 ARG   B HE   1 
ATOM   6391 H HH11 . ARG   B 1 141 ? 28.932 -33.737 -6.106  1.00 25.59 ?  141 ARG   B HH11 1 
ATOM   6392 H HH12 . ARG   B 1 141 ? 28.625 -33.373 -7.512  1.00 25.59 ?  141 ARG   B HH12 1 
ATOM   6393 H HH21 . ARG   B 1 141 ? 27.470 -30.344 -6.954  1.00 26.39 ?  141 ARG   B HH21 1 
ATOM   6394 H HH22 . ARG   B 1 141 ? 27.747 -31.337 -8.028  1.00 26.39 ?  141 ARG   B HH22 1 
ATOM   6395 N N    . VAL   B 1 142 ? 31.502 -29.113 -2.612  1.00 16.10 ?  142 VAL   B N    1 
ATOM   6396 C CA   . VAL   B 1 142 ? 31.164 -27.775 -2.135  1.00 15.77 ?  142 VAL   B CA   1 
ATOM   6397 C C    . VAL   B 1 142 ? 31.641 -26.725 -3.130  1.00 15.18 ?  142 VAL   B C    1 
ATOM   6398 O O    . VAL   B 1 142 ? 30.935 -25.744 -3.402  1.00 15.65 ?  142 VAL   B O    1 
ATOM   6399 C CB   . VAL   B 1 142 ? 31.719 -27.542 -0.718  1.00 16.58 ?  142 VAL   B CB   1 
ATOM   6400 C CG1  . VAL   B 1 142 ? 31.400 -26.124 -0.245  1.00 16.18 ?  142 VAL   B CG1  1 
ATOM   6401 C CG2  . VAL   B 1 142 ? 31.154 -28.577 0.250   1.00 17.10 ?  142 VAL   B CG2  1 
ATOM   6402 H H    . VAL   B 1 142 ? 32.065 -29.541 -2.117  1.00 19.33 ?  142 VAL   B H    1 
ATOM   6403 H HA   . VAL   B 1 142 ? 30.206 -27.700 -2.081  1.00 18.93 ?  142 VAL   B HA   1 
ATOM   6404 H HB   . VAL   B 1 142 ? 32.688 -27.640 -0.733  1.00 19.90 ?  142 VAL   B HB   1 
ATOM   6405 H HG11 . VAL   B 1 142 ? 31.594 -26.057 0.703   1.00 19.42 ?  142 VAL   B HG11 1 
ATOM   6406 H HG12 . VAL   B 1 142 ? 31.950 -25.492 -0.738  1.00 19.42 ?  142 VAL   B HG12 1 
ATOM   6407 H HG13 . VAL   B 1 142 ? 30.462 -25.943 -0.406  1.00 19.42 ?  142 VAL   B HG13 1 
ATOM   6408 H HG21 . VAL   B 1 142 ? 31.475 -28.381 1.143   1.00 20.52 ?  142 VAL   B HG21 1 
ATOM   6409 H HG22 . VAL   B 1 142 ? 30.188 -28.534 0.224   1.00 20.52 ?  142 VAL   B HG22 1 
ATOM   6410 H HG23 . VAL   B 1 142 ? 31.456 -29.459 -0.023  1.00 20.52 ?  142 VAL   B HG23 1 
ATOM   6411 N N    . CYS   B 1 143 ? 32.830 -26.927 -3.707  1.00 14.73 ?  143 CYS   B N    1 
ATOM   6412 C CA   . CYS   B 1 143 ? 33.331 -26.001 -4.718  1.00 14.35 ?  143 CYS   B CA   1 
ATOM   6413 C C    . CYS   B 1 143 ? 32.331 -25.859 -5.864  1.00 14.47 ?  143 CYS   B C    1 
ATOM   6414 O O    . CYS   B 1 143 ? 31.916 -24.749 -6.222  1.00 14.90 ?  143 CYS   B O    1 
ATOM   6415 C CB   . CYS   B 1 143 ? 34.697 -26.474 -5.226  1.00 14.95 ?  143 CYS   B CB   1 
ATOM   6416 S SG   . CYS   B 1 143 ? 35.428 -25.396 -6.472  1.00 15.09 ?  143 CYS   B SG   1 
ATOM   6417 H H    . CYS   B 1 143 ? 33.364 -27.578 -3.527  1.00 17.68 ?  143 CYS   B H    1 
ATOM   6418 H HA   . CYS   B 1 143 ? 33.457 -25.126 -4.317  1.00 17.22 ?  143 CYS   B HA   1 
ATOM   6419 H HB2  . CYS   B 1 143 ? 35.318 -26.528 -4.479  1.00 17.94 ?  143 CYS   B HB2  1 
ATOM   6420 H HB3  . CYS   B 1 143 ? 34.598 -27.354 -5.619  1.00 17.94 ?  143 CYS   B HB3  1 
ATOM   6421 H HG   . CYS   B 1 143 ? 36.514 -25.818 -6.781  1.00 18.10 ?  143 CYS   B HG   1 
ATOM   6422 N N    . VAL   B 1 144 ? 31.906 -26.985 -6.435  1.00 15.46 ?  144 VAL   B N    1 
ATOM   6423 C CA   . VAL   B 1 144 ? 30.999 -26.929 -7.574  1.00 16.38 ?  144 VAL   B CA   1 
ATOM   6424 C C    . VAL   B 1 144 ? 29.659 -26.310 -7.204  1.00 16.66 ?  144 VAL   B C    1 
ATOM   6425 O O    . VAL   B 1 144 ? 29.044 -25.611 -8.020  1.00 17.61 ?  144 VAL   B O    1 
ATOM   6426 C CB   . VAL   B 1 144 ? 30.835 -28.355 -8.119  1.00 19.04 ?  144 VAL   B CB   1 
ATOM   6427 C CG1  . VAL   B 1 144 ? 29.528 -28.519 -8.894  1.00 21.29 ?  144 VAL   B CG1  1 
ATOM   6428 C CG2  . VAL   B 1 144 ? 32.054 -28.754 -8.949  1.00 19.17 ?  144 VAL   B CG2  1 
ATOM   6429 H H    . VAL   B 1 144 ? 32.134 -27.776 -6.188  1.00 18.55 ?  144 VAL   B H    1 
ATOM   6430 H HA   . VAL   B 1 144 ? 31.389 -26.389 -8.272  1.00 19.65 ?  144 VAL   B HA   1 
ATOM   6431 H HB   . VAL   B 1 144 ? 30.795 -28.971 -7.369  1.00 22.85 ?  144 VAL   B HB   1 
ATOM   6432 H HG11 . VAL   B 1 144 ? 29.583 -29.328 -9.432  1.00 25.55 ?  144 VAL   B HG11 1 
ATOM   6433 H HG12 . VAL   B 1 144 ? 28.793 -28.598 -8.266  1.00 25.55 ?  144 VAL   B HG12 1 
ATOM   6434 H HG13 . VAL   B 1 144 ? 29.402 -27.752 -9.469  1.00 25.55 ?  144 VAL   B HG13 1 
ATOM   6435 H HG21 . VAL   B 1 144 ? 31.933 -29.657 -9.281  1.00 23.00 ?  144 VAL   B HG21 1 
ATOM   6436 H HG22 . VAL   B 1 144 ? 32.139 -28.137 -9.695  1.00 23.00 ?  144 VAL   B HG22 1 
ATOM   6437 H HG23 . VAL   B 1 144 ? 32.843 -28.707 -8.390  1.00 23.00 ?  144 VAL   B HG23 1 
ATOM   6438 N N    . ASP   B 1 145 ? 29.188 -26.548 -5.986  1.00 17.10 ?  145 ASP   B N    1 
ATOM   6439 C CA   . ASP   B 1 145 ? 27.883 -26.065 -5.561  1.00 17.64 ?  145 ASP   B CA   1 
ATOM   6440 C C    . ASP   B 1 145 ? 27.917 -24.643 -5.023  1.00 17.05 ?  145 ASP   B C    1 
ATOM   6441 O O    . ASP   B 1 145 ? 26.858 -24.100 -4.686  1.00 18.49 ?  145 ASP   B O    1 
ATOM   6442 C CB   . ASP   B 1 145 ? 27.305 -26.971 -4.473  1.00 19.61 ?  145 ASP   B CB   1 
ATOM   6443 C CG   . ASP   B 1 145 ? 26.931 -28.350 -4.979  1.00 21.50 ?  145 ASP   B CG   1 
ATOM   6444 O OD1  . ASP   B 1 145 ? 26.820 -28.560 -6.205  1.00 21.07 ?  145 ASP   B OD1  1 
ATOM   6445 O OD2  . ASP   B 1 145 ? 26.729 -29.231 -4.125  1.00 23.27 -1 145 ASP   B OD2  1 
ATOM   6446 H H    . ASP   B 1 145 ? 29.618 -26.981 -5.380  1.00 20.52 ?  145 ASP   B H    1 
ATOM   6447 H HA   . ASP   B 1 145 ? 27.285 -26.066 -6.319  1.00 21.17 ?  145 ASP   B HA   1 
ATOM   6448 H HB2  . ASP   B 1 145 ? 27.958 -27.082 -3.773  1.00 23.53 ?  145 ASP   B HB2  1 
ATOM   6449 H HB3  . ASP   B 1 145 ? 26.501 -26.555 -4.119  1.00 23.53 ?  145 ASP   B HB3  1 
ATOM   6450 N N    . THR   B 1 146 ? 29.093 -24.034 -4.925  1.00 15.32 ?  146 THR   B N    1 
ATOM   6451 C CA   . THR   B 1 146 ? 29.232 -22.708 -4.325  1.00 15.13 ?  146 THR   B CA   1 
ATOM   6452 C C    . THR   B 1 146 ? 29.860 -21.686 -5.253  1.00 14.92 ?  146 THR   B C    1 
ATOM   6453 O O    . THR   B 1 146 ? 29.395 -20.530 -5.312  1.00 14.89 ?  146 THR   B O    1 
ATOM   6454 C CB   . THR   B 1 146 ? 30.069 -22.813 -3.040  1.00 14.84 ?  146 THR   B CB   1 
ATOM   6455 O OG1  . THR   B 1 146 ? 29.486 -23.777 -2.159  1.00 15.15 ?  146 THR   B OG1  1 
ATOM   6456 C CG2  . THR   B 1 146 ? 30.185 -21.460 -2.346  1.00 15.58 ?  146 THR   B CG2  1 
ATOM   6457 H H    . THR   B 1 146 ? 29.840 -24.352 -5.216  1.00 18.39 ?  146 THR   B H    1 
ATOM   6458 H HA   . THR   B 1 146 ? 28.362 -22.369 -4.082  1.00 18.16 ?  146 THR   B HA   1 
ATOM   6459 H HB   . THR   B 1 146 ? 30.967 -23.098 -3.270  1.00 17.81 ?  146 THR   B HB   1 
ATOM   6460 H HG1  . THR   B 1 146 ? 29.487 -24.538 -2.523  1.00 18.18 ?  146 THR   B HG1  1 
ATOM   6461 H HG21 . THR   B 1 146 ? 30.520 -21.576 -1.445  1.00 18.69 ?  146 THR   B HG21 1 
ATOM   6462 H HG22 . THR   B 1 146 ? 30.806 -20.887 -2.835  1.00 18.69 ?  146 THR   B HG22 1 
ATOM   6463 H HG23 . THR   B 1 146 ? 29.322 -21.026 -2.312  1.00 18.69 ?  146 THR   B HG23 1 
ATOM   6464 N N    . VAL   B 1 147 ? 30.927 -22.062 -5.952  1.00 14.54 ?  147 VAL   B N    1 
ATOM   6465 C CA   . VAL   B 1 147 ? 31.652 -21.123 -6.793  1.00 14.13 ?  147 VAL   B CA   1 
ATOM   6466 C C    . VAL   B 1 147 ? 30.918 -20.984 -8.115  1.00 14.45 ?  147 VAL   B C    1 
ATOM   6467 O O    . VAL   B 1 147 ? 30.534 -21.984 -8.737  1.00 15.42 ?  147 VAL   B O    1 
ATOM   6468 C CB   . VAL   B 1 147 ? 33.105 -21.582 -6.996  1.00 14.04 ?  147 VAL   B CB   1 
ATOM   6469 C CG1  . VAL   B 1 147 ? 33.866 -20.563 -7.824  1.00 13.96 ?  147 VAL   B CG1  1 
ATOM   6470 C CG2  . VAL   B 1 147 ? 33.795 -21.786 -5.651  1.00 14.35 ?  147 VAL   B CG2  1 
ATOM   6471 H H    . VAL   B 1 147 ? 31.246 -22.865 -5.969  1.00 17.45 ?  147 VAL   B H    1 
ATOM   6472 H HA   . VAL   B 1 147 ? 31.671 -20.257 -6.362  1.00 16.95 ?  147 VAL   B HA   1 
ATOM   6473 H HB   . VAL   B 1 147 ? 33.115 -22.429 -7.473  1.00 16.84 ?  147 VAL   B HB   1 
ATOM   6474 H HG11 . VAL   B 1 147 ? 34.811 -20.776 -7.808  1.00 16.75 ?  147 VAL   B HG11 1 
ATOM   6475 H HG12 . VAL   B 1 147 ? 33.537 -20.575 -8.735  1.00 16.75 ?  147 VAL   B HG12 1 
ATOM   6476 H HG13 . VAL   B 1 147 ? 33.726 -19.677 -7.438  1.00 16.75 ?  147 VAL   B HG13 1 
ATOM   6477 H HG21 . VAL   B 1 147 ? 34.731 -21.992 -5.800  1.00 17.22 ?  147 VAL   B HG21 1 
ATOM   6478 H HG22 . VAL   B 1 147 ? 33.716 -20.969 -5.131  1.00 17.22 ?  147 VAL   B HG22 1 
ATOM   6479 H HG23 . VAL   B 1 147 ? 33.366 -22.518 -5.180  1.00 17.22 ?  147 VAL   B HG23 1 
ATOM   6480 N N    . ARG   B 1 148 ? 30.710 -19.733 -8.534  1.00 13.95 ?  148 ARG   B N    1 
ATOM   6481 C CA   . ARG   B 1 148 ? 30.088 -19.417 -9.810  1.00 14.28 ?  148 ARG   B CA   1 
ATOM   6482 C C    . ARG   B 1 148 ? 31.036 -18.739 -10.786 1.00 14.09 ?  148 ARG   B C    1 
ATOM   6483 O O    . ARG   B 1 148 ? 30.735 -18.700 -11.982 1.00 15.76 ?  148 ARG   B O    1 
ATOM   6484 C CB   . ARG   B 1 148 ? 28.848 -18.531 -9.598  1.00 14.27 ?  148 ARG   B CB   1 
ATOM   6485 C CG   . ARG   B 1 148 ? 27.780 -19.234 -8.780  1.00 15.58 ?  148 ARG   B CG   1 
ATOM   6486 C CD   . ARG   B 1 148 ? 26.558 -18.371 -8.473  1.00 16.65 ?  148 ARG   B CD   1 
ATOM   6487 N NE   . ARG   B 1 148 ? 26.935 -17.169 -7.741  1.00 16.76 ?  148 ARG   B NE   1 
ATOM   6488 C CZ   . ARG   B 1 148 ? 27.239 -17.133 -6.450  1.00 15.89 ?  148 ARG   B CZ   1 
ATOM   6489 N NH1  . ARG   B 1 148 ? 27.178 -18.215 -5.687  1.00 16.17 ?  148 ARG   B NH1  1 
ATOM   6490 N NH2  . ARG   B 1 148 ? 27.639 -15.985 -5.911  1.00 16.01 ?  148 ARG   B NH2  1 
ATOM   6491 H H    . ARG   B 1 148 ? 30.938 -19.030 -8.081  1.00 16.74 ?  148 ARG   B H    1 
ATOM   6492 H HA   . ARG   B 1 148 ? 29.789 -20.239 -10.218 1.00 17.13 ?  148 ARG   B HA   1 
ATOM   6493 H HB2  . ARG   B 1 148 ? 29.110 -17.723 -9.125  1.00 17.12 ?  148 ARG   B HB2  1 
ATOM   6494 H HB3  . ARG   B 1 148 ? 28.470 -18.302 -10.461 1.00 17.12 ?  148 ARG   B HB3  1 
ATOM   6495 H HG2  . ARG   B 1 148 ? 27.481 -20.015 -9.274  1.00 18.70 ?  148 ARG   B HG2  1 
ATOM   6496 H HG3  . ARG   B 1 148 ? 28.171 -19.512 -7.936  1.00 18.70 ?  148 ARG   B HG3  1 
ATOM   6497 H HD2  . ARG   B 1 148 ? 26.143 -18.104 -9.307  1.00 19.98 ?  148 ARG   B HD2  1 
ATOM   6498 H HD3  . ARG   B 1 148 ? 25.939 -18.881 -7.932  1.00 19.98 ?  148 ARG   B HD3  1 
ATOM   6499 H HE   . ARG   B 1 148 ? 26.969 -16.430 -8.177  1.00 20.11 ?  148 ARG   B HE   1 
ATOM   6500 H HH11 . ARG   B 1 148 ? 26.921 -18.968 -6.020  1.00 19.41 ?  148 ARG   B HH11 1 
ATOM   6501 H HH12 . ARG   B 1 148 ? 27.380 -18.168 -4.851  1.00 19.41 ?  148 ARG   B HH12 1 
ATOM   6502 H HH21 . ARG   B 1 148 ? 27.697 -15.280 -6.397  1.00 19.21 ?  148 ARG   B HH21 1 
ATOM   6503 H HH22 . ARG   B 1 148 ? 27.847 -15.950 -5.076  1.00 19.21 ?  148 ARG   B HH22 1 
ATOM   6504 N N    . THR   B 1 149 ? 32.148 -18.186 -10.303 1.00 14.06 ?  149 THR   B N    1 
ATOM   6505 C CA   . THR   B 1 149 ? 33.186 -17.622 -11.152 1.00 14.24 ?  149 THR   B CA   1 
ATOM   6506 C C    . THR   B 1 149 ? 34.068 -18.764 -11.668 1.00 13.98 ?  149 THR   B C    1 
ATOM   6507 O O    . THR   B 1 149 ? 33.870 -19.938 -11.332 1.00 14.56 ?  149 THR   B O    1 
ATOM   6508 C CB   . THR   B 1 149 ? 33.963 -16.577 -10.365 1.00 14.44 ?  149 THR   B CB   1 
ATOM   6509 O OG1  . THR   B 1 149 ? 34.421 -17.181 -9.155  1.00 14.33 ?  149 THR   B OG1  1 
ATOM   6510 C CG2  . THR   B 1 149 ? 33.084 -15.362 -10.055 1.00 15.04 ?  149 THR   B CG2  1 
ATOM   6511 H H    . THR   B 1 149 ? 32.317 -18.120 -9.462  1.00 16.87 ?  149 THR   B H    1 
ATOM   6512 H HA   . THR   B 1 149 ? 32.776 -17.184 -11.910 1.00 17.09 ?  149 THR   B HA   1 
ATOM   6513 H HB   . THR   B 1 149 ? 34.728 -16.290 -10.879 1.00 17.32 ?  149 THR   B HB   1 
ATOM   6514 H HG1  . THR   B 1 149 ? 34.850 -16.620 -8.689  1.00 17.20 ?  149 THR   B HG1  1 
ATOM   6515 H HG21 . THR   B 1 149 ? 33.594 -14.702 -9.559  1.00 18.05 ?  149 THR   B HG21 1 
ATOM   6516 H HG22 . THR   B 1 149 ? 32.771 -14.965 -10.881 1.00 18.05 ?  149 THR   B HG22 1 
ATOM   6517 H HG23 . THR   B 1 149 ? 32.317 -15.631 -9.524  1.00 18.05 ?  149 THR   B HG23 1 
ATOM   6518 N N    . ASN   B 1 150 ? 35.031 -18.444 -12.523 1.00 13.89 ?  150 ASN   B N    1 
ATOM   6519 C CA   . ASN   B 1 150 ? 35.802 -19.471 -13.217 1.00 14.21 ?  150 ASN   B CA   1 
ATOM   6520 C C    . ASN   B 1 150 ? 36.970 -19.921 -12.342 1.00 13.46 ?  150 ASN   B C    1 
ATOM   6521 O O    . ASN   B 1 150 ? 37.903 -19.155 -12.094 1.00 14.19 ?  150 ASN   B O    1 
ATOM   6522 C CB   . ASN   B 1 150 ? 36.270 -18.957 -14.571 1.00 16.32 ?  150 ASN   B CB   1 
ATOM   6523 C CG   . ASN   B 1 150 ? 35.126 -18.745 -15.519 1.00 19.09 ?  150 ASN   B CG   1 
ATOM   6524 O OD1  . ASN   B 1 150 ? 34.200 -19.542 -15.555 1.00 20.13 ?  150 ASN   B OD1  1 
ATOM   6525 N ND2  . ASN   B 1 150 ? 35.163 -17.659 -16.271 1.00 21.26 ?  150 ASN   B ND2  1 
ATOM   6526 H H    . ASN   B 1 150 ? 35.262 -17.636 -12.713 1.00 16.67 ?  150 ASN   B H    1 
ATOM   6527 H HA   . ASN   B 1 150 ? 35.224 -20.237 -13.370 1.00 17.05 ?  150 ASN   B HA   1 
ATOM   6528 H HB2  . ASN   B 1 150 ? 36.721 -18.105 -14.447 1.00 19.58 ?  150 ASN   B HB2  1 
ATOM   6529 H HB3  . ASN   B 1 150 ? 36.873 -19.602 -14.963 1.00 19.58 ?  150 ASN   B HB3  1 
ATOM   6530 H HD21 . ASN   B 1 150 ? 34.527 -17.494 -16.831 1.00 25.51 ?  150 ASN   B HD21 1 
ATOM   6531 H HD22 . ASN   B 1 150 ? 35.830 -17.117 -16.215 1.00 25.51 ?  150 ASN   B HD22 1 
ATOM   6532 N N    . VAL   B 1 151 ? 36.924 -21.168 -11.881 1.00 13.71 ?  151 VAL   B N    1 
ATOM   6533 C CA   . VAL   B 1 151 ? 37.938 -21.699 -10.983 1.00 13.77 ?  151 VAL   B CA   1 
ATOM   6534 C C    . VAL   B 1 151 ? 38.636 -22.875 -11.652 1.00 13.23 ?  151 VAL   B C    1 
ATOM   6535 O O    . VAL   B 1 151 ? 37.991 -23.811 -12.147 1.00 14.72 ?  151 VAL   B O    1 
ATOM   6536 C CB   . VAL   B 1 151 ? 37.377 -22.036 -9.586  1.00 14.91 ?  151 VAL   B CB   1 
ATOM   6537 C CG1  . VAL   B 1 151 ? 36.200 -23.019 -9.655  1.00 16.29 ?  151 VAL   B CG1  1 
ATOM   6538 C CG2  . VAL   B 1 151 ? 38.493 -22.540 -8.677  1.00 14.71 ?  151 VAL   B CG2  1 
ATOM   6539 H H    . VAL   B 1 151 ? 36.300 -21.735 -12.083 1.00 16.45 ?  151 VAL   B H    1 
ATOM   6540 H HA   . VAL   B 1 151 ? 38.604 -21.008 -10.856 1.00 16.52 ?  151 VAL   B HA   1 
ATOM   6541 H HB   . VAL   B 1 151 ? 37.038 -21.210 -9.193  1.00 17.89 ?  151 VAL   B HB   1 
ATOM   6542 H HG11 . VAL   B 1 151 ? 35.886 -23.200 -8.753  1.00 19.55 ?  151 VAL   B HG11 1 
ATOM   6543 H HG12 . VAL   B 1 151 ? 35.481 -22.621 -10.176 1.00 19.55 ?  151 VAL   B HG12 1 
ATOM   6544 H HG13 . VAL   B 1 151 ? 36.496 -23.840 -10.074 1.00 19.55 ?  151 VAL   B HG13 1 
ATOM   6545 H HG21 . VAL   B 1 151 ? 38.150 -22.603 -7.771  1.00 17.65 ?  151 VAL   B HG21 1 
ATOM   6546 H HG22 . VAL   B 1 151 ? 38.779 -23.411 -8.985  1.00 17.65 ?  151 VAL   B HG22 1 
ATOM   6547 H HG23 . VAL   B 1 151 ? 39.231 -21.913 -8.707  1.00 17.65 ?  151 VAL   B HG23 1 
ATOM   6548 N N    . TYR   B 1 152 ? 39.965 -22.791 -11.677 1.00 12.98 ?  152 TYR   B N    1 
ATOM   6549 C CA   . TYR   B 1 152 ? 40.863 -23.783 -12.251 1.00 13.07 ?  152 TYR   B CA   1 
ATOM   6550 C C    . TYR   B 1 152 ? 41.583 -24.464 -11.092 1.00 12.22 ?  152 TYR   B C    1 
ATOM   6551 O O    . TYR   B 1 152 ? 42.443 -23.855 -10.450 1.00 12.98 ?  152 TYR   B O    1 
ATOM   6552 C CB   . TYR   B 1 152 ? 41.831 -23.077 -13.202 1.00 14.35 ?  152 TYR   B CB   1 
ATOM   6553 C CG   . TYR   B 1 152 ? 41.151 -22.605 -14.469 1.00 14.97 ?  152 TYR   B CG   1 
ATOM   6554 C CD1  . TYR   B 1 152 ? 40.483 -21.380 -14.522 1.00 14.84 ?  152 TYR   B CD1  1 
ATOM   6555 C CD2  . TYR   B 1 152 ? 41.142 -23.403 -15.599 1.00 16.13 ?  152 TYR   B CD2  1 
ATOM   6556 C CE1  . TYR   B 1 152 ? 39.847 -20.965 -15.675 1.00 16.68 ?  152 TYR   B CE1  1 
ATOM   6557 C CE2  . TYR   B 1 152 ? 40.498 -23.006 -16.752 1.00 17.18 ?  152 TYR   B CE2  1 
ATOM   6558 C CZ   . TYR   B 1 152 ? 39.858 -21.782 -16.787 1.00 17.16 ?  152 TYR   B CZ   1 
ATOM   6559 O OH   . TYR   B 1 152 ? 39.231 -21.390 -17.943 1.00 20.37 ?  152 TYR   B OH   1 
ATOM   6560 H H    . TYR   B 1 152 ? 40.399 -22.127 -11.330 1.00 15.58 ?  152 TYR   B H    1 
ATOM   6561 H HA   . TYR   B 1 152 ? 40.354 -24.444 -12.743 1.00 15.69 ?  152 TYR   B HA   1 
ATOM   6562 H HB2  . TYR   B 1 152 ? 42.206 -22.302 -12.749 1.00 17.22 ?  152 TYR   B HB2  1 
ATOM   6563 H HB3  . TYR   B 1 152 ? 42.538 -23.691 -13.446 1.00 17.22 ?  152 TYR   B HB3  1 
ATOM   6564 H HD1  . TYR   B 1 152 ? 40.474 -20.828 -13.770 1.00 17.81 ?  152 TYR   B HD1  1 
ATOM   6565 H HD2  . TYR   B 1 152 ? 41.571 -24.229 -15.575 1.00 19.36 ?  152 TYR   B HD2  1 
ATOM   6566 H HE1  . TYR   B 1 152 ? 39.413 -20.141 -15.705 1.00 20.01 ?  152 TYR   B HE1  1 
ATOM   6567 H HE2  . TYR   B 1 152 ? 40.515 -23.550 -17.507 1.00 20.62 ?  152 TYR   B HE2  1 
ATOM   6568 H HH   . TYR   B 1 152 ? 39.325 -21.972 -18.541 1.00 24.44 ?  152 TYR   B HH   1 
ATOM   6569 N N    . LEU   B 1 153 ? 41.206 -25.714 -10.812 1.00 12.76 ?  153 LEU   B N    1 
ATOM   6570 C CA   . LEU   B 1 153 ? 41.728 -26.462 -9.678  1.00 12.70 ?  153 LEU   B CA   1 
ATOM   6571 C C    . LEU   B 1 153 ? 42.952 -27.269 -10.089 1.00 13.03 ?  153 LEU   B C    1 
ATOM   6572 O O    . LEU   B 1 153 ? 42.922 -27.990 -11.089 1.00 14.26 ?  153 LEU   B O    1 
ATOM   6573 C CB   . LEU   B 1 153 ? 40.654 -27.415 -9.155  1.00 13.06 ?  153 LEU   B CB   1 
ATOM   6574 C CG   . LEU   B 1 153 ? 39.397 -26.763 -8.585  1.00 14.08 ?  153 LEU   B CG   1 
ATOM   6575 C CD1  . LEU   B 1 153 ? 38.292 -27.802 -8.435  1.00 15.32 ?  153 LEU   B CD1  1 
ATOM   6576 C CD2  . LEU   B 1 153 ? 39.723 -26.125 -7.243  1.00 14.36 ?  153 LEU   B CD2  1 
ATOM   6577 H H    . LEU   B 1 153 ? 40.622 -26.153 -11.274 1.00 15.31 ?  153 LEU   B H    1 
ATOM   6578 H HA   . LEU   B 1 153 ? 41.963 -25.846 -8.968  1.00 15.24 ?  153 LEU   B HA   1 
ATOM   6579 H HB2  . LEU   B 1 153 ? 40.371 -27.992 -9.879  1.00 15.67 ?  153 LEU   B HB2  1 
ATOM   6580 H HB3  . LEU   B 1 153 ? 41.042 -27.954 -8.445  1.00 15.67 ?  153 LEU   B HB3  1 
ATOM   6581 H HG   . LEU   B 1 153 ? 39.086 -26.064 -9.183  1.00 16.89 ?  153 LEU   B HG   1 
ATOM   6582 H HD11 . LEU   B 1 153 ? 37.488 -27.363 -8.108  1.00 18.39 ?  153 LEU   B HD11 1 
ATOM   6583 H HD12 . LEU   B 1 153 ? 38.121 -28.202 -9.298  1.00 18.39 ?  153 LEU   B HD12 1 
ATOM   6584 H HD13 . LEU   B 1 153 ? 38.579 -28.476 -7.802  1.00 18.39 ?  153 LEU   B HD13 1 
ATOM   6585 H HD21 . LEU   B 1 153 ? 38.917 -25.753 -6.857  1.00 17.23 ?  153 LEU   B HD21 1 
ATOM   6586 H HD22 . LEU   B 1 153 ? 40.088 -26.807 -6.650  1.00 17.23 ?  153 LEU   B HD22 1 
ATOM   6587 H HD23 . LEU   B 1 153 ? 40.383 -25.424 -7.375  1.00 17.23 ?  153 LEU   B HD23 1 
ATOM   6588 N N    . ALA   B 1 154 ? 44.014 -27.157 -9.300  1.00 13.14 ?  154 ALA   B N    1 
ATOM   6589 C CA   . ALA   B 1 154 ? 45.242 -27.919 -9.491  1.00 14.40 ?  154 ALA   B CA   1 
ATOM   6590 C C    . ALA   B 1 154 ? 45.322 -28.989 -8.409  1.00 15.21 ?  154 ALA   B C    1 
ATOM   6591 O O    . ALA   B 1 154 ? 45.282 -28.674 -7.212  1.00 16.87 ?  154 ALA   B O    1 
ATOM   6592 C CB   . ALA   B 1 154 ? 46.462 -27.004 -9.441  1.00 15.31 ?  154 ALA   B CB   1 
ATOM   6593 H H    . ALA   B 1 154 ? 44.041 -26.614 -8.628  1.00 15.77 ?  154 ALA   B H    1 
ATOM   6594 H HA   . ALA   B 1 154 ? 45.212 -28.350 -10.355 1.00 17.27 ?  154 ALA   B HA   1 
ATOM   6595 H HB1  . ALA   B 1 154 ? 47.259 -27.539 -9.571  1.00 18.37 ?  154 ALA   B HB1  1 
ATOM   6596 H HB2  . ALA   B 1 154 ? 46.392 -26.340 -10.150 1.00 18.37 ?  154 ALA   B HB2  1 
ATOM   6597 H HB3  . ALA   B 1 154 ? 46.495 -26.560 -8.579  1.00 18.37 ?  154 ALA   B HB3  1 
ATOM   6598 N N    . VAL   B 1 155 ? 45.416 -30.245 -8.832  1.00 14.40 ?  155 VAL   B N    1 
ATOM   6599 C CA   . VAL   B 1 155 ? 45.525 -31.389 -7.934  1.00 15.09 ?  155 VAL   B CA   1 
ATOM   6600 C C    . VAL   B 1 155 ? 46.861 -32.062 -8.220  1.00 14.51 ?  155 VAL   B C    1 
ATOM   6601 O O    . VAL   B 1 155 ? 47.086 -32.561 -9.330  1.00 16.40 ?  155 VAL   B O    1 
ATOM   6602 C CB   . VAL   B 1 155 ? 44.357 -32.370 -8.113  1.00 16.23 ?  155 VAL   B CB   1 
ATOM   6603 C CG1  . VAL   B 1 155 ? 44.557 -33.578 -7.218  1.00 16.52 ?  155 VAL   B CG1  1 
ATOM   6604 C CG2  . VAL   B 1 155 ? 43.027 -31.666 -7.803  1.00 16.84 ?  155 VAL   B CG2  1 
ATOM   6605 H H    . VAL   B 1 155 ? 45.432 -30.465 -9.666  1.00 17.28 ?  155 VAL   B H    1 
ATOM   6606 H HA   . VAL   B 1 155 ? 45.527 -31.076 -7.016  1.00 18.11 ?  155 VAL   B HA   1 
ATOM   6607 H HB   . VAL   B 1 155 ? 44.330 -32.667 -9.036  1.00 19.47 ?  155 VAL   B HB   1 
ATOM   6608 H HG11 . VAL   B 1 155 ? 43.724 -34.073 -7.163  1.00 19.82 ?  155 VAL   B HG11 1 
ATOM   6609 H HG12 . VAL   B 1 155 ? 45.249 -34.146 -7.596  1.00 19.82 ?  155 VAL   B HG12 1 
ATOM   6610 H HG13 . VAL   B 1 155 ? 44.821 -33.280 -6.333  1.00 19.82 ?  155 VAL   B HG13 1 
ATOM   6611 H HG21 . VAL   B 1 155 ? 42.307 -32.310 -7.887  1.00 20.20 ?  155 VAL   B HG21 1 
ATOM   6612 H HG22 . VAL   B 1 155 ? 43.059 -31.322 -6.896  1.00 20.20 ?  155 VAL   B HG22 1 
ATOM   6613 H HG23 . VAL   B 1 155 ? 42.898 -30.939 -8.429  1.00 20.20 ?  155 VAL   B HG23 1 
ATOM   6614 N N    . PHE   B 1 156 ? 47.732 -32.103 -7.207  1.00 15.01 ?  156 PHE   B N    1 
ATOM   6615 C CA   . PHE   B 1 156 ? 49.105 -32.570 -7.408  1.00 16.26 ?  156 PHE   B CA   1 
ATOM   6616 C C    . PHE   B 1 156 ? 49.181 -34.072 -7.686  1.00 17.42 ?  156 PHE   B C    1 
ATOM   6617 O O    . PHE   B 1 156 ? 49.883 -34.511 -8.607  1.00 19.81 ?  156 PHE   B O    1 
ATOM   6618 C CB   . PHE   B 1 156 ? 49.939 -32.209 -6.182  1.00 15.94 ?  156 PHE   B CB   1 
ATOM   6619 C CG   . PHE   B 1 156 ? 51.363 -32.669 -6.265  1.00 16.41 ?  156 PHE   B CG   1 
ATOM   6620 C CD1  . PHE   B 1 156 ? 52.216 -32.150 -7.223  1.00 18.24 ?  156 PHE   B CD1  1 
ATOM   6621 C CD2  . PHE   B 1 156 ? 51.852 -33.606 -5.378  1.00 17.58 ?  156 PHE   B CD2  1 
ATOM   6622 C CE1  . PHE   B 1 156 ? 53.536 -32.563 -7.298  1.00 19.41 ?  156 PHE   B CE1  1 
ATOM   6623 C CE2  . PHE   B 1 156 ? 53.173 -34.023 -5.450  1.00 19.02 ?  156 PHE   B CE2  1 
ATOM   6624 C CZ   . PHE   B 1 156 ? 54.006 -33.500 -6.414  1.00 19.40 ?  156 PHE   B CZ   1 
ATOM   6625 H H    . PHE   B 1 156 ? 47.546 -31.875 -6.397  1.00 18.01 ?  156 PHE   B H    1 
ATOM   6626 H HA   . PHE   B 1 156 ? 49.479 -32.105 -8.168  1.00 19.52 ?  156 PHE   B HA   1 
ATOM   6627 H HB2  . PHE   B 1 156 ? 49.941 -31.245 -6.080  1.00 19.12 ?  156 PHE   B HB2  1 
ATOM   6628 H HB3  . PHE   B 1 156 ? 49.541 -32.621 -5.398  1.00 19.12 ?  156 PHE   B HB3  1 
ATOM   6629 H HD1  . PHE   B 1 156 ? 51.898 -31.508 -7.825  1.00 21.89 ?  156 PHE   B HD1  1 
ATOM   6630 H HD2  . PHE   B 1 156 ? 51.287 -33.964 -4.731  1.00 21.10 ?  156 PHE   B HD2  1 
ATOM   6631 H HE1  . PHE   B 1 156 ? 54.102 -32.209 -7.948  1.00 23.29 ?  156 PHE   B HE1  1 
ATOM   6632 H HE2  . PHE   B 1 156 ? 53.494 -34.665 -4.854  1.00 22.82 ?  156 PHE   B HE2  1 
ATOM   6633 H HZ   . PHE   B 1 156 ? 54.892 -33.785 -6.463  1.00 23.28 ?  156 PHE   B HZ   1 
ATOM   6634 N N    . ASP   B 1 157 ? 48.514 -34.882 -6.875  1.00 18.08 ?  157 ASP   B N    1 
ATOM   6635 C CA   . ASP   B 1 157 ? 48.655 -36.333 -6.965  1.00 19.67 ?  157 ASP   B CA   1 
ATOM   6636 C C    . ASP   B 1 157 ? 47.743 -36.895 -8.054  1.00 19.95 ?  157 ASP   B C    1 
ATOM   6637 O O    . ASP   B 1 157 ? 46.518 -36.767 -7.966  1.00 19.30 ?  157 ASP   B O    1 
ATOM   6638 C CB   . ASP   B 1 157 ? 48.293 -36.942 -5.617  1.00 21.56 ?  157 ASP   B CB   1 
ATOM   6639 C CG   . ASP   B 1 157 ? 48.455 -38.450 -5.592  1.00 24.00 ?  157 ASP   B CG   1 
ATOM   6640 O OD1  . ASP   B 1 157 ? 48.803 -39.049 -6.637  1.00 24.39 ?  157 ASP   B OD1  1 
ATOM   6641 O OD2  . ASP   B 1 157 ? 48.242 -39.029 -4.513  1.00 26.15 -1 157 ASP   B OD2  1 
ATOM   6642 H H    . ASP   B 1 157 ? 47.980 -34.620 -6.263  1.00 21.69 ?  157 ASP   B H    1 
ATOM   6643 H HA   . ASP   B 1 157 ? 49.577 -36.566 -7.175  1.00 23.61 ?  157 ASP   B HA   1 
ATOM   6644 H HB2  . ASP   B 1 157 ? 48.858 -36.548 -4.933  1.00 25.87 ?  157 ASP   B HB2  1 
ATOM   6645 H HB3  . ASP   B 1 157 ? 47.362 -36.736 -5.426  1.00 25.87 ?  157 ASP   B HB3  1 
ATOM   6646 N N    A LYS   B 1 158 ? 48.344 -37.514 -9.079  0.80 21.66 ?  158 LYS   B N    1 
ATOM   6647 N N    B LYS   B 1 158 ? 48.343 -37.556 -9.049  0.20 20.63 ?  158 LYS   B N    1 
ATOM   6648 C CA   A LYS   B 1 158 ? 47.571 -38.127 -10.162 0.80 22.81 ?  158 LYS   B CA   1 
ATOM   6649 C CA   B LYS   B 1 158 ? 47.566 -38.119 -10.151 0.20 21.34 ?  158 LYS   B CA   1 
ATOM   6650 C C    A LYS   B 1 158 ? 46.504 -39.085 -9.633  0.80 22.36 ?  158 LYS   B C    1 
ATOM   6651 C C    B LYS   B 1 158 ? 46.509 -39.094 -9.644  0.20 21.20 ?  158 LYS   B C    1 
ATOM   6652 O O    A LYS   B 1 158 ? 45.397 -39.162 -10.182 0.80 22.48 ?  158 LYS   B O    1 
ATOM   6653 O O    B LYS   B 1 158 ? 45.409 -39.175 -10.204 0.20 20.79 ?  158 LYS   B O    1 
ATOM   6654 C CB   A LYS   B 1 158 ? 48.519 -38.852 -11.128 0.80 24.67 ?  158 LYS   B CB   1 
ATOM   6655 C CB   B LYS   B 1 158 ? 48.509 -38.799 -11.149 0.20 22.58 ?  158 LYS   B CB   1 
ATOM   6656 C CG   A LYS   B 1 158 ? 47.836 -39.773 -12.132 0.80 27.02 ?  158 LYS   B CG   1 
ATOM   6657 C CG   B LYS   B 1 158 ? 47.836 -39.709 -12.169 0.20 24.13 ?  158 LYS   B CG   1 
ATOM   6658 C CD   A LYS   B 1 158 ? 46.961 -39.012 -13.107 0.80 29.09 ?  158 LYS   B CD   1 
ATOM   6659 C CD   B LYS   B 1 158 ? 46.928 -38.942 -13.113 0.20 25.64 ?  158 LYS   B CD   1 
ATOM   6660 C CE   A LYS   B 1 158 ? 46.365 -39.948 -14.148 0.80 30.95 ?  158 LYS   B CE   1 
ATOM   6661 C CE   B LYS   B 1 158 ? 46.371 -39.855 -14.196 0.20 26.88 ?  158 LYS   B CE   1 
ATOM   6662 N NZ   A LYS   B 1 158 ? 45.272 -39.302 -14.926 0.80 31.50 ?  158 LYS   B NZ   1 
ATOM   6663 N NZ   B LYS   B 1 158 ? 45.329 -39.183 -15.022 0.20 27.41 ?  158 LYS   B NZ   1 
ATOM   6664 H H    A LYS   B 1 158 ? 49.201 -37.591 -9.171  0.80 26.00 ?  158 LYS   B H    1 
ATOM   6665 H H    B LYS   B 1 158 ? 49.190 -37.704 -9.104  0.20 24.76 ?  158 LYS   B H    1 
ATOM   6666 H HA   A LYS   B 1 158 ? 47.129 -37.425 -10.666 0.80 27.37 ?  158 LYS   B HA   1 
ATOM   6667 H HA   B LYS   B 1 158 ? 47.113 -37.398 -10.613 0.20 25.60 ?  158 LYS   B HA   1 
ATOM   6668 H HB2  A LYS   B 1 158 ? 49.017 -38.187 -11.640 0.80 29.60 ?  158 LYS   B HB2  1 
ATOM   6669 H HB2  B LYS   B 1 158 ? 48.983 -38.110 -11.646 0.20 27.10 ?  158 LYS   B HB2  1 
ATOM   6670 H HB3  A LYS   B 1 158 ? 49.142 -39.389 -10.614 0.80 29.60 ?  158 LYS   B HB3  1 
ATOM   6671 H HB3  B LYS   B 1 158 ? 49.148 -39.337 -10.657 0.20 27.10 ?  158 LYS   B HB3  1 
ATOM   6672 H HG2  A LYS   B 1 158 ? 48.519 -40.234 -12.646 0.80 32.42 ?  158 LYS   B HG2  1 
ATOM   6673 H HG2  B LYS   B 1 158 ? 48.522 -40.138 -12.702 0.20 28.96 ?  158 LYS   B HG2  1 
ATOM   6674 H HG3  A LYS   B 1 158 ? 47.288 -40.425 -11.668 0.80 32.42 ?  158 LYS   B HG3  1 
ATOM   6675 H HG3  B LYS   B 1 158 ? 47.308 -40.383 -11.713 0.20 28.96 ?  158 LYS   B HG3  1 
ATOM   6676 H HD2  A LYS   B 1 158 ? 46.234 -38.587 -12.626 0.80 34.90 ?  158 LYS   B HD2  1 
ATOM   6677 H HD2  B LYS   B 1 158 ? 46.185 -38.570 -12.614 0.20 30.76 ?  158 LYS   B HD2  1 
ATOM   6678 H HD3  A LYS   B 1 158 ? 47.496 -38.345 -13.567 0.80 34.90 ?  158 LYS   B HD3  1 
ATOM   6679 H HD3  B LYS   B 1 158 ? 47.436 -38.234 -13.541 0.20 30.76 ?  158 LYS   B HD3  1 
ATOM   6680 H HE2  A LYS   B 1 158 ? 47.060 -40.215 -14.769 0.80 37.14 ?  158 LYS   B HE2  1 
ATOM   6681 H HE2  B LYS   B 1 158 ? 47.093 -40.128 -14.784 0.20 32.25 ?  158 LYS   B HE2  1 
ATOM   6682 H HE3  A LYS   B 1 158 ? 46.000 -40.727 -13.701 0.80 37.14 ?  158 LYS   B HE3  1 
ATOM   6683 H HE3  B LYS   B 1 158 ? 45.970 -40.634 -13.779 0.20 32.25 ?  158 LYS   B HE3  1 
ATOM   6684 H HZ1  A LYS   B 1 158 ? 44.945 -39.873 -15.524 0.80 37.80 ?  158 LYS   B HZ1  1 
ATOM   6685 H HZ1  B LYS   B 1 158 ? 45.025 -39.743 -15.643 0.20 32.89 ?  158 LYS   B HZ1  1 
ATOM   6686 H HZ2  A LYS   B 1 158 ? 44.617 -39.049 -14.379 0.80 37.80 ?  158 LYS   B HZ2  1 
ATOM   6687 H HZ2  B LYS   B 1 158 ? 44.650 -38.927 -14.506 0.20 32.89 ?  158 LYS   B HZ2  1 
ATOM   6688 H HZ3  A LYS   B 1 158 ? 45.585 -38.585 -15.352 0.80 37.80 ?  158 LYS   B HZ3  1 
ATOM   6689 H HZ3  B LYS   B 1 158 ? 45.674 -38.467 -15.422 0.20 32.89 ?  158 LYS   B HZ3  1 
ATOM   6690 N N    . ASN   B 1 159 ? 46.822 -39.848 -8.587  1.00 21.96 ?  159 ASN   B N    1 
ATOM   6691 C CA   . ASN   B 1 159 ? 45.859 -40.822 -8.071  1.00 23.43 ?  159 ASN   B CA   1 
ATOM   6692 C C    . ASN   B 1 159 ? 44.665 -40.139 -7.392  1.00 21.72 ?  159 ASN   B C    1 
ATOM   6693 O O    . ASN   B 1 159 ? 43.531 -40.634 -7.468  1.00 21.88 ?  159 ASN   B O    1 
ATOM   6694 C CB   . ASN   B 1 159 ? 46.565 -41.801 -7.136  1.00 26.55 ?  159 ASN   B CB   1 
ATOM   6695 C CG   . ASN   B 1 159 ? 47.579 -42.662 -7.862  1.00 29.49 ?  159 ASN   B CG   1 
ATOM   6696 O OD1  . ASN   B 1 159 ? 47.333 -43.113 -8.986  1.00 29.54 ?  159 ASN   B OD1  1 
ATOM   6697 N ND2  . ASN   B 1 159 ? 48.734 -42.885 -7.231  1.00 30.91 ?  159 ASN   B ND2  1 
ATOM   6698 H H    A ASN   B 1 159 ? 47.570 -39.817 -8.171  0.80 26.35 ?  159 ASN   B H    1 
ATOM   6699 H H    B ASN   B 1 159 ? 47.569 -39.813 -8.170  0.20 26.35 ?  159 ASN   B H    1 
ATOM   6700 H HA   . ASN   B 1 159 ? 45.521 -41.334 -8.826  1.00 28.11 ?  159 ASN   B HA   1 
ATOM   6701 H HB2  . ASN   B 1 159 ? 47.032 -41.302 -6.447  1.00 31.86 ?  159 ASN   B HB2  1 
ATOM   6702 H HB3  . ASN   B 1 159 ? 45.909 -42.390 -6.743  1.00 31.86 ?  159 ASN   B HB3  1 
ATOM   6703 H HD21 . ASN   B 1 159 ? 49.348 -43.365 -7.600  1.00 37.09 ?  159 ASN   B HD21 1 
ATOM   6704 H HD22 . ASN   B 1 159 ? 48.869 -42.556 -6.445  1.00 37.09 ?  159 ASN   B HD22 1 
ATOM   6705 N N    . LEU   B 1 160 ? 44.892 -39.011 -6.716  1.00 21.26 ?  160 LEU   B N    1 
ATOM   6706 C CA   . LEU   B 1 160 ? 43.771 -38.265 -6.163  1.00 19.89 ?  160 LEU   B CA   1 
ATOM   6707 C C    . LEU   B 1 160 ? 42.978 -37.595 -7.271  1.00 18.85 ?  160 LEU   B C    1 
ATOM   6708 O O    . LEU   B 1 160 ? 41.741 -37.604 -7.243  1.00 18.64 ?  160 LEU   B O    1 
ATOM   6709 C CB   . LEU   B 1 160 ? 44.257 -37.236 -5.145  1.00 19.36 ?  160 LEU   B CB   1 
ATOM   6710 C CG   . LEU   B 1 160 ? 43.130 -36.333 -4.619  1.00 18.93 ?  160 LEU   B CG   1 
ATOM   6711 C CD1  . LEU   B 1 160 ? 42.010 -37.154 -4.004  1.00 20.15 ?  160 LEU   B CD1  1 
ATOM   6712 C CD2  . LEU   B 1 160 ? 43.669 -35.327 -3.611  1.00 18.75 ?  160 LEU   B CD2  1 
ATOM   6713 H H    . LEU   B 1 160 ? 45.671 -38.676 -6.570  1.00 25.52 ?  160 LEU   B H    1 
ATOM   6714 H HA   . LEU   B 1 160 ? 43.182 -38.887 -5.715  1.00 23.87 ?  160 LEU   B HA   1 
ATOM   6715 H HB2  . LEU   B 1 160 ? 44.647 -37.710 -4.392  1.00 23.24 ?  160 LEU   B HB2  1 
ATOM   6716 H HB3  . LEU   B 1 160 ? 44.930 -36.676 -5.565  1.00 23.24 ?  160 LEU   B HB3  1 
ATOM   6717 H HG   . LEU   B 1 160 ? 42.760 -35.834 -5.363  1.00 22.71 ?  160 LEU   B HG   1 
ATOM   6718 H HD11 . LEU   B 1 160 ? 41.400 -36.561 -3.549  1.00 24.18 ?  160 LEU   B HD11 1 
ATOM   6719 H HD12 . LEU   B 1 160 ? 41.541 -37.637 -4.708  1.00 24.18 ?  160 LEU   B HD12 1 
ATOM   6720 H HD13 . LEU   B 1 160 ? 42.392 -37.789 -3.373  1.00 24.18 ?  160 LEU   B HD13 1 
ATOM   6721 H HD21 . LEU   B 1 160 ? 42.942 -34.753 -3.328  1.00 22.50 ?  160 LEU   B HD21 1 
ATOM   6722 H HD22 . LEU   B 1 160 ? 44.030 -35.808 -2.851  1.00 22.50 ?  160 LEU   B HD22 1 
ATOM   6723 H HD23 . LEU   B 1 160 ? 44.366 -34.800 -4.033  1.00 22.50 ?  160 LEU   B HD23 1 
ATOM   6724 N N    . TYR   B 1 161 ? 43.668 -37.022 -8.263  1.00 19.02 ?  161 TYR   B N    1 
ATOM   6725 C CA   . TYR   B 1 161 ? 42.988 -36.465 -9.428  1.00 19.10 ?  161 TYR   B CA   1 
ATOM   6726 C C    . TYR   B 1 161 ? 42.038 -37.492 -10.028 1.00 19.17 ?  161 TYR   B C    1 
ATOM   6727 O O    . TYR   B 1 161 ? 40.866 -37.200 -10.279 1.00 19.24 ?  161 TYR   B O    1 
ATOM   6728 C CB   . TYR   B 1 161 ? 44.020 -36.002 -10.469 1.00 19.92 ?  161 TYR   B CB   1 
ATOM   6729 C CG   . TYR   B 1 161 ? 43.429 -35.533 -11.785 1.00 20.40 ?  161 TYR   B CG   1 
ATOM   6730 C CD1  . TYR   B 1 161 ? 43.030 -34.209 -11.950 1.00 20.26 ?  161 TYR   B CD1  1 
ATOM   6731 C CD2  . TYR   B 1 161 ? 43.265 -36.404 -12.861 1.00 20.35 ?  161 TYR   B CD2  1 
ATOM   6732 C CE1  . TYR   B 1 161 ? 42.494 -33.766 -13.140 1.00 21.28 ?  161 TYR   B CE1  1 
ATOM   6733 C CE2  . TYR   B 1 161 ? 42.721 -35.968 -14.056 1.00 21.54 ?  161 TYR   B CE2  1 
ATOM   6734 C CZ   . TYR   B 1 161 ? 42.342 -34.646 -14.189 1.00 21.48 ?  161 TYR   B CZ   1 
ATOM   6735 O OH   . TYR   B 1 161 ? 41.798 -34.210 -15.373 1.00 23.62 ?  161 TYR   B OH   1 
ATOM   6736 H H    . TYR   B 1 161 ? 44.526 -36.955 -8.295  1.00 22.83 ?  161 TYR   B H    1 
ATOM   6737 H HA   . TYR   B 1 161 ? 42.467 -35.697 -9.161  1.00 22.92 ?  161 TYR   B HA   1 
ATOM   6738 H HB2  . TYR   B 1 161 ? 44.524 -35.262 -10.099 1.00 23.90 ?  161 TYR   B HB2  1 
ATOM   6739 H HB3  . TYR   B 1 161 ? 44.617 -36.738 -10.670 1.00 23.90 ?  161 TYR   B HB3  1 
ATOM   6740 H HD1  . TYR   B 1 161 ? 43.130 -33.603 -11.251 1.00 24.31 ?  161 TYR   B HD1  1 
ATOM   6741 H HD2  . TYR   B 1 161 ? 43.518 -37.294 -12.780 1.00 24.41 ?  161 TYR   B HD2  1 
ATOM   6742 H HE1  . TYR   B 1 161 ? 42.230 -32.873 -13.234 1.00 25.54 ?  161 TYR   B HE1  1 
ATOM   6743 H HE2  . TYR   B 1 161 ? 42.614 -36.558 -14.770 1.00 25.85 ?  161 TYR   B HE2  1 
ATOM   6744 H HH   . TYR   B 1 161 ? 41.765 -34.840 -15.930 1.00 28.34 ?  161 TYR   B HH   1 
ATOM   6745 N N    . ASP   B 1 162 ? 42.532 -38.712 -10.251 1.00 19.58 ?  162 ASP   B N    1 
ATOM   6746 C CA   . ASP   B 1 162 ? 41.706 -39.750 -10.858 1.00 20.16 ?  162 ASP   B CA   1 
ATOM   6747 C C    . ASP   B 1 162 ? 40.503 -40.085 -9.984  1.00 19.22 ?  162 ASP   B C    1 
ATOM   6748 O O    . ASP   B 1 162 ? 39.394 -40.291 -10.492 1.00 19.96 ?  162 ASP   B O    1 
ATOM   6749 C CB   . ASP   B 1 162 ? 42.542 -41.014 -11.091 1.00 21.41 ?  162 ASP   B CB   1 
ATOM   6750 C CG   . ASP   B 1 162 ? 43.537 -40.870 -12.231 1.00 23.30 ?  162 ASP   B CG   1 
ATOM   6751 O OD1  . ASP   B 1 162 ? 43.402 -39.940 -13.050 1.00 23.54 ?  162 ASP   B OD1  1 
ATOM   6752 O OD2  . ASP   B 1 162 ? 44.441 -41.727 -12.331 1.00 24.82 -1 162 ASP   B OD2  1 
ATOM   6753 H H    . ASP   B 1 162 ? 43.337 -38.956 -10.071 1.00 23.50 ?  162 ASP   B H    1 
ATOM   6754 H HA   . ASP   B 1 162 ? 41.382 -39.447 -11.718 1.00 24.19 ?  162 ASP   B HA   1 
ATOM   6755 H HB2  . ASP   B 1 162 ? 43.045 -41.218 -10.288 1.00 25.70 ?  162 ASP   B HB2  1 
ATOM   6756 H HB3  . ASP   B 1 162 ? 41.951 -41.752 -11.309 1.00 25.70 ?  162 ASP   B HB3  1 
ATOM   6757 N N    A LYS   B 1 163 ? 40.706 -40.164 -8.667  0.80 18.65 ?  163 LYS   B N    1 
ATOM   6758 N N    B LYS   B 1 163 ? 40.700 -40.143 -8.665  0.20 19.61 ?  163 LYS   B N    1 
ATOM   6759 C CA   A LYS   B 1 163 ? 39.586 -40.435 -7.775  0.80 19.16 ?  163 LYS   B CA   1 
ATOM   6760 C CA   B LYS   B 1 163 ? 39.585 -40.432 -7.769  0.20 20.35 ?  163 LYS   B CA   1 
ATOM   6761 C C    A LYS   B 1 163 ? 38.548 -39.320 -7.843  0.80 17.94 ?  163 LYS   B C    1 
ATOM   6762 C C    B LYS   B 1 163 ? 38.549 -39.314 -7.801  0.20 18.51 ?  163 LYS   B C    1 
ATOM   6763 O O    A LYS   B 1 163 ? 37.338 -39.587 -7.855  0.80 18.67 ?  163 LYS   B O    1 
ATOM   6764 O O    B LYS   B 1 163 ? 37.341 -39.575 -7.743  0.20 18.54 ?  163 LYS   B O    1 
ATOM   6765 C CB   A LYS   B 1 163 ? 40.078 -40.611 -6.341  0.80 22.01 ?  163 LYS   B CB   1 
ATOM   6766 C CB   B LYS   B 1 163 ? 40.098 -40.640 -6.346  0.20 23.19 ?  163 LYS   B CB   1 
ATOM   6767 C CG   A LYS   B 1 163 ? 39.000 -41.136 -5.412  0.80 27.11 ?  163 LYS   B CG   1 
ATOM   6768 C CG   B LYS   B 1 163 ? 39.030 -41.127 -5.384  0.20 26.33 ?  163 LYS   B CG   1 
ATOM   6769 C CD   A LYS   B 1 163 ? 39.441 -41.183 -3.961  0.80 31.91 ?  163 LYS   B CD   1 
ATOM   6770 C CD   B LYS   B 1 163 ? 39.545 -41.223 -3.960  0.20 29.60 ?  163 LYS   B CD   1 
ATOM   6771 C CE   A LYS   B 1 163 ? 38.380 -41.868 -3.109  0.80 35.28 ?  163 LYS   B CE   1 
ATOM   6772 C CE   B LYS   B 1 163 ? 38.503 -41.856 -3.050  0.20 32.07 ?  163 LYS   B CE   1 
ATOM   6773 N NZ   A LYS   B 1 163 ? 38.535 -41.573 -1.658  0.80 37.14 ?  163 LYS   B NZ   1 
ATOM   6774 N NZ   B LYS   B 1 163 ? 38.801 -41.631 -1.609  0.20 33.09 ?  163 LYS   B NZ   1 
ATOM   6775 H H    A LYS   B 1 163 ? 41.471 -40.076 -8.280  0.80 22.38 ?  163 LYS   B H    1 
ATOM   6776 H H    B LYS   B 1 163 ? 41.459 -40.024 -8.274  0.20 23.53 ?  163 LYS   B H    1 
ATOM   6777 H HA   A LYS   B 1 163 ? 39.161 -41.260 -8.050  0.80 22.99 ?  163 LYS   B HA   1 
ATOM   6778 H HA   B LYS   B 1 163 ? 39.154 -41.250 -8.058  0.20 24.43 ?  163 LYS   B HA   1 
ATOM   6779 H HB2  A LYS   B 1 163 ? 40.815 -41.244 -6.334  0.80 26.41 ?  163 LYS   B HB2  1 
ATOM   6780 H HB2  B LYS   B 1 163 ? 40.809 -41.301 -6.361  0.20 27.83 ?  163 LYS   B HB2  1 
ATOM   6781 H HB3  A LYS   B 1 163 ? 40.376 -39.754 -6.000  0.80 26.41 ?  163 LYS   B HB3  1 
ATOM   6782 H HB3  B LYS   B 1 163 ? 40.441 -39.797 -6.009  0.20 27.83 ?  163 LYS   B HB3  1 
ATOM   6783 H HG2  A LYS   B 1 163 ? 38.222 -40.561 -5.468  0.80 32.53 ?  163 LYS   B HG2  1 
ATOM   6784 H HG2  B LYS   B 1 163 ? 38.284 -40.507 -5.393  0.20 31.60 ?  163 LYS   B HG2  1 
ATOM   6785 H HG3  A LYS   B 1 163 ? 38.762 -42.039 -5.682  0.80 32.53 ?  163 LYS   B HG3  1 
ATOM   6786 H HG3  B LYS   B 1 163 ? 38.734 -42.009 -5.659  0.20 31.60 ?  163 LYS   B HG3  1 
ATOM   6787 H HD2  A LYS   B 1 163 ? 40.266 -41.689 -3.889  0.80 38.29 ?  163 LYS   B HD2  1 
ATOM   6788 H HD2  B LYS   B 1 163 ? 40.343 -41.775 -3.942  0.20 35.52 ?  163 LYS   B HD2  1 
ATOM   6789 H HD3  A LYS   B 1 163 ? 39.565 -40.280 -3.631  0.80 38.29 ?  163 LYS   B HD3  1 
ATOM   6790 H HD3  B LYS   B 1 163 ? 39.741 -40.333 -3.627  0.20 35.52 ?  163 LYS   B HD3  1 
ATOM   6791 H HE2  A LYS   B 1 163 ? 37.501 -41.569 -3.390  0.80 42.34 ?  163 LYS   B HE2  1 
ATOM   6792 H HE2  B LYS   B 1 163 ? 37.633 -41.474 -3.245  0.20 38.49 ?  163 LYS   B HE2  1 
ATOM   6793 H HE3  A LYS   B 1 163 ? 38.454 -42.828 -3.229  0.80 42.34 ?  163 LYS   B HE3  1 
ATOM   6794 H HE3  B LYS   B 1 163 ? 38.486 -42.813 -3.209  0.20 38.49 ?  163 LYS   B HE3  1 
ATOM   6795 H HZ1  A LYS   B 1 163 ? 37.898 -41.988 -1.195  0.80 44.57 ?  163 LYS   B HZ1  1 
ATOM   6796 H HZ1  B LYS   B 1 163 ? 38.173 -42.013 -1.106  0.20 39.70 ?  163 LYS   B HZ1  1 
ATOM   6797 H HZ2  A LYS   B 1 163 ? 39.329 -41.854 -1.375  0.80 44.57 ?  163 LYS   B HZ2  1 
ATOM   6798 H HZ2  B LYS   B 1 163 ? 39.591 -41.984 -1.403  0.20 39.70 ?  163 LYS   B HZ2  1 
ATOM   6799 H HZ3  A LYS   B 1 163 ? 38.469 -40.697 -1.518  0.80 44.57 ?  163 LYS   B HZ3  1 
ATOM   6800 H HZ3  B LYS   B 1 163 ? 38.819 -40.758 -1.435  0.20 39.70 ?  163 LYS   B HZ3  1 
ATOM   6801 N N    . LEU   B 1 164 ? 39.006 -38.064 -7.885  1.00 17.06 ?  164 LEU   B N    1 
ATOM   6802 C CA   . LEU   B 1 164 ? 38.093 -36.926 -7.937  1.00 16.57 ?  164 LEU   B CA   1 
ATOM   6803 C C    . LEU   B 1 164 ? 37.304 -36.905 -9.241  1.00 17.01 ?  164 LEU   B C    1 
ATOM   6804 O O    . LEU   B 1 164 ? 36.082 -36.690 -9.237  1.00 18.35 ?  164 LEU   B O    1 
ATOM   6805 C CB   . LEU   B 1 164 ? 38.896 -35.632 -7.785  1.00 15.91 ?  164 LEU   B CB   1 
ATOM   6806 C CG   . LEU   B 1 164 ? 39.439 -35.332 -6.391  1.00 16.38 ?  164 LEU   B CG   1 
ATOM   6807 C CD1  . LEU   B 1 164 ? 40.506 -34.248 -6.467  1.00 16.20 ?  164 LEU   B CD1  1 
ATOM   6808 C CD2  . LEU   B 1 164 ? 38.334 -34.919 -5.441  1.00 18.14 ?  164 LEU   B CD2  1 
ATOM   6809 H H    A LEU   B 1 164 ? 39.845 -37.847 -7.877  0.80 20.47 ?  164 LEU   B H    1 
ATOM   6810 H H    B LEU   B 1 164 ? 39.846 -37.850 -7.914  0.20 20.47 ?  164 LEU   B H    1 
ATOM   6811 H HA   . LEU   B 1 164 ? 37.470 -36.984 -7.206  1.00 19.88 ?  164 LEU   B HA   1 
ATOM   6812 H HB2  . LEU   B 1 164 ? 39.661 -35.671 -8.389  1.00 19.09 ?  164 LEU   B HB2  1 
ATOM   6813 H HB3  . LEU   B 1 164 ? 38.331 -34.889 -8.037  1.00 19.09 ?  164 LEU   B HB3  1 
ATOM   6814 H HG   . LEU   B 1 164 ? 39.861 -36.135 -6.038  1.00 19.65 ?  164 LEU   B HG   1 
ATOM   6815 H HD11 . LEU   B 1 164 ? 40.837 -34.064 -5.572  1.00 19.44 ?  164 LEU   B HD11 1 
ATOM   6816 H HD12 . LEU   B 1 164 ? 41.237 -34.554 -7.030  1.00 19.44 ?  164 LEU   B HD12 1 
ATOM   6817 H HD13 . LEU   B 1 164 ? 40.114 -33.444 -6.844  1.00 19.44 ?  164 LEU   B HD13 1 
ATOM   6818 H HD21 . LEU   B 1 164 ? 38.723 -34.682 -4.586  1.00 21.77 ?  164 LEU   B HD21 1 
ATOM   6819 H HD22 . LEU   B 1 164 ? 37.868 -34.156 -5.817  1.00 21.77 ?  164 LEU   B HD22 1 
ATOM   6820 H HD23 . LEU   B 1 164 ? 37.719 -35.661 -5.332  1.00 21.77 ?  164 LEU   B HD23 1 
ATOM   6821 N N    . VAL   B 1 165 ? 37.990 -37.092 -10.371 1.00 18.52 ?  165 VAL   B N    1 
ATOM   6822 C CA   . VAL   B 1 165 ? 37.323 -37.031 -11.668 1.00 20.60 ?  165 VAL   B CA   1 
ATOM   6823 C C    . VAL   B 1 165 ? 36.384 -38.217 -11.834 1.00 22.80 ?  165 VAL   B C    1 
ATOM   6824 O O    . VAL   B 1 165 ? 35.213 -38.065 -12.207 1.00 24.24 ?  165 VAL   B O    1 
ATOM   6825 C CB   . VAL   B 1 165 ? 38.359 -36.974 -12.807 1.00 21.93 ?  165 VAL   B CB   1 
ATOM   6826 C CG1  . VAL   B 1 165 ? 37.670 -37.089 -14.147 1.00 23.24 ?  165 VAL   B CG1  1 
ATOM   6827 C CG2  . VAL   B 1 165 ? 39.172 -35.687 -12.738 1.00 21.70 ?  165 VAL   B CG2  1 
ATOM   6828 H H    . VAL   B 1 165 ? 38.843 -37.247 -10.414 1.00 22.23 ?  165 VAL   B H    1 
ATOM   6829 H HA   . VAL   B 1 165 ? 36.800 -36.216 -11.712 1.00 24.73 ?  165 VAL   B HA   1 
ATOM   6830 H HB   . VAL   B 1 165 ? 38.980 -37.713 -12.717 1.00 26.31 ?  165 VAL   B HB   1 
ATOM   6831 H HG11 . VAL   B 1 165 ? 38.265 -36.774 -14.841 1.00 27.89 ?  165 VAL   B HG11 1 
ATOM   6832 H HG12 . VAL   B 1 165 ? 37.449 -38.021 -14.303 1.00 27.89 ?  165 VAL   B HG12 1 
ATOM   6833 H HG13 . VAL   B 1 165 ? 36.862 -36.555 -14.133 1.00 27.89 ?  165 VAL   B HG13 1 
ATOM   6834 H HG21 . VAL   B 1 165 ? 39.805 -35.669 -13.477 1.00 26.04 ?  165 VAL   B HG21 1 
ATOM   6835 H HG22 . VAL   B 1 165 ? 38.570 -34.928 -12.806 1.00 26.04 ?  165 VAL   B HG22 1 
ATOM   6836 H HG23 . VAL   B 1 165 ? 39.650 -35.655 -11.896 1.00 26.04 ?  165 VAL   B HG23 1 
ATOM   6837 N N    . SER   B 1 166 ? 36.893 -39.420 -11.559 1.00 23.80 ?  166 SER   B N    1 
ATOM   6838 C CA   . SER   B 1 166 ? 36.135 -40.630 -11.840 1.00 25.37 ?  166 SER   B CA   1 
ATOM   6839 C C    . SER   B 1 166 ? 34.878 -40.712 -10.988 1.00 25.68 ?  166 SER   B C    1 
ATOM   6840 O O    . SER   B 1 166 ? 33.908 -41.342 -11.401 1.00 27.30 ?  166 SER   B O    1 
ATOM   6841 C CB   . SER   B 1 166 ? 37.007 -41.883 -11.668 1.00 25.96 ?  166 SER   B CB   1 
ATOM   6842 O OG   . SER   B 1 166 ? 37.366 -42.101 -10.314 1.00 25.63 ?  166 SER   B OG   1 
ATOM   6843 H H    . SER   B 1 166 ? 37.677 -39.557 -11.222 1.00 28.56 ?  166 SER   B H    1 
ATOM   6844 H HA   . SER   B 1 166 ? 35.858 -40.608 -12.771 1.00 30.44 ?  166 SER   B HA   1 
ATOM   6845 H HB2  . SER   B 1 166 ? 36.516 -42.654 -11.989 1.00 31.15 ?  166 SER   B HB2  1 
ATOM   6846 H HB3  . SER   B 1 166 ? 37.821 -41.774 -12.189 1.00 31.15 ?  166 SER   B HB3  1 
ATOM   6847 H HG   . SER   B 1 166 ? 37.794 -41.438 -10.023 1.00 30.76 ?  166 SER   B HG   1 
ATOM   6848 N N    . SER   B 1 167 ? 34.861 -40.087 -9.815  1.00 23.77 ?  167 SER   B N    1 
ATOM   6849 C CA   . SER   B 1 167 ? 33.707 -40.141 -8.924  1.00 24.09 ?  167 SER   B CA   1 
ATOM   6850 C C    . SER   B 1 167 ? 32.800 -38.911 -9.010  1.00 22.95 ?  167 SER   B C    1 
ATOM   6851 O O    . SER   B 1 167 ? 31.721 -38.919 -8.408  1.00 23.16 ?  167 SER   B O    1 
ATOM   6852 C CB   . SER   B 1 167 ? 34.166 -40.333 -7.472  1.00 24.01 ?  167 SER   B CB   1 
ATOM   6853 O OG   . SER   B 1 167 ? 34.842 -39.171 -7.003  1.00 23.75 ?  167 SER   B OG   1 
ATOM   6854 H H    . SER   B 1 167 ? 35.513 -39.634 -9.511  1.00 28.53 ?  167 SER   B H    1 
ATOM   6855 H HA   . SER   B 1 167 ? 33.169 -40.918 -9.161  1.00 28.91 ?  167 SER   B HA   1 
ATOM   6856 H HB2  . SER   B 1 167 ? 33.386 -40.498 -6.915  1.00 28.82 ?  167 SER   B HB2  1 
ATOM   6857 H HB3  . SER   B 1 167 ? 34.764 -41.100 -7.428  1.00 28.82 ?  167 SER   B HB3  1 
ATOM   6858 H HG   . SER   B 1 167 ? 35.523 -39.033 -7.472  1.00 28.50 ?  167 SER   B HG   1 
ATOM   6859 N N    . PHE   B 1 168 ? 33.190 -37.863 -9.742  1.00 22.32 ?  168 PHE   B N    1 
ATOM   6860 C CA   . PHE   B 1 168 ? 32.352 -36.665 -9.818  1.00 20.90 ?  168 PHE   B CA   1 
ATOM   6861 C C    . PHE   B 1 168 ? 31.056 -36.947 -10.575 1.00 17.97 ?  168 PHE   B C    1 
ATOM   6862 O O    . PHE   B 1 168 ? 29.992 -36.380 -10.255 1.00 17.65 ?  168 PHE   B O    1 
ATOM   6863 C CB   . PHE   B 1 168 ? 33.124 -35.527 -10.483 1.00 21.91 ?  168 PHE   B CB   1 
ATOM   6864 C CG   . PHE   B 1 168 ? 32.313 -34.287 -10.666 1.00 21.71 ?  168 PHE   B CG   1 
ATOM   6865 C CD1  . PHE   B 1 168 ? 31.935 -33.530 -9.566  1.00 23.11 ?  168 PHE   B CD1  1 
ATOM   6866 C CD2  . PHE   B 1 168 ? 31.903 -33.883 -11.924 1.00 21.20 ?  168 PHE   B CD2  1 
ATOM   6867 C CE1  . PHE   B 1 168 ? 31.169 -32.390 -9.713  1.00 22.71 ?  168 PHE   B CE1  1 
ATOM   6868 C CE2  . PHE   B 1 168 ? 31.152 -32.724 -12.086 1.00 21.86 ?  168 PHE   B CE2  1 
ATOM   6869 C CZ   . PHE   B 1 168 ? 30.774 -31.980 -10.974 1.00 22.31 ?  168 PHE   B CZ   1 
ATOM   6870 H H    . PHE   B 1 168 ? 33.915 -37.827 -10.197 1.00 26.79 ?  168 PHE   B H    1 
ATOM   6871 H HA   . PHE   B 1 168 ? 32.114 -36.390 -8.922  1.00 25.09 ?  168 PHE   B HA   1 
ATOM   6872 H HB2  . PHE   B 1 168 ? 33.885 -35.305 -9.928  1.00 26.29 ?  168 PHE   B HB2  1 
ATOM   6873 H HB3  . PHE   B 1 168 ? 33.421 -35.818 -11.357 1.00 26.29 ?  168 PHE   B HB3  1 
ATOM   6874 H HD1  . PHE   B 1 168 ? 32.190 -33.806 -8.716  1.00 27.73 ?  168 PHE   B HD1  1 
ATOM   6875 H HD2  . PHE   B 1 168 ? 32.151 -34.372 -12.671 1.00 25.44 ?  168 PHE   B HD2  1 
ATOM   6876 H HE1  . PHE   B 1 168 ? 30.921 -31.898 -8.966  1.00 27.25 ?  168 PHE   B HE1  1 
ATOM   6877 H HE2  . PHE   B 1 168 ? 30.877 -32.458 -12.936 1.00 26.23 ?  168 PHE   B HE2  1 
ATOM   6878 H HZ   . PHE   B 1 168 ? 30.257 -31.212 -11.079 1.00 26.78 ?  168 PHE   B HZ   1 
ATOM   6879 N N    . LEU   B 1 169 ? 31.133 -37.795 -11.597 1.00 18.32 ?  169 LEU   B N    1 
ATOM   6880 C CA   . LEU   B 1 169 ? 29.974 -38.142 -12.413 1.00 20.56 ?  169 LEU   B CA   1 
ATOM   6881 C C    . LEU   B 1 169 ? 29.983 -39.582 -12.907 1.00 23.97 ?  169 LEU   B C    1 
ATOM   6882 O O    . LEU   B 1 169 ? 29.095 -40.004 -13.652 1.00 26.39 ?  169 LEU   B O    1 
ATOM   6883 C CB   . LEU   B 1 169 ? 29.892 -37.220 -13.627 1.00 22.80 ?  169 LEU   B CB   1 
ATOM   6884 C CG   . LEU   B 1 169 ? 28.632 -36.364 -13.748 1.00 26.00 ?  169 LEU   B CG   1 
ATOM   6885 C CD1  . LEU   B 1 169 ? 28.565 -35.774 -15.136 1.00 27.03 ?  169 LEU   B CD1  1 
ATOM   6886 C CD2  . LEU   B 1 169 ? 27.368 -37.155 -13.435 1.00 25.76 ?  169 LEU   B CD2  1 
ATOM   6887 O OXT  . LEU   B 1 169 ? 30.877 -40.352 -12.592 1.00 25.00 -1 169 LEU   B OXT  1 
ATOM   6888 H H    . LEU   B 1 169 ? 31.860 -38.180 -11.851 1.00 21.99 ?  169 LEU   B H    1 
ATOM   6889 H HA   . LEU   B 1 169 ? 29.184 -38.014 -11.876 1.00 24.67 ?  169 LEU   B HA   1 
ATOM   6890 H HB2  . LEU   B 1 169 ? 30.648 -36.614 -13.607 1.00 27.36 ?  169 LEU   B HB2  1 
ATOM   6891 H HB3  . LEU   B 1 169 ? 29.942 -37.765 -14.430 1.00 27.36 ?  169 LEU   B HB3  1 
ATOM   6892 H HG   . LEU   B 1 169 ? 28.688 -35.631 -13.116 1.00 31.20 ?  169 LEU   B HG   1 
ATOM   6893 H HD11 . LEU   B 1 169 ? 27.783 -35.204 -15.197 1.00 32.43 ?  169 LEU   B HD11 1 
ATOM   6894 H HD12 . LEU   B 1 169 ? 29.368 -35.255 -15.294 1.00 32.43 ?  169 LEU   B HD12 1 
ATOM   6895 H HD13 . LEU   B 1 169 ? 28.502 -36.495 -15.781 1.00 32.43 ?  169 LEU   B HD13 1 
ATOM   6896 H HD21 . LEU   B 1 169 ? 26.614 -36.739 -13.876 1.00 30.91 ?  169 LEU   B HD21 1 
ATOM   6897 H HD22 . LEU   B 1 169 ? 27.479 -38.066 -13.756 1.00 30.91 ?  169 LEU   B HD22 1 
ATOM   6898 H HD23 . LEU   B 1 169 ? 27.231 -37.161 -12.475 1.00 30.91 ?  169 LEU   B HD23 1 
HETATM 6899 C C1   T TFA   C 2 .   ? 12.143 -1.222  1.404   0.30 10.70 ?  201 TFA   A C1   1 
HETATM 6900 C C2   T TFA   C 2 .   ? 12.762 -1.722  0.080   0.30 12.96 ?  201 TFA   A C2   1 
HETATM 6901 O O    T TFA   C 2 .   ? 12.836 -1.480  2.389   0.30 9.55  ?  201 TFA   A O    1 
HETATM 6902 F F1   T TFA   C 2 .   ? 12.758 -3.064  0.075   0.30 14.60 ?  201 TFA   A F1   1 
HETATM 6903 F F2   T TFA   C 2 .   ? 12.082 -1.337  -1.009  0.30 13.05 ?  201 TFA   A F2   1 
HETATM 6904 F F3   T TFA   C 2 .   ? 14.017 -1.298  -0.095  0.30 14.48 ?  201 TFA   A F3   1 
HETATM 6905 O OXT  T TFA   C 2 .   ? 11.070 -0.638  1.296   0.30 10.86 ?  201 TFA   A OXT  1 
HETATM 6906 N N2   B A1A98 D 3 .   ? 14.771 -0.227  4.357   0.20 13.06 ?  202 A1A98 A N2   1 
HETATM 6907 C C3   B A1A98 D 3 .   ? 15.031 0.799   3.481   0.20 13.72 ?  202 A1A98 A C3   1 
HETATM 6908 C C6   B A1A98 D 3 .   ? 15.317 2.121   4.023   0.20 12.57 ?  202 A1A98 A C6   1 
HETATM 6909 C C9   B A1A98 D 3 .   ? 14.301 -0.208  -0.153  0.20 17.45 ?  202 A1A98 A C9   1 
HETATM 6910 C C12  B A1A98 D 3 .   ? 12.812 -0.670  1.752   0.20 17.27 ?  202 A1A98 A C12  1 
HETATM 6911 C C1   B A1A98 D 3 .   ? 15.064 -1.966  1.603   0.20 17.26 ?  202 A1A98 A C1   1 
HETATM 6912 C C10  B A1A98 D 3 .   ? 12.854 -0.061  -0.649  0.20 17.60 ?  202 A1A98 A C10  1 
HETATM 6913 C C11  B A1A98 D 3 .   ? 11.935 -0.232  0.560   0.20 17.65 ?  202 A1A98 A C11  1 
HETATM 6914 C C2   B A1A98 D 3 .   ? 14.331 -0.559  1.353   0.20 16.86 ?  202 A1A98 A C2   1 
HETATM 6915 C C4   B A1A98 D 3 .   ? 14.782 0.023   5.705   0.20 12.79 ?  202 A1A98 A C4   1 
HETATM 6916 C C5   B A1A98 D 3 .   ? 15.287 2.195   5.449   0.20 12.07 ?  202 A1A98 A C5   1 
HETATM 6917 C C7   B A1A98 D 3 .   ? 15.647 3.485   3.625   0.20 12.20 ?  202 A1A98 A C7   1 
HETATM 6918 C C8   B A1A98 D 3 .   ? 15.788 4.272   4.763   0.20 11.23 ?  202 A1A98 A C8   1 
HETATM 6919 N N1   B A1A98 D 3 .   ? 15.030 0.531   2.106   0.20 15.36 ?  202 A1A98 A N1   1 
HETATM 6920 N N3   B A1A98 D 3 .   ? 15.020 1.187   6.303   0.20 12.55 ?  202 A1A98 A N3   1 
HETATM 6921 N N4   B A1A98 D 3 .   ? 15.570 3.469   5.874   0.20 10.97 ?  202 A1A98 A N4   1 
HETATM 6922 O O1   B A1A98 D 3 .   ? 14.938 -2.431  2.921   0.20 17.52 ?  202 A1A98 A O1   1 
HETATM 6923 H H10  B A1A98 D 3 .   ? 14.907 0.701   -0.340  0.20 20.94 ?  202 A1A98 A H10  1 
HETATM 6924 H H9   B A1A98 D 3 .   ? 14.833 -0.983  -0.752  0.20 20.94 ?  202 A1A98 A H9   1 
HETATM 6925 H H16  B A1A98 D 3 .   ? 12.536 -1.703  2.064   0.20 20.73 ?  202 A1A98 A H16  1 
HETATM 6926 H H15  B A1A98 D 3 .   ? 12.541 -0.077  2.648   0.20 20.73 ?  202 A1A98 A H15  1 
HETATM 6927 H H2   B A1A98 D 3 .   ? 16.105 -1.856  1.422   0.20 20.71 ?  202 A1A98 A H2   1 
HETATM 6928 H H3   B A1A98 D 3 .   ? 14.733 -2.724  0.845   0.20 20.71 ?  202 A1A98 A H3   1 
HETATM 6929 H H11  B A1A98 D 3 .   ? 12.622 -0.790  -1.447  0.20 21.12 ?  202 A1A98 A H11  1 
HETATM 6930 H H12  B A1A98 D 3 .   ? 12.687 0.919   -1.171  0.20 21.12 ?  202 A1A98 A H12  1 
HETATM 6931 H H13  B A1A98 D 3 .   ? 11.104 -0.942  0.367   0.20 21.18 ?  202 A1A98 A H13  1 
HETATM 6932 H H14  B A1A98 D 3 .   ? 11.366 0.697   0.788   0.20 21.18 ?  202 A1A98 A H14  1 
HETATM 6933 H H5   B A1A98 D 3 .   ? 14.565 -0.797  6.415   0.20 15.35 ?  202 A1A98 A H5   1 
HETATM 6934 H H6   B A1A98 D 3 .   ? 15.771 3.902   2.640   0.20 14.64 ?  202 A1A98 A H6   1 
HETATM 6935 H H7   B A1A98 D 3 .   ? 16.012 5.314   4.972   0.20 13.47 ?  202 A1A98 A H7   1 
HETATM 6936 H H4   B A1A98 D 3 .   ? 15.579 1.168   1.532   0.20 18.43 ?  202 A1A98 A H4   1 
HETATM 6937 H H8   B A1A98 D 3 .   ? 15.601 3.802   6.863   0.20 13.17 ?  202 A1A98 A H8   1 
HETATM 6938 H H1   B A1A98 D 3 .   ? 14.037 -2.676  3.103   0.20 21.02 ?  202 A1A98 A H1   1 
HETATM 6939 O O    . HOH   E 4 .   ? 4.686  3.698   0.420   1.00 24.49 ?  301 HOH   A O    1 
HETATM 6940 O O    A HOH   E 4 .   ? 14.764 -4.521  20.398  0.80 45.09 ?  302 HOH   A O    1 
HETATM 6941 O O    . HOH   E 4 .   ? 11.954 0.354   14.702  1.00 34.13 ?  303 HOH   A O    1 
HETATM 6942 O O    . HOH   E 4 .   ? 15.092 -12.137 18.617  1.00 46.18 ?  304 HOH   A O    1 
HETATM 6943 O O    . HOH   E 4 .   ? 26.887 11.475  1.621   1.00 18.51 ?  305 HOH   A O    1 
HETATM 6944 O O    . HOH   E 4 .   ? 17.014 -17.884 15.004  1.00 30.48 ?  306 HOH   A O    1 
HETATM 6945 O O    . HOH   E 4 .   ? 17.628 -1.709  0.119   1.00 31.97 ?  307 HOH   A O    1 
HETATM 6946 O O    . HOH   E 4 .   ? 16.962 -19.204 4.879   1.00 18.01 ?  308 HOH   A O    1 
HETATM 6947 O O    A HOH   E 4 .   ? -0.481 -3.035  3.058   0.80 36.55 ?  309 HOH   A O    1 
HETATM 6948 O O    . HOH   E 4 .   ? 34.368 -1.814  12.508  1.00 39.91 ?  310 HOH   A O    1 
HETATM 6949 O O    . HOH   E 4 .   ? 22.700 12.510  1.561   1.00 16.57 ?  311 HOH   A O    1 
HETATM 6950 O O    . HOH   E 4 .   ? 28.632 -10.595 -13.991 1.00 46.12 ?  312 HOH   A O    1 
HETATM 6951 O O    . HOH   E 4 .   ? 18.706 -2.385  -16.446 1.00 48.89 ?  313 HOH   A O    1 
HETATM 6952 O O    . HOH   E 4 .   ? 28.040 -6.229  19.636  1.00 44.22 ?  314 HOH   A O    1 
HETATM 6953 O O    . HOH   E 4 .   ? 10.410 -22.251 -1.211  1.00 48.05 ?  315 HOH   A O    1 
HETATM 6954 O O    . HOH   E 4 .   ? 18.902 -21.944 7.080   1.00 38.35 ?  316 HOH   A O    1 
HETATM 6955 O O    . HOH   E 4 .   ? 9.891  -21.313 5.578   1.00 22.52 ?  317 HOH   A O    1 
HETATM 6956 O O    . HOH   E 4 .   ? 14.620 -13.852 16.657  1.00 30.78 ?  318 HOH   A O    1 
HETATM 6957 O O    . HOH   E 4 .   ? 30.203 -13.319 -8.443  1.00 28.15 ?  319 HOH   A O    1 
HETATM 6958 O O    . HOH   E 4 .   ? 19.478 -10.931 24.094  1.00 82.54 ?  320 HOH   A O    1 
HETATM 6959 O O    . HOH   E 4 .   ? 9.067  -10.025 19.313  1.00 43.18 ?  321 HOH   A O    1 
HETATM 6960 O O    . HOH   E 4 .   ? 13.977 -22.993 7.379   1.00 20.77 ?  322 HOH   A O    1 
HETATM 6961 O O    . HOH   E 4 .   ? 6.797  -7.927  11.723  1.00 19.82 ?  323 HOH   A O    1 
HETATM 6962 O O    . HOH   E 4 .   ? 28.964 0.534   -9.693  1.00 22.87 ?  324 HOH   A O    1 
HETATM 6963 O O    . HOH   E 4 .   ? 0.753  -4.207  0.001   1.00 31.30 ?  325 HOH   A O    1 
HETATM 6964 O O    . HOH   E 4 .   ? 11.766 -10.900 -10.162 1.00 48.31 ?  326 HOH   A O    1 
HETATM 6965 O O    . HOH   E 4 .   ? 42.423 10.564  5.058   1.00 21.17 ?  327 HOH   A O    1 
HETATM 6966 O O    . HOH   E 4 .   ? 38.204 10.211  7.135   1.00 45.22 ?  328 HOH   A O    1 
HETATM 6967 O O    . HOH   E 4 .   ? 14.540 -0.590  -12.281 1.00 24.18 ?  329 HOH   A O    1 
HETATM 6968 O O    . HOH   E 4 .   ? 19.960 -12.517 -8.932  1.00 27.53 ?  330 HOH   A O    1 
HETATM 6969 O O    . HOH   E 4 .   ? 36.140 -5.091  -0.501  1.00 31.56 ?  331 HOH   A O    1 
HETATM 6970 O O    . HOH   E 4 .   ? 14.170 -4.584  -11.975 1.00 33.45 ?  332 HOH   A O    1 
HETATM 6971 O O    A HOH   E 4 .   ? 14.270 0.625   6.767   0.80 19.48 ?  333 HOH   A O    1 
HETATM 6972 O O    . HOH   E 4 .   ? 15.219 -8.069  -9.946  1.00 25.25 ?  334 HOH   A O    1 
HETATM 6973 O O    A HOH   E 4 .   ? 14.631 -3.610  3.073   0.80 17.79 ?  335 HOH   A O    1 
HETATM 6974 O O    . HOH   E 4 .   ? 22.221 5.416   18.929  1.00 41.46 ?  336 HOH   A O    1 
HETATM 6975 O O    . HOH   E 4 .   ? 37.507 2.849   10.272  1.00 26.47 ?  337 HOH   A O    1 
HETATM 6976 O O    . HOH   E 4 .   ? 27.485 -6.055  -13.960 1.00 39.32 ?  338 HOH   A O    1 
HETATM 6977 O O    . HOH   E 4 .   ? 44.313 7.145   6.416   1.00 28.03 ?  339 HOH   A O    1 
HETATM 6978 O O    . HOH   E 4 .   ? 28.307 -0.131  -13.414 1.00 39.35 ?  340 HOH   A O    1 
HETATM 6979 O O    . HOH   E 4 .   ? 3.580  -9.260  9.756   1.00 29.50 ?  341 HOH   A O    1 
HETATM 6980 O O    . HOH   E 4 .   ? 7.899  -12.448 -0.991  1.00 22.05 ?  342 HOH   A O    1 
HETATM 6981 O O    . HOH   E 4 .   ? 20.667 -19.792 -5.008  1.00 27.71 ?  343 HOH   A O    1 
HETATM 6982 O O    . HOH   E 4 .   ? 14.991 4.032   17.697  1.00 41.34 ?  344 HOH   A O    1 
HETATM 6983 O O    . HOH   E 4 .   ? -0.664 -8.346  2.129   1.00 40.65 ?  345 HOH   A O    1 
HETATM 6984 O O    . HOH   E 4 .   ? 31.021 -18.061 7.824   1.00 20.07 ?  346 HOH   A O    1 
HETATM 6985 O O    . HOH   E 4 .   ? 21.293 3.036   -0.259  1.00 15.44 ?  347 HOH   A O    1 
HETATM 6986 O O    . HOH   E 4 .   ? 42.621 4.327   5.558   1.00 35.76 ?  348 HOH   A O    1 
HETATM 6987 O O    . HOH   E 4 .   ? 14.369 -21.236 -4.230  1.00 31.07 ?  349 HOH   A O    1 
HETATM 6988 O O    . HOH   E 4 .   ? 27.438 13.833  2.770   1.00 31.40 ?  350 HOH   A O    1 
HETATM 6989 O O    . HOH   E 4 .   ? 13.227 -1.466  -6.759  1.00 18.82 ?  351 HOH   A O    1 
HETATM 6990 O O    . HOH   E 4 .   ? 38.551 5.000   7.042   1.00 15.66 ?  352 HOH   A O    1 
HETATM 6991 O O    . HOH   E 4 .   ? 39.781 -1.061  -5.146  1.00 22.56 ?  353 HOH   A O    1 
HETATM 6992 O O    . HOH   E 4 .   ? 43.333 7.771   2.714   1.00 40.59 ?  354 HOH   A O    1 
HETATM 6993 O O    . HOH   E 4 .   ? 13.563 -15.236 -7.605  1.00 27.81 ?  355 HOH   A O    1 
HETATM 6994 O O    . HOH   E 4 .   ? 34.003 -1.095  -8.962  1.00 28.05 ?  356 HOH   A O    1 
HETATM 6995 O O    . HOH   E 4 .   ? 24.036 -2.092  -2.099  1.00 11.50 ?  357 HOH   A O    1 
HETATM 6996 O O    . HOH   E 4 .   ? 18.631 -19.361 13.561  1.00 38.65 ?  358 HOH   A O    1 
HETATM 6997 O O    . HOH   E 4 .   ? 24.537 1.999   -6.959  1.00 19.66 ?  359 HOH   A O    1 
HETATM 6998 O O    . HOH   E 4 .   ? 21.281 -2.298  -2.402  1.00 16.41 ?  360 HOH   A O    1 
HETATM 6999 O O    . HOH   E 4 .   ? 31.080 -13.926 -2.418  1.00 15.16 ?  361 HOH   A O    1 
HETATM 7000 O O    . HOH   E 4 .   ? 37.195 -2.745  9.769   1.00 43.72 ?  362 HOH   A O    1 
HETATM 7001 O O    . HOH   E 4 .   ? 7.845  -21.528 4.047   1.00 44.99 ?  363 HOH   A O    1 
HETATM 7002 O O    . HOH   E 4 .   ? 31.657 8.237   14.899  1.00 27.93 ?  364 HOH   A O    1 
HETATM 7003 O O    . HOH   E 4 .   ? 33.522 -16.856 8.160   1.00 21.32 ?  365 HOH   A O    1 
HETATM 7004 O O    . HOH   E 4 .   ? 17.118 -17.765 -5.108  1.00 29.38 ?  366 HOH   A O    1 
HETATM 7005 O O    . HOH   E 4 .   ? 35.763 -12.593 6.903   1.00 16.63 ?  367 HOH   A O    1 
HETATM 7006 O O    . HOH   E 4 .   ? 31.880 -9.332  -6.655  1.00 24.62 ?  368 HOH   A O    1 
HETATM 7007 O O    . HOH   E 4 .   ? 22.045 -19.272 11.442  1.00 41.69 ?  369 HOH   A O    1 
HETATM 7008 O O    . HOH   E 4 .   ? 15.463 11.849  7.933   1.00 51.86 ?  370 HOH   A O    1 
HETATM 7009 O O    . HOH   E 4 .   ? 30.790 3.130   8.273   1.00 13.05 ?  371 HOH   A O    1 
HETATM 7010 O O    . HOH   E 4 .   ? 27.368 -10.495 14.119  1.00 19.70 ?  372 HOH   A O    1 
HETATM 7011 O O    . HOH   E 4 .   ? 37.294 12.010  4.940   1.00 27.46 ?  373 HOH   A O    1 
HETATM 7012 O O    . HOH   E 4 .   ? 24.120 -7.681  14.413  1.00 18.58 ?  374 HOH   A O    1 
HETATM 7013 O O    . HOH   E 4 .   ? 21.196 10.279  14.989  1.00 36.13 ?  375 HOH   A O    1 
HETATM 7014 O O    . HOH   E 4 .   ? 33.623 -7.138  4.354   1.00 17.75 ?  376 HOH   A O    1 
HETATM 7015 O O    . HOH   E 4 .   ? 18.526 9.499   8.983   1.00 23.27 ?  377 HOH   A O    1 
HETATM 7016 O O    . HOH   E 4 .   ? 24.585 -17.420 12.789  1.00 27.31 ?  378 HOH   A O    1 
HETATM 7017 O O    . HOH   E 4 .   ? 44.045 8.517   -2.927  1.00 30.72 ?  379 HOH   A O    1 
HETATM 7018 O O    . HOH   E 4 .   ? 16.480 -22.054 0.918   1.00 30.95 ?  380 HOH   A O    1 
HETATM 7019 O O    A HOH   E 4 .   ? 11.067 -0.335  1.899   0.50 24.75 ?  381 HOH   A O    1 
HETATM 7020 O O    T HOH   E 4 .   ? 15.406 -0.379  2.357   0.30 14.82 ?  382 HOH   A O    1 
HETATM 7021 O O    . HOH   E 4 .   ? 24.356 3.632   -1.810  1.00 16.92 ?  383 HOH   A O    1 
HETATM 7022 O O    . HOH   E 4 .   ? 25.708 -0.758  -7.308  1.00 16.71 ?  384 HOH   A O    1 
HETATM 7023 O O    . HOH   E 4 .   ? 21.870 -21.895 8.485   1.00 30.53 ?  385 HOH   A O    1 
HETATM 7024 O O    . HOH   E 4 .   ? 6.323  -5.386  10.936  1.00 19.91 ?  386 HOH   A O    1 
HETATM 7025 O O    . HOH   E 4 .   ? 37.555 -2.065  5.927   1.00 28.30 ?  387 HOH   A O    1 
HETATM 7026 O O    . HOH   E 4 .   ? 31.861 -7.284  -9.814  1.00 23.08 ?  388 HOH   A O    1 
HETATM 7027 O O    . HOH   E 4 .   ? 22.612 -11.834 21.803  1.00 49.83 ?  389 HOH   A O    1 
HETATM 7028 O O    . HOH   E 4 .   ? 10.882 1.800   12.449  1.00 26.22 ?  390 HOH   A O    1 
HETATM 7029 O O    . HOH   E 4 .   ? 8.930  -12.036 17.115  1.00 43.22 ?  391 HOH   A O    1 
HETATM 7030 O O    . HOH   E 4 .   ? 32.733 -9.226  5.981   1.00 20.75 ?  392 HOH   A O    1 
HETATM 7031 O O    . HOH   E 4 .   ? 23.845 -15.710 -9.196  1.00 37.55 ?  393 HOH   A O    1 
HETATM 7032 O O    . HOH   E 4 .   ? 15.851 2.166   24.617  1.00 44.60 ?  394 HOH   A O    1 
HETATM 7033 O O    A HOH   E 4 .   ? 15.796 -0.898  5.242   0.80 21.34 ?  395 HOH   A O    1 
HETATM 7034 O O    . HOH   E 4 .   ? 15.136 -21.413 14.205  1.00 20.54 ?  396 HOH   A O    1 
HETATM 7035 O O    . HOH   E 4 .   ? 23.462 11.404  4.053   1.00 13.20 ?  397 HOH   A O    1 
HETATM 7036 O O    . HOH   E 4 .   ? 20.070 4.530   -7.576  1.00 20.39 ?  398 HOH   A O    1 
HETATM 7037 O O    . HOH   E 4 .   ? 16.166 16.611  8.491   1.00 41.76 ?  399 HOH   A O    1 
HETATM 7038 O O    . HOH   E 4 .   ? 13.822 -4.770  17.355  1.00 31.15 ?  400 HOH   A O    1 
HETATM 7039 O O    . HOH   E 4 .   ? 30.981 6.179   -12.222 1.00 29.24 ?  401 HOH   A O    1 
HETATM 7040 O O    . HOH   E 4 .   ? 20.533 -19.998 2.787   1.00 21.73 ?  402 HOH   A O    1 
HETATM 7041 O O    . HOH   E 4 .   ? 21.822 -13.713 -8.224  1.00 37.93 ?  403 HOH   A O    1 
HETATM 7042 O O    . HOH   E 4 .   ? 30.616 1.939   16.687  1.00 23.23 ?  404 HOH   A O    1 
HETATM 7043 O O    . HOH   E 4 .   ? 23.934 -20.266 -1.326  1.00 19.46 ?  405 HOH   A O    1 
HETATM 7044 O O    . HOH   E 4 .   ? 6.577  -3.053  12.677  1.00 29.98 ?  406 HOH   A O    1 
HETATM 7045 O O    . HOH   E 4 .   ? 11.542 -10.666 16.862  1.00 28.98 ?  407 HOH   A O    1 
HETATM 7046 O O    . HOH   E 4 .   ? 26.913 4.197   -0.670  1.00 13.15 ?  408 HOH   A O    1 
HETATM 7047 O O    . HOH   E 4 .   ? 24.015 3.931   -4.825  1.00 20.32 ?  409 HOH   A O    1 
HETATM 7048 O O    . HOH   E 4 .   ? 18.877 -0.732  -1.676  1.00 17.10 ?  410 HOH   A O    1 
HETATM 7049 O O    A HOH   E 4 .   ? 7.718  -6.300  -6.537  0.80 39.23 ?  411 HOH   A O    1 
HETATM 7050 O O    . HOH   E 4 .   ? 30.234 -12.831 13.563  1.00 22.20 ?  412 HOH   A O    1 
HETATM 7051 O O    . HOH   E 4 .   ? 27.267 2.374   18.752  1.00 34.22 ?  413 HOH   A O    1 
HETATM 7052 O O    . HOH   E 4 .   ? 38.137 -1.345  -1.901  1.00 20.08 ?  414 HOH   A O    1 
HETATM 7053 O O    . HOH   E 4 .   ? 40.905 -8.240  -6.768  1.00 36.32 ?  415 HOH   A O    1 
HETATM 7054 O O    . HOH   E 4 .   ? 32.682 -4.273  -9.856  1.00 28.47 ?  416 HOH   A O    1 
HETATM 7055 O O    . HOH   E 4 .   ? 27.952 0.818   -7.128  1.00 15.04 ?  417 HOH   A O    1 
HETATM 7056 O O    . HOH   E 4 .   ? 44.946 -0.612  3.042   1.00 41.18 ?  418 HOH   A O    1 
HETATM 7057 O O    . HOH   E 4 .   ? 29.988 -10.009 13.092  1.00 25.08 ?  419 HOH   A O    1 
HETATM 7058 O O    . HOH   E 4 .   ? 35.106 -5.219  -3.031  1.00 17.91 ?  420 HOH   A O    1 
HETATM 7059 O O    . HOH   E 4 .   ? 14.470 -24.595 11.572  1.00 45.16 ?  421 HOH   A O    1 
HETATM 7060 O O    . HOH   E 4 .   ? 10.338 -13.712 -1.746  1.00 18.10 ?  422 HOH   A O    1 
HETATM 7061 O O    . HOH   E 4 .   ? 36.719 -4.937  5.411   1.00 25.21 ?  423 HOH   A O    1 
HETATM 7062 O O    . HOH   E 4 .   ? 5.327  2.959   4.725   1.00 38.56 ?  424 HOH   A O    1 
HETATM 7063 O O    . HOH   E 4 .   ? 41.655 1.504   5.083   1.00 38.57 ?  425 HOH   A O    1 
HETATM 7064 O O    . HOH   E 4 .   ? 32.465 -10.649 3.297   1.00 33.40 ?  426 HOH   A O    1 
HETATM 7065 O O    . HOH   E 4 .   ? 22.609 8.253   18.364  1.00 45.72 ?  427 HOH   A O    1 
HETATM 7066 O O    . HOH   E 4 .   ? 9.440  -16.226 -2.025  1.00 35.57 ?  428 HOH   A O    1 
HETATM 7067 O O    . HOH   E 4 .   ? 15.959 6.868   2.872   1.00 19.94 ?  429 HOH   A O    1 
HETATM 7068 O O    . HOH   E 4 .   ? 16.221 -14.184 20.110  1.00 54.61 ?  430 HOH   A O    1 
HETATM 7069 O O    . HOH   E 4 .   ? 23.430 -20.874 1.365   1.00 21.59 ?  431 HOH   A O    1 
HETATM 7070 O O    . HOH   E 4 .   ? 23.466 -7.958  17.102  1.00 24.63 ?  432 HOH   A O    1 
HETATM 7071 O O    . HOH   E 4 .   ? 16.058 2.872   -1.497  1.00 16.80 ?  433 HOH   A O    1 
HETATM 7072 O O    . HOH   E 4 .   ? 27.022 -3.151  19.467  1.00 39.55 ?  434 HOH   A O    1 
HETATM 7073 O O    . HOH   E 4 .   ? 18.504 4.899   -15.123 1.00 56.29 ?  435 HOH   A O    1 
HETATM 7074 O O    A HOH   E 4 .   ? 14.025 -0.293  3.430   0.50 31.19 ?  436 HOH   A O    1 
HETATM 7075 O O    . HOH   E 4 .   ? 18.844 1.984   -0.725  1.00 16.24 ?  437 HOH   A O    1 
HETATM 7076 O O    . HOH   E 4 .   ? 31.315 -12.774 0.055   1.00 22.00 ?  438 HOH   A O    1 
HETATM 7077 O O    . HOH   E 4 .   ? 21.414 -14.744 17.886  1.00 53.17 ?  439 HOH   A O    1 
HETATM 7078 O O    . HOH   E 4 .   ? 34.411 -8.088  -0.521  1.00 30.94 ?  440 HOH   A O    1 
HETATM 7079 O O    . HOH   E 4 .   ? 18.355 -15.901 16.238  1.00 43.57 ?  441 HOH   A O    1 
HETATM 7080 O O    . HOH   E 4 .   ? 23.207 7.478   -3.231  1.00 35.63 ?  442 HOH   A O    1 
HETATM 7081 O O    . HOH   E 4 .   ? 37.722 -8.782  -3.341  1.00 24.46 ?  443 HOH   A O    1 
HETATM 7082 O O    . HOH   E 4 .   ? 20.580 -17.681 24.806  1.00 57.77 ?  444 HOH   A O    1 
HETATM 7083 O O    . HOH   E 4 .   ? 30.536 14.787  2.709   1.00 20.37 ?  445 HOH   A O    1 
HETATM 7084 O O    . HOH   E 4 .   ? -1.508 -4.839  7.479   1.00 47.84 ?  446 HOH   A O    1 
HETATM 7085 O O    . HOH   E 4 .   ? 21.378 -9.108  21.345  1.00 61.89 ?  447 HOH   A O    1 
HETATM 7086 O O    . HOH   E 4 .   ? 32.402 -15.835 10.945  1.00 30.09 ?  448 HOH   A O    1 
HETATM 7087 O O    . HOH   E 4 .   ? 25.394 8.216   -4.872  1.00 38.75 ?  449 HOH   A O    1 
HETATM 7088 O O    . HOH   E 4 .   ? 29.822 -16.091 10.905  1.00 36.44 ?  450 HOH   A O    1 
HETATM 7089 O O    . HOH   E 4 .   ? 29.845 -1.933  -12.758 1.00 46.54 ?  451 HOH   A O    1 
HETATM 7090 O O    . HOH   E 4 .   ? 24.817 5.661   20.740  1.00 54.12 ?  452 HOH   A O    1 
HETATM 7091 O O    . HOH   E 4 .   ? 27.861 7.126   -6.663  1.00 41.31 ?  453 HOH   A O    1 
HETATM 7092 O O    . HOH   E 4 .   ? 19.882 -17.346 -5.056  1.00 26.00 ?  454 HOH   A O    1 
HETATM 7093 O O    . HOH   E 4 .   ? 11.033 -14.977 -6.168  1.00 38.01 ?  455 HOH   A O    1 
HETATM 7094 O O    . HOH   E 4 .   ? 23.158 -22.392 -3.278  1.00 41.94 ?  456 HOH   A O    1 
HETATM 7095 O O    . HOH   E 4 .   ? 21.848 5.086   -5.837  1.00 36.65 ?  457 HOH   A O    1 
HETATM 7096 O O    . HOH   E 4 .   ? 24.583 14.794  7.762   1.00 39.99 ?  458 HOH   A O    1 
HETATM 7097 O O    . HOH   E 4 .   ? 26.908 11.707  -1.445  1.00 38.39 ?  459 HOH   A O    1 
HETATM 7098 O O    . HOH   E 4 .   ? 18.766 10.944  11.252  1.00 34.10 ?  460 HOH   A O    1 
HETATM 7099 O O    . HOH   E 4 .   ? 27.410 -11.267 16.658  1.00 40.77 ?  461 HOH   A O    1 
HETATM 7100 O O    . HOH   E 4 .   ? 15.719 -21.497 3.702   1.00 27.96 ?  462 HOH   A O    1 
HETATM 7101 O O    . HOH   E 4 .   ? 18.104 -16.243 -8.946  1.00 43.96 ?  463 HOH   A O    1 
HETATM 7102 O O    . HOH   E 4 .   ? 12.310 1.660   17.272  1.00 43.20 ?  464 HOH   A O    1 
HETATM 7103 O O    . HOH   E 4 .   ? 39.639 -6.961  -3.407  1.00 45.04 ?  465 HOH   A O    1 
HETATM 7104 O O    . HOH   E 4 .   ? 23.418 13.717  5.499   1.00 19.93 ?  466 HOH   A O    1 
HETATM 7105 O O    . HOH   E 4 .   ? 8.077  -3.220  -5.897  1.00 52.47 ?  467 HOH   A O    1 
HETATM 7106 O O    . HOH   E 4 .   ? 12.016 -13.300 16.353  1.00 55.13 ?  468 HOH   A O    1 
HETATM 7107 O O    . HOH   E 4 .   ? 25.779 10.782  -3.782  1.00 30.83 ?  469 HOH   A O    1 
HETATM 7108 O O    . HOH   E 4 .   ? 15.779 -17.139 -7.037  1.00 34.11 ?  470 HOH   A O    1 
HETATM 7109 O O    . HOH   E 4 .   ? 28.834 8.995   17.501  1.00 39.97 ?  471 HOH   A O    1 
HETATM 7110 O O    . HOH   E 4 .   ? 16.083 -6.736  -11.968 1.00 45.36 ?  472 HOH   A O    1 
HETATM 7111 O O    . HOH   E 4 .   ? 16.825 -20.419 16.051  1.00 32.06 ?  473 HOH   A O    1 
HETATM 7112 O O    . HOH   E 4 .   ? 16.202 -23.358 5.800   1.00 33.42 ?  474 HOH   A O    1 
HETATM 7113 O O    . HOH   E 4 .   ? 35.196 7.581   12.232  1.00 55.43 ?  475 HOH   A O    1 
HETATM 7114 O O    . HOH   E 4 .   ? 20.061 -22.302 4.271   1.00 31.57 ?  476 HOH   A O    1 
HETATM 7115 O O    . HOH   E 4 .   ? 17.431 -18.728 19.777  1.00 58.51 ?  477 HOH   A O    1 
HETATM 7116 O O    . HOH   E 4 .   ? 40.994 -3.958  -0.434  1.00 41.66 ?  478 HOH   A O    1 
HETATM 7117 O O    . HOH   E 4 .   ? 30.799 0.721   19.178  1.00 41.97 ?  479 HOH   A O    1 
HETATM 7118 O O    . HOH   E 4 .   ? 23.097 11.843  -4.095  1.00 21.50 ?  480 HOH   A O    1 
HETATM 7119 O O    . HOH   E 4 .   ? 13.964 -10.336 -10.987 1.00 36.52 ?  481 HOH   A O    1 
HETATM 7120 O O    . HOH   E 4 .   ? 44.569 10.435  -1.578  1.00 32.37 ?  482 HOH   A O    1 
HETATM 7121 O O    . HOH   E 4 .   ? 28.710 -7.965  -15.286 1.00 53.54 ?  483 HOH   A O    1 
HETATM 7122 O O    . HOH   E 4 .   ? 13.835 -25.098 8.925   1.00 36.01 ?  484 HOH   A O    1 
HETATM 7123 O O    . HOH   E 4 .   ? 28.578 -4.658  -12.325 1.00 40.44 ?  485 HOH   A O    1 
HETATM 7124 O O    . HOH   E 4 .   ? 39.195 2.408   7.337   1.00 33.25 ?  486 HOH   A O    1 
HETATM 7125 O O    . HOH   E 4 .   ? 18.393 -23.129 1.932   1.00 53.25 ?  487 HOH   A O    1 
HETATM 7126 O O    . HOH   E 4 .   ? 23.218 -12.806 19.313  1.00 52.49 ?  488 HOH   A O    1 
HETATM 7127 O O    . HOH   E 4 .   ? 41.779 9.439   -3.902  1.00 32.40 ?  489 HOH   A O    1 
HETATM 7128 O O    . HOH   E 4 .   ? 31.498 -0.536  -10.523 1.00 31.61 ?  490 HOH   A O    1 
HETATM 7129 O O    . HOH   E 4 .   ? 40.667 -0.288  -7.736  1.00 34.07 ?  491 HOH   A O    1 
HETATM 7130 O O    . HOH   E 4 .   ? 30.775 -5.807  -11.874 1.00 50.93 ?  492 HOH   A O    1 
HETATM 7131 O O    . HOH   E 4 .   ? 37.390 -6.624  7.682   1.00 27.87 ?  493 HOH   A O    1 
HETATM 7132 O O    . HOH   E 4 .   ? 39.513 -0.015  6.640   1.00 32.87 ?  494 HOH   A O    1 
HETATM 7133 O O    . HOH   E 4 .   ? 20.589 -16.121 -7.423  1.00 30.09 ?  495 HOH   A O    1 
HETATM 7134 O O    . HOH   E 4 .   ? 30.784 5.763   -14.757 1.00 35.81 ?  496 HOH   A O    1 
HETATM 7135 O O    . HOH   E 4 .   ? 28.981 14.437  0.830   1.00 53.30 ?  497 HOH   A O    1 
HETATM 7136 O O    . HOH   E 4 .   ? 37.948 14.009  6.712   1.00 36.02 ?  498 HOH   A O    1 
HETATM 7137 O O    . HOH   E 4 .   ? 14.677 8.312   4.951   1.00 42.67 ?  499 HOH   A O    1 
HETATM 7138 O O    . HOH   E 4 .   ? 36.411 -6.470  10.296  1.00 51.45 ?  500 HOH   A O    1 
HETATM 7139 O O    . HOH   E 4 .   ? 22.034 -24.006 4.552   1.00 28.25 ?  501 HOH   A O    1 
HETATM 7140 O O    T HOH   E 4 .   ? 11.926 -2.115  -3.684  0.30 11.45 ?  502 HOH   A O    1 
HETATM 7141 O O    . HOH   E 4 .   ? 24.071 9.105   -7.200  1.00 39.45 ?  503 HOH   A O    1 
HETATM 7142 O O    . HOH   E 4 .   ? 17.331 -6.623  -14.159 1.00 46.89 ?  504 HOH   A O    1 
HETATM 7143 O O    . HOH   E 4 .   ? 15.714 -12.210 27.386  1.00 48.44 ?  505 HOH   A O    1 
HETATM 7144 O O    . HOH   E 4 .   ? 16.314 -21.134 18.764  1.00 40.77 ?  506 HOH   A O    1 
HETATM 7145 O O    . HOH   E 4 .   ? 14.740 -22.731 19.840  1.00 37.59 ?  507 HOH   A O    1 
HETATM 7146 O O    . HOH   F 4 .   ? 29.832 -22.411 5.576   1.00 22.36 ?  201 HOH   B O    1 
HETATM 7147 O O    . HOH   F 4 .   ? 30.992 -28.671 4.522   1.00 32.31 ?  202 HOH   B O    1 
HETATM 7148 O O    . HOH   F 4 .   ? 27.670 -29.140 -1.774  1.00 37.87 ?  203 HOH   B O    1 
HETATM 7149 O O    . HOH   F 4 .   ? 41.603 -36.074 -17.091 1.00 36.26 ?  204 HOH   B O    1 
HETATM 7150 O O    . HOH   F 4 .   ? 52.941 -13.466 -20.289 1.00 37.32 ?  205 HOH   B O    1 
HETATM 7151 O O    . HOH   F 4 .   ? 30.007 -26.257 4.218   1.00 29.29 ?  206 HOH   B O    1 
HETATM 7152 O O    . HOH   F 4 .   ? 49.439 -22.699 -19.728 1.00 50.00 ?  207 HOH   B O    1 
HETATM 7153 O O    . HOH   F 4 .   ? 48.099 -6.910  15.538  1.00 29.46 ?  208 HOH   B O    1 
HETATM 7154 O O    . HOH   F 4 .   ? 30.215 -40.990 -7.947  1.00 19.03 ?  209 HOH   B O    1 
HETATM 7155 O O    . HOH   F 4 .   ? 54.530 -9.455  -8.626  1.00 20.03 ?  210 HOH   B O    1 
HETATM 7156 O O    . HOH   F 4 .   ? 27.918 -41.813 -15.111 1.00 39.85 ?  211 HOH   B O    1 
HETATM 7157 O O    . HOH   F 4 .   ? 59.160 -18.642 6.937   1.00 36.87 ?  212 HOH   B O    1 
HETATM 7158 O O    . HOH   F 4 .   ? 50.206 -3.349  7.148   1.00 38.23 ?  213 HOH   B O    1 
HETATM 7159 O O    . HOH   F 4 .   ? 38.106 -39.444 -0.094  1.00 41.19 ?  214 HOH   B O    1 
HETATM 7160 O O    . HOH   F 4 .   ? 57.749 -24.444 5.098   1.00 39.84 ?  215 HOH   B O    1 
HETATM 7161 O O    . HOH   F 4 .   ? 37.104 -19.826 -18.100 1.00 43.53 ?  216 HOH   B O    1 
HETATM 7162 O O    . HOH   F 4 .   ? 57.161 -26.976 -7.605  1.00 40.04 ?  217 HOH   B O    1 
HETATM 7163 O O    . HOH   F 4 .   ? 41.324 -7.725  5.456   1.00 41.82 ?  218 HOH   B O    1 
HETATM 7164 O O    . HOH   F 4 .   ? 56.401 -19.702 7.241   1.00 31.74 ?  219 HOH   B O    1 
HETATM 7165 O O    . HOH   F 4 .   ? 56.692 -30.772 -7.704  1.00 31.41 ?  220 HOH   B O    1 
HETATM 7166 O O    . HOH   F 4 .   ? 58.216 -12.895 8.410   1.00 33.14 ?  221 HOH   B O    1 
HETATM 7167 O O    . HOH   F 4 .   ? 41.524 -39.228 -14.803 1.00 24.56 ?  222 HOH   B O    1 
HETATM 7168 O O    . HOH   F 4 .   ? 26.493 -19.331 -1.710  1.00 15.90 ?  223 HOH   B O    1 
HETATM 7169 O O    . HOH   F 4 .   ? 34.531 -36.391 -7.082  1.00 21.24 ?  224 HOH   B O    1 
HETATM 7170 O O    . HOH   F 4 .   ? 34.894 -24.618 13.848  1.00 37.96 ?  225 HOH   B O    1 
HETATM 7171 O O    . HOH   F 4 .   ? 32.743 -43.754 -11.220 1.00 24.41 ?  226 HOH   B O    1 
HETATM 7172 O O    . HOH   F 4 .   ? 55.403 -16.587 -14.295 1.00 32.23 ?  227 HOH   B O    1 
HETATM 7173 O O    . HOH   F 4 .   ? 50.751 -6.086  0.180   1.00 29.65 ?  228 HOH   B O    1 
HETATM 7174 O O    . HOH   F 4 .   ? 25.384 -25.858 -1.141  1.00 33.13 ?  229 HOH   B O    1 
HETATM 7175 O O    . HOH   F 4 .   ? 44.404 -7.110  2.026   1.00 36.81 ?  230 HOH   B O    1 
HETATM 7176 O O    . HOH   F 4 .   ? 57.410 -16.312 -12.216 1.00 18.63 ?  231 HOH   B O    1 
HETATM 7177 O O    . HOH   F 4 .   ? 50.937 -39.925 -8.089  1.00 41.19 ?  232 HOH   B O    1 
HETATM 7178 O O    . HOH   F 4 .   ? 47.396 -7.298  -3.765  1.00 41.58 ?  233 HOH   B O    1 
HETATM 7179 O O    . HOH   F 4 .   ? 48.599 -36.505 -15.467 1.00 46.75 ?  234 HOH   B O    1 
HETATM 7180 O O    . HOH   F 4 .   ? 46.417 -1.519  13.152  1.00 29.45 ?  235 HOH   B O    1 
HETATM 7181 O O    . HOH   F 4 .   ? 51.681 -6.464  4.364   1.00 20.82 ?  236 HOH   B O    1 
HETATM 7182 O O    . HOH   F 4 .   ? 57.645 -24.353 -3.722  1.00 21.55 ?  237 HOH   B O    1 
HETATM 7183 O O    . HOH   F 4 .   ? 39.305 -10.887 6.154   1.00 25.75 ?  238 HOH   B O    1 
HETATM 7184 O O    . HOH   F 4 .   ? 50.759 -12.978 -0.438  1.00 12.61 ?  239 HOH   B O    1 
HETATM 7185 O O    . HOH   F 4 .   ? 35.099 -7.993  -2.934  1.00 19.31 ?  240 HOH   B O    1 
HETATM 7186 O O    . HOH   F 4 .   ? 41.371 -9.591  13.125  1.00 23.43 ?  241 HOH   B O    1 
HETATM 7187 O O    . HOH   F 4 .   ? 40.556 -16.089 14.110  1.00 24.42 ?  242 HOH   B O    1 
HETATM 7188 O O    . HOH   F 4 .   ? 34.296 -18.311 11.479  1.00 26.80 ?  243 HOH   B O    1 
HETATM 7189 O O    . HOH   F 4 .   ? 44.541 -27.747 -0.636  1.00 23.51 ?  244 HOH   B O    1 
HETATM 7190 O O    . HOH   F 4 .   ? 43.003 -43.264 -8.105  1.00 31.14 ?  245 HOH   B O    1 
HETATM 7191 O O    . HOH   F 4 .   ? 42.593 -25.347 2.730   1.00 16.37 ?  246 HOH   B O    1 
HETATM 7192 O O    . HOH   F 4 .   ? 39.520 -11.089 0.356   1.00 17.81 ?  247 HOH   B O    1 
HETATM 7193 O O    . HOH   F 4 .   ? 42.639 -22.848 3.908   1.00 12.73 ?  248 HOH   B O    1 
HETATM 7194 O O    . HOH   F 4 .   ? 38.477 -11.081 -2.201  1.00 20.48 ?  249 HOH   B O    1 
HETATM 7195 O O    . HOH   F 4 .   ? 45.211 -34.942 6.858   1.00 46.59 ?  250 HOH   B O    1 
HETATM 7196 O O    . HOH   F 4 .   ? 58.216 -10.683 -4.024  1.00 22.79 ?  251 HOH   B O    1 
HETATM 7197 O O    . HOH   F 4 .   ? 43.127 -32.408 -17.006 1.00 26.58 ?  252 HOH   B O    1 
HETATM 7198 O O    . HOH   F 4 .   ? 46.868 -29.590 9.864   1.00 33.20 ?  253 HOH   B O    1 
HETATM 7199 O O    . HOH   F 4 .   ? 28.404 -19.710 -13.100 1.00 26.72 ?  254 HOH   B O    1 
HETATM 7200 O O    . HOH   F 4 .   ? 28.497 -30.993 -14.674 1.00 33.89 ?  255 HOH   B O    1 
HETATM 7201 O O    . HOH   F 4 .   ? 29.850 -34.187 -0.375  1.00 39.59 ?  256 HOH   B O    1 
HETATM 7202 O O    . HOH   F 4 .   ? 42.909 -20.283 -20.662 1.00 36.49 ?  257 HOH   B O    1 
HETATM 7203 O O    . HOH   F 4 .   ? 40.353 -12.755 -11.455 1.00 16.44 ?  258 HOH   B O    1 
HETATM 7204 O O    . HOH   F 4 .   ? 44.912 -43.621 -10.341 1.00 28.06 ?  259 HOH   B O    1 
HETATM 7205 O O    . HOH   F 4 .   ? 29.717 -25.202 -10.698 1.00 18.62 ?  260 HOH   B O    1 
HETATM 7206 O O    . HOH   F 4 .   ? 31.748 -17.793 -14.420 1.00 32.37 ?  261 HOH   B O    1 
HETATM 7207 O O    . HOH   F 4 .   ? 30.858 -15.704 2.724   1.00 15.27 ?  262 HOH   B O    1 
HETATM 7208 O O    . HOH   F 4 .   ? 30.501 -42.237 -10.562 1.00 31.75 ?  263 HOH   B O    1 
HETATM 7209 O O    . HOH   F 4 .   ? 51.535 -13.784 11.067  1.00 26.60 ?  264 HOH   B O    1 
HETATM 7210 O O    . HOH   F 4 .   ? 34.988 -33.292 -19.109 1.00 35.02 ?  265 HOH   B O    1 
HETATM 7211 O O    . HOH   F 4 .   ? 47.912 -24.507 -17.756 1.00 34.65 ?  266 HOH   B O    1 
HETATM 7212 O O    . HOH   F 4 .   ? 56.149 -23.648 -14.687 1.00 28.22 ?  267 HOH   B O    1 
HETATM 7213 O O    . HOH   F 4 .   ? 49.307 -28.700 -6.821  1.00 16.89 ?  268 HOH   B O    1 
HETATM 7214 O O    . HOH   F 4 .   ? 42.343 -9.890  9.408   1.00 22.20 ?  269 HOH   B O    1 
HETATM 7215 O O    . HOH   F 4 .   ? 38.924 -11.875 12.406  1.00 37.35 ?  270 HOH   B O    1 
HETATM 7216 O O    . HOH   F 4 .   ? 41.916 -23.459 9.347   1.00 20.78 ?  271 HOH   B O    1 
HETATM 7217 O O    . HOH   F 4 .   ? 48.069 -22.764 5.875   1.00 19.89 ?  272 HOH   B O    1 
HETATM 7218 O O    . HOH   F 4 .   ? 27.111 -31.829 -9.851  1.00 22.77 ?  273 HOH   B O    1 
HETATM 7219 O O    . HOH   F 4 .   ? 28.253 -34.377 -9.290  1.00 18.59 ?  274 HOH   B O    1 
HETATM 7220 O O    . HOH   F 4 .   ? 43.403 -15.798 -12.162 1.00 15.67 ?  275 HOH   B O    1 
HETATM 7221 O O    . HOH   F 4 .   ? 41.142 -5.528  11.584  1.00 50.50 ?  276 HOH   B O    1 
HETATM 7222 O O    . HOH   F 4 .   ? 36.046 -43.479 -8.221  1.00 41.26 ?  277 HOH   B O    1 
HETATM 7223 O O    . HOH   F 4 .   ? 34.488 -12.755 2.673   1.00 26.24 ?  278 HOH   B O    1 
HETATM 7224 O O    . HOH   F 4 .   ? 56.942 -8.627  8.458   1.00 19.93 ?  279 HOH   B O    1 
HETATM 7225 O O    . HOH   F 4 .   ? 49.940 -24.662 5.834   1.00 35.86 ?  280 HOH   B O    1 
HETATM 7226 O O    . HOH   F 4 .   ? 48.410 -25.023 3.173   1.00 14.62 ?  281 HOH   B O    1 
HETATM 7227 O O    . HOH   F 4 .   ? 27.958 -22.883 -7.934  1.00 19.22 ?  282 HOH   B O    1 
HETATM 7228 O O    . HOH   F 4 .   ? 46.615 -31.228 -4.742  1.00 25.85 ?  283 HOH   B O    1 
HETATM 7229 O O    . HOH   F 4 .   ? 57.502 -9.212  1.410   1.00 21.47 ?  284 HOH   B O    1 
HETATM 7230 O O    . HOH   F 4 .   ? 48.622 -12.145 -14.320 1.00 27.02 ?  285 HOH   B O    1 
HETATM 7231 O O    . HOH   F 4 .   ? 49.720 -0.438  10.217  1.00 30.66 ?  286 HOH   B O    1 
HETATM 7232 O O    . HOH   F 4 .   ? 42.448 -34.701 3.905   1.00 27.77 ?  287 HOH   B O    1 
HETATM 7233 O O    . HOH   F 4 .   ? 52.530 -10.334 13.001  1.00 23.61 ?  288 HOH   B O    1 
HETATM 7234 O O    . HOH   F 4 .   ? 27.550 -26.630 -15.503 1.00 34.95 ?  289 HOH   B O    1 
HETATM 7235 O O    . HOH   F 4 .   ? 33.553 -15.303 -13.887 1.00 23.47 ?  290 HOH   B O    1 
HETATM 7236 O O    . HOH   F 4 .   ? 57.117 -12.059 12.386  1.00 41.92 ?  291 HOH   B O    1 
HETATM 7237 O O    . HOH   F 4 .   ? 47.074 -33.966 -4.555  1.00 20.34 ?  292 HOH   B O    1 
HETATM 7238 O O    . HOH   F 4 .   ? 48.715 -20.006 5.996   1.00 15.04 ?  293 HOH   B O    1 
HETATM 7239 O O    . HOH   F 4 .   ? 45.262 -33.396 -15.896 1.00 25.09 ?  294 HOH   B O    1 
HETATM 7240 O O    . HOH   F 4 .   ? 36.796 -12.741 -1.459  1.00 29.34 ?  295 HOH   B O    1 
HETATM 7241 O O    . HOH   F 4 .   ? 59.806 -15.271 8.204   1.00 34.45 ?  296 HOH   B O    1 
HETATM 7242 O O    . HOH   F 4 .   ? 51.726 -6.044  -7.939  1.00 42.57 ?  297 HOH   B O    1 
HETATM 7243 O O    . HOH   F 4 .   ? 42.713 -12.317 -18.468 1.00 29.88 ?  298 HOH   B O    1 
HETATM 7244 O O    . HOH   F 4 .   ? 51.199 -37.636 -9.581  1.00 29.46 ?  299 HOH   B O    1 
HETATM 7245 O O    . HOH   F 4 .   ? 37.437 -17.916 13.170  1.00 33.40 ?  300 HOH   B O    1 
HETATM 7246 O O    . HOH   F 4 .   ? 62.748 -13.609 4.778   1.00 29.05 ?  301 HOH   B O    1 
HETATM 7247 O O    . HOH   F 4 .   ? 45.873 -40.397 -3.449  1.00 33.79 ?  302 HOH   B O    1 
HETATM 7248 O O    . HOH   F 4 .   ? 52.988 -16.022 -12.738 1.00 26.89 ?  303 HOH   B O    1 
HETATM 7249 O O    . HOH   F 4 .   ? 44.644 -27.450 2.106   1.00 17.50 ?  304 HOH   B O    1 
HETATM 7250 O O    . HOH   F 4 .   ? 52.581 -35.695 -8.701  1.00 32.09 ?  305 HOH   B O    1 
HETATM 7251 O O    . HOH   F 4 .   ? 37.318 -35.637 7.343   1.00 36.59 ?  306 HOH   B O    1 
HETATM 7252 O O    . HOH   F 4 .   ? 37.871 -10.231 -10.738 1.00 19.50 ?  307 HOH   B O    1 
HETATM 7253 O O    . HOH   F 4 .   ? 44.076 -29.336 -4.599  1.00 24.65 ?  308 HOH   B O    1 
HETATM 7254 O O    . HOH   F 4 .   ? 52.471 -29.292 -13.029 1.00 27.03 ?  309 HOH   B O    1 
HETATM 7255 O O    . HOH   F 4 .   ? 40.264 -10.832 -9.497  1.00 18.72 ?  310 HOH   B O    1 
HETATM 7256 O O    . HOH   F 4 .   ? 42.441 -9.760  -14.822 1.00 40.51 ?  311 HOH   B O    1 
HETATM 7257 O O    . HOH   F 4 .   ? 43.227 -21.393 10.738  1.00 17.37 ?  312 HOH   B O    1 
HETATM 7258 O O    . HOH   F 4 .   ? 53.661 -12.639 -22.177 1.00 32.72 ?  313 HOH   B O    1 
HETATM 7259 O O    . HOH   F 4 .   ? 25.956 -21.457 -3.443  1.00 19.09 ?  314 HOH   B O    1 
HETATM 7260 O O    . HOH   F 4 .   ? 53.495 -30.207 4.602   1.00 20.02 ?  315 HOH   B O    1 
HETATM 7261 O O    . HOH   F 4 .   ? 51.329 -33.106 -10.783 1.00 44.19 ?  316 HOH   B O    1 
HETATM 7262 O O    . HOH   F 4 .   ? 37.006 -30.612 -20.934 1.00 33.77 ?  317 HOH   B O    1 
HETATM 7263 O O    . HOH   F 4 .   ? 35.038 -33.622 4.672   1.00 34.29 ?  318 HOH   B O    1 
HETATM 7264 O O    . HOH   F 4 .   ? 44.120 -1.781  7.628   1.00 49.41 ?  319 HOH   B O    1 
HETATM 7265 O O    . HOH   F 4 .   ? 38.480 -12.205 -16.193 1.00 46.55 ?  320 HOH   B O    1 
HETATM 7266 O O    . HOH   F 4 .   ? 26.358 -21.033 -6.182  1.00 18.45 ?  321 HOH   B O    1 
HETATM 7267 O O    . HOH   F 4 .   ? 38.340 -12.644 7.973   1.00 18.72 ?  322 HOH   B O    1 
HETATM 7268 O O    . HOH   F 4 .   ? 38.418 -9.336  -13.267 1.00 29.95 ?  323 HOH   B O    1 
HETATM 7269 O O    . HOH   F 4 .   ? 32.842 -34.594 -5.786  1.00 18.86 ?  324 HOH   B O    1 
HETATM 7270 O O    . HOH   F 4 .   ? 44.667 -24.572 9.640   1.00 22.93 ?  325 HOH   B O    1 
HETATM 7271 O O    . HOH   F 4 .   ? 41.756 -8.037  1.396   1.00 25.74 ?  326 HOH   B O    1 
HETATM 7272 O O    . HOH   F 4 .   ? 36.738 -12.394 4.297   1.00 18.51 ?  327 HOH   B O    1 
HETATM 7273 O O    . HOH   F 4 .   ? 47.279 -24.443 8.263   1.00 25.82 ?  328 HOH   B O    1 
HETATM 7274 O O    . HOH   F 4 .   ? 59.996 -17.235 -10.460 1.00 35.57 ?  329 HOH   B O    1 
HETATM 7275 O O    . HOH   F 4 .   ? 43.139 -34.563 0.197   1.00 23.29 ?  330 HOH   B O    1 
HETATM 7276 O O    . HOH   F 4 .   ? 43.533 -15.408 18.140  1.00 32.27 ?  331 HOH   B O    1 
HETATM 7277 O O    . HOH   F 4 .   ? 48.034 -32.699 -16.621 1.00 44.63 ?  332 HOH   B O    1 
HETATM 7278 O O    . HOH   F 4 .   ? 27.724 -14.791 -9.474  1.00 39.32 ?  333 HOH   B O    1 
HETATM 7279 O O    . HOH   F 4 .   ? 33.664 -31.146 11.095  1.00 38.47 ?  334 HOH   B O    1 
HETATM 7280 O O    . HOH   F 4 .   ? 57.568 -21.990 3.425   1.00 32.29 ?  335 HOH   B O    1 
HETATM 7281 O O    . HOH   F 4 .   ? 62.929 -20.226 -0.656  1.00 37.97 ?  336 HOH   B O    1 
HETATM 7282 O O    . HOH   F 4 .   ? 47.491 -27.426 2.091   1.00 16.24 ?  337 HOH   B O    1 
HETATM 7283 O O    . HOH   F 4 .   ? 45.652 -36.284 -16.067 1.00 36.65 ?  338 HOH   B O    1 
HETATM 7284 O O    . HOH   F 4 .   ? 37.038 -45.118 -9.640  1.00 37.47 ?  339 HOH   B O    1 
HETATM 7285 O O    . HOH   F 4 .   ? 42.887 -43.569 -14.317 1.00 42.83 ?  340 HOH   B O    1 
HETATM 7286 O O    . HOH   F 4 .   ? 37.043 -15.162 -16.525 1.00 44.99 ?  341 HOH   B O    1 
HETATM 7287 O O    . HOH   F 4 .   ? 41.285 -24.487 15.950  1.00 50.58 ?  342 HOH   B O    1 
HETATM 7288 O O    . HOH   F 4 .   ? 46.825 -19.877 12.349  1.00 31.73 ?  343 HOH   B O    1 
HETATM 7289 O O    . HOH   F 4 .   ? 34.485 -10.315 7.738   1.00 23.26 ?  344 HOH   B O    1 
HETATM 7290 O O    . HOH   F 4 .   ? 28.930 -42.919 -12.240 1.00 43.92 ?  345 HOH   B O    1 
HETATM 7291 O O    . HOH   F 4 .   ? 33.007 -14.671 1.114   1.00 20.94 ?  346 HOH   B O    1 
HETATM 7292 O O    . HOH   F 4 .   ? 38.653 -22.327 15.046  1.00 44.81 ?  347 HOH   B O    1 
HETATM 7293 O O    . HOH   F 4 .   ? 44.223 -37.444 -17.660 1.00 36.81 ?  348 HOH   B O    1 
HETATM 7294 O O    . HOH   F 4 .   ? 40.414 -43.504 -9.060  1.00 28.51 ?  349 HOH   B O    1 
HETATM 7295 O O    . HOH   F 4 .   ? 39.849 -44.238 -11.136 1.00 43.13 ?  350 HOH   B O    1 
HETATM 7296 O O    . HOH   F 4 .   ? 39.621 -23.699 -20.384 1.00 40.27 ?  351 HOH   B O    1 
HETATM 7297 O O    . HOH   F 4 .   ? 33.701 -9.644  -8.844  1.00 34.12 ?  352 HOH   B O    1 
HETATM 7298 O O    . HOH   F 4 .   ? 27.741 -26.620 -0.485  1.00 34.55 ?  353 HOH   B O    1 
HETATM 7299 O O    . HOH   F 4 .   ? 62.535 -20.125 -4.809  1.00 46.05 ?  354 HOH   B O    1 
HETATM 7300 O O    . HOH   F 4 .   ? 33.970 -7.829  11.497  1.00 40.76 ?  355 HOH   B O    1 
HETATM 7301 O O    . HOH   F 4 .   ? 55.753 -8.268  10.871  1.00 25.28 ?  356 HOH   B O    1 
HETATM 7302 O O    . HOH   F 4 .   ? 23.181 -23.619 6.904   1.00 36.75 ?  357 HOH   B O    1 
HETATM 7303 O O    . HOH   F 4 .   ? 56.618 -7.274  3.070   1.00 27.48 ?  358 HOH   B O    1 
HETATM 7304 O O    . HOH   F 4 .   ? 36.128 -8.477  -9.700  1.00 36.01 ?  359 HOH   B O    1 
HETATM 7305 O O    . HOH   F 4 .   ? 56.869 -21.602 -16.347 1.00 41.25 ?  360 HOH   B O    1 
HETATM 7306 O O    . HOH   F 4 .   ? 61.515 -19.898 1.827   1.00 37.66 ?  361 HOH   B O    1 
HETATM 7307 O O    . HOH   F 4 .   ? 40.285 -8.801  9.922   1.00 37.57 ?  362 HOH   B O    1 
HETATM 7308 O O    . HOH   F 4 .   ? 27.160 -25.936 -11.256 1.00 37.26 ?  363 HOH   B O    1 
HETATM 7309 O O    . HOH   F 4 .   ? 40.432 -11.277 -13.904 1.00 33.83 ?  364 HOH   B O    1 
HETATM 7310 O O    . HOH   F 4 .   ? 43.205 -12.679 -21.096 1.00 43.76 ?  365 HOH   B O    1 
HETATM 7311 O O    . HOH   F 4 .   ? 48.225 -26.451 8.876   1.00 44.60 ?  366 HOH   B O    1 
HETATM 7312 O O    . HOH   F 4 .   ? 36.147 -8.641  9.046   1.00 35.05 ?  367 HOH   B O    1 
HETATM 7313 O O    . HOH   F 4 .   ? 54.242 -5.728  2.985   1.00 35.60 ?  368 HOH   B O    1 
HETATM 7314 O O    . HOH   F 4 .   ? 32.591 -23.587 14.106  1.00 44.15 ?  369 HOH   B O    1 
HETATM 7315 O O    . HOH   F 4 .   ? 58.952 -10.432 9.233   1.00 36.54 ?  370 HOH   B O    1 
HETATM 7316 O O    . HOH   F 4 .   ? 41.840 -10.107 -17.452 1.00 53.90 ?  371 HOH   B O    1 
HETATM 7317 O O    . HOH   F 4 .   ? 39.885 -6.962  7.894   1.00 41.58 ?  372 HOH   B O    1 
HETATM 7318 O O    . HOH   F 4 .   ? 52.070 -12.894 13.337  1.00 29.99 ?  373 HOH   B O    1 
HETATM 7319 O O    . HOH   F 4 .   ? 63.046 -12.449 6.964   1.00 38.43 ?  374 HOH   B O    1 
HETATM 7320 O O    . HOH   F 4 .   ? 56.055 -7.722  -0.651  1.00 36.04 ?  375 HOH   B O    1 
HETATM 7321 O O    . HOH   F 4 .   ? 41.892 -6.677  -4.887  1.00 47.98 ?  376 HOH   B O    1 
HETATM 7322 O O    . HOH   F 4 .   ? 36.527 -22.854 13.356  1.00 33.52 ?  377 HOH   B O    1 
HETATM 7323 O O    . HOH   F 4 .   ? 42.659 -17.139 -23.075 1.00 47.28 ?  378 HOH   B O    1 
HETATM 7324 O O    . HOH   F 4 .   ? 40.154 -7.681  3.171   1.00 39.41 ?  379 HOH   B O    1 
HETATM 7325 O O    . HOH   F 4 .   ? 38.024 -10.480 10.060  1.00 29.46 ?  380 HOH   B O    1 
HETATM 7326 O O    . HOH   F 4 .   ? 44.090 -5.575  -3.548  1.00 42.10 ?  381 HOH   B O    1 
HETATM 7327 O O    . HOH   F 4 .   ? 39.620 -14.075 15.676  1.00 53.43 ?  382 HOH   B O    1 
HETATM 7328 O O    . HOH   F 4 .   ? 60.482 -22.209 2.940   1.00 50.64 ?  383 HOH   B O    1 
HETATM 7329 O O    . HOH   F 4 .   ? 52.883 -29.911 7.284   1.00 24.43 ?  384 HOH   B O    1 
HETATM 7330 O O    . HOH   F 4 .   ? 46.782 -5.383  2.887   1.00 39.73 ?  385 HOH   B O    1 
HETATM 7331 O O    . HOH   F 4 .   ? 25.766 -18.801 -11.807 1.00 41.75 ?  386 HOH   B O    1 
HETATM 7332 O O    . HOH   F 4 .   ? 41.015 -9.762  15.821  1.00 50.94 ?  387 HOH   B O    1 
HETATM 7333 O O    . HOH   F 4 .   ? 23.893 -20.826 -7.545  1.00 31.35 ?  388 HOH   B O    1 
HETATM 7334 O O    . HOH   F 4 .   ? 35.429 -33.748 7.488   1.00 45.32 ?  389 HOH   B O    1 
HETATM 7335 O O    . HOH   F 4 .   ? 35.244 -20.349 13.340  1.00 34.85 ?  390 HOH   B O    1 
HETATM 7336 O O    . HOH   F 4 .   ? 23.126 -23.752 1.555   1.00 37.09 ?  391 HOH   B O    1 
HETATM 7337 O O    . HOH   F 4 .   ? 40.775 -6.563  -0.871  1.00 27.64 ?  392 HOH   B O    1 
HETATM 7338 O O    . HOH   F 4 .   ? 44.181 -31.722 -3.731  1.00 44.52 ?  393 HOH   B O    1 
HETATM 7339 O O    . HOH   F 4 .   ? 27.987 -27.061 2.370   1.00 30.76 ?  394 HOH   B O    1 
HETATM 7340 O O    . HOH   F 4 .   ? 26.622 -27.910 -13.417 1.00 37.63 ?  395 HOH   B O    1 
HETATM 7341 O O    . HOH   F 4 .   ? 24.633 -20.578 -10.503 1.00 41.90 ?  396 HOH   B O    1 
HETATM 7342 O O    . HOH   F 4 .   ? 34.331 -33.435 9.695   1.00 40.78 ?  397 HOH   B O    1 
HETATM 7343 O O    . HOH   F 4 .   ? 26.840 -30.649 -12.558 1.00 30.58 ?  398 HOH   B O    1 
HETATM 7344 O O    . HOH   F 4 .   ? 50.687 -30.811 8.816   1.00 31.85 ?  399 HOH   B O    1 
HETATM 7345 O O    . HOH   F 4 .   ? 45.658 -20.083 15.279  1.00 49.55 ?  400 HOH   B O    1 
HETATM 7346 O O    . HOH   F 4 .   ? 57.615 -6.491  -2.261  1.00 34.91 ?  401 HOH   B O    1 
HETATM 7347 O O    . HOH   F 4 .   ? 40.923 -11.749 -22.205 1.00 42.97 ?  402 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   ? 0.7555 0.7658 0.8714 -0.0116 -0.0405 0.0868  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.7121 0.7136 0.8012 -0.0063 -0.0106 0.0196  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.7529 0.7631 0.8583 -0.0137 -0.0391 0.0874  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.7082 0.7096 0.7923 -0.0068 -0.0104 0.0198  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.7329 0.7466 0.8189 -0.0234 -0.0381 0.0913  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6890 0.6916 0.7537 -0.0097 -0.0113 0.0204  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.7366 0.7509 0.8429 -0.0219 -0.0410 0.0934  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6921 0.6947 0.7652 -0.0094 -0.0117 0.0205  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.7673 0.7746 0.8727 -0.0084 -0.0384 0.0839  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7203 0.7207 0.8127 -0.0050 -0.0095 0.0192  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.7720 0.7779 0.8739 -0.0061 -0.0384 0.0828  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7241 0.7239 0.8179 -0.0042 -0.0092 0.0190  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.7724 0.7789 0.8750 -0.0072 -0.0378 0.0833  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7249 0.7250 0.8182 -0.0045 -0.0092 0.0193  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.7049 0.7222 0.7425 -0.0357 -0.0321 0.0927  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.6633 0.6673 0.6968 -0.0133 -0.0115 0.0206  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.6724 0.6944 0.6546 -0.0488 -0.0253 0.0917  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.6345 0.6403 0.6344 -0.0169 -0.0118 0.0198  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.6237 0.6633 0.6010 -0.0650 -0.0095 0.0718  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5966 0.6068 0.5969 -0.0217 -0.0082 0.0144  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.6250 0.6654 0.5920 -0.0642 -0.0113 0.0736  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.5982 0.6087 0.5958 -0.0219 -0.0083 0.0156  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.6840 0.6952 0.6121 -0.0471 -0.0330 0.1116  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.6415 0.6451 0.6063 -0.0161 -0.0155 0.0244  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.6920 0.6943 0.5711 -0.0461 -0.0404 0.1290  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.6465 0.6482 0.5809 -0.0154 -0.0190 0.0280  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.6962 0.6941 0.5567 -0.0463 -0.0478 0.1355  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.6485 0.6495 0.5731 -0.0152 -0.0215 0.0290  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.6935 0.6937 0.5618 -0.0449 -0.0395 0.1368  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.6476 0.6489 0.5744 -0.0149 -0.0193 0.0302  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.5716 0.6275 0.5533 -0.0844 0.0091  0.0512  5   SER   A N   
60   N N   B SER   A 5   ? 0.5560 0.5702 0.5581 -0.0265 -0.0046 0.0076  5   SER   A N   
61   C CA  A SER   A 5   ? 0.5167 0.5899 0.5075 -0.1037 0.0327  0.0332  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.5137 0.5321 0.5184 -0.0312 -0.0004 0.0012  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4570 0.5408 0.4376 -0.1231 0.0558  0.0317  5   SER   A C   
64   C C   B SER   A 5   ? 0.4689 0.4895 0.4658 -0.0344 0.0028  -0.0031 5   SER   A C   
65   O O   A SER   A 5   ? 0.4602 0.5436 0.4320 -0.1209 0.0617  0.0263  5   SER   A O   
66   O O   B SER   A 5   ? 0.4692 0.4900 0.4626 -0.0343 0.0036  -0.0044 5   SER   A O   
67   C CB  A SER   A 5   ? 0.5224 0.6002 0.5425 -0.1040 0.0341  0.0193  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.5159 0.5355 0.5349 -0.0323 0.0004  -0.0010 5   SER   A CB  
69   O OG  A SER   A 5   ? 0.5258 0.6037 0.5596 -0.1055 0.0347  0.0112  5   SER   A OG  
70   O OG  B SER   A 5   ? 0.5172 0.5374 0.5414 -0.0332 0.0006  -0.0024 5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3922 0.4890 0.3628 -0.1424 0.0709  0.0431  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.4234 0.4465 0.4153 -0.0372 0.0045  -0.0049 6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.3315 0.4344 0.2930 -0.1549 0.0719  0.0609  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3784 0.4035 0.3642 -0.0392 0.0051  -0.0046 6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.3204 0.4258 0.2864 -0.1566 0.0788  0.0554  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3553 0.3791 0.3505 -0.0410 0.0123  -0.0042 6   PHE   A C   
87   O O   A PHE   A 6   ? 0.3279 0.4342 0.3182 -0.1554 0.0752  0.0667  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3579 0.3818 0.3606 -0.0398 0.0131  -0.0035 6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.3029 0.3896 0.2607 -0.1522 0.0453  0.0761  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.3583 0.3850 0.3343 -0.0394 0.0013  -0.0045 6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2799 0.3533 0.2416 -0.1398 0.0194  0.0669  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.3416 0.3686 0.3093 -0.0398 -0.0026 -0.0045 6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2641 0.3375 0.2329 -0.1300 0.0132  0.0591  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.3342 0.3608 0.2954 -0.0397 -0.0040 -0.0047 6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2880 0.3403 0.2534 -0.1191 0.0208  0.0711  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.3349 0.3621 0.3007 -0.0399 -0.0022 -0.0042 6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2639 0.3255 0.2372 -0.1238 0.0150  0.0651  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.3307 0.3570 0.2888 -0.0388 -0.0046 -0.0022 6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2848 0.3318 0.2583 -0.1128 0.0154  0.0626  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.3308 0.3577 0.2944 -0.0400 -0.0031 -0.0037 6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2738 0.3230 0.2459 -0.1188 0.0106  0.0575  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.3295 0.3568 0.2880 -0.0384 -0.0045 -0.0028 6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.3047 0.4027 0.2598 -0.1541 0.0815  0.0420  7   SER   A N   
122  N N   B SER   A 7   ? 0.3293 0.3520 0.3284 -0.0441 0.0184  -0.0055 7   SER   A N   
123  C CA  A SER   A 7   ? 0.3016 0.3911 0.2674 -0.1324 0.0758  0.0138  7   SER   A CA  
124  C CA  B SER   A 7   ? 0.3035 0.3237 0.3051 -0.0478 0.0233  -0.0074 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2801 0.3512 0.2261 -0.1190 0.0801  0.0139  7   SER   A C   
126  C C   B SER   A 7   ? 0.2790 0.2960 0.2743 -0.0516 0.0317  -0.0057 7   SER   A C   
127  O O   A SER   A 7   ? 0.3011 0.3496 0.2110 -0.1198 0.0835  0.0208  7   SER   A O   
128  O O   B SER   A 7   ? 0.2760 0.2957 0.2737 -0.0559 0.0391  -0.0034 7   SER   A O   
129  C CB  A SER   A 7   ? 0.3227 0.4132 0.3091 -0.1214 0.0681  -0.0054 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.3043 0.3229 0.3122 -0.0451 0.0222  -0.0106 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.3442 0.4269 0.3466 -0.1106 0.0516  -0.0280 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3056 0.3242 0.3229 -0.0439 0.0187  -0.0156 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2461 0.3151 0.2199 -0.1018 0.0723  0.0021  8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2581 0.2689 0.2454 -0.0502 0.0345  -0.0101 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.2340 0.2716 0.2312 -0.0730 0.0540  0.0070  8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2415 0.2442 0.2211 -0.0413 0.0390  -0.0081 8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.2007 0.2435 0.2234 -0.0471 0.0453  0.0123  8   GLY   A C   
148  C C   B GLY   A 8   ? 0.2229 0.2228 0.1978 -0.0335 0.0429  -0.0072 8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1964 0.2426 0.2426 -0.0257 0.0441  -0.0065 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.2227 0.2222 0.2026 -0.0281 0.0453  -0.0067 8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1805 0.2326 0.2297 -0.0323 0.0462  0.0386  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.2052 0.2028 0.1774 -0.0296 0.0460  -0.0118 9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1698 0.2182 0.2129 -0.0256 0.0383  0.0457  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1909 0.1856 0.1673 -0.0263 0.0434  -0.0139 9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1621 0.1904 0.2002 -0.0075 0.0387  0.0605  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1850 0.1682 0.1596 -0.0207 0.0490  -0.0169 9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1893 0.2125 0.2137 -0.0016 0.0178  0.0541  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1884 0.1576 0.1383 -0.0123 0.0618  -0.0332 9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1652 0.2407 0.2144 -0.0195 0.0340  0.0506  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1805 0.1864 0.1623 -0.0223 0.0383  -0.0082 9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1626 0.2510 0.2087 -0.0097 0.0363  0.0395  9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1716 0.1870 0.1568 -0.0152 0.0388  -0.0016 9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1773 0.2626 0.2276 -0.0308 0.0333  0.0317  9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1710 0.1872 0.1635 -0.0187 0.0362  -0.0042 9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1624 0.2432 0.2189 -0.0100 0.0287  0.0541  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1703 0.1874 0.1624 -0.0171 0.0357  0.0044  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1828 0.2671 0.2523 -0.0357 0.0422  0.0230  9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1746 0.1870 0.1748 -0.0203 0.0368  -0.0060 9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1725 0.2499 0.2187 -0.0136 0.0332  0.0377  9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1719 0.1894 0.1638 -0.0194 0.0350  -0.0030 9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1762 0.2638 0.2521 -0.0321 0.0476  0.0309  9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1749 0.1893 0.1810 -0.0242 0.0370  -0.0052 9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1782 0.2752 0.2768 -0.0494 0.0638  0.0258  9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1827 0.1889 0.1979 -0.0309 0.0377  -0.0069 9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1583 0.1770 0.1982 -0.0114 0.0322  0.0420  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1821 0.1679 0.1709 -0.0242 0.0364  -0.0033 10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1566 0.1801 0.1998 -0.0217 0.0226  0.0495  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1755 0.1724 0.1678 -0.0369 0.0382  0.0072  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1647 0.1738 0.1790 -0.0264 0.0086  0.0435  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1702 0.1542 0.1652 -0.0514 0.0429  0.0017  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1686 0.1565 0.1712 -0.0277 0.0242  0.0288  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1733 0.1478 0.1651 -0.0462 0.0530  -0.0014 10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1574 0.1796 0.2366 -0.0206 0.0078  0.0710  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1796 0.1989 0.1853 -0.0307 0.0289  0.0130  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1734 0.1886 0.2888 -0.0051 -0.0256 0.0726  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1892 0.2240 0.2051 -0.0214 0.0144  0.0081  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.2002 0.2014 0.3258 -0.0146 -0.0084 0.0630  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.1912 0.2343 0.2092 -0.0113 0.0070  0.0010  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.2017 0.2142 0.3173 0.0022  -0.0269 0.0648  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.1907 0.2313 0.2188 -0.0210 0.0090  0.0092  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1676 0.1814 0.1758 -0.0318 0.0021  0.0571  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1604 0.1471 0.1674 -0.0663 0.0466  0.0038  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1742 0.1714 0.1831 -0.0474 -0.0071 0.0496  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1599 0.1508 0.1863 -0.0650 0.0315  0.0033  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1709 0.1812 0.1741 -0.0584 -0.0081 0.0358  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1598 0.1546 0.1947 -0.0653 0.0374  0.0070  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1910 0.2056 0.1988 -0.0781 -0.0070 0.0098  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1657 0.1502 0.2154 -0.0784 0.0398  -0.0076 11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1899 0.1571 0.1755 -0.0508 -0.0186 0.0299  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1664 0.1580 0.1946 -0.0521 0.0185  0.0048  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.2053 0.1576 0.1806 -0.0482 -0.0177 0.0407  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1725 0.1596 0.1987 -0.0432 0.0149  0.0036  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.2205 0.1567 0.1812 -0.0470 -0.0151 0.0366  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.1791 0.1672 0.2023 -0.0300 0.0188  0.0139  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.2359 0.1670 0.1868 -0.0406 -0.0127 0.0357  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.1794 0.1687 0.2124 -0.0236 0.0165  0.0242  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.2397 0.1676 0.1974 -0.0287 -0.0156 0.0587  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.1786 0.1666 0.2108 -0.0214 0.0113  0.0287  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1510 0.1859 0.1770 -0.0419 -0.0122 0.0368  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1566 0.1593 0.1810 -0.0568 0.0336  0.0184  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1508 0.2043 0.1675 -0.0240 -0.0096 0.0529  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1613 0.1693 0.1652 -0.0437 0.0234  0.0296  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1594 0.1963 0.1608 -0.0351 -0.0071 0.0513  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1637 0.1689 0.1527 -0.0441 0.0192  0.0238  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1639 0.2099 0.1701 -0.0329 -0.0040 0.0396  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1594 0.1643 0.1405 -0.0506 0.0288  0.0396  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1718 0.2171 0.1956 -0.0177 -0.0080 0.0637  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1678 0.1741 0.1625 -0.0389 0.0196  0.0353  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1699 0.2260 0.2212 -0.0137 -0.0019 0.0741  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1726 0.1817 0.1685 -0.0339 0.0232  0.0347  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1949 0.2329 0.2287 -0.0038 0.0124  0.0778  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1813 0.1857 0.1599 -0.0290 0.0258  0.0354  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1682 0.2307 0.2497 -0.0188 -0.0132 0.0723  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1727 0.1836 0.1862 -0.0351 0.0211  0.0359  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1577 0.1751 0.1648 -0.0320 -0.0036 0.0358  13  THR   A N   
320  N N   B THR   A 13  ? 0.1687 0.1712 0.1556 -0.0356 0.0103  0.0113  13  THR   A N   
321  C CA  A THR   A 13  ? 0.1648 0.1743 0.1722 -0.0371 0.0048  0.0409  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1723 0.1745 0.1541 -0.0294 0.0105  0.0042  13  THR   A CA  
323  C C   A THR   A 13  ? 0.1638 0.1793 0.1908 -0.0388 -0.0066 0.0481  13  THR   A C   
324  C C   B THR   A 13  ? 0.1614 0.1730 0.1554 -0.0274 0.0107  0.0098  13  THR   A C   
325  O O   A THR   A 13  ? 0.1732 0.1822 0.1921 -0.0438 -0.0238 0.0520  13  THR   A O   
326  O O   B THR   A 13  ? 0.1612 0.1731 0.1547 -0.0214 0.0123  0.0149  13  THR   A O   
327  C CB  A THR   A 13  ? 0.1721 0.1920 0.1835 -0.0336 0.0045  0.0397  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1819 0.1778 0.1476 -0.0318 0.0065  -0.0063 13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1603 0.1946 0.1857 -0.0441 -0.0055 0.0497  13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1890 0.1758 0.1522 -0.0354 0.0036  -0.0063 13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1738 0.2069 0.2105 -0.0403 0.0095  0.0215  13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1862 0.1808 0.1399 -0.0299 0.0121  -0.0198 13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1687 0.1804 0.2122 -0.0486 -0.0044 0.0576  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1598 0.1746 0.1726 -0.0230 0.0090  0.0044  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1753 0.1875 0.2406 -0.0396 -0.0200 0.0702  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1586 0.1720 0.1704 -0.0169 0.0076  0.0069  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1648 0.1820 0.2147 -0.0362 -0.0125 0.0635  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1493 0.1569 0.1339 -0.0153 0.0116  0.0041  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1917 0.1852 0.2243 -0.0403 -0.0087 0.0565  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1569 0.1599 0.1438 -0.0051 0.0237  -0.0045 14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.2077 0.2095 0.3061 -0.0433 -0.0344 0.0920  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.1735 0.1939 0.2229 -0.0083 0.0022  0.0072  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.2447 0.2539 0.3843 -0.0399 -0.0280 0.0901  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.1818 0.2128 0.2692 -0.0043 -0.0003 0.0052  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.2583 0.2754 0.4115 -0.0291 -0.0356 0.1094  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.1899 0.2231 0.2814 0.0082  -0.0072 0.0109  14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.2636 0.2743 0.4224 -0.0325 -0.0410 0.0537  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.1792 0.2187 0.3005 -0.0092 -0.0011 -0.0009 14  ASP   A OD2 
371  N N   A ASN   A 15  ? 0.1548 0.1746 0.1933 -0.0304 0.0037  0.0590  15  ASN   A N   
372  N N   B ASN   A 15  ? 0.1407 0.1374 0.1196 -0.0242 0.0156  0.0123  15  ASN   A N   
373  C CA  A ASN   A 15  ? 0.1630 0.1734 0.1947 -0.0154 -0.0043 0.0361  15  ASN   A CA  
374  C CA  B ASN   A 15  ? 0.1419 0.1265 0.1305 -0.0211 0.0147  0.0045  15  ASN   A CA  
375  C C   A ASN   A 15  ? 0.1595 0.1676 0.1972 -0.0169 -0.0072 0.0447  15  ASN   A C   
376  C C   B ASN   A 15  ? 0.1436 0.1257 0.1374 -0.0190 0.0122  -0.0002 15  ASN   A C   
377  O O   A ASN   A 15  ? 0.1617 0.1710 0.2201 -0.0259 -0.0157 0.0292  15  ASN   A O   
378  O O   B ASN   A 15  ? 0.1459 0.1233 0.1572 -0.0132 0.0097  0.0046  15  ASN   A O   
379  C CB  A ASN   A 15  ? 0.1665 0.1756 0.1885 -0.0132 0.0046  0.0381  15  ASN   A CB  
380  C CB  B ASN   A 15  ? 0.1365 0.1161 0.1244 -0.0245 0.0100  0.0014  15  ASN   A CB  
381  C CG  A ASN   A 15  ? 0.1640 0.1802 0.2019 -0.0171 0.0105  0.0174  15  ASN   A CG  
382  C CG  B ASN   A 15  ? 0.1389 0.1207 0.1363 -0.0230 0.0100  -0.0076 15  ASN   A CG  
383  O OD1 A ASN   A 15  ? 0.1781 0.1878 0.2189 -0.0310 0.0163  0.0241  15  ASN   A OD1 
384  O OD1 B ASN   A 15  ? 0.1446 0.1232 0.1257 -0.0301 0.0207  -0.0187 15  ASN   A OD1 
385  N ND2 A ASN   A 15  ? 0.1663 0.1842 0.1957 -0.0158 0.0026  0.0219  15  ASN   A ND2 
386  N ND2 B ASN   A 15  ? 0.1442 0.1309 0.1454 -0.0215 0.0035  0.0006  15  ASN   A ND2 
399  N N   A VAL   A 16  ? 0.1597 0.1651 0.2029 -0.0174 -0.0019 0.0545  16  VAL   A N   
400  N N   B VAL   A 16  ? 0.1452 0.1300 0.1290 -0.0275 0.0095  0.0009  16  VAL   A N   
401  C CA  A VAL   A 16  ? 0.1651 0.1701 0.2006 -0.0178 -0.0115 0.0526  16  VAL   A CA  
402  C CA  B VAL   A 16  ? 0.1448 0.1323 0.1289 -0.0335 0.0110  -0.0006 16  VAL   A CA  
403  C C   A VAL   A 16  ? 0.1626 0.1723 0.2053 -0.0253 -0.0072 0.0552  16  VAL   A C   
404  C C   B VAL   A 16  ? 0.1436 0.1341 0.1330 -0.0405 0.0184  -0.0042 16  VAL   A C   
405  O O   A VAL   A 16  ? 0.1637 0.1618 0.2141 -0.0242 0.0097  0.0422  16  VAL   A O   
406  O O   B VAL   A 16  ? 0.1388 0.1295 0.1364 -0.0514 0.0191  -0.0009 16  VAL   A O   
407  C CB  A VAL   A 16  ? 0.1704 0.1803 0.1946 -0.0021 0.0014  0.0452  16  VAL   A CB  
408  C CB  B VAL   A 16  ? 0.1469 0.1303 0.1278 -0.0310 0.0157  -0.0019 16  VAL   A CB  
409  C CG1 A VAL   A 16  ? 0.1796 0.1889 0.2031 0.0006  0.0024  0.0434  16  VAL   A CG1 
410  C CG1 B VAL   A 16  ? 0.1467 0.1313 0.1346 -0.0327 0.0115  -0.0024 16  VAL   A CG1 
411  C CG2 A VAL   A 16  ? 0.1788 0.1877 0.2172 0.0051  0.0215  0.0354  16  VAL   A CG2 
412  C CG2 B VAL   A 16  ? 0.1440 0.1262 0.1210 -0.0419 0.0298  -0.0058 16  VAL   A CG2 
431  N N   A TYR   A 17  ? 0.1553 0.1591 0.2024 -0.0233 -0.0004 0.0538  17  TYR   A N   
432  N N   B TYR   A 17  ? 0.1438 0.1382 0.1418 -0.0357 0.0382  -0.0017 17  TYR   A N   
433  C CA  A TYR   A 17  ? 0.1611 0.1544 0.1945 -0.0245 0.0053  0.0471  17  TYR   A CA  
434  C CA  B TYR   A 17  ? 0.1517 0.1468 0.1497 -0.0344 0.0397  -0.0022 17  TYR   A CA  
435  C C   A TYR   A 17  ? 0.1605 0.1571 0.2063 -0.0159 0.0040  0.0511  17  TYR   A C   
436  C C   B TYR   A 17  ? 0.1599 0.1556 0.1520 -0.0306 0.0326  -0.0138 17  TYR   A C   
437  O O   A TYR   A 17  ? 0.1427 0.1554 0.1984 -0.0311 0.0020  0.0550  17  TYR   A O   
438  O O   B TYR   A 17  ? 0.1548 0.1533 0.1466 -0.0294 0.0420  -0.0244 17  TYR   A O   
439  C CB  A TYR   A 17  ? 0.1839 0.1575 0.2077 -0.0286 -0.0177 0.0459  17  TYR   A CB  
440  C CB  B TYR   A 17  ? 0.1553 0.1448 0.1581 -0.0345 0.0289  0.0006  17  TYR   A CB  
441  C CG  A TYR   A 17  ? 0.2183 0.1691 0.1978 -0.0307 -0.0271 0.0326  17  TYR   A CG  
442  C CG  B TYR   A 17  ? 0.1673 0.1478 0.1695 -0.0299 0.0184  0.0025  17  TYR   A CG  
443  C CD1 A TYR   A 17  ? 0.2380 0.1786 0.2215 -0.0174 -0.0283 0.0385  17  TYR   A CD1 
444  C CD1 B TYR   A 17  ? 0.1735 0.1533 0.1804 -0.0261 0.0101  -0.0020 17  TYR   A CD1 
445  C CD2 A TYR   A 17  ? 0.2375 0.1722 0.1776 -0.0506 -0.0245 0.0258  17  TYR   A CD2 
446  C CD2 B TYR   A 17  ? 0.1706 0.1469 0.1718 -0.0313 0.0123  0.0068  17  TYR   A CD2 
447  C CE1 A TYR   A 17  ? 0.2522 0.1844 0.2196 -0.0181 -0.0244 0.0388  17  TYR   A CE1 
448  C CE1 B TYR   A 17  ? 0.1774 0.1536 0.1792 -0.0253 0.0048  -0.0022 17  TYR   A CE1 
449  C CE2 A TYR   A 17  ? 0.2593 0.1865 0.1918 -0.0445 -0.0285 0.0250  17  TYR   A CE2 
450  C CE2 B TYR   A 17  ? 0.1752 0.1425 0.1774 -0.0280 0.0071  0.0009  17  TYR   A CE2 
451  C CZ  A TYR   A 17  ? 0.2674 0.1816 0.1903 -0.0331 -0.0296 0.0366  17  TYR   A CZ  
452  C CZ  B TYR   A 17  ? 0.1771 0.1455 0.1811 -0.0263 0.0011  0.0027  17  TYR   A CZ  
453  O OH  A TYR   A 17  ? 0.2893 0.1841 0.2108 -0.0224 -0.0211 0.0264  17  TYR   A OH  
454  O OH  B TYR   A 17  ? 0.1763 0.1446 0.1854 -0.0200 -0.0020 0.0006  17  TYR   A OH  
473  N N   A ILE   A 18  ? 0.1556 0.1705 0.2096 -0.0177 0.0053  0.0738  18  ILE   A N   
474  N N   B ILE   A 18  ? 0.1682 0.1723 0.1573 -0.0303 0.0174  0.0015  18  ILE   A N   
475  C CA  A ILE   A 18  ? 0.1439 0.1745 0.2047 -0.0204 0.0047  0.0706  18  ILE   A CA  
476  C CA  B ILE   A 18  ? 0.1717 0.1826 0.1440 -0.0233 -0.0004 0.0026  18  ILE   A CA  
477  C C   A ILE   A 18  ? 0.1411 0.1849 0.2173 -0.0359 0.0090  0.0694  18  ILE   A C   
478  C C   B ILE   A 18  ? 0.1686 0.1974 0.1310 -0.0194 -0.0139 0.0012  18  ILE   A C   
479  O O   A ILE   A 18  ? 0.1385 0.1898 0.2068 -0.0362 0.0028  0.0678  18  ILE   A O   
480  O O   B ILE   A 18  ? 0.1672 0.2087 0.1389 -0.0171 -0.0177 -0.0000 18  ILE   A O   
481  C CB  A ILE   A 18  ? 0.1588 0.1739 0.1911 -0.0102 0.0181  0.0667  18  ILE   A CB  
482  C CB  B ILE   A 18  ? 0.1726 0.1758 0.1428 -0.0298 0.0090  0.0103  18  ILE   A CB  
483  C CG1 A ILE   A 18  ? 0.1735 0.1920 0.1855 0.0126  0.0197  0.0664  18  ILE   A CG1 
484  C CG1 B ILE   A 18  ? 0.1783 0.1778 0.1551 -0.0343 0.0290  0.0210  18  ILE   A CG1 
485  C CG2 A ILE   A 18  ? 0.1711 0.1775 0.2036 -0.0162 0.0087  0.0652  18  ILE   A CG2 
486  C CG2 B ILE   A 18  ? 0.1748 0.1776 0.1537 -0.0344 0.0008  0.0131  18  ILE   A CG2 
487  C CD1 A ILE   A 18  ? 0.1941 0.2077 0.1904 0.0319  0.0157  0.0675  18  ILE   A CD1 
488  C CD1 B ILE   A 18  ? 0.1815 0.1822 0.1717 -0.0330 0.0355  0.0126  18  ILE   A CD1 
511  N N   A LYS   A 19  ? 0.1464 0.1944 0.2272 -0.0207 0.0418  0.0653  19  LYS   A N   
512  N N   B LYS   A 19  ? 0.1653 0.1964 0.1270 -0.0128 -0.0112 -0.0048 19  LYS   A N   
513  C CA  A LYS   A 19  ? 0.1786 0.2054 0.2071 -0.0112 0.0441  0.0560  19  LYS   A CA  
514  C CA  B LYS   A 19  ? 0.1718 0.1991 0.1567 -0.0037 0.0072  -0.0012 19  LYS   A CA  
515  C C   A LYS   A 19  ? 0.1773 0.1869 0.2062 -0.0060 0.0487  0.0497  19  LYS   A C   
516  C C   B LYS   A 19  ? 0.1646 0.1900 0.1583 0.0034  0.0091  0.0045  19  LYS   A C   
517  O O   A LYS   A 19  ? 0.1700 0.1873 0.2093 -0.0081 0.0469  0.0617  19  LYS   A O   
518  O O   B LYS   A 19  ? 0.1624 0.1864 0.1502 -0.0047 -0.0022 0.0144  19  LYS   A O   
519  C CB  A LYS   A 19  ? 0.1938 0.2288 0.2030 -0.0109 0.0497  0.0581  19  LYS   A CB  
520  C CB  B LYS   A 19  ? 0.1767 0.2078 0.1760 -0.0006 0.0198  -0.0019 19  LYS   A CB  
521  C CG  A LYS   A 19  ? 0.2408 0.2419 0.2162 -0.0169 0.0534  0.0499  19  LYS   A CG  
522  C CG  B LYS   A 19  ? 0.1911 0.2133 0.1890 0.0019  0.0260  -0.0033 19  LYS   A CG  
523  C CD  A LYS   A 19  ? 0.2731 0.2630 0.2413 -0.0144 0.0635  0.0417  19  LYS   A CD  
524  C CD  B LYS   A 19  ? 0.2008 0.2223 0.2035 0.0068  0.0322  -0.0001 19  LYS   A CD  
525  C CE  A LYS   A 19  ? 0.2947 0.2705 0.2741 -0.0245 0.0584  0.0320  19  LYS   A CE  
526  C CE  B LYS   A 19  ? 0.2058 0.2284 0.2147 0.0062  0.0321  0.0009  19  LYS   A CE  
527  N NZ  A LYS   A 19  ? 0.3044 0.2736 0.2734 -0.0362 0.0701  0.0230  19  LYS   A NZ  
528  N NZ  B LYS   A 19  ? 0.2089 0.2304 0.2184 0.0075  0.0299  0.0001  19  LYS   A NZ  
555  N N   A ASN   A 20  ? 0.1831 0.1861 0.2413 -0.0129 0.0521  0.0582  20  ASN   A N   
556  N N   B ASN   A 20  ? 0.1585 0.1843 0.1670 0.0124  0.0234  0.0011  20  ASN   A N   
557  C CA  A ASN   A 20  ? 0.1916 0.1954 0.2568 -0.0002 0.0647  0.0494  20  ASN   A CA  
558  C CA  B ASN   A 20  ? 0.1494 0.1785 0.1802 0.0230  0.0318  0.0043  20  ASN   A CA  
559  C C   A ASN   A 20  ? 0.2057 0.2090 0.2594 -0.0109 0.0801  0.0322  20  ASN   A C   
560  C C   B ASN   A 20  ? 0.1570 0.1753 0.1940 0.0280  0.0388  0.0077  20  ASN   A C   
561  O O   A ASN   A 20  ? 0.2231 0.2282 0.2670 -0.0258 0.0760  0.0083  20  ASN   A O   
562  O O   B ASN   A 20  ? 0.1543 0.1688 0.2080 0.0412  0.0384  0.0202  20  ASN   A O   
563  C CB  A ASN   A 20  ? 0.2067 0.1946 0.2682 0.0201  0.0685  0.0579  20  ASN   A CB  
564  C CB  B ASN   A 20  ? 0.1388 0.1745 0.1827 0.0260  0.0362  0.0097  20  ASN   A CB  
565  C CG  A ASN   A 20  ? 0.2250 0.1917 0.3043 0.0354  0.0810  0.0496  20  ASN   A CG  
566  C CG  B ASN   A 20  ? 0.1291 0.1685 0.2002 0.0265  0.0459  0.0062  20  ASN   A CG  
567  O OD1 A ASN   A 20  ? 0.2609 0.2140 0.3755 0.0397  0.0970  0.0397  20  ASN   A OD1 
568  O OD1 B ASN   A 20  ? 0.1243 0.1515 0.2090 0.0319  0.0538  -0.0081 20  ASN   A OD1 
569  N ND2 A ASN   A 20  ? 0.2325 0.1703 0.3044 0.0334  0.0609  0.0720  20  ASN   A ND2 
570  N ND2 B ASN   A 20  ? 0.1404 0.1776 0.2230 0.0173  0.0403  0.0180  20  ASN   A ND2 
583  N N   A ALA   A 21  ? 0.2078 0.2098 0.2645 -0.0077 0.0694  0.0283  21  ALA   A N   
584  N N   B ALA   A 21  ? 0.1677 0.1785 0.2037 0.0187  0.0311  -0.0031 21  ALA   A N   
585  C CA  A ALA   A 21  ? 0.2119 0.2028 0.2613 -0.0085 0.0571  0.0409  21  ALA   A CA  
586  C CA  B ALA   A 21  ? 0.1742 0.1771 0.2072 0.0084  0.0281  -0.0076 21  ALA   A CA  
587  C C   A ALA   A 21  ? 0.1982 0.2019 0.2538 -0.0081 0.0436  0.0431  21  ALA   A C   
588  C C   B ALA   A 21  ? 0.1641 0.1718 0.1937 -0.0072 0.0410  -0.0063 21  ALA   A C   
589  O O   A ALA   A 21  ? 0.1988 0.2102 0.2535 0.0010  0.0440  0.0394  21  ALA   A O   
590  O O   B ALA   A 21  ? 0.1579 0.1643 0.1927 -0.0097 0.0497  -0.0139 21  ALA   A O   
591  C CB  A ALA   A 21  ? 0.2223 0.2009 0.2782 -0.0117 0.0572  0.0382  21  ALA   A CB  
592  C CB  B ALA   A 21  ? 0.1822 0.1798 0.2217 0.0153  0.0199  -0.0163 21  ALA   A CB  
603  N N   A ASP   A 22  ? 0.1990 0.1945 0.2735 -0.0114 0.0422  0.0434  22  ASP   A N   
604  N N   B ASP   A 22  ? 0.1656 0.1740 0.1962 -0.0161 0.0494  0.0046  22  ASP   A N   
605  C CA  A ASP   A 22  ? 0.2021 0.1853 0.2722 -0.0001 0.0273  0.0503  22  ASP   A CA  
606  C CA  B ASP   A 22  ? 0.1684 0.1753 0.1980 -0.0222 0.0505  0.0137  22  ASP   A CA  
607  C C   A ASP   A 22  ? 0.1915 0.1846 0.2223 0.0005  0.0269  0.0488  22  ASP   A C   
608  C C   B ASP   A 22  ? 0.1611 0.1712 0.1730 -0.0336 0.0593  0.0109  22  ASP   A C   
609  O O   A ASP   A 22  ? 0.2027 0.1916 0.2486 -0.0078 0.0264  0.0444  22  ASP   A O   
610  O O   B ASP   A 22  ? 0.1563 0.1722 0.1772 -0.0457 0.0717  0.0076  22  ASP   A O   
611  C CB  A ASP   A 22  ? 0.2264 0.1934 0.3393 0.0007  0.0233  0.0360  22  ASP   A CB  
612  C CB  B ASP   A 22  ? 0.1773 0.1805 0.2242 -0.0113 0.0509  0.0158  22  ASP   A CB  
613  C CG  A ASP   A 22  ? 0.2404 0.2091 0.3977 -0.0058 0.0007  0.0457  22  ASP   A CG  
614  C CG  B ASP   A 22  ? 0.1801 0.1776 0.2341 -0.0069 0.0532  0.0246  22  ASP   A CG  
615  O OD1 A ASP   A 22  ? 0.2411 0.2077 0.4234 -0.0235 -0.0215 0.0607  22  ASP   A OD1 
616  O OD1 B ASP   A 22  ? 0.1825 0.1668 0.2289 -0.0073 0.0606  0.0281  22  ASP   A OD1 
617  O OD2 A ASP   A 22  ? 0.2592 0.2218 0.4429 0.0060  0.0073  0.0369  22  ASP   A OD2 
618  O OD2 B ASP   A 22  ? 0.1766 0.1871 0.2375 -0.0106 0.0583  0.0265  22  ASP   A OD2 
627  N N   A ILE   A 23  ? 0.1879 0.1903 0.2090 -0.0018 0.0349  0.0382  23  ILE   A N   
628  N N   B ILE   A 23  ? 0.1631 0.1696 0.1668 -0.0253 0.0480  0.0094  23  ILE   A N   
629  C CA  A ILE   A 23  ? 0.1826 0.1873 0.1913 -0.0084 0.0370  0.0279  23  ILE   A CA  
630  C CA  B ILE   A 23  ? 0.1617 0.1764 0.1595 -0.0225 0.0286  0.0107  23  ILE   A CA  
631  C C   A ILE   A 23  ? 0.1757 0.1935 0.1883 -0.0107 0.0597  0.0342  23  ILE   A C   
632  C C   B ILE   A 23  ? 0.1748 0.1870 0.1655 -0.0317 0.0284  0.0078  23  ILE   A C   
633  O O   A ILE   A 23  ? 0.1881 0.2067 0.1875 -0.0126 0.0409  0.0110  23  ILE   A O   
634  O O   B ILE   A 23  ? 0.1758 0.1841 0.1601 -0.0299 0.0246  0.0037  23  ILE   A O   
635  C CB  A ILE   A 23  ? 0.1948 0.1832 0.1603 -0.0073 0.0389  0.0294  23  ILE   A CB  
636  C CB  B ILE   A 23  ? 0.1542 0.1675 0.1539 -0.0101 0.0130  0.0154  23  ILE   A CB  
637  C CG1 A ILE   A 23  ? 0.1994 0.1818 0.1702 -0.0049 0.0313  0.0225  23  ILE   A CG1 
638  C CG1 B ILE   A 23  ? 0.1490 0.1651 0.1525 -0.0098 0.0080  0.0049  23  ILE   A CG1 
639  C CG2 A ILE   A 23  ? 0.2056 0.1927 0.1715 -0.0040 0.0453  0.0330  23  ILE   A CG2 
640  C CG2 B ILE   A 23  ? 0.1546 0.1655 0.1496 -0.0011 0.0034  0.0195  23  ILE   A CG2 
641  C CD1 A ILE   A 23  ? 0.2089 0.1816 0.1881 -0.0004 0.0110  0.0072  23  ILE   A CD1 
642  C CD1 B ILE   A 23  ? 0.1433 0.1657 0.1532 -0.0115 0.0001  -0.0020 23  ILE   A CD1 
665  N N   A VAL   A 24  ? 0.1847 0.2001 0.2096 -0.0202 0.0451  0.0180  24  VAL   A N   
666  N N   B VAL   A 24  ? 0.1898 0.1998 0.1912 -0.0397 0.0224  0.0022  24  VAL   A N   
667  C CA  A VAL   A 24  ? 0.2101 0.2101 0.2429 -0.0315 0.0420  0.0108  24  VAL   A CA  
668  C CA  B VAL   A 24  ? 0.2085 0.2110 0.2146 -0.0413 0.0227  0.0038  24  VAL   A CA  
669  C C   A VAL   A 24  ? 0.2125 0.2265 0.2454 -0.0422 0.0492  -0.0054 24  VAL   A C   
670  C C   B VAL   A 24  ? 0.2177 0.2303 0.2256 -0.0344 0.0292  -0.0008 24  VAL   A C   
671  O O   A VAL   A 24  ? 0.2351 0.2281 0.2546 -0.0354 0.0556  -0.0109 24  VAL   A O   
672  O O   B VAL   A 24  ? 0.2245 0.2360 0.2357 -0.0287 0.0332  0.0055  24  VAL   A O   
673  C CB  A VAL   A 24  ? 0.2215 0.2098 0.2783 -0.0306 0.0445  0.0166  24  VAL   A CB  
674  C CB  B VAL   A 24  ? 0.2152 0.2073 0.2309 -0.0467 0.0162  0.0136  24  VAL   A CB  
675  C CG1 A VAL   A 24  ? 0.2247 0.2222 0.3045 -0.0218 0.0430  -0.0054 24  VAL   A CG1 
676  C CG1 B VAL   A 24  ? 0.2228 0.2120 0.2444 -0.0426 0.0135  0.0185  24  VAL   A CG1 
677  C CG2 A VAL   A 24  ? 0.2351 0.2235 0.2945 -0.0263 0.0584  0.0356  24  VAL   A CG2 
678  C CG2 B VAL   A 24  ? 0.2161 0.2016 0.2331 -0.0550 0.0122  0.0118  24  VAL   A CG2 
697  N N   A GLU   A 25  ? 0.2138 0.2519 0.2413 -0.0470 0.0725  -0.0119 25  GLU   A N   
698  N N   B GLU   A 25  ? 0.2243 0.2450 0.2324 -0.0316 0.0391  -0.0058 25  GLU   A N   
699  C CA  A GLU   A 25  ? 0.2342 0.2808 0.2502 -0.0309 0.0812  -0.0171 25  GLU   A CA  
700  C CA  B GLU   A 25  ? 0.2359 0.2602 0.2443 -0.0274 0.0413  -0.0063 25  GLU   A CA  
701  C C   A GLU   A 25  ? 0.2242 0.2881 0.2033 -0.0435 0.0803  -0.0155 25  GLU   A C   
702  C C   B GLU   A 25  ? 0.2334 0.2639 0.2274 -0.0312 0.0455  -0.0055 25  GLU   A C   
703  O O   A GLU   A 25  ? 0.2323 0.3043 0.2164 -0.0464 0.0747  -0.0141 25  GLU   A O   
704  O O   B GLU   A 25  ? 0.2389 0.2660 0.2357 -0.0310 0.0482  -0.0078 25  GLU   A O   
705  C CB  A GLU   A 25  ? 0.2649 0.3080 0.3004 -0.0145 0.0911  -0.0115 25  GLU   A CB  
706  C CB  B GLU   A 25  ? 0.2507 0.2714 0.2737 -0.0220 0.0390  -0.0057 25  GLU   A CB  
707  C CG  A GLU   A 25  ? 0.3073 0.3362 0.3903 -0.0091 0.0777  -0.0104 25  GLU   A CG  
708  C CG  B GLU   A 25  ? 0.2700 0.2847 0.3188 -0.0188 0.0319  -0.0041 25  GLU   A CG  
709  C CD  A GLU   A 25  ? 0.3421 0.3639 0.4672 -0.0018 0.0607  -0.0101 25  GLU   A CD  
710  C CD  B GLU   A 25  ? 0.2867 0.2966 0.3595 -0.0150 0.0237  -0.0042 25  GLU   A CD  
711  O OE1 A GLU   A 25  ? 0.3600 0.3758 0.4868 0.0081  0.0477  -0.0175 25  GLU   A OE1 
712  O OE1 B GLU   A 25  ? 0.2942 0.3036 0.3778 -0.0117 0.0208  -0.0044 25  GLU   A OE1 
713  O OE2 A GLU   A 25  ? 0.3515 0.3736 0.5054 -0.0039 0.0493  -0.0202 25  GLU   A OE2 
714  O OE2 B GLU   A 25  ? 0.2942 0.2994 0.3775 -0.0159 0.0203  -0.0068 25  GLU   A OE2 
727  N N   A GLU   A 26  ? 0.2064 0.2811 0.2091 -0.0639 0.0737  -0.0105 26  GLU   A N   
728  N N   B GLU   A 26  ? 0.2265 0.2654 0.2131 -0.0376 0.0490  -0.0041 26  GLU   A N   
729  C CA  A GLU   A 26  ? 0.2275 0.2838 0.1815 -0.0744 0.0632  -0.0058 26  GLU   A CA  
730  C CA  B GLU   A 26  ? 0.2259 0.2664 0.2010 -0.0448 0.0471  -0.0023 26  GLU   A CA  
731  C C   A GLU   A 26  ? 0.2317 0.2672 0.1585 -0.0703 0.0564  0.0052  26  GLU   A C   
732  C C   B GLU   A 26  ? 0.2254 0.2567 0.1811 -0.0515 0.0520  -0.0015 26  GLU   A C   
733  O O   A GLU   A 26  ? 0.2397 0.2692 0.1662 -0.0801 0.0429  0.0037  26  GLU   A O   
734  O O   B GLU   A 26  ? 0.2294 0.2545 0.1765 -0.0513 0.0547  -0.0030 26  GLU   A O   
735  C CB  A GLU   A 26  ? 0.2485 0.3010 0.2204 -0.0848 0.0552  -0.0002 26  GLU   A CB  
736  C CB  B GLU   A 26  ? 0.2254 0.2749 0.2107 -0.0457 0.0334  -0.0013 26  GLU   A CB  
737  C CG  A GLU   A 26  ? 0.2736 0.3311 0.3011 -0.0902 0.0592  -0.0146 26  GLU   A CG  
738  C CG  B GLU   A 26  ? 0.2249 0.2831 0.2228 -0.0448 0.0248  -0.0025 26  GLU   A CG  
739  C CD  A GLU   A 26  ? 0.2848 0.3456 0.3360 -0.1070 0.0834  -0.0227 26  GLU   A CD  
740  C CD  B GLU   A 26  ? 0.2205 0.2865 0.2206 -0.0472 0.0193  -0.0014 26  GLU   A CD  
741  O OE1 A GLU   A 26  ? 0.2770 0.3658 0.3285 -0.0995 0.1119  -0.0553 26  GLU   A OE1 
742  O OE1 B GLU   A 26  ? 0.2242 0.2933 0.2306 -0.0468 0.0184  0.0017  26  GLU   A OE1 
743  O OE2 A GLU   A 26  ? 0.3044 0.3502 0.3552 -0.1166 0.0849  -0.0147 26  GLU   A OE2 
744  O OE2 B GLU   A 26  ? 0.2140 0.2848 0.1908 -0.0472 0.0142  -0.0042 26  GLU   A OE2 
757  N N   . ALA   A 27  ? 0.2161 0.2507 0.1641 -0.0607 0.0525  -0.0012 27  ALA   A N   
758  C CA  . ALA   A 27  ? 0.2244 0.2673 0.1574 -0.0553 0.0369  -0.0031 27  ALA   A CA  
759  C C   . ALA   A 27  ? 0.2452 0.3017 0.1669 -0.0610 0.0438  -0.0046 27  ALA   A C   
760  O O   . ALA   A 27  ? 0.2409 0.2974 0.1947 -0.0674 0.0271  0.0067  27  ALA   A O   
761  C CB  . ALA   A 27  ? 0.2061 0.2570 0.1608 -0.0549 0.0280  -0.0049 27  ALA   A CB  
768  N N   A LYS   A 28  ? 0.2734 0.3259 0.1866 -0.0636 0.0398  -0.0444 28  LYS   A N   
769  N N   B LYS   A 28  ? 0.2671 0.3150 0.2075 -0.0494 0.0354  -0.0148 28  LYS   A N   
770  C CA  A LYS   A 28  ? 0.3088 0.3637 0.2179 -0.0606 0.0402  -0.0681 28  LYS   A CA  
771  C CA  B LYS   A 28  ? 0.2896 0.3315 0.2505 -0.0376 0.0275  -0.0220 28  LYS   A CA  
772  C C   A LYS   A 28  ? 0.3347 0.3984 0.2116 -0.0681 0.0572  -0.0566 28  LYS   A C   
773  C C   B LYS   A 28  ? 0.3142 0.3519 0.2786 -0.0332 0.0222  -0.0195 28  LYS   A C   
774  O O   A LYS   A 28  ? 0.3476 0.4106 0.2520 -0.0669 0.0319  -0.0635 28  LYS   A O   
775  O O   B LYS   A 28  ? 0.3184 0.3574 0.2873 -0.0330 0.0187  -0.0218 28  LYS   A O   
776  C CB  A LYS   A 28  ? 0.3265 0.3729 0.2788 -0.0450 0.0249  -0.0845 28  LYS   A CB  
777  C CB  B LYS   A 28  ? 0.2900 0.3297 0.2673 -0.0298 0.0253  -0.0277 28  LYS   A CB  
778  C CG  A LYS   A 28  ? 0.3441 0.3800 0.3344 -0.0318 0.0176  -0.0926 28  LYS   A CG  
779  C CG  B LYS   A 28  ? 0.2923 0.3294 0.2798 -0.0223 0.0245  -0.0312 28  LYS   A CG  
780  C CD  A LYS   A 28  ? 0.3632 0.3972 0.4102 -0.0196 0.0106  -0.0881 28  LYS   A CD  
781  C CD  B LYS   A 28  ? 0.2958 0.3322 0.3024 -0.0154 0.0224  -0.0338 28  LYS   A CD  
782  C CE  A LYS   A 28  ? 0.3782 0.4087 0.4554 -0.0122 0.0108  -0.0894 28  LYS   A CE  
783  C CE  B LYS   A 28  ? 0.2998 0.3346 0.3193 -0.0115 0.0219  -0.0383 28  LYS   A CE  
784  N NZ  A LYS   A 28  ? 0.3891 0.4143 0.4921 -0.0054 0.0138  -0.0998 28  LYS   A NZ  
785  N NZ  B LYS   A 28  ? 0.3033 0.3361 0.3272 -0.0099 0.0215  -0.0410 28  LYS   A NZ  
812  N N   A LYS   A 29  ? 0.3431 0.4183 0.1972 -0.0803 0.0972  -0.0303 29  LYS   A N   
813  N N   B LYS   A 29  ? 0.3330 0.3654 0.3018 -0.0300 0.0213  -0.0123 29  LYS   A N   
814  C CA  A LYS   A 29  ? 0.3596 0.4448 0.2250 -0.0905 0.1215  -0.0110 29  LYS   A CA  
815  C CA  B LYS   A 29  ? 0.3524 0.3801 0.3291 -0.0274 0.0203  -0.0062 29  LYS   A CA  
816  C C   A LYS   A 29  ? 0.3708 0.4419 0.2314 -0.1050 0.0986  0.0058  29  LYS   A C   
817  C C   B LYS   A 29  ? 0.3578 0.3799 0.3126 -0.0288 0.0141  -0.0002 29  LYS   A C   
818  O O   A LYS   A 29  ? 0.3887 0.4596 0.2647 -0.0953 0.0956  0.0036  29  LYS   A O   
819  O O   B LYS   A 29  ? 0.3612 0.3844 0.3129 -0.0289 0.0151  0.0018  29  LYS   A O   
820  C CB  A LYS   A 29  ? 0.3692 0.4751 0.2764 -0.0772 0.1489  -0.0083 29  LYS   A CB  
821  C CB  B LYS   A 29  ? 0.3665 0.3941 0.3727 -0.0219 0.0241  -0.0051 29  LYS   A CB  
822  C CG  A LYS   A 29  ? 0.3876 0.5033 0.3571 -0.0597 0.1479  -0.0048 29  LYS   A CG  
823  C CG  B LYS   A 29  ? 0.3806 0.4073 0.4154 -0.0162 0.0260  -0.0035 29  LYS   A CG  
824  C CD  A LYS   A 29  ? 0.4043 0.5248 0.4342 -0.0453 0.1399  -0.0047 29  LYS   A CD  
825  C CD  B LYS   A 29  ? 0.3918 0.4181 0.4530 -0.0112 0.0266  -0.0024 29  LYS   A CD  
826  C CE  A LYS   A 29  ? 0.4158 0.5398 0.4834 -0.0353 0.1342  -0.0076 29  LYS   A CE  
827  C CE  B LYS   A 29  ? 0.3995 0.4261 0.4799 -0.0078 0.0268  -0.0029 29  LYS   A CE  
828  N NZ  A LYS   A 29  ? 0.4212 0.5482 0.5167 -0.0280 0.1266  -0.0090 29  LYS   A NZ  
829  N NZ  B LYS   A 29  ? 0.4038 0.4308 0.4955 -0.0055 0.0257  -0.0025 29  LYS   A NZ  
856  N N   A VAL   A 30  ? 0.3584 0.4187 0.2025 -0.1258 0.0869  0.0162  30  VAL   A N   
857  N N   B VAL   A 30  ? 0.3583 0.3742 0.2987 -0.0300 0.0104  0.0029  30  VAL   A N   
858  C CA  A VAL   A 30  ? 0.3564 0.3955 0.1834 -0.1407 0.0493  0.0276  30  VAL   A CA  
859  C CA  B VAL   A 30  ? 0.3584 0.3679 0.2885 -0.0315 0.0030  0.0077  30  VAL   A CA  
860  C C   A VAL   A 30  ? 0.3541 0.3805 0.1491 -0.1386 0.0262  0.0337  30  VAL   A C   
861  C C   B VAL   A 30  ? 0.3574 0.3641 0.2777 -0.0295 -0.0014 0.0079  30  VAL   A C   
862  O O   A VAL   A 30  ? 0.3631 0.3823 0.1640 -0.1355 0.0180  0.0411  30  VAL   A O   
863  O O   B VAL   A 30  ? 0.3592 0.3650 0.2712 -0.0287 -0.0034 0.0095  30  VAL   A O   
864  C CB  A VAL   A 30  ? 0.3590 0.3859 0.2292 -0.1553 0.0297  0.0324  30  VAL   A CB  
865  C CB  B VAL   A 30  ? 0.3586 0.3649 0.2934 -0.0350 -0.0003 0.0104  30  VAL   A CB  
866  C CG1 A VAL   A 30  ? 0.3664 0.3848 0.2565 -0.1556 0.0274  0.0347  30  VAL   A CG1 
867  C CG1 B VAL   A 30  ? 0.3593 0.3638 0.2984 -0.0357 0.0000  0.0103  30  VAL   A CG1 
868  C CG2 A VAL   A 30  ? 0.3586 0.3847 0.2637 -0.1642 0.0293  0.0298  30  VAL   A CG2 
869  C CG2 B VAL   A 30  ? 0.3590 0.3645 0.2997 -0.0368 -0.0010 0.0128  30  VAL   A CG2 
888  N N   A LYS   A 31  ? 0.3396 0.3650 0.1278 -0.1385 -0.0020 0.0265  31  LYS   A N   
889  N N   B LYS   A 31  ? 0.3537 0.3596 0.2818 -0.0285 -0.0057 0.0072  31  LYS   A N   
890  C CA  A LYS   A 31  ? 0.3470 0.3633 0.1507 -0.1201 -0.0319 0.0318  31  LYS   A CA  
891  C CA  B LYS   A 31  ? 0.3513 0.3573 0.2973 -0.0263 -0.0108 0.0069  31  LYS   A CA  
892  C C   A LYS   A 31  ? 0.3171 0.3352 0.1305 -0.0979 -0.0331 0.0672  31  LYS   A C   
893  C C   B LYS   A 31  ? 0.3302 0.3406 0.2618 -0.0246 -0.0117 0.0147  31  LYS   A C   
894  O O   A LYS   A 31  ? 0.3292 0.3580 0.1598 -0.0921 -0.0507 0.0803  31  LYS   A O   
895  O O   B LYS   A 31  ? 0.3324 0.3454 0.2636 -0.0231 -0.0155 0.0175  31  LYS   A O   
896  C CB  A LYS   A 31  ? 0.3874 0.3926 0.2703 -0.1124 -0.0491 0.0094  31  LYS   A CB  
897  C CB  B LYS   A 31  ? 0.3695 0.3722 0.3554 -0.0254 -0.0150 0.0006  31  LYS   A CB  
898  C CG  A LYS   A 31  ? 0.4309 0.4234 0.4182 -0.0998 -0.0613 -0.0072 31  LYS   A CG  
899  C CG  B LYS   A 31  ? 0.3873 0.3870 0.4196 -0.0236 -0.0194 -0.0043 31  LYS   A CG  
900  C CD  A LYS   A 31  ? 0.4651 0.4503 0.5240 -0.0875 -0.0731 -0.0254 31  LYS   A CD  
901  C CD  B LYS   A 31  ? 0.4017 0.4000 0.4725 -0.0213 -0.0241 -0.0096 31  LYS   A CD  
902  C CE  A LYS   A 31  ? 0.4892 0.4711 0.5914 -0.0778 -0.0822 -0.0402 31  LYS   A CE  
903  C CE  B LYS   A 31  ? 0.4118 0.4103 0.5075 -0.0194 -0.0268 -0.0129 31  LYS   A CE  
904  N NZ  A LYS   A 31  ? 0.5001 0.4766 0.6279 -0.0717 -0.0893 -0.0503 31  LYS   A NZ  
905  N NZ  B LYS   A 31  ? 0.4177 0.4149 0.5299 -0.0178 -0.0284 -0.0161 31  LYS   A NZ  
932  N N   A PRO   A 32  ? 0.2788 0.2965 0.1181 -0.0984 -0.0245 0.0595  32  PRO   A N   
933  N N   B PRO   A 32  ? 0.3061 0.3188 0.2309 -0.0257 -0.0081 0.0163  32  PRO   A N   
934  C CA  A PRO   A 32  ? 0.2714 0.2752 0.1490 -0.0885 -0.0293 0.0803  32  PRO   A CA  
935  C CA  B PRO   A 32  ? 0.2914 0.3044 0.2189 -0.0272 -0.0089 0.0227  32  PRO   A CA  
936  C C   A PRO   A 32  ? 0.2684 0.2694 0.1556 -0.0771 -0.0396 0.0873  32  PRO   A C   
937  C C   B PRO   A 32  ? 0.2765 0.2911 0.2081 -0.0313 -0.0141 0.0312  32  PRO   A C   
938  O O   A PRO   A 32  ? 0.2663 0.2672 0.1764 -0.0772 -0.0509 0.0805  32  PRO   A O   
939  O O   B PRO   A 32  ? 0.2749 0.2903 0.2120 -0.0310 -0.0159 0.0351  32  PRO   A O   
940  C CB  A PRO   A 32  ? 0.2640 0.2736 0.1567 -0.0858 -0.0181 0.0612  32  PRO   A CB  
941  C CB  B PRO   A 32  ? 0.2918 0.3057 0.2180 -0.0240 -0.0054 0.0179  32  PRO   A CB  
942  C CG  A PRO   A 32  ? 0.2626 0.2814 0.1104 -0.0820 -0.0462 0.0438  32  PRO   A CG  
943  C CG  B PRO   A 32  ? 0.2950 0.3090 0.2173 -0.0222 -0.0061 0.0138  32  PRO   A CG  
944  C CD  A PRO   A 32  ? 0.2636 0.2879 0.1063 -0.0869 -0.0365 0.0448  32  PRO   A CD  
945  C CD  B PRO   A 32  ? 0.2992 0.3137 0.2206 -0.0235 -0.0063 0.0135  32  PRO   A CD  
960  N N   A THR   A 33  ? 0.2767 0.2673 0.1649 -0.0647 -0.0449 0.0948  33  THR   A N   
961  N N   B THR   A 33  ? 0.2666 0.2799 0.2018 -0.0350 -0.0190 0.0364  33  THR   A N   
962  C CA  A THR   A 33  ? 0.2781 0.2658 0.1741 -0.0535 -0.0598 0.0863  33  THR   A CA  
963  C CA  B THR   A 33  ? 0.2562 0.2690 0.1976 -0.0384 -0.0243 0.0389  33  THR   A CA  
964  C C   A THR   A 33  ? 0.2470 0.2454 0.1603 -0.0552 -0.0500 0.0678  33  THR   A C   
965  C C   B THR   A 33  ? 0.2377 0.2509 0.1730 -0.0458 -0.0295 0.0437  33  THR   A C   
966  O O   A THR   A 33  ? 0.2404 0.2384 0.1826 -0.0538 -0.0494 0.0732  33  THR   A O   
967  O O   B THR   A 33  ? 0.2352 0.2493 0.1775 -0.0458 -0.0289 0.0451  33  THR   A O   
968  C CB  A THR   A 33  ? 0.3132 0.2904 0.1985 -0.0448 -0.0626 0.1058  33  THR   A CB  
969  C CB  B THR   A 33  ? 0.2657 0.2771 0.2199 -0.0357 -0.0209 0.0415  33  THR   A CB  
970  O OG1 A THR   A 33  ? 0.3395 0.3135 0.2229 -0.0306 -0.0572 0.1195  33  THR   A OG1 
971  O OG1 B THR   A 33  ? 0.2747 0.2848 0.2360 -0.0311 -0.0180 0.0443  33  THR   A OG1 
972  C CG2 A THR   A 33  ? 0.3181 0.2957 0.2128 -0.0391 -0.0777 0.0967  33  THR   A CG2 
973  C CG2 B THR   A 33  ? 0.2665 0.2782 0.2276 -0.0346 -0.0224 0.0394  33  THR   A CG2 
988  N N   . VAL   A 34  ? 0.2224 0.2368 0.1457 -0.0519 -0.0337 0.0505  34  VAL   A N   
989  C CA  . VAL   A 34  ? 0.2039 0.2102 0.1200 -0.0375 -0.0234 0.0405  34  VAL   A CA  
990  C C   . VAL   A 34  ? 0.1925 0.1825 0.1359 -0.0384 -0.0139 0.0381  34  VAL   A C   
991  O O   . VAL   A 34  ? 0.1967 0.1929 0.1645 -0.0459 -0.0136 0.0439  34  VAL   A O   
992  C CB  . VAL   A 34  ? 0.2061 0.2081 0.1441 -0.0393 -0.0025 0.0318  34  VAL   A CB  
993  C CG1 . VAL   A 34  ? 0.2149 0.2050 0.1475 -0.0333 0.0085  0.0219  34  VAL   A CG1 
994  C CG2 . VAL   A 34  ? 0.2151 0.2265 0.1837 -0.0300 -0.0102 0.0361  34  VAL   A CG2 
1005 N N   . VAL   A 35  ? 0.1705 0.1776 0.1367 -0.0388 -0.0061 0.0372  35  VAL   A N   
1006 C CA  . VAL   A 35  ? 0.1532 0.1762 0.1259 -0.0306 -0.0034 0.0333  35  VAL   A CA  
1007 C C   . VAL   A 35  ? 0.1525 0.1619 0.1254 -0.0263 -0.0007 0.0219  35  VAL   A C   
1008 O O   . VAL   A 35  ? 0.1523 0.1809 0.1448 -0.0349 0.0132  0.0251  35  VAL   A O   
1009 C CB  . VAL   A 35  ? 0.1705 0.1810 0.1373 -0.0172 0.0094  0.0115  35  VAL   A CB  
1010 C CG1 . VAL   A 35  ? 0.1835 0.1884 0.1403 -0.0125 0.0003  0.0103  35  VAL   A CG1 
1011 C CG2 . VAL   A 35  ? 0.1785 0.1811 0.1636 -0.0127 0.0148  0.0012  35  VAL   A CG2 
1021 N N   . VAL   A 36  ? 0.1392 0.1541 0.1217 -0.0183 0.0022  0.0232  36  VAL   A N   
1022 C CA  . VAL   A 36  ? 0.1315 0.1514 0.1329 -0.0112 0.0042  0.0053  36  VAL   A CA  
1023 C C   . VAL   A 36  ? 0.1403 0.1405 0.1445 -0.0081 0.0107  0.0207  36  VAL   A C   
1024 O O   . VAL   A 36  ? 0.1450 0.1393 0.1613 -0.0089 0.0152  0.0227  36  VAL   A O   
1025 C CB  . VAL   A 36  ? 0.1303 0.1498 0.1393 -0.0096 -0.0023 0.0221  36  VAL   A CB  
1026 C CG1 . VAL   A 36  ? 0.1413 0.1495 0.1388 -0.0164 0.0054  0.0028  36  VAL   A CG1 
1027 C CG2 . VAL   A 36  ? 0.1455 0.1530 0.1565 -0.0111 0.0027  0.0413  36  VAL   A CG2 
1037 N N   . ASN   A 37  ? 0.1331 0.1413 0.1177 -0.0069 0.0083  0.0209  37  ASN   A N   
1038 C CA  . ASN   A 37  ? 0.1314 0.1411 0.1176 -0.0069 0.0043  0.0270  37  ASN   A CA  
1039 C C   . ASN   A 37  ? 0.1307 0.1346 0.1273 -0.0091 0.0072  0.0367  37  ASN   A C   
1040 O O   . ASN   A 37  ? 0.1399 0.1430 0.1280 0.0054  0.0146  0.0150  37  ASN   A O   
1041 C CB  . ASN   A 37  ? 0.1407 0.1346 0.1283 0.0054  0.0059  0.0209  37  ASN   A CB  
1042 C CG  . ASN   A 37  ? 0.1429 0.1271 0.1427 0.0065  0.0121  0.0103  37  ASN   A CG  
1043 O OD1 . ASN   A 37  ? 0.1383 0.1380 0.1618 0.0068  0.0089  0.0176  37  ASN   A OD1 
1044 N ND2 . ASN   A 37  ? 0.1474 0.1269 0.1481 -0.0023 0.0086  0.0311  37  ASN   A ND2 
1051 N N   A ALA   A 38  ? 0.1344 0.1407 0.1280 0.0018  0.0121  0.0218  38  ALA   A N   
1052 N N   B ALA   A 38  ? 0.1270 0.1428 0.1314 -0.0128 -0.0037 0.0287  38  ALA   A N   
1053 C CA  A ALA   A 38  ? 0.1411 0.1397 0.1194 -0.0063 0.0064  0.0065  38  ALA   A CA  
1054 C CA  B ALA   A 38  ? 0.1247 0.1498 0.1438 -0.0186 -0.0140 0.0228  38  ALA   A CA  
1055 C C   A ALA   A 38  ? 0.1328 0.1467 0.1243 0.0075  -0.0021 0.0033  38  ALA   A C   
1056 C C   B ALA   A 38  ? 0.1160 0.1529 0.1586 -0.0199 -0.0140 0.0190  38  ALA   A C   
1057 O O   A ALA   A 38  ? 0.1350 0.1384 0.1323 0.0084  -0.0089 0.0055  38  ALA   A O   
1058 O O   B ALA   A 38  ? 0.0962 0.1504 0.1800 -0.0296 -0.0134 0.0158  38  ALA   A O   
1059 C CB  A ALA   A 38  ? 0.1418 0.1660 0.1419 -0.0193 0.0031  -0.0040 38  ALA   A CB  
1060 C CB  B ALA   A 38  ? 0.1242 0.1546 0.1540 -0.0232 -0.0268 0.0138  38  ALA   A CB  
1071 N N   A ALA   A 39  ? 0.1299 0.1359 0.1303 0.0096  0.0055  0.0156  39  ALA   A N   
1072 N N   B ALA   A 39  ? 0.1301 0.1519 0.1584 -0.0163 -0.0036 0.0245  39  ALA   A N   
1073 C CA  A ALA   A 39  ? 0.1289 0.1353 0.1270 0.0096  0.0060  0.0175  39  ALA   A CA  
1074 C CA  B ALA   A 39  ? 0.1423 0.1582 0.1535 -0.0143 -0.0060 0.0245  39  ALA   A CA  
1075 C C   A ALA   A 39  ? 0.1250 0.1362 0.1277 0.0010  -0.0021 0.0138  39  ALA   A C   
1076 C C   B ALA   A 39  ? 0.1439 0.1520 0.1462 -0.0136 0.0015  0.0205  39  ALA   A C   
1077 O O   A ALA   A 39  ? 0.1342 0.1406 0.1354 -0.0076 0.0026  0.0064  39  ALA   A O   
1078 O O   B ALA   A 39  ? 0.1460 0.1524 0.1460 -0.0169 0.0036  0.0195  39  ALA   A O   
1079 C CB  A ALA   A 39  ? 0.1350 0.1238 0.1417 0.0072  -0.0104 0.0024  39  ALA   A CB  
1080 C CB  B ALA   A 39  ? 0.1543 0.1667 0.1594 -0.0106 -0.0105 0.0171  39  ALA   A CB  
1091 N N   A ASN   A 40  ? 0.1432 0.1392 0.1362 -0.0094 0.0286  0.0084  40  ASN   A N   
1092 N N   B ASN   A 40  ? 0.1483 0.1484 0.1451 -0.0110 0.0117  0.0169  40  ASN   A N   
1093 C CA  A ASN   A 40  ? 0.1489 0.1495 0.1359 0.0006  0.0189  0.0111  40  ASN   A CA  
1094 C CA  B ASN   A 40  ? 0.1528 0.1475 0.1413 -0.0048 0.0118  0.0124  40  ASN   A CA  
1095 C C   A ASN   A 40  ? 0.1454 0.1378 0.1281 -0.0033 0.0252  0.0102  40  ASN   A C   
1096 C C   B ASN   A 40  ? 0.1525 0.1421 0.1347 -0.0034 0.0187  0.0123  40  ASN   A C   
1097 O O   A ASN   A 40  ? 0.1388 0.1392 0.1451 -0.0055 0.0252  0.0245  40  ASN   A O   
1098 O O   B ASN   A 40  ? 0.1499 0.1427 0.1326 -0.0033 0.0204  0.0161  40  ASN   A O   
1099 C CB  A ASN   A 40  ? 0.1573 0.1532 0.1477 0.0030  -0.0044 0.0094  40  ASN   A CB  
1100 C CB  B ASN   A 40  ? 0.1567 0.1467 0.1448 -0.0038 0.0028  0.0053  40  ASN   A CB  
1101 C CG  A ASN   A 40  ? 0.1656 0.1472 0.1818 -0.0061 0.0021  0.0202  40  ASN   A CG  
1102 C CG  B ASN   A 40  ? 0.1621 0.1417 0.1585 -0.0053 0.0016  -0.0038 40  ASN   A CG  
1103 O OD1 A ASN   A 40  ? 0.1808 0.1366 0.1887 -0.0088 0.0092  0.0164  40  ASN   A OD1 
1104 O OD1 B ASN   A 40  ? 0.1675 0.1400 0.1561 -0.0024 0.0008  -0.0156 40  ASN   A OD1 
1105 N ND2 A ASN   A 40  ? 0.1682 0.1537 0.2073 0.0007  -0.0005 0.0068  40  ASN   A ND2 
1106 N ND2 B ASN   A 40  ? 0.1649 0.1385 0.1697 -0.0084 0.0018  -0.0036 40  ASN   A ND2 
1119 N N   . VAL   A 41  ? 0.1557 0.1417 0.1437 -0.0037 0.0244  0.0114  41  VAL   A N   
1120 C CA  . VAL   A 41  ? 0.1633 0.1425 0.1410 0.0021  0.0388  0.0172  41  VAL   A CA  
1121 C C   . VAL   A 41  ? 0.1642 0.1450 0.1407 0.0128  0.0240  0.0196  41  VAL   A C   
1122 O O   . VAL   A 41  ? 0.1702 0.1283 0.1737 0.0092  0.0238  0.0086  41  VAL   A O   
1123 C CB  . VAL   A 41  ? 0.1747 0.1545 0.1560 -0.0085 0.0414  0.0103  41  VAL   A CB  
1124 C CG1 . VAL   A 41  ? 0.1812 0.1632 0.1860 -0.0122 0.0417  -0.0026 41  VAL   A CG1 
1125 C CG2 . VAL   A 41  ? 0.2097 0.1688 0.1439 -0.0157 0.0458  0.0144  41  VAL   A CG2 
1136 N N   . TYR   A 42  ? 0.1476 0.1407 0.1556 0.0046  0.0303  0.0235  42  TYR   A N   
1137 C CA  . TYR   A 42  ? 0.1521 0.1397 0.1563 -0.0060 0.0265  0.0288  42  TYR   A CA  
1138 C C   . TYR   A 42  ? 0.1407 0.1336 0.1469 -0.0059 0.0221  0.0336  42  TYR   A C   
1139 O O   . TYR   A 42  ? 0.1378 0.1405 0.1797 -0.0234 0.0197  0.0089  42  TYR   A O   
1140 C CB  . TYR   A 42  ? 0.1672 0.1472 0.1551 -0.0052 0.0279  0.0361  42  TYR   A CB  
1141 C CG  . TYR   A 42  ? 0.1877 0.1536 0.1462 0.0001  0.0192  0.0342  42  TYR   A CG  
1142 C CD1 . TYR   A 42  ? 0.1985 0.1596 0.1595 -0.0218 0.0270  0.0271  42  TYR   A CD1 
1143 C CD2 . TYR   A 42  ? 0.2100 0.1731 0.1717 -0.0004 0.0202  0.0176  42  TYR   A CD2 
1144 C CE1 . TYR   A 42  ? 0.2141 0.1722 0.1675 -0.0172 0.0390  0.0149  42  TYR   A CE1 
1145 C CE2 . TYR   A 42  ? 0.2230 0.1833 0.1984 -0.0120 0.0308  0.0178  42  TYR   A CE2 
1146 C CZ  . TYR   A 42  ? 0.2348 0.1869 0.1734 -0.0197 0.0433  0.0083  42  TYR   A CZ  
1147 O OH  . TYR   A 42  ? 0.2503 0.2041 0.2032 -0.0322 0.0415  -0.0043 42  TYR   A OH  
1157 N N   . LEU   A 43  ? 0.1433 0.1329 0.1342 -0.0071 0.0150  0.0131  43  LEU   A N   
1158 C CA  . LEU   A 43  ? 0.1363 0.1293 0.1339 -0.0073 0.0053  0.0150  43  LEU   A CA  
1159 C C   . LEU   A 43  ? 0.1343 0.1279 0.1512 -0.0004 0.0059  0.0116  43  LEU   A C   
1160 O O   . LEU   A 43  ? 0.1491 0.1429 0.1771 0.0002  -0.0037 0.0039  43  LEU   A O   
1161 C CB  . LEU   A 43  ? 0.1459 0.1325 0.1615 0.0001  0.0082  0.0157  43  LEU   A CB  
1162 C CG  . LEU   A 43  ? 0.1539 0.1325 0.1670 -0.0002 -0.0002 0.0212  43  LEU   A CG  
1163 C CD1 . LEU   A 43  ? 0.1609 0.1458 0.1826 -0.0060 -0.0099 0.0260  43  LEU   A CD1 
1164 C CD2 . LEU   A 43  ? 0.1753 0.1290 0.1696 0.0006  0.0100  0.0297  43  LEU   A CD2 
1176 N N   A LYS   A 44  ? 0.1388 0.1286 0.1565 0.0033  0.0107  0.0137  44  LYS   A N   
1177 N N   B LYS   A 44  ? 0.1516 0.1475 0.1659 -0.0021 0.0032  0.0103  44  LYS   A N   
1178 C CA  A LYS   A 44  ? 0.1568 0.1308 0.1413 -0.0030 0.0174  0.0183  44  LYS   A CA  
1179 C CA  B LYS   A 44  ? 0.1712 0.1681 0.1792 -0.0050 0.0002  0.0090  44  LYS   A CA  
1180 C C   A LYS   A 44  ? 0.1394 0.1265 0.1114 0.0023  0.0054  0.0122  44  LYS   A C   
1181 C C   B LYS   A 44  ? 0.1653 0.1701 0.1583 -0.0004 -0.0042 0.0076  44  LYS   A C   
1182 O O   A LYS   A 44  ? 0.1557 0.1459 0.1490 0.0032  0.0020  -0.0018 44  LYS   A O   
1183 O O   B LYS   A 44  ? 0.1707 0.1750 0.1600 -0.0027 -0.0037 0.0052  44  LYS   A O   
1184 C CB  A LYS   A 44  ? 0.1827 0.1612 0.1778 -0.0022 0.0219  0.0212  44  LYS   A CB  
1185 C CB  B LYS   A 44  ? 0.1935 0.1908 0.2197 -0.0090 -0.0008 0.0083  44  LYS   A CB  
1186 C CG  A LYS   A 44  ? 0.2167 0.1988 0.2462 -0.0081 0.0454  0.0322  44  LYS   A CG  
1187 C CG  B LYS   A 44  ? 0.2159 0.2122 0.2652 -0.0124 0.0026  0.0097  44  LYS   A CG  
1188 C CD  A LYS   A 44  ? 0.2618 0.2587 0.3444 -0.0124 0.0447  0.0334  44  LYS   A CD  
1189 C CD  B LYS   A 44  ? 0.2395 0.2362 0.3151 -0.0174 0.0009  0.0114  44  LYS   A CD  
1190 C CE  A LYS   A 44  ? 0.2862 0.2970 0.4143 -0.0180 0.0416  0.0346  44  LYS   A CE  
1191 C CE  B LYS   A 44  ? 0.2544 0.2544 0.3502 -0.0226 -0.0023 0.0140  44  LYS   A CE  
1192 N NZ  A LYS   A 44  ? 0.2966 0.3222 0.4422 -0.0238 0.0374  0.0359  44  LYS   A NZ  
1193 N NZ  B LYS   A 44  ? 0.2628 0.2666 0.3675 -0.0278 -0.0058 0.0170  44  LYS   A NZ  
1220 N N   A HIS   A 45  ? 0.1326 0.1298 0.1266 -0.0037 0.0005  0.0201  45  HIS   A N   
1221 N N   B HIS   A 45  ? 0.1568 0.1696 0.1517 0.0048  -0.0094 0.0096  45  HIS   A N   
1222 C CA  A HIS   A 45  ? 0.1299 0.1359 0.1358 -0.0020 0.0062  0.0114  45  HIS   A CA  
1223 C CA  B HIS   A 45  ? 0.1474 0.1691 0.1470 0.0143  -0.0138 0.0048  45  HIS   A CA  
1224 C C   A HIS   A 45  ? 0.1335 0.1451 0.1563 0.0042  0.0116  0.0195  45  HIS   A C   
1225 C C   B HIS   A 45  ? 0.1453 0.1695 0.1501 0.0206  -0.0098 0.0011  45  HIS   A C   
1226 O O   A HIS   A 45  ? 0.1460 0.1542 0.1886 0.0143  0.0108  0.0114  45  HIS   A O   
1227 O O   B HIS   A 45  ? 0.1420 0.1683 0.1504 0.0284  -0.0033 -0.0035 45  HIS   A O   
1228 C CB  A HIS   A 45  ? 0.1352 0.1333 0.1285 -0.0085 0.0057  0.0080  45  HIS   A CB  
1229 C CB  B HIS   A 45  ? 0.1442 0.1692 0.1397 0.0202  -0.0194 0.0056  45  HIS   A CB  
1230 C CG  A HIS   A 45  ? 0.1354 0.1274 0.1322 -0.0129 0.0152  0.0131  45  HIS   A CG  
1231 C CG  B HIS   A 45  ? 0.1305 0.1651 0.1257 0.0222  -0.0211 0.0093  45  HIS   A CG  
1232 N ND1 A HIS   A 45  ? 0.1342 0.1340 0.1613 -0.0117 0.0185  0.0152  45  HIS   A ND1 
1233 N ND1 B HIS   A 45  ? 0.1250 0.1659 0.1234 0.0232  -0.0345 0.0131  45  HIS   A ND1 
1234 C CD2 A HIS   A 45  ? 0.1332 0.1320 0.1445 -0.0183 0.0067  0.0205  45  HIS   A CD2 
1235 C CD2 B HIS   A 45  ? 0.1276 0.1644 0.1225 0.0191  -0.0202 0.0098  45  HIS   A CD2 
1236 C CE1 A HIS   A 45  ? 0.1284 0.1378 0.1560 -0.0112 0.0049  0.0229  45  HIS   A CE1 
1237 C CE1 B HIS   A 45  ? 0.1203 0.1615 0.1107 0.0234  -0.0368 0.0094  45  HIS   A CE1 
1238 N NE2 A HIS   A 45  ? 0.1319 0.1400 0.1483 -0.0038 0.0143  0.0278  45  HIS   A NE2 
1239 N NE2 B HIS   A 45  ? 0.1214 0.1645 0.1148 0.0215  -0.0278 0.0077  45  HIS   A NE2 
1254 N N   A GLY   A 46  ? 0.1577 0.1576 0.1832 0.0145  -0.0158 0.0235  46  GLY   A N   
1255 N N   B GLY   A 46  ? 0.1535 0.1727 0.1598 0.0204  -0.0160 0.0037  46  GLY   A N   
1256 C CA  A GLY   A 46  ? 0.1633 0.1767 0.1895 0.0252  -0.0211 0.0340  46  GLY   A CA  
1257 C CA  B GLY   A 46  ? 0.1535 0.1769 0.1582 0.0196  -0.0078 0.0020  46  GLY   A CA  
1258 C C   A GLY   A 46  ? 0.1588 0.1820 0.1943 0.0338  -0.0203 0.0384  46  GLY   A C   
1259 C C   B GLY   A 46  ? 0.1523 0.1766 0.1523 0.0203  0.0048  -0.0094 46  GLY   A C   
1260 O O   A GLY   A 46  ? 0.1737 0.1900 0.2154 0.0352  -0.0426 0.0163  46  GLY   A O   
1261 O O   B GLY   A 46  ? 0.1541 0.1851 0.1579 0.0233  0.0053  -0.0220 46  GLY   A O   
1268 N N   A GLY   A 47  ? 0.1664 0.1793 0.1778 0.0340  -0.0210 0.0298  47  GLY   A N   
1269 N N   B GLY   A 47  ? 0.1591 0.1685 0.1427 0.0176  0.0082  -0.0097 47  GLY   A N   
1270 C CA  A GLY   A 47  ? 0.1772 0.1834 0.1670 0.0301  -0.0274 0.0059  47  GLY   A CA  
1271 C CA  B GLY   A 47  ? 0.1617 0.1656 0.1462 0.0144  0.0033  -0.0060 47  GLY   A CA  
1272 C C   A GLY   A 47  ? 0.1731 0.1660 0.1673 0.0295  -0.0410 -0.0028 47  GLY   A C   
1273 C C   B GLY   A 47  ? 0.1617 0.1575 0.1320 0.0141  0.0089  -0.0083 47  GLY   A C   
1274 O O   A GLY   A 47  ? 0.1714 0.1509 0.1959 0.0347  -0.0449 0.0063  47  GLY   A O   
1275 O O   B GLY   A 47  ? 0.1614 0.1527 0.1201 0.0142  0.0087  0.0042  47  GLY   A O   
1282 N N   A GLY   A 48  ? 0.1669 0.1704 0.1701 0.0260  -0.0454 -0.0120 48  GLY   A N   
1283 N N   B GLY   A 48  ? 0.1595 0.1534 0.1363 0.0122  0.0095  -0.0197 48  GLY   A N   
1284 C CA  A GLY   A 48  ? 0.1544 0.1632 0.1892 0.0110  -0.0359 -0.0145 48  GLY   A CA  
1285 C CA  B GLY   A 48  ? 0.1527 0.1479 0.1304 0.0146  0.0132  -0.0246 48  GLY   A CA  
1286 C C   A GLY   A 48  ? 0.1436 0.1604 0.1705 0.0050  -0.0157 -0.0093 48  GLY   A C   
1287 C C   B GLY   A 48  ? 0.1459 0.1498 0.1290 0.0202  0.0230  -0.0143 48  GLY   A C   
1288 O O   A GLY   A 48  ? 0.1539 0.1575 0.1708 0.0096  -0.0108 -0.0032 48  GLY   A O   
1289 O O   B GLY   A 48  ? 0.1484 0.1495 0.1239 0.0247  0.0320  -0.0135 48  GLY   A O   
1296 N N   A VAL   A 49  ? 0.1322 0.1502 0.1819 -0.0029 -0.0149 -0.0056 49  VAL   A N   
1297 N N   B VAL   A 49  ? 0.1328 0.1471 0.1195 0.0192  0.0086  -0.0109 49  VAL   A N   
1298 C CA  A VAL   A 49  ? 0.1467 0.1323 0.1904 -0.0163 0.0008  0.0102  49  VAL   A CA  
1299 C CA  B VAL   A 49  ? 0.1247 0.1477 0.1234 0.0147  0.0039  0.0006  49  VAL   A CA  
1300 C C   A VAL   A 49  ? 0.1398 0.1265 0.1600 -0.0109 0.0054  0.0146  49  VAL   A C   
1301 C C   B VAL   A 49  ? 0.1212 0.1387 0.1175 0.0137  0.0128  -0.0106 49  VAL   A C   
1302 O O   A VAL   A 49  ? 0.1379 0.1353 0.1623 -0.0048 0.0068  0.0058  49  VAL   A O   
1303 O O   B VAL   A 49  ? 0.1234 0.1392 0.1275 0.0155  0.0205  -0.0089 49  VAL   A O   
1304 C CB  A VAL   A 49  ? 0.1590 0.1426 0.2236 -0.0169 -0.0073 0.0019  49  VAL   A CB  
1305 C CB  B VAL   A 49  ? 0.1221 0.1555 0.1316 0.0226  -0.0048 0.0120  49  VAL   A CB  
1306 C CG1 A VAL   A 49  ? 0.1539 0.1385 0.2225 -0.0090 0.0034  0.0117  49  VAL   A CG1 
1307 C CG1 B VAL   A 49  ? 0.1189 0.1529 0.1316 0.0354  -0.0020 0.0199  49  VAL   A CG1 
1308 C CG2 A VAL   A 49  ? 0.1771 0.1630 0.2874 -0.0414 -0.0170 0.0143  49  VAL   A CG2 
1309 C CG2 B VAL   A 49  ? 0.1283 0.1602 0.1409 0.0209  -0.0188 0.0169  49  VAL   A CG2 
1328 N N   A ALA   A 50  ? 0.1354 0.1250 0.1453 -0.0118 -0.0156 0.0174  50  ALA   A N   
1329 N N   B ALA   A 50  ? 0.1237 0.1329 0.1122 0.0188  0.0107  -0.0178 50  ALA   A N   
1330 C CA  A ALA   A 50  ? 0.1368 0.1346 0.1361 -0.0185 -0.0028 0.0252  50  ALA   A CA  
1331 C CA  B ALA   A 50  ? 0.1287 0.1325 0.1091 0.0143  0.0058  -0.0266 50  ALA   A CA  
1332 C C   A ALA   A 50  ? 0.1321 0.1334 0.1292 -0.0178 -0.0009 0.0097  50  ALA   A C   
1333 C C   B ALA   A 50  ? 0.1329 0.1320 0.1001 0.0157  -0.0031 -0.0279 50  ALA   A C   
1334 O O   A ALA   A 50  ? 0.1312 0.1365 0.1616 -0.0126 -0.0016 0.0070  50  ALA   A O   
1335 O O   B ALA   A 50  ? 0.1352 0.1334 0.0927 0.0227  -0.0100 -0.0301 50  ALA   A O   
1336 C CB  A ALA   A 50  ? 0.1390 0.1427 0.1386 -0.0080 0.0041  0.0190  50  ALA   A CB  
1337 C CB  B ALA   A 50  ? 0.1320 0.1346 0.1051 0.0115  0.0137  -0.0381 50  ALA   A CB  
1348 N N   A GLY   A 51  ? 0.1390 0.1343 0.1459 0.0051  -0.0081 0.0142  51  GLY   A N   
1349 N N   B GLY   A 51  ? 0.1350 0.1368 0.1204 0.0157  -0.0037 -0.0255 51  GLY   A N   
1350 C CA  A GLY   A 51  ? 0.1544 0.1268 0.1468 0.0089  -0.0144 0.0115  51  GLY   A CA  
1351 C CA  B GLY   A 51  ? 0.1392 0.1376 0.1312 0.0068  -0.0048 -0.0214 51  GLY   A CA  
1352 C C   A GLY   A 51  ? 0.1310 0.1385 0.1534 0.0066  -0.0043 -0.0194 51  GLY   A C   
1353 C C   B GLY   A 51  ? 0.1316 0.1442 0.1416 0.0010  -0.0025 -0.0156 51  GLY   A C   
1354 O O   A GLY   A 51  ? 0.1387 0.1519 0.1690 0.0076  -0.0089 -0.0200 51  GLY   A O   
1355 O O   B GLY   A 51  ? 0.1326 0.1495 0.1364 -0.0006 -0.0048 -0.0105 51  GLY   A O   
1362 N N   . ALA   A 52  ? 0.1321 0.1498 0.1574 -0.0012 0.0017  -0.0113 52  ALA   A N   
1363 C CA  . ALA   A 52  ? 0.1365 0.1610 0.1661 -0.0037 0.0026  -0.0144 52  ALA   A CA  
1364 C C   . ALA   A 52  ? 0.1340 0.1541 0.1428 -0.0103 0.0122  -0.0057 52  ALA   A C   
1365 O O   . ALA   A 52  ? 0.1452 0.1661 0.1661 -0.0040 0.0046  -0.0126 52  ALA   A O   
1366 C CB  . ALA   A 52  ? 0.1424 0.1856 0.1786 -0.0095 -0.0064 0.0023  52  ALA   A CB  
1373 N N   A LEU   A 53  ? 0.1306 0.1460 0.1397 0.0005  0.0045  0.0011  53  LEU   A N   
1374 N N   B LEU   A 53  ? 0.1333 0.1523 0.1334 -0.0121 0.0069  -0.0021 53  LEU   A N   
1375 C CA  A LEU   A 53  ? 0.1457 0.1638 0.1372 -0.0026 0.0071  0.0099  53  LEU   A CA  
1376 C CA  B LEU   A 53  ? 0.1376 0.1561 0.1288 -0.0150 0.0061  0.0004  53  LEU   A CA  
1377 C C   A LEU   A 53  ? 0.1456 0.1653 0.1004 0.0062  0.0059  0.0100  53  LEU   A C   
1378 C C   B LEU   A 53  ? 0.1387 0.1546 0.1206 -0.0109 0.0034  0.0044  53  LEU   A C   
1379 O O   A LEU   A 53  ? 0.1589 0.1719 0.1277 -0.0057 0.0072  0.0110  53  LEU   A O   
1380 O O   B LEU   A 53  ? 0.1436 0.1546 0.1285 -0.0215 0.0079  0.0038  53  LEU   A O   
1381 C CB  A LEU   A 53  ? 0.1440 0.1679 0.1448 -0.0084 0.0056  0.0110  53  LEU   A CB  
1382 C CB  B LEU   A 53  ? 0.1352 0.1564 0.1254 -0.0192 0.0068  -0.0046 53  LEU   A CB  
1383 C CG  A LEU   A 53  ? 0.1743 0.1628 0.1584 -0.0250 0.0071  0.0181  53  LEU   A CG  
1384 C CG  B LEU   A 53  ? 0.1393 0.1535 0.1183 -0.0279 0.0064  -0.0116 53  LEU   A CG  
1385 C CD1 A LEU   A 53  ? 0.1842 0.1761 0.1585 0.0061  0.0009  0.0239  53  LEU   A CD1 
1386 C CD1 B LEU   A 53  ? 0.1446 0.1578 0.1194 -0.0199 0.0028  -0.0222 53  LEU   A CD1 
1387 C CD2 A LEU   A 53  ? 0.1991 0.1798 0.1677 -0.0381 0.0102  0.0097  53  LEU   A CD2 
1388 C CD2 B LEU   A 53  ? 0.1422 0.1576 0.1197 -0.0350 0.0154  -0.0123 53  LEU   A CD2 
1411 N N   . ASN   A 54  ? 0.1316 0.1483 0.1237 -0.0049 -0.0068 0.0060  54  ASN   A N   
1412 C CA  . ASN   A 54  ? 0.1222 0.1507 0.1324 -0.0019 0.0006  0.0056  54  ASN   A CA  
1413 C C   . ASN   A 54  ? 0.1349 0.1477 0.1322 -0.0042 0.0077  -0.0122 54  ASN   A C   
1414 O O   . ASN   A 54  ? 0.1408 0.1549 0.1515 -0.0017 -0.0012 -0.0181 54  ASN   A O   
1415 C CB  . ASN   A 54  ? 0.1274 0.1513 0.1313 -0.0068 -0.0061 0.0092  54  ASN   A CB  
1416 C CG  . ASN   A 54  ? 0.1373 0.1633 0.1362 -0.0007 -0.0135 -0.0007 54  ASN   A CG  
1417 O OD1 . ASN   A 54  ? 0.1354 0.1526 0.1462 -0.0081 -0.0020 0.0001  54  ASN   A OD1 
1418 N ND2 . ASN   A 54  ? 0.1404 0.1669 0.1667 -0.0084 -0.0116 0.0239  54  ASN   A ND2 
1426 N N   . LYS   A 55  ? 0.1404 0.1441 0.1503 -0.0035 0.0024  -0.0058 55  LYS   A N   
1427 C CA  . LYS   A 55  ? 0.1524 0.1647 0.1633 0.0120  -0.0064 -0.0152 55  LYS   A CA  
1428 C C   . LYS   A 55  ? 0.1467 0.1695 0.1567 -0.0068 0.0015  -0.0186 55  LYS   A C   
1429 O O   . LYS   A 55  ? 0.1558 0.1859 0.1704 -0.0013 -0.0016 -0.0270 55  LYS   A O   
1430 C CB  . LYS   A 55  ? 0.1564 0.1716 0.1746 0.0255  -0.0066 -0.0276 55  LYS   A CB  
1431 C CG  . LYS   A 55  ? 0.1848 0.2169 0.1916 0.0437  -0.0238 -0.0343 55  LYS   A CG  
1432 C CD  . LYS   A 55  ? 0.2003 0.2570 0.2108 0.0665  -0.0238 -0.0439 55  LYS   A CD  
1433 C CE  . LYS   A 55  ? 0.2269 0.2972 0.2451 0.0768  -0.0308 -0.0465 55  LYS   A CE  
1434 N NZ  . LYS   A 55  ? 0.2408 0.3165 0.2635 0.0904  -0.0480 -0.0345 55  LYS   A NZ  
1448 N N   . ALA   A 56  ? 0.1536 0.1754 0.1578 -0.0115 0.0008  -0.0212 56  ALA   A N   
1449 C CA  . ALA   A 56  ? 0.1686 0.1966 0.1517 -0.0168 0.0048  -0.0229 56  ALA   A CA  
1450 C C   . ALA   A 56  ? 0.1741 0.2064 0.1265 -0.0118 0.0102  -0.0205 56  ALA   A C   
1451 O O   . ALA   A 56  ? 0.1753 0.2361 0.1421 0.0023  0.0183  -0.0139 56  ALA   A O   
1452 C CB  . ALA   A 56  ? 0.1807 0.2118 0.1772 -0.0234 0.0104  -0.0103 56  ALA   A CB  
1458 N N   . THR   A 57  ? 0.1652 0.1895 0.1373 -0.0205 0.0170  -0.0235 57  THR   A N   
1459 C CA  . THR   A 57  ? 0.1571 0.1810 0.1386 -0.0243 0.0048  -0.0140 57  THR   A CA  
1460 C C   . THR   A 57  ? 0.1534 0.1866 0.1449 -0.0175 0.0032  -0.0112 57  THR   A C   
1461 O O   . THR   A 57  ? 0.1504 0.1897 0.1701 -0.0185 -0.0087 -0.0193 57  THR   A O   
1462 C CB  . THR   A 57  ? 0.1526 0.1752 0.1291 -0.0134 0.0059  -0.0113 57  THR   A CB  
1463 O OG1 . THR   A 57  ? 0.1393 0.1787 0.1384 -0.0053 0.0063  -0.0075 57  THR   A OG1 
1464 C CG2 . THR   A 57  ? 0.1630 0.1745 0.1366 -0.0089 -0.0047 0.0046  57  THR   A CG2 
1472 N N   . ASN   A 58  ? 0.1471 0.1856 0.1718 -0.0097 0.0073  -0.0241 58  ASN   A N   
1473 C CA  . ASN   A 58  ? 0.1731 0.1780 0.1746 -0.0136 0.0205  -0.0351 58  ASN   A CA  
1474 C C   . ASN   A 58  ? 0.1535 0.1626 0.1700 -0.0040 0.0077  -0.0255 58  ASN   A C   
1475 O O   . ASN   A 58  ? 0.1615 0.1671 0.1935 -0.0154 -0.0014 -0.0270 58  ASN   A O   
1476 C CB  . ASN   A 58  ? 0.2255 0.1931 0.2078 -0.0129 0.0495  -0.0394 58  ASN   A CB  
1477 C CG  . ASN   A 58  ? 0.2698 0.2160 0.2960 -0.0103 0.0488  -0.0179 58  ASN   A CG  
1478 O OD1 . ASN   A 58  ? 0.2927 0.2035 0.3506 0.0202  0.0743  -0.0164 58  ASN   A OD1 
1479 N ND2 . ASN   A 58  ? 0.2721 0.2225 0.3182 -0.0013 0.0343  -0.0149 58  ASN   A ND2 
1486 N N   . ASN   A 59  ? 0.1464 0.1495 0.1637 -0.0077 -0.0049 -0.0205 59  ASN   A N   
1487 C CA  . ASN   A 59  ? 0.1502 0.1453 0.1487 -0.0041 -0.0039 -0.0125 59  ASN   A CA  
1488 C C   . ASN   A 59  ? 0.1522 0.1505 0.1395 -0.0087 -0.0037 0.0009  59  ASN   A C   
1489 O O   . ASN   A 59  ? 0.1470 0.1531 0.1490 -0.0090 0.0010  0.0076  59  ASN   A O   
1490 C CB  . ASN   A 59  ? 0.1526 0.1411 0.1664 -0.0036 -0.0132 -0.0119 59  ASN   A CB  
1491 C CG  . ASN   A 59  ? 0.1537 0.1396 0.1716 -0.0018 -0.0223 -0.0011 59  ASN   A CG  
1492 O OD1 . ASN   A 59  ? 0.1579 0.1475 0.1635 -0.0094 -0.0164 0.0048  59  ASN   A OD1 
1493 N ND2 . ASN   A 59  ? 0.1688 0.1455 0.1787 -0.0138 -0.0160 0.0068  59  ASN   A ND2 
1500 N N   . ALA   A 60  ? 0.1447 0.1531 0.1457 -0.0062 0.0033  -0.0014 60  ALA   A N   
1501 C CA  . ALA   A 60  ? 0.1498 0.1536 0.1516 0.0054  -0.0066 0.0000  60  ALA   A CA  
1502 C C   . ALA   A 60  ? 0.1539 0.1481 0.1571 0.0023  0.0033  0.0020  60  ALA   A C   
1503 O O   . ALA   A 60  ? 0.1413 0.1492 0.1804 0.0005  -0.0011 -0.0106 60  ALA   A O   
1504 C CB  . ALA   A 60  ? 0.1526 0.1613 0.1556 -0.0028 -0.0112 -0.0217 60  ALA   A CB  
1510 N N   . MET   A 61  ? 0.1411 0.1358 0.1487 -0.0120 -0.0006 -0.0071 61  MET   A N   
1511 C CA  . MET   A 61  ? 0.1385 0.1311 0.1445 -0.0098 0.0094  0.0071  61  MET   A CA  
1512 C C   . MET   A 61  ? 0.1206 0.1362 0.1479 -0.0112 -0.0087 -0.0009 61  MET   A C   
1513 O O   . MET   A 61  ? 0.1299 0.1352 0.1726 -0.0008 0.0090  0.0092  61  MET   A O   
1514 C CB  . MET   A 61  ? 0.1432 0.1316 0.1422 -0.0139 0.0027  -0.0043 61  MET   A CB  
1515 C CG  . MET   A 61  ? 0.1300 0.1551 0.1486 -0.0046 -0.0006 0.0103  61  MET   A CG  
1516 S SD  . MET   A 61  ? 0.1507 0.1553 0.1738 -0.0109 0.0000  -0.0108 61  MET   A SD  
1517 C CE  . MET   A 61  ? 0.1741 0.1476 0.2239 -0.0156 0.0202  -0.0149 61  MET   A CE  
1527 N N   . GLN   A 62  ? 0.1305 0.1304 0.1537 -0.0027 0.0077  0.0045  62  GLN   A N   
1528 C CA  . GLN   A 62  ? 0.1285 0.1314 0.1635 -0.0071 0.0045  0.0111  62  GLN   A CA  
1529 C C   . GLN   A 62  ? 0.1379 0.1164 0.1620 -0.0016 0.0045  0.0049  62  GLN   A C   
1530 O O   . GLN   A 62  ? 0.1388 0.1409 0.1634 -0.0035 0.0082  -0.0031 62  GLN   A O   
1531 C CB  . GLN   A 62  ? 0.1357 0.1294 0.1672 -0.0015 0.0020  0.0115  62  GLN   A CB  
1532 C CG  . GLN   A 62  ? 0.1367 0.1272 0.1750 -0.0102 0.0039  0.0204  62  GLN   A CG  
1533 C CD  . GLN   A 62  ? 0.1494 0.1292 0.1582 -0.0103 0.0109  0.0075  62  GLN   A CD  
1534 O OE1 . GLN   A 62  ? 0.1501 0.1441 0.1661 -0.0080 -0.0019 0.0074  62  GLN   A OE1 
1535 N NE2 . GLN   A 62  ? 0.1543 0.1354 0.1732 0.0018  0.0087  -0.0100 62  GLN   A NE2 
1544 N N   . VAL   A 63  ? 0.1333 0.1309 0.1794 -0.0069 0.0058  -0.0136 63  VAL   A N   
1545 C CA  . VAL   A 63  ? 0.1295 0.1514 0.1986 -0.0149 -0.0021 -0.0166 63  VAL   A CA  
1546 C C   . VAL   A 63  ? 0.1305 0.1546 0.1749 -0.0151 0.0002  -0.0147 63  VAL   A C   
1547 O O   . VAL   A 63  ? 0.1328 0.1536 0.1912 -0.0182 -0.0020 -0.0046 63  VAL   A O   
1548 C CB  . VAL   A 63  ? 0.1470 0.1681 0.2376 -0.0183 -0.0070 -0.0318 63  VAL   A CB  
1549 C CG1 . VAL   A 63  ? 0.1608 0.1897 0.2867 -0.0158 -0.0157 -0.0605 63  VAL   A CG1 
1550 C CG2 . VAL   A 63  ? 0.1522 0.1616 0.2401 -0.0115 0.0035  -0.0257 63  VAL   A CG2 
1560 N N   . GLU   A 64  ? 0.1313 0.1612 0.1661 -0.0075 -0.0019 -0.0021 64  GLU   A N   
1561 C CA  . GLU   A 64  ? 0.1330 0.1563 0.1633 -0.0082 -0.0082 0.0108  64  GLU   A CA  
1562 C C   . GLU   A 64  ? 0.1432 0.1293 0.1610 -0.0053 -0.0084 0.0154  64  GLU   A C   
1563 O O   . GLU   A 64  ? 0.1442 0.1467 0.1734 -0.0004 0.0009  -0.0007 64  GLU   A O   
1564 C CB  . GLU   A 64  ? 0.1366 0.1677 0.1678 -0.0099 -0.0002 -0.0035 64  GLU   A CB  
1565 C CG  . GLU   A 64  ? 0.1460 0.1644 0.1901 -0.0113 -0.0081 0.0035  64  GLU   A CG  
1566 C CD  . GLU   A 64  ? 0.1623 0.1849 0.1907 -0.0150 -0.0071 0.0080  64  GLU   A CD  
1567 O OE1 . GLU   A 64  ? 0.1680 0.1870 0.2077 -0.0250 0.0070  0.0052  64  GLU   A OE1 
1568 O OE2 . GLU   A 64  ? 0.1749 0.1811 0.1806 -0.0214 -0.0108 0.0177  64  GLU   A OE2 
1575 N N   . SER   A 65  ? 0.1389 0.1384 0.1497 -0.0038 -0.0033 0.0131  65  SER   A N   
1576 C CA  . SER   A 65  ? 0.1378 0.1327 0.1556 0.0003  -0.0064 0.0038  65  SER   A CA  
1577 C C   . SER   A 65  ? 0.1357 0.1374 0.1560 -0.0041 -0.0023 0.0049  65  SER   A C   
1578 O O   . SER   A 65  ? 0.1413 0.1386 0.2017 0.0004  0.0204  -0.0027 65  SER   A O   
1579 C CB  . SER   A 65  ? 0.1438 0.1374 0.1597 -0.0072 0.0006  0.0022  65  SER   A CB  
1580 O OG  . SER   A 65  ? 0.1332 0.1497 0.1629 -0.0096 0.0056  0.0159  65  SER   A OG  
1586 N N   . ASP   A 66  ? 0.1350 0.1410 0.1507 -0.0060 0.0117  0.0056  66  ASP   A N   
1587 C CA  . ASP   A 66  ? 0.1434 0.1522 0.1727 -0.0016 0.0160  0.0161  66  ASP   A CA  
1588 C C   . ASP   A 66  ? 0.1360 0.1551 0.1706 -0.0043 0.0136  0.0102  66  ASP   A C   
1589 O O   . ASP   A 66  ? 0.1497 0.1667 0.1849 -0.0066 0.0302  0.0275  66  ASP   A O   
1590 C CB  . ASP   A 66  ? 0.1615 0.1545 0.2190 0.0133  0.0207  0.0361  66  ASP   A CB  
1591 C CG  . ASP   A 66  ? 0.1824 0.1689 0.2496 0.0027  0.0110  0.0514  66  ASP   A CG  
1592 O OD1 . ASP   A 66  ? 0.1772 0.1954 0.2282 -0.0075 0.0005  0.0494  66  ASP   A OD1 
1593 O OD2 . ASP   A 66  ? 0.1992 0.1963 0.3129 0.0190  -0.0066 0.0239  66  ASP   A OD2 
1598 N N   . ASP   A 67  ? 0.1291 0.1512 0.1879 0.0022  0.0117  0.0146  67  ASP   A N   
1599 C CA  . ASP   A 67  ? 0.1376 0.1696 0.1889 -0.0016 0.0097  0.0274  67  ASP   A CA  
1600 C C   . ASP   A 67  ? 0.1442 0.1663 0.1801 0.0025  0.0217  0.0254  67  ASP   A C   
1601 O O   . ASP   A 67  ? 0.1454 0.1652 0.2211 0.0060  0.0275  0.0303  67  ASP   A O   
1602 C CB  . ASP   A 67  ? 0.1496 0.1660 0.2226 -0.0088 -0.0112 0.0395  67  ASP   A CB  
1603 C CG  . ASP   A 67  ? 0.1563 0.1850 0.2694 -0.0172 -0.0244 0.0455  67  ASP   A CG  
1604 O OD1 . ASP   A 67  ? 0.1559 0.2013 0.3581 -0.0194 -0.0362 0.0535  67  ASP   A OD1 
1605 O OD2 . ASP   A 67  ? 0.1610 0.1946 0.2588 0.0059  -0.0177 0.0370  67  ASP   A OD2 
1610 N N   . TYR   A 68  ? 0.1413 0.1517 0.2019 0.0105  0.0187  0.0388  68  TYR   A N   
1611 C CA  . TYR   A 68  ? 0.1565 0.1528 0.1928 0.0058  0.0192  0.0294  68  TYR   A CA  
1612 C C   . TYR   A 68  ? 0.1402 0.1536 0.1923 0.0002  0.0223  0.0120  68  TYR   A C   
1613 O O   . TYR   A 68  ? 0.1542 0.1521 0.2121 0.0155  0.0321  0.0181  68  TYR   A O   
1614 C CB  . TYR   A 68  ? 0.1539 0.1487 0.2063 0.0069  0.0477  0.0345  68  TYR   A CB  
1615 C CG  . TYR   A 68  ? 0.1569 0.1671 0.2381 0.0078  0.0532  0.0352  68  TYR   A CG  
1616 C CD1 . TYR   A 68  ? 0.1730 0.1753 0.2801 -0.0170 0.0464  -0.0135 68  TYR   A CD1 
1617 C CD2 . TYR   A 68  ? 0.1851 0.1770 0.2774 0.0106  0.0604  0.0306  68  TYR   A CD2 
1618 C CE1 . TYR   A 68  ? 0.1789 0.1873 0.3203 -0.0219 0.0624  -0.0260 68  TYR   A CE1 
1619 C CE2 . TYR   A 68  ? 0.1881 0.1765 0.3137 -0.0037 0.0765  -0.0098 68  TYR   A CE2 
1620 C CZ  . TYR   A 68  ? 0.1910 0.1846 0.3460 -0.0226 0.0601  -0.0322 68  TYR   A CZ  
1621 O OH  . TYR   A 68  ? 0.2115 0.1964 0.3944 -0.0203 0.0521  -0.0682 68  TYR   A OH  
1631 N N   . ILE   A 69  ? 0.1369 0.1434 0.1838 -0.0007 0.0143  0.0157  69  ILE   A N   
1632 C CA  . ILE   A 69  ? 0.1426 0.1478 0.1753 0.0016  0.0093  0.0086  69  ILE   A CA  
1633 C C   . ILE   A 69  ? 0.1476 0.1475 0.1709 0.0079  0.0197  0.0169  69  ILE   A C   
1634 O O   . ILE   A 69  ? 0.1469 0.1553 0.1831 0.0026  0.0214  0.0098  69  ILE   A O   
1635 C CB  . ILE   A 69  ? 0.1541 0.1715 0.1871 0.0049  0.0101  -0.0022 69  ILE   A CB  
1636 C CG1 . ILE   A 69  ? 0.1586 0.1710 0.1951 0.0062  0.0255  -0.0187 69  ILE   A CG1 
1637 C CG2 . ILE   A 69  ? 0.1755 0.1953 0.2041 0.0114  0.0063  -0.0188 69  ILE   A CG2 
1638 C CD1 . ILE   A 69  ? 0.1632 0.1770 0.2145 -0.0080 0.0330  -0.0203 69  ILE   A CD1 
1650 N N   . ALA   A 70  ? 0.1562 0.1499 0.1867 -0.0052 0.0174  0.0263  70  ALA   A N   
1651 C CA  . ALA   A 70  ? 0.1610 0.1653 0.2112 -0.0162 0.0302  0.0256  70  ALA   A CA  
1652 C C   . ALA   A 70  ? 0.1641 0.1806 0.2161 -0.0101 0.0393  0.0259  70  ALA   A C   
1653 O O   . ALA   A 70  ? 0.1791 0.2130 0.2377 0.0101  0.0542  0.0522  70  ALA   A O   
1654 C CB  . ALA   A 70  ? 0.1635 0.1608 0.2339 -0.0165 0.0248  0.0259  70  ALA   A CB  
1660 N N   . THR   A 71  ? 0.1514 0.1706 0.2092 0.0018  0.0302  0.0421  71  THR   A N   
1661 C CA  . THR   A 71  ? 0.1703 0.1943 0.2385 0.0126  0.0276  0.0365  71  THR   A CA  
1662 C C   . THR   A 71  ? 0.1570 0.1864 0.2681 0.0222  0.0439  0.0303  71  THR   A C   
1663 O O   . THR   A 71  ? 0.1669 0.2055 0.3234 0.0201  0.0515  0.0034  71  THR   A O   
1664 C CB  . THR   A 71  ? 0.2050 0.2202 0.2707 0.0213  -0.0113 0.0494  71  THR   A CB  
1665 O OG1 . THR   A 71  ? 0.2299 0.2466 0.2784 0.0166  -0.0401 0.0387  71  THR   A OG1 
1666 C CG2 . THR   A 71  ? 0.2211 0.2386 0.3099 0.0306  -0.0341 0.0703  71  THR   A CG2 
1674 N N   . ASN   A 72  ? 0.1596 0.1732 0.2387 0.0142  0.0331  0.0346  72  ASN   A N   
1675 C CA  . ASN   A 72  ? 0.1635 0.1812 0.2318 0.0168  0.0464  0.0320  72  ASN   A CA  
1676 C C   . ASN   A 72  ? 0.1723 0.1807 0.2284 0.0071  0.0536  0.0226  72  ASN   A C   
1677 O O   . ASN   A 72  ? 0.1886 0.1768 0.2510 0.0165  0.0496  0.0076  72  ASN   A O   
1678 C CB  . ASN   A 72  ? 0.1887 0.1896 0.2356 0.0242  0.0535  0.0489  72  ASN   A CB  
1679 C CG  . ASN   A 72  ? 0.2125 0.2098 0.2355 0.0280  0.0468  0.0534  72  ASN   A CG  
1680 O OD1 . ASN   A 72  ? 0.2327 0.2401 0.2571 0.0259  0.0481  0.0476  72  ASN   A OD1 
1681 N ND2 . ASN   A 72  ? 0.2283 0.2068 0.2401 0.0659  0.0237  0.0445  72  ASN   A ND2 
1688 N N   . GLY   A 73  ? 0.1689 0.1693 0.2085 0.0053  0.0472  0.0115  73  GLY   A N   
1689 C CA  . GLY   A 73  ? 0.1741 0.1604 0.2049 -0.0054 0.0433  0.0105  73  GLY   A CA  
1690 C C   . GLY   A 73  ? 0.1742 0.1531 0.1862 0.0032  0.0485  0.0199  73  GLY   A C   
1691 O O   . GLY   A 73  ? 0.1671 0.1585 0.2068 0.0179  0.0352  0.0304  73  GLY   A O   
1695 N N   . PRO   A 74  ? 0.1835 0.1577 0.1828 -0.0073 0.0558  0.0139  74  PRO   A N   
1696 C CA  . PRO   A 74  ? 0.1795 0.1477 0.2019 -0.0045 0.0476  0.0116  74  PRO   A CA  
1697 C C   . PRO   A 74  ? 0.1727 0.1280 0.2040 -0.0020 0.0409  0.0017  74  PRO   A C   
1698 O O   . PRO   A 74  ? 0.1760 0.1447 0.2222 0.0015  0.0392  -0.0084 74  PRO   A O   
1699 C CB  . PRO   A 74  ? 0.2002 0.1741 0.2237 0.0030  0.0518  0.0223  74  PRO   A CB  
1700 C CG  . PRO   A 74  ? 0.2295 0.2253 0.2737 -0.0236 0.0383  0.0142  74  PRO   A CG  
1701 C CD  . PRO   A 74  ? 0.2058 0.1950 0.2068 -0.0206 0.0416  0.0118  74  PRO   A CD  
1709 N N   . LEU   A 75  ? 0.1776 0.1401 0.1711 -0.0020 0.0305  0.0028  75  LEU   A N   
1710 C CA  . LEU   A 75  ? 0.1727 0.1353 0.1482 -0.0034 0.0117  0.0192  75  LEU   A CA  
1711 C C   . LEU   A 75  ? 0.1804 0.1444 0.1478 0.0098  0.0085  0.0190  75  LEU   A C   
1712 O O   . LEU   A 75  ? 0.2115 0.1615 0.1613 0.0154  0.0058  0.0069  75  LEU   A O   
1713 C CB  . LEU   A 75  ? 0.1739 0.1357 0.1640 -0.0078 0.0124  0.0230  75  LEU   A CB  
1714 C CG  . LEU   A 75  ? 0.1915 0.1734 0.1614 -0.0380 0.0197  0.0193  75  LEU   A CG  
1715 C CD1 . LEU   A 75  ? 0.2046 0.2289 0.1714 -0.0428 0.0109  -0.0088 75  LEU   A CD1 
1716 C CD2 . LEU   A 75  ? 0.2311 0.2085 0.2225 -0.0106 0.0142  0.0257  75  LEU   A CD2 
1728 N N   . LYS   A 76  ? 0.1798 0.1447 0.1733 -0.0027 -0.0022 0.0003  76  LYS   A N   
1729 C CA  . LYS   A 76  ? 0.1714 0.1666 0.1795 -0.0041 0.0062  -0.0117 76  LYS   A CA  
1730 C C   . LYS   A 76  ? 0.1660 0.1537 0.1494 0.0094  0.0051  0.0104  76  LYS   A C   
1731 O O   . LYS   A 76  ? 0.1748 0.1463 0.1547 0.0015  0.0154  0.0193  76  LYS   A O   
1732 C CB  . LYS   A 76  ? 0.1707 0.1924 0.2240 0.0088  0.0127  -0.0382 76  LYS   A CB  
1733 C CG  . LYS   A 76  ? 0.1847 0.1932 0.2792 0.0115  0.0042  -0.0314 76  LYS   A CG  
1734 C CD  . LYS   A 76  ? 0.1957 0.1942 0.3298 0.0191  -0.0129 -0.0255 76  LYS   A CD  
1735 C CE  . LYS   A 76  ? 0.2069 0.2068 0.3813 0.0066  -0.0000 -0.0266 76  LYS   A CE  
1736 N NZ  . LYS   A 76  ? 0.2082 0.1959 0.4187 -0.0103 0.0001  -0.0339 76  LYS   A NZ  
1750 N N   . VAL   A 77  ? 0.1828 0.1545 0.1511 0.0060  0.0250  0.0146  77  VAL   A N   
1751 C CA  . VAL   A 77  ? 0.1749 0.1556 0.1498 0.0080  0.0136  0.0123  77  VAL   A CA  
1752 C C   . VAL   A 77  ? 0.1670 0.1531 0.1503 0.0056  0.0124  0.0054  77  VAL   A C   
1753 O O   . VAL   A 77  ? 0.1782 0.1678 0.1505 0.0145  0.0362  -0.0088 77  VAL   A O   
1754 C CB  . VAL   A 77  ? 0.1971 0.1739 0.1655 -0.0024 0.0229  0.0251  77  VAL   A CB  
1755 C CG1 . VAL   A 77  ? 0.1996 0.1855 0.1883 -0.0027 0.0093  0.0103  77  VAL   A CG1 
1756 C CG2 . VAL   A 77  ? 0.2260 0.1783 0.1856 -0.0051 0.0015  0.0261  77  VAL   A CG2 
1766 N N   . GLY   A 78  ? 0.1613 0.1485 0.1394 0.0047  0.0217  0.0120  78  GLY   A N   
1767 C CA  . GLY   A 78  ? 0.1682 0.1554 0.1510 0.0063  0.0270  0.0182  78  GLY   A CA  
1768 C C   . GLY   A 78  ? 0.1575 0.1463 0.1617 0.0076  0.0213  0.0250  78  GLY   A C   
1769 O O   . GLY   A 78  ? 0.1571 0.1537 0.1806 0.0038  0.0160  0.0247  78  GLY   A O   
1773 N N   . GLY   A 79  ? 0.1624 0.1360 0.1559 0.0001  0.0192  0.0167  79  GLY   A N   
1774 C CA  . GLY   A 79  ? 0.1596 0.1395 0.1561 0.0042  0.0165  0.0217  79  GLY   A CA  
1775 C C   . GLY   A 79  ? 0.1415 0.1345 0.1461 0.0010  0.0122  0.0160  79  GLY   A C   
1776 O O   . GLY   A 79  ? 0.1454 0.1454 0.1801 0.0178  0.0110  0.0108  79  GLY   A O   
1780 N N   . SER   A 80  ? 0.1417 0.1436 0.1798 -0.0007 0.0115  0.0063  80  SER   A N   
1781 C CA  . SER   A 80  ? 0.1404 0.1371 0.1708 -0.0007 0.0078  0.0003  80  SER   A CA  
1782 C C   . SER   A 80  ? 0.1480 0.1421 0.1618 -0.0002 0.0126  0.0135  80  SER   A C   
1783 O O   . SER   A 80  ? 0.1499 0.1690 0.1920 0.0148  0.0138  0.0001  80  SER   A O   
1784 C CB  . SER   A 80  ? 0.1512 0.1422 0.1912 0.0005  0.0162  0.0050  80  SER   A CB  
1785 O OG  . SER   A 80  ? 0.1733 0.1491 0.2303 -0.0011 0.0049  0.0310  80  SER   A OG  
1791 N N   . CYS   A 81  ? 0.1424 0.1345 0.1670 -0.0043 -0.0016 0.0180  81  CYS   A N   
1792 C CA  . CYS   A 81  ? 0.1423 0.1522 0.1590 -0.0107 -0.0078 0.0222  81  CYS   A CA  
1793 C C   . CYS   A 81  ? 0.1399 0.1556 0.1398 -0.0058 -0.0003 0.0381  81  CYS   A C   
1794 O O   . CYS   A 81  ? 0.1355 0.1738 0.1822 0.0043  0.0033  0.0425  81  CYS   A O   
1795 C CB  . CYS   A 81  ? 0.1457 0.1550 0.1711 -0.0170 0.0015  0.0258  81  CYS   A CB  
1796 S SG  . CYS   A 81  ? 0.1561 0.1468 0.1711 -0.0155 0.0016  0.0155  81  CYS   A SG  
1802 N N   . VAL   A 82  ? 0.1367 0.1585 0.1518 -0.0079 -0.0165 0.0298  82  VAL   A N   
1803 C CA  . VAL   A 82  ? 0.1535 0.1760 0.1472 -0.0057 -0.0116 0.0295  82  VAL   A CA  
1804 C C   . VAL   A 82  ? 0.1415 0.1782 0.1635 -0.0071 -0.0040 0.0340  82  VAL   A C   
1805 O O   . VAL   A 82  ? 0.1405 0.1763 0.1869 -0.0047 -0.0029 0.0118  82  VAL   A O   
1806 C CB  . VAL   A 82  ? 0.1866 0.1871 0.1734 0.0011  -0.0089 0.0446  82  VAL   A CB  
1807 C CG1 . VAL   A 82  ? 0.2072 0.1917 0.2151 0.0031  -0.0035 0.0309  82  VAL   A CG1 
1808 C CG2 . VAL   A 82  ? 0.1834 0.1849 0.2070 -0.0053 -0.0058 0.0307  82  VAL   A CG2 
1818 N N   . LEU   A 83  ? 0.1333 0.1785 0.1550 -0.0219 -0.0123 0.0167  83  LEU   A N   
1819 C CA  . LEU   A 83  ? 0.1462 0.1719 0.1358 -0.0151 -0.0080 0.0184  83  LEU   A CA  
1820 C C   . LEU   A 83  ? 0.1555 0.1650 0.1382 -0.0209 -0.0214 0.0174  83  LEU   A C   
1821 O O   . LEU   A 83  ? 0.1553 0.1627 0.1703 -0.0183 -0.0067 0.0219  83  LEU   A O   
1822 C CB  . LEU   A 83  ? 0.1557 0.1784 0.1447 -0.0168 -0.0115 0.0299  83  LEU   A CB  
1823 C CG  . LEU   A 83  ? 0.1615 0.1765 0.1640 -0.0175 -0.0000 0.0158  83  LEU   A CG  
1824 C CD1 . LEU   A 83  ? 0.1731 0.1780 0.1670 -0.0267 -0.0007 0.0222  83  LEU   A CD1 
1825 C CD2 . LEU   A 83  ? 0.1620 0.1897 0.1870 -0.0100 0.0155  0.0199  83  LEU   A CD2 
1837 N N   . SER   A 84  ? 0.1705 0.1719 0.1549 -0.0211 -0.0152 0.0216  84  SER   A N   
1838 C CA  . SER   A 84  ? 0.1795 0.1757 0.1344 -0.0194 -0.0119 0.0231  84  SER   A CA  
1839 C C   . SER   A 84  ? 0.1788 0.1796 0.1257 -0.0255 0.0058  0.0180  84  SER   A C   
1840 O O   . SER   A 84  ? 0.1813 0.1897 0.1335 -0.0128 -0.0001 0.0191  84  SER   A O   
1841 C CB  . SER   A 84  ? 0.1883 0.1982 0.1359 -0.0176 -0.0178 0.0098  84  SER   A CB  
1842 O OG  . SER   A 84  ? 0.1863 0.2205 0.1680 -0.0183 -0.0208 -0.0040 84  SER   A OG  
1848 N N   . GLY   A 85  ? 0.1926 0.1928 0.1461 -0.0238 0.0064  0.0232  85  GLY   A N   
1849 C CA  . GLY   A 85  ? 0.1937 0.2028 0.1532 -0.0228 0.0087  0.0044  85  GLY   A CA  
1850 C C   . GLY   A 85  ? 0.1926 0.2057 0.1422 -0.0224 -0.0073 0.0064  85  GLY   A C   
1851 O O   . GLY   A 85  ? 0.1990 0.2242 0.1565 -0.0275 0.0096  -0.0153 85  GLY   A O   
1855 N N   . HIS   A 86  ? 0.1930 0.2013 0.1345 -0.0237 -0.0135 0.0093  86  HIS   A N   
1856 C CA  . HIS   A 86  ? 0.2058 0.2124 0.1286 -0.0274 0.0009  0.0098  86  HIS   A CA  
1857 C C   . HIS   A 86  ? 0.2269 0.2325 0.1120 -0.0304 0.0015  0.0059  86  HIS   A C   
1858 O O   . HIS   A 86  ? 0.2374 0.2587 0.1377 -0.0297 0.0092  0.0084  86  HIS   A O   
1859 C CB  . HIS   A 86  ? 0.2087 0.2086 0.1306 -0.0141 0.0068  0.0196  86  HIS   A CB  
1860 C CG  . HIS   A 86  ? 0.1987 0.2027 0.1373 -0.0105 0.0054  0.0265  86  HIS   A CG  
1861 N ND1 . HIS   A 86  ? 0.2082 0.2020 0.1878 -0.0250 0.0019  0.0235  86  HIS   A ND1 
1862 C CD2 . HIS   A 86  ? 0.2028 0.2011 0.1409 0.0050  0.0151  0.0218  86  HIS   A CD2 
1863 C CE1 . HIS   A 86  ? 0.1967 0.2003 0.1624 -0.0181 0.0195  0.0256  86  HIS   A CE1 
1864 N NE2 . HIS   A 86  ? 0.2033 0.1984 0.1570 0.0095  0.0182  0.0283  86  HIS   A NE2 
1872 N N   . ASN   A 87  ? 0.2384 0.2426 0.1294 -0.0139 0.0168  -0.0102 87  ASN   A N   
1873 C CA  . ASN   A 87  ? 0.2594 0.2515 0.1416 -0.0182 0.0367  -0.0110 87  ASN   A CA  
1874 C C   . ASN   A 87  ? 0.2606 0.2637 0.1755 -0.0290 0.0558  0.0035  87  ASN   A C   
1875 O O   . ASN   A 87  ? 0.2927 0.2867 0.2156 -0.0428 0.0967  -0.0155 87  ASN   A O   
1876 C CB  . ASN   A 87  ? 0.2763 0.2567 0.1612 -0.0113 0.0347  -0.0095 87  ASN   A CB  
1877 C CG  . ASN   A 87  ? 0.2892 0.2690 0.1612 -0.0095 0.0518  0.0010  87  ASN   A CG  
1878 O OD1 . ASN   A 87  ? 0.2987 0.2715 0.1608 0.0048  0.0491  0.0148  87  ASN   A OD1 
1879 N ND2 . ASN   A 87  ? 0.2967 0.2919 0.1730 -0.0130 0.0506  0.0062  87  ASN   A ND2 
1886 N N   A LEU   A 88  ? 0.2367 0.2425 0.1696 -0.0318 0.0343  0.0133  88  LEU   A N   
1887 N N   B LEU   A 88  ? 0.2464 0.2566 0.1844 -0.0290 0.0424  0.0055  88  LEU   A N   
1888 C CA  A LEU   A 88  ? 0.2248 0.2374 0.1843 -0.0365 0.0237  0.0388  88  LEU   A CA  
1889 C CA  B LEU   A 88  ? 0.2347 0.2537 0.1940 -0.0295 0.0313  0.0127  88  LEU   A CA  
1890 C C   A LEU   A 88  ? 0.2175 0.2439 0.1645 -0.0374 0.0330  0.0471  88  LEU   A C   
1891 C C   B LEU   A 88  ? 0.2237 0.2534 0.1779 -0.0308 0.0269  0.0235  88  LEU   A C   
1892 O O   A LEU   A 88  ? 0.2221 0.2475 0.2064 -0.0305 0.0420  0.0500  88  LEU   A O   
1893 O O   B LEU   A 88  ? 0.2244 0.2545 0.1903 -0.0284 0.0297  0.0252  88  LEU   A O   
1894 C CB  A LEU   A 88  ? 0.2219 0.2463 0.1991 -0.0375 -0.0117 0.0495  88  LEU   A CB  
1895 C CB  B LEU   A 88  ? 0.2354 0.2556 0.2131 -0.0294 0.0212  0.0084  88  LEU   A CB  
1896 C CG  A LEU   A 88  ? 0.2314 0.2509 0.2209 -0.0417 -0.0236 0.0575  88  LEU   A CG  
1897 C CG  B LEU   A 88  ? 0.2374 0.2557 0.2271 -0.0303 0.0154  0.0035  88  LEU   A CG  
1898 C CD1 A LEU   A 88  ? 0.2424 0.2601 0.2286 -0.0381 -0.0282 0.0475  88  LEU   A CD1 
1899 C CD1 B LEU   A 88  ? 0.2384 0.2567 0.2298 -0.0301 0.0123  -0.0046 88  LEU   A CD1 
1900 C CD2 A LEU   A 88  ? 0.2493 0.2590 0.2623 -0.0321 -0.0107 0.0426  88  LEU   A CD2 
1901 C CD2 B LEU   A 88  ? 0.2413 0.2569 0.2383 -0.0278 0.0166  -0.0000 88  LEU   A CD2 
1924 N N   . ALA   A 89  ? 0.2127 0.2521 0.1545 -0.0316 0.0186  0.0277  89  ALA   A N   
1925 C CA  . ALA   A 89  ? 0.2186 0.2601 0.1267 -0.0238 0.0012  0.0364  89  ALA   A CA  
1926 C C   . ALA   A 89  ? 0.2242 0.2535 0.1357 -0.0258 -0.0048 0.0409  89  ALA   A C   
1927 O O   . ALA   A 89  ? 0.2206 0.2420 0.1874 -0.0370 -0.0014 0.0038  89  ALA   A O   
1928 C CB  . ALA   A 89  ? 0.2075 0.2555 0.1291 -0.0263 0.0008  0.0294  89  ALA   A CB  
1935 N N   . LYS   A 90  ? 0.2269 0.2649 0.1410 -0.0395 -0.0216 0.0347  90  LYS   A N   
1936 C CA  . LYS   A 90  ? 0.2392 0.2808 0.1534 -0.0226 -0.0387 0.0410  90  LYS   A CA  
1937 C C   . LYS   A 90  ? 0.2165 0.2569 0.1545 -0.0280 -0.0358 0.0237  90  LYS   A C   
1938 O O   . LYS   A 90  ? 0.2167 0.2707 0.1862 -0.0338 -0.0406 0.0153  90  LYS   A O   
1939 C CB  . LYS   A 90  ? 0.2750 0.3288 0.1799 -0.0215 -0.0445 0.0780  90  LYS   A CB  
1940 C CG  . LYS   A 90  ? 0.3422 0.3804 0.3005 -0.0232 -0.0329 0.0819  90  LYS   A CG  
1941 C CD  . LYS   A 90  ? 0.4108 0.4390 0.4283 -0.0275 -0.0073 0.0812  90  LYS   A CD  
1942 C CE  . LYS   A 90  ? 0.4770 0.4904 0.5282 -0.0323 0.0132  0.0749  90  LYS   A CE  
1943 N NZ  . LYS   A 90  ? 0.5113 0.5113 0.5928 -0.0368 0.0235  0.0731  90  LYS   A NZ  
1957 N N   . HIS   A 91  ? 0.2013 0.2250 0.1174 -0.0332 -0.0390 0.0344  91  HIS   A N   
1958 C CA  . HIS   A 91  ? 0.1932 0.2010 0.1196 -0.0202 -0.0277 0.0220  91  HIS   A CA  
1959 C C   . HIS   A 91  ? 0.1728 0.1834 0.1059 -0.0182 -0.0263 0.0351  91  HIS   A C   
1960 O O   . HIS   A 91  ? 0.1609 0.2049 0.1459 -0.0297 -0.0005 0.0282  91  HIS   A O   
1961 C CB  . HIS   A 91  ? 0.2046 0.2263 0.1800 0.0050  -0.0366 0.0267  91  HIS   A CB  
1962 C CG  . HIS   A 91  ? 0.2548 0.2749 0.2519 0.0081  -0.0714 0.0107  91  HIS   A CG  
1963 N ND1 . HIS   A 91  ? 0.2661 0.2995 0.2987 0.0104  -0.0890 -0.0158 91  HIS   A ND1 
1964 C CD2 . HIS   A 91  ? 0.2850 0.2987 0.2823 0.0182  -0.0959 0.0157  91  HIS   A CD2 
1965 C CE1 . HIS   A 91  ? 0.2839 0.3094 0.3180 0.0184  -0.0891 -0.0039 91  HIS   A CE1 
1966 N NE2 . HIS   A 91  ? 0.2980 0.3129 0.3091 0.0247  -0.1031 0.0060  91  HIS   A NE2 
1974 N N   . CYS   A 92  ? 0.1601 0.1723 0.1330 -0.0222 -0.0145 0.0377  92  CYS   A N   
1975 C CA  . CYS   A 92  ? 0.1478 0.1686 0.1292 -0.0180 -0.0033 0.0295  92  CYS   A CA  
1976 C C   . CYS   A 92  ? 0.1453 0.1618 0.1435 -0.0218 0.0068  0.0282  92  CYS   A C   
1977 O O   . CYS   A 92  ? 0.1514 0.1629 0.1637 -0.0214 0.0032  0.0221  92  CYS   A O   
1978 C CB  . CYS   A 92  ? 0.1627 0.1684 0.1411 -0.0045 0.0005  0.0166  92  CYS   A CB  
1979 S SG  . CYS   A 92  ? 0.1544 0.1607 0.1440 -0.0158 -0.0031 0.0176  92  CYS   A SG  
1985 N N   . LEU   A 93  ? 0.1467 0.1515 0.1380 -0.0131 0.0120  0.0188  93  LEU   A N   
1986 C CA  . LEU   A 93  ? 0.1176 0.1417 0.1426 -0.0170 0.0016  0.0231  93  LEU   A CA  
1987 C C   . LEU   A 93  ? 0.1377 0.1379 0.1327 -0.0057 0.0047  0.0243  93  LEU   A C   
1988 O O   . LEU   A 93  ? 0.1295 0.1463 0.1408 -0.0056 -0.0049 0.0189  93  LEU   A O   
1989 C CB  . LEU   A 93  ? 0.1387 0.1572 0.1567 -0.0075 -0.0013 0.0308  93  LEU   A CB  
1990 C CG  . LEU   A 93  ? 0.1550 0.1516 0.1631 -0.0118 -0.0017 0.0318  93  LEU   A CG  
1991 C CD1 . LEU   A 93  ? 0.1490 0.1538 0.1995 0.0010  0.0127  0.0352  93  LEU   A CD1 
1992 C CD2 . LEU   A 93  ? 0.1716 0.1475 0.1772 -0.0117 0.0015  0.0277  93  LEU   A CD2 
2004 N N   . HIS   A 94  ? 0.1274 0.1342 0.1408 -0.0048 0.0032  0.0239  94  HIS   A N   
2005 C CA  . HIS   A 94  ? 0.1270 0.1341 0.1323 -0.0058 -0.0010 0.0166  94  HIS   A CA  
2006 C C   . HIS   A 94  ? 0.1378 0.1289 0.1372 -0.0087 0.0022  0.0068  94  HIS   A C   
2007 O O   . HIS   A 94  ? 0.1381 0.1443 0.1813 -0.0002 0.0052  -0.0021 94  HIS   A O   
2008 C CB  . HIS   A 94  ? 0.1275 0.1366 0.1392 -0.0048 -0.0033 0.0183  94  HIS   A CB  
2009 C CG  . HIS   A 94  ? 0.1375 0.1340 0.1308 -0.0050 -0.0024 0.0183  94  HIS   A CG  
2010 N ND1 . HIS   A 94  ? 0.1317 0.1322 0.1358 -0.0017 0.0042  0.0219  94  HIS   A ND1 
2011 C CD2 . HIS   A 94  ? 0.1336 0.1510 0.1452 -0.0051 -0.0071 0.0125  94  HIS   A CD2 
2012 C CE1 . HIS   A 94  ? 0.1363 0.1372 0.1444 -0.0073 -0.0123 0.0138  94  HIS   A CE1 
2013 N NE2 . HIS   A 94  ? 0.1404 0.1431 0.1458 -0.0110 -0.0076 0.0012  94  HIS   A NE2 
2021 N N   . VAL   A 95  ? 0.1351 0.1349 0.1133 -0.0157 0.0001  0.0029  95  VAL   A N   
2022 C CA  . VAL   A 95  ? 0.1404 0.1399 0.1084 -0.0080 0.0070  0.0122  95  VAL   A CA  
2023 C C   . VAL   A 95  ? 0.1287 0.1341 0.1079 -0.0223 0.0040  0.0056  95  VAL   A C   
2024 O O   . VAL   A 95  ? 0.1326 0.1445 0.1403 0.0070  0.0044  0.0118  95  VAL   A O   
2025 C CB  . VAL   A 95  ? 0.1346 0.1355 0.1378 -0.0158 0.0055  0.0122  95  VAL   A CB  
2026 C CG1 . VAL   A 95  ? 0.1483 0.1480 0.1454 -0.0214 0.0057  -0.0011 95  VAL   A CG1 
2027 C CG2 . VAL   A 95  ? 0.1386 0.1284 0.1463 -0.0185 0.0070  0.0261  95  VAL   A CG2 
2037 N N   . VAL   A 96  ? 0.1413 0.1332 0.1112 -0.0038 0.0087  0.0133  96  VAL   A N   
2038 C CA  . VAL   A 96  ? 0.1448 0.1332 0.1185 -0.0041 0.0054  0.0202  96  VAL   A CA  
2039 C C   . VAL   A 96  ? 0.1438 0.1429 0.1360 0.0009  0.0142  0.0142  96  VAL   A C   
2040 O O   . VAL   A 96  ? 0.1498 0.1415 0.1630 -0.0061 0.0227  -0.0082 96  VAL   A O   
2041 C CB  . VAL   A 96  ? 0.1430 0.1375 0.1313 -0.0027 0.0167  0.0186  96  VAL   A CB  
2042 C CG1 . VAL   A 96  ? 0.1504 0.1452 0.1338 -0.0071 0.0198  0.0126  96  VAL   A CG1 
2043 C CG2 . VAL   A 96  ? 0.1416 0.1496 0.1507 -0.0154 0.0222  0.0067  96  VAL   A CG2 
2053 N N   . GLY   A 97  ? 0.1378 0.1449 0.1451 -0.0042 0.0104  0.0111  97  GLY   A N   
2054 C CA  . GLY   A 97  ? 0.1563 0.1599 0.1351 -0.0047 0.0033  0.0097  97  GLY   A CA  
2055 C C   . GLY   A 97  ? 0.1546 0.1783 0.1285 -0.0124 -0.0041 0.0109  97  GLY   A C   
2056 O O   . GLY   A 97  ? 0.1695 0.1660 0.1571 -0.0142 -0.0010 0.0170  97  GLY   A O   
2060 N N   A PRO   A 98  ? 0.1547 0.1759 0.1268 -0.0068 0.0009  0.0162  98  PRO   A N   
2061 N N   B PRO   A 98  ? 0.1609 0.1783 0.1373 -0.0058 -0.0033 0.0149  98  PRO   A N   
2062 C CA  A PRO   A 98  ? 0.1686 0.2104 0.1388 -0.0195 0.0040  0.0009  98  PRO   A CA  
2063 C CA  B PRO   A 98  ? 0.1692 0.1874 0.1463 -0.0059 -0.0060 0.0151  98  PRO   A CA  
2064 C C   A PRO   A 98  ? 0.1750 0.2208 0.1297 -0.0267 -0.0008 0.0230  98  PRO   A C   
2065 C C   B PRO   A 98  ? 0.1784 0.1879 0.1466 -0.0056 -0.0127 0.0304  98  PRO   A C   
2066 O O   A PRO   A 98  ? 0.1648 0.1846 0.1450 -0.0172 0.0083  0.0186  98  PRO   A O   
2067 O O   B PRO   A 98  ? 0.1772 0.1840 0.1646 0.0004  -0.0108 0.0178  98  PRO   A O   
2068 C CB  A PRO   A 98  ? 0.1830 0.2225 0.1484 -0.0034 0.0049  -0.0088 98  PRO   A CB  
2069 C CB  B PRO   A 98  ? 0.1707 0.1904 0.1493 -0.0008 -0.0043 0.0106  98  PRO   A CB  
2070 C CG  A PRO   A 98  ? 0.1823 0.1991 0.1444 0.0019  0.0035  -0.0222 98  PRO   A CG  
2071 C CG  B PRO   A 98  ? 0.1702 0.1851 0.1466 -0.0014 -0.0002 0.0052  98  PRO   A CG  
2072 C CD  A PRO   A 98  ? 0.1606 0.1800 0.1370 0.0032  0.0101  -0.0035 98  PRO   A CD  
2073 C CD  B PRO   A 98  ? 0.1643 0.1790 0.1371 -0.0027 0.0019  0.0118  98  PRO   A CD  
2088 N N   A ASN   A 99  ? 0.1816 0.2506 0.1449 -0.0335 -0.0103 0.0490  99  ASN   A N   
2089 N N   B ASN   A 99  ? 0.1871 0.1913 0.1412 -0.0052 -0.0196 0.0627  99  ASN   A N   
2090 C CA  A ASN   A 99  ? 0.2067 0.2728 0.1513 -0.0353 -0.0160 0.0680  99  ASN   A CA  
2091 C CA  B ASN   A 99  ? 0.2010 0.1977 0.1490 -0.0026 -0.0259 0.0838  99  ASN   A CA  
2092 C C   A ASN   A 99  ? 0.2272 0.3107 0.1525 -0.0442 -0.0115 0.0848  99  ASN   A C   
2093 C C   B ASN   A 99  ? 0.2139 0.2059 0.1581 0.0006  -0.0235 0.0783  99  ASN   A C   
2094 O O   A ASN   A 99  ? 0.2449 0.3307 0.1789 -0.0391 -0.0250 0.0700  99  ASN   A O   
2095 O O   B ASN   A 99  ? 0.2116 0.1889 0.1442 0.0103  -0.0320 0.0763  99  ASN   A O   
2096 C CB  A ASN   A 99  ? 0.2057 0.2634 0.1953 -0.0384 -0.0441 0.0658  99  ASN   A CB  
2097 C CB  B ASN   A 99  ? 0.2019 0.2005 0.1733 -0.0017 -0.0386 0.0990  99  ASN   A CB  
2098 C CG  A ASN   A 99  ? 0.2071 0.2611 0.2371 -0.0394 -0.0487 0.0325  99  ASN   A CG  
2099 C CG  B ASN   A 99  ? 0.2018 0.2079 0.1978 -0.0031 -0.0420 0.1031  99  ASN   A CG  
2100 O OD1 A ASN   A 99  ? 0.2192 0.2729 0.2396 -0.0252 -0.0453 0.0364  99  ASN   A OD1 
2101 O OD1 B ASN   A 99  ? 0.2045 0.2074 0.1884 -0.0105 -0.0380 0.1135  99  ASN   A OD1 
2102 N ND2 A ASN   A 99  ? 0.2122 0.2499 0.2591 -0.0368 -0.0450 0.0289  99  ASN   A ND2 
2103 N ND2 B ASN   A 99  ? 0.2005 0.2132 0.1936 0.0085  -0.0418 0.1016  99  ASN   A ND2 
2116 N N   A VAL   A 100 ? 0.2416 0.3293 0.1598 -0.0598 -0.0429 0.0790  100 VAL   A N   
2117 N N   B VAL   A 100 ? 0.2315 0.2338 0.1839 -0.0058 -0.0218 0.0674  100 VAL   A N   
2118 C CA  A VAL   A 100 ? 0.2711 0.3551 0.1781 -0.0665 -0.0480 0.0694  100 VAL   A CA  
2119 C CA  B VAL   A 100 ? 0.2521 0.2647 0.2216 -0.0109 -0.0188 0.0501  100 VAL   A CA  
2120 C C   A VAL   A 100 ? 0.2841 0.3749 0.1500 -0.0644 -0.0518 0.0901  100 VAL   A C   
2121 C C   B VAL   A 100 ? 0.2651 0.2860 0.2370 -0.0100 -0.0201 0.0546  100 VAL   A C   
2122 O O   A VAL   A 100 ? 0.2934 0.3941 0.1819 -0.0533 -0.0213 0.0902  100 VAL   A O   
2123 O O   B VAL   A 100 ? 0.2667 0.2924 0.2451 -0.0058 -0.0193 0.0518  100 VAL   A O   
2124 C CB  A VAL   A 100 ? 0.2900 0.3568 0.2120 -0.0715 -0.0529 0.0469  100 VAL   A CB  
2125 C CB  B VAL   A 100 ? 0.2584 0.2715 0.2459 -0.0121 -0.0177 0.0331  100 VAL   A CB  
2126 C CG1 A VAL   A 100 ? 0.2917 0.3622 0.2395 -0.0697 -0.0478 0.0361  100 VAL   A CG1 
2127 C CG1 B VAL   A 100 ? 0.2599 0.2736 0.2611 -0.0137 -0.0172 0.0273  100 VAL   A CG1 
2128 C CG2 A VAL   A 100 ? 0.3025 0.3579 0.2245 -0.0767 -0.0447 0.0397  100 VAL   A CG2 
2129 C CG2 B VAL   A 100 ? 0.2604 0.2742 0.2555 -0.0112 -0.0136 0.0264  100 VAL   A CG2 
2148 N N   A ASN   A 101 ? 0.2903 0.3747 0.1850 -0.0747 -0.0631 0.1222  101 ASN   A N   
2149 N N   B ASN   A 101 ? 0.2791 0.2970 0.2509 -0.0155 -0.0208 0.0595  101 ASN   A N   
2150 C CA  A ASN   A 101 ? 0.3124 0.3810 0.2187 -0.0737 -0.0610 0.1468  101 ASN   A CA  
2151 C CA  B ASN   A 101 ? 0.2957 0.3071 0.2681 -0.0169 -0.0228 0.0625  101 ASN   A CA  
2152 C C   A ASN   A 101 ? 0.3371 0.4124 0.2516 -0.0742 -0.0232 0.1744  101 ASN   A C   
2153 C C   B ASN   A 101 ? 0.3105 0.3273 0.2929 -0.0185 -0.0160 0.0718  101 ASN   A C   
2154 O O   A ASN   A 101 ? 0.3508 0.4194 0.3083 -0.0755 -0.0199 0.1525  101 ASN   A O   
2155 O O   B ASN   A 101 ? 0.3125 0.3276 0.2805 -0.0158 -0.0171 0.0823  101 ASN   A O   
2156 C CB  A ASN   A 101 ? 0.3070 0.3545 0.2175 -0.0691 -0.0817 0.1234  101 ASN   A CB  
2157 C CB  B ASN   A 101 ? 0.2973 0.2979 0.2606 -0.0182 -0.0265 0.0548  101 ASN   A CB  
2158 C CG  A ASN   A 101 ? 0.3040 0.3287 0.2043 -0.0727 -0.0793 0.0885  101 ASN   A CG  
2159 C CG  B ASN   A 101 ? 0.2988 0.2921 0.2612 -0.0208 -0.0287 0.0488  101 ASN   A CG  
2160 O OD1 A ASN   A 101 ? 0.2936 0.3217 0.2080 -0.0634 -0.0692 0.0522  101 ASN   A OD1 
2161 O OD1 B ASN   A 101 ? 0.2991 0.2918 0.2680 -0.0208 -0.0291 0.0517  101 ASN   A OD1 
2162 N ND2 A ASN   A 101 ? 0.3097 0.3237 0.2054 -0.0752 -0.0846 0.0860  101 ASN   A ND2 
2163 N ND2 B ASN   A 101 ? 0.2996 0.2881 0.2597 -0.0246 -0.0292 0.0423  101 ASN   A ND2 
2176 N N   A LYS   A 102 ? 0.3427 0.4538 0.2897 -0.0892 -0.0057 0.1913  102 LYS   A N   
2177 N N   B LYS   A 102 ? 0.3217 0.3465 0.3281 -0.0262 -0.0079 0.0626  102 LYS   A N   
2178 C CA  A LYS   A 102 ? 0.3592 0.4898 0.2948 -0.0911 -0.0069 0.1813  102 LYS   A CA  
2179 C CA  B LYS   A 102 ? 0.3331 0.3631 0.3506 -0.0336 -0.0036 0.0474  102 LYS   A CA  
2180 C C   A LYS   A 102 ? 0.3690 0.5182 0.2816 -0.0806 -0.0102 0.1689  102 LYS   A C   
2181 C C   B LYS   A 102 ? 0.3388 0.3720 0.3614 -0.0329 -0.0074 0.0446  102 LYS   A C   
2182 O O   A LYS   A 102 ? 0.3739 0.5380 0.2940 -0.0753 -0.0087 0.1562  102 LYS   A O   
2183 O O   B LYS   A 102 ? 0.3433 0.3776 0.3706 -0.0345 -0.0088 0.0423  102 LYS   A O   
2184 C CB  A LYS   A 102 ? 0.3744 0.5001 0.3462 -0.1003 -0.0193 0.1581  102 LYS   A CB  
2185 C CB  B LYS   A 102 ? 0.3395 0.3695 0.3654 -0.0398 0.0018  0.0343  102 LYS   A CB  
2186 C CG  A LYS   A 102 ? 0.3882 0.5089 0.3960 -0.1077 -0.0317 0.1265  102 LYS   A CG  
2187 C CG  B LYS   A 102 ? 0.3457 0.3745 0.3769 -0.0453 0.0081  0.0230  102 LYS   A CG  
2188 C CD  A LYS   A 102 ? 0.4036 0.5188 0.4436 -0.1091 -0.0416 0.0912  102 LYS   A CD  
2189 C CD  B LYS   A 102 ? 0.3520 0.3783 0.3867 -0.0492 0.0146  0.0112  102 LYS   A CD  
2190 C CE  A LYS   A 102 ? 0.4176 0.5270 0.4816 -0.1064 -0.0494 0.0697  102 LYS   A CE  
2191 C CE  B LYS   A 102 ? 0.3569 0.3810 0.3957 -0.0516 0.0211  0.0021  102 LYS   A CE  
2192 N NZ  A LYS   A 102 ? 0.4249 0.5314 0.5030 -0.1082 -0.0535 0.0555  102 LYS   A NZ  
2193 N NZ  B LYS   A 102 ? 0.3598 0.3815 0.3997 -0.0536 0.0261  -0.0038 102 LYS   A NZ  
2220 N N   A GLY   A 103 ? 0.3672 0.5292 0.2894 -0.0677 -0.0261 0.1406  103 GLY   A N   
2221 N N   B GLY   A 103 ? 0.3394 0.3738 0.3620 -0.0290 -0.0106 0.0428  103 GLY   A N   
2222 C CA  A GLY   A 103 ? 0.3630 0.5323 0.2824 -0.0564 -0.0212 0.1091  103 GLY   A CA  
2223 C CA  B GLY   A 103 ? 0.3382 0.3742 0.3498 -0.0255 -0.0122 0.0406  103 GLY   A CA  
2224 C C   A GLY   A 103 ? 0.3514 0.5339 0.2729 -0.0509 -0.0039 0.0768  103 GLY   A C   
2225 C C   B GLY   A 103 ? 0.3358 0.3739 0.3370 -0.0197 -0.0123 0.0352  103 GLY   A C   
2226 O O   A GLY   A 103 ? 0.3605 0.5417 0.2877 -0.0468 -0.0073 0.0623  103 GLY   A O   
2227 O O   B GLY   A 103 ? 0.3371 0.3764 0.3528 -0.0208 -0.0124 0.0342  103 GLY   A O   
2234 N N   A GLU   A 104 ? 0.3257 0.5224 0.2168 -0.0535 0.0158  0.0617  104 GLU   A N   
2235 N N   B GLU   A 104 ? 0.3304 0.3684 0.3006 -0.0120 -0.0132 0.0344  104 GLU   A N   
2236 C CA  A GLU   A 104 ? 0.3014 0.5051 0.1921 -0.0615 0.0279  0.0440  104 GLU   A CA  
2237 C CA  B GLU   A 104 ? 0.3265 0.3628 0.2725 -0.0067 -0.0149 0.0272  104 GLU   A CA  
2238 C C   A GLU   A 104 ? 0.3075 0.5100 0.1836 -0.0595 0.0253  0.0087  104 GLU   A C   
2239 C C   B GLU   A 104 ? 0.3264 0.3610 0.2645 -0.0007 -0.0139 0.0194  104 GLU   A C   
2240 O O   A GLU   A 104 ? 0.2997 0.5155 0.2030 -0.0635 0.0086  -0.0019 104 GLU   A O   
2241 O O   B GLU   A 104 ? 0.3239 0.3574 0.2546 -0.0002 -0.0186 0.0219  104 GLU   A O   
2242 C CB  A GLU   A 104 ? 0.2691 0.4796 0.1815 -0.0703 0.0281  0.0711  104 GLU   A CB  
2243 C CB  B GLU   A 104 ? 0.3242 0.3609 0.2616 -0.0076 -0.0169 0.0269  104 GLU   A CB  
2244 C CG  A GLU   A 104 ? 0.2533 0.4566 0.1925 -0.0715 0.0109  0.0872  104 GLU   A CG  
2245 C CG  B GLU   A 104 ? 0.3244 0.3617 0.2632 -0.0079 -0.0195 0.0264  104 GLU   A CG  
2246 C CD  A GLU   A 104 ? 0.2311 0.4313 0.1839 -0.0745 0.0016  0.1072  104 GLU   A CD  
2247 C CD  B GLU   A 104 ? 0.3243 0.3641 0.2628 -0.0076 -0.0201 0.0241  104 GLU   A CD  
2248 O OE1 A GLU   A 104 ? 0.2140 0.4045 0.1566 -0.0749 -0.0150 0.1049  104 GLU   A OE1 
2249 O OE1 B GLU   A 104 ? 0.3252 0.3647 0.2629 -0.0090 -0.0215 0.0212  104 GLU   A OE1 
2250 O OE2 A GLU   A 104 ? 0.2411 0.4312 0.2022 -0.0753 0.0037  0.1282  104 GLU   A OE2 
2251 O OE2 B GLU   A 104 ? 0.3248 0.3664 0.2664 -0.0059 -0.0211 0.0221  104 GLU   A OE2 
2264 N N   A ASP   A 105 ? 0.3170 0.5076 0.1919 -0.0550 0.0333  -0.0245 105 ASP   A N   
2265 N N   B ASP   A 105 ? 0.3299 0.3634 0.2817 0.0029  -0.0091 0.0092  105 ASP   A N   
2266 C CA  A ASP   A 105 ? 0.3261 0.5026 0.2356 -0.0443 0.0450  -0.0577 105 ASP   A CA  
2267 C CA  B ASP   A 105 ? 0.3333 0.3654 0.3104 0.0074  -0.0029 -0.0033 105 ASP   A CA  
2268 C C   A ASP   A 105 ? 0.2936 0.4767 0.1915 -0.0543 0.0358  -0.0822 105 ASP   A C   
2269 C C   B ASP   A 105 ? 0.3357 0.3644 0.3066 0.0001  -0.0017 -0.0072 105 ASP   A C   
2270 O O   A ASP   A 105 ? 0.2722 0.4574 0.1629 -0.0507 0.0365  -0.1051 105 ASP   A O   
2271 O O   B ASP   A 105 ? 0.3335 0.3654 0.2978 0.0011  -0.0021 -0.0072 105 ASP   A O   
2272 C CB  A ASP   A 105 ? 0.3597 0.5228 0.3163 -0.0276 0.0569  -0.0678 105 ASP   A CB  
2273 C CB  B ASP   A 105 ? 0.3332 0.3669 0.3445 0.0170  0.0028  -0.0134 105 ASP   A CB  
2274 C CG  A ASP   A 105 ? 0.3868 0.5391 0.3911 -0.0117 0.0582  -0.0820 105 ASP   A CG  
2275 C CG  B ASP   A 105 ? 0.3330 0.3677 0.3763 0.0253  0.0077  -0.0248 105 ASP   A CG  
2276 O OD1 A ASP   A 105 ? 0.3931 0.5456 0.4039 -0.0096 0.0587  -0.0959 105 ASP   A OD1 
2277 O OD1 B ASP   A 105 ? 0.3317 0.3671 0.3796 0.0263  0.0055  -0.0313 105 ASP   A OD1 
2278 O OD2 A ASP   A 105 ? 0.4028 0.5463 0.4399 -0.0084 0.0559  -0.0769 105 ASP   A OD2 
2279 O OD2 B ASP   A 105 ? 0.3325 0.3676 0.3885 0.0299  0.0145  -0.0271 105 ASP   A OD2 
2288 N N   A ILE   A 106 ? 0.2763 0.4573 0.2020 -0.0635 0.0163  -0.0847 106 ILE   A N   
2289 N N   B ILE   A 106 ? 0.3388 0.3614 0.3107 -0.0065 0.0002  -0.0111 106 ILE   A N   
2290 C CA  A ILE   A 106 ? 0.2515 0.4292 0.2225 -0.0780 -0.0072 -0.1056 106 ILE   A CA  
2291 C CA  B ILE   A 106 ? 0.3414 0.3589 0.3184 -0.0153 0.0012  -0.0167 106 ILE   A CA  
2292 C C   A ILE   A 106 ? 0.2399 0.3938 0.2453 -0.0940 0.0026  -0.1233 106 ILE   A C   
2293 C C   B ILE   A 106 ? 0.3393 0.3523 0.3203 -0.0221 0.0105  -0.0228 106 ILE   A C   
2294 O O   A ILE   A 106 ? 0.2163 0.3755 0.2610 -0.0956 0.0231  -0.1162 106 ILE   A O   
2295 O O   B ILE   A 106 ? 0.3377 0.3508 0.3128 -0.0203 0.0119  -0.0181 106 ILE   A O   
2296 C CB  A ILE   A 106 ? 0.2570 0.4405 0.2834 -0.0656 -0.0349 -0.0703 106 ILE   A CB  
2297 C CB  B ILE   A 106 ? 0.3463 0.3634 0.3334 -0.0168 -0.0056 -0.0140 106 ILE   A CB  
2298 C CG1 A ILE   A 106 ? 0.2451 0.4400 0.3279 -0.0513 -0.0301 -0.0392 106 ILE   A CG1 
2299 C CG1 B ILE   A 106 ? 0.3457 0.3642 0.3458 -0.0161 -0.0061 -0.0117 106 ILE   A CG1 
2300 C CG2 A ILE   A 106 ? 0.2720 0.4457 0.3121 -0.0625 -0.0402 -0.0604 106 ILE   A CG2 
2301 C CG2 B ILE   A 106 ? 0.3494 0.3656 0.3354 -0.0174 -0.0080 -0.0125 106 ILE   A CG2 
2302 C CD1 A ILE   A 106 ? 0.2454 0.4356 0.3506 -0.0368 -0.0182 -0.0235 106 ILE   A CD1 
2303 C CD1 B ILE   A 106 ? 0.3462 0.3631 0.3540 -0.0150 -0.0047 -0.0110 106 ILE   A CD1 
2326 N N   A GLN   A 107 ? 0.2690 0.3798 0.2787 -0.0900 0.0162  -0.1390 107 GLN   A N   
2327 N N   B GLN   A 107 ? 0.3374 0.3460 0.3305 -0.0301 0.0207  -0.0340 107 GLN   A N   
2328 C CA  A GLN   A 107 ? 0.3048 0.3644 0.3674 -0.0776 0.0369  -0.1303 107 GLN   A CA  
2329 C CA  B GLN   A 107 ? 0.3339 0.3395 0.3572 -0.0394 0.0299  -0.0421 107 GLN   A CA  
2330 C C   A GLN   A 107 ? 0.2701 0.3059 0.3579 -0.0709 0.0645  -0.1002 107 GLN   A C   
2331 C C   B GLN   A 107 ? 0.2915 0.3015 0.3232 -0.0513 0.0505  -0.0578 107 GLN   A C   
2332 O O   A GLN   A 107 ? 0.2664 0.2937 0.4251 -0.0676 0.0803  -0.1076 107 GLN   A O   
2333 O O   B GLN   A 107 ? 0.2940 0.3010 0.3411 -0.0550 0.0538  -0.0577 107 GLN   A O   
2334 C CB  A GLN   A 107 ? 0.3640 0.4036 0.4712 -0.0818 0.0157  -0.1315 107 GLN   A CB  
2335 C CB  B GLN   A 107 ? 0.3673 0.3674 0.4156 -0.0389 0.0173  -0.0334 107 GLN   A CB  
2336 C CG  A GLN   A 107 ? 0.4277 0.4476 0.5896 -0.0784 -0.0013 -0.1134 107 GLN   A CG  
2337 C CG  B GLN   A 107 ? 0.3966 0.3934 0.4745 -0.0372 0.0052  -0.0233 107 GLN   A CG  
2338 C CD  A GLN   A 107 ? 0.4785 0.4799 0.6958 -0.0736 -0.0110 -0.0933 107 GLN   A CD  
2339 C CD  B GLN   A 107 ? 0.4192 0.4129 0.5276 -0.0352 -0.0037 -0.0143 107 GLN   A CD  
2340 O OE1 A GLN   A 107 ? 0.4972 0.4896 0.7330 -0.0729 -0.0134 -0.0838 107 GLN   A OE1 
2341 O OE1 B GLN   A 107 ? 0.4261 0.4189 0.5445 -0.0341 -0.0076 -0.0110 107 GLN   A OE1 
2342 N NE2 A GLN   A 107 ? 0.4926 0.4908 0.7285 -0.0716 -0.0157 -0.0909 107 GLN   A NE2 
2343 N NE2 B GLN   A 107 ? 0.4259 0.4174 0.5426 -0.0348 -0.0081 -0.0119 107 GLN   A NE2 
2360 N N   . LEU   A 108 ? 0.2461 0.2639 0.2831 -0.0587 0.0621  -0.0775 108 LEU   A N   
2361 C CA  . LEU   A 108 ? 0.2077 0.2136 0.2294 -0.0263 0.0467  -0.0455 108 LEU   A CA  
2362 C C   . LEU   A 108 ? 0.1810 0.1708 0.2062 -0.0078 0.0351  -0.0087 108 LEU   A C   
2363 O O   . LEU   A 108 ? 0.1834 0.1629 0.2329 -0.0002 0.0410  0.0033  108 LEU   A O   
2364 C CB  . LEU   A 108 ? 0.2096 0.2274 0.2111 -0.0260 0.0540  -0.0425 108 LEU   A CB  
2365 C CG  . LEU   A 108 ? 0.2215 0.2476 0.2436 -0.0259 0.0614  -0.0478 108 LEU   A CG  
2366 C CD1 . LEU   A 108 ? 0.2418 0.2522 0.2581 -0.0368 0.0665  -0.0338 108 LEU   A CD1 
2367 C CD2 . LEU   A 108 ? 0.2253 0.2725 0.2995 -0.0138 0.0597  -0.0335 108 LEU   A CD2 
2380 N N   . LEU   A 109 ? 0.1605 0.1657 0.2051 0.0013  0.0221  0.0005  109 LEU   A N   
2381 C CA  . LEU   A 109 ? 0.1578 0.1641 0.1882 0.0049  0.0056  0.0130  109 LEU   A CA  
2382 C C   . LEU   A 109 ? 0.1515 0.1517 0.1850 -0.0068 0.0136  0.0034  109 LEU   A C   
2383 O O   . LEU   A 109 ? 0.1567 0.1397 0.2174 -0.0038 0.0020  0.0063  109 LEU   A O   
2384 C CB  . LEU   A 109 ? 0.1639 0.1670 0.2224 0.0149  0.0052  0.0210  109 LEU   A CB  
2385 C CG  . LEU   A 109 ? 0.1632 0.1728 0.2250 0.0061  0.0111  0.0250  109 LEU   A CG  
2386 C CD1 . LEU   A 109 ? 0.1635 0.1639 0.2285 -0.0082 0.0143  0.0038  109 LEU   A CD1 
2387 C CD2 . LEU   A 109 ? 0.1609 0.1917 0.2425 0.0068  0.0060  0.0354  109 LEU   A CD2 
2399 N N   . LYS   A 110 ? 0.1536 0.1581 0.1901 -0.0025 -0.0066 -0.0050 110 LYS   A N   
2400 C CA  . LYS   A 110 ? 0.1568 0.1518 0.2006 -0.0084 -0.0141 0.0099  110 LYS   A CA  
2401 C C   . LYS   A 110 ? 0.1543 0.1370 0.1834 -0.0120 0.0024  0.0039  110 LYS   A C   
2402 O O   . LYS   A 110 ? 0.1422 0.1319 0.2137 -0.0053 0.0037  -0.0033 110 LYS   A O   
2403 C CB  . LYS   A 110 ? 0.1679 0.1625 0.2249 -0.0013 -0.0203 -0.0072 110 LYS   A CB  
2404 C CG  . LYS   A 110 ? 0.1685 0.1626 0.2254 -0.0039 -0.0208 -0.0086 110 LYS   A CG  
2405 C CD  . LYS   A 110 ? 0.1703 0.1709 0.2348 -0.0130 -0.0109 -0.0068 110 LYS   A CD  
2406 C CE  . LYS   A 110 ? 0.1738 0.1755 0.2512 -0.0080 -0.0025 -0.0057 110 LYS   A CE  
2407 N NZ  . LYS   A 110 ? 0.1735 0.1763 0.2629 -0.0176 0.0142  0.0031  110 LYS   A NZ  
2421 N N   . SER   A 111 ? 0.1596 0.1456 0.1884 -0.0073 0.0024  0.0004  111 SER   A N   
2422 C CA  . SER   A 111 ? 0.1524 0.1519 0.1931 -0.0070 0.0092  0.0028  111 SER   A CA  
2423 C C   . SER   A 111 ? 0.1423 0.1490 0.1893 -0.0092 0.0174  0.0016  111 SER   A C   
2424 O O   . SER   A 111 ? 0.1511 0.1411 0.2177 -0.0073 0.0197  0.0046  111 SER   A O   
2425 C CB  . SER   A 111 ? 0.1618 0.1724 0.2108 -0.0055 0.0141  -0.0203 111 SER   A CB  
2426 O OG  . SER   A 111 ? 0.2053 0.1931 0.2110 0.0049  0.0148  -0.0251 111 SER   A OG  
2432 N N   . ALA   A 112 ? 0.1452 0.1444 0.1858 0.0034  0.0211  0.0018  112 ALA   A N   
2433 C CA  . ALA   A 112 ? 0.1472 0.1378 0.1723 -0.0039 0.0235  -0.0033 112 ALA   A CA  
2434 C C   . ALA   A 112 ? 0.1384 0.1187 0.1857 0.0058  0.0095  -0.0038 112 ALA   A C   
2435 O O   . ALA   A 112 ? 0.1473 0.1355 0.1910 -0.0155 0.0136  0.0065  112 ALA   A O   
2436 C CB  . ALA   A 112 ? 0.1609 0.1402 0.1855 -0.0076 0.0178  0.0123  112 ALA   A CB  
2442 N N   . TYR   A 113 ? 0.1275 0.1364 0.1983 -0.0099 0.0113  0.0095  113 TYR   A N   
2443 C CA  . TYR   A 113 ? 0.1345 0.1302 0.1954 -0.0089 0.0228  0.0122  113 TYR   A CA  
2444 C C   . TYR   A 113 ? 0.1376 0.1292 0.1820 -0.0098 0.0102  0.0077  113 TYR   A C   
2445 O O   . TYR   A 113 ? 0.1377 0.1388 0.2072 -0.0083 0.0180  0.0091  113 TYR   A O   
2446 C CB  . TYR   A 113 ? 0.1396 0.1401 0.1940 -0.0056 0.0082  0.0200  113 TYR   A CB  
2447 C CG  . TYR   A 113 ? 0.1325 0.1373 0.1762 -0.0136 0.0172  0.0216  113 TYR   A CG  
2448 C CD1 . TYR   A 113 ? 0.1380 0.1484 0.1883 0.0059  0.0172  0.0263  113 TYR   A CD1 
2449 C CD2 . TYR   A 113 ? 0.1443 0.1405 0.1861 -0.0184 0.0068  0.0201  113 TYR   A CD2 
2450 C CE1 . TYR   A 113 ? 0.1421 0.1573 0.1832 -0.0024 0.0172  0.0249  113 TYR   A CE1 
2451 C CE2 . TYR   A 113 ? 0.1409 0.1461 0.2003 -0.0085 0.0064  0.0260  113 TYR   A CE2 
2452 C CZ  . TYR   A 113 ? 0.1411 0.1514 0.1803 -0.0023 0.0169  0.0301  113 TYR   A CZ  
2453 O OH  . TYR   A 113 ? 0.1426 0.1569 0.1977 0.0102  0.0143  0.0273  113 TYR   A OH  
2463 N N   . GLU   A 114 ? 0.1297 0.1242 0.1950 0.0017  0.0156  0.0100  114 GLU   A N   
2464 C CA  . GLU   A 114 ? 0.1390 0.1164 0.2008 0.0050  0.0098  0.0063  114 GLU   A CA  
2465 C C   . GLU   A 114 ? 0.1297 0.1259 0.1994 -0.0013 0.0066  0.0154  114 GLU   A C   
2466 O O   . GLU   A 114 ? 0.1467 0.1298 0.2097 0.0013  0.0053  0.0176  114 GLU   A O   
2467 C CB  . GLU   A 114 ? 0.1381 0.1245 0.2131 -0.0036 0.0019  0.0061  114 GLU   A CB  
2468 C CG  . GLU   A 114 ? 0.1406 0.1272 0.2345 -0.0029 0.0123  -0.0023 114 GLU   A CG  
2469 C CD  . GLU   A 114 ? 0.1554 0.1265 0.2439 -0.0089 -0.0033 0.0013  114 GLU   A CD  
2470 O OE1 . GLU   A 114 ? 0.1622 0.1304 0.2444 -0.0114 0.0136  -0.0113 114 GLU   A OE1 
2471 O OE2 . GLU   A 114 ? 0.1704 0.1495 0.2564 -0.0185 0.0078  -0.0148 114 GLU   A OE2 
2478 N N   . ASN   A 115 ? 0.1326 0.1336 0.1940 -0.0093 0.0115  0.0109  115 ASN   A N   
2479 C CA  . ASN   A 115 ? 0.1410 0.1407 0.2065 -0.0098 0.0113  0.0138  115 ASN   A CA  
2480 C C   . ASN   A 115 ? 0.1380 0.1476 0.1930 -0.0116 0.0039  0.0170  115 ASN   A C   
2481 O O   . ASN   A 115 ? 0.1412 0.1489 0.2108 -0.0083 0.0135  0.0234  115 ASN   A O   
2482 C CB  . ASN   A 115 ? 0.1468 0.1393 0.2010 -0.0130 0.0085  0.0212  115 ASN   A CB  
2483 C CG  . ASN   A 115 ? 0.1485 0.1581 0.2028 -0.0094 0.0214  0.0196  115 ASN   A CG  
2484 O OD1 . ASN   A 115 ? 0.1488 0.2536 0.2261 -0.0092 0.0305  0.0253  115 ASN   A OD1 
2485 N ND2 . ASN   A 115 ? 0.1427 0.1429 0.2021 -0.0101 0.0356  0.0197  115 ASN   A ND2 
2492 N N   . PHE   A 116 ? 0.1312 0.1505 0.1986 -0.0026 0.0111  0.0218  116 PHE   A N   
2493 C CA  . PHE   A 116 ? 0.1344 0.1528 0.1899 -0.0021 0.0156  0.0181  116 PHE   A CA  
2494 C C   . PHE   A 116 ? 0.1298 0.1586 0.1973 -0.0047 0.0183  0.0307  116 PHE   A C   
2495 O O   . PHE   A 116 ? 0.1469 0.1558 0.2050 0.0047  0.0179  0.0359  116 PHE   A O   
2496 C CB  . PHE   A 116 ? 0.1291 0.1486 0.2113 -0.0038 0.0216  0.0228  116 PHE   A CB  
2497 C CG  . PHE   A 116 ? 0.1303 0.1438 0.1972 -0.0075 0.0209  0.0188  116 PHE   A CG  
2498 C CD1 . PHE   A 116 ? 0.1340 0.1364 0.1871 -0.0044 0.0136  0.0181  116 PHE   A CD1 
2499 C CD2 . PHE   A 116 ? 0.1337 0.1477 0.2085 -0.0048 0.0202  0.0254  116 PHE   A CD2 
2500 C CE1 . PHE   A 116 ? 0.1374 0.1406 0.1909 -0.0268 0.0063  0.0106  116 PHE   A CE1 
2501 C CE2 . PHE   A 116 ? 0.1318 0.1469 0.2198 -0.0042 0.0176  0.0107  116 PHE   A CE2 
2502 C CZ  . PHE   A 116 ? 0.1429 0.1324 0.2030 -0.0109 0.0051  0.0090  116 PHE   A CZ  
2512 N N   . ASN   A 117 ? 0.1340 0.1505 0.2096 -0.0025 0.0180  0.0384  117 ASN   A N   
2513 C CA  . ASN   A 117 ? 0.1475 0.1561 0.2139 -0.0013 0.0167  0.0376  117 ASN   A CA  
2514 C C   . ASN   A 117 ? 0.1435 0.1569 0.2236 -0.0032 0.0148  0.0325  117 ASN   A C   
2515 O O   . ASN   A 117 ? 0.1509 0.1591 0.2424 -0.0100 0.0003  0.0403  117 ASN   A O   
2516 C CB  . ASN   A 117 ? 0.1482 0.1643 0.2166 -0.0014 0.0092  0.0408  117 ASN   A CB  
2517 C CG  . ASN   A 117 ? 0.1450 0.1540 0.2316 -0.0079 0.0124  0.0390  117 ASN   A CG  
2518 O OD1 . ASN   A 117 ? 0.1434 0.1735 0.2343 -0.0166 0.0162  0.0247  117 ASN   A OD1 
2519 N ND2 . ASN   A 117 ? 0.1340 0.1436 0.2269 -0.0065 0.0106  0.0354  117 ASN   A ND2 
2526 N N   . GLN   A 118 ? 0.1405 0.1511 0.2293 -0.0086 0.0077  0.0337  118 GLN   A N   
2527 C CA  . GLN   A 118 ? 0.1497 0.1659 0.2262 -0.0165 -0.0040 0.0340  118 GLN   A CA  
2528 C C   . GLN   A 118 ? 0.1520 0.1679 0.2228 -0.0114 -0.0042 0.0457  118 GLN   A C   
2529 O O   . GLN   A 118 ? 0.1501 0.1990 0.2437 -0.0030 -0.0107 0.0210  118 GLN   A O   
2530 C CB  . GLN   A 118 ? 0.1527 0.1706 0.2358 -0.0132 0.0136  0.0318  118 GLN   A CB  
2531 C CG  . GLN   A 118 ? 0.1351 0.1704 0.2283 -0.0050 0.0025  0.0418  118 GLN   A CG  
2532 C CD  . GLN   A 118 ? 0.1418 0.1803 0.2361 -0.0034 0.0014  0.0246  118 GLN   A CD  
2533 O OE1 . GLN   A 118 ? 0.1443 0.1792 0.2724 0.0063  0.0016  0.0173  118 GLN   A OE1 
2534 N NE2 . GLN   A 118 ? 0.1507 0.1784 0.2274 0.0063  0.0016  0.0244  118 GLN   A NE2 
2543 N N   . HIS   A 119 ? 0.1555 0.1599 0.2109 -0.0034 0.0006  0.0409  119 HIS   A N   
2544 C CA  . HIS   A 119 ? 0.1638 0.1775 0.2061 -0.0092 0.0055  0.0527  119 HIS   A CA  
2545 C C   . HIS   A 119 ? 0.1885 0.1963 0.2055 -0.0162 0.0148  0.0509  119 HIS   A C   
2546 O O   . HIS   A 119 ? 0.1877 0.1939 0.2031 -0.0350 -0.0085 0.0494  119 HIS   A O   
2547 C CB  . HIS   A 119 ? 0.1609 0.1765 0.2150 -0.0134 0.0232  0.0406  119 HIS   A CB  
2548 C CG  . HIS   A 119 ? 0.1592 0.1720 0.2654 -0.0008 0.0118  0.0475  119 HIS   A CG  
2549 N ND1 . HIS   A 119 ? 0.1747 0.1917 0.3323 -0.0137 0.0154  0.0316  119 HIS   A ND1 
2550 C CD2 . HIS   A 119 ? 0.1683 0.1815 0.2766 0.0126  0.0248  0.0600  119 HIS   A CD2 
2551 C CE1 . HIS   A 119 ? 0.1727 0.1938 0.3403 -0.0176 0.0193  0.0516  119 HIS   A CE1 
2552 N NE2 . HIS   A 119 ? 0.1777 0.1920 0.3188 -0.0065 0.0363  0.0703  119 HIS   A NE2 
2560 N N   A GLU   A 120 ? 0.1824 0.2117 0.2093 -0.0080 -0.0045 0.0833  120 GLU   A N   
2561 N N   B GLU   A 120 ? 0.2221 0.2342 0.2371 -0.0150 0.0122  0.0494  120 GLU   A N   
2562 C CA  A GLU   A 120 ? 0.2066 0.2355 0.2443 0.0003  -0.0127 0.1294  120 GLU   A CA  
2563 C CA  B GLU   A 120 ? 0.2570 0.2701 0.2782 -0.0136 0.0081  0.0528  120 GLU   A CA  
2564 C C   A GLU   A 120 ? 0.1876 0.2222 0.2130 -0.0133 -0.0028 0.1263  120 GLU   A C   
2565 C C   B GLU   A 120 ? 0.2463 0.2649 0.2450 -0.0172 0.0046  0.0542  120 GLU   A C   
2566 O O   A GLU   A 120 ? 0.1821 0.2139 0.2370 -0.0245 -0.0023 0.1161  120 GLU   A O   
2567 O O   B GLU   A 120 ? 0.2491 0.2682 0.2370 -0.0184 0.0002  0.0528  120 GLU   A O   
2568 C CB  A GLU   A 120 ? 0.2671 0.2857 0.3001 0.0154  -0.0090 0.1644  120 GLU   A CB  
2569 C CB  B GLU   A 120 ? 0.3014 0.3113 0.3528 -0.0084 0.0082  0.0520  120 GLU   A CB  
2570 C CG  A GLU   A 120 ? 0.3499 0.3402 0.4028 0.0302  -0.0111 0.1669  120 GLU   A CG  
2571 C CG  B GLU   A 120 ? 0.3495 0.3545 0.4292 -0.0030 0.0083  0.0472  120 GLU   A CG  
2572 C CD  A GLU   A 120 ? 0.4222 0.3862 0.5100 0.0456  -0.0011 0.1493  120 GLU   A CD  
2573 C CD  B GLU   A 120 ? 0.3875 0.3881 0.4958 0.0024  0.0102  0.0411  120 GLU   A CD  
2574 O OE1 A GLU   A 120 ? 0.4460 0.4007 0.5321 0.0468  0.0048  0.1439  120 GLU   A OE1 
2575 O OE1 B GLU   A 120 ? 0.3963 0.3958 0.5150 0.0031  0.0112  0.0392  120 GLU   A OE1 
2576 O OE2 A GLU   A 120 ? 0.4495 0.4040 0.5562 0.0511  -0.0003 0.1383  120 GLU   A OE2 
2577 O OE2 B GLU   A 120 ? 0.3993 0.3985 0.5221 0.0044  0.0103  0.0387  120 GLU   A OE2 
2590 N N   A VAL   A 121 ? 0.1849 0.2292 0.1803 -0.0091 0.0129  0.1004  121 VAL   A N   
2591 N N   B VAL   A 121 ? 0.2315 0.2554 0.2260 -0.0179 0.0041  0.0530  121 VAL   A N   
2592 C CA  A VAL   A 121 ? 0.1862 0.2439 0.1767 -0.0189 0.0248  0.0970  121 VAL   A CA  
2593 C CA  B VAL   A 121 ? 0.2162 0.2470 0.2140 -0.0199 0.0043  0.0532  121 VAL   A CA  
2594 C C   A VAL   A 121 ? 0.1718 0.2206 0.1674 -0.0309 0.0047  0.0739  121 VAL   A C   
2595 C C   B VAL   A 121 ? 0.1901 0.2237 0.1909 -0.0252 0.0024  0.0558  121 VAL   A C   
2596 O O   A VAL   A 121 ? 0.1733 0.2172 0.1792 -0.0410 -0.0116 0.0653  121 VAL   A O   
2597 O O   B VAL   A 121 ? 0.1910 0.2246 0.1944 -0.0257 -0.0006 0.0545  121 VAL   A O   
2598 C CB  A VAL   A 121 ? 0.2205 0.2844 0.2161 -0.0051 0.0345  0.1091  121 VAL   A CB  
2599 C CB  B VAL   A 121 ? 0.2294 0.2603 0.2322 -0.0147 0.0043  0.0510  121 VAL   A CB  
2600 C CG1 A VAL   A 121 ? 0.2218 0.3023 0.2191 0.0007  0.0478  0.1100  121 VAL   A CG1 
2601 C CG1 B VAL   A 121 ? 0.2312 0.2653 0.2370 -0.0123 0.0060  0.0510  121 VAL   A CG1 
2602 C CG2 A VAL   A 121 ? 0.2383 0.3003 0.2594 -0.0124 0.0283  0.0991  121 VAL   A CG2 
2603 C CG2 B VAL   A 121 ? 0.2357 0.2655 0.2446 -0.0161 0.0034  0.0471  121 VAL   A CG2 
2622 N N   . LEU   A 122 ? 0.1642 0.2003 0.1678 -0.0308 0.0042  0.0606  122 LEU   A N   
2623 C CA  . LEU   A 122 ? 0.1712 0.1747 0.1615 -0.0264 0.0148  0.0551  122 LEU   A CA  
2624 C C   . LEU   A 122 ? 0.1669 0.1721 0.1676 -0.0312 0.0042  0.0542  122 LEU   A C   
2625 O O   . LEU   A 122 ? 0.1747 0.1803 0.1884 -0.0395 0.0044  0.0478  122 LEU   A O   
2626 C CB  . LEU   A 122 ? 0.1871 0.1795 0.1980 -0.0164 0.0057  0.0559  122 LEU   A CB  
2627 C CG  . LEU   A 122 ? 0.1711 0.1791 0.2066 -0.0199 0.0223  0.0417  122 LEU   A CG  
2628 C CD1 . LEU   A 122 ? 0.1897 0.1903 0.2061 -0.0221 0.0340  0.0332  122 LEU   A CD1 
2629 C CD2 . LEU   A 122 ? 0.1581 0.1707 0.1952 -0.0166 0.0344  0.0379  122 LEU   A CD2 
2642 N N   A LEU   A 123 ? 0.1563 0.1685 0.1705 -0.0368 0.0004  0.0442  123 LEU   A N   
2643 N N   B LEU   A 123 ? 0.1644 0.1665 0.1614 -0.0248 0.0021  0.0370  123 LEU   A N   
2644 C CA  A LEU   A 123 ? 0.1568 0.1730 0.1549 -0.0283 0.0058  0.0403  123 LEU   A CA  
2645 C CA  B LEU   A 123 ? 0.1625 0.1604 0.1564 -0.0161 0.0017  0.0197  123 LEU   A CA  
2646 C C   A LEU   A 123 ? 0.1586 0.1647 0.1433 -0.0153 0.0106  0.0491  123 LEU   A C   
2647 C C   B LEU   A 123 ? 0.1601 0.1464 0.1421 -0.0160 0.0151  0.0040  123 LEU   A C   
2648 O O   A LEU   A 123 ? 0.1413 0.1619 0.1616 -0.0264 0.0078  0.0405  123 LEU   A O   
2649 O O   B LEU   A 123 ? 0.1555 0.1413 0.1388 -0.0138 0.0223  -0.0083 123 LEU   A O   
2650 C CB  A LEU   A 123 ? 0.1758 0.1839 0.1490 -0.0251 0.0255  0.0319  123 LEU   A CB  
2651 C CB  B LEU   A 123 ? 0.1684 0.1674 0.1687 -0.0067 -0.0101 0.0234  123 LEU   A CB  
2652 C CG  A LEU   A 123 ? 0.1826 0.2004 0.1607 -0.0219 0.0338  0.0153  123 LEU   A CG  
2653 C CG  B LEU   A 123 ? 0.1714 0.1770 0.1768 -0.0032 -0.0157 0.0263  123 LEU   A CG  
2654 C CD1 A LEU   A 123 ? 0.1861 0.2073 0.1861 -0.0238 0.0314  0.0084  123 LEU   A CD1 
2655 C CD1 B LEU   A 123 ? 0.1721 0.1804 0.1802 -0.0034 -0.0166 0.0240  123 LEU   A CD1 
2656 C CD2 A LEU   A 123 ? 0.1975 0.2037 0.1669 -0.0273 0.0217  0.0144  123 LEU   A CD2 
2657 C CD2 B LEU   A 123 ? 0.1757 0.1826 0.1924 -0.0015 -0.0227 0.0247  123 LEU   A CD2 
2680 N N   A ALA   A 124 ? 0.1506 0.1482 0.1431 -0.0093 0.0007  0.0354  124 ALA   A N   
2681 N N   B ALA   A 124 ? 0.1551 0.1339 0.1410 -0.0210 0.0170  -0.0082 124 ALA   A N   
2682 C CA  A ALA   A 124 ? 0.1362 0.1436 0.1442 -0.0043 -0.0040 0.0323  124 ALA   A CA  
2683 C CA  B ALA   A 124 ? 0.1523 0.1394 0.1425 -0.0229 0.0050  0.0050  124 ALA   A CA  
2684 C C   A ALA   A 124 ? 0.1369 0.1509 0.1527 -0.0111 0.0187  0.0391  124 ALA   A C   
2685 C C   B ALA   A 124 ? 0.1519 0.1476 0.1216 -0.0169 0.0015  0.0204  124 ALA   A C   
2686 O O   A ALA   A 124 ? 0.1372 0.1536 0.1740 -0.0183 0.0181  0.0386  124 ALA   A O   
2687 O O   B ALA   A 124 ? 0.1574 0.1549 0.1125 -0.0048 0.0017  0.0204  124 ALA   A O   
2688 C CB  A ALA   A 124 ? 0.1327 0.1358 0.1650 -0.0019 -0.0026 0.0196  124 ALA   A CB  
2689 C CB  B ALA   A 124 ? 0.1559 0.1385 0.1663 -0.0296 0.0069  0.0059  124 ALA   A CB  
2700 N N   A PRO   A 125 ? 0.1396 0.1430 0.1560 -0.0061 0.0055  0.0322  125 PRO   A N   
2701 N N   B PRO   A 125 ? 0.1397 0.1416 0.1031 -0.0120 -0.0056 0.0377  125 PRO   A N   
2702 C CA  A PRO   A 125 ? 0.1510 0.1524 0.1562 -0.0046 0.0042  0.0226  125 PRO   A CA  
2703 C CA  B PRO   A 125 ? 0.1400 0.1466 0.1079 -0.0168 -0.0085 0.0373  125 PRO   A CA  
2704 C C   A PRO   A 125 ? 0.1465 0.1506 0.1538 0.0007  0.0163  0.0226  125 PRO   A C   
2705 C C   B PRO   A 125 ? 0.1457 0.1504 0.1303 -0.0246 -0.0078 0.0254  125 PRO   A C   
2706 O O   A PRO   A 125 ? 0.1487 0.1425 0.1722 0.0044  0.0099  0.0169  125 PRO   A O   
2707 O O   B PRO   A 125 ? 0.1406 0.1447 0.1403 -0.0371 -0.0083 0.0293  125 PRO   A O   
2708 C CB  A PRO   A 125 ? 0.1519 0.1486 0.1625 -0.0166 0.0038  0.0144  125 PRO   A CB  
2709 C CB  B PRO   A 125 ? 0.1351 0.1439 0.1026 -0.0151 -0.0097 0.0438  125 PRO   A CB  
2710 C CG  A PRO   A 125 ? 0.1566 0.1541 0.1563 -0.0154 0.0029  0.0290  125 PRO   A CG  
2711 C CG  B PRO   A 125 ? 0.1312 0.1441 0.1071 -0.0113 -0.0057 0.0373  125 PRO   A CG  
2712 C CD  A PRO   A 125 ? 0.1421 0.1514 0.1585 -0.0210 0.0141  0.0307  125 PRO   A CD  
2713 C CD  B PRO   A 125 ? 0.1259 0.1395 0.1030 -0.0120 0.0006  0.0368  125 PRO   A CD  
2728 N N   A LEU   A 126 ? 0.1419 0.1566 0.1581 0.0007  0.0103  0.0281  126 LEU   A N   
2729 N N   B LEU   A 126 ? 0.1558 0.1567 0.1426 -0.0176 -0.0125 0.0178  126 LEU   A N   
2730 C CA  A LEU   A 126 ? 0.1390 0.1517 0.1677 -0.0035 0.0065  0.0262  126 LEU   A CA  
2731 C CA  B LEU   A 126 ? 0.1595 0.1603 0.1526 -0.0132 -0.0136 0.0146  126 LEU   A CA  
2732 C C   A LEU   A 126 ? 0.1434 0.1422 0.1680 0.0039  0.0017  0.0181  126 LEU   A C   
2733 C C   B LEU   A 126 ? 0.1539 0.1567 0.1542 -0.0075 -0.0169 0.0058  126 LEU   A C   
2734 O O   A LEU   A 126 ? 0.1521 0.1431 0.1979 0.0117  0.0238  0.0300  126 LEU   A O   
2735 O O   B LEU   A 126 ? 0.1598 0.1628 0.1685 -0.0108 -0.0265 0.0017  126 LEU   A O   
2736 C CB  A LEU   A 126 ? 0.1527 0.1677 0.1614 -0.0083 0.0125  0.0092  126 LEU   A CB  
2737 C CB  B LEU   A 126 ? 0.1688 0.1782 0.1811 -0.0125 -0.0212 0.0116  126 LEU   A CB  
2738 C CG  A LEU   A 126 ? 0.1451 0.1857 0.1721 -0.0127 0.0156  0.0124  126 LEU   A CG  
2739 C CG  B LEU   A 126 ? 0.1782 0.1920 0.2018 -0.0093 -0.0341 0.0129  126 LEU   A CG  
2740 C CD1 A LEU   A 126 ? 0.1519 0.1932 0.2261 -0.0209 0.0183  0.0041  126 LEU   A CD1 
2741 C CD1 B LEU   A 126 ? 0.1804 0.1972 0.2048 -0.0108 -0.0384 0.0174  126 LEU   A CD1 
2742 C CD2 A LEU   A 126 ? 0.1572 0.1835 0.1741 -0.0232 0.0020  0.0369  126 LEU   A CD2 
2743 C CD2 B LEU   A 126 ? 0.1844 0.1979 0.2153 -0.0077 -0.0398 0.0140  126 LEU   A CD2 
2766 N N   A LEU   A 127 ? 0.1385 0.1450 0.1481 0.0065  0.0115  0.0248  127 LEU   A N   
2767 N N   B LEU   A 127 ? 0.1488 0.1482 0.1419 0.0046  -0.0101 0.0157  127 LEU   A N   
2768 C CA  A LEU   A 127 ? 0.1341 0.1562 0.1480 -0.0025 0.0054  0.0232  127 LEU   A CA  
2769 C CA  B LEU   A 127 ? 0.1494 0.1530 0.1375 0.0072  -0.0088 0.0155  127 LEU   A CA  
2770 C C   A LEU   A 127 ? 0.1243 0.1401 0.1484 -0.0013 0.0015  0.0124  127 LEU   A C   
2771 C C   B LEU   A 127 ? 0.1502 0.1576 0.1323 -0.0016 -0.0081 -0.0002 127 LEU   A C   
2772 O O   A LEU   A 127 ? 0.1305 0.1303 0.1533 -0.0097 0.0068  0.0158  127 LEU   A O   
2773 O O   B LEU   A 127 ? 0.1551 0.1618 0.1390 -0.0099 0.0026  -0.0079 127 LEU   A O   
2774 C CB  A LEU   A 127 ? 0.1443 0.1773 0.1751 0.0147  0.0076  0.0196  127 LEU   A CB  
2775 C CB  B LEU   A 127 ? 0.1512 0.1540 0.1397 0.0142  -0.0106 0.0264  127 LEU   A CB  
2776 C CG  A LEU   A 127 ? 0.1535 0.1807 0.1831 0.0151  0.0054  0.0350  127 LEU   A CG  
2777 C CG  B LEU   A 127 ? 0.1469 0.1519 0.1263 0.0223  -0.0114 0.0417  127 LEU   A CG  
2778 C CD1 A LEU   A 127 ? 0.1713 0.1825 0.2085 0.0154  0.0099  0.0428  127 LEU   A CD1 
2779 C CD1 B LEU   A 127 ? 0.1491 0.1486 0.1397 0.0272  -0.0017 0.0450  127 LEU   A CD1 
2780 C CD2 A LEU   A 127 ? 0.1677 0.1865 0.2014 0.0241  -0.0017 0.0375  127 LEU   A CD2 
2781 C CD2 B LEU   A 127 ? 0.1503 0.1532 0.1113 0.0251  -0.0212 0.0410  127 LEU   A CD2 
2804 N N   A SER   A 128 ? 0.1352 0.1394 0.1533 -0.0072 0.0025  0.0175  128 SER   A N   
2805 N N   B SER   A 128 ? 0.1537 0.1583 0.1394 -0.0028 -0.0135 -0.0022 128 SER   A N   
2806 C CA  A SER   A 128 ? 0.1472 0.1455 0.1464 -0.0061 -0.0030 0.0170  128 SER   A CA  
2807 C CA  B SER   A 128 ? 0.1579 0.1626 0.1390 -0.0033 -0.0196 0.0015  128 SER   A CA  
2808 C C   A SER   A 128 ? 0.1530 0.1505 0.1247 -0.0024 -0.0107 0.0177  128 SER   A C   
2809 C C   B SER   A 128 ? 0.1599 0.1665 0.1329 -0.0028 -0.0213 0.0089  128 SER   A C   
2810 O O   A SER   A 128 ? 0.1686 0.1589 0.1540 -0.0003 -0.0097 0.0097  128 SER   A O   
2811 O O   B SER   A 128 ? 0.1695 0.1716 0.1470 0.0013  -0.0141 0.0078  128 SER   A O   
2812 C CB  A SER   A 128 ? 0.1438 0.1622 0.1481 -0.0079 0.0042  0.0200  128 SER   A CB  
2813 C CB  B SER   A 128 ? 0.1613 0.1669 0.1338 -0.0030 -0.0202 -0.0010 128 SER   A CB  
2814 O OG  A SER   A 128 ? 0.1444 0.1752 0.1678 -0.0057 0.0169  0.0106  128 SER   A OG  
2815 O OG  B SER   A 128 ? 0.1661 0.1692 0.1303 -0.0031 -0.0151 -0.0030 128 SER   A OG  
2826 N N   A ALA   A 129 ? 0.1535 0.1523 0.1659 0.0027  -0.0151 0.0388  129 ALA   A N   
2827 N N   B ALA   A 129 ? 0.1598 0.1680 0.1374 -0.0067 -0.0196 0.0185  129 ALA   A N   
2828 C CA  A ALA   A 129 ? 0.1529 0.1569 0.1940 0.0057  -0.0047 0.0393  129 ALA   A CA  
2829 C CA  B ALA   A 129 ? 0.1608 0.1735 0.1404 -0.0103 -0.0087 0.0288  129 ALA   A CA  
2830 C C   A ALA   A 129 ? 0.1611 0.1545 0.1718 0.0046  -0.0133 0.0145  129 ALA   A C   
2831 C C   B ALA   A 129 ? 0.1748 0.1750 0.1464 -0.0040 0.0061  0.0249  129 ALA   A C   
2832 O O   A ALA   A 129 ? 0.1673 0.1574 0.1832 0.0027  -0.0124 0.0199  129 ALA   A O   
2833 O O   B ALA   A 129 ? 0.1813 0.1725 0.1389 -0.0064 0.0101  0.0307  129 ALA   A O   
2834 C CB  A ALA   A 129 ? 0.1567 0.1706 0.2198 0.0108  -0.0064 0.0474  129 ALA   A CB  
2835 C CB  B ALA   A 129 ? 0.1568 0.1800 0.1384 -0.0166 -0.0069 0.0370  129 ALA   A CB  
2846 N N   A GLY   A 130 ? 0.1748 0.1599 0.1706 0.0074  -0.0225 0.0121  130 GLY   A N   
2847 N N   B GLY   A 130 ? 0.1845 0.1829 0.1523 0.0002  0.0019  0.0312  130 GLY   A N   
2848 C CA  A GLY   A 130 ? 0.1889 0.1586 0.1683 0.0127  -0.0158 0.0211  130 GLY   A CA  
2849 C CA  B GLY   A 130 ? 0.1936 0.1856 0.1610 -0.0010 -0.0024 0.0300  130 GLY   A CA  
2850 C C   A GLY   A 130 ? 0.1882 0.1488 0.1582 0.0091  -0.0232 0.0108  130 GLY   A C   
2851 C C   B GLY   A 130 ? 0.2008 0.1858 0.1685 -0.0045 -0.0113 0.0305  130 GLY   A C   
2852 O O   A GLY   A 130 ? 0.1860 0.1584 0.1708 0.0079  -0.0293 0.0177  130 GLY   A O   
2853 O O   B GLY   A 130 ? 0.2039 0.1859 0.1677 -0.0095 -0.0214 0.0379  130 GLY   A O   
2860 N N   A ILE   A 131 ? 0.2058 0.1471 0.1690 -0.0056 -0.0224 0.0191  131 ILE   A N   
2861 N N   B ILE   A 131 ? 0.2051 0.1846 0.1689 -0.0070 -0.0091 0.0330  131 ILE   A N   
2862 C CA  A ILE   A 131 ? 0.2182 0.1593 0.1528 -0.0175 -0.0356 0.0134  131 ILE   A CA  
2863 C CA  B ILE   A 131 ? 0.2084 0.1910 0.1813 -0.0142 -0.0094 0.0266  131 ILE   A CA  
2864 C C   A ILE   A 131 ? 0.1996 0.1551 0.1504 -0.0150 -0.0281 0.0243  131 ILE   A C   
2865 C C   B ILE   A 131 ? 0.2032 0.1933 0.1750 -0.0159 -0.0119 0.0357  131 ILE   A C   
2866 O O   A ILE   A 131 ? 0.2088 0.1642 0.1710 -0.0078 -0.0319 0.0307  131 ILE   A O   
2867 O O   B ILE   A 131 ? 0.2024 0.1922 0.1669 -0.0158 -0.0210 0.0442  131 ILE   A O   
2868 C CB  A ILE   A 131 ? 0.2573 0.1873 0.1729 -0.0325 -0.0513 0.0077  131 ILE   A CB  
2869 C CB  B ILE   A 131 ? 0.2177 0.1959 0.1965 -0.0126 -0.0080 0.0157  131 ILE   A CB  
2870 C CG1 A ILE   A 131 ? 0.2733 0.2207 0.1867 -0.0492 -0.0557 -0.0024 131 ILE   A CG1 
2871 C CG1 B ILE   A 131 ? 0.2283 0.2069 0.2162 -0.0142 -0.0038 0.0107  131 ILE   A CG1 
2872 C CG2 A ILE   A 131 ? 0.2844 0.1787 0.2048 -0.0231 -0.0288 0.0041  131 ILE   A CG2 
2873 C CG2 B ILE   A 131 ? 0.2171 0.1893 0.1881 -0.0064 -0.0107 0.0150  131 ILE   A CG2 
2874 C CD1 A ILE   A 131 ? 0.2893 0.2313 0.2146 -0.0569 -0.0419 -0.0204 131 ILE   A CD1 
2875 C CD1 B ILE   A 131 ? 0.2355 0.2120 0.2230 -0.0165 -0.0037 0.0093  131 ILE   A CD1 
2898 N N   A PHE   A 132 ? 0.1803 0.1559 0.1536 -0.0170 -0.0219 0.0270  132 PHE   A N   
2899 N N   B PHE   A 132 ? 0.2014 0.1981 0.1813 -0.0165 -0.0014 0.0320  132 PHE   A N   
2900 C CA  A PHE   A 132 ? 0.1788 0.1669 0.1528 -0.0272 -0.0151 0.0156  132 PHE   A CA  
2901 C CA  B PHE   A 132 ? 0.1969 0.2011 0.1781 -0.0152 0.0033  0.0249  132 PHE   A CA  
2902 C C   A PHE   A 132 ? 0.1893 0.1763 0.1615 -0.0213 -0.0212 0.0228  132 PHE   A C   
2903 C C   B PHE   A 132 ? 0.2034 0.2016 0.1820 -0.0147 0.0002  0.0363  132 PHE   A C   
2904 O O   A PHE   A 132 ? 0.1933 0.1792 0.1637 -0.0208 -0.0138 0.0292  132 PHE   A O   
2905 O O   B PHE   A 132 ? 0.2099 0.2053 0.1864 -0.0176 0.0013  0.0486  132 PHE   A O   
2906 C CB  A PHE   A 132 ? 0.1714 0.1585 0.1376 -0.0234 -0.0266 0.0237  132 PHE   A CB  
2907 C CB  B PHE   A 132 ? 0.1867 0.2020 0.1698 -0.0097 0.0095  0.0095  132 PHE   A CB  
2908 C CG  A PHE   A 132 ? 0.1699 0.1563 0.1237 -0.0069 -0.0202 0.0170  132 PHE   A CG  
2909 C CG  B PHE   A 132 ? 0.1763 0.2032 0.1681 -0.0023 0.0199  -0.0001 132 PHE   A CG  
2910 C CD1 A PHE   A 132 ? 0.1714 0.1692 0.1610 0.0003  -0.0188 -0.0086 132 PHE   A CD1 
2911 C CD1 B PHE   A 132 ? 0.1728 0.2059 0.1680 -0.0020 0.0207  -0.0088 132 PHE   A CD1 
2912 C CD2 A PHE   A 132 ? 0.1672 0.1613 0.1482 0.0095  -0.0325 0.0047  132 PHE   A CD2 
2913 C CD2 B PHE   A 132 ? 0.1686 0.2008 0.1705 -0.0007 0.0326  -0.0067 132 PHE   A CD2 
2914 C CE1 A PHE   A 132 ? 0.1699 0.1728 0.1741 0.0024  -0.0246 -0.0019 132 PHE   A CE1 
2915 C CE1 B PHE   A 132 ? 0.1709 0.2078 0.1705 -0.0008 0.0238  -0.0139 132 PHE   A CE1 
2916 C CE2 A PHE   A 132 ? 0.1645 0.1704 0.1799 0.0168  -0.0344 0.0032  132 PHE   A CE2 
2917 C CE2 B PHE   A 132 ? 0.1672 0.2013 0.1756 0.0030  0.0346  -0.0140 132 PHE   A CE2 
2918 C CZ  A PHE   A 132 ? 0.1674 0.1634 0.1866 0.0040  -0.0333 0.0094  132 PHE   A CZ  
2919 C CZ  B PHE   A 132 ? 0.1689 0.2030 0.1690 -0.0013 0.0272  -0.0169 132 PHE   A CZ  
2938 N N   A GLY   A 133 ? 0.1851 0.1940 0.1488 -0.0207 -0.0252 0.0285  133 GLY   A N   
2939 N N   B GLY   A 133 ? 0.1994 0.2002 0.1750 -0.0107 -0.0037 0.0317  133 GLY   A N   
2940 C CA  A GLY   A 133 ? 0.1913 0.2043 0.1495 -0.0227 -0.0280 0.0217  133 GLY   A CA  
2941 C CA  B GLY   A 133 ? 0.1959 0.1980 0.1731 -0.0075 -0.0037 0.0180  133 GLY   A CA  
2942 C C   A GLY   A 133 ? 0.1964 0.2167 0.1551 -0.0302 -0.0423 0.0080  133 GLY   A C   
2943 C C   B GLY   A 133 ? 0.1927 0.2013 0.1814 -0.0027 -0.0050 0.0031  133 GLY   A C   
2944 O O   A GLY   A 133 ? 0.2226 0.2234 0.1825 -0.0289 -0.0493 -0.0105 133 GLY   A O   
2945 O O   B GLY   A 133 ? 0.1937 0.2011 0.1813 0.0015  -0.0094 -0.0028 133 GLY   A O   
2952 N N   A ALA   A 134 ? 0.1927 0.2061 0.1484 -0.0309 -0.0219 0.0053  134 ALA   A N   
2953 N N   B ALA   A 134 ? 0.1907 0.2023 0.1878 0.0015  0.0009  -0.0028 134 ALA   A N   
2954 C CA  A ALA   A 134 ? 0.1853 0.2041 0.1588 -0.0214 -0.0202 0.0063  134 ALA   A CA  
2955 C CA  B ALA   A 134 ? 0.1882 0.2044 0.1965 0.0035  -0.0087 -0.0025 134 ALA   A CA  
2956 C C   A ALA   A 134 ? 0.1866 0.2132 0.1735 -0.0235 -0.0204 0.0045  134 ALA   A C   
2957 C C   B ALA   A 134 ? 0.1840 0.2054 0.1946 0.0009  -0.0141 0.0061  134 ALA   A C   
2958 O O   A ALA   A 134 ? 0.2041 0.2138 0.2012 -0.0132 0.0010  0.0096  134 ALA   A O   
2959 O O   B ALA   A 134 ? 0.1902 0.2045 0.1898 0.0003  -0.0206 0.0107  134 ALA   A O   
2960 C CB  A ALA   A 134 ? 0.1986 0.1890 0.1985 -0.0127 -0.0208 -0.0022 134 ALA   A CB  
2961 C CB  B ALA   A 134 ? 0.1925 0.2023 0.2101 0.0077  -0.0104 -0.0114 134 ALA   A CB  
2972 N N   A ASP   A 135 ? 0.1929 0.2201 0.1795 -0.0330 -0.0205 0.0215  135 ASP   A N   
2973 N N   B ASP   A 135 ? 0.1791 0.2070 0.2012 0.0029  -0.0101 0.0149  135 ASP   A N   
2974 C CA  A ASP   A 135 ? 0.1939 0.2343 0.1856 -0.0394 -0.0384 0.0267  135 ASP   A CA  
2975 C CA  B ASP   A 135 ? 0.1771 0.2115 0.2113 0.0022  -0.0121 0.0226  135 ASP   A CA  
2976 C C   A ASP   A 135 ? 0.1794 0.2110 0.1830 -0.0213 -0.0254 0.0306  135 ASP   A C   
2977 C C   B ASP   A 135 ? 0.1712 0.2018 0.1917 -0.0032 -0.0144 0.0280  135 ASP   A C   
2978 O O   A ASP   A 135 ? 0.1767 0.2005 0.1935 -0.0192 -0.0146 0.0333  135 ASP   A O   
2979 O O   B ASP   A 135 ? 0.1695 0.1958 0.1937 -0.0040 -0.0124 0.0375  135 ASP   A O   
2980 C CB  A ASP   A 135 ? 0.2167 0.2771 0.2229 -0.0639 -0.0592 0.0171  135 ASP   A CB  
2981 C CB  B ASP   A 135 ? 0.1830 0.2258 0.2501 0.0039  -0.0111 0.0260  135 ASP   A CB  
2982 C CG  A ASP   A 135 ? 0.2328 0.3099 0.2789 -0.0847 -0.0711 0.0123  135 ASP   A CG  
2983 C CG  B ASP   A 135 ? 0.1852 0.2343 0.2844 0.0071  -0.0129 0.0296  135 ASP   A CG  
2984 O OD1 A ASP   A 135 ? 0.2293 0.3239 0.2681 -0.0880 -0.0660 0.0502  135 ASP   A OD1 
2985 O OD1 B ASP   A 135 ? 0.1916 0.2369 0.2926 0.0123  -0.0015 0.0299  135 ASP   A OD1 
2986 O OD2 A ASP   A 135 ? 0.2640 0.3302 0.3508 -0.0888 -0.0584 0.0009  135 ASP   A OD2 
2987 O OD2 B ASP   A 135 ? 0.1802 0.2389 0.2985 0.0114  -0.0226 0.0377  135 ASP   A OD2 
2996 N N   A PRO   A 136 ? 0.1727 0.2019 0.2018 -0.0058 -0.0053 0.0339  136 PRO   A N   
2997 N N   B PRO   A 136 ? 0.1684 0.1992 0.1778 -0.0062 -0.0182 0.0262  136 PRO   A N   
2998 C CA  A PRO   A 136 ? 0.1656 0.1959 0.2037 -0.0152 0.0029  0.0154  136 PRO   A CA  
2999 C CA  B PRO   A 136 ? 0.1652 0.1949 0.1765 -0.0101 -0.0200 0.0228  136 PRO   A CA  
3000 C C   A PRO   A 136 ? 0.1524 0.1905 0.1960 -0.0131 -0.0003 0.0158  136 PRO   A C   
3001 C C   B PRO   A 136 ? 0.1632 0.1898 0.1708 -0.0104 -0.0169 0.0159  136 PRO   A C   
3002 O O   A PRO   A 136 ? 0.1523 0.1844 0.1767 -0.0045 0.0079  0.0217  136 PRO   A O   
3003 O O   B PRO   A 136 ? 0.1604 0.1904 0.1688 -0.0140 -0.0170 0.0176  136 PRO   A O   
3004 C CB  A PRO   A 136 ? 0.1810 0.1927 0.2291 -0.0060 -0.0100 0.0167  136 PRO   A CB  
3005 C CB  B PRO   A 136 ? 0.1683 0.1955 0.1790 -0.0078 -0.0206 0.0267  136 PRO   A CB  
3006 C CG  A PRO   A 136 ? 0.1938 0.2036 0.2584 0.0040  -0.0101 0.0217  136 PRO   A CG  
3007 C CG  B PRO   A 136 ? 0.1713 0.1974 0.1736 -0.0065 -0.0215 0.0206  136 PRO   A CG  
3008 C CD  A PRO   A 136 ? 0.1844 0.2009 0.2371 0.0049  0.0014  0.0343  136 PRO   A CD  
3009 C CD  B PRO   A 136 ? 0.1700 0.1992 0.1719 -0.0053 -0.0221 0.0227  136 PRO   A CD  
3024 N N   A ILE   A 137 ? 0.1521 0.1941 0.2030 -0.0142 -0.0134 0.0158  137 ILE   A N   
3025 N N   B ILE   A 137 ? 0.1665 0.1875 0.1721 -0.0079 -0.0133 0.0136  137 ILE   A N   
3026 C CA  A ILE   A 137 ? 0.1518 0.2060 0.1981 -0.0138 -0.0185 0.0174  137 ILE   A CA  
3027 C CA  B ILE   A 137 ? 0.1706 0.1883 0.1825 -0.0054 -0.0119 0.0031  137 ILE   A CA  
3028 C C   A ILE   A 137 ? 0.1465 0.2051 0.1949 -0.0173 -0.0084 0.0224  137 ILE   A C   
3029 C C   B ILE   A 137 ? 0.1712 0.1871 0.1916 -0.0023 -0.0118 0.0033  137 ILE   A C   
3030 O O   A ILE   A 137 ? 0.1530 0.1985 0.1959 -0.0270 -0.0046 0.0152  137 ILE   A O   
3031 O O   B ILE   A 137 ? 0.1737 0.1829 0.2007 0.0020  -0.0110 -0.0050 137 ILE   A O   
3032 C CB  A ILE   A 137 ? 0.1735 0.2229 0.2331 -0.0149 -0.0296 0.0127  137 ILE   A CB  
3033 C CB  B ILE   A 137 ? 0.1763 0.1938 0.1818 -0.0072 -0.0112 -0.0109 137 ILE   A CB  
3034 C CG1 A ILE   A 137 ? 0.1944 0.2479 0.2617 -0.0019 -0.0503 0.0198  137 ILE   A CG1 
3035 C CG1 B ILE   A 137 ? 0.1790 0.2002 0.1892 -0.0069 -0.0202 -0.0307 137 ILE   A CG1 
3036 C CG2 A ILE   A 137 ? 0.1794 0.2253 0.2459 -0.0275 -0.0294 0.0014  137 ILE   A CG2 
3037 C CG2 B ILE   A 137 ? 0.1786 0.1928 0.1655 -0.0084 0.0000  -0.0129 137 ILE   A CG2 
3038 C CD1 A ILE   A 137 ? 0.2156 0.2616 0.2910 0.0038  -0.0490 0.0214  137 ILE   A CD1 
3039 C CD1 B ILE   A 137 ? 0.1842 0.2041 0.1986 -0.0071 -0.0190 -0.0454 137 ILE   A CD1 
3062 N N   A HIS   A 138 ? 0.1520 0.2174 0.1984 -0.0187 0.0035  0.0185  138 HIS   A N   
3063 N N   B HIS   A 138 ? 0.1726 0.1912 0.1965 -0.0039 -0.0087 0.0052  138 HIS   A N   
3064 C CA  A HIS   A 138 ? 0.1529 0.2261 0.1927 -0.0152 0.0114  0.0057  138 HIS   A CA  
3065 C CA  B HIS   A 138 ? 0.1715 0.1967 0.2000 -0.0072 -0.0068 0.0084  138 HIS   A CA  
3066 C C   A HIS   A 138 ? 0.1474 0.2084 0.1912 -0.0147 0.0043  0.0170  138 HIS   A C   
3067 C C   B HIS   A 138 ? 0.1594 0.1926 0.1930 -0.0085 -0.0017 0.0133  138 HIS   A C   
3068 O O   A HIS   A 138 ? 0.1595 0.2112 0.2077 -0.0140 0.0090  0.0225  138 HIS   A O   
3069 O O   B HIS   A 138 ? 0.1575 0.1899 0.1926 -0.0078 0.0102  0.0166  138 HIS   A O   
3070 C CB  A HIS   A 138 ? 0.1749 0.2428 0.1881 -0.0040 0.0084  -0.0048 138 HIS   A CB  
3071 C CB  B HIS   A 138 ? 0.1890 0.2060 0.2120 -0.0115 -0.0161 0.0067  138 HIS   A CB  
3072 C CG  A HIS   A 138 ? 0.1939 0.2455 0.2087 -0.0108 0.0077  -0.0199 138 HIS   A CG  
3073 C CG  B HIS   A 138 ? 0.2009 0.2097 0.2212 -0.0169 -0.0126 0.0049  138 HIS   A CG  
3074 N ND1 A HIS   A 138 ? 0.2131 0.2494 0.2412 -0.0107 0.0190  -0.0355 138 HIS   A ND1 
3075 N ND1 B HIS   A 138 ? 0.2075 0.2136 0.2327 -0.0178 -0.0063 0.0004  138 HIS   A ND1 
3076 C CD2 A HIS   A 138 ? 0.1894 0.2497 0.2076 -0.0069 0.0060  -0.0175 138 HIS   A CD2 
3077 C CD2 B HIS   A 138 ? 0.2041 0.2122 0.2216 -0.0169 -0.0142 0.0059  138 HIS   A CD2 
3078 C CE1 A HIS   A 138 ? 0.2183 0.2503 0.2537 -0.0016 0.0065  -0.0380 138 HIS   A CE1 
3079 C CE1 B HIS   A 138 ? 0.2111 0.2160 0.2387 -0.0142 -0.0092 0.0005  138 HIS   A CE1 
3080 N NE2 A HIS   A 138 ? 0.2029 0.2570 0.2223 -0.0029 0.0068  -0.0340 138 HIS   A NE2 
3081 N NE2 B HIS   A 138 ? 0.2080 0.2160 0.2283 -0.0141 -0.0122 0.0029  138 HIS   A NE2 
3096 N N   . SER   A 139 ? 0.1544 0.1866 0.1881 -0.0096 0.0005  0.0192  139 SER   A N   
3097 C CA  . SER   A 139 ? 0.1570 0.1826 0.1824 -0.0126 0.0063  0.0364  139 SER   A CA  
3098 C C   . SER   A 139 ? 0.1487 0.1753 0.1954 -0.0102 0.0105  0.0234  139 SER   A C   
3099 O O   . SER   A 139 ? 0.1452 0.1640 0.2128 -0.0153 -0.0013 0.0297  139 SER   A O   
3100 C CB  . SER   A 139 ? 0.1544 0.1812 0.1738 -0.0208 0.0015  0.0377  139 SER   A CB  
3101 O OG  . SER   A 139 ? 0.1561 0.1801 0.2016 -0.0275 -0.0131 0.0393  139 SER   A OG  
3108 N N   . LEU   A 140 ? 0.1423 0.1810 0.1740 -0.0036 0.0085  0.0368  140 LEU   A N   
3109 C CA  . LEU   A 140 ? 0.1372 0.1727 0.1878 -0.0057 0.0039  0.0262  140 LEU   A CA  
3110 C C   . LEU   A 140 ? 0.1328 0.1738 0.2062 -0.0102 0.0023  0.0315  140 LEU   A C   
3111 O O   . LEU   A 140 ? 0.1372 0.1764 0.2393 -0.0089 0.0036  0.0379  140 LEU   A O   
3112 C CB  . LEU   A 140 ? 0.1326 0.1789 0.2151 -0.0087 0.0092  0.0308  140 LEU   A CB  
3113 C CG  . LEU   A 140 ? 0.1442 0.1883 0.2182 -0.0190 0.0139  0.0459  140 LEU   A CG  
3114 C CD1 . LEU   A 140 ? 0.1596 0.1898 0.2261 -0.0121 0.0116  0.0441  140 LEU   A CD1 
3115 C CD2 . LEU   A 140 ? 0.1517 0.2057 0.2192 -0.0176 0.0151  0.0467  140 LEU   A CD2 
3127 N N   . ARG   A 141 ? 0.1499 0.1747 0.2101 -0.0104 -0.0004 0.0239  141 ARG   A N   
3128 C CA  . ARG   A 141 ? 0.1663 0.1918 0.2279 -0.0141 -0.0048 0.0078  141 ARG   A CA  
3129 C C   . ARG   A 141 ? 0.1590 0.1721 0.2258 -0.0138 -0.0053 0.0064  141 ARG   A C   
3130 O O   . ARG   A 141 ? 0.1534 0.1725 0.2397 -0.0178 0.0036  0.0075  141 ARG   A O   
3131 C CB  . ARG   A 141 ? 0.1757 0.2144 0.2513 -0.0258 -0.0003 -0.0154 141 ARG   A CB  
3132 C CG  . ARG   A 141 ? 0.2135 0.2524 0.2949 -0.0333 0.0217  -0.0211 141 ARG   A CG  
3133 C CD  . ARG   A 141 ? 0.2505 0.2838 0.3450 -0.0475 0.0104  -0.0236 141 ARG   A CD  
3134 N NE  . ARG   A 141 ? 0.2455 0.3159 0.3665 -0.0478 0.0010  -0.0141 141 ARG   A NE  
3135 C CZ  . ARG   A 141 ? 0.2429 0.3420 0.3546 -0.0656 0.0092  -0.0042 141 ARG   A CZ  
3136 N NH1 . ARG   A 141 ? 0.2284 0.3457 0.3354 -0.0799 0.0400  -0.0251 141 ARG   A NH1 
3137 N NH2 . ARG   A 141 ? 0.2506 0.3545 0.3680 -0.0632 -0.0201 0.0153  141 ARG   A NH2 
3151 N N   . VAL   A 142 ? 0.1473 0.1662 0.2170 -0.0101 -0.0067 0.0079  142 VAL   A N   
3152 C CA  . VAL   A 142 ? 0.1536 0.1671 0.2158 -0.0063 0.0144  0.0049  142 VAL   A CA  
3153 C C   . VAL   A 142 ? 0.1315 0.1568 0.2144 -0.0145 0.0140  0.0039  142 VAL   A C   
3154 O O   . VAL   A 142 ? 0.1452 0.1539 0.2289 0.0029  0.0129  0.0126  142 VAL   A O   
3155 C CB  . VAL   A 142 ? 0.1570 0.1790 0.2103 -0.0125 0.0186  0.0105  142 VAL   A CB  
3156 C CG1 . VAL   A 142 ? 0.1548 0.1670 0.2148 -0.0214 0.0233  0.0023  142 VAL   A CG1 
3157 C CG2 . VAL   A 142 ? 0.1737 0.1916 0.2326 -0.0035 0.0267  0.0041  142 VAL   A CG2 
3167 N N   . CYS   A 143 ? 0.1369 0.1603 0.2005 -0.0189 0.0146  0.0103  143 CYS   A N   
3168 C CA  . CYS   A 143 ? 0.1437 0.1672 0.2022 -0.0178 0.0154  0.0164  143 CYS   A CA  
3169 C C   . CYS   A 143 ? 0.1497 0.1578 0.2169 -0.0182 0.0042  0.0369  143 CYS   A C   
3170 O O   . CYS   A 143 ? 0.1481 0.1518 0.2258 -0.0057 -0.0020 0.0350  143 CYS   A O   
3171 C CB  . CYS   A 143 ? 0.1373 0.1718 0.2189 -0.0109 0.0214  0.0322  143 CYS   A CB  
3172 S SG  . CYS   A 143 ? 0.1639 0.1758 0.2025 -0.0002 0.0131  0.0247  143 CYS   A SG  
3178 N N   . VAL   A 144 ? 0.1426 0.1556 0.2446 -0.0209 0.0071  0.0441  144 VAL   A N   
3179 C CA  . VAL   A 144 ? 0.1515 0.1816 0.2893 -0.0177 0.0154  0.0447  144 VAL   A CA  
3180 C C   . VAL   A 144 ? 0.1445 0.1715 0.2851 -0.0217 -0.0233 0.0375  144 VAL   A C   
3181 O O   . VAL   A 144 ? 0.1641 0.1686 0.2885 -0.0113 -0.0126 0.0463  144 VAL   A O   
3182 C CB  . VAL   A 144 ? 0.1777 0.2027 0.3438 -0.0071 0.0450  0.0546  144 VAL   A CB  
3183 C CG1 . VAL   A 144 ? 0.1929 0.2322 0.3810 -0.0219 0.0333  0.0358  144 VAL   A CG1 
3184 C CG2 . VAL   A 144 ? 0.1685 0.2170 0.3467 -0.0053 0.0575  0.0677  144 VAL   A CG2 
3194 N N   . ASP   A 145 ? 0.1609 0.1680 0.2976 -0.0181 -0.0057 0.0270  145 ASP   A N   
3195 C CA  . ASP   A 145 ? 0.1600 0.1761 0.3024 -0.0227 -0.0097 0.0085  145 ASP   A CA  
3196 C C   . ASP   A 145 ? 0.1561 0.1694 0.3015 -0.0161 -0.0043 0.0072  145 ASP   A C   
3197 O O   . ASP   A 145 ? 0.1825 0.1709 0.3402 -0.0156 -0.0164 -0.0229 145 ASP   A O   
3198 C CB  . ASP   A 145 ? 0.1751 0.1978 0.3237 -0.0243 -0.0338 0.0092  145 ASP   A CB  
3199 C CG  . ASP   A 145 ? 0.2039 0.2306 0.3507 -0.0528 -0.0471 0.0208  145 ASP   A CG  
3200 O OD1 . ASP   A 145 ? 0.2008 0.2545 0.3615 -0.0596 -0.0254 0.0362  145 ASP   A OD1 
3201 O OD2 . ASP   A 145 ? 0.2306 0.2578 0.3633 -0.0677 -0.0718 0.0168  145 ASP   A OD2 
3206 N N   . THR   A 146 ? 0.1427 0.1523 0.2536 -0.0259 0.0083  0.0133  146 THR   A N   
3207 C CA  . THR   A 146 ? 0.1350 0.1531 0.2500 -0.0125 0.0004  0.0202  146 THR   A CA  
3208 C C   . THR   A 146 ? 0.1349 0.1497 0.2522 -0.0023 0.0116  0.0220  146 THR   A C   
3209 O O   . THR   A 146 ? 0.1510 0.1530 0.2698 0.0089  0.0000  0.0207  146 THR   A O   
3210 C CB  . THR   A 146 ? 0.1350 0.1545 0.2578 -0.0116 0.0015  0.0166  146 THR   A CB  
3211 O OG1 . THR   A 146 ? 0.1410 0.1659 0.2696 0.0013  0.0047  0.0072  146 THR   A OG1 
3212 C CG2 . THR   A 146 ? 0.1415 0.1616 0.2616 -0.0077 0.0057  0.0322  146 THR   A CG2 
3220 N N   . VAL   A 147 ? 0.1310 0.1513 0.2431 0.0033  0.0120  0.0189  147 VAL   A N   
3221 C CA  . VAL   A 147 ? 0.1319 0.1609 0.2439 -0.0146 0.0314  0.0286  147 VAL   A CA  
3222 C C   . VAL   A 147 ? 0.1527 0.1486 0.2371 -0.0179 0.0265  0.0434  147 VAL   A C   
3223 O O   . VAL   A 147 ? 0.1626 0.1505 0.2604 -0.0207 0.0127  0.0436  147 VAL   A O   
3224 C CB  . VAL   A 147 ? 0.1459 0.1626 0.2372 -0.0173 0.0209  0.0325  147 VAL   A CB  
3225 C CG1 . VAL   A 147 ? 0.1774 0.1708 0.2352 -0.0060 0.0241  0.0352  147 VAL   A CG1 
3226 C CG2 . VAL   A 147 ? 0.1591 0.1654 0.2466 -0.0143 0.0188  0.0313  147 VAL   A CG2 
3236 N N   . ARG   A 148 ? 0.1549 0.1558 0.2466 -0.0164 0.0211  0.0595  148 ARG   A N   
3237 C CA  . ARG   A 148 ? 0.1603 0.1573 0.2613 -0.0207 0.0089  0.0613  148 ARG   A CA  
3238 C C   . ARG   A 148 ? 0.1600 0.1661 0.2654 -0.0276 0.0209  0.0769  148 ARG   A C   
3239 O O   . ARG   A 148 ? 0.1870 0.1767 0.2795 -0.0278 0.0212  0.0652  148 ARG   A O   
3240 C CB  . ARG   A 148 ? 0.1647 0.1618 0.2687 -0.0155 0.0210  0.0506  148 ARG   A CB  
3241 C CG  . ARG   A 148 ? 0.1788 0.1609 0.3051 -0.0109 0.0449  0.0421  148 ARG   A CG  
3242 C CD  . ARG   A 148 ? 0.1955 0.1611 0.3219 -0.0076 0.0565  0.0536  148 ARG   A CD  
3243 N NE  . ARG   A 148 ? 0.1882 0.1633 0.3274 0.0070  0.0577  0.0575  148 ARG   A NE  
3244 C CZ  . ARG   A 148 ? 0.1865 0.1525 0.3063 -0.0009 0.0562  0.0576  148 ARG   A CZ  
3245 N NH1 . ARG   A 148 ? 0.1933 0.1543 0.3194 -0.0107 0.0540  0.0303  148 ARG   A NH1 
3246 N NH2 . ARG   A 148 ? 0.1776 0.1752 0.3039 0.0102  0.0490  0.0538  148 ARG   A NH2 
3260 N N   . THR   A 149 ? 0.1560 0.1774 0.2559 -0.0232 -0.0029 0.0673  149 THR   A N   
3261 C CA  . THR   A 149 ? 0.1723 0.1758 0.2504 -0.0198 0.0002  0.0613  149 THR   A CA  
3262 C C   . THR   A 149 ? 0.1639 0.1817 0.2306 -0.0261 0.0082  0.0623  149 THR   A C   
3263 O O   . THR   A 149 ? 0.1633 0.1976 0.2423 -0.0306 0.0035  0.0621  149 THR   A O   
3264 C CB  . THR   A 149 ? 0.1722 0.1861 0.2586 -0.0203 0.0052  0.0506  149 THR   A CB  
3265 O OG1 . THR   A 149 ? 0.1693 0.1760 0.2599 -0.0287 0.0112  0.0557  149 THR   A OG1 
3266 C CG2 . THR   A 149 ? 0.1658 0.1966 0.2552 -0.0143 -0.0075 0.0340  149 THR   A CG2 
3274 N N   . ASN   A 150 ? 0.1649 0.1838 0.2249 -0.0095 0.0018  0.0807  150 ASN   A N   
3275 C CA  . ASN   A 150 ? 0.1879 0.1943 0.2351 -0.0154 0.0074  0.0729  150 ASN   A CA  
3276 C C   . ASN   A 150 ? 0.1674 0.1793 0.2373 -0.0231 0.0158  0.0700  150 ASN   A C   
3277 O O   . ASN   A 150 ? 0.1662 0.1979 0.2677 -0.0216 -0.0037 0.0691  150 ASN   A O   
3278 C CB  . ASN   A 150 ? 0.2410 0.2276 0.2682 -0.0224 0.0211  0.0863  150 ASN   A CB  
3279 C CG  . ASN   A 150 ? 0.2952 0.2548 0.3333 -0.0284 0.0113  0.0967  150 ASN   A CG  
3280 O OD1 . ASN   A 150 ? 0.3164 0.2622 0.3577 -0.0314 0.0257  0.1067  150 ASN   A OD1 
3281 N ND2 . ASN   A 150 ? 0.3296 0.2767 0.3805 -0.0247 -0.0101 0.0909  150 ASN   A ND2 
3288 N N   . VAL   A 151 ? 0.1674 0.1637 0.2288 -0.0182 0.0048  0.0620  151 VAL   A N   
3289 C CA  . VAL   A 151 ? 0.1711 0.1681 0.2189 -0.0183 0.0082  0.0668  151 VAL   A CA  
3290 C C   . VAL   A 151 ? 0.1611 0.1635 0.2163 -0.0315 0.0082  0.0589  151 VAL   A C   
3291 O O   . VAL   A 151 ? 0.1790 0.1726 0.2578 -0.0251 0.0121  0.0558  151 VAL   A O   
3292 C CB  . VAL   A 151 ? 0.1980 0.1963 0.2223 -0.0132 0.0025  0.0602  151 VAL   A CB  
3293 C CG1 . VAL   A 151 ? 0.1931 0.2191 0.2518 -0.0240 0.0037  0.0474  151 VAL   A CG1 
3294 C CG2 . VAL   A 151 ? 0.2193 0.1941 0.2046 -0.0089 0.0101  0.0610  151 VAL   A CG2 
3304 N N   A TYR   A 152 ? 0.1588 0.1691 0.2126 -0.0313 -0.0008 0.0569  152 TYR   A N   
3305 N N   B TYR   A 152 ? 0.1642 0.1746 0.2069 -0.0222 0.0024  0.0504  152 TYR   A N   
3306 C CA  A TYR   A 152 ? 0.1607 0.1818 0.1917 -0.0320 -0.0009 0.0554  152 TYR   A CA  
3307 C CA  B TYR   A 152 ? 0.1689 0.1851 0.1924 -0.0154 -0.0008 0.0417  152 TYR   A CA  
3308 C C   A TYR   A 152 ? 0.1518 0.1765 0.1709 -0.0290 0.0186  0.0511  152 TYR   A C   
3309 C C   B TYR   A 152 ? 0.1617 0.1820 0.1716 -0.0128 -0.0036 0.0378  152 TYR   A C   
3310 O O   A TYR   A 152 ? 0.1502 0.1619 0.1834 -0.0302 0.0263  0.0380  152 TYR   A O   
3311 O O   B TYR   A 152 ? 0.1610 0.1820 0.1765 -0.0122 -0.0094 0.0287  152 TYR   A O   
3312 C CB  A TYR   A 152 ? 0.1825 0.1966 0.2030 -0.0370 0.0160  0.0721  152 TYR   A CB  
3313 C CB  B TYR   A 152 ? 0.1859 0.1967 0.2031 -0.0133 0.0073  0.0408  152 TYR   A CB  
3314 C CG  A TYR   A 152 ? 0.1956 0.2262 0.1917 -0.0363 0.0198  0.0847  152 TYR   A CG  
3315 C CG  B TYR   A 152 ? 0.2015 0.2110 0.2090 -0.0118 0.0092  0.0394  152 TYR   A CG  
3316 C CD1 A TYR   A 152 ? 0.2195 0.2504 0.2114 -0.0202 0.0322  0.0867  152 TYR   A CD1 
3317 C CD1 B TYR   A 152 ? 0.2126 0.2195 0.2197 -0.0089 0.0150  0.0413  152 TYR   A CD1 
3318 C CD2 A TYR   A 152 ? 0.2027 0.2424 0.1941 -0.0482 0.0110  0.0815  152 TYR   A CD2 
3319 C CD2 B TYR   A 152 ? 0.2091 0.2180 0.2134 -0.0145 0.0067  0.0371  152 TYR   A CD2 
3320 C CE1 A TYR   A 152 ? 0.2485 0.2700 0.2252 -0.0167 0.0156  0.1027  152 TYR   A CE1 
3321 C CE1 B TYR   A 152 ? 0.2253 0.2283 0.2294 -0.0088 0.0107  0.0456  152 TYR   A CE1 
3322 C CE2 A TYR   A 152 ? 0.2289 0.2626 0.2162 -0.0452 0.0157  0.0914  152 TYR   A CE2 
3323 C CE2 B TYR   A 152 ? 0.2204 0.2261 0.2246 -0.0158 0.0081  0.0412  152 TYR   A CE2 
3324 C CZ  A TYR   A 152 ? 0.2592 0.2659 0.2334 -0.0326 0.0111  0.1223  152 TYR   A CZ  
3325 C CZ  B TYR   A 152 ? 0.2317 0.2293 0.2348 -0.0140 0.0094  0.0505  152 TYR   A CZ  
3326 O OH  A TYR   A 152 ? 0.2905 0.2896 0.2915 -0.0254 0.0142  0.1390  152 TYR   A OH  
3327 O OH  B TYR   A 152 ? 0.2449 0.2410 0.2596 -0.0136 0.0134  0.0586  152 TYR   A OH  
3346 N N   A LEU   A 153 ? 0.1515 0.1748 0.1909 -0.0332 0.0160  0.0506  153 LEU   A N   
3347 N N   B LEU   A 153 ? 0.1570 0.1762 0.1561 -0.0091 -0.0051 0.0409  153 LEU   A N   
3348 C CA  A LEU   A 153 ? 0.1377 0.1598 0.1997 -0.0160 0.0188  0.0481  153 LEU   A CA  
3349 C CA  B LEU   A 153 ? 0.1510 0.1676 0.1428 0.0011  -0.0084 0.0421  153 LEU   A CA  
3350 C C   A LEU   A 153 ? 0.1369 0.1697 0.2147 -0.0147 0.0282  0.0473  153 LEU   A C   
3351 C C   B LEU   A 153 ? 0.1492 0.1692 0.1353 0.0000  -0.0120 0.0366  153 LEU   A C   
3352 O O   A LEU   A 153 ? 0.1511 0.1772 0.2345 -0.0228 0.0466  0.0528  153 LEU   A O   
3353 O O   B LEU   A 153 ? 0.1512 0.1733 0.1281 -0.0056 -0.0134 0.0318  153 LEU   A O   
3354 C CB  A LEU   A 153 ? 0.1347 0.1615 0.2110 -0.0188 0.0170  0.0442  153 LEU   A CB  
3355 C CB  B LEU   A 153 ? 0.1506 0.1644 0.1464 0.0086  -0.0033 0.0485  153 LEU   A CB  
3356 C CG  A LEU   A 153 ? 0.1439 0.1560 0.2192 -0.0203 0.0145  0.0341  153 LEU   A CG  
3357 C CG  B LEU   A 153 ? 0.1541 0.1595 0.1543 0.0117  0.0066  0.0499  153 LEU   A CG  
3358 C CD1 A LEU   A 153 ? 0.1561 0.1523 0.2088 -0.0093 0.0015  0.0409  153 LEU   A CD1 
3359 C CD1 B LEU   A 153 ? 0.1586 0.1641 0.1632 0.0099  0.0157  0.0439  153 LEU   A CD1 
3360 C CD2 A LEU   A 153 ? 0.1453 0.1582 0.2244 -0.0296 0.0135  0.0122  153 LEU   A CD2 
3361 C CD2 B LEU   A 153 ? 0.1556 0.1574 0.1660 0.0138  0.0077  0.0384  153 LEU   A CD2 
3384 N N   A ALA   A 154 ? 0.1415 0.1636 0.2257 -0.0154 0.0368  0.0475  154 ALA   A N   
3385 N N   B ALA   A 154 ? 0.1514 0.1642 0.1434 0.0018  -0.0039 0.0335  154 ALA   A N   
3386 C CA  A ALA   A 154 ? 0.1590 0.1665 0.2091 -0.0124 0.0339  0.0458  154 ALA   A CA  
3387 C CA  B ALA   A 154 ? 0.1590 0.1614 0.1516 0.0031  -0.0033 0.0285  154 ALA   A CA  
3388 C C   A ALA   A 154 ? 0.1536 0.1562 0.1964 -0.0047 0.0355  0.0458  154 ALA   A C   
3389 C C   B ALA   A 154 ? 0.1578 0.1561 0.1543 0.0025  -0.0030 0.0294  154 ALA   A C   
3390 O O   A ALA   A 154 ? 0.1547 0.1730 0.2036 -0.0114 0.0370  0.0312  154 ALA   A O   
3391 O O   B ALA   A 154 ? 0.1592 0.1490 0.1509 -0.0037 -0.0085 0.0295  154 ALA   A O   
3392 C CB  A ALA   A 154 ? 0.1829 0.1728 0.2116 -0.0036 0.0373  0.0375  154 ALA   A CB  
3393 C CB  B ALA   A 154 ? 0.1643 0.1619 0.1595 0.0060  -0.0013 0.0236  154 ALA   A CB  
3404 N N   A VAL   A 155 ? 0.1374 0.1387 0.1669 0.0085  0.0423  0.0658  155 VAL   A N   
3405 N N   B VAL   A 155 ? 0.1531 0.1604 0.1524 0.0100  0.0083  0.0327  155 VAL   A N   
3406 C CA  A VAL   A 155 ? 0.1566 0.1704 0.2172 0.0131  0.0356  0.0688  155 VAL   A CA  
3407 C CA  B VAL   A 155 ? 0.1603 0.1804 0.1801 0.0099  0.0101  0.0303  155 VAL   A CA  
3408 C CA  T VAL   A 155 ? 0.1650 0.1937 0.1973 -0.0320 0.0361  0.0404  155 VAL   A CA  
3409 C C   A VAL   A 155 ? 0.1710 0.1896 0.2449 0.0273  0.0385  0.0792  155 VAL   A C   
3410 C C   B VAL   A 155 ? 0.1676 0.1883 0.2052 0.0124  0.0109  0.0325  155 VAL   A C   
3411 C C   T VAL   A 155 ? 0.1650 0.1951 0.1837 -0.0233 0.0328  0.0417  155 VAL   A C   
3412 O O   A VAL   A 155 ? 0.1694 0.1918 0.2681 0.0310  0.0592  0.0696  155 VAL   A O   
3413 O O   B VAL   A 155 ? 0.1700 0.1886 0.2278 0.0147  0.0215  0.0301  155 VAL   A O   
3414 O O   T VAL   A 155 ? 0.1568 0.2000 0.1644 -0.0227 0.0252  0.0264  155 VAL   A O   
3415 C CB  A VAL   A 155 ? 0.1596 0.1811 0.2257 0.0227  0.0120  0.0594  155 VAL   A CB  
3416 C CB  B VAL   A 155 ? 0.1554 0.1870 0.1760 0.0129  0.0128  0.0279  155 VAL   A CB  
3417 C CB  T VAL   A 155 ? 0.1682 0.1976 0.2037 -0.0276 0.0205  0.0355  155 VAL   A CB  
3418 C CG1 A VAL   A 155 ? 0.1706 0.1828 0.2241 0.0233  0.0081  0.0521  155 VAL   A CG1 
3419 C CG1 B VAL   A 155 ? 0.1538 0.1907 0.1776 0.0098  0.0116  0.0225  155 VAL   A CG1 
3420 C CG1 T VAL   A 155 ? 0.1753 0.2005 0.1985 -0.0254 0.0190  0.0306  155 VAL   A CG1 
3421 C CG2 A VAL   A 155 ? 0.1687 0.1919 0.2380 0.0250  -0.0084 0.0518  155 VAL   A CG2 
3422 C CG2 B VAL   A 155 ? 0.1506 0.1900 0.1725 0.0141  0.0197  0.0297  155 VAL   A CG2 
3423 C CG2 T VAL   A 155 ? 0.1729 0.2003 0.2119 -0.0265 0.0068  0.0338  155 VAL   A CG2 
3449 N N   A PHE   A 156 ? 0.1847 0.1962 0.2738 0.0482  0.0387  0.0911  156 PHE   A N   
3450 N N   B PHE   A 156 ? 0.1715 0.1925 0.2168 0.0165  0.0115  0.0389  156 PHE   A N   
3451 N N   T PHE   A 156 ? 0.1770 0.1890 0.2017 -0.0135 0.0407  0.0609  156 PHE   A N   
3452 C CA  A PHE   A 156 ? 0.2127 0.2061 0.3021 0.0617  0.0347  0.0884  156 PHE   A CA  
3453 C CA  B PHE   A 156 ? 0.1848 0.1991 0.2387 0.0197  0.0169  0.0439  156 PHE   A CA  
3454 C CA  T PHE   A 156 ? 0.1956 0.1838 0.2060 -0.0042 0.0441  0.0720  156 PHE   A CA  
3455 C C   A PHE   A 156 ? 0.2155 0.2086 0.3059 0.0681  0.0500  0.0841  156 PHE   A C   
3456 C C   B PHE   A 156 ? 0.1876 0.2033 0.2446 0.0227  0.0275  0.0464  156 PHE   A C   
3457 C C   T PHE   A 156 ? 0.2020 0.1949 0.2197 0.0021  0.0601  0.0804  156 PHE   A C   
3458 O O   A PHE   A 156 ? 0.2122 0.2122 0.3268 0.0515  0.0610  0.0712  156 PHE   A O   
3459 O O   B PHE   A 156 ? 0.1846 0.2071 0.2611 0.0147  0.0384  0.0451  156 PHE   A O   
3460 O O   T PHE   A 156 ? 0.2039 0.1992 0.2434 0.0018  0.0657  0.0727  156 PHE   A O   
3461 C CB  A PHE   A 156 ? 0.2382 0.2208 0.3158 0.0585  0.0267  0.0809  156 PHE   A CB  
3462 C CB  B PHE   A 156 ? 0.1976 0.2066 0.2534 0.0137  0.0129  0.0449  156 PHE   A CB  
3463 C CB  T PHE   A 156 ? 0.2044 0.1635 0.1835 -0.0006 0.0348  0.0757  156 PHE   A CB  
3464 C CG  A PHE   A 156 ? 0.2634 0.2352 0.3359 0.0623  0.0202  0.0609  156 PHE   A CG  
3465 C CG  B PHE   A 156 ? 0.2115 0.2114 0.2693 0.0119  0.0057  0.0325  156 PHE   A CG  
3466 C CG  T PHE   A 156 ? 0.2131 0.1565 0.1730 0.0041  0.0272  0.0905  156 PHE   A CG  
3467 C CD1 A PHE   A 156 ? 0.2778 0.2400 0.3387 0.0688  0.0227  0.0495  156 PHE   A CD1 
3468 C CD1 B PHE   A 156 ? 0.2197 0.2139 0.2767 0.0150  0.0028  0.0327  156 PHE   A CD1 
3469 C CD1 T PHE   A 156 ? 0.2187 0.1691 0.1959 0.0051  0.0198  0.0761  156 PHE   A CD1 
3470 C CD2 A PHE   A 156 ? 0.2760 0.2453 0.3485 0.0666  0.0168  0.0526  156 PHE   A CD2 
3471 C CD2 B PHE   A 156 ? 0.2177 0.2171 0.2792 0.0152  0.0041  0.0243  156 PHE   A CD2 
3472 C CD2 T PHE   A 156 ? 0.2180 0.1565 0.1849 0.0086  0.0277  0.0972  156 PHE   A CD2 
3473 C CE1 A PHE   A 156 ? 0.2853 0.2444 0.3463 0.0734  0.0237  0.0435  156 PHE   A CE1 
3474 C CE1 B PHE   A 156 ? 0.2250 0.2167 0.2849 0.0173  0.0005  0.0339  156 PHE   A CE1 
3475 C CE1 T PHE   A 156 ? 0.2229 0.1722 0.2118 0.0035  0.0154  0.0708  156 PHE   A CE1 
3476 C CE2 A PHE   A 156 ? 0.2849 0.2523 0.3528 0.0707  0.0122  0.0429  156 PHE   A CE2 
3477 C CE2 B PHE   A 156 ? 0.2214 0.2186 0.2778 0.0153  0.0033  0.0238  156 PHE   A CE2 
3478 C CE2 T PHE   A 156 ? 0.2250 0.1608 0.2079 0.0073  0.0183  0.0806  156 PHE   A CE2 
3479 C CZ  A PHE   A 156 ? 0.2870 0.2519 0.3498 0.0729  0.0228  0.0408  156 PHE   A CZ  
3480 C CZ  B PHE   A 156 ? 0.2271 0.2201 0.2908 0.0162  -0.0002 0.0270  156 PHE   A CZ  
3481 C CZ  T PHE   A 156 ? 0.2271 0.1639 0.2234 0.0023  0.0156  0.0734  156 PHE   A CZ  
3509 N N   A ASP   A 157 ? 0.2146 0.2187 0.2988 0.0787  0.0403  0.0923  157 ASP   A N   
3510 N N   B ASP   A 157 ? 0.1879 0.2071 0.2341 0.0297  0.0222  0.0500  157 ASP   A N   
3511 N N   T ASP   A 157 ? 0.2016 0.2063 0.2285 0.0048  0.0560  0.0920  157 ASP   A N   
3512 C CA  A ASP   A 157 ? 0.2296 0.2465 0.2970 0.0750  0.0384  0.0978  157 ASP   A CA  
3513 C CA  B ASP   A 157 ? 0.1901 0.2155 0.2263 0.0367  0.0187  0.0579  157 ASP   A CA  
3514 C CA  T ASP   A 157 ? 0.2051 0.2229 0.2317 0.0154  0.0476  0.0975  157 ASP   A CA  
3515 C C   A ASP   A 157 ? 0.2152 0.2715 0.2977 0.0754  0.0439  0.0991  157 ASP   A C   
3516 C C   B ASP   A 157 ? 0.1861 0.2248 0.2182 0.0529  0.0266  0.0682  157 ASP   A C   
3517 C C   T ASP   A 157 ? 0.2064 0.2450 0.2374 0.0229  0.0503  0.0950  157 ASP   A C   
3518 O O   A ASP   A 157 ? 0.1952 0.2744 0.2855 0.0768  0.0411  0.0938  157 ASP   A O   
3519 O O   B ASP   A 157 ? 0.1822 0.2242 0.2218 0.0600  0.0297  0.0626  157 ASP   A O   
3520 O O   T ASP   A 157 ? 0.1925 0.2471 0.2317 0.0247  0.0526  0.0865  157 ASP   A O   
3521 C CB  A ASP   A 157 ? 0.2600 0.2509 0.3068 0.0773  0.0350  0.0896  157 ASP   A CB  
3522 C CB  B ASP   A 157 ? 0.1936 0.2136 0.2295 0.0327  0.0112  0.0541  157 ASP   A CB  
3523 C CB  T ASP   A 157 ? 0.2071 0.2176 0.2319 0.0244  0.0403  0.0970  157 ASP   A CB  
3524 C CG  A ASP   A 157 ? 0.2849 0.2540 0.3335 0.0787  0.0316  0.0810  157 ASP   A CG  
3525 C CG  B ASP   A 157 ? 0.1909 0.2087 0.2393 0.0301  0.0103  0.0520  157 ASP   A CG  
3526 C CG  T ASP   A 157 ? 0.1990 0.2062 0.2333 0.0300  0.0387  0.0994  157 ASP   A CG  
3527 O OD1 A ASP   A 157 ? 0.3064 0.2608 0.3609 0.0764  0.0209  0.0633  157 ASP   A OD1 
3528 O OD1 B ASP   A 157 ? 0.1887 0.1996 0.2477 0.0280  0.0134  0.0448  157 ASP   A OD1 
3529 O OD1 T ASP   A 157 ? 0.1973 0.2049 0.2537 0.0273  0.0360  0.0799  157 ASP   A OD1 
3530 O OD2 A ASP   A 157 ? 0.2820 0.2472 0.3388 0.0774  0.0398  0.0954  157 ASP   A OD2 
3531 O OD2 B ASP   A 157 ? 0.1890 0.2131 0.2428 0.0285  0.0066  0.0530  157 ASP   A OD2 
3532 O OD2 T ASP   A 157 ? 0.1875 0.2001 0.2183 0.0359  0.0461  0.1065  157 ASP   A OD2 
3545 N N   A LYS   A 158 ? 0.2305 0.2915 0.3102 0.0672  0.0609  0.1012  158 LYS   A N   
3546 N N   B LYS   A 158 ? 0.1872 0.2325 0.2035 0.0603  0.0368  0.0825  158 LYS   A N   
3547 N N   T LYS   A 158 ? 0.2241 0.2610 0.2439 0.0250  0.0557  0.0945  158 LYS   A N   
3548 C CA  A LYS   A 158 ? 0.2315 0.3124 0.3290 0.0624  0.0776  0.0924  158 LYS   A CA  
3549 C CA  B LYS   A 158 ? 0.1875 0.2417 0.1938 0.0593  0.0442  0.0887  158 LYS   A CA  
3550 C CA  T LYS   A 158 ? 0.2344 0.2785 0.2641 0.0276  0.0572  0.0835  158 LYS   A CA  
3551 C C   A LYS   A 158 ? 0.2101 0.3128 0.2966 0.0550  0.0658  0.1017  158 LYS   A C   
3552 C C   B LYS   A 158 ? 0.1851 0.2514 0.1972 0.0648  0.0426  0.0919  158 LYS   A C   
3553 C C   T LYS   A 158 ? 0.2306 0.2785 0.2526 0.0252  0.0419  0.0757  158 LYS   A C   
3554 O O   A LYS   A 158 ? 0.2078 0.3170 0.2997 0.0466  0.0706  0.1021  158 LYS   A O   
3555 O O   B LYS   A 158 ? 0.1769 0.2555 0.1859 0.0611  0.0552  0.0875  158 LYS   A O   
3556 O O   T LYS   A 158 ? 0.2302 0.2788 0.2560 0.0241  0.0414  0.0725  158 LYS   A O   
3557 C CB  A LYS   A 158 ? 0.2619 0.3312 0.3771 0.0615  0.1009  0.0753  158 LYS   A CB  
3558 C CB  B LYS   A 158 ? 0.1913 0.2431 0.1953 0.0468  0.0411  0.0815  158 LYS   A CB  
3559 C CB  T LYS   A 158 ? 0.2572 0.2966 0.3075 0.0290  0.0711  0.0747  158 LYS   A CB  
3560 C CG  A LYS   A 158 ? 0.2907 0.3455 0.4173 0.0609  0.1168  0.0666  158 LYS   A CG  
3561 C CG  B LYS   A 158 ? 0.1943 0.2468 0.2021 0.0348  0.0342  0.0700  158 LYS   A CG  
3562 C CG  T LYS   A 158 ? 0.2816 0.3117 0.3506 0.0307  0.0777  0.0688  158 LYS   A CG  
3563 C CD  A LYS   A 158 ? 0.3095 0.3551 0.4508 0.0608  0.1352  0.0653  158 LYS   A CD  
3564 C CD  B LYS   A 158 ? 0.1967 0.2493 0.2183 0.0242  0.0236  0.0591  158 LYS   A CD  
3565 C CD  T LYS   A 158 ? 0.3024 0.3235 0.3949 0.0346  0.0796  0.0654  158 LYS   A CD  
3566 C CE  A LYS   A 158 ? 0.3233 0.3564 0.4612 0.0572  0.1484  0.0780  158 LYS   A CE  
3567 C CE  B LYS   A 158 ? 0.1956 0.2491 0.2231 0.0193  0.0127  0.0548  158 LYS   A CE  
3568 C CE  T LYS   A 158 ? 0.3191 0.3303 0.4241 0.0384  0.0770  0.0639  158 LYS   A CE  
3569 N NZ  A LYS   A 158 ? 0.3246 0.3556 0.4672 0.0514  0.1565  0.0873  158 LYS   A NZ  
3570 N NZ  B LYS   A 158 ? 0.1965 0.2498 0.2283 0.0144  0.0010  0.0574  158 LYS   A NZ  
3571 N NZ  T LYS   A 158 ? 0.3285 0.3343 0.4408 0.0430  0.0722  0.0624  158 LYS   A NZ  
3611 N N   A ASN   A 159 ? 0.1921 0.3096 0.3012 0.0550  0.0423  0.0936  159 ASN   A N   
3612 N N   B ASN   A 159 ? 0.1895 0.2566 0.2107 0.0738  0.0321  0.0846  159 ASN   A N   
3613 N N   T ASN   A 159 ? 0.2277 0.2789 0.2642 0.0228  0.0272  0.0608  159 ASN   A N   
3614 C CA  A ASN   A 159 ? 0.1915 0.3051 0.2818 0.0427  0.0234  0.0980  159 ASN   A CA  
3615 C CA  B ASN   A 159 ? 0.2031 0.2606 0.2396 0.0733  0.0238  0.0669  159 ASN   A CA  
3616 C CA  T ASN   A 159 ? 0.2307 0.2791 0.2632 0.0158  0.0204  0.0556  159 ASN   A CA  
3617 C C   A ASN   A 159 ? 0.1792 0.2999 0.2549 0.0310  0.0251  0.0925  159 ASN   A C   
3618 C C   B ASN   A 159 ? 0.2049 0.2645 0.2333 0.0664  0.0248  0.0525  159 ASN   A C   
3619 C C   T ASN   A 159 ? 0.2320 0.2797 0.2580 0.0085  0.0313  0.0504  159 ASN   A C   
3620 O O   A ASN   A 159 ? 0.1559 0.2948 0.2276 0.0343  -0.0023 0.0776  159 ASN   A O   
3621 O O   B ASN   A 159 ? 0.1996 0.2689 0.2271 0.0633  0.0238  0.0491  159 ASN   A O   
3622 O O   T ASN   A 159 ? 0.2285 0.2782 0.2429 0.0059  0.0270  0.0379  159 ASN   A O   
3623 C CB  A ASN   A 159 ? 0.2046 0.3105 0.3237 0.0413  0.0103  0.1072  159 ASN   A CB  
3624 C CB  B ASN   A 159 ? 0.2135 0.2587 0.2644 0.0762  0.0248  0.0718  159 ASN   A CB  
3625 C CB  T ASN   A 159 ? 0.2355 0.2824 0.2873 0.0166  0.0087  0.0600  159 ASN   A CB  
3626 C CG  A ASN   A 159 ? 0.2195 0.3185 0.3713 0.0361  0.0064  0.1052  159 ASN   A CG  
3627 C CG  B ASN   A 159 ? 0.2239 0.2574 0.2919 0.0707  0.0313  0.0711  159 ASN   A CG  
3628 C CG  T ASN   A 159 ? 0.2413 0.2863 0.3166 0.0160  0.0037  0.0600  159 ASN   A CG  
3629 O OD1 A ASN   A 159 ? 0.2300 0.3322 0.4045 0.0293  0.0203  0.1022  159 ASN   A OD1 
3630 O OD1 B ASN   A 159 ? 0.2299 0.2651 0.3054 0.0658  0.0389  0.0735  159 ASN   A OD1 
3631 O OD1 T ASN   A 159 ? 0.2455 0.2964 0.3391 0.0150  0.0119  0.0583  159 ASN   A OD1 
3632 N ND2 A ASN   A 159 ? 0.2219 0.3205 0.3954 0.0388  0.0002  0.0937  159 ASN   A ND2 
3633 N ND2 B ASN   A 159 ? 0.2267 0.2565 0.2990 0.0672  0.0342  0.0690  159 ASN   A ND2 
3634 N ND2 T ASN   A 159 ? 0.2422 0.2870 0.3295 0.0176  -0.0014 0.0547  159 ASN   A ND2 
3653 N N   A LEU   A 160 ? 0.1709 0.2850 0.2489 0.0311  0.0199  0.1078  160 LEU   A N   
3654 N N   B LEU   A 160 ? 0.2027 0.2578 0.2230 0.0646  0.0174  0.0542  160 LEU   A N   
3655 N N   T LEU   A 160 ? 0.2291 0.2740 0.2637 0.0058  0.0332  0.0583  160 LEU   A N   
3656 C CA  A LEU   A 160 ? 0.1665 0.2754 0.2320 0.0210  0.0312  0.1163  160 LEU   A CA  
3657 C CA  B LEU   A 160 ? 0.2013 0.2509 0.2192 0.0570  0.0214  0.0480  160 LEU   A CA  
3658 C CA  T LEU   A 160 ? 0.2297 0.2688 0.2600 0.0004  0.0392  0.0668  160 LEU   A CA  
3659 C C   A LEU   A 160 ? 0.1506 0.2702 0.2009 0.0096  0.0296  0.1171  160 LEU   A C   
3660 C C   B LEU   A 160 ? 0.1898 0.2439 0.2007 0.0477  0.0227  0.0483  160 LEU   A C   
3661 O O   A LEU   A 160 ? 0.1340 0.2766 0.1944 0.0039  0.0228  0.1101  160 LEU   A O   
3662 O O   B LEU   A 160 ? 0.1818 0.2474 0.1921 0.0443  0.0229  0.0453  160 LEU   A O   
3663 C CB  A LEU   A 160 ? 0.1656 0.2731 0.2402 0.0169  0.0291  0.1155  160 LEU   A CB  
3664 C CB  B LEU   A 160 ? 0.2094 0.2522 0.2336 0.0534  0.0287  0.0353  160 LEU   A CB  
3665 C CB  T LEU   A 160 ? 0.2273 0.2652 0.2552 -0.0075 0.0426  0.0726  160 LEU   A CB  
3666 C CG  A LEU   A 160 ? 0.1708 0.2777 0.2687 0.0053  0.0168  0.0927  160 LEU   A CG  
3667 C CG  B LEU   A 160 ? 0.2137 0.2549 0.2497 0.0491  0.0308  0.0202  160 LEU   A CG  
3668 C CG  T LEU   A 160 ? 0.2280 0.2650 0.2614 -0.0171 0.0401  0.0672  160 LEU   A CG  
3669 C CD1 A LEU   A 160 ? 0.1879 0.2877 0.2824 0.0043  0.0200  0.0760  160 LEU   A CD1 
3670 C CD1 B LEU   A 160 ? 0.2095 0.2565 0.2505 0.0437  0.0381  0.0161  160 LEU   A CD1 
3671 C CD1 T LEU   A 160 ? 0.2341 0.2702 0.2650 -0.0166 0.0407  0.0598  160 LEU   A CD1 
3672 C CD2 A LEU   A 160 ? 0.1711 0.2729 0.2786 -0.0028 0.0253  0.0894  160 LEU   A CD2 
3673 C CD2 B LEU   A 160 ? 0.2212 0.2556 0.2622 0.0466  0.0279  0.0148  160 LEU   A CD2 
3674 C CD2 T LEU   A 160 ? 0.2273 0.2603 0.2591 -0.0234 0.0457  0.0707  160 LEU   A CD2 
3707 N N   A TYR   A 161 ? 0.1649 0.2579 0.2279 0.0055  0.0261  0.1079  161 TYR   A N   
3708 N N   B TYR   A 161 ? 0.1894 0.2322 0.1923 0.0423  0.0273  0.0428  161 TYR   A N   
3709 C CA  A TYR   A 161 ? 0.1751 0.2524 0.2200 -0.0065 0.0293  0.0928  161 TYR   A CA  
3710 C CA  B TYR   A 161 ? 0.1940 0.2247 0.1895 0.0310  0.0240  0.0397  161 TYR   A CA  
3711 C C   A TYR   A 161 ? 0.1802 0.2778 0.2305 -0.0056 0.0190  0.0884  161 TYR   A C   
3712 C C   B TYR   A 161 ? 0.2010 0.2321 0.1938 0.0237  0.0181  0.0396  161 TYR   A C   
3713 O O   A TYR   A 161 ? 0.1671 0.2835 0.2117 -0.0086 0.0206  0.0853  161 TYR   A O   
3714 O O   B TYR   A 161 ? 0.1992 0.2343 0.1871 0.0214  0.0162  0.0370  161 TYR   A O   
3715 C CB  A TYR   A 161 ? 0.1926 0.2363 0.2211 -0.0048 0.0383  0.0825  161 TYR   A CB  
3716 C CB  B TYR   A 161 ? 0.1948 0.2134 0.1835 0.0284  0.0248  0.0382  161 TYR   A CB  
3717 C CG  A TYR   A 161 ? 0.1819 0.2181 0.2245 0.0052  0.0386  0.0533  161 TYR   A CG  
3718 C CG  B TYR   A 161 ? 0.1900 0.2011 0.1813 0.0279  0.0227  0.0353  161 TYR   A CG  
3719 C CD1 A TYR   A 161 ? 0.1678 0.2105 0.2386 0.0004  0.0285  0.0442  161 TYR   A CD1 
3720 C CD1 B TYR   A 161 ? 0.1874 0.1948 0.1856 0.0283  0.0180  0.0301  161 TYR   A CD1 
3721 C CD2 A TYR   A 161 ? 0.1789 0.2132 0.2404 0.0144  0.0370  0.0476  161 TYR   A CD2 
3722 C CD2 B TYR   A 161 ? 0.1889 0.1970 0.1894 0.0258  0.0237  0.0409  161 TYR   A CD2 
3723 C CE1 A TYR   A 161 ? 0.1650 0.2032 0.2318 0.0012  0.0285  0.0471  161 TYR   A CE1 
3724 C CE1 B TYR   A 161 ? 0.1867 0.1935 0.1901 0.0274  0.0195  0.0341  161 TYR   A CE1 
3725 C CE2 A TYR   A 161 ? 0.1800 0.2034 0.2335 0.0027  0.0181  0.0517  161 TYR   A CE2 
3726 C CE2 B TYR   A 161 ? 0.1894 0.1953 0.1898 0.0203  0.0191  0.0464  161 TYR   A CE2 
3727 C CZ  A TYR   A 161 ? 0.1803 0.1978 0.2214 -0.0051 0.0188  0.0487  161 TYR   A CZ  
3728 C CZ  B TYR   A 161 ? 0.1926 0.1931 0.1932 0.0231  0.0197  0.0450  161 TYR   A CZ  
3729 O OH  A TYR   A 161 ? 0.1949 0.1887 0.2334 0.0047  0.0096  0.0516  161 TYR   A OH  
3730 O OH  B TYR   A 161 ? 0.2002 0.1907 0.2211 0.0223  0.0166  0.0484  161 TYR   A OH  
3749 N N   A ASP   A 162 ? 0.1763 0.2893 0.2559 0.0009  0.0312  0.0963  162 ASP   A N   
3750 N N   B ASP   A 162 ? 0.2056 0.2348 0.2023 0.0211  0.0201  0.0468  162 ASP   A N   
3751 C CA  A ASP   A 162 ? 0.1722 0.3118 0.2756 -0.0051 0.0352  0.0912  162 ASP   A CA  
3752 C CA  B ASP   A 162 ? 0.2105 0.2380 0.2098 0.0201  0.0146  0.0561  162 ASP   A CA  
3753 C C   A ASP   A 162 ? 0.1583 0.3245 0.2677 -0.0112 0.0227  0.0898  162 ASP   A C   
3754 C C   B ASP   A 162 ? 0.2214 0.2479 0.2217 0.0168  0.0067  0.0441  162 ASP   A C   
3755 O O   A ASP   A 162 ? 0.1378 0.3274 0.2899 -0.0087 0.0102  0.0798  162 ASP   A O   
3756 O O   B ASP   A 162 ? 0.2207 0.2471 0.2134 0.0190  -0.0032 0.0425  162 ASP   A O   
3757 C CB  A ASP   A 162 ? 0.1732 0.3289 0.3028 0.0000  0.0506  0.0773  162 ASP   A CB  
3758 C CB  B ASP   A 162 ? 0.2022 0.2286 0.2080 0.0223  0.0149  0.0783  162 ASP   A CB  
3759 C CG  A ASP   A 162 ? 0.1861 0.3517 0.3280 0.0049  0.0522  0.0679  162 ASP   A CG  
3760 C CG  B ASP   A 162 ? 0.1937 0.2210 0.2104 0.0225  0.0195  0.1010  162 ASP   A CG  
3761 O OD1 A ASP   A 162 ? 0.1968 0.3607 0.3256 0.0028  0.0535  0.0706  162 ASP   A OD1 
3762 O OD1 B ASP   A 162 ? 0.1905 0.2203 0.2086 0.0259  0.0154  0.1130  162 ASP   A OD1 
3763 O OD2 A ASP   A 162 ? 0.1976 0.3614 0.3418 0.0211  0.0614  0.0513  162 ASP   A OD2 
3764 O OD2 B ASP   A 162 ? 0.1890 0.2191 0.2031 0.0214  0.0296  0.1148  162 ASP   A OD2 
3773 N N   A LYS   A 163 ? 0.1761 0.3368 0.2659 -0.0061 0.0100  0.0788  163 LYS   A N   
3774 N N   B LYS   A 163 ? 0.2343 0.2614 0.2364 0.0143  0.0126  0.0346  163 LYS   A N   
3775 C CA  A LYS   A 163 ? 0.1879 0.3513 0.2677 -0.0035 -0.0018 0.0702  163 LYS   A CA  
3776 C CA  B LYS   A 163 ? 0.2432 0.2717 0.2491 0.0117  0.0147  0.0289  163 LYS   A CA  
3777 C C   A LYS   A 163 ? 0.1802 0.3379 0.2536 -0.0159 0.0102  0.0669  163 LYS   A C   
3778 C C   B LYS   A 163 ? 0.2403 0.2658 0.2342 0.0113  0.0201  0.0184  163 LYS   A C   
3779 O O   A LYS   A 163 ? 0.1728 0.3465 0.2608 -0.0228 0.0118  0.0490  163 LYS   A O   
3780 O O   B LYS   A 163 ? 0.2407 0.2631 0.2296 0.0131  0.0247  0.0047  163 LYS   A O   
3781 C CB  A LYS   A 163 ? 0.2333 0.3768 0.3123 0.0235  -0.0183 0.0675  163 LYS   A CB  
3782 C CB  B LYS   A 163 ? 0.2573 0.2872 0.2803 0.0115  0.0150  0.0336  163 LYS   A CB  
3783 C CG  A LYS   A 163 ? 0.2695 0.3998 0.3683 0.0330  -0.0208 0.0569  163 LYS   A CG  
3784 C CG  B LYS   A 163 ? 0.2741 0.3018 0.3165 0.0092  0.0139  0.0333  163 LYS   A CG  
3785 C CD  A LYS   A 163 ? 0.3113 0.4219 0.4454 0.0376  -0.0217 0.0463  163 LYS   A CD  
3786 C CD  B LYS   A 163 ? 0.2876 0.3148 0.3559 0.0078  0.0146  0.0312  163 LYS   A CD  
3787 C CE  A LYS   A 163 ? 0.3476 0.4374 0.5042 0.0351  -0.0203 0.0443  163 LYS   A CE  
3788 C CE  B LYS   A 163 ? 0.2954 0.3224 0.3833 0.0080  0.0150  0.0326  163 LYS   A CE  
3789 N NZ  A LYS   A 163 ? 0.3568 0.4486 0.5369 0.0323  -0.0188 0.0469  163 LYS   A NZ  
3790 N NZ  B LYS   A 163 ? 0.2996 0.3261 0.4035 0.0086  0.0151  0.0307  163 LYS   A NZ  
3817 N N   A LEU   A 164 ? 0.1570 0.3038 0.2188 -0.0212 0.0129  0.0708  164 LEU   A N   
3818 N N   B LEU   A 164 ? 0.2305 0.2589 0.2186 0.0107  0.0195  0.0179  164 LEU   A N   
3819 C CA  A LEU   A 164 ? 0.1679 0.2855 0.2107 -0.0331 0.0300  0.0604  164 LEU   A CA  
3820 C CA  B LEU   A 164 ? 0.2260 0.2562 0.2174 0.0055  0.0207  0.0144  164 LEU   A CA  
3821 C C   A LEU   A 164 ? 0.1773 0.2890 0.2135 -0.0400 0.0251  0.0583  164 LEU   A C   
3822 C C   B LEU   A 164 ? 0.2195 0.2514 0.2178 0.0041  0.0174  0.0125  164 LEU   A C   
3823 O O   A LEU   A 164 ? 0.1729 0.2901 0.2221 -0.0413 0.0354  0.0539  164 LEU   A O   
3824 O O   B LEU   A 164 ? 0.2170 0.2527 0.2273 0.0050  0.0183  0.0090  164 LEU   A O   
3825 C CB  A LEU   A 164 ? 0.1669 0.2639 0.2104 -0.0314 0.0335  0.0627  164 LEU   A CB  
3826 C CB  B LEU   A 164 ? 0.2265 0.2569 0.2136 0.0025  0.0220  0.0180  164 LEU   A CB  
3827 C CG  A LEU   A 164 ? 0.1723 0.2488 0.2101 -0.0145 0.0288  0.0576  164 LEU   A CG  
3828 C CG  B LEU   A 164 ? 0.2280 0.2563 0.2083 0.0021  0.0248  0.0202  164 LEU   A CG  
3829 C CD1 A LEU   A 164 ? 0.1579 0.2402 0.2017 -0.0002 0.0216  0.0704  164 LEU   A CD1 
3830 C CD1 B LEU   A 164 ? 0.2261 0.2555 0.2011 0.0007  0.0271  0.0220  164 LEU   A CD1 
3831 C CD2 A LEU   A 164 ? 0.1791 0.2530 0.2075 -0.0195 0.0296  0.0345  164 LEU   A CD2 
3832 C CD2 B LEU   A 164 ? 0.2307 0.2586 0.2159 0.0009  0.0217  0.0146  164 LEU   A CD2 
3855 N N   A VAL   A 165 ? 0.1768 0.2882 0.1979 -0.0419 0.0219  0.0682  165 VAL   A N   
3856 N N   B VAL   A 165 ? 0.2108 0.2446 0.2050 0.0009  0.0174  0.0174  165 VAL   A N   
3857 C CA  A VAL   A 165 ? 0.1764 0.2887 0.1856 -0.0461 0.0240  0.0703  165 VAL   A CA  
3858 C CA  B VAL   A 165 ? 0.2058 0.2396 0.2007 0.0019  0.0133  0.0173  165 VAL   A CA  
3859 C C   A VAL   A 165 ? 0.1773 0.2975 0.2065 -0.0399 0.0248  0.0594  165 VAL   A C   
3860 C C   B VAL   A 165 ? 0.2045 0.2369 0.2002 -0.0001 0.0089  0.0177  165 VAL   A C   
3861 O O   A VAL   A 165 ? 0.1739 0.2940 0.2075 -0.0322 0.0354  0.0495  165 VAL   A O   
3862 O O   B VAL   A 165 ? 0.2055 0.2367 0.2043 -0.0001 0.0027  0.0208  165 VAL   A O   
3863 C CB  A VAL   A 165 ? 0.2024 0.2814 0.1898 -0.0490 0.0302  0.0685  165 VAL   A CB  
3864 C CB  B VAL   A 165 ? 0.2039 0.2395 0.2025 0.0040  0.0157  0.0124  165 VAL   A CB  
3865 C CG1 A VAL   A 165 ? 0.2121 0.2855 0.1992 -0.0481 0.0352  0.0528  165 VAL   A CG1 
3866 C CG1 B VAL   A 165 ? 0.2054 0.2407 0.2043 0.0023  0.0196  0.0136  165 VAL   A CG1 
3867 C CG2 A VAL   A 165 ? 0.2157 0.2854 0.1949 -0.0424 0.0174  0.0774  165 VAL   A CG2 
3868 C CG2 B VAL   A 165 ? 0.2032 0.2392 0.2046 0.0070  0.0129  0.0075  165 VAL   A CG2 
3887 N N   A SER   A 166 ? 0.1696 0.3059 0.2274 -0.0334 0.0248  0.0529  166 SER   A N   
3888 N N   B SER   A 166 ? 0.1991 0.2388 0.2015 -0.0010 0.0151  0.0183  166 SER   A N   
3889 C CA  A SER   A 166 ? 0.1664 0.3233 0.2473 -0.0294 0.0325  0.0470  166 SER   A CA  
3890 C CA  B SER   A 166 ? 0.1994 0.2453 0.2046 -0.0000 0.0147  0.0157  166 SER   A CA  
3891 C C   A SER   A 166 ? 0.1667 0.3407 0.2672 -0.0178 0.0193  0.0264  166 SER   A C   
3892 C C   B SER   A 166 ? 0.2076 0.2491 0.2055 0.0069  0.0114  0.0093  166 SER   A C   
3893 O O   A SER   A 166 ? 0.1738 0.3588 0.3147 -0.0284 0.0214  -0.0132 166 SER   A O   
3894 O O   B SER   A 166 ? 0.2034 0.2450 0.2065 0.0121  0.0132  -0.0019 166 SER   A O   
3895 C CB  A SER   A 166 ? 0.1816 0.3344 0.2661 -0.0096 0.0209  0.0430  166 SER   A CB  
3896 C CB  B SER   A 166 ? 0.1909 0.2485 0.2103 0.0010  0.0086  0.0174  166 SER   A CB  
3897 O OG  A SER   A 166 ? 0.2085 0.3485 0.2929 -0.0044 0.0090  0.0502  166 SER   A OG  
3898 O OG  B SER   A 166 ? 0.1853 0.2517 0.2151 -0.0003 0.0037  0.0227  166 SER   A OG  
3909 N N   A SER   A 167 ? 0.1655 0.3426 0.2220 0.0074  0.0093  0.0405  167 SER   A N   
3910 N N   B SER   A 167 ? 0.2239 0.2616 0.2137 0.0070  0.0070  0.0142  167 SER   A N   
3911 C CA  A SER   A 167 ? 0.1847 0.3375 0.2308 0.0227  -0.0051 0.0336  167 SER   A CA  
3912 C CA  B SER   A 167 ? 0.2408 0.2738 0.2299 0.0046  0.0040  0.0150  167 SER   A CA  
3913 C C   A SER   A 167 ? 0.1879 0.3320 0.2194 0.0298  0.0160  0.0344  167 SER   A C   
3914 C C   B SER   A 167 ? 0.2545 0.2799 0.2456 -0.0009 0.0084  0.0134  167 SER   A C   
3915 O O   A SER   A 167 ? 0.2099 0.3294 0.2352 0.0346  -0.0012 0.0365  167 SER   A O   
3916 O O   B SER   A 167 ? 0.2560 0.2786 0.2483 -0.0027 0.0093  0.0163  167 SER   A O   
3917 C CB  A SER   A 167 ? 0.1964 0.3383 0.2361 0.0289  -0.0075 0.0358  167 SER   A CB  
3918 C CB  B SER   A 167 ? 0.2448 0.2813 0.2327 0.0058  -0.0010 0.0226  167 SER   A CB  
3919 O OG  A SER   A 167 ? 0.1976 0.3452 0.2581 0.0301  0.0043  0.0357  167 SER   A OG  
3920 O OG  B SER   A 167 ? 0.2478 0.2868 0.2372 0.0079  -0.0060 0.0275  167 SER   A OG  
3931 N N   A PHE   A 168 ? 0.1806 0.3296 0.2152 0.0343  0.0295  0.0408  168 PHE   A N   
3932 N N   B PHE   A 168 ? 0.2696 0.2888 0.2664 -0.0026 0.0081  0.0090  168 PHE   A N   
3933 C CA  A PHE   A 168 ? 0.1809 0.3320 0.2317 0.0245  0.0353  0.0429  168 PHE   A CA  
3934 C CA  B PHE   A 168 ? 0.2855 0.2992 0.2890 -0.0047 0.0074  0.0024  168 PHE   A CA  
3935 C C   A PHE   A 168 ? 0.1875 0.3466 0.2652 0.0147  0.0717  0.0368  168 PHE   A C   
3936 C C   B PHE   A 168 ? 0.3078 0.3185 0.3303 -0.0034 0.0123  0.0022  168 PHE   A C   
3937 O O   A PHE   A 168 ? 0.2044 0.3594 0.3244 -0.0036 0.0762  0.0559  168 PHE   A O   
3938 O O   B PHE   A 168 ? 0.3117 0.3206 0.3377 -0.0066 0.0155  0.0058  168 PHE   A O   
3939 C CB  A PHE   A 168 ? 0.1800 0.3180 0.2180 0.0199  0.0228  0.0329  168 PHE   A CB  
3940 C CB  B PHE   A 168 ? 0.2792 0.2906 0.2715 -0.0074 -0.0008 -0.0041 168 PHE   A CB  
3941 C CG  A PHE   A 168 ? 0.1826 0.3062 0.2084 0.0152  0.0162  0.0378  168 PHE   A CG  
3942 C CG  B PHE   A 168 ? 0.2730 0.2826 0.2521 -0.0092 -0.0065 -0.0085 168 PHE   A CG  
3943 C CD1 A PHE   A 168 ? 0.1845 0.3034 0.2220 0.0076  0.0133  0.0456  168 PHE   A CD1 
3944 C CD1 B PHE   A 168 ? 0.2704 0.2805 0.2442 -0.0090 -0.0122 -0.0105 168 PHE   A CD1 
3945 C CD2 A PHE   A 168 ? 0.1761 0.2991 0.2005 0.0043  0.0265  0.0377  168 PHE   A CD2 
3946 C CD2 B PHE   A 168 ? 0.2683 0.2775 0.2413 -0.0128 -0.0068 -0.0098 168 PHE   A CD2 
3947 C CE1 A PHE   A 168 ? 0.1778 0.2941 0.2165 0.0076  0.0086  0.0599  168 PHE   A CE1 
3948 C CE1 B PHE   A 168 ? 0.2680 0.2775 0.2392 -0.0093 -0.0152 -0.0108 168 PHE   A CE1 
3949 C CE2 A PHE   A 168 ? 0.1852 0.2856 0.2106 0.0032  0.0203  0.0474  168 PHE   A CE2 
3950 C CE2 B PHE   A 168 ? 0.2661 0.2740 0.2382 -0.0149 -0.0086 -0.0091 168 PHE   A CE2 
3951 C CZ  A PHE   A 168 ? 0.1763 0.2857 0.2215 0.0025  0.0132  0.0524  168 PHE   A CZ  
3952 C CZ  B PHE   A 168 ? 0.2655 0.2750 0.2349 -0.0129 -0.0130 -0.0098 168 PHE   A CZ  
3971 N N   A LEU   A 169 ? 0.2297 0.3510 0.2954 0.0045  0.0677  0.0100  169 LEU   A N   
3972 N N   B LEU   A 169 ? 0.3290 0.3348 0.3669 -0.0006 0.0098  -0.0030 169 LEU   A N   
3973 C CA  A LEU   A 169 ? 0.2932 0.3665 0.3797 0.0094  0.0265  0.0018  169 LEU   A CA  
3974 C CA  B LEU   A 169 ? 0.3493 0.3530 0.4018 0.0037  0.0030  -0.0061 169 LEU   A CA  
3975 C C   A LEU   A 169 ? 0.3014 0.3590 0.4042 0.0083  0.0199  0.0203  169 LEU   A C   
3976 C C   B LEU   A 169 ? 0.3562 0.3597 0.4202 0.0053  -0.0026 -0.0064 169 LEU   A C   
3977 O O   A LEU   A 169 ? 0.3067 0.3579 0.4065 0.0141  0.0205  0.0186  169 LEU   A O   
3978 O O   B LEU   A 169 ? 0.3621 0.3653 0.4290 0.0057  -0.0057 -0.0063 169 LEU   A O   
3979 C CB  A LEU   A 169 ? 0.3385 0.3870 0.4102 0.0078  -0.0021 -0.0264 169 LEU   A CB  
3980 C CB  B LEU   A 169 ? 0.3599 0.3634 0.4136 0.0056  0.0030  -0.0110 169 LEU   A CB  
3981 C CG  A LEU   A 169 ? 0.3797 0.4057 0.4467 0.0003  -0.0220 -0.0567 169 LEU   A CG  
3982 C CG  B LEU   A 169 ? 0.3673 0.3717 0.4239 0.0070  0.0009  -0.0156 169 LEU   A CG  
3983 C CD1 A LEU   A 169 ? 0.3926 0.4090 0.4644 -0.0026 -0.0320 -0.0629 169 LEU   A CD1 
3984 C CD1 B LEU   A 169 ? 0.3690 0.3738 0.4242 0.0069  0.0001  -0.0175 169 LEU   A CD1 
3985 C CD2 A LEU   A 169 ? 0.3948 0.4153 0.4555 -0.0032 -0.0235 -0.0695 169 LEU   A CD2 
3986 C CD2 B LEU   A 169 ? 0.3703 0.3749 0.4244 0.0065  -0.0003 -0.0155 169 LEU   A CD2 
3987 O OXT A LEU   A 169 ? 0.2814 0.3554 0.3921 -0.0029 0.0284  0.0305  169 LEU   A OXT 
3988 O OXT B LEU   A 169 ? 0.3545 0.3599 0.4243 0.0067  -0.0025 -0.0078 169 LEU   A OXT 
4011 N N   A SER   B 1   ? 0.3723 0.3103 0.3205 -0.1036 -0.0662 0.0150  1   SER   B N   
4012 N N   B SER   B 1   ? 0.3473 0.3377 0.3404 -0.0462 -0.0373 0.0165  1   SER   B N   
4013 C CA  A SER   B 1   ? 0.3659 0.3252 0.3484 -0.1149 -0.0764 0.0105  1   SER   B CA  
4014 C CA  B SER   B 1   ? 0.3448 0.3400 0.3460 -0.0490 -0.0377 0.0181  1   SER   B CA  
4015 C C   A SER   B 1   ? 0.3356 0.3349 0.3391 -0.1214 -0.0897 0.0358  1   SER   B C   
4016 C C   B SER   B 1   ? 0.3329 0.3399 0.3396 -0.0517 -0.0454 0.0356  1   SER   B C   
4017 O O   A SER   B 1   ? 0.3484 0.3399 0.3223 -0.1094 -0.0769 0.0358  1   SER   B O   
4018 O O   B SER   B 1   ? 0.3364 0.3405 0.3328 -0.0491 -0.0431 0.0322  1   SER   B O   
4019 C CB  A SER   B 1   ? 0.3814 0.3210 0.3612 -0.1205 -0.0680 -0.0159 1   SER   B CB  
4020 C CB  B SER   B 1   ? 0.3509 0.3405 0.3478 -0.0486 -0.0303 0.0043  1   SER   B CB  
4021 O OG  A SER   B 1   ? 0.3980 0.3352 0.4304 -0.1176 -0.0585 -0.0236 1   SER   B OG  
4022 O OG  B SER   B 1   ? 0.3560 0.3440 0.3675 -0.0489 -0.0273 -0.0030 1   SER   B OG  
4037 N N   A MET   B 2   ? 0.3091 0.3357 0.3399 -0.1331 -0.0933 0.0858  2   MET   B N   
4038 N N   B MET   B 2   ? 0.3195 0.3387 0.3381 -0.0572 -0.0531 0.0636  2   MET   B N   
4039 C CA  A MET   B 2   ? 0.3000 0.3484 0.3616 -0.1133 -0.0931 0.1093  2   MET   B CA  
4040 C CA  B MET   B 2   ? 0.3062 0.3385 0.3398 -0.0594 -0.0613 0.0891  2   MET   B CA  
4041 C C   A MET   B 2   ? 0.2780 0.3394 0.3335 -0.0853 -0.1026 0.1368  2   MET   B C   
4042 C C   B MET   B 2   ? 0.2811 0.3252 0.3172 -0.0707 -0.0730 0.1203  2   MET   B C   
4043 O O   A MET   B 2   ? 0.2800 0.3533 0.3369 -0.0717 -0.1251 0.1430  2   MET   B O   
4044 O O   B MET   B 2   ? 0.2838 0.3280 0.3119 -0.0685 -0.0770 0.1207  2   MET   B O   
4045 C CB  A MET   B 2   ? 0.3284 0.3821 0.4511 -0.0967 -0.0714 0.0832  2   MET   B CB  
4046 C CB  B MET   B 2   ? 0.3201 0.3537 0.3737 -0.0449 -0.0569 0.0802  2   MET   B CB  
4047 C CG  A MET   B 2   ? 0.3590 0.4161 0.5395 -0.0713 -0.0431 0.0686  2   MET   B CG  
4048 C CG  B MET   B 2   ? 0.3322 0.3679 0.4031 -0.0300 -0.0530 0.0786  2   MET   B CG  
4049 S SD  A MET   B 2   ? 0.3927 0.4549 0.6308 -0.0461 -0.0204 0.0531  2   MET   B SD  
4050 S SD  B MET   B 2   ? 0.3436 0.3835 0.4267 -0.0156 -0.0535 0.0772  2   MET   B SD  
4051 C CE  A MET   B 2   ? 0.3951 0.4576 0.6304 -0.0455 -0.0121 0.0524  2   MET   B CE  
4052 C CE  B MET   B 2   ? 0.3458 0.3865 0.4336 -0.0148 -0.0505 0.0711  2   MET   B CE  
4071 N N   . VAL   B 3   ? 0.2506 0.3047 0.3013 -0.0880 -0.0793 0.1516  3   VAL   B N   
4072 C CA  . VAL   B 3   ? 0.2322 0.2782 0.3006 -0.0812 -0.0778 0.1246  3   VAL   B CA  
4073 C C   . VAL   B 3   ? 0.2131 0.2694 0.2639 -0.0784 -0.0722 0.1069  3   VAL   B C   
4074 O O   . VAL   B 3   ? 0.2108 0.2831 0.2689 -0.0815 -0.0819 0.1167  3   VAL   B O   
4075 C CB  . VAL   B 3   ? 0.2413 0.2615 0.3582 -0.0789 -0.0726 0.1012  3   VAL   B CB  
4076 C CG1 . VAL   B 3   ? 0.2511 0.2518 0.3866 -0.0777 -0.0731 0.0871  3   VAL   B CG1 
4077 C CG2 . VAL   B 3   ? 0.2443 0.2631 0.3819 -0.0737 -0.0566 0.1081  3   VAL   B CG2 
4088 N N   . ASN   B 4   ? 0.2132 0.2325 0.2303 -0.0753 -0.0579 0.0871  4   ASN   B N   
4089 C CA  . ASN   B 4   ? 0.2118 0.2364 0.1948 -0.0701 -0.0529 0.0594  4   ASN   B CA  
4090 C C   . ASN   B 4   ? 0.2173 0.2490 0.1952 -0.0682 -0.0484 0.0409  4   ASN   B C   
4091 O O   . ASN   B 4   ? 0.2151 0.2511 0.2073 -0.0653 -0.0367 0.0294  4   ASN   B O   
4092 C CB  . ASN   B 4   ? 0.2163 0.2310 0.1768 -0.0632 -0.0652 0.0467  4   ASN   B CB  
4093 C CG  . ASN   B 4   ? 0.2193 0.2113 0.1528 -0.0622 -0.0638 0.0414  4   ASN   B CG  
4094 O OD1 . ASN   B 4   ? 0.2232 0.2010 0.1728 -0.0620 -0.0611 0.0388  4   ASN   B OD1 
4095 N ND2 . ASN   B 4   ? 0.2327 0.2138 0.1913 -0.0374 -0.0458 0.0344  4   ASN   B ND2 
4102 N N   . SER   B 5   ? 0.2248 0.2679 0.2063 -0.0754 -0.0336 0.0355  5   SER   B N   
4103 C CA  . SER   B 5   ? 0.2511 0.3038 0.2259 -0.0656 -0.0055 0.0321  5   SER   B CA  
4104 C C   . SER   B 5   ? 0.2692 0.3121 0.2658 -0.0833 0.0199  0.0273  5   SER   B C   
4105 O O   . SER   B 5   ? 0.2872 0.3126 0.3610 -0.0657 0.0647  0.0337  5   SER   B O   
4106 C CB  . SER   B 5   ? 0.2666 0.3243 0.2521 -0.0443 -0.0039 0.0439  5   SER   B CB  
4107 O OG  . SER   B 5   ? 0.2984 0.3503 0.3111 -0.0274 0.0041  0.0460  5   SER   B OG  
4113 N N   . PHE   B 6   ? 0.2931 0.3305 0.2407 -0.0951 0.0285  0.0358  6   PHE   B N   
4114 C CA  . PHE   B 6   ? 0.3012 0.3327 0.2043 -0.1195 0.0191  0.0138  6   PHE   B CA  
4115 C C   . PHE   B 6   ? 0.3579 0.3652 0.2698 -0.1292 0.0506  -0.0161 6   PHE   B C   
4116 O O   . PHE   B 6   ? 0.3709 0.4016 0.3132 -0.1173 0.0356  -0.0248 6   PHE   B O   
4117 C CB  . PHE   B 6   ? 0.2721 0.3137 0.1893 -0.1032 0.0051  0.0217  6   PHE   B CB  
4118 C CG  . PHE   B 6   ? 0.2375 0.2817 0.1872 -0.0989 -0.0145 0.0239  6   PHE   B CG  
4119 C CD1 . PHE   B 6   ? 0.2411 0.2559 0.1812 -0.0932 -0.0293 0.0223  6   PHE   B CD1 
4120 C CD2 . PHE   B 6   ? 0.2152 0.2789 0.1767 -0.0836 -0.0137 0.0609  6   PHE   B CD2 
4121 C CE1 . PHE   B 6   ? 0.2359 0.2355 0.1880 -0.0811 -0.0340 0.0278  6   PHE   B CE1 
4122 C CE2 . PHE   B 6   ? 0.2208 0.2678 0.2171 -0.0731 -0.0124 0.0529  6   PHE   B CE2 
4123 C CZ  . PHE   B 6   ? 0.2244 0.2446 0.2074 -0.0710 -0.0339 0.0385  6   PHE   B CZ  
4133 N N   A SER   B 7   ? 0.3925 0.3497 0.2846 -0.1567 0.0819  -0.0433 7   SER   B N   
4134 N N   B SER   B 7   ? 0.3687 0.3537 0.2961 -0.1298 0.0536  -0.0203 7   SER   B N   
4135 C CA  A SER   B 7   ? 0.4320 0.3748 0.3404 -0.1486 0.1017  -0.0558 7   SER   B CA  
4136 C CA  B SER   B 7   ? 0.3795 0.3479 0.3310 -0.1213 0.0527  -0.0235 7   SER   B CA  
4137 C C   A SER   B 7   ? 0.4317 0.3613 0.3236 -0.1524 0.1219  -0.0746 7   SER   B C   
4138 C C   B SER   B 7   ? 0.3833 0.3397 0.3392 -0.1187 0.0562  -0.0316 7   SER   B C   
4139 O O   A SER   B 7   ? 0.4423 0.3608 0.3415 -0.1574 0.1260  -0.0859 7   SER   B O   
4140 O O   B SER   B 7   ? 0.3866 0.3406 0.3520 -0.1186 0.0537  -0.0318 7   SER   B O   
4141 C CB  A SER   B 7   ? 0.4575 0.4017 0.4145 -0.1392 0.1091  -0.0468 7   SER   B CB  
4142 C CB  B SER   B 7   ? 0.3827 0.3470 0.3520 -0.1168 0.0502  -0.0189 7   SER   B CB  
4143 O OG  A SER   B 7   ? 0.4716 0.4091 0.4691 -0.1336 0.1088  -0.0365 7   SER   B OG  
4144 O OG  B SER   B 7   ? 0.3845 0.3455 0.3668 -0.1142 0.0472  -0.0148 7   SER   B OG  
4155 N N   A GLY   B 8   ? 0.4278 0.3541 0.3198 -0.1366 0.1320  -0.0807 8   GLY   B N   
4156 N N   B GLY   B 8   ? 0.3853 0.3309 0.3384 -0.1137 0.0629  -0.0414 8   GLY   B N   
4157 C CA  A GLY   B 8   ? 0.4141 0.3420 0.3187 -0.1226 0.1366  -0.0832 8   GLY   B CA  
4158 C CA  B GLY   B 8   ? 0.3839 0.3202 0.3326 -0.1096 0.0719  -0.0527 8   GLY   B CA  
4159 C C   A GLY   B 8   ? 0.3946 0.3174 0.3141 -0.1147 0.1344  -0.0785 8   GLY   B C   
4160 C C   B GLY   B 8   ? 0.3803 0.3065 0.3194 -0.1074 0.0848  -0.0639 8   GLY   B C   
4161 O O   A GLY   B 8   ? 0.4073 0.3277 0.3541 -0.1052 0.1310  -0.0980 8   GLY   B O   
4162 O O   B GLY   B 8   ? 0.3846 0.3099 0.3351 -0.1049 0.0798  -0.0656 8   GLY   B O   
4169 N N   . TYR   B 9   ? 0.3752 0.2920 0.2934 -0.1061 0.0997  -0.0834 9   TYR   B N   
4170 C CA  . TYR   B 9   ? 0.3461 0.2555 0.2539 -0.0914 0.0814  -0.0731 9   TYR   B CA  
4171 C C   . TYR   B 9   ? 0.3391 0.2533 0.2508 -0.0852 0.0555  -0.0626 9   TYR   B C   
4172 O O   . TYR   B 9   ? 0.3456 0.2699 0.2999 -0.0843 0.0637  -0.0519 9   TYR   B O   
4173 C CB  . TYR   B 9   ? 0.3340 0.2213 0.2656 -0.0866 0.0751  -0.0676 9   TYR   B CB  
4174 C CG  . TYR   B 9   ? 0.3259 0.2006 0.2662 -0.0930 0.0641  -0.0725 9   TYR   B CG  
4175 C CD1 . TYR   B 9   ? 0.3267 0.2131 0.2875 -0.1011 0.0748  -0.0560 9   TYR   B CD1 
4176 C CD2 . TYR   B 9   ? 0.3239 0.1901 0.2556 -0.0879 0.0565  -0.0718 9   TYR   B CD2 
4177 C CE1 . TYR   B 9   ? 0.3276 0.2165 0.2784 -0.1045 0.0784  -0.0712 9   TYR   B CE1 
4178 C CE2 . TYR   B 9   ? 0.3262 0.1869 0.2587 -0.0934 0.0649  -0.0606 9   TYR   B CE2 
4179 C CZ  . TYR   B 9   ? 0.3274 0.2078 0.2681 -0.1029 0.0645  -0.0834 9   TYR   B CZ  
4180 O OH  . TYR   B 9   ? 0.3209 0.2249 0.2825 -0.1087 0.0702  -0.0886 9   TYR   B OH  
4191 N N   . LEU   B 10  ? 0.3242 0.2243 0.2231 -0.0895 0.0332  -0.0616 10  LEU   B N   
4192 C CA  . LEU   B 10  ? 0.3308 0.2198 0.2191 -0.1086 -0.0083 -0.0530 10  LEU   B CA  
4193 C C   . LEU   B 10  ? 0.3158 0.2350 0.2315 -0.1021 -0.0381 -0.0338 10  LEU   B C   
4194 O O   . LEU   B 10  ? 0.2967 0.2358 0.2342 -0.0863 -0.0310 -0.0163 10  LEU   B O   
4195 C CB  . LEU   B 10  ? 0.3586 0.2220 0.2506 -0.1068 -0.0257 -0.0343 10  LEU   B CB  
4196 C CG  . LEU   B 10  ? 0.3831 0.2301 0.2921 -0.1045 -0.0662 -0.0161 10  LEU   B CG  
4197 C CD1 . LEU   B 10  ? 0.4019 0.2424 0.3243 -0.0985 -0.0643 -0.0231 10  LEU   B CD1 
4198 C CD2 . LEU   B 10  ? 0.3915 0.2349 0.3264 -0.1016 -0.0584 0.0160  10  LEU   B CD2 
4210 N N   A LYS   B 11  ? 0.3349 0.2633 0.2224 -0.0895 -0.0479 -0.0234 11  LYS   B N   
4211 N N   B LYS   B 11  ? 0.3242 0.2524 0.2577 -0.0920 -0.0390 -0.0275 11  LYS   B N   
4212 C CA  A LYS   B 11  ? 0.3538 0.2872 0.2813 -0.0786 -0.0531 -0.0252 11  LYS   B CA  
4213 C CA  B LYS   B 11  ? 0.3318 0.2679 0.2977 -0.0832 -0.0397 -0.0245 11  LYS   B CA  
4214 C C   A LYS   B 11  ? 0.3328 0.2594 0.2890 -0.0991 -0.0465 -0.0404 11  LYS   B C   
4215 C C   B LYS   B 11  ? 0.3171 0.2536 0.2877 -0.0916 -0.0441 -0.0309 11  LYS   B C   
4216 O O   A LYS   B 11  ? 0.3461 0.2746 0.3210 -0.1139 -0.0419 -0.0722 11  LYS   B O   
4217 O O   B LYS   B 11  ? 0.3227 0.2617 0.2930 -0.0942 -0.0411 -0.0390 11  LYS   B O   
4218 C CB  A LYS   B 11  ? 0.3887 0.3332 0.3584 -0.0475 -0.0556 -0.0270 11  LYS   B CB  
4219 C CB  B LYS   B 11  ? 0.3524 0.2954 0.3538 -0.0660 -0.0349 -0.0198 11  LYS   B CB  
4220 C CG  A LYS   B 11  ? 0.4193 0.3644 0.4375 -0.0297 -0.0557 -0.0282 11  LYS   B CG  
4221 C CG  B LYS   B 11  ? 0.3703 0.3167 0.4066 -0.0536 -0.0309 -0.0153 11  LYS   B CG  
4222 C CD  A LYS   B 11  ? 0.4417 0.3846 0.5040 -0.0212 -0.0534 -0.0332 11  LYS   B CD  
4223 C CD  B LYS   B 11  ? 0.3831 0.3313 0.4534 -0.0455 -0.0271 -0.0134 11  LYS   B CD  
4224 C CE  A LYS   B 11  ? 0.4572 0.3973 0.5522 -0.0191 -0.0526 -0.0379 11  LYS   B CE  
4225 C CE  B LYS   B 11  ? 0.3918 0.3410 0.4861 -0.0403 -0.0247 -0.0115 11  LYS   B CE  
4226 N NZ  A LYS   B 11  ? 0.4657 0.4046 0.5747 -0.0180 -0.0552 -0.0391 11  LYS   B NZ  
4227 N NZ  B LYS   B 11  ? 0.3965 0.3462 0.5018 -0.0376 -0.0244 -0.0099 11  LYS   B NZ  
4254 N N   . LEU   B 12  ? 0.2941 0.2357 0.2784 -0.0935 -0.0570 -0.0325 12  LEU   B N   
4255 C CA  . LEU   B 12  ? 0.2667 0.2033 0.2924 -0.0715 -0.0521 -0.0244 12  LEU   B CA  
4256 C C   . LEU   B 12  ? 0.2493 0.2059 0.2922 -0.0743 -0.0718 -0.0291 12  LEU   B C   
4257 O O   . LEU   B 12  ? 0.2517 0.2087 0.3175 -0.0740 -0.0793 -0.0255 12  LEU   B O   
4258 C CB  . LEU   B 12  ? 0.2577 0.1847 0.2894 -0.0554 -0.0429 -0.0183 12  LEU   B CB  
4259 C CG  . LEU   B 12  ? 0.2502 0.1787 0.2861 -0.0498 -0.0295 -0.0232 12  LEU   B CG  
4260 C CD1 . LEU   B 12  ? 0.2602 0.1848 0.2786 -0.0300 -0.0287 -0.0090 12  LEU   B CD1 
4261 C CD2 . LEU   B 12  ? 0.2538 0.1770 0.2932 -0.0515 -0.0203 -0.0296 12  LEU   B CD2 
4274 N N   . THR   B 13  ? 0.2342 0.2116 0.3029 -0.0714 -0.0635 -0.0448 13  THR   B N   
4275 C CA  . THR   B 13  ? 0.2377 0.2184 0.2916 -0.0814 -0.0732 -0.0216 13  THR   B CA  
4276 C C   . THR   B 13  ? 0.2845 0.2401 0.3186 -0.0935 -0.0835 -0.0112 13  THR   B C   
4277 O O   . THR   B 13  ? 0.3095 0.2374 0.3294 -0.0931 -0.0476 -0.0034 13  THR   B O   
4278 C CB  . THR   B 13  ? 0.2176 0.2143 0.2742 -0.0699 -0.0654 -0.0041 13  THR   B CB  
4279 O OG1 . THR   B 13  ? 0.2117 0.2093 0.2754 -0.0533 -0.0597 -0.0123 13  THR   B OG1 
4280 C CG2 . THR   B 13  ? 0.2267 0.2207 0.2770 -0.0656 -0.0578 0.0118  13  THR   B CG2 
4288 N N   A ASP   B 14  ? 0.2999 0.2649 0.3213 -0.1028 -0.1273 0.0050  14  ASP   B N   
4289 N N   B ASP   B 14  ? 0.2933 0.2515 0.3277 -0.0901 -0.0860 -0.0032 14  ASP   B N   
4290 C CA  A ASP   B 14  ? 0.3152 0.2835 0.3508 -0.1032 -0.1328 0.0306  14  ASP   B CA  
4291 C CA  B ASP   B 14  ? 0.3013 0.2604 0.3434 -0.0853 -0.0836 0.0057  14  ASP   B CA  
4292 C C   A ASP   B 14  ? 0.3099 0.2563 0.3097 -0.1070 -0.1239 0.0240  14  ASP   B C   
4293 C C   B ASP   B 14  ? 0.2900 0.2416 0.3056 -0.0878 -0.0970 0.0119  14  ASP   B C   
4294 O O   A ASP   B 14  ? 0.3530 0.2716 0.3256 -0.1030 -0.1175 0.0342  14  ASP   B O   
4295 O O   B ASP   B 14  ? 0.3013 0.2404 0.3052 -0.0853 -0.0961 0.0142  14  ASP   B O   
4296 C CB  A ASP   B 14  ? 0.3333 0.3307 0.4244 -0.0955 -0.1517 0.0332  14  ASP   B CB  
4297 C CB  B ASP   B 14  ? 0.3189 0.2864 0.3965 -0.0773 -0.0718 0.0024  14  ASP   B CB  
4298 C CG  A ASP   B 14  ? 0.3581 0.3716 0.5117 -0.0827 -0.1461 0.0177  14  ASP   B CG  
4299 C CG  B ASP   B 14  ? 0.3360 0.3089 0.4476 -0.0681 -0.0612 -0.0053 14  ASP   B CG  
4300 O OD1 A ASP   B 14  ? 0.3722 0.3876 0.5334 -0.0767 -0.1408 0.0069  14  ASP   B OD1 
4301 O OD1 B ASP   B 14  ? 0.3437 0.3192 0.4615 -0.0641 -0.0570 -0.0088 14  ASP   B OD1 
4302 O OD2 A ASP   B 14  ? 0.3600 0.3858 0.5571 -0.0837 -0.1424 0.0164  14  ASP   B OD2 
4303 O OD2 B ASP   B 14  ? 0.3402 0.3151 0.4669 -0.0672 -0.0587 -0.0080 14  ASP   B OD2 
4312 N N   . ASN   B 15  ? 0.2696 0.2230 0.2794 -0.0853 -0.1107 0.0223  15  ASN   B N   
4313 C CA  . ASN   B 15  ? 0.2221 0.1923 0.2599 -0.0556 -0.0866 0.0130  15  ASN   B CA  
4314 C C   . ASN   B 15  ? 0.2007 0.1705 0.2407 -0.0288 -0.0709 0.0053  15  ASN   B C   
4315 O O   . ASN   B 15  ? 0.1982 0.1624 0.2510 -0.0336 -0.0680 -0.0074 15  ASN   B O   
4316 C CB  . ASN   B 15  ? 0.2102 0.1821 0.2732 -0.0296 -0.0827 0.0184  15  ASN   B CB  
4317 C CG  . ASN   B 15  ? 0.1921 0.1663 0.2942 -0.0358 -0.0521 0.0126  15  ASN   B CG  
4318 O OD1 . ASN   B 15  ? 0.2031 0.2004 0.3443 -0.0594 -0.0572 0.0250  15  ASN   B OD1 
4319 N ND2 . ASN   B 15  ? 0.1850 0.1581 0.2746 -0.0234 -0.0240 -0.0194 15  ASN   B ND2 
4327 N N   . VAL   B 16  ? 0.1870 0.1653 0.2552 -0.0401 -0.0689 -0.0002 16  VAL   B N   
4328 C CA  . VAL   B 16  ? 0.1874 0.1657 0.2387 -0.0328 -0.0481 -0.0164 16  VAL   B CA  
4329 C C   . VAL   B 16  ? 0.1878 0.1835 0.2234 -0.0480 -0.0472 -0.0124 16  VAL   B C   
4330 O O   . VAL   B 16  ? 0.1849 0.1987 0.2512 -0.0428 -0.0413 -0.0224 16  VAL   B O   
4331 C CB  . VAL   B 16  ? 0.1881 0.1624 0.2391 -0.0208 -0.0350 -0.0215 16  VAL   B CB  
4332 C CG1 . VAL   B 16  ? 0.1950 0.1559 0.2318 -0.0109 -0.0306 -0.0173 16  VAL   B CG1 
4333 C CG2 . VAL   B 16  ? 0.1855 0.1756 0.2576 -0.0008 -0.0236 -0.0308 16  VAL   B CG2 
4343 N N   . TYR   B 17  ? 0.1971 0.1950 0.2239 -0.0473 -0.0292 -0.0220 17  TYR   B N   
4344 C CA  . TYR   B 17  ? 0.2121 0.2008 0.2166 -0.0548 -0.0490 -0.0014 17  TYR   B CA  
4345 C C   . TYR   B 17  ? 0.2086 0.1679 0.2093 -0.0526 -0.0293 -0.0119 17  TYR   B C   
4346 O O   . TYR   B 17  ? 0.2001 0.1722 0.2175 -0.0458 -0.0346 -0.0326 17  TYR   B O   
4347 C CB  . TYR   B 17  ? 0.2508 0.2575 0.2519 -0.0459 -0.0498 0.0481  17  TYR   B CB  
4348 C CG  . TYR   B 17  ? 0.2841 0.3306 0.3002 -0.0349 -0.0748 0.0678  17  TYR   B CG  
4349 C CD1 . TYR   B 17  ? 0.3014 0.3601 0.3407 -0.0358 -0.0871 0.0765  17  TYR   B CD1 
4350 C CD2 . TYR   B 17  ? 0.3095 0.3668 0.3453 -0.0219 -0.0848 0.0730  17  TYR   B CD2 
4351 C CE1 . TYR   B 17  ? 0.3240 0.3970 0.3669 -0.0209 -0.1019 0.0741  17  TYR   B CE1 
4352 C CE2 . TYR   B 17  ? 0.3288 0.3983 0.3720 -0.0083 -0.0989 0.0813  17  TYR   B CE2 
4353 C CZ  . TYR   B 17  ? 0.3382 0.4156 0.3857 -0.0051 -0.1127 0.0816  17  TYR   B CZ  
4354 O OH  . TYR   B 17  ? 0.3514 0.4318 0.4009 0.0033  -0.1240 0.0887  17  TYR   B OH  
4364 N N   . ILE   B 18  ? 0.2184 0.1788 0.2054 -0.0497 -0.0176 -0.0175 18  ILE   B N   
4365 C CA  . ILE   B 18  ? 0.2250 0.1695 0.2109 -0.0497 -0.0045 -0.0201 18  ILE   B CA  
4366 C C   . ILE   B 18  ? 0.2383 0.1739 0.2085 -0.0555 0.0050  -0.0356 18  ILE   B C   
4367 O O   . ILE   B 18  ? 0.2547 0.1855 0.2209 -0.0501 0.0071  -0.0431 18  ILE   B O   
4368 C CB  . ILE   B 18  ? 0.2250 0.1665 0.2163 -0.0598 -0.0074 -0.0189 18  ILE   B CB  
4369 C CG1 . ILE   B 18  ? 0.2259 0.1709 0.2189 -0.0536 -0.0066 -0.0091 18  ILE   B CG1 
4370 C CG2 . ILE   B 18  ? 0.2282 0.1792 0.2066 -0.0598 -0.0135 -0.0109 18  ILE   B CG2 
4371 C CD1 . ILE   B 18  ? 0.2365 0.1936 0.2416 -0.0399 -0.0225 0.0240  18  ILE   B CD1 
4383 N N   . LYS   B 19  ? 0.2393 0.1775 0.2222 -0.0389 0.0453  -0.0449 19  LYS   B N   
4384 C CA  . LYS   B 19  ? 0.2401 0.1797 0.2538 -0.0439 0.0378  -0.0563 19  LYS   B CA  
4385 C C   . LYS   B 19  ? 0.2179 0.1686 0.2714 -0.0387 0.0458  -0.0780 19  LYS   B C   
4386 O O   . LYS   B 19  ? 0.2061 0.1752 0.2408 -0.0291 0.0313  -0.0628 19  LYS   B O   
4387 C CB  . LYS   B 19  ? 0.2653 0.2017 0.2596 -0.0491 0.0564  -0.0457 19  LYS   B CB  
4388 C CG  . LYS   B 19  ? 0.2960 0.2202 0.2986 -0.0575 0.0621  -0.0457 19  LYS   B CG  
4389 C CD  . LYS   B 19  ? 0.3321 0.2511 0.3234 -0.0632 0.0752  -0.0444 19  LYS   B CD  
4390 C CE  . LYS   B 19  ? 0.3643 0.2787 0.3492 -0.0658 0.0694  -0.0509 19  LYS   B CE  
4391 N NZ  . LYS   B 19  ? 0.3844 0.2968 0.3575 -0.0673 0.0760  -0.0540 19  LYS   B NZ  
4405 N N   . ASN   B 20  ? 0.2217 0.1877 0.3185 -0.0313 0.0568  -0.0856 20  ASN   B N   
4406 C CA  . ASN   B 20  ? 0.2201 0.2037 0.3505 -0.0243 0.0594  -0.1087 20  ASN   B CA  
4407 C C   . ASN   B 20  ? 0.2169 0.2335 0.3420 -0.0327 0.0753  -0.1158 20  ASN   B C   
4408 O O   . ASN   B 20  ? 0.2413 0.2753 0.3579 -0.0488 0.0775  -0.1185 20  ASN   B O   
4409 C CB  . ASN   B 20  ? 0.2526 0.2114 0.3882 0.0089  0.0373  -0.1151 20  ASN   B CB  
4410 C CG  . ASN   B 20  ? 0.2848 0.2272 0.4025 0.0443  0.0279  -0.1291 20  ASN   B CG  
4411 O OD1 . ASN   B 20  ? 0.3210 0.2635 0.4224 0.0586  0.0251  -0.1308 20  ASN   B OD1 
4412 N ND2 . ASN   B 20  ? 0.2734 0.2243 0.4004 0.0519  0.0042  -0.1222 20  ASN   B ND2 
4419 N N   . ALA   B 21  ? 0.2177 0.2102 0.3352 -0.0395 0.0754  -0.0919 21  ALA   B N   
4420 C CA  . ALA   B 21  ? 0.2310 0.2116 0.3402 -0.0384 0.0592  -0.0720 21  ALA   B CA  
4421 C C   . ALA   B 21  ? 0.2288 0.1938 0.3127 -0.0293 0.0597  -0.0588 21  ALA   B C   
4422 O O   . ALA   B 21  ? 0.2370 0.1846 0.3061 -0.0369 0.0520  -0.0577 21  ALA   B O   
4423 C CB  . ALA   B 21  ? 0.2548 0.2395 0.3601 -0.0564 0.0610  -0.0519 21  ALA   B CB  
4429 N N   . ASP   B 22  ? 0.2109 0.1719 0.3085 -0.0246 0.0397  -0.0440 22  ASP   B N   
4430 C CA  . ASP   B 22  ? 0.2064 0.1657 0.2932 -0.0148 0.0282  -0.0281 22  ASP   B CA  
4431 C C   . ASP   B 22  ? 0.2029 0.1579 0.2312 -0.0216 0.0190  -0.0135 22  ASP   B C   
4432 O O   . ASP   B 22  ? 0.2062 0.1763 0.2352 -0.0154 0.0087  -0.0081 22  ASP   B O   
4433 C CB  . ASP   B 22  ? 0.2083 0.1788 0.3322 -0.0062 0.0258  -0.0168 22  ASP   B CB  
4434 C CG  . ASP   B 22  ? 0.2085 0.2079 0.3625 0.0081  0.0087  -0.0073 22  ASP   B CG  
4435 O OD1 . ASP   B 22  ? 0.2137 0.1942 0.3527 0.0158  -0.0092 -0.0035 22  ASP   B OD1 
4436 O OD2 . ASP   B 22  ? 0.2270 0.2353 0.4251 0.0195  -0.0222 -0.0281 22  ASP   B OD2 
4441 N N   . ILE   B 23  ? 0.1985 0.1582 0.2048 -0.0125 -0.0044 0.0108  23  ILE   B N   
4442 C CA  . ILE   B 23  ? 0.1907 0.1597 0.1799 -0.0155 -0.0046 0.0037  23  ILE   B CA  
4443 C C   . ILE   B 23  ? 0.1820 0.1619 0.1775 -0.0047 -0.0123 0.0088  23  ILE   B C   
4444 O O   . ILE   B 23  ? 0.1718 0.1549 0.1778 -0.0082 -0.0053 0.0129  23  ILE   B O   
4445 C CB  . ILE   B 23  ? 0.1815 0.1636 0.1972 -0.0212 -0.0058 0.0085  23  ILE   B CB  
4446 C CG1 . ILE   B 23  ? 0.1827 0.1655 0.2221 -0.0037 0.0022  0.0220  23  ILE   B CG1 
4447 C CG2 . ILE   B 23  ? 0.1871 0.1863 0.1993 -0.0246 0.0064  0.0058  23  ILE   B CG2 
4448 C CD1 . ILE   B 23  ? 0.1911 0.1703 0.2338 -0.0090 -0.0039 0.0193  23  ILE   B CD1 
4460 N N   . VAL   B 24  ? 0.1865 0.1584 0.1988 -0.0075 -0.0162 -0.0002 24  VAL   B N   
4461 C CA  . VAL   B 24  ? 0.1819 0.1659 0.2174 -0.0137 -0.0332 0.0037  24  VAL   B CA  
4462 C C   . VAL   B 24  ? 0.1804 0.1824 0.2125 -0.0126 -0.0174 -0.0064 24  VAL   B C   
4463 O O   . VAL   B 24  ? 0.1742 0.1922 0.2261 -0.0196 -0.0006 0.0126  24  VAL   B O   
4464 C CB  . VAL   B 24  ? 0.1890 0.1755 0.2170 -0.0066 -0.0406 0.0048  24  VAL   B CB  
4465 C CG1 . VAL   B 24  ? 0.1856 0.1845 0.2632 -0.0118 -0.0420 0.0045  24  VAL   B CG1 
4466 C CG2 . VAL   B 24  ? 0.1930 0.2059 0.2136 -0.0037 -0.0376 -0.0023 24  VAL   B CG2 
4476 N N   A GLU   B 25  ? 0.1898 0.1897 0.2263 -0.0092 -0.0036 -0.0145 25  GLU   B N   
4477 N N   B GLU   B 25  ? 0.2017 0.2058 0.2296 -0.0130 -0.0082 -0.0034 25  GLU   B N   
4478 C CA  A GLU   B 25  ? 0.2058 0.2124 0.2482 -0.0015 0.0098  -0.0209 25  GLU   B CA  
4479 C CA  B GLU   B 25  ? 0.2232 0.2316 0.2525 -0.0129 -0.0004 -0.0016 25  GLU   B CA  
4480 C C   A GLU   B 25  ? 0.2047 0.1944 0.1992 -0.0184 0.0125  -0.0124 25  GLU   B C   
4481 C C   B GLU   B 25  ? 0.2235 0.2301 0.2285 -0.0184 0.0023  0.0031  25  GLU   B C   
4482 O O   A GLU   B 25  ? 0.2127 0.2086 0.2216 -0.0168 0.0148  -0.0090 25  GLU   B O   
4483 O O   B GLU   B 25  ? 0.2279 0.2352 0.2312 -0.0158 0.0033  0.0054  25  GLU   B O   
4484 C CB  A GLU   B 25  ? 0.2445 0.2672 0.3169 0.0224  0.0150  -0.0246 25  GLU   B CB  
4485 C CB  B GLU   B 25  ? 0.2475 0.2610 0.3008 -0.0065 0.0032  -0.0027 25  GLU   B CB  
4486 C CG  A GLU   B 25  ? 0.2874 0.3311 0.4192 0.0271  0.0085  -0.0250 25  GLU   B CG  
4487 C CG  B GLU   B 25  ? 0.2705 0.2903 0.3567 -0.0044 0.0038  -0.0048 25  GLU   B CG  
4488 C CD  A GLU   B 25  ? 0.3293 0.3888 0.5013 0.0215  -0.0027 -0.0245 25  GLU   B CD  
4489 C CD  B GLU   B 25  ? 0.2908 0.3173 0.4050 -0.0061 0.0025  -0.0066 25  GLU   B CD  
4490 O OE1 A GLU   B 25  ? 0.3472 0.4121 0.5289 0.0249  0.0032  -0.0170 25  GLU   B OE1 
4491 O OE1 B GLU   B 25  ? 0.2999 0.3284 0.4214 -0.0052 0.0045  -0.0067 25  GLU   B OE1 
4492 O OE2 A GLU   B 25  ? 0.3426 0.4042 0.5262 0.0216  -0.0173 -0.0354 25  GLU   B OE2 
4493 O OE2 B GLU   B 25  ? 0.2962 0.3274 0.4196 -0.0060 -0.0014 -0.0091 25  GLU   B OE2 
4506 N N   A GLU   B 26  ? 0.2041 0.1760 0.1879 -0.0373 0.0175  -0.0042 26  GLU   B N   
4507 N N   B GLU   B 26  ? 0.2192 0.2242 0.2192 -0.0271 0.0050  0.0052  26  GLU   B N   
4508 C CA  A GLU   B 26  ? 0.2153 0.1994 0.2151 -0.0435 0.0044  0.0097  26  GLU   B CA  
4509 C CA  B GLU   B 26  ? 0.2151 0.2236 0.2177 -0.0341 0.0065  0.0066  26  GLU   B CA  
4510 C C   A GLU   B 26  ? 0.1869 0.1991 0.1940 -0.0377 0.0151  0.0236  26  GLU   B C   
4511 C C   B GLU   B 26  ? 0.1904 0.2093 0.1965 -0.0339 0.0103  0.0166  26  GLU   B C   
4512 O O   A GLU   B 26  ? 0.2019 0.2265 0.1979 -0.0313 0.0045  0.0202  26  GLU   B O   
4513 O O   B GLU   B 26  ? 0.1945 0.2171 0.1940 -0.0320 0.0074  0.0161  26  GLU   B O   
4514 C CB  A GLU   B 26  ? 0.2492 0.2191 0.2351 -0.0545 0.0227  0.0354  26  GLU   B CB  
4515 C CB  B GLU   B 26  ? 0.2332 0.2358 0.2309 -0.0409 0.0154  0.0038  26  GLU   B CB  
4516 C CG  A GLU   B 26  ? 0.2869 0.2643 0.3031 -0.0534 0.0239  0.0068  26  GLU   B CG  
4517 C CG  B GLU   B 26  ? 0.2506 0.2524 0.2578 -0.0458 0.0239  -0.0078 26  GLU   B CG  
4518 C CD  A GLU   B 26  ? 0.3038 0.2912 0.3238 -0.0698 0.0342  -0.0269 26  GLU   B CD  
4519 C CD  B GLU   B 26  ? 0.2607 0.2639 0.2653 -0.0560 0.0385  -0.0197 26  GLU   B CD  
4520 O OE1 A GLU   B 26  ? 0.3127 0.2845 0.3486 -0.0803 0.0707  -0.0290 26  GLU   B OE1 
4521 O OE1 B GLU   B 26  ? 0.2677 0.2630 0.2624 -0.0580 0.0613  -0.0199 26  GLU   B OE1 
4522 O OE2 A GLU   B 26  ? 0.3098 0.3288 0.3682 -0.0676 0.0212  -0.0302 26  GLU   B OE2 
4523 O OE2 B GLU   B 26  ? 0.2624 0.2765 0.2929 -0.0597 0.0367  -0.0152 26  GLU   B OE2 
4536 N N   . ALA   B 27  ? 0.1671 0.1897 0.1884 -0.0332 0.0125  0.0238  27  ALA   B N   
4537 C CA  . ALA   B 27  ? 0.1752 0.1775 0.1939 -0.0159 -0.0007 0.0340  27  ALA   B CA  
4538 C C   . ALA   B 27  ? 0.1833 0.1872 0.2118 -0.0089 0.0044  0.0406  27  ALA   B C   
4539 O O   . ALA   B 27  ? 0.1871 0.2017 0.2225 -0.0041 0.0023  0.0540  27  ALA   B O   
4540 C CB  . ALA   B 27  ? 0.1848 0.1636 0.2056 -0.0193 -0.0040 0.0258  27  ALA   B CB  
4547 N N   . LYS   B 28  ? 0.1844 0.2029 0.2548 -0.0193 0.0053  0.0556  28  LYS   B N   
4548 C CA  . LYS   B 28  ? 0.1990 0.2467 0.2759 -0.0120 0.0481  0.0915  28  LYS   B CA  
4549 C C   . LYS   B 28  ? 0.2294 0.2753 0.2698 -0.0033 0.0556  0.0843  28  LYS   B C   
4550 O O   . LYS   B 28  ? 0.2418 0.2869 0.2856 -0.0041 0.0612  0.0872  28  LYS   B O   
4551 C CB  . LYS   B 28  ? 0.2172 0.2804 0.3382 0.0071  0.0732  0.1000  28  LYS   B CB  
4552 C CG  . LYS   B 28  ? 0.2467 0.3310 0.3805 0.0171  0.0788  0.1086  28  LYS   B CG  
4553 C CD  . LYS   B 28  ? 0.3059 0.3963 0.4510 0.0211  0.0844  0.1058  28  LYS   B CD  
4554 C CE  . LYS   B 28  ? 0.3519 0.4436 0.5125 0.0276  0.0809  0.1078  28  LYS   B CE  
4555 N NZ  . LYS   B 28  ? 0.3809 0.4646 0.5395 0.0357  0.0769  0.1101  28  LYS   B NZ  
4569 N N   A LYS   B 29  ? 0.2447 0.2965 0.2782 0.0073  0.0585  0.0687  29  LYS   B N   
4570 N N   B LYS   B 29  ? 0.2510 0.2953 0.2879 -0.0007 0.0448  0.0722  29  LYS   B N   
4571 C CA  A LYS   B 29  ? 0.2870 0.3215 0.2875 0.0091  0.0564  0.0668  29  LYS   B CA  
4572 C CA  B LYS   B 29  ? 0.2783 0.3153 0.3076 -0.0011 0.0343  0.0633  29  LYS   B CA  
4573 C C   A LYS   B 29  ? 0.2856 0.3195 0.2538 0.0081  0.0371  0.0813  29  LYS   B C   
4574 C C   B LYS   B 29  ? 0.2750 0.3115 0.2750 -0.0024 0.0270  0.0706  29  LYS   B C   
4575 O O   A LYS   B 29  ? 0.3020 0.3471 0.2800 0.0140  0.0496  0.0813  29  LYS   B O   
4576 O O   B LYS   B 29  ? 0.2816 0.3211 0.2853 -0.0010 0.0305  0.0707  29  LYS   B O   
4577 C CB  A LYS   B 29  ? 0.3406 0.3545 0.3758 0.0100  0.0501  0.0438  29  LYS   B CB  
4578 C CB  B LYS   B 29  ? 0.3108 0.3397 0.3708 0.0001  0.0260  0.0460  29  LYS   B CB  
4579 C CG  A LYS   B 29  ? 0.3816 0.3782 0.4700 0.0092  0.0457  0.0324  29  LYS   B CG  
4580 C CG  B LYS   B 29  ? 0.3380 0.3590 0.4326 0.0008  0.0192  0.0332  29  LYS   B CG  
4581 C CD  A LYS   B 29  ? 0.4143 0.3942 0.5367 0.0064  0.0528  0.0215  29  LYS   B CD  
4582 C CD  B LYS   B 29  ? 0.3590 0.3741 0.4798 0.0007  0.0172  0.0226  29  LYS   B CD  
4583 C CE  A LYS   B 29  ? 0.4410 0.4057 0.5808 0.0018  0.0633  0.0154  29  LYS   B CE  
4584 C CE  B LYS   B 29  ? 0.3743 0.3852 0.5124 0.0001  0.0176  0.0159  29  LYS   B CE  
4585 N NZ  A LYS   B 29  ? 0.4502 0.4127 0.6078 -0.0005 0.0673  0.0119  29  LYS   B NZ  
4586 N NZ  B LYS   B 29  ? 0.3816 0.3902 0.5319 -0.0005 0.0180  0.0123  29  LYS   B NZ  
4613 N N   . VAL   B 30  ? 0.2614 0.2994 0.2450 -0.0068 0.0209  0.0733  30  VAL   B N   
4614 C CA  . VAL   B 30  ? 0.2418 0.2804 0.2696 -0.0217 -0.0097 0.0791  30  VAL   B CA  
4615 C C   . VAL   B 30  ? 0.2155 0.2715 0.2456 -0.0264 -0.0188 0.0878  30  VAL   B C   
4616 O O   . VAL   B 30  ? 0.2236 0.2907 0.2488 -0.0239 -0.0156 0.0974  30  VAL   B O   
4617 C CB  . VAL   B 30  ? 0.2420 0.2717 0.3234 -0.0444 -0.0320 0.0806  30  VAL   B CB  
4618 C CG1 . VAL   B 30  ? 0.2538 0.2865 0.3356 -0.0399 -0.0146 0.0626  30  VAL   B CG1 
4619 C CG2 . VAL   B 30  ? 0.2565 0.2670 0.3546 -0.0601 -0.0479 0.0632  30  VAL   B CG2 
4630 N N   A LYS   B 31  ? 0.1964 0.2408 0.2703 -0.0453 -0.0135 0.0898  31  LYS   B N   
4631 N N   B LYS   B 31  ? 0.2192 0.2583 0.2563 -0.0305 -0.0215 0.0757  31  LYS   B N   
4632 C CA  A LYS   B 31  ? 0.1749 0.2458 0.3101 -0.0515 -0.0117 0.1001  31  LYS   B CA  
4633 C CA  B LYS   B 31  ? 0.2240 0.2518 0.2750 -0.0327 -0.0273 0.0650  31  LYS   B CA  
4634 C C   A LYS   B 31  ? 0.1673 0.2038 0.2830 -0.0424 -0.0337 0.0884  31  LYS   B C   
4635 C C   B LYS   B 31  ? 0.2049 0.2142 0.2457 -0.0368 -0.0389 0.0610  31  LYS   B C   
4636 O O   A LYS   B 31  ? 0.1636 0.2063 0.3086 -0.0358 -0.0247 0.1003  31  LYS   B O   
4637 O O   B LYS   B 31  ? 0.2070 0.2159 0.2435 -0.0371 -0.0411 0.0615  31  LYS   B O   
4638 C CB  A LYS   B 31  ? 0.1864 0.3019 0.3689 -0.0423 0.0176  0.1098  31  LYS   B CB  
4639 C CB  B LYS   B 31  ? 0.2498 0.2827 0.3202 -0.0274 -0.0196 0.0559  31  LYS   B CB  
4640 C CG  A LYS   B 31  ? 0.2152 0.3533 0.4141 -0.0427 0.0303  0.1158  31  LYS   B CG  
4641 C CG  B LYS   B 31  ? 0.2729 0.3083 0.3612 -0.0251 -0.0134 0.0451  31  LYS   B CG  
4642 C CD  A LYS   B 31  ? 0.2530 0.4112 0.4638 -0.0389 0.0198  0.1037  31  LYS   B CD  
4643 C CD  B LYS   B 31  ? 0.2931 0.3312 0.4010 -0.0236 -0.0100 0.0350  31  LYS   B CD  
4644 C CE  A LYS   B 31  ? 0.2837 0.4498 0.5123 -0.0325 0.0036  0.0886  31  LYS   B CE  
4645 C CE  B LYS   B 31  ? 0.3093 0.3471 0.4340 -0.0216 -0.0083 0.0285  31  LYS   B CE  
4646 N NZ  A LYS   B 31  ? 0.2957 0.4727 0.5268 -0.0250 -0.0085 0.0769  31  LYS   B NZ  
4647 N NZ  B LYS   B 31  ? 0.3148 0.3555 0.4484 -0.0193 -0.0091 0.0238  31  LYS   B NZ  
4674 N N   . PRO   B 32  ? 0.1858 0.1761 0.2201 -0.0416 -0.0458 0.0554  32  PRO   B N   
4675 C CA  . PRO   B 32  ? 0.2021 0.1698 0.1735 -0.0429 -0.0445 0.0281  32  PRO   B CA  
4676 C C   . PRO   B 32  ? 0.2083 0.1562 0.1773 -0.0522 -0.0654 0.0394  32  PRO   B C   
4677 O O   . PRO   B 32  ? 0.2133 0.1640 0.2185 -0.0491 -0.0811 0.0346  32  PRO   B O   
4678 C CB  . PRO   B 32  ? 0.2050 0.1687 0.1841 -0.0544 -0.0292 0.0116  32  PRO   B CB  
4679 C CG  . PRO   B 32  ? 0.2224 0.1514 0.1847 -0.0377 -0.0580 0.0233  32  PRO   B CG  
4680 C CD  . PRO   B 32  ? 0.2055 0.1641 0.2159 -0.0323 -0.0618 0.0359  32  PRO   B CD  
4688 N N   . THR   B 33  ? 0.2152 0.1580 0.1653 -0.0425 -0.0555 0.0321  33  THR   B N   
4689 C CA  . THR   B 33  ? 0.2226 0.1609 0.1669 -0.0446 -0.0523 0.0363  33  THR   B CA  
4690 C C   . THR   B 33  ? 0.2154 0.1450 0.1676 -0.0451 -0.0617 0.0242  33  THR   B C   
4691 O O   . THR   B 33  ? 0.2317 0.1507 0.1824 -0.0523 -0.0631 0.0250  33  THR   B O   
4692 C CB  . THR   B 33  ? 0.2353 0.1750 0.1622 -0.0326 -0.0651 0.0253  33  THR   B CB  
4693 O OG1 . THR   B 33  ? 0.2197 0.1758 0.1812 -0.0328 -0.0681 0.0352  33  THR   B OG1 
4694 C CG2 . THR   B 33  ? 0.2559 0.1818 0.1951 -0.0305 -0.0595 0.0319  33  THR   B CG2 
4702 N N   . VAL   B 34  ? 0.1981 0.1420 0.1566 -0.0454 -0.0464 0.0180  34  VAL   B N   
4703 C CA  . VAL   B 34  ? 0.1836 0.1442 0.1402 -0.0309 -0.0428 0.0152  34  VAL   B CA  
4704 C C   . VAL   B 34  ? 0.1702 0.1369 0.1292 -0.0334 -0.0277 0.0057  34  VAL   B C   
4705 O O   . VAL   B 34  ? 0.1868 0.1448 0.1459 -0.0256 -0.0422 0.0088  34  VAL   B O   
4706 C CB  . VAL   B 34  ? 0.1909 0.1542 0.1762 -0.0100 -0.0335 0.0140  34  VAL   B CB  
4707 C CG1 . VAL   B 34  ? 0.1752 0.1688 0.1850 -0.0082 -0.0092 0.0053  34  VAL   B CG1 
4708 C CG2 . VAL   B 34  ? 0.1970 0.1502 0.2095 -0.0081 -0.0391 0.0127  34  VAL   B CG2 
4718 N N   . VAL   B 35  ? 0.1614 0.1325 0.1192 -0.0337 -0.0167 0.0127  35  VAL   B N   
4719 C CA  . VAL   B 35  ? 0.1590 0.1339 0.1191 -0.0222 -0.0162 0.0150  35  VAL   B CA  
4720 C C   . VAL   B 35  ? 0.1430 0.1276 0.1257 -0.0212 -0.0226 0.0079  35  VAL   B C   
4721 O O   . VAL   B 35  ? 0.1511 0.1286 0.1407 -0.0237 -0.0106 -0.0057 35  VAL   B O   
4722 C CB  . VAL   B 35  ? 0.1493 0.1525 0.1399 -0.0227 -0.0035 0.0098  35  VAL   B CB  
4723 C CG1 . VAL   B 35  ? 0.1483 0.1714 0.1749 -0.0291 -0.0035 -0.0006 35  VAL   B CG1 
4724 C CG2 . VAL   B 35  ? 0.1636 0.1494 0.1672 -0.0153 0.0006  0.0027  35  VAL   B CG2 
4734 N N   . VAL   B 36  ? 0.1389 0.1332 0.1392 -0.0195 -0.0168 0.0092  36  VAL   B N   
4735 C CA  . VAL   B 36  ? 0.1397 0.1238 0.1290 -0.0132 -0.0139 0.0067  36  VAL   B CA  
4736 C C   . VAL   B 36  ? 0.1355 0.1246 0.1224 -0.0100 -0.0084 -0.0003 36  VAL   B C   
4737 O O   . VAL   B 36  ? 0.1437 0.1406 0.1483 -0.0121 -0.0044 -0.0060 36  VAL   B O   
4738 C CB  . VAL   B 36  ? 0.1397 0.1362 0.1346 -0.0182 -0.0120 0.0131  36  VAL   B CB  
4739 C CG1 . VAL   B 36  ? 0.1332 0.1425 0.1562 -0.0223 -0.0129 0.0079  36  VAL   B CG1 
4740 C CG2 . VAL   B 36  ? 0.1534 0.1472 0.1403 -0.0183 -0.0234 0.0126  36  VAL   B CG2 
4750 N N   . ASN   B 37  ? 0.1408 0.1333 0.1258 -0.0038 -0.0111 0.0051  37  ASN   B N   
4751 C CA  . ASN   B 37  ? 0.1415 0.1320 0.1275 -0.0006 -0.0189 0.0116  37  ASN   B CA  
4752 C C   . ASN   B 37  ? 0.1435 0.1398 0.1411 0.0060  -0.0164 0.0112  37  ASN   B C   
4753 O O   . ASN   B 37  ? 0.1517 0.1431 0.1483 0.0031  -0.0061 0.0101  37  ASN   B O   
4754 C CB  . ASN   B 37  ? 0.1455 0.1333 0.1183 -0.0034 -0.0217 0.0065  37  ASN   B CB  
4755 C CG  . ASN   B 37  ? 0.1563 0.1344 0.1400 -0.0040 -0.0119 0.0059  37  ASN   B CG  
4756 O OD1 . ASN   B 37  ? 0.1538 0.1391 0.1605 0.0073  -0.0214 0.0001  37  ASN   B OD1 
4757 N ND2 . ASN   B 37  ? 0.1531 0.1292 0.1377 0.0013  -0.0210 0.0026  37  ASN   B ND2 
4764 N N   . ALA   B 38  ? 0.1554 0.1318 0.1425 0.0071  0.0004  0.0112  38  ALA   B N   
4765 C CA  . ALA   B 38  ? 0.1569 0.1314 0.1493 0.0007  0.0024  0.0082  38  ALA   B CA  
4766 C C   . ALA   B 38  ? 0.1537 0.1337 0.1543 -0.0028 -0.0053 0.0148  38  ALA   B C   
4767 O O   . ALA   B 38  ? 0.1777 0.1466 0.1561 0.0022  -0.0054 0.0120  38  ALA   B O   
4768 C CB  . ALA   B 38  ? 0.1828 0.1491 0.1498 -0.0097 0.0115  0.0010  38  ALA   B CB  
4774 N N   . ALA   B 39  ? 0.1491 0.1401 0.1359 0.0076  -0.0105 0.0022  39  ALA   B N   
4775 C CA  . ALA   B 39  ? 0.1624 0.1382 0.1374 0.0096  -0.0090 0.0006  39  ALA   B CA  
4776 C C   . ALA   B 39  ? 0.1683 0.1462 0.1224 0.0130  -0.0068 0.0006  39  ALA   B C   
4777 O O   . ALA   B 39  ? 0.1841 0.1593 0.1526 -0.0060 -0.0158 0.0052  39  ALA   B O   
4778 C CB  . ALA   B 39  ? 0.1543 0.1424 0.1573 -0.0058 -0.0071 -0.0040 39  ALA   B CB  
4784 N N   . ASN   B 40  ? 0.1697 0.1772 0.1153 0.0007  -0.0030 -0.0082 40  ASN   B N   
4785 C CA  . ASN   B 40  ? 0.1776 0.1817 0.1315 0.0025  -0.0101 -0.0065 40  ASN   B CA  
4786 C C   . ASN   B 40  ? 0.1850 0.1806 0.1203 0.0075  -0.0105 0.0061  40  ASN   B C   
4787 O O   . ASN   B 40  ? 0.1865 0.1719 0.1238 0.0038  -0.0113 0.0012  40  ASN   B O   
4788 C CB  . ASN   B 40  ? 0.1874 0.1721 0.1684 0.0089  -0.0120 0.0106  40  ASN   B CB  
4789 C CG  . ASN   B 40  ? 0.1984 0.1774 0.1842 0.0031  -0.0259 0.0267  40  ASN   B CG  
4790 O OD1 . ASN   B 40  ? 0.2050 0.1744 0.2705 0.0063  -0.0372 0.0290  40  ASN   B OD1 
4791 N ND2 . ASN   B 40  ? 0.2000 0.1768 0.1908 -0.0026 -0.0185 0.0260  40  ASN   B ND2 
4798 N N   . VAL   B 41  ? 0.2014 0.1738 0.1297 0.0196  0.0050  -0.0049 41  VAL   B N   
4799 C CA  . VAL   B 41  ? 0.2040 0.1840 0.1518 0.0126  -0.0023 -0.0062 41  VAL   B CA  
4800 C C   . VAL   B 41  ? 0.1998 0.1844 0.1374 0.0189  -0.0078 -0.0059 41  VAL   B C   
4801 O O   . VAL   B 41  ? 0.1934 0.1886 0.1546 0.0145  -0.0107 -0.0116 41  VAL   B O   
4802 C CB  . VAL   B 41  ? 0.2245 0.2030 0.1738 -0.0018 0.0189  -0.0163 41  VAL   B CB  
4803 C CG1 . VAL   B 41  ? 0.2295 0.2069 0.1843 -0.0102 0.0304  -0.0194 41  VAL   B CG1 
4804 C CG2 . VAL   B 41  ? 0.2213 0.2181 0.1775 -0.0139 0.0155  -0.0177 41  VAL   B CG2 
4814 N N   . TYR   B 42  ? 0.2107 0.1789 0.1392 0.0254  -0.0208 0.0002  42  TYR   B N   
4815 C CA  . TYR   B 42  ? 0.2207 0.1954 0.1251 0.0201  -0.0313 -0.0103 42  TYR   B CA  
4816 C C   . TYR   B 42  ? 0.1989 0.1766 0.1259 0.0192  -0.0228 -0.0082 42  TYR   B C   
4817 O O   . TYR   B 42  ? 0.1967 0.1886 0.1869 0.0087  -0.0251 -0.0121 42  TYR   B O   
4818 C CB  . TYR   B 42  ? 0.2351 0.2219 0.1683 0.0223  -0.0392 -0.0014 42  TYR   B CB  
4819 C CG  . TYR   B 42  ? 0.2357 0.2334 0.1561 0.0089  -0.0285 0.0101  42  TYR   B CG  
4820 C CD1 . TYR   B 42  ? 0.2290 0.2267 0.1403 -0.0001 -0.0141 0.0132  42  TYR   B CD1 
4821 C CD2 . TYR   B 42  ? 0.2411 0.2451 0.1978 0.0095  -0.0220 0.0193  42  TYR   B CD2 
4822 C CE1 . TYR   B 42  ? 0.2387 0.2426 0.1457 0.0043  -0.0144 0.0123  42  TYR   B CE1 
4823 C CE2 . TYR   B 42  ? 0.2414 0.2586 0.1978 0.0107  0.0084  0.0373  42  TYR   B CE2 
4824 C CZ  . TYR   B 42  ? 0.2512 0.2651 0.1814 0.0274  0.0147  0.0162  42  TYR   B CZ  
4825 O OH  . TYR   B 42  ? 0.2857 0.2912 0.2090 0.0412  0.0188  0.0261  42  TYR   B OH  
4835 N N   . LEU   B 43  ? 0.1824 0.1556 0.1288 0.0066  -0.0155 -0.0046 43  LEU   B N   
4836 C CA  . LEU   B 43  ? 0.1798 0.1635 0.1166 -0.0029 -0.0214 0.0032  43  LEU   B CA  
4837 C C   . LEU   B 43  ? 0.1859 0.1624 0.1379 0.0026  -0.0265 0.0015  43  LEU   B C   
4838 O O   . LEU   B 43  ? 0.1774 0.1690 0.1757 0.0046  -0.0222 0.0001  43  LEU   B O   
4839 C CB  . LEU   B 43  ? 0.1710 0.1600 0.1524 -0.0055 -0.0180 -0.0002 43  LEU   B CB  
4840 C CG  . LEU   B 43  ? 0.1726 0.1548 0.1678 -0.0056 -0.0233 -0.0028 43  LEU   B CG  
4841 C CD1 . LEU   B 43  ? 0.1826 0.1640 0.2005 -0.0045 -0.0384 -0.0077 43  LEU   B CD1 
4842 C CD2 . LEU   B 43  ? 0.1770 0.1544 0.1833 -0.0096 -0.0292 -0.0004 43  LEU   B CD2 
4854 N N   . LYS   B 44  ? 0.1914 0.1621 0.1476 0.0156  -0.0190 -0.0059 44  LYS   B N   
4855 C CA  . LYS   B 44  ? 0.2020 0.1754 0.1385 0.0140  -0.0099 -0.0033 44  LYS   B CA  
4856 C C   . LYS   B 44  ? 0.1908 0.1720 0.1352 0.0134  -0.0204 0.0064  44  LYS   B C   
4857 O O   . LYS   B 44  ? 0.2036 0.1649 0.1735 0.0013  -0.0089 0.0099  44  LYS   B O   
4858 C CB  . LYS   B 44  ? 0.2289 0.1966 0.1585 0.0197  -0.0258 -0.0068 44  LYS   B CB  
4859 C CG  . LYS   B 44  ? 0.2680 0.2242 0.1918 0.0055  -0.0588 0.0079  44  LYS   B CG  
4860 C CD  . LYS   B 44  ? 0.3064 0.2442 0.2722 -0.0196 -0.0685 -0.0011 44  LYS   B CD  
4861 C CE  . LYS   B 44  ? 0.3421 0.2717 0.3263 -0.0267 -0.0771 0.0109  44  LYS   B CE  
4862 N NZ  . LYS   B 44  ? 0.3496 0.2739 0.3519 -0.0242 -0.0971 0.0350  44  LYS   B NZ  
4876 N N   . HIS   B 45  ? 0.1844 0.1743 0.1252 0.0039  -0.0175 0.0128  45  HIS   B N   
4877 C CA  . HIS   B 45  ? 0.1843 0.1654 0.1375 0.0057  -0.0141 -0.0025 45  HIS   B CA  
4878 C C   . HIS   B 45  ? 0.2034 0.1891 0.1767 0.0185  -0.0204 -0.0063 45  HIS   B C   
4879 O O   . HIS   B 45  ? 0.2221 0.2075 0.2470 0.0466  0.0012  -0.0061 45  HIS   B O   
4880 C CB  . HIS   B 45  ? 0.1721 0.1690 0.1519 0.0035  -0.0100 -0.0106 45  HIS   B CB  
4881 C CG  . HIS   B 45  ? 0.1661 0.1656 0.1460 -0.0102 -0.0184 -0.0069 45  HIS   B CG  
4882 N ND1 . HIS   B 45  ? 0.1775 0.1603 0.1542 -0.0021 -0.0130 -0.0046 45  HIS   B ND1 
4883 C CD2 . HIS   B 45  ? 0.1767 0.1738 0.1680 -0.0165 -0.0282 -0.0003 45  HIS   B CD2 
4884 C CE1 . HIS   B 45  ? 0.1883 0.1470 0.1472 0.0069  -0.0263 -0.0004 45  HIS   B CE1 
4885 N NE2 . HIS   B 45  ? 0.1923 0.1614 0.1548 -0.0018 -0.0233 -0.0032 45  HIS   B NE2 
4893 N N   A GLY   B 46  ? 0.2130 0.1838 0.2126 0.0232  -0.0480 0.0065  46  GLY   B N   
4894 N N   B GLY   B 46  ? 0.2133 0.1939 0.2042 0.0182  -0.0324 0.0039  46  GLY   B N   
4895 C CA  A GLY   B 46  ? 0.2378 0.1914 0.2599 0.0174  -0.0583 0.0019  46  GLY   B CA  
4896 C CA  B GLY   B 46  ? 0.2263 0.2014 0.2321 0.0148  -0.0405 0.0093  46  GLY   B CA  
4897 C C   A GLY   B 46  ? 0.2459 0.2099 0.3122 0.0217  -0.0523 0.0058  46  GLY   B C   
4898 C C   B GLY   B 46  ? 0.2359 0.2122 0.2615 0.0158  -0.0428 0.0170  46  GLY   B C   
4899 O O   A GLY   B 46  ? 0.2606 0.2302 0.4179 0.0229  -0.0226 -0.0335 46  GLY   B O   
4900 O O   B GLY   B 46  ? 0.2410 0.2181 0.2770 0.0211  -0.0380 0.0257  46  GLY   B O   
4907 N N   . GLY   B 47  ? 0.2408 0.2191 0.2789 0.0021  -0.0376 0.0061  47  GLY   B N   
4908 C CA  . GLY   B 47  ? 0.2180 0.1980 0.2379 0.0017  -0.0309 0.0059  47  GLY   B CA  
4909 C C   . GLY   B 47  ? 0.1872 0.1887 0.1924 0.0003  -0.0106 0.0069  47  GLY   B C   
4910 O O   . GLY   B 47  ? 0.1890 0.1680 0.2075 0.0055  -0.0182 0.0175  47  GLY   B O   
4915 N N   . GLY   B 48  ? 0.1742 0.1779 0.1976 -0.0021 -0.0160 0.0326  48  GLY   B N   
4916 C CA  . GLY   B 48  ? 0.1757 0.1678 0.1961 -0.0094 -0.0096 0.0201  48  GLY   B CA  
4917 C C   . GLY   B 48  ? 0.1657 0.1510 0.1831 -0.0025 0.0052  0.0110  48  GLY   B C   
4918 O O   . GLY   B 48  ? 0.1551 0.1423 0.2166 0.0040  -0.0108 0.0089  48  GLY   B O   
4922 N N   . VAL   B 49  ? 0.1654 0.1642 0.1704 0.0164  -0.0058 0.0080  49  VAL   B N   
4923 C CA  . VAL   B 49  ? 0.1572 0.1692 0.1516 0.0110  -0.0115 -0.0103 49  VAL   B CA  
4924 C C   . VAL   B 49  ? 0.1577 0.1494 0.1358 0.0057  -0.0113 -0.0011 49  VAL   B C   
4925 O O   . VAL   B 49  ? 0.1716 0.1526 0.1582 0.0047  -0.0082 0.0075  49  VAL   B O   
4926 C CB  . VAL   B 49  ? 0.1620 0.1783 0.1839 0.0006  -0.0231 -0.0044 49  VAL   B CB  
4927 C CG1 . VAL   B 49  ? 0.1613 0.1786 0.1826 0.0071  -0.0400 0.0002  49  VAL   B CG1 
4928 C CG2 . VAL   B 49  ? 0.1843 0.2055 0.2239 -0.0111 -0.0396 -0.0161 49  VAL   B CG2 
4938 N N   . ALA   B 50  ? 0.1512 0.1484 0.1458 0.0008  -0.0048 0.0038  50  ALA   B N   
4939 C CA  . ALA   B 50  ? 0.1515 0.1428 0.1495 0.0091  -0.0089 0.0049  50  ALA   B CA  
4940 C C   . ALA   B 50  ? 0.1497 0.1517 0.1461 0.0002  -0.0030 -0.0016 50  ALA   B C   
4941 O O   . ALA   B 50  ? 0.1566 0.1566 0.1557 -0.0057 -0.0002 0.0038  50  ALA   B O   
4942 C CB  . ALA   B 50  ? 0.1662 0.1390 0.1694 -0.0015 -0.0129 0.0088  50  ALA   B CB  
4948 N N   . GLY   B 51  ? 0.1537 0.1579 0.1648 0.0137  -0.0199 0.0153  51  GLY   B N   
4949 C CA  . GLY   B 51  ? 0.1589 0.1553 0.1808 0.0171  -0.0200 0.0043  51  GLY   B CA  
4950 C C   . GLY   B 51  ? 0.1566 0.1551 0.1779 0.0191  -0.0152 0.0062  51  GLY   B C   
4951 O O   . GLY   B 51  ? 0.1525 0.1691 0.2038 0.0072  -0.0060 0.0023  51  GLY   B O   
4955 N N   . ALA   B 52  ? 0.1533 0.1535 0.1727 0.0115  -0.0084 0.0084  52  ALA   B N   
4956 C CA  . ALA   B 52  ? 0.1646 0.1627 0.1786 0.0135  -0.0064 -0.0072 52  ALA   B CA  
4957 C C   . ALA   B 52  ? 0.1573 0.1476 0.1589 0.0059  -0.0054 0.0002  52  ALA   B C   
4958 O O   . ALA   B 52  ? 0.1598 0.1565 0.1942 0.0037  -0.0030 -0.0013 52  ALA   B O   
4959 C CB  . ALA   B 52  ? 0.1810 0.1666 0.1877 0.0113  -0.0060 -0.0063 52  ALA   B CB  
4965 N N   . LEU   B 53  ? 0.1542 0.1498 0.1495 0.0157  -0.0106 0.0061  53  LEU   B N   
4966 C CA  . LEU   B 53  ? 0.1538 0.1610 0.1408 0.0124  -0.0131 0.0003  53  LEU   B CA  
4967 C C   . LEU   B 53  ? 0.1582 0.1498 0.1501 0.0094  -0.0025 0.0119  53  LEU   B C   
4968 O O   . LEU   B 53  ? 0.1578 0.1608 0.1746 -0.0026 0.0004  0.0179  53  LEU   B O   
4969 C CB  . LEU   B 53  ? 0.1580 0.1631 0.1732 0.0146  -0.0108 0.0100  53  LEU   B CB  
4970 C CG  . LEU   B 53  ? 0.1551 0.1726 0.1763 0.0061  -0.0103 0.0098  53  LEU   B CG  
4971 C CD1 . LEU   B 53  ? 0.1620 0.1930 0.2029 0.0219  -0.0095 0.0053  53  LEU   B CD1 
4972 C CD2 . LEU   B 53  ? 0.1731 0.2104 0.2010 -0.0064 -0.0187 -0.0178 53  LEU   B CD2 
4984 N N   . ASN   B 54  ? 0.1576 0.1460 0.1531 0.0031  -0.0038 0.0019  54  ASN   B N   
4985 C CA  . ASN   B 54  ? 0.1627 0.1593 0.1548 0.0104  -0.0078 -0.0082 54  ASN   B CA  
4986 C C   . ASN   B 54  ? 0.1483 0.1653 0.1874 0.0062  -0.0024 0.0003  54  ASN   B C   
4987 O O   . ASN   B 54  ? 0.1565 0.1724 0.1885 -0.0038 0.0044  -0.0057 54  ASN   B O   
4988 C CB  . ASN   B 54  ? 0.1615 0.1759 0.1749 0.0102  0.0001  -0.0047 54  ASN   B CB  
4989 C CG  . ASN   B 54  ? 0.1703 0.1765 0.1674 0.0034  -0.0150 0.0037  54  ASN   B CG  
4990 O OD1 . ASN   B 54  ? 0.1629 0.1769 0.1937 0.0042  -0.0238 -0.0117 54  ASN   B OD1 
4991 N ND2 . ASN   B 54  ? 0.1870 0.1868 0.2034 -0.0013 -0.0374 0.0110  54  ASN   B ND2 
4998 N N   . LYS   B 55  ? 0.1465 0.1691 0.2102 0.0165  -0.0060 -0.0012 55  LYS   B N   
4999 C CA  . LYS   B 55  ? 0.1575 0.1756 0.2240 0.0140  -0.0071 -0.0032 55  LYS   B CA  
5000 C C   . LYS   B 55  ? 0.1602 0.1768 0.2108 0.0048  0.0022  -0.0119 55  LYS   B C   
5001 O O   . LYS   B 55  ? 0.1560 0.1922 0.2333 0.0042  -0.0046 -0.0099 55  LYS   B O   
5002 C CB  . LYS   B 55  ? 0.1686 0.1865 0.2781 0.0330  0.0030  0.0063  55  LYS   B CB  
5003 C CG  . LYS   B 55  ? 0.2155 0.2274 0.3629 0.0322  0.0103  0.0310  55  LYS   B CG  
5004 C CD  . LYS   B 55  ? 0.2555 0.2582 0.4282 0.0406  0.0313  0.0494  55  LYS   B CD  
5005 C CE  . LYS   B 55  ? 0.2834 0.2816 0.4913 0.0402  0.0557  0.0612  55  LYS   B CE  
5006 N NZ  . LYS   B 55  ? 0.2976 0.2996 0.5304 0.0363  0.0452  0.0759  55  LYS   B NZ  
5020 N N   . ALA   B 56  ? 0.1577 0.1841 0.1929 0.0101  -0.0056 -0.0118 56  ALA   B N   
5021 C CA  . ALA   B 56  ? 0.1658 0.1997 0.1987 -0.0021 -0.0013 -0.0079 56  ALA   B CA  
5022 C C   . ALA   B 56  ? 0.1593 0.1927 0.1897 -0.0035 0.0107  -0.0011 56  ALA   B C   
5023 O O   . ALA   B 56  ? 0.1820 0.2012 0.1969 0.0035  0.0313  0.0036  56  ALA   B O   
5024 C CB  . ALA   B 56  ? 0.1845 0.2222 0.2019 -0.0160 -0.0046 -0.0040 56  ALA   B CB  
5030 N N   . THR   B 57  ? 0.1563 0.1854 0.2043 -0.0108 0.0236  0.0004  57  THR   B N   
5031 C CA  . THR   B 57  ? 0.1683 0.1830 0.1972 -0.0073 0.0236  -0.0082 57  THR   B CA  
5032 C C   . THR   B 57  ? 0.1686 0.1983 0.2230 -0.0076 0.0241  0.0041  57  THR   B C   
5033 O O   . THR   B 57  ? 0.1707 0.1967 0.2390 -0.0265 0.0152  0.0030  57  THR   B O   
5034 C CB  . THR   B 57  ? 0.1809 0.1676 0.1561 -0.0073 0.0182  0.0049  57  THR   B CB  
5035 O OG1 . THR   B 57  ? 0.1782 0.1604 0.1899 -0.0141 0.0049  -0.0003 57  THR   B OG1 
5036 C CG2 . THR   B 57  ? 0.1753 0.1713 0.1633 -0.0134 0.0126  -0.0027 57  THR   B CG2 
5044 N N   . ASN   B 58  ? 0.1515 0.2193 0.2353 -0.0148 0.0041  -0.0106 58  ASN   B N   
5045 C CA  . ASN   B 58  ? 0.1905 0.2762 0.2758 -0.0332 0.0519  -0.0032 58  ASN   B CA  
5046 C C   . ASN   B 58  ? 0.1570 0.2379 0.2346 -0.0255 0.0029  -0.0205 58  ASN   B C   
5047 O O   . ASN   B 58  ? 0.1566 0.2497 0.2503 -0.0249 0.0049  -0.0347 58  ASN   B O   
5048 C CB  . ASN   B 58  ? 0.3312 0.3959 0.4191 -0.0418 0.0934  0.0112  58  ASN   B CB  
5049 C CG  . ASN   B 58  ? 0.4859 0.5148 0.5945 -0.0447 0.1126  0.0292  58  ASN   B CG  
5050 O OD1 . ASN   B 58  ? 0.5143 0.5347 0.6508 -0.0468 0.1189  0.0364  58  ASN   B OD1 
5051 N ND2 . ASN   B 58  ? 0.6208 0.6208 0.6659 -0.0460 0.1192  0.0331  58  ASN   B ND2 
5058 N N   . ASN   B 59  ? 0.1557 0.2159 0.2100 -0.0162 -0.0061 -0.0025 59  ASN   B N   
5059 C CA  . ASN   B 59  ? 0.1595 0.2169 0.1981 -0.0182 -0.0147 0.0092  59  ASN   B CA  
5060 C C   . ASN   B 59  ? 0.1526 0.2049 0.1950 -0.0219 -0.0162 -0.0080 59  ASN   B C   
5061 O O   . ASN   B 59  ? 0.1621 0.2054 0.1965 -0.0197 -0.0144 -0.0082 59  ASN   B O   
5062 C CB  . ASN   B 59  ? 0.1660 0.2363 0.2145 -0.0179 -0.0275 0.0109  59  ASN   B CB  
5063 C CG  . ASN   B 59  ? 0.1798 0.2528 0.2453 -0.0137 -0.0417 0.0061  59  ASN   B CG  
5064 O OD1 . ASN   B 59  ? 0.1720 0.2554 0.2341 -0.0092 -0.0331 0.0199  59  ASN   B OD1 
5065 N ND2 . ASN   B 59  ? 0.1915 0.2597 0.2643 -0.0174 -0.0539 -0.0039 59  ASN   B ND2 
5072 N N   . ALA   B 60  ? 0.1545 0.1929 0.2026 -0.0162 0.0041  -0.0152 60  ALA   B N   
5073 C CA  . ALA   B 60  ? 0.1679 0.1871 0.1939 -0.0222 0.0017  -0.0060 60  ALA   B CA  
5074 C C   . ALA   B 60  ? 0.1635 0.1774 0.1828 -0.0093 -0.0076 -0.0101 60  ALA   B C   
5075 O O   . ALA   B 60  ? 0.1680 0.1753 0.1907 -0.0184 0.0008  -0.0078 60  ALA   B O   
5076 C CB  . ALA   B 60  ? 0.1801 0.1853 0.2194 -0.0187 0.0136  -0.0076 60  ALA   B CB  
5082 N N   . MET   B 61  ? 0.1580 0.1613 0.1690 -0.0115 -0.0066 -0.0054 61  MET   B N   
5083 C CA  . MET   B 61  ? 0.1563 0.1606 0.1599 -0.0144 -0.0199 0.0028  61  MET   B CA  
5084 C C   . MET   B 61  ? 0.1574 0.1546 0.1631 -0.0170 -0.0154 -0.0004 61  MET   B C   
5085 O O   . MET   B 61  ? 0.1630 0.1550 0.1590 -0.0019 -0.0084 -0.0109 61  MET   B O   
5086 C CB  . MET   B 61  ? 0.1488 0.1646 0.1686 -0.0081 -0.0153 0.0068  61  MET   B CB  
5087 C CG  . MET   B 61  ? 0.1476 0.1560 0.1562 -0.0020 -0.0045 0.0086  61  MET   B CG  
5088 S SD  . MET   B 61  ? 0.1558 0.1601 0.1783 -0.0060 -0.0076 -0.0099 61  MET   B SD  
5089 C CE  . MET   B 61  ? 0.1629 0.1765 0.1942 -0.0047 -0.0140 -0.0218 61  MET   B CE  
5099 N N   . GLN   B 62  ? 0.1531 0.1641 0.1506 -0.0065 -0.0242 0.0015  62  GLN   B N   
5100 C CA  . GLN   B 62  ? 0.1617 0.1690 0.1630 0.0043  -0.0232 -0.0014 62  GLN   B CA  
5101 C C   . GLN   B 62  ? 0.1658 0.1649 0.1722 -0.0020 -0.0415 -0.0046 62  GLN   B C   
5102 O O   . GLN   B 62  ? 0.1752 0.1716 0.1803 -0.0086 -0.0290 -0.0164 62  GLN   B O   
5103 C CB  . GLN   B 62  ? 0.1718 0.1785 0.1679 0.0002  -0.0159 0.0035  62  GLN   B CB  
5104 C CG  . GLN   B 62  ? 0.1798 0.1857 0.1706 -0.0025 -0.0238 -0.0092 62  GLN   B CG  
5105 C CD  . GLN   B 62  ? 0.1752 0.1818 0.1639 -0.0007 -0.0229 0.0041  62  GLN   B CD  
5106 O OE1 . GLN   B 62  ? 0.1801 0.1764 0.1879 0.0012  -0.0331 -0.0070 62  GLN   B OE1 
5107 N NE2 . GLN   B 62  ? 0.1753 0.1750 0.1690 -0.0021 -0.0194 -0.0088 62  GLN   B NE2 
5116 N N   . VAL   B 63  ? 0.1681 0.1632 0.2017 -0.0147 -0.0321 -0.0094 63  VAL   B N   
5117 C CA  . VAL   B 63  ? 0.1826 0.1717 0.2163 -0.0169 -0.0314 -0.0069 63  VAL   B CA  
5118 C C   . VAL   B 63  ? 0.1797 0.1658 0.2006 -0.0199 -0.0334 -0.0214 63  VAL   B C   
5119 O O   . VAL   B 63  ? 0.1955 0.1616 0.2078 -0.0171 -0.0419 -0.0140 63  VAL   B O   
5120 C CB  . VAL   B 63  ? 0.1768 0.1906 0.2531 -0.0232 -0.0203 -0.0135 63  VAL   B CB  
5121 C CG1 . VAL   B 63  ? 0.1745 0.1961 0.2705 -0.0286 -0.0075 -0.0100 63  VAL   B CG1 
5122 C CG2 . VAL   B 63  ? 0.1777 0.2072 0.2701 -0.0179 -0.0330 -0.0104 63  VAL   B CG2 
5132 N N   . GLU   B 64  ? 0.1750 0.1597 0.1875 -0.0116 -0.0276 -0.0236 64  GLU   B N   
5133 C CA  . GLU   B 64  ? 0.1664 0.1547 0.1845 -0.0162 -0.0401 -0.0014 64  GLU   B CA  
5134 C C   . GLU   B 64  ? 0.1642 0.1527 0.1785 -0.0098 -0.0352 -0.0136 64  GLU   B C   
5135 O O   . GLU   B 64  ? 0.1785 0.1628 0.1688 -0.0132 -0.0331 -0.0222 64  GLU   B O   
5136 C CB  . GLU   B 64  ? 0.1772 0.1642 0.1786 -0.0210 -0.0309 -0.0031 64  GLU   B CB  
5137 C CG  . GLU   B 64  ? 0.1824 0.1628 0.1815 -0.0252 -0.0342 -0.0128 64  GLU   B CG  
5138 C CD  . GLU   B 64  ? 0.1872 0.1825 0.1947 -0.0335 -0.0433 -0.0064 64  GLU   B CD  
5139 O OE1 . GLU   B 64  ? 0.1868 0.1962 0.2195 -0.0450 -0.0279 -0.0300 64  GLU   B OE1 
5140 O OE2 . GLU   B 64  ? 0.1956 0.1847 0.1938 -0.0412 -0.0418 -0.0051 64  GLU   B OE2 
5147 N N   . SER   B 65  ? 0.1745 0.1490 0.1581 -0.0136 -0.0189 -0.0158 65  SER   B N   
5148 C CA  . SER   B 65  ? 0.1782 0.1431 0.1631 -0.0042 -0.0259 -0.0124 65  SER   B CA  
5149 C C   . SER   B 65  ? 0.1803 0.1551 0.1597 0.0028  -0.0285 -0.0134 65  SER   B C   
5150 O O   . SER   B 65  ? 0.1801 0.1650 0.1586 -0.0029 -0.0224 -0.0158 65  SER   B O   
5151 C CB  . SER   B 65  ? 0.1776 0.1452 0.1717 -0.0142 -0.0134 -0.0089 65  SER   B CB  
5152 O OG  . SER   B 65  ? 0.1763 0.1558 0.1657 -0.0077 -0.0184 -0.0232 65  SER   B OG  
5158 N N   . ASP   B 66  ? 0.1811 0.1600 0.1614 -0.0017 -0.0347 -0.0165 66  ASP   B N   
5159 C CA  . ASP   B 66  ? 0.1924 0.1633 0.1510 0.0053  -0.0394 -0.0039 66  ASP   B CA  
5160 C C   . ASP   B 66  ? 0.2009 0.1714 0.1545 -0.0002 -0.0259 -0.0114 66  ASP   B C   
5161 O O   . ASP   B 66  ? 0.1988 0.1855 0.1603 0.0029  -0.0231 -0.0208 66  ASP   B O   
5162 C CB  . ASP   B 66  ? 0.2035 0.1858 0.1782 0.0154  -0.0574 -0.0157 66  ASP   B CB  
5163 C CG  . ASP   B 66  ? 0.2300 0.2017 0.2094 0.0245  -0.0623 -0.0051 66  ASP   B CG  
5164 O OD1 . ASP   B 66  ? 0.2549 0.2037 0.2156 0.0134  -0.0555 0.0011  66  ASP   B OD1 
5165 O OD2 . ASP   B 66  ? 0.2526 0.2242 0.2744 0.0432  -0.0507 -0.0100 66  ASP   B OD2 
5170 N N   . ASP   B 67  ? 0.1850 0.1627 0.1513 -0.0079 -0.0264 -0.0199 67  ASP   B N   
5171 C CA  . ASP   B 67  ? 0.1970 0.1625 0.1818 -0.0108 -0.0233 -0.0037 67  ASP   B CA  
5172 C C   . ASP   B 67  ? 0.1908 0.1638 0.1933 0.0017  -0.0250 -0.0144 67  ASP   B C   
5173 O O   . ASP   B 67  ? 0.1970 0.1742 0.1936 -0.0010 -0.0130 -0.0300 67  ASP   B O   
5174 C CB  . ASP   B 67  ? 0.2258 0.1684 0.2111 -0.0152 -0.0419 -0.0061 67  ASP   B CB  
5175 C CG  . ASP   B 67  ? 0.2590 0.1784 0.2069 -0.0146 -0.0752 -0.0144 67  ASP   B CG  
5176 O OD1 . ASP   B 67  ? 0.2863 0.1883 0.2206 -0.0111 -0.0726 -0.0117 67  ASP   B OD1 
5177 O OD2 . ASP   B 67  ? 0.2729 0.1871 0.2283 -0.0044 -0.0832 -0.0028 67  ASP   B OD2 
5182 N N   . TYR   B 68  ? 0.1888 0.1629 0.1792 -0.0040 -0.0366 -0.0296 68  TYR   B N   
5183 C CA  . TYR   B 68  ? 0.1879 0.1779 0.1868 0.0114  -0.0386 -0.0293 68  TYR   B CA  
5184 C C   . TYR   B 68  ? 0.1889 0.1747 0.1901 0.0088  -0.0334 -0.0422 68  TYR   B C   
5185 O O   . TYR   B 68  ? 0.1954 0.1746 0.2131 0.0118  -0.0262 -0.0540 68  TYR   B O   
5186 C CB  . TYR   B 68  ? 0.1939 0.2001 0.1888 0.0087  -0.0496 -0.0455 68  TYR   B CB  
5187 C CG  . TYR   B 68  ? 0.2053 0.2227 0.2054 0.0115  -0.0438 -0.0678 68  TYR   B CG  
5188 C CD1 . TYR   B 68  ? 0.2096 0.2286 0.2295 -0.0071 -0.0439 -0.0751 68  TYR   B CD1 
5189 C CD2 . TYR   B 68  ? 0.2082 0.2467 0.2299 0.0213  -0.0614 -0.0667 68  TYR   B CD2 
5190 C CE1 . TYR   B 68  ? 0.2118 0.2493 0.2637 -0.0024 -0.0374 -0.0786 68  TYR   B CE1 
5191 C CE2 . TYR   B 68  ? 0.2042 0.2560 0.2518 0.0204  -0.0475 -0.0893 68  TYR   B CE2 
5192 C CZ  . TYR   B 68  ? 0.1978 0.2547 0.2750 0.0054  -0.0421 -0.0923 68  TYR   B CZ  
5193 O OH  . TYR   B 68  ? 0.1926 0.2847 0.3192 -0.0068 -0.0209 -0.0785 68  TYR   B OH  
5203 N N   . ILE   B 69  ? 0.1819 0.1652 0.1853 0.0087  -0.0274 -0.0351 69  ILE   B N   
5204 C CA  . ILE   B 69  ? 0.1913 0.1765 0.1903 0.0006  -0.0215 -0.0297 69  ILE   B CA  
5205 C C   . ILE   B 69  ? 0.1901 0.1758 0.1864 0.0074  -0.0326 -0.0285 69  ILE   B C   
5206 O O   . ILE   B 69  ? 0.1990 0.1875 0.1696 0.0097  -0.0220 -0.0323 69  ILE   B O   
5207 C CB  . ILE   B 69  ? 0.2016 0.1803 0.2099 -0.0004 -0.0012 -0.0334 69  ILE   B CB  
5208 C CG1 . ILE   B 69  ? 0.2002 0.1832 0.2285 -0.0063 0.0097  -0.0306 69  ILE   B CG1 
5209 C CG2 . ILE   B 69  ? 0.2189 0.1792 0.2272 -0.0026 -0.0020 -0.0240 69  ILE   B CG2 
5210 C CD1 . ILE   B 69  ? 0.1978 0.1882 0.2520 -0.0267 0.0150  -0.0444 69  ILE   B CD1 
5222 N N   . ALA   B 70  ? 0.1906 0.1696 0.1832 0.0043  -0.0327 -0.0318 70  ALA   B N   
5223 C CA  . ALA   B 70  ? 0.1935 0.1790 0.1756 -0.0023 -0.0394 -0.0340 70  ALA   B CA  
5224 C C   . ALA   B 70  ? 0.2023 0.1762 0.1993 -0.0080 -0.0380 -0.0391 70  ALA   B C   
5225 O O   . ALA   B 70  ? 0.2118 0.1687 0.2030 0.0095  -0.0435 -0.0334 70  ALA   B O   
5226 C CB  . ALA   B 70  ? 0.1974 0.1898 0.1795 -0.0035 -0.0377 -0.0407 70  ALA   B CB  
5232 N N   . THR   B 71  ? 0.2076 0.1782 0.1985 0.0069  -0.0532 -0.0348 71  THR   B N   
5233 C CA  . THR   B 71  ? 0.2167 0.1843 0.2138 0.0100  -0.0655 -0.0269 71  THR   B CA  
5234 C C   . THR   B 71  ? 0.2028 0.1869 0.2458 0.0329  -0.0610 -0.0534 71  THR   B C   
5235 O O   . THR   B 71  ? 0.2101 0.1914 0.2868 0.0394  -0.0568 -0.0611 71  THR   B O   
5236 C CB  . THR   B 71  ? 0.2465 0.1967 0.2419 0.0001  -0.0655 -0.0028 71  THR   B CB  
5237 O OG1 . THR   B 71  ? 0.2636 0.2199 0.2899 -0.0216 -0.0665 0.0123  71  THR   B OG1 
5238 C CG2 . THR   B 71  ? 0.2634 0.1961 0.2647 0.0019  -0.0562 -0.0021 71  THR   B CG2 
5246 N N   . ASN   B 72  ? 0.1930 0.1889 0.2416 0.0146  -0.0650 -0.0637 72  ASN   B N   
5247 C CA  . ASN   B 72  ? 0.1965 0.1939 0.2490 0.0096  -0.0423 -0.0753 72  ASN   B CA  
5248 C C   . ASN   B 72  ? 0.1975 0.2017 0.2584 -0.0064 -0.0211 -0.0670 72  ASN   B C   
5249 O O   . ASN   B 72  ? 0.2034 0.2169 0.2978 -0.0044 0.0007  -0.0787 72  ASN   B O   
5250 C CB  . ASN   B 72  ? 0.2005 0.2112 0.2562 0.0118  -0.0583 -0.0630 72  ASN   B CB  
5251 C CG  . ASN   B 72  ? 0.2172 0.2323 0.2658 0.0232  -0.0642 -0.0346 72  ASN   B CG  
5252 O OD1 . ASN   B 72  ? 0.2450 0.2525 0.2647 0.0136  -0.0476 -0.0373 72  ASN   B OD1 
5253 N ND2 . ASN   B 72  ? 0.2292 0.2421 0.3078 0.0388  -0.0584 0.0015  72  ASN   B ND2 
5260 N N   . GLY   B 73  ? 0.2025 0.1974 0.2338 -0.0027 -0.0307 -0.0658 73  GLY   B N   
5261 C CA  . GLY   B 73  ? 0.1937 0.2164 0.2099 -0.0047 -0.0200 -0.0563 73  GLY   B CA  
5262 C C   . GLY   B 73  ? 0.1924 0.2151 0.1572 0.0023  -0.0152 -0.0390 73  GLY   B C   
5263 O O   . GLY   B 73  ? 0.1875 0.2000 0.1652 0.0067  -0.0158 -0.0325 73  GLY   B O   
5267 N N   . PRO   B 74  ? 0.1976 0.2271 0.1572 -0.0011 -0.0204 -0.0397 74  PRO   B N   
5268 C CA  . PRO   B 74  ? 0.1924 0.2237 0.1397 0.0061  -0.0156 -0.0179 74  PRO   B CA  
5269 C C   . PRO   B 74  ? 0.1776 0.2016 0.1533 0.0033  -0.0146 -0.0103 74  PRO   B C   
5270 O O   . PRO   B 74  ? 0.1796 0.1973 0.2062 0.0035  -0.0071 -0.0295 74  PRO   B O   
5271 C CB  . PRO   B 74  ? 0.2080 0.2422 0.1565 0.0006  -0.0149 -0.0201 74  PRO   B CB  
5272 C CG  . PRO   B 74  ? 0.2266 0.2590 0.1729 0.0008  -0.0176 -0.0107 74  PRO   B CG  
5273 C CD  . PRO   B 74  ? 0.2250 0.2447 0.1617 0.0080  -0.0112 -0.0191 74  PRO   B CD  
5281 N N   . LEU   B 75  ? 0.1794 0.1854 0.1537 0.0011  -0.0214 -0.0176 75  LEU   B N   
5282 C CA  . LEU   B 75  ? 0.1879 0.1877 0.1228 0.0004  -0.0182 0.0032  75  LEU   B CA  
5283 C C   . LEU   B 75  ? 0.1890 0.2039 0.1289 0.0059  -0.0081 0.0026  75  LEU   B C   
5284 O O   . LEU   B 75  ? 0.1967 0.2129 0.1461 -0.0015 -0.0044 -0.0012 75  LEU   B O   
5285 C CB  . LEU   B 75  ? 0.1910 0.1940 0.1217 -0.0094 -0.0167 0.0134  75  LEU   B CB  
5286 C CG  . LEU   B 75  ? 0.2214 0.2151 0.1496 -0.0282 -0.0073 0.0139  75  LEU   B CG  
5287 C CD1 . LEU   B 75  ? 0.2525 0.2260 0.1566 -0.0422 0.0105  0.0053  75  LEU   B CD1 
5288 C CD2 . LEU   B 75  ? 0.2594 0.2392 0.2489 -0.0196 0.0058  0.0266  75  LEU   B CD2 
5300 N N   . LYS   B 76  ? 0.1912 0.2229 0.1673 0.0039  0.0017  0.0150  76  LYS   B N   
5301 C CA  . LYS   B 76  ? 0.2003 0.2282 0.2023 -0.0079 0.0254  0.0104  76  LYS   B CA  
5302 C C   . LYS   B 76  ? 0.1895 0.2206 0.1715 -0.0051 0.0179  0.0256  76  LYS   B C   
5303 O O   . LYS   B 76  ? 0.1881 0.1982 0.1788 -0.0022 0.0042  0.0256  76  LYS   B O   
5304 C CB  . LYS   B 76  ? 0.2169 0.2242 0.2551 -0.0122 0.0395  -0.0176 76  LYS   B CB  
5305 C CG  . LYS   B 76  ? 0.2258 0.2424 0.2896 0.0019  0.0336  -0.0251 76  LYS   B CG  
5306 C CD  . LYS   B 76  ? 0.2294 0.2554 0.3267 0.0087  0.0283  -0.0337 76  LYS   B CD  
5307 C CE  . LYS   B 76  ? 0.2323 0.2774 0.3865 0.0101  0.0117  -0.0360 76  LYS   B CE  
5308 N NZ  . LYS   B 76  ? 0.2252 0.2839 0.4048 0.0043  -0.0140 -0.0545 76  LYS   B NZ  
5322 N N   . VAL   B 77  ? 0.1915 0.2386 0.1868 -0.0023 0.0127  0.0327  77  VAL   B N   
5323 C CA  . VAL   B 77  ? 0.1971 0.2284 0.1898 -0.0037 0.0193  0.0589  77  VAL   B CA  
5324 C C   . VAL   B 77  ? 0.1850 0.1926 0.1861 0.0057  0.0328  0.0418  77  VAL   B C   
5325 O O   . VAL   B 77  ? 0.1857 0.1924 0.1876 0.0137  0.0384  0.0261  77  VAL   B O   
5326 C CB  . VAL   B 77  ? 0.2181 0.2429 0.2359 -0.0092 0.0159  0.0784  77  VAL   B CB  
5327 C CG1 . VAL   B 77  ? 0.2238 0.2335 0.2652 -0.0136 0.0205  0.0910  77  VAL   B CG1 
5328 C CG2 . VAL   B 77  ? 0.2362 0.2561 0.2531 -0.0145 -0.0090 0.0749  77  VAL   B CG2 
5338 N N   . GLY   B 78  ? 0.1807 0.1765 0.1864 0.0105  0.0278  0.0293  78  GLY   B N   
5339 C CA  . GLY   B 78  ? 0.1868 0.1703 0.1736 0.0077  0.0349  0.0269  78  GLY   B CA  
5340 C C   . GLY   B 78  ? 0.1781 0.1682 0.1651 0.0099  0.0226  0.0298  78  GLY   B C   
5341 O O   . GLY   B 78  ? 0.1638 0.1705 0.1863 0.0158  0.0144  0.0301  78  GLY   B O   
5345 N N   . GLY   B 79  ? 0.1644 0.1762 0.1795 0.0038  0.0181  0.0190  79  GLY   B N   
5346 C CA  . GLY   B 79  ? 0.1621 0.1645 0.1792 0.0064  0.0175  0.0275  79  GLY   B CA  
5347 C C   . GLY   B 79  ? 0.1510 0.1624 0.1657 0.0048  0.0190  0.0081  79  GLY   B C   
5348 O O   . GLY   B 79  ? 0.1594 0.1608 0.1688 0.0107  0.0208  0.0176  79  GLY   B O   
5352 N N   . SER   B 80  ? 0.1569 0.1584 0.1624 -0.0037 0.0262  0.0109  80  SER   B N   
5353 C CA  . SER   B 80  ? 0.1434 0.1612 0.1621 -0.0042 0.0057  0.0075  80  SER   B CA  
5354 C C   . SER   B 80  ? 0.1447 0.1542 0.1656 -0.0005 0.0012  0.0025  80  SER   B C   
5355 O O   . SER   B 80  ? 0.1588 0.1571 0.1934 0.0065  0.0131  0.0014  80  SER   B O   
5356 C CB  . SER   B 80  ? 0.1482 0.1588 0.1647 -0.0033 -0.0018 0.0119  80  SER   B CB  
5357 O OG  . SER   B 80  ? 0.1632 0.1732 0.1760 -0.0115 -0.0115 0.0140  80  SER   B OG  
5363 N N   . CYS   B 81  ? 0.1459 0.1416 0.1665 -0.0071 -0.0073 0.0060  81  CYS   B N   
5364 C CA  . CYS   B 81  ? 0.1585 0.1440 0.1585 -0.0044 -0.0165 0.0056  81  CYS   B CA  
5365 C C   . CYS   B 81  ? 0.1515 0.1456 0.1381 -0.0087 -0.0145 0.0139  81  CYS   B C   
5366 O O   . CYS   B 81  ? 0.1679 0.1395 0.1677 0.0091  0.0020  0.0024  81  CYS   B O   
5367 C CB  . CYS   B 81  ? 0.1693 0.1488 0.1794 -0.0049 -0.0071 0.0062  81  CYS   B CB  
5368 S SG  . CYS   B 81  ? 0.1737 0.1706 0.1627 -0.0079 -0.0229 -0.0086 81  CYS   B SG  
5374 N N   . VAL   B 82  ? 0.1595 0.1447 0.1428 -0.0061 -0.0218 0.0127  82  VAL   B N   
5375 C CA  . VAL   B 82  ? 0.1704 0.1427 0.1406 -0.0239 -0.0132 0.0159  82  VAL   B CA  
5376 C C   . VAL   B 82  ? 0.1788 0.1324 0.1547 -0.0134 -0.0065 0.0004  82  VAL   B C   
5377 O O   . VAL   B 82  ? 0.1771 0.1355 0.2032 -0.0091 -0.0079 -0.0131 82  VAL   B O   
5378 C CB  . VAL   B 82  ? 0.1730 0.1513 0.1624 -0.0132 -0.0182 0.0177  82  VAL   B CB  
5379 C CG1 . VAL   B 82  ? 0.1959 0.1783 0.1804 -0.0020 -0.0268 0.0232  82  VAL   B CG1 
5380 C CG2 . VAL   B 82  ? 0.1847 0.1623 0.1817 -0.0144 -0.0280 0.0253  82  VAL   B CG2 
5390 N N   . LEU   B 83  ? 0.1669 0.1296 0.1550 -0.0170 -0.0156 -0.0077 83  LEU   B N   
5391 C CA  . LEU   B 83  ? 0.1632 0.1380 0.1467 -0.0177 -0.0247 -0.0008 83  LEU   B CA  
5392 C C   . LEU   B 83  ? 0.1578 0.1385 0.1427 -0.0260 -0.0325 -0.0069 83  LEU   B C   
5393 O O   . LEU   B 83  ? 0.1544 0.1454 0.1369 -0.0213 -0.0121 0.0061  83  LEU   B O   
5394 C CB  . LEU   B 83  ? 0.1688 0.1448 0.1634 -0.0165 -0.0165 -0.0071 83  LEU   B CB  
5395 C CG  . LEU   B 83  ? 0.1831 0.1644 0.1642 -0.0278 -0.0098 -0.0050 83  LEU   B CG  
5396 C CD1 . LEU   B 83  ? 0.2006 0.1690 0.1779 -0.0150 -0.0200 0.0034  83  LEU   B CD1 
5397 C CD2 . LEU   B 83  ? 0.1979 0.1720 0.1638 -0.0163 -0.0248 -0.0189 83  LEU   B CD2 
5409 N N   . SER   B 84  ? 0.1682 0.1491 0.1648 -0.0287 -0.0320 0.0009  84  SER   B N   
5410 C CA  . SER   B 84  ? 0.1754 0.1726 0.1576 -0.0299 -0.0181 0.0187  84  SER   B CA  
5411 C C   . SER   B 84  ? 0.1629 0.1824 0.1070 -0.0246 -0.0151 0.0246  84  SER   B C   
5412 O O   . SER   B 84  ? 0.1662 0.1742 0.1107 -0.0259 -0.0152 0.0016  84  SER   B O   
5413 C CB  . SER   B 84  ? 0.1885 0.1737 0.2062 -0.0319 -0.0040 0.0054  84  SER   B CB  
5414 O OG  . SER   B 84  ? 0.1847 0.1940 0.2529 -0.0483 0.0032  0.0184  84  SER   B OG  
5420 N N   . GLY   B 85  ? 0.1651 0.1989 0.1354 -0.0210 -0.0103 0.0286  85  GLY   B N   
5421 C CA  . GLY   B 85  ? 0.1675 0.2079 0.1629 -0.0337 0.0047  -0.0013 85  GLY   B CA  
5422 C C   . GLY   B 85  ? 0.1571 0.1971 0.1515 -0.0372 -0.0058 0.0014  85  GLY   B C   
5423 O O   . GLY   B 85  ? 0.1665 0.1892 0.1594 -0.0464 0.0075  -0.0210 85  GLY   B O   
5427 N N   . HIS   B 86  ? 0.1638 0.1726 0.1601 -0.0406 -0.0134 0.0140  86  HIS   B N   
5428 C CA  . HIS   B 86  ? 0.1668 0.1678 0.1580 -0.0403 -0.0210 0.0117  86  HIS   B CA  
5429 C C   . HIS   B 86  ? 0.1616 0.1845 0.1538 -0.0452 -0.0080 0.0318  86  HIS   B C   
5430 O O   . HIS   B 86  ? 0.1838 0.1923 0.1644 -0.0320 0.0053  0.0280  86  HIS   B O   
5431 C CB  . HIS   B 86  ? 0.1762 0.1812 0.1574 -0.0327 -0.0292 0.0024  86  HIS   B CB  
5432 C CG  . HIS   B 86  ? 0.1714 0.1942 0.1545 -0.0193 -0.0295 0.0087  86  HIS   B CG  
5433 N ND1 . HIS   B 86  ? 0.1773 0.2204 0.1907 -0.0273 -0.0306 -0.0167 86  HIS   B ND1 
5434 C CD2 . HIS   B 86  ? 0.1762 0.1946 0.1693 -0.0133 -0.0218 0.0122  86  HIS   B CD2 
5435 C CE1 . HIS   B 86  ? 0.1887 0.2150 0.1874 -0.0186 -0.0123 -0.0385 86  HIS   B CE1 
5436 N NE2 . HIS   B 86  ? 0.1823 0.2053 0.1757 -0.0026 -0.0159 -0.0082 86  HIS   B NE2 
5444 N N   . ASN   B 87  ? 0.1665 0.1848 0.1689 -0.0342 0.0065  0.0236  87  ASN   B N   
5445 C CA  . ASN   B 87  ? 0.1856 0.2029 0.1739 -0.0258 0.0251  0.0262  87  ASN   B CA  
5446 C C   . ASN   B 87  ? 0.2006 0.1871 0.1664 -0.0301 0.0309  0.0156  87  ASN   B C   
5447 O O   . ASN   B 87  ? 0.2198 0.1971 0.2098 -0.0235 0.0468  0.0110  87  ASN   B O   
5448 C CB  . ASN   B 87  ? 0.1867 0.2374 0.2122 -0.0177 0.0180  0.0195  87  ASN   B CB  
5449 C CG  . ASN   B 87  ? 0.1836 0.2619 0.2142 0.0133  0.0173  0.0337  87  ASN   B CG  
5450 O OD1 . ASN   B 87  ? 0.1818 0.2501 0.2021 0.0151  0.0433  0.0498  87  ASN   B OD1 
5451 N ND2 . ASN   B 87  ? 0.2166 0.2751 0.2757 0.0198  0.0295  0.0347  87  ASN   B ND2 
5458 N N   . LEU   B 88  ? 0.1793 0.1721 0.1437 -0.0351 0.0081  0.0116  88  LEU   B N   
5459 C CA  . LEU   B 88  ? 0.1898 0.1669 0.1512 -0.0391 -0.0004 0.0031  88  LEU   B CA  
5460 C C   . LEU   B 88  ? 0.1905 0.1714 0.1498 -0.0398 -0.0136 0.0043  88  LEU   B C   
5461 O O   . LEU   B 88  ? 0.2118 0.1796 0.1846 -0.0286 -0.0303 -0.0002 88  LEU   B O   
5462 C CB  . LEU   B 88  ? 0.2066 0.1766 0.1716 -0.0473 -0.0167 0.0059  88  LEU   B CB  
5463 C CG  . LEU   B 88  ? 0.2434 0.2023 0.1945 -0.0415 -0.0409 0.0306  88  LEU   B CG  
5464 C CD1 . LEU   B 88  ? 0.2521 0.2345 0.2160 -0.0537 -0.0407 0.0503  88  LEU   B CD1 
5465 C CD2 . LEU   B 88  ? 0.2859 0.2333 0.2669 0.0016  -0.0672 0.0185  88  LEU   B CD2 
5477 N N   . ALA   B 89  ? 0.1815 0.1669 0.1308 -0.0438 0.0144  0.0015  89  ALA   B N   
5478 C CA  . ALA   B 89  ? 0.1791 0.1591 0.1137 -0.0395 0.0009  0.0059  89  ALA   B CA  
5479 C C   . ALA   B 89  ? 0.1836 0.1550 0.1417 -0.0433 0.0091  0.0016  89  ALA   B C   
5480 O O   . ALA   B 89  ? 0.1598 0.1681 0.1779 -0.0427 0.0039  -0.0162 89  ALA   B O   
5481 C CB  . ALA   B 89  ? 0.1649 0.1579 0.1472 -0.0406 0.0087  0.0105  89  ALA   B CB  
5487 N N   . LYS   B 90  ? 0.2065 0.1517 0.1438 -0.0431 -0.0129 0.0071  90  LYS   B N   
5488 C CA  . LYS   B 90  ? 0.2127 0.1540 0.1336 -0.0428 -0.0152 0.0078  90  LYS   B CA  
5489 C C   . LYS   B 90  ? 0.1939 0.1454 0.1479 -0.0414 -0.0146 -0.0032 90  LYS   B C   
5490 O O   . LYS   B 90  ? 0.1946 0.1561 0.1621 -0.0504 -0.0052 0.0019  90  LYS   B O   
5491 C CB  . LYS   B 90  ? 0.2296 0.1601 0.1657 -0.0361 0.0006  0.0155  90  LYS   B CB  
5492 C CG  . LYS   B 90  ? 0.2263 0.1773 0.1678 -0.0201 0.0181  0.0047  90  LYS   B CG  
5493 C CD  . LYS   B 90  ? 0.2522 0.1940 0.2296 -0.0064 0.0273  -0.0150 90  LYS   B CD  
5494 C CE  . LYS   B 90  ? 0.2604 0.2083 0.2794 -0.0143 0.0406  -0.0143 90  LYS   B CE  
5495 N NZ  . LYS   B 90  ? 0.2690 0.1963 0.2597 -0.0282 0.0637  -0.0203 90  LYS   B NZ  
5509 N N   . HIS   B 91  ? 0.1706 0.1388 0.1322 -0.0404 -0.0258 0.0107  91  HIS   B N   
5510 C CA  . HIS   B 91  ? 0.1702 0.1447 0.1322 -0.0277 -0.0230 0.0081  91  HIS   B CA  
5511 C C   . HIS   B 91  ? 0.1611 0.1506 0.1051 -0.0357 -0.0098 0.0031  91  HIS   B C   
5512 O O   . HIS   B 91  ? 0.1695 0.1527 0.1195 -0.0279 -0.0272 0.0036  91  HIS   B O   
5513 C CB  . HIS   B 91  ? 0.1840 0.1451 0.1675 -0.0091 -0.0180 0.0238  91  HIS   B CB  
5514 C CG  . HIS   B 91  ? 0.2241 0.1691 0.2337 -0.0030 0.0090  0.0222  91  HIS   B CG  
5515 N ND1 . HIS   B 91  ? 0.2575 0.1734 0.3085 0.0008  0.0183  0.0147  91  HIS   B ND1 
5516 C CD2 . HIS   B 91  ? 0.2421 0.1872 0.3003 0.0165  -0.0016 0.0632  91  HIS   B CD2 
5517 C CE1 . HIS   B 91  ? 0.2626 0.1866 0.3331 0.0239  0.0181  0.0224  91  HIS   B CE1 
5518 N NE2 . HIS   B 91  ? 0.2543 0.1959 0.3367 0.0303  0.0167  0.0684  91  HIS   B NE2 
5526 N N   . CYS   B 92  ? 0.1495 0.1456 0.1242 -0.0352 -0.0169 -0.0021 92  CYS   B N   
5527 C CA  . CYS   B 92  ? 0.1569 0.1325 0.1188 -0.0235 -0.0033 0.0015  92  CYS   B CA  
5528 C C   . CYS   B 92  ? 0.1552 0.1302 0.1110 -0.0165 0.0023  -0.0021 92  CYS   B C   
5529 O O   . CYS   B 92  ? 0.1632 0.1408 0.1337 -0.0159 0.0021  -0.0008 92  CYS   B O   
5530 C CB  . CYS   B 92  ? 0.1539 0.1363 0.1383 -0.0178 -0.0097 0.0074  92  CYS   B CB  
5531 S SG  . CYS   B 92  ? 0.1515 0.1457 0.1428 -0.0141 -0.0125 0.0061  92  CYS   B SG  
5537 N N   . LEU   B 93  ? 0.1470 0.1346 0.1265 -0.0162 -0.0089 -0.0024 93  LEU   B N   
5538 C CA  . LEU   B 93  ? 0.1526 0.1442 0.1161 -0.0121 -0.0168 0.0081  93  LEU   B CA  
5539 C C   . LEU   B 93  ? 0.1364 0.1323 0.1204 -0.0030 -0.0165 0.0080  93  LEU   B C   
5540 O O   . LEU   B 93  ? 0.1450 0.1304 0.1518 -0.0099 -0.0078 0.0009  93  LEU   B O   
5541 C CB  . LEU   B 93  ? 0.1526 0.1357 0.1384 -0.0037 -0.0206 0.0060  93  LEU   B CB  
5542 C CG  . LEU   B 93  ? 0.1442 0.1444 0.1668 -0.0077 -0.0093 0.0138  93  LEU   B CG  
5543 C CD1 . LEU   B 93  ? 0.1516 0.1525 0.1667 0.0116  -0.0065 -0.0054 93  LEU   B CD1 
5544 C CD2 . LEU   B 93  ? 0.1423 0.1453 0.1766 -0.0019 -0.0219 -0.0006 93  LEU   B CD2 
5556 N N   . HIS   B 94  ? 0.1507 0.1211 0.1246 -0.0047 -0.0131 0.0080  94  HIS   B N   
5557 C CA  . HIS   B 94  ? 0.1506 0.1280 0.1293 -0.0095 -0.0048 0.0052  94  HIS   B CA  
5558 C C   . HIS   B 94  ? 0.1411 0.1337 0.1501 -0.0115 -0.0081 0.0095  94  HIS   B C   
5559 O O   . HIS   B 94  ? 0.1402 0.1459 0.1820 -0.0097 0.0160  -0.0061 94  HIS   B O   
5560 C CB  . HIS   B 94  ? 0.1502 0.1350 0.1446 -0.0099 -0.0030 0.0014  94  HIS   B CB  
5561 C CG  . HIS   B 94  ? 0.1489 0.1344 0.1437 -0.0160 -0.0248 0.0046  94  HIS   B CG  
5562 N ND1 . HIS   B 94  ? 0.1540 0.1319 0.1475 -0.0112 -0.0250 0.0021  94  HIS   B ND1 
5563 C CD2 . HIS   B 94  ? 0.1485 0.1385 0.1431 0.0012  -0.0176 -0.0025 94  HIS   B CD2 
5564 C CE1 . HIS   B 94  ? 0.1591 0.1364 0.1707 -0.0133 -0.0201 -0.0021 94  HIS   B CE1 
5565 N NE2 . HIS   B 94  ? 0.1512 0.1414 0.1579 -0.0123 -0.0179 0.0016  94  HIS   B NE2 
5573 N N   . VAL   B 95  ? 0.1372 0.1319 0.1537 -0.0098 -0.0075 0.0100  95  VAL   B N   
5574 C CA  . VAL   B 95  ? 0.1426 0.1376 0.1433 -0.0022 -0.0006 0.0159  95  VAL   B CA  
5575 C C   . VAL   B 95  ? 0.1463 0.1437 0.1435 0.0021  0.0041  0.0206  95  VAL   B C   
5576 O O   . VAL   B 95  ? 0.1565 0.1464 0.1599 0.0060  -0.0018 0.0208  95  VAL   B O   
5577 C CB  . VAL   B 95  ? 0.1522 0.1384 0.1387 -0.0055 -0.0121 0.0098  95  VAL   B CB  
5578 C CG1 . VAL   B 95  ? 0.1559 0.1582 0.1783 -0.0188 -0.0047 0.0115  95  VAL   B CG1 
5579 C CG2 . VAL   B 95  ? 0.1631 0.1376 0.1361 0.0017  -0.0118 0.0118  95  VAL   B CG2 
5589 N N   . VAL   B 96  ? 0.1643 0.1431 0.1482 0.0071  0.0085  0.0203  96  VAL   B N   
5590 C CA  . VAL   B 96  ? 0.1769 0.1548 0.1338 0.0122  0.0128  0.0240  96  VAL   B CA  
5591 C C   . VAL   B 96  ? 0.1832 0.1481 0.1586 0.0171  0.0194  0.0256  96  VAL   B C   
5592 O O   . VAL   B 96  ? 0.1873 0.1589 0.1821 0.0013  0.0306  0.0019  96  VAL   B O   
5593 C CB  . VAL   B 96  ? 0.1821 0.1771 0.1378 0.0076  0.0080  0.0227  96  VAL   B CB  
5594 C CG1 . VAL   B 96  ? 0.1773 0.1984 0.1550 0.0262  0.0131  0.0101  96  VAL   B CG1 
5595 C CG2 . VAL   B 96  ? 0.1913 0.1720 0.1476 0.0061  0.0186  0.0123  96  VAL   B CG2 
5605 N N   . GLY   B 97  ? 0.1878 0.1501 0.1478 0.0055  0.0106  0.0291  97  GLY   B N   
5606 C CA  . GLY   B 97  ? 0.2082 0.1621 0.1684 0.0071  0.0074  0.0355  97  GLY   B CA  
5607 C C   . GLY   B 97  ? 0.2336 0.1670 0.1889 0.0029  0.0132  0.0286  97  GLY   B C   
5608 O O   . GLY   B 97  ? 0.2497 0.1672 0.1732 0.0062  0.0031  0.0098  97  GLY   B O   
5612 N N   . PRO   B 98  ? 0.2487 0.1752 0.2085 0.0062  0.0497  0.0472  98  PRO   B N   
5613 C CA  . PRO   B 98  ? 0.2663 0.2002 0.2227 0.0304  0.0653  0.0493  98  PRO   B CA  
5614 C C   . PRO   B 98  ? 0.2768 0.2017 0.1919 0.0508  0.0701  0.0622  98  PRO   B C   
5615 O O   . PRO   B 98  ? 0.2594 0.1958 0.2120 0.0343  0.0658  0.0544  98  PRO   B O   
5616 C CB  . PRO   B 98  ? 0.2590 0.2148 0.2302 0.0276  0.0858  0.0635  98  PRO   B CB  
5617 C CG  . PRO   B 98  ? 0.2514 0.2052 0.2406 0.0130  0.0775  0.0794  98  PRO   B CG  
5618 C CD  . PRO   B 98  ? 0.2362 0.1843 0.2436 0.0124  0.0703  0.0694  98  PRO   B CD  
5626 N N   . ASN   B 99  ? 0.2924 0.2306 0.1998 0.0758  0.0759  0.0427  99  ASN   B N   
5627 C CA  . ASN   B 99  ? 0.3217 0.2473 0.2028 0.0909  0.0777  0.0672  99  ASN   B CA  
5628 C C   . ASN   B 99  ? 0.3503 0.2882 0.2304 0.0978  0.1060  0.1035  99  ASN   B C   
5629 O O   . ASN   B 99  ? 0.3745 0.3055 0.2388 0.0988  0.0969  0.1185  99  ASN   B O   
5630 C CB  . ASN   B 99  ? 0.3363 0.2448 0.2005 0.0902  0.0559  0.0607  99  ASN   B CB  
5631 C CG  . ASN   B 99  ? 0.3456 0.2513 0.2060 0.0809  0.0501  0.0534  99  ASN   B CG  
5632 O OD1 . ASN   B 99  ? 0.3478 0.2471 0.2401 0.0880  0.0630  0.0703  99  ASN   B OD1 
5633 N ND2 . ASN   B 99  ? 0.3392 0.2516 0.2007 0.0855  0.0197  0.0389  99  ASN   B ND2 
5640 N N   . VAL   B 100 ? 0.3725 0.3013 0.3033 0.0862  0.1104  0.1323  100 VAL   B N   
5641 C CA  . VAL   B 100 ? 0.4070 0.3253 0.3771 0.0677  0.0964  0.1602  100 VAL   B CA  
5642 C C   . VAL   B 100 ? 0.4409 0.3348 0.3619 0.0711  0.0886  0.1857  100 VAL   B C   
5643 O O   . VAL   B 100 ? 0.4550 0.3473 0.3706 0.0710  0.1045  0.1795  100 VAL   B O   
5644 C CB  . VAL   B 100 ? 0.4089 0.3370 0.4557 0.0341  0.0952  0.1740  100 VAL   B CB  
5645 C CG1 . VAL   B 100 ? 0.4169 0.3416 0.4943 0.0296  0.0885  0.1693  100 VAL   B CG1 
5646 C CG2 . VAL   B 100 ? 0.4032 0.3435 0.4754 0.0187  0.0998  0.1852  100 VAL   B CG2 
5656 N N   . ASN   B 101 ? 0.4623 0.3467 0.3652 0.0757  0.0552  0.1825  101 ASN   B N   
5657 C CA  . ASN   B 101 ? 0.4896 0.3681 0.3630 0.0722  0.0278  0.1710  101 ASN   B CA  
5658 C C   . ASN   B 101 ? 0.5383 0.4273 0.3839 0.0553  0.0167  0.1578  101 ASN   B C   
5659 O O   . ASN   B 101 ? 0.5414 0.4358 0.4063 0.0618  0.0243  0.1340  101 ASN   B O   
5660 C CB  . ASN   B 101 ? 0.4723 0.3438 0.3767 0.0731  0.0273  0.1380  101 ASN   B CB  
5661 C CG  . ASN   B 101 ? 0.4540 0.3199 0.3825 0.0787  0.0255  0.1266  101 ASN   B CG  
5662 O OD1 . ASN   B 101 ? 0.4495 0.3172 0.4098 0.0708  0.0417  0.1210  101 ASN   B OD1 
5663 N ND2 . ASN   B 101 ? 0.4414 0.3079 0.3611 0.0864  0.0203  0.1107  101 ASN   B ND2 
5670 N N   A LYS   B 102 ? 0.5653 0.4562 0.4056 0.0407  0.0142  0.1474  102 LYS   B N   
5671 N N   B LYS   B 102 ? 0.5559 0.4568 0.4178 0.0424  0.0131  0.1404  102 LYS   B N   
5672 C CA  A LYS   B 102 ? 0.5897 0.4890 0.4325 0.0229  0.0134  0.1221  102 LYS   B CA  
5673 C CA  B LYS   B 102 ? 0.5710 0.4844 0.4516 0.0297  0.0128  0.1182  102 LYS   B CA  
5674 C C   A LYS   B 102 ? 0.5861 0.4906 0.4093 0.0230  0.0146  0.1337  102 LYS   B C   
5675 C C   B LYS   B 102 ? 0.5740 0.4891 0.4350 0.0260  0.0179  0.1266  102 LYS   B C   
5676 O O   A LYS   B 102 ? 0.5940 0.4934 0.4115 0.0219  0.0009  0.1364  102 LYS   B O   
5677 O O   B LYS   B 102 ? 0.5770 0.4916 0.4431 0.0246  0.0127  0.1291  102 LYS   B O   
5678 C CB  A LYS   B 102 ? 0.6132 0.5170 0.4984 0.0062  0.0218  0.0760  102 LYS   B CB  
5679 C CB  B LYS   B 102 ? 0.5810 0.5042 0.5045 0.0223  0.0115  0.0847  102 LYS   B CB  
5680 C CG  A LYS   B 102 ? 0.6333 0.5415 0.5610 -0.0079 0.0312  0.0338  102 LYS   B CG  
5681 C CG  B LYS   B 102 ? 0.5893 0.5208 0.5480 0.0165  0.0114  0.0544  102 LYS   B CG  
5682 C CD  A LYS   B 102 ? 0.6511 0.5618 0.6308 -0.0185 0.0408  0.0004  102 LYS   B CD  
5683 C CD  B LYS   B 102 ? 0.5959 0.5335 0.5923 0.0123  0.0123  0.0296  102 LYS   B CD  
5684 C CE  A LYS   B 102 ? 0.6638 0.5759 0.6794 -0.0263 0.0483  -0.0247 102 LYS   B CE  
5685 C CE  B LYS   B 102 ? 0.6006 0.5423 0.6215 0.0095  0.0130  0.0114  102 LYS   B CE  
5686 N NZ  A LYS   B 102 ? 0.6717 0.5846 0.7092 -0.0298 0.0504  -0.0396 102 LYS   B NZ  
5687 N NZ  B LYS   B 102 ? 0.6036 0.5476 0.6386 0.0083  0.0130  0.0015  102 LYS   B NZ  
5714 N N   . GLY   B 103 ? 0.5715 0.4879 0.4199 0.0249  0.0294  0.1263  103 GLY   B N   
5715 C CA  . GLY   B 103 ? 0.5522 0.4816 0.4290 0.0279  0.0529  0.1070  103 GLY   B CA  
5716 C C   . GLY   B 103 ? 0.5294 0.4711 0.4264 0.0313  0.0731  0.0881  103 GLY   B C   
5717 O O   . GLY   B 103 ? 0.5353 0.4785 0.4279 0.0291  0.0805  0.0928  103 GLY   B O   
5722 N N   A GLU   B 104 ? 0.5111 0.4536 0.4096 0.0415  0.1003  0.0780  104 GLU   B N   
5723 N N   B GLU   B 104 ? 0.5145 0.4664 0.4297 0.0256  0.0603  0.0696  104 GLU   B N   
5724 C CA  A GLU   B 104 ? 0.4906 0.4359 0.3962 0.0576  0.1186  0.0653  104 GLU   B CA  
5725 C CA  B GLU   B 104 ? 0.4983 0.4601 0.4286 0.0212  0.0472  0.0483  104 GLU   B CA  
5726 C C   A GLU   B 104 ? 0.4919 0.4358 0.4153 0.0385  0.1688  0.0787  104 GLU   B C   
5727 C C   B GLU   B 104 ? 0.4935 0.4609 0.4449 0.0156  0.0514  0.0397  104 GLU   B C   
5728 O O   A GLU   B 104 ? 0.4924 0.4401 0.4369 0.0353  0.1735  0.0785  104 GLU   B O   
5729 O O   B GLU   B 104 ? 0.4947 0.4628 0.4487 0.0147  0.0518  0.0387  104 GLU   B O   
5730 C CB  A GLU   B 104 ? 0.4756 0.4161 0.3847 0.0926  0.0759  0.0266  104 GLU   B CB  
5731 C CB  B GLU   B 104 ? 0.4890 0.4525 0.4139 0.0224  0.0304  0.0323  104 GLU   B CB  
5732 C CG  A GLU   B 104 ? 0.4629 0.4008 0.3652 0.1269  0.0302  -0.0133 104 GLU   B CG  
5733 C CG  B GLU   B 104 ? 0.4823 0.4467 0.4004 0.0238  0.0141  0.0156  104 GLU   B CG  
5734 C CD  A GLU   B 104 ? 0.4546 0.3900 0.3412 0.1536  -0.0088 -0.0413 104 GLU   B CD  
5735 C CD  B GLU   B 104 ? 0.4786 0.4428 0.3891 0.0246  0.0009  0.0026  104 GLU   B CD  
5736 O OE1 A GLU   B 104 ? 0.4438 0.3781 0.2864 0.1705  -0.0056 -0.0486 104 GLU   B OE1 
5737 O OE1 B GLU   B 104 ? 0.4763 0.4396 0.3772 0.0244  -0.0006 -0.0001 104 GLU   B OE1 
5738 O OE2 A GLU   B 104 ? 0.4561 0.3930 0.3367 0.1568  -0.0401 -0.0581 104 GLU   B OE2 
5739 O OE2 B GLU   B 104 ? 0.4789 0.4434 0.3847 0.0254  -0.0082 -0.0044 104 GLU   B OE2 
5752 N N   A ASP   B 105 ? 0.4846 0.4296 0.3918 0.0265  0.2107  0.0872  105 ASP   B N   
5753 N N   B ASP   B 105 ? 0.4862 0.4589 0.4460 0.0114  0.0544  0.0312  105 ASP   B N   
5754 C CA  A ASP   B 105 ? 0.4843 0.4282 0.4147 0.0139  0.2367  0.0664  105 ASP   B CA  
5755 C CA  B ASP   B 105 ? 0.4800 0.4567 0.4576 0.0069  0.0557  0.0192  105 ASP   B CA  
5756 C C   A ASP   B 105 ? 0.4635 0.3981 0.3900 -0.0067 0.2420  0.0552  105 ASP   B C   
5757 C C   B ASP   B 105 ? 0.4683 0.4462 0.4353 0.0014  0.0560  0.0120  105 ASP   B C   
5758 O O   A ASP   B 105 ? 0.4453 0.3922 0.3787 -0.0021 0.2380  0.0527  105 ASP   B O   
5759 O O   B ASP   B 105 ? 0.4688 0.4463 0.4268 0.0015  0.0575  0.0132  105 ASP   B O   
5760 C CB  A ASP   B 105 ? 0.5007 0.4532 0.4851 0.0246  0.2456  0.0458  105 ASP   B CB  
5761 C CB  B ASP   B 105 ? 0.4847 0.4643 0.4862 0.0089  0.0568  0.0137  105 ASP   B CB  
5762 C CG  A ASP   B 105 ? 0.5138 0.4740 0.5609 0.0284  0.2577  0.0320  105 ASP   B CG  
5763 C CG  B ASP   B 105 ? 0.4892 0.4706 0.5169 0.0095  0.0586  0.0099  105 ASP   B CG  
5764 O OD1 A ASP   B 105 ? 0.5113 0.4779 0.5632 0.0228  0.2866  0.0446  105 ASP   B OD1 
5765 O OD1 B ASP   B 105 ? 0.4903 0.4729 0.5253 0.0086  0.0606  0.0105  105 ASP   B OD1 
5766 O OD2 A ASP   B 105 ? 0.5223 0.4854 0.6130 0.0369  0.2392  0.0141  105 ASP   B OD2 
5767 O OD2 B ASP   B 105 ? 0.4900 0.4728 0.5300 0.0106  0.0579  0.0077  105 ASP   B OD2 
5776 N N   A ILE   B 106 ? 0.4580 0.3719 0.3941 -0.0239 0.2239  0.0493  106 ILE   B N   
5777 N N   B ILE   B 106 ? 0.4559 0.4349 0.4178 -0.0025 0.0534  0.0060  106 ILE   B N   
5778 C CA  A ILE   B 106 ? 0.4373 0.3397 0.4018 -0.0517 0.2215  0.0453  106 ILE   B CA  
5779 C CA  B ILE   B 106 ? 0.4410 0.4228 0.4090 -0.0065 0.0533  0.0012  106 ILE   B CA  
5780 C C   A ILE   B 106 ? 0.3975 0.3303 0.3846 -0.0516 0.2197  0.0292  106 ILE   B C   
5781 C C   B ILE   B 106 ? 0.4214 0.4116 0.4012 -0.0064 0.0562  -0.0019 106 ILE   B C   
5782 O O   A ILE   B 106 ? 0.3835 0.3093 0.3810 -0.0531 0.2124  0.0287  106 ILE   B O   
5783 O O   B ILE   B 106 ? 0.4204 0.4093 0.3983 -0.0078 0.0542  -0.0040 106 ILE   B O   
5784 C CB  A ILE   B 106 ? 0.4584 0.3216 0.4236 -0.0688 0.2119  0.0492  106 ILE   B CB  
5785 C CB  B ILE   B 106 ? 0.4447 0.4220 0.4090 -0.0096 0.0510  -0.0007 106 ILE   B CB  
5786 C CG1 A ILE   B 106 ? 0.4669 0.3167 0.4304 -0.0650 0.1956  0.0352  106 ILE   B CG1 
5787 C CG1 B ILE   B 106 ? 0.4447 0.4196 0.4078 -0.0095 0.0483  -0.0022 106 ILE   B CG1 
5788 C CG2 A ILE   B 106 ? 0.4649 0.3259 0.4479 -0.0755 0.2129  0.0524  106 ILE   B CG2 
5789 C CG2 B ILE   B 106 ? 0.4472 0.4246 0.4128 -0.0108 0.0511  -0.0011 106 ILE   B CG2 
5790 C CD1 A ILE   B 106 ? 0.4706 0.3183 0.4178 -0.0607 0.1914  0.0302  106 ILE   B CD1 
5791 C CD1 B ILE   B 106 ? 0.4444 0.4181 0.4070 -0.0091 0.0469  -0.0031 106 ILE   B CD1 
5814 N N   A GLN   B 107 ? 0.3799 0.3487 0.4013 -0.0494 0.2039  0.0226  107 GLN   B N   
5815 N N   B GLN   B 107 ? 0.4036 0.4037 0.4051 -0.0060 0.0614  -0.0014 107 GLN   B N   
5816 C CA  A GLN   B 107 ? 0.3591 0.3614 0.4089 -0.0472 0.1708  0.0209  107 GLN   B CA  
5817 C CA  B GLN   B 107 ? 0.3835 0.3929 0.4060 -0.0055 0.0656  0.0024  107 GLN   B CA  
5818 C C   A GLN   B 107 ? 0.3191 0.3385 0.3669 -0.0351 0.1387  0.0106  107 GLN   B C   
5819 C C   B GLN   B 107 ? 0.3421 0.3602 0.3631 -0.0050 0.0859  0.0062  107 GLN   B C   
5820 O O   A GLN   B 107 ? 0.3000 0.3410 0.3932 -0.0303 0.1136  -0.0204 107 GLN   B O   
5821 O O   B GLN   B 107 ? 0.3410 0.3633 0.3667 -0.0032 0.0792  -0.0013 107 GLN   B O   
5822 C CB  A GLN   B 107 ? 0.3948 0.4059 0.4943 -0.0448 0.1374  0.0174  107 GLN   B CB  
5823 C CB  B GLN   B 107 ? 0.4048 0.4137 0.4622 -0.0047 0.0492  0.0018  107 GLN   B CB  
5824 C CG  A GLN   B 107 ? 0.4291 0.4474 0.5695 -0.0406 0.0963  0.0147  107 GLN   B CG  
5825 C CG  B GLN   B 107 ? 0.4223 0.4308 0.5108 -0.0037 0.0339  0.0022  107 GLN   B CG  
5826 C CD  A GLN   B 107 ? 0.4550 0.4789 0.6285 -0.0401 0.0650  0.0130  107 GLN   B CD  
5827 C CD  B GLN   B 107 ? 0.4355 0.4436 0.5509 -0.0040 0.0219  0.0024  107 GLN   B CD  
5828 O OE1 A GLN   B 107 ? 0.4643 0.4898 0.6487 -0.0407 0.0606  0.0095  107 GLN   B OE1 
5829 O OE1 B GLN   B 107 ? 0.4397 0.4474 0.5640 -0.0048 0.0199  0.0023  107 GLN   B OE1 
5830 N NE2 A GLN   B 107 ? 0.4646 0.4881 0.6495 -0.0360 0.0491  0.0155  107 GLN   B NE2 
5831 N NE2 B GLN   B 107 ? 0.4406 0.4485 0.5656 -0.0028 0.0166  0.0029  107 GLN   B NE2 
5848 N N   . LEU   B 108 ? 0.2991 0.3235 0.3260 -0.0024 0.1132  0.0155  108 LEU   B N   
5849 C CA  . LEU   B 108 ? 0.2642 0.2893 0.2652 0.0176  0.0820  0.0370  108 LEU   B CA  
5850 C C   . LEU   B 108 ? 0.2093 0.2402 0.2482 0.0183  0.0474  0.0291  108 LEU   B C   
5851 O O   . LEU   B 108 ? 0.1940 0.2210 0.2329 0.0221  0.0381  0.0333  108 LEU   B O   
5852 C CB  . LEU   B 108 ? 0.2786 0.3031 0.2552 0.0277  0.0853  0.0608  108 LEU   B CB  
5853 C CG  . LEU   B 108 ? 0.2972 0.3308 0.2679 0.0365  0.0809  0.0388  108 LEU   B CG  
5854 C CD1 . LEU   B 108 ? 0.3057 0.3434 0.2636 0.0348  0.0881  0.0368  108 LEU   B CD1 
5855 C CD2 . LEU   B 108 ? 0.3077 0.3421 0.2730 0.0466  0.0592  0.0195  108 LEU   B CD2 
5868 N N   . LEU   B 109 ? 0.1850 0.2048 0.2454 0.0095  0.0392  0.0098  109 LEU   B N   
5869 C CA  . LEU   B 109 ? 0.1688 0.1679 0.2583 0.0029  0.0399  0.0353  109 LEU   B CA  
5870 C C   . LEU   B 109 ? 0.1621 0.1444 0.2590 -0.0034 0.0323  0.0227  109 LEU   B C   
5871 O O   . LEU   B 109 ? 0.1588 0.1433 0.2486 0.0020  0.0270  0.0312  109 LEU   B O   
5872 C CB  . LEU   B 109 ? 0.1728 0.1543 0.2823 0.0059  0.0244  0.0298  109 LEU   B CB  
5873 C CG  . LEU   B 109 ? 0.1668 0.1468 0.2737 0.0008  0.0263  0.0222  109 LEU   B CG  
5874 C CD1 . LEU   B 109 ? 0.1628 0.1596 0.2526 0.0143  0.0255  0.0330  109 LEU   B CD1 
5875 C CD2 . LEU   B 109 ? 0.1848 0.1480 0.2845 -0.0060 0.0259  0.0186  109 LEU   B CD2 
5887 N N   . LYS   B 110 ? 0.1628 0.1462 0.2440 -0.0121 0.0267  0.0269  110 LYS   B N   
5888 C CA  . LYS   B 110 ? 0.1479 0.1486 0.2535 -0.0110 0.0315  0.0254  110 LYS   B CA  
5889 C C   . LYS   B 110 ? 0.1507 0.1396 0.2438 -0.0068 0.0395  0.0178  110 LYS   B C   
5890 O O   . LYS   B 110 ? 0.1438 0.1507 0.2359 -0.0100 0.0226  0.0080  110 LYS   B O   
5891 C CB  . LYS   B 110 ? 0.1560 0.1475 0.2850 -0.0041 0.0386  0.0252  110 LYS   B CB  
5892 C CG  . LYS   B 110 ? 0.1597 0.1472 0.3012 -0.0104 0.0073  0.0290  110 LYS   B CG  
5893 C CD  . LYS   B 110 ? 0.1647 0.1469 0.3020 -0.0117 0.0064  0.0204  110 LYS   B CD  
5894 C CE  . LYS   B 110 ? 0.1654 0.1616 0.3331 -0.0096 0.0082  -0.0026 110 LYS   B CE  
5895 N NZ  . LYS   B 110 ? 0.1628 0.1759 0.3269 -0.0061 0.0029  0.0012  110 LYS   B NZ  
5909 N N   . SER   B 111 ? 0.1540 0.1409 0.2709 -0.0006 0.0439  0.0165  111 SER   B N   
5910 C CA  . SER   B 111 ? 0.1675 0.1522 0.2510 -0.0021 0.0363  0.0157  111 SER   B CA  
5911 C C   . SER   B 111 ? 0.1528 0.1504 0.2295 -0.0112 0.0212  0.0100  111 SER   B C   
5912 O O   . SER   B 111 ? 0.1439 0.1526 0.2394 -0.0117 0.0157  0.0059  111 SER   B O   
5913 C CB  . SER   B 111 ? 0.1784 0.1735 0.2698 0.0076  0.0494  0.0180  111 SER   B CB  
5914 O OG  . SER   B 111 ? 0.1992 0.2060 0.2574 0.0109  0.0447  0.0370  111 SER   B OG  
5920 N N   . ALA   B 112 ? 0.1444 0.1498 0.2329 0.0011  0.0308  0.0094  112 ALA   B N   
5921 C CA  . ALA   B 112 ? 0.1470 0.1552 0.2176 0.0001  0.0151  0.0012  112 ALA   B CA  
5922 C C   . ALA   B 112 ? 0.1278 0.1495 0.2237 -0.0021 0.0183  0.0073  112 ALA   B C   
5923 O O   . ALA   B 112 ? 0.1355 0.1524 0.2268 -0.0050 0.0168  0.0017  112 ALA   B O   
5924 C CB  . ALA   B 112 ? 0.1501 0.1620 0.2208 0.0052  0.0166  0.0111  112 ALA   B CB  
5930 N N   . TYR   B 113 ? 0.1318 0.1379 0.2272 -0.0062 0.0080  0.0115  113 TYR   B N   
5931 C CA  . TYR   B 113 ? 0.1357 0.1448 0.2147 -0.0067 0.0091  -0.0002 113 TYR   B CA  
5932 C C   . TYR   B 113 ? 0.1347 0.1241 0.2128 -0.0041 0.0092  0.0011  113 TYR   B C   
5933 O O   . TYR   B 113 ? 0.1391 0.1352 0.2063 -0.0043 0.0105  0.0002  113 TYR   B O   
5934 C CB  . TYR   B 113 ? 0.1380 0.1420 0.2184 -0.0087 0.0214  0.0112  113 TYR   B CB  
5935 C CG  . TYR   B 113 ? 0.1438 0.1514 0.2193 -0.0099 0.0082  0.0116  113 TYR   B CG  
5936 C CD1 . TYR   B 113 ? 0.1430 0.1548 0.2380 -0.0109 0.0160  0.0202  113 TYR   B CD1 
5937 C CD2 . TYR   B 113 ? 0.1461 0.1503 0.2212 -0.0112 0.0092  0.0156  113 TYR   B CD2 
5938 C CE1 . TYR   B 113 ? 0.1475 0.1535 0.2338 -0.0129 0.0140  0.0088  113 TYR   B CE1 
5939 C CE2 . TYR   B 113 ? 0.1500 0.1449 0.2338 0.0037  0.0014  0.0191  113 TYR   B CE2 
5940 C CZ  . TYR   B 113 ? 0.1405 0.1430 0.2459 -0.0028 0.0054  0.0194  113 TYR   B CZ  
5941 O OH  . TYR   B 113 ? 0.1565 0.1372 0.2686 0.0132  0.0300  0.0001  113 TYR   B OH  
5951 N N   . GLU   B 114 ? 0.1331 0.1307 0.2299 -0.0070 0.0059  0.0064  114 GLU   B N   
5952 C CA  . GLU   B 114 ? 0.1412 0.1265 0.2184 0.0076  0.0078  0.0029  114 GLU   B CA  
5953 C C   . GLU   B 114 ? 0.1435 0.1367 0.1946 0.0020  -0.0053 0.0002  114 GLU   B C   
5954 O O   . GLU   B 114 ? 0.1415 0.1347 0.2185 0.0067  -0.0089 0.0113  114 GLU   B O   
5955 C CB  . GLU   B 114 ? 0.1487 0.1332 0.2208 -0.0007 0.0148  0.0074  114 GLU   B CB  
5956 C CG  . GLU   B 114 ? 0.1515 0.1266 0.2277 -0.0049 0.0147  0.0054  114 GLU   B CG  
5957 C CD  . GLU   B 114 ? 0.1448 0.1315 0.2407 -0.0128 0.0175  0.0072  114 GLU   B CD  
5958 O OE1 . GLU   B 114 ? 0.1345 0.1446 0.2379 -0.0103 0.0237  0.0027  114 GLU   B OE1 
5959 O OE2 . GLU   B 114 ? 0.1456 0.1536 0.2618 -0.0211 0.0189  0.0109  114 GLU   B OE2 
5966 N N   . ASN   B 115 ? 0.1469 0.1252 0.1853 -0.0033 -0.0083 -0.0032 115 ASN   B N   
5967 C CA  . ASN   B 115 ? 0.1425 0.1310 0.1680 -0.0082 0.0025  0.0013  115 ASN   B CA  
5968 C C   . ASN   B 115 ? 0.1281 0.1412 0.1883 -0.0204 -0.0024 -0.0087 115 ASN   B C   
5969 O O   . ASN   B 115 ? 0.1443 0.1354 0.1956 -0.0155 0.0033  0.0028  115 ASN   B O   
5970 C CB  . ASN   B 115 ? 0.1592 0.1425 0.1938 -0.0192 -0.0018 0.0033  115 ASN   B CB  
5971 C CG  . ASN   B 115 ? 0.1570 0.1640 0.1867 -0.0137 0.0062  0.0030  115 ASN   B CG  
5972 O OD1 . ASN   B 115 ? 0.1951 0.1737 0.2146 -0.0055 0.0166  -0.0042 115 ASN   B OD1 
5973 N ND2 . ASN   B 115 ? 0.1507 0.1795 0.1817 -0.0141 0.0115  0.0138  115 ASN   B ND2 
5980 N N   . PHE   B 116 ? 0.1349 0.1416 0.1784 -0.0068 0.0012  -0.0104 116 PHE   B N   
5981 C CA  . PHE   B 116 ? 0.1414 0.1421 0.1876 -0.0065 -0.0083 -0.0135 116 PHE   B CA  
5982 C C   . PHE   B 116 ? 0.1369 0.1195 0.1925 -0.0153 -0.0089 0.0070  116 PHE   B C   
5983 O O   . PHE   B 116 ? 0.1421 0.1315 0.2026 -0.0069 -0.0058 0.0110  116 PHE   B O   
5984 C CB  . PHE   B 116 ? 0.1385 0.1296 0.1803 0.0002  -0.0099 0.0012  116 PHE   B CB  
5985 C CG  . PHE   B 116 ? 0.1252 0.1417 0.1821 -0.0077 0.0012  -0.0028 116 PHE   B CG  
5986 C CD1 . PHE   B 116 ? 0.1353 0.1380 0.1976 -0.0098 -0.0000 -0.0066 116 PHE   B CD1 
5987 C CD2 . PHE   B 116 ? 0.1306 0.1515 0.1708 -0.0028 0.0022  -0.0056 116 PHE   B CD2 
5988 C CE1 . PHE   B 116 ? 0.1419 0.1482 0.1871 -0.0066 -0.0259 -0.0103 116 PHE   B CE1 
5989 C CE2 . PHE   B 116 ? 0.1370 0.1467 0.1764 -0.0044 -0.0047 0.0105  116 PHE   B CE2 
5990 C CZ  . PHE   B 116 ? 0.1320 0.1546 0.1838 -0.0054 -0.0160 0.0039  116 PHE   B CZ  
6000 N N   . ASN   B 117 ? 0.1421 0.1275 0.2062 -0.0062 -0.0103 0.0083  117 ASN   B N   
6001 C CA  . ASN   B 117 ? 0.1495 0.1319 0.2115 -0.0039 -0.0114 0.0008  117 ASN   B CA  
6002 C C   . ASN   B 117 ? 0.1517 0.1232 0.2244 -0.0087 -0.0211 0.0054  117 ASN   B C   
6003 O O   . ASN   B 117 ? 0.1536 0.1378 0.2566 -0.0074 -0.0449 0.0183  117 ASN   B O   
6004 C CB  . ASN   B 117 ? 0.1493 0.1359 0.2185 -0.0052 -0.0068 -0.0122 117 ASN   B CB  
6005 C CG  . ASN   B 117 ? 0.1365 0.1335 0.2311 -0.0039 -0.0059 -0.0074 117 ASN   B CG  
6006 O OD1 . ASN   B 117 ? 0.1601 0.1389 0.2331 -0.0155 -0.0023 -0.0034 117 ASN   B OD1 
6007 N ND2 . ASN   B 117 ? 0.1428 0.1369 0.2239 -0.0042 -0.0050 -0.0043 117 ASN   B ND2 
6014 N N   . GLN   B 118 ? 0.1442 0.1261 0.2073 -0.0160 -0.0219 0.0035  118 GLN   B N   
6015 C CA  . GLN   B 118 ? 0.1547 0.1342 0.2394 -0.0046 -0.0226 0.0044  118 GLN   B CA  
6016 C C   . GLN   B 118 ? 0.1537 0.1384 0.2422 -0.0081 -0.0131 0.0066  118 GLN   B C   
6017 O O   . GLN   B 118 ? 0.1681 0.1439 0.2648 -0.0112 -0.0018 0.0113  118 GLN   B O   
6018 C CB  . GLN   B 118 ? 0.1603 0.1408 0.2420 -0.0067 -0.0252 -0.0007 118 GLN   B CB  
6019 C CG  . GLN   B 118 ? 0.1689 0.1482 0.2355 0.0011  -0.0124 -0.0052 118 GLN   B CG  
6020 C CD  . GLN   B 118 ? 0.1702 0.1424 0.2264 -0.0078 -0.0155 -0.0145 118 GLN   B CD  
6021 O OE1 . GLN   B 118 ? 0.1773 0.1428 0.2523 0.0006  0.0005  -0.0015 118 GLN   B OE1 
6022 N NE2 . GLN   B 118 ? 0.1815 0.1413 0.2262 -0.0015 -0.0140 0.0005  118 GLN   B NE2 
6031 N N   . HIS   B 119 ? 0.1665 0.1411 0.1915 -0.0088 -0.0123 0.0060  119 HIS   B N   
6032 C CA  . HIS   B 119 ? 0.1772 0.1484 0.1812 -0.0107 -0.0216 0.0114  119 HIS   B CA  
6033 C C   . HIS   B 119 ? 0.1795 0.1489 0.1774 -0.0124 -0.0389 0.0023  119 HIS   B C   
6034 O O   . HIS   B 119 ? 0.1808 0.1449 0.2021 -0.0331 -0.0303 0.0055  119 HIS   B O   
6035 C CB  . HIS   B 119 ? 0.1744 0.1401 0.1895 -0.0038 -0.0301 0.0056  119 HIS   B CB  
6036 C CG  . HIS   B 119 ? 0.1693 0.1729 0.2111 0.0080  -0.0551 -0.0076 119 HIS   B CG  
6037 N ND1 . HIS   B 119 ? 0.1851 0.1857 0.2397 0.0063  -0.0502 -0.0277 119 HIS   B ND1 
6038 C CD2 . HIS   B 119 ? 0.1844 0.1938 0.2170 0.0393  -0.0689 -0.0107 119 HIS   B CD2 
6039 C CE1 . HIS   B 119 ? 0.2073 0.2015 0.2498 0.0155  -0.0571 -0.0431 119 HIS   B CE1 
6040 N NE2 . HIS   B 119 ? 0.2041 0.2193 0.2403 0.0305  -0.0583 -0.0346 119 HIS   B NE2 
6048 N N   A GLU   B 120 ? 0.2014 0.1444 0.1812 -0.0108 -0.0549 0.0168  120 GLU   B N   
6049 N N   B GLU   B 120 ? 0.2022 0.1703 0.2023 -0.0141 -0.0366 0.0063  120 GLU   B N   
6050 C CA  A GLU   B 120 ? 0.2301 0.1673 0.1833 -0.0032 -0.0637 0.0446  120 GLU   B CA  
6051 C CA  B GLU   B 120 ? 0.2233 0.1941 0.2293 -0.0136 -0.0355 0.0117  120 GLU   B CA  
6052 C C   A GLU   B 120 ? 0.2009 0.1588 0.1777 -0.0179 -0.0538 0.0263  120 GLU   B C   
6053 C C   B GLU   B 120 ? 0.2065 0.1772 0.1995 -0.0212 -0.0368 0.0154  120 GLU   B C   
6054 O O   A GLU   B 120 ? 0.1929 0.1710 0.1880 -0.0207 -0.0544 0.0189  120 GLU   B O   
6055 O O   B GLU   B 120 ? 0.2063 0.1816 0.1975 -0.0215 -0.0375 0.0131  120 GLU   B O   
6056 C CB  A GLU   B 120 ? 0.2987 0.2104 0.2666 0.0213  -0.0865 0.0662  120 GLU   B CB  
6057 C CB  B GLU   B 120 ? 0.2627 0.2338 0.3032 -0.0040 -0.0371 0.0124  120 GLU   B CB  
6058 C CG  A GLU   B 120 ? 0.3573 0.2891 0.3827 0.0320  -0.0942 0.0776  120 GLU   B CG  
6059 C CG  B GLU   B 120 ? 0.2974 0.2770 0.3795 0.0015  -0.0366 0.0159  120 GLU   B CG  
6060 C CD  A GLU   B 120 ? 0.4019 0.3538 0.4896 0.0372  -0.0973 0.0875  120 GLU   B CD  
6061 C CD  B GLU   B 120 ? 0.3254 0.3123 0.4450 0.0042  -0.0339 0.0201  120 GLU   B CD  
6062 O OE1 A GLU   B 120 ? 0.4223 0.3753 0.5269 0.0323  -0.0930 0.0996  120 GLU   B OE1 
6063 O OE1 B GLU   B 120 ? 0.3358 0.3226 0.4700 0.0036  -0.0329 0.0232  120 GLU   B OE1 
6064 O OE2 A GLU   B 120 ? 0.4214 0.3818 0.5408 0.0389  -0.0941 0.0784  120 GLU   B OE2 
6065 O OE2 B GLU   B 120 ? 0.3353 0.3242 0.4694 0.0048  -0.0336 0.0209  120 GLU   B OE2 
6078 N N   . VAL   B 121 ? 0.1898 0.1578 0.1795 -0.0283 -0.0394 0.0249  121 VAL   B N   
6079 C CA  . VAL   B 121 ? 0.1767 0.1668 0.1537 -0.0254 -0.0355 0.0307  121 VAL   B CA  
6080 C C   . VAL   B 121 ? 0.1742 0.1585 0.1554 -0.0237 -0.0337 0.0243  121 VAL   B C   
6081 O O   . VAL   B 121 ? 0.1808 0.1542 0.1770 -0.0399 -0.0367 0.0160  121 VAL   B O   
6082 C CB  . VAL   B 121 ? 0.2089 0.2080 0.1720 -0.0157 -0.0437 0.0329  121 VAL   B CB  
6083 C CG1 . VAL   B 121 ? 0.2216 0.2229 0.2218 -0.0304 -0.0332 0.0247  121 VAL   B CG1 
6084 C CG2 . VAL   B 121 ? 0.2389 0.2395 0.1717 -0.0012 -0.0295 0.0108  121 VAL   B CG2 
6095 N N   . LEU   B 122 ? 0.1662 0.1461 0.1576 -0.0135 -0.0324 0.0162  122 LEU   B N   
6096 C CA  . LEU   B 122 ? 0.1504 0.1597 0.1405 -0.0154 -0.0250 0.0133  122 LEU   B CA  
6097 C C   . LEU   B 122 ? 0.1532 0.1510 0.1481 -0.0273 -0.0283 0.0175  122 LEU   B C   
6098 O O   . LEU   B 122 ? 0.1623 0.1495 0.1791 -0.0392 -0.0309 0.0056  122 LEU   B O   
6099 C CB  . LEU   B 122 ? 0.1797 0.1737 0.1841 -0.0036 -0.0387 0.0112  122 LEU   B CB  
6100 C CG  . LEU   B 122 ? 0.1663 0.1807 0.2022 -0.0177 -0.0217 0.0108  122 LEU   B CG  
6101 C CD1 . LEU   B 122 ? 0.1652 0.2020 0.1868 -0.0308 -0.0321 0.0131  122 LEU   B CD1 
6102 C CD2 . LEU   B 122 ? 0.1764 0.1796 0.1757 -0.0111 -0.0186 -0.0095 122 LEU   B CD2 
6114 N N   . LEU   B 123 ? 0.1550 0.1372 0.1485 -0.0257 -0.0235 0.0118  123 LEU   B N   
6115 C CA  . LEU   B 123 ? 0.1642 0.1418 0.1532 -0.0326 -0.0305 -0.0003 123 LEU   B CA  
6116 C C   . LEU   B 123 ? 0.1549 0.1388 0.1439 -0.0328 -0.0253 0.0021  123 LEU   B C   
6117 O O   . LEU   B 123 ? 0.1584 0.1432 0.1475 -0.0363 -0.0235 0.0020  123 LEU   B O   
6118 C CB  . LEU   B 123 ? 0.1654 0.1477 0.1690 -0.0333 -0.0206 -0.0019 123 LEU   B CB  
6119 C CG  . LEU   B 123 ? 0.1646 0.1539 0.1718 -0.0272 -0.0126 0.0047  123 LEU   B CG  
6120 C CD1 . LEU   B 123 ? 0.1716 0.1632 0.1913 -0.0258 -0.0072 -0.0036 123 LEU   B CD1 
6121 C CD2 . LEU   B 123 ? 0.1813 0.1599 0.1840 -0.0234 -0.0086 0.0165  123 LEU   B CD2 
6133 N N   . ALA   B 124 ? 0.1520 0.1373 0.1465 -0.0257 -0.0214 0.0005  124 ALA   B N   
6134 C CA  . ALA   B 124 ? 0.1437 0.1372 0.1583 -0.0149 -0.0156 -0.0016 124 ALA   B CA  
6135 C C   . ALA   B 124 ? 0.1386 0.1288 0.1393 -0.0208 -0.0156 0.0054  124 ALA   B C   
6136 O O   . ALA   B 124 ? 0.1506 0.1356 0.1702 -0.0196 -0.0234 0.0034  124 ALA   B O   
6137 C CB  . ALA   B 124 ? 0.1469 0.1385 0.1762 0.0012  -0.0074 -0.0032 124 ALA   B CB  
6143 N N   . PRO   B 125 ? 0.1493 0.1312 0.1455 -0.0211 -0.0231 0.0162  125 PRO   B N   
6144 C CA  . PRO   B 125 ? 0.1640 0.1441 0.1587 -0.0265 -0.0224 0.0260  125 PRO   B CA  
6145 C C   . PRO   B 125 ? 0.1450 0.1444 0.1976 -0.0201 -0.0089 0.0195  125 PRO   B C   
6146 O O   . PRO   B 125 ? 0.1489 0.1426 0.2053 -0.0171 -0.0074 0.0185  125 PRO   B O   
6147 C CB  . PRO   B 125 ? 0.1660 0.1681 0.1691 -0.0214 -0.0290 0.0361  125 PRO   B CB  
6148 C CG  . PRO   B 125 ? 0.1681 0.1687 0.1589 -0.0295 -0.0261 0.0231  125 PRO   B CG  
6149 C CD  . PRO   B 125 ? 0.1598 0.1523 0.1483 -0.0420 -0.0195 0.0122  125 PRO   B CD  
6157 N N   . LEU   B 126 ? 0.1548 0.1351 0.2133 -0.0244 0.0057  0.0177  126 LEU   B N   
6158 C CA  . LEU   B 126 ? 0.1697 0.1411 0.2148 -0.0184 0.0190  0.0162  126 LEU   B CA  
6159 C C   . LEU   B 126 ? 0.1646 0.1421 0.2115 0.0028  0.0166  0.0205  126 LEU   B C   
6160 O O   . LEU   B 126 ? 0.1804 0.1809 0.2373 0.0244  -0.0117 -0.0020 126 LEU   B O   
6161 C CB  . LEU   B 126 ? 0.1837 0.1302 0.2546 -0.0226 0.0277  0.0106  126 LEU   B CB  
6162 C CG  . LEU   B 126 ? 0.2090 0.1451 0.2790 -0.0253 0.0201  -0.0095 126 LEU   B CG  
6163 C CD1 . LEU   B 126 ? 0.2257 0.1587 0.3364 -0.0259 0.0160  -0.0180 126 LEU   B CD1 
6164 C CD2 . LEU   B 126 ? 0.2083 0.1636 0.2724 -0.0281 0.0159  -0.0174 126 LEU   B CD2 
6176 N N   . LEU   B 127 ? 0.1617 0.1322 0.2175 0.0052  0.0238  0.0144  127 LEU   B N   
6177 C CA  . LEU   B 127 ? 0.1576 0.1466 0.2196 -0.0051 0.0363  0.0239  127 LEU   B CA  
6178 C C   . LEU   B 127 ? 0.1515 0.1462 0.2297 -0.0057 0.0220  0.0318  127 LEU   B C   
6179 O O   . LEU   B 127 ? 0.1602 0.1465 0.2424 -0.0180 0.0114  0.0277  127 LEU   B O   
6180 C CB  . LEU   B 127 ? 0.1743 0.1528 0.2400 -0.0066 0.0312  0.0153  127 LEU   B CB  
6181 C CG  . LEU   B 127 ? 0.1863 0.1453 0.2437 -0.0083 0.0343  0.0179  127 LEU   B CG  
6182 C CD1 . LEU   B 127 ? 0.1955 0.1544 0.2491 0.0053  0.0179  0.0021  127 LEU   B CD1 
6183 C CD2 . LEU   B 127 ? 0.1946 0.1563 0.2697 -0.0168 0.0321  0.0263  127 LEU   B CD2 
6195 N N   . SER   B 128 ? 0.1570 0.1495 0.2271 0.0032  0.0020  0.0171  128 SER   B N   
6196 C CA  . SER   B 128 ? 0.1779 0.1570 0.2226 0.0165  -0.0065 0.0333  128 SER   B CA  
6197 C C   . SER   B 128 ? 0.1843 0.1614 0.2722 0.0113  -0.0267 0.0235  128 SER   B C   
6198 O O   . SER   B 128 ? 0.2086 0.1649 0.3150 0.0036  -0.0260 0.0393  128 SER   B O   
6199 C CB  . SER   B 128 ? 0.1828 0.1656 0.2146 0.0098  0.0053  0.0281  128 SER   B CB  
6200 O OG  . SER   B 128 ? 0.1823 0.1756 0.2252 0.0095  0.0174  0.0404  128 SER   B OG  
6206 N N   . ALA   B 129 ? 0.1953 0.1710 0.3098 0.0284  -0.0147 -0.0005 129 ALA   B N   
6207 C CA  . ALA   B 129 ? 0.2073 0.1782 0.3148 0.0355  -0.0137 -0.0135 129 ALA   B CA  
6208 C C   . ALA   B 129 ? 0.1864 0.1730 0.3007 0.0220  0.0046  -0.0068 129 ALA   B C   
6209 O O   . ALA   B 129 ? 0.1890 0.1715 0.2862 0.0178  -0.0020 0.0066  129 ALA   B O   
6210 C CB  . ALA   B 129 ? 0.2336 0.2018 0.3392 0.0328  -0.0018 -0.0283 129 ALA   B CB  
6216 N N   . GLY   B 130 ? 0.1891 0.1686 0.3006 0.0307  0.0056  -0.0094 130 GLY   B N   
6217 C CA  . GLY   B 130 ? 0.1895 0.1735 0.3132 0.0261  0.0261  -0.0011 130 GLY   B CA  
6218 C C   . GLY   B 130 ? 0.1961 0.1773 0.3030 0.0129  0.0204  0.0133  130 GLY   B C   
6219 O O   . GLY   B 130 ? 0.2040 0.1867 0.3136 0.0123  0.0072  0.0243  130 GLY   B O   
6223 N N   . ILE   B 131 ? 0.2023 0.1875 0.3011 0.0255  0.0175  0.0147  131 ILE   B N   
6224 C CA  . ILE   B 131 ? 0.2287 0.1995 0.3055 0.0243  0.0107  0.0202  131 ILE   B CA  
6225 C C   . ILE   B 131 ? 0.2400 0.1817 0.2671 0.0194  0.0103  0.0278  131 ILE   B C   
6226 O O   . ILE   B 131 ? 0.2739 0.2065 0.2869 0.0153  -0.0095 0.0344  131 ILE   B O   
6227 C CB  . ILE   B 131 ? 0.2302 0.2271 0.3508 0.0233  -0.0059 0.0350  131 ILE   B CB  
6228 C CG1 . ILE   B 131 ? 0.2332 0.2381 0.3750 -0.0030 -0.0104 0.0390  131 ILE   B CG1 
6229 C CG2 . ILE   B 131 ? 0.2383 0.2471 0.3809 0.0367  -0.0014 0.0336  131 ILE   B CG2 
6230 C CD1 . ILE   B 131 ? 0.2418 0.2444 0.3925 -0.0156 -0.0221 0.0491  131 ILE   B CD1 
6242 N N   . PHE   B 132 ? 0.2293 0.1696 0.2505 0.0137  0.0211  0.0231  132 PHE   B N   
6243 C CA  . PHE   B 132 ? 0.2415 0.1793 0.2579 0.0076  0.0439  0.0220  132 PHE   B CA  
6244 C C   . PHE   B 132 ? 0.2627 0.1987 0.2807 0.0038  0.0555  0.0132  132 PHE   B C   
6245 O O   . PHE   B 132 ? 0.2764 0.2184 0.3077 0.0012  0.0652  0.0227  132 PHE   B O   
6246 C CB  . PHE   B 132 ? 0.2230 0.1858 0.2374 0.0049  0.0498  0.0234  132 PHE   B CB  
6247 C CG  . PHE   B 132 ? 0.2110 0.1970 0.2232 0.0121  0.0278  0.0285  132 PHE   B CG  
6248 C CD1 . PHE   B 132 ? 0.2149 0.2013 0.2589 0.0047  0.0333  0.0361  132 PHE   B CD1 
6249 C CD2 . PHE   B 132 ? 0.2068 0.1971 0.1962 0.0264  0.0191  0.0321  132 PHE   B CD2 
6250 C CE1 . PHE   B 132 ? 0.2192 0.2091 0.2698 -0.0026 0.0227  0.0374  132 PHE   B CE1 
6251 C CE2 . PHE   B 132 ? 0.2204 0.2122 0.2083 0.0237  0.0126  0.0228  132 PHE   B CE2 
6252 C CZ  . PHE   B 132 ? 0.2251 0.2170 0.2483 0.0072  0.0008  0.0287  132 PHE   B CZ  
6262 N N   . GLY   B 133 ? 0.2580 0.1879 0.2777 -0.0092 0.0323  0.0445  133 GLY   B N   
6263 C CA  . GLY   B 133 ? 0.2635 0.2011 0.2994 -0.0338 0.0408  0.0517  133 GLY   B CA  
6264 C C   . GLY   B 133 ? 0.2670 0.2098 0.3047 -0.0459 0.0527  0.0580  133 GLY   B C   
6265 O O   . GLY   B 133 ? 0.2887 0.2183 0.3402 -0.0542 0.0525  0.0542  133 GLY   B O   
6269 N N   . ALA   B 134 ? 0.2491 0.2087 0.2912 -0.0394 0.0518  0.0443  134 ALA   B N   
6270 C CA  . ALA   B 134 ? 0.2505 0.2086 0.2925 -0.0301 0.0523  0.0345  134 ALA   B CA  
6271 C C   . ALA   B 134 ? 0.2535 0.1953 0.2957 -0.0235 0.0426  0.0431  134 ALA   B C   
6272 O O   . ALA   B 134 ? 0.2559 0.2089 0.3023 0.0004  0.0375  0.0376  134 ALA   B O   
6273 C CB  . ALA   B 134 ? 0.2469 0.2083 0.2973 -0.0175 0.0356  0.0207  134 ALA   B CB  
6279 N N   . ASP   B 135 ? 0.2685 0.1906 0.3028 -0.0245 0.0280  0.0466  135 ASP   B N   
6280 C CA  . ASP   B 135 ? 0.2855 0.1857 0.3291 -0.0237 0.0138  0.0448  135 ASP   B CA  
6281 C C   . ASP   B 135 ? 0.2538 0.1740 0.3129 -0.0055 0.0065  0.0394  135 ASP   B C   
6282 O O   . ASP   B 135 ? 0.2337 0.1697 0.3252 -0.0074 0.0143  0.0300  135 ASP   B O   
6283 C CB  . ASP   B 135 ? 0.3261 0.1963 0.3567 -0.0487 0.0033  0.0480  135 ASP   B CB  
6284 C CG  . ASP   B 135 ? 0.3549 0.1927 0.3995 -0.0731 -0.0033 0.0527  135 ASP   B CG  
6285 O OD1 . ASP   B 135 ? 0.3677 0.1835 0.3994 -0.0412 -0.0206 0.0417  135 ASP   B OD1 
6286 O OD2 . ASP   B 135 ? 0.3795 0.2304 0.4566 -0.0885 -0.0026 0.0408  135 ASP   B OD2 
6291 N N   . PRO   B 136 ? 0.2406 0.1778 0.3216 0.0200  -0.0244 0.0335  136 PRO   B N   
6292 C CA  . PRO   B 136 ? 0.2143 0.1640 0.3140 0.0222  -0.0241 0.0144  136 PRO   B CA  
6293 C C   . PRO   B 136 ? 0.1858 0.1569 0.3218 0.0172  -0.0159 0.0192  136 PRO   B C   
6294 O O   . PRO   B 136 ? 0.1724 0.1581 0.3096 0.0143  -0.0097 0.0150  136 PRO   B O   
6295 C CB  . PRO   B 136 ? 0.2231 0.1839 0.3184 0.0354  -0.0336 -0.0019 136 PRO   B CB  
6296 C CG  . PRO   B 136 ? 0.2483 0.1981 0.3487 0.0362  -0.0175 -0.0005 136 PRO   B CG  
6297 C CD  . PRO   B 136 ? 0.2511 0.1917 0.3336 0.0414  -0.0094 0.0157  136 PRO   B CD  
6305 N N   . ILE   B 137 ? 0.2000 0.1517 0.3288 0.0045  -0.0116 0.0066  137 ILE   B N   
6306 C CA  . ILE   B 137 ? 0.2086 0.1460 0.3303 -0.0038 -0.0073 0.0025  137 ILE   B CA  
6307 C C   . ILE   B 137 ? 0.1979 0.1422 0.3167 -0.0145 0.0052  0.0039  137 ILE   B C   
6308 O O   . ILE   B 137 ? 0.1874 0.1502 0.3035 -0.0116 -0.0078 0.0059  137 ILE   B O   
6309 C CB  . ILE   B 137 ? 0.2352 0.1490 0.3751 -0.0040 -0.0091 -0.0006 137 ILE   B CB  
6310 C CG1 . ILE   B 137 ? 0.2558 0.1765 0.4183 0.0073  0.0009  -0.0076 137 ILE   B CG1 
6311 C CG2 . ILE   B 137 ? 0.2436 0.1560 0.3849 -0.0351 -0.0153 -0.0010 137 ILE   B CG2 
6312 C CD1 . ILE   B 137 ? 0.2754 0.1997 0.4688 0.0171  0.0004  -0.0031 137 ILE   B CD1 
6324 N N   . HIS   B 138 ? 0.2018 0.1497 0.3297 -0.0129 0.0223  0.0094  138 HIS   B N   
6325 C CA  . HIS   B 138 ? 0.2123 0.1542 0.3316 -0.0094 0.0391  0.0152  138 HIS   B CA  
6326 C C   . HIS   B 138 ? 0.1956 0.1462 0.3228 -0.0153 0.0266  0.0264  138 HIS   B C   
6327 O O   . HIS   B 138 ? 0.1889 0.1576 0.3476 0.0010  0.0385  0.0307  138 HIS   B O   
6328 C CB  . HIS   B 138 ? 0.2474 0.1723 0.3507 -0.0173 0.0714  0.0232  138 HIS   B CB  
6329 C CG  . HIS   B 138 ? 0.2780 0.1887 0.3599 -0.0137 0.0970  0.0403  138 HIS   B CG  
6330 N ND1 . HIS   B 138 ? 0.2892 0.2077 0.3873 -0.0078 0.1093  0.0349  138 HIS   B ND1 
6331 C CD2 . HIS   B 138 ? 0.3022 0.1973 0.3560 -0.0074 0.1031  0.0399  138 HIS   B CD2 
6332 C CE1 . HIS   B 138 ? 0.2971 0.2035 0.3792 -0.0034 0.1170  0.0420  138 HIS   B CE1 
6333 N NE2 . HIS   B 138 ? 0.3084 0.1971 0.3543 0.0015  0.1153  0.0340  138 HIS   B NE2 
6341 N N   . SER   B 139 ? 0.1882 0.1394 0.2983 -0.0069 0.0132  0.0167  139 SER   B N   
6342 C CA  . SER   B 139 ? 0.1871 0.1417 0.2708 -0.0050 0.0196  0.0116  139 SER   B CA  
6343 C C   . SER   B 139 ? 0.1673 0.1391 0.2762 0.0023  0.0135  0.0104  139 SER   B C   
6344 O O   . SER   B 139 ? 0.1675 0.1380 0.2816 0.0010  0.0018  0.0146  139 SER   B O   
6345 C CB  . SER   B 139 ? 0.1923 0.1472 0.2799 0.0012  0.0003  0.0113  139 SER   B CB  
6346 O OG  . SER   B 139 ? 0.1959 0.1425 0.2893 -0.0014 -0.0117 0.0266  139 SER   B OG  
6352 N N   . LEU   B 140 ? 0.1662 0.1295 0.2775 -0.0085 0.0215  0.0050  140 LEU   B N   
6353 C CA  . LEU   B 140 ? 0.1584 0.1266 0.2900 -0.0051 0.0125  0.0004  140 LEU   B CA  
6354 C C   . LEU   B 140 ? 0.1505 0.1276 0.3003 -0.0017 -0.0069 -0.0022 140 LEU   B C   
6355 O O   . LEU   B 140 ? 0.1537 0.1448 0.2892 -0.0034 -0.0049 0.0110  140 LEU   B O   
6356 C CB  . LEU   B 140 ? 0.1604 0.1369 0.2946 -0.0077 0.0211  -0.0009 140 LEU   B CB  
6357 C CG  . LEU   B 140 ? 0.1633 0.1404 0.2828 -0.0178 -0.0017 0.0102  140 LEU   B CG  
6358 C CD1 . LEU   B 140 ? 0.1789 0.1536 0.3007 -0.0183 0.0039  0.0086  140 LEU   B CD1 
6359 C CD2 . LEU   B 140 ? 0.1949 0.1580 0.2836 -0.0076 -0.0033 -0.0005 140 LEU   B CD2 
6371 N N   . ARG   B 141 ? 0.1488 0.1265 0.3134 -0.0091 0.0041  0.0061  141 ARG   B N   
6372 C CA  . ARG   B 141 ? 0.1488 0.1298 0.3436 -0.0224 0.0209  0.0034  141 ARG   B CA  
6373 C C   . ARG   B 141 ? 0.1403 0.1274 0.3322 -0.0137 0.0126  0.0009  141 ARG   B C   
6374 O O   . ARG   B 141 ? 0.1512 0.1362 0.3364 -0.0168 0.0051  -0.0088 141 ARG   B O   
6375 C CB  . ARG   B 141 ? 0.1685 0.1553 0.3611 -0.0239 0.0325  -0.0093 141 ARG   B CB  
6376 C CG  . ARG   B 141 ? 0.2074 0.1865 0.3667 -0.0203 0.0318  -0.0121 141 ARG   B CG  
6377 C CD  . ARG   B 141 ? 0.2480 0.1974 0.3610 -0.0197 0.0238  -0.0170 141 ARG   B CD  
6378 N NE  . ARG   B 141 ? 0.2705 0.1993 0.3544 -0.0340 0.0226  -0.0232 141 ARG   B NE  
6379 C CZ  . ARG   B 141 ? 0.2950 0.1881 0.3275 -0.0356 0.0215  -0.0286 141 ARG   B CZ  
6380 N NH1 . ARG   B 141 ? 0.3151 0.1772 0.3180 -0.0306 0.0146  -0.0211 141 ARG   B NH1 
6381 N NH2 . ARG   B 141 ? 0.3013 0.1893 0.3449 -0.0288 0.0044  -0.0238 141 ARG   B NH2 
6395 N N   . VAL   B 142 ? 0.1580 0.1334 0.3205 -0.0091 0.0122  -0.0009 142 VAL   B N   
6396 C CA  . VAL   B 142 ? 0.1573 0.1365 0.3055 -0.0041 0.0314  -0.0000 142 VAL   B CA  
6397 C C   . VAL   B 142 ? 0.1417 0.1437 0.2913 -0.0084 0.0107  -0.0062 142 VAL   B C   
6398 O O   . VAL   B 142 ? 0.1516 0.1377 0.3053 0.0044  0.0031  -0.0030 142 VAL   B O   
6399 C CB  . VAL   B 142 ? 0.1688 0.1490 0.3122 -0.0007 0.0256  0.0080  142 VAL   B CB  
6400 C CG1 . VAL   B 142 ? 0.1660 0.1418 0.3072 0.0106  0.0240  0.0018  142 VAL   B CG1 
6401 C CG2 . VAL   B 142 ? 0.1823 0.1558 0.3116 -0.0040 0.0105  0.0186  142 VAL   B CG2 
6411 N N   . CYS   B 143 ? 0.1406 0.1476 0.2714 -0.0090 0.0110  0.0070  143 CYS   B N   
6412 C CA  . CYS   B 143 ? 0.1416 0.1426 0.2612 -0.0097 0.0017  0.0019  143 CYS   B CA  
6413 C C   . CYS   B 143 ? 0.1340 0.1537 0.2621 -0.0034 -0.0061 -0.0114 143 CYS   B C   
6414 O O   . CYS   B 143 ? 0.1436 0.1573 0.2652 0.0017  -0.0172 -0.0102 143 CYS   B O   
6415 C CB  . CYS   B 143 ? 0.1453 0.1553 0.2674 -0.0049 -0.0175 -0.0056 143 CYS   B CB  
6416 S SG  . CYS   B 143 ? 0.1555 0.1584 0.2593 -0.0090 0.0005  0.0064  143 CYS   B SG  
6422 N N   . VAL   B 144 ? 0.1399 0.1500 0.2974 -0.0157 -0.0105 -0.0255 144 VAL   B N   
6423 C CA  . VAL   B 144 ? 0.1487 0.1463 0.3274 -0.0217 -0.0254 -0.0253 144 VAL   B CA  
6424 C C   . VAL   B 144 ? 0.1431 0.1448 0.3452 -0.0116 -0.0246 -0.0049 144 VAL   B C   
6425 O O   . VAL   B 144 ? 0.1487 0.1600 0.3604 0.0020  -0.0261 0.0151  144 VAL   B O   
6426 C CB  . VAL   B 144 ? 0.1766 0.1662 0.3807 -0.0151 -0.0276 -0.0415 144 VAL   B CB  
6427 C CG1 . VAL   B 144 ? 0.1964 0.2049 0.4077 -0.0203 -0.0207 -0.0361 144 VAL   B CG1 
6428 C CG2 . VAL   B 144 ? 0.1883 0.1635 0.3764 -0.0059 -0.0326 -0.0455 144 VAL   B CG2 
6438 N N   . ASP   B 145 ? 0.1449 0.1394 0.3655 -0.0075 -0.0136 -0.0271 145 ASP   B N   
6439 C CA  . ASP   B 145 ? 0.1526 0.1333 0.3845 -0.0094 0.0082  -0.0114 145 ASP   B CA  
6440 C C   . ASP   B 145 ? 0.1596 0.1384 0.3498 -0.0094 0.0135  -0.0145 145 ASP   B C   
6441 O O   . ASP   B 145 ? 0.1587 0.1570 0.3869 -0.0123 0.0058  -0.0200 145 ASP   B O   
6442 C CB  . ASP   B 145 ? 0.1581 0.1529 0.4339 -0.0231 0.0143  -0.0060 145 ASP   B CB  
6443 C CG  . ASP   B 145 ? 0.1789 0.1614 0.4767 -0.0242 0.0358  -0.0032 145 ASP   B CG  
6444 O OD1 . ASP   B 145 ? 0.1813 0.1581 0.4610 -0.0254 -0.0039 -0.0126 145 ASP   B OD1 
6445 O OD2 . ASP   B 145 ? 0.2062 0.1606 0.5175 -0.0359 0.0626  -0.0066 145 ASP   B OD2 
6450 N N   . THR   B 146 ? 0.1468 0.1378 0.2976 -0.0197 0.0035  -0.0038 146 THR   B N   
6451 C CA  . THR   B 146 ? 0.1500 0.1446 0.2803 -0.0126 0.0058  -0.0007 146 THR   B CA  
6452 C C   . THR   B 146 ? 0.1506 0.1412 0.2753 -0.0003 -0.0092 0.0037  146 THR   B C   
6453 O O   . THR   B 146 ? 0.1467 0.1416 0.2775 -0.0019 -0.0127 0.0030  146 THR   B O   
6454 C CB  . THR   B 146 ? 0.1468 0.1429 0.2744 -0.0088 0.0191  -0.0028 146 THR   B CB  
6455 O OG1 . THR   B 146 ? 0.1481 0.1470 0.2807 -0.0118 0.0113  0.0072  146 THR   B OG1 
6456 C CG2 . THR   B 146 ? 0.1617 0.1527 0.2774 -0.0096 0.0244  -0.0060 146 THR   B CG2 
6464 N N   . VAL   B 147 ? 0.1508 0.1422 0.2594 -0.0025 0.0032  0.0014  147 VAL   B N   
6465 C CA  . VAL   B 147 ? 0.1490 0.1403 0.2474 -0.0113 -0.0078 0.0059  147 VAL   B CA  
6466 C C   . VAL   B 147 ? 0.1444 0.1435 0.2613 -0.0286 -0.0178 0.0032  147 VAL   B C   
6467 O O   . VAL   B 147 ? 0.1630 0.1565 0.2663 -0.0278 -0.0401 0.0081  147 VAL   B O   
6468 C CB  . VAL   B 147 ? 0.1588 0.1469 0.2276 -0.0084 -0.0117 0.0066  147 VAL   B CB  
6469 C CG1 . VAL   B 147 ? 0.1578 0.1571 0.2156 -0.0128 -0.0170 0.0098  147 VAL   B CG1 
6470 C CG2 . VAL   B 147 ? 0.1586 0.1471 0.2396 -0.0056 0.0038  0.0023  147 VAL   B CG2 
6480 N N   . ARG   B 148 ? 0.1476 0.1344 0.2479 -0.0116 -0.0221 0.0009  148 ARG   B N   
6481 C CA  . ARG   B 148 ? 0.1613 0.1394 0.2418 -0.0085 -0.0343 -0.0042 148 ARG   B CA  
6482 C C   . ARG   B 148 ? 0.1626 0.1501 0.2227 -0.0119 -0.0386 0.0045  148 ARG   B C   
6483 O O   . ARG   B 148 ? 0.1804 0.1843 0.2342 -0.0318 -0.0536 0.0094  148 ARG   B O   
6484 C CB  . ARG   B 148 ? 0.1599 0.1448 0.2373 -0.0036 -0.0398 -0.0114 148 ARG   B CB  
6485 C CG  . ARG   B 148 ? 0.1662 0.1669 0.2589 -0.0079 -0.0233 -0.0303 148 ARG   B CG  
6486 C CD  . ARG   B 148 ? 0.1701 0.1866 0.2760 0.0085  -0.0251 -0.0439 148 ARG   B CD  
6487 N NE  . ARG   B 148 ? 0.1682 0.1945 0.2740 0.0181  -0.0481 -0.0368 148 ARG   B NE  
6488 C CZ  . ARG   B 148 ? 0.1575 0.1950 0.2512 0.0113  -0.0400 -0.0301 148 ARG   B CZ  
6489 N NH1 . ARG   B 148 ? 0.1523 0.1930 0.2692 0.0052  0.0008  -0.0256 148 ARG   B NH1 
6490 N NH2 . ARG   B 148 ? 0.1783 0.1822 0.2478 0.0147  -0.0321 -0.0283 148 ARG   B NH2 
6504 N N   . THR   B 149 ? 0.1634 0.1417 0.2291 -0.0196 -0.0344 0.0046  149 THR   B N   
6505 C CA  . THR   B 149 ? 0.1662 0.1570 0.2179 -0.0208 -0.0426 0.0072  149 THR   B CA  
6506 C C   . THR   B 149 ? 0.1620 0.1589 0.2103 -0.0263 -0.0373 0.0077  149 THR   B C   
6507 O O   . THR   B 149 ? 0.1713 0.1579 0.2243 -0.0284 -0.0195 0.0003  149 THR   B O   
6508 C CB  . THR   B 149 ? 0.1649 0.1587 0.2249 -0.0176 -0.0405 0.0035  149 THR   B CB  
6509 O OG1 . THR   B 149 ? 0.1716 0.1550 0.2181 -0.0268 -0.0394 0.0034  149 THR   B OG1 
6510 C CG2 . THR   B 149 ? 0.1783 0.1656 0.2277 -0.0104 -0.0258 0.0072  149 THR   B CG2 
6518 N N   . ASN   B 150 ? 0.1679 0.1526 0.2072 -0.0238 -0.0446 0.0020  150 ASN   B N   
6519 C CA  . ASN   B 150 ? 0.1879 0.1694 0.1826 -0.0265 -0.0445 -0.0014 150 ASN   B CA  
6520 C C   . ASN   B 150 ? 0.1762 0.1596 0.1755 -0.0264 -0.0347 -0.0054 150 ASN   B C   
6521 O O   . ASN   B 150 ? 0.1817 0.1603 0.1973 -0.0388 -0.0440 0.0073  150 ASN   B O   
6522 C CB  . ASN   B 150 ? 0.2235 0.2024 0.1941 -0.0321 -0.0539 0.0198  150 ASN   B CB  
6523 C CG  . ASN   B 150 ? 0.2551 0.2342 0.2358 -0.0362 -0.0620 0.0406  150 ASN   B CG  
6524 O OD1 . ASN   B 150 ? 0.2697 0.2515 0.2436 -0.0440 -0.0721 0.0249  150 ASN   B OD1 
6525 N ND2 . ASN   B 150 ? 0.2670 0.2536 0.2871 -0.0332 -0.0653 0.0882  150 ASN   B ND2 
6532 N N   . VAL   B 151 ? 0.1701 0.1606 0.1902 -0.0302 -0.0325 0.0018  151 VAL   B N   
6533 C CA  . VAL   B 151 ? 0.1741 0.1655 0.1836 -0.0335 -0.0385 -0.0001 151 VAL   B CA  
6534 C C   . VAL   B 151 ? 0.1672 0.1599 0.1755 -0.0430 -0.0385 -0.0023 151 VAL   B C   
6535 O O   . VAL   B 151 ? 0.1834 0.1662 0.2098 -0.0364 -0.0283 -0.0119 151 VAL   B O   
6536 C CB  . VAL   B 151 ? 0.1989 0.1737 0.1938 -0.0153 -0.0292 -0.0003 151 VAL   B CB  
6537 C CG1 . VAL   B 151 ? 0.1943 0.1787 0.2458 -0.0278 -0.0140 -0.0037 151 VAL   B CG1 
6538 C CG2 . VAL   B 151 ? 0.2083 0.1860 0.1645 -0.0011 -0.0202 0.0097  151 VAL   B CG2 
6548 N N   . TYR   B 152 ? 0.1614 0.1509 0.1809 -0.0277 -0.0334 -0.0011 152 TYR   B N   
6549 C CA  . TYR   B 152 ? 0.1656 0.1630 0.1681 -0.0357 -0.0299 -0.0026 152 TYR   B CA  
6550 C C   . TYR   B 152 ? 0.1651 0.1409 0.1583 -0.0319 -0.0233 -0.0019 152 TYR   B C   
6551 O O   . TYR   B 152 ? 0.1813 0.1463 0.1656 -0.0321 -0.0185 -0.0005 152 TYR   B O   
6552 C CB  . TYR   B 152 ? 0.1880 0.1894 0.1678 -0.0398 -0.0247 0.0086  152 TYR   B CB  
6553 C CG  . TYR   B 152 ? 0.2008 0.1986 0.1692 -0.0547 -0.0246 -0.0034 152 TYR   B CG  
6554 C CD1 . TYR   B 152 ? 0.2189 0.2068 0.1382 -0.0485 -0.0339 0.0026  152 TYR   B CD1 
6555 C CD2 . TYR   B 152 ? 0.2232 0.2211 0.1686 -0.0617 -0.0152 -0.0135 152 TYR   B CD2 
6556 C CE1 . TYR   B 152 ? 0.2379 0.2327 0.1630 -0.0455 -0.0411 0.0228  152 TYR   B CE1 
6557 C CE2 . TYR   B 152 ? 0.2375 0.2434 0.1720 -0.0596 -0.0317 -0.0256 152 TYR   B CE2 
6558 C CZ  . TYR   B 152 ? 0.2410 0.2582 0.1528 -0.0506 -0.0605 0.0079  152 TYR   B CZ  
6559 O OH  . TYR   B 152 ? 0.2645 0.2969 0.2125 -0.0344 -0.0562 0.0072  152 TYR   B OH  
6569 N N   . LEU   B 153 ? 0.1705 0.1423 0.1721 -0.0345 -0.0174 -0.0035 153 LEU   B N   
6570 C CA  . LEU   B 153 ? 0.1849 0.1358 0.1618 -0.0312 -0.0147 -0.0160 153 LEU   B CA  
6571 C C   . LEU   B 153 ? 0.1887 0.1419 0.1647 -0.0243 -0.0096 -0.0197 153 LEU   B C   
6572 O O   . LEU   B 153 ? 0.1866 0.1666 0.1885 -0.0126 -0.0099 -0.0364 153 LEU   B O   
6573 C CB  . LEU   B 153 ? 0.1828 0.1327 0.1808 -0.0316 -0.0082 0.0050  153 LEU   B CB  
6574 C CG  . LEU   B 153 ? 0.1778 0.1426 0.2144 -0.0315 -0.0086 -0.0013 153 LEU   B CG  
6575 C CD1 . LEU   B 153 ? 0.1918 0.1556 0.2348 -0.0297 -0.0034 0.0083  153 LEU   B CD1 
6576 C CD2 . LEU   B 153 ? 0.1688 0.1612 0.2157 -0.0332 0.0025  0.0114  153 LEU   B CD2 
6588 N N   . ALA   B 154 ? 0.1740 0.1428 0.1823 -0.0116 -0.0140 -0.0228 154 ALA   B N   
6589 C CA  . ALA   B 154 ? 0.1846 0.1558 0.2065 -0.0072 -0.0136 -0.0263 154 ALA   B CA  
6590 C C   . ALA   B 154 ? 0.1996 0.1601 0.2184 0.0013  -0.0311 -0.0412 154 ALA   B C   
6591 O O   . ALA   B 154 ? 0.2403 0.1517 0.2489 0.0062  -0.0235 -0.0184 154 ALA   B O   
6592 C CB  . ALA   B 154 ? 0.1816 0.1621 0.2380 -0.0048 -0.0019 -0.0289 154 ALA   B CB  
6598 N N   . VAL   B 155 ? 0.1651 0.1507 0.2313 -0.0142 0.0054  -0.0260 155 VAL   B N   
6599 C CA  . VAL   B 155 ? 0.1689 0.1452 0.2593 -0.0071 -0.0073 -0.0161 155 VAL   B CA  
6600 C C   . VAL   B 155 ? 0.1604 0.1420 0.2490 -0.0013 -0.0086 -0.0218 155 VAL   B C   
6601 O O   . VAL   B 155 ? 0.1728 0.1616 0.2888 0.0050  -0.0111 -0.0479 155 VAL   B O   
6602 C CB  . VAL   B 155 ? 0.1729 0.1594 0.2843 -0.0056 -0.0239 0.0033  155 VAL   B CB  
6603 C CG1 . VAL   B 155 ? 0.1804 0.1621 0.2851 -0.0219 -0.0135 -0.0000 155 VAL   B CG1 
6604 C CG2 . VAL   B 155 ? 0.1663 0.1631 0.3103 -0.0040 -0.0179 0.0314  155 VAL   B CG2 
6614 N N   . PHE   B 156 ? 0.1516 0.1548 0.2639 0.0046  -0.0050 -0.0223 156 PHE   B N   
6615 C CA  . PHE   B 156 ? 0.1602 0.1608 0.2970 0.0163  -0.0079 -0.0326 156 PHE   B CA  
6616 C C   . PHE   B 156 ? 0.1575 0.1641 0.3404 0.0142  -0.0181 -0.0539 156 PHE   B C   
6617 O O   . PHE   B 156 ? 0.1885 0.1968 0.3675 0.0236  -0.0113 -0.0587 156 PHE   B O   
6618 C CB  . PHE   B 156 ? 0.1700 0.1562 0.2793 0.0116  -0.0057 -0.0211 156 PHE   B CB  
6619 C CG  . PHE   B 156 ? 0.1668 0.1715 0.2854 0.0107  -0.0027 -0.0046 156 PHE   B CG  
6620 C CD1 . PHE   B 156 ? 0.1712 0.1966 0.3253 0.0114  0.0030  0.0312  156 PHE   B CD1 
6621 C CD2 . PHE   B 156 ? 0.1808 0.1877 0.2995 0.0240  -0.0129 0.0002  156 PHE   B CD2 
6622 C CE1 . PHE   B 156 ? 0.1760 0.2136 0.3478 0.0095  0.0004  0.0318  156 PHE   B CE1 
6623 C CE2 . PHE   B 156 ? 0.1847 0.2085 0.3294 0.0277  -0.0171 0.0114  156 PHE   B CE2 
6624 C CZ  . PHE   B 156 ? 0.1755 0.2122 0.3494 0.0198  -0.0275 0.0169  156 PHE   B CZ  
6634 N N   . ASP   B 157 ? 0.1548 0.1633 0.3686 0.0200  -0.0306 -0.0265 157 ASP   B N   
6635 C CA  . ASP   B 157 ? 0.1738 0.1743 0.3993 0.0169  -0.0309 -0.0419 157 ASP   B CA  
6636 C C   . ASP   B 157 ? 0.1737 0.1794 0.4048 0.0103  -0.0244 -0.0655 157 ASP   B C   
6637 O O   . ASP   B 157 ? 0.1571 0.1720 0.4043 0.0101  -0.0255 -0.0445 157 ASP   B O   
6638 C CB  . ASP   B 157 ? 0.2181 0.1872 0.4137 0.0138  -0.0505 -0.0304 157 ASP   B CB  
6639 C CG  . ASP   B 157 ? 0.2649 0.2044 0.4427 0.0013  -0.0470 -0.0309 157 ASP   B CG  
6640 O OD1 . ASP   B 157 ? 0.2599 0.2033 0.4637 0.0098  -0.0419 -0.0291 157 ASP   B OD1 
6641 O OD2 . ASP   B 157 ? 0.3030 0.2262 0.4646 -0.0017 -0.0341 -0.0187 157 ASP   B OD2 
6646 N N   A LYS   B 158 ? 0.1794 0.2129 0.4309 0.0046  -0.0073 -0.0918 158 LYS   B N   
6647 N N   B LYS   B 158 ? 0.1912 0.2039 0.3888 0.0103  -0.0185 -0.0694 158 LYS   B N   
6648 C CA  A LYS   B 158 ? 0.2016 0.2338 0.4314 0.0041  -0.0022 -0.1163 158 LYS   B CA  
6649 C CA  B LYS   B 158 ? 0.2125 0.2206 0.3775 0.0111  -0.0167 -0.0744 158 LYS   B CA  
6650 C C   A LYS   B 158 ? 0.2022 0.2145 0.4328 0.0089  -0.0183 -0.1041 158 LYS   B C   
6651 C C   B LYS   B 158 ? 0.2074 0.2104 0.3877 0.0134  -0.0245 -0.0776 158 LYS   B C   
6652 O O   A LYS   B 158 ? 0.1931 0.2093 0.4517 -0.0060 -0.0157 -0.1040 158 LYS   B O   
6653 O O   B LYS   B 158 ? 0.2057 0.2104 0.3739 0.0114  -0.0222 -0.0776 158 LYS   B O   
6654 C CB  A LYS   B 158 ? 0.2272 0.2866 0.4235 0.0021  0.0149  -0.1421 158 LYS   B CB  
6655 C CB  B LYS   B 158 ? 0.2379 0.2492 0.3710 0.0108  -0.0087 -0.0740 158 LYS   B CB  
6656 C CG  A LYS   B 158 ? 0.2609 0.3393 0.4263 0.0013  0.0203  -0.1513 158 LYS   B CG  
6657 C CG  B LYS   B 158 ? 0.2627 0.2738 0.3805 0.0111  -0.0031 -0.0712 158 LYS   B CG  
6658 C CD  A LYS   B 158 ? 0.2847 0.3890 0.4315 -0.0025 0.0255  -0.1455 158 LYS   B CD  
6659 C CD  B LYS   B 158 ? 0.2825 0.2972 0.3944 0.0103  0.0008  -0.0644 158 LYS   B CD  
6660 C CE  A LYS   B 158 ? 0.3055 0.4283 0.4421 -0.0019 0.0277  -0.1360 158 LYS   B CE  
6661 C CE  B LYS   B 158 ? 0.2974 0.3135 0.4103 0.0117  0.0030  -0.0591 158 LYS   B CE  
6662 N NZ  A LYS   B 158 ? 0.3069 0.4500 0.4398 -0.0052 0.0314  -0.1301 158 LYS   B NZ  
6663 N NZ  B LYS   B 158 ? 0.3030 0.3210 0.4174 0.0119  0.0048  -0.0560 158 LYS   B NZ  
6690 N N   . ASN   B 159 ? 0.1999 0.2009 0.4336 0.0117  -0.0329 -0.0785 159 ASN   B N   
6691 C CA  . ASN   B 159 ? 0.2268 0.2011 0.4622 0.0305  -0.0555 -0.0657 159 ASN   B CA  
6692 C C   . ASN   B 159 ? 0.1966 0.1654 0.4632 0.0150  -0.0677 -0.0632 159 ASN   B C   
6693 O O   . ASN   B 159 ? 0.1961 0.1523 0.4829 -0.0028 -0.0766 -0.0474 159 ASN   B O   
6694 C CB  . ASN   B 159 ? 0.2827 0.2401 0.4859 0.0591  -0.0751 -0.0576 159 ASN   B CB  
6695 C CG  . ASN   B 159 ? 0.3284 0.2857 0.5065 0.0815  -0.1009 -0.0478 159 ASN   B CG  
6696 O OD1 . ASN   B 159 ? 0.3341 0.2859 0.5023 0.1006  -0.0998 -0.0625 159 ASN   B OD1 
6697 N ND2 . ASN   B 159 ? 0.3469 0.3042 0.5232 0.0856  -0.1162 -0.0446 159 ASN   B ND2 
6705 N N   . LEU   B 160 ? 0.1828 0.1714 0.4538 0.0101  -0.0556 -0.0595 160 LEU   B N   
6706 C CA  . LEU   B 160 ? 0.1796 0.1617 0.4145 0.0088  -0.0487 -0.0384 160 LEU   B CA  
6707 C C   . LEU   B 160 ? 0.1662 0.1494 0.4006 -0.0035 -0.0391 -0.0340 160 LEU   B C   
6708 O O   . LEU   B 160 ? 0.1543 0.1594 0.3946 -0.0040 -0.0432 -0.0215 160 LEU   B O   
6709 C CB  . LEU   B 160 ? 0.1784 0.1680 0.3893 0.0071  -0.0595 -0.0210 160 LEU   B CB  
6710 C CG  . LEU   B 160 ? 0.1774 0.1831 0.3587 0.0037  -0.0448 -0.0031 160 LEU   B CG  
6711 C CD1 . LEU   B 160 ? 0.1912 0.2028 0.3715 -0.0002 -0.0257 0.0023  160 LEU   B CD1 
6712 C CD2 . LEU   B 160 ? 0.1771 0.1939 0.3413 0.0221  -0.0341 -0.0070 160 LEU   B CD2 
6724 N N   . TYR   B 161 ? 0.1638 0.1558 0.4031 -0.0085 -0.0014 -0.0551 161 TYR   B N   
6725 C CA  . TYR   B 161 ? 0.1804 0.1540 0.3912 -0.0223 0.0247  -0.0551 161 TYR   B CA  
6726 C C   . TYR   B 161 ? 0.1848 0.1595 0.3843 -0.0107 0.0328  -0.0528 161 TYR   B C   
6727 O O   . TYR   B 161 ? 0.1864 0.1647 0.3799 -0.0187 0.0230  -0.0473 161 TYR   B O   
6728 C CB  . TYR   B 161 ? 0.1995 0.1678 0.3895 -0.0286 0.0435  -0.0621 161 TYR   B CB  
6729 C CG  . TYR   B 161 ? 0.2276 0.1814 0.3660 -0.0326 0.0462  -0.0661 161 TYR   B CG  
6730 C CD1 . TYR   B 161 ? 0.2288 0.1806 0.3605 -0.0439 0.0484  -0.0669 161 TYR   B CD1 
6731 C CD2 . TYR   B 161 ? 0.2454 0.1894 0.3382 -0.0304 0.0357  -0.0667 161 TYR   B CD2 
6732 C CE1 . TYR   B 161 ? 0.2490 0.2075 0.3521 -0.0472 0.0502  -0.0684 161 TYR   B CE1 
6733 C CE2 . TYR   B 161 ? 0.2676 0.2077 0.3432 -0.0340 0.0453  -0.0648 161 TYR   B CE2 
6734 C CZ  . TYR   B 161 ? 0.2680 0.2096 0.3385 -0.0548 0.0363  -0.0625 161 TYR   B CZ  
6735 O OH  . TYR   B 161 ? 0.3014 0.2413 0.3546 -0.0571 0.0399  -0.0627 161 TYR   B OH  
6745 N N   . ASP   B 162 ? 0.1865 0.1645 0.3931 -0.0126 0.0012  -0.0758 162 ASP   B N   
6746 C CA  . ASP   B 162 ? 0.1924 0.1772 0.3964 -0.0103 -0.0036 -0.0671 162 ASP   B CA  
6747 C C   . ASP   B 162 ? 0.1896 0.1588 0.3817 -0.0144 -0.0193 -0.0371 162 ASP   B C   
6748 O O   . ASP   B 162 ? 0.1984 0.1577 0.4024 -0.0172 -0.0476 -0.0333 162 ASP   B O   
6749 C CB  . ASP   B 162 ? 0.2083 0.1869 0.4184 -0.0049 -0.0065 -0.0986 162 ASP   B CB  
6750 C CG  . ASP   B 162 ? 0.2182 0.2176 0.4494 0.0091  -0.0074 -0.1003 162 ASP   B CG  
6751 O OD1 . ASP   B 162 ? 0.2188 0.2363 0.4392 -0.0019 0.0083  -0.1008 162 ASP   B OD1 
6752 O OD2 . ASP   B 162 ? 0.2335 0.2320 0.4776 0.0237  -0.0110 -0.0949 162 ASP   B OD2 
6757 N N   A LYS   B 163 ? 0.1863 0.1484 0.3738 -0.0198 -0.0447 -0.0271 163 LYS   B N   
6758 N N   B LYS   B 163 ? 0.2001 0.1780 0.3668 -0.0154 -0.0243 -0.0247 163 LYS   B N   
6759 C CA  A LYS   B 163 ? 0.1982 0.1596 0.3702 -0.0293 -0.0376 -0.0050 163 LYS   B CA  
6760 C CA  B LYS   B 163 ? 0.2124 0.2011 0.3598 -0.0170 -0.0226 -0.0123 163 LYS   B CA  
6761 C C   A LYS   B 163 ? 0.1694 0.1559 0.3562 -0.0376 -0.0343 0.0073  163 LYS   B C   
6762 C C   B LYS   B 163 ? 0.1828 0.1816 0.3389 -0.0204 -0.0248 -0.0035 163 LYS   B C   
6763 O O   A LYS   B 163 ? 0.1684 0.1579 0.3830 -0.0440 -0.0322 0.0145  163 LYS   B O   
6764 O O   B LYS   B 163 ? 0.1835 0.1842 0.3368 -0.0194 -0.0212 0.0010  163 LYS   B O   
6765 C CB  A LYS   B 163 ? 0.2501 0.1914 0.3947 -0.0285 -0.0418 0.0043  163 LYS   B CB  
6766 C CB  B LYS   B 163 ? 0.2543 0.2440 0.3830 -0.0165 -0.0221 -0.0086 163 LYS   B CB  
6767 C CG  A LYS   B 163 ? 0.3285 0.2627 0.4389 -0.0301 -0.0273 0.0048  163 LYS   B CG  
6768 C CG  B LYS   B 163 ? 0.2963 0.2879 0.4164 -0.0162 -0.0180 -0.0055 163 LYS   B CG  
6769 C CD  A LYS   B 163 ? 0.3972 0.3213 0.4938 -0.0396 -0.0187 -0.0014 163 LYS   B CD  
6770 C CD  B LYS   B 163 ? 0.3376 0.3308 0.4562 -0.0178 -0.0147 -0.0042 163 LYS   B CD  
6771 C CE  A LYS   B 163 ? 0.4481 0.3658 0.5267 -0.0462 -0.0088 -0.0040 163 LYS   B CE  
6772 C CE  B LYS   B 163 ? 0.3688 0.3638 0.4860 -0.0192 -0.0107 -0.0034 163 LYS   B CE  
6773 N NZ  A LYS   B 163 ? 0.4759 0.3858 0.5495 -0.0505 -0.0062 -0.0093 163 LYS   B NZ  
6774 N NZ  B LYS   B 163 ? 0.3786 0.3731 0.5054 -0.0200 -0.0094 -0.0038 163 LYS   B NZ  
6801 N N   . LEU   B 164 ? 0.1537 0.1605 0.3340 -0.0227 -0.0305 -0.0007 164 LEU   B N   
6802 C CA  . LEU   B 164 ? 0.1584 0.1570 0.3141 -0.0177 -0.0294 -0.0028 164 LEU   B CA  
6803 C C   . LEU   B 164 ? 0.1676 0.1594 0.3191 -0.0211 -0.0326 0.0038  164 LEU   B C   
6804 O O   . LEU   B 164 ? 0.1636 0.1837 0.3500 -0.0179 -0.0357 -0.0010 164 LEU   B O   
6805 C CB  . LEU   B 164 ? 0.1531 0.1583 0.2931 -0.0210 -0.0204 -0.0044 164 LEU   B CB  
6806 C CG  . LEU   B 164 ? 0.1617 0.1664 0.2942 -0.0107 -0.0175 -0.0076 164 LEU   B CG  
6807 C CD1 . LEU   B 164 ? 0.1664 0.1641 0.2850 -0.0176 -0.0288 -0.0209 164 LEU   B CD1 
6808 C CD2 . LEU   B 164 ? 0.1874 0.1945 0.3075 -0.0101 -0.0098 -0.0074 164 LEU   B CD2 
6821 N N   . VAL   B 165 ? 0.2048 0.1601 0.3389 -0.0363 -0.0456 -0.0082 165 VAL   B N   
6822 C CA  . VAL   B 165 ? 0.2524 0.1803 0.3502 -0.0436 -0.0737 -0.0135 165 VAL   B CA  
6823 C C   . VAL   B 165 ? 0.2834 0.1967 0.3860 -0.0446 -0.1177 -0.0034 165 VAL   B C   
6824 O O   . VAL   B 165 ? 0.3093 0.2052 0.4063 -0.0502 -0.1281 0.0020  165 VAL   B O   
6825 C CB  . VAL   B 165 ? 0.2828 0.2011 0.3493 -0.0273 -0.0488 -0.0256 165 VAL   B CB  
6826 C CG1 . VAL   B 165 ? 0.3053 0.2077 0.3700 -0.0360 -0.0384 -0.0261 165 VAL   B CG1 
6827 C CG2 . VAL   B 165 ? 0.2824 0.2013 0.3407 -0.0186 -0.0361 -0.0248 165 VAL   B CG2 
6837 N N   . SER   B 166 ? 0.2945 0.1875 0.4224 -0.0475 -0.1322 -0.0250 166 SER   B N   
6838 C CA  . SER   B 166 ? 0.2956 0.1921 0.4762 -0.0463 -0.1089 -0.0324 166 SER   B CA  
6839 C C   . SER   B 166 ? 0.2755 0.2028 0.4973 -0.0606 -0.0954 0.0077  166 SER   B C   
6840 O O   . SER   B 166 ? 0.2794 0.2255 0.5323 -0.0772 -0.1095 -0.0265 166 SER   B O   
6841 C CB  . SER   B 166 ? 0.2951 0.1918 0.4994 -0.0383 -0.0964 -0.0391 166 SER   B CB  
6842 O OG  . SER   B 166 ? 0.2783 0.1838 0.5120 -0.0295 -0.0990 -0.0207 166 SER   B OG  
6848 N N   . SER   B 167 ? 0.2470 0.1968 0.4595 -0.0684 -0.1010 0.0658  167 SER   B N   
6849 C CA  . SER   B 167 ? 0.2410 0.2159 0.4585 -0.0506 -0.0688 0.0665  167 SER   B CA  
6850 C C   . SER   B 167 ? 0.2210 0.2184 0.4324 -0.0664 -0.0662 0.0842  167 SER   B C   
6851 O O   . SER   B 167 ? 0.2146 0.2312 0.4341 -0.0717 -0.0627 0.0737  167 SER   B O   
6852 C CB  . SER   B 167 ? 0.2230 0.2112 0.4783 -0.0505 -0.0395 0.0557  167 SER   B CB  
6853 O OG  . SER   B 167 ? 0.2129 0.2101 0.4794 -0.0396 -0.0069 0.0571  167 SER   B OG  
6859 N N   . PHE   B 168 ? 0.2210 0.2101 0.4170 -0.0608 -0.0514 0.0790  168 PHE   B N   
6860 C CA  . PHE   B 168 ? 0.2266 0.1988 0.3689 -0.0594 -0.0496 0.0434  168 PHE   B CA  
6861 C C   . PHE   B 168 ? 0.2042 0.1809 0.2976 -0.0311 -0.0227 0.0123  168 PHE   B C   
6862 O O   . PHE   B 168 ? 0.2265 0.1589 0.2854 -0.0063 -0.0159 -0.0032 168 PHE   B O   
6863 C CB  . PHE   B 168 ? 0.2480 0.2016 0.3830 -0.0689 -0.0602 0.0603  168 PHE   B CB  
6864 C CG  . PHE   B 168 ? 0.2685 0.1882 0.3680 -0.0675 -0.0495 0.0431  168 PHE   B CG  
6865 C CD1 . PHE   B 168 ? 0.2977 0.1996 0.3807 -0.0621 -0.0531 0.0289  168 PHE   B CD1 
6866 C CD2 . PHE   B 168 ? 0.2605 0.1827 0.3622 -0.0668 -0.0468 0.0398  168 PHE   B CD2 
6867 C CE1 . PHE   B 168 ? 0.3085 0.1971 0.3571 -0.0588 -0.0354 0.0495  168 PHE   B CE1 
6868 C CE2 . PHE   B 168 ? 0.2863 0.1839 0.3603 -0.0528 -0.0434 0.0319  168 PHE   B CE2 
6869 C CZ  . PHE   B 168 ? 0.3016 0.1864 0.3599 -0.0452 -0.0434 0.0491  168 PHE   B CZ  
6879 N N   . LEU   B 169 ? 0.2204 0.1954 0.2802 -0.0090 -0.0042 0.0069  169 LEU   B N   
6880 C CA  . LEU   B 169 ? 0.2506 0.2221 0.3084 -0.0049 0.0023  -0.0338 169 LEU   B CA  
6881 C C   . LEU   B 169 ? 0.2878 0.2520 0.3709 0.0130  0.0038  -0.0496 169 LEU   B C   
6882 O O   . LEU   B 169 ? 0.3108 0.2711 0.4207 0.0091  0.0074  -0.0633 169 LEU   B O   
6883 C CB  . LEU   B 169 ? 0.2780 0.2676 0.3209 -0.0126 0.0064  -0.0090 169 LEU   B CB  
6884 C CG  . LEU   B 169 ? 0.3150 0.3051 0.3679 -0.0038 0.0108  -0.0016 169 LEU   B CG  
6885 C CD1 . LEU   B 169 ? 0.3298 0.3220 0.3751 -0.0050 0.0081  0.0167  169 LEU   B CD1 
6886 C CD2 . LEU   B 169 ? 0.3039 0.3110 0.3638 0.0132  0.0358  -0.0119 169 LEU   B CD2 
6887 O OXT . LEU   B 169 ? 0.3031 0.2702 0.3767 0.0463  0.0133  -0.0433 169 LEU   B OXT 
6899 C C1  T TFA   C .   ? 0.1262 0.1518 0.1287 -0.0255 0.0230  0.0174  201 TFA   A C1  
6900 C C2  T TFA   C .   ? 0.1474 0.1764 0.1686 -0.0229 0.0163  0.0016  201 TFA   A C2  
6901 O O   T TFA   C .   ? 0.1077 0.1307 0.1245 -0.0216 0.0177  0.0288  201 TFA   A O   
6902 F F1  T TFA   C .   ? 0.1668 0.1822 0.2059 -0.0148 0.0087  -0.0049 201 TFA   A F1  
6903 F F2  T TFA   C .   ? 0.1587 0.1758 0.1611 -0.0154 0.0283  0.0181  201 TFA   A F2  
6904 F F3  T TFA   C .   ? 0.1504 0.1981 0.2017 -0.0296 0.0319  -0.0119 201 TFA   A F3  
6905 O OXT T TFA   C .   ? 0.1267 0.1537 0.1324 -0.0027 0.0407  0.0232  201 TFA   A OXT 
6906 N N2  B A1A98 D .   ? 0.1625 0.1982 0.1354 -0.0152 0.0133  0.0184  202 A1A98 A N2  
6907 C C3  B A1A98 D .   ? 0.1642 0.2035 0.1536 -0.0222 0.0059  0.0237  202 A1A98 A C3  
6908 C C6  B A1A98 D .   ? 0.1444 0.1964 0.1370 -0.0099 0.0018  0.0338  202 A1A98 A C6  
6909 C C9  B A1A98 D .   ? 0.2231 0.2303 0.2095 -0.0233 0.0077  0.0057  202 A1A98 A C9  
6910 C C12 B A1A98 D .   ? 0.2192 0.2300 0.2071 -0.0200 0.0038  0.0015  202 A1A98 A C12 
6911 C C1  B A1A98 D .   ? 0.2251 0.2166 0.2140 -0.0264 0.0115  0.0100  202 A1A98 A C1  
6912 C C10 B A1A98 D .   ? 0.2263 0.2354 0.2070 -0.0197 0.0076  0.0039  202 A1A98 A C10 
6913 C C11 B A1A98 D .   ? 0.2251 0.2346 0.2109 -0.0172 0.0041  0.0014  202 A1A98 A C11 
6914 C C2  B A1A98 D .   ? 0.2147 0.2210 0.2049 -0.0261 0.0060  0.0070  202 A1A98 A C2  
6915 C C4  B A1A98 D .   ? 0.1594 0.1976 0.1291 -0.0110 0.0069  0.0257  202 A1A98 A C4  
6916 C C5  B A1A98 D .   ? 0.1396 0.1901 0.1290 -0.0026 -0.0084 0.0328  202 A1A98 A C5  
6917 C C7  B A1A98 D .   ? 0.1334 0.1947 0.1354 -0.0029 0.0008  0.0368  202 A1A98 A C7  
6918 C C8  B A1A98 D .   ? 0.1179 0.1837 0.1250 -0.0049 -0.0178 0.0471  202 A1A98 A C8  
6919 N N1  B A1A98 D .   ? 0.1879 0.2115 0.1842 -0.0311 0.0045  0.0124  202 A1A98 A N1  
6920 N N3  B A1A98 D .   ? 0.1543 0.1961 0.1265 -0.0056 0.0034  0.0270  202 A1A98 A N3  
6921 N N4  B A1A98 D .   ? 0.1239 0.1768 0.1163 0.0006  -0.0244 0.0477  202 A1A98 A N4  
6922 O O1  B A1A98 D .   ? 0.2300 0.2114 0.2242 -0.0333 0.0136  0.0162  202 A1A98 A O1  
6939 O O   . HOH   E .   ? 0.2496 0.2556 0.4254 -0.0396 -0.0641 0.0451  301 HOH   A O   
6940 O O   A HOH   E .   ? 0.4318 0.7654 0.5159 -0.1235 0.0495  0.1074  302 HOH   A O   
6941 O O   . HOH   E .   ? 0.4717 0.3830 0.4421 0.0011  0.1269  0.0139  303 HOH   A O   
6942 O O   . HOH   E .   ? 0.6523 0.5040 0.5984 -0.0983 0.2001  0.1495  304 HOH   A O   
6943 O O   . HOH   E .   ? 0.2391 0.1973 0.2668 0.0497  -0.0388 -0.0030 305 HOH   A O   
6944 O O   . HOH   E .   ? 0.3791 0.3116 0.4674 -0.0451 -0.1511 0.1335  306 HOH   A O   
6945 O O   . HOH   E .   ? 0.5514 0.3042 0.3593 -0.0410 -0.0181 -0.0633 307 HOH   A O   
6946 O O   . HOH   E .   ? 0.1868 0.1989 0.2987 -0.0350 -0.0017 0.0630  308 HOH   A O   
6947 O O   A HOH   E .   ? 0.2701 0.5156 0.6032 0.0748  0.0773  0.0865  309 HOH   A O   
6948 O O   . HOH   E .   ? 0.6830 0.4993 0.3342 0.1943  -0.1388 0.0537  310 HOH   A O   
6949 O O   . HOH   E .   ? 0.1923 0.1997 0.2376 0.0151  -0.0172 0.0236  311 HOH   A O   
6950 O O   . HOH   E .   ? 0.6101 0.7036 0.4388 0.2543  0.0261  -0.0052 312 HOH   A O   
6951 O O   . HOH   E .   ? 0.7420 0.6676 0.4480 -0.1353 0.0156  0.2419  313 HOH   A O   
6952 O O   . HOH   E .   ? 0.6413 0.6420 0.3970 -0.0464 -0.0223 0.1181  314 HOH   A O   
6953 O O   . HOH   E .   ? 0.5487 0.6679 0.6090 -0.0398 0.0584  -0.0482 315 HOH   A O   
6954 O O   . HOH   E .   ? 0.5476 0.2590 0.6505 0.0823  -0.0164 -0.0213 316 HOH   A O   
6955 O O   . HOH   E .   ? 0.2711 0.2572 0.3274 -0.0187 0.0155  -0.0408 317 HOH   A O   
6956 O O   . HOH   E .   ? 0.3856 0.3856 0.3982 -0.1509 -0.0165 0.1449  318 HOH   A O   
6957 O O   . HOH   E .   ? 0.2083 0.5094 0.3518 0.1201  0.0317  0.0800  319 HOH   A O   
6958 O O   . HOH   E .   ? 1.1136 1.0834 0.9390 -0.0069 -0.0681 -0.0193 320 HOH   A O   
6959 O O   . HOH   E .   ? 0.5808 0.5014 0.5583 -0.0479 0.1391  0.2420  321 HOH   A O   
6960 O O   . HOH   E .   ? 0.2835 0.2253 0.2804 0.0026  0.0228  0.0279  322 HOH   A O   
6961 O O   . HOH   E .   ? 0.2292 0.2460 0.2778 -0.0001 0.0565  0.0696  323 HOH   A O   
6962 O O   . HOH   E .   ? 0.3009 0.3895 0.1785 -0.0474 0.0376  0.0359  324 HOH   A O   
6963 O O   . HOH   E .   ? 0.3215 0.4490 0.4189 0.0775  -0.0773 0.0435  325 HOH   A O   
6964 O O   . HOH   E .   ? 0.5805 0.6156 0.6393 -0.1313 -0.1246 -0.0914 326 HOH   A O   
6965 O O   . HOH   E .   ? 0.2382 0.2092 0.3569 -0.0507 0.0228  -0.0190 327 HOH   A O   
6966 O O   . HOH   E .   ? 0.6095 0.5834 0.5251 0.0286  0.0918  -0.1334 328 HOH   A O   
6967 O O   . HOH   E .   ? 0.3347 0.3498 0.2342 -0.0740 -0.0671 0.0438  329 HOH   A O   
6968 O O   . HOH   E .   ? 0.2260 0.3809 0.4393 -0.0445 0.0620  -0.1085 330 HOH   A O   
6969 O O   . HOH   E .   ? 0.3138 0.3667 0.5188 -0.0946 0.1351  -0.0215 331 HOH   A O   
6970 O O   . HOH   E .   ? 0.5443 0.4032 0.3234 -0.1212 -0.1350 0.0148  332 HOH   A O   
6971 O O   A HOH   E .   ? 0.1995 0.2691 0.2717 0.0115  0.0562  0.0137  333 HOH   A O   
6972 O O   . HOH   E .   ? 0.2599 0.3249 0.3746 -0.0183 -0.0321 -0.0909 334 HOH   A O   
6973 O O   A HOH   E .   ? 0.1603 0.2515 0.2643 0.0570  0.0523  0.0662  335 HOH   A O   
6974 O O   . HOH   E .   ? 0.4713 0.5892 0.5148 0.0048  0.2285  -0.0989 336 HOH   A O   
6975 O O   . HOH   E .   ? 0.2341 0.3668 0.4046 -0.0617 -0.0859 0.1497  337 HOH   A O   
6976 O O   . HOH   E .   ? 0.3739 0.6722 0.4477 -0.0900 -0.0055 0.1392  338 HOH   A O   
6977 O O   . HOH   E .   ? 0.2558 0.4112 0.3981 0.0947  -0.0854 -0.0140 339 HOH   A O   
6978 O O   . HOH   E .   ? 0.5866 0.5418 0.3666 -0.1332 0.1876  0.0975  340 HOH   A O   
6979 O O   . HOH   E .   ? 0.2546 0.3541 0.5122 0.0044  0.1086  0.2024  341 HOH   A O   
6980 O O   . HOH   E .   ? 0.1852 0.3547 0.2980 0.0014  0.0334  0.0651  342 HOH   A O   
6981 O O   . HOH   E .   ? 0.2724 0.3439 0.4366 -0.0713 -0.0385 -0.0777 343 HOH   A O   
6982 O O   . HOH   E .   ? 0.4708 0.5145 0.5855 0.1282  0.0744  -0.1258 344 HOH   A O   
6983 O O   . HOH   E .   ? 0.6181 0.3808 0.5458 -0.0538 -0.0238 0.0008  345 HOH   A O   
6984 O O   . HOH   E .   ? 0.2374 0.2261 0.2991 0.0256  0.0193  0.0312  346 HOH   A O   
6985 O O   . HOH   E .   ? 0.1697 0.1912 0.2258 0.0196  -0.0441 -0.0575 347 HOH   A O   
6986 O O   . HOH   E .   ? 0.4042 0.4624 0.4923 0.2142  0.0699  0.0232  348 HOH   A O   
6987 O O   . HOH   E .   ? 0.2894 0.3780 0.5131 -0.0830 -0.0776 -0.1053 349 HOH   A O   
6988 O O   . HOH   E .   ? 0.5475 0.2116 0.4340 0.0550  -0.1617 0.0367  350 HOH   A O   
6989 O O   . HOH   E .   ? 0.2565 0.1894 0.2691 -0.0124 -0.0596 0.0067  351 HOH   A O   
6990 O O   . HOH   E .   ? 0.1583 0.2161 0.2207 -0.0029 -0.0095 0.0347  352 HOH   A O   
6991 O O   . HOH   E .   ? 0.2124 0.2201 0.4245 0.0280  0.1071  -0.0043 353 HOH   A O   
6992 O O   . HOH   E .   ? 0.5144 0.5878 0.4402 -0.0571 -0.0630 0.2076  354 HOH   A O   
6993 O O   . HOH   E .   ? 0.3537 0.3162 0.3869 -0.0904 -0.0031 -0.0375 355 HOH   A O   
6994 O O   . HOH   E .   ? 0.3509 0.4464 0.2686 -0.0246 0.0519  0.0162  356 HOH   A O   
6995 O O   . HOH   E .   ? 0.1372 0.1442 0.1554 -0.0030 0.0195  0.0072  357 HOH   A O   
6996 O O   . HOH   E .   ? 0.5055 0.4390 0.5239 -0.1950 -0.1367 0.2391  358 HOH   A O   
6997 O O   . HOH   E .   ? 0.2092 0.2241 0.3137 -0.0030 -0.0563 0.0392  359 HOH   A O   
6998 O O   . HOH   E .   ? 0.1748 0.1976 0.2509 0.0152  -0.0307 -0.0478 360 HOH   A O   
6999 O O   . HOH   E .   ? 0.1801 0.1517 0.2442 -0.0131 0.0260  -0.0123 361 HOH   A O   
7000 O O   . HOH   E .   ? 0.4007 0.7309 0.5294 -0.0695 -0.1624 0.1265  362 HOH   A O   
7001 O O   . HOH   E .   ? 0.6639 0.4391 0.6063 -0.0446 -0.1377 -0.0033 363 HOH   A O   
7002 O O   . HOH   E .   ? 0.3613 0.4380 0.2618 -0.1546 -0.0096 -0.0642 364 HOH   A O   
7003 O O   . HOH   E .   ? 0.2029 0.3063 0.3009 0.0425  0.0508  0.1058  365 HOH   A O   
7004 O O   . HOH   E .   ? 0.2720 0.4435 0.4009 -0.0618 0.0905  0.0104  366 HOH   A O   
7005 O O   . HOH   E .   ? 0.1624 0.1954 0.2742 0.0038  -0.0006 0.0198  367 HOH   A O   
7006 O O   . HOH   E .   ? 0.3620 0.2303 0.3432 0.0944  0.0687  0.0465  368 HOH   A O   
7007 O O   . HOH   E .   ? 0.7004 0.4636 0.4200 -0.0169 -0.0797 0.2028  369 HOH   A O   
7008 O O   . HOH   E .   ? 0.6091 0.6884 0.6728 0.0645  -0.0939 0.2315  370 HOH   A O   
7009 O O   . HOH   E .   ? 0.1567 0.1773 0.1617 -0.0026 -0.0058 0.0003  371 HOH   A O   
7010 O O   . HOH   E .   ? 0.2168 0.2508 0.2809 -0.0346 -0.0594 0.0577  372 HOH   A O   
7011 O O   . HOH   E .   ? 0.3750 0.2524 0.4158 -0.1080 0.1305  -0.0282 373 HOH   A O   
7012 O O   . HOH   E .   ? 0.2635 0.2408 0.2019 -0.0731 0.0089  0.0472  374 HOH   A O   
7013 O O   . HOH   E .   ? 0.3455 0.7153 0.3122 0.1324  0.0436  -0.0656 375 HOH   A O   
7014 O O   . HOH   E .   ? 0.1991 0.2042 0.2713 -0.0245 0.0000  0.0263  376 HOH   A O   
7015 O O   . HOH   E .   ? 0.2199 0.2865 0.3779 0.0233  0.0768  -0.0709 377 HOH   A O   
7016 O O   . HOH   E .   ? 0.3580 0.3181 0.3616 -0.0104 -0.0338 0.1185  378 HOH   A O   
7017 O O   . HOH   E .   ? 0.2622 0.5182 0.3868 0.0495  0.0696  0.2477  379 HOH   A O   
7018 O O   . HOH   E .   ? 0.4301 0.2817 0.4641 -0.1249 -0.0365 0.0082  380 HOH   A O   
7019 O O   A HOH   E .   ? 0.3307 0.3083 0.3012 0.1668  0.0841  0.0816  381 HOH   A O   
7020 O O   T HOH   E .   ? 0.1163 0.1228 0.3241 -0.0116 0.0227  0.0732  382 HOH   A O   
7021 O O   . HOH   E .   ? 0.2255 0.2224 0.1951 0.0118  0.0133  0.0245  383 HOH   A O   
7022 O O   . HOH   E .   ? 0.1892 0.2316 0.2141 -0.0175 -0.0072 0.0699  384 HOH   A O   
7023 O O   . HOH   E .   ? 0.4145 0.2756 0.4697 -0.1287 0.0746  0.0358  385 HOH   A O   
7024 O O   . HOH   E .   ? 0.2105 0.2519 0.2941 -0.0286 0.0636  0.0722  386 HOH   A O   
7025 O O   . HOH   E .   ? 0.3012 0.3513 0.4226 0.0009  0.1189  -0.0400 387 HOH   A O   
7026 O O   . HOH   E .   ? 0.3221 0.3197 0.2353 0.0202  0.0735  0.0092  388 HOH   A O   
7027 O O   . HOH   E .   ? 0.6254 0.5184 0.7495 -0.1308 -0.0591 0.0981  389 HOH   A O   
7028 O O   . HOH   E .   ? 0.3115 0.3666 0.3181 -0.0679 0.1003  -0.0658 390 HOH   A O   
7029 O O   . HOH   E .   ? 0.6902 0.5312 0.4207 -0.1396 0.0361  0.1833  391 HOH   A O   
7030 O O   . HOH   E .   ? 0.2065 0.1959 0.3861 0.0384  0.1084  0.0890  392 HOH   A O   
7031 O O   . HOH   E .   ? 0.5317 0.3277 0.5673 0.0630  0.0078  -0.0157 393 HOH   A O   
7032 O O   . HOH   E .   ? 0.5872 0.5553 0.5520 0.0514  0.1064  0.0389  394 HOH   A O   
7033 O O   A HOH   E .   ? 0.2133 0.1961 0.4012 -0.0074 0.0630  -0.0032 395 HOH   A O   
7034 O O   . HOH   E .   ? 0.2223 0.2401 0.3180 -0.0370 -0.0536 0.0856  396 HOH   A O   
7035 O O   . HOH   E .   ? 0.1508 0.1571 0.1936 0.0026  -0.0147 -0.0008 397 HOH   A O   
7036 O O   . HOH   E .   ? 0.2350 0.2399 0.2999 0.0075  -0.0052 0.0436  398 HOH   A O   
7037 O O   . HOH   E .   ? 0.5386 0.5352 0.5128 0.1471  -0.1080 -0.1641 399 HOH   A O   
7038 O O   . HOH   E .   ? 0.3416 0.4491 0.3930 -0.1809 0.1035  -0.0251 400 HOH   A O   
7039 O O   . HOH   E .   ? 0.5535 0.2704 0.2870 -0.1289 0.0576  -0.0040 401 HOH   A O   
7040 O O   . HOH   E .   ? 0.2592 0.1967 0.3697 0.0099  -0.0582 0.0281  402 HOH   A O   
7041 O O   . HOH   E .   ? 0.3907 0.5345 0.5160 0.1436  0.1171  -0.0661 403 HOH   A O   
7042 O O   . HOH   E .   ? 0.3543 0.2722 0.2560 -0.0828 -0.0986 0.0429  404 HOH   A O   
7043 O O   . HOH   E .   ? 0.1655 0.1891 0.3849 0.0043  -0.0048 0.0334  405 HOH   A O   
7044 O O   . HOH   E .   ? 0.3294 0.3809 0.4287 -0.0919 0.1494  -0.0052 406 HOH   A O   
7045 O O   . HOH   E .   ? 0.3873 0.4401 0.2735 -0.0670 -0.0815 0.0475  407 HOH   A O   
7046 O O   . HOH   E .   ? 0.1789 0.1520 0.1688 -0.0259 0.0178  0.0017  408 HOH   A O   
7047 O O   . HOH   E .   ? 0.2108 0.2469 0.3142 0.0050  -0.0064 -0.0115 409 HOH   A O   
7048 O O   . HOH   E .   ? 0.2040 0.2263 0.2193 0.0182  -0.0331 -0.0031 410 HOH   A O   
7049 O O   A HOH   E .   ? 0.2338 0.6996 0.5572 -0.0120 -0.0555 0.2240  411 HOH   A O   
7050 O O   . HOH   E .   ? 0.2452 0.3078 0.2907 -0.0300 -0.0800 0.0828  412 HOH   A O   
7051 O O   . HOH   E .   ? 0.5544 0.5145 0.2313 -0.0103 0.1028  0.1051  413 HOH   A O   
7052 O O   . HOH   E .   ? 0.2635 0.2073 0.2919 -0.0445 0.0004  0.0536  414 HOH   A O   
7053 O O   . HOH   E .   ? 0.2973 0.3397 0.7428 0.0032  0.0818  -0.0760 415 HOH   A O   
7054 O O   . HOH   E .   ? 0.2743 0.6098 0.1977 -0.0109 0.0434  0.0476  416 HOH   A O   
7055 O O   . HOH   E .   ? 0.2169 0.1791 0.1754 -0.0115 0.0203  0.0266  417 HOH   A O   
7056 O O   . HOH   E .   ? 0.6016 0.4076 0.5554 0.1336  -0.1398 0.1562  418 HOH   A O   
7057 O O   . HOH   E .   ? 0.2105 0.2872 0.4550 -0.0166 -0.0200 0.0557  419 HOH   A O   
7058 O O   . HOH   E .   ? 0.3190 0.1498 0.2116 0.0071  -0.0385 0.0200  420 HOH   A O   
7059 O O   . HOH   E .   ? 0.6074 0.4605 0.6479 0.0486  0.1523  -0.1623 421 HOH   A O   
7060 O O   . HOH   E .   ? 0.1931 0.2024 0.2922 -0.0102 0.0027  0.0246  422 HOH   A O   
7061 O O   . HOH   E .   ? 0.2491 0.4119 0.2968 0.1503  0.0128  0.0508  423 HOH   A O   
7062 O O   . HOH   E .   ? 0.4854 0.6197 0.3601 0.3165  -0.0380 -0.0897 424 HOH   A O   
7063 O O   . HOH   E .   ? 0.4472 0.6841 0.3342 -0.0551 -0.0099 0.1312  425 HOH   A O   
7064 O O   . HOH   E .   ? 0.3883 0.2759 0.6051 -0.1126 -0.2423 0.1350  426 HOH   A O   
7065 O O   . HOH   E .   ? 0.6777 0.6489 0.4108 0.0428  0.2918  -0.0369 427 HOH   A O   
7066 O O   . HOH   E .   ? 0.4636 0.2434 0.6444 -0.0531 0.1197  -0.0565 428 HOH   A O   
7067 O O   . HOH   E .   ? 0.2121 0.2128 0.3327 0.0161  -0.0757 0.0177  429 HOH   A O   
7068 O O   . HOH   E .   ? 0.5901 0.7210 0.7638 -0.0485 -0.0389 -0.0199 430 HOH   A O   
7069 O O   . HOH   E .   ? 0.2970 0.1897 0.3337 0.0226  -0.0046 0.0159  431 HOH   A O   
7070 O O   . HOH   E .   ? 0.3826 0.3374 0.2159 -0.0893 0.0082  0.0847  432 HOH   A O   
7071 O O   . HOH   E .   ? 0.2160 0.1892 0.2333 -0.0170 -0.0326 -0.0213 433 HOH   A O   
7072 O O   . HOH   E .   ? 0.5403 0.5179 0.4445 -0.0499 -0.1526 0.0346  434 HOH   A O   
7073 O O   . HOH   E .   ? 0.6716 0.9164 0.5506 0.2593  -0.1061 0.2591  435 HOH   A O   
7074 O O   A HOH   E .   ? 0.4998 0.3548 0.3303 0.1869  0.0868  0.1422  436 HOH   A O   
7075 O O   . HOH   E .   ? 0.2314 0.1840 0.2016 -0.0109 -0.0080 -0.0229 437 HOH   A O   
7076 O O   . HOH   E .   ? 0.2472 0.2997 0.2892 0.0030  -0.0138 -0.0478 438 HOH   A O   
7077 O O   . HOH   E .   ? 0.6961 0.5520 0.7721 0.0685  -0.0590 0.1610  439 HOH   A O   
7078 O O   . HOH   E .   ? 0.4546 0.3958 0.3252 0.2527  -0.0200 -0.0048 440 HOH   A O   
7079 O O   . HOH   E .   ? 0.5580 0.5250 0.5724 -0.1700 -0.0800 -0.1143 441 HOH   A O   
7080 O O   . HOH   E .   ? 0.3142 0.4363 0.6035 -0.0279 0.0915  -0.2049 442 HOH   A O   
7081 O O   . HOH   E .   ? 0.2018 0.2323 0.4953 -0.0170 -0.0860 0.0610  443 HOH   A O   
7082 O O   . HOH   E .   ? 0.7263 0.7190 0.7498 0.0324  -0.1059 -0.0712 444 HOH   A O   
7083 O O   . HOH   E .   ? 0.2431 0.2124 0.3184 -0.0002 0.0222  0.0434  445 HOH   A O   
7084 O O   . HOH   E .   ? 0.9327 0.3895 0.4956 0.0408  0.1419  0.1811  446 HOH   A O   
7085 O O   . HOH   E .   ? 0.7785 0.7616 0.8115 -0.1070 0.0181  -0.1341 447 HOH   A O   
7086 O O   . HOH   E .   ? 0.4120 0.3195 0.4116 0.0395  -0.0055 0.0589  448 HOH   A O   
7087 O O   . HOH   E .   ? 0.4591 0.5003 0.5130 0.2072  -0.0806 0.0697  449 HOH   A O   
7088 O O   . HOH   E .   ? 0.4359 0.5011 0.4475 -0.0144 0.1253  -0.0328 450 HOH   A O   
7089 O O   . HOH   E .   ? 0.6363 0.6422 0.4899 -0.0841 0.0611  0.1067  451 HOH   A O   
7090 O O   . HOH   E .   ? 0.7628 0.7773 0.5161 0.1306  -0.0539 -0.0764 452 HOH   A O   
7091 O O   . HOH   E .   ? 0.5537 0.5617 0.4544 0.0809  0.0140  0.0691  453 HOH   A O   
7092 O O   . HOH   E .   ? 0.2915 0.2726 0.4237 -0.0418 0.0426  -0.0900 454 HOH   A O   
7093 O O   . HOH   E .   ? 0.4363 0.5712 0.4368 0.0649  -0.0717 -0.0920 455 HOH   A O   
7094 O O   . HOH   E .   ? 0.4480 0.5207 0.6247 -0.1194 0.1519  -0.1390 456 HOH   A O   
7095 O O   . HOH   E .   ? 0.3337 0.3351 0.7239 0.0736  -0.2109 -0.0866 457 HOH   A O   
7096 O O   . HOH   E .   ? 0.4578 0.5106 0.5512 0.0327  0.0026  0.1382  458 HOH   A O   
7097 O O   . HOH   E .   ? 0.4862 0.4513 0.5213 -0.1164 0.0566  0.0232  459 HOH   A O   
7098 O O   . HOH   E .   ? 0.2605 0.4674 0.5677 0.0472  0.0019  -0.1993 460 HOH   A O   
7099 O O   . HOH   E .   ? 0.3994 0.7296 0.4199 -0.1230 -0.1263 0.2516  461 HOH   A O   
7100 O O   . HOH   E .   ? 0.2880 0.2952 0.4793 -0.1040 0.0533  -0.0368 462 HOH   A O   
7101 O O   . HOH   E .   ? 0.6652 0.5243 0.4809 0.1135  -0.0557 -0.0756 463 HOH   A O   
7102 O O   . HOH   E .   ? 0.6271 0.4903 0.5240 -0.0176 0.1077  0.0253  464 HOH   A O   
7103 O O   . HOH   E .   ? 0.6716 0.3955 0.6442 0.0897  -0.0320 0.2218  465 HOH   A O   
7104 O O   . HOH   E .   ? 0.2706 0.1943 0.2921 0.0056  -0.0829 -0.0372 466 HOH   A O   
7105 O O   . HOH   E .   ? 0.7499 0.6840 0.5595 0.1972  -0.1453 -0.0429 467 HOH   A O   
7106 O O   . HOH   E .   ? 0.7440 0.6756 0.6751 0.0549  0.1231  0.2359  468 HOH   A O   
7107 O O   . HOH   E .   ? 0.4038 0.3433 0.4244 0.0456  0.1022  0.0453  469 HOH   A O   
7108 O O   . HOH   E .   ? 0.4366 0.5504 0.3089 0.0374  -0.0051 -0.0071 470 HOH   A O   
7109 O O   . HOH   E .   ? 0.4743 0.5014 0.5431 -0.2180 -0.0494 -0.0352 471 HOH   A O   
7110 O O   . HOH   E .   ? 0.7046 0.4871 0.5319 -0.0862 -0.0631 -0.0405 472 HOH   A O   
7111 O O   . HOH   E .   ? 0.4964 0.3309 0.3910 -0.1122 -0.1466 0.0666  473 HOH   A O   
7112 O O   . HOH   E .   ? 0.2746 0.4007 0.5945 -0.0124 0.1075  -0.0703 474 HOH   A O   
7113 O O   . HOH   E .   ? 0.7232 0.6760 0.7068 -0.1731 -0.1406 -0.0307 475 HOH   A O   
7114 O O   . HOH   E .   ? 0.3486 0.2705 0.5803 0.0290  0.0228  0.0992  476 HOH   A O   
7115 O O   . HOH   E .   ? 0.7561 0.6985 0.7687 -0.0445 0.0378  -0.1014 477 HOH   A O   
7116 O O   . HOH   E .   ? 0.6317 0.4331 0.5181 -0.0423 -0.0235 -0.1062 478 HOH   A O   
7117 O O   . HOH   E .   ? 0.8008 0.4241 0.3699 0.0240  -0.1452 0.0373  479 HOH   A O   
7118 O O   . HOH   E .   ? 0.2822 0.2629 0.2719 0.0252  -0.0206 0.0081  480 HOH   A O   
7119 O O   . HOH   E .   ? 0.4329 0.6076 0.3471 -0.0330 -0.0362 -0.0156 481 HOH   A O   
7120 O O   . HOH   E .   ? 0.2993 0.4150 0.5155 -0.0039 0.1166  0.0880  482 HOH   A O   
7121 O O   . HOH   E .   ? 0.6657 0.6450 0.7237 0.0693  0.2764  -0.1001 483 HOH   A O   
7122 O O   . HOH   E .   ? 0.4708 0.3545 0.5429 -0.0663 -0.0191 0.1701  484 HOH   A O   
7123 O O   . HOH   E .   ? 0.7123 0.4014 0.4230 -0.0309 0.1561  -0.0185 485 HOH   A O   
7124 O O   . HOH   E .   ? 0.2821 0.2479 0.7333 -0.0024 -0.1436 0.0359  486 HOH   A O   
7125 O O   . HOH   E .   ? 0.6108 0.6796 0.7327 0.0403  -0.1085 0.1216  487 HOH   A O   
7126 O O   . HOH   E .   ? 0.6809 0.8064 0.5070 -0.1229 0.1365  0.1894  488 HOH   A O   
7127 O O   . HOH   E .   ? 0.2877 0.5431 0.4002 0.0991  0.1086  0.2541  489 HOH   A O   
7128 O O   . HOH   E .   ? 0.4642 0.4178 0.3189 -0.1251 0.1306  -0.1021 490 HOH   A O   
7129 O O   . HOH   E .   ? 0.4984 0.3485 0.4474 -0.0072 0.1943  0.0143  491 HOH   A O   
7130 O O   . HOH   E .   ? 0.4170 0.8706 0.6475 -0.1356 -0.0620 0.2772  492 HOH   A O   
7131 O O   . HOH   E .   ? 0.3126 0.3766 0.3699 0.0973  -0.0379 0.0797  493 HOH   A O   
7132 O O   . HOH   E .   ? 0.3211 0.4275 0.5004 0.0834  -0.0761 -0.0403 494 HOH   A O   
7133 O O   . HOH   E .   ? 0.3206 0.4468 0.3758 0.0219  -0.0549 -0.0828 495 HOH   A O   
7134 O O   . HOH   E .   ? 0.6745 0.2539 0.4323 -0.0791 0.1094  0.0079  496 HOH   A O   
7135 O O   . HOH   E .   ? 0.6191 0.8489 0.5573 0.1221  -0.0756 0.1399  497 HOH   A O   
7136 O O   . HOH   E .   ? 0.5132 0.3360 0.5193 0.1555  -0.1083 0.0536  498 HOH   A O   
7137 O O   . HOH   E .   ? 0.3753 0.9253 0.3208 0.1711  0.0245  0.0847  499 HOH   A O   
7138 O O   . HOH   E .   ? 0.5674 0.7597 0.6278 0.3076  0.0301  0.2171  500 HOH   A O   
7139 O O   . HOH   E .   ? 0.3174 0.2532 0.5027 0.0022  0.0298  0.0482  501 HOH   A O   
7140 O O   T HOH   E .   ? 0.0987 0.1219 0.2145 -0.0232 0.0027  0.0483  502 HOH   A O   
7141 O O   . HOH   E .   ? 0.3342 0.6423 0.5223 0.0152  0.0463  -0.0984 503 HOH   A O   
7142 O O   . HOH   E .   ? 0.6529 0.6659 0.4630 -0.0773 -0.1092 -0.1371 504 HOH   A O   
7143 O O   . HOH   E .   ? 0.5026 0.8003 0.5374 -0.0819 -0.0681 0.1297  505 HOH   A O   
7144 O O   . HOH   E .   ? 0.4914 0.5311 0.5265 0.1522  0.0345  0.1701  506 HOH   A O   
7145 O O   . HOH   E .   ? 0.2677 0.4890 0.6715 0.0301  -0.0265 0.3051  507 HOH   A O   
7146 O O   . HOH   F .   ? 0.2331 0.2578 0.3585 -0.0042 0.0580  0.0266  201 HOH   B O   
7147 O O   . HOH   F .   ? 0.3444 0.2410 0.6424 -0.0242 0.2360  0.0012  202 HOH   B O   
7148 O O   . HOH   F .   ? 0.3559 0.3809 0.7021 -0.0551 -0.0088 -0.0457 203 HOH   B O   
7149 O O   . HOH   F .   ? 0.5327 0.3789 0.4659 -0.0173 0.0024  -0.1946 204 HOH   B O   
7150 O O   . HOH   F .   ? 0.4646 0.3833 0.5701 -0.0888 -0.0192 -0.1373 205 HOH   B O   
7151 O O   . HOH   F .   ? 0.3017 0.1989 0.6124 0.0122  0.1916  0.0705  206 HOH   B O   
7152 O O   . HOH   F .   ? 0.6400 0.6155 0.6443 0.1640  0.0841  0.0040  207 HOH   B O   
7153 O O   . HOH   F .   ? 0.3296 0.4693 0.3205 -0.0247 -0.0157 -0.1244 208 HOH   B O   
7154 O O   . HOH   F .   ? 0.1640 0.2197 0.3395 -0.0180 -0.0167 0.0022  209 HOH   B O   
7155 O O   . HOH   F .   ? 0.1987 0.2247 0.3375 -0.0073 0.0150  -0.0200 210 HOH   B O   
7156 O O   . HOH   F .   ? 0.3074 0.6136 0.5933 -0.0047 0.1718  -0.1977 211 HOH   B O   
7157 O O   . HOH   F .   ? 0.3032 0.7213 0.3765 0.0663  0.0275  0.2621  212 HOH   B O   
7158 O O   . HOH   F .   ? 0.4835 0.5772 0.3918 0.3021  -0.0245 0.0446  213 HOH   B O   
7159 O O   . HOH   F .   ? 0.7400 0.3492 0.4757 0.0862  0.0825  -0.0018 214 HOH   B O   
7160 O O   . HOH   F .   ? 0.4291 0.5155 0.5691 0.2521  0.0558  -0.0106 215 HOH   B O   
7161 O O   . HOH   F .   ? 0.5248 0.7134 0.4159 0.2368  0.0527  0.0955  216 HOH   B O   
7162 O O   . HOH   F .   ? 0.4738 0.4183 0.6293 -0.0199 -0.1877 -0.0787 217 HOH   B O   
7163 O O   . HOH   F .   ? 0.4655 0.6442 0.4792 0.2811  -0.1372 -0.0161 218 HOH   B O   
7164 O O   . HOH   F .   ? 0.2846 0.2776 0.6437 0.0542  -0.0655 0.0654  219 HOH   B O   
7165 O O   . HOH   F .   ? 0.3461 0.3597 0.4875 0.0296  -0.0889 0.0448  220 HOH   B O   
7166 O O   . HOH   F .   ? 0.4861 0.4040 0.3690 0.0208  -0.1264 0.0228  221 HOH   B O   
7167 O O   . HOH   F .   ? 0.2706 0.2466 0.4160 -0.0513 0.0170  -0.0666 222 HOH   B O   
7168 O O   . HOH   F .   ? 0.1748 0.1577 0.2718 -0.0271 -0.0078 0.0095  223 HOH   B O   
7169 O O   . HOH   F .   ? 0.1897 0.2291 0.3881 -0.0229 0.0157  -0.0161 224 HOH   B O   
7170 O O   . HOH   F .   ? 0.6434 0.4930 0.3059 -0.1216 0.0477  0.0161  225 HOH   B O   
7171 O O   . HOH   F .   ? 0.2492 0.3105 0.3679 -0.0927 0.0185  -0.0069 226 HOH   B O   
7172 O O   . HOH   F .   ? 0.5347 0.2979 0.3919 -0.1353 -0.0386 0.0058  227 HOH   B O   
7173 O O   . HOH   F .   ? 0.5799 0.2253 0.3213 -0.0129 -0.1149 0.0192  228 HOH   B O   
7174 O O   . HOH   F .   ? 0.5438 0.3006 0.4146 -0.2198 -0.0376 0.0333  229 HOH   B O   
7175 O O   . HOH   F .   ? 0.5036 0.4777 0.4173 0.0385  0.1083  -0.1836 230 HOH   B O   
7176 O O   . HOH   F .   ? 0.2462 0.1973 0.2644 -0.0267 0.0912  -0.0080 231 HOH   B O   
7177 O O   . HOH   F .   ? 0.2875 0.6578 0.6196 0.1798  -0.0590 -0.1017 232 HOH   B O   
7178 O O   . HOH   F .   ? 0.4966 0.4197 0.6635 0.0218  -0.0994 0.2814  233 HOH   B O   
7179 O O   . HOH   F .   ? 0.7275 0.5740 0.4749 0.2204  -0.0284 -0.1006 234 HOH   B O   
7180 O O   . HOH   F .   ? 0.3730 0.2689 0.4771 0.0293  -0.0829 -0.1390 235 HOH   B O   
7181 O O   . HOH   F .   ? 0.3691 0.2104 0.2115 0.0153  -0.0832 -0.0211 236 HOH   B O   
7182 O O   . HOH   F .   ? 0.2757 0.2220 0.3210 0.0596  0.0620  -0.0090 237 HOH   B O   
7183 O O   . HOH   F .   ? 0.3247 0.3345 0.3191 -0.0927 -0.0129 -0.0009 238 HOH   B O   
7184 O O   . HOH   F .   ? 0.1675 0.1557 0.1558 -0.0112 -0.0078 -0.0059 239 HOH   B O   
7185 O O   . HOH   F .   ? 0.2064 0.1477 0.3796 0.0121  -0.0587 -0.0176 240 HOH   B O   
7186 O O   . HOH   F .   ? 0.2702 0.2746 0.3454 0.0321  0.0007  -0.0911 241 HOH   B O   
7187 O O   . HOH   F .   ? 0.4053 0.2926 0.2300 0.0348  0.0743  0.0448  242 HOH   B O   
7188 O O   . HOH   F .   ? 0.3261 0.4214 0.2710 0.0153  0.0842  0.0436  243 HOH   B O   
7189 O O   . HOH   F .   ? 0.2496 0.3504 0.2931 -0.0509 -0.0354 0.0459  244 HOH   B O   
7190 O O   . HOH   F .   ? 0.3237 0.2037 0.6559 -0.0371 -0.1206 0.0084  245 HOH   B O   
7191 O O   . HOH   F .   ? 0.1721 0.1725 0.2774 -0.0008 0.0016  -0.0023 246 HOH   B O   
7192 O O   . HOH   F .   ? 0.2209 0.2245 0.2315 -0.0456 -0.0502 0.0228  247 HOH   B O   
7193 O O   . HOH   F .   ? 0.1630 0.1530 0.1676 -0.0018 -0.0101 0.0050  248 HOH   B O   
7194 O O   . HOH   F .   ? 0.2409 0.2241 0.3130 0.0790  -0.0840 -0.0627 249 HOH   B O   
7195 O O   . HOH   F .   ? 0.7049 0.6780 0.3875 0.0013  -0.0401 0.0825  250 HOH   B O   
7196 O O   . HOH   F .   ? 0.2703 0.3731 0.2224 -0.0998 0.0393  0.0382  251 HOH   B O   
7197 O O   . HOH   F .   ? 0.3630 0.2887 0.3583 -0.0504 0.0174  -0.0591 252 HOH   B O   
7198 O O   . HOH   F .   ? 0.4143 0.4189 0.4283 0.1522  -0.0595 -0.1222 253 HOH   B O   
7199 O O   . HOH   F .   ? 0.2524 0.3955 0.3674 -0.0797 -0.0910 -0.0427 254 HOH   B O   
7200 O O   . HOH   F .   ? 0.2174 0.5074 0.5627 -0.0554 -0.0176 -0.1249 255 HOH   B O   
7201 O O   . HOH   F .   ? 0.4060 0.4854 0.6128 -0.1808 -0.0006 0.0963  256 HOH   B O   
7202 O O   . HOH   F .   ? 0.4765 0.6442 0.2657 -0.0805 -0.0835 0.0829  257 HOH   B O   
7203 O O   . HOH   F .   ? 0.2269 0.1715 0.2264 -0.0434 -0.0570 0.0384  258 HOH   B O   
7204 O O   . HOH   F .   ? 0.3587 0.2758 0.4318 0.0646  -0.0606 -0.0774 259 HOH   B O   
7205 O O   . HOH   F .   ? 0.1655 0.1815 0.3605 -0.0316 -0.0287 0.0157  260 HOH   B O   
7206 O O   . HOH   F .   ? 0.3578 0.5191 0.3531 -0.0374 -0.1243 0.0391  261 HOH   B O   
7207 O O   . HOH   F .   ? 0.1574 0.1797 0.2432 -0.0072 0.0066  0.0222  262 HOH   B O   
7208 O O   . HOH   F .   ? 0.4228 0.4459 0.3378 0.0636  0.0011  -0.0293 263 HOH   B O   
7209 O O   . HOH   F .   ? 0.2979 0.4085 0.3045 -0.0950 -0.0304 -0.0309 264 HOH   B O   
7210 O O   . HOH   F .   ? 0.4763 0.3534 0.5010 -0.0380 0.0670  -0.0408 265 HOH   B O   
7211 O O   . HOH   F .   ? 0.4864 0.4018 0.4283 -0.1552 0.0767  -0.1427 266 HOH   B O   
7212 O O   . HOH   F .   ? 0.2934 0.3672 0.4118 0.0321  0.1262  0.0516  267 HOH   B O   
7213 O O   . HOH   F .   ? 0.2237 0.1733 0.2445 -0.0304 -0.0192 0.0153  268 HOH   B O   
7214 O O   . HOH   F .   ? 0.2775 0.2818 0.2842 -0.0464 -0.0967 0.0251  269 HOH   B O   
7215 O O   . HOH   F .   ? 0.3053 0.4856 0.6283 -0.0195 0.0409  -0.1409 270 HOH   B O   
7216 O O   . HOH   F .   ? 0.3571 0.2323 0.2003 0.0370  -0.0388 -0.0145 271 HOH   B O   
7217 O O   . HOH   F .   ? 0.2702 0.2627 0.2226 -0.0020 -0.0063 0.0080  272 HOH   B O   
7218 O O   . HOH   F .   ? 0.2397 0.2177 0.4078 -0.0014 -0.0804 -0.0398 273 HOH   B O   
7219 O O   . HOH   F .   ? 0.1977 0.1640 0.3446 -0.0041 -0.0309 -0.0323 274 HOH   B O   
7220 O O   . HOH   F .   ? 0.2108 0.2046 0.1801 -0.0588 -0.0665 0.0247  275 HOH   B O   
7221 O O   . HOH   F .   ? 0.3194 0.8320 0.7676 0.1972  -0.0959 -0.1092 276 HOH   B O   
7222 O O   . HOH   F .   ? 0.3934 0.4965 0.6779 -0.0021 0.1183  0.0243  277 HOH   B O   
7223 O O   . HOH   F .   ? 0.2387 0.3731 0.3852 -0.0351 0.0337  -0.1277 278 HOH   B O   
7224 O O   . HOH   F .   ? 0.2566 0.2655 0.2351 -0.0399 -0.0659 -0.0440 279 HOH   B O   
7225 O O   . HOH   F .   ? 0.6025 0.4145 0.3455 0.2787  0.1361  0.0978  280 HOH   B O   
7226 O O   . HOH   F .   ? 0.1768 0.1704 0.2084 0.0014  0.0020  0.0106  281 HOH   B O   
7227 O O   . HOH   F .   ? 0.1922 0.1672 0.3707 -0.0162 -0.0049 -0.0115 282 HOH   B O   
7228 O O   . HOH   F .   ? 0.2863 0.4383 0.2575 0.1395  -0.0492 -0.0632 283 HOH   B O   
7229 O O   . HOH   F .   ? 0.2699 0.2181 0.3276 -0.0737 0.0287  -0.0282 284 HOH   B O   
7230 O O   . HOH   F .   ? 0.2228 0.2405 0.5631 -0.0521 0.0035  0.1373  285 HOH   B O   
7231 O O   . HOH   F .   ? 0.4362 0.2894 0.4391 -0.0077 -0.1415 -0.0164 286 HOH   B O   
7232 O O   . HOH   F .   ? 0.3334 0.2392 0.4824 0.0281  0.0336  0.0732  287 HOH   B O   
7233 O O   . HOH   F .   ? 0.3783 0.2880 0.2308 0.0069  -0.0817 0.0009  288 HOH   B O   
7234 O O   . HOH   F .   ? 0.3363 0.4973 0.4942 -0.1161 -0.1187 0.0722  289 HOH   B O   
7235 O O   . HOH   F .   ? 0.2818 0.2731 0.3368 0.0083  -0.0749 0.0429  290 HOH   B O   
7236 O O   . HOH   F .   ? 0.4971 0.5896 0.5062 0.0648  -0.1704 0.0369  291 HOH   B O   
7237 O O   . HOH   F .   ? 0.1925 0.2474 0.3328 0.0208  0.0065  0.0204  292 HOH   B O   
7238 O O   . HOH   F .   ? 0.1749 0.2146 0.1819 -0.0144 -0.0216 0.0071  293 HOH   B O   
7239 O O   . HOH   F .   ? 0.3034 0.3262 0.3239 -0.0340 0.0362  -0.1422 294 HOH   B O   
7240 O O   . HOH   F .   ? 0.3821 0.2435 0.4893 -0.1101 -0.2236 0.1174  295 HOH   B O   
7241 O O   . HOH   F .   ? 0.3172 0.7424 0.2493 0.1473  -0.0458 -0.0672 296 HOH   B O   
7242 O O   . HOH   F .   ? 0.5643 0.5588 0.4945 0.2698  -0.0049 0.0186  297 HOH   B O   
7243 O O   . HOH   F .   ? 0.5018 0.3732 0.2605 0.1136  -0.0939 0.0401  298 HOH   B O   
7244 O O   . HOH   F .   ? 0.1865 0.3847 0.5481 0.0514  -0.0164 -0.1688 299 HOH   B O   
7245 O O   . HOH   F .   ? 0.4834 0.5346 0.2512 0.0185  0.0909  0.0984  300 HOH   B O   
7246 O O   . HOH   F .   ? 0.2623 0.3122 0.5292 -0.0166 -0.0667 0.0125  301 HOH   B O   
7247 O O   . HOH   F .   ? 0.3853 0.3392 0.5594 -0.0709 -0.1202 0.1715  302 HOH   B O   
7248 O O   . HOH   F .   ? 0.4646 0.2879 0.2693 -0.1608 0.0503  -0.0219 303 HOH   B O   
7249 O O   . HOH   F .   ? 0.1932 0.1706 0.3011 0.0121  0.0054  0.0174  304 HOH   B O   
7250 O O   . HOH   F .   ? 0.2223 0.3309 0.6660 0.0765  -0.0437 -0.1382 305 HOH   B O   
7251 O O   . HOH   F .   ? 0.5637 0.3593 0.4672 -0.1226 0.0028  0.1098  306 HOH   B O   
7252 O O   . HOH   F .   ? 0.2714 0.1650 0.3046 -0.0287 -0.0461 0.0383  307 HOH   B O   
7253 O O   . HOH   F .   ? 0.3359 0.2046 0.3960 0.0659  0.0988  0.0378  308 HOH   B O   
7254 O O   . HOH   F .   ? 0.3131 0.2967 0.4171 -0.0500 0.1543  -0.0913 309 HOH   B O   
7255 O O   . HOH   F .   ? 0.2277 0.1796 0.3040 -0.0385 -0.0305 -0.0001 310 HOH   B O   
7256 O O   . HOH   F .   ? 0.4486 0.6427 0.4481 0.1235  -0.0659 0.0981  311 HOH   B O   
7257 O O   . HOH   F .   ? 0.2415 0.1977 0.2208 -0.0026 0.0180  0.0093  312 HOH   B O   
7258 O O   . HOH   F .   ? 0.2361 0.4873 0.5199 -0.0878 -0.0355 -0.0056 313 HOH   B O   
7259 O O   . HOH   F .   ? 0.1649 0.1644 0.3959 0.0103  0.0041  -0.0039 314 HOH   B O   
7260 O O   . HOH   F .   ? 0.2058 0.1869 0.3679 0.0371  -0.0798 0.0073  315 HOH   B O   
7261 O O   . HOH   F .   ? 0.3571 0.4917 0.8304 -0.0154 -0.0983 0.2390  316 HOH   B O   
7262 O O   . HOH   F .   ? 0.5462 0.4629 0.2739 -0.0037 -0.0579 -0.0706 317 HOH   B O   
7263 O O   . HOH   F .   ? 0.4205 0.4470 0.4355 -0.2192 0.1288  -0.0742 318 HOH   B O   
7264 O O   . HOH   F .   ? 0.6322 0.5048 0.7405 0.1476  -0.0947 0.1922  319 HOH   B O   
7265 O O   . HOH   F .   ? 0.8086 0.6262 0.3339 -0.0154 -0.0380 0.1004  320 HOH   B O   
7266 O O   . HOH   F .   ? 0.1763 0.1721 0.3528 -0.0193 -0.0178 -0.0105 321 HOH   B O   
7267 O O   . HOH   F .   ? 0.1796 0.2759 0.2557 -0.0153 -0.0186 0.0722  322 HOH   B O   
7268 O O   . HOH   F .   ? 0.5111 0.2807 0.3461 0.0165  0.0301  0.1065  323 HOH   B O   
7269 O O   . HOH   F .   ? 0.1752 0.1957 0.3456 -0.0308 -0.0121 0.0060  324 HOH   B O   
7270 O O   . HOH   F .   ? 0.3622 0.2380 0.2712 0.0459  -0.0336 0.0179  325 HOH   B O   
7271 O O   . HOH   F .   ? 0.4277 0.2616 0.2889 0.1627  0.0875  0.0350  326 HOH   B O   
7272 O O   . HOH   F .   ? 0.2274 0.1832 0.2928 0.0336  0.0467  0.0306  327 HOH   B O   
7273 O O   . HOH   F .   ? 0.3009 0.2251 0.4551 -0.0124 -0.0310 0.0807  328 HOH   B O   
7274 O O   . HOH   F .   ? 0.4662 0.3217 0.5637 0.1245  0.2184  0.1777  329 HOH   B O   
7275 O O   . HOH   F .   ? 0.2118 0.3178 0.3551 0.0595  -0.0365 -0.0901 330 HOH   B O   
7276 O O   . HOH   F .   ? 0.4953 0.4905 0.2405 0.1516  -0.0629 -0.0445 331 HOH   B O   
7277 O O   . HOH   F .   ? 0.6924 0.4850 0.5186 0.0901  0.1714  -0.0380 332 HOH   B O   
7278 O O   . HOH   F .   ? 0.8386 0.2348 0.4206 0.0432  -0.1064 -0.0245 333 HOH   B O   
7279 O O   . HOH   F .   ? 0.5695 0.4381 0.4541 0.0996  0.1591  0.2104  334 HOH   B O   
7280 O O   . HOH   F .   ? 0.2973 0.3420 0.5876 -0.0643 -0.1690 0.1787  335 HOH   B O   
7281 O O   . HOH   F .   ? 0.5335 0.4071 0.5020 0.0663  -0.0115 0.0328  336 HOH   B O   
7282 O O   . HOH   F .   ? 0.1836 0.1624 0.2711 0.0050  -0.0210 0.0140  337 HOH   B O   
7283 O O   . HOH   F .   ? 0.5074 0.4174 0.4676 0.0247  0.0523  -0.1410 338 HOH   B O   
7284 O O   . HOH   F .   ? 0.3541 0.6232 0.4462 -0.1132 -0.0830 -0.0398 339 HOH   B O   
7285 O O   . HOH   F .   ? 0.5985 0.4419 0.5872 -0.0671 -0.1085 -0.1548 340 HOH   B O   
7286 O O   . HOH   F .   ? 0.5183 0.7649 0.4262 -0.0478 -0.0973 0.2145  341 HOH   B O   
7287 O O   . HOH   F .   ? 0.6452 0.6312 0.6453 -0.1055 -0.0666 0.2403  342 HOH   B O   
7288 O O   . HOH   F .   ? 0.5174 0.3188 0.3692 0.0212  -0.1273 -0.0675 343 HOH   B O   
7289 O O   . HOH   F .   ? 0.2849 0.1976 0.4012 0.0289  -0.0741 -0.0366 344 HOH   B O   
7290 O O   . HOH   F .   ? 0.3129 0.6053 0.7507 -0.0375 -0.0925 0.0021  345 HOH   B O   
7291 O O   . HOH   F .   ? 0.2328 0.2166 0.3461 -0.0037 0.0571  -0.0100 346 HOH   B O   
7292 O O   . HOH   F .   ? 0.4747 0.6386 0.5891 -0.1242 -0.0082 0.0555  347 HOH   B O   
7293 O O   . HOH   F .   ? 0.3853 0.4158 0.5976 -0.1444 0.0045  -0.0619 348 HOH   B O   
7294 O O   . HOH   F .   ? 0.3197 0.2518 0.5119 -0.0462 -0.1027 -0.0570 349 HOH   B O   
7295 O O   . HOH   F .   ? 0.4047 0.6302 0.6037 -0.0116 -0.0932 0.0196  350 HOH   B O   
7296 O O   . HOH   F .   ? 0.5592 0.5740 0.3970 -0.0125 -0.1196 0.0013  351 HOH   B O   
7297 O O   . HOH   F .   ? 0.2584 0.6731 0.3650 0.1599  -0.0735 -0.1749 352 HOH   B O   
7298 O O   . HOH   F .   ? 0.2589 0.4613 0.5926 -0.0259 0.0275  0.0602  353 HOH   B O   
7299 O O   . HOH   F .   ? 0.5037 0.5887 0.6573 0.0277  0.0150  -0.0206 354 HOH   B O   
7300 O O   . HOH   F .   ? 0.5042 0.5493 0.4951 0.1929  -0.1196 0.1351  355 HOH   B O   
7301 O O   . HOH   F .   ? 0.3921 0.2328 0.3355 -0.0523 0.0321  -0.0790 356 HOH   B O   
7302 O O   . HOH   F .   ? 0.4827 0.3254 0.5881 -0.1349 0.1269  0.0358  357 HOH   B O   
7303 O O   . HOH   F .   ? 0.3889 0.2813 0.3739 -0.1122 0.0037  -0.0507 358 HOH   B O   
7304 O O   . HOH   F .   ? 0.5580 0.3568 0.4534 0.0460  0.1506  -0.0831 359 HOH   B O   
7305 O O   . HOH   F .   ? 0.4734 0.4839 0.6102 -0.0086 0.0412  0.1822  360 HOH   B O   
7306 O O   . HOH   F .   ? 0.5322 0.3551 0.5437 -0.0245 -0.1660 -0.0666 361 HOH   B O   
7307 O O   . HOH   F .   ? 0.3814 0.7137 0.3325 0.1824  -0.0265 -0.0001 362 HOH   B O   
7308 O O   . HOH   F .   ? 0.2538 0.4417 0.7203 -0.1214 -0.0530 -0.0620 363 HOH   B O   
7309 O O   . HOH   F .   ? 0.6450 0.2688 0.3714 -0.0219 0.0108  0.0664  364 HOH   B O   
7310 O O   . HOH   F .   ? 0.5962 0.5533 0.5134 -0.0435 -0.0056 0.0596  365 HOH   B O   
7311 O O   . HOH   F .   ? 0.5375 0.6281 0.5289 -0.1029 -0.0358 -0.1263 366 HOH   B O   
7312 O O   . HOH   F .   ? 0.3815 0.3882 0.5620 0.0788  -0.1637 0.0228  367 HOH   B O   
7313 O O   . HOH   F .   ? 0.4702 0.3288 0.5538 -0.1215 -0.0760 0.0025  368 HOH   B O   
7314 O O   . HOH   F .   ? 0.6614 0.5537 0.4624 0.1772  0.0340  0.0800  369 HOH   B O   
7315 O O   . HOH   F .   ? 0.4881 0.5466 0.3535 0.0749  -0.1435 0.0456  370 HOH   B O   
7316 O O   . HOH   F .   ? 0.7404 0.7675 0.5402 0.1669  -0.1254 0.0420  371 HOH   B O   
7317 O O   . HOH   F .   ? 0.4501 0.5346 0.5952 0.2242  0.1533  0.1345  372 HOH   B O   
7318 O O   . HOH   F .   ? 0.4277 0.3421 0.3697 0.0881  -0.1216 -0.0264 373 HOH   B O   
7319 O O   . HOH   F .   ? 0.4265 0.5197 0.5139 -0.0411 -0.0510 -0.0062 374 HOH   B O   
7320 O O   . HOH   F .   ? 0.6263 0.4061 0.3370 -0.0866 -0.1246 -0.0581 375 HOH   B O   
7321 O O   . HOH   F .   ? 0.5049 0.7038 0.6143 0.1408  0.0371  0.2507  376 HOH   B O   
7322 O O   . HOH   F .   ? 0.4076 0.6152 0.2509 -0.0950 0.0106  -0.0087 377 HOH   B O   
7323 O O   . HOH   F .   ? 0.6062 0.7277 0.4626 -0.1424 0.0532  -0.1483 378 HOH   B O   
7324 O O   . HOH   F .   ? 0.3947 0.5207 0.5819 0.1311  -0.0219 0.0345  379 HOH   B O   
7325 O O   . HOH   F .   ? 0.2330 0.4312 0.4550 0.0242  -0.0383 -0.0637 380 HOH   B O   
7326 O O   . HOH   F .   ? 0.6793 0.4053 0.5150 -0.0857 -0.0512 -0.0016 381 HOH   B O   
7327 O O   . HOH   F .   ? 0.5825 0.7187 0.7287 -0.1174 0.1391  0.0892  382 HOH   B O   
7328 O O   . HOH   F .   ? 0.4782 0.8845 0.5616 0.0252  0.1555  0.0466  383 HOH   B O   
7329 O O   . HOH   F .   ? 0.3057 0.2597 0.3628 0.0056  0.0263  0.0151  384 HOH   B O   
7330 O O   . HOH   F .   ? 0.6680 0.4161 0.4254 0.1062  0.1196  -0.0048 385 HOH   B O   
7331 O O   . HOH   F .   ? 0.5299 0.5737 0.4826 0.0618  -0.0597 -0.0697 386 HOH   B O   
7332 O O   . HOH   F .   ? 0.8142 0.5880 0.5333 0.1952  0.0408  -0.0325 387 HOH   B O   
7333 O O   . HOH   F .   ? 0.2700 0.4921 0.4291 -0.1019 -0.1046 -0.0345 388 HOH   B O   
7334 O O   . HOH   F .   ? 0.6234 0.5179 0.5806 -0.0609 0.0963  -0.0462 389 HOH   B O   
7335 O O   . HOH   F .   ? 0.4755 0.4540 0.3946 0.0042  0.0698  -0.0657 390 HOH   B O   
7336 O O   . HOH   F .   ? 0.4987 0.3781 0.5324 -0.1909 0.0062  0.0709  391 HOH   B O   
7337 O O   . HOH   F .   ? 0.4452 0.2479 0.3572 0.0822  -0.0433 0.0134  392 HOH   B O   
7338 O O   . HOH   F .   ? 0.5504 0.5840 0.5570 0.1153  0.1217  0.0497  393 HOH   B O   
7339 O O   . HOH   F .   ? 0.3845 0.2572 0.5272 -0.0019 0.0303  0.0974  394 HOH   B O   
7340 O O   . HOH   F .   ? 0.2671 0.4419 0.7207 -0.1321 -0.0800 -0.0242 395 HOH   B O   
7341 O O   . HOH   F .   ? 0.4672 0.6545 0.4703 0.0716  0.0276  -0.1153 396 HOH   B O   
7342 O O   . HOH   F .   ? 0.5061 0.4993 0.5440 0.0594  0.1048  0.0942  397 HOH   B O   
7343 O O   . HOH   F .   ? 0.2074 0.3234 0.6310 -0.0600 -0.1038 0.0180  398 HOH   B O   
7344 O O   . HOH   F .   ? 0.3849 0.3859 0.4394 0.0052  0.0392  -0.0732 399 HOH   B O   
7345 O O   . HOH   F .   ? 0.5735 0.6754 0.6339 0.0435  -0.1429 0.2384  400 HOH   B O   
7346 O O   . HOH   F .   ? 0.5472 0.4339 0.3451 -0.2504 -0.0562 0.1145  401 HOH   B O   
7347 O O   . HOH   F .   ? 0.6445 0.5767 0.4113 0.1723  0.0219  -0.0593 402 HOH   B O   
# 
