data_7HE3
# 
_entry.id   7HE3 
# 
_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   7HE3         pdb_00007he3 10.2210/pdb7he3/pdb 
WWPDB D_1001407357 ?            ?                   
# 
_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                        7HE3 
_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 '(2S)-3-(1-methyl-1H-pyrazol-4-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 272.306   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                            35.453    1   ? ? ? ? 
5 water       nat water                                                                                     18.015    418 ? ? ? ? 
# 
_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 '(2S)-3-(1-methyl-1H-pyrazol-4-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A9F 
4 'CHLORIDE ION'                                                                            CL    
5 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 
A1A9F non-polymer         . '(2S)-3-(1-methyl-1H-pyrazol-4-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 
'C13 H16 N6 O'   272.306 
ALA   'L-peptide linking' y ALANINE                                                                                   ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                  ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                           ? 
'C4 H7 N O4'     133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                                            ? 'Cl -1' 
35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                                  ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                 ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                           ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                   ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                 ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                     ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                   ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                    ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                             ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                   ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                    ? 
'C3 H7 N O3'     105.093 
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 A1A9F 1   202 201  A1A9F LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 292  HOH   HOH A . 
F 5 HOH   2   302 196  HOH   HOH A . 
F 5 HOH   3   303 86   HOH   HOH A . 
F 5 HOH   4   304 153  HOH   HOH A . 
F 5 HOH   5   305 229  HOH   HOH A . 
F 5 HOH   6   306 625  HOH   HOH A . 
F 5 HOH   7   307 121  HOH   HOH A . 
F 5 HOH   8   308 405  HOH   HOH A . 
F 5 HOH   9   309 148  HOH   HOH A . 
F 5 HOH   10  310 209  HOH   HOH A . 
F 5 HOH   11  311 109  HOH   HOH A . 
F 5 HOH   12  312 247  HOH   HOH A . 
F 5 HOH   13  313 7    HOH   HOH A . 
F 5 HOH   14  314 151  HOH   HOH A . 
F 5 HOH   15  315 320  HOH   HOH A . 
F 5 HOH   16  316 140  HOH   HOH A . 
F 5 HOH   17  317 17   HOH   HOH A . 
F 5 HOH   18  318 76   HOH   HOH A . 
F 5 HOH   19  319 964  HOH   HOH A . 
F 5 HOH   20  320 1295 HOH   HOH A . 
F 5 HOH   21  321 124  HOH   HOH A . 
F 5 HOH   22  322 1301 HOH   HOH A . 
F 5 HOH   23  323 62   HOH   HOH A . 
F 5 HOH   24  324 154  HOH   HOH A . 
F 5 HOH   25  325 136  HOH   HOH A . 
F 5 HOH   26  326 195  HOH   HOH A . 
F 5 HOH   27  327 105  HOH   HOH A . 
F 5 HOH   28  328 21   HOH   HOH A . 
F 5 HOH   29  329 1300 HOH   HOH A . 
F 5 HOH   30  330 15   HOH   HOH A . 
F 5 HOH   31  331 225  HOH   HOH A . 
F 5 HOH   32  332 8    HOH   HOH A . 
F 5 HOH   33  333 46   HOH   HOH A . 
F 5 HOH   34  334 18   HOH   HOH A . 
F 5 HOH   35  335 241  HOH   HOH A . 
F 5 HOH   36  336 493  HOH   HOH A . 
F 5 HOH   37  337 236  HOH   HOH A . 
F 5 HOH   38  338 155  HOH   HOH A . 
F 5 HOH   39  339 1290 HOH   HOH A . 
F 5 HOH   40  340 469  HOH   HOH A . 
F 5 HOH   41  341 661  HOH   HOH A . 
F 5 HOH   42  342 337  HOH   HOH A . 
F 5 HOH   43  343 57   HOH   HOH A . 
F 5 HOH   44  344 192  HOH   HOH A . 
F 5 HOH   45  345 1283 HOH   HOH A . 
F 5 HOH   46  346 9    HOH   HOH A . 
F 5 HOH   47  347 8    HOH   HOH A . 
F 5 HOH   48  348 42   HOH   HOH A . 
F 5 HOH   49  349 164  HOH   HOH A . 
F 5 HOH   50  350 66   HOH   HOH A . 
F 5 HOH   51  351 35   HOH   HOH A . 
F 5 HOH   52  352 409  HOH   HOH A . 
F 5 HOH   53  353 630  HOH   HOH A . 
F 5 HOH   54  354 93   HOH   HOH A . 
F 5 HOH   55  355 393  HOH   HOH A . 
F 5 HOH   56  356 58   HOH   HOH A . 
F 5 HOH   57  357 92   HOH   HOH A . 
F 5 HOH   58  358 102  HOH   HOH A . 
F 5 HOH   59  359 2    HOH   HOH A . 
F 5 HOH   60  360 26   HOH   HOH A . 
F 5 HOH   61  361 354  HOH   HOH A . 
F 5 HOH   62  362 33   HOH   HOH A . 
F 5 HOH   63  363 165  HOH   HOH A . 
F 5 HOH   64  364 139  HOH   HOH A . 
F 5 HOH   65  365 70   HOH   HOH A . 
F 5 HOH   66  366 939  HOH   HOH A . 
F 5 HOH   67  367 81   HOH   HOH A . 
F 5 HOH   68  368 169  HOH   HOH A . 
F 5 HOH   69  369 39   HOH   HOH A . 
F 5 HOH   70  370 162  HOH   HOH A . 
F 5 HOH   71  371 5    HOH   HOH A . 
F 5 HOH   72  372 19   HOH   HOH A . 
F 5 HOH   73  373 85   HOH   HOH A . 
F 5 HOH   74  374 27   HOH   HOH A . 
F 5 HOH   75  375 1310 HOH   HOH A . 
F 5 HOH   76  376 56   HOH   HOH A . 
F 5 HOH   77  377 396  HOH   HOH A . 
F 5 HOH   78  378 3    HOH   HOH A . 
F 5 HOH   79  379 36   HOH   HOH A . 
F 5 HOH   80  380 1094 HOH   HOH A . 
F 5 HOH   81  381 461  HOH   HOH A . 
F 5 HOH   82  382 366  HOH   HOH A . 
F 5 HOH   83  383 296  HOH   HOH A . 
F 5 HOH   84  384 45   HOH   HOH A . 
F 5 HOH   85  385 115  HOH   HOH A . 
F 5 HOH   86  386 186  HOH   HOH A . 
F 5 HOH   87  387 138  HOH   HOH A . 
F 5 HOH   88  388 10   HOH   HOH A . 
F 5 HOH   89  389 74   HOH   HOH A . 
F 5 HOH   90  390 199  HOH   HOH A . 
F 5 HOH   91  391 159  HOH   HOH A . 
F 5 HOH   92  392 24   HOH   HOH A . 
F 5 HOH   93  393 140  HOH   HOH A . 
F 5 HOH   94  394 49   HOH   HOH A . 
F 5 HOH   95  395 1275 HOH   HOH A . 
F 5 HOH   96  396 25   HOH   HOH A . 
F 5 HOH   97  397 218  HOH   HOH A . 
F 5 HOH   98  398 134  HOH   HOH A . 
F 5 HOH   99  399 34   HOH   HOH A . 
F 5 HOH   100 400 662  HOH   HOH A . 
F 5 HOH   101 401 6    HOH   HOH A . 
F 5 HOH   102 402 1308 HOH   HOH A . 
F 5 HOH   103 403 281  HOH   HOH A . 
F 5 HOH   104 404 1    HOH   HOH A . 
F 5 HOH   105 405 12   HOH   HOH A . 
F 5 HOH   106 406 116  HOH   HOH A . 
F 5 HOH   107 407 303  HOH   HOH A . 
F 5 HOH   108 408 351  HOH   HOH A . 
F 5 HOH   109 409 83   HOH   HOH A . 
F 5 HOH   110 410 1315 HOH   HOH A . 
F 5 HOH   111 411 4    HOH   HOH A . 
F 5 HOH   112 412 1313 HOH   HOH A . 
F 5 HOH   113 413 67   HOH   HOH A . 
F 5 HOH   114 414 381  HOH   HOH A . 
F 5 HOH   115 415 123  HOH   HOH A . 
F 5 HOH   116 416 3    HOH   HOH A . 
F 5 HOH   117 417 278  HOH   HOH A . 
F 5 HOH   118 418 68   HOH   HOH A . 
F 5 HOH   119 419 1279 HOH   HOH A . 
F 5 HOH   120 420 78   HOH   HOH A . 
F 5 HOH   121 421 125  HOH   HOH A . 
F 5 HOH   122 422 397  HOH   HOH A . 
F 5 HOH   123 423 156  HOH   HOH A . 
F 5 HOH   124 424 96   HOH   HOH A . 
F 5 HOH   125 425 1296 HOH   HOH A . 
F 5 HOH   126 426 132  HOH   HOH A . 
F 5 HOH   127 427 333  HOH   HOH A . 
F 5 HOH   128 428 1309 HOH   HOH A . 
F 5 HOH   129 429 95   HOH   HOH A . 
F 5 HOH   130 430 53   HOH   HOH A . 
F 5 HOH   131 431 51   HOH   HOH A . 
F 5 HOH   132 432 1068 HOH   HOH A . 
F 5 HOH   133 433 122  HOH   HOH A . 
F 5 HOH   134 434 7    HOH   HOH A . 
F 5 HOH   135 435 582  HOH   HOH A . 
F 5 HOH   136 436 1222 HOH   HOH A . 
F 5 HOH   137 437 1289 HOH   HOH A . 
F 5 HOH   138 438 1238 HOH   HOH A . 
F 5 HOH   139 439 71   HOH   HOH A . 
F 5 HOH   140 440 80   HOH   HOH A . 
F 5 HOH   141 441 212  HOH   HOH A . 
F 5 HOH   142 442 188  HOH   HOH A . 
F 5 HOH   143 443 16   HOH   HOH A . 
F 5 HOH   144 444 952  HOH   HOH A . 
F 5 HOH   145 445 94   HOH   HOH A . 
F 5 HOH   146 446 40   HOH   HOH A . 
F 5 HOH   147 447 5    HOH   HOH A . 
F 5 HOH   148 448 1286 HOH   HOH A . 
F 5 HOH   149 449 944  HOH   HOH A . 
F 5 HOH   150 450 73   HOH   HOH A . 
F 5 HOH   151 451 576  HOH   HOH A . 
F 5 HOH   152 452 97   HOH   HOH A . 
F 5 HOH   153 453 104  HOH   HOH A . 
F 5 HOH   154 454 79   HOH   HOH A . 
F 5 HOH   155 455 509  HOH   HOH A . 
F 5 HOH   156 456 1189 HOH   HOH A . 
F 5 HOH   157 457 330  HOH   HOH A . 
F 5 HOH   158 458 1134 HOH   HOH A . 
F 5 HOH   159 459 2    HOH   HOH A . 
F 5 HOH   160 460 1119 HOH   HOH A . 
F 5 HOH   161 461 107  HOH   HOH A . 
F 5 HOH   162 462 163  HOH   HOH A . 
F 5 HOH   163 463 726  HOH   HOH A . 
F 5 HOH   164 464 408  HOH   HOH A . 
F 5 HOH   165 465 756  HOH   HOH A . 
F 5 HOH   166 466 1276 HOH   HOH A . 
F 5 HOH   167 467 126  HOH   HOH A . 
F 5 HOH   168 468 556  HOH   HOH A . 
F 5 HOH   169 469 319  HOH   HOH A . 
F 5 HOH   170 470 361  HOH   HOH A . 
F 5 HOH   171 471 63   HOH   HOH A . 
F 5 HOH   172 472 280  HOH   HOH A . 
F 5 HOH   173 473 801  HOH   HOH A . 
F 5 HOH   174 474 1307 HOH   HOH A . 
F 5 HOH   175 475 250  HOH   HOH A . 
F 5 HOH   176 476 342  HOH   HOH A . 
F 5 HOH   177 477 370  HOH   HOH A . 
F 5 HOH   178 478 202  HOH   HOH A . 
F 5 HOH   179 479 1287 HOH   HOH A . 
F 5 HOH   180 480 1306 HOH   HOH A . 
F 5 HOH   181 481 224  HOH   HOH A . 
F 5 HOH   182 482 695  HOH   HOH A . 
F 5 HOH   183 483 267  HOH   HOH A . 
F 5 HOH   184 484 135  HOH   HOH A . 
F 5 HOH   185 485 919  HOH   HOH A . 
F 5 HOH   186 486 674  HOH   HOH A . 
F 5 HOH   187 487 521  HOH   HOH A . 
F 5 HOH   188 488 326  HOH   HOH A . 
F 5 HOH   189 489 1299 HOH   HOH A . 
F 5 HOH   190 490 1314 HOH   HOH A . 
F 5 HOH   191 491 331  HOH   HOH A . 
F 5 HOH   192 492 309  HOH   HOH A . 
F 5 HOH   193 493 318  HOH   HOH A . 
F 5 HOH   194 494 941  HOH   HOH A . 
F 5 HOH   195 495 805  HOH   HOH A . 
F 5 HOH   196 496 711  HOH   HOH A . 
F 5 HOH   197 497 263  HOH   HOH A . 
F 5 HOH   198 498 315  HOH   HOH A . 
F 5 HOH   199 499 152  HOH   HOH A . 
F 5 HOH   200 500 208  HOH   HOH A . 
F 5 HOH   201 501 180  HOH   HOH A . 
F 5 HOH   202 502 356  HOH   HOH A . 
F 5 HOH   203 503 6    HOH   HOH A . 
F 5 HOH   204 504 350  HOH   HOH A . 
F 5 HOH   205 505 1071 HOH   HOH A . 
F 5 HOH   206 506 363  HOH   HOH A . 
F 5 HOH   207 507 371  HOH   HOH A . 
F 5 HOH   208 508 313  HOH   HOH A . 
F 5 HOH   209 509 1284 HOH   HOH A . 
F 5 HOH   210 510 185  HOH   HOH A . 
F 5 HOH   211 511 429  HOH   HOH A . 
F 5 HOH   212 512 70   HOH   HOH A . 
F 5 HOH   213 513 376  HOH   HOH A . 
F 5 HOH   214 514 1074 HOH   HOH A . 
F 5 HOH   215 515 772  HOH   HOH A . 
F 5 HOH   216 516 346  HOH   HOH A . 
F 5 HOH   217 517 1292 HOH   HOH A . 
F 5 HOH   218 518 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 531  HOH   HOH B . 
G 5 HOH   3   203 549  HOH   HOH B . 
G 5 HOH   4   204 364  HOH   HOH B . 
G 5 HOH   5   205 358  HOH   HOH B . 
G 5 HOH   6   206 1249 HOH   HOH B . 
G 5 HOH   7   207 758  HOH   HOH B . 
G 5 HOH   8   208 240  HOH   HOH B . 
G 5 HOH   9   209 398  HOH   HOH B . 
G 5 HOH   10  210 452  HOH   HOH B . 
G 5 HOH   11  211 120  HOH   HOH B . 
G 5 HOH   12  212 900  HOH   HOH B . 
G 5 HOH   13  213 743  HOH   HOH B . 
G 5 HOH   14  214 353  HOH   HOH B . 
G 5 HOH   15  215 50   HOH   HOH B . 
G 5 HOH   16  216 232  HOH   HOH B . 
G 5 HOH   17  217 654  HOH   HOH B . 
G 5 HOH   18  218 264  HOH   HOH B . 
G 5 HOH   19  219 444  HOH   HOH B . 
G 5 HOH   20  220 343  HOH   HOH B . 
G 5 HOH   21  221 1278 HOH   HOH B . 
G 5 HOH   22  222 131  HOH   HOH B . 
G 5 HOH   23  223 205  HOH   HOH B . 
G 5 HOH   24  224 332  HOH   HOH B . 
G 5 HOH   25  225 1140 HOH   HOH B . 
G 5 HOH   26  226 75   HOH   HOH B . 
G 5 HOH   27  227 82   HOH   HOH B . 
G 5 HOH   28  228 54   HOH   HOH B . 
G 5 HOH   29  229 282  HOH   HOH B . 
G 5 HOH   30  230 166  HOH   HOH B . 
G 5 HOH   31  231 1312 HOH   HOH B . 
G 5 HOH   32  232 276  HOH   HOH B . 
G 5 HOH   33  233 60   HOH   HOH B . 
G 5 HOH   34  234 69   HOH   HOH B . 
G 5 HOH   35  235 272  HOH   HOH B . 
G 5 HOH   36  236 110  HOH   HOH B . 
G 5 HOH   37  237 172  HOH   HOH B . 
G 5 HOH   38  238 128  HOH   HOH B . 
G 5 HOH   39  239 133  HOH   HOH B . 
G 5 HOH   40  240 723  HOH   HOH B . 
G 5 HOH   41  241 300  HOH   HOH B . 
G 5 HOH   42  242 127  HOH   HOH B . 
G 5 HOH   43  243 252  HOH   HOH B . 
G 5 HOH   44  244 1    HOH   HOH B . 
G 5 HOH   45  245 181  HOH   HOH B . 
G 5 HOH   46  246 14   HOH   HOH B . 
G 5 HOH   47  247 30   HOH   HOH B . 
G 5 HOH   48  248 143  HOH   HOH B . 
G 5 HOH   49  249 144  HOH   HOH B . 
G 5 HOH   50  250 9    HOH   HOH B . 
G 5 HOH   51  251 325  HOH   HOH B . 
G 5 HOH   52  252 31   HOH   HOH B . 
G 5 HOH   53  253 52   HOH   HOH B . 
G 5 HOH   54  254 41   HOH   HOH B . 
G 5 HOH   55  255 129  HOH   HOH B . 
G 5 HOH   56  256 231  HOH   HOH B . 
G 5 HOH   57  257 391  HOH   HOH B . 
G 5 HOH   58  258 72   HOH   HOH B . 
G 5 HOH   59  259 1277 HOH   HOH B . 
G 5 HOH   60  260 47   HOH   HOH B . 
G 5 HOH   61  261 10   HOH   HOH B . 
G 5 HOH   62  262 271  HOH   HOH B . 
G 5 HOH   63  263 59   HOH   HOH B . 
G 5 HOH   64  264 347  HOH   HOH B . 
G 5 HOH   65  265 243  HOH   HOH B . 
G 5 HOH   66  266 150  HOH   HOH B . 
G 5 HOH   67  267 61   HOH   HOH B . 
G 5 HOH   68  268 103  HOH   HOH B . 
G 5 HOH   69  269 175  HOH   HOH B . 
G 5 HOH   70  270 117  HOH   HOH B . 
G 5 HOH   71  271 11   HOH   HOH B . 
G 5 HOH   72  272 242  HOH   HOH B . 
G 5 HOH   73  273 20   HOH   HOH B . 
G 5 HOH   74  274 147  HOH   HOH B . 
G 5 HOH   75  275 77   HOH   HOH B . 
G 5 HOH   76  276 84   HOH   HOH B . 
G 5 HOH   77  277 302  HOH   HOH B . 
G 5 HOH   78  278 43   HOH   HOH B . 
G 5 HOH   79  279 114  HOH   HOH B . 
G 5 HOH   80  280 1106 HOH   HOH B . 
G 5 HOH   81  281 1305 HOH   HOH B . 
G 5 HOH   82  282 22   HOH   HOH B . 
G 5 HOH   83  283 287  HOH   HOH B . 
G 5 HOH   84  284 216  HOH   HOH B . 
G 5 HOH   85  285 235  HOH   HOH B . 
G 5 HOH   86  286 416  HOH   HOH B . 
G 5 HOH   87  287 387  HOH   HOH B . 
G 5 HOH   88  288 99   HOH   HOH B . 
G 5 HOH   89  289 88   HOH   HOH B . 
G 5 HOH   90  290 220  HOH   HOH B . 
G 5 HOH   91  291 1066 HOH   HOH B . 
G 5 HOH   92  292 106  HOH   HOH B . 
G 5 HOH   93  293 221  HOH   HOH B . 
G 5 HOH   94  294 13   HOH   HOH B . 
G 5 HOH   95  295 141  HOH   HOH B . 
G 5 HOH   96  296 89   HOH   HOH B . 
G 5 HOH   97  297 137  HOH   HOH B . 
G 5 HOH   98  298 160  HOH   HOH B . 
G 5 HOH   99  299 142  HOH   HOH B . 
G 5 HOH   100 300 299  HOH   HOH B . 
G 5 HOH   101 301 112  HOH   HOH B . 
G 5 HOH   102 302 635  HOH   HOH B . 
G 5 HOH   103 303 32   HOH   HOH B . 
G 5 HOH   104 304 311  HOH   HOH B . 
G 5 HOH   105 305 170  HOH   HOH B . 
G 5 HOH   106 306 316  HOH   HOH B . 
G 5 HOH   107 307 1274 HOH   HOH B . 
G 5 HOH   108 308 101  HOH   HOH B . 
G 5 HOH   109 309 297  HOH   HOH B . 
G 5 HOH   110 310 215  HOH   HOH B . 
G 5 HOH   111 311 118  HOH   HOH B . 
G 5 HOH   112 312 38   HOH   HOH B . 
G 5 HOH   113 313 48   HOH   HOH B . 
G 5 HOH   114 314 161  HOH   HOH B . 
G 5 HOH   115 315 37   HOH   HOH B . 
G 5 HOH   116 316 1285 HOH   HOH B . 
G 5 HOH   117 317 1291 HOH   HOH B . 
G 5 HOH   118 318 341  HOH   HOH B . 
G 5 HOH   119 319 44   HOH   HOH B . 
G 5 HOH   120 320 177  HOH   HOH B . 
G 5 HOH   121 321 704  HOH   HOH B . 
G 5 HOH   122 322 23   HOH   HOH B . 
G 5 HOH   123 323 28   HOH   HOH B . 
G 5 HOH   124 324 91   HOH   HOH B . 
G 5 HOH   125 325 197  HOH   HOH B . 
G 5 HOH   126 326 1126 HOH   HOH B . 
G 5 HOH   127 327 334  HOH   HOH B . 
G 5 HOH   128 328 100  HOH   HOH B . 
G 5 HOH   129 329 1294 HOH   HOH B . 
G 5 HOH   130 330 182  HOH   HOH B . 
G 5 HOH   131 331 29   HOH   HOH B . 
G 5 HOH   132 332 55   HOH   HOH B . 
G 5 HOH   133 333 717  HOH   HOH B . 
G 5 HOH   134 334 98   HOH   HOH B . 
G 5 HOH   135 335 234  HOH   HOH B . 
G 5 HOH   136 336 65   HOH   HOH B . 
G 5 HOH   137 337 207  HOH   HOH B . 
G 5 HOH   138 338 445  HOH   HOH B . 
G 5 HOH   139 339 1293 HOH   HOH B . 
G 5 HOH   140 340 619  HOH   HOH B . 
G 5 HOH   141 341 339  HOH   HOH B . 
G 5 HOH   142 342 178  HOH   HOH B . 
G 5 HOH   143 343 362  HOH   HOH B . 
G 5 HOH   144 344 90   HOH   HOH B . 
G 5 HOH   145 345 960  HOH   HOH B . 
G 5 HOH   146 346 1304 HOH   HOH B . 
G 5 HOH   147 347 463  HOH   HOH B . 
G 5 HOH   148 348 623  HOH   HOH B . 
G 5 HOH   149 349 191  HOH   HOH B . 
G 5 HOH   150 350 1046 HOH   HOH B . 
G 5 HOH   151 351 335  HOH   HOH B . 
G 5 HOH   152 352 304  HOH   HOH B . 
G 5 HOH   153 353 87   HOH   HOH B . 
G 5 HOH   154 354 1280 HOH   HOH B . 
G 5 HOH   155 355 203  HOH   HOH B . 
G 5 HOH   156 356 290  HOH   HOH B . 
G 5 HOH   157 357 541  HOH   HOH B . 
G 5 HOH   158 358 479  HOH   HOH B . 
G 5 HOH   159 359 389  HOH   HOH B . 
G 5 HOH   160 360 1077 HOH   HOH B . 
G 5 HOH   161 361 283  HOH   HOH B . 
G 5 HOH   162 362 1072 HOH   HOH B . 
G 5 HOH   163 363 718  HOH   HOH B . 
G 5 HOH   164 364 1316 HOH   HOH B . 
G 5 HOH   165 365 615  HOH   HOH B . 
G 5 HOH   166 366 898  HOH   HOH B . 
G 5 HOH   167 367 340  HOH   HOH B . 
G 5 HOH   168 368 291  HOH   HOH B . 
G 5 HOH   169 369 373  HOH   HOH B . 
G 5 HOH   170 370 667  HOH   HOH B . 
G 5 HOH   171 371 190  HOH   HOH B . 
G 5 HOH   172 372 1303 HOH   HOH B . 
G 5 HOH   173 373 431  HOH   HOH B . 
G 5 HOH   174 374 310  HOH   HOH B . 
G 5 HOH   175 375 149  HOH   HOH B . 
G 5 HOH   176 376 1163 HOH   HOH B . 
G 5 HOH   177 377 183  HOH   HOH B . 
G 5 HOH   178 378 418  HOH   HOH B . 
G 5 HOH   179 379 1000 HOH   HOH B . 
G 5 HOH   180 380 1173 HOH   HOH B . 
G 5 HOH   181 381 176  HOH   HOH B . 
G 5 HOH   182 382 1311 HOH   HOH B . 
G 5 HOH   183 383 424  HOH   HOH B . 
G 5 HOH   184 384 491  HOH   HOH B . 
G 5 HOH   185 385 981  HOH   HOH B . 
G 5 HOH   186 386 1298 HOH   HOH B . 
G 5 HOH   187 387 248  HOH   HOH B . 
G 5 HOH   188 388 470  HOH   HOH B . 
G 5 HOH   189 389 265  HOH   HOH B . 
G 5 HOH   190 390 184  HOH   HOH B . 
G 5 HOH   191 391 360  HOH   HOH B . 
G 5 HOH   192 392 355  HOH   HOH B . 
G 5 HOH   193 393 410  HOH   HOH B . 
G 5 HOH   194 394 274  HOH   HOH B . 
G 5 HOH   195 395 566  HOH   HOH B . 
G 5 HOH   196 396 314  HOH   HOH B . 
G 5 HOH   197 397 157  HOH   HOH B . 
G 5 HOH   198 398 792  HOH   HOH B . 
G 5 HOH   199 399 321  HOH   HOH B . 
G 5 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HE3 
_cell.length_a           88.819 
_cell.length_b           88.819 
_cell.length_c           39.535 
_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                         7HE3 
_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          7HE3 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.74 
_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   2023-05-20 
_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                     7HE3 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.410 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165192 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            0.051 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.200 
_reflns.B_iso_Wilson_estimate        12.270 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.056 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1043406 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 33502 7318 ? 2.362 ? ? ? 4.600 ? 0.500  ? ? ? ? ? ? 89.200 2.665 1.200 0.275 
1 2 5.480 44.410 ? 7426  1094 ? 0.029 ? ? ? 6.800 ? 50.500 ? ? ? ? ? ? 99.800 0.031 0.012 0.999 
# 
_refine.entry_id                                 7HE3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.4100 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.1200 
_refine.ls_number_reflns_obs                     164595 
_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                          0.1498 
_refine.ls_R_factor_R_work                       0.1491 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1623 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7927 
_refine.ls_number_reflns_R_work                  156668 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.4033 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1300 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                67.550 
_refine.B_iso_min                                9.190 
_refine.pdbx_overall_phase_error                 18.9100 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.4100 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.number_atoms_solvent             418 
_refine_hist.number_atoms_total               3004 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           15.75 
_refine_hist.pdbx_B_iso_mean_solvent          30.49 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 80.0000  4228 . 0.4623 0.3921 . 220 0.0000 4448 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 96.0000  5032 . 0.4094 0.4480 . 218 0.0000 5250 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5270 . 0.3557 0.3495 . 252 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5160 . 0.3120 0.3147 . 278 0.0000 5438 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5195 . 0.2754 0.3027 . 327 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5265 . 0.2601 0.2694 . 249 0.0000 5514 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5265 . 0.2484 0.2762 . 263 0.0000 5528 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5224 . 0.2210 0.2494 . 249 0.0000 5473 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5219 . 0.2018 0.2235 . 275 0.0000 5494 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5274 . 0.1819 0.2126 . 243 0.0000 5517 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5277 . 0.1667 0.1908 . 262 0.0000 5539 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 5264 . 0.1489 0.1710 . 270 0.0000 5534 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5169 . 0.1344 0.1647 . 287 0.0000 5456 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5332 . 0.1277 0.1518 . 237 0.0000 5569 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5188 . 0.1311 0.1439 . 258 0.0000 5446 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5265 . 0.1293 0.1565 . 276 0.0000 5541 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5241 . 0.1338 0.1474 . 284 0.0000 5525 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5228 . 0.1379 0.1498 . 275 0.0000 5503 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5296 . 0.1367 0.1723 . 248 0.0000 5544 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5228 . 0.1287 0.1646 . 264 0.0000 5492 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5315 . 0.1211 0.1265 . 253 0.0000 5568 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5203 . 0.1172 0.1311 . 278 0.0000 5481 . 'X-RAY DIFFRACTION' 
1.5500 1.6300  30 100.0000 5309 . 0.1179 0.1354 . 259 0.0000 5568 . 'X-RAY DIFFRACTION' 
1.6300 1.7100  30 100.0000 5296 . 0.1255 0.1423 . 272 0.0000 5568 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5270 . 0.1346 0.1516 . 250 0.0000 5520 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5277 . 0.1323 0.1407 . 281 0.0000 5558 . 'X-RAY DIFFRACTION' 
1.9600 2.1600  30 100.0000 5298 . 0.1383 0.1393 . 282 0.0000 5580 . 'X-RAY DIFFRACTION' 
2.1600 2.4700  30 100.0000 5285 . 0.1379 0.1422 . 293 0.0000 5578 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5321 . 0.1526 0.1611 . 256 0.0000 5577 . 'X-RAY DIFFRACTION' 
3.1100 44.4100 30 100.0000 5474 . 0.1510 0.1700 . 268 0.0000 5742 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HE3 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003657' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HE3 
_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 5 ? 
G N N 5 ? 
# 
_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 7HE3 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HE3 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 7HE3 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HE3 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HE3 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HE3 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N ALA A 124 ? N ALA A 124 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HE3 
_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_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.59 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.86 -133.17 
2 1 SER A 128 ? B 66.36 -0.51   
3 1 HIS B 86  ? ? 57.17 -128.07 
# 
_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 516 ? 5.91 . 
2 1 O ? A HOH 517 ? 5.92 . 
3 1 O ? A HOH 518 ? 7.63 . 
4 1 O ? B HOH 400 ? 6.24 . 
# 
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 
A1A9F N2   N  N N 1   
A1A9F C3   C  Y N 2   
A1A9F C6   C  N N 3   
A1A9F C9   C  Y N 4   
A1A9F C12  C  Y N 5   
A1A9F C1   C  N N 6   
A1A9F C10  C  Y N 7   
A1A9F C11  C  Y N 8   
A1A9F C13  C  Y N 9   
A1A9F C2   C  Y N 10  
A1A9F C4   C  N N 11  
A1A9F C5   C  N S 12  
A1A9F C7   C  Y N 13  
A1A9F C8   C  Y N 14  
A1A9F N1   N  Y N 15  
A1A9F N3   N  Y N 16  
A1A9F N4   N  Y N 17  
A1A9F N5   N  Y N 18  
A1A9F N6   N  Y N 19  
A1A9F O1   O  N N 20  
A1A9F H11  H  N N 21  
A1A9F H9   H  N N 22  
A1A9F H8   H  N N 23  
A1A9F H14  H  N N 24  
A1A9F H4   H  N N 25  
A1A9F H3   H  N N 26  
A1A9F H2   H  N N 27  
A1A9F H13  H  N N 28  
A1A9F H16  H  N N 29  
A1A9F H5   H  N N 30  
A1A9F H6   H  N N 31  
A1A9F H7   H  N N 32  
A1A9F H1   H  N N 33  
A1A9F H12  H  N N 34  
A1A9F H15  H  N N 35  
A1A9F H10  H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CL    CL   CL N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
GLN   N    N  N N 125 
GLN   CA   C  N S 126 
GLN   C    C  N N 127 
GLN   O    O  N N 128 
GLN   CB   C  N N 129 
GLN   CG   C  N N 130 
GLN   CD   C  N N 131 
GLN   OE1  O  N N 132 
GLN   NE2  N  N N 133 
GLN   OXT  O  N N 134 
GLN   H    H  N N 135 
GLN   H2   H  N N 136 
GLN   HA   H  N N 137 
GLN   HB2  H  N N 138 
GLN   HB3  H  N N 139 
GLN   HG2  H  N N 140 
GLN   HG3  H  N N 141 
GLN   HE21 H  N N 142 
GLN   HE22 H  N N 143 
GLN   HXT  H  N N 144 
GLU   N    N  N N 145 
GLU   CA   C  N S 146 
GLU   C    C  N N 147 
GLU   O    O  N N 148 
GLU   CB   C  N N 149 
GLU   CG   C  N N 150 
GLU   CD   C  N N 151 
GLU   OE1  O  N N 152 
GLU   OE2  O  N N 153 
GLU   OXT  O  N N 154 
GLU   H    H  N N 155 
GLU   H2   H  N N 156 
GLU   HA   H  N N 157 
GLU   HB2  H  N N 158 
GLU   HB3  H  N N 159 
GLU   HG2  H  N N 160 
GLU   HG3  H  N N 161 
GLU   HE2  H  N N 162 
GLU   HXT  H  N N 163 
GLY   N    N  N N 164 
GLY   CA   C  N N 165 
GLY   C    C  N N 166 
GLY   O    O  N N 167 
GLY   OXT  O  N N 168 
GLY   H    H  N N 169 
GLY   H2   H  N N 170 
GLY   HA2  H  N N 171 
GLY   HA3  H  N N 172 
GLY   HXT  H  N N 173 
HIS   N    N  N N 174 
HIS   CA   C  N S 175 
HIS   C    C  N N 176 
HIS   O    O  N N 177 
HIS   CB   C  N N 178 
HIS   CG   C  Y N 179 
HIS   ND1  N  Y N 180 
HIS   CD2  C  Y N 181 
HIS   CE1  C  Y N 182 
HIS   NE2  N  Y N 183 
HIS   OXT  O  N N 184 
HIS   H    H  N N 185 
HIS   H2   H  N N 186 
HIS   HA   H  N N 187 
HIS   HB2  H  N N 188 
HIS   HB3  H  N N 189 
HIS   HD1  H  N N 190 
HIS   HD2  H  N N 191 
HIS   HE1  H  N N 192 
HIS   HE2  H  N N 193 
HIS   HXT  H  N N 194 
HOH   O    O  N N 195 
HOH   H1   H  N N 196 
HOH   H2   H  N N 197 
ILE   N    N  N N 198 
ILE   CA   C  N S 199 
ILE   C    C  N N 200 
ILE   O    O  N N 201 
ILE   CB   C  N S 202 
ILE   CG1  C  N N 203 
ILE   CG2  C  N N 204 
ILE   CD1  C  N N 205 
ILE   OXT  O  N N 206 
ILE   H    H  N N 207 
ILE   H2   H  N N 208 
ILE   HA   H  N N 209 
ILE   HB   H  N N 210 
ILE   HG12 H  N N 211 
ILE   HG13 H  N N 212 
ILE   HG21 H  N N 213 
ILE   HG22 H  N N 214 
ILE   HG23 H  N N 215 
ILE   HD11 H  N N 216 
ILE   HD12 H  N N 217 
ILE   HD13 H  N N 218 
ILE   HXT  H  N N 219 
LEU   N    N  N N 220 
LEU   CA   C  N S 221 
LEU   C    C  N N 222 
LEU   O    O  N N 223 
LEU   CB   C  N N 224 
LEU   CG   C  N N 225 
LEU   CD1  C  N N 226 
LEU   CD2  C  N N 227 
LEU   OXT  O  N N 228 
LEU   H    H  N N 229 
LEU   H2   H  N N 230 
LEU   HA   H  N N 231 
LEU   HB2  H  N N 232 
LEU   HB3  H  N N 233 
LEU   HG   H  N N 234 
LEU   HD11 H  N N 235 
LEU   HD12 H  N N 236 
LEU   HD13 H  N N 237 
LEU   HD21 H  N N 238 
LEU   HD22 H  N N 239 
LEU   HD23 H  N N 240 
LEU   HXT  H  N N 241 
LYS   N    N  N N 242 
LYS   CA   C  N S 243 
LYS   C    C  N N 244 
LYS   O    O  N N 245 
LYS   CB   C  N N 246 
LYS   CG   C  N N 247 
LYS   CD   C  N N 248 
LYS   CE   C  N N 249 
LYS   NZ   N  N N 250 
LYS   OXT  O  N N 251 
LYS   H    H  N N 252 
LYS   H2   H  N N 253 
LYS   HA   H  N N 254 
LYS   HB2  H  N N 255 
LYS   HB3  H  N N 256 
LYS   HG2  H  N N 257 
LYS   HG3  H  N N 258 
LYS   HD2  H  N N 259 
LYS   HD3  H  N N 260 
LYS   HE2  H  N N 261 
LYS   HE3  H  N N 262 
LYS   HZ1  H  N N 263 
LYS   HZ2  H  N N 264 
LYS   HZ3  H  N N 265 
LYS   HXT  H  N N 266 
MET   N    N  N N 267 
MET   CA   C  N S 268 
MET   C    C  N N 269 
MET   O    O  N N 270 
MET   CB   C  N N 271 
MET   CG   C  N N 272 
MET   SD   S  N N 273 
MET   CE   C  N N 274 
MET   OXT  O  N N 275 
MET   H    H  N N 276 
MET   H2   H  N N 277 
MET   HA   H  N N 278 
MET   HB2  H  N N 279 
MET   HB3  H  N N 280 
MET   HG2  H  N N 281 
MET   HG3  H  N N 282 
MET   HE1  H  N N 283 
MET   HE2  H  N N 284 
MET   HE3  H  N N 285 
MET   HXT  H  N N 286 
PHE   N    N  N N 287 
PHE   CA   C  N S 288 
PHE   C    C  N N 289 
PHE   O    O  N N 290 
PHE   CB   C  N N 291 
PHE   CG   C  Y N 292 
PHE   CD1  C  Y N 293 
PHE   CD2  C  Y N 294 
PHE   CE1  C  Y N 295 
PHE   CE2  C  Y N 296 
PHE   CZ   C  Y N 297 
PHE   OXT  O  N N 298 
PHE   H    H  N N 299 
PHE   H2   H  N N 300 
PHE   HA   H  N N 301 
PHE   HB2  H  N N 302 
PHE   HB3  H  N N 303 
PHE   HD1  H  N N 304 
PHE   HD2  H  N N 305 
PHE   HE1  H  N N 306 
PHE   HE2  H  N N 307 
PHE   HZ   H  N N 308 
PHE   HXT  H  N N 309 
PRO   N    N  N N 310 
PRO   CA   C  N S 311 
PRO   C    C  N N 312 
PRO   O    O  N N 313 
PRO   CB   C  N N 314 
PRO   CG   C  N N 315 
PRO   CD   C  N N 316 
PRO   OXT  O  N N 317 
PRO   H    H  N N 318 
PRO   HA   H  N N 319 
PRO   HB2  H  N N 320 
PRO   HB3  H  N N 321 
PRO   HG2  H  N N 322 
PRO   HG3  H  N N 323 
PRO   HD2  H  N N 324 
PRO   HD3  H  N N 325 
PRO   HXT  H  N N 326 
SER   N    N  N N 327 
SER   CA   C  N S 328 
SER   C    C  N N 329 
SER   O    O  N N 330 
SER   CB   C  N N 331 
SER   OG   O  N N 332 
SER   OXT  O  N N 333 
SER   H    H  N N 334 
SER   H2   H  N N 335 
SER   HA   H  N N 336 
SER   HB2  H  N N 337 
SER   HB3  H  N N 338 
SER   HG   H  N N 339 
SER   HXT  H  N N 340 
TFA   C1   C  N N 341 
TFA   C2   C  N N 342 
TFA   O    O  N N 343 
TFA   F1   F  N N 344 
TFA   F2   F  N N 345 
TFA   F3   F  N N 346 
TFA   OXT  O  N N 347 
TFA   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TYR   N    N  N N 366 
TYR   CA   C  N S 367 
TYR   C    C  N N 368 
TYR   O    O  N N 369 
TYR   CB   C  N N 370 
TYR   CG   C  Y N 371 
TYR   CD1  C  Y N 372 
TYR   CD2  C  Y N 373 
TYR   CE1  C  Y N 374 
TYR   CE2  C  Y N 375 
TYR   CZ   C  Y N 376 
TYR   OH   O  N N 377 
TYR   OXT  O  N N 378 
TYR   H    H  N N 379 
TYR   H2   H  N N 380 
TYR   HA   H  N N 381 
TYR   HB2  H  N N 382 
TYR   HB3  H  N N 383 
TYR   HD1  H  N N 384 
TYR   HD2  H  N N 385 
TYR   HE1  H  N N 386 
TYR   HE2  H  N N 387 
TYR   HH   H  N N 388 
TYR   HXT  H  N N 389 
VAL   N    N  N N 390 
VAL   CA   C  N S 391 
VAL   C    C  N N 392 
VAL   O    O  N N 393 
VAL   CB   C  N N 394 
VAL   CG1  C  N N 395 
VAL   CG2  C  N N 396 
VAL   OXT  O  N N 397 
VAL   H    H  N N 398 
VAL   H2   H  N N 399 
VAL   HA   H  N N 400 
VAL   HB   H  N N 401 
VAL   HG11 H  N N 402 
VAL   HG12 H  N N 403 
VAL   HG13 H  N N 404 
VAL   HG21 H  N N 405 
VAL   HG22 H  N N 406 
VAL   HG23 H  N N 407 
VAL   HXT  H  N N 408 
# 
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 
A1A9F C1  N1   sing N N 1   
A1A9F C2  N1   sing Y N 2   
A1A9F C2  C3   doub Y N 3   
A1A9F N1  N6   sing Y N 4   
A1A9F C3  C4   sing N N 5   
A1A9F C3  C13  sing Y N 6   
A1A9F C4  C5   sing N N 7   
A1A9F N6  C13  doub Y N 8   
A1A9F O1  C6   sing N N 9   
A1A9F C6  C5   sing N N 10  
A1A9F C5  N2   sing N N 11  
A1A9F N2  C7   sing N N 12  
A1A9F C7  C10  doub Y N 13  
A1A9F C7  N3   sing Y N 14  
A1A9F C11 C10  sing Y N 15  
A1A9F C11 C12  doub Y N 16  
A1A9F C10 C9   sing Y N 17  
A1A9F N3  C8   doub Y N 18  
A1A9F C12 N5   sing Y N 19  
A1A9F C8  N4   sing Y N 20  
A1A9F C9  N5   sing Y N 21  
A1A9F C9  N4   doub Y N 22  
A1A9F N2  H11  sing N N 23  
A1A9F C6  H9   sing N N 24  
A1A9F C6  H8   sing N N 25  
A1A9F C12 H14  sing N N 26  
A1A9F C1  H4   sing N N 27  
A1A9F C1  H3   sing N N 28  
A1A9F C1  H2   sing N N 29  
A1A9F C11 H13  sing N N 30  
A1A9F C13 H16  sing N N 31  
A1A9F C2  H5   sing N N 32  
A1A9F C4  H6   sing N N 33  
A1A9F C4  H7   sing N N 34  
A1A9F C5  H1   sing N N 35  
A1A9F C8  H12  sing N N 36  
A1A9F N5  H15  sing N N 37  
A1A9F O1  H10  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
HOH   O   H1   sing N N 188 
HOH   O   H2   sing N N 189 
ILE   N   CA   sing N N 190 
ILE   N   H    sing N N 191 
ILE   N   H2   sing N N 192 
ILE   CA  C    sing N N 193 
ILE   CA  CB   sing N N 194 
ILE   CA  HA   sing N N 195 
ILE   C   O    doub N N 196 
ILE   C   OXT  sing N N 197 
ILE   CB  CG1  sing N N 198 
ILE   CB  CG2  sing N N 199 
ILE   CB  HB   sing N N 200 
ILE   CG1 CD1  sing N N 201 
ILE   CG1 HG12 sing N N 202 
ILE   CG1 HG13 sing N N 203 
ILE   CG2 HG21 sing N N 204 
ILE   CG2 HG22 sing N N 205 
ILE   CG2 HG23 sing N N 206 
ILE   CD1 HD11 sing N N 207 
ILE   CD1 HD12 sing N N 208 
ILE   CD1 HD13 sing N N 209 
ILE   OXT HXT  sing N N 210 
LEU   N   CA   sing N N 211 
LEU   N   H    sing N N 212 
LEU   N   H2   sing N N 213 
LEU   CA  C    sing N N 214 
LEU   CA  CB   sing N N 215 
LEU   CA  HA   sing N N 216 
LEU   C   O    doub N N 217 
LEU   C   OXT  sing N N 218 
LEU   CB  CG   sing N N 219 
LEU   CB  HB2  sing N N 220 
LEU   CB  HB3  sing N N 221 
LEU   CG  CD1  sing N N 222 
LEU   CG  CD2  sing N N 223 
LEU   CG  HG   sing N N 224 
LEU   CD1 HD11 sing N N 225 
LEU   CD1 HD12 sing N N 226 
LEU   CD1 HD13 sing N N 227 
LEU   CD2 HD21 sing N N 228 
LEU   CD2 HD22 sing N N 229 
LEU   CD2 HD23 sing N N 230 
LEU   OXT HXT  sing N N 231 
LYS   N   CA   sing N N 232 
LYS   N   H    sing N N 233 
LYS   N   H2   sing N N 234 
LYS   CA  C    sing N N 235 
LYS   CA  CB   sing N N 236 
LYS   CA  HA   sing N N 237 
LYS   C   O    doub N N 238 
LYS   C   OXT  sing N N 239 
LYS   CB  CG   sing N N 240 
LYS   CB  HB2  sing N N 241 
LYS   CB  HB3  sing N N 242 
LYS   CG  CD   sing N N 243 
LYS   CG  HG2  sing N N 244 
LYS   CG  HG3  sing N N 245 
LYS   CD  CE   sing N N 246 
LYS   CD  HD2  sing N N 247 
LYS   CD  HD3  sing N N 248 
LYS   CE  NZ   sing N N 249 
LYS   CE  HE2  sing N N 250 
LYS   CE  HE3  sing N N 251 
LYS   NZ  HZ1  sing N N 252 
LYS   NZ  HZ2  sing N N 253 
LYS   NZ  HZ3  sing N N 254 
LYS   OXT HXT  sing N N 255 
MET   N   CA   sing N N 256 
MET   N   H    sing N N 257 
MET   N   H2   sing N N 258 
MET   CA  C    sing N N 259 
MET   CA  CB   sing N N 260 
MET   CA  HA   sing N N 261 
MET   C   O    doub N N 262 
MET   C   OXT  sing N N 263 
MET   CB  CG   sing N N 264 
MET   CB  HB2  sing N N 265 
MET   CB  HB3  sing N N 266 
MET   CG  SD   sing N N 267 
MET   CG  HG2  sing N N 268 
MET   CG  HG3  sing N N 269 
MET   SD  CE   sing N N 270 
MET   CE  HE1  sing N N 271 
MET   CE  HE2  sing N N 272 
MET   CE  HE3  sing N N 273 
MET   OXT HXT  sing N N 274 
PHE   N   CA   sing N N 275 
PHE   N   H    sing N N 276 
PHE   N   H2   sing N N 277 
PHE   CA  C    sing N N 278 
PHE   CA  CB   sing N N 279 
PHE   CA  HA   sing N N 280 
PHE   C   O    doub N N 281 
PHE   C   OXT  sing N N 282 
PHE   CB  CG   sing N N 283 
PHE   CB  HB2  sing N N 284 
PHE   CB  HB3  sing N N 285 
PHE   CG  CD1  doub Y N 286 
PHE   CG  CD2  sing Y N 287 
PHE   CD1 CE1  sing Y N 288 
PHE   CD1 HD1  sing N N 289 
PHE   CD2 CE2  doub Y N 290 
PHE   CD2 HD2  sing N N 291 
PHE   CE1 CZ   doub Y N 292 
PHE   CE1 HE1  sing N N 293 
PHE   CE2 CZ   sing Y N 294 
PHE   CE2 HE2  sing N N 295 
PHE   CZ  HZ   sing N N 296 
PHE   OXT HXT  sing N N 297 
PRO   N   CA   sing N N 298 
PRO   N   CD   sing N N 299 
PRO   N   H    sing N N 300 
PRO   CA  C    sing N N 301 
PRO   CA  CB   sing N N 302 
PRO   CA  HA   sing N N 303 
PRO   C   O    doub N N 304 
PRO   C   OXT  sing N N 305 
PRO   CB  CG   sing N N 306 
PRO   CB  HB2  sing N N 307 
PRO   CB  HB3  sing N N 308 
PRO   CG  CD   sing N N 309 
PRO   CG  HG2  sing N N 310 
PRO   CG  HG3  sing N N 311 
PRO   CD  HD2  sing N N 312 
PRO   CD  HD3  sing N N 313 
PRO   OXT HXT  sing N N 314 
SER   N   CA   sing N N 315 
SER   N   H    sing N N 316 
SER   N   H2   sing N N 317 
SER   CA  C    sing N N 318 
SER   CA  CB   sing N N 319 
SER   CA  HA   sing N N 320 
SER   C   O    doub N N 321 
SER   C   OXT  sing N N 322 
SER   CB  OG   sing N N 323 
SER   CB  HB2  sing N N 324 
SER   CB  HB3  sing N N 325 
SER   OG  HG   sing N N 326 
SER   OXT HXT  sing N N 327 
TFA   C1  C2   sing N N 328 
TFA   C1  O    doub N N 329 
TFA   C1  OXT  sing N N 330 
TFA   C2  F1   sing N N 331 
TFA   C2  F2   sing N N 332 
TFA   C2  F3   sing N N 333 
TFA   OXT HXT  sing N N 334 
THR   N   CA   sing N N 335 
THR   N   H    sing N N 336 
THR   N   H2   sing N N 337 
THR   CA  C    sing N N 338 
THR   CA  CB   sing N N 339 
THR   CA  HA   sing N N 340 
THR   C   O    doub N N 341 
THR   C   OXT  sing N N 342 
THR   CB  OG1  sing N N 343 
THR   CB  CG2  sing N N 344 
THR   CB  HB   sing N N 345 
THR   OG1 HG1  sing N N 346 
THR   CG2 HG21 sing N N 347 
THR   CG2 HG22 sing N N 348 
THR   CG2 HG23 sing N N 349 
THR   OXT HXT  sing N N 350 
TYR   N   CA   sing N N 351 
TYR   N   H    sing N N 352 
TYR   N   H2   sing N N 353 
TYR   CA  C    sing N N 354 
TYR   CA  CB   sing N N 355 
TYR   CA  HA   sing N N 356 
TYR   C   O    doub N N 357 
TYR   C   OXT  sing N N 358 
TYR   CB  CG   sing N N 359 
TYR   CB  HB2  sing N N 360 
TYR   CB  HB3  sing N N 361 
TYR   CG  CD1  doub Y N 362 
TYR   CG  CD2  sing Y N 363 
TYR   CD1 CE1  sing Y N 364 
TYR   CD1 HD1  sing N N 365 
TYR   CD2 CE2  doub Y N 366 
TYR   CD2 HD2  sing N N 367 
TYR   CE1 CZ   doub Y N 368 
TYR   CE1 HE1  sing N N 369 
TYR   CE2 CZ   sing Y N 370 
TYR   CE2 HE2  sing N N 371 
TYR   CZ  OH   sing N N 372 
TYR   OH  HH   sing N N 373 
TYR   OXT HXT  sing N N 374 
VAL   N   CA   sing N N 375 
VAL   N   H    sing N N 376 
VAL   N   H2   sing N N 377 
VAL   CA  C    sing N N 378 
VAL   CA  CB   sing N N 379 
VAL   CA  HA   sing N N 380 
VAL   C   O    doub N N 381 
VAL   C   OXT  sing N N 382 
VAL   CB  CG1  sing N N 383 
VAL   CB  CG2  sing N N 384 
VAL   CB  HB   sing N N 385 
VAL   CG1 HG11 sing N N 386 
VAL   CG1 HG12 sing N N 387 
VAL   CG1 HG13 sing N N 388 
VAL   CG2 HG21 sing N N 389 
VAL   CG2 HG22 sing N N 390 
VAL   CG2 HG23 sing N N 391 
VAL   OXT HXT  sing N N 392 
# 
_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                    7HE3 
_atom_sites.fract_transf_matrix[1][1]   0.011259 
_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]   0.011259 
_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]   0.025294 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
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   ? 19.659 -16.169 22.231  0.70 55.03 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.591 -16.135 22.342  0.30 54.29 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.681 -15.102 22.407  0.70 54.66 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.624 -15.056 22.500  0.30 54.02 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.320 -13.748 22.118  0.70 53.03 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.276 -13.713 22.192  0.30 52.67 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.439 -13.475 22.554  0.70 53.44 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.364 -13.416 22.686  0.30 53.06 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.054 -15.145 23.816  0.70 55.43 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.004 -15.062 23.911  0.30 54.63 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.030 -14.030 23.982  0.70 55.94 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 16.989 -13.937 24.052  0.30 55.10 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.413 -16.503 24.071  0.70 55.71 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.359 -16.409 24.205  0.30 54.88 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.965 -15.228 21.770  0.70 65.57 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.904 -15.186 21.866  0.30 64.80 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.750 -15.014 24.479  0.70 66.49 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.704 -14.917 24.567  0.30 65.54 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.528 -14.182 24.798  0.70 67.10 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.485 -14.069 24.870  0.30 66.10 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.493 -13.179 24.033  0.70 67.10 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.457 -13.088 24.087  0.30 66.10 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.430 -14.037 23.220  0.70 67.10 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.390 -13.956 23.289  0.30 66.10 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.964 -16.484 24.931  0.70 66.83 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.912 -16.364 25.065  0.30 65.83 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.771 -16.686 23.367  0.70 66.83 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.716 -16.609 23.507  0.30 65.83 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.104 -17.184 24.074  0.70 66.83 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.048 -17.092 24.226  0.30 65.83 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.608 -12.906 21.370  1.00 50.44 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.058 -11.556 21.047  1.00 45.39 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.924 -10.570 21.323  1.00 40.79 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.830 -10.952 21.752  1.00 40.91 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.608 -11.456 19.616  1.00 44.77 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.600 -11.864 18.567  1.00 44.13 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.473 -11.370 18.545  1.00 43.55 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.002 -12.776 17.687  1.00 43.80 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.841 -13.103 21.031  0.70 60.51 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.871 -13.125 20.981  0.30 60.51 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.786 -11.332 21.640  1.00 54.45 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.869 -10.536 19.443  1.00 53.71 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.380 -12.037 19.534  1.00 53.71 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.469 -13.041 17.068  1.00 52.54 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.799 -13.100 17.736  1.00 52.54 ?  4   ASN   A HD22 1 
ATOM   46   N  N    A SER   A 1 5   ? 18.195 -9.288  21.083  0.70 38.10 ?  5   SER   A N    1 
ATOM   47   N  N    B SER   A 1 5   ? 18.188 -9.291  21.056  0.30 38.55 ?  5   SER   A N    1 
ATOM   48   C  CA   A SER   A 1 5   ? 17.285 -8.212  21.454  0.70 35.48 ?  5   SER   A CA   1 
ATOM   49   C  CA   B SER   A 1 5   ? 17.308 -8.204  21.466  0.30 36.26 ?  5   SER   A CA   1 
ATOM   50   C  C    A SER   A 1 5   ? 16.410 -7.737  20.298  0.70 31.74 ?  5   SER   A C    1 
ATOM   51   C  C    B SER   A 1 5   ? 16.431 -7.671  20.337  0.30 33.07 ?  5   SER   A C    1 
ATOM   52   O  O    A SER   A 1 5   ? 15.726 -6.717  20.433  0.70 32.24 ?  5   SER   A O    1 
ATOM   53   O  O    B SER   A 1 5   ? 15.769 -6.645  20.519  0.30 33.37 ?  5   SER   A O    1 
ATOM   54   C  CB   A SER   A 1 5   ? 18.065 -7.035  22.044  0.70 36.19 ?  5   SER   A CB   1 
ATOM   55   C  CB   B SER   A 1 5   ? 18.127 -7.061  22.070  0.30 36.84 ?  5   SER   A CB   1 
ATOM   56   O  OG   A SER   A 1 5   ? 19.010 -6.533  21.117  0.70 36.69 ?  5   SER   A OG   1 
ATOM   57   O  OG   B SER   A 1 5   ? 18.993 -6.490  21.105  0.30 37.25 ?  5   SER   A OG   1 
ATOM   58   H  H    A SER   A 1 5   ? 18.913 -9.016  20.694  0.70 45.70 ?  5   SER   A H    1 
ATOM   59   H  H    B SER   A 1 5   ? 18.885 -9.028  20.626  0.30 46.24 ?  5   SER   A H    1 
ATOM   60   H  HA   A SER   A 1 5   ? 16.696 -8.539  22.149  0.70 42.56 ?  5   SER   A HA   1 
ATOM   61   H  HA   B SER   A 1 5   ? 16.720 -8.533  22.161  0.30 43.49 ?  5   SER   A HA   1 
ATOM   62   H  HB2  A SER   A 1 5   ? 17.443 -6.325  22.271  0.70 43.41 ?  5   SER   A HB2  1 
ATOM   63   H  HB2  B SER   A 1 5   ? 17.520 -6.377  22.396  0.30 44.19 ?  5   SER   A HB2  1 
ATOM   64   H  HB3  A SER   A 1 5   ? 18.530 -7.332  22.844  0.70 43.41 ?  5   SER   A HB3  1 
ATOM   65   H  HB3  B SER   A 1 5   ? 18.659 -7.407  22.804  0.30 44.19 ?  5   SER   A HB3  1 
ATOM   66   H  HG   A SER   A 1 5   ? 19.434 -5.891  21.459  0.70 44.01 ?  5   SER   A HG   1 
ATOM   67   H  HG   B SER   A 1 5   ? 19.433 -5.862  21.450  0.30 44.67 ?  5   SER   A HG   1 
ATOM   68   N  N    A PHE   A 1 6   ? 16.411 -8.444  19.171  0.70 27.45 ?  6   PHE   A N    1 
ATOM   69   N  N    B PHE   A 1 6   ? 16.408 -8.329  19.181  0.30 29.62 ?  6   PHE   A N    1 
ATOM   70   C  CA   A PHE   A 1 6   ? 15.516 -8.090  18.077  0.70 23.60 ?  6   PHE   A CA   1 
ATOM   71   C  CA   B PHE   A 1 6   ? 15.528 -7.900  18.100  0.30 26.27 ?  6   PHE   A CA   1 
ATOM   72   C  C    A PHE   A 1 6   ? 14.086 -8.486  18.426  0.70 22.97 ?  6   PHE   A C    1 
ATOM   73   C  C    B PHE   A 1 6   ? 14.075 -8.131  18.507  0.30 25.23 ?  6   PHE   A C    1 
ATOM   74   O  O    A PHE   A 1 6   ? 13.836 -9.590  18.915  0.70 24.27 ?  6   PHE   A O    1 
ATOM   75   O  O    B PHE   A 1 6   ? 13.687 -9.255  18.841  0.30 25.32 ?  6   PHE   A O    1 
ATOM   76   C  CB   A PHE   A 1 6   ? 15.952 -8.798  16.798  0.70 21.22 ?  6   PHE   A CB   1 
ATOM   77   C  CB   B PHE   A 1 6   ? 15.862 -8.657  16.817  0.30 24.25 ?  6   PHE   A CB   1 
ATOM   78   C  CG   A PHE   A 1 6   ? 17.226 -8.250  16.208  0.70 19.65 ?  6   PHE   A CG   1 
ATOM   79   C  CG   B PHE   A 1 6   ? 17.175 -8.252  16.198  0.30 22.64 ?  6   PHE   A CG   1 
ATOM   80   C  CD1  A PHE   A 1 6   ? 17.219 -7.056  15.507  0.70 19.16 ?  6   PHE   A CD1  1 
ATOM   81   C  CD1  B PHE   A 1 6   ? 17.282 -7.072  15.479  0.30 22.01 ?  6   PHE   A CD1  1 
ATOM   82   C  CD2  A PHE   A 1 6   ? 18.422 -8.931  16.349  0.70 20.33 ?  6   PHE   A CD2  1 
ATOM   83   C  CD2  B PHE   A 1 6   ? 18.298 -9.053  16.328  0.30 22.24 ?  6   PHE   A CD2  1 
ATOM   84   C  CE1  A PHE   A 1 6   ? 18.380 -6.547  14.960  0.70 19.26 ?  6   PHE   A CE1  1 
ATOM   85   C  CE1  B PHE   A 1 6   ? 18.484 -6.695  14.906  0.30 21.73 ?  6   PHE   A CE1  1 
ATOM   86   C  CE2  A PHE   A 1 6   ? 19.588 -8.428  15.803  0.70 20.66 ?  6   PHE   A CE2  1 
ATOM   87   C  CE2  B PHE   A 1 6   ? 19.504 -8.682  15.756  0.30 21.93 ?  6   PHE   A CE2  1 
ATOM   88   C  CZ   A PHE   A 1 6   ? 19.566 -7.234  15.107  0.70 19.66 ?  6   PHE   A CZ   1 
ATOM   89   C  CZ   B PHE   A 1 6   ? 19.596 -7.501  15.044  0.30 21.60 ?  6   PHE   A CZ   1 
ATOM   90   H  H    A PHE   A 1 6   ? 16.911 -9.127  19.021  0.70 32.92 ?  6   PHE   A H    1 
ATOM   91   H  H    B PHE   A 1 6   ? 16.889 -9.018  18.998  0.30 35.52 ?  6   PHE   A H    1 
ATOM   92   H  HA   A PHE   A 1 6   ? 15.541 -7.138  17.934  0.70 28.30 ?  6   PHE   A HA   1 
ATOM   93   H  HA   B PHE   A 1 6   ? 15.651 -6.954  17.940  0.30 31.51 ?  6   PHE   A HA   1 
ATOM   94   H  HB2  A PHE   A 1 6   ? 16.091 -9.741  16.995  0.70 25.44 ?  6   PHE   A HB2  1 
ATOM   95   H  HB2  B PHE   A 1 6   ? 15.908 -9.605  17.015  0.30 29.08 ?  6   PHE   A HB2  1 
ATOM   96   H  HB3  A PHE   A 1 6   ? 15.248 -8.705  16.137  0.70 25.44 ?  6   PHE   A HB3  1 
ATOM   97   H  HB3  B PHE   A 1 6   ? 15.164 -8.491  16.164  0.30 29.08 ?  6   PHE   A HB3  1 
ATOM   98   H  HD1  A PHE   A 1 6   ? 16.418 -6.593  15.408  0.70 22.97 ?  6   PHE   A HD1  1 
ATOM   99   H  HD1  B PHE   A 1 6   ? 16.538 -6.524  15.383  0.30 26.39 ?  6   PHE   A HD1  1 
ATOM   100  H  HD2  A PHE   A 1 6   ? 18.441 -9.738  16.820  0.70 24.38 ?  6   PHE   A HD2  1 
ATOM   101  H  HD2  B PHE   A 1 6   ? 18.243 -9.849  16.806  0.30 26.67 ?  6   PHE   A HD2  1 
ATOM   102  H  HE1  A PHE   A 1 6   ? 18.360 -5.744  14.494  0.70 23.10 ?  6   PHE   A HE1  1 
ATOM   103  H  HE1  B PHE   A 1 6   ? 18.544 -5.900  14.427  0.30 26.05 ?  6   PHE   A HE1  1 
ATOM   104  H  HE2  A PHE   A 1 6   ? 20.388 -8.891  15.906  0.70 24.78 ?  6   PHE   A HE2  1 
ATOM   105  H  HE2  B PHE   A 1 6   ? 20.253 -9.226  15.850  0.30 26.30 ?  6   PHE   A HE2  1 
ATOM   106  H  HZ   A PHE   A 1 6   ? 20.346 -6.891  14.742  0.70 23.58 ?  6   PHE   A HZ   1 
ATOM   107  H  HZ   B PHE   A 1 6   ? 20.405 -7.249  14.659  0.30 25.90 ?  6   PHE   A HZ   1 
ATOM   108  N  N    A SER   A 1 7   ? 13.138 -7.584  18.160  0.70 21.08 ?  7   SER   A N    1 
ATOM   109  N  N    B SER   A 1 7   ? 13.273 -7.069  18.475  0.30 24.32 ?  7   SER   A N    1 
ATOM   110  C  CA   A SER   A 1 7   ? 11.762 -7.733  18.625  0.70 20.68 ?  7   SER   A CA   1 
ATOM   111  C  CA   B SER   A 1 7   ? 11.938 -7.067  19.058  0.30 23.91 ?  7   SER   A CA   1 
ATOM   112  C  C    A SER   A 1 7   ? 10.767 -7.438  17.508  0.70 18.40 ?  7   SER   A C    1 
ATOM   113  C  C    B SER   A 1 7   ? 10.885 -7.027  17.960  0.30 22.70 ?  7   SER   A C    1 
ATOM   114  O  O    A SER   A 1 7   ? 10.989 -6.544  16.687  0.70 18.81 ?  7   SER   A O    1 
ATOM   115  O  O    B SER   A 1 7   ? 10.927 -6.157  17.084  0.30 22.83 ?  7   SER   A O    1 
ATOM   116  C  CB   A SER   A 1 7   ? 11.499 -6.781  19.801  0.70 22.91 ?  7   SER   A CB   1 
ATOM   117  C  CB   B SER   A 1 7   ? 11.766 -5.858  19.982  0.30 24.89 ?  7   SER   A CB   1 
ATOM   118  O  OG   A SER   A 1 7   ? 10.149 -6.842  20.218  0.70 24.66 ?  7   SER   A OG   1 
ATOM   119  O  OG   B SER   A 1 7   ? 10.616 -5.994  20.798  0.30 25.67 ?  7   SER   A OG   1 
ATOM   120  H  H    A SER   A 1 7   ? 13.270 -6.877  17.693  0.70 25.27 ?  7   SER   A H    1 
ATOM   121  H  H    B SER   A 1 7   ? 13.485 -6.320  18.108  0.30 29.17 ?  7   SER   A H    1 
ATOM   122  H  HA   A SER   A 1 7   ? 11.617 -8.643  18.929  0.70 24.79 ?  7   SER   A HA   1 
ATOM   123  H  HA   B SER   A 1 7   ? 11.807 -7.871  19.582  0.30 28.68 ?  7   SER   A HA   1 
ATOM   124  H  HB2  A SER   A 1 7   ? 12.068 -7.036  20.544  0.70 27.47 ?  7   SER   A HB2  1 
ATOM   125  H  HB2  B SER   A 1 7   ? 12.553 -5.777  20.546  0.30 29.85 ?  7   SER   A HB2  1 
ATOM   126  H  HB3  A SER   A 1 7   ? 11.701 -5.875  19.523  0.70 27.47 ?  7   SER   A HB3  1 
ATOM   127  H  HB3  B SER   A 1 7   ? 11.666 -5.057  19.443  0.30 29.85 ?  7   SER   A HB3  1 
ATOM   128  H  HG   A SER   A 1 7   ? 10.019 -6.318  20.860  0.70 29.57 ?  7   SER   A HG   1 
ATOM   129  H  HG   B SER   A 1 7   ? 10.547 -5.329  21.309  0.30 30.78 ?  7   SER   A HG   1 
ATOM   130  N  N    A GLY   A 1 8   ? 9.657  -8.183  17.492  0.70 16.89 ?  8   GLY   A N    1 
ATOM   131  N  N    B GLY   A 1 8   ? 9.947  -7.971  18.009  0.30 21.19 ?  8   GLY   A N    1 
ATOM   132  C  CA   A GLY   A 1 8   ? 8.579  -7.931  16.553  0.70 16.13 ?  8   GLY   A CA   1 
ATOM   133  C  CA   B GLY   A 1 8   ? 8.777  -7.915  17.157  0.30 19.71 ?  8   GLY   A CA   1 
ATOM   134  C  C    A GLY   A 1 8   ? 8.791  -8.454  15.150  0.70 14.83 ?  8   GLY   A C    1 
ATOM   135  C  C    B GLY   A 1 8   ? 8.971  -8.368  15.730  0.30 18.00 ?  8   GLY   A C    1 
ATOM   136  O  O    A GLY   A 1 8   ? 8.051  -8.058  14.243  0.70 15.42 ?  8   GLY   A O    1 
ATOM   137  O  O    B GLY   A 1 8   ? 8.173  -7.995  14.865  0.30 18.04 ?  8   GLY   A O    1 
ATOM   138  H  H    A GLY   A 1 8   ? 9.506  -8.840  18.026  0.70 20.24 ?  8   GLY   A H    1 
ATOM   139  H  H    B GLY   A 1 8   ? 9.972  -8.655  18.531  0.30 25.41 ?  8   GLY   A H    1 
ATOM   140  H  HA2  A GLY   A 1 8   ? 7.763  -8.325  16.902  0.70 19.34 ?  8   GLY   A HA2  1 
ATOM   141  H  HA2  B GLY   A 1 8   ? 8.083  -8.468  17.543  0.30 23.63 ?  8   GLY   A HA2  1 
ATOM   142  H  HA3  A GLY   A 1 8   ? 8.440  -6.972  16.490  0.70 19.34 ?  8   GLY   A HA3  1 
ATOM   143  H  HA3  B GLY   A 1 8   ? 8.453  -7.002  17.133  0.30 23.63 ?  8   GLY   A HA3  1 
ATOM   144  N  N    A TYR   A 1 9   ? 9.768  -9.333  14.935  0.70 14.03 ?  9   TYR   A N    1 
ATOM   145  N  N    B TYR   A 1 9   ? 10.000 -9.163  15.446  0.30 16.53 ?  9   TYR   A N    1 
ATOM   146  C  CA   A TYR   A 1 9   ? 10.045 -9.872  13.611  0.70 13.22 ?  9   TYR   A CA   1 
ATOM   147  C  CA   B TYR   A 1 9   ? 10.213 -9.648  14.089  0.30 15.12 ?  9   TYR   A CA   1 
ATOM   148  C  C    A TYR   A 1 9   ? 9.193  -11.100 13.332  0.70 12.69 ?  9   TYR   A C    1 
ATOM   149  C  C    B TYR   A 1 9   ? 9.353  -10.873 13.802  0.30 14.35 ?  9   TYR   A C    1 
ATOM   150  O  O    A TYR   A 1 9   ? 8.926  -11.912 14.222  0.70 14.16 ?  9   TYR   A O    1 
ATOM   151  O  O    B TYR   A 1 9   ? 9.154  -11.731 14.667  0.30 15.54 ?  9   TYR   A O    1 
ATOM   152  C  CB   A TYR   A 1 9   ? 11.524 -10.260 13.460  0.70 13.97 ?  9   TYR   A CB   1 
ATOM   153  C  CB   B TYR   A 1 9   ? 11.690 -9.983  13.864  0.30 15.19 ?  9   TYR   A CB   1 
ATOM   154  C  CG   A TYR   A 1 9   ? 12.455 -9.084  13.317  0.70 14.75 ?  9   TYR   A CG   1 
ATOM   155  C  CG   B TYR   A 1 9   ? 12.539 -8.757  13.613  0.30 14.89 ?  9   TYR   A CG   1 
ATOM   156  C  CD1  A TYR   A 1 9   ? 12.804 -8.325  14.422  0.70 15.42 ?  9   TYR   A CD1  1 
ATOM   157  C  CD1  B TYR   A 1 9   ? 12.789 -7.847  14.630  0.30 15.09 ?  9   TYR   A CD1  1 
ATOM   158  C  CD2  A TYR   A 1 9   ? 12.972 -8.728  12.078  0.70 14.74 ?  9   TYR   A CD2  1 
ATOM   159  C  CD2  B TYR   A 1 9   ? 13.071 -8.498  12.355  0.30 14.46 ?  9   TYR   A CD2  1 
ATOM   160  C  CE1  A TYR   A 1 9   ? 13.636 -7.238  14.302  0.70 16.02 ?  9   TYR   A CE1  1 
ATOM   161  C  CE1  B TYR   A 1 9   ? 13.547 -6.718  14.407  0.30 14.78 ?  9   TYR   A CE1  1 
ATOM   162  C  CE2  A TYR   A 1 9   ? 13.806 -7.643  11.948  0.70 15.49 ?  9   TYR   A CE2  1 
ATOM   163  C  CE2  B TYR   A 1 9   ? 13.834 -7.366  12.122  0.30 14.23 ?  9   TYR   A CE2  1 
ATOM   164  C  CZ   A TYR   A 1 9   ? 14.135 -6.904  13.062  0.70 16.18 ?  9   TYR   A CZ   1 
ATOM   165  C  CZ   B TYR   A 1 9   ? 14.068 -6.483  13.153  0.30 14.40 ?  9   TYR   A CZ   1 
ATOM   166  O  OH   A TYR   A 1 9   ? 14.965 -5.825  12.923  0.70 17.74 ?  9   TYR   A OH   1 
ATOM   167  O  OH   B TYR   A 1 9   ? 14.819 -5.353  12.932  0.30 14.80 ?  9   TYR   A OH   1 
ATOM   168  H  H    A TYR   A 1 9   ? 10.276 -9.646  15.548  0.70 16.81 ?  9   TYR   A H    1 
ATOM   169  H  H    B TYR   A 1 9   ? 10.594 -9.422  16.017  0.30 19.82 ?  9   TYR   A H    1 
ATOM   170  H  HA   A TYR   A 1 9   ? 9.834  -9.208  12.938  0.70 15.84 ?  9   TYR   A HA   1 
ATOM   171  H  HA   B TYR   A 1 9   ? 9.968  -8.948  13.465  0.30 18.12 ?  9   TYR   A HA   1 
ATOM   172  H  HB2  A TYR   A 1 9   ? 11.796 -10.769 14.239  0.70 16.75 ?  9   TYR   A HB2  1 
ATOM   173  H  HB2  B TYR   A 1 9   ? 12.038 -10.440 14.646  0.30 18.20 ?  9   TYR   A HB2  1 
ATOM   174  H  HB3  A TYR   A 1 9   ? 11.610 -10.807 12.663  0.70 16.75 ?  9   TYR   A HB3  1 
ATOM   175  H  HB3  B TYR   A 1 9   ? 11.760 -10.561 13.087  0.30 18.20 ?  9   TYR   A HB3  1 
ATOM   176  H  HD1  A TYR   A 1 9   ? 12.454 -8.550  15.259  0.70 18.48 ?  9   TYR   A HD1  1 
ATOM   177  H  HD1  B TYR   A 1 9   ? 12.438 -8.005  15.478  0.30 18.08 ?  9   TYR   A HD1  1 
ATOM   178  H  HD2  A TYR   A 1 9   ? 12.745 -9.227  11.325  0.70 17.67 ?  9   TYR   A HD2  1 
ATOM   179  H  HD2  B TYR   A 1 9   ? 12.914 -9.095  11.659  0.30 17.33 ?  9   TYR   A HD2  1 
ATOM   180  H  HE1  A TYR   A 1 9   ? 13.863 -6.739  15.053  0.70 19.20 ?  9   TYR   A HE1  1 
ATOM   181  H  HE1  B TYR   A 1 9   ? 13.710 -6.121  15.100  0.30 17.72 ?  9   TYR   A HE1  1 
ATOM   182  H  HE2  A TYR   A 1 9   ? 14.155 -7.415  11.115  0.70 18.57 ?  9   TYR   A HE2  1 
ATOM   183  H  HE2  B TYR   A 1 9   ? 14.192 -7.205  11.277  0.30 17.05 ?  9   TYR   A HE2  1 
ATOM   184  H  HH   A TYR   A 1 9   ? 15.106 -5.471  13.672  0.70 21.26 ?  9   TYR   A HH   1 
ATOM   185  H  HH   B TYR   A 1 9   ? 14.886 -4.908  13.643  0.30 17.74 ?  9   TYR   A HH   1 
ATOM   186  N  N    A LEU   A 1 10  ? 8.780  -11.232 12.079  0.70 12.23 ?  10  LEU   A N    1 
ATOM   187  N  N    B LEU   A 1 10  ? 8.833  -10.936 12.577  0.30 13.25 ?  10  LEU   A N    1 
ATOM   188  C  CA   A LEU   A 1 10  ? 8.199  -12.474 11.589  0.70 11.99 ?  10  LEU   A CA   1 
ATOM   189  C  CA   B LEU   A 1 10  ? 8.160  -12.127 12.079  0.30 13.09 ?  10  LEU   A CA   1 
ATOM   190  C  C    A LEU   A 1 10  ? 9.324  -13.417 11.156  0.70 12.07 ?  10  LEU   A C    1 
ATOM   191  C  C    B LEU   A 1 10  ? 9.209  -13.104 11.562  0.30 12.43 ?  10  LEU   A C    1 
ATOM   192  O  O    A LEU   A 1 10  ? 10.279 -12.999 10.496  0.70 12.30 ?  10  LEU   A O    1 
ATOM   193  O  O    B LEU   A 1 10  ? 10.109 -12.723 10.808  0.30 12.33 ?  10  LEU   A O    1 
ATOM   194  C  CB   A LEU   A 1 10  ? 7.299  -12.156 10.399  0.70 13.18 ?  10  LEU   A CB   1 
ATOM   195  C  CB   B LEU   A 1 10  ? 7.198  -11.756 10.948  0.30 13.34 ?  10  LEU   A CB   1 
ATOM   196  C  CG   A LEU   A 1 10  ? 6.609  -13.325 9.704   0.70 15.52 ?  10  LEU   A CG   1 
ATOM   197  C  CG   B LEU   A 1 10  ? 6.399  -12.915 10.354  0.30 14.15 ?  10  LEU   A CG   1 
ATOM   198  C  CD1  A LEU   A 1 10  ? 5.558  -13.938 10.609  0.70 16.69 ?  10  LEU   A CD1  1 
ATOM   199  C  CD1  B LEU   A 1 10  ? 5.491  -13.510 11.415  0.30 14.67 ?  10  LEU   A CD1  1 
ATOM   200  C  CD2  A LEU   A 1 10  ? 6.001  -12.862 8.390   0.70 16.72 ?  10  LEU   A CD2  1 
ATOM   201  C  CD2  B LEU   A 1 10  ? 5.590  -12.430 9.168   0.30 15.17 ?  10  LEU   A CD2  1 
ATOM   202  H  H    A LEU   A 1 10  ? 8.833  -10.622 11.475  0.70 14.65 ?  10  LEU   A H    1 
ATOM   203  H  H    B LEU   A 1 10  ? 8.858  -10.290 12.016  0.30 15.89 ?  10  LEU   A H    1 
ATOM   204  H  HA   A LEU   A 1 10  ? 7.673  -12.905 12.286  0.70 14.37 ?  10  LEU   A HA   1 
ATOM   205  H  HA   B LEU   A 1 10  ? 7.652  -12.547 12.795  0.30 15.68 ?  10  LEU   A HA   1 
ATOM   206  H  HB2  A LEU   A 1 10  ? 6.598  -11.565 10.701  0.70 15.80 ?  10  LEU   A HB2  1 
ATOM   207  H  HB2  B LEU   A 1 10  ? 6.552  -11.108 11.282  0.30 15.99 ?  10  LEU   A HB2  1 
ATOM   208  H  HB3  A LEU   A 1 10  ? 7.833  -11.714 9.727   0.70 15.80 ?  10  LEU   A HB3  1 
ATOM   209  H  HB3  B LEU   A 1 10  ? 7.707  -11.357 10.227  0.30 15.99 ?  10  LEU   A HB3  1 
ATOM   210  H  HG   A LEU   A 1 10  ? 7.265  -14.018 9.504   0.70 18.61 ?  10  LEU   A HG   1 
ATOM   211  H  HG   B LEU   A 1 10  ? 7.009  -13.606 10.048  0.30 16.96 ?  10  LEU   A HG   1 
ATOM   212  H  HD11 A LEU   A 1 10  ? 5.164  -14.709 10.168  0.70 20.01 ?  10  LEU   A HD11 1 
ATOM   213  H  HD11 B LEU   A 1 10  ? 4.953  -14.209 11.012  0.30 17.58 ?  10  LEU   A HD11 1 
ATOM   214  H  HD12 A LEU   A 1 10  ? 5.974  -14.214 11.442  0.70 20.01 ?  10  LEU   A HD12 1 
ATOM   215  H  HD12 B LEU   A 1 10  ? 6.032  -13.878 12.129  0.30 17.58 ?  10  LEU   A HD12 1 
ATOM   216  H  HD13 A LEU   A 1 10  ? 4.872  -13.275 10.789  0.70 20.01 ?  10  LEU   A HD13 1 
ATOM   217  H  HD13 B LEU   A 1 10  ? 4.916  -12.810 11.763  0.30 17.58 ?  10  LEU   A HD13 1 
ATOM   218  H  HD21 A LEU   A 1 10  ? 5.558  -13.615 7.965   0.70 20.05 ?  10  LEU   A HD21 1 
ATOM   219  H  HD21 B LEU   A 1 10  ? 5.092  -13.174 8.802   0.30 18.18 ?  10  LEU   A HD21 1 
ATOM   220  H  HD22 A LEU   A 1 10  ? 5.359  -12.162 8.575   0.70 20.05 ?  10  LEU   A HD22 1 
ATOM   221  H  HD22 B LEU   A 1 10  ? 4.982  -11.736 9.468   0.30 18.18 ?  10  LEU   A HD22 1 
ATOM   222  H  HD23 A LEU   A 1 10  ? 6.708  -12.528 7.820   0.70 20.05 ?  10  LEU   A HD23 1 
ATOM   223  H  HD23 B LEU   A 1 10  ? 6.197  -12.073 8.501   0.30 18.18 ?  10  LEU   A HD23 1 
ATOM   224  N  N    A LYS   A 1 11  ? 9.219  -14.693 11.540  0.70 12.32 ?  11  LYS   A N    1 
ATOM   225  N  N    B LYS   A 1 11  ? 9.098  -14.360 11.975  0.30 12.43 ?  11  LYS   A N    1 
ATOM   226  C  CA   A LYS   A 1 11  ? 10.223 -15.699 11.206  0.70 12.43 ?  11  LYS   A CA   1 
ATOM   227  C  CA   B LYS   A 1 11  ? 10.060 -15.377 11.578  0.30 12.05 ?  11  LYS   A CA   1 
ATOM   228  C  C    A LYS   A 1 11  ? 9.878  -16.297 9.849   0.70 12.44 ?  11  LYS   A C    1 
ATOM   229  C  C    B LYS   A 1 11  ? 9.692  -15.899 10.193  0.30 11.41 ?  11  LYS   A C    1 
ATOM   230  O  O    A LYS   A 1 11  ? 8.817  -16.906 9.696   0.70 14.73 ?  11  LYS   A O    1 
ATOM   231  O  O    B LYS   A 1 11  ? 8.563  -16.350 9.976   0.30 11.53 ?  11  LYS   A O    1 
ATOM   232  C  CB   A LYS   A 1 11  ? 10.254 -16.782 12.286  0.70 12.60 ?  11  LYS   A CB   1 
ATOM   233  C  CB   B LYS   A 1 11  ? 10.053 -16.508 12.603  0.30 12.45 ?  11  LYS   A CB   1 
ATOM   234  C  CG   A LYS   A 1 11  ? 11.311 -17.870 12.114  0.70 13.17 ?  11  LYS   A CG   1 
ATOM   235  C  CG   B LYS   A 1 11  ? 11.008 -17.638 12.289  0.30 12.89 ?  11  LYS   A CG   1 
ATOM   236  C  CD   A LYS   A 1 11  ? 11.400 -18.700 13.403  0.70 13.41 ?  11  LYS   A CD   1 
ATOM   237  C  CD   B LYS   A 1 11  ? 10.991 -18.692 13.383  0.30 13.30 ?  11  LYS   A CD   1 
ATOM   238  C  CE   A LYS   A 1 11  ? 12.407 -19.845 13.324  0.70 13.52 ?  11  LYS   A CE   1 
ATOM   239  C  CE   B LYS   A 1 11  ? 11.961 -19.827 13.077  0.30 13.40 ?  11  LYS   A CE   1 
ATOM   240  N  NZ   A LYS   A 1 11  ? 13.782 -19.374 13.022  0.70 13.80 ?  11  LYS   A NZ   1 
ATOM   241  N  NZ   B LYS   A 1 11  ? 13.382 -19.369 13.033  0.30 13.84 ?  11  LYS   A NZ   1 
ATOM   242  H  H    A LYS   A 1 11  ? 8.559  -15.012 11.994  0.70 14.77 ?  11  LYS   A H    1 
ATOM   243  H  H    B LYS   A 1 11  ? 8.468  -14.646 12.482  0.30 14.89 ?  11  LYS   A H    1 
ATOM   244  H  HA   A LYS   A 1 11  ? 11.099 -15.289 11.151  0.70 14.89 ?  11  LYS   A HA   1 
ATOM   245  H  HA   B LYS   A 1 11  ? 10.948 -14.984 11.542  0.30 14.44 ?  11  LYS   A HA   1 
ATOM   246  H  HB2  A LYS   A 1 11  ? 10.425 -16.355 13.139  0.70 15.10 ?  11  LYS   A HB2  1 
ATOM   247  H  HB2  B LYS   A 1 11  ? 10.300 -16.139 13.467  0.30 14.92 ?  11  LYS   A HB2  1 
ATOM   248  H  HB3  A LYS   A 1 11  ? 9.393  -17.222 12.309  0.70 15.10 ?  11  LYS   A HB3  1 
ATOM   249  H  HB3  B LYS   A 1 11  ? 9.159  -16.875 12.648  0.30 14.92 ?  11  LYS   A HB3  1 
ATOM   250  H  HG2  A LYS   A 1 11  ? 11.060 -18.463 11.386  0.70 15.78 ?  11  LYS   A HG2  1 
ATOM   251  H  HG2  B LYS   A 1 11  ? 10.744 -18.059 11.457  0.30 15.45 ?  11  LYS   A HG2  1 
ATOM   252  H  HG3  A LYS   A 1 11  ? 12.177 -17.471 11.947  0.70 15.78 ?  11  LYS   A HG3  1 
ATOM   253  H  HG3  B LYS   A 1 11  ? 11.909 -17.286 12.218  0.30 15.45 ?  11  LYS   A HG3  1 
ATOM   254  H  HD2  A LYS   A 1 11  ? 11.665 -18.123 14.134  0.70 16.07 ?  11  LYS   A HD2  1 
ATOM   255  H  HD2  B LYS   A 1 11  ? 11.251 -18.288 14.225  0.30 15.94 ?  11  LYS   A HD2  1 
ATOM   256  H  HD3  A LYS   A 1 11  ? 10.529 -19.090 13.589  0.70 16.07 ?  11  LYS   A HD3  1 
ATOM   257  H  HD3  B LYS   A 1 11  ? 10.097 -19.066 13.454  0.30 15.94 ?  11  LYS   A HD3  1 
ATOM   258  H  HE2  A LYS   A 1 11  ? 12.432 -20.308 14.179  0.70 16.21 ?  11  LYS   A HE2  1 
ATOM   259  H  HE2  B LYS   A 1 11  ? 11.885 -20.507 13.764  0.30 16.06 ?  11  LYS   A HE2  1 
ATOM   260  H  HE3  A LYS   A 1 11  ? 12.140 -20.460 12.624  0.70 16.21 ?  11  LYS   A HE3  1 
ATOM   261  H  HE3  B LYS   A 1 11  ? 11.742 -20.206 12.209  0.30 16.06 ?  11  LYS   A HE3  1 
ATOM   262  H  HZ1  A LYS   A 1 11  ? 14.338 -20.068 12.973  0.70 16.54 ?  11  LYS   A HZ1  1 
ATOM   263  H  HZ1  B LYS   A 1 11  ? 13.921 -20.058 12.868  0.30 16.58 ?  11  LYS   A HZ1  1 
ATOM   264  H  HZ2  A LYS   A 1 11  ? 13.790 -18.943 12.244  0.70 16.54 ?  11  LYS   A HZ2  1 
ATOM   265  H  HZ2  B LYS   A 1 11  ? 13.487 -18.760 12.391  0.30 16.58 ?  11  LYS   A HZ2  1 
ATOM   266  H  HZ3  A LYS   A 1 11  ? 14.063 -18.824 13.662  0.70 16.54 ?  11  LYS   A HZ3  1 
ATOM   267  H  HZ3  B LYS   A 1 11  ? 13.608 -19.006 13.814  0.30 16.58 ?  11  LYS   A HZ3  1 
ATOM   268  N  N    A LEU   A 1 12  ? 10.771 -16.148 8.868   0.70 11.50 ?  12  LEU   A N    1 
ATOM   269  N  N    B LEU   A 1 12  ? 10.629 -15.817 9.250   0.30 11.46 ?  12  LEU   A N    1 
ATOM   270  C  CA   A LEU   A 1 12  ? 10.515 -16.727 7.551   0.70 12.05 ?  12  LEU   A CA   1 
ATOM   271  C  CA   B LEU   A 1 12  ? 10.404 -16.319 7.898   0.30 11.72 ?  12  LEU   A CA   1 
ATOM   272  C  C    A LEU   A 1 12  ? 11.103 -18.126 7.406   0.70 12.32 ?  12  LEU   A C    1 
ATOM   273  C  C    B LEU   A 1 12  ? 10.977 -17.710 7.674   0.30 11.63 ?  12  LEU   A C    1 
ATOM   274  O  O    A LEU   A 1 12  ? 10.468 -19.004 6.810   0.70 12.74 ?  12  LEU   A O    1 
ATOM   275  O  O    B LEU   A 1 12  ? 10.320 -18.556 7.056   0.30 11.84 ?  12  LEU   A O    1 
ATOM   276  C  CB   A LEU   A 1 12  ? 11.065 -15.829 6.435   0.70 12.29 ?  12  LEU   A CB   1 
ATOM   277  C  CB   B LEU   A 1 12  ? 10.991 -15.354 6.861   0.30 12.69 ?  12  LEU   A CB   1 
ATOM   278  C  CG   A LEU   A 1 12  ? 10.421 -14.452 6.254   0.70 12.98 ?  12  LEU   A CG   1 
ATOM   279  C  CG   B LEU   A 1 12  ? 10.283 -14.004 6.756   0.30 13.47 ?  12  LEU   A CG   1 
ATOM   280  C  CD1  A LEU   A 1 12  ? 11.184 -13.658 5.216   0.70 13.24 ?  12  LEU   A CD1  1 
ATOM   281  C  CD1  B LEU   A 1 12  ? 10.785 -13.230 5.549   0.30 13.87 ?  12  LEU   A CD1  1 
ATOM   282  C  CD2  A LEU   A 1 12  ? 8.950  -14.578 5.861   0.70 13.99 ?  12  LEU   A CD2  1 
ATOM   283  C  CD2  B LEU   A 1 12  ? 8.774  -14.208 6.686   0.30 13.81 ?  12  LEU   A CD2  1 
ATOM   284  H  H    A LEU   A 1 12  ? 11.531 -15.729 8.936   0.70 13.78 ?  12  LEU   A H    1 
ATOM   285  H  H    B LEU   A 1 12  ? 11.404 -15.452 9.366   0.30 13.73 ?  12  LEU   A H    1 
ATOM   286  H  HA   A LEU   A 1 12  ? 9.559  -16.801 7.433   0.70 14.44 ?  12  LEU   A HA   1 
ATOM   287  H  HA   B LEU   A 1 12  ? 9.450  -16.377 7.750   0.30 14.05 ?  12  LEU   A HA   1 
ATOM   288  H  HB2  A LEU   A 1 12  ? 12.006 -15.688 6.605   0.70 14.72 ?  12  LEU   A HB2  1 
ATOM   289  H  HB2  B LEU   A 1 12  ? 11.918 -15.176 7.089   0.30 15.21 ?  12  LEU   A HB2  1 
ATOM   290  H  HB3  A LEU   A 1 12  ? 10.959 -16.309 5.597   0.70 14.72 ?  12  LEU   A HB3  1 
ATOM   291  H  HB3  B LEU   A 1 12  ? 10.946 -15.773 5.988   0.30 15.21 ?  12  LEU   A HB3  1 
ATOM   292  H  HG   A LEU   A 1 12  ? 10.465 -13.975 7.094   0.70 15.55 ?  12  LEU   A HG   1 
ATOM   293  H  HG   B LEU   A 1 12  ? 10.478 -13.479 7.550   0.30 16.14 ?  12  LEU   A HG   1 
ATOM   294  H  HD11 A LEU   A 1 12  ? 10.765 -12.792 5.111   0.70 15.87 ?  12  LEU   A HD11 1 
ATOM   295  H  HD11 B LEU   A 1 12  ? 10.326 -12.376 5.508   0.30 16.62 ?  12  LEU   A HD11 1 
ATOM   296  H  HD12 A LEU   A 1 12  ? 12.102 -13.548 5.516   0.70 15.87 ?  12  LEU   A HD12 1 
ATOM   297  H  HD12 B LEU   A 1 12  ? 11.739 -13.089 5.639   0.30 16.62 ?  12  LEU   A HD12 1 
ATOM   298  H  HD13 A LEU   A 1 12  ? 11.169 -14.139 4.374   0.70 15.87 ?  12  LEU   A HD13 1 
ATOM   299  H  HD13 B LEU   A 1 12  ? 10.599 -13.744 4.747   0.30 16.62 ?  12  LEU   A HD13 1 
ATOM   300  H  HD21 A LEU   A 1 12  ? 8.587  -13.695 5.701   0.70 16.77 ?  12  LEU   A HD21 1 
ATOM   301  H  HD21 B LEU   A 1 12  ? 8.361  -13.411 6.329   0.30 16.55 ?  12  LEU   A HD21 1 
ATOM   302  H  HD22 A LEU   A 1 12  ? 8.881  -15.114 5.053   0.70 16.77 ?  12  LEU   A HD22 1 
ATOM   303  H  HD22 B LEU   A 1 12  ? 8.586  -14.968 6.112   0.30 16.55 ?  12  LEU   A HD22 1 
ATOM   304  H  HD23 A LEU   A 1 12  ? 8.461  -15.012 6.581   0.70 16.77 ?  12  LEU   A HD23 1 
ATOM   305  H  HD23 B LEU   A 1 12  ? 8.437  -14.383 7.582   0.30 16.55 ?  12  LEU   A HD23 1 
ATOM   306  N  N    A THR   A 1 13  ? 12.314 -18.333 7.914   0.70 12.70 ?  13  THR   A N    1 
ATOM   307  N  N    B THR   A 1 13  ? 12.193 -17.962 8.146   0.30 11.59 ?  13  THR   A N    1 
ATOM   308  C  CA   A THR   A 1 13  ? 13.011 -19.611 7.837   0.70 13.57 ?  13  THR   A CA   1 
ATOM   309  C  CA   B THR   A 1 13  ? 12.833 -19.262 8.010   0.30 12.17 ?  13  THR   A CA   1 
ATOM   310  C  C    A THR   A 1 13  ? 13.776 -19.811 9.139   0.70 13.63 ?  13  THR   A C    1 
ATOM   311  C  C    B THR   A 1 13  ? 13.605 -19.556 9.290   0.30 12.48 ?  13  THR   A C    1 
ATOM   312  O  O    A THR   A 1 13  ? 13.677 -19.014 10.076  0.70 13.84 ?  13  THR   A O    1 
ATOM   313  O  O    B THR   A 1 13  ? 13.516 -18.829 10.285  0.30 12.55 ?  13  THR   A O    1 
ATOM   314  C  CB   A THR   A 1 13  ? 13.989 -19.670 6.654   0.70 14.11 ?  13  THR   A CB   1 
ATOM   315  C  CB   B THR   A 1 13  ? 13.784 -19.298 6.807   0.30 12.39 ?  13  THR   A CB   1 
ATOM   316  O  OG1  A THR   A 1 13  ? 15.072 -18.770 6.905   0.70 14.42 ?  13  THR   A OG1  1 
ATOM   317  O  OG1  B THR   A 1 13  ? 14.845 -18.365 7.025   0.30 12.00 ?  13  THR   A OG1  1 
ATOM   318  C  CG2  A THR   A 1 13  ? 13.320 -19.297 5.341   0.70 15.47 ?  13  THR   A CG2  1 
ATOM   319  C  CG2  B THR   A 1 13  ? 13.066 -18.972 5.498   0.30 12.87 ?  13  THR   A CG2  1 
ATOM   320  H  H    A THR   A 1 13  ? 12.772 -17.728 8.311   0.70 15.22 ?  13  THR   A H    1 
ATOM   321  H  H    B THR   A 1 13  ? 12.677 -17.371 8.543   0.30 13.89 ?  13  THR   A H    1 
ATOM   322  H  HA   A THR   A 1 13  ? 12.367 -20.333 7.736   0.70 16.26 ?  13  THR   A HA   1 
ATOM   323  H  HA   B THR   A 1 13  ? 12.153 -19.941 7.886   0.30 14.58 ?  13  THR   A HA   1 
ATOM   324  H  HB   A THR   A 1 13  ? 14.340 -20.572 6.565   0.70 16.91 ?  13  THR   A HB   1 
ATOM   325  H  HB   B THR   A 1 13  ? 14.161 -20.184 6.725   0.30 14.85 ?  13  THR   A HB   1 
ATOM   326  H  HG1  A THR   A 1 13  ? 15.614 -18.785 6.255   0.70 17.28 ?  13  THR   A HG1  1 
ATOM   327  H  HG1  B THR   A 1 13  ? 15.372 -18.366 6.366   0.30 14.38 ?  13  THR   A HG1  1 
ATOM   328  H  HG21 A THR   A 1 13  ? 13.925 -19.467 4.600   0.70 18.54 ?  13  THR   A HG21 1 
ATOM   329  H  HG21 B THR   A 1 13  ? 13.685 -19.052 4.751   0.30 15.42 ?  13  THR   A HG21 1 
ATOM   330  H  HG22 A THR   A 1 13  ? 12.517 -19.827 5.216   0.70 18.54 ?  13  THR   A HG22 1 
ATOM   331  H  HG22 B THR   A 1 13  ? 12.332 -19.595 5.359   0.30 15.42 ?  13  THR   A HG22 1 
ATOM   332  H  HG23 A THR   A 1 13  ? 13.082 -18.358 5.344   0.70 18.54 ?  13  THR   A HG23 1 
ATOM   333  H  HG23 B THR   A 1 13  ? 12.715 -18.071 5.520   0.30 15.42 ?  13  THR   A HG23 1 
ATOM   334  N  N    A ASP   A 1 14  ? 14.581 -20.874 9.183   0.70 14.52 ?  14  ASP   A N    1 
ATOM   335  N  N    B ASP   A 1 14  ? 14.388 -20.633 9.239   0.30 13.48 ?  14  ASP   A N    1 
ATOM   336  C  CA   A ASP   A 1 14  ? 15.421 -21.116 10.349  0.70 15.23 ?  14  ASP   A CA   1 
ATOM   337  C  CA   B ASP   A 1 14  ? 15.258 -20.997 10.349  0.30 14.53 ?  14  ASP   A CA   1 
ATOM   338  C  C    A ASP   A 1 14  ? 16.221 -19.879 10.747  0.70 14.80 ?  14  ASP   A C    1 
ATOM   339  C  C    B ASP   A 1 14  ? 16.167 -19.841 10.748  0.30 14.35 ?  14  ASP   A C    1 
ATOM   340  O  O    A ASP   A 1 14  ? 16.436 -19.630 11.939  0.70 16.31 ?  14  ASP   A O    1 
ATOM   341  O  O    B ASP   A 1 14  ? 16.411 -19.616 11.940  0.30 14.92 ?  14  ASP   A O    1 
ATOM   342  C  CB   A ASP   A 1 14  ? 16.380 -22.268 10.066  0.70 17.57 ?  14  ASP   A CB   1 
ATOM   343  C  CB   B ASP   A 1 14  ? 16.093 -22.214 9.950   0.30 16.17 ?  14  ASP   A CB   1 
ATOM   344  C  CG   A ASP   A 1 14  ? 17.312 -22.524 11.221  0.70 21.69 ?  14  ASP   A CG   1 
ATOM   345  C  CG   B ASP   A 1 14  ? 17.011 -22.686 11.060  0.30 17.68 ?  14  ASP   A CG   1 
ATOM   346  O  OD1  A ASP   A 1 14  ? 16.841 -23.002 12.274  0.70 23.52 ?  14  ASP   A OD1  1 
ATOM   347  O  OD1  B ASP   A 1 14  ? 16.518 -22.881 12.191  0.30 17.92 ?  14  ASP   A OD1  1 
ATOM   348  O  OD2  A ASP   A 1 14  ? 18.510 -22.215 11.078  0.70 23.81 -1 14  ASP   A OD2  1 
ATOM   349  O  OD2  B ASP   A 1 14  ? 18.217 -22.883 10.800  0.30 18.64 -1 14  ASP   A OD2  1 
ATOM   350  H  H    A ASP   A 1 14  ? 14.669 -21.459 8.552   0.70 17.41 ?  14  ASP   A H    1 
ATOM   351  H  H    B ASP   A 1 14  ? 14.426 -21.159 8.567   0.30 16.16 ?  14  ASP   A H    1 
ATOM   352  H  HA   A ASP   A 1 14  ? 14.861 -21.372 11.098  0.70 18.26 ?  14  ASP   A HA   1 
ATOM   353  H  HA   B ASP   A 1 14  ? 14.711 -21.234 11.115  0.30 17.42 ?  14  ASP   A HA   1 
ATOM   354  H  HB2  A ASP   A 1 14  ? 15.863 -23.079 9.885   0.70 21.06 ?  14  ASP   A HB2  1 
ATOM   355  H  HB2  B ASP   A 1 14  ? 15.491 -22.945 9.731   0.30 19.38 ?  14  ASP   A HB2  1 
ATOM   356  H  HB3  A ASP   A 1 14  ? 16.927 -22.054 9.297   0.70 21.06 ?  14  ASP   A HB3  1 
ATOM   357  H  HB3  B ASP   A 1 14  ? 16.625 -21.984 9.172   0.30 19.38 ?  14  ASP   A HB3  1 
ATOM   358  N  N    . ASN   A 1 15  ? 16.677 -19.090 9.768   1.00 14.07 ?  15  ASN   A N    1 
ATOM   359  C  CA   . ASN   A 1 15  ? 17.659 -18.040 10.033  1.00 14.26 ?  15  ASN   A CA   1 
ATOM   360  C  C    . ASN   A 1 15  ? 17.289 -16.641 9.551   1.00 14.78 ?  15  ASN   A C    1 
ATOM   361  O  O    . ASN   A 1 15  ? 18.072 -15.714 9.787   1.00 16.04 ?  15  ASN   A O    1 
ATOM   362  C  CB   . ASN   A 1 15  ? 19.033 -18.435 9.457   1.00 14.04 ?  15  ASN   A CB   1 
ATOM   363  C  CG   . ASN   A 1 15  ? 19.026 -18.538 7.947   1.00 14.56 ?  15  ASN   A CG   1 
ATOM   364  O  OD1  . ASN   A 1 15  ? 18.302 -19.354 7.377   1.00 15.31 ?  15  ASN   A OD1  1 
ATOM   365  N  ND2  . ASN   A 1 15  ? 19.823 -17.699 7.286   1.00 14.92 ?  15  ASN   A ND2  1 
ATOM   366  H  H    A ASN   A 1 15  ? 16.427 -19.141 8.947   0.70 16.86 ?  15  ASN   A H    1 
ATOM   367  H  H    B ASN   A 1 15  ? 16.471 -19.175 8.938   0.30 16.86 ?  15  ASN   A H    1 
ATOM   368  H  HA   . ASN   A 1 15  ? 17.781 -17.975 10.989  1.00 17.09 ?  15  ASN   A HA   1 
ATOM   369  H  HB2  . ASN   A 1 15  ? 19.691 -17.759 9.711   1.00 16.83 ?  15  ASN   A HB2  1 
ATOM   370  H  HB3  . ASN   A 1 15  ? 19.300 -19.297 9.816   1.00 16.83 ?  15  ASN   A HB3  1 
ATOM   371  H  HD21 . ASN   A 1 15  ? 19.855 -17.716 6.425   1.00 17.89 ?  15  ASN   A HD21 1 
ATOM   372  H  HD22 . ASN   A 1 15  ? 20.319 -17.133 7.715   1.00 17.89 ?  15  ASN   A HD22 1 
ATOM   373  N  N    A VAL   A 1 16  ? 16.182 -16.481 8.827   0.70 13.80 ?  16  VAL   A N    1 
ATOM   374  N  N    B VAL   A 1 16  ? 16.100 -16.425 8.987   0.30 14.08 ?  16  VAL   A N    1 
ATOM   375  C  CA   A VAL   A 1 16  ? 15.791 -15.208 8.233   0.70 13.75 ?  16  VAL   A CA   1 
ATOM   376  C  CA   B VAL   A 1 16  ? 15.717 -15.122 8.445   0.30 13.42 ?  16  VAL   A CA   1 
ATOM   377  C  C    A VAL   A 1 16  ? 14.502 -14.726 8.884   0.70 12.83 ?  16  VAL   A C    1 
ATOM   378  C  C    B VAL   A 1 16  ? 14.481 -14.597 9.172   0.30 13.29 ?  16  VAL   A C    1 
ATOM   379  O  O    A VAL   A 1 16  ? 13.498 -15.452 8.933   0.70 11.96 ?  16  VAL   A O    1 
ATOM   380  O  O    B VAL   A 1 16  ? 13.519 -15.339 9.402   0.30 13.31 ?  16  VAL   A O    1 
ATOM   381  C  CB   A VAL   A 1 16  ? 15.640 -15.303 6.705   0.70 14.52 ?  16  VAL   A CB   1 
ATOM   382  C  CB   B VAL   A 1 16  ? 15.491 -15.188 6.920   0.30 13.24 ?  16  VAL   A CB   1 
ATOM   383  C  CG1  A VAL   A 1 16  ? 15.223 -13.951 6.126   0.70 15.28 ?  16  VAL   A CG1  1 
ATOM   384  C  CG1  B VAL   A 1 16  ? 15.093 -13.822 6.363   0.30 13.61 ?  16  VAL   A CG1  1 
ATOM   385  C  CG2  A VAL   A 1 16  ? 16.935 -15.786 6.058   0.70 15.02 ?  16  VAL   A CG2  1 
ATOM   386  C  CG2  B VAL   A 1 16  ? 16.742 -15.718 6.217   0.30 13.60 ?  16  VAL   A CG2  1 
ATOM   387  H  H    A VAL   A 1 16  ? 15.632 -17.123 8.662   0.70 16.54 ?  16  VAL   A H    1 
ATOM   388  H  H    B VAL   A 1 16  ? 15.484 -17.022 8.919   0.30 16.88 ?  16  VAL   A H    1 
ATOM   389  H  HA   A VAL   A 1 16  ? 16.488 -14.559 8.419   0.70 16.48 ?  16  VAL   A HA   1 
ATOM   390  H  HA   B VAL   A 1 16  ? 16.436 -14.491 8.603   0.30 16.09 ?  16  VAL   A HA   1 
ATOM   391  H  HB   A VAL   A 1 16  ? 14.947 -15.949 6.498   0.70 17.41 ?  16  VAL   A HB   1 
ATOM   392  H  HB   B VAL   A 1 16  ? 14.769 -15.805 6.738   0.30 15.86 ?  16  VAL   A HB   1 
ATOM   393  H  HG11 A VAL   A 1 16  ? 15.313 -13.983 5.161   0.70 18.32 ?  16  VAL   A HG11 1 
ATOM   394  H  HG11 B VAL   A 1 16  ? 15.134 -13.855 5.393   0.30 16.31 ?  16  VAL   A HG11 1 
ATOM   395  H  HG12 A VAL   A 1 16  ? 14.298 -13.777 6.365   0.70 18.32 ?  16  VAL   A HG12 1 
ATOM   396  H  HG12 B VAL   A 1 16  ? 14.189 -13.616 6.646   0.30 16.31 ?  16  VAL   A HG12 1 
ATOM   397  H  HG13 A VAL   A 1 16  ? 15.797 -13.262 6.490   0.70 18.32 ?  16  VAL   A HG13 1 
ATOM   398  H  HG13 B VAL   A 1 16  ? 15.709 -13.152 6.696   0.30 16.31 ?  16  VAL   A HG13 1 
ATOM   399  H  HG21 A VAL   A 1 16  ? 16.834 -15.756 5.093   0.70 18.01 ?  16  VAL   A HG21 1 
ATOM   400  H  HG21 B VAL   A 1 16  ? 16.606 -15.680 5.257   0.30 16.30 ?  16  VAL   A HG21 1 
ATOM   401  H  HG22 A VAL   A 1 16  ? 17.662 -15.208 6.332   0.70 18.01 ?  16  VAL   A HG22 1 
ATOM   402  H  HG22 B VAL   A 1 16  ? 17.504 -15.170 6.464   0.30 16.30 ?  16  VAL   A HG22 1 
ATOM   403  H  HG23 A VAL   A 1 16  ? 17.112 -16.697 6.343   0.70 18.01 ?  16  VAL   A HG23 1 
ATOM   404  H  HG23 B VAL   A 1 16  ? 16.895 -16.637 6.492   0.30 16.30 ?  16  VAL   A HG23 1 
ATOM   405  N  N    A TYR   A 1 17  ? 14.544 -13.483 9.352   0.70 12.63 ?  17  TYR   A N    1 
ATOM   406  N  N    B TYR   A 1 17  ? 14.515 -13.305 9.522   0.30 13.06 ?  17  TYR   A N    1 
ATOM   407  C  CA   A TYR   A 1 17  ? 13.456 -12.788 10.015  0.70 12.38 ?  17  TYR   A CA   1 
ATOM   408  C  CA   B TYR   A 1 17  ? 13.463 -12.634 10.279  0.30 12.58 ?  17  TYR   A CA   1 
ATOM   409  C  C    A TYR   A 1 17  ? 13.187 -11.482 9.275   0.70 12.32 ?  17  TYR   A C    1 
ATOM   410  C  C    B TYR   A 1 17  ? 13.205 -11.266 9.657   0.30 12.26 ?  17  TYR   A C    1 
ATOM   411  O  O    A TYR   A 1 17  ? 14.081 -10.941 8.625   0.70 12.31 ?  17  TYR   A O    1 
ATOM   412  O  O    B TYR   A 1 17  ? 14.126 -10.646 9.124   0.30 11.77 ?  17  TYR   A O    1 
ATOM   413  C  CB   A TYR   A 1 17  ? 13.866 -12.486 11.461  0.70 13.72 ?  17  TYR   A CB   1 
ATOM   414  C  CB   B TYR   A 1 17  ? 13.899 -12.467 11.745  0.30 12.71 ?  17  TYR   A CB   1 
ATOM   415  C  CG   A TYR   A 1 17  ? 14.014 -13.730 12.305  0.70 14.90 ?  17  TYR   A CG   1 
ATOM   416  C  CG   B TYR   A 1 17  ? 14.168 -13.783 12.457  0.30 12.87 ?  17  TYR   A CG   1 
ATOM   417  C  CD1  A TYR   A 1 17  ? 15.165 -14.513 12.254  0.70 15.95 ?  17  TYR   A CD1  1 
ATOM   418  C  CD1  B TYR   A 1 17  ? 15.381 -14.452 12.314  0.30 13.15 ?  17  TYR   A CD1  1 
ATOM   419  C  CD2  A TYR   A 1 17  ? 12.986 -14.135 13.141  0.70 15.19 ?  17  TYR   A CD2  1 
ATOM   420  C  CD2  B TYR   A 1 17  ? 13.203 -14.353 13.272  0.30 13.13 ?  17  TYR   A CD2  1 
ATOM   421  C  CE1  A TYR   A 1 17  ? 15.283 -15.668 13.025  0.70 16.41 ?  17  TYR   A CE1  1 
ATOM   422  C  CE1  B TYR   A 1 17  ? 15.617 -15.661 12.964  0.30 13.54 ?  17  TYR   A CE1  1 
ATOM   423  C  CE2  A TYR   A 1 17  ? 13.090 -15.286 13.910  0.70 15.73 ?  17  TYR   A CE2  1 
ATOM   424  C  CE2  B TYR   A 1 17  ? 13.427 -15.554 13.925  0.30 13.30 ?  17  TYR   A CE2  1 
ATOM   425  C  CZ   A TYR   A 1 17  ? 14.238 -16.047 13.854  0.70 16.06 ?  17  TYR   A CZ   1 
ATOM   426  C  CZ   B TYR   A 1 17  ? 14.632 -16.205 13.771  0.30 13.10 ?  17  TYR   A CZ   1 
ATOM   427  O  OH   A TYR   A 1 17  ? 14.327 -17.189 14.625  0.70 16.43 ?  17  TYR   A OH   1 
ATOM   428  O  OH   B TYR   A 1 17  ? 14.834 -17.397 14.431  0.30 12.78 ?  17  TYR   A OH   1 
ATOM   429  H  H    A TYR   A 1 17  ? 15.253 -12.999 9.291   0.70 15.13 ?  17  TYR   A H    1 
ATOM   430  H  H    B TYR   A 1 17  ? 15.170 -12.772 9.327   0.30 15.65 ?  17  TYR   A H    1 
ATOM   431  H  HA   A TYR   A 1 17  ? 12.659 -13.346 10.011  0.70 14.84 ?  17  TYR   A HA   1 
ATOM   432  H  HA   B TYR   A 1 17  ? 12.645 -13.145 10.245  0.30 15.07 ?  17  TYR   A HA   1 
ATOM   433  H  HB2  A TYR   A 1 17  ? 14.720 -12.028 11.454  0.70 16.45 ?  17  TYR   A HB2  1 
ATOM   434  H  HB2  B TYR   A 1 17  ? 14.715 -11.943 11.767  0.30 15.24 ?  17  TYR   A HB2  1 
ATOM   435  H  HB3  A TYR   A 1 17  ? 13.191 -11.931 11.865  0.70 16.45 ?  17  TYR   A HB3  1 
ATOM   436  H  HB3  B TYR   A 1 17  ? 13.198 -12.003 12.229  0.30 15.24 ?  17  TYR   A HB3  1 
ATOM   437  H  HD1  A TYR   A 1 17  ? 15.871 -14.264 11.695  0.70 19.12 ?  17  TYR   A HD1  1 
ATOM   438  H  HD1  B TYR   A 1 17  ? 16.044 -14.090 11.769  0.30 15.76 ?  17  TYR   A HD1  1 
ATOM   439  H  HD2  A TYR   A 1 17  ? 12.207 -13.633 13.184  0.70 18.21 ?  17  TYR   A HD2  1 
ATOM   440  H  HD2  B TYR   A 1 17  ? 12.386 -13.921 13.379  0.30 15.73 ?  17  TYR   A HD2  1 
ATOM   441  H  HE1  A TYR   A 1 17  ? 16.062 -16.188 12.986  0.70 19.67 ?  17  TYR   A HE1  1 
ATOM   442  H  HE1  B TYR   A 1 17  ? 16.432 -16.101 12.862  0.30 16.23 ?  17  TYR   A HE1  1 
ATOM   443  H  HE2  A TYR   A 1 17  ? 12.390 -15.539 14.467  0.70 18.86 ?  17  TYR   A HE2  1 
ATOM   444  H  HE2  B TYR   A 1 17  ? 12.767 -15.919 14.467  0.30 15.95 ?  17  TYR   A HE2  1 
ATOM   445  H  HH   A TYR   A 1 17  ? 13.563 -17.391 14.920  0.70 19.70 ?  17  TYR   A HH   1 
ATOM   446  H  HH   B TYR   A 1 17  ? 15.586 -17.713 14.233  0.30 15.32 ?  17  TYR   A HH   1 
ATOM   447  N  N    A ILE   A 1 18  ? 11.964 -10.952 9.382   0.70 12.10 ?  18  ILE   A N    1 
ATOM   448  N  N    B ILE   A 1 18  ? 11.959 -10.779 9.732   0.30 11.96 ?  18  ILE   A N    1 
ATOM   449  C  CA   A ILE   A 1 18  ? 11.579 -9.768  8.612   0.70 12.14 ?  18  ILE   A CA   1 
ATOM   450  C  CA   B ILE   A 1 18  ? 11.574 -9.566  9.008   0.30 11.29 ?  18  ILE   A CA   1 
ATOM   451  C  C    A ILE   A 1 18  ? 10.598 -8.909  9.408   0.70 12.89 ?  18  ILE   A C    1 
ATOM   452  C  C    B ILE   A 1 18  ? 10.658 -8.689  9.856   0.30 10.97 ?  18  ILE   A C    1 
ATOM   453  O  O    A ILE   A 1 18  ? 9.770  -9.420  10.165  0.70 13.27 ?  18  ILE   A O    1 
ATOM   454  O  O    B ILE   A 1 18  ? 9.825  -9.186  10.621  0.30 11.24 ?  18  ILE   A O    1 
ATOM   455  C  CB   A ILE   A 1 18  ? 11.030 -10.192 7.229   0.70 12.24 ?  18  ILE   A CB   1 
ATOM   456  C  CB   B ILE   A 1 18  ? 10.935 -9.901  7.644   0.30 10.61 ?  18  ILE   A CB   1 
ATOM   457  C  CG1  A ILE   A 1 18  ? 10.982 -9.005  6.273   0.70 12.07 ?  18  ILE   A CG1  1 
ATOM   458  C  CG1  B ILE   A 1 18  ? 10.953 -8.681  6.719   0.30 11.25 ?  18  ILE   A CG1  1 
ATOM   459  C  CG2  A ILE   A 1 18  ? 9.674  -10.898 7.362   0.70 12.57 ?  18  ILE   A CG2  1 
ATOM   460  C  CG2  B ILE   A 1 18  ? 9.515  -10.431 7.822   0.30 11.18 ?  18  ILE   A CG2  1 
ATOM   461  C  CD1  A ILE   A 1 18  ? 10.781 -9.413  4.840   0.70 13.64 ?  18  ILE   A CD1  1 
ATOM   462  C  CD1  B ILE   A 1 18  ? 10.555 -9.011  5.298   0.30 12.13 ?  18  ILE   A CD1  1 
ATOM   463  H  H    A ILE   A 1 18  ? 11.356 -11.272 9.895   0.70 14.50 ?  18  ILE   A H    1 
ATOM   464  H  H    B ILE   A 1 18  ? 11.324 -11.128 10.201  0.30 14.33 ?  18  ILE   A H    1 
ATOM   465  H  HA   A ILE   A 1 18  ? 12.381 -9.247  8.456   0.70 14.55 ?  18  ILE   A HA   1 
ATOM   466  H  HA   B ILE   A 1 18  ? 12.373 -9.049  8.838   0.30 13.52 ?  18  ILE   A HA   1 
ATOM   467  H  HB   A ILE   A 1 18  ? 11.653 -10.840 6.851   0.70 14.66 ?  18  ILE   A HB   1 
ATOM   468  H  HB   B ILE   A 1 18  ? 11.468 -10.592 7.233   0.30 12.71 ?  18  ILE   A HB   1 
ATOM   469  H  HG12 A ILE   A 1 18  ? 10.254 -8.426  6.528   0.70 14.46 ?  18  ILE   A HG12 1 
ATOM   470  H  HG12 B ILE   A 1 18  ? 10.335 -8.014  7.055   0.30 13.48 ?  18  ILE   A HG12 1 
ATOM   471  H  HG13 A ILE   A 1 18  ? 11.827 -8.526  6.327   0.70 14.46 ?  18  ILE   A HG13 1 
ATOM   472  H  HG13 B ILE   A 1 18  ? 11.854 -8.312  6.698   0.30 13.48 ?  18  ILE   A HG13 1 
ATOM   473  H  HG21 A ILE   A 1 18  ? 9.431  -11.285 6.502   0.70 15.07 ?  18  ILE   A HG21 1 
ATOM   474  H  HG21 B ILE   A 1 18  ? 9.220  -10.822 6.983   0.30 13.39 ?  18  ILE   A HG21 1 
ATOM   475  H  HG22 A ILE   A 1 18  ? 9.744  -11.601 8.026   0.70 15.07 ?  18  ILE   A HG22 1 
ATOM   476  H  HG22 B ILE   A 1 18  ? 9.515  -11.104 8.518   0.30 13.39 ?  18  ILE   A HG22 1 
ATOM   477  H  HG23 A ILE   A 1 18  ? 9.004  -10.252 7.631   0.70 15.07 ?  18  ILE   A HG23 1 
ATOM   478  H  HG23 B ILE   A 1 18  ? 8.926  -9.700  8.067   0.30 13.39 ?  18  ILE   A HG23 1 
ATOM   479  H  HD11 A ILE   A 1 18  ? 10.809 -8.619  4.280   0.70 16.35 ?  18  ILE   A HD11 1 
ATOM   480  H  HD11 B ILE   A 1 18  ? 10.725 -8.242  4.732   0.30 14.53 ?  18  ILE   A HD11 1 
ATOM   481  H  HD12 A ILE   A 1 18  ? 11.483 -10.027 4.578   0.70 16.35 ?  18  ILE   A HD12 1 
ATOM   482  H  HD12 B ILE   A 1 18  ? 11.081 -9.767  4.992   0.30 14.53 ?  18  ILE   A HD12 1 
ATOM   483  H  HD13 A ILE   A 1 18  ? 9.915  -9.844  4.753   0.70 16.35 ?  18  ILE   A HD13 1 
ATOM   484  H  HD13 B ILE   A 1 18  ? 9.613  -9.236  5.279   0.30 14.53 ?  18  ILE   A HD13 1 
ATOM   485  N  N    A LYS   A 1 19  ? 10.681 -7.589  9.207   0.70 12.59 ?  19  LYS   A N    1 
ATOM   486  N  N    B LYS   A 1 19  ? 10.811 -7.371  9.697   0.30 11.03 ?  19  LYS   A N    1 
ATOM   487  C  CA   A LYS   A 1 19  ? 9.865  -6.628  9.943   0.70 13.19 ?  19  LYS   A CA   1 
ATOM   488  C  CA   B LYS   A 1 19  ? 10.030 -6.395  10.444  0.30 12.43 ?  19  LYS   A CA   1 
ATOM   489  C  C    A LYS   A 1 19  ? 9.696  -5.364  9.109   0.70 13.09 ?  19  LYS   A C    1 
ATOM   490  C  C    B LYS   A 1 19  ? 9.830  -5.162  9.577   0.30 12.85 ?  19  LYS   A C    1 
ATOM   491  O  O    A LYS   A 1 19  ? 10.589 -4.995  8.345   0.70 13.00 ?  19  LYS   A O    1 
ATOM   492  O  O    B LYS   A 1 19  ? 10.741 -4.753  8.854   0.30 13.42 ?  19  LYS   A O    1 
ATOM   493  C  CB   A LYS   A 1 19  ? 10.555 -6.275  11.269  0.70 15.09 ?  19  LYS   A CB   1 
ATOM   494  C  CB   B LYS   A 1 19  ? 10.756 -6.002  11.737  0.30 13.46 ?  19  LYS   A CB   1 
ATOM   495  C  CG   A LYS   A 1 19  ? 9.828  -5.285  12.173  0.70 16.52 ?  19  LYS   A CG   1 
ATOM   496  C  CG   B LYS   A 1 19  ? 9.955  -5.138  12.691  0.30 14.93 ?  19  LYS   A CG   1 
ATOM   497  C  CD   A LYS   A 1 19  ? 10.705 -4.982  13.385  0.70 18.13 ?  19  LYS   A CD   1 
ATOM   498  C  CD   B LYS   A 1 19  ? 10.804 -4.759  13.893  0.30 16.50 ?  19  LYS   A CD   1 
ATOM   499  C  CE   A LYS   A 1 19  ? 10.035 -4.075  14.398  0.70 19.03 ?  19  LYS   A CE   1 
ATOM   500  C  CE   B LYS   A 1 19  ? 10.068 -3.834  14.839  0.30 17.31 ?  19  LYS   A CE   1 
ATOM   501  N  NZ   A LYS   A 1 19  ? 10.929 -3.838  15.571  0.70 19.34 ?  19  LYS   A NZ   1 
ATOM   502  N  NZ   B LYS   A 1 19  ? 10.922 -3.475  16.001  0.30 17.87 ?  19  LYS   A NZ   1 
ATOM   503  H  H    A LYS   A 1 19  ? 11.218 -7.232  8.638   0.70 15.08 ?  19  LYS   A H    1 
ATOM   504  H  H    B LYS   A 1 19  ? 11.383 -7.008  9.154   0.30 13.21 ?  19  LYS   A H    1 
ATOM   505  H  HA   A LYS   A 1 19  ? 8.993  -7.019  10.125  0.70 15.80 ?  19  LYS   A HA   1 
ATOM   506  H  HA   B LYS   A 1 19  ? 9.167  -6.765  10.673  0.30 14.90 ?  19  LYS   A HA   1 
ATOM   507  H  HB2  A LYS   A 1 19  ? 10.670 -7.096  11.777  0.70 18.09 ?  19  LYS   A HB2  1 
ATOM   508  H  HB2  B LYS   A 1 19  ? 10.990 -6.809  12.220  0.30 16.13 ?  19  LYS   A HB2  1 
ATOM   509  H  HB3  A LYS   A 1 19  ? 11.422 -5.900  11.065  0.70 18.09 ?  19  LYS   A HB3  1 
ATOM   510  H  HB3  B LYS   A 1 19  ? 11.562 -5.511  11.512  0.30 16.13 ?  19  LYS   A HB3  1 
ATOM   511  H  HG2  A LYS   A 1 19  ? 9.664  -4.459  11.691  0.70 19.80 ?  19  LYS   A HG2  1 
ATOM   512  H  HG2  B LYS   A 1 19  ? 9.679  -4.325  12.243  0.30 17.90 ?  19  LYS   A HG2  1 
ATOM   513  H  HG3  A LYS   A 1 19  ? 8.992  -5.673  12.480  0.70 19.80 ?  19  LYS   A HG3  1 
ATOM   514  H  HG3  B LYS   A 1 19  ? 9.182  -5.633  13.007  0.30 17.90 ?  19  LYS   A HG3  1 
ATOM   515  H  HD2  A LYS   A 1 19  ? 10.924 -5.815  13.832  0.70 21.73 ?  19  LYS   A HD2  1 
ATOM   516  H  HD2  B LYS   A 1 19  ? 11.038 -5.564  14.382  0.30 19.77 ?  19  LYS   A HD2  1 
ATOM   517  H  HD3  A LYS   A 1 19  ? 11.517 -4.545  13.085  0.70 21.73 ?  19  LYS   A HD3  1 
ATOM   518  H  HD3  B LYS   A 1 19  ? 11.606 -4.307  13.588  0.30 19.77 ?  19  LYS   A HD3  1 
ATOM   519  H  HE2  A LYS   A 1 19  ? 9.840  -3.217  13.987  0.70 22.81 ?  19  LYS   A HE2  1 
ATOM   520  H  HE2  B LYS   A 1 19  ? 9.830  -3.019  14.370  0.30 20.75 ?  19  LYS   A HE2  1 
ATOM   521  H  HE3  A LYS   A 1 19  ? 9.218  -4.489  14.716  0.70 22.81 ?  19  LYS   A HE3  1 
ATOM   522  H  HE3  B LYS   A 1 19  ? 9.272  -4.279  15.169  0.30 20.75 ?  19  LYS   A HE3  1 
ATOM   523  H  HZ1  A LYS   A 1 19  ? 10.520 -3.319  16.166  0.70 23.18 ?  19  LYS   A HZ1  1 
ATOM   524  H  HZ1  B LYS   A 1 19  ? 10.473 -2.943  16.554  0.30 21.42 ?  19  LYS   A HZ1  1 
ATOM   525  H  HZ2  A LYS   A 1 19  ? 11.134 -4.614  15.957  0.70 23.18 ?  19  LYS   A HZ2  1 
ATOM   526  H  HZ2  B LYS   A 1 19  ? 11.163 -4.212  16.440  0.30 21.42 ?  19  LYS   A HZ2  1 
ATOM   527  H  HZ3  A LYS   A 1 19  ? 11.679 -3.441  15.306  0.70 23.18 ?  19  LYS   A HZ3  1 
ATOM   528  H  HZ3  B LYS   A 1 19  ? 11.654 -3.053  15.722  0.30 21.42 ?  19  LYS   A HZ3  1 
ATOM   529  N  N    A ASN   A 1 20  ? 8.535  -4.711  9.241   0.70 13.98 ?  20  ASN   A N    1 
ATOM   530  N  N    B ASN   A 1 20  ? 8.634  -4.579  9.645   0.30 13.82 ?  20  ASN   A N    1 
ATOM   531  C  CA   A ASN   A 1 20  ? 8.344  -3.367  8.691   0.70 16.05 ?  20  ASN   A CA   1 
ATOM   532  C  CA   B ASN   A 1 20  ? 8.336  -3.326  8.949   0.30 15.21 ?  20  ASN   A CA   1 
ATOM   533  C  C    A ASN   A 1 20  ? 8.981  -2.381  9.663   0.70 16.97 ?  20  ASN   A C    1 
ATOM   534  C  C    B ASN   A 1 20  ? 8.886  -2.178  9.784   0.30 15.76 ?  20  ASN   A C    1 
ATOM   535  O  O    A ASN   A 1 20  ? 8.472  -2.175  10.771  0.70 18.01 ?  20  ASN   A O    1 
ATOM   536  O  O    B ASN   A 1 20  ? 8.217  -1.655  10.678  0.30 16.45 ?  20  ASN   A O    1 
ATOM   537  C  CB   A ASN   A 1 20  ? 6.856  -3.081  8.478   0.70 16.91 ?  20  ASN   A CB   1 
ATOM   538  C  CB   B ASN   A 1 20  ? 6.833  -3.180  8.746   0.30 15.98 ?  20  ASN   A CB   1 
ATOM   539  C  CG   A ASN   A 1 20  ? 6.562  -1.622  8.124   0.70 18.79 ?  20  ASN   A CG   1 
ATOM   540  C  CG   B ASN   A 1 20  ? 6.452  -1.890  8.034   0.30 17.38 ?  20  ASN   A CG   1 
ATOM   541  O  OD1  A ASN   A 1 20  ? 5.580  -1.060  8.601   0.70 22.47 ?  20  ASN   A OD1  1 
ATOM   542  O  OD1  B ASN   A 1 20  ? 5.436  -1.278  8.352   0.30 18.50 ?  20  ASN   A OD1  1 
ATOM   543  N  ND2  A ASN   A 1 20  ? 7.394  -1.016  7.280   0.70 17.87 ?  20  ASN   A ND2  1 
ATOM   544  N  ND2  B ASN   A 1 20  ? 7.263  -1.472  7.070   0.30 17.98 ?  20  ASN   A ND2  1 
ATOM   545  H  H    A ASN   A 1 20  ? 7.841  -5.035  9.640   0.70 16.76 ?  20  ASN   A H    1 
ATOM   546  H  H    B ASN   A 1 20  ? 7.971  -4.905  10.080  0.30 16.56 ?  20  ASN   A H    1 
ATOM   547  H  HA   A ASN   A 1 20  ? 8.795  -3.306  7.838   0.70 19.24 ?  20  ASN   A HA   1 
ATOM   548  H  HA   B ASN   A 1 20  ? 8.782  -3.328  8.086   0.30 18.24 ?  20  ASN   A HA   1 
ATOM   549  H  HB2  A ASN   A 1 20  ? 6.530  -3.632  7.749   0.70 20.28 ?  20  ASN   A HB2  1 
ATOM   550  H  HB2  B ASN   A 1 20  ? 6.509  -3.924  8.227   0.30 19.16 ?  20  ASN   A HB2  1 
ATOM   551  H  HB3  A ASN   A 1 20  ? 6.374  -3.294  9.293   0.70 20.28 ?  20  ASN   A HB3  1 
ATOM   552  H  HB3  B ASN   A 1 20  ? 6.405  -3.184  9.615   0.30 19.16 ?  20  ASN   A HB3  1 
ATOM   553  H  HD21 A ASN   A 1 20  ? 7.262  -0.196  7.059   0.70 21.42 ?  20  ASN   A HD21 1 
ATOM   554  H  HD21 B ASN   A 1 20  ? 7.081  -0.748  6.647   0.30 21.55 ?  20  ASN   A HD21 1 
ATOM   555  H  HD22 A ASN   A 1 20  ? 8.069  -1.443  6.960   0.70 21.42 ?  20  ASN   A HD22 1 
ATOM   556  H  HD22 B ASN   A 1 20  ? 7.967  -1.922  6.870   0.30 21.55 ?  20  ASN   A HD22 1 
ATOM   557  N  N    A ALA   A 1 21  ? 10.108 -1.790  9.268   0.70 17.16 ?  21  ALA   A N    1 
ATOM   558  N  N    B ALA   A 1 21  ? 10.116 -1.767  9.480   0.30 16.09 ?  21  ALA   A N    1 
ATOM   559  C  CA   A ALA   A 1 21  ? 10.823 -0.911  10.181  0.70 16.80 ?  21  ALA   A CA   1 
ATOM   560  C  CA   B ALA   A 1 21  ? 10.757 -0.708  10.244  0.30 16.10 ?  21  ALA   A CA   1 
ATOM   561  C  C    A ALA   A 1 21  ? 11.766 -0.005  9.410   0.70 16.08 ?  21  ALA   A C    1 
ATOM   562  C  C    B ALA   A 1 21  ? 11.876 -0.096  9.417   0.30 15.17 ?  21  ALA   A C    1 
ATOM   563  O  O    A ALA   A 1 21  ? 12.223 -0.343  8.314   0.70 16.12 ?  21  ALA   A O    1 
ATOM   564  O  O    B ALA   A 1 21  ? 12.433 -0.741  8.526   0.30 15.33 ?  21  ALA   A O    1 
ATOM   565  C  CB   A ALA   A 1 21  ? 11.615 -1.708  11.221  0.70 17.21 ?  21  ALA   A CB   1 
ATOM   566  C  CB   B ALA   A 1 21  ? 11.302 -1.232  11.579  0.30 17.00 ?  21  ALA   A CB   1 
ATOM   567  H  H    A ALA   A 1 21  ? 10.468 -1.883  8.493   0.70 20.57 ?  21  ALA   A H    1 
ATOM   568  H  H    B ALA   A 1 21  ? 10.597 -2.077  8.836   0.30 19.29 ?  21  ALA   A H    1 
ATOM   569  H  HA   A ALA   A 1 21  ? 10.178 -0.355  10.650  0.70 20.14 ?  21  ALA   A HA   1 
ATOM   570  H  HA   B ALA   A 1 21  ? 10.109 -0.015  10.435  0.30 19.30 ?  21  ALA   A HA   1 
ATOM   571  H  HB1  A ALA   A 1 21  ? 12.039 -1.086  11.829  0.70 20.63 ?  21  ALA   A HB1  1 
ATOM   572  H  HB1  B ALA   A 1 21  ? 11.719 -0.499  12.060  0.30 20.38 ?  21  ALA   A HB1  1 
ATOM   573  H  HB2  A ALA   A 1 21  ? 11.001 -2.283  11.710  0.70 20.63 ?  21  ALA   A HB2  1 
ATOM   574  H  HB2  B ALA   A 1 21  ? 10.567 -1.593  12.101  0.30 20.38 ?  21  ALA   A HB2  1 
ATOM   575  H  HB3  A ALA   A 1 21  ? 12.280 -2.244  10.767  0.70 20.63 ?  21  ALA   A HB3  1 
ATOM   576  H  HB3  B ALA   A 1 21  ? 11.956 -1.927  11.405  0.30 20.38 ?  21  ALA   A HB3  1 
ATOM   577  N  N    A ASP   A 1 22  ? 12.035 1.154   10.010  0.70 16.54 ?  22  ASP   A N    1 
ATOM   578  N  N    B ASP   A 1 22  ? 12.170 1.168   9.711   0.30 14.81 ?  22  ASP   A N    1 
ATOM   579  C  CA   A ASP   A 1 22  ? 13.073 2.073   9.560   0.70 16.44 ?  22  ASP   A CA   1 
ATOM   580  C  CA   B ASP   A 1 22  ? 13.344 1.834   9.165   0.30 14.85 ?  22  ASP   A CA   1 
ATOM   581  C  C    A ASP   A 1 22  ? 14.398 1.588   10.136  0.70 15.21 ?  22  ASP   A C    1 
ATOM   582  C  C    B ASP   A 1 22  ? 14.592 1.213   9.782   0.30 13.75 ?  22  ASP   A C    1 
ATOM   583  O  O    A ASP   A 1 22  ? 14.587 1.590   11.356  0.70 15.80 ?  22  ASP   A O    1 
ATOM   584  O  O    B ASP   A 1 22  ? 14.699 1.105   11.007  0.30 13.77 ?  22  ASP   A O    1 
ATOM   585  C  CB   A ASP   A 1 22  ? 12.737 3.473   10.063  0.70 18.51 ?  22  ASP   A CB   1 
ATOM   586  C  CB   B ASP   A 1 22  ? 13.266 3.320   9.525   0.30 15.69 ?  22  ASP   A CB   1 
ATOM   587  C  CG   A ASP   A 1 22  ? 13.741 4.522   9.616   0.70 20.88 ?  22  ASP   A CG   1 
ATOM   588  C  CG   B ASP   A 1 22  ? 14.266 4.171   8.775   0.30 16.16 ?  22  ASP   A CG   1 
ATOM   589  O  OD1  A ASP   A 1 22  ? 14.874 4.172   9.240   0.70 21.57 ?  22  ASP   A OD1  1 
ATOM   590  O  OD1  B ASP   A 1 22  ? 15.308 3.635   8.349   0.30 15.59 ?  22  ASP   A OD1  1 
ATOM   591  O  OD2  A ASP   A 1 22  ? 13.392 5.720   9.653   0.70 22.66 -1 22  ASP   A OD2  1 
ATOM   592  O  OD2  B ASP   A 1 22  ? 14.017 5.388   8.627   0.30 17.09 -1 22  ASP   A OD2  1 
ATOM   593  H  H    A ASP   A 1 22  ? 11.594 1.443   10.695  0.70 19.83 ?  22  ASP   A H    1 
ATOM   594  H  H    B ASP   A 1 22  ? 11.690 1.666   10.221  0.30 17.75 ?  22  ASP   A H    1 
ATOM   595  H  HA   A ASP   A 1 22  ? 13.119 2.076   8.591   0.70 19.71 ?  22  ASP   A HA   1 
ATOM   596  H  HA   B ASP   A 1 22  ? 13.371 1.730   8.199   0.30 17.79 ?  22  ASP   A HA   1 
ATOM   597  H  HB2  A ASP   A 1 22  ? 11.862 3.731   9.725   0.70 22.19 ?  22  ASP   A HB2  1 
ATOM   598  H  HB2  B ASP   A 1 22  ? 12.382 3.649   9.316   0.30 18.81 ?  22  ASP   A HB2  1 
ATOM   599  H  HB3  A ASP   A 1 22  ? 12.719 3.461   11.035  0.70 22.19 ?  22  ASP   A HB3  1 
ATOM   600  H  HB3  B ASP   A 1 22  ? 13.450 3.422   10.470  0.30 18.81 ?  22  ASP   A HB3  1 
ATOM   601  N  N    A ILE   A 1 23  ? 15.314 1.169   9.258   0.70 14.52 ?  23  ILE   A N    1 
ATOM   602  N  N    B ILE   A 1 23  ? 15.536 0.786   8.936   0.30 13.39 ?  23  ILE   A N    1 
ATOM   603  C  CA   A ILE   A 1 23  ? 16.567 0.556   9.698   0.70 14.03 ?  23  ILE   A CA   1 
ATOM   604  C  CA   B ILE   A 1 23  ? 16.752 0.157   9.452   0.30 12.94 ?  23  ILE   A CA   1 
ATOM   605  C  C    A ILE   A 1 23  ? 17.372 1.500   10.582  0.70 14.51 ?  23  ILE   A C    1 
ATOM   606  C  C    B ILE   A 1 23  ? 17.501 1.117   10.362  0.30 13.95 ?  23  ILE   A C    1 
ATOM   607  O  O    A ILE   A 1 23  ? 18.093 1.051   11.482  0.70 15.05 ?  23  ILE   A O    1 
ATOM   608  O  O    B ILE   A 1 23  ? 18.169 0.694   11.313  0.30 13.35 ?  23  ILE   A O    1 
ATOM   609  C  CB   A ILE   A 1 23  ? 17.370 0.042   8.483   0.70 13.54 ?  23  ILE   A CB   1 
ATOM   610  C  CB   B ILE   A 1 23  ? 17.642 -0.381  8.309   0.30 12.18 ?  23  ILE   A CB   1 
ATOM   611  C  CG1  A ILE   A 1 23  ? 18.519 -0.863  8.936   0.70 13.74 ?  23  ILE   A CG1  1 
ATOM   612  C  CG1  B ILE   A 1 23  ? 18.715 -1.325  8.869   0.30 11.32 ?  23  ILE   A CG1  1 
ATOM   613  C  CG2  A ILE   A 1 23  ? 17.865 1.207   7.624   0.70 13.95 ?  23  ILE   A CG2  1 
ATOM   614  C  CG2  B ILE   A 1 23  ? 18.288 0.760   7.532   0.30 12.02 ?  23  ILE   A CG2  1 
ATOM   615  C  CD1  A ILE   A 1 23  ? 19.212 -1.568  7.790   0.70 14.38 ?  23  ILE   A CD1  1 
ATOM   616  C  CD1  B ILE   A 1 23  ? 19.583 -1.995  7.808   0.30 11.35 ?  23  ILE   A CD1  1 
ATOM   617  H  H    A ILE   A 1 23  ? 15.223 1.222   8.408   0.70 17.40 ?  23  ILE   A H    1 
ATOM   618  H  H    B ILE   A 1 23  ? 15.499 0.845   8.086   0.30 16.05 ?  23  ILE   A H    1 
ATOM   619  H  HA   A ILE   A 1 23  ? 16.348 -0.216  10.240  0.70 16.82 ?  23  ILE   A HA   1 
ATOM   620  H  HA   B ILE   A 1 23  ? 16.491 -0.605  9.990   0.30 15.51 ?  23  ILE   A HA   1 
ATOM   621  H  HB   A ILE   A 1 23  ? 16.770 -0.490  7.939   0.70 16.23 ?  23  ILE   A HB   1 
ATOM   622  H  HB   B ILE   A 1 23  ? 17.086 -0.889  7.700   0.30 14.60 ?  23  ILE   A HB   1 
ATOM   623  H  HG12 A ILE   A 1 23  ? 19.181 -0.325  9.399   0.70 16.47 ?  23  ILE   A HG12 1 
ATOM   624  H  HG12 B ILE   A 1 23  ? 19.304 -0.823  9.453   0.30 13.56 ?  23  ILE   A HG12 1 
ATOM   625  H  HG13 A ILE   A 1 23  ? 18.167 -1.541  9.534   0.70 16.47 ?  23  ILE   A HG13 1 
ATOM   626  H  HG13 B ILE   A 1 23  ? 18.280 -2.031  9.375   0.30 13.56 ?  23  ILE   A HG13 1 
ATOM   627  H  HG21 A ILE   A 1 23  ? 18.220 0.857   6.792   0.70 16.72 ?  23  ILE   A HG21 1 
ATOM   628  H  HG21 B ILE   A 1 23  ? 18.670 0.406   6.710   0.30 14.40 ?  23  ILE   A HG21 1 
ATOM   629  H  HG22 A ILE   A 1 23  ? 17.117 1.800   7.436   0.70 16.72 ?  23  ILE   A HG22 1 
ATOM   630  H  HG22 B ILE   A 1 23  ? 17.611 1.419   7.323   0.30 14.40 ?  23  ILE   A HG22 1 
ATOM   631  H  HG23 A ILE   A 1 23  ? 18.553 1.688   8.104   0.70 16.72 ?  23  ILE   A HG23 1 
ATOM   632  H  HG23 B ILE   A 1 23  ? 18.987 1.159   8.072   0.30 14.40 ?  23  ILE   A HG23 1 
ATOM   633  H  HD11 A ILE   A 1 23  ? 19.868 -2.181  8.152   0.70 17.24 ?  23  ILE   A HD11 1 
ATOM   634  H  HD11 B ILE   A 1 23  ? 20.174 -2.637  8.240   0.30 13.59 ?  23  ILE   A HD11 1 
ATOM   635  H  HD12 A ILE   A 1 23  ? 18.549 -2.053  7.276   0.70 17.24 ?  23  ILE   A HD12 1 
ATOM   636  H  HD12 B ILE   A 1 23  ? 19.012 -2.452  7.173   0.30 13.59 ?  23  ILE   A HD12 1 
ATOM   637  H  HD13 A ILE   A 1 23  ? 19.646 -0.905  7.232   0.70 17.24 ?  23  ILE   A HD13 1 
ATOM   638  H  HD13 B ILE   A 1 23  ? 20.111 -1.319  7.356   0.30 13.59 ?  23  ILE   A HD13 1 
ATOM   639  N  N    A VAL   A 1 24  ? 17.264 2.812   10.352  0.70 14.67 ?  24  VAL   A N    1 
ATOM   640  N  N    B VAL   A 1 24  ? 17.393 2.420   10.096  0.30 15.09 ?  24  VAL   A N    1 
ATOM   641  C  CA   A VAL   A 1 24  ? 17.950 3.775   11.213  0.70 16.20 ?  24  VAL   A CA   1 
ATOM   642  C  CA   B VAL   A 1 24  ? 18.036 3.416   10.945  0.30 16.20 ?  24  VAL   A CA   1 
ATOM   643  C  C    A VAL   A 1 24  ? 17.423 3.676   12.638  0.70 16.87 ?  24  VAL   A C    1 
ATOM   644  C  C    B VAL   A 1 24  ? 17.419 3.404   12.337  0.30 16.94 ?  24  VAL   A C    1 
ATOM   645  O  O    A VAL   A 1 24  ? 18.193 3.578   13.604  0.70 17.37 ?  24  VAL   A O    1 
ATOM   646  O  O    B VAL   A 1 24  ? 18.130 3.452   13.349  0.30 17.47 ?  24  VAL   A O    1 
ATOM   647  C  CB   A VAL   A 1 24  ? 17.794 5.201   10.654  0.70 17.00 ?  24  VAL   A CB   1 
ATOM   648  C  CB   B VAL   A 1 24  ? 17.945 4.803   10.283  0.30 16.64 ?  24  VAL   A CB   1 
ATOM   649  C  CG1  A VAL   A 1 24  ? 18.278 6.238   11.670  0.70 17.60 ?  24  VAL   A CG1  1 
ATOM   650  C  CG1  B VAL   A 1 24  ? 18.594 5.860   11.160  0.30 17.31 ?  24  VAL   A CG1  1 
ATOM   651  C  CG2  A VAL   A 1 24  ? 18.536 5.341   9.335   0.70 17.29 ?  24  VAL   A CG2  1 
ATOM   652  C  CG2  B VAL   A 1 24  ? 18.585 4.770   8.903   0.30 16.23 ?  24  VAL   A CG2  1 
ATOM   653  H  H    A VAL   A 1 24  ? 16.813 3.165   9.709   0.70 17.59 ?  24  VAL   A H    1 
ATOM   654  H  H    B VAL   A 1 24  ? 16.954 2.747   9.437   0.30 18.09 ?  24  VAL   A H    1 
ATOM   655  H  HA   A VAL   A 1 24  ? 18.897 3.567   11.228  0.70 19.42 ?  24  VAL   A HA   1 
ATOM   656  H  HA   B VAL   A 1 24  ? 18.975 3.194   11.036  0.30 19.41 ?  24  VAL   A HA   1 
ATOM   657  H  HB   A VAL   A 1 24  ? 16.854 5.371   10.479  0.70 20.38 ?  24  VAL   A HB   1 
ATOM   658  H  HB   B VAL   A 1 24  ? 17.011 5.039   10.171  0.30 19.94 ?  24  VAL   A HB   1 
ATOM   659  H  HG11 A VAL   A 1 24  ? 18.434 7.077   11.210  0.70 21.10 ?  24  VAL   A HG11 1 
ATOM   660  H  HG11 B VAL   A 1 24  ? 18.689 6.677   10.648  0.30 20.76 ?  24  VAL   A HG11 1 
ATOM   661  H  HG12 A VAL   A 1 24  ? 17.598 6.354   12.350  0.70 21.10 ?  24  VAL   A HG12 1 
ATOM   662  H  HG12 B VAL   A 1 24  ? 18.029 6.019   11.933  0.30 20.76 ?  24  VAL   A HG12 1 
ATOM   663  H  HG13 A VAL   A 1 24  ? 19.103 5.921   12.070  0.70 21.10 ?  24  VAL   A HG13 1 
ATOM   664  H  HG13 B VAL   A 1 24  ? 19.464 5.542   11.443  0.30 20.76 ?  24  VAL   A HG13 1 
ATOM   665  H  HG21 A VAL   A 1 24  ? 18.345 6.213   8.951   0.70 20.72 ?  24  VAL   A HG21 1 
ATOM   666  H  HG21 B VAL   A 1 24  ? 18.626 5.673   8.552   0.30 19.46 ?  24  VAL   A HG21 1 
ATOM   667  H  HG22 A VAL   A 1 24  ? 19.491 5.259   9.498   0.70 20.72 ?  24  VAL   A HG22 1 
ATOM   668  H  HG22 B VAL   A 1 24  ? 19.481 4.406   8.981   0.30 19.46 ?  24  VAL   A HG22 1 
ATOM   669  H  HG23 A VAL   A 1 24  ? 18.245 4.644   8.727   0.70 20.72 ?  24  VAL   A HG23 1 
ATOM   670  H  HG23 B VAL   A 1 24  ? 18.051 4.211   8.318   0.30 19.46 ?  24  VAL   A HG23 1 
ATOM   671  N  N    A GLU   A 1 25  ? 16.098 3.717   12.788  0.70 17.60 ?  25  GLU   A N    1 
ATOM   672  N  N    B GLU   A 1 25  ? 16.087 3.331   12.413  0.30 17.45 ?  25  GLU   A N    1 
ATOM   673  C  CA   A GLU   A 1 25  ? 15.503 3.647   14.117  0.70 18.94 ?  25  GLU   A CA   1 
ATOM   674  C  CA   B GLU   A 1 25  ? 15.421 3.290   13.712  0.30 18.53 ?  25  GLU   A CA   1 
ATOM   675  C  C    A GLU   A 1 25  ? 15.738 2.284   14.757  0.70 18.07 ?  25  GLU   A C    1 
ATOM   676  C  C    B GLU   A 1 25  ? 15.676 1.966   14.425  0.30 18.32 ?  25  GLU   A C    1 
ATOM   677  O  O    A GLU   A 1 25  ? 15.973 2.194   15.967  0.70 18.65 ?  25  GLU   A O    1 
ATOM   678  O  O    B GLU   A 1 25  ? 15.843 1.937   15.650  0.30 18.67 ?  25  GLU   A O    1 
ATOM   679  C  CB   A GLU   A 1 25  ? 14.012 3.981   14.035  0.70 21.46 ?  25  GLU   A CB   1 
ATOM   680  C  CB   B GLU   A 1 25  ? 13.923 3.551   13.540  0.30 19.98 ?  25  GLU   A CB   1 
ATOM   681  C  CG   A GLU   A 1 25  ? 13.749 5.437   13.668  0.70 24.56 ?  25  GLU   A CG   1 
ATOM   682  C  CG   B GLU   A 1 25  ? 13.605 4.931   12.979  0.30 21.75 ?  25  GLU   A CG   1 
ATOM   683  C  CD   A GLU   A 1 25  ? 14.534 6.411   14.537  0.70 27.07 ?  25  GLU   A CD   1 
ATOM   684  C  CD   B GLU   A 1 25  ? 14.069 6.047   13.889  0.30 23.32 ?  25  GLU   A CD   1 
ATOM   685  O  OE1  A GLU   A 1 25  ? 14.592 6.204   15.769  0.70 27.72 ?  25  GLU   A OE1  1 
ATOM   686  O  OE1  B GLU   A 1 25  ? 14.026 5.860   15.124  0.30 23.89 ?  25  GLU   A OE1  1 
ATOM   687  O  OE2  A GLU   A 1 25  ? 15.116 7.368   13.984  0.70 28.61 -1 25  GLU   A OE2  1 
ATOM   688  O  OE2  B GLU   A 1 25  ? 14.479 7.105   13.369  0.30 23.96 -1 25  GLU   A OE2  1 
ATOM   689  H  H    A GLU   A 1 25  ? 15.533 3.800   12.143  0.70 21.11 ?  25  GLU   A H    1 
ATOM   690  H  H    B GLU   A 1 25  ? 15.559 3.309   11.735  0.30 20.92 ?  25  GLU   A H    1 
ATOM   691  H  HA   A GLU   A 1 25  ? 15.928 4.305   14.686  0.70 22.70 ?  25  GLU   A HA   1 
ATOM   692  H  HA   B GLU   A 1 25  ? 15.783 3.998   14.265  0.30 22.22 ?  25  GLU   A HA   1 
ATOM   693  H  HB2  A GLU   A 1 25  ? 13.595 3.426   13.354  0.70 25.73 ?  25  GLU   A HB2  1 
ATOM   694  H  HB2  B GLU   A 1 25  ? 13.556 2.894   12.929  0.30 23.95 ?  25  GLU   A HB2  1 
ATOM   695  H  HB3  A GLU   A 1 25  ? 13.597 3.815   14.895  0.70 25.73 ?  25  GLU   A HB3  1 
ATOM   696  H  HB3  B GLU   A 1 25  ? 13.492 3.477   14.405  0.30 23.95 ?  25  GLU   A HB3  1 
ATOM   697  H  HG2  A GLU   A 1 25  ? 14.014 5.582   12.747  0.70 29.45 ?  25  GLU   A HG2  1 
ATOM   698  H  HG2  B GLU   A 1 25  ? 14.048 5.039   12.122  0.30 26.08 ?  25  GLU   A HG2  1 
ATOM   699  H  HG3  A GLU   A 1 25  ? 12.801 5.624   13.775  0.70 29.45 ?  25  GLU   A HG3  1 
ATOM   700  H  HG3  B GLU   A 1 25  ? 12.646 5.020   12.871  0.30 26.08 ?  25  GLU   A HG3  1 
ATOM   701  N  N    A GLU   A 1 26  ? 15.691 1.214   13.960  0.70 17.23 ?  26  GLU   A N    1 
ATOM   702  N  N    B GLU   A 1 26  ? 15.711 0.858   13.679  0.30 18.12 ?  26  GLU   A N    1 
ATOM   703  C  CA   A GLU   A 1 26  ? 15.988 -0.113  14.492  0.70 16.71 ?  26  GLU   A CA   1 
ATOM   704  C  CA   B GLU   A 1 26  ? 16.063 -0.423  14.284  0.30 18.37 ?  26  GLU   A CA   1 
ATOM   705  C  C    A GLU   A 1 26  ? 17.414 -0.182  15.026  0.70 15.67 ?  26  GLU   A C    1 
ATOM   706  C  C    B GLU   A 1 26  ? 17.490 -0.409  14.817  0.30 18.17 ?  26  GLU   A C    1 
ATOM   707  O  O    A GLU   A 1 26  ? 17.657 -0.691  16.126  0.70 16.00 ?  26  GLU   A O    1 
ATOM   708  O  O    B GLU   A 1 26  ? 17.779 -1.008  15.859  0.30 17.93 ?  26  GLU   A O    1 
ATOM   709  C  CB   A GLU   A 1 26  ? 15.793 -1.166  13.401  0.70 17.99 ?  26  GLU   A CB   1 
ATOM   710  C  CB   B GLU   A 1 26  ? 15.886 -1.552  13.268  0.30 19.02 ?  26  GLU   A CB   1 
ATOM   711  C  CG   A GLU   A 1 26  ? 14.382 -1.685  13.245  0.70 21.63 ?  26  GLU   A CG   1 
ATOM   712  C  CG   B GLU   A 1 26  ? 14.444 -1.970  13.051  0.30 19.53 ?  26  GLU   A CG   1 
ATOM   713  C  CD   A GLU   A 1 26  ? 13.925 -2.524  14.425  0.70 24.15 ?  26  GLU   A CD   1 
ATOM   714  C  CD   B GLU   A 1 26  ? 13.765 -2.450  14.310  0.30 19.74 ?  26  GLU   A CD   1 
ATOM   715  O  OE1  A GLU   A 1 26  ? 14.407 -3.668  14.609  0.70 24.11 ?  26  GLU   A OE1  1 
ATOM   716  O  OE1  B GLU   A 1 26  ? 14.346 -3.295  15.022  0.30 20.32 ?  26  GLU   A OE1  1 
ATOM   717  O  OE2  A GLU   A 1 26  ? 13.075 -2.022  15.175  0.70 25.11 -1 26  GLU   A OE2  1 
ATOM   718  O  OE2  B GLU   A 1 26  ? 12.649 -1.965  14.585  0.30 18.40 -1 26  GLU   A OE2  1 
ATOM   719  H  H    A GLU   A 1 26  ? 15.497 1.238   13.122  0.70 20.65 ?  26  GLU   A H    1 
ATOM   720  H  H    B GLU   A 1 26  ? 15.534 0.822   12.840  0.30 21.72 ?  26  GLU   A H    1 
ATOM   721  H  HA   A GLU   A 1 26  ? 15.377 -0.302  15.217  0.70 20.04 ?  26  GLU   A HA   1 
ATOM   722  H  HA   B GLU   A 1 26  ? 15.473 -0.593  15.032  0.30 22.02 ?  26  GLU   A HA   1 
ATOM   723  H  HB2  A GLU   A 1 26  ? 16.059 -0.776  12.551  0.70 21.57 ?  26  GLU   A HB2  1 
ATOM   724  H  HB2  B GLU   A 1 26  ? 16.236 -1.258  12.408  0.30 22.81 ?  26  GLU   A HB2  1 
ATOM   725  H  HB3  A GLU   A 1 26  ? 16.365 -1.918  13.606  0.70 21.57 ?  26  GLU   A HB3  1 
ATOM   726  H  HB3  B GLU   A 1 26  ? 16.380 -2.330  13.570  0.30 22.81 ?  26  GLU   A HB3  1 
ATOM   727  H  HG2  A GLU   A 1 26  ? 13.781 -0.926  13.159  0.70 25.93 ?  26  GLU   A HG2  1 
ATOM   728  H  HG2  B GLU   A 1 26  ? 13.940 -1.209  12.736  0.30 23.41 ?  26  GLU   A HG2  1 
ATOM   729  H  HG3  A GLU   A 1 26  ? 14.336 -2.235  12.449  0.70 25.93 ?  26  GLU   A HG3  1 
ATOM   730  H  HG3  B GLU   A 1 26  ? 14.417 -2.689  12.405  0.30 23.41 ?  26  GLU   A HG3  1 
ATOM   731  N  N    A ALA   A 1 27  ? 18.378 0.312   14.247  0.70 14.75 ?  27  ALA   A N    1 
ATOM   732  N  N    B ALA   A 1 27  ? 18.400 0.263   14.111  0.30 18.32 ?  27  ALA   A N    1 
ATOM   733  C  CA   A ALA   A 1 27  ? 19.769 0.266   14.684  0.70 15.51 ?  27  ALA   A CA   1 
ATOM   734  C  CA   B ALA   A 1 27  ? 19.784 0.313   14.568  0.30 18.55 ?  27  ALA   A CA   1 
ATOM   735  C  C    A ALA   A 1 27  ? 19.968 1.067   15.963  0.70 16.80 ?  27  ALA   A C    1 
ATOM   736  C  C    B ALA   A 1 27  ? 19.911 1.128   15.850  0.30 19.54 ?  27  ALA   A C    1 
ATOM   737  O  O    A ALA   A 1 27  ? 20.639 0.611   16.895  0.70 17.20 ?  27  ALA   A O    1 
ATOM   738  O  O    B ALA   A 1 27  ? 20.602 0.715   16.789  0.30 19.38 ?  27  ALA   A O    1 
ATOM   739  C  CB   A ALA   A 1 27  ? 20.690 0.776   13.573  0.70 14.73 ?  27  ALA   A CB   1 
ATOM   740  C  CB   B ALA   A 1 27  ? 20.679 0.885   13.467  0.30 18.12 ?  27  ALA   A CB   1 
ATOM   741  H  H    A ALA   A 1 27  ? 18.253 0.673   13.476  0.70 17.68 ?  27  ALA   A H    1 
ATOM   742  H  H    B ALA   A 1 27  ? 18.241 0.687   13.381  0.30 21.96 ?  27  ALA   A H    1 
ATOM   743  H  HA   A ALA   A 1 27  ? 20.004 -0.654  14.870  0.70 18.59 ?  27  ALA   A HA   1 
ATOM   744  H  HA   B ALA   A 1 27  ? 20.085 -0.589  14.754  0.30 22.24 ?  27  ALA   A HA   1 
ATOM   745  H  HB1  A ALA   A 1 27  ? 21.610 0.734   13.883  0.70 17.66 ?  27  ALA   A HB1  1 
ATOM   746  H  HB1  B ALA   A 1 27  ? 21.595 0.904   13.785  0.30 21.72 ?  27  ALA   A HB1  1 
ATOM   747  H  HB2  A ALA   A 1 27  ? 20.581 0.213   12.790  0.70 17.66 ?  27  ALA   A HB2  1 
ATOM   748  H  HB2  B ALA   A 1 27  ? 20.614 0.318   12.681  0.30 21.72 ?  27  ALA   A HB2  1 
ATOM   749  H  HB3  A ALA   A 1 27  ? 20.455 1.691   13.359  0.70 17.66 ?  27  ALA   A HB3  1 
ATOM   750  H  HB3  B ALA   A 1 27  ? 20.383 1.783   13.252  0.30 21.72 ?  27  ALA   A HB3  1 
ATOM   751  N  N    A LYS   A 1 28  ? 19.382 2.264   16.036  0.70 19.07 ?  28  LYS   A N    1 
ATOM   752  N  N    B LYS   A 1 28  ? 19.241 2.281   15.916  0.30 21.20 ?  28  LYS   A N    1 
ATOM   753  C  CA   A LYS   A 1 28  ? 19.533 3.076   17.238  0.70 22.04 ?  28  LYS   A CA   1 
ATOM   754  C  CA   B LYS   A 1 28  ? 19.358 3.135   17.094  0.30 23.13 ?  28  LYS   A CA   1 
ATOM   755  C  C    A LYS   A 1 28  ? 18.967 2.366   18.461  0.70 22.93 ?  28  LYS   A C    1 
ATOM   756  C  C    B LYS   A 1 28  ? 18.815 2.460   18.346  0.30 24.23 ?  28  LYS   A C    1 
ATOM   757  O  O    A LYS   A 1 28  ? 19.525 2.472   19.559  0.70 24.16 ?  28  LYS   A O    1 
ATOM   758  O  O    B LYS   A 1 28  ? 19.276 2.752   19.455  0.30 24.28 ?  28  LYS   A O    1 
ATOM   759  C  CB   A LYS   A 1 28  ? 18.897 4.453   17.039  0.70 24.48 ?  28  LYS   A CB   1 
ATOM   760  C  CB   B LYS   A 1 28  ? 18.642 4.466   16.860  0.30 24.12 ?  28  LYS   A CB   1 
ATOM   761  C  CG   A LYS   A 1 28  ? 19.735 5.375   16.167  0.70 26.70 ?  28  LYS   A CG   1 
ATOM   762  C  CG   B LYS   A 1 28  ? 19.312 5.336   15.812  0.30 25.45 ?  28  LYS   A CG   1 
ATOM   763  C  CD   A LYS   A 1 28  ? 19.267 6.817   16.238  0.70 29.03 ?  28  LYS   A CD   1 
ATOM   764  C  CD   B LYS   A 1 28  ? 18.841 6.779   15.874  0.30 26.79 ?  28  LYS   A CD   1 
ATOM   765  C  CE   A LYS   A 1 28  ? 17.965 7.012   15.494  0.70 30.76 ?  28  LYS   A CE   1 
ATOM   766  C  CE   B LYS   A 1 28  ? 17.424 6.934   15.356  0.30 28.03 ?  28  LYS   A CE   1 
ATOM   767  N  NZ   A LYS   A 1 28  ? 17.579 8.448   15.446  0.70 31.72 ?  28  LYS   A NZ   1 
ATOM   768  N  NZ   B LYS   A 1 28  ? 17.085 8.367   15.124  0.30 28.53 ?  28  LYS   A NZ   1 
ATOM   769  H  H    A LYS   A 1 28  ? 18.912 2.620   15.417  0.70 22.86 ?  28  LYS   A H    1 
ATOM   770  H  H    B LYS   A 1 28  ? 18.730 2.587   15.298  0.30 25.42 ?  28  LYS   A H    1 
ATOM   771  H  HA   A LYS   A 1 28  ? 20.475 3.215   17.409  0.70 26.43 ?  28  LYS   A HA   1 
ATOM   772  H  HA   B LYS   A 1 28  ? 20.295 3.326   17.246  0.30 27.73 ?  28  LYS   A HA   1 
ATOM   773  H  HB2  A LYS   A 1 28  ? 18.035 4.348   16.612  0.70 29.36 ?  28  LYS   A HB2  1 
ATOM   774  H  HB2  B LYS   A 1 28  ? 17.736 4.287   16.566  0.30 28.92 ?  28  LYS   A HB2  1 
ATOM   775  H  HB3  A LYS   A 1 28  ? 18.789 4.884   17.902  0.70 29.36 ?  28  LYS   A HB3  1 
ATOM   776  H  HB3  B LYS   A 1 28  ? 18.627 4.962   17.694  0.30 28.92 ?  28  LYS   A HB3  1 
ATOM   777  H  HG2  A LYS   A 1 28  ? 20.658 5.345   16.466  0.70 32.02 ?  28  LYS   A HG2  1 
ATOM   778  H  HG2  B LYS   A 1 28  ? 20.270 5.324   15.956  0.30 30.52 ?  28  LYS   A HG2  1 
ATOM   779  H  HG3  A LYS   A 1 28  ? 19.674 5.084   15.244  0.70 32.02 ?  28  LYS   A HG3  1 
ATOM   780  H  HG3  B LYS   A 1 28  ? 19.103 4.989   14.931  0.30 30.52 ?  28  LYS   A HG3  1 
ATOM   781  H  HD2  A LYS   A 1 28  ? 19.127 7.064   17.166  0.70 34.81 ?  28  LYS   A HD2  1 
ATOM   782  H  HD2  B LYS   A 1 28  ? 18.861 7.082   16.796  0.30 32.13 ?  28  LYS   A HD2  1 
ATOM   783  H  HD3  A LYS   A 1 28  ? 19.936 7.392   15.835  0.70 34.81 ?  28  LYS   A HD3  1 
ATOM   784  H  HD3  B LYS   A 1 28  ? 19.425 7.328   15.329  0.30 32.13 ?  28  LYS   A HD3  1 
ATOM   785  H  HE2  A LYS   A 1 28  ? 18.066 6.693   14.583  0.70 36.89 ?  28  LYS   A HE2  1 
ATOM   786  H  HE2  B LYS   A 1 28  ? 17.338 6.461   14.514  0.30 33.61 ?  28  LYS   A HE2  1 
ATOM   787  H  HE3  A LYS   A 1 28  ? 17.260 6.521   15.945  0.70 36.89 ?  28  LYS   A HE3  1 
ATOM   788  H  HE3  B LYS   A 1 28  ? 16.803 6.576   16.009  0.30 33.61 ?  28  LYS   A HE3  1 
ATOM   789  H  HZ1  A LYS   A 1 28  ? 16.812 8.542   15.005  0.70 38.04 ?  28  LYS   A HZ1  1 
ATOM   790  H  HZ1  B LYS   A 1 28  ? 16.252 8.437   14.820  0.30 34.21 ?  28  LYS   A HZ1  1 
ATOM   791  H  HZ2  A LYS   A 1 28  ? 17.478 8.763   16.272  0.70 38.04 ?  28  LYS   A HZ2  1 
ATOM   792  H  HZ2  B LYS   A 1 28  ? 17.156 8.823   15.885  0.30 34.21 ?  28  LYS   A HZ2  1 
ATOM   793  H  HZ3  A LYS   A 1 28  ? 18.211 8.919   15.032  0.70 38.04 ?  28  LYS   A HZ3  1 
ATOM   794  H  HZ3  B LYS   A 1 28  ? 17.643 8.718   14.525  0.30 34.21 ?  28  LYS   A HZ3  1 
ATOM   795  N  N    A LYS   A 1 29  ? 17.875 1.619   18.288  0.70 23.34 ?  29  LYS   A N    1 
ATOM   796  N  N    B LYS   A 1 29  ? 17.839 1.565   18.199  0.30 25.38 ?  29  LYS   A N    1 
ATOM   797  C  CA   A LYS   A 1 29  ? 17.270 0.902   19.407  0.70 25.12 ?  29  LYS   A CA   1 
ATOM   798  C  CA   B LYS   A 1 29  ? 17.240 0.898   19.349  0.30 26.71 ?  29  LYS   A CA   1 
ATOM   799  C  C    A LYS   A 1 29  ? 18.086 -0.328  19.789  0.70 24.55 ?  29  LYS   A C    1 
ATOM   800  C  C    B LYS   A 1 29  ? 18.021 -0.342  19.770  0.30 25.62 ?  29  LYS   A C    1 
ATOM   801  O  O    A LYS   A 1 29  ? 18.388 -0.540  20.970  0.70 25.69 ?  29  LYS   A O    1 
ATOM   802  O  O    B LYS   A 1 29  ? 18.236 -0.563  20.967  0.30 26.11 ?  29  LYS   A O    1 
ATOM   803  C  CB   A LYS   A 1 29  ? 15.839 0.490   19.049  0.70 27.93 ?  29  LYS   A CB   1 
ATOM   804  C  CB   B LYS   A 1 29  ? 15.799 0.500   19.023  0.30 29.06 ?  29  LYS   A CB   1 
ATOM   805  C  CG   A LYS   A 1 29  ? 15.090 -0.214  20.174  0.70 30.85 ?  29  LYS   A CG   1 
ATOM   806  C  CG   B LYS   A 1 29  ? 15.032 -0.123  20.180  0.30 30.98 ?  29  LYS   A CG   1 
ATOM   807  C  CD   A LYS   A 1 29  ? 14.764 0.744   21.309  0.70 33.50 ?  29  LYS   A CD   1 
ATOM   808  C  CD   B LYS   A 1 29  ? 14.665 0.912   21.229  0.30 32.59 ?  29  LYS   A CD   1 
ATOM   809  C  CE   A LYS   A 1 29  ? 13.895 0.078   22.366  0.70 35.38 ?  29  LYS   A CE   1 
ATOM   810  C  CE   B LYS   A 1 29  ? 13.758 0.319   22.295  0.30 33.83 ?  29  LYS   A CE   1 
ATOM   811  N  NZ   A LYS   A 1 29  ? 13.499 1.033   23.437  0.70 36.35 ?  29  LYS   A NZ   1 
ATOM   812  N  NZ   B LYS   A 1 29  ? 13.391 1.320   23.334  0.30 34.48 ?  29  LYS   A NZ   1 
ATOM   813  H  H    A LYS   A 1 29  ? 17.467 1.511   17.538  0.70 27.98 ?  29  LYS   A H    1 
ATOM   814  H  H    B LYS   A 1 29  ? 17.501 1.327   17.441  0.30 30.44 ?  29  LYS   A H    1 
ATOM   815  H  HA   A LYS   A 1 29  ? 17.229 1.487   20.179  0.70 30.12 ?  29  LYS   A HA   1 
ATOM   816  H  HA   B LYS   A 1 29  ? 17.222 1.514   20.098  0.30 32.03 ?  29  LYS   A HA   1 
ATOM   817  H  HB2  A LYS   A 1 29  ? 15.334 1.284   18.817  0.70 33.49 ?  29  LYS   A HB2  1 
ATOM   818  H  HB2  B LYS   A 1 29  ? 15.316 1.294   18.746  0.30 34.85 ?  29  LYS   A HB2  1 
ATOM   819  H  HB3  A LYS   A 1 29  ? 15.867 -0.115  18.293  0.70 33.49 ?  29  LYS   A HB3  1 
ATOM   820  H  HB3  B LYS   A 1 29  ? 15.812 -0.144  18.299  0.30 34.85 ?  29  LYS   A HB3  1 
ATOM   821  H  HG2  A LYS   A 1 29  ? 14.255 -0.568  19.829  0.70 37.00 ?  29  LYS   A HG2  1 
ATOM   822  H  HG2  B LYS   A 1 29  ? 14.212 -0.515  19.842  0.30 37.16 ?  29  LYS   A HG2  1 
ATOM   823  H  HG3  A LYS   A 1 29  ? 15.633 -0.936  20.531  0.70 37.00 ?  29  LYS   A HG3  1 
ATOM   824  H  HG3  B LYS   A 1 29  ? 15.577 -0.806  20.604  0.30 37.16 ?  29  LYS   A HG3  1 
ATOM   825  H  HD2  A LYS   A 1 29  ? 15.588 1.034   21.731  0.70 40.18 ?  29  LYS   A HD2  1 
ATOM   826  H  HD2  B LYS   A 1 29  ? 15.472 1.234   21.660  0.30 39.09 ?  29  LYS   A HD2  1 
ATOM   827  H  HD3  A LYS   A 1 29  ? 14.281 1.507   20.955  0.70 40.18 ?  29  LYS   A HD3  1 
ATOM   828  H  HD3  B LYS   A 1 29  ? 14.195 1.647   20.804  0.30 39.09 ?  29  LYS   A HD3  1 
ATOM   829  H  HE2  A LYS   A 1 29  ? 13.088 -0.263  21.948  0.70 42.44 ?  29  LYS   A HE2  1 
ATOM   830  H  HE2  B LYS   A 1 29  ? 12.941 0.001   21.878  0.30 40.57 ?  29  LYS   A HE2  1 
ATOM   831  H  HE3  A LYS   A 1 29  ? 14.391 -0.649  22.776  0.70 42.44 ?  29  LYS   A HE3  1 
ATOM   832  H  HE3  B LYS   A 1 29  ? 14.218 -0.416  22.731  0.30 40.57 ?  29  LYS   A HE3  1 
ATOM   833  H  HZ1  A LYS   A 1 29  ? 12.992 0.620   24.041  0.70 43.60 ?  29  LYS   A HZ1  1 
ATOM   834  H  HZ1  B LYS   A 1 29  ? 12.861 0.946   23.943  0.30 41.36 ?  29  LYS   A HZ1  1 
ATOM   835  H  HZ2  A LYS   A 1 29  ? 14.223 1.357   23.840  0.70 43.60 ?  29  LYS   A HZ2  1 
ATOM   836  H  HZ2  B LYS   A 1 29  ? 14.125 1.624   23.736  0.30 41.36 ?  29  LYS   A HZ2  1 
ATOM   837  H  HZ3  A LYS   A 1 29  ? 13.036 1.708   23.086  0.70 43.60 ?  29  LYS   A HZ3  1 
ATOM   838  H  HZ3  B LYS   A 1 29  ? 12.962 2.004   22.959  0.30 41.36 ?  29  LYS   A HZ3  1 
ATOM   839  N  N    . VAL   A 1 30  ? 18.436 -1.158  18.805  1.00 24.30 ?  30  VAL   A N    1 
ATOM   840  C  CA   . VAL   A 1 30  ? 19.086 -2.430  19.109  1.00 22.86 ?  30  VAL   A CA   1 
ATOM   841  C  C    . VAL   A 1 30  ? 20.590 -2.286  19.335  1.00 21.90 ?  30  VAL   A C    1 
ATOM   842  O  O    . VAL   A 1 30  ? 21.170 -3.024  20.139  1.00 22.73 ?  30  VAL   A O    1 
ATOM   843  C  CB   . VAL   A 1 30  ? 18.781 -3.430  17.978  1.00 23.90 ?  30  VAL   A CB   1 
ATOM   844  C  CG1  . VAL   A 1 30  ? 19.515 -4.747  18.199  1.00 24.91 ?  30  VAL   A CG1  1 
ATOM   845  C  CG2  . VAL   A 1 30  ? 17.277 -3.664  17.865  1.00 24.31 ?  30  VAL   A CG2  1 
ATOM   846  H  H    A VAL   A 1 30  ? 18.307 -1.012  17.965  0.70 29.13 ?  30  VAL   A H    1 
ATOM   847  H  H    B VAL   A 1 30  ? 18.337 -1.006  17.963  0.30 29.13 ?  30  VAL   A H    1 
ATOM   848  H  HA   . VAL   A 1 30  ? 18.694 -2.788  19.918  1.00 27.41 ?  30  VAL   A HA   1 
ATOM   849  H  HB   . VAL   A 1 30  ? 19.085 -3.062  17.134  1.00 28.65 ?  30  VAL   A HB   1 
ATOM   850  H  HG11 . VAL   A 1 30  ? 19.138 -5.422  17.610  1.00 29.88 ?  30  VAL   A HG11 1 
ATOM   851  H  HG12 . VAL   A 1 30  ? 20.454 -4.625  17.999  1.00 29.88 ?  30  VAL   A HG12 1 
ATOM   852  H  HG13 . VAL   A 1 30  ? 19.401 -5.019  19.123  1.00 29.88 ?  30  VAL   A HG13 1 
ATOM   853  H  HG21 . VAL   A 1 30  ? 17.109 -4.345  17.193  1.00 29.15 ?  30  VAL   A HG21 1 
ATOM   854  H  HG22 . VAL   A 1 30  ? 16.939 -3.960  18.725  1.00 29.15 ?  30  VAL   A HG22 1 
ATOM   855  H  HG23 . VAL   A 1 30  ? 16.846 -2.834  17.608  1.00 29.15 ?  30  VAL   A HG23 1 
ATOM   856  N  N    . LYS   A 1 31  ? 21.239 -1.352  18.647  1.00 20.94 ?  31  LYS   A N    1 
ATOM   857  C  CA   . LYS   A 1 31  ? 22.694 -1.257  18.615  1.00 21.44 ?  31  LYS   A CA   1 
ATOM   858  C  C    . LYS   A 1 31  ? 23.306 -2.619  18.274  1.00 19.46 ?  31  LYS   A C    1 
ATOM   859  O  O    . LYS   A 1 31  ? 24.083 -3.175  19.058  1.00 20.99 ?  31  LYS   A O    1 
ATOM   860  C  CB   . LYS   A 1 31  ? 23.260 -0.708  19.917  1.00 25.86 ?  31  LYS   A CB   1 
ATOM   861  C  CG   . LYS   A 1 31  ? 22.557 0.547   20.409  1.00 31.92 ?  31  LYS   A CG   1 
ATOM   862  C  CD   . LYS   A 1 31  ? 23.550 1.605   20.868  1.00 37.16 ?  31  LYS   A CD   1 
ATOM   863  C  CE   . LYS   A 1 31  ? 22.891 2.632   21.777  1.00 40.10 ?  31  LYS   A CE   1 
ATOM   864  N  NZ   . LYS   A 1 31  ? 21.700 3.273   21.162  1.00 42.75 ?  31  LYS   A NZ   1 
ATOM   865  H  H    . LYS   A 1 31  ? 20.845 -0.746  18.180  1.00 25.11 ?  31  LYS   A H    1 
ATOM   866  H  HA   . LYS   A 1 31  ? 22.939 -0.639  17.912  1.00 25.71 ?  31  LYS   A HA   1 
ATOM   867  H  HB2  . LYS   A 1 31  ? 23.178 -1.385  20.602  1.00 31.01 ?  31  LYS   A HB2  1 
ATOM   868  H  HB3  . LYS   A 1 31  ? 24.195 -0.489  19.778  1.00 31.01 ?  31  LYS   A HB3  1 
ATOM   869  H  HG2  . LYS   A 1 31  ? 22.027 0.923   19.688  1.00 38.28 ?  31  LYS   A HG2  1 
ATOM   870  H  HG3  . LYS   A 1 31  ? 21.986 0.320   21.160  1.00 38.28 ?  31  LYS   A HG3  1 
ATOM   871  H  HD2  . LYS   A 1 31  ? 24.268 1.177   21.360  1.00 44.57 ?  31  LYS   A HD2  1 
ATOM   872  H  HD3  . LYS   A 1 31  ? 23.904 2.070   20.093  1.00 44.57 ?  31  LYS   A HD3  1 
ATOM   873  H  HE2  . LYS   A 1 31  ? 22.590 2.185   22.579  1.00 48.10 ?  31  LYS   A HE2  1 
ATOM   874  H  HE3  . LYS   A 1 31  ? 23.534 3.324   22.003  1.00 48.10 ?  31  LYS   A HE3  1 
ATOM   875  H  HZ1  . LYS   A 1 31  ? 21.358 3.877   21.719  1.00 51.28 ?  31  LYS   A HZ1  1 
ATOM   876  H  HZ2  . LYS   A 1 31  ? 21.931 3.675   20.404  1.00 51.28 ?  31  LYS   A HZ2  1 
ATOM   877  H  HZ3  . LYS   A 1 31  ? 21.081 2.657   20.988  1.00 51.28 ?  31  LYS   A HZ3  1 
ATOM   878  N  N    . PRO   A 1 32  ? 22.974 -3.174  17.113  1.00 17.04 ?  32  PRO   A N    1 
ATOM   879  C  CA   . PRO   A 1 32  ? 23.446 -4.515  16.768  1.00 17.88 ?  32  PRO   A CA   1 
ATOM   880  C  C    . PRO   A 1 32  ? 24.947 -4.531  16.557  1.00 17.83 ?  32  PRO   A C    1 
ATOM   881  O  O    . PRO   A 1 32  ? 25.590 -3.501  16.340  1.00 17.55 ?  32  PRO   A O    1 
ATOM   882  C  CB   . PRO   A 1 32  ? 22.720 -4.806  15.451  1.00 17.71 ?  32  PRO   A CB   1 
ATOM   883  C  CG   . PRO   A 1 32  ? 22.560 -3.447  14.833  1.00 16.07 ?  32  PRO   A CG   1 
ATOM   884  C  CD   . PRO   A 1 32  ? 22.246 -2.550  15.998  1.00 16.50 ?  32  PRO   A CD   1 
ATOM   885  H  HA   . PRO   A 1 32  ? 23.192 -5.163  17.445  1.00 21.44 ?  32  PRO   A HA   1 
ATOM   886  H  HB2  . PRO   A 1 32  ? 23.266 -5.386  14.892  1.00 21.23 ?  32  PRO   A HB2  1 
ATOM   887  H  HB3  . PRO   A 1 32  ? 21.857 -5.216  15.631  1.00 21.23 ?  32  PRO   A HB3  1 
ATOM   888  H  HG2  . PRO   A 1 32  ? 23.386 -3.189  14.401  1.00 19.26 ?  32  PRO   A HG2  1 
ATOM   889  H  HG3  . PRO   A 1 32  ? 21.826 -3.468  14.196  1.00 19.26 ?  32  PRO   A HG3  1 
ATOM   890  H  HD2  . PRO   A 1 32  ? 22.581 -1.658  15.821  1.00 19.78 ?  32  PRO   A HD2  1 
ATOM   891  H  HD3  . PRO   A 1 32  ? 21.293 -2.549  16.167  1.00 19.78 ?  32  PRO   A HD3  1 
ATOM   892  N  N    . THR   A 1 33  ? 25.503 -5.739  16.598  1.00 17.62 ?  33  THR   A N    1 
ATOM   893  C  CA   . THR   A 1 33  ? 26.912 -5.902  16.274  1.00 17.77 ?  33  THR   A CA   1 
ATOM   894  C  C    . THR   A 1 33  ? 27.207 -5.443  14.851  1.00 16.40 ?  33  THR   A C    1 
ATOM   895  O  O    . THR   A 1 33  ? 28.238 -4.800  14.601  1.00 16.47 ?  33  THR   A O    1 
ATOM   896  C  CB   . THR   A 1 33  ? 27.320 -7.360  16.471  1.00 19.49 ?  33  THR   A CB   1 
ATOM   897  O  OG1  . THR   A 1 33  ? 27.006 -7.758  17.808  1.00 21.50 ?  33  THR   A OG1  1 
ATOM   898  C  CG2  . THR   A 1 33  ? 28.809 -7.533  16.232  1.00 20.52 ?  33  THR   A CG2  1 
ATOM   899  H  H    . THR   A 1 33  ? 25.090 -6.467  16.799  1.00 21.12 ?  33  THR   A H    1 
ATOM   900  H  HA   . THR   A 1 33  ? 27.439 -5.361  16.881  1.00 21.30 ?  33  THR   A HA   1 
ATOM   901  H  HB   . THR   A 1 33  ? 26.836 -7.924  15.843  1.00 23.36 ?  33  THR   A HB   1 
ATOM   902  H  HG1  . THR   A 1 33  ? 27.429 -7.281  18.358  1.00 25.78 ?  33  THR   A HG1  1 
ATOM   903  H  HG21 . THR   A 1 33  ? 29.089 -8.416  16.519  1.00 24.61 ?  33  THR   A HG21 1 
ATOM   904  H  HG22 . THR   A 1 33  ? 29.010 -7.430  15.289  1.00 24.61 ?  33  THR   A HG22 1 
ATOM   905  H  HG23 . THR   A 1 33  ? 29.302 -6.868  16.736  1.00 24.61 ?  33  THR   A HG23 1 
ATOM   906  N  N    . VAL   A 1 34  ? 26.313 -5.757  13.911  1.00 14.79 ?  34  VAL   A N    1 
ATOM   907  C  CA   . VAL   A 1 34  ? 26.502 -5.423  12.502  1.00 13.46 ?  34  VAL   A CA   1 
ATOM   908  C  C    . VAL   A 1 34  ? 25.202 -4.867  11.935  1.00 12.52 ?  34  VAL   A C    1 
ATOM   909  O  O    . VAL   A 1 34  ? 24.165 -5.541  11.975  1.00 13.12 ?  34  VAL   A O    1 
ATOM   910  C  CB   . VAL   A 1 34  ? 26.945 -6.634  11.662  1.00 14.30 ?  34  VAL   A CB   1 
ATOM   911  C  CG1  . VAL   A 1 34  ? 27.118 -6.238  10.204  1.00 14.39 ?  34  VAL   A CG1  1 
ATOM   912  C  CG2  . VAL   A 1 34  ? 28.223 -7.252  12.217  1.00 15.51 ?  34  VAL   A CG2  1 
ATOM   913  H  H    . VAL   A 1 34  ? 25.576 -6.174  14.069  1.00 17.72 ?  34  VAL   A H    1 
ATOM   914  H  HA   . VAL   A 1 34  ? 27.182 -4.731  12.422  1.00 16.13 ?  34  VAL   A HA   1 
ATOM   915  H  HB   . VAL   A 1 34  ? 26.246 -7.305  11.705  1.00 17.14 ?  34  VAL   A HB   1 
ATOM   916  H  HG11 . VAL   A 1 34  ? 27.613 -6.934  9.749   1.00 17.25 ?  34  VAL   A HG11 1 
ATOM   917  H  HG12 . VAL   A 1 34  ? 26.245 -6.130  9.795   1.00 17.25 ?  34  VAL   A HG12 1 
ATOM   918  H  HG13 . VAL   A 1 34  ? 27.610 -5.401  10.161  1.00 17.25 ?  34  VAL   A HG13 1 
ATOM   919  H  HG21 . VAL   A 1 34  ? 28.484 -7.992  11.648  1.00 18.60 ?  34  VAL   A HG21 1 
ATOM   920  H  HG22 . VAL   A 1 34  ? 28.919 -6.578  12.229  1.00 18.60 ?  34  VAL   A HG22 1 
ATOM   921  H  HG23 . VAL   A 1 34  ? 28.054 -7.571  13.118  1.00 18.60 ?  34  VAL   A HG23 1 
ATOM   922  N  N    . VAL   A 1 35  ? 25.261 -3.653  11.389  1.00 11.75 ?  35  VAL   A N    1 
ATOM   923  C  CA   . VAL   A 1 35  ? 24.232 -3.144  10.493  1.00 11.25 ?  35  VAL   A CA   1 
ATOM   924  C  C    . VAL   A 1 35  ? 24.790 -3.155  9.076   1.00 11.26 ?  35  VAL   A C    1 
ATOM   925  O  O    . VAL   A 1 35  ? 25.935 -2.747  8.845   1.00 11.55 ?  35  VAL   A O    1 
ATOM   926  C  CB   . VAL   A 1 35  ? 23.704 -1.749  10.895  1.00 12.36 ?  35  VAL   A CB   1 
ATOM   927  C  CG1  . VAL   A 1 35  ? 24.781 -0.654  10.793  1.00 12.92 ?  35  VAL   A CG1  1 
ATOM   928  C  CG2  . VAL   A 1 35  ? 22.478 -1.391  10.058  1.00 13.23 ?  35  VAL   A CG2  1 
ATOM   929  H  H    . VAL   A 1 35  ? 25.892 -3.088  11.529  1.00 14.08 ?  35  VAL   A H    1 
ATOM   930  H  HA   . VAL   A 1 35  ? 23.472 -3.751  10.510  1.00 13.48 ?  35  VAL   A HA   1 
ATOM   931  H  HB   . VAL   A 1 35  ? 23.410 -1.784  11.817  1.00 14.81 ?  35  VAL   A HB   1 
ATOM   932  H  HG11 . VAL   A 1 35  ? 24.422 0.180   11.139  1.00 15.48 ?  35  VAL   A HG11 1 
ATOM   933  H  HG12 . VAL   A 1 35  ? 25.551 -0.923  11.319  1.00 15.48 ?  35  VAL   A HG12 1 
ATOM   934  H  HG13 . VAL   A 1 35  ? 25.038 -0.541  9.865   1.00 15.48 ?  35  VAL   A HG13 1 
ATOM   935  H  HG21 . VAL   A 1 35  ? 22.116 -0.548  10.364  1.00 15.85 ?  35  VAL   A HG21 1 
ATOM   936  H  HG22 . VAL   A 1 35  ? 22.746 -1.314  9.123   1.00 15.85 ?  35  VAL   A HG22 1 
ATOM   937  H  HG23 . VAL   A 1 35  ? 21.815 -2.093  10.149  1.00 15.85 ?  35  VAL   A HG23 1 
ATOM   938  N  N    . VAL   A 1 36  ? 23.976 -3.605  8.124   1.00 10.27 ?  36  VAL   A N    1 
ATOM   939  C  CA   . VAL   A 1 36  ? 24.352 -3.620  6.716   1.00 9.91  ?  36  VAL   A CA   1 
ATOM   940  C  C    . VAL   A 1 36  ? 23.895 -2.328  6.052   1.00 10.20 ?  36  VAL   A C    1 
ATOM   941  O  O    . VAL   A 1 36  ? 22.729 -1.929  6.182   1.00 10.94 ?  36  VAL   A O    1 
ATOM   942  C  CB   . VAL   A 1 36  ? 23.743 -4.837  5.999   1.00 10.31 ?  36  VAL   A CB   1 
ATOM   943  C  CG1  . VAL   A 1 36  ? 24.012 -4.764  4.510   1.00 10.88 ?  36  VAL   A CG1  1 
ATOM   944  C  CG2  . VAL   A 1 36  ? 24.297 -6.134  6.578   1.00 11.17 ?  36  VAL   A CG2  1 
ATOM   945  H  H    . VAL   A 1 36  ? 23.182 -3.913  8.274   1.00 12.31 ?  36  VAL   A H    1 
ATOM   946  H  HA   . VAL   A 1 36  ? 25.320 -3.683  6.646   1.00 11.87 ?  36  VAL   A HA   1 
ATOM   947  H  HB   . VAL   A 1 36  ? 22.782 -4.833  6.131   1.00 12.35 ?  36  VAL   A HB   1 
ATOM   948  H  HG11 . VAL   A 1 36  ? 23.866 -5.641  4.122   1.00 13.04 ?  36  VAL   A HG11 1 
ATOM   949  H  HG12 . VAL   A 1 36  ? 23.404 -4.123  4.107   1.00 13.04 ?  36  VAL   A HG12 1 
ATOM   950  H  HG13 . VAL   A 1 36  ? 24.929 -4.488  4.369   1.00 13.04 ?  36  VAL   A HG13 1 
ATOM   951  H  HG21 . VAL   A 1 36  ? 23.909 -6.891  6.108   1.00 13.38 ?  36  VAL   A HG21 1 
ATOM   952  H  HG22 . VAL   A 1 36  ? 25.265 -6.145  6.469   1.00 13.38 ?  36  VAL   A HG22 1 
ATOM   953  H  HG23 . VAL   A 1 36  ? 24.077 -6.188  7.523   1.00 13.38 ?  36  VAL   A HG23 1 
ATOM   954  N  N    . ASN   A 1 37  ? 24.810 -1.701  5.315   1.00 9.81  ?  37  ASN   A N    1 
ATOM   955  C  CA   . ASN   A 1 37  ? 24.484 -0.584  4.447   1.00 9.54  ?  37  ASN   A CA   1 
ATOM   956  C  C    . ASN   A 1 37  ? 24.347 -1.055  3.010   1.00 9.70  ?  37  ASN   A C    1 
ATOM   957  O  O    . ASN   A 1 37  ? 25.136 -1.882  2.532   1.00 10.61 ?  37  ASN   A O    1 
ATOM   958  C  CB   . ASN   A 1 37  ? 25.560 0.501   4.530   1.00 10.00 ?  37  ASN   A CB   1 
ATOM   959  C  CG   . ASN   A 1 37  ? 25.237 1.698   3.673   1.00 10.28 ?  37  ASN   A CG   1 
ATOM   960  O  OD1  . ASN   A 1 37  ? 24.067 2.034   3.478   1.00 10.80 ?  37  ASN   A OD1  1 
ATOM   961  N  ND2  . ASN   A 1 37  ? 26.273 2.350   3.156   1.00 10.65 ?  37  ASN   A ND2  1 
ATOM   962  H  H    . ASN   A 1 37  ? 25.648 -1.901  5.318   1.00 11.76 ?  37  ASN   A H    1 
ATOM   963  H  HA   . ASN   A 1 37  ? 23.641 -0.193  4.730   1.00 11.43 ?  37  ASN   A HA   1 
ATOM   964  H  HB2  . ASN   A 1 37  ? 25.640 0.802   5.451   1.00 11.98 ?  37  ASN   A HB2  1 
ATOM   965  H  HB3  . ASN   A 1 37  ? 26.408 0.130   4.231   1.00 11.98 ?  37  ASN   A HB3  1 
ATOM   966  H  HD21 . ASN   A 1 37  ? 26.141 3.039   2.659   1.00 12.75 ?  37  ASN   A HD21 1 
ATOM   967  H  HD22 . ASN   A 1 37  ? 27.071 2.090   3.316   1.00 12.75 ?  37  ASN   A HD22 1 
ATOM   968  N  N    A ALA   A 1 38  ? 23.325 -0.514  2.333   0.70 9.87  ?  38  ALA   A N    1 
ATOM   969  N  N    B ALA   A 1 38  ? 23.332 -0.541  2.313   0.30 10.29 ?  38  ALA   A N    1 
ATOM   970  C  CA   A ALA   A 1 38  ? 23.135 -0.639  0.888   0.70 10.22 ?  38  ALA   A CA   1 
ATOM   971  C  CA   B ALA   A 1 38  ? 23.170 -0.817  0.885   0.30 10.67 ?  38  ALA   A CA   1 
ATOM   972  C  C    A ALA   A 1 38  ? 24.054 0.359   0.185   0.70 10.10 ?  38  ALA   A C    1 
ATOM   973  C  C    B ALA   A 1 38  ? 23.981 0.216   0.104   0.30 10.57 ?  38  ALA   A C    1 
ATOM   974  O  O    A ALA   A 1 38  ? 23.651 1.454   -0.215  0.70 9.96  ?  38  ALA   A O    1 
ATOM   975  O  O    B ALA   A 1 38  ? 23.466 1.218   -0.399  0.30 10.57 ?  38  ALA   A O    1 
ATOM   976  C  CB   A ALA   A 1 38  ? 21.673 -0.386  0.535   0.70 11.30 ?  38  ALA   A CB   1 
ATOM   977  C  CB   B ALA   A 1 38  ? 21.696 -0.807  0.503   0.30 11.57 ?  38  ALA   A CB   1 
ATOM   978  H  H    A ALA   A 1 38  ? 22.718 -0.037  2.712   0.70 11.83 ?  38  ALA   A H    1 
ATOM   979  H  H    B ALA   A 1 38  ? 22.726 -0.027  2.648   0.30 12.32 ?  38  ALA   A H    1 
ATOM   980  H  HA   A ALA   A 1 38  ? 23.373 -1.529  0.602   0.70 12.25 ?  38  ALA   A HA   1 
ATOM   981  H  HA   B ALA   A 1 38  ? 23.528 -1.700  0.691   0.30 12.79 ?  38  ALA   A HA   1 
ATOM   982  H  HB1  A ALA   A 1 38  ? 21.556 -0.472  -0.423  0.70 13.54 ?  38  ALA   A HB1  1 
ATOM   983  H  HB1  B ALA   A 1 38  ? 21.620 -0.940  -0.454  0.30 13.86 ?  38  ALA   A HB1  1 
ATOM   984  H  HB2  A ALA   A 1 38  ? 21.119 -1.039  0.995   0.70 13.54 ?  38  ALA   A HB2  1 
ATOM   985  H  HB2  B ALA   A 1 38  ? 21.238 -1.522  0.974   0.30 13.86 ?  38  ALA   A HB2  1 
ATOM   986  H  HB3  A ALA   A 1 38  ? 21.425 0.510   0.818   0.70 13.54 ?  38  ALA   A HB3  1 
ATOM   987  H  HB3  B ALA   A 1 38  ? 21.313 0.049   0.747   0.30 13.86 ?  38  ALA   A HB3  1 
ATOM   988  N  N    A ALA   A 1 39  ? 25.315 -0.034  0.037   0.70 10.23 ?  39  ALA   A N    1 
ATOM   989  N  N    B ALA   A 1 39  ? 25.281 -0.043  0.003   0.30 10.85 ?  39  ALA   A N    1 
ATOM   990  C  CA   A ALA   A 1 39  ? 26.375 0.837   -0.441  0.70 10.02 ?  39  ALA   A CA   1 
ATOM   991  C  CA   B ALA   A 1 39  ? 26.219 0.938   -0.517  0.30 10.90 ?  39  ALA   A CA   1 
ATOM   992  C  C    A ALA   A 1 39  ? 26.495 0.799   -1.963  0.70 10.23 ?  39  ALA   A C    1 
ATOM   993  C  C    B ALA   A 1 39  ? 26.411 0.785   -2.024  0.30 10.51 ?  39  ALA   A C    1 
ATOM   994  O  O    A ALA   A 1 39  ? 25.967 -0.092  -2.640  0.70 11.06 ?  39  ALA   A O    1 
ATOM   995  O  O    B ALA   A 1 39  ? 26.042 -0.224  -2.633  0.30 10.45 ?  39  ALA   A O    1 
ATOM   996  C  CB   A ALA   A 1 39  ? 27.702 0.414   0.197   0.70 10.30 ?  39  ALA   A CB   1 
ATOM   997  C  CB   B ALA   A 1 39  ? 27.563 0.805   0.195   0.30 11.78 ?  39  ALA   A CB   1 
ATOM   998  H  H    A ALA   A 1 39  ? 25.583 -0.830  0.220   0.70 12.25 ?  39  ALA   A H    1 
ATOM   999  H  H    B ALA   A 1 39  ? 25.646 -0.792  0.231   0.30 13.00 ?  39  ALA   A H    1 
ATOM   1000 H  HA   A ALA   A 1 39  ? 26.183 1.749   -0.170  0.70 12.00 ?  39  ALA   A HA   1 
ATOM   1001 H  HA   B ALA   A 1 39  ? 25.872 1.825   -0.341  0.30 13.06 ?  39  ALA   A HA   1 
ATOM   1002 H  HB1  A ALA   A 1 39  ? 28.404 1.002   -0.122  0.70 12.33 ?  39  ALA   A HB1  1 
ATOM   1003 H  HB1  B ALA   A 1 39  ? 28.174 1.468   -0.164  0.30 14.11 ?  39  ALA   A HB1  1 
ATOM   1004 H  HB2  A ALA   A 1 39  ? 27.624 0.494   1.166   0.70 12.33 ?  39  ALA   A HB2  1 
ATOM   1005 H  HB2  B ALA   A 1 39  ? 27.434 0.956   1.146   0.30 14.11 ?  39  ALA   A HB2  1 
ATOM   1006 H  HB3  A ALA   A 1 39  ? 27.893 -0.500  -0.044  0.70 12.33 ?  39  ALA   A HB3  1 
ATOM   1007 H  HB3  B ALA   A 1 39  ? 27.914 -0.086  0.046   0.30 14.11 ?  39  ALA   A HB3  1 
ATOM   1008 N  N    A ASN   A 1 40  ? 27.211 1.792   -2.496  0.70 10.35 ?  40  ASN   A N    1 
ATOM   1009 N  N    B ASN   A 1 40  ? 26.997 1.818   -2.625  0.30 10.50 ?  40  ASN   A N    1 
ATOM   1010 C  CA   A ASN   A 1 40  ? 27.755 1.744   -3.846  0.70 10.57 ?  40  ASN   A CA   1 
ATOM   1011 C  CA   B ASN   A 1 40  ? 27.494 1.757   -3.990  0.30 10.46 ?  40  ASN   A CA   1 
ATOM   1012 C  C    A ASN   A 1 40  ? 29.279 1.633   -3.775  0.70 9.68  ?  40  ASN   A C    1 
ATOM   1013 C  C    B ASN   A 1 40  ? 29.015 1.606   -3.973  0.30 10.34 ?  40  ASN   A C    1 
ATOM   1014 O  O    A ASN   A 1 40  ? 29.881 1.754   -2.704  0.70 9.98  ?  40  ASN   A O    1 
ATOM   1015 O  O    B ASN   A 1 40  ? 29.657 1.649   -2.922  0.30 10.42 ?  40  ASN   A O    1 
ATOM   1016 C  CB   A ASN   A 1 40  ? 27.270 2.918   -4.720  0.70 11.74 ?  40  ASN   A CB   1 
ATOM   1017 C  CB   B ASN   A 1 40  ? 27.064 2.995   -4.790  0.30 10.99 ?  40  ASN   A CB   1 
ATOM   1018 C  CG   A ASN   A 1 40  ? 27.632 4.275   -4.158  0.70 12.83 ?  40  ASN   A CG   1 
ATOM   1019 C  CG   B ASN   A 1 40  ? 27.480 4.293   -4.131  0.30 11.73 ?  40  ASN   A CG   1 
ATOM   1020 O  OD1  A ASN   A 1 40  ? 28.786 4.530   -3.803  0.70 13.41 ?  40  ASN   A OD1  1 
ATOM   1021 O  OD1  B ASN   A 1 40  ? 28.670 4.599   -4.026  0.30 11.97 ?  40  ASN   A OD1  1 
ATOM   1022 N  ND2  A ASN   A 1 40  ? 26.632 5.161   -4.071  0.70 13.74 ?  40  ASN   A ND2  1 
ATOM   1023 N  ND2  B ASN   A 1 40  ? 26.496 5.071   -3.687  0.30 12.13 ?  40  ASN   A ND2  1 
ATOM   1024 H  H    A ASN   A 1 40  ? 27.407 2.515   -2.077  0.70 12.40 ?  40  ASN   A H    1 
ATOM   1025 H  H    B ASN   A 1 40  ? 27.119 2.582   -2.248  0.30 12.58 ?  40  ASN   A H    1 
ATOM   1026 H  HA   A ASN   A 1 40  ? 27.442 0.932   -4.268  0.70 12.66 ?  40  ASN   A HA   1 
ATOM   1027 H  HA   B ASN   A 1 40  ? 27.117 0.975   -4.429  0.30 12.54 ?  40  ASN   A HA   1 
ATOM   1028 H  HB2  A ASN   A 1 40  ? 27.671 2.836   -5.603  0.70 14.07 ?  40  ASN   A HB2  1 
ATOM   1029 H  HB2  B ASN   A 1 40  ? 27.470 2.959   -5.667  0.30 13.16 ?  40  ASN   A HB2  1 
ATOM   1030 H  HB3  A ASN   A 1 40  ? 26.305 2.869   -4.795  0.70 14.07 ?  40  ASN   A HB3  1 
ATOM   1031 H  HB3  B ASN   A 1 40  ? 26.096 2.989   -4.875  0.30 13.16 ?  40  ASN   A HB3  1 
ATOM   1032 H  HD21 A ASN   A 1 40  ? 26.779 5.951   -3.761  0.70 16.46 ?  40  ASN   A HD21 1 
ATOM   1033 H  HD21 B ASN   A 1 40  ? 26.681 5.817   -3.302  0.30 14.54 ?  40  ASN   A HD21 1 
ATOM   1034 H  HD22 A ASN   A 1 40  ? 25.838 4.939   -4.318  0.70 16.46 ?  40  ASN   A HD22 1 
ATOM   1035 H  HD22 B ASN   A 1 40  ? 25.675 4.829   -3.783  0.30 14.54 ?  40  ASN   A HD22 1 
ATOM   1036 N  N    A VAL   A 1 41  ? 29.902 1.355   -4.926  0.70 10.12 ?  41  VAL   A N    1 
ATOM   1037 N  N    B VAL   A 1 41  ? 29.593 1.419   -5.163  0.30 10.59 ?  41  VAL   A N    1 
ATOM   1038 C  CA   A VAL   A 1 41  ? 31.334 1.048   -4.952  0.70 10.67 ?  41  VAL   A CA   1 
ATOM   1039 C  CA   B VAL   A 1 41  ? 31.016 1.089   -5.241  0.30 10.93 ?  41  VAL   A CA   1 
ATOM   1040 C  C    A VAL   A 1 41  ? 32.192 2.215   -4.493  0.70 10.68 ?  41  VAL   A C    1 
ATOM   1041 C  C    B VAL   A 1 41  ? 31.895 2.214   -4.711  0.30 11.43 ?  41  VAL   A C    1 
ATOM   1042 O  O    A VAL   A 1 41  ? 33.344 2.006   -4.088  0.70 11.22 ?  41  VAL   A O    1 
ATOM   1043 O  O    B VAL   A 1 41  ? 33.018 1.965   -4.254  0.30 12.12 ?  41  VAL   A O    1 
ATOM   1044 C  CB   A VAL   A 1 41  ? 31.817 0.556   -6.337  0.70 10.70 ?  41  VAL   A CB   1 
ATOM   1045 C  CB   B VAL   A 1 41  ? 31.421 0.676   -6.670  0.30 11.45 ?  41  VAL   A CB   1 
ATOM   1046 C  CG1  A VAL   A 1 41  ? 31.122 -0.737  -6.734  0.70 11.72 ?  41  VAL   A CG1  1 
ATOM   1047 C  CG1  B VAL   A 1 41  ? 30.788 -0.658  -7.038  0.30 12.22 ?  41  VAL   A CG1  1 
ATOM   1048 C  CG2  A VAL   A 1 41  ? 31.675 1.636   -7.408  0.70 11.26 ?  41  VAL   A CG2  1 
ATOM   1049 C  CG2  B VAL   A 1 41  ? 31.051 1.762   -7.673  0.30 11.95 ?  41  VAL   A CG2  1 
ATOM   1050 H  H    A VAL   A 1 41  ? 29.524 1.324   -5.692  0.70 12.13 ?  41  VAL   A H    1 
ATOM   1051 H  H    B VAL   A 1 41  ? 29.185 1.464   -5.919  0.30 12.68 ?  41  VAL   A H    1 
ATOM   1052 H  HA   A VAL   A 1 41  ? 31.500 0.323   -4.328  0.70 12.78 ?  41  VAL   A HA   1 
ATOM   1053 H  HA   B VAL   A 1 41  ? 31.171 0.321   -4.672  0.30 13.10 ?  41  VAL   A HA   1 
ATOM   1054 H  HB   A VAL   A 1 41  ? 32.766 0.352   -6.269  0.70 12.82 ?  41  VAL   A HB   1 
ATOM   1055 H  HB   B VAL   A 1 41  ? 32.382 0.561   -6.696  0.30 13.72 ?  41  VAL   A HB   1 
ATOM   1056 H  HG11 A VAL   A 1 41  ? 31.456 -1.030  -7.596  0.70 14.04 ?  41  VAL   A HG11 1 
ATOM   1057 H  HG11 B VAL   A 1 41  ? 31.048 -0.892  -7.941  0.30 14.64 ?  41  VAL   A HG11 1 
ATOM   1058 H  HG12 A VAL   A 1 41  ? 31.298 -1.415  -6.063  0.70 14.04 ?  41  VAL   A HG12 1 
ATOM   1059 H  HG12 B VAL   A 1 41  ? 31.101 -1.338  -6.417  0.30 14.64 ?  41  VAL   A HG12 1 
ATOM   1060 H  HG13 A VAL   A 1 41  ? 30.164 -0.575  -6.792  0.70 14.04 ?  41  VAL   A HG13 1 
ATOM   1061 H  HG13 B VAL   A 1 41  ? 29.824 -0.581  -6.979  0.30 14.64 ?  41  VAL   A HG13 1 
ATOM   1062 H  HG21 A VAL   A 1 41  ? 31.883 1.251   -8.274  0.70 13.49 ?  41  VAL   A HG21 1 
ATOM   1063 H  HG21 B VAL   A 1 41  ? 31.416 1.524   -8.539  0.30 14.32 ?  41  VAL   A HG21 1 
ATOM   1064 H  HG22 A VAL   A 1 41  ? 30.767 1.968   -7.401  0.70 13.49 ?  41  VAL   A HG22 1 
ATOM   1065 H  HG22 B VAL   A 1 41  ? 30.085 1.829   -7.730  0.30 14.32 ?  41  VAL   A HG22 1 
ATOM   1066 H  HG23 A VAL   A 1 41  ? 32.295 2.358   -7.213  0.70 13.49 ?  41  VAL   A HG23 1 
ATOM   1067 H  HG23 B VAL   A 1 41  ? 31.425 2.605   -7.376  0.30 14.32 ?  41  VAL   A HG23 1 
ATOM   1068 N  N    A TYR   A 1 42  ? 31.671 3.444   -4.569  0.70 10.78 ?  42  TYR   A N    1 
ATOM   1069 N  N    B TYR   A 1 42  ? 31.421 3.459   -4.768  0.30 11.72 ?  42  TYR   A N    1 
ATOM   1070 C  CA   A TYR   A 1 42  ? 32.390 4.646   -4.161  0.70 10.82 ?  42  TYR   A CA   1 
ATOM   1071 C  CA   B TYR   A 1 42  ? 32.217 4.602   -4.330  0.30 12.01 ?  42  TYR   A CA   1 
ATOM   1072 C  C    A TYR   A 1 42  ? 32.135 5.012   -2.708  0.70 10.92 ?  42  TYR   A C    1 
ATOM   1073 C  C    B TYR   A 1 42  ? 31.963 4.989   -2.881  0.30 11.62 ?  42  TYR   A C    1 
ATOM   1074 O  O    A TYR   A 1 42  ? 32.702 5.999   -2.220  0.70 11.76 ?  42  TYR   A O    1 
ATOM   1075 O  O    B TYR   A 1 42  ? 32.560 5.960   -2.404  0.30 12.07 ?  42  TYR   A O    1 
ATOM   1076 C  CB   A TYR   A 1 42  ? 32.011 5.829   -5.079  0.70 11.92 ?  42  TYR   A CB   1 
ATOM   1077 C  CB   B TYR   A 1 42  ? 31.961 5.816   -5.230  0.30 12.87 ?  42  TYR   A CB   1 
ATOM   1078 C  CG   A TYR   A 1 42  ? 32.181 5.514   -6.555  0.70 12.69 ?  42  TYR   A CG   1 
ATOM   1079 C  CG   B TYR   A 1 42  ? 32.196 5.524   -6.689  0.30 13.56 ?  42  TYR   A CG   1 
ATOM   1080 C  CD1  A TYR   A 1 42  ? 33.438 5.312   -7.097  0.70 13.53 ?  42  TYR   A CD1  1 
ATOM   1081 C  CD1  B TYR   A 1 42  ? 33.476 5.303   -7.174  0.30 14.13 ?  42  TYR   A CD1  1 
ATOM   1082 C  CD2  A TYR   A 1 42  ? 31.081 5.390   -7.398  0.70 14.41 ?  42  TYR   A CD2  1 
ATOM   1083 C  CD2  B TYR   A 1 42  ? 31.136 5.452   -7.578  0.30 14.26 ?  42  TYR   A CD2  1 
ATOM   1084 C  CE1  A TYR   A 1 42  ? 33.604 5.004   -8.438  0.70 14.24 ?  42  TYR   A CE1  1 
ATOM   1085 C  CE1  B TYR   A 1 42  ? 33.692 5.023   -8.510  0.30 14.67 ?  42  TYR   A CE1  1 
ATOM   1086 C  CE2  A TYR   A 1 42  ? 31.239 5.089   -8.742  0.70 15.41 ?  42  TYR   A CE2  1 
ATOM   1087 C  CE2  B TYR   A 1 42  ? 31.342 5.178   -8.910  0.30 15.04 ?  42  TYR   A CE2  1 
ATOM   1088 C  CZ   A TYR   A 1 42  ? 32.504 4.898   -9.255  0.70 15.36 ?  42  TYR   A CZ   1 
ATOM   1089 C  CZ   B TYR   A 1 42  ? 32.620 4.964   -9.373  0.30 15.28 ?  42  TYR   A CZ   1 
ATOM   1090 O  OH   A TYR   A 1 42  ? 32.670 4.590   -10.586 0.70 16.97 ?  42  TYR   A OH   1 
ATOM   1091 O  OH   B TYR   A 1 42  ? 32.821 4.686   -10.704 0.30 16.43 ?  42  TYR   A OH   1 
ATOM   1092 H  H    A TYR   A 1 42  ? 30.881 3.605   -4.863  0.70 12.91 ?  42  TYR   A H    1 
ATOM   1093 H  H    B TYR   A 1 42  ? 30.635 3.669   -5.056  0.30 14.04 ?  42  TYR   A H    1 
ATOM   1094 H  HA   A TYR   A 1 42  ? 33.340 4.499   -4.268  0.70 12.97 ?  42  TYR   A HA   1 
ATOM   1095 H  HA   B TYR   A 1 42  ? 33.152 4.374   -4.413  0.30 14.39 ?  42  TYR   A HA   1 
ATOM   1096 H  HB2  A TYR   A 1 42  ? 31.076 6.060   -4.928  0.70 14.28 ?  42  TYR   A HB2  1 
ATOM   1097 H  HB2  B TYR   A 1 42  ? 31.038 6.099   -5.123  0.30 15.42 ?  42  TYR   A HB2  1 
ATOM   1098 H  HB3  A TYR   A 1 42  ? 32.573 6.590   -4.871  0.70 14.28 ?  42  TYR   A HB3  1 
ATOM   1099 H  HB3  B TYR   A 1 42  ? 32.558 6.533   -4.965  0.30 15.42 ?  42  TYR   A HB3  1 
ATOM   1100 H  HD1  A TYR   A 1 42  ? 34.183 5.380   -6.548  0.70 16.21 ?  42  TYR   A HD1  1 
ATOM   1101 H  HD1  B TYR   A 1 42  ? 34.200 5.342   -6.589  0.30 16.93 ?  42  TYR   A HD1  1 
ATOM   1102 H  HD2  A TYR   A 1 42  ? 30.223 5.522   -7.058  0.70 17.27 ?  42  TYR   A HD2  1 
ATOM   1103 H  HD2  B TYR   A 1 42  ? 30.270 5.597   -7.267  0.30 17.10 ?  42  TYR   A HD2  1 
ATOM   1104 H  HE1  A TYR   A 1 42  ? 34.457 4.875   -8.784  0.70 17.06 ?  42  TYR   A HE1  1 
ATOM   1105 H  HE1  B TYR   A 1 42  ? 34.556 4.881   -8.823  0.30 17.58 ?  42  TYR   A HE1  1 
ATOM   1106 H  HE2  A TYR   A 1 42  ? 30.495 5.017   -9.298  0.70 18.47 ?  42  TYR   A HE2  1 
ATOM   1107 H  HE2  B TYR   A 1 42  ? 30.621 5.137   -9.494  0.30 18.03 ?  42  TYR   A HE2  1 
ATOM   1108 H  HH   A TYR   A 1 42  ? 33.492 4.496   -10.761 0.70 20.34 ?  42  TYR   A HH   1 
ATOM   1109 H  HH   B TYR   A 1 42  ? 33.635 4.540   -10.845 0.30 19.70 ?  42  TYR   A HH   1 
ATOM   1110 N  N    A LEU   A 1 43  ? 31.289 4.248   -2.017  0.70 10.52 ?  43  LEU   A N    1 
ATOM   1111 N  N    B LEU   A 1 43  ? 31.089 4.264   -2.181  0.30 11.01 ?  43  LEU   A N    1 
ATOM   1112 C  CA   A LEU   A 1 43  ? 30.835 4.593   -0.671  0.70 10.39 ?  43  LEU   A CA   1 
ATOM   1113 C  CA   B LEU   A 1 43  ? 30.693 4.595   -0.810  0.30 10.93 ?  43  LEU   A CA   1 
ATOM   1114 C  C    A LEU   A 1 43  ? 30.368 6.045   -0.589  0.70 10.57 ?  43  LEU   A C    1 
ATOM   1115 C  C    B LEU   A 1 43  ? 30.205 6.036   -0.691  0.30 11.07 ?  43  LEU   A C    1 
ATOM   1116 O  O    A LEU   A 1 43  ? 30.658 6.764   0.372   0.70 11.89 ?  43  LEU   A O    1 
ATOM   1117 O  O    B LEU   A 1 43  ? 30.407 6.697   0.330   0.30 10.87 ?  43  LEU   A O    1 
ATOM   1118 C  CB   A LEU   A 1 43  ? 31.883 4.288   0.396   0.70 10.92 ?  43  LEU   A CB   1 
ATOM   1119 C  CB   B LEU   A 1 43  ? 31.793 4.285   0.208   0.30 10.92 ?  43  LEU   A CB   1 
ATOM   1120 C  CG   A LEU   A 1 43  ? 32.363 2.835   0.508   0.70 11.13 ?  43  LEU   A CG   1 
ATOM   1121 C  CG   B LEU   A 1 43  ? 32.276 2.828   0.225   0.30 10.84 ?  43  LEU   A CG   1 
ATOM   1122 C  CD1  A LEU   A 1 43  ? 33.398 2.759   1.619   0.70 12.16 ?  43  LEU   A CD1  1 
ATOM   1123 C  CD1  B LEU   A 1 43  ? 33.354 2.637   1.282   0.30 10.97 ?  43  LEU   A CD1  1 
ATOM   1124 C  CD2  A LEU   A 1 43  ? 31.235 1.845   0.761   0.70 11.75 ?  43  LEU   A CD2  1 
ATOM   1125 C  CD2  B LEU   A 1 43  ? 31.119 1.854   0.443   0.30 11.24 ?  43  LEU   A CD2  1 
ATOM   1126 H  H    A LEU   A 1 43  ? 30.965 3.502   -2.311  0.70 12.60 ?  43  LEU   A H    1 
ATOM   1127 H  H    B LEU   A 1 43  ? 30.699 3.561   -2.483  0.30 13.20 ?  43  LEU   A H    1 
ATOM   1128 H  HA   A LEU   A 1 43  ? 30.064 4.036   -0.473  0.70 12.45 ?  43  LEU   A HA   1 
ATOM   1129 H  HA   B LEU   A 1 43  ? 29.938 4.034   -0.580  0.30 13.09 ?  43  LEU   A HA   1 
ATOM   1130 H  HB2  A LEU   A 1 43  ? 32.661 4.839   0.225   0.70 13.09 ?  43  LEU   A HB2  1 
ATOM   1131 H  HB2  B LEU   A 1 43  ? 32.559 4.844   0.020   0.30 13.08 ?  43  LEU   A HB2  1 
ATOM   1132 H  HB3  A LEU   A 1 43  ? 31.504 4.525   1.257   0.70 13.09 ?  43  LEU   A HB3  1 
ATOM   1133 H  HB3  B LEU   A 1 43  ? 31.455 4.487   1.098   0.30 13.08 ?  43  LEU   A HB3  1 
ATOM   1134 H  HG   A LEU   A 1 43  ? 32.803 2.587   -0.320  0.70 13.33 ?  43  LEU   A HG   1 
ATOM   1135 H  HG   B LEU   A 1 43  ? 32.673 2.625   -0.635  0.30 12.99 ?  43  LEU   A HG   1 
ATOM   1136 H  HD11 A LEU   A 1 43  ? 33.711 1.844   1.697   0.70 14.57 ?  43  LEU   A HD11 1 
ATOM   1137 H  HD11 B LEU   A 1 43  ? 33.647 1.712   1.272   0.30 13.14 ?  43  LEU   A HD11 1 
ATOM   1138 H  HD12 A LEU   A 1 43  ? 34.141 3.344   1.402   0.70 14.57 ?  43  LEU   A HD12 1 
ATOM   1139 H  HD12 B LEU   A 1 43  ? 34.102 3.222   1.081   0.30 13.14 ?  43  LEU   A HD12 1 
ATOM   1140 H  HD13 A LEU   A 1 43  ? 32.988 3.040   2.453   0.70 14.57 ?  43  LEU   A HD13 1 
ATOM   1141 H  HD13 B LEU   A 1 43  ? 32.987 2.858   2.153   0.30 13.14 ?  43  LEU   A HD13 1 
ATOM   1142 H  HD21 A LEU   A 1 43  ? 31.616 0.962   0.884   0.70 14.07 ?  43  LEU   A HD21 1 
ATOM   1143 H  HD21 B LEU   A 1 43  ? 31.479 0.968   0.599   0.30 13.46 ?  43  LEU   A HD21 1 
ATOM   1144 H  HD22 A LEU   A 1 43  ? 30.754 2.115   1.557   0.70 14.07 ?  43  LEU   A HD22 1 
ATOM   1145 H  HD22 B LEU   A 1 43  ? 30.605 2.144   1.213   0.30 13.46 ?  43  LEU   A HD22 1 
ATOM   1146 H  HD23 A LEU   A 1 43  ? 30.642 1.848   -0.005  0.70 14.07 ?  43  LEU   A HD23 1 
ATOM   1147 H  HD23 B LEU   A 1 43  ? 30.558 1.850   -0.348  0.30 13.46 ?  43  LEU   A HD23 1 
ATOM   1148 N  N    A LYS   A 1 44  ? 29.622 6.475   -1.607  0.70 10.39 ?  44  LYS   A N    1 
ATOM   1149 N  N    B LYS   A 1 44  ? 29.533 6.520   -1.733  0.30 11.65 ?  44  LYS   A N    1 
ATOM   1150 C  CA   A LYS   A 1 44  ? 28.973 7.783   -1.614  0.70 11.00 ?  44  LYS   A CA   1 
ATOM   1151 C  CA   B LYS   A 1 44  ? 28.881 7.828   -1.712  0.30 12.25 ?  44  LYS   A CA   1 
ATOM   1152 C  C    A LYS   A 1 44  ? 27.539 7.592   -1.132  0.70 10.52 ?  44  LYS   A C    1 
ATOM   1153 C  C    B LYS   A 1 44  ? 27.479 7.631   -1.157  0.30 11.17 ?  44  LYS   A C    1 
ATOM   1154 O  O    A LYS   A 1 44  ? 26.684 7.076   -1.857  0.70 11.74 ?  44  LYS   A O    1 
ATOM   1155 O  O    B LYS   A 1 44  ? 26.580 7.153   -1.854  0.30 11.37 ?  44  LYS   A O    1 
ATOM   1156 C  CB   A LYS   A 1 44  ? 29.034 8.412   -2.998  0.70 13.44 ?  44  LYS   A CB   1 
ATOM   1157 C  CB   B LYS   A 1 44  ? 28.845 8.428   -3.113  0.30 14.82 ?  44  LYS   A CB   1 
ATOM   1158 C  CG   A LYS   A 1 44  ? 30.425 8.874   -3.402  0.70 16.42 ?  44  LYS   A CG   1 
ATOM   1159 C  CG   B LYS   A 1 44  ? 30.193 8.905   -3.624  0.30 17.47 ?  44  LYS   A CG   1 
ATOM   1160 C  CD   A LYS   A 1 44  ? 31.057 9.810   -2.375  0.70 21.49 ?  44  LYS   A CD   1 
ATOM   1161 C  CD   B LYS   A 1 44  ? 30.909 9.764   -2.593  0.30 20.25 ?  44  LYS   A CD   1 
ATOM   1162 C  CE   A LYS   A 1 44  ? 32.393 10.341  -2.868  0.70 24.68 ?  44  LYS   A CE   1 
ATOM   1163 C  CE   B LYS   A 1 44  ? 32.188 10.349  -3.154  0.30 22.06 ?  44  LYS   A CE   1 
ATOM   1164 N  NZ   A LYS   A 1 44  ? 33.223 10.894  -1.762  0.70 26.34 ?  44  LYS   A NZ   1 
ATOM   1165 N  NZ   B LYS   A 1 44  ? 33.029 10.966  -2.092  0.30 23.19 ?  44  LYS   A NZ   1 
ATOM   1166 H  H    A LYS   A 1 44  ? 29.477 6.015   -2.323  0.70 12.45 ?  44  LYS   A H    1 
ATOM   1167 H  H    B LYS   A 1 44  ? 29.437 6.098   -2.475  0.30 13.96 ?  44  LYS   A H    1 
ATOM   1168 H  HA   A LYS   A 1 44  ? 29.419 8.358   -0.974  0.70 13.18 ?  44  LYS   A HA   1 
ATOM   1169 H  HA   B LYS   A 1 44  ? 29.352 8.422   -1.109  0.30 14.67 ?  44  LYS   A HA   1 
ATOM   1170 H  HB2  A LYS   A 1 44  ? 28.735 7.762   -3.651  0.70 16.11 ?  44  LYS   A HB2  1 
ATOM   1171 H  HB2  B LYS   A 1 44  ? 28.519 7.755   -3.732  0.30 17.77 ?  44  LYS   A HB2  1 
ATOM   1172 H  HB3  A LYS   A 1 44  ? 28.449 9.186   -3.011  0.70 16.11 ?  44  LYS   A HB3  1 
ATOM   1173 H  HB3  B LYS   A 1 44  ? 28.245 9.189   -3.112  0.30 17.77 ?  44  LYS   A HB3  1 
ATOM   1174 H  HG2  A LYS   A 1 44  ? 31.001 8.100   -3.498  0.70 19.69 ?  44  LYS   A HG2  1 
ATOM   1175 H  HG2  B LYS   A 1 44  ? 30.751 8.138   -3.823  0.30 20.94 ?  44  LYS   A HG2  1 
ATOM   1176 H  HG3  A LYS   A 1 44  ? 30.367 9.353   -4.245  0.70 19.69 ?  44  LYS   A HG3  1 
ATOM   1177 H  HG3  B LYS   A 1 44  ? 30.061 9.441   -4.424  0.30 20.94 ?  44  LYS   A HG3  1 
ATOM   1178 H  HD2  A LYS   A 1 44  ? 30.461 10.558  -2.214  0.70 25.77 ?  44  LYS   A HD2  1 
ATOM   1179 H  HD2  B LYS   A 1 44  ? 30.323 10.488  -2.317  0.30 24.28 ?  44  LYS   A HD2  1 
ATOM   1180 H  HD3  A LYS   A 1 44  ? 31.217 9.322   -1.551  0.70 25.77 ?  44  LYS   A HD3  1 
ATOM   1181 H  HD3  B LYS   A 1 44  ? 31.149 9.215   -1.829  0.30 24.28 ?  44  LYS   A HD3  1 
ATOM   1182 H  HE2  A LYS   A 1 44  ? 32.889 9.617   -3.283  0.70 29.60 ?  44  LYS   A HE2  1 
ATOM   1183 H  HE2  B LYS   A 1 44  ? 32.702 9.641   -3.573  0.30 26.45 ?  44  LYS   A HE2  1 
ATOM   1184 H  HE3  A LYS   A 1 44  ? 32.235 11.048  -3.512  0.70 29.60 ?  44  LYS   A HE3  1 
ATOM   1185 H  HE3  B LYS   A 1 44  ? 31.967 11.033  -3.802  0.30 26.45 ?  44  LYS   A HE3  1 
ATOM   1186 H  HZ1  A LYS   A 1 44  ? 33.995 11.198  -2.084  0.70 31.58 ?  44  LYS   A HZ1  1 
ATOM   1187 H  HZ1  B LYS   A 1 44  ? 33.772 11.300  -2.450  0.30 27.81 ?  44  LYS   A HZ1  1 
ATOM   1188 H  HZ2  A LYS   A 1 44  ? 32.791 11.567  -1.367  0.70 31.58 ?  44  LYS   A HZ2  1 
ATOM   1189 H  HZ2  B LYS   A 1 44  ? 32.580 11.622  -1.692  0.30 27.81 ?  44  LYS   A HZ2  1 
ATOM   1190 H  HZ3  A LYS   A 1 44  ? 33.387 10.263  -1.158  0.70 31.58 ?  44  LYS   A HZ3  1 
ATOM   1191 H  HZ3  B LYS   A 1 44  ? 33.250 10.355  -1.484  0.30 27.81 ?  44  LYS   A HZ3  1 
ATOM   1192 N  N    . HIS   A 1 45  ? 27.285 7.995   0.109   1.00 10.56 ?  45  HIS   A N    1 
ATOM   1193 C  CA   . HIS   A 1 45  ? 26.044 7.661   0.807   1.00 10.46 ?  45  HIS   A CA   1 
ATOM   1194 C  C    . HIS   A 1 45  ? 25.022 8.786   0.640   1.00 11.39 ?  45  HIS   A C    1 
ATOM   1195 O  O    . HIS   A 1 45  ? 24.744 9.562   1.553   1.00 13.45 ?  45  HIS   A O    1 
ATOM   1196 C  CB   . HIS   A 1 45  ? 26.338 7.401   2.272   1.00 10.50 ?  45  HIS   A CB   1 
ATOM   1197 C  CG   . HIS   A 1 45  ? 27.453 6.432   2.497   1.00 10.11 ?  45  HIS   A CG   1 
ATOM   1198 N  ND1  . HIS   A 1 45  ? 27.447 5.145   1.994   1.00 10.72 ?  45  HIS   A ND1  1 
ATOM   1199 C  CD2  . HIS   A 1 45  ? 28.617 6.580   3.175   1.00 10.85 ?  45  HIS   A CD2  1 
ATOM   1200 C  CE1  . HIS   A 1 45  ? 28.568 4.548   2.363   1.00 10.43 ?  45  HIS   A CE1  1 
ATOM   1201 N  NE2  . HIS   A 1 45  ? 29.293 5.395   3.078   1.00 10.87 ?  45  HIS   A NE2  1 
ATOM   1202 H  H    A HIS   A 1 45  ? 27.821 8.481   0.577   0.70 12.65 ?  45  HIS   A H    1 
ATOM   1203 H  H    B HIS   A 1 45  ? 27.852 8.432   0.588   0.30 12.65 ?  45  HIS   A H    1 
ATOM   1204 H  HA   . HIS   A 1 45  ? 25.668 6.854   0.424   1.00 12.53 ?  45  HIS   A HA   1 
ATOM   1205 H  HB2  . HIS   A 1 45  ? 26.572 8.242   2.699   1.00 12.58 ?  45  HIS   A HB2  1 
ATOM   1206 H  HB3  . HIS   A 1 45  ? 25.535 7.040   2.691   1.00 12.58 ?  45  HIS   A HB3  1 
ATOM   1207 H  HD2  . HIS   A 1 45  ? 28.906 7.348   3.621   1.00 12.99 ?  45  HIS   A HD2  1 
ATOM   1208 H  HE1  . HIS   A 1 45  ? 28.802 3.672   2.165   1.00 12.50 ?  45  HIS   A HE1  1 
ATOM   1209 H  HE2  . HIS   A 1 45  ? 30.059 5.226   3.427   1.00 13.02 ?  45  HIS   A HE2  1 
ATOM   1210 N  N    A GLY   A 1 46  ? 24.427 8.843   -0.547  0.70 12.77 ?  46  GLY   A N    1 
ATOM   1211 N  N    B GLY   A 1 46  ? 24.456 8.860   -0.562  0.30 11.88 ?  46  GLY   A N    1 
ATOM   1212 C  CA   A GLY   A 1 46  ? 23.595 9.981   -0.895  0.70 13.60 ?  46  GLY   A CA   1 
ATOM   1213 C  CA   B GLY   A 1 46  ? 23.648 10.007  -0.938  0.30 12.14 ?  46  GLY   A CA   1 
ATOM   1214 C  C    A GLY   A 1 46  ? 22.114 9.829   -0.614  0.70 13.78 ?  46  GLY   A C    1 
ATOM   1215 C  C    B GLY   A 1 46  ? 22.180 9.939   -0.562  0.30 11.96 ?  46  GLY   A C    1 
ATOM   1216 O  O    A GLY   A 1 46  ? 21.448 10.799  -0.233  0.70 15.09 ?  46  GLY   A O    1 
ATOM   1217 O  O    B GLY   A 1 46  ? 21.570 10.967  -0.249  0.30 12.84 ?  46  GLY   A O    1 
ATOM   1218 H  H    A GLY   A 1 46  ? 24.476 8.237   -1.155  0.70 15.30 ?  46  GLY   A H    1 
ATOM   1219 H  H    B GLY   A 1 46  ? 24.522 8.258   -1.172  0.30 14.24 ?  46  GLY   A H    1 
ATOM   1220 H  HA2  A GLY   A 1 46  ? 23.901 10.758  -0.404  0.70 16.30 ?  46  GLY   A HA2  1 
ATOM   1221 H  HA2  B GLY   A 1 46  ? 24.025 10.802  -0.527  0.30 14.55 ?  46  GLY   A HA2  1 
ATOM   1222 H  HA3  A GLY   A 1 46  ? 23.697 10.165  -1.840  0.70 16.30 ?  46  GLY   A HA3  1 
ATOM   1223 H  HA3  B GLY   A 1 46  ? 23.696 10.120  -1.899  0.30 14.55 ?  46  GLY   A HA3  1 
ATOM   1224 N  N    A GLY   A 1 47  ? 21.579 8.629   -0.819  0.70 13.13 ?  47  GLY   A N    1 
ATOM   1225 N  N    B GLY   A 1 47  ? 21.595 8.749   -0.617  0.30 11.44 ?  47  GLY   A N    1 
ATOM   1226 C  CA   A GLY   A 1 47  ? 20.150 8.417   -0.756  0.70 13.08 ?  47  GLY   A CA   1 
ATOM   1227 C  CA   B GLY   A 1 47  ? 20.185 8.583   -0.342  0.30 11.67 ?  47  GLY   A CA   1 
ATOM   1228 C  C    A GLY   A 1 47  ? 19.829 6.987   -0.377  0.70 12.72 ?  47  GLY   A C    1 
ATOM   1229 C  C    B GLY   A 1 47  ? 19.867 7.137   -0.019  0.30 11.47 ?  47  GLY   A C    1 
ATOM   1230 O  O    A GLY   A 1 47  ? 20.719 6.162   -0.157  0.70 12.68 ?  47  GLY   A O    1 
ATOM   1231 O  O    B GLY   A 1 47  ? 20.761 6.297   0.114   0.30 11.58 ?  47  GLY   A O    1 
ATOM   1232 H  H    A GLY   A 1 47  ? 22.030 7.912   -0.983  0.70 15.74 ?  47  GLY   A H    1 
ATOM   1233 H  H    B GLY   A 1 47  ? 22.002 8.021   -0.815  0.30 13.71 ?  47  GLY   A H    1 
ATOM   1234 H  HA2  A GLY   A 1 47  ? 19.752 9.012   -0.100  0.70 15.68 ?  47  GLY   A HA2  1 
ATOM   1235 H  HA2  B GLY   A 1 47  ? 19.924 9.135   0.415   0.30 13.98 ?  47  GLY   A HA2  1 
ATOM   1236 H  HA3  A GLY   A 1 47  ? 19.751 8.596   -1.622  0.70 15.68 ?  47  GLY   A HA3  1 
ATOM   1237 H  HA3  B GLY   A 1 47  ? 19.664 8.860   -1.116  0.30 13.98 ?  47  GLY   A HA3  1 
ATOM   1238 N  N    A GLY   A 1 48  ? 18.534 6.691   -0.323  0.70 12.60 ?  48  GLY   A N    1 
ATOM   1239 N  N    B GLY   A 1 48  ? 18.574 6.854   0.113   0.30 12.09 ?  48  GLY   A N    1 
ATOM   1240 C  CA   A GLY   A 1 48  ? 18.121 5.372   0.102   0.70 12.87 ?  48  GLY   A CA   1 
ATOM   1241 C  CA   B GLY   A 1 48  ? 18.146 5.510   0.450   0.30 11.72 ?  48  GLY   A CA   1 
ATOM   1242 C  C    A GLY   A 1 48  ? 18.589 5.090   1.515   0.70 12.06 ?  48  GLY   A C    1 
ATOM   1243 C  C    B GLY   A 1 48  ? 18.689 5.073   1.799   0.30 11.57 ?  48  GLY   A C    1 
ATOM   1244 O  O    A GLY   A 1 48  ? 18.732 5.997   2.349   0.70 11.94 ?  48  GLY   A O    1 
ATOM   1245 O  O    B GLY   A 1 48  ? 18.874 5.876   2.722   0.30 11.92 ?  48  GLY   A O    1 
ATOM   1246 H  H    A GLY   A 1 48  ? 17.891 7.226   -0.509  0.70 15.10 ?  48  GLY   A H    1 
ATOM   1247 H  H    B GLY   A 1 48  ? 17.936 7.419   0.016   0.30 14.48 ?  48  GLY   A H    1 
ATOM   1248 H  HA2  A GLY   A 1 48  ? 17.154 5.299   0.077   0.70 15.42 ?  48  GLY   A HA2  1 
ATOM   1249 H  HA2  B GLY   A 1 48  ? 17.176 5.473   0.467   0.30 14.04 ?  48  GLY   A HA2  1 
ATOM   1250 H  HA3  A GLY   A 1 48  ? 18.502 4.700   -0.482  0.70 15.42 ?  48  GLY   A HA3  1 
ATOM   1251 H  HA3  B GLY   A 1 48  ? 18.465 4.885   -0.223  0.30 14.04 ?  48  GLY   A HA3  1 
ATOM   1252 N  N    A VAL   A 1 49  ? 18.834 3.807   1.788   0.70 12.05 ?  49  VAL   A N    1 
ATOM   1253 N  N    B VAL   A 1 49  ? 18.942 3.766   1.914   0.30 11.02 ?  49  VAL   A N    1 
ATOM   1254 C  CA   A VAL   A 1 49  ? 19.324 3.403   3.101   0.70 11.77 ?  49  VAL   A CA   1 
ATOM   1255 C  CA   B VAL   A 1 49  ? 19.545 3.218   3.127   0.30 10.29 ?  49  VAL   A CA   1 
ATOM   1256 C  C    A VAL   A 1 49  ? 20.634 4.104   3.433   0.70 10.67 ?  49  VAL   A C    1 
ATOM   1257 C  C    B VAL   A 1 49  ? 20.828 3.964   3.464   0.30 9.59  ?  49  VAL   A C    1 
ATOM   1258 O  O    A VAL   A 1 49  ? 20.826 4.563   4.562   0.70 11.17 ?  49  VAL   A O    1 
ATOM   1259 O  O    B VAL   A 1 49  ? 21.069 4.332   4.619   0.30 9.19  ?  49  VAL   A O    1 
ATOM   1260 C  CB   A VAL   A 1 49  ? 19.454 1.867   3.167   0.70 12.42 ?  49  VAL   A CB   1 
ATOM   1261 C  CB   B VAL   A 1 49  ? 19.811 1.711   2.956   0.30 9.86  ?  49  VAL   A CB   1 
ATOM   1262 C  CG1  A VAL   A 1 49  ? 20.277 1.438   4.384   0.70 12.98 ?  49  VAL   A CG1  1 
ATOM   1263 C  CG1  B VAL   A 1 49  ? 20.698 1.203   4.084   0.30 9.64  ?  49  VAL   A CG1  1 
ATOM   1264 C  CG2  A VAL   A 1 49  ? 18.077 1.218   3.188   0.70 14.82 ?  49  VAL   A CG2  1 
ATOM   1265 C  CG2  B VAL   A 1 49  ? 18.509 0.930   2.890   0.30 9.38  ?  49  VAL   A CG2  1 
ATOM   1266 H  H    A VAL   A 1 49  ? 18.727 3.154   1.237   0.70 14.44 ?  49  VAL   A H    1 
ATOM   1267 H  H    B VAL   A 1 49  ? 18.783 3.182   1.305   0.30 13.21 ?  49  VAL   A H    1 
ATOM   1268 H  HA   A VAL   A 1 49  ? 18.680 3.663   3.774   0.70 14.10 ?  49  VAL   A HA   1 
ATOM   1269 H  HA   B VAL   A 1 49  ? 18.928 3.330   3.869   0.30 12.32 ?  49  VAL   A HA   1 
ATOM   1270 H  HB   A VAL   A 1 49  ? 19.923 1.554   2.375   0.70 14.88 ?  49  VAL   A HB   1 
ATOM   1271 H  HB   B VAL   A 1 49  ? 20.283 1.569   2.120   0.30 11.81 ?  49  VAL   A HB   1 
ATOM   1272 H  HG11 A VAL   A 1 49  ? 20.115 0.501   4.559   0.70 15.55 ?  49  VAL   A HG11 1 
ATOM   1273 H  HG11 B VAL   A 1 49  ? 20.608 0.240   4.147   0.30 11.55 ?  49  VAL   A HG11 1 
ATOM   1274 H  HG12 A VAL   A 1 49  ? 21.219 1.584   4.202   0.70 15.55 ?  49  VAL   A HG12 1 
ATOM   1275 H  HG12 B VAL   A 1 49  ? 21.623 1.433   3.892   0.30 11.55 ?  49  VAL   A HG12 1 
ATOM   1276 H  HG13 A VAL   A 1 49  ? 20.001 1.969   5.150   0.70 15.55 ?  49  VAL   A HG13 1 
ATOM   1277 H  HG13 B VAL   A 1 49  ? 20.419 1.614   4.916   0.30 11.55 ?  49  VAL   A HG13 1 
ATOM   1278 H  HG21 A VAL   A 1 49  ? 18.182 0.256   3.225   0.70 17.76 ?  49  VAL   A HG21 1 
ATOM   1279 H  HG21 B VAL   A 1 49  ? 18.709 -0.010  2.759   0.30 11.23 ?  49  VAL   A HG21 1 
ATOM   1280 H  HG22 A VAL   A 1 49  ? 17.598 1.531   3.971   0.70 17.76 ?  49  VAL   A HG22 1 
ATOM   1281 H  HG22 B VAL   A 1 49  ? 18.026 1.052   3.724   0.30 11.23 ?  49  VAL   A HG22 1 
ATOM   1282 H  HG23 A VAL   A 1 49  ? 17.602 1.473   2.383   0.70 17.76 ?  49  VAL   A HG23 1 
ATOM   1283 H  HG23 B VAL   A 1 49  ? 17.978 1.263   2.150   0.30 11.23 ?  49  VAL   A HG23 1 
ATOM   1284 N  N    A ALA   A 1 50  ? 21.561 4.164   2.470   0.70 10.14 ?  50  ALA   A N    1 
ATOM   1285 N  N    B ALA   A 1 50  ? 21.681 4.166   2.459   0.30 9.77  ?  50  ALA   A N    1 
ATOM   1286 C  CA   A ALA   A 1 50  ? 22.885 4.714   2.742   0.70 9.99  ?  50  ALA   A CA   1 
ATOM   1287 C  CA   B ALA   A 1 50  ? 22.987 4.770   2.697   0.30 9.98  ?  50  ALA   A CA   1 
ATOM   1288 C  C    A ALA   A 1 50  ? 22.803 6.177   3.159   0.70 10.20 ?  50  ALA   A C    1 
ATOM   1289 C  C    B ALA   A 1 50  ? 22.850 6.216   3.156   0.30 9.84  ?  50  ALA   A C    1 
ATOM   1290 O  O    A ALA   A 1 50  ? 23.447 6.595   4.128   0.70 10.61 ?  50  ALA   A O    1 
ATOM   1291 O  O    B ALA   A 1 50  ? 23.460 6.623   4.152   0.30 9.87  ?  50  ALA   A O    1 
ATOM   1292 C  CB   A ALA   A 1 50  ? 23.776 4.565   1.511   0.70 10.00 ?  50  ALA   A CB   1 
ATOM   1293 C  CB   B ALA   A 1 50  ? 23.832 4.687   1.428   0.30 10.08 ?  50  ALA   A CB   1 
ATOM   1294 H  H    A ALA   A 1 50  ? 21.447 3.898   1.658   0.70 12.14 ?  50  ALA   A H    1 
ATOM   1295 H  H    B ALA   A 1 50  ? 21.523 3.964   1.638   0.30 11.70 ?  50  ALA   A H    1 
ATOM   1296 H  HA   A ALA   A 1 50  ? 23.294 4.224   3.471   0.70 11.97 ?  50  ALA   A HA   1 
ATOM   1297 H  HA   B ALA   A 1 50  ? 23.440 4.280   3.397   0.30 11.95 ?  50  ALA   A HA   1 
ATOM   1298 H  HB1  A ALA   A 1 50  ? 24.653 4.938   1.705   0.70 11.97 ?  50  ALA   A HB1  1 
ATOM   1299 H  HB1  B ALA   A 1 50  ? 24.698 5.086   1.601   0.30 12.08 ?  50  ALA   A HB1  1 
ATOM   1300 H  HB2  A ALA   A 1 50  ? 23.859 3.625   1.291   0.70 11.97 ?  50  ALA   A HB2  1 
ATOM   1301 H  HB2  B ALA   A 1 50  ? 23.939 3.754   1.183   0.30 12.08 ?  50  ALA   A HB2  1 
ATOM   1302 H  HB3  A ALA   A 1 50  ? 23.374 5.045   0.768   0.70 11.97 ?  50  ALA   A HB3  1 
ATOM   1303 H  HB3  B ALA   A 1 50  ? 23.381 5.166   0.715   0.30 12.08 ?  50  ALA   A HB3  1 
ATOM   1304 N  N    A GLY   A 1 51  ? 22.024 6.975   2.432   0.70 10.53 ?  51  GLY   A N    1 
ATOM   1305 N  N    B GLY   A 1 51  ? 22.054 7.009   2.440   0.30 10.25 ?  51  GLY   A N    1 
ATOM   1306 C  CA   A GLY   A 1 51  ? 21.873 8.367   2.815   0.70 10.94 ?  51  GLY   A CA   1 
ATOM   1307 C  CA   B GLY   A 1 51  ? 21.878 8.395   2.832   0.30 10.64 ?  51  GLY   A CA   1 
ATOM   1308 C  C    A GLY   A 1 51  ? 21.271 8.513   4.198   0.70 10.72 ?  51  GLY   A C    1 
ATOM   1309 C  C    B GLY   A 1 51  ? 21.257 8.530   4.208   0.30 10.82 ?  51  GLY   A C    1 
ATOM   1310 O  O    A GLY   A 1 51  ? 21.663 9.395   4.964   0.70 11.50 ?  51  GLY   A O    1 
ATOM   1311 O  O    B GLY   A 1 51  ? 21.626 9.417   4.981   0.30 11.13 ?  51  GLY   A O    1 
ATOM   1312 H  H    A GLY   A 1 51  ? 21.590 6.737   1.727   0.70 12.62 ?  51  GLY   A H    1 
ATOM   1313 H  H    B GLY   A 1 51  ? 21.617 6.768   1.738   0.30 12.28 ?  51  GLY   A H    1 
ATOM   1314 H  HA2  A GLY   A 1 51  ? 22.738 8.801   2.805   0.70 13.11 ?  51  GLY   A HA2  1 
ATOM   1315 H  HA2  B GLY   A 1 51  ? 22.739 8.838   2.840   0.30 12.75 ?  51  GLY   A HA2  1 
ATOM   1316 H  HA3  A GLY   A 1 51  ? 21.295 8.814   2.175   0.70 13.11 ?  51  GLY   A HA3  1 
ATOM   1317 H  HA3  B GLY   A 1 51  ? 21.305 8.842   2.191   0.30 12.75 ?  51  GLY   A HA3  1 
ATOM   1318 N  N    . ALA   A 1 52  ? 20.307 7.650   4.534   1.00 10.95 ?  52  ALA   A N    1 
ATOM   1319 C  CA   . ALA   A 1 52  ? 19.665 7.710   5.844   1.00 11.62 ?  52  ALA   A CA   1 
ATOM   1320 C  C    . ALA   A 1 52  ? 20.618 7.295   6.966   1.00 10.83 ?  52  ALA   A C    1 
ATOM   1321 O  O    . ALA   A 1 52  ? 20.687 7.953   8.008   1.00 11.88 ?  52  ALA   A O    1 
ATOM   1322 C  CB   . ALA   A 1 52  ? 18.409 6.838   5.838   1.00 12.93 ?  52  ALA   A CB   1 
ATOM   1323 H  H    A ALA   A 1 52  ? 20.015 7.019   4.022   0.70 13.12 ?  52  ALA   A H    1 
ATOM   1324 H  H    B ALA   A 1 52  ? 20.027 7.014   4.022   0.30 13.12 ?  52  ALA   A H    1 
ATOM   1325 H  HA   . ALA   A 1 52  ? 19.390 8.619   6.013   1.00 13.92 ?  52  ALA   A HA   1 
ATOM   1326 H  HB1  . ALA   A 1 52  ? 17.977 6.898   6.707   1.00 15.49 ?  52  ALA   A HB1  1 
ATOM   1327 H  HB2  . ALA   A 1 52  ? 17.803 7.159   5.150   1.00 15.49 ?  52  ALA   A HB2  1 
ATOM   1328 H  HB3  . ALA   A 1 52  ? 18.655 5.918   5.656   1.00 15.49 ?  52  ALA   A HB3  1 
ATOM   1329 N  N    A LEU   A 1 53  ? 21.346 6.193   6.787   0.70 11.01 ?  53  LEU   A N    1 
ATOM   1330 N  N    B LEU   A 1 53  ? 21.356 6.198   6.770   0.30 11.01 ?  53  LEU   A N    1 
ATOM   1331 C  CA   A LEU   A 1 53  ? 22.316 5.804   7.807   0.70 10.93 ?  53  LEU   A CA   1 
ATOM   1332 C  CA   B LEU   A 1 53  ? 22.325 5.772   7.777   0.30 11.12 ?  53  LEU   A CA   1 
ATOM   1333 C  C    A LEU   A 1 53  ? 23.355 6.896   7.992   0.70 10.17 ?  53  LEU   A C    1 
ATOM   1334 C  C    B LEU   A 1 53  ? 23.391 6.836   7.992   0.30 11.03 ?  53  LEU   A C    1 
ATOM   1335 O  O    A LEU   A 1 53  ? 23.667 7.290   9.119   0.70 11.38 ?  53  LEU   A O    1 
ATOM   1336 O  O    B LEU   A 1 53  ? 23.771 7.124   9.131   0.30 11.44 ?  53  LEU   A O    1 
ATOM   1337 C  CB   A LEU   A 1 53  ? 22.989 4.475   7.446   0.70 11.21 ?  53  LEU   A CB   1 
ATOM   1338 C  CB   B LEU   A 1 53  ? 22.989 4.454   7.365   0.30 11.08 ?  53  LEU   A CB   1 
ATOM   1339 C  CG   A LEU   A 1 53  ? 22.094 3.224   7.462   0.70 12.55 ?  53  LEU   A CG   1 
ATOM   1340 C  CG   B LEU   A 1 53  ? 22.229 3.132   7.536   0.30 11.12 ?  53  LEU   A CG   1 
ATOM   1341 C  CD1  A LEU   A 1 53  ? 22.839 2.031   6.886   0.70 13.09 ?  53  LEU   A CD1  1 
ATOM   1342 C  CD1  B LEU   A 1 53  ? 23.004 2.003   6.872   0.30 11.57 ?  53  LEU   A CD1  1 
ATOM   1343 C  CD2  A LEU   A 1 53  ? 21.593 2.915   8.866   0.70 13.39 ?  53  LEU   A CD2  1 
ATOM   1344 C  CD2  B LEU   A 1 53  ? 21.985 2.807   9.001   0.30 11.24 ?  53  LEU   A CD2  1 
ATOM   1345 H  H    A LEU   A 1 53  ? 21.297 5.664   6.107   0.70 13.19 ?  53  LEU   A H    1 
ATOM   1346 H  H    B LEU   A 1 53  ? 21.315 5.691   6.076   0.30 13.20 ?  53  LEU   A H    1 
ATOM   1347 H  HA   A LEU   A 1 53  ? 21.854 5.679   8.651   0.70 13.10 ?  53  LEU   A HA   1 
ATOM   1348 H  HA   B LEU   A 1 53  ? 21.867 5.627   8.620   0.30 13.32 ?  53  LEU   A HA   1 
ATOM   1349 H  HB2  A LEU   A 1 53  ? 23.357 4.552   6.550   0.70 13.44 ?  53  LEU   A HB2  1 
ATOM   1350 H  HB2  B LEU   A 1 53  ? 23.212 4.521   6.424   0.30 13.28 ?  53  LEU   A HB2  1 
ATOM   1351 H  HB3  A LEU   A 1 53  ? 23.711 4.315   8.074   0.70 13.44 ?  53  LEU   A HB3  1 
ATOM   1352 H  HB3  B LEU   A 1 53  ? 23.807 4.364   7.875   0.30 13.28 ?  53  LEU   A HB3  1 
ATOM   1353 H  HG   A LEU   A 1 53  ? 21.321 3.386   6.897   0.70 15.03 ?  53  LEU   A HG   1 
ATOM   1354 H  HG   B LEU   A 1 53  ? 21.369 3.200   7.093   0.30 13.32 ?  53  LEU   A HG   1 
ATOM   1355 H  HD11 A LEU   A 1 53  ? 22.256 1.255   6.904   0.70 15.69 ?  53  LEU   A HD11 1 
ATOM   1356 H  HD11 B LEU   A 1 53  ? 22.515 1.172   6.990   0.30 13.87 ?  53  LEU   A HD11 1 
ATOM   1357 H  HD12 A LEU   A 1 53  ? 23.096 2.228   5.971   0.70 15.69 ?  53  LEU   A HD12 1 
ATOM   1358 H  HD12 B LEU   A 1 53  ? 23.101 2.198   5.927   0.30 13.87 ?  53  LEU   A HD12 1 
ATOM   1359 H  HD13 A LEU   A 1 53  ? 23.629 1.863   7.422   0.70 15.69 ?  53  LEU   A HD13 1 
ATOM   1360 H  HD13 B LEU   A 1 53  ? 23.878 1.934   7.287   0.30 13.87 ?  53  LEU   A HD13 1 
ATOM   1361 H  HD21 A LEU   A 1 53  ? 21.076 2.095   8.844   0.70 16.05 ?  53  LEU   A HD21 1 
ATOM   1362 H  HD21 B LEU   A 1 53  ? 21.449 1.999   9.060   0.30 13.47 ?  53  LEU   A HD21 1 
ATOM   1363 H  HD22 A LEU   A 1 53  ? 22.356 2.809   9.456   0.70 16.05 ?  53  LEU   A HD22 1 
ATOM   1364 H  HD22 B LEU   A 1 53  ? 22.837 2.671   9.441   0.30 13.47 ?  53  LEU   A HD22 1 
ATOM   1365 H  HD23 A LEU   A 1 53  ? 21.037 3.648   9.172   0.70 16.05 ?  53  LEU   A HD23 1 
ATOM   1366 H  HD23 B LEU   A 1 53  ? 21.511 3.545   9.414   0.30 13.47 ?  53  LEU   A HD23 1 
ATOM   1367 N  N    A ASN   A 1 54  ? 23.891 7.408   6.890   0.70 10.12 ?  54  ASN   A N    1 
ATOM   1368 N  N    B ASN   A 1 54  ? 23.898 7.419   6.907   0.30 11.03 ?  54  ASN   A N    1 
ATOM   1369 C  CA   A ASN   A 1 54  ? 24.941 8.408   7.014   0.70 10.26 ?  54  ASN   A CA   1 
ATOM   1370 C  CA   B ASN   A 1 54  ? 24.949 8.418   7.050   0.30 11.03 ?  54  ASN   A CA   1 
ATOM   1371 C  C    A ASN   A 1 54  ? 24.435 9.656   7.735   0.70 10.91 ?  54  ASN   A C    1 
ATOM   1372 C  C    B ASN   A 1 54  ? 24.432 9.669   7.748   0.30 11.16 ?  54  ASN   A C    1 
ATOM   1373 O  O    A ASN   A 1 54  ? 25.124 10.201  8.605   0.70 11.07 ?  54  ASN   A O    1 
ATOM   1374 O  O    B ASN   A 1 54  ? 25.119 10.236  8.606   0.30 11.19 ?  54  ASN   A O    1 
ATOM   1375 C  CB   A ASN   A 1 54  ? 25.505 8.759   5.647   0.70 10.55 ?  54  ASN   A CB   1 
ATOM   1376 C  CB   B ASN   A 1 54  ? 25.544 8.769   5.691   0.30 11.25 ?  54  ASN   A CB   1 
ATOM   1377 C  CG   A ASN   A 1 54  ? 26.527 9.849   5.746   0.70 10.72 ?  54  ASN   A CG   1 
ATOM   1378 C  CG   B ASN   A 1 54  ? 26.533 9.907   5.786   0.30 11.22 ?  54  ASN   A CG   1 
ATOM   1379 O  OD1  A ASN   A 1 54  ? 27.514 9.710   6.476   0.70 10.74 ?  54  ASN   A OD1  1 
ATOM   1380 O  OD1  B ASN   A 1 54  ? 27.585 9.772   6.411   0.30 11.45 ?  54  ASN   A OD1  1 
ATOM   1381 N  ND2  A ASN   A 1 54  ? 26.297 10.953  5.053   0.70 11.36 ?  54  ASN   A ND2  1 
ATOM   1382 N  ND2  B ASN   A 1 54  ? 26.196 11.044  5.189   0.30 11.35 ?  54  ASN   A ND2  1 
ATOM   1383 H  H    A ASN   A 1 54  ? 23.667 7.201   6.087   0.70 12.13 ?  54  ASN   A H    1 
ATOM   1384 H  H    B ASN   A 1 54  ? 23.654 7.254   6.101   0.30 13.22 ?  54  ASN   A H    1 
ATOM   1385 H  HA   A ASN   A 1 54  ? 25.658 8.036   7.545   0.70 12.29 ?  54  ASN   A HA   1 
ATOM   1386 H  HA   B ASN   A 1 54  ? 25.656 8.048   7.598   0.30 13.21 ?  54  ASN   A HA   1 
ATOM   1387 H  HB2  A ASN   A 1 54  ? 25.931 7.968   5.270   0.70 12.65 ?  54  ASN   A HB2  1 
ATOM   1388 H  HB2  B ASN   A 1 54  ? 26.007 7.989   5.340   0.30 13.48 ?  54  ASN   A HB2  1 
ATOM   1389 H  HB3  A ASN   A 1 54  ? 24.788 9.059   5.070   0.70 12.65 ?  54  ASN   A HB3  1 
ATOM   1390 H  HB3  B ASN   A 1 54  ? 24.831 9.032   5.089   0.30 13.48 ?  54  ASN   A HB3  1 
ATOM   1391 H  HD21 A ASN   A 1 54  ? 26.857 11.603  5.088   0.70 13.61 ?  54  ASN   A HD21 1 
ATOM   1392 H  HD21 B ASN   A 1 54  ? 26.730 11.718  5.222   0.30 13.60 ?  54  ASN   A HD21 1 
ATOM   1393 H  HD22 A ASN   A 1 54  ? 25.591 11.015  4.569   0.70 13.61 ?  54  ASN   A HD22 1 
ATOM   1394 H  HD22 B ASN   A 1 54  ? 25.451 11.103  4.767   0.30 13.60 ?  54  ASN   A HD22 1 
ATOM   1395 N  N    . LYS   A 1 55  ? 23.222 10.116  7.398   1.00 11.15 ?  55  LYS   A N    1 
ATOM   1396 C  CA   . LYS   A 1 55  ? 22.642 11.274  8.069   1.00 11.73 ?  55  LYS   A CA   1 
ATOM   1397 C  C    . LYS   A 1 55  ? 22.548 11.040  9.573   1.00 11.87 ?  55  LYS   A C    1 
ATOM   1398 O  O    . LYS   A 1 55  ? 22.836 11.941  10.372  1.00 12.54 ?  55  LYS   A O    1 
ATOM   1399 C  CB   . LYS   A 1 55  ? 21.271 11.568  7.456   1.00 12.72 ?  55  LYS   A CB   1 
ATOM   1400 C  CG   . LYS   A 1 55  ? 20.505 12.710  8.099   1.00 14.05 ?  55  LYS   A CG   1 
ATOM   1401 C  CD   . LYS   A 1 55  ? 19.174 12.936  7.368   1.00 15.66 ?  55  LYS   A CD   1 
ATOM   1402 C  CE   . LYS   A 1 55  ? 18.322 14.014  8.026   1.00 17.60 ?  55  LYS   A CE   1 
ATOM   1403 N  NZ   . LYS   A 1 55  ? 16.976 14.141  7.385   1.00 18.87 ?  55  LYS   A NZ   1 
ATOM   1404 H  H    A LYS   A 1 55  ? 22.715 9.765   6.795   0.70 13.36 ?  55  LYS   A H    1 
ATOM   1405 H  H    B LYS   A 1 55  ? 22.719 9.761   6.794   0.30 13.36 ?  55  LYS   A H    1 
ATOM   1406 H  HA   . LYS   A 1 55  ? 23.211 12.043  7.919   1.00 14.05 ?  55  LYS   A HA   1 
ATOM   1407 H  HB2  . LYS   A 1 55  ? 21.394 11.797  6.520   1.00 15.24 ?  55  LYS   A HB2  1 
ATOM   1408 H  HB3  . LYS   A 1 55  ? 20.721 10.773  7.525   1.00 15.24 ?  55  LYS   A HB3  1 
ATOM   1409 H  HG2  . LYS   A 1 55  ? 20.304 12.488  9.024   1.00 16.84 ?  55  LYS   A HG2  1 
ATOM   1410 H  HG3  . LYS   A 1 55  ? 21.023 13.524  8.048   1.00 16.84 ?  55  LYS   A HG3  1 
ATOM   1411 H  HD2  . LYS   A 1 55  ? 19.360 13.210  6.455   1.00 18.77 ?  55  LYS   A HD2  1 
ATOM   1412 H  HD3  . LYS   A 1 55  ? 18.668 12.106  7.367   1.00 18.77 ?  55  LYS   A HD3  1 
ATOM   1413 H  HE2  . LYS   A 1 55  ? 18.192 13.788  8.960   1.00 21.10 ?  55  LYS   A HE2  1 
ATOM   1414 H  HE3  . LYS   A 1 55  ? 18.777 14.867  7.949   1.00 21.10 ?  55  LYS   A HE3  1 
ATOM   1415 H  HZ1  . LYS   A 1 55  ? 16.430 14.605  7.914   1.00 22.62 ?  55  LYS   A HZ1  1 
ATOM   1416 H  HZ2  . LYS   A 1 55  ? 17.048 14.566  6.605   1.00 22.62 ?  55  LYS   A HZ2  1 
ATOM   1417 H  HZ3  . LYS   A 1 55  ? 16.625 13.335  7.245   1.00 22.62 ?  55  LYS   A HZ3  1 
ATOM   1418 N  N    . ALA   A 1 56  ? 22.162 9.824   9.977   1.00 12.29 ?  56  ALA   A N    1 
ATOM   1419 C  CA   . ALA   A 1 56  ? 22.041 9.503   11.391  1.00 13.17 ?  56  ALA   A CA   1 
ATOM   1420 C  C    . ALA   A 1 56  ? 23.382 9.532   12.116  1.00 13.03 ?  56  ALA   A C    1 
ATOM   1421 O  O    . ALA   A 1 56  ? 23.405 9.711   13.337  1.00 14.30 ?  56  ALA   A O    1 
ATOM   1422 C  CB   . ALA   A 1 56  ? 21.357 8.144   11.566  1.00 13.61 ?  56  ALA   A CB   1 
ATOM   1423 H  H    . ALA   A 1 56  ? 21.966 9.180   9.446   1.00 14.72 ?  56  ALA   A H    1 
ATOM   1424 H  HA   . ALA   A 1 56  ? 21.476 10.161  11.810  1.00 15.79 ?  56  ALA   A HA   1 
ATOM   1425 H  HB1  . ALA   A 1 56  ? 21.287 7.944   12.515  1.00 16.31 ?  56  ALA   A HB1  1 
ATOM   1426 H  HB2  . ALA   A 1 56  ? 20.471 8.183   11.173  1.00 16.31 ?  56  ALA   A HB2  1 
ATOM   1427 H  HB3  . ALA   A 1 56  ? 21.885 7.459   11.126  1.00 16.31 ?  56  ALA   A HB3  1 
ATOM   1428 N  N    . THR   A 1 57  ? 24.496 9.347   11.400  1.00 12.24 ?  57  THR   A N    1 
ATOM   1429 C  CA   . THR   A 1 57  ? 25.838 9.476   11.973  1.00 12.09 ?  57  THR   A CA   1 
ATOM   1430 C  C    . THR   A 1 57  ? 26.391 10.893  11.886  1.00 12.37 ?  57  THR   A C    1 
ATOM   1431 O  O    . THR   A 1 57  ? 27.578 11.103  12.174  1.00 12.96 ?  57  THR   A O    1 
ATOM   1432 C  CB   . THR   A 1 57  ? 26.847 8.521   11.306  1.00 12.22 ?  57  THR   A CB   1 
ATOM   1433 O  OG1  . THR   A 1 57  ? 27.225 9.010   10.007  1.00 12.00 ?  57  THR   A OG1  1 
ATOM   1434 C  CG2  . THR   A 1 57  ? 26.313 7.109   11.215  1.00 12.09 ?  57  THR   A CG2  1 
ATOM   1435 H  H    . THR   A 1 57  ? 24.502 9.120   10.570  1.00 14.67 ?  57  THR   A H    1 
ATOM   1436 H  HA   . THR   A 1 57  ? 25.795 9.227   12.914  1.00 14.48 ?  57  THR   A HA   1 
ATOM   1437 H  HB   . THR   A 1 57  ? 27.646 8.485   11.861  1.00 14.64 ?  57  THR   A HB   1 
ATOM   1438 H  HG1  . THR   A 1 57  ? 26.545 9.069   9.516   1.00 14.37 ?  57  THR   A HG1  1 
ATOM   1439 H  HG21 . THR   A 1 57  ? 26.985 6.518   10.841  1.00 14.49 ?  57  THR   A HG21 1 
ATOM   1440 H  HG22 . THR   A 1 57  ? 26.068 6.786   12.098  1.00 14.49 ?  57  THR   A HG22 1 
ATOM   1441 H  HG23 . THR   A 1 57  ? 25.527 7.085   10.648  1.00 14.49 ?  57  THR   A HG23 1 
ATOM   1442 N  N    . ASN   A 1 58  ? 25.572 11.864  11.487  1.00 12.89 ?  58  ASN   A N    1 
ATOM   1443 C  CA   . ASN   A 1 58  ? 26.038 13.245  11.385  1.00 13.82 ?  58  ASN   A CA   1 
ATOM   1444 C  C    . ASN   A 1 58  ? 27.192 13.362  10.384  1.00 12.58 ?  58  ASN   A C    1 
ATOM   1445 O  O    . ASN   A 1 58  ? 28.084 14.200  10.535  1.00 13.47 ?  58  ASN   A O    1 
ATOM   1446 C  CB   . ASN   A 1 58  ? 26.402 13.788  12.779  1.00 16.99 ?  58  ASN   A CB   1 
ATOM   1447 C  CG   . ASN   A 1 58  ? 26.807 15.244  12.773  1.00 20.77 ?  58  ASN   A CG   1 
ATOM   1448 O  OD1  . ASN   A 1 58  ? 26.174 16.064  12.122  1.00 22.86 ?  58  ASN   A OD1  1 
ATOM   1449 N  ND2  . ASN   A 1 58  ? 27.866 15.575  13.517  1.00 22.30 ?  58  ASN   A ND2  1 
ATOM   1450 H  H    . ASN   A 1 58  ? 24.750 11.740  11.253  1.00 15.44 ?  58  ASN   A H    1 
ATOM   1451 H  HA   . ASN   A 1 58  ? 25.304 13.777  11.046  1.00 16.57 ?  58  ASN   A HA   1 
ATOM   1452 H  HB2  . ASN   A 1 58  ? 25.622 13.693  13.363  1.00 20.37 ?  58  ASN   A HB2  1 
ATOM   1453 H  HB3  . ASN   A 1 58  ? 27.138 13.281  13.140  1.00 20.37 ?  58  ASN   A HB3  1 
ATOM   1454 H  HD21 . ASN   A 1 58  ? 28.129 16.396  13.553  1.00 26.74 ?  58  ASN   A HD21 1 
ATOM   1455 H  HD22 . ASN   A 1 58  ? 28.280 14.971  13.958  1.00 26.74 ?  58  ASN   A HD22 1 
ATOM   1456 N  N    . ASN   A 1 59  ? 27.171 12.543  9.330   1.00 11.62 ?  59  ASN   A N    1 
ATOM   1457 C  CA   . ASN   A 1 59  ? 28.148 12.520  8.234   1.00 11.42 ?  59  ASN   A CA   1 
ATOM   1458 C  C    . ASN   A 1 59  ? 29.465 11.836  8.621   1.00 11.52 ?  59  ASN   A C    1 
ATOM   1459 O  O    . ASN   A 1 59  ? 30.384 11.792  7.792   1.00 11.38 ?  59  ASN   A O    1 
ATOM   1460 C  CB   . ASN   A 1 59  ? 28.437 13.907  7.625   1.00 11.59 ?  59  ASN   A CB   1 
ATOM   1461 C  CG   . ASN   A 1 59  ? 28.795 13.831  6.154   1.00 11.77 ?  59  ASN   A CG   1 
ATOM   1462 O  OD1  . ASN   A 1 59  ? 28.083 13.206  5.359   1.00 11.94 ?  59  ASN   A OD1  1 
ATOM   1463 N  ND2  . ASN   A 1 59  ? 29.886 14.489  5.773   1.00 12.59 ?  59  ASN   A ND2  1 
ATOM   1464 H  H    . ASN   A 1 59  ? 26.555 11.952  9.214   1.00 13.93 ?  59  ASN   A H    1 
ATOM   1465 H  HA   . ASN   A 1 59  ? 27.768 11.989  7.523   1.00 13.68 ?  59  ASN   A HA   1 
ATOM   1466 H  HB2  . ASN   A 1 59  ? 27.649 14.465  7.707   1.00 13.89 ?  59  ASN   A HB2  1 
ATOM   1467 H  HB3  . ASN   A 1 59  ? 29.185 14.314  8.087   1.00 13.89 ?  59  ASN   A HB3  1 
ATOM   1468 H  HD21 . ASN   A 1 59  ? 30.129 14.476  4.946   1.00 15.09 ?  59  ASN   A HD21 1 
ATOM   1469 H  HD22 . ASN   A 1 59  ? 30.359 14.914  6.351   1.00 15.09 ?  59  ASN   A HD22 1 
ATOM   1470 N  N    . ALA   A 1 60  ? 29.591 11.288  9.830   1.00 11.60 ?  60  ALA   A N    1 
ATOM   1471 C  CA   . ALA   A 1 60  ? 30.829 10.605  10.187  1.00 11.61 ?  60  ALA   A CA   1 
ATOM   1472 C  C    . ALA   A 1 60  ? 31.050 9.365   9.324   1.00 11.46 ?  60  ALA   A C    1 
ATOM   1473 O  O    . ALA   A 1 60  ? 32.195 9.038   8.984   1.00 11.87 ?  60  ALA   A O    1 
ATOM   1474 C  CB   . ALA   A 1 60  ? 30.822 10.240  11.670  1.00 12.46 ?  60  ALA   A CB   1 
ATOM   1475 H  H    . ALA   A 1 60  ? 28.991 11.294  10.446  1.00 13.90 ?  60  ALA   A H    1 
ATOM   1476 H  HA   . ALA   A 1 60  ? 31.575 11.206  10.033  1.00 13.91 ?  60  ALA   A HA   1 
ATOM   1477 H  HB1  . ALA   A 1 60  ? 31.651 9.791   11.891  1.00 14.93 ?  60  ALA   A HB1  1 
ATOM   1478 H  HB2  . ALA   A 1 60  ? 30.741 11.058  12.192  1.00 14.93 ?  60  ALA   A HB2  1 
ATOM   1479 H  HB3  . ALA   A 1 60  ? 30.068 9.660   11.850  1.00 14.93 ?  60  ALA   A HB3  1 
ATOM   1480 N  N    . MET   A 1 61  ? 29.975 8.675   8.942   1.00 10.74 ?  61  MET   A N    1 
ATOM   1481 C  CA   . MET   A 1 61  ? 30.110 7.540   8.032   1.00 10.72 ?  61  MET   A CA   1 
ATOM   1482 C  C    . MET   A 1 61  ? 30.745 7.962   6.710   1.00 10.73 ?  61  MET   A C    1 
ATOM   1483 O  O    . MET   A 1 61  ? 31.631 7.274   6.187   1.00 11.18 ?  61  MET   A O    1 
ATOM   1484 C  CB   . MET   A 1 61  ? 28.743 6.884   7.808   1.00 10.68 ?  61  MET   A CB   1 
ATOM   1485 C  CG   . MET   A 1 61  ? 28.761 5.701   6.845   1.00 11.40 ?  61  MET   A CG   1 
ATOM   1486 S  SD   . MET   A 1 61  ? 27.131 4.957   6.650   1.00 12.21 ?  61  MET   A SD   1 
ATOM   1487 C  CE   . MET   A 1 61  ? 27.020 4.079   8.212   1.00 13.92 ?  61  MET   A CE   1 
ATOM   1488 H  H    . MET   A 1 61  ? 29.170 8.843   9.187   1.00 12.86 ?  61  MET   A H    1 
ATOM   1489 H  HA   . MET   A 1 61  ? 30.682 6.878   8.449   1.00 12.84 ?  61  MET   A HA   1 
ATOM   1490 H  HB2  . MET   A 1 61  ? 28.409 6.568   8.659   1.00 12.80 ?  61  MET   A HB2  1 
ATOM   1491 H  HB3  . MET   A 1 61  ? 28.137 7.549   7.445   1.00 12.80 ?  61  MET   A HB3  1 
ATOM   1492 H  HG2  . MET   A 1 61  ? 29.049 5.999   5.969   1.00 13.66 ?  61  MET   A HG2  1 
ATOM   1493 H  HG3  . MET   A 1 61  ? 29.361 5.021   7.184   1.00 13.66 ?  61  MET   A HG3  1 
ATOM   1494 H  HE1  . MET   A 1 61  ? 26.187 3.587   8.242   1.00 16.68 ?  61  MET   A HE1  1 
ATOM   1495 H  HE2  . MET   A 1 61  ? 27.771 3.467   8.284   1.00 16.68 ?  61  MET   A HE2  1 
ATOM   1496 H  HE3  . MET   A 1 61  ? 27.051 4.722   8.941   1.00 16.68 ?  61  MET   A HE3  1 
ATOM   1497 N  N    . GLN   A 1 62  ? 30.301 9.088   6.148   1.00 10.71 ?  62  GLN   A N    1 
ATOM   1498 C  CA   . GLN   A 1 62  ? 30.868 9.560   4.888   1.00 10.92 ?  62  GLN   A CA   1 
ATOM   1499 C  C    . GLN   A 1 62  ? 32.338 9.935   5.037   1.00 10.95 ?  62  GLN   A C    1 
ATOM   1500 O  O    . GLN   A 1 62  ? 33.147 9.628   4.154   1.00 11.29 ?  62  GLN   A O    1 
ATOM   1501 C  CB   . GLN   A 1 62  ? 30.057 10.740  4.347   1.00 11.29 ?  62  GLN   A CB   1 
ATOM   1502 C  CG   . GLN   A 1 62  ? 30.440 11.110  2.926   1.00 11.28 ?  62  GLN   A CG   1 
ATOM   1503 C  CD   . GLN   A 1 62  ? 30.115 9.979   1.974   1.00 11.06 ?  62  GLN   A CD   1 
ATOM   1504 O  OE1  . GLN   A 1 62  ? 28.933 9.674   1.756   1.00 11.64 ?  62  GLN   A OE1  1 
ATOM   1505 N  NE2  . GLN   A 1 62  ? 31.140 9.313   1.448   1.00 11.70 ?  62  GLN   A NE2  1 
ATOM   1506 H  H    . GLN   A 1 62  ? 29.677 9.581   6.473   1.00 12.84 ?  62  GLN   A H    1 
ATOM   1507 H  HA   . GLN   A 1 62  ? 30.813 8.838   4.243   1.00 13.09 ?  62  GLN   A HA   1 
ATOM   1508 H  HB2  . GLN   A 1 62  ? 29.115 10.510  4.358   1.00 13.53 ?  62  GLN   A HB2  1 
ATOM   1509 H  HB3  . GLN   A 1 62  ? 30.214 11.515  4.913   1.00 13.53 ?  62  GLN   A HB3  1 
ATOM   1510 H  HG2  . GLN   A 1 62  ? 29.934 11.889  2.656   1.00 13.51 ?  62  GLN   A HG2  1 
ATOM   1511 H  HG3  . GLN   A 1 62  ? 31.390 11.287  2.885   1.00 13.51 ?  62  GLN   A HG3  1 
ATOM   1512 H  HE21 . GLN   A 1 62  ? 31.946 9.543   1.641   1.00 14.02 ?  62  GLN   A HE21 1 
ATOM   1513 H  HE22 . GLN   A 1 62  ? 30.996 8.656   0.915   1.00 14.02 ?  62  GLN   A HE22 1 
ATOM   1514 N  N    . VAL   A 1 63  ? 32.701 10.610  6.131   1.00 11.53 ?  63  VAL   A N    1 
ATOM   1515 C  CA   . VAL   A 1 63  ? 34.095 11.004  6.339   1.00 12.52 ?  63  VAL   A CA   1 
ATOM   1516 C  C    . VAL   A 1 63  ? 34.993 9.770   6.403   1.00 11.60 ?  63  VAL   A C    1 
ATOM   1517 O  O    . VAL   A 1 63  ? 36.040 9.697   5.743   1.00 12.23 ?  63  VAL   A O    1 
ATOM   1518 C  CB   . VAL   A 1 63  ? 34.202 11.885  7.597   1.00 14.18 ?  63  VAL   A CB   1 
ATOM   1519 C  CG1  . VAL   A 1 63  ? 35.650 12.128  7.960   1.00 16.12 ?  63  VAL   A CG1  1 
ATOM   1520 C  CG2  . VAL   A 1 63  ? 33.466 13.209  7.378   1.00 14.76 ?  63  VAL   A CG2  1 
ATOM   1521 H  H    . VAL   A 1 63  ? 32.159 10.852  6.760   1.00 13.81 ?  63  VAL   A H    1 
ATOM   1522 H  HA   . VAL   A 1 63  ? 34.376 11.539  5.584   1.00 15.00 ?  63  VAL   A HA   1 
ATOM   1523 H  HB   . VAL   A 1 63  ? 33.783 11.429  8.343   1.00 17.00 ?  63  VAL   A HB   1 
ATOM   1524 H  HG11 . VAL   A 1 63  ? 35.696 12.863  8.596   1.00 19.33 ?  63  VAL   A HG11 1 
ATOM   1525 H  HG12 . VAL   A 1 63  ? 36.021 11.328  8.356   1.00 19.33 ?  63  VAL   A HG12 1 
ATOM   1526 H  HG13 . VAL   A 1 63  ? 36.142 12.364  7.156   1.00 19.33 ?  63  VAL   A HG13 1 
ATOM   1527 H  HG21 . VAL   A 1 63  ? 33.560 13.757  8.174   1.00 17.69 ?  63  VAL   A HG21 1 
ATOM   1528 H  HG22 . VAL   A 1 63  ? 33.856 13.664  6.615   1.00 17.69 ?  63  VAL   A HG22 1 
ATOM   1529 H  HG23 . VAL   A 1 63  ? 32.529 13.025  7.212   1.00 17.69 ?  63  VAL   A HG23 1 
ATOM   1530 N  N    . GLU   A 1 64  ? 34.571 8.765   7.173   1.00 11.89 ?  64  GLU   A N    1 
ATOM   1531 C  CA   . GLU   A 1 64  ? 35.328 7.526   7.271   1.00 12.02 ?  64  GLU   A CA   1 
ATOM   1532 C  C    . GLU   A 1 64  ? 35.416 6.834   5.917   1.00 11.50 ?  64  GLU   A C    1 
ATOM   1533 O  O    . GLU   A 1 64  ? 36.466 6.277   5.547   1.00 11.98 ?  64  GLU   A O    1 
ATOM   1534 C  CB   . GLU   A 1 64  ? 34.634 6.617   8.285   1.00 12.20 ?  64  GLU   A CB   1 
ATOM   1535 C  CG   . GLU   A 1 64  ? 35.278 5.268   8.427   1.00 12.95 ?  64  GLU   A CG   1 
ATOM   1536 C  CD   . GLU   A 1 64  ? 34.397 4.276   9.162   1.00 13.94 ?  64  GLU   A CD   1 
ATOM   1537 O  OE1  . GLU   A 1 64  ? 33.160 4.363   9.028   1.00 14.22 ?  64  GLU   A OE1  1 
ATOM   1538 O  OE2  . GLU   A 1 64  ? 34.941 3.390   9.854   1.00 14.00 -1 64  GLU   A OE2  1 
ATOM   1539 H  H    . GLU   A 1 64  ? 33.845 8.774   7.637   1.00 14.25 ?  64  GLU   A H    1 
ATOM   1540 H  HA   . GLU   A 1 64  ? 36.227 7.722   7.589   1.00 14.40 ?  64  GLU   A HA   1 
ATOM   1541 H  HB2  . GLU   A 1 64  ? 34.658 7.051   9.159   1.00 14.62 ?  64  GLU   A HB2  1 
ATOM   1542 H  HB3  . GLU   A 1 64  ? 33.715 6.493   8.009   1.00 14.62 ?  64  GLU   A HB3  1 
ATOM   1543 H  HG2  . GLU   A 1 64  ? 35.466 4.902   7.544   1.00 15.52 ?  64  GLU   A HG2  1 
ATOM   1544 H  HG3  . GLU   A 1 64  ? 36.102 5.364   8.922   1.00 15.52 ?  64  GLU   A HG3  1 
ATOM   1545 N  N    . SER   A 1 65  ? 34.299 6.835   5.180   1.00 11.03 ?  65  SER   A N    1 
ATOM   1546 C  CA   . SER   A 1 65  ? 34.244 6.169   3.882   1.00 11.08 ?  65  SER   A CA   1 
ATOM   1547 C  C    . SER   A 1 65  ? 35.166 6.837   2.870   1.00 11.39 ?  65  SER   A C    1 
ATOM   1548 O  O    . SER   A 1 65  ? 35.807 6.153   2.064   1.00 12.14 ?  65  SER   A O    1 
ATOM   1549 C  CB   . SER   A 1 65  ? 32.810 6.173   3.348   1.00 10.92 ?  65  SER   A CB   1 
ATOM   1550 O  OG   . SER   A 1 65  ? 31.955 5.359   4.141   1.00 11.60 ?  65  SER   A OG   1 
ATOM   1551 H  H    . SER   A 1 65  ? 33.565 7.218   5.411   1.00 13.22 ?  65  SER   A H    1 
ATOM   1552 H  HA   . SER   A 1 65  ? 34.527 5.250   3.983   1.00 13.27 ?  65  SER   A HA   1 
ATOM   1553 H  HB2  . SER   A 1 65  ? 32.471 7.080   3.357   1.00 13.08 ?  65  SER   A HB2  1 
ATOM   1554 H  HB3  . SER   A 1 65  ? 32.815 5.831   2.441   1.00 13.08 ?  65  SER   A HB3  1 
ATOM   1555 H  HG   . SER   A 1 65  ? 31.944 5.643   4.936   1.00 13.90 ?  65  SER   A HG   1 
ATOM   1556 N  N    . ASP   A 1 66  ? 35.243 8.171   2.891   1.00 11.32 ?  66  ASP   A N    1 
ATOM   1557 C  CA   . ASP   A 1 66  ? 36.106 8.863   1.943   1.00 12.15 ?  66  ASP   A CA   1 
ATOM   1558 C  C    . ASP   A 1 66  ? 37.568 8.503   2.180   1.00 12.15 ?  66  ASP   A C    1 
ATOM   1559 O  O    . ASP   A 1 66  ? 38.338 8.331   1.228   1.00 13.14 ?  66  ASP   A O    1 
ATOM   1560 C  CB   . ASP   A 1 66  ? 35.896 10.372  2.045   1.00 13.70 ?  66  ASP   A CB   1 
ATOM   1561 C  CG   . ASP   A 1 66  ? 34.557 10.838  1.454   1.00 15.82 ?  66  ASP   A CG   1 
ATOM   1562 O  OD1  . ASP   A 1 66  ? 33.828 10.045  0.823   1.00 15.46 ?  66  ASP   A OD1  1 
ATOM   1563 O  OD2  . ASP   A 1 66  ? 34.266 12.040  1.601   1.00 18.61 -1 66  ASP   A OD2  1 
ATOM   1564 H  H    . ASP   A 1 66  ? 34.806 8.684   3.431   1.00 13.56 ?  66  ASP   A H    1 
ATOM   1565 H  HA   . ASP   A 1 66  ? 35.869 8.588   1.045   1.00 14.56 ?  66  ASP   A HA   1 
ATOM   1566 H  HB2  . ASP   A 1 66  ? 35.905 10.636  2.976   1.00 16.42 ?  66  ASP   A HB2  1 
ATOM   1567 H  HB3  . ASP   A 1 66  ? 36.612 10.823  1.565   1.00 16.42 ?  66  ASP   A HB3  1 
ATOM   1568 N  N    . ASP   A 1 67  ? 37.969 8.368   3.445   1.00 12.62 ?  67  ASP   A N    1 
ATOM   1569 C  CA   . ASP   A 1 67  ? 39.322 7.917   3.742   1.00 13.39 ?  67  ASP   A CA   1 
ATOM   1570 C  C    . ASP   A 1 67  ? 39.540 6.480   3.276   1.00 13.25 ?  67  ASP   A C    1 
ATOM   1571 O  O    . ASP   A 1 67  ? 40.604 6.153   2.731   1.00 13.80 ?  67  ASP   A O    1 
ATOM   1572 C  CB   . ASP   A 1 67  ? 39.597 8.060   5.238   1.00 14.37 ?  67  ASP   A CB   1 
ATOM   1573 C  CG   . ASP   A 1 67  ? 40.887 7.393   5.657   1.00 15.60 ?  67  ASP   A CG   1 
ATOM   1574 O  OD1  . ASP   A 1 67  ? 41.961 8.030   5.520   1.00 19.08 ?  67  ASP   A OD1  1 
ATOM   1575 O  OD2  . ASP   A 1 67  ? 40.829 6.228   6.121   1.00 15.85 -1 67  ASP   A OD2  1 
ATOM   1576 H  H    . ASP   A 1 67  ? 37.483 8.531   4.133   1.00 15.12 ?  67  ASP   A H    1 
ATOM   1577 H  HA   . ASP   A 1 67  ? 39.952 8.485   3.267   1.00 16.04 ?  67  ASP   A HA   1 
ATOM   1578 H  HB2  . ASP   A 1 67  ? 39.658 8.997   5.458   1.00 17.22 ?  67  ASP   A HB2  1 
ATOM   1579 H  HB3  . ASP   A 1 67  ? 38.869 7.644   5.729   1.00 17.22 ?  67  ASP   A HB3  1 
ATOM   1580 N  N    . TYR   A 1 68  ? 38.542 5.604   3.471   1.00 12.92 ?  68  TYR   A N    1 
ATOM   1581 C  CA   . TYR   A 1 68  ? 38.655 4.224   2.996   1.00 12.99 ?  68  TYR   A CA   1 
ATOM   1582 C  C    . TYR   A 1 68  ? 38.902 4.180   1.488   1.00 12.47 ?  68  TYR   A C    1 
ATOM   1583 O  O    . TYR   A 1 68  ? 39.778 3.445   1.012   1.00 12.91 ?  68  TYR   A O    1 
ATOM   1584 C  CB   . TYR   A 1 68  ? 37.406 3.406   3.372   1.00 13.39 ?  68  TYR   A CB   1 
ATOM   1585 C  CG   . TYR   A 1 68  ? 37.433 2.021   2.742   1.00 14.36 ?  68  TYR   A CG   1 
ATOM   1586 C  CD1  . TYR   A 1 68  ? 36.976 1.827   1.443   1.00 15.74 ?  68  TYR   A CD1  1 
ATOM   1587 C  CD2  . TYR   A 1 68  ? 37.967 0.935   3.410   1.00 16.22 ?  68  TYR   A CD2  1 
ATOM   1588 C  CE1  . TYR   A 1 68  ? 37.039 0.607   0.827   1.00 17.14 ?  68  TYR   A CE1  1 
ATOM   1589 C  CE2  . TYR   A 1 68  ? 38.033 -0.325  2.792   1.00 16.32 ?  68  TYR   A CE2  1 
ATOM   1590 C  CZ   . TYR   A 1 68  ? 37.572 -0.464  1.501   1.00 17.19 ?  68  TYR   A CZ   1 
ATOM   1591 O  OH   . TYR   A 1 68  ? 37.648 -1.678  0.869   1.00 18.28 ?  68  TYR   A OH   1 
ATOM   1592 H  H    . TYR   A 1 68  ? 37.797 5.786   3.868   1.00 15.49 ?  68  TYR   A H    1 
ATOM   1593 H  HA   . TYR   A 1 68  ? 39.414 3.813   3.431   1.00 15.56 ?  68  TYR   A HA   1 
ATOM   1594 H  HB2  . TYR   A 1 68  ? 37.372 3.297   4.337   1.00 16.05 ?  68  TYR   A HB2  1 
ATOM   1595 H  HB3  . TYR   A 1 68  ? 36.610 3.868   3.061   1.00 16.05 ?  68  TYR   A HB3  1 
ATOM   1596 H  HD1  . TYR   A 1 68  ? 36.626 2.558   0.977   1.00 18.87 ?  68  TYR   A HD1  1 
ATOM   1597 H  HD2  . TYR   A 1 68  ? 38.297 1.040   4.269   1.00 19.44 ?  68  TYR   A HD2  1 
ATOM   1598 H  HE1  . TYR   A 1 68  ? 36.719 0.511   -0.042  1.00 20.55 ?  68  TYR   A HE1  1 
ATOM   1599 H  HE2  . TYR   A 1 68  ? 38.394 -1.056  3.233   1.00 19.56 ?  68  TYR   A HE2  1 
ATOM   1600 H  HH   . TYR   A 1 68  ? 37.974 -2.249  1.388   1.00 21.92 ?  68  TYR   A HH   1 
ATOM   1601 N  N    . ILE   A 1 69  ? 38.122 4.944   0.716   1.00 12.28 ?  69  ILE   A N    1 
ATOM   1602 C  CA   . ILE   A 1 69  ? 38.257 4.929   -0.738  1.00 12.25 ?  69  ILE   A CA   1 
ATOM   1603 C  C    . ILE   A 1 69  ? 39.592 5.531   -1.167  1.00 12.26 ?  69  ILE   A C    1 
ATOM   1604 O  O    . ILE   A 1 69  ? 40.237 5.044   -2.103  1.00 12.80 ?  69  ILE   A O    1 
ATOM   1605 C  CB   . ILE   A 1 69  ? 37.062 5.646   -1.399  1.00 13.12 ?  69  ILE   A CB   1 
ATOM   1606 C  CG1  . ILE   A 1 69  ? 35.743 4.914   -1.128  1.00 13.40 ?  69  ILE   A CG1  1 
ATOM   1607 C  CG2  . ILE   A 1 69  ? 37.310 5.865   -2.902  1.00 14.56 ?  69  ILE   A CG2  1 
ATOM   1608 C  CD1  . ILE   A 1 69  ? 35.575 3.628   -1.913  1.00 14.08 ?  69  ILE   A CD1  1 
ATOM   1609 H  H    . ILE   A 1 69  ? 37.524 5.486   1.012   1.00 14.71 ?  69  ILE   A H    1 
ATOM   1610 H  HA   . ILE   A 1 69  ? 38.249 4.007   -1.036  1.00 14.68 ?  69  ILE   A HA   1 
ATOM   1611 H  HB   . ILE   A 1 69  ? 36.988 6.518   -0.991  1.00 15.73 ?  69  ILE   A HB   1 
ATOM   1612 H  HG12 . ILE   A 1 69  ? 35.703 4.684   -0.186  1.00 16.06 ?  69  ILE   A HG12 1 
ATOM   1613 H  HG13 . ILE   A 1 69  ? 35.008 5.496   -1.357  1.00 16.06 ?  69  ILE   A HG13 1 
ATOM   1614 H  HG21 . ILE   A 1 69  ? 36.466 6.073   -3.335  1.00 17.45 ?  69  ILE   A HG21 1 
ATOM   1615 H  HG22 . ILE   A 1 69  ? 37.923 6.615   -3.016  1.00 17.45 ?  69  ILE   A HG22 1 
ATOM   1616 H  HG23 . ILE   A 1 69  ? 37.692 5.065   -3.286  1.00 17.45 ?  69  ILE   A HG23 1 
ATOM   1617 H  HD11 . ILE   A 1 69  ? 34.769 3.183   -1.616  1.00 16.88 ?  69  ILE   A HD11 1 
ATOM   1618 H  HD12 . ILE   A 1 69  ? 35.503 3.846   -2.858  1.00 16.88 ?  69  ILE   A HD12 1 
ATOM   1619 H  HD13 . ILE   A 1 69  ? 36.345 3.060   -1.763  1.00 16.88 ?  69  ILE   A HD13 1 
ATOM   1620 N  N    . ALA   A 1 70  ? 40.009 6.619   -0.518  1.00 12.65 ?  70  ALA   A N    1 
ATOM   1621 C  CA   . ALA   A 1 70  ? 41.292 7.219   -0.868  1.00 13.73 ?  70  ALA   A CA   1 
ATOM   1622 C  C    . ALA   A 1 70  ? 42.438 6.234   -0.693  1.00 13.89 ?  70  ALA   A C    1 
ATOM   1623 O  O    . ALA   A 1 70  ? 43.403 6.266   -1.456  1.00 16.09 ?  70  ALA   A O    1 
ATOM   1624 C  CB   . ALA   A 1 70  ? 41.536 8.471   -0.026  1.00 14.73 ?  70  ALA   A CB   1 
ATOM   1625 H  H    . ALA   A 1 70  ? 39.575 7.018   0.109   1.00 15.16 ?  70  ALA   A H    1 
ATOM   1626 H  HA   . ALA   A 1 70  ? 41.263 7.495   -1.801  1.00 16.45 ?  70  ALA   A HA   1 
ATOM   1627 H  HB1  . ALA   A 1 70  ? 42.399 8.851   -0.275  1.00 17.66 ?  70  ALA   A HB1  1 
ATOM   1628 H  HB2  . ALA   A 1 70  ? 40.834 9.113   -0.191  1.00 17.66 ?  70  ALA   A HB2  1 
ATOM   1629 H  HB3  . ALA   A 1 70  ? 41.551 8.221   0.911   1.00 17.66 ?  70  ALA   A HB3  1 
ATOM   1630 N  N    . THR   A 1 71  ? 42.338 5.338   0.287   1.00 13.53 ?  71  THR   A N    1 
ATOM   1631 C  CA   . THR   A 1 71  ? 43.387 4.355   0.531   1.00 15.01 ?  71  THR   A CA   1 
ATOM   1632 C  C    . THR   A 1 71  ? 43.260 3.132   -0.370  1.00 15.25 ?  71  THR   A C    1 
ATOM   1633 O  O    . THR   A 1 71  ? 44.271 2.620   -0.873  1.00 17.26 ?  71  THR   A O    1 
ATOM   1634 C  CB   . THR   A 1 71  ? 43.321 3.904   1.986   1.00 17.33 ?  71  THR   A CB   1 
ATOM   1635 O  OG1  . THR   A 1 71  ? 43.563 5.027   2.840   1.00 18.81 ?  71  THR   A OG1  1 
ATOM   1636 C  CG2  . THR   A 1 71  ? 44.339 2.803   2.270   1.00 18.67 ?  71  THR   A CG2  1 
ATOM   1637 H  H    . THR   A 1 71  ? 41.670 5.279   0.820   1.00 16.22 ?  71  THR   A H    1 
ATOM   1638 H  HA   . THR   A 1 71  ? 44.252 4.758   0.368   1.00 17.99 ?  71  THR   A HA   1 
ATOM   1639 H  HB   . THR   A 1 71  ? 42.434 3.539   2.158   1.00 20.78 ?  71  THR   A HB   1 
ATOM   1640 H  HG1  . THR   A 1 71  ? 43.514 4.777   3.641   1.00 22.55 ?  71  THR   A HG1  1 
ATOM   1641 H  HG21 . THR   A 1 71  ? 44.472 2.718   3.227   1.00 22.39 ?  71  THR   A HG21 1 
ATOM   1642 H  HG22 . THR   A 1 71  ? 44.032 1.952   1.919   1.00 22.39 ?  71  THR   A HG22 1 
ATOM   1643 H  HG23 . THR   A 1 71  ? 45.191 3.025   1.856   1.00 22.39 ?  71  THR   A HG23 1 
ATOM   1644 N  N    . ASN   A 1 72  ? 42.037 2.625   -0.557  1.00 13.84 ?  72  ASN   A N    1 
ATOM   1645 C  CA   . ASN   A 1 72  ? 41.815 1.298   -1.118  1.00 14.63 ?  72  ASN   A CA   1 
ATOM   1646 C  C    . ASN   A 1 72  ? 41.190 1.289   -2.500  1.00 14.61 ?  72  ASN   A C    1 
ATOM   1647 O  O    . ASN   A 1 72  ? 41.195 0.235   -3.150  1.00 15.27 ?  72  ASN   A O    1 
ATOM   1648 C  CB   . ASN   A 1 72  ? 40.923 0.483   -0.174  1.00 15.26 ?  72  ASN   A CB   1 
ATOM   1649 C  CG   . ASN   A 1 72  ? 41.539 0.329   1.191   1.00 16.19 ?  72  ASN   A CG   1 
ATOM   1650 O  OD1  . ASN   A 1 72  ? 41.088 0.925   2.166   1.00 18.14 ?  72  ASN   A OD1  1 
ATOM   1651 N  ND2  . ASN   A 1 72  ? 42.595 -0.447  1.263   1.00 16.53 ?  72  ASN   A ND2  1 
ATOM   1652 H  H    . ASN   A 1 72  ? 41.308 3.042   -0.364  1.00 16.59 ?  72  ASN   A H    1 
ATOM   1653 H  HA   . ASN   A 1 72  ? 42.668 0.844   -1.182  1.00 17.53 ?  72  ASN   A HA   1 
ATOM   1654 H  HB2  . ASN   A 1 72  ? 40.070 0.932   -0.075  1.00 18.29 ?  72  ASN   A HB2  1 
ATOM   1655 H  HB3  . ASN   A 1 72  ? 40.794 -0.404  -0.546  1.00 18.29 ?  72  ASN   A HB3  1 
ATOM   1656 H  HD21 . ASN   A 1 72  ? 42.994 -0.560  2.019   1.00 19.81 ?  72  ASN   A HD21 1 
ATOM   1657 H  HD22 . ASN   A 1 72  ? 42.895 -0.837  0.558   1.00 19.81 ?  72  ASN   A HD22 1 
ATOM   1658 N  N    . GLY   A 1 73  ? 40.647 2.406   -2.964  1.00 14.42 ?  73  GLY   A N    1 
ATOM   1659 C  CA   . GLY   A 1 73  ? 39.914 2.416   -4.203  1.00 14.07 ?  73  GLY   A CA   1 
ATOM   1660 C  C    . GLY   A 1 73  ? 38.522 1.835   -4.033  1.00 13.26 ?  73  GLY   A C    1 
ATOM   1661 O  O    . GLY   A 1 73  ? 38.133 1.376   -2.952  1.00 13.69 ?  73  GLY   A O    1 
ATOM   1662 H  H    . GLY   A 1 73  ? 40.698 3.179   -2.579  1.00 17.28 ?  73  GLY   A H    1 
ATOM   1663 H  HA2  . GLY   A 1 73  ? 39.838 3.331   -4.526  1.00 16.86 ?  73  GLY   A HA2  1 
ATOM   1664 H  HA3  . GLY   A 1 73  ? 40.393 1.896   -4.871  1.00 16.86 ?  73  GLY   A HA3  1 
ATOM   1665 N  N    . PRO   A 1 74  ? 37.746 1.855   -5.115  1.00 13.56 ?  74  PRO   A N    1 
ATOM   1666 C  CA   . PRO   A 1 74  ? 36.344 1.431   -5.039  1.00 13.79 ?  74  PRO   A CA   1 
ATOM   1667 C  C    . PRO   A 1 74  ? 36.186 -0.050  -4.719  1.00 12.78 ?  74  PRO   A C    1 
ATOM   1668 O  O    . PRO   A 1 74  ? 37.058 -0.879  -4.999  1.00 13.91 ?  74  PRO   A O    1 
ATOM   1669 C  CB   . PRO   A 1 74  ? 35.806 1.737   -6.443  1.00 15.30 ?  74  PRO   A CB   1 
ATOM   1670 C  CG   . PRO   A 1 74  ? 36.773 2.696   -7.050  1.00 18.14 ?  74  PRO   A CG   1 
ATOM   1671 C  CD   . PRO   A 1 74  ? 38.101 2.375   -6.445  1.00 15.51 ?  74  PRO   A CD   1 
ATOM   1672 H  HA   . PRO   A 1 74  ? 35.864 1.963   -4.384  1.00 16.53 ?  74  PRO   A HA   1 
ATOM   1673 H  HB2  . PRO   A 1 74  ? 35.766 0.915   -6.957  1.00 18.34 ?  74  PRO   A HB2  1 
ATOM   1674 H  HB3  . PRO   A 1 74  ? 34.925 2.138   -6.371  1.00 18.34 ?  74  PRO   A HB3  1 
ATOM   1675 H  HG2  . PRO   A 1 74  ? 36.801 2.568   -8.011  1.00 21.74 ?  74  PRO   A HG2  1 
ATOM   1676 H  HG3  . PRO   A 1 74  ? 36.515 3.604   -6.833  1.00 21.74 ?  74  PRO   A HG3  1 
ATOM   1677 H  HD2  . PRO   A 1 74  ? 38.562 1.695   -6.965  1.00 18.59 ?  74  PRO   A HD2  1 
ATOM   1678 H  HD3  . PRO   A 1 74  ? 38.640 3.184   -6.375  1.00 18.59 ?  74  PRO   A HD3  1 
ATOM   1679 N  N    . LEU   A 1 75  ? 35.039 -0.366  -4.126  1.00 12.09 ?  75  LEU   A N    1 
ATOM   1680 C  CA   . LEU   A 1 75  ? 34.638 -1.755  -3.977  1.00 12.11 ?  75  LEU   A CA   1 
ATOM   1681 C  C    . LEU   A 1 75  ? 34.257 -2.336  -5.337  1.00 12.62 ?  75  LEU   A C    1 
ATOM   1682 O  O    . LEU   A 1 75  ? 34.131 -1.622  -6.336  1.00 14.08 ?  75  LEU   A O    1 
ATOM   1683 C  CB   . LEU   A 1 75  ? 33.446 -1.871  -3.028  1.00 12.04 ?  75  LEU   A CB   1 
ATOM   1684 C  CG   . LEU   A 1 75  ? 33.651 -1.458  -1.573  1.00 13.68 ?  75  LEU   A CG   1 
ATOM   1685 C  CD1  . LEU   A 1 75  ? 32.361 -1.640  -0.774  1.00 15.41 ?  75  LEU   A CD1  1 
ATOM   1686 C  CD2  . LEU   A 1 75  ? 34.790 -2.183  -0.912  1.00 17.43 ?  75  LEU   A CD2  1 
ATOM   1687 H  H    . LEU   A 1 75  ? 34.482 0.207   -3.810  1.00 14.49 ?  75  LEU   A H    1 
ATOM   1688 H  HA   . LEU   A 1 75  ? 35.375 -2.267  -3.623  1.00 14.51 ?  75  LEU   A HA   1 
ATOM   1689 H  HB2  . LEU   A 1 75  ? 32.725 -1.332  -3.377  1.00 14.43 ?  75  LEU   A HB2  1 
ATOM   1690 H  HB3  . LEU   A 1 75  ? 33.169 -2.804  -3.017  1.00 14.43 ?  75  LEU   A HB3  1 
ATOM   1691 H  HG   . LEU   A 1 75  ? 33.871 -0.512  -1.557  1.00 16.39 ?  75  LEU   A HG   1 
ATOM   1692 H  HD11 . LEU   A 1 75  ? 32.519 -1.362  0.144   1.00 18.47 ?  75  LEU   A HD11 1 
ATOM   1693 H  HD12 . LEU   A 1 75  ? 31.669 -1.085  -1.169  1.00 18.47 ?  75  LEU   A HD12 1 
ATOM   1694 H  HD13 . LEU   A 1 75  ? 32.102 -2.569  -0.801  1.00 18.47 ?  75  LEU   A HD13 1 
ATOM   1695 H  HD21 . LEU   A 1 75  ? 34.836 -1.923  0.021   1.00 20.90 ?  75  LEU   A HD21 1 
ATOM   1696 H  HD22 . LEU   A 1 75  ? 34.644 -3.138  -0.983  1.00 20.90 ?  75  LEU   A HD22 1 
ATOM   1697 H  HD23 . LEU   A 1 75  ? 35.622 -1.944  -1.359  1.00 20.90 ?  75  LEU   A HD23 1 
ATOM   1698 N  N    . LYS   A 1 76  ? 34.056 -3.653  -5.355  1.00 12.67 ?  76  LYS   A N    1 
ATOM   1699 C  CA   . LYS   A 1 76  ? 33.461 -4.364  -6.481  1.00 13.57 ?  76  LYS   A CA   1 
ATOM   1700 C  C    . LYS   A 1 76  ? 31.949 -4.449  -6.288  1.00 12.23 ?  76  LYS   A C    1 
ATOM   1701 O  O    . LYS   A 1 76  ? 31.469 -4.573  -5.165  1.00 12.11 ?  76  LYS   A O    1 
ATOM   1702 C  CB   . LYS   A 1 76  ? 34.006 -5.802  -6.542  1.00 15.17 ?  76  LYS   A CB   1 
ATOM   1703 C  CG   . LYS   A 1 76  ? 35.519 -5.912  -6.711  1.00 16.71 ?  76  LYS   A CG   1 
ATOM   1704 C  CD   . LYS   A 1 76  ? 36.026 -7.325  -6.514  1.00 18.22 ?  76  LYS   A CD   1 
ATOM   1705 C  CE   . LYS   A 1 76  ? 37.522 -7.395  -6.729  1.00 21.01 ?  76  LYS   A CE   1 
ATOM   1706 N  NZ   . LYS   A 1 76  ? 38.048 -8.755  -6.498  1.00 22.05 ?  76  LYS   A NZ   1 
ATOM   1707 H  H    . LYS   A 1 76  ? 34.266 -4.174  -4.699  1.00 15.18 ?  76  LYS   A H    1 
ATOM   1708 H  HA   . LYS   A 1 76  ? 33.661 -3.905  -7.314  1.00 16.26 ?  76  LYS   A HA   1 
ATOM   1709 H  HB2  . LYS   A 1 76  ? 33.771 -6.254  -5.718  1.00 18.18 ?  76  LYS   A HB2  1 
ATOM   1710 H  HB3  . LYS   A 1 76  ? 33.595 -6.254  -7.293  1.00 18.18 ?  76  LYS   A HB3  1 
ATOM   1711 H  HG2  . LYS   A 1 76  ? 35.759 -5.627  -7.607  1.00 20.04 ?  76  LYS   A HG2  1 
ATOM   1712 H  HG3  . LYS   A 1 76  ? 35.954 -5.343  -6.055  1.00 20.04 ?  76  LYS   A HG3  1 
ATOM   1713 H  HD2  . LYS   A 1 76  ? 35.829 -7.618  -5.609  1.00 21.85 ?  76  LYS   A HD2  1 
ATOM   1714 H  HD3  . LYS   A 1 76  ? 35.595 -7.916  -7.156  1.00 21.85 ?  76  LYS   A HD3  1 
ATOM   1715 H  HE2  . LYS   A 1 76  ? 37.722 -7.141  -7.642  1.00 25.19 ?  76  LYS   A HE2  1 
ATOM   1716 H  HE3  . LYS   A 1 76  ? 37.957 -6.792  -6.107  1.00 25.19 ?  76  LYS   A HE3  1 
ATOM   1717 H  HZ1  . LYS   A 1 76  ? 38.926 -8.771  -6.631  1.00 26.44 ?  76  LYS   A HZ1  1 
ATOM   1718 H  HZ2  . LYS   A 1 76  ? 37.875 -9.015  -5.664  1.00 26.44 ?  76  LYS   A HZ2  1 
ATOM   1719 H  HZ3  . LYS   A 1 76  ? 37.661 -9.332  -7.061  1.00 26.44 ?  76  LYS   A HZ3  1 
ATOM   1720 N  N    . VAL   A 1 77  ? 31.198 -4.425  -7.394  1.00 12.57 ?  77  VAL   A N    1 
ATOM   1721 C  CA   . VAL   A 1 77  ? 29.791 -4.809  -7.309  1.00 12.40 ?  77  VAL   A CA   1 
ATOM   1722 C  C    . VAL   A 1 77  ? 29.723 -6.261  -6.859  1.00 12.28 ?  77  VAL   A C    1 
ATOM   1723 O  O    . VAL   A 1 77  ? 30.377 -7.137  -7.437  1.00 12.53 ?  77  VAL   A O    1 
ATOM   1724 C  CB   . VAL   A 1 77  ? 29.069 -4.597  -8.648  1.00 13.68 ?  77  VAL   A CB   1 
ATOM   1725 C  CG1  . VAL   A 1 77  ? 27.608 -5.016  -8.528  1.00 14.61 ?  77  VAL   A CG1  1 
ATOM   1726 C  CG2  . VAL   A 1 77  ? 29.172 -3.145  -9.088  1.00 15.46 ?  77  VAL   A CG2  1 
ATOM   1727 H  H    . VAL   A 1 77  ? 31.475 -4.195  -8.177  1.00 15.06 ?  77  VAL   A H    1 
ATOM   1728 H  HA   . VAL   A 1 77  ? 29.356 -4.258  -6.639  1.00 14.86 ?  77  VAL   A HA   1 
ATOM   1729 H  HB   . VAL   A 1 77  ? 29.491 -5.148  -9.326  1.00 16.39 ?  77  VAL   A HB   1 
ATOM   1730 H  HG11 . VAL   A 1 77  ? 27.138 -4.728  -9.322  1.00 17.51 ?  77  VAL   A HG11 1 
ATOM   1731 H  HG12 . VAL   A 1 77  ? 27.564 -5.981  -8.445  1.00 17.51 ?  77  VAL   A HG12 1 
ATOM   1732 H  HG13 . VAL   A 1 77  ? 27.228 -4.596  -7.742  1.00 17.51 ?  77  VAL   A HG13 1 
ATOM   1733 H  HG21 . VAL   A 1 77  ? 28.657 -3.028  -9.900  1.00 18.53 ?  77  VAL   A HG21 1 
ATOM   1734 H  HG22 . VAL   A 1 77  ? 28.817 -2.579  -8.385  1.00 18.53 ?  77  VAL   A HG22 1 
ATOM   1735 H  HG23 . VAL   A 1 77  ? 30.103 -2.929  -9.250  1.00 18.53 ?  77  VAL   A HG23 1 
ATOM   1736 N  N    . GLY   A 1 78  ? 28.942 -6.520  -5.812  1.00 11.56 ?  78  GLY   A N    1 
ATOM   1737 C  CA   . GLY   A 1 78  ? 28.916 -7.808  -5.159  1.00 12.03 ?  78  GLY   A CA   1 
ATOM   1738 C  C    . GLY   A 1 78  ? 29.831 -7.901  -3.959  1.00 11.62 ?  78  GLY   A C    1 
ATOM   1739 O  O    . GLY   A 1 78  ? 29.773 -8.907  -3.231  1.00 12.37 ?  78  GLY   A O    1 
ATOM   1740 H  H    . GLY   A 1 78  ? 28.399 -5.941  -5.465  1.00 13.85 ?  78  GLY   A H    1 
ATOM   1741 H  HA2  . GLY   A 1 78  ? 28.010 -7.993  -4.867  1.00 14.41 ?  78  GLY   A HA2  1 
ATOM   1742 H  HA3  . GLY   A 1 78  ? 29.175 -8.488  -5.798  1.00 14.41 ?  78  GLY   A HA3  1 
ATOM   1743 N  N    . GLY   A 1 79  ? 30.688 -6.898  -3.739  1.00 11.57 ?  79  GLY   A N    1 
ATOM   1744 C  CA   . GLY   A 1 79  ? 31.653 -6.917  -2.663  1.00 12.11 ?  79  GLY   A CA   1 
ATOM   1745 C  C    . GLY   A 1 79  ? 31.213 -6.124  -1.447  1.00 11.04 ?  79  GLY   A C    1 
ATOM   1746 O  O    . GLY   A 1 79  ? 30.093 -5.615  -1.366  1.00 11.72 ?  79  GLY   A O    1 
ATOM   1747 H  H    . GLY   A 1 79  ? 30.723 -6.180  -4.218  1.00 13.87 ?  79  GLY   A H    1 
ATOM   1748 H  HA2  . GLY   A 1 79  ? 31.807 -7.843  -2.396  1.00 14.51 ?  79  GLY   A HA2  1 
ATOM   1749 H  HA3  . GLY   A 1 79  ? 32.494 -6.557  -2.984  1.00 14.51 ?  79  GLY   A HA3  1 
ATOM   1750 N  N    . SER   A 1 80  ? 32.120 -6.031  -0.478  1.00 11.85 ?  80  SER   A N    1 
ATOM   1751 C  CA   . SER   A 1 80  ? 31.801 -5.401  0.792   1.00 11.60 ?  80  SER   A CA   1 
ATOM   1752 C  C    . SER   A 1 80  ? 33.072 -4.950  1.497   1.00 11.53 ?  80  SER   A C    1 
ATOM   1753 O  O    . SER   A 1 80  ? 34.188 -5.385  1.177   1.00 12.98 ?  80  SER   A O    1 
ATOM   1754 C  CB   . SER   A 1 80  ? 31.039 -6.368  1.708   1.00 12.78 ?  80  SER   A CB   1 
ATOM   1755 O  OG   . SER   A 1 80  ? 31.873 -7.414  2.179   1.00 14.41 ?  80  SER   A OG   1 
ATOM   1756 H  H    . SER   A 1 80  ? 32.929 -6.323  -0.538  1.00 14.20 ?  80  SER   A H    1 
ATOM   1757 H  HA   . SER   A 1 80  ? 31.245 -4.623  0.615   1.00 13.90 ?  80  SER   A HA   1 
ATOM   1758 H  HB2  . SER   A 1 80  ? 30.698 -5.871  2.468   1.00 15.32 ?  80  SER   A HB2  1 
ATOM   1759 H  HB3  . SER   A 1 80  ? 30.300 -6.752  1.209   1.00 15.32 ?  80  SER   A HB3  1 
ATOM   1760 H  HG   . SER   A 1 80  ? 32.172 -7.851  1.524   1.00 17.27 ?  80  SER   A HG   1 
ATOM   1761 N  N    . CYS   A 1 81  ? 32.876 -4.097  2.501   1.00 11.13 ?  81  CYS   A N    1 
ATOM   1762 C  CA   . CYS   A 1 81  ? 33.927 -3.817  3.465   1.00 11.34 ?  81  CYS   A CA   1 
ATOM   1763 C  C    . CYS   A 1 81  ? 33.290 -3.581  4.825   1.00 11.37 ?  81  CYS   A C    1 
ATOM   1764 O  O    . CYS   A 1 81  ? 32.126 -3.178  4.915   1.00 12.18 ?  81  CYS   A O    1 
ATOM   1765 C  CB   . CYS   A 1 81  ? 34.808 -2.627  3.052   1.00 12.20 ?  81  CYS   A CB   1 
ATOM   1766 S  SG   . CYS   A 1 81  ? 33.919 -1.043  3.060   1.00 12.08 ?  81  CYS   A SG   1 
ATOM   1767 H  H    . CYS   A 1 81  ? 32.138 -3.669  2.648   1.00 13.34 ?  81  CYS   A H    1 
ATOM   1768 H  HA   . CYS   A 1 81  ? 34.499 -4.594  3.535   1.00 13.58 ?  81  CYS   A HA   1 
ATOM   1769 H  HB2  . CYS   A 1 81  ? 35.556 -2.557  3.672   1.00 14.62 ?  81  CYS   A HB2  1 
ATOM   1770 H  HB3  . CYS   A 1 81  ? 35.146 -2.779  2.152   1.00 14.62 ?  81  CYS   A HB3  1 
ATOM   1771 H  HG   . CYS   A 1 81  ? 34.669 -0.168  2.731   1.00 14.47 ?  81  CYS   A HG   1 
ATOM   1772 N  N    . VAL   A 1 82  ? 34.056 -3.840  5.880   1.00 11.75 ?  82  VAL   A N    1 
ATOM   1773 C  CA   . VAL   A 1 82  ? 33.633 -3.589  7.252   1.00 12.49 ?  82  VAL   A CA   1 
ATOM   1774 C  C    . VAL   A 1 82  ? 34.231 -2.273  7.723   1.00 12.44 ?  82  VAL   A C    1 
ATOM   1775 O  O    . VAL   A 1 82  ? 35.458 -2.106  7.718   1.00 12.99 ?  82  VAL   A O    1 
ATOM   1776 C  CB   . VAL   A 1 82  ? 34.051 -4.731  8.191   1.00 13.82 ?  82  VAL   A CB   1 
ATOM   1777 C  CG1  . VAL   A 1 82  ? 33.612 -4.427  9.619   1.00 15.29 ?  82  VAL   A CG1  1 
ATOM   1778 C  CG2  . VAL   A 1 82  ? 33.482 -6.062  7.720   1.00 14.65 ?  82  VAL   A CG2  1 
ATOM   1779 H  H    . VAL   A 1 82  ? 34.849 -4.180  5.825   1.00 14.08 ?  82  VAL   A H    1 
ATOM   1780 H  HA   . VAL   A 1 82  ? 32.664 -3.510  7.275   1.00 14.96 ?  82  VAL   A HA   1 
ATOM   1781 H  HB   . VAL   A 1 82  ? 35.013 -4.798  8.187   1.00 16.56 ?  82  VAL   A HB   1 
ATOM   1782 H  HG11 . VAL   A 1 82  ? 33.690 -5.233  10.149  1.00 18.32 ?  82  VAL   A HG11 1 
ATOM   1783 H  HG12 . VAL   A 1 82  ? 34.180 -3.732  9.987   1.00 18.32 ?  82  VAL   A HG12 1 
ATOM   1784 H  HG13 . VAL   A 1 82  ? 32.687 -4.127  9.610   1.00 18.32 ?  82  VAL   A HG13 1 
ATOM   1785 H  HG21 . VAL   A 1 82  ? 33.726 -6.752  8.356   1.00 17.56 ?  82  VAL   A HG21 1 
ATOM   1786 H  HG22 . VAL   A 1 82  ? 32.513 -5.992  7.666   1.00 17.56 ?  82  VAL   A HG22 1 
ATOM   1787 H  HG23 . VAL   A 1 82  ? 33.846 -6.270  6.847   1.00 17.56 ?  82  VAL   A HG23 1 
ATOM   1788 N  N    . LEU   A 1 83  ? 33.373 -1.348  8.143   1.00 11.75 ?  83  LEU   A N    1 
ATOM   1789 C  CA   . LEU   A 1 83  ? 33.800 -0.086  8.726   1.00 11.51 ?  83  LEU   A CA   1 
ATOM   1790 C  C    . LEU   A 1 83  ? 33.081 0.099   10.057  1.00 11.94 ?  83  LEU   A C    1 
ATOM   1791 O  O    . LEU   A 1 83  ? 32.361 -0.790  10.523  1.00 12.47 ?  83  LEU   A O    1 
ATOM   1792 C  CB   . LEU   A 1 83  ? 33.561 1.077   7.753   1.00 12.15 ?  83  LEU   A CB   1 
ATOM   1793 C  CG   . LEU   A 1 83  ? 34.451 1.081   6.509   1.00 12.75 ?  83  LEU   A CG   1 
ATOM   1794 C  CD1  . LEU   A 1 83  ? 34.020 2.129   5.505   1.00 13.62 ?  83  LEU   A CD1  1 
ATOM   1795 C  CD2  . LEU   A 1 83  ? 35.917 1.285   6.891   1.00 13.46 ?  83  LEU   A CD2  1 
ATOM   1796 H  H    . LEU   A 1 83  ? 32.514 -1.429  8.091   1.00 14.08 ?  83  LEU   A H    1 
ATOM   1797 H  HA   . LEU   A 1 83  ? 34.749 -0.124  8.909   1.00 13.79 ?  83  LEU   A HA   1 
ATOM   1798 H  HB2  . LEU   A 1 83  ? 32.641 1.041   7.445   1.00 14.55 ?  83  LEU   A HB2  1 
ATOM   1799 H  HB3  . LEU   A 1 83  ? 33.711 1.913   8.220   1.00 14.55 ?  83  LEU   A HB3  1 
ATOM   1800 H  HG   . LEU   A 1 83  ? 34.385 0.218   6.078   1.00 15.28 ?  83  LEU   A HG   1 
ATOM   1801 H  HD11 . LEU   A 1 83  ? 34.612 2.088   4.734   1.00 16.32 ?  83  LEU   A HD11 1 
ATOM   1802 H  HD12 . LEU   A 1 83  ? 33.110 1.942   5.231   1.00 16.32 ?  83  LEU   A HD12 1 
ATOM   1803 H  HD13 . LEU   A 1 83  ? 34.073 3.003   5.916   1.00 16.32 ?  83  LEU   A HD13 1 
ATOM   1804 H  HD21 . LEU   A 1 83  ? 36.441 1.437   6.085   1.00 16.13 ?  83  LEU   A HD21 1 
ATOM   1805 H  HD22 . LEU   A 1 83  ? 35.994 2.053   7.479   1.00 16.13 ?  83  LEU   A HD22 1 
ATOM   1806 H  HD23 . LEU   A 1 83  ? 36.245 0.491   7.345   1.00 16.13 ?  83  LEU   A HD23 1 
ATOM   1807 N  N    . SER   A 1 84  ? 33.299 1.250   10.689  1.00 12.50 ?  84  SER   A N    1 
ATOM   1808 C  CA   . SER   A 1 84  ? 32.659 1.509   11.967  1.00 12.64 ?  84  SER   A CA   1 
ATOM   1809 C  C    . SER   A 1 84  ? 31.140 1.596   11.822  1.00 12.69 ?  84  SER   A C    1 
ATOM   1810 O  O    . SER   A 1 84  ? 30.613 2.062   10.813  1.00 12.68 ?  84  SER   A O    1 
ATOM   1811 C  CB   . SER   A 1 84  ? 33.160 2.831   12.540  1.00 13.50 ?  84  SER   A CB   1 
ATOM   1812 O  OG   . SER   A 1 84  ? 32.528 3.101   13.775  1.00 14.39 ?  84  SER   A OG   1 
ATOM   1813 H  H    . SER   A 1 84  ? 33.807 1.888   10.400  1.00 14.98 ?  84  SER   A H    1 
ATOM   1814 H  HA   . SER   A 1 84  ? 32.880 0.798   12.588  1.00 15.15 ?  84  SER   A HA   1 
ATOM   1815 H  HB2  . SER   A 1 84  ? 34.120 2.778   12.674  1.00 16.18 ?  84  SER   A HB2  1 
ATOM   1816 H  HB3  . SER   A 1 84  ? 32.954 3.545   11.913  1.00 16.18 ?  84  SER   A HB3  1 
ATOM   1817 H  HG   . SER   A 1 84  ? 32.809 3.834   14.085  1.00 17.25 ?  84  SER   A HG   1 
ATOM   1818 N  N    . GLY   A 1 85  ? 30.436 1.184   12.874  1.00 13.31 ?  85  GLY   A N    1 
ATOM   1819 C  CA   . GLY   A 1 85  ? 29.012 1.415   12.968  1.00 14.05 ?  85  GLY   A CA   1 
ATOM   1820 C  C    . GLY   A 1 85  ? 28.646 2.735   13.612  1.00 13.31 ?  85  GLY   A C    1 
ATOM   1821 O  O    . GLY   A 1 85  ? 27.456 3.057   13.727  1.00 14.09 ?  85  GLY   A O    1 
ATOM   1822 H  H    . GLY   A 1 85  ? 30.773 0.763   13.549  1.00 15.96 ?  85  GLY   A H    1 
ATOM   1823 H  HA2  . GLY   A 1 85  ? 28.630 1.394   12.079  1.00 16.83 ?  85  GLY   A HA2  1 
ATOM   1824 H  HA3  . GLY   A 1 85  ? 28.610 0.706   13.489  1.00 16.83 ?  85  GLY   A HA3  1 
ATOM   1825 N  N    . HIS   A 1 86  ? 29.638 3.504   14.050  1.00 13.05 ?  86  HIS   A N    1 
ATOM   1826 C  CA   . HIS   A 1 86  ? 29.416 4.844   14.613  1.00 13.55 ?  86  HIS   A CA   1 
ATOM   1827 C  C    . HIS   A 1 86  ? 28.433 4.725   15.771  1.00 14.37 ?  86  HIS   A C    1 
ATOM   1828 O  O    . HIS   A 1 86  ? 28.618 3.851   16.633  1.00 15.75 ?  86  HIS   A O    1 
ATOM   1829 C  CB   . HIS   A 1 86  ? 29.040 5.823   13.507  1.00 13.81 ?  86  HIS   A CB   1 
ATOM   1830 C  CG   . HIS   A 1 86  ? 30.097 5.926   12.469  1.00 13.37 ?  86  HIS   A CG   1 
ATOM   1831 N  ND1  . HIS   A 1 86  ? 31.192 6.754   12.603  1.00 15.02 ?  86  HIS   A ND1  1 
ATOM   1832 C  CD2  . HIS   A 1 86  ? 30.275 5.238   11.320  1.00 13.15 ?  86  HIS   A CD2  1 
ATOM   1833 C  CE1  . HIS   A 1 86  ? 31.982 6.590   11.557  1.00 14.54 ?  86  HIS   A CE1  1 
ATOM   1834 N  NE2  . HIS   A 1 86  ? 31.458 5.665   10.775  1.00 13.96 ?  86  HIS   A NE2  1 
ATOM   1835 H  H    . HIS   A 1 86  ? 30.461 3.271   14.048  1.00 15.64 ?  86  HIS   A H    1 
ATOM   1836 H  HA   . HIS   A 1 86  ? 30.255 5.155   14.984  1.00 16.23 ?  86  HIS   A HA   1 
ATOM   1837 H  HB2  . HIS   A 1 86  ? 28.222 5.529   13.078  1.00 16.55 ?  86  HIS   A HB2  1 
ATOM   1838 H  HB3  . HIS   A 1 86  ? 28.912 6.709   13.888  1.00 16.55 ?  86  HIS   A HB3  1 
ATOM   1839 H  HD2  . HIS   A 1 86  ? 29.708 4.582   10.969  1.00 15.76 ?  86  HIS   A HD2  1 
ATOM   1840 H  HE1  . HIS   A 1 86  ? 32.776 7.044   11.389  1.00 17.43 ?  86  HIS   A HE1  1 
ATOM   1841 H  HE2  . HIS   A 1 86  ? 31.788 5.393   10.020  1.00 16.73 ?  86  HIS   A HE2  1 
ATOM   1842 N  N    . ASN   A 1 87  ? 27.420 5.576   15.842  1.00 15.71 ?  87  ASN   A N    1 
ATOM   1843 C  CA   . ASN   A 1 87  ? 26.443 5.568   16.913  1.00 16.73 ?  87  ASN   A CA   1 
ATOM   1844 C  C    . ASN   A 1 87  ? 25.310 4.581   16.679  1.00 17.90 ?  87  ASN   A C    1 
ATOM   1845 O  O    . ASN   A 1 87  ? 24.391 4.524   17.499  1.00 20.02 ?  87  ASN   A O    1 
ATOM   1846 C  CB   . ASN   A 1 87  ? 25.851 6.975   17.071  1.00 17.41 ?  87  ASN   A CB   1 
ATOM   1847 C  CG   . ASN   A 1 87  ? 25.338 7.553   15.752  1.00 17.96 ?  87  ASN   A CG   1 
ATOM   1848 O  OD1  . ASN   A 1 87  ? 25.984 7.443   14.712  1.00 18.74 ?  87  ASN   A OD1  1 
ATOM   1849 N  ND2  . ASN   A 1 87  ? 24.172 8.172   15.798  1.00 19.38 ?  87  ASN   A ND2  1 
ATOM   1850 H  H    . ASN   A 1 87  ? 27.272 6.184   15.260  1.00 18.84 ?  87  ASN   A H    1 
ATOM   1851 H  HA   . ASN   A 1 87  ? 26.872 5.323   17.750  1.00 20.06 ?  87  ASN   A HA   1 
ATOM   1852 H  HB2  . ASN   A 1 87  ? 25.105 6.937   17.699  1.00 20.87 ?  87  ASN   A HB2  1 
ATOM   1853 H  HB3  . ASN   A 1 87  ? 26.536 7.567   17.412  1.00 20.87 ?  87  ASN   A HB3  1 
ATOM   1854 H  HD21 . ASN   A 1 87  ? 23.840 8.509   15.083  1.00 23.23 ?  87  ASN   A HD21 1 
ATOM   1855 H  HD22 . ASN   A 1 87  ? 23.749 8.243   16.546  1.00 23.23 ?  87  ASN   A HD22 1 
ATOM   1856 N  N    A LEU   A 1 88  ? 25.359 3.800   15.602  0.70 16.53 ?  88  LEU   A N    1 
ATOM   1857 N  N    B LEU   A 1 88  ? 25.357 3.793   15.605  0.30 17.27 ?  88  LEU   A N    1 
ATOM   1858 C  CA   A LEU   A 1 88  ? 24.249 2.939   15.209  0.70 16.27 ?  88  LEU   A CA   1 
ATOM   1859 C  CA   B LEU   A 1 88  ? 24.240 2.941   15.219  0.30 17.13 ?  88  LEU   A CA   1 
ATOM   1860 C  C    A LEU   A 1 88  ? 24.468 1.465   15.519  0.70 16.02 ?  88  LEU   A C    1 
ATOM   1861 C  C    B LEU   A 1 88  ? 24.467 1.458   15.477  0.30 16.38 ?  88  LEU   A C    1 
ATOM   1862 O  O    A LEU   A 1 88  ? 23.490 0.738   15.736  0.70 17.25 ?  88  LEU   A O    1 
ATOM   1863 O  O    B LEU   A 1 88  ? 23.488 0.719   15.620  0.30 17.00 ?  88  LEU   A O    1 
ATOM   1864 C  CB   A LEU   A 1 88  ? 24.000 3.079   13.705  0.70 16.87 ?  88  LEU   A CB   1 
ATOM   1865 C  CB   B LEU   A 1 88  ? 23.935 3.127   13.727  0.30 17.82 ?  88  LEU   A CB   1 
ATOM   1866 C  CG   A LEU   A 1 88  ? 23.708 4.487   13.188  0.70 18.73 ?  88  LEU   A CG   1 
ATOM   1867 C  CG   B LEU   A 1 88  ? 23.661 4.564   13.279  0.30 18.59 ?  88  LEU   A CG   1 
ATOM   1868 C  CD1  A LEU   A 1 88  ? 23.571 4.454   11.677  0.70 19.09 ?  88  LEU   A CD1  1 
ATOM   1869 C  CD1  B LEU   A 1 88  ? 23.506 4.634   11.767  0.30 18.69 ?  88  LEU   A CD1  1 
ATOM   1870 C  CD2  A LEU   A 1 88  ? 22.454 5.061   13.833  0.70 20.42 ?  88  LEU   A CD2  1 
ATOM   1871 C  CD2  B LEU   A 1 88  ? 22.427 5.120   13.972  0.30 19.21 ?  88  LEU   A CD2  1 
ATOM   1872 H  H    A LEU   A 1 88  ? 26.039 3.753   15.078  0.70 19.81 ?  88  LEU   A H    1 
ATOM   1873 H  H    B LEU   A 1 88  ? 26.038 3.735   15.085  0.30 20.70 ?  88  LEU   A H    1 
ATOM   1874 H  HA   A LEU   A 1 88  ? 23.448 3.227   15.671  0.70 19.50 ?  88  LEU   A HA   1 
ATOM   1875 H  HA   B LEU   A 1 88  ? 23.453 3.212   15.716  0.30 20.54 ?  88  LEU   A HA   1 
ATOM   1876 H  HB2  A LEU   A 1 88  ? 24.782 2.760   13.233  0.70 20.23 ?  88  LEU   A HB2  1 
ATOM   1877 H  HB2  B LEU   A 1 88  ? 24.692 2.802   13.218  0.30 21.36 ?  88  LEU   A HB2  1 
ATOM   1878 H  HB3  A LEU   A 1 88  ? 23.235 2.529   13.472  0.70 20.23 ?  88  LEU   A HB3  1 
ATOM   1879 H  HB3  B LEU   A 1 88  ? 23.149 2.601   13.511  0.30 21.36 ?  88  LEU   A HB3  1 
ATOM   1880 H  HG   A LEU   A 1 88  ? 24.452 5.069   13.407  0.70 22.46 ?  88  LEU   A HG   1 
ATOM   1881 H  HG   B LEU   A 1 88  ? 24.417 5.119   13.524  0.30 22.29 ?  88  LEU   A HG   1 
ATOM   1882 H  HD11 A LEU   A 1 88  ? 23.407 5.355   11.353  0.70 22.88 ?  88  LEU   A HD11 1 
ATOM   1883 H  HD11 B LEU   A 1 88  ? 23.335 5.554   11.509  0.30 22.41 ?  88  LEU   A HD11 1 
ATOM   1884 H  HD12 A LEU   A 1 88  ? 24.393 4.110   11.292  0.70 22.88 ?  88  LEU   A HD12 1 
ATOM   1885 H  HD12 B LEU   A 1 88  ? 24.324 4.321   11.350  0.30 22.41 ?  88  LEU   A HD12 1 
ATOM   1886 H  HD13 A LEU   A 1 88  ? 22.828 3.878   11.439  0.70 22.88 ?  88  LEU   A HD13 1 
ATOM   1887 H  HD13 B LEU   A 1 88  ? 22.762 4.072   11.499  0.30 22.41 ?  88  LEU   A HD13 1 
ATOM   1888 H  HD21 A LEU   A 1 88  ? 22.249 5.915   13.420  0.70 24.49 ?  88  LEU   A HD21 1 
ATOM   1889 H  HD21 B LEU   A 1 88  ? 22.224 5.991   13.599  0.30 23.03 ?  88  LEU   A HD21 1 
ATOM   1890 H  HD22 A LEU   A 1 88  ? 21.720 4.442   13.697  0.70 24.49 ?  88  LEU   A HD22 1 
ATOM   1891 H  HD22 B LEU   A 1 88  ? 21.685 4.514   13.825  0.30 23.03 ?  88  LEU   A HD22 1 
ATOM   1892 H  HD23 A LEU   A 1 88  ? 22.616 5.182   14.781  0.70 24.49 ?  88  LEU   A HD23 1 
ATOM   1893 H  HD23 B LEU   A 1 88  ? 22.609 5.198   14.921  0.30 23.03 ?  88  LEU   A HD23 1 
ATOM   1894 N  N    . ALA   A 1 89  ? 25.717 1.011   15.529  1.00 15.24 ?  89  ALA   A N    1 
ATOM   1895 C  CA   . ALA   A 1 89  ? 26.048 -0.401  15.650  1.00 14.72 ?  89  ALA   A CA   1 
ATOM   1896 C  C    . ALA   A 1 89  ? 27.533 -0.470  15.964  1.00 15.27 ?  89  ALA   A C    1 
ATOM   1897 O  O    . ALA   A 1 89  ? 28.249 0.527   15.851  1.00 16.25 ?  89  ALA   A O    1 
ATOM   1898 C  CB   . ALA   A 1 89  ? 25.769 -1.124  14.333  1.00 14.46 ?  89  ALA   A CB   1 
ATOM   1899 H  H    A ALA   A 1 89  ? 26.407 1.520   15.460  0.70 18.26 ?  89  ALA   A H    1 
ATOM   1900 H  H    B ALA   A 1 89  ? 26.407 1.523   15.478  0.30 18.26 ?  89  ALA   A H    1 
ATOM   1901 H  HA   . ALA   A 1 89  ? 25.537 -0.810  16.369  1.00 17.65 ?  89  ALA   A HA   1 
ATOM   1902 H  HB1  . ALA   A 1 89  ? 26.015 -2.058  14.429  1.00 17.33 ?  89  ALA   A HB1  1 
ATOM   1903 H  HB2  . ALA   A 1 89  ? 24.822 -1.053  14.126  1.00 17.33 ?  89  ALA   A HB2  1 
ATOM   1904 H  HB3  . ALA   A 1 89  ? 26.293 -0.713  13.631  1.00 17.33 ?  89  ALA   A HB3  1 
ATOM   1905 N  N    . LYS   A 1 90  ? 28.008 -1.653  16.349  1.00 16.08 ?  90  LYS   A N    1 
ATOM   1906 C  CA   . LYS   A 1 90  ? 29.453 -1.811  16.491  1.00 16.87 ?  90  LYS   A CA   1 
ATOM   1907 C  C    . LYS   A 1 90  ? 30.150 -1.615  15.148  1.00 15.37 ?  90  LYS   A C    1 
ATOM   1908 O  O    . LYS   A 1 90  ? 31.083 -0.804  15.022  1.00 16.29 ?  90  LYS   A O    1 
ATOM   1909 C  CB   . LYS   A 1 90  ? 29.792 -3.177  17.090  1.00 19.03 ?  90  LYS   A CB   1 
ATOM   1910 C  CG   . LYS   A 1 90  ? 31.266 -3.329  17.441  1.00 23.61 ?  90  LYS   A CG   1 
ATOM   1911 C  CD   . LYS   A 1 90  ? 31.509 -4.595  18.246  1.00 27.49 ?  90  LYS   A CD   1 
ATOM   1912 C  CE   . LYS   A 1 90  ? 32.900 -4.619  18.862  1.00 30.50 ?  90  LYS   A CE   1 
ATOM   1913 N  NZ   . LYS   A 1 90  ? 33.969 -4.882  17.861  1.00 34.58 ?  90  LYS   A NZ   1 
ATOM   1914 H  H    . LYS   A 1 90  ? 27.534 -2.343  16.532  1.00 19.27 ?  90  LYS   A H    1 
ATOM   1915 H  HA   . LYS   A 1 90  ? 29.784 -1.132  17.097  1.00 20.22 ?  90  LYS   A HA   1 
ATOM   1916 H  HB2  . LYS   A 1 90  ? 29.276 -3.302  17.904  1.00 22.82 ?  90  LYS   A HB2  1 
ATOM   1917 H  HB3  . LYS   A 1 90  ? 29.564 -3.870  16.449  1.00 22.82 ?  90  LYS   A HB3  1 
ATOM   1918 H  HG2  . LYS   A 1 90  ? 31.788 -3.380  16.625  1.00 28.31 ?  90  LYS   A HG2  1 
ATOM   1919 H  HG3  . LYS   A 1 90  ? 31.549 -2.568  17.974  1.00 28.31 ?  90  LYS   A HG3  1 
ATOM   1920 H  HD2  . LYS   A 1 90  ? 30.859 -4.647  18.964  1.00 32.97 ?  90  LYS   A HD2  1 
ATOM   1921 H  HD3  . LYS   A 1 90  ? 31.423 -5.366  17.662  1.00 32.97 ?  90  LYS   A HD3  1 
ATOM   1922 H  HE2  . LYS   A 1 90  ? 33.080 -3.758  19.272  1.00 36.58 ?  90  LYS   A HE2  1 
ATOM   1923 H  HE3  . LYS   A 1 90  ? 32.938 -5.319  19.532  1.00 36.58 ?  90  LYS   A HE3  1 
ATOM   1924 H  HZ1  . LYS   A 1 90  ? 34.765 -4.888  18.260  1.00 41.47 ?  90  LYS   A HZ1  1 
ATOM   1925 H  HZ2  . LYS   A 1 90  ? 33.835 -5.673  17.474  1.00 41.47 ?  90  LYS   A HZ2  1 
ATOM   1926 H  HZ3  . LYS   A 1 90  ? 33.964 -4.250  17.236  1.00 41.47 ?  90  LYS   A HZ3  1 
ATOM   1927 N  N    . HIS   A 1 91  ? 29.687 -2.337  14.128  1.00 13.80 ?  91  HIS   A N    1 
ATOM   1928 C  CA   . HIS   A 1 91  ? 30.262 -2.317  12.798  1.00 13.15 ?  91  HIS   A CA   1 
ATOM   1929 C  C    . HIS   A 1 91  ? 29.178 -2.043  11.770  1.00 12.13 ?  91  HIS   A C    1 
ATOM   1930 O  O    . HIS   A 1 91  ? 28.015 -2.408  11.961  1.00 12.65 ?  91  HIS   A O    1 
ATOM   1931 C  CB   . HIS   A 1 91  ? 30.851 -3.684  12.433  1.00 15.97 ?  91  HIS   A CB   1 
ATOM   1932 C  CG   . HIS   A 1 91  ? 31.843 -4.205  13.421  1.00 20.57 ?  91  HIS   A CG   1 
ATOM   1933 N  ND1  . HIS   A 1 91  ? 33.129 -3.720  13.510  1.00 22.70 ?  91  HIS   A ND1  1 
ATOM   1934 C  CD2  . HIS   A 1 91  ? 31.743 -5.180  14.355  1.00 22.37 ?  91  HIS   A CD2  1 
ATOM   1935 C  CE1  . HIS   A 1 91  ? 33.779 -4.372  14.458  1.00 23.80 ?  91  HIS   A CE1  1 
ATOM   1936 N  NE2  . HIS   A 1 91  ? 32.960 -5.265  14.986  1.00 23.78 ?  91  HIS   A NE2  1 
ATOM   1937 H  H    . HIS   A 1 91  ? 29.012 -2.881  14.194  1.00 16.54 ?  91  HIS   A H    1 
ATOM   1938 H  HA   . HIS   A 1 91  ? 30.953 -1.642  12.736  1.00 15.76 ?  91  HIS   A HA   1 
ATOM   1939 H  HB2  . HIS   A 1 91  ? 30.128 -4.330  12.375  1.00 19.14 ?  91  HIS   A HB2  1 
ATOM   1940 H  HB3  . HIS   A 1 91  ? 31.296 -3.614  11.574  1.00 19.14 ?  91  HIS   A HB3  1 
ATOM   1941 H  HD1  . HIS   A 1 91  ? 33.460 -3.092  13.019  1.00 27.22 ?  91  HIS   A HD1  1 
ATOM   1942 H  HD2  . HIS   A 1 91  ? 30.997 -5.695  14.539  1.00 26.82 ?  91  HIS   A HD2  1 
ATOM   1943 H  HE1  . HIS   A 1 91  ? 34.666 -4.220  14.709  1.00 28.54 ?  91  HIS   A HE1  1 
ATOM   1944 N  N    . CYS   A 1 92  ? 29.584 -1.448  10.653  1.00 11.70 ?  92  CYS   A N    1 
ATOM   1945 C  CA   . CYS   A 1 92  ? 28.748 -1.376  9.463   1.00 11.55 ?  92  CYS   A CA   1 
ATOM   1946 C  C    . CYS   A 1 92  ? 29.394 -2.195  8.356   1.00 11.38 ?  92  CYS   A C    1 
ATOM   1947 O  O    . CYS   A 1 92  ? 30.554 -1.952  7.992   1.00 11.71 ?  92  CYS   A O    1 
ATOM   1948 C  CB   . CYS   A 1 92  ? 28.536 0.068   9.000   1.00 11.97 ?  92  CYS   A CB   1 
ATOM   1949 S  SG   . CYS   A 1 92  ? 27.522 0.179   7.489   1.00 11.57 ?  92  CYS   A SG   1 
ATOM   1950 H  H    . CYS   A 1 92  ? 30.352 -1.067  10.561  1.00 14.03 ?  92  CYS   A H    1 
ATOM   1951 H  HA   . CYS   A 1 92  ? 27.881 -1.757  9.659   1.00 13.84 ?  92  CYS   A HA   1 
ATOM   1952 H  HB2  . CYS   A 1 92  ? 28.078 0.566   9.699   1.00 14.35 ?  92  CYS   A HB2  1 
ATOM   1953 H  HB3  . CYS   A 1 92  ? 29.395 0.476   8.813   1.00 14.35 ?  92  CYS   A HB3  1 
ATOM   1954 H  HG   . CYS   A 1 92  ? 27.392 1.330   7.199   1.00 13.87 ?  92  CYS   A HG   1 
ATOM   1955 N  N    . LEU   A 1 93  ? 28.655 -3.181  7.850   1.00 10.77 ?  93  LEU   A N    1 
ATOM   1956 C  CA   . LEU   A 1 93  ? 29.061 -3.941  6.675   1.00 10.55 ?  93  LEU   A CA   1 
ATOM   1957 C  C    . LEU   A 1 93  ? 28.466 -3.248  5.454   1.00 10.04 ?  93  LEU   A C    1 
ATOM   1958 O  O    . LEU   A 1 93  ? 27.251 -3.306  5.228   1.00 10.56 ?  93  LEU   A O    1 
ATOM   1959 C  CB   . LEU   A 1 93  ? 28.581 -5.387  6.780   1.00 10.99 ?  93  LEU   A CB   1 
ATOM   1960 C  CG   . LEU   A 1 93  ? 28.965 -6.292  5.610   1.00 11.47 ?  93  LEU   A CG   1 
ATOM   1961 C  CD1  . LEU   A 1 93  ? 30.471 -6.550  5.594   1.00 12.64 ?  93  LEU   A CD1  1 
ATOM   1962 C  CD2  . LEU   A 1 93  ? 28.200 -7.612  5.650   1.00 12.27 ?  93  LEU   A CD2  1 
ATOM   1963 H  H    . LEU   A 1 93  ? 27.902 -3.431  8.183   1.00 12.91 ?  93  LEU   A H    1 
ATOM   1964 H  HA   . LEU   A 1 93  ? 30.024 -3.931  6.601   1.00 12.64 ?  93  LEU   A HA   1 
ATOM   1965 H  HB2  . LEU   A 1 93  ? 28.960 -5.771  7.589   1.00 13.16 ?  93  LEU   A HB2  1 
ATOM   1966 H  HB3  . LEU   A 1 93  ? 27.616 -5.387  6.844   1.00 13.16 ?  93  LEU   A HB3  1 
ATOM   1967 H  HG   . LEU   A 1 93  ? 28.746 -5.845  4.786   1.00 13.74 ?  93  LEU   A HG   1 
ATOM   1968 H  HD11 . LEU   A 1 93  ? 30.683 -7.162  4.871   1.00 15.15 ?  93  LEU   A HD11 1 
ATOM   1969 H  HD12 . LEU   A 1 93  ? 30.944 -5.714  5.470   1.00 15.15 ?  93  LEU   A HD12 1 
ATOM   1970 H  HD13 . LEU   A 1 93  ? 30.738 -6.952  6.445   1.00 15.15 ?  93  LEU   A HD13 1 
ATOM   1971 H  HD21 . LEU   A 1 93  ? 28.487 -8.163  4.901   1.00 14.70 ?  93  LEU   A HD21 1 
ATOM   1972 H  HD22 . LEU   A 1 93  ? 28.390 -8.067  6.484   1.00 14.70 ?  93  LEU   A HD22 1 
ATOM   1973 H  HD23 . LEU   A 1 93  ? 27.253 -7.426  5.578   1.00 14.70 ?  93  LEU   A HD23 1 
ATOM   1974 N  N    . HIS   A 1 94  ? 29.317 -2.557  4.692   1.00 9.83  ?  94  HIS   A N    1 
ATOM   1975 C  CA   . HIS   A 1 94  ? 28.892 -1.884  3.470   1.00 9.92  ?  94  HIS   A CA   1 
ATOM   1976 C  C    . HIS   A 1 94  ? 28.895 -2.917  2.360   1.00 10.06 ?  94  HIS   A C    1 
ATOM   1977 O  O    . HIS   A 1 94  ? 29.958 -3.434  2.012   1.00 11.65 ?  94  HIS   A O    1 
ATOM   1978 C  CB   . HIS   A 1 94  ? 29.855 -0.742  3.141   1.00 9.95  ?  94  HIS   A CB   1 
ATOM   1979 C  CG   . HIS   A 1 94  ? 29.840 0.351   4.152   1.00 10.02 ?  94  HIS   A CG   1 
ATOM   1980 N  ND1  . HIS   A 1 94  ? 28.974 1.421   4.086   1.00 10.16 ?  94  HIS   A ND1  1 
ATOM   1981 C  CD2  . HIS   A 1 94  ? 30.575 0.519   5.273   1.00 10.74 ?  94  HIS   A CD2  1 
ATOM   1982 C  CE1  . HIS   A 1 94  ? 29.186 2.203   5.130   1.00 10.36 ?  94  HIS   A CE1  1 
ATOM   1983 N  NE2  . HIS   A 1 94  ? 30.150 1.676   5.866   1.00 10.85 ?  94  HIS   A NE2  1 
ATOM   1984 H  H    . HIS   A 1 94  ? 30.159 -2.464  4.864   1.00 11.78 ?  94  HIS   A H    1 
ATOM   1985 H  HA   . HIS   A 1 94  ? 27.993 -1.531  3.580   1.00 11.88 ?  94  HIS   A HA   1 
ATOM   1986 H  HB2  . HIS   A 1 94  ? 30.751 -1.093  3.094   1.00 11.92 ?  94  HIS   A HB2  1 
ATOM   1987 H  HB3  . HIS   A 1 94  ? 29.598 -0.358  2.286   1.00 11.92 ?  94  HIS   A HB3  1 
ATOM   1988 H  HD2  . HIS   A 1 94  ? 31.239 -0.044  5.588   1.00 12.87 ?  94  HIS   A HD2  1 
ATOM   1989 H  HE1  . HIS   A 1 94  ? 28.723 2.994   5.315   1.00 12.42 ?  94  HIS   A HE1  1 
ATOM   1990 H  HE2  . HIS   A 1 94  ? 30.460 2.016   6.591   1.00 12.99 ?  94  HIS   A HE2  1 
ATOM   1991 N  N    . VAL   A 1 95  ? 27.724 -3.239  1.816   1.00 9.63  ?  95  VAL   A N    1 
ATOM   1992 C  CA   . VAL   A 1 95  ? 27.579 -4.270  0.794   1.00 10.04 ?  95  VAL   A CA   1 
ATOM   1993 C  C    . VAL   A 1 95  ? 27.032 -3.639  -0.474  1.00 9.63  ?  95  VAL   A C    1 
ATOM   1994 O  O    . VAL   A 1 95  ? 26.027 -2.920  -0.425  1.00 10.52 ?  95  VAL   A O    1 
ATOM   1995 C  CB   . VAL   A 1 95  ? 26.659 -5.421  1.247   1.00 10.55 ?  95  VAL   A CB   1 
ATOM   1996 C  CG1  . VAL   A 1 95  ? 26.559 -6.462  0.150   1.00 11.71 ?  95  VAL   A CG1  1 
ATOM   1997 C  CG2  . VAL   A 1 95  ? 27.161 -6.036  2.536   1.00 10.83 ?  95  VAL   A CG2  1 
ATOM   1998 H  H    . VAL   A 1 95  ? 26.975 -2.866  2.031   1.00 11.54 ?  95  VAL   A H    1 
ATOM   1999 H  HA   . VAL   A 1 95  ? 28.447 -4.646  0.592   1.00 12.03 ?  95  VAL   A HA   1 
ATOM   2000 H  HB   . VAL   A 1 95  ? 25.769 -5.074  1.411   1.00 12.64 ?  95  VAL   A HB   1 
ATOM   2001 H  HG11 . VAL   A 1 95  ? 26.179 -7.277  0.518   1.00 14.03 ?  95  VAL   A HG11 1 
ATOM   2002 H  HG12 . VAL   A 1 95  ? 25.990 -6.127  -0.559  1.00 14.03 ?  95  VAL   A HG12 1 
ATOM   2003 H  HG13 . VAL   A 1 95  ? 27.449 -6.645  -0.196  1.00 14.03 ?  95  VAL   A HG13 1 
ATOM   2004 H  HG21 . VAL   A 1 95  ? 26.597 -6.796  2.764   1.00 12.97 ?  95  VAL   A HG21 1 
ATOM   2005 H  HG22 . VAL   A 1 95  ? 28.075 -6.325  2.416   1.00 12.97 ?  95  VAL   A HG22 1 
ATOM   2006 H  HG23 . VAL   A 1 95  ? 27.111 -5.370  3.242   1.00 12.97 ?  95  VAL   A HG23 1 
ATOM   2007 N  N    . VAL   A 1 96  ? 27.663 -3.932  -1.610  1.00 9.64  ?  96  VAL   A N    1 
ATOM   2008 C  CA   . VAL   A 1 96  ? 27.259 -3.386  -2.899  1.00 10.45 ?  96  VAL   A CA   1 
ATOM   2009 C  C    . VAL   A 1 96  ? 26.456 -4.433  -3.666  1.00 10.56 ?  96  VAL   A C    1 
ATOM   2010 O  O    . VAL   A 1 96  ? 27.018 -5.381  -4.224  1.00 11.38 ?  96  VAL   A O    1 
ATOM   2011 C  CB   . VAL   A 1 96  ? 28.455 -2.911  -3.725  1.00 11.15 ?  96  VAL   A CB   1 
ATOM   2012 C  CG1  . VAL   A 1 96  ? 27.952 -2.277  -5.005  1.00 11.26 ?  96  VAL   A CG1  1 
ATOM   2013 C  CG2  . VAL   A 1 96  ? 29.318 -1.940  -2.935  1.00 11.92 ?  96  VAL   A CG2  1 
ATOM   2014 H  H    . VAL   A 1 96  ? 28.349 -4.457  -1.656  1.00 11.54 ?  96  VAL   A H    1 
ATOM   2015 H  HA   . VAL   A 1 96  ? 26.684 -2.625  -2.747  1.00 12.52 ?  96  VAL   A HA   1 
ATOM   2016 H  HB   . VAL   A 1 96  ? 29.005 -3.674  -3.963  1.00 13.36 ?  96  VAL   A HB   1 
ATOM   2017 H  HG11 . VAL   A 1 96  ? 28.684 -1.793  -5.422  1.00 13.49 ?  96  VAL   A HG11 1 
ATOM   2018 H  HG12 . VAL   A 1 96  ? 27.631 -2.968  -5.600  1.00 13.49 ?  96  VAL   A HG12 1 
ATOM   2019 H  HG13 . VAL   A 1 96  ? 27.234 -1.659  -4.790  1.00 13.49 ?  96  VAL   A HG13 1 
ATOM   2020 H  HG21 . VAL   A 1 96  ? 30.024 -1.601  -3.503  1.00 14.28 ?  96  VAL   A HG21 1 
ATOM   2021 H  HG22 . VAL   A 1 96  ? 28.762 -1.203  -2.624  1.00 14.28 ?  96  VAL   A HG22 1 
ATOM   2022 H  HG23 . VAL   A 1 96  ? 29.700 -2.402  -2.169  1.00 14.28 ?  96  VAL   A HG23 1 
ATOM   2023 N  N    A GLY   A 1 97  ? 25.136 -4.277  -3.680  0.70 10.77 ?  97  GLY   A N    1 
ATOM   2024 N  N    B GLY   A 1 97  ? 25.141 -4.250  -3.735  0.30 10.77 ?  97  GLY   A N    1 
ATOM   2025 C  CA   A GLY   A 1 97  ? 24.311 -5.026  -4.588  0.70 11.61 ?  97  GLY   A CA   1 
ATOM   2026 C  CA   B GLY   A 1 97  ? 24.330 -5.029  -4.637  0.30 11.29 ?  97  GLY   A CA   1 
ATOM   2027 C  C    A GLY   A 1 97  ? 24.276 -4.339  -5.939  0.70 11.44 ?  97  GLY   A C    1 
ATOM   2028 C  C    B GLY   A 1 97  ? 24.403 -4.464  -6.044  0.30 11.51 ?  97  GLY   A C    1 
ATOM   2029 O  O    A GLY   A 1 97  ? 24.528 -3.135  -6.049  0.70 11.85 ?  97  GLY   A O    1 
ATOM   2030 O  O    B GLY   A 1 97  ? 24.786 -3.308  -6.247  0.30 11.84 ?  97  GLY   A O    1 
ATOM   2031 H  H    A GLY   A 1 97  ? 24.704 -3.736  -3.165  0.70 12.90 ?  97  GLY   A H    1 
ATOM   2032 H  H    B GLY   A 1 97  ? 24.702 -3.675  -3.267  0.30 12.91 ?  97  GLY   A H    1 
ATOM   2033 H  HA2  A GLY   A 1 97  ? 24.673 -5.917  -4.690  0.70 13.91 ?  97  GLY   A HA2  1 
ATOM   2034 H  HA2  B GLY   A 1 97  ? 24.647 -5.945  -4.646  0.30 13.53 ?  97  GLY   A HA2  1 
ATOM   2035 H  HA3  A GLY   A 1 97  ? 23.409 -5.089  -4.234  0.70 13.91 ?  97  GLY   A HA3  1 
ATOM   2036 H  HA3  B GLY   A 1 97  ? 23.407 -5.019  -4.341  0.30 13.53 ?  97  GLY   A HA3  1 
ATOM   2037 N  N    A PRO   A 1 98  ? 23.966 -5.082  -6.996  0.70 11.06 ?  98  PRO   A N    1 
ATOM   2038 N  N    B PRO   A 1 98  ? 24.042 -5.265  -7.045  0.30 11.98 ?  98  PRO   A N    1 
ATOM   2039 C  CA   A PRO   A 1 98  ? 23.830 -4.455  -8.315  0.70 12.04 ?  98  PRO   A CA   1 
ATOM   2040 C  CA   B PRO   A 1 98  ? 24.048 -4.761  -8.424  0.30 12.97 ?  98  PRO   A CA   1 
ATOM   2041 C  C    A PRO   A 1 98  ? 22.709 -3.427  -8.340  0.70 11.72 ?  98  PRO   A C    1 
ATOM   2042 C  C    B PRO   A 1 98  ? 22.959 -3.722  -8.644  0.30 13.32 ?  98  PRO   A C    1 
ATOM   2043 O  O    A PRO   A 1 98  ? 21.643 -3.619  -7.749  0.70 11.61 ?  98  PRO   A O    1 
ATOM   2044 O  O    B PRO   A 1 98  ? 21.834 -3.856  -8.156  0.30 13.63 ?  98  PRO   A O    1 
ATOM   2045 C  CB   A PRO   A 1 98  ? 23.530 -5.640  -9.239  0.70 12.70 ?  98  PRO   A CB   1 
ATOM   2046 C  CB   B PRO   A 1 98  ? 23.786 -6.019  -9.261  0.30 12.90 ?  98  PRO   A CB   1 
ATOM   2047 C  CG   A PRO   A 1 98  ? 22.951 -6.692  -8.336  0.70 12.85 ?  98  PRO   A CG   1 
ATOM   2048 C  CG   B PRO   A 1 98  ? 23.029 -6.926  -8.341  0.30 12.78 ?  98  PRO   A CG   1 
ATOM   2049 C  CD   A PRO   A 1 98  ? 23.706 -6.533  -7.039  0.70 11.60 ?  98  PRO   A CD   1 
ATOM   2050 C  CD   B PRO   A 1 98  ? 23.612 -6.674  -6.973  0.30 11.88 ?  98  PRO   A CD   1 
ATOM   2051 H  HA   A PRO   A 1 98  ? 24.665 -4.037  -8.569  0.70 14.43 ?  98  PRO   A HA   1 
ATOM   2052 H  HA   B PRO   A 1 98  ? 24.914 -4.387  -8.652  0.30 15.54 ?  98  PRO   A HA   1 
ATOM   2053 H  HB2  A PRO   A 1 98  ? 22.886 -5.371  -9.910  0.70 15.22 ?  98  PRO   A HB2  1 
ATOM   2054 H  HB2  B PRO   A 1 98  ? 23.252 -5.788  -10.038 0.30 15.46 ?  98  PRO   A HB2  1 
ATOM   2055 H  HB3  A PRO   A 1 98  ? 24.351 -5.949  -9.648  0.70 15.22 ?  98  PRO   A HB3  1 
ATOM   2056 H  HB3  B PRO   A 1 98  ? 24.628 -6.419  -9.527  0.30 15.46 ?  98  PRO   A HB3  1 
ATOM   2057 H  HG2  A PRO   A 1 98  ? 22.005 -6.531  -8.205  0.70 15.40 ?  98  PRO   A HG2  1 
ATOM   2058 H  HG2  B PRO   A 1 98  ? 22.087 -6.694  -8.361  0.30 15.31 ?  98  PRO   A HG2  1 
ATOM   2059 H  HG3  A PRO   A 1 98  ? 23.106 -7.571  -8.715  0.70 15.40 ?  98  PRO   A HG3  1 
ATOM   2060 H  HG3  B PRO   A 1 98  ? 23.163 -7.846  -8.611  0.30 15.31 ?  98  PRO   A HG3  1 
ATOM   2061 H  HD2  A PRO   A 1 98  ? 23.154 -6.812  -6.287  0.70 13.89 ?  98  PRO   A HD2  1 
ATOM   2062 H  HD2  B PRO   A 1 98  ? 22.932 -6.786  -6.290  0.30 14.23 ?  98  PRO   A HD2  1 
ATOM   2063 H  HD3  A PRO   A 1 98  ? 24.544 -7.019  -7.064  0.70 13.89 ?  98  PRO   A HD3  1 
ATOM   2064 H  HD3  B PRO   A 1 98  ? 24.372 -7.257  -6.818  0.30 14.23 ?  98  PRO   A HD3  1 
ATOM   2065 N  N    A ASN   A 1 99  ? 22.973 -2.317  -9.027  0.70 12.59 ?  99  ASN   A N    1 
ATOM   2066 N  N    B ASN   A 1 99  ? 23.302 -2.682  -9.399  0.30 13.85 ?  99  ASN   A N    1 
ATOM   2067 C  CA   A ASN   A 1 99  ? 21.995 -1.256  -9.239  0.70 13.55 ?  99  ASN   A CA   1 
ATOM   2068 C  CA   B ASN   A 1 99  ? 22.357 -1.630  -9.756  0.30 14.36 ?  99  ASN   A CA   1 
ATOM   2069 C  C    A ASN   A 1 99  ? 21.442 -1.408  -10.651 0.70 14.08 ?  99  ASN   A C    1 
ATOM   2070 C  C    B ASN   A 1 99  ? 21.738 -1.987  -11.099 0.30 14.41 ?  99  ASN   A C    1 
ATOM   2071 O  O    A ASN   A 1 99  ? 22.137 -1.124  -11.635 0.70 15.84 ?  99  ASN   A O    1 
ATOM   2072 O  O    B ASN   A 1 99  ? 22.394 -1.892  -12.142 0.30 14.25 ?  99  ASN   A O    1 
ATOM   2073 C  CB   A ASN   A 1 99  ? 22.651 0.110   -9.053  0.70 13.62 ?  99  ASN   A CB   1 
ATOM   2074 C  CB   B ASN   A 1 99  ? 23.054 -0.277  -9.844  0.30 15.20 ?  99  ASN   A CB   1 
ATOM   2075 C  CG   A ASN   A 1 99  ? 21.642 1.252   -9.055  0.70 14.15 ?  99  ASN   A CG   1 
ATOM   2076 C  CG   B ASN   A 1 99  ? 22.083 0.863   -10.109 0.30 16.24 ?  99  ASN   A CG   1 
ATOM   2077 O  OD1  A ASN   A 1 99  ? 20.636 1.208   -9.766  0.70 14.98 ?  99  ASN   A OD1  1 
ATOM   2078 O  OD1  B ASN   A 1 99  ? 21.007 0.662   -10.666 0.30 16.21 ?  99  ASN   A OD1  1 
ATOM   2079 N  ND2  A ASN   A 1 99  ? 21.911 2.278   -8.254  0.70 14.89 ?  99  ASN   A ND2  1 
ATOM   2080 N  ND2  B ASN   A 1 99  ? 22.469 2.071   -9.719  0.30 17.73 ?  99  ASN   A ND2  1 
ATOM   2081 H  H    A ASN   A 1 99  ? 23.738 -2.148  -9.373  0.70 15.08 ?  99  ASN   A H    1 
ATOM   2082 H  H    B ASN   A 1 99  ? 24.087 -2.563  -9.722  0.30 16.59 ?  99  ASN   A H    1 
ATOM   2083 H  HA   A ASN   A 1 99  ? 21.266 -1.348  -8.595  0.70 16.24 ?  99  ASN   A HA   1 
ATOM   2084 H  HA   B ASN   A 1 99  ? 21.650 -1.581  -9.093  0.30 17.21 ?  99  ASN   A HA   1 
ATOM   2085 H  HB2  A ASN   A 1 99  ? 23.123 0.124   -8.206  0.70 16.33 ?  99  ASN   A HB2  1 
ATOM   2086 H  HB2  B ASN   A 1 99  ? 23.502 -0.103  -9.009  0.30 18.22 ?  99  ASN   A HB2  1 
ATOM   2087 H  HB3  A ASN   A 1 99  ? 23.271 0.257   -9.783  0.70 16.33 ?  99  ASN   A HB3  1 
ATOM   2088 H  HB3  B ASN   A 1 99  ? 23.695 -0.307  -10.574 0.30 18.22 ?  99  ASN   A HB3  1 
ATOM   2089 H  HD21 A ASN   A 1 99  ? 21.374 2.948   -8.214  0.70 17.84 ?  99  ASN   A HD21 1 
ATOM   2090 H  HD21 B ASN   A 1 99  ? 21.961 2.751   -9.855  0.30 21.25 ?  99  ASN   A HD21 1 
ATOM   2091 H  HD22 A ASN   A 1 99  ? 22.624 2.271   -7.769  0.70 17.84 ?  99  ASN   A HD22 1 
ATOM   2092 H  HD22 B ASN   A 1 99  ? 23.231 2.174   -9.343  0.30 21.25 ?  99  ASN   A HD22 1 
ATOM   2093 N  N    A VAL   A 1 100 ? 20.188 -1.859  -10.740 0.70 15.46 ?  100 VAL   A N    1 
ATOM   2094 N  N    B VAL   A 1 100 ? 20.464 -2.374  -11.069 0.30 16.07 ?  100 VAL   A N    1 
ATOM   2095 C  CA   A VAL   A 1 100 ? 19.558 -2.084  -12.037 0.70 17.40 ?  100 VAL   A CA   1 
ATOM   2096 C  CA   B VAL   A 1 100 ? 19.793 -2.824  -12.282 0.30 18.25 ?  100 VAL   A CA   1 
ATOM   2097 C  C    A VAL   A 1 100 ? 19.447 -0.779  -12.811 0.70 17.60 ?  100 VAL   A C    1 
ATOM   2098 C  C    B VAL   A 1 100 ? 19.480 -1.648  -13.195 0.30 18.17 ?  100 VAL   A C    1 
ATOM   2099 O  O    A VAL   A 1 100 ? 19.517 -0.767  -14.046 0.70 18.85 ?  100 VAL   A O    1 
ATOM   2100 O  O    B VAL   A 1 100 ? 19.385 -1.814  -14.417 0.30 18.11 ?  100 VAL   A O    1 
ATOM   2101 C  CB   A VAL   A 1 100 ? 18.192 -2.780  -11.847 0.70 19.24 ?  100 VAL   A CB   1 
ATOM   2102 C  CB   B VAL   A 1 100 ? 18.542 -3.651  -11.932 0.30 19.94 ?  100 VAL   A CB   1 
ATOM   2103 C  CG1  A VAL   A 1 100 ? 17.470 -2.943  -13.179 0.70 20.00 ?  100 VAL   A CG1  1 
ATOM   2104 C  CG1  B VAL   A 1 100 ? 18.411 -4.826  -12.880 0.30 20.82 ?  100 VAL   A CG1  1 
ATOM   2105 C  CG2  A VAL   A 1 100 ? 18.379 -4.136  -11.180 0.70 19.79 ?  100 VAL   A CG2  1 
ATOM   2106 C  CG2  B VAL   A 1 100 ? 18.614 -4.137  -10.494 0.30 20.24 ?  100 VAL   A CG2  1 
ATOM   2107 H  H    A VAL   A 1 100 ? 19.678 -2.040  -10.061 0.70 18.53 ?  100 VAL   A H    1 
ATOM   2108 H  H    B VAL   A 1 100 ? 19.980 -2.372  -10.358 0.30 19.26 ?  100 VAL   A H    1 
ATOM   2109 H  HA   A VAL   A 1 100 ? 20.116 -2.683  -12.550 0.70 20.86 ?  100 VAL   A HA   1 
ATOM   2110 H  HA   B VAL   A 1 100 ? 20.385 -3.408  -12.777 0.30 21.88 ?  100 VAL   A HA   1 
ATOM   2111 H  HB   A VAL   A 1 100 ? 17.632 -2.237  -11.271 0.70 23.06 ?  100 VAL   A HB   1 
ATOM   2112 H  HB   B VAL   A 1 100 ? 17.747 -3.100  -12.027 0.30 23.91 ?  100 VAL   A HB   1 
ATOM   2113 H  HG11 A VAL   A 1 100 ? 16.713 -3.539  -13.059 0.70 23.98 ?  100 VAL   A HG11 1 
ATOM   2114 H  HG11 B VAL   A 1 100 ? 17.554 -5.254  -12.735 0.30 24.96 ?  100 VAL   A HG11 1 
ATOM   2115 H  HG12 A VAL   A 1 100 ? 17.160 -2.076  -13.483 0.70 23.98 ?  100 VAL   A HG12 1 
ATOM   2116 H  HG12 B VAL   A 1 100 ? 18.473 -4.503  -13.790 0.30 24.96 ?  100 VAL   A HG12 1 
ATOM   2117 H  HG13 A VAL   A 1 100 ? 18.085 -3.322  -13.828 0.70 23.98 ?  100 VAL   A HG13 1 
ATOM   2118 H  HG13 B VAL   A 1 100 ? 19.130 -5.453  -12.700 0.30 24.96 ?  100 VAL   A HG13 1 
ATOM   2119 H  HG21 A VAL   A 1 100 ? 17.520 -4.582  -11.122 0.70 23.73 ?  100 VAL   A HG21 1 
ATOM   2120 H  HG21 B VAL   A 1 100 ? 17.967 -4.836  -10.375 0.30 24.26 ?  100 VAL   A HG21 1 
ATOM   2121 H  HG22 A VAL   A 1 100 ? 18.994 -4.666  -11.710 0.70 23.73 ?  100 VAL   A HG22 1 
ATOM   2122 H  HG22 B VAL   A 1 100 ? 19.506 -4.480  -10.316 0.30 24.26 ?  100 VAL   A HG22 1 
ATOM   2123 H  HG23 A VAL   A 1 100 ? 18.741 -4.000  -10.290 0.70 23.73 ?  100 VAL   A HG23 1 
ATOM   2124 H  HG23 B VAL   A 1 100 ? 18.414 -3.397  -9.896  0.30 24.26 ?  100 VAL   A HG23 1 
ATOM   2125 N  N    A ASN   A 1 101 ? 19.281 0.338   -12.108 0.70 18.40 ?  101 ASN   A N    1 
ATOM   2126 N  N    B ASN   A 1 101 ? 19.321 -0.445  -12.632 0.30 18.52 ?  101 ASN   A N    1 
ATOM   2127 C  CA   A ASN   A 1 101 ? 19.220 1.626   -12.784 0.70 20.04 ?  101 ASN   A CA   1 
ATOM   2128 C  CA   B ASN   A 1 101 ? 19.137 0.735   -13.471 0.30 18.70 ?  101 ASN   A CA   1 
ATOM   2129 C  C    A ASN   A 1 101 ? 20.573 2.068   -13.340 0.70 21.84 ?  101 ASN   A C    1 
ATOM   2130 C  C    B ASN   A 1 101 ? 20.381 1.011   -14.301 0.30 19.52 ?  101 ASN   A C    1 
ATOM   2131 O  O    A ASN   A 1 101 ? 20.633 3.116   -13.994 0.70 23.86 ?  101 ASN   A O    1 
ATOM   2132 O  O    B ASN   A 1 101 ? 20.283 1.551   -15.410 0.30 19.48 ?  101 ASN   A O    1 
ATOM   2133 C  CB   A ASN   A 1 101 ? 18.584 2.664   -11.852 0.70 19.53 ?  101 ASN   A CB   1 
ATOM   2134 C  CB   B ASN   A 1 101 ? 18.801 1.950   -12.606 0.30 18.18 ?  101 ASN   A CB   1 
ATOM   2135 C  CG   A ASN   A 1 101 ? 17.178 2.257   -11.411 0.70 19.00 ?  101 ASN   A CG   1 
ATOM   2136 C  CG   B ASN   A 1 101 ? 17.598 1.715   -11.711 0.30 18.34 ?  101 ASN   A CG   1 
ATOM   2137 O  OD1  A ASN   A 1 101 ? 16.377 1.782   -12.220 0.70 19.69 ?  101 ASN   A OD1  1 
ATOM   2138 O  OD1  B ASN   A 1 101 ? 16.596 1.138   -12.134 0.30 18.73 ?  101 ASN   A OD1  1 
ATOM   2139 N  ND2  A ASN   A 1 101 ? 16.882 2.419   -10.126 0.70 19.27 ?  101 ASN   A ND2  1 
ATOM   2140 N  ND2  B ASN   A 1 101 ? 17.695 2.155   -10.463 0.30 18.30 ?  101 ASN   A ND2  1 
ATOM   2141 H  H    A ASN   A 1 101 ? 19.196 0.375   -11.254 0.70 22.06 ?  101 ASN   A H    1 
ATOM   2142 H  H    B ASN   A 1 101 ? 19.321 -0.286  -11.784 0.30 22.20 ?  101 ASN   A H    1 
ATOM   2143 H  HA   A ASN   A 1 101 ? 18.633 1.535   -13.545 0.70 24.03 ?  101 ASN   A HA   1 
ATOM   2144 H  HA   B ASN   A 1 101 ? 18.391 0.585   -14.073 0.30 22.42 ?  101 ASN   A HA   1 
ATOM   2145 H  HB2  A ASN   A 1 101 ? 19.134 2.766   -11.061 0.70 23.41 ?  101 ASN   A HB2  1 
ATOM   2146 H  HB2  B ASN   A 1 101 ? 19.559 2.159   -12.038 0.30 21.80 ?  101 ASN   A HB2  1 
ATOM   2147 H  HB3  A ASN   A 1 101 ? 18.519 3.513   -12.323 0.70 23.41 ?  101 ASN   A HB3  1 
ATOM   2148 H  HB3  B ASN   A 1 101 ? 18.602 2.708   -13.183 0.30 21.80 ?  101 ASN   A HB3  1 
ATOM   2149 H  HD21 A ASN   A 1 101 ? 16.103 2.202   -9.834  0.70 23.10 ?  101 ASN   A HD21 1 
ATOM   2150 H  HD21 B ASN   A 1 101 ? 17.039 2.047   -9.919  0.30 21.94 ?  101 ASN   A HD21 1 
ATOM   2151 H  HD22 A ASN   A 1 101 ? 17.464 2.755   -9.591  0.70 23.10 ?  101 ASN   A HD22 1 
ATOM   2152 H  HD22 B ASN   A 1 101 ? 18.410 2.554   -10.202 0.30 21.94 ?  101 ASN   A HD22 1 
ATOM   2153 N  N    A LYS   A 1 102 ? 21.635 1.277   -13.132 0.70 23.54 ?  102 LYS   A N    1 
ATOM   2154 N  N    B LYS   A 1 102 ? 21.556 0.664   -13.778 0.30 20.97 ?  102 LYS   A N    1 
ATOM   2155 C  CA   A LYS   A 1 102 ? 22.932 1.475   -13.772 0.70 24.97 ?  102 LYS   A CA   1 
ATOM   2156 C  CA   B LYS   A 1 102 ? 22.806 0.747   -14.517 0.30 21.85 ?  102 LYS   A CA   1 
ATOM   2157 C  C    A LYS   A 1 102 ? 23.267 0.387   -14.784 0.70 25.41 ?  102 LYS   A C    1 
ATOM   2158 C  C    B LYS   A 1 102 ? 23.084 -0.506  -15.341 0.30 21.22 ?  102 LYS   A C    1 
ATOM   2159 O  O    A LYS   A 1 102 ? 24.354 0.425   -15.368 0.70 25.73 ?  102 LYS   A O    1 
ATOM   2160 O  O    B LYS   A 1 102 ? 24.174 -0.629  -15.911 0.30 21.10 ?  102 LYS   A O    1 
ATOM   2161 C  CB   A LYS   A 1 102 ? 24.054 1.515   -12.726 0.70 25.83 ?  102 LYS   A CB   1 
ATOM   2162 C  CB   B LYS   A 1 102 ? 23.982 0.967   -13.564 0.30 23.47 ?  102 LYS   A CB   1 
ATOM   2163 C  CG   A LYS   A 1 102 ? 23.958 2.640   -11.722 0.70 26.69 ?  102 LYS   A CG   1 
ATOM   2164 C  CG   B LYS   A 1 102 ? 23.917 2.222   -12.714 0.30 25.06 ?  102 LYS   A CG   1 
ATOM   2165 C  CD   A LYS   A 1 102 ? 25.118 2.572   -10.740 0.70 27.82 ?  102 LYS   A CD   1 
ATOM   2166 C  CD   B LYS   A 1 102 ? 25.293 2.537   -12.142 0.30 26.26 ?  102 LYS   A CD   1 
ATOM   2167 C  CE   A LYS   A 1 102 ? 25.065 3.697   -9.721  0.70 28.60 ?  102 LYS   A CE   1 
ATOM   2168 C  CE   B LYS   A 1 102 ? 25.224 3.383   -10.882 0.30 27.38 ?  102 LYS   A CE   1 
ATOM   2169 N  NZ   A LYS   A 1 102 ? 26.152 3.573   -8.705  0.70 29.28 ?  102 LYS   A NZ   1 
ATOM   2170 N  NZ   B LYS   A 1 102 ? 25.397 2.555   -9.654  0.30 28.06 ?  102 LYS   A NZ   1 
ATOM   2171 H  H    A LYS   A 1 102 ? 21.624 0.584   -12.619 0.70 28.23 ?  102 LYS   A H    1 
ATOM   2172 H  H    B LYS   A 1 102 ? 21.649 0.384   -12.971 0.30 25.14 ?  102 LYS   A H    1 
ATOM   2173 H  HA   A LYS   A 1 102 ? 22.932 2.315   -14.244 0.70 29.94 ?  102 LYS   A HA   1 
ATOM   2174 H  HA   B LYS   A 1 102 ? 22.762 1.517   -15.103 0.30 26.20 ?  102 LYS   A HA   1 
ATOM   2175 H  HB2  A LYS   A 1 102 ? 24.045 0.679   -12.233 0.70 30.98 ?  102 LYS   A HB2  1 
ATOM   2176 H  HB2  B LYS   A 1 102 ? 24.029 0.209   -12.964 0.30 28.14 ?  102 LYS   A HB2  1 
ATOM   2177 H  HB3  A LYS   A 1 102 ? 24.903 1.605   -13.189 0.70 30.98 ?  102 LYS   A HB3  1 
ATOM   2178 H  HB3  B LYS   A 1 102 ? 24.794 1.017   -14.091 0.30 28.14 ?  102 LYS   A HB3  1 
ATOM   2179 H  HG2  A LYS   A 1 102 ? 23.994 3.490   -12.188 0.70 32.01 ?  102 LYS   A HG2  1 
ATOM   2180 H  HG2  B LYS   A 1 102 ? 23.635 2.970   -13.261 0.30 30.05 ?  102 LYS   A HG2  1 
ATOM   2181 H  HG3  A LYS   A 1 102 ? 23.127 2.559   -11.228 0.70 32.01 ?  102 LYS   A HG3  1 
ATOM   2182 H  HG3  B LYS   A 1 102 ? 23.294 2.091   -11.986 0.30 30.05 ?  102 LYS   A HG3  1 
ATOM   2183 H  HD2  A LYS   A 1 102 ? 25.083 1.728   -10.264 0.70 33.36 ?  102 LYS   A HD2  1 
ATOM   2184 H  HD2  B LYS   A 1 102 ? 25.741 1.705   -11.922 0.30 31.50 ?  102 LYS   A HD2  1 
ATOM   2185 H  HD3  A LYS   A 1 102 ? 25.953 2.644   -11.230 0.70 33.36 ?  102 LYS   A HD3  1 
ATOM   2186 H  HD3  B LYS   A 1 102 ? 25.805 3.025   -12.805 0.30 31.50 ?  102 LYS   A HD3  1 
ATOM   2187 H  HE2  A LYS   A 1 102 ? 25.170 4.546   -10.179 0.70 34.30 ?  102 LYS   A HE2  1 
ATOM   2188 H  HE2  B LYS   A 1 102 ? 25.934 4.045   -10.902 0.30 32.83 ?  102 LYS   A HE2  1 
ATOM   2189 H  HE3  A LYS   A 1 102 ? 24.211 3.669   -9.261  0.70 34.30 ?  102 LYS   A HE3  1 
ATOM   2190 H  HE3  B LYS   A 1 102 ? 24.360 3.820   -10.835 0.30 32.83 ?  102 LYS   A HE3  1 
ATOM   2191 H  HZ1  A LYS   A 1 102 ? 26.099 4.241   -8.121  0.70 35.11 ?  102 LYS   A HZ1  1 
ATOM   2192 H  HZ1  B LYS   A 1 102 ? 25.024 2.962   -8.955  0.30 33.66 ?  102 LYS   A HZ1  1 
ATOM   2193 H  HZ2  A LYS   A 1 102 ? 26.073 2.800   -8.270  0.70 35.11 ?  102 LYS   A HZ2  1 
ATOM   2194 H  HZ2  B LYS   A 1 102 ? 25.010 1.760   -9.766  0.30 33.66 ?  102 LYS   A HZ2  1 
ATOM   2195 H  HZ3  A LYS   A 1 102 ? 26.946 3.599   -9.106  0.70 35.11 ?  102 LYS   A HZ3  1 
ATOM   2196 H  HZ3  B LYS   A 1 102 ? 26.262 2.430   -9.490  0.30 33.66 ?  102 LYS   A HZ3  1 
ATOM   2197 N  N    A GLY   A 1 103 ? 22.387 -0.592  -14.988 0.70 26.26 ?  103 GLY   A N    1 
ATOM   2198 N  N    B GLY   A 1 103 ? 22.148 -1.452  -15.384 0.30 21.02 ?  103 GLY   A N    1 
ATOM   2199 C  CA   A GLY   A 1 103 ? 22.655 -1.668  -15.925 0.70 26.47 ?  103 GLY   A CA   1 
ATOM   2200 C  CA   B GLY   A 1 103 ? 22.350 -2.659  -16.160 0.30 20.55 ?  103 GLY   A CA   1 
ATOM   2201 C  C    A GLY   A 1 103 ? 23.513 -2.788  -15.387 0.70 27.18 ?  103 GLY   A C    1 
ATOM   2202 C  C    B GLY   A 1 103 ? 23.320 -3.649  -15.557 0.30 19.91 ?  103 GLY   A C    1 
ATOM   2203 O  O    A GLY   A 1 103 ? 24.123 -3.516  -16.176 0.70 28.12 ?  103 GLY   A O    1 
ATOM   2204 O  O    B GLY   A 1 103 ? 23.800 -4.539  -16.263 0.30 19.77 ?  103 GLY   A O    1 
ATOM   2205 H  H    A GLY   A 1 103 ? 21.633 -0.665  -14.590 0.70 31.49 ?  103 GLY   A H    1 
ATOM   2206 H  H    B GLY   A 1 103 ? 21.395 -1.419  -14.967 0.30 25.20 ?  103 GLY   A H    1 
ATOM   2207 H  HA2  A GLY   A 1 103 ? 21.809 -2.044  -16.231 0.70 31.75 ?  103 GLY   A HA2  1 
ATOM   2208 H  HA2  B GLY   A 1 103 ? 21.495 -3.100  -16.280 0.30 24.65 ?  103 GLY   A HA2  1 
ATOM   2209 H  HA3  A GLY   A 1 103 ? 23.117 -1.313  -16.699 0.70 31.75 ?  103 GLY   A HA3  1 
ATOM   2210 H  HA3  B GLY   A 1 103 ? 22.685 -2.414  -17.037 0.30 24.65 ?  103 GLY   A HA3  1 
ATOM   2211 N  N    A GLU   A 1 104 ? 23.583 -2.957  -14.070 0.70 26.12 ?  104 GLU   A N    1 
ATOM   2212 N  N    B GLU   A 1 104 ? 23.630 -3.519  -14.269 0.30 19.46 ?  104 GLU   A N    1 
ATOM   2213 C  CA   A GLU   A 1 104 ? 24.444 -3.963  -13.467 0.70 25.08 ?  104 GLU   A CA   1 
ATOM   2214 C  CA   B GLU   A 1 104 ? 24.567 -4.433  -13.631 0.30 18.94 ?  104 GLU   A CA   1 
ATOM   2215 C  C    A GLU   A 1 104 ? 23.744 -5.319  -13.387 0.70 25.17 ?  104 GLU   A C    1 
ATOM   2216 C  C    B GLU   A 1 104 ? 23.914 -5.797  -13.416 0.30 18.68 ?  104 GLU   A C    1 
ATOM   2217 O  O    A GLU   A 1 104 ? 22.515 -5.407  -13.300 0.70 25.70 ?  104 GLU   A O    1 
ATOM   2218 O  O    B GLU   A 1 104 ? 22.723 -5.895  -13.101 0.30 18.72 ?  104 GLU   A O    1 
ATOM   2219 C  CB   A GLU   A 1 104 ? 24.930 -3.480  -12.095 0.70 23.15 ?  104 GLU   A CB   1 
ATOM   2220 C  CB   B GLU   A 1 104 ? 25.058 -3.833  -12.311 0.30 19.11 ?  104 GLU   A CB   1 
ATOM   2221 C  CG   A GLU   A 1 104 ? 25.895 -2.289  -12.237 0.70 22.38 ?  104 GLU   A CG   1 
ATOM   2222 C  CG   B GLU   A 1 104 ? 25.710 -2.459  -12.496 0.30 19.82 ?  104 GLU   A CG   1 
ATOM   2223 C  CD   A GLU   A 1 104 ? 26.183 -1.510  -10.956 0.70 21.00 ?  104 GLU   A CD   1 
ATOM   2224 C  CD   B GLU   A 1 104 ? 26.208 -1.835  -11.204 0.30 20.03 ?  104 GLU   A CD   1 
ATOM   2225 O  OE1  A GLU   A 1 104 ? 25.592 -1.804  -9.896  0.70 19.01 ?  104 GLU   A OE1  1 
ATOM   2226 O  OE1  B GLU   A 1 104 ? 25.765 -2.254  -10.116 0.30 20.24 ?  104 GLU   A OE1  1 
ATOM   2227 O  OE2  A GLU   A 1 104 ? 27.015 -0.572  -11.035 0.70 21.59 -1 104 GLU   A OE2  1 
ATOM   2228 O  OE2  B GLU   A 1 104 ? 27.047 -0.911  -11.285 0.30 20.06 -1 104 GLU   A OE2  1 
ATOM   2229 H  H    A GLU   A 1 104 ? 23.139 -2.493  -13.499 0.70 31.33 ?  104 GLU   A H    1 
ATOM   2230 H  H    B GLU   A 1 104 ? 23.317 -2.907  -13.749 0.30 23.33 ?  104 GLU   A H    1 
ATOM   2231 H  HA   A GLU   A 1 104 ? 25.220 -4.080  -14.032 0.70 30.08 ?  104 GLU   A HA   1 
ATOM   2232 H  HA   B GLU   A 1 104 ? 25.336 -4.550  -14.211 0.30 22.70 ?  104 GLU   A HA   1 
ATOM   2233 H  HB2  A GLU   A 1 104 ? 24.165 -3.200  -11.570 0.70 27.76 ?  104 GLU   A HB2  1 
ATOM   2234 H  HB2  B GLU   A 1 104 ? 24.306 -3.726  -11.710 0.30 22.91 ?  104 GLU   A HB2  1 
ATOM   2235 H  HB3  A GLU   A 1 104 ? 25.397 -4.205  -11.651 0.70 27.76 ?  104 GLU   A HB3  1 
ATOM   2236 H  HB3  B GLU   A 1 104 ? 25.719 -4.424  -11.921 0.30 22.91 ?  104 GLU   A HB3  1 
ATOM   2237 H  HG2  A GLU   A 1 104 ? 26.740 -2.622  -12.567 0.70 26.84 ?  104 GLU   A HG2  1 
ATOM   2238 H  HG2  B GLU   A 1 104 ? 26.472 -2.548  -13.089 0.30 23.76 ?  104 GLU   A HG2  1 
ATOM   2239 H  HG3  A GLU   A 1 104 ? 25.514 -1.667  -12.876 0.70 26.84 ?  104 GLU   A HG3  1 
ATOM   2240 H  HG3  B GLU   A 1 104 ? 25.061 -1.851  -12.885 0.30 23.76 ?  104 GLU   A HG3  1 
ATOM   2241 N  N    A ASP   A 1 105 ? 24.552 -6.380  -13.425 0.70 25.89 ?  105 ASP   A N    1 
ATOM   2242 N  N    B ASP   A 1 105 ? 24.708 -6.853  -13.597 0.30 18.97 ?  105 ASP   A N    1 
ATOM   2243 C  CA   A ASP   A 1 105 ? 24.054 -7.743  -13.578 0.70 27.15 ?  105 ASP   A CA   1 
ATOM   2244 C  CA   B ASP   A 1 105 ? 24.196 -8.222  -13.630 0.30 19.86 ?  105 ASP   A CA   1 
ATOM   2245 C  C    A ASP   A 1 105 ? 23.347 -8.199  -12.307 0.70 24.85 ?  105 ASP   A C    1 
ATOM   2246 C  C    B ASP   A 1 105 ? 23.512 -8.594  -12.319 0.30 19.00 ?  105 ASP   A C    1 
ATOM   2247 O  O    A ASP   A 1 105 ? 23.973 -8.307  -11.249 0.70 23.23 ?  105 ASP   A O    1 
ATOM   2248 O  O    B ASP   A 1 105 ? 24.130 -8.559  -11.251 0.30 17.98 ?  105 ASP   A O    1 
ATOM   2249 C  CB   A ASP   A 1 105 ? 25.231 -8.667  -13.887 0.70 30.39 ?  105 ASP   A CB   1 
ATOM   2250 C  CB   B ASP   A 1 105 ? 25.362 -9.171  -13.903 0.30 21.60 ?  105 ASP   A CB   1 
ATOM   2251 C  CG   A ASP   A 1 105 ? 24.797 -10.078 -14.207 0.70 33.13 ?  105 ASP   A CG   1 
ATOM   2252 C  CG   B ASP   A 1 105 ? 24.966 -10.635 -13.835 0.30 22.89 ?  105 ASP   A CG   1 
ATOM   2253 O  OD1  A ASP   A 1 105 ? 23.575 -10.318 -14.295 0.70 33.62 ?  105 ASP   A OD1  1 
ATOM   2254 O  OD1  B ASP   A 1 105 ? 23.759 -10.942 -13.921 0.30 23.41 ?  105 ASP   A OD1  1 
ATOM   2255 O  OD2  A ASP   A 1 105 ? 25.683 -10.945 -14.378 0.70 34.59 -1 105 ASP   A OD2  1 
ATOM   2256 O  OD2  B ASP   A 1 105 ? 25.877 -11.481 -13.689 0.30 23.84 -1 105 ASP   A OD2  1 
ATOM   2257 H  H    A ASP   A 1 105 ? 25.409 -6.339  -13.362 0.70 31.05 ?  105 ASP   A H    1 
ATOM   2258 H  H    B ASP   A 1 105 ? 25.558 -6.793  -13.716 0.30 22.74 ?  105 ASP   A H    1 
ATOM   2259 H  HA   A ASP   A 1 105 ? 23.428 -7.794  -14.315 0.70 32.56 ?  105 ASP   A HA   1 
ATOM   2260 H  HA   B ASP   A 1 105 ? 23.549 -8.301  -14.349 0.30 23.81 ?  105 ASP   A HA   1 
ATOM   2261 H  HB2  A ASP   A 1 105 ? 25.708 -8.333  -14.663 0.70 36.45 ?  105 ASP   A HB2  1 
ATOM   2262 H  HB2  B ASP   A 1 105 ? 25.713 -8.983  -14.787 0.30 25.90 ?  105 ASP   A HB2  1 
ATOM   2263 H  HB3  A ASP   A 1 105 ? 25.830 -8.696  -13.121 0.70 36.45 ?  105 ASP   A HB3  1 
ATOM   2264 H  HB3  B ASP   A 1 105 ? 26.043 -9.026  -13.234 0.30 25.90 ?  105 ASP   A HB3  1 
ATOM   2265 N  N    A ILE   A 1 106 ? 22.051 -8.505  -12.419 0.70 24.70 ?  106 ILE   A N    1 
ATOM   2266 N  N    B ILE   A 1 106 ? 22.239 -8.988  -12.411 0.30 19.27 ?  106 ILE   A N    1 
ATOM   2267 C  CA   A ILE   A 1 106 ? 21.278 -8.918  -11.250 0.70 23.74 ?  106 ILE   A CA   1 
ATOM   2268 C  CA   B ILE   A 1 106 ? 21.471 -9.317  -11.216 0.30 19.72 ?  106 ILE   A CA   1 
ATOM   2269 C  C    A ILE   A 1 106 ? 21.821 -10.214 -10.669 0.70 22.80 ?  106 ILE   A C    1 
ATOM   2270 C  C    B ILE   A 1 106 ? 22.009 -10.557 -10.512 0.30 19.23 ?  106 ILE   A C    1 
ATOM   2271 O  O    A ILE   A 1 106 ? 21.643 -10.488 -9.477  0.70 22.27 ?  106 ILE   A O    1 
ATOM   2272 O  O    B ILE   A 1 106 ? 21.743 -10.747 -9.320  0.30 19.53 ?  106 ILE   A O    1 
ATOM   2273 C  CB   A ILE   A 1 106 ? 19.775 -9.017  -11.589 0.70 25.37 ?  106 ILE   A CB   1 
ATOM   2274 C  CB   B ILE   A 1 106 ? 19.970 -9.437  -11.554 0.30 20.85 ?  106 ILE   A CB   1 
ATOM   2275 C  CG1  A ILE   A 1 106 ? 18.937 -9.138  -10.313 0.70 25.72 ?  106 ILE   A CG1  1 
ATOM   2276 C  CG1  B ILE   A 1 106 ? 19.118 -9.358  -10.284 0.30 21.75 ?  106 ILE   A CG1  1 
ATOM   2277 C  CG2  A ILE   A 1 106 ? 19.508 -10.216 -12.480 0.70 25.93 ?  106 ILE   A CG2  1 
ATOM   2278 C  CG2  B ILE   A 1 106 ? 19.685 -10.733 -12.298 0.30 21.03 ?  106 ILE   A CG2  1 
ATOM   2279 C  CD1  A ILE   A 1 106 ? 19.074 -7.964  -9.373  0.70 26.25 ?  106 ILE   A CD1  1 
ATOM   2280 C  CD1  B ILE   A 1 106 ? 19.289 -8.064  -9.512  0.30 22.27 ?  106 ILE   A CD1  1 
ATOM   2281 H  H    A ILE   A 1 106 ? 21.607 -8.487  -13.152 0.70 29.61 ?  106 ILE   A H    1 
ATOM   2282 H  H    B ILE   A 1 106 ? 21.807 -9.068  -13.147 0.30 23.11 ?  106 ILE   A H    1 
ATOM   2283 H  HA   A ILE   A 1 106 ? 21.382 -8.243  -10.573 0.70 28.47 ?  106 ILE   A HA   1 
ATOM   2284 H  HA   B ILE   A 1 106 ? 21.572 -8.586  -10.595 0.30 23.65 ?  106 ILE   A HA   1 
ATOM   2285 H  HB   A ILE   A 1 106 ? 19.509 -8.213  -12.063 0.70 30.42 ?  106 ILE   A HB   1 
ATOM   2286 H  HB   B ILE   A 1 106 ? 19.726 -8.695  -12.129 0.30 25.00 ?  106 ILE   A HB   1 
ATOM   2287 H  HG12 A ILE   A 1 106 ? 18.001 -9.209  -10.559 0.70 30.85 ?  106 ILE   A HG12 1 
ATOM   2288 H  HG12 B ILE   A 1 106 ? 18.181 -9.430  -10.529 0.30 26.08 ?  106 ILE   A HG12 1 
ATOM   2289 H  HG13 A ILE   A 1 106 ? 19.209 -9.935  -9.832  0.70 30.85 ?  106 ILE   A HG13 1 
ATOM   2290 H  HG13 B ILE   A 1 106 ? 19.360 -10.088 -9.695  0.30 26.08 ?  106 ILE   A HG13 1 
ATOM   2291 H  HG21 A ILE   A 1 106 ? 18.622 -10.132 -12.863 0.70 31.09 ?  106 ILE   A HG21 1 
ATOM   2292 H  HG21 B ILE   A 1 106 ? 18.796 -10.685 -12.685 0.30 25.21 ?  106 ILE   A HG21 1 
ATOM   2293 H  HG22 A ILE   A 1 106 ? 20.175 -10.237 -13.183 0.70 31.09 ?  106 ILE   A HG22 1 
ATOM   2294 H  HG22 B ILE   A 1 106 ? 20.345 -10.843 -12.999 0.30 25.21 ?  106 ILE   A HG22 1 
ATOM   2295 H  HG23 A ILE   A 1 106 ? 19.565 -11.024 -11.946 0.70 31.09 ?  106 ILE   A HG23 1 
ATOM   2296 H  HG23 B ILE   A 1 106 ? 19.735 -11.474 -11.676 0.30 25.21 ?  106 ILE   A HG23 1 
ATOM   2297 H  HD11 A ILE   A 1 106 ? 18.341 -7.981  -8.740  0.70 31.48 ?  106 ILE   A HD11 1 
ATOM   2298 H  HD11 B ILE   A 1 106 ? 18.529 -7.945  -8.925  0.30 26.70 ?  106 ILE   A HD11 1 
ATOM   2299 H  HD12 A ILE   A 1 106 ? 19.920 -8.032  -8.902  0.70 31.48 ?  106 ILE   A HD12 1 
ATOM   2300 H  HD12 B ILE   A 1 106 ? 20.106 -8.114  -8.990  0.30 26.70 ?  106 ILE   A HD12 1 
ATOM   2301 H  HD13 A ILE   A 1 106 ? 19.046 -7.143  -9.890  0.70 31.48 ?  106 ILE   A HD13 1 
ATOM   2302 H  HD13 B ILE   A 1 106 ? 19.341 -7.327  -10.141 0.30 26.70 ?  106 ILE   A HD13 1 
ATOM   2303 N  N    A GLN   A 1 107 ? 22.494 -11.029 -11.491 0.70 23.28 ?  107 GLN   A N    1 
ATOM   2304 N  N    B GLN   A 1 107 ? 22.770 -11.405 -11.212 0.30 19.02 ?  107 GLN   A N    1 
ATOM   2305 C  CA   A GLN   A 1 107 ? 23.121 -12.248 -10.991 0.70 25.21 ?  107 GLN   A CA   1 
ATOM   2306 C  CA   B GLN   A 1 107 ? 23.367 -12.568 -10.562 0.30 19.82 ?  107 GLN   A CA   1 
ATOM   2307 C  C    A GLN   A 1 107 ? 24.119 -11.955 -9.883  0.70 22.49 ?  107 GLN   A C    1 
ATOM   2308 C  C    B GLN   A 1 107 ? 24.333 -12.168 -9.451  0.30 17.43 ?  107 GLN   A C    1 
ATOM   2309 O  O    A GLN   A 1 107 ? 24.381 -12.826 -9.048  0.70 24.54 ?  107 GLN   A O    1 
ATOM   2310 O  O    B GLN   A 1 107 ? 24.563 -12.953 -8.523  0.30 16.51 ?  107 GLN   A O    1 
ATOM   2311 C  CB   A GLN   A 1 107 ? 23.832 -12.985 -12.132 0.70 29.19 ?  107 GLN   A CB   1 
ATOM   2312 C  CB   B GLN   A 1 107 ? 24.057 -13.451 -11.608 0.30 23.00 ?  107 GLN   A CB   1 
ATOM   2313 C  CG   A GLN   A 1 107 ? 22.952 -13.281 -13.337 0.70 33.32 ?  107 GLN   A CG   1 
ATOM   2314 C  CG   B GLN   A 1 107 ? 23.123 -13.925 -12.717 0.30 26.10 ?  107 GLN   A CG   1 
ATOM   2315 C  CD   A GLN   A 1 107 ? 21.716 -14.075 -12.974 0.70 36.61 ?  107 GLN   A CD   1 
ATOM   2316 C  CD   B GLN   A 1 107 ? 21.952 -14.729 -12.188 0.30 28.76 ?  107 GLN   A CD   1 
ATOM   2317 O  OE1  A GLN   A 1 107 ? 21.802 -15.126 -12.338 0.70 38.46 ?  107 GLN   A OE1  1 
ATOM   2318 O  OE1  B GLN   A 1 107 ? 22.103 -15.538 -11.271 0.30 29.74 ?  107 GLN   A OE1  1 
ATOM   2319 N  NE2  A GLN   A 1 107 ? 20.555 -13.572 -13.373 0.70 38.20 ?  107 GLN   A NE2  1 
ATOM   2320 N  NE2  B GLN   A 1 107 ? 20.772 -14.506 -12.760 0.30 29.55 ?  107 GLN   A NE2  1 
ATOM   2321 H  H    A GLN   A 1 107 ? 22.595 -10.899 -12.332 0.70 27.91 ?  107 GLN   A H    1 
ATOM   2322 H  H    B GLN   A 1 107 ? 22.951 -11.329 -12.052 0.30 22.80 ?  107 GLN   A H    1 
ATOM   2323 H  HA   A GLN   A 1 107 ? 22.440 -12.842 -10.636 0.70 30.24 ?  107 GLN   A HA   1 
ATOM   2324 H  HA   B GLN   A 1 107 ? 22.661 -13.094 -10.166 0.30 23.77 ?  107 GLN   A HA   1 
ATOM   2325 H  HB2  A GLN   A 1 107 ? 24.574 -12.442 -12.441 0.70 35.01 ?  107 GLN   A HB2  1 
ATOM   2326 H  HB2  B GLN   A 1 107 ? 24.775 -12.952 -12.024 0.30 27.57 ?  107 GLN   A HB2  1 
ATOM   2327 H  HB3  A GLN   A 1 107 ? 24.165 -13.834 -11.800 0.70 35.01 ?  107 GLN   A HB3  1 
ATOM   2328 H  HB3  B GLN   A 1 107 ? 24.413 -14.241 -11.170 0.30 27.57 ?  107 GLN   A HB3  1 
ATOM   2329 H  HG2  A GLN   A 1 107 ? 22.665 -12.446 -13.735 0.70 39.96 ?  107 GLN   A HG2  1 
ATOM   2330 H  HG2  B GLN   A 1 107 ? 22.770 -13.152 -13.187 0.30 31.30 ?  107 GLN   A HG2  1 
ATOM   2331 H  HG3  A GLN   A 1 107 ? 23.463 -13.797 -13.981 0.70 39.96 ?  107 GLN   A HG3  1 
ATOM   2332 H  HG3  B GLN   A 1 107 ? 23.619 -14.488 -13.332 0.30 31.30 ?  107 GLN   A HG3  1 
ATOM   2333 H  HE21 A GLN   A 1 107 ? 20.535 -12.836 -13.815 0.70 45.82 ?  107 GLN   A HE21 1 
ATOM   2334 H  HE21 B GLN   A 1 107 ? 20.705 -13.931 -13.397 0.30 35.44 ?  107 GLN   A HE21 1 
ATOM   2335 H  HE22 A GLN   A 1 107 ? 19.824 -13.986 -13.190 0.70 45.82 ?  107 GLN   A HE22 1 
ATOM   2336 H  HE22 B GLN   A 1 107 ? 20.075 -14.935 -12.495 0.30 35.44 ?  107 GLN   A HE22 1 
ATOM   2337 N  N    A LEU   A 1 108 ? 24.668 -10.740 -9.843  0.70 18.34 ?  108 LEU   A N    1 
ATOM   2338 N  N    B LEU   A 1 108 ? 24.879 -10.951 -9.509  0.30 16.10 ?  108 LEU   A N    1 
ATOM   2339 C  CA   A LEU   A 1 108 ? 25.599 -10.379 -8.784  0.70 15.54 ?  108 LEU   A CA   1 
ATOM   2340 C  CA   B LEU   A 1 108 ? 25.779 -10.455 -8.475  0.30 15.37 ?  108 LEU   A CA   1 
ATOM   2341 C  C    A LEU   A 1 108 ? 24.913 -10.241 -7.435  0.70 13.54 ?  108 LEU   A C    1 
ATOM   2342 C  C    B LEU   A 1 108 ? 25.075 -10.220 -7.143  0.30 14.29 ?  108 LEU   A C    1 
ATOM   2343 O  O    A LEU   A 1 108 ? 25.601 -10.080 -6.424  0.70 13.70 ?  108 LEU   A O    1 
ATOM   2344 O  O    B LEU   A 1 108 ? 25.754 -10.031 -6.129  0.30 14.82 ?  108 LEU   A O    1 
ATOM   2345 C  CB   A LEU   A 1 108 ? 26.350 -9.094  -9.145  0.70 15.59 ?  108 LEU   A CB   1 
ATOM   2346 C  CB   B LEU   A 1 108 ? 26.457 -9.167  -8.956  0.30 15.73 ?  108 LEU   A CB   1 
ATOM   2347 C  CG   A LEU   A 1 108 ? 27.369 -9.296  -10.269 0.70 17.62 ?  108 LEU   A CG   1 
ATOM   2348 C  CG   B LEU   A 1 108 ? 27.391 -9.328  -10.160 0.30 16.90 ?  108 LEU   A CG   1 
ATOM   2349 C  CD1  A LEU   A 1 108 ? 27.881 -7.969  -10.798 0.70 18.28 ?  108 LEU   A CD1  1 
ATOM   2350 C  CD1  B LEU   A 1 108 ? 27.781 -7.975  -10.742 0.30 17.19 ?  108 LEU   A CD1  1 
ATOM   2351 C  CD2  A LEU   A 1 108 ? 28.534 -10.158 -9.796  0.70 19.55 ?  108 LEU   A CD2  1 
ATOM   2352 C  CD2  B LEU   A 1 108 ? 28.633 -10.112 -9.766  0.30 17.75 ?  108 LEU   A CD2  1 
ATOM   2353 H  H    A LEU   A 1 108 ? 24.512 -10.121 -10.414 0.70 21.99 ?  108 LEU   A H    1 
ATOM   2354 H  H    B LEU   A 1 108 ? 24.737 -10.395 -10.143 0.30 19.30 ?  108 LEU   A H    1 
ATOM   2355 H  HA   A LEU   A 1 108 ? 26.246 -11.089 -8.696  0.70 18.63 ?  108 LEU   A HA   1 
ATOM   2356 H  HA   B LEU   A 1 108 ? 26.474 -11.115 -8.326  0.30 18.43 ?  108 LEU   A HA   1 
ATOM   2357 H  HB2  A LEU   A 1 108 ? 25.710 -8.426  -9.440  0.70 18.68 ?  108 LEU   A HB2  1 
ATOM   2358 H  HB2  B LEU   A 1 108 ? 25.770 -8.532  -9.208  0.30 18.86 ?  108 LEU   A HB2  1 
ATOM   2359 H  HB3  A LEU   A 1 108 ? 26.823 -8.778  -8.362  0.70 18.68 ?  108 LEU   A HB3  1 
ATOM   2360 H  HB3  B LEU   A 1 108 ? 26.984 -8.806  -8.228  0.30 18.86 ?  108 LEU   A HB3  1 
ATOM   2361 H  HG   A LEU   A 1 108 ? 26.938 -9.764  -11.002 0.70 21.12 ?  108 LEU   A HG   1 
ATOM   2362 H  HG   B LEU   A 1 108 ? 26.932 -9.827  -10.854 0.30 20.26 ?  108 LEU   A HG   1 
ATOM   2363 H  HD11 A LEU   A 1 108 ? 28.509 -8.138  -11.521 0.70 21.91 ?  108 LEU   A HD11 1 
ATOM   2364 H  HD11 B LEU   A 1 108 ? 28.339 -8.115  -11.525 0.30 20.60 ?  108 LEU   A HD11 1 
ATOM   2365 H  HD12 A LEU   A 1 108 ? 27.132 -7.449  -11.126 0.70 21.91 ?  108 LEU   A HD12 1 
ATOM   2366 H  HD12 B LEU   A 1 108 ? 26.977 -7.495  -10.992 0.30 20.60 ?  108 LEU   A HD12 1 
ATOM   2367 H  HD13 A LEU   A 1 108 ? 28.327 -7.493  -10.080 0.70 21.91 ?  108 LEU   A HD13 1 
ATOM   2368 H  HD13 B LEU   A 1 108 ? 28.272 -7.472  -10.073 0.30 20.60 ?  108 LEU   A HD13 1 
ATOM   2369 H  HD21 A LEU   A 1 108 ? 29.247 -10.107 -10.448 0.70 23.43 ?  108 LEU   A HD21 1 
ATOM   2370 H  HD21 B LEU   A 1 108 ? 29.256 -10.111 -10.509 0.30 21.28 ?  108 LEU   A HD21 1 
ATOM   2371 H  HD22 A LEU   A 1 108 ? 28.842 -9.825  -8.939  0.70 23.43 ?  108 LEU   A HD22 1 
ATOM   2372 H  HD22 B LEU   A 1 108 ? 29.038 -9.689  -8.993  0.30 21.28 ?  108 LEU   A HD22 1 
ATOM   2373 H  HD23 A LEU   A 1 108 ? 28.232 -11.076 -9.704  0.70 23.43 ?  108 LEU   A HD23 1 
ATOM   2374 H  HD23 B LEU   A 1 108 ? 28.375 -11.021 -9.550  0.30 21.28 ?  108 LEU   A HD23 1 
ATOM   2375 N  N    A LEU   A 1 109 ? 23.581 -10.323 -7.390  0.70 13.14 ?  109 LEU   A N    1 
ATOM   2376 N  N    B LEU   A 1 109 ? 23.739 -10.232 -7.116  0.30 13.10 ?  109 LEU   A N    1 
ATOM   2377 C  CA   A LEU   A 1 109 ? 22.887 -10.209 -6.114  0.70 12.44 ?  109 LEU   A CA   1 
ATOM   2378 C  CA   B LEU   A 1 109 ? 23.022 -10.074 -5.855  0.30 12.11 ?  109 LEU   A CA   1 
ATOM   2379 C  C    A LEU   A 1 109 ? 23.271 -11.343 -5.169  0.70 12.05 ?  109 LEU   A C    1 
ATOM   2380 C  C    B LEU   A 1 109 ? 23.263 -11.258 -4.926  0.30 11.70 ?  109 LEU   A C    1 
ATOM   2381 O  O    A LEU   A 1 109 ? 23.458 -11.122 -3.969  0.70 12.47 ?  109 LEU   A O    1 
ATOM   2382 O  O    B LEU   A 1 109 ? 23.287 -11.089 -3.702  0.30 11.71 ?  109 LEU   A O    1 
ATOM   2383 C  CB   A LEU   A 1 109 ? 21.377 -10.168 -6.349  0.70 13.10 ?  109 LEU   A CB   1 
ATOM   2384 C  CB   B LEU   A 1 109 ? 21.527 -9.890  -6.128  0.30 11.77 ?  109 LEU   A CB   1 
ATOM   2385 C  CG   A LEU   A 1 109 ? 20.492 -9.869  -5.140  0.70 13.73 ?  109 LEU   A CG   1 
ATOM   2386 C  CG   B LEU   A 1 109 ? 20.596 -9.611  -4.941  0.30 11.39 ?  109 LEU   A CG   1 
ATOM   2387 C  CD1  A LEU   A 1 109 ? 20.886 -8.549  -4.481  0.70 13.84 ?  109 LEU   A CD1  1 
ATOM   2388 C  CD1  B LEU   A 1 109 ? 21.088 -8.425  -4.133  0.30 11.33 ?  109 LEU   A CD1  1 
ATOM   2389 C  CD2  A LEU   A 1 109 ? 19.030 -9.838  -5.559  0.70 14.86 ?  109 LEU   A CD2  1 
ATOM   2390 C  CD2  B LEU   A 1 109 ? 19.158 -9.373  -5.412  0.30 10.98 ?  109 LEU   A CD2  1 
ATOM   2391 H  H    A LEU   A 1 109 ? 23.059 -10.444 -8.069  0.70 15.75 ?  109 LEU   A H    1 
ATOM   2392 H  H    B LEU   A 1 109 ? 23.237 -10.329 -7.803  0.30 15.70 ?  109 LEU   A H    1 
ATOM   2393 H  HA   A LEU   A 1 109 ? 23.144 -9.376  -5.694  0.70 14.90 ?  109 LEU   A HA   1 
ATOM   2394 H  HA   B LEU   A 1 109 ? 23.347 -9.277  -5.409  0.30 14.51 ?  109 LEU   A HA   1 
ATOM   2395 H  HB2  A LEU   A 1 109 ? 21.192 -9.485  -7.011  0.70 15.70 ?  109 LEU   A HB2  1 
ATOM   2396 H  HB2  B LEU   A 1 109 ? 21.430 -9.146  -6.739  0.30 14.11 ?  109 LEU   A HB2  1 
ATOM   2397 H  HB3  A LEU   A 1 109 ? 21.098 -11.030 -6.692  0.70 15.70 ?  109 LEU   A HB3  1 
ATOM   2398 H  HB3  B LEU   A 1 109 ? 21.203 -10.696 -6.553  0.30 14.11 ?  109 LEU   A HB3  1 
ATOM   2399 H  HG   A LEU   A 1 109 ? 20.600 -10.569 -4.483  0.70 16.46 ?  109 LEU   A HG   1 
ATOM   2400 H  HG   B LEU   A 1 109 ? 20.588 -10.383 -4.358  0.30 13.65 ?  109 LEU   A HG   1 
ATOM   2401 H  HD11 A LEU   A 1 109 ? 20.222 -8.314  -3.811  0.70 16.59 ?  109 LEU   A HD11 1 
ATOM   2402 H  HD11 B LEU   A 1 109 ? 20.425 -8.201  -3.461  0.30 13.57 ?  109 LEU   A HD11 1 
ATOM   2403 H  HD12 A LEU   A 1 109 ? 21.754 -8.645  -4.063  0.70 16.59 ?  109 LEU   A HD12 1 
ATOM   2404 H  HD12 B LEU   A 1 109 ? 21.926 -8.658  -3.707  0.30 13.57 ?  109 LEU   A HD12 1 
ATOM   2405 H  HD13 A LEU   A 1 109 ? 20.922 -7.851  -5.160  0.70 16.59 ?  109 LEU   A HD13 1 
ATOM   2406 H  HD13 B LEU   A 1 109 ? 21.219 -7.668  -4.730  0.30 13.57 ?  109 LEU   A HD13 1 
ATOM   2407 H  HD21 A LEU   A 1 109 ? 18.497 -9.472  -4.835  0.70 17.81 ?  109 LEU   A HD21 1 
ATOM   2408 H  HD21 B LEU   A 1 109 ? 18.598 -9.181  -4.641  0.30 13.15 ?  109 LEU   A HD21 1 
ATOM   2409 H  HD22 A LEU   A 1 109 ? 18.935 -9.288  -6.351  0.70 17.81 ?  109 LEU   A HD22 1 
ATOM   2410 H  HD22 B LEU   A 1 109 ? 19.142 -8.621  -6.025  0.30 13.15 ?  109 LEU   A HD22 1 
ATOM   2411 H  HD23 A LEU   A 1 109 ? 18.739 -10.747 -5.754  0.70 17.81 ?  109 LEU   A HD23 1 
ATOM   2412 H  HD23 B LEU   A 1 109 ? 18.834 -10.171 -5.861  0.30 13.15 ?  109 LEU   A HD23 1 
ATOM   2413 N  N    A LYS   A 1 110 ? 23.402 -12.566 -5.685  0.70 11.81 ?  110 LYS   A N    1 
ATOM   2414 N  N    B LYS   A 1 110 ? 23.439 -12.458 -5.480  0.30 11.88 ?  110 LYS   A N    1 
ATOM   2415 C  CA   A LYS   A 1 110 ? 23.783 -13.671 -4.812  0.70 11.70 ?  110 LYS   A CA   1 
ATOM   2416 C  CA   B LYS   A 1 110 ? 23.812 -13.595 -4.646  0.30 12.08 ?  110 LYS   A CA   1 
ATOM   2417 C  C    A LYS   A 1 110 ? 25.159 -13.430 -4.201  0.70 11.36 ?  110 LYS   A C    1 
ATOM   2418 C  C    B LYS   A 1 110 ? 25.210 -13.406 -4.068  0.30 11.94 ?  110 LYS   A C    1 
ATOM   2419 O  O    A LYS   A 1 110 ? 25.352 -13.594 -2.993  0.70 11.68 ?  110 LYS   A O    1 
ATOM   2420 O  O    B LYS   A 1 110 ? 25.444 -13.692 -2.889  0.30 12.23 ?  110 LYS   A O    1 
ATOM   2421 C  CB   A LYS   A 1 110 ? 23.732 -15.007 -5.556  0.70 12.54 ?  110 LYS   A CB   1 
ATOM   2422 C  CB   B LYS   A 1 110 ? 23.712 -14.894 -5.449  0.30 12.65 ?  110 LYS   A CB   1 
ATOM   2423 C  CG   A LYS   A 1 110 ? 23.922 -16.197 -4.618  0.70 13.43 ?  110 LYS   A CG   1 
ATOM   2424 C  CG   B LYS   A 1 110 ? 23.895 -16.154 -4.611  0.30 13.17 ?  110 LYS   A CG   1 
ATOM   2425 C  CD   A LYS   A 1 110 ? 23.677 -17.541 -5.294  0.70 13.79 ?  110 LYS   A CD   1 
ATOM   2426 C  CD   B LYS   A 1 110 ? 23.710 -17.419 -5.439  0.30 13.50 ?  110 LYS   A CD   1 
ATOM   2427 C  CE   A LYS   A 1 110 ? 23.805 -18.696 -4.306  0.70 14.84 ?  110 LYS   A CE   1 
ATOM   2428 C  CE   B LYS   A 1 110 ? 23.762 -18.667 -4.570  0.30 14.14 ?  110 LYS   A CE   1 
ATOM   2429 N  NZ   A LYS   A 1 110 ? 22.631 -18.825 -3.402  0.70 15.15 ?  110 LYS   A NZ   1 
ATOM   2430 N  NZ   B LYS   A 1 110 ? 22.595 -18.770 -3.651  0.30 14.47 ?  110 LYS   A NZ   1 
ATOM   2431 H  H    A LYS   A 1 110 ? 23.275 -12.779 -6.508  0.70 14.16 ?  110 LYS   A H    1 
ATOM   2432 H  H    B LYS   A 1 110 ? 23.349 -12.636 -6.314  0.30 14.24 ?  110 LYS   A H    1 
ATOM   2433 H  HA   A LYS   A 1 110 ? 23.144 -13.724 -4.083  0.70 14.01 ?  110 LYS   A HA   1 
ATOM   2434 H  HA   B LYS   A 1 110 ? 23.192 -13.659 -3.904  0.30 14.47 ?  110 LYS   A HA   1 
ATOM   2435 H  HB2  A LYS   A 1 110 ? 22.868 -15.100 -5.986  0.70 15.02 ?  110 LYS   A HB2  1 
ATOM   2436 H  HB2  B LYS   A 1 110 ? 22.834 -14.942 -5.861  0.30 15.16 ?  110 LYS   A HB2  1 
ATOM   2437 H  HB3  A LYS   A 1 110 ? 24.440 -15.030 -6.218  0.70 15.02 ?  110 LYS   A HB3  1 
ATOM   2438 H  HB3  B LYS   A 1 110 ? 24.397 -14.895 -6.135  0.30 15.16 ?  110 LYS   A HB3  1 
ATOM   2439 H  HG2  A LYS   A 1 110 ? 24.835 -16.192 -4.282  0.70 16.09 ?  110 LYS   A HG2  1 
ATOM   2440 H  HG2  B LYS   A 1 110 ? 24.793 -16.164 -4.240  0.30 15.78 ?  110 LYS   A HG2  1 
ATOM   2441 H  HG3  A LYS   A 1 110 ? 23.301 -16.118 -3.877  0.70 16.09 ?  110 LYS   A HG3  1 
ATOM   2442 H  HG3  B LYS   A 1 110 ? 23.239 -16.161 -3.897  0.30 15.78 ?  110 LYS   A HG3  1 
ATOM   2443 H  HD2  A LYS   A 1 110 ? 22.784 -17.554 -5.663  0.70 16.52 ?  110 LYS   A HD2  1 
ATOM   2444 H  HD2  B LYS   A 1 110 ? 22.846 -17.392 -5.878  0.30 16.17 ?  110 LYS   A HD2  1 
ATOM   2445 H  HD3  A LYS   A 1 110 ? 24.336 -17.667 -5.997  0.70 16.52 ?  110 LYS   A HD3  1 
ATOM   2446 H  HD3  B LYS   A 1 110 ? 24.421 -17.478 -6.098  0.30 16.17 ?  110 LYS   A HD3  1 
ATOM   2447 H  HE2  A LYS   A 1 110 ? 23.898 -19.525 -4.801  0.70 17.79 ?  110 LYS   A HE2  1 
ATOM   2448 H  HE2  B LYS   A 1 110 ? 23.768 -19.451 -5.141  0.30 16.95 ?  110 LYS   A HE2  1 
ATOM   2449 H  HE3  A LYS   A 1 110 ? 24.595 -18.554 -3.755  0.70 17.79 ?  110 LYS   A HE3  1 
ATOM   2450 H  HE3  B LYS   A 1 110 ? 24.570 -18.644 -4.031  0.30 16.95 ?  110 LYS   A HE3  1 
ATOM   2451 H  HZ1  A LYS   A 1 110 ? 22.747 -19.506 -2.846  0.70 18.16 ?  110 LYS   A HZ1  1 
ATOM   2452 H  HZ1  B LYS   A 1 110 ? 22.651 -19.516 -3.170  0.30 17.34 ?  110 LYS   A HZ1  1 
ATOM   2453 H  HZ2  A LYS   A 1 110 ? 22.530 -18.076 -2.930  0.70 18.16 ?  110 LYS   A HZ2  1 
ATOM   2454 H  HZ2  B LYS   A 1 110 ? 22.580 -18.070 -3.100  0.30 17.34 ?  110 LYS   A HZ2  1 
ATOM   2455 H  HZ3  A LYS   A 1 110 ? 21.895 -18.961 -3.884  0.70 18.16 ?  110 LYS   A HZ3  1 
ATOM   2456 H  HZ3  B LYS   A 1 110 ? 21.839 -18.784 -4.121  0.30 17.34 ?  110 LYS   A HZ3  1 
ATOM   2457 N  N    A SER   A 1 111 ? 26.128 -13.025 -5.025  0.70 11.65 ?  111 SER   A N    1 
ATOM   2458 N  N    B SER   A 1 111 ? 26.146 -12.906 -4.879  0.30 11.60 ?  111 SER   A N    1 
ATOM   2459 C  CA   A SER   A 1 111 ? 27.454 -12.704 -4.509  0.70 12.06 ?  111 SER   A CA   1 
ATOM   2460 C  CA   B SER   A 1 111 ? 27.489 -12.629 -4.380  0.30 11.34 ?  111 SER   A CA   1 
ATOM   2461 C  C    A SER   A 1 111 ? 27.378 -11.647 -3.415  0.70 11.61 ?  111 SER   A C    1 
ATOM   2462 C  C    B SER   A 1 111 ? 27.457 -11.604 -3.255  0.30 11.33 ?  111 SER   A C    1 
ATOM   2463 O  O    A SER   A 1 111 ? 28.073 -11.739 -2.399  0.70 12.27 ?  111 SER   A O    1 
ATOM   2464 O  O    B SER   A 1 111 ? 28.177 -11.738 -2.258  0.30 11.64 ?  111 SER   A O    1 
ATOM   2465 C  CB   A SER   A 1 111 ? 28.346 -12.219 -5.652  0.70 13.79 ?  111 SER   A CB   1 
ATOM   2466 C  CB   B SER   A 1 111 ? 28.374 -12.132 -5.524  0.30 12.09 ?  111 SER   A CB   1 
ATOM   2467 O  OG   A SER   A 1 111 ? 28.457 -13.215 -6.657  0.70 15.95 ?  111 SER   A OG   1 
ATOM   2468 O  OG   B SER   A 1 111 ? 28.482 -13.115 -6.539  0.30 13.07 ?  111 SER   A OG   1 
ATOM   2469 H  H    A SER   A 1 111 ? 26.041 -12.931 -5.873  0.70 13.96 ?  111 SER   A H    1 
ATOM   2470 H  H    B SER   A 1 111 ? 26.027 -12.722 -5.710  0.30 13.90 ?  111 SER   A H    1 
ATOM   2471 H  HA   A SER   A 1 111 ? 27.855 -13.503 -4.131  0.70 14.45 ?  111 SER   A HA   1 
ATOM   2472 H  HA   B SER   A 1 111 ? 27.878 -13.447 -4.037  0.30 13.58 ?  111 SER   A HA   1 
ATOM   2473 H  HB2  A SER   A 1 111 ? 27.949 -11.424 -6.044  0.70 16.53 ?  111 SER   A HB2  1 
ATOM   2474 H  HB2  B SER   A 1 111 ? 27.983 -11.327 -5.901  0.30 14.48 ?  111 SER   A HB2  1 
ATOM   2475 H  HB3  A SER   A 1 111 ? 29.225 -12.008 -5.298  0.70 16.53 ?  111 SER   A HB3  1 
ATOM   2476 H  HB3  B SER   A 1 111 ? 29.260 -11.938 -5.180  0.30 14.48 ?  111 SER   A HB3  1 
ATOM   2477 H  HG   A SER   A 1 111 ? 28.965 -12.935 -7.270  0.70 19.12 ?  111 SER   A HG   1 
ATOM   2478 H  HG   B SER   A 1 111 ? 27.729 -13.279 -6.869  0.30 15.66 ?  111 SER   A HG   1 
ATOM   2479 N  N    A ALA   A 1 112 ? 26.524 -10.638 -3.602  0.70 11.68 ?  112 ALA   A N    1 
ATOM   2480 N  N    B ALA   A 1 112 ? 26.626 -10.570 -3.398  0.30 11.77 ?  112 ALA   A N    1 
ATOM   2481 C  CA   A ALA   A 1 112 ? 26.376 -9.593  -2.592  0.70 11.08 ?  112 ALA   A CA   1 
ATOM   2482 C  CA   B ALA   A 1 112 ? 26.518 -9.552  -2.358  0.30 11.69 ?  112 ALA   A CA   1 
ATOM   2483 C  C    A ALA   A 1 112 ? 25.909 -10.179 -1.262  0.70 11.38 ?  112 ALA   A C    1 
ATOM   2484 C  C    B ALA   A 1 112 ? 26.001 -10.160 -1.059  0.30 10.98 ?  112 ALA   A C    1 
ATOM   2485 O  O    A ALA   A 1 112 ? 26.453 -9.858  -0.201  0.70 11.70 ?  112 ALA   A O    1 
ATOM   2486 O  O    B ALA   A 1 112 ? 26.556 -9.922  0.019   0.30 10.62 ?  112 ALA   A O    1 
ATOM   2487 C  CB   A ALA   A 1 112 ? 25.397 -8.521  -3.086  0.70 11.35 ?  112 ALA   A CB   1 
ATOM   2488 C  CB   B ALA   A 1 112 ? 25.597 -8.427  -2.836  0.30 12.19 ?  112 ALA   A CB   1 
ATOM   2489 H  H    A ALA   A 1 112 ? 26.039 -10.529 -4.299  0.70 13.99 ?  112 ALA   A H    1 
ATOM   2490 H  H    B ALA   A 1 112 ? 26.122 -10.438 -4.078  0.30 14.10 ?  112 ALA   A H    1 
ATOM   2491 H  HA   A ALA   A 1 112 ? 27.233 -9.160  -2.444  0.70 13.28 ?  112 ALA   A HA   1 
ATOM   2492 H  HA   B ALA   A 1 112 ? 27.393 -9.167  -2.189  0.30 14.01 ?  112 ALA   A HA   1 
ATOM   2493 H  HB1  A ALA   A 1 112 ? 25.316 -7.824  -2.408  0.70 13.60 ?  112 ALA   A HB1  1 
ATOM   2494 H  HB1  B ALA   A 1 112 ? 25.525 -7.754  -2.139  0.30 14.61 ?  112 ALA   A HB1  1 
ATOM   2495 H  HB2  A ALA   A 1 112 ? 25.735 -8.132  -3.909  0.70 13.60 ?  112 ALA   A HB2  1 
ATOM   2496 H  HB2  B ALA   A 1 112 ? 25.970 -8.029  -3.640  0.30 14.61 ?  112 ALA   A HB2  1 
ATOM   2497 H  HB3  A ALA   A 1 112 ? 24.530 -8.925  -3.242  0.70 13.60 ?  112 ALA   A HB3  1 
ATOM   2498 H  HB3  B ALA   A 1 112 ? 24.720 -8.795  -3.028  0.30 14.61 ?  112 ALA   A HB3  1 
ATOM   2499 N  N    A TYR   A 1 113 ? 24.895 -11.049 -1.298  0.70 11.76 ?  113 TYR   A N    1 
ATOM   2500 N  N    B TYR   A 1 113 ? 24.936 -10.961 -1.146  0.30 10.71 ?  113 TYR   A N    1 
ATOM   2501 C  CA   A TYR   A 1 113 ? 24.383 -11.626 -0.058  0.70 11.63 ?  113 TYR   A CA   1 
ATOM   2502 C  CA   B TYR   A 1 113 ? 24.400 -11.601 0.051   0.30 10.86 ?  113 TYR   A CA   1 
ATOM   2503 C  C    A TYR   A 1 113 ? 25.391 -12.555 0.619   0.70 10.91 ?  113 TYR   A C    1 
ATOM   2504 C  C    B TYR   A 1 113 ? 25.378 -12.609 0.652   0.30 10.88 ?  113 TYR   A C    1 
ATOM   2505 O  O    A TYR   A 1 113 ? 25.360 -12.697 1.846   0.70 11.59 ?  113 TYR   A O    1 
ATOM   2506 O  O    B TYR   A 1 113 ? 25.317 -12.870 1.859   0.30 11.23 ?  113 TYR   A O    1 
ATOM   2507 C  CB   A TYR   A 1 113 ? 23.073 -12.369 -0.325  0.70 11.86 ?  113 TYR   A CB   1 
ATOM   2508 C  CB   B TYR   A 1 113 ? 23.047 -12.261 -0.245  0.30 10.87 ?  113 TYR   A CB   1 
ATOM   2509 C  CG   A TYR   A 1 113 ? 21.846 -11.489 -0.263  0.70 11.19 ?  113 TYR   A CG   1 
ATOM   2510 C  CG   B TYR   A 1 113 ? 21.845 -11.340 -0.104  0.30 10.36 ?  113 TYR   A CG   1 
ATOM   2511 C  CD1  A TYR   A 1 113 ? 21.463 -10.893 0.929   0.70 11.49 ?  113 TYR   A CD1  1 
ATOM   2512 C  CD1  B TYR   A 1 113 ? 21.543 -10.741 1.114   0.30 10.38 ?  113 TYR   A CD1  1 
ATOM   2513 C  CD2  A TYR   A 1 113 ? 21.058 -11.278 -1.385  0.70 11.10 ?  113 TYR   A CD2  1 
ATOM   2514 C  CD2  B TYR   A 1 113 ? 20.998 -11.094 -1.181  0.30 10.41 ?  113 TYR   A CD2  1 
ATOM   2515 C  CE1  A TYR   A 1 113 ? 20.331 -10.107 1.005   0.70 11.52 ?  113 TYR   A CE1  1 
ATOM   2516 C  CE1  B TYR   A 1 113 ? 20.440 -9.915  1.254   0.30 10.75 ?  113 TYR   A CE1  1 
ATOM   2517 C  CE2  A TYR   A 1 113 ? 19.911 -10.487 -1.320  0.70 11.37 ?  113 TYR   A CE2  1 
ATOM   2518 C  CE2  B TYR   A 1 113 ? 19.889 -10.262 -1.049  0.30 10.79 ?  113 TYR   A CE2  1 
ATOM   2519 C  CZ   A TYR   A 1 113 ? 19.557 -9.909  -0.118  0.70 11.15 ?  113 TYR   A CZ   1 
ATOM   2520 C  CZ   B TYR   A 1 113 ? 19.619 -9.682  0.172   0.30 10.75 ?  113 TYR   A CZ   1 
ATOM   2521 O  OH   A TYR   A 1 113 ? 18.419 -9.126  -0.012  0.70 11.69 ?  113 TYR   A OH   1 
ATOM   2522 O  OH   B TYR   A 1 113 ? 18.521 -8.861  0.323   0.30 10.26 ?  113 TYR   A OH   1 
ATOM   2523 H  H    A TYR   A 1 113 ? 24.496 -11.314 -2.014  0.70 14.09 ?  113 TYR   A H    1 
ATOM   2524 H  H    B TYR   A 1 113 ? 24.517 -11.140 -1.873  0.30 12.84 ?  113 TYR   A H    1 
ATOM   2525 H  HA   A TYR   A 1 113 ? 24.192 -10.906 0.560   0.70 13.94 ?  113 TYR   A HA   1 
ATOM   2526 H  HA   B TYR   A 1 113 ? 24.247 -10.915 0.717   0.30 13.01 ?  113 TYR   A HA   1 
ATOM   2527 H  HB2  A TYR   A 1 113 ? 23.109 -12.761 -1.211  0.70 14.21 ?  113 TYR   A HB2  1 
ATOM   2528 H  HB2  B TYR   A 1 113 ? 23.054 -12.595 -1.154  0.30 13.02 ?  113 TYR   A HB2  1 
ATOM   2529 H  HB3  A TYR   A 1 113 ? 22.969 -13.067 0.340   0.70 14.21 ?  113 TYR   A HB3  1 
ATOM   2530 H  HB3  B TYR   A 1 113 ? 22.922 -12.999 0.373   0.30 13.02 ?  113 TYR   A HB3  1 
ATOM   2531 H  HD1  A TYR   A 1 113 ? 21.980 -11.030 1.693   0.70 13.77 ?  113 TYR   A HD1  1 
ATOM   2532 H  HD1  B TYR   A 1 113 ? 22.091 -10.898 1.847   0.30 12.44 ?  113 TYR   A HD1  1 
ATOM   2533 H  HD2  A TYR   A 1 113 ? 21.292 -11.675 -2.192  0.70 13.30 ?  113 TYR   A HD2  1 
ATOM   2534 H  HD2  B TYR   A 1 113 ? 21.175 -11.487 -2.005  0.30 12.47 ?  113 TYR   A HD2  1 
ATOM   2535 H  HE1  A TYR   A 1 113 ? 20.092 -9.713  1.814   0.70 13.81 ?  113 TYR   A HE1  1 
ATOM   2536 H  HE1  B TYR   A 1 113 ? 20.253 -9.517  2.073   0.30 12.87 ?  113 TYR   A HE1  1 
ATOM   2537 H  HE2  A TYR   A 1 113 ? 19.387 -10.348 -2.076  0.70 13.62 ?  113 TYR   A HE2  1 
ATOM   2538 H  HE2  B TYR   A 1 113 ? 19.329 -10.101 -1.780  0.30 12.93 ?  113 TYR   A HE2  1 
ATOM   2539 H  HH   A TYR   A 1 113 ? 18.038 -9.070  -0.760  0.70 14.00 ?  113 TYR   A HH   1 
ATOM   2540 H  HH   B TYR   A 1 113 ? 18.110 -8.792  -0.408  0.30 12.29 ?  113 TYR   A HH   1 
ATOM   2541 N  N    . GLU   A 1 114 ? 26.284 -13.189 -0.151  1.00 11.31 ?  114 GLU   A N    1 
ATOM   2542 C  CA   . GLU   A 1 114 ? 27.282 -14.083 0.439   1.00 11.89 ?  114 GLU   A CA   1 
ATOM   2543 C  C    . GLU   A 1 114 ? 28.134 -13.375 1.486   1.00 11.46 ?  114 GLU   A C    1 
ATOM   2544 O  O    . GLU   A 1 114 ? 28.614 -14.012 2.431   1.00 11.69 ?  114 GLU   A O    1 
ATOM   2545 C  CB   . GLU   A 1 114 ? 28.150 -14.737 -0.646  1.00 11.97 ?  114 GLU   A CB   1 
ATOM   2546 C  CG   . GLU   A 1 114 ? 27.386 -15.789 -1.424  1.00 12.15 ?  114 GLU   A CG   1 
ATOM   2547 C  CD   . GLU   A 1 114 ? 28.095 -16.316 -2.664  1.00 12.55 ?  114 GLU   A CD   1 
ATOM   2548 O  OE1  . GLU   A 1 114 ? 29.044 -15.688 -3.165  1.00 12.56 ?  114 GLU   A OE1  1 
ATOM   2549 O  OE2  . GLU   A 1 114 ? 27.656 -17.381 -3.157  1.00 13.93 -1 114 GLU   A OE2  1 
ATOM   2550 H  H    A GLU   A 1 114 ? 26.337 -13.106 -1.010  0.70 13.55 ?  114 GLU   A H    1 
ATOM   2551 H  H    B GLU   A 1 114 ? 26.338 -13.081 -1.007  0.30 13.55 ?  114 GLU   A H    1 
ATOM   2552 H  HA   . GLU   A 1 114 ? 26.813 -14.794 0.888   1.00 14.25 ?  114 GLU   A HA   1 
ATOM   2553 H  HB2  . GLU   A 1 114 ? 28.449 -14.060 -1.277  1.00 14.34 ?  114 GLU   A HB2  1 
ATOM   2554 H  HB3  . GLU   A 1 114 ? 28.912 -15.168 -0.234  1.00 14.34 ?  114 GLU   A HB3  1 
ATOM   2555 H  HG2  . GLU   A 1 114 ? 27.225 -16.545 -0.842  1.00 14.55 ?  114 GLU   A HG2  1 
ATOM   2556 H  HG3  . GLU   A 1 114 ? 26.536 -15.413 -1.707  1.00 14.55 ?  114 GLU   A HG3  1 
ATOM   2557 N  N    . ASN   A 1 115 ? 28.327 -12.057 1.356   1.00 11.22 ?  115 ASN   A N    1 
ATOM   2558 C  CA   . ASN   A 1 115 ? 29.092 -11.329 2.363   1.00 11.83 ?  115 ASN   A CA   1 
ATOM   2559 C  C    . ASN   A 1 115 ? 28.472 -11.463 3.748   1.00 11.26 ?  115 ASN   A C    1 
ATOM   2560 O  O    . ASN   A 1 115 ? 29.186 -11.389 4.757   1.00 11.79 ?  115 ASN   A O    1 
ATOM   2561 C  CB   . ASN   A 1 115 ? 29.196 -9.852  1.985   1.00 11.98 ?  115 ASN   A CB   1 
ATOM   2562 C  CG   . ASN   A 1 115 ? 29.990 -9.638  0.725   1.00 12.33 ?  115 ASN   A CG   1 
ATOM   2563 O  OD1  . ASN   A 1 115 ? 31.208 -9.744  0.742   1.00 15.48 ?  115 ASN   A OD1  1 
ATOM   2564 N  ND2  . ASN   A 1 115 ? 29.321 -9.333  -0.368  1.00 12.00 ?  115 ASN   A ND2  1 
ATOM   2565 H  H    . ASN   A 1 115 ? 28.030 -11.571 0.709   1.00 13.45 ?  115 ASN   A H    1 
ATOM   2566 H  HA   . ASN   A 1 115 ? 29.989 -11.689 2.403   1.00 14.18 ?  115 ASN   A HA   1 
ATOM   2567 H  HB2  . ASN   A 1 115 ? 28.302 -9.495  1.855   1.00 14.36 ?  115 ASN   A HB2  1 
ATOM   2568 H  HB3  . ASN   A 1 115 ? 29.636 -9.373  2.712   1.00 14.36 ?  115 ASN   A HB3  1 
ATOM   2569 H  HD21 . ASN   A 1 115 ? 29.737 -9.202  -1.106  1.00 14.38 ?  115 ASN   A HD21 1 
ATOM   2570 H  HD22 . ASN   A 1 115 ? 28.458 -9.294  -0.348  1.00 14.38 ?  115 ASN   A HD22 1 
ATOM   2571 N  N    . PHE   A 1 116 ? 27.144 -11.624 3.826   1.00 11.42 ?  116 PHE   A N    1 
ATOM   2572 C  CA   . PHE   A 1 116 ? 26.494 -11.719 5.129   1.00 11.45 ?  116 PHE   A CA   1 
ATOM   2573 C  C    . PHE   A 1 116 ? 26.962 -12.953 5.903   1.00 11.87 ?  116 PHE   A C    1 
ATOM   2574 O  O    . PHE   A 1 116 ? 26.890 -12.970 7.134   1.00 12.35 ?  116 PHE   A O    1 
ATOM   2575 C  CB   . PHE   A 1 116 ? 24.961 -11.843 4.993   1.00 11.59 ?  116 PHE   A CB   1 
ATOM   2576 C  CG   . PHE   A 1 116 ? 24.208 -10.595 4.529   1.00 11.56 ?  116 PHE   A CG   1 
ATOM   2577 C  CD1  . PHE   A 1 116 ? 24.788 -9.567  3.794   1.00 11.03 ?  116 PHE   A CD1  1 
ATOM   2578 C  CD2  . PHE   A 1 116 ? 22.850 -10.493 4.839   1.00 11.83 ?  116 PHE   A CD2  1 
ATOM   2579 C  CE1  . PHE   A 1 116 ? 24.016 -8.488  3.374   1.00 11.67 ?  116 PHE   A CE1  1 
ATOM   2580 C  CE2  . PHE   A 1 116 ? 22.087 -9.426  4.431   1.00 11.83 ?  116 PHE   A CE2  1 
ATOM   2581 C  CZ   . PHE   A 1 116 ? 22.658 -8.418  3.699   1.00 11.40 ?  116 PHE   A CZ   1 
ATOM   2582 H  H    . PHE   A 1 116 ? 26.609 -11.670 3.148   1.00 13.68 ?  116 PHE   A H    1 
ATOM   2583 H  HA   . PHE   A 1 116 ? 26.692 -10.929 5.652   1.00 13.72 ?  116 PHE   A HA   1 
ATOM   2584 H  HB2  . PHE   A 1 116 ? 24.771 -12.550 4.353   1.00 13.89 ?  116 PHE   A HB2  1 
ATOM   2585 H  HB3  . PHE   A 1 116 ? 24.601 -12.093 5.858   1.00 13.89 ?  116 PHE   A HB3  1 
ATOM   2586 H  HD1  . PHE   A 1 116 ? 25.684 -9.622  3.563   1.00 13.22 ?  116 PHE   A HD1  1 
ATOM   2587 H  HD2  . PHE   A 1 116 ? 22.446 -11.183 5.325   1.00 14.18 ?  116 PHE   A HD2  1 
ATOM   2588 H  HE1  . PHE   A 1 116 ? 24.410 -7.801  2.887   1.00 13.99 ?  116 PHE   A HE1  1 
ATOM   2589 H  HE2  . PHE   A 1 116 ? 21.185 -9.392  4.661   1.00 14.17 ?  116 PHE   A HE2  1 
ATOM   2590 H  HZ   . PHE   A 1 116 ? 22.147 -7.685  3.439   1.00 13.66 ?  116 PHE   A HZ   1 
ATOM   2591 N  N    A ASN   A 1 117 ? 27.403 -14.004 5.203   0.70 11.97 ?  117 ASN   A N    1 
ATOM   2592 N  N    B ASN   A 1 117 ? 27.420 -13.994 5.202   0.30 11.88 ?  117 ASN   A N    1 
ATOM   2593 C  CA   A ASN   A 1 117 ? 27.767 -15.243 5.882   0.70 12.47 ?  117 ASN   A CA   1 
ATOM   2594 C  CA   B ASN   A 1 117 ? 27.777 -15.243 5.866   0.30 12.09 ?  117 ASN   A CA   1 
ATOM   2595 C  C    A ASN   A 1 117 ? 29.026 -15.113 6.722   0.70 12.75 ?  117 ASN   A C    1 
ATOM   2596 C  C    B ASN   A 1 117 ? 29.061 -15.150 6.673   0.30 12.33 ?  117 ASN   A C    1 
ATOM   2597 O  O    A ASN   A 1 117 ? 29.301 -16.001 7.537   0.70 13.59 ?  117 ASN   A O    1 
ATOM   2598 O  O    B ASN   A 1 117 ? 29.418 -16.127 7.342   0.30 12.89 ?  117 ASN   A O    1 
ATOM   2599 C  CB   A ASN   A 1 117 ? 27.879 -16.379 4.867   0.70 12.26 ?  117 ASN   A CB   1 
ATOM   2600 C  CB   B ASN   A 1 117 ? 27.892 -16.371 4.843   0.30 11.89 ?  117 ASN   A CB   1 
ATOM   2601 C  CG   A ASN   A 1 117 ? 26.527 -16.742 4.306   0.70 12.63 ?  117 ASN   A CG   1 
ATOM   2602 C  CG   B ASN   A 1 117 ? 26.544 -16.821 4.343   0.30 12.02 ?  117 ASN   A CG   1 
ATOM   2603 O  OD1  A ASN   A 1 117 ? 25.535 -16.720 5.032   0.70 13.53 ?  117 ASN   A OD1  1 
ATOM   2604 O  OD1  B ASN   A 1 117 ? 25.606 -16.965 5.125   0.30 12.24 ?  117 ASN   A OD1  1 
ATOM   2605 N  ND2  A ASN   A 1 117 ? 26.464 -17.034 3.020   0.70 12.65 ?  117 ASN   A ND2  1 
ATOM   2606 N  ND2  B ASN   A 1 117 ? 26.431 -17.030 3.040   0.30 11.86 ?  117 ASN   A ND2  1 
ATOM   2607 H  H    A ASN   A 1 117 ? 27.481 -14.025 4.343   0.70 14.35 ?  117 ASN   A H    1 
ATOM   2608 H  H    B ASN   A 1 117 ? 27.527 -14.000 4.346   0.30 14.24 ?  117 ASN   A H    1 
ATOM   2609 H  HA   A ASN   A 1 117 ? 27.044 -15.472 6.486   0.70 14.94 ?  117 ASN   A HA   1 
ATOM   2610 H  HA   B ASN   A 1 117 ? 27.055 -15.474 6.474   0.30 14.48 ?  117 ASN   A HA   1 
ATOM   2611 H  HB2  A ASN   A 1 117 ? 28.447 -16.101 4.133   0.70 14.69 ?  117 ASN   A HB2  1 
ATOM   2612 H  HB2  B ASN   A 1 117 ? 28.409 -16.060 4.085   0.30 14.25 ?  117 ASN   A HB2  1 
ATOM   2613 H  HB3  A ASN   A 1 117 ? 28.244 -17.161 5.304   0.70 14.69 ?  117 ASN   A HB3  1 
ATOM   2614 H  HB3  B ASN   A 1 117 ? 28.324 -17.130 5.260   0.30 14.25 ?  117 ASN   A HB3  1 
ATOM   2615 H  HD21 A ASN   A 1 117 ? 25.711 -17.236 2.664   0.70 15.15 ?  117 ASN   A HD21 1 
ATOM   2616 H  HD21 B ASN   A 1 117 ? 25.681 -17.283 2.707   0.30 14.21 ?  117 ASN   A HD21 1 
ATOM   2617 H  HD22 A ASN   A 1 117 ? 27.181 -17.027 2.544   0.70 15.15 ?  117 ASN   A HD22 1 
ATOM   2618 H  HD22 B ASN   A 1 117 ? 27.113 -16.916 2.527   0.30 14.21 ?  117 ASN   A HD22 1 
ATOM   2619 N  N    A GLN   A 1 118 ? 29.768 -14.020 6.572   0.70 12.69 ?  118 GLN   A N    1 
ATOM   2620 N  N    B GLN   A 1 118 ? 29.764 -14.023 6.624   0.30 12.51 ?  118 GLN   A N    1 
ATOM   2621 C  CA   A GLN   A 1 118 ? 30.941 -13.776 7.394   0.70 13.25 ?  118 GLN   A CA   1 
ATOM   2622 C  CA   B GLN   A 1 118 ? 30.952 -13.824 7.440   0.30 12.88 ?  118 GLN   A CA   1 
ATOM   2623 C  C    A GLN   A 1 118 ? 30.592 -13.181 8.757   0.70 13.43 ?  118 GLN   A C    1 
ATOM   2624 C  C    B GLN   A 1 118 ? 30.630 -13.280 8.826   0.30 12.66 ?  118 GLN   A C    1 
ATOM   2625 O  O    A GLN   A 1 118 ? 31.506 -12.815 9.509   0.70 14.36 ?  118 GLN   A O    1 
ATOM   2626 O  O    B GLN   A 1 118 ? 31.544 -13.133 9.645   0.30 13.03 ?  118 GLN   A O    1 
ATOM   2627 C  CB   A GLN   A 1 118 ? 31.935 -12.886 6.641   0.70 13.40 ?  118 GLN   A CB   1 
ATOM   2628 C  CB   B GLN   A 1 118 ? 31.949 -12.909 6.718   0.30 13.04 ?  118 GLN   A CB   1 
ATOM   2629 C  CG   A GLN   A 1 118 ? 32.384 -13.471 5.314   0.70 13.23 ?  118 GLN   A CG   1 
ATOM   2630 C  CG   B GLN   A 1 118 ? 32.468 -13.484 5.408   0.30 12.83 ?  118 GLN   A CG   1 
ATOM   2631 C  CD   A GLN   A 1 118 ? 33.247 -14.707 5.487   0.70 14.14 ?  118 GLN   A CD   1 
ATOM   2632 C  CD   B GLN   A 1 118 ? 33.236 -14.781 5.599   0.30 13.06 ?  118 GLN   A CD   1 
ATOM   2633 O  OE1  A GLN   A 1 118 ? 34.131 -14.746 6.349   0.70 14.92 ?  118 GLN   A OE1  1 
ATOM   2634 O  OE1  B GLN   A 1 118 ? 34.041 -14.910 6.523   0.30 13.22 ?  118 GLN   A OE1  1 
ATOM   2635 N  NE2  A GLN   A 1 118 ? 32.997 -15.725 4.667   0.70 14.38 ?  118 GLN   A NE2  1 
ATOM   2636 N  NE2  B GLN   A 1 118 ? 32.987 -15.750 4.724   0.30 13.16 ?  118 GLN   A NE2  1 
ATOM   2637 H  H    A GLN   A 1 118 ? 29.603 -13.393 5.998   0.70 15.21 ?  118 GLN   A H    1 
ATOM   2638 H  H    B GLN   A 1 118 ? 29.571 -13.353 6.118   0.30 14.99 ?  118 GLN   A H    1 
ATOM   2639 H  HA   A GLN   A 1 118 ? 31.373 -14.629 7.552   0.70 15.88 ?  118 GLN   A HA   1 
ATOM   2640 H  HA   B GLN   A 1 118 ? 31.379 -14.681 7.567   0.30 15.44 ?  118 GLN   A HA   1 
ATOM   2641 H  HB2  A GLN   A 1 118 ? 31.517 -12.030 6.468   0.70 16.06 ?  118 GLN   A HB2  1 
ATOM   2642 H  HB2  B GLN   A 1 118 ? 31.514 -12.065 6.521   0.30 15.62 ?  118 GLN   A HB2  1 
ATOM   2643 H  HB3  A GLN   A 1 118 ? 32.720 -12.765 7.198   0.70 16.06 ?  118 GLN   A HB3  1 
ATOM   2644 H  HB3  B GLN   A 1 118 ? 32.710 -12.758 7.300   0.30 15.62 ?  118 GLN   A HB3  1 
ATOM   2645 H  HG2  A GLN   A 1 118 ? 31.603 -13.714 4.791   0.70 15.85 ?  118 GLN   A HG2  1 
ATOM   2646 H  HG2  B GLN   A 1 118 ? 31.717 -13.662 4.821   0.30 15.37 ?  118 GLN   A HG2  1 
ATOM   2647 H  HG3  A GLN   A 1 118 ? 32.908 -12.809 4.839   0.70 15.85 ?  118 GLN   A HG3  1 
ATOM   2648 H  HG3  B GLN   A 1 118 ? 33.066 -12.841 4.996   0.30 15.37 ?  118 GLN   A HG3  1 
ATOM   2649 H  HE21 A GLN   A 1 118 ? 32.370 -15.658 4.075   0.70 17.23 ?  118 GLN   A HE21 1 
ATOM   2650 H  HE21 B GLN   A 1 118 ? 32.415 -15.623 4.091   0.30 15.77 ?  118 GLN   A HE21 1 
ATOM   2651 H  HE22 A GLN   A 1 118 ? 33.450 -16.452 4.725   0.70 17.23 ?  118 GLN   A HE22 1 
ATOM   2652 H  HE22 B GLN   A 1 118 ? 33.392 -16.505 4.788   0.30 15.77 ?  118 GLN   A HE22 1 
ATOM   2653 N  N    A HIS   A 1 119 ? 29.302 -13.088 9.094   0.70 13.37 ?  119 HIS   A N    1 
ATOM   2654 N  N    B HIS   A 1 119 ? 29.357 -13.005 9.114   0.30 12.63 ?  119 HIS   A N    1 
ATOM   2655 C  CA   A HIS   A 1 119 ? 28.848 -12.441 10.320  0.70 13.39 ?  119 HIS   A CA   1 
ATOM   2656 C  CA   B HIS   A 1 119 ? 28.926 -12.478 10.401  0.30 12.98 ?  119 HIS   A CA   1 
ATOM   2657 C  C    A HIS   A 1 119 ? 27.704 -13.233 10.929  0.70 14.00 ?  119 HIS   A C    1 
ATOM   2658 C  C    B HIS   A 1 119 ? 27.775 -13.330 10.910  0.30 13.58 ?  119 HIS   A C    1 
ATOM   2659 O  O    A HIS   A 1 119 ? 26.747 -13.576 10.230  0.70 14.50 ?  119 HIS   A O    1 
ATOM   2660 O  O    B HIS   A 1 119 ? 26.840 -13.626 10.160  0.30 13.80 ?  119 HIS   A O    1 
ATOM   2661 C  CB   A HIS   A 1 119 ? 28.393 -11.019 9.999   0.70 13.41 ?  119 HIS   A CB   1 
ATOM   2662 C  CB   B HIS   A 1 119 ? 28.506 -11.014 10.253  0.30 12.83 ?  119 HIS   A CB   1 
ATOM   2663 C  CG   A HIS   A 1 119 ? 29.458 -10.238 9.312   0.70 13.91 ?  119 HIS   A CG   1 
ATOM   2664 C  CG   B HIS   A 1 119 ? 29.611 -10.140 9.754   0.30 12.49 ?  119 HIS   A CG   1 
ATOM   2665 N  ND1  A HIS   A 1 119 ? 30.465 -9.603  10.002  0.70 16.22 ?  119 HIS   A ND1  1 
ATOM   2666 N  ND1  B HIS   A 1 119 ? 30.507 -9.527  10.600  0.30 12.84 ?  119 HIS   A ND1  1 
ATOM   2667 C  CD2  A HIS   A 1 119 ? 29.744 -10.089 7.998   0.70 14.28 ?  119 HIS   A CD2  1 
ATOM   2668 C  CD2  B HIS   A 1 119 ? 29.998 -9.821  8.497   0.30 12.36 ?  119 HIS   A CD2  1 
ATOM   2669 C  CE1  A HIS   A 1 119 ? 31.301 -9.053  9.141   0.70 15.52 ?  119 HIS   A CE1  1 
ATOM   2670 C  CE1  B HIS   A 1 119 ? 31.387 -8.847  9.886   0.30 12.82 ?  119 HIS   A CE1  1 
ATOM   2671 N  NE2  A HIS   A 1 119 ? 30.890 -9.337  7.918   0.70 15.14 ?  119 HIS   A NE2  1 
ATOM   2672 N  NE2  B HIS   A 1 119 ? 31.104 -9.014  8.607   0.30 12.72 ?  119 HIS   A NE2  1 
ATOM   2673 H  H    A HIS   A 1 119 ? 28.655 -13.408 8.617   0.70 16.03 ?  119 HIS   A H    1 
ATOM   2674 H  H    B HIS   A 1 119 ? 28.704 -13.128 8.567   0.30 15.14 ?  119 HIS   A H    1 
ATOM   2675 H  HA   A HIS   A 1 119 ? 29.579 -12.409 10.958  0.70 16.05 ?  119 HIS   A HA   1 
ATOM   2676 H  HA   B HIS   A 1 119 ? 29.656 -12.527 11.039  0.30 15.56 ?  119 HIS   A HA   1 
ATOM   2677 H  HB2  A HIS   A 1 119 ? 27.617 -11.066 9.419   0.70 16.07 ?  119 HIS   A HB2  1 
ATOM   2678 H  HB2  B HIS   A 1 119 ? 27.774 -10.957 9.622   0.30 15.37 ?  119 HIS   A HB2  1 
ATOM   2679 H  HB3  A HIS   A 1 119 ? 28.168 -10.574 10.829  0.70 16.07 ?  119 HIS   A HB3  1 
ATOM   2680 H  HB3  B HIS   A 1 119 ? 28.228 -10.674 11.118  0.30 15.37 ?  119 HIS   A HB3  1 
ATOM   2681 H  HD1  B HIS   A 1 119 ? 30.494 -9.569  11.456  0.30 15.39 ?  119 HIS   A HD1  1 
ATOM   2682 H  HD2  A HIS   A 1 119 ? 29.248 -10.427 7.283   0.70 17.11 ?  119 HIS   A HD2  1 
ATOM   2683 H  HD2  B HIS   A 1 119 ? 29.592 -10.096 7.706   0.30 14.81 ?  119 HIS   A HD2  1 
ATOM   2684 H  HE1  A HIS   A 1 119 ? 32.049 -8.551  9.359   0.70 18.60 ?  119 HIS   A HE1  1 
ATOM   2685 H  HE1  B HIS   A 1 119 ? 32.090 -8.338  10.224  0.30 15.36 ?  119 HIS   A HE1  1 
ATOM   2686 H  HE2  A HIS   A 1 119 ? 31.264 -9.079  7.191   0.70 18.14 ?  119 HIS   A HE2  1 
ATOM   2687 N  N    A GLU   A 1 120 ? 27.791 -13.496 12.237  0.70 14.82 ?  120 GLU   A N    1 
ATOM   2688 N  N    B GLU   A 1 120 ? 27.849 -13.731 12.183  0.30 14.20 ?  120 GLU   A N    1 
ATOM   2689 C  CA   A GLU   A 1 120 ? 26.828 -14.395 12.873  0.70 16.18 ?  120 GLU   A CA   1 
ATOM   2690 C  CA   B GLU   A 1 120 ? 26.895 -14.705 12.709  0.30 15.19 ?  120 GLU   A CA   1 
ATOM   2691 C  C    A GLU   A 1 120 ? 25.422 -13.808 12.957  0.70 14.94 ?  120 GLU   A C    1 
ATOM   2692 C  C    B GLU   A 1 120 ? 25.475 -14.146 12.757  0.30 13.25 ?  120 GLU   A C    1 
ATOM   2693 O  O    A GLU   A 1 120 ? 24.441 -14.566 12.897  0.70 15.16 ?  120 GLU   A O    1 
ATOM   2694 O  O    B GLU   A 1 120 ? 24.507 -14.881 12.527  0.30 12.11 ?  120 GLU   A O    1 
ATOM   2695 C  CB   A GLU   A 1 120 ? 27.323 -14.809 14.260  0.70 19.58 ?  120 GLU   A CB   1 
ATOM   2696 C  CB   B GLU   A 1 120 ? 27.334 -15.172 14.097  0.30 18.67 ?  120 GLU   A CB   1 
ATOM   2697 C  CG   A GLU   A 1 120 ? 28.461 -15.814 14.221  0.70 23.18 ?  120 GLU   A CG   1 
ATOM   2698 C  CG   B GLU   A 1 120 ? 28.592 -16.023 14.098  0.30 22.00 ?  120 GLU   A CG   1 
ATOM   2699 C  CD   A GLU   A 1 120 ? 28.635 -16.534 15.541  0.70 27.50 ?  120 GLU   A CD   1 
ATOM   2700 C  CD   B GLU   A 1 120 ? 28.821 -16.728 15.422  0.30 24.67 ?  120 GLU   A CD   1 
ATOM   2701 O  OE1  A GLU   A 1 120 ? 28.358 -15.917 16.593  0.70 30.03 ?  120 GLU   A OE1  1 
ATOM   2702 O  OE1  B GLU   A 1 120 ? 28.046 -16.487 16.372  0.30 25.97 ?  120 GLU   A OE1  1 
ATOM   2703 O  OE2  A GLU   A 1 120 ? 29.036 -17.718 15.527  0.70 30.21 -1 120 GLU   A OE2  1 
ATOM   2704 O  OE2  B GLU   A 1 120 ? 29.780 -17.524 15.511  0.30 25.98 -1 120 GLU   A OE2  1 
ATOM   2705 H  H    A GLU   A 1 120 ? 28.392 -13.171 12.767  0.70 17.77 ?  120 GLU   A H    1 
ATOM   2706 H  H    B GLU   A 1 120 ? 28.436 -13.458 12.753  0.30 17.02 ?  120 GLU   A H    1 
ATOM   2707 H  HA   A GLU   A 1 120 ? 26.764 -15.191 12.342  0.70 19.40 ?  120 GLU   A HA   1 
ATOM   2708 H  HA   B GLU   A 1 120 ? 26.894 -15.480 12.126  0.30 18.21 ?  120 GLU   A HA   1 
ATOM   2709 H  HB2  A GLU   A 1 120 ? 27.639 -14.027 14.739  0.70 23.47 ?  120 GLU   A HB2  1 
ATOM   2710 H  HB2  B GLU   A 1 120 ? 27.507 -14.394 14.649  0.30 22.38 ?  120 GLU   A HB2  1 
ATOM   2711 H  HB3  A GLU   A 1 120 ? 26.587 -15.216 14.749  0.70 23.47 ?  120 GLU   A HB3  1 
ATOM   2712 H  HB3  B GLU   A 1 120 ? 26.621 -15.700 14.488  0.30 22.38 ?  120 GLU   A HB3  1 
ATOM   2713 H  HG2  A GLU   A 1 120 ? 28.283 -16.472 13.529  0.70 27.79 ?  120 GLU   A HG2  1 
ATOM   2714 H  HG2  B GLU   A 1 120 ? 28.521 -16.691 13.398  0.30 26.38 ?  120 GLU   A HG2  1 
ATOM   2715 H  HG3  A GLU   A 1 120 ? 29.291 -15.352 14.034  0.70 27.79 ?  120 GLU   A HG3  1 
ATOM   2716 H  HG3  B GLU   A 1 120 ? 29.360 -15.455 13.943  0.30 26.38 ?  120 GLU   A HG3  1 
ATOM   2717 N  N    A VAL   A 1 121 ? 25.301 -12.489 13.123  0.70 14.53 ?  121 VAL   A N    1 
ATOM   2718 N  N    B VAL   A 1 121 ? 25.331 -12.864 13.085  0.30 12.67 ?  121 VAL   A N    1 
ATOM   2719 C  CA   A VAL   A 1 121 ? 24.002 -11.830 13.264  0.70 14.53 ?  121 VAL   A CA   1 
ATOM   2720 C  CA   B VAL   A 1 121 ? 24.038 -12.190 13.147  0.30 12.90 ?  121 VAL   A CA   1 
ATOM   2721 C  C    A VAL   A 1 121 ? 24.086 -10.463 12.601  0.70 13.05 ?  121 VAL   A C    1 
ATOM   2722 C  C    B VAL   A 1 121 ? 24.194 -10.816 12.510  0.30 12.20 ?  121 VAL   A C    1 
ATOM   2723 O  O    A VAL   A 1 121 ? 25.041 -9.720  12.837  0.70 13.40 ?  121 VAL   A O    1 
ATOM   2724 O  O    B VAL   A 1 121 ? 25.201 -10.136 12.730  0.30 12.64 ?  121 VAL   A O    1 
ATOM   2725 C  CB   A VAL   A 1 121 ? 23.590 -11.661 14.744  0.70 17.22 ?  121 VAL   A CB   1 
ATOM   2726 C  CB   B VAL   A 1 121 ? 23.540 -12.039 14.602  0.30 14.85 ?  121 VAL   A CB   1 
ATOM   2727 C  CG1  A VAL   A 1 121 ? 22.206 -11.034 14.843  0.70 17.75 ?  121 VAL   A CG1  1 
ATOM   2728 C  CG1  B VAL   A 1 121 ? 22.191 -11.326 14.640  0.30 15.09 ?  121 VAL   A CG1  1 
ATOM   2729 C  CG2  A VAL   A 1 121 ? 23.615 -12.987 15.487  0.70 18.72 ?  121 VAL   A CG2  1 
ATOM   2730 C  CG2  B VAL   A 1 121 ? 23.444 -13.386 15.298  0.30 16.30 ?  121 VAL   A CG2  1 
ATOM   2731 H  H    A VAL   A 1 121 ? 25.966 -11.926 13.152  0.70 17.41 ?  121 VAL   A H    1 
ATOM   2732 H  H    B VAL   A 1 121 ? 25.990 -12.353 13.278  0.30 15.18 ?  121 VAL   A H    1 
ATOM   2733 H  HA   A VAL   A 1 121 ? 23.321 -12.344 12.813  0.70 17.41 ?  121 VAL   A HA   1 
ATOM   2734 H  HA   B VAL   A 1 121 ? 23.385 -12.702 12.647  0.30 15.46 ?  121 VAL   A HA   1 
ATOM   2735 H  HB   A VAL   A 1 121 ? 24.214 -11.065 15.185  0.70 20.64 ?  121 VAL   A HB   1 
ATOM   2736 H  HB   B VAL   A 1 121 ? 24.175 -11.492 15.091  0.30 17.80 ?  121 VAL   A HB   1 
ATOM   2737 H  HG11 A VAL   A 1 121 ? 21.887 -11.114 15.756  0.70 21.27 ?  121 VAL   A HG11 1 
ATOM   2738 H  HG11 B VAL   A 1 121 ? 21.833 -11.382 15.541  0.30 18.08 ?  121 VAL   A HG11 1 
ATOM   2739 H  HG12 A VAL   A 1 121 ? 22.261 -10.101 14.593  0.70 21.27 ?  121 VAL   A HG12 1 
ATOM   2740 H  HG12 B VAL   A 1 121 ? 22.312 -10.394 14.394  0.30 18.08 ?  121 VAL   A HG12 1 
ATOM   2741 H  HG13 A VAL   A 1 121 ? 21.604 -11.505 14.243  0.70 21.27 ?  121 VAL   A HG13 1 
ATOM   2742 H  HG13 B VAL   A 1 121 ? 21.586 -11.757 14.018  0.30 18.08 ?  121 VAL   A HG13 1 
ATOM   2743 H  HG21 A VAL   A 1 121 ? 23.271 -12.855 16.389  0.70 22.45 ?  121 VAL   A HG21 1 
ATOM   2744 H  HG21 B VAL   A 1 121 ? 23.257 -13.235 16.238  0.30 19.54 ?  121 VAL   A HG21 1 
ATOM   2745 H  HG22 A VAL   A 1 121 ? 23.052 -13.626 15.018  0.70 22.45 ?  121 VAL   A HG22 1 
ATOM   2746 H  HG22 B VAL   A 1 121 ? 22.724 -13.897 14.900  0.30 19.54 ?  121 VAL   A HG22 1 
ATOM   2747 H  HG23 A VAL   A 1 121 ? 24.524 -13.315 15.528  0.70 22.45 ?  121 VAL   A HG23 1 
ATOM   2748 H  HG23 B VAL   A 1 121 ? 24.283 -13.856 15.199  0.30 19.54 ?  121 VAL   A HG23 1 
ATOM   2749 N  N    A LEU   A 1 122 ? 23.074 -10.108 11.801  0.70 12.27 ?  122 LEU   A N    1 
ATOM   2750 N  N    B LEU   A 1 122 ? 23.195 -10.397 11.731  0.30 12.09 ?  122 LEU   A N    1 
ATOM   2751 C  CA   A LEU   A 1 122 ? 23.056 -8.819  11.111  0.70 11.74 ?  122 LEU   A CA   1 
ATOM   2752 C  CA   B LEU   A 1 122 ? 23.245 -9.091  11.086  0.30 11.98 ?  122 LEU   A CA   1 
ATOM   2753 C  C    A LEU   A 1 122 ? 21.658 -8.217  11.116  0.70 11.50 ?  122 LEU   A C    1 
ATOM   2754 C  C    B LEU   A 1 122 ? 21.847 -8.496  10.998  0.30 11.10 ?  122 LEU   A C    1 
ATOM   2755 O  O    A LEU   A 1 122 ? 20.659 -8.932  11.025  0.70 12.91 ?  122 LEU   A O    1 
ATOM   2756 O  O    B LEU   A 1 122 ? 20.861 -9.209  10.797  0.30 10.91 ?  122 LEU   A O    1 
ATOM   2757 C  CB   A LEU   A 1 122 ? 23.468 -8.931  9.635   0.70 12.91 ?  122 LEU   A CB   1 
ATOM   2758 C  CB   B LEU   A 1 122 ? 23.799 -9.149  9.654   0.30 13.60 ?  122 LEU   A CB   1 
ATOM   2759 C  CG   A LEU   A 1 122 ? 24.658 -9.809  9.258   0.70 12.51 ?  122 LEU   A CG   1 
ATOM   2760 C  CG   B LEU   A 1 122 ? 25.065 -9.933  9.323   0.30 14.31 ?  122 LEU   A CG   1 
ATOM   2761 C  CD1  A LEU   A 1 122 ? 24.221 -11.247 9.030   0.70 13.04 ?  122 LEU   A CD1  1 
ATOM   2762 C  CD1  B LEU   A 1 122 ? 24.769 -11.416 9.140   0.30 14.44 ?  122 LEU   A CD1  1 
ATOM   2763 C  CD2  A LEU   A 1 122 ? 25.353 -9.256  8.020   0.70 12.62 ?  122 LEU   A CD2  1 
ATOM   2764 C  CD2  B LEU   A 1 122 ? 25.691 -9.354  8.064   0.30 14.07 ?  122 LEU   A CD2  1 
ATOM   2765 H  H    A LEU   A 1 122 ? 22.380 -10.597 11.638  0.70 14.70 ?  122 LEU   A H    1 
ATOM   2766 H  H    B LEU   A 1 122 ? 22.479 -10.848 11.561  0.30 14.49 ?  122 LEU   A H    1 
ATOM   2767 H  HA   A LEU   A 1 122 ? 23.650 -8.197  11.556  0.70 14.07 ?  122 LEU   A HA   1 
ATOM   2768 H  HA   B LEU   A 1 122 ? 23.801 -8.494  11.607  0.30 14.35 ?  122 LEU   A HA   1 
ATOM   2769 H  HB2  A LEU   A 1 122 ? 22.710 -9.271  9.142   0.70 15.48 ?  122 LEU   A HB2  1 
ATOM   2770 H  HB2  B LEU   A 1 122 ? 23.102 -9.518  9.093   0.30 16.29 ?  122 LEU   A HB2  1 
ATOM   2771 H  HB3  A LEU   A 1 122 ? 23.675 -8.038  9.321   0.70 15.48 ?  122 LEU   A HB3  1 
ATOM   2772 H  HB3  B LEU   A 1 122 ? 23.967 -8.235  9.377   0.30 16.29 ?  122 LEU   A HB3  1 
ATOM   2773 H  HG   A LEU   A 1 122 ? 25.305 -9.805  9.981   0.70 15.00 ?  122 LEU   A HG   1 
ATOM   2774 H  HG   B LEU   A 1 122 ? 25.705 -9.835  10.046  0.30 17.15 ?  122 LEU   A HG   1 
ATOM   2775 H  HD11 A LEU   A 1 122 ? 24.989 -11.777 8.769   0.70 15.63 ?  122 LEU   A HD11 1 
ATOM   2776 H  HD11 B LEU   A 1 122 ? 25.588 -11.871 8.889   0.30 17.30 ?  122 LEU   A HD11 1 
ATOM   2777 H  HD12 A LEU   A 1 122 ? 23.840 -11.594 9.850   0.70 15.63 ?  122 LEU   A HD12 1 
ATOM   2778 H  HD12 B LEU   A 1 122 ? 24.432 -11.779 9.971   0.30 17.30 ?  122 LEU   A HD12 1 
ATOM   2779 H  HD13 A LEU   A 1 122 ? 23.553 -11.265 8.323   0.70 15.63 ?  122 LEU   A HD13 1 
ATOM   2780 H  HD13 B LEU   A 1 122 ? 24.107 -11.520 8.439   0.30 17.30 ?  122 LEU   A HD13 1 
ATOM   2781 H  HD21 A LEU   A 1 122 ? 26.087 -9.844  7.775   0.70 15.12 ?  122 LEU   A HD21 1 
ATOM   2782 H  HD21 B LEU   A 1 122 ? 26.466 -9.883  7.822   0.30 16.86 ?  122 LEU   A HD21 1 
ATOM   2783 H  HD22 A LEU   A 1 122 ? 24.713 -9.209  7.291   0.70 15.12 ?  122 LEU   A HD22 1 
ATOM   2784 H  HD22 B LEU   A 1 122 ? 25.036 -9.379  7.347   0.30 16.86 ?  122 LEU   A HD22 1 
ATOM   2785 H  HD23 A LEU   A 1 122 ? 25.695 -8.368  8.216   0.70 15.12 ?  122 LEU   A HD23 1 
ATOM   2786 H  HD23 B LEU   A 1 122 ? 25.956 -8.436  8.235   0.30 16.86 ?  122 LEU   A HD23 1 
ATOM   2787 N  N    A LEU   A 1 123 ? 21.605 -6.883  11.194  0.70 11.25 ?  123 LEU   A N    1 
ATOM   2788 N  N    B LEU   A 1 123 ? 21.784 -7.175  11.128  0.30 10.99 ?  123 LEU   A N    1 
ATOM   2789 C  CA   A LEU   A 1 123 ? 20.430 -6.086  10.841  0.70 11.03 ?  123 LEU   A CA   1 
ATOM   2790 C  CA   B LEU   A 1 123 ? 20.619 -6.387  10.749  0.30 10.86 ?  123 LEU   A CA   1 
ATOM   2791 C  C    A LEU   A 1 123 ? 20.653 -5.553  9.432   0.70 10.82 ?  123 LEU   A C    1 
ATOM   2792 C  C    B LEU   A 1 123 ? 20.881 -5.843  9.354   0.30 10.27 ?  123 LEU   A C    1 
ATOM   2793 O  O    A LEU   A 1 123 ? 21.697 -4.950  9.171   0.70 11.47 ?  123 LEU   A O    1 
ATOM   2794 O  O    B LEU   A 1 123 ? 21.938 -5.254  9.112   0.30 9.92  ?  123 LEU   A O    1 
ATOM   2795 C  CB   A LEU   A 1 123 ? 20.295 -4.902  11.802  0.70 12.03 ?  123 LEU   A CB   1 
ATOM   2796 C  CB   B LEU   A 1 123 ? 20.455 -5.225  11.727  0.30 10.95 ?  123 LEU   A CB   1 
ATOM   2797 C  CG   A LEU   A 1 123 ? 19.234 -3.853  11.448  0.70 13.32 ?  123 LEU   A CG   1 
ATOM   2798 C  CG   B LEU   A 1 123 ? 19.457 -4.114  11.391  0.30 11.76 ?  123 LEU   A CG   1 
ATOM   2799 C  CD1  A LEU   A 1 123 ? 17.846 -4.472  11.442  0.70 13.92 ?  123 LEU   A CD1  1 
ATOM   2800 C  CD1  B LEU   A 1 123 ? 18.023 -4.624  11.385  0.30 12.41 ?  123 LEU   A CD1  1 
ATOM   2801 C  CD2  A LEU   A 1 123 ? 19.304 -2.671  12.411  0.70 13.44 ?  123 LEU   A CD2  1 
ATOM   2802 C  CD2  B LEU   A 1 123 ? 19.620 -2.967  12.376  0.30 11.59 ?  123 LEU   A CD2  1 
ATOM   2803 H  H    A LEU   A 1 123 ? 22.264 -6.394  11.458  0.70 13.48 ?  123 LEU   A H    1 
ATOM   2804 H  H    B LEU   A 1 123 ? 22.427 -6.702  11.443  0.30 13.17 ?  123 LEU   A H    1 
ATOM   2805 H  HA   A LEU   A 1 123 ? 19.622 -6.620  10.872  0.70 13.22 ?  123 LEU   A HA   1 
ATOM   2806 H  HA   B LEU   A 1 123 ? 19.819 -6.938  10.744  0.30 13.01 ?  123 LEU   A HA   1 
ATOM   2807 H  HB2  A LEU   A 1 123 ? 20.066 -5.239  12.685  0.70 14.41 ?  123 LEU   A HB2  1 
ATOM   2808 H  HB2  B LEU   A 1 123 ? 20.182 -5.599  12.578  0.30 13.12 ?  123 LEU   A HB2  1 
ATOM   2809 H  HB3  A LEU   A 1 123 ? 21.144 -4.437  11.849  0.70 14.41 ?  123 LEU   A HB3  1 
ATOM   2810 H  HB3  B LEU   A 1 123 ? 21.321 -4.806  11.828  0.30 13.12 ?  123 LEU   A HB3  1 
ATOM   2811 H  HG   A LEU   A 1 123 ? 19.409 -3.508  10.555  0.70 15.97 ?  123 LEU   A HG   1 
ATOM   2812 H  HG   B LEU   A 1 123 ? 19.654 -3.771  10.506  0.30 14.10 ?  123 LEU   A HG   1 
ATOM   2813 H  HD11 A LEU   A 1 123 ? 17.190 -3.782  11.274  0.70 16.68 ?  123 LEU   A HD11 1 
ATOM   2814 H  HD11 B LEU   A 1 123 ? 17.426 -3.879  11.211  0.30 14.88 ?  123 LEU   A HD11 1 
ATOM   2815 H  HD12 A LEU   A 1 123 ? 17.806 -5.146  10.742  0.70 16.68 ?  123 LEU   A HD12 1 
ATOM   2816 H  HD12 B LEU   A 1 123 ? 17.929 -5.293  10.690  0.30 14.88 ?  123 LEU   A HD12 1 
ATOM   2817 H  HD13 A LEU   A 1 123 ? 17.685 -4.885  12.305  0.70 16.68 ?  123 LEU   A HD13 1 
ATOM   2818 H  HD13 B LEU   A 1 123 ? 17.823 -5.014  12.250  0.30 14.88 ?  123 LEU   A HD13 1 
ATOM   2819 H  HD21 A LEU   A 1 123 ? 18.625 -2.023  12.165  0.70 16.11 ?  123 LEU   A HD21 1 
ATOM   2820 H  HD21 B LEU   A 1 123 ? 18.982 -2.272  12.158  0.30 13.88 ?  123 LEU   A HD21 1 
ATOM   2821 H  HD22 A LEU   A 1 123 ? 19.141 -2.995  13.312  0.70 16.11 ?  123 LEU   A HD22 1 
ATOM   2822 H  HD22 B LEU   A 1 123 ? 19.457 -3.298  13.274  0.30 13.88 ?  123 LEU   A HD22 1 
ATOM   2823 H  HD23 A LEU   A 1 123 ? 20.183 -2.271  12.356  0.70 16.11 ?  123 LEU   A HD23 1 
ATOM   2824 H  HD23 B LEU   A 1 123 ? 20.524 -2.621  12.311  0.30 13.88 ?  123 LEU   A HD23 1 
ATOM   2825 N  N    A ALA   A 1 124 ? 19.693 -5.758  8.526   0.70 10.38 ?  124 ALA   A N    1 
ATOM   2826 N  N    B ALA   A 1 124 ? 19.943 -6.045  8.438   0.30 9.86  ?  124 ALA   A N    1 
ATOM   2827 C  CA   A ALA   A 1 124 ? 19.986 -5.484  7.123   0.70 10.46 ?  124 ALA   A CA   1 
ATOM   2828 C  CA   B ALA   A 1 124 ? 20.194 -5.758  7.035   0.30 10.36 ?  124 ALA   A CA   1 
ATOM   2829 C  C    A ALA   A 1 124 ? 18.759 -5.057  6.329   0.70 10.47 ?  124 ALA   A C    1 
ATOM   2830 C  C    B ALA   A 1 124 ? 18.950 -5.209  6.357   0.30 10.49 ?  124 ALA   A C    1 
ATOM   2831 O  O    A ALA   A 1 124 ? 17.630 -5.445  6.661   0.70 11.30 ?  124 ALA   A O    1 
ATOM   2832 O  O    B ALA   A 1 124 ? 17.824 -5.452  6.807   0.30 10.94 ?  124 ALA   A O    1 
ATOM   2833 C  CB   A ALA   A 1 124 ? 20.610 -6.712  6.446   0.70 10.80 ?  124 ALA   A CB   1 
ATOM   2834 C  CB   B ALA   A 1 124 ? 20.661 -7.012  6.283   0.30 10.77 ?  124 ALA   A CB   1 
ATOM   2835 H  H    A ALA   A 1 124 ? 18.892 -6.038  8.693   0.70 12.44 ?  124 ALA   A H    1 
ATOM   2836 H  H    B ALA   A 1 124 ? 19.156 -6.357  8.598   0.30 11.82 ?  124 ALA   A H    1 
ATOM   2837 H  HA   A ALA   A 1 124 ? 20.633 -4.764  7.088   0.70 12.53 ?  124 ALA   A HA   1 
ATOM   2838 H  HA   B ALA   A 1 124 ? 20.896 -5.095  6.984   0.30 12.41 ?  124 ALA   A HA   1 
ATOM   2839 H  HB1  A ALA   A 1 124 ? 20.800 -6.501  5.520   0.70 12.94 ?  124 ALA   A HB1  1 
ATOM   2840 H  HB1  B ALA   A 1 124 ? 20.824 -6.783  5.355   0.30 12.90 ?  124 ALA   A HB1  1 
ATOM   2841 H  HB2  A ALA   A 1 124 ? 21.438 -6.937  6.907   0.70 12.94 ?  124 ALA   A HB2  1 
ATOM   2842 H  HB2  B ALA   A 1 124 ? 21.481 -7.340  6.689   0.30 12.90 ?  124 ALA   A HB2  1 
ATOM   2843 H  HB3  A ALA   A 1 124 ? 19.992 -7.454  6.501   0.70 12.94 ?  124 ALA   A HB3  1 
ATOM   2844 H  HB3  B ALA   A 1 124 ? 19.971 -7.691  6.341   0.30 12.90 ?  124 ALA   A HB3  1 
ATOM   2845 N  N    A PRO   A 1 125 ? 18.960 -4.312  5.245   0.70 10.85 ?  125 PRO   A N    1 
ATOM   2846 N  N    B PRO   A 1 125 ? 19.127 -4.468  5.256   0.30 9.91  ?  125 PRO   A N    1 
ATOM   2847 C  CA   A PRO   A 1 125 ? 17.912 -4.097  4.248   0.70 11.10 ?  125 PRO   A CA   1 
ATOM   2848 C  CA   B PRO   A 1 125 ? 17.995 -4.097  4.404   0.30 10.41 ?  125 PRO   A CA   1 
ATOM   2849 C  C    A PRO   A 1 125 ? 17.974 -5.182  3.177   0.70 11.03 ?  125 PRO   A C    1 
ATOM   2850 C  C    B PRO   A 1 125 ? 17.898 -5.077  3.248   0.30 11.29 ?  125 PRO   A C    1 
ATOM   2851 O  O    A PRO   A 1 125 ? 18.943 -5.941  3.075   0.70 10.75 ?  125 PRO   A O    1 
ATOM   2852 O  O    B PRO   A 1 125 ? 18.781 -5.927  3.097   0.30 11.61 ?  125 PRO   A O    1 
ATOM   2853 C  CB   A PRO   A 1 125 ? 18.340 -2.757  3.631   0.70 11.15 ?  125 PRO   A CB   1 
ATOM   2854 C  CB   B PRO   A 1 125 ? 18.413 -2.713  3.897   0.30 10.11 ?  125 PRO   A CB   1 
ATOM   2855 C  CG   A PRO   A 1 125 ? 19.848 -2.910  3.558   0.70 11.50 ?  125 PRO   A CG   1 
ATOM   2856 C  CG   B PRO   A 1 125 ? 19.922 -2.857  3.722   0.30 10.16 ?  125 PRO   A CG   1 
ATOM   2857 C  CD   A PRO   A 1 125 ? 20.206 -3.612  4.870   0.70 11.75 ?  125 PRO   A CD   1 
ATOM   2858 C  CD   B PRO   A 1 125 ? 20.387 -3.901  4.740   0.30 9.63  ?  125 PRO   A CD   1 
ATOM   2859 H  HA   A PRO   A 1 125 ? 17.027 -4.042  4.648   0.70 13.30 ?  125 PRO   A HA   1 
ATOM   2860 H  HA   B PRO   A 1 125 ? 17.162 -4.049  4.905   0.30 12.47 ?  125 PRO   A HA   1 
ATOM   2861 H  HB2  A PRO   A 1 125 ? 17.942 -2.655  2.748   0.70 13.36 ?  125 PRO   A HB2  1 
ATOM   2862 H  HB2  B PRO   A 1 125 ? 17.978 -2.524  3.049   0.30 12.12 ?  125 PRO   A HB2  1 
ATOM   2863 H  HB3  A PRO   A 1 125 ? 18.080 -2.023  4.215   0.70 13.36 ?  125 PRO   A HB3  1 
ATOM   2864 H  HB3  B PRO   A 1 125 ? 18.197 -2.035  4.557   0.30 12.12 ?  125 PRO   A HB3  1 
ATOM   2865 H  HG2  A PRO   A 1 125 ? 20.089 -3.460  2.793   0.70 13.78 ?  125 PRO   A HG2  1 
ATOM   2866 H  HG2  B PRO   A 1 125 ? 20.114 -3.154  2.818   0.30 12.17 ?  125 PRO   A HG2  1 
ATOM   2867 H  HG3  A PRO   A 1 125 ? 20.266 -2.037  3.499   0.70 13.78 ?  125 PRO   A HG3  1 
ATOM   2868 H  HG3  B PRO   A 1 125 ? 20.349 -2.002  3.892   0.30 12.17 ?  125 PRO   A HG3  1 
ATOM   2869 H  HD2  A PRO   A 1 125 ? 20.927 -4.239  4.731   0.70 14.08 ?  125 PRO   A HD2  1 
ATOM   2870 H  HD2  B PRO   A 1 125 ? 20.923 -4.582  4.298   0.30 11.54 ?  125 PRO   A HD2  1 
ATOM   2871 H  HD3  A PRO   A 1 125 ? 20.437 -2.949  5.547   0.70 14.08 ?  125 PRO   A HD3  1 
ATOM   2872 H  HD3  B PRO   A 1 125 ? 20.884 -3.469  5.453   0.30 11.54 ?  125 PRO   A HD3  1 
ATOM   2873 N  N    A LEU   A 1 126 ? 16.933 -5.211  2.348   0.70 10.95 ?  126 LEU   A N    1 
ATOM   2874 N  N    B LEU   A 1 126 ? 16.865 -4.974  2.416   0.30 11.72 ?  126 LEU   A N    1 
ATOM   2875 C  CA   A LEU   A 1 126 ? 16.942 -6.042  1.153   0.70 11.10 ?  126 LEU   A CA   1 
ATOM   2876 C  CA   B LEU   A 1 126 ? 16.846 -5.748  1.179   0.30 11.73 ?  126 LEU   A CA   1 
ATOM   2877 C  C    A LEU   A 1 126 ? 17.855 -5.434  0.094   0.70 11.36 ?  126 LEU   A C    1 
ATOM   2878 C  C    B LEU   A 1 126 ? 17.815 -5.132  0.174   0.30 11.36 ?  126 LEU   A C    1 
ATOM   2879 O  O    A LEU   A 1 126 ? 17.610 -4.331  -0.407  0.70 12.40 ?  126 LEU   A O    1 
ATOM   2880 O  O    B LEU   A 1 126 ? 17.622 -3.996  -0.271  0.30 11.92 ?  126 LEU   A O    1 
ATOM   2881 C  CB   A LEU   A 1 126 ? 15.527 -6.202  0.615   0.70 11.46 ?  126 LEU   A CB   1 
ATOM   2882 C  CB   B LEU   A 1 126 ? 15.439 -5.784  0.588   0.30 12.94 ?  126 LEU   A CB   1 
ATOM   2883 C  CG   A LEU   A 1 126 ? 14.633 -7.134  1.432   0.70 12.41 ?  126 LEU   A CG   1 
ATOM   2884 C  CG   B LEU   A 1 126 ? 14.458 -6.840  1.102   0.30 13.89 ?  126 LEU   A CG   1 
ATOM   2885 C  CD1  A LEU   A 1 126 ? 13.189 -6.961  0.996   0.70 13.43 ?  126 LEU   A CD1  1 
ATOM   2886 C  CD1  B LEU   A 1 126 ? 13.194 -6.862  0.246   0.30 14.10 ?  126 LEU   A CD1  1 
ATOM   2887 C  CD2  A LEU   A 1 126 ? 15.075 -8.591  1.285   0.70 12.84 ?  126 LEU   A CD2  1 
ATOM   2888 C  CD2  B LEU   A 1 126 ? 15.089 -8.223  1.133   0.30 14.44 ?  126 LEU   A CD2  1 
ATOM   2889 H  H    A LEU   A 1 126 ? 16.213 -4.750  2.447   0.70 13.12 ?  126 LEU   A H    1 
ATOM   2890 H  H    B LEU   A 1 126 ? 16.171 -4.474  2.548   0.30 14.05 ?  126 LEU   A H    1 
ATOM   2891 H  HA   A LEU   A 1 126 ? 17.285 -6.918  1.372   0.70 13.29 ?  126 LEU   A HA   1 
ATOM   2892 H  HA   B LEU   A 1 126 ? 17.137 -6.654  1.372   0.30 14.06 ?  126 LEU   A HA   1 
ATOM   2893 H  HB2  A LEU   A 1 126 ? 15.098 -5.333  0.600   0.70 13.73 ?  126 LEU   A HB2  1 
ATOM   2894 H  HB2  B LEU   A 1 126 ? 15.029 -4.919  0.746   0.30 15.51 ?  126 LEU   A HB2  1 
ATOM   2895 H  HB3  A LEU   A 1 126 ? 15.570 -6.560  -0.285  0.70 13.73 ?  126 LEU   A HB3  1 
ATOM   2896 H  HB3  B LEU   A 1 126 ? 15.527 -5.923  -0.366  0.30 15.51 ?  126 LEU   A HB3  1 
ATOM   2897 H  HG   A LEU   A 1 126 ? 14.691 -6.898  2.371   0.70 14.88 ?  126 LEU   A HG   1 
ATOM   2898 H  HG   B LEU   A 1 126 ? 14.196 -6.610  2.006   0.30 16.64 ?  126 LEU   A HG   1 
ATOM   2899 H  HD11 A LEU   A 1 126 ? 12.628 -7.566  1.511   0.70 16.09 ?  126 LEU   A HD11 1 
ATOM   2900 H  HD11 B LEU   A 1 126 ? 12.583 -7.527  0.602   0.30 16.90 ?  126 LEU   A HD11 1 
ATOM   2901 H  HD12 A LEU   A 1 126 ? 12.920 -6.045  1.155   0.70 16.09 ?  126 LEU   A HD12 1 
ATOM   2902 H  HD12 B LEU   A 1 126 ? 12.779 -5.986  0.269   0.30 16.90 ?  126 LEU   A HD12 1 
ATOM   2903 H  HD13 A LEU   A 1 126 ? 13.117 -7.172  0.052   0.70 16.09 ?  126 LEU   A HD13 1 
ATOM   2904 H  HD13 B LEU   A 1 126 ? 13.434 -7.091  -0.667  0.30 16.90 ?  126 LEU   A HD13 1 
ATOM   2905 H  HD21 A LEU   A 1 126 ? 14.427 -9.167  1.718   0.70 15.38 ?  126 LEU   A HD21 1 
ATOM   2906 H  HD21 B LEU   A 1 126 ? 14.388 -8.887  1.214   0.30 17.31 ?  126 LEU   A HD21 1 
ATOM   2907 H  HD22 A LEU   A 1 126 ? 15.134 -8.809  0.341   0.70 15.38 ?  126 LEU   A HD22 1 
ATOM   2908 H  HD22 B LEU   A 1 126 ? 15.583 -8.361  0.309   0.30 17.31 ?  126 LEU   A HD22 1 
ATOM   2909 H  HD23 A LEU   A 1 126 ? 15.945 -8.700  1.703   0.70 15.38 ?  126 LEU   A HD23 1 
ATOM   2910 H  HD23 B LEU   A 1 126 ? 15.690 -8.277  1.892   0.30 17.31 ?  126 LEU   A HD23 1 
ATOM   2911 N  N    A LEU   A 1 127 ? 18.911 -6.164  -0.253  0.70 11.52 ?  127 LEU   A N    1 
ATOM   2912 N  N    B LEU   A 1 127 ? 18.858 -5.872  -0.189  0.30 10.94 ?  127 LEU   A N    1 
ATOM   2913 C  CA   A LEU   A 1 127 ? 19.894 -5.670  -1.204  0.70 11.18 ?  127 LEU   A CA   1 
ATOM   2914 C  CA   B LEU   A 1 127 ? 19.846 -5.337  -1.116  0.30 10.78 ?  127 LEU   A CA   1 
ATOM   2915 C  C    A LEU   A 1 127 ? 19.273 -5.495  -2.578  0.70 10.57 ?  127 LEU   A C    1 
ATOM   2916 C  C    B LEU   A 1 127 ? 19.274 -5.216  -2.525  0.30 11.26 ?  127 LEU   A C    1 
ATOM   2917 O  O    A LEU   A 1 127 ? 18.440 -6.294  -3.017  0.70 11.13 ?  127 LEU   A O    1 
ATOM   2918 O  O    B LEU   A 1 127 ? 18.468 -6.037  -2.973  0.30 11.39 ?  127 LEU   A O    1 
ATOM   2919 C  CB   A LEU   A 1 127 ? 21.067 -6.645  -1.296  0.70 12.13 ?  127 LEU   A CB   1 
ATOM   2920 C  CB   B LEU   A 1 127 ? 21.089 -6.226  -1.145  0.30 11.16 ?  127 LEU   A CB   1 
ATOM   2921 C  CG   A LEU   A 1 127 ? 21.855 -6.880  -0.010  0.70 12.45 ?  127 LEU   A CG   1 
ATOM   2922 C  CG   B LEU   A 1 127 ? 21.887 -6.286  0.161   0.30 11.30 ?  127 LEU   A CG   1 
ATOM   2923 C  CD1  A LEU   A 1 127 ? 22.954 -7.880  -0.280  0.70 12.87 ?  127 LEU   A CD1  1 
ATOM   2924 C  CD1  B LEU   A 1 127 ? 23.038 -7.276  0.051   0.30 11.55 ?  127 LEU   A CD1  1 
ATOM   2925 C  CD2  A LEU   A 1 127 ? 22.453 -5.595  0.515   0.70 13.46 ?  127 LEU   A CD2  1 
ATOM   2926 C  CD2  B LEU   A 1 127 ? 22.399 -4.901  0.556   0.30 11.45 ?  127 LEU   A CD2  1 
ATOM   2927 H  H    A LEU   A 1 127 ? 19.077 -6.952  0.047   0.70 13.81 ?  127 LEU   A H    1 
ATOM   2928 H  H    B LEU   A 1 127 ? 19.017 -6.672  0.093   0.30 13.11 ?  127 LEU   A H    1 
ATOM   2929 H  HA   A LEU   A 1 127 ? 20.229 -4.815  -0.909  0.70 13.40 ?  127 LEU   A HA   1 
ATOM   2930 H  HA   B LEU   A 1 127 ? 20.109 -4.454  -0.815  0.30 12.91 ?  127 LEU   A HA   1 
ATOM   2931 H  HB2  A LEU   A 1 127 ? 20.727 -7.506  -1.590  0.70 14.53 ?  127 LEU   A HB2  1 
ATOM   2932 H  HB2  B LEU   A 1 127 ? 20.813 -7.130  -1.363  0.30 13.37 ?  127 LEU   A HB2  1 
ATOM   2933 H  HB3  A LEU   A 1 127 ? 21.692 -6.306  -1.956  0.70 14.53 ?  127 LEU   A HB3  1 
ATOM   2934 H  HB3  B LEU   A 1 127 ? 21.681 -5.892  -1.838  0.30 13.37 ?  127 LEU   A HB3  1 
ATOM   2935 H  HG   A LEU   A 1 127 ? 21.265 -7.251  0.671   0.70 14.91 ?  127 LEU   A HG   1 
ATOM   2936 H  HG   B LEU   A 1 127 ? 21.301 -6.595  0.867   0.30 13.54 ?  127 LEU   A HG   1 
ATOM   2937 H  HD11 A LEU   A 1 127 ? 23.439 -8.054  0.544   0.70 15.43 ?  127 LEU   A HD11 1 
ATOM   2938 H  HD11 B LEU   A 1 127 ? 23.549 -7.256  0.876   0.30 13.84 ?  127 LEU   A HD11 1 
ATOM   2939 H  HD12 A LEU   A 1 127 ? 22.562 -8.707  -0.609  0.70 15.43 ?  127 LEU   A HD12 1 
ATOM   2940 H  HD12 B LEU   A 1 127 ? 22.677 -8.165  -0.093  0.30 13.84 ?  127 LEU   A HD12 1 
ATOM   2941 H  HD13 A LEU   A 1 127 ? 23.557 -7.515  -0.946  0.70 15.43 ?  127 LEU   A HD13 1 
ATOM   2942 H  HD13 B LEU   A 1 127 ? 23.604 -7.022  -0.694  0.30 13.84 ?  127 LEU   A HD13 1 
ATOM   2943 H  HD21 A LEU   A 1 127 ? 23.036 -5.799  1.261   0.70 16.13 ?  127 LEU   A HD21 1 
ATOM   2944 H  HD21 B LEU   A 1 127 ? 23.028 -4.995  1.288   0.30 13.72 ?  127 LEU   A HD21 1 
ATOM   2945 H  HD22 A LEU   A 1 127 ? 22.963 -5.176  -0.199  0.70 16.13 ?  127 LEU   A HD22 1 
ATOM   2946 H  HD22 B LEU   A 1 127 ? 22.837 -4.496  -0.208  0.30 13.72 ?  127 LEU   A HD22 1 
ATOM   2947 H  HD23 A LEU   A 1 127 ? 21.739 -5.007  0.799   0.70 16.13 ?  127 LEU   A HD23 1 
ATOM   2948 H  HD23 B LEU   A 1 127 ? 21.647 -4.354  0.834   0.30 13.72 ?  127 LEU   A HD23 1 
ATOM   2949 N  N    A SER   A 1 128 ? 19.704 -4.441  -3.261  0.70 10.63 ?  128 SER   A N    1 
ATOM   2950 N  N    B SER   A 1 128 ? 19.706 -4.168  -3.222  0.30 11.92 ?  128 SER   A N    1 
ATOM   2951 C  CA   A SER   A 1 128 ? 19.293 -4.064  -4.603  0.70 10.42 ?  128 SER   A CA   1 
ATOM   2952 C  CA   B SER   A 1 128 ? 19.384 -3.860  -4.613  0.30 12.64 ?  128 SER   A CA   1 
ATOM   2953 C  C    A SER   A 1 128 ? 17.840 -3.597  -4.685  0.70 10.71 ?  128 SER   A C    1 
ATOM   2954 C  C    B SER   A 1 128 ? 17.920 -3.514  -4.862  0.30 13.40 ?  128 SER   A C    1 
ATOM   2955 O  O    A SER   A 1 128 ? 17.387 -3.273  -5.780  0.70 12.63 ?  128 SER   A O    1 
ATOM   2956 O  O    B SER   A 1 128 ? 17.566 -3.216  -6.008  0.30 13.40 ?  128 SER   A O    1 
ATOM   2957 C  CB   A SER   A 1 128 ? 19.604 -5.131  -5.665  0.70 10.86 ?  128 SER   A CB   1 
ATOM   2958 C  CB   B SER   A 1 128 ? 19.804 -4.965  -5.592  0.30 12.19 ?  128 SER   A CB   1 
ATOM   2959 O  OG   A SER   A 1 128 ? 21.004 -5.362  -5.750  0.70 11.55 ?  128 SER   A OG   1 
ATOM   2960 O  OG   B SER   A 1 128 ? 21.214 -5.096  -5.630  0.30 11.94 ?  128 SER   A OG   1 
ATOM   2961 H  H    A SER   A 1 128 ? 20.299 -3.902  -2.943  0.70 12.74 ?  128 SER   A H    1 
ATOM   2962 H  H    B SER   A 1 128 ? 20.245 -3.588  -2.882  0.30 14.28 ?  128 SER   A H    1 
ATOM   2963 H  HA   A SER   A 1 128 ? 19.819 -3.292  -4.844  0.70 12.49 ?  128 SER   A HA   1 
ATOM   2964 H  HA   B SER   A 1 128 ? 19.896 -3.075  -4.850  0.30 15.14 ?  128 SER   A HA   1 
ATOM   2965 H  HB2  A SER   A 1 128 ? 19.157 -5.955  -5.434  0.70 13.02 ?  128 SER   A HB2  1 
ATOM   2966 H  HB2  B SER   A 1 128 ? 19.412 -5.803  -5.309  0.30 14.61 ?  128 SER   A HB2  1 
ATOM   2967 H  HB3  A SER   A 1 128 ? 19.291 -4.812  -6.530  0.70 13.02 ?  128 SER   A HB3  1 
ATOM   2968 H  HB3  B SER   A 1 128 ? 19.480 -4.731  -6.480  0.30 14.61 ?  128 SER   A HB3  1 
ATOM   2969 H  HG   A SER   A 1 128 ? 21.406 -4.646  -5.939  0.70 13.83 ?  128 SER   A HG   1 
ATOM   2970 H  HG   B SER   A 1 128 ? 21.556 -4.370  -5.877  0.30 14.30 ?  128 SER   A HG   1 
ATOM   2971 N  N    A ALA   A 1 129 ? 17.117 -3.517  -3.563  0.70 11.05 ?  129 ALA   A N    1 
ATOM   2972 N  N    B ALA   A 1 129 ? 17.065 -3.525  -3.841  0.30 15.06 ?  129 ALA   A N    1 
ATOM   2973 C  CA   A ALA   A 1 129 ? 15.746 -3.023  -3.569  0.70 11.06 ?  129 ALA   A CA   1 
ATOM   2974 C  CA   B ALA   A 1 129 ? 15.631 -3.353  -4.039  0.30 16.76 ?  129 ALA   A CA   1 
ATOM   2975 C  C    A ALA   A 1 129 ? 15.736 -1.495  -3.536  0.70 10.47 ?  129 ALA   A C    1 
ATOM   2976 C  C    B ALA   A 1 129 ? 15.161 -1.913  -3.906  0.30 18.71 ?  129 ALA   A C    1 
ATOM   2977 O  O    A ALA   A 1 129 ? 16.782 -0.839  -3.600  0.70 10.30 ?  129 ALA   A O    1 
ATOM   2978 O  O    B ALA   A 1 129 ? 13.955 -1.663  -4.008  0.30 19.20 ?  129 ALA   A O    1 
ATOM   2979 C  CB   A ALA   A 1 129 ? 14.948 -3.632  -2.413  0.70 12.51 ?  129 ALA   A CB   1 
ATOM   2980 C  CB   B ALA   A 1 129 ? 14.854 -4.228  -3.053  0.30 16.40 ?  129 ALA   A CB   1 
ATOM   2981 H  H    A ALA   A 1 129 ? 17.409 -3.741  -2.774  0.70 13.24 ?  129 ALA   A H    1 
ATOM   2982 H  H    B ALA   A 1 129 ? 17.291 -3.633  -3.017  0.30 18.05 ?  129 ALA   A H    1 
ATOM   2983 H  HA   A ALA   A 1 129 ? 15.327 -3.302  -4.387  0.70 13.26 ?  129 ALA   A HA   1 
ATOM   2984 H  HA   B ALA   A 1 129 ? 15.407 -3.642  -4.932  0.30 20.10 ?  129 ALA   A HA   1 
ATOM   2985 H  HB1  A ALA   A 1 129 ? 14.038 -3.295  -2.443  0.70 14.99 ?  129 ALA   A HB1  1 
ATOM   2986 H  HB1  B ALA   A 1 129 ? 13.906 -4.054  -3.159  0.30 19.66 ?  129 ALA   A HB1  1 
ATOM   2987 H  HB2  A ALA   A 1 129 ? 14.946 -4.598  -2.501  0.70 14.99 ?  129 ALA   A HB2  1 
ATOM   2988 H  HB2  B ALA   A 1 129 ? 15.043 -5.159  -3.245  0.30 19.66 ?  129 ALA   A HB2  1 
ATOM   2989 H  HB3  A ALA   A 1 129 ? 15.361 -3.381  -1.567  0.70 14.99 ?  129 ALA   A HB3  1 
ATOM   2990 H  HB3  B ALA   A 1 129 ? 15.127 -4.010  -2.150  0.30 19.66 ?  129 ALA   A HB3  1 
ATOM   2991 N  N    A GLY   A 1 130 ? 14.537 -0.922  -3.468  0.70 10.61 ?  130 GLY   A N    1 
ATOM   2992 N  N    B GLY   A 1 130 ? 16.063 -0.966  -3.687  0.30 20.30 ?  130 GLY   A N    1 
ATOM   2993 C  CA   A GLY   A 1 130 ? 14.426 0.528   -3.401  0.70 11.34 ?  130 GLY   A CA   1 
ATOM   2994 C  CA   B GLY   A 1 130 ? 15.646 0.413   -3.566  0.30 21.62 ?  130 GLY   A CA   1 
ATOM   2995 C  C    A GLY   A 1 130 ? 15.025 1.164   -4.635  0.70 10.85 ?  130 GLY   A C    1 
ATOM   2996 C  C    B GLY   A 1 130 ? 15.880 1.199   -4.834  0.30 22.63 ?  130 GLY   A C    1 
ATOM   2997 O  O    A GLY   A 1 130 ? 14.789 0.718   -5.763  0.70 11.40 ?  130 GLY   A O    1 
ATOM   2998 O  O    B GLY   A 1 130 ? 15.257 0.950   -5.871  0.30 22.79 ?  130 GLY   A O    1 
ATOM   2999 H  H    A GLY   A 1 130 ? 13.787 -1.349  -3.466  0.70 12.71 ?  130 GLY   A H    1 
ATOM   3000 H  H    B GLY   A 1 130 ? 16.914 -1.092  -3.607  0.30 24.34 ?  130 GLY   A H    1 
ATOM   3001 H  HA2  A GLY   A 1 130 ? 13.488 0.777   -3.332  0.70 13.59 ?  130 GLY   A HA2  1 
ATOM   3002 H  HA2  B GLY   A 1 130 ? 14.704 0.464   -3.356  0.30 25.92 ?  130 GLY   A HA2  1 
ATOM   3003 H  HA3  A GLY   A 1 130 ? 14.896 0.855   -2.625  0.70 13.59 ?  130 GLY   A HA3  1 
ATOM   3004 H  HA3  B GLY   A 1 130 ? 16.147 0.833   -2.851  0.30 25.92 ?  130 GLY   A HA3  1 
ATOM   3005 N  N    A ILE   A 1 131 ? 15.824 2.218   -4.418  0.70 11.03 ?  131 ILE   A N    1 
ATOM   3006 N  N    B ILE   A 1 131 ? 16.795 2.163   -4.742  0.30 23.15 ?  131 ILE   A N    1 
ATOM   3007 C  CA   A ILE   A 1 131 ? 16.393 2.995   -5.516  0.70 10.84 ?  131 ILE   A CA   1 
ATOM   3008 C  CA   B ILE   A 1 131 ? 17.169 2.984   -5.890  0.30 23.24 ?  131 ILE   A CA   1 
ATOM   3009 C  C    A ILE   A 1 131 ? 17.430 2.229   -6.325  0.70 10.64 ?  131 ILE   A C    1 
ATOM   3010 C  C    B ILE   A 1 131 ? 17.938 2.182   -6.931  0.30 22.46 ?  131 ILE   A C    1 
ATOM   3011 O  O    A ILE   A 1 131 ? 17.850 2.730   -7.377  0.70 11.31 ?  131 ILE   A O    1 
ATOM   3012 O  O    B ILE   A 1 131 ? 18.080 2.642   -8.070  0.30 22.31 ?  131 ILE   A O    1 
ATOM   3013 C  CB   A ILE   A 1 131 ? 16.965 4.352   -5.049  0.70 12.68 ?  131 ILE   A CB   1 
ATOM   3014 C  CB   B ILE   A 1 131 ? 17.886 4.275   -5.417  0.30 23.96 ?  131 ILE   A CB   1 
ATOM   3015 C  CG1  A ILE   A 1 131 ? 18.203 4.168   -4.162  0.70 14.13 ?  131 ILE   A CG1  1 
ATOM   3016 C  CG1  B ILE   A 1 131 ? 19.185 4.538   -6.192  0.30 24.55 ?  131 ILE   A CG1  1 
ATOM   3017 C  CG2  A ILE   A 1 131 ? 15.889 5.163   -4.343  0.70 13.82 ?  131 ILE   A CG2  1 
ATOM   3018 C  CG2  B ILE   A 1 131 ? 18.198 4.211   -3.926  0.30 24.03 ?  131 ILE   A CG2  1 
ATOM   3019 C  CD1  A ILE   A 1 131 ? 18.855 5.490   -3.735  0.70 15.96 ?  131 ILE   A CD1  1 
ATOM   3020 C  CD1  B ILE   A 1 131 ? 20.004 5.685   -5.625  0.30 24.96 ?  131 ILE   A CD1  1 
ATOM   3021 H  H    A ILE   A 1 131 ? 16.033 2.500   -3.635  0.70 13.22 ?  131 ILE   A H    1 
ATOM   3022 H  H    B ILE   A 1 131 ? 17.212 2.325   -4.013  0.30 27.76 ?  131 ILE   A H    1 
ATOM   3023 H  HA   A ILE   A 1 131 ? 15.669 3.199   -6.125  0.70 12.99 ?  131 ILE   A HA   1 
ATOM   3024 H  HA   B ILE   A 1 131 ? 16.351 3.280   -6.322  0.30 27.87 ?  131 ILE   A HA   1 
ATOM   3025 H  HB   A ILE   A 1 131 ? 17.232 4.842   -5.839  0.70 15.20 ?  131 ILE   A HB   1 
ATOM   3026 H  HB   B ILE   A 1 131 ? 17.289 5.029   -5.565  0.30 28.73 ?  131 ILE   A HB   1 
ATOM   3027 H  HG12 A ILE   A 1 131 ? 17.946 3.690   -3.360  0.70 16.94 ?  131 ILE   A HG12 1 
ATOM   3028 H  HG12 B ILE   A 1 131 ? 19.749 3.754   -6.150  0.30 29.44 ?  131 ILE   A HG12 1 
ATOM   3029 H  HG13 A ILE   A 1 131 ? 18.869 3.659   -4.651  0.70 16.94 ?  131 ILE   A HG13 1 
ATOM   3030 H  HG13 B ILE   A 1 131 ? 18.974 4.754   -7.113  0.30 29.44 ?  131 ILE   A HG13 1 
ATOM   3031 H  HG21 A ILE   A 1 131 ? 16.212 6.066   -4.208  0.70 16.56 ?  131 ILE   A HG21 1 
ATOM   3032 H  HG21 B ILE   A 1 131 ? 18.631 5.017   -3.651  0.30 28.82 ?  131 ILE   A HG21 1 
ATOM   3033 H  HG22 A ILE   A 1 131 ? 15.091 5.176   -4.895  0.70 16.56 ?  131 ILE   A HG22 1 
ATOM   3034 H  HG22 B ILE   A 1 131 ? 17.367 4.120   -3.434  0.30 28.82 ?  131 ILE   A HG22 1 
ATOM   3035 H  HG23 A ILE   A 1 131 ? 15.691 4.749   -3.488  0.70 16.56 ?  131 ILE   A HG23 1 
ATOM   3036 H  HG23 B ILE   A 1 131 ? 18.779 3.446   -3.763  0.30 28.82 ?  131 ILE   A HG23 1 
ATOM   3037 H  HD11 A ILE   A 1 131 ? 19.690 5.298   -3.279  0.70 19.13 ?  131 ILE   A HD11 1 
ATOM   3038 H  HD11 B ILE   A 1 131 ? 20.621 5.997   -6.300  0.30 29.93 ?  131 ILE   A HD11 1 
ATOM   3039 H  HD12 A ILE   A 1 131 ? 19.028 6.029   -4.524  0.70 19.13 ?  131 ILE   A HD12 1 
ATOM   3040 H  HD12 B ILE   A 1 131 ? 19.404 6.402   -5.364  0.30 29.93 ?  131 ILE   A HD12 1 
ATOM   3041 H  HD13 A ILE   A 1 131 ? 18.254 5.964   -3.138  0.70 19.13 ?  131 ILE   A HD13 1 
ATOM   3042 H  HD13 B ILE   A 1 131 ? 20.495 5.368   -4.848  0.30 29.93 ?  131 ILE   A HD13 1 
ATOM   3043 N  N    A PHE   A 1 132 ? 17.850 1.032   -5.879  0.70 10.71 ?  132 PHE   A N    1 
ATOM   3044 N  N    B PHE   A 1 132 ? 18.430 0.989   -6.574  0.30 21.95 ?  132 PHE   A N    1 
ATOM   3045 C  CA   A PHE   A 1 132 ? 18.718 0.192   -6.699  0.70 10.69 ?  132 PHE   A CA   1 
ATOM   3046 C  CA   B PHE   A 1 132 ? 19.116 0.140   -7.547  0.30 21.36 ?  132 PHE   A CA   1 
ATOM   3047 C  C    A PHE   A 1 132 ? 17.952 -0.569  -7.777  0.70 11.41 ?  132 PHE   A C    1 
ATOM   3048 C  C    B PHE   A 1 132 ? 18.171 -0.587  -8.492  0.30 20.03 ?  132 PHE   A C    1 
ATOM   3049 O  O    A PHE   A 1 132 ? 18.580 -1.200  -8.635  0.70 12.06 ?  132 PHE   A O    1 
ATOM   3050 O  O    B PHE   A 1 132 ? 18.629 -1.124  -9.506  0.30 20.31 ?  132 PHE   A O    1 
ATOM   3051 C  CB   A PHE   A 1 132 ? 19.534 -0.781  -5.841  0.70 10.35 ?  132 PHE   A CB   1 
ATOM   3052 C  CB   B PHE   A 1 132 ? 20.039 -0.868  -6.851  0.30 22.20 ?  132 PHE   A CB   1 
ATOM   3053 C  CG   A PHE   A 1 132 ? 20.756 -0.170  -5.179  0.70 10.06 ?  132 PHE   A CG   1 
ATOM   3054 C  CG   B PHE   A 1 132 ? 21.368 -0.291  -6.443  0.30 22.92 ?  132 PHE   A CG   1 
ATOM   3055 C  CD1  A PHE   A 1 132 ? 20.633 0.845   -4.246  0.70 10.87 ?  132 PHE   A CD1  1 
ATOM   3056 C  CD1  B PHE   A 1 132 ? 21.739 0.983   -6.850  0.30 23.21 ?  132 PHE   A CD1  1 
ATOM   3057 C  CD2  A PHE   A 1 132 ? 22.021 -0.669  -5.442  0.70 10.98 ?  132 PHE   A CD2  1 
ATOM   3058 C  CD2  B PHE   A 1 132 ? 22.248 -1.019  -5.664  0.30 23.15 ?  132 PHE   A CD2  1 
ATOM   3059 C  CE1  A PHE   A 1 132 ? 21.758 1.369   -3.622  0.70 11.34 ?  132 PHE   A CE1  1 
ATOM   3060 C  CE1  B PHE   A 1 132 ? 22.946 1.518   -6.491  0.30 23.31 ?  132 PHE   A CE1  1 
ATOM   3061 C  CE2  A PHE   A 1 132 ? 23.141 -0.149  -4.817  0.70 11.51 ?  132 PHE   A CE2  1 
ATOM   3062 C  CE2  B PHE   A 1 132 ? 23.468 -0.483  -5.298  0.30 23.16 ?  132 PHE   A CE2  1 
ATOM   3063 C  CZ   A PHE   A 1 132 ? 23.005 0.871   -3.907  0.70 11.27 ?  132 PHE   A CZ   1 
ATOM   3064 C  CZ   B PHE   A 1 132 ? 23.815 0.788   -5.713  0.30 23.16 ?  132 PHE   A CZ   1 
ATOM   3065 H  H    A PHE   A 1 132 ? 17.644 0.691   -5.110  0.70 12.83 ?  132 PHE   A H    1 
ATOM   3066 H  H    B PHE   A 1 132 ? 18.398 0.668   -5.770  0.30 26.31 ?  132 PHE   A H    1 
ATOM   3067 H  HA   A PHE   A 1 132 ? 19.347 0.770   -7.150  0.70 12.81 ?  132 PHE   A HA   1 
ATOM   3068 H  HA   B PHE   A 1 132 ? 19.648 0.712   -8.114  0.30 25.61 ?  132 PHE   A HA   1 
ATOM   3069 H  HB2  A PHE   A 1 132 ? 18.966 -1.132  -5.137  0.70 12.40 ?  132 PHE   A HB2  1 
ATOM   3070 H  HB2  B PHE   A 1 132 ? 19.602 -1.203  -6.054  0.30 26.61 ?  132 PHE   A HB2  1 
ATOM   3071 H  HB3  A PHE   A 1 132 ? 19.841 -1.511  -6.403  0.70 12.40 ?  132 PHE   A HB3  1 
ATOM   3072 H  HB3  B PHE   A 1 132 ? 20.207 -1.606  -7.459  0.30 26.61 ?  132 PHE   A HB3  1 
ATOM   3073 H  HD1  A PHE   A 1 132 ? 19.795 1.185   -4.038  0.70 13.02 ?  132 PHE   A HD1  1 
ATOM   3074 H  HD1  B PHE   A 1 132 ? 21.158 1.484   -7.379  0.30 27.83 ?  132 PHE   A HD1  1 
ATOM   3075 H  HD2  A PHE   A 1 132 ? 22.122 -1.359  -6.057  0.70 13.15 ?  132 PHE   A HD2  1 
ATOM   3076 H  HD2  B PHE   A 1 132 ? 22.018 -1.877  -5.383  0.30 27.76 ?  132 PHE   A HD2  1 
ATOM   3077 H  HE1  A PHE   A 1 132 ? 21.666 2.061   -3.001  0.70 13.59 ?  132 PHE   A HE1  1 
ATOM   3078 H  HE1  B PHE   A 1 132 ? 23.170 2.374   -6.777  0.30 27.95 ?  132 PHE   A HE1  1 
ATOM   3079 H  HE2  A PHE   A 1 132 ? 23.983 -0.481  -5.020  0.70 13.79 ?  132 PHE   A HE2  1 
ATOM   3080 H  HE2  B PHE   A 1 132 ? 24.055 -0.976  -4.773  0.30 27.77 ?  132 PHE   A HE2  1 
ATOM   3081 H  HZ   A PHE   A 1 132 ? 23.754 1.231   -3.493  0.70 13.50 ?  132 PHE   A HZ   1 
ATOM   3082 H  HZ   B PHE   A 1 132 ? 24.633 1.153   -5.470  0.30 27.77 ?  132 PHE   A HZ   1 
ATOM   3083 N  N    A GLY   A 1 133 ? 16.618 -0.532  -7.751  0.70 11.61 ?  133 GLY   A N    1 
ATOM   3084 N  N    B GLY   A 1 133 ? 16.884 -0.642  -8.177  0.30 18.57 ?  133 GLY   A N    1 
ATOM   3085 C  CA   A GLY   A 1 133 ? 15.820 -0.883  -8.909  0.70 13.08 ?  133 GLY   A CA   1 
ATOM   3086 C  CA   B GLY   A 1 133 ? 15.872 -0.973  -9.156  0.30 17.62 ?  133 GLY   A CA   1 
ATOM   3087 C  C    A GLY   A 1 133 ? 15.512 -2.346  -9.135  0.70 13.58 ?  133 GLY   A C    1 
ATOM   3088 C  C    B GLY   A 1 133 ? 15.421 -2.418  -9.202  0.30 16.69 ?  133 GLY   A C    1 
ATOM   3089 O  O    A GLY   A 1 133 ? 14.925 -2.663  -10.175 0.70 14.97 ?  133 GLY   A O    1 
ATOM   3090 O  O    B GLY   A 1 133 ? 14.498 -2.728  -9.966  0.30 16.83 ?  133 GLY   A O    1 
ATOM   3091 H  H    A GLY   A 1 133 ? 16.149 -0.293  -7.065  0.70 13.91 ?  133 GLY   A H    1 
ATOM   3092 H  H    B GLY   A 1 133 ? 16.586 -0.503  -7.384  0.30 22.26 ?  133 GLY   A H    1 
ATOM   3093 H  HA2  A GLY   A 1 133 ? 14.962 -0.431  -8.840  0.70 15.68 ?  133 GLY   A HA2  1 
ATOM   3094 H  HA2  B GLY   A 1 133 ? 15.095 -0.426  -8.975  0.30 21.13 ?  133 GLY   A HA2  1 
ATOM   3095 H  HA3  A GLY   A 1 133 ? 16.263 -0.545  -9.702  0.70 15.68 ?  133 GLY   A HA3  1 
ATOM   3096 H  HA3  B GLY   A 1 133 ? 16.206 -0.729  -10.036 0.30 21.13 ?  133 GLY   A HA3  1 
ATOM   3097 N  N    A ALA   A 1 134 ? 15.855 -3.242  -8.210  0.70 13.37 ?  134 ALA   A N    1 
ATOM   3098 N  N    B ALA   A 1 134 ? 16.022 -3.306  -8.416  0.30 16.04 ?  134 ALA   A N    1 
ATOM   3099 C  CA   A ALA   A 1 134 ? 15.526 -4.647  -8.401  0.70 14.65 ?  134 ALA   A CA   1 
ATOM   3100 C  CA   B ALA   A 1 134 ? 15.651 -4.711  -8.485  0.30 15.77 ?  134 ALA   A CA   1 
ATOM   3101 C  C    A ALA   A 1 134 ? 14.184 -4.981  -7.751  0.70 15.04 ?  134 ALA   A C    1 
ATOM   3102 C  C    B ALA   A 1 134 ? 14.294 -4.950  -7.826  0.30 15.65 ?  134 ALA   A C    1 
ATOM   3103 O  O    A ALA   A 1 134 ? 13.638 -4.217  -6.951  0.70 16.20 ?  134 ALA   A O    1 
ATOM   3104 O  O    B ALA   A 1 134 ? 13.786 -4.126  -7.059  0.30 15.98 ?  134 ALA   A O    1 
ATOM   3105 C  CB   A ALA   A 1 134 ? 16.620 -5.555  -7.845  0.70 15.67 ?  134 ALA   A CB   1 
ATOM   3106 C  CB   B ALA   A 1 134 ? 16.709 -5.584  -7.813  0.30 16.02 ?  134 ALA   A CB   1 
ATOM   3107 H  H    A ALA   A 1 134 ? 16.262 -3.057  -7.469  0.70 16.03 ?  134 ALA   A H    1 
ATOM   3108 H  H    B ALA   A 1 134 ? 16.637 -3.120  -7.843  0.30 19.23 ?  134 ALA   A H    1 
ATOM   3109 H  HA   A ALA   A 1 134 ? 15.449 -4.818  -9.352  0.70 17.56 ?  134 ALA   A HA   1 
ATOM   3110 H  HA   B ALA   A 1 134 ? 15.584 -4.973  -9.416  0.30 18.90 ?  134 ALA   A HA   1 
ATOM   3111 H  HB1  A ALA   A 1 134 ? 16.372 -6.475  -8.015  0.70 18.78 ?  134 ALA   A HB1  1 
ATOM   3112 H  HB1  B ALA   A 1 134 ? 16.452 -6.514  -7.911  0.30 19.20 ?  134 ALA   A HB1  1 
ATOM   3113 H  HB2  A ALA   A 1 134 ? 17.454 -5.345  -8.292  0.70 18.78 ?  134 ALA   A HB2  1 
ATOM   3114 H  HB2  B ALA   A 1 134 ? 17.564 -5.428  -8.242  0.30 19.20 ?  134 ALA   A HB2  1 
ATOM   3115 H  HB3  A ALA   A 1 134 ? 16.702 -5.399  -6.894  0.70 18.78 ?  134 ALA   A HB3  1 
ATOM   3116 H  HB3  B ALA   A 1 134 ? 16.760 -5.349  -6.875  0.30 19.20 ?  134 ALA   A HB3  1 
ATOM   3117 N  N    A ASP   A 1 135 ? 13.655 -6.151  -8.113  0.70 15.41 ?  135 ASP   A N    1 
ATOM   3118 N  N    B ASP   A 1 135 ? 13.709 -6.104  -8.140  0.30 15.93 ?  135 ASP   A N    1 
ATOM   3119 C  CA   A ASP   A 1 135 ? 12.410 -6.657  -7.543  0.70 16.23 ?  135 ASP   A CA   1 
ATOM   3120 C  CA   B ASP   A 1 135 ? 12.420 -6.485  -7.581  0.30 16.40 ?  135 ASP   A CA   1 
ATOM   3121 C  C    A ASP   A 1 135 ? 12.662 -7.083  -6.102  0.70 15.60 ?  135 ASP   A C    1 
ATOM   3122 C  C    B ASP   A 1 135 ? 12.612 -6.947  -6.141  0.30 16.06 ?  135 ASP   A C    1 
ATOM   3123 O  O    A ASP   A 1 135 ? 13.461 -7.998  -5.872  0.70 15.46 ?  135 ASP   A O    1 
ATOM   3124 O  O    B ASP   A 1 135 ? 13.369 -7.895  -5.905  0.30 15.83 ?  135 ASP   A O    1 
ATOM   3125 C  CB   A ASP   A 1 135 ? 11.959 -7.857  -8.377  0.70 18.88 ?  135 ASP   A CB   1 
ATOM   3126 C  CB   B ASP   A 1 135 ? 11.822 -7.618  -8.401  0.30 17.61 ?  135 ASP   A CB   1 
ATOM   3127 C  CG   A ASP   A 1 135 ? 10.672 -8.497  -7.869  0.70 20.99 ?  135 ASP   A CG   1 
ATOM   3128 C  CG   B ASP   A 1 135 ? 10.359 -7.869  -8.071  0.30 18.96 ?  135 ASP   A CG   1 
ATOM   3129 O  OD1  A ASP   A 1 135 ? 10.106 -8.036  -6.855  0.70 21.14 ?  135 ASP   A OD1  1 
ATOM   3130 O  OD1  B ASP   A 1 135 ? 9.921  -7.468  -6.971  0.30 19.41 ?  135 ASP   A OD1  1 
ATOM   3131 O  OD2  A ASP   A 1 135 ? 10.216 -9.471  -8.506  0.70 23.54 -1 135 ASP   A OD2  1 
ATOM   3132 O  OD2  B ASP   A 1 135 ? 9.650  -8.478  -8.901  0.30 19.34 -1 135 ASP   A OD2  1 
ATOM   3133 H  H    A ASP   A 1 135 ? 14.005 -6.677  -8.695  0.70 18.47 ?  135 ASP   A H    1 
ATOM   3134 H  H    B ASP   A 1 135 ? 14.039 -6.685  -8.680  0.30 19.09 ?  135 ASP   A H    1 
ATOM   3135 H  HA   A ASP   A 1 135 ? 11.724 -5.970  -7.582  0.70 19.46 ?  135 ASP   A HA   1 
ATOM   3136 H  HA   B ASP   A 1 135 ? 11.811 -5.730  -7.616  0.30 19.66 ?  135 ASP   A HA   1 
ATOM   3137 H  HB2  A ASP   A 1 135 ? 11.806 -7.566  -9.288  0.70 22.64 ?  135 ASP   A HB2  1 
ATOM   3138 H  HB2  B ASP   A 1 135 ? 11.923 -7.407  -9.346  0.30 21.12 ?  135 ASP   A HB2  1 
ATOM   3139 H  HB3  A ASP   A 1 135 ? 12.655 -8.531  -8.355  0.70 22.64 ?  135 ASP   A HB3  1 
ATOM   3140 H  HB3  B ASP   A 1 135 ? 12.294 -8.440  -8.198  0.30 21.12 ?  135 ASP   A HB3  1 
ATOM   3141 N  N    A PRO   A 1 136 ? 12.026 -6.454  -5.111  0.70 15.61 ?  136 PRO   A N    1 
ATOM   3142 N  N    B PRO   A 1 136 ? 11.956 -6.322  -5.160  0.30 16.22 ?  136 PRO   A N    1 
ATOM   3143 C  CA   A PRO   A 1 136 ? 12.277 -6.852  -3.715  0.70 15.30 ?  136 PRO   A CA   1 
ATOM   3144 C  CA   B PRO   A 1 136 ? 12.176 -6.732  -3.761  0.30 16.14 ?  136 PRO   A CA   1 
ATOM   3145 C  C    A PRO   A 1 136 ? 11.857 -8.276  -3.390  0.70 14.05 ?  136 PRO   A C    1 
ATOM   3146 C  C    B PRO   A 1 136 ? 11.791 -8.175  -3.472  0.30 15.67 ?  136 PRO   A C    1 
ATOM   3147 O  O    A PRO   A 1 136 ? 12.452 -8.894  -2.501  0.70 13.35 ?  136 PRO   A O    1 
ATOM   3148 O  O    B PRO   A 1 136 ? 12.395 -8.799  -2.592  0.30 15.15 ?  136 PRO   A O    1 
ATOM   3149 C  CB   A PRO   A 1 136 ? 11.483 -5.816  -2.906  0.70 16.36 ?  136 PRO   A CB   1 
ATOM   3150 C  CB   B PRO   A 1 136 ? 11.325 -5.733  -2.963  0.30 16.67 ?  136 PRO   A CB   1 
ATOM   3151 C  CG   A PRO   A 1 136 ? 10.433 -5.309  -3.856  0.70 17.02 ?  136 PRO   A CG   1 
ATOM   3152 C  CG   B PRO   A 1 136 ? 11.138 -4.568  -3.884  0.30 17.01 ?  136 PRO   A CG   1 
ATOM   3153 C  CD   A PRO   A 1 136 ? 11.061 -5.345  -5.213  0.70 16.90 ?  136 PRO   A CD   1 
ATOM   3154 C  CD   B PRO   A 1 136 ? 11.076 -5.145  -5.256  0.30 17.00 ?  136 PRO   A CD   1 
ATOM   3155 H  HA   A PRO   A 1 136 ? 13.221 -6.755  -3.505  0.70 18.34 ?  136 PRO   A HA   1 
ATOM   3156 H  HA   B PRO   A 1 136 ? 13.106 -6.603  -3.518  0.30 19.35 ?  136 PRO   A HA   1 
ATOM   3157 H  HB2  A PRO   A 1 136 ? 11.075 -6.246  -2.137  0.70 19.61 ?  136 PRO   A HB2  1 
ATOM   3158 H  HB2  B PRO   A 1 136 ? 10.472 -6.137  -2.743  0.30 19.98 ?  136 PRO   A HB2  1 
ATOM   3159 H  HB3  A PRO   A 1 136 ? 12.075 -5.100  -2.626  0.70 19.61 ?  136 PRO   A HB3  1 
ATOM   3160 H  HB3  B PRO   A 1 136 ? 11.795 -5.460  -2.157  0.30 19.98 ?  136 PRO   A HB3  1 
ATOM   3161 H  HG2  A PRO   A 1 136 ? 9.660  -5.891  -3.828  0.70 20.40 ?  136 PRO   A HG2  1 
ATOM   3162 H  HG2  B PRO   A 1 136 ? 10.309 -4.114  -3.671  0.30 20.39 ?  136 PRO   A HG2  1 
ATOM   3163 H  HG3  A PRO   A 1 136 ? 10.193 -4.402  -3.621  0.70 20.40 ?  136 PRO   A HG3  1 
ATOM   3164 H  HG3  B PRO   A 1 136 ? 11.887 -3.957  -3.806  0.30 20.39 ?  136 PRO   A HG3  1 
ATOM   3165 H  HD2  A PRO   A 1 136 ? 10.392 -5.544  -5.889  0.70 20.26 ?  136 PRO   A HD2  1 
ATOM   3166 H  HD2  B PRO   A 1 136 ? 10.168 -5.417  -5.473  0.30 20.38 ?  136 PRO   A HD2  1 
ATOM   3167 H  HD3  A PRO   A 1 136 ? 11.520 -4.512  -5.403  0.70 20.26 ?  136 PRO   A HD3  1 
ATOM   3168 H  HD3  B PRO   A 1 136 ? 11.422 -4.510  -5.902  0.30 20.38 ?  136 PRO   A HD3  1 
ATOM   3169 N  N    A ILE   A 1 137 ? 10.824 -8.803  -4.051  0.70 14.36 ?  137 ILE   A N    1 
ATOM   3170 N  N    B ILE   A 1 137 ? 10.797 -8.724  -4.176  0.30 15.91 ?  137 ILE   A N    1 
ATOM   3171 C  CA   A ILE   A 1 137 ? 10.445 -10.197 -3.837  0.70 14.45 ?  137 ILE   A CA   1 
ATOM   3172 C  CA   B ILE   A 1 137 ? 10.432 -10.125 -3.974  0.30 15.99 ?  137 ILE   A CA   1 
ATOM   3173 C  C    A ILE   A 1 137 ? 11.594 -11.108 -4.241  0.70 13.71 ?  137 ILE   A C    1 
ATOM   3174 C  C    B ILE   A 1 137 ? 11.603 -11.027 -4.334  0.30 15.47 ?  137 ILE   A C    1 
ATOM   3175 O  O    A ILE   A 1 137 ? 11.925 -12.074 -3.541  0.70 14.24 ?  137 ILE   A O    1 
ATOM   3176 O  O    B ILE   A 1 137 ? 11.907 -11.996 -3.626  0.30 15.72 ?  137 ILE   A O    1 
ATOM   3177 C  CB   A ILE   A 1 137 ? 9.146  -10.524 -4.600  0.70 16.26 ?  137 ILE   A CB   1 
ATOM   3178 C  CB   B ILE   A 1 137 ? 9.168  -10.478 -4.785  0.30 17.18 ?  137 ILE   A CB   1 
ATOM   3179 C  CG1  A ILE   A 1 137 ? 8.004  -9.590  -4.167  0.70 18.09 ?  137 ILE   A CG1  1 
ATOM   3180 C  CG1  B ILE   A 1 137 ? 7.922  -9.838  -4.165  0.30 18.27 ?  137 ILE   A CG1  1 
ATOM   3181 C  CG2  A ILE   A 1 137 ? 8.758  -11.993 -4.400  0.70 16.67 ?  137 ILE   A CG2  1 
ATOM   3182 C  CG2  B ILE   A 1 137 ? 8.994  -11.994 -4.885  0.30 17.14 ?  137 ILE   A CG2  1 
ATOM   3183 C  CD1  A ILE   A 1 137 ? 6.702  -9.824  -4.916  0.70 19.31 ?  137 ILE   A CD1  1 
ATOM   3184 C  CD1  B ILE   A 1 137 ? 7.676  -8.411  -4.607  0.30 18.98 ?  137 ILE   A CD1  1 
ATOM   3185 H  H    A ILE   A 1 137 ? 10.332 -8.378  -4.614  0.70 17.22 ?  137 ILE   A H    1 
ATOM   3186 H  H    B ILE   A 1 137 ? 10.335 -8.311  -4.768  0.30 19.07 ?  137 ILE   A H    1 
ATOM   3187 H  HA   A ILE   A 1 137 ? 10.280 -10.338 -2.894  0.70 17.32 ?  137 ILE   A HA   1 
ATOM   3188 H  HA   B ILE   A 1 137 ? 10.233 -10.263 -3.036  0.30 19.17 ?  137 ILE   A HA   1 
ATOM   3189 H  HB   A ILE   A 1 137 ? 9.304  -10.383 -5.543  0.70 19.49 ?  137 ILE   A HB   1 
ATOM   3190 H  HB   B ILE   A 1 137 ? 9.276  -10.126 -5.682  0.30 20.59 ?  137 ILE   A HB   1 
ATOM   3191 H  HG12 A ILE   A 1 137 ? 7.835  -9.719  -3.221  0.70 21.69 ?  137 ILE   A HG12 1 
ATOM   3192 H  HG12 B ILE   A 1 137 ? 7.145  -10.360 -4.413  0.30 21.90 ?  137 ILE   A HG12 1 
ATOM   3193 H  HG13 A ILE   A 1 137 ? 8.276  -8.670  -4.327  0.70 21.69 ?  137 ILE   A HG13 1 
ATOM   3194 H  HG13 B ILE   A 1 137 ? 8.021  -9.834  -3.201  0.30 21.90 ?  137 ILE   A HG13 1 
ATOM   3195 H  HG21 A ILE   A 1 137 ? 7.942  -12.184 -4.884  0.70 19.99 ?  137 ILE   A HG21 1 
ATOM   3196 H  HG21 B ILE   A 1 137 ? 8.091  -12.189 -5.184  0.30 20.55 ?  137 ILE   A HG21 1 
ATOM   3197 H  HG22 A ILE   A 1 137 ? 9.470  -12.556 -4.737  0.70 19.99 ?  137 ILE   A HG22 1 
ATOM   3198 H  HG22 B ILE   A 1 137 ? 9.632  -12.347 -5.524  0.30 20.55 ?  137 ILE   A HG22 1 
ATOM   3199 H  HG23 A ILE   A 1 137 ? 8.626  -12.155 -3.454  0.70 19.99 ?  137 ILE   A HG23 1 
ATOM   3200 H  HG23 B ILE   A 1 137 ? 9.143  -12.387 -4.011  0.30 20.55 ?  137 ILE   A HG23 1 
ATOM   3201 H  HD11 A ILE   A 1 137 ? 6.015  -10.081 -4.283  0.70 23.15 ?  137 ILE   A HD11 1 
ATOM   3202 H  HD11 B ILE   A 1 137 ? 6.791  -8.141  -4.310  0.30 22.75 ?  137 ILE   A HD11 1 
ATOM   3203 H  HD12 A ILE   A 1 137 ? 6.461  -9.003  -5.363  0.70 23.15 ?  137 ILE   A HD12 1 
ATOM   3204 H  HD12 B ILE   A 1 137 ? 8.345  -7.834  -4.212  0.30 22.75 ?  137 ILE   A HD12 1 
ATOM   3205 H  HD13 A ILE   A 1 137 ? 6.829  -10.524 -5.575  0.70 23.15 ?  137 ILE   A HD13 1 
ATOM   3206 H  HD13 B ILE   A 1 137 ? 7.723  -8.366  -5.575  0.30 22.75 ?  137 ILE   A HD13 1 
ATOM   3207 N  N    A HIS   A 1 138 ? 12.232 -10.800 -5.372  0.70 14.43 ?  138 HIS   A N    1 
ATOM   3208 N  N    B HIS   A 1 138 ? 12.275 -10.720 -5.443  0.30 15.30 ?  138 HIS   A N    1 
ATOM   3209 C  CA   A HIS   A 1 138 ? 13.413 -11.545 -5.790  0.70 14.48 ?  138 HIS   A CA   1 
ATOM   3210 C  CA   B HIS   A 1 138 ? 13.437 -11.497 -5.857  0.30 14.68 ?  138 HIS   A CA   1 
ATOM   3211 C  C    A HIS   A 1 138 ? 14.550 -11.390 -4.786  0.70 13.99 ?  138 HIS   A C    1 
ATOM   3212 C  C    B HIS   A 1 138 ? 14.581 -11.368 -4.857  0.30 14.08 ?  138 HIS   A C    1 
ATOM   3213 O  O    A HIS   A 1 138 ? 15.206 -12.371 -4.418  0.70 14.08 ?  138 HIS   A O    1 
ATOM   3214 O  O    B HIS   A 1 138 ? 15.263 -12.353 -4.554  0.30 13.98 ?  138 HIS   A O    1 
ATOM   3215 C  CB   A HIS   A 1 138 ? 13.837 -11.106 -7.190  0.70 15.61 ?  138 HIS   A CB   1 
ATOM   3216 C  CB   B HIS   A 1 138 ? 13.867 -11.048 -7.253  0.30 15.13 ?  138 HIS   A CB   1 
ATOM   3217 C  CG   A HIS   A 1 138 ? 15.088 -11.771 -7.667  0.70 16.50 ?  138 HIS   A CG   1 
ATOM   3218 C  CG   B HIS   A 1 138 ? 15.168 -11.631 -7.700  0.30 15.41 ?  138 HIS   A CG   1 
ATOM   3219 N  ND1  A HIS   A 1 138 ? 15.171 -13.130 -7.887  0.70 17.89 ?  138 HIS   A ND1  1 
ATOM   3220 N  ND1  B HIS   A 1 138 ? 15.322 -12.968 -7.999  0.30 15.95 ?  138 HIS   A ND1  1 
ATOM   3221 C  CD2  A HIS   A 1 138 ? 16.314 -11.269 -7.943  0.70 17.21 ?  138 HIS   A CD2  1 
ATOM   3222 C  CD2  B HIS   A 1 138 ? 16.378 -11.059 -7.897  0.30 15.51 ?  138 HIS   A CD2  1 
ATOM   3223 C  CE1  A HIS   A 1 138 ? 16.391 -13.434 -8.290  0.70 18.39 ?  138 HIS   A CE1  1 
ATOM   3224 C  CE1  B HIS   A 1 138 ? 16.571 -13.194 -8.362  0.30 16.02 ?  138 HIS   A CE1  1 
ATOM   3225 N  NE2  A HIS   A 1 138 ? 17.105 -12.323 -8.333  0.70 17.53 ?  138 HIS   A NE2  1 
ATOM   3226 N  NE2  B HIS   A 1 138 ? 17.233 -12.052 -8.309  0.30 15.81 ?  138 HIS   A NE2  1 
ATOM   3227 H  H    A HIS   A 1 138 ? 11.998 -10.167 -5.915  0.70 17.30 ?  138 HIS   A H    1 
ATOM   3228 H  H    B HIS   A 1 138 ? 12.073 -10.073 -5.973  0.30 18.34 ?  138 HIS   A H    1 
ATOM   3229 H  HA   A HIS   A 1 138 ? 13.184 -12.484 -5.838  0.70 17.36 ?  138 HIS   A HA   1 
ATOM   3230 H  HA   B HIS   A 1 138 ? 13.188 -12.432 -5.910  0.30 17.60 ?  138 HIS   A HA   1 
ATOM   3231 H  HB2  A HIS   A 1 138 ? 13.128 -11.325 -7.821  0.70 18.71 ?  138 HIS   A HB2  1 
ATOM   3232 H  HB2  B HIS   A 1 138 ? 13.185 -11.317 -7.892  0.30 18.13 ?  138 HIS   A HB2  1 
ATOM   3233 H  HB3  A HIS   A 1 138 ? 13.990 -10.148 -7.192  0.70 18.71 ?  138 HIS   A HB3  1 
ATOM   3234 H  HB3  B HIS   A 1 138 ? 13.957 -10.082 -7.259  0.30 18.13 ?  138 HIS   A HB3  1 
ATOM   3235 H  HD1  A HIS   A 1 138 ? 14.528 -13.691 -7.784  0.70 21.44 ?  138 HIS   A HD1  1 
ATOM   3236 H  HD2  A HIS   A 1 138 ? 16.569 -10.376 -7.886  0.70 20.63 ?  138 HIS   A HD2  1 
ATOM   3237 H  HD2  B HIS   A 1 138 ? 16.589 -10.163 -7.778  0.30 18.59 ?  138 HIS   A HD2  1 
ATOM   3238 H  HE1  A HIS   A 1 138 ? 16.700 -14.284 -8.505  0.70 22.05 ?  138 HIS   A HE1  1 
ATOM   3239 H  HE1  B HIS   A 1 138 ? 16.921 -14.018 -8.612  0.30 19.21 ?  138 HIS   A HE1  1 
ATOM   3240 H  HE2  B HIS   A 1 138 ? 18.063 -11.949 -8.501  0.30 18.95 ?  138 HIS   A HE2  1 
ATOM   3241 N  N    . SER   A 1 139 ? 14.806 -10.161 -4.333  1.00 13.15 ?  139 SER   A N    1 
ATOM   3242 C  CA   . SER   A 1 139 ? 15.879 -9.965  -3.367  1.00 12.85 ?  139 SER   A CA   1 
ATOM   3243 C  C    . SER   A 1 139 ? 15.662 -10.798 -2.108  1.00 12.32 ?  139 SER   A C    1 
ATOM   3244 O  O    . SER   A 1 139 ? 16.610 -11.389 -1.577  1.00 12.45 ?  139 SER   A O    1 
ATOM   3245 C  CB   . SER   A 1 139 ? 16.022 -8.486  -3.028  1.00 12.52 ?  139 SER   A CB   1 
ATOM   3246 O  OG   . SER   A 1 139 ? 17.100 -8.311  -2.128  1.00 13.00 ?  139 SER   A OG   1 
ATOM   3247 H  H    A SER   A 1 139 ? 14.382 -9.446  -4.558  0.70 15.75 ?  139 SER   A H    1 
ATOM   3248 H  H    B SER   A 1 139 ? 14.355 -9.451  -4.519  0.30 15.75 ?  139 SER   A H    1 
ATOM   3249 H  HA   . SER   A 1 139 ? 16.713 -10.252 -3.768  1.00 15.40 ?  139 SER   A HA   1 
ATOM   3250 H  HB2  . SER   A 1 139 ? 16.208 -7.983  -3.840  1.00 15.01 ?  139 SER   A HB2  1 
ATOM   3251 H  HB3  . SER   A 1 139 ? 15.201 -8.165  -2.621  1.00 15.01 ?  139 SER   A HB3  1 
ATOM   3252 H  HG   . SER   A 1 139 ? 17.180 -7.496  -1.926  1.00 15.57 ?  139 SER   A HG   1 
ATOM   3253 N  N    . LEU   A 1 140 ? 14.422 -10.860 -1.618  1.00 12.52 ?  140 LEU   A N    1 
ATOM   3254 C  CA   . LEU   A 1 140 ? 14.138 -11.676 -0.439  1.00 12.63 ?  140 LEU   A CA   1 
ATOM   3255 C  C    . LEU   A 1 140 ? 14.411 -13.151 -0.712  1.00 12.79 ?  140 LEU   A C    1 
ATOM   3256 O  O    . LEU   A 1 140 ? 14.953 -13.861 0.144   1.00 13.37 ?  140 LEU   A O    1 
ATOM   3257 C  CB   . LEU   A 1 140 ? 12.693 -11.457 0.008   1.00 13.35 ?  140 LEU   A CB   1 
ATOM   3258 C  CG   . LEU   A 1 140 ? 12.233 -12.283 1.208   1.00 13.80 ?  140 LEU   A CG   1 
ATOM   3259 C  CD1  . LEU   A 1 140 ? 13.147 -12.098 2.414   1.00 14.07 ?  140 LEU   A CD1  1 
ATOM   3260 C  CD2  . LEU   A 1 140 ? 10.775 -11.948 1.561   1.00 14.57 ?  140 LEU   A CD2  1 
ATOM   3261 H  H    . LEU   A 1 140 ? 13.742 -10.443 -1.941  1.00 15.00 ?  140 LEU   A H    1 
ATOM   3262 H  HA   . LEU   A 1 140 ? 14.717 -11.397 0.280   1.00 15.14 ?  140 LEU   A HA   1 
ATOM   3263 H  HB2  . LEU   A 1 140 ? 12.579 -10.527 0.239   1.00 16.00 ?  140 LEU   A HB2  1 
ATOM   3264 H  HB3  . LEU   A 1 140 ? 12.106 -11.682 -0.734  1.00 16.00 ?  140 LEU   A HB3  1 
ATOM   3265 H  HG   . LEU   A 1 140 ? 12.253 -13.223 0.966   1.00 16.54 ?  140 LEU   A HG   1 
ATOM   3266 H  HD11 . LEU   A 1 140 ? 12.761 -12.558 3.177   1.00 16.87 ?  140 LEU   A HD11 1 
ATOM   3267 H  HD12 . LEU   A 1 140 ? 14.017 -12.481 2.208   1.00 16.87 ?  140 LEU   A HD12 1 
ATOM   3268 H  HD13 . LEU   A 1 140 ? 13.235 -11.155 2.603   1.00 16.87 ?  140 LEU   A HD13 1 
ATOM   3269 H  HD21 . LEU   A 1 140 ? 10.501 -12.483 2.328   1.00 17.46 ?  140 LEU   A HD21 1 
ATOM   3270 H  HD22 . LEU   A 1 140 ? 10.707 -11.006 1.781   1.00 17.46 ?  140 LEU   A HD22 1 
ATOM   3271 H  HD23 . LEU   A 1 140 ? 10.205 -12.152 0.802   1.00 17.46 ?  140 LEU   A HD23 1 
ATOM   3272 N  N    . ARG   A 1 141 ? 14.027 -13.633 -1.896  1.00 13.27 ?  141 ARG   A N    1 
ATOM   3273 C  CA   . ARG   A 1 141 ? 14.269 -15.028 -2.248  1.00 14.42 ?  141 ARG   A CA   1 
ATOM   3274 C  C    . ARG   A 1 141 ? 15.764 -15.331 -2.268  1.00 13.60 ?  141 ARG   A C    1 
ATOM   3275 O  O    . ARG   A 1 141 ? 16.214 -16.343 -1.714  1.00 14.08 ?  141 ARG   A O    1 
ATOM   3276 C  CB   . ARG   A 1 141 ? 13.645 -15.298 -3.617  1.00 15.99 ?  141 ARG   A CB   1 
ATOM   3277 C  CG   . ARG   A 1 141 ? 13.639 -16.749 -4.051  1.00 19.02 ?  141 ARG   A CG   1 
ATOM   3278 C  CD   . ARG   A 1 141 ? 12.601 -17.513 -3.294  1.00 21.54 ?  141 ARG   A CD   1 
ATOM   3279 N  NE   . ARG   A 1 141 ? 13.205 -18.305 -2.237  1.00 22.65 ?  141 ARG   A NE   1 
ATOM   3280 C  CZ   . ARG   A 1 141 ? 12.522 -18.859 -1.244  1.00 23.10 ?  141 ARG   A CZ   1 
ATOM   3281 N  NH1  . ARG   A 1 141 ? 11.238 -18.602 -1.060  1.00 21.76 ?  141 ARG   A NH1  1 
ATOM   3282 N  NH2  . ARG   A 1 141 ? 13.146 -19.687 -0.411  1.00 24.85 ?  141 ARG   A NH2  1 
ATOM   3283 H  H    . ARG   A 1 141 ? 13.630 -13.176 -2.511  1.00 15.90 ?  141 ARG   A H    1 
ATOM   3284 H  HA   . ARG   A 1 141 ? 13.846 -15.607 -1.597  1.00 17.28 ?  141 ARG   A HA   1 
ATOM   3285 H  HB2  . ARG   A 1 141 ? 12.725 -14.990 -3.607  1.00 19.16 ?  141 ARG   A HB2  1 
ATOM   3286 H  HB3  . ARG   A 1 141 ? 14.142 -14.801 -4.285  1.00 19.16 ?  141 ARG   A HB3  1 
ATOM   3287 H  HG2  . ARG   A 1 141 ? 13.436 -16.806 -5.000  1.00 22.81 ?  141 ARG   A HG2  1 
ATOM   3288 H  HG3  . ARG   A 1 141 ? 14.509 -17.149 -3.872  1.00 22.81 ?  141 ARG   A HG3  1 
ATOM   3289 H  HD2  . ARG   A 1 141 ? 11.975 -16.894 -2.884  1.00 25.82 ?  141 ARG   A HD2  1 
ATOM   3290 H  HD3  . ARG   A 1 141 ? 12.128 -18.108 -3.902  1.00 25.82 ?  141 ARG   A HD3  1 
ATOM   3291 H  HE   . ARG   A 1 141 ? 14.029 -18.525 -2.322  1.00 27.16 ?  141 ARG   A HE   1 
ATOM   3292 H  HH11 . ARG   A 1 141 ? 10.815 -18.081 -1.598  1.00 26.09 ?  141 ARG   A HH11 1 
ATOM   3293 H  HH12 . ARG   A 1 141 ? 10.812 -18.971 -0.405  1.00 26.09 ?  141 ARG   A HH12 1 
ATOM   3294 H  HH21 . ARG   A 1 141 ? 13.980 -19.858 -0.521  1.00 29.80 ?  141 ARG   A HH21 1 
ATOM   3295 H  HH22 . ARG   A 1 141 ? 12.716 -20.043 0.246   1.00 29.80 ?  141 ARG   A HH22 1 
ATOM   3296 N  N    . VAL   A 1 142 ? 16.552 -14.463 -2.909  1.00 12.93 ?  142 VAL   A N    1 
ATOM   3297 C  CA   . VAL   A 1 142 ? 17.997 -14.674 -2.944  1.00 13.16 ?  142 VAL   A CA   1 
ATOM   3298 C  C    . VAL   A 1 142 ? 18.572 -14.649 -1.533  1.00 12.58 ?  142 VAL   A C    1 
ATOM   3299 O  O    . VAL   A 1 142 ? 19.431 -15.465 -1.185  1.00 13.10 ?  142 VAL   A O    1 
ATOM   3300 C  CB   . VAL   A 1 142 ? 18.682 -13.650 -3.867  1.00 13.28 ?  142 VAL   A CB   1 
ATOM   3301 C  CG1  . VAL   A 1 142 ? 20.192 -13.854 -3.832  1.00 13.86 ?  142 VAL   A CG1  1 
ATOM   3302 C  CG2  . VAL   A 1 142 ? 18.173 -13.783 -5.295  1.00 14.48 ?  142 VAL   A CG2  1 
ATOM   3303 H  H    . VAL   A 1 142 ? 16.280 -13.752 -3.321  1.00 15.49 ?  142 VAL   A H    1 
ATOM   3304 H  HA   . VAL   A 1 142 ? 18.168 -15.549 -3.315  1.00 15.77 ?  142 VAL   A HA   1 
ATOM   3305 H  HB   . VAL   A 1 142 ? 18.494 -12.747 -3.557  1.00 15.91 ?  142 VAL   A HB   1 
ATOM   3306 H  HG11 . VAL   A 1 142 ? 20.599 -13.348 -4.555  1.00 16.62 ?  142 VAL   A HG11 1 
ATOM   3307 H  HG12 . VAL   A 1 142 ? 20.540 -13.540 -2.980  1.00 16.62 ?  142 VAL   A HG12 1 
ATOM   3308 H  HG13 . VAL   A 1 142 ? 20.386 -14.797 -3.941  1.00 16.62 ?  142 VAL   A HG13 1 
ATOM   3309 H  HG21 . VAL   A 1 142 ? 18.628 -13.129 -5.851  1.00 17.35 ?  142 VAL   A HG21 1 
ATOM   3310 H  HG22 . VAL   A 1 142 ? 18.372 -14.678 -5.610  1.00 17.35 ?  142 VAL   A HG22 1 
ATOM   3311 H  HG23 . VAL   A 1 142 ? 17.222 -13.626 -5.303  1.00 17.35 ?  142 VAL   A HG23 1 
ATOM   3312 N  N    . CYS   A 1 143 ? 18.104 -13.724 -0.695  1.00 12.40 ?  143 CYS   A N    1 
ATOM   3313 C  CA   . CYS   A 1 143 ? 18.562 -13.672 0.691   1.00 12.74 ?  143 CYS   A CA   1 
ATOM   3314 C  C    . CYS   A 1 143 ? 18.334 -15.011 1.387   1.00 12.73 ?  143 CYS   A C    1 
ATOM   3315 O  O    . CYS   A 1 143 ? 19.255 -15.595 1.961   1.00 12.56 ?  143 CYS   A O    1 
ATOM   3316 C  CB   . CYS   A 1 143 ? 17.825 -12.560 1.434   1.00 13.08 ?  143 CYS   A CB   1 
ATOM   3317 S  SG   . CYS   A 1 143 ? 18.331 -12.371 3.153   1.00 13.36 ?  143 CYS   A SG   1 
ATOM   3318 H  H    . CYS   A 1 143 ? 17.524 -13.127 -0.904  1.00 14.86 ?  143 CYS   A H    1 
ATOM   3319 H  HA   . CYS   A 1 143 ? 19.511 -13.481 0.704   1.00 15.26 ?  143 CYS   A HA   1 
ATOM   3320 H  HB2  . CYS   A 1 143 ? 17.984 -11.720 0.979   1.00 15.67 ?  143 CYS   A HB2  1 
ATOM   3321 H  HB3  . CYS   A 1 143 ? 16.879 -12.759 1.425   1.00 15.67 ?  143 CYS   A HB3  1 
ATOM   3322 H  HG   . CYS   A 1 143 ? 17.759 -11.428 3.615   1.00 16.01 ?  143 CYS   A HG   1 
ATOM   3323 N  N    . VAL   A 1 144 ? 17.105 -15.514 1.334   1.00 13.34 ?  144 VAL   A N    1 
ATOM   3324 C  CA   . VAL   A 1 144 ? 16.763 -16.748 2.033   1.00 14.68 ?  144 VAL   A CA   1 
ATOM   3325 C  C    . VAL   A 1 144 ? 17.580 -17.918 1.506   1.00 14.41 ?  144 VAL   A C    1 
ATOM   3326 O  O    . VAL   A 1 144 ? 17.948 -18.829 2.264   1.00 14.75 ?  144 VAL   A O    1 
ATOM   3327 C  CB   . VAL   A 1 144 ? 15.245 -16.980 1.906   1.00 17.42 ?  144 VAL   A CB   1 
ATOM   3328 C  CG1  . VAL   A 1 144 ? 14.875 -18.413 2.230   1.00 19.34 ?  144 VAL   A CG1  1 
ATOM   3329 C  CG2  . VAL   A 1 144 ? 14.494 -15.977 2.793   1.00 17.78 ?  144 VAL   A CG2  1 
ATOM   3330 H  H    . VAL   A 1 144 ? 16.447 -15.152 0.903   1.00 15.99 ?  144 VAL   A H    1 
ATOM   3331 H  HA   . VAL   A 1 144 ? 16.964 -16.639 2.971   1.00 17.60 ?  144 VAL   A HA   1 
ATOM   3332 H  HB   . VAL   A 1 144 ? 14.975 -16.806 0.986   1.00 20.89 ?  144 VAL   A HB   1 
ATOM   3333 H  HG11 . VAL   A 1 144 ? 13.921 -18.457 2.416   1.00 23.18 ?  144 VAL   A HG11 1 
ATOM   3334 H  HG12 . VAL   A 1 144 ? 15.086 -18.974 1.469   1.00 23.18 ?  144 VAL   A HG12 1 
ATOM   3335 H  HG13 . VAL   A 1 144 ? 15.375 -18.696 3.008   1.00 23.18 ?  144 VAL   A HG13 1 
ATOM   3336 H  HG21 . VAL   A 1 144 ? 13.537 -16.131 2.717   1.00 21.31 ?  144 VAL   A HG21 1 
ATOM   3337 H  HG22 . VAL   A 1 144 ? 14.774 -16.093 3.714   1.00 21.31 ?  144 VAL   A HG22 1 
ATOM   3338 H  HG23 . VAL   A 1 144 ? 14.701 -15.071 2.500   1.00 21.31 ?  144 VAL   A HG23 1 
ATOM   3339 N  N    . ASP   A 1 145 ? 17.848 -17.934 0.203   1.00 14.70 ?  145 ASP   A N    1 
ATOM   3340 C  CA   . ASP   A 1 145 ? 18.556 -19.038 -0.432  1.00 15.23 ?  145 ASP   A CA   1 
ATOM   3341 C  C    . ASP   A 1 145 ? 20.077 -18.897 -0.384  1.00 15.03 ?  145 ASP   A C    1 
ATOM   3342 O  O    . ASP   A 1 145 ? 20.778 -19.804 -0.853  1.00 17.09 ?  145 ASP   A O    1 
ATOM   3343 C  CB   . ASP   A 1 145 ? 18.110 -19.180 -1.890  1.00 16.61 ?  145 ASP   A CB   1 
ATOM   3344 C  CG   . ASP   A 1 145 ? 16.664 -19.626 -2.024  1.00 19.06 ?  145 ASP   A CG   1 
ATOM   3345 O  OD1  . ASP   A 1 145 ? 16.091 -20.165 -1.051  1.00 19.26 ?  145 ASP   A OD1  1 
ATOM   3346 O  OD2  . ASP   A 1 145 ? 16.093 -19.424 -3.112  1.00 20.13 -1 145 ASP   A OD2  1 
ATOM   3347 H  H    . ASP   A 1 145 ? 17.604 -17.313 -0.348  1.00 17.62 ?  145 ASP   A H    1 
ATOM   3348 H  HA   . ASP   A 1 145 ? 18.315 -19.858 0.025   1.00 18.26 ?  145 ASP   A HA   1 
ATOM   3349 H  HB2  . ASP   A 1 145 ? 18.206 -18.324 -2.335  1.00 19.91 ?  145 ASP   A HB2  1 
ATOM   3350 H  HB3  . ASP   A 1 145 ? 18.660 -19.847 -2.324  1.00 19.91 ?  145 ASP   A HB3  1 
ATOM   3351 N  N    . THR   A 1 146 ? 20.604 -17.801 0.162   1.00 13.23 ?  146 THR   A N    1 
ATOM   3352 C  CA   . THR   A 1 146 ? 22.043 -17.556 0.184   1.00 12.85 ?  146 THR   A CA   1 
ATOM   3353 C  C    . THR   A 1 146 ? 22.600 -17.372 1.580   1.00 12.96 ?  146 THR   A C    1 
ATOM   3354 O  O    . THR   A 1 146 ? 23.679 -17.900 1.886   1.00 14.04 ?  146 THR   A O    1 
ATOM   3355 C  CB   . THR   A 1 146 ? 22.367 -16.305 -0.650  1.00 12.61 ?  146 THR   A CB   1 
ATOM   3356 O  OG1  . THR   A 1 146 ? 21.844 -16.472 -1.969  1.00 13.22 ?  146 THR   A OG1  1 
ATOM   3357 C  CG2  . THR   A 1 146 ? 23.867 -16.078 -0.737  1.00 13.41 ?  146 THR   A CG2  1 
ATOM   3358 H  H    . THR   A 1 146 ? 20.138 -17.167 0.520   1.00 15.86 ?  146 THR   A H    1 
ATOM   3359 H  HA   . THR   A 1 146 ? 22.498 -18.304 -0.220  1.00 15.40 ?  146 THR   A HA   1 
ATOM   3360 H  HB   . THR   A 1 146 ? 21.968 -15.521 -0.236  1.00 15.11 ?  146 THR   A HB   1 
ATOM   3361 H  HG1  . THR   A 1 146 ? 21.006 -16.537 -1.936  1.00 15.84 ?  146 THR   A HG1  1 
ATOM   3362 H  HG21 . THR   A 1 146 ? 24.062 -15.415 -1.418  1.00 16.07 ?  146 THR   A HG21 1 
ATOM   3363 H  HG22 . THR   A 1 146 ? 24.207 -15.762 0.115   1.00 16.07 ?  146 THR   A HG22 1 
ATOM   3364 H  HG23 . THR   A 1 146 ? 24.312 -16.907 -0.969  1.00 16.07 ?  146 THR   A HG23 1 
ATOM   3365 N  N    . VAL   A 1 147 ? 21.922 -16.593 2.416   1.00 12.42 ?  147 VAL   A N    1 
ATOM   3366 C  CA   . VAL   A 1 147 ? 22.408 -16.294 3.755   1.00 12.84 ?  147 VAL   A CA   1 
ATOM   3367 C  C    . VAL   A 1 147 ? 22.087 -17.463 4.673   1.00 13.30 ?  147 VAL   A C    1 
ATOM   3368 O  O    . VAL   A 1 147 ? 20.947 -17.936 4.726   1.00 14.04 ?  147 VAL   A O    1 
ATOM   3369 C  CB   . VAL   A 1 147 ? 21.793 -14.986 4.275   1.00 12.93 ?  147 VAL   A CB   1 
ATOM   3370 C  CG1  . VAL   A 1 147 ? 22.341 -14.673 5.650   1.00 13.92 ?  147 VAL   A CG1  1 
ATOM   3371 C  CG2  . VAL   A 1 147 ? 22.054 -13.840 3.303   1.00 13.19 ?  147 VAL   A CG2  1 
ATOM   3372 H  H    . VAL   A 1 147 ? 21.163 -16.227 2.234   1.00 14.88 ?  147 VAL   A H    1 
ATOM   3373 H  HA   . VAL   A 1 147 ? 23.372 -16.185 3.723   1.00 15.38 ?  147 VAL   A HA   1 
ATOM   3374 H  HB   . VAL   A 1 147 ? 20.836 -15.100 4.355   1.00 15.50 ?  147 VAL   A HB   1 
ATOM   3375 H  HG11 . VAL   A 1 147 ? 22.099 -13.769 5.887   1.00 16.69 ?  147 VAL   A HG11 1 
ATOM   3376 H  HG12 . VAL   A 1 147 ? 21.960 -15.299 6.291   1.00 16.69 ?  147 VAL   A HG12 1 
ATOM   3377 H  HG13 . VAL   A 1 147 ? 23.307 -14.768 5.634   1.00 16.69 ?  147 VAL   A HG13 1 
ATOM   3378 H  HG21 . VAL   A 1 147 ? 21.728 -13.016 3.698   1.00 15.80 ?  147 VAL   A HG21 1 
ATOM   3379 H  HG22 . VAL   A 1 147 ? 23.005 -13.777 3.139   1.00 15.80 ?  147 VAL   A HG22 1 
ATOM   3380 H  HG23 . VAL   A 1 147 ? 21.583 -14.020 2.475   1.00 15.80 ?  147 VAL   A HG23 1 
ATOM   3381 N  N    . ARG   A 1 148 ? 23.107 -17.937 5.388   1.00 13.64 ?  148 ARG   A N    1 
ATOM   3382 C  CA   . ARG   A 1 148 ? 22.972 -19.014 6.353   1.00 13.91 ?  148 ARG   A CA   1 
ATOM   3383 C  C    . ARG   A 1 148 ? 23.102 -18.539 7.789   1.00 13.84 ?  148 ARG   A C    1 
ATOM   3384 O  O    . ARG   A 1 148 ? 22.695 -19.262 8.706   1.00 15.62 ?  148 ARG   A O    1 
ATOM   3385 C  CB   . ARG   A 1 148 ? 24.011 -20.110 6.070   1.00 14.65 ?  148 ARG   A CB   1 
ATOM   3386 C  CG   . ARG   A 1 148 ? 23.843 -20.751 4.699   1.00 15.95 ?  148 ARG   A CG   1 
ATOM   3387 C  CD   . ARG   A 1 148 ? 24.938 -21.781 4.406   1.00 16.61 ?  148 ARG   A CD   1 
ATOM   3388 N  NE   . ARG   A 1 148 ? 26.280 -21.207 4.438   1.00 16.71 ?  148 ARG   A NE   1 
ATOM   3389 C  CZ   . ARG   A 1 148 ? 26.800 -20.472 3.465   1.00 15.92 ?  148 ARG   A CZ   1 
ATOM   3390 N  NH1  . ARG   A 1 148 ? 26.132 -20.233 2.348   1.00 16.14 ?  148 ARG   A NH1  1 
ATOM   3391 N  NH2  . ARG   A 1 148 ? 28.018 -19.948 3.622   1.00 16.29 ?  148 ARG   A NH2  1 
ATOM   3392 H  H    . ARG   A 1 148 ? 23.914 -17.635 5.322   1.00 16.34 ?  148 ARG   A H    1 
ATOM   3393 H  HA   . ARG   A 1 148 ? 22.096 -19.410 6.252   1.00 16.67 ?  148 ARG   A HA   1 
ATOM   3394 H  HB2  . ARG   A 1 148 ? 24.898 -19.734 6.114   1.00 17.56 ?  148 ARG   A HB2  1 
ATOM   3395 H  HB3  . ARG   A 1 148 ? 23.913 -20.817 6.731   1.00 17.56 ?  148 ARG   A HB3  1 
ATOM   3396 H  HG2  . ARG   A 1 148 ? 22.982 -21.194 4.659   1.00 19.12 ?  148 ARG   A HG2  1 
ATOM   3397 H  HG3  . ARG   A 1 148 ? 23.889 -20.053 4.022   1.00 19.12 ?  148 ARG   A HG3  1 
ATOM   3398 H  HD2  . ARG   A 1 148 ? 24.895 -22.481 5.072   1.00 19.91 ?  148 ARG   A HD2  1 
ATOM   3399 H  HD3  . ARG   A 1 148 ? 24.790 -22.151 3.520   1.00 19.91 ?  148 ARG   A HD3  1 
ATOM   3400 H  HE   . ARG   A 1 148 ? 26.756 -21.341 5.137   1.00 20.03 ?  148 ARG   A HE   1 
ATOM   3401 H  HH11 . ARG   A 1 148 ? 25.343 -20.549 2.237   1.00 19.34 ?  148 ARG   A HH11 1 
ATOM   3402 H  HH12 . ARG   A 1 148 ? 26.487 -19.744 1.730   1.00 19.34 ?  148 ARG   A HH12 1 
ATOM   3403 H  HH21 . ARG   A 1 148 ? 28.458 -20.091 4.348   1.00 19.53 ?  148 ARG   A HH21 1 
ATOM   3404 H  HH22 . ARG   A 1 148 ? 28.368 -19.464 3.000   1.00 19.53 ?  148 ARG   A HH22 1 
ATOM   3405 N  N    . THR   A 1 149 ? 23.656 -17.349 8.001   1.00 14.08 ?  149 THR   A N    1 
ATOM   3406 C  CA   . THR   A 1 149 ? 23.737 -16.748 9.318   1.00 14.08 ?  149 THR   A CA   1 
ATOM   3407 C  C    . THR   A 1 149 ? 22.411 -16.045 9.625   1.00 13.53 ?  149 THR   A C    1 
ATOM   3408 O  O    . THR   A 1 149 ? 21.475 -16.041 8.815   1.00 14.49 ?  149 THR   A O    1 
ATOM   3409 C  CB   . THR   A 1 149 ? 24.938 -15.812 9.375   1.00 14.70 ?  149 THR   A CB   1 
ATOM   3410 O  OG1  . THR   A 1 149 ? 24.805 -14.869 8.310   1.00 14.98 ?  149 THR   A OG1  1 
ATOM   3411 C  CG2  . THR   A 1 149 ? 26.250 -16.602 9.238   1.00 15.28 ?  149 THR   A CG2  1 
ATOM   3412 H  H    . THR   A 1 149 ? 23.999 -16.860 7.379   1.00 16.87 ?  149 THR   A H    1 
ATOM   3413 H  HA   . THR   A 1 149 ? 23.862 -17.453 9.974   1.00 16.87 ?  149 THR   A HA   1 
ATOM   3414 H  HB   . THR   A 1 149 ? 24.933 -15.349 10.222  1.00 17.62 ?  149 THR   A HB   1 
ATOM   3415 H  HG1  . THR   A 1 149 ? 25.456 -14.338 8.317   1.00 17.95 ?  149 THR   A HG1  1 
ATOM   3416 H  HG21 . THR   A 1 149 ? 27.006 -15.998 9.289   1.00 18.32 ?  149 THR   A HG21 1 
ATOM   3417 H  HG22 . THR   A 1 149 ? 26.323 -17.259 9.951   1.00 18.32 ?  149 THR   A HG22 1 
ATOM   3418 H  HG23 . THR   A 1 149 ? 26.277 -17.067 8.384   1.00 18.32 ?  149 THR   A HG23 1 
ATOM   3419 N  N    . ASN   A 1 150 ? 22.291 -15.502 10.830  1.00 14.08 ?  150 ASN   A N    1 
ATOM   3420 C  CA   . ASN   A 1 150 ? 21.009 -14.987 11.307  1.00 14.78 ?  150 ASN   A CA   1 
ATOM   3421 C  C    . ASN   A 1 150 ? 20.829 -13.545 10.854  1.00 13.83 ?  150 ASN   A C    1 
ATOM   3422 O  O    . ASN   A 1 150 ? 21.581 -12.653 11.271  1.00 15.24 ?  150 ASN   A O    1 
ATOM   3423 C  CB   . ASN   A 1 150 ? 20.943 -15.106 12.827  1.00 17.57 ?  150 ASN   A CB   1 
ATOM   3424 C  CG   . ASN   A 1 150 ? 20.819 -16.542 13.285  1.00 22.02 ?  150 ASN   A CG   1 
ATOM   3425 O  OD1  . ASN   A 1 150 ? 20.208 -17.364 12.602  1.00 22.96 ?  150 ASN   A OD1  1 
ATOM   3426 N  ND2  . ASN   A 1 150 ? 21.406 -16.858 14.438  1.00 24.34 ?  150 ASN   A ND2  1 
ATOM   3427 H  H    . ASN   A 1 150 ? 22.938 -15.417 11.389  1.00 16.88 ?  150 ASN   A H    1 
ATOM   3428 H  HA   . ASN   A 1 150 ? 20.289 -15.527 10.939  1.00 17.72 ?  150 ASN   A HA   1 
ATOM   3429 H  HB2  . ASN   A 1 150 ? 21.756 -14.747 13.209  1.00 21.06 ?  150 ASN   A HB2  1 
ATOM   3430 H  HB3  . ASN   A 1 150 ? 20.171 -14.625 13.161  1.00 21.06 ?  150 ASN   A HB3  1 
ATOM   3431 H  HD21 . ASN   A 1 150 ? 21.367 -17.668 14.744  1.00 29.18 ?  150 ASN   A HD21 1 
ATOM   3432 H  HD22 . ASN   A 1 150 ? 21.825 -16.258 14.891  1.00 29.18 ?  150 ASN   A HD22 1 
ATOM   3433 N  N    . VAL   A 1 151 ? 19.834 -13.314 10.007  1.00 13.36 ?  151 VAL   A N    1 
ATOM   3434 C  CA   . VAL   A 1 151 ? 19.624 -12.010 9.401   1.00 13.12 ?  151 VAL   A CA   1 
ATOM   3435 C  C    . VAL   A 1 151 ? 18.235 -11.500 9.762   1.00 13.27 ?  151 VAL   A C    1 
ATOM   3436 O  O    . VAL   A 1 151 ? 17.229 -12.211 9.609   1.00 14.62 ?  151 VAL   A O    1 
ATOM   3437 C  CB   . VAL   A 1 151 ? 19.910 -12.018 7.883   1.00 14.72 ?  151 VAL   A CB   1 
ATOM   3438 C  CG1  . VAL   A 1 151 ? 19.074 -13.050 7.147   1.00 16.00 ?  151 VAL   A CG1  1 
ATOM   3439 C  CG2  . VAL   A 1 151 ? 19.738 -10.617 7.287   1.00 14.68 ?  151 VAL   A CG2  1 
ATOM   3440 H  H    . VAL   A 1 151 ? 19.254 -13.908 9.771   1.00 16.01 ?  151 VAL   A H    1 
ATOM   3441 H  HA   . VAL   A 1 151 ? 20.264 -11.395 9.792   1.00 15.73 ?  151 VAL   A HA   1 
ATOM   3442 H  HB   . VAL   A 1 151 ? 20.842 -12.269 7.753   1.00 17.64 ?  151 VAL   A HB   1 
ATOM   3443 H  HG11 . VAL   A 1 151 ? 19.277 -13.014 6.198   1.00 19.17 ?  151 VAL   A HG11 1 
ATOM   3444 H  HG12 . VAL   A 1 151 ? 19.287 -13.939 7.489   1.00 19.17 ?  151 VAL   A HG12 1 
ATOM   3445 H  HG13 . VAL   A 1 151 ? 18.134 -12.865 7.291   1.00 19.17 ?  151 VAL   A HG13 1 
ATOM   3446 H  HG21 . VAL   A 1 151 ? 20.043 -10.630 6.362   1.00 17.60 ?  151 VAL   A HG21 1 
ATOM   3447 H  HG22 . VAL   A 1 151 ? 18.803 -10.370 7.320   1.00 17.60 ?  151 VAL   A HG22 1 
ATOM   3448 H  HG23 . VAL   A 1 151 ? 20.270 -9.989  7.797   1.00 17.60 ?  151 VAL   A HG23 1 
ATOM   3449 N  N    . TYR   A 1 152 ? 18.212 -10.251 10.243  1.00 13.11 ?  152 TYR   A N    1 
ATOM   3450 C  CA   . TYR   A 1 152 ? 17.018 -9.515  10.626  1.00 12.58 ?  152 TYR   A CA   1 
ATOM   3451 C  C    . TYR   A 1 152 ? 16.830 -8.413  9.594   1.00 11.98 ?  152 TYR   A C    1 
ATOM   3452 O  O    . TYR   A 1 152 ? 17.611 -7.451  9.547   1.00 12.45 ?  152 TYR   A O    1 
ATOM   3453 C  CB   . TYR   A 1 152 ? 17.193 -8.963  12.037  1.00 13.64 ?  152 TYR   A CB   1 
ATOM   3454 C  CG   . TYR   A 1 152 ? 17.152 -10.084 13.037  1.00 14.36 ?  152 TYR   A CG   1 
ATOM   3455 C  CD1  . TYR   A 1 152 ? 18.278 -10.855 13.297  1.00 15.97 ?  152 TYR   A CD1  1 
ATOM   3456 C  CD2  . TYR   A 1 152 ? 15.971 -10.426 13.675  1.00 14.92 ?  152 TYR   A CD2  1 
ATOM   3457 C  CE1  . TYR   A 1 152 ? 18.239 -11.915 14.182  1.00 17.69 ?  152 TYR   A CE1  1 
ATOM   3458 C  CE2  . TYR   A 1 152 ? 15.920 -11.491 14.570  1.00 16.79 ?  152 TYR   A CE2  1 
ATOM   3459 C  CZ   . TYR   A 1 152 ? 17.059 -12.229 14.820  1.00 17.42 ?  152 TYR   A CZ   1 
ATOM   3460 O  OH   . TYR   A 1 152 ? 17.015 -13.293 15.698  1.00 20.33 ?  152 TYR   A OH   1 
ATOM   3461 H  H    . TYR   A 1 152 ? 18.933 -9.780  10.344  1.00 15.71 ?  152 TYR   A H    1 
ATOM   3462 H  HA   . TYR   A 1 152 ? 16.251 -10.103 10.603  1.00 15.07 ?  152 TYR   A HA   1 
ATOM   3463 H  HB2  . TYR   A 1 152 ? 18.054 -8.523  12.104  1.00 16.35 ?  152 TYR   A HB2  1 
ATOM   3464 H  HB3  . TYR   A 1 152 ? 16.477 -8.346  12.232  1.00 16.35 ?  152 TYR   A HB3  1 
ATOM   3465 H  HD1  . TYR   A 1 152 ? 19.075 -10.646 12.861  1.00 19.14 ?  152 TYR   A HD1  1 
ATOM   3466 H  HD2  . TYR   A 1 152 ? 15.197 -9.930  13.505  1.00 17.89 ?  152 TYR   A HD2  1 
ATOM   3467 H  HE1  . TYR   A 1 152 ? 19.004 -12.407 14.348  1.00 21.21 ?  152 TYR   A HE1  1 
ATOM   3468 H  HE2  . TYR   A 1 152 ? 15.120 -11.698 15.000  1.00 20.12 ?  152 TYR   A HE2  1 
ATOM   3469 H  HH   . TYR   A 1 152 ? 16.242 -13.358 16.020  1.00 24.37 ?  152 TYR   A HH   1 
ATOM   3470 N  N    A LEU   A 1 153 ? 15.829 -8.596  8.731   0.70 12.38 ?  153 LEU   A N    1 
ATOM   3471 N  N    B LEU   A 1 153 ? 15.781 -8.521  8.788   0.30 12.16 ?  153 LEU   A N    1 
ATOM   3472 C  CA   A LEU   A 1 153 ? 15.567 -7.714  7.600   0.70 12.51 ?  153 LEU   A CA   1 
ATOM   3473 C  CA   B LEU   A 1 153 ? 15.538 -7.571  7.711   0.30 11.89 ?  153 LEU   A CA   1 
ATOM   3474 C  C    A LEU   A 1 153 ? 14.560 -6.635  7.974   0.70 12.45 ?  153 LEU   A C    1 
ATOM   3475 C  C    B LEU   A 1 153 ? 14.577 -6.486  8.178   0.30 11.72 ?  153 LEU   A C    1 
ATOM   3476 O  O    A LEU   A 1 153 ? 13.461 -6.936  8.454   0.70 14.02 ?  153 LEU   A O    1 
ATOM   3477 O  O    B LEU   A 1 153 ? 13.460 -6.783  8.617   0.30 12.55 ?  153 LEU   A O    1 
ATOM   3478 C  CB   A LEU   A 1 153 ? 14.999 -8.522  6.433   0.70 12.66 ?  153 LEU   A CB   1 
ATOM   3479 C  CB   B LEU   A 1 153 ? 14.985 -8.282  6.479   0.30 12.12 ?  153 LEU   A CB   1 
ATOM   3480 C  CG   A LEU   A 1 153 ? 15.950 -9.503  5.747   0.70 12.25 ?  153 LEU   A CG   1 
ATOM   3481 C  CG   B LEU   A 1 153 ? 15.885 -9.378  5.900   0.30 12.58 ?  153 LEU   A CG   1 
ATOM   3482 C  CD1  A LEU   A 1 153 ? 15.166 -10.435 4.827   0.70 12.61 ?  153 LEU   A CD1  1 
ATOM   3483 C  CD1  B LEU   A 1 153 ? 15.137 -10.148 4.821   0.30 13.12 ?  153 LEU   A CD1  1 
ATOM   3484 C  CD2  A LEU   A 1 153 ? 17.007 -8.750  4.966   0.70 12.13 ?  153 LEU   A CD2  1 
ATOM   3485 C  CD2  B LEU   A 1 153 ? 17.192 -8.806  5.354   0.30 12.88 ?  153 LEU   A CD2  1 
ATOM   3486 H  H    A LEU   A 1 153 ? 15.268 -9.251  8.786   0.70 14.83 ?  153 LEU   A H    1 
ATOM   3487 H  H    B LEU   A 1 153 ? 15.180 -9.140  8.849   0.30 14.58 ?  153 LEU   A H    1 
ATOM   3488 H  HA   A LEU   A 1 153 ? 16.394 -7.301  7.316   0.70 14.99 ?  153 LEU   A HA   1 
ATOM   3489 H  HA   B LEU   A 1 153 ? 16.371 -7.146  7.473   0.30 14.24 ?  153 LEU   A HA   1 
ATOM   3490 H  HB2  A LEU   A 1 153 ? 14.243 -9.040  6.758   0.70 15.18 ?  153 LEU   A HB2  1 
ATOM   3491 H  HB2  B LEU   A 1 153 ? 14.141 -8.692  6.717   0.30 14.52 ?  153 LEU   A HB2  1 
ATOM   3492 H  HB3  A LEU   A 1 153 ? 14.693 -7.904  5.753   0.70 15.18 ?  153 LEU   A HB3  1 
ATOM   3493 H  HB3  B LEU   A 1 153 ? 14.844 -7.620  5.786   0.30 14.52 ?  153 LEU   A HB3  1 
ATOM   3494 H  HG   A LEU   A 1 153 ? 16.394 -10.046 6.423   0.70 14.68 ?  153 LEU   A HG   1 
ATOM   3495 H  HG   B LEU   A 1 153 ? 16.111 -10.001 6.608   0.30 15.08 ?  153 LEU   A HG   1 
ATOM   3496 H  HD11 A LEU   A 1 153 ? 15.758 -11.133 4.508   0.70 15.11 ?  153 LEU   A HD11 1 
ATOM   3497 H  HD11 B LEU   A 1 153 ? 15.707 -10.857 4.487   0.30 15.73 ?  153 LEU   A HD11 1 
ATOM   3498 H  HD12 A LEU   A 1 153 ? 14.431 -10.821 5.322   0.70 15.11 ?  153 LEU   A HD12 1 
ATOM   3499 H  HD12 B LEU   A 1 153 ? 14.330 -10.524 5.206   0.30 15.73 ?  153 LEU   A HD12 1 
ATOM   3500 H  HD13 A LEU   A 1 153 ? 14.829 -9.918  4.078   0.70 15.11 ?  153 LEU   A HD13 1 
ATOM   3501 H  HD13 B LEU   A 1 153 ? 14.908 -9.539  4.101   0.30 15.73 ?  153 LEU   A HD13 1 
ATOM   3502 H  HD21 A LEU   A 1 153 ? 17.578 -9.388  4.520   0.70 14.53 ?  153 LEU   A HD21 1 
ATOM   3503 H  HD21 B LEU   A 1 153 ? 17.706 -9.524  4.953   0.30 15.44 ?  153 LEU   A HD21 1 
ATOM   3504 H  HD22 A LEU   A 1 153 ? 16.564 -8.182  4.319   0.70 14.53 ?  153 LEU   A HD22 1 
ATOM   3505 H  HD22 B LEU   A 1 153 ? 16.989 -8.131  4.689   0.30 15.44 ?  153 LEU   A HD22 1 
ATOM   3506 H  HD23 A LEU   A 1 153 ? 17.524 -8.212  5.585   0.70 14.53 ?  153 LEU   A HD23 1 
ATOM   3507 H  HD23 B LEU   A 1 153 ? 17.695 -8.410  6.084   0.30 15.44 ?  153 LEU   A HD23 1 
ATOM   3508 N  N    A ALA   A 1 154 ? 14.923 -5.385  7.709   0.70 11.89 ?  154 ALA   A N    1 
ATOM   3509 N  N    B ALA   A 1 154 ? 15.014 -5.233  8.075   0.30 11.21 ?  154 ALA   A N    1 
ATOM   3510 C  CA   A ALA   A 1 154 ? 14.059 -4.236  7.928   0.70 12.30 ?  154 ALA   A CA   1 
ATOM   3511 C  CA   B ALA   A 1 154 ? 14.187 -4.073  8.370   0.30 11.62 ?  154 ALA   A CA   1 
ATOM   3512 C  C    A ALA   A 1 154 ? 13.578 -3.739  6.573   0.70 11.39 ?  154 ALA   A C    1 
ATOM   3513 C  C    B ALA   A 1 154 ? 13.669 -3.531  7.044   0.30 11.12 ?  154 ALA   A C    1 
ATOM   3514 O  O    A ALA   A 1 154 ? 14.389 -3.369  5.719   0.70 12.41 ?  154 ALA   A O    1 
ATOM   3515 O  O    B ALA   A 1 154 ? 14.456 -3.104  6.195   0.30 10.79 ?  154 ALA   A O    1 
ATOM   3516 C  CB   A ALA   A 1 154 ? 14.825 -3.127  8.647   0.70 12.55 ?  154 ALA   A CB   1 
ATOM   3517 C  CB   B ALA   A 1 154 ? 15.002 -3.014  9.116   0.30 12.54 ?  154 ALA   A CB   1 
ATOM   3518 H  H    A ALA   A 1 154 ? 15.691 -5.179  7.374   0.70 14.25 ?  154 ALA   A H    1 
ATOM   3519 H  H    B ALA   A 1 154 ? 15.807 -5.017  7.814   0.30 13.44 ?  154 ALA   A H    1 
ATOM   3520 H  HA   A ALA   A 1 154 ? 13.294 -4.498  8.464   0.70 14.74 ?  154 ALA   A HA   1 
ATOM   3521 H  HA   B ALA   A 1 154 ? 13.430 -4.324  8.918   0.30 13.93 ?  154 ALA   A HA   1 
ATOM   3522 H  HB1  A ALA   A 1 154 ? 14.231 -2.377  8.784   0.70 15.04 ?  154 ALA   A HB1  1 
ATOM   3523 H  HB1  B ALA   A 1 154 ? 14.439 -2.248  9.310   0.30 15.03 ?  154 ALA   A HB1  1 
ATOM   3524 H  HB2  A ALA   A 1 154 ? 15.141 -3.466  9.500   0.70 15.04 ?  154 ALA   A HB2  1 
ATOM   3525 H  HB2  B ALA   A 1 154 ? 15.330 -3.400  9.947   0.30 15.03 ?  154 ALA   A HB2  1 
ATOM   3526 H  HB3  A ALA   A 1 154 ? 15.580 -2.862  8.098   0.70 15.04 ?  154 ALA   A HB3  1 
ATOM   3527 H  HB3  B ALA   A 1 154 ? 15.753 -2.741  8.565   0.30 15.03 ?  154 ALA   A HB3  1 
ATOM   3528 N  N    A VAL   A 1 155 ? 12.262 -3.739  6.379   0.40 9.27  ?  155 VAL   A N    1 
ATOM   3529 N  N    B VAL   A 1 155 ? 12.353 -3.579  6.858   0.30 11.25 ?  155 VAL   A N    1 
ATOM   3530 C  CA   A VAL   A 1 155 ? 11.617 -3.269  5.156   0.40 11.71 ?  155 VAL   A CA   1 
ATOM   3531 C  CA   B VAL   A 1 155 ? 11.702 -3.124  5.635   0.30 11.96 ?  155 VAL   A CA   1 
ATOM   3532 C  CA   T VAL   A 1 155 ? 11.601 -3.327  5.186   0.30 13.87 ?  155 VAL   A CA   1 
ATOM   3533 C  C    A VAL   A 1 155 ? 10.881 -1.979  5.505   0.40 13.23 ?  155 VAL   A C    1 
ATOM   3534 C  C    B VAL   A 1 155 ? 11.077 -1.763  5.906   0.30 13.26 ?  155 VAL   A C    1 
ATOM   3535 C  C    T VAL   A 1 155 ? 10.974 -1.963  5.490   0.30 13.99 ?  155 VAL   A C    1 
ATOM   3536 O  O    A VAL   A 1 155 ? 9.916  -2.000  6.277   0.40 13.54 ?  155 VAL   A O    1 
ATOM   3537 O  O    B VAL   A 1 155 ? 10.171 -1.640  6.740   0.30 12.97 ?  155 VAL   A O    1 
ATOM   3538 O  O    T VAL   A 1 155 ? 10.102 -1.848  6.349   0.30 13.77 ?  155 VAL   A O    1 
ATOM   3539 C  CB   A VAL   A 1 155 ? 10.666 -4.330  4.581   0.40 12.26 ?  155 VAL   A CB   1 
ATOM   3540 C  CB   B VAL   A 1 155 ? 10.648 -4.131  5.153   0.30 12.08 ?  155 VAL   A CB   1 
ATOM   3541 C  CB   T VAL   A 1 155 ? 10.574 -4.354  4.664   0.30 13.68 ?  155 VAL   A CB   1 
ATOM   3542 C  CG1  A VAL   A 1 155 ? 9.994  -3.827  3.312   0.40 12.65 ?  155 VAL   A CG1  1 
ATOM   3543 C  CG1  B VAL   A 1 155 ? 9.891  -3.573  3.950   0.30 12.40 ?  155 VAL   A CG1  1 
ATOM   3544 C  CG1  T VAL   A 1 155 ? 9.874  -3.825  3.426   0.30 13.69 ?  155 VAL   A CG1  1 
ATOM   3545 C  CG2  A VAL   A 1 155 ? 11.428 -5.626  4.304   0.40 13.30 ?  155 VAL   A CG2  1 
ATOM   3546 C  CG2  B VAL   A 1 155 ? 11.306 -5.462  4.819   0.30 12.91 ?  155 VAL   A CG2  1 
ATOM   3547 C  CG2  T VAL   A 1 155 ? 11.257 -5.689  4.364   0.30 14.07 ?  155 VAL   A CG2  1 
ATOM   3548 H  H    A VAL   A 1 155 ? 11.699 -4.034  6.961   0.40 11.10 ?  155 VAL   A H    1 
ATOM   3549 H  H    B VAL   A 1 155 ? 11.804 -3.872  7.444   0.30 13.48 ?  155 VAL   A H    1 
ATOM   3550 H  HA   A VAL   A 1 155 ? 12.292 -3.070  4.490   0.40 14.03 ?  155 VAL   A HA   1 
ATOM   3551 H  HA   B VAL   A 1 155 ? 12.368 -3.016  4.934   0.30 14.33 ?  155 VAL   A HA   1 
ATOM   3552 H  HB   A VAL   A 1 155 ? 9.975  -4.526  5.233   0.40 14.69 ?  155 VAL   A HB   1 
ATOM   3553 H  HB   B VAL   A 1 155 ? 10.012 -4.281  5.868   0.30 14.47 ?  155 VAL   A HB   1 
ATOM   3554 H  HB   T VAL   A 1 155 ? 9.907  -4.506  5.350   0.30 16.39 ?  155 VAL   A HB   1 
ATOM   3555 H  HG11 A VAL   A 1 155 ? 9.499  -4.559  2.908   0.40 15.16 ?  155 VAL   A HG11 1 
ATOM   3556 H  HG11 B VAL   A 1 155 ? 9.392  -4.290  3.533   0.30 14.86 ?  155 VAL   A HG11 1 
ATOM   3557 H  HG11 T VAL   A 1 155 ? 9.351  -4.541  3.034   0.30 16.41 ?  155 VAL   A HG11 1 
ATOM   3558 H  HG12 A VAL   A 1 155 ? 9.387  -3.107  3.539   0.40 15.16 ?  155 VAL   A HG12 1 
ATOM   3559 H  HG12 B VAL   A 1 155 ? 9.283  -2.878  4.249   0.30 14.86 ?  155 VAL   A HG12 1 
ATOM   3560 H  HG12 T VAL   A 1 155 ? 9.295  -3.091  3.680   0.30 16.41 ?  155 VAL   A HG12 1 
ATOM   3561 H  HG13 A VAL   A 1 155 ? 10.674 -3.511  2.698   0.40 15.16 ?  155 VAL   A HG13 1 
ATOM   3562 H  HG13 B VAL   A 1 155 ? 10.530 -3.204  3.318   0.30 14.86 ?  155 VAL   A HG13 1 
ATOM   3563 H  HG13 T VAL   A 1 155 ? 10.544 -3.520  2.793   0.30 16.41 ?  155 VAL   A HG13 1 
ATOM   3564 H  HG21 A VAL   A 1 155 ? 10.832 -6.260  3.878   0.40 15.94 ?  155 VAL   A HG21 1 
ATOM   3565 H  HG21 B VAL   A 1 155 ? 10.650 -6.039  4.402   0.30 15.47 ?  155 VAL   A HG21 1 
ATOM   3566 H  HG21 T VAL   A 1 155 ? 10.594 -6.319  4.043   0.30 16.86 ?  155 VAL   A HG21 1 
ATOM   3567 H  HG22 A VAL   A 1 155 ? 12.178 -5.432  3.718   0.40 15.94 ?  155 VAL   A HG22 1 
ATOM   3568 H  HG22 B VAL   A 1 155 ? 12.045 -5.305  4.208   0.30 15.47 ?  155 VAL   A HG22 1 
ATOM   3569 H  HG22 T VAL   A 1 155 ? 11.938 -5.551  3.685   0.30 16.86 ?  155 VAL   A HG22 1 
ATOM   3570 H  HG23 A VAL   A 1 155 ? 11.753 -5.990  5.144   0.40 15.94 ?  155 VAL   A HG23 1 
ATOM   3571 H  HG23 B VAL   A 1 155 ? 11.637 -5.868  5.637   0.30 15.47 ?  155 VAL   A HG23 1 
ATOM   3572 H  HG23 T VAL   A 1 155 ? 11.667 -6.026  5.177   0.30 16.86 ?  155 VAL   A HG23 1 
ATOM   3573 N  N    A PHE   A 1 156 ? 11.340 -0.850  4.950   0.40 15.17 ?  156 PHE   A N    1 
ATOM   3574 N  N    B PHE   A 1 156 ? 11.555 -0.749  5.186   0.30 14.10 ?  156 PHE   A N    1 
ATOM   3575 N  N    T PHE   A 1 156 ? 11.441 -0.931  4.778   0.30 14.88 ?  156 PHE   A N    1 
ATOM   3576 C  CA   A PHE   A 1 156 ? 10.789 0.452   5.334   0.40 16.88 ?  156 PHE   A CA   1 
ATOM   3577 C  CA   B PHE   A 1 156 ? 11.134 0.625   5.435   0.30 15.55 ?  156 PHE   A CA   1 
ATOM   3578 C  CA   T PHE   A 1 156 ? 11.014 0.440   5.058   0.30 15.25 ?  156 PHE   A CA   1 
ATOM   3579 C  C    A PHE   A 1 156 ? 9.334  0.603   4.904   0.40 16.84 ?  156 PHE   A C    1 
ATOM   3580 C  C    B PHE   A 1 156 ? 9.643  0.805   5.174   0.30 15.57 ?  156 PHE   A C    1 
ATOM   3581 C  C    T PHE   A 1 156 ? 9.552  0.658   4.688   0.30 15.51 ?  156 PHE   A C    1 
ATOM   3582 O  O    A PHE   A 1 156 ? 8.505  1.114   5.669   0.40 17.22 ?  156 PHE   A O    1 
ATOM   3583 O  O    B PHE   A 1 156 ? 8.925  1.406   5.981   0.30 15.74 ?  156 PHE   A O    1 
ATOM   3584 O  O    T PHE   A 1 156 ? 8.799  1.287   5.442   0.30 15.67 ?  156 PHE   A O    1 
ATOM   3585 C  CB   A PHE   A 1 156 ? 11.643 1.578   4.742   0.40 18.12 ?  156 PHE   A CB   1 
ATOM   3586 C  CB   B PHE   A 1 156 ? 11.947 1.554   4.534   0.30 16.30 ?  156 PHE   A CB   1 
ATOM   3587 C  CB   T PHE   A 1 156 ? 11.909 1.412   4.282   0.30 15.16 ?  156 PHE   A CB   1 
ATOM   3588 C  CG   A PHE   A 1 156 ? 11.147 2.966   5.076   0.40 19.40 ?  156 PHE   A CG   1 
ATOM   3589 C  CG   B PHE   A 1 156 ? 11.578 3.000   4.656   0.30 16.80 ?  156 PHE   A CG   1 
ATOM   3590 C  CG   T PHE   A 1 156 ? 11.573 2.871   4.491   0.30 14.76 ?  156 PHE   A CG   1 
ATOM   3591 C  CD1  A PHE   A 1 156 ? 11.086 3.390   6.392   0.40 19.64 ?  156 PHE   A CD1  1 
ATOM   3592 C  CD1  B PHE   A 1 156 ? 12.160 3.790   5.635   0.30 16.89 ?  156 PHE   A CD1  1 
ATOM   3593 C  CD1  T PHE   A 1 156 ? 11.925 3.514   5.670   0.30 15.72 ?  156 PHE   A CD1  1 
ATOM   3594 C  CD2  A PHE   A 1 156 ? 10.764 3.849   4.074   0.40 20.01 ?  156 PHE   A CD2  1 
ATOM   3595 C  CD2  B PHE   A 1 156 ? 10.661 3.573   3.791   0.30 17.52 ?  156 PHE   A CD2  1 
ATOM   3596 C  CD2  T PHE   A 1 156 ? 10.935 3.604   3.499   0.30 15.05 ?  156 PHE   A CD2  1 
ATOM   3597 C  CE1  A PHE   A 1 156 ? 10.640 4.662   6.708   0.40 20.29 ?  156 PHE   A CE1  1 
ATOM   3598 C  CE1  B PHE   A 1 156 ? 11.829 5.124   5.754   0.30 17.21 ?  156 PHE   A CE1  1 
ATOM   3599 C  CE1  T PHE   A 1 156 ? 11.630 4.854   5.865   0.30 16.49 ?  156 PHE   A CE1  1 
ATOM   3600 C  CE2  A PHE   A 1 156 ? 10.314 5.123   4.385   0.40 20.71 ?  156 PHE   A CE2  1 
ATOM   3601 C  CE2  B PHE   A 1 156 ? 10.322 4.906   3.906   0.30 17.98 ?  156 PHE   A CE2  1 
ATOM   3602 C  CE2  T PHE   A 1 156 ? 10.640 4.946   3.686   0.30 15.92 ?  156 PHE   A CE2  1 
ATOM   3603 C  CZ   A PHE   A 1 156 ? 10.256 5.529   5.703   0.40 20.68 ?  156 PHE   A CZ   1 
ATOM   3604 C  CZ   B PHE   A 1 156 ? 10.911 5.685   4.888   0.30 17.61 ?  156 PHE   A CZ   1 
ATOM   3605 C  CZ   T PHE   A 1 156 ? 10.989 5.572   4.872   0.30 16.39 ?  156 PHE   A CZ   1 
ATOM   3606 H  H    A PHE   A 1 156 ? 11.971 -0.817  4.364   0.40 18.19 ?  156 PHE   A H    1 
ATOM   3607 H  H    B PHE   A 1 156 ? 12.122 -0.833  4.544   0.30 16.90 ?  156 PHE   A H    1 
ATOM   3608 H  H    T PHE   A 1 156 ? 12.006 -1.003  4.134   0.30 17.84 ?  156 PHE   A H    1 
ATOM   3609 H  HA   A PHE   A 1 156 ? 10.827 0.532   6.298   0.40 20.23 ?  156 PHE   A HA   1 
ATOM   3610 H  HA   B PHE   A 1 156 ? 11.319 0.856   6.359   0.30 18.64 ?  156 PHE   A HA   1 
ATOM   3611 H  HA   T PHE   A 1 156 ? 11.121 0.619   6.006   0.30 18.28 ?  156 PHE   A HA   1 
ATOM   3612 H  HB2  A PHE   A 1 156 ? 12.550 1.498   5.084   0.40 21.72 ?  156 PHE   A HB2  1 
ATOM   3613 H  HB2  B PHE   A 1 156 ? 12.883 1.470   4.769   0.30 19.54 ?  156 PHE   A HB2  1 
ATOM   3614 H  HB2  T PHE   A 1 156 ? 12.829 1.275   4.561   0.30 18.17 ?  156 PHE   A HB2  1 
ATOM   3615 H  HB3  A PHE   A 1 156 ? 11.652 1.491   3.776   0.40 21.72 ?  156 PHE   A HB3  1 
ATOM   3616 H  HB3  B PHE   A 1 156 ? 11.818 1.289   3.610   0.30 19.54 ?  156 PHE   A HB3  1 
ATOM   3617 H  HB3  T PHE   A 1 156 ? 11.823 1.221   3.335   0.30 18.17 ?  156 PHE   A HB3  1 
ATOM   3618 H  HD1  A PHE   A 1 156 ? 11.344 2.810   7.074   0.40 23.54 ?  156 PHE   A HD1  1 
ATOM   3619 H  HD1  B PHE   A 1 156 ? 12.779 3.411   6.220   0.30 20.25 ?  156 PHE   A HD1  1 
ATOM   3620 H  HD1  T PHE   A 1 156 ? 12.356 3.036   6.344   0.30 18.85 ?  156 PHE   A HD1  1 
ATOM   3621 H  HD2  A PHE   A 1 156 ? 10.804 3.578   3.186   0.40 23.99 ?  156 PHE   A HD2  1 
ATOM   3622 H  HD2  B PHE   A 1 156 ? 10.265 3.051   3.130   0.30 21.00 ?  156 PHE   A HD2  1 
ATOM   3623 H  HD2  T PHE   A 1 156 ? 10.697 3.185   2.705   0.30 18.04 ?  156 PHE   A HD2  1 
ATOM   3624 H  HE1  A PHE   A 1 156 ? 10.601 4.932   7.598   0.40 24.33 ?  156 PHE   A HE1  1 
ATOM   3625 H  HE1  B PHE   A 1 156 ? 12.223 5.640   6.419   0.30 20.63 ?  156 PHE   A HE1  1 
ATOM   3626 H  HE1  T PHE   A 1 156 ? 11.865 5.271   6.665   0.30 19.77 ?  156 PHE   A HE1  1 
ATOM   3627 H  HE2  A PHE   A 1 156 ? 10.059 5.705   3.706   0.40 24.83 ?  156 PHE   A HE2  1 
ATOM   3628 H  HE2  B PHE   A 1 156 ? 9.704  5.280   3.322   0.30 21.55 ?  156 PHE   A HE2  1 
ATOM   3629 H  HE2  T PHE   A 1 156 ? 10.204 5.423   3.021   0.30 19.08 ?  156 PHE   A HE2  1 
ATOM   3630 H  HZ   A PHE   A 1 156 ? 9.956  6.384   5.916   0.40 24.79 ?  156 PHE   A HZ   1 
ATOM   3631 H  HZ   B PHE   A 1 156 ? 10.684 6.581   4.970   0.30 21.11 ?  156 PHE   A HZ   1 
ATOM   3632 H  HZ   T PHE   A 1 156 ? 10.787 6.469   5.005   0.30 19.64 ?  156 PHE   A HZ   1 
ATOM   3633 N  N    A ASP   A 1 157 ? 9.008  0.189   3.686   0.40 17.02 ?  157 ASP   A N    1 
ATOM   3634 N  N    B ASP   A 1 157 ? 9.162  0.282   4.053   0.30 15.66 ?  157 ASP   A N    1 
ATOM   3635 N  N    T ASP   A 1 157 ? 9.139  0.151   3.534   0.30 15.62 ?  157 ASP   A N    1 
ATOM   3636 C  CA   A ASP   A 1 157 ? 7.686  0.442   3.124   0.40 18.18 ?  157 ASP   A CA   1 
ATOM   3637 C  CA   B ASP   A 1 157 ? 7.852  0.614   3.514   0.30 16.72 ?  157 ASP   A CA   1 
ATOM   3638 C  CA   T ASP   A 1 157 ? 7.833  0.447   2.963   0.30 16.13 ?  157 ASP   A CA   1 
ATOM   3639 C  C    A ASP   A 1 157 ? 6.705  -0.591  3.664   0.40 18.66 ?  157 ASP   A C    1 
ATOM   3640 C  C    B ASP   A 1 157 ? 6.814  -0.425  3.927   0.30 17.67 ?  157 ASP   A C    1 
ATOM   3641 C  C    T ASP   A 1 157 ? 6.802  -0.521  3.532   0.30 16.87 ?  157 ASP   A C    1 
ATOM   3642 O  O    A ASP   A 1 157 ? 6.824  -1.785  3.371   0.40 17.85 ?  157 ASP   A O    1 
ATOM   3643 O  O    B ASP   A 1 157 ? 7.058  -1.632  3.841   0.30 17.38 ?  157 ASP   A O    1 
ATOM   3644 O  O    T ASP   A 1 157 ? 6.888  -1.732  3.301   0.30 16.35 ?  157 ASP   A O    1 
ATOM   3645 C  CB   A ASP   A 1 157 ? 7.753  0.397   1.602   0.40 19.34 ?  157 ASP   A CB   1 
ATOM   3646 C  CB   B ASP   A 1 157 ? 7.954  0.666   1.991   0.30 16.73 ?  157 ASP   A CB   1 
ATOM   3647 C  CB   T ASP   A 1 157 ? 7.933  0.299   1.448   0.30 16.25 ?  157 ASP   A CB   1 
ATOM   3648 C  CG   A ASP   A 1 157 ? 6.449  0.820   0.952   0.40 20.34 ?  157 ASP   A CG   1 
ATOM   3649 C  CG   B ASP   A 1 157 ? 6.725  1.230   1.341   0.30 16.64 ?  157 ASP   A CG   1 
ATOM   3650 C  CG   T ASP   A 1 157 ? 6.787  0.941   0.722   0.30 15.63 ?  157 ASP   A CG   1 
ATOM   3651 O  OD1  A ASP   A 1 157 ? 6.018  1.971   1.163   0.40 21.10 ?  157 ASP   A OD1  1 
ATOM   3652 O  OD1  B ASP   A 1 157 ? 5.688  0.535   1.355   0.30 16.87 ?  157 ASP   A OD1  1 
ATOM   3653 O  OD1  T ASP   A 1 157 ? 5.695  0.336   0.715   0.30 15.12 ?  157 ASP   A OD1  1 
ATOM   3654 O  OD2  A ASP   A 1 157 ? 5.840  -0.010  0.245   0.40 20.29 -1 157 ASP   A OD2  1 
ATOM   3655 O  OD2  B ASP   A 1 157 ? 6.797  2.363   0.818   0.30 16.56 -1 157 ASP   A OD2  1 
ATOM   3656 O  OD2  T ASP   A 1 157 ? 6.966  2.047   0.170   0.30 15.64 -1 157 ASP   A OD2  1 
ATOM   3657 H  H    A ASP   A 1 157 ? 9.539  -0.245  3.161   0.40 20.40 ?  157 ASP   A H    1 
ATOM   3658 H  H    B ASP   A 1 157 ? 9.599  -0.279  3.571   0.30 18.77 ?  157 ASP   A H    1 
ATOM   3659 H  H    T ASP   A 1 157 ? 9.615  -0.375  3.047   0.30 18.73 ?  157 ASP   A H    1 
ATOM   3660 H  HA   A ASP   A 1 157 ? 7.388  1.323   3.397   0.40 21.80 ?  157 ASP   A HA   1 
ATOM   3661 H  HA   B ASP   A 1 157 ? 7.579  1.486   3.846   0.30 20.04 ?  157 ASP   A HA   1 
ATOM   3662 H  HA   T ASP   A 1 157 ? 7.573  1.357   3.181   0.30 19.34 ?  157 ASP   A HA   1 
ATOM   3663 H  HB2  A ASP   A 1 157 ? 8.501  0.954   1.309   0.40 23.19 ?  157 ASP   A HB2  1 
ATOM   3664 H  HB2  B ASP   A 1 157 ? 8.715  1.212   1.746   0.30 20.05 ?  157 ASP   A HB2  1 
ATOM   3665 H  HB2  T ASP   A 1 157 ? 8.759  0.700   1.148   0.30 19.48 ?  157 ASP   A HB2  1 
ATOM   3666 H  HB3  A ASP   A 1 157 ? 7.904  -0.513  1.317   0.40 23.19 ?  157 ASP   A HB3  1 
ATOM   3667 H  HB3  B ASP   A 1 157 ? 8.064  -0.236  1.658   0.30 20.05 ?  157 ASP   A HB3  1 
ATOM   3668 H  HB3  T ASP   A 1 157 ? 7.925  -0.644  1.228   0.30 19.48 ?  157 ASP   A HB3  1 
ATOM   3669 N  N    A LYS   A 1 158 ? 5.727  -0.130  4.451   0.40 20.50 ?  158 LYS   A N    1 
ATOM   3670 N  N    B LYS   A 1 158 ? 5.642  0.052   4.356   0.30 19.19 ?  158 LYS   A N    1 
ATOM   3671 N  N    T LYS   A 1 158 ? 5.826  0.012   4.275   0.30 18.75 ?  158 LYS   A N    1 
ATOM   3672 C  CA   A LYS   A 1 158 ? 4.758  -1.050  5.040   0.40 21.73 ?  158 LYS   A CA   1 
ATOM   3673 C  CA   B LYS   A 1 158 ? 4.624  -0.858  4.875   0.30 20.49 ?  158 LYS   A CA   1 
ATOM   3674 C  CA   T LYS   A 1 158 ? 4.839  -0.853  4.918   0.30 20.62 ?  158 LYS   A CA   1 
ATOM   3675 C  C    A LYS   A 1 158 ? 3.983  -1.791  3.961   0.40 21.25 ?  158 LYS   A C    1 
ATOM   3676 C  C    B LYS   A 1 158 ? 3.957  -1.645  3.754   0.30 19.97 ?  158 LYS   A C    1 
ATOM   3677 C  C    T LYS   A 1 158 ? 4.055  -1.654  3.888   0.30 20.61 ?  158 LYS   A C    1 
ATOM   3678 O  O    A LYS   A 1 158 ? 3.768  -3.005  4.063   0.40 21.37 ?  158 LYS   A O    1 
ATOM   3679 O  O    B LYS   A 1 158 ? 3.758  -2.859  3.876   0.30 19.96 ?  158 LYS   A O    1 
ATOM   3680 O  O    T LYS   A 1 158 ? 3.817  -2.854  4.073   0.30 20.76 ?  158 LYS   A O    1 
ATOM   3681 C  CB   A LYS   A 1 158 ? 3.808  -0.296  5.975   0.40 23.24 ?  158 LYS   A CB   1 
ATOM   3682 C  CB   B LYS   A 1 158 ? 3.583  -0.085  5.687   0.30 22.65 ?  158 LYS   A CB   1 
ATOM   3683 C  CB   T LYS   A 1 158 ? 3.893  -0.033  5.800   0.30 22.85 ?  158 LYS   A CB   1 
ATOM   3684 C  CG   A LYS   A 1 158 ? 2.556  -1.078  6.396   0.40 24.85 ?  158 LYS   A CG   1 
ATOM   3685 C  CG   B LYS   A 1 158 ? 2.400  -0.924  6.181   0.30 24.62 ?  158 LYS   A CG   1 
ATOM   3686 C  CG   T LYS   A 1 158 ? 2.655  -0.800  6.279   0.30 24.89 ?  158 LYS   A CG   1 
ATOM   3687 C  CD   A LYS   A 1 158 ? 2.881  -2.363  7.166   0.40 25.83 ?  158 LYS   A CD   1 
ATOM   3688 C  CD   B LYS   A 1 158 ? 2.850  -2.153  6.966   0.30 26.08 ?  158 LYS   A CD   1 
ATOM   3689 C  CD   T LYS   A 1 158 ? 3.017  -2.027  7.115   0.30 26.47 ?  158 LYS   A CD   1 
ATOM   3690 C  CE   A LYS   A 1 158 ? 1.603  -3.044  7.662   0.40 26.38 ?  158 LYS   A CE   1 
ATOM   3691 C  CE   B LYS   A 1 158 ? 1.720  -2.740  7.797   0.30 27.07 ?  158 LYS   A CE   1 
ATOM   3692 C  CE   T LYS   A 1 158 ? 1.773  -2.831  7.489   0.30 27.61 ?  158 LYS   A CE   1 
ATOM   3693 N  NZ   A LYS   A 1 158 ? 1.844  -4.387  8.271   0.40 26.37 ?  158 LYS   A NZ   1 
ATOM   3694 N  NZ   B LYS   A 1 158 ? 2.092  -4.046  8.418   0.30 27.52 ?  158 LYS   A NZ   1 
ATOM   3695 N  NZ   T LYS   A 1 158 ? 2.089  -4.047  8.295   0.30 28.09 ?  158 LYS   A NZ   1 
ATOM   3696 H  H    A LYS   A 1 158 ? 5.610  0.693   4.651   0.40 24.58 ?  158 LYS   A H    1 
ATOM   3697 H  H    B LYS   A 1 158 ? 5.417  0.879   4.347   0.30 23.00 ?  158 LYS   A H    1 
ATOM   3698 H  H    T LYS   A 1 158 ? 5.716  0.851   4.417   0.30 22.48 ?  158 LYS   A H    1 
ATOM   3699 H  HA   A LYS   A 1 158 ? 5.231  -1.710  5.568   0.40 26.05 ?  158 LYS   A HA   1 
ATOM   3700 H  HA   B LYS   A 1 158 ? 5.049  -1.495  5.471   0.30 24.56 ?  158 LYS   A HA   1 
ATOM   3701 H  HA   T LYS   A 1 158 ? 5.301  -1.483  5.494   0.30 24.72 ?  158 LYS   A HA   1 
ATOM   3702 H  HB2  A LYS   A 1 158 ? 4.292  -0.062  6.785   0.40 27.87 ?  158 LYS   A HB2  1 
ATOM   3703 H  HB2  B LYS   A 1 158 ? 4.017  0.294   6.467   0.30 27.16 ?  158 LYS   A HB2  1 
ATOM   3704 H  HB2  T LYS   A 1 158 ? 4.377  0.261   6.590   0.30 27.40 ?  158 LYS   A HB2  1 
ATOM   3705 H  HB3  A LYS   A 1 158 ? 3.513  0.514   5.530   0.40 27.87 ?  158 LYS   A HB3  1 
ATOM   3706 H  HB3  B LYS   A 1 158 ? 3.225  0.626   5.135   0.30 27.16 ?  158 LYS   A HB3  1 
ATOM   3707 H  HB3  T LYS   A 1 158 ? 3.586  0.737   5.299   0.30 27.40 ?  158 LYS   A HB3  1 
ATOM   3708 H  HG2  A LYS   A 1 158 ? 2.022  -0.515  6.975   0.40 29.80 ?  158 LYS   A HG2  1 
ATOM   3709 H  HG2  B LYS   A 1 158 ? 1.849  -0.382  6.767   0.30 29.53 ?  158 LYS   A HG2  1 
ATOM   3710 H  HG2  T LYS   A 1 158 ? 2.120  -0.214  6.834   0.30 29.84 ?  158 LYS   A HG2  1 
ATOM   3711 H  HG3  A LYS   A 1 158 ? 2.040  -1.316  5.609   0.40 29.80 ?  158 LYS   A HG3  1 
ATOM   3712 H  HG3  B LYS   A 1 158 ? 1.879  -1.227  5.422   0.30 29.53 ?  158 LYS   A HG3  1 
ATOM   3713 H  HG3  T LYS   A 1 158 ? 2.132  -1.094  5.516   0.30 29.84 ?  158 LYS   A HG3  1 
ATOM   3714 H  HD2  A LYS   A 1 158 ? 3.349  -2.979  6.582   0.40 30.98 ?  158 LYS   A HD2  1 
ATOM   3715 H  HD2  B LYS   A 1 158 ? 3.166  -2.834  6.352   0.30 31.27 ?  158 LYS   A HD2  1 
ATOM   3716 H  HD2  T LYS   A 1 158 ? 3.607  -2.605  6.607   0.30 31.74 ?  158 LYS   A HD2  1 
ATOM   3717 H  HD3  A LYS   A 1 158 ? 3.430  -2.145  7.936   0.40 30.98 ?  158 LYS   A HD3  1 
ATOM   3718 H  HD3  B LYS   A 1 158 ? 3.552  -1.900  7.574   0.30 31.27 ?  158 LYS   A HD3  1 
ATOM   3719 H  HD3  T LYS   A 1 158 ? 3.451  -1.740  7.934   0.30 31.74 ?  158 LYS   A HD3  1 
ATOM   3720 H  HE2  A LYS   A 1 158 ? 1.187  -2.481  8.334   0.40 31.63 ?  158 LYS   A HE2  1 
ATOM   3721 H  HE2  B LYS   A 1 158 ? 1.499  -2.118  8.509   0.30 32.47 ?  158 LYS   A HE2  1 
ATOM   3722 H  HE2  T LYS   A 1 158 ? 1.177  -2.271  8.011   0.30 33.11 ?  158 LYS   A HE2  1 
ATOM   3723 H  HE3  A LYS   A 1 158 ? 0.999  -3.160  6.913   0.40 31.63 ?  158 LYS   A HE3  1 
ATOM   3724 H  HE3  B LYS   A 1 158 ? 0.951  -2.883  7.229   0.30 32.47 ?  158 LYS   A HE3  1 
ATOM   3725 H  HE3  T LYS   A 1 158 ? 1.327  -3.120  6.677   0.30 33.11 ?  158 LYS   A HE3  1 
ATOM   3726 H  HZ1  A LYS   A 1 158 ? 1.074  -4.740  8.543   0.40 31.62 ?  158 LYS   A HZ1  1 
ATOM   3727 H  HZ1  B LYS   A 1 158 ? 1.411  -4.360  8.897   0.30 33.00 ?  158 LYS   A HZ1  1 
ATOM   3728 H  HZ1  T LYS   A 1 158 ? 1.340  -4.486  8.492   0.30 33.68 ?  158 LYS   A HZ1  1 
ATOM   3729 H  HZ2  A LYS   A 1 158 ? 2.215  -4.930  7.671   0.40 31.62 ?  158 LYS   A HZ2  1 
ATOM   3730 H  HZ2  B LYS   A 1 158 ? 2.297  -4.636  7.783   0.30 33.00 ?  158 LYS   A HZ2  1 
ATOM   3731 H  HZ2  T LYS   A 1 158 ? 2.627  -4.587  7.835   0.30 33.68 ?  158 LYS   A HZ2  1 
ATOM   3732 H  HZ3  A LYS   A 1 158 ? 2.390  -4.311  8.970   0.40 31.62 ?  158 LYS   A HZ3  1 
ATOM   3733 H  HZ3  B LYS   A 1 158 ? 2.797  -3.941  8.952   0.30 33.00 ?  158 LYS   A HZ3  1 
ATOM   3734 H  HZ3  T LYS   A 1 158 ? 2.494  -3.814  9.053   0.30 33.68 ?  158 LYS   A HZ3  1 
ATOM   3735 N  N    A ASN   A 1 159 ? 3.557  -1.084  2.916   0.40 21.19 ?  159 ASN   A N    1 
ATOM   3736 N  N    B ASN   A 1 159 ? 3.599  -0.976  2.656   0.30 20.26 ?  159 ASN   A N    1 
ATOM   3737 N  N    T ASN   A 1 159 ? 3.637  -1.014  2.803   0.30 20.99 ?  159 ASN   A N    1 
ATOM   3738 C  CA   A ASN   A 1 159 ? 2.856  -1.757  1.829   0.40 20.30 ?  159 ASN   A CA   1 
ATOM   3739 C  CA   B ASN   A 1 159 ? 2.968  -1.689  1.551   0.30 20.65 ?  159 ASN   A CA   1 
ATOM   3740 C  CA   T ASN   A 1 159 ? 2.882  -1.712  1.772   0.30 21.06 ?  159 ASN   A CA   1 
ATOM   3741 C  C    A ASN   A 1 159 ? 3.730  -2.848  1.216   0.40 19.06 ?  159 ASN   A C    1 
ATOM   3742 C  C    B ASN   A 1 159 ? 3.884  -2.765  0.989   0.30 19.66 ?  159 ASN   A C    1 
ATOM   3743 C  C    T ASN   A 1 159 ? 3.705  -2.838  1.149   0.30 20.80 ?  159 ASN   A C    1 
ATOM   3744 O  O    A ASN   A 1 159 ? 3.282  -3.983  1.017   0.40 18.04 ?  159 ASN   A O    1 
ATOM   3745 O  O    B ASN   A 1 159 ? 3.405  -3.808  0.531   0.30 19.48 ?  159 ASN   A O    1 
ATOM   3746 O  O    T ASN   A 1 159 ? 3.187  -3.922  0.894   0.30 20.58 ?  159 ASN   A O    1 
ATOM   3747 C  CB   A ASN   A 1 159 ? 2.383  -0.734  0.792   0.40 21.47 ?  159 ASN   A CB   1 
ATOM   3748 C  CB   B ASN   A 1 159 ? 2.544  -0.713  0.454   0.30 22.20 ?  159 ASN   A CB   1 
ATOM   3749 C  CB   T ASN   A 1 159 ? 2.386  -0.733  0.704   0.30 21.76 ?  159 ASN   A CB   1 
ATOM   3750 C  CG   A ASN   A 1 159 ? 1.173  0.060   1.266   0.40 23.00 ?  159 ASN   A CG   1 
ATOM   3751 C  CG   B ASN   A 1 159 ? 1.247  0.000   0.780   0.30 23.75 ?  159 ASN   A CG   1 
ATOM   3752 C  CG   T ASN   A 1 159 ? 1.199  0.092   1.177   0.30 22.61 ?  159 ASN   A CG   1 
ATOM   3753 O  OD1  A ASN   A 1 159 ? 0.365  -0.442  2.044   0.40 23.75 ?  159 ASN   A OD1  1 
ATOM   3754 O  OD1  B ASN   A 1 159 ? 0.182  -0.616  0.813   0.30 24.48 ?  159 ASN   A OD1  1 
ATOM   3755 O  OD1  T ASN   A 1 159 ? 0.418  -0.357  2.013   0.30 23.15 ?  159 ASN   A OD1  1 
ATOM   3756 N  ND2  A ASN   A 1 159 ? 1.044  1.298   0.798   0.40 23.59 ?  159 ASN   A ND2  1 
ATOM   3757 N  ND2  B ASN   A 1 159 ? 1.327  1.304   1.012   0.30 24.33 ?  159 ASN   A ND2  1 
ATOM   3758 N  ND2  T ASN   A 1 159 ? 1.058  1.297   0.642   0.30 22.89 ?  159 ASN   A ND2  1 
ATOM   3759 H  H    A ASN   A 1 159 ? 3.658  -0.234  2.819   0.40 25.41 ?  159 ASN   A H    1 
ATOM   3760 H  H    B ASN   A 1 159 ? 3.712  -0.137  2.529   0.30 24.29 ?  159 ASN   A H    1 
ATOM   3761 H  H    T ASN   A 1 159 ? 3.770  -0.180  2.649   0.30 25.17 ?  159 ASN   A H    1 
ATOM   3762 H  HA   A ASN   A 1 159 ? 2.067  -2.186  2.190   0.40 24.34 ?  159 ASN   A HA   1 
ATOM   3763 H  HA   B ASN   A 1 159 ? 2.171  -2.132  1.878   0.30 24.76 ?  159 ASN   A HA   1 
ATOM   3764 H  HA   T ASN   A 1 159 ? 2.106  -2.120  2.180   0.30 25.26 ?  159 ASN   A HA   1 
ATOM   3765 H  HB2  A ASN   A 1 159 ? 3.093  -0.101  0.613   0.40 25.75 ?  159 ASN   A HB2  1 
ATOM   3766 H  HB2  B ASN   A 1 159 ? 3.233  -0.043  0.341   0.30 26.61 ?  159 ASN   A HB2  1 
ATOM   3767 H  HB2  T ASN   A 1 159 ? 3.100  -0.121  0.474   0.30 26.09 ?  159 ASN   A HB2  1 
ATOM   3768 H  HB3  A ASN   A 1 159 ? 2.133  -1.197  -0.023  0.40 25.75 ?  159 ASN   A HB3  1 
ATOM   3769 H  HB3  B ASN   A 1 159 ? 2.416  -1.203  -0.374  0.30 26.61 ?  159 ASN   A HB3  1 
ATOM   3770 H  HB3  T ASN   A 1 159 ? 2.111  -1.234  -0.082  0.30 26.09 ?  159 ASN   A HB3  1 
ATOM   3771 H  HD21 A ASN   A 1 159 ? 0.374  1.782   1.038   0.40 28.29 ?  159 ASN   A HD21 1 
ATOM   3772 H  HD21 B ASN   A 1 159 ? 0.617  1.750   1.199   0.30 29.17 ?  159 ASN   A HD21 1 
ATOM   3773 H  HD21 T ASN   A 1 159 ? 0.399  1.795   0.879   0.30 27.45 ?  159 ASN   A HD21 1 
ATOM   3774 H  HD22 A ASN   A 1 159 ? 1.633  1.615   0.262   0.40 28.29 ?  159 ASN   A HD22 1 
ATOM   3775 H  HD22 B ASN   A 1 159 ? 2.089  1.699   0.974   0.30 29.17 ?  159 ASN   A HD22 1 
ATOM   3776 H  HD22 T ASN   A 1 159 ? 1.626  1.577   0.064   0.30 27.45 ?  159 ASN   A HD22 1 
ATOM   3777 N  N    A LEU   A 1 160 ? 5.003  -2.541  0.957   0.40 18.14 ?  160 LEU   A N    1 
ATOM   3778 N  N    B LEU   A 1 160 ? 5.197  -2.541  1.021   0.30 18.79 ?  160 LEU   A N    1 
ATOM   3779 N  N    T LEU   A 1 160 ? 4.991  -2.592  0.925   0.30 20.59 ?  160 LEU   A N    1 
ATOM   3780 C  CA   A LEU   A 1 160 ? 5.893  -3.554  0.397   0.40 17.27 ?  160 LEU   A CA   1 
ATOM   3781 C  CA   B LEU   A 1 160 ? 6.118  -3.581  0.577   0.30 17.59 ?  160 LEU   A CA   1 
ATOM   3782 C  CA   T LEU   A 1 160 ? 5.862  -3.619  0.365   0.30 20.26 ?  160 LEU   A CA   1 
ATOM   3783 C  C    A LEU   A 1 160 ? 6.078  -4.719  1.363   0.40 15.89 ?  160 LEU   A C    1 
ATOM   3784 C  C    B LEU   A 1 160 ? 6.216  -4.703  1.604   0.30 16.06 ?  160 LEU   A C    1 
ATOM   3785 O  O    A LEU   A 1 160 ? 6.086  -5.885  0.951   0.40 15.48 ?  160 LEU   A O    1 
ATOM   3786 O  O    B LEU   A 1 160 ? 6.223  -5.885  1.242   0.30 15.23 ?  160 LEU   A O    1 
ATOM   3787 C  CB   A LEU   A 1 160 ? 7.240  -2.927  0.049   0.40 17.16 ?  160 LEU   A CB   1 
ATOM   3788 C  CB   B LEU   A 1 160 ? 7.496  -2.986  0.298   0.30 18.15 ?  160 LEU   A CB   1 
ATOM   3789 C  CB   T LEU   A 1 160 ? 7.237  -3.038  0.043   0.30 19.83 ?  160 LEU   A CB   1 
ATOM   3790 C  CG   A LEU   A 1 160 ? 8.313  -3.924  -0.376  0.40 18.12 ?  160 LEU   A CG   1 
ATOM   3791 C  CG   B LEU   A 1 160 ? 8.522  -4.008  -0.194  0.30 18.92 ?  160 LEU   A CG   1 
ATOM   3792 C  CG   T LEU   A 1 160 ? 8.296  -4.054  -0.377  0.30 19.94 ?  160 LEU   A CG   1 
ATOM   3793 C  CD1  A LEU   A 1 160 ? 7.840  -4.741  -1.562  0.40 19.00 ?  160 LEU   A CD1  1 
ATOM   3794 C  CD1  B LEU   A 1 160 ? 8.055  -4.663  -1.484  0.30 19.31 ?  160 LEU   A CD1  1 
ATOM   3795 C  CD1  T LEU   A 1 160 ? 7.845  -4.831  -1.596  0.30 20.33 ?  160 LEU   A CD1  1 
ATOM   3796 C  CD2  A LEU   A 1 160 ? 9.601  -3.199  -0.701  0.40 18.03 ?  160 LEU   A CD2  1 
ATOM   3797 C  CD2  B LEU   A 1 160 ? 9.877  -3.356  -0.385  0.30 19.06 ?  160 LEU   A CD2  1 
ATOM   3798 C  CD2  T LEU   A 1 160 ? 9.613  -3.351  -0.647  0.30 19.69 ?  160 LEU   A CD2  1 
ATOM   3799 H  H    A LEU   A 1 160 ? 5.369  -1.772  1.107   0.40 21.75 ?  160 LEU   A H    1 
ATOM   3800 H  H    B LEU   A 1 160 ? 5.570  -1.812  1.289   0.30 22.53 ?  160 LEU   A H    1 
ATOM   3801 H  H    T LEU   A 1 160 ? 5.385  -1.845  1.094   0.30 24.69 ?  160 LEU   A H    1 
ATOM   3802 H  HA   A LEU   A 1 160 ? 5.500  -3.891  -0.420  0.40 20.70 ?  160 LEU   A HA   1 
ATOM   3803 H  HA   B LEU   A 1 160 ? 5.781  -3.954  -0.251  0.30 21.08 ?  160 LEU   A HA   1 
ATOM   3804 H  HB2  A LEU   A 1 160 ? 7.119  -2.285  -0.676  0.40 20.57 ?  160 LEU   A HB2  1 
ATOM   3805 H  HB2  B LEU   A 1 160 ? 7.410  -2.300  -0.384  0.30 21.76 ?  160 LEU   A HB2  1 
ATOM   3806 H  HB2  T LEU   A 1 160 ? 7.140  -2.388  -0.675  0.30 23.78 ?  160 LEU   A HB2  1 
ATOM   3807 H  HB3  A LEU   A 1 160 ? 7.572  -2.471  0.834   0.40 20.57 ?  160 LEU   A HB3  1 
ATOM   3808 H  HB3  B LEU   A 1 160 ? 7.838  -2.593  1.116   0.30 21.76 ?  160 LEU   A HB3  1 
ATOM   3809 H  HB3  T LEU   A 1 160 ? 7.575  -2.601  0.838   0.30 23.78 ?  160 LEU   A HB3  1 
ATOM   3810 H  HG   A LEU   A 1 160 ? 8.495  -4.529  0.359   0.40 21.72 ?  160 LEU   A HG   1 
ATOM   3811 H  HG   B LEU   A 1 160 ? 8.623  -4.704  0.474   0.30 22.68 ?  160 LEU   A HG   1 
ATOM   3812 H  HG   T LEU   A 1 160 ? 8.437  -4.680  0.350   0.30 23.90 ?  160 LEU   A HG   1 
ATOM   3813 H  HD11 A LEU   A 1 160 ? 8.569  -5.299  -1.866  0.40 22.78 ?  160 LEU   A HD11 1 
ATOM   3814 H  HD11 B LEU   A 1 160 ? 8.781  -5.186  -1.851  0.30 23.15 ?  160 LEU   A HD11 1 
ATOM   3815 H  HD11 T LEU   A 1 160 ? 8.573  -5.397  -1.894  0.30 24.37 ?  160 LEU   A HD11 1 
ATOM   3816 H  HD12 A LEU   A 1 160 ? 7.091  -5.293  -1.289  0.40 22.78 ?  160 LEU   A HD12 1 
ATOM   3817 H  HD12 B LEU   A 1 160 ? 7.298  -5.240  -1.292  0.30 23.15 ?  160 LEU   A HD12 1 
ATOM   3818 H  HD12 T LEU   A 1 160 ? 7.078  -5.374  -1.357  0.30 24.37 ?  160 LEU   A HD12 1 
ATOM   3819 H  HD13 A LEU   A 1 160 ? 7.565  -4.137  -2.270  0.40 22.78 ?  160 LEU   A HD13 1 
ATOM   3820 H  HD13 B LEU   A 1 160 ? 7.794  -3.972  -2.113  0.30 23.15 ?  160 LEU   A HD13 1 
ATOM   3821 H  HD13 T LEU   A 1 160 ? 7.603  -4.205  -2.296  0.30 24.37 ?  160 LEU   A HD13 1 
ATOM   3822 H  HD21 A LEU   A 1 160 ? 10.271 -3.849  -0.965  0.40 21.62 ?  160 LEU   A HD21 1 
ATOM   3823 H  HD21 B LEU   A 1 160 ? 10.509 -4.025  -0.694  0.30 22.85 ?  160 LEU   A HD21 1 
ATOM   3824 H  HD21 T LEU   A 1 160 ? 10.275 -4.010  -0.910  0.30 23.60 ?  160 LEU   A HD21 1 
ATOM   3825 H  HD22 A LEU   A 1 160 ? 9.441  -2.577  -1.428  0.40 21.62 ?  160 LEU   A HD22 1 
ATOM   3826 H  HD22 B LEU   A 1 160 ? 9.797  -2.649  -1.045  0.30 22.85 ?  160 LEU   A HD22 1 
ATOM   3827 H  HD22 T LEU   A 1 160 ? 9.486  -2.707  -1.362  0.30 23.60 ?  160 LEU   A HD22 1 
ATOM   3828 H  HD23 A LEU   A 1 160 ? 9.903  -2.716  0.086   0.40 21.62 ?  160 LEU   A HD23 1 
ATOM   3829 H  HD23 B LEU   A 1 160 ? 10.173 -2.987  0.461   0.30 22.85 ?  160 LEU   A HD23 1 
ATOM   3830 H  HD23 T LEU   A 1 160 ? 9.902  -2.896  0.160   0.30 23.60 ?  160 LEU   A HD23 1 
ATOM   3831 N  N    A TYR   A 1 161 ? 6.241  -4.421  2.651   0.70 16.22 ?  161 TYR   A N    1 
ATOM   3832 N  N    B TYR   A 1 161 ? 6.304  -4.352  2.889   0.30 15.77 ?  161 TYR   A N    1 
ATOM   3833 C  CA   A TYR   A 1 161 ? 6.371  -5.474  3.652   0.70 15.96 ?  161 TYR   A CA   1 
ATOM   3834 C  CA   B TYR   A 1 161 ? 6.395  -5.370  3.931   0.30 15.36 ?  161 TYR   A CA   1 
ATOM   3835 C  C    A TYR   A 1 161 ? 5.211  -6.456  3.572   0.70 16.66 ?  161 TYR   A C    1 
ATOM   3836 C  C    B TYR   A 1 161 ? 5.213  -6.330  3.868   0.30 15.85 ?  161 TYR   A C    1 
ATOM   3837 O  O    A TYR   A 1 161 ? 5.411  -7.677  3.538   0.70 16.40 ?  161 TYR   A O    1 
ATOM   3838 O  O    B TYR   A 1 161 ? 5.385  -7.553  3.936   0.30 15.22 ?  161 TYR   A O    1 
ATOM   3839 C  CB   A TYR   A 1 161 ? 6.438  -4.859  5.046   0.70 15.73 ?  161 TYR   A CB   1 
ATOM   3840 C  CB   B TYR   A 1 161 ? 6.481  -4.708  5.307   0.30 15.03 ?  161 TYR   A CB   1 
ATOM   3841 C  CG   A TYR   A 1 161 ? 6.357  -5.896  6.131   0.70 14.91 ?  161 TYR   A CG   1 
ATOM   3842 C  CG   B TYR   A 1 161 ? 6.407  -5.692  6.454   0.30 14.41 ?  161 TYR   A CG   1 
ATOM   3843 C  CD1  A TYR   A 1 161 ? 7.482  -6.612  6.510   0.70 14.49 ?  161 TYR   A CD1  1 
ATOM   3844 C  CD1  B TYR   A 1 161 ? 7.539  -6.370  6.892   0.30 14.19 ?  161 TYR   A CD1  1 
ATOM   3845 C  CD2  A TYR   A 1 161 ? 5.151  -6.179  6.764   0.70 14.86 ?  161 TYR   A CD2  1 
ATOM   3846 C  CD2  B TYR   A 1 161 ? 5.206  -5.933  7.111   0.30 14.18 ?  161 TYR   A CD2  1 
ATOM   3847 C  CE1  A TYR   A 1 161 ? 7.416  -7.572  7.490   0.70 14.04 ?  161 TYR   A CE1  1 
ATOM   3848 C  CE1  B TYR   A 1 161 ? 7.474  -7.268  7.943   0.30 14.22 ?  161 TYR   A CE1  1 
ATOM   3849 C  CE2  A TYR   A 1 161 ? 5.074  -7.141  7.747   0.70 14.37 ?  161 TYR   A CE2  1 
ATOM   3850 C  CE2  B TYR   A 1 161 ? 5.131  -6.828  8.163   0.30 14.15 ?  161 TYR   A CE2  1 
ATOM   3851 C  CZ   A TYR   A 1 161 ? 6.211  -7.836  8.107   0.70 13.85 ?  161 TYR   A CZ   1 
ATOM   3852 C  CZ   B TYR   A 1 161 ? 6.268  -7.494  8.575   0.30 14.52 ?  161 TYR   A CZ   1 
ATOM   3853 O  OH   A TYR   A 1 161 ? 6.161  -8.797  9.086   0.70 14.42 ?  161 TYR   A OH   1 
ATOM   3854 O  OH   B TYR   A 1 161 ? 6.198  -8.387  9.621   0.30 15.23 ?  161 TYR   A OH   1 
ATOM   3855 H  H    A TYR   A 1 161 ? 6.272  -3.623  2.968   0.70 19.44 ?  161 TYR   A H    1 
ATOM   3856 H  H    B TYR   A 1 161 ? 6.315  -3.541  3.175   0.30 18.90 ?  161 TYR   A H    1 
ATOM   3857 H  HA   A TYR   A 1 161 ? 7.188  -5.965  3.493   0.70 19.13 ?  161 TYR   A HA   1 
ATOM   3858 H  HA   B TYR   A 1 161 ? 7.203  -5.883  3.796   0.30 18.41 ?  161 TYR   A HA   1 
ATOM   3859 H  HB2  A TYR   A 1 161 ? 7.281  -4.388  5.144   0.70 18.86 ?  161 TYR   A HB2  1 
ATOM   3860 H  HB2  B TYR   A 1 161 ? 7.325  -4.234  5.375   0.30 18.02 ?  161 TYR   A HB2  1 
ATOM   3861 H  HB3  A TYR   A 1 161 ? 5.697  -4.243  5.161   0.70 18.86 ?  161 TYR   A HB3  1 
ATOM   3862 H  HB3  B TYR   A 1 161 ? 5.745  -4.082  5.403   0.30 18.02 ?  161 TYR   A HB3  1 
ATOM   3863 H  HD1  A TYR   A 1 161 ? 8.293  -6.439  6.093   0.70 17.37 ?  161 TYR   A HD1  1 
ATOM   3864 H  HD1  B TYR   A 1 161 ? 8.353  -6.218  6.470   0.30 17.00 ?  161 TYR   A HD1  1 
ATOM   3865 H  HD2  A TYR   A 1 161 ? 4.380  -5.717  6.523   0.70 17.82 ?  161 TYR   A HD2  1 
ATOM   3866 H  HD2  B TYR   A 1 161 ? 4.436  -5.486  6.840   0.30 17.00 ?  161 TYR   A HD2  1 
ATOM   3867 H  HE1  A TYR   A 1 161 ? 8.179  -8.046  7.732   0.70 16.82 ?  161 TYR   A HE1  1 
ATOM   3868 H  HE1  B TYR   A 1 161 ? 8.240  -7.715  8.225   0.30 17.04 ?  161 TYR   A HE1  1 
ATOM   3869 H  HE2  A TYR   A 1 161 ? 4.257  -7.325  8.166   0.70 17.23 ?  161 TYR   A HE2  1 
ATOM   3870 H  HE2  B TYR   A 1 161 ? 4.318  -6.979  8.592   0.30 16.96 ?  161 TYR   A HE2  1 
ATOM   3871 H  HH   A TYR   A 1 161 ? 6.915  -9.145  9.197   0.70 17.29 ?  161 TYR   A HH   1 
ATOM   3872 H  HH   B TYR   A 1 161 ? 5.415  -8.401  9.932   0.30 18.25 ?  161 TYR   A HH   1 
ATOM   3873 N  N    A ASP   A 1 162 ? 3.981  -5.938  3.566   0.70 17.95 ?  162 ASP   A N    1 
ATOM   3874 N  N    B ASP   A 1 162 ? 3.998  -5.793  3.740   0.30 17.04 ?  162 ASP   A N    1 
ATOM   3875 C  CA   A ASP   A 1 162 ? 2.819  -6.818  3.477   0.70 19.20 ?  162 ASP   A CA   1 
ATOM   3876 C  CA   B ASP   A 1 162 ? 2.816  -6.650  3.741   0.30 18.30 ?  162 ASP   A CA   1 
ATOM   3877 C  C    A ASP   A 1 162 ? 2.863  -7.637  2.197   0.70 18.71 ?  162 ASP   A C    1 
ATOM   3878 C  C    B ASP   A 1 162 ? 2.832  -7.625  2.569   0.30 18.50 ?  162 ASP   A C    1 
ATOM   3879 O  O    A ASP   A 1 162 ? 2.516  -8.825  2.195   0.70 18.64 ?  162 ASP   A O    1 
ATOM   3880 O  O    B ASP   A 1 162 ? 2.443  -8.790  2.718   0.30 18.02 ?  162 ASP   A O    1 
ATOM   3881 C  CB   A ASP   A 1 162 ? 1.523  -6.007  3.544   0.70 21.11 ?  162 ASP   A CB   1 
ATOM   3882 C  CB   B ASP   A 1 162 ? 1.542  -5.805  3.731   0.30 19.43 ?  162 ASP   A CB   1 
ATOM   3883 C  CG   A ASP   A 1 162 ? 1.266  -5.416  4.915   0.70 23.04 ?  162 ASP   A CG   1 
ATOM   3884 C  CG   B ASP   A 1 162 ? 1.204  -5.238  5.091   0.30 20.30 ?  162 ASP   A CG   1 
ATOM   3885 O  OD1  A ASP   A 1 162 ? 1.815  -5.935  5.908   0.70 23.59 ?  162 ASP   A OD1  1 
ATOM   3886 O  OD1  B ASP   A 1 162 ? 2.064  -5.266  5.994   0.30 20.85 ?  162 ASP   A OD1  1 
ATOM   3887 O  OD2  A ASP   A 1 162 ? 0.481  -4.442  4.999   0.70 24.23 -1 162 ASP   A OD2  1 
ATOM   3888 O  OD2  B ASP   A 1 162 ? 0.060  -4.769  5.256   0.30 20.64 -1 162 ASP   A OD2  1 
ATOM   3889 H  H    A ASP   A 1 162 ? 3.791  -5.099  3.610   0.70 21.52 ?  162 ASP   A H    1 
ATOM   3890 H  H    B ASP   A 1 162 ? 3.833  -4.952  3.656   0.30 20.43 ?  162 ASP   A H    1 
ATOM   3891 H  HA   A ASP   A 1 162 ? 2.825  -7.434  4.224   0.70 23.02 ?  162 ASP   A HA   1 
ATOM   3892 H  HA   B ASP   A 1 162 ? 2.812  -7.174  4.554   0.30 21.94 ?  162 ASP   A HA   1 
ATOM   3893 H  HB2  A ASP   A 1 162 ? 1.570  -5.274  2.915   0.70 25.31 ?  162 ASP   A HB2  1 
ATOM   3894 H  HB2  B ASP   A 1 162 ? 1.655  -5.056  3.131   0.30 23.29 ?  162 ASP   A HB2  1 
ATOM   3895 H  HB3  A ASP   A 1 162 ? 0.773  -6.585  3.329   0.70 25.31 ?  162 ASP   A HB3  1 
ATOM   3896 H  HB3  B ASP   A 1 162 ? 0.794  -6.354  3.447   0.30 23.29 ?  162 ASP   A HB3  1 
ATOM   3897 N  N    A LYS   A 1 163 ? 3.287  -7.020  1.094   0.70 19.36 ?  163 LYS   A N    1 
ATOM   3898 N  N    B LYS   A 1 163 ? 3.281  -7.176  1.395   0.30 19.22 ?  163 LYS   A N    1 
ATOM   3899 C  CA   A LYS   A 1 163 ? 3.409  -7.767  -0.150  0.70 19.63 ?  163 LYS   A CA   1 
ATOM   3900 C  CA   B LYS   A 1 163 ? 3.307  -8.070  0.241   0.30 20.09 ?  163 LYS   A CA   1 
ATOM   3901 C  C    A LYS   A 1 163 ? 4.469  -8.858  -0.035  0.70 18.43 ?  163 LYS   A C    1 
ATOM   3902 C  C    B LYS   A 1 163 ? 4.409  -9.116  0.377   0.30 19.69 ?  163 LYS   A C    1 
ATOM   3903 O  O    A LYS   A 1 163 ? 4.296  -9.960  -0.567  0.70 17.91 ?  163 LYS   A O    1 
ATOM   3904 O  O    B LYS   A 1 163 ? 4.223  -10.274 -0.013  0.30 19.62 ?  163 LYS   A O    1 
ATOM   3905 C  CB   A LYS   A 1 163 ? 3.721  -6.823  -1.311  0.70 21.77 ?  163 LYS   A CB   1 
ATOM   3906 C  CB   B LYS   A 1 163 ? 3.476  -7.271  -1.051  0.30 21.54 ?  163 LYS   A CB   1 
ATOM   3907 C  CG   A LYS   A 1 163 ? 3.782  -7.539  -2.648  0.70 24.52 ?  163 LYS   A CG   1 
ATOM   3908 C  CG   B LYS   A 1 163 ? 3.171  -8.077  -2.302  0.30 23.05 ?  163 LYS   A CG   1 
ATOM   3909 C  CD   A LYS   A 1 163 ? 4.190  -6.613  -3.775  0.70 26.81 ?  163 LYS   A CD   1 
ATOM   3910 C  CD   B LYS   A 1 163 ? 3.832  -7.486  -3.533  0.30 24.45 ?  163 LYS   A CD   1 
ATOM   3911 C  CE   A LYS   A 1 163 ? 4.117  -7.329  -5.114  0.70 28.79 ?  163 LYS   A CE   1 
ATOM   3912 C  CE   B LYS   A 1 163 ? 3.349  -8.180  -4.796  0.30 25.32 ?  163 LYS   A CE   1 
ATOM   3913 N  NZ   A LYS   A 1 163 ? 4.772  -6.554  -6.201  0.70 29.83 ?  163 LYS   A NZ   1 
ATOM   3914 N  NZ   B LYS   A 1 163 ? 4.465  -8.770  -5.586  0.30 25.90 ?  163 LYS   A NZ   1 
ATOM   3915 H  H    A LYS   A 1 163 ? 3.500  -6.183  1.043   0.70 23.21 ?  163 LYS   A H    1 
ATOM   3916 H  H    B LYS   A 1 163 ? 3.568  -6.379  1.243   0.30 23.04 ?  163 LYS   A H    1 
ATOM   3917 H  HA   A LYS   A 1 163 ? 2.560  -8.192  -0.338  0.70 23.53 ?  163 LYS   A HA   1 
ATOM   3918 H  HA   B LYS   A 1 163 ? 2.461  -8.538  0.188   0.30 24.09 ?  163 LYS   A HA   1 
ATOM   3919 H  HB2  A LYS   A 1 163 ? 3.025  -6.143  -1.369  0.70 26.10 ?  163 LYS   A HB2  1 
ATOM   3920 H  HB2  B LYS   A 1 163 ? 2.871  -6.511  -1.034  0.30 25.82 ?  163 LYS   A HB2  1 
ATOM   3921 H  HB3  A LYS   A 1 163 ? 4.580  -6.399  -1.158  0.70 26.10 ?  163 LYS   A HB3  1 
ATOM   3922 H  HB3  B LYS   A 1 163 ? 4.392  -6.961  -1.115  0.30 25.82 ?  163 LYS   A HB3  1 
ATOM   3923 H  HG2  A LYS   A 1 163 ? 4.434  -8.255  -2.602  0.70 29.41 ?  163 LYS   A HG2  1 
ATOM   3924 H  HG2  B LYS   A 1 163 ? 3.497  -8.983  -2.188  0.30 27.63 ?  163 LYS   A HG2  1 
ATOM   3925 H  HG3  A LYS   A 1 163 ? 2.905  -7.900  -2.856  0.70 29.41 ?  163 LYS   A HG3  1 
ATOM   3926 H  HG3  B LYS   A 1 163 ? 2.211  -8.084  -2.449  0.30 27.63 ?  163 LYS   A HG3  1 
ATOM   3927 H  HD2  A LYS   A 1 163 ? 3.588  -5.854  -3.801  0.70 32.15 ?  163 LYS   A HD2  1 
ATOM   3928 H  HD2  B LYS   A 1 163 ? 3.612  -6.544  -3.596  0.30 29.32 ?  163 LYS   A HD2  1 
ATOM   3929 H  HD3  A LYS   A 1 163 ? 5.103  -6.318  -3.633  0.70 32.15 ?  163 LYS   A HD3  1 
ATOM   3930 H  HD3  B LYS   A 1 163 ? 4.794  -7.603  -3.466  0.30 29.32 ?  163 LYS   A HD3  1 
ATOM   3931 H  HE2  A LYS   A 1 163 ? 4.553  -8.192  -5.039  0.70 34.52 ?  163 LYS   A HE2  1 
ATOM   3932 H  HE2  B LYS   A 1 163 ? 2.742  -8.896  -4.550  0.30 30.36 ?  163 LYS   A HE2  1 
ATOM   3933 H  HE3  A LYS   A 1 163 ? 3.187  -7.452  -5.354  0.70 34.52 ?  163 LYS   A HE3  1 
ATOM   3934 H  HE3  B LYS   A 1 163 ? 2.892  -7.534  -5.356  0.30 30.36 ?  163 LYS   A HE3  1 
ATOM   3935 H  HZ1  A LYS   A 1 163 ? 4.714  -6.999  -6.969  0.70 35.78 ?  163 LYS   A HZ1  1 
ATOM   3936 H  HZ1  B LYS   A 1 163 ? 4.143  -9.166  -6.315  0.30 31.06 ?  163 LYS   A HZ1  1 
ATOM   3937 H  HZ2  A LYS   A 1 163 ? 4.372  -5.764  -6.292  0.70 35.78 ?  163 LYS   A HZ2  1 
ATOM   3938 H  HZ2  B LYS   A 1 163 ? 5.034  -8.132  -5.831  0.30 31.06 ?  163 LYS   A HZ2  1 
ATOM   3939 H  HZ3  A LYS   A 1 163 ? 5.631  -6.422  -6.006  0.70 35.78 ?  163 LYS   A HZ3  1 
ATOM   3940 H  HZ3  B LYS   A 1 163 ? 4.898  -9.373  -5.096  0.30 31.06 ?  163 LYS   A HZ3  1 
ATOM   3941 N  N    A LEU   A 1 164 ? 5.580  -8.569  0.647   0.70 16.58 ?  164 LEU   A N    1 
ATOM   3942 N  N    B LEU   A 1 164 ? 5.564  -8.726  0.922   0.30 19.49 ?  164 LEU   A N    1 
ATOM   3943 C  CA   A LEU   A 1 164 ? 6.650  -9.559  0.770   0.70 15.96 ?  164 LEU   A CA   1 
ATOM   3944 C  CA   B LEU   A 1 164 ? 6.643  -9.688  1.132   0.30 19.01 ?  164 LEU   A CA   1 
ATOM   3945 C  C    A LEU   A 1 164 ? 6.217  -10.747 1.624   0.70 15.96 ?  164 LEU   A C    1 
ATOM   3946 C  C    B LEU   A 1 164 ? 6.205  -10.799 2.075   0.30 19.22 ?  164 LEU   A C    1 
ATOM   3947 O  O    A LEU   A 1 164 ? 6.509  -11.900 1.287   0.70 15.66 ?  164 LEU   A O    1 
ATOM   3948 O  O    B LEU   A 1 164 ? 6.557  -11.968 1.879   0.30 19.19 ?  164 LEU   A O    1 
ATOM   3949 C  CB   A LEU   A 1 164 ? 7.889  -8.902  1.369   0.70 15.46 ?  164 LEU   A CB   1 
ATOM   3950 C  CB   B LEU   A 1 164 ? 7.872  -8.973  1.696   0.30 18.58 ?  164 LEU   A CB   1 
ATOM   3951 C  CG   A LEU   A 1 164 ? 8.653  -7.943  0.457   0.70 15.82 ?  164 LEU   A CG   1 
ATOM   3952 C  CG   B LEU   A 1 164 ? 8.648  -8.061  0.747   0.30 18.52 ?  164 LEU   A CG   1 
ATOM   3953 C  CD1  A LEU   A 1 164 ? 9.560  -7.051  1.283   0.70 15.23 ?  164 LEU   A CD1  1 
ATOM   3954 C  CD1  B LEU   A 1 164 ? 9.699  -7.290  1.524   0.30 18.56 ?  164 LEU   A CD1  1 
ATOM   3955 C  CD2  A LEU   A 1 164 ? 9.468  -8.704  -0.576  0.70 16.12 ?  164 LEU   A CD2  1 
ATOM   3956 C  CD2  B LEU   A 1 164 ? 9.295  -8.870  -0.364  0.30 18.49 ?  164 LEU   A CD2  1 
ATOM   3957 H  H    A LEU   A 1 164 ? 5.738  -7.813  1.042   0.70 19.87 ?  164 LEU   A H    1 
ATOM   3958 H  H    B LEU   A 1 164 ? 5.744  -7.925  1.180   0.30 23.37 ?  164 LEU   A H    1 
ATOM   3959 H  HA   A LEU   A 1 164 ? 6.877  -9.880  -0.118  0.70 19.13 ?  164 LEU   A HA   1 
ATOM   3960 H  HA   B LEU   A 1 164 ? 6.887  -10.089 0.284   0.30 22.79 ?  164 LEU   A HA   1 
ATOM   3961 H  HB2  A LEU   A 1 164 ? 7.621  -8.397  2.151   0.70 18.53 ?  164 LEU   A HB2  1 
ATOM   3962 H  HB2  B LEU   A 1 164 ? 7.587  -8.424  2.442   0.30 22.28 ?  164 LEU   A HB2  1 
ATOM   3963 H  HB3  A LEU   A 1 164 ? 8.507  -9.600  1.627   0.70 18.53 ?  164 LEU   A HB3  1 
ATOM   3964 H  HB3  B LEU   A 1 164 ? 8.495  -9.644  2.012   0.30 22.28 ?  164 LEU   A HB3  1 
ATOM   3965 H  HG   A LEU   A 1 164 ? 8.022  -7.373  -0.014  0.70 18.97 ?  164 LEU   A HG   1 
ATOM   3966 H  HG   B LEU   A 1 164 ? 8.040  -7.421  0.344   0.30 22.20 ?  164 LEU   A HG   1 
ATOM   3967 H  HD11 A LEU   A 1 164 ? 10.024 -6.433  0.695   0.70 18.26 ?  164 LEU   A HD11 1 
ATOM   3968 H  HD11 B LEU   A 1 164 ? 10.188 -6.718  0.914   0.30 22.25 ?  164 LEU   A HD11 1 
ATOM   3969 H  HD12 A LEU   A 1 164 ? 9.021  -6.554  1.921   0.70 18.26 ?  164 LEU   A HD12 1 
ATOM   3970 H  HD12 B LEU   A 1 164 ? 9.259  -6.752  2.201   0.30 22.25 ?  164 LEU   A HD12 1 
ATOM   3971 H  HD13 A LEU   A 1 164 ? 10.203 -7.602  1.756   0.70 18.26 ?  164 LEU   A HD13 1 
ATOM   3972 H  HD13 B LEU   A 1 164 ? 10.305 -7.920  1.945   0.30 22.25 ?  164 LEU   A HD13 1 
ATOM   3973 H  HD21 A LEU   A 1 164 ? 9.951  -8.069  -1.129  0.70 19.32 ?  164 LEU   A HD21 1 
ATOM   3974 H  HD21 B LEU   A 1 164 ? 9.870  -8.288  -0.886  0.30 22.17 ?  164 LEU   A HD21 1 
ATOM   3975 H  HD22 A LEU   A 1 164 ? 10.092 -9.286  -0.118  0.70 19.32 ?  164 LEU   A HD22 1 
ATOM   3976 H  HD22 B LEU   A 1 164 ? 9.819  -9.585  0.031   0.30 22.17 ?  164 LEU   A HD22 1 
ATOM   3977 H  HD23 A LEU   A 1 164 ? 8.865  -9.229  -1.126  0.70 19.32 ?  164 LEU   A HD23 1 
ATOM   3978 H  HD23 B LEU   A 1 164 ? 8.600  -9.242  -0.929  0.30 22.17 ?  164 LEU   A HD23 1 
ATOM   3979 N  N    A VAL   A 1 165 ? 5.533  -10.482 2.737   0.70 15.68 ?  165 VAL   A N    1 
ATOM   3980 N  N    B VAL   A 1 165 ? 5.438  -10.449 3.110   0.30 19.56 ?  165 VAL   A N    1 
ATOM   3981 C  CA   A VAL   A 1 165 ? 5.073  -11.562 3.606   0.70 15.44 ?  165 VAL   A CA   1 
ATOM   3982 C  CA   B VAL   A 1 165 ? 4.950  -11.449 4.052   0.30 20.30 ?  165 VAL   A CA   1 
ATOM   3983 C  C    A VAL   A 1 165 ? 4.052  -12.425 2.885   0.70 15.63 ?  165 VAL   A C    1 
ATOM   3984 C  C    B VAL   A 1 165 ? 3.864  -12.306 3.417   0.30 20.70 ?  165 VAL   A C    1 
ATOM   3985 O  O    A VAL   A 1 165 ? 4.150  -13.658 2.874   0.70 14.86 ?  165 VAL   A O    1 
ATOM   3986 O  O    B VAL   A 1 165 ? 3.724  -13.488 3.752   0.30 21.74 ?  165 VAL   A O    1 
ATOM   3987 C  CB   A VAL   A 1 165 ? 4.497  -10.986 4.910   0.70 15.98 ?  165 VAL   A CB   1 
ATOM   3988 C  CB   B VAL   A 1 165 ? 4.486  -10.760 5.352   0.30 20.87 ?  165 VAL   A CB   1 
ATOM   3989 C  CG1  A VAL   A 1 165 ? 3.758  -12.069 5.699   0.70 15.95 ?  165 VAL   A CG1  1 
ATOM   3990 C  CG1  B VAL   A 1 165 ? 3.662  -11.708 6.218   0.30 21.00 ?  165 VAL   A CG1  1 
ATOM   3991 C  CG2  A VAL   A 1 165 ? 5.599  -10.347 5.736   0.70 16.45 ?  165 VAL   A CG2  1 
ATOM   3992 C  CG2  B VAL   A 1 165 ? 5.689  -10.238 6.126   0.30 20.99 ?  165 VAL   A CG2  1 
ATOM   3993 H  H    A VAL   A 1 165 ? 5.322  -9.693  3.002   0.70 18.79 ?  165 VAL   A H    1 
ATOM   3994 H  H    B VAL   A 1 165 ? 5.184  -9.647  3.281   0.30 23.45 ?  165 VAL   A H    1 
ATOM   3995 H  HA   A VAL   A 1 165 ? 5.830  -12.123 3.832   0.70 18.51 ?  165 VAL   A HA   1 
ATOM   3996 H  HA   B VAL   A 1 165 ? 5.679  -12.040 4.282   0.30 24.34 ?  165 VAL   A HA   1 
ATOM   3997 H  HB   A VAL   A 1 165 ? 3.858  -10.292 4.687   0.70 19.16 ?  165 VAL   A HB   1 
ATOM   3998 H  HB   B VAL   A 1 165 ? 3.930  -9.998  5.128   0.30 25.02 ?  165 VAL   A HB   1 
ATOM   3999 H  HG11 A VAL   A 1 165 ? 3.660  -11.775 6.618   0.70 19.11 ?  165 VAL   A HG11 1 
ATOM   4000 H  HG11 B VAL   A 1 165 ? 3.605  -11.343 7.118   0.30 25.18 ?  165 VAL   A HG11 1 
ATOM   4001 H  HG12 A VAL   A 1 165 ? 2.882  -12.207 5.304   0.70 19.11 ?  165 VAL   A HG12 1 
ATOM   4002 H  HG12 B VAL   A 1 165 ? 2.772  -11.788 5.842   0.30 25.18 ?  165 VAL   A HG12 1 
ATOM   4003 H  HG13 A VAL   A 1 165 ? 4.272  -12.890 5.667   0.70 19.11 ?  165 VAL   A HG13 1 
ATOM   4004 H  HG13 B VAL   A 1 165 ? 4.095  -12.573 6.242   0.30 25.18 ?  165 VAL   A HG13 1 
ATOM   4005 H  HG21 A VAL   A 1 165 ? 5.220  -10.010 6.562   0.70 19.72 ?  165 VAL   A HG21 1 
ATOM   4006 H  HG21 B VAL   A 1 165 ? 5.381  -9.803  6.936   0.30 25.17 ?  165 VAL   A HG21 1 
ATOM   4007 H  HG22 A VAL   A 1 165 ? 6.278  -11.012 5.930   0.70 19.72 ?  165 VAL   A HG22 1 
ATOM   4008 H  HG22 B VAL   A 1 165 ? 6.267  -10.984 6.351   0.30 25.17 ?  165 VAL   A HG22 1 
ATOM   4009 H  HG23 A VAL   A 1 165 ? 5.991  -9.615  5.231   0.70 19.72 ?  165 VAL   A HG23 1 
ATOM   4010 H  HG23 B VAL   A 1 165 ? 6.170  -9.603  5.571   0.30 25.17 ?  165 VAL   A HG23 1 
ATOM   4011 N  N    A SER   A 1 166 ? 3.041  -11.787 2.288   0.70 16.62 ?  166 SER   A N    1 
ATOM   4012 N  N    B SER   A 1 166 ? 3.103  -11.747 2.474   0.30 20.02 ?  166 SER   A N    1 
ATOM   4013 C  CA   A SER   A 1 166 ? 1.932  -12.532 1.703   0.70 17.70 ?  166 SER   A CA   1 
ATOM   4014 C  CA   B SER   A 1 166 ? 1.960  -12.441 1.898   0.30 19.32 ?  166 SER   A CA   1 
ATOM   4015 C  C    A SER   A 1 166 ? 2.388  -13.397 0.542   0.70 18.34 ?  166 SER   A C    1 
ATOM   4016 C  C    B SER   A 1 166 ? 2.273  -13.167 0.594   0.30 18.77 ?  166 SER   A C    1 
ATOM   4017 O  O    A SER   A 1 166 ? 1.790  -14.450 0.285   0.70 20.34 ?  166 SER   A O    1 
ATOM   4018 O  O    B SER   A 1 166 ? 1.417  -13.910 0.103   0.30 18.13 ?  166 SER   A O    1 
ATOM   4019 C  CB   A SER   A 1 166 ? 0.835  -11.570 1.236   0.70 18.49 ?  166 SER   A CB   1 
ATOM   4020 C  CB   B SER   A 1 166 ? 0.810  -11.458 1.653   0.30 19.30 ?  166 SER   A CB   1 
ATOM   4021 O  OG   A SER   A 1 166 ? 0.171  -10.965 2.336   0.70 19.81 ?  166 SER   A OG   1 
ATOM   4022 O  OG   B SER   A 1 166 ? 1.052  -10.696 0.484   0.30 19.48 ?  166 SER   A OG   1 
ATOM   4023 H  H    A SER   A 1 166 ? 2.968  -10.939 2.219   0.70 19.92 ?  166 SER   A H    1 
ATOM   4024 H  H    B SER   A 1 166 ? 3.234  -10.958 2.155   0.30 24.01 ?  166 SER   A H    1 
ATOM   4025 H  HA   A SER   A 1 166 ? 1.544  -13.119 2.372   0.70 21.22 ?  166 SER   A HA   1 
ATOM   4026 H  HA   B SER   A 1 166 ? 1.646  -13.103 2.531   0.30 23.16 ?  166 SER   A HA   1 
ATOM   4027 H  HB2  A SER   A 1 166 ? 1.236  -10.882 0.681   0.70 22.17 ?  166 SER   A HB2  1 
ATOM   4028 H  HB2  B SER   A 1 166 ? -0.016 -11.957 1.546   0.30 23.14 ?  166 SER   A HB2  1 
ATOM   4029 H  HB3  A SER   A 1 166 ? 0.176  -12.063 0.721   0.70 22.17 ?  166 SER   A HB3  1 
ATOM   4030 H  HB3  B SER   A 1 166 ? 0.735  -10.860 2.418   0.30 23.14 ?  166 SER   A HB3  1 
ATOM   4031 H  HG   A SER   A 1 166 ? -0.410 -10.426 2.060   0.70 23.75 ?  166 SER   A HG   1 
ATOM   4032 H  HG   B SER   A 1 166 ? 0.419  -10.158 0.358   0.30 23.35 ?  166 SER   A HG   1 
ATOM   4033 N  N    A SER   A 1 167 ? 3.433  -12.974 -0.169  0.70 18.33 ?  167 SER   A N    1 
ATOM   4034 N  N    B SER   A 1 167 ? 3.457  -12.966 0.012   0.30 19.30 ?  167 SER   A N    1 
ATOM   4035 C  CA   A SER   A 1 167 ? 3.927  -13.695 -1.331  0.70 19.29 ?  167 SER   A CA   1 
ATOM   4036 C  CA   B SER   A 1 167 ? 3.847  -13.674 -1.204  0.30 19.97 ?  167 SER   A CA   1 
ATOM   4037 C  C    A SER   A 1 167 ? 5.069  -14.646 -1.001  0.70 20.07 ?  167 SER   A C    1 
ATOM   4038 C  C    B SER   A 1 167 ? 5.038  -14.599 -0.981  0.30 20.18 ?  167 SER   A C    1 
ATOM   4039 O  O    A SER   A 1 167 ? 5.567  -15.324 -1.908  0.70 21.09 ?  167 SER   A O    1 
ATOM   4040 O  O    B SER   A 1 167 ? 5.544  -15.194 -1.940  0.30 20.55 ?  167 SER   A O    1 
ATOM   4041 C  CB   A SER   A 1 167 ? 4.370  -12.706 -2.423  0.70 19.90 ?  167 SER   A CB   1 
ATOM   4042 C  CB   B SER   A 1 167 ? 4.150  -12.688 -2.336  0.30 20.78 ?  167 SER   A CB   1 
ATOM   4043 O  OG   A SER   A 1 167 ? 5.470  -11.918 -1.991  0.70 19.80 ?  167 SER   A OG   1 
ATOM   4044 O  OG   B SER   A 1 167 ? 5.126  -11.739 -1.942  0.30 21.31 ?  167 SER   A OG   1 
ATOM   4045 H  H    A SER   A 1 167 ? 3.872  -12.253 0.005   0.70 21.97 ?  167 SER   A H    1 
ATOM   4046 H  H    B SER   A 1 167 ? 4.054  -12.416 0.308   0.30 23.14 ?  167 SER   A H    1 
ATOM   4047 H  HA   A SER   A 1 167 ? 3.205  -14.222 -1.698  0.70 23.13 ?  167 SER   A HA   1 
ATOM   4048 H  HA   B SER   A 1 167 ? 3.095  -14.217 -1.486  0.30 23.95 ?  167 SER   A HA   1 
ATOM   4049 H  HB2  A SER   A 1 167 ? 4.635  -13.204 -3.213  0.70 23.86 ?  167 SER   A HB2  1 
ATOM   4050 H  HB2  B SER   A 1 167 ? 4.485  -13.187 -3.098  0.30 24.91 ?  167 SER   A HB2  1 
ATOM   4051 H  HB3  A SER   A 1 167 ? 3.620  -12.123 -2.645  0.70 23.86 ?  167 SER   A HB3  1 
ATOM   4052 H  HB3  B SER   A 1 167 ? 3.333  -12.224 -2.579  0.30 24.91 ?  167 SER   A HB3  1 
ATOM   4053 H  HG   A SER   A 1 167 ? 5.240  -11.459 -1.322  0.70 23.74 ?  167 SER   A HG   1 
ATOM   4054 H  HG   B SER   A 1 167 ? 4.844  -11.296 -1.285  0.30 25.56 ?  167 SER   A HG   1 
ATOM   4055 N  N    . PHE   A 1 168 ? 5.495  -14.729 0.259   1.00 20.04 ?  168 PHE   A N    1 
ATOM   4056 C  CA   . PHE   A 1 168 ? 6.670  -15.536 0.566   1.00 20.66 ?  168 PHE   A CA   1 
ATOM   4057 C  C    . PHE   A 1 168 ? 6.357  -17.019 0.452   1.00 23.63 ?  168 PHE   A C    1 
ATOM   4058 O  O    . PHE   A 1 168 ? 5.358  -17.501 0.998   1.00 24.97 ?  168 PHE   A O    1 
ATOM   4059 C  CB   . PHE   A 1 168 ? 7.176  -15.250 1.975   1.00 19.34 ?  168 PHE   A CB   1 
ATOM   4060 C  CG   . PHE   A 1 168 ? 8.441  -15.990 2.297   1.00 18.41 ?  168 PHE   A CG   1 
ATOM   4061 C  CD1  . PHE   A 1 168 ? 9.628  -15.618 1.697   1.00 18.76 ?  168 PHE   A CD1  1 
ATOM   4062 C  CD2  . PHE   A 1 168 ? 8.448  -17.079 3.156   1.00 18.04 ?  168 PHE   A CD2  1 
ATOM   4063 C  CE1  . PHE   A 1 168 ? 10.798 -16.295 1.961   1.00 18.33 ?  168 PHE   A CE1  1 
ATOM   4064 C  CE2  . PHE   A 1 168 ? 9.628  -17.759 3.429   1.00 18.73 ?  168 PHE   A CE2  1 
ATOM   4065 C  CZ   . PHE   A 1 168 ? 10.798 -17.364 2.826   1.00 18.71 ?  168 PHE   A CZ   1 
ATOM   4066 H  H    A PHE   A 1 168 ? 5.133  -14.339 0.933   0.70 24.03 ?  168 PHE   A H    1 
ATOM   4067 H  H    B PHE   A 1 168 ? 5.154  -14.341 0.945   0.30 24.03 ?  168 PHE   A H    1 
ATOM   4068 H  HA   . PHE   A 1 168 ? 7.380  -15.320 -0.065  1.00 24.77 ?  168 PHE   A HA   1 
ATOM   4069 H  HB2  . PHE   A 1 168 ? 7.355  -14.301 2.062   1.00 23.19 ?  168 PHE   A HB2  1 
ATOM   4070 H  HB3  . PHE   A 1 168 ? 6.498  -15.521 2.613   1.00 23.19 ?  168 PHE   A HB3  1 
ATOM   4071 H  HD1  . PHE   A 1 168 ? 9.641  -14.895 1.113   1.00 22.50 ?  168 PHE   A HD1  1 
ATOM   4072 H  HD2  . PHE   A 1 168 ? 7.657  -17.350 3.565   1.00 21.63 ?  168 PHE   A HD2  1 
ATOM   4073 H  HE1  . PHE   A 1 168 ? 11.598 -16.028 1.559   1.00 21.98 ?  168 PHE   A HE1  1 
ATOM   4074 H  HE2  . PHE   A 1 168 ? 9.623  -18.485 4.010   1.00 22.46 ?  168 PHE   A HE2  1 
ATOM   4075 H  HZ   . PHE   A 1 168 ? 11.592 -17.819 3.005   1.00 22.43 ?  168 PHE   A HZ   1 
ATOM   4076 N  N    A LEU   A 1 169 ? 7.231  -17.750 -0.234  0.70 26.13 ?  169 LEU   A N    1 
ATOM   4077 N  N    B LEU   A 1 169 ? 7.224  -17.751 -0.241  0.30 26.67 ?  169 LEU   A N    1 
ATOM   4078 C  CA   A LEU   A 1 169 ? 7.037  -19.179 -0.407  0.70 30.41 ?  169 LEU   A CA   1 
ATOM   4079 C  CA   B LEU   A 1 169 ? 7.030  -19.186 -0.397  0.30 29.87 ?  169 LEU   A CA   1 
ATOM   4080 C  C    A LEU   A 1 169 ? 7.909  -19.946 0.578   0.70 31.38 ?  169 LEU   A C    1 
ATOM   4081 C  C    B LEU   A 1 169 ? 7.886  -19.955 0.601   0.30 30.64 ?  169 LEU   A C    1 
ATOM   4082 O  O    A LEU   A 1 169 ? 7.415  -20.418 1.604   0.70 31.90 ?  169 LEU   A O    1 
ATOM   4083 O  O    B LEU   A 1 169 ? 7.362  -20.599 1.510   0.30 30.79 ?  169 LEU   A O    1 
ATOM   4084 C  CB   A LEU   A 1 169 ? 7.342  -19.596 -1.849  0.70 32.78 ?  169 LEU   A CB   1 
ATOM   4085 C  CB   B LEU   A 1 169 ? 7.352  -19.627 -1.827  0.30 31.83 ?  169 LEU   A CB   1 
ATOM   4086 C  CG   A LEU   A 1 169 ? 7.027  -21.051 -2.209  0.70 34.15 ?  169 LEU   A CG   1 
ATOM   4087 C  CG   B LEU   A 1 169 ? 7.040  -21.090 -2.156  0.30 33.04 ?  169 LEU   A CG   1 
ATOM   4088 C  CD1  A LEU   A 1 169 ? 5.600  -21.410 -1.818  0.70 35.19 ?  169 LEU   A CD1  1 
ATOM   4089 C  CD1  B LEU   A 1 169 ? 5.622  -21.445 -1.735  0.30 33.83 ?  169 LEU   A CD1  1 
ATOM   4090 C  CD2  A LEU   A 1 169 ? 7.251  -21.298 -3.695  0.70 34.65 ?  169 LEU   A CD2  1 
ATOM   4091 C  CD2  B LEU   A 1 169 ? 7.238  -21.361 -3.640  0.30 33.31 ?  169 LEU   A CD2  1 
ATOM   4092 O  OXT  A LEU   A 1 169 ? 9.116  -20.095 0.383   0.70 31.64 -1 169 LEU   A OXT  1 
ATOM   4093 O  OXT  B LEU   A 1 169 ? 9.116  -19.943 0.529   0.30 31.07 -1 169 LEU   A OXT  1 
ATOM   4094 H  H    A LEU   A 1 169 ? 7.946  -17.440 -0.603  0.70 31.34 ?  169 LEU   A H    1 
ATOM   4095 H  H    B LEU   A 1 169 ? 7.931  -17.442 -0.627  0.30 31.98 ?  169 LEU   A H    1 
ATOM   4096 H  HA   A LEU   A 1 169 ? 6.115  -19.395 -0.215  0.70 36.47 ?  169 LEU   A HA   1 
ATOM   4097 H  HA   B LEU   A 1 169 ? 6.102  -19.391 -0.217  0.30 35.82 ?  169 LEU   A HA   1 
ATOM   4098 H  HB2  A LEU   A 1 169 ? 6.822  -19.034 -2.445  0.70 39.32 ?  169 LEU   A HB2  1 
ATOM   4099 H  HB2  B LEU   A 1 169 ? 6.840  -19.078 -2.440  0.30 38.17 ?  169 LEU   A HB2  1 
ATOM   4100 H  HB3  A LEU   A 1 169 ? 8.286  -19.456 -2.017  0.70 39.32 ?  169 LEU   A HB3  1 
ATOM   4101 H  HB3  B LEU   A 1 169 ? 8.299  -19.492 -1.985  0.30 38.17 ?  169 LEU   A HB3  1 
ATOM   4102 H  HG   A LEU   A 1 169 ? 7.626  -21.635 -1.719  0.70 40.96 ?  169 LEU   A HG   1 
ATOM   4103 H  HG   B LEU   A 1 169 ? 7.650  -21.663 -1.665  0.30 39.63 ?  169 LEU   A HG   1 
ATOM   4104 H  HD11 A LEU   A 1 169 ? 5.361  -22.251 -2.236  0.70 42.21 ?  169 LEU   A HD11 1 
ATOM   4105 H  HD11 B LEU   A 1 169 ? 5.371  -22.285 -2.148  0.30 40.58 ?  169 LEU   A HD11 1 
ATOM   4106 H  HD12 A LEU   A 1 169 ? 5.549  -21.494 -0.853  0.70 42.21 ?  169 LEU   A HD12 1 
ATOM   4107 H  HD12 B LEU   A 1 169 ? 5.591  -21.530 -0.768  0.30 40.58 ?  169 LEU   A HD12 1 
ATOM   4108 H  HD13 A LEU   A 1 169 ? 5.005  -20.707 -2.123  0.70 42.21 ?  169 LEU   A HD13 1 
ATOM   4109 H  HD13 B LEU   A 1 169 ? 5.021  -20.741 -2.026  0.30 40.58 ?  169 LEU   A HD13 1 
ATOM   4110 H  HD21 A LEU   A 1 169 ? 7.051  -22.227 -3.895  0.70 41.56 ?  169 LEU   A HD21 1 
ATOM   4111 H  HD21 B LEU   A 1 169 ? 7.041  -22.294 -3.820  0.30 39.95 ?  169 LEU   A HD21 1 
ATOM   4112 H  HD22 A LEU   A 1 169 ? 6.663  -20.718 -4.204  0.70 41.56 ?  169 LEU   A HD22 1 
ATOM   4113 H  HD22 B LEU   A 1 169 ? 6.636  -20.793 -4.147  0.30 39.95 ?  169 LEU   A HD22 1 
ATOM   4114 H  HD23 A LEU   A 1 169 ? 8.176  -21.105 -3.912  0.70 41.56 ?  169 LEU   A HD23 1 
ATOM   4115 H  HD23 B LEU   A 1 169 ? 8.157  -21.164 -3.877  0.30 39.95 ?  169 LEU   A HD23 1 
ATOM   4116 N  N    A SER   B 1 1   ? 50.826 -9.286  -23.762 0.70 28.42 ?  1   SER   B N    1 
ATOM   4117 N  N    B SER   B 1 1   ? 50.739 -9.259  -23.736 0.30 27.08 ?  1   SER   B N    1 
ATOM   4118 C  CA   A SER   B 1 1   ? 51.306 -10.317 -22.820 0.70 27.92 ?  1   SER   B CA   1 
ATOM   4119 C  CA   B SER   B 1 1   ? 51.229 -10.255 -22.761 0.30 26.58 ?  1   SER   B CA   1 
ATOM   4120 C  C    A SER   B 1 1   ? 50.229 -11.361 -22.560 0.70 27.07 ?  1   SER   B C    1 
ATOM   4121 C  C    B SER   B 1 1   ? 50.168 -11.316 -22.510 0.30 26.06 ?  1   SER   B C    1 
ATOM   4122 O  O    A SER   B 1 1   ? 49.033 -11.147 -22.809 0.70 27.22 ?  1   SER   B O    1 
ATOM   4123 O  O    B SER   B 1 1   ? 48.995 -11.147 -22.860 0.30 25.82 ?  1   SER   B O    1 
ATOM   4124 C  CB   A SER   B 1 1   ? 51.746 -9.687  -21.500 0.70 29.03 ?  1   SER   B CB   1 
ATOM   4125 C  CB   B SER   B 1 1   ? 51.606 -9.580  -21.447 0.30 27.34 ?  1   SER   B CB   1 
ATOM   4126 O  OG   A SER   B 1 1   ? 50.629 -9.398  -20.681 0.70 30.66 ?  1   SER   B OG   1 
ATOM   4127 O  OG   B SER   B 1 1   ? 50.471 -9.436  -20.614 0.30 28.00 ?  1   SER   B OG   1 
ATOM   4128 H  H1   A SER   B 1 1   ? 50.747 -9.647  -24.569 0.70 34.08 ?  1   SER   B H1   1 
ATOM   4129 H  H1   B SER   B 1 1   ? 51.434 -8.814  -24.065 0.30 32.47 ?  1   SER   B H1   1 
ATOM   4130 H  H2   A SER   B 1 1   ? 50.041 -8.985  -23.484 0.70 34.08 ?  1   SER   B H2   1 
ATOM   4131 H  H2   B SER   B 1 1   ? 50.313 -9.680  -24.390 0.30 32.47 ?  1   SER   B H2   1 
ATOM   4132 H  H3   A SER   B 1 1   ? 51.416 -8.622  -23.785 0.70 34.08 ?  1   SER   B H3   1 
ATOM   4133 H  H3   B SER   B 1 1   ? 50.189 -8.700  -23.325 0.30 32.47 ?  1   SER   B H3   1 
ATOM   4134 H  HA   A SER   B 1 1   ? 52.072 -10.754 -23.217 0.70 33.48 ?  1   SER   B HA   1 
ATOM   4135 H  HA   B SER   B 1 1   ? 52.015 -10.680 -23.128 0.30 31.88 ?  1   SER   B HA   1 
ATOM   4136 H  HB2  A SER   B 1 1   ? 52.322 -10.313 -21.037 0.70 34.81 ?  1   SER   B HB2  1 
ATOM   4137 H  HB2  B SER   B 1 1   ? 52.270 -10.126 -21.000 0.30 32.78 ?  1   SER   B HB2  1 
ATOM   4138 H  HB3  A SER   B 1 1   ? 52.227 -8.865  -21.685 0.70 34.81 ?  1   SER   B HB3  1 
ATOM   4139 H  HB3  B SER   B 1 1   ? 51.970 -8.700  -21.634 0.30 32.78 ?  1   SER   B HB3  1 
ATOM   4140 H  HG   A SER   B 1 1   ? 50.867 -8.902  -20.045 0.70 36.77 ?  1   SER   B HG   1 
ATOM   4141 H  HG   B SER   B 1 1   ? 50.611 -8.833  -20.047 0.30 33.58 ?  1   SER   B HG   1 
ATOM   4142 N  N    A MET   B 1 2   ? 50.679 -12.495 -22.044 0.70 26.21 ?  2   MET   B N    1 
ATOM   4143 N  N    B MET   B 1 2   ? 50.592 -12.408 -21.888 0.30 25.55 ?  2   MET   B N    1 
ATOM   4144 C  CA   A MET   B 1 2   ? 49.853 -13.681 -21.877 0.70 26.07 ?  2   MET   B CA   1 
ATOM   4145 C  CA   B MET   B 1 2   ? 49.774 -13.601 -21.723 0.30 25.09 ?  2   MET   B CA   1 
ATOM   4146 C  C    A MET   B 1 2   ? 49.606 -13.876 -20.388 0.70 23.94 ?  2   MET   B C    1 
ATOM   4147 C  C    B MET   B 1 2   ? 49.505 -13.800 -20.238 0.30 23.38 ?  2   MET   B C    1 
ATOM   4148 O  O    A MET   B 1 2   ? 50.543 -14.132 -19.626 0.70 24.18 ?  2   MET   B O    1 
ATOM   4149 O  O    B MET   B 1 2   ? 50.405 -14.185 -19.483 0.30 23.47 ?  2   MET   B O    1 
ATOM   4150 C  CB   A MET   B 1 2   ? 50.576 -14.878 -22.481 0.70 29.80 ?  2   MET   B CB   1 
ATOM   4151 C  CB   B MET   B 1 2   ? 50.523 -14.793 -22.303 0.30 26.71 ?  2   MET   B CB   1 
ATOM   4152 C  CG   A MET   B 1 2   ? 49.724 -16.124 -22.639 0.70 33.51 ?  2   MET   B CG   1 
ATOM   4153 C  CG   B MET   B 1 2   ? 49.645 -15.949 -22.750 0.30 28.07 ?  2   MET   B CG   1 
ATOM   4154 S  SD   A MET   B 1 2   ? 50.554 -17.354 -23.663 0.70 36.73 ?  2   MET   B SD   1 
ATOM   4155 S  SD   B MET   B 1 2   ? 50.551 -17.052 -23.840 0.30 29.31 ?  2   MET   B SD   1 
ATOM   4156 C  CE   A MET   B 1 2   ? 51.099 -16.310 -25.007 0.70 36.86 ?  2   MET   B CE   1 
ATOM   4157 C  CE   B MET   B 1 2   ? 51.441 -15.863 -24.823 0.30 29.28 ?  2   MET   B CE   1 
ATOM   4158 H  H    A MET   B 1 2   ? 51.489 -12.611 -21.774 0.70 31.44 ?  2   MET   B H    1 
ATOM   4159 H  H    B MET   B 1 2   ? 51.381 -12.489 -21.550 0.30 30.63 ?  2   MET   B H    1 
ATOM   4160 H  HA   A MET   B 1 2   ? 49.012 -13.571 -22.344 0.70 31.27 ?  2   MET   B HA   1 
ATOM   4161 H  HA   B MET   B 1 2   ? 48.942 -13.505 -22.214 0.30 30.09 ?  2   MET   B HA   1 
ATOM   4162 H  HB2  A MET   B 1 2   ? 50.895 -14.597 -23.350 0.70 35.74 ?  2   MET   B HB2  1 
ATOM   4163 H  HB2  B MET   B 1 2   ? 51.028 -14.443 -23.048 0.30 32.03 ?  2   MET   B HB2  1 
ATOM   4164 H  HB3  A MET   B 1 2   ? 51.329 -15.121 -21.924 0.70 35.74 ?  2   MET   B HB3  1 
ATOM   4165 H  HB3  B MET   B 1 2   ? 51.133 -15.153 -21.649 0.30 32.03 ?  2   MET   B HB3  1 
ATOM   4166 H  HG2  A MET   B 1 2   ? 49.558 -16.512 -21.762 0.70 40.19 ?  2   MET   B HG2  1 
ATOM   4167 H  HG2  B MET   B 1 2   ? 49.357 -16.457 -21.971 0.30 33.67 ?  2   MET   B HG2  1 
ATOM   4168 H  HG3  A MET   B 1 2   ? 48.886 -15.895 -23.070 0.70 40.19 ?  2   MET   B HG3  1 
ATOM   4169 H  HG3  B MET   B 1 2   ? 48.875 -15.619 -23.234 0.30 33.67 ?  2   MET   B HG3  1 
ATOM   4170 H  HE1  A MET   B 1 2   ? 51.247 -16.859 -25.779 0.70 44.21 ?  2   MET   B HE1  1 
ATOM   4171 H  HE1  B MET   B 1 2   ? 51.666 -16.292 -25.638 0.30 35.12 ?  2   MET   B HE1  1 
ATOM   4172 H  HE2  A MET   B 1 2   ? 50.404 -15.654 -25.188 0.70 44.21 ?  2   MET   B HE2  1 
ATOM   4173 H  HE2  B MET   B 1 2   ? 50.867 -15.096 -25.000 0.30 35.12 ?  2   MET   B HE2  1 
ATOM   4174 H  HE3  A MET   B 1 2   ? 51.922 -15.855 -24.753 0.70 44.21 ?  2   MET   B HE3  1 
ATOM   4175 H  HE3  B MET   B 1 2   ? 52.246 -15.582 -24.346 0.30 35.12 ?  2   MET   B HE3  1 
ATOM   4176 N  N    A VAL   B 1 3   ? 48.353 -13.724 -19.973 0.70 21.61 ?  3   VAL   B N    1 
ATOM   4177 N  N    B VAL   B 1 3   ? 48.276 -13.523 -19.819 0.30 21.67 ?  3   VAL   B N    1 
ATOM   4178 C  CA   A VAL   B 1 3   ? 47.946 -13.969 -18.598 0.70 20.60 ?  3   VAL   B CA   1 
ATOM   4179 C  CA   B VAL   B 1 3   ? 47.840 -13.787 -18.455 0.30 20.39 ?  3   VAL   B CA   1 
ATOM   4180 C  C    A VAL   B 1 3   ? 46.704 -14.847 -18.615 0.70 18.79 ?  3   VAL   B C    1 
ATOM   4181 C  C    B VAL   B 1 3   ? 46.583 -14.643 -18.490 0.30 18.62 ?  3   VAL   B C    1 
ATOM   4182 O  O    A VAL   B 1 3   ? 45.996 -14.946 -19.621 0.70 19.19 ?  3   VAL   B O    1 
ATOM   4183 O  O    B VAL   B 1 3   ? 45.751 -14.531 -19.396 0.30 18.39 ?  3   VAL   B O    1 
ATOM   4184 C  CB   A VAL   B 1 3   ? 47.683 -12.658 -17.825 0.70 22.49 ?  3   VAL   B CB   1 
ATOM   4185 C  CB   B VAL   B 1 3   ? 47.594 -12.495 -17.644 0.30 21.07 ?  3   VAL   B CB   1 
ATOM   4186 C  CG1  A VAL   B 1 3   ? 48.961 -11.817 -17.734 0.70 22.79 ?  3   VAL   B CG1  1 
ATOM   4187 C  CG1  B VAL   B 1 3   ? 48.878 -11.684 -17.522 0.30 21.38 ?  3   VAL   B CG1  1 
ATOM   4188 C  CG2  A VAL   B 1 3   ? 46.565 -11.866 -18.488 0.70 23.62 ?  3   VAL   B CG2  1 
ATOM   4189 C  CG2  B VAL   B 1 3   ? 46.485 -11.670 -18.275 0.30 21.30 ?  3   VAL   B CG2  1 
ATOM   4190 H  H    A VAL   B 1 3   ? 47.710 -13.476 -20.485 0.70 25.92 ?  3   VAL   B H    1 
ATOM   4191 H  H    B VAL   B 1 3   ? 47.675 -13.172 -20.323 0.30 25.99 ?  3   VAL   B H    1 
ATOM   4192 H  HA   A VAL   B 1 3   ? 48.652 -14.452 -18.138 0.70 24.70 ?  3   VAL   B HA   1 
ATOM   4193 H  HA   B VAL   B 1 3   ? 48.531 -14.293 -18.004 0.30 24.45 ?  3   VAL   B HA   1 
ATOM   4194 H  HB   A VAL   B 1 3   ? 47.405 -12.877 -16.922 0.70 26.96 ?  3   VAL   B HB   1 
ATOM   4195 H  HB   B VAL   B 1 3   ? 47.313 -12.743 -16.751 0.30 25.26 ?  3   VAL   B HB   1 
ATOM   4196 H  HG11 A VAL   B 1 3   ? 48.769 -11.009 -17.235 0.70 27.33 ?  3   VAL   B HG11 1 
ATOM   4197 H  HG11 B VAL   B 1 3   ? 48.698 -10.889 -16.997 0.30 25.64 ?  3   VAL   B HG11 1 
ATOM   4198 H  HG12 A VAL   B 1 3   ? 49.646 -12.333 -17.280 0.70 27.33 ?  3   VAL   B HG12 1 
ATOM   4199 H  HG12 B VAL   B 1 3   ? 49.552 -12.226 -17.082 0.30 25.64 ?  3   VAL   B HG12 1 
ATOM   4200 H  HG13 A VAL   B 1 3   ? 49.254 -11.593 -18.630 0.70 27.33 ?  3   VAL   B HG13 1 
ATOM   4201 H  HG13 B VAL   B 1 3   ? 49.180 -11.435 -18.409 0.30 25.64 ?  3   VAL   B HG13 1 
ATOM   4202 H  HG21 A VAL   B 1 3   ? 46.507 -10.996 -18.069 0.70 28.33 ?  3   VAL   B HG21 1 
ATOM   4203 H  HG21 B VAL   B 1 3   ? 46.446 -10.809 -17.833 0.30 25.54 ?  3   VAL   B HG21 1 
ATOM   4204 H  HG22 A VAL   B 1 3   ? 46.762 -11.771 -19.432 0.70 28.33 ?  3   VAL   B HG22 1 
ATOM   4205 H  HG22 B VAL   B 1 3   ? 46.676 -11.551 -19.218 0.30 25.54 ?  3   VAL   B HG22 1 
ATOM   4206 H  HG23 A VAL   B 1 3   ? 45.728 -12.346 -18.371 0.70 28.33 ?  3   VAL   B HG23 1 
ATOM   4207 H  HG23 B VAL   B 1 3   ? 45.641 -12.138 -18.165 0.30 25.54 ?  3   VAL   B HG23 1 
ATOM   4208 N  N    . ASN   B 1 4   ? 46.448 -15.498 -17.480 1.00 17.22 ?  4   ASN   B N    1 
ATOM   4209 C  CA   . ASN   B 1 4   ? 45.311 -16.410 -17.360 1.00 16.29 ?  4   ASN   B CA   1 
ATOM   4210 C  C    . ASN   B 1 4   ? 45.250 -17.373 -18.544 1.00 16.58 ?  4   ASN   B C    1 
ATOM   4211 O  O    . ASN   B 1 4   ? 44.189 -17.621 -19.110 1.00 17.17 ?  4   ASN   B O    1 
ATOM   4212 C  CB   . ASN   B 1 4   ? 43.991 -15.648 -17.200 1.00 15.80 ?  4   ASN   B CB   1 
ATOM   4213 C  CG   . ASN   B 1 4   ? 43.947 -14.832 -15.923 1.00 15.00 ?  4   ASN   B CG   1 
ATOM   4214 O  OD1  . ASN   B 1 4   ? 44.223 -15.347 -14.839 1.00 14.74 ?  4   ASN   B OD1  1 
ATOM   4215 N  ND2  . ASN   B 1 4   ? 43.619 -13.548 -16.046 1.00 16.07 ?  4   ASN   B ND2  1 
ATOM   4216 H  H    A ASN   B 1 4   ? 46.922 -15.431 -16.766 0.70 20.65 ?  4   ASN   B H    1 
ATOM   4217 H  H    B ASN   B 1 4   ? 47.014 -15.568 -16.836 0.30 20.65 ?  4   ASN   B H    1 
ATOM   4218 H  HA   . ASN   B 1 4   ? 45.436 -16.946 -16.562 1.00 19.53 ?  4   ASN   B HA   1 
ATOM   4219 H  HB2  . ASN   B 1 4   ? 43.879 -15.041 -17.947 1.00 18.94 ?  4   ASN   B HB2  1 
ATOM   4220 H  HB3  . ASN   B 1 4   ? 43.259 -16.284 -17.176 1.00 18.94 ?  4   ASN   B HB3  1 
ATOM   4221 H  HD21 . ASN   B 1 4   ? 43.587 -13.040 -15.349 1.00 19.26 ?  4   ASN   B HD21 1 
ATOM   4222 H  HD22 . ASN   B 1 4   ? 43.443 -13.218 -16.820 1.00 19.26 ?  4   ASN   B HD22 1 
ATOM   4223 N  N    . SER   B 1 5   ? 46.407 -17.918 -18.925 1.00 17.47 ?  5   SER   B N    1 
ATOM   4224 C  CA   . SER   B 1 5   ? 46.500 -18.828 -20.067 1.00 19.93 ?  5   SER   B CA   1 
ATOM   4225 C  C    . SER   B 1 5   ? 46.491 -20.253 -19.528 1.00 21.57 ?  5   SER   B C    1 
ATOM   4226 O  O    . SER   B 1 5   ? 47.513 -20.931 -19.458 1.00 23.93 ?  5   SER   B O    1 
ATOM   4227 C  CB   . SER   B 1 5   ? 47.750 -18.536 -20.892 1.00 21.74 ?  5   SER   B CB   1 
ATOM   4228 O  OG   . SER   B 1 5   ? 48.921 -18.686 -20.109 1.00 25.06 ?  5   SER   B OG   1 
ATOM   4229 H  H    . SER   B 1 5   ? 47.160 -17.781 -18.531 1.00 20.95 ?  5   SER   B H    1 
ATOM   4230 H  HA   . SER   B 1 5   ? 45.727 -18.715 -20.636 1.00 23.90 ?  5   SER   B HA   1 
ATOM   4231 H  HB2  . SER   B 1 5   ? 47.783 -19.150 -21.645 1.00 26.07 ?  5   SER   B HB2  1 
ATOM   4232 H  HB3  . SER   B 1 5   ? 47.695 -17.624 -21.216 1.00 26.07 ?  5   SER   B HB3  1 
ATOM   4233 H  HG   . SER   B 1 5   ? 48.989 -19.482 -19.849 1.00 30.05 ?  5   SER   B HG   1 
ATOM   4234 N  N    . PHE   B 1 6   ? 45.303 -20.699 -19.127 1.00 21.82 ?  6   PHE   B N    1 
ATOM   4235 C  CA   . PHE   B 1 6   ? 45.119 -22.039 -18.590 1.00 21.21 ?  6   PHE   B CA   1 
ATOM   4236 C  C    . PHE   B 1 6   ? 45.059 -23.035 -19.739 1.00 24.78 ?  6   PHE   B C    1 
ATOM   4237 O  O    . PHE   B 1 6   ? 44.391 -22.786 -20.746 1.00 26.82 ?  6   PHE   B O    1 
ATOM   4238 C  CB   . PHE   B 1 6   ? 43.828 -22.096 -17.773 1.00 19.87 ?  6   PHE   B CB   1 
ATOM   4239 C  CG   . PHE   B 1 6   ? 43.847 -21.229 -16.541 1.00 17.59 ?  6   PHE   B CG   1 
ATOM   4240 C  CD1  . PHE   B 1 6   ? 44.344 -21.718 -15.348 1.00 16.50 ?  6   PHE   B CD1  1 
ATOM   4241 C  CD2  . PHE   B 1 6   ? 43.374 -19.925 -16.580 1.00 16.85 ?  6   PHE   B CD2  1 
ATOM   4242 C  CE1  . PHE   B 1 6   ? 44.360 -20.924 -14.209 1.00 15.95 ?  6   PHE   B CE1  1 
ATOM   4243 C  CE2  . PHE   B 1 6   ? 43.393 -19.123 -15.450 1.00 17.43 ?  6   PHE   B CE2  1 
ATOM   4244 C  CZ   . PHE   B 1 6   ? 43.891 -19.617 -14.266 1.00 16.49 ?  6   PHE   B CZ   1 
ATOM   4245 H  H    . PHE   B 1 6   ? 44.578 -20.240 -19.167 1.00 26.16 ?  6   PHE   B H    1 
ATOM   4246 H  HA   . PHE   B 1 6   ? 45.863 -22.272 -18.018 1.00 25.43 ?  6   PHE   B HA   1 
ATOM   4247 H  HB2  . PHE   B 1 6   ? 43.090 -21.801 -18.330 1.00 23.83 ?  6   PHE   B HB2  1 
ATOM   4248 H  HB3  . PHE   B 1 6   ? 43.676 -23.011 -17.487 1.00 23.83 ?  6   PHE   B HB3  1 
ATOM   4249 H  HD1  . PHE   B 1 6   ? 44.670 -22.588 -15.306 1.00 19.78 ?  6   PHE   B HD1  1 
ATOM   4250 H  HD2  . PHE   B 1 6   ? 43.037 -19.587 -17.377 1.00 20.20 ?  6   PHE   B HD2  1 
ATOM   4251 H  HE1  . PHE   B 1 6   ? 44.706 -21.259 -13.411 1.00 19.12 ?  6   PHE   B HE1  1 
ATOM   4252 H  HE2  . PHE   B 1 6   ? 43.068 -18.251 -15.492 1.00 20.89 ?  6   PHE   B HE2  1 
ATOM   4253 H  HZ   . PHE   B 1 6   ? 43.904 -19.087 -13.502 1.00 19.77 ?  6   PHE   B HZ   1 
ATOM   4254 N  N    . SER   B 1 7   ? 45.778 -24.150 -19.599 1.00 25.35 ?  7   SER   B N    1 
ATOM   4255 C  CA   . SER   B 1 7   ? 45.871 -25.148 -20.654 1.00 28.07 ?  7   SER   B CA   1 
ATOM   4256 C  C    . SER   B 1 7   ? 45.805 -26.549 -20.063 1.00 27.73 ?  7   SER   B C    1 
ATOM   4257 O  O    . SER   B 1 7   ? 46.388 -26.821 -19.011 1.00 28.81 ?  7   SER   B O    1 
ATOM   4258 C  CB   . SER   B 1 7   ? 47.177 -24.990 -21.446 1.00 30.62 ?  7   SER   B CB   1 
ATOM   4259 O  OG   . SER   B 1 7   ? 47.210 -25.867 -22.558 1.00 34.32 ?  7   SER   B OG   1 
ATOM   4260 H  H    . SER   B 1 7   ? 46.237 -24.344 -18.894 1.00 30.40 ?  7   SER   B H    1 
ATOM   4261 H  HA   . SER   B 1 7   ? 45.129 -25.043 -21.264 1.00 33.67 ?  7   SER   B HA   1 
ATOM   4262 H  HB2  . SER   B 1 7   ? 47.241 -24.078 -21.770 1.00 36.73 ?  7   SER   B HB2  1 
ATOM   4263 H  HB3  . SER   B 1 7   ? 47.928 -25.186 -20.862 1.00 36.73 ?  7   SER   B HB3  1 
ATOM   4264 H  HG   . SER   B 1 7   ? 47.933 -25.775 -22.975 1.00 41.17 ?  7   SER   B HG   1 
ATOM   4265 N  N    . GLY   B 1 8   ? 45.092 -27.436 -20.754 1.00 27.07 ?  8   GLY   B N    1 
ATOM   4266 C  CA   . GLY   B 1 8   ? 45.048 -28.827 -20.368 1.00 26.61 ?  8   GLY   B CA   1 
ATOM   4267 C  C    . GLY   B 1 8   ? 44.092 -29.150 -19.249 1.00 25.22 ?  8   GLY   B C    1 
ATOM   4268 O  O    . GLY   B 1 8   ? 44.224 -30.213 -18.629 1.00 26.62 ?  8   GLY   B O    1 
ATOM   4269 H  H    . GLY   B 1 8   ? 44.631 -27.244 -21.449 1.00 32.46 ?  8   GLY   B H    1 
ATOM   4270 H  HA2  . GLY   B 1 8   ? 44.789 -29.356 -21.136 1.00 31.92 ?  8   GLY   B HA2  1 
ATOM   4271 H  HA3  . GLY   B 1 8   ? 45.931 -29.108 -20.088 1.00 31.92 ?  8   GLY   B HA3  1 
ATOM   4272 N  N    . TYR   B 1 9   ? 43.112 -28.291 -18.982 1.00 23.42 ?  9   TYR   B N    1 
ATOM   4273 C  CA   . TYR   B 1 9   ? 42.151 -28.560 -17.925 1.00 21.65 ?  9   TYR   B CA   1 
ATOM   4274 C  C    . TYR   B 1 9   ? 40.971 -29.360 -18.446 1.00 20.80 ?  9   TYR   B C    1 
ATOM   4275 O  O    . TYR   B 1 9   ? 40.559 -29.232 -19.603 1.00 22.45 ?  9   TYR   B O    1 
ATOM   4276 C  CB   . TYR   B 1 9   ? 41.638 -27.273 -17.288 1.00 20.89 ?  9   TYR   B CB   1 
ATOM   4277 C  CG   . TYR   B 1 9   ? 42.660 -26.648 -16.373 1.00 19.89 ?  9   TYR   B CG   1 
ATOM   4278 C  CD1  . TYR   B 1 9   ? 43.767 -25.987 -16.892 1.00 20.41 ?  9   TYR   B CD1  1 
ATOM   4279 C  CD2  . TYR   B 1 9   ? 42.539 -26.741 -14.996 1.00 19.00 ?  9   TYR   B CD2  1 
ATOM   4280 C  CE1  . TYR   B 1 9   ? 44.720 -25.428 -16.065 1.00 20.37 ?  9   TYR   B CE1  1 
ATOM   4281 C  CE2  . TYR   B 1 9   ? 43.490 -26.180 -14.157 1.00 19.29 ?  9   TYR   B CE2  1 
ATOM   4282 C  CZ   . TYR   B 1 9   ? 44.578 -25.523 -14.702 1.00 20.06 ?  9   TYR   B CZ   1 
ATOM   4283 O  OH   . TYR   B 1 9   ? 45.531 -24.973 -13.883 1.00 20.60 ?  9   TYR   B OH   1 
ATOM   4284 H  H    . TYR   B 1 9   ? 42.962 -27.564 -19.414 1.00 28.09 ?  9   TYR   B H    1 
ATOM   4285 H  HA   . TYR   B 1 9   ? 42.573 -29.086 -17.234 1.00 25.96 ?  9   TYR   B HA   1 
ATOM   4286 H  HB2  . TYR   B 1 9   ? 41.414 -26.630 -17.981 1.00 25.05 ?  9   TYR   B HB2  1 
ATOM   4287 H  HB3  . TYR   B 1 9   ? 40.857 -27.482 -16.759 1.00 25.05 ?  9   TYR   B HB3  1 
ATOM   4288 H  HD1  . TYR   B 1 9   ? 43.867 -25.924 -17.815 1.00 24.47 ?  9   TYR   B HD1  1 
ATOM   4289 H  HD2  . TYR   B 1 9   ? 41.804 -27.183 -14.628 1.00 22.78 ?  9   TYR   B HD2  1 
ATOM   4290 H  HE1  . TYR   B 1 9   ? 45.448 -24.992 -16.428 1.00 24.43 ?  9   TYR   B HE1  1 
ATOM   4291 H  HE2  . TYR   B 1 9   ? 43.387 -26.249 -13.233 1.00 23.12 ?  9   TYR   B HE2  1 
ATOM   4292 H  HH   . TYR   B 1 9   ? 46.123 -24.606 -14.344 1.00 24.70 ?  9   TYR   B HH   1 
ATOM   4293 N  N    . LEU   B 1 10  ? 40.438 -30.201 -17.569 1.00 18.94 ?  10  LEU   B N    1 
ATOM   4294 C  CA   . LEU   B 1 10  ? 39.234 -30.966 -17.839 1.00 19.03 ?  10  LEU   B CA   1 
ATOM   4295 C  C    . LEU   B 1 10  ? 38.044 -30.200 -17.278 1.00 18.28 ?  10  LEU   B C    1 
ATOM   4296 O  O    . LEU   B 1 10  ? 38.061 -29.775 -16.119 1.00 18.09 ?  10  LEU   B O    1 
ATOM   4297 C  CB   . LEU   B 1 10  ? 39.341 -32.335 -17.166 1.00 19.77 ?  10  LEU   B CB   1 
ATOM   4298 C  CG   . LEU   B 1 10  ? 38.180 -33.284 -17.445 1.00 21.73 ?  10  LEU   B CG   1 
ATOM   4299 C  CD1  . LEU   B 1 10  ? 38.226 -33.758 -18.889 1.00 23.18 ?  10  LEU   B CD1  1 
ATOM   4300 C  CD2  . LEU   B 1 10  ? 38.205 -34.458 -16.484 1.00 22.94 ?  10  LEU   B CD2  1 
ATOM   4301 H  H    . LEU   B 1 10  ? 40.761 -30.349 -16.781 1.00 22.71 ?  10  LEU   B H    1 
ATOM   4302 H  HA   . LEU   B 1 10  ? 39.114 -31.089 -18.790 1.00 22.81 ?  10  LEU   B HA   1 
ATOM   4303 H  HB2  . LEU   B 1 10  ? 40.153 -32.769 -17.475 1.00 23.71 ?  10  LEU   B HB2  1 
ATOM   4304 H  HB3  . LEU   B 1 10  ? 39.389 -32.209 -16.204 1.00 23.71 ?  10  LEU   B HB3  1 
ATOM   4305 H  HG   . LEU   B 1 10  ? 37.344 -32.810 -17.313 1.00 26.05 ?  10  LEU   B HG   1 
ATOM   4306 H  HD11 . LEU   B 1 10  ? 37.528 -34.417 -19.025 1.00 27.80 ?  10  LEU   B HD11 1 
ATOM   4307 H  HD12 . LEU   B 1 10  ? 38.083 -32.998 -19.475 1.00 27.80 ?  10  LEU   B HD12 1 
ATOM   4308 H  HD13 . LEU   B 1 10  ? 39.094 -34.153 -19.063 1.00 27.80 ?  10  LEU   B HD13 1 
ATOM   4309 H  HD21 . LEU   B 1 10  ? 37.461 -35.043 -16.686 1.00 27.51 ?  10  LEU   B HD21 1 
ATOM   4310 H  HD22 . LEU   B 1 10  ? 39.043 -34.931 -16.591 1.00 27.51 ?  10  LEU   B HD22 1 
ATOM   4311 H  HD23 . LEU   B 1 10  ? 38.127 -34.119 -15.578 1.00 27.51 ?  10  LEU   B HD23 1 
ATOM   4312 N  N    . LYS   B 1 11  ? 37.020 -30.019 -18.102 1.00 19.30 ?  11  LYS   B N    1 
ATOM   4313 C  CA   . LYS   B 1 11  ? 35.825 -29.300 -17.687 1.00 20.92 ?  11  LYS   B CA   1 
ATOM   4314 C  C    . LYS   B 1 11  ? 34.944 -30.225 -16.851 1.00 20.38 ?  11  LYS   B C    1 
ATOM   4315 O  O    . LYS   B 1 11  ? 34.574 -31.314 -17.304 1.00 22.48 ?  11  LYS   B O    1 
ATOM   4316 C  CB   . LYS   B 1 11  ? 35.082 -28.822 -18.933 1.00 24.69 ?  11  LYS   B CB   1 
ATOM   4317 C  CG   . LYS   B 1 11  ? 33.920 -27.881 -18.678 1.00 28.40 ?  11  LYS   B CG   1 
ATOM   4318 C  CD   . LYS   B 1 11  ? 33.210 -27.552 -19.986 1.00 31.37 ?  11  LYS   B CD   1 
ATOM   4319 C  CE   . LYS   B 1 11  ? 32.179 -26.451 -19.810 1.00 33.59 ?  11  LYS   B CE   1 
ATOM   4320 N  NZ   . LYS   B 1 11  ? 32.816 -25.122 -19.604 1.00 34.84 ?  11  LYS   B NZ   1 
ATOM   4321 H  H    . LYS   B 1 11  ? 36.988 -30.311 -18.910 1.00 23.14 ?  11  LYS   B H    1 
ATOM   4322 H  HA   . LYS   B 1 11  ? 36.071 -28.532 -17.151 1.00 25.08 ?  11  LYS   B HA   1 
ATOM   4323 H  HB2  . LYS   B 1 11  ? 35.713 -28.354 -19.504 1.00 29.61 ?  11  LYS   B HB2  1 
ATOM   4324 H  HB3  . LYS   B 1 11  ? 34.733 -29.595 -19.401 1.00 29.61 ?  11  LYS   B HB3  1 
ATOM   4325 H  HG2  . LYS   B 1 11  ? 33.284 -28.306 -18.083 1.00 34.06 ?  11  LYS   B HG2  1 
ATOM   4326 H  HG3  . LYS   B 1 11  ? 34.250 -27.055 -18.292 1.00 34.06 ?  11  LYS   B HG3  1 
ATOM   4327 H  HD2  . LYS   B 1 11  ? 33.865 -27.254 -20.638 1.00 37.62 ?  11  LYS   B HD2  1 
ATOM   4328 H  HD3  . LYS   B 1 11  ? 32.755 -28.346 -20.310 1.00 37.62 ?  11  LYS   B HD3  1 
ATOM   4329 H  HE2  . LYS   B 1 11  ? 31.626 -26.402 -20.605 1.00 40.29 ?  11  LYS   B HE2  1 
ATOM   4330 H  HE3  . LYS   B 1 11  ? 31.633 -26.652 -19.034 1.00 40.29 ?  11  LYS   B HE3  1 
ATOM   4331 H  HZ1  . LYS   B 1 11  ? 32.190 -24.497 -19.509 1.00 41.79 ?  11  LYS   B HZ1  1 
ATOM   4332 H  HZ2  . LYS   B 1 11  ? 33.324 -25.138 -18.874 1.00 41.79 ?  11  LYS   B HZ2  1 
ATOM   4333 H  HZ3  . LYS   B 1 11  ? 33.325 -24.917 -20.306 1.00 41.79 ?  11  LYS   B HZ3  1 
ATOM   4334 N  N    . LEU   B 1 12  ? 34.608 -29.796 -15.633 1.00 19.05 ?  12  LEU   B N    1 
ATOM   4335 C  CA   . LEU   B 1 12  ? 33.656 -30.507 -14.785 1.00 18.38 ?  12  LEU   B CA   1 
ATOM   4336 C  C    . LEU   B 1 12  ? 32.264 -29.903 -14.866 1.00 18.05 ?  12  LEU   B C    1 
ATOM   4337 O  O    . LEU   B 1 12  ? 31.280 -30.629 -15.025 1.00 18.59 ?  12  LEU   B O    1 
ATOM   4338 C  CB   . LEU   B 1 12  ? 34.121 -30.521 -13.324 1.00 17.80 ?  12  LEU   B CB   1 
ATOM   4339 C  CG   . LEU   B 1 12  ? 35.461 -31.200 -13.043 1.00 17.95 ?  12  LEU   B CG   1 
ATOM   4340 C  CD1  . LEU   B 1 12  ? 35.792 -31.134 -11.566 1.00 18.07 ?  12  LEU   B CD1  1 
ATOM   4341 C  CD2  . LEU   B 1 12  ? 35.464 -32.643 -13.533 1.00 18.62 ?  12  LEU   B CD2  1 
ATOM   4342 H  H    . LEU   B 1 12  ? 34.918 -29.079 -15.273 1.00 22.84 ?  12  LEU   B H    1 
ATOM   4343 H  HA   . LEU   B 1 12  ? 33.586 -31.422 -15.089 1.00 22.04 ?  12  LEU   B HA   1 
ATOM   4344 H  HB2  . LEU   B 1 12  ? 34.189 -29.606 -13.018 1.00 21.34 ?  12  LEU   B HB2  1 
ATOM   4345 H  HB3  . LEU   B 1 12  ? 33.446 -30.985 -12.799 1.00 21.34 ?  12  LEU   B HB3  1 
ATOM   4346 H  HG   . LEU   B 1 12  ? 36.153 -30.724 -13.524 1.00 21.52 ?  12  LEU   B HG   1 
ATOM   4347 H  HD11 . LEU   B 1 12  ? 36.649 -31.568 -11.415 1.00 21.66 ?  12  LEU   B HD11 1 
ATOM   4348 H  HD12 . LEU   B 1 12  ? 35.843 -30.204 -11.293 1.00 21.66 ?  12  LEU   B HD12 1 
ATOM   4349 H  HD13 . LEU   B 1 12  ? 35.099 -31.589 -11.062 1.00 21.66 ?  12  LEU   B HD13 1 
ATOM   4350 H  HD21 . LEU   B 1 12  ? 36.275 -33.077 -13.231 1.00 22.32 ?  12  LEU   B HD21 1 
ATOM   4351 H  HD22 . LEU   B 1 12  ? 34.688 -33.101 -13.172 1.00 22.32 ?  12  LEU   B HD22 1 
ATOM   4352 H  HD23 . LEU   B 1 12  ? 35.426 -32.648 -14.503 1.00 22.32 ?  12  LEU   B HD23 1 
ATOM   4353 N  N    . THR   B 1 13  ? 32.171 -28.583 -14.748 1.00 18.08 ?  13  THR   B N    1 
ATOM   4354 C  CA   . THR   B 1 13  ? 30.944 -27.833 -14.954 1.00 18.27 ?  13  THR   B CA   1 
ATOM   4355 C  C    . THR   B 1 13  ? 31.278 -26.636 -15.838 1.00 20.15 ?  13  THR   B C    1 
ATOM   4356 O  O    . THR   B 1 13  ? 32.422 -26.450 -16.268 1.00 21.04 ?  13  THR   B O    1 
ATOM   4357 C  CB   . THR   B 1 13  ? 30.343 -27.354 -13.626 1.00 18.14 ?  13  THR   B CB   1 
ATOM   4358 O  OG1  . THR   B 1 13  ? 31.182 -26.330 -13.078 1.00 17.82 ?  13  THR   B OG1  1 
ATOM   4359 C  CG2  . THR   B 1 13  ? 30.223 -28.507 -12.631 1.00 18.49 ?  13  THR   B CG2  1 
ATOM   4360 H  H    . THR   B 1 13  ? 32.836 -28.076 -14.543 1.00 21.67 ?  13  THR   B H    1 
ATOM   4361 H  HA   . THR   B 1 13  ? 30.289 -28.388 -15.405 1.00 21.91 ?  13  THR   B HA   1 
ATOM   4362 H  HB   . THR   B 1 13  ? 29.453 -26.990 -13.785 1.00 21.75 ?  13  THR   B HB   1 
ATOM   4363 H  HG1  . THR   B 1 13  ? 30.872 -25.566 -13.268 1.00 21.37 ?  13  THR   B HG1  1 
ATOM   4364 H  HG21 . THR   B 1 13  ? 29.727 -28.220 -11.848 1.00 22.17 ?  13  THR   B HG21 1 
ATOM   4365 H  HG22 . THR   B 1 13  ? 29.758 -29.251 -13.043 1.00 22.17 ?  13  THR   B HG22 1 
ATOM   4366 H  HG23 . THR   B 1 13  ? 31.106 -28.799 -12.356 1.00 22.17 ?  13  THR   B HG23 1 
ATOM   4367 N  N    A ASP   B 1 14  ? 30.264 -25.812 -16.102 0.70 21.17 ?  14  ASP   B N    1 
ATOM   4368 N  N    B ASP   B 1 14  ? 30.269 -25.799 -16.098 0.30 21.10 ?  14  ASP   B N    1 
ATOM   4369 C  CA   A ASP   B 1 14  ? 30.472 -24.652 -16.960 0.70 22.70 ?  14  ASP   B CA   1 
ATOM   4370 C  CA   B ASP   B 1 14  ? 30.470 -24.646 -16.970 0.30 21.93 ?  14  ASP   B CA   1 
ATOM   4371 C  C    A ASP   B 1 14  ? 31.573 -23.742 -16.429 0.70 21.18 ?  14  ASP   B C    1 
ATOM   4372 C  C    B ASP   B 1 14  ? 31.459 -23.637 -16.402 0.30 20.25 ?  14  ASP   B C    1 
ATOM   4373 O  O    A ASP   B 1 14  ? 32.235 -23.053 -17.216 0.70 22.56 ?  14  ASP   B O    1 
ATOM   4374 O  O    B ASP   B 1 14  ? 31.898 -22.745 -17.136 0.30 20.23 ?  14  ASP   B O    1 
ATOM   4375 C  CB   A ASP   B 1 14  ? 29.167 -23.873 -17.120 0.70 26.02 ?  14  ASP   B CB   1 
ATOM   4376 C  CB   B ASP   B 1 14  ? 29.143 -23.935 -17.237 0.30 24.44 ?  14  ASP   B CB   1 
ATOM   4377 C  CG   A ASP   B 1 14  ? 28.196 -24.543 -18.066 0.70 29.63 ?  14  ASP   B CG   1 
ATOM   4378 C  CG   B ASP   B 1 14  ? 28.282 -24.672 -18.244 0.30 26.56 ?  14  ASP   B CG   1 
ATOM   4379 O  OD1  A ASP   B 1 14  ? 28.585 -25.513 -18.756 0.70 31.32 ?  14  ASP   B OD1  1 
ATOM   4380 O  OD1  B ASP   B 1 14  ? 28.850 -25.320 -19.149 0.30 27.29 ?  14  ASP   B OD1  1 
ATOM   4381 O  OD2  A ASP   B 1 14  ? 27.031 -24.099 -18.113 0.70 31.15 -1 14  ASP   B OD2  1 
ATOM   4382 O  OD2  B ASP   B 1 14  ? 27.040 -24.608 -18.132 0.30 27.58 -1 14  ASP   B OD2  1 
ATOM   4383 H  H    A ASP   B 1 14  ? 29.465 -25.893 -15.792 0.70 25.38 ?  14  ASP   B H    1 
ATOM   4384 H  H    B ASP   B 1 14  ? 29.472 -25.877 -15.787 0.30 25.30 ?  14  ASP   B H    1 
ATOM   4385 H  HA   A ASP   B 1 14  ? 30.746 -24.951 -17.836 0.70 27.23 ?  14  ASP   B HA   1 
ATOM   4386 H  HA   B ASP   B 1 14  ? 30.813 -24.956 -17.822 0.30 26.30 ?  14  ASP   B HA   1 
ATOM   4387 H  HB2  A ASP   B 1 14  ? 28.722 -23.807 -16.262 0.70 31.21 ?  14  ASP   B HB2  1 
ATOM   4388 H  HB2  B ASP   B 1 14  ? 28.649 -23.868 -16.405 0.30 29.31 ?  14  ASP   B HB2  1 
ATOM   4389 H  HB3  A ASP   B 1 14  ? 29.359 -22.988 -17.466 0.70 31.21 ?  14  ASP   B HB3  1 
ATOM   4390 H  HB3  B ASP   B 1 14  ? 29.329 -23.042 -17.580 0.30 29.31 ?  14  ASP   B HB3  1 
ATOM   4391 N  N    . ASN   B 1 15  ? 31.794 -23.727 -15.112 1.00 18.60 ?  15  ASN   B N    1 
ATOM   4392 C  CA   . ASN   B 1 15  ? 32.754 -22.806 -14.510 1.00 16.38 ?  15  ASN   B CA   1 
ATOM   4393 C  C    . ASN   B 1 15  ? 33.850 -23.459 -13.678 1.00 15.16 ?  15  ASN   B C    1 
ATOM   4394 O  O    . ASN   B 1 15  ? 34.696 -22.731 -13.149 1.00 15.48 ?  15  ASN   B O    1 
ATOM   4395 C  CB   . ASN   B 1 15  ? 32.040 -21.752 -13.648 1.00 16.27 ?  15  ASN   B CB   1 
ATOM   4396 C  CG   . ASN   B 1 15  ? 31.419 -22.348 -12.405 1.00 16.02 ?  15  ASN   B CG   1 
ATOM   4397 O  OD1  . ASN   B 1 15  ? 30.478 -23.141 -12.492 1.00 17.60 ?  15  ASN   B OD1  1 
ATOM   4398 N  ND2  . ASN   B 1 15  ? 31.946 -21.996 -11.244 1.00 14.91 ?  15  ASN   B ND2  1 
ATOM   4399 H  H    A ASN   B 1 15  ? 31.398 -24.246 -14.547 0.70 22.30 ?  15  ASN   B H    1 
ATOM   4400 H  H    B ASN   B 1 15  ? 31.448 -24.291 -14.559 0.30 22.30 ?  15  ASN   B H    1 
ATOM   4401 H  HA   . ASN   B 1 15  ? 33.197 -22.323 -15.217 1.00 19.63 ?  15  ASN   B HA   1 
ATOM   4402 H  HB2  . ASN   B 1 15  ? 32.686 -21.072 -13.372 1.00 19.50 ?  15  ASN   B HB2  1 
ATOM   4403 H  HB3  . ASN   B 1 15  ? 31.333 -21.328 -14.167 1.00 19.50 ?  15  ASN   B HB3  1 
ATOM   4404 H  HD21 . ASN   B 1 15  ? 31.627 -22.308 -10.507 1.00 17.87 ?  15  ASN   B HD21 1 
ATOM   4405 H  HD22 . ASN   B 1 15  ? 32.618 -21.449 -11.214 1.00 17.87 ?  15  ASN   B HD22 1 
ATOM   4406 N  N    . VAL   B 1 16  ? 33.866 -24.786 -13.532 1.00 15.00 ?  16  VAL   B N    1 
ATOM   4407 C  CA   . VAL   B 1 16  ? 34.864 -25.475 -12.722 1.00 14.52 ?  16  VAL   B CA   1 
ATOM   4408 C  C    . VAL   B 1 16  ? 35.655 -26.411 -13.616 1.00 14.44 ?  16  VAL   B C    1 
ATOM   4409 O  O    . VAL   B 1 16  ? 35.076 -27.292 -14.270 1.00 15.61 ?  16  VAL   B O    1 
ATOM   4410 C  CB   . VAL   B 1 16  ? 34.236 -26.237 -11.541 1.00 15.23 ?  16  VAL   B CB   1 
ATOM   4411 C  CG1  . VAL   B 1 16  ? 35.318 -26.973 -10.743 1.00 15.09 ?  16  VAL   B CG1  1 
ATOM   4412 C  CG2  . VAL   B 1 16  ? 33.430 -25.282 -10.659 1.00 15.27 ?  16  VAL   B CG2  1 
ATOM   4413 H  H    . VAL   B 1 16  ? 33.290 -25.313 -13.896 1.00 17.98 ?  16  VAL   B H    1 
ATOM   4414 H  HA   . VAL   B 1 16  ? 35.478 -24.820 -12.354 1.00 17.40 ?  16  VAL   B HA   1 
ATOM   4415 H  HB   . VAL   B 1 16  ? 33.624 -26.905 -11.893 1.00 18.26 ?  16  VAL   B HB   1 
ATOM   4416 H  HG11 . VAL   B 1 16  ? 34.938 -27.276 -9.905  1.00 18.09 ?  16  VAL   B HG11 1 
ATOM   4417 H  HG12 . VAL   B 1 16  ? 35.636 -27.730 -11.257 1.00 18.09 ?  16  VAL   B HG12 1 
ATOM   4418 H  HG13 . VAL   B 1 16  ? 36.051 -26.358 -10.568 1.00 18.09 ?  16  VAL   B HG13 1 
ATOM   4419 H  HG21 . VAL   B 1 16  ? 33.096 -25.770 -9.891  1.00 18.30 ?  16  VAL   B HG21 1 
ATOM   4420 H  HG22 . VAL   B 1 16  ? 34.003 -24.558 -10.372 1.00 18.30 ?  16  VAL   B HG22 1 
ATOM   4421 H  HG23 . VAL   B 1 16  ? 32.685 -24.930 -11.175 1.00 18.30 ?  16  VAL   B HG23 1 
ATOM   4422 N  N    . TYR   B 1 17  ? 36.978 -26.248 -13.593 1.00 14.94 ?  17  TYR   B N    1 
ATOM   4423 C  CA   . TYR   B 1 17  ? 37.928 -26.999 -14.400 1.00 15.11 ?  17  TYR   B CA   1 
ATOM   4424 C  C    . TYR   B 1 17  ? 38.980 -27.604 -13.481 1.00 14.35 ?  17  TYR   B C    1 
ATOM   4425 O  O    . TYR   B 1 17  ? 39.254 -27.067 -12.404 1.00 14.55 ?  17  TYR   B O    1 
ATOM   4426 C  CB   . TYR   B 1 17  ? 38.635 -26.080 -15.407 1.00 17.91 ?  17  TYR   B CB   1 
ATOM   4427 C  CG   . TYR   B 1 17  ? 37.705 -25.310 -16.312 1.00 21.44 ?  17  TYR   B CG   1 
ATOM   4428 C  CD1  . TYR   B 1 17  ? 37.121 -24.118 -15.899 1.00 22.55 ?  17  TYR   B CD1  1 
ATOM   4429 C  CD2  . TYR   B 1 17  ? 37.410 -25.778 -17.585 1.00 23.21 ?  17  TYR   B CD2  1 
ATOM   4430 C  CE1  . TYR   B 1 17  ? 36.265 -23.413 -16.729 1.00 24.24 ?  17  TYR   B CE1  1 
ATOM   4431 C  CE2  . TYR   B 1 17  ? 36.561 -25.082 -18.423 1.00 24.61 ?  17  TYR   B CE2  1 
ATOM   4432 C  CZ   . TYR   B 1 17  ? 35.989 -23.902 -17.989 1.00 25.22 ?  17  TYR   B CZ   1 
ATOM   4433 O  OH   . TYR   B 1 17  ? 35.145 -23.205 -18.821 1.00 26.94 ?  17  TYR   B OH   1 
ATOM   4434 H  H    . TYR   B 1 17  ? 37.375 -25.669 -13.085 1.00 17.90 ?  17  TYR   B H    1 
ATOM   4435 H  HA   . TYR   B 1 17  ? 37.468 -27.709 -14.880 1.00 18.11 ?  17  TYR   B HA   1 
ATOM   4436 H  HB2  . TYR   B 1 17  ? 39.179 -25.441 -14.922 1.00 21.47 ?  17  TYR   B HB2  1 
ATOM   4437 H  HB3  . TYR   B 1 17  ? 39.196 -26.625 -15.974 1.00 21.47 ?  17  TYR   B HB3  1 
ATOM   4438 H  HD1  . TYR   B 1 17  ? 37.305 -23.789 -15.050 1.00 27.03 ?  17  TYR   B HD1  1 
ATOM   4439 H  HD2  . TYR   B 1 17  ? 37.788 -26.572 -17.881 1.00 27.83 ?  17  TYR   B HD2  1 
ATOM   4440 H  HE1  . TYR   B 1 17  ? 35.881 -22.615 -16.442 1.00 29.06 ?  17  TYR   B HE1  1 
ATOM   4441 H  HE2  . TYR   B 1 17  ? 36.367 -25.407 -19.275 1.00 29.51 ?  17  TYR   B HE2  1 
ATOM   4442 H  HH   . TYR   B 1 17  ? 35.059 -23.605 -19.555 1.00 32.30 ?  17  TYR   B HH   1 
ATOM   4443 N  N    . ILE   B 1 18  ? 39.592 -28.712 -13.911 1.00 14.65 ?  18  ILE   B N    1 
ATOM   4444 C  CA   . ILE   B 1 18  ? 40.526 -29.431 -13.049 1.00 14.53 ?  18  ILE   B CA   1 
ATOM   4445 C  C    . ILE   B 1 18  ? 41.692 -29.977 -13.868 1.00 15.06 ?  18  ILE   B C    1 
ATOM   4446 O  O    . ILE   B 1 18  ? 41.536 -30.369 -15.029 1.00 16.58 ?  18  ILE   B O    1 
ATOM   4447 C  CB   . ILE   B 1 18  ? 39.776 -30.536 -12.253 1.00 15.17 ?  18  ILE   B CB   1 
ATOM   4448 C  CG1  . ILE   B 1 18  ? 40.638 -31.088 -11.114 1.00 15.35 ?  18  ILE   B CG1  1 
ATOM   4449 C  CG2  . ILE   B 1 18  ? 39.283 -31.660 -13.178 1.00 15.30 ?  18  ILE   B CG2  1 
ATOM   4450 C  CD1  . ILE   B 1 18  ? 39.823 -31.877 -10.088 1.00 16.37 ?  18  ILE   B CD1  1 
ATOM   4451 H  H    . ILE   B 1 18  ? 39.483 -29.065 -14.686 1.00 17.56 ?  18  ILE   B H    1 
ATOM   4452 H  HA   . ILE   B 1 18  ? 40.884 -28.814 -12.396 1.00 17.42 ?  18  ILE   B HA   1 
ATOM   4453 H  HB   . ILE   B 1 18  ? 38.990 -30.135 -11.846 1.00 18.18 ?  18  ILE   B HB   1 
ATOM   4454 H  HG12 . ILE   B 1 18  ? 41.309 -31.681 -11.480 1.00 18.40 ?  18  ILE   B HG12 1 
ATOM   4455 H  HG13 . ILE   B 1 18  ? 41.059 -30.348 -10.650 1.00 18.40 ?  18  ILE   B HG13 1 
ATOM   4456 H  HG21 . ILE   B 1 18  ? 38.696 -32.249 -12.676 1.00 18.34 ?  18  ILE   B HG21 1 
ATOM   4457 H  HG22 . ILE   B 1 18  ? 38.798 -31.261 -13.916 1.00 18.34 ?  18  ILE   B HG22 1 
ATOM   4458 H  HG23 . ILE   B 1 18  ? 40.047 -32.153 -13.508 1.00 18.34 ?  18  ILE   B HG23 1 
ATOM   4459 H  HD11 . ILE   B 1 18  ? 40.412 -32.162 -9.369  1.00 19.62 ?  18  ILE   B HD11 1 
ATOM   4460 H  HD12 . ILE   B 1 18  ? 39.123 -31.308 -9.733  1.00 19.62 ?  18  ILE   B HD12 1 
ATOM   4461 H  HD13 . ILE   B 1 18  ? 39.434 -32.652 -10.521 1.00 19.62 ?  18  ILE   B HD13 1 
ATOM   4462 N  N    . LYS   B 1 19  ? 42.868 -30.023 -13.238 1.00 15.42 ?  19  LYS   B N    1 
ATOM   4463 C  CA   . LYS   B 1 19  ? 44.085 -30.490 -13.889 1.00 16.29 ?  19  LYS   B CA   1 
ATOM   4464 C  C    . LYS   B 1 19  ? 44.978 -31.175 -12.865 1.00 15.81 ?  19  LYS   B C    1 
ATOM   4465 O  O    . LYS   B 1 19  ? 45.051 -30.749 -11.711 1.00 15.08 ?  19  LYS   B O    1 
ATOM   4466 C  CB   . LYS   B 1 19  ? 44.858 -29.320 -14.516 1.00 17.47 ?  19  LYS   B CB   1 
ATOM   4467 C  CG   . LYS   B 1 19  ? 46.061 -29.730 -15.341 1.00 19.35 ?  19  LYS   B CG   1 
ATOM   4468 C  CD   . LYS   B 1 19  ? 46.772 -28.501 -15.892 1.00 21.37 ?  19  LYS   B CD   1 
ATOM   4469 C  CE   . LYS   B 1 19  ? 47.928 -28.883 -16.795 1.00 23.27 ?  19  LYS   B CE   1 
ATOM   4470 N  NZ   . LYS   B 1 19  ? 48.675 -27.692 -17.278 1.00 24.61 ?  19  LYS   B NZ   1 
ATOM   4471 H  H    . LYS   B 1 19  ? 42.975 -29.780 -12.416 1.00 18.48 ?  19  LYS   B H    1 
ATOM   4472 H  HA   . LYS   B 1 19  ? 43.852 -31.125 -14.583 1.00 19.53 ?  19  LYS   B HA   1 
ATOM   4473 H  HB2  . LYS   B 1 19  ? 44.253 -28.830 -15.095 1.00 20.94 ?  19  LYS   B HB2  1 
ATOM   4474 H  HB3  . LYS   B 1 19  ? 45.165 -28.737 -13.800 1.00 20.94 ?  19  LYS   B HB3  1 
ATOM   4475 H  HG2  . LYS   B 1 19  ? 46.679 -30.224 -14.780 1.00 23.20 ?  19  LYS   B HG2  1 
ATOM   4476 H  HG3  . LYS   B 1 19  ? 45.763 -30.280 -16.083 1.00 23.20 ?  19  LYS   B HG3  1 
ATOM   4477 H  HD2  . LYS   B 1 19  ? 46.140 -27.973 -16.406 1.00 25.62 ?  19  LYS   B HD2  1 
ATOM   4478 H  HD3  . LYS   B 1 19  ? 47.120 -27.978 -15.152 1.00 25.62 ?  19  LYS   B HD3  1 
ATOM   4479 H  HE2  . LYS   B 1 19  ? 48.541 -29.450 -16.301 1.00 27.91 ?  19  LYS   B HE2  1 
ATOM   4480 H  HE3  . LYS   B 1 19  ? 47.581 -29.360 -17.566 1.00 27.91 ?  19  LYS   B HE3  1 
ATOM   4481 H  HZ1  . LYS   B 1 19  ? 49.325 -27.947 -17.831 1.00 29.51 ?  19  LYS   B HZ1  1 
ATOM   4482 H  HZ2  . LYS   B 1 19  ? 48.125 -27.144 -17.713 1.00 29.51 ?  19  LYS   B HZ2  1 
ATOM   4483 H  HZ3  . LYS   B 1 19  ? 49.034 -27.259 -16.590 1.00 29.51 ?  19  LYS   B HZ3  1 
ATOM   4484 N  N    . ASN   B 1 20  ? 45.655 -32.234 -13.297 1.00 17.09 ?  20  ASN   B N    1 
ATOM   4485 C  CA   . ASN   B 1 20  ? 46.693 -32.867 -12.488 1.00 18.30 ?  20  ASN   B CA   1 
ATOM   4486 C  C    . ASN   B 1 20  ? 47.958 -32.038 -12.680 1.00 18.47 ?  20  ASN   B C    1 
ATOM   4487 O  O    . ASN   B 1 20  ? 48.596 -32.102 -13.735 1.00 20.45 ?  20  ASN   B O    1 
ATOM   4488 C  CB   . ASN   B 1 20  ? 46.869 -34.315 -12.940 1.00 20.04 ?  20  ASN   B CB   1 
ATOM   4489 C  CG   . ASN   B 1 20  ? 48.017 -35.030 -12.247 1.00 21.15 ?  20  ASN   B CG   1 
ATOM   4490 O  OD1  . ASN   B 1 20  ? 48.679 -35.884 -12.850 1.00 23.61 ?  20  ASN   B OD1  1 
ATOM   4491 N  ND2  . ASN   B 1 20  ? 48.253 -34.706 -10.984 1.00 20.67 ?  20  ASN   B ND2  1 
ATOM   4492 H  H    . ASN   B 1 20  ? 45.523 -32.612 -14.059 1.00 20.48 ?  20  ASN   B H    1 
ATOM   4493 H  HA   . ASN   B 1 20  ? 46.421 -32.852 -11.553 1.00 21.94 ?  20  ASN   B HA   1 
ATOM   4494 H  HB2  . ASN   B 1 20  ? 46.050 -34.803 -12.749 1.00 24.03 ?  20  ASN   B HB2  1 
ATOM   4495 H  HB3  . ASN   B 1 20  ? 47.040 -34.320 -13.893 1.00 24.03 ?  20  ASN   B HB3  1 
ATOM   4496 H  HD21 . ASN   B 1 20  ? 48.894 -35.082 -10.556 1.00 24.79 ?  20  ASN   B HD21 1 
ATOM   4497 H  HD22 . ASN   B 1 20  ? 47.769 -34.108 -10.587 1.00 24.79 ?  20  ASN   B HD22 1 
ATOM   4498 N  N    . ALA   B 1 21  ? 48.316 -31.238 -11.671 1.00 18.22 ?  21  ALA   B N    1 
ATOM   4499 C  CA   . ALA   B 1 21  ? 49.427 -30.309 -11.818 1.00 19.07 ?  21  ALA   B CA   1 
ATOM   4500 C  C    . ALA   B 1 21  ? 49.884 -29.812 -10.456 1.00 17.83 ?  21  ALA   B C    1 
ATOM   4501 O  O    . ALA   B 1 21  ? 49.136 -29.837 -9.474  1.00 17.78 ?  21  ALA   B O    1 
ATOM   4502 C  CB   . ALA   B 1 21  ? 49.042 -29.125 -12.704 1.00 20.46 ?  21  ALA   B CB   1 
ATOM   4503 H  H    . ALA   B 1 21  ? 47.929 -31.217 -10.895 1.00 21.84 ?  21  ALA   B H    1 
ATOM   4504 H  HA   . ALA   B 1 21  ? 50.168 -30.775 -12.230 1.00 22.87 ?  21  ALA   B HA   1 
ATOM   4505 H  HB1  . ALA   B 1 21  ? 49.830 -28.584 -12.843 1.00 24.54 ?  21  ALA   B HB1  1 
ATOM   4506 H  HB2  . ALA   B 1 21  ? 48.715 -29.469 -13.547 1.00 24.54 ?  21  ALA   B HB2  1 
ATOM   4507 H  HB3  . ALA   B 1 21  ? 48.350 -28.614 -12.259 1.00 24.54 ?  21  ALA   B HB3  1 
ATOM   4508 N  N    . ASP   B 1 22  ? 51.143 -29.373 -10.430 1.00 17.11 ?  22  ASP   B N    1 
ATOM   4509 C  CA   . ASP   B 1 22  ? 51.755 -28.670 -9.306  1.00 16.51 ?  22  ASP   B CA   1 
ATOM   4510 C  C    . ASP   B 1 22  ? 51.346 -27.199 -9.391  1.00 15.37 ?  22  ASP   B C    1 
ATOM   4511 O  O    . ASP   B 1 22  ? 51.648 -26.526 -10.382 1.00 15.57 ?  22  ASP   B O    1 
ATOM   4512 C  CB   . ASP   B 1 22  ? 53.273 -28.843 -9.457  1.00 18.06 ?  22  ASP   B CB   1 
ATOM   4513 C  CG   . ASP   B 1 22  ? 54.096 -28.081 -8.432  1.00 19.63 ?  22  ASP   B CG   1 
ATOM   4514 O  OD1  . ASP   B 1 22  ? 53.730 -26.969 -8.025  1.00 19.53 ?  22  ASP   B OD1  1 
ATOM   4515 O  OD2  . ASP   B 1 22  ? 55.173 -28.595 -8.060  1.00 22.20 -1 22  ASP   B OD2  1 
ATOM   4516 H  H    . ASP   B 1 22  ? 51.692 -29.475 -11.088 1.00 20.51 ?  22  ASP   B H    1 
ATOM   4517 H  HA   . ASP   B 1 22  ? 51.467 -29.049 -8.459  1.00 19.79 ?  22  ASP   B HA   1 
ATOM   4518 H  HB2  . ASP   B 1 22  ? 53.498 -29.778 -9.368  1.00 21.65 ?  22  ASP   B HB2  1 
ATOM   4519 H  HB3  . ASP   B 1 22  ? 53.542 -28.514 -10.326 1.00 21.65 ?  22  ASP   B HB3  1 
ATOM   4520 N  N    . ILE   B 1 23  ? 50.641 -26.705 -8.365  1.00 14.09 ?  23  ILE   B N    1 
ATOM   4521 C  CA   . ILE   B 1 23  ? 50.048 -25.366 -8.438  1.00 13.43 ?  23  ILE   B CA   1 
ATOM   4522 C  C    . ILE   B 1 23  ? 51.103 -24.273 -8.583  1.00 13.15 ?  23  ILE   B C    1 
ATOM   4523 O  O    . ILE   B 1 23  ? 50.834 -23.228 -9.190  1.00 12.82 ?  23  ILE   B O    1 
ATOM   4524 C  CB   . ILE   B 1 23  ? 49.105 -25.120 -7.243  1.00 13.99 ?  23  ILE   B CB   1 
ATOM   4525 C  CG1  . ILE   B 1 23  ? 48.270 -23.850 -7.452  1.00 14.79 ?  23  ILE   B CG1  1 
ATOM   4526 C  CG2  . ILE   B 1 23  ? 49.864 -25.078 -5.936  1.00 15.17 ?  23  ILE   B CG2  1 
ATOM   4527 C  CD1  . ILE   B 1 23  ? 47.145 -23.685 -6.437  1.00 15.21 ?  23  ILE   B CD1  1 
ATOM   4528 H  H    . ILE   B 1 23  ? 50.500 -27.118 -7.624  1.00 16.89 ?  23  ILE   B H    1 
ATOM   4529 H  HA   . ILE   B 1 23  ? 49.502 -25.330 -9.236  1.00 16.10 ?  23  ILE   B HA   1 
ATOM   4530 H  HB   . ILE   B 1 23  ? 48.485 -25.868 -7.202  1.00 16.77 ?  23  ILE   B HB   1 
ATOM   4531 H  HG12 . ILE   B 1 23  ? 48.853 -23.076 -7.377  1.00 17.73 ?  23  ILE   B HG12 1 
ATOM   4532 H  HG13 . ILE   B 1 23  ? 47.872 -23.874 -8.338  1.00 17.73 ?  23  ILE   B HG13 1 
ATOM   4533 H  HG21 . ILE   B 1 23  ? 49.231 -25.072 -5.202  1.00 18.19 ?  23  ILE   B HG21 1 
ATOM   4534 H  HG22 . ILE   B 1 23  ? 50.431 -25.862 -5.877  1.00 18.19 ?  23  ILE   B HG22 1 
ATOM   4535 H  HG23 . ILE   B 1 23  ? 50.408 -24.275 -5.913  1.00 18.19 ?  23  ILE   B HG23 1 
ATOM   4536 H  HD11 . ILE   B 1 23  ? 46.615 -22.911 -6.679  1.00 18.23 ?  23  ILE   B HD11 1 
ATOM   4537 H  HD12 . ILE   B 1 23  ? 46.591 -24.483 -6.455  1.00 18.23 ?  23  ILE   B HD12 1 
ATOM   4538 H  HD13 . ILE   B 1 23  ? 47.529 -23.567 -5.557  1.00 18.23 ?  23  ILE   B HD13 1 
ATOM   4539 N  N    . VAL   B 1 24  ? 52.300 -24.478 -8.028  1.00 13.66 ?  24  VAL   B N    1 
ATOM   4540 C  CA   . VAL   B 1 24  ? 53.373 -23.497 -8.195  1.00 14.10 ?  24  VAL   B CA   1 
ATOM   4541 C  C    . VAL   B 1 24  ? 53.827 -23.455 -9.646  1.00 14.32 ?  24  VAL   B C    1 
ATOM   4542 O  O    . VAL   B 1 24  ? 53.977 -22.379 -10.238 1.00 14.96 ?  24  VAL   B O    1 
ATOM   4543 C  CB   . VAL   B 1 24  ? 54.547 -23.815 -7.249  1.00 15.06 ?  24  VAL   B CB   1 
ATOM   4544 C  CG1  . VAL   B 1 24  ? 55.753 -22.926 -7.563  1.00 16.22 ?  24  VAL   B CG1  1 
ATOM   4545 C  CG2  . VAL   B 1 24  ? 54.118 -23.646 -5.805  1.00 16.14 ?  24  VAL   B CG2  1 
ATOM   4546 H  H    . VAL   B 1 24  ? 52.514 -25.165 -7.557  1.00 16.38 ?  24  VAL   B H    1 
ATOM   4547 H  HA   . VAL   B 1 24  ? 53.039 -22.621 -7.961  1.00 16.90 ?  24  VAL   B HA   1 
ATOM   4548 H  HB   . VAL   B 1 24  ? 54.817 -24.743 -7.369  1.00 18.05 ?  24  VAL   B HB   1 
ATOM   4549 H  HG11 . VAL   B 1 24  ? 56.355 -22.934 -6.801  1.00 19.44 ?  24  VAL   B HG11 1 
ATOM   4550 H  HG12 . VAL   B 1 24  ? 56.206 -23.276 -8.344  1.00 19.44 ?  24  VAL   B HG12 1 
ATOM   4551 H  HG13 . VAL   B 1 24  ? 55.441 -22.025 -7.728  1.00 19.44 ?  24  VAL   B HG13 1 
ATOM   4552 H  HG21 . VAL   B 1 24  ? 54.842 -23.923 -5.223  1.00 19.34 ?  24  VAL   B HG21 1 
ATOM   4553 H  HG22 . VAL   B 1 24  ? 53.907 -22.712 -5.650  1.00 19.34 ?  24  VAL   B HG22 1 
ATOM   4554 H  HG23 . VAL   B 1 24  ? 53.334 -24.194 -5.641  1.00 19.34 ?  24  VAL   B HG23 1 
ATOM   4555 N  N    . GLU   B 1 25  ? 54.079 -24.628 -10.234 1.00 15.22 ?  25  GLU   B N    1 
ATOM   4556 C  CA   . GLU   B 1 25  ? 54.473 -24.668 -11.637 1.00 16.90 ?  25  GLU   B CA   1 
ATOM   4557 C  C    . GLU   B 1 25  ? 53.366 -24.123 -12.526 1.00 15.76 ?  25  GLU   B C    1 
ATOM   4558 O  O    . GLU   B 1 25  ? 53.634 -23.402 -13.497 1.00 16.56 ?  25  GLU   B O    1 
ATOM   4559 C  CB   . GLU   B 1 25  ? 54.860 -26.090 -12.035 1.00 20.43 ?  25  GLU   B CB   1 
ATOM   4560 C  CG   . GLU   B 1 25  ? 56.161 -26.542 -11.390 1.00 25.48 ?  25  GLU   B CG   1 
ATOM   4561 C  CD   . GLU   B 1 25  ? 57.277 -25.510 -11.494 1.00 31.23 ?  25  GLU   B CD   1 
ATOM   4562 O  OE1  . GLU   B 1 25  ? 57.655 -25.148 -12.629 1.00 32.73 ?  25  GLU   B OE1  1 
ATOM   4563 O  OE2  . GLU   B 1 25  ? 57.763 -25.044 -10.437 1.00 32.75 -1 25  GLU   B OE2  1 
ATOM   4564 H  H    . GLU   B 1 25  ? 54.027 -25.397 -9.849  1.00 18.24 ?  25  GLU   B H    1 
ATOM   4565 H  HA   . GLU   B 1 25  ? 55.231 -24.086 -11.762 1.00 20.25 ?  25  GLU   B HA   1 
ATOM   4566 H  HB2  . GLU   B 1 25  ? 54.156 -26.701 -11.754 1.00 24.50 ?  25  GLU   B HB2  1 
ATOM   4567 H  HB3  . GLU   B 1 25  ? 54.965 -26.131 -12.999 1.00 24.50 ?  25  GLU   B HB3  1 
ATOM   4568 H  HG2  . GLU   B 1 25  ? 56.007 -26.699 -10.451 1.00 30.55 ?  25  GLU   B HG2  1 
ATOM   4569 H  HG3  . GLU   B 1 25  ? 56.461 -27.351 -11.829 1.00 30.55 ?  25  GLU   B HG3  1 
ATOM   4570 N  N    . GLU   B 1 26  ? 52.114 -24.438 -12.193 1.00 14.52 ?  26  GLU   B N    1 
ATOM   4571 C  CA   . GLU   B 1 26  ? 50.989 -23.906 -12.951 1.00 15.06 ?  26  GLU   B CA   1 
ATOM   4572 C  C    . GLU   B 1 26  ? 50.952 -22.389 -12.879 1.00 14.04 ?  26  GLU   B C    1 
ATOM   4573 O  O    . GLU   B 1 26  ? 50.749 -21.718 -13.894 1.00 15.69 ?  26  GLU   B O    1 
ATOM   4574 C  CB   . GLU   B 1 26  ? 49.675 -24.481 -12.422 1.00 17.28 ?  26  GLU   B CB   1 
ATOM   4575 C  CG   . GLU   B 1 26  ? 49.207 -25.757 -13.099 1.00 20.93 ?  26  GLU   B CG   1 
ATOM   4576 C  CD   . GLU   B 1 26  ? 48.990 -25.622 -14.603 1.00 22.88 ?  26  GLU   B CD   1 
ATOM   4577 O  OE1  . GLU   B 1 26  ? 48.031 -24.957 -15.055 1.00 23.27 ?  26  GLU   B OE1  1 
ATOM   4578 O  OE2  . GLU   B 1 26  ? 49.784 -26.222 -15.335 1.00 24.56 -1 26  GLU   B OE2  1 
ATOM   4579 H  H    . GLU   B 1 26  ? 51.890 -24.960 -11.539 1.00 17.40 ?  26  GLU   B H    1 
ATOM   4580 H  HA   . GLU   B 1 26  ? 51.081 -24.162 -13.878 1.00 18.05 ?  26  GLU   B HA   1 
ATOM   4581 H  HB2  . GLU   B 1 26  ? 49.777 -24.678 -11.474 1.00 20.72 ?  26  GLU   B HB2  1 
ATOM   4582 H  HB3  . GLU   B 1 26  ? 48.975 -23.816 -12.535 1.00 20.72 ?  26  GLU   B HB3  1 
ATOM   4583 H  HG2  . GLU   B 1 26  ? 49.883 -26.431 -12.971 1.00 25.10 ?  26  GLU   B HG2  1 
ATOM   4584 H  HG3  . GLU   B 1 26  ? 48.369 -26.033 -12.698 1.00 25.10 ?  26  GLU   B HG3  1 
ATOM   4585 N  N    . ALA   B 1 27  ? 51.096 -21.833 -11.674 1.00 13.49 ?  27  ALA   B N    1 
ATOM   4586 C  CA   . ALA   B 1 27  ? 51.053 -20.382 -11.529 1.00 13.72 ?  27  ALA   B CA   1 
ATOM   4587 C  C    . ALA   B 1 27  ? 52.122 -19.717 -12.387 1.00 14.92 ?  27  ALA   B C    1 
ATOM   4588 O  O    . ALA   B 1 27  ? 51.861 -18.703 -13.052 1.00 15.60 ?  27  ALA   B O    1 
ATOM   4589 C  CB   . ALA   B 1 27  ? 51.213 -19.997 -10.058 1.00 14.18 ?  27  ALA   B CB   1 
ATOM   4590 H  H    . ALA   B 1 27  ? 51.210 -22.266 -10.936 1.00 16.16 ?  27  ALA   B H    1 
ATOM   4591 H  HA   . ALA   B 1 27  ? 50.190 -20.059 -11.827 1.00 16.44 ?  27  ALA   B HA   1 
ATOM   4592 H  HB1  . ALA   B 1 27  ? 51.175 -19.030 -9.978  1.00 17.00 ?  27  ALA   B HB1  1 
ATOM   4593 H  HB2  . ALA   B 1 27  ? 50.487 -20.396 -9.548  1.00 17.00 ?  27  ALA   B HB2  1 
ATOM   4594 H  HB3  . ALA   B 1 27  ? 52.064 -20.324 -9.734  1.00 17.00 ?  27  ALA   B HB3  1 
ATOM   4595 N  N    . LYS   B 1 28  ? 53.337 -20.268 -12.382 1.00 16.39 ?  28  LYS   B N    1 
ATOM   4596 C  CA   . LYS   B 1 28  ? 54.409 -19.648 -13.151 1.00 18.24 ?  28  LYS   B CA   1 
ATOM   4597 C  C    . LYS   B 1 28  ? 54.153 -19.737 -14.651 1.00 18.86 ?  28  LYS   B C    1 
ATOM   4598 O  O    . LYS   B 1 28  ? 54.559 -18.838 -15.399 1.00 20.49 ?  28  LYS   B O    1 
ATOM   4599 C  CB   . LYS   B 1 28  ? 55.767 -20.245 -12.763 1.00 20.77 ?  28  LYS   B CB   1 
ATOM   4600 C  CG   . LYS   B 1 28  ? 56.172 -19.908 -11.330 1.00 23.95 ?  28  LYS   B CG   1 
ATOM   4601 C  CD   . LYS   B 1 28  ? 57.604 -20.311 -11.003 1.00 27.67 ?  28  LYS   B CD   1 
ATOM   4602 C  CE   . LYS   B 1 28  ? 57.721 -21.785 -10.695 1.00 31.93 ?  28  LYS   B CE   1 
ATOM   4603 N  NZ   . LYS   B 1 28  ? 59.076 -22.112 -10.165 1.00 36.31 ?  28  LYS   B NZ   1 
ATOM   4604 H  H    . LYS   B 1 28  ? 53.561 -20.981 -11.954 1.00 19.65 ?  28  LYS   B H    1 
ATOM   4605 H  HA   . LYS   B 1 28  ? 54.439 -18.706 -12.927 1.00 21.87 ?  28  LYS   B HA   1 
ATOM   4606 H  HB2  . LYS   B 1 28  ? 55.726 -21.209 -12.841 1.00 24.91 ?  28  LYS   B HB2  1 
ATOM   4607 H  HB3  . LYS   B 1 28  ? 56.450 -19.891 -13.355 1.00 24.91 ?  28  LYS   B HB3  1 
ATOM   4608 H  HG2  . LYS   B 1 28  ? 56.093 -18.949 -11.200 1.00 28.72 ?  28  LYS   B HG2  1 
ATOM   4609 H  HG3  . LYS   B 1 28  ? 55.582 -20.374 -10.720 1.00 28.72 ?  28  LYS   B HG3  1 
ATOM   4610 H  HD2  . LYS   B 1 28  ? 58.170 -20.113 -11.765 1.00 33.18 ?  28  LYS   B HD2  1 
ATOM   4611 H  HD3  . LYS   B 1 28  ? 57.902 -19.812 -10.227 1.00 33.18 ?  28  LYS   B HD3  1 
ATOM   4612 H  HE2  . LYS   B 1 28  ? 57.064 -22.028 -10.023 1.00 38.30 ?  28  LYS   B HE2  1 
ATOM   4613 H  HE3  . LYS   B 1 28  ? 57.579 -22.298 -11.506 1.00 38.30 ?  28  LYS   B HE3  1 
ATOM   4614 H  HZ1  . LYS   B 1 28  ? 59.132 -22.981 -9.987  1.00 43.56 ?  28  LYS   B HZ1  1 
ATOM   4615 H  HZ2  . LYS   B 1 28  ? 59.696 -21.898 -10.767 1.00 43.56 ?  28  LYS   B HZ2  1 
ATOM   4616 H  HZ3  . LYS   B 1 28  ? 59.228 -21.653 -9.418  1.00 43.56 ?  28  LYS   B HZ3  1 
ATOM   4617 N  N    . LYS   B 1 29  ? 53.453 -20.778 -15.105 1.00 19.83 ?  29  LYS   B N    1 
ATOM   4618 C  CA   . LYS   B 1 29  ? 53.159 -20.931 -16.526 1.00 22.76 ?  29  LYS   B CA   1 
ATOM   4619 C  C    . LYS   B 1 29  ? 51.912 -20.162 -16.958 1.00 22.21 ?  29  LYS   B C    1 
ATOM   4620 O  O    . LYS   B 1 29  ? 51.912 -19.536 -18.023 1.00 23.57 ?  29  LYS   B O    1 
ATOM   4621 C  CB   . LYS   B 1 29  ? 52.997 -22.415 -16.869 1.00 27.21 ?  29  LYS   B CB   1 
ATOM   4622 C  CG   . LYS   B 1 29  ? 52.978 -22.703 -18.364 1.00 31.42 ?  29  LYS   B CG   1 
ATOM   4623 C  CD   . LYS   B 1 29  ? 53.210 -24.181 -18.656 1.00 34.75 ?  29  LYS   B CD   1 
ATOM   4624 C  CE   . LYS   B 1 29  ? 52.054 -25.040 -18.173 1.00 36.70 ?  29  LYS   B CE   1 
ATOM   4625 N  NZ   . LYS   B 1 29  ? 52.298 -26.489 -18.426 1.00 38.99 ?  29  LYS   B NZ   1 
ATOM   4626 H  H    . LYS   B 1 29  ? 53.132 -21.406 -14.605 1.00 23.77 ?  29  LYS   B H    1 
ATOM   4627 H  HA   . LYS   B 1 29  ? 53.910 -20.590 -17.033 1.00 27.29 ?  29  LYS   B HA   1 
ATOM   4628 H  HB2  . LYS   B 1 29  ? 53.739 -22.908 -16.483 1.00 32.63 ?  29  LYS   B HB2  1 
ATOM   4629 H  HB3  . LYS   B 1 29  ? 52.161 -22.733 -16.496 1.00 32.63 ?  29  LYS   B HB3  1 
ATOM   4630 H  HG2  . LYS   B 1 29  ? 52.113 -22.454 -18.726 1.00 37.68 ?  29  LYS   B HG2  1 
ATOM   4631 H  HG3  . LYS   B 1 29  ? 53.681 -22.193 -18.797 1.00 37.68 ?  29  LYS   B HG3  1 
ATOM   4632 H  HD2  . LYS   B 1 29  ? 53.303 -24.307 -19.613 1.00 41.68 ?  29  LYS   B HD2  1 
ATOM   4633 H  HD3  . LYS   B 1 29  ? 54.016 -24.474 -18.201 1.00 41.68 ?  29  LYS   B HD3  1 
ATOM   4634 H  HE2  . LYS   B 1 29  ? 51.938 -24.916 -17.219 1.00 44.02 ?  29  LYS   B HE2  1 
ATOM   4635 H  HE3  . LYS   B 1 29  ? 51.247 -24.782 -18.646 1.00 44.02 ?  29  LYS   B HE3  1 
ATOM   4636 H  HZ1  . LYS   B 1 29  ? 51.607 -26.969 -18.135 1.00 46.76 ?  29  LYS   B HZ1  1 
ATOM   4637 H  HZ2  . LYS   B 1 29  ? 52.403 -26.632 -19.298 1.00 46.76 ?  29  LYS   B HZ2  1 
ATOM   4638 H  HZ3  . LYS   B 1 29  ? 53.033 -26.752 -17.999 1.00 46.76 ?  29  LYS   B HZ3  1 
ATOM   4639 N  N    . VAL   B 1 30  ? 50.850 -20.210 -16.149 1.00 20.13 ?  30  VAL   B N    1 
ATOM   4640 C  CA   . VAL   B 1 30  ? 49.560 -19.617 -16.510 1.00 20.25 ?  30  VAL   B CA   1 
ATOM   4641 C  C    . VAL   B 1 30  ? 49.574 -18.106 -16.361 1.00 19.52 ?  30  VAL   B C    1 
ATOM   4642 O  O    . VAL   B 1 30  ? 48.833 -17.395 -17.057 1.00 20.58 ?  30  VAL   B O    1 
ATOM   4643 C  CB   . VAL   B 1 30  ? 48.461 -20.225 -15.614 1.00 21.15 ?  30  VAL   B CB   1 
ATOM   4644 C  CG1  . VAL   B 1 30  ? 47.174 -19.410 -15.687 1.00 21.20 ?  30  VAL   B CG1  1 
ATOM   4645 C  CG2  . VAL   B 1 30  ? 48.211 -21.678 -15.987 1.00 21.82 ?  30  VAL   B CG2  1 
ATOM   4646 H  H    . VAL   B 1 30  ? 50.843 -20.607 -15.374 1.00 24.13 ?  30  VAL   B H    1 
ATOM   4647 H  HA   . VAL   B 1 30  ? 49.352 -19.849 -17.430 1.00 24.28 ?  30  VAL   B HA   1 
ATOM   4648 H  HB   . VAL   B 1 30  ? 48.762 -20.217 -14.691 1.00 25.36 ?  30  VAL   B HB   1 
ATOM   4649 H  HG11 . VAL   B 1 30  ? 46.431 -19.983 -15.439 1.00 25.42 ?  30  VAL   B HG11 1 
ATOM   4650 H  HG12 . VAL   B 1 30  ? 47.232 -18.666 -15.070 1.00 25.42 ?  30  VAL   B HG12 1 
ATOM   4651 H  HG13 . VAL   B 1 30  ? 47.048 -19.096 -16.592 1.00 25.42 ?  30  VAL   B HG13 1 
ATOM   4652 H  HG21 . VAL   B 1 30  ? 47.522 -22.046 -15.403 1.00 26.17 ?  30  VAL   B HG21 1 
ATOM   4653 H  HG22 . VAL   B 1 30  ? 47.909 -21.721 -16.910 1.00 26.17 ?  30  VAL   B HG22 1 
ATOM   4654 H  HG23 . VAL   B 1 30  ? 49.031 -22.180 -15.882 1.00 26.17 ?  30  VAL   B HG23 1 
ATOM   4655 N  N    . LYS   B 1 31  ? 50.365 -17.606 -15.422 1.00 19.54 ?  31  LYS   B N    1 
ATOM   4656 C  CA   . LYS   B 1 31  ? 50.379 -16.195 -15.061 1.00 19.81 ?  31  LYS   B CA   1 
ATOM   4657 C  C    . LYS   B 1 31  ? 48.981 -15.700 -14.678 1.00 17.66 ?  31  LYS   B C    1 
ATOM   4658 O  O    . LYS   B 1 31  ? 48.449 -14.776 -15.304 1.00 18.53 ?  31  LYS   B O    1 
ATOM   4659 C  CB   . LYS   B 1 31  ? 51.000 -15.355 -16.169 1.00 22.77 ?  31  LYS   B CB   1 
ATOM   4660 C  CG   . LYS   B 1 31  ? 52.429 -15.812 -16.511 1.00 26.00 ?  31  LYS   B CG   1 
ATOM   4661 C  CD   . LYS   B 1 31  ? 53.003 -15.058 -17.692 1.00 28.75 ?  31  LYS   B CD   1 
ATOM   4662 C  CE   . LYS   B 1 31  ? 54.482 -15.342 -17.854 1.00 31.69 ?  31  LYS   B CE   1 
ATOM   4663 N  NZ   . LYS   B 1 31  ? 55.243 -14.922 -16.646 1.00 35.18 ?  31  LYS   B NZ   1 
ATOM   4664 H  H    . LYS   B 1 31  ? 50.916 -18.088 -14.974 1.00 23.42 ?  31  LYS   B H    1 
ATOM   4665 H  HA   . LYS   B 1 31  ? 50.933 -16.103 -14.286 1.00 23.75 ?  31  LYS   B HA   1 
ATOM   4666 H  HB2  . LYS   B 1 31  ? 50.463 -15.430 -16.973 1.00 27.30 ?  31  LYS   B HB2  1 
ATOM   4667 H  HB3  . LYS   B 1 31  ? 51.043 -14.436 -15.875 1.00 27.30 ?  31  LYS   B HB3  1 
ATOM   4668 H  HG2  . LYS   B 1 31  ? 53.000 -15.662 -15.740 1.00 31.18 ?  31  LYS   B HG2  1 
ATOM   4669 H  HG3  . LYS   B 1 31  ? 52.419 -16.760 -16.733 1.00 31.18 ?  31  LYS   B HG3  1 
ATOM   4670 H  HD2  . LYS   B 1 31  ? 52.545 -15.339 -18.499 1.00 34.48 ?  31  LYS   B HD2  1 
ATOM   4671 H  HD3  . LYS   B 1 31  ? 52.886 -14.108 -17.547 1.00 34.48 ?  31  LYS   B HD3  1 
ATOM   4672 H  HE2  . LYS   B 1 31  ? 54.616 -16.295 -17.983 1.00 38.01 ?  31  LYS   B HE2  1 
ATOM   4673 H  HE3  . LYS   B 1 31  ? 54.821 -14.848 -18.616 1.00 38.01 ?  31  LYS   B HE3  1 
ATOM   4674 H  HZ1  . LYS   B 1 31  ? 56.116 -14.958 -16.810 1.00 42.19 ?  31  LYS   B HZ1  1 
ATOM   4675 H  HZ2  . LYS   B 1 31  ? 55.023 -14.088 -16.425 1.00 42.19 ?  31  LYS   B HZ2  1 
ATOM   4676 H  HZ3  . LYS   B 1 31  ? 55.054 -15.461 -15.964 1.00 42.19 ?  31  LYS   B HZ3  1 
ATOM   4677 N  N    . PRO   B 1 32  ? 48.366 -16.292 -13.648 1.00 15.46 ?  32  PRO   B N    1 
ATOM   4678 C  CA   . PRO   B 1 32  ? 46.986 -15.935 -13.291 1.00 14.25 ?  32  PRO   B CA   1 
ATOM   4679 C  C    . PRO   B 1 32  ? 46.906 -14.590 -12.587 1.00 14.36 ?  32  PRO   B C    1 
ATOM   4680 O  O    . PRO   B 1 32  ? 47.826 -14.168 -11.883 1.00 15.83 ?  32  PRO   B O    1 
ATOM   4681 C  CB   . PRO   B 1 32  ? 46.591 -17.054 -12.319 1.00 14.03 ?  32  PRO   B CB   1 
ATOM   4682 C  CG   . PRO   B 1 32  ? 47.896 -17.408 -11.651 1.00 14.46 ?  32  PRO   B CG   1 
ATOM   4683 C  CD   . PRO   B 1 32  ? 48.942 -17.285 -12.716 1.00 15.53 ?  32  PRO   B CD   1 
ATOM   4684 H  HA   . PRO   B 1 32  ? 46.407 -15.946 -14.071 1.00 17.07 ?  32  PRO   B HA   1 
ATOM   4685 H  HB2  . PRO   B 1 32  ? 45.947 -16.721 -11.671 1.00 16.82 ?  32  PRO   B HB2  1 
ATOM   4686 H  HB3  . PRO   B 1 32  ? 46.234 -17.812 -12.807 1.00 16.82 ?  32  PRO   B HB3  1 
ATOM   4687 H  HG2  . PRO   B 1 32  ? 48.074 -16.784 -10.926 1.00 17.33 ?  32  PRO   B HG2  1 
ATOM   4688 H  HG3  . PRO   B 1 32  ? 47.860 -18.317 -11.313 1.00 17.33 ?  32  PRO   B HG3  1 
ATOM   4689 H  HD2  . PRO   B 1 32  ? 49.771 -16.951 -12.338 1.00 18.61 ?  32  PRO   B HD2  1 
ATOM   4690 H  HD3  . PRO   B 1 32  ? 49.069 -18.134 -13.161 1.00 18.61 ?  32  PRO   B HD3  1 
ATOM   4691 N  N    . THR   B 1 33  ? 45.761 -13.926 -12.765 1.00 13.66 ?  33  THR   B N    1 
ATOM   4692 C  CA   . THR   B 1 33  ? 45.465 -12.750 -11.954 1.00 14.25 ?  33  THR   B CA   1 
ATOM   4693 C  C    . THR   B 1 33  ? 45.419 -13.105 -10.473 1.00 13.52 ?  33  THR   B C    1 
ATOM   4694 O  O    . THR   B 1 33  ? 45.888 -12.328 -9.628  1.00 14.41 ?  33  THR   B O    1 
ATOM   4695 C  CB   . THR   B 1 33  ? 44.145 -12.118 -12.403 1.00 14.79 ?  33  THR   B CB   1 
ATOM   4696 O  OG1  . THR   B 1 33  ? 44.194 -11.851 -13.808 1.00 14.71 ?  33  THR   B OG1  1 
ATOM   4697 C  CG2  . THR   B 1 33  ? 43.880 -10.825 -11.650 1.00 15.90 ?  33  THR   B CG2  1 
ATOM   4698 H  H    . THR   B 1 33  ? 45.150 -14.135 -13.337 1.00 16.38 ?  33  THR   B H    1 
ATOM   4699 H  HA   . THR   B 1 33  ? 46.164 -12.097 -12.082 1.00 17.07 ?  33  THR   B HA   1 
ATOM   4700 H  HB   . THR   B 1 33  ? 43.413 -12.734 -12.218 1.00 17.73 ?  33  THR   B HB   1 
ATOM   4701 H  HG1  . THR   B 1 33  ? 43.471 -11.496 -14.061 1.00 17.63 ?  33  THR   B HG1  1 
ATOM   4702 H  HG21 . THR   B 1 33  ? 43.125 -10.364 -12.040 1.00 19.06 ?  33  THR   B HG21 1 
ATOM   4703 H  HG22 . THR   B 1 33  ? 43.689 -11.016 -10.718 1.00 19.06 ?  33  THR   B HG22 1 
ATOM   4704 H  HG23 . THR   B 1 33  ? 44.663 -10.252 -11.701 1.00 19.06 ?  33  THR   B HG23 1 
ATOM   4705 N  N    . VAL   B 1 34  ? 44.861 -14.273 -10.138 1.00 12.75 ?  34  VAL   B N    1 
ATOM   4706 C  CA   . VAL   B 1 34  ? 44.669 -14.678 -8.747  1.00 12.40 ?  34  VAL   B CA   1 
ATOM   4707 C  C    . VAL   B 1 34  ? 45.096 -16.130 -8.581  1.00 11.47 ?  34  VAL   B C    1 
ATOM   4708 O  O    . VAL   B 1 34  ? 44.574 -17.021 -9.265  1.00 12.05 ?  34  VAL   B O    1 
ATOM   4709 C  CB   . VAL   B 1 34  ? 43.197 -14.535 -8.299  1.00 13.33 ?  34  VAL   B CB   1 
ATOM   4710 C  CG1  . VAL   B 1 34  ? 43.031 -14.991 -6.855  1.00 13.84 ?  34  VAL   B CG1  1 
ATOM   4711 C  CG2  . VAL   B 1 34  ? 42.690 -13.109 -8.483  1.00 14.33 ?  34  VAL   B CG2  1 
ATOM   4712 H  H    . VAL   B 1 34  ? 44.585 -14.859 -10.706 1.00 15.27 ?  34  VAL   B H    1 
ATOM   4713 H  HA   . VAL   B 1 34  ? 45.220 -14.132 -8.168  1.00 14.86 ?  34  VAL   B HA   1 
ATOM   4714 H  HB   . VAL   B 1 34  ? 42.647 -15.113 -8.851  1.00 15.98 ?  34  VAL   B HB   1 
ATOM   4715 H  HG11 . VAL   B 1 34  ? 42.172 -14.682 -6.520  1.00 16.59 ?  34  VAL   B HG11 1 
ATOM   4716 H  HG12 . VAL   B 1 34  ? 43.062 -15.963 -6.819  1.00 16.59 ?  34  VAL   B HG12 1 
ATOM   4717 H  HG13 . VAL   B 1 34  ? 43.746 -14.618 -6.318  1.00 16.59 ?  34  VAL   B HG13 1 
ATOM   4718 H  HG21 . VAL   B 1 34  ? 41.771 -13.056 -8.173  1.00 17.18 ?  34  VAL   B HG21 1 
ATOM   4719 H  HG22 . VAL   B 1 34  ? 43.248 -12.505 -7.971  1.00 17.18 ?  34  VAL   B HG22 1 
ATOM   4720 H  HG23 . VAL   B 1 34  ? 42.731 -12.878 -9.426  1.00 17.18 ?  34  VAL   B HG23 1 
ATOM   4721 N  N    . VAL   B 1 35  ? 46.004 -16.376 -7.638  1.00 11.01 ?  35  VAL   B N    1 
ATOM   4722 C  CA   . VAL   B 1 35  ? 46.236 -17.719 -7.114  1.00 10.74 ?  35  VAL   B CA   1 
ATOM   4723 C  C    . VAL   B 1 35  ? 45.702 -17.773 -5.693  1.00 10.48 ?  35  VAL   B C    1 
ATOM   4724 O  O    . VAL   B 1 35  ? 45.918 -16.846 -4.904  1.00 10.95 ?  35  VAL   B O    1 
ATOM   4725 C  CB   . VAL   B 1 35  ? 47.717 -18.144 -7.198  1.00 11.50 ?  35  VAL   B CB   1 
ATOM   4726 C  CG1  . VAL   B 1 35  ? 48.627 -17.283 -6.293  1.00 12.34 ?  35  VAL   B CG1  1 
ATOM   4727 C  CG2  . VAL   B 1 35  ? 47.856 -19.641 -6.868  1.00 12.26 ?  35  VAL   B CG2  1 
ATOM   4728 H  H    . VAL   B 1 35  ? 46.505 -15.771 -7.278  1.00 13.19 ?  35  VAL   B H    1 
ATOM   4729 H  HA   . VAL   B 1 35  ? 45.719 -18.346 -7.639  1.00 12.87 ?  35  VAL   B HA   1 
ATOM   4730 H  HB   . VAL   B 1 35  ? 48.016 -18.026 -8.114  1.00 13.78 ?  35  VAL   B HB   1 
ATOM   4731 H  HG11 . VAL   B 1 35  ? 49.548 -17.518 -6.463  1.00 14.79 ?  35  VAL   B HG11 1 
ATOM   4732 H  HG12 . VAL   B 1 35  ? 48.471 -16.351 -6.493  1.00 14.79 ?  35  VAL   B HG12 1 
ATOM   4733 H  HG13 . VAL   B 1 35  ? 48.401 -17.466 -5.364  1.00 14.79 ?  35  VAL   B HG13 1 
ATOM   4734 H  HG21 . VAL   B 1 35  ? 48.775 -19.914 -6.982  1.00 14.69 ?  35  VAL   B HG21 1 
ATOM   4735 H  HG22 . VAL   B 1 35  ? 47.575 -19.794 -5.948  1.00 14.69 ?  35  VAL   B HG22 1 
ATOM   4736 H  HG23 . VAL   B 1 35  ? 47.282 -20.157 -7.467  1.00 14.69 ?  35  VAL   B HG23 1 
ATOM   4737 N  N    . VAL   B 1 36  ? 44.975 -18.850 -5.377  1.00 10.32 ?  36  VAL   B N    1 
ATOM   4738 C  CA   . VAL   B 1 36  ? 44.435 -19.059 -4.044  1.00 10.05 ?  36  VAL   B CA   1 
ATOM   4739 C  C    . VAL   B 1 36  ? 45.448 -19.815 -3.192  1.00 10.03 ?  36  VAL   B C    1 
ATOM   4740 O  O    . VAL   B 1 36  ? 45.987 -20.850 -3.612  1.00 11.20 ?  36  VAL   B O    1 
ATOM   4741 C  CB   . VAL   B 1 36  ? 43.106 -19.825 -4.121  1.00 10.67 ?  36  VAL   B CB   1 
ATOM   4742 C  CG1  . VAL   B 1 36  ? 42.612 -20.184 -2.733  1.00 11.41 ?  36  VAL   B CG1  1 
ATOM   4743 C  CG2  . VAL   B 1 36  ? 42.073 -18.992 -4.869  1.00 11.46 ?  36  VAL   B CG2  1 
ATOM   4744 H  H    . VAL   B 1 36  ? 44.786 -19.479 -5.929  1.00 12.37 ?  36  VAL   B H    1 
ATOM   4745 H  HA   . VAL   B 1 36  ? 44.263 -18.200 -3.625  1.00 12.04 ?  36  VAL   B HA   1 
ATOM   4746 H  HB   . VAL   B 1 36  ? 43.244 -20.650 -4.616  1.00 12.78 ?  36  VAL   B HB   1 
ATOM   4747 H  HG11 . VAL   B 1 36  ? 41.670 -20.411 -2.786  1.00 13.67 ?  36  VAL   B HG11 1 
ATOM   4748 H  HG12 . VAL   B 1 36  ? 43.117 -20.938 -2.399  1.00 13.67 ?  36  VAL   B HG12 1 
ATOM   4749 H  HG13 . VAL   B 1 36  ? 42.731 -19.415 -2.151  1.00 13.67 ?  36  VAL   B HG13 1 
ATOM   4750 H  HG21 . VAL   B 1 36  ? 41.230 -19.476 -4.888  1.00 13.73 ?  36  VAL   B HG21 1 
ATOM   4751 H  HG22 . VAL   B 1 36  ? 41.957 -18.147 -4.410  1.00 13.73 ?  36  VAL   B HG22 1 
ATOM   4752 H  HG23 . VAL   B 1 36  ? 42.383 -18.838 -5.775  1.00 13.73 ?  36  VAL   B HG23 1 
ATOM   4753 N  N    . ASN   B 1 37  ? 45.667 -19.325 -1.975  1.00 10.30 ?  37  ASN   B N    1 
ATOM   4754 C  CA   . ASN   B 1 37  ? 46.420 -20.049 -0.964  1.00 10.48 ?  37  ASN   B CA   1 
ATOM   4755 C  C    . ASN   B 1 37  ? 45.469 -20.723 0.018   1.00 10.72 ?  37  ASN   B C    1 
ATOM   4756 O  O    . ASN   B 1 37  ? 44.455 -20.147 0.424   1.00 11.25 ?  37  ASN   B O    1 
ATOM   4757 C  CB   . ASN   B 1 37  ? 47.346 -19.103 -0.203  1.00 10.62 ?  37  ASN   B CB   1 
ATOM   4758 C  CG   . ASN   B 1 37  ? 48.200 -19.820 0.799   1.00 11.22 ?  37  ASN   B CG   1 
ATOM   4759 O  OD1  . ASN   B 1 37  ? 48.536 -20.998 0.617   1.00 11.73 ?  37  ASN   B OD1  1 
ATOM   4760 N  ND2  . ASN   B 1 37  ? 48.554 -19.125 1.876   1.00 11.04 ?  37  ASN   B ND2  1 
ATOM   4761 H  H    . ASN   B 1 37  ? 45.376 -18.559 -1.701  1.00 12.34 ?  37  ASN   B H    1 
ATOM   4762 H  HA   . ASN   B 1 37  ? 46.953 -20.740 -1.385  1.00 12.56 ?  37  ASN   B HA   1 
ATOM   4763 H  HB2  . ASN   B 1 37  ? 47.933 -18.667 -0.837  1.00 12.73 ?  37  ASN   B HB2  1 
ATOM   4764 H  HB3  . ASN   B 1 37  ? 46.814 -18.447 0.270   1.00 12.73 ?  37  ASN   B HB3  1 
ATOM   4765 H  HD21 . ASN   B 1 37  ? 49.055 -19.486 2.479   1.00 13.22 ?  37  ASN   B HD21 1 
ATOM   4766 H  HD22 . ASN   B 1 37  ? 48.310 -18.310 1.966   1.00 13.22 ?  37  ASN   B HD22 1 
ATOM   4767 N  N    . ALA   B 1 38  ? 45.820 -21.955 0.399   1.00 10.96 ?  38  ALA   B N    1 
ATOM   4768 C  CA   . ALA   B 1 38  ? 45.166 -22.699 1.476   1.00 11.35 ?  38  ALA   B CA   1 
ATOM   4769 C  C    . ALA   B 1 38  ? 45.753 -22.210 2.797   1.00 11.47 ?  38  ALA   B C    1 
ATOM   4770 O  O    . ALA   B 1 38  ? 46.656 -22.819 3.384   1.00 12.10 ?  38  ALA   B O    1 
ATOM   4771 C  CB   . ALA   B 1 38  ? 45.397 -24.192 1.288   1.00 12.67 ?  38  ALA   B CB   1 
ATOM   4772 H  H    . ALA   B 1 38  ? 46.471 -22.391 0.046   1.00 13.14 ?  38  ALA   B H    1 
ATOM   4773 H  HA   . ALA   B 1 38  ? 44.213 -22.524 1.474   1.00 13.60 ?  38  ALA   B HA   1 
ATOM   4774 H  HB1  . ALA   B 1 38  ? 44.951 -24.676 2.010   1.00 15.18 ?  38  ALA   B HB1  1 
ATOM   4775 H  HB2  . ALA   B 1 38  ? 45.023 -24.467 0.437   1.00 15.18 ?  38  ALA   B HB2  1 
ATOM   4776 H  HB3  . ALA   B 1 38  ? 46.346 -24.376 1.311   1.00 15.18 ?  38  ALA   B HB3  1 
ATOM   4777 N  N    . ALA   B 1 39  ? 45.232 -21.072 3.257   1.00 11.11 ?  39  ALA   B N    1 
ATOM   4778 C  CA   . ALA   B 1 39  ? 45.775 -20.337 4.388   1.00 11.55 ?  39  ALA   B CA   1 
ATOM   4779 C  C    . ALA   B 1 39  ? 45.162 -20.777 5.714   1.00 11.28 ?  39  ALA   B C    1 
ATOM   4780 O  O    . ALA   B 1 39  ? 44.136 -21.454 5.765   1.00 12.36 ?  39  ALA   B O    1 
ATOM   4781 C  CB   . ALA   B 1 39  ? 45.529 -18.838 4.197   1.00 11.99 ?  39  ALA   B CB   1 
ATOM   4782 H  H    . ALA   B 1 39  ? 44.543 -20.699 2.912   1.00 13.31 ?  39  ALA   B H    1 
ATOM   4783 H  HA   . ALA   B 1 39  ? 46.729 -20.480 4.438   1.00 13.84 ?  39  ALA   B HA   1 
ATOM   4784 H  HB1  . ALA   B 1 39  ? 45.891 -18.356 4.958   1.00 14.37 ?  39  ALA   B HB1  1 
ATOM   4785 H  HB2  . ALA   B 1 39  ? 45.967 -18.546 3.383   1.00 14.37 ?  39  ALA   B HB2  1 
ATOM   4786 H  HB3  . ALA   B 1 39  ? 44.572 -18.677 4.132   1.00 14.37 ?  39  ALA   B HB3  1 
ATOM   4787 N  N    . ASN   B 1 40  ? 45.801 -20.350 6.799   1.00 11.94 ?  40  ASN   B N    1 
ATOM   4788 C  CA   . ASN   B 1 40  ? 45.247 -20.403 8.142   1.00 13.02 ?  40  ASN   B CA   1 
ATOM   4789 C  C    . ASN   B 1 40  ? 45.064 -18.976 8.668   1.00 12.79 ?  40  ASN   B C    1 
ATOM   4790 O  O    . ASN   B 1 40  ? 45.469 -17.994 8.035   1.00 12.40 ?  40  ASN   B O    1 
ATOM   4791 C  CB   . ASN   B 1 40  ? 46.103 -21.277 9.078   1.00 13.76 ?  40  ASN   B CB   1 
ATOM   4792 C  CG   . ASN   B 1 40  ? 47.561 -20.873 9.096   1.00 14.81 ?  40  ASN   B CG   1 
ATOM   4793 O  OD1  . ASN   B 1 40  ? 47.879 -19.690 9.147   1.00 16.86 ?  40  ASN   B OD1  1 
ATOM   4794 N  ND2  . ASN   B 1 40  ? 48.458 -21.852 9.065   1.00 15.28 ?  40  ASN   B ND2  1 
ATOM   4795 H  H    . ASN   B 1 40  ? 46.591 -20.012 6.775   1.00 14.30 ?  40  ASN   B H    1 
ATOM   4796 H  HA   . ASN   B 1 40  ? 44.366 -20.798 8.101   1.00 15.60 ?  40  ASN   B HA   1 
ATOM   4797 H  HB2  . ASN   B 1 40  ? 45.759 -21.199 9.981   1.00 16.49 ?  40  ASN   B HB2  1 
ATOM   4798 H  HB3  . ASN   B 1 40  ? 46.050 -22.194 8.777   1.00 16.49 ?  40  ASN   B HB3  1 
ATOM   4799 H  HD21 . ASN   B 1 40  ? 49.300 -21.670 9.080   1.00 18.31 ?  40  ASN   B HD21 1 
ATOM   4800 H  HD22 . ASN   B 1 40  ? 48.199 -22.672 9.034   1.00 18.31 ?  40  ASN   B HD22 1 
ATOM   4801 N  N    . VAL   B 1 41  ? 44.413 -18.852 9.827   1.00 13.24 ?  41  VAL   B N    1 
ATOM   4802 C  CA   . VAL   B 1 41  ? 43.951 -17.535 10.275  1.00 13.84 ?  41  VAL   B CA   1 
ATOM   4803 C  C    . VAL   B 1 41  ? 45.101 -16.578 10.566  1.00 13.49 ?  41  VAL   B C    1 
ATOM   4804 O  O    . VAL   B 1 41  ? 44.926 -15.358 10.467  1.00 13.91 ?  41  VAL   B O    1 
ATOM   4805 C  CB   . VAL   B 1 41  ? 42.973 -17.620 11.467  1.00 15.35 ?  41  VAL   B CB   1 
ATOM   4806 C  CG1  . VAL   B 1 41  ? 41.672 -18.305 11.059  1.00 15.92 ?  41  VAL   B CG1  1 
ATOM   4807 C  CG2  . VAL   B 1 41  ? 43.626 -18.309 12.652  1.00 16.52 ?  41  VAL   B CG2  1 
ATOM   4808 H  H    . VAL   B 1 41  ? 44.229 -19.496 10.357  1.00 15.86 ?  41  VAL   B H    1 
ATOM   4809 H  HA   . VAL   B 1 41  ? 43.451 -17.137 9.547   1.00 16.59 ?  41  VAL   B HA   1 
ATOM   4810 H  HB   . VAL   B 1 41  ? 42.748 -16.717 11.746  1.00 18.40 ?  41  VAL   B HB   1 
ATOM   4811 H  HG11 . VAL   B 1 41  ? 41.069 -18.315 11.818  1.00 19.08 ?  41  VAL   B HG11 1 
ATOM   4812 H  HG12 . VAL   B 1 41  ? 41.273 -17.813 10.325  1.00 19.08 ?  41  VAL   B HG12 1 
ATOM   4813 H  HG13 . VAL   B 1 41  ? 41.869 -19.213 10.781  1.00 19.08 ?  41  VAL   B HG13 1 
ATOM   4814 H  HG21 . VAL   B 1 41  ? 42.995 -18.337 13.385  1.00 19.80 ?  41  VAL   B HG21 1 
ATOM   4815 H  HG22 . VAL   B 1 41  ? 43.874 -19.211 12.393  1.00 19.80 ?  41  VAL   B HG22 1 
ATOM   4816 H  HG23 . VAL   B 1 41  ? 44.416 -17.810 12.910  1.00 19.80 ?  41  VAL   B HG23 1 
ATOM   4817 N  N    . TYR   B 1 42  ? 46.270 -17.091 10.947  1.00 13.68 ?  42  TYR   B N    1 
ATOM   4818 C  CA   . TYR   B 1 42  ? 47.427 -16.242 11.210  1.00 14.01 ?  42  TYR   B CA   1 
ATOM   4819 C  C    . TYR   B 1 42  ? 48.394 -16.173 10.030  1.00 13.46 ?  42  TYR   B C    1 
ATOM   4820 O  O    . TYR   B 1 42  ? 49.488 -15.609 10.164  1.00 14.63 ?  42  TYR   B O    1 
ATOM   4821 C  CB   . TYR   B 1 42  ? 48.123 -16.647 12.515  1.00 15.83 ?  42  TYR   B CB   1 
ATOM   4822 C  CG   . TYR   B 1 42  ? 47.521 -15.967 13.741  1.00 16.18 ?  42  TYR   B CG   1 
ATOM   4823 C  CD1  . TYR   B 1 42  ? 47.738 -14.611 13.978  1.00 16.18 ?  42  TYR   B CD1  1 
ATOM   4824 C  CD2  . TYR   B 1 42  ? 46.737 -16.665 14.647  1.00 18.23 ?  42  TYR   B CD2  1 
ATOM   4825 C  CE1  . TYR   B 1 42  ? 47.195 -13.976 15.076  1.00 16.59 ?  42  TYR   B CE1  1 
ATOM   4826 C  CE2  . TYR   B 1 42  ? 46.196 -16.037 15.757  1.00 18.48 ?  42  TYR   B CE2  1 
ATOM   4827 C  CZ   . TYR   B 1 42  ? 46.425 -14.687 15.966  1.00 18.71 ?  42  TYR   B CZ   1 
ATOM   4828 O  OH   . TYR   B 1 42  ? 45.895 -14.041 17.066  1.00 21.80 ?  42  TYR   B OH   1 
ATOM   4829 H  H    . TYR   B 1 42  ? 46.420 -17.937 11.048  1.00 16.39 ?  42  TYR   B H    1 
ATOM   4830 H  HA   . TYR   B 1 42  ? 47.099 -15.344 11.341  1.00 16.79 ?  42  TYR   B HA   1 
ATOM   4831 H  HB2  . TYR   B 1 42  ? 48.045 -17.603 12.635  1.00 18.97 ?  42  TYR   B HB2  1 
ATOM   4832 H  HB3  . TYR   B 1 42  ? 49.060 -16.393 12.461  1.00 18.97 ?  42  TYR   B HB3  1 
ATOM   4833 H  HD1  . TYR   B 1 42  ? 48.261 -14.121 13.374  1.00 19.40 ?  42  TYR   B HD1  1 
ATOM   4834 H  HD2  . TYR   B 1 42  ? 46.579 -17.571 14.505  1.00 21.86 ?  42  TYR   B HD2  1 
ATOM   4835 H  HE1  . TYR   B 1 42  ? 47.356 -13.069 15.215  1.00 19.89 ?  42  TYR   B HE1  1 
ATOM   4836 H  HE2  . TYR   B 1 42  ? 45.670 -16.519 16.353  1.00 22.16 ?  42  TYR   B HE2  1 
ATOM   4837 H  HH   . TYR   B 1 42  ? 46.122 -13.235 17.053  1.00 26.14 ?  42  TYR   B HH   1 
ATOM   4838 N  N    . LEU   B 1 43  ? 47.996 -16.691 8.869   1.00 12.40 ?  43  LEU   B N    1 
ATOM   4839 C  CA   . LEU   B 1 43  ? 48.809 -16.621 7.659   1.00 12.31 ?  43  LEU   B CA   1 
ATOM   4840 C  C    . LEU   B 1 43  ? 50.223 -17.129 7.917   1.00 12.24 ?  43  LEU   B C    1 
ATOM   4841 O  O    . LEU   B 1 43  ? 51.204 -16.538 7.464   1.00 13.12 ?  43  LEU   B O    1 
ATOM   4842 C  CB   . LEU   B 1 43  ? 48.827 -15.215 7.053   1.00 12.70 ?  43  LEU   B CB   1 
ATOM   4843 C  CG   . LEU   B 1 43  ? 47.476 -14.593 6.682   1.00 12.94 ?  43  LEU   B CG   1 
ATOM   4844 C  CD1  . LEU   B 1 43  ? 47.698 -13.195 6.082   1.00 14.13 ?  43  LEU   B CD1  1 
ATOM   4845 C  CD2  . LEU   B 1 43  ? 46.689 -15.481 5.727   1.00 12.76 ?  43  LEU   B CD2  1 
ATOM   4846 H  H    . LEU   B 1 43  ? 47.251 -17.106 8.755   1.00 14.85 ?  43  LEU   B H    1 
ATOM   4847 H  HA   . LEU   B 1 43  ? 48.409 -17.212 6.992   1.00 14.75 ?  43  LEU   B HA   1 
ATOM   4848 H  HB2  . LEU   B 1 43  ? 49.252 -14.622 7.688   1.00 15.22 ?  43  LEU   B HB2  1 
ATOM   4849 H  HB3  . LEU   B 1 43  ? 49.356 -15.247 6.239   1.00 15.22 ?  43  LEU   B HB3  1 
ATOM   4850 H  HG   . LEU   B 1 43  ? 46.951 -14.481 7.487   1.00 15.51 ?  43  LEU   B HG   1 
ATOM   4851 H  HD11 . LEU   B 1 43  ? 46.835 -12.810 5.852   1.00 16.94 ?  43  LEU   B HD11 1 
ATOM   4852 H  HD12 . LEU   B 1 43  ? 48.143 -12.636 6.737   1.00 16.94 ?  43  LEU   B HD12 1 
ATOM   4853 H  HD13 . LEU   B 1 43  ? 48.245 -13.275 5.285   1.00 16.94 ?  43  LEU   B HD13 1 
ATOM   4854 H  HD21 . LEU   B 1 43  ? 45.885 -15.012 5.446   1.00 15.29 ?  43  LEU   B HD21 1 
ATOM   4855 H  HD22 . LEU   B 1 43  ? 47.237 -15.685 4.954   1.00 15.29 ?  43  LEU   B HD22 1 
ATOM   4856 H  HD23 . LEU   B 1 43  ? 46.446 -16.300 6.187   1.00 15.29 ?  43  LEU   B HD23 1 
ATOM   4857 N  N    . LYS   B 1 44  ? 50.325 -18.251 8.637   1.00 12.71 ?  44  LYS   B N    1 
ATOM   4858 C  CA   . LYS   B 1 44  ? 51.591 -18.933 8.877   1.00 13.36 ?  44  LYS   B CA   1 
ATOM   4859 C  C    . LYS   B 1 44  ? 51.711 -20.050 7.848   1.00 13.13 ?  44  LYS   B C    1 
ATOM   4860 O  O    . LYS   B 1 44  ? 51.012 -21.065 7.931   1.00 14.30 ?  44  LYS   B O    1 
ATOM   4861 C  CB   . LYS   B 1 44  ? 51.645 -19.453 10.312  1.00 15.47 ?  44  LYS   B CB   1 
ATOM   4862 C  CG   . LYS   B 1 44  ? 51.828 -18.350 11.346  1.00 18.25 ?  44  LYS   B CG   1 
ATOM   4863 C  CD   . LYS   B 1 44  ? 53.014 -17.465 10.953  1.00 21.40 ?  44  LYS   B CD   1 
ATOM   4864 C  CE   . LYS   B 1 44  ? 53.558 -16.648 12.096  1.00 24.20 ?  44  LYS   B CE   1 
ATOM   4865 N  NZ   . LYS   B 1 44  ? 54.702 -15.798 11.683  1.00 25.32 ?  44  LYS   B NZ   1 
ATOM   4866 H  H    . LYS   B 1 44  ? 49.650 -18.639 9.004   1.00 15.24 ?  44  LYS   B H    1 
ATOM   4867 H  HA   . LYS   B 1 44  ? 52.322 -18.315 8.722   1.00 16.01 ?  44  LYS   B HA   1 
ATOM   4868 H  HB2  . LYS   B 1 44  ? 50.809 -19.910 10.512  1.00 18.54 ?  44  LYS   B HB2  1 
ATOM   4869 H  HB3  . LYS   B 1 44  ? 52.385 -20.069 10.397  1.00 18.54 ?  44  LYS   B HB3  1 
ATOM   4870 H  HG2  . LYS   B 1 44  ? 51.029 -17.806 11.388  1.00 21.88 ?  44  LYS   B HG2  1 
ATOM   4871 H  HG3  . LYS   B 1 44  ? 52.014 -18.751 12.214  1.00 21.88 ?  44  LYS   B HG3  1 
ATOM   4872 H  HD2  . LYS   B 1 44  ? 53.724 -18.035 10.609  1.00 25.66 ?  44  LYS   B HD2  1 
ATOM   4873 H  HD3  . LYS   B 1 44  ? 52.721 -16.851 10.261  1.00 25.66 ?  44  LYS   B HD3  1 
ATOM   4874 H  HE2  . LYS   B 1 44  ? 52.867 -16.047 12.382  1.00 29.02 ?  44  LYS   B HE2  1 
ATOM   4875 H  HE3  . LYS   B 1 44  ? 53.837 -17.236 12.820  1.00 29.02 ?  44  LYS   B HE3  1 
ATOM   4876 H  HZ1  . LYS   B 1 44  ? 54.997 -15.329 12.379  1.00 30.36 ?  44  LYS   B HZ1  1 
ATOM   4877 H  HZ2  . LYS   B 1 44  ? 55.364 -16.302 11.370  1.00 30.36 ?  44  LYS   B HZ2  1 
ATOM   4878 H  HZ3  . LYS   B 1 44  ? 54.443 -15.232 11.044  1.00 30.36 ?  44  LYS   B HZ3  1 
ATOM   4879 N  N    . HIS   B 1 45  ? 52.566 -19.833 6.850   1.00 12.65 ?  45  HIS   B N    1 
ATOM   4880 C  CA   . HIS   B 1 45  ? 52.590 -20.670 5.650   1.00 12.77 ?  45  HIS   B CA   1 
ATOM   4881 C  C    . HIS   B 1 45  ? 53.605 -21.795 5.814   1.00 14.72 ?  45  HIS   B C    1 
ATOM   4882 O  O    . HIS   B 1 45  ? 54.660 -21.823 5.191   1.00 17.24 ?  45  HIS   B O    1 
ATOM   4883 C  CB   . HIS   B 1 45  ? 52.897 -19.822 4.429   1.00 12.88 ?  45  HIS   B CB   1 
ATOM   4884 C  CG   . HIS   B 1 45  ? 52.028 -18.616 4.318   1.00 12.83 ?  45  HIS   B CG   1 
ATOM   4885 N  ND1  . HIS   B 1 45  ? 50.649 -18.689 4.287   1.00 12.76 ?  45  HIS   B ND1  1 
ATOM   4886 C  CD2  . HIS   B 1 45  ? 52.347 -17.301 4.247   1.00 13.65 ?  45  HIS   B CD2  1 
ATOM   4887 C  CE1  . HIS   B 1 45  ? 50.163 -17.464 4.188   1.00 12.36 ?  45  HIS   B CE1  1 
ATOM   4888 N  NE2  . HIS   B 1 45  ? 51.169 -16.605 4.158   1.00 12.94 ?  45  HIS   B NE2  1 
ATOM   4889 H  H    . HIS   B 1 45  ? 53.137 -19.190 6.836   1.00 15.16 ?  45  HIS   B H    1 
ATOM   4890 H  HA   . HIS   B 1 45  ? 51.707 -21.066 5.524   1.00 15.30 ?  45  HIS   B HA   1 
ATOM   4891 H  HB2  . HIS   B 1 45  ? 53.815 -19.525 4.474   1.00 15.44 ?  45  HIS   B HB2  1 
ATOM   4892 H  HB3  . HIS   B 1 45  ? 52.761 -20.361 3.630   1.00 15.44 ?  45  HIS   B HB3  1 
ATOM   4893 H  HD2  . HIS   B 1 45  ? 53.203 -16.939 4.255   1.00 16.36 ?  45  HIS   B HD2  1 
ATOM   4894 H  HE1  . HIS   B 1 45  ? 49.260 -17.242 4.138   1.00 14.82 ?  45  HIS   B HE1  1 
ATOM   4895 H  HE2  . HIS   B 1 45  ? 51.094 -15.750 4.109   1.00 15.51 ?  45  HIS   B HE2  1 
ATOM   4896 N  N    A GLY   B 1 46  ? 53.239 -22.757 6.656   0.70 15.85 ?  46  GLY   B N    1 
ATOM   4897 N  N    B GLY   B 1 46  ? 53.252 -22.739 6.678   0.30 15.82 ?  46  GLY   B N    1 
ATOM   4898 C  CA   A GLY   B 1 46  ? 54.159 -23.811 7.040   0.70 17.24 ?  46  GLY   B CA   1 
ATOM   4899 C  CA   B GLY   B 1 46  ? 54.164 -23.809 7.019   0.30 16.83 ?  46  GLY   B CA   1 
ATOM   4900 C  C    A GLY   B 1 46  ? 54.221 -25.028 6.138   0.70 18.82 ?  46  GLY   B C    1 
ATOM   4901 C  C    B GLY   B 1 46  ? 54.204 -24.940 6.011   0.30 17.82 ?  46  GLY   B C    1 
ATOM   4902 O  O    A GLY   B 1 46  ? 55.308 -25.470 5.753   0.70 22.19 ?  46  GLY   B O    1 
ATOM   4903 O  O    B GLY   B 1 46  ? 55.242 -25.200 5.393   0.30 18.58 ?  46  GLY   B O    1 
ATOM   4904 H  H    A GLY   B 1 46  ? 52.463 -22.805 7.033   0.70 19.00 ?  46  GLY   B H    1 
ATOM   4905 H  H    B GLY   B 1 46  ? 52.489 -22.773 7.082   0.30 18.96 ?  46  GLY   B H    1 
ATOM   4906 H  HA2  A GLY   B 1 46  ? 55.050 -23.433 7.098   0.70 20.67 ?  46  GLY   B HA2  1 
ATOM   4907 H  HA2  B GLY   B 1 46  ? 55.057 -23.442 7.101   0.30 20.17 ?  46  GLY   B HA2  1 
ATOM   4908 H  HA3  A GLY   B 1 46  ? 53.912 -24.128 7.921   0.70 20.67 ?  46  GLY   B HA3  1 
ATOM   4909 H  HA3  B GLY   B 1 46  ? 53.908 -24.170 7.884   0.30 20.17 ?  46  GLY   B HA3  1 
ATOM   4910 N  N    . GLY   B 1 47  ? 53.070 -25.610 5.816   1.00 18.36 ?  47  GLY   B N    1 
ATOM   4911 C  CA   . GLY   B 1 47  ? 53.027 -26.870 5.104   1.00 16.29 ?  47  GLY   B CA   1 
ATOM   4912 C  C    . GLY   B 1 47  ? 52.093 -26.855 3.911   1.00 14.27 ?  47  GLY   B C    1 
ATOM   4913 O  O    . GLY   B 1 47  ? 51.429 -25.860 3.626   1.00 14.31 ?  47  GLY   B O    1 
ATOM   4914 H  H    A GLY   B 1 47  ? 52.294 -25.303 6.027   0.70 22.01 ?  47  GLY   B H    1 
ATOM   4915 H  H    B GLY   B 1 47  ? 52.299 -25.341 6.089   0.30 22.01 ?  47  GLY   B H    1 
ATOM   4916 H  HA2  . GLY   B 1 47  ? 53.915 -27.098 4.786   1.00 19.53 ?  47  GLY   B HA2  1 
ATOM   4917 H  HA3  . GLY   B 1 47  ? 52.738 -27.569 5.712   1.00 19.53 ?  47  GLY   B HA3  1 
ATOM   4918 N  N    . GLY   B 1 48  ? 52.046 -27.998 3.228   1.00 13.78 ?  48  GLY   B N    1 
ATOM   4919 C  CA   . GLY   B 1 48  ? 51.119 -28.153 2.123   1.00 13.42 ?  48  GLY   B CA   1 
ATOM   4920 C  C    . GLY   B 1 48  ? 51.255 -27.046 1.101   1.00 12.29 ?  48  GLY   B C    1 
ATOM   4921 O  O    . GLY   B 1 48  ? 52.354 -26.581 0.786   1.00 13.21 ?  48  GLY   B O    1 
ATOM   4922 H  H    . GLY   B 1 48  ? 52.545 -28.680 3.378   1.00 16.52 ?  48  GLY   B H    1 
ATOM   4923 H  HA2  . GLY   B 1 48  ? 51.279 -29.006 1.683   1.00 16.09 ?  48  GLY   B HA2  1 
ATOM   4924 H  HA3  . GLY   B 1 48  ? 50.208 -28.153 2.461   1.00 16.09 ?  48  GLY   B HA3  1 
ATOM   4925 N  N    . VAL   B 1 49  ? 50.109 -26.615 0.572   1.00 12.52 ?  49  VAL   B N    1 
ATOM   4926 C  CA   . VAL   B 1 49  ? 50.087 -25.590 -0.469  1.00 12.57 ?  49  VAL   B CA   1 
ATOM   4927 C  C    . VAL   B 1 49  ? 50.746 -24.302 0.016   1.00 11.88 ?  49  VAL   B C    1 
ATOM   4928 O  O    . VAL   B 1 49  ? 51.536 -23.681 -0.707  1.00 12.66 ?  49  VAL   B O    1 
ATOM   4929 C  CB   . VAL   B 1 49  ? 48.641 -25.338 -0.937  1.00 14.15 ?  49  VAL   B CB   1 
ATOM   4930 C  CG1  . VAL   B 1 49  ? 48.562 -24.095 -1.825  1.00 14.10 ?  49  VAL   B CG1  1 
ATOM   4931 C  CG2  . VAL   B 1 49  ? 48.088 -26.560 -1.665  1.00 16.02 ?  49  VAL   B CG2  1 
ATOM   4932 H  H    . VAL   B 1 49  ? 49.323 -26.894 0.802   1.00 15.00 ?  49  VAL   B H    1 
ATOM   4933 H  HA   . VAL   B 1 49  ? 50.588 -25.908 -1.233  1.00 15.06 ?  49  VAL   B HA   1 
ATOM   4934 H  HB   . VAL   B 1 49  ? 48.081 -25.180 -0.162  1.00 16.96 ?  49  VAL   B HB   1 
ATOM   4935 H  HG11 . VAL   B 1 49  ? 47.726 -24.107 -2.319  1.00 16.90 ?  49  VAL   B HG11 1 
ATOM   4936 H  HG12 . VAL   B 1 49  ? 48.597 -23.299 -1.266  1.00 16.90 ?  49  VAL   B HG12 1 
ATOM   4937 H  HG13 . VAL   B 1 49  ? 49.308 -24.095 -2.444  1.00 16.90 ?  49  VAL   B HG13 1 
ATOM   4938 H  HG21 . VAL   B 1 49  ? 47.177 -26.374 -1.952  1.00 19.20 ?  49  VAL   B HG21 1 
ATOM   4939 H  HG22 . VAL   B 1 49  ? 48.642 -26.747 -2.439  1.00 19.20 ?  49  VAL   B HG22 1 
ATOM   4940 H  HG23 . VAL   B 1 49  ? 48.093 -27.317 -1.061  1.00 19.20 ?  49  VAL   B HG23 1 
ATOM   4941 N  N    . ALA   B 1 50  ? 50.398 -23.855 1.224   1.00 11.84 ?  50  ALA   B N    1 
ATOM   4942 C  CA   . ALA   B 1 50  ? 50.922 -22.580 1.702   1.00 11.74 ?  50  ALA   B CA   1 
ATOM   4943 C  C    . ALA   B 1 50  ? 52.442 -22.611 1.808   1.00 11.85 ?  50  ALA   B C    1 
ATOM   4944 O  O    . ALA   B 1 50  ? 53.121 -21.642 1.441   1.00 11.99 ?  50  ALA   B O    1 
ATOM   4945 C  CB   . ALA   B 1 50  ? 50.291 -22.217 3.044   1.00 12.32 ?  50  ALA   B CB   1 
ATOM   4946 H  H    . ALA   B 1 50  ? 49.874 -24.258 1.772   1.00 14.18 ?  50  ALA   B H    1 
ATOM   4947 H  HA   . ALA   B 1 50  ? 50.688 -21.884 1.071   1.00 14.07 ?  50  ALA   B HA   1 
ATOM   4948 H  HB1  . ALA   B 1 50  ? 50.648 -21.364 3.344   1.00 14.76 ?  50  ALA   B HB1  1 
ATOM   4949 H  HB2  . ALA   B 1 50  ? 49.328 -22.146 2.933   1.00 14.76 ?  50  ALA   B HB2  1 
ATOM   4950 H  HB3  . ALA   B 1 50  ? 50.498 -22.907 3.692   1.00 14.76 ?  50  ALA   B HB3  1 
ATOM   4951 N  N    . GLY   B 1 51  ? 52.993 -23.701 2.329   1.00 12.60 ?  51  GLY   B N    1 
ATOM   4952 C  CA   . GLY   B 1 51  ? 54.437 -23.805 2.399   1.00 12.78 ?  51  GLY   B CA   1 
ATOM   4953 C  C    . GLY   B 1 51  ? 55.083 -23.752 1.031   1.00 12.95 ?  51  GLY   B C    1 
ATOM   4954 O  O    . GLY   B 1 51  ? 56.126 -23.115 0.849   1.00 13.69 ?  51  GLY   B O    1 
ATOM   4955 H  H    . GLY   B 1 51  ? 52.566 -24.380 2.639   1.00 15.09 ?  51  GLY   B H    1 
ATOM   4956 H  HA2  . GLY   B 1 51  ? 54.792 -23.074 2.930   1.00 15.32 ?  51  GLY   B HA2  1 
ATOM   4957 H  HA3  . GLY   B 1 51  ? 54.685 -24.642 2.823   1.00 15.32 ?  51  GLY   B HA3  1 
ATOM   4958 N  N    . ALA   B 1 52  ? 54.478 -24.422 0.049   1.00 12.59 ?  52  ALA   B N    1 
ATOM   4959 C  CA   . ALA   B 1 52  ? 55.038 -24.433 -1.294  1.00 12.55 ?  52  ALA   B CA   1 
ATOM   4960 C  C    . ALA   B 1 52  ? 54.955 -23.056 -1.943  1.00 11.81 ?  52  ALA   B C    1 
ATOM   4961 O  O    . ALA   B 1 52  ? 55.919 -22.600 -2.579  1.00 12.90 ?  52  ALA   B O    1 
ATOM   4962 C  CB   . ALA   B 1 52  ? 54.323 -25.480 -2.147  1.00 13.46 ?  52  ALA   B CB   1 
ATOM   4963 H  H    . ALA   B 1 52  ? 53.746 -24.872 0.137   1.00 15.09 ?  52  ALA   B H    1 
ATOM   4964 H  HA   . ALA   B 1 52  ? 55.970 -24.680 -1.242  1.00 15.04 ?  52  ALA   B HA   1 
ATOM   4965 H  HB1  . ALA   B 1 52  ? 54.708 -25.476 -3.039  1.00 16.14 ?  52  ALA   B HB1  1 
ATOM   4966 H  HB2  . ALA   B 1 52  ? 54.445 -26.354 -1.741  1.00 16.14 ?  52  ALA   B HB2  1 
ATOM   4967 H  HB3  . ALA   B 1 52  ? 53.380 -25.266 -2.193  1.00 16.14 ?  52  ALA   B HB3  1 
ATOM   4968 N  N    . LEU   B 1 53  ? 53.809 -22.381 -1.821  1.00 11.69 ?  53  LEU   B N    1 
ATOM   4969 C  CA   . LEU   B 1 53  ? 53.700 -21.038 -2.390  1.00 12.09 ?  53  LEU   B CA   1 
ATOM   4970 C  C    . LEU   B 1 53  ? 54.706 -20.092 -1.746  1.00 12.13 ?  53  LEU   B C    1 
ATOM   4971 O  O    . LEU   B 1 53  ? 55.411 -19.346 -2.439  1.00 12.57 ?  53  LEU   B O    1 
ATOM   4972 C  CB   . LEU   B 1 53  ? 52.279 -20.491 -2.226  1.00 12.49 ?  53  LEU   B CB   1 
ATOM   4973 C  CG   . LEU   B 1 53  ? 51.144 -21.211 -2.961  1.00 12.58 ?  53  LEU   B CG   1 
ATOM   4974 C  CD1  . LEU   B 1 53  ? 49.806 -20.592 -2.616  1.00 14.48 ?  53  LEU   B CD1  1 
ATOM   4975 C  CD2  . LEU   B 1 53  ? 51.353 -21.210 -4.464  1.00 14.93 ?  53  LEU   B CD2  1 
ATOM   4976 H  H    . LEU   B 1 53  ? 53.100 -22.666 -1.425  1.00 14.01 ?  53  LEU   B H    1 
ATOM   4977 H  HA   . LEU   B 1 53  ? 53.899 -21.081 -3.341  1.00 14.49 ?  53  LEU   B HA   1 
ATOM   4978 H  HB2  . LEU   B 1 53  ? 52.061 -20.507 -1.284  1.00 14.96 ?  53  LEU   B HB2  1 
ATOM   4979 H  HB3  . LEU   B 1 53  ? 52.277 -19.572 -2.538  1.00 14.96 ?  53  LEU   B HB3  1 
ATOM   4980 H  HG   . LEU   B 1 53  ? 51.121 -22.133 -2.667  1.00 15.07 ?  53  LEU   B HG   1 
ATOM   4981 H  HD11 . LEU   B 1 53  ? 49.106 -21.068 -3.090  1.00 17.36 ?  53  LEU   B HD11 1 
ATOM   4982 H  HD12 . LEU   B 1 53  ? 49.663 -20.665 -1.657  1.00 17.36 ?  53  LEU   B HD12 1 
ATOM   4983 H  HD13 . LEU   B 1 53  ? 49.810 -19.660 -2.879  1.00 17.36 ?  53  LEU   B HD13 1 
ATOM   4984 H  HD21 . LEU   B 1 53  ? 50.636 -21.714 -4.883  1.00 17.90 ?  53  LEU   B HD21 1 
ATOM   4985 H  HD22 . LEU   B 1 53  ? 51.343 -20.296 -4.786  1.00 17.90 ?  53  LEU   B HD22 1 
ATOM   4986 H  HD23 . LEU   B 1 53  ? 52.206 -21.625 -4.668  1.00 17.90 ?  53  LEU   B HD23 1 
ATOM   4987 N  N    . ASN   B 1 54  ? 54.800 -20.117 -0.416  1.00 11.94 ?  54  ASN   B N    1 
ATOM   4988 C  CA   . ASN   B 1 54  ? 55.719 -19.206 0.251   1.00 12.60 ?  54  ASN   B CA   1 
ATOM   4989 C  C    . ASN   B 1 54  ? 57.159 -19.489 -0.152  1.00 13.14 ?  54  ASN   B C    1 
ATOM   4990 O  O    . ASN   B 1 54  ? 57.937 -18.552 -0.386  1.00 13.50 ?  54  ASN   B O    1 
ATOM   4991 C  CB   . ASN   B 1 54  ? 55.558 -19.279 1.762   1.00 13.19 ?  54  ASN   B CB   1 
ATOM   4992 C  CG   . ASN   B 1 54  ? 56.536 -18.370 2.468   1.00 13.53 ?  54  ASN   B CG   1 
ATOM   4993 O  OD1  . ASN   B 1 54  ? 56.558 -17.161 2.218   1.00 13.48 ?  54  ASN   B OD1  1 
ATOM   4994 N  ND2  . ASN   B 1 54  ? 57.373 -18.943 3.327   1.00 15.22 ?  54  ASN   B ND2  1 
ATOM   4995 H  H    . ASN   B 1 54  ? 54.355 -20.639 0.103   1.00 14.31 ?  54  ASN   B H    1 
ATOM   4996 H  HA   . ASN   B 1 54  ? 55.507 -18.301 -0.024  1.00 15.10 ?  54  ASN   B HA   1 
ATOM   4997 H  HB2  . ASN   B 1 54  ? 54.659 -19.001 2.004   1.00 15.81 ?  54  ASN   B HB2  1 
ATOM   4998 H  HB3  . ASN   B 1 54  ? 55.719 -20.187 2.060   1.00 15.81 ?  54  ASN   B HB3  1 
ATOM   4999 H  HD21 . ASN   B 1 54  ? 57.955 -18.468 3.747   1.00 18.24 ?  54  ASN   B HD21 1 
ATOM   5000 H  HD22 . ASN   B 1 54  ? 57.337 -19.793 3.464   1.00 18.24 ?  54  ASN   B HD22 1 
ATOM   5001 N  N    . LYS   B 1 55  ? 57.543 -20.769 -0.211  1.00 13.44 ?  55  LYS   B N    1 
ATOM   5002 C  CA   . LYS   B 1 55  ? 58.897 -21.115 -0.629  1.00 14.44 ?  55  LYS   B CA   1 
ATOM   5003 C  C    . LYS   B 1 55  ? 59.194 -20.573 -2.020  1.00 14.28 ?  55  LYS   B C    1 
ATOM   5004 O  O    . LYS   B 1 55  ? 60.289 -20.057 -2.270  1.00 14.68 ?  55  LYS   B O    1 
ATOM   5005 C  CB   . LYS   B 1 55  ? 59.086 -22.631 -0.582  1.00 15.99 ?  55  LYS   B CB   1 
ATOM   5006 C  CG   . LYS   B 1 55  ? 60.466 -23.087 -0.997  1.00 20.15 ?  55  LYS   B CG   1 
ATOM   5007 C  CD   . LYS   B 1 55  ? 60.636 -24.585 -0.824  1.00 23.65 ?  55  LYS   B CD   1 
ATOM   5008 C  CE   . LYS   B 1 55  ? 60.690 -24.984 0.648   1.00 26.50 ?  55  LYS   B CE   1 
ATOM   5009 N  NZ   . LYS   B 1 55  ? 61.105 -26.397 0.821   1.00 28.16 ?  55  LYS   B NZ   1 
ATOM   5010 H  H    . LYS   B 1 55  ? 57.038 -21.441 -0.019  1.00 16.11 ?  55  LYS   B H    1 
ATOM   5011 H  HA   . LYS   B 1 55  ? 59.526 -20.716 -0.016  1.00 17.31 ?  55  LYS   B HA   1 
ATOM   5012 H  HB2  . LYS   B 1 55  ? 58.931 -22.932 0.328   1.00 19.16 ?  55  LYS   B HB2  1 
ATOM   5013 H  HB3  . LYS   B 1 55  ? 58.444 -23.047 -1.178  1.00 19.16 ?  55  LYS   B HB3  1 
ATOM   5014 H  HG2  . LYS   B 1 55  ? 60.609 -22.874 -1.933  1.00 24.16 ?  55  LYS   B HG2  1 
ATOM   5015 H  HG3  . LYS   B 1 55  ? 61.130 -22.640 -0.447  1.00 24.16 ?  55  LYS   B HG3  1 
ATOM   5016 H  HD2  . LYS   B 1 55  ? 59.885 -25.046 -1.233  1.00 28.36 ?  55  LYS   B HD2  1 
ATOM   5017 H  HD3  . LYS   B 1 55  ? 61.467 -24.868 -1.241  1.00 28.36 ?  55  LYS   B HD3  1 
ATOM   5018 H  HE2  . LYS   B 1 55  ? 61.330 -24.414 1.106   1.00 31.78 ?  55  LYS   B HE2  1 
ATOM   5019 H  HE3  . LYS   B 1 55  ? 59.807 -24.872 1.038   1.00 31.78 ?  55  LYS   B HE3  1 
ATOM   5020 H  HZ1  . LYS   B 1 55  ? 61.098 -26.610 1.685   1.00 33.77 ?  55  LYS   B HZ1  1 
ATOM   5021 H  HZ2  . LYS   B 1 55  ? 60.543 -26.931 0.385   1.00 33.77 ?  55  LYS   B HZ2  1 
ATOM   5022 H  HZ3  . LYS   B 1 55  ? 61.925 -26.512 0.499   1.00 33.77 ?  55  LYS   B HZ3  1 
ATOM   5023 N  N    . ALA   B 1 56  ? 58.222 -20.655 -2.934  1.00 13.87 ?  56  ALA   B N    1 
ATOM   5024 C  CA   . ALA   B 1 56  ? 58.444 -20.156 -4.286  1.00 15.02 ?  56  ALA   B CA   1 
ATOM   5025 C  C    . ALA   B 1 56  ? 58.720 -18.657 -4.290  1.00 14.59 ?  56  ALA   B C    1 
ATOM   5026 O  O    . ALA   B 1 56  ? 59.444 -18.162 -5.165  1.00 15.04 ?  56  ALA   B O    1 
ATOM   5027 C  CB   . ALA   B 1 56  ? 57.251 -20.497 -5.181  1.00 15.61 ?  56  ALA   B CB   1 
ATOM   5028 H  H    . ALA   B 1 56  ? 57.433 -20.980 -2.798  1.00 16.62 ?  56  ALA   B H    1 
ATOM   5029 H  HA   . ALA   B 1 56  ? 59.221 -20.594 -4.656  1.00 18.00 ?  56  ALA   B HA   1 
ATOM   5030 H  HB1  . ALA   B 1 56  ? 57.422 -20.163 -6.080  1.00 18.71 ?  56  ALA   B HB1  1 
ATOM   5031 H  HB2  . ALA   B 1 56  ? 57.141 -21.462 -5.208  1.00 18.71 ?  56  ALA   B HB2  1 
ATOM   5032 H  HB3  . ALA   B 1 56  ? 56.451 -20.083 -4.824  1.00 18.71 ?  56  ALA   B HB3  1 
ATOM   5033 N  N    . THR   B 1 57  ? 58.164 -17.922 -3.326  1.00 13.94 ?  57  THR   B N    1 
ATOM   5034 C  CA   . THR   B 1 57  ? 58.400 -16.487 -3.205  1.00 13.94 ?  57  THR   B CA   1 
ATOM   5035 C  C    . THR   B 1 57  ? 59.646 -16.159 -2.393  1.00 15.19 ?  57  THR   B C    1 
ATOM   5036 O  O    . THR   B 1 57  ? 59.882 -14.983 -2.092  1.00 15.43 ?  57  THR   B O    1 
ATOM   5037 C  CB   . THR   B 1 57  ? 57.194 -15.759 -2.576  1.00 13.28 ?  57  THR   B CB   1 
ATOM   5038 O  OG1  . THR   B 1 57  ? 57.175 -15.967 -1.158  1.00 13.87 ?  57  THR   B OG1  1 
ATOM   5039 C  CG2  . THR   B 1 57  ? 55.874 -16.185 -3.219  1.00 13.42 ?  57  THR   B CG2  1 
ATOM   5040 H  H    . THR   B 1 57  ? 57.625 -18.234 -2.729  1.00 16.70 ?  57  THR   B H    1 
ATOM   5041 H  HA   . THR   B 1 57  ? 58.523 -16.122 -4.094  1.00 16.70 ?  57  THR   B HA   1 
ATOM   5042 H  HB   . THR   B 1 57  ? 57.296 -14.808 -2.743  1.00 15.92 ?  57  THR   B HB   1 
ATOM   5043 H  HG1  . THR   B 1 57  ? 57.097 -16.787 -0.992  1.00 16.62 ?  57  THR   B HG1  1 
ATOM   5044 H  HG21 . THR   B 1 57  ? 55.144 -15.656 -2.865  1.00 16.08 ?  57  THR   B HG21 1 
ATOM   5045 H  HG22 . THR   B 1 57  ? 55.916 -16.062 -4.181  1.00 16.08 ?  57  THR   B HG22 1 
ATOM   5046 H  HG23 . THR   B 1 57  ? 55.700 -17.122 -3.033  1.00 16.08 ?  57  THR   B HG23 1 
ATOM   5047 N  N    . ASN   B 1 58  ? 60.443 -17.162 -2.028  1.00 15.74 ?  58  ASN   B N    1 
ATOM   5048 C  CA   . ASN   B 1 58  ? 61.642 -16.943 -1.222  1.00 18.03 ?  58  ASN   B CA   1 
ATOM   5049 C  C    . ASN   B 1 58  ? 61.305 -16.226 0.086   1.00 16.50 ?  58  ASN   B C    1 
ATOM   5050 O  O    . ASN   B 1 58  ? 62.038 -15.347 0.549   1.00 17.46 ?  58  ASN   B O    1 
ATOM   5051 C  CB   . ASN   B 1 58  ? 62.725 -16.196 -2.008  1.00 24.57 ?  58  ASN   B CB   1 
ATOM   5052 C  CG   . ASN   B 1 58  ? 64.100 -16.339 -1.384  1.00 35.87 ?  58  ASN   B CG   1 
ATOM   5053 O  OD1  . ASN   B 1 58  ? 64.407 -17.351 -0.756  1.00 38.27 ?  58  ASN   B OD1  1 
ATOM   5054 N  ND2  . ASN   B 1 58  ? 64.935 -15.320 -1.555  1.00 42.54 ?  58  ASN   B ND2  1 
ATOM   5055 H  H    . ASN   B 1 58  ? 60.309 -17.991 -2.234  1.00 18.86 ?  58  ASN   B H    1 
ATOM   5056 H  HA   . ASN   B 1 58  ? 62.008 -17.813 -0.994  1.00 21.62 ?  58  ASN   B HA   1 
ATOM   5057 H  HB2  . ASN   B 1 58  ? 62.766 -16.551 -2.912  1.00 29.46 ?  58  ASN   B HB2  1 
ATOM   5058 H  HB3  . ASN   B 1 58  ? 62.506 -15.253 -2.033  1.00 29.46 ?  58  ASN   B HB3  1 
ATOM   5059 H  HD21 . ASN   B 1 58  ? 65.728 -15.353 -1.223  1.00 51.03 ?  58  ASN   B HD21 1 
ATOM   5060 H  HD22 . ASN   B 1 58  ? 64.683 -14.628 -1.999  1.00 51.03 ?  58  ASN   B HD22 1 
ATOM   5061 N  N    . ASN   B 1 59  ? 60.178 -16.610 0.689   1.00 15.41 ?  59  ASN   B N    1 
ATOM   5062 C  CA   . ASN   B 1 59  ? 59.695 -16.138 1.987   1.00 14.82 ?  59  ASN   B CA   1 
ATOM   5063 C  C    . ASN   B 1 59  ? 59.100 -14.733 1.931   1.00 14.53 ?  59  ASN   B C    1 
ATOM   5064 O  O    . ASN   B 1 59  ? 58.671 -14.226 2.972   1.00 14.60 ?  59  ASN   B O    1 
ATOM   5065 C  CB   . ASN   B 1 59  ? 60.768 -16.204 3.089   1.00 16.16 ?  59  ASN   B CB   1 
ATOM   5066 C  CG   . ASN   B 1 59  ? 60.184 -16.371 4.472   1.00 17.21 ?  59  ASN   B CG   1 
ATOM   5067 O  OD1  . ASN   B 1 59  ? 59.358 -17.258 4.707   1.00 17.62 ?  59  ASN   B OD1  1 
ATOM   5068 N  ND2  . ASN   B 1 59  ? 60.609 -15.522 5.401   1.00 18.16 ?  59  ASN   B ND2  1 
ATOM   5069 H  H    . ASN   B 1 59  ? 59.636 -17.188 0.339   1.00 18.47 ?  59  ASN   B H    1 
ATOM   5070 H  HA   . ASN   B 1 59  ? 58.984 -16.734 2.266   1.00 17.76 ?  59  ASN   B HA   1 
ATOM   5071 H  HB2  . ASN   B 1 59  ? 61.351 -16.964 2.926   1.00 19.37 ?  59  ASN   B HB2  1 
ATOM   5072 H  HB3  . ASN   B 1 59  ? 61.282 -15.385 3.087   1.00 19.37 ?  59  ASN   B HB3  1 
ATOM   5073 H  HD21 . ASN   B 1 59  ? 60.308 -15.577 6.207   1.00 21.77 ?  59  ASN   B HD21 1 
ATOM   5074 H  HD22 . ASN   B 1 59  ? 61.184 -14.917 5.198   1.00 21.77 ?  59  ASN   B HD22 1 
ATOM   5075 N  N    . ALA   B 1 60  ? 59.044 -14.092 0.761   1.00 14.71 ?  60  ALA   B N    1 
ATOM   5076 C  CA   . ALA   B 1 60  ? 58.448 -12.761 0.685   1.00 14.51 ?  60  ALA   B CA   1 
ATOM   5077 C  C    . ALA   B 1 60  ? 56.979 -12.789 1.085   1.00 13.24 ?  60  ALA   B C    1 
ATOM   5078 O  O    . ALA   B 1 60  ? 56.471 -11.839 1.697   1.00 14.08 ?  60  ALA   B O    1 
ATOM   5079 C  CB   . ALA   B 1 60  ? 58.610 -12.187 -0.723  1.00 15.69 ?  60  ALA   B CB   1 
ATOM   5080 H  H    . ALA   B 1 60  ? 59.335 -14.406 0.013   1.00 17.63 ?  60  ALA   B H    1 
ATOM   5081 H  HA   . ALA   B 1 60  ? 58.912 -12.179 1.303   1.00 17.39 ?  60  ALA   B HA   1 
ATOM   5082 H  HB1  . ALA   B 1 60  ? 58.211 -11.307 -0.750  1.00 18.81 ?  60  ALA   B HB1  1 
ATOM   5083 H  HB2  . ALA   B 1 60  ? 59.557 -12.131 -0.933  1.00 18.81 ?  60  ALA   B HB2  1 
ATOM   5084 H  HB3  . ALA   B 1 60  ? 58.168 -12.775 -1.356  1.00 18.81 ?  60  ALA   B HB3  1 
ATOM   5085 N  N    . MET   B 1 61  ? 56.277 -13.871 0.742   1.00 12.73 ?  61  MET   B N    1 
ATOM   5086 C  CA   . MET   B 1 61  ? 54.880 -13.993 1.131   1.00 12.78 ?  61  MET   B CA   1 
ATOM   5087 C  C    . MET   B 1 61  ? 54.738 -13.997 2.654   1.00 12.89 ?  61  MET   B C    1 
ATOM   5088 O  O    . MET   B 1 61  ? 53.838 -13.345 3.202   1.00 12.38 ?  61  MET   B O    1 
ATOM   5089 C  CB   . MET   B 1 61  ? 54.295 -15.262 0.500   1.00 12.62 ?  61  MET   B CB   1 
ATOM   5090 C  CG   . MET   B 1 61  ? 52.854 -15.546 0.906   1.00 11.94 ?  61  MET   B CG   1 
ATOM   5091 S  SD   . MET   B 1 61  ? 52.207 -17.056 0.155   1.00 12.87 ?  61  MET   B SD   1 
ATOM   5092 C  CE   . MET   B 1 61  ? 51.940 -16.470 -1.512  1.00 14.27 ?  61  MET   B CE   1 
ATOM   5093 H  H    . MET   B 1 61  ? 56.586 -14.543 0.292   1.00 15.26 ?  61  MET   B H    1 
ATOM   5094 H  HA   . MET   B 1 61  ? 54.390 -13.239 0.770   1.00 15.31 ?  61  MET   B HA   1 
ATOM   5095 H  HB2  . MET   B 1 61  ? 54.312 -15.167 -0.469  1.00 15.12 ?  61  MET   B HB2  1 
ATOM   5096 H  HB3  . MET   B 1 61  ? 54.831 -16.022 0.763   1.00 15.12 ?  61  MET   B HB3  1 
ATOM   5097 H  HG2  . MET   B 1 61  ? 52.806 -15.651 1.870   1.00 14.31 ?  61  MET   B HG2  1 
ATOM   5098 H  HG3  . MET   B 1 61  ? 52.290 -14.805 0.626   1.00 14.31 ?  61  MET   B HG3  1 
ATOM   5099 H  HE1  . MET   B 1 61  ? 51.560 -17.191 -2.041  1.00 17.11 ?  61  MET   B HE1  1 
ATOM   5100 H  HE2  . MET   B 1 61  ? 51.323 -15.720 -1.490  1.00 17.11 ?  61  MET   B HE2  1 
ATOM   5101 H  HE3  . MET   B 1 61  ? 52.785 -16.190 -1.895  1.00 17.11 ?  61  MET   B HE3  1 
ATOM   5102 N  N    . GLN   B 1 62  ? 55.617 -14.718 3.358   1.00 12.62 ?  62  GLN   B N    1 
ATOM   5103 C  CA   . GLN   B 1 62  ? 55.513 -14.776 4.813   1.00 13.24 ?  62  GLN   B CA   1 
ATOM   5104 C  C    . GLN   B 1 62  ? 55.794 -13.419 5.448   1.00 13.31 ?  62  GLN   B C    1 
ATOM   5105 O  O    . GLN   B 1 62  ? 55.106 -13.017 6.395   1.00 13.97 ?  62  GLN   B O    1 
ATOM   5106 C  CB   . GLN   B 1 62  ? 56.466 -15.831 5.376   1.00 13.16 ?  62  GLN   B CB   1 
ATOM   5107 C  CG   . GLN   B 1 62  ? 56.247 -16.099 6.853   1.00 13.35 ?  62  GLN   B CG   1 
ATOM   5108 C  CD   . GLN   B 1 62  ? 54.873 -16.684 7.104   1.00 13.24 ?  62  GLN   B CD   1 
ATOM   5109 O  OE1  . GLN   B 1 62  ? 54.611 -17.836 6.753   1.00 13.70 ?  62  GLN   B OE1  1 
ATOM   5110 N  NE2  . GLN   B 1 62  ? 53.968 -15.880 7.659   1.00 13.49 ?  62  GLN   B NE2  1 
ATOM   5111 H  H    . GLN   B 1 62  ? 56.261 -15.178 3.017   1.00 15.12 ?  62  GLN   B H    1 
ATOM   5112 H  HA   . GLN   B 1 62  ? 54.608 -15.035 5.049   1.00 15.87 ?  62  GLN   B HA   1 
ATOM   5113 H  HB2  . GLN   B 1 62  ? 56.340 -16.666 4.897   1.00 15.77 ?  62  GLN   B HB2  1 
ATOM   5114 H  HB3  . GLN   B 1 62  ? 57.382 -15.523 5.261   1.00 15.77 ?  62  GLN   B HB3  1 
ATOM   5115 H  HG2  . GLN   B 1 62  ? 56.910 -16.740 7.161   1.00 15.99 ?  62  GLN   B HG2  1 
ATOM   5116 H  HG3  . GLN   B 1 62  ? 56.326 -15.272 7.348   1.00 15.99 ?  62  GLN   B HG3  1 
ATOM   5117 H  HE21 . GLN   B 1 62  ? 54.187 -15.077 7.877   1.00 16.16 ?  62  GLN   B HE21 1 
ATOM   5118 H  HE22 . GLN   B 1 62  ? 53.175 -16.168 7.814   1.00 16.16 ?  62  GLN   B HE22 1 
ATOM   5119 N  N    . VAL   B 1 63  ? 56.807 -12.703 4.956   1.00 13.87 ?  63  VAL   B N    1 
ATOM   5120 C  CA   . VAL   B 1 63  ? 57.111 -11.383 5.510   1.00 14.96 ?  63  VAL   B CA   1 
ATOM   5121 C  C    . VAL   B 1 63  ? 55.916 -10.450 5.335   1.00 14.24 ?  63  VAL   B C    1 
ATOM   5122 O  O    . VAL   B 1 63  ? 55.504 -9.745  6.268   1.00 15.11 ?  63  VAL   B O    1 
ATOM   5123 C  CB   . VAL   B 1 63  ? 58.399 -10.820 4.881   1.00 16.53 ?  63  VAL   B CB   1 
ATOM   5124 C  CG1  . VAL   B 1 63  ? 58.616 -9.371  5.313   1.00 17.25 ?  63  VAL   B CG1  1 
ATOM   5125 C  CG2  . VAL   B 1 63  ? 59.595 -11.682 5.280   1.00 17.17 ?  63  VAL   B CG2  1 
ATOM   5126 H  H    . VAL   B 1 63  ? 57.316 -12.951 4.303   1.00 16.63 ?  63  VAL   B H    1 
ATOM   5127 H  HA   . VAL   B 1 63  ? 57.272 -11.483 6.457   1.00 17.93 ?  63  VAL   B HA   1 
ATOM   5128 H  HB   . VAL   B 1 63  ? 58.327 -10.844 3.913   1.00 19.82 ?  63  VAL   B HB   1 
ATOM   5129 H  HG11 . VAL   B 1 63  ? 59.533 -9.120  5.124   1.00 20.69 ?  63  VAL   B HG11 1 
ATOM   5130 H  HG12 . VAL   B 1 63  ? 58.007 -8.801  4.821   1.00 20.69 ?  63  VAL   B HG12 1 
ATOM   5131 H  HG13 . VAL   B 1 63  ? 58.445 -9.300  6.266   1.00 20.69 ?  63  VAL   B HG13 1 
ATOM   5132 H  HG21 . VAL   B 1 63  ? 60.401 -11.305 4.890   1.00 20.58 ?  63  VAL   B HG21 1 
ATOM   5133 H  HG22 . VAL   B 1 63  ? 59.671 -11.683 6.249   1.00 20.58 ?  63  VAL   B HG22 1 
ATOM   5134 H  HG23 . VAL   B 1 63  ? 59.461 -12.584 4.957   1.00 20.58 ?  63  VAL   B HG23 1 
ATOM   5135 N  N    . GLU   B 1 64  ? 55.343 -10.434 4.131   1.00 13.63 ?  64  GLU   B N    1 
ATOM   5136 C  CA   . GLU   B 1 64  ? 54.179 -9.597  3.857   1.00 13.06 ?  64  GLU   B CA   1 
ATOM   5137 C  C    . GLU   B 1 64  ? 52.998 -10.001 4.731   1.00 12.26 ?  64  GLU   B C    1 
ATOM   5138 O  O    . GLU   B 1 64  ? 52.251 -9.143  5.227   1.00 13.04 ?  64  GLU   B O    1 
ATOM   5139 C  CB   . GLU   B 1 64  ? 53.821 -9.751  2.378   1.00 13.97 ?  64  GLU   B CB   1 
ATOM   5140 C  CG   . GLU   B 1 64  ? 52.563 -9.017  1.938   1.00 13.79 ?  64  GLU   B CG   1 
ATOM   5141 C  CD   . GLU   B 1 64  ? 52.031 -9.512  0.600   1.00 14.54 ?  64  GLU   B CD   1 
ATOM   5142 O  OE1  . GLU   B 1 64  ? 52.197 -10.718 0.278   1.00 15.12 ?  64  GLU   B OE1  1 
ATOM   5143 O  OE2  . GLU   B 1 64  ? 51.416 -8.695  -0.124  1.00 15.29 -1 64  GLU   B OE2  1 
ATOM   5144 H  H    . GLU   B 1 64  ? 55.615 -10.897 3.454   1.00 16.33 ?  64  GLU   B H    1 
ATOM   5145 H  HA   . GLU   B 1 64  ? 54.395 -8.668  4.032   1.00 15.65 ?  64  GLU   B HA   1 
ATOM   5146 H  HB2  . GLU   B 1 64  ? 54.552 -9.404  1.842   1.00 16.74 ?  64  GLU   B HB2  1 
ATOM   5147 H  HB3  . GLU   B 1 64  ? 53.691 -10.689 2.187   1.00 16.74 ?  64  GLU   B HB3  1 
ATOM   5148 H  HG2  . GLU   B 1 64  ? 51.861 -9.144  2.600   1.00 16.53 ?  64  GLU   B HG2  1 
ATOM   5149 H  HG3  . GLU   B 1 64  ? 52.762 -8.071  1.853   1.00 16.53 ?  64  GLU   B HG3  1 
ATOM   5150 N  N    . SER   B 1 65  ? 52.814 -11.309 4.915   1.00 12.56 ?  65  SER   B N    1 
ATOM   5151 C  CA   . SER   B 1 65  ? 51.707 -11.816 5.716   1.00 12.99 ?  65  SER   B CA   1 
ATOM   5152 C  C    . SER   B 1 65  ? 51.847 -11.420 7.179   1.00 13.45 ?  65  SER   B C    1 
ATOM   5153 O  O    . SER   B 1 65  ? 50.852 -11.048 7.819   1.00 13.13 ?  65  SER   B O    1 
ATOM   5154 C  CB   . SER   B 1 65  ? 51.628 -13.335 5.586   1.00 13.20 ?  65  SER   B CB   1 
ATOM   5155 O  OG   . SER   B 1 65  ? 51.278 -13.731 4.272   1.00 13.13 ?  65  SER   B OG   1 
ATOM   5156 H  H    . SER   B 1 65  ? 53.314 -11.930 4.580   1.00 15.05 ?  65  SER   B H    1 
ATOM   5157 H  HA   . SER   B 1 65  ? 50.874 -11.444 5.383   1.00 15.56 ?  65  SER   B HA   1 
ATOM   5158 H  HB2  . SER   B 1 65  ? 52.487 -13.718 5.802   1.00 15.82 ?  65  SER   B HB2  1 
ATOM   5159 H  HB3  . SER   B 1 65  ? 50.951 -13.667 6.203   1.00 15.82 ?  65  SER   B HB3  1 
ATOM   5160 H  HG   . SER   B 1 65  ? 51.841 -13.436 3.720   1.00 15.73 ?  65  SER   B HG   1 
ATOM   5161 N  N    . ASP   B 1 66  ? 53.059 -11.515 7.740   1.00 13.41 ?  66  ASP   B N    1 
ATOM   5162 C  CA   . ASP   B 1 66  ? 53.246 -11.122 9.135   1.00 13.62 ?  66  ASP   B CA   1 
ATOM   5163 C  C    . ASP   B 1 66  ? 52.930 -9.644  9.335   1.00 13.55 ?  66  ASP   B C    1 
ATOM   5164 O  O    . ASP   B 1 66  ? 52.350 -9.254  10.356  1.00 14.16 ?  66  ASP   B O    1 
ATOM   5165 C  CB   . ASP   B 1 66  ? 54.673 -11.432 9.589   1.00 14.73 ?  66  ASP   B CB   1 
ATOM   5166 C  CG   . ASP   B 1 66  ? 54.939 -12.923 9.748   1.00 16.59 ?  66  ASP   B CG   1 
ATOM   5167 O  OD1  . ASP   B 1 66  ? 53.989 -13.740 9.687   1.00 17.35 ?  66  ASP   B OD1  1 
ATOM   5168 O  OD2  . ASP   B 1 66  ? 56.121 -13.282 9.948   1.00 19.53 -1 66  ASP   B OD2  1 
ATOM   5169 H  H    . ASP   B 1 66  ? 53.766 -11.807 7.344   1.00 16.07 ?  66  ASP   B H    1 
ATOM   5170 H  HA   . ASP   B 1 66  ? 52.640 -11.628 9.692   1.00 16.32 ?  66  ASP   B HA   1 
ATOM   5171 H  HB2  . ASP   B 1 66  ? 55.299 -11.094 8.932   1.00 17.65 ?  66  ASP   B HB2  1 
ATOM   5172 H  HB3  . ASP   B 1 66  ? 54.832 -11.004 10.448  1.00 17.65 ?  66  ASP   B HB3  1 
ATOM   5173 N  N    . ASP   B 1 67  ? 53.302 -8.803  8.370   1.00 13.34 ?  67  ASP   B N    1 
ATOM   5174 C  CA   . ASP   B 1 67  ? 52.957 -7.390  8.454   1.00 14.04 ?  67  ASP   B CA   1 
ATOM   5175 C  C    . ASP   B 1 67  ? 51.446 -7.181  8.375   1.00 14.15 ?  67  ASP   B C    1 
ATOM   5176 O  O    . ASP   B 1 67  ? 50.888 -6.370  9.122   1.00 14.67 ?  67  ASP   B O    1 
ATOM   5177 C  CB   . ASP   B 1 67  ? 53.663 -6.623  7.346   1.00 15.65 ?  67  ASP   B CB   1 
ATOM   5178 C  CG   . ASP   B 1 67  ? 53.240 -5.181  7.307   1.00 17.22 ?  67  ASP   B CG   1 
ATOM   5179 O  OD1  . ASP   B 1 67  ? 53.729 -4.378  8.135   1.00 18.53 ?  67  ASP   B OD1  1 
ATOM   5180 O  OD2  . ASP   B 1 67  ? 52.381 -4.865  6.468   1.00 18.18 -1 67  ASP   B OD2  1 
ATOM   5181 H  H    . ASP   B 1 67  ? 53.760 -9.023  7.672   1.00 15.99 ?  67  ASP   B H    1 
ATOM   5182 H  HA   . ASP   B 1 67  ? 53.270 -7.037  9.304   1.00 16.83 ?  67  ASP   B HA   1 
ATOM   5183 H  HB2  . ASP   B 1 67  ? 54.624 -6.648  7.493   1.00 18.76 ?  67  ASP   B HB2  1 
ATOM   5184 H  HB3  . ASP   B 1 67  ? 53.452 -7.030  6.488   1.00 18.76 ?  67  ASP   B HB3  1 
ATOM   5185 N  N    . TYR   B 1 68  ? 50.764 -7.915  7.487   1.00 14.01 ?  68  TYR   B N    1 
ATOM   5186 C  CA   . TYR   B 1 68  ? 49.307 -7.837  7.418   1.00 14.68 ?  68  TYR   B CA   1 
ATOM   5187 C  C    . TYR   B 1 68  ? 48.675 -8.181  8.764   1.00 14.24 ?  68  TYR   B C    1 
ATOM   5188 O  O    . TYR   B 1 68  ? 47.739 -7.507  9.211   1.00 15.15 ?  68  TYR   B O    1 
ATOM   5189 C  CB   . TYR   B 1 68  ? 48.772 -8.764  6.316   1.00 15.15 ?  68  TYR   B CB   1 
ATOM   5190 C  CG   . TYR   B 1 68  ? 47.265 -8.915  6.371   1.00 16.32 ?  68  TYR   B CG   1 
ATOM   5191 C  CD1  . TYR   B 1 68  ? 46.679 -9.873  7.189   1.00 17.39 ?  68  TYR   B CD1  1 
ATOM   5192 C  CD2  . TYR   B 1 68  ? 46.433 -8.081  5.641   1.00 17.16 ?  68  TYR   B CD2  1 
ATOM   5193 C  CE1  . TYR   B 1 68  ? 45.312 -9.997  7.278   1.00 18.28 ?  68  TYR   B CE1  1 
ATOM   5194 C  CE2  . TYR   B 1 68  ? 45.050 -8.211  5.716   1.00 17.63 ?  68  TYR   B CE2  1 
ATOM   5195 C  CZ   . TYR   B 1 68  ? 44.510 -9.165  6.540   1.00 18.23 ?  68  TYR   B CZ   1 
ATOM   5196 O  OH   . TYR   B 1 68  ? 43.143 -9.286  6.630   1.00 19.63 ?  68  TYR   B OH   1 
ATOM   5197 H  H    . TYR   B 1 68  ? 51.123 -8.466  6.928   1.00 16.79 ?  68  TYR   B H    1 
ATOM   5198 H  HA   . TYR   B 1 68  ? 49.059 -6.929  7.198   1.00 17.59 ?  68  TYR   B HA   1 
ATOM   5199 H  HB2  . TYR   B 1 68  ? 49.002 -8.390  5.453   1.00 18.15 ?  68  TYR   B HB2  1 
ATOM   5200 H  HB3  . TYR   B 1 68  ? 49.167 -9.642  6.420   1.00 18.15 ?  68  TYR   B HB3  1 
ATOM   5201 H  HD1  . TYR   B 1 68  ? 47.222 -10.440 7.693   1.00 20.84 ?  68  TYR   B HD1  1 
ATOM   5202 H  HD2  . TYR   B 1 68  ? 46.805 -7.426  5.101   1.00 20.57 ?  68  TYR   B HD2  1 
ATOM   5203 H  HE1  . TYR   B 1 68  ? 44.932 -10.657 7.819   1.00 21.92 ?  68  TYR   B HE1  1 
ATOM   5204 H  HE2  . TYR   B 1 68  ? 44.495 -7.646  5.229   1.00 21.13 ?  68  TYR   B HE2  1 
ATOM   5205 H  HH   . TYR   B 1 68  ? 42.758 -8.733  6.121   1.00 23.54 ?  68  TYR   B HH   1 
ATOM   5206 N  N    . ILE   B 1 69  ? 49.161 -9.243  9.413   1.00 13.85 ?  69  ILE   B N    1 
ATOM   5207 C  CA   . ILE   B 1 69  ? 48.598 -9.669  10.691  1.00 14.45 ?  69  ILE   B CA   1 
ATOM   5208 C  C    . ILE   B 1 69  ? 48.850 -8.622  11.767  1.00 14.09 ?  69  ILE   B C    1 
ATOM   5209 O  O    . ILE   B 1 69  ? 47.980 -8.343  12.599  1.00 14.38 ?  69  ILE   B O    1 
ATOM   5210 C  CB   . ILE   B 1 69  ? 49.170 -11.047 11.083  1.00 15.22 ?  69  ILE   B CB   1 
ATOM   5211 C  CG1  . ILE   B 1 69  ? 48.636 -12.148 10.157  1.00 15.64 ?  69  ILE   B CG1  1 
ATOM   5212 C  CG2  . ILE   B 1 69  ? 48.887 -11.361 12.552  1.00 16.19 ?  69  ILE   B CG2  1 
ATOM   5213 C  CD1  . ILE   B 1 69  ? 47.154 -12.447 10.308  1.00 16.30 ?  69  ILE   B CD1  1 
ATOM   5214 H  H    . ILE   B 1 69  ? 49.808 -9.734  9.136   1.00 16.60 ?  69  ILE   B H    1 
ATOM   5215 H  HA   . ILE   B 1 69  ? 47.638 -9.766  10.597  1.00 17.32 ?  69  ILE   B HA   1 
ATOM   5216 H  HB   . ILE   B 1 69  ? 50.135 -11.009 10.974  1.00 18.25 ?  69  ILE   B HB   1 
ATOM   5217 H  HG12 . ILE   B 1 69  ? 48.792 -11.875 9.239   1.00 18.75 ?  69  ILE   B HG12 1 
ATOM   5218 H  HG13 . ILE   B 1 69  ? 49.123 -12.967 10.340  1.00 18.75 ?  69  ILE   B HG13 1 
ATOM   5219 H  HG21 . ILE   B 1 69  ? 49.028 -12.309 12.701  1.00 19.40 ?  69  ILE   B HG21 1 
ATOM   5220 H  HG22 . ILE   B 1 69  ? 49.496 -10.850 13.110  1.00 19.40 ?  69  ILE   B HG22 1 
ATOM   5221 H  HG23 . ILE   B 1 69  ? 47.971 -11.126 12.754  1.00 19.40 ?  69  ILE   B HG23 1 
ATOM   5222 H  HD11 . ILE   B 1 69  ? 46.922 -13.174 9.715   1.00 19.53 ?  69  ILE   B HD11 1 
ATOM   5223 H  HD12 . ILE   B 1 69  ? 46.973 -12.696 11.227  1.00 19.53 ?  69  ILE   B HD12 1 
ATOM   5224 H  HD13 . ILE   B 1 69  ? 46.646 -11.654 10.074  1.00 19.53 ?  69  ILE   B HD13 1 
ATOM   5225 N  N    . ALA   B 1 70  ? 50.045 -8.034  11.784  1.00 14.15 ?  70  ALA   B N    1 
ATOM   5226 C  CA   . ALA   B 1 70  ? 50.332 -7.005  12.775  1.00 13.86 ?  70  ALA   B CA   1 
ATOM   5227 C  C    . ALA   B 1 70  ? 49.341 -5.857  12.668  1.00 14.48 ?  70  ALA   B C    1 
ATOM   5228 O  O    . ALA   B 1 70  ? 48.905 -5.307  13.684  1.00 14.83 ?  70  ALA   B O    1 
ATOM   5229 C  CB   . ALA   B 1 70  ? 51.764 -6.501  12.611  1.00 14.54 ?  70  ALA   B CB   1 
ATOM   5230 H  H    . ALA   B 1 70  ? 50.683 -8.208  11.247  1.00 16.96 ?  70  ALA   B H    1 
ATOM   5231 H  HA   . ALA   B 1 70  ? 50.251 -7.385  13.666  1.00 16.61 ?  70  ALA   B HA   1 
ATOM   5232 H  HB1  . ALA   B 1 70  ? 51.948 -5.835  13.293  1.00 17.43 ?  70  ALA   B HB1  1 
ATOM   5233 H  HB2  . ALA   B 1 70  ? 52.376 -7.249  12.711  1.00 17.43 ?  70  ALA   B HB2  1 
ATOM   5234 H  HB3  . ALA   B 1 70  ? 51.864 -6.110  11.730  1.00 17.43 ?  70  ALA   B HB3  1 
ATOM   5235 N  N    . THR   B 1 71  ? 48.963 -5.493  11.446  1.00 15.32 ?  71  THR   B N    1 
ATOM   5236 C  CA   . THR   B 1 71  ? 48.069 -4.360  11.235  1.00 16.12 ?  71  THR   B CA   1 
ATOM   5237 C  C    . THR   B 1 71  ? 46.601 -4.726  11.435  1.00 16.75 ?  71  THR   B C    1 
ATOM   5238 O  O    . THR   B 1 71  ? 45.819 -3.909  11.944  1.00 18.34 ?  71  THR   B O    1 
ATOM   5239 C  CB   . THR   B 1 71  ? 48.291 -3.791  9.831   1.00 17.89 ?  71  THR   B CB   1 
ATOM   5240 O  OG1  . THR   B 1 71  ? 49.618 -3.263  9.736   1.00 20.14 ?  71  THR   B OG1  1 
ATOM   5241 C  CG2  . THR   B 1 71  ? 47.275 -2.697  9.507   1.00 19.19 ?  71  THR   B CG2  1 
ATOM   5242 H  H    . THR   B 1 71  ? 49.210 -5.887  10.724  1.00 18.36 ?  71  THR   B H    1 
ATOM   5243 H  HA   . THR   B 1 71  ? 48.291 -3.663  11.871  1.00 19.32 ?  71  THR   B HA   1 
ATOM   5244 H  HB   . THR   B 1 71  ? 48.200 -4.494  9.173   1.00 21.45 ?  71  THR   B HB   1 
ATOM   5245 H  HG1  . THR   B 1 71  ? 49.750 -2.921  8.976   1.00 24.15 ?  71  THR   B HG1  1 
ATOM   5246 H  HG21 . THR   B 1 71  ? 47.580 -2.171  8.749   1.00 23.01 ?  71  THR   B HG21 1 
ATOM   5247 H  HG22 . THR   B 1 71  ? 46.418 -3.093  9.288   1.00 23.01 ?  71  THR   B HG22 1 
ATOM   5248 H  HG23 . THR   B 1 71  ? 47.166 -2.107  10.271  1.00 23.01 ?  71  THR   B HG23 1 
ATOM   5249 N  N    . ASN   B 1 72  ? 46.206 -5.940  11.042  1.00 16.30 ?  72  ASN   B N    1 
ATOM   5250 C  CA   . ASN   B 1 72  ? 44.801 -6.293  10.910  1.00 16.41 ?  72  ASN   B CA   1 
ATOM   5251 C  C    . ASN   B 1 72  ? 44.321 -7.389  11.851  1.00 17.33 ?  72  ASN   B C    1 
ATOM   5252 O  O    . ASN   B 1 72  ? 43.102 -7.543  12.013  1.00 18.80 ?  72  ASN   B O    1 
ATOM   5253 C  CB   . ASN   B 1 72  ? 44.501 -6.721  9.466   1.00 17.98 ?  72  ASN   B CB   1 
ATOM   5254 C  CG   . ASN   B 1 72  ? 44.777 -5.618  8.473   1.00 18.82 ?  72  ASN   B CG   1 
ATOM   5255 O  OD1  . ASN   B 1 72  ? 45.784 -5.636  7.758   1.00 19.83 ?  72  ASN   B OD1  1 
ATOM   5256 N  ND2  . ASN   B 1 72  ? 43.902 -4.632  8.444   1.00 20.34 ?  72  ASN   B ND2  1 
ATOM   5257 H  H    . ASN   B 1 72  ? 46.747 -6.587  10.847  1.00 19.53 ?  72  ASN   B H    1 
ATOM   5258 H  HA   . ASN   B 1 72  ? 44.272 -5.504  11.092  1.00 19.67 ?  72  ASN   B HA   1 
ATOM   5259 H  HB2  . ASN   B 1 72  ? 45.063 -7.480  9.237   1.00 21.56 ?  72  ASN   B HB2  1 
ATOM   5260 H  HB3  . ASN   B 1 72  ? 43.568 -6.964  9.395   1.00 21.56 ?  72  ASN   B HB3  1 
ATOM   5261 H  HD21 . ASN   B 1 72  ? 44.010 -3.977  7.898   1.00 24.39 ?  72  ASN   B HD21 1 
ATOM   5262 H  HD22 . ASN   B 1 72  ? 43.212 -4.653  8.959   1.00 24.39 ?  72  ASN   B HD22 1 
ATOM   5263 N  N    . GLY   B 1 73  ? 45.222 -8.140  12.475  1.00 16.65 ?  73  GLY   B N    1 
ATOM   5264 C  CA   . GLY   B 1 73  ? 44.827 -9.285  13.260  1.00 16.28 ?  73  GLY   B CA   1 
ATOM   5265 C  C    . GLY   B 1 73  ? 44.471 -10.473 12.391  1.00 14.78 ?  73  GLY   B C    1 
ATOM   5266 O  O    . GLY   B 1 73  ? 44.462 -10.392 11.160  1.00 14.56 ?  73  GLY   B O    1 
ATOM   5267 H  H    . GLY   B 1 73  ? 46.073 -8.001  12.457  1.00 19.96 ?  73  GLY   B H    1 
ATOM   5268 H  HA2  . GLY   B 1 73  ? 45.552 -9.537  13.853  1.00 19.51 ?  73  GLY   B HA2  1 
ATOM   5269 H  HA3  . GLY   B 1 73  ? 44.054 -9.054  13.801  1.00 19.51 ?  73  GLY   B HA3  1 
ATOM   5270 N  N    . PRO   B 1 74  ? 44.164 -11.600 13.029  1.00 14.87 ?  74  PRO   B N    1 
ATOM   5271 C  CA   . PRO   B 1 74  ? 43.912 -12.833 12.281  1.00 14.27 ?  74  PRO   B CA   1 
ATOM   5272 C  C    . PRO   B 1 74  ? 42.610 -12.779 11.494  1.00 13.57 ?  74  PRO   B C    1 
ATOM   5273 O  O    . PRO   B 1 74  ? 41.666 -12.046 11.816  1.00 15.06 ?  74  PRO   B O    1 
ATOM   5274 C  CB   . PRO   B 1 74  ? 43.839 -13.897 13.381  1.00 15.35 ?  74  PRO   B CB   1 
ATOM   5275 C  CG   . PRO   B 1 74  ? 43.402 -13.151 14.597  1.00 17.42 ?  74  PRO   B CG   1 
ATOM   5276 C  CD   . PRO   B 1 74  ? 44.060 -11.805 14.484  1.00 16.58 ?  74  PRO   B CD   1 
ATOM   5277 H  HA   . PRO   B 1 74  ? 44.657 -13.024 11.683  1.00 17.10 ?  74  PRO   B HA   1 
ATOM   5278 H  HB2  . PRO   B 1 74  ? 43.187 -14.573 13.134  1.00 18.40 ?  74  PRO   B HB2  1 
ATOM   5279 H  HB3  . PRO   B 1 74  ? 44.714 -14.294 13.512  1.00 18.40 ?  74  PRO   B HB3  1 
ATOM   5280 H  HG2  . PRO   B 1 74  ? 42.435 -13.062 14.593  1.00 20.88 ?  74  PRO   B HG2  1 
ATOM   5281 H  HG3  . PRO   B 1 74  ? 43.703 -13.617 15.389  1.00 20.88 ?  74  PRO   B HG3  1 
ATOM   5282 H  HD2  . PRO   B 1 74  ? 43.502 -11.118 14.889  1.00 19.87 ?  74  PRO   B HD2  1 
ATOM   5283 H  HD3  . PRO   B 1 74  ? 44.944 -11.822 14.884  1.00 19.87 ?  74  PRO   B HD3  1 
ATOM   5284 N  N    . LEU   B 1 75  ? 42.581 -13.591 10.440  1.00 13.14 ?  75  LEU   B N    1 
ATOM   5285 C  CA   . LEU   B 1 75  ? 41.366 -13.805 9.672   1.00 13.49 ?  75  LEU   B CA   1 
ATOM   5286 C  C    . LEU   B 1 75  ? 40.391 -14.666 10.474  1.00 13.80 ?  75  LEU   B C    1 
ATOM   5287 O  O    . LEU   B 1 75  ? 40.732 -15.233 11.513  1.00 14.92 ?  75  LEU   B O    1 
ATOM   5288 C  CB   . LEU   B 1 75  ? 41.686 -14.516 8.356   1.00 13.55 ?  75  LEU   B CB   1 
ATOM   5289 C  CG   . LEU   B 1 75  ? 42.547 -13.775 7.326   1.00 15.26 ?  75  LEU   B CG   1 
ATOM   5290 C  CD1  . LEU   B 1 75  ? 42.731 -14.610 6.061   1.00 16.69 ?  75  LEU   B CD1  1 
ATOM   5291 C  CD2  . LEU   B 1 75  ? 41.970 -12.429 6.978   1.00 18.71 ?  75  LEU   B CD2  1 
ATOM   5292 H  H    . LEU   B 1 75  ? 43.257 -14.038 10.147  1.00 15.75 ?  75  LEU   B H    1 
ATOM   5293 H  HA   . LEU   B 1 75  ? 40.943 -12.954 9.475   1.00 16.16 ?  75  LEU   B HA   1 
ATOM   5294 H  HB2  . LEU   B 1 75  ? 42.149 -15.342 8.566   1.00 16.24 ?  75  LEU   B HB2  1 
ATOM   5295 H  HB3  . LEU   B 1 75  ? 40.847 -14.728 7.916   1.00 16.24 ?  75  LEU   B HB3  1 
ATOM   5296 H  HG   . LEU   B 1 75  ? 43.429 -13.626 7.706   1.00 18.29 ?  75  LEU   B HG   1 
ATOM   5297 H  HD11 . LEU   B 1 75  ? 43.285 -14.115 5.432   1.00 20.01 ?  75  LEU   B HD11 1 
ATOM   5298 H  HD12 . LEU   B 1 75  ? 43.167 -15.445 6.293   1.00 20.01 ?  75  LEU   B HD12 1 
ATOM   5299 H  HD13 . LEU   B 1 75  ? 41.864 -14.785 5.668   1.00 20.01 ?  75  LEU   B HD13 1 
ATOM   5300 H  HD21 . LEU   B 1 75  ? 42.498 -12.031 6.269   1.00 22.43 ?  75  LEU   B HD21 1 
ATOM   5301 H  HD22 . LEU   B 1 75  ? 41.054 -12.546 6.686   1.00 22.43 ?  75  LEU   B HD22 1 
ATOM   5302 H  HD23 . LEU   B 1 75  ? 41.997 -11.862 7.767   1.00 22.43 ?  75  LEU   B HD23 1 
ATOM   5303 N  N    . LYS   B 1 76  ? 39.159 -14.760 9.973   1.00 15.31 ?  76  LYS   B N    1 
ATOM   5304 C  CA   . LYS   B 1 76  ? 38.178 -15.720 10.459  1.00 16.60 ?  76  LYS   B CA   1 
ATOM   5305 C  C    . LYS   B 1 76  ? 38.267 -16.990 9.620   1.00 15.03 ?  76  LYS   B C    1 
ATOM   5306 O  O    . LYS   B 1 76  ? 38.540 -16.930 8.420   1.00 14.56 ?  76  LYS   B O    1 
ATOM   5307 C  CB   . LYS   B 1 76  ? 36.760 -15.154 10.285  1.00 18.65 ?  76  LYS   B CB   1 
ATOM   5308 C  CG   . LYS   B 1 76  ? 36.477 -13.775 10.908  1.00 20.12 ?  76  LYS   B CG   1 
ATOM   5309 C  CD   . LYS   B 1 76  ? 35.069 -13.257 10.549  1.00 21.83 ?  76  LYS   B CD   1 
ATOM   5310 C  CE   . LYS   B 1 76  ? 34.789 -11.893 11.161  1.00 23.62 ?  76  LYS   B CE   1 
ATOM   5311 N  NZ   . LYS   B 1 76  ? 33.498 -11.301 10.706  1.00 24.69 ?  76  LYS   B NZ   1 
ATOM   5312 H  H    . LYS   B 1 76  ? 38.866 -14.269 9.333   1.00 18.35 ?  76  LYS   B H    1 
ATOM   5313 H  HA   . LYS   B 1 76  ? 38.332 -15.936 11.393  1.00 19.90 ?  76  LYS   B HA   1 
ATOM   5314 H  HB2  . LYS   B 1 76  ? 36.578 -15.078 9.335   1.00 22.36 ?  76  LYS   B HB2  1 
ATOM   5315 H  HB3  . LYS   B 1 76  ? 36.131 -15.776 10.682  1.00 22.36 ?  76  LYS   B HB3  1 
ATOM   5316 H  HG2  . LYS   B 1 76  ? 36.541 -13.841 11.873  1.00 24.13 ?  76  LYS   B HG2  1 
ATOM   5317 H  HG3  . LYS   B 1 76  ? 37.130 -13.136 10.574  1.00 24.13 ?  76  LYS   B HG3  1 
ATOM   5318 H  HD2  . LYS   B 1 76  ? 34.998 -13.178 9.583   1.00 26.18 ?  76  LYS   B HD2  1 
ATOM   5319 H  HD3  . LYS   B 1 76  ? 34.408 -13.883 10.882  1.00 26.18 ?  76  LYS   B HD3  1 
ATOM   5320 H  HE2  . LYS   B 1 76  ? 34.755 -11.984 12.126  1.00 28.32 ?  76  LYS   B HE2  1 
ATOM   5321 H  HE3  . LYS   B 1 76  ? 35.504 -11.285 10.912  1.00 28.32 ?  76  LYS   B HE3  1 
ATOM   5322 H  HZ1  . LYS   B 1 76  ? 33.376 -10.505 11.089  1.00 29.61 ?  76  LYS   B HZ1  1 
ATOM   5323 H  HZ2  . LYS   B 1 76  ? 33.504 -11.196 9.822   1.00 29.61 ?  76  LYS   B HZ2  1 
ATOM   5324 H  HZ3  . LYS   B 1 76  ? 32.821 -11.834 10.929  1.00 29.61 ?  76  LYS   B HZ3  1 
ATOM   5325 N  N    . VAL   B 1 77  ? 38.014 -18.146 10.247  1.00 15.88 ?  77  VAL   B N    1 
ATOM   5326 C  CA   . VAL   B 1 77  ? 37.803 -19.357 9.461   1.00 16.01 ?  77  VAL   B CA   1 
ATOM   5327 C  C    . VAL   B 1 77  ? 36.613 -19.119 8.544   1.00 14.53 ?  77  VAL   B C    1 
ATOM   5328 O  O    . VAL   B 1 77  ? 35.547 -18.673 8.990   1.00 14.24 ?  77  VAL   B O    1 
ATOM   5329 C  CB   . VAL   B 1 77  ? 37.601 -20.582 10.368  1.00 17.50 ?  77  VAL   B CB   1 
ATOM   5330 C  CG1  . VAL   B 1 77  ? 37.315 -21.813 9.518   1.00 18.26 ?  77  VAL   B CG1  1 
ATOM   5331 C  CG2  . VAL   B 1 77  ? 38.832 -20.813 11.250  1.00 18.63 ?  77  VAL   B CG2  1 
ATOM   5332 H  H    . VAL   B 1 77  ? 37.960 -18.251 11.096  1.00 19.03 ?  77  VAL   B H    1 
ATOM   5333 H  HA   . VAL   B 1 77  ? 38.579 -19.516 8.906   1.00 19.19 ?  77  VAL   B HA   1 
ATOM   5334 H  HB   . VAL   B 1 77  ? 36.832 -20.430 10.941  1.00 20.98 ?  77  VAL   B HB   1 
ATOM   5335 H  HG11 . VAL   B 1 77  ? 37.370 -22.601 10.081  1.00 21.90 ?  77  VAL   B HG11 1 
ATOM   5336 H  HG12 . VAL   B 1 77  ? 36.421 -21.744 9.141   1.00 21.90 ?  77  VAL   B HG12 1 
ATOM   5337 H  HG13 . VAL   B 1 77  ? 37.970 -21.867 8.808   1.00 21.90 ?  77  VAL   B HG13 1 
ATOM   5338 H  HG21 . VAL   B 1 77  ? 38.688 -21.611 11.780  1.00 22.34 ?  77  VAL   B HG21 1 
ATOM   5339 H  HG22 . VAL   B 1 77  ? 39.606 -20.923 10.680  1.00 22.34 ?  77  VAL   B HG22 1 
ATOM   5340 H  HG23 . VAL   B 1 77  ? 38.947 -20.044 11.827  1.00 22.34 ?  77  VAL   B HG23 1 
ATOM   5341 N  N    . GLY   B 1 78  ? 36.796 -19.398 7.253   1.00 13.88 ?  78  GLY   B N    1 
ATOM   5342 C  CA   . GLY   B 1 78  ? 35.821 -19.079 6.239   1.00 13.48 ?  78  GLY   B CA   1 
ATOM   5343 C  C    . GLY   B 1 78  ? 36.063 -17.763 5.540   1.00 12.83 ?  78  GLY   B C    1 
ATOM   5344 O  O    . GLY   B 1 78  ? 35.380 -17.475 4.551   1.00 13.36 ?  78  GLY   B O    1 
ATOM   5345 H  H    . GLY   B 1 78  ? 37.497 -19.790 6.940   1.00 16.64 ?  78  GLY   B H    1 
ATOM   5346 H  HA2  . GLY   B 1 78  ? 35.816 -19.773 5.567   1.00 16.15 ?  78  GLY   B HA2  1 
ATOM   5347 H  HA3  . GLY   B 1 78  ? 34.941 -19.039 6.645   1.00 16.15 ?  78  GLY   B HA3  1 
ATOM   5348 N  N    . GLY   B 1 79  ? 37.012 -16.959 6.029   1.00 12.85 ?  79  GLY   B N    1 
ATOM   5349 C  CA   . GLY   B 1 79  ? 37.314 -15.665 5.452   1.00 12.50 ?  79  GLY   B CA   1 
ATOM   5350 C  C    . GLY   B 1 79  ? 38.552 -15.686 4.561   1.00 12.10 ?  79  GLY   B C    1 
ATOM   5351 O  O    . GLY   B 1 79  ? 39.171 -16.718 4.313   1.00 12.58 ?  79  GLY   B O    1 
ATOM   5352 H  H    . GLY   B 1 79  ? 37.507 -17.148 6.704   1.00 15.40 ?  79  GLY   B H    1 
ATOM   5353 H  HA2  . GLY   B 1 79  ? 36.560 -15.360 4.919   1.00 14.98 ?  79  GLY   B HA2  1 
ATOM   5354 H  HA3  . GLY   B 1 79  ? 37.464 -15.019 6.160   1.00 14.98 ?  79  GLY   B HA3  1 
ATOM   5355 N  N    . SER   B 1 80  ? 38.919 -14.491 4.089   1.00 12.13 ?  80  SER   B N    1 
ATOM   5356 C  CA   . SER   B 1 80  ? 40.027 -14.355 3.152   1.00 11.98 ?  80  SER   B CA   1 
ATOM   5357 C  C    . SER   B 1 80  ? 40.606 -12.948 3.216   1.00 12.03 ?  80  SER   B C    1 
ATOM   5358 O  O    . SER   B 1 80  ? 39.986 -12.013 3.730   1.00 12.97 ?  80  SER   B O    1 
ATOM   5359 C  CB   . SER   B 1 80  ? 39.586 -14.636 1.710   1.00 12.54 ?  80  SER   B CB   1 
ATOM   5360 O  OG   . SER   B 1 80  ? 38.738 -13.614 1.209   1.00 13.48 ?  80  SER   B OG   1 
ATOM   5361 H  H    . SER   B 1 80  ? 38.545 -13.743 4.298   1.00 14.54 ?  80  SER   B H    1 
ATOM   5362 H  HA   . SER   B 1 80  ? 40.719 -14.985 3.397   1.00 14.36 ?  80  SER   B HA   1 
ATOM   5363 H  HB2  . SER   B 1 80  ? 40.374 -14.687 1.145   1.00 15.02 ?  80  SER   B HB2  1 
ATOM   5364 H  HB3  . SER   B 1 80  ? 39.108 -15.478 1.686   1.00 15.02 ?  80  SER   B HB3  1 
ATOM   5365 H  HG   . SER   B 1 80  ? 38.047 -13.552 1.693   1.00 16.15 ?  80  SER   B HG   1 
ATOM   5366 N  N    . CYS   B 1 81  ? 41.788 -12.803 2.626   1.00 11.83 ?  81  CYS   B N    1 
ATOM   5367 C  CA   . CYS   B 1 81  ? 42.339 -11.490 2.316   1.00 11.96 ?  81  CYS   B CA   1 
ATOM   5368 C  C    . CYS   B 1 81  ? 43.108 -11.580 1.007   1.00 11.34 ?  81  CYS   B C    1 
ATOM   5369 O  O    . CYS   B 1 81  ? 43.620 -12.642 0.637   1.00 12.25 ?  81  CYS   B O    1 
ATOM   5370 C  CB   . CYS   B 1 81  ? 43.239 -10.939 3.434   1.00 12.33 ?  81  CYS   B CB   1 
ATOM   5371 S  SG   . CYS   B 1 81  ? 44.752 -11.875 3.685   1.00 13.12 ?  81  CYS   B SG   1 
ATOM   5372 H  H    . CYS   B 1 81  ? 42.297 -13.456 2.384   1.00 14.17 ?  81  CYS   B H    1 
ATOM   5373 H  HA   . CYS   B 1 81  ? 41.606 -10.864 2.187   1.00 14.33 ?  81  CYS   B HA   1 
ATOM   5374 H  HB2  . CYS   B 1 81  ? 43.489 -10.028 3.215   1.00 14.77 ?  81  CYS   B HB2  1 
ATOM   5375 H  HB3  . CYS   B 1 81  ? 42.738 -10.947 4.268   1.00 14.77 ?  81  CYS   B HB3  1 
ATOM   5376 H  HG   . CYS   B 1 81  ? 45.376 -11.372 4.581   1.00 15.73 ?  81  CYS   B HG   1 
ATOM   5377 N  N    . VAL   B 1 82  ? 43.209 -10.437 0.330   1.00 11.70 ?  82  VAL   B N    1 
ATOM   5378 C  CA   . VAL   B 1 82  ? 43.980 -10.309 -0.905  1.00 11.94 ?  82  VAL   B CA   1 
ATOM   5379 C  C    . VAL   B 1 82  ? 45.321 -9.669  -0.585  1.00 12.24 ?  82  VAL   B C    1 
ATOM   5380 O  O    . VAL   B 1 82  ? 45.373 -8.549  -0.056  1.00 13.26 ?  82  VAL   B O    1 
ATOM   5381 C  CB   . VAL   B 1 82  ? 43.233 -9.473  -1.955  1.00 12.98 ?  82  VAL   B CB   1 
ATOM   5382 C  CG1  . VAL   B 1 82  ? 44.078 -9.315  -3.213  1.00 14.22 ?  82  VAL   B CG1  1 
ATOM   5383 C  CG2  . VAL   B 1 82  ? 41.882 -10.084 -2.272  1.00 13.95 ?  82  VAL   B CG2  1 
ATOM   5384 H  H    . VAL   B 1 82  ? 42.828 -9.699  0.570   1.00 14.02 ?  82  VAL   B H    1 
ATOM   5385 H  HA   . VAL   B 1 82  ? 44.143 -11.186 -1.276  1.00 14.30 ?  82  VAL   B HA   1 
ATOM   5386 H  HB   . VAL   B 1 82  ? 43.073 -8.590  -1.598  1.00 15.55 ?  82  VAL   B HB   1 
ATOM   5387 H  HG11 . VAL   B 1 82  ? 43.513 -8.996  -3.937  1.00 17.04 ?  82  VAL   B HG11 1 
ATOM   5388 H  HG12 . VAL   B 1 82  ? 44.783 -8.667  -3.042  1.00 17.04 ?  82  VAL   B HG12 1 
ATOM   5389 H  HG13 . VAL   B 1 82  ? 44.464 -10.171 -3.449  1.00 17.04 ?  82  VAL   B HG13 1 
ATOM   5390 H  HG21 . VAL   B 1 82  ? 41.449 -9.563  -2.968  1.00 16.72 ?  82  VAL   B HG21 1 
ATOM   5391 H  HG22 . VAL   B 1 82  ? 42.007 -10.999 -2.579  1.00 16.72 ?  82  VAL   B HG22 1 
ATOM   5392 H  HG23 . VAL   B 1 82  ? 41.334 -10.081 -1.471  1.00 16.72 ?  82  VAL   B HG23 1 
ATOM   5393 N  N    . LEU   B 1 83  ? 46.402 -10.358 -0.948  1.00 11.51 ?  83  LEU   B N    1 
ATOM   5394 C  CA   . LEU   B 1 83  ? 47.760 -9.839  -0.831  1.00 11.81 ?  83  LEU   B CA   1 
ATOM   5395 C  C    . LEU   B 1 83  ? 48.463 -9.981  -2.182  1.00 11.67 ?  83  LEU   B C    1 
ATOM   5396 O  O    . LEU   B 1 83  ? 47.866 -10.400 -3.177  1.00 11.55 ?  83  LEU   B O    1 
ATOM   5397 C  CB   . LEU   B 1 83  ? 48.507 -10.517 0.325   1.00 12.66 ?  83  LEU   B CB   1 
ATOM   5398 C  CG   . LEU   B 1 83  ? 48.003 -10.157 1.726   1.00 13.36 ?  83  LEU   B CG   1 
ATOM   5399 C  CD1  . LEU   B 1 83  ? 48.623 -11.032 2.794   1.00 14.40 ?  83  LEU   B CD1  1 
ATOM   5400 C  CD2  . LEU   B 1 83  ? 48.227 -8.680  2.049   1.00 14.42 ?  83  LEU   B CD2  1 
ATOM   5401 H  H    . LEU   B 1 83  ? 46.364 -11.154 -1.272  1.00 13.79 ?  83  LEU   B H    1 
ATOM   5402 H  HA   . LEU   B 1 83  ? 47.708 -8.896  -0.633  1.00 14.15 ?  83  LEU   B HA   1 
ATOM   5403 H  HB2  . LEU   B 1 83  ? 48.428 -11.477 0.221   1.00 15.17 ?  83  LEU   B HB2  1 
ATOM   5404 H  HB3  . LEU   B 1 83  ? 49.441 -10.261 0.272   1.00 15.17 ?  83  LEU   B HB3  1 
ATOM   5405 H  HG   . LEU   B 1 83  ? 47.049 -10.312 1.749   1.00 16.01 ?  83  LEU   B HG   1 
ATOM   5406 H  HD11 . LEU   B 1 83  ? 48.267 -10.775 3.661   1.00 17.26 ?  83  LEU   B HD11 1 
ATOM   5407 H  HD12 . LEU   B 1 83  ? 48.396 -11.961 2.613   1.00 17.26 ?  83  LEU   B HD12 1 
ATOM   5408 H  HD13 . LEU   B 1 83  ? 49.584 -10.920 2.785   1.00 17.26 ?  83  LEU   B HD13 1 
ATOM   5409 H  HD21 . LEU   B 1 83  ? 48.021 -8.529  2.983   1.00 17.29 ?  83  LEU   B HD21 1 
ATOM   5410 H  HD22 . LEU   B 1 83  ? 49.150 -8.453  1.868   1.00 17.29 ?  83  LEU   B HD22 1 
ATOM   5411 H  HD23 . LEU   B 1 83  ? 47.637 -8.146  1.490   1.00 17.29 ?  83  LEU   B HD23 1 
ATOM   5412 N  N    . SER   B 1 84  ? 49.738 -9.604  -2.234  1.00 12.77 ?  84  SER   B N    1 
ATOM   5413 C  CA   . SER   B 1 84  ? 50.470 -9.728  -3.485  1.00 12.89 ?  84  SER   B CA   1 
ATOM   5414 C  C    . SER   B 1 84  ? 50.622 -11.189 -3.900  1.00 11.85 ?  84  SER   B C    1 
ATOM   5415 O  O    . SER   B 1 84  ? 50.740 -12.087 -3.069  1.00 11.96 ?  84  SER   B O    1 
ATOM   5416 C  CB   . SER   B 1 84  ? 51.867 -9.129  -3.336  1.00 15.26 ?  84  SER   B CB   1 
ATOM   5417 O  OG   . SER   B 1 84  ? 52.610 -9.322  -4.526  1.00 16.42 ?  84  SER   B OG   1 
ATOM   5418 H  H    . SER   B 1 84  ? 50.183 -9.271  -1.579  1.00 15.30 ?  84  SER   B H    1 
ATOM   5419 H  HA   . SER   B 1 84  ? 50.003 -9.253  -4.187  1.00 15.44 ?  84  SER   B HA   1 
ATOM   5420 H  HB2  . SER   B 1 84  ? 51.787 -8.176  -3.155  1.00 18.29 ?  84  SER   B HB2  1 
ATOM   5421 H  HB3  . SER   B 1 84  ? 52.326 -9.566  -2.602  1.00 18.29 ?  84  SER   B HB3  1 
ATOM   5422 H  HG   . SER   B 1 84  ? 53.379 -8.980  -4.443  1.00 19.68 ?  84  SER   B HG   1 
ATOM   5423 N  N    . GLY   B 1 85  ? 50.692 -11.405 -5.206  1.00 13.00 ?  85  GLY   B N    1 
ATOM   5424 C  CA   . GLY   B 1 85  ? 51.040 -12.690 -5.759  1.00 13.85 ?  85  GLY   B CA   1 
ATOM   5425 C  C    . GLY   B 1 85  ? 52.511 -12.888 -6.056  1.00 12.93 ?  85  GLY   B C    1 
ATOM   5426 O  O    . GLY   B 1 85  ? 52.890 -13.968 -6.509  1.00 13.17 ?  85  GLY   B O    1 
ATOM   5427 H  H    . GLY   B 1 85  ? 50.543 -10.808 -5.799  1.00 15.58 ?  85  GLY   B H    1 
ATOM   5428 H  HA2  . GLY   B 1 85  ? 50.768 -13.387 -5.138  1.00 16.59 ?  85  GLY   B HA2  1 
ATOM   5429 H  HA3  . GLY   B 1 85  ? 50.553 -12.823 -6.584  1.00 16.59 ?  85  GLY   B HA3  1 
ATOM   5430 N  N    . HIS   B 1 86  ? 53.364 -11.893 -5.829  1.00 12.99 ?  86  HIS   B N    1 
ATOM   5431 C  CA   . HIS   B 1 86  ? 54.829 -12.060 -5.913  1.00 12.81 ?  86  HIS   B CA   1 
ATOM   5432 C  C    . HIS   B 1 86  ? 55.200 -12.573 -7.303  1.00 13.35 ?  86  HIS   B C    1 
ATOM   5433 O  O    . HIS   B 1 86  ? 54.817 -11.956 -8.308  1.00 14.27 ?  86  HIS   B O    1 
ATOM   5434 C  CB   . HIS   B 1 86  ? 55.324 -12.899 -4.741  1.00 13.39 ?  86  HIS   B CB   1 
ATOM   5435 C  CG   . HIS   B 1 86  ? 55.004 -12.296 -3.415  1.00 13.54 ?  86  HIS   B CG   1 
ATOM   5436 N  ND1  . HIS   B 1 86  ? 55.827 -11.379 -2.795  1.00 14.91 ?  86  HIS   B ND1  1 
ATOM   5437 C  CD2  . HIS   B 1 86  ? 53.934 -12.459 -2.601  1.00 13.69 ?  86  HIS   B CD2  1 
ATOM   5438 C  CE1  . HIS   B 1 86  ? 55.266 -10.996 -1.662  1.00 14.55 ?  86  HIS   B CE1  1 
ATOM   5439 N  NE2  . HIS   B 1 86  ? 54.117 -11.633 -1.521  1.00 13.89 ?  86  HIS   B NE2  1 
ATOM   5440 H  H    . HIS   B 1 86  ? 53.125 -11.097 -5.620  1.00 15.56 ?  86  HIS   B H    1 
ATOM   5441 H  HA   . HIS   B 1 86  ? 55.235 -11.185 -5.818  1.00 15.35 ?  86  HIS   B HA   1 
ATOM   5442 H  HB2  . HIS   B 1 86  ? 54.920 -13.777 -4.778  1.00 16.04 ?  86  HIS   B HB2  1 
ATOM   5443 H  HB3  . HIS   B 1 86  ? 56.295 -12.983 -4.797  1.00 16.04 ?  86  HIS   B HB3  1 
ATOM   5444 H  HD2  . HIS   B 1 86  ? 53.197 -13.011 -2.760  1.00 16.41 ?  86  HIS   B HD2  1 
ATOM   5445 H  HE1  . HIS   B 1 86  ? 55.625 -10.396 -1.049  1.00 17.44 ?  86  HIS   B HE1  1 
ATOM   5446 H  HE2  . HIS   B 1 86  ? 53.576 -11.561 -0.852  1.00 16.64 ?  86  HIS   B HE2  1 
ATOM   5447 N  N    . ASN   B 1 87  ? 55.967 -13.652 -7.411  1.00 13.53 ?  87  ASN   B N    1 
ATOM   5448 C  CA   . ASN   B 1 87  ? 56.354 -14.222 -8.692  1.00 14.38 ?  87  ASN   B CA   1 
ATOM   5449 C  C    . ASN   B 1 87  ? 55.372 -15.267 -9.191  1.00 13.85 ?  87  ASN   B C    1 
ATOM   5450 O  O    . ASN   B 1 87  ? 55.692 -15.981 -10.149 1.00 15.82 ?  87  ASN   B O    1 
ATOM   5451 C  CB   . ASN   B 1 87  ? 57.749 -14.847 -8.581  1.00 16.53 ?  87  ASN   B CB   1 
ATOM   5452 C  CG   . ASN   B 1 87  ? 57.814 -15.963 -7.539  1.00 17.56 ?  87  ASN   B CG   1 
ATOM   5453 O  OD1  . ASN   B 1 87  ? 57.178 -15.891 -6.480  1.00 16.84 ?  87  ASN   B OD1  1 
ATOM   5454 N  ND2  . ASN   B 1 87  ? 58.566 -17.021 -7.853  1.00 19.67 ?  87  ASN   B ND2  1 
ATOM   5455 H  H    . ASN   B 1 87  ? 56.281 -14.084 -6.739  1.00 16.21 ?  87  ASN   B H    1 
ATOM   5456 H  HA   . ASN   B 1 87  ? 56.394 -13.512 -9.353  1.00 17.23 ?  87  ASN   B HA   1 
ATOM   5457 H  HB2  . ASN   B 1 87  ? 57.995 -15.219 -9.444  1.00 19.82 ?  87  ASN   B HB2  1 
ATOM   5458 H  HB3  . ASN   B 1 87  ? 58.382 -14.158 -8.326  1.00 19.82 ?  87  ASN   B HB3  1 
ATOM   5459 H  HD21 . ASN   B 1 87  ? 58.637 -17.674 -7.304  1.00 23.58 ?  87  ASN   B HD21 1 
ATOM   5460 H  HD22 . ASN   B 1 87  ? 58.990 -17.040 -8.605  1.00 23.58 ?  87  ASN   B HD22 1 
ATOM   5461 N  N    . LEU   B 1 88  ? 54.195 -15.371 -8.568  1.00 12.92 ?  88  LEU   B N    1 
ATOM   5462 C  CA   . LEU   B 1 88  ? 53.216 -16.404 -8.894  1.00 13.26 ?  88  LEU   B CA   1 
ATOM   5463 C  C    . LEU   B 1 88  ? 51.986 -15.888 -9.620  1.00 13.01 ?  88  LEU   B C    1 
ATOM   5464 O  O    . LEU   B 1 88  ? 51.387 -16.637 -10.400 1.00 14.75 ?  88  LEU   B O    1 
ATOM   5465 C  CB   . LEU   B 1 88  ? 52.742 -17.091 -7.609  1.00 14.01 ?  88  LEU   B CB   1 
ATOM   5466 C  CG   . LEU   B 1 88  ? 53.860 -17.754 -6.814  1.00 16.46 ?  88  LEU   B CG   1 
ATOM   5467 C  CD1  . LEU   B 1 88  ? 53.361 -18.138 -5.432  1.00 17.51 ?  88  LEU   B CD1  1 
ATOM   5468 C  CD2  . LEU   B 1 88  ? 54.377 -18.962 -7.570  1.00 19.55 ?  88  LEU   B CD2  1 
ATOM   5469 H  H    . LEU   B 1 88  ? 53.938 -14.843 -7.930  1.00 15.48 ?  88  LEU   B H    1 
ATOM   5470 H  HA   . LEU   B 1 88  ? 53.630 -17.065 -9.453  1.00 15.89 ?  88  LEU   B HA   1 
ATOM   5471 H  HB2  . LEU   B 1 88  ? 52.316 -16.438 -7.032  1.00 16.79 ?  88  LEU   B HB2  1 
ATOM   5472 H  HB3  . LEU   B 1 88  ? 52.099 -17.784 -7.845  1.00 16.79 ?  88  LEU   B HB3  1 
ATOM   5473 H  HG   . LEU   B 1 88  ? 54.588 -17.123 -6.711  1.00 19.73 ?  88  LEU   B HG   1 
ATOM   5474 H  HD11 . LEU   B 1 88  ? 54.013 -18.722 -5.016  1.00 20.99 ?  88  LEU   B HD11 1 
ATOM   5475 H  HD12 . LEU   B 1 88  ? 53.247 -17.334 -4.904  1.00 20.99 ?  88  LEU   B HD12 1 
ATOM   5476 H  HD13 . LEU   B 1 88  ? 52.513 -18.599 -5.524  1.00 20.99 ?  88  LEU   B HD13 1 
ATOM   5477 H  HD21 . LEU   B 1 88  ? 55.012 -19.432 -7.009  1.00 23.44 ?  88  LEU   B HD21 1 
ATOM   5478 H  HD22 . LEU   B 1 88  ? 53.631 -19.541 -7.787  1.00 23.44 ?  88  LEU   B HD22 1 
ATOM   5479 H  HD23 . LEU   B 1 88  ? 54.813 -18.663 -8.384  1.00 23.44 ?  88  LEU   B HD23 1 
ATOM   5480 N  N    . ALA   B 1 89  ? 51.577 -14.654 -9.355  1.00 11.99 ?  89  ALA   B N    1 
ATOM   5481 C  CA   . ALA   B 1 89  ? 50.286 -14.158 -9.804  1.00 11.73 ?  89  ALA   B CA   1 
ATOM   5482 C  C    . ALA   B 1 89  ? 50.265 -12.663 -9.523  1.00 12.21 ?  89  ALA   B C    1 
ATOM   5483 O  O    . ALA   B 1 89  ? 51.106 -12.145 -8.786  1.00 13.20 ?  89  ALA   B O    1 
ATOM   5484 C  CB   . ALA   B 1 89  ? 49.145 -14.833 -9.049  1.00 12.25 ?  89  ALA   B CB   1 
ATOM   5485 H  H    . ALA   B 1 89  ? 52.026 -14.072 -8.900  1.00 14.37 ?  89  ALA   B H    1 
ATOM   5486 H  HA   . ALA   B 1 89  ? 50.176 -14.306 -10.759 1.00 14.05 ?  89  ALA   B HA   1 
ATOM   5487 H  HB1  . ALA   B 1 89  ? 48.297 -14.500 -9.392  1.00 14.67 ?  89  ALA   B HB1  1 
ATOM   5488 H  HB2  . ALA   B 1 89  ? 49.200 -15.792 -9.193  1.00 14.67 ?  89  ALA   B HB2  1 
ATOM   5489 H  HB3  . ALA   B 1 89  ? 49.226 -14.632 -8.109  1.00 14.67 ?  89  ALA   B HB3  1 
ATOM   5490 N  N    . LYS   B 1 90  ? 49.270 -11.973 -10.080 1.00 13.14 ?  90  LYS   B N    1 
ATOM   5491 C  CA   . LYS   B 1 90  ? 49.083 -10.583 -9.678  1.00 13.53 ?  90  LYS   B CA   1 
ATOM   5492 C  C    . LYS   B 1 90  ? 48.760 -10.508 -8.188  1.00 13.42 ?  90  LYS   B C    1 
ATOM   5493 O  O    . LYS   B 1 90  ? 49.396 -9.755  -7.438  1.00 14.22 ?  90  LYS   B O    1 
ATOM   5494 C  CB   . LYS   B 1 90  ? 47.996 -9.929  -10.528 1.00 15.12 ?  90  LYS   B CB   1 
ATOM   5495 C  CG   . LYS   B 1 90  ? 47.714 -8.484  -10.153 1.00 15.35 ?  90  LYS   B CG   1 
ATOM   5496 C  CD   . LYS   B 1 90  ? 48.934 -7.595  -10.231 1.00 18.33 ?  90  LYS   B CD   1 
ATOM   5497 C  CE   . LYS   B 1 90  ? 48.505 -6.161  -10.020 1.00 20.82 ?  90  LYS   B CE   1 
ATOM   5498 N  NZ   . LYS   B 1 90  ? 49.664 -5.245  -9.878  1.00 20.53 ?  90  LYS   B NZ   1 
ATOM   5499 H  H    . LYS   B 1 90  ? 48.712 -12.279 -10.659 1.00 15.74 ?  90  LYS   B H    1 
ATOM   5500 H  HA   . LYS   B 1 90  ? 49.907 -10.108 -9.827  1.00 16.22 ?  90  LYS   B HA   1 
ATOM   5501 H  HB2  . LYS   B 1 90  ? 48.278 -9.943  -11.459 1.00 18.13 ?  90  LYS   B HB2  1 
ATOM   5502 H  HB3  . LYS   B 1 90  ? 47.170 -10.430 -10.432 1.00 18.13 ?  90  LYS   B HB3  1 
ATOM   5503 H  HG2  . LYS   B 1 90  ? 47.046 -8.128  -10.762 1.00 18.40 ?  90  LYS   B HG2  1 
ATOM   5504 H  HG3  . LYS   B 1 90  ? 47.373 -8.455  -9.243  1.00 18.40 ?  90  LYS   B HG3  1 
ATOM   5505 H  HD2  . LYS   B 1 90  ? 49.562 -7.840  -9.530  1.00 21.98 ?  90  LYS   B HD2  1 
ATOM   5506 H  HD3  . LYS   B 1 90  ? 49.346 -7.679  -11.104 1.00 21.98 ?  90  LYS   B HD3  1 
ATOM   5507 H  HE2  . LYS   B 1 90  ? 47.986 -5.864  -10.786 1.00 24.96 ?  90  LYS   B HE2  1 
ATOM   5508 H  HE3  . LYS   B 1 90  ? 47.975 -6.094  -9.212  1.00 24.96 ?  90  LYS   B HE3  1 
ATOM   5509 H  HZ1  . LYS   B 1 90  ? 49.385 -4.408  -9.759  1.00 24.62 ?  90  LYS   B HZ1  1 
ATOM   5510 H  HZ2  . LYS   B 1 90  ? 50.161 -5.485  -9.179  1.00 24.62 ?  90  LYS   B HZ2  1 
ATOM   5511 H  HZ3  . LYS   B 1 90  ? 50.171 -5.275  -10.612 1.00 24.62 ?  90  LYS   B HZ3  1 
ATOM   5512 N  N    . HIS   B 1 91  ? 47.803 -11.327 -7.739  1.00 11.57 ?  91  HIS   B N    1 
ATOM   5513 C  CA   . HIS   B 1 91  ? 47.345 -11.346 -6.364  1.00 11.96 ?  91  HIS   B CA   1 
ATOM   5514 C  C    . HIS   B 1 91  ? 47.337 -12.776 -5.846  1.00 11.22 ?  91  HIS   B C    1 
ATOM   5515 O  O    . HIS   B 1 91  ? 47.104 -13.730 -6.600  1.00 11.58 ?  91  HIS   B O    1 
ATOM   5516 C  CB   . HIS   B 1 91  ? 45.888 -10.872 -6.258  1.00 13.52 ?  91  HIS   B CB   1 
ATOM   5517 C  CG   . HIS   B 1 91  ? 45.673 -9.464  -6.699  1.00 17.21 ?  91  HIS   B CG   1 
ATOM   5518 N  ND1  . HIS   B 1 91  ? 46.271 -8.384  -6.083  1.00 19.69 ?  91  HIS   B ND1  1 
ATOM   5519 C  CD2  . HIS   B 1 91  ? 44.897 -8.954  -7.681  1.00 19.18 ?  91  HIS   B CD2  1 
ATOM   5520 C  CE1  . HIS   B 1 91  ? 45.887 -7.269  -6.681  1.00 20.89 ?  91  HIS   B CE1  1 
ATOM   5521 N  NE2  . HIS   B 1 91  ? 45.046 -7.588  -7.649  1.00 20.75 ?  91  HIS   B NE2  1 
ATOM   5522 H  H    . HIS   B 1 91  ? 47.386 -11.894 -8.234  1.00 13.87 ?  91  HIS   B H    1 
ATOM   5523 H  HA   . HIS   B 1 91  ? 47.910 -10.788 -5.798  1.00 14.33 ?  91  HIS   B HA   1 
ATOM   5524 H  HB2  . HIS   B 1 91  ? 45.334 -11.444 -6.810  1.00 16.21 ?  91  HIS   B HB2  1 
ATOM   5525 H  HB3  . HIS   B 1 91  ? 45.602 -10.939 -5.330  1.00 16.21 ?  91  HIS   B HB3  1 
ATOM   5526 H  HD1  . HIS   B 1 91  ? 46.815 -8.433  -5.416  1.00 23.60 ?  91  HIS   B HD1  1 
ATOM   5527 H  HD2  . HIS   B 1 91  ? 44.368 -9.431  -8.275  1.00 22.99 ?  91  HIS   B HD2  1 
ATOM   5528 H  HE1  . HIS   B 1 91  ? 46.160 -6.410  -6.449  1.00 25.05 ?  91  HIS   B HE1  1 
ATOM   5529 N  N    . CYS   B 1 92  ? 47.535 -12.912 -4.541  1.00 11.03 ?  92  CYS   B N    1 
ATOM   5530 C  CA   . CYS   B 1 92  ? 47.229 -14.148 -3.830  1.00 10.72 ?  92  CYS   B CA   1 
ATOM   5531 C  C    . CYS   B 1 92  ? 46.005 -13.911 -2.950  1.00 10.61 ?  92  CYS   B C    1 
ATOM   5532 O  O    . CYS   B 1 92  ? 46.007 -13.010 -2.099  1.00 11.41 ?  92  CYS   B O    1 
ATOM   5533 C  CB   . CYS   B 1 92  ? 48.407 -14.600 -2.973  1.00 11.57 ?  92  CYS   B CB   1 
ATOM   5534 S  SG   . CYS   B 1 92  ? 48.048 -16.140 -2.082  1.00 11.40 ?  92  CYS   B SG   1 
ATOM   5535 H  H    . CYS   B 1 92  ? 47.866 -12.297 -4.032  1.00 13.21 ?  92  CYS   B H    1 
ATOM   5536 H  HA   . CYS   B 1 92  ? 47.032 -14.848 -4.473  1.00 12.85 ?  92  CYS   B HA   1 
ATOM   5537 H  HB2  . CYS   B 1 92  ? 49.175 -14.752 -3.537  1.00 13.86 ?  92  CYS   B HB2  1 
ATOM   5538 H  HB3  . CYS   B 1 92  ? 48.599 -13.911 -2.316  1.00 13.86 ?  92  CYS   B HB3  1 
ATOM   5539 H  HG   . CYS   B 1 92  ? 49.016 -16.452 -1.445  1.00 13.66 ?  92  CYS   B HG   1 
ATOM   5540 N  N    . LEU   B 1 93  ? 44.966 -14.717 -3.164  1.00 10.42 ?  93  LEU   B N    1 
ATOM   5541 C  CA   . LEU   B 1 93  ? 43.787 -14.737 -2.305  1.00 10.79 ?  93  LEU   B CA   1 
ATOM   5542 C  C    . LEU   B 1 93  ? 44.012 -15.799 -1.232  1.00 10.42 ?  93  LEU   B C    1 
ATOM   5543 O  O    . LEU   B 1 93  ? 43.963 -17.002 -1.517  1.00 10.72 ?  93  LEU   B O    1 
ATOM   5544 C  CB   . LEU   B 1 93  ? 42.523 -15.024 -3.115  1.00 11.43 ?  93  LEU   B CB   1 
ATOM   5545 C  CG   . LEU   B 1 93  ? 41.226 -15.040 -2.301  1.00 11.87 ?  93  LEU   B CG   1 
ATOM   5546 C  CD1  . LEU   B 1 93  ? 40.875 -13.657 -1.798  1.00 12.07 ?  93  LEU   B CD1  1 
ATOM   5547 C  CD2  . LEU   B 1 93  ? 40.103 -15.624 -3.136  1.00 11.76 ?  93  LEU   B CD2  1 
ATOM   5548 H  H    . LEU   B 1 93  ? 44.922 -15.287 -3.819  1.00 12.49 ?  93  LEU   B H    1 
ATOM   5549 H  HA   . LEU   B 1 93  ? 43.692 -13.872 -1.877  1.00 12.93 ?  93  LEU   B HA   1 
ATOM   5550 H  HB2  . LEU   B 1 93  ? 42.431 -14.335 -3.796  1.00 13.70 ?  93  LEU   B HB2  1 
ATOM   5551 H  HB3  . LEU   B 1 93  ? 42.617 -15.888 -3.538  1.00 13.70 ?  93  LEU   B HB3  1 
ATOM   5552 H  HG   . LEU   B 1 93  ? 41.349 -15.613 -1.533  1.00 14.22 ?  93  LEU   B HG   1 
ATOM   5553 H  HD11 . LEU   B 1 93  ? 40.021 -13.696 -1.343  1.00 14.46 ?  93  LEU   B HD11 1 
ATOM   5554 H  HD12 . LEU   B 1 93  ? 41.565 -13.357 -1.188  1.00 14.46 ?  93  LEU   B HD12 1 
ATOM   5555 H  HD13 . LEU   B 1 93  ? 40.817 -13.050 -2.556  1.00 14.46 ?  93  LEU   B HD13 1 
ATOM   5556 H  HD21 . LEU   B 1 93  ? 39.287 -15.623 -2.612  1.00 14.09 ?  93  LEU   B HD21 1 
ATOM   5557 H  HD22 . LEU   B 1 93  ? 39.984 -15.085 -3.934  1.00 14.09 ?  93  LEU   B HD22 1 
ATOM   5558 H  HD23 . LEU   B 1 93  ? 40.333 -16.535 -3.386  1.00 14.09 ?  93  LEU   B HD23 1 
ATOM   5559 N  N    . HIS   B 1 94  ? 44.296 -15.361 -0.009  1.00 10.38 ?  94  HIS   B N    1 
ATOM   5560 C  CA   . HIS   B 1 94  ? 44.512 -16.264 1.114   1.00 10.39 ?  94  HIS   B CA   1 
ATOM   5561 C  C    . HIS   B 1 94  ? 43.149 -16.618 1.690   1.00 10.82 ?  94  HIS   B C    1 
ATOM   5562 O  O    . HIS   B 1 94  ? 42.481 -15.747 2.247   1.00 12.31 ?  94  HIS   B O    1 
ATOM   5563 C  CB   . HIS   B 1 94  ? 45.387 -15.587 2.169   1.00 11.04 ?  94  HIS   B CB   1 
ATOM   5564 C  CG   . HIS   B 1 94  ? 46.772 -15.286 1.697   1.00 10.93 ?  94  HIS   B CG   1 
ATOM   5565 N  ND1  . HIS   B 1 94  ? 47.801 -16.198 1.788   1.00 11.02 ?  94  HIS   B ND1  1 
ATOM   5566 C  CD2  . HIS   B 1 94  ? 47.283 -14.178 1.104   1.00 11.08 ?  94  HIS   B CD2  1 
ATOM   5567 C  CE1  . HIS   B 1 94  ? 48.888 -15.651 1.273   1.00 11.15 ?  94  HIS   B CE1  1 
ATOM   5568 N  NE2  . HIS   B 1 94  ? 48.604 -14.430 0.852   1.00 11.26 ?  94  HIS   B NE2  1 
ATOM   5569 H  H    . HIS   B 1 94  ? 44.380 -14.524 0.195   1.00 12.43 ?  94  HIS   B H    1 
ATOM   5570 H  HA   . HIS   B 1 94  ? 44.952 -17.073 0.805   1.00 12.45 ?  94  HIS   B HA   1 
ATOM   5571 H  HB2  . HIS   B 1 94  ? 44.975 -14.753 2.427   1.00 13.23 ?  94  HIS   B HB2  1 
ATOM   5572 H  HB3  . HIS   B 1 94  ? 45.460 -16.177 2.934   1.00 13.23 ?  94  HIS   B HB3  1 
ATOM   5573 H  HD2  . HIS   B 1 94  ? 46.825 -13.397 0.902   1.00 13.28 ?  94  HIS   B HD2  1 
ATOM   5574 H  HE1  . HIS   B 1 94  ? 49.721 -16.067 1.218   1.00 13.35 ?  94  HIS   B HE1  1 
ATOM   5575 H  HE2  . HIS   B 1 94  ? 49.161 -13.891 0.485   1.00 13.49 ?  94  HIS   B HE2  1 
ATOM   5576 N  N    . VAL   B 1 95  ? 42.718 -17.874 1.543   1.00 10.44 ?  95  VAL   B N    1 
ATOM   5577 C  CA   . VAL   B 1 95  ? 41.392 -18.316 1.975   1.00 10.82 ?  95  VAL   B CA   1 
ATOM   5578 C  C    . VAL   B 1 95  ? 41.559 -19.351 3.072   1.00 11.30 ?  95  VAL   B C    1 
ATOM   5579 O  O    . VAL   B 1 95  ? 42.333 -20.299 2.913   1.00 11.57 ?  95  VAL   B O    1 
ATOM   5580 C  CB   . VAL   B 1 95  ? 40.575 -18.922 0.818   1.00 11.00 ?  95  VAL   B CB   1 
ATOM   5581 C  CG1  . VAL   B 1 95  ? 39.193 -19.366 1.304   1.00 12.44 ?  95  VAL   B CG1  1 
ATOM   5582 C  CG2  . VAL   B 1 95  ? 40.447 -17.936 -0.323  1.00 11.33 ?  95  VAL   B CG2  1 
ATOM   5583 H  H    . VAL   B 1 95  ? 43.181 -18.505 1.183   1.00 12.51 ?  95  VAL   B H    1 
ATOM   5584 H  HA   . VAL   B 1 95  ? 40.895 -17.563 2.337   1.00 12.96 ?  95  VAL   B HA   1 
ATOM   5585 H  HB   . VAL   B 1 95  ? 41.037 -19.703 0.482   1.00 13.18 ?  95  VAL   B HB   1 
ATOM   5586 H  HG11 . VAL   B 1 95  ? 38.631 -19.564 0.532   1.00 14.90 ?  95  VAL   B HG11 1 
ATOM   5587 H  HG12 . VAL   B 1 95  ? 39.282 -20.163 1.850   1.00 14.90 ?  95  VAL   B HG12 1 
ATOM   5588 H  HG13 . VAL   B 1 95  ? 38.788 -18.652 1.823   1.00 14.90 ?  95  VAL   B HG13 1 
ATOM   5589 H  HG21 . VAL   B 1 95  ? 39.872 -18.318 -1.004  1.00 13.57 ?  95  VAL   B HG21 1 
ATOM   5590 H  HG22 . VAL   B 1 95  ? 40.055 -17.115 0.016   1.00 13.57 ?  95  VAL   B HG22 1 
ATOM   5591 H  HG23 . VAL   B 1 95  ? 41.325 -17.761 -0.686  1.00 13.57 ?  95  VAL   B HG23 1 
ATOM   5592 N  N    . VAL   B 1 96  ? 40.821 -19.187 4.166   1.00 11.58 ?  96  VAL   B N    1 
ATOM   5593 C  CA   . VAL   B 1 96  ? 40.906 -20.098 5.307   1.00 11.87 ?  96  VAL   B CA   1 
ATOM   5594 C  C    . VAL   B 1 96  ? 39.718 -21.057 5.262   1.00 12.61 ?  96  VAL   B C    1 
ATOM   5595 O  O    . VAL   B 1 96  ? 38.599 -20.702 5.646   1.00 13.18 ?  96  VAL   B O    1 
ATOM   5596 C  CB   . VAL   B 1 96  ? 40.959 -19.350 6.643   1.00 12.64 ?  96  VAL   B CB   1 
ATOM   5597 C  CG1  . VAL   B 1 96  ? 41.148 -20.346 7.786   1.00 13.67 ?  96  VAL   B CG1  1 
ATOM   5598 C  CG2  . VAL   B 1 96  ? 42.067 -18.307 6.650   1.00 13.55 ?  96  VAL   B CG2  1 
ATOM   5599 H  H    . VAL   B 1 96  ? 40.254 -18.551 4.278   1.00 13.87 ?  96  VAL   B H    1 
ATOM   5600 H  HA   . VAL   B 1 96  ? 41.720 -20.624 5.233   1.00 14.22 ?  96  VAL   B HA   1 
ATOM   5601 H  HB   . VAL   B 1 96  ? 40.115 -18.895 6.786   1.00 15.15 ?  96  VAL   B HB   1 
ATOM   5602 H  HG11 . VAL   B 1 96  ? 41.337 -19.856 8.606   1.00 16.38 ?  96  VAL   B HG11 1 
ATOM   5603 H  HG12 . VAL   B 1 96  ? 40.344 -20.871 7.896   1.00 16.38 ?  96  VAL   B HG12 1 
ATOM   5604 H  HG13 . VAL   B 1 96  ? 41.900 -20.928 7.579   1.00 16.38 ?  96  VAL   B HG13 1 
ATOM   5605 H  HG21 . VAL   B 1 96  ? 42.114 -17.896 7.530   1.00 16.24 ?  96  VAL   B HG21 1 
ATOM   5606 H  HG22 . VAL   B 1 96  ? 42.911 -18.735 6.442   1.00 16.24 ?  96  VAL   B HG22 1 
ATOM   5607 H  HG23 . VAL   B 1 96  ? 41.867 -17.628 5.984   1.00 16.24 ?  96  VAL   B HG23 1 
ATOM   5608 N  N    . GLY   B 1 97  ? 39.951 -22.288 4.820   1.00 12.21 ?  97  GLY   B N    1 
ATOM   5609 C  CA   . GLY   B 1 97  ? 38.975 -23.344 4.978   1.00 13.09 ?  97  GLY   B CA   1 
ATOM   5610 C  C    . GLY   B 1 97  ? 39.098 -23.959 6.355   1.00 14.12 ?  97  GLY   B C    1 
ATOM   5611 O  O    . GLY   B 1 97  ? 40.140 -23.836 7.014   1.00 14.54 ?  97  GLY   B O    1 
ATOM   5612 H  H    . GLY   B 1 97  ? 40.680 -22.534 4.426   1.00 14.63 ?  97  GLY   B H    1 
ATOM   5613 H  HA2  . GLY   B 1 97  ? 38.082 -22.974 4.862   1.00 15.69 ?  97  GLY   B HA2  1 
ATOM   5614 H  HA3  . GLY   B 1 97  ? 39.117 -24.026 4.301   1.00 15.69 ?  97  GLY   B HA3  1 
ATOM   5615 N  N    . PRO   B 1 98  ? 38.051 -24.642 6.818   1.00 14.57 ?  98  PRO   B N    1 
ATOM   5616 C  CA   . PRO   B 1 98  ? 38.150 -25.338 8.103   1.00 15.32 ?  98  PRO   B CA   1 
ATOM   5617 C  C    . PRO   B 1 98  ? 39.179 -26.457 8.052   1.00 15.21 ?  98  PRO   B C    1 
ATOM   5618 O  O    . PRO   B 1 98  ? 39.281 -27.193 7.071   1.00 15.82 ?  98  PRO   B O    1 
ATOM   5619 C  CB   . PRO   B 1 98  ? 36.733 -25.884 8.314   1.00 16.07 ?  98  PRO   B CB   1 
ATOM   5620 C  CG   . PRO   B 1 98  ? 36.162 -26.010 6.945   1.00 15.69 ?  98  PRO   B CG   1 
ATOM   5621 C  CD   . PRO   B 1 98  ? 36.726 -24.825 6.195   1.00 14.80 ?  98  PRO   B CD   1 
ATOM   5622 H  HA   . PRO   B 1 98  ? 38.373 -24.717 8.808   1.00 18.37 ?  98  PRO   B HA   1 
ATOM   5623 H  HB2  . PRO   B 1 98  ? 36.780 -26.752 8.748   1.00 19.26 ?  98  PRO   B HB2  1 
ATOM   5624 H  HB3  . PRO   B 1 98  ? 36.217 -25.261 8.843   1.00 19.26 ?  98  PRO   B HB3  1 
ATOM   5625 H  HG2  . PRO   B 1 98  ? 36.455 -26.848 6.542   1.00 18.81 ?  98  PRO   B HG2  1 
ATOM   5626 H  HG3  . PRO   B 1 98  ? 35.195 -25.971 6.986   1.00 18.81 ?  98  PRO   B HG3  1 
ATOM   5627 H  HD2  . PRO   B 1 98  ? 36.814 -25.035 5.248   1.00 17.74 ?  98  PRO   B HD2  1 
ATOM   5628 H  HD3  . PRO   B 1 98  ? 36.173 -24.042 6.334   1.00 17.74 ?  98  PRO   B HD3  1 
ATOM   5629 N  N    . ASN   B 1 99  ? 39.934 -26.585 9.134   1.00 16.39 ?  99  ASN   B N    1 
ATOM   5630 C  CA   . ASN   B 1 99  ? 40.913 -27.656 9.298   1.00 17.34 ?  99  ASN   B CA   1 
ATOM   5631 C  C    . ASN   B 1 99  ? 40.284 -28.740 10.174  1.00 19.95 ?  99  ASN   B C    1 
ATOM   5632 O  O    . ASN   B 1 99  ? 40.206 -28.597 11.397  1.00 20.65 ?  99  ASN   B O    1 
ATOM   5633 C  CB   . ASN   B 1 99  ? 42.186 -27.098 9.922   1.00 17.57 ?  99  ASN   B CB   1 
ATOM   5634 C  CG   . ASN   B 1 99  ? 43.314 -28.108 9.943   1.00 18.66 ?  99  ASN   B CG   1 
ATOM   5635 O  OD1  . ASN   B 1 99  ? 43.084 -29.296 10.118  1.00 19.39 ?  99  ASN   B OD1  1 
ATOM   5636 N  ND2  . ASN   B 1 99  ? 44.536 -27.640 9.752   1.00 18.84 ?  99  ASN   B ND2  1 
ATOM   5637 H  H    . ASN   B 1 99  ? 39.898 -26.047 9.801   1.00 19.64 ?  99  ASN   B H    1 
ATOM   5638 H  HA   . ASN   B 1 99  ? 41.128 -28.042 8.435   1.00 20.79 ?  99  ASN   B HA   1 
ATOM   5639 H  HB2  . ASN   B 1 99  ? 42.476 -26.332 9.414   1.00 21.06 ?  99  ASN   B HB2  1 
ATOM   5640 H  HB3  . ASN   B 1 99  ? 41.994 -26.842 10.841  1.00 21.06 ?  99  ASN   B HB3  1 
ATOM   5641 H  HD21 . ASN   B 1 99  ? 45.206 -28.175 9.753   1.00 22.58 ?  99  ASN   B HD21 1 
ATOM   5642 H  HD22 . ASN   B 1 99  ? 44.652 -26.798 9.630   1.00 22.58 ?  99  ASN   B HD22 1 
ATOM   5643 N  N    A VAL   B 1 100 ? 39.813 -29.818 9.541   0.70 21.67 ?  100 VAL   B N    1 
ATOM   5644 N  N    B VAL   B 1 100 ? 39.827 -29.821 9.534   0.30 21.84 ?  100 VAL   B N    1 
ATOM   5645 C  CA   A VAL   B 1 100 ? 39.196 -30.912 10.291  0.70 24.48 ?  100 VAL   B CA   1 
ATOM   5646 C  CA   B VAL   B 1 100 ? 39.204 -30.925 10.260  0.30 24.10 ?  100 VAL   B CA   1 
ATOM   5647 C  C    A VAL   B 1 100 ? 40.203 -31.583 11.217  0.70 24.77 ?  100 VAL   B C    1 
ATOM   5648 C  C    B VAL   B 1 100 ? 40.199 -31.591 11.201  0.30 24.65 ?  100 VAL   B C    1 
ATOM   5649 O  O    A VAL   B 1 100 ? 39.830 -32.105 12.275  0.70 25.25 ?  100 VAL   B O    1 
ATOM   5650 O  O    B VAL   B 1 100 ? 39.817 -32.102 12.261  0.30 24.97 ?  100 VAL   B O    1 
ATOM   5651 C  CB   A VAL   B 1 100 ? 38.531 -31.918 9.330   0.70 26.92 ?  100 VAL   B CB   1 
ATOM   5652 C  CB   B VAL   B 1 100 ? 38.582 -31.926 9.265   0.30 25.72 ?  100 VAL   B CB   1 
ATOM   5653 C  CG1  A VAL   B 1 100 ? 38.044 -33.143 10.091  0.70 27.51 ?  100 VAL   B CG1  1 
ATOM   5654 C  CG1  B VAL   B 1 100 ? 38.075 -33.166 9.988   0.30 26.13 ?  100 VAL   B CG1  1 
ATOM   5655 C  CG2  A VAL   B 1 100 ? 37.378 -31.258 8.592   0.70 27.43 ?  100 VAL   B CG2  1 
ATOM   5656 C  CG2  B VAL   B 1 100 ? 37.455 -31.264 8.487   0.30 26.05 ?  100 VAL   B CG2  1 
ATOM   5657 H  H    A VAL   B 1 100 ? 39.821 -29.927 8.685   0.70 25.99 ?  100 VAL   B H    1 
ATOM   5658 H  H    B VAL   B 1 100 ? 39.861 -29.932 8.681   0.30 26.19 ?  100 VAL   B H    1 
ATOM   5659 H  HA   A VAL   B 1 100 ? 38.490 -30.539 10.844  0.70 29.36 ?  100 VAL   B HA   1 
ATOM   5660 H  HA   B VAL   B 1 100 ? 38.482 -30.571 10.801  0.30 28.90 ?  100 VAL   B HA   1 
ATOM   5661 H  HB   A VAL   B 1 100 ? 39.183 -32.214 8.677   0.70 32.29 ?  100 VAL   B HB   1 
ATOM   5662 H  HB   B VAL   B 1 100 ? 39.260 -32.207 8.631   0.30 30.85 ?  100 VAL   B HB   1 
ATOM   5663 H  HG11 A VAL   B 1 100 ? 37.443 -33.650 9.521   0.70 32.99 ?  100 VAL   B HG11 1 
ATOM   5664 H  HG11 B VAL   B 1 100 ? 37.504 -33.670 9.385   0.30 31.34 ?  100 VAL   B HG11 1 
ATOM   5665 H  HG12 A VAL   B 1 100 ? 38.805 -33.693 10.336  0.70 32.99 ?  100 VAL   B HG12 1 
ATOM   5666 H  HG12 B VAL   B 1 100 ? 38.831 -33.711 10.256  0.30 31.34 ?  100 VAL   B HG12 1 
ATOM   5667 H  HG13 A VAL   B 1 100 ? 37.572 -32.855 10.889  0.70 32.99 ?  100 VAL   B HG13 1 
ATOM   5668 H  HG13 B VAL   B 1 100 ? 37.567 -32.892 10.767  0.30 31.34 ?  100 VAL   B HG13 1 
ATOM   5669 H  HG21 A VAL   B 1 100 ? 36.972 -31.909 7.997   0.70 32.89 ?  100 VAL   B HG21 1 
ATOM   5670 H  HG21 B VAL   B 1 100 ? 37.066 -31.914 7.881   0.30 31.23 ?  100 VAL   B HG21 1 
ATOM   5671 H  HG22 A VAL   B 1 100 ? 36.724 -30.951 9.240   0.70 32.89 ?  100 VAL   B HG22 1 
ATOM   5672 H  HG22 B VAL   B 1 100 ? 36.783 -30.950 9.112   0.30 31.23 ?  100 VAL   B HG22 1 
ATOM   5673 H  HG23 A VAL   B 1 100 ? 37.718 -30.509 8.082   0.70 32.89 ?  100 VAL   B HG23 1 
ATOM   5674 H  HG23 B VAL   B 1 100 ? 37.815 -30.518 7.984   0.30 31.23 ?  100 VAL   B HG23 1 
ATOM   5675 N  N    . ASN   B 1 101 ? 41.483 -31.609 10.833  1.00 24.95 ?  101 ASN   B N    1 
ATOM   5676 C  CA   . ASN   B 1 101 ? 42.516 -32.150 11.715  1.00 27.05 ?  101 ASN   B CA   1 
ATOM   5677 C  C    . ASN   B 1 101 ? 42.713 -31.315 12.974  1.00 28.51 ?  101 ASN   B C    1 
ATOM   5678 O  O    . ASN   B 1 101 ? 43.357 -31.791 13.918  1.00 30.00 ?  101 ASN   B O    1 
ATOM   5679 C  CB   . ASN   B 1 101 ? 43.846 -32.291 10.967  1.00 26.81 ?  101 ASN   B CB   1 
ATOM   5680 C  CG   . ASN   B 1 101 ? 43.838 -33.440 9.975   1.00 26.30 ?  101 ASN   B CG   1 
ATOM   5681 O  OD1  . ASN   B 1 101 ? 43.179 -34.450 10.193  1.00 27.67 ?  101 ASN   B OD1  1 
ATOM   5682 N  ND2  . ASN   B 1 101 ? 44.563 -33.283 8.876   1.00 25.93 ?  101 ASN   B ND2  1 
ATOM   5683 H  H    A ASN   B 1 101 ? 41.770 -31.341 10.066  0.70 29.91 ?  101 ASN   B H    1 
ATOM   5684 H  H    B ASN   B 1 101 ? 41.776 -31.323 10.074  0.30 29.91 ?  101 ASN   B H    1 
ATOM   5685 H  HA   . ASN   B 1 101 ? 42.244 -33.033 11.995  1.00 32.44 ?  101 ASN   B HA   1 
ATOM   5686 H  HB2  . ASN   B 1 101 ? 44.031 -31.477 10.476  1.00 32.16 ?  101 ASN   B HB2  1 
ATOM   5687 H  HB3  . ASN   B 1 101 ? 44.555 -32.455 11.612  1.00 32.16 ?  101 ASN   B HB3  1 
ATOM   5688 H  HD21 . ASN   B 1 101 ? 44.590 -33.909 8.287   1.00 31.10 ?  101 ASN   B HD21 1 
ATOM   5689 H  HD22 . ASN   B 1 101 ? 45.005 -32.557 8.754   1.00 31.10 ?  101 ASN   B HD22 1 
ATOM   5690 N  N    . LYS   B 1 102 ? 42.186 -30.089 13.004  1.00 30.35 ?  102 LYS   B N    1 
ATOM   5691 C  CA   . LYS   B 1 102 ? 42.154 -29.256 14.199  1.00 33.03 ?  102 LYS   B CA   1 
ATOM   5692 C  C    . LYS   B 1 102 ? 40.770 -29.211 14.836  1.00 32.38 ?  102 LYS   B C    1 
ATOM   5693 O  O    . LYS   B 1 102 ? 40.546 -28.412 15.749  1.00 33.06 ?  102 LYS   B O    1 
ATOM   5694 C  CB   . LYS   B 1 102 ? 42.593 -27.829 13.867  1.00 35.80 ?  102 LYS   B CB   1 
ATOM   5695 C  CG   . LYS   B 1 102 ? 44.056 -27.662 13.500  1.00 39.00 ?  102 LYS   B CG   1 
ATOM   5696 C  CD   . LYS   B 1 102 ? 44.299 -26.243 13.006  1.00 41.37 ?  102 LYS   B CD   1 
ATOM   5697 C  CE   . LYS   B 1 102 ? 45.774 -25.927 12.846  1.00 43.42 ?  102 LYS   B CE   1 
ATOM   5698 N  NZ   . LYS   B 1 102 ? 45.969 -24.527 12.368  1.00 44.65 ?  102 LYS   B NZ   1 
ATOM   5699 H  H    . LYS   B 1 102 ? 41.826 -29.707 12.320  1.00 36.40 ?  102 LYS   B H    1 
ATOM   5700 H  HA   . LYS   B 1 102 ? 42.778 -29.614 14.850  1.00 39.62 ?  102 LYS   B HA   1 
ATOM   5701 H  HB2  . LYS   B 1 102 ? 42.067 -27.511 13.117  1.00 42.94 ?  102 LYS   B HB2  1 
ATOM   5702 H  HB3  . LYS   B 1 102 ? 42.423 -27.266 14.641  1.00 42.94 ?  102 LYS   B HB3  1 
ATOM   5703 H  HG2  . LYS   B 1 102 ? 44.610 -27.817 14.282  1.00 46.78 ?  102 LYS   B HG2  1 
ATOM   5704 H  HG3  . LYS   B 1 102 ? 44.287 -28.281 12.790  1.00 46.78 ?  102 LYS   B HG3  1 
ATOM   5705 H  HD2  . LYS   B 1 102 ? 43.871 -26.131 12.142  1.00 49.63 ?  102 LYS   B HD2  1 
ATOM   5706 H  HD3  . LYS   B 1 102 ? 43.924 -25.617 13.646  1.00 49.63 ?  102 LYS   B HD3  1 
ATOM   5707 H  HE2  . LYS   B 1 102 ? 46.219 -26.022 13.703  1.00 52.09 ?  102 LYS   B HE2  1 
ATOM   5708 H  HE3  . LYS   B 1 102 ? 46.164 -26.530 12.194  1.00 52.09 ?  102 LYS   B HE3  1 
ATOM   5709 H  HZ1  . LYS   B 1 102 ? 46.836 -24.354 12.278  1.00 53.56 ?  102 LYS   B HZ1  1 
ATOM   5710 H  HZ2  . LYS   B 1 102 ? 45.568 -24.417 11.581  1.00 53.56 ?  102 LYS   B HZ2  1 
ATOM   5711 H  HZ3  . LYS   B 1 102 ? 45.618 -23.955 12.953  1.00 53.56 ?  102 LYS   B HZ3  1 
ATOM   5712 N  N    . GLY   B 1 103 ? 39.833 -30.027 14.359  1.00 31.24 ?  103 GLY   B N    1 
ATOM   5713 C  CA   . GLY   B 1 103 ? 38.503 -30.081 14.930  1.00 30.84 ?  103 GLY   B CA   1 
ATOM   5714 C  C    . GLY   B 1 103 ? 37.559 -28.991 14.477  1.00 30.04 ?  103 GLY   B C    1 
ATOM   5715 O  O    . GLY   B 1 103 ? 36.477 -28.852 15.059  1.00 30.58 ?  103 GLY   B O    1 
ATOM   5716 H  H    . GLY   B 1 103 ? 39.949 -30.560 13.698  1.00 37.46 ?  103 GLY   B H    1 
ATOM   5717 H  HA2  . GLY   B 1 103 ? 38.100 -30.933 14.705  1.00 36.98 ?  103 GLY   B HA2  1 
ATOM   5718 H  HA3  . GLY   B 1 103 ? 38.573 -30.031 15.898  1.00 36.98 ?  103 GLY   B HA3  1 
ATOM   5719 N  N    A GLU   B 1 104 ? 37.933 -28.210 13.467  0.70 28.64 ?  104 GLU   B N    1 
ATOM   5720 N  N    B GLU   B 1 104 ? 37.915 -28.227 13.450  0.30 29.62 ?  104 GLU   B N    1 
ATOM   5721 C  CA   A GLU   B 1 104 ? 37.102 -27.105 13.017  0.70 27.13 ?  104 GLU   B CA   1 
ATOM   5722 C  CA   B GLU   B 1 104 ? 37.065 -27.138 12.994  0.30 28.96 ?  104 GLU   B CA   1 
ATOM   5723 C  C    A GLU   B 1 104 ? 35.915 -27.620 12.203  0.70 27.42 ?  104 GLU   B C    1 
ATOM   5724 C  C    B GLU   B 1 104 ? 35.903 -27.671 12.161  0.30 28.80 ?  104 GLU   B C    1 
ATOM   5725 O  O    A GLU   B 1 104 ? 35.947 -28.707 11.618  0.70 28.12 ?  104 GLU   B O    1 
ATOM   5726 O  O    B GLU   B 1 104 ? 35.981 -28.744 11.556  0.30 29.00 ?  104 GLU   B O    1 
ATOM   5727 C  CB   A GLU   B 1 104 ? 37.943 -26.104 12.221  0.70 25.84 ?  104 GLU   B CB   1 
ATOM   5728 C  CB   B GLU   B 1 104 ? 37.892 -26.127 12.199  0.30 28.31 ?  104 GLU   B CB   1 
ATOM   5729 C  CG   A GLU   B 1 104 ? 39.034 -25.462 13.071  0.70 24.43 ?  104 GLU   B CG   1 
ATOM   5730 C  CG   B GLU   B 1 104 ? 38.969 -25.469 13.052  0.30 27.55 ?  104 GLU   B CG   1 
ATOM   5731 C  CD   A GLU   B 1 104 ? 39.984 -24.579 12.290  0.70 22.78 ?  104 GLU   B CD   1 
ATOM   5732 C  CD   B GLU   B 1 104 ? 39.928 -24.611 12.253  0.30 26.72 ?  104 GLU   B CD   1 
ATOM   5733 O  OE1  A GLU   B 1 104 ? 39.984 -24.619 11.041  0.70 20.65 ?  104 GLU   B OE1  1 
ATOM   5734 O  OE1  B GLU   B 1 104 ? 39.860 -24.625 11.006  0.30 26.17 ?  104 GLU   B OE1  1 
ATOM   5735 O  OE2  A GLU   B 1 104 ? 40.743 -23.837 12.945  0.70 23.32 -1 104 GLU   B OE2  1 
ATOM   5736 O  OE2  B GLU   B 1 104 ? 40.758 -23.922 12.881  0.30 26.69 -1 104 GLU   B OE2  1 
ATOM   5737 H  H    A GLU   B 1 104 ? 38.670 -28.298 13.032  0.70 34.34 ?  104 GLU   B H    1 
ATOM   5738 H  H    B GLU   B 1 104 ? 38.645 -28.318 13.003  0.30 35.53 ?  104 GLU   B H    1 
ATOM   5739 H  HA   A GLU   B 1 104 ? 36.753 -26.641 13.795  0.70 32.54 ?  104 GLU   B HA   1 
ATOM   5740 H  HA   B GLU   B 1 104 ? 36.697 -26.680 13.766  0.30 34.73 ?  104 GLU   B HA   1 
ATOM   5741 H  HB2  A GLU   B 1 104 ? 38.371 -26.561 11.481  0.70 30.99 ?  104 GLU   B HB2  1 
ATOM   5742 H  HB2  B GLU   B 1 104 ? 38.326 -26.581 11.460  0.30 33.95 ?  104 GLU   B HB2  1 
ATOM   5743 H  HB3  A GLU   B 1 104 ? 37.369 -25.396 11.889  0.70 30.99 ?  104 GLU   B HB3  1 
ATOM   5744 H  HB3  B GLU   B 1 104 ? 37.305 -25.430 11.863  0.30 33.95 ?  104 GLU   B HB3  1 
ATOM   5745 H  HG2  A GLU   B 1 104 ? 38.622 -24.912 13.756  0.70 29.29 ?  104 GLU   B HG2  1 
ATOM   5746 H  HG2  B GLU   B 1 104 ? 38.542 -24.904 13.716  0.30 33.03 ?  104 GLU   B HG2  1 
ATOM   5747 H  HG3  A GLU   B 1 104 ? 39.566 -26.158 13.486  0.70 29.29 ?  104 GLU   B HG3  1 
ATOM   5748 H  HG3  B GLU   B 1 104 ? 39.486 -26.161 13.495  0.30 33.03 ?  104 GLU   B HG3  1 
ATOM   5749 N  N    A ASP   B 1 105 ? 34.853 -26.818 12.179  0.70 27.60 ?  105 ASP   B N    1 
ATOM   5750 N  N    B ASP   B 1 105 ? 34.815 -26.903 12.139  0.30 28.86 ?  105 ASP   B N    1 
ATOM   5751 C  CA   A ASP   B 1 105 ? 33.572 -27.261 11.639  0.70 28.20 ?  105 ASP   B CA   1 
ATOM   5752 C  CA   B ASP   B 1 105 ? 33.558 -27.376 11.574  0.30 28.74 ?  105 ASP   B CA   1 
ATOM   5753 C  C    A ASP   B 1 105 ? 33.622 -27.315 10.116  0.70 26.28 ?  105 ASP   B C    1 
ATOM   5754 C  C    B ASP   B 1 105 ? 33.632 -27.393 10.050  0.30 27.69 ?  105 ASP   B C    1 
ATOM   5755 O  O    A ASP   B 1 105 ? 33.771 -26.283 9.453   0.70 26.00 ?  105 ASP   B O    1 
ATOM   5756 O  O    B ASP   B 1 105 ? 33.837 -26.352 9.417   0.30 27.53 ?  105 ASP   B O    1 
ATOM   5757 C  CB   A ASP   B 1 105 ? 32.467 -26.313 12.102  0.70 31.33 ?  105 ASP   B CB   1 
ATOM   5758 C  CB   B ASP   B 1 105 ? 32.413 -26.481 12.046  0.30 29.67 ?  105 ASP   B CB   1 
ATOM   5759 C  CG   A ASP   B 1 105 ? 31.085 -26.777 11.683  0.70 33.45 ?  105 ASP   B CG   1 
ATOM   5760 C  CG   B ASP   B 1 105 ? 31.048 -27.070 11.736  0.30 30.02 ?  105 ASP   B CG   1 
ATOM   5761 O  OD1  A ASP   B 1 105 ? 30.971 -27.876 11.099  0.70 33.46 ?  105 ASP   B OD1  1 
ATOM   5762 O  OD1  B ASP   B 1 105 ? 30.981 -28.054 10.969  0.30 30.17 ?  105 ASP   B OD1  1 
ATOM   5763 O  OD2  A ASP   B 1 105 ? 30.108 -26.039 11.935  0.70 35.03 -1 105 ASP   B OD2  1 
ATOM   5764 O  OD2  B ASP   B 1 105 ? 30.040 -26.560 12.270  0.30 30.20 -1 105 ASP   B OD2  1 
ATOM   5765 H  H    A ASP   B 1 105 ? 34.851 -26.010 12.472  0.70 33.10 ?  105 ASP   B H    1 
ATOM   5766 H  H    B ASP   B 1 105 ? 34.781 -26.101 12.446  0.30 34.61 ?  105 ASP   B H    1 
ATOM   5767 H  HA   A ASP   B 1 105 ? 33.373 -28.150 11.973  0.70 33.82 ?  105 ASP   B HA   1 
ATOM   5768 H  HA   B ASP   B 1 105 ? 33.382 -28.280 11.880  0.30 34.46 ?  105 ASP   B HA   1 
ATOM   5769 H  HB2  A ASP   B 1 105 ? 32.494 -26.243 13.071  0.70 37.58 ?  105 ASP   B HB2  1 
ATOM   5770 H  HB2  B ASP   B 1 105 ? 32.477 -26.366 13.008  0.30 35.59 ?  105 ASP   B HB2  1 
ATOM   5771 H  HB3  A ASP   B 1 105 ? 32.610 -25.441 11.704  0.70 37.58 ?  105 ASP   B HB3  1 
ATOM   5772 H  HB3  B ASP   B 1 105 ? 32.484 -25.616 11.607  0.30 35.59 ?  105 ASP   B HB3  1 
ATOM   5773 N  N    A ILE   B 1 106 ? 33.464 -28.520 9.563   0.70 25.88 ?  106 ILE   B N    1 
ATOM   5774 N  N    B ILE   B 1 106 ? 33.451 -28.580 9.464   0.30 27.15 ?  106 ILE   B N    1 
ATOM   5775 C  CA   A ILE   B 1 106 ? 33.465 -28.707 8.117   0.70 25.07 ?  106 ILE   B CA   1 
ATOM   5776 C  CA   B ILE   B 1 106 ? 33.463 -28.729 8.013   0.30 26.69 ?  106 ILE   B CA   1 
ATOM   5777 C  C    A ILE   B 1 106 ? 32.369 -27.892 7.437   0.70 23.69 ?  106 ILE   B C    1 
ATOM   5778 C  C    B ILE   B 1 106 ? 32.365 -27.908 7.349   0.30 26.11 ?  106 ILE   B C    1 
ATOM   5779 O  O    A ILE   B 1 106 ? 32.477 -27.582 6.245   0.70 22.75 ?  106 ILE   B O    1 
ATOM   5780 O  O    B ILE   B 1 106 ? 32.455 -27.608 6.153   0.30 25.85 ?  106 ILE   B O    1 
ATOM   5781 C  CB   A ILE   B 1 106 ? 33.368 -30.216 7.793   0.70 25.88 ?  106 ILE   B CB   1 
ATOM   5782 C  CB   B ILE   B 1 106 ? 33.371 -30.229 7.644   0.30 27.00 ?  106 ILE   B CB   1 
ATOM   5783 C  CG1  A ILE   B 1 106 ? 33.638 -30.478 6.312   0.70 26.65 ?  106 ILE   B CG1  1 
ATOM   5784 C  CG1  B ILE   B 1 106 ? 33.654 -30.449 6.156   0.30 27.32 ?  106 ILE   B CG1  1 
ATOM   5785 C  CG2  A ILE   B 1 106 ? 32.004 -30.767 8.194   0.70 26.66 ?  106 ILE   B CG2  1 
ATOM   5786 C  CG2  B ILE   B 1 106 ? 32.004 -30.789 8.014   0.30 27.31 ?  106 ILE   B CG2  1 
ATOM   5787 C  CD1  A ILE   B 1 106 ? 35.004 -30.023 5.861   0.70 26.75 ?  106 ILE   B CD1  1 
ATOM   5788 C  CD1  B ILE   B 1 106 ? 35.021 -29.976 5.722   0.30 27.43 ?  106 ILE   B CD1  1 
ATOM   5789 H  H    A ILE   B 1 106 ? 33.355 -29.244 10.013  0.70 31.03 ?  106 ILE   B H    1 
ATOM   5790 H  H    B ILE   B 1 106 ? 33.328 -29.315 9.890   0.30 32.56 ?  106 ILE   B H    1 
ATOM   5791 H  HA   A ILE   B 1 106 ? 34.311 -28.389 7.780   0.70 30.07 ?  106 ILE   B HA   1 
ATOM   5792 H  HA   B ILE   B 1 106 ? 34.308 -28.396 7.684   0.30 32.00 ?  106 ILE   B HA   1 
ATOM   5793 H  HB   A ILE   B 1 106 ? 34.040 -30.682 8.312   0.70 31.03 ?  106 ILE   B HB   1 
ATOM   5794 H  HB   B ILE   B 1 106 ? 34.041 -30.709 8.154   0.30 32.38 ?  106 ILE   B HB   1 
ATOM   5795 H  HG12 A ILE   B 1 106 ? 33.578 -31.433 6.147   0.70 31.96 ?  106 ILE   B HG12 1 
ATOM   5796 H  HG12 B ILE   B 1 106 ? 33.598 -31.400 5.964   0.30 32.76 ?  106 ILE   B HG12 1 
ATOM   5797 H  HG13 A ILE   B 1 106 ? 32.978 -30.010 5.782   0.70 31.96 ?  106 ILE   B HG13 1 
ATOM   5798 H  HG13 B ILE   B 1 106 ? 32.994 -29.971 5.632   0.30 32.76 ?  106 ILE   B HG13 1 
ATOM   5799 H  HG21 A ILE   B 1 106 ? 32.017 -31.734 8.111   0.70 31.97 ?  106 ILE   B HG21 1 
ATOM   5800 H  HG21 B ILE   B 1 106 ? 32.024 -31.755 7.923   0.30 32.75 ?  106 ILE   B HG21 1 
ATOM   5801 H  HG22 A ILE   B 1 106 ? 31.821 -30.520 9.116   0.70 31.97 ?  106 ILE   B HG22 1 
ATOM   5802 H  HG22 B ILE   B 1 106 ? 31.803 -30.549 8.932   0.30 32.75 ?  106 ILE   B HG22 1 
ATOM   5803 H  HG23 A ILE   B 1 106 ? 31.324 -30.395 7.612   0.70 31.97 ?  106 ILE   B HG23 1 
ATOM   5804 H  HG23 B ILE   B 1 106 ? 31.335 -30.416 7.420   0.30 32.75 ?  106 ILE   B HG23 1 
ATOM   5805 H  HD11 A ILE   B 1 106 ? 35.211 -30.441 5.012   0.70 32.08 ?  106 ILE   B HD11 1 
ATOM   5806 H  HD11 B ILE   B 1 106 ? 35.230 -30.368 4.861   0.30 32.89 ?  106 ILE   B HD11 1 
ATOM   5807 H  HD12 A ILE   B 1 106 ? 35.000 -29.057 5.761   0.70 32.08 ?  106 ILE   B HD12 1 
ATOM   5808 H  HD12 B ILE   B 1 106 ? 35.013 -29.009 5.652   0.30 32.89 ?  106 ILE   B HD12 1 
ATOM   5809 H  HD13 A ILE   B 1 106 ? 35.661 -30.285 6.526   0.70 32.08 ?  106 ILE   B HD13 1 
ATOM   5810 H  HD13 B ILE   B 1 106 ? 35.675 -30.257 6.381   0.30 32.89 ?  106 ILE   B HD13 1 
ATOM   5811 N  N    A GLN   B 1 107 ? 31.316 -27.521 8.170   0.70 24.36 ?  107 GLN   B N    1 
ATOM   5812 N  N    B GLN   B 1 107 ? 31.326 -27.532 8.098   0.30 26.14 ?  107 GLN   B N    1 
ATOM   5813 C  CA   A GLN   B 1 107 ? 30.242 -26.722 7.587   0.70 24.97 ?  107 GLN   B CA   1 
ATOM   5814 C  CA   B GLN   B 1 107 ? 30.246 -26.728 7.535   0.30 26.22 ?  107 GLN   B CA   1 
ATOM   5815 C  C    A GLN   B 1 107 ? 30.731 -25.375 7.070   0.70 23.27 ?  107 GLN   B C    1 
ATOM   5816 C  C    B GLN   B 1 107 ? 30.724 -25.356 7.070   0.30 23.87 ?  107 GLN   B C    1 
ATOM   5817 O  O    A GLN   B 1 107 ? 30.095 -24.800 6.184   0.70 23.86 ?  107 GLN   B O    1 
ATOM   5818 O  O    B GLN   B 1 107 ? 30.062 -24.739 6.230   0.30 24.19 ?  107 GLN   B O    1 
ATOM   5819 C  CB   A GLN   B 1 107 ? 29.127 -26.518 8.618   0.70 28.48 ?  107 GLN   B CB   1 
ATOM   5820 C  CB   B GLN   B 1 107 ? 29.121 -26.580 8.565   0.30 28.65 ?  107 GLN   B CB   1 
ATOM   5821 C  CG   A GLN   B 1 107 ? 27.808 -26.004 8.045   0.70 32.24 ?  107 GLN   B CG   1 
ATOM   5822 C  CG   B GLN   B 1 107 ? 27.804 -26.056 8.003   0.30 31.12 ?  107 GLN   B CG   1 
ATOM   5823 C  CD   A GLN   B 1 107 ? 27.749 -24.488 7.952   0.70 34.87 ?  107 GLN   B CD   1 
ATOM   5824 C  CD   B GLN   B 1 107 ? 27.703 -24.542 8.046   0.30 32.88 ?  107 GLN   B CD   1 
ATOM   5825 O  OE1  A GLN   B 1 107 ? 28.583 -23.785 8.524   0.70 35.89 ?  107 GLN   B OE1  1 
ATOM   5826 O  OE1  B GLN   B 1 107 ? 28.542 -23.867 8.644   0.30 33.51 ?  107 GLN   B OE1  1 
ATOM   5827 N  NE2  A GLN   B 1 107 ? 26.754 -23.978 7.230   0.70 36.03 ?  107 GLN   B NE2  1 
ATOM   5828 N  NE2  B GLN   B 1 107 ? 26.666 -24.002 7.414   0.30 33.69 ?  107 GLN   B NE2  1 
ATOM   5829 H  H    A GLN   B 1 107 ? 31.202 -27.715 8.997   0.70 29.21 ?  107 GLN   B H    1 
ATOM   5830 H  H    B GLN   B 1 107 ? 31.220 -27.734 8.924   0.30 31.35 ?  107 GLN   B H    1 
ATOM   5831 H  HA   A GLN   B 1 107 ? 29.864 -27.208 6.837   0.70 29.94 ?  107 GLN   B HA   1 
ATOM   5832 H  HA   B GLN   B 1 107 ? 29.878 -27.191 6.766   0.30 31.45 ?  107 GLN   B HA   1 
ATOM   5833 H  HB2  A GLN   B 1 107 ? 28.946 -27.366 9.046   0.70 34.15 ?  107 GLN   B HB2  1 
ATOM   5834 H  HB2  B GLN   B 1 107 ? 28.944 -27.449 8.953   0.30 34.36 ?  107 GLN   B HB2  1 
ATOM   5835 H  HB3  A GLN   B 1 107 ? 29.431 -25.877 9.279   0.70 34.15 ?  107 GLN   B HB3  1 
ATOM   5836 H  HB3  B GLN   B 1 107 ? 29.412 -25.968 9.259   0.30 34.36 ?  107 GLN   B HB3  1 
ATOM   5837 H  HG2  A GLN   B 1 107 ? 27.689 -26.361 7.152   0.70 38.66 ?  107 GLN   B HG2  1 
ATOM   5838 H  HG2  B GLN   B 1 107 ? 27.719 -26.335 7.078   0.30 37.32 ?  107 GLN   B HG2  1 
ATOM   5839 H  HG3  A GLN   B 1 107 ? 27.080 -26.301 8.618   0.70 38.66 ?  107 GLN   B HG3  1 
ATOM   5840 H  HG3  B GLN   B 1 107 ? 27.070 -26.423 8.526   0.30 37.32 ?  107 GLN   B HG3  1 
ATOM   5841 H  HE21 A GLN   B 1 107 ? 26.189 -24.501 6.843   0.70 43.22 ?  107 GLN   B HE21 1 
ATOM   5842 H  HE21 B GLN   B 1 107 ? 26.100 -24.505 7.006   0.30 40.40 ?  107 GLN   B HE21 1 
ATOM   5843 H  HE22 A GLN   B 1 107 ? 26.672 -23.125 7.150   0.70 43.22 ?  107 GLN   B HE22 1 
ATOM   5844 H  HE22 B GLN   B 1 107 ? 26.562 -23.148 7.412   0.30 40.40 ?  107 GLN   B HE22 1 
ATOM   5845 N  N    . LEU   B 1 108 ? 31.854 -24.867 7.586   1.00 21.20 ?  108 LEU   B N    1 
ATOM   5846 C  CA   . LEU   B 1 108 ? 32.390 -23.570 7.173   1.00 19.02 ?  108 LEU   B CA   1 
ATOM   5847 C  C    . LEU   B 1 108 ? 33.042 -23.596 5.799   1.00 17.01 ?  108 LEU   B C    1 
ATOM   5848 O  O    . LEU   B 1 108 ? 33.469 -22.539 5.310   1.00 16.12 ?  108 LEU   B O    1 
ATOM   5849 C  CB   . LEU   B 1 108 ? 33.393 -23.070 8.209   1.00 19.41 ?  108 LEU   B CB   1 
ATOM   5850 C  CG   . LEU   B 1 108 ? 32.766 -22.631 9.529   1.00 21.32 ?  108 LEU   B CG   1 
ATOM   5851 C  CD1  . LEU   B 1 108 ? 33.800 -22.575 10.636  1.00 21.17 ?  108 LEU   B CD1  1 
ATOM   5852 C  CD2  . LEU   B 1 108 ? 32.108 -21.274 9.358   1.00 22.60 ?  108 LEU   B CD2  1 
ATOM   5853 H  H    A LEU   B 1 108 ? 32.319 -25.258 8.191   0.70 25.41 ?  108 LEU   B H    1 
ATOM   5854 H  H    B LEU   B 1 108 ? 32.321 -25.266 8.185   0.30 25.41 ?  108 LEU   B H    1 
ATOM   5855 H  HA   . LEU   B 1 108 ? 31.661 -22.936 7.134   1.00 22.80 ?  108 LEU   B HA   1 
ATOM   5856 H  HB2  . LEU   B 1 108 ? 34.019 -23.781 8.405   1.00 23.27 ?  108 LEU   B HB2  1 
ATOM   5857 H  HB3  . LEU   B 1 108 ? 33.862 -22.307 7.841   1.00 23.27 ?  108 LEU   B HB3  1 
ATOM   5858 H  HG   . LEU   B 1 108 ? 32.077 -23.269 9.788   1.00 25.57 ?  108 LEU   B HG   1 
ATOM   5859 H  HD11 . LEU   B 1 108 ? 33.364 -22.315 11.464  1.00 25.38 ?  108 LEU   B HD11 1 
ATOM   5860 H  HD12 . LEU   B 1 108 ? 34.203 -23.450 10.736  1.00 25.38 ?  108 LEU   B HD12 1 
ATOM   5861 H  HD13 . LEU   B 1 108 ? 34.476 -21.921 10.400  1.00 25.38 ?  108 LEU   B HD13 1 
ATOM   5862 H  HD21 . LEU   B 1 108 ? 31.760 -20.980 10.215  1.00 27.09 ?  108 LEU   B HD21 1 
ATOM   5863 H  HD22 . LEU   B 1 108 ? 32.768 -20.643 9.035   1.00 27.09 ?  108 LEU   B HD22 1 
ATOM   5864 H  HD23 . LEU   B 1 108 ? 31.381 -21.351 8.718   1.00 27.09 ?  108 LEU   B HD23 1 
ATOM   5865 N  N    . LEU   B 1 109 ? 33.118 -24.766 5.169   1.00 15.95 ?  109 LEU   B N    1 
ATOM   5866 C  CA   . LEU   B 1 109 ? 33.750 -24.875 3.863   1.00 14.94 ?  109 LEU   B CA   1 
ATOM   5867 C  C    . LEU   B 1 109 ? 32.989 -24.089 2.804   1.00 14.45 ?  109 LEU   B C    1 
ATOM   5868 O  O    . LEU   B 1 109 ? 33.606 -23.503 1.907   1.00 14.12 ?  109 LEU   B O    1 
ATOM   5869 C  CB   . LEU   B 1 109 ? 33.860 -26.348 3.480   1.00 15.18 ?  109 LEU   B CB   1 
ATOM   5870 C  CG   . LEU   B 1 109 ? 34.650 -26.695 2.222   1.00 15.06 ?  109 LEU   B CG   1 
ATOM   5871 C  CD1  . LEU   B 1 109 ? 36.030 -26.048 2.230   1.00 14.80 ?  109 LEU   B CD1  1 
ATOM   5872 C  CD2  . LEU   B 1 109 ? 34.778 -28.208 2.105   1.00 16.19 ?  109 LEU   B CD2  1 
ATOM   5873 H  H    . LEU   B 1 109 ? 32.820 -25.510 5.473   1.00 19.12 ?  109 LEU   B H    1 
ATOM   5874 H  HA   . LEU   B 1 109 ? 34.646 -24.513 3.908   1.00 17.91 ?  109 LEU   B HA   1 
ATOM   5875 H  HB2  . LEU   B 1 109 ? 34.284 -26.820 4.214   1.00 18.19 ?  109 LEU   B HB2  1 
ATOM   5876 H  HB3  . LEU   B 1 109 ? 32.963 -26.700 3.354   1.00 18.19 ?  109 LEU   B HB3  1 
ATOM   5877 H  HG   . LEU   B 1 109 ? 34.168 -26.382 1.438   1.00 18.05 ?  109 LEU   B HG   1 
ATOM   5878 H  HD11 . LEU   B 1 109 ? 36.555 -26.417 1.501   1.00 17.74 ?  109 LEU   B HD11 1 
ATOM   5879 H  HD12 . LEU   B 1 109 ? 35.926 -25.094 2.115   1.00 17.74 ?  109 LEU   B HD12 1 
ATOM   5880 H  HD13 . LEU   B 1 109 ? 36.459 -26.243 3.077   1.00 17.74 ?  109 LEU   B HD13 1 
ATOM   5881 H  HD21 . LEU   B 1 109 ? 35.334 -28.425 1.338   1.00 19.41 ?  109 LEU   B HD21 1 
ATOM   5882 H  HD22 . LEU   B 1 109 ? 35.184 -28.557 2.914   1.00 19.41 ?  109 LEU   B HD22 1 
ATOM   5883 H  HD23 . LEU   B 1 109 ? 33.894 -28.597 1.988   1.00 19.41 ?  109 LEU   B HD23 1 
ATOM   5884 N  N    . LYS   B 1 110 ? 31.653 -24.054 2.886   1.00 14.19 ?  110 LYS   B N    1 
ATOM   5885 C  CA   . LYS   B 1 110 ? 30.895 -23.293 1.897   1.00 13.61 ?  110 LYS   B CA   1 
ATOM   5886 C  C    . LYS   B 1 110 ? 31.233 -21.804 1.982   1.00 13.36 ?  110 LYS   B C    1 
ATOM   5887 O  O    . LYS   B 1 110 ? 31.485 -21.157 0.962   1.00 13.06 ?  110 LYS   B O    1 
ATOM   5888 C  CB   . LYS   B 1 110 ? 29.388 -23.538 2.046   1.00 14.35 ?  110 LYS   B CB   1 
ATOM   5889 C  CG   . LYS   B 1 110 ? 28.581 -22.928 0.899   1.00 14.40 ?  110 LYS   B CG   1 
ATOM   5890 C  CD   . LYS   B 1 110 ? 27.114 -23.345 0.931   1.00 15.28 ?  110 LYS   B CD   1 
ATOM   5891 C  CE   . LYS   B 1 110 ? 26.356 -22.813 -0.283  1.00 15.90 ?  110 LYS   B CE   1 
ATOM   5892 N  NZ   . LYS   B 1 110 ? 26.681 -23.534 -1.539  1.00 16.46 ?  110 LYS   B NZ   1 
ATOM   5893 H  H    . LYS   B 1 110 ? 31.179 -24.457 3.478   1.00 17.01 ?  110 LYS   B H    1 
ATOM   5894 H  HA   . LYS   B 1 110 ? 31.148 -23.596 1.011   1.00 16.31 ?  110 LYS   B HA   1 
ATOM   5895 H  HB2  . LYS   B 1 110 ? 29.223 -24.499 2.051   1.00 17.20 ?  110 LYS   B HB2  1 
ATOM   5896 H  HB3  . LYS   B 1 110 ? 29.079 -23.147 2.876   1.00 17.20 ?  110 LYS   B HB3  1 
ATOM   5897 H  HG2  . LYS   B 1 110 ? 28.614 -21.962 0.965   1.00 17.26 ?  110 LYS   B HG2  1 
ATOM   5898 H  HG3  . LYS   B 1 110 ? 28.955 -23.219 0.053   1.00 17.26 ?  110 LYS   B HG3  1 
ATOM   5899 H  HD2  . LYS   B 1 110 ? 27.054 -24.319 0.922   1.00 18.31 ?  110 LYS   B HD2  1 
ATOM   5900 H  HD3  . LYS   B 1 110 ? 26.692 -22.997 1.733   1.00 18.31 ?  110 LYS   B HD3  1 
ATOM   5901 H  HE2  . LYS   B 1 110 ? 25.403 -22.900 -0.127  1.00 19.06 ?  110 LYS   B HE2  1 
ATOM   5902 H  HE3  . LYS   B 1 110 ? 26.586 -21.878 -0.407  1.00 19.06 ?  110 LYS   B HE3  1 
ATOM   5903 H  HZ1  . LYS   B 1 110 ? 26.222 -23.188 -2.216  1.00 19.74 ?  110 LYS   B HZ1  1 
ATOM   5904 H  HZ2  . LYS   B 1 110 ? 27.552 -23.463 -1.712  1.00 19.74 ?  110 LYS   B HZ2  1 
ATOM   5905 H  HZ3  . LYS   B 1 110 ? 26.473 -24.395 -1.456  1.00 19.74 ?  110 LYS   B HZ3  1 
ATOM   5906 N  N    . SER   B 1 111 ? 31.251 -21.248 3.199   1.00 13.92 ?  111 SER   B N    1 
ATOM   5907 C  CA   . SER   B 1 111 ? 31.644 -19.849 3.375   1.00 13.83 ?  111 SER   B CA   1 
ATOM   5908 C  C    . SER   B 1 111 ? 33.026 -19.589 2.790   1.00 13.26 ?  111 SER   B C    1 
ATOM   5909 O  O    . SER   B 1 111 ? 33.249 -18.559 2.139   1.00 13.14 ?  111 SER   B O    1 
ATOM   5910 C  CB   . SER   B 1 111 ? 31.636 -19.486 4.858   1.00 15.05 ?  111 SER   B CB   1 
ATOM   5911 O  OG   . SER   B 1 111 ? 30.328 -19.493 5.385   1.00 16.79 ?  111 SER   B OG   1 
ATOM   5912 H  H    . SER   B 1 111 ? 31.048 -21.657 3.926   1.00 16.68 ?  111 SER   B H    1 
ATOM   5913 H  HA   . SER   B 1 111 ? 31.012 -19.279 2.917   1.00 16.58 ?  111 SER   B HA   1 
ATOM   5914 H  HB2  . SER   B 1 111 ? 32.171 -20.132 5.345   1.00 18.05 ?  111 SER   B HB2  1 
ATOM   5915 H  HB3  . SER   B 1 111 ? 32.009 -18.599 4.967   1.00 18.05 ?  111 SER   B HB3  1 
ATOM   5916 H  HG   . SER   B 1 111 ? 30.343 -19.291 6.207   1.00 20.13 ?  111 SER   B HG   1 
ATOM   5917 N  N    . ALA   B 1 112 ? 33.968 -20.509 3.012   1.00 13.19 ?  112 ALA   B N    1 
ATOM   5918 C  CA   . ALA   B 1 112 ? 35.314 -20.341 2.470   1.00 12.75 ?  112 ALA   B CA   1 
ATOM   5919 C  C    . ALA   B 1 112 ? 35.282 -20.253 0.946   1.00 12.34 ?  112 ALA   B C    1 
ATOM   5920 O  O    . ALA   B 1 112 ? 35.906 -19.368 0.351   1.00 12.60 ?  112 ALA   B O    1 
ATOM   5921 C  CB   . ALA   B 1 112 ? 36.223 -21.479 2.954   1.00 13.65 ?  112 ALA   B CB   1 
ATOM   5922 H  H    . ALA   B 1 112 ? 33.854 -21.228 3.478   1.00 15.80 ?  112 ALA   B H    1 
ATOM   5923 H  HA   . ALA   B 1 112 ? 35.680 -19.510 2.806   1.00 15.28 ?  112 ALA   B HA   1 
ATOM   5924 H  HB1  . ALA   B 1 112 ? 37.113 -21.343 2.590   1.00 16.36 ?  112 ALA   B HB1  1 
ATOM   5925 H  HB2  . ALA   B 1 112 ? 36.262 -21.457 3.927   1.00 16.36 ?  112 ALA   B HB2  1 
ATOM   5926 H  HB3  . ALA   B 1 112 ? 35.863 -22.323 2.656   1.00 16.36 ?  112 ALA   B HB3  1 
ATOM   5927 N  N    . TYR   B 1 113 ? 34.545 -21.157 0.292   1.00 12.30 ?  113 TYR   B N    1 
ATOM   5928 C  CA   . TYR   B 1 113 ? 34.466 -21.105 -1.163  1.00 11.84 ?  113 TYR   B CA   1 
ATOM   5929 C  C    . TYR   B 1 113 ? 33.755 -19.853 -1.677  1.00 11.78 ?  113 TYR   B C    1 
ATOM   5930 O  O    . TYR   B 1 113 ? 34.021 -19.421 -2.803  1.00 11.78 ?  113 TYR   B O    1 
ATOM   5931 C  CB   . TYR   B 1 113 ? 33.792 -22.365 -1.713  1.00 12.29 ?  113 TYR   B CB   1 
ATOM   5932 C  CG   . TYR   B 1 113 ? 34.759 -23.516 -1.970  1.00 12.83 ?  113 TYR   B CG   1 
ATOM   5933 C  CD1  . TYR   B 1 113 ? 35.752 -23.414 -2.940  1.00 13.36 ?  113 TYR   B CD1  1 
ATOM   5934 C  CD2  . TYR   B 1 113 ? 34.663 -24.705 -1.264  1.00 13.08 ?  113 TYR   B CD2  1 
ATOM   5935 C  CE1  . TYR   B 1 113 ? 36.632 -24.450 -3.183  1.00 13.20 ?  113 TYR   B CE1  1 
ATOM   5936 C  CE2  . TYR   B 1 113 ? 35.535 -25.751 -1.505  1.00 13.41 ?  113 TYR   B CE2  1 
ATOM   5937 C  CZ   . TYR   B 1 113 ? 36.509 -25.625 -2.472  1.00 12.96 ?  113 TYR   B CZ   1 
ATOM   5938 O  OH   . TYR   B 1 113 ? 37.392 -26.642 -2.742  1.00 13.82 ?  113 TYR   B OH   1 
ATOM   5939 H  H    . TYR   B 1 113 ? 34.081 -21.786 0.663   1.00 14.74 ?  113 TYR   B H    1 
ATOM   5940 H  HA   . TYR   B 1 113 ? 35.368 -21.086 -1.504  1.00 14.19 ?  113 TYR   B HA   1 
ATOM   5941 H  HB2  . TYR   B 1 113 ? 33.131 -22.677 -1.072  1.00 14.73 ?  113 TYR   B HB2  1 
ATOM   5942 H  HB3  . TYR   B 1 113 ? 33.356 -22.146 -2.551  1.00 14.73 ?  113 TYR   B HB3  1 
ATOM   5943 H  HD1  . TYR   B 1 113 ? 35.834 -22.619 -3.431  1.00 16.01 ?  113 TYR   B HD1  1 
ATOM   5944 H  HD2  . TYR   B 1 113 ? 33.999 -24.796 -0.622  1.00 15.67 ?  113 TYR   B HD2  1 
ATOM   5945 H  HE1  . TYR   B 1 113 ? 37.288 -24.359 -3.843  1.00 15.82 ?  113 TYR   B HE1  1 
ATOM   5946 H  HE2  . TYR   B 1 113 ? 35.453 -26.547 -1.030  1.00 16.07 ?  113 TYR   B HE2  1 
ATOM   5947 H  HH   . TYR   B 1 113 ? 37.215 -27.307 -2.258  1.00 16.56 ?  113 TYR   B HH   1 
ATOM   5948 N  N    . GLU   B 1 114 ? 32.832 -19.273 -0.898  1.00 11.95 ?  114 GLU   B N    1 
ATOM   5949 C  CA   . GLU   B 1 114 ? 32.150 -18.066 -1.360  1.00 11.97 ?  114 GLU   B CA   1 
ATOM   5950 C  C    . GLU   B 1 114 ? 33.139 -16.944 -1.656  1.00 11.90 ?  114 GLU   B C    1 
ATOM   5951 O  O    . GLU   B 1 114 ? 32.870 -16.088 -2.500  1.00 11.94 ?  114 GLU   B O    1 
ATOM   5952 C  CB   . GLU   B 1 114 ? 31.087 -17.636 -0.347  1.00 12.71 ?  114 GLU   B CB   1 
ATOM   5953 C  CG   . GLU   B 1 114 ? 29.877 -18.559 -0.409  1.00 12.39 ?  114 GLU   B CG   1 
ATOM   5954 C  CD   . GLU   B 1 114 ? 28.853 -18.362 0.700   1.00 12.61 ?  114 GLU   B CD   1 
ATOM   5955 O  OE1  . GLU   B 1 114 ? 29.146 -17.744 1.741   1.00 12.87 ?  114 GLU   B OE1  1 
ATOM   5956 O  OE2  . GLU   B 1 114 ? 27.729 -18.902 0.543   1.00 13.42 -1 114 GLU   B OE2  1 
ATOM   5957 H  H    . GLU   B 1 114 ? 32.582 -19.562 -0.124  1.00 14.32 ?  114 GLU   B H    1 
ATOM   5958 H  HA   . GLU   B 1 114 ? 31.698 -18.269 -2.186  1.00 14.35 ?  114 GLU   B HA   1 
ATOM   5959 H  HB2  . GLU   B 1 114 ? 31.454 -17.678 0.551   1.00 15.23 ?  114 GLU   B HB2  1 
ATOM   5960 H  HB3  . GLU   B 1 114 ? 30.791 -16.738 -0.550  1.00 15.23 ?  114 GLU   B HB3  1 
ATOM   5961 H  HG2  . GLU   B 1 114 ? 29.427 -18.421 -1.254  1.00 14.84 ?  114 GLU   B HG2  1 
ATOM   5962 H  HG3  . GLU   B 1 114 ? 30.191 -19.480 -0.356  1.00 14.84 ?  114 GLU   B HG3  1 
ATOM   5963 N  N    . ASN   B 1 115 ? 34.304 -16.942 -1.005  1.00 11.52 ?  115 ASN   B N    1 
ATOM   5964 C  CA   . ASN   B 1 115 ? 35.293 -15.907 -1.299  1.00 11.54 ?  115 ASN   B CA   1 
ATOM   5965 C  C    . ASN   B 1 115 ? 35.702 -15.925 -2.766  1.00 11.25 ?  115 ASN   B C    1 
ATOM   5966 O  O    . ASN   B 1 115 ? 36.092 -14.887 -3.321  1.00 11.92 ?  115 ASN   B O    1 
ATOM   5967 C  CB   . ASN   B 1 115 ? 36.533 -16.085 -0.416  1.00 12.07 ?  115 ASN   B CB   1 
ATOM   5968 C  CG   . ASN   B 1 115 ? 36.265 -15.813 1.045   1.00 12.50 ?  115 ASN   B CG   1 
ATOM   5969 O  OD1  . ASN   B 1 115 ? 36.258 -14.662 1.478   1.00 14.38 ?  115 ASN   B OD1  1 
ATOM   5970 N  ND2  . ASN   B 1 115 ? 36.107 -16.879 1.829   1.00 12.68 ?  115 ASN   B ND2  1 
ATOM   5971 H  H    . ASN   B 1 115 ? 34.538 -17.505 -0.392  1.00 13.81 ?  115 ASN   B H    1 
ATOM   5972 H  HA   . ASN   B 1 115 ? 34.914 -15.037 -1.104  1.00 13.83 ?  115 ASN   B HA   1 
ATOM   5973 H  HB2  . ASN   B 1 115 ? 36.855 -16.995 -0.500  1.00 14.47 ?  115 ASN   B HB2  1 
ATOM   5974 H  HB3  . ASN   B 1 115 ? 37.219 -15.463 -0.706  1.00 14.47 ?  115 ASN   B HB3  1 
ATOM   5975 H  HD21 . ASN   B 1 115 ? 35.962 -16.780 2.671   1.00 15.19 ?  115 ASN   B HD21 1 
ATOM   5976 H  HD22 . ASN   B 1 115 ? 36.137 -17.673 1.492   1.00 15.19 ?  115 ASN   B HD22 1 
ATOM   5977 N  N    . PHE   B 1 116 ? 35.679 -17.104 -3.399  1.00 11.14 ?  116 PHE   B N    1 
ATOM   5978 C  CA   . PHE   B 1 116 ? 36.115 -17.201 -4.788  1.00 11.62 ?  116 PHE   B CA   1 
ATOM   5979 C  C    . PHE   B 1 116 ? 35.210 -16.384 -5.707  1.00 11.60 ?  116 PHE   B C    1 
ATOM   5980 O  O    . PHE   B 1 116 ? 35.642 -15.949 -6.779  1.00 11.82 ?  116 PHE   B O    1 
ATOM   5981 C  CB   . PHE   B 1 116 ? 36.067 -18.652 -5.293  1.00 11.16 ?  116 PHE   B CB   1 
ATOM   5982 C  CG   . PHE   B 1 116 ? 37.146 -19.604 -4.758  1.00 11.05 ?  116 PHE   B CG   1 
ATOM   5983 C  CD1  . PHE   B 1 116 ? 37.801 -19.425 -3.552  1.00 12.13 ?  116 PHE   B CD1  1 
ATOM   5984 C  CD2  . PHE   B 1 116 ? 37.438 -20.743 -5.496  1.00 11.70 ?  116 PHE   B CD2  1 
ATOM   5985 C  CE1  . PHE   B 1 116 ? 38.738 -20.360 -3.110  1.00 11.78 ?  116 PHE   B CE1  1 
ATOM   5986 C  CE2  . PHE   B 1 116 ? 38.369 -21.679 -5.058  1.00 11.90 ?  116 PHE   B CE2  1 
ATOM   5987 C  CZ   . PHE   B 1 116 ? 39.016 -21.485 -3.870  1.00 12.07 ?  116 PHE   B CZ   1 
ATOM   5988 H  H    . PHE   B 1 116 ? 35.413 -17.850 -3.051  1.00 13.35 ?  116 PHE   B H    1 
ATOM   5989 H  HA   . PHE   B 1 116 ? 37.023 -16.878 -4.869  1.00 13.92 ?  116 PHE   B HA   1 
ATOM   5990 H  HB2  . PHE   B 1 116 ? 35.198 -19.026 -5.047  1.00 13.37 ?  116 PHE   B HB2  1 
ATOM   5991 H  HB3  . PHE   B 1 116 ? 36.138 -18.639 -6.260  1.00 13.37 ?  116 PHE   B HB3  1 
ATOM   5992 H  HD1  . PHE   B 1 116 ? 37.611 -18.678 -3.031  1.00 14.54 ?  116 PHE   B HD1  1 
ATOM   5993 H  HD2  . PHE   B 1 116 ? 36.991 -20.891 -6.302  1.00 14.03 ?  116 PHE   B HD2  1 
ATOM   5994 H  HE1  . PHE   B 1 116 ? 39.183 -20.228 -2.306  1.00 14.12 ?  116 PHE   B HE1  1 
ATOM   5995 H  HE2  . PHE   B 1 116 ? 38.556 -22.430 -5.574  1.00 14.26 ?  116 PHE   B HE2  1 
ATOM   5996 H  HZ   . PHE   B 1 116 ? 39.652 -22.100 -3.580  1.00 14.47 ?  116 PHE   B HZ   1 
ATOM   5997 N  N    . ASN   B 1 117 ? 33.939 -16.180 -5.323  1.00 11.88 ?  117 ASN   B N    1 
ATOM   5998 C  CA   . ASN   B 1 117 ? 32.989 -15.473 -6.186  1.00 12.25 ?  117 ASN   B CA   1 
ATOM   5999 C  C    . ASN   B 1 117 ? 33.306 -13.991 -6.337  1.00 12.50 ?  117 ASN   B C    1 
ATOM   6000 O  O    . ASN   B 1 117 ? 32.711 -13.334 -7.193  1.00 13.64 ?  117 ASN   B O    1 
ATOM   6001 C  CB   . ASN   B 1 117 ? 31.563 -15.693 -5.695  1.00 12.53 ?  117 ASN   B CB   1 
ATOM   6002 C  CG   . ASN   B 1 117 ? 31.113 -17.108 -5.941  1.00 12.45 ?  117 ASN   B CG   1 
ATOM   6003 O  OD1  . ASN   B 1 117 ? 31.466 -17.699 -6.962  1.00 13.35 ?  117 ASN   B OD1  1 
ATOM   6004 N  ND2  . ASN   B 1 117 ? 30.373 -17.679 -5.003  1.00 12.37 ?  117 ASN   B ND2  1 
ATOM   6005 H  H    . ASN   B 1 117 ? 33.613 -16.439 -4.567  1.00 14.24 ?  117 ASN   B H    1 
ATOM   6006 H  HA   . ASN   B 1 117 ? 33.047 -15.868 -7.065  1.00 14.68 ?  117 ASN   B HA   1 
ATOM   6007 H  HB2  . ASN   B 1 117 ? 31.520 -15.522 -4.736  1.00 15.02 ?  117 ASN   B HB2  1 
ATOM   6008 H  HB3  . ASN   B 1 117 ? 30.965 -15.089 -6.164  1.00 15.02 ?  117 ASN   B HB3  1 
ATOM   6009 H  HD21 . ASN   B 1 117 ? 30.093 -18.488 -5.107  1.00 14.82 ?  117 ASN   B HD21 1 
ATOM   6010 H  HD22 . ASN   B 1 117 ? 30.150 -17.238 -4.298  1.00 14.82 ?  117 ASN   B HD22 1 
ATOM   6011 N  N    . GLN   B 1 118 ? 34.243 -13.465 -5.559  1.00 12.04 ?  118 GLN   B N    1 
ATOM   6012 C  CA   . GLN   B 1 118 ? 34.671 -12.079 -5.698  1.00 12.63 ?  118 GLN   B CA   1 
ATOM   6013 C  C    . GLN   B 1 118 ? 35.736 -11.892 -6.772  1.00 12.81 ?  118 GLN   B C    1 
ATOM   6014 O  O    . GLN   B 1 118 ? 36.210 -10.766 -6.953  1.00 14.08 ?  118 GLN   B O    1 
ATOM   6015 C  CB   . GLN   B 1 118 ? 35.155 -11.547 -4.347  1.00 13.29 ?  118 GLN   B CB   1 
ATOM   6016 C  CG   . GLN   B 1 118 ? 34.073 -11.590 -3.282  1.00 13.04 ?  118 GLN   B CG   1 
ATOM   6017 C  CD   . GLN   B 1 118 ? 32.899 -10.681 -3.609  1.00 13.28 ?  118 GLN   B CD   1 
ATOM   6018 O  OE1  . GLN   B 1 118 ? 33.083 -9.536  -4.036  1.00 13.84 ?  118 GLN   B OE1  1 
ATOM   6019 N  NE2  . GLN   B 1 118 ? 31.685 -11.179 -3.401  1.00 13.51 ?  118 GLN   B NE2  1 
ATOM   6020 H  H    . GLN   B 1 118 ? 34.664 -13.892 -4.939  1.00 14.43 ?  118 GLN   B H    1 
ATOM   6021 H  HA   . GLN   B 1 118 ? 33.908 -11.547 -5.968  1.00 15.14 ?  118 GLN   B HA   1 
ATOM   6022 H  HB2  . GLN   B 1 118 ? 35.900 -12.078 -4.040  1.00 15.92 ?  118 GLN   B HB2  1 
ATOM   6023 H  HB3  . GLN   B 1 118 ? 35.428 -10.617 -4.451  1.00 15.92 ?  118 GLN   B HB3  1 
ATOM   6024 H  HG2  . GLN   B 1 118 ? 33.744 -12.497 -3.205  1.00 15.63 ?  118 GLN   B HG2  1 
ATOM   6025 H  HG3  . GLN   B 1 118 ? 34.454 -11.301 -2.437  1.00 15.63 ?  118 GLN   B HG3  1 
ATOM   6026 H  HE21 . GLN   B 1 118 ? 31.598 -11.983 -3.099  1.00 16.19 ?  118 GLN   B HE21 1 
ATOM   6027 H  HE22 . GLN   B 1 118 ? 30.994 -10.706 -3.570  1.00 16.19 ?  118 GLN   B HE22 1 
ATOM   6028 N  N    . HIS   B 1 119 ? 36.094 -12.948 -7.505  1.00 12.24 ?  119 HIS   B N    1 
ATOM   6029 C  CA   . HIS   B 1 119 ? 37.138 -12.898 -8.522  1.00 12.28 ?  119 HIS   B CA   1 
ATOM   6030 C  C    . HIS   B 1 119 ? 36.664 -13.636 -9.758  1.00 12.33 ?  119 HIS   B C    1 
ATOM   6031 O  O    . HIS   B 1 119 ? 36.154 -14.752 -9.651  1.00 12.97 ?  119 HIS   B O    1 
ATOM   6032 C  CB   . HIS   B 1 119 ? 38.421 -13.526 -7.979  1.00 13.23 ?  119 HIS   B CB   1 
ATOM   6033 C  CG   . HIS   B 1 119 ? 38.908 -12.828 -6.758  1.00 14.40 ?  119 HIS   B CG   1 
ATOM   6034 N  ND1  . HIS   B 1 119 ? 39.702 -11.701 -6.816  1.00 15.64 ?  119 HIS   B ND1  1 
ATOM   6035 C  CD2  . HIS   B 1 119 ? 38.624 -13.025 -5.450  1.00 15.31 ?  119 HIS   B CD2  1 
ATOM   6036 C  CE1  . HIS   B 1 119 ? 39.915 -11.259 -5.591  1.00 16.88 ?  119 HIS   B CE1  1 
ATOM   6037 N  NE2  . HIS   B 1 119 ? 39.266 -12.038 -4.745  1.00 16.70 ?  119 HIS   B NE2  1 
ATOM   6038 H  H    . HIS   B 1 119 ? 35.733 -13.726 -7.433  1.00 14.67 ?  119 HIS   B H    1 
ATOM   6039 H  HA   . HIS   B 1 119 ? 37.317 -11.975 -8.765  1.00 14.72 ?  119 HIS   B HA   1 
ATOM   6040 H  HB2  . HIS   B 1 119 ? 38.252 -14.453 -7.756  1.00 15.85 ?  119 HIS   B HB2  1 
ATOM   6041 H  HB3  . HIS   B 1 119 ? 39.114 -13.468 -8.660  1.00 15.85 ?  119 HIS   B HB3  1 
ATOM   6042 H  HD2  . HIS   B 1 119 ? 38.094 -13.704 -5.098  1.00 18.35 ?  119 HIS   B HD2  1 
ATOM   6043 H  HE1  . HIS   B 1 119 ? 40.443 -10.531 -5.359  1.00 20.23 ?  119 HIS   B HE1  1 
ATOM   6044 H  HE2  . HIS   B 1 119 ? 39.274 -11.963 -3.888  1.00 20.02 ?  119 HIS   B HE2  1 
ATOM   6045 N  N    . GLU   B 1 120 ? 36.812 -13.020 -10.931 1.00 12.90 ?  120 GLU   B N    1 
ATOM   6046 C  CA   . GLU   B 1 120 ? 36.217 -13.608 -12.126 1.00 14.48 ?  120 GLU   B CA   1 
ATOM   6047 C  C    . GLU   B 1 120 ? 36.896 -14.906 -12.544 1.00 13.32 ?  120 GLU   B C    1 
ATOM   6048 O  O    . GLU   B 1 120 ? 36.235 -15.776 -13.128 1.00 13.63 ?  120 GLU   B O    1 
ATOM   6049 C  CB   . GLU   B 1 120 ? 36.207 -12.603 -13.274 1.00 18.30 ?  120 GLU   B CB   1 
ATOM   6050 C  CG   . GLU   B 1 120 ? 35.247 -11.446 -13.047 1.00 23.51 ?  120 GLU   B CG   1 
ATOM   6051 C  CD   . GLU   B 1 120 ? 35.105 -10.546 -14.256 1.00 29.76 ?  120 GLU   B CD   1 
ATOM   6052 O  OE1  . GLU   B 1 120 ? 36.105 -10.350 -14.980 1.00 32.89 ?  120 GLU   B OE1  1 
ATOM   6053 O  OE2  . GLU   B 1 120 ? 33.986 -10.040 -14.483 1.00 33.58 -1 120 GLU   B OE2  1 
ATOM   6054 H  H    . GLU   B 1 120 ? 37.238 -12.280 -11.063 1.00 15.46 ?  120 GLU   B H    1 
ATOM   6055 H  HA   . GLU   B 1 120 ? 35.297 -13.823 -11.930 1.00 17.35 ?  120 GLU   B HA   1 
ATOM   6056 H  HB2  . GLU   B 1 120 ? 37.093 -12.232 -13.386 1.00 21.94 ?  120 GLU   B HB2  1 
ATOM   6057 H  HB3  . GLU   B 1 120 ? 35.931 -13.055 -14.090 1.00 21.94 ?  120 GLU   B HB3  1 
ATOM   6058 H  HG2  . GLU   B 1 120 ? 34.364 -11.798 -12.848 1.00 28.19 ?  120 GLU   B HG2  1 
ATOM   6059 H  HG3  . GLU   B 1 120 ? 35.566 -10.910 -12.305 1.00 28.19 ?  120 GLU   B HG3  1 
ATOM   6060 N  N    . VAL   B 1 121 ? 38.199 -15.044 -12.285 1.00 12.87 ?  121 VAL   B N    1 
ATOM   6061 C  CA   . VAL   B 1 121 ? 38.948 -16.253 -12.633 1.00 12.53 ?  121 VAL   B CA   1 
ATOM   6062 C  C    . VAL   B 1 121 ? 40.061 -16.454 -11.612 1.00 12.32 ?  121 VAL   B C    1 
ATOM   6063 O  O    . VAL   B 1 121 ? 40.736 -15.494 -11.221 1.00 12.77 ?  121 VAL   B O    1 
ATOM   6064 C  CB   . VAL   B 1 121 ? 39.471 -16.210 -14.089 1.00 14.75 ?  121 VAL   B CB   1 
ATOM   6065 C  CG1  . VAL   B 1 121 ? 40.332 -14.978 -14.339 1.00 16.15 ?  121 VAL   B CG1  1 
ATOM   6066 C  CG2  . VAL   B 1 121 ? 40.218 -17.493 -14.436 1.00 16.17 ?  121 VAL   B CG2  1 
ATOM   6067 H  H    . VAL   B 1 121 ? 38.683 -14.440 -11.910 1.00 15.43 ?  121 VAL   B H    1 
ATOM   6068 H  HA   . VAL   B 1 121 ? 38.344 -17.010 -12.567 1.00 15.02 ?  121 VAL   B HA   1 
ATOM   6069 H  HB   . VAL   B 1 121 ? 38.705 -16.156 -14.688 1.00 17.68 ?  121 VAL   B HB   1 
ATOM   6070 H  HG11 . VAL   B 1 121 ? 40.644 -14.991 -15.258 1.00 19.36 ?  121 VAL   B HG11 1 
ATOM   6071 H  HG12 . VAL   B 1 121 ? 39.798 -14.182 -14.184 1.00 19.36 ?  121 VAL   B HG12 1 
ATOM   6072 H  HG13 . VAL   B 1 121 ? 41.089 -14.992 -13.733 1.00 19.36 ?  121 VAL   B HG13 1 
ATOM   6073 H  HG21 . VAL   B 1 121 ? 40.417 -17.494 -15.388 1.00 19.38 ?  121 VAL   B HG21 1 
ATOM   6074 H  HG22 . VAL   B 1 121 ? 41.044 -17.525 -13.929 1.00 19.38 ?  121 VAL   B HG22 1 
ATOM   6075 H  HG23 . VAL   B 1 121 ? 39.661 -18.255 -14.216 1.00 19.38 ?  121 VAL   B HG23 1 
ATOM   6076 N  N    . LEU   B 1 122 ? 40.246 -17.710 -11.178 1.00 11.91 ?  122 LEU   B N    1 
ATOM   6077 C  CA   . LEU   B 1 122 ? 41.230 -18.060 -10.154 1.00 11.80 ?  122 LEU   B CA   1 
ATOM   6078 C  C    . LEU   B 1 122 ? 41.885 -19.395 -10.472 1.00 11.46 ?  122 LEU   B C    1 
ATOM   6079 O  O    . LEU   B 1 122 ? 41.225 -20.317 -10.966 1.00 12.45 ?  122 LEU   B O    1 
ATOM   6080 C  CB   . LEU   B 1 122 ? 40.578 -18.278 -8.776  1.00 13.46 ?  122 LEU   B CB   1 
ATOM   6081 C  CG   . LEU   B 1 122 ? 39.540 -17.263 -8.293  1.00 13.31 ?  122 LEU   B CG   1 
ATOM   6082 C  CD1  . LEU   B 1 122 ? 38.140 -17.615 -8.774  1.00 14.42 ?  122 LEU   B CD1  1 
ATOM   6083 C  CD2  . LEU   B 1 122 ? 39.578 -17.158 -6.782  1.00 12.86 ?  122 LEU   B CD2  1 
ATOM   6084 H  H    . LEU   B 1 122 ? 39.805 -18.392 -11.471 1.00 14.27 ?  122 LEU   B H    1 
ATOM   6085 H  HA   . LEU   B 1 122 ? 41.909 -17.371 -10.083 1.00 14.14 ?  122 LEU   B HA   1 
ATOM   6086 H  HB2  . LEU   B 1 122 ? 40.137 -19.139 -8.789  1.00 16.13 ?  122 LEU   B HB2  1 
ATOM   6087 H  HB3  . LEU   B 1 122 ? 41.282 -18.290 -8.112  1.00 16.13 ?  122 LEU   B HB3  1 
ATOM   6088 H  HG   . LEU   B 1 122 ? 39.763 -16.390 -8.650  1.00 15.95 ?  122 LEU   B HG   1 
ATOM   6089 H  HD11 . LEU   B 1 122 ? 37.508 -16.975 -8.404  1.00 17.28 ?  122 LEU   B HD11 1 
ATOM   6090 H  HD12 . LEU   B 1 122 ? 38.119 -17.566 -9.745  1.00 17.28 ?  122 LEU   B HD12 1 
ATOM   6091 H  HD13 . LEU   B 1 122 ? 37.917 -18.508 -8.482  1.00 17.28 ?  122 LEU   B HD13 1 
ATOM   6092 H  HD21 . LEU   B 1 122 ? 38.891 -16.539 -6.488  1.00 15.42 ?  122 LEU   B HD21 1 
ATOM   6093 H  HD22 . LEU   B 1 122 ? 39.420 -18.034 -6.398  1.00 15.42 ?  122 LEU   B HD22 1 
ATOM   6094 H  HD23 . LEU   B 1 122 ? 40.452 -16.832 -6.510  1.00 15.42 ?  122 LEU   B HD23 1 
ATOM   6095 N  N    . LEU   B 1 123 ? 43.172 -19.504 -10.117 1.00 11.09 ?  123 LEU   B N    1 
ATOM   6096 C  CA   . LEU   B 1 123 ? 43.883 -20.773 -9.999  1.00 11.64 ?  123 LEU   B CA   1 
ATOM   6097 C  C    . LEU   B 1 123 ? 43.854 -21.166 -8.527  1.00 10.95 ?  123 LEU   B C    1 
ATOM   6098 O  O    . LEU   B 1 123 ? 44.205 -20.340 -7.675  1.00 11.49 ?  123 LEU   B O    1 
ATOM   6099 C  CB   . LEU   B 1 123 ? 45.333 -20.595 -10.459 1.00 11.99 ?  123 LEU   B CB   1 
ATOM   6100 C  CG   . LEU   B 1 123 ? 46.281 -21.773 -10.226 1.00 12.06 ?  123 LEU   B CG   1 
ATOM   6101 C  CD1  . LEU   B 1 123 ? 45.861 -23.015 -11.014 1.00 12.75 ?  123 LEU   B CD1  1 
ATOM   6102 C  CD2  . LEU   B 1 123 ? 47.693 -21.386 -10.592 1.00 13.42 ?  123 LEU   B CD2  1 
ATOM   6103 H  H    . LEU   B 1 123 ? 43.669 -18.825 -9.929  1.00 13.29 ?  123 LEU   B H    1 
ATOM   6104 H  HA   . LEU   B 1 123 ? 43.448 -21.461 -10.528 1.00 13.94 ?  123 LEU   B HA   1 
ATOM   6105 H  HB2  . LEU   B 1 123 ? 45.324 -20.418 -11.413 1.00 14.37 ?  123 LEU   B HB2  1 
ATOM   6106 H  HB3  . LEU   B 1 123 ? 45.704 -19.831 -9.994  1.00 14.37 ?  123 LEU   B HB3  1 
ATOM   6107 H  HG   . LEU   B 1 123 ? 46.277 -22.004 -9.284  1.00 14.45 ?  123 LEU   B HG   1 
ATOM   6108 H  HD11 . LEU   B 1 123 ? 46.498 -23.725 -10.843 1.00 15.28 ?  123 LEU   B HD11 1 
ATOM   6109 H  HD12 . LEU   B 1 123 ? 44.976 -23.285 -10.722 1.00 15.28 ?  123 LEU   B HD12 1 
ATOM   6110 H  HD13 . LEU   B 1 123 ? 45.848 -22.797 -11.958 1.00 15.28 ?  123 LEU   B HD13 1 
ATOM   6111 H  HD21 . LEU   B 1 123 ? 48.279 -22.144 -10.439 1.00 16.08 ?  123 LEU   B HD21 1 
ATOM   6112 H  HD22 . LEU   B 1 123 ? 47.717 -21.133 -11.529 1.00 16.08 ?  123 LEU   B HD22 1 
ATOM   6113 H  HD23 . LEU   B 1 123 ? 47.968 -20.638 -10.041 1.00 16.08 ?  123 LEU   B HD23 1 
ATOM   6114 N  N    . ALA   B 1 124 ? 43.419 -22.396 -8.216  1.00 10.93 ?  124 ALA   B N    1 
ATOM   6115 C  CA   . ALA   B 1 124 ? 43.163 -22.715 -6.819  1.00 10.97 ?  124 ALA   B CA   1 
ATOM   6116 C  C    . ALA   B 1 124 ? 43.433 -24.178 -6.493  1.00 10.87 ?  124 ALA   B C    1 
ATOM   6117 O  O    . ALA   B 1 124 ? 43.302 -25.056 -7.359  1.00 11.51 ?  124 ALA   B O    1 
ATOM   6118 C  CB   . ALA   B 1 124 ? 41.714 -22.394 -6.445  1.00 11.50 ?  124 ALA   B CB   1 
ATOM   6119 H  H    . ALA   B 1 124 ? 43.263 -23.035 -8.778  1.00 13.10 ?  124 ALA   B H    1 
ATOM   6120 H  HA   . ALA   B 1 124 ? 43.744 -22.169 -6.274  1.00 13.15 ?  124 ALA   B HA   1 
ATOM   6121 H  HB1  . ALA   B 1 124 ? 41.565 -22.614 -5.514  1.00 13.78 ?  124 ALA   B HB1  1 
ATOM   6122 H  HB2  . ALA   B 1 124 ? 41.556 -21.445 -6.590  1.00 13.78 ?  124 ALA   B HB2  1 
ATOM   6123 H  HB3  . ALA   B 1 124 ? 41.116 -22.914 -7.009  1.00 13.78 ?  124 ALA   B HB3  1 
ATOM   6124 N  N    . PRO   B 1 125 ? 43.731 -24.472 -5.229  1.00 10.92 ?  125 PRO   B N    1 
ATOM   6125 C  CA   . PRO   B 1 125 ? 43.669 -25.836 -4.706  1.00 11.58 ?  125 PRO   B CA   1 
ATOM   6126 C  C    . PRO   B 1 125 ? 42.271 -26.109 -4.155  1.00 11.75 ?  125 PRO   B C    1 
ATOM   6127 O  O    . PRO   B 1 125 ? 41.470 -25.199 -3.953  1.00 12.23 ?  125 PRO   B O    1 
ATOM   6128 C  CB   . PRO   B 1 125 ? 44.654 -25.755 -3.535  1.00 12.73 ?  125 PRO   B CB   1 
ATOM   6129 C  CG   . PRO   B 1 125 ? 44.391 -24.369 -2.960  1.00 12.93 ?  125 PRO   B CG   1 
ATOM   6130 C  CD   . PRO   B 1 125 ? 44.055 -23.501 -4.166  1.00 11.77 ?  125 PRO   B CD   1 
ATOM   6131 H  HA   . PRO   B 1 125 ? 43.943 -26.506 -5.349  1.00 13.88 ?  125 PRO   B HA   1 
ATOM   6132 H  HB2  . PRO   B 1 125 ? 44.457 -26.444 -2.876  1.00 15.26 ?  125 PRO   B HB2  1 
ATOM   6133 H  HB3  . PRO   B 1 125 ? 45.566 -25.830 -3.852  1.00 15.26 ?  125 PRO   B HB3  1 
ATOM   6134 H  HG2  . PRO   B 1 125 ? 43.639 -24.402 -2.343  1.00 15.50 ?  125 PRO   B HG2  1 
ATOM   6135 H  HG3  . PRO   B 1 125 ? 45.185 -24.041 -2.505  1.00 15.50 ?  125 PRO   B HG3  1 
ATOM   6136 H  HD2  . PRO   B 1 125 ? 43.292 -22.935 -3.976  1.00 14.10 ?  125 PRO   B HD2  1 
ATOM   6137 H  HD3  . PRO   B 1 125 ? 44.832 -22.967 -4.418  1.00 14.10 ?  125 PRO   B HD3  1 
ATOM   6138 N  N    . LEU   B 1 126 ? 42.004 -27.384 -3.872  1.00 12.74 ?  126 LEU   B N    1 
ATOM   6139 C  CA   . LEU   B 1 126 ? 40.783 -27.748 -3.161  1.00 13.37 ?  126 LEU   B CA   1 
ATOM   6140 C  C    . LEU   B 1 126 ? 40.891 -27.344 -1.699  1.00 13.09 ?  126 LEU   B C    1 
ATOM   6141 O  O    . LEU   B 1 126 ? 41.782 -27.805 -0.981  1.00 15.14 ?  126 LEU   B O    1 
ATOM   6142 C  CB   . LEU   B 1 126 ? 40.519 -29.245 -3.271  1.00 14.90 ?  126 LEU   B CB   1 
ATOM   6143 C  CG   . LEU   B 1 126 ? 39.995 -29.728 -4.624  1.00 15.65 ?  126 LEU   B CG   1 
ATOM   6144 C  CD1  . LEU   B 1 126 ? 40.042 -31.238 -4.712  1.00 17.87 ?  126 LEU   B CD1  1 
ATOM   6145 C  CD2  . LEU   B 1 126 ? 38.578 -29.241 -4.879  1.00 16.46 ?  126 LEU   B CD2  1 
ATOM   6146 H  H    . LEU   B 1 126 ? 42.510 -28.050 -4.070  1.00 15.27 ?  126 LEU   B H    1 
ATOM   6147 H  HA   . LEU   B 1 126 ? 40.035 -27.272 -3.547  1.00 16.03 ?  126 LEU   B HA   1 
ATOM   6148 H  HB2  . LEU   B 1 126 ? 41.344 -29.714 -3.094  1.00 17.86 ?  126 LEU   B HB2  1 
ATOM   6149 H  HB3  . LEU   B 1 126 ? 39.856 -29.485 -2.603  1.00 17.86 ?  126 LEU   B HB3  1 
ATOM   6150 H  HG   . LEU   B 1 126 ? 40.563 -29.368 -5.325  1.00 18.75 ?  126 LEU   B HG   1 
ATOM   6151 H  HD11 . LEU   B 1 126 ? 39.706 -31.514 -5.579  1.00 21.42 ?  126 LEU   B HD11 1 
ATOM   6152 H  HD12 . LEU   B 1 126 ? 40.957 -31.533 -4.600  1.00 21.42 ?  126 LEU   B HD12 1 
ATOM   6153 H  HD13 . LEU   B 1 126 ? 39.485 -31.611 -4.009  1.00 21.42 ?  126 LEU   B HD13 1 
ATOM   6154 H  HD21 . LEU   B 1 126 ? 38.249 -29.641 -5.701  1.00 19.74 ?  126 LEU   B HD21 1 
ATOM   6155 H  HD22 . LEU   B 1 126 ? 38.013 -29.500 -4.136  1.00 19.74 ?  126 LEU   B HD22 1 
ATOM   6156 H  HD23 . LEU   B 1 126 ? 38.583 -28.272 -4.967  1.00 19.74 ?  126 LEU   B HD23 1 
ATOM   6157 N  N    . LEU   B 1 127 ? 39.962 -26.510 -1.246  1.00 12.81 ?  127 LEU   B N    1 
ATOM   6158 C  CA   . LEU   B 1 127 ? 40.013 -26.020 0.119   1.00 13.14 ?  127 LEU   B CA   1 
ATOM   6159 C  C    . LEU   B 1 127 ? 39.743 -27.143 1.113   1.00 13.39 ?  127 LEU   B C    1 
ATOM   6160 O  O    . LEU   B 1 127 ? 38.928 -28.047 0.877   1.00 13.76 ?  127 LEU   B O    1 
ATOM   6161 C  CB   . LEU   B 1 127 ? 38.994 -24.899 0.322   1.00 14.26 ?  127 LEU   B CB   1 
ATOM   6162 C  CG   . LEU   B 1 127 ? 39.173 -23.629 -0.508  1.00 14.61 ?  127 LEU   B CG   1 
ATOM   6163 C  CD1  . LEU   B 1 127 ? 38.041 -22.668 -0.191  1.00 14.23 ?  127 LEU   B CD1  1 
ATOM   6164 C  CD2  . LEU   B 1 127 ? 40.525 -22.977 -0.250  1.00 15.49 ?  127 LEU   B CD2  1 
ATOM   6165 H  H    . LEU   B 1 127 ? 39.299 -26.208 -1.707  1.00 15.35 ?  127 LEU   B H    1 
ATOM   6166 H  HA   . LEU   B 1 127 ? 40.896 -25.654 0.296   1.00 15.74 ?  127 LEU   B HA   1 
ATOM   6167 H  HB2  . LEU   B 1 127 ? 38.113 -25.246 0.115   1.00 17.09 ?  127 LEU   B HB2  1 
ATOM   6168 H  HB3  . LEU   B 1 127 ? 39.018 -24.627 1.253   1.00 17.09 ?  127 LEU   B HB3  1 
ATOM   6169 H  HG   . LEU   B 1 127 ? 39.108 -23.840 -1.448  1.00 17.52 ?  127 LEU   B HG   1 
ATOM   6170 H  HD11 . LEU   B 1 127 ? 38.152 -21.852 -0.714  1.00 17.05 ?  127 LEU   B HD11 1 
ATOM   6171 H  HD12 . LEU   B 1 127 ? 37.192 -23.082 -0.411  1.00 17.05 ?  127 LEU   B HD12 1 
ATOM   6172 H  HD13 . LEU   B 1 127 ? 38.062 -22.447 0.757   1.00 17.05 ?  127 LEU   B HD13 1 
ATOM   6173 H  HD21 . LEU   B 1 127 ? 40.564 -22.121 -0.710  1.00 18.57 ?  127 LEU   B HD21 1 
ATOM   6174 H  HD22 . LEU   B 1 127 ? 40.635 -22.840 0.705   1.00 18.57 ?  127 LEU   B HD22 1 
ATOM   6175 H  HD23 . LEU   B 1 127 ? 41.220 -23.562 -0.583  1.00 18.57 ?  127 LEU   B HD23 1 
ATOM   6176 N  N    . SER   B 1 128 ? 40.431 -27.061 2.243   1.00 13.67 ?  128 SER   B N    1 
ATOM   6177 C  CA   . SER   B 1 128 ? 40.318 -27.978 3.364   1.00 14.16 ?  128 SER   B CA   1 
ATOM   6178 C  C    . SER   B 1 128 ? 40.814 -29.382 3.040   1.00 14.97 ?  128 SER   B C    1 
ATOM   6179 O  O    . SER   B 1 128 ? 40.720 -30.260 3.892   1.00 16.31 ?  128 SER   B O    1 
ATOM   6180 C  CB   . SER   B 1 128 ? 38.913 -27.984 3.987   1.00 14.13 ?  128 SER   B CB   1 
ATOM   6181 O  OG   . SER   B 1 128 ? 38.600 -26.709 4.545   1.00 14.76 ?  128 SER   B OG   1 
ATOM   6182 H  H    . SER   B 1 128 ? 41.007 -26.439 2.391   1.00 16.38 ?  128 SER   B H    1 
ATOM   6183 H  HA   . SER   B 1 128 ? 40.903 -27.649 4.052   1.00 16.98 ?  128 SER   B HA   1 
ATOM   6184 H  HB2  . SER   B 1 128 ? 38.255 -28.204 3.305   1.00 16.93 ?  128 SER   B HB2  1 
ATOM   6185 H  HB3  . SER   B 1 128 ? 38.882 -28.659 4.694   1.00 16.93 ?  128 SER   B HB3  1 
ATOM   6186 H  HG   . SER   B 1 128 ? 39.163 -26.519 5.140   1.00 17.69 ?  128 SER   B HG   1 
ATOM   6187 N  N    . ALA   B 1 129 ? 41.392 -29.604 1.857   1.00 16.02 ?  129 ALA   B N    1 
ATOM   6188 C  CA   . ALA   B 1 129 ? 41.934 -30.907 1.501   1.00 16.86 ?  129 ALA   B CA   1 
ATOM   6189 C  C    . ALA   B 1 129 ? 43.326 -31.086 2.097   1.00 16.06 ?  129 ALA   B C    1 
ATOM   6190 O  O    . ALA   B 1 129 ? 43.882 -30.190 2.745   1.00 15.75 ?  129 ALA   B O    1 
ATOM   6191 C  CB   . ALA   B 1 129 ? 41.976 -31.071 -0.016  1.00 18.70 ?  129 ALA   B CB   1 
ATOM   6192 H  H    . ALA   B 1 129 ? 41.487 -29.008 1.241   1.00 19.20 ?  129 ALA   B H    1 
ATOM   6193 H  HA   . ALA   B 1 129 ? 41.360 -31.598 1.861   1.00 20.21 ?  129 ALA   B HA   1 
ATOM   6194 H  HB1  . ALA   B 1 129 ? 42.330 -31.951 -0.229  1.00 22.42 ?  129 ALA   B HB1  1 
ATOM   6195 H  HB2  . ALA   B 1 129 ? 41.079 -30.982 -0.369  1.00 22.42 ?  129 ALA   B HB2  1 
ATOM   6196 H  HB3  . ALA   B 1 129 ? 42.551 -30.386 -0.393  1.00 22.42 ?  129 ALA   B HB3  1 
ATOM   6197 N  N    . GLY   B 1 130 ? 43.896 -32.268 1.862   1.00 16.02 ?  130 GLY   B N    1 
ATOM   6198 C  CA   . GLY   B 1 130 ? 45.284 -32.498 2.219   1.00 17.04 ?  130 GLY   B CA   1 
ATOM   6199 C  C    . GLY   B 1 130 ? 45.493 -32.401 3.713   1.00 16.83 ?  130 GLY   B C    1 
ATOM   6200 O  O    . GLY   B 1 130 ? 44.791 -33.043 4.511   1.00 17.57 ?  130 GLY   B O    1 
ATOM   6201 H  H    . GLY   B 1 130 ? 43.502 -32.942 1.496   1.00 19.21 ?  130 GLY   B H    1 
ATOM   6202 H  HA2  . GLY   B 1 130 ? 45.554 -33.383 1.920   1.00 20.43 ?  130 GLY   B HA2  1 
ATOM   6203 H  HA3  . GLY   B 1 130 ? 45.847 -31.842 1.779   1.00 20.43 ?  130 GLY   B HA3  1 
ATOM   6204 N  N    . ILE   B 1 131 ? 46.470 -31.577 4.101   1.00 17.32 ?  131 ILE   B N    1 
ATOM   6205 C  CA   . ILE   B 1 131 ? 46.832 -31.441 5.501   1.00 18.01 ?  131 ILE   B CA   1 
ATOM   6206 C  C    . ILE   B 1 131 ? 45.717 -30.839 6.339   1.00 17.15 ?  131 ILE   B C    1 
ATOM   6207 O  O    . ILE   B 1 131 ? 45.793 -30.898 7.568   1.00 18.41 ?  131 ILE   B O    1 
ATOM   6208 C  CB   . ILE   B 1 131 ? 48.158 -30.659 5.683   1.00 19.96 ?  131 ILE   B CB   1 
ATOM   6209 C  CG1  . ILE   B 1 131 ? 47.982 -29.175 5.324   1.00 20.76 ?  131 ILE   B CG1  1 
ATOM   6210 C  CG2  . ILE   B 1 131 ? 49.270 -31.294 4.852   1.00 21.04 ?  131 ILE   B CG2  1 
ATOM   6211 C  CD1  . ILE   B 1 131 ? 49.180 -28.299 5.667   1.00 21.64 ?  131 ILE   B CD1  1 
ATOM   6212 H  H    . ILE   B 1 131 ? 46.934 -31.085 3.567   1.00 20.77 ?  131 ILE   B H    1 
ATOM   6213 H  HA   . ILE   B 1 131 ? 46.981 -32.329 5.849   1.00 21.59 ?  131 ILE   B HA   1 
ATOM   6214 H  HB   . ILE   B 1 131 ? 48.408 -30.716 6.619   1.00 23.93 ?  131 ILE   B HB   1 
ATOM   6215 H  HG12 . ILE   B 1 131 ? 47.824 -29.107 4.371   1.00 24.89 ?  131 ILE   B HG12 1 
ATOM   6216 H  HG13 . ILE   B 1 131 ? 47.217 -28.819 5.807   1.00 24.89 ?  131 ILE   B HG13 1 
ATOM   6217 H  HG21 . ILE   B 1 131 ? 50.110 -30.879 5.088   1.00 25.23 ?  131 ILE   B HG21 1 
ATOM   6218 H  HG22 . ILE   B 1 131 ? 49.296 -32.242 5.040   1.00 25.23 ?  131 ILE   B HG22 1 
ATOM   6219 H  HG23 . ILE   B 1 131 ? 49.075 -31.146 3.912   1.00 25.23 ?  131 ILE   B HG23 1 
ATOM   6220 H  HD11 . ILE   B 1 131 ? 48.957 -27.376 5.475   1.00 25.95 ?  131 ILE   B HD11 1 
ATOM   6221 H  HD12 . ILE   B 1 131 ? 49.384 -28.403 6.610   1.00 25.95 ?  131 ILE   B HD12 1 
ATOM   6222 H  HD13 . ILE   B 1 131 ? 49.936 -28.579 5.131   1.00 25.95 ?  131 ILE   B HD13 1 
ATOM   6223 N  N    . PHE   B 1 132 ? 44.684 -30.261 5.709   1.00 16.09 ?  132 PHE   B N    1 
ATOM   6224 C  CA   . PHE   B 1 132 ? 43.520 -29.760 6.436   1.00 16.41 ?  132 PHE   B CA   1 
ATOM   6225 C  C    . PHE   B 1 132 ? 42.496 -30.853 6.763   1.00 17.58 ?  132 PHE   B C    1 
ATOM   6226 O  O    . PHE   B 1 132 ? 41.589 -30.605 7.563   1.00 19.50 ?  132 PHE   B O    1 
ATOM   6227 C  CB   . PHE   B 1 132 ? 42.842 -28.621 5.660   1.00 15.24 ?  132 PHE   B CB   1 
ATOM   6228 C  CG   . PHE   B 1 132 ? 43.541 -27.284 5.774   1.00 15.44 ?  132 PHE   B CG   1 
ATOM   6229 C  CD1  . PHE   B 1 132 ? 44.830 -27.110 5.294   1.00 16.33 ?  132 PHE   B CD1  1 
ATOM   6230 C  CD2  . PHE   B 1 132 ? 42.876 -26.187 6.302   1.00 14.76 ?  132 PHE   B CD2  1 
ATOM   6231 C  CE1  . PHE   B 1 132 ? 45.458 -25.873 5.384   1.00 16.74 ?  132 PHE   B CE1  1 
ATOM   6232 C  CE2  . PHE   B 1 132 ? 43.491 -24.945 6.379   1.00 15.45 ?  132 PHE   B CE2  1 
ATOM   6233 C  CZ   . PHE   B 1 132 ? 44.784 -24.791 5.925   1.00 16.71 ?  132 PHE   B CZ   1 
ATOM   6234 H  H    . PHE   B 1 132 ? 44.633 -30.145 4.855   1.00 19.28 ?  132 PHE   B H    1 
ATOM   6235 H  HA   . PHE   B 1 132 ? 43.824 -29.389 7.276   1.00 19.67 ?  132 PHE   B HA   1 
ATOM   6236 H  HB2  . PHE   B 1 132 ? 42.819 -28.856 4.722   1.00 18.27 ?  132 PHE   B HB2  1 
ATOM   6237 H  HB3  . PHE   B 1 132 ? 41.938 -28.508 5.994   1.00 18.27 ?  132 PHE   B HB3  1 
ATOM   6238 H  HD1  . PHE   B 1 132 ? 45.290 -27.833 4.934   1.00 19.58 ?  132 PHE   B HD1  1 
ATOM   6239 H  HD2  . PHE   B 1 132 ? 42.007 -26.284 6.612   1.00 17.69 ?  132 PHE   B HD2  1 
ATOM   6240 H  HE1  . PHE   B 1 132 ? 46.328 -25.767 5.075   1.00 20.06 ?  132 PHE   B HE1  1 
ATOM   6241 H  HE2  . PHE   B 1 132 ? 43.039 -24.220 6.753   1.00 18.52 ?  132 PHE   B HE2  1 
ATOM   6242 H  HZ   . PHE   B 1 132 ? 45.200 -23.958 5.988   1.00 20.03 ?  132 PHE   B HZ   1 
ATOM   6243 N  N    . GLY   B 1 133 ? 42.595 -32.046 6.161   1.00 17.29 ?  133 GLY   B N    1 
ATOM   6244 C  CA   . GLY   B 1 133 ? 41.884 -33.218 6.648   1.00 18.03 ?  133 GLY   B CA   1 
ATOM   6245 C  C    . GLY   B 1 133 ? 40.488 -33.477 6.114   1.00 18.18 ?  133 GLY   B C    1 
ATOM   6246 O  O    . GLY   B 1 133 ? 39.902 -34.500 6.475   1.00 19.96 ?  133 GLY   B O    1 
ATOM   6247 H  H    . GLY   B 1 133 ? 43.078 -32.190 5.463   1.00 20.72 ?  133 GLY   B H    1 
ATOM   6248 H  HA2  . GLY   B 1 133 ? 42.423 -33.996 6.448   1.00 21.62 ?  133 GLY   B HA2  1 
ATOM   6249 H  HA3  . GLY   B 1 133 ? 41.817 -33.145 7.612   1.00 21.62 ?  133 GLY   B HA3  1 
ATOM   6250 N  N    . ALA   B 1 134 ? 39.927 -32.609 5.281   1.00 17.40 ?  134 ALA   B N    1 
ATOM   6251 C  CA   . ALA   B 1 134 ? 38.602 -32.894 4.753   1.00 17.93 ?  134 ALA   B CA   1 
ATOM   6252 C  C    . ALA   B 1 134 ? 38.685 -33.887 3.600   1.00 17.90 ?  134 ALA   B C    1 
ATOM   6253 O  O    . ALA   B 1 134 ? 39.737 -34.079 2.984   1.00 19.15 ?  134 ALA   B O    1 
ATOM   6254 C  CB   . ALA   B 1 134 ? 37.925 -31.609 4.279   1.00 18.49 ?  134 ALA   B CB   1 
ATOM   6255 H  H    . ALA   B 1 134 ? 40.276 -31.864 5.023   1.00 20.86 ?  134 ALA   B H    1 
ATOM   6256 H  HA   . ALA   B 1 134 ? 38.055 -33.279 5.458   1.00 21.50 ?  134 ALA   B HA   1 
ATOM   6257 H  HB1  . ALA   B 1 134 ? 37.038 -31.825 3.950   1.00 22.16 ?  134 ALA   B HB1  1 
ATOM   6258 H  HB2  . ALA   B 1 134 ? 37.861 -30.989 5.021   1.00 22.16 ?  134 ALA   B HB2  1 
ATOM   6259 H  HB3  . ALA   B 1 134 ? 38.456 -31.219 3.566   1.00 22.16 ?  134 ALA   B HB3  1 
ATOM   6260 N  N    . ASP   B 1 135 ? 37.551 -34.516 3.311   1.00 18.13 ?  135 ASP   B N    1 
ATOM   6261 C  CA   . ASP   B 1 135 ? 37.457 -35.413 2.168   1.00 19.06 ?  135 ASP   B CA   1 
ATOM   6262 C  C    . ASP   B 1 135 ? 37.551 -34.573 0.901   1.00 17.68 ?  135 ASP   B C    1 
ATOM   6263 O  O    . ASP   B 1 135 ? 36.700 -33.697 0.683   1.00 17.53 ?  135 ASP   B O    1 
ATOM   6264 C  CB   . ASP   B 1 135 ? 36.121 -36.152 2.222   1.00 20.78 ?  135 ASP   B CB   1 
ATOM   6265 C  CG   . ASP   B 1 135 ? 35.939 -37.137 1.084   1.00 22.37 ?  135 ASP   B CG   1 
ATOM   6266 O  OD1  . ASP   B 1 135 ? 36.797 -37.181 0.177   1.00 22.23 ?  135 ASP   B OD1  1 
ATOM   6267 O  OD2  . ASP   B 1 135 ? 34.941 -37.895 1.116   1.00 25.59 -1 135 ASP   B OD2  1 
ATOM   6268 H  H    . ASP   B 1 135 ? 36.827 -34.446 3.764   1.00 21.73 ?  135 ASP   B H    1 
ATOM   6269 H  HA   . ASP   B 1 135 ? 38.181 -36.064 2.201   1.00 22.85 ?  135 ASP   B HA   1 
ATOM   6270 H  HB2  . ASP   B 1 135 ? 36.074 -36.653 3.049   1.00 24.92 ?  135 ASP   B HB2  1 
ATOM   6271 H  HB3  . ASP   B 1 135 ? 35.406 -35.505 2.177   1.00 24.92 ?  135 ASP   B HB3  1 
ATOM   6272 N  N    . PRO   B 1 136 ? 38.561 -34.780 0.053   1.00 17.80 ?  136 PRO   B N    1 
ATOM   6273 C  CA   . PRO   B 1 136 ? 38.658 -33.960 -1.164  1.00 17.26 ?  136 PRO   B CA   1 
ATOM   6274 C  C    . PRO   B 1 136 ? 37.464 -34.110 -2.085  1.00 16.32 ?  136 PRO   B C    1 
ATOM   6275 O  O    . PRO   B 1 136 ? 37.141 -33.166 -2.812  1.00 15.79 ?  136 PRO   B O    1 
ATOM   6276 C  CB   . PRO   B 1 136 ? 39.965 -34.442 -1.813  1.00 17.99 ?  136 PRO   B CB   1 
ATOM   6277 C  CG   . PRO   B 1 136 ? 40.166 -35.834 -1.268  1.00 19.20 ?  136 PRO   B CG   1 
ATOM   6278 C  CD   . PRO   B 1 136 ? 39.639 -35.782 0.135   1.00 18.76 ?  136 PRO   B CD   1 
ATOM   6279 H  HA   . PRO   B 1 136 ? 38.752 -33.027 -0.930  1.00 20.69 ?  136 PRO   B HA   1 
ATOM   6280 H  HB2  . PRO   B 1 136 ? 39.867 -34.464 -2.781  1.00 21.57 ?  136 PRO   B HB2  1 
ATOM   6281 H  HB3  . PRO   B 1 136 ? 40.695 -33.860 -1.556  1.00 21.57 ?  136 PRO   B HB3  1 
ATOM   6282 H  HG2  . PRO   B 1 136 ? 39.665 -36.475 -1.797  1.00 23.02 ?  136 PRO   B HG2  1 
ATOM   6283 H  HG3  . PRO   B 1 136 ? 41.112 -36.056 -1.269  1.00 23.02 ?  136 PRO   B HG3  1 
ATOM   6284 H  HD2  . PRO   B 1 136 ? 39.283 -36.648 0.394   1.00 22.49 ?  136 PRO   B HD2  1 
ATOM   6285 H  HD3  . PRO   B 1 136 ? 40.330 -35.485 0.750   1.00 22.49 ?  136 PRO   B HD3  1 
ATOM   6286 N  N    . ILE   B 1 137 ? 36.804 -35.276 -2.085  1.00 16.65 ?  137 ILE   B N    1 
ATOM   6287 C  CA   . ILE   B 1 137 ? 35.589 -35.440 -2.880  1.00 16.82 ?  137 ILE   B CA   1 
ATOM   6288 C  C    . ILE   B 1 137 ? 34.512 -34.471 -2.405  1.00 16.51 ?  137 ILE   B C    1 
ATOM   6289 O  O    . ILE   B 1 137 ? 33.800 -33.854 -3.210  1.00 16.40 ?  137 ILE   B O    1 
ATOM   6290 C  CB   . ILE   B 1 137 ? 35.119 -36.909 -2.824  1.00 19.25 ?  137 ILE   B CB   1 
ATOM   6291 C  CG1  . ILE   B 1 137 ? 36.138 -37.815 -3.524  1.00 21.67 ?  137 ILE   B CG1  1 
ATOM   6292 C  CG2  . ILE   B 1 137 ? 33.722 -37.058 -3.433  1.00 19.82 ?  137 ILE   B CG2  1 
ATOM   6293 C  CD1  . ILE   B 1 137 ? 35.821 -39.301 -3.433  1.00 23.82 ?  137 ILE   B CD1  1 
ATOM   6294 H  H    . ILE   B 1 137 ? 37.030 -35.977 -1.638  1.00 19.96 ?  137 ILE   B H    1 
ATOM   6295 H  HA   . ILE   B 1 137 ? 35.787 -35.235 -3.809  1.00 20.17 ?  137 ILE   B HA   1 
ATOM   6296 H  HB   . ILE   B 1 137 ? 35.065 -37.177 -1.899  1.00 23.07 ?  137 ILE   B HB   1 
ATOM   6297 H  HG12 . ILE   B 1 137 ? 36.175 -37.585 -4.465  1.00 25.98 ?  137 ILE   B HG12 1 
ATOM   6298 H  HG13 . ILE   B 1 137 ? 37.007 -37.679 -3.117  1.00 25.98 ?  137 ILE   B HG13 1 
ATOM   6299 H  HG21 . ILE   B 1 137 ? 33.477 -37.997 -3.468  1.00 23.77 ?  137 ILE   B HG21 1 
ATOM   6300 H  HG22 . ILE   B 1 137 ? 33.078 -36.586 -2.882  1.00 23.77 ?  137 ILE   B HG22 1 
ATOM   6301 H  HG23 . ILE   B 1 137 ? 33.723 -36.688 -4.330  1.00 23.77 ?  137 ILE   B HG23 1 
ATOM   6302 H  HD11 . ILE   B 1 137 ? 36.493 -39.785 -3.933  1.00 28.56 ?  137 ILE   B HD11 1 
ATOM   6303 H  HD12 . ILE   B 1 137 ? 35.836 -39.574 -2.501  1.00 28.56 ?  137 ILE   B HD12 1 
ATOM   6304 H  HD13 . ILE   B 1 137 ? 34.947 -39.474 -3.816  1.00 28.56 ?  137 ILE   B HD13 1 
ATOM   6305 N  N    . HIS   B 1 138 ? 34.380 -34.319 -1.091  1.00 16.66 ?  138 HIS   B N    1 
ATOM   6306 C  CA   . HIS   B 1 138 ? 33.433 -33.349 -0.556  1.00 17.04 ?  138 HIS   B CA   1 
ATOM   6307 C  C    . HIS   B 1 138 ? 33.855 -31.922 -0.878  1.00 16.11 ?  138 HIS   B C    1 
ATOM   6308 O  O    . HIS   B 1 138 ? 33.010 -31.073 -1.181  1.00 16.30 ?  138 HIS   B O    1 
ATOM   6309 C  CB   . HIS   B 1 138 ? 33.312 -33.525 0.950   1.00 18.53 ?  138 HIS   B CB   1 
ATOM   6310 C  CG   . HIS   B 1 138 ? 32.382 -32.544 1.583   1.00 19.78 ?  138 HIS   B CG   1 
ATOM   6311 N  ND1  . HIS   B 1 138 ? 31.043 -32.478 1.260   1.00 21.30 ?  138 HIS   B ND1  1 
ATOM   6312 C  CD2  . HIS   B 1 138 ? 32.598 -31.570 2.499   1.00 20.17 ?  138 HIS   B CD2  1 
ATOM   6313 C  CE1  . HIS   B 1 138 ? 30.472 -31.515 1.960   1.00 21.12 ?  138 HIS   B CE1  1 
ATOM   6314 N  NE2  . HIS   B 1 138 ? 31.392 -30.951 2.722   1.00 20.71 ?  138 HIS   B NE2  1 
ATOM   6315 H  H    . HIS   B 1 138 ? 34.823 -34.757 -0.503  1.00 19.97 ?  138 HIS   B H    1 
ATOM   6316 H  HA   . HIS   B 1 138 ? 32.560 -33.509 -0.952  1.00 20.43 ?  138 HIS   B HA   1 
ATOM   6317 H  HB2  . HIS   B 1 138 ? 32.974 -34.413 1.138   1.00 22.21 ?  138 HIS   B HB2  1 
ATOM   6318 H  HB3  . HIS   B 1 138 ? 34.184 -33.408 1.351   1.00 22.21 ?  138 HIS   B HB3  1 
ATOM   6319 H  HD1  . HIS   B 1 138 ? 30.640 -32.988 0.695   1.00 25.53 ?  138 HIS   B HD1  1 
ATOM   6320 H  HD2  . HIS   B 1 138 ? 33.399 -31.362 2.913   1.00 24.18 ?  138 HIS   B HD2  1 
ATOM   6321 H  HE1  . HIS   B 1 138 ? 29.566 -31.283 1.927   1.00 25.32 ?  138 HIS   B HE1  1 
ATOM   6322 N  N    . SER   B 1 139 ? 35.150 -31.629 -0.810  1.00 15.42 ?  139 SER   B N    1 
ATOM   6323 C  CA   . SER   B 1 139 ? 35.591 -30.279 -1.128  1.00 14.79 ?  139 SER   B CA   1 
ATOM   6324 C  C    . SER   B 1 139 ? 35.253 -29.926 -2.567  1.00 14.17 ?  139 SER   B C    1 
ATOM   6325 O  O    . SER   B 1 139 ? 34.803 -28.812 -2.844  1.00 14.29 ?  139 SER   B O    1 
ATOM   6326 C  CB   . SER   B 1 139 ? 37.087 -30.138 -0.866  1.00 15.36 ?  139 SER   B CB   1 
ATOM   6327 O  OG   . SER   B 1 139 ? 37.495 -28.802 -1.110  1.00 15.46 ?  139 SER   B OG   1 
ATOM   6328 H  H    . SER   B 1 139 ? 35.770 -32.177 -0.599  1.00 18.48 ?  139 SER   B H    1 
ATOM   6329 H  HA   . SER   B 1 139 ? 35.121 -29.654 -0.561  1.00 17.72 ?  139 SER   B HA   1 
ATOM   6330 H  HB2  . SER   B 1 139 ? 37.264 -30.364 0.061   1.00 18.41 ?  139 SER   B HB2  1 
ATOM   6331 H  HB3  . SER   B 1 139 ? 37.572 -30.736 -1.455  1.00 18.41 ?  139 SER   B HB3  1 
ATOM   6332 H  HG   . SER   B 1 139 ? 38.323 -28.726 -0.961  1.00 18.54 ?  139 SER   B HG   1 
ATOM   6333 N  N    . LEU   B 1 140 ? 35.440 -30.872 -3.492  1.00 13.68 ?  140 LEU   B N    1 
ATOM   6334 C  CA   . LEU   B 1 140 ? 35.074 -30.627 -4.882  1.00 13.75 ?  140 LEU   B CA   1 
ATOM   6335 C  C    . LEU   B 1 140 ? 33.575 -30.397 -5.009  1.00 14.02 ?  140 LEU   B C    1 
ATOM   6336 O  O    . LEU   B 1 140 ? 33.137 -29.512 -5.748  1.00 14.33 ?  140 LEU   B O    1 
ATOM   6337 C  CB   . LEU   B 1 140 ? 35.541 -31.790 -5.764  1.00 14.14 ?  140 LEU   B CB   1 
ATOM   6338 C  CG   . LEU   B 1 140 ? 35.185 -31.681 -7.244  1.00 14.43 ?  140 LEU   B CG   1 
ATOM   6339 C  CD1  . LEU   B 1 140 ? 35.756 -30.401 -7.843  1.00 15.15 ?  140 LEU   B CD1  1 
ATOM   6340 C  CD2  . LEU   B 1 140 ? 35.665 -32.912 -7.995  1.00 15.63 ?  140 LEU   B CD2  1 
ATOM   6341 H  H    . LEU   B 1 140 ? 35.772 -31.651 -3.348  1.00 16.40 ?  140 LEU   B H    1 
ATOM   6342 H  HA   . LEU   B 1 140 ? 35.529 -29.827 -5.193  1.00 16.48 ?  140 LEU   B HA   1 
ATOM   6343 H  HB2  . LEU   B 1 140 ? 36.508 -31.858 -5.708  1.00 16.94 ?  140 LEU   B HB2  1 
ATOM   6344 H  HB3  . LEU   B 1 140 ? 35.139 -32.609 -5.437  1.00 16.94 ?  140 LEU   B HB3  1 
ATOM   6345 H  HG   . LEU   B 1 140 ? 34.221 -31.635 -7.332  1.00 17.30 ?  140 LEU   B HG   1 
ATOM   6346 H  HD11 . LEU   B 1 140 ? 35.634 -30.424 -8.805  1.00 18.16 ?  140 LEU   B HD11 1 
ATOM   6347 H  HD12 . LEU   B 1 140 ? 35.287 -29.638 -7.469  1.00 18.16 ?  140 LEU   B HD12 1 
ATOM   6348 H  HD13 . LEU   B 1 140 ? 36.700 -30.348 -7.631  1.00 18.16 ?  140 LEU   B HD13 1 
ATOM   6349 H  HD21 . LEU   B 1 140 ? 35.426 -32.819 -8.932  1.00 18.73 ?  140 LEU   B HD21 1 
ATOM   6350 H  HD22 . LEU   B 1 140 ? 36.623 -32.984 -7.901  1.00 18.73 ?  140 LEU   B HD22 1 
ATOM   6351 H  HD23 . LEU   B 1 140 ? 35.229 -33.692 -7.619  1.00 18.73 ?  140 LEU   B HD23 1 
ATOM   6352 N  N    . ARG   B 1 141 ? 32.775 -31.195 -4.298  1.00 14.19 ?  141 ARG   B N    1 
ATOM   6353 C  CA   . ARG   B 1 141 ? 31.324 -31.016 -4.271  1.00 15.50 ?  141 ARG   B CA   1 
ATOM   6354 C  C    . ARG   B 1 141 ? 30.944 -29.601 -3.844  1.00 14.99 ?  141 ARG   B C    1 
ATOM   6355 O  O    . ARG   B 1 141 ? 30.143 -28.924 -4.507  1.00 15.24 ?  141 ARG   B O    1 
ATOM   6356 C  CB   . ARG   B 1 141 ? 30.744 -32.043 -3.292  1.00 16.92 ?  141 ARG   B CB   1 
ATOM   6357 C  CG   . ARG   B 1 141 ? 29.281 -31.912 -2.957  1.00 18.81 ?  141 ARG   B CG   1 
ATOM   6358 C  CD   . ARG   B 1 141 ? 28.476 -32.553 -4.011  1.00 20.28 ?  141 ARG   B CD   1 
ATOM   6359 N  NE   . ARG   B 1 141 ? 28.215 -31.653 -5.124  1.00 20.68 ?  141 ARG   B NE   1 
ATOM   6360 C  CZ   . ARG   B 1 141 ? 28.215 -32.013 -6.400  1.00 20.72 ?  141 ARG   B CZ   1 
ATOM   6361 N  NH1  . ARG   B 1 141 ? 28.654 -33.202 -6.788  1.00 20.12 ?  141 ARG   B NH1  1 
ATOM   6362 N  NH2  . ARG   B 1 141 ? 27.773 -31.152 -7.313  1.00 21.11 ?  141 ARG   B NH2  1 
ATOM   6363 H  H    . ARG   B 1 141 ? 33.057 -31.847 -3.818  1.00 17.01 ?  141 ARG   B H    1 
ATOM   6364 H  HA   . ARG   B 1 141 ? 30.957 -31.179 -5.149  1.00 18.57 ?  141 ARG   B HA   1 
ATOM   6365 H  HB2  . ARG   B 1 141 ? 30.887 -32.929 -3.663  1.00 20.29 ?  141 ARG   B HB2  1 
ATOM   6366 H  HB3  . ARG   B 1 141 ? 31.233 -31.975 -2.457  1.00 20.29 ?  141 ARG   B HB3  1 
ATOM   6367 H  HG2  . ARG   B 1 141 ? 29.108 -32.352 -2.113  1.00 22.55 ?  141 ARG   B HG2  1 
ATOM   6368 H  HG3  . ARG   B 1 141 ? 29.032 -30.971 -2.899  1.00 22.55 ?  141 ARG   B HG3  1 
ATOM   6369 H  HD2  . ARG   B 1 141 ? 28.948 -33.337 -4.341  1.00 24.31 ?  141 ARG   B HD2  1 
ATOM   6370 H  HD3  . ARG   B 1 141 ? 27.630 -32.825 -3.632  1.00 24.31 ?  141 ARG   B HD3  1 
ATOM   6371 H  HE   . ARG   B 1 141 ? 28.016 -30.839 -4.937  1.00 24.79 ?  141 ARG   B HE   1 
ATOM   6372 H  HH11 . ARG   B 1 141 ? 28.935 -33.775 -6.211  1.00 24.12 ?  141 ARG   B HH11 1 
ATOM   6373 H  HH12 . ARG   B 1 141 ? 28.656 -33.406 -7.622  1.00 24.12 ?  141 ARG   B HH12 1 
ATOM   6374 H  HH21 . ARG   B 1 141 ? 27.494 -30.374 -7.074  1.00 25.31 ?  141 ARG   B HH21 1 
ATOM   6375 H  HH22 . ARG   B 1 141 ? 27.790 -31.363 -8.148  1.00 25.31 ?  141 ARG   B HH22 1 
ATOM   6376 N  N    . VAL   B 1 142 ? 31.486 -29.152 -2.714  1.00 14.70 ?  142 VAL   B N    1 
ATOM   6377 C  CA   . VAL   B 1 142 ? 31.152 -27.817 -2.230  1.00 14.49 ?  142 VAL   B CA   1 
ATOM   6378 C  C    . VAL   B 1 142 ? 31.622 -26.757 -3.221  1.00 14.33 ?  142 VAL   B C    1 
ATOM   6379 O  O    . VAL   B 1 142 ? 30.918 -25.774 -3.480  1.00 14.70 ?  142 VAL   B O    1 
ATOM   6380 C  CB   . VAL   B 1 142 ? 31.704 -27.586 -0.810  1.00 15.39 ?  142 VAL   B CB   1 
ATOM   6381 C  CG1  . VAL   B 1 142 ? 31.392 -26.159 -0.344  1.00 15.45 ?  142 VAL   B CG1  1 
ATOM   6382 C  CG2  . VAL   B 1 142 ? 31.132 -28.614 0.161   1.00 16.08 ?  142 VAL   B CG2  1 
ATOM   6383 H  H    . VAL   B 1 142 ? 32.043 -29.587 -2.217  1.00 17.62 ?  142 VAL   B H    1 
ATOM   6384 H  HA   . VAL   B 1 142 ? 30.192 -27.747 -2.172  1.00 17.37 ?  142 VAL   B HA   1 
ATOM   6385 H  HB   . VAL   B 1 142 ? 32.671 -27.690 -0.823  1.00 18.45 ?  142 VAL   B HB   1 
ATOM   6386 H  HG11 . VAL   B 1 142 ? 31.571 -26.092 0.605   1.00 18.52 ?  142 VAL   B HG11 1 
ATOM   6387 H  HG12 . VAL   B 1 142 ? 31.957 -25.535 -0.831  1.00 18.52 ?  142 VAL   B HG12 1 
ATOM   6388 H  HG13 . VAL   B 1 142 ? 30.459 -25.969 -0.521  1.00 18.52 ?  142 VAL   B HG13 1 
ATOM   6389 H  HG21 . VAL   B 1 142 ? 31.462 -28.422 1.052   1.00 19.28 ?  142 VAL   B HG21 1 
ATOM   6390 H  HG22 . VAL   B 1 142 ? 30.167 -28.559 0.142   1.00 19.28 ?  142 VAL   B HG22 1 
ATOM   6391 H  HG23 . VAL   B 1 142 ? 31.421 -29.499 -0.115  1.00 19.28 ?  142 VAL   B HG23 1 
ATOM   6392 N  N    . CYS   B 1 143 ? 32.804 -26.951 -3.807  1.00 13.82 ?  143 CYS   B N    1 
ATOM   6393 C  CA   . CYS   B 1 143 ? 33.300 -26.013 -4.811  1.00 13.66 ?  143 CYS   B CA   1 
ATOM   6394 C  C    . CYS   B 1 143 ? 32.306 -25.866 -5.956  1.00 13.79 ?  143 CYS   B C    1 
ATOM   6395 O  O    . CYS   B 1 143 ? 31.900 -24.757 -6.312  1.00 13.81 ?  143 CYS   B O    1 
ATOM   6396 C  CB   . CYS   B 1 143 ? 34.654 -26.503 -5.336  1.00 14.23 ?  143 CYS   B CB   1 
ATOM   6397 S  SG   . CYS   B 1 143 ? 35.417 -25.406 -6.557  1.00 14.46 ?  143 CYS   B SG   1 
ATOM   6398 H  H    . CYS   B 1 143 ? 33.335 -27.604 -3.641  1.00 16.56 ?  143 CYS   B H    1 
ATOM   6399 H  HA   . CYS   B 1 143 ? 33.433 -25.142 -4.407  1.00 16.37 ?  143 CYS   B HA   1 
ATOM   6400 H  HB2  . CYS   B 1 143 ? 35.276 -26.588 -4.593  1.00 17.06 ?  143 CYS   B HB2  1 
ATOM   6401 H  HB3  . CYS   B 1 143 ? 34.538 -27.366 -5.756  1.00 17.06 ?  143 CYS   B HB3  1 
ATOM   6402 H  HG   . CYS   B 1 143 ? 36.492 -25.846 -6.869  1.00 17.33 ?  143 CYS   B HG   1 
ATOM   6403 N  N    . VAL   B 1 144 ? 31.902 -26.988 -6.545  1.00 13.98 ?  144 VAL   B N    1 
ATOM   6404 C  CA   . VAL   B 1 144 ? 30.993 -26.940 -7.686  1.00 14.80 ?  144 VAL   B CA   1 
ATOM   6405 C  C    . VAL   B 1 144 ? 29.653 -26.319 -7.306  1.00 15.14 ?  144 VAL   B C    1 
ATOM   6406 O  O    . VAL   B 1 144 ? 29.031 -25.618 -8.113  1.00 16.66 ?  144 VAL   B O    1 
ATOM   6407 C  CB   . VAL   B 1 144 ? 30.829 -28.356 -8.250  1.00 18.45 ?  144 VAL   B CB   1 
ATOM   6408 C  CG1  . VAL   B 1 144 ? 29.555 -28.480 -9.080  1.00 20.79 ?  144 VAL   B CG1  1 
ATOM   6409 C  CG2  . VAL   B 1 144 ? 32.073 -28.750 -9.037  1.00 18.00 ?  144 VAL   B CG2  1 
ATOM   6410 H  H    . VAL   B 1 144 ? 32.145 -27.781 -6.319  1.00 16.76 ?  144 VAL   B H    1 
ATOM   6411 H  HA   . VAL   B 1 144 ? 31.380 -26.386 -8.382  1.00 17.74 ?  144 VAL   B HA   1 
ATOM   6412 H  HB   . VAL   B 1 144 ? 30.753 -28.975 -7.505  1.00 22.12 ?  144 VAL   B HB   1 
ATOM   6413 H  HG11 . VAL   B 1 144 ? 29.630 -29.273 -9.640  1.00 24.92 ?  144 VAL   B HG11 1 
ATOM   6414 H  HG12 . VAL   B 1 144 ? 28.798 -28.574 -8.484  1.00 24.92 ?  144 VAL   B HG12 1 
ATOM   6415 H  HG13 . VAL   B 1 144 ? 29.461 -27.695 -9.633  1.00 24.92 ?  144 VAL   B HG13 1 
ATOM   6416 H  HG21 . VAL   B 1 144 ? 31.960 -29.650 -9.379  1.00 21.59 ?  144 VAL   B HG21 1 
ATOM   6417 H  HG22 . VAL   B 1 144 ? 32.187 -28.128 -9.776  1.00 21.59 ?  144 VAL   B HG22 1 
ATOM   6418 H  HG23 . VAL   B 1 144 ? 32.844 -28.711 -8.452  1.00 21.59 ?  144 VAL   B HG23 1 
ATOM   6419 N  N    . ASP   B 1 145 ? 29.180 -26.575 -6.090  1.00 15.42 ?  145 ASP   B N    1 
ATOM   6420 C  CA   . ASP   B 1 145 ? 27.871 -26.095 -5.665  1.00 16.16 ?  145 ASP   B CA   1 
ATOM   6421 C  C    . ASP   B 1 145 ? 27.907 -24.670 -5.122  1.00 15.57 ?  145 ASP   B C    1 
ATOM   6422 O  O    . ASP   B 1 145 ? 26.846 -24.125 -4.787  1.00 17.24 ?  145 ASP   B O    1 
ATOM   6423 C  CB   . ASP   B 1 145 ? 27.269 -27.008 -4.587  1.00 17.74 ?  145 ASP   B CB   1 
ATOM   6424 C  CG   . ASP   B 1 145 ? 26.916 -28.390 -5.095  1.00 19.03 ?  145 ASP   B CG   1 
ATOM   6425 O  OD1  . ASP   B 1 145 ? 26.825 -28.597 -6.322  1.00 19.41 ?  145 ASP   B OD1  1 
ATOM   6426 O  OD2  . ASP   B 1 145 ? 26.714 -29.272 -4.240  1.00 21.51 -1 145 ASP   B OD2  1 
ATOM   6427 H  H    . ASP   B 1 145 ? 29.605 -27.017 -5.490  1.00 18.48 ?  145 ASP   B H    1 
ATOM   6428 H  HA   . ASP   B 1 145 ? 27.279 -26.088 -6.432  1.00 19.38 ?  145 ASP   B HA   1 
ATOM   6429 H  HB2  . ASP   B 1 145 ? 27.904 -27.111 -3.873  1.00 21.26 ?  145 ASP   B HB2  1 
ATOM   6430 H  HB3  . ASP   B 1 145 ? 26.453 -26.593 -4.257  1.00 21.26 ?  145 ASP   B HB3  1 
ATOM   6431 N  N    . THR   B 1 146 ? 29.083 -24.059 -5.011  1.00 14.07 ?  146 THR   B N    1 
ATOM   6432 C  CA   . THR   B 1 146 ? 29.211 -22.734 -4.403  1.00 13.58 ?  146 THR   B CA   1 
ATOM   6433 C  C    . THR   B 1 146 ? 29.842 -21.700 -5.319  1.00 13.45 ?  146 THR   B C    1 
ATOM   6434 O  O    . THR   B 1 146 ? 29.387 -20.539 -5.362  1.00 13.60 ?  146 THR   B O    1 
ATOM   6435 C  CB   . THR   B 1 146 ? 30.042 -22.842 -3.118  1.00 13.96 ?  146 THR   B CB   1 
ATOM   6436 O  OG1  . THR   B 1 146 ? 29.465 -23.829 -2.250  1.00 14.12 ?  146 THR   B OG1  1 
ATOM   6437 C  CG2  . THR   B 1 146 ? 30.134 -21.499 -2.408  1.00 14.33 ?  146 THR   B CG2  1 
ATOM   6438 H  H    . THR   B 1 146 ? 29.835 -24.383 -5.287  1.00 16.86 ?  146 THR   B H    1 
ATOM   6439 H  HA   . THR   B 1 146 ? 28.334 -22.408 -4.165  1.00 16.28 ?  146 THR   B HA   1 
ATOM   6440 H  HB   . THR   B 1 146 ? 30.943 -23.113 -3.350  1.00 16.73 ?  146 THR   B HB   1 
ATOM   6441 H  HG1  . THR   B 1 146 ? 29.485 -24.586 -2.628  1.00 16.92 ?  146 THR   B HG1  1 
ATOM   6442 H  HG21 . THR   B 1 146 ? 30.470 -21.624 -1.509  1.00 17.17 ?  146 THR   B HG21 1 
ATOM   6443 H  HG22 . THR   B 1 146 ? 30.742 -20.909 -2.889  1.00 17.17 ?  146 THR   B HG22 1 
ATOM   6444 H  HG23 . THR   B 1 146 ? 29.261 -21.084 -2.367  1.00 17.17 ?  146 THR   B HG23 1 
ATOM   6445 N  N    . VAL   B 1 147 ? 30.907 -22.076 -6.019  1.00 13.25 ?  147 VAL   B N    1 
ATOM   6446 C  CA   . VAL   B 1 147 ? 31.630 -21.133 -6.857  1.00 13.04 ?  147 VAL   B CA   1 
ATOM   6447 C  C    . VAL   B 1 147 ? 30.896 -21.007 -8.179  1.00 13.49 ?  147 VAL   B C    1 
ATOM   6448 O  O    . VAL   B 1 147 ? 30.525 -22.013 -8.803  1.00 14.38 ?  147 VAL   B O    1 
ATOM   6449 C  CB   . VAL   B 1 147 ? 33.082 -21.592 -7.065  1.00 13.37 ?  147 VAL   B CB   1 
ATOM   6450 C  CG1  . VAL   B 1 147 ? 33.842 -20.569 -7.893  1.00 13.04 ?  147 VAL   B CG1  1 
ATOM   6451 C  CG2  . VAL   B 1 147 ? 33.768 -21.807 -5.725  1.00 13.81 ?  147 VAL   B CG2  1 
ATOM   6452 H  H    . VAL   B 1 147 ? 31.234 -22.876 -6.030  1.00 15.88 ?  147 VAL   B H    1 
ATOM   6453 H  HA   . VAL   B 1 147 ? 31.649 -20.263 -6.425  1.00 15.63 ?  147 VAL   B HA   1 
ATOM   6454 H  HB   . VAL   B 1 147 ? 33.088 -22.436 -7.547  1.00 16.02 ?  147 VAL   B HB   1 
ATOM   6455 H  HG11 . VAL   B 1 147 ? 34.787 -20.786 -7.879  1.00 15.63 ?  147 VAL   B HG11 1 
ATOM   6456 H  HG12 . VAL   B 1 147 ? 33.512 -20.585 -8.804  1.00 15.63 ?  147 VAL   B HG12 1 
ATOM   6457 H  HG13 . VAL   B 1 147 ? 33.703 -19.687 -7.506  1.00 15.63 ?  147 VAL   B HG13 1 
ATOM   6458 H  HG21 . VAL   B 1 147 ? 34.707 -22.004 -5.878  1.00 16.55 ?  147 VAL   B HG21 1 
ATOM   6459 H  HG22 . VAL   B 1 147 ? 33.685 -20.997 -5.196  1.00 16.55 ?  147 VAL   B HG22 1 
ATOM   6460 H  HG23 . VAL   B 1 147 ? 33.346 -22.548 -5.266  1.00 16.55 ?  147 VAL   B HG23 1 
ATOM   6461 N  N    . ARG   B 1 148 ? 30.690 -19.759 -8.602  1.00 12.96 ?  148 ARG   B N    1 
ATOM   6462 C  CA   . ARG   B 1 148 ? 30.066 -19.439 -9.873  1.00 13.56 ?  148 ARG   B CA   1 
ATOM   6463 C  C    . ARG   B 1 148 ? 31.021 -18.764 -10.847 1.00 13.50 ?  148 ARG   B C    1 
ATOM   6464 O  O    . ARG   B 1 148 ? 30.729 -18.739 -12.046 1.00 14.69 ?  148 ARG   B O    1 
ATOM   6465 C  CB   . ARG   B 1 148 ? 28.831 -18.552 -9.653  1.00 13.82 ?  148 ARG   B CB   1 
ATOM   6466 C  CG   . ARG   B 1 148 ? 27.750 -19.259 -8.842  1.00 14.64 ?  148 ARG   B CG   1 
ATOM   6467 C  CD   . ARG   B 1 148 ? 26.540 -18.374 -8.539  1.00 15.47 ?  148 ARG   B CD   1 
ATOM   6468 N  NE   . ARG   B 1 148 ? 26.925 -17.171 -7.811  1.00 15.50 ?  148 ARG   B NE   1 
ATOM   6469 C  CZ   . ARG   B 1 148 ? 27.225 -17.131 -6.518  1.00 14.52 ?  148 ARG   B CZ   1 
ATOM   6470 N  NH1  . ARG   B 1 148 ? 27.162 -18.213 -5.756  1.00 14.61 ?  148 ARG   B NH1  1 
ATOM   6471 N  NH2  . ARG   B 1 148 ? 27.624 -15.980 -5.982  1.00 14.24 ?  148 ARG   B NH2  1 
ATOM   6472 H  H    . ARG   B 1 148 ? 30.918 -19.054 -8.148  1.00 15.53 ?  148 ARG   B H    1 
ATOM   6473 H  HA   . ARG   B 1 148 ? 29.765 -20.260 -10.280 1.00 16.25 ?  148 ARG   B HA   1 
ATOM   6474 H  HB2  . ARG   B 1 148 ? 29.091 -17.751 -9.169  1.00 16.57 ?  148 ARG   B HB2  1 
ATOM   6475 H  HB3  . ARG   B 1 148 ? 28.452 -18.313 -10.513 1.00 16.57 ?  148 ARG   B HB3  1 
ATOM   6476 H  HG2  . ARG   B 1 148 ? 27.436 -20.030 -9.342  1.00 17.55 ?  148 ARG   B HG2  1 
ATOM   6477 H  HG3  . ARG   B 1 148 ? 28.126 -19.547 -7.996  1.00 17.55 ?  148 ARG   B HG3  1 
ATOM   6478 H  HD2  . ARG   B 1 148 ? 26.126 -18.106 -9.373  1.00 18.55 ?  148 ARG   B HD2  1 
ATOM   6479 H  HD3  . ARG   B 1 148 ? 25.908 -18.874 -7.996  1.00 18.55 ?  148 ARG   B HD3  1 
ATOM   6480 H  HE   . ARG   B 1 148 ? 26.963 -16.437 -8.249  1.00 18.58 ?  148 ARG   B HE   1 
ATOM   6481 H  HH11 . ARG   B 1 148 ? 26.903 -18.967 -6.087  1.00 17.51 ?  148 ARG   B HH11 1 
ATOM   6482 H  HH12 . ARG   B 1 148 ? 27.355 -18.165 -4.917  1.00 17.51 ?  148 ARG   B HH12 1 
ATOM   6483 H  HH21 . ARG   B 1 148 ? 27.674 -15.276 -6.469  1.00 17.07 ?  148 ARG   B HH21 1 
ATOM   6484 H  HH22 . ARG   B 1 148 ? 27.821 -15.941 -5.146  1.00 17.07 ?  148 ARG   B HH22 1 
ATOM   6485 N  N    . THR   B 1 149 ? 32.132 -18.213 -10.362 1.00 13.26 ?  149 THR   B N    1 
ATOM   6486 C  CA   . THR   B 1 149 ? 33.170 -17.652 -11.212 1.00 13.51 ?  149 THR   B CA   1 
ATOM   6487 C  C    . THR   B 1 149 ? 34.061 -18.788 -11.713 1.00 12.82 ?  149 THR   B C    1 
ATOM   6488 O  O    . THR   B 1 149 ? 33.863 -19.957 -11.373 1.00 13.53 ?  149 THR   B O    1 
ATOM   6489 C  CB   . THR   B 1 149 ? 33.937 -16.593 -10.432 1.00 13.61 ?  149 THR   B CB   1 
ATOM   6490 O  OG1  . THR   B 1 149 ? 34.396 -17.193 -9.220  1.00 13.55 ?  149 THR   B OG1  1 
ATOM   6491 C  CG2  . THR   B 1 149 ? 33.031 -15.406 -10.120 1.00 14.41 ?  149 THR   B CG2  1 
ATOM   6492 H  H    . THR   B 1 149 ? 32.305 -18.154 -9.523  1.00 15.89 ?  149 THR   B H    1 
ATOM   6493 H  HA   . THR   B 1 149 ? 32.758 -17.225 -11.980 1.00 16.19 ?  149 THR   B HA   1 
ATOM   6494 H  HB   . THR   B 1 149 ? 34.696 -16.290 -10.953 1.00 16.31 ?  149 THR   B HB   1 
ATOM   6495 H  HG1  . THR   B 1 149 ? 34.822 -16.627 -8.761  1.00 16.23 ?  149 THR   B HG1  1 
ATOM   6496 H  HG21 . THR   B 1 149 ? 33.532 -14.723 -9.644  1.00 17.27 ?  149 THR   B HG21 1 
ATOM   6497 H  HG22 . THR   B 1 149 ? 32.688 -15.025 -10.944 1.00 17.27 ?  149 THR   B HG22 1 
ATOM   6498 H  HG23 . THR   B 1 149 ? 32.285 -15.689 -9.569  1.00 17.27 ?  149 THR   B HG23 1 
ATOM   6499 N  N    . ASN   B 1 150 ? 35.026 -18.471 -12.565 1.00 13.21 ?  150 ASN   B N    1 
ATOM   6500 C  CA   . ASN   B 1 150 ? 35.785 -19.503 -13.265 1.00 13.65 ?  150 ASN   B CA   1 
ATOM   6501 C  C    . ASN   B 1 150 ? 36.952 -19.950 -12.394 1.00 13.25 ?  150 ASN   B C    1 
ATOM   6502 O  O    . ASN   B 1 150 ? 37.882 -19.176 -12.140 1.00 13.82 ?  150 ASN   B O    1 
ATOM   6503 C  CB   . ASN   B 1 150 ? 36.263 -18.974 -14.610 1.00 15.63 ?  150 ASN   B CB   1 
ATOM   6504 C  CG   . ASN   B 1 150 ? 35.122 -18.744 -15.556 1.00 18.36 ?  150 ASN   B CG   1 
ATOM   6505 O  OD1  . ASN   B 1 150 ? 34.223 -19.568 -15.651 1.00 19.37 ?  150 ASN   B OD1  1 
ATOM   6506 N  ND2  . ASN   B 1 150 ? 35.125 -17.609 -16.232 1.00 20.15 ?  150 ASN   B ND2  1 
ATOM   6507 H  H    . ASN   B 1 150 ? 35.271 -17.665 -12.752 1.00 15.83 ?  150 ASN   B H    1 
ATOM   6508 H  HA   . ASN   B 1 150 ? 35.209 -20.268 -13.427 1.00 16.36 ?  150 ASN   B HA   1 
ATOM   6509 H  HB2  . ASN   B 1 150 ? 36.719 -18.128 -14.476 1.00 18.73 ?  150 ASN   B HB2  1 
ATOM   6510 H  HB3  . ASN   B 1 150 ? 36.864 -19.619 -15.012 1.00 18.73 ?  150 ASN   B HB3  1 
ATOM   6511 H  HD21 . ASN   B 1 150 ? 34.489 -17.433 -16.787 1.00 24.16 ?  150 ASN   B HD21 1 
ATOM   6512 H  HD22 . ASN   B 1 150 ? 35.770 -17.048 -16.132 1.00 24.16 ?  150 ASN   B HD22 1 
ATOM   6513 N  N    . VAL   B 1 151 ? 36.910 -21.198 -11.939 1.00 13.11 ?  151 VAL   B N    1 
ATOM   6514 C  CA   . VAL   B 1 151 ? 37.931 -21.729 -11.049 1.00 13.16 ?  151 VAL   B CA   1 
ATOM   6515 C  C    . VAL   B 1 151 ? 38.640 -22.895 -11.724 1.00 12.80 ?  151 VAL   B C    1 
ATOM   6516 O  O    . VAL   B 1 151 ? 38.001 -23.836 -12.217 1.00 13.71 ?  151 VAL   B O    1 
ATOM   6517 C  CB   . VAL   B 1 151 ? 37.372 -22.075 -9.654  1.00 14.35 ?  151 VAL   B CB   1 
ATOM   6518 C  CG1  . VAL   B 1 151 ? 36.219 -23.078 -9.732  1.00 15.01 ?  151 VAL   B CG1  1 
ATOM   6519 C  CG2  . VAL   B 1 151 ? 38.489 -22.559 -8.740  1.00 14.73 ?  151 VAL   B CG2  1 
ATOM   6520 H  H    . VAL   B 1 151 ? 36.289 -21.763 -12.140 1.00 15.71 ?  151 VAL   B H    1 
ATOM   6521 H  HA   . VAL   B 1 151 ? 38.595 -21.037 -10.917 1.00 15.77 ?  151 VAL   B HA   1 
ATOM   6522 H  HB   . VAL   B 1 151 ? 37.017 -21.259 -9.262  1.00 17.20 ?  151 VAL   B HB   1 
ATOM   6523 H  HG11 . VAL   B 1 151 ? 35.897 -23.265 -8.834  1.00 17.99 ?  151 VAL   B HG11 1 
ATOM   6524 H  HG12 . VAL   B 1 151 ? 35.500 -22.700 -10.265 1.00 17.99 ?  151 VAL   B HG12 1 
ATOM   6525 H  HG13 . VAL   B 1 151 ? 36.536 -23.899 -10.144 1.00 17.99 ?  151 VAL   B HG13 1 
ATOM   6526 H  HG21 . VAL   B 1 151 ? 38.145 -22.637 -7.835  1.00 17.65 ?  151 VAL   B HG21 1 
ATOM   6527 H  HG22 . VAL   B 1 151 ? 38.803 -23.422 -9.049  1.00 17.65 ?  151 VAL   B HG22 1 
ATOM   6528 H  HG23 . VAL   B 1 151 ? 39.217 -21.915 -8.758  1.00 17.65 ?  151 VAL   B HG23 1 
ATOM   6529 N  N    . TYR   B 1 152 ? 39.968 -22.808 -11.741 1.00 12.07 ?  152 TYR   B N    1 
ATOM   6530 C  CA   . TYR   B 1 152 ? 40.875 -23.789 -12.320 1.00 12.38 ?  152 TYR   B CA   1 
ATOM   6531 C  C    . TYR   B 1 152 ? 41.597 -24.467 -11.160 1.00 11.86 ?  152 TYR   B C    1 
ATOM   6532 O  O    . TYR   B 1 152 ? 42.442 -23.849 -10.506 1.00 12.46 ?  152 TYR   B O    1 
ATOM   6533 C  CB   . TYR   B 1 152 ? 41.843 -23.073 -13.263 1.00 13.53 ?  152 TYR   B CB   1 
ATOM   6534 C  CG   . TYR   B 1 152 ? 41.163 -22.615 -14.530 1.00 14.29 ?  152 TYR   B CG   1 
ATOM   6535 C  CD1  . TYR   B 1 152 ? 40.495 -21.395 -14.597 1.00 14.58 ?  152 TYR   B CD1  1 
ATOM   6536 C  CD2  . TYR   B 1 152 ? 41.157 -23.426 -15.653 1.00 15.20 ?  152 TYR   B CD2  1 
ATOM   6537 C  CE1  . TYR   B 1 152 ? 39.855 -20.999 -15.756 1.00 15.65 ?  152 TYR   B CE1  1 
ATOM   6538 C  CE2  . TYR   B 1 152 ? 40.516 -23.045 -16.813 1.00 16.30 ?  152 TYR   B CE2  1 
ATOM   6539 C  CZ   . TYR   B 1 152 ? 39.868 -21.829 -16.863 1.00 16.00 ?  152 TYR   B CZ   1 
ATOM   6540 O  OH   . TYR   B 1 152 ? 39.235 -21.455 -18.024 1.00 18.50 ?  152 TYR   B OH   1 
ATOM   6541 H  H    . TYR   B 1 152 ? 40.399 -22.147 -11.386 1.00 14.46 ?  152 TYR   B H    1 
ATOM   6542 H  HA   . TYR   B 1 152 ? 40.369 -24.454 -12.819 1.00 14.83 ?  152 TYR   B HA   1 
ATOM   6543 H  HB2  . TYR   B 1 152 ? 42.200 -22.292 -12.809 1.00 16.21 ?  152 TYR   B HB2  1 
ATOM   6544 H  HB3  . TYR   B 1 152 ? 42.559 -23.677 -13.502 1.00 16.21 ?  152 TYR   B HB3  1 
ATOM   6545 H  HD1  . TYR   B 1 152 ? 40.479 -20.836 -13.852 1.00 17.47 ?  152 TYR   B HD1  1 
ATOM   6546 H  HD2  . TYR   B 1 152 ? 41.590 -24.250 -15.620 1.00 18.21 ?  152 TYR   B HD2  1 
ATOM   6547 H  HE1  . TYR   B 1 152 ? 39.416 -20.179 -15.794 1.00 18.76 ?  152 TYR   B HE1  1 
ATOM   6548 H  HE2  . TYR   B 1 152 ? 40.534 -23.601 -17.558 1.00 19.54 ?  152 TYR   B HE2  1 
ATOM   6549 H  HH   . TYR   B 1 152 ? 38.888 -20.695 -17.925 1.00 22.18 ?  152 TYR   B HH   1 
ATOM   6550 N  N    . LEU   B 1 153 ? 41.227 -25.724 -10.885 1.00 12.18 ?  153 LEU   B N    1 
ATOM   6551 C  CA   . LEU   B 1 153 ? 41.742 -26.463 -9.743  1.00 11.98 ?  153 LEU   B CA   1 
ATOM   6552 C  C    . LEU   B 1 153 ? 42.973 -27.265 -10.141 1.00 12.59 ?  153 LEU   B C    1 
ATOM   6553 O  O    . LEU   B 1 153 ? 42.953 -27.986 -11.141 1.00 13.65 ?  153 LEU   B O    1 
ATOM   6554 C  CB   . LEU   B 1 153 ? 40.667 -27.421 -9.220  1.00 12.39 ?  153 LEU   B CB   1 
ATOM   6555 C  CG   . LEU   B 1 153 ? 39.403 -26.775 -8.652  1.00 13.55 ?  153 LEU   B CG   1 
ATOM   6556 C  CD1  . LEU   B 1 153 ? 38.303 -27.806 -8.506  1.00 14.38 ?  153 LEU   B CD1  1 
ATOM   6557 C  CD2  . LEU   B 1 153 ? 39.704 -26.113 -7.311  1.00 13.82 ?  153 LEU   B CD2  1 
ATOM   6558 H  H    . LEU   B 1 153 ? 40.654 -26.172 -11.356 1.00 14.59 ?  153 LEU   B H    1 
ATOM   6559 H  HA   . LEU   B 1 153 ? 41.972 -25.843 -9.038  1.00 14.35 ?  153 LEU   B HA   1 
ATOM   6560 H  HB2  . LEU   B 1 153 ? 40.390 -28.001 -9.943  1.00 14.84 ?  153 LEU   B HB2  1 
ATOM   6561 H  HB3  . LEU   B 1 153 ? 41.056 -27.956 -8.507  1.00 14.84 ?  153 LEU   B HB3  1 
ATOM   6562 H  HG   . LEU   B 1 153 ? 39.093 -26.084 -9.260  1.00 16.24 ?  153 LEU   B HG   1 
ATOM   6563 H  HD11 . LEU   B 1 153 ? 37.497 -27.363 -8.191  1.00 17.23 ?  153 LEU   B HD11 1 
ATOM   6564 H  HD12 . LEU   B 1 153 ? 38.141 -28.211 -9.369  1.00 17.23 ?  153 LEU   B HD12 1 
ATOM   6565 H  HD13 . LEU   B 1 153 ? 38.585 -28.475 -7.867  1.00 17.23 ?  153 LEU   B HD13 1 
ATOM   6566 H  HD21 . LEU   B 1 153 ? 38.889 -25.736 -6.945  1.00 16.56 ?  153 LEU   B HD21 1 
ATOM   6567 H  HD22 . LEU   B 1 153 ? 40.059 -26.782 -6.699  1.00 16.56 ?  153 LEU   B HD22 1 
ATOM   6568 H  HD23 . LEU   B 1 153 ? 40.363 -25.410 -7.441  1.00 16.56 ?  153 LEU   B HD23 1 
ATOM   6569 N  N    . ALA   B 1 154 ? 44.027 -27.163 -9.336  1.00 12.62 ?  154 ALA   B N    1 
ATOM   6570 C  CA   . ALA   B 1 154 ? 45.253 -27.927 -9.524  1.00 13.87 ?  154 ALA   B CA   1 
ATOM   6571 C  C    . ALA   B 1 154 ? 45.325 -29.002 -8.446  1.00 14.21 ?  154 ALA   B C    1 
ATOM   6572 O  O    . ALA   B 1 154 ? 45.259 -28.695 -7.248  1.00 15.57 ?  154 ALA   B O    1 
ATOM   6573 C  CB   . ALA   B 1 154 ? 46.474 -27.011 -9.465  1.00 14.69 ?  154 ALA   B CB   1 
ATOM   6574 H  H    . ALA   B 1 154 ? 44.047 -26.637 -8.653  1.00 15.12 ?  154 ALA   B H    1 
ATOM   6575 H  HA   . ALA   B 1 154 ? 45.234 -28.356 -10.390 1.00 16.62 ?  154 ALA   B HA   1 
ATOM   6576 H  HB1  . ALA   B 1 154 ? 47.275 -27.540 -9.591  1.00 17.61 ?  154 ALA   B HB1  1 
ATOM   6577 H  HB2  . ALA   B 1 154 ? 46.406 -26.341 -10.167 1.00 17.61 ?  154 ALA   B HB2  1 
ATOM   6578 H  HB3  . ALA   B 1 154 ? 46.502 -26.571 -8.598  1.00 17.61 ?  154 ALA   B HB3  1 
ATOM   6579 N  N    . VAL   B 1 155 ? 45.438 -30.254 -8.874  1.00 13.36 ?  155 VAL   B N    1 
ATOM   6580 C  CA   . VAL   B 1 155 ? 45.548 -31.399 -7.977  1.00 14.03 ?  155 VAL   B CA   1 
ATOM   6581 C  C    . VAL   B 1 155 ? 46.888 -32.070 -8.259  1.00 13.78 ?  155 VAL   B C    1 
ATOM   6582 O  O    . VAL   B 1 155 ? 47.121 -32.562 -9.370  1.00 15.30 ?  155 VAL   B O    1 
ATOM   6583 C  CB   . VAL   B 1 155 ? 44.389 -32.395 -8.165  1.00 15.27 ?  155 VAL   B CB   1 
ATOM   6584 C  CG1  . VAL   B 1 155 ? 44.563 -33.593 -7.250  1.00 15.39 ?  155 VAL   B CG1  1 
ATOM   6585 C  CG2  . VAL   B 1 155 ? 43.054 -31.704 -7.901  1.00 16.40 ?  155 VAL   B CG2  1 
ATOM   6586 H  H    . VAL   B 1 155 ? 45.467 -30.472 -9.706  1.00 16.01 ?  155 VAL   B H    1 
ATOM   6587 H  HA   . VAL   B 1 155 ? 45.544 -31.092 -7.057  1.00 16.82 ?  155 VAL   B HA   1 
ATOM   6588 H  HB   . VAL   B 1 155 ? 44.385 -32.704 -9.083  1.00 18.30 ?  155 VAL   B HB   1 
ATOM   6589 H  HG11 . VAL   B 1 155 ? 43.736 -34.099 -7.231  1.00 18.44 ?  155 VAL   B HG11 1 
ATOM   6590 H  HG12 . VAL   B 1 155 ? 45.282 -34.150 -7.589  1.00 18.44 ?  155 VAL   B HG12 1 
ATOM   6591 H  HG13 . VAL   B 1 155 ? 44.779 -33.282 -6.356  1.00 18.44 ?  155 VAL   B HG13 1 
ATOM   6592 H  HG21 . VAL   B 1 155 ? 42.341 -32.357 -7.991  1.00 19.66 ?  155 VAL   B HG21 1 
ATOM   6593 H  HG22 . VAL   B 1 155 ? 43.058 -31.344 -7.000  1.00 19.66 ?  155 VAL   B HG22 1 
ATOM   6594 H  HG23 . VAL   B 1 155 ? 42.931 -30.989 -8.543  1.00 19.66 ?  155 VAL   B HG23 1 
ATOM   6595 N  N    . PHE   B 1 156 ? 47.757 -32.105 -7.250  1.00 14.32 ?  156 PHE   B N    1 
ATOM   6596 C  CA   . PHE   B 1 156 ? 49.134 -32.562 -7.456  1.00 15.41 ?  156 PHE   B CA   1 
ATOM   6597 C  C    . PHE   B 1 156 ? 49.226 -34.065 -7.733  1.00 16.44 ?  156 PHE   B C    1 
ATOM   6598 O  O    . PHE   B 1 156 ? 49.942 -34.497 -8.646  1.00 18.29 ?  156 PHE   B O    1 
ATOM   6599 C  CB   . PHE   B 1 156 ? 49.968 -32.185 -6.234  1.00 15.63 ?  156 PHE   B CB   1 
ATOM   6600 C  CG   . PHE   B 1 156 ? 51.396 -32.648 -6.291  1.00 16.16 ?  156 PHE   B CG   1 
ATOM   6601 C  CD1  . PHE   B 1 156 ? 52.276 -32.120 -7.216  1.00 17.72 ?  156 PHE   B CD1  1 
ATOM   6602 C  CD2  . PHE   B 1 156 ? 51.855 -33.599 -5.403  1.00 16.67 ?  156 PHE   B CD2  1 
ATOM   6603 C  CE1  . PHE   B 1 156 ? 53.598 -32.535 -7.257  1.00 18.68 ?  156 PHE   B CE1  1 
ATOM   6604 C  CE2  . PHE   B 1 156 ? 53.171 -34.017 -5.439  1.00 18.02 ?  156 PHE   B CE2  1 
ATOM   6605 C  CZ   . PHE   B 1 156 ? 54.035 -33.487 -6.370  1.00 18.77 ?  156 PHE   B CZ   1 
ATOM   6606 H  H    . PHE   B 1 156 ? 47.578 -31.874 -6.443  1.00 17.16 ?  156 PHE   B H    1 
ATOM   6607 H  HA   . PHE   B 1 156 ? 49.504 -32.100 -8.222  1.00 18.47 ?  156 PHE   B HA   1 
ATOM   6608 H  HB2  . PHE   B 1 156 ? 49.978 -31.218 -6.155  1.00 18.73 ?  156 PHE   B HB2  1 
ATOM   6609 H  HB3  . PHE   B 1 156 ? 49.564 -32.575 -5.445  1.00 18.73 ?  156 PHE   B HB3  1 
ATOM   6610 H  HD1  . PHE   B 1 156 ? 51.984 -31.471 -7.818  1.00 21.24 ?  156 PHE   B HD1  1 
ATOM   6611 H  HD2  . PHE   B 1 156 ? 51.268 -33.961 -4.775  1.00 19.98 ?  156 PHE   B HD2  1 
ATOM   6612 H  HE1  . PHE   B 1 156 ? 54.186 -32.176 -7.885  1.00 22.39 ?  156 PHE   B HE1  1 
ATOM   6613 H  HE2  . PHE   B 1 156 ? 53.467 -34.668 -4.840  1.00 21.60 ?  156 PHE   B HE2  1 
ATOM   6614 H  HZ   . PHE   B 1 156 ? 54.922 -33.775 -6.394  1.00 22.51 ?  156 PHE   B HZ   1 
ATOM   6615 N  N    . ASP   B 1 157 ? 48.564 -34.882 -6.924  1.00 17.18 ?  157 ASP   B N    1 
ATOM   6616 C  CA   . ASP   B 1 157 ? 48.710 -36.330 -7.018  1.00 18.27 ?  157 ASP   B CA   1 
ATOM   6617 C  C    . ASP   B 1 157 ? 47.793 -36.877 -8.106  1.00 18.74 ?  157 ASP   B C    1 
ATOM   6618 O  O    . ASP   B 1 157 ? 46.566 -36.759 -7.999  1.00 17.88 ?  157 ASP   B O    1 
ATOM   6619 C  CB   . ASP   B 1 157 ? 48.346 -36.940 -5.671  1.00 19.65 ?  157 ASP   B CB   1 
ATOM   6620 C  CG   . ASP   B 1 157 ? 48.489 -38.451 -5.651  1.00 21.75 ?  157 ASP   B CG   1 
ATOM   6621 O  OD1  . ASP   B 1 157 ? 48.815 -39.059 -6.699  1.00 22.14 ?  157 ASP   B OD1  1 
ATOM   6622 O  OD2  . ASP   B 1 157 ? 48.282 -39.030 -4.569  1.00 24.09 -1 157 ASP   B OD2  1 
ATOM   6623 H  H    . ASP   B 1 157 ? 48.032 -34.624 -6.307  1.00 20.60 ?  157 ASP   B H    1 
ATOM   6624 H  HA   . ASP   B 1 157 ? 49.631 -36.563 -7.232  1.00 21.91 ?  157 ASP   B HA   1 
ATOM   6625 H  HB2  . ASP   B 1 157 ? 48.919 -36.557 -4.991  1.00 23.56 ?  157 ASP   B HB2  1 
ATOM   6626 H  HB3  . ASP   B 1 157 ? 47.417 -36.728 -5.477  1.00 23.56 ?  157 ASP   B HB3  1 
ATOM   6627 N  N    . LYS   B 1 158 ? 48.384 -37.494 -9.138  1.00 19.92 ?  158 LYS   B N    1 
ATOM   6628 C  CA   . LYS   B 1 158 ? 47.608 -38.110 -10.217 1.00 20.78 ?  158 LYS   B CA   1 
ATOM   6629 C  C    . LYS   B 1 158 ? 46.552 -39.077 -9.684  1.00 20.73 ?  158 LYS   B C    1 
ATOM   6630 O  O    . LYS   B 1 158 ? 45.446 -39.164 -10.232 1.00 20.83 ?  158 LYS   B O    1 
ATOM   6631 C  CB   . LYS   B 1 158 ? 48.554 -38.827 -11.189 1.00 22.34 ?  158 LYS   B CB   1 
ATOM   6632 C  CG   . LYS   B 1 158 ? 47.873 -39.724 -12.217 1.00 24.16 ?  158 LYS   B CG   1 
ATOM   6633 C  CD   . LYS   B 1 158 ? 47.022 -38.936 -13.193 1.00 26.28 ?  158 LYS   B CD   1 
ATOM   6634 C  CE   . LYS   B 1 158 ? 46.423 -39.848 -14.252 1.00 28.23 ?  158 LYS   B CE   1 
ATOM   6635 N  NZ   . LYS   B 1 158 ? 45.328 -39.182 -15.014 1.00 28.54 ?  158 LYS   B NZ   1 
ATOM   6636 H  H    . LYS   B 1 158 ? 49.238 -37.569 -9.239  1.00 23.89 ?  158 LYS   B H    1 
ATOM   6637 H  HA   . LYS   B 1 158 ? 47.154 -37.411 -10.716 1.00 24.91 ?  158 LYS   B HA   1 
ATOM   6638 H  HB2  . LYS   B 1 158 ? 49.060 -38.158 -11.684 1.00 26.79 ?  158 LYS   B HB2  1 
ATOM   6639 H  HB3  . LYS   B 1 158 ? 49.165 -39.380 -10.680 1.00 26.79 ?  158 LYS   B HB3  1 
ATOM   6640 H  HG2  . LYS   B 1 158 ? 48.557 -40.186 -12.728 1.00 28.97 ?  158 LYS   B HG2  1 
ATOM   6641 H  HG3  . LYS   B 1 158 ? 47.309 -40.375 -11.770 1.00 28.97 ?  158 LYS   B HG3  1 
ATOM   6642 H  HD2  . LYS   B 1 158 ? 46.297 -38.505 -12.713 1.00 31.52 ?  158 LYS   B HD2  1 
ATOM   6643 H  HD3  . LYS   B 1 158 ? 47.573 -38.272 -13.638 1.00 31.52 ?  158 LYS   B HD3  1 
ATOM   6644 H  HE2  . LYS   B 1 158 ? 47.115 -40.104 -14.881 1.00 33.86 ?  158 LYS   B HE2  1 
ATOM   6645 H  HE3  . LYS   B 1 158 ? 46.055 -40.637 -13.823 1.00 33.86 ?  158 LYS   B HE3  1 
ATOM   6646 H  HZ1  . LYS   B 1 158 ? 44.998 -39.739 -15.624 1.00 34.23 ?  158 LYS   B HZ1  1 
ATOM   6647 H  HZ2  . LYS   B 1 158 ? 44.675 -38.939 -14.460 1.00 34.23 ?  158 LYS   B HZ2  1 
ATOM   6648 H  HZ3  . LYS   B 1 158 ? 45.642 -38.456 -15.424 1.00 34.23 ?  158 LYS   B HZ3  1 
ATOM   6649 N  N    . ASN   B 1 159 ? 46.875 -39.836 -8.635  1.00 20.87 ?  159 ASN   B N    1 
ATOM   6650 C  CA   . ASN   B 1 159 ? 45.919 -40.818 -8.128  1.00 21.30 ?  159 ASN   B CA   1 
ATOM   6651 C  C    . ASN   B 1 159 ? 44.718 -40.144 -7.461  1.00 20.23 ?  159 ASN   B C    1 
ATOM   6652 O  O    . ASN   B 1 159 ? 43.584 -40.630 -7.573  1.00 20.75 ?  159 ASN   B O    1 
ATOM   6653 C  CB   . ASN   B 1 159 ? 46.625 -41.789 -7.189  1.00 23.00 ?  159 ASN   B CB   1 
ATOM   6654 C  CG   . ASN   B 1 159 ? 47.651 -42.644 -7.907  1.00 24.45 ?  159 ASN   B CG   1 
ATOM   6655 O  OD1  . ASN   B 1 159 ? 47.404 -43.134 -9.018  1.00 25.75 ?  159 ASN   B OD1  1 
ATOM   6656 N  ND2  . ASN   B 1 159 ? 48.809 -42.836 -7.277  1.00 25.58 ?  159 ASN   B ND2  1 
ATOM   6657 H  H    . ASN   B 1 159 ? 47.624 -39.795 -8.220  1.00 25.02 ?  159 ASN   B H    1 
ATOM   6658 H  HA   . ASN   B 1 159 ? 45.588 -41.329 -8.883  1.00 25.54 ?  159 ASN   B HA   1 
ATOM   6659 H  HB2  . ASN   B 1 159 ? 47.082 -41.288 -6.498  1.00 27.58 ?  159 ASN   B HB2  1 
ATOM   6660 H  HB3  . ASN   B 1 159 ? 45.968 -42.381 -6.800  1.00 27.58 ?  159 ASN   B HB3  1 
ATOM   6661 H  HD21 . ASN   B 1 159 ? 49.427 -43.317 -7.641  1.00 30.68 ?  159 ASN   B HD21 1 
ATOM   6662 H  HD22 . ASN   B 1 159 ? 48.940 -42.497 -6.497  1.00 30.68 ?  159 ASN   B HD22 1 
ATOM   6663 N  N    . LEU   B 1 160 ? 44.932 -39.013 -6.777  1.00 19.12 ?  160 LEU   B N    1 
ATOM   6664 C  CA   . LEU   B 1 160 ? 43.797 -38.278 -6.231  1.00 17.96 ?  160 LEU   B CA   1 
ATOM   6665 C  C    . LEU   B 1 160 ? 43.008 -37.606 -7.343  1.00 17.32 ?  160 LEU   B C    1 
ATOM   6666 O  O    . LEU   B 1 160 ? 41.771 -37.615 -7.328  1.00 16.80 ?  160 LEU   B O    1 
ATOM   6667 C  CB   . LEU   B 1 160 ? 44.266 -37.244 -5.206  1.00 17.69 ?  160 LEU   B CB   1 
ATOM   6668 C  CG   . LEU   B 1 160 ? 43.134 -36.347 -4.679  1.00 17.63 ?  160 LEU   B CG   1 
ATOM   6669 C  CD1  . LEU   B 1 160 ? 42.011 -37.170 -4.063  1.00 18.69 ?  160 LEU   B CD1  1 
ATOM   6670 C  CD2  . LEU   B 1 160 ? 43.666 -35.340 -3.673  1.00 17.85 ?  160 LEU   B CD2  1 
ATOM   6671 H  H    . LEU   B 1 160 ? 45.706 -38.662 -6.628  1.00 22.92 ?  160 LEU   B H    1 
ATOM   6672 H  HA   . LEU   B 1 160 ? 43.210 -38.903 -5.788  1.00 21.53 ?  160 LEU   B HA   1 
ATOM   6673 H  HB2  . LEU   B 1 160 ? 44.658 -37.715 -4.451  1.00 21.21 ?  160 LEU   B HB2  1 
ATOM   6674 H  HB3  . LEU   B 1 160 ? 44.937 -36.675 -5.619  1.00 21.21 ?  160 LEU   B HB3  1 
ATOM   6675 H  HG   . LEU   B 1 160 ? 42.763 -35.851 -5.421  1.00 21.13 ?  160 LEU   B HG   1 
ATOM   6676 H  HD11 . LEU   B 1 160 ? 41.380 -36.571 -3.639  1.00 22.40 ?  160 LEU   B HD11 1 
ATOM   6677 H  HD12 . LEU   B 1 160 ? 41.564 -37.679 -4.761  1.00 22.40 ?  160 LEU   B HD12 1 
ATOM   6678 H  HD13 . LEU   B 1 160 ? 42.385 -37.778 -3.403  1.00 22.40 ?  160 LEU   B HD13 1 
ATOM   6679 H  HD21 . LEU   B 1 160 ? 42.931 -34.781 -3.377  1.00 21.40 ?  160 LEU   B HD21 1 
ATOM   6680 H  HD22 . LEU   B 1 160 ? 44.047 -35.814 -2.920  1.00 21.40 ?  160 LEU   B HD22 1 
ATOM   6681 H  HD23 . LEU   B 1 160 ? 44.344 -34.795 -4.102  1.00 21.40 ?  160 LEU   B HD23 1 
ATOM   6682 N  N    . TYR   B 1 161 ? 43.707 -37.031 -8.327  1.00 17.20 ?  161 TYR   B N    1 
ATOM   6683 C  CA   . TYR   B 1 161 ? 43.038 -36.466 -9.494  1.00 17.52 ?  161 TYR   B CA   1 
ATOM   6684 C  C    . TYR   B 1 161 ? 42.092 -37.487 -10.116 1.00 17.57 ?  161 TYR   B C    1 
ATOM   6685 O  O    . TYR   B 1 161 ? 40.920 -37.193 -10.376 1.00 17.51 ?  161 TYR   B O    1 
ATOM   6686 C  CB   . TYR   B 1 161 ? 44.082 -35.999 -10.517 1.00 17.97 ?  161 TYR   B CB   1 
ATOM   6687 C  CG   . TYR   B 1 161 ? 43.499 -35.529 -11.831 1.00 18.37 ?  161 TYR   B CG   1 
ATOM   6688 C  CD1  . TYR   B 1 161 ? 43.110 -34.207 -11.998 1.00 18.64 ?  161 TYR   B CD1  1 
ATOM   6689 C  CD2  . TYR   B 1 161 ? 43.326 -36.403 -12.901 1.00 19.30 ?  161 TYR   B CD2  1 
ATOM   6690 C  CE1  . TYR   B 1 161 ? 42.576 -33.768 -13.183 1.00 19.70 ?  161 TYR   B CE1  1 
ATOM   6691 C  CE2  . TYR   B 1 161 ? 42.789 -35.970 -14.093 1.00 20.09 ?  161 TYR   B CE2  1 
ATOM   6692 C  CZ   . TYR   B 1 161 ? 42.413 -34.651 -14.228 1.00 20.18 ?  161 TYR   B CZ   1 
ATOM   6693 O  OH   . TYR   B 1 161 ? 41.872 -34.209 -15.411 1.00 22.17 ?  161 TYR   B OH   1 
ATOM   6694 H  H    . TYR   B 1 161 ? 44.562 -36.963 -8.346  1.00 20.62 ?  161 TYR   B H    1 
ATOM   6695 H  HA   . TYR   B 1 161 ? 42.515 -35.698 -9.228  1.00 21.01 ?  161 TYR   B HA   1 
ATOM   6696 H  HB2  . TYR   B 1 161 ? 44.580 -35.258 -10.138 1.00 21.54 ?  161 TYR   B HB2  1 
ATOM   6697 H  HB3  . TYR   B 1 161 ? 44.684 -36.733 -10.712 1.00 21.54 ?  161 TYR   B HB3  1 
ATOM   6698 H  HD1  . TYR   B 1 161 ? 43.219 -33.601 -11.299 1.00 22.35 ?  161 TYR   B HD1  1 
ATOM   6699 H  HD2  . TYR   B 1 161 ? 43.571 -37.296 -12.815 1.00 23.14 ?  161 TYR   B HD2  1 
ATOM   6700 H  HE1  . TYR   B 1 161 ? 42.325 -32.874 -13.277 1.00 23.62 ?  161 TYR   B HE1  1 
ATOM   6701 H  HE2  . TYR   B 1 161 ? 42.673 -36.564 -14.801 1.00 24.09 ?  161 TYR   B HE2  1 
ATOM   6702 H  HH   . TYR   B 1 161 ? 41.829 -34.844 -15.961 1.00 26.58 ?  161 TYR   B HH   1 
ATOM   6703 N  N    . ASP   B 1 162 ? 42.587 -38.708 -10.340 1.00 17.95 ?  162 ASP   B N    1 
ATOM   6704 C  CA   . ASP   B 1 162 ? 41.763 -39.747 -10.955 1.00 18.34 ?  162 ASP   B CA   1 
ATOM   6705 C  C    . ASP   B 1 162 ? 40.556 -40.088 -10.088 1.00 17.59 ?  162 ASP   B C    1 
ATOM   6706 O  O    . ASP   B 1 162 ? 39.453 -40.304 -10.604 1.00 18.00 ?  162 ASP   B O    1 
ATOM   6707 C  CB   . ASP   B 1 162 ? 42.597 -41.008 -11.206 1.00 19.92 ?  162 ASP   B CB   1 
ATOM   6708 C  CG   . ASP   B 1 162 ? 43.604 -40.844 -12.334 1.00 21.13 ?  162 ASP   B CG   1 
ATOM   6709 O  OD1  . ASP   B 1 162 ? 43.469 -39.901 -13.137 1.00 21.66 ?  162 ASP   B OD1  1 
ATOM   6710 O  OD2  . ASP   B 1 162 ? 44.520 -41.688 -12.433 1.00 22.87 -1 162 ASP   B OD2  1 
ATOM   6711 H  H    . ASP   B 1 162 ? 43.386 -38.954 -10.153 1.00 21.52 ?  162 ASP   B H    1 
ATOM   6712 H  HA   . ASP   B 1 162 ? 41.435 -39.429 -11.811 1.00 21.99 ?  162 ASP   B HA   1 
ATOM   6713 H  HB2  . ASP   B 1 162 ? 43.093 -41.224 -10.404 1.00 23.88 ?  162 ASP   B HB2  1 
ATOM   6714 H  HB3  . ASP   B 1 162 ? 42.003 -41.738 -11.440 1.00 23.88 ?  162 ASP   B HB3  1 
ATOM   6715 N  N    A LYS   B 1 163 ? 40.747 -40.158 -8.769  0.70 16.83 ?  163 LYS   B N    1 
ATOM   6716 N  N    B LYS   B 1 163 ? 40.744 -40.146 -8.768  0.30 17.83 ?  163 LYS   B N    1 
ATOM   6717 C  CA   A LYS   B 1 163 ? 39.624 -40.429 -7.879  0.70 17.17 ?  163 LYS   B CA   1 
ATOM   6718 C  CA   B LYS   B 1 163 ? 39.622 -40.430 -7.879  0.30 18.18 ?  163 LYS   B CA   1 
ATOM   6719 C  C    A LYS   B 1 163 ? 38.582 -39.318 -7.944  0.70 16.40 ?  163 LYS   B C    1 
ATOM   6720 C  C    B LYS   B 1 163 ? 38.583 -39.315 -7.924  0.30 16.84 ?  163 LYS   B C    1 
ATOM   6721 O  O    A LYS   B 1 163 ? 37.372 -39.586 -7.940  0.70 17.20 ?  163 LYS   B O    1 
ATOM   6722 O  O    B LYS   B 1 163 ? 37.374 -39.581 -7.891  0.30 16.90 ?  163 LYS   B O    1 
ATOM   6723 C  CB   A LYS   B 1 163 ? 40.112 -40.609 -6.443  0.70 19.50 ?  163 LYS   B CB   1 
ATOM   6724 C  CB   B LYS   B 1 163 ? 40.122 -40.632 -6.450  0.30 20.33 ?  163 LYS   B CB   1 
ATOM   6725 C  CG   A LYS   B 1 163 ? 39.032 -41.139 -5.519  0.70 23.40 ?  163 LYS   B CG   1 
ATOM   6726 C  CG   B LYS   B 1 163 ? 39.044 -41.123 -5.503  0.30 22.93 ?  163 LYS   B CG   1 
ATOM   6727 C  CD   A LYS   B 1 163 ? 39.461 -41.176 -4.065  0.70 26.31 ?  163 LYS   B CD   1 
ATOM   6728 C  CD   B LYS   B 1 163 ? 39.555 -41.303 -4.087  0.30 25.20 ?  163 LYS   B CD   1 
ATOM   6729 C  CE   A LYS   B 1 163 ? 38.392 -41.859 -3.220  0.70 28.67 ?  163 LYS   B CE   1 
ATOM   6730 C  CE   B LYS   B 1 163 ? 38.509 -42.000 -3.233  0.30 26.52 ?  163 LYS   B CE   1 
ATOM   6731 N  NZ   A LYS   B 1 163 ? 38.520 -41.553 -1.769  0.70 31.25 ?  163 LYS   B NZ   1 
ATOM   6732 N  NZ   B LYS   B 1 163 ? 38.698 -41.747 -1.779  0.30 28.16 ?  163 LYS   B NZ   1 
ATOM   6733 H  H    A LYS   B 1 163 ? 41.506 -40.055 -8.377  0.70 20.18 ?  163 LYS   B H    1 
ATOM   6734 H  H    B LYS   B 1 163 ? 41.499 -40.029 -8.373  0.30 21.37 ?  163 LYS   B H    1 
ATOM   6735 H  HA   A LYS   B 1 163 ? 39.200 -41.255 -8.158  0.70 20.58 ?  163 LYS   B HA   1 
ATOM   6736 H  HA   B LYS   B 1 163 ? 39.194 -41.250 -8.166  0.30 21.79 ?  163 LYS   B HA   1 
ATOM   6737 H  HB2  A LYS   B 1 163 ? 40.848 -41.244 -6.437  0.70 23.38 ?  163 LYS   B HB2  1 
ATOM   6738 H  HB2  B LYS   B 1 163 ? 40.834 -41.291 -6.456  0.30 24.38 ?  163 LYS   B HB2  1 
ATOM   6739 H  HB3  A LYS   B 1 163 ? 40.409 -39.755 -6.099  0.70 23.38 ?  163 LYS   B HB3  1 
ATOM   6740 H  HB3  B LYS   B 1 163 ? 40.456 -39.788 -6.110  0.30 24.38 ?  163 LYS   B HB3  1 
ATOM   6741 H  HG2  A LYS   B 1 163 ? 38.250 -40.570 -5.584  0.70 28.06 ?  163 LYS   B HG2  1 
ATOM   6742 H  HG2  B LYS   B 1 163 ? 38.321 -40.476 -5.480  0.30 27.49 ?  163 LYS   B HG2  1 
ATOM   6743 H  HG3  A LYS   B 1 163 ? 38.803 -42.045 -5.787  0.70 28.06 ?  163 LYS   B HG3  1 
ATOM   6744 H  HG3  B LYS   B 1 163 ? 38.713 -41.980 -5.815  0.30 27.49 ?  163 LYS   B HG3  1 
ATOM   6745 H  HD2  A LYS   B 1 163 ? 40.286 -41.681 -3.984  0.70 31.56 ?  163 LYS   B HD2  1 
ATOM   6746 H  HD2  B LYS   B 1 163 ? 40.357 -41.850 -4.099  0.30 30.22 ?  163 LYS   B HD2  1 
ATOM   6747 H  HD3  A LYS   B 1 163 ? 39.581 -40.271 -3.740  0.70 31.56 ?  163 LYS   B HD3  1 
ATOM   6748 H  HD3  B LYS   B 1 163 ? 39.743 -40.435 -3.697  0.30 30.22 ?  163 LYS   B HD3  1 
ATOM   6749 H  HE2  A LYS   B 1 163 ? 37.515 -41.573 -3.518  0.70 34.39 ?  163 LYS   B HE2  1 
ATOM   6750 H  HE2  B LYS   B 1 163 ? 37.629 -41.678 -3.485  0.30 31.81 ?  163 LYS   B HE2  1 
ATOM   6751 H  HE3  A LYS   B 1 163 ? 38.475 -42.818 -3.330  0.70 34.39 ?  163 LYS   B HE3  1 
ATOM   6752 H  HE3  B LYS   B 1 163 ? 38.567 -42.957 -3.382  0.30 31.81 ?  163 LYS   B HE3  1 
ATOM   6753 H  HZ1  A LYS   B 1 163 ? 37.877 -41.969 -1.314  0.70 37.48 ?  163 LYS   B HZ1  1 
ATOM   6754 H  HZ1  B LYS   B 1 163 ? 38.068 -42.170 -1.314  0.30 33.77 ?  163 LYS   B HZ1  1 
ATOM   6755 H  HZ2  A LYS   B 1 163 ? 39.311 -41.828 -1.470  0.70 37.48 ?  163 LYS   B HZ2  1 
ATOM   6756 H  HZ2  B LYS   B 1 163 ? 39.496 -42.042 -1.521  0.30 33.77 ?  163 LYS   B HZ2  1 
ATOM   6757 H  HZ3  A LYS   B 1 163 ? 38.447 -40.676 -1.636  0.70 37.48 ?  163 LYS   B HZ3  1 
ATOM   6758 H  HZ3  B LYS   B 1 163 ? 38.643 -40.874 -1.614  0.30 33.77 ?  163 LYS   B HZ3  1 
ATOM   6759 N  N    . LEU   B 1 164 ? 39.036 -38.062 -7.992  1.00 15.36 ?  164 LEU   B N    1 
ATOM   6760 C  CA   . LEU   B 1 164 ? 38.118 -36.929 -8.040  1.00 14.76 ?  164 LEU   B CA   1 
ATOM   6761 C  C    . LEU   B 1 164 ? 37.335 -36.914 -9.347  1.00 15.45 ?  164 LEU   B C    1 
ATOM   6762 O  O    . LEU   B 1 164 ? 36.111 -36.714 -9.349  1.00 16.61 ?  164 LEU   B O    1 
ATOM   6763 C  CB   . LEU   B 1 164 ? 38.918 -35.635 -7.879  1.00 14.52 ?  164 LEU   B CB   1 
ATOM   6764 C  CG   . LEU   B 1 164 ? 39.451 -35.349 -6.481  1.00 15.82 ?  164 LEU   B CG   1 
ATOM   6765 C  CD1  . LEU   B 1 164 ? 40.520 -34.267 -6.552  1.00 15.69 ?  164 LEU   B CD1  1 
ATOM   6766 C  CD2  . LEU   B 1 164 ? 38.332 -34.926 -5.547  1.00 17.34 ?  164 LEU   B CD2  1 
ATOM   6767 H  H    A LEU   B 1 164 ? 39.873 -37.844 -7.999  0.70 18.42 ?  164 LEU   B H    1 
ATOM   6768 H  H    B LEU   B 1 164 ? 39.873 -37.846 -8.017  0.30 18.42 ?  164 LEU   B H    1 
ATOM   6769 H  HA   . LEU   B 1 164 ? 37.491 -36.994 -7.312  1.00 17.69 ?  164 LEU   B HA   1 
ATOM   6770 H  HB2  . LEU   B 1 164 ? 39.684 -35.669 -8.478  1.00 17.40 ?  164 LEU   B HB2  1 
ATOM   6771 H  HB3  . LEU   B 1 164 ? 38.351 -34.891 -8.129  1.00 17.40 ?  164 LEU   B HB3  1 
ATOM   6772 H  HG   . LEU   B 1 164 ? 39.865 -36.149 -6.126  1.00 18.97 ?  164 LEU   B HG   1 
ATOM   6773 H  HD11 . LEU   B 1 164 ? 40.844 -34.078 -5.657  1.00 18.81 ?  164 LEU   B HD11 1 
ATOM   6774 H  HD12 . LEU   B 1 164 ? 41.253 -34.574 -7.110  1.00 18.81 ?  164 LEU   B HD12 1 
ATOM   6775 H  HD13 . LEU   B 1 164 ? 40.132 -33.460 -6.936  1.00 18.81 ?  164 LEU   B HD13 1 
ATOM   6776 H  HD21 . LEU   B 1 164 ? 38.710 -34.690 -4.686  1.00 20.78 ?  164 LEU   B HD21 1 
ATOM   6777 H  HD22 . LEU   B 1 164 ? 37.872 -34.163 -5.927  1.00 20.78 ?  164 LEU   B HD22 1 
ATOM   6778 H  HD23 . LEU   B 1 164 ? 37.714 -35.668 -5.443  1.00 20.78 ?  164 LEU   B HD23 1 
ATOM   6779 N  N    . VAL   B 1 165 ? 38.029 -37.089 -10.473 1.00 17.14 ?  165 VAL   B N    1 
ATOM   6780 C  CA   . VAL   B 1 165 ? 37.375 -37.031 -11.776 1.00 18.66 ?  165 VAL   B CA   1 
ATOM   6781 C  C    . VAL   B 1 165 ? 36.449 -38.225 -11.955 1.00 20.57 ?  165 VAL   B C    1 
ATOM   6782 O  O    . VAL   B 1 165 ? 35.285 -38.082 -12.352 1.00 21.53 ?  165 VAL   B O    1 
ATOM   6783 C  CB   . VAL   B 1 165 ? 38.421 -36.952 -12.905 1.00 19.50 ?  165 VAL   B CB   1 
ATOM   6784 C  CG1  . VAL   B 1 165 ? 37.753 -37.065 -14.257 1.00 21.12 ?  165 VAL   B CG1  1 
ATOM   6785 C  CG2  . VAL   B 1 165 ? 39.217 -35.658 -12.814 1.00 19.35 ?  165 VAL   B CG2  1 
ATOM   6786 H  H    . VAL   B 1 165 ? 38.883 -37.232 -10.511 1.00 20.55 ?  165 VAL   B H    1 
ATOM   6787 H  HA   . VAL   B 1 165 ? 36.837 -36.229 -11.823 1.00 22.38 ?  165 VAL   B HA   1 
ATOM   6788 H  HB   . VAL   B 1 165 ? 39.048 -37.687 -12.814 1.00 23.38 ?  165 VAL   B HB   1 
ATOM   6789 H  HG11 . VAL   B 1 165 ? 38.370 -36.766 -14.941 1.00 25.32 ?  165 VAL   B HG11 1 
ATOM   6790 H  HG12 . VAL   B 1 165 ? 37.519 -37.995 -14.412 1.00 25.32 ?  165 VAL   B HG12 1 
ATOM   6791 H  HG13 . VAL   B 1 165 ? 36.957 -36.516 -14.262 1.00 25.32 ?  165 VAL   B HG13 1 
ATOM   6792 H  HG21 . VAL   B 1 165 ? 39.855 -35.621 -13.548 1.00 23.20 ?  165 VAL   B HG21 1 
ATOM   6793 H  HG22 . VAL   B 1 165 ? 38.607 -34.904 -12.874 1.00 23.20 ?  165 VAL   B HG22 1 
ATOM   6794 H  HG23 . VAL   B 1 165 ? 39.691 -35.631 -11.967 1.00 23.20 ?  165 VAL   B HG23 1 
ATOM   6795 N  N    . SER   B 1 166 ? 36.958 -39.429 -11.664 1.00 21.10 ?  166 SER   B N    1 
ATOM   6796 C  CA   . SER   B 1 166 ? 36.205 -40.642 -11.954 1.00 21.88 ?  166 SER   B CA   1 
ATOM   6797 C  C    . SER   B 1 166 ? 34.946 -40.737 -11.108 1.00 22.06 ?  166 SER   B C    1 
ATOM   6798 O  O    . SER   B 1 166 ? 33.985 -41.381 -11.525 1.00 23.54 ?  166 SER   B O    1 
ATOM   6799 C  CB   . SER   B 1 166 ? 37.077 -41.894 -11.783 1.00 22.98 ?  166 SER   B CB   1 
ATOM   6800 O  OG   . SER   B 1 166 ? 37.434 -42.105 -10.427 1.00 22.86 ?  166 SER   B OG   1 
ATOM   6801 H  H    . SER   B 1 166 ? 37.740 -39.564 -11.313 1.00 25.30 ?  166 SER   B H    1 
ATOM   6802 H  HA   . SER   B 1 166 ? 35.937 -40.616 -12.886 1.00 26.23 ?  166 SER   B HA   1 
ATOM   6803 H  HB2  . SER   B 1 166 ? 36.581 -42.666 -12.097 1.00 27.55 ?  166 SER   B HB2  1 
ATOM   6804 H  HB3  . SER   B 1 166 ? 37.886 -41.792 -12.316 1.00 27.55 ?  166 SER   B HB3  1 
ATOM   6805 H  HG   . SER   B 1 166 ? 37.891 -41.454 -10.149 1.00 27.41 ?  166 SER   B HG   1 
ATOM   6806 N  N    . SER   B 1 167 ? 34.921 -40.118 -9.930  1.00 20.62 ?  167 SER   B N    1 
ATOM   6807 C  CA   . SER   B 1 167 ? 33.770 -40.172 -9.037  1.00 20.07 ?  167 SER   B CA   1 
ATOM   6808 C  C    . SER   B 1 167 ? 32.855 -38.950 -9.130  1.00 19.56 ?  167 SER   B C    1 
ATOM   6809 O  O    . SER   B 1 167 ? 31.776 -38.953 -8.526  1.00 20.17 ?  167 SER   B O    1 
ATOM   6810 C  CB   . SER   B 1 167 ? 34.227 -40.356 -7.584  1.00 20.26 ?  167 SER   B CB   1 
ATOM   6811 O  OG   . SER   B 1 167 ? 34.890 -39.187 -7.109  1.00 19.97 ?  167 SER   B OG   1 
ATOM   6812 H  H    . SER   B 1 167 ? 35.575 -39.663 -9.625  1.00 24.72 ?  167 SER   B H    1 
ATOM   6813 H  HA   . SER   B 1 167 ? 33.239 -40.952 -9.275  1.00 24.06 ?  167 SER   B HA   1 
ATOM   6814 H  HB2  . SER   B 1 167 ? 33.449 -40.534 -7.032  1.00 24.29 ?  167 SER   B HB2  1 
ATOM   6815 H  HB3  . SER   B 1 167 ? 34.836 -41.119 -7.542  1.00 24.29 ?  167 SER   B HB3  1 
ATOM   6816 H  HG   . SER   B 1 167 ? 35.571 -39.043 -7.577  1.00 23.94 ?  167 SER   B HG   1 
ATOM   6817 N  N    . PHE   B 1 168 ? 33.234 -37.915 -9.881  1.00 19.47 ?  168 PHE   B N    1 
ATOM   6818 C  CA   . PHE   B 1 168 ? 32.396 -36.717 -9.952  1.00 18.74 ?  168 PHE   B CA   1 
ATOM   6819 C  C    . PHE   B 1 168 ? 31.086 -36.987 -10.689 1.00 16.24 ?  168 PHE   B C    1 
ATOM   6820 O  O    . PHE   B 1 168 ? 30.037 -36.402 -10.352 1.00 17.14 ?  168 PHE   B O    1 
ATOM   6821 C  CB   . PHE   B 1 168 ? 33.158 -35.581 -10.633 1.00 19.99 ?  168 PHE   B CB   1 
ATOM   6822 C  CG   . PHE   B 1 168 ? 32.354 -34.333 -10.770 1.00 19.73 ?  168 PHE   B CG   1 
ATOM   6823 C  CD1  . PHE   B 1 168 ? 32.025 -33.590 -9.646  1.00 21.00 ?  168 PHE   B CD1  1 
ATOM   6824 C  CD2  . PHE   B 1 168 ? 31.910 -33.902 -12.006 1.00 19.12 ?  168 PHE   B CD2  1 
ATOM   6825 C  CE1  . PHE   B 1 168 ? 31.265 -32.441 -9.749  1.00 21.09 ?  168 PHE   B CE1  1 
ATOM   6826 C  CE2  . PHE   B 1 168 ? 31.161 -32.737 -12.123 1.00 20.21 ?  168 PHE   B CE2  1 
ATOM   6827 C  CZ   . PHE   B 1 168 ? 30.837 -32.005 -10.988 1.00 20.62 ?  168 PHE   B CZ   1 
ATOM   6828 H  H    . PHE   B 1 168 ? 33.950 -37.884 -10.352 1.00 23.34 ?  168 PHE   B H    1 
ATOM   6829 H  HA   . PHE   B 1 168 ? 32.173 -36.436 -9.054  1.00 22.47 ?  168 PHE   B HA   1 
ATOM   6830 H  HB2  . PHE   B 1 168 ? 33.944 -35.375 -10.107 1.00 23.97 ?  168 PHE   B HB2  1 
ATOM   6831 H  HB3  . PHE   B 1 168 ? 33.418 -35.866 -11.523 1.00 23.97 ?  168 PHE   B HB3  1 
ATOM   6832 H  HD1  . PHE   B 1 168 ? 32.307 -33.881 -8.809  1.00 25.18 ?  168 PHE   B HD1  1 
ATOM   6833 H  HD2  . PHE   B 1 168 ? 32.127 -34.385 -12.767 1.00 22.92 ?  168 PHE   B HD2  1 
ATOM   6834 H  HE1  . PHE   B 1 168 ? 31.051 -31.955 -8.987  1.00 25.29 ?  168 PHE   B HE1  1 
ATOM   6835 H  HE2  . PHE   B 1 168 ? 30.867 -32.452 -12.960 1.00 24.23 ?  168 PHE   B HE2  1 
ATOM   6836 H  HZ   . PHE   B 1 168 ? 30.326 -31.231 -11.063 1.00 24.72 ?  168 PHE   B HZ   1 
ATOM   6837 N  N    . LEU   B 1 169 ? 31.131 -37.858 -11.694 1.00 17.02 ?  169 LEU   B N    1 
ATOM   6838 C  CA   . LEU   B 1 169 ? 29.957 -38.174 -12.497 1.00 18.96 ?  169 LEU   B CA   1 
ATOM   6839 C  C    . LEU   B 1 169 ? 29.951 -39.606 -13.001 1.00 22.08 ?  169 LEU   B C    1 
ATOM   6840 O  O    . LEU   B 1 169 ? 29.047 -40.000 -13.738 1.00 24.68 ?  169 LEU   B O    1 
ATOM   6841 C  CB   . LEU   B 1 169 ? 29.873 -37.235 -13.698 1.00 21.01 ?  169 LEU   B CB   1 
ATOM   6842 C  CG   . LEU   B 1 169 ? 28.608 -36.381 -13.780 1.00 24.40 ?  169 LEU   B CG   1 
ATOM   6843 C  CD1  . LEU   B 1 169 ? 28.544 -35.701 -15.130 1.00 25.52 ?  169 LEU   B CD1  1 
ATOM   6844 C  CD2  . LEU   B 1 169 ? 27.355 -37.207 -13.532 1.00 24.36 ?  169 LEU   B CD2  1 
ATOM   6845 O  OXT  . LEU   B 1 169 ? 30.849 -40.383 -12.697 1.00 22.61 -1 169 LEU   B OXT  1 
ATOM   6846 H  H    . LEU   B 1 169 ? 31.840 -38.275 -11.943 1.00 20.40 ?  169 LEU   B H    1 
ATOM   6847 H  HA   . LEU   B 1 169 ? 29.170 -38.043 -11.951 1.00 22.73 ?  169 LEU   B HA   1 
ATOM   6848 H  HB2  . LEU   B 1 169 ? 30.629 -36.628 -13.672 1.00 25.19 ?  169 LEU   B HB2  1 
ATOM   6849 H  HB3  . LEU   B 1 169 ? 29.913 -37.764 -14.513 1.00 25.19 ?  169 LEU   B HB3  1 
ATOM   6850 H  HG   . LEU   B 1 169 ? 28.649 -35.688 -13.101 1.00 29.26 ?  169 LEU   B HG   1 
ATOM   6851 H  HD11 . LEU   B 1 169 ? 27.753 -35.140 -15.162 1.00 30.61 ?  169 LEU   B HD11 1 
ATOM   6852 H  HD12 . LEU   B 1 169 ? 29.340 -35.159 -15.246 1.00 30.61 ?  169 LEU   B HD12 1 
ATOM   6853 H  HD13 . LEU   B 1 169 ? 28.500 -36.379 -15.820 1.00 30.61 ?  169 LEU   B HD13 1 
ATOM   6854 H  HD21 . LEU   B 1 169 ? 26.599 -36.778 -13.957 1.00 29.22 ?  169 LEU   B HD21 1 
ATOM   6855 H  HD22 . LEU   B 1 169 ? 27.485 -38.095 -13.905 1.00 29.22 ?  169 LEU   B HD22 1 
ATOM   6856 H  HD23 . LEU   B 1 169 ? 27.207 -37.272 -12.576 1.00 29.22 ?  169 LEU   B HD23 1 
HETATM 6857 C  C1   T TFA   C 2 .   ? 12.143 -1.280  1.468   0.30 11.74 ?  201 TFA   A C1   1 
HETATM 6858 C  C2   T TFA   C 2 .   ? 12.751 -1.722  0.112   0.30 13.67 ?  201 TFA   A C2   1 
HETATM 6859 O  O    T TFA   C 2 .   ? 12.857 -1.536  2.442   0.30 10.52 ?  201 TFA   A O    1 
HETATM 6860 F  F1   T TFA   C 2 .   ? 12.814 -3.065  0.060   0.30 15.36 ?  201 TFA   A F1   1 
HETATM 6861 F  F2   T TFA   C 2 .   ? 12.026 -1.337  -0.952  0.30 14.18 ?  201 TFA   A F2   1 
HETATM 6862 F  F3   T TFA   C 2 .   ? 13.980 -1.234  -0.088  0.30 15.26 ?  201 TFA   A F3   1 
HETATM 6863 O  OXT  T TFA   C 2 .   ? 11.044 -0.732  1.403   0.30 11.89 ?  201 TFA   A OXT  1 
HETATM 6864 N  N2   B A1A9F D 3 .   ? 15.060 0.899   1.750   0.30 13.93 ?  202 A1A9F A N2   1 
HETATM 6865 C  C3   B A1A9F D 3 .   ? 12.789 0.606   -0.459  0.30 15.98 ?  202 A1A9F A C3   1 
HETATM 6866 C  C6   B A1A9F D 3 .   ? 15.993 -1.184  0.851   0.30 15.54 ?  202 A1A9F A C6   1 
HETATM 6867 C  C9   B A1A9F D 3 .   ? 15.438 2.113   5.224   0.30 13.03 ?  202 A1A9F A C9   1 
HETATM 6868 C  C12  B A1A9F D 3 .   ? 15.844 4.269   4.692   0.30 12.23 ?  202 A1A9F A C12  1 
HETATM 6869 C  C1   B A1A9F D 3 .   ? 9.319  1.164   -1.518  0.30 16.78 ?  202 A1A9F A C1   1 
HETATM 6870 C  C10  B A1A9F D 3 .   ? 15.400 2.212   3.807   0.30 13.36 ?  202 A1A9F A C10  1 
HETATM 6871 C  C11  B A1A9F D 3 .   ? 15.669 3.585   3.504   0.30 12.95 ?  202 A1A9F A C11  1 
HETATM 6872 C  C13  B A1A9F D 3 .   ? 12.342 1.752   0.281   0.30 15.81 ?  202 A1A9F A C13  1 
HETATM 6873 C  C2   B A1A9F D 3 .   ? 11.692 0.237   -1.242  0.30 16.06 ?  202 A1A9F A C2   1 
HETATM 6874 C  C4   B A1A9F D 3 .   ? 14.135 -0.030  -0.393  0.30 15.57 ?  202 A1A9F A C4   1 
HETATM 6875 C  C5   B A1A9F D 3 .   ? 14.701 -0.335  1.029   0.30 14.79 ?  202 A1A9F A C5   1 
HETATM 6876 C  C7   B A1A9F D 3 .   ? 15.132 0.992   3.122   0.30 13.99 ?  202 A1A9F A C7   1 
HETATM 6877 C  C8   B A1A9F D 3 .   ? 14.999 -0.099  5.193   0.30 14.49 ?  202 A1A9F A C8   1 
HETATM 6878 N  N1   B A1A9F D 3 .   ? 10.673 1.143   -0.947  0.30 16.11 ?  202 A1A9F A N1   1 
HETATM 6879 N  N3   B A1A9F D 3 .   ? 14.937 -0.164  3.831   0.30 14.53 ?  202 A1A9F A N3   1 
HETATM 6880 N  N4   B A1A9F D 3 .   ? 15.237 0.972   5.964   0.30 13.99 ?  202 A1A9F A N4   1 
HETATM 6881 N  N5   B A1A9F D 3 .   ? 15.704 3.362   5.756   0.30 11.91 ?  202 A1A9F A N5   1 
HETATM 6882 N  N6   B A1A9F D 3 .   ? 11.059 2.059   -0.022  0.30 15.73 ?  202 A1A9F A N6   1 
HETATM 6883 O  O1   B A1A9F D 3 .   ? 15.605 -2.359  0.226   0.30 16.18 ?  202 A1A9F A O1   1 
HETATM 6884 H  H11  B A1A9F D 3 .   ? 15.267 1.732   1.219   0.30 16.69 ?  202 A1A9F A H11  1 
HETATM 6885 H  H9   B A1A9F D 3 .   ? 16.771 -0.641  0.268   0.30 18.62 ?  202 A1A9F A H9   1 
HETATM 6886 H  H8   B A1A9F D 3 .   ? 16.478 -1.389  1.834   0.30 18.62 ?  202 A1A9F A H8   1 
HETATM 6887 H  H14  B A1A9F D 3 .   ? 16.059 5.308   4.888   0.30 14.66 ?  202 A1A9F A H14  1 
HETATM 6888 H  H4   B A1A9F D 3 .   ? 9.049  0.198   -1.985  0.30 20.11 ?  202 A1A9F A H4   1 
HETATM 6889 H  H3   B A1A9F D 3 .   ? 9.221  1.934   -2.303  0.30 20.11 ?  202 A1A9F A H3   1 
HETATM 6890 H  H2   B A1A9F D 3 .   ? 8.565  1.383   -0.747  0.30 20.11 ?  202 A1A9F A H2   1 
HETATM 6891 H  H13  B A1A9F D 3 .   ? 15.713 4.032   2.535   0.30 15.52 ?  202 A1A9F A H13  1 
HETATM 6892 H  H16  B A1A9F D 3 .   ? 12.896 2.333   1.005   0.30 18.95 ?  202 A1A9F A H16  1 
HETATM 6893 H  H5   B A1A9F D 3 .   ? 11.567 -0.569  -1.960  0.30 19.25 ?  202 A1A9F A H5   1 
HETATM 6894 H  H6   B A1A9F D 3 .   ? 14.825 0.597   -0.974  0.30 18.66 ?  202 A1A9F A H6   1 
HETATM 6895 H  H7   B A1A9F D 3 .   ? 14.088 -0.960  -0.982  0.30 18.66 ?  202 A1A9F A H7   1 
HETATM 6896 H  H1   B A1A9F D 3 .   ? 13.924 -0.902  1.612   0.30 17.73 ?  202 A1A9F A H1   1 
HETATM 6897 H  H12  B A1A9F D 3 .   ? 14.827 -1.044  5.728   0.30 17.37 ?  202 A1A9F A H12  1 
HETATM 6898 H  H15  B A1A9F D 3 .   ? 15.784 3.563   6.742   0.30 14.27 ?  202 A1A9F A H15  1 
HETATM 6899 H  H10  B A1A9F D 3 .   ? 16.345 -2.963  0.269   0.30 19.40 ?  202 A1A9F A H10  1 
HETATM 6900 CL CL   B CL    E 4 .   ? 16.059 2.820   -1.270  0.30 18.57 ?  203 CL    A CL   1 
HETATM 6901 O  O    . HOH   F 5 .   ? 14.768 -4.583  20.521  1.00 45.22 ?  301 HOH   A O    1 
HETATM 6902 O  O    . HOH   F 5 .   ? 4.672  3.774   0.627   1.00 22.52 ?  302 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 6.877  -7.961  11.836  1.00 18.83 ?  303 HOH   A O    1 
HETATM 6904 O  O    . HOH   F 5 .   ? 17.073 -18.001 15.035  1.00 26.64 ?  304 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 11.975 0.362   14.713  1.00 34.43 ?  305 HOH   A O    1 
HETATM 6906 O  O    . HOH   F 5 .   ? 34.346 -1.861  12.483  1.00 37.54 ?  306 HOH   A O    1 
HETATM 6907 O  O    . HOH   F 5 .   ? 30.034 -10.078 12.989  1.00 22.55 ?  307 HOH   A O    1 
HETATM 6908 O  O    . HOH   F 5 .   ? 8.863  -12.047 17.134  1.00 42.90 ?  308 HOH   A O    1 
HETATM 6909 O  O    . HOH   F 5 .   ? 13.909 -4.879  17.417  1.00 27.42 ?  309 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 15.081 -12.205 18.652  1.00 41.45 ?  310 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 28.943 0.455   -9.732  1.00 21.63 ?  311 HOH   A O    1 
HETATM 6912 O  O    . HOH   F 5 .   ? 0.765  -4.186  0.139   1.00 30.87 ?  312 HOH   A O    1 
HETATM 6913 O  O    B HOH   F 5 .   ? 15.260 6.927   6.963   0.30 20.22 ?  313 HOH   A O    1 
HETATM 6914 O  O    . HOH   F 5 .   ? 19.896 -12.517 -8.931  1.00 26.50 ?  314 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 20.649 -19.737 -5.066  1.00 26.97 ?  315 HOH   A O    1 
HETATM 6916 O  O    . HOH   F 5 .   ? 31.027 -18.118 7.809   1.00 20.70 ?  316 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 21.284 -2.266  -2.377  1.00 16.78 ?  317 HOH   A O    1 
HETATM 6918 O  O    . HOH   F 5 .   ? 42.484 10.563  5.150   1.00 20.85 ?  318 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 28.306 -0.098  -13.429 1.00 35.33 ?  319 HOH   A O    1 
HETATM 6920 O  O    . HOH   F 5 .   ? 28.192 -6.297  19.629  1.00 43.00 ?  320 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 30.235 -13.328 -8.577  1.00 20.52 ?  321 HOH   A O    1 
HETATM 6922 O  O    . HOH   F 5 .   ? 11.737 -10.869 -10.117 1.00 44.60 ?  322 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 33.520 -16.948 8.091   1.00 20.03 ?  323 HOH   A O    1 
HETATM 6924 O  O    . HOH   F 5 .   ? 24.683 -17.496 12.713  1.00 25.19 ?  324 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 14.674 -13.965 16.686  1.00 24.74 ?  325 HOH   A O    1 
HETATM 6926 O  O    . HOH   F 5 .   ? 14.523 -0.502  -12.155 1.00 22.94 ?  326 HOH   A O    1 
HETATM 6927 O  O    . HOH   F 5 .   ? 7.921  -12.525 -0.871  1.00 21.83 ?  327 HOH   A O    1 
HETATM 6928 O  O    A HOH   F 5 .   ? 14.639 -3.630  3.081   0.70 15.58 ?  328 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 22.322 5.379   18.953  1.00 41.25 ?  329 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? 26.473 -19.337 -1.775  1.00 14.77 ?  330 HOH   A O    1 
HETATM 6931 O  O    . HOH   F 5 .   ? 34.018 -1.053  -8.945  1.00 26.87 ?  331 HOH   A O    1 
HETATM 6932 O  O    . HOH   F 5 .   ? 27.919 0.830   -7.162  1.00 14.46 ?  332 HOH   A O    1 
HETATM 6933 O  O    . HOH   F 5 .   ? 27.472 -10.596 14.063  1.00 18.23 ?  333 HOH   A O    1 
HETATM 6934 O  O    . HOH   F 5 .   ? 22.724 12.507  1.608   1.00 15.38 ?  334 HOH   A O    1 
HETATM 6935 O  O    . HOH   F 5 .   ? 27.350 13.798  2.849   1.00 28.56 ?  335 HOH   A O    1 
HETATM 6936 O  O    . HOH   F 5 .   ? 7.621  -6.092  -6.843  1.00 43.10 ?  336 HOH   A O    1 
HETATM 6937 O  O    . HOH   F 5 .   ? 36.246 -5.074  -0.517  1.00 30.01 ?  337 HOH   A O    1 
HETATM 6938 O  O    . HOH   F 5 .   ? 13.549 -15.236 -7.499  1.00 26.83 ?  338 HOH   A O    1 
HETATM 6939 O  O    . HOH   F 5 .   ? -0.617 -8.405  2.129   1.00 42.67 ?  339 HOH   A O    1 
HETATM 6940 O  O    . HOH   F 5 .   ? 38.290 10.117  7.153   1.00 32.22 ?  340 HOH   A O    1 
HETATM 6941 O  O    . HOH   F 5 .   ? 9.250  -10.138 19.451  1.00 38.45 ?  341 HOH   A O    1 
HETATM 6942 O  O    . HOH   F 5 .   ? 18.884 -21.951 6.944   1.00 33.59 ?  342 HOH   A O    1 
HETATM 6943 O  O    . HOH   F 5 .   ? 9.852  -21.377 5.687   1.00 19.60 ?  343 HOH   A O    1 
HETATM 6944 O  O    . HOH   F 5 .   ? 14.176 -4.563  -11.937 1.00 34.12 ?  344 HOH   A O    1 
HETATM 6945 O  O    A HOH   F 5 .   ? 15.193 4.013   17.801  0.70 38.78 ?  345 HOH   A O    1 
HETATM 6946 O  O    B HOH   F 5 .   ? 14.825 3.949   17.133  0.30 29.16 ?  346 HOH   A O    1 
HETATM 6947 O  O    B HOH   F 5 .   ? 10.971 2.086   11.949  0.30 19.92 ?  347 HOH   A O    1 
HETATM 6948 O  O    . HOH   F 5 .   ? 38.581 4.978   6.944   1.00 16.47 ?  348 HOH   A O    1 
HETATM 6949 O  O    . HOH   F 5 .   ? 37.558 2.805   10.186  1.00 29.49 ?  349 HOH   A O    1 
HETATM 6950 O  O    . HOH   F 5 .   ? 35.767 -12.651 6.837   1.00 15.97 ?  350 HOH   A O    1 
HETATM 6951 O  O    . HOH   F 5 .   ? 24.193 -7.710  14.435  1.00 17.54 ?  351 HOH   A O    1 
HETATM 6952 O  O    . HOH   F 5 .   ? -0.455 -2.871  2.920   1.00 37.49 ?  352 HOH   A O    1 
HETATM 6953 O  O    . HOH   F 5 .   ? 18.646 -19.369 13.544  1.00 35.11 ?  353 HOH   A O    1 
HETATM 6954 O  O    . HOH   F 5 .   ? 26.869 11.431  1.655   1.00 16.90 ?  354 HOH   A O    1 
HETATM 6955 O  O    A HOH   F 5 .   ? 3.598  -9.427  9.716   0.70 23.10 ?  355 HOH   A O    1 
HETATM 6956 O  O    . HOH   F 5 .   ? 32.786 -9.234  5.978   1.00 20.74 ?  356 HOH   A O    1 
HETATM 6957 O  O    . HOH   F 5 .   ? 39.764 -1.038  -5.196  1.00 21.49 ?  357 HOH   A O    1 
HETATM 6958 O  O    . HOH   F 5 .   ? 31.730 8.233   14.828  1.00 24.00 ?  358 HOH   A O    1 
HETATM 6959 O  O    . HOH   F 5 .   ? 24.035 -2.089  -2.091  1.00 10.97 ?  359 HOH   A O    1 
HETATM 6960 O  O    . HOH   F 5 .   ? 25.701 -0.796  -7.360  1.00 16.42 ?  360 HOH   A O    1 
HETATM 6961 O  O    . HOH   F 5 .   ? 42.616 4.296   5.383   1.00 31.43 ?  361 HOH   A O    1 
HETATM 6962 O  O    A HOH   F 5 .   ? 14.282 0.600   6.781   0.70 17.87 ?  362 HOH   A O    1 
HETATM 6963 O  O    . HOH   F 5 .   ? 44.370 7.110   6.431   1.00 26.60 ?  363 HOH   A O    1 
HETATM 6964 O  O    . HOH   F 5 .   ? 17.123 -17.758 -5.026  1.00 27.29 ?  364 HOH   A O    1 
HETATM 6965 O  O    . HOH   F 5 .   ? 11.664 -10.676 17.011  1.00 25.46 ?  365 HOH   A O    1 
HETATM 6966 O  O    . HOH   F 5 .   ? 37.256 -2.843  9.652   1.00 41.66 ?  366 HOH   A O    1 
HETATM 6967 O  O    . HOH   F 5 .   ? 31.806 -9.348  -6.668  1.00 23.02 ?  367 HOH   A O    1 
HETATM 6968 O  O    . HOH   F 5 .   ? 14.332 -21.204 -4.232  1.00 30.14 ?  368 HOH   A O    1 
HETATM 6969 O  O    . HOH   F 5 .   ? 13.206 -1.472  -6.667  1.00 18.21 ?  369 HOH   A O    1 
HETATM 6970 O  O    . HOH   F 5 .   ? 37.343 11.970  4.924   1.00 30.00 ?  370 HOH   A O    1 
HETATM 6971 O  O    . HOH   F 5 .   ? 30.808 3.095   8.262   1.00 12.45 ?  371 HOH   A O    1 
HETATM 6972 O  O    . HOH   F 5 .   ? 31.080 -13.946 -2.506  1.00 14.55 ?  372 HOH   A O    1 
HETATM 6973 O  O    A HOH   F 5 .   ? 24.592 2.052   -7.005  0.70 16.25 ?  373 HOH   A O    1 
HETATM 6974 O  O    . HOH   F 5 .   ? 24.379 3.593   -1.807  1.00 15.70 ?  374 HOH   A O    1 
HETATM 6975 O  O    . HOH   F 5 .   ? 28.507 -10.686 -13.991 1.00 43.42 ?  375 HOH   A O    1 
HETATM 6976 O  O    . HOH   F 5 .   ? 18.614 9.482   9.012   1.00 22.11 ?  376 HOH   A O    1 
HETATM 6977 O  O    . HOH   F 5 .   ? 22.183 -19.260 11.423  1.00 34.22 ?  377 HOH   A O    1 
HETATM 6978 O  O    B HOH   F 5 .   ? 14.883 -2.898  3.412   0.30 17.18 ?  378 HOH   A O    1 
HETATM 6979 O  O    A HOH   F 5 .   ? 17.502 -1.693  0.425   0.70 19.29 ?  379 HOH   A O    1 
HETATM 6980 O  O    . HOH   F 5 .   ? -1.424 -4.872  7.592   1.00 45.37 ?  380 HOH   A O    1 
HETATM 6981 O  O    . HOH   F 5 .   ? 22.624 -11.955 21.780  1.00 47.26 ?  381 HOH   A O    1 
HETATM 6982 O  O    . HOH   F 5 .   ? 21.282 10.307  15.017  1.00 34.23 ?  382 HOH   A O    1 
HETATM 6983 O  O    . HOH   F 5 .   ? 15.499 11.853  7.906   1.00 35.87 ?  383 HOH   A O    1 
HETATM 6984 O  O    . HOH   F 5 .   ? 33.643 -7.138  4.296   1.00 16.93 ?  384 HOH   A O    1 
HETATM 6985 O  O    A HOH   F 5 .   ? 11.073 -0.353  1.915   0.40 19.48 ?  385 HOH   A O    1 
HETATM 6986 O  O    . HOH   F 5 .   ? 16.502 -22.048 0.946   1.00 28.78 ?  386 HOH   A O    1 
HETATM 6987 O  O    . HOH   F 5 .   ? 21.892 -21.911 8.447   1.00 29.59 ?  387 HOH   A O    1 
HETATM 6988 O  O    B HOH   F 5 .   ? 8.968  4.102   0.841   0.30 21.09 ?  388 HOH   A O    1 
HETATM 6989 O  O    . HOH   F 5 .   ? 15.175 -21.543 14.234  1.00 18.74 ?  389 HOH   A O    1 
HETATM 6990 O  O    . HOH   F 5 .   ? 23.928 -15.711 -9.169  1.00 35.38 ?  390 HOH   A O    1 
HETATM 6991 O  O    . HOH   F 5 .   ? 43.956 8.451   -3.101  1.00 27.82 ?  391 HOH   A O    1 
HETATM 6992 O  O    . HOH   F 5 .   ? 6.396  -5.414  11.101  1.00 19.66 ?  392 HOH   A O    1 
HETATM 6993 O  O    T HOH   F 5 .   ? 15.413 -0.398  2.368   0.30 12.51 ?  393 HOH   A O    1 
HETATM 6994 O  O    . HOH   F 5 .   ? 16.975 -19.244 4.901   1.00 15.90 ?  394 HOH   A O    1 
HETATM 6995 O  O    . HOH   F 5 .   ? 14.447 -24.672 11.579  1.00 37.56 ?  395 HOH   A O    1 
HETATM 6996 O  O    . HOH   F 5 .   ? 23.910 -20.273 -1.363  1.00 16.77 ?  396 HOH   A O    1 
HETATM 6997 O  O    . HOH   F 5 .   ? 43.402 7.830   2.688   1.00 26.21 ?  397 HOH   A O    1 
HETATM 6998 O  O    . HOH   F 5 .   ? 31.768 -7.304  -9.876  1.00 22.04 ?  398 HOH   A O    1 
HETATM 6999 O  O    . HOH   F 5 .   ? 14.050 -23.029 7.446   1.00 18.56 ?  399 HOH   A O    1 
HETATM 7000 O  O    . HOH   F 5 .   ? 8.390  -21.671 3.943   1.00 47.09 ?  400 HOH   A O    1 
HETATM 7001 O  O    . HOH   F 5 .   ? 21.321 3.067   -0.298  1.00 14.06 ?  401 HOH   A O    1 
HETATM 7002 O  O    . HOH   F 5 .   ? 27.407 -6.082  -14.005 1.00 38.98 ?  402 HOH   A O    1 
HETATM 7003 O  O    . HOH   F 5 .   ? 31.003 6.201   -12.281 1.00 29.43 ?  403 HOH   A O    1 
HETATM 7004 O  O    B HOH   F 5 .   ? 11.177 -0.973  2.373   0.30 22.26 ?  404 HOH   A O    1 
HETATM 7005 O  O    . HOH   F 5 .   ? 23.491 11.396  4.062   1.00 12.57 ?  405 HOH   A O    1 
HETATM 7006 O  O    . HOH   F 5 .   ? 37.569 -1.982  5.791   1.00 26.31 ?  406 HOH   A O    1 
HETATM 7007 O  O    A HOH   F 5 .   ? 15.806 -0.920  5.253   0.70 18.88 ?  407 HOH   A O    1 
HETATM 7008 O  O    . HOH   F 5 .   ? 6.700  -3.147  12.806  1.00 29.15 ?  408 HOH   A O    1 
HETATM 7009 O  O    . HOH   F 5 .   ? 30.733 1.914   16.680  1.00 21.22 ?  409 HOH   A O    1 
HETATM 7010 O  O    . HOH   F 5 .   ? 27.313 2.352   18.705  1.00 29.05 ?  410 HOH   A O    1 
HETATM 7011 O  O    . HOH   F 5 .   ? 18.856 -0.723  -1.618  1.00 14.52 ?  411 HOH   A O    1 
HETATM 7012 O  O    . HOH   F 5 .   ? 15.835 2.120   24.707  1.00 44.72 ?  412 HOH   A O    1 
HETATM 7013 O  O    . HOH   F 5 .   ? 20.565 -20.008 2.752   1.00 18.90 ?  413 HOH   A O    1 
HETATM 7014 O  O    . HOH   F 5 .   ? 5.414  2.874   4.932   1.00 32.23 ?  414 HOH   A O    1 
HETATM 7015 O  O    . HOH   F 5 .   ? 30.328 -12.892 13.492  1.00 20.60 ?  415 HOH   A O    1 
HETATM 7016 O  O    . HOH   F 5 .   ? 26.936 4.181   -0.691  1.00 13.11 ?  416 HOH   A O    1 
HETATM 7017 O  O    . HOH   F 5 .   ? 16.187 16.622  8.659   1.00 33.83 ?  417 HOH   A O    1 
HETATM 7018 O  O    . HOH   F 5 .   ? 38.148 -1.374  -1.978  1.00 19.69 ?  418 HOH   A O    1 
HETATM 7019 O  O    . HOH   F 5 .   ? 44.904 -0.680  3.019   1.00 40.50 ?  419 HOH   A O    1 
HETATM 7020 O  O    A HOH   F 5 .   ? 20.110 4.557   -7.566  0.70 16.86 ?  420 HOH   A O    1 
HETATM 7021 O  O    . HOH   F 5 .   ? 32.647 -4.268  -9.922  1.00 29.07 ?  421 HOH   A O    1 
HETATM 7022 O  O    . HOH   F 5 .   ? 41.610 1.524   4.974   1.00 36.44 ?  422 HOH   A O    1 
HETATM 7023 O  O    . HOH   F 5 .   ? 32.529 -10.644 3.188   1.00 33.12 ?  423 HOH   A O    1 
HETATM 7024 O  O    . HOH   F 5 .   ? 15.152 -8.088  -9.735  1.00 23.20 ?  424 HOH   A O    1 
HETATM 7025 O  O    . HOH   F 5 .   ? 19.491 -10.972 24.043  1.00 67.55 ?  425 HOH   A O    1 
HETATM 7026 O  O    A HOH   F 5 .   ? 11.042 1.585   12.732  0.70 20.89 ?  426 HOH   A O    1 
HETATM 7027 O  O    . HOH   F 5 .   ? 21.760 -13.777 -8.143  1.00 39.18 ?  427 HOH   A O    1 
HETATM 7028 O  O    . HOH   F 5 .   ? 10.393 -22.216 -1.191  1.00 46.02 ?  428 HOH   A O    1 
HETATM 7029 O  O    . HOH   F 5 .   ? 36.728 -4.948  5.388   1.00 24.60 ?  429 HOH   A O    1 
HETATM 7030 O  O    . HOH   F 5 .   ? 35.096 -5.226  -3.107  1.00 18.70 ?  430 HOH   A O    1 
HETATM 7031 O  O    . HOH   F 5 .   ? 10.355 -13.721 -1.680  1.00 17.56 ?  431 HOH   A O    1 
HETATM 7032 O  O    . HOH   F 5 .   ? 40.937 -8.243  -6.766  1.00 37.67 ?  432 HOH   A O    1 
HETATM 7033 O  O    . HOH   F 5 .   ? 24.019 3.949   -4.839  1.00 24.00 ?  433 HOH   A O    1 
HETATM 7034 O  O    . HOH   F 5 .   ? 15.972 6.853   2.993   1.00 18.66 ?  434 HOH   A O    1 
HETATM 7035 O  O    . HOH   F 5 .   ? 16.193 -14.144 20.177  1.00 46.44 ?  435 HOH   A O    1 
HETATM 7036 O  O    . HOH   F 5 .   ? 22.677 8.172   18.359  1.00 47.30 ?  436 HOH   A O    1 
HETATM 7037 O  O    A HOH   F 5 .   ? 18.580 -2.452  -16.354 0.70 34.32 ?  437 HOH   A O    1 
HETATM 7038 O  O    . HOH   F 5 .   ? 18.514 4.949   -15.119 1.00 46.98 ?  438 HOH   A O    1 
HETATM 7039 O  O    . HOH   F 5 .   ? 23.540 -8.016  17.113  1.00 22.86 ?  439 HOH   A O    1 
HETATM 7040 O  O    . HOH   F 5 .   ? 23.323 -20.905 1.339   1.00 19.40 ?  440 HOH   A O    1 
HETATM 7041 O  O    . HOH   F 5 .   ? 27.134 -3.137  19.310  1.00 36.83 ?  441 HOH   A O    1 
HETATM 7042 O  O    . HOH   F 5 .   ? 23.200 7.586   -3.210  1.00 33.32 ?  442 HOH   A O    1 
HETATM 7043 O  O    . HOH   F 5 .   ? 18.837 1.968   -0.678  1.00 13.95 ?  443 HOH   A O    1 
HETATM 7044 O  O    . HOH   F 5 .   ? 9.436  -16.285 -1.983  1.00 37.97 ?  444 HOH   A O    1 
HETATM 7045 O  O    . HOH   F 5 .   ? 34.413 -8.082  -0.556  1.00 28.22 ?  445 HOH   A O    1 
HETATM 7046 O  O    A HOH   F 5 .   ? 16.267 2.969   -1.461  0.70 19.19 ?  446 HOH   A O    1 
HETATM 7047 O  O    B HOH   F 5 .   ? 19.124 -0.456  -3.919  0.30 30.65 ?  447 HOH   A O    1 
HETATM 7048 O  O    . HOH   F 5 .   ? 21.288 -9.196  21.328  1.00 50.77 ?  448 HOH   A O    1 
HETATM 7049 O  O    . HOH   F 5 .   ? 18.382 -16.020 16.312  1.00 38.51 ?  449 HOH   A O    1 
HETATM 7050 O  O    . HOH   F 5 .   ? 37.715 -8.819  -3.397  1.00 25.37 ?  450 HOH   A O    1 
HETATM 7051 O  O    . HOH   F 5 .   ? 21.500 -14.627 17.946  1.00 55.08 ?  451 HOH   A O    1 
HETATM 7052 O  O    . HOH   F 5 .   ? 30.617 14.779  2.746   1.00 19.35 ?  452 HOH   A O    1 
HETATM 7053 O  O    . HOH   F 5 .   ? 31.324 -12.786 0.013   1.00 19.78 ?  453 HOH   A O    1 
HETATM 7054 O  O    A HOH   F 5 .   ? 14.034 -0.313  3.443   0.40 26.29 ?  454 HOH   A O    1 
HETATM 7055 O  O    . HOH   F 5 .   ? 32.445 -15.893 10.824  1.00 33.62 ?  455 HOH   A O    1 
HETATM 7056 O  O    . HOH   F 5 .   ? 20.592 -17.780 24.816  1.00 51.18 ?  456 HOH   A O    1 
HETATM 7057 O  O    . HOH   F 5 .   ? 29.797 -16.025 10.709  1.00 34.61 ?  457 HOH   A O    1 
HETATM 7058 O  O    . HOH   F 5 .   ? 29.771 -1.942  -12.742 1.00 46.58 ?  458 HOH   A O    1 
HETATM 7059 O  O    B HOH   F 5 .   ? 12.751 -3.252  1.576   0.30 20.44 ?  459 HOH   A O    1 
HETATM 7060 O  O    . HOH   F 5 .   ? 27.804 7.046   -6.510  1.00 37.54 ?  460 HOH   A O    1 
HETATM 7061 O  O    . HOH   F 5 .   ? 25.407 8.230   -4.821  1.00 29.72 ?  461 HOH   A O    1 
HETATM 7062 O  O    . HOH   F 5 .   ? 19.840 -17.327 -5.094  1.00 24.70 ?  462 HOH   A O    1 
HETATM 7063 O  O    . HOH   F 5 .   ? 24.908 5.680   20.753  1.00 51.94 ?  463 HOH   A O    1 
HETATM 7064 O  O    . HOH   F 5 .   ? 23.171 -22.373 -3.335  1.00 35.67 ?  464 HOH   A O    1 
HETATM 7065 O  O    . HOH   F 5 .   ? 24.651 14.654  7.798   1.00 35.36 ?  465 HOH   A O    1 
HETATM 7066 O  O    . HOH   F 5 .   ? 12.033 -13.424 16.372  1.00 53.61 ?  466 HOH   A O    1 
HETATM 7067 O  O    . HOH   F 5 .   ? 15.728 -21.529 3.705   1.00 24.85 ?  467 HOH   A O    1 
HETATM 7068 O  O    . HOH   F 5 .   ? 39.621 -7.063  -3.494  1.00 42.26 ?  468 HOH   A O    1 
HETATM 7069 O  O    . HOH   F 5 .   ? 18.773 10.921  11.289  1.00 33.18 ?  469 HOH   A O    1 
HETATM 7070 O  O    . HOH   F 5 .   ? 26.908 11.672  -1.365  1.00 32.87 ?  470 HOH   A O    1 
HETATM 7071 O  O    . HOH   F 5 .   ? 23.474 13.738  5.504   1.00 18.97 ?  471 HOH   A O    1 
HETATM 7072 O  O    A HOH   F 5 .   ? 21.977 5.281   -5.856  0.70 28.24 ?  472 HOH   A O    1 
HETATM 7073 O  O    . HOH   F 5 .   ? 27.506 -11.399 16.577  1.00 37.04 ?  473 HOH   A O    1 
HETATM 7074 O  O    . HOH   F 5 .   ? 12.325 1.659   17.285  1.00 42.66 ?  474 HOH   A O    1 
HETATM 7075 O  O    . HOH   F 5 .   ? 25.803 10.789  -3.774  1.00 27.52 ?  475 HOH   A O    1 
HETATM 7076 O  O    . HOH   F 5 .   ? 11.031 -15.016 -6.092  1.00 35.08 ?  476 HOH   A O    1 
HETATM 7077 O  O    . HOH   F 5 .   ? 18.063 -16.255 -8.783  1.00 38.57 ?  477 HOH   A O    1 
HETATM 7078 O  O    . HOH   F 5 .   ? 16.813 -20.539 16.154  1.00 29.61 ?  478 HOH   A O    1 
HETATM 7079 O  O    . HOH   F 5 .   ? 28.914 9.018   17.525  1.00 38.32 ?  479 HOH   A O    1 
HETATM 7080 O  O    . HOH   F 5 .   ? 35.228 7.447   12.201  1.00 39.87 ?  480 HOH   A O    1 
HETATM 7081 O  O    . HOH   F 5 .   ? 15.685 -17.144 -7.016  1.00 31.21 ?  481 HOH   A O    1 
HETATM 7082 O  O    . HOH   F 5 .   ? 17.337 -18.637 19.831  1.00 51.60 ?  482 HOH   A O    1 
HETATM 7083 O  O    . HOH   F 5 .   ? 13.932 -10.337 -10.900 1.00 32.78 ?  483 HOH   A O    1 
HETATM 7084 O  O    . HOH   F 5 .   ? 23.121 11.826  -4.073  1.00 19.61 ?  484 HOH   A O    1 
HETATM 7085 O  O    . HOH   F 5 .   ? 30.893 0.736   19.134  1.00 41.07 ?  485 HOH   A O    1 
HETATM 7086 O  O    . HOH   F 5 .   ? 40.954 -3.990  -0.376  1.00 37.82 ?  486 HOH   A O    1 
HETATM 7087 O  O    . HOH   F 5 .   ? 28.589 -4.722  -12.315 1.00 37.15 ?  487 HOH   A O    1 
HETATM 7088 O  O    . HOH   F 5 .   ? 20.503 -16.048 -7.368  1.00 30.08 ?  488 HOH   A O    1 
HETATM 7089 O  O    . HOH   F 5 .   ? 23.242 -12.886 19.330  1.00 45.73 ?  489 HOH   A O    1 
HETATM 7090 O  O    . HOH   F 5 .   ? 28.654 -7.951  -15.288 1.00 48.35 ?  490 HOH   A O    1 
HETATM 7091 O  O    . HOH   F 5 .   ? 39.201 2.434   7.432   1.00 33.59 ?  491 HOH   A O    1 
HETATM 7092 O  O    . HOH   F 5 .   ? 41.753 9.336   -4.044  1.00 31.22 ?  492 HOH   A O    1 
HETATM 7093 O  O    . HOH   F 5 .   ? 44.546 10.454  -1.612  1.00 31.88 ?  493 HOH   A O    1 
HETATM 7094 O  O    . HOH   F 5 .   ? 13.891 -25.217 8.914   1.00 32.48 ?  494 HOH   A O    1 
HETATM 7095 O  O    . HOH   F 5 .   ? 18.408 -23.202 1.891   1.00 42.78 ?  495 HOH   A O    1 
HETATM 7096 O  O    . HOH   F 5 .   ? 15.990 -6.854  -11.885 1.00 44.21 ?  496 HOH   A O    1 
HETATM 7097 O  O    . HOH   F 5 .   ? 40.575 -0.251  -7.854  1.00 34.76 ?  497 HOH   A O    1 
HETATM 7098 O  O    . HOH   F 5 .   ? 31.461 -0.597  -10.595 1.00 29.36 ?  498 HOH   A O    1 
HETATM 7099 O  O    . HOH   F 5 .   ? 20.003 -22.320 4.194   1.00 28.46 ?  499 HOH   A O    1 
HETATM 7100 O  O    . HOH   F 5 .   ? 16.152 -23.357 5.759   1.00 27.53 ?  500 HOH   A O    1 
HETATM 7101 O  O    . HOH   F 5 .   ? 37.389 -6.637  7.559   1.00 25.49 ?  501 HOH   A O    1 
HETATM 7102 O  O    . HOH   F 5 .   ? 30.776 5.807   -14.758 1.00 34.79 ?  502 HOH   A O    1 
HETATM 7103 O  O    B HOH   F 5 .   ? 14.710 8.096   4.870   0.30 23.52 ?  503 HOH   A O    1 
HETATM 7104 O  O    . HOH   F 5 .   ? 23.148 -23.772 1.640   1.00 31.78 ?  504 HOH   A O    1 
HETATM 7105 O  O    . HOH   F 5 .   ? 30.772 -5.870  -11.938 1.00 45.12 ?  505 HOH   A O    1 
HETATM 7106 O  O    . HOH   F 5 .   ? 39.544 0.039   6.567   1.00 30.62 ?  506 HOH   A O    1 
HETATM 7107 O  O    . HOH   F 5 .   ? 29.026 14.432  0.825   1.00 48.44 ?  507 HOH   A O    1 
HETATM 7108 O  O    . HOH   F 5 .   ? 38.045 13.949  6.712   1.00 43.92 ?  508 HOH   A O    1 
HETATM 7109 O  O    . HOH   F 5 .   ? 8.142  -3.136  -5.816  1.00 46.29 ?  509 HOH   A O    1 
HETATM 7110 O  O    . HOH   F 5 .   ? 21.997 -24.028 4.435   1.00 27.61 ?  510 HOH   A O    1 
HETATM 7111 O  O    . HOH   F 5 .   ? 36.456 -6.530  10.163  1.00 43.59 ?  511 HOH   A O    1 
HETATM 7112 O  O    T HOH   F 5 .   ? 11.928 -2.126  -3.672  0.30 12.99 ?  512 HOH   A O    1 
HETATM 7113 O  O    A HOH   F 5 .   ? 14.863 8.676   4.866   0.70 43.82 ?  513 HOH   A O    1 
HETATM 7114 O  O    . HOH   F 5 .   ? 24.087 8.975   -7.229  1.00 37.65 ?  514 HOH   A O    1 
HETATM 7115 O  O    . HOH   F 5 .   ? 16.931 -7.069  -14.436 1.00 50.34 ?  515 HOH   A O    1 
HETATM 7116 O  O    . HOH   F 5 .   ? 16.374 -21.100 18.766  1.00 36.25 ?  516 HOH   A O    1 
HETATM 7117 O  O    . HOH   F 5 .   ? 15.824 -12.276 27.438  1.00 47.04 ?  517 HOH   A O    1 
HETATM 7118 O  O    . HOH   F 5 .   ? 14.728 -22.773 19.838  1.00 36.04 ?  518 HOH   A O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 29.830 -22.430 5.499   1.00 21.56 ?  201 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 52.900 -13.457 -20.300 1.00 33.81 ?  202 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 41.771 -36.019 -17.205 1.00 32.29 ?  203 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 59.178 -18.726 6.827   1.00 35.83 ?  204 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 48.076 -6.894  15.557  1.00 34.03 ?  205 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 38.018 -39.452 -0.134  1.00 39.27 ?  206 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 41.383 -7.756  5.458   1.00 38.69 ?  207 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 27.693 -29.181 -1.814  1.00 36.55 ?  208 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 27.859 -41.843 -15.170 1.00 34.74 ?  209 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 57.749 -24.485 5.079   1.00 36.35 ?  210 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 54.506 -9.389  -8.776  1.00 19.76 ?  211 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 49.442 -22.692 -19.763 1.00 46.90 ?  212 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 56.386 -19.696 7.307   1.00 33.13 ?  213 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 50.251 -3.367  7.182   1.00 37.85 ?  214 HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 30.227 -41.037 -8.085  1.00 17.74 ?  215 HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 29.896 -26.305 4.031   1.00 27.90 ?  216 HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 47.402 -7.384  -3.919  1.00 39.99 ?  217 HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 58.243 -12.875 8.429   1.00 32.32 ?  218 HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 44.465 -7.287  2.081   1.00 35.48 ?  219 HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 55.378 -16.538 -14.348 1.00 34.69 ?  220 HOH   B O    1 
HETATM 7139 O  O    . HOH   G 5 .   ? 37.100 -19.852 -18.093 1.00 37.92 ?  221 HOH   B O    1 
HETATM 7140 O  O    . HOH   G 5 .   ? 50.761 -6.111  0.163   1.00 27.80 ?  222 HOH   B O    1 
HETATM 7141 O  O    . HOH   G 5 .   ? 30.896 -28.779 4.310   1.00 26.87 ?  223 HOH   B O    1 
HETATM 7142 O  O    . HOH   G 5 .   ? 56.713 -30.772 -7.752  1.00 29.41 ?  224 HOH   B O    1 
HETATM 7143 O  O    . HOH   G 5 .   ? 57.187 -26.845 -7.683  1.00 41.49 ?  225 HOH   B O    1 
HETATM 7144 O  O    . HOH   G 5 .   ? 34.544 -36.406 -7.177  1.00 19.15 ?  226 HOH   B O    1 
HETATM 7145 O  O    . HOH   G 5 .   ? 41.527 -39.194 -14.890 1.00 24.04 ?  227 HOH   B O    1 
HETATM 7146 O  O    . HOH   G 5 .   ? 57.426 -16.270 -12.212 1.00 19.32 ?  228 HOH   B O    1 
HETATM 7147 O  O    . HOH   G 5 .   ? 36.000 -43.308 -8.466  1.00 30.60 ?  229 HOH   B O    1 
HETATM 7148 O  O    . HOH   G 5 .   ? 44.986 -43.562 -10.526 1.00 28.88 ?  230 HOH   B O    1 
HETATM 7149 O  O    . HOH   G 5 .   ? 48.594 -36.510 -15.490 1.00 45.60 ?  231 HOH   B O    1 
HETATM 7150 O  O    . HOH   G 5 .   ? 29.838 -34.212 -0.452  1.00 34.92 ?  232 HOH   B O    1 
HETATM 7151 O  O    . HOH   G 5 .   ? 51.704 -6.490  4.387   1.00 20.37 ?  233 HOH   B O    1 
HETATM 7152 O  O    . HOH   G 5 .   ? 32.834 -43.847 -11.334 1.00 20.97 ?  234 HOH   B O    1 
HETATM 7153 O  O    . HOH   G 5 .   ? 39.312 -10.900 6.135   1.00 27.41 ?  235 HOH   B O    1 
HETATM 7154 O  O    . HOH   G 5 .   ? 35.097 -8.000  -2.989  1.00 18.92 ?  236 HOH   B O    1 
HETATM 7155 O  O    . HOH   G 5 .   ? 34.891 -24.663 13.874  1.00 30.66 ?  237 HOH   B O    1 
HETATM 7156 O  O    . HOH   G 5 .   ? 40.659 -16.052 14.130  1.00 24.99 ?  238 HOH   B O    1 
HETATM 7157 O  O    . HOH   G 5 .   ? 44.511 -27.760 -0.704  1.00 23.65 ?  239 HOH   B O    1 
HETATM 7158 O  O    . HOH   G 5 .   ? 45.145 -35.022 6.834   1.00 41.02 ?  240 HOH   B O    1 
HETATM 7159 O  O    . HOH   G 5 .   ? 25.432 -25.965 -1.274  1.00 33.61 ?  241 HOH   B O    1 
HETATM 7160 O  O    . HOH   G 5 .   ? 41.367 -9.623  13.073  1.00 23.53 ?  242 HOH   B O    1 
HETATM 7161 O  O    . HOH   G 5 .   ? 48.089 -24.510 -17.764 1.00 31.80 ?  243 HOH   B O    1 
HETATM 7162 O  O    . HOH   G 5 .   ? 50.741 -12.983 -0.470  1.00 12.60 ?  244 HOH   B O    1 
HETATM 7163 O  O    . HOH   G 5 .   ? 28.384 -19.690 -13.123 1.00 25.34 ?  245 HOH   B O    1 
HETATM 7164 O  O    . HOH   G 5 .   ? 42.576 -25.383 2.645   1.00 16.04 ?  246 HOH   B O    1 
HETATM 7165 O  O    . HOH   G 5 .   ? 39.504 -11.111 0.345   1.00 17.78 ?  247 HOH   B O    1 
HETATM 7166 O  O    . HOH   G 5 .   ? 43.210 -32.435 -17.050 1.00 23.96 ?  248 HOH   B O    1 
HETATM 7167 O  O    . HOH   G 5 .   ? 34.222 -18.465 11.405  1.00 24.55 ?  249 HOH   B O    1 
HETATM 7168 O  O    . HOH   G 5 .   ? 42.642 -22.885 3.851   1.00 12.51 ?  250 HOH   B O    1 
HETATM 7169 O  O    . HOH   G 5 .   ? 46.430 -1.529  13.219  1.00 28.98 ?  251 HOH   B O    1 
HETATM 7170 O  O    . HOH   G 5 .   ? 40.324 -12.771 -11.520 1.00 15.61 ?  252 HOH   B O    1 
HETATM 7171 O  O    . HOH   G 5 .   ? 57.630 -24.396 -3.819  1.00 21.71 ?  253 HOH   B O    1 
HETATM 7172 O  O    . HOH   G 5 .   ? 38.485 -11.066 -2.266  1.00 19.60 ?  254 HOH   B O    1 
HETATM 7173 O  O    . HOH   G 5 .   ? 43.082 -43.281 -8.223  1.00 30.16 ?  255 HOH   B O    1 
HETATM 7174 O  O    . HOH   G 5 .   ? 51.581 -13.860 11.067  1.00 27.77 ?  256 HOH   B O    1 
HETATM 7175 O  O    . HOH   G 5 .   ? 50.978 -39.950 -8.230  1.00 33.53 ?  257 HOH   B O    1 
HETATM 7176 O  O    . HOH   G 5 .   ? 41.885 -23.528 9.303   1.00 18.33 ?  258 HOH   B O    1 
HETATM 7177 O  O    . HOH   G 5 .   ? 34.953 -33.348 -19.187 1.00 32.43 ?  259 HOH   B O    1 
HETATM 7178 O  O    . HOH   G 5 .   ? 29.730 -25.244 -10.803 1.00 17.38 ?  260 HOH   B O    1 
HETATM 7179 O  O    . HOH   G 5 .   ? 30.856 -15.735 2.678   1.00 14.66 ?  261 HOH   B O    1 
HETATM 7180 O  O    . HOH   G 5 .   ? 31.787 -17.892 -14.500 1.00 30.32 ?  262 HOH   B O    1 
HETATM 7181 O  O    . HOH   G 5 .   ? 48.017 -22.792 5.838   1.00 18.13 ?  263 HOH   B O    1 
HETATM 7182 O  O    . HOH   G 5 .   ? 38.915 -11.964 12.365  1.00 33.21 ?  264 HOH   B O    1 
HETATM 7183 O  O    . HOH   G 5 .   ? 28.506 -30.924 -14.715 1.00 30.85 ?  265 HOH   B O    1 
HETATM 7184 O  O    . HOH   G 5 .   ? 58.216 -10.647 -4.078  1.00 20.70 ?  266 HOH   B O    1 
HETATM 7185 O  O    . HOH   G 5 .   ? 57.535 -9.249  1.446   1.00 20.62 ?  267 HOH   B O    1 
HETATM 7186 O  O    . HOH   G 5 .   ? 27.141 -31.857 -9.962  1.00 21.25 ?  268 HOH   B O    1 
HETATM 7187 O  O    . HOH   G 5 .   ? 34.491 -12.786 2.607   1.00 25.24 ?  269 HOH   B O    1 
HETATM 7188 O  O    . HOH   G 5 .   ? 42.319 -9.897  9.397   1.00 21.61 ?  270 HOH   B O    1 
HETATM 7189 O  O    . HOH   G 5 .   ? 43.371 -15.803 -12.176 1.00 14.31 ?  271 HOH   B O    1 
HETATM 7190 O  O    . HOH   G 5 .   ? 56.166 -23.568 -14.736 1.00 27.44 ?  272 HOH   B O    1 
HETATM 7191 O  O    . HOH   G 5 .   ? 49.327 -28.719 -6.884  1.00 16.15 ?  273 HOH   B O    1 
HETATM 7192 O  O    . HOH   G 5 .   ? 42.372 -34.718 3.776   1.00 26.76 ?  274 HOH   B O    1 
HETATM 7193 O  O    . HOH   G 5 .   ? 28.281 -34.394 -9.416  1.00 18.00 ?  275 HOH   B O    1 
HETATM 7194 O  O    . HOH   G 5 .   ? 56.966 -8.637  8.426   1.00 20.17 ?  276 HOH   B O    1 
HETATM 7195 O  O    . HOH   G 5 .   ? 49.729 -0.474  10.230  1.00 31.06 ?  277 HOH   B O    1 
HETATM 7196 O  O    . HOH   G 5 .   ? 27.946 -22.908 -8.015  1.00 18.35 ?  278 HOH   B O    1 
HETATM 7197 O  O    . HOH   G 5 .   ? 46.617 -31.265 -4.777  1.00 23.67 ?  279 HOH   B O    1 
HETATM 7198 O  O    . HOH   G 5 .   ? 57.148 -12.096 12.329  1.00 39.99 ?  280 HOH   B O    1 
HETATM 7199 O  O    . HOH   G 5 .   ? 41.175 -5.491  11.548  1.00 45.62 ?  281 HOH   B O    1 
HETATM 7200 O  O    . HOH   G 5 .   ? 48.426 -25.056 3.119   1.00 13.79 ?  282 HOH   B O    1 
HETATM 7201 O  O    . HOH   G 5 .   ? 46.861 -29.606 9.892   1.00 32.04 ?  283 HOH   B O    1 
HETATM 7202 O  O    . HOH   G 5 .   ? 59.803 -15.314 8.150   1.00 32.75 ?  284 HOH   B O    1 
HETATM 7203 O  O    . HOH   G 5 .   ? 27.568 -26.691 -15.629 1.00 34.52 ?  285 HOH   B O    1 
HETATM 7204 O  O    . HOH   G 5 .   ? 42.882 -20.336 -20.799 1.00 35.15 ?  286 HOH   B O    1 
HETATM 7205 O  O    . HOH   G 5 .   ? 42.344 -9.941  -14.918 1.00 35.69 ?  287 HOH   B O    1 
HETATM 7206 O  O    . HOH   G 5 .   ? 45.341 -33.417 -15.911 1.00 24.54 ?  288 HOH   B O    1 
HETATM 7207 O  O    . HOH   G 5 .   ? 52.541 -10.395 13.001  1.00 23.29 ?  289 HOH   B O    1 
HETATM 7208 O  O    . HOH   G 5 .   ? 50.020 -24.626 5.824   1.00 33.75 ?  290 HOH   B O    1 
HETATM 7209 O  O    . HOH   G 5 .   ? 36.818 -12.772 -1.493  1.00 27.76 ?  291 HOH   B O    1 
HETATM 7210 O  O    . HOH   G 5 .   ? 33.507 -15.317 -13.963 1.00 22.50 ?  292 HOH   B O    1 
HETATM 7211 O  O    . HOH   G 5 .   ? 30.535 -42.301 -10.556 1.00 30.31 ?  293 HOH   B O    1 
HETATM 7212 O  O    . HOH   G 5 .   ? 48.714 -20.048 5.955   1.00 14.31 ?  294 HOH   B O    1 
HETATM 7213 O  O    . HOH   G 5 .   ? 57.692 -22.110 3.066   1.00 29.11 ?  295 HOH   B O    1 
HETATM 7214 O  O    . HOH   G 5 .   ? 47.088 -33.986 -4.596  1.00 18.38 ?  296 HOH   B O    1 
HETATM 7215 O  O    . HOH   G 5 .   ? 51.246 -37.619 -9.580  1.00 26.99 ?  297 HOH   B O    1 
HETATM 7216 O  O    . HOH   G 5 .   ? 42.746 -12.297 -18.513 1.00 29.61 ?  298 HOH   B O    1 
HETATM 7217 O  O    . HOH   G 5 .   ? 44.048 -29.372 -4.690  1.00 23.86 ?  299 HOH   B O    1 
HETATM 7218 O  O    . HOH   G 5 .   ? 45.933 -40.427 -3.569  1.00 30.10 ?  300 HOH   B O    1 
HETATM 7219 O  O    . HOH   G 5 .   ? 44.638 -27.469 2.023   1.00 15.74 ?  301 HOH   B O    1 
HETATM 7220 O  O    . HOH   G 5 .   ? 37.333 -35.671 7.211   1.00 34.63 ?  302 HOH   B O    1 
HETATM 7221 O  O    . HOH   G 5 .   ? 40.256 -10.834 -9.547  1.00 17.44 ?  303 HOH   B O    1 
HETATM 7222 O  O    . HOH   G 5 .   ? 37.518 -18.160 13.126  1.00 30.23 ?  304 HOH   B O    1 
HETATM 7223 O  O    . HOH   G 5 .   ? 62.696 -13.576 4.764   1.00 27.29 ?  305 HOH   B O    1 
HETATM 7224 O  O    . HOH   G 5 .   ? 52.628 -35.664 -8.628  1.00 29.98 ?  306 HOH   B O    1 
HETATM 7225 O  O    . HOH   G 5 .   ? 51.351 -32.999 -10.734 1.00 40.54 ?  307 HOH   B O    1 
HETATM 7226 O  O    . HOH   G 5 .   ? 53.496 -30.202 4.505   1.00 19.60 ?  308 HOH   B O    1 
HETATM 7227 O  O    . HOH   G 5 .   ? 35.034 -33.568 4.502   1.00 28.27 ?  309 HOH   B O    1 
HETATM 7228 O  O    . HOH   G 5 .   ? 53.108 -16.057 -12.726 1.00 28.29 ?  310 HOH   B O    1 
HETATM 7229 O  O    . HOH   G 5 .   ? 52.536 -29.282 -13.027 1.00 25.26 ?  311 HOH   B O    1 
HETATM 7230 O  O    . HOH   G 5 .   ? 25.939 -21.490 -3.532  1.00 17.06 ?  312 HOH   B O    1 
HETATM 7231 O  O    . HOH   G 5 .   ? 32.819 -34.618 -5.887  1.00 18.17 ?  313 HOH   B O    1 
HETATM 7232 O  O    . HOH   G 5 .   ? 60.003 -17.149 -10.438 1.00 33.15 ?  314 HOH   B O    1 
HETATM 7233 O  O    . HOH   G 5 .   ? 37.856 -10.251 -10.765 1.00 17.28 ?  315 HOH   B O    1 
HETATM 7234 O  O    . HOH   G 5 .   ? 51.752 -5.988  -7.903  1.00 47.40 ?  316 HOH   B O    1 
HETATM 7235 O  O    . HOH   G 5 .   ? 48.086 -32.660 -16.609 1.00 42.31 ?  317 HOH   B O    1 
HETATM 7236 O  O    . HOH   G 5 .   ? 43.516 -15.418 18.212  1.00 31.18 ?  318 HOH   B O    1 
HETATM 7237 O  O    . HOH   G 5 .   ? 38.337 -12.755 7.929   1.00 18.93 ?  319 HOH   B O    1 
HETATM 7238 O  O    . HOH   G 5 .   ? 37.148 -30.601 -21.023 1.00 32.16 ?  320 HOH   B O    1 
HETATM 7239 O  O    . HOH   G 5 .   ? 62.869 -20.167 -0.780  1.00 38.49 ?  321 HOH   B O    1 
HETATM 7240 O  O    . HOH   G 5 .   ? 43.216 -21.451 10.683  1.00 16.66 ?  322 HOH   B O    1 
HETATM 7241 O  O    . HOH   G 5 .   ? 26.337 -21.044 -6.248  1.00 17.08 ?  323 HOH   B O    1 
HETATM 7242 O  O    . HOH   G 5 .   ? 41.726 -8.058  1.371   1.00 25.22 ?  324 HOH   B O    1 
HETATM 7243 O  O    . HOH   G 5 .   ? 53.669 -12.600 -22.217 1.00 33.60 ?  325 HOH   B O    1 
HETATM 7244 O  O    . HOH   G 5 .   ? 41.216 -24.450 15.860  1.00 45.50 ?  326 HOH   B O    1 
HETATM 7245 O  O    . HOH   G 5 .   ? 27.885 -14.813 -9.432  1.00 35.48 ?  327 HOH   B O    1 
HETATM 7246 O  O    . HOH   G 5 .   ? 44.595 -24.627 9.580   1.00 21.06 ?  328 HOH   B O    1 
HETATM 7247 O  O    . HOH   G 5 .   ? 44.190 -1.757  7.566   1.00 46.20 ?  329 HOH   B O    1 
HETATM 7248 O  O    . HOH   G 5 .   ? 38.397 -9.366  -13.274 1.00 27.10 ?  330 HOH   B O    1 
HETATM 7249 O  O    . HOH   G 5 .   ? 36.728 -12.414 4.301   1.00 18.97 ?  331 HOH   B O    1 
HETATM 7250 O  O    . HOH   G 5 .   ? 43.133 -34.640 0.098   1.00 21.81 ?  332 HOH   B O    1 
HETATM 7251 O  O    . HOH   G 5 .   ? 33.614 -31.167 11.087  1.00 36.22 ?  333 HOH   B O    1 
HETATM 7252 O  O    . HOH   G 5 .   ? 47.201 -24.504 8.198   1.00 26.22 ?  334 HOH   B O    1 
HETATM 7253 O  O    . HOH   G 5 .   ? 42.911 -43.515 -14.355 1.00 42.17 ?  335 HOH   B O    1 
HETATM 7254 O  O    . HOH   G 5 .   ? 47.490 -27.451 2.023   1.00 15.46 ?  336 HOH   B O    1 
HETATM 7255 O  O    . HOH   G 5 .   ? 48.624 -11.967 -13.977 1.00 27.86 ?  337 HOH   B O    1 
HETATM 7256 O  O    . HOH   G 5 .   ? 45.708 -36.280 -16.116 1.00 35.84 ?  338 HOH   B O    1 
HETATM 7257 O  O    . HOH   G 5 .   ? 37.026 -15.128 -16.527 1.00 41.93 ?  339 HOH   B O    1 
HETATM 7258 O  O    . HOH   G 5 .   ? 46.840 -19.890 12.288  1.00 30.05 ?  340 HOH   B O    1 
HETATM 7259 O  O    . HOH   G 5 .   ? 39.511 -23.621 -20.334 1.00 37.66 ?  341 HOH   B O    1 
HETATM 7260 O  O    . HOH   G 5 .   ? 37.063 -45.221 -9.758  1.00 37.96 ?  342 HOH   B O    1 
HETATM 7261 O  O    . HOH   G 5 .   ? 28.888 -42.980 -12.358 1.00 37.50 ?  343 HOH   B O    1 
HETATM 7262 O  O    . HOH   G 5 .   ? 32.995 -14.694 1.041   1.00 18.97 ?  344 HOH   B O    1 
HETATM 7263 O  O    . HOH   G 5 .   ? 38.479 -12.264 -16.284 1.00 40.81 ?  345 HOH   B O    1 
HETATM 7264 O  O    . HOH   G 5 .   ? 38.618 -22.332 15.037  1.00 39.64 ?  346 HOH   B O    1 
HETATM 7265 O  O    . HOH   G 5 .   ? 39.805 -44.350 -11.170 1.00 40.47 ?  347 HOH   B O    1 
HETATM 7266 O  O    . HOH   G 5 .   ? 33.737 -9.415  -8.834  1.00 33.27 ?  348 HOH   B O    1 
HETATM 7267 O  O    . HOH   G 5 .   ? 40.419 -43.521 -9.052  1.00 27.98 ?  349 HOH   B O    1 
HETATM 7268 O  O    . HOH   G 5 .   ? 62.557 -20.097 -4.804  1.00 45.28 ?  350 HOH   B O    1 
HETATM 7269 O  O    . HOH   G 5 .   ? 27.745 -26.655 -0.571  1.00 31.78 ?  351 HOH   B O    1 
HETATM 7270 O  O    . HOH   G 5 .   ? 55.661 -8.250  10.825  1.00 25.13 ?  352 HOH   B O    1 
HETATM 7271 O  O    . HOH   G 5 .   ? 34.620 -10.302 7.581   1.00 25.19 ?  353 HOH   B O    1 
HETATM 7272 O  O    . HOH   G 5 .   ? 44.179 -37.359 -17.766 1.00 34.45 ?  354 HOH   B O    1 
HETATM 7273 O  O    . HOH   G 5 .   ? 23.184 -23.661 6.828   1.00 33.71 ?  355 HOH   B O    1 
HETATM 7274 O  O    . HOH   G 5 .   ? 56.605 -7.274  3.083   1.00 26.92 ?  356 HOH   B O    1 
HETATM 7275 O  O    . HOH   G 5 .   ? 36.047 -8.556  -9.771  1.00 36.46 ?  357 HOH   B O    1 
HETATM 7276 O  O    . HOH   G 5 .   ? 43.175 -12.730 -21.232 1.00 41.25 ?  358 HOH   B O    1 
HETATM 7277 O  O    . HOH   G 5 .   ? 61.512 -19.913 1.638   1.00 35.69 ?  359 HOH   B O    1 
HETATM 7278 O  O    . HOH   G 5 .   ? 34.133 -7.724  11.468  1.00 40.86 ?  360 HOH   B O    1 
HETATM 7279 O  O    . HOH   G 5 .   ? 40.273 -8.814  9.875   1.00 37.09 ?  361 HOH   B O    1 
HETATM 7280 O  O    . HOH   G 5 .   ? 27.177 -25.975 -11.388 1.00 35.10 ?  362 HOH   B O    1 
HETATM 7281 O  O    . HOH   G 5 .   ? 56.972 -21.582 -16.395 1.00 41.00 ?  363 HOH   B O    1 
HETATM 7282 O  O    . HOH   G 5 .   ? 54.195 -5.719  3.001   1.00 37.11 ?  364 HOH   B O    1 
HETATM 7283 O  O    . HOH   G 5 .   ? 48.338 -26.559 8.857   1.00 41.71 ?  365 HOH   B O    1 
HETATM 7284 O  O    . HOH   G 5 .   ? 32.567 -23.628 14.128  1.00 39.54 ?  366 HOH   B O    1 
HETATM 7285 O  O    . HOH   G 5 .   ? 36.153 -8.718  8.981   1.00 36.63 ?  367 HOH   B O    1 
HETATM 7286 O  O    . HOH   G 5 .   ? 40.140 -11.364 -13.994 1.00 32.42 ?  368 HOH   B O    1 
HETATM 7287 O  O    . HOH   G 5 .   ? 58.969 -10.408 9.211   1.00 38.62 ?  369 HOH   B O    1 
HETATM 7288 O  O    . HOH   G 5 .   ? 39.859 -7.041  7.816   1.00 42.16 ?  370 HOH   B O    1 
HETATM 7289 O  O    . HOH   G 5 .   ? 56.099 -7.828  -0.595  1.00 34.22 ?  371 HOH   B O    1 
HETATM 7290 O  O    . HOH   G 5 .   ? 41.855 -9.999  -17.461 1.00 52.84 ?  372 HOH   B O    1 
HETATM 7291 O  O    . HOH   G 5 .   ? 63.070 -12.421 6.930   1.00 39.09 ?  373 HOH   B O    1 
HETATM 7292 O  O    . HOH   G 5 .   ? 52.046 -12.915 13.389  1.00 31.43 ?  374 HOH   B O    1 
HETATM 7293 O  O    . HOH   G 5 .   ? 38.062 -10.593 10.064  1.00 30.06 ?  375 HOH   B O    1 
HETATM 7294 O  O    . HOH   G 5 .   ? 44.154 -5.588  -3.569  1.00 45.04 ?  376 HOH   B O    1 
HETATM 7295 O  O    . HOH   G 5 .   ? 36.544 -22.839 13.284  1.00 27.03 ?  377 HOH   B O    1 
HETATM 7296 O  O    . HOH   G 5 .   ? 40.151 -7.676  3.207   1.00 37.54 ?  378 HOH   B O    1 
HETATM 7297 O  O    . HOH   G 5 .   ? 42.634 -17.093 -23.183 1.00 44.39 ?  379 HOH   B O    1 
HETATM 7298 O  O    . HOH   G 5 .   ? 41.798 -6.677  -4.827  1.00 46.90 ?  380 HOH   B O    1 
HETATM 7299 O  O    . HOH   G 5 .   ? 52.858 -29.905 7.199   1.00 24.82 ?  381 HOH   B O    1 
HETATM 7300 O  O    . HOH   G 5 .   ? 39.671 -14.022 15.708  1.00 48.29 ?  382 HOH   B O    1 
HETATM 7301 O  O    . HOH   G 5 .   ? 60.498 -22.226 2.864   1.00 46.43 ?  383 HOH   B O    1 
HETATM 7302 O  O    . HOH   G 5 .   ? 46.834 -5.380  2.912   1.00 41.57 ?  384 HOH   B O    1 
HETATM 7303 O  O    . HOH   G 5 .   ? 25.795 -18.850 -11.934 1.00 40.47 ?  385 HOH   B O    1 
HETATM 7304 O  O    . HOH   G 5 .   ? 40.996 -9.787  15.826  1.00 43.48 ?  386 HOH   B O    1 
HETATM 7305 O  O    . HOH   G 5 .   ? 23.932 -20.889 -7.664  1.00 29.02 ?  387 HOH   B O    1 
HETATM 7306 O  O    . HOH   G 5 .   ? 35.424 -33.750 7.360   1.00 41.07 ?  388 HOH   B O    1 
HETATM 7307 O  O    . HOH   G 5 .   ? 35.337 -20.330 13.331  1.00 30.42 ?  389 HOH   B O    1 
HETATM 7308 O  O    . HOH   G 5 .   ? 40.679 -6.640  -0.853  1.00 25.45 ?  390 HOH   B O    1 
HETATM 7309 O  O    . HOH   G 5 .   ? 44.118 -31.807 -3.844  1.00 34.27 ?  391 HOH   B O    1 
HETATM 7310 O  O    . HOH   G 5 .   ? 26.611 -28.012 -13.495 1.00 35.13 ?  392 HOH   B O    1 
HETATM 7311 O  O    . HOH   G 5 .   ? 27.871 -27.100 2.216   1.00 31.00 ?  393 HOH   B O    1 
HETATM 7312 O  O    . HOH   G 5 .   ? 24.622 -20.666 -10.505 1.00 36.40 ?  394 HOH   B O    1 
HETATM 7313 O  O    . HOH   G 5 .   ? 34.358 -33.487 9.615   1.00 36.31 ?  395 HOH   B O    1 
HETATM 7314 O  O    . HOH   G 5 .   ? 50.685 -30.797 8.699   1.00 28.68 ?  396 HOH   B O    1 
HETATM 7315 O  O    . HOH   G 5 .   ? 26.851 -30.685 -12.618 1.00 27.92 ?  397 HOH   B O    1 
HETATM 7316 O  O    . HOH   G 5 .   ? 45.743 -20.230 15.201  1.00 52.59 ?  398 HOH   B O    1 
HETATM 7317 O  O    . HOH   G 5 .   ? 57.621 -6.497  -2.347  1.00 34.79 ?  399 HOH   B O    1 
HETATM 7318 O  O    . HOH   G 5 .   ? 40.959 -11.796 -22.303 1.00 41.14 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.6723 0.6785 0.7399 -0.0160 -0.0132 0.0735  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6699 0.6763 0.7167 -0.0175 -0.0115 0.0538  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6691 0.6753 0.7324 -0.0161 -0.0137 0.0722  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6667 0.6737 0.7119 -0.0176 -0.0122 0.0549  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6507 0.6600 0.7041 -0.0217 -0.0158 0.0730  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6492 0.6594 0.6927 -0.0222 -0.0146 0.0633  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6553 0.6629 0.7125 -0.0207 -0.0162 0.0760  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6537 0.6629 0.6995 -0.0213 -0.0144 0.0637  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6807 0.6847 0.7405 -0.0119 -0.0111 0.0720  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6775 0.6826 0.7157 -0.0142 -0.0099 0.0492  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6864 0.6906 0.7483 -0.0116 -0.0100 0.0724  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6832 0.6880 0.7224 -0.0135 -0.0089 0.0473  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6827 0.6850 0.7492 -0.0095 -0.0100 0.0723  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6791 0.6832 0.7227 -0.0124 -0.0090 0.0473  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6246 0.6393 0.6527 -0.0289 -0.0161 0.0723  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5718 0.5953 0.5575 -0.0446 -0.0168 0.0775  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5104 0.5454 0.4942 -0.0598 -0.0032 0.0505  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5136 0.5479 0.4930 -0.0604 -0.0068 0.0558  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5797 0.5996 0.5219 -0.0468 -0.0303 0.1075  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.5869 0.6009 0.4889 -0.0518 -0.0397 0.1360  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.5916 0.5991 0.4641 -0.0547 -0.0426 0.1491  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.5883 0.6026 0.4735 -0.0521 -0.0439 0.1478  4   ASN   A ND2 
46   N  N   A SER   A 5   ? 0.4724 0.5201 0.4552 -0.0754 0.0061  0.0326  5   SER   A N   
47   N  N   B SER   A 5   ? 0.4808 0.5137 0.4702 -0.0618 0.0025  0.0365  5   SER   A N   
48   C  CA  A SER   A 5   ? 0.4328 0.4942 0.4211 -0.0874 0.0145  0.0172  5   SER   A CA  
49   C  CA  B SER   A 5   ? 0.4508 0.4818 0.4452 -0.0612 0.0078  0.0232  5   SER   A CA  
50   C  C   A SER   A 5   ? 0.3867 0.4582 0.3611 -0.0981 0.0241  0.0056  5   SER   A C   
51   C  C   B SER   A 5   ? 0.4157 0.4446 0.3962 -0.0609 0.0131  0.0131  5   SER   A C   
52   O  O   A SER   A 5   ? 0.3926 0.4685 0.3637 -0.0908 0.0246  -0.0076 5   SER   A O   
53   O  O   B SER   A 5   ? 0.4188 0.4485 0.4007 -0.0569 0.0153  0.0084  5   SER   A O   
54   C  CB  A SER   A 5   ? 0.4397 0.5020 0.4335 -0.0877 0.0156  0.0133  5   SER   A CB  
55   C  CB  B SER   A 5   ? 0.4555 0.4862 0.4579 -0.0608 0.0087  0.0202  5   SER   A CB  
56   O  OG  A SER   A 5   ? 0.4436 0.5059 0.4445 -0.0879 0.0179  0.0111  5   SER   A OG  
57   O  OG  B SER   A 5   ? 0.4584 0.4889 0.4678 -0.0603 0.0095  0.0186  5   SER   A OG  
68   N  N   A PHE   A 6   ? 0.3323 0.4098 0.3009 -0.1150 0.0364  0.0118  6   PHE   A N   
69   N  N   B PHE   A 6   ? 0.3762 0.4028 0.3463 -0.0645 0.0177  0.0096  6   PHE   A N   
70   C  CA  A PHE   A 6   ? 0.2844 0.3644 0.2477 -0.1232 0.0420  0.0281  6   PHE   A CA  
71   C  CA  B PHE   A 6   ? 0.3374 0.3612 0.2997 -0.0660 0.0218  0.0092  6   PHE   A CA  
72   C  C   A PHE   A 6   ? 0.2759 0.3586 0.2381 -0.1303 0.0472  0.0218  6   PHE   A C   
73   C  C   B PHE   A 6   ? 0.3234 0.3456 0.2895 -0.0669 0.0322  0.0100  6   PHE   A C   
74   O  O   A PHE   A 6   ? 0.2818 0.3695 0.2709 -0.1357 0.0538  0.0322  6   PHE   A O   
75   O  O   B PHE   A 6   ? 0.3239 0.3469 0.2914 -0.0648 0.0311  0.0150  6   PHE   A O   
76   C  CB  A PHE   A 6   ? 0.2640 0.3343 0.2080 -0.1116 0.0289  0.0417  6   PHE   A CB  
77   C  CB  B PHE   A 6   ? 0.3177 0.3383 0.2655 -0.0630 0.0124  0.0049  6   PHE   A CB  
78   C  CG  A PHE   A 6   ? 0.2473 0.3158 0.1835 -0.1007 0.0208  0.0472  6   PHE   A CG  
79   C  CG  B PHE   A 6   ? 0.2991 0.3189 0.2423 -0.0603 0.0037  0.0021  6   PHE   A CG  
80   C  CD1 A PHE   A 6   ? 0.2396 0.3079 0.1804 -0.0912 0.0169  0.0500  6   PHE   A CD1 
81   C  CD1 B PHE   A 6   ? 0.2922 0.3109 0.2330 -0.0570 0.0022  0.0025  6   PHE   A CD1 
82   C  CD2 A PHE   A 6   ? 0.2532 0.3145 0.2048 -0.0867 0.0117  0.0481  6   PHE   A CD2 
83   C  CD2 B PHE   A 6   ? 0.2919 0.3105 0.2425 -0.0580 -0.0013 0.0014  6   PHE   A CD2 
84   C  CE1 A PHE   A 6   ? 0.2348 0.3062 0.1909 -0.0887 0.0183  0.0504  6   PHE   A CE1 
85   C  CE1 B PHE   A 6   ? 0.2872 0.3059 0.2325 -0.0559 0.0006  0.0018  6   PHE   A CE1 
86   C  CE2 A PHE   A 6   ? 0.2512 0.3144 0.2196 -0.0832 0.0109  0.0436  6   PHE   A CE2 
87   C  CE2 B PHE   A 6   ? 0.2868 0.3049 0.2416 -0.0578 -0.0021 -0.0018 6   PHE   A CE2 
88   C  CZ  A PHE   A 6   ? 0.2408 0.3084 0.1979 -0.0887 0.0107  0.0385  6   PHE   A CZ  
89   C  CZ  B PHE   A 6   ? 0.2852 0.3037 0.2319 -0.0570 -0.0022 -0.0036 6   PHE   A CZ  
108  N  N   A SER   A 7   ? 0.2598 0.3422 0.1988 -0.1281 0.0508  0.0097  7   SER   A N   
109  N  N   B SER   A 7   ? 0.3108 0.3291 0.2843 -0.0677 0.0396  0.0038  7   SER   A N   
110  C  CA  A SER   A 7   ? 0.2567 0.3307 0.1983 -0.1122 0.0514  -0.0147 7   SER   A CA  
111  C  CA  B SER   A 7   ? 0.3036 0.3181 0.2870 -0.0605 0.0383  -0.0063 7   SER   A CA  
112  C  C   A SER   A 7   ? 0.2418 0.2930 0.1642 -0.1000 0.0565  -0.0134 7   SER   A C   
113  C  C   B SER   A 7   ? 0.2888 0.3012 0.2725 -0.0590 0.0450  -0.0081 7   SER   A C   
114  O  O   A SER   A 7   ? 0.2603 0.2802 0.1743 -0.0976 0.0689  -0.0104 7   SER   A O   
115  O  O   B SER   A 7   ? 0.2940 0.3056 0.2680 -0.0581 0.0476  -0.0101 7   SER   A O   
116  C  CB  A SER   A 7   ? 0.2752 0.3577 0.2376 -0.0992 0.0560  -0.0173 7   SER   A CB  
117  C  CB  B SER   A 7   ? 0.3094 0.3235 0.3128 -0.0568 0.0313  -0.0119 7   SER   A CB  
118  O  OG  A SER   A 7   ? 0.2926 0.3760 0.2682 -0.0902 0.0636  -0.0118 7   SER   A OG  
119  O  OG  B SER   A 7   ? 0.3149 0.3292 0.3312 -0.0522 0.0269  -0.0106 7   SER   A OG  
130  N  N   A GLY   A 8   ? 0.2138 0.2695 0.1583 -0.0841 0.0450  -0.0152 8   GLY   A N   
131  N  N   B GLY   A 8   ? 0.2705 0.2834 0.2513 -0.0556 0.0481  -0.0048 8   GLY   A N   
132  C  CA  A GLY   A 8   ? 0.2010 0.2480 0.1640 -0.0563 0.0346  0.0008  8   GLY   A CA  
133  C  CA  B GLY   A 8   ? 0.2521 0.2646 0.2322 -0.0526 0.0442  -0.0009 8   GLY   A CA  
134  C  C   A GLY   A 8   ? 0.1783 0.2253 0.1600 -0.0386 0.0344  0.0068  8   GLY   A C   
135  C  C   B GLY   A 8   ? 0.2319 0.2485 0.2036 -0.0515 0.0381  0.0015  8   GLY   A C   
136  O  O   A GLY   A 8   ? 0.1895 0.2255 0.1709 -0.0174 0.0308  -0.0100 8   GLY   A O   
137  O  O   B GLY   A 8   ? 0.2372 0.2491 0.1993 -0.0513 0.0385  -0.0075 8   GLY   A O   
144  N  N   A TYR   A 9   ? 0.1556 0.2147 0.1627 -0.0294 0.0260  0.0129  9   TYR   A N   
145  N  N   B TYR   A 9   ? 0.2065 0.2329 0.1888 -0.0442 0.0288  0.0114  9   TYR   A N   
146  C  CA  A TYR   A 9   ? 0.1501 0.2016 0.1505 -0.0359 0.0197  0.0146  9   TYR   A CA  
147  C  CA  B TYR   A 9   ? 0.1847 0.2135 0.1763 -0.0366 0.0225  0.0187  9   TYR   A CA  
148  C  C   A TYR   A 9   ? 0.1526 0.1817 0.1478 -0.0281 0.0179  0.0327  9   TYR   A C   
149  C  C   B TYR   A 9   ? 0.1729 0.1965 0.1759 -0.0270 0.0203  0.0186  9   TYR   A C   
150  O  O   A TYR   A 9   ? 0.1742 0.2039 0.1601 -0.0214 0.0110  0.0317  9   TYR   A O   
151  O  O   B TYR   A 9   ? 0.1771 0.2081 0.2051 -0.0307 0.0203  0.0296  9   TYR   A O   
152  C  CB  A TYR   A 9   ? 0.1451 0.2199 0.1659 -0.0304 0.0218  0.0006  9   TYR   A CB  
153  C  CB  B TYR   A 9   ? 0.1748 0.2147 0.1875 -0.0332 0.0132  0.0131  9   TYR   A CB  
154  C  CG  A TYR   A 9   ? 0.1555 0.2255 0.1792 -0.0269 0.0306  -0.0066 9   TYR   A CG  
155  C  CG  B TYR   A 9   ? 0.1691 0.2137 0.1829 -0.0291 0.0112  0.0159  9   TYR   A CG  
156  C  CD1 A TYR   A 9   ? 0.1598 0.2267 0.1993 -0.0337 0.0451  -0.0196 9   TYR   A CD1 
157  C  CD1 B TYR   A 9   ? 0.1704 0.2137 0.1892 -0.0317 0.0212  0.0167  9   TYR   A CD1 
158  C  CD2 A TYR   A 9   ? 0.1580 0.2239 0.1782 -0.0229 0.0279  0.0111  9   TYR   A CD2 
159  C  CD2 B TYR   A 9   ? 0.1641 0.2134 0.1718 -0.0225 -0.0003 0.0216  9   TYR   A CD2 
160  C  CE1 A TYR   A 9   ? 0.1723 0.2265 0.2098 -0.0345 0.0486  -0.0236 9   TYR   A CE1 
161  C  CE1 B TYR   A 9   ? 0.1675 0.2129 0.1812 -0.0300 0.0248  0.0155  9   TYR   A CE1 
162  C  CE2 A TYR   A 9   ? 0.1651 0.2251 0.1986 -0.0227 0.0354  0.0025  9   TYR   A CE2 
163  C  CE2 B TYR   A 9   ? 0.1596 0.2132 0.1676 -0.0194 0.0089  0.0212  9   TYR   A CE2 
164  C  CZ  A TYR   A 9   ? 0.1708 0.2260 0.2181 -0.0378 0.0553  -0.0137 9   TYR   A CZ  
165  C  CZ  B TYR   A 9   ? 0.1564 0.2128 0.1779 -0.0249 0.0298  0.0129  9   TYR   A CZ  
166  O  OH  A TYR   A 9   ? 0.1835 0.2321 0.2582 -0.0515 0.0580  -0.0192 9   TYR   A OH  
167  O  OH  B TYR   A 9   ? 0.1485 0.2154 0.1985 -0.0281 0.0483  0.0043  9   TYR   A OH  
186  N  N   A LEU   A 10  ? 0.1543 0.1615 0.1487 -0.0243 0.0133  0.0186  10  LEU   A N   
187  N  N   B LEU   A 10  ? 0.1687 0.1747 0.1602 -0.0164 0.0205  0.0017  10  LEU   A N   
188  C  CA  A LEU   A 10  ? 0.1496 0.1555 0.1506 -0.0267 0.0193  0.0351  10  LEU   A CA  
189  C  CA  B LEU   A 10  ? 0.1673 0.1668 0.1631 -0.0093 0.0206  -0.0089 10  LEU   A CA  
190  C  C   A LEU   A 10  ? 0.1445 0.1462 0.1678 -0.0218 0.0130  0.0368  10  LEU   A C   
191  C  C   B LEU   A 10  ? 0.1663 0.1543 0.1516 -0.0068 0.0124  -0.0061 10  LEU   A C   
192  O  O   A LEU   A 10  ? 0.1502 0.1383 0.1790 -0.0212 0.0374  0.0317  10  LEU   A O   
193  O  O   B LEU   A 10  ? 0.1724 0.1499 0.1462 -0.0044 0.0227  -0.0057 10  LEU   A O   
194  C  CB  A LEU   A 10  ? 0.1520 0.1666 0.1823 -0.0251 -0.0058 0.0474  10  LEU   A CB  
195  C  CB  B LEU   A 10  ? 0.1718 0.1685 0.1665 -0.0100 0.0041  -0.0092 10  LEU   A CB  
196  C  CG  A LEU   A 10  ? 0.1709 0.1805 0.2384 -0.0090 -0.0267 0.0511  10  LEU   A CG  
197  C  CG  B LEU   A 10  ? 0.1759 0.1739 0.1877 -0.0058 -0.0177 -0.0084 10  LEU   A CG  
198  C  CD1 A LEU   A 10  ? 0.1902 0.1887 0.2555 -0.0138 -0.0163 0.0419  10  LEU   A CD1 
199  C  CD1 B LEU   A 10  ? 0.1796 0.1782 0.1995 -0.0197 -0.0133 -0.0110 10  LEU   A CD1 
200  C  CD2 A LEU   A 10  ? 0.1839 0.2005 0.2511 0.0026  -0.0087 0.0404  10  LEU   A CD2 
201  C  CD2 B LEU   A 10  ? 0.1932 0.1824 0.2008 0.0117  -0.0361 -0.0114 10  LEU   A CD2 
224  N  N   A LYS   A 11  ? 0.1469 0.1530 0.1683 -0.0211 0.0144  0.0416  11  LYS   A N   
225  N  N   B LYS   A 11  ? 0.1681 0.1530 0.1511 -0.0074 -0.0028 0.0037  11  LYS   A N   
226  C  CA  A LYS   A 11  ? 0.1418 0.1532 0.1771 -0.0322 0.0169  0.0362  11  LYS   A CA  
227  C  CA  B LYS   A 11  ? 0.1630 0.1429 0.1518 -0.0143 -0.0010 0.0131  11  LYS   A CA  
228  C  C   A LYS   A 11  ? 0.1426 0.1589 0.1713 -0.0312 0.0169  0.0222  11  LYS   A C   
229  C  C   B LYS   A 11  ? 0.1514 0.1314 0.1508 -0.0187 -0.0018 0.0042  11  LYS   A C   
230  O  O   A LYS   A 11  ? 0.1527 0.1871 0.2199 -0.0476 0.0270  0.0044  11  LYS   A O   
231  O  O   B LYS   A 11  ? 0.1492 0.1256 0.1635 -0.0169 0.0026  -0.0123 11  LYS   A O   
232  C  CB  A LYS   A 11  ? 0.1570 0.1467 0.1750 -0.0271 0.0141  0.0236  11  LYS   A CB  
233  C  CB  B LYS   A 11  ? 0.1702 0.1457 0.1572 -0.0098 -0.0020 0.0217  11  LYS   A CB  
234  C  CG  A LYS   A 11  ? 0.1679 0.1464 0.1859 -0.0252 0.0136  0.0289  11  LYS   A CG  
235  C  CG  B LYS   A 11  ? 0.1734 0.1544 0.1620 -0.0084 0.0014  0.0312  11  LYS   A CG  
236  C  CD  A LYS   A 11  ? 0.1734 0.1558 0.1802 -0.0311 0.0011  0.0372  11  LYS   A CD  
237  C  CD  B LYS   A 11  ? 0.1714 0.1638 0.1702 -0.0088 0.0043  0.0318  11  LYS   A CD  
238  C  CE  A LYS   A 11  ? 0.1792 0.1591 0.1755 -0.0189 -0.0038 0.0448  11  LYS   A CE  
239  C  CE  B LYS   A 11  ? 0.1686 0.1670 0.1734 -0.0092 -0.0025 0.0311  11  LYS   A CE  
240  N  NZ  A LYS   A 11  ? 0.1673 0.1664 0.1906 -0.0062 0.0013  0.0468  11  LYS   A NZ  
241  N  NZ  B LYS   A 11  ? 0.1683 0.1683 0.1892 -0.0067 -0.0027 0.0224  11  LYS   A NZ  
268  N  N   A LEU   A 12  ? 0.1364 0.1475 0.1529 -0.0282 0.0130  0.0214  12  LEU   A N   
269  N  N   B LEU   A 12  ? 0.1446 0.1377 0.1533 -0.0093 -0.0047 -0.0052 12  LEU   A N   
270  C  CA  A LEU   A 12  ? 0.1413 0.1589 0.1578 -0.0139 0.0029  0.0329  12  LEU   A CA  
271  C  CA  B LEU   A 12  ? 0.1416 0.1424 0.1614 -0.0107 0.0080  -0.0027 12  LEU   A CA  
272  C  C   A LEU   A 12  ? 0.1462 0.1510 0.1710 -0.0266 0.0051  0.0351  12  LEU   A C   
273  C  C   B LEU   A 12  ? 0.1384 0.1417 0.1618 -0.0124 0.0241  0.0093  12  LEU   A C   
274  O  O   A LEU   A 12  ? 0.1573 0.1468 0.1799 -0.0199 0.0049  0.0164  12  LEU   A O   
275  O  O   B LEU   A 12  ? 0.1411 0.1448 0.1641 -0.0057 0.0287  0.0156  12  LEU   A O   
276  C  CB  A LEU   A 12  ? 0.1525 0.1537 0.1606 -0.0176 -0.0046 0.0300  12  LEU   A CB  
277  C  CB  B LEU   A 12  ? 0.1545 0.1544 0.1733 -0.0026 0.0184  0.0030  12  LEU   A CB  
278  C  CG  A LEU   A 12  ? 0.1525 0.1589 0.1816 -0.0074 0.0093  0.0242  12  LEU   A CG  
279  C  CG  B LEU   A 12  ? 0.1567 0.1615 0.1936 0.0097  0.0296  0.0030  12  LEU   A CG  
280  C  CD1 A LEU   A 12  ? 0.1533 0.1635 0.1863 0.0061  0.0108  0.0403  12  LEU   A CD1 
281  C  CD1 B LEU   A 12  ? 0.1566 0.1681 0.2021 0.0169  0.0398  0.0078  12  LEU   A CD1 
282  C  CD2 A LEU   A 12  ? 0.1586 0.1710 0.2019 -0.0126 0.0142  0.0214  12  LEU   A CD2 
283  C  CD2 B LEU   A 12  ? 0.1579 0.1664 0.2004 0.0139  0.0211  -0.0171 12  LEU   A CD2 
306  N  N   A THR   A 13  ? 0.1432 0.1463 0.1930 -0.0234 0.0054  0.0256  13  THR   A N   
307  N  N   B THR   A 13  ? 0.1309 0.1410 0.1684 -0.0177 0.0212  0.0014  13  THR   A N   
308  C  CA  A THR   A 13  ? 0.1525 0.1518 0.2113 -0.0121 0.0191  0.0232  13  THR   A CA  
309  C  CA  B THR   A 13  ? 0.1331 0.1450 0.1841 -0.0234 0.0143  0.0063  13  THR   A CA  
310  C  C   A THR   A 13  ? 0.1549 0.1487 0.2141 -0.0181 0.0114  0.0426  13  THR   A C   
311  C  C   B THR   A 13  ? 0.1360 0.1605 0.1778 -0.0244 0.0120  0.0132  13  THR   A C   
312  O  O   A THR   A 13  ? 0.1562 0.1548 0.2149 -0.0073 0.0102  0.0348  13  THR   A O   
313  O  O   B THR   A 13  ? 0.1413 0.1693 0.1664 -0.0306 -0.0002 0.0248  13  THR   A O   
314  C  CB  A THR   A 13  ? 0.1608 0.1683 0.2069 -0.0043 0.0246  0.0290  13  THR   A CB  
315  C  CB  B THR   A 13  ? 0.1299 0.1508 0.1900 -0.0162 0.0156  0.0170  13  THR   A CB  
316  O  OG1 A THR   A 13  ? 0.1655 0.1586 0.2238 -0.0039 0.0030  0.0382  13  THR   A OG1 
317  O  OG1 B THR   A 13  ? 0.1115 0.1520 0.1925 -0.0238 0.0435  0.0379  13  THR   A OG1 
318  C  CG2 A THR   A 13  ? 0.1686 0.1887 0.2304 0.0002  0.0299  0.0320  13  THR   A CG2 
319  C  CG2 B THR   A 13  ? 0.1335 0.1548 0.2006 -0.0068 0.0083  0.0093  13  THR   A CG2 
334  N  N   A ASP   A 14  ? 0.1538 0.1535 0.2445 -0.0237 0.0023  0.0559  14  ASP   A N   
335  N  N   B ASP   A 14  ? 0.1382 0.1716 0.2025 -0.0208 0.0093  0.0149  14  ASP   A N   
336  C  CA  A ASP   A 14  ? 0.1544 0.1712 0.2531 -0.0285 -0.0065 0.0753  14  ASP   A CA  
337  C  CA  B ASP   A 14  ? 0.1508 0.1851 0.2163 -0.0141 0.0024  0.0348  14  ASP   A CA  
338  C  C   A ASP   A 14  ? 0.1592 0.1833 0.2199 -0.0309 -0.0191 0.0771  14  ASP   A C   
339  C  C   B ASP   A 14  ? 0.1555 0.1829 0.2070 -0.0226 -0.0088 0.0539  14  ASP   A C   
340  O  O   A ASP   A 14  ? 0.1851 0.1960 0.2387 -0.0487 -0.0296 0.0758  14  ASP   A O   
341  O  O   B ASP   A 14  ? 0.1700 0.1849 0.2119 -0.0328 -0.0144 0.0525  14  ASP   A O   
342  C  CB  A ASP   A 14  ? 0.1629 0.1983 0.3063 -0.0238 -0.0107 0.0864  14  ASP   A CB  
343  C  CB  B ASP   A 14  ? 0.1643 0.2019 0.2482 -0.0003 0.0016  0.0385  14  ASP   A CB  
344  C  CG  A ASP   A 14  ? 0.1938 0.2485 0.3817 -0.0190 -0.0093 0.0780  14  ASP   A CG  
345  C  CG  B ASP   A 14  ? 0.1762 0.2179 0.2777 0.0017  -0.0005 0.0407  14  ASP   A CG  
346  O  OD1 A ASP   A 14  ? 0.2097 0.2761 0.4080 0.0010  -0.0324 0.0768  14  ASP   A OD1 
347  O  OD1 B ASP   A 14  ? 0.1771 0.2238 0.2800 0.0123  0.0010  0.0450  14  ASP   A OD1 
348  O  OD2 A ASP   A 14  ? 0.2164 0.2657 0.4224 -0.0276 -0.0123 0.0505  14  ASP   A OD2 
349  O  OD2 B ASP   A 14  ? 0.1850 0.2261 0.2970 -0.0016 -0.0072 0.0330  14  ASP   A OD2 
358  N  N   . ASN   A 15  ? 0.1516 0.1701 0.2128 -0.0283 -0.0061 0.0684  15  ASN   A N   
359  C  CA  . ASN   A 15  ? 0.1428 0.1710 0.2280 -0.0232 -0.0123 0.0569  15  ASN   A CA  
360  C  C   . ASN   A 15  ? 0.1465 0.1719 0.2431 -0.0217 -0.0067 0.0542  15  ASN   A C   
361  O  O   . ASN   A 15  ? 0.1507 0.1674 0.2915 -0.0271 -0.0253 0.0517  15  ASN   A O   
362  C  CB  . ASN   A 15  ? 0.1484 0.1705 0.2147 -0.0180 -0.0135 0.0476  15  ASN   A CB  
363  C  CG  . ASN   A 15  ? 0.1459 0.1822 0.2251 -0.0198 -0.0106 0.0325  15  ASN   A CG  
364  O  OD1 . ASN   A 15  ? 0.1611 0.1855 0.2352 -0.0294 -0.0025 0.0376  15  ASN   A OD1 
365  N  ND2 . ASN   A 15  ? 0.1557 0.1930 0.2184 -0.0262 0.0020  0.0350  15  ASN   A ND2 
373  N  N   A VAL   A 16  ? 0.1394 0.1619 0.2231 -0.0245 -0.0059 0.0574  16  VAL   A N   
374  N  N   B VAL   A 16  ? 0.1494 0.1742 0.2114 -0.0136 0.0006  0.0460  16  VAL   A N   
375  C  CA  A VAL   A 16  ? 0.1440 0.1690 0.2095 -0.0210 0.0007  0.0483  16  VAL   A CA  
376  C  CA  B VAL   A 16  ? 0.1544 0.1796 0.1760 -0.0087 0.0069  0.0436  16  VAL   A CA  
377  C  C   A VAL   A 16  ? 0.1365 0.1612 0.1898 -0.0244 -0.0074 0.0411  16  VAL   A C   
378  C  C   B VAL   A 16  ? 0.1507 0.1836 0.1706 -0.0128 0.0055  0.0392  16  VAL   A C   
379  O  O   A VAL   A 16  ? 0.1283 0.1557 0.1703 -0.0272 -0.0020 0.0314  16  VAL   A O   
380  O  O   B VAL   A 16  ? 0.1486 0.1933 0.1637 -0.0106 0.0177  0.0339  16  VAL   A O   
381  C  CB  A VAL   A 16  ? 0.1522 0.1836 0.2160 0.0030  0.0283  0.0565  16  VAL   A CB  
382  C  CB  B VAL   A 16  ? 0.1628 0.1789 0.1612 0.0083  0.0216  0.0450  16  VAL   A CB  
383  C  CG1 A VAL   A 16  ? 0.1651 0.1913 0.2242 0.0131  0.0361  0.0629  16  VAL   A CG1 
384  C  CG1 B VAL   A 16  ? 0.1708 0.1805 0.1657 0.0112  0.0283  0.0504  16  VAL   A CG1 
385  C  CG2 A VAL   A 16  ? 0.1575 0.1909 0.2225 0.0021  0.0505  0.0548  16  VAL   A CG2 
386  C  CG2 B VAL   A 16  ? 0.1663 0.1807 0.1696 0.0140  0.0346  0.0371  16  VAL   A CG2 
405  N  N   A TYR   A 17  ? 0.1363 0.1490 0.1945 -0.0177 0.0154  0.0489  17  TYR   A N   
406  N  N   B TYR   A 17  ? 0.1483 0.1738 0.1741 -0.0189 -0.0025 0.0348  17  TYR   A N   
407  C  CA  A TYR   A 17  ? 0.1430 0.1550 0.1725 -0.0250 0.0042  0.0467  17  TYR   A CA  
408  C  CA  B TYR   A 17  ? 0.1426 0.1717 0.1636 -0.0263 -0.0044 0.0341  17  TYR   A CA  
409  C  C   A TYR   A 17  ? 0.1399 0.1489 0.1794 -0.0207 0.0022  0.0328  17  TYR   A C   
410  C  C   B TYR   A 17  ? 0.1420 0.1730 0.1507 -0.0316 -0.0017 0.0297  17  TYR   A C   
411  O  O   A TYR   A 17  ? 0.1371 0.1448 0.1858 -0.0196 0.0077  0.0376  17  TYR   A O   
412  O  O   B TYR   A 17  ? 0.1356 0.1763 0.1353 -0.0335 -0.0031 0.0279  17  TYR   A O   
413  C  CB  A TYR   A 17  ? 0.1670 0.1649 0.1895 -0.0374 -0.0109 0.0458  17  TYR   A CB  
414  C  CB  B TYR   A 17  ? 0.1488 0.1724 0.1619 -0.0204 -0.0049 0.0350  17  TYR   A CB  
415  C  CG  A TYR   A 17  ? 0.1862 0.1717 0.2084 -0.0395 -0.0273 0.0443  17  TYR   A CG  
416  C  CG  B TYR   A 17  ? 0.1545 0.1750 0.1597 -0.0098 -0.0044 0.0303  17  TYR   A CG  
417  C  CD1 A TYR   A 17  ? 0.1972 0.1789 0.2300 -0.0328 -0.0301 0.0371  17  TYR   A CD1 
418  C  CD1 B TYR   A 17  ? 0.1609 0.1757 0.1629 0.0009  -0.0041 0.0314  17  TYR   A CD1 
419  C  CD2 A TYR   A 17  ? 0.1989 0.1737 0.2047 -0.0467 -0.0272 0.0509  17  TYR   A CD2 
420  C  CD2 B TYR   A 17  ? 0.1601 0.1782 0.1604 -0.0102 0.0015  0.0289  17  TYR   A CD2 
421  C  CE1 A TYR   A 17  ? 0.2016 0.1797 0.2421 -0.0379 -0.0428 0.0379  17  TYR   A CE1 
422  C  CE1 B TYR   A 17  ? 0.1681 0.1772 0.1691 0.0001  -0.0034 0.0348  17  TYR   A CE1 
423  C  CE2 A TYR   A 17  ? 0.2092 0.1726 0.2161 -0.0408 -0.0381 0.0436  17  TYR   A CE2 
424  C  CE2 B TYR   A 17  ? 0.1661 0.1776 0.1618 -0.0052 -0.0037 0.0307  17  TYR   A CE2 
425  C  CZ  A TYR   A 17  ? 0.2115 0.1712 0.2276 -0.0409 -0.0398 0.0464  17  TYR   A CZ  
426  C  CZ  B TYR   A 17  ? 0.1643 0.1739 0.1595 -0.0023 -0.0053 0.0408  17  TYR   A CZ  
427  O  OH  A TYR   A 17  ? 0.2290 0.1732 0.2221 -0.0270 -0.0262 0.0385  17  TYR   A OH  
428  O  OH  B TYR   A 17  ? 0.1575 0.1724 0.1557 0.0069  -0.0020 0.0460  17  TYR   A OH  
447  N  N   A ILE   A 18  ? 0.1487 0.1559 0.1553 -0.0182 0.0091  0.0462  18  ILE   A N   
448  N  N   B ILE   A 18  ? 0.1441 0.1693 0.1410 -0.0349 0.0102  0.0247  18  ILE   A N   
449  C  CA  A ILE   A 18  ? 0.1502 0.1529 0.1581 -0.0112 0.0125  0.0318  18  ILE   A CA  
450  C  CA  B ILE   A 18  ? 0.1438 0.1633 0.1218 -0.0286 0.0174  0.0175  18  ILE   A CA  
451  C  C   A ILE   A 18  ? 0.1564 0.1568 0.1767 -0.0249 0.0097  0.0369  18  ILE   A C   
452  C  C   B ILE   A 18  ? 0.1392 0.1697 0.1077 -0.0378 0.0070  0.0135  18  ILE   A C   
453  O  O   A ILE   A 18  ? 0.1525 0.1767 0.1751 -0.0292 0.0238  0.0434  18  ILE   A O   
454  O  O   B ILE   A 18  ? 0.1382 0.1760 0.1130 -0.0420 0.0119  0.0197  18  ILE   A O   
455  C  CB  A ILE   A 18  ? 0.1558 0.1559 0.1533 0.0023  0.0117  0.0318  18  ILE   A CB  
456  C  CB  B ILE   A 18  ? 0.1473 0.1509 0.1047 -0.0138 0.0301  0.0173  18  ILE   A CB  
457  C  CG1 A ILE   A 18  ? 0.1626 0.1588 0.1371 0.0065  0.0053  0.0203  18  ILE   A CG1 
458  C  CG1 B ILE   A 18  ? 0.1599 0.1507 0.1167 -0.0134 0.0408  0.0200  18  ILE   A CG1 
459  C  CG2 A ILE   A 18  ? 0.1608 0.1527 0.1643 0.0019  0.0152  0.0245  18  ILE   A CG2 
460  C  CG2 B ILE   A 18  ? 0.1539 0.1541 0.1167 -0.0152 0.0293  0.0226  18  ILE   A CG2 
461  C  CD1 A ILE   A 18  ? 0.1856 0.1671 0.1656 0.0177  0.0029  0.0296  18  ILE   A CD1 
462  C  CD1 B ILE   A 18  ? 0.1713 0.1551 0.1344 -0.0096 0.0455  0.0039  18  ILE   A CD1 
485  N  N   A LYS   A 19  ? 0.1569 0.1538 0.1675 -0.0183 0.0218  0.0365  19  LYS   A N   
486  N  N   B LYS   A 19  ? 0.1411 0.1723 0.1055 -0.0299 0.0211  0.0074  19  LYS   A N   
487  C  CA  A LYS   A 19  ? 0.1709 0.1749 0.1551 -0.0200 0.0321  0.0279  19  LYS   A CA  
488  C  CA  B LYS   A 19  ? 0.1576 0.1866 0.1283 -0.0227 0.0225  -0.0078 19  LYS   A CA  
489  C  C   A LYS   A 19  ? 0.1587 0.1676 0.1709 -0.0130 0.0301  0.0401  19  LYS   A C   
490  C  C   B LYS   A 19  ? 0.1597 0.1853 0.1434 -0.0113 0.0183  -0.0038 19  LYS   A C   
491  O  O   A LYS   A 19  ? 0.1575 0.1580 0.1785 -0.0177 0.0314  0.0375  19  LYS   A O   
492  O  O   B LYS   A 19  ? 0.1662 0.1893 0.1544 -0.0147 0.0134  -0.0001 19  LYS   A O   
493  C  CB  A LYS   A 19  ? 0.1957 0.2036 0.1743 -0.0287 0.0337  0.0160  19  LYS   A CB  
494  C  CB  B LYS   A 19  ? 0.1692 0.2025 0.1395 -0.0207 0.0305  -0.0277 19  LYS   A CB  
495  C  CG  A LYS   A 19  ? 0.2292 0.2175 0.1809 -0.0358 0.0371  0.0012  19  LYS   A CG  
496  C  CG  B LYS   A 19  ? 0.1938 0.2176 0.1559 -0.0188 0.0291  -0.0316 19  LYS   A CG  
497  C  CD  A LYS   A 19  ? 0.2563 0.2338 0.1987 -0.0422 0.0528  0.0031  19  LYS   A CD  
498  C  CD  B LYS   A 19  ? 0.2154 0.2302 0.1811 -0.0188 0.0226  -0.0259 19  LYS   A CD  
499  C  CE  A LYS   A 19  ? 0.2772 0.2369 0.2088 -0.0483 0.0537  -0.0057 19  LYS   A CE  
500  C  CE  B LYS   A 19  ? 0.2286 0.2374 0.1918 -0.0214 0.0218  -0.0231 19  LYS   A CE  
501  N  NZ  A LYS   A 19  ? 0.2884 0.2377 0.2086 -0.0564 0.0696  -0.0181 19  LYS   A NZ  
502  N  NZ  B LYS   A 19  ? 0.2368 0.2392 0.2030 -0.0245 0.0281  -0.0299 19  LYS   A NZ  
529  N  N   A ASN   A 20  ? 0.1616 0.1691 0.2006 -0.0174 0.0317  0.0500  20  ASN   A N   
530  N  N   B ASN   A 20  ? 0.1656 0.1897 0.1699 0.0019  0.0295  -0.0048 20  ASN   A N   
531  C  CA  A ASN   A 20  ? 0.1808 0.1857 0.2433 -0.0015 0.0555  0.0459  20  ASN   A CA  
532  C  CA  B ASN   A 20  ? 0.1755 0.1990 0.2036 0.0110  0.0385  -0.0068 20  ASN   A CA  
533  C  C   A ASN   A 20  ? 0.2005 0.1904 0.2540 -0.0051 0.0820  0.0353  20  ASN   A C   
534  C  C   B ASN   A 20  ? 0.1907 0.1947 0.2135 0.0078  0.0527  -0.0149 20  ASN   A C   
535  O  O   A ASN   A 20  ? 0.2194 0.1903 0.2745 -0.0166 0.0793  0.0201  20  ASN   A O   
536  O  O   B ASN   A 20  ? 0.1952 0.1954 0.2346 0.0128  0.0558  -0.0248 20  ASN   A O   
537  C  CB  A ASN   A 20  ? 0.1914 0.1854 0.2658 0.0141  0.0595  0.0628  20  ASN   A CB  
538  C  CB  B ASN   A 20  ? 0.1755 0.2095 0.2223 0.0230  0.0402  0.0005  20  ASN   A CB  
539  C  CG  A ASN   A 20  ? 0.2105 0.1889 0.3146 0.0322  0.0718  0.0637  20  ASN   A CG  
540  C  CG  B ASN   A 20  ? 0.1808 0.2190 0.2605 0.0359  0.0513  0.0103  20  ASN   A CG  
541  O  OD1 A ASN   A 20  ? 0.2480 0.2136 0.3922 0.0414  0.0933  0.0575  20  ASN   A OD1 
542  O  OD1 B ASN   A 20  ? 0.1925 0.2201 0.2905 0.0479  0.0769  0.0030  20  ASN   A OD1 
543  N  ND2 A ASN   A 20  ? 0.2142 0.1649 0.2997 0.0308  0.0521  0.0730  20  ASN   A ND2 
544  N  ND2 B ASN   A 20  ? 0.1875 0.2227 0.2729 0.0285  0.0371  0.0271  20  ASN   A ND2 
557  N  N   A ALA   A 21  ? 0.2036 0.1931 0.2552 0.0019  0.0736  0.0226  21  ALA   A N   
558  N  N   B ALA   A 21  ? 0.2011 0.1885 0.2217 0.0035  0.0436  -0.0157 21  ALA   A N   
559  C  CA  A ALA   A 21  ? 0.2053 0.1855 0.2474 -0.0022 0.0616  0.0277  21  ALA   A CA  
560  C  CA  B ALA   A 21  ? 0.2098 0.1803 0.2217 -0.0060 0.0380  -0.0100 21  ALA   A CA  
561  C  C   A ALA   A 21  ? 0.1824 0.1851 0.2435 -0.0037 0.0524  0.0220  21  ALA   A C   
562  C  C   B ALA   A 21  ? 0.1997 0.1723 0.2046 -0.0104 0.0497  0.0019  21  ALA   A C   
563  O  O   A ALA   A 21  ? 0.1789 0.1917 0.2418 0.0080  0.0449  0.0308  21  ALA   A O   
564  O  O   B ALA   A 21  ? 0.2004 0.1666 0.2154 -0.0035 0.0511  0.0013  21  ALA   A O   
565  C  CB  A ALA   A 21  ? 0.2215 0.1851 0.2472 -0.0092 0.0600  0.0306  21  ALA   A CB  
566  C  CB  B ALA   A 21  ? 0.2209 0.1791 0.2459 -0.0065 0.0262  -0.0121 21  ALA   A CB  
577  N  N   A ASP   A 22  ? 0.1828 0.1853 0.2604 -0.0121 0.0497  0.0194  22  ASP   A N   
578  N  N   B ASP   A 22  ? 0.1960 0.1710 0.1958 -0.0156 0.0553  0.0221  22  ASP   A N   
579  C  CA  A ASP   A 22  ? 0.1850 0.1802 0.2596 -0.0075 0.0400  0.0305  22  ASP   A CA  
580  C  CA  B ASP   A 22  ? 0.1970 0.1705 0.1965 -0.0136 0.0469  0.0282  22  ASP   A CA  
581  C  C   A ASP   A 22  ? 0.1772 0.1775 0.2233 -0.0057 0.0323  0.0278  22  ASP   A C   
582  C  C   B ASP   A 22  ? 0.1827 0.1669 0.1727 -0.0251 0.0484  0.0284  22  ASP   A C   
583  O  O   A ASP   A 22  ? 0.1846 0.1793 0.2365 -0.0110 0.0324  0.0247  22  ASP   A O   
584  O  O   B ASP   A 22  ? 0.1775 0.1708 0.1749 -0.0296 0.0417  0.0116  22  ASP   A O   
585  C  CB  A ASP   A 22  ? 0.2057 0.1844 0.3133 -0.0088 0.0290  0.0270  22  ASP   A CB  
586  C  CB  B ASP   A 22  ? 0.2125 0.1721 0.2116 0.0024  0.0485  0.0226  22  ASP   A CB  
587  C  CG  A ASP   A 22  ? 0.2255 0.1963 0.3715 -0.0115 0.0098  0.0320  22  ASP   A CG  
588  C  CG  B ASP   A 22  ? 0.2250 0.1707 0.2184 0.0130  0.0476  0.0214  22  ASP   A CG  
589  O  OD1 A ASP   A 22  ? 0.2226 0.1999 0.3970 -0.0209 -0.0001 0.0428  22  ASP   A OD1 
590  O  OD1 B ASP   A 22  ? 0.2250 0.1694 0.1979 0.0158  0.0496  0.0096  22  ASP   A OD1 
591  O  OD2 A ASP   A 22  ? 0.2495 0.2062 0.4051 -0.0029 0.0084  0.0162  22  ASP   A OD2 
592  O  OD2 B ASP   A 22  ? 0.2338 0.1767 0.2391 0.0138  0.0567  0.0256  22  ASP   A OD2 
601  N  N   A ILE   A 23  ? 0.1774 0.1784 0.1958 -0.0036 0.0279  0.0200  23  ILE   A N   
602  N  N   B ILE   A 23  ? 0.1789 0.1622 0.1677 -0.0217 0.0428  0.0215  23  ILE   A N   
603  C  CA  A ILE   A 23  ? 0.1755 0.1730 0.1846 -0.0076 0.0317  0.0203  23  ILE   A CA  
604  C  CA  B ILE   A 23  ? 0.1726 0.1650 0.1540 -0.0174 0.0316  0.0178  23  ILE   A CA  
605  C  C   A ILE   A 23  ? 0.1765 0.1835 0.1913 -0.0074 0.0458  0.0160  23  ILE   A C   
606  C  C   B ILE   A 23  ? 0.1813 0.1765 0.1723 -0.0231 0.0386  0.0029  23  ILE   A C   
607  O  O   A ILE   A 23  ? 0.1855 0.1883 0.1981 -0.0021 0.0416  0.0033  23  ILE   A O   
608  O  O   B ILE   A 23  ? 0.1796 0.1692 0.1584 -0.0184 0.0447  0.0038  23  ILE   A O   
609  C  CB  A ILE   A 23  ? 0.1854 0.1661 0.1629 -0.0033 0.0289  0.0162  23  ILE   A CB  
610  C  CB  B ILE   A 23  ? 0.1654 0.1598 0.1376 -0.0068 0.0099  0.0270  23  ILE   A CB  
611  C  CG1 A ILE   A 23  ? 0.1948 0.1621 0.1653 0.0007  0.0213  0.0133  23  ILE   A CG1 
612  C  CG1 B ILE   A 23  ? 0.1593 0.1548 0.1158 -0.0016 -0.0009 0.0242  23  ILE   A CG1 
613  C  CG2 A ILE   A 23  ? 0.1848 0.1744 0.1709 -0.0042 0.0326  0.0237  23  ILE   A CG2 
614  C  CG2 B ILE   A 23  ? 0.1650 0.1589 0.1328 -0.0018 -0.0029 0.0221  23  ILE   A CG2 
615  C  CD1 A ILE   A 23  ? 0.2004 0.1605 0.1856 0.0039  0.0074  0.0045  23  ILE   A CD1 
616  C  CD1 B ILE   A 23  ? 0.1490 0.1541 0.1280 0.0062  -0.0180 0.0131  23  ILE   A CD1 
639  N  N   A VAL   A 24  ? 0.1806 0.1919 0.1851 -0.0147 0.0495  0.0189  24  VAL   A N   
640  N  N   B VAL   A 24  ? 0.1927 0.1944 0.1862 -0.0320 0.0353  -0.0075 24  VAL   A N   
641  C  CA  A VAL   A 24  ? 0.1982 0.2033 0.2139 -0.0271 0.0420  0.0047  24  VAL   A CA  
642  C  CA  B VAL   A 24  ? 0.2047 0.2060 0.2047 -0.0341 0.0358  -0.0079 24  VAL   A CA  
643  C  C   A VAL   A 24  ? 0.2045 0.2166 0.2201 -0.0403 0.0379  0.0011  24  VAL   A C   
644  C  C   B VAL   A 24  ? 0.2114 0.2175 0.2145 -0.0365 0.0389  -0.0128 24  VAL   A C   
645  O  O   A VAL   A 24  ? 0.2183 0.2182 0.2233 -0.0345 0.0360  -0.0080 24  VAL   A O   
646  O  O   B VAL   A 24  ? 0.2199 0.2189 0.2250 -0.0276 0.0427  -0.0088 24  VAL   A O   
647  C  CB  A VAL   A 24  ? 0.2035 0.2030 0.2394 -0.0240 0.0473  -0.0021 24  VAL   A CB  
648  C  CB  B VAL   A 24  ? 0.2101 0.2078 0.2142 -0.0303 0.0335  -0.0087 24  VAL   A CB  
649  C  CG1 A VAL   A 24  ? 0.2066 0.2112 0.2510 -0.0159 0.0496  -0.0196 24  VAL   A CG1 
650  C  CG1 B VAL   A 24  ? 0.2189 0.2131 0.2259 -0.0201 0.0325  -0.0153 24  VAL   A CG1 
651  C  CG2 A VAL   A 24  ? 0.2172 0.2064 0.2332 -0.0185 0.0677  0.0094  24  VAL   A CG2 
652  C  CG2 B VAL   A 24  ? 0.2110 0.2032 0.2025 -0.0416 0.0341  -0.0115 24  VAL   A CG2 
671  N  N   A GLU   A 25  ? 0.2064 0.2425 0.2200 -0.0365 0.0551  -0.0069 25  GLU   A N   
672  N  N   B GLU   A 25  ? 0.2132 0.2351 0.2147 -0.0351 0.0452  -0.0271 25  GLU   A N   
673  C  CA  A GLU   A 25  ? 0.2213 0.2700 0.2282 -0.0209 0.0625  -0.0202 25  GLU   A CA  
674  C  CA  B GLU   A 25  ? 0.2229 0.2560 0.2252 -0.0339 0.0402  -0.0272 25  GLU   A CA  
675  C  C   A GLU   A 25  ? 0.2094 0.2769 0.2001 -0.0366 0.0624  -0.0182 25  GLU   A C   
676  C  C   B GLU   A 25  ? 0.2235 0.2628 0.2099 -0.0336 0.0436  -0.0251 25  GLU   A C   
677  O  O   A GLU   A 25  ? 0.2140 0.2898 0.2048 -0.0437 0.0541  -0.0231 25  GLU   A O   
678  O  O   B GLU   A 25  ? 0.2278 0.2646 0.2168 -0.0344 0.0454  -0.0261 25  GLU   A O   
679  C  CB  A GLU   A 25  ? 0.2489 0.2940 0.2725 -0.0083 0.0594  -0.0241 25  GLU   A CB  
680  C  CB  B GLU   A 25  ? 0.2331 0.2681 0.2578 -0.0330 0.0357  -0.0251 25  GLU   A CB  
681  C  CG  A GLU   A 25  ? 0.2830 0.3171 0.3331 -0.0142 0.0300  -0.0240 25  GLU   A CG  
682  C  CG  B GLU   A 25  ? 0.2471 0.2804 0.2989 -0.0342 0.0257  -0.0193 25  GLU   A CG  
683  C  CD  A GLU   A 25  ? 0.3099 0.3382 0.3803 -0.0218 0.0158  -0.0243 25  GLU   A CD  
684  C  CD  B GLU   A 25  ? 0.2551 0.2896 0.3414 -0.0396 0.0105  -0.0181 25  GLU   A CD  
685  O  OE1 A GLU   A 25  ? 0.3202 0.3438 0.3892 -0.0190 0.0081  -0.0384 25  GLU   A OE1 
686  O  OE1 B GLU   A 25  ? 0.2560 0.2922 0.3597 -0.0414 0.0041  -0.0186 25  GLU   A OE1 
687  O  OE2 A GLU   A 25  ? 0.3190 0.3507 0.4172 -0.0261 0.0085  -0.0300 25  GLU   A OE2 
688  O  OE2 B GLU   A 25  ? 0.2605 0.2945 0.3552 -0.0415 0.0042  -0.0185 25  GLU   A OE2 
701  N  N   A GLU   A 26  ? 0.1979 0.2652 0.1914 -0.0529 0.0709  -0.0109 26  GLU   A N   
702  N  N   B GLU   A 26  ? 0.2223 0.2662 0.2000 -0.0364 0.0497  -0.0206 26  GLU   A N   
703  C  CA  A GLU   A 26  ? 0.2119 0.2586 0.1645 -0.0665 0.0613  -0.0047 26  GLU   A CA  
704  C  CA  B GLU   A 26  ? 0.2286 0.2712 0.1981 -0.0353 0.0447  -0.0144 26  GLU   A CA  
705  C  C   A GLU   A 26  ? 0.2083 0.2467 0.1404 -0.0638 0.0458  -0.0038 26  GLU   A C   
706  C  C   B GLU   A 26  ? 0.2302 0.2681 0.1921 -0.0273 0.0452  -0.0077 26  GLU   A C   
707  O  O   A GLU   A 26  ? 0.2162 0.2486 0.1430 -0.0726 0.0398  -0.0019 26  GLU   A O   
708  O  O   B GLU   A 26  ? 0.2293 0.2648 0.1871 -0.0291 0.0573  -0.0044 26  GLU   A O   
709  C  CB  A GLU   A 26  ? 0.2367 0.2620 0.1850 -0.0794 0.0526  0.0019  26  GLU   A CB  
710  C  CB  B GLU   A 26  ? 0.2343 0.2783 0.2102 -0.0423 0.0297  -0.0187 26  GLU   A CB  
711  C  CG  A GLU   A 26  ? 0.2689 0.2903 0.2626 -0.0792 0.0504  -0.0104 26  GLU   A CG  
712  C  CG  B GLU   A 26  ? 0.2428 0.2836 0.2156 -0.0508 0.0231  -0.0221 26  GLU   A CG  
713  C  CD  A GLU   A 26  ? 0.2871 0.3099 0.3206 -0.0868 0.0696  -0.0251 26  GLU   A CD  
714  C  CD  B GLU   A 26  ? 0.2477 0.2872 0.2153 -0.0656 0.0230  -0.0245 26  GLU   A CD  
715  O  OE1 A GLU   A 26  ? 0.2799 0.3362 0.3001 -0.0809 0.1115  -0.0708 26  GLU   A OE1 
716  O  OE1 B GLU   A 26  ? 0.2581 0.3016 0.2123 -0.0596 0.0262  -0.0293 26  GLU   A OE1 
717  O  OE2 A GLU   A 26  ? 0.3104 0.3098 0.3340 -0.0898 0.0572  -0.0127 26  GLU   A OE2 
718  O  OE2 B GLU   A 26  ? 0.2413 0.2788 0.1789 -0.0825 0.0232  -0.0324 26  GLU   A OE2 
731  N  N   A ALA   A 27  ? 0.1948 0.2342 0.1314 -0.0649 0.0465  0.0015  27  ALA   A N   
732  N  N   B ALA   A 27  ? 0.2320 0.2681 0.1958 -0.0222 0.0376  -0.0019 27  ALA   A N   
733  C  CA  A ALA   A 27  ? 0.1998 0.2448 0.1446 -0.0603 0.0310  0.0004  27  ALA   A CA  
734  C  CA  B ALA   A 27  ? 0.2395 0.2748 0.1906 -0.0182 0.0280  0.0010  27  ALA   A CA  
735  C  C   A ALA   A 27  ? 0.2281 0.2570 0.1533 -0.0720 0.0350  -0.0203 27  ALA   A C   
736  C  C   B ALA   A 27  ? 0.2562 0.2869 0.1994 -0.0210 0.0203  -0.0045 27  ALA   A C   
737  O  O   A ALA   A 27  ? 0.2349 0.2573 0.1615 -0.0760 0.0191  -0.0087 27  ALA   A O   
738  O  O   B ALA   A 27  ? 0.2549 0.2844 0.1970 -0.0198 0.0141  0.0008  27  ALA   A O   
739  C  CB  A ALA   A 27  ? 0.1720 0.2428 0.1450 -0.0616 0.0190  0.0100  27  ALA   A CB  
740  C  CB  B ALA   A 27  ? 0.2307 0.2722 0.1855 -0.0175 0.0282  0.0059  27  ALA   A CB  
751  N  N   A LYS   A 28  ? 0.2647 0.2801 0.1798 -0.0679 0.0321  -0.0545 28  LYS   A N   
752  N  N   B LYS   A 28  ? 0.2788 0.3040 0.2228 -0.0234 0.0149  -0.0154 28  LYS   A N   
753  C  CA  A LYS   A 28  ? 0.3038 0.3136 0.2202 -0.0615 0.0399  -0.0720 28  LYS   A CA  
754  C  CA  B LYS   A 28  ? 0.3024 0.3242 0.2521 -0.0247 0.0098  -0.0218 28  LYS   A CA  
755  C  C   A LYS   A 28  ? 0.3180 0.3431 0.2101 -0.0691 0.0643  -0.0590 28  LYS   A C   
756  C  C   B LYS   A 28  ? 0.3200 0.3443 0.2562 -0.0341 0.0193  -0.0175 28  LYS   A C   
757  O  O   A LYS   A 28  ? 0.3235 0.3494 0.2450 -0.0647 0.0371  -0.0544 28  LYS   A O   
758  O  O   B LYS   A 28  ? 0.3214 0.3432 0.2578 -0.0323 0.0071  -0.0168 28  LYS   A O   
759  C  CB  A LYS   A 28  ? 0.3243 0.3242 0.2818 -0.0453 0.0334  -0.0763 28  LYS   A CB  
760  C  CB  B LYS   A 28  ? 0.3094 0.3260 0.2809 -0.0170 -0.0012 -0.0261 28  LYS   A CB  
761  C  CG  A LYS   A 28  ? 0.3396 0.3319 0.3430 -0.0344 0.0285  -0.0792 28  LYS   A CG  
762  C  CG  B LYS   A 28  ? 0.3165 0.3280 0.3226 -0.0117 -0.0069 -0.0287 28  LYS   A CG  
763  C  CD  A LYS   A 28  ? 0.3503 0.3473 0.4053 -0.0253 0.0195  -0.0843 28  LYS   A CD  
764  C  CD  B LYS   A 28  ? 0.3238 0.3346 0.3595 -0.0074 -0.0110 -0.0321 28  LYS   A CD  
765  C  CE  A LYS   A 28  ? 0.3537 0.3563 0.4585 -0.0219 0.0086  -0.0860 28  LYS   A CE  
766  C  CE  B LYS   A 28  ? 0.3293 0.3394 0.3964 -0.0077 -0.0130 -0.0305 28  LYS   A CE  
767  N  NZ  A LYS   A 28  ? 0.3612 0.3619 0.4822 -0.0173 0.0065  -0.0746 28  LYS   A NZ  
768  N  NZ  B LYS   A 28  ? 0.3309 0.3421 0.4108 -0.0062 -0.0166 -0.0279 28  LYS   A NZ  
795  N  N   A LYS   A 29  ? 0.3276 0.3700 0.1890 -0.0808 0.1023  -0.0354 29  LYS   A N   
796  N  N   B LYS   A 29  ? 0.3358 0.3661 0.2626 -0.0459 0.0399  -0.0092 29  LYS   A N   
797  C  CA  A LYS   A 29  ? 0.3466 0.4011 0.2067 -0.0820 0.1161  -0.0106 29  LYS   A CA  
798  C  CA  B LYS   A 29  ? 0.3512 0.3862 0.2773 -0.0550 0.0556  -0.0006 29  LYS   A CA  
799  C  C   A LYS   A 29  ? 0.3540 0.3977 0.1811 -0.0827 0.0952  0.0009  29  LYS   A C   
800  C  C   B LYS   A 29  ? 0.3516 0.3874 0.2343 -0.0711 0.0696  0.0059  29  LYS   A C   
801  O  O   A LYS   A 29  ? 0.3679 0.4082 0.2000 -0.0763 0.0788  -0.0049 29  LYS   A O   
802  O  O   B LYS   A 29  ? 0.3568 0.3918 0.2434 -0.0700 0.0641  0.0040  29  LYS   A O   
803  C  CB  A LYS   A 29  ? 0.3588 0.4317 0.2706 -0.0759 0.1345  0.0029  29  LYS   A CB  
804  C  CB  B LYS   A 29  ? 0.3643 0.4018 0.3379 -0.0468 0.0548  0.0030  29  LYS   A CB  
805  C  CG  A LYS   A 29  ? 0.3754 0.4531 0.3437 -0.0644 0.1364  -0.0001 29  LYS   A CG  
806  C  CG  B LYS   A 29  ? 0.3757 0.4116 0.3899 -0.0381 0.0548  0.0021  29  LYS   A CG  
807  C  CD  A LYS   A 29  ? 0.3900 0.4680 0.4147 -0.0559 0.1295  -0.0041 29  LYS   A CD  
808  C  CD  B LYS   A 29  ? 0.3846 0.4187 0.4349 -0.0323 0.0531  0.0022  29  LYS   A CD  
809  C  CE  A LYS   A 29  ? 0.4006 0.4769 0.4670 -0.0515 0.1263  -0.0007 29  LYS   A CE  
810  C  CE  B LYS   A 29  ? 0.3921 0.4246 0.4686 -0.0288 0.0523  0.0035  29  LYS   A CE  
811  N  NZ  A LYS   A 29  ? 0.4050 0.4821 0.4941 -0.0490 0.1222  0.0018  29  LYS   A NZ  
812  N  NZ  B LYS   A 29  ? 0.3959 0.4277 0.4866 -0.0269 0.0510  0.0051  29  LYS   A NZ  
839  N  N   . VAL   A 30  ? 0.3469 0.3843 0.1919 -0.0905 0.0883  0.0114  30  VAL   A N   
840  C  CA  . VAL   A 30  ? 0.3387 0.3685 0.1614 -0.1099 0.0600  0.0337  30  VAL   A CA  
841  C  C   . VAL   A 30  ? 0.3381 0.3563 0.1375 -0.1116 0.0316  0.0383  30  VAL   A C   
842  O  O   . VAL   A 30  ? 0.3521 0.3615 0.1501 -0.1117 0.0237  0.0411  30  VAL   A O   
843  C  CB  . VAL   A 30  ? 0.3342 0.3591 0.2146 -0.1316 0.0295  0.0338  30  VAL   A CB  
844  C  CG1 . VAL   A 30  ? 0.3405 0.3615 0.2446 -0.1304 0.0163  0.0303  30  VAL   A CG1 
845  C  CG2 . VAL   A 30  ? 0.3249 0.3493 0.2496 -0.1386 0.0289  0.0373  30  VAL   A CG2 
856  N  N   . LYS   A 31  ? 0.3300 0.3408 0.1248 -0.1178 0.0043  0.0294  31  LYS   A N   
857  C  CA  . LYS   A 31  ? 0.3391 0.3376 0.1379 -0.1080 -0.0191 0.0289  31  LYS   A CA  
858  C  C   . LYS   A 31  ? 0.3121 0.3063 0.1210 -0.0852 -0.0183 0.0611  31  LYS   A C   
859  O  O   . LYS   A 31  ? 0.3213 0.3246 0.1517 -0.0783 -0.0316 0.0780  31  LYS   A O   
860  C  CB  . LYS   A 31  ? 0.3742 0.3660 0.2425 -0.1109 -0.0367 -0.0006 31  LYS   A CB  
861  C  CG  . LYS   A 31  ? 0.4201 0.4084 0.3841 -0.0944 -0.0525 -0.0191 31  LYS   A CG  
862  C  CD  . LYS   A 31  ? 0.4725 0.4392 0.5002 -0.0836 -0.0703 -0.0348 31  LYS   A CD  
863  C  CE  . LYS   A 31  ? 0.4948 0.4530 0.5758 -0.0766 -0.0801 -0.0439 31  LYS   A CE  
864  N  NZ  . LYS   A 31  ? 0.5176 0.4960 0.6107 -0.0745 -0.0826 -0.0480 31  LYS   A NZ  
878  N  N   . PRO   A 32  ? 0.2720 0.2717 0.1037 -0.0838 -0.0054 0.0444  32  PRO   A N   
879  C  CA  . PRO   A 32  ? 0.2645 0.2570 0.1580 -0.0766 -0.0204 0.0637  32  PRO   A CA  
880  C  C   . PRO   A 32  ? 0.2627 0.2540 0.1608 -0.0664 -0.0332 0.0650  32  PRO   A C   
881  O  O   . PRO   A 32  ? 0.2555 0.2493 0.1621 -0.0605 -0.0498 0.0540  32  PRO   A O   
882  C  CB  . PRO   A 32  ? 0.2541 0.2622 0.1565 -0.0703 -0.0242 0.0481  32  PRO   A CB  
883  C  CG  . PRO   A 32  ? 0.2455 0.2637 0.1014 -0.0641 -0.0363 0.0334  32  PRO   A CG  
884  C  CD  . PRO   A 32  ? 0.2559 0.2709 0.1000 -0.0717 -0.0183 0.0345  32  PRO   A CD  
892  N  N   . THR   A 33  ? 0.2692 0.2559 0.1443 -0.0589 -0.0271 0.0618  33  THR   A N   
893  C  CA  . THR   A 33  ? 0.2656 0.2544 0.1551 -0.0444 -0.0454 0.0624  33  THR   A CA  
894  C  C   . THR   A 33  ? 0.2376 0.2359 0.1498 -0.0460 -0.0473 0.0531  33  THR   A C   
895  O  O   . THR   A 33  ? 0.2307 0.2286 0.1665 -0.0515 -0.0556 0.0580  33  THR   A O   
896  C  CB  . THR   A 33  ? 0.2898 0.2773 0.1732 -0.0329 -0.0480 0.0801  33  THR   A CB  
897  O  OG1 . THR   A 33  ? 0.3188 0.2933 0.2047 -0.0140 -0.0390 0.0953  33  THR   A OG1 
898  C  CG2 . THR   A 33  ? 0.2909 0.2913 0.1976 -0.0239 -0.0649 0.0797  33  THR   A CG2 
906  N  N   . VAL   A 34  ? 0.2125 0.2155 0.1338 -0.0475 -0.0352 0.0471  34  VAL   A N   
907  C  CA  . VAL   A 34  ? 0.1913 0.1957 0.1244 -0.0418 -0.0269 0.0443  34  VAL   A CA  
908  C  C   . VAL   A 34  ? 0.1793 0.1880 0.1083 -0.0323 -0.0090 0.0357  34  VAL   A C   
909  O  O   . VAL   A 34  ? 0.1758 0.1857 0.1369 -0.0386 -0.0025 0.0329  34  VAL   A O   
910  C  CB  . VAL   A 34  ? 0.1928 0.1990 0.1518 -0.0371 -0.0201 0.0329  34  VAL   A CB  
911  C  CG1 . VAL   A 34  ? 0.1954 0.1940 0.1575 -0.0357 -0.0020 0.0207  34  VAL   A CG1 
912  C  CG2 . VAL   A 34  ? 0.2039 0.2194 0.1661 -0.0326 -0.0228 0.0370  34  VAL   A CG2 
922  N  N   . VAL   A 35  ? 0.1625 0.1778 0.1061 -0.0307 -0.0091 0.0225  35  VAL   A N   
923  C  CA  . VAL   A 35  ? 0.1533 0.1714 0.1026 -0.0256 -0.0036 0.0230  35  VAL   A CA  
924  C  C   . VAL   A 35  ? 0.1538 0.1594 0.1145 -0.0206 0.0007  0.0239  35  VAL   A C   
925  O  O   . VAL   A 35  ? 0.1414 0.1704 0.1269 -0.0298 0.0136  0.0153  35  VAL   A O   
926  C  CB  . VAL   A 35  ? 0.1582 0.1734 0.1381 -0.0133 0.0072  0.0165  35  VAL   A CB  
927  C  CG1 . VAL   A 35  ? 0.1670 0.1802 0.1437 -0.0132 -0.0058 0.0062  35  VAL   A CG1 
928  C  CG2 . VAL   A 35  ? 0.1553 0.1778 0.1694 -0.0072 0.0091  0.0122  35  VAL   A CG2 
938  N  N   . VAL   A 36  ? 0.1362 0.1507 0.1035 -0.0158 -0.0034 0.0207  36  VAL   A N   
939  C  CA  . VAL   A 36  ? 0.1322 0.1417 0.1025 -0.0129 -0.0049 0.0108  36  VAL   A CA  
940  C  C   . VAL   A 36  ? 0.1268 0.1507 0.1100 -0.0181 0.0004  0.0181  36  VAL   A C   
941  O  O   . VAL   A 36  ? 0.1337 0.1494 0.1328 -0.0091 0.0141  0.0142  36  VAL   A O   
942  C  CB  . VAL   A 36  ? 0.1351 0.1380 0.1187 -0.0076 -0.0084 0.0127  36  VAL   A CB  
943  C  CG1 . VAL   A 36  ? 0.1389 0.1392 0.1355 -0.0150 -0.0011 0.0047  36  VAL   A CG1 
944  C  CG2 . VAL   A 36  ? 0.1374 0.1501 0.1368 -0.0056 -0.0017 0.0263  36  VAL   A CG2 
954  N  N   . ASN   A 37  ? 0.1220 0.1423 0.1087 -0.0068 0.0032  0.0196  37  ASN   A N   
955  C  CA  . ASN   A 37  ? 0.1284 0.1344 0.0997 -0.0054 0.0111  0.0198  37  ASN   A CA  
956  C  C   . ASN   A 37  ? 0.1332 0.1280 0.1072 -0.0082 0.0085  0.0278  37  ASN   A C   
957  O  O   . ASN   A 37  ? 0.1434 0.1412 0.1184 0.0030  0.0100  0.0091  37  ASN   A O   
958  C  CB  . ASN   A 37  ? 0.1246 0.1373 0.1180 0.0039  0.0043  0.0167  37  ASN   A CB  
959  C  CG  . ASN   A 37  ? 0.1277 0.1350 0.1280 -0.0007 0.0011  0.0069  37  ASN   A CG  
960  O  OD1 . ASN   A 37  ? 0.1328 0.1381 0.1393 -0.0013 0.0013  0.0169  37  ASN   A OD1 
961  N  ND2 . ASN   A 37  ? 0.1328 0.1353 0.1364 -0.0050 -0.0017 0.0195  37  ASN   A ND2 
968  N  N   A ALA   A 38  ? 0.1268 0.1440 0.1042 -0.0027 0.0088  0.0150  38  ALA   A N   
969  N  N   B ALA   A 38  ? 0.1347 0.1366 0.1196 -0.0097 0.0042  0.0191  38  ALA   A N   
970  C  CA  A ALA   A 38  ? 0.1294 0.1451 0.1140 -0.0042 0.0050  0.0111  38  ALA   A CA  
971  C  CA  B ALA   A 38  ? 0.1410 0.1386 0.1260 -0.0150 0.0003  0.0113  38  ALA   A CA  
972  C  C   A ALA   A 38  ? 0.1279 0.1504 0.1056 0.0027  -0.0028 -0.0032 38  ALA   A C   
973  C  C   B ALA   A 38  ? 0.1357 0.1414 0.1246 -0.0107 -0.0110 0.0075  38  ALA   A C   
974  O  O   A ALA   A 38  ? 0.1237 0.1355 0.1192 0.0038  -0.0026 -0.0097 38  ALA   A O   
975  O  O   B ALA   A 38  ? 0.1288 0.1358 0.1368 -0.0119 -0.0244 0.0200  38  ALA   A O   
976  C  CB  A ALA   A 38  ? 0.1261 0.1622 0.1411 -0.0105 0.0012  0.0043  38  ALA   A CB  
977  C  CB  B ALA   A 38  ? 0.1518 0.1415 0.1462 -0.0166 -0.0051 0.0017  38  ALA   A CB  
988  N  N   A ALA   A 39  ? 0.1273 0.1477 0.1135 0.0066  0.0047  0.0097  39  ALA   A N   
989  N  N   B ALA   A 39  ? 0.1369 0.1472 0.1282 -0.0104 -0.0038 0.0200  39  ALA   A N   
990  C  CA  A ALA   A 39  ? 0.1278 0.1386 0.1142 0.0067  0.0101  0.0137  39  ALA   A CA  
991  C  CA  B ALA   A 39  ? 0.1413 0.1495 0.1233 -0.0125 -0.0002 0.0222  39  ALA   A CA  
992  C  C   A ALA   A 39  ? 0.1294 0.1434 0.1159 0.0020  0.0099  0.0054  39  ALA   A C   
993  C  C   B ALA   A 39  ? 0.1362 0.1439 0.1191 -0.0078 0.0001  0.0131  39  ALA   A C   
994  O  O   A ALA   A 39  ? 0.1470 0.1408 0.1325 -0.0008 0.0071  0.0055  39  ALA   A O   
995  O  O   B ALA   A 39  ? 0.1433 0.1381 0.1157 -0.0169 -0.0018 -0.0004 39  ALA   A O   
996  C  CB  A ALA   A 39  ? 0.1269 0.1386 0.1258 0.0071  0.0004  0.0005  39  ALA   A CB  
997  C  CB  B ALA   A 39  ? 0.1548 0.1583 0.1344 -0.0140 -0.0030 0.0110  39  ALA   A CB  
1008 N  N   A ASN   A 40  ? 0.1324 0.1419 0.1190 -0.0095 0.0157  0.0073  40  ASN   A N   
1009 N  N   B ASN   A 40  ? 0.1332 0.1416 0.1243 0.0008  0.0188  0.0182  40  ASN   A N   
1010 C  CA  A ASN   A 40  ? 0.1371 0.1363 0.1280 -0.0043 0.0011  0.0025  40  ASN   A CA  
1011 C  CA  B ASN   A 40  ? 0.1316 0.1361 0.1299 0.0061  0.0113  0.0242  40  ASN   A CA  
1012 C  C   A ASN   A 40  ? 0.1364 0.1272 0.1044 -0.0036 0.0143  0.0153  40  ASN   A C   
1013 C  C   B ASN   A 40  ? 0.1316 0.1340 0.1271 0.0017  0.0096  0.0261  40  ASN   A C   
1014 O  O   A ASN   A 40  ? 0.1355 0.1291 0.1147 -0.0110 0.0151  0.0094  40  ASN   A O   
1015 O  O   B ASN   A 40  ? 0.1289 0.1358 0.1313 -0.0051 0.0032  0.0245  40  ASN   A O   
1016 C  CB  A ASN   A 40  ? 0.1511 0.1345 0.1605 0.0019  -0.0047 0.0053  40  ASN   A CB  
1017 C  CB  B ASN   A 40  ? 0.1420 0.1370 0.1385 -0.0001 0.0033  0.0133  40  ASN   A CB  
1018 C  CG  A ASN   A 40  ? 0.1655 0.1334 0.1887 0.0067  -0.0014 0.0218  40  ASN   A CG  
1019 C  CG  B ASN   A 40  ? 0.1507 0.1418 0.1533 -0.0108 0.0060  0.0022  40  ASN   A CG  
1020 O  OD1 A ASN   A 40  ? 0.1768 0.1425 0.1901 0.0046  -0.0089 0.0179  40  ASN   A OD1 
1021 O  OD1 B ASN   A 40  ? 0.1623 0.1457 0.1468 -0.0126 0.0153  -0.0120 40  ASN   A OD1 
1022 N  ND2 A ASN   A 40  ? 0.1803 0.1498 0.1918 0.0086  0.0112  0.0040  40  ASN   A ND2 
1023 N  ND2 B ASN   A 40  ? 0.1436 0.1506 0.1668 -0.0204 0.0183  -0.0092 40  ASN   A ND2 
1036 N  N   A VAL   A 41  ? 0.1401 0.1376 0.1069 -0.0070 0.0087  0.0204  41  VAL   A N   
1037 N  N   B VAL   A 41  ? 0.1354 0.1347 0.1321 -0.0006 -0.0013 0.0203  41  VAL   A N   
1038 C  CA  A VAL   A 41  ? 0.1375 0.1401 0.1276 0.0004  0.0166  0.0136  41  VAL   A CA  
1039 C  CA  B VAL   A 41  ? 0.1388 0.1393 0.1374 -0.0031 -0.0013 0.0240  41  VAL   A CA  
1040 C  C   A VAL   A 41  ? 0.1376 0.1408 0.1273 0.0059  0.0210  0.0126  41  VAL   A C   
1041 C  C   B VAL   A 41  ? 0.1414 0.1399 0.1530 -0.0063 0.0073  0.0306  41  VAL   A C   
1042 O  O   A VAL   A 41  ? 0.1386 0.1353 0.1525 0.0008  0.0174  -0.0038 41  VAL   A O   
1043 O  O   B VAL   A 41  ? 0.1502 0.1337 0.1765 -0.0110 -0.0016 0.0277  41  VAL   A O   
1044 C  CB  A VAL   A 41  ? 0.1458 0.1447 0.1159 -0.0049 0.0162  0.0112  41  VAL   A CB  
1045 C  CB  B VAL   A 41  ? 0.1422 0.1423 0.1505 0.0033  0.0168  0.0274  41  VAL   A CB  
1046 C  CG1 A VAL   A 41  ? 0.1555 0.1491 0.1407 0.0028  0.0006  0.0080  41  VAL   A CG1 
1047 C  CG1 B VAL   A 41  ? 0.1561 0.1488 0.1593 0.0009  0.0356  0.0117  41  VAL   A CG1 
1048 C  CG2 A VAL   A 41  ? 0.1533 0.1517 0.1227 -0.0098 0.0331  0.0004  41  VAL   A CG2 
1049 C  CG2 B VAL   A 41  ? 0.1447 0.1477 0.1617 0.0081  0.0063  0.0313  41  VAL   A CG2 
1068 N  N   A TYR   A 42  ? 0.1321 0.1312 0.1463 -0.0017 0.0216  0.0196  42  TYR   A N   
1069 N  N   B TYR   A 42  ? 0.1350 0.1478 0.1625 0.0006  0.0184  0.0427  42  TYR   A N   
1070 C  CA  A TYR   A 42  ? 0.1394 0.1247 0.1472 -0.0079 0.0281  0.0175  42  TYR   A CA  
1071 C  CA  B TYR   A 42  ? 0.1438 0.1549 0.1577 -0.0013 0.0239  0.0369  42  TYR   A CA  
1072 C  C   A TYR   A 42  ? 0.1276 0.1258 0.1617 -0.0053 0.0167  0.0186  42  TYR   A C   
1073 C  C   B TYR   A 42  ? 0.1413 0.1538 0.1463 -0.0008 0.0115  0.0428  42  TYR   A C   
1074 O  O   A TYR   A 42  ? 0.1325 0.1283 0.1861 -0.0237 0.0135  -0.0083 42  TYR   A O   
1075 O  O   B TYR   A 42  ? 0.1415 0.1598 0.1574 -0.0021 0.0096  0.0383  42  TYR   A O   
1076 C  CB  A TYR   A 42  ? 0.1649 0.1384 0.1496 0.0001  0.0372  0.0256  42  TYR   A CB  
1077 C  CB  B TYR   A 42  ? 0.1567 0.1672 0.1651 -0.0033 0.0268  0.0289  42  TYR   A CB  
1078 C  CG  A TYR   A 42  ? 0.1905 0.1440 0.1476 0.0038  0.0358  0.0452  42  TYR   A CG  
1079 C  CG  B TYR   A 42  ? 0.1713 0.1774 0.1665 -0.0070 0.0287  0.0274  42  TYR   A CG  
1080 C  CD1 A TYR   A 42  ? 0.2041 0.1582 0.1517 -0.0107 0.0411  0.0335  42  TYR   A CD1 
1081 C  CD1 B TYR   A 42  ? 0.1818 0.1857 0.1692 -0.0104 0.0297  0.0173  42  TYR   A CD1 
1082 C  CD2 A TYR   A 42  ? 0.2122 0.1637 0.1716 0.0023  0.0286  0.0365  42  TYR   A CD2 
1083 C  CD2 B TYR   A 42  ? 0.1809 0.1882 0.1728 -0.0120 0.0259  0.0212  42  TYR   A CD2 
1084 C  CE1 A TYR   A 42  ? 0.2124 0.1675 0.1610 -0.0219 0.0485  0.0275  42  TYR   A CE1 
1085 C  CE1 B TYR   A 42  ? 0.1883 0.1919 0.1772 -0.0147 0.0327  0.0100  42  TYR   A CE1 
1086 C  CE2 A TYR   A 42  ? 0.2284 0.1786 0.1786 -0.0133 0.0312  0.0451  42  TYR   A CE2 
1087 C  CE2 B TYR   A 42  ? 0.1896 0.1977 0.1841 -0.0199 0.0267  0.0194  42  TYR   A CE2 
1088 C  CZ  A TYR   A 42  ? 0.2344 0.1846 0.1648 -0.0242 0.0451  0.0274  42  TYR   A CZ  
1089 C  CZ  B TYR   A 42  ? 0.1972 0.2017 0.1817 -0.0207 0.0329  0.0104  42  TYR   A CZ  
1090 O  OH  A TYR   A 42  ? 0.2510 0.2017 0.1920 -0.0411 0.0436  0.0122  42  TYR   A OH  
1091 O  OH  B TYR   A 42  ? 0.2104 0.2142 0.1998 -0.0269 0.0262  0.0050  42  TYR   A OH  
1110 N  N   A LEU   A 43  ? 0.1310 0.1295 0.1393 -0.0097 0.0128  0.0024  43  LEU   A N   
1111 N  N   B LEU   A 43  ? 0.1371 0.1469 0.1345 -0.0030 0.0005  0.0356  43  LEU   A N   
1112 C  CA  A LEU   A 43  ? 0.1286 0.1271 0.1392 -0.0105 0.0138  0.0026  43  LEU   A CA  
1113 C  CA  B LEU   A 43  ? 0.1406 0.1426 0.1321 -0.0030 -0.0013 0.0377  43  LEU   A CA  
1114 C  C   A LEU   A 43  ? 0.1293 0.1324 0.1399 0.0012  0.0049  0.0014  43  LEU   A C   
1115 C  C   B LEU   A 43  ? 0.1407 0.1439 0.1361 -0.0129 -0.0002 0.0308  43  LEU   A C   
1116 O  O   A LEU   A 43  ? 0.1443 0.1384 0.1692 0.0051  -0.0140 -0.0074 43  LEU   A O   
1117 O  O   B LEU   A 43  ? 0.1375 0.1386 0.1369 -0.0228 -0.0014 0.0251  43  LEU   A O   
1118 C  CB  A LEU   A 43  ? 0.1345 0.1326 0.1480 -0.0088 0.0132  -0.0013 43  LEU   A CB  
1119 C  CB  B LEU   A 43  ? 0.1420 0.1391 0.1338 0.0020  -0.0019 0.0369  43  LEU   A CB  
1120 C  CG  A LEU   A 43  ? 0.1428 0.1358 0.1442 -0.0070 0.0036  0.0019  43  LEU   A CG  
1121 C  CG  B LEU   A 43  ? 0.1419 0.1373 0.1328 0.0064  -0.0090 0.0275  43  LEU   A CG  
1122 C  CD1 A LEU   A 43  ? 0.1523 0.1452 0.1644 -0.0063 0.0005  -0.0007 43  LEU   A CD1 
1123 C  CD1 B LEU   A 43  ? 0.1458 0.1442 0.1268 0.0042  -0.0125 0.0376  43  LEU   A CD1 
1124 C  CD2 A LEU   A 43  ? 0.1570 0.1386 0.1506 -0.0148 0.0067  0.0183  43  LEU   A CD2 
1125 C  CD2 B LEU   A 43  ? 0.1525 0.1333 0.1411 0.0059  -0.0013 0.0306  43  LEU   A CD2 
1148 N  N   A LYS   A 44  ? 0.1383 0.1320 0.1246 0.0088  0.0118  0.0059  44  LYS   A N   
1149 N  N   B LYS   A 44  ? 0.1486 0.1487 0.1454 -0.0060 -0.0007 0.0259  44  LYS   A N   
1150 C  CA  A LYS   A 44  ? 0.1489 0.1360 0.1331 0.0022  0.0229  0.0185  44  LYS   A CA  
1151 C  CA  B LYS   A 44  ? 0.1577 0.1536 0.1539 -0.0058 0.0032  0.0227  44  LYS   A CA  
1152 C  C   A LYS   A 44  ? 0.1334 0.1383 0.1280 0.0015  0.0094  0.0092  44  LYS   A C   
1153 C  C   B LYS   A 44  ? 0.1427 0.1429 0.1386 -0.0014 0.0047  0.0167  44  LYS   A C   
1154 O  O   A LYS   A 44  ? 0.1446 0.1509 0.1506 -0.0003 0.0026  -0.0087 44  LYS   A O   
1155 O  O   B LYS   A 44  ? 0.1479 0.1429 0.1413 -0.0004 0.0016  0.0096  44  LYS   A O   
1156 C  CB  A LYS   A 44  ? 0.1841 0.1470 0.1797 0.0005  0.0413  0.0332  44  LYS   A CB  
1157 C  CB  B LYS   A 44  ? 0.1828 0.1758 0.2046 -0.0043 0.0121  0.0205  44  LYS   A CB  
1158 C  CG  A LYS   A 44  ? 0.2200 0.1695 0.2345 -0.0080 0.0584  0.0378  44  LYS   A CG  
1159 C  CG  B LYS   A 44  ? 0.2048 0.1982 0.2607 -0.0023 0.0207  0.0230  44  LYS   A CG  
1160 C  CD  A LYS   A 44  ? 0.2573 0.2212 0.3382 -0.0167 0.0366  0.0262  44  LYS   A CD  
1161 C  CD  B LYS   A 44  ? 0.2244 0.2274 0.3175 -0.0090 0.0152  0.0182  44  LYS   A CD  
1162 C  CE  A LYS   A 44  ? 0.2782 0.2605 0.3992 -0.0257 0.0228  0.0238  44  LYS   A CE  
1163 C  CE  B LYS   A 44  ? 0.2342 0.2499 0.3542 -0.0174 0.0081  0.0201  44  LYS   A CE  
1164 N  NZ  A LYS   A 44  ? 0.2874 0.2868 0.4264 -0.0322 0.0262  0.0293  44  LYS   A NZ  
1165 N  NZ  B LYS   A 44  ? 0.2414 0.2644 0.3755 -0.0272 0.0091  0.0182  44  LYS   A NZ  
1192 N  N   . HIS   A 45  ? 0.1314 0.1383 0.1315 -0.0027 0.0037  0.0162  45  HIS   A N   
1193 C  CA  . HIS   A 45  ? 0.1328 0.1295 0.1351 -0.0005 0.0007  0.0062  45  HIS   A CA  
1194 C  C   . HIS   A 45  ? 0.1398 0.1425 0.1506 0.0083  0.0100  0.0127  45  HIS   A C   
1195 O  O   . HIS   A 45  ? 0.1630 0.1595 0.1884 0.0220  -0.0009 -0.0024 45  HIS   A O   
1196 C  CB  . HIS   A 45  ? 0.1371 0.1288 0.1329 -0.0015 0.0005  0.0076  45  HIS   A CB  
1197 C  CG  . HIS   A 45  ? 0.1339 0.1312 0.1192 -0.0049 0.0055  0.0039  45  HIS   A CG  
1198 N  ND1 . HIS   A 45  ? 0.1299 0.1436 0.1336 -0.0038 -0.0016 0.0105  45  HIS   A ND1 
1199 C  CD2 . HIS   A 45  ? 0.1347 0.1346 0.1428 -0.0165 -0.0052 0.0150  45  HIS   A CD2 
1200 C  CE1 . HIS   A 45  ? 0.1253 0.1431 0.1279 -0.0008 -0.0019 0.0180  45  HIS   A CE1 
1201 N  NE2 . HIS   A 45  ? 0.1320 0.1453 0.1358 -0.0073 0.0012  0.0166  45  HIS   A NE2 
1210 N  N   A GLY   A 46  ? 0.1571 0.1497 0.1783 0.0084  -0.0127 0.0165  46  GLY   A N   
1211 N  N   B GLY   A 46  ? 0.1476 0.1412 0.1627 0.0169  -0.0048 0.0188  46  GLY   A N   
1212 C  CA  A GLY   A 46  ? 0.1649 0.1613 0.1906 0.0084  -0.0207 0.0187  46  GLY   A CA  
1213 C  CA  B GLY   A 46  ? 0.1543 0.1419 0.1652 0.0198  -0.0147 0.0195  46  GLY   A CA  
1214 C  C   A GLY   A 46  ? 0.1717 0.1566 0.1954 0.0148  -0.0327 0.0196  46  GLY   A C   
1215 C  C   B GLY   A 46  ? 0.1605 0.1339 0.1599 0.0256  -0.0266 0.0220  46  GLY   A C   
1216 O  O   A GLY   A 46  ? 0.1740 0.1624 0.2368 0.0065  -0.0392 0.0002  46  GLY   A O   
1217 O  O   B GLY   A 46  ? 0.1660 0.1345 0.1873 0.0258  -0.0378 0.0235  46  GLY   A O   
1224 N  N   A GLY   A 47  ? 0.1696 0.1595 0.1698 0.0201  -0.0290 0.0081  47  GLY   A N   
1225 N  N   B GLY   A 47  ? 0.1556 0.1344 0.1449 0.0265  -0.0192 0.0090  47  GLY   A N   
1226 C  CA  A GLY   A 47  ? 0.1714 0.1635 0.1623 0.0192  -0.0466 -0.0013 47  GLY   A CA  
1227 C  CA  B GLY   A 47  ? 0.1582 0.1426 0.1425 0.0202  -0.0316 -0.0003 47  GLY   A CA  
1228 C  C   A GLY   A 47  ? 0.1664 0.1496 0.1672 0.0134  -0.0485 -0.0068 47  GLY   A C   
1229 C  C   B GLY   A 47  ? 0.1588 0.1439 0.1333 0.0243  -0.0278 -0.0096 47  GLY   A C   
1230 O  O   A GLY   A 47  ? 0.1632 0.1389 0.1798 0.0138  -0.0481 0.0056  47  GLY   A O   
1231 O  O   B GLY   A 47  ? 0.1625 0.1432 0.1343 0.0317  -0.0221 0.0021  47  GLY   A O   
1238 N  N   A GLY   A 48  ? 0.1593 0.1503 0.1693 0.0144  -0.0520 -0.0081 48  GLY   A N   
1239 N  N   B GLY   A 48  ? 0.1562 0.1484 0.1546 0.0148  -0.0294 -0.0128 48  GLY   A N   
1240 C  CA  A GLY   A 48  ? 0.1542 0.1432 0.1916 0.0049  -0.0395 -0.0139 48  GLY   A CA  
1241 C  CA  B GLY   A 48  ? 0.1491 0.1424 0.1538 0.0195  -0.0210 -0.0048 48  GLY   A CA  
1242 C  C   A GLY   A 48  ? 0.1450 0.1460 0.1671 0.0052  -0.0079 -0.0013 48  GLY   A C   
1243 C  C   B GLY   A 48  ? 0.1434 0.1430 0.1530 0.0153  -0.0071 0.0042  48  GLY   A C   
1244 O  O   A GLY   A 48  ? 0.1558 0.1439 0.1541 0.0119  -0.0114 -0.0039 48  GLY   A O   
1245 O  O   B GLY   A 48  ? 0.1549 0.1486 0.1496 0.0095  -0.0057 -0.0037 48  GLY   A O   
1252 N  N   A VAL   A 49  ? 0.1308 0.1357 0.1913 -0.0023 -0.0083 -0.0048 49  VAL   A N   
1253 N  N   B VAL   A 49  ? 0.1281 0.1350 0.1557 0.0062  -0.0033 0.0083  49  VAL   A N   
1254 C  CA  A VAL   A 49  ? 0.1408 0.1328 0.1736 -0.0047 0.0101  -0.0039 49  VAL   A CA  
1255 C  CA  B VAL   A 49  ? 0.1147 0.1388 0.1374 0.0007  0.0062  0.0131  49  VAL   A CA  
1256 C  C   A VAL   A 49  ? 0.1409 0.1238 0.1407 -0.0008 0.0174  0.0009  49  VAL   A C   
1257 C  C   B VAL   A 49  ? 0.1160 0.1307 0.1175 0.0048  0.0130  0.0122  49  VAL   A C   
1258 O  O   A VAL   A 49  ? 0.1429 0.1337 0.1476 -0.0015 0.0184  -0.0041 49  VAL   A O   
1259 O  O   B VAL   A 49  ? 0.1191 0.1270 0.1032 0.0134  0.0115  0.0164  49  VAL   A O   
1260 C  CB  A VAL   A 49  ? 0.1530 0.1393 0.1796 -0.0043 0.0175  -0.0130 49  VAL   A CB  
1261 C  CB  B VAL   A 49  ? 0.1052 0.1364 0.1328 0.0010  0.0016  0.0086  49  VAL   A CB  
1262 C  CG1 A VAL   A 49  ? 0.1569 0.1373 0.1989 0.0067  0.0249  -0.0076 49  VAL   A CG1 
1263 C  CG1 B VAL   A 49  ? 0.1023 0.1310 0.1329 0.0126  0.0135  0.0156  49  VAL   A CG1 
1264 C  CG2 A VAL   A 49  ? 0.1712 0.1543 0.2374 -0.0201 0.0206  -0.0102 49  VAL   A CG2 
1265 C  CG2 B VAL   A 49  ? 0.1000 0.1380 0.1183 0.0026  0.0107  0.0020  49  VAL   A CG2 
1284 N  N   A ALA   A 50  ? 0.1316 0.1220 0.1316 -0.0068 -0.0074 0.0071  50  ALA   A N   
1285 N  N   B ALA   A 50  ? 0.1233 0.1341 0.1137 0.0023  0.0078  0.0017  50  ALA   A N   
1286 C  CA  A ALA   A 50  ? 0.1293 0.1228 0.1277 -0.0149 -0.0002 0.0199  50  ALA   A CA  
1287 C  CA  B ALA   A 50  ? 0.1291 0.1370 0.1130 -0.0058 0.0040  0.0025  50  ALA   A CA  
1288 C  C   A ALA   A 50  ? 0.1310 0.1299 0.1265 -0.0057 -0.0024 0.0053  50  ALA   A C   
1289 C  C   B ALA   A 50  ? 0.1313 0.1367 0.1060 -0.0051 0.0037  -0.0071 50  ALA   A C   
1290 O  O   A ALA   A 50  ? 0.1311 0.1284 0.1437 -0.0018 -0.0034 0.0037  50  ALA   A O   
1291 O  O   B ALA   A 50  ? 0.1328 0.1347 0.1073 -0.0017 0.0070  -0.0096 50  ALA   A O   
1292 C  CB  A ALA   A 50  ? 0.1242 0.1285 0.1271 -0.0091 0.0002  0.0091  50  ALA   A CB  
1293 C  CB  B ALA   A 50  ? 0.1282 0.1395 0.1153 -0.0108 0.0088  -0.0071 50  ALA   A CB  
1304 N  N   A GLY   A 51  ? 0.1363 0.1216 0.1422 0.0049  -0.0048 0.0081  51  GLY   A N   
1305 N  N   B GLY   A 51  ? 0.1343 0.1357 0.1195 -0.0038 0.0012  -0.0129 51  GLY   A N   
1306 C  CA  A GLY   A 51  ? 0.1475 0.1266 0.1418 0.0103  -0.0151 0.0126  51  GLY   A CA  
1307 C  CA  B GLY   A 51  ? 0.1401 0.1378 0.1263 -0.0022 -0.0058 -0.0143 51  GLY   A CA  
1308 C  C   A GLY   A 51  ? 0.1305 0.1396 0.1373 0.0117  -0.0038 -0.0095 51  GLY   A C   
1309 C  C   B GLY   A 51  ? 0.1340 0.1444 0.1326 0.0010  -0.0012 -0.0156 51  GLY   A C   
1310 O  O   A GLY   A 51  ? 0.1362 0.1467 0.1539 0.0047  -0.0078 -0.0108 51  GLY   A O   
1311 O  O   B GLY   A 51  ? 0.1394 0.1457 0.1379 -0.0011 -0.0032 -0.0154 51  GLY   A O   
1318 N  N   . ALA   A 52  ? 0.1329 0.1490 0.1342 -0.0022 0.0005  -0.0114 52  ALA   A N   
1319 C  CA  . ALA   A 52  ? 0.1321 0.1600 0.1494 -0.0026 0.0036  -0.0087 52  ALA   A CA  
1320 C  C   . ALA   A 52  ? 0.1282 0.1594 0.1239 -0.0038 0.0129  -0.0036 52  ALA   A C   
1321 O  O   . ALA   A 52  ? 0.1422 0.1647 0.1446 -0.0023 0.0114  -0.0121 52  ALA   A O   
1322 C  CB  . ALA   A 52  ? 0.1366 0.1842 0.1705 -0.0112 -0.0032 -0.0019 52  ALA   A CB  
1329 N  N   A LEU   A 53  ? 0.1313 0.1488 0.1382 -0.0024 0.0045  -0.0034 53  LEU   A N   
1330 N  N   B LEU   A 53  ? 0.1295 0.1536 0.1354 -0.0037 0.0098  -0.0060 53  LEU   A N   
1331 C  CA  A LEU   A 53  ? 0.1448 0.1518 0.1188 -0.0049 0.0003  0.0019  53  LEU   A CA  
1332 C  CA  B LEU   A 53  ? 0.1365 0.1549 0.1310 -0.0057 0.0065  -0.0044 53  LEU   A CA  
1333 C  C   A LEU   A 53  ? 0.1435 0.1503 0.0926 0.0050  0.0061  0.0017  53  LEU   A C   
1334 C  C   B LEU   A 53  ? 0.1384 0.1534 0.1274 -0.0074 0.0107  -0.0107 53  LEU   A C   
1335 O  O   A LEU   A 53  ? 0.1611 0.1608 0.1106 -0.0045 0.0014  0.0072  53  LEU   A O   
1336 O  O   B LEU   A 53  ? 0.1426 0.1520 0.1401 -0.0220 0.0155  -0.0088 53  LEU   A O   
1337 C  CB  A LEU   A 53  ? 0.1523 0.1531 0.1207 -0.0152 -0.0011 0.0053  53  LEU   A CB  
1338 C  CB  B LEU   A 53  ? 0.1376 0.1532 0.1302 -0.0040 0.0038  -0.0010 53  LEU   A CB  
1339 C  CG  A LEU   A 53  ? 0.1718 0.1564 0.1485 -0.0184 0.0054  0.0162  53  LEU   A CG  
1340 C  CG  B LEU   A 53  ? 0.1435 0.1495 0.1294 -0.0021 -0.0008 0.0015  53  LEU   A CG  
1341 C  CD1 A LEU   A 53  ? 0.1809 0.1669 0.1496 -0.0058 0.0107  0.0174  53  LEU   A CD1 
1342 C  CD1 B LEU   A 53  ? 0.1516 0.1535 0.1346 -0.0014 -0.0014 0.0021  53  LEU   A CD1 
1343 C  CD2 A LEU   A 53  ? 0.1813 0.1710 0.1566 -0.0273 0.0041  0.0209  53  LEU   A CD2 
1344 C  CD2 B LEU   A 53  ? 0.1433 0.1534 0.1303 0.0007  0.0026  0.0001  53  LEU   A CD2 
1367 N  N   A ASN   A 54  ? 0.1316 0.1436 0.1095 -0.0035 0.0009  0.0058  54  ASN   A N   
1368 N  N   B ASN   A 54  ? 0.1360 0.1516 0.1316 -0.0054 0.0033  -0.0104 54  ASN   A N   
1369 C  CA  A ASN   A 54  ? 0.1195 0.1424 0.1280 -0.0062 -0.0031 0.0009  54  ASN   A CA  
1370 C  CA  B ASN   A 54  ? 0.1319 0.1510 0.1361 -0.0021 -0.0004 -0.0127 54  ASN   A CA  
1371 C  C   A ASN   A 54  ? 0.1341 0.1491 0.1311 -0.0069 0.0048  -0.0053 54  ASN   A C   
1372 C  C   B ASN   A 54  ? 0.1360 0.1507 0.1373 -0.0029 0.0017  -0.0097 54  ASN   A C   
1373 O  O   A ASN   A 54  ? 0.1402 0.1527 0.1276 -0.0128 -0.0072 -0.0121 54  ASN   A O   
1374 O  O   B ASN   A 54  ? 0.1370 0.1515 0.1367 -0.0038 -0.0045 -0.0133 54  ASN   A O   
1375 C  CB  A ASN   A 54  ? 0.1159 0.1386 0.1466 -0.0123 -0.0110 0.0056  54  ASN   A CB  
1376 C  CB  B ASN   A 54  ? 0.1326 0.1516 0.1433 0.0005  -0.0011 -0.0161 54  ASN   A CB  
1377 C  CG  A ASN   A 54  ? 0.1203 0.1482 0.1389 -0.0053 -0.0103 0.0085  54  ASN   A CG  
1378 C  CG  B ASN   A 54  ? 0.1350 0.1538 0.1376 0.0029  -0.0017 -0.0207 54  ASN   A CG  
1379 O  OD1 A ASN   A 54  ? 0.1231 0.1445 0.1407 -0.0079 -0.0082 0.0169  54  ASN   A OD1 
1380 O  OD1 B ASN   A 54  ? 0.1345 0.1524 0.1483 -0.0049 0.0045  -0.0252 54  ASN   A OD1 
1381 N  ND2 A ASN   A 54  ? 0.1226 0.1547 0.1541 -0.0131 -0.0083 0.0160  54  ASN   A ND2 
1382 N  ND2 B ASN   A 54  ? 0.1368 0.1549 0.1394 0.0044  -0.0065 -0.0146 54  ASN   A ND2 
1395 N  N   . LYS   A 55  ? 0.1370 0.1465 0.1401 -0.0034 0.0016  -0.0070 55  LYS   A N   
1396 C  CA  . LYS   A 55  ? 0.1438 0.1531 0.1486 0.0029  -0.0041 -0.0122 55  LYS   A CA  
1397 C  C   . LYS   A 55  ? 0.1465 0.1627 0.1420 -0.0028 0.0026  -0.0204 55  LYS   A C   
1398 O  O   . LYS   A 55  ? 0.1510 0.1787 0.1467 -0.0008 -0.0033 -0.0221 55  LYS   A O   
1399 C  CB  . LYS   A 55  ? 0.1508 0.1657 0.1668 0.0087  -0.0043 -0.0180 55  LYS   A CB  
1400 C  CG  . LYS   A 55  ? 0.1652 0.1955 0.1731 0.0229  -0.0133 -0.0216 55  LYS   A CG  
1401 C  CD  . LYS   A 55  ? 0.1809 0.2197 0.1944 0.0396  -0.0077 -0.0259 55  LYS   A CD  
1402 C  CE  . LYS   A 55  ? 0.2007 0.2510 0.2171 0.0471  -0.0116 -0.0299 55  LYS   A CE  
1403 N  NZ  . LYS   A 55  ? 0.2033 0.2753 0.2384 0.0611  -0.0102 -0.0251 55  LYS   A NZ  
1418 N  N   . ALA   A 56  ? 0.1498 0.1719 0.1452 -0.0138 0.0087  -0.0132 56  ALA   A N   
1419 C  CA  . ALA   A 56  ? 0.1602 0.1928 0.1475 -0.0185 0.0113  -0.0164 56  ALA   A CA  
1420 C  C   . ALA   A 56  ? 0.1632 0.2025 0.1296 -0.0193 0.0154  -0.0275 56  ALA   A C   
1421 O  O   . ALA   A 56  ? 0.1696 0.2339 0.1400 -0.0039 0.0197  -0.0263 56  ALA   A O   
1422 C  CB  . ALA   A 56  ? 0.1629 0.2110 0.1431 -0.0238 0.0112  -0.0049 56  ALA   A CB  
1428 N  N   . THR   A 57  ? 0.1481 0.1824 0.1346 -0.0160 0.0108  -0.0217 57  THR   A N   
1429 C  CA  . THR   A 57  ? 0.1508 0.1723 0.1362 -0.0166 -0.0001 -0.0131 57  THR   A CA  
1430 C  C   . THR   A 57  ? 0.1511 0.1805 0.1385 -0.0126 -0.0046 -0.0217 57  THR   A C   
1431 O  O   . THR   A 57  ? 0.1466 0.1894 0.1565 -0.0136 -0.0101 -0.0253 57  THR   A O   
1432 C  CB  . THR   A 57  ? 0.1475 0.1741 0.1425 -0.0097 -0.0028 -0.0141 57  THR   A CB  
1433 O  OG1 . THR   A 57  ? 0.1381 0.1734 0.1443 -0.0087 0.0013  -0.0079 57  THR   A OG1 
1434 C  CG2 . THR   A 57  ? 0.1553 0.1765 0.1277 -0.0049 0.0003  -0.0077 57  THR   A CG2 
1442 N  N   . ASN   A 58  ? 0.1540 0.1769 0.1588 -0.0075 0.0031  -0.0324 58  ASN   A N   
1443 C  CA  . ASN   A 58  ? 0.1697 0.1690 0.1866 -0.0167 0.0110  -0.0435 58  ASN   A CA  
1444 C  C   . ASN   A 58  ? 0.1497 0.1606 0.1678 -0.0076 -0.0006 -0.0286 58  ASN   A C   
1445 O  O   . ASN   A 58  ? 0.1513 0.1736 0.1870 -0.0192 -0.0059 -0.0273 58  ASN   A O   
1446 C  CB  . ASN   A 58  ? 0.2265 0.1922 0.2268 -0.0232 0.0381  -0.0630 58  ASN   A CB  
1447 C  CG  . ASN   A 58  ? 0.2757 0.2144 0.2989 -0.0245 0.0367  -0.0445 58  ASN   A CG  
1448 O  OD1 . ASN   A 58  ? 0.3091 0.2086 0.3509 0.0065  0.0686  -0.0363 58  ASN   A OD1 
1449 N  ND2 . ASN   A 58  ? 0.2912 0.2312 0.3250 -0.0234 0.0202  -0.0381 58  ASN   A ND2 
1456 N  N   . ASN   A 59  ? 0.1373 0.1525 0.1518 -0.0050 -0.0061 -0.0149 59  ASN   A N   
1457 C  CA  . ASN   A 59  ? 0.1407 0.1367 0.1566 -0.0028 0.0022  -0.0100 59  ASN   A CA  
1458 C  C   . ASN   A 59  ? 0.1418 0.1417 0.1541 -0.0075 -0.0035 -0.0057 59  ASN   A C   
1459 O  O   . ASN   A 59  ? 0.1400 0.1484 0.1440 -0.0091 0.0016  -0.0012 59  ASN   A O   
1460 C  CB  . ASN   A 59  ? 0.1452 0.1379 0.1573 0.0033  -0.0151 -0.0167 59  ASN   A CB  
1461 C  CG  . ASN   A 59  ? 0.1459 0.1469 0.1544 -0.0014 -0.0248 0.0057  59  ASN   A CG  
1462 O  OD1 . ASN   A 59  ? 0.1590 0.1523 0.1424 -0.0094 -0.0207 0.0027  59  ASN   A OD1 
1463 N  ND2 . ASN   A 59  ? 0.1508 0.1558 0.1718 -0.0131 -0.0203 0.0146  59  ASN   A ND2 
1470 N  N   . ALA   A 60  ? 0.1317 0.1517 0.1572 -0.0035 -0.0019 0.0026  60  ALA   A N   
1471 C  CA  . ALA   A 60  ? 0.1319 0.1508 0.1583 0.0017  -0.0114 -0.0003 60  ALA   A CA  
1472 C  C   . ALA   A 60  ? 0.1313 0.1521 0.1521 -0.0059 0.0019  -0.0056 60  ALA   A C   
1473 O  O   . ALA   A 60  ? 0.1327 0.1427 0.1756 -0.0056 -0.0066 -0.0090 60  ALA   A O   
1474 C  CB  . ALA   A 60  ? 0.1463 0.1621 0.1649 -0.0027 -0.0185 -0.0123 60  ALA   A CB  
1480 N  N   . MET   A 61  ? 0.1317 0.1462 0.1301 -0.0056 -0.0026 -0.0092 61  MET   A N   
1481 C  CA  . MET   A 61  ? 0.1337 0.1420 0.1314 -0.0012 0.0026  0.0020  61  MET   A CA  
1482 C  C   . MET   A 61  ? 0.1304 0.1419 0.1356 -0.0007 -0.0009 -0.0065 61  MET   A C   
1483 O  O   . MET   A 61  ? 0.1366 0.1334 0.1547 -0.0021 0.0022  -0.0029 61  MET   A O   
1484 C  CB  . MET   A 61  ? 0.1388 0.1454 0.1217 -0.0104 0.0007  -0.0019 61  MET   A CB  
1485 C  CG  . MET   A 61  ? 0.1380 0.1523 0.1428 -0.0044 0.0004  0.0014  61  MET   A CG  
1486 S  SD  . MET   A 61  ? 0.1422 0.1481 0.1735 -0.0101 0.0021  -0.0146 61  MET   A SD  
1487 C  CE  . MET   A 61  ? 0.1640 0.1650 0.1998 -0.0176 0.0092  -0.0161 61  MET   A CE  
1497 N  N   . GLN   A 62  ? 0.1273 0.1369 0.1428 -0.0047 0.0002  -0.0039 62  GLN   A N   
1498 C  CA  . GLN   A 62  ? 0.1327 0.1287 0.1536 -0.0099 0.0034  -0.0005 62  GLN   A CA  
1499 C  C   . GLN   A 62  ? 0.1343 0.1216 0.1601 -0.0044 0.0043  0.0026  62  GLN   A C   
1500 O  O   . GLN   A 62  ? 0.1384 0.1445 0.1461 -0.0043 0.0015  0.0021  62  GLN   A O   
1501 C  CB  . GLN   A 62  ? 0.1383 0.1284 0.1623 -0.0023 -0.0042 0.0033  62  GLN   A CB  
1502 C  CG  . GLN   A 62  ? 0.1414 0.1238 0.1633 -0.0050 -0.0022 0.0107  62  GLN   A CG  
1503 C  CD  . GLN   A 62  ? 0.1468 0.1283 0.1450 -0.0008 0.0057  0.0026  62  GLN   A CD  
1504 O  OE1 . GLN   A 62  ? 0.1490 0.1441 0.1491 -0.0036 -0.0004 0.0050  62  GLN   A OE1 
1505 N  NE2 . GLN   A 62  ? 0.1601 0.1362 0.1482 0.0012  0.0023  -0.0091 62  GLN   A NE2 
1514 N  N   . VAL   A 63  ? 0.1337 0.1323 0.1719 -0.0091 0.0039  -0.0152 63  VAL   A N   
1515 C  CA  . VAL   A 63  ? 0.1339 0.1424 0.1993 -0.0199 0.0043  -0.0146 63  VAL   A CA  
1516 C  C   . VAL   A 63  ? 0.1243 0.1453 0.1711 -0.0170 -0.0004 -0.0144 63  VAL   A C   
1517 O  O   . VAL   A 63  ? 0.1266 0.1472 0.1909 -0.0218 -0.0000 -0.0052 63  VAL   A O   
1518 C  CB  . VAL   A 63  ? 0.1479 0.1605 0.2305 -0.0184 -0.0059 -0.0341 63  VAL   A CB  
1519 C  CG1 . VAL   A 63  ? 0.1616 0.1775 0.2735 -0.0218 -0.0094 -0.0607 63  VAL   A CG1 
1520 C  CG2 . VAL   A 63  ? 0.1561 0.1560 0.2487 -0.0115 0.0071  -0.0341 63  VAL   A CG2 
1530 N  N   . GLU   A 64  ? 0.1351 0.1502 0.1665 -0.0111 -0.0037 -0.0122 64  GLU   A N   
1531 C  CA  . GLU   A 64  ? 0.1293 0.1543 0.1729 -0.0049 -0.0061 0.0003  64  GLU   A CA  
1532 C  C   . GLU   A 64  ? 0.1235 0.1385 0.1750 -0.0159 -0.0006 0.0065  64  GLU   A C   
1533 O  O   . GLU   A 64  ? 0.1298 0.1507 0.1745 -0.0035 -0.0013 -0.0059 64  GLU   A O   
1534 C  CB  . GLU   A 64  ? 0.1308 0.1617 0.1710 -0.0084 0.0020  -0.0010 64  GLU   A CB  
1535 C  CG  . GLU   A 64  ? 0.1442 0.1626 0.1853 -0.0096 0.0075  0.0048  64  GLU   A CG  
1536 C  CD  . GLU   A 64  ? 0.1606 0.1717 0.1974 -0.0092 0.0053  0.0007  64  GLU   A CD  
1537 O  OE1 . GLU   A 64  ? 0.1581 0.1791 0.2032 -0.0224 0.0147  0.0022  64  GLU   A OE1 
1538 O  OE2 . GLU   A 64  ? 0.1724 0.1712 0.1885 -0.0245 -0.0074 0.0101  64  GLU   A OE2 
1545 N  N   . SER   A 65  ? 0.1274 0.1439 0.1478 -0.0046 -0.0030 0.0049  65  SER   A N   
1546 C  CA  . SER   A 65  ? 0.1256 0.1429 0.1524 -0.0069 -0.0017 0.0004  65  SER   A CA  
1547 C  C   . SER   A 65  ? 0.1298 0.1427 0.1603 0.0018  -0.0045 -0.0022 65  SER   A C   
1548 O  O   . SER   A 65  ? 0.1416 0.1365 0.1830 0.0003  0.0141  -0.0084 65  SER   A O   
1549 C  CB  . SER   A 65  ? 0.1210 0.1467 0.1470 -0.0011 0.0081  -0.0021 65  SER   A CB  
1550 O  OG  . SER   A 65  ? 0.1263 0.1539 0.1606 -0.0136 -0.0012 0.0134  65  SER   A OG  
1556 N  N   . ASP   A 66  ? 0.1321 0.1369 0.1610 -0.0070 0.0118  0.0026  66  ASP   A N   
1557 C  CA  . ASP   A 66  ? 0.1395 0.1522 0.1700 -0.0008 0.0106  0.0144  66  ASP   A CA  
1558 C  C   . ASP   A 66  ? 0.1379 0.1446 0.1792 -0.0035 0.0132  0.0245  66  ASP   A C   
1559 O  O   . ASP   A 66  ? 0.1442 0.1576 0.1975 -0.0020 0.0252  0.0255  66  ASP   A O   
1560 C  CB  . ASP   A 66  ? 0.1438 0.1604 0.2164 0.0056  0.0184  0.0380  66  ASP   A CB  
1561 C  CG  . ASP   A 66  ? 0.1714 0.1819 0.2477 -0.0005 0.0011  0.0516  66  ASP   A CG  
1562 O  OD1 . ASP   A 66  ? 0.1723 0.2157 0.1995 -0.0105 -0.0158 0.0516  66  ASP   A OD1 
1563 O  OD2 . ASP   A 66  ? 0.1880 0.1871 0.3319 0.0212  -0.0189 0.0278  66  ASP   A OD2 
1568 N  N   . ASP   A 67  ? 0.1332 0.1488 0.1973 -0.0009 0.0056  0.0182  67  ASP   A N   
1569 C  CA  . ASP   A 67  ? 0.1321 0.1649 0.2116 -0.0042 0.0032  0.0203  67  ASP   A CA  
1570 C  C   . ASP   A 67  ? 0.1336 0.1633 0.2064 0.0009  0.0104  0.0187  67  ASP   A C   
1571 O  O   . ASP   A 67  ? 0.1328 0.1694 0.2221 0.0001  0.0217  0.0230  67  ASP   A O   
1572 C  CB  . ASP   A 67  ? 0.1354 0.1709 0.2396 -0.0101 -0.0107 0.0220  67  ASP   A CB  
1573 C  CG  . ASP   A 67  ? 0.1362 0.1881 0.2683 -0.0117 -0.0302 0.0341  67  ASP   A CG  
1574 O  OD1 . ASP   A 67  ? 0.1471 0.2091 0.3688 -0.0149 -0.0406 0.0487  67  ASP   A OD1 
1575 O  OD2 . ASP   A 67  ? 0.1438 0.1959 0.2624 0.0020  -0.0188 0.0286  67  ASP   A OD2 
1580 N  N   . TYR   A 68  ? 0.1355 0.1504 0.2051 0.0010  0.0191  0.0266  68  TYR   A N   
1581 C  CA  . TYR   A 68  ? 0.1491 0.1469 0.1975 0.0018  0.0266  0.0245  68  TYR   A CA  
1582 C  C   . TYR   A 68  ? 0.1415 0.1443 0.1879 -0.0057 0.0298  0.0211  68  TYR   A C   
1583 O  O   . TYR   A 68  ? 0.1491 0.1481 0.1935 0.0022  0.0285  0.0174  68  TYR   A O   
1584 C  CB  . TYR   A 68  ? 0.1512 0.1413 0.2163 0.0037  0.0441  0.0230  68  TYR   A CB  
1585 C  CG  . TYR   A 68  ? 0.1485 0.1597 0.2373 0.0063  0.0508  0.0334  68  TYR   A CG  
1586 C  CD1 . TYR   A 68  ? 0.1672 0.1690 0.2618 -0.0187 0.0448  0.0007  68  TYR   A CD1 
1587 C  CD2 . TYR   A 68  ? 0.1844 0.1698 0.2621 0.0157  0.0523  0.0343  68  TYR   A CD2 
1588 C  CE1 . TYR   A 68  ? 0.1719 0.1786 0.3007 -0.0145 0.0569  -0.0153 68  TYR   A CE1 
1589 C  CE2 . TYR   A 68  ? 0.1782 0.1635 0.2783 0.0088  0.0672  0.0109  68  TYR   A CE2 
1590 C  CZ  . TYR   A 68  ? 0.1831 0.1713 0.2986 -0.0155 0.0551  -0.0153 68  TYR   A CZ  
1591 O  OH  . TYR   A 68  ? 0.2079 0.1730 0.3136 -0.0110 0.0278  -0.0425 68  TYR   A OH  
1601 N  N   . ILE   A 69  ? 0.1371 0.1419 0.1875 -0.0002 0.0194  0.0194  69  ILE   A N   
1602 C  CA  . ILE   A 69  ? 0.1440 0.1422 0.1792 0.0042  0.0125  0.0104  69  ILE   A CA  
1603 C  C   . ILE   A 69  ? 0.1527 0.1505 0.1626 0.0030  0.0166  0.0118  69  ILE   A C   
1604 O  O   . ILE   A 69  ? 0.1616 0.1595 0.1654 -0.0035 0.0250  0.0112  69  ILE   A O   
1605 C  CB  . ILE   A 69  ? 0.1516 0.1683 0.1788 0.0018  0.0170  -0.0011 69  ILE   A CB  
1606 C  CG1 . ILE   A 69  ? 0.1544 0.1728 0.1818 0.0088  0.0253  -0.0167 69  ILE   A CG1 
1607 C  CG2 . ILE   A 69  ? 0.1677 0.1914 0.1941 0.0120  0.0066  -0.0080 69  ILE   A CG2 
1608 C  CD1 . ILE   A 69  ? 0.1558 0.1813 0.1980 -0.0001 0.0213  -0.0116 69  ILE   A CD1 
1620 N  N   . ALA   A 70  ? 0.1508 0.1506 0.1792 -0.0056 0.0172  0.0143  70  ALA   A N   
1621 C  CA  . ALA   A 70  ? 0.1549 0.1618 0.2047 -0.0171 0.0293  0.0165  70  ALA   A CA  
1622 C  C   . ALA   A 70  ? 0.1554 0.1716 0.2006 -0.0175 0.0379  0.0163  70  ALA   A C   
1623 O  O   . ALA   A 70  ? 0.1698 0.2098 0.2319 0.0050  0.0567  0.0307  70  ALA   A O   
1624 C  CB  . ALA   A 70  ? 0.1586 0.1608 0.2403 -0.0185 0.0234  0.0094  70  ALA   A CB  
1630 N  N   . THR   A 71  ? 0.1502 0.1695 0.1944 -0.0009 0.0217  0.0212  71  THR   A N   
1631 C  CA  . THR   A 71  ? 0.1620 0.1812 0.2272 0.0078  0.0217  0.0283  71  THR   A CA  
1632 C  C   . THR   A 71  ? 0.1516 0.1797 0.2482 0.0114  0.0355  0.0198  71  THR   A C   
1633 O  O   . THR   A 71  ? 0.1613 0.2021 0.2925 0.0078  0.0494  -0.0099 71  THR   A O   
1634 C  CB  . THR   A 71  ? 0.1900 0.1999 0.2688 0.0168  -0.0071 0.0301  71  THR   A CB  
1635 O  OG1 . THR   A 71  ? 0.2218 0.2217 0.2711 0.0075  -0.0318 0.0233  71  THR   A OG1 
1636 C  CG2 . THR   A 71  ? 0.2053 0.2187 0.2856 0.0252  -0.0265 0.0384  71  THR   A CG2 
1644 N  N   . ASN   A 72  ? 0.1499 0.1665 0.2096 0.0076  0.0262  0.0194  72  ASN   A N   
1645 C  CA  . ASN   A 72  ? 0.1489 0.1689 0.2379 0.0144  0.0392  0.0133  72  ASN   A CA  
1646 C  C   . ASN   A 72  ? 0.1606 0.1696 0.2251 0.0100  0.0495  0.0095  72  ASN   A C   
1647 O  O   . ASN   A 72  ? 0.1853 0.1671 0.2279 0.0116  0.0406  0.0008  72  ASN   A O   
1648 C  CB  . ASN   A 72  ? 0.1648 0.1818 0.2331 0.0207  0.0427  0.0226  72  ASN   A CB  
1649 C  CG  . ASN   A 72  ? 0.1890 0.1943 0.2320 0.0262  0.0363  0.0302  72  ASN   A CG  
1650 O  OD1 . ASN   A 72  ? 0.2031 0.2317 0.2543 0.0265  0.0486  0.0326  72  ASN   A OD1 
1651 N  ND2 . ASN   A 72  ? 0.2106 0.1838 0.2336 0.0507  0.0094  0.0154  72  ASN   A ND2 
1658 N  N   . GLY   A 73  ? 0.1612 0.1644 0.2222 0.0030  0.0487  0.0045  73  GLY   A N   
1659 C  CA  . GLY   A 73  ? 0.1614 0.1631 0.2101 -0.0065 0.0448  0.0061  73  GLY   A CA  
1660 C  C   . GLY   A 73  ? 0.1661 0.1519 0.1859 0.0009  0.0511  0.0206  73  GLY   A C   
1661 O  O   . GLY   A 73  ? 0.1633 0.1553 0.2014 0.0109  0.0373  0.0306  73  GLY   A O   
1665 N  N   . PRO   A 74  ? 0.1778 0.1530 0.1844 -0.0159 0.0497  0.0088  74  PRO   A N   
1666 C  CA  . PRO   A 74  ? 0.1788 0.1553 0.1899 -0.0034 0.0446  0.0159  74  PRO   A CA  
1667 C  C   . PRO   A 74  ? 0.1755 0.1316 0.1784 -0.0037 0.0350  0.0076  74  PRO   A C   
1668 O  O   . PRO   A 74  ? 0.1827 0.1408 0.2050 -0.0003 0.0348  -0.0063 74  PRO   A O   
1669 C  CB  . PRO   A 74  ? 0.1911 0.1830 0.2075 -0.0002 0.0477  0.0270  74  PRO   A CB  
1670 C  CG  . PRO   A 74  ? 0.2168 0.2190 0.2534 -0.0239 0.0368  0.0026  74  PRO   A CG  
1671 C  CD  . PRO   A 74  ? 0.1933 0.1874 0.2086 -0.0281 0.0372  -0.0109 74  PRO   A CD  
1679 N  N   . LEU   A 75  ? 0.1746 0.1280 0.1567 -0.0045 0.0278  0.0052  75  LEU   A N   
1680 C  CA  . LEU   A 75  ? 0.1752 0.1320 0.1531 -0.0038 0.0112  0.0065  75  LEU   A CA  
1681 C  C   . LEU   A 75  ? 0.1799 0.1439 0.1558 0.0062  0.0172  0.0120  75  LEU   A C   
1682 O  O   . LEU   A 75  ? 0.2158 0.1629 0.1564 0.0119  0.0191  0.0106  75  LEU   A O   
1683 C  CB  . LEU   A 75  ? 0.1766 0.1356 0.1453 -0.0165 0.0106  0.0149  75  LEU   A CB  
1684 C  CG  . LEU   A 75  ? 0.1875 0.1613 0.1708 -0.0356 0.0116  0.0132  75  LEU   A CG  
1685 C  CD1 . LEU   A 75  ? 0.1997 0.2092 0.1764 -0.0367 0.0096  -0.0006 75  LEU   A CD1 
1686 C  CD2 . LEU   A 75  ? 0.2210 0.2027 0.2385 -0.0127 -0.0018 0.0306  75  LEU   A CD2 
1698 N  N   . LYS   A 76  ? 0.1750 0.1314 0.1749 -0.0092 0.0156  -0.0032 76  LYS   A N   
1699 C  CA  . LYS   A 76  ? 0.1739 0.1584 0.1833 -0.0074 0.0162  -0.0084 76  LYS   A CA  
1700 C  C   . LYS   A 76  ? 0.1684 0.1461 0.1503 0.0045  0.0095  0.0105  76  LYS   A C   
1701 O  O   . LYS   A 76  ? 0.1746 0.1419 0.1438 0.0009  0.0140  0.0112  76  LYS   A O   
1702 C  CB  . LYS   A 76  ? 0.1762 0.1863 0.2138 0.0029  0.0262  -0.0289 76  LYS   A CB  
1703 C  CG  . LYS   A 76  ? 0.1886 0.1827 0.2638 0.0095  0.0186  -0.0251 76  LYS   A CG  
1704 C  CD  . LYS   A 76  ? 0.1941 0.1825 0.3158 0.0098  -0.0033 -0.0424 76  LYS   A CD  
1705 C  CE  . LYS   A 76  ? 0.2155 0.2124 0.3705 -0.0040 0.0055  -0.0592 76  LYS   A CE  
1706 N  NZ  . LYS   A 76  ? 0.2176 0.2084 0.4119 -0.0227 0.0077  -0.0749 76  LYS   A NZ  
1720 N  N   . VAL   A 77  ? 0.1797 0.1497 0.1482 -0.0022 0.0244  0.0211  77  VAL   A N   
1721 C  CA  . VAL   A 77  ? 0.1810 0.1567 0.1335 0.0042  0.0223  0.0123  77  VAL   A CA  
1722 C  C   . VAL   A 77  ? 0.1774 0.1501 0.1390 0.0127  0.0151  0.0074  77  VAL   A C   
1723 O  O   . VAL   A 77  ? 0.1825 0.1549 0.1388 0.0147  0.0250  -0.0061 77  VAL   A O   
1724 C  CB  . VAL   A 77  ? 0.1982 0.1728 0.1487 -0.0027 0.0137  0.0276  77  VAL   A CB  
1725 C  CG1 . VAL   A 77  ? 0.1932 0.1976 0.1642 0.0036  0.0032  0.0187  77  VAL   A CG1 
1726 C  CG2 . VAL   A 77  ? 0.2282 0.1789 0.1803 0.0002  0.0064  0.0311  77  VAL   A CG2 
1736 N  N   . GLY   A 78  ? 0.1716 0.1382 0.1295 0.0028  0.0189  0.0080  78  GLY   A N   
1737 C  CA  . GLY   A 78  ? 0.1653 0.1430 0.1487 0.0011  0.0294  0.0135  78  GLY   A CA  
1738 C  C   . GLY   A 78  ? 0.1523 0.1421 0.1471 0.0090  0.0219  0.0159  78  GLY   A C   
1739 O  O   . GLY   A 78  ? 0.1559 0.1536 0.1607 0.0017  0.0153  0.0254  78  GLY   A O   
1743 N  N   . GLY   A 79  ? 0.1510 0.1397 0.1490 0.0013  0.0178  0.0137  79  GLY   A N   
1744 C  CA  . GLY   A 79  ? 0.1578 0.1424 0.1598 -0.0014 0.0218  0.0139  79  GLY   A CA  
1745 C  C   . GLY   A 79  ? 0.1412 0.1336 0.1448 0.0033  0.0134  0.0062  79  GLY   A C   
1746 O  O   . GLY   A 79  ? 0.1498 0.1436 0.1518 0.0189  0.0126  0.0067  79  GLY   A O   
1750 N  N   . SER   A 80  ? 0.1357 0.1493 0.1654 0.0026  0.0156  0.0023  80  SER   A N   
1751 C  CA  . SER   A 80  ? 0.1354 0.1414 0.1638 -0.0005 0.0076  0.0060  80  SER   A CA  
1752 C  C   . SER   A 80  ? 0.1327 0.1424 0.1629 -0.0050 0.0094  0.0122  80  SER   A C   
1753 O  O   . SER   A 80  ? 0.1312 0.1647 0.1973 0.0056  0.0109  0.0001  80  SER   A O   
1754 C  CB  . SER   A 80  ? 0.1486 0.1464 0.1906 -0.0010 0.0130  0.0123  80  SER   A CB  
1755 O  OG  . SER   A 80  ? 0.1723 0.1434 0.2317 0.0075  -0.0008 0.0232  80  SER   A OG  
1761 N  N   . CYS   A 81  ? 0.1296 0.1428 0.1506 0.0017  0.0016  0.0188  81  CYS   A N   
1762 C  CA  . CYS   A 81  ? 0.1269 0.1471 0.1567 -0.0001 -0.0109 0.0253  81  CYS   A CA  
1763 C  C   . CYS   A 81  ? 0.1310 0.1475 0.1533 -0.0057 -0.0083 0.0280  81  CYS   A C   
1764 O  O   . CYS   A 81  ? 0.1294 0.1725 0.1610 -0.0044 -0.0019 0.0335  81  CYS   A O   
1765 C  CB  . CYS   A 81  ? 0.1395 0.1524 0.1716 -0.0079 -0.0044 0.0265  81  CYS   A CB  
1766 S  SG  . CYS   A 81  ? 0.1531 0.1456 0.1601 -0.0126 0.0004  0.0155  81  CYS   A SG  
1772 N  N   . VAL   A 82  ? 0.1352 0.1482 0.1632 -0.0006 -0.0089 0.0193  82  VAL   A N   
1773 C  CA  . VAL   A 82  ? 0.1427 0.1588 0.1729 -0.0014 -0.0054 0.0309  82  VAL   A CA  
1774 C  C   . VAL   A 82  ? 0.1410 0.1597 0.1719 -0.0077 -0.0103 0.0349  82  VAL   A C   
1775 O  O   . VAL   A 82  ? 0.1432 0.1665 0.1839 -0.0074 -0.0085 0.0068  82  VAL   A O   
1776 C  CB  . VAL   A 82  ? 0.1745 0.1744 0.1762 0.0067  0.0005  0.0291  82  VAL   A CB  
1777 C  CG1 . VAL   A 82  ? 0.1925 0.1899 0.1984 0.0077  0.0009  0.0310  82  VAL   A CG1 
1778 C  CG2 . VAL   A 82  ? 0.1800 0.1729 0.2038 -0.0032 -0.0045 0.0314  82  VAL   A CG2 
1788 N  N   . LEU   A 83  ? 0.1408 0.1584 0.1473 -0.0126 -0.0066 0.0108  83  LEU   A N   
1789 C  CA  . LEU   A 83  ? 0.1447 0.1553 0.1371 -0.0142 -0.0057 0.0118  83  LEU   A CA  
1790 C  C   . LEU   A 83  ? 0.1476 0.1676 0.1385 -0.0163 -0.0150 0.0241  83  LEU   A C   
1791 O  O   . LEU   A 83  ? 0.1557 0.1715 0.1468 -0.0212 -0.0027 0.0246  83  LEU   A O   
1792 C  CB  . LEU   A 83  ? 0.1525 0.1625 0.1464 -0.0098 -0.0064 0.0133  83  LEU   A CB  
1793 C  CG  . LEU   A 83  ? 0.1639 0.1714 0.1491 -0.0097 0.0024  0.0072  83  LEU   A CG  
1794 C  CD1 . LEU   A 83  ? 0.1746 0.1777 0.1651 -0.0254 0.0055  0.0329  83  LEU   A CD1 
1795 C  CD2 . LEU   A 83  ? 0.1642 0.1882 0.1589 -0.0073 0.0084  0.0122  83  LEU   A CD2 
1807 N  N   . SER   A 84  ? 0.1618 0.1763 0.1370 -0.0176 -0.0158 0.0158  84  SER   A N   
1808 C  CA  . SER   A 84  ? 0.1709 0.1754 0.1340 -0.0156 -0.0171 0.0167  84  SER   A CA  
1809 C  C   . SER   A 84  ? 0.1769 0.1726 0.1327 -0.0216 -0.0021 0.0131  84  SER   A C   
1810 O  O   . SER   A 84  ? 0.1678 0.1804 0.1334 -0.0134 -0.0081 0.0112  84  SER   A O   
1811 C  CB  . SER   A 84  ? 0.1722 0.1923 0.1483 -0.0046 -0.0139 -0.0007 84  SER   A CB  
1812 O  OG  . SER   A 84  ? 0.1776 0.2194 0.1497 -0.0075 -0.0237 -0.0100 84  SER   A OG  
1818 N  N   . GLY   A 85  ? 0.1875 0.1861 0.1323 -0.0264 0.0037  0.0058  85  GLY   A N   
1819 C  CA  . GLY   A 85  ? 0.1917 0.1996 0.1424 -0.0263 0.0117  -0.0048 85  GLY   A CA  
1820 C  C   . GLY   A 85  ? 0.1803 0.2029 0.1224 -0.0242 -0.0042 -0.0032 85  GLY   A C   
1821 O  O   . GLY   A 85  ? 0.1820 0.2117 0.1417 -0.0298 0.0112  -0.0118 85  GLY   A O   
1825 N  N   . HIS   A 86  ? 0.1839 0.1934 0.1187 -0.0196 -0.0071 0.0023  86  HIS   A N   
1826 C  CA  . HIS   A 86  ? 0.1999 0.2051 0.1096 -0.0203 -0.0080 0.0077  86  HIS   A CA  
1827 C  C   . HIS   A 86  ? 0.2141 0.2167 0.1152 -0.0222 -0.0153 0.0112  86  HIS   A C   
1828 O  O   . HIS   A 86  ? 0.2286 0.2391 0.1309 -0.0283 -0.0040 0.0044  86  HIS   A O   
1829 C  CB  . HIS   A 86  ? 0.1993 0.1987 0.1267 -0.0169 -0.0024 0.0073  86  HIS   A CB  
1830 C  CG  . HIS   A 86  ? 0.1861 0.1948 0.1271 -0.0128 0.0020  0.0092  86  HIS   A CG  
1831 N  ND1 . HIS   A 86  ? 0.1964 0.1945 0.1798 -0.0265 0.0001  0.0143  86  HIS   A ND1 
1832 C  CD2 . HIS   A 86  ? 0.1853 0.1892 0.1251 0.0044  0.0103  0.0125  86  HIS   A CD2 
1833 C  CE1 . HIS   A 86  ? 0.1863 0.1964 0.1697 -0.0163 0.0135  0.0184  86  HIS   A CE1 
1834 N  NE2 . HIS   A 86  ? 0.1865 0.1932 0.1507 0.0020  0.0133  0.0257  86  HIS   A NE2 
1842 N  N   . ASN   A 87  ? 0.2286 0.2223 0.1461 -0.0229 0.0109  -0.0038 87  ASN   A N   
1843 C  CA  . ASN   A 87  ? 0.2471 0.2356 0.1531 -0.0156 0.0385  -0.0169 87  ASN   A CA  
1844 C  C   . ASN   A 87  ? 0.2444 0.2538 0.1819 -0.0238 0.0500  -0.0026 87  ASN   A C   
1845 O  O   . ASN   A 87  ? 0.2729 0.2705 0.2171 -0.0383 0.0856  -0.0094 87  ASN   A O   
1846 C  CB  . ASN   A 87  ? 0.2655 0.2401 0.1559 -0.0032 0.0439  -0.0207 87  ASN   A CB  
1847 C  CG  . ASN   A 87  ? 0.2812 0.2481 0.1533 0.0078  0.0557  -0.0084 87  ASN   A CG  
1848 O  OD1 . ASN   A 87  ? 0.3012 0.2481 0.1626 0.0260  0.0536  0.0088  87  ASN   A OD1 
1849 N  ND2 . ASN   A 87  ? 0.2811 0.2740 0.1812 0.0064  0.0633  -0.0001 87  ASN   A ND2 
1856 N  N   A LEU   A 88  ? 0.2177 0.2434 0.1669 -0.0286 0.0298  0.0135  88  LEU   A N   
1857 N  N   B LEU   A 88  ? 0.2295 0.2477 0.1788 -0.0277 0.0363  0.0018  88  LEU   A N   
1858 C  CA  A LEU   A 88  ? 0.2009 0.2412 0.1760 -0.0359 0.0297  0.0367  88  LEU   A CA  
1859 C  CA  B LEU   A 88  ? 0.2176 0.2453 0.1880 -0.0291 0.0301  0.0104  88  LEU   A CA  
1860 C  C   A LEU   A 88  ? 0.1931 0.2446 0.1708 -0.0348 0.0269  0.0411  88  LEU   A C   
1861 C  C   B LEU   A 88  ? 0.2046 0.2432 0.1745 -0.0287 0.0250  0.0221  88  LEU   A C   
1862 O  O   A LEU   A 88  ? 0.1989 0.2491 0.2073 -0.0320 0.0254  0.0540  88  LEU   A O   
1863 O  O   B LEU   A 88  ? 0.2074 0.2441 0.1946 -0.0263 0.0254  0.0352  88  LEU   A O   
1864 C  CB  A LEU   A 88  ? 0.2038 0.2477 0.1895 -0.0414 -0.0078 0.0562  88  LEU   A CB  
1865 C  CB  B LEU   A 88  ? 0.2220 0.2499 0.2052 -0.0299 0.0152  0.0100  88  LEU   A CB  
1866 C  CG  A LEU   A 88  ? 0.2266 0.2578 0.2273 -0.0412 -0.0185 0.0603  88  LEU   A CG  
1867 C  CG  B LEU   A 88  ? 0.2288 0.2554 0.2220 -0.0274 0.0110  0.0032  88  LEU   A CG  
1868 C  CD1 A LEU   A 88  ? 0.2387 0.2639 0.2226 -0.0391 -0.0221 0.0475  88  LEU   A CD1 
1869 C  CD1 B LEU   A 88  ? 0.2317 0.2590 0.2197 -0.0250 0.0133  -0.0092 88  LEU   A CD1 
1870 C  CD2 A LEU   A 88  ? 0.2426 0.2668 0.2666 -0.0347 -0.0203 0.0463  88  LEU   A CD2 
1871 C  CD2 B LEU   A 88  ? 0.2336 0.2592 0.2371 -0.0241 0.0082  -0.0021 88  LEU   A CD2 
1894 N  N   . ALA   A 89  ? 0.1942 0.2377 0.1470 -0.0283 0.0156  0.0157  89  ALA   A N   
1895 C  CA  . ALA   A 89  ? 0.2026 0.2351 0.1217 -0.0162 0.0043  0.0241  89  ALA   A CA  
1896 C  C   . ALA   A 89  ? 0.2173 0.2288 0.1340 -0.0182 -0.0070 0.0207  89  ALA   A C   
1897 O  O   . ALA   A 89  ? 0.2137 0.2242 0.1793 -0.0330 -0.0128 -0.0057 89  ALA   A O   
1898 C  CB  . ALA   A 89  ? 0.1890 0.2322 0.1282 -0.0142 0.0074  0.0358  89  ALA   A CB  
1905 N  N   . LYS   A 90  ? 0.2264 0.2415 0.1430 -0.0294 -0.0219 0.0243  90  LYS   A N   
1906 C  CA  . LYS   A 90  ? 0.2277 0.2525 0.1608 -0.0248 -0.0355 0.0243  90  LYS   A CA  
1907 C  C   . LYS   A 90  ? 0.2050 0.2372 0.1416 -0.0303 -0.0314 0.0159  90  LYS   A C   
1908 O  O   . LYS   A 90  ? 0.2085 0.2580 0.1523 -0.0329 -0.0350 0.0033  90  LYS   A O   
1909 C  CB  . LYS   A 90  ? 0.2474 0.2870 0.1887 -0.0165 -0.0513 0.0436  90  LYS   A CB  
1910 C  CG  . LYS   A 90  ? 0.2887 0.3235 0.2847 -0.0118 -0.0547 0.0473  90  LYS   A CG  
1911 C  CD  . LYS   A 90  ? 0.3191 0.3497 0.3757 -0.0136 -0.0418 0.0585  90  LYS   A CD  
1912 C  CE  . LYS   A 90  ? 0.3410 0.3582 0.4598 -0.0143 -0.0276 0.0553  90  LYS   A CE  
1913 N  NZ  . LYS   A 90  ? 0.4057 0.4057 0.5024 -0.0157 -0.0154 0.0412  90  LYS   A NZ  
1927 N  N   . HIS   A 91  ? 0.1966 0.2091 0.1188 -0.0298 -0.0330 0.0285  91  HIS   A N   
1928 C  CA  . HIS   A 91  ? 0.1849 0.1924 0.1224 -0.0276 -0.0337 0.0244  91  HIS   A CA  
1929 C  C   . HIS   A 91  ? 0.1678 0.1822 0.1108 -0.0267 -0.0155 0.0178  91  HIS   A C   
1930 O  O   . HIS   A 91  ? 0.1609 0.1904 0.1292 -0.0313 -0.0060 0.0218  91  HIS   A O   
1931 C  CB  . HIS   A 91  ? 0.1991 0.2213 0.1863 -0.0011 -0.0472 0.0273  91  HIS   A CB  
1932 C  CG  . HIS   A 91  ? 0.2469 0.2710 0.2635 0.0089  -0.0728 0.0146  91  HIS   A CG  
1933 N  ND1 . HIS   A 91  ? 0.2585 0.2999 0.3040 0.0177  -0.0865 -0.0120 91  HIS   A ND1 
1934 C  CD2 . HIS   A 91  ? 0.2700 0.2915 0.2883 0.0237  -0.0941 0.0272  91  HIS   A CD2 
1935 C  CE1 . HIS   A 91  ? 0.2694 0.3090 0.3261 0.0253  -0.0940 -0.0018 91  HIS   A CE1 
1936 N  NE2 . HIS   A 91  ? 0.2824 0.3091 0.3121 0.0305  -0.1020 0.0136  91  HIS   A NE2 
1944 N  N   . CYS   A 92  ? 0.1565 0.1723 0.1159 -0.0275 -0.0162 0.0216  92  CYS   A N   
1945 C  CA  . CYS   A 92  ? 0.1451 0.1632 0.1305 -0.0227 -0.0055 0.0172  92  CYS   A CA  
1946 C  C   . CYS   A 92  ? 0.1451 0.1605 0.1268 -0.0258 0.0019  0.0167  92  CYS   A C   
1947 O  O   . CYS   A 92  ? 0.1451 0.1661 0.1339 -0.0244 -0.0030 0.0158  92  CYS   A O   
1948 C  CB  . CYS   A 92  ? 0.1457 0.1662 0.1431 -0.0126 -0.0111 0.0116  92  CYS   A CB  
1949 S  SG  . CYS   A 92  ? 0.1481 0.1549 0.1367 -0.0119 -0.0039 0.0137  92  CYS   A SG  
1955 N  N   . LEU   A 93  ? 0.1406 0.1458 0.1230 -0.0143 0.0028  0.0134  93  LEU   A N   
1956 C  CA  . LEU   A 93  ? 0.1295 0.1398 0.1316 -0.0105 -0.0009 0.0139  93  LEU   A CA  
1957 C  C   . LEU   A 93  ? 0.1226 0.1341 0.1249 -0.0044 0.0011  0.0090  93  LEU   A C   
1958 O  O   . LEU   A 93  ? 0.1292 0.1423 0.1298 -0.0073 -0.0015 0.0130  93  LEU   A O   
1959 C  CB  . LEU   A 93  ? 0.1387 0.1400 0.1387 -0.0084 -0.0109 0.0233  93  LEU   A CB  
1960 C  CG  . LEU   A 93  ? 0.1445 0.1439 0.1475 -0.0099 -0.0021 0.0280  93  LEU   A CG  
1961 C  CD1 . LEU   A 93  ? 0.1482 0.1529 0.1792 -0.0036 0.0122  0.0240  93  LEU   A CD1 
1962 C  CD2 . LEU   A 93  ? 0.1575 0.1409 0.1676 -0.0117 -0.0064 0.0165  93  LEU   A CD2 
1974 N  N   . HIS   A 94  ? 0.1181 0.1277 0.1277 -0.0063 0.0010  0.0179  94  HIS   A N   
1975 C  CA  . HIS   A 94  ? 0.1194 0.1306 0.1270 -0.0025 -0.0014 0.0150  94  HIS   A CA  
1976 C  C   . HIS   A 94  ? 0.1238 0.1279 0.1304 -0.0060 0.0005  0.0046  94  HIS   A C   
1977 O  O   . HIS   A 94  ? 0.1316 0.1510 0.1599 -0.0028 0.0017  -0.0117 94  HIS   A O   
1978 C  CB  . HIS   A 94  ? 0.1213 0.1275 0.1294 -0.0041 -0.0040 0.0161  94  HIS   A CB  
1979 C  CG  . HIS   A 94  ? 0.1303 0.1278 0.1225 -0.0048 -0.0065 0.0089  94  HIS   A CG  
1980 N  ND1 . HIS   A 94  ? 0.1313 0.1262 0.1283 -0.0047 -0.0019 0.0146  94  HIS   A ND1 
1981 C  CD2 . HIS   A 94  ? 0.1315 0.1410 0.1357 -0.0023 -0.0033 0.0029  94  HIS   A CD2 
1982 C  CE1 . HIS   A 94  ? 0.1308 0.1366 0.1265 -0.0084 -0.0138 0.0136  94  HIS   A CE1 
1983 N  NE2 . HIS   A 94  ? 0.1359 0.1428 0.1334 -0.0149 -0.0112 0.0000  94  HIS   A NE2 
1991 N  N   . VAL   A 95  ? 0.1235 0.1255 0.1169 -0.0052 0.0092  -0.0004 95  VAL   A N   
1992 C  CA  . VAL   A 95  ? 0.1327 0.1346 0.1143 -0.0030 0.0135  0.0098  95  VAL   A CA  
1993 C  C   . VAL   A 95  ? 0.1345 0.1226 0.1088 -0.0151 -0.0012 0.0144  95  VAL   A C   
1994 O  O   . VAL   A 95  ? 0.1338 0.1414 0.1245 0.0068  0.0039  0.0082  95  VAL   A O   
1995 C  CB  . VAL   A 95  ? 0.1355 0.1284 0.1371 -0.0134 0.0082  0.0097  95  VAL   A CB  
1996 C  CG1 . VAL   A 95  ? 0.1471 0.1369 0.1607 -0.0206 0.0062  0.0010  95  VAL   A CG1 
1997 C  CG2 . VAL   A 95  ? 0.1361 0.1336 0.1417 -0.0131 0.0063  0.0191  95  VAL   A CG2 
2007 N  N   . VAL   A 96  ? 0.1333 0.1258 0.1071 -0.0029 0.0064  0.0140  96  VAL   A N   
2008 C  CA  . VAL   A 96  ? 0.1383 0.1325 0.1262 0.0001  0.0115  0.0143  96  VAL   A CA  
2009 C  C   . VAL   A 96  ? 0.1372 0.1459 0.1179 -0.0025 0.0095  0.0081  96  VAL   A C   
2010 O  O   . VAL   A 96  ? 0.1471 0.1434 0.1418 -0.0080 0.0161  -0.0022 96  VAL   A O   
2011 C  CB  . VAL   A 96  ? 0.1446 0.1379 0.1412 -0.0013 0.0210  0.0094  96  VAL   A CB  
2012 C  CG1 . VAL   A 96  ? 0.1556 0.1350 0.1373 -0.0069 0.0186  0.0119  96  VAL   A CG1 
2013 C  CG2 . VAL   A 96  ? 0.1484 0.1410 0.1635 -0.0055 0.0184  0.0117  96  VAL   A CG2 
2023 N  N   A GLY   A 97  ? 0.1439 0.1492 0.1161 -0.0091 0.0031  0.0114  97  GLY   A N   
2024 N  N   B GLY   A 97  ? 0.1411 0.1456 0.1226 -0.0065 0.0088  0.0133  97  GLY   A N   
2025 C  CA  A GLY   A 97  ? 0.1549 0.1586 0.1278 -0.0096 -0.0050 0.0113  97  GLY   A CA  
2026 C  CA  B GLY   A 97  ? 0.1480 0.1496 0.1313 -0.0066 0.0081  0.0137  97  GLY   A CA  
2027 C  C   A GLY   A 97  ? 0.1574 0.1671 0.1102 -0.0080 -0.0068 0.0025  97  GLY   A C   
2028 C  C   B GLY   A 97  ? 0.1538 0.1519 0.1316 -0.0045 0.0151  0.0161  97  GLY   A C   
2029 O  O   A GLY   A 97  ? 0.1625 0.1649 0.1228 -0.0086 0.0043  0.0074  97  GLY   A O   
2030 O  O   B GLY   A 97  ? 0.1531 0.1485 0.1482 -0.0041 0.0240  0.0131  97  GLY   A O   
2037 N  N   A PRO   A 98  ? 0.1547 0.1646 0.1009 -0.0048 -0.0131 0.0109  98  PRO   A N   
2038 N  N   B PRO   A 98  ? 0.1667 0.1541 0.1345 -0.0070 0.0124  0.0323  98  PRO   A N   
2039 C  CA  A PRO   A 98  ? 0.1635 0.1805 0.1136 -0.0032 -0.0036 0.0045  98  PRO   A CA  
2040 C  CA  B PRO   A 98  ? 0.1806 0.1597 0.1523 -0.0076 0.0073  0.0240  98  PRO   A CA  
2041 C  C   A PRO   A 98  ? 0.1638 0.1879 0.0936 -0.0110 0.0024  0.0147  98  PRO   A C   
2042 C  C   B PRO   A 98  ? 0.1957 0.1603 0.1502 -0.0083 0.0022  0.0254  98  PRO   A C   
2043 O  O   A PRO   A 98  ? 0.1594 0.1738 0.1080 -0.0094 0.0089  0.0115  98  PRO   A O   
2044 O  O   B PRO   A 98  ? 0.1933 0.1558 0.1690 -0.0045 -0.0011 0.0264  98  PRO   A O   
2045 C  CB  A PRO   A 98  ? 0.1737 0.1907 0.1182 0.0103  -0.0076 -0.0107 98  PRO   A CB  
2046 C  CB  B PRO   A 98  ? 0.1800 0.1618 0.1481 0.0008  0.0040  0.0166  98  PRO   A CB  
2047 C  CG  A PRO   A 98  ? 0.1773 0.1874 0.1235 0.0138  -0.0011 -0.0208 98  PRO   A CG  
2048 C  CG  B PRO   A 98  ? 0.1823 0.1638 0.1395 -0.0021 0.0069  0.0217  98  PRO   A CG  
2049 C  CD  A PRO   A 98  ? 0.1641 0.1701 0.1064 0.0079  -0.0024 -0.0048 98  PRO   A CD  
2050 C  CD  B PRO   A 98  ? 0.1741 0.1543 0.1229 -0.0027 0.0083  0.0382  98  PRO   A CD  
2065 N  N   A ASN   A 99  ? 0.1620 0.2097 0.1066 -0.0044 0.0207  0.0250  99  ASN   A N   
2066 N  N   B ASN   A 99  ? 0.2121 0.1687 0.1453 -0.0075 0.0029  0.0346  99  ASN   A N   
2067 C  CA  A ASN   A 99  ? 0.1774 0.2244 0.1131 -0.0033 0.0137  0.0441  99  ASN   A CA  
2068 C  CA  B ASN   A 99  ? 0.2343 0.1750 0.1362 -0.0034 0.0030  0.0536  99  ASN   A CA  
2069 C  C   A ASN   A 99  ? 0.1874 0.2487 0.0990 -0.0119 0.0133  0.0478  99  ASN   A C   
2070 C  C   B ASN   A 99  ? 0.2461 0.1749 0.1263 -0.0025 -0.0133 0.0614  99  ASN   A C   
2071 O  O   A ASN   A 99  ? 0.2024 0.2662 0.1334 -0.0098 -0.0021 0.0344  99  ASN   A O   
2072 O  O   B ASN   A 99  ? 0.2487 0.1617 0.1310 0.0005  -0.0294 0.0491  99  ASN   A O   
2073 C  CB  A ASN   A 99  ? 0.1754 0.2166 0.1256 -0.0078 0.0045  0.0465  99  ASN   A CB  
2074 C  CB  B ASN   A 99  ? 0.2446 0.1769 0.1560 0.0018  0.0128  0.0551  99  ASN   A CB  
2075 C  CG  A ASN   A 99  ? 0.1819 0.2117 0.1440 -0.0086 -0.0168 0.0233  99  ASN   A CG  
2076 C  CG  B ASN   A 99  ? 0.2563 0.1838 0.1769 0.0022  0.0142  0.0562  99  ASN   A CG  
2077 O  OD1 A ASN   A 99  ? 0.1991 0.2195 0.1504 -0.0030 -0.0173 0.0120  99  ASN   A OD1 
2078 O  OD1 B ASN   A 99  ? 0.2616 0.1844 0.1698 0.0064  0.0172  0.0606  99  ASN   A OD1 
2079 N  ND2 A ASN   A 99  ? 0.1821 0.2008 0.1828 -0.0106 -0.0239 0.0418  99  ASN   A ND2 
2080 N  ND2 B ASN   A 99  ? 0.2586 0.1897 0.2253 0.0051  0.0028  0.0503  99  ASN   A ND2 
2093 N  N   A VAL   A 100 ? 0.2085 0.2587 0.1201 -0.0263 -0.0081 0.0295  100 VAL   A N   
2094 N  N   B VAL   A 100 ? 0.2593 0.1970 0.1542 -0.0009 -0.0130 0.0605  100 VAL   A N   
2095 C  CA  A VAL   A 100 ? 0.2396 0.2759 0.1458 -0.0337 -0.0202 0.0271  100 VAL   A CA  
2096 C  CA  B VAL   A 100 ? 0.2770 0.2118 0.2048 -0.0005 -0.0183 0.0504  100 VAL   A CA  
2097 C  C   A VAL   A 100 ? 0.2502 0.2862 0.1322 -0.0503 -0.0249 0.0506  100 VAL   A C   
2098 C  C   B VAL   A 100 ? 0.2872 0.2071 0.1961 0.0048  -0.0250 0.0486  100 VAL   A C   
2099 O  O   A VAL   A 100 ? 0.2630 0.2915 0.1617 -0.0533 -0.0119 0.0613  100 VAL   A O   
2100 O  O   B VAL   A 100 ? 0.2957 0.2018 0.1907 0.0006  -0.0277 0.0378  100 VAL   A O   
2101 C  CB  A VAL   A 100 ? 0.2630 0.2831 0.1847 -0.0366 -0.0346 0.0161  100 VAL   A CB  
2102 C  CB  B VAL   A 100 ? 0.2854 0.2303 0.2420 -0.0028 -0.0214 0.0411  100 VAL   A CB  
2103 C  CG1 A VAL   A 100 ? 0.2613 0.2934 0.2054 -0.0456 -0.0310 0.0124  100 VAL   A CG1 
2104 C  CG1 B VAL   A 100 ? 0.2896 0.2425 0.2589 -0.0039 -0.0171 0.0297  100 VAL   A CG1 
2105 C  CG2 A VAL   A 100 ? 0.2850 0.2882 0.1789 -0.0359 -0.0306 0.0271  100 VAL   A CG2 
2106 C  CG2 B VAL   A 100 ? 0.2848 0.2334 0.2508 0.0023  -0.0262 0.0391  100 VAL   A CG2 
2125 N  N   A ASN   A 101 ? 0.2509 0.2962 0.1522 -0.0588 -0.0319 0.0730  101 ASN   A N   
2126 N  N   B ASN   A 101 ? 0.2895 0.2112 0.2030 0.0091  -0.0208 0.0477  101 ASN   A N   
2127 C  CA  A ASN   A 101 ? 0.2683 0.3100 0.1832 -0.0610 -0.0345 0.0890  101 ASN   A CA  
2128 C  CA  B ASN   A 101 ? 0.2915 0.2154 0.2035 0.0129  -0.0151 0.0466  101 ASN   A CA  
2129 C  C   A ASN   A 101 ? 0.2953 0.3404 0.1943 -0.0777 -0.0098 0.1150  101 ASN   A C   
2130 C  C   B ASN   A 101 ? 0.3013 0.2323 0.2081 0.0122  0.0021  0.0566  101 ASN   A C   
2131 O  O   A ASN   A 101 ? 0.3135 0.3454 0.2477 -0.0753 -0.0106 0.1049  101 ASN   A O   
2132 O  O   B ASN   A 101 ? 0.3066 0.2367 0.1970 0.0124  0.0136  0.0682  101 ASN   A O   
2133 C  CB  A ASN   A 101 ? 0.2653 0.2961 0.1805 -0.0444 -0.0561 0.0781  101 ASN   A CB  
2134 C  CB  B ASN   A 101 ? 0.2846 0.2063 0.2000 0.0146  -0.0195 0.0435  101 ASN   A CB  
2135 C  CG  A ASN   A 101 ? 0.2641 0.2824 0.1753 -0.0326 -0.0622 0.0703  101 ASN   A CG  
2136 C  CG  B ASN   A 101 ? 0.2793 0.2103 0.2073 0.0108  -0.0212 0.0419  101 ASN   A CG  
2137 O  OD1 A ASN   A 101 ? 0.2597 0.2827 0.2058 -0.0152 -0.0640 0.0377  101 ASN   A OD1 
2138 O  OD1 B ASN   A 101 ? 0.2846 0.2178 0.2093 0.0033  -0.0204 0.0492  101 ASN   A OD1 
2139 N  ND2 A ASN   A 101 ? 0.2671 0.2755 0.1894 -0.0403 -0.0571 0.0804  101 ASN   A ND2 
2140 N  ND2 B ASN   A 101 ? 0.2722 0.2046 0.2188 0.0128  -0.0150 0.0230  101 ASN   A ND2 
2153 N  N   A LYS   A 102 ? 0.3005 0.3727 0.2213 -0.0932 0.0011  0.1129  102 LYS   A N   
2154 N  N   B LYS   A 102 ? 0.3079 0.2503 0.2384 0.0069  0.0106  0.0477  102 LYS   A N   
2155 C  CA  A LYS   A 102 ? 0.3102 0.4027 0.2357 -0.0959 0.0004  0.1036  102 LYS   A CA  
2156 C  CA  B LYS   A 102 ? 0.3145 0.2632 0.2527 -0.0005 0.0113  0.0480  102 LYS   A CA  
2157 C  C   A LYS   A 102 ? 0.3186 0.4271 0.2197 -0.0887 0.0098  0.0879  102 LYS   A C   
2158 C  C   B LYS   A 102 ? 0.3113 0.2595 0.2356 -0.0093 0.0019  0.0630  102 LYS   A C   
2159 O  O   A LYS   A 102 ? 0.3231 0.4350 0.2194 -0.0868 0.0182  0.0735  102 LYS   A O   
2160 O  O   B LYS   A 102 ? 0.3126 0.2548 0.2343 -0.0160 -0.0041 0.0686  102 LYS   A O   
2161 C  CB  A LYS   A 102 ? 0.3162 0.4062 0.2592 -0.1008 -0.0029 0.0997  102 LYS   A CB  
2162 C  CB  B LYS   A 102 ? 0.3235 0.2795 0.2887 -0.0055 0.0115  0.0289  102 LYS   A CB  
2163 C  CG  A LYS   A 102 ? 0.3210 0.4089 0.2843 -0.1019 -0.0089 0.0854  102 LYS   A CG  
2164 C  CG  B LYS   A 102 ? 0.3287 0.2909 0.3325 -0.0088 0.0112  0.0171  102 LYS   A CG  
2165 C  CD  A LYS   A 102 ? 0.3306 0.4121 0.3143 -0.1018 -0.0243 0.0672  102 LYS   A CD  
2166 C  CD  B LYS   A 102 ? 0.3322 0.3013 0.3644 -0.0114 0.0072  0.0081  102 LYS   A CD  
2167 C  CE  A LYS   A 102 ? 0.3398 0.4136 0.3334 -0.1039 -0.0338 0.0571  102 LYS   A CE  
2168 C  CE  B LYS   A 102 ? 0.3351 0.3086 0.3965 -0.0149 0.0009  -0.0001 102 LYS   A CE  
2169 N  NZ  A LYS   A 102 ? 0.3442 0.4130 0.3551 -0.1113 -0.0280 0.0503  102 LYS   A NZ  
2170 N  NZ  B LYS   A 102 ? 0.3373 0.3138 0.4152 -0.0174 0.0001  -0.0029 102 LYS   A NZ  
2197 N  N   A GLY   A 103 ? 0.3193 0.4434 0.2349 -0.0793 0.0104  0.0687  103 GLY   A N   
2198 N  N   B GLY   A 103 ? 0.3063 0.2620 0.2301 -0.0111 -0.0112 0.0646  103 GLY   A N   
2199 C  CA  A GLY   A 103 ? 0.3272 0.4532 0.2255 -0.0659 0.0151  0.0526  103 GLY   A CA  
2200 C  CA  B GLY   A 103 ? 0.3032 0.2630 0.2147 -0.0175 -0.0168 0.0708  103 GLY   A CA  
2201 C  C   A GLY   A 103 ? 0.3355 0.4613 0.2359 -0.0560 0.0231  0.0395  103 GLY   A C   
2202 C  C   B GLY   A 103 ? 0.3017 0.2615 0.1932 -0.0230 -0.0200 0.0745  103 GLY   A C   
2203 O  O   A GLY   A 103 ? 0.3502 0.4640 0.2541 -0.0521 0.0286  0.0273  103 GLY   A O   
2204 O  O   B GLY   A 103 ? 0.3054 0.2656 0.1802 -0.0267 -0.0216 0.0816  103 GLY   A O   
2211 N  N   A GLU   A 104 ? 0.3244 0.4619 0.2063 -0.0538 0.0267  0.0347  104 GLU   A N   
2212 N  N   B GLU   A 104 ? 0.2982 0.2568 0.1844 -0.0203 -0.0288 0.0677  104 GLU   A N   
2213 C  CA  A GLU   A 104 ? 0.3057 0.4555 0.1919 -0.0602 0.0272  0.0244  104 GLU   A CA  
2214 C  CA  B GLU   A 104 ? 0.2916 0.2508 0.1770 -0.0220 -0.0294 0.0538  104 GLU   A CA  
2215 C  C   A GLU   A 104 ? 0.3082 0.4650 0.1830 -0.0579 0.0320  0.0066  104 GLU   A C   
2216 C  C   B GLU   A 104 ? 0.2854 0.2431 0.1812 -0.0164 -0.0196 0.0417  104 GLU   A C   
2217 O  O   A GLU   A 104 ? 0.3029 0.4659 0.2077 -0.0587 0.0146  0.0058  104 GLU   A O   
2218 O  O   B GLU   A 104 ? 0.2816 0.2315 0.1983 -0.0163 -0.0165 0.0465  104 GLU   A O   
2219 C  CB  A GLU   A 104 ? 0.2779 0.4367 0.1650 -0.0678 0.0350  0.0457  104 GLU   A CB  
2220 C  CB  B GLU   A 104 ? 0.2907 0.2558 0.1797 -0.0260 -0.0293 0.0528  104 GLU   A CB  
2221 C  CG  A GLU   A 104 ? 0.2569 0.4161 0.1775 -0.0709 0.0250  0.0660  104 GLU   A CG  
2222 C  CG  B GLU   A 104 ? 0.2916 0.2610 0.2005 -0.0271 -0.0352 0.0546  104 GLU   A CG  
2223 C  CD  A GLU   A 104 ? 0.2353 0.3914 0.1713 -0.0716 0.0230  0.0796  104 GLU   A CD  
2224 C  CD  B GLU   A 104 ? 0.2899 0.2606 0.2104 -0.0272 -0.0409 0.0559  104 GLU   A CD  
2225 O  OE1 A GLU   A 104 ? 0.2145 0.3733 0.1347 -0.0672 0.0070  0.0773  104 GLU   A OE1 
2226 O  OE1 B GLU   A 104 ? 0.2905 0.2642 0.2142 -0.0257 -0.0478 0.0603  104 GLU   A OE1 
2227 O  OE2 A GLU   A 104 ? 0.2516 0.3854 0.1833 -0.0690 0.0236  0.0882  104 GLU   A OE2 
2228 O  OE2 B GLU   A 104 ? 0.2919 0.2574 0.2130 -0.0300 -0.0389 0.0519  104 GLU   A OE2 
2241 N  N   A ASP   A 105 ? 0.3173 0.4723 0.1942 -0.0508 0.0473  -0.0182 105 ASP   A N   
2242 N  N   B ASP   A 105 ? 0.2877 0.2472 0.1859 -0.0154 -0.0118 0.0296  105 ASP   A N   
2243 C  CA  A ASP   A 105 ? 0.3224 0.4772 0.2321 -0.0454 0.0527  -0.0429 105 ASP   A CA  
2244 C  CA  B ASP   A 105 ? 0.2901 0.2538 0.2105 -0.0077 -0.0019 0.0016  105 ASP   A CA  
2245 C  C   A ASP   A 105 ? 0.2881 0.4608 0.1952 -0.0524 0.0474  -0.0683 105 ASP   A C   
2246 C  C   B ASP   A 105 ? 0.2814 0.2480 0.1924 -0.0073 0.0006  -0.0060 105 ASP   A C   
2247 O  O   A ASP   A 105 ? 0.2704 0.4532 0.1591 -0.0503 0.0437  -0.0951 105 ASP   A O   
2248 O  O   B ASP   A 105 ? 0.2735 0.2460 0.1637 -0.0043 -0.0002 -0.0130 105 ASP   A O   
2249 C  CB  A ASP   A 105 ? 0.3545 0.4903 0.3098 -0.0346 0.0570  -0.0437 105 ASP   A CB  
2250 C  CB  B ASP   A 105 ? 0.3019 0.2645 0.2542 -0.0023 0.0033  -0.0118 105 ASP   A CB  
2251 C  CG  A ASP   A 105 ? 0.3814 0.4992 0.3781 -0.0262 0.0571  -0.0475 105 ASP   A CG  
2252 C  CG  B ASP   A 105 ? 0.3127 0.2734 0.2836 0.0057  0.0033  -0.0234 105 ASP   A CG  
2253 O  OD1 A ASP   A 105 ? 0.3856 0.5049 0.3868 -0.0297 0.0545  -0.0575 105 ASP   A OD1 
2254 O  OD1 B ASP   A 105 ? 0.3254 0.2747 0.2892 0.0064  0.0009  -0.0305 105 ASP   A OD1 
2255 O  OD2 A ASP   A 105 ? 0.4034 0.5009 0.4100 -0.0196 0.0617  -0.0391 105 ASP   A OD2 
2256 O  OD2 B ASP   A 105 ? 0.3107 0.2796 0.3153 0.0075  -0.0010 -0.0213 105 ASP   A OD2 
2265 N  N   A ILE   A 106 ? 0.2732 0.4419 0.2233 -0.0625 0.0176  -0.0646 106 ILE   A N   
2266 N  N   B ILE   A 106 ? 0.2809 0.2463 0.2051 -0.0075 -0.0008 -0.0022 106 ILE   A N   
2267 C  CA  A ILE   A 106 ? 0.2493 0.4198 0.2330 -0.0753 -0.0164 -0.0743 106 ILE   A CA  
2268 C  CA  B ILE   A 106 ? 0.2791 0.2482 0.2221 -0.0137 -0.0056 -0.0005 106 ILE   A CA  
2269 C  C   A ILE   A 106 ? 0.2307 0.3896 0.2459 -0.0952 -0.0150 -0.1001 106 ILE   A C   
2270 C  C   B ILE   A 106 ? 0.2779 0.2433 0.2093 -0.0178 -0.0034 0.0095  106 ILE   A C   
2271 O  O   A ILE   A 106 ? 0.2087 0.3789 0.2584 -0.1033 0.0047  -0.0991 106 ILE   A O   
2272 O  O   B ILE   A 106 ? 0.2772 0.2480 0.2168 -0.0180 -0.0026 0.0097  106 ILE   A O   
2273 C  CB  A ILE   A 106 ? 0.2511 0.4315 0.2812 -0.0615 -0.0387 -0.0430 106 ILE   A CB  
2274 C  CB  B ILE   A 106 ? 0.2813 0.2570 0.2541 -0.0185 -0.0156 0.0023  106 ILE   A CB  
2275 C  CG1 A ILE   A 106 ? 0.2386 0.4367 0.3021 -0.0501 -0.0479 -0.0200 106 ILE   A CG1 
2276 C  CG1 B ILE   A 106 ? 0.2826 0.2673 0.2766 -0.0162 -0.0202 0.0106  106 ILE   A CG1 
2277 C  CG2 A ILE   A 106 ? 0.2620 0.4344 0.2887 -0.0583 -0.0420 -0.0458 106 ILE   A CG2 
2278 C  CG2 B ILE   A 106 ? 0.2820 0.2561 0.2608 -0.0216 -0.0166 -0.0011 106 ILE   A CG2 
2279 C  CD1 A ILE   A 106 ? 0.2386 0.4392 0.3198 -0.0373 -0.0416 -0.0146 106 ILE   A CD1 
2280 C  CD1 B ILE   A 106 ? 0.2856 0.2728 0.2876 -0.0119 -0.0196 0.0090  106 ILE   A CD1 
2303 N  N   A GLN   A 107 ? 0.2445 0.3716 0.2684 -0.0908 -0.0054 -0.1227 107 GLN   A N   
2304 N  N   B GLN   A 107 ? 0.2772 0.2307 0.2147 -0.0172 -0.0039 0.0193  107 GLN   A N   
2305 C  CA  A GLN   A 107 ? 0.2626 0.3496 0.3458 -0.0682 0.0256  -0.1100 107 GLN   A CA  
2306 C  CA  B GLN   A 107 ? 0.2794 0.2294 0.2443 -0.0205 0.0008  0.0198  107 GLN   A CA  
2307 C  C   A GLN   A 107 ? 0.2342 0.2988 0.3216 -0.0566 0.0446  -0.0904 107 GLN   A C   
2308 C  C   B GLN   A 107 ? 0.2550 0.2021 0.2051 -0.0245 0.0025  0.0345  107 GLN   A C   
2309 O  O   A GLN   A 107 ? 0.2411 0.2986 0.3928 -0.0473 0.0554  -0.0780 107 GLN   A O   
2310 O  O   B GLN   A 107 ? 0.2509 0.1970 0.1795 -0.0280 -0.0113 0.0376  107 GLN   A O   
2311 C  CB  A GLN   A 107 ? 0.3032 0.3737 0.4322 -0.0647 0.0178  -0.1069 107 GLN   A CB  
2312 C  CB  B GLN   A 107 ? 0.3032 0.2573 0.3133 -0.0233 -0.0040 0.0116  107 GLN   A CB  
2313 C  CG  A GLN   A 107 ? 0.3378 0.3997 0.5285 -0.0602 0.0080  -0.0938 107 GLN   A CG  
2314 C  CG  B GLN   A 107 ? 0.3264 0.2837 0.3816 -0.0240 -0.0103 0.0150  107 GLN   A CG  
2315 C  CD  A GLN   A 107 ? 0.3647 0.4201 0.6062 -0.0611 0.0073  -0.0784 107 GLN   A CD  
2316 C  CD  B GLN   A 107 ? 0.3467 0.3080 0.4381 -0.0248 -0.0119 0.0178  107 GLN   A CD  
2317 O  OE1 A GLN   A 107 ? 0.3926 0.4260 0.6425 -0.0567 0.0071  -0.0741 107 GLN   A OE1 
2318 O  OE1 B GLN   A 107 ? 0.3540 0.3190 0.4571 -0.0254 -0.0114 0.0200  107 GLN   A OE1 
2319 N  NE2 A GLN   A 107 ? 0.3843 0.4324 0.6347 -0.0684 0.0082  -0.0764 107 GLN   A NE2 
2320 N  NE2 B GLN   A 107 ? 0.3518 0.3127 0.4583 -0.0263 -0.0151 0.0193  107 GLN   A NE2 
2337 N  N   A LEU   A 108 ? 0.2028 0.2445 0.2496 -0.0516 0.0403  -0.0848 108 LEU   A N   
2338 N  N   B LEU   A 108 ? 0.2360 0.1867 0.1890 -0.0291 0.0121  0.0270  108 LEU   A N   
2339 C  CA  A LEU   A 108 ? 0.1850 0.2023 0.2032 -0.0214 0.0323  -0.0449 108 LEU   A CA  
2340 C  CA  B LEU   A 108 ? 0.2189 0.1806 0.1846 -0.0233 0.0171  0.0178  108 LEU   A CA  
2341 C  C   A LEU   A 108 ? 0.1589 0.1639 0.1916 -0.0097 0.0252  -0.0129 108 LEU   A C   
2342 C  C   B LEU   A 108 ? 0.1963 0.1663 0.1803 -0.0158 0.0162  0.0211  108 LEU   A C   
2343 O  O   A LEU   A 108 ? 0.1561 0.1581 0.2063 0.0028  0.0340  0.0056  108 LEU   A O   
2344 O  O   B LEU   A 108 ? 0.1978 0.1711 0.1941 -0.0089 0.0225  0.0216  108 LEU   A O   
2345 C  CB  A LEU   A 108 ? 0.1921 0.2101 0.1900 -0.0248 0.0430  -0.0265 108 LEU   A CB  
2346 C  CB  B LEU   A 108 ? 0.2205 0.1907 0.1865 -0.0291 0.0266  0.0115  108 LEU   A CB  
2347 C  CG  A LEU   A 108 ? 0.2093 0.2370 0.2230 -0.0275 0.0577  -0.0263 108 LEU   A CG  
2348 C  CG  B LEU   A 108 ? 0.2257 0.2077 0.2087 -0.0320 0.0379  -0.0001 108 LEU   A CG  
2349 C  CD1 A LEU   A 108 ? 0.2275 0.2439 0.2231 -0.0343 0.0660  -0.0187 108 LEU   A CD1 
2350 C  CD1 B LEU   A 108 ? 0.2328 0.2135 0.2068 -0.0340 0.0468  -0.0012 108 LEU   A CD1 
2351 C  CD2 A LEU   A 108 ? 0.2120 0.2544 0.2763 -0.0276 0.0520  -0.0199 108 LEU   A CD2 
2352 C  CD2 B LEU   A 108 ? 0.2240 0.2173 0.2331 -0.0344 0.0384  -0.0011 108 LEU   A CD2 
2375 N  N   A LEU   A 109 ? 0.1480 0.1550 0.1963 -0.0022 0.0170  -0.0038 109 LEU   A N   
2376 N  N   B LEU   A 109 ? 0.1769 0.1577 0.1631 -0.0103 0.0116  0.0249  109 LEU   A N   
2377 C  CA  A LEU   A 109 ? 0.1457 0.1406 0.1863 -0.0026 0.0078  0.0020  109 LEU   A CA  
2378 C  CA  B LEU   A 109 ? 0.1592 0.1477 0.1531 -0.0094 0.0070  0.0267  109 LEU   A CA  
2379 C  C   A LEU   A 109 ? 0.1430 0.1351 0.1798 -0.0065 0.0129  -0.0029 109 LEU   A C   
2380 C  C   B LEU   A 109 ? 0.1525 0.1459 0.1460 -0.0129 0.0064  0.0190  109 LEU   A C   
2381 O  O   A LEU   A 109 ? 0.1525 0.1318 0.1895 -0.0009 0.0064  -0.0040 109 LEU   A O   
2382 O  O   B LEU   A 109 ? 0.1534 0.1471 0.1445 -0.0053 0.0058  0.0170  109 LEU   A O   
2383 C  CB  A LEU   A 109 ? 0.1544 0.1438 0.1997 0.0109  -0.0068 0.0105  109 LEU   A CB  
2384 C  CB  B LEU   A 109 ? 0.1497 0.1417 0.1560 -0.0057 0.0032  0.0249  109 LEU   A CB  
2385 C  CG  A LEU   A 109 ? 0.1553 0.1537 0.2128 -0.0023 -0.0023 0.0181  109 LEU   A CG  
2386 C  CG  B LEU   A 109 ? 0.1399 0.1413 0.1516 -0.0067 0.0023  0.0236  109 LEU   A CG  
2387 C  CD1 A LEU   A 109 ? 0.1555 0.1511 0.2193 0.0018  -0.0009 -0.0072 109 LEU   A CD1 
2388 C  CD1 B LEU   A 109 ? 0.1396 0.1391 0.1517 -0.0044 -0.0107 0.0136  109 LEU   A CD1 
2389 C  CD2 A LEU   A 109 ? 0.1561 0.1607 0.2478 -0.0081 -0.0152 0.0299  109 LEU   A CD2 
2390 C  CD2 B LEU   A 109 ? 0.1290 0.1314 0.1567 -0.0114 0.0083  0.0164  109 LEU   A CD2 
2413 N  N   A LYS   A 110 ? 0.1386 0.1377 0.1726 0.0027  -0.0060 -0.0068 110 LYS   A N   
2414 N  N   B LYS   A 110 ? 0.1481 0.1495 0.1539 -0.0132 -0.0007 0.0162  110 LYS   A N   
2415 C  CA  A LYS   A 110 ? 0.1451 0.1309 0.1684 0.0018  -0.0122 0.0047  110 LYS   A CA  
2416 C  CA  B LYS   A 110 ? 0.1477 0.1479 0.1632 -0.0198 -0.0049 0.0160  110 LYS   A CA  
2417 C  C   A LYS   A 110 ? 0.1431 0.1261 0.1624 0.0024  -0.0029 0.0032  110 LYS   A C   
2418 C  C   B LYS   A 110 ? 0.1427 0.1474 0.1635 -0.0190 -0.0005 0.0066  110 LYS   A C   
2419 O  O   A LYS   A 110 ? 0.1342 0.1274 0.1821 0.0024  0.0028  0.0054  110 LYS   A O   
2420 O  O   B LYS   A 110 ? 0.1395 0.1434 0.1819 -0.0176 0.0006  0.0103  110 LYS   A O   
2421 C  CB  A LYS   A 110 ? 0.1472 0.1350 0.1942 0.0017  -0.0193 -0.0057 110 LYS   A CB  
2422 C  CB  B LYS   A 110 ? 0.1518 0.1510 0.1779 -0.0181 -0.0129 0.0113  110 LYS   A CB  
2423 C  CG  A LYS   A 110 ? 0.1540 0.1333 0.2228 0.0059  -0.0171 -0.0009 110 LYS   A CG  
2424 C  CG  B LYS   A 110 ? 0.1571 0.1535 0.1897 -0.0119 -0.0197 0.0107  110 LYS   A CG  
2425 C  CD  A LYS   A 110 ? 0.1574 0.1401 0.2265 -0.0007 -0.0040 -0.0097 110 LYS   A CD  
2426 C  CD  B LYS   A 110 ? 0.1625 0.1596 0.1907 -0.0106 -0.0233 0.0094  110 LYS   A CD  
2427 C  CE  A LYS   A 110 ? 0.1616 0.1471 0.2552 -0.0087 0.0177  -0.0170 110 LYS   A CE  
2428 C  CE  B LYS   A 110 ? 0.1678 0.1638 0.2057 -0.0127 -0.0139 0.0074  110 LYS   A CE  
2429 N  NZ  A LYS   A 110 ? 0.1632 0.1459 0.2666 -0.0190 0.0321  -0.0113 110 LYS   A NZ  
2430 N  NZ  B LYS   A 110 ? 0.1739 0.1662 0.2094 -0.0143 -0.0064 0.0090  110 LYS   A NZ  
2457 N  N   A SER   A 111 ? 0.1490 0.1281 0.1655 0.0062  0.0030  0.0054  111 SER   A N   
2458 N  N   B SER   A 111 ? 0.1416 0.1542 0.1452 -0.0171 -0.0024 -0.0035 111 SER   A N   
2459 C  CA  A SER   A 111 ? 0.1404 0.1372 0.1807 0.0035  0.0040  -0.0014 111 SER   A CA  
2460 C  CA  B SER   A 111 ? 0.1389 0.1602 0.1317 -0.0133 -0.0027 -0.0149 111 SER   A CA  
2461 C  C   A SER   A 111 ? 0.1319 0.1305 0.1788 -0.0065 0.0104  0.0017  111 SER   A C   
2462 C  C   B SER   A 111 ? 0.1362 0.1532 0.1412 -0.0212 -0.0072 -0.0064 111 SER   A C   
2463 O  O   A SER   A 111 ? 0.1478 0.1194 0.1992 0.0013  0.0143  0.0071  111 SER   A O   
2464 O  O   B SER   A 111 ? 0.1429 0.1504 0.1492 -0.0228 -0.0102 -0.0053 111 SER   A O   
2465 C  CB  A SER   A 111 ? 0.1594 0.1497 0.2148 -0.0029 0.0103  -0.0135 111 SER   A CB  
2466 C  CB  B SER   A 111 ? 0.1503 0.1748 0.1341 -0.0097 0.0155  -0.0273 111 SER   A CB  
2467 O  OG  A SER   A 111 ? 0.2062 0.1783 0.2216 0.0031  0.0131  -0.0203 111 SER   A OG  
2468 O  OG  B SER   A 111 ? 0.1760 0.1921 0.1286 -0.0032 0.0241  -0.0357 111 SER   A OG  
2479 N  N   A ALA   A 112 ? 0.1340 0.1290 0.1808 0.0023  0.0166  -0.0046 112 ALA   A N   
2480 N  N   B ALA   A 112 ? 0.1413 0.1529 0.1531 -0.0187 0.0013  0.0002  112 ALA   A N   
2481 C  CA  A ALA   A 112 ? 0.1344 0.1224 0.1644 0.0009  0.0177  -0.0060 112 ALA   A CA  
2482 C  CA  B ALA   A 112 ? 0.1412 0.1461 0.1569 -0.0244 0.0100  0.0012  112 ALA   A CA  
2483 C  C   A ALA   A 112 ? 0.1311 0.1219 0.1794 0.0078  0.0090  0.0124  112 ALA   A C   
2484 C  C   B ALA   A 112 ? 0.1352 0.1389 0.1433 -0.0197 0.0044  0.0087  112 ALA   A C   
2485 O  O   A ALA   A 112 ? 0.1384 0.1206 0.1857 -0.0079 0.0099  0.0088  112 ALA   A O   
2486 O  O   B ALA   A 112 ? 0.1377 0.1367 0.1291 -0.0285 0.0106  0.0188  112 ALA   A O   
2487 C  CB  A ALA   A 112 ? 0.1452 0.1224 0.1638 -0.0039 0.0106  -0.0072 112 ALA   A CB  
2488 C  CB  B ALA   A 112 ? 0.1486 0.1502 0.1644 -0.0301 0.0185  -0.0040 112 ALA   A CB  
2499 N  N   A TYR   A 113 ? 0.1286 0.1308 0.1873 -0.0033 0.0101  0.0162  113 TYR   A N   
2500 N  N   B TYR   A 113 ? 0.1313 0.1362 0.1396 -0.0127 0.0036  0.0077  113 TYR   A N   
2501 C  CA  A TYR   A 113 ? 0.1335 0.1279 0.1806 -0.0036 0.0062  0.0135  113 TYR   A CA  
2502 C  CA  B TYR   A 113 ? 0.1321 0.1299 0.1507 -0.0097 0.0065  0.0093  113 TYR   A CA  
2503 C  C   A TYR   A 113 ? 0.1308 0.1216 0.1621 -0.0054 0.0060  0.0086  113 TYR   A C   
2504 C  C   B TYR   A 113 ? 0.1316 0.1272 0.1544 -0.0088 0.0079  0.0111  113 TYR   A C   
2505 O  O   A TYR   A 113 ? 0.1381 0.1251 0.1770 -0.0015 0.0144  0.0030  113 TYR   A O   
2506 O  O   B TYR   A 113 ? 0.1339 0.1298 0.1630 -0.0117 0.0156  0.0170  113 TYR   A O   
2507 C  CB  A TYR   A 113 ? 0.1343 0.1347 0.1815 -0.0153 -0.0024 0.0152  113 TYR   A CB  
2508 C  CB  B TYR   A 113 ? 0.1323 0.1284 0.1522 -0.0118 0.0066  0.0070  113 TYR   A CB  
2509 C  CG  A TYR   A 113 ? 0.1300 0.1380 0.1571 -0.0089 0.0106  0.0176  113 TYR   A CG  
2510 C  CG  B TYR   A 113 ? 0.1305 0.1182 0.1450 -0.0060 0.0054  0.0124  113 TYR   A CG  
2511 C  CD1 A TYR   A 113 ? 0.1367 0.1505 0.1494 -0.0065 0.0089  0.0144  113 TYR   A CD1 
2512 C  CD1 B TYR   A 113 ? 0.1326 0.1193 0.1427 0.0016  0.0046  0.0113  113 TYR   A CD1 
2513 C  CD2 A TYR   A 113 ? 0.1384 0.1375 0.1458 -0.0110 0.0063  0.0129  113 TYR   A CD2 
2514 C  CD2 B TYR   A 113 ? 0.1398 0.1137 0.1420 -0.0082 -0.0090 0.0176  113 TYR   A CD2 
2515 C  CE1 A TYR   A 113 ? 0.1365 0.1464 0.1550 -0.0159 0.0115  0.0106  113 TYR   A CE1 
2516 C  CE1 B TYR   A 113 ? 0.1406 0.1173 0.1504 0.0024  0.0000  0.0187  113 TYR   A CE1 
2517 C  CE2 A TYR   A 113 ? 0.1353 0.1479 0.1488 -0.0101 0.0023  0.0094  113 TYR   A CE2 
2518 C  CE2 B TYR   A 113 ? 0.1418 0.1161 0.1522 -0.0024 -0.0107 0.0134  113 TYR   A CE2 
2519 C  CZ  A TYR   A 113 ? 0.1385 0.1427 0.1423 -0.0082 0.0039  0.0091  113 TYR   A CZ  
2520 C  CZ  B TYR   A 113 ? 0.1451 0.1199 0.1435 0.0072  -0.0096 0.0106  113 TYR   A CZ  
2521 O  OH  A TYR   A 113 ? 0.1356 0.1524 0.1561 0.0009  0.0069  0.0097  113 TYR   A OH  
2522 O  OH  B TYR   A 113 ? 0.1500 0.1192 0.1205 0.0153  -0.0219 -0.0101 113 TYR   A OH  
2541 N  N   . GLU   A 114 ? 0.1337 0.1292 0.1668 -0.0041 0.0099  0.0138  114 GLU   A N   
2542 C  CA  . GLU   A 114 ? 0.1388 0.1220 0.1911 0.0061  0.0046  0.0154  114 GLU   A CA  
2543 C  C   . GLU   A 114 ? 0.1223 0.1282 0.1851 0.0027  0.0126  0.0082  114 GLU   A C   
2544 O  O   . GLU   A 114 ? 0.1311 0.1309 0.1823 -0.0001 0.0000  0.0112  114 GLU   A O   
2545 C  CB  . GLU   A 114 ? 0.1350 0.1269 0.1928 -0.0070 0.0102  0.0085  114 GLU   A CB  
2546 C  CG  . GLU   A 114 ? 0.1427 0.1315 0.1874 0.0020  0.0132  0.0016  114 GLU   A CG  
2547 C  CD  . GLU   A 114 ? 0.1523 0.1297 0.1950 -0.0029 0.0026  -0.0004 114 GLU   A CD  
2548 O  OE1 . GLU   A 114 ? 0.1524 0.1284 0.1964 -0.0128 0.0143  -0.0038 114 GLU   A OE1 
2549 O  OE2 . GLU   A 114 ? 0.1745 0.1431 0.2118 -0.0074 0.0105  -0.0190 114 GLU   A OE2 
2557 N  N   . ASN   A 115 ? 0.1304 0.1301 0.1659 -0.0055 0.0075  0.0076  115 ASN   A N   
2558 C  CA  . ASN   A 115 ? 0.1356 0.1332 0.1808 -0.0107 0.0116  0.0138  115 ASN   A CA  
2559 C  C   . ASN   A 115 ? 0.1359 0.1232 0.1687 -0.0150 0.0036  0.0117  115 ASN   A C   
2560 O  O   . ASN   A 115 ? 0.1382 0.1451 0.1647 -0.0111 0.0094  0.0149  115 ASN   A O   
2561 C  CB  . ASN   A 115 ? 0.1456 0.1404 0.1692 -0.0188 0.0129  0.0019  115 ASN   A CB  
2562 C  CG  . ASN   A 115 ? 0.1378 0.1614 0.1694 -0.0198 0.0153  0.0060  115 ASN   A CG  
2563 O  OD1 . ASN   A 115 ? 0.1458 0.2612 0.1814 -0.0189 0.0191  0.0289  115 ASN   A OD1 
2564 N  ND2 . ASN   A 115 ? 0.1394 0.1414 0.1752 -0.0139 0.0205  0.0001  115 ASN   A ND2 
2571 N  N   . PHE   A 116 ? 0.1299 0.1330 0.1709 -0.0017 0.0108  0.0209  116 PHE   A N   
2572 C  CA  . PHE   A 116 ? 0.1321 0.1442 0.1587 -0.0019 0.0137  0.0215  116 PHE   A CA  
2573 C  C   . PHE   A 116 ? 0.1292 0.1462 0.1755 -0.0068 0.0185  0.0272  116 PHE   A C   
2574 O  O   . PHE   A 116 ? 0.1392 0.1529 0.1773 -0.0037 0.0139  0.0326  116 PHE   A O   
2575 C  CB  . PHE   A 116 ? 0.1316 0.1368 0.1719 -0.0046 0.0149  0.0201  116 PHE   A CB  
2576 C  CG  . PHE   A 116 ? 0.1371 0.1388 0.1632 -0.0103 0.0127  0.0155  116 PHE   A CG  
2577 C  CD1 . PHE   A 116 ? 0.1329 0.1302 0.1562 -0.0091 0.0150  0.0047  116 PHE   A CD1 
2578 C  CD2 . PHE   A 116 ? 0.1388 0.1446 0.1663 -0.0089 0.0182  0.0193  116 PHE   A CD2 
2579 C  CE1 . PHE   A 116 ? 0.1418 0.1287 0.1730 -0.0177 0.0121  0.0134  116 PHE   A CE1 
2580 C  CE2 . PHE   A 116 ? 0.1400 0.1402 0.1692 -0.0072 0.0140  0.0082  116 PHE   A CE2 
2581 C  CZ  . PHE   A 116 ? 0.1437 0.1253 0.1643 -0.0073 0.0052  0.0119  116 PHE   A CZ  
2591 N  N   A ASN   A 117 ? 0.1236 0.1358 0.1955 -0.0018 0.0167  0.0271  117 ASN   A N   
2592 N  N   B ASN   A 117 ? 0.1282 0.1445 0.1788 -0.0044 0.0106  0.0258  117 ASN   A N   
2593 C  CA  A ASN   A 117 ? 0.1326 0.1396 0.2017 -0.0049 0.0180  0.0313  117 ASN   A CA  
2594 C  CA  B ASN   A 117 ? 0.1331 0.1474 0.1787 -0.0071 0.0018  0.0248  117 ASN   A CA  
2595 C  C   A ASN   A 117 ? 0.1354 0.1462 0.2026 -0.0021 0.0189  0.0311  117 ASN   A C   
2596 C  C   B ASN   A 117 ? 0.1399 0.1488 0.1797 -0.0048 -0.0009 0.0306  117 ASN   A C   
2597 O  O   A ASN   A 117 ? 0.1402 0.1526 0.2236 -0.0069 -0.0050 0.0352  117 ASN   A O   
2598 O  O   B ASN   A 117 ? 0.1442 0.1443 0.2012 -0.0059 -0.0128 0.0443  117 ASN   A O   
2599 C  CB  A ASN   A 117 ? 0.1322 0.1421 0.1915 -0.0067 0.0216  0.0377  117 ASN   A CB  
2600 C  CB  B ASN   A 117 ? 0.1288 0.1511 0.1719 -0.0102 -0.0031 0.0211  117 ASN   A CB  
2601 C  CG  A ASN   A 117 ? 0.1382 0.1383 0.2035 -0.0062 0.0250  0.0392  117 ASN   A CG  
2602 C  CG  B ASN   A 117 ? 0.1280 0.1520 0.1767 -0.0136 -0.0080 0.0165  117 ASN   A CG  
2603 O  OD1 A ASN   A 117 ? 0.1432 0.1513 0.2197 -0.0101 0.0248  0.0328  117 ASN   A OD1 
2604 O  OD1 B ASN   A 117 ? 0.1228 0.1576 0.1847 -0.0192 -0.0224 0.0207  117 ASN   A OD1 
2605 N  ND2 A ASN   A 117 ? 0.1337 0.1370 0.2098 -0.0006 0.0188  0.0336  117 ASN   A ND2 
2606 N  ND2 B ASN   A 117 ? 0.1270 0.1510 0.1725 -0.0128 -0.0058 0.0076  117 ASN   A ND2 
2619 N  N   A GLN   A 118 ? 0.1323 0.1459 0.2041 -0.0090 0.0005  0.0341  118 GLN   A N   
2620 N  N   B GLN   A 118 ? 0.1401 0.1553 0.1800 -0.0074 -0.0075 0.0252  118 GLN   A N   
2621 C  CA  A GLN   A 118 ? 0.1404 0.1559 0.2073 -0.0105 -0.0023 0.0366  118 GLN   A CA  
2622 C  CA  B GLN   A 118 ? 0.1461 0.1663 0.1770 -0.0084 -0.0046 0.0217  118 GLN   A CA  
2623 C  C   A GLN   A 118 ? 0.1397 0.1615 0.2089 -0.0122 -0.0041 0.0361  118 GLN   A C   
2624 C  C   B GLN   A 118 ? 0.1460 0.1667 0.1682 -0.0078 -0.0038 0.0282  118 GLN   A C   
2625 O  O   A GLN   A 118 ? 0.1362 0.1810 0.2283 -0.0050 -0.0179 0.0211  118 GLN   A O   
2626 O  O   B GLN   A 118 ? 0.1440 0.1737 0.1773 -0.0061 -0.0216 0.0332  118 GLN   A O   
2627 C  CB  A GLN   A 118 ? 0.1353 0.1596 0.2143 -0.0062 0.0063  0.0316  118 GLN   A CB  
2628 C  CB  B GLN   A 118 ? 0.1438 0.1704 0.1811 -0.0045 -0.0002 0.0154  118 GLN   A CB  
2629 C  CG  A GLN   A 118 ? 0.1345 0.1637 0.2043 -0.0035 0.0061  0.0390  118 GLN   A CG  
2630 C  CG  B GLN   A 118 ? 0.1414 0.1736 0.1723 -0.0036 0.0024  0.0180  118 GLN   A CG  
2631 C  CD  A GLN   A 118 ? 0.1369 0.1710 0.2296 0.0004  0.0029  0.0265  118 GLN   A CD  
2632 C  CD  B GLN   A 118 ? 0.1406 0.1747 0.1811 -0.0008 0.0049  0.0184  118 GLN   A CD  
2633 O  OE1 A GLN   A 118 ? 0.1400 0.1759 0.2510 0.0069  -0.0052 0.0123  118 GLN   A OE1 
2634 O  OE1 B GLN   A 118 ? 0.1422 0.1743 0.1858 0.0027  0.0107  0.0222  118 GLN   A OE1 
2635 N  NE2 A GLN   A 118 ? 0.1440 0.1663 0.2359 0.0046  0.0109  0.0311  118 GLN   A NE2 
2636 N  NE2 B GLN   A 118 ? 0.1429 0.1740 0.1830 0.0033  0.0012  0.0181  118 GLN   A NE2 
2653 N  N   A HIS   A 119 ? 0.1436 0.1625 0.2021 -0.0101 -0.0068 0.0411  119 HIS   A N   
2654 N  N   B HIS   A 119 ? 0.1507 0.1685 0.1608 -0.0045 0.0051  0.0295  119 HIS   A N   
2655 C  CA  A HIS   A 119 ? 0.1458 0.1721 0.1908 -0.0028 -0.0114 0.0520  119 HIS   A CA  
2656 C  CA  B HIS   A 119 ? 0.1563 0.1805 0.1565 0.0011  0.0163  0.0276  119 HIS   A CA  
2657 C  C   A HIS   A 119 ? 0.1586 0.1845 0.1890 -0.0116 -0.0208 0.0618  119 HIS   A C   
2658 C  C   B HIS   A 119 ? 0.1671 0.1866 0.1625 0.0030  0.0240  0.0274  119 HIS   A C   
2659 O  O   A HIS   A 119 ? 0.1642 0.1943 0.1925 -0.0324 -0.0267 0.0586  119 HIS   A O   
2660 O  O   B HIS   A 119 ? 0.1668 0.1933 0.1642 -0.0054 0.0203  0.0249  119 HIS   A O   
2661 C  CB  A HIS   A 119 ? 0.1518 0.1712 0.1864 -0.0028 0.0020  0.0441  119 HIS   A CB  
2662 C  CB  B HIS   A 119 ? 0.1575 0.1875 0.1424 -0.0027 0.0203  0.0227  119 HIS   A CB  
2663 C  CG  A HIS   A 119 ? 0.1542 0.1700 0.2043 0.0038  -0.0026 0.0365  119 HIS   A CG  
2664 C  CG  B HIS   A 119 ? 0.1493 0.1914 0.1340 -0.0095 0.0080  0.0265  119 HIS   A CG  
2665 N  ND1 A HIS   A 119 ? 0.1728 0.1883 0.2552 -0.0134 -0.0121 0.0117  119 HIS   A ND1 
2666 N  ND1 B HIS   A 119 ? 0.1527 0.1975 0.1378 -0.0169 0.0056  0.0245  119 HIS   A ND1 
2667 C  CD2 A HIS   A 119 ? 0.1562 0.1704 0.2160 0.0047  0.0089  0.0378  119 HIS   A CD2 
2668 C  CD2 B HIS   A 119 ? 0.1429 0.1932 0.1336 -0.0112 -0.0004 0.0342  119 HIS   A CD2 
2669 C  CE1 A HIS   A 119 ? 0.1609 0.1762 0.2526 -0.0205 -0.0042 0.0295  119 HIS   A CE1 
2670 C  CE1 B HIS   A 119 ? 0.1469 0.1958 0.1444 -0.0227 0.0071  0.0349  119 HIS   A CE1 
2671 N  NE2 A HIS   A 119 ? 0.1672 0.1677 0.2402 -0.0121 0.0217  0.0341  119 HIS   A NE2 
2672 N  NE2 B HIS   A 119 ? 0.1434 0.1950 0.1449 -0.0234 -0.0064 0.0364  119 HIS   A NE2 
2687 N  N   A GLU   A 120 ? 0.1602 0.1994 0.2037 -0.0064 -0.0321 0.0777  120 GLU   A N   
2688 N  N   B GLU   A 120 ? 0.1769 0.1888 0.1741 0.0075  0.0340  0.0296  120 GLU   A N   
2689 C  CA  A GLU   A 120 ? 0.1788 0.2131 0.2229 -0.0056 -0.0239 0.1080  120 GLU   A CA  
2690 C  CA  B GLU   A 120 ? 0.1879 0.1875 0.2016 0.0084  0.0357  0.0372  120 GLU   A CA  
2691 C  C   A GLU   A 120 ? 0.1651 0.2114 0.1911 -0.0134 -0.0148 0.0941  120 GLU   A C   
2692 C  C   B GLU   A 120 ? 0.1783 0.1615 0.1636 0.0048  0.0356  0.0329  120 GLU   A C   
2693 O  O   A GLU   A 120 ? 0.1751 0.2175 0.1833 -0.0186 -0.0186 0.0737  120 GLU   A O   
2694 O  O   B GLU   A 120 ? 0.1747 0.1494 0.1363 0.0046  0.0372  0.0384  120 GLU   A O   
2695 C  CB  A GLU   A 120 ? 0.2236 0.2492 0.2710 -0.0009 -0.0198 0.1317  120 GLU   A CB  
2696 C  CB  B GLU   A 120 ? 0.2146 0.2209 0.2737 0.0148  0.0347  0.0482  120 GLU   A CB  
2697 C  CG  A GLU   A 120 ? 0.2613 0.2736 0.3458 0.0076  -0.0164 0.1351  120 GLU   A CG  
2698 C  CG  B GLU   A 120 ? 0.2401 0.2483 0.3475 0.0192  0.0362  0.0494  120 GLU   A CG  
2699 C  CD  A GLU   A 120 ? 0.3254 0.3033 0.4162 0.0163  -0.0106 0.1138  120 GLU   A CD  
2700 C  CD  B GLU   A 120 ? 0.2619 0.2730 0.4025 0.0236  0.0402  0.0464  120 GLU   A CD  
2701 O  OE1 A GLU   A 120 ? 0.3662 0.3248 0.4501 0.0164  -0.0140 0.1027  120 GLU   A OE1 
2702 O  OE1 B GLU   A 120 ? 0.2757 0.2824 0.4288 0.0205  0.0414  0.0433  120 GLU   A OE1 
2703 O  OE2 A GLU   A 120 ? 0.3647 0.3202 0.4630 0.0198  -0.0145 0.1094  120 GLU   A OE2 
2704 O  OE2 B GLU   A 120 ? 0.2694 0.2913 0.4263 0.0234  0.0418  0.0474  120 GLU   A OE2 
2717 N  N   A VAL   A 121 ? 0.1591 0.2101 0.1827 -0.0119 -0.0083 0.0899  121 VAL   A N   
2718 N  N   B VAL   A 121 ? 0.1787 0.1594 0.1432 0.0021  0.0273  0.0296  121 VAL   A N   
2719 C  CA  A VAL   A 121 ? 0.1694 0.2122 0.1703 -0.0175 0.0128  0.0845  121 VAL   A CA  
2720 C  CA  B VAL   A 121 ? 0.1832 0.1645 0.1426 -0.0003 0.0242  0.0217  121 VAL   A CA  
2721 C  C   A VAL   A 121 ? 0.1570 0.1915 0.1473 -0.0180 0.0035  0.0587  121 VAL   A C   
2722 C  C   B VAL   A 121 ? 0.1702 0.1526 0.1409 -0.0133 0.0169  0.0189  121 VAL   A C   
2723 O  O   A VAL   A 121 ? 0.1596 0.1849 0.1646 -0.0176 -0.0034 0.0528  121 VAL   A O   
2724 O  O   B VAL   A 121 ? 0.1698 0.1488 0.1617 -0.0223 0.0065  0.0147  121 VAL   A O   
2725 C  CB  A VAL   A 121 ? 0.2044 0.2414 0.2084 -0.0191 0.0237  0.0823  121 VAL   A CB  
2726 C  CB  B VAL   A 121 ? 0.2065 0.1878 0.1701 0.0109  0.0220  0.0182  121 VAL   A CB  
2727 C  CG1 A VAL   A 121 ? 0.2117 0.2599 0.2027 -0.0150 0.0282  0.0766  121 VAL   A CG1 
2728 C  CG1 B VAL   A 121 ? 0.2094 0.1991 0.1648 0.0122  0.0250  0.0210  121 VAL   A CG1 
2729 C  CG2 A VAL   A 121 ? 0.2180 0.2471 0.2462 -0.0402 0.0224  0.0692  121 VAL   A CG2 
2730 C  CG2 B VAL   A 121 ? 0.2226 0.1992 0.1976 0.0084  0.0153  0.0058  121 VAL   A CG2 
2749 N  N   A LEU   A 122 ? 0.1451 0.1708 0.1501 -0.0176 -0.0007 0.0418  122 LEU   A N   
2750 N  N   B LEU   A 122 ? 0.1640 0.1487 0.1467 -0.0137 0.0175  0.0348  122 LEU   A N   
2751 C  CA  A LEU   A 122 ? 0.1498 0.1555 0.1407 -0.0104 0.0115  0.0328  122 LEU   A CA  
2752 C  CA  B LEU   A 122 ? 0.1627 0.1473 0.1452 -0.0159 0.0292  0.0351  122 LEU   A CA  
2753 C  C   A LEU   A 122 ? 0.1467 0.1563 0.1340 -0.0160 0.0028  0.0284  122 LEU   A C   
2754 C  C   B LEU   A 122 ? 0.1526 0.1335 0.1355 -0.0086 0.0149  0.0235  122 LEU   A C   
2755 O  O   A LEU   A 122 ? 0.1469 0.1635 0.1800 -0.0221 0.0036  0.0251  122 LEU   A O   
2756 O  O   B LEU   A 122 ? 0.1492 0.1364 0.1288 -0.0098 0.0057  0.0139  122 LEU   A O   
2757 C  CB  A LEU   A 122 ? 0.1530 0.1581 0.1796 0.0034  0.0045  0.0496  122 LEU   A CB  
2758 C  CB  B LEU   A 122 ? 0.1745 0.1605 0.1816 -0.0196 0.0248  0.0398  122 LEU   A CB  
2759 C  CG  A LEU   A 122 ? 0.1409 0.1658 0.1688 0.0055  0.0163  0.0324  122 LEU   A CG  
2760 C  CG  B LEU   A 122 ? 0.1755 0.1761 0.1922 -0.0244 0.0076  0.0314  122 LEU   A CG  
2761 C  CD1 A LEU   A 122 ? 0.1560 0.1667 0.1729 -0.0050 0.0151  0.0352  122 LEU   A CD1 
2762 C  CD1 B LEU   A 122 ? 0.1714 0.1829 0.1942 -0.0277 0.0042  0.0346  122 LEU   A CD1 
2763 C  CD2 A LEU   A 122 ? 0.1371 0.1665 0.1758 0.0069  0.0307  0.0304  122 LEU   A CD2 
2764 C  CD2 B LEU   A 122 ? 0.1724 0.1743 0.1878 -0.0296 -0.0040 0.0294  122 LEU   A CD2 
2787 N  N   A LEU   A 123 ? 0.1407 0.1536 0.1333 -0.0175 -0.0002 0.0259  123 LEU   A N   
2788 N  N   B LEU   A 123 ? 0.1487 0.1305 0.1384 -0.0054 0.0061  0.0162  123 LEU   A N   
2789 C  CA  A LEU   A 123 ? 0.1411 0.1536 0.1246 -0.0103 0.0007  0.0245  123 LEU   A CA  
2790 C  CA  B LEU   A 123 ? 0.1444 0.1361 0.1321 -0.0080 0.0134  0.0240  123 LEU   A CA  
2791 C  C   A LEU   A 123 ? 0.1363 0.1537 0.1209 -0.0087 0.0044  0.0320  123 LEU   A C   
2792 C  C   B LEU   A 123 ? 0.1417 0.1224 0.1260 -0.0101 0.0122  0.0189  123 LEU   A C   
2793 O  O   A LEU   A 123 ? 0.1332 0.1673 0.1351 -0.0115 -0.0017 0.0252  123 LEU   A O   
2794 O  O   B LEU   A 123 ? 0.1338 0.1186 0.1247 -0.0114 0.0088  0.0286  123 LEU   A O   
2795 C  CB  A LEU   A 123 ? 0.1565 0.1602 0.1403 -0.0173 0.0030  0.0194  123 LEU   A CB  
2796 C  CB  B LEU   A 123 ? 0.1412 0.1504 0.1246 -0.0047 0.0262  0.0276  123 LEU   A CB  
2797 C  CG  A LEU   A 123 ? 0.1623 0.1739 0.1700 -0.0069 0.0085  0.0108  123 LEU   A CG  
2798 C  CG  B LEU   A 123 ? 0.1486 0.1673 0.1310 -0.0031 0.0218  0.0203  123 LEU   A CG  
2799 C  CD1 A LEU   A 123 ? 0.1662 0.1895 0.1731 -0.0105 0.0120  0.0085  123 LEU   A CD1 
2800 C  CD1 B LEU   A 123 ? 0.1573 0.1783 0.1360 -0.0004 0.0227  0.0122  123 LEU   A CD1 
2801 C  CD2 A LEU   A 123 ? 0.1637 0.1775 0.1694 0.0010  0.0170  0.0091  123 LEU   A CD2 
2802 C  CD2 B LEU   A 123 ? 0.1408 0.1748 0.1246 -0.0007 0.0199  0.0116  123 LEU   A CD2 
2825 N  N   A ALA   A 124 ? 0.1398 0.1403 0.1143 -0.0081 -0.0029 0.0244  124 ALA   A N   
2826 N  N   B ALA   A 124 ? 0.1386 0.1178 0.1184 -0.0116 0.0156  -0.0066 124 ALA   A N   
2827 C  CA  A ALA   A 124 ? 0.1336 0.1402 0.1237 -0.0041 -0.0078 0.0265  124 ALA   A CA  
2828 C  CA  B ALA   A 124 ? 0.1381 0.1274 0.1281 -0.0178 0.0136  -0.0014 124 ALA   A CA  
2829 C  C   A ALA   A 124 ? 0.1269 0.1428 0.1280 -0.0100 0.0020  0.0322  124 ALA   A C   
2830 C  C   B ALA   A 124 ? 0.1389 0.1417 0.1178 -0.0148 0.0047  0.0109  124 ALA   A C   
2831 O  O   A ALA   A 124 ? 0.1271 0.1531 0.1492 -0.0223 0.0196  0.0376  124 ALA   A O   
2832 O  O   B ALA   A 124 ? 0.1395 0.1545 0.1216 -0.0025 -0.0022 0.0093  124 ALA   A O   
2833 C  CB  A ALA   A 124 ? 0.1417 0.1257 0.1430 -0.0027 0.0022  0.0190  124 ALA   A CB  
2834 C  CB  B ALA   A 124 ? 0.1474 0.1230 0.1386 -0.0216 0.0220  -0.0052 124 ALA   A CB  
2845 N  N   A PRO   A 125 ? 0.1269 0.1429 0.1424 -0.0032 0.0023  0.0356  125 PRO   A N   
2846 N  N   B PRO   A 125 ? 0.1362 0.1334 0.1067 -0.0159 0.0038  0.0227  125 PRO   A N   
2847 C  CA  A PRO   A 125 ? 0.1372 0.1463 0.1384 -0.0007 0.0045  0.0284  125 PRO   A CA  
2848 C  CA  B PRO   A 125 ? 0.1435 0.1377 0.1142 -0.0171 0.0055  0.0192  125 PRO   A CA  
2849 C  C   A PRO   A 125 ? 0.1301 0.1443 0.1449 0.0001  0.0085  0.0260  125 PRO   A C   
2850 C  C   B PRO   A 125 ? 0.1466 0.1478 0.1347 -0.0137 0.0042  0.0137  125 PRO   A C   
2851 O  O   A PRO   A 125 ? 0.1337 0.1387 0.1360 0.0027  0.0024  0.0221  125 PRO   A O   
2852 O  O   B PRO   A 125 ? 0.1532 0.1504 0.1375 -0.0105 0.0014  0.0126  125 PRO   A O   
2853 C  CB  A PRO   A 125 ? 0.1482 0.1526 0.1228 -0.0043 0.0116  0.0282  125 PRO   A CB  
2854 C  CB  B PRO   A 125 ? 0.1414 0.1330 0.1098 -0.0223 0.0058  0.0167  125 PRO   A CB  
2855 C  CG  A PRO   A 125 ? 0.1451 0.1467 0.1452 -0.0069 0.0198  0.0379  125 PRO   A CG  
2856 C  CG  B PRO   A 125 ? 0.1368 0.1229 0.1264 -0.0262 0.0108  0.0193  125 PRO   A CG  
2857 C  CD  A PRO   A 125 ? 0.1296 0.1513 0.1654 -0.0017 0.0136  0.0322  125 PRO   A CD  
2858 C  CD  B PRO   A 125 ? 0.1316 0.1206 0.1139 -0.0248 0.0136  0.0190  125 PRO   A CD  
2873 N  N   A LEU   A 126 ? 0.1286 0.1494 0.1380 0.0000  0.0115  0.0232  126 LEU   A N   
2874 N  N   B LEU   A 126 ? 0.1504 0.1522 0.1429 -0.0100 0.0013  0.0166  126 LEU   A N   
2875 C  CA  A LEU   A 126 ? 0.1308 0.1485 0.1423 0.0005  0.0117  0.0167  126 LEU   A CA  
2876 C  CA  B LEU   A 126 ? 0.1487 0.1481 0.1489 -0.0075 0.0050  0.0175  126 LEU   A CA  
2877 C  C   A LEU   A 126 ? 0.1409 0.1369 0.1539 0.0058  -0.0009 0.0075  126 LEU   A C   
2878 C  C   B LEU   A 126 ? 0.1422 0.1335 0.1560 0.0023  0.0189  0.0114  126 LEU   A C   
2879 O  O   A LEU   A 126 ? 0.1521 0.1305 0.1887 0.0080  0.0056  0.0099  126 LEU   A O   
2880 O  O   B LEU   A 126 ? 0.1581 0.1215 0.1733 -0.0041 0.0383  0.0310  126 LEU   A O   
2881 C  CB  A LEU   A 126 ? 0.1350 0.1515 0.1488 0.0003  -0.0013 0.0198  126 LEU   A CB  
2882 C  CB  B LEU   A 126 ? 0.1532 0.1644 0.1742 -0.0159 -0.0036 0.0225  126 LEU   A CB  
2883 C  CG  A LEU   A 126 ? 0.1302 0.1792 0.1622 -0.0077 0.0040  0.0256  126 LEU   A CG  
2884 C  CG  B LEU   A 126 ? 0.1556 0.1777 0.1943 -0.0111 -0.0011 0.0315  126 LEU   A CG  
2885 C  CD1 A LEU   A 126 ? 0.1347 0.2012 0.1742 -0.0206 0.0078  0.0280  126 LEU   A CD1 
2886 C  CD1 B LEU   A 126 ? 0.1508 0.1823 0.2028 -0.0091 0.0041  0.0399  126 LEU   A CD1 
2887 C  CD2 A LEU   A 126 ? 0.1393 0.1722 0.1763 -0.0187 0.0127  0.0385  126 LEU   A CD2 
2888 C  CD2 B LEU   A 126 ? 0.1631 0.1824 0.2032 -0.0097 -0.0029 0.0324  126 LEU   A CD2 
2911 N  N   A LEU   A 127 ? 0.1496 0.1441 0.1440 0.0029  -0.0009 0.0134  127 LEU   A N   
2912 N  N   B LEU   A 127 ? 0.1331 0.1388 0.1438 0.0053  0.0155  0.0181  127 LEU   A N   
2913 C  CA  A LEU   A 127 ? 0.1444 0.1446 0.1358 0.0002  -0.0022 0.0124  127 LEU   A CA  
2914 C  CA  B LEU   A 127 ? 0.1265 0.1436 0.1394 0.0024  0.0131  0.0289  127 LEU   A CA  
2915 C  C   A LEU   A 127 ? 0.1373 0.1349 0.1293 -0.0030 -0.0066 0.0065  127 LEU   A C   
2916 C  C   B LEU   A 127 ? 0.1263 0.1567 0.1449 -0.0020 0.0208  0.0217  127 LEU   A C   
2917 O  O   A LEU   A 127 ? 0.1448 0.1367 0.1413 -0.0195 -0.0149 0.0011  127 LEU   A O   
2918 O  O   B LEU   A 127 ? 0.1298 0.1588 0.1443 -0.0095 0.0339  0.0335  127 LEU   A O   
2919 C  CB  A LEU   A 127 ? 0.1525 0.1517 0.1565 0.0068  0.0087  0.0108  127 LEU   A CB  
2920 C  CB  B LEU   A 127 ? 0.1300 0.1515 0.1425 0.0046  -0.0020 0.0214  127 LEU   A CB  
2921 C  CG  A LEU   A 127 ? 0.1563 0.1532 0.1634 0.0121  0.0059  0.0129  127 LEU   A CG  
2922 C  CG  B LEU   A 127 ? 0.1278 0.1581 0.1436 0.0076  -0.0168 0.0264  127 LEU   A CG  
2923 C  CD1 A LEU   A 127 ? 0.1581 0.1492 0.1818 0.0143  0.0145  0.0105  127 LEU   A CD1 
2924 C  CD1 B LEU   A 127 ? 0.1270 0.1596 0.1523 0.0109  -0.0060 0.0321  127 LEU   A CD1 
2925 C  CD2 A LEU   A 127 ? 0.1665 0.1566 0.1884 0.0186  -0.0073 0.0166  127 LEU   A CD2 
2926 C  CD2 B LEU   A 127 ? 0.1340 0.1670 0.1339 0.0065  -0.0349 0.0133  127 LEU   A CD2 
2949 N  N   A SER   A 128 ? 0.1466 0.1298 0.1276 -0.0057 -0.0039 0.0052  128 SER   A N   
2950 N  N   B SER   A 128 ? 0.1309 0.1666 0.1553 -0.0049 0.0107  0.0198  128 SER   A N   
2951 C  CA  A SER   A 128 ? 0.1532 0.1338 0.1091 -0.0022 0.0033  0.0108  128 SER   A CA  
2952 C  CA  B SER   A 128 ? 0.1413 0.1785 0.1604 -0.0140 -0.0056 0.0186  128 SER   A CA  
2953 C  C   A SER   A 128 ? 0.1530 0.1392 0.1146 0.0110  -0.0040 0.0163  128 SER   A C   
2954 C  C   B SER   A 128 ? 0.1606 0.1857 0.1628 -0.0127 -0.0238 0.0224  128 SER   A C   
2955 O  O   A SER   A 128 ? 0.1685 0.1547 0.1565 0.0069  -0.0063 0.0133  128 SER   A O   
2956 O  O   B SER   A 128 ? 0.1569 0.1807 0.1714 -0.0122 -0.0349 0.0185  128 SER   A O   
2957 C  CB  A SER   A 128 ? 0.1517 0.1437 0.1173 -0.0081 -0.0006 0.0088  128 SER   A CB  
2958 C  CB  B SER   A 128 ? 0.1320 0.1773 0.1539 -0.0162 -0.0143 0.0093  128 SER   A CB  
2959 O  OG  A SER   A 128 ? 0.1549 0.1532 0.1306 -0.0144 0.0037  0.0064  128 SER   A OG  
2960 O  OG  B SER   A 128 ? 0.1192 0.1696 0.1647 -0.0201 -0.0187 -0.0099 128 SER   A OG  
2971 N  N   A ALA   A 129 ? 0.1429 0.1423 0.1345 0.0085  -0.0060 0.0290  129 ALA   A N   
2972 N  N   B ALA   A 129 ? 0.1823 0.2038 0.1861 -0.0112 -0.0271 0.0239  129 ALA   A N   
2973 C  CA  A ALA   A 129 ? 0.1311 0.1389 0.1503 0.0013  -0.0069 0.0236  129 ALA   A CA  
2974 C  CA  B ALA   A 129 ? 0.2035 0.2222 0.2113 -0.0079 -0.0285 0.0228  129 ALA   A CA  
2975 C  C   A ALA   A 129 ? 0.1366 0.1327 0.1286 0.0008  -0.0109 0.0094  129 ALA   A C   
2976 C  C   B ALA   A 129 ? 0.2312 0.2440 0.2357 -0.0063 -0.0186 0.0140  129 ALA   A C   
2977 O  O   A ALA   A 129 ? 0.1333 0.1404 0.1177 -0.0008 -0.0028 0.0190  129 ALA   A O   
2978 O  O   B ALA   A 129 ? 0.2380 0.2480 0.2435 -0.0007 -0.0197 0.0119  129 ALA   A O   
2979 C  CB  A ALA   A 129 ? 0.1349 0.1475 0.1930 0.0066  0.0080  0.0335  129 ALA   A CB  
2980 C  CB  B ALA   A 129 ? 0.1968 0.2221 0.2043 -0.0089 -0.0284 0.0304  129 ALA   A CB  
2991 N  N   A GLY   A 130 ? 0.1347 0.1307 0.1377 0.0004  -0.0106 0.0063  130 GLY   A N   
2992 N  N   B GLY   A 130 ? 0.2546 0.2596 0.2572 -0.0043 -0.0145 0.0140  130 GLY   A N   
2993 C  CA  A GLY   A 130 ? 0.1478 0.1356 0.1476 0.0035  -0.0023 0.0056  130 GLY   A CA  
2994 C  CA  B GLY   A 130 ? 0.2743 0.2737 0.2733 -0.0045 -0.0089 0.0089  130 GLY   A CA  
2995 C  C   A GLY   A 130 ? 0.1492 0.1358 0.1274 0.0026  -0.0139 0.0100  130 GLY   A C   
2996 C  C   B GLY   A 130 ? 0.2887 0.2832 0.2879 -0.0050 -0.0079 0.0073  130 GLY   A C   
2997 O  O   A GLY   A 130 ? 0.1586 0.1344 0.1401 0.0022  -0.0150 0.0135  130 GLY   A O   
2998 O  O   B GLY   A 130 ? 0.2914 0.2855 0.2891 -0.0062 -0.0048 0.0099  130 GLY   A O   
3005 N  N   A ILE   A 131 ? 0.1598 0.1316 0.1278 -0.0004 -0.0131 0.0130  131 ILE   A N   
3006 N  N   B ILE   A 131 ? 0.2971 0.2860 0.2965 -0.0049 -0.0096 0.0077  131 ILE   A N   
3007 C  CA  A ILE   A 131 ? 0.1766 0.1264 0.1090 -0.0092 -0.0150 0.0150  131 ILE   A CA  
3008 C  CA  B ILE   A 131 ? 0.2998 0.2871 0.2961 -0.0031 -0.0135 0.0106  131 ILE   A CA  
3009 C  C   A ILE   A 131 ? 0.1683 0.1299 0.1059 -0.0083 -0.0087 0.0134  131 ILE   A C   
3010 C  C   B ILE   A 131 ? 0.2949 0.2805 0.2780 0.0008  -0.0137 0.0250  131 ILE   A C   
3011 O  O   A ILE   A 131 ? 0.1792 0.1408 0.1096 -0.0043 -0.0122 0.0174  131 ILE   A O   
3012 O  O   B ILE   A 131 ? 0.2950 0.2799 0.2727 0.0033  -0.0134 0.0321  131 ILE   A O   
3013 C  CB  A ILE   A 131 ? 0.2076 0.1415 0.1328 -0.0198 -0.0154 0.0068  131 ILE   A CB  
3014 C  CB  B ILE   A 131 ? 0.3067 0.2962 0.3075 -0.0039 -0.0163 -0.0009 131 ILE   A CB  
3015 C  CG1 A ILE   A 131 ? 0.2166 0.1786 0.1417 -0.0315 -0.0268 -0.0071 131 ILE   A CG1 
3016 C  CG1 B ILE   A 131 ? 0.3091 0.3005 0.3231 -0.0001 -0.0206 -0.0063 131 ILE   A CG1 
3017 C  CG2 A ILE   A 131 ? 0.2349 0.1279 0.1623 -0.0156 0.0141  -0.0049 131 ILE   A CG2 
3018 C  CG2 B ILE   A 131 ? 0.3090 0.2998 0.3043 -0.0078 -0.0163 -0.0034 131 ILE   A CG2 
3019 C  CD1 A ILE   A 131 ? 0.2213 0.1923 0.1929 -0.0338 -0.0164 -0.0342 131 ILE   A CD1 
3020 C  CD1 B ILE   A 131 ? 0.3102 0.3033 0.3349 0.0023  -0.0198 -0.0122 131 ILE   A CD1 
3043 N  N   A PHE   A 132 ? 0.1593 0.1307 0.1170 -0.0050 0.0013  0.0189  132 PHE   A N   
3044 N  N   B PHE   A 132 ? 0.2892 0.2739 0.2708 0.0015  -0.0183 0.0306  132 PHE   A N   
3045 C  CA  A PHE   A 132 ? 0.1665 0.1334 0.1063 -0.0091 0.0029  0.0101  132 PHE   A CA  
3046 C  CA  B PHE   A 132 ? 0.2817 0.2661 0.2637 -0.0015 -0.0228 0.0336  132 PHE   A CA  
3047 C  C   A PHE   A 132 ? 0.1750 0.1627 0.0956 -0.0053 -0.0101 0.0080  132 PHE   A C   
3048 C  C   B PHE   A 132 ? 0.2688 0.2576 0.2346 0.0022  -0.0166 0.0342  132 PHE   A C   
3049 O  O   A PHE   A 132 ? 0.1900 0.1750 0.0931 -0.0038 -0.0109 0.0099  132 PHE   A O   
3050 O  O   B PHE   A 132 ? 0.2718 0.2663 0.2335 0.0054  -0.0138 0.0359  132 PHE   A O   
3051 C  CB  A PHE   A 132 ? 0.1575 0.1342 0.1016 -0.0049 -0.0109 0.0185  132 PHE   A CB  
3052 C  CB  B PHE   A 132 ? 0.2840 0.2675 0.2919 -0.0069 -0.0349 0.0323  132 PHE   A CB  
3053 C  CG  A PHE   A 132 ? 0.1565 0.1315 0.0943 0.0019  -0.0124 0.0159  132 PHE   A CG  
3054 C  CG  B PHE   A 132 ? 0.2863 0.2675 0.3170 -0.0127 -0.0380 0.0339  132 PHE   A CG  
3055 C  CD1 A PHE   A 132 ? 0.1500 0.1406 0.1223 0.0058  -0.0056 -0.0085 132 PHE   A CD1 
3056 C  CD1 B PHE   A 132 ? 0.2855 0.2658 0.3305 -0.0151 -0.0357 0.0342  132 PHE   A CD1 
3057 C  CD2 A PHE   A 132 ? 0.1585 0.1421 0.1164 0.0094  -0.0119 -0.0026 132 PHE   A CD2 
3058 C  CD2 B PHE   A 132 ? 0.2861 0.2675 0.3262 -0.0164 -0.0429 0.0347  132 PHE   A CD2 
3059 C  CE1 A PHE   A 132 ? 0.1500 0.1483 0.1326 0.0049  -0.0168 -0.0010 132 PHE   A CE1 
3060 C  CE1 B PHE   A 132 ? 0.2846 0.2643 0.3367 -0.0189 -0.0356 0.0312  132 PHE   A CE1 
3061 C  CE2 A PHE   A 132 ? 0.1541 0.1469 0.1364 0.0122  -0.0066 -0.0036 132 PHE   A CE2 
3062 C  CE2 B PHE   A 132 ? 0.2847 0.2654 0.3300 -0.0207 -0.0447 0.0319  132 PHE   A CE2 
3063 C  CZ  A PHE   A 132 ? 0.1478 0.1428 0.1376 -0.0020 -0.0207 0.0057  132 PHE   A CZ  
3064 C  CZ  B PHE   A 132 ? 0.2833 0.2634 0.3334 -0.0222 -0.0425 0.0285  132 PHE   A CZ  
3083 N  N   A GLY   A 133 ? 0.1691 0.1664 0.1056 -0.0040 -0.0228 0.0150  133 GLY   A N   
3084 N  N   B GLY   A 133 ? 0.2519 0.2420 0.2116 0.0015  -0.0196 0.0309  133 GLY   A N   
3085 C  CA  A GLY   A 133 ? 0.1796 0.1800 0.1374 -0.0103 -0.0394 0.0052  133 GLY   A CA  
3086 C  CA  B GLY   A 133 ? 0.2364 0.2338 0.1994 0.0007  -0.0204 0.0160  133 GLY   A CA  
3087 C  C   A GLY   A 133 ? 0.1845 0.1934 0.1379 -0.0155 -0.0537 -0.0017 133 GLY   A C   
3088 C  C   B GLY   A 133 ? 0.2175 0.2307 0.1861 0.0006  -0.0195 0.0040  133 GLY   A C   
3089 O  O   A GLY   A 133 ? 0.1997 0.2083 0.1609 -0.0176 -0.0493 -0.0157 133 GLY   A O   
3090 O  O   B GLY   A 133 ? 0.2111 0.2371 0.1912 0.0022  -0.0205 -0.0069 133 GLY   A O   
3097 N  N   A ALA   A 134 ? 0.1870 0.1816 0.1395 -0.0170 -0.0383 -0.0087 134 ALA   A N   
3098 N  N   B ALA   A 134 ? 0.2083 0.2188 0.1823 0.0020  -0.0105 0.0037  134 ALA   A N   
3099 C  CA  A ALA   A 134 ? 0.1949 0.1855 0.1761 -0.0116 -0.0320 -0.0051 134 ALA   A CA  
3100 C  CA  B ALA   A 134 ? 0.2016 0.2122 0.1853 0.0024  -0.0112 0.0068  134 ALA   A CA  
3101 C  C   A ALA   A 134 ? 0.1944 0.1908 0.1862 -0.0199 -0.0200 0.0135  134 ALA   A C   
3102 C  C   B ALA   A 134 ? 0.1969 0.2060 0.1916 -0.0072 -0.0064 0.0138  134 ALA   A C   
3103 O  O   A ALA   A 134 ? 0.2046 0.2031 0.2078 -0.0108 0.0036  0.0149  134 ALA   A O   
3104 O  O   B ALA   A 134 ? 0.1965 0.2059 0.2049 -0.0124 -0.0003 0.0191  134 ALA   A O   
3105 C  CB  A ALA   A 134 ? 0.2097 0.1729 0.2127 -0.0058 -0.0368 -0.0131 134 ALA   A CB  
3106 C  CB  B ALA   A 134 ? 0.2059 0.2073 0.1955 0.0084  -0.0171 0.0031  134 ALA   A CB  
3117 N  N   A ASP   A 135 ? 0.1989 0.1963 0.1903 -0.0348 -0.0323 0.0302  135 ASP   A N   
3118 N  N   B ASP   A 135 ? 0.2033 0.2057 0.1962 -0.0074 -0.0133 0.0130  135 ASP   A N   
3119 C  CA  A ASP   A 135 ? 0.1946 0.2086 0.2136 -0.0360 -0.0511 0.0446  135 ASP   A CA  
3120 C  CA  B ASP   A 135 ? 0.2036 0.2087 0.2107 -0.0064 -0.0253 0.0155  135 ASP   A CA  
3121 C  C   A ASP   A 135 ? 0.1771 0.1869 0.2286 -0.0236 -0.0377 0.0467  135 ASP   A C   
3122 C  C   B ASP   A 135 ? 0.1985 0.2015 0.2103 -0.0071 -0.0224 0.0143  135 ASP   A C   
3123 O  O   A ASP   A 135 ? 0.1783 0.1749 0.2342 -0.0225 -0.0406 0.0444  135 ASP   A O   
3124 O  O   B ASP   A 135 ? 0.1988 0.1957 0.2071 -0.0072 -0.0263 0.0160  135 ASP   A O   
3125 C  CB  A ASP   A 135 ? 0.2187 0.2417 0.2570 -0.0544 -0.0744 0.0333  135 ASP   A CB  
3126 C  CB  B ASP   A 135 ? 0.2118 0.2185 0.2390 -0.0086 -0.0372 0.0165  135 ASP   A CB  
3127 C  CG  A ASP   A 135 ? 0.2386 0.2630 0.2960 -0.0714 -0.0921 0.0355  135 ASP   A CG  
3128 C  CG  B ASP   A 135 ? 0.2167 0.2266 0.2770 -0.0097 -0.0388 0.0190  135 ASP   A CG  
3129 O  OD1 A ASP   A 135 ? 0.2439 0.2715 0.2879 -0.0766 -0.1050 0.0731  135 ASP   A OD1 
3130 O  OD1 B ASP   A 135 ? 0.2179 0.2248 0.2948 -0.0038 -0.0379 0.0268  135 ASP   A OD1 
3131 O  OD2 A ASP   A 135 ? 0.2615 0.2821 0.3506 -0.0718 -0.0674 0.0267  135 ASP   A OD2 
3132 O  OD2 B ASP   A 135 ? 0.2144 0.2340 0.2865 -0.0153 -0.0386 0.0207  135 ASP   A OD2 
3141 N  N   A PRO   A 136 ? 0.1590 0.1819 0.2524 0.0002  -0.0160 0.0593  136 PRO   A N   
3142 N  N   B PRO   A 136 ? 0.1936 0.2042 0.2183 -0.0053 -0.0109 0.0208  136 PRO   A N   
3143 C  CA  A PRO   A 136 ? 0.1507 0.1786 0.2521 -0.0043 0.0001  0.0428  136 PRO   A CA  
3144 C  CA  B PRO   A 136 ? 0.1882 0.2074 0.2176 -0.0076 -0.0060 0.0162  136 PRO   A CA  
3145 C  C   A PRO   A 136 ? 0.1362 0.1737 0.2238 -0.0017 -0.0012 0.0371  136 PRO   A C   
3146 C  C   B PRO   A 136 ? 0.1808 0.2081 0.2065 -0.0078 -0.0046 0.0151  136 PRO   A C   
3147 O  O   A PRO   A 136 ? 0.1294 0.1731 0.2046 -0.0046 0.0008  0.0318  136 PRO   A O   
3148 O  O   B PRO   A 136 ? 0.1762 0.2019 0.1975 -0.0078 -0.0053 0.0182  136 PRO   A O   
3149 C  CB  A PRO   A 136 ? 0.1666 0.1800 0.2750 0.0085  0.0078  0.0410  136 PRO   A CB  
3150 C  CB  B PRO   A 136 ? 0.1960 0.2104 0.2268 -0.0062 -0.0049 0.0206  136 PRO   A CB  
3151 C  CG  A PRO   A 136 ? 0.1723 0.1776 0.2968 0.0140  0.0009  0.0557  136 PRO   A CG  
3152 C  CG  B PRO   A 136 ? 0.2023 0.2107 0.2332 -0.0076 -0.0015 0.0274  136 PRO   A CG  
3153 C  CD  A PRO   A 136 ? 0.1766 0.1836 0.2820 0.0135  0.0015  0.0644  136 PRO   A CD  
3154 C  CD  B PRO   A 136 ? 0.2018 0.2074 0.2366 -0.0046 -0.0028 0.0264  136 PRO   A CD  
3169 N  N   A ILE   A 137 ? 0.1340 0.1799 0.2319 -0.0014 -0.0181 0.0447  137 ILE   A N   
3170 N  N   B ILE   A 137 ? 0.1779 0.2121 0.2145 -0.0081 -0.0084 0.0155  137 ILE   A N   
3171 C  CA  A ILE   A 137 ? 0.1348 0.1904 0.2239 -0.0149 -0.0208 0.0451  137 ILE   A CA  
3172 C  CA  B ILE   A 137 ? 0.1771 0.2162 0.2143 -0.0118 -0.0100 0.0205  137 ILE   A CA  
3173 C  C   A ILE   A 137 ? 0.1385 0.1831 0.1995 -0.0216 -0.0155 0.0383  137 ILE   A C   
3174 C  C   B ILE   A 137 ? 0.1752 0.2068 0.2056 -0.0133 -0.0091 0.0162  137 ILE   A C   
3175 O  O   A ILE   A 137 ? 0.1550 0.1795 0.2066 -0.0211 -0.0057 0.0350  137 ILE   A O   
3176 O  O   B ILE   A 137 ? 0.1811 0.2059 0.2101 -0.0107 -0.0029 0.0158  137 ILE   A O   
3177 C  CB  A ILE   A 137 ? 0.1501 0.2122 0.2555 -0.0166 -0.0337 0.0428  137 ILE   A CB  
3178 C  CB  B ILE   A 137 ? 0.1843 0.2286 0.2397 -0.0151 -0.0090 0.0231  137 ILE   A CB  
3179 C  CG1 A ILE   A 137 ? 0.1600 0.2425 0.2850 -0.0010 -0.0476 0.0449  137 ILE   A CG1 
3180 C  CG1 B ILE   A 137 ? 0.1894 0.2403 0.2645 -0.0124 -0.0115 0.0216  137 ILE   A CG1 
3181 C  CG2 A ILE   A 137 ? 0.1637 0.2108 0.2591 -0.0265 -0.0261 0.0281  137 ILE   A CG2 
3182 C  CG2 B ILE   A 137 ? 0.1886 0.2309 0.2319 -0.0176 -0.0024 0.0226  137 ILE   A CG2 
3183 C  CD1 A ILE   A 137 ? 0.1679 0.2598 0.3060 0.0066  -0.0442 0.0393  137 ILE   A CD1 
3184 C  CD1 B ILE   A 137 ? 0.1959 0.2459 0.2792 -0.0084 -0.0079 0.0189  137 ILE   A CD1 
3207 N  N   A HIS   A 138 ? 0.1464 0.1996 0.2023 -0.0148 -0.0059 0.0254  138 HIS   A N   
3208 N  N   B HIS   A 138 ? 0.1705 0.2056 0.2051 -0.0141 -0.0098 0.0064  138 HIS   A N   
3209 C  CA  A HIS   A 138 ? 0.1607 0.2076 0.1820 -0.0204 0.0012  0.0141  138 HIS   A CA  
3210 C  CA  B HIS   A 138 ? 0.1664 0.1996 0.1919 -0.0182 -0.0091 0.0038  138 HIS   A CA  
3211 C  C   A HIS   A 138 ? 0.1535 0.1903 0.1878 -0.0131 -0.0018 0.0198  138 HIS   A C   
3212 C  C   B HIS   A 138 ? 0.1563 0.1887 0.1898 -0.0121 -0.0079 0.0185  138 HIS   A C   
3213 O  O   A HIS   A 138 ? 0.1567 0.1893 0.1888 -0.0133 0.0002  0.0163  138 HIS   A O   
3214 O  O   B HIS   A 138 ? 0.1580 0.1886 0.1847 -0.0121 -0.0051 0.0262  138 HIS   A O   
3215 C  CB  A HIS   A 138 ? 0.1808 0.2312 0.1810 -0.0145 0.0023  0.0084  138 HIS   A CB  
3216 C  CB  B HIS   A 138 ? 0.1733 0.2087 0.1927 -0.0160 -0.0139 -0.0107 138 HIS   A CB  
3217 C  CG  A HIS   A 138 ? 0.1967 0.2453 0.1849 -0.0208 0.0026  0.0134  138 HIS   A CG  
3218 C  CG  B HIS   A 138 ? 0.1759 0.2138 0.1960 -0.0195 -0.0182 -0.0249 138 HIS   A CG  
3219 N  ND1 A HIS   A 138 ? 0.2116 0.2555 0.2125 -0.0256 0.0039  0.0007  138 HIS   A ND1 
3220 N  ND1 B HIS   A 138 ? 0.1813 0.2194 0.2055 -0.0193 -0.0147 -0.0361 138 HIS   A ND1 
3221 C  CD2 A HIS   A 138 ? 0.2001 0.2543 0.1993 -0.0210 0.0103  0.0199  138 HIS   A CD2 
3222 C  CD2 B HIS   A 138 ? 0.1744 0.2148 0.2001 -0.0201 -0.0215 -0.0287 138 HIS   A CD2 
3223 C  CE1 A HIS   A 138 ? 0.2158 0.2611 0.2219 -0.0158 0.0054  0.0095  138 HIS   A CE1 
3224 C  CE1 B HIS   A 138 ? 0.1810 0.2194 0.2083 -0.0159 -0.0190 -0.0343 138 HIS   A CE1 
3225 N  NE2 A HIS   A 138 ? 0.2067 0.2625 0.1967 -0.0157 0.0190  0.0170  138 HIS   A NE2 
3226 N  NE2 B HIS   A 138 ? 0.1766 0.2179 0.2060 -0.0157 -0.0172 -0.0341 138 HIS   A NE2 
3241 N  N   . SER   A 139 ? 0.1441 0.1781 0.1773 -0.0083 -0.0056 0.0273  139 SER   A N   
3242 C  CA  . SER   A 139 ? 0.1423 0.1711 0.1748 -0.0059 -0.0038 0.0306  139 SER   A CA  
3243 C  C   . SER   A 139 ? 0.1406 0.1622 0.1655 -0.0087 0.0031  0.0238  139 SER   A C   
3244 O  O   . SER   A 139 ? 0.1395 0.1558 0.1778 -0.0159 0.0005  0.0225  139 SER   A O   
3245 C  CB  . SER   A 139 ? 0.1414 0.1700 0.1645 -0.0186 -0.0056 0.0305  139 SER   A CB  
3246 O  OG  . SER   A 139 ? 0.1489 0.1690 0.1759 -0.0213 -0.0095 0.0372  139 SER   A OG  
3253 N  N   . LEU   A 140 ? 0.1418 0.1647 0.1692 -0.0104 0.0016  0.0325  140 LEU   A N   
3254 C  CA  . LEU   A 140 ? 0.1392 0.1619 0.1789 -0.0062 0.0009  0.0298  140 LEU   A CA  
3255 C  C   . LEU   A 140 ? 0.1316 0.1722 0.1820 -0.0137 0.0046  0.0299  140 LEU   A C   
3256 O  O   . LEU   A 140 ? 0.1356 0.1710 0.2015 -0.0096 -0.0017 0.0361  140 LEU   A O   
3257 C  CB  . LEU   A 140 ? 0.1365 0.1736 0.1972 -0.0138 0.0069  0.0353  140 LEU   A CB  
3258 C  CG  . LEU   A 140 ? 0.1394 0.1882 0.1968 -0.0194 0.0070  0.0462  140 LEU   A CG  
3259 C  CD1 . LEU   A 140 ? 0.1445 0.1863 0.2039 -0.0163 0.0030  0.0365  140 LEU   A CD1 
3260 C  CD2 . LEU   A 140 ? 0.1384 0.2006 0.2145 -0.0157 0.0150  0.0568  140 LEU   A CD2 
3272 N  N   . ARG   A 141 ? 0.1392 0.1745 0.1903 -0.0134 0.0023  0.0237  141 ARG   A N   
3273 C  CA  . ARG   A 141 ? 0.1512 0.1843 0.2122 -0.0225 -0.0072 0.0101  141 ARG   A CA  
3274 C  C   . ARG   A 141 ? 0.1484 0.1711 0.1975 -0.0149 -0.0070 0.0067  141 ARG   A C   
3275 O  O   . ARG   A 141 ? 0.1496 0.1652 0.2202 -0.0115 0.0026  0.0062  141 ARG   A O   
3276 C  CB  . ARG   A 141 ? 0.1637 0.2092 0.2344 -0.0328 -0.0064 -0.0105 141 ARG   A CB  
3277 C  CG  . ARG   A 141 ? 0.1977 0.2456 0.2794 -0.0342 0.0043  -0.0132 141 ARG   A CG  
3278 C  CD  . ARG   A 141 ? 0.2293 0.2678 0.3212 -0.0362 0.0080  -0.0128 141 ARG   A CD  
3279 N  NE  . ARG   A 141 ? 0.2260 0.2888 0.3460 -0.0353 -0.0036 -0.0121 141 ARG   A NE  
3280 C  CZ  . ARG   A 141 ? 0.2254 0.3122 0.3402 -0.0487 0.0083  -0.0148 141 ARG   A CZ  
3281 N  NH1 . ARG   A 141 ? 0.2010 0.3078 0.3181 -0.0608 0.0300  -0.0328 141 ARG   A NH1 
3282 N  NH2 . ARG   A 141 ? 0.2397 0.3346 0.3701 -0.0467 -0.0043 -0.0032 141 ARG   A NH2 
3296 N  N   . VAL   A 142 ? 0.1424 0.1653 0.1836 -0.0138 0.0015  0.0060  142 VAL   A N   
3297 C  CA  . VAL   A 142 ? 0.1484 0.1603 0.1912 -0.0088 0.0163  0.0081  142 VAL   A CA  
3298 C  C   . VAL   A 142 ? 0.1349 0.1508 0.1921 -0.0120 0.0077  0.0117  142 VAL   A C   
3299 O  O   . VAL   A 142 ? 0.1437 0.1521 0.2017 -0.0027 0.0107  0.0154  142 VAL   A O   
3300 C  CB  . VAL   A 142 ? 0.1536 0.1652 0.1857 -0.0110 0.0179  0.0075  142 VAL   A CB  
3301 C  CG1 . VAL   A 142 ? 0.1550 0.1631 0.2087 -0.0211 0.0210  0.0062  142 VAL   A CG1 
3302 C  CG2 . VAL   A 142 ? 0.1670 0.1791 0.2040 -0.0035 0.0135  0.0078  142 VAL   A CG2 
3312 N  N   . CYS   A 143 ? 0.1394 0.1510 0.1806 -0.0155 0.0028  0.0142  143 CYS   A N   
3313 C  CA  . CYS   A 143 ? 0.1420 0.1528 0.1891 -0.0112 0.0083  0.0208  143 CYS   A CA  
3314 C  C   . CYS   A 143 ? 0.1394 0.1501 0.1940 -0.0120 0.0069  0.0296  143 CYS   A C   
3315 O  O   . CYS   A 143 ? 0.1330 0.1465 0.1976 -0.0055 0.0043  0.0310  143 CYS   A O   
3316 C  CB  . CYS   A 143 ? 0.1426 0.1542 0.2002 -0.0070 0.0117  0.0245  143 CYS   A CB  
3317 S  SG  . CYS   A 143 ? 0.1637 0.1650 0.1787 0.0016  0.0093  0.0184  143 CYS   A SG  
3323 N  N   . VAL   A 144 ? 0.1341 0.1628 0.2101 -0.0181 0.0159  0.0353  144 VAL   A N   
3324 C  CA  . VAL   A 144 ? 0.1430 0.1680 0.2469 -0.0174 0.0237  0.0332  144 VAL   A CA  
3325 C  C   . VAL   A 144 ? 0.1443 0.1588 0.2446 -0.0203 -0.0054 0.0284  144 VAL   A C   
3326 O  O   . VAL   A 144 ? 0.1560 0.1624 0.2420 -0.0037 -0.0099 0.0332  144 VAL   A O   
3327 C  CB  . VAL   A 144 ? 0.1746 0.1845 0.3029 -0.0090 0.0357  0.0357  144 VAL   A CB  
3328 C  CG1 . VAL   A 144 ? 0.1959 0.2030 0.3358 -0.0193 0.0155  0.0434  144 VAL   A CG1 
3329 C  CG2 . VAL   A 144 ? 0.1692 0.1946 0.3118 -0.0052 0.0400  0.0386  144 VAL   A CG2 
3339 N  N   . ASP   A 145 ? 0.1548 0.1506 0.2531 -0.0224 -0.0018 0.0202  145 ASP   A N   
3340 C  CA  . ASP   A 145 ? 0.1647 0.1609 0.2531 -0.0238 -0.0029 0.0063  145 ASP   A CA  
3341 C  C   . ASP   A 145 ? 0.1639 0.1477 0.2593 -0.0146 0.0028  0.0074  145 ASP   A C   
3342 O  O   . ASP   A 145 ? 0.1785 0.1540 0.3168 -0.0161 0.0022  -0.0271 145 ASP   A O   
3343 C  CB  . ASP   A 145 ? 0.1735 0.1850 0.2727 -0.0260 -0.0164 0.0003  145 ASP   A CB  
3344 C  CG  . ASP   A 145 ? 0.1934 0.2240 0.3066 -0.0396 -0.0280 0.0200  145 ASP   A CG  
3345 O  OD1 . ASP   A 145 ? 0.1875 0.2388 0.3055 -0.0515 -0.0196 0.0231  145 ASP   A OD1 
3346 O  OD2 . ASP   A 145 ? 0.2110 0.2437 0.3103 -0.0515 -0.0489 0.0127  145 ASP   A OD2 
3351 N  N   . THR   A 146 ? 0.1450 0.1444 0.2133 -0.0187 0.0099  0.0096  146 THR   A N   
3352 C  CA  . THR   A 146 ? 0.1395 0.1429 0.2059 -0.0071 0.0038  0.0064  146 THR   A CA  
3353 C  C   . THR   A 146 ? 0.1383 0.1418 0.2123 -0.0021 0.0074  0.0205  146 THR   A C   
3354 O  O   . THR   A 146 ? 0.1544 0.1518 0.2271 0.0049  -0.0096 0.0180  146 THR   A O   
3355 C  CB  . THR   A 146 ? 0.1405 0.1431 0.1954 -0.0038 0.0060  0.0177  146 THR   A CB  
3356 O  OG1 . THR   A 146 ? 0.1434 0.1591 0.1998 -0.0008 -0.0005 0.0051  146 THR   A OG1 
3357 C  CG2 . THR   A 146 ? 0.1449 0.1463 0.2183 -0.0126 0.0098  0.0171  146 THR   A CG2 
3365 N  N   . VAL   A 147 ? 0.1311 0.1436 0.1971 -0.0024 0.0127  0.0145  147 VAL   A N   
3366 C  CA  . VAL   A 147 ? 0.1388 0.1480 0.2009 -0.0107 0.0174  0.0270  147 VAL   A CA  
3367 C  C   . VAL   A 147 ? 0.1417 0.1466 0.2170 -0.0153 0.0158  0.0371  147 VAL   A C   
3368 O  O   . VAL   A 147 ? 0.1487 0.1565 0.2280 -0.0219 0.0112  0.0321  147 VAL   A O   
3369 C  CB  . VAL   A 147 ? 0.1496 0.1514 0.1904 -0.0102 0.0178  0.0275  147 VAL   A CB  
3370 C  CG1 . VAL   A 147 ? 0.1771 0.1599 0.1920 -0.0045 0.0165  0.0323  147 VAL   A CG1 
3371 C  CG2 . VAL   A 147 ? 0.1544 0.1522 0.1944 -0.0161 0.0163  0.0234  147 VAL   A CG2 
3381 N  N   . ARG   A 148 ? 0.1426 0.1539 0.2216 -0.0161 0.0124  0.0552  148 ARG   A N   
3382 C  CA  . ARG   A 148 ? 0.1535 0.1588 0.2161 -0.0201 0.0082  0.0636  148 ARG   A CA  
3383 C  C   . ARG   A 148 ? 0.1599 0.1634 0.2025 -0.0233 0.0049  0.0810  148 ARG   A C   
3384 O  O   . ARG   A 148 ? 0.1820 0.1750 0.2364 -0.0215 0.0175  0.0578  148 ARG   A O   
3385 C  CB  . ARG   A 148 ? 0.1589 0.1545 0.2431 -0.0097 0.0223  0.0547  148 ARG   A CB  
3386 C  CG  . ARG   A 148 ? 0.1773 0.1632 0.2654 -0.0075 0.0318  0.0462  148 ARG   A CG  
3387 C  CD  . ARG   A 148 ? 0.1878 0.1565 0.2866 -0.0016 0.0484  0.0651  148 ARG   A CD  
3388 N  NE  . ARG   A 148 ? 0.1817 0.1618 0.2914 0.0081  0.0513  0.0607  148 ARG   A NE  
3389 C  CZ  . ARG   A 148 ? 0.1781 0.1527 0.2741 0.0029  0.0452  0.0512  148 ARG   A CZ  
3390 N  NH1 . ARG   A 148 ? 0.1741 0.1515 0.2875 -0.0074 0.0365  0.0299  148 ARG   A NH1 
3391 N  NH2 . ARG   A 148 ? 0.1730 0.1705 0.2755 0.0137  0.0432  0.0542  148 ARG   A NH2 
3405 N  N   . THR   A 149 ? 0.1584 0.1708 0.2057 -0.0235 -0.0052 0.0656  149 THR   A N   
3406 C  CA  . THR   A 149 ? 0.1557 0.1726 0.2066 -0.0161 0.0013  0.0611  149 THR   A CA  
3407 C  C   . THR   A 149 ? 0.1535 0.1702 0.1905 -0.0221 0.0050  0.0615  149 THR   A C   
3408 O  O   . THR   A 149 ? 0.1540 0.1817 0.2150 -0.0284 0.0004  0.0588  149 THR   A O   
3409 C  CB  . THR   A 149 ? 0.1561 0.1856 0.2168 -0.0209 0.0043  0.0590  149 THR   A CB  
3410 O  OG1 . THR   A 149 ? 0.1588 0.1725 0.2378 -0.0321 0.0053  0.0488  149 THR   A OG1 
3411 C  CG2 . THR   A 149 ? 0.1527 0.1996 0.2283 -0.0131 -0.0140 0.0508  149 THR   A CG2 
3419 N  N   . ASN   A 150 ? 0.1522 0.1787 0.2042 -0.0083 0.0045  0.0653  150 ASN   A N   
3420 C  CA  . ASN   A 150 ? 0.1724 0.1909 0.1985 -0.0125 0.0131  0.0604  150 ASN   A CA  
3421 C  C   . ASN   A 150 ? 0.1461 0.1749 0.2043 -0.0229 0.0072  0.0556  150 ASN   A C   
3422 O  O   . ASN   A 150 ? 0.1569 0.1869 0.2352 -0.0168 -0.0155 0.0485  150 ASN   A O   
3423 C  CB  . ASN   A 150 ? 0.2220 0.2138 0.2318 -0.0179 0.0361  0.0819  150 ASN   A CB  
3424 C  CG  . ASN   A 150 ? 0.2797 0.2472 0.3099 -0.0152 0.0090  0.0874  150 ASN   A CG  
3425 O  OD1 . ASN   A 150 ? 0.3018 0.2588 0.3119 -0.0275 0.0035  0.1111  150 ASN   A OD1 
3426 N  ND2 . ASN   A 150 ? 0.3098 0.2652 0.3496 -0.0115 -0.0074 0.0736  150 ASN   A ND2 
3433 N  N   . VAL   A 151 ? 0.1465 0.1596 0.2016 -0.0177 -0.0068 0.0501  151 VAL   A N   
3434 C  CA  . VAL   A 151 ? 0.1528 0.1649 0.1809 -0.0158 0.0044  0.0464  151 VAL   A CA  
3435 C  C   . VAL   A 151 ? 0.1456 0.1654 0.1930 -0.0258 0.0048  0.0524  151 VAL   A C   
3436 O  O   . VAL   A 151 ? 0.1530 0.1761 0.2266 -0.0266 0.0062  0.0432  151 VAL   A O   
3437 C  CB  . VAL   A 151 ? 0.1843 0.1877 0.1873 -0.0049 0.0053  0.0399  151 VAL   A CB  
3438 C  CG1 . VAL   A 151 ? 0.1769 0.2059 0.2249 -0.0033 -0.0011 0.0333  151 VAL   A CG1 
3439 C  CG2 . VAL   A 151 ? 0.1948 0.1823 0.1807 -0.0063 0.0242  0.0406  151 VAL   A CG2 
3449 N  N   . TYR   A 152 ? 0.1475 0.1682 0.1825 -0.0243 0.0049  0.0459  152 TYR   A N   
3450 C  CA  . TYR   A 152 ? 0.1492 0.1708 0.1579 -0.0224 0.0069  0.0379  152 TYR   A CA  
3451 C  C   . TYR   A 152 ? 0.1392 0.1622 0.1539 -0.0180 0.0131  0.0406  152 TYR   A C   
3452 O  O   . TYR   A 152 ? 0.1537 0.1624 0.1571 -0.0265 0.0120  0.0349  152 TYR   A O   
3453 C  CB  . TYR   A 152 ? 0.1702 0.1762 0.1720 -0.0233 0.0185  0.0394  152 TYR   A CB  
3454 C  CG  . TYR   A 152 ? 0.1821 0.1963 0.1674 -0.0272 0.0217  0.0455  152 TYR   A CG  
3455 C  CD1 . TYR   A 152 ? 0.1912 0.2250 0.1906 -0.0177 0.0241  0.0564  152 TYR   A CD1 
3456 C  CD2 . TYR   A 152 ? 0.1854 0.2036 0.1779 -0.0424 0.0128  0.0425  152 TYR   A CD2 
3457 C  CE1 . TYR   A 152 ? 0.2207 0.2413 0.2101 -0.0110 0.0069  0.0813  152 TYR   A CE1 
3458 C  CE2 . TYR   A 152 ? 0.2118 0.2273 0.1987 -0.0377 0.0162  0.0554  152 TYR   A CE2 
3459 C  CZ  . TYR   A 152 ? 0.2331 0.2396 0.1894 -0.0291 0.0067  0.0906  152 TYR   A CZ  
3460 O  OH  . TYR   A 152 ? 0.2620 0.2701 0.2404 -0.0235 0.0142  0.1007  152 TYR   A OH  
3470 N  N   A LEU   A 153 ? 0.1358 0.1602 0.1742 -0.0290 0.0180  0.0413  153 LEU   A N   
3471 N  N   B LEU   A 153 ? 0.1397 0.1656 0.1569 -0.0257 0.0031  0.0391  153 LEU   A N   
3472 C  CA  A LEU   A 153 ? 0.1348 0.1526 0.1877 -0.0137 0.0176  0.0396  153 LEU   A CA  
3473 C  CA  B LEU   A 153 ? 0.1400 0.1643 0.1472 -0.0213 0.0002  0.0321  153 LEU   A CA  
3474 C  C   A LEU   A 153 ? 0.1379 0.1517 0.1836 -0.0103 0.0297  0.0349  153 LEU   A C   
3475 C  C   B LEU   A 153 ? 0.1433 0.1647 0.1374 -0.0174 0.0013  0.0319  153 LEU   A C   
3476 O  O   A LEU   A 153 ? 0.1469 0.1637 0.2222 -0.0135 0.0408  0.0235  153 LEU   A O   
3477 O  O   B LEU   A 153 ? 0.1476 0.1688 0.1604 -0.0250 0.0129  0.0336  153 LEU   A O   
3478 C  CB  A LEU   A 153 ? 0.1366 0.1451 0.1995 -0.0093 0.0105  0.0396  153 LEU   A CB  
3479 C  CB  B LEU   A 153 ? 0.1418 0.1687 0.1501 -0.0160 -0.0029 0.0335  153 LEU   A CB  
3480 C  CG  A LEU   A 153 ? 0.1354 0.1471 0.1829 -0.0069 0.0154  0.0305  153 LEU   A CG  
3481 C  CG  B LEU   A 153 ? 0.1501 0.1768 0.1511 -0.0098 -0.0065 0.0351  153 LEU   A CG  
3482 C  CD1 A LEU   A 153 ? 0.1451 0.1411 0.1928 -0.0122 0.0006  0.0309  153 LEU   A CD1 
3483 C  CD1 B LEU   A 153 ? 0.1553 0.1800 0.1635 0.0001  -0.0051 0.0326  153 LEU   A CD1 
3484 C  CD2 A LEU   A 153 ? 0.1358 0.1485 0.1765 -0.0144 0.0127  0.0168  153 LEU   A CD2 
3485 C  CD2 B LEU   A 153 ? 0.1549 0.1823 0.1523 -0.0185 -0.0145 0.0328  153 LEU   A CD2 
3508 N  N   A ALA   A 154 ? 0.1364 0.1462 0.1691 -0.0092 0.0290  0.0375  154 ALA   A N   
3509 N  N   B ALA   A 154 ? 0.1463 0.1608 0.1190 -0.0121 -0.0048 0.0269  154 ALA   A N   
3510 C  CA  A ALA   A 154 ? 0.1472 0.1488 0.1713 -0.0128 0.0282  0.0349  154 ALA   A CA  
3511 C  CA  B ALA   A 154 ? 0.1541 0.1604 0.1271 -0.0082 -0.0116 0.0169  154 ALA   A CA  
3512 C  C   A ALA   A 154 ? 0.1403 0.1408 0.1516 -0.0028 0.0240  0.0339  154 ALA   A C   
3513 C  C   B ALA   A 154 ? 0.1473 0.1598 0.1154 -0.0048 -0.0058 0.0201  154 ALA   A C   
3514 O  O   A ALA   A 154 ? 0.1533 0.1517 0.1664 -0.0103 0.0204  0.0209  154 ALA   A O   
3515 O  O   B ALA   A 154 ? 0.1510 0.1641 0.0949 -0.0102 0.0063  0.0223  154 ALA   A O   
3516 C  CB  A ALA   A 154 ? 0.1584 0.1583 0.1602 -0.0051 0.0237  0.0284  154 ALA   A CB  
3517 C  CB  B ALA   A 154 ? 0.1669 0.1608 0.1488 -0.0065 -0.0208 -0.0008 154 ALA   A CB  
3528 N  N   A VAL   A 155 ? 0.1221 0.1213 0.1088 0.0047  0.0293  0.0480  155 VAL   A N   
3529 N  N   B VAL   A 155 ? 0.1430 0.1572 0.1272 0.0009  -0.0068 0.0171  155 VAL   A N   
3530 C  CA  A VAL   A 155 ? 0.1422 0.1399 0.1627 0.0082  0.0229  0.0508  155 VAL   A CA  
3531 C  CA  B VAL   A 155 ? 0.1637 0.1683 0.1222 -0.0058 -0.0092 0.0114  155 VAL   A CA  
3532 C  CA  T VAL   A 155 ? 0.1848 0.1697 0.1725 -0.0129 0.0308  0.0372  155 VAL   A CA  
3533 C  C   A VAL   A 155 ? 0.1489 0.1517 0.2020 0.0174  0.0202  0.0596  155 VAL   A C   
3534 C  C   B VAL   A 155 ? 0.1753 0.1732 0.1551 -0.0027 -0.0264 0.0149  155 VAL   A C   
3535 C  C   T VAL   A 155 ? 0.1882 0.1739 0.1694 -0.0055 0.0413  0.0427  155 VAL   A C   
3536 O  O   A VAL   A 155 ? 0.1434 0.1476 0.2234 0.0172  0.0263  0.0436  155 VAL   A O   
3537 O  O   B VAL   A 155 ? 0.1749 0.1716 0.1463 -0.0028 -0.0318 -0.0060 155 VAL   A O   
3538 O  O   T VAL   A 155 ? 0.1818 0.1742 0.1671 -0.0094 0.0426  0.0333  155 VAL   A O   
3539 C  CB  A VAL   A 155 ? 0.1560 0.1473 0.1624 0.0206  0.0196  0.0416  155 VAL   A CB  
3540 C  CB  B VAL   A 155 ? 0.1713 0.1747 0.1130 0.0006  -0.0018 -0.0029 155 VAL   A CB  
3541 C  CB  T VAL   A 155 ? 0.1849 0.1679 0.1668 -0.0109 0.0187  0.0291  155 VAL   A CB  
3542 C  CG1 A VAL   A 155 ? 0.1748 0.1564 0.1495 0.0199  0.0056  0.0429  155 VAL   A CG1 
3543 C  CG1 B VAL   A 155 ? 0.1783 0.1745 0.1185 0.0019  -0.0079 -0.0094 155 VAL   A CG1 
3544 C  CG1 T VAL   A 155 ? 0.1925 0.1716 0.1560 -0.0089 0.0103  0.0301  155 VAL   A CG1 
3545 C  CG2 A VAL   A 155 ? 0.1667 0.1588 0.1799 0.0292  0.0137  0.0347  155 VAL   A CG2 
3546 C  CG2 B VAL   A 155 ? 0.1830 0.1846 0.1228 0.0063  0.0076  -0.0047 155 VAL   A CG2 
3547 C  CG2 T VAL   A 155 ? 0.1883 0.1715 0.1746 -0.0105 0.0048  0.0224  155 VAL   A CG2 
3573 N  N   A PHE   A 156 ? 0.1642 0.1649 0.2474 0.0276  0.0212  0.0806  156 PHE   A N   
3574 N  N   B PHE   A 156 ? 0.1847 0.1743 0.1768 -0.0064 -0.0314 0.0295  156 PHE   A N   
3575 N  N   T PHE   A 156 ? 0.1985 0.1750 0.1921 0.0041  0.0553  0.0598  156 PHE   A N   
3576 C  CA  A PHE   A 156 ? 0.1875 0.1768 0.2770 0.0306  0.0206  0.0815  156 PHE   A CA  
3577 C  CA  B PHE   A 156 ? 0.2040 0.1766 0.2103 -0.0091 -0.0233 0.0257  156 PHE   A CA  
3578 C  CA  T PHE   A 156 ? 0.2140 0.1745 0.1910 0.0104  0.0616  0.0610  156 PHE   A CA  
3579 C  C   A PHE   A 156 ? 0.1890 0.1763 0.2745 0.0376  0.0382  0.0737  156 PHE   A C   
3580 C  C   B PHE   A 156 ? 0.2060 0.1842 0.2014 -0.0038 -0.0239 0.0214  156 PHE   A C   
3581 C  C   T PHE   A 156 ? 0.2116 0.1787 0.1991 0.0181  0.0773  0.0621  156 PHE   A C   
3582 O  O   A PHE   A 156 ? 0.1939 0.1765 0.2837 0.0176  0.0534  0.0567  156 PHE   A O   
3583 O  O   B PHE   A 156 ? 0.2105 0.1850 0.2024 -0.0037 -0.0291 0.0027  156 PHE   A O   
3584 O  O   T PHE   A 156 ? 0.2187 0.1786 0.1982 0.0194  0.0879  0.0481  156 PHE   A O   
3585 C  CB  A PHE   A 156 ? 0.2062 0.1911 0.2910 0.0285  0.0063  0.0761  156 PHE   A CB  
3586 C  CB  B PHE   A 156 ? 0.2127 0.1762 0.2303 -0.0115 -0.0136 0.0342  156 PHE   A CB  
3587 C  CB  T PHE   A 156 ? 0.2227 0.1664 0.1868 0.0098  0.0545  0.0569  156 PHE   A CB  
3588 C  CG  A PHE   A 156 ? 0.2244 0.2040 0.3088 0.0314  -0.0024 0.0638  156 PHE   A CG  
3589 C  CG  B PHE   A 156 ? 0.2209 0.1752 0.2422 -0.0114 -0.0093 0.0428  156 PHE   A CG  
3590 C  CG  T PHE   A 156 ? 0.2301 0.1600 0.1707 0.0141  0.0448  0.0748  156 PHE   A CG  
3591 C  CD1 A PHE   A 156 ? 0.2320 0.2097 0.3045 0.0344  0.0113  0.0509  156 PHE   A CD1 
3592 C  CD1 B PHE   A 156 ? 0.2210 0.1745 0.2464 -0.0167 -0.0049 0.0457  156 PHE   A CD1 
3593 C  CD1 T PHE   A 156 ? 0.2365 0.1633 0.1976 0.0106  0.0352  0.0697  156 PHE   A CD1 
3594 C  CD2 A PHE   A 156 ? 0.2343 0.2162 0.3098 0.0366  -0.0131 0.0636  156 PHE   A CD2 
3595 C  CD2 B PHE   A 156 ? 0.2274 0.1801 0.2580 -0.0113 -0.0118 0.0410  156 PHE   A CD2 
3596 C  CD2 T PHE   A 156 ? 0.2332 0.1615 0.1771 0.0219  0.0380  0.0815  156 PHE   A CD2 
3597 C  CE1 A PHE   A 156 ? 0.2412 0.2166 0.3131 0.0364  0.0177  0.0459  156 PHE   A CE1 
3598 C  CE1 B PHE   A 156 ? 0.2230 0.1735 0.2575 -0.0205 0.0007  0.0425  156 PHE   A CE1 
3599 C  CE1 T PHE   A 156 ? 0.2419 0.1630 0.2217 0.0126  0.0287  0.0589  156 PHE   A CE1 
3600 C  CE2 A PHE   A 156 ? 0.2454 0.2259 0.3155 0.0371  -0.0059 0.0502  156 PHE   A CE2 
3601 C  CE2 B PHE   A 156 ? 0.2326 0.1781 0.2724 -0.0150 -0.0104 0.0366  156 PHE   A CE2 
3602 C  CE2 T PHE   A 156 ? 0.2387 0.1636 0.2023 0.0213  0.0326  0.0678  156 PHE   A CE2 
3603 C  CZ  A PHE   A 156 ? 0.2466 0.2267 0.3124 0.0376  0.0126  0.0447  156 PHE   A CZ  
3604 C  CZ  B PHE   A 156 ? 0.2281 0.1702 0.2707 -0.0202 -0.0019 0.0425  156 PHE   A CZ  
3605 C  CZ  T PHE   A 156 ? 0.2408 0.1589 0.2230 0.0147  0.0302  0.0587  156 PHE   A CZ  
3633 N  N   A ASP   A 157 ? 0.1895 0.1864 0.2706 0.0577  0.0337  0.0794  157 ASP   A N   
3634 N  N   B ASP   A 157 ? 0.2005 0.1893 0.2050 0.0018  -0.0244 0.0319  157 ASP   A N   
3635 N  N   T ASP   A 157 ? 0.2002 0.1878 0.2056 0.0237  0.0686  0.0768  157 ASP   A N   
3636 C  CA  A ASP   A 157 ? 0.2024 0.2106 0.2779 0.0643  0.0342  0.0733  157 ASP   A CA  
3637 C  CA  B ASP   A 157 ? 0.2051 0.2054 0.2247 0.0094  -0.0134 0.0395  157 ASP   A CA  
3638 C  CA  T ASP   A 157 ? 0.1967 0.2011 0.2152 0.0351  0.0663  0.0831  157 ASP   A CA  
3639 C  C   A ASP   A 157 ? 0.1892 0.2320 0.2878 0.0608  0.0326  0.0791  157 ASP   A C   
3640 C  C   B ASP   A 157 ? 0.2053 0.2227 0.2434 0.0263  -0.0060 0.0526  157 ASP   A C   
3641 C  C   T ASP   A 157 ? 0.1927 0.2200 0.2283 0.0378  0.0632  0.0920  157 ASP   A C   
3642 O  O   A ASP   A 157 ? 0.1786 0.2317 0.2678 0.0507  0.0303  0.0854  157 ASP   A O   
3643 O  O   B ASP   A 157 ? 0.2054 0.2191 0.2357 0.0196  -0.0065 0.0559  157 ASP   A O   
3644 O  O   T ASP   A 157 ? 0.1841 0.2173 0.2200 0.0337  0.0597  0.0949  157 ASP   A O   
3645 C  CB  A ASP   A 157 ? 0.2302 0.2194 0.2852 0.0664  0.0334  0.0630  157 ASP   A CB  
3646 C  CB  B ASP   A 157 ? 0.2081 0.2031 0.2244 -0.0022 -0.0143 0.0293  157 ASP   A CB  
3647 C  CB  T ASP   A 157 ? 0.1991 0.1976 0.2207 0.0444  0.0605  0.0794  157 ASP   A CB  
3648 C  CG  A ASP   A 157 ? 0.2505 0.2257 0.2968 0.0687  0.0299  0.0657  157 ASP   A CG  
3649 C  CG  B ASP   A 157 ? 0.2053 0.2024 0.2245 -0.0112 -0.0195 0.0289  157 ASP   A CG  
3650 C  CG  T ASP   A 157 ? 0.1921 0.1890 0.2127 0.0556  0.0528  0.0703  157 ASP   A CG  
3651 O  OD1 A ASP   A 157 ? 0.2570 0.2292 0.3154 0.0695  0.0241  0.0679  157 ASP   A OD1 
3652 O  OD1 B ASP   A 157 ? 0.2030 0.2048 0.2333 -0.0134 -0.0254 0.0233  157 ASP   A OD1 
3653 O  OD1 T ASP   A 157 ? 0.1829 0.1788 0.2128 0.0594  0.0714  0.0456  157 ASP   A OD1 
3654 O  OD2 A ASP   A 157 ? 0.2532 0.2181 0.2997 0.0671  0.0321  0.0799  157 ASP   A OD2 
3655 O  OD2 B ASP   A 157 ? 0.2012 0.2031 0.2250 -0.0111 -0.0119 0.0414  157 ASP   A OD2 
3656 O  OD2 T ASP   A 157 ? 0.1859 0.1901 0.2184 0.0628  0.0311  0.0795  157 ASP   A OD2 
3669 N  N   A LYS   A 158 ? 0.2019 0.2571 0.3200 0.0568  0.0499  0.0694  158 LYS   A N   
3670 N  N   B LYS   A 158 ? 0.2124 0.2438 0.2728 0.0444  0.0118  0.0609  158 LYS   A N   
3671 N  N   T LYS   A 158 ? 0.2081 0.2445 0.2599 0.0371  0.0692  0.0856  158 LYS   A N   
3672 C  CA  A LYS   A 158 ? 0.2033 0.2847 0.3375 0.0591  0.0639  0.0648  158 LYS   A CA  
3673 C  CA  B LYS   A 158 ? 0.2187 0.2704 0.2893 0.0545  0.0277  0.0654  158 LYS   A CA  
3674 C  CA  T LYS   A 158 ? 0.2207 0.2734 0.2894 0.0408  0.0626  0.0719  158 LYS   A CA  
3675 C  C   A LYS   A 158 ? 0.1873 0.2947 0.3254 0.0634  0.0537  0.0790  158 LYS   A C   
3676 C  C   B LYS   A 158 ? 0.2080 0.2731 0.2775 0.0576  0.0218  0.0781  158 LYS   A C   
3677 C  C   T LYS   A 158 ? 0.2167 0.2803 0.2859 0.0442  0.0495  0.0753  158 LYS   A C   
3678 O  O   A LYS   A 158 ? 0.1826 0.3015 0.3278 0.0569  0.0550  0.0860  158 LYS   A O   
3679 O  O   B LYS   A 158 ? 0.2061 0.2793 0.2731 0.0524  0.0262  0.0826  158 LYS   A O   
3680 O  O   T LYS   A 158 ? 0.2162 0.2834 0.2889 0.0425  0.0480  0.0777  158 LYS   A O   
3681 C  CB  A LYS   A 158 ? 0.2211 0.2963 0.3657 0.0545  0.0802  0.0617  158 LYS   A CB  
3682 C  CB  B LYS   A 158 ? 0.2382 0.2923 0.3302 0.0514  0.0453  0.0543  158 LYS   A CB  
3683 C  CB  T LYS   A 158 ? 0.2417 0.2924 0.3341 0.0371  0.0637  0.0561  158 LYS   A CB  
3684 C  CG  A LYS   A 158 ? 0.2437 0.3061 0.3943 0.0534  0.0898  0.0591  158 LYS   A CG  
3685 C  CG  B LYS   A 158 ? 0.2590 0.3108 0.3657 0.0513  0.0559  0.0478  158 LYS   A CG  
3686 C  CG  T LYS   A 158 ? 0.2637 0.3086 0.3734 0.0365  0.0653  0.0484  158 LYS   A CG  
3687 C  CD  A LYS   A 158 ? 0.2584 0.3128 0.4104 0.0543  0.1016  0.0629  158 LYS   A CD  
3688 C  CD  B LYS   A 158 ? 0.2763 0.3235 0.3911 0.0530  0.0644  0.0483  158 LYS   A CD  
3689 C  CD  T LYS   A 158 ? 0.2810 0.3202 0.4044 0.0397  0.0643  0.0474  158 LYS   A CD  
3690 C  CE  A LYS   A 158 ? 0.2651 0.3126 0.4246 0.0497  0.1079  0.0750  158 LYS   A CE  
3691 C  CE  B LYS   A 158 ? 0.2858 0.3280 0.4148 0.0541  0.0665  0.0506  158 LYS   A CE  
3692 C  CE  T LYS   A 158 ? 0.2921 0.3247 0.4321 0.0407  0.0588  0.0470  158 LYS   A CE  
3693 N  NZ  A LYS   A 158 ? 0.2642 0.3111 0.4265 0.0436  0.1187  0.0846  158 LYS   A NZ  
3694 N  NZ  B LYS   A 158 ? 0.2907 0.3302 0.4246 0.0556  0.0693  0.0491  158 LYS   A NZ  
3695 N  NZ  T LYS   A 158 ? 0.2971 0.3267 0.4434 0.0421  0.0576  0.0446  158 LYS   A NZ  
3735 N  N   A ASN   A 159 ? 0.1850 0.2987 0.3214 0.0613  0.0338  0.0862  159 ASN   A N   
3736 N  N   B ASN   A 159 ? 0.2086 0.2726 0.2886 0.0515  0.0114  0.0716  159 ASN   A N   
3737 N  N   T ASN   A 159 ? 0.2199 0.2859 0.2918 0.0406  0.0359  0.0719  159 ASN   A N   
3738 C  CA  A ASN   A 159 ? 0.1791 0.2977 0.2946 0.0582  0.0024  0.1074  159 ASN   A CA  
3739 C  CA  B ASN   A 159 ? 0.2120 0.2723 0.3003 0.0375  0.0013  0.0629  159 ASN   A CA  
3740 C  CA  T ASN   A 159 ? 0.2256 0.2894 0.2854 0.0337  0.0196  0.0774  159 ASN   A CA  
3741 C  C   A ASN   A 159 ? 0.1620 0.2956 0.2664 0.0483  -0.0033 0.1055  159 ASN   A C   
3742 C  C   B ASN   A 159 ? 0.1999 0.2652 0.2818 0.0270  0.0095  0.0563  159 ASN   A C   
3743 C  C   T ASN   A 159 ? 0.2261 0.2917 0.2726 0.0238  0.0239  0.0702  159 ASN   A C   
3744 O  O   A ASN   A 159 ? 0.1415 0.2948 0.2492 0.0540  -0.0184 0.0910  159 ASN   A O   
3745 O  O   B ASN   A 159 ? 0.1947 0.2609 0.2845 0.0155  0.0100  0.0450  159 ASN   A O   
3746 O  O   T ASN   A 159 ? 0.2217 0.2918 0.2684 0.0216  0.0275  0.0573  159 ASN   A O   
3747 C  CB  A ASN   A 159 ? 0.1968 0.3053 0.3138 0.0561  -0.0095 0.1125  159 ASN   A CB  
3748 C  CB  B ASN   A 159 ? 0.2299 0.2826 0.3308 0.0312  -0.0116 0.0548  159 ASN   A CB  
3749 C  CB  T ASN   A 159 ? 0.2343 0.2935 0.2988 0.0333  0.0059  0.0831  159 ASN   A CB  
3750 C  CG  A ASN   A 159 ? 0.2135 0.3148 0.3456 0.0531  -0.0154 0.1029  159 ASN   A CG  
3751 C  CG  B ASN   A 159 ? 0.2453 0.2937 0.3632 0.0244  -0.0176 0.0426  159 ASN   A CG  
3752 C  CG  T ASN   A 159 ? 0.2428 0.2975 0.3189 0.0327  -0.0047 0.0814  159 ASN   A CG  
3753 O  OD1 A ASN   A 159 ? 0.2188 0.3239 0.3597 0.0554  -0.0046 0.0996  159 ASN   A OD1 
3754 O  OD1 B ASN   A 159 ? 0.2535 0.3039 0.3727 0.0210  -0.0208 0.0379  159 ASN   A OD1 
3755 O  OD1 T ASN   A 159 ? 0.2455 0.3043 0.3298 0.0339  0.0041  0.0787  159 ASN   A OD1 
3756 N  ND2 A ASN   A 159 ? 0.2167 0.3174 0.3624 0.0490  -0.0211 0.0924  159 ASN   A ND2 
3757 N  ND2 B ASN   A 159 ? 0.2460 0.2955 0.3827 0.0216  -0.0169 0.0322  159 ASN   A ND2 
3758 N  ND2 T ASN   A 159 ? 0.2434 0.2982 0.3281 0.0315  -0.0150 0.0786  159 ASN   A ND2 
3777 N  N   A LEU   A 160 ? 0.1542 0.2836 0.2514 0.0412  -0.0031 0.1205  160 LEU   A N   
3778 N  N   B LEU   A 160 ? 0.1886 0.2575 0.2678 0.0316  0.0115  0.0613  160 LEU   A N   
3779 N  N   T LEU   A 160 ? 0.2250 0.2876 0.2697 0.0180  0.0227  0.0758  160 LEU   A N   
3780 C  CA  A LEU   A 160 ? 0.1539 0.2724 0.2298 0.0286  0.0077  0.1207  160 LEU   A CA  
3781 C  CA  B LEU   A 160 ? 0.1824 0.2479 0.2379 0.0294  0.0142  0.0670  160 LEU   A CA  
3782 C  CA  T LEU   A 160 ? 0.2281 0.2829 0.2586 0.0100  0.0269  0.0787  160 LEU   A CA  
3783 C  C   A LEU   A 160 ? 0.1323 0.2640 0.2073 0.0213  0.0064  0.1116  160 LEU   A C   
3784 C  C   B LEU   A 160 ? 0.1695 0.2370 0.2039 0.0232  0.0181  0.0642  160 LEU   A C   
3785 O  O   A LEU   A 160 ? 0.1194 0.2760 0.1928 0.0142  0.0028  0.1168  160 LEU   A O   
3786 O  O   B LEU   A 160 ? 0.1580 0.2401 0.1806 0.0199  0.0128  0.0766  160 LEU   A O   
3787 C  CB  A LEU   A 160 ? 0.1521 0.2726 0.2274 0.0277  0.0062  0.1175  160 LEU   A CB  
3788 C  CB  B LEU   A 160 ? 0.1897 0.2520 0.2482 0.0216  0.0177  0.0666  160 LEU   A CB  
3789 C  CB  T LEU   A 160 ? 0.2252 0.2814 0.2470 0.0027  0.0267  0.0787  160 LEU   A CB  
3790 C  CG  A LEU   A 160 ? 0.1565 0.2831 0.2488 0.0153  0.0080  0.0859  160 LEU   A CG  
3791 C  CG  B LEU   A 160 ? 0.1977 0.2573 0.2637 0.0098  0.0160  0.0508  160 LEU   A CG  
3792 C  CG  T LEU   A 160 ? 0.2249 0.2845 0.2480 -0.0068 0.0278  0.0666  160 LEU   A CG  
3793 C  CD1 A LEU   A 160 ? 0.1722 0.2897 0.2600 0.0066  0.0080  0.0723  160 LEU   A CD1 
3794 C  CD1 B LEU   A 160 ? 0.2044 0.2592 0.2699 0.0016  0.0189  0.0383  160 LEU   A CD1 
3795 C  CD1 T LEU   A 160 ? 0.2311 0.2877 0.2535 -0.0093 0.0273  0.0585  160 LEU   A CD1 
3796 C  CD2 A LEU   A 160 ? 0.1469 0.2850 0.2533 0.0131  0.0151  0.0746  160 LEU   A CD2 
3797 C  CD2 B LEU   A 160 ? 0.1997 0.2580 0.2665 0.0065  0.0162  0.0496  160 LEU   A CD2 
3798 C  CD2 T LEU   A 160 ? 0.2186 0.2832 0.2462 -0.0110 0.0343  0.0649  160 LEU   A CD2 
3831 N  N   A TYR   A 161 ? 0.1448 0.2486 0.2228 0.0113  0.0183  0.0911  161 TYR   A N   
3832 N  N   B TYR   A 161 ? 0.1779 0.2247 0.1964 0.0164  0.0173  0.0511  161 TYR   A N   
3833 C  CA  A TYR   A 161 ? 0.1531 0.2397 0.2136 0.0011  0.0248  0.0799  161 TYR   A CA  
3834 C  CA  B TYR   A 161 ? 0.1812 0.2164 0.1859 0.0085  0.0230  0.0309  161 TYR   A CA  
3835 C  C   A TYR   A 161 ? 0.1525 0.2602 0.2202 -0.0003 0.0178  0.0777  161 TYR   A C   
3836 C  C   B TYR   A 161 ? 0.1857 0.2313 0.1852 -0.0003 0.0273  0.0264  161 TYR   A C   
3837 O  O   A TYR   A 161 ? 0.1513 0.2637 0.2083 -0.0092 0.0098  0.0759  161 TYR   A O   
3838 O  O   B TYR   A 161 ? 0.1826 0.2296 0.1662 -0.0033 0.0403  0.0192  161 TYR   A O   
3839 C  CB  A TYR   A 161 ? 0.1641 0.2261 0.2076 -0.0006 0.0350  0.0668  161 TYR   A CB  
3840 C  CB  B TYR   A 161 ? 0.1822 0.2027 0.1862 0.0119  0.0286  0.0134  161 TYR   A CB  
3841 C  CG  A TYR   A 161 ? 0.1612 0.2111 0.1942 -0.0043 0.0223  0.0448  161 TYR   A CG  
3842 C  CG  B TYR   A 161 ? 0.1780 0.1860 0.1836 0.0125  0.0248  0.0065  161 TYR   A CG  
3843 C  CD1 A TYR   A 161 ? 0.1605 0.1976 0.1926 -0.0086 0.0159  0.0357  161 TYR   A CD1 
3844 C  CD1 B TYR   A 161 ? 0.1792 0.1802 0.1796 0.0108  0.0224  0.0015  161 TYR   A CD1 
3845 C  CD2 A TYR   A 161 ? 0.1580 0.2106 0.1961 0.0027  0.0212  0.0281  161 TYR   A CD2 
3846 C  CD2 B TYR   A 161 ? 0.1760 0.1781 0.1846 0.0129  0.0259  0.0155  161 TYR   A CD2 
3847 C  CE1 A TYR   A 161 ? 0.1595 0.1874 0.1865 -0.0074 0.0096  0.0299  161 TYR   A CE1 
3848 C  CE1 B TYR   A 161 ? 0.1833 0.1770 0.1800 0.0123  0.0231  0.0002  161 TYR   A CE1 
3849 C  CE2 A TYR   A 161 ? 0.1582 0.1967 0.1913 -0.0086 0.0189  0.0318  161 TYR   A CE2 
3850 C  CE2 B TYR   A 161 ? 0.1795 0.1725 0.1857 0.0062  0.0294  0.0194  161 TYR   A CE2 
3851 C  CZ  A TYR   A 161 ? 0.1655 0.1852 0.1757 -0.0103 0.0062  0.0307  161 TYR   A CZ  
3852 C  CZ  B TYR   A 161 ? 0.1876 0.1747 0.1892 0.0103  0.0248  0.0112  161 TYR   A CZ  
3853 O  OH  A TYR   A 161 ? 0.1841 0.1810 0.1829 -0.0107 0.0004  0.0330  161 TYR   A OH  
3854 O  OH  B TYR   A 161 ? 0.1995 0.1718 0.2073 0.0091  0.0178  0.0125  161 TYR   A OH  
3873 N  N   A ASP   A 162 ? 0.1478 0.2826 0.2515 0.0069  0.0340  0.0805  162 ASP   A N   
3874 N  N   B ASP   A 162 ? 0.1903 0.2518 0.2055 -0.0034 0.0281  0.0281  162 ASP   A N   
3875 C  CA  A ASP   A 162 ? 0.1461 0.3109 0.2724 0.0016  0.0369  0.0709  162 ASP   A CA  
3876 C  CA  B ASP   A 162 ? 0.1963 0.2717 0.2273 -0.0084 0.0245  0.0285  162 ASP   A CA  
3877 C  C   A ASP   A 162 ? 0.1417 0.3196 0.2497 -0.0079 0.0253  0.0726  162 ASP   A C   
3878 C  C   B ASP   A 162 ? 0.2033 0.2798 0.2200 -0.0098 0.0205  0.0353  162 ASP   A C   
3879 O  O   A ASP   A 162 ? 0.1434 0.3192 0.2455 -0.0087 0.0234  0.0563  162 ASP   A O   
3880 O  O   B ASP   A 162 ? 0.2048 0.2768 0.2031 -0.0079 0.0196  0.0290  162 ASP   A O   
3881 C  CB  A ASP   A 162 ? 0.1534 0.3352 0.3134 0.0116  0.0464  0.0497  162 ASP   A CB  
3882 C  CB  B ASP   A 162 ? 0.1986 0.2843 0.2553 -0.0104 0.0302  0.0190  162 ASP   A CB  
3883 C  CG  A ASP   A 162 ? 0.1664 0.3574 0.3516 0.0143  0.0566  0.0243  162 ASP   A CG  
3884 C  CG  B ASP   A 162 ? 0.2028 0.2927 0.2759 -0.0161 0.0341  0.0137  162 ASP   A CG  
3885 O  OD1 A ASP   A 162 ? 0.1768 0.3583 0.3612 0.0003  0.0557  0.0188  162 ASP   A OD1 
3886 O  OD1 B ASP   A 162 ? 0.2083 0.2996 0.2842 -0.0225 0.0324  0.0073  162 ASP   A OD1 
3887 O  OD2 A ASP   A 162 ? 0.1742 0.3709 0.3756 0.0200  0.0707  0.0131  162 ASP   A OD2 
3888 O  OD2 B ASP   A 162 ? 0.1992 0.2897 0.2953 -0.0208 0.0462  0.0216  162 ASP   A OD2 
3897 N  N   A LYS   A 163 ? 0.1482 0.3316 0.2557 -0.0030 -0.0016 0.0762  163 LYS   A N   
3898 N  N   B LYS   A 163 ? 0.2116 0.2896 0.2291 -0.0081 0.0121  0.0442  163 LYS   A N   
3899 C  CA  A LYS   A 163 ? 0.1583 0.3363 0.2512 -0.0064 -0.0104 0.0698  163 LYS   A CA  
3900 C  CA  B LYS   A 163 ? 0.2193 0.2967 0.2475 -0.0099 0.0061  0.0492  163 LYS   A CA  
3901 C  C   A LYS   A 163 ? 0.1614 0.3198 0.2192 -0.0218 -0.0031 0.0730  163 LYS   A C   
3902 C  C   B LYS   A 163 ? 0.2169 0.2958 0.2356 -0.0128 0.0081  0.0522  163 LYS   A C   
3903 O  O   A LYS   A 163 ? 0.1550 0.3187 0.2067 -0.0329 0.0050  0.0718  163 LYS   A O   
3904 O  O   B LYS   A 163 ? 0.2166 0.3005 0.2285 -0.0086 0.0085  0.0566  163 LYS   A O   
3905 C  CB  A LYS   A 163 ? 0.1833 0.3517 0.2921 0.0164  -0.0183 0.0545  163 LYS   A CB  
3906 C  CB  B LYS   A 163 ? 0.2329 0.3028 0.2826 -0.0040 0.0061  0.0461  163 LYS   A CB  
3907 C  CG  A LYS   A 163 ? 0.2167 0.3663 0.3487 0.0155  -0.0130 0.0420  163 LYS   A CG  
3908 C  CG  B LYS   A 163 ? 0.2483 0.3100 0.3173 -0.0001 0.0093  0.0395  163 LYS   A CG  
3909 C  CD  A LYS   A 163 ? 0.2437 0.3773 0.3978 0.0117  -0.0115 0.0390  163 LYS   A CD  
3910 C  CD  B LYS   A 163 ? 0.2593 0.3174 0.3524 0.0023  0.0109  0.0287  163 LYS   A CD  
3911 C  CE  A LYS   A 163 ? 0.2637 0.3858 0.4442 0.0026  -0.0073 0.0325  163 LYS   A CE  
3912 C  CE  B LYS   A 163 ? 0.2637 0.3237 0.3747 0.0063  0.0106  0.0183  163 LYS   A CE  
3913 N  NZ  A LYS   A 163 ? 0.2742 0.3927 0.4666 -0.0056 -0.0107 0.0243  163 LYS   A NZ  
3914 N  NZ  B LYS   A 163 ? 0.2667 0.3283 0.3891 0.0083  0.0091  0.0153  163 LYS   A NZ  
3941 N  N   A LEU   A 164 ? 0.1445 0.2922 0.1931 -0.0245 0.0002  0.0697  164 LEU   A N   
3942 N  N   B LEU   A 164 ? 0.2109 0.2859 0.2439 -0.0178 0.0125  0.0484  164 LEU   A N   
3943 C  CA  A LEU   A 164 ? 0.1494 0.2747 0.1823 -0.0305 0.0190  0.0574  164 LEU   A CA  
3944 C  CA  B LEU   A 164 ? 0.2141 0.2760 0.2321 -0.0238 0.0172  0.0544  164 LEU   A CA  
3945 C  C   A LEU   A 164 ? 0.1615 0.2725 0.1725 -0.0312 0.0128  0.0464  164 LEU   A C   
3946 C  C   B LEU   A 164 ? 0.2200 0.2756 0.2345 -0.0289 0.0167  0.0561  164 LEU   A C   
3947 O  O   A LEU   A 164 ? 0.1612 0.2703 0.1634 -0.0383 0.0287  0.0256  164 LEU   A O   
3948 O  O   B LEU   A 164 ? 0.2221 0.2765 0.2304 -0.0347 0.0200  0.0530  164 LEU   A O   
3949 C  CB  A LEU   A 164 ? 0.1434 0.2591 0.1848 -0.0296 0.0249  0.0630  164 LEU   A CB  
3950 C  CB  B LEU   A 164 ? 0.2105 0.2675 0.2281 -0.0215 0.0224  0.0562  164 LEU   A CB  
3951 C  CG  A LEU   A 164 ? 0.1467 0.2459 0.2086 -0.0217 0.0136  0.0578  164 LEU   A CG  
3952 C  CG  B LEU   A 164 ? 0.2099 0.2617 0.2320 -0.0168 0.0257  0.0512  164 LEU   A CG  
3953 C  CD1 A LEU   A 164 ? 0.1398 0.2377 0.2014 -0.0136 -0.0015 0.0715  164 LEU   A CD1 
3954 C  CD1 B LEU   A 164 ? 0.2065 0.2616 0.2369 -0.0106 0.0232  0.0435  164 LEU   A CD1 
3955 C  CD2 A LEU   A 164 ? 0.1539 0.2449 0.2135 -0.0317 0.0313  0.0426  164 LEU   A CD2 
3956 C  CD2 B LEU   A 164 ? 0.2137 0.2601 0.2287 -0.0196 0.0312  0.0487  164 LEU   A CD2 
3979 N  N   A VAL   A 165 ? 0.1502 0.2692 0.1762 -0.0349 0.0199  0.0516  165 VAL   A N   
3980 N  N   B VAL   A 165 ? 0.2215 0.2769 0.2447 -0.0283 0.0119  0.0525  165 VAL   A N   
3981 C  CA  A VAL   A 165 ? 0.1596 0.2655 0.1616 -0.0324 0.0267  0.0489  165 VAL   A CA  
3982 C  CA  B VAL   A 165 ? 0.2288 0.2788 0.2638 -0.0260 0.0035  0.0456  165 VAL   A CA  
3983 C  C   A VAL   A 165 ? 0.1506 0.2733 0.1700 -0.0276 0.0322  0.0550  165 VAL   A C   
3984 C  C   B VAL   A 165 ? 0.2275 0.2834 0.2757 -0.0218 -0.0078 0.0400  165 VAL   A C   
3985 O  O   A VAL   A 165 ? 0.1388 0.2621 0.1637 -0.0287 0.0359  0.0488  165 VAL   A O   
3986 O  O   B VAL   A 165 ? 0.2378 0.2878 0.3004 -0.0258 -0.0138 0.0388  165 VAL   A O   
3987 C  CB  A VAL   A 165 ? 0.1798 0.2571 0.1702 -0.0361 0.0298  0.0334  165 VAL   A CB  
3988 C  CB  B VAL   A 165 ? 0.2396 0.2803 0.2729 -0.0253 0.0038  0.0414  165 VAL   A CB  
3989 C  CG1 A VAL   A 165 ? 0.1834 0.2579 0.1645 -0.0420 0.0255  0.0153  165 VAL   A CG1 
3990 C  CG1 B VAL   A 165 ? 0.2437 0.2845 0.2696 -0.0243 0.0029  0.0373  165 VAL   A CG1 
3991 C  CG2 A VAL   A 165 ? 0.1940 0.2528 0.1784 -0.0310 0.0234  0.0411  165 VAL   A CG2 
3992 C  CG2 B VAL   A 165 ? 0.2438 0.2772 0.2766 -0.0257 0.0036  0.0403  165 VAL   A CG2 
4011 N  N   A SER   A 166 ? 0.1392 0.2879 0.2044 -0.0242 0.0294  0.0492  166 SER   A N   
4012 N  N   B SER   A 166 ? 0.2116 0.2832 0.2660 -0.0151 -0.0119 0.0384  166 SER   A N   
4013 C  CA  A SER   A 166 ? 0.1415 0.3042 0.2267 -0.0249 0.0320  0.0409  166 SER   A CA  
4014 C  CA  B SER   A 166 ? 0.1995 0.2860 0.2485 -0.0112 -0.0183 0.0339  166 SER   A CA  
4015 C  C   A SER   A 166 ? 0.1331 0.3230 0.2408 -0.0153 0.0162  0.0234  166 SER   A C   
4016 C  C   B SER   A 166 ? 0.1918 0.2887 0.2327 -0.0034 -0.0320 0.0289  166 SER   A C   
4017 O  O   A SER   A 166 ? 0.1459 0.3346 0.2924 -0.0210 0.0223  -0.0035 166 SER   A O   
4018 O  O   B SER   A 166 ? 0.1831 0.2821 0.2239 -0.0010 -0.0427 0.0269  166 SER   A O   
4019 C  CB  A SER   A 166 ? 0.1519 0.3051 0.2455 -0.0189 0.0183  0.0346  166 SER   A CB  
4020 C  CB  B SER   A 166 ? 0.1924 0.2884 0.2526 -0.0108 -0.0204 0.0285  166 SER   A CB  
4021 O  OG  A SER   A 166 ? 0.1721 0.3103 0.2704 -0.0168 0.0125  0.0401  166 SER   A OG  
4022 O  OG  B SER   A 166 ? 0.1844 0.2900 0.2656 -0.0145 -0.0220 0.0308  166 SER   A OG  
4033 N  N   A SER   A 167 ? 0.1451 0.3318 0.2194 0.0105  0.0035  0.0281  167 SER   A N   
4034 N  N   B SER   A 167 ? 0.2000 0.3031 0.2303 0.0058  -0.0285 0.0312  167 SER   A N   
4035 C  CA  A SER   A 167 ? 0.1744 0.3395 0.2191 0.0182  -0.0047 0.0196  167 SER   A CA  
4036 C  CA  B SER   A 167 ? 0.2097 0.3163 0.2329 0.0140  -0.0222 0.0293  167 SER   A CA  
4037 C  C   A SER   A 167 ? 0.1884 0.3439 0.2303 0.0270  0.0110  0.0178  167 SER   A C   
4038 C  C   B SER   A 167 ? 0.2028 0.3282 0.2357 0.0228  -0.0016 0.0238  167 SER   A C   
4039 O  O   A SER   A 167 ? 0.2070 0.3503 0.2440 0.0328  0.0099  0.0326  167 SER   A O   
4040 O  O   B SER   A 167 ? 0.2122 0.3272 0.2416 0.0257  -0.0041 0.0330  167 SER   A O   
4041 C  CB  A SER   A 167 ? 0.1784 0.3452 0.2326 0.0198  0.0094  0.0300  167 SER   A CB  
4042 C  CB  B SER   A 167 ? 0.2221 0.3194 0.2480 0.0169  -0.0244 0.0379  167 SER   A CB  
4043 O  OG  A SER   A 167 ? 0.1776 0.3511 0.2236 0.0189  0.0319  0.0353  167 SER   A OG  
4044 O  OG  B SER   A 167 ? 0.2304 0.3217 0.2577 0.0176  -0.0247 0.0393  167 SER   A OG  
4055 N  N   . PHE   A 168 ? 0.1909 0.3420 0.2285 0.0328  0.0083  0.0174  168 PHE   A N   
4056 C  CA  . PHE   A 168 ? 0.1927 0.3500 0.2424 0.0183  0.0221  0.0208  168 PHE   A CA  
4057 C  C   . PHE   A 168 ? 0.2228 0.3750 0.3000 -0.0034 0.0687  0.0060  168 PHE   A C   
4058 O  O   . PHE   A 168 ? 0.2242 0.3724 0.3520 -0.0182 0.0755  0.0240  168 PHE   A O   
4059 C  CB  . PHE   A 168 ? 0.1873 0.3360 0.2117 0.0097  0.0109  0.0293  168 PHE   A CB  
4060 C  CG  . PHE   A 168 ? 0.1778 0.3203 0.2016 0.0001  -0.0012 0.0322  168 PHE   A CG  
4061 C  CD1 . PHE   A 168 ? 0.1779 0.3184 0.2166 -0.0087 -0.0083 0.0369  168 PHE   A CD1 
4062 C  CD2 . PHE   A 168 ? 0.1747 0.3133 0.1975 -0.0053 0.0224  0.0301  168 PHE   A CD2 
4063 C  CE1 . PHE   A 168 ? 0.1679 0.3112 0.2174 -0.0131 -0.0081 0.0465  168 PHE   A CE1 
4064 C  CE2 . PHE   A 168 ? 0.1842 0.3039 0.2237 -0.0048 0.0146  0.0404  168 PHE   A CE2 
4065 C  CZ  . PHE   A 168 ? 0.1754 0.3030 0.2324 -0.0145 0.0067  0.0465  168 PHE   A CZ  
4076 N  N   A LEU   A 169 ? 0.2584 0.3896 0.3450 -0.0172 0.0624  -0.0172 169 LEU   A N   
4077 N  N   B LEU   A 169 ? 0.2681 0.3910 0.3542 -0.0120 0.0490  -0.0032 169 LEU   A N   
4078 C  CA  A LEU   A 169 ? 0.3248 0.4135 0.4170 -0.0192 0.0297  -0.0256 169 LEU   A CA  
4079 C  CA  B LEU   A 169 ? 0.3163 0.4103 0.4082 -0.0153 0.0215  -0.0056 169 LEU   A CA  
4080 C  C   A LEU   A 169 ? 0.3325 0.4146 0.4450 -0.0176 0.0215  -0.0137 169 LEU   A C   
4081 C  C   B LEU   A 169 ? 0.3272 0.4123 0.4245 -0.0175 0.0110  0.0017  169 LEU   A C   
4082 O  O   A LEU   A 169 ? 0.3428 0.4094 0.4600 -0.0160 0.0207  -0.0144 169 LEU   A O   
4083 O  O   B LEU   A 169 ? 0.3260 0.4086 0.4352 -0.0183 0.0085  0.0032  169 LEU   A O   
4084 C  CB  A LEU   A 169 ? 0.3646 0.4287 0.4523 -0.0232 0.0085  -0.0455 169 LEU   A CB  
4085 C  CB  B LEU   A 169 ? 0.3456 0.4220 0.4418 -0.0172 0.0081  -0.0152 169 LEU   A CB  
4086 C  CG  A LEU   A 169 ? 0.3895 0.4396 0.4684 -0.0253 -0.0043 -0.0620 169 LEU   A CG  
4087 C  CG  B LEU   A 169 ? 0.3668 0.4301 0.4585 -0.0183 -0.0003 -0.0242 169 LEU   A CG  
4088 C  CD1 A LEU   A 169 ? 0.4076 0.4458 0.4837 -0.0238 -0.0085 -0.0664 169 LEU   A CD1 
4089 C  CD1 B LEU   A 169 ? 0.3796 0.4351 0.4708 -0.0172 -0.0033 -0.0270 169 LEU   A CD1 
4090 C  CD2 A LEU   A 169 ? 0.3991 0.4404 0.4771 -0.0282 -0.0050 -0.0659 169 LEU   A CD2 
4091 C  CD2 B LEU   A 169 ? 0.3679 0.4301 0.4676 -0.0200 -0.0014 -0.0270 169 LEU   A CD2 
4092 O  OXT A LEU   A 169 ? 0.3293 0.4189 0.4541 -0.0176 0.0215  -0.0095 169 LEU   A OXT 
4093 O  OXT B LEU   A 169 ? 0.3344 0.4166 0.4294 -0.0191 0.0080  0.0038  169 LEU   A OXT 
4116 N  N   A SER   B 1   ? 0.3533 0.3677 0.3588 -0.1265 -0.0741 0.0314  1   SER   B N   
4117 N  N   B SER   B 1   ? 0.3306 0.3474 0.3508 -0.0732 -0.0474 0.0229  1   SER   B N   
4118 C  CA  A SER   B 1   ? 0.3437 0.3699 0.3471 -0.1306 -0.0902 0.0285  1   SER   B CA  
4119 C  CA  B SER   B 1   ? 0.3253 0.3477 0.3370 -0.0745 -0.0502 0.0231  1   SER   B CA  
4120 C  C   A SER   B 1   ? 0.3190 0.3693 0.3402 -0.1307 -0.0966 0.0457  1   SER   B C   
4121 C  C   B SER   B 1   ? 0.3129 0.3465 0.3307 -0.0721 -0.0548 0.0331  1   SER   B C   
4122 O  O   A SER   B 1   ? 0.3336 0.3730 0.3277 -0.1142 -0.0813 0.0510  1   SER   B O   
4123 O  O   B SER   B 1   ? 0.3166 0.3460 0.3183 -0.0683 -0.0531 0.0323  1   SER   B O   
4124 C  CB  A SER   B 1   ? 0.3532 0.3688 0.3809 -0.1300 -0.0817 0.0112  1   SER   B CB  
4125 C  CB  B SER   B 1   ? 0.3290 0.3470 0.3627 -0.0755 -0.0427 0.0123  1   SER   B CB  
4126 O  OG  A SER   B 1   ? 0.3685 0.3788 0.4177 -0.1255 -0.0555 0.0008  1   SER   B OG  
4127 O  OG  B SER   B 1   ? 0.3351 0.3511 0.3777 -0.0760 -0.0332 0.0041  1   SER   B OG  
4142 N  N   A MET   B 2   ? 0.2934 0.3634 0.3392 -0.1353 -0.0944 0.0818  2   MET   B N   
4143 N  N   B MET   B 2   ? 0.3002 0.3449 0.3255 -0.0703 -0.0533 0.0536  2   MET   B N   
4144 C  CA  A MET   B 2   ? 0.2799 0.3586 0.3522 -0.1104 -0.0981 0.1080  2   MET   B CA  
4145 C  CA  B MET   B 2   ? 0.2880 0.3416 0.3238 -0.0608 -0.0503 0.0712  2   MET   B CA  
4146 C  C   A MET   B 2   ? 0.2502 0.3323 0.3271 -0.0841 -0.1055 0.1429  2   MET   B C   
4147 C  C   B MET   B 2   ? 0.2674 0.3225 0.2985 -0.0528 -0.0447 0.0811  2   MET   B C   
4148 O  O   A MET   B 2   ? 0.2469 0.3448 0.3270 -0.0667 -0.1175 0.1474  2   MET   B O   
4149 O  O   B MET   B 2   ? 0.2658 0.3269 0.2990 -0.0484 -0.0390 0.0792  2   MET   B O   
4150 C  CB  A MET   B 2   ? 0.3134 0.3907 0.4281 -0.0883 -0.0758 0.0851  2   MET   B CB  
4151 C  CB  B MET   B 2   ? 0.2996 0.3583 0.3571 -0.0526 -0.0491 0.0745  2   MET   B CB  
4152 C  CG  A MET   B 2   ? 0.3415 0.4198 0.5118 -0.0612 -0.0600 0.0744  2   MET   B CG  
4153 C  CG  B MET   B 2   ? 0.3081 0.3706 0.3879 -0.0419 -0.0504 0.0855  2   MET   B CG  
4154 S  SD  A MET   B 2   ? 0.3695 0.4443 0.5819 -0.0378 -0.0467 0.0596  2   MET   B SD  
4155 S  SD  B MET   B 2   ? 0.3177 0.3826 0.4133 -0.0317 -0.0531 0.0948  2   MET   B SD  
4156 C  CE  A MET   B 2   ? 0.3674 0.4485 0.5845 -0.0356 -0.0337 0.0558  2   MET   B CE  
4157 C  CE  B MET   B 2   ? 0.3144 0.3799 0.4183 -0.0325 -0.0479 0.0883  2   MET   B CE  
4176 N  N   A VAL   B 3   ? 0.2262 0.2919 0.3031 -0.0853 -0.0926 0.1562  3   VAL   B N   
4177 N  N   B VAL   B 3   ? 0.2485 0.2985 0.2765 -0.0509 -0.0446 0.0887  3   VAL   B N   
4178 C  CA  A VAL   B 3   ? 0.2165 0.2601 0.3061 -0.0782 -0.0792 0.1305  3   VAL   B CA  
4179 C  CA  B VAL   B 3   ? 0.2330 0.2770 0.2649 -0.0469 -0.0432 0.0835  3   VAL   B CA  
4180 C  C   A VAL   B 3   ? 0.1975 0.2479 0.2686 -0.0701 -0.0691 0.1049  3   VAL   B C   
4181 C  C   B VAL   B 3   ? 0.2108 0.2595 0.2374 -0.0479 -0.0445 0.0864  3   VAL   B C   
4182 O  O   A VAL   B 3   ? 0.1966 0.2462 0.2864 -0.0726 -0.0766 0.1045  3   VAL   B O   
4183 O  O   B VAL   B 3   ? 0.2118 0.2633 0.2237 -0.0393 -0.0459 0.0918  3   VAL   B O   
4184 C  CB  A VAL   B 3   ? 0.2338 0.2518 0.3688 -0.0812 -0.0753 0.1051  3   VAL   B CB  
4185 C  CB  B VAL   B 3   ? 0.2413 0.2737 0.2854 -0.0457 -0.0399 0.0745  3   VAL   B CB  
4186 C  CG1 A VAL   B 3   ? 0.2394 0.2367 0.3898 -0.0853 -0.0784 0.0980  3   VAL   B CG1 
4187 C  CG1 B VAL   B 3   ? 0.2450 0.2700 0.2975 -0.0465 -0.0403 0.0700  3   VAL   B CG1 
4188 C  CG2 A VAL   B 3   ? 0.2447 0.2627 0.3903 -0.0787 -0.0548 0.1079  3   VAL   B CG2 
4189 C  CG2 B VAL   B 3   ? 0.2450 0.2738 0.2905 -0.0454 -0.0335 0.0771  3   VAL   B CG2 
4208 N  N   . ASN   B 4   ? 0.1917 0.2357 0.2270 -0.0587 -0.0504 0.0873  4   ASN   B N   
4209 C  CA  . ASN   B 4   ? 0.1930 0.2252 0.2008 -0.0524 -0.0512 0.0498  4   ASN   B CA  
4210 C  C   . ASN   B 4   ? 0.2040 0.2289 0.1970 -0.0487 -0.0419 0.0397  4   ASN   B C   
4211 O  O   . ASN   B 4   ? 0.2043 0.2328 0.2153 -0.0436 -0.0347 0.0165  4   ASN   B O   
4212 C  CB  . ASN   B 4   ? 0.1951 0.2151 0.1900 -0.0450 -0.0660 0.0442  4   ASN   B CB  
4213 C  CG  . ASN   B 4   ? 0.1948 0.1991 0.1761 -0.0500 -0.0592 0.0339  4   ASN   B CG  
4214 O  OD1 . ASN   B 4   ? 0.2001 0.1821 0.1780 -0.0483 -0.0512 0.0324  4   ASN   B OD1 
4215 N  ND2 . ASN   B 4   ? 0.2150 0.2044 0.1911 -0.0241 -0.0416 0.0262  4   ASN   B ND2 
4223 N  N   . SER   B 5   ? 0.2214 0.2488 0.1937 -0.0532 -0.0216 0.0356  5   SER   B N   
4224 C  CA  . SER   B 5   ? 0.2492 0.2844 0.2237 -0.0434 -0.0059 0.0433  5   SER   B CA  
4225 C  C   . SER   B 5   ? 0.2659 0.2908 0.2627 -0.0604 0.0109  0.0530  5   SER   B C   
4226 O  O   . SER   B 5   ? 0.2766 0.2861 0.3465 -0.0519 0.0378  0.0452  5   SER   B O   
4227 C  CB  . SER   B 5   ? 0.2613 0.3100 0.2549 -0.0339 -0.0022 0.0564  5   SER   B CB  
4228 O  OG  . SER   B 5   ? 0.2882 0.3496 0.3143 -0.0215 -0.0042 0.0612  5   SER   B OG  
4234 N  N   . PHE   B 6   ? 0.2862 0.3130 0.2298 -0.0717 0.0217  0.0588  6   PHE   B N   
4235 C  CA  . PHE   B 6   ? 0.2954 0.3198 0.1906 -0.0949 0.0303  0.0336  6   PHE   B CA  
4236 C  C   . PHE   B 6   ? 0.3452 0.3542 0.2422 -0.0983 0.0510  -0.0040 6   PHE   B C   
4237 O  O   . PHE   B 6   ? 0.3599 0.3850 0.2739 -0.0841 0.0354  -0.0218 6   PHE   B O   
4238 C  CB  . PHE   B 6   ? 0.2660 0.2989 0.1902 -0.0869 0.0102  0.0284  6   PHE   B CB  
4239 C  CG  . PHE   B 6   ? 0.2273 0.2618 0.1791 -0.0792 -0.0083 0.0208  6   PHE   B CG  
4240 C  CD1 . PHE   B 6   ? 0.2250 0.2309 0.1712 -0.0707 -0.0251 0.0110  6   PHE   B CD1 
4241 C  CD2 . PHE   B 6   ? 0.1990 0.2572 0.1841 -0.0649 -0.0051 0.0435  6   PHE   B CD2 
4242 C  CE1 . PHE   B 6   ? 0.2166 0.2132 0.1762 -0.0535 -0.0273 0.0088  6   PHE   B CE1 
4243 C  CE2 . PHE   B 6   ? 0.2009 0.2443 0.2170 -0.0467 -0.0017 0.0395  6   PHE   B CE2 
4244 C  CZ  . PHE   B 6   ? 0.2061 0.2204 0.2001 -0.0504 -0.0162 0.0156  6   PHE   B CZ  
4254 N  N   . SER   B 7   ? 0.3828 0.3418 0.2387 -0.1254 0.0770  -0.0439 7   SER   B N   
4255 C  CA  . SER   B 7   ? 0.4146 0.3460 0.3060 -0.1300 0.1042  -0.0473 7   SER   B CA  
4256 C  C   . SER   B 7   ? 0.4175 0.3381 0.2979 -0.1376 0.1290  -0.0615 7   SER   B C   
4257 O  O   . SER   B 7   ? 0.4330 0.3375 0.3243 -0.1410 0.1365  -0.0558 7   SER   B O   
4258 C  CB  . SER   B 7   ? 0.4318 0.3597 0.3720 -0.1222 0.1135  -0.0418 7   SER   B CB  
4259 O  OG  . SER   B 7   ? 0.4531 0.4246 0.4265 -0.1164 0.1220  -0.0331 7   SER   B OG  
4265 N  N   . GLY   B 8   ? 0.4043 0.3253 0.2989 -0.1200 0.1285  -0.0765 8   GLY   B N   
4266 C  CA  . GLY   B 8   ? 0.3887 0.3073 0.3152 -0.1099 0.1289  -0.0813 8   GLY   B CA  
4267 C  C   . GLY   B 8   ? 0.3739 0.2785 0.3061 -0.1091 0.1355  -0.0685 8   GLY   B C   
4268 O  O   . GLY   B 8   ? 0.3902 0.2851 0.3361 -0.1015 0.1440  -0.0721 8   GLY   B O   
4272 N  N   . TYR   B 9   ? 0.3579 0.2570 0.2751 -0.0940 0.1086  -0.0744 9   TYR   B N   
4273 C  CA  . TYR   B 9   ? 0.3369 0.2320 0.2537 -0.0710 0.0871  -0.0596 9   TYR   B CA  
4274 C  C   . TYR   B 9   ? 0.3282 0.2271 0.2350 -0.0632 0.0571  -0.0422 9   TYR   B C   
4275 O  O   . TYR   B 9   ? 0.3372 0.2424 0.2736 -0.0615 0.0472  -0.0289 9   TYR   B O   
4276 C  CB  . TYR   B 9   ? 0.3292 0.2128 0.2517 -0.0613 0.0785  -0.0599 9   TYR   B CB  
4277 C  CG  . TYR   B 9   ? 0.3149 0.1881 0.2528 -0.0712 0.0691  -0.0591 9   TYR   B CG  
4278 C  CD1 . TYR   B 9   ? 0.3138 0.1948 0.2669 -0.0866 0.0745  -0.0538 9   TYR   B CD1 
4279 C  CD2 . TYR   B 9   ? 0.3002 0.1815 0.2402 -0.0635 0.0586  -0.0538 9   TYR   B CD2 
4280 C  CE1 . TYR   B 9   ? 0.3055 0.2022 0.2664 -0.0839 0.0842  -0.0553 9   TYR   B CE1 
4281 C  CE2 . TYR   B 9   ? 0.2990 0.1781 0.2557 -0.0637 0.0637  -0.0434 9   TYR   B CE2 
4282 C  CZ  . TYR   B 9   ? 0.2992 0.1942 0.2686 -0.0729 0.0741  -0.0637 9   TYR   B CZ  
4283 O  OH  . TYR   B 9   ? 0.2942 0.2026 0.2859 -0.0840 0.0754  -0.0793 9   TYR   B OH  
4293 N  N   . LEU   B 10  ? 0.3120 0.2090 0.1988 -0.0622 0.0290  -0.0365 10  LEU   B N   
4294 C  CA  . LEU   B 10  ? 0.3076 0.2082 0.2071 -0.0769 -0.0133 -0.0344 10  LEU   B CA  
4295 C  C   . LEU   B 10  ? 0.2824 0.2093 0.2028 -0.0770 -0.0355 -0.0354 10  LEU   B C   
4296 O  O   . LEU   B 10  ? 0.2688 0.2112 0.2072 -0.0564 -0.0212 -0.0282 10  LEU   B O   
4297 C  CB  . LEU   B 10  ? 0.3235 0.2052 0.2227 -0.0858 -0.0314 -0.0081 10  LEU   B CB  
4298 C  CG  . LEU   B 10  ? 0.3421 0.2112 0.2722 -0.0794 -0.0584 0.0018  10  LEU   B CG  
4299 C  CD1 . LEU   B 10  ? 0.3535 0.2249 0.3024 -0.0707 -0.0606 0.0001  10  LEU   B CD1 
4300 C  CD2 . LEU   B 10  ? 0.3516 0.2206 0.2995 -0.0729 -0.0485 0.0166  10  LEU   B CD2 
4312 N  N   . LYS   B 11  ? 0.2922 0.2343 0.2068 -0.0734 -0.0328 -0.0228 11  LYS   B N   
4313 C  CA  . LYS   B 11  ? 0.3063 0.2544 0.2342 -0.0591 -0.0495 -0.0281 11  LYS   B CA  
4314 C  C   . LYS   B 11  ? 0.2912 0.2330 0.2500 -0.0730 -0.0559 -0.0482 11  LYS   B C   
4315 O  O   . LYS   B 11  ? 0.3120 0.2517 0.2903 -0.0807 -0.0478 -0.0739 11  LYS   B O   
4316 C  CB  . LYS   B 11  ? 0.3363 0.3000 0.3018 -0.0327 -0.0493 -0.0230 11  LYS   B CB  
4317 C  CG  . LYS   B 11  ? 0.3668 0.3311 0.3814 -0.0136 -0.0546 -0.0188 11  LYS   B CG  
4318 C  CD  . LYS   B 11  ? 0.3897 0.3573 0.4448 -0.0019 -0.0578 -0.0246 11  LYS   B CD  
4319 C  CE  . LYS   B 11  ? 0.4032 0.3787 0.4942 0.0039  -0.0507 -0.0238 11  LYS   B CE  
4320 N  NZ  . LYS   B 11  ? 0.4098 0.3911 0.5230 0.0080  -0.0440 -0.0182 11  LYS   B NZ  
4334 N  N   . LEU   B 12  ? 0.2576 0.2101 0.2561 -0.0643 -0.0472 -0.0460 12  LEU   B N   
4335 C  CA  . LEU   B 12  ? 0.2455 0.1886 0.2643 -0.0566 -0.0420 -0.0384 12  LEU   B CA  
4336 C  C   . LEU   B 12  ? 0.2321 0.1905 0.2631 -0.0590 -0.0471 -0.0246 12  LEU   B C   
4337 O  O   . LEU   B 12  ? 0.2316 0.1938 0.2810 -0.0603 -0.0621 -0.0234 12  LEU   B O   
4338 C  CB  . LEU   B 12  ? 0.2494 0.1646 0.2622 -0.0412 -0.0365 -0.0398 12  LEU   B CB  
4339 C  CG  . LEU   B 12  ? 0.2473 0.1632 0.2717 -0.0449 -0.0240 -0.0270 12  LEU   B CG  
4340 C  CD1 . LEU   B 12  ? 0.2540 0.1666 0.2658 -0.0296 -0.0181 -0.0067 12  LEU   B CD1 
4341 C  CD2 . LEU   B 12  ? 0.2548 0.1654 0.2872 -0.0479 -0.0147 -0.0213 12  LEU   B CD2 
4353 N  N   . THR   B 13  ? 0.2244 0.1919 0.2705 -0.0574 -0.0492 -0.0348 13  THR   B N   
4354 C  CA  . THR   B 13  ? 0.2266 0.2019 0.2658 -0.0604 -0.0638 -0.0316 13  THR   B CA  
4355 C  C   . THR   B 13  ? 0.2684 0.2153 0.2820 -0.0705 -0.0794 -0.0202 13  THR   B C   
4356 O  O   . THR   B 13  ? 0.2909 0.2187 0.2899 -0.0734 -0.0476 -0.0145 13  THR   B O   
4357 C  CB  . THR   B 13  ? 0.2098 0.2039 0.2754 -0.0492 -0.0558 -0.0206 13  THR   B CB  
4358 O  OG1 . THR   B 13  ? 0.1991 0.2004 0.2778 -0.0446 -0.0442 -0.0316 13  THR   B OG1 
4359 C  CG2 . THR   B 13  ? 0.2256 0.2074 0.2694 -0.0452 -0.0556 0.0039  13  THR   B CG2 
4367 N  N   A ASP   B 14  ? 0.2825 0.2286 0.2930 -0.0675 -0.1123 -0.0064 14  ASP   B N   
4368 N  N   B ASP   B 14  ? 0.2783 0.2280 0.2955 -0.0687 -0.0851 -0.0117 14  ASP   B N   
4369 C  CA  A ASP   B 14  ? 0.2891 0.2463 0.3273 -0.0664 -0.1204 0.0142  14  ASP   B CA  
4370 C  CA  B ASP   B 14  ? 0.2788 0.2374 0.3171 -0.0670 -0.0866 0.0010  14  ASP   B CA  
4371 C  C   A ASP   B 14  ? 0.2756 0.2328 0.2964 -0.0716 -0.1007 0.0126  14  ASP   B C   
4372 C  C   B ASP   B 14  ? 0.2601 0.2213 0.2879 -0.0666 -0.0906 0.0019  14  ASP   B C   
4373 O  O   A ASP   B 14  ? 0.3042 0.2530 0.3001 -0.0727 -0.0971 0.0280  14  ASP   B O   
4374 O  O   B ASP   B 14  ? 0.2652 0.2204 0.2829 -0.0671 -0.0958 -0.0016 14  ASP   B O   
4375 C  CB  A ASP   B 14  ? 0.3084 0.2784 0.4019 -0.0581 -0.1339 0.0194  14  ASP   B CB  
4376 C  CB  B ASP   B 14  ? 0.2960 0.2610 0.3718 -0.0616 -0.0801 0.0039  14  ASP   B CB  
4377 C  CG  A ASP   B 14  ? 0.3347 0.3099 0.4814 -0.0500 -0.1286 0.0073  14  ASP   B CG  
4378 C  CG  B ASP   B 14  ? 0.3118 0.2795 0.4178 -0.0556 -0.0705 -0.0014 14  ASP   B CG  
4379 O  OD1 A ASP   B 14  ? 0.3592 0.3275 0.5034 -0.0547 -0.1272 -0.0099 14  ASP   B OD1 
4380 O  OD1 B ASP   B 14  ? 0.3149 0.2867 0.4354 -0.0540 -0.0650 -0.0070 14  ASP   B OD1 
4381 O  OD2 A ASP   B 14  ? 0.3347 0.3250 0.5238 -0.0480 -0.1244 0.0104  14  ASP   B OD2 
4382 O  OD2 B ASP   B 14  ? 0.3196 0.2864 0.4418 -0.0584 -0.0691 -0.0016 14  ASP   B OD2 
4391 N  N   . ASN   B 15  ? 0.2383 0.2039 0.2645 -0.0608 -0.0915 0.0035  15  ASN   B N   
4392 C  CA  . ASN   B 15  ? 0.1959 0.1750 0.2514 -0.0415 -0.0708 0.0031  15  ASN   B CA  
4393 C  C   . ASN   B 15  ? 0.1812 0.1634 0.2314 -0.0299 -0.0524 -0.0022 15  ASN   B C   
4394 O  O   . ASN   B 15  ? 0.1734 0.1600 0.2546 -0.0268 -0.0552 -0.0138 15  ASN   B O   
4395 C  CB  . ASN   B 15  ? 0.1937 0.1664 0.2581 -0.0230 -0.0636 0.0092  15  ASN   B CB  
4396 C  CG  . ASN   B 15  ? 0.1769 0.1624 0.2695 -0.0274 -0.0393 0.0091  15  ASN   B CG  
4397 O  OD1 . ASN   B 15  ? 0.1860 0.1961 0.2866 -0.0496 -0.0427 0.0205  15  ASN   B OD1 
4398 N  ND2 . ASN   B 15  ? 0.1759 0.1497 0.2409 -0.0136 -0.0126 -0.0049 15  ASN   B ND2 
4406 N  N   . VAL   B 16  ? 0.1851 0.1546 0.2304 -0.0345 -0.0543 0.0027  16  VAL   B N   
4407 C  CA  . VAL   B 16  ? 0.1895 0.1561 0.2060 -0.0345 -0.0450 -0.0108 16  VAL   B CA  
4408 C  C   . VAL   B 16  ? 0.1835 0.1710 0.1940 -0.0407 -0.0407 -0.0101 16  VAL   B C   
4409 O  O   . VAL   B 16  ? 0.1853 0.1839 0.2238 -0.0377 -0.0360 -0.0212 16  VAL   B O   
4410 C  CB  . VAL   B 16  ? 0.1969 0.1557 0.2262 -0.0190 -0.0296 -0.0120 16  VAL   B CB  
4411 C  CG1 . VAL   B 16  ? 0.2087 0.1531 0.2116 -0.0089 -0.0298 -0.0028 16  VAL   B CG1 
4412 C  CG2 . VAL   B 16  ? 0.1921 0.1542 0.2338 -0.0075 -0.0175 -0.0153 16  VAL   B CG2 
4422 N  N   . TYR   B 17  ? 0.1843 0.1760 0.2072 -0.0328 -0.0386 -0.0191 17  TYR   B N   
4423 C  CA  . TYR   B 17  ? 0.1974 0.1839 0.1928 -0.0394 -0.0345 -0.0008 17  TYR   B CA  
4424 C  C   . TYR   B 17  ? 0.1906 0.1632 0.1916 -0.0388 -0.0240 -0.0080 17  TYR   B C   
4425 O  O   . TYR   B 17  ? 0.1864 0.1681 0.1984 -0.0355 -0.0308 -0.0242 17  TYR   B O   
4426 C  CB  . TYR   B 17  ? 0.2333 0.2285 0.2185 -0.0325 -0.0355 0.0364  17  TYR   B CB  
4427 C  CG  . TYR   B 17  ? 0.2639 0.2733 0.2774 -0.0254 -0.0454 0.0479  17  TYR   B CG  
4428 C  CD1 . TYR   B 17  ? 0.2794 0.2859 0.2913 -0.0253 -0.0522 0.0638  17  TYR   B CD1 
4429 C  CD2 . TYR   B 17  ? 0.2851 0.3036 0.2931 -0.0153 -0.0532 0.0492  17  TYR   B CD2 
4430 C  CE1 . TYR   B 17  ? 0.2996 0.3092 0.3120 -0.0138 -0.0677 0.0593  17  TYR   B CE1 
4431 C  CE2 . TYR   B 17  ? 0.3028 0.3191 0.3131 0.0001  -0.0732 0.0583  17  TYR   B CE2 
4432 C  CZ  . TYR   B 17  ? 0.3152 0.3254 0.3177 0.0015  -0.0809 0.0574  17  TYR   B CZ  
4433 O  OH  . TYR   B 17  ? 0.3347 0.3475 0.3412 0.0126  -0.0939 0.0543  17  TYR   B OH  
4443 N  N   . ILE   B 18  ? 0.1999 0.1699 0.1869 -0.0370 -0.0133 -0.0163 18  ILE   B N   
4444 C  CA  . ILE   B 18  ? 0.2022 0.1606 0.1893 -0.0388 -0.0120 -0.0189 18  ILE   B CA  
4445 C  C   . ILE   B 18  ? 0.2134 0.1673 0.1916 -0.0489 -0.0054 -0.0223 18  ILE   B C   
4446 O  O   . ILE   B 18  ? 0.2347 0.1796 0.2158 -0.0485 -0.0026 -0.0291 18  ILE   B O   
4447 C  CB  . ILE   B 18  ? 0.2046 0.1615 0.2102 -0.0411 -0.0076 -0.0168 18  ILE   B CB  
4448 C  CG1 . ILE   B 18  ? 0.2052 0.1729 0.2052 -0.0376 -0.0097 0.0056  18  ILE   B CG1 
4449 C  CG2 . ILE   B 18  ? 0.2028 0.1652 0.2135 -0.0431 -0.0169 -0.0143 18  ILE   B CG2 
4450 C  CD1 . ILE   B 18  ? 0.2081 0.1985 0.2152 -0.0254 -0.0292 0.0306  18  ILE   B CD1 
4462 N  N   . LYS   B 19  ? 0.2112 0.1670 0.2076 -0.0283 0.0362  -0.0336 19  LYS   B N   
4463 C  CA  . LYS   B 19  ? 0.2188 0.1711 0.2291 -0.0265 0.0310  -0.0395 19  LYS   B CA  
4464 C  C   . LYS   B 19  ? 0.2012 0.1660 0.2336 -0.0246 0.0420  -0.0509 19  LYS   B C   
4465 O  O   . LYS   B 19  ? 0.1903 0.1671 0.2154 -0.0098 0.0272  -0.0438 19  LYS   B O   
4466 C  CB  . LYS   B 19  ? 0.2382 0.1872 0.2383 -0.0300 0.0440  -0.0289 19  LYS   B CB  
4467 C  CG  . LYS   B 19  ? 0.2644 0.2022 0.2685 -0.0383 0.0459  -0.0324 19  LYS   B CG  
4468 C  CD  . LYS   B 19  ? 0.2966 0.2328 0.2826 -0.0466 0.0542  -0.0292 19  LYS   B CD  
4469 C  CE  . LYS   B 19  ? 0.3242 0.2617 0.2984 -0.0498 0.0473  -0.0303 19  LYS   B CE  
4470 N  NZ  . LYS   B 19  ? 0.3474 0.2801 0.3076 -0.0571 0.0586  -0.0240 19  LYS   B NZ  
4484 N  N   . ASN   B 20  ? 0.2030 0.1827 0.2635 -0.0215 0.0442  -0.0684 20  ASN   B N   
4485 C  CA  . ASN   B 20  ? 0.2035 0.1964 0.2954 -0.0155 0.0462  -0.0795 20  ASN   B CA  
4486 C  C   . ASN   B 20  ? 0.1961 0.2143 0.2915 -0.0250 0.0548  -0.0869 20  ASN   B C   
4487 O  O   . ASN   B 20  ? 0.2133 0.2463 0.3175 -0.0417 0.0520  -0.0833 20  ASN   B O   
4488 C  CB  . ASN   B 20  ? 0.2337 0.1981 0.3297 0.0064  0.0289  -0.0772 20  ASN   B CB  
4489 C  CG  . ASN   B 20  ? 0.2607 0.2019 0.3411 0.0364  0.0294  -0.0882 20  ASN   B CG  
4490 O  OD1 . ASN   B 20  ? 0.2955 0.2266 0.3748 0.0541  0.0311  -0.0894 20  ASN   B OD1 
4491 N  ND2 . ASN   B 20  ? 0.2485 0.2072 0.3297 0.0399  0.0123  -0.0868 20  ASN   B ND2 
4498 N  N   . ALA   B 21  ? 0.2016 0.1928 0.2977 -0.0344 0.0554  -0.0632 21  ALA   B N   
4499 C  CA  . ALA   B 21  ? 0.2137 0.1992 0.3118 -0.0312 0.0376  -0.0576 21  ALA   B CA  
4500 C  C   . ALA   B 21  ? 0.2107 0.1747 0.2921 -0.0219 0.0489  -0.0399 21  ALA   B C   
4501 O  O   . ALA   B 21  ? 0.2123 0.1694 0.2940 -0.0263 0.0440  -0.0285 21  ALA   B O   
4502 C  CB  . ALA   B 21  ? 0.2287 0.2213 0.3275 -0.0463 0.0305  -0.0432 21  ALA   B CB  
4508 N  N   . ASP   B 22  ? 0.2037 0.1658 0.2808 -0.0201 0.0433  -0.0312 22  ASP   B N   
4509 C  CA  . ASP   B 22  ? 0.2003 0.1595 0.2673 -0.0119 0.0394  -0.0239 22  ASP   B CA  
4510 C  C   . ASP   B 22  ? 0.1943 0.1586 0.2313 -0.0167 0.0198  -0.0114 22  ASP   B C   
4511 O  O   . ASP   B 22  ? 0.1909 0.1631 0.2377 -0.0116 0.0122  -0.0129 22  ASP   B O   
4512 C  CB  . ASP   B 22  ? 0.2049 0.1661 0.3151 -0.0081 0.0465  -0.0133 22  ASP   B CB  
4513 C  CG  . ASP   B 22  ? 0.2074 0.1811 0.3572 -0.0008 0.0135  -0.0072 22  ASP   B CG  
4514 O  OD1 . ASP   B 22  ? 0.2206 0.1725 0.3491 0.0066  -0.0105 -0.0048 22  ASP   B OD1 
4515 O  OD2 . ASP   B 22  ? 0.2153 0.2137 0.4144 0.0118  -0.0110 -0.0106 22  ASP   B OD2 
4520 N  N   . ILE   B 23  ? 0.1872 0.1512 0.1970 -0.0054 -0.0017 0.0139  23  ILE   B N   
4521 C  CA  . ILE   B 23  ? 0.1773 0.1594 0.1737 -0.0114 -0.0084 0.0073  23  ILE   B CA  
4522 C  C   . ILE   B 23  ? 0.1689 0.1609 0.1697 -0.0044 -0.0117 0.0020  23  ILE   B C   
4523 O  O   . ILE   B 23  ? 0.1638 0.1584 0.1649 -0.0078 -0.0059 0.0060  23  ILE   B O   
4524 C  CB  . ILE   B 23  ? 0.1694 0.1668 0.1955 -0.0192 -0.0018 0.0128  23  ILE   B CB  
4525 C  CG1 . ILE   B 23  ? 0.1720 0.1739 0.2163 -0.0176 -0.0016 0.0287  23  ILE   B CG1 
4526 C  CG2 . ILE   B 23  ? 0.1783 0.1936 0.2046 -0.0222 -0.0001 0.0060  23  ILE   B CG2 
4527 C  CD1 . ILE   B 23  ? 0.1774 0.1800 0.2205 -0.0182 0.0031  0.0379  23  ILE   B CD1 
4539 N  N   . VAL   B 24  ? 0.1673 0.1587 0.1932 -0.0050 -0.0112 0.0006  24  VAL   B N   
4540 C  CA  . VAL   B 24  ? 0.1647 0.1618 0.2092 -0.0039 -0.0276 0.0040  24  VAL   B CA  
4541 C  C   . VAL   B 24  ? 0.1627 0.1641 0.2173 -0.0080 -0.0139 0.0039  24  VAL   B C   
4542 O  O   . VAL   B 24  ? 0.1620 0.1717 0.2346 -0.0180 -0.0085 0.0232  24  VAL   B O   
4543 C  CB  . VAL   B 24  ? 0.1776 0.1802 0.2145 0.0018  -0.0257 0.0037  24  VAL   B CB  
4544 C  CG1 . VAL   B 24  ? 0.1782 0.1892 0.2488 -0.0079 -0.0297 0.0038  24  VAL   B CG1 
4545 C  CG2 . VAL   B 24  ? 0.1892 0.2065 0.2174 0.0090  -0.0269 -0.0083 24  VAL   B CG2 
4555 N  N   . GLU   B 25  ? 0.1838 0.1751 0.2192 -0.0083 0.0037  -0.0072 25  GLU   B N   
4556 C  CA  . GLU   B 25  ? 0.2028 0.1998 0.2394 -0.0005 0.0157  -0.0130 25  GLU   B CA  
4557 C  C   . GLU   B 25  ? 0.1991 0.1949 0.2047 -0.0141 0.0202  -0.0018 25  GLU   B C   
4558 O  O   . GLU   B 25  ? 0.2036 0.2042 0.2212 -0.0122 0.0237  0.0072  25  GLU   B O   
4559 C  CB  . GLU   B 25  ? 0.2334 0.2389 0.3041 0.0191  0.0167  -0.0105 25  GLU   B CB  
4560 C  CG  . GLU   B 25  ? 0.2782 0.2797 0.4101 0.0285  0.0052  -0.0093 25  GLU   B CG  
4561 C  CD  . GLU   B 25  ? 0.3477 0.3477 0.4914 0.0207  0.0048  -0.0088 25  GLU   B CD  
4562 O  OE1 . GLU   B 25  ? 0.3381 0.3727 0.5328 0.0194  0.0118  -0.0078 25  GLU   B OE1 
4563 O  OE2 . GLU   B 25  ? 0.3456 0.3704 0.5282 0.0192  0.0047  -0.0135 25  GLU   B OE2 
4570 N  N   . GLU   B 26  ? 0.1924 0.1804 0.1787 -0.0344 0.0109  0.0054  26  GLU   B N   
4571 C  CA  . GLU   B 26  ? 0.1887 0.1965 0.1869 -0.0411 -0.0119 0.0022  26  GLU   B CA  
4572 C  C   . GLU   B 26  ? 0.1687 0.1913 0.1733 -0.0253 -0.0017 0.0173  26  GLU   B C   
4573 O  O   . GLU   B 26  ? 0.1947 0.2216 0.1800 -0.0199 -0.0069 0.0252  26  GLU   B O   
4574 C  CB  . GLU   B 26  ? 0.2178 0.2202 0.2187 -0.0465 -0.0061 0.0222  26  GLU   B CB  
4575 C  CG  . GLU   B 26  ? 0.2637 0.2627 0.2690 -0.0534 0.0139  -0.0068 26  GLU   B CG  
4576 C  CD  . GLU   B 26  ? 0.2939 0.2868 0.2886 -0.0779 0.0274  -0.0476 26  GLU   B CD  
4577 O  OE1 . GLU   B 26  ? 0.3229 0.2738 0.2873 -0.0933 0.0847  -0.0460 26  GLU   B OE1 
4578 O  OE2 . GLU   B 26  ? 0.2916 0.3252 0.3164 -0.0699 0.0217  -0.0376 26  GLU   B OE2 
4585 N  N   . ALA   B 27  ? 0.1581 0.1758 0.1784 -0.0225 0.0006  0.0191  27  ALA   B N   
4586 C  CA  . ALA   B 27  ? 0.1630 0.1730 0.1852 -0.0179 -0.0051 0.0254  27  ALA   B CA  
4587 C  C   . ALA   B 27  ? 0.1695 0.1799 0.2176 -0.0155 0.0067  0.0399  27  ALA   B C   
4588 O  O   . ALA   B 27  ? 0.1750 0.1832 0.2346 -0.0048 0.0073  0.0495  27  ALA   B O   
4589 C  CB  . ALA   B 27  ? 0.1795 0.1544 0.2051 -0.0232 -0.0089 0.0255  27  ALA   B CB  
4595 N  N   . LYS   B 28  ? 0.1665 0.1952 0.2611 -0.0178 0.0136  0.0601  28  LYS   B N   
4596 C  CA  . LYS   B 28  ? 0.1794 0.2305 0.2831 -0.0054 0.0425  0.0857  28  LYS   B CA  
4597 C  C   . LYS   B 28  ? 0.1997 0.2497 0.2674 -0.0035 0.0570  0.0789  28  LYS   B C   
4598 O  O   . LYS   B 28  ? 0.2273 0.2599 0.2914 -0.0052 0.0611  0.0737  28  LYS   B O   
4599 C  CB  . LYS   B 28  ? 0.2004 0.2609 0.3280 0.0036  0.0749  0.0907  28  LYS   B CB  
4600 C  CG  . LYS   B 28  ? 0.2222 0.3071 0.3808 0.0138  0.0802  0.0979  28  LYS   B CG  
4601 C  CD  . LYS   B 28  ? 0.2536 0.3474 0.4504 0.0181  0.0929  0.0927  28  LYS   B CD  
4602 C  CE  . LYS   B 28  ? 0.3191 0.4010 0.4931 0.0262  0.0909  0.0934  28  LYS   B CE  
4603 N  NZ  . LYS   B 28  ? 0.4009 0.4553 0.5236 0.0354  0.0978  0.1009  28  LYS   B NZ  
4617 N  N   . LYS   B 29  ? 0.2145 0.2732 0.2657 0.0145  0.0576  0.0579  29  LYS   B N   
4618 C  CA  . LYS   B 29  ? 0.2619 0.3094 0.2934 0.0162  0.0564  0.0607  29  LYS   B CA  
4619 C  C   . LYS   B 29  ? 0.2584 0.3183 0.2671 0.0189  0.0477  0.0751  29  LYS   B C   
4620 O  O   . LYS   B 29  ? 0.2762 0.3423 0.2772 0.0268  0.0489  0.0877  29  LYS   B O   
4621 C  CB  . LYS   B 29  ? 0.3132 0.3408 0.3798 0.0158  0.0543  0.0522  29  LYS   B CB  
4622 C  CG  . LYS   B 29  ? 0.3598 0.3726 0.4613 0.0157  0.0558  0.0463  29  LYS   B CG  
4623 C  CD  . LYS   B 29  ? 0.3931 0.3965 0.5307 0.0132  0.0634  0.0359  29  LYS   B CD  
4624 C  CE  . LYS   B 29  ? 0.4055 0.4045 0.5844 0.0102  0.0702  0.0299  29  LYS   B CE  
4625 N  NZ  . LYS   B 29  ? 0.4561 0.4190 0.6062 0.0097  0.0728  0.0271  29  LYS   B NZ  
4639 N  N   . VAL   B 30  ? 0.2246 0.2980 0.2422 0.0082  0.0413  0.0702  30  VAL   B N   
4640 C  CA  . VAL   B 30  ? 0.2114 0.2839 0.2742 -0.0008 0.0019  0.0794  30  VAL   B CA  
4641 C  C   . VAL   B 30  ? 0.1922 0.2802 0.2692 -0.0044 0.0002  0.1022  30  VAL   B C   
4642 O  O   . VAL   B 30  ? 0.2090 0.2946 0.2782 0.0027  0.0039  0.1137  30  VAL   B O   
4643 C  CB  . VAL   B 30  ? 0.2171 0.2749 0.3117 -0.0223 -0.0253 0.0738  30  VAL   B CB  
4644 C  CG1 . VAL   B 30  ? 0.2214 0.2869 0.2974 -0.0228 -0.0298 0.0734  30  VAL   B CG1 
4645 C  CG2 . VAL   B 30  ? 0.2339 0.2691 0.3263 -0.0334 -0.0265 0.0478  30  VAL   B CG2 
4655 N  N   . LYS   B 31  ? 0.1833 0.2470 0.3120 -0.0264 -0.0030 0.1108  31  LYS   B N   
4656 C  CA  . LYS   B 31  ? 0.1701 0.2392 0.3432 -0.0399 -0.0125 0.1115  31  LYS   B CA  
4657 C  C   . LYS   B 31  ? 0.1688 0.2006 0.3017 -0.0355 -0.0311 0.0961  31  LYS   B C   
4658 O  O   . LYS   B 31  ? 0.1745 0.2137 0.3157 -0.0321 -0.0235 0.1032  31  LYS   B O   
4659 C  CB  . LYS   B 31  ? 0.1797 0.2885 0.3969 -0.0401 0.0134  0.1200  31  LYS   B CB  
4660 C  CG  . LYS   B 31  ? 0.2212 0.3270 0.4396 -0.0459 0.0364  0.1110  31  LYS   B CG  
4661 C  CD  . LYS   B 31  ? 0.2541 0.3572 0.4811 -0.0391 0.0326  0.0968  31  LYS   B CD  
4662 C  CE  . LYS   B 31  ? 0.2863 0.3981 0.5197 -0.0320 0.0224  0.0825  31  LYS   B CE  
4663 N  NZ  . LYS   B 31  ? 0.3700 0.4274 0.5391 -0.0167 0.0086  0.0633  31  LYS   B NZ  
4677 N  N   . PRO   B 32  ? 0.1768 0.1682 0.2423 -0.0348 -0.0513 0.0556  32  PRO   B N   
4678 C  CA  . PRO   B 32  ? 0.1864 0.1664 0.1884 -0.0379 -0.0505 0.0323  32  PRO   B CA  
4679 C  C   . PRO   B 32  ? 0.1992 0.1555 0.1910 -0.0416 -0.0604 0.0428  32  PRO   B C   
4680 O  O   . PRO   B 32  ? 0.2137 0.1568 0.2311 -0.0444 -0.0785 0.0406  32  PRO   B O   
4681 C  CB  . PRO   B 32  ? 0.2040 0.1638 0.1655 -0.0397 -0.0378 0.0118  32  PRO   B CB  
4682 C  CG  . PRO   B 32  ? 0.2205 0.1507 0.1783 -0.0279 -0.0594 0.0225  32  PRO   B CG  
4683 C  CD  . PRO   B 32  ? 0.2061 0.1543 0.2296 -0.0298 -0.0695 0.0325  32  PRO   B CD  
4691 N  N   . THR   B 33  ? 0.2002 0.1447 0.1743 -0.0327 -0.0565 0.0271  33  THR   B N   
4692 C  CA  . THR   B 33  ? 0.2070 0.1571 0.1772 -0.0387 -0.0523 0.0310  33  THR   B CA  
4693 C  C   . THR   B 33  ? 0.2044 0.1428 0.1666 -0.0344 -0.0498 0.0273  33  THR   B C   
4694 O  O   . THR   B 33  ? 0.2280 0.1440 0.1756 -0.0389 -0.0549 0.0184  33  THR   B O   
4695 C  CB  . THR   B 33  ? 0.2201 0.1697 0.1722 -0.0270 -0.0626 0.0274  33  THR   B CB  
4696 O  OG1 . THR   B 33  ? 0.2068 0.1677 0.1845 -0.0263 -0.0562 0.0294  33  THR   B OG1 
4697 C  CG2 . THR   B 33  ? 0.2409 0.1722 0.1912 -0.0128 -0.0651 0.0259  33  THR   B CG2 
4705 N  N   . VAL   B 34  ? 0.1875 0.1439 0.1529 -0.0349 -0.0454 0.0192  34  VAL   B N   
4706 C  CA  . VAL   B 34  ? 0.1737 0.1406 0.1568 -0.0256 -0.0424 0.0112  34  VAL   B CA  
4707 C  C   . VAL   B 34  ? 0.1608 0.1343 0.1407 -0.0263 -0.0245 0.0063  34  VAL   B C   
4708 O  O   . VAL   B 34  ? 0.1764 0.1430 0.1383 -0.0215 -0.0348 0.0048  34  VAL   B O   
4709 C  CB  . VAL   B 34  ? 0.1801 0.1448 0.1817 -0.0094 -0.0446 0.0063  34  VAL   B CB  
4710 C  CG1 . VAL   B 34  ? 0.1841 0.1553 0.1866 -0.0032 -0.0225 0.0082  34  VAL   B CG1 
4711 C  CG2 . VAL   B 34  ? 0.1864 0.1540 0.2040 -0.0108 -0.0251 0.0112  34  VAL   B CG2 
4721 N  N   . VAL   B 35  ? 0.1557 0.1340 0.1284 -0.0247 -0.0116 0.0060  35  VAL   B N   
4722 C  CA  . VAL   B 35  ? 0.1517 0.1311 0.1252 -0.0216 -0.0115 0.0040  35  VAL   B CA  
4723 C  C   . VAL   B 35  ? 0.1420 0.1327 0.1235 -0.0176 -0.0112 0.0080  35  VAL   B C   
4724 O  O   . VAL   B 35  ? 0.1461 0.1389 0.1311 -0.0214 -0.0057 -0.0078 35  VAL   B O   
4725 C  CB  . VAL   B 35  ? 0.1466 0.1508 0.1397 -0.0146 -0.0026 0.0058  35  VAL   B CB  
4726 C  CG1 . VAL   B 35  ? 0.1426 0.1644 0.1619 -0.0221 0.0012  -0.0001 35  VAL   B CG1 
4727 C  CG2 . VAL   B 35  ? 0.1457 0.1525 0.1677 -0.0072 -0.0061 -0.0050 35  VAL   B CG2 
4737 N  N   . VAL   B 36  ? 0.1352 0.1295 0.1275 -0.0170 -0.0100 0.0161  36  VAL   B N   
4738 C  CA  . VAL   B 36  ? 0.1364 0.1215 0.1241 -0.0143 -0.0091 0.0076  36  VAL   B CA  
4739 C  C   . VAL   B 36  ? 0.1342 0.1262 0.1207 -0.0136 -0.0085 0.0072  36  VAL   B C   
4740 O  O   . VAL   B 36  ? 0.1470 0.1400 0.1385 -0.0112 0.0018  -0.0009 36  VAL   B O   
4741 C  CB  . VAL   B 36  ? 0.1382 0.1282 0.1390 -0.0196 -0.0072 0.0094  36  VAL   B CB  
4742 C  CG1 . VAL   B 36  ? 0.1401 0.1427 0.1508 -0.0255 -0.0073 0.0006  36  VAL   B CG1 
4743 C  CG2 . VAL   B 36  ? 0.1499 0.1347 0.1508 -0.0137 -0.0242 0.0076  36  VAL   B CG2 
4753 N  N   . ASN   B 37  ? 0.1357 0.1298 0.1259 -0.0069 -0.0086 0.0071  37  ASN   B N   
4754 C  CA  . ASN   B 37  ? 0.1405 0.1305 0.1273 -0.0029 -0.0080 0.0077  37  ASN   B CA  
4755 C  C   . ASN   B 37  ? 0.1394 0.1347 0.1334 0.0041  -0.0095 0.0050  37  ASN   B C   
4756 O  O   . ASN   B 37  ? 0.1469 0.1441 0.1365 0.0023  -0.0009 0.0065  37  ASN   B O   
4757 C  CB  . ASN   B 37  ? 0.1356 0.1355 0.1325 -0.0041 -0.0196 0.0056  37  ASN   B CB  
4758 C  CG  . ASN   B 37  ? 0.1463 0.1404 0.1398 -0.0026 -0.0094 0.0000  37  ASN   B CG  
4759 O  OD1 . ASN   B 37  ? 0.1521 0.1428 0.1508 0.0125  -0.0193 0.0048  37  ASN   B OD1 
4760 N  ND2 . ASN   B 37  ? 0.1512 0.1366 0.1316 0.0037  -0.0081 0.0023  37  ASN   B ND2 
4767 N  N   . ALA   B 38  ? 0.1518 0.1352 0.1296 0.0115  0.0024  0.0047  38  ALA   B N   
4768 C  CA  . ALA   B 38  ? 0.1586 0.1400 0.1327 -0.0010 0.0020  0.0066  38  ALA   B CA  
4769 C  C   . ALA   B 38  ? 0.1539 0.1365 0.1453 0.0024  0.0020  0.0148  38  ALA   B C   
4770 O  O   . ALA   B 38  ? 0.1710 0.1443 0.1444 0.0042  -0.0058 0.0113  38  ALA   B O   
4771 C  CB  . ALA   B 38  ? 0.1861 0.1515 0.1439 -0.0080 0.0078  0.0106  38  ALA   B CB  
4777 N  N   . ALA   B 39  ? 0.1549 0.1429 0.1242 0.0118  -0.0047 0.0057  39  ALA   B N   
4778 C  CA  . ALA   B 39  ? 0.1671 0.1431 0.1288 0.0032  -0.0089 0.0071  39  ALA   B CA  
4779 C  C   . ALA   B 39  ? 0.1694 0.1441 0.1151 0.0084  -0.0061 0.0013  39  ALA   B C   
4780 O  O   . ALA   B 39  ? 0.1749 0.1497 0.1452 -0.0009 -0.0109 0.0134  39  ALA   B O   
4781 C  CB  . ALA   B 39  ? 0.1590 0.1471 0.1496 -0.0027 -0.0015 0.0012  39  ALA   B CB  
4787 N  N   . ASN   B 40  ? 0.1757 0.1680 0.1099 -0.0032 -0.0025 -0.0066 40  ASN   B N   
4788 C  CA  . ASN   B 40  ? 0.1779 0.1777 0.1390 0.0008  -0.0110 -0.0093 40  ASN   B CA  
4789 C  C   . ASN   B 40  ? 0.1773 0.1816 0.1270 0.0041  -0.0035 -0.0037 40  ASN   B C   
4790 O  O   . ASN   B 40  ? 0.1755 0.1691 0.1266 0.0061  -0.0135 0.0004  40  ASN   B O   
4791 C  CB  . ASN   B 40  ? 0.1933 0.1690 0.1605 0.0069  -0.0197 0.0101  40  ASN   B CB  
4792 C  CG  . ASN   B 40  ? 0.1942 0.1807 0.1876 0.0011  -0.0337 0.0167  40  ASN   B CG  
4793 O  OD1 . ASN   B 40  ? 0.1868 0.1765 0.2772 -0.0000 -0.0333 0.0177  40  ASN   B OD1 
4794 N  ND2 . ASN   B 40  ? 0.1993 0.1792 0.2018 -0.0004 -0.0257 0.0209  40  ASN   B ND2 
4801 N  N   . VAL   B 41  ? 0.1864 0.1852 0.1313 0.0131  0.0073  -0.0061 41  VAL   B N   
4802 C  CA  . VAL   B 41  ? 0.1886 0.1972 0.1401 0.0099  -0.0010 -0.0100 41  VAL   B CA  
4803 C  C   . VAL   B 41  ? 0.1893 0.1912 0.1319 0.0157  -0.0042 -0.0124 41  VAL   B C   
4804 O  O   . VAL   B 41  ? 0.1910 0.1918 0.1458 0.0091  -0.0129 -0.0108 41  VAL   B O   
4805 C  CB  . VAL   B 41  ? 0.2021 0.2094 0.1718 -0.0027 0.0196  -0.0241 41  VAL   B CB  
4806 C  CG1 . VAL   B 41  ? 0.2008 0.2090 0.1950 -0.0087 0.0254  -0.0246 41  VAL   B CG1 
4807 C  CG2 . VAL   B 41  ? 0.2157 0.2262 0.1858 -0.0125 0.0216  -0.0192 41  VAL   B CG2 
4817 N  N   . TYR   B 42  ? 0.1960 0.1885 0.1353 0.0159  -0.0134 0.0077  42  TYR   B N   
4818 C  CA  . TYR   B 42  ? 0.2035 0.1953 0.1334 0.0123  -0.0238 -0.0047 42  TYR   B CA  
4819 C  C   . TYR   B 42  ? 0.1864 0.1738 0.1514 0.0160  -0.0281 -0.0069 42  TYR   B C   
4820 O  O   . TYR   B 42  ? 0.1923 0.1823 0.1813 0.0115  -0.0301 -0.0154 42  TYR   B O   
4821 C  CB  . TYR   B 42  ? 0.2252 0.2198 0.1564 0.0117  -0.0292 0.0069  42  TYR   B CB  
4822 C  CG  . TYR   B 42  ? 0.2248 0.2397 0.1500 0.0029  -0.0321 0.0174  42  TYR   B CG  
4823 C  CD1 . TYR   B 42  ? 0.2179 0.2401 0.1567 -0.0012 -0.0276 -0.0019 42  TYR   B CD1 
4824 C  CD2 . TYR   B 42  ? 0.2427 0.2480 0.2020 0.0116  -0.0127 0.0205  42  TYR   B CD2 
4825 C  CE1 . TYR   B 42  ? 0.2337 0.2593 0.1374 0.0055  -0.0193 -0.0040 42  TYR   B CE1 
4826 C  CE2 . TYR   B 42  ? 0.2519 0.2632 0.1871 0.0165  0.0044  0.0297  42  TYR   B CE2 
4827 C  CZ  . TYR   B 42  ? 0.2584 0.2835 0.1691 0.0263  0.0101  0.0090  42  TYR   B CZ  
4828 O  OH  . TYR   B 42  ? 0.2903 0.3225 0.2154 0.0440  0.0238  0.0190  42  TYR   B OH  
4838 N  N   . LEU   B 43  ? 0.1702 0.1573 0.1436 0.0057  -0.0167 -0.0095 43  LEU   B N   
4839 C  CA  . LEU   B 43  ? 0.1695 0.1632 0.1350 0.0024  -0.0193 -0.0016 43  LEU   B CA  
4840 C  C   . LEU   B 43  ? 0.1802 0.1644 0.1204 0.0029  -0.0166 0.0005  43  LEU   B C   
4841 O  O   . LEU   B 43  ? 0.1709 0.1677 0.1600 0.0048  -0.0189 0.0021  43  LEU   B O   
4842 C  CB  . LEU   B 43  ? 0.1644 0.1590 0.1592 0.0011  -0.0240 -0.0140 43  LEU   B CB  
4843 C  CG  . LEU   B 43  ? 0.1720 0.1583 0.1614 0.0027  -0.0230 -0.0090 43  LEU   B CG  
4844 C  CD1 . LEU   B 43  ? 0.1786 0.1588 0.1996 0.0009  -0.0338 -0.0089 43  LEU   B CD1 
4845 C  CD2 . LEU   B 43  ? 0.1711 0.1584 0.1553 -0.0017 -0.0318 -0.0038 43  LEU   B CD2 
4857 N  N   . LYS   B 44  ? 0.1831 0.1644 0.1356 0.0073  -0.0066 -0.0039 44  LYS   B N   
4858 C  CA  . LYS   B 44  ? 0.1886 0.1738 0.1453 0.0119  -0.0134 0.0118  44  LYS   B CA  
4859 C  C   . LYS   B 44  ? 0.1756 0.1656 0.1576 0.0166  -0.0115 0.0108  44  LYS   B C   
4860 O  O   . LYS   B 44  ? 0.1985 0.1676 0.1774 0.0037  -0.0016 0.0047  44  LYS   B O   
4861 C  CB  . LYS   B 44  ? 0.2179 0.1900 0.1798 0.0189  -0.0324 0.0077  44  LYS   B CB  
4862 C  CG  . LYS   B 44  ? 0.2587 0.2206 0.2142 0.0121  -0.0565 0.0072  44  LYS   B CG  
4863 C  CD  . LYS   B 44  ? 0.2942 0.2467 0.2723 -0.0019 -0.0661 -0.0006 44  LYS   B CD  
4864 C  CE  . LYS   B 44  ? 0.3218 0.2775 0.3204 -0.0110 -0.0647 0.0036  44  LYS   B CE  
4865 N  NZ  . LYS   B 44  ? 0.3366 0.2892 0.3361 -0.0089 -0.0684 0.0080  44  LYS   B NZ  
4879 N  N   . HIS   B 45  ? 0.1713 0.1689 0.1406 0.0063  -0.0156 0.0150  45  HIS   B N   
4880 C  CA  . HIS   B 45  ? 0.1746 0.1610 0.1496 0.0085  -0.0103 0.0016  45  HIS   B CA  
4881 C  C   . HIS   B 45  ? 0.1937 0.1781 0.1873 0.0200  -0.0246 -0.0071 45  HIS   B C   
4882 O  O   . HIS   B 45  ? 0.2101 0.2096 0.2355 0.0416  0.0039  -0.0035 45  HIS   B O   
4883 C  CB  . HIS   B 45  ? 0.1703 0.1629 0.1562 0.0060  -0.0078 -0.0103 45  HIS   B CB  
4884 C  CG  . HIS   B 45  ? 0.1685 0.1629 0.1560 -0.0090 -0.0123 -0.0014 45  HIS   B CG  
4885 N  ND1 . HIS   B 45  ? 0.1698 0.1587 0.1564 -0.0018 -0.0188 -0.0104 45  HIS   B ND1 
4886 C  CD2 . HIS   B 45  ? 0.1721 0.1699 0.1768 -0.0165 -0.0218 0.0036  45  HIS   B CD2 
4887 C  CE1 . HIS   B 45  ? 0.1779 0.1506 0.1414 -0.0059 -0.0280 -0.0060 45  HIS   B CE1 
4888 N  NE2 . HIS   B 45  ? 0.1776 0.1555 0.1587 -0.0050 -0.0197 -0.0040 45  HIS   B NE2 
4896 N  N   A GLY   B 46  ? 0.2056 0.1741 0.2225 0.0168  -0.0448 0.0067  46  GLY   B N   
4897 N  N   B GLY   B 46  ? 0.2037 0.1857 0.2118 0.0201  -0.0350 0.0042  46  GLY   B N   
4898 C  CA  A GLY   B 46  ? 0.2155 0.1868 0.2528 0.0136  -0.0611 0.0115  46  GLY   B CA  
4899 C  CA  B GLY   B 46  ? 0.2106 0.1998 0.2289 0.0189  -0.0450 0.0135  46  GLY   B CA  
4900 C  C   A GLY   B 46  ? 0.2114 0.2041 0.2995 0.0220  -0.0499 0.0093  46  GLY   B C   
4901 C  C   B GLY   B 46  ? 0.2091 0.2132 0.2548 0.0205  -0.0439 0.0182  46  GLY   B C   
4902 O  O   A GLY   B 46  ? 0.2225 0.2182 0.4024 0.0295  -0.0178 -0.0167 46  GLY   B O   
4903 O  O   B GLY   B 46  ? 0.2107 0.2254 0.2699 0.0264  -0.0453 0.0329  46  GLY   B O   
4910 N  N   . GLY   B 47  ? 0.2106 0.2153 0.2716 0.0083  -0.0260 0.0010  47  GLY   B N   
4911 C  CA  . GLY   B 47  ? 0.2021 0.1901 0.2269 0.0085  -0.0215 0.0034  47  GLY   B CA  
4912 C  C   . GLY   B 47  ? 0.1805 0.1714 0.1902 0.0107  0.0027  0.0048  47  GLY   B C   
4913 O  O   . GLY   B 47  ? 0.1923 0.1536 0.1979 0.0030  -0.0104 0.0103  47  GLY   B O   
4918 N  N   . GLY   B 48  ? 0.1654 0.1558 0.2024 0.0008  -0.0066 0.0157  48  GLY   B N   
4919 C  CA  . GLY   B 48  ? 0.1589 0.1565 0.1947 -0.0015 -0.0039 0.0025  48  GLY   B CA  
4920 C  C   . GLY   B 48  ? 0.1568 0.1482 0.1620 -0.0018 0.0023  0.0091  48  GLY   B C   
4921 O  O   . GLY   B 48  ? 0.1529 0.1512 0.1979 0.0047  -0.0067 0.0050  48  GLY   B O   
4925 N  N   . VAL   B 49  ? 0.1587 0.1576 0.1594 0.0107  -0.0010 0.0116  49  VAL   B N   
4926 C  CA  . VAL   B 49  ? 0.1598 0.1611 0.1565 0.0149  -0.0169 -0.0057 49  VAL   B CA  
4927 C  C   . VAL   B 49  ? 0.1504 0.1530 0.1481 0.0136  -0.0108 0.0024  49  VAL   B C   
4928 O  O   . VAL   B 49  ? 0.1624 0.1592 0.1596 0.0015  -0.0018 0.0060  49  VAL   B O   
4929 C  CB  . VAL   B 49  ? 0.1651 0.1777 0.1947 0.0069  -0.0287 0.0081  49  VAL   B CB  
4930 C  CG1 . VAL   B 49  ? 0.1651 0.1856 0.1851 0.0126  -0.0324 0.0087  49  VAL   B CG1 
4931 C  CG2 . VAL   B 49  ? 0.1820 0.1925 0.2340 -0.0063 -0.0541 0.0076  49  VAL   B CG2 
4941 N  N   . ALA   B 50  ? 0.1449 0.1495 0.1553 0.0048  -0.0070 0.0069  50  ALA   B N   
4942 C  CA  . ALA   B 50  ? 0.1462 0.1434 0.1566 0.0074  -0.0053 0.0081  50  ALA   B CA  
4943 C  C   . ALA   B 50  ? 0.1502 0.1470 0.1532 0.0047  -0.0041 0.0038  50  ALA   B C   
4944 O  O   . ALA   B 50  ? 0.1524 0.1547 0.1485 0.0068  -0.0047 -0.0014 50  ALA   B O   
4945 C  CB  . ALA   B 50  ? 0.1568 0.1453 0.1659 0.0062  -0.0027 0.0065  50  ALA   B CB  
4951 N  N   . GLY   B 51  ? 0.1569 0.1614 0.1603 0.0079  -0.0156 0.0096  51  GLY   B N   
4952 C  CA  . GLY   B 51  ? 0.1569 0.1626 0.1661 0.0207  -0.0129 0.0152  51  GLY   B CA  
4953 C  C   . GLY   B 51  ? 0.1547 0.1545 0.1829 0.0145  -0.0187 0.0111  51  GLY   B C   
4954 O  O   . GLY   B 51  ? 0.1566 0.1632 0.2003 0.0023  -0.0130 0.0021  51  GLY   B O   
4958 N  N   . ALA   B 52  ? 0.1504 0.1517 0.1764 0.0159  -0.0077 0.0123  52  ALA   B N   
4959 C  CA  . ALA   B 52  ? 0.1543 0.1584 0.1643 0.0171  0.0010  0.0011  52  ALA   B CA  
4960 C  C   . ALA   B 52  ? 0.1441 0.1593 0.1454 0.0149  0.0041  0.0007  52  ALA   B C   
4961 O  O   . ALA   B 52  ? 0.1526 0.1661 0.1713 0.0097  0.0021  0.0031  52  ALA   B O   
4962 C  CB  . ALA   B 52  ? 0.1756 0.1602 0.1759 0.0063  -0.0000 -0.0102 52  ALA   B CB  
4968 N  N   . LEU   B 53  ? 0.1469 0.1547 0.1426 0.0171  -0.0020 0.0095  53  LEU   B N   
4969 C  CA  . LEU   B 53  ? 0.1448 0.1657 0.1490 0.0137  -0.0089 0.0053  53  LEU   B CA  
4970 C  C   . LEU   B 53  ? 0.1482 0.1599 0.1527 0.0106  0.0033  -0.0000 53  LEU   B C   
4971 O  O   . LEU   B 53  ? 0.1514 0.1681 0.1580 0.0037  0.0003  0.0122  53  LEU   B O   
4972 C  CB  . LEU   B 53  ? 0.1491 0.1672 0.1580 0.0058  -0.0030 0.0209  53  LEU   B CB  
4973 C  CG  . LEU   B 53  ? 0.1417 0.1736 0.1626 0.0019  -0.0021 0.0256  53  LEU   B CG  
4974 C  CD1 . LEU   B 53  ? 0.1504 0.1943 0.2056 0.0070  -0.0024 0.0163  53  LEU   B CD1 
4975 C  CD2 . LEU   B 53  ? 0.1641 0.2034 0.1999 -0.0111 -0.0108 -0.0024 53  LEU   B CD2 
4987 N  N   . ASN   B 54  ? 0.1543 0.1511 0.1483 0.0090  -0.0046 0.0015  54  ASN   B N   
4988 C  CA  . ASN   B 54  ? 0.1547 0.1614 0.1627 0.0073  -0.0101 -0.0022 54  ASN   B CA  
4989 C  C   . ASN   B 54  ? 0.1454 0.1662 0.1875 0.0019  0.0026  -0.0003 54  ASN   B C   
4990 O  O   . ASN   B 54  ? 0.1423 0.1730 0.1978 0.0003  0.0044  -0.0030 54  ASN   B O   
4991 C  CB  . ASN   B 54  ? 0.1578 0.1764 0.1672 0.0096  -0.0077 0.0081  54  ASN   B CB  
4992 C  CG  . ASN   B 54  ? 0.1643 0.1826 0.1672 0.0066  -0.0142 0.0031  54  ASN   B CG  
4993 O  OD1 . ASN   B 54  ? 0.1533 0.1758 0.1830 0.0061  -0.0119 -0.0102 54  ASN   B OD1 
4994 N  ND2 . ASN   B 54  ? 0.1820 0.1930 0.2032 -0.0005 -0.0370 0.0111  54  ASN   B ND2 
5001 N  N   . LYS   B 55  ? 0.1497 0.1719 0.1891 0.0101  -0.0045 0.0007  55  LYS   B N   
5002 C  CA  . LYS   B 55  ? 0.1484 0.1809 0.2193 0.0178  -0.0038 0.0035  55  LYS   B CA  
5003 C  C   . LYS   B 55  ? 0.1455 0.1750 0.2219 0.0128  0.0037  -0.0016 55  LYS   B C   
5004 O  O   . LYS   B 55  ? 0.1430 0.1883 0.2266 0.0107  0.0011  -0.0067 55  LYS   B O   
5005 C  CB  . LYS   B 55  ? 0.1616 0.1964 0.2494 0.0284  0.0082  0.0150  55  LYS   B CB  
5006 C  CG  . LYS   B 55  ? 0.2102 0.2240 0.3314 0.0295  0.0187  0.0246  55  LYS   B CG  
5007 C  CD  . LYS   B 55  ? 0.2527 0.2454 0.4005 0.0399  0.0318  0.0280  55  LYS   B CD  
5008 C  CE  . LYS   B 55  ? 0.2849 0.2670 0.4550 0.0430  0.0467  0.0265  55  LYS   B CE  
5009 N  NZ  . LYS   B 55  ? 0.2977 0.2822 0.4899 0.0462  0.0318  0.0479  55  LYS   B NZ  
5023 N  N   . ALA   B 56  ? 0.1465 0.1780 0.2024 0.0077  -0.0028 0.0019  56  ALA   B N   
5024 C  CA  . ALA   B 56  ? 0.1639 0.2030 0.2037 0.0011  0.0023  -0.0007 56  ALA   B CA  
5025 C  C   . ALA   B 56  ? 0.1639 0.1986 0.1920 -0.0030 0.0167  0.0008  56  ALA   B C   
5026 O  O   . ALA   B 56  ? 0.1714 0.2014 0.1986 0.0046  0.0282  0.0062  56  ALA   B O   
5027 C  CB  . ALA   B 56  ? 0.1778 0.2216 0.1937 -0.0174 -0.0038 0.0039  56  ALA   B CB  
5033 N  N   . THR   B 57  ? 0.1552 0.1854 0.1889 0.0016  0.0104  0.0014  57  THR   B N   
5034 C  CA  . THR   B 57  ? 0.1635 0.1834 0.1827 -0.0066 0.0173  0.0111  57  THR   B CA  
5035 C  C   . THR   B 57  ? 0.1646 0.1965 0.2160 -0.0026 0.0143  0.0086  57  THR   B C   
5036 O  O   . THR   B 57  ? 0.1688 0.2025 0.2150 -0.0158 0.0122  0.0046  57  THR   B O   
5037 C  CB  . THR   B 57  ? 0.1763 0.1671 0.1613 -0.0091 0.0143  0.0168  57  THR   B CB  
5038 O  OG1 . THR   B 57  ? 0.1724 0.1652 0.1894 -0.0030 0.0063  0.0118  57  THR   B OG1 
5039 C  CG2 . THR   B 57  ? 0.1691 0.1698 0.1710 -0.0055 0.0107  0.0096  57  THR   B CG2 
5047 N  N   . ASN   B 58  ? 0.1519 0.2108 0.2353 -0.0179 -0.0018 -0.0106 58  ASN   B N   
5048 C  CA  . ASN   B 58  ? 0.1627 0.2498 0.2726 -0.0320 0.0278  0.0051  58  ASN   B CA  
5049 C  C   . ASN   B 58  ? 0.1540 0.2326 0.2404 -0.0257 -0.0063 0.0049  58  ASN   B C   
5050 O  O   . ASN   B 58  ? 0.1620 0.2454 0.2560 -0.0293 -0.0070 -0.0134 58  ASN   B O   
5051 C  CB  . ASN   B 58  ? 0.2378 0.3042 0.3914 -0.0501 0.0625  0.0098  58  ASN   B CB  
5052 C  CG  . ASN   B 58  ? 0.4112 0.4242 0.5275 -0.0609 0.0661  0.0279  58  ASN   B CG  
5053 O  OD1 . ASN   B 58  ? 0.4355 0.4355 0.5832 -0.0647 0.0618  0.0327  58  ASN   B OD1 
5054 N  ND2 . ASN   B 58  ? 0.5188 0.5188 0.5788 -0.0664 0.0686  0.0379  58  ASN   B ND2 
5061 N  N   . ASN   B 59  ? 0.1526 0.2126 0.2203 -0.0124 -0.0078 0.0096  59  ASN   B N   
5062 C  CA  . ASN   B 59  ? 0.1573 0.2104 0.1954 -0.0099 -0.0199 0.0108  59  ASN   B CA  
5063 C  C   . ASN   B 59  ? 0.1552 0.2011 0.1959 -0.0153 -0.0144 -0.0074 59  ASN   B C   
5064 O  O   . ASN   B 59  ? 0.1563 0.2077 0.1906 -0.0151 -0.0107 -0.0016 59  ASN   B O   
5065 C  CB  . ASN   B 59  ? 0.1656 0.2239 0.2244 -0.0082 -0.0252 0.0133  59  ASN   B CB  
5066 C  CG  . ASN   B 59  ? 0.1818 0.2420 0.2302 -0.0116 -0.0379 0.0133  59  ASN   B CG  
5067 O  OD1 . ASN   B 59  ? 0.1897 0.2489 0.2309 -0.0126 -0.0306 0.0333  59  ASN   B OD1 
5068 N  ND2 . ASN   B 59  ? 0.1887 0.2554 0.2458 -0.0134 -0.0437 0.0018  59  ASN   B ND2 
5075 N  N   . ALA   B 60  ? 0.1585 0.1943 0.2062 -0.0118 -0.0036 -0.0054 60  ALA   B N   
5076 C  CA  . ALA   B 60  ? 0.1653 0.1831 0.2029 -0.0216 0.0047  -0.0003 60  ALA   B CA  
5077 C  C   . ALA   B 60  ? 0.1639 0.1707 0.1682 -0.0164 -0.0026 -0.0004 60  ALA   B C   
5078 O  O   . ALA   B 60  ? 0.1714 0.1723 0.1914 -0.0231 0.0049  -0.0068 60  ALA   B O   
5079 C  CB  . ALA   B 60  ? 0.1777 0.1764 0.2422 -0.0185 0.0134  0.0033  60  ALA   B CB  
5085 N  N   . MET   B 61  ? 0.1543 0.1591 0.1705 -0.0164 -0.0047 -0.0020 61  MET   B N   
5086 C  CA  . MET   B 61  ? 0.1554 0.1580 0.1721 -0.0061 -0.0156 0.0008  61  MET   B CA  
5087 C  C   . MET   B 61  ? 0.1656 0.1529 0.1713 -0.0083 -0.0130 0.0012  61  MET   B C   
5088 O  O   . MET   B 61  ? 0.1622 0.1560 0.1521 -0.0008 -0.0069 -0.0117 61  MET   B O   
5089 C  CB  . MET   B 61  ? 0.1513 0.1638 0.1644 -0.0025 -0.0139 -0.0043 61  MET   B CB  
5090 C  CG  . MET   B 61  ? 0.1519 0.1570 0.1448 -0.0014 -0.0070 0.0063  61  MET   B CG  
5091 S  SD  . MET   B 61  ? 0.1517 0.1604 0.1768 -0.0041 -0.0064 -0.0076 61  MET   B SD  
5092 C  CE  . MET   B 61  ? 0.1566 0.1809 0.2047 0.0004  -0.0001 -0.0277 61  MET   B CE  
5102 N  N   . GLN   B 62  ? 0.1618 0.1591 0.1585 -0.0031 -0.0278 0.0007  62  GLN   B N   
5103 C  CA  . GLN   B 62  ? 0.1671 0.1673 0.1689 0.0012  -0.0304 -0.0066 62  GLN   B CA  
5104 C  C   . GLN   B 62  ? 0.1632 0.1669 0.1757 -0.0006 -0.0371 -0.0070 62  GLN   B C   
5105 O  O   . GLN   B 62  ? 0.1744 0.1700 0.1863 -0.0004 -0.0350 -0.0158 62  GLN   B O   
5106 C  CB  . GLN   B 62  ? 0.1664 0.1722 0.1614 -0.0012 -0.0219 0.0026  62  GLN   B CB  
5107 C  CG  . GLN   B 62  ? 0.1709 0.1808 0.1554 -0.0012 -0.0313 -0.0042 62  GLN   B CG  
5108 C  CD  . GLN   B 62  ? 0.1734 0.1727 0.1569 0.0045  -0.0261 0.0067  62  GLN   B CD  
5109 O  OE1 . GLN   B 62  ? 0.1694 0.1675 0.1836 -0.0021 -0.0268 -0.0042 62  GLN   B OE1 
5110 N  NE2 . GLN   B 62  ? 0.1750 0.1783 0.1591 -0.0034 -0.0251 -0.0026 62  GLN   B NE2 
5119 N  N   . VAL   B 63  ? 0.1605 0.1717 0.1949 -0.0084 -0.0328 -0.0066 63  VAL   B N   
5120 C  CA  . VAL   B 63  ? 0.1762 0.1779 0.2143 -0.0169 -0.0391 -0.0067 63  VAL   B CA  
5121 C  C   . VAL   B 63  ? 0.1765 0.1662 0.1985 -0.0235 -0.0402 -0.0172 63  VAL   B C   
5122 O  O   . VAL   B 63  ? 0.1930 0.1676 0.2136 -0.0187 -0.0530 -0.0173 63  VAL   B O   
5123 C  CB  . VAL   B 63  ? 0.1749 0.1996 0.2537 -0.0250 -0.0386 -0.0138 63  VAL   B CB  
5124 C  CG1 . VAL   B 63  ? 0.1828 0.2031 0.2697 -0.0356 -0.0230 -0.0118 63  VAL   B CG1 
5125 C  CG2 . VAL   B 63  ? 0.1650 0.2210 0.2663 -0.0179 -0.0402 -0.0118 63  VAL   B CG2 
5135 N  N   . GLU   B 64  ? 0.1690 0.1592 0.1896 -0.0118 -0.0288 -0.0129 64  GLU   B N   
5136 C  CA  . GLU   B 64  ? 0.1730 0.1513 0.1718 -0.0072 -0.0309 -0.0015 64  GLU   B CA  
5137 C  C   . GLU   B 64  ? 0.1714 0.1448 0.1494 -0.0085 -0.0325 -0.0175 64  GLU   B C   
5138 O  O   . GLU   B 64  ? 0.1826 0.1586 0.1544 -0.0072 -0.0279 -0.0192 64  GLU   B O   
5139 C  CB  . GLU   B 64  ? 0.1695 0.1641 0.1970 -0.0166 -0.0229 0.0015  64  GLU   B CB  
5140 C  CG  . GLU   B 64  ? 0.1773 0.1678 0.1789 -0.0240 -0.0300 -0.0076 64  GLU   B CG  
5141 C  CD  . GLU   B 64  ? 0.1831 0.1817 0.1878 -0.0391 -0.0294 -0.0147 64  GLU   B CD  
5142 O  OE1 . GLU   B 64  ? 0.1869 0.1951 0.1925 -0.0371 -0.0182 -0.0239 64  GLU   B OE1 
5143 O  OE2 . GLU   B 64  ? 0.1989 0.1898 0.1922 -0.0363 -0.0407 -0.0116 64  GLU   B OE2 
5150 N  N   . SER   B 65  ? 0.1721 0.1465 0.1585 -0.0098 -0.0203 -0.0162 65  SER   B N   
5151 C  CA  . SER   B 65  ? 0.1721 0.1512 0.1701 0.0008  -0.0281 -0.0124 65  SER   B CA  
5152 C  C   . SER   B 65  ? 0.1778 0.1621 0.1712 -0.0019 -0.0339 -0.0187 65  SER   B C   
5153 O  O   . SER   B 65  ? 0.1717 0.1661 0.1612 -0.0019 -0.0233 -0.0175 65  SER   B O   
5154 C  CB  . SER   B 65  ? 0.1750 0.1548 0.1717 -0.0035 -0.0209 -0.0145 65  SER   B CB  
5155 O  OG  . SER   B 65  ? 0.1703 0.1526 0.1759 -0.0102 -0.0177 -0.0190 65  SER   B OG  
5161 N  N   . ASP   B 66  ? 0.1826 0.1632 0.1636 -0.0027 -0.0275 -0.0176 66  ASP   B N   
5162 C  CA  . ASP   B 66  ? 0.1850 0.1694 0.1630 -0.0019 -0.0353 -0.0118 66  ASP   B CA  
5163 C  C   . ASP   B 66  ? 0.1883 0.1739 0.1526 -0.0050 -0.0309 -0.0182 66  ASP   B C   
5164 O  O   . ASP   B 66  ? 0.1941 0.1803 0.1636 0.0059  -0.0303 -0.0260 66  ASP   B O   
5165 C  CB  . ASP   B 66  ? 0.2026 0.1761 0.1808 0.0061  -0.0484 -0.0226 66  ASP   B CB  
5166 C  CG  . ASP   B 66  ? 0.2312 0.1874 0.2117 0.0152  -0.0537 -0.0037 66  ASP   B CG  
5167 O  OD1 . ASP   B 66  ? 0.2577 0.1866 0.2150 0.0045  -0.0537 0.0103  66  ASP   B OD1 
5168 O  OD2 . ASP   B 66  ? 0.2472 0.2104 0.2844 0.0366  -0.0532 -0.0060 66  ASP   B OD2 
5173 N  N   . ASP   B 67  ? 0.1881 0.1628 0.1561 -0.0162 -0.0295 -0.0186 67  ASP   B N   
5174 C  CA  . ASP   B 67  ? 0.2024 0.1653 0.1659 -0.0076 -0.0266 -0.0091 67  ASP   B CA  
5175 C  C   . ASP   B 67  ? 0.1942 0.1646 0.1786 -0.0027 -0.0233 -0.0184 67  ASP   B C   
5176 O  O   . ASP   B 67  ? 0.1988 0.1739 0.1846 -0.0018 -0.0154 -0.0244 67  ASP   B O   
5177 C  CB  . ASP   B 67  ? 0.2226 0.1719 0.2001 -0.0130 -0.0393 -0.0078 67  ASP   B CB  
5178 C  CG  . ASP   B 67  ? 0.2613 0.1784 0.2147 -0.0098 -0.0702 -0.0161 67  ASP   B CG  
5179 O  OD1 . ASP   B 67  ? 0.2831 0.1883 0.2326 -0.0122 -0.0688 -0.0166 67  ASP   B OD1 
5180 O  OD2 . ASP   B 67  ? 0.2788 0.1838 0.2283 0.0024  -0.0770 -0.0141 67  ASP   B OD2 
5185 N  N   . TYR   B 68  ? 0.1866 0.1628 0.1828 -0.0041 -0.0436 -0.0262 68  TYR   B N   
5186 C  CA  . TYR   B 68  ? 0.1835 0.1780 0.1962 0.0090  -0.0442 -0.0312 68  TYR   B CA  
5187 C  C   . TYR   B 68  ? 0.1789 0.1756 0.1865 0.0045  -0.0429 -0.0388 68  TYR   B C   
5188 O  O   . TYR   B 68  ? 0.1886 0.1834 0.2038 0.0089  -0.0415 -0.0570 68  TYR   B O   
5189 C  CB  . TYR   B 68  ? 0.1936 0.1928 0.1891 0.0130  -0.0546 -0.0463 68  TYR   B CB  
5190 C  CG  . TYR   B 68  ? 0.2028 0.2134 0.2038 0.0206  -0.0460 -0.0606 68  TYR   B CG  
5191 C  CD1 . TYR   B 68  ? 0.2015 0.2218 0.2374 0.0055  -0.0417 -0.0698 68  TYR   B CD1 
5192 C  CD2 . TYR   B 68  ? 0.2010 0.2373 0.2138 0.0249  -0.0515 -0.0579 68  TYR   B CD2 
5193 C  CE1 . TYR   B 68  ? 0.2062 0.2408 0.2476 0.0082  -0.0360 -0.0783 68  TYR   B CE1 
5194 C  CE2 . TYR   B 68  ? 0.1960 0.2450 0.2288 0.0216  -0.0327 -0.0794 68  TYR   B CE2 
5195 C  CZ  . TYR   B 68  ? 0.1974 0.2481 0.2471 0.0112  -0.0345 -0.0756 68  TYR   B CZ  
5196 O  OH  . TYR   B 68  ? 0.1942 0.2694 0.2824 0.0021  -0.0291 -0.0509 68  TYR   B OH  
5206 N  N   . ILE   B 69  ? 0.1761 0.1683 0.1819 0.0015  -0.0366 -0.0362 69  ILE   B N   
5207 C  CA  . ILE   B 69  ? 0.1863 0.1700 0.1927 -0.0030 -0.0194 -0.0370 69  ILE   B CA  
5208 C  C   . ILE   B 69  ? 0.1865 0.1674 0.1814 0.0050  -0.0394 -0.0323 69  ILE   B C   
5209 O  O   . ILE   B 69  ? 0.1949 0.1788 0.1725 0.0065  -0.0256 -0.0314 69  ILE   B O   
5210 C  CB  . ILE   B 69  ? 0.1972 0.1765 0.2047 -0.0079 0.0048  -0.0382 69  ILE   B CB  
5211 C  CG1 . ILE   B 69  ? 0.1935 0.1810 0.2197 -0.0117 0.0054  -0.0448 69  ILE   B CG1 
5212 C  CG2 . ILE   B 69  ? 0.2114 0.1889 0.2148 -0.0088 0.0092  -0.0298 69  ILE   B CG2 
5213 C  CD1 . ILE   B 69  ? 0.1869 0.1950 0.2373 -0.0176 -0.0023 -0.0486 69  ILE   B CD1 
5225 N  N   . ALA   B 70  ? 0.1879 0.1696 0.1801 0.0076  -0.0409 -0.0297 70  ALA   B N   
5226 C  CA  . ALA   B 70  ? 0.1866 0.1745 0.1656 0.0074  -0.0527 -0.0257 70  ALA   B CA  
5227 C  C   . ALA   B 70  ? 0.1926 0.1719 0.1855 -0.0030 -0.0487 -0.0345 70  ALA   B C   
5228 O  O   . ALA   B 70  ? 0.2015 0.1735 0.1884 -0.0014 -0.0376 -0.0340 70  ALA   B O   
5229 C  CB  . ALA   B 70  ? 0.1922 0.1897 0.1706 -0.0012 -0.0508 -0.0236 70  ALA   B CB  
5235 N  N   . THR   B 71  ? 0.2093 0.1715 0.2012 -0.0013 -0.0613 -0.0360 71  THR   B N   
5236 C  CA  . THR   B 71  ? 0.2208 0.1780 0.2135 0.0069  -0.0703 -0.0394 71  THR   B CA  
5237 C  C   . THR   B 71  ? 0.2117 0.1777 0.2470 0.0276  -0.0683 -0.0579 71  THR   B C   
5238 O  O   . THR   B 71  ? 0.2260 0.1843 0.2866 0.0304  -0.0641 -0.0638 71  THR   B O   
5239 C  CB  . THR   B 71  ? 0.2439 0.1993 0.2365 0.0051  -0.0807 -0.0246 71  THR   B CB  
5240 O  OG1 . THR   B 71  ? 0.2567 0.2193 0.2892 -0.0114 -0.0724 -0.0104 71  THR   B OG1 
5241 C  CG2 . THR   B 71  ? 0.2634 0.1963 0.2696 0.0036  -0.0734 -0.0054 71  THR   B CG2 
5249 N  N   . ASN   B 72  ? 0.1962 0.1898 0.2332 0.0186  -0.0614 -0.0670 72  ASN   B N   
5250 C  CA  . ASN   B 72  ? 0.1930 0.2025 0.2281 0.0148  -0.0522 -0.0765 72  ASN   B CA  
5251 C  C   . ASN   B 72  ? 0.1942 0.2187 0.2457 -0.0043 -0.0359 -0.0733 72  ASN   B C   
5252 O  O   . ASN   B 72  ? 0.2013 0.2326 0.2806 0.0008  -0.0136 -0.0834 72  ASN   B O   
5253 C  CB  . ASN   B 72  ? 0.2016 0.2199 0.2617 0.0141  -0.0614 -0.0663 72  ASN   B CB  
5254 C  CG  . ASN   B 72  ? 0.2172 0.2347 0.2632 0.0279  -0.0624 -0.0446 72  ASN   B CG  
5255 O  OD1 . ASN   B 72  ? 0.2394 0.2568 0.2574 0.0193  -0.0455 -0.0438 72  ASN   B OD1 
5256 N  ND2 . ASN   B 72  ? 0.2312 0.2428 0.2990 0.0475  -0.0578 -0.0065 72  ASN   B ND2 
5263 N  N   . GLY   B 73  ? 0.1967 0.2151 0.2209 -0.0076 -0.0356 -0.0642 73  GLY   B N   
5264 C  CA  . GLY   B 73  ? 0.1922 0.2199 0.2065 -0.0071 -0.0258 -0.0510 73  GLY   B CA  
5265 C  C   . GLY   B 73  ? 0.1870 0.2139 0.1608 0.0060  -0.0290 -0.0424 73  GLY   B C   
5266 O  O   . GLY   B 73  ? 0.1832 0.1978 0.1722 0.0029  -0.0204 -0.0302 73  GLY   B O   
5270 N  N   . PRO   B 74  ? 0.1922 0.2272 0.1455 0.0050  -0.0262 -0.0410 74  PRO   B N   
5271 C  CA  . PRO   B 74  ? 0.1842 0.2267 0.1311 0.0109  -0.0187 -0.0227 74  PRO   B CA  
5272 C  C   . PRO   B 74  ? 0.1709 0.2114 0.1333 0.0112  -0.0151 -0.0113 74  PRO   B C   
5273 O  O   . PRO   B 74  ? 0.1761 0.2101 0.1858 0.0083  -0.0108 -0.0270 74  PRO   B O   
5274 C  CB  . PRO   B 74  ? 0.1935 0.2456 0.1442 0.0060  -0.0153 -0.0135 74  PRO   B CB  
5275 C  CG  . PRO   B 74  ? 0.2158 0.2582 0.1880 0.0068  -0.0165 -0.0152 74  PRO   B CG  
5276 C  CD  . PRO   B 74  ? 0.2132 0.2457 0.1710 0.0137  -0.0204 -0.0313 74  PRO   B CD  
5284 N  N   . LEU   B 75  ? 0.1679 0.2022 0.1293 0.0077  -0.0165 -0.0154 75  LEU   B N   
5285 C  CA  . LEU   B 75  ? 0.1694 0.2012 0.1419 0.0007  -0.0182 -0.0109 75  LEU   B CA  
5286 C  C   . LEU   B 75  ? 0.1773 0.2143 0.1329 0.0053  -0.0104 -0.0101 75  LEU   B C   
5287 O  O   . LEU   B 75  ? 0.1912 0.2255 0.1504 -0.0018 -0.0142 -0.0009 75  LEU   B O   
5288 C  CB  . LEU   B 75  ? 0.1794 0.1999 0.1358 -0.0116 -0.0227 0.0040  75  LEU   B CB  
5289 C  CG  . LEU   B 75  ? 0.2085 0.2146 0.1566 -0.0302 -0.0087 0.0046  75  LEU   B CG  
5290 C  CD1 . LEU   B 75  ? 0.2379 0.2268 0.1696 -0.0416 0.0151  0.0013  75  LEU   B CD1 
5291 C  CD2 . LEU   B 75  ? 0.2454 0.2350 0.2305 -0.0252 -0.0004 0.0080  75  LEU   B CD2 
5303 N  N   . LYS   B 76  ? 0.1785 0.2389 0.1643 -0.0004 -0.0063 0.0047  76  LYS   B N   
5304 C  CA  . LYS   B 76  ? 0.1893 0.2466 0.1950 -0.0132 0.0193  0.0038  76  LYS   B CA  
5305 C  C   . LYS   B 76  ? 0.1796 0.2214 0.1699 -0.0012 0.0115  0.0238  76  LYS   B C   
5306 O  O   . LYS   B 76  ? 0.1820 0.2035 0.1677 -0.0027 0.0020  0.0248  76  LYS   B O   
5307 C  CB  . LYS   B 76  ? 0.2041 0.2581 0.2465 -0.0209 0.0478  -0.0216 76  LYS   B CB  
5308 C  CG  . LYS   B 76  ? 0.2047 0.2764 0.2835 -0.0029 0.0377  -0.0321 76  LYS   B CG  
5309 C  CD  . LYS   B 76  ? 0.2093 0.2832 0.3370 0.0077  0.0187  -0.0582 76  LYS   B CD  
5310 C  CE  . LYS   B 76  ? 0.2242 0.2981 0.3750 0.0134  0.0068  -0.0708 76  LYS   B CE  
5311 N  NZ  . LYS   B 76  ? 0.2267 0.3014 0.4100 0.0088  -0.0126 -0.0899 76  LYS   B NZ  
5325 N  N   . VAL   B 77  ? 0.1908 0.2326 0.1798 0.0113  0.0136  0.0258  77  VAL   B N   
5326 C  CA  . VAL   B 77  ? 0.1919 0.2260 0.1902 0.0221  0.0248  0.0543  77  VAL   B CA  
5327 C  C   . VAL   B 77  ? 0.1750 0.2015 0.1758 0.0211  0.0248  0.0392  77  VAL   B C   
5328 O  O   . VAL   B 77  ? 0.1784 0.1969 0.1660 0.0250  0.0247  0.0290  77  VAL   B O   
5329 C  CB  . VAL   B 77  ? 0.1983 0.2387 0.2280 0.0200  0.0366  0.0700  77  VAL   B CB  
5330 C  CG1 . VAL   B 77  ? 0.2036 0.2277 0.2627 0.0059  0.0360  0.0791  77  VAL   B CG1 
5331 C  CG2 . VAL   B 77  ? 0.2086 0.2570 0.2423 0.0164  0.0196  0.0835  77  VAL   B CG2 
5341 N  N   . GLY   B 78  ? 0.1691 0.1828 0.1755 0.0141  0.0143  0.0270  78  GLY   B N   
5342 C  CA  . GLY   B 78  ? 0.1717 0.1817 0.1586 0.0128  0.0253  0.0253  78  GLY   B CA  
5343 C  C   . GLY   B 78  ? 0.1635 0.1704 0.1536 0.0146  0.0238  0.0270  78  GLY   B C   
5344 O  O   . GLY   B 78  ? 0.1674 0.1637 0.1766 0.0189  0.0097  0.0237  78  GLY   B O   
5348 N  N   . GLY   B 79  ? 0.1625 0.1756 0.1503 0.0062  0.0121  0.0114  79  GLY   B N   
5349 C  CA  . GLY   B 79  ? 0.1658 0.1636 0.1455 0.0070  0.0092  0.0102  79  GLY   B CA  
5350 C  C   . GLY   B 79  ? 0.1506 0.1567 0.1526 0.0120  0.0108  0.0045  79  GLY   B C   
5351 O  O   . GLY   B 79  ? 0.1574 0.1530 0.1676 0.0142  0.0157  0.0136  79  GLY   B O   
5355 N  N   . SER   B 80  ? 0.1510 0.1458 0.1643 0.0004  0.0153  0.0046  80  SER   B N   
5356 C  CA  . SER   B 80  ? 0.1427 0.1473 0.1653 0.0028  0.0003  0.0020  80  SER   B CA  
5357 C  C   . SER   B 80  ? 0.1503 0.1451 0.1618 0.0097  -0.0042 0.0010  80  SER   B C   
5358 O  O   . SER   B 80  ? 0.1634 0.1475 0.1820 0.0094  0.0024  -0.0022 80  SER   B O   
5359 C  CB  . SER   B 80  ? 0.1526 0.1548 0.1690 -0.0035 -0.0048 -0.0012 80  SER   B CB  
5360 O  OG  . SER   B 80  ? 0.1608 0.1677 0.1836 -0.0061 -0.0154 0.0083  80  SER   B OG  
5366 N  N   . CYS   B 81  ? 0.1493 0.1346 0.1656 0.0002  -0.0085 -0.0031 81  CYS   B N   
5367 C  CA  . CYS   B 81  ? 0.1552 0.1335 0.1657 0.0057  -0.0197 -0.0041 81  CYS   B CA  
5368 C  C   . CYS   B 81  ? 0.1485 0.1379 0.1446 0.0035  -0.0162 -0.0002 81  CYS   B C   
5369 O  O   . CYS   B 81  ? 0.1725 0.1390 0.1540 0.0098  -0.0006 -0.0039 81  CYS   B O   
5370 C  CB  . CYS   B 81  ? 0.1644 0.1499 0.1542 0.0026  -0.0105 -0.0010 81  CYS   B CB  
5371 S  SG  . CYS   B 81  ? 0.1705 0.1661 0.1621 -0.0051 -0.0272 -0.0103 81  CYS   B SG  
5377 N  N   . VAL   B 82  ? 0.1484 0.1376 0.1585 -0.0027 -0.0155 -0.0017 82  VAL   B N   
5378 C  CA  . VAL   B 82  ? 0.1637 0.1396 0.1502 -0.0076 -0.0175 0.0051  82  VAL   B CA  
5379 C  C   . VAL   B 82  ? 0.1753 0.1331 0.1568 -0.0009 -0.0123 -0.0098 82  VAL   B C   
5380 O  O   . VAL   B 82  ? 0.1789 0.1372 0.1878 0.0028  -0.0141 -0.0162 82  VAL   B O   
5381 C  CB  . VAL   B 82  ? 0.1714 0.1577 0.1641 -0.0079 -0.0216 0.0073  82  VAL   B CB  
5382 C  CG1 . VAL   B 82  ? 0.1887 0.1762 0.1754 0.0073  -0.0213 0.0247  82  VAL   B CG1 
5383 C  CG2 . VAL   B 82  ? 0.1770 0.1713 0.1818 -0.0130 -0.0291 0.0150  82  VAL   B CG2 
5393 N  N   . LEU   B 83  ? 0.1577 0.1270 0.1525 -0.0142 -0.0206 -0.0106 83  LEU   B N   
5394 C  CA  . LEU   B 83  ? 0.1594 0.1379 0.1514 -0.0153 -0.0201 -0.0055 83  LEU   B CA  
5395 C  C   . LEU   B 83  ? 0.1599 0.1343 0.1493 -0.0198 -0.0184 -0.0012 83  LEU   B C   
5396 O  O   . LEU   B 83  ? 0.1607 0.1411 0.1371 -0.0227 -0.0166 0.0055  83  LEU   B O   
5397 C  CB  . LEU   B 83  ? 0.1666 0.1536 0.1608 -0.0199 -0.0208 -0.0069 83  LEU   B CB  
5398 C  CG  . LEU   B 83  ? 0.1844 0.1720 0.1513 -0.0233 -0.0149 -0.0109 83  LEU   B CG  
5399 C  CD1 . LEU   B 83  ? 0.1929 0.1794 0.1748 -0.0073 -0.0259 -0.0096 83  LEU   B CD1 
5400 C  CD2 . LEU   B 83  ? 0.2025 0.1766 0.1690 -0.0110 -0.0157 -0.0231 83  LEU   B CD2 
5412 N  N   . SER   B 84  ? 0.1648 0.1469 0.1734 -0.0255 -0.0199 0.0012  84  SER   B N   
5413 C  CA  . SER   B 84  ? 0.1597 0.1647 0.1651 -0.0285 -0.0191 0.0167  84  SER   B CA  
5414 C  C   . SER   B 84  ? 0.1516 0.1833 0.1155 -0.0203 -0.0161 0.0178  84  SER   B C   
5415 O  O   . SER   B 84  ? 0.1646 0.1656 0.1243 -0.0166 -0.0139 0.0055  84  SER   B O   
5416 C  CB  . SER   B 84  ? 0.1788 0.1796 0.2213 -0.0293 0.0097  0.0208  84  SER   B CB  
5417 O  OG  . SER   B 84  ? 0.1775 0.1901 0.2563 -0.0395 0.0005  0.0255  84  SER   B OG  
5423 N  N   . GLY   B 85  ? 0.1529 0.2025 0.1385 -0.0264 -0.0130 0.0212  85  GLY   B N   
5424 C  CA  . GLY   B 85  ? 0.1577 0.2077 0.1607 -0.0364 0.0012  -0.0038 85  GLY   B CA  
5425 C  C   . GLY   B 85  ? 0.1563 0.1909 0.1441 -0.0398 -0.0011 -0.0023 85  GLY   B C   
5426 O  O   . GLY   B 85  ? 0.1652 0.1920 0.1433 -0.0554 0.0127  -0.0067 85  GLY   B O   
5430 N  N   . HIS   B 86  ? 0.1578 0.1741 0.1615 -0.0304 -0.0118 0.0152  86  HIS   B N   
5431 C  CA  . HIS   B 86  ? 0.1603 0.1735 0.1529 -0.0333 -0.0132 0.0235  86  HIS   B CA  
5432 C  C   . HIS   B 86  ? 0.1575 0.1944 0.1553 -0.0420 -0.0074 0.0341  86  HIS   B C   
5433 O  O   . HIS   B 86  ? 0.1774 0.2079 0.1570 -0.0385 0.0016  0.0332  86  HIS   B O   
5434 C  CB  . HIS   B 86  ? 0.1679 0.1755 0.1652 -0.0277 -0.0259 0.0072  86  HIS   B CB  
5435 C  CG  . HIS   B 86  ? 0.1677 0.1837 0.1630 -0.0189 -0.0250 0.0101  86  HIS   B CG  
5436 N  ND1 . HIS   B 86  ? 0.1727 0.2047 0.1891 -0.0233 -0.0265 0.0013  86  HIS   B ND1 
5437 C  CD2 . HIS   B 86  ? 0.1680 0.1827 0.1694 -0.0109 -0.0321 0.0086  86  HIS   B CD2 
5438 C  CE1 . HIS   B 86  ? 0.1844 0.1992 0.1693 -0.0143 -0.0131 -0.0225 86  HIS   B CE1 
5439 N  NE2 . HIS   B 86  ? 0.1740 0.1915 0.1621 -0.0035 -0.0189 -0.0027 86  HIS   B NE2 
5447 N  N   . ASN   B 87  ? 0.1605 0.1916 0.1620 -0.0387 0.0044  0.0260  87  ASN   B N   
5448 C  CA  . ASN   B 87  ? 0.1660 0.2091 0.1712 -0.0340 0.0237  0.0232  87  ASN   B CA  
5449 C  C   . ASN   B 87  ? 0.1804 0.1918 0.1540 -0.0352 0.0362  0.0130  87  ASN   B C   
5450 O  O   . ASN   B 87  ? 0.2063 0.2081 0.1867 -0.0248 0.0505  0.0106  87  ASN   B O   
5451 C  CB  . ASN   B 87  ? 0.1731 0.2517 0.2034 -0.0337 0.0251  0.0247  87  ASN   B CB  
5452 C  CG  . ASN   B 87  ? 0.1807 0.2735 0.2132 0.0012  0.0298  0.0391  87  ASN   B CG  
5453 O  OD1 . ASN   B 87  ? 0.1746 0.2594 0.2058 0.0026  0.0437  0.0538  87  ASN   B OD1 
5454 N  ND2 . ASN   B 87  ? 0.2131 0.2840 0.2502 0.0046  0.0380  0.0295  87  ASN   B ND2 
5461 N  N   . LEU   B 88  ? 0.1685 0.1810 0.1412 -0.0382 0.0141  0.0051  88  LEU   B N   
5462 C  CA  . LEU   B 88  ? 0.1741 0.1746 0.1550 -0.0335 0.0077  -0.0003 88  LEU   B CA  
5463 C  C   . LEU   B 88  ? 0.1705 0.1655 0.1584 -0.0355 -0.0027 0.0016  88  LEU   B C   
5464 O  O   . LEU   B 88  ? 0.1964 0.1731 0.1908 -0.0251 -0.0323 -0.0088 88  LEU   B O   
5465 C  CB  . LEU   B 88  ? 0.1918 0.1751 0.1655 -0.0469 -0.0047 0.0158  88  LEU   B CB  
5466 C  CG  . LEU   B 88  ? 0.2325 0.2052 0.1876 -0.0383 -0.0285 0.0325  88  LEU   B CG  
5467 C  CD1 . LEU   B 88  ? 0.2472 0.2372 0.1809 -0.0471 -0.0291 0.0523  88  LEU   B CD1 
5468 C  CD2 . LEU   B 88  ? 0.2679 0.2329 0.2420 0.0049  -0.0572 0.0153  88  LEU   B CD2 
5480 N  N   . ALA   B 89  ? 0.1667 0.1606 0.1283 -0.0355 0.0149  0.0043  89  ALA   B N   
5481 C  CA  . ALA   B 89  ? 0.1683 0.1644 0.1129 -0.0380 -0.0013 0.0035  89  ALA   B CA  
5482 C  C   . ALA   B 89  ? 0.1783 0.1667 0.1189 -0.0372 0.0121  0.0063  89  ALA   B C   
5483 O  O   . ALA   B 89  ? 0.1653 0.1784 0.1578 -0.0413 0.0080  -0.0268 89  ALA   B O   
5484 C  CB  . ALA   B 89  ? 0.1615 0.1655 0.1383 -0.0440 0.0049  0.0168  89  ALA   B CB  
5490 N  N   . LYS   B 90  ? 0.2128 0.1490 0.1374 -0.0410 -0.0090 0.0076  90  LYS   B N   
5491 C  CA  . LYS   B 90  ? 0.2208 0.1484 0.1448 -0.0429 -0.0161 0.0127  90  LYS   B CA  
5492 C  C   . LYS   B 90  ? 0.2015 0.1550 0.1535 -0.0425 -0.0164 -0.0045 90  LYS   B C   
5493 O  O   . LYS   B 90  ? 0.2088 0.1708 0.1608 -0.0587 -0.0044 -0.0021 90  LYS   B O   
5494 C  CB  . LYS   B 90  ? 0.2403 0.1520 0.1822 -0.0360 -0.0078 0.0173  90  LYS   B CB  
5495 C  CG  . LYS   B 90  ? 0.2398 0.1755 0.1679 -0.0173 0.0221  0.0175  90  LYS   B CG  
5496 C  CD  . LYS   B 90  ? 0.2718 0.2003 0.2244 -0.0049 0.0388  0.0073  90  LYS   B CD  
5497 C  CE  . LYS   B 90  ? 0.2934 0.2244 0.2733 -0.0173 0.0397  -0.0055 90  LYS   B CE  
5498 N  NZ  . LYS   B 90  ? 0.2920 0.2212 0.2669 -0.0405 0.0576  -0.0185 90  LYS   B NZ  
5512 N  N   . HIS   B 91  ? 0.1762 0.1377 0.1259 -0.0319 -0.0185 0.0033  91  HIS   B N   
5513 C  CA  . HIS   B 91  ? 0.1705 0.1392 0.1449 -0.0214 -0.0212 0.0046  91  HIS   B CA  
5514 C  C   . HIS   B 91  ? 0.1608 0.1463 0.1192 -0.0213 -0.0081 0.0040  91  HIS   B C   
5515 O  O   . HIS   B 91  ? 0.1758 0.1480 0.1162 -0.0237 -0.0242 0.0033  91  HIS   B O   
5516 C  CB  . HIS   B 91  ? 0.1862 0.1386 0.1891 -0.0090 -0.0064 0.0168  91  HIS   B CB  
5517 C  CG  . HIS   B 91  ? 0.2266 0.1592 0.2680 0.0037  0.0241  0.0240  91  HIS   B CG  
5518 N  ND1 . HIS   B 91  ? 0.2561 0.1647 0.3272 0.0146  0.0333  0.0103  91  HIS   B ND1 
5519 C  CD2 . HIS   B 91  ? 0.2330 0.1862 0.3095 0.0171  0.0097  0.0611  91  HIS   B CD2 
5520 C  CE1 . HIS   B 91  ? 0.2568 0.1830 0.3540 0.0332  0.0317  0.0196  91  HIS   B CE1 
5521 N  NE2 . HIS   B 91  ? 0.2450 0.1943 0.3491 0.0324  0.0306  0.0687  91  HIS   B NE2 
5529 N  N   . CYS   B 92  ? 0.1550 0.1395 0.1245 -0.0242 -0.0167 -0.0021 92  CYS   B N   
5530 C  CA  . CYS   B 92  ? 0.1536 0.1310 0.1228 -0.0214 -0.0063 0.0014  92  CYS   B CA  
5531 C  C   . CYS   B 92  ? 0.1460 0.1332 0.1241 -0.0185 -0.0081 0.0005  92  CYS   B C   
5532 O  O   . CYS   B 92  ? 0.1529 0.1380 0.1425 -0.0186 -0.0035 -0.0035 92  CYS   B O   
5533 C  CB  . CYS   B 92  ? 0.1489 0.1459 0.1447 -0.0165 -0.0067 0.0045  92  CYS   B CB  
5534 S  SG  . CYS   B 92  ? 0.1488 0.1437 0.1406 -0.0119 -0.0126 0.0052  92  CYS   B SG  
5540 N  N   . LEU   B 93  ? 0.1400 0.1360 0.1201 -0.0153 -0.0064 -0.0051 93  LEU   B N   
5541 C  CA  . LEU   B 93  ? 0.1407 0.1343 0.1351 -0.0058 -0.0107 -0.0022 93  LEU   B CA  
5542 C  C   . LEU   B 93  ? 0.1368 0.1278 0.1314 -0.0033 -0.0053 0.0052  93  LEU   B C   
5543 O  O   . LEU   B 93  ? 0.1417 0.1282 0.1373 -0.0014 -0.0066 -0.0031 93  LEU   B O   
5544 C  CB  . LEU   B 93  ? 0.1431 0.1336 0.1577 -0.0060 -0.0135 0.0035  93  LEU   B CB  
5545 C  CG  . LEU   B 93  ? 0.1384 0.1452 0.1674 -0.0079 -0.0126 0.0152  93  LEU   B CG  
5546 C  CD1 . LEU   B 93  ? 0.1417 0.1527 0.1642 0.0029  -0.0063 -0.0024 93  LEU   B CD1 
5547 C  CD2 . LEU   B 93  ? 0.1414 0.1510 0.1543 -0.0063 -0.0143 0.0045  93  LEU   B CD2 
5559 N  N   . HIS   B 94  ? 0.1363 0.1260 0.1320 -0.0123 -0.0152 0.0040  94  HIS   B N   
5560 C  CA  . HIS   B 94  ? 0.1391 0.1259 0.1300 -0.0025 -0.0046 0.0067  94  HIS   B CA  
5561 C  C   . HIS   B 94  ? 0.1380 0.1277 0.1452 -0.0038 -0.0019 0.0083  94  HIS   B C   
5562 O  O   . HIS   B 94  ? 0.1426 0.1414 0.1836 -0.0091 0.0150  -0.0064 94  HIS   B O   
5563 C  CB  . HIS   B 94  ? 0.1443 0.1377 0.1374 -0.0023 -0.0074 0.0050  94  HIS   B CB  
5564 C  CG  . HIS   B 94  ? 0.1474 0.1353 0.1324 -0.0050 -0.0164 0.0092  94  HIS   B CG  
5565 N  ND1 . HIS   B 94  ? 0.1454 0.1390 0.1342 -0.0033 -0.0197 0.0094  94  HIS   B ND1 
5566 C  CD2 . HIS   B 94  ? 0.1450 0.1357 0.1403 -0.0005 -0.0167 0.0018  94  HIS   B CD2 
5567 C  CE1 . HIS   B 94  ? 0.1526 0.1381 0.1328 -0.0097 -0.0239 0.0130  94  HIS   B CE1 
5568 N  NE2 . HIS   B 94  ? 0.1420 0.1422 0.1435 -0.0143 -0.0135 0.0068  94  HIS   B NE2 
5576 N  N   . VAL   B 95  ? 0.1280 0.1289 0.1399 -0.0021 0.0006  0.0060  95  VAL   B N   
5577 C  CA  . VAL   B 95  ? 0.1338 0.1392 0.1379 0.0013  0.0026  0.0114  95  VAL   B CA  
5578 C  C   . VAL   B 95  ? 0.1480 0.1361 0.1454 -0.0034 0.0080  0.0043  95  VAL   B C   
5579 O  O   . VAL   B 95  ? 0.1502 0.1342 0.1552 0.0064  0.0041  0.0108  95  VAL   B O   
5580 C  CB  . VAL   B 95  ? 0.1388 0.1385 0.1409 -0.0028 -0.0104 0.0059  95  VAL   B CB  
5581 C  CG1 . VAL   B 95  ? 0.1558 0.1534 0.1634 -0.0107 -0.0002 0.0156  95  VAL   B CG1 
5582 C  CG2 . VAL   B 95  ? 0.1525 0.1375 0.1405 0.0070  -0.0106 0.0027  95  VAL   B CG2 
5592 N  N   . VAL   B 96  ? 0.1472 0.1465 0.1463 0.0121  0.0017  0.0134  96  VAL   B N   
5593 C  CA  . VAL   B 96  ? 0.1520 0.1564 0.1425 0.0110  0.0014  0.0173  96  VAL   B CA  
5594 C  C   . VAL   B 96  ? 0.1605 0.1613 0.1574 0.0108  0.0102  0.0209  96  VAL   B C   
5595 O  O   . VAL   B 96  ? 0.1620 0.1619 0.1768 0.0044  0.0161  0.0126  96  VAL   B O   
5596 C  CB  . VAL   B 96  ? 0.1603 0.1710 0.1490 0.0072  0.0051  0.0123  96  VAL   B CB  
5597 C  CG1 . VAL   B 96  ? 0.1667 0.1784 0.1742 0.0196  0.0038  0.0048  96  VAL   B CG1 
5598 C  CG2 . VAL   B 96  ? 0.1744 0.1751 0.1655 0.0079  0.0072  0.0013  96  VAL   B CG2 
5608 N  N   . GLY   B 97  ? 0.1599 0.1587 0.1454 0.0082  0.0003  0.0219  97  GLY   B N   
5609 C  CA  . GLY   B 97  ? 0.1801 0.1649 0.1525 0.0043  0.0044  0.0281  97  GLY   B CA  
5610 C  C   . GLY   B 97  ? 0.2003 0.1702 0.1659 0.0094  0.0007  0.0198  97  GLY   B C   
5611 O  O   . GLY   B 97  ? 0.2142 0.1757 0.1625 0.0087  -0.0014 0.0140  97  GLY   B O   
5615 N  N   . PRO   B 98  ? 0.2084 0.1763 0.1689 0.0077  0.0211  0.0326  98  PRO   B N   
5616 C  CA  . PRO   B 98  ? 0.2173 0.1935 0.1714 0.0138  0.0323  0.0209  98  PRO   B CA  
5617 C  C   . PRO   B 98  ? 0.2347 0.1944 0.1487 0.0328  0.0451  0.0487  98  PRO   B C   
5618 O  O   . PRO   B 98  ? 0.2276 0.1905 0.1830 0.0311  0.0483  0.0472  98  PRO   B O   
5619 C  CB  . PRO   B 98  ? 0.2084 0.1956 0.2067 0.0048  0.0412  0.0205  98  PRO   B CB  
5620 C  CG  . PRO   B 98  ? 0.2008 0.1895 0.2059 0.0021  0.0326  0.0384  98  PRO   B CG  
5621 C  CD  . PRO   B 98  ? 0.1920 0.1751 0.1953 0.0067  0.0253  0.0370  98  PRO   B CD  
5629 N  N   . ASN   B 99  ? 0.2508 0.2086 0.1633 0.0492  0.0399  0.0306  99  ASN   B N   
5630 C  CA  . ASN   B 99  ? 0.2716 0.2160 0.1712 0.0556  0.0379  0.0451  99  ASN   B CA  
5631 C  C   . ASN   B 99  ? 0.2931 0.2556 0.2095 0.0528  0.0497  0.0744  99  ASN   B C   
5632 O  O   . ASN   B 99  ? 0.2999 0.2600 0.2248 0.0509  0.0334  0.0776  99  ASN   B O   
5633 C  CB  . ASN   B 99  ? 0.2786 0.2122 0.1766 0.0561  0.0281  0.0358  99  ASN   B CB  
5634 C  CG  . ASN   B 99  ? 0.2829 0.2230 0.2031 0.0479  0.0048  0.0316  99  ASN   B CG  
5635 O  OD1 . ASN   B 99  ? 0.2860 0.2260 0.2246 0.0471  0.0068  0.0383  99  ASN   B OD1 
5636 N  ND2 . ASN   B 99  ? 0.2801 0.2207 0.2149 0.0541  -0.0171 0.0326  99  ASN   B ND2 
5643 N  N   A VAL   B 100 ? 0.3080 0.2680 0.2474 0.0409  0.0615  0.1023  100 VAL   B N   
5644 N  N   B VAL   B 100 ? 0.3126 0.2679 0.2494 0.0467  0.0466  0.0886  100 VAL   B N   
5645 C  CA  A VAL   B 100 ? 0.3337 0.2873 0.3092 0.0296  0.0591  0.1107  100 VAL   B CA  
5646 C  CA  B VAL   B 100 ? 0.3359 0.2842 0.2957 0.0392  0.0391  0.0967  100 VAL   B CA  
5647 C  C   A VAL   B 100 ? 0.3539 0.2890 0.2985 0.0375  0.0576  0.1286  100 VAL   B C   
5648 C  C   B VAL   B 100 ? 0.3537 0.2882 0.2948 0.0425  0.0403  0.1174  100 VAL   B C   
5649 O  O   A VAL   B 100 ? 0.3622 0.2991 0.2982 0.0362  0.0630  0.1193  100 VAL   B O   
5650 O  O   B VAL   B 100 ? 0.3570 0.2942 0.2977 0.0396  0.0409  0.1113  100 VAL   B O   
5651 C  CB  A VAL   B 100 ? 0.3414 0.3036 0.3781 0.0049  0.0565  0.1126  100 VAL   B CB  
5652 C  CB  B VAL   B 100 ? 0.3418 0.2959 0.3396 0.0251  0.0338  0.0908  100 VAL   B CB  
5653 C  CG1 A VAL   B 100 ? 0.3439 0.3066 0.3946 -0.0030 0.0552  0.1116  100 VAL   B CG1 
5654 C  CG1 B VAL   B 100 ? 0.3446 0.2994 0.3489 0.0206  0.0326  0.0894  100 VAL   B CG1 
5655 C  CG2 A VAL   B 100 ? 0.3448 0.3103 0.3870 -0.0022 0.0629  0.1195  100 VAL   B CG2 
5656 C  CG2 B VAL   B 100 ? 0.3429 0.2995 0.3472 0.0208  0.0345  0.0907  100 VAL   B CG2 
5675 N  N   . ASN   B 101 ? 0.3683 0.2896 0.2899 0.0499  0.0414  0.1344  101 ASN   B N   
5676 C  CA  . ASN   B 101 ? 0.4046 0.3007 0.3223 0.0623  0.0236  0.1436  101 ASN   B CA  
5677 C  C   . ASN   B 101 ? 0.4384 0.3314 0.3136 0.0676  0.0052  0.1570  101 ASN   B C   
5678 O  O   . ASN   B 101 ? 0.4400 0.3462 0.3537 0.0781  0.0081  0.1199  101 ASN   B O   
5679 C  CB  . ASN   B 101 ? 0.4056 0.2858 0.3274 0.0593  0.0362  0.1239  101 ASN   B CB  
5680 C  CG  . ASN   B 101 ? 0.4023 0.2739 0.3230 0.0594  0.0414  0.1152  101 ASN   B CG  
5681 O  OD1 . ASN   B 101 ? 0.4088 0.2744 0.3680 0.0572  0.0558  0.1054  101 ASN   B OD1 
5682 N  ND2 . ASN   B 101 ? 0.3928 0.2690 0.3236 0.0558  0.0365  0.1029  101 ASN   B ND2 
5690 N  N   . LYS   B 102 ? 0.4689 0.3613 0.3230 0.0545  0.0068  0.1492  102 LYS   B N   
5691 C  CA  . LYS   B 102 ? 0.4955 0.4001 0.3594 0.0393  0.0145  0.1184  102 LYS   B CA  
5692 C  C   . LYS   B 102 ? 0.4908 0.3996 0.3399 0.0392  0.0215  0.1149  102 LYS   B C   
5693 O  O   . LYS   B 102 ? 0.5027 0.4064 0.3470 0.0372  0.0098  0.1068  102 LYS   B O   
5694 C  CB  . LYS   B 102 ? 0.5207 0.4349 0.4048 0.0285  0.0259  0.0798  102 LYS   B CB  
5695 C  CG  . LYS   B 102 ? 0.5400 0.4614 0.4803 0.0222  0.0333  0.0385  102 LYS   B CG  
5696 C  CD  . LYS   B 102 ? 0.5560 0.4829 0.5331 0.0161  0.0412  0.0067  102 LYS   B CD  
5697 C  CE  . LYS   B 102 ? 0.5669 0.4996 0.5835 0.0087  0.0513  -0.0135 102 LYS   B CE  
5698 N  NZ  . LYS   B 102 ? 0.5730 0.5108 0.6128 0.0045  0.0585  -0.0257 102 LYS   B NZ  
5712 N  N   . GLY   B 103 ? 0.4706 0.3907 0.3256 0.0382  0.0425  0.1124  103 GLY   B N   
5713 C  CA  . GLY   B 103 ? 0.4522 0.3844 0.3350 0.0319  0.0676  0.0977  103 GLY   B CA  
5714 C  C   . GLY   B 103 ? 0.4308 0.3771 0.3336 0.0184  0.0830  0.0763  103 GLY   B C   
5715 O  O   . GLY   B 103 ? 0.4365 0.3876 0.3379 0.0079  0.0841  0.0718  103 GLY   B O   
5719 N  N   A GLU   B 104 ? 0.4133 0.3616 0.3131 0.0183  0.1054  0.0661  104 GLU   B N   
5720 N  N   B GLU   B 104 ? 0.4186 0.3706 0.3364 0.0141  0.0707  0.0595  104 GLU   B N   
5721 C  CA  A GLU   B 104 ? 0.3955 0.3455 0.2898 0.0254  0.1162  0.0512  104 GLU   B CA  
5722 C  CA  B GLU   B 104 ? 0.4056 0.3627 0.3320 0.0123  0.0565  0.0406  104 GLU   B CA  
5723 C  C   A GLU   B 104 ? 0.3987 0.3454 0.2978 0.0074  0.1406  0.0556  104 GLU   B C   
5724 C  C   B GLU   B 104 ? 0.3977 0.3583 0.3383 0.0051  0.0610  0.0337  104 GLU   B C   
5725 O  O   A GLU   B 104 ? 0.3950 0.3433 0.3301 0.0067  0.1385  0.0479  104 GLU   B O   
5726 O  O   B GLU   B 104 ? 0.3935 0.3548 0.3536 0.0047  0.0607  0.0311  104 GLU   B O   
5727 C  CB  A GLU   B 104 ? 0.3807 0.3277 0.2735 0.0509  0.0828  0.0245  104 GLU   B CB  
5728 C  CB  B GLU   B 104 ? 0.4009 0.3569 0.3180 0.0160  0.0370  0.0280  104 GLU   B CB  
5729 C  CG  A GLU   B 104 ? 0.3659 0.3122 0.2501 0.0697  0.0344  -0.0063 104 GLU   B CG  
5730 C  CG  B GLU   B 104 ? 0.3939 0.3495 0.3032 0.0168  0.0152  0.0141  104 GLU   B CG  
5731 C  CD  A GLU   B 104 ? 0.3503 0.2949 0.2203 0.0804  -0.0017 -0.0189 104 GLU   B CD  
5732 C  CD  B GLU   B 104 ? 0.3854 0.3402 0.2896 0.0138  -0.0007 0.0046  104 GLU   B CD  
5733 O  OE1 A GLU   B 104 ? 0.3263 0.2784 0.1800 0.0882  0.0023  -0.0149 104 GLU   B OE1 
5734 O  OE1 B GLU   B 104 ? 0.3791 0.3350 0.2802 0.0077  -0.0015 0.0047  104 GLU   B OE1 
5735 O  OE2 A GLU   B 104 ? 0.3578 0.3013 0.2271 0.0764  -0.0275 -0.0335 104 GLU   B OE2 
5736 O  OE2 B GLU   B 104 ? 0.3845 0.3387 0.2911 0.0155  -0.0115 -0.0027 104 GLU   B OE2 
5749 N  N   A ASP   B 105 ? 0.3998 0.3496 0.2994 -0.0084 0.1678  0.0658  105 ASP   B N   
5750 N  N   B ASP   B 105 ? 0.3930 0.3584 0.3450 -0.0017 0.0678  0.0309  105 ASP   B N   
5751 C  CA  A ASP   B 105 ? 0.4037 0.3507 0.3170 -0.0211 0.1895  0.0551  105 ASP   B CA  
5752 C  CA  B ASP   B 105 ? 0.3880 0.3561 0.3477 -0.0071 0.0743  0.0232  105 ASP   B CA  
5753 C  C   A ASP   B 105 ? 0.3858 0.3168 0.2960 -0.0292 0.1837  0.0506  105 ASP   B C   
5754 C  C   B ASP   B 105 ? 0.3781 0.3439 0.3302 -0.0076 0.0729  0.0153  105 ASP   B C   
5755 O  O   A ASP   B 105 ? 0.3789 0.3099 0.2992 -0.0262 0.1830  0.0532  105 ASP   B O   
5756 O  O   B ASP   B 105 ? 0.3762 0.3420 0.3276 -0.0055 0.0724  0.0123  105 ASP   B O   
5757 C  CB  A ASP   B 105 ? 0.4172 0.3801 0.3931 -0.0103 0.1968  0.0293  105 ASP   B CB  
5758 C  CB  B ASP   B 105 ? 0.3884 0.3622 0.3769 -0.0078 0.0811  0.0196  105 ASP   B CB  
5759 C  CG  A ASP   B 105 ? 0.4215 0.3963 0.4530 -0.0043 0.2039  0.0135  105 ASP   B CG  
5760 C  CG  B ASP   B 105 ? 0.3846 0.3624 0.3938 -0.0093 0.0866  0.0189  105 ASP   B CG  
5761 O  OD1 A ASP   B 105 ? 0.4118 0.4014 0.4583 -0.0111 0.2264  0.0186  105 ASP   B OD1 
5762 O  OD1 B ASP   B 105 ? 0.3814 0.3619 0.4031 -0.0113 0.0886  0.0187  105 ASP   B OD1 
5763 O  OD2 A ASP   B 105 ? 0.4297 0.4014 0.4998 0.0048  0.1876  0.0001  105 ASP   B OD2 
5764 O  OD2 B ASP   B 105 ? 0.3805 0.3618 0.4053 -0.0120 0.0915  0.0224  105 ASP   B OD2 
5773 N  N   A ILE   B 106 ? 0.3776 0.2897 0.3160 -0.0303 0.1641  0.0465  106 ILE   B N   
5774 N  N   B ILE   B 106 ? 0.3697 0.3334 0.3286 -0.0063 0.0662  0.0110  106 ILE   B N   
5775 C  CA  A ILE   B 106 ? 0.3595 0.2629 0.3303 -0.0357 0.1666  0.0375  106 ILE   B CA  
5776 C  CA  B ILE   B 106 ? 0.3598 0.3255 0.3286 -0.0049 0.0664  0.0055  106 ILE   B CA  
5777 C  C   A ILE   B 106 ? 0.3266 0.2536 0.3200 -0.0314 0.1667  0.0123  106 ILE   B C   
5778 C  C   B ILE   B 106 ? 0.3444 0.3220 0.3257 -0.0021 0.0672  -0.0031 106 ILE   B C   
5779 O  O   A ILE   B 106 ? 0.3179 0.2280 0.3184 -0.0371 0.1591  0.0019  106 ILE   B O   
5780 O  O   B ILE   B 106 ? 0.3435 0.3174 0.3214 -0.0034 0.0624  -0.0078 106 ILE   B O   
5781 C  CB  A ILE   B 106 ? 0.3802 0.2570 0.3461 -0.0454 0.1588  0.0522  106 ILE   B CB  
5782 C  CB  B ILE   B 106 ? 0.3673 0.3260 0.3328 -0.0070 0.0635  0.0083  106 ILE   B CB  
5783 C  CG1 A ILE   B 106 ? 0.3906 0.2595 0.3625 -0.0378 0.1450  0.0432  106 ILE   B CG1 
5784 C  CG1 B ILE   B 106 ? 0.3720 0.3276 0.3383 -0.0051 0.0592  0.0078  106 ILE   B CG1 
5785 C  CG2 A ILE   B 106 ? 0.3840 0.2587 0.3702 -0.0522 0.1603  0.0610  106 ILE   B CG2 
5786 C  CG2 B ILE   B 106 ? 0.3680 0.3278 0.3419 -0.0079 0.0648  0.0089  106 ILE   B CG2 
5787 C  CD1 A ILE   B 106 ? 0.3974 0.2651 0.3539 -0.0307 0.1438  0.0429  106 ILE   B CD1 
5788 C  CD1 B ILE   B 106 ? 0.3752 0.3292 0.3377 -0.0032 0.0590  0.0084  106 ILE   B CD1 
5811 N  N   A GLN   B 107 ? 0.3099 0.2809 0.3347 -0.0287 0.1581  0.0088  107 GLN   B N   
5812 N  N   B GLN   B 107 ? 0.3311 0.3257 0.3365 -0.0012 0.0691  -0.0043 107 GLN   B N   
5813 C  CA  A GLN   B 107 ? 0.2929 0.3010 0.3548 -0.0286 0.1456  0.0135  107 GLN   B CA  
5814 C  CA  B GLN   B 107 ? 0.3174 0.3257 0.3533 -0.0010 0.0711  -0.0006 107 GLN   B CA  
5815 C  C   A GLN   B 107 ? 0.2697 0.2844 0.3301 -0.0122 0.1079  0.0067  107 GLN   B C   
5816 C  C   B GLN   B 107 ? 0.2871 0.3008 0.3192 0.0036  0.0762  -0.0011 107 GLN   B C   
5817 O  O   A GLN   B 107 ? 0.2589 0.2817 0.3657 0.0002  0.0736  -0.0037 107 GLN   B O   
5818 O  O   B GLN   B 107 ? 0.2849 0.3023 0.3318 0.0080  0.0639  -0.0037 107 GLN   B O   
5819 C  CB  A GLN   B 107 ? 0.3184 0.3405 0.4231 -0.0361 0.1330  0.0184  107 GLN   B CB  
5820 C  CB  B GLN   B 107 ? 0.3368 0.3496 0.4021 -0.0042 0.0629  0.0028  107 GLN   B CB  
5821 C  CG  A GLN   B 107 ? 0.3497 0.3732 0.5019 -0.0308 0.0961  0.0205  107 GLN   B CG  
5822 C  CG  B GLN   B 107 ? 0.3553 0.3694 0.4577 -0.0031 0.0483  0.0057  107 GLN   B CG  
5823 C  CD  A GLN   B 107 ? 0.3740 0.3943 0.5568 -0.0235 0.0704  0.0220  107 GLN   B CD  
5824 C  CD  B GLN   B 107 ? 0.3696 0.3826 0.4970 -0.0002 0.0367  0.0080  107 GLN   B CD  
5825 O  OE1 A GLN   B 107 ? 0.3798 0.4033 0.5804 -0.0104 0.0659  0.0196  107 GLN   B OE1 
5826 O  OE1 B GLN   B 107 ? 0.3724 0.3876 0.5134 0.0050  0.0348  0.0084  107 GLN   B OE1 
5827 N  NE2 A GLN   B 107 ? 0.3888 0.3993 0.5810 -0.0254 0.0620  0.0275  107 GLN   B NE2 
5828 N  NE2 B GLN   B 107 ? 0.3781 0.3863 0.5155 -0.0007 0.0335  0.0106  107 GLN   B NE2 
5845 N  N   . LEU   B 108 ? 0.2549 0.2724 0.2780 0.0086  0.0895  0.0022  108 LEU   B N   
5846 C  CA  . LEU   B 108 ? 0.2340 0.2459 0.2427 0.0215  0.0658  0.0173  108 LEU   B CA  
5847 C  C   . LEU   B 108 ? 0.1944 0.2069 0.2450 0.0186  0.0396  0.0278  108 LEU   B C   
5848 O  O   . LEU   B 108 ? 0.1918 0.1925 0.2282 0.0169  0.0320  0.0331  108 LEU   B O   
5849 C  CB  . LEU   B 108 ? 0.2524 0.2643 0.2206 0.0217  0.0700  0.0355  108 LEU   B CB  
5850 C  CG  . LEU   B 108 ? 0.2779 0.2975 0.2348 0.0208  0.0570  0.0102  108 LEU   B CG  
5851 C  CD1 . LEU   B 108 ? 0.2817 0.3133 0.2093 0.0103  0.0675  0.0178  108 LEU   B CD1 
5852 C  CD2 . LEU   B 108 ? 0.2991 0.3111 0.2483 0.0326  0.0428  -0.0172 108 LEU   B CD2 
5865 N  N   . LEU   B 109 ? 0.1820 0.1903 0.2338 0.0120  0.0366  0.0201  109 LEU   B N   
5866 C  CA  . LEU   B 109 ? 0.1625 0.1571 0.2483 0.0071  0.0349  0.0268  109 LEU   B CA  
5867 C  C   . LEU   B 109 ? 0.1576 0.1389 0.2524 0.0039  0.0379  0.0171  109 LEU   B C   
5868 O  O   . LEU   B 109 ? 0.1489 0.1424 0.2454 0.0053  0.0312  0.0341  109 LEU   B O   
5869 C  CB  . LEU   B 109 ? 0.1701 0.1513 0.2552 0.0075  0.0242  0.0408  109 LEU   B CB  
5870 C  CG  . LEU   B 109 ? 0.1722 0.1512 0.2488 0.0014  0.0211  0.0300  109 LEU   B CG  
5871 C  CD1 . LEU   B 109 ? 0.1666 0.1575 0.2383 0.0138  0.0263  0.0345  109 LEU   B CD1 
5872 C  CD2 . LEU   B 109 ? 0.1825 0.1542 0.2786 0.0007  0.0120  0.0275  109 LEU   B CD2 
5884 N  N   . LYS   B 110 ? 0.1619 0.1431 0.2342 -0.0051 0.0377  0.0192  110 LYS   B N   
5885 C  CA  . LYS   B 110 ? 0.1556 0.1377 0.2237 0.0012  0.0346  0.0193  110 LYS   B CA  
5886 C  C   . LYS   B 110 ? 0.1523 0.1459 0.2094 -0.0059 0.0316  0.0109  110 LYS   B C   
5887 O  O   . LYS   B 110 ? 0.1451 0.1455 0.2058 -0.0065 0.0200  0.0056  110 LYS   B O   
5888 C  CB  . LYS   B 110 ? 0.1586 0.1407 0.2460 -0.0016 0.0399  0.0179  110 LYS   B CB  
5889 C  CG  . LYS   B 110 ? 0.1585 0.1440 0.2446 -0.0055 0.0122  0.0195  110 LYS   B CG  
5890 C  CD  . LYS   B 110 ? 0.1602 0.1461 0.2742 -0.0085 0.0233  0.0202  110 LYS   B CD  
5891 C  CE  . LYS   B 110 ? 0.1545 0.1604 0.2892 0.0011  0.0249  0.0101  110 LYS   B CE  
5892 N  NZ  . LYS   B 110 ? 0.1557 0.1760 0.2938 0.0040  0.0028  0.0047  110 LYS   B NZ  
5906 N  N   . SER   B 111 ? 0.1600 0.1453 0.2236 -0.0060 0.0248  0.0186  111 SER   B N   
5907 C  CA  . SER   B 111 ? 0.1650 0.1484 0.2122 -0.0016 0.0313  0.0149  111 SER   B CA  
5908 C  C   . SER   B 111 ? 0.1599 0.1371 0.2066 0.0010  0.0183  0.0163  111 SER   B C   
5909 O  O   . SER   B 111 ? 0.1487 0.1432 0.2075 0.0055  0.0134  0.0153  111 SER   B O   
5910 C  CB  . SER   B 111 ? 0.1788 0.1716 0.2217 0.0033  0.0491  0.0271  111 SER   B CB  
5911 O  OG  . SER   B 111 ? 0.1982 0.2058 0.2341 0.0080  0.0502  0.0290  111 SER   B OG  
5917 N  N   . ALA   B 112 ? 0.1504 0.1389 0.2117 0.0048  0.0225  0.0245  112 ALA   B N   
5918 C  CA  . ALA   B 112 ? 0.1484 0.1543 0.1819 -0.0001 0.0086  0.0097  112 ALA   B CA  
5919 C  C   . ALA   B 112 ? 0.1354 0.1512 0.1824 0.0021  0.0042  0.0090  112 ALA   B C   
5920 O  O   . ALA   B 112 ? 0.1372 0.1492 0.1924 -0.0005 0.0082  -0.0006 112 ALA   B O   
5921 C  CB  . ALA   B 112 ? 0.1537 0.1557 0.2094 0.0085  0.0081  0.0191  112 ALA   B CB  
5927 N  N   . TYR   B 113 ? 0.1329 0.1361 0.1983 -0.0005 0.0122  0.0066  113 TYR   B N   
5928 C  CA  . TYR   B 113 ? 0.1318 0.1283 0.1898 -0.0025 0.0108  0.0063  113 TYR   B CA  
5929 C  C   . TYR   B 113 ? 0.1332 0.1266 0.1877 -0.0136 0.0065  0.0107  113 TYR   B C   
5930 O  O   . TYR   B 113 ? 0.1405 0.1326 0.1745 -0.0098 0.0045  -0.0016 113 TYR   B O   
5931 C  CB  . TYR   B 113 ? 0.1365 0.1247 0.2058 -0.0009 0.0200  0.0166  113 TYR   B CB  
5932 C  CG  . TYR   B 113 ? 0.1446 0.1305 0.2125 -0.0075 0.0137  0.0189  113 TYR   B CG  
5933 C  CD1 . TYR   B 113 ? 0.1525 0.1352 0.2200 -0.0069 0.0121  0.0228  113 TYR   B CD1 
5934 C  CD2 . TYR   B 113 ? 0.1568 0.1325 0.2075 -0.0047 0.0104  0.0193  113 TYR   B CD2 
5935 C  CE1 . TYR   B 113 ? 0.1529 0.1367 0.2119 0.0012  0.0188  0.0070  113 TYR   B CE1 
5936 C  CE2 . TYR   B 113 ? 0.1638 0.1234 0.2221 0.0033  0.0141  0.0241  113 TYR   B CE2 
5937 C  CZ  . TYR   B 113 ? 0.1487 0.1257 0.2178 0.0120  0.0097  0.0158  113 TYR   B CZ  
5938 O  OH  . TYR   B 113 ? 0.1525 0.1237 0.2490 0.0082  0.0160  0.0124  113 TYR   B OH  
5948 N  N   . GLU   B 114 ? 0.1321 0.1195 0.2024 0.0013  0.0075  0.0086  114 GLU   B N   
5949 C  CA  . GLU   B 114 ? 0.1362 0.1248 0.1939 0.0003  0.0065  0.0030  114 GLU   B CA  
5950 C  C   . GLU   B 114 ? 0.1357 0.1284 0.1881 -0.0053 0.0026  0.0042  114 GLU   B C   
5951 O  O   . GLU   B 114 ? 0.1312 0.1246 0.1979 -0.0013 -0.0051 0.0108  114 GLU   B O   
5952 C  CB  . GLU   B 114 ? 0.1367 0.1343 0.2119 -0.0049 0.0167  0.0056  114 GLU   B CB  
5953 C  CG  . GLU   B 114 ? 0.1386 0.1319 0.2001 -0.0048 0.0098  0.0063  114 GLU   B CG  
5954 C  CD  . GLU   B 114 ? 0.1424 0.1367 0.2000 -0.0077 0.0077  0.0050  114 GLU   B CD  
5955 O  OE1 . GLU   B 114 ? 0.1372 0.1468 0.2051 -0.0106 0.0167  0.0064  114 GLU   B OE1 
5956 O  OE2 . GLU   B 114 ? 0.1412 0.1557 0.2131 -0.0191 0.0100  0.0028  114 GLU   B OE2 
5963 N  N   . ASN   B 115 ? 0.1375 0.1151 0.1852 -0.0074 -0.0019 0.0090  115 ASN   B N   
5964 C  CA  . ASN   B 115 ? 0.1355 0.1268 0.1762 -0.0066 -0.0039 0.0057  115 ASN   B CA  
5965 C  C   . ASN   B 115 ? 0.1350 0.1266 0.1660 -0.0078 -0.0018 0.0021  115 ASN   B C   
5966 O  O   . ASN   B 115 ? 0.1440 0.1317 0.1771 -0.0081 0.0068  0.0056  115 ASN   B O   
5967 C  CB  . ASN   B 115 ? 0.1454 0.1427 0.1706 -0.0069 0.0005  0.0078  115 ASN   B CB  
5968 C  CG  . ASN   B 115 ? 0.1586 0.1523 0.1641 0.0084  -0.0021 -0.0031 115 ASN   B CG  
5969 O  OD1 . ASN   B 115 ? 0.2021 0.1592 0.1852 0.0072  0.0165  -0.0145 115 ASN   B OD1 
5970 N  ND2 . ASN   B 115 ? 0.1585 0.1662 0.1570 -0.0014 0.0053  0.0052  115 ASN   B ND2 
5977 N  N   . PHE   B 116 ? 0.1364 0.1320 0.1549 0.0004  -0.0072 -0.0021 116 PHE   B N   
5978 C  CA  . PHE   B 116 ? 0.1458 0.1305 0.1651 -0.0108 -0.0115 -0.0019 116 PHE   B CA  
5979 C  C   . PHE   B 116 ? 0.1423 0.1154 0.1830 -0.0172 -0.0008 0.0083  116 PHE   B C   
5980 O  O   . PHE   B 116 ? 0.1412 0.1278 0.1801 -0.0090 -0.0043 0.0039  116 PHE   B O   
5981 C  CB  . PHE   B 116 ? 0.1364 0.1249 0.1625 -0.0043 -0.0082 0.0020  116 PHE   B CB  
5982 C  CG  . PHE   B 116 ? 0.1293 0.1250 0.1657 -0.0045 0.0033  -0.0016 116 PHE   B CG  
5983 C  CD1 . PHE   B 116 ? 0.1398 0.1317 0.1896 -0.0036 0.0037  0.0048  116 PHE   B CD1 
5984 C  CD2 . PHE   B 116 ? 0.1362 0.1404 0.1681 -0.0039 0.0007  -0.0007 116 PHE   B CD2 
5985 C  CE1 . PHE   B 116 ? 0.1351 0.1330 0.1795 -0.0020 -0.0144 0.0032  116 PHE   B CE1 
5986 C  CE2 . PHE   B 116 ? 0.1350 0.1349 0.1825 -0.0061 -0.0058 0.0124  116 PHE   B CE2 
5987 C  CZ  . PHE   B 116 ? 0.1318 0.1390 0.1880 0.0025  -0.0090 0.0044  116 PHE   B CZ  
5997 N  N   . ASN   B 117 ? 0.1409 0.1218 0.1887 -0.0066 -0.0064 0.0052  117 ASN   B N   
5998 C  CA  . ASN   B 117 ? 0.1467 0.1272 0.1916 0.0028  -0.0109 -0.0030 117 ASN   B CA  
5999 C  C   . ASN   B 117 ? 0.1453 0.1244 0.2054 0.0032  -0.0072 0.0051  117 ASN   B C   
6000 O  O   . ASN   B 117 ? 0.1527 0.1313 0.2344 -0.0041 -0.0278 0.0066  117 ASN   B O   
6001 C  CB  . ASN   B 117 ? 0.1439 0.1325 0.1997 -0.0016 -0.0141 -0.0050 117 ASN   B CB  
6002 C  CG  . ASN   B 117 ? 0.1372 0.1309 0.2049 0.0008  -0.0071 -0.0064 117 ASN   B CG  
6003 O  OD1 . ASN   B 117 ? 0.1624 0.1378 0.2070 -0.0097 -0.0008 -0.0079 117 ASN   B OD1 
6004 N  ND2 . ASN   B 117 ? 0.1366 0.1357 0.1976 -0.0041 -0.0050 0.0024  117 ASN   B ND2 
6011 N  N   . GLN   B 118 ? 0.1463 0.1274 0.1838 -0.0096 -0.0175 -0.0002 118 GLN   B N   
6012 C  CA  . GLN   B 118 ? 0.1544 0.1228 0.2028 -0.0023 -0.0139 0.0039  118 GLN   B CA  
6013 C  C   . GLN   B 118 ? 0.1503 0.1231 0.2132 -0.0009 -0.0126 -0.0009 118 GLN   B C   
6014 O  O   . GLN   B 118 ? 0.1638 0.1294 0.2418 -0.0078 -0.0011 0.0049  118 GLN   B O   
6015 C  CB  . GLN   B 118 ? 0.1596 0.1340 0.2112 0.0015  -0.0122 0.0024  118 GLN   B CB  
6016 C  CG  . GLN   B 118 ? 0.1655 0.1231 0.2070 0.0007  -0.0095 -0.0055 118 GLN   B CG  
6017 C  CD  . GLN   B 118 ? 0.1724 0.1249 0.2073 0.0011  -0.0098 -0.0110 118 GLN   B CD  
6018 O  OE1 . GLN   B 118 ? 0.1747 0.1294 0.2219 0.0087  0.0063  0.0026  118 GLN   B OE1 
6019 N  NE2 . GLN   B 118 ? 0.1749 0.1345 0.2038 0.0005  -0.0103 -0.0001 118 GLN   B NE2 
6028 N  N   . HIS   B 119 ? 0.1552 0.1357 0.1742 -0.0010 -0.0183 0.0086  119 HIS   B N   
6029 C  CA  . HIS   B 119 ? 0.1641 0.1448 0.1578 -0.0007 -0.0224 0.0139  119 HIS   B CA  
6030 C  C   . HIS   B 119 ? 0.1679 0.1448 0.1558 -0.0040 -0.0348 0.0101  119 HIS   B C   
6031 O  O   . HIS   B 119 ? 0.1734 0.1394 0.1801 -0.0249 -0.0213 0.0089  119 HIS   B O   
6032 C  CB  . HIS   B 119 ? 0.1733 0.1564 0.1729 -0.0042 -0.0208 0.0071  119 HIS   B CB  
6033 C  CG  . HIS   B 119 ? 0.1749 0.1793 0.1928 0.0059  -0.0428 -0.0139 119 HIS   B CG  
6034 N  ND1 . HIS   B 119 ? 0.1830 0.1885 0.2229 0.0031  -0.0501 -0.0321 119 HIS   B ND1 
6035 C  CD2 . HIS   B 119 ? 0.1832 0.1932 0.2054 0.0330  -0.0503 -0.0164 119 HIS   B CD2 
6036 C  CE1 . HIS   B 119 ? 0.2028 0.2058 0.2326 0.0163  -0.0550 -0.0402 119 HIS   B CE1 
6037 N  NE2 . HIS   B 119 ? 0.1989 0.2163 0.2192 0.0291  -0.0499 -0.0417 119 HIS   B NE2 
6045 N  N   . GLU   B 120 ? 0.1850 0.1498 0.1553 -0.0094 -0.0392 0.0139  120 GLU   B N   
6046 C  CA  . GLU   B 120 ? 0.2116 0.1655 0.1729 0.0002  -0.0475 0.0293  120 GLU   B CA  
6047 C  C   . GLU   B 120 ? 0.1891 0.1574 0.1596 -0.0140 -0.0335 0.0222  120 GLU   B C   
6048 O  O   . GLU   B 120 ? 0.1801 0.1642 0.1736 -0.0115 -0.0330 0.0094  120 GLU   B O   
6049 C  CB  . GLU   B 120 ? 0.2687 0.1824 0.2444 0.0238  -0.0714 0.0384  120 GLU   B CB  
6050 C  CG  . GLU   B 120 ? 0.3157 0.2307 0.3469 0.0338  -0.0947 0.0494  120 GLU   B CG  
6051 C  CD  . GLU   B 120 ? 0.3585 0.3208 0.4515 0.0315  -0.0989 0.0621  120 GLU   B CD  
6052 O  OE1 . GLU   B 120 ? 0.4106 0.3449 0.4941 0.0200  -0.0831 0.0704  120 GLU   B OE1 
6053 O  OE2 . GLU   B 120 ? 0.3912 0.3739 0.5107 0.0338  -0.0981 0.0574  120 GLU   B OE2 
6060 N  N   . VAL   B 121 ? 0.1801 0.1502 0.1587 -0.0217 -0.0128 0.0151  121 VAL   B N   
6061 C  CA  . VAL   B 121 ? 0.1719 0.1590 0.1452 -0.0253 -0.0183 0.0136  121 VAL   B CA  
6062 C  C   . VAL   B 121 ? 0.1647 0.1574 0.1461 -0.0267 -0.0201 0.0149  121 VAL   B C   
6063 O  O   . VAL   B 121 ? 0.1746 0.1484 0.1622 -0.0329 -0.0251 -0.0001 121 VAL   B O   
6064 C  CB  . VAL   B 121 ? 0.1915 0.2005 0.1684 -0.0045 -0.0260 0.0247  121 VAL   B CB  
6065 C  CG1 . VAL   B 121 ? 0.1924 0.2151 0.2064 -0.0167 -0.0118 0.0343  121 VAL   B CG1 
6066 C  CG2 . VAL   B 121 ? 0.2152 0.2201 0.1791 0.0005  -0.0313 0.0104  121 VAL   B CG2 
6076 N  N   . LEU   B 122 ? 0.1567 0.1473 0.1484 -0.0134 -0.0215 0.0146  122 LEU   B N   
6077 C  CA  . LEU   B 122 ? 0.1487 0.1518 0.1480 -0.0146 -0.0215 0.0068  122 LEU   B CA  
6078 C  C   . LEU   B 122 ? 0.1494 0.1424 0.1436 -0.0241 -0.0195 0.0076  122 LEU   B C   
6079 O  O   . LEU   B 122 ? 0.1542 0.1455 0.1734 -0.0296 -0.0187 -0.0011 122 LEU   B O   
6080 C  CB  . LEU   B 122 ? 0.1721 0.1634 0.1759 -0.0018 -0.0248 0.0102  122 LEU   B CB  
6081 C  CG  . LEU   B 122 ? 0.1620 0.1703 0.1733 -0.0127 -0.0076 0.0012  122 LEU   B CG  
6082 C  CD1 . LEU   B 122 ? 0.1612 0.1931 0.1935 -0.0235 -0.0205 0.0029  122 LEU   B CD1 
6083 C  CD2 . LEU   B 122 ? 0.1699 0.1619 0.1571 -0.0021 -0.0042 -0.0138 122 LEU   B CD2 
6095 N  N   . LEU   B 123 ? 0.1521 0.1309 0.1385 -0.0233 -0.0190 0.0072  123 LEU   B N   
6096 C  CA  . LEU   B 123 ? 0.1599 0.1358 0.1464 -0.0260 -0.0216 -0.0014 123 LEU   B CA  
6097 C  C   . LEU   B 123 ? 0.1513 0.1348 0.1298 -0.0246 -0.0245 -0.0017 123 LEU   B C   
6098 O  O   . LEU   B 123 ? 0.1648 0.1381 0.1335 -0.0299 -0.0208 0.0028  123 LEU   B O   
6099 C  CB  . LEU   B 123 ? 0.1602 0.1355 0.1599 -0.0232 -0.0109 0.0016  123 LEU   B CB  
6100 C  CG  . LEU   B 123 ? 0.1524 0.1379 0.1678 -0.0206 -0.0076 0.0059  123 LEU   B CG  
6101 C  CD1 . LEU   B 123 ? 0.1645 0.1419 0.1782 -0.0150 0.0033  -0.0053 123 LEU   B CD1 
6102 C  CD2 . LEU   B 123 ? 0.1654 0.1508 0.1935 -0.0176 -0.0044 0.0177  123 LEU   B CD2 
6114 N  N   . ALA   B 124 ? 0.1494 0.1334 0.1326 -0.0213 -0.0119 -0.0023 124 ALA   B N   
6115 C  CA  . ALA   B 124 ? 0.1386 0.1343 0.1439 -0.0124 -0.0146 -0.0097 124 ALA   B CA  
6116 C  C   . ALA   B 124 ? 0.1384 0.1347 0.1399 -0.0146 -0.0092 -0.0063 124 ALA   B C   
6117 O  O   . ALA   B 124 ? 0.1511 0.1328 0.1534 -0.0115 -0.0087 -0.0011 124 ALA   B O   
6118 C  CB  . ALA   B 124 ? 0.1429 0.1386 0.1556 -0.0036 0.0003  0.0047  124 ALA   B CB  
6124 N  N   . PRO   B 125 ? 0.1455 0.1319 0.1375 -0.0134 -0.0171 0.0100  125 PRO   B N   
6125 C  CA  . PRO   B 125 ? 0.1625 0.1278 0.1498 -0.0164 -0.0111 0.0170  125 PRO   B CA  
6126 C  C   . PRO   B 125 ? 0.1550 0.1257 0.1656 -0.0166 -0.0081 0.0130  125 PRO   B C   
6127 O  O   . PRO   B 125 ? 0.1531 0.1272 0.1843 -0.0164 -0.0064 0.0181  125 PRO   B O   
6128 C  CB  . PRO   B 125 ? 0.1568 0.1542 0.1727 -0.0192 -0.0236 0.0319  125 PRO   B CB  
6129 C  CG  . PRO   B 125 ? 0.1624 0.1609 0.1681 -0.0309 -0.0208 0.0148  125 PRO   B CG  
6130 C  CD  . PRO   B 125 ? 0.1562 0.1463 0.1448 -0.0288 -0.0147 0.0124  125 PRO   B CD  
6138 N  N   . LEU   B 126 ? 0.1543 0.1252 0.2047 -0.0132 0.0142  0.0135  126 LEU   B N   
6139 C  CA  . LEU   B 126 ? 0.1641 0.1331 0.2109 -0.0139 0.0207  0.0195  126 LEU   B CA  
6140 C  C   . LEU   B 126 ? 0.1594 0.1403 0.1976 -0.0035 0.0211  0.0271  126 LEU   B C   
6141 O  O   . LEU   B 126 ? 0.1780 0.1709 0.2264 0.0186  -0.0107 0.0026  126 LEU   B O   
6142 C  CB  . LEU   B 126 ? 0.1828 0.1469 0.2365 -0.0180 0.0331  0.0101  126 LEU   B CB  
6143 C  CG  . LEU   B 126 ? 0.2039 0.1533 0.2373 -0.0245 0.0324  -0.0149 126 LEU   B CG  
6144 C  CD1 . LEU   B 126 ? 0.2148 0.1711 0.2931 -0.0257 0.0275  -0.0132 126 LEU   B CD1 
6145 C  CD2 . LEU   B 126 ? 0.2028 0.1664 0.2564 -0.0256 0.0239  -0.0223 126 LEU   B CD2 
6157 N  N   . LEU   B 127 ? 0.1558 0.1323 0.1987 0.0024  0.0230  0.0174  127 LEU   B N   
6158 C  CA  . LEU   B 127 ? 0.1523 0.1432 0.2037 -0.0015 0.0256  0.0285  127 LEU   B CA  
6159 C  C   . LEU   B 127 ? 0.1449 0.1433 0.2205 0.0032  0.0177  0.0227  127 LEU   B C   
6160 O  O   . LEU   B 127 ? 0.1486 0.1451 0.2290 -0.0125 0.0115  0.0185  127 LEU   B O   
6161 C  CB  . LEU   B 127 ? 0.1599 0.1421 0.2399 0.0004  0.0185  0.0263  127 LEU   B CB  
6162 C  CG  . LEU   B 127 ? 0.1757 0.1395 0.2400 0.0016  0.0260  0.0228  127 LEU   B CG  
6163 C  CD1 . LEU   B 127 ? 0.1782 0.1380 0.2244 0.0078  0.0205  0.0086  127 LEU   B CD1 
6164 C  CD2 . LEU   B 127 ? 0.1787 0.1572 0.2527 -0.0051 0.0127  0.0289  127 LEU   B CD2 
6176 N  N   . SER   B 128 ? 0.1516 0.1466 0.2212 0.0040  0.0024  0.0222  128 SER   B N   
6177 C  CA  . SER   B 128 ? 0.1711 0.1504 0.2166 0.0150  -0.0087 0.0239  128 SER   B CA  
6178 C  C   . SER   B 128 ? 0.1827 0.1557 0.2304 0.0099  -0.0278 0.0256  128 SER   B C   
6179 O  O   . SER   B 128 ? 0.1969 0.1590 0.2639 0.0062  -0.0209 0.0359  128 SER   B O   
6180 C  CB  . SER   B 128 ? 0.1820 0.1508 0.2039 0.0084  0.0040  0.0333  128 SER   B CB  
6181 O  OG  . SER   B 128 ? 0.1827 0.1682 0.2098 0.0133  0.0119  0.0369  128 SER   B OG  
6187 N  N   . ALA   B 129 ? 0.1947 0.1589 0.2550 0.0256  -0.0176 0.0063  129 ALA   B N   
6188 C  CA  . ALA   B 129 ? 0.2075 0.1634 0.2697 0.0308  -0.0202 -0.0030 129 ALA   B CA  
6189 C  C   . ALA   B 129 ? 0.1956 0.1597 0.2550 0.0184  0.0044  0.0090  129 ALA   B C   
6190 O  O   . ALA   B 129 ? 0.1842 0.1599 0.2543 0.0141  -0.0027 0.0172  129 ALA   B O   
6191 C  CB  . ALA   B 129 ? 0.2313 0.1865 0.2926 0.0259  -0.0099 -0.0120 129 ALA   B CB  
6197 N  N   . GLY   B 130 ? 0.1915 0.1594 0.2578 0.0336  0.0153  0.0068  130 GLY   B N   
6198 C  CA  . GLY   B 130 ? 0.2022 0.1703 0.2751 0.0237  0.0387  -0.0014 130 GLY   B CA  
6199 C  C   . GLY   B 130 ? 0.2071 0.1693 0.2631 0.0149  0.0235  0.0097  130 GLY   B C   
6200 O  O   . GLY   B 130 ? 0.2165 0.1812 0.2697 0.0163  0.0133  0.0163  130 GLY   B O   
6204 N  N   . ILE   B 131 ? 0.2006 0.1815 0.2761 0.0296  0.0127  0.0060  131 ILE   B N   
6205 C  CA  . ILE   B 131 ? 0.2159 0.1923 0.2760 0.0236  -0.0059 0.0201  131 ILE   B CA  
6206 C  C   . ILE   B 131 ? 0.2241 0.1895 0.2381 0.0152  0.0008  0.0256  131 ILE   B C   
6207 O  O   . ILE   B 131 ? 0.2494 0.2061 0.2441 0.0228  -0.0171 0.0326  131 ILE   B O   
6208 C  CB  . ILE   B 131 ? 0.2161 0.2202 0.3221 0.0236  -0.0131 0.0214  131 ILE   B CB  
6209 C  CG1 . ILE   B 131 ? 0.2276 0.2294 0.3316 -0.0030 -0.0012 0.0211  131 ILE   B CG1 
6210 C  CG2 . ILE   B 131 ? 0.2130 0.2390 0.3474 0.0314  -0.0096 0.0114  131 ILE   B CG2 
6211 C  CD1 . ILE   B 131 ? 0.2371 0.2420 0.3432 -0.0195 -0.0072 0.0254  131 ILE   B CD1 
6223 N  N   . PHE   B 132 ? 0.2053 0.1732 0.2327 0.0114  0.0182  0.0229  132 PHE   B N   
6224 C  CA  . PHE   B 132 ? 0.2172 0.1773 0.2291 0.0078  0.0398  0.0207  132 PHE   B CA  
6225 C  C   . PHE   B 132 ? 0.2399 0.1871 0.2411 0.0124  0.0525  0.0207  132 PHE   B C   
6226 O  O   . PHE   B 132 ? 0.2614 0.2072 0.2725 0.0092  0.0672  0.0320  132 PHE   B O   
6227 C  CB  . PHE   B 132 ? 0.1949 0.1755 0.2086 0.0145  0.0444  0.0296  132 PHE   B CB  
6228 C  CG  . PHE   B 132 ? 0.1997 0.1792 0.2075 0.0145  0.0413  0.0247  132 PHE   B CG  
6229 C  CD1 . PHE   B 132 ? 0.2057 0.1790 0.2359 0.0085  0.0367  0.0225  132 PHE   B CD1 
6230 C  CD2 . PHE   B 132 ? 0.2007 0.1846 0.1755 0.0262  0.0314  0.0381  132 PHE   B CD2 
6231 C  CE1 . PHE   B 132 ? 0.2073 0.1808 0.2478 0.0056  0.0292  0.0301  132 PHE   B CE1 
6232 C  CE2 . PHE   B 132 ? 0.2115 0.1891 0.1864 0.0214  0.0206  0.0318  132 PHE   B CE2 
6233 C  CZ  . PHE   B 132 ? 0.2107 0.1846 0.2395 0.0087  0.0005  0.0408  132 PHE   B CZ  
6243 N  N   . GLY   B 133 ? 0.2385 0.1777 0.2406 0.0068  0.0250  0.0404  133 GLY   B N   
6244 C  CA  . GLY   B 133 ? 0.2355 0.1884 0.2613 -0.0135 0.0135  0.0423  133 GLY   B CA  
6245 C  C   . GLY   B 133 ? 0.2372 0.1914 0.2620 -0.0261 0.0209  0.0506  133 GLY   B C   
6246 O  O   . GLY   B 133 ? 0.2553 0.2013 0.3019 -0.0383 0.0257  0.0626  133 GLY   B O   
6250 N  N   . ALA   B 134 ? 0.2254 0.1906 0.2451 -0.0257 0.0248  0.0370  134 ALA   B N   
6251 C  CA  . ALA   B 134 ? 0.2236 0.1941 0.2636 -0.0157 0.0382  0.0219  134 ALA   B CA  
6252 C  C   . ALA   B 134 ? 0.2274 0.1905 0.2621 -0.0133 0.0386  0.0453  134 ALA   B C   
6253 O  O   . ALA   B 134 ? 0.2289 0.2091 0.2897 0.0011  0.0302  0.0341  134 ALA   B O   
6254 C  CB  . ALA   B 134 ? 0.2236 0.1905 0.2883 -0.0134 0.0337  0.0090  134 ALA   B CB  
6260 N  N   . ASP   B 135 ? 0.2419 0.1823 0.2645 -0.0137 0.0236  0.0481  135 ASP   B N   
6261 C  CA  . ASP   B 135 ? 0.2632 0.1692 0.2919 -0.0122 0.0019  0.0491  135 ASP   B CA  
6262 C  C   . ASP   B 135 ? 0.2455 0.1587 0.2677 -0.0034 -0.0033 0.0307  135 ASP   B C   
6263 O  O   . ASP   B 135 ? 0.2405 0.1560 0.2694 -0.0046 0.0050  0.0328  135 ASP   B O   
6264 C  CB  . ASP   B 135 ? 0.2924 0.1806 0.3167 -0.0283 -0.0018 0.0580  135 ASP   B CB  
6265 C  CG  . ASP   B 135 ? 0.3203 0.1814 0.3484 -0.0532 0.0014  0.0442  135 ASP   B CG  
6266 O  OD1 . ASP   B 135 ? 0.3313 0.1671 0.3464 -0.0360 -0.0207 0.0328  135 ASP   B OD1 
6267 O  OD2 . ASP   B 135 ? 0.3421 0.2218 0.4085 -0.0685 0.0174  0.0214  135 ASP   B OD2 
6272 N  N   . PRO   B 136 ? 0.2270 0.1685 0.2809 0.0162  -0.0189 0.0222  136 PRO   B N   
6273 C  CA  . PRO   B 136 ? 0.2084 0.1594 0.2879 0.0151  -0.0193 0.0119  136 PRO   B CA  
6274 C  C   . PRO   B 136 ? 0.1935 0.1444 0.2823 0.0125  -0.0104 0.0102  136 PRO   B C   
6275 O  O   . PRO   B 136 ? 0.1761 0.1403 0.2834 0.0093  0.0036  0.0095  136 PRO   B O   
6276 C  CB  . PRO   B 136 ? 0.2106 0.1759 0.2972 0.0277  -0.0289 0.0023  136 PRO   B CB  
6277 C  CG  . PRO   B 136 ? 0.2279 0.1891 0.3127 0.0316  -0.0154 0.0000  136 PRO   B CG  
6278 C  CD  . PRO   B 136 ? 0.2303 0.1778 0.3046 0.0369  -0.0081 0.0062  136 PRO   B CD  
6286 N  N   . ILE   B 137 ? 0.2045 0.1349 0.2934 0.0105  -0.0087 0.0004  137 ILE   B N   
6287 C  CA  . ILE   B 137 ? 0.2061 0.1253 0.3078 -0.0080 -0.0054 0.0083  137 ILE   B CA  
6288 C  C   . ILE   B 137 ? 0.1957 0.1394 0.2923 -0.0147 0.0043  0.0226  137 ILE   B C   
6289 O  O   . ILE   B 137 ? 0.1877 0.1461 0.2893 -0.0124 0.0059  0.0111  137 ILE   B O   
6290 C  CB  . ILE   B 137 ? 0.2347 0.1443 0.3523 -0.0092 -0.0013 0.0162  137 ILE   B CB  
6291 C  CG1 . ILE   B 137 ? 0.2607 0.1653 0.3974 0.0017  0.0118  0.0127  137 ILE   B CG1 
6292 C  CG2 . ILE   B 137 ? 0.2400 0.1471 0.3661 -0.0335 -0.0019 0.0193  137 ILE   B CG2 
6293 C  CD1 . ILE   B 137 ? 0.2843 0.1926 0.4282 0.0144  0.0044  0.0192  137 ILE   B CD1 
6305 N  N   . HIS   B 138 ? 0.2004 0.1390 0.2937 -0.0066 0.0139  0.0263  138 HIS   B N   
6306 C  CA  . HIS   B 138 ? 0.2112 0.1482 0.2881 -0.0022 0.0273  0.0253  138 HIS   B CA  
6307 C  C   . HIS   B 138 ? 0.1967 0.1411 0.2743 -0.0101 0.0231  0.0289  138 HIS   B C   
6308 O  O   . HIS   B 138 ? 0.1842 0.1500 0.2851 -0.0017 0.0309  0.0357  138 HIS   B O   
6309 C  CB  . HIS   B 138 ? 0.2415 0.1644 0.2980 -0.0071 0.0519  0.0218  138 HIS   B CB  
6310 C  CG  . HIS   B 138 ? 0.2607 0.1786 0.3122 -0.0029 0.0752  0.0388  138 HIS   B CG  
6311 N  ND1 . HIS   B 138 ? 0.2670 0.1950 0.3471 -0.0066 0.0793  0.0306  138 HIS   B ND1 
6312 C  CD2 . HIS   B 138 ? 0.2756 0.1899 0.3009 -0.0034 0.0759  0.0323  138 HIS   B CD2 
6313 C  CE1 . HIS   B 138 ? 0.2680 0.1968 0.3376 -0.0038 0.0779  0.0313  138 HIS   B CE1 
6314 N  NE2 . HIS   B 138 ? 0.2783 0.1908 0.3177 0.0029  0.0806  0.0263  138 HIS   B NE2 
6322 N  N   . SER   B 139 ? 0.1932 0.1271 0.2655 -0.0028 0.0219  0.0171  139 SER   B N   
6323 C  CA  . SER   B 139 ? 0.1872 0.1356 0.2390 0.0018  0.0262  0.0069  139 SER   B CA  
6324 C  C   . SER   B 139 ? 0.1638 0.1242 0.2505 0.0022  0.0210  0.0148  139 SER   B C   
6325 O  O   . SER   B 139 ? 0.1593 0.1268 0.2570 0.0021  0.0083  0.0140  139 SER   B O   
6326 C  CB  . SER   B 139 ? 0.1920 0.1371 0.2544 0.0010  0.0081  0.0012  139 SER   B CB  
6327 O  OG  . SER   B 139 ? 0.1902 0.1328 0.2645 0.0017  -0.0127 0.0226  139 SER   B OG  
6333 N  N   . LEU   B 140 ? 0.1621 0.1154 0.2424 -0.0060 0.0218  0.0018  140 LEU   B N   
6334 C  CA  . LEU   B 140 ? 0.1574 0.1262 0.2390 -0.0033 0.0116  0.0091  140 LEU   B CA  
6335 C  C   . LEU   B 140 ? 0.1484 0.1253 0.2590 -0.0020 0.0006  -0.0026 140 LEU   B C   
6336 O  O   . LEU   B 140 ? 0.1474 0.1377 0.2594 -0.0023 -0.0021 0.0095  140 LEU   B O   
6337 C  CB  . LEU   B 140 ? 0.1557 0.1301 0.2514 -0.0087 0.0157  -0.0016 140 LEU   B CB  
6338 C  CG  . LEU   B 140 ? 0.1642 0.1329 0.2512 -0.0070 0.0048  0.0088  140 LEU   B CG  
6339 C  CD1 . LEU   B 140 ? 0.1697 0.1442 0.2619 -0.0078 0.0081  0.0086  140 LEU   B CD1 
6340 C  CD2 . LEU   B 140 ? 0.1832 0.1446 0.2660 -0.0092 0.0048  -0.0095 140 LEU   B CD2 
6352 N  N   . ARG   B 141 ? 0.1450 0.1342 0.2601 -0.0062 0.0093  0.0066  141 ARG   B N   
6353 C  CA  . ARG   B 141 ? 0.1545 0.1299 0.3043 -0.0159 0.0213  -0.0027 141 ARG   B CA  
6354 C  C   . ARG   B 141 ? 0.1488 0.1267 0.2942 -0.0155 0.0115  -0.0010 141 ARG   B C   
6355 O  O   . ARG   B 141 ? 0.1524 0.1360 0.2906 -0.0130 -0.0003 -0.0094 141 ARG   B O   
6356 C  CB  . ARG   B 141 ? 0.1696 0.1453 0.3281 -0.0257 0.0408  0.0090  141 ARG   B CB  
6357 C  CG  . ARG   B 141 ? 0.2009 0.1698 0.3441 -0.0250 0.0367  0.0025  141 ARG   B CG  
6358 C  CD  . ARG   B 141 ? 0.2340 0.1904 0.3461 -0.0147 0.0157  -0.0126 141 ARG   B CD  
6359 N  NE  . ARG   B 141 ? 0.2549 0.1957 0.3352 -0.0282 0.0110  -0.0248 141 ARG   B NE  
6360 C  CZ  . ARG   B 141 ? 0.2727 0.1923 0.3223 -0.0237 0.0204  -0.0328 141 ARG   B CZ  
6361 N  NH1 . ARG   B 141 ? 0.2877 0.1720 0.3047 -0.0189 0.0173  -0.0308 141 ARG   B NH1 
6362 N  NH2 . ARG   B 141 ? 0.2760 0.2020 0.3239 -0.0191 0.0151  -0.0337 141 ARG   B NH2 
6376 N  N   . VAL   B 142 ? 0.1526 0.1226 0.2833 -0.0099 0.0143  -0.0038 142 VAL   B N   
6377 C  CA  . VAL   B 142 ? 0.1464 0.1257 0.2785 -0.0081 0.0226  -0.0020 142 VAL   B CA  
6378 C  C   . VAL   B 142 ? 0.1462 0.1262 0.2720 -0.0070 0.0155  -0.0088 142 VAL   B C   
6379 O  O   . VAL   B 142 ? 0.1541 0.1250 0.2796 -0.0062 0.0087  0.0009  142 VAL   B O   
6380 C  CB  . VAL   B 142 ? 0.1611 0.1430 0.2805 0.0061  0.0231  0.0197  142 VAL   B CB  
6381 C  CG1 . VAL   B 142 ? 0.1607 0.1358 0.2905 0.0100  0.0309  0.0154  142 VAL   B CG1 
6382 C  CG2 . VAL   B 142 ? 0.1795 0.1465 0.2851 0.0087  0.0141  0.0255  142 VAL   B CG2 
6392 N  N   . CYS   B 143 ? 0.1441 0.1311 0.2500 -0.0020 0.0106  0.0114  143 CYS   B N   
6393 C  CA  . CYS   B 143 ? 0.1390 0.1302 0.2499 -0.0087 0.0015  0.0037  143 CYS   B CA  
6394 C  C   . CYS   B 143 ? 0.1382 0.1369 0.2488 -0.0059 0.0098  -0.0039 143 CYS   B C   
6395 O  O   . CYS   B 143 ? 0.1419 0.1430 0.2396 -0.0070 -0.0054 -0.0115 143 CYS   B O   
6396 C  CB  . CYS   B 143 ? 0.1492 0.1461 0.2455 -0.0025 -0.0055 0.0018  143 CYS   B CB  
6397 S  SG  . CYS   B 143 ? 0.1477 0.1520 0.2497 -0.0046 0.0065  0.0081  143 CYS   B SG  
6403 N  N   . VAL   B 144 ? 0.1462 0.1324 0.2527 -0.0088 0.0043  -0.0205 144 VAL   B N   
6404 C  CA  . VAL   B 144 ? 0.1517 0.1402 0.2706 -0.0156 -0.0075 -0.0290 144 VAL   B CA  
6405 C  C   . VAL   B 144 ? 0.1431 0.1419 0.2901 -0.0102 -0.0092 -0.0026 144 VAL   B C   
6406 O  O   . VAL   B 144 ? 0.1522 0.1581 0.3226 -0.0022 -0.0216 0.0156  144 VAL   B O   
6407 C  CB  . VAL   B 144 ? 0.1730 0.1709 0.3572 -0.0258 -0.0158 -0.0422 144 VAL   B CB  
6408 C  CG1 . VAL   B 144 ? 0.1912 0.2185 0.3801 -0.0217 -0.0249 -0.0336 144 VAL   B CG1 
6409 C  CG2 . VAL   B 144 ? 0.1838 0.1708 0.3295 -0.0142 -0.0230 -0.0573 144 VAL   B CG2 
6419 N  N   . ASP   B 145 ? 0.1464 0.1404 0.2991 -0.0075 -0.0025 -0.0275 145 ASP   B N   
6420 C  CA  . ASP   B 145 ? 0.1494 0.1457 0.3191 -0.0117 0.0039  -0.0073 145 ASP   B CA  
6421 C  C   . ASP   B 145 ? 0.1498 0.1442 0.2974 -0.0082 0.0067  -0.0129 145 ASP   B C   
6422 O  O   . ASP   B 145 ? 0.1499 0.1616 0.3437 -0.0138 0.0099  -0.0236 145 ASP   B O   
6423 C  CB  . ASP   B 145 ? 0.1592 0.1547 0.3600 -0.0183 0.0123  0.0020  145 ASP   B CB  
6424 C  CG  . ASP   B 145 ? 0.1713 0.1552 0.3967 -0.0249 0.0325  -0.0070 145 ASP   B CG  
6425 O  OD1 . ASP   B 145 ? 0.1752 0.1522 0.4102 -0.0208 -0.0024 -0.0143 145 ASP   B OD1 
6426 O  OD2 . ASP   B 145 ? 0.2037 0.1665 0.4469 -0.0289 0.0721  -0.0129 145 ASP   B OD2 
6431 N  N   . THR   B 146 ? 0.1405 0.1386 0.2555 -0.0179 0.0007  0.0004  146 THR   B N   
6432 C  CA  . THR   B 146 ? 0.1419 0.1346 0.2396 -0.0083 0.0029  -0.0013 146 THR   B CA  
6433 C  C   . THR   B 146 ? 0.1402 0.1377 0.2333 -0.0100 0.0010  -0.0029 146 THR   B C   
6434 O  O   . THR   B 146 ? 0.1490 0.1303 0.2373 -0.0017 -0.0006 0.0003  146 THR   B O   
6435 C  CB  . THR   B 146 ? 0.1434 0.1374 0.2497 -0.0017 0.0193  0.0023  146 THR   B CB  
6436 O  OG1 . THR   B 146 ? 0.1566 0.1364 0.2434 -0.0045 0.0179  0.0112  146 THR   B OG1 
6437 C  CG2 . THR   B 146 ? 0.1556 0.1325 0.2563 -0.0018 0.0186  -0.0018 146 THR   B CG2 
6445 N  N   . VAL   B 147 ? 0.1450 0.1429 0.2154 -0.0056 0.0067  0.0014  147 VAL   B N   
6446 C  CA  . VAL   B 147 ? 0.1449 0.1380 0.2126 -0.0086 -0.0052 0.0109  147 VAL   B CA  
6447 C  C   . VAL   B 147 ? 0.1443 0.1374 0.2308 -0.0200 -0.0173 -0.0013 147 VAL   B C   
6448 O  O   . VAL   B 147 ? 0.1562 0.1441 0.2461 -0.0274 -0.0325 -0.0080 147 VAL   B O   
6449 C  CB  . VAL   B 147 ? 0.1538 0.1511 0.2032 -0.0078 -0.0080 0.0072  147 VAL   B CB  
6450 C  CG1 . VAL   B 147 ? 0.1542 0.1582 0.1832 -0.0170 -0.0045 0.0113  147 VAL   B CG1 
6451 C  CG2 . VAL   B 147 ? 0.1576 0.1498 0.2171 -0.0073 0.0020  0.0027  147 VAL   B CG2 
6461 N  N   . ARG   B 148 ? 0.1463 0.1384 0.2077 -0.0101 -0.0212 -0.0117 148 ARG   B N   
6462 C  CA  . ARG   B 148 ? 0.1465 0.1448 0.2238 -0.0040 -0.0255 -0.0113 148 ARG   B CA  
6463 C  C   . ARG   B 148 ? 0.1532 0.1503 0.2093 -0.0084 -0.0311 -0.0015 148 ARG   B C   
6464 O  O   . ARG   B 148 ? 0.1731 0.1777 0.2072 -0.0242 -0.0402 0.0037  148 ARG   B O   
6465 C  CB  . ARG   B 148 ? 0.1493 0.1578 0.2182 -0.0040 -0.0361 -0.0204 148 ARG   B CB  
6466 C  CG  . ARG   B 148 ? 0.1573 0.1764 0.2226 -0.0099 -0.0302 -0.0342 148 ARG   B CG  
6467 C  CD  . ARG   B 148 ? 0.1649 0.1834 0.2396 0.0078  -0.0298 -0.0386 148 ARG   B CD  
6468 N  NE  . ARG   B 148 ? 0.1710 0.1778 0.2400 0.0188  -0.0392 -0.0340 148 ARG   B NE  
6469 C  CZ  . ARG   B 148 ? 0.1540 0.1719 0.2258 0.0146  -0.0355 -0.0237 148 ARG   B CZ  
6470 N  NH1 . ARG   B 148 ? 0.1475 0.1756 0.2319 -0.0040 -0.0072 -0.0186 148 ARG   B NH1 
6471 N  NH2 . ARG   B 148 ? 0.1773 0.1606 0.2031 0.0149  -0.0213 -0.0162 148 ARG   B NH2 
6485 N  N   . THR   B 149 ? 0.1552 0.1417 0.2071 -0.0094 -0.0304 -0.0051 149 THR   B N   
6486 C  CA  . THR   B 149 ? 0.1653 0.1511 0.1968 -0.0091 -0.0310 0.0043  149 THR   B CA  
6487 C  C   . THR   B 149 ? 0.1623 0.1493 0.1755 -0.0163 -0.0299 0.0031  149 THR   B C   
6488 O  O   . THR   B 149 ? 0.1664 0.1453 0.2025 -0.0230 -0.0133 -0.0009 149 THR   B O   
6489 C  CB  . THR   B 149 ? 0.1653 0.1469 0.2048 -0.0133 -0.0278 0.0066  149 THR   B CB  
6490 O  OG1 . THR   B 149 ? 0.1640 0.1511 0.1995 -0.0209 -0.0295 0.0018  149 THR   B OG1 
6491 C  CG2 . THR   B 149 ? 0.1703 0.1470 0.2300 -0.0068 -0.0279 0.0050  149 THR   B CG2 
6499 N  N   . ASN   B 150 ? 0.1712 0.1424 0.1883 -0.0171 -0.0373 -0.0006 150 ASN   B N   
6500 C  CA  . ASN   B 150 ? 0.1792 0.1577 0.1818 -0.0195 -0.0302 -0.0064 150 ASN   B CA  
6501 C  C   . ASN   B 150 ? 0.1686 0.1519 0.1830 -0.0191 -0.0271 -0.0018 150 ASN   B C   
6502 O  O   . ASN   B 150 ? 0.1745 0.1526 0.1979 -0.0287 -0.0373 -0.0002 150 ASN   B O   
6503 C  CB  . ASN   B 150 ? 0.1970 0.1945 0.2023 -0.0197 -0.0524 0.0088  150 ASN   B CB  
6504 C  CG  . ASN   B 150 ? 0.2244 0.2363 0.2371 -0.0218 -0.0566 0.0251  150 ASN   B CG  
6505 O  OD1 . ASN   B 150 ? 0.2322 0.2531 0.2508 -0.0320 -0.0692 0.0227  150 ASN   B OD1 
6506 N  ND2 . ASN   B 150 ? 0.2356 0.2558 0.2741 -0.0038 -0.0617 0.0694  150 ASN   B ND2 
6513 N  N   . VAL   B 151 ? 0.1586 0.1531 0.1862 -0.0183 -0.0283 0.0062  151 VAL   B N   
6514 C  CA  . VAL   B 151 ? 0.1617 0.1569 0.1813 -0.0230 -0.0188 -0.0066 151 VAL   B CA  
6515 C  C   . VAL   B 151 ? 0.1573 0.1486 0.1805 -0.0344 -0.0310 -0.0130 151 VAL   B C   
6516 O  O   . VAL   B 151 ? 0.1676 0.1539 0.1993 -0.0325 -0.0207 -0.0119 151 VAL   B O   
6517 C  CB  . VAL   B 151 ? 0.1781 0.1686 0.1985 -0.0050 -0.0183 -0.0060 151 VAL   B CB  
6518 C  CG1 . VAL   B 151 ? 0.1875 0.1719 0.2110 -0.0149 -0.0069 -0.0201 151 VAL   B CG1 
6519 C  CG2 . VAL   B 151 ? 0.1910 0.1802 0.1884 0.0111  -0.0243 0.0037  151 VAL   B CG2 
6529 N  N   . TYR   B 152 ? 0.1521 0.1328 0.1737 -0.0284 -0.0242 -0.0027 152 TYR   B N   
6530 C  CA  . TYR   B 152 ? 0.1583 0.1519 0.1600 -0.0257 -0.0128 -0.0049 152 TYR   B CA  
6531 C  C   . TYR   B 152 ? 0.1549 0.1414 0.1542 -0.0236 -0.0115 -0.0082 152 TYR   B C   
6532 O  O   . TYR   B 152 ? 0.1665 0.1470 0.1598 -0.0281 -0.0139 -0.0004 152 TYR   B O   
6533 C  CB  . TYR   B 152 ? 0.1786 0.1712 0.1642 -0.0268 -0.0151 0.0161  152 TYR   B CB  
6534 C  CG  . TYR   B 152 ? 0.1937 0.1818 0.1677 -0.0390 -0.0173 0.0083  152 TYR   B CG  
6535 C  CD1 . TYR   B 152 ? 0.2026 0.1896 0.1617 -0.0328 -0.0335 0.0128  152 TYR   B CD1 
6536 C  CD2 . TYR   B 152 ? 0.2106 0.1919 0.1749 -0.0390 -0.0189 -0.0069 152 TYR   B CD2 
6537 C  CE1 . TYR   B 152 ? 0.2169 0.1969 0.1808 -0.0280 -0.0329 0.0257  152 TYR   B CE1 
6538 C  CE2 . TYR   B 152 ? 0.2222 0.2125 0.1848 -0.0340 -0.0185 -0.0169 152 TYR   B CE2 
6539 C  CZ  . TYR   B 152 ? 0.2218 0.2216 0.1645 -0.0321 -0.0449 0.0161  152 TYR   B CZ  
6540 O  OH  . TYR   B 152 ? 0.2374 0.2570 0.2083 -0.0171 -0.0406 0.0233  152 TYR   B OH  
6550 N  N   . LEU   B 153 ? 0.1577 0.1361 0.1688 -0.0302 -0.0146 -0.0051 153 LEU   B N   
6551 C  CA  . LEU   B 153 ? 0.1642 0.1262 0.1648 -0.0235 -0.0105 -0.0097 153 LEU   B CA  
6552 C  C   . LEU   B 153 ? 0.1644 0.1290 0.1851 -0.0275 -0.0089 -0.0166 153 LEU   B C   
6553 O  O   . LEU   B 153 ? 0.1724 0.1543 0.1919 -0.0176 -0.0125 -0.0339 153 LEU   B O   
6554 C  CB  . LEU   B 153 ? 0.1677 0.1285 0.1745 -0.0215 -0.0083 -0.0088 153 LEU   B CB  
6555 C  CG  . LEU   B 153 ? 0.1636 0.1436 0.2075 -0.0209 -0.0054 -0.0083 153 LEU   B CG  
6556 C  CD1 . LEU   B 153 ? 0.1719 0.1572 0.2172 -0.0253 0.0041  -0.0002 153 LEU   B CD1 
6557 C  CD2 . LEU   B 153 ? 0.1665 0.1570 0.2016 -0.0227 0.0123  -0.0014 153 LEU   B CD2 
6569 N  N   . ALA   B 154 ? 0.1607 0.1317 0.1870 -0.0084 -0.0195 -0.0171 154 ALA   B N   
6570 C  CA  . ALA   B 154 ? 0.1693 0.1452 0.2125 0.0007  -0.0154 -0.0239 154 ALA   B CA  
6571 C  C   . ALA   B 154 ? 0.1810 0.1530 0.2061 0.0119  -0.0234 -0.0328 154 ALA   B C   
6572 O  O   . ALA   B 154 ? 0.2174 0.1502 0.2242 0.0076  -0.0108 -0.0171 154 ALA   B O   
6573 C  CB  . ALA   B 154 ? 0.1665 0.1654 0.2263 -0.0020 -0.0104 -0.0303 154 ALA   B CB  
6579 N  N   . VAL   B 155 ? 0.1477 0.1478 0.2122 0.0054  0.0049  -0.0175 155 VAL   B N   
6580 C  CA  . VAL   B 155 ? 0.1450 0.1466 0.2416 0.0053  -0.0119 -0.0064 155 VAL   B CA  
6581 C  C   . VAL   B 155 ? 0.1459 0.1411 0.2368 -0.0006 -0.0148 -0.0237 155 VAL   B C   
6582 O  O   . VAL   B 155 ? 0.1591 0.1547 0.2675 -0.0030 -0.0093 -0.0381 155 VAL   B O   
6583 C  CB  . VAL   B 155 ? 0.1473 0.1576 0.2752 0.0014  -0.0212 0.0103  155 VAL   B CB  
6584 C  CG1 . VAL   B 155 ? 0.1571 0.1561 0.2714 -0.0053 -0.0179 0.0097  155 VAL   B CG1 
6585 C  CG2 . VAL   B 155 ? 0.1504 0.1741 0.2986 -0.0059 -0.0256 0.0368  155 VAL   B CG2 
6595 N  N   . PHE   B 156 ? 0.1358 0.1524 0.2558 -0.0005 -0.0041 -0.0213 156 PHE   B N   
6596 C  CA  . PHE   B 156 ? 0.1442 0.1615 0.2798 0.0073  -0.0055 -0.0186 156 PHE   B CA  
6597 C  C   . PHE   B 156 ? 0.1434 0.1721 0.3093 0.0133  -0.0090 -0.0336 156 PHE   B C   
6598 O  O   . PHE   B 156 ? 0.1691 0.1899 0.3357 0.0240  0.0009  -0.0399 156 PHE   B O   
6599 C  CB  . PHE   B 156 ? 0.1526 0.1511 0.2900 0.0001  -0.0153 -0.0128 156 PHE   B CB  
6600 C  CG  . PHE   B 156 ? 0.1500 0.1583 0.3056 -0.0006 -0.0150 -0.0014 156 PHE   B CG  
6601 C  CD1 . PHE   B 156 ? 0.1547 0.1826 0.3360 0.0011  -0.0025 0.0391  156 PHE   B CD1 
6602 C  CD2 . PHE   B 156 ? 0.1597 0.1685 0.3052 0.0083  -0.0212 -0.0052 156 PHE   B CD2 
6603 C  CE1 . PHE   B 156 ? 0.1609 0.1977 0.3510 0.0045  -0.0058 0.0464  156 PHE   B CE1 
6604 C  CE2 . PHE   B 156 ? 0.1685 0.1857 0.3304 0.0069  -0.0191 0.0056  156 PHE   B CE2 
6605 C  CZ  . PHE   B 156 ? 0.1628 0.1945 0.3560 0.0101  -0.0168 0.0302  156 PHE   B CZ  
6615 N  N   . ASP   B 157 ? 0.1501 0.1651 0.3377 0.0184  -0.0185 -0.0173 157 ASP   B N   
6616 C  CA  . ASP   B 157 ? 0.1573 0.1654 0.3716 0.0126  -0.0214 -0.0281 157 ASP   B CA  
6617 C  C   . ASP   B 157 ? 0.1622 0.1632 0.3866 0.0092  -0.0250 -0.0506 157 ASP   B C   
6618 O  O   . ASP   B 157 ? 0.1541 0.1634 0.3619 0.0053  -0.0274 -0.0385 157 ASP   B O   
6619 C  CB  . ASP   B 157 ? 0.1826 0.1841 0.3800 0.0038  -0.0372 -0.0149 157 ASP   B CB  
6620 C  CG  . ASP   B 157 ? 0.2232 0.1969 0.4064 -0.0039 -0.0183 -0.0114 157 ASP   B CG  
6621 O  OD1 . ASP   B 157 ? 0.2334 0.1894 0.4184 0.0066  -0.0250 -0.0084 157 ASP   B OD1 
6622 O  OD2 . ASP   B 157 ? 0.2605 0.2209 0.4341 -0.0048 0.0046  -0.0076 157 ASP   B OD2 
6627 N  N   . LYS   B 158 ? 0.1700 0.1884 0.3986 0.0056  -0.0106 -0.0739 158 LYS   B N   
6628 C  CA  . LYS   B 158 ? 0.1793 0.2025 0.4076 0.0103  0.0015  -0.0813 158 LYS   B CA  
6629 C  C   . LYS   B 158 ? 0.1787 0.1905 0.4184 0.0146  -0.0069 -0.0748 158 LYS   B C   
6630 O  O   . LYS   B 158 ? 0.1755 0.1860 0.4299 0.0000  -0.0053 -0.0862 158 LYS   B O   
6631 C  CB  . LYS   B 158 ? 0.2025 0.2380 0.4084 0.0104  0.0114  -0.1067 158 LYS   B CB  
6632 C  CG  . LYS   B 158 ? 0.2437 0.2656 0.4085 0.0151  0.0207  -0.1200 158 LYS   B CG  
6633 C  CD  . LYS   B 158 ? 0.2793 0.3015 0.4178 0.0086  0.0229  -0.1029 158 LYS   B CD  
6634 C  CE  . LYS   B 158 ? 0.3079 0.3323 0.4325 0.0117  0.0249  -0.0918 158 LYS   B CE  
6635 N  NZ  . LYS   B 158 ? 0.3151 0.3375 0.4318 0.0086  0.0259  -0.0898 158 LYS   B NZ  
6649 N  N   . ASN   B 159 ? 0.1744 0.1804 0.4381 0.0089  -0.0241 -0.0633 159 ASN   B N   
6650 C  CA  . ASN   B 159 ? 0.1914 0.1717 0.4462 0.0188  -0.0365 -0.0424 159 ASN   B CA  
6651 C  C   . ASN   B 159 ? 0.1770 0.1519 0.4399 0.0084  -0.0526 -0.0325 159 ASN   B C   
6652 O  O   . ASN   B 159 ? 0.1830 0.1477 0.4575 -0.0047 -0.0615 -0.0279 159 ASN   B O   
6653 C  CB  . ASN   B 159 ? 0.2136 0.1874 0.4729 0.0279  -0.0378 -0.0352 159 ASN   B CB  
6654 C  CG  . ASN   B 159 ? 0.2441 0.2111 0.4736 0.0342  -0.0438 -0.0517 159 ASN   B CG  
6655 O  OD1 . ASN   B 159 ? 0.2647 0.2132 0.5003 0.0305  -0.0423 -0.0568 159 ASN   B OD1 
6656 N  ND2 . ASN   B 159 ? 0.2446 0.2238 0.5035 0.0470  -0.0483 -0.0548 159 ASN   B ND2 
6663 N  N   . LEU   B 160 ? 0.1669 0.1502 0.4091 0.0050  -0.0462 -0.0298 160 LEU   B N   
6664 C  CA  . LEU   B 160 ? 0.1645 0.1563 0.3614 0.0096  -0.0379 -0.0165 160 LEU   B CA  
6665 C  C   . LEU   B 160 ? 0.1625 0.1535 0.3422 -0.0015 -0.0183 -0.0320 160 LEU   B C   
6666 O  O   . LEU   B 160 ? 0.1483 0.1529 0.3370 -0.0056 -0.0248 -0.0247 160 LEU   B O   
6667 C  CB  . LEU   B 160 ? 0.1616 0.1691 0.3415 0.0030  -0.0374 -0.0006 160 LEU   B CB  
6668 C  CG  . LEU   B 160 ? 0.1584 0.1943 0.3170 0.0069  -0.0283 -0.0013 160 LEU   B CG  
6669 C  CD1 . LEU   B 160 ? 0.1678 0.2190 0.3232 -0.0029 -0.0182 -0.0048 160 LEU   B CD1 
6670 C  CD2 . LEU   B 160 ? 0.1584 0.2014 0.3185 0.0202  -0.0204 -0.0052 160 LEU   B CD2 
6682 N  N   . TYR   B 161 ? 0.1578 0.1602 0.3355 -0.0073 -0.0048 -0.0506 161 TYR   B N   
6683 C  CA  . TYR   B 161 ? 0.1647 0.1647 0.3365 -0.0158 0.0132  -0.0534 161 TYR   B CA  
6684 C  C   . TYR   B 161 ? 0.1730 0.1634 0.3311 -0.0117 0.0131  -0.0481 161 TYR   B C   
6685 O  O   . TYR   B 161 ? 0.1805 0.1630 0.3217 -0.0182 0.0017  -0.0420 161 TYR   B O   
6686 C  CB  . TYR   B 161 ? 0.1796 0.1731 0.3300 -0.0244 0.0297  -0.0671 161 TYR   B CB  
6687 C  CG  . TYR   B 161 ? 0.2038 0.1719 0.3222 -0.0315 0.0417  -0.0680 161 TYR   B CG  
6688 C  CD1 . TYR   B 161 ? 0.2105 0.1715 0.3263 -0.0448 0.0466  -0.0556 161 TYR   B CD1 
6689 C  CD2 . TYR   B 161 ? 0.2314 0.1778 0.3242 -0.0248 0.0437  -0.0548 161 TYR   B CD2 
6690 C  CE1 . TYR   B 161 ? 0.2314 0.1931 0.3239 -0.0429 0.0447  -0.0527 161 TYR   B CE1 
6691 C  CE2 . TYR   B 161 ? 0.2539 0.1961 0.3133 -0.0269 0.0479  -0.0455 161 TYR   B CE2 
6692 C  CZ  . TYR   B 161 ? 0.2520 0.1998 0.3149 -0.0448 0.0357  -0.0429 161 TYR   B CZ  
6693 O  OH  . TYR   B 161 ? 0.2838 0.2233 0.3352 -0.0476 0.0378  -0.0422 161 TYR   B OH  
6703 N  N   . ASP   B 162 ? 0.1738 0.1609 0.3474 -0.0073 -0.0027 -0.0621 162 ASP   B N   
6704 C  CA  . ASP   B 162 ? 0.1841 0.1667 0.3461 -0.0046 -0.0125 -0.0584 162 ASP   B CA  
6705 C  C   . ASP   B 162 ? 0.1787 0.1525 0.3373 -0.0110 -0.0069 -0.0421 162 ASP   B C   
6706 O  O   . ASP   B 162 ? 0.1828 0.1589 0.3424 -0.0183 -0.0223 -0.0317 162 ASP   B O   
6707 C  CB  . ASP   B 162 ? 0.2051 0.1852 0.3666 0.0033  -0.0213 -0.0788 162 ASP   B CB  
6708 C  CG  . ASP   B 162 ? 0.2099 0.2067 0.3861 0.0127  -0.0117 -0.0929 162 ASP   B CG  
6709 O  OD1 . ASP   B 162 ? 0.2135 0.2270 0.3823 0.0055  0.0027  -0.0845 162 ASP   B OD1 
6710 O  OD2 . ASP   B 162 ? 0.2216 0.2258 0.4213 0.0279  0.0062  -0.0847 162 ASP   B OD2 
6715 N  N   A LYS   B 163 ? 0.1694 0.1373 0.3328 -0.0079 -0.0202 -0.0256 163 LYS   B N   
6716 N  N   B LYS   B 163 ? 0.1842 0.1608 0.3325 -0.0107 -0.0128 -0.0280 163 LYS   B N   
6717 C  CA  A LYS   B 163 ? 0.1746 0.1460 0.3318 -0.0092 -0.0243 -0.0053 163 LYS   B CA  
6718 C  CA  B LYS   B 163 ? 0.1892 0.1724 0.3290 -0.0127 -0.0133 -0.0111 163 LYS   B CA  
6719 C  C   A LYS   B 163 ? 0.1575 0.1452 0.3202 -0.0199 -0.0203 -0.0000 163 LYS   B C   
6720 C  C   B LYS   B 163 ? 0.1692 0.1564 0.3142 -0.0187 -0.0128 -0.0050 163 LYS   B C   
6721 O  O   A LYS   B 163 ? 0.1564 0.1548 0.3424 -0.0253 -0.0266 0.0047  163 LYS   B O   
6722 O  O   B LYS   B 163 ? 0.1665 0.1576 0.3181 -0.0218 -0.0156 -0.0007 163 LYS   B O   
6723 C  CB  A LYS   B 163 ? 0.2094 0.1684 0.3631 0.0067  -0.0374 0.0115  163 LYS   B CB  
6724 C  CB  B LYS   B 163 ? 0.2142 0.2007 0.3576 -0.0085 -0.0183 -0.0030 163 LYS   B CB  
6725 C  CG  A LYS   B 163 ? 0.2636 0.2224 0.4029 0.0062  -0.0232 0.0123  163 LYS   B CG  
6726 C  CG  B LYS   B 163 ? 0.2451 0.2380 0.3881 -0.0070 -0.0138 -0.0005 163 LYS   B CG  
6727 C  CD  A LYS   B 163 ? 0.3002 0.2551 0.4445 -0.0019 -0.0152 -0.0034 163 LYS   B CD  
6728 C  CD  B LYS   B 163 ? 0.2719 0.2642 0.4213 -0.0085 -0.0116 -0.0044 163 LYS   B CD  
6729 C  CE  A LYS   B 163 ? 0.3432 0.2733 0.4729 -0.0085 -0.0105 -0.0069 163 LYS   B CE  
6730 C  CE  B LYS   B 163 ? 0.2883 0.2721 0.4474 -0.0109 -0.0094 -0.0046 163 LYS   B CE  
6731 N  NZ  A LYS   B 163 ? 0.3825 0.3156 0.4893 -0.0134 -0.0075 -0.0120 163 LYS   B NZ  
6732 N  NZ  B LYS   B 163 ? 0.3041 0.3041 0.4617 -0.0127 -0.0084 -0.0052 163 LYS   B NZ  
6759 N  N   . LEU   B 164 ? 0.1552 0.1399 0.2888 -0.0211 -0.0123 -0.0065 164 LEU   B N   
6760 C  CA  . LEU   B 164 ? 0.1552 0.1386 0.2669 -0.0154 -0.0168 -0.0094 164 LEU   B CA  
6761 C  C   . LEU   B 164 ? 0.1584 0.1411 0.2876 -0.0205 -0.0232 -0.0072 164 LEU   B C   
6762 O  O   . LEU   B 164 ? 0.1583 0.1643 0.3084 -0.0159 -0.0322 -0.0068 164 LEU   B O   
6763 C  CB  . LEU   B 164 ? 0.1483 0.1384 0.2650 -0.0152 -0.0205 -0.0082 164 LEU   B CB  
6764 C  CG  . LEU   B 164 ? 0.1591 0.1621 0.2799 -0.0117 -0.0087 -0.0032 164 LEU   B CG  
6765 C  CD1 . LEU   B 164 ? 0.1644 0.1628 0.2690 -0.0143 -0.0236 -0.0072 164 LEU   B CD1 
6766 C  CD2 . LEU   B 164 ? 0.1712 0.1983 0.2893 -0.0162 0.0138  -0.0181 164 LEU   B CD2 
6779 N  N   . VAL   B 165 ? 0.1920 0.1502 0.3092 -0.0198 -0.0398 -0.0123 165 VAL   B N   
6780 C  CA  . VAL   B 165 ? 0.2235 0.1646 0.3211 -0.0310 -0.0635 -0.0096 165 VAL   B CA  
6781 C  C   . VAL   B 165 ? 0.2540 0.1759 0.3518 -0.0390 -0.0887 -0.0136 165 VAL   B C   
6782 O  O   . VAL   B 165 ? 0.2711 0.1878 0.3592 -0.0376 -0.0911 -0.0004 165 VAL   B O   
6783 C  CB  . VAL   B 165 ? 0.2414 0.1829 0.3168 -0.0006 -0.0344 -0.0147 165 VAL   B CB  
6784 C  CG1 . VAL   B 165 ? 0.2594 0.1929 0.3501 -0.0009 -0.0196 -0.0085 165 VAL   B CG1 
6785 C  CG2 . VAL   B 165 ? 0.2345 0.1868 0.3138 0.0096  -0.0275 -0.0181 165 VAL   B CG2 
6795 N  N   . SER   B 166 ? 0.2618 0.1653 0.3748 -0.0386 -0.0910 -0.0305 166 SER   B N   
6796 C  CA  . SER   B 166 ? 0.2570 0.1664 0.4079 -0.0355 -0.0747 -0.0399 166 SER   B CA  
6797 C  C   . SER   B 166 ? 0.2450 0.1702 0.4229 -0.0337 -0.0725 -0.0126 166 SER   B C   
6798 O  O   . SER   B 166 ? 0.2511 0.1975 0.4457 -0.0479 -0.0981 -0.0291 166 SER   B O   
6799 C  CB  . SER   B 166 ? 0.2540 0.1831 0.4360 -0.0211 -0.0655 -0.0394 166 SER   B CB  
6800 O  OG  . SER   B 166 ? 0.2363 0.1798 0.4524 -0.0143 -0.0730 -0.0225 166 SER   B OG  
6806 N  N   . SER   B 167 ? 0.2165 0.1703 0.3966 -0.0335 -0.0721 0.0227  167 SER   B N   
6807 C  CA  . SER   B 167 ? 0.2091 0.1783 0.3751 -0.0251 -0.0510 0.0263  167 SER   B CA  
6808 C  C   . SER   B 167 ? 0.1958 0.1850 0.3623 -0.0423 -0.0555 0.0376  167 SER   B C   
6809 O  O   . SER   B 167 ? 0.1989 0.2012 0.3664 -0.0490 -0.0594 0.0356  167 SER   B O   
6810 C  CB  . SER   B 167 ? 0.2073 0.1857 0.3767 -0.0288 -0.0324 0.0231  167 SER   B CB  
6811 O  OG  . SER   B 167 ? 0.2035 0.1935 0.3618 -0.0264 -0.0260 0.0328  167 SER   B OG  
6817 N  N   . PHE   B 168 ? 0.1944 0.1804 0.3648 -0.0401 -0.0296 0.0453  168 PHE   B N   
6818 C  CA  . PHE   B 168 ? 0.1999 0.1781 0.3341 -0.0431 -0.0343 0.0329  168 PHE   B CA  
6819 C  C   . PHE   B 168 ? 0.1793 0.1681 0.2694 -0.0237 -0.0133 0.0125  168 PHE   B C   
6820 O  O   . PHE   B 168 ? 0.2115 0.1640 0.2758 -0.0031 -0.0113 -0.0029 168 PHE   B O   
6821 C  CB  . PHE   B 168 ? 0.2255 0.1866 0.3475 -0.0494 -0.0498 0.0465  168 PHE   B CB  
6822 C  CG  . PHE   B 168 ? 0.2547 0.1696 0.3254 -0.0522 -0.0504 0.0223  168 PHE   B CG  
6823 C  CD1 . PHE   B 168 ? 0.2867 0.1762 0.3351 -0.0468 -0.0539 0.0138  168 PHE   B CD1 
6824 C  CD2 . PHE   B 168 ? 0.2421 0.1630 0.3212 -0.0438 -0.0541 0.0199  168 PHE   B CD2 
6825 C  CE1 . PHE   B 168 ? 0.2985 0.1824 0.3205 -0.0366 -0.0429 0.0254  168 PHE   B CE1 
6826 C  CE2 . PHE   B 168 ? 0.2692 0.1715 0.3273 -0.0268 -0.0555 0.0194  168 PHE   B CE2 
6827 C  CZ  . PHE   B 168 ? 0.2852 0.1684 0.3299 -0.0196 -0.0583 0.0373  168 PHE   B CZ  
6837 N  N   . LEU   B 169 ? 0.1900 0.1837 0.2729 -0.0026 -0.0018 0.0007  169 LEU   B N   
6838 C  CA  . LEU   B 169 ? 0.2019 0.2138 0.3049 -0.0090 -0.0060 -0.0248 169 LEU   B CA  
6839 C  C   . LEU   B 169 ? 0.2390 0.2391 0.3606 0.0078  -0.0104 -0.0489 169 LEU   B C   
6840 O  O   . LEU   B 169 ? 0.2627 0.2591 0.4158 0.0069  -0.0066 -0.0712 169 LEU   B O   
6841 C  CB  . LEU   B 169 ? 0.2212 0.2583 0.3187 -0.0195 -0.0056 -0.0054 169 LEU   B CB  
6842 C  CG  . LEU   B 169 ? 0.2663 0.2987 0.3621 -0.0050 0.0070  0.0033  169 LEU   B CG  
6843 C  CD1 . LEU   B 169 ? 0.2902 0.3185 0.3610 -0.0053 0.0048  0.0230  169 LEU   B CD1 
6844 C  CD2 . LEU   B 169 ? 0.2594 0.3067 0.3596 0.0144  0.0295  -0.0114 169 LEU   B CD2 
6845 O  OXT . LEU   B 169 ? 0.2593 0.2507 0.3491 0.0358  -0.0009 -0.0514 169 LEU   B OXT 
6857 C  C1  T TFA   C .   ? 0.1434 0.1589 0.1440 -0.0156 0.0331  0.0110  201 TFA   A C1  
6858 C  C2  T TFA   C .   ? 0.1594 0.1853 0.1748 -0.0233 0.0167  -0.0039 201 TFA   A C2  
6859 O  O   T TFA   C .   ? 0.1246 0.1406 0.1344 -0.0097 0.0370  0.0294  201 TFA   A O   
6860 F  F1  T TFA   C .   ? 0.1666 0.1935 0.2233 -0.0184 0.0057  -0.0073 201 TFA   A F1  
6861 F  F2  T TFA   C .   ? 0.1708 0.1978 0.1702 -0.0245 0.0223  0.0030  201 TFA   A F2  
6862 F  F3  T TFA   C .   ? 0.1708 0.2003 0.2088 -0.0350 0.0318  -0.0148 201 TFA   A F3  
6863 O  OXT T TFA   C .   ? 0.1501 0.1519 0.1496 0.0066  0.0441  0.0095  201 TFA   A OXT 
6864 N  N2  B A1A9F D .   ? 0.1741 0.1706 0.1844 -0.0017 0.0042  0.0367  202 A1A9F A N2  
6865 C  C3  B A1A9F D .   ? 0.2165 0.1888 0.2020 -0.0047 0.0146  0.0163  202 A1A9F A C3  
6866 C  C6  B A1A9F D .   ? 0.1887 0.1799 0.2218 -0.0116 0.0247  0.0001  202 A1A9F A C6  
6867 C  C9  B A1A9F D .   ? 0.1504 0.1699 0.1747 -0.0036 -0.0075 0.0307  202 A1A9F A C9  
6868 C  C12 B A1A9F D .   ? 0.1244 0.1658 0.1744 -0.0199 -0.0081 0.0315  202 A1A9F A C12 
6869 C  C1  B A1A9F D .   ? 0.2285 0.2045 0.2044 -0.0135 0.0139  0.0180  202 A1A9F A C1  
6870 C  C10 B A1A9F D .   ? 0.1524 0.1770 0.1780 -0.0061 0.0026  0.0209  202 A1A9F A C10 
6871 C  C11 B A1A9F D .   ? 0.1387 0.1756 0.1777 -0.0145 0.0080  0.0130  202 A1A9F A C11 
6872 C  C13 B A1A9F D .   ? 0.2209 0.1883 0.1914 -0.0125 0.0175  0.0241  202 A1A9F A C13 
6873 C  C2  B A1A9F D .   ? 0.2218 0.1927 0.1958 -0.0042 0.0163  0.0148  202 A1A9F A C2  
6874 C  C4  B A1A9F D .   ? 0.2042 0.1863 0.2009 0.0004  0.0128  0.0073  202 A1A9F A C4  
6875 C  C5  B A1A9F D .   ? 0.1882 0.1761 0.1978 -0.0034 0.0154  0.0154  202 A1A9F A C5  
6876 C  C7  B A1A9F D .   ? 0.1673 0.1776 0.1867 -0.0031 -0.0020 0.0233  202 A1A9F A C7  
6877 C  C8  B A1A9F D .   ? 0.1705 0.1786 0.2016 -0.0005 0.0039  0.0194  202 A1A9F A C8  
6878 N  N1  B A1A9F D .   ? 0.2238 0.1950 0.1931 -0.0109 0.0207  0.0237  202 A1A9F A N1  
6879 N  N3  B A1A9F D .   ? 0.1715 0.1783 0.2022 -0.0040 -0.0071 0.0047  202 A1A9F A N3  
6880 N  N4  B A1A9F D .   ? 0.1673 0.1760 0.1883 -0.0017 0.0062  0.0367  202 A1A9F A N4  
6881 N  N5  B A1A9F D .   ? 0.1285 0.1578 0.1660 -0.0053 -0.0178 0.0431  202 A1A9F A N5  
6882 N  N6  B A1A9F D .   ? 0.2242 0.1913 0.1821 -0.0193 0.0267  0.0333  202 A1A9F A N6  
6883 O  O1  B A1A9F D .   ? 0.1872 0.1880 0.2397 -0.0196 0.0272  -0.0131 202 A1A9F A O1  
6900 CL CL  B CL    E .   ? 0.2008 0.1678 0.3370 -0.0225 -0.0360 0.0191  203 CL    A CL  
6901 O  O   . HOH   F .   ? 0.4281 0.7976 0.4924 -0.1169 0.0465  0.1050  301 HOH   A O   
6902 O  O   . HOH   F .   ? 0.2394 0.2272 0.3889 -0.0197 -0.0432 0.0287  302 HOH   A O   
6903 O  O   . HOH   F .   ? 0.2169 0.2550 0.2438 -0.0245 0.0306  0.0548  303 HOH   A O   
6904 O  O   . HOH   F .   ? 0.3104 0.2784 0.4234 -0.0236 -0.1227 0.1060  304 HOH   A O   
6905 O  O   . HOH   F .   ? 0.4954 0.3745 0.4384 -0.0463 0.1491  -0.0060 305 HOH   A O   
6906 O  O   . HOH   F .   ? 0.6505 0.4315 0.3443 0.1528  -0.1607 0.0369  306 HOH   A O   
6907 O  O   . HOH   F .   ? 0.2058 0.2692 0.3818 -0.0167 -0.0167 0.0264  307 HOH   A O   
6908 O  O   . HOH   F .   ? 0.6096 0.6153 0.4052 -0.0982 0.0006  0.2433  308 HOH   A O   
6909 O  O   . HOH   F .   ? 0.3183 0.3747 0.3488 -0.1361 0.0801  -0.0186 309 HOH   A O   
6910 O  O   . HOH   F .   ? 0.6041 0.4295 0.5412 -0.0949 0.1329  0.1355  310 HOH   A O   
6911 O  O   . HOH   F .   ? 0.3008 0.3429 0.1783 -0.0370 0.0467  0.0465  311 HOH   A O   
6912 O  O   . HOH   F .   ? 0.2736 0.4939 0.4054 0.0396  -0.0627 0.0405  312 HOH   A O   
6913 O  O   B HOH   F .   ? 0.1861 0.2511 0.3310 -0.0719 0.0107  -0.0057 313 HOH   A O   
6914 O  O   . HOH   F .   ? 0.1969 0.3717 0.4384 -0.0406 0.0296  -0.1175 314 HOH   A O   
6915 O  O   . HOH   F .   ? 0.2850 0.3673 0.3723 -0.0832 -0.0478 -0.0361 315 HOH   A O   
6916 O  O   . HOH   F .   ? 0.2642 0.2348 0.2875 0.0307  0.0333  0.0458  316 HOH   A O   
6917 O  O   . HOH   F .   ? 0.1701 0.1907 0.2769 0.0179  -0.0449 -0.0620 317 HOH   A O   
6918 O  O   . HOH   F .   ? 0.2369 0.1978 0.3573 -0.0474 -0.0093 -0.0150 318 HOH   A O   
6919 O  O   . HOH   F .   ? 0.5376 0.5363 0.2687 -0.1371 0.0889  0.1229  319 HOH   A O   
6920 O  O   . HOH   F .   ? 0.6901 0.5603 0.3834 -0.0522 -0.0565 0.0995  320 HOH   A O   
6921 O  O   . HOH   F .   ? 0.1988 0.2719 0.3090 0.0131  -0.0215 -0.0357 321 HOH   A O   
6922 O  O   . HOH   F .   ? 0.5626 0.6296 0.5024 -0.0956 -0.1297 -0.0721 322 HOH   A O   
6923 O  O   . HOH   F .   ? 0.1907 0.2918 0.2787 0.0532  0.0460  0.1017  323 HOH   A O   
6924 O  O   . HOH   F .   ? 0.3241 0.2882 0.3447 -0.0005 -0.0290 0.1023  324 HOH   A O   
6925 O  O   . HOH   F .   ? 0.3339 0.3252 0.2808 -0.1032 0.0031  0.0838  325 HOH   A O   
6926 O  O   . HOH   F .   ? 0.3467 0.2902 0.2348 -0.0060 -0.0794 0.0215  326 HOH   A O   
6927 O  O   . HOH   F .   ? 0.1611 0.4008 0.2677 0.0019  0.0333  0.0588  327 HOH   A O   
6928 O  O   A HOH   F .   ? 0.1541 0.2177 0.2201 0.0496  0.0591  0.0551  328 HOH   A O   
6929 O  O   . HOH   F .   ? 0.5312 0.4973 0.5386 0.0448  0.2399  -0.0737 329 HOH   A O   
6930 O  O   . HOH   F .   ? 0.1637 0.1622 0.2354 -0.0150 0.0092  0.0140  330 HOH   A O   
6931 O  O   . HOH   F .   ? 0.3067 0.4294 0.2849 -0.0047 0.0389  0.0234  331 HOH   A O   
6932 O  O   . HOH   F .   ? 0.2155 0.1823 0.1517 -0.0034 0.0181  0.0160  332 HOH   A O   
6933 O  O   . HOH   F .   ? 0.2102 0.2455 0.2370 -0.0329 -0.0566 0.0559  333 HOH   A O   
6934 O  O   . HOH   F .   ? 0.1828 0.1807 0.2210 0.0153  -0.0181 0.0311  334 HOH   A O   
6935 O  O   . HOH   F .   ? 0.4165 0.2100 0.4586 0.0095  -0.1979 0.0292  335 HOH   A O   
6936 O  O   . HOH   F .   ? 0.3304 0.7111 0.5959 -0.0034 -0.0718 0.0628  336 HOH   A O   
6937 O  O   . HOH   F .   ? 0.3755 0.3457 0.4191 -0.0926 0.1424  -0.0098 337 HOH   A O   
6938 O  O   . HOH   F .   ? 0.3265 0.3373 0.3557 -0.0901 -0.0080 -0.0231 338 HOH   A O   
6939 O  O   . HOH   F .   ? 0.6301 0.4377 0.5534 0.1072  -0.0376 0.0278  339 HOH   A O   
6940 O  O   . HOH   F .   ? 0.4171 0.4172 0.3902 0.0784  0.0161  -0.1590 340 HOH   A O   
6941 O  O   . HOH   F .   ? 0.5209 0.4905 0.4496 -0.0366 0.1199  0.2201  341 HOH   A O   
6942 O  O   . HOH   F .   ? 0.5266 0.2468 0.5030 0.0796  0.0139  0.0205  342 HOH   A O   
6943 O  O   . HOH   F .   ? 0.2660 0.2346 0.2441 -0.0268 0.0161  -0.0147 343 HOH   A O   
6944 O  O   . HOH   F .   ? 0.6079 0.3820 0.3064 -0.0840 -0.1194 0.0050  344 HOH   A O   
6945 O  O   A HOH   F .   ? 0.4675 0.4764 0.5294 0.1354  0.0885  -0.1320 345 HOH   A O   
6946 O  O   B HOH   F .   ? 0.3033 0.4507 0.3541 0.0910  0.0075  -0.0718 346 HOH   A O   
6947 O  O   B HOH   F .   ? 0.2939 0.3210 0.1418 -0.0049 0.0139  0.0429  347 HOH   A O   
6948 O  O   . HOH   F .   ? 0.1627 0.2400 0.2231 -0.0044 -0.0154 0.0612  348 HOH   A O   
6949 O  O   . HOH   F .   ? 0.2230 0.4600 0.4375 -0.0229 -0.0787 0.1914  349 HOH   A O   
6950 O  O   . HOH   F .   ? 0.1557 0.1993 0.2520 0.0056  -0.0083 0.0112  350 HOH   A O   
6951 O  O   . HOH   F .   ? 0.2673 0.2133 0.1858 -0.0641 -0.0027 0.0363  351 HOH   A O   
6952 O  O   . HOH   F .   ? 0.2643 0.5322 0.6280 0.0653  0.0492  0.0303  352 HOH   A O   
6953 O  O   . HOH   F .   ? 0.4631 0.4124 0.4585 -0.2014 -0.1212 0.2019  353 HOH   A O   
6954 O  O   . HOH   F .   ? 0.2195 0.1735 0.2491 0.0133  -0.0228 -0.0032 354 HOH   A O   
6955 O  O   A HOH   F .   ? 0.2064 0.2533 0.4181 0.0044  0.0844  0.1270  355 HOH   A O   
6956 O  O   . HOH   F .   ? 0.1999 0.2015 0.3868 0.0360  0.0983  0.1035  356 HOH   A O   
6957 O  O   . HOH   F .   ? 0.2083 0.2183 0.3898 0.0152  0.1058  -0.0076 357 HOH   A O   
6958 O  O   . HOH   F .   ? 0.3049 0.3582 0.2489 -0.0914 -0.0212 -0.0612 358 HOH   A O   
6959 O  O   . HOH   F .   ? 0.1425 0.1417 0.1328 -0.0038 0.0074  0.0071  359 HOH   A O   
6960 O  O   . HOH   F .   ? 0.1872 0.2469 0.1899 -0.0136 0.0024  0.0737  360 HOH   A O   
6961 O  O   . HOH   F .   ? 0.3957 0.4203 0.3783 0.1984  0.0901  0.0498  361 HOH   A O   
6962 O  O   A HOH   F .   ? 0.2112 0.2308 0.2372 0.0249  0.0231  0.0109  362 HOH   A O   
6963 O  O   . HOH   F .   ? 0.2523 0.3806 0.3776 0.0882  -0.0827 -0.0130 363 HOH   A O   
6964 O  O   . HOH   F .   ? 0.2817 0.4201 0.3351 -0.0337 0.0657  0.0098  364 HOH   A O   
6965 O  O   . HOH   F .   ? 0.3400 0.3739 0.2536 -0.0359 -0.0546 0.0393  365 HOH   A O   
6966 O  O   . HOH   F .   ? 0.3725 0.7110 0.4993 -0.0277 -0.1417 0.0945  366 HOH   A O   
6967 O  O   . HOH   F .   ? 0.4288 0.2204 0.2256 0.1235  0.0573  0.0260  367 HOH   A O   
6968 O  O   . HOH   F .   ? 0.2872 0.3606 0.4972 -0.0524 -0.0792 -0.1130 368 HOH   A O   
6969 O  O   . HOH   F .   ? 0.2454 0.1931 0.2533 -0.0180 -0.0656 -0.0019 369 HOH   A O   
6970 O  O   . HOH   F .   ? 0.4430 0.2755 0.4215 -0.1312 0.1559  -0.0540 370 HOH   A O   
6971 O  O   . HOH   F .   ? 0.1479 0.1684 0.1566 -0.0034 -0.0061 -0.0040 371 HOH   A O   
6972 O  O   . HOH   F .   ? 0.1657 0.1401 0.2469 -0.0022 0.0144  -0.0090 372 HOH   A O   
6973 O  O   A HOH   F .   ? 0.1797 0.1881 0.2495 0.0054  -0.0543 0.0187  373 HOH   A O   
6974 O  O   . HOH   F .   ? 0.2084 0.2101 0.1782 0.0031  0.0145  0.0146  374 HOH   A O   
6975 O  O   . HOH   F .   ? 0.6119 0.6122 0.4254 0.2082  -0.0209 -0.0146 375 HOH   A O   
6976 O  O   . HOH   F .   ? 0.2188 0.2757 0.3457 0.0102  0.0923  -0.0740 376 HOH   A O   
6977 O  O   . HOH   F .   ? 0.5839 0.3858 0.3306 -0.0151 -0.0278 0.1366  377 HOH   A O   
6978 O  O   B HOH   F .   ? 0.2589 0.1713 0.2225 0.0241  -0.0023 -0.0020 378 HOH   A O   
6979 O  O   A HOH   F .   ? 0.3558 0.1656 0.2114 0.0159  0.0245  -0.0080 379 HOH   A O   
6980 O  O   . HOH   F .   ? 0.8227 0.3966 0.5047 -0.0314 0.1710  0.1665  380 HOH   A O   
6981 O  O   . HOH   F .   ? 0.5933 0.5415 0.6607 -0.1029 0.0172  0.1410  381 HOH   A O   
6982 O  O   . HOH   F .   ? 0.2947 0.6721 0.3336 0.0738  0.0306  -0.1369 382 HOH   A O   
6983 O  O   . HOH   F .   ? 0.2640 0.5796 0.5192 0.0853  0.0281  0.1494  383 HOH   A O   
6984 O  O   . HOH   F .   ? 0.1937 0.2070 0.2425 -0.0322 0.0141  0.0311  384 HOH   A O   
6985 O  O   A HOH   F .   ? 0.2423 0.2408 0.2569 0.0616  0.0492  0.0545  385 HOH   A O   
6986 O  O   . HOH   F .   ? 0.3312 0.2565 0.5057 -0.0414 -0.0449 0.0088  386 HOH   A O   
6987 O  O   . HOH   F .   ? 0.4218 0.2558 0.4468 -0.1374 0.0747  0.0473  387 HOH   A O   
6988 O  O   B HOH   F .   ? 0.3176 0.2354 0.2481 0.1093  -0.0632 0.0020  388 HOH   A O   
6989 O  O   . HOH   F .   ? 0.2007 0.2378 0.2736 -0.0213 -0.0209 0.0883  389 HOH   A O   
6990 O  O   . HOH   F .   ? 0.5458 0.2650 0.5333 0.0660  -0.0047 -0.0373 390 HOH   A O   
6991 O  O   . HOH   F .   ? 0.3053 0.4649 0.2870 0.0559  0.0919  0.1818  391 HOH   A O   
6992 O  O   . HOH   F .   ? 0.1869 0.2623 0.2978 -0.0256 0.0667  0.0628  392 HOH   A O   
6993 O  O   T HOH   F .   ? 0.1010 0.1232 0.2510 -0.0040 0.0241  0.0336  393 HOH   A O   
6994 O  O   . HOH   F .   ? 0.1813 0.1887 0.2343 -0.0258 0.0059  0.0437  394 HOH   A O   
6995 O  O   . HOH   F .   ? 0.4749 0.4151 0.5369 0.0629  0.1616  -0.1444 395 HOH   A O   
6996 O  O   . HOH   F .   ? 0.1570 0.1779 0.3023 0.0025  -0.0076 0.0248  396 HOH   A O   
6997 O  O   . HOH   F .   ? 0.2494 0.3902 0.3563 -0.0150 0.0033  0.0710  397 HOH   A O   
6998 O  O   . HOH   F .   ? 0.3338 0.2738 0.2297 0.0151  0.0813  -0.0028 398 HOH   A O   
6999 O  O   . HOH   F .   ? 0.2475 0.2009 0.2567 0.0015  0.0048  0.0292  399 HOH   A O   
7000 O  O   . HOH   F .   ? 0.7463 0.4409 0.6021 -0.0414 -0.1434 0.0386  400 HOH   A O   
7001 O  O   . HOH   F .   ? 0.1580 0.1905 0.1857 0.0167  -0.0284 -0.0425 401 HOH   A O   
7002 O  O   . HOH   F .   ? 0.3776 0.6801 0.4231 -0.0946 0.0079  0.1324  402 HOH   A O   
7003 O  O   . HOH   F .   ? 0.5251 0.2787 0.3145 -0.1139 0.0281  0.0278  403 HOH   A O   
7004 O  O   B HOH   F .   ? 0.3202 0.2442 0.2814 -0.0056 0.0104  0.0630  404 HOH   A O   
7005 O  O   . HOH   F .   ? 0.1478 0.1503 0.1793 0.0002  -0.0122 0.0028  405 HOH   A O   
7006 O  O   . HOH   F .   ? 0.2811 0.3703 0.3481 -0.0397 0.0984  -0.0392 406 HOH   A O   
7007 O  O   A HOH   F .   ? 0.2002 0.1907 0.3265 -0.0010 0.0550  -0.0148 407 HOH   A O   
7008 O  O   . HOH   F .   ? 0.3259 0.3953 0.3863 -0.0825 0.1518  -0.0108 408 HOH   A O   
7009 O  O   . HOH   F .   ? 0.3174 0.2804 0.2085 -0.0632 -0.0877 0.0225  409 HOH   A O   
7010 O  O   . HOH   F .   ? 0.4549 0.4309 0.2181 -0.0266 0.0809  0.0700  410 HOH   A O   
7011 O  O   . HOH   F .   ? 0.1783 0.1876 0.1857 0.0027  -0.0267 0.0019  411 HOH   A O   
7012 O  O   . HOH   F .   ? 0.6163 0.5301 0.5526 0.0442  0.1191  0.0527  412 HOH   A O   
7013 O  O   . HOH   F .   ? 0.2271 0.1801 0.3110 -0.0046 -0.0205 0.0218  413 HOH   A O   
7014 O  O   . HOH   F .   ? 0.4174 0.4220 0.3854 0.1716  0.0227  -0.0659 414 HOH   A O   
7015 O  O   . HOH   F .   ? 0.2201 0.2987 0.2640 -0.0201 -0.0534 0.0590  415 HOH   A O   
7016 O  O   . HOH   F .   ? 0.1885 0.1553 0.1541 -0.0240 0.0129  -0.0006 416 HOH   A O   
7017 O  O   . HOH   F .   ? 0.4339 0.4866 0.3649 0.1822  -0.0926 -0.1398 417 HOH   A O   
7018 O  O   . HOH   F .   ? 0.2632 0.2120 0.2728 -0.0617 -0.0028 0.0662  418 HOH   A O   
7019 O  O   . HOH   F .   ? 0.6562 0.3906 0.4922 0.1929  -0.0653 0.1391  419 HOH   A O   
7020 O  O   A HOH   F .   ? 0.2119 0.2098 0.2191 0.0072  -0.0135 0.0795  420 HOH   A O   
7021 O  O   . HOH   F .   ? 0.2898 0.6228 0.1919 -0.0451 0.0294  0.0067  421 HOH   A O   
7022 O  O   . HOH   F .   ? 0.4196 0.6244 0.3407 -0.0761 0.0223  0.1277  422 HOH   A O   
7023 O  O   . HOH   F .   ? 0.4259 0.2409 0.5918 -0.0844 -0.2636 0.1144  423 HOH   A O   
7024 O  O   . HOH   F .   ? 0.2499 0.2890 0.3427 0.0026  -0.0122 -0.0676 424 HOH   A O   
7025 O  O   . HOH   F .   ? 0.8821 0.8920 0.7924 -0.0217 -0.0043 0.0230  425 HOH   A O   
7026 O  O   A HOH   F .   ? 0.2615 0.3036 0.2286 -0.0406 0.0872  -0.0149 426 HOH   A O   
7027 O  O   . HOH   F .   ? 0.3680 0.6059 0.5148 0.1780  0.0580  0.0165  427 HOH   A O   
7028 O  O   . HOH   F .   ? 0.5643 0.6138 0.5704 0.0339  0.1273  0.0603  428 HOH   A O   
7029 O  O   . HOH   F .   ? 0.2398 0.4270 0.2680 0.1630  -0.0018 0.0114  429 HOH   A O   
7030 O  O   . HOH   F .   ? 0.3473 0.1394 0.2237 0.0039  -0.0532 0.0120  430 HOH   A O   
7031 O  O   . HOH   F .   ? 0.1688 0.2064 0.2922 -0.0087 0.0094  0.0234  431 HOH   A O   
7032 O  O   . HOH   F .   ? 0.3110 0.3741 0.7461 -0.0015 0.1096  -0.0502 432 HOH   A O   
7033 O  O   . HOH   F .   ? 0.2387 0.2467 0.4264 0.0051  -0.0427 -0.0500 433 HOH   A O   
7034 O  O   . HOH   F .   ? 0.2086 0.2017 0.2986 0.0227  -0.0575 0.0060  434 HOH   A O   
7035 O  O   . HOH   F .   ? 0.5694 0.5520 0.6432 -0.1404 -0.1093 -0.0812 435 HOH   A O   
7036 O  O   . HOH   F .   ? 0.6514 0.7088 0.4370 0.0965  0.2863  -0.0566 436 HOH   A O   
7037 O  O   A HOH   F .   ? 0.5914 0.4223 0.2903 -0.1433 0.0292  0.0867  437 HOH   A O   
7038 O  O   . HOH   F .   ? 0.5695 0.7825 0.4329 0.1689  -0.0722 0.1924  438 HOH   A O   
7039 O  O   . HOH   F .   ? 0.3809 0.3046 0.1830 -0.0917 0.0113  0.0609  439 HOH   A O   
7040 O  O   . HOH   F .   ? 0.2716 0.1806 0.2850 0.0123  0.0049  0.0063  440 HOH   A O   
7041 O  O   . HOH   F .   ? 0.5167 0.5092 0.3734 -0.0020 -0.1590 0.0394  441 HOH   A O   
7042 O  O   . HOH   F .   ? 0.2906 0.4163 0.5592 -0.0193 0.1221  -0.2087 442 HOH   A O   
7043 O  O   . HOH   F .   ? 0.1822 0.1697 0.1782 -0.0026 -0.0085 -0.0105 443 HOH   A O   
7044 O  O   . HOH   F .   ? 0.5222 0.3944 0.5260 0.0234  0.1431  -0.0787 444 HOH   A O   
7045 O  O   . HOH   F .   ? 0.3877 0.3441 0.3404 0.1950  -0.0472 -0.0332 445 HOH   A O   
7046 O  O   A HOH   F .   ? 0.2623 0.2253 0.2413 -0.0012 -0.0092 -0.0531 446 HOH   A O   
7047 O  O   B HOH   F .   ? 0.4468 0.3885 0.3293 0.0869  -0.0439 0.0617  447 HOH   A O   
7048 O  O   . HOH   F .   ? 0.6315 0.6317 0.6656 -0.1491 -0.0155 -0.1336 448 HOH   A O   
7049 O  O   . HOH   F .   ? 0.4563 0.4869 0.5201 -0.1194 -0.0750 -0.1239 449 HOH   A O   
7050 O  O   . HOH   F .   ? 0.1981 0.2437 0.5222 -0.0232 -0.0994 0.0618  450 HOH   A O   
7051 O  O   . HOH   F .   ? 0.6671 0.6233 0.8022 0.0792  -0.1324 0.2325  451 HOH   A O   
7052 O  O   . HOH   F .   ? 0.2504 0.2207 0.2639 0.0206  0.0293  0.0364  452 HOH   A O   
7053 O  O   . HOH   F .   ? 0.2262 0.2706 0.2546 0.0001  -0.0268 -0.0473 453 HOH   A O   
7054 O  O   A HOH   F .   ? 0.4369 0.2044 0.3578 -0.0939 0.0478  0.0635  454 HOH   A O   
7055 O  O   . HOH   F .   ? 0.4244 0.3726 0.4805 0.0454  0.0163  0.0704  455 HOH   A O   
7056 O  O   . HOH   F .   ? 0.6333 0.6847 0.6267 0.0753  -0.1319 0.0116  456 HOH   A O   
7057 O  O   . HOH   F .   ? 0.5341 0.3742 0.4068 -0.0232 -0.0034 0.1167  457 HOH   A O   
7058 O  O   . HOH   F .   ? 0.6472 0.6042 0.5185 -0.0812 0.0836  0.1110  458 HOH   A O   
7059 O  O   B HOH   F .   ? 0.2727 0.1951 0.3090 0.0272  0.0214  0.0451  459 HOH   A O   
7060 O  O   . HOH   F .   ? 0.4471 0.5174 0.4617 0.0798  0.0035  0.0338  460 HOH   A O   
7061 O  O   . HOH   F .   ? 0.3328 0.4046 0.3920 0.1587  -0.0336 0.0608  461 HOH   A O   
7062 O  O   . HOH   F .   ? 0.2847 0.2727 0.3812 -0.0613 0.0349  -0.0911 462 HOH   A O   
7063 O  O   . HOH   F .   ? 0.6917 0.7872 0.4946 0.1083  -0.1060 -0.0295 463 HOH   A O   
7064 O  O   . HOH   F .   ? 0.3367 0.4714 0.5474 -0.1340 0.0810  -0.1724 464 HOH   A O   
7065 O  O   . HOH   F .   ? 0.3646 0.4754 0.5036 0.0791  -0.0840 0.1135  465 HOH   A O   
7066 O  O   . HOH   F .   ? 0.7271 0.6418 0.6682 0.0906  0.1622  0.1803  466 HOH   A O   
7067 O  O   . HOH   F .   ? 0.2774 0.2866 0.3802 -0.0977 0.0523  -0.0321 467 HOH   A O   
7068 O  O   . HOH   F .   ? 0.5632 0.3771 0.6655 0.0620  0.0459  0.2325  468 HOH   A O   
7069 O  O   . HOH   F .   ? 0.2847 0.4489 0.5270 0.0695  -0.0134 -0.2056 469 HOH   A O   
7070 O  O   . HOH   F .   ? 0.3035 0.4948 0.4505 -0.0705 -0.0357 0.0234  470 HOH   A O   
7071 O  O   . HOH   F .   ? 0.2804 0.1873 0.2531 0.0201  -0.0910 -0.0227 471 HOH   A O   
7072 O  O   A HOH   F .   ? 0.2846 0.2655 0.5231 0.0882  -0.1638 -0.0693 472 HOH   A O   
7073 O  O   . HOH   F .   ? 0.4344 0.6116 0.3614 -0.1039 -0.0985 0.1982  473 HOH   A O   
7074 O  O   . HOH   F .   ? 0.5720 0.5104 0.5387 0.0030  0.1247  0.0191  474 HOH   A O   
7075 O  O   . HOH   F .   ? 0.3728 0.2671 0.4057 0.0385  0.1114  0.0051  475 HOH   A O   
7076 O  O   . HOH   F .   ? 0.4212 0.5319 0.3797 0.0458  -0.0224 -0.0639 476 HOH   A O   
7077 O  O   . HOH   F .   ? 0.5287 0.5111 0.4258 0.0192  -0.0903 -0.0611 477 HOH   A O   
7078 O  O   . HOH   F .   ? 0.4963 0.2905 0.3381 -0.0715 -0.1252 0.0684  478 HOH   A O   
7079 O  O   . HOH   F .   ? 0.4638 0.4447 0.5475 -0.2124 -0.0158 0.0025  479 HOH   A O   
7080 O  O   . HOH   F .   ? 0.4920 0.5025 0.5205 -0.1752 -0.0639 0.0130  480 HOH   A O   
7081 O  O   . HOH   F .   ? 0.4191 0.4937 0.2729 0.0036  -0.0031 -0.0346 481 HOH   A O   
7082 O  O   . HOH   F .   ? 0.7106 0.5940 0.6560 -0.1200 0.0771  -0.0940 482 HOH   A O   
7083 O  O   . HOH   F .   ? 0.4363 0.4513 0.3577 -0.0430 -0.0414 -0.0043 483 HOH   A O   
7084 O  O   . HOH   F .   ? 0.2442 0.2344 0.2663 0.0131  0.0012  -0.0089 484 HOH   A O   
7085 O  O   . HOH   F .   ? 0.7779 0.4306 0.3521 -0.0661 -0.1177 0.0183  485 HOH   A O   
7086 O  O   . HOH   F .   ? 0.5918 0.4096 0.4356 0.0592  0.0206  -0.1126 486 HOH   A O   
7087 O  O   . HOH   F .   ? 0.6225 0.4046 0.3845 -0.0214 0.0952  -0.0309 487 HOH   A O   
7088 O  O   . HOH   F .   ? 0.3008 0.4841 0.3580 -0.0112 -0.0340 -0.0918 488 HOH   A O   
7089 O  O   . HOH   F .   ? 0.6591 0.6185 0.4599 -0.0988 0.0991  0.1025  489 HOH   A O   
7090 O  O   . HOH   F .   ? 0.5532 0.6191 0.6649 0.0988  0.1403  -0.0972 490 HOH   A O   
7091 O  O   . HOH   F .   ? 0.2810 0.2599 0.7355 -0.0282 -0.1298 0.0275  491 HOH   A O   
7092 O  O   . HOH   F .   ? 0.2860 0.5269 0.3733 0.0961  0.1045  0.2386  492 HOH   A O   
7093 O  O   . HOH   F .   ? 0.3140 0.3797 0.5178 -0.0014 0.1395  0.1043  493 HOH   A O   
7094 O  O   . HOH   F .   ? 0.4166 0.3647 0.4528 -0.1017 -0.0071 0.1184  494 HOH   A O   
7095 O  O   . HOH   F .   ? 0.5420 0.5168 0.5665 -0.0260 -0.0968 0.0576  495 HOH   A O   
7096 O  O   . HOH   F .   ? 0.6654 0.5145 0.4997 -0.0542 -0.1254 -0.0687 496 HOH   A O   
7097 O  O   . HOH   F .   ? 0.4878 0.3500 0.4827 -0.0142 0.2628  0.0340  497 HOH   A O   
7098 O  O   . HOH   F .   ? 0.4326 0.4083 0.2746 -0.0976 0.1328  -0.0577 498 HOH   A O   
7099 O  O   . HOH   F .   ? 0.2985 0.2490 0.5338 0.0022  0.0181  0.1096  499 HOH   A O   
7100 O  O   . HOH   F .   ? 0.2509 0.3072 0.4877 0.0071  0.0676  -0.0034 500 HOH   A O   
7101 O  O   . HOH   F .   ? 0.2296 0.3857 0.3533 0.0427  -0.0238 0.0841  501 HOH   A O   
7102 O  O   . HOH   F .   ? 0.6644 0.2473 0.4100 -0.0817 0.0699  0.0389  502 HOH   A O   
7103 O  O   B HOH   F .   ? 0.2508 0.3874 0.2553 0.0543  0.0534  0.0900  503 HOH   A O   
7104 O  O   . HOH   F .   ? 0.4893 0.2673 0.4507 -0.1537 0.0008  0.0399  504 HOH   A O   
7105 O  O   . HOH   F .   ? 0.3719 0.7599 0.5827 -0.0948 -0.0176 0.2331  505 HOH   A O   
7106 O  O   . HOH   F .   ? 0.2810 0.4151 0.4671 0.0103  -0.0709 -0.0250 506 HOH   A O   
7107 O  O   . HOH   F .   ? 0.6152 0.6878 0.5374 0.1413  -0.0838 0.0733  507 HOH   A O   
7108 O  O   . HOH   F .   ? 0.6654 0.4931 0.5101 0.0119  0.0236  0.0709  508 HOH   A O   
7109 O  O   . HOH   F .   ? 0.6763 0.5969 0.4854 0.1513  -0.1552 0.0263  509 HOH   A O   
7110 O  O   . HOH   F .   ? 0.2835 0.2428 0.5227 0.0078  0.0324  0.0565  510 HOH   A O   
7111 O  O   . HOH   F .   ? 0.5137 0.6845 0.4580 0.2810  0.0061  0.1508  511 HOH   A O   
7112 O  O   T HOH   F .   ? 0.1109 0.1299 0.2527 -0.0228 -0.0209 0.0773  512 HOH   A O   
7113 O  O   A HOH   F .   ? 0.4292 0.7984 0.4374 0.1535  0.0528  0.0298  513 HOH   A O   
7114 O  O   . HOH   F .   ? 0.2798 0.6640 0.4868 0.0469  0.0427  -0.0567 514 HOH   A O   
7115 O  O   . HOH   F .   ? 0.5976 0.7578 0.5572 -0.0663 0.0380  -0.1287 515 HOH   A O   
7116 O  O   . HOH   F .   ? 0.4775 0.4449 0.4548 0.0922  -0.0447 0.1134  516 HOH   A O   
7117 O  O   . HOH   F .   ? 0.5107 0.7190 0.5576 -0.0583 -0.0919 0.0598  517 HOH   A O   
7118 O  O   . HOH   F .   ? 0.3007 0.4889 0.5798 0.0004  -0.0559 0.2722  518 HOH   A O   
7119 O  O   . HOH   G .   ? 0.2660 0.2248 0.3283 0.0197  0.0904  0.0416  201 HOH   B O   
7120 O  O   . HOH   G .   ? 0.3354 0.4352 0.5141 -0.0736 0.0726  -0.1809 202 HOH   B O   
7121 O  O   . HOH   G .   ? 0.4698 0.3491 0.4079 -0.0545 0.0151  -0.1337 203 HOH   B O   
7122 O  O   . HOH   G .   ? 0.3239 0.6534 0.3842 0.0347  0.0278  0.2358  204 HOH   B O   
7123 O  O   . HOH   G .   ? 0.4496 0.5388 0.3047 -0.0116 -0.0432 -0.1179 205 HOH   B O   
7124 O  O   . HOH   G .   ? 0.7034 0.3201 0.4684 0.0770  0.1073  0.0278  206 HOH   B O   
7125 O  O   . HOH   G .   ? 0.4856 0.6106 0.3737 0.2694  -0.1216 -0.0302 207 HOH   B O   
7126 O  O   . HOH   G .   ? 0.3513 0.3785 0.6588 -0.0414 0.0071  -0.0613 208 HOH   B O   
7127 O  O   . HOH   G .   ? 0.2758 0.5219 0.5224 -0.0213 0.1202  -0.2441 209 HOH   B O   
7128 O  O   . HOH   G .   ? 0.3591 0.5189 0.5030 0.2016  0.0493  -0.0137 210 HOH   B O   
7129 O  O   . HOH   G .   ? 0.1837 0.2296 0.3375 -0.0188 0.0340  0.0107  211 HOH   B O   
7130 O  O   . HOH   G .   ? 0.6118 0.5772 0.5931 0.1471  0.0793  0.0115  212 HOH   B O   
7131 O  O   . HOH   G .   ? 0.2717 0.2874 0.6998 0.0527  -0.1024 0.0726  213 HOH   B O   
7132 O  O   . HOH   G .   ? 0.4518 0.5636 0.4227 0.2635  -0.0758 0.0327  214 HOH   B O   
7133 O  O   . HOH   G .   ? 0.1657 0.2067 0.3016 -0.0155 -0.0025 0.0077  215 HOH   B O   
7134 O  O   . HOH   G .   ? 0.3122 0.2062 0.5417 0.0182  0.1744  0.0823  216 HOH   B O   
7135 O  O   . HOH   G .   ? 0.5118 0.4039 0.6037 0.0481  -0.1206 0.2476  217 HOH   B O   
7136 O  O   . HOH   G .   ? 0.4458 0.4093 0.3729 0.0061  -0.0987 0.0580  218 HOH   B O   
7137 O  O   . HOH   G .   ? 0.4608 0.4898 0.3973 0.0488  0.0742  -0.1419 219 HOH   B O   
7138 O  O   . HOH   G .   ? 0.5896 0.3222 0.4063 -0.1738 -0.0018 0.0256  220 HOH   B O   
7139 O  O   . HOH   G .   ? 0.4157 0.6325 0.3925 0.2050  0.0304  0.0056  221 HOH   B O   
7140 O  O   . HOH   G .   ? 0.4960 0.2337 0.3264 -0.0140 -0.0807 0.0107  222 HOH   B O   
7141 O  O   . HOH   G .   ? 0.3329 0.2336 0.4546 -0.0133 0.1465  0.0181  223 HOH   B O   
7142 O  O   . HOH   G .   ? 0.3214 0.3310 0.4650 0.0476  -0.0777 -0.0198 224 HOH   B O   
7143 O  O   . HOH   G .   ? 0.4657 0.4703 0.6405 0.0255  -0.1742 -0.0880 225 HOH   B O   
7144 O  O   . HOH   G .   ? 0.1812 0.2240 0.3225 -0.0139 0.0057  0.0064  226 HOH   B O   
7145 O  O   . HOH   G .   ? 0.2418 0.2393 0.4324 -0.0464 -0.0119 -0.0812 227 HOH   B O   
7146 O  O   . HOH   G .   ? 0.2460 0.2008 0.2872 -0.0268 0.1034  0.0010  228 HOH   B O   
7147 O  O   . HOH   G .   ? 0.3091 0.2531 0.6006 -0.0366 0.0497  0.0090  229 HOH   B O   
7148 O  O   . HOH   G .   ? 0.4073 0.2776 0.4124 0.0949  -0.0496 -0.0795 230 HOH   B O   
7149 O  O   . HOH   G .   ? 0.7297 0.4897 0.5133 0.2090  0.0025  -0.1171 231 HOH   B O   
7150 O  O   . HOH   G .   ? 0.4487 0.4153 0.4628 -0.1823 0.0014  0.0899  232 HOH   B O   
7151 O  O   . HOH   G .   ? 0.3553 0.1891 0.2294 0.0065  -0.0747 -0.0187 233 HOH   B O   
7152 O  O   . HOH   G .   ? 0.2195 0.2447 0.3328 -0.0464 -0.0086 -0.0318 234 HOH   B O   
7153 O  O   . HOH   G .   ? 0.2886 0.4138 0.3392 -0.0909 0.0098  -0.0226 235 HOH   B O   
7154 O  O   . HOH   G .   ? 0.2264 0.1427 0.3499 0.0079  -0.0715 -0.0099 236 HOH   B O   
7155 O  O   . HOH   G .   ? 0.5721 0.3101 0.2826 -0.0081 0.1140  -0.0333 237 HOH   B O   
7156 O  O   . HOH   G .   ? 0.3934 0.3346 0.2214 0.0548  0.0692  0.0530  238 HOH   B O   
7157 O  O   . HOH   G .   ? 0.2298 0.4179 0.2511 -0.0519 -0.0362 0.0794  239 HOH   B O   
7158 O  O   . HOH   G .   ? 0.5948 0.6287 0.3350 0.0674  0.0064  0.0517  240 HOH   B O   
7159 O  O   . HOH   G .   ? 0.5054 0.3396 0.4320 -0.2369 -0.0329 0.0304  241 HOH   B O   
7160 O  O   . HOH   G .   ? 0.2831 0.2615 0.3494 0.0381  0.0238  -0.0991 242 HOH   B O   
7161 O  O   . HOH   G .   ? 0.4972 0.3390 0.3720 -0.1374 0.0684  -0.0918 243 HOH   B O   
7162 O  O   . HOH   G .   ? 0.1610 0.1532 0.1645 -0.0156 -0.0080 -0.0023 244 HOH   B O   
7163 O  O   . HOH   G .   ? 0.2335 0.3960 0.3335 -0.0454 -0.0695 -0.0589 245 HOH   B O   
7164 O  O   . HOH   G .   ? 0.1674 0.1568 0.2853 -0.0033 -0.0024 -0.0194 246 HOH   B O   
7165 O  O   . HOH   G .   ? 0.2381 0.2089 0.2285 -0.0386 -0.0663 0.0310  247 HOH   B O   
7166 O  O   . HOH   G .   ? 0.3106 0.2545 0.3453 -0.0332 0.0027  -0.0541 248 HOH   B O   
7167 O  O   . HOH   G .   ? 0.3351 0.3868 0.2108 0.0310  0.0812  0.0276  249 HOH   B O   
7168 O  O   . HOH   G .   ? 0.1587 0.1465 0.1699 -0.0005 -0.0052 0.0066  250 HOH   B O   
7169 O  O   . HOH   G .   ? 0.3766 0.2817 0.4429 0.0605  -0.0999 -0.1261 251 HOH   B O   
7170 O  O   . HOH   G .   ? 0.2179 0.1594 0.2158 -0.0281 -0.0391 0.0259  252 HOH   B O   
7171 O  O   . HOH   G .   ? 0.3081 0.2113 0.3054 0.0699  0.0718  -0.0009 253 HOH   B O   
7172 O  O   . HOH   G .   ? 0.2538 0.2200 0.2709 0.0807  -0.0856 -0.0654 254 HOH   B O   
7173 O  O   . HOH   G .   ? 0.3192 0.1871 0.6397 -0.0101 -0.1291 -0.0421 255 HOH   B O   
7174 O  O   . HOH   G .   ? 0.2937 0.4545 0.3071 -0.0991 -0.0459 -0.0437 256 HOH   B O   
7175 O  O   . HOH   G .   ? 0.2609 0.4443 0.5687 0.0991  -0.0575 -0.1369 257 HOH   B O   
7176 O  O   . HOH   G .   ? 0.2627 0.2225 0.2114 0.0219  -0.0203 -0.0052 258 HOH   B O   
7177 O  O   . HOH   G .   ? 0.3817 0.3207 0.5299 -0.0181 0.0391  -0.1503 259 HOH   B O   
7178 O  O   . HOH   G .   ? 0.1718 0.1816 0.3069 -0.0228 -0.0228 -0.0011 260 HOH   B O   
7179 O  O   . HOH   G .   ? 0.1514 0.1827 0.2228 -0.0081 0.0059  0.0111  261 HOH   B O   
7180 O  O   . HOH   G .   ? 0.3500 0.4596 0.3422 -0.0482 -0.1195 0.0881  262 HOH   B O   
7181 O  O   . HOH   G .   ? 0.2323 0.2399 0.2165 0.0026  -0.0128 -0.0072 263 HOH   B O   
7182 O  O   . HOH   G .   ? 0.2389 0.4459 0.5770 -0.0087 0.0296  -0.1152 264 HOH   B O   
7183 O  O   . HOH   G .   ? 0.2360 0.4551 0.4811 -0.0290 -0.0032 -0.1696 265 HOH   B O   
7184 O  O   . HOH   G .   ? 0.2399 0.3244 0.2220 -0.0571 0.0322  0.0504  266 HOH   B O   
7185 O  O   . HOH   G .   ? 0.2717 0.2046 0.3070 -0.0584 0.0009  -0.0108 267 HOH   B O   
7186 O  O   . HOH   G .   ? 0.2495 0.1903 0.3678 -0.0055 -0.0426 -0.0295 268 HOH   B O   
7187 O  O   . HOH   G .   ? 0.2544 0.3468 0.3577 -0.0317 0.0361  -0.1067 269 HOH   B O   
7188 O  O   . HOH   G .   ? 0.2512 0.2859 0.2841 -0.0480 -0.0872 0.0187  270 HOH   B O   
7189 O  O   . HOH   G .   ? 0.2058 0.1954 0.1426 -0.0492 -0.0313 0.0069  271 HOH   B O   
7190 O  O   . HOH   G .   ? 0.2506 0.3889 0.4032 0.0324  0.1123  0.0439  272 HOH   B O   
7191 O  O   . HOH   G .   ? 0.2122 0.1629 0.2384 -0.0274 -0.0134 0.0125  273 HOH   B O   
7192 O  O   . HOH   G .   ? 0.2909 0.2283 0.4975 0.0035  0.0614  0.0670  274 HOH   B O   
7193 O  O   . HOH   G .   ? 0.1918 0.1600 0.3320 -0.0063 -0.0304 -0.0048 275 HOH   B O   
7194 O  O   . HOH   G .   ? 0.2527 0.2729 0.2409 -0.0359 -0.0659 -0.0422 276 HOH   B O   
7195 O  O   . HOH   G .   ? 0.4420 0.2877 0.4505 -0.0176 -0.1535 -0.0483 277 HOH   B O   
7196 O  O   . HOH   G .   ? 0.1720 0.1695 0.3557 -0.0110 0.0092  0.0066  278 HOH   B O   
7197 O  O   . HOH   G .   ? 0.2839 0.3672 0.2481 0.1199  -0.0405 -0.0177 279 HOH   B O   
7198 O  O   . HOH   G .   ? 0.5080 0.5062 0.5052 0.0653  -0.1648 -0.0019 280 HOH   B O   
7199 O  O   . HOH   G .   ? 0.2842 0.6974 0.7518 0.1609  -0.0635 -0.1310 281 HOH   B O   
7200 O  O   . HOH   G .   ? 0.1765 0.1675 0.1801 0.0030  0.0032  0.0035  282 HOH   B O   
7201 O  O   . HOH   G .   ? 0.3570 0.3988 0.4614 0.1179  -0.0551 -0.1128 283 HOH   B O   
7202 O  O   . HOH   G .   ? 0.2770 0.7006 0.2670 0.0612  -0.0502 -0.0353 284 HOH   B O   
7203 O  O   . HOH   G .   ? 0.2961 0.5093 0.5064 -0.1058 -0.1121 0.0789  285 HOH   B O   
7204 O  O   . HOH   G .   ? 0.4730 0.6124 0.2503 0.0381  -0.0868 0.1166  286 HOH   B O   
7205 O  O   . HOH   G .   ? 0.3680 0.6316 0.3565 0.1942  -0.0249 0.0955  287 HOH   B O   
7206 O  O   . HOH   G .   ? 0.3215 0.2880 0.3230 -0.0189 -0.0073 -0.1431 288 HOH   B O   
7207 O  O   . HOH   G .   ? 0.3576 0.2953 0.2321 0.0174  -0.0858 -0.0176 289 HOH   B O   
7208 O  O   . HOH   G .   ? 0.5559 0.3964 0.3299 0.2631  0.1202  0.0933  290 HOH   B O   
7209 O  O   . HOH   G .   ? 0.3726 0.2446 0.4376 -0.1032 -0.2183 0.1060  291 HOH   B O   
7210 O  O   . HOH   G .   ? 0.2509 0.2904 0.3138 0.0097  -0.0925 0.0264  292 HOH   B O   
7211 O  O   . HOH   G .   ? 0.4675 0.3893 0.2948 0.0367  -0.0141 -0.0869 293 HOH   B O   
7212 O  O   . HOH   G .   ? 0.1784 0.2167 0.1484 -0.0117 -0.0209 0.0121  294 HOH   B O   
7213 O  O   . HOH   G .   ? 0.2598 0.3466 0.4996 -0.0492 -0.1436 0.1070  295 HOH   B O   
7214 O  O   . HOH   G .   ? 0.1810 0.2129 0.3044 0.0182  -0.0023 0.0111  296 HOH   B O   
7215 O  O   . HOH   G .   ? 0.1743 0.3448 0.5065 0.0247  -0.0016 -0.1409 297 HOH   B O   
7216 O  O   . HOH   G .   ? 0.5088 0.3722 0.2441 0.1226  -0.0828 0.0224  298 HOH   B O   
7217 O  O   . HOH   G .   ? 0.3639 0.1963 0.3463 0.0653  0.1112  0.0357  299 HOH   B O   
7218 O  O   . HOH   G .   ? 0.3142 0.2855 0.5440 -0.0302 -0.1154 0.1235  300 HOH   B O   
7219 O  O   . HOH   G .   ? 0.1876 0.1745 0.2359 0.0082  0.0025  0.0203  301 HOH   B O   
7220 O  O   . HOH   G .   ? 0.4854 0.3416 0.4889 -0.0957 0.0011  0.1539  302 HOH   B O   
7221 O  O   . HOH   G .   ? 0.2162 0.1736 0.2729 -0.0290 -0.0316 -0.0013 303 HOH   B O   
7222 O  O   . HOH   G .   ? 0.4393 0.4775 0.2317 0.0213  0.0443  0.0561  304 HOH   B O   
7223 O  O   . HOH   G .   ? 0.2416 0.3067 0.4887 -0.0238 -0.0402 0.0126  305 HOH   B O   
7224 O  O   . HOH   G .   ? 0.2079 0.3005 0.6308 0.0540  -0.0459 -0.1129 306 HOH   B O   
7225 O  O   . HOH   G .   ? 0.3457 0.4623 0.7324 -0.0122 -0.0815 0.2101  307 HOH   B O   
7226 O  O   . HOH   G .   ? 0.2299 0.1743 0.3405 0.0392  -0.1032 -0.0084 308 HOH   B O   
7227 O  O   . HOH   G .   ? 0.3083 0.3253 0.4405 -0.1161 0.1173  -0.0470 309 HOH   B O   
7228 O  O   . HOH   G .   ? 0.5381 0.3093 0.2273 -0.1924 0.0909  -0.0221 310 HOH   B O   
7229 O  O   . HOH   G .   ? 0.2899 0.2864 0.3836 -0.0366 0.1088  -0.0737 311 HOH   B O   
7230 O  O   . HOH   G .   ? 0.1657 0.1586 0.3238 0.0108  -0.0044 -0.0091 312 HOH   B O   
7231 O  O   . HOH   G .   ? 0.1661 0.1933 0.3308 -0.0215 -0.0146 0.0145  313 HOH   B O   
7232 O  O   . HOH   G .   ? 0.4476 0.3034 0.5087 0.0693  0.1771  0.1501  314 HOH   B O   
7233 O  O   . HOH   G .   ? 0.2477 0.1587 0.2502 -0.0198 -0.0154 0.0321  315 HOH   B O   
7234 O  O   . HOH   G .   ? 0.6256 0.6701 0.5054 0.2975  0.0029  -0.0513 316 HOH   B O   
7235 O  O   . HOH   G .   ? 0.6368 0.4369 0.5340 0.1079  0.1387  -0.0088 317 HOH   B O   
7236 O  O   . HOH   G .   ? 0.4628 0.4750 0.2468 0.1760  -0.0564 -0.0139 318 HOH   B O   
7237 O  O   . HOH   G .   ? 0.1812 0.2935 0.2445 -0.0053 -0.0192 0.0724  319 HOH   B O   
7238 O  O   . HOH   G .   ? 0.4740 0.4882 0.2596 0.0612  -0.0547 -0.0785 320 HOH   B O   
7239 O  O   . HOH   G .   ? 0.4479 0.4262 0.5882 0.0680  -0.0032 0.0497  321 HOH   B O   
7240 O  O   . HOH   G .   ? 0.2307 0.2014 0.2007 -0.0044 0.0185  0.0220  322 HOH   B O   
7241 O  O   . HOH   G .   ? 0.1771 0.1696 0.3023 -0.0179 -0.0192 -0.0103 323 HOH   B O   
7242 O  O   . HOH   G .   ? 0.4120 0.2622 0.2840 0.1619  0.1120  0.0468  324 HOH   B O   
7243 O  O   . HOH   G .   ? 0.2334 0.5337 0.5095 -0.0449 -0.0247 -0.0481 325 HOH   B O   
7244 O  O   . HOH   G .   ? 0.6037 0.5535 0.5716 -0.1009 -0.0291 0.1461  326 HOH   B O   
7245 O  O   . HOH   G .   ? 0.8035 0.2140 0.3307 0.0097  -0.0669 0.0127  327 HOH   B O   
7246 O  O   . HOH   G .   ? 0.3095 0.2451 0.2457 0.0411  -0.0270 0.0208  328 HOH   B O   
7247 O  O   . HOH   G .   ? 0.6020 0.4790 0.6743 0.1261  -0.1231 0.1869  329 HOH   B O   
7248 O  O   . HOH   G .   ? 0.4414 0.2716 0.3166 0.0033  0.0494  0.0886  330 HOH   B O   
7249 O  O   . HOH   G .   ? 0.1970 0.2255 0.2981 0.0411  0.0326  0.0260  331 HOH   B O   
7250 O  O   . HOH   G .   ? 0.1780 0.3129 0.3377 0.0290  -0.0248 -0.0613 332 HOH   B O   
7251 O  O   . HOH   G .   ? 0.5937 0.3782 0.4042 0.0369  0.1165  0.1486  333 HOH   B O   
7252 O  O   . HOH   G .   ? 0.2818 0.2134 0.5011 -0.0077 -0.0156 0.0325  334 HOH   B O   
7253 O  O   . HOH   G .   ? 0.5738 0.4051 0.6234 -0.0264 -0.0702 -0.1071 335 HOH   B O   
7254 O  O   . HOH   G .   ? 0.1811 0.1572 0.2491 0.0101  -0.0256 0.0124  336 HOH   B O   
7255 O  O   . HOH   G .   ? 0.2383 0.2460 0.5742 -0.0532 0.0066  0.1435  337 HOH   B O   
7256 O  O   . HOH   G .   ? 0.5354 0.3628 0.4635 0.0206  0.0746  -0.1560 338 HOH   B O   
7257 O  O   . HOH   G .   ? 0.4595 0.7378 0.3959 -0.0138 -0.0329 0.2030  339 HOH   B O   
7258 O  O   . HOH   G .   ? 0.4577 0.3372 0.3470 0.0710  -0.1393 -0.0771 340 HOH   B O   
7259 O  O   . HOH   G .   ? 0.5058 0.5678 0.3575 -0.0211 -0.1211 0.0256  341 HOH   B O   
7260 O  O   . HOH   G .   ? 0.3878 0.6349 0.4197 -0.1102 -0.1108 -0.0611 342 HOH   B O   
7261 O  O   . HOH   G .   ? 0.1943 0.6154 0.6150 -0.0199 -0.0241 0.0088  343 HOH   B O   
7262 O  O   . HOH   G .   ? 0.2135 0.2107 0.2964 -0.0012 0.0450  -0.0082 344 HOH   B O   
7263 O  O   . HOH   G .   ? 0.6926 0.5622 0.2958 -0.0031 -0.0368 0.0782  345 HOH   B O   
7264 O  O   . HOH   G .   ? 0.5195 0.5404 0.4464 -0.1095 0.0077  0.1620  346 HOH   B O   
7265 O  O   . HOH   G .   ? 0.4254 0.5352 0.5769 -0.0025 -0.0908 0.1186  347 HOH   B O   
7266 O  O   . HOH   G .   ? 0.2646 0.6348 0.3649 0.1708  -0.0757 -0.1707 348 HOH   B O   
7267 O  O   . HOH   G .   ? 0.2850 0.2418 0.5365 -0.0291 -0.0869 -0.0716 349 HOH   B O   
7268 O  O   . HOH   G .   ? 0.4601 0.6013 0.6591 -0.0051 0.0289  -0.0363 350 HOH   B O   
7269 O  O   . HOH   G .   ? 0.2474 0.4223 0.5380 0.0233  0.0494  0.0160  351 HOH   B O   
7270 O  O   . HOH   G .   ? 0.3790 0.2307 0.3451 -0.0571 0.0097  -0.0709 352 HOH   B O   
7271 O  O   . HOH   G .   ? 0.3267 0.2038 0.4266 0.0473  -0.1310 -0.0625 353 HOH   B O   
7272 O  O   . HOH   G .   ? 0.3603 0.4414 0.5073 -0.1435 0.0016  -0.0600 354 HOH   B O   
7273 O  O   . HOH   G .   ? 0.4414 0.3043 0.5351 -0.1019 0.0791  0.0408  355 HOH   B O   
7274 O  O   . HOH   G .   ? 0.3553 0.2729 0.3947 -0.0778 -0.0052 -0.0429 356 HOH   B O   
7275 O  O   . HOH   G .   ? 0.5595 0.3795 0.4461 0.0867  0.1452  -0.0735 357 HOH   B O   
7276 O  O   . HOH   G .   ? 0.5153 0.4999 0.5523 -0.0494 -0.0639 0.0447  358 HOH   B O   
7277 O  O   . HOH   G .   ? 0.5345 0.3454 0.4761 -0.0042 -0.2032 -0.0255 359 HOH   B O   
7278 O  O   . HOH   G .   ? 0.4701 0.5391 0.5433 0.1698  -0.1308 0.1751  360 HOH   B O   
7279 O  O   . HOH   G .   ? 0.4720 0.6366 0.3007 0.1900  0.0127  0.0272  361 HOH   B O   
7280 O  O   . HOH   G .   ? 0.2459 0.3888 0.6990 -0.0902 -0.0579 -0.0828 362 HOH   B O   
7281 O  O   . HOH   G .   ? 0.5342 0.4386 0.5848 0.0026  0.0748  0.1525  363 HOH   B O   
7282 O  O   . HOH   G .   ? 0.5277 0.3138 0.5683 -0.1420 -0.0631 0.0177  364 HOH   B O   
7283 O  O   . HOH   G .   ? 0.5104 0.5757 0.4989 -0.0747 -0.0534 -0.1123 365 HOH   B O   
7284 O  O   . HOH   G .   ? 0.5704 0.4859 0.4462 0.0930  0.0409  0.0638  366 HOH   B O   
7285 O  O   . HOH   G .   ? 0.4763 0.3759 0.5394 0.0882  -0.1613 0.0118  367 HOH   B O   
7286 O  O   . HOH   G .   ? 0.6645 0.2282 0.3392 -0.0102 0.0268  0.0371  368 HOH   B O   
7287 O  O   . HOH   G .   ? 0.5397 0.5566 0.3712 0.1054  -0.1645 0.0553  369 HOH   B O   
7288 O  O   . HOH   G .   ? 0.4326 0.6315 0.5378 0.2875  0.0894  0.1349  370 HOH   B O   
7289 O  O   . HOH   G .   ? 0.6157 0.3714 0.3131 -0.1013 -0.0919 -0.0477 371 HOH   B O   
7290 O  O   . HOH   G .   ? 0.7610 0.7380 0.5086 0.2191  -0.1509 0.0767  372 HOH   B O   
7291 O  O   . HOH   G .   ? 0.4642 0.5295 0.4916 -0.1072 -0.0629 0.0395  373 HOH   B O   
7292 O  O   . HOH   G .   ? 0.4035 0.3941 0.3965 0.0894  -0.1579 -0.0955 374 HOH   B O   
7293 O  O   . HOH   G .   ? 0.2392 0.4844 0.4184 0.0271  -0.0464 -0.0547 375 HOH   B O   
7294 O  O   . HOH   G .   ? 0.7450 0.4382 0.5280 -0.1086 -0.0350 -0.0336 376 HOH   B O   
7295 O  O   . HOH   G .   ? 0.3371 0.4466 0.2434 0.0226  0.0474  -0.0035 377 HOH   B O   
7296 O  O   . HOH   G .   ? 0.3678 0.4954 0.5632 0.1332  -0.0298 0.0443  378 HOH   B O   
7297 O  O   . HOH   G .   ? 0.5454 0.6840 0.4572 -0.1363 -0.0120 -0.1598 379 HOH   B O   
7298 O  O   . HOH   G .   ? 0.4865 0.6694 0.6259 0.1376  0.0328  0.2489  380 HOH   B O   
7299 O  O   . HOH   G .   ? 0.3201 0.2726 0.3503 0.0132  0.0227  0.0321  381 HOH   B O   
7300 O  O   . HOH   G .   ? 0.5731 0.6496 0.6123 -0.0369 0.2166  0.1126  382 HOH   B O   
7301 O  O   . HOH   G .   ? 0.4182 0.7912 0.5547 -0.0188 0.1947  0.0865  383 HOH   B O   
7302 O  O   . HOH   G .   ? 0.6511 0.4530 0.4755 0.1496  0.1011  -0.0286 384 HOH   B O   
7303 O  O   . HOH   G .   ? 0.5462 0.5204 0.4711 0.0172  -0.0886 -0.0769 385 HOH   B O   
7304 O  O   . HOH   G .   ? 0.7034 0.5387 0.4100 0.1245  -0.0045 -0.0089 386 HOH   B O   
7305 O  O   . HOH   G .   ? 0.2579 0.4361 0.4085 -0.0826 -0.0980 -0.0407 387 HOH   B O   
7306 O  O   . HOH   G .   ? 0.5647 0.4546 0.5409 -0.0351 0.0376  -0.0043 388 HOH   B O   
7307 O  O   . HOH   G .   ? 0.4613 0.3682 0.3262 -0.0095 0.0183  -0.0411 389 HOH   B O   
7308 O  O   . HOH   G .   ? 0.3691 0.2444 0.3535 0.0721  -0.0145 0.0224  390 HOH   B O   
7309 O  O   . HOH   G .   ? 0.4860 0.4306 0.3855 0.0436  0.0765  0.0984  391 HOH   B O   
7310 O  O   . HOH   G .   ? 0.2703 0.4230 0.6413 -0.1262 -0.0729 0.0094  392 HOH   B O   
7311 O  O   . HOH   G .   ? 0.4003 0.2487 0.5287 -0.0263 0.0523  0.0495  393 HOH   B O   
7312 O  O   . HOH   G .   ? 0.4036 0.5667 0.4126 0.0797  -0.0289 -0.0968 394 HOH   B O   
7313 O  O   . HOH   G .   ? 0.4745 0.4363 0.4690 0.0481  0.1141  0.1040  395 HOH   B O   
7314 O  O   . HOH   G .   ? 0.3288 0.3608 0.4000 0.0115  -0.0009 -0.0352 396 HOH   B O   
7315 O  O   . HOH   G .   ? 0.2091 0.2949 0.5568 -0.0454 -0.0688 -0.0166 397 HOH   B O   
7316 O  O   . HOH   G .   ? 0.6037 0.6442 0.7503 0.1373  -0.1263 0.2195  398 HOH   B O   
7317 O  O   . HOH   G .   ? 0.5484 0.4371 0.3364 -0.2278 -0.0449 0.1183  399 HOH   B O   
7318 O  O   . HOH   G .   ? 0.5696 0.6303 0.3633 0.1726  0.0132  -0.0232 400 HOH   B O   
# 
