data_9BT7
# 
_entry.id   9BT7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9BT7         pdb_00009bt7 10.2210/pdb9bt7/pdb 
WWPDB D_1000284088 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'Structure model' 1 1 2025-03-26 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BT7 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu       Scott Lovell  ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 jinglese@mail.nih.gov James Inglese ? 'principal investigator/group leader' 0000-0002-7332-5717 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, L.'        1 0000-0003-0514-281X 
'Lovell, S.'     2 0000-0002-3215-4472 
'Battaile, K.P.' 3 0000-0003-0833-3259 
'Inglese, J.'    4 0000-0002-7332-5717 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Infect Dis.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2373-8227 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            11 
_citation.language                  ? 
_citation.page_first                703 
_citation.page_last                 714 
_citation.title                     
'Active- and Allosteric-Site Cyclic Peptide Inhibitors of Secreted M. tuberculosis Chorismate Mutase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsinfecdis.4c00798 
_citation.pdbx_database_id_PubMed   39903128 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'van Neer, R.H.P.' 1  ? 
primary 'Dranchak, P.K.'   2  ? 
primary 'Aitha, M.'        3  ? 
primary 'Liu, L.'          4  ? 
primary 'Carlson, E.K.'    5  ? 
primary 'Jacobsen, I.E.'   6  ? 
primary 'Battaile, K.'     7  ? 
primary 'Fang, Y.'         8  ? 
primary 'Tao, D.'          9  ? 
primary 'Rai, G.'          10 ? 
primary 'Padia, J.'        11 ? 
primary 'Lovell, S.'       12 ? 
primary 'Suga, H.'         13 ? 
primary 'Inglese, J.'      14 ? 
# 
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 'Secreted chorismate mutase'    22973.375 2   5.4.99.5 ? D34-A199 ? 
2 polymer syn 'Cyclic peptide inhibitor D1.3' 1886.120  2   ?        ? ?        ? 
3 water   nat water                           18.015    262 ?        ? ?        ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        CM,*MtCM 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;DGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEYSRF
SDWKLNPASAPPEPPDLSASRSAIDSLNNRMLSQIWSHWSLLSAPSCAAQLDRAKRDIVRSRHLDSLYQRALTTATQSYC
QALPPAGLNDIFEAQKIEWHESSGLVPRGSAAGHHHHHHHHHHEL
;
;DGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEYSRF
SDWKLNPASAPPEPPDLSASRSAIDSLNNRMLSQIWSHWSLLSAPSCAAQLDRAKRDIVRSRHLDSLYQRALTTATQSYC
QALPPAGLNDIFEAQKIEWHESSGLVPRGSAAGHHHHHHHHHHEL
;
A,B ? 
2 'polypeptide(L)' no yes '(ACE)(DTY)QFEQWHIRGRYAC' XYQFEQWHIRGRYAC C,D ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   GLY n 
1 3   THR n 
1 4   SER n 
1 5   GLN n 
1 6   LEU n 
1 7   ALA n 
1 8   GLU n 
1 9   LEU n 
1 10  VAL n 
1 11  ASP n 
1 12  ALA n 
1 13  ALA n 
1 14  ALA n 
1 15  GLU n 
1 16  ARG n 
1 17  LEU n 
1 18  GLU n 
1 19  VAL n 
1 20  ALA n 
1 21  ASP n 
1 22  PRO n 
1 23  VAL n 
1 24  ALA n 
1 25  ALA n 
1 26  PHE n 
1 27  LYS n 
1 28  TRP n 
1 29  ARG n 
1 30  ALA n 
1 31  GLN n 
1 32  LEU n 
1 33  PRO n 
1 34  ILE n 
1 35  GLU n 
1 36  ASP n 
1 37  SER n 
1 38  GLY n 
1 39  ARG n 
1 40  VAL n 
1 41  GLU n 
1 42  GLN n 
1 43  GLN n 
1 44  LEU n 
1 45  ALA n 
1 46  LYS n 
1 47  LEU n 
1 48  GLY n 
1 49  GLU n 
1 50  ASP n 
1 51  ALA n 
1 52  ARG n 
1 53  SER n 
1 54  GLN n 
1 55  HIS n 
1 56  ILE n 
1 57  ASP n 
1 58  PRO n 
1 59  ASP n 
1 60  TYR n 
1 61  VAL n 
1 62  THR n 
1 63  ARG n 
1 64  VAL n 
1 65  PHE n 
1 66  ASP n 
1 67  ASP n 
1 68  GLN n 
1 69  ILE n 
1 70  ARG n 
1 71  ALA n 
1 72  THR n 
1 73  GLU n 
1 74  ALA n 
1 75  ILE n 
1 76  GLU n 
1 77  TYR n 
1 78  SER n 
1 79  ARG n 
1 80  PHE n 
1 81  SER n 
1 82  ASP n 
1 83  TRP n 
1 84  LYS n 
1 85  LEU n 
1 86  ASN n 
1 87  PRO n 
1 88  ALA n 
1 89  SER n 
1 90  ALA n 
1 91  PRO n 
1 92  PRO n 
1 93  GLU n 
1 94  PRO n 
1 95  PRO n 
1 96  ASP n 
1 97  LEU n 
1 98  SER n 
1 99  ALA n 
1 100 SER n 
1 101 ARG n 
1 102 SER n 
1 103 ALA n 
1 104 ILE n 
1 105 ASP n 
1 106 SER n 
1 107 LEU n 
1 108 ASN n 
1 109 ASN n 
1 110 ARG n 
1 111 MET n 
1 112 LEU n 
1 113 SER n 
1 114 GLN n 
1 115 ILE n 
1 116 TRP n 
1 117 SER n 
1 118 HIS n 
1 119 TRP n 
1 120 SER n 
1 121 LEU n 
1 122 LEU n 
1 123 SER n 
1 124 ALA n 
1 125 PRO n 
1 126 SER n 
1 127 CYS n 
1 128 ALA n 
1 129 ALA n 
1 130 GLN n 
1 131 LEU n 
1 132 ASP n 
1 133 ARG n 
1 134 ALA n 
1 135 LYS n 
1 136 ARG n 
1 137 ASP n 
1 138 ILE n 
1 139 VAL n 
1 140 ARG n 
1 141 SER n 
1 142 ARG n 
1 143 HIS n 
1 144 LEU n 
1 145 ASP n 
1 146 SER n 
1 147 LEU n 
1 148 TYR n 
1 149 GLN n 
1 150 ARG n 
1 151 ALA n 
1 152 LEU n 
1 153 THR n 
1 154 THR n 
1 155 ALA n 
1 156 THR n 
1 157 GLN n 
1 158 SER n 
1 159 TYR n 
1 160 CYS n 
1 161 GLN n 
1 162 ALA n 
1 163 LEU n 
1 164 PRO n 
1 165 PRO n 
1 166 ALA n 
1 167 GLY n 
1 168 LEU n 
1 169 ASN n 
1 170 ASP n 
1 171 ILE n 
1 172 PHE n 
1 173 GLU n 
1 174 ALA n 
1 175 GLN n 
1 176 LYS n 
1 177 ILE n 
1 178 GLU n 
1 179 TRP n 
1 180 HIS n 
1 181 GLU n 
1 182 SER n 
1 183 SER n 
1 184 GLY n 
1 185 LEU n 
1 186 VAL n 
1 187 PRO n 
1 188 ARG n 
1 189 GLY n 
1 190 SER n 
1 191 ALA n 
1 192 ALA n 
1 193 GLY n 
1 194 HIS n 
1 195 HIS n 
1 196 HIS n 
1 197 HIS n 
1 198 HIS n 
1 199 HIS n 
1 200 HIS n 
1 201 HIS n 
1 202 HIS n 
1 203 HIS n 
1 204 GLU n 
1 205 LEU n 
2 1   ACE n 
2 2   DTY n 
2 3   GLN n 
2 4   PHE n 
2 5   GLU n 
2 6   GLN n 
2 7   TRP n 
2 8   HIS n 
2 9   ILE n 
2 10  ARG n 
2 11  GLY n 
2 12  ARG n 
2 13  TYR n 
2 14  ALA n 
2 15  CYS 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                   205 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Rv1885c 
_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      'Mycobacterium tuberculosis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1773 
_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                       pET21a+ 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       15 
_pdbx_entity_src_syn.organism_scientific    'Mycobacterium tuberculosis' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       1773 
_pdbx_entity_src_syn.details                ? 
# 
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 
ACE non-polymer         . 'ACETYL GROUP'  ? 'C2 H4 O'        44.053  
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
DTY 'D-peptide linking' . D-TYROSINE      ? 'C9 H11 N O3'    181.189 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
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   ASP 1   34  ?   ?   ?   A . n 
A 1 2   GLY 2   35  ?   ?   ?   A . n 
A 1 3   THR 3   36  36  THR THR A . n 
A 1 4   SER 4   37  37  SER SER A . n 
A 1 5   GLN 5   38  38  GLN GLN A . n 
A 1 6   LEU 6   39  39  LEU LEU A . n 
A 1 7   ALA 7   40  40  ALA ALA A . n 
A 1 8   GLU 8   41  41  GLU GLU A . n 
A 1 9   LEU 9   42  42  LEU LEU A . n 
A 1 10  VAL 10  43  43  VAL VAL A . n 
A 1 11  ASP 11  44  44  ASP ASP A . n 
A 1 12  ALA 12  45  45  ALA ALA A . n 
A 1 13  ALA 13  46  46  ALA ALA A . n 
A 1 14  ALA 14  47  47  ALA ALA A . n 
A 1 15  GLU 15  48  48  GLU GLU A . n 
A 1 16  ARG 16  49  49  ARG ARG A . n 
A 1 17  LEU 17  50  50  LEU LEU A . n 
A 1 18  GLU 18  51  51  GLU GLU A . n 
A 1 19  VAL 19  52  52  VAL VAL A . n 
A 1 20  ALA 20  53  53  ALA ALA A . n 
A 1 21  ASP 21  54  54  ASP ASP A . n 
A 1 22  PRO 22  55  55  PRO PRO A . n 
A 1 23  VAL 23  56  56  VAL VAL A . n 
A 1 24  ALA 24  57  57  ALA ALA A . n 
A 1 25  ALA 25  58  58  ALA ALA A . n 
A 1 26  PHE 26  59  59  PHE PHE A . n 
A 1 27  LYS 27  60  60  LYS LYS A . n 
A 1 28  TRP 28  61  61  TRP TRP A . n 
A 1 29  ARG 29  62  62  ARG ARG A . n 
A 1 30  ALA 30  63  63  ALA ALA A . n 
A 1 31  GLN 31  64  64  GLN GLN A . n 
A 1 32  LEU 32  65  65  LEU LEU A . n 
A 1 33  PRO 33  66  66  PRO PRO A . n 
A 1 34  ILE 34  67  67  ILE ILE A . n 
A 1 35  GLU 35  68  68  GLU GLU A . n 
A 1 36  ASP 36  69  69  ASP ASP A . n 
A 1 37  SER 37  70  70  SER SER A . n 
A 1 38  GLY 38  71  71  GLY GLY A . n 
A 1 39  ARG 39  72  72  ARG ARG A . n 
A 1 40  VAL 40  73  73  VAL VAL A . n 
A 1 41  GLU 41  74  74  GLU GLU A . n 
A 1 42  GLN 42  75  75  GLN GLN A . n 
A 1 43  GLN 43  76  76  GLN GLN A . n 
A 1 44  LEU 44  77  77  LEU LEU A . n 
A 1 45  ALA 45  78  78  ALA ALA A . n 
A 1 46  LYS 46  79  79  LYS LYS A . n 
A 1 47  LEU 47  80  80  LEU LEU A . n 
A 1 48  GLY 48  81  81  GLY GLY A . n 
A 1 49  GLU 49  82  82  GLU GLU A . n 
A 1 50  ASP 50  83  83  ASP ASP A . n 
A 1 51  ALA 51  84  84  ALA ALA A . n 
A 1 52  ARG 52  85  85  ARG ARG A . n 
A 1 53  SER 53  86  86  SER SER A . n 
A 1 54  GLN 54  87  87  GLN GLN A . n 
A 1 55  HIS 55  88  88  HIS HIS A . n 
A 1 56  ILE 56  89  89  ILE ILE A . n 
A 1 57  ASP 57  90  90  ASP ASP A . n 
A 1 58  PRO 58  91  91  PRO PRO A . n 
A 1 59  ASP 59  92  92  ASP ASP A . n 
A 1 60  TYR 60  93  93  TYR TYR A . n 
A 1 61  VAL 61  94  94  VAL VAL A . n 
A 1 62  THR 62  95  95  THR THR A . n 
A 1 63  ARG 63  96  96  ARG ARG A . n 
A 1 64  VAL 64  97  97  VAL VAL A . n 
A 1 65  PHE 65  98  98  PHE PHE A . n 
A 1 66  ASP 66  99  99  ASP ASP A . n 
A 1 67  ASP 67  100 100 ASP ASP A . n 
A 1 68  GLN 68  101 101 GLN GLN A . n 
A 1 69  ILE 69  102 102 ILE ILE A . n 
A 1 70  ARG 70  103 103 ARG ARG A . n 
A 1 71  ALA 71  104 104 ALA ALA A . n 
A 1 72  THR 72  105 105 THR THR A . n 
A 1 73  GLU 73  106 106 GLU GLU A . n 
A 1 74  ALA 74  107 107 ALA ALA A . n 
A 1 75  ILE 75  108 108 ILE ILE A . n 
A 1 76  GLU 76  109 109 GLU GLU A . n 
A 1 77  TYR 77  110 110 TYR TYR A . n 
A 1 78  SER 78  111 111 SER SER A . n 
A 1 79  ARG 79  112 112 ARG ARG A . n 
A 1 80  PHE 80  113 113 PHE PHE A . n 
A 1 81  SER 81  114 114 SER SER A . n 
A 1 82  ASP 82  115 115 ASP ASP A . n 
A 1 83  TRP 83  116 116 TRP TRP A . n 
A 1 84  LYS 84  117 117 LYS LYS A . n 
A 1 85  LEU 85  118 118 LEU LEU A . n 
A 1 86  ASN 86  119 119 ASN ASN A . n 
A 1 87  PRO 87  120 120 PRO PRO A . n 
A 1 88  ALA 88  121 121 ALA ALA A . n 
A 1 89  SER 89  122 122 SER SER A . n 
A 1 90  ALA 90  123 123 ALA ALA A . n 
A 1 91  PRO 91  124 124 PRO PRO A . n 
A 1 92  PRO 92  125 125 PRO PRO A . n 
A 1 93  GLU 93  126 126 GLU GLU A . n 
A 1 94  PRO 94  127 127 PRO PRO A . n 
A 1 95  PRO 95  128 128 PRO PRO A . n 
A 1 96  ASP 96  129 129 ASP ASP A . n 
A 1 97  LEU 97  130 130 LEU LEU A . n 
A 1 98  SER 98  131 131 SER SER A . n 
A 1 99  ALA 99  132 132 ALA ALA A . n 
A 1 100 SER 100 133 133 SER SER A . n 
A 1 101 ARG 101 134 134 ARG ARG A . n 
A 1 102 SER 102 135 135 SER SER A . n 
A 1 103 ALA 103 136 136 ALA ALA A . n 
A 1 104 ILE 104 137 137 ILE ILE A . n 
A 1 105 ASP 105 138 138 ASP ASP A . n 
A 1 106 SER 106 139 139 SER SER A . n 
A 1 107 LEU 107 140 140 LEU LEU A . n 
A 1 108 ASN 108 141 141 ASN ASN A . n 
A 1 109 ASN 109 142 142 ASN ASN A . n 
A 1 110 ARG 110 143 143 ARG ARG A . n 
A 1 111 MET 111 144 144 MET MET A . n 
A 1 112 LEU 112 145 145 LEU LEU A . n 
A 1 113 SER 113 146 146 SER SER A . n 
A 1 114 GLN 114 147 147 GLN GLN A . n 
A 1 115 ILE 115 148 148 ILE ILE A . n 
A 1 116 TRP 116 149 149 TRP TRP A . n 
A 1 117 SER 117 150 150 SER SER A . n 
A 1 118 HIS 118 151 151 HIS HIS A . n 
A 1 119 TRP 119 152 152 TRP TRP A . n 
A 1 120 SER 120 153 153 SER SER A . n 
A 1 121 LEU 121 154 154 LEU LEU A . n 
A 1 122 LEU 122 155 155 LEU LEU A . n 
A 1 123 SER 123 156 156 SER SER A . n 
A 1 124 ALA 124 157 157 ALA ALA A . n 
A 1 125 PRO 125 158 158 PRO PRO A . n 
A 1 126 SER 126 159 159 SER SER A . n 
A 1 127 CYS 127 160 160 CYS CYS A . n 
A 1 128 ALA 128 161 161 ALA ALA A . n 
A 1 129 ALA 129 162 162 ALA ALA A . n 
A 1 130 GLN 130 163 163 GLN GLN A . n 
A 1 131 LEU 131 164 164 LEU LEU A . n 
A 1 132 ASP 132 165 165 ASP ASP A . n 
A 1 133 ARG 133 166 166 ARG ARG A . n 
A 1 134 ALA 134 167 167 ALA ALA A . n 
A 1 135 LYS 135 168 168 LYS LYS A . n 
A 1 136 ARG 136 169 169 ARG ARG A . n 
A 1 137 ASP 137 170 170 ASP ASP A . n 
A 1 138 ILE 138 171 171 ILE ILE A . n 
A 1 139 VAL 139 172 172 VAL VAL A . n 
A 1 140 ARG 140 173 173 ARG ARG A . n 
A 1 141 SER 141 174 174 SER SER A . n 
A 1 142 ARG 142 175 175 ARG ARG A . n 
A 1 143 HIS 143 176 176 HIS HIS A . n 
A 1 144 LEU 144 177 177 LEU LEU A . n 
A 1 145 ASP 145 178 178 ASP ASP A . n 
A 1 146 SER 146 179 179 SER SER A . n 
A 1 147 LEU 147 180 180 LEU LEU A . n 
A 1 148 TYR 148 181 181 TYR TYR A . n 
A 1 149 GLN 149 182 182 GLN GLN A . n 
A 1 150 ARG 150 183 183 ARG ARG A . n 
A 1 151 ALA 151 184 184 ALA ALA A . n 
A 1 152 LEU 152 185 185 LEU LEU A . n 
A 1 153 THR 153 186 186 THR THR A . n 
A 1 154 THR 154 187 187 THR THR A . n 
A 1 155 ALA 155 188 188 ALA ALA A . n 
A 1 156 THR 156 189 189 THR THR A . n 
A 1 157 GLN 157 190 190 GLN GLN A . n 
A 1 158 SER 158 191 191 SER SER A . n 
A 1 159 TYR 159 192 192 TYR TYR A . n 
A 1 160 CYS 160 193 193 CYS CYS A . n 
A 1 161 GLN 161 194 194 GLN GLN A . n 
A 1 162 ALA 162 195 195 ALA ALA A . n 
A 1 163 LEU 163 196 196 LEU LEU A . n 
A 1 164 PRO 164 197 ?   ?   ?   A . n 
A 1 165 PRO 165 198 ?   ?   ?   A . n 
A 1 166 ALA 166 199 ?   ?   ?   A . n 
A 1 167 GLY 167 200 ?   ?   ?   A . n 
A 1 168 LEU 168 201 ?   ?   ?   A . n 
A 1 169 ASN 169 202 ?   ?   ?   A . n 
A 1 170 ASP 170 203 ?   ?   ?   A . n 
A 1 171 ILE 171 204 ?   ?   ?   A . n 
A 1 172 PHE 172 205 ?   ?   ?   A . n 
A 1 173 GLU 173 206 ?   ?   ?   A . n 
A 1 174 ALA 174 207 ?   ?   ?   A . n 
A 1 175 GLN 175 208 ?   ?   ?   A . n 
A 1 176 LYS 176 209 ?   ?   ?   A . n 
A 1 177 ILE 177 210 ?   ?   ?   A . n 
A 1 178 GLU 178 211 ?   ?   ?   A . n 
A 1 179 TRP 179 212 ?   ?   ?   A . n 
A 1 180 HIS 180 213 ?   ?   ?   A . n 
A 1 181 GLU 181 214 ?   ?   ?   A . n 
A 1 182 SER 182 215 ?   ?   ?   A . n 
A 1 183 SER 183 216 ?   ?   ?   A . n 
A 1 184 GLY 184 217 ?   ?   ?   A . n 
A 1 185 LEU 185 218 ?   ?   ?   A . n 
A 1 186 VAL 186 219 ?   ?   ?   A . n 
A 1 187 PRO 187 220 ?   ?   ?   A . n 
A 1 188 ARG 188 221 ?   ?   ?   A . n 
A 1 189 GLY 189 222 ?   ?   ?   A . n 
A 1 190 SER 190 223 ?   ?   ?   A . n 
A 1 191 ALA 191 224 ?   ?   ?   A . n 
A 1 192 ALA 192 225 ?   ?   ?   A . n 
A 1 193 GLY 193 226 ?   ?   ?   A . n 
A 1 194 HIS 194 227 ?   ?   ?   A . n 
A 1 195 HIS 195 228 ?   ?   ?   A . n 
A 1 196 HIS 196 229 ?   ?   ?   A . n 
A 1 197 HIS 197 230 ?   ?   ?   A . n 
A 1 198 HIS 198 231 ?   ?   ?   A . n 
A 1 199 HIS 199 232 ?   ?   ?   A . n 
A 1 200 HIS 200 233 ?   ?   ?   A . n 
A 1 201 HIS 201 234 ?   ?   ?   A . n 
A 1 202 HIS 202 235 ?   ?   ?   A . n 
A 1 203 HIS 203 236 ?   ?   ?   A . n 
A 1 204 GLU 204 237 ?   ?   ?   A . n 
A 1 205 LEU 205 238 ?   ?   ?   A . n 
B 1 1   ASP 1   34  ?   ?   ?   B . n 
B 1 2   GLY 2   35  ?   ?   ?   B . n 
B 1 3   THR 3   36  36  THR THR B . n 
B 1 4   SER 4   37  37  SER SER B . n 
B 1 5   GLN 5   38  38  GLN GLN B . n 
B 1 6   LEU 6   39  39  LEU LEU B . n 
B 1 7   ALA 7   40  40  ALA ALA B . n 
B 1 8   GLU 8   41  41  GLU GLU B . n 
B 1 9   LEU 9   42  42  LEU LEU B . n 
B 1 10  VAL 10  43  43  VAL VAL B . n 
B 1 11  ASP 11  44  44  ASP ASP B . n 
B 1 12  ALA 12  45  45  ALA ALA B . n 
B 1 13  ALA 13  46  46  ALA ALA B . n 
B 1 14  ALA 14  47  47  ALA ALA B . n 
B 1 15  GLU 15  48  48  GLU GLU B . n 
B 1 16  ARG 16  49  49  ARG ARG B . n 
B 1 17  LEU 17  50  50  LEU LEU B . n 
B 1 18  GLU 18  51  51  GLU GLU B . n 
B 1 19  VAL 19  52  52  VAL VAL B . n 
B 1 20  ALA 20  53  53  ALA ALA B . n 
B 1 21  ASP 21  54  54  ASP ASP B . n 
B 1 22  PRO 22  55  55  PRO PRO B . n 
B 1 23  VAL 23  56  56  VAL VAL B . n 
B 1 24  ALA 24  57  57  ALA ALA B . n 
B 1 25  ALA 25  58  58  ALA ALA B . n 
B 1 26  PHE 26  59  59  PHE PHE B . n 
B 1 27  LYS 27  60  60  LYS LYS B . n 
B 1 28  TRP 28  61  61  TRP TRP B . n 
B 1 29  ARG 29  62  62  ARG ARG B . n 
B 1 30  ALA 30  63  63  ALA ALA B . n 
B 1 31  GLN 31  64  64  GLN GLN B . n 
B 1 32  LEU 32  65  65  LEU LEU B . n 
B 1 33  PRO 33  66  66  PRO PRO B . n 
B 1 34  ILE 34  67  67  ILE ILE B . n 
B 1 35  GLU 35  68  68  GLU GLU B . n 
B 1 36  ASP 36  69  69  ASP ASP B . n 
B 1 37  SER 37  70  70  SER SER B . n 
B 1 38  GLY 38  71  71  GLY GLY B . n 
B 1 39  ARG 39  72  72  ARG ARG B . n 
B 1 40  VAL 40  73  73  VAL VAL B . n 
B 1 41  GLU 41  74  74  GLU GLU B . n 
B 1 42  GLN 42  75  75  GLN GLN B . n 
B 1 43  GLN 43  76  76  GLN GLN B . n 
B 1 44  LEU 44  77  77  LEU LEU B . n 
B 1 45  ALA 45  78  78  ALA ALA B . n 
B 1 46  LYS 46  79  79  LYS LYS B . n 
B 1 47  LEU 47  80  80  LEU LEU B . n 
B 1 48  GLY 48  81  81  GLY GLY B . n 
B 1 49  GLU 49  82  82  GLU GLU B . n 
B 1 50  ASP 50  83  83  ASP ASP B . n 
B 1 51  ALA 51  84  84  ALA ALA B . n 
B 1 52  ARG 52  85  85  ARG ARG B . n 
B 1 53  SER 53  86  86  SER SER B . n 
B 1 54  GLN 54  87  87  GLN GLN B . n 
B 1 55  HIS 55  88  88  HIS HIS B . n 
B 1 56  ILE 56  89  89  ILE ILE B . n 
B 1 57  ASP 57  90  90  ASP ASP B . n 
B 1 58  PRO 58  91  91  PRO PRO B . n 
B 1 59  ASP 59  92  92  ASP ASP B . n 
B 1 60  TYR 60  93  93  TYR TYR B . n 
B 1 61  VAL 61  94  94  VAL VAL B . n 
B 1 62  THR 62  95  95  THR THR B . n 
B 1 63  ARG 63  96  96  ARG ARG B . n 
B 1 64  VAL 64  97  97  VAL VAL B . n 
B 1 65  PHE 65  98  98  PHE PHE B . n 
B 1 66  ASP 66  99  99  ASP ASP B . n 
B 1 67  ASP 67  100 100 ASP ASP B . n 
B 1 68  GLN 68  101 101 GLN GLN B . n 
B 1 69  ILE 69  102 102 ILE ILE B . n 
B 1 70  ARG 70  103 103 ARG ARG B . n 
B 1 71  ALA 71  104 104 ALA ALA B . n 
B 1 72  THR 72  105 105 THR THR B . n 
B 1 73  GLU 73  106 106 GLU GLU B . n 
B 1 74  ALA 74  107 107 ALA ALA B . n 
B 1 75  ILE 75  108 108 ILE ILE B . n 
B 1 76  GLU 76  109 109 GLU GLU B . n 
B 1 77  TYR 77  110 110 TYR TYR B . n 
B 1 78  SER 78  111 111 SER SER B . n 
B 1 79  ARG 79  112 112 ARG ARG B . n 
B 1 80  PHE 80  113 113 PHE PHE B . n 
B 1 81  SER 81  114 114 SER SER B . n 
B 1 82  ASP 82  115 115 ASP ASP B . n 
B 1 83  TRP 83  116 116 TRP TRP B . n 
B 1 84  LYS 84  117 117 LYS LYS B . n 
B 1 85  LEU 85  118 118 LEU LEU B . n 
B 1 86  ASN 86  119 119 ASN ASN B . n 
B 1 87  PRO 87  120 120 PRO PRO B . n 
B 1 88  ALA 88  121 121 ALA ALA B . n 
B 1 89  SER 89  122 122 SER SER B . n 
B 1 90  ALA 90  123 123 ALA ALA B . n 
B 1 91  PRO 91  124 124 PRO PRO B . n 
B 1 92  PRO 92  125 125 PRO PRO B . n 
B 1 93  GLU 93  126 126 GLU GLU B . n 
B 1 94  PRO 94  127 127 PRO PRO B . n 
B 1 95  PRO 95  128 128 PRO PRO B . n 
B 1 96  ASP 96  129 129 ASP ASP B . n 
B 1 97  LEU 97  130 130 LEU LEU B . n 
B 1 98  SER 98  131 131 SER SER B . n 
B 1 99  ALA 99  132 132 ALA ALA B . n 
B 1 100 SER 100 133 133 SER SER B . n 
B 1 101 ARG 101 134 134 ARG ARG B . n 
B 1 102 SER 102 135 135 SER SER B . n 
B 1 103 ALA 103 136 136 ALA ALA B . n 
B 1 104 ILE 104 137 137 ILE ILE B . n 
B 1 105 ASP 105 138 138 ASP ASP B . n 
B 1 106 SER 106 139 139 SER SER B . n 
B 1 107 LEU 107 140 140 LEU LEU B . n 
B 1 108 ASN 108 141 141 ASN ASN B . n 
B 1 109 ASN 109 142 142 ASN ASN B . n 
B 1 110 ARG 110 143 143 ARG ARG B . n 
B 1 111 MET 111 144 144 MET MET B . n 
B 1 112 LEU 112 145 145 LEU LEU B . n 
B 1 113 SER 113 146 146 SER SER B . n 
B 1 114 GLN 114 147 147 GLN GLN B . n 
B 1 115 ILE 115 148 148 ILE ILE B . n 
B 1 116 TRP 116 149 149 TRP TRP B . n 
B 1 117 SER 117 150 150 SER SER B . n 
B 1 118 HIS 118 151 151 HIS HIS B . n 
B 1 119 TRP 119 152 152 TRP TRP B . n 
B 1 120 SER 120 153 153 SER SER B . n 
B 1 121 LEU 121 154 154 LEU LEU B . n 
B 1 122 LEU 122 155 155 LEU LEU B . n 
B 1 123 SER 123 156 156 SER SER B . n 
B 1 124 ALA 124 157 157 ALA ALA B . n 
B 1 125 PRO 125 158 158 PRO PRO B . n 
B 1 126 SER 126 159 159 SER SER B . n 
B 1 127 CYS 127 160 160 CYS CYS B . n 
B 1 128 ALA 128 161 161 ALA ALA B . n 
B 1 129 ALA 129 162 162 ALA ALA B . n 
B 1 130 GLN 130 163 163 GLN GLN B . n 
B 1 131 LEU 131 164 164 LEU LEU B . n 
B 1 132 ASP 132 165 165 ASP ASP B . n 
B 1 133 ARG 133 166 166 ARG ARG B . n 
B 1 134 ALA 134 167 167 ALA ALA B . n 
B 1 135 LYS 135 168 168 LYS LYS B . n 
B 1 136 ARG 136 169 169 ARG ARG B . n 
B 1 137 ASP 137 170 170 ASP ASP B . n 
B 1 138 ILE 138 171 171 ILE ILE B . n 
B 1 139 VAL 139 172 172 VAL VAL B . n 
B 1 140 ARG 140 173 173 ARG ARG B . n 
B 1 141 SER 141 174 174 SER SER B . n 
B 1 142 ARG 142 175 175 ARG ARG B . n 
B 1 143 HIS 143 176 176 HIS HIS B . n 
B 1 144 LEU 144 177 177 LEU LEU B . n 
B 1 145 ASP 145 178 178 ASP ASP B . n 
B 1 146 SER 146 179 179 SER SER B . n 
B 1 147 LEU 147 180 180 LEU LEU B . n 
B 1 148 TYR 148 181 181 TYR TYR B . n 
B 1 149 GLN 149 182 182 GLN GLN B . n 
B 1 150 ARG 150 183 183 ARG ARG B . n 
B 1 151 ALA 151 184 184 ALA ALA B . n 
B 1 152 LEU 152 185 185 LEU LEU B . n 
B 1 153 THR 153 186 186 THR THR B . n 
B 1 154 THR 154 187 187 THR THR B . n 
B 1 155 ALA 155 188 188 ALA ALA B . n 
B 1 156 THR 156 189 189 THR THR B . n 
B 1 157 GLN 157 190 190 GLN GLN B . n 
B 1 158 SER 158 191 191 SER SER B . n 
B 1 159 TYR 159 192 192 TYR TYR B . n 
B 1 160 CYS 160 193 193 CYS CYS B . n 
B 1 161 GLN 161 194 194 GLN GLN B . n 
B 1 162 ALA 162 195 195 ALA ALA B . n 
B 1 163 LEU 163 196 196 LEU LEU B . n 
B 1 164 PRO 164 197 ?   ?   ?   B . n 
B 1 165 PRO 165 198 ?   ?   ?   B . n 
B 1 166 ALA 166 199 ?   ?   ?   B . n 
B 1 167 GLY 167 200 ?   ?   ?   B . n 
B 1 168 LEU 168 201 ?   ?   ?   B . n 
B 1 169 ASN 169 202 ?   ?   ?   B . n 
B 1 170 ASP 170 203 ?   ?   ?   B . n 
B 1 171 ILE 171 204 ?   ?   ?   B . n 
B 1 172 PHE 172 205 ?   ?   ?   B . n 
B 1 173 GLU 173 206 ?   ?   ?   B . n 
B 1 174 ALA 174 207 ?   ?   ?   B . n 
B 1 175 GLN 175 208 ?   ?   ?   B . n 
B 1 176 LYS 176 209 ?   ?   ?   B . n 
B 1 177 ILE 177 210 ?   ?   ?   B . n 
B 1 178 GLU 178 211 ?   ?   ?   B . n 
B 1 179 TRP 179 212 ?   ?   ?   B . n 
B 1 180 HIS 180 213 ?   ?   ?   B . n 
B 1 181 GLU 181 214 ?   ?   ?   B . n 
B 1 182 SER 182 215 ?   ?   ?   B . n 
B 1 183 SER 183 216 ?   ?   ?   B . n 
B 1 184 GLY 184 217 ?   ?   ?   B . n 
B 1 185 LEU 185 218 ?   ?   ?   B . n 
B 1 186 VAL 186 219 ?   ?   ?   B . n 
B 1 187 PRO 187 220 ?   ?   ?   B . n 
B 1 188 ARG 188 221 ?   ?   ?   B . n 
B 1 189 GLY 189 222 ?   ?   ?   B . n 
B 1 190 SER 190 223 ?   ?   ?   B . n 
B 1 191 ALA 191 224 ?   ?   ?   B . n 
B 1 192 ALA 192 225 ?   ?   ?   B . n 
B 1 193 GLY 193 226 ?   ?   ?   B . n 
B 1 194 HIS 194 227 ?   ?   ?   B . n 
B 1 195 HIS 195 228 ?   ?   ?   B . n 
B 1 196 HIS 196 229 ?   ?   ?   B . n 
B 1 197 HIS 197 230 ?   ?   ?   B . n 
B 1 198 HIS 198 231 ?   ?   ?   B . n 
B 1 199 HIS 199 232 ?   ?   ?   B . n 
B 1 200 HIS 200 233 ?   ?   ?   B . n 
B 1 201 HIS 201 234 ?   ?   ?   B . n 
B 1 202 HIS 202 235 ?   ?   ?   B . n 
B 1 203 HIS 203 236 ?   ?   ?   B . n 
B 1 204 GLU 204 237 ?   ?   ?   B . n 
B 1 205 LEU 205 238 ?   ?   ?   B . n 
C 2 1   ACE 1   0   0   ACE ACE C . n 
C 2 2   DTY 2   1   1   DTY DTY C . n 
C 2 3   GLN 3   2   2   GLN GLN C . n 
C 2 4   PHE 4   3   3   PHE PHE C . n 
C 2 5   GLU 5   4   4   GLU GLU C . n 
C 2 6   GLN 6   5   5   GLN GLN C . n 
C 2 7   TRP 7   6   6   TRP TRP C . n 
C 2 8   HIS 8   7   7   HIS HIS C . n 
C 2 9   ILE 9   8   8   ILE ILE C . n 
C 2 10  ARG 10  9   9   ARG ARG C . n 
C 2 11  GLY 11  10  10  GLY GLY C . n 
C 2 12  ARG 12  11  11  ARG ARG C . n 
C 2 13  TYR 13  12  12  TYR TYR C . n 
C 2 14  ALA 14  13  13  ALA ALA C . n 
C 2 15  CYS 15  14  14  CYS CYS C . n 
D 2 1   ACE 1   0   0   ACE ACE D . n 
D 2 2   DTY 2   1   1   DTY DTY D . n 
D 2 3   GLN 3   2   2   GLN GLN D . n 
D 2 4   PHE 4   3   3   PHE PHE D . n 
D 2 5   GLU 5   4   4   GLU GLU D . n 
D 2 6   GLN 6   5   5   GLN GLN D . n 
D 2 7   TRP 7   6   6   TRP TRP D . n 
D 2 8   HIS 8   7   7   HIS HIS D . n 
D 2 9   ILE 9   8   8   ILE ILE D . n 
D 2 10  ARG 10  9   9   ARG ARG D . n 
D 2 11  GLY 11  10  10  GLY GLY D . n 
D 2 12  ARG 12  11  11  ARG ARG D . n 
D 2 13  TYR 13  12  12  TYR TYR D . n 
D 2 14  ALA 14  13  13  ALA ALA D . n 
D 2 15  CYS 15  14  14  CYS CYS D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ACE ? ? ACE ? ? 'SUBJECT OF INVESTIGATION' ? 
2 DTY ? ? DTY ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
E 3 HOH 1   301 158 HOH HOH A . 
E 3 HOH 2   302 218 HOH HOH A . 
E 3 HOH 3   303 40  HOH HOH A . 
E 3 HOH 4   304 25  HOH HOH A . 
E 3 HOH 5   305 141 HOH HOH A . 
E 3 HOH 6   306 210 HOH HOH A . 
E 3 HOH 7   307 190 HOH HOH A . 
E 3 HOH 8   308 238 HOH HOH A . 
E 3 HOH 9   309 262 HOH HOH A . 
E 3 HOH 10  310 29  HOH HOH A . 
E 3 HOH 11  311 51  HOH HOH A . 
E 3 HOH 12  312 135 HOH HOH A . 
E 3 HOH 13  313 44  HOH HOH A . 
E 3 HOH 14  314 101 HOH HOH A . 
E 3 HOH 15  315 228 HOH HOH A . 
E 3 HOH 16  316 176 HOH HOH A . 
E 3 HOH 17  317 234 HOH HOH A . 
E 3 HOH 18  318 17  HOH HOH A . 
E 3 HOH 19  319 224 HOH HOH A . 
E 3 HOH 20  320 122 HOH HOH A . 
E 3 HOH 21  321 166 HOH HOH A . 
E 3 HOH 22  322 180 HOH HOH A . 
E 3 HOH 23  323 250 HOH HOH A . 
E 3 HOH 24  324 205 HOH HOH A . 
E 3 HOH 25  325 112 HOH HOH A . 
E 3 HOH 26  326 231 HOH HOH A . 
E 3 HOH 27  327 72  HOH HOH A . 
E 3 HOH 28  328 66  HOH HOH A . 
E 3 HOH 29  329 156 HOH HOH A . 
E 3 HOH 30  330 4   HOH HOH A . 
E 3 HOH 31  331 14  HOH HOH A . 
E 3 HOH 32  332 203 HOH HOH A . 
E 3 HOH 33  333 71  HOH HOH A . 
E 3 HOH 34  334 9   HOH HOH A . 
E 3 HOH 35  335 192 HOH HOH A . 
E 3 HOH 36  336 50  HOH HOH A . 
E 3 HOH 37  337 76  HOH HOH A . 
E 3 HOH 38  338 41  HOH HOH A . 
E 3 HOH 39  339 7   HOH HOH A . 
E 3 HOH 40  340 24  HOH HOH A . 
E 3 HOH 41  341 22  HOH HOH A . 
E 3 HOH 42  342 119 HOH HOH A . 
E 3 HOH 43  343 32  HOH HOH A . 
E 3 HOH 44  344 118 HOH HOH A . 
E 3 HOH 45  345 39  HOH HOH A . 
E 3 HOH 46  346 21  HOH HOH A . 
E 3 HOH 47  347 146 HOH HOH A . 
E 3 HOH 48  348 134 HOH HOH A . 
E 3 HOH 49  349 237 HOH HOH A . 
E 3 HOH 50  350 260 HOH HOH A . 
E 3 HOH 51  351 124 HOH HOH A . 
E 3 HOH 52  352 160 HOH HOH A . 
E 3 HOH 53  353 182 HOH HOH A . 
E 3 HOH 54  354 241 HOH HOH A . 
E 3 HOH 55  355 138 HOH HOH A . 
E 3 HOH 56  356 175 HOH HOH A . 
E 3 HOH 57  357 28  HOH HOH A . 
E 3 HOH 58  358 187 HOH HOH A . 
E 3 HOH 59  359 42  HOH HOH A . 
E 3 HOH 60  360 157 HOH HOH A . 
E 3 HOH 61  361 106 HOH HOH A . 
E 3 HOH 62  362 34  HOH HOH A . 
E 3 HOH 63  363 159 HOH HOH A . 
E 3 HOH 64  364 168 HOH HOH A . 
E 3 HOH 65  365 12  HOH HOH A . 
E 3 HOH 66  366 147 HOH HOH A . 
E 3 HOH 67  367 209 HOH HOH A . 
E 3 HOH 68  368 232 HOH HOH A . 
E 3 HOH 69  369 77  HOH HOH A . 
E 3 HOH 70  370 148 HOH HOH A . 
E 3 HOH 71  371 137 HOH HOH A . 
E 3 HOH 72  372 26  HOH HOH A . 
E 3 HOH 73  373 128 HOH HOH A . 
E 3 HOH 74  374 169 HOH HOH A . 
E 3 HOH 75  375 11  HOH HOH A . 
E 3 HOH 76  376 94  HOH HOH A . 
E 3 HOH 77  377 213 HOH HOH A . 
E 3 HOH 78  378 240 HOH HOH A . 
E 3 HOH 79  379 99  HOH HOH A . 
E 3 HOH 80  380 45  HOH HOH A . 
E 3 HOH 81  381 73  HOH HOH A . 
E 3 HOH 82  382 256 HOH HOH A . 
E 3 HOH 83  383 48  HOH HOH A . 
E 3 HOH 84  384 31  HOH HOH A . 
E 3 HOH 85  385 113 HOH HOH A . 
E 3 HOH 86  386 63  HOH HOH A . 
E 3 HOH 87  387 236 HOH HOH A . 
E 3 HOH 88  388 89  HOH HOH A . 
E 3 HOH 89  389 54  HOH HOH A . 
E 3 HOH 90  390 257 HOH HOH A . 
E 3 HOH 91  391 173 HOH HOH A . 
E 3 HOH 92  392 46  HOH HOH A . 
E 3 HOH 93  393 116 HOH HOH A . 
E 3 HOH 94  394 37  HOH HOH A . 
E 3 HOH 95  395 100 HOH HOH A . 
E 3 HOH 96  396 93  HOH HOH A . 
E 3 HOH 97  397 223 HOH HOH A . 
E 3 HOH 98  398 258 HOH HOH A . 
E 3 HOH 99  399 197 HOH HOH A . 
E 3 HOH 100 400 155 HOH HOH A . 
E 3 HOH 101 401 259 HOH HOH A . 
E 3 HOH 102 402 220 HOH HOH A . 
E 3 HOH 103 403 185 HOH HOH A . 
E 3 HOH 104 404 126 HOH HOH A . 
E 3 HOH 105 405 201 HOH HOH A . 
E 3 HOH 106 406 174 HOH HOH A . 
E 3 HOH 107 407 202 HOH HOH A . 
E 3 HOH 108 408 242 HOH HOH A . 
E 3 HOH 109 409 143 HOH HOH A . 
E 3 HOH 110 410 132 HOH HOH A . 
E 3 HOH 111 411 186 HOH HOH A . 
E 3 HOH 112 412 198 HOH HOH A . 
E 3 HOH 113 413 219 HOH HOH A . 
E 3 HOH 114 414 38  HOH HOH A . 
E 3 HOH 115 415 151 HOH HOH A . 
E 3 HOH 116 416 195 HOH HOH A . 
E 3 HOH 117 417 261 HOH HOH A . 
E 3 HOH 118 418 193 HOH HOH A . 
F 3 HOH 1   301 221 HOH HOH B . 
F 3 HOH 2   302 188 HOH HOH B . 
F 3 HOH 3   303 177 HOH HOH B . 
F 3 HOH 4   304 30  HOH HOH B . 
F 3 HOH 5   305 129 HOH HOH B . 
F 3 HOH 6   306 154 HOH HOH B . 
F 3 HOH 7   307 229 HOH HOH B . 
F 3 HOH 8   308 121 HOH HOH B . 
F 3 HOH 9   309 70  HOH HOH B . 
F 3 HOH 10  310 243 HOH HOH B . 
F 3 HOH 11  311 85  HOH HOH B . 
F 3 HOH 12  312 125 HOH HOH B . 
F 3 HOH 13  313 82  HOH HOH B . 
F 3 HOH 14  314 83  HOH HOH B . 
F 3 HOH 15  315 53  HOH HOH B . 
F 3 HOH 16  316 49  HOH HOH B . 
F 3 HOH 17  317 149 HOH HOH B . 
F 3 HOH 18  318 226 HOH HOH B . 
F 3 HOH 19  319 15  HOH HOH B . 
F 3 HOH 20  320 123 HOH HOH B . 
F 3 HOH 21  321 105 HOH HOH B . 
F 3 HOH 22  322 75  HOH HOH B . 
F 3 HOH 23  323 110 HOH HOH B . 
F 3 HOH 24  324 150 HOH HOH B . 
F 3 HOH 25  325 64  HOH HOH B . 
F 3 HOH 26  326 8   HOH HOH B . 
F 3 HOH 27  327 61  HOH HOH B . 
F 3 HOH 28  328 47  HOH HOH B . 
F 3 HOH 29  329 254 HOH HOH B . 
F 3 HOH 30  330 139 HOH HOH B . 
F 3 HOH 31  331 23  HOH HOH B . 
F 3 HOH 32  332 81  HOH HOH B . 
F 3 HOH 33  333 140 HOH HOH B . 
F 3 HOH 34  334 90  HOH HOH B . 
F 3 HOH 35  335 36  HOH HOH B . 
F 3 HOH 36  336 170 HOH HOH B . 
F 3 HOH 37  337 3   HOH HOH B . 
F 3 HOH 38  338 212 HOH HOH B . 
F 3 HOH 39  339 87  HOH HOH B . 
F 3 HOH 40  340 244 HOH HOH B . 
F 3 HOH 41  341 18  HOH HOH B . 
F 3 HOH 42  342 178 HOH HOH B . 
F 3 HOH 43  343 35  HOH HOH B . 
F 3 HOH 44  344 152 HOH HOH B . 
F 3 HOH 45  345 206 HOH HOH B . 
F 3 HOH 46  346 225 HOH HOH B . 
F 3 HOH 47  347 69  HOH HOH B . 
F 3 HOH 48  348 13  HOH HOH B . 
F 3 HOH 49  349 164 HOH HOH B . 
F 3 HOH 50  350 103 HOH HOH B . 
F 3 HOH 51  351 239 HOH HOH B . 
F 3 HOH 52  352 88  HOH HOH B . 
F 3 HOH 53  353 130 HOH HOH B . 
F 3 HOH 54  354 43  HOH HOH B . 
F 3 HOH 55  355 79  HOH HOH B . 
F 3 HOH 56  356 92  HOH HOH B . 
F 3 HOH 57  357 214 HOH HOH B . 
F 3 HOH 58  358 222 HOH HOH B . 
F 3 HOH 59  359 208 HOH HOH B . 
F 3 HOH 60  360 217 HOH HOH B . 
F 3 HOH 61  361 1   HOH HOH B . 
F 3 HOH 62  362 102 HOH HOH B . 
F 3 HOH 63  363 33  HOH HOH B . 
F 3 HOH 64  364 133 HOH HOH B . 
F 3 HOH 65  365 245 HOH HOH B . 
F 3 HOH 66  366 165 HOH HOH B . 
F 3 HOH 67  367 60  HOH HOH B . 
F 3 HOH 68  368 233 HOH HOH B . 
F 3 HOH 69  369 56  HOH HOH B . 
F 3 HOH 70  370 78  HOH HOH B . 
F 3 HOH 71  371 117 HOH HOH B . 
F 3 HOH 72  372 153 HOH HOH B . 
F 3 HOH 73  373 163 HOH HOH B . 
F 3 HOH 74  374 127 HOH HOH B . 
F 3 HOH 75  375 62  HOH HOH B . 
F 3 HOH 76  376 215 HOH HOH B . 
F 3 HOH 77  377 74  HOH HOH B . 
F 3 HOH 78  378 97  HOH HOH B . 
F 3 HOH 79  379 235 HOH HOH B . 
F 3 HOH 80  380 211 HOH HOH B . 
F 3 HOH 81  381 27  HOH HOH B . 
F 3 HOH 82  382 145 HOH HOH B . 
F 3 HOH 83  383 248 HOH HOH B . 
F 3 HOH 84  384 179 HOH HOH B . 
F 3 HOH 85  385 253 HOH HOH B . 
F 3 HOH 86  386 104 HOH HOH B . 
F 3 HOH 87  387 247 HOH HOH B . 
F 3 HOH 88  388 161 HOH HOH B . 
F 3 HOH 89  389 114 HOH HOH B . 
F 3 HOH 90  390 207 HOH HOH B . 
F 3 HOH 91  391 59  HOH HOH B . 
F 3 HOH 92  392 95  HOH HOH B . 
F 3 HOH 93  393 2   HOH HOH B . 
F 3 HOH 94  394 230 HOH HOH B . 
F 3 HOH 95  395 251 HOH HOH B . 
F 3 HOH 96  396 189 HOH HOH B . 
F 3 HOH 97  397 181 HOH HOH B . 
F 3 HOH 98  398 142 HOH HOH B . 
F 3 HOH 99  399 131 HOH HOH B . 
F 3 HOH 100 400 162 HOH HOH B . 
F 3 HOH 101 401 55  HOH HOH B . 
F 3 HOH 102 402 204 HOH HOH B . 
F 3 HOH 103 403 196 HOH HOH B . 
F 3 HOH 104 404 115 HOH HOH B . 
F 3 HOH 105 405 91  HOH HOH B . 
F 3 HOH 106 406 96  HOH HOH B . 
F 3 HOH 107 407 58  HOH HOH B . 
F 3 HOH 108 408 199 HOH HOH B . 
F 3 HOH 109 409 249 HOH HOH B . 
F 3 HOH 110 410 172 HOH HOH B . 
F 3 HOH 111 411 216 HOH HOH B . 
F 3 HOH 112 412 246 HOH HOH B . 
F 3 HOH 113 413 194 HOH HOH B . 
F 3 HOH 114 414 68  HOH HOH B . 
F 3 HOH 115 415 200 HOH HOH B . 
G 3 HOH 1   101 16  HOH HOH C . 
G 3 HOH 2   102 184 HOH HOH C . 
G 3 HOH 3   103 171 HOH HOH C . 
G 3 HOH 4   104 98  HOH HOH C . 
G 3 HOH 5   105 111 HOH HOH C . 
G 3 HOH 6   106 6   HOH HOH C . 
G 3 HOH 7   107 144 HOH HOH C . 
G 3 HOH 8   108 86  HOH HOH C . 
G 3 HOH 9   109 183 HOH HOH C . 
G 3 HOH 10  110 255 HOH HOH C . 
G 3 HOH 11  111 5   HOH HOH C . 
G 3 HOH 12  112 120 HOH HOH C . 
G 3 HOH 13  113 67  HOH HOH C . 
G 3 HOH 14  114 108 HOH HOH C . 
G 3 HOH 15  115 107 HOH HOH C . 
G 3 HOH 16  116 191 HOH HOH C . 
H 3 HOH 1   101 167 HOH HOH D . 
H 3 HOH 2   102 80  HOH HOH D . 
H 3 HOH 3   103 52  HOH HOH D . 
H 3 HOH 4   104 10  HOH HOH D . 
H 3 HOH 5   105 19  HOH HOH D . 
H 3 HOH 6   106 227 HOH HOH D . 
H 3 HOH 7   107 20  HOH HOH D . 
H 3 HOH 8   108 57  HOH HOH D . 
H 3 HOH 9   109 65  HOH HOH D . 
H 3 HOH 10  110 136 HOH HOH D . 
H 3 HOH 11  111 84  HOH HOH D . 
H 3 HOH 12  112 252 HOH HOH D . 
H 3 HOH 13  113 109 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ARG 62 ? CD  ? A ARG 29 CD  
2 1 Y 1 A ARG 62 ? NE  ? A ARG 29 NE  
3 1 Y 1 A ARG 62 ? CZ  ? A ARG 29 CZ  
4 1 Y 1 A ARG 62 ? NH1 ? A ARG 29 NH1 
5 1 Y 1 A ARG 62 ? NH2 ? A ARG 29 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BT7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     70.186 
_cell.length_a_esd                 ? 
_cell.length_b                     71.102 
_cell.length_b_esd                 ? 
_cell.length_c                     71.603 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BT7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BT7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.80 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          31.54 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;JCSG+ H7: (25% (w/v) PEG 3350, 0.1 M Bis-Tris pH 5.5, 0.2M Ammonium Sulfate), chorismate mutase at 10 mg/mL. plate 12878, well H7 drop 2. Puck: PSL-0513, Cryo: 80% crystallant and 20% PEG 200 .
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-02-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Double Crystal Si 111' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BT7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               71.60 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     33927 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.216 
_reflns.pdbx_Rpim_I_all                                0.069 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       315844 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.204 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.85 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           22687 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2458 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               9.2 
_reflns_shell.pdbx_chi_squared                              1.01 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.4 
_reflns_shell.pdbx_Rrim_I_all                               1.720 
_reflns_shell.pdbx_Rpim_I_all                               0.557 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.636 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.625 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BT7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             49.95 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     33845 
_refine.ls_number_reflns_R_free                  1785 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_percent_reflns_R_free                 5.27 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1773 
_refine.ls_R_factor_R_free                       0.2082 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1756 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.16 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        49.95 
_refine_hist.number_atoms_solvent             262 
_refine_hist.number_atoms_total               3067 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2805 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 2928 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.786  ? 3992 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.807 ? 1105 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047  ? 429  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 534  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.85  . . 184 2367 100.00 . . . . 0.2852 . . . . . . . . . . . 0.3456 
'X-RAY DIFFRACTION' 1.85 1.90  . . 132 2430 100.00 . . . . 0.2335 . . . . . . . . . . . 0.2964 
'X-RAY DIFFRACTION' 1.90 1.96  . . 126 2446 100.00 . . . . 0.2072 . . . . . . . . . . . 0.2306 
'X-RAY DIFFRACTION' 1.96 2.03  . . 134 2430 100.00 . . . . 0.1908 . . . . . . . . . . . 0.2364 
'X-RAY DIFFRACTION' 2.03 2.12  . . 93  2484 100.00 . . . . 0.1816 . . . . . . . . . . . 0.2175 
'X-RAY DIFFRACTION' 2.12 2.21  . . 104 2476 100.00 . . . . 0.1777 . . . . . . . . . . . 0.2455 
'X-RAY DIFFRACTION' 2.21 2.33  . . 167 2412 100.00 . . . . 0.1622 . . . . . . . . . . . 0.2043 
'X-RAY DIFFRACTION' 2.33 2.48  . . 168 2421 100.00 . . . . 0.1662 . . . . . . . . . . . 0.1959 
'X-RAY DIFFRACTION' 2.48 2.67  . . 119 2493 100.00 . . . . 0.1686 . . . . . . . . . . . 0.2334 
'X-RAY DIFFRACTION' 2.67 2.93  . . 124 2480 100.00 . . . . 0.1760 . . . . . . . . . . . 0.2134 
'X-RAY DIFFRACTION' 2.93 3.36  . . 125 2508 100.00 . . . . 0.1766 . . . . . . . . . . . 0.2095 
'X-RAY DIFFRACTION' 3.36 4.23  . . 151 2505 100.00 . . . . 0.1537 . . . . . . . . . . . 0.1736 
'X-RAY DIFFRACTION' 4.23 49.95 . . 158 2608 99.00  . . . . 0.1679 . . . . . . . . . . . 0.1761 
# 
_struct.entry_id                     9BT7 
_struct.title                        
'Crystal structure of Chorismate Mutase from Mycobacterium tuberculosis in complex with the cyclic peptide inhibitor D1.3' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BT7 
_struct_keywords.text            'Chorismate Mutase, Mycobacterium tuberculosis, cyclic peptide inhibitor, ISOMERASE' 
_struct_keywords.pdbx_keywords   ISOMERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SCMU_MYCTU P9WIB9 ? 1 
;DGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEYSRF
SDWKLNPASAPPEPPDLSASRSAIDSLNNRMLSQIWSHWSLLSAPSCAAQLDRAKRDIVRSRHLDSLYQRALTTATQSYC
QALPPA
;
34 
2 PDB 9BT7       9BT7   ? 2 ? 1  
# 
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 9BT7 A 1 ? 166 ? P9WIB9 34 ? 199 ? 34 199 
2 1 9BT7 B 1 ? 166 ? P9WIB9 34 ? 199 ? 34 199 
3 2 9BT7 C 1 ? 15  ? 9BT7   0  ? 14  ? 0  14  
4 2 9BT7 D 1 ? 15  ? 9BT7   0  ? 14  ? 0  14  
# 
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 9BT7 GLY A 167 ? UNP P9WIB9 ? ? 'expression tag' 200 1  
1 9BT7 LEU A 168 ? UNP P9WIB9 ? ? 'expression tag' 201 2  
1 9BT7 ASN A 169 ? UNP P9WIB9 ? ? 'expression tag' 202 3  
1 9BT7 ASP A 170 ? UNP P9WIB9 ? ? 'expression tag' 203 4  
1 9BT7 ILE A 171 ? UNP P9WIB9 ? ? 'expression tag' 204 5  
1 9BT7 PHE A 172 ? UNP P9WIB9 ? ? 'expression tag' 205 6  
1 9BT7 GLU A 173 ? UNP P9WIB9 ? ? 'expression tag' 206 7  
1 9BT7 ALA A 174 ? UNP P9WIB9 ? ? 'expression tag' 207 8  
1 9BT7 GLN A 175 ? UNP P9WIB9 ? ? 'expression tag' 208 9  
1 9BT7 LYS A 176 ? UNP P9WIB9 ? ? 'expression tag' 209 10 
1 9BT7 ILE A 177 ? UNP P9WIB9 ? ? 'expression tag' 210 11 
1 9BT7 GLU A 178 ? UNP P9WIB9 ? ? 'expression tag' 211 12 
1 9BT7 TRP A 179 ? UNP P9WIB9 ? ? 'expression tag' 212 13 
1 9BT7 HIS A 180 ? UNP P9WIB9 ? ? 'expression tag' 213 14 
1 9BT7 GLU A 181 ? UNP P9WIB9 ? ? 'expression tag' 214 15 
1 9BT7 SER A 182 ? UNP P9WIB9 ? ? 'expression tag' 215 16 
1 9BT7 SER A 183 ? UNP P9WIB9 ? ? 'expression tag' 216 17 
1 9BT7 GLY A 184 ? UNP P9WIB9 ? ? 'expression tag' 217 18 
1 9BT7 LEU A 185 ? UNP P9WIB9 ? ? 'expression tag' 218 19 
1 9BT7 VAL A 186 ? UNP P9WIB9 ? ? 'expression tag' 219 20 
1 9BT7 PRO A 187 ? UNP P9WIB9 ? ? 'expression tag' 220 21 
1 9BT7 ARG A 188 ? UNP P9WIB9 ? ? 'expression tag' 221 22 
1 9BT7 GLY A 189 ? UNP P9WIB9 ? ? 'expression tag' 222 23 
1 9BT7 SER A 190 ? UNP P9WIB9 ? ? 'expression tag' 223 24 
1 9BT7 ALA A 191 ? UNP P9WIB9 ? ? 'expression tag' 224 25 
1 9BT7 ALA A 192 ? UNP P9WIB9 ? ? 'expression tag' 225 26 
1 9BT7 GLY A 193 ? UNP P9WIB9 ? ? 'expression tag' 226 27 
1 9BT7 HIS A 194 ? UNP P9WIB9 ? ? 'expression tag' 227 28 
1 9BT7 HIS A 195 ? UNP P9WIB9 ? ? 'expression tag' 228 29 
1 9BT7 HIS A 196 ? UNP P9WIB9 ? ? 'expression tag' 229 30 
1 9BT7 HIS A 197 ? UNP P9WIB9 ? ? 'expression tag' 230 31 
1 9BT7 HIS A 198 ? UNP P9WIB9 ? ? 'expression tag' 231 32 
1 9BT7 HIS A 199 ? UNP P9WIB9 ? ? 'expression tag' 232 33 
1 9BT7 HIS A 200 ? UNP P9WIB9 ? ? 'expression tag' 233 34 
1 9BT7 HIS A 201 ? UNP P9WIB9 ? ? 'expression tag' 234 35 
1 9BT7 HIS A 202 ? UNP P9WIB9 ? ? 'expression tag' 235 36 
1 9BT7 HIS A 203 ? UNP P9WIB9 ? ? 'expression tag' 236 37 
1 9BT7 GLU A 204 ? UNP P9WIB9 ? ? 'expression tag' 237 38 
1 9BT7 LEU A 205 ? UNP P9WIB9 ? ? 'expression tag' 238 39 
2 9BT7 GLY B 167 ? UNP P9WIB9 ? ? 'expression tag' 200 40 
2 9BT7 LEU B 168 ? UNP P9WIB9 ? ? 'expression tag' 201 41 
2 9BT7 ASN B 169 ? UNP P9WIB9 ? ? 'expression tag' 202 42 
2 9BT7 ASP B 170 ? UNP P9WIB9 ? ? 'expression tag' 203 43 
2 9BT7 ILE B 171 ? UNP P9WIB9 ? ? 'expression tag' 204 44 
2 9BT7 PHE B 172 ? UNP P9WIB9 ? ? 'expression tag' 205 45 
2 9BT7 GLU B 173 ? UNP P9WIB9 ? ? 'expression tag' 206 46 
2 9BT7 ALA B 174 ? UNP P9WIB9 ? ? 'expression tag' 207 47 
2 9BT7 GLN B 175 ? UNP P9WIB9 ? ? 'expression tag' 208 48 
2 9BT7 LYS B 176 ? UNP P9WIB9 ? ? 'expression tag' 209 49 
2 9BT7 ILE B 177 ? UNP P9WIB9 ? ? 'expression tag' 210 50 
2 9BT7 GLU B 178 ? UNP P9WIB9 ? ? 'expression tag' 211 51 
2 9BT7 TRP B 179 ? UNP P9WIB9 ? ? 'expression tag' 212 52 
2 9BT7 HIS B 180 ? UNP P9WIB9 ? ? 'expression tag' 213 53 
2 9BT7 GLU B 181 ? UNP P9WIB9 ? ? 'expression tag' 214 54 
2 9BT7 SER B 182 ? UNP P9WIB9 ? ? 'expression tag' 215 55 
2 9BT7 SER B 183 ? UNP P9WIB9 ? ? 'expression tag' 216 56 
2 9BT7 GLY B 184 ? UNP P9WIB9 ? ? 'expression tag' 217 57 
2 9BT7 LEU B 185 ? UNP P9WIB9 ? ? 'expression tag' 218 58 
2 9BT7 VAL B 186 ? UNP P9WIB9 ? ? 'expression tag' 219 59 
2 9BT7 PRO B 187 ? UNP P9WIB9 ? ? 'expression tag' 220 60 
2 9BT7 ARG B 188 ? UNP P9WIB9 ? ? 'expression tag' 221 61 
2 9BT7 GLY B 189 ? UNP P9WIB9 ? ? 'expression tag' 222 62 
2 9BT7 SER B 190 ? UNP P9WIB9 ? ? 'expression tag' 223 63 
2 9BT7 ALA B 191 ? UNP P9WIB9 ? ? 'expression tag' 224 64 
2 9BT7 ALA B 192 ? UNP P9WIB9 ? ? 'expression tag' 225 65 
2 9BT7 GLY B 193 ? UNP P9WIB9 ? ? 'expression tag' 226 66 
2 9BT7 HIS B 194 ? UNP P9WIB9 ? ? 'expression tag' 227 67 
2 9BT7 HIS B 195 ? UNP P9WIB9 ? ? 'expression tag' 228 68 
2 9BT7 HIS B 196 ? UNP P9WIB9 ? ? 'expression tag' 229 69 
2 9BT7 HIS B 197 ? UNP P9WIB9 ? ? 'expression tag' 230 70 
2 9BT7 HIS B 198 ? UNP P9WIB9 ? ? 'expression tag' 231 71 
2 9BT7 HIS B 199 ? UNP P9WIB9 ? ? 'expression tag' 232 72 
2 9BT7 HIS B 200 ? UNP P9WIB9 ? ? 'expression tag' 233 73 
2 9BT7 HIS B 201 ? UNP P9WIB9 ? ? 'expression tag' 234 74 
2 9BT7 HIS B 202 ? UNP P9WIB9 ? ? 'expression tag' 235 75 
2 9BT7 HIS B 203 ? UNP P9WIB9 ? ? 'expression tag' 236 76 
2 9BT7 GLU B 204 ? UNP P9WIB9 ? ? 'expression tag' 237 77 
2 9BT7 LEU B 205 ? UNP P9WIB9 ? ? 'expression tag' 238 78 
# 
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_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1270 ? 
1 MORE         -5   ? 
1 'SSA (A^2)'  9310 ? 
2 'ABSA (A^2)' 1290 ? 
2 MORE         -5   ? 
2 'SSA (A^2)'  9350 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,H 
2 1 B,C,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 LEU A 6   ? GLU A 18  ? LEU A 39  GLU A 51  1 ? 13 
HELX_P HELX_P2  AA2 VAL A 19  ? GLN A 31  ? VAL A 52  GLN A 64  1 ? 13 
HELX_P HELX_P3  AA3 ASP A 36  ? GLN A 54  ? ASP A 69  GLN A 87  1 ? 19 
HELX_P HELX_P4  AA4 ASP A 57  ? ASN A 86  ? ASP A 90  ASN A 119 1 ? 30 
HELX_P HELX_P5  AA5 PRO A 87  ? ALA A 90  ? PRO A 120 ALA A 123 5 ? 4  
HELX_P HELX_P6  AA6 LEU A 97  ? HIS A 118 ? LEU A 130 HIS A 151 1 ? 22 
HELX_P HELX_P7  AA7 HIS A 118 ? SER A 123 ? HIS A 151 SER A 156 1 ? 6  
HELX_P HELX_P8  AA8 SER A 126 ? ARG A 142 ? SER A 159 ARG A 175 1 ? 17 
HELX_P HELX_P9  AA9 ASP A 145 ? GLN A 157 ? ASP A 178 GLN A 190 1 ? 13 
HELX_P HELX_P10 AB1 SER A 158 ? ALA A 162 ? SER A 191 ALA A 195 5 ? 5  
HELX_P HELX_P11 AB2 LEU B 6   ? GLU B 18  ? LEU B 39  GLU B 51  1 ? 13 
HELX_P HELX_P12 AB3 VAL B 19  ? GLN B 31  ? VAL B 52  GLN B 64  1 ? 13 
HELX_P HELX_P13 AB4 ASP B 36  ? GLN B 54  ? ASP B 69  GLN B 87  1 ? 19 
HELX_P HELX_P14 AB5 ASP B 57  ? ASN B 86  ? ASP B 90  ASN B 119 1 ? 30 
HELX_P HELX_P15 AB6 PRO B 87  ? ALA B 90  ? PRO B 120 ALA B 123 5 ? 4  
HELX_P HELX_P16 AB7 LEU B 97  ? HIS B 118 ? LEU B 130 HIS B 151 1 ? 22 
HELX_P HELX_P17 AB8 HIS B 118 ? SER B 123 ? HIS B 151 SER B 156 1 ? 6  
HELX_P HELX_P18 AB9 SER B 126 ? ARG B 142 ? SER B 159 ARG B 175 1 ? 17 
HELX_P HELX_P19 AC1 ASP B 145 ? GLN B 157 ? ASP B 178 GLN B 190 1 ? 13 
HELX_P HELX_P20 AC2 SER B 158 ? ALA B 162 ? SER B 191 ALA B 195 5 ? 5  
HELX_P HELX_P21 AC3 HIS C 8   ? TYR C 13  ? HIS C 7   TYR C 12  5 ? 6  
HELX_P HELX_P22 AC4 HIS D 8   ? TYR D 13  ? HIS D 7   TYR D 12  5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 127 SG  ? ? ? 1_555 A CYS 160 SG ? ? A CYS 160 A CYS 193 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
disulf2 disulf ?    ? B CYS 127 SG  ? ? ? 1_555 B CYS 160 SG ? ? B CYS 160 B CYS 193 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
covale1 covale both ? C ACE 1   C   ? ? ? 1_555 C DTY 2   N  ? ? C ACE 0   C DTY 1   1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale2 covale none ? C ACE 1   CH3 ? ? ? 1_555 C CYS 15  SG ? ? C ACE 0   C CYS 14  1_555 ? ? ? ? ? ? ? 1.815 ? ? 
covale3 covale both ? C DTY 2   C   ? ? ? 1_555 C GLN 3   N  ? ? C DTY 1   C GLN 2   1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale4 covale both ? D ACE 1   C   ? ? ? 1_555 D DTY 2   N  ? ? D ACE 0   D DTY 1   1_555 ? ? ? ? ? ? ? 1.341 ? ? 
covale5 covale none ? D ACE 1   CH3 ? ? ? 1_555 D CYS 15  SG ? ? D ACE 0   D CYS 14  1_555 ? ? ? ? ? ? ? 1.816 ? ? 
covale6 covale both ? D DTY 2   C   ? ? ? 1_555 D GLN 3   N  ? ? D DTY 1   D GLN 2   1_555 ? ? ? ? ? ? ? 1.333 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE C 1   ? DTY C 2   ? ACE C 0   ? 1_555 DTY C 1   ? 1_555 .   .  DTY 24 ACE None 'Terminal acetylation' 
2 ACE D 1   ? DTY D 2   ? ACE D 0   ? 1_555 DTY D 1   ? 1_555 .   .  DTY 24 ACE None 'Terminal acetylation' 
3 CYS A 127 ? CYS A 160 ? CYS A 160 ? 1_555 CYS A 193 ? 1_555 SG  SG .   .  .   None 'Disulfide bridge'     
4 CYS B 127 ? CYS B 160 ? CYS B 160 ? 1_555 CYS B 193 ? 1_555 SG  SG .   .  .   None 'Disulfide bridge'     
5 ACE C 1   ? CYS C 15  ? ACE C 0   ? 1_555 CYS C 14  ? 1_555 CH3 SG .   .  .   None 'Non-standard linkage' 
6 ACE D 1   ? CYS D 15  ? ACE D 0   ? 1_555 CYS D 14  ? 1_555 CH3 SG .   .  .   None 'Non-standard linkage' 
# 
_pdbx_entry_details.entry_id                   9BT7 
_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   Y 
# 
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 ASP A 69  ? ? -150.21 87.40   
2 1 CYS A 193 ? ? -87.12  48.42   
3 1 TYR C 12  ? ? -121.18 -153.30 
4 1 PHE D 3   ? ? -172.57 149.15  
5 1 TYR D 12  ? ? -121.87 -154.41 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 21.8930 28.4078  7.5613  0.1255 ? -0.0256 ? -0.0104 ? 0.1450 ? -0.0200 ? 0.1547 ? 1.4715 ? 
-1.3158 ? -0.1127 ? 2.0122 ? -0.0995 ? 0.5250 ? 0.0218  ? 0.0920  ? 0.1076  ? -0.0825 ? -0.0582 ? -0.2378 ? -0.0426 ? 0.0694  ? 
0.0211  ? 
2  'X-RAY DIFFRACTION' ? refined 20.1100 39.2454  21.5181 0.2112 ? -0.0085 ? -0.0262 ? 0.2325 ? -0.0301 ? 0.1735 ? 0.8409 ? 
-0.2745 ? 0.5415  ? 5.9170 ? -1.7112 ? 1.3888 ? -0.0885 ? 0.0143  ? 0.0496  ? 0.3811  ? 0.0965  ? -0.4345 ? -0.1956 ? 0.1166  ? 
-0.0455 ? 
3  'X-RAY DIFFRACTION' ? refined 21.0125 22.8889  10.6008 0.1248 ? -0.0132 ? -0.0035 ? 0.1673 ? -0.0044 ? 0.1392 ? 0.0231 ? 
-0.1357 ? 0.0966  ? 1.8887 ? 0.0237  ? 0.5941 ? -0.0053 ? 0.0049  ? 0.0184  ? -0.0713 ? 0.0107  ? -0.1013 ? -0.0430 ? 0.0399  ? 
-0.0207 ? 
4  'X-RAY DIFFRACTION' ? refined 18.7361 41.4230  9.8015  0.1598 ? -0.0042 ? 0.0047  ? 0.1330 ? -0.0085 ? 0.1542 ? 2.4736 ? 
-0.7972 ? 0.5214  ? 1.5945 ? -0.0924 ? 1.2558 ? 0.0347  ? -0.0016 ? 0.0407  ? 0.1053  ? -0.0340 ? 0.0161  ? -0.1562 ? 0.0538  ? 
-0.0009 ? 
5  'X-RAY DIFFRACTION' ? refined 6.6498  36.5279  -1.1182 0.1706 ? 0.0085  ? -0.0339 ? 0.2316 ? 0.0059  ? 0.1812 ? 4.5636 ? 
-3.5816 ? -3.5425 ? 3.0894 ? 2.5458  ? 2.9418 ? 0.2908  ? 0.4195  ? -0.0743 ? -0.4226 ? -0.3180 ? 0.3209  ? -0.4266 ? -0.3636 ? 
0.0429  ? 
6  'X-RAY DIFFRACTION' ? refined 10.8728 30.0189  5.3938  0.1569 ? -0.0087 ? -0.0056 ? 0.1614 ? 0.0072  ? 0.1118 ? 1.3864 ? 0.1711 
? 0.2917  ? 2.2057 ? 0.0512  ? 1.5209 ? 0.1017  ? 0.0362  ? -0.0267 ? 0.0750  ? -0.1166 ? 0.0769  ? 0.0288  ? -0.2569 ? 0.0276  ? 
7  'X-RAY DIFFRACTION' ? refined 13.3741 1.8264   15.6783 0.1519 ? -0.0054 ? 0.0031  ? 0.1553 ? 0.0228  ? 0.1665 ? 0.5836 ? 
-0.4625 ? -0.0368 ? 2.6677 ? 1.4398  ? 1.5242 ? -0.0298 ? -0.0153 ? -0.0843 ? 0.0241  ? -0.0606 ? 0.3170  ? 0.0296  ? -0.0173 ? 
0.0541  ? 
8  'X-RAY DIFFRACTION' ? refined 26.5910 -8.5093  20.4542 0.1477 ? -0.0040 ? -0.0065 ? 0.1909 ? 0.0101  ? 0.1722 ? 1.1314 ? 1.0800 
? 0.5701  ? 5.9768 ? 0.6470  ? 1.2381 ? 0.1502  ? -0.0916 ? -0.1911 ? 0.4521  ? -0.2256 ? 0.0921  ? 0.2025  ? -0.0302 ? 0.0887  ? 
9  'X-RAY DIFFRACTION' ? refined 16.2695 6.1999   14.7263 0.1293 ? -0.0141 ? 0.0071  ? 0.1634 ? -0.0010 ? 0.1711 ? 0.3999 ? 
-0.7182 ? 0.2530  ? 1.7937 ? -0.1265 ? 0.3548 ? -0.0388 ? -0.0446 ? -0.0939 ? 0.0635  ? 0.0608  ? 0.1714  ? 0.0180  ? -0.0472 ? 
-0.0157 ? 
10 'X-RAY DIFFRACTION' ? refined 17.1190 -11.8987 14.9669 0.1488 ? -0.0056 ? -0.0082 ? 0.1409 ? 0.0118  ? 0.1610 ? 1.9325 ? 
-1.2209 ? -0.8281 ? 2.6392 ? 0.6404  ? 2.9694 ? 0.0242  ? -0.0484 ? -0.0283 ? 0.1968  ? 0.0299  ? 0.1007  ? 0.2488  ? -0.0092 ? 
-0.0978 ? 
11 'X-RAY DIFFRACTION' ? refined 12.6213 -9.4285  -1.7875 0.2060 ? -0.0113 ? -0.0464 ? 0.1921 ? -0.0305 ? 0.1506 ? 3.3334 ? 
-2.3570 ? -1.4028 ? 2.8196 ? 1.2591  ? 1.9971 ? 0.0436  ? 0.6174  ? -0.1883 ? -0.1374 ? -0.2767 ? 0.2561  ? 0.1177  ? -0.3229 ? 
0.1526  ? 
12 'X-RAY DIFFRACTION' ? refined 16.3774 -2.1168  4.0393  0.1706 ? -0.0156 ? -0.0219 ? 0.1617 ? -0.0033 ? 0.1540 ? 1.8513 ? 
-0.7526 ? 0.3668  ? 2.2212 ? -0.2750 ? 1.2817 ? 0.0830  ? 0.2272  ? 0.0072  ? -0.1487 ? -0.1749 ? -0.0285 ? -0.0841 ? 0.0623  ? 
0.1003  ? 
13 'X-RAY DIFFRACTION' ? refined 32.8217 3.4512   15.6423 0.1595 ? -0.0084 ? -0.0169 ? 0.1811 ? -0.0060 ? 0.2096 ? 1.0002 ? 
-0.8434 ? 0.4464  ? 1.5240 ? -0.3294 ? 1.5280 ? 0.0151  ? -0.0497 ? 0.0797  ? 0.0533  ? -0.0172 ? -0.2484 ? -0.1306 ? 0.1314  ? 
-0.0361 ? 
14 'X-RAY DIFFRACTION' ? refined 13.9121 26.4907  25.6748 0.2961 ? 0.0389  ? 0.0181  ? 0.2206 ? -0.0030 ? 0.1508 ? 0.9163 ? 
-0.4756 ? 0.0385  ? 2.7182 ? 1.6078  ? 1.8605 ? -0.0727 ? -0.2565 ? -0.0297 ? 0.7094  ? 0.1339  ? 0.0828  ? -0.0424 ? -0.0053 ? 
-0.0697 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 36 through 69 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 70 through 90 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 91 through 130 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 131 through 157 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 158 through 174 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 175 through 196 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 36 through 69 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 70 through 90 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 91 through 130 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 131 through 157 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 158 through 174 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 175 through 196 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C'
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D'
;
# 
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 ASP 34  ? A ASP 1   
2  1 Y 1 A GLY 35  ? A GLY 2   
3  1 Y 1 A PRO 197 ? A PRO 164 
4  1 Y 1 A PRO 198 ? A PRO 165 
5  1 Y 1 A ALA 199 ? A ALA 166 
6  1 Y 1 A GLY 200 ? A GLY 167 
7  1 Y 1 A LEU 201 ? A LEU 168 
8  1 Y 1 A ASN 202 ? A ASN 169 
9  1 Y 1 A ASP 203 ? A ASP 170 
10 1 Y 1 A ILE 204 ? A ILE 171 
11 1 Y 1 A PHE 205 ? A PHE 172 
12 1 Y 1 A GLU 206 ? A GLU 173 
13 1 Y 1 A ALA 207 ? A ALA 174 
14 1 Y 1 A GLN 208 ? A GLN 175 
15 1 Y 1 A LYS 209 ? A LYS 176 
16 1 Y 1 A ILE 210 ? A ILE 177 
17 1 Y 1 A GLU 211 ? A GLU 178 
18 1 Y 1 A TRP 212 ? A TRP 179 
19 1 Y 1 A HIS 213 ? A HIS 180 
20 1 Y 1 A GLU 214 ? A GLU 181 
21 1 Y 1 A SER 215 ? A SER 182 
22 1 Y 1 A SER 216 ? A SER 183 
23 1 Y 1 A GLY 217 ? A GLY 184 
24 1 Y 1 A LEU 218 ? A LEU 185 
25 1 Y 1 A VAL 219 ? A VAL 186 
26 1 Y 1 A PRO 220 ? A PRO 187 
27 1 Y 1 A ARG 221 ? A ARG 188 
28 1 Y 1 A GLY 222 ? A GLY 189 
29 1 Y 1 A SER 223 ? A SER 190 
30 1 Y 1 A ALA 224 ? A ALA 191 
31 1 Y 1 A ALA 225 ? A ALA 192 
32 1 Y 1 A GLY 226 ? A GLY 193 
33 1 Y 1 A HIS 227 ? A HIS 194 
34 1 Y 1 A HIS 228 ? A HIS 195 
35 1 Y 1 A HIS 229 ? A HIS 196 
36 1 Y 1 A HIS 230 ? A HIS 197 
37 1 Y 1 A HIS 231 ? A HIS 198 
38 1 Y 1 A HIS 232 ? A HIS 199 
39 1 Y 1 A HIS 233 ? A HIS 200 
40 1 Y 1 A HIS 234 ? A HIS 201 
41 1 Y 1 A HIS 235 ? A HIS 202 
42 1 Y 1 A HIS 236 ? A HIS 203 
43 1 Y 1 A GLU 237 ? A GLU 204 
44 1 Y 1 A LEU 238 ? A LEU 205 
45 1 Y 1 B ASP 34  ? B ASP 1   
46 1 Y 1 B GLY 35  ? B GLY 2   
47 1 Y 1 B PRO 197 ? B PRO 164 
48 1 Y 1 B PRO 198 ? B PRO 165 
49 1 Y 1 B ALA 199 ? B ALA 166 
50 1 Y 1 B GLY 200 ? B GLY 167 
51 1 Y 1 B LEU 201 ? B LEU 168 
52 1 Y 1 B ASN 202 ? B ASN 169 
53 1 Y 1 B ASP 203 ? B ASP 170 
54 1 Y 1 B ILE 204 ? B ILE 171 
55 1 Y 1 B PHE 205 ? B PHE 172 
56 1 Y 1 B GLU 206 ? B GLU 173 
57 1 Y 1 B ALA 207 ? B ALA 174 
58 1 Y 1 B GLN 208 ? B GLN 175 
59 1 Y 1 B LYS 209 ? B LYS 176 
60 1 Y 1 B ILE 210 ? B ILE 177 
61 1 Y 1 B GLU 211 ? B GLU 178 
62 1 Y 1 B TRP 212 ? B TRP 179 
63 1 Y 1 B HIS 213 ? B HIS 180 
64 1 Y 1 B GLU 214 ? B GLU 181 
65 1 Y 1 B SER 215 ? B SER 182 
66 1 Y 1 B SER 216 ? B SER 183 
67 1 Y 1 B GLY 217 ? B GLY 184 
68 1 Y 1 B LEU 218 ? B LEU 185 
69 1 Y 1 B VAL 219 ? B VAL 186 
70 1 Y 1 B PRO 220 ? B PRO 187 
71 1 Y 1 B ARG 221 ? B ARG 188 
72 1 Y 1 B GLY 222 ? B GLY 189 
73 1 Y 1 B SER 223 ? B SER 190 
74 1 Y 1 B ALA 224 ? B ALA 191 
75 1 Y 1 B ALA 225 ? B ALA 192 
76 1 Y 1 B GLY 226 ? B GLY 193 
77 1 Y 1 B HIS 227 ? B HIS 194 
78 1 Y 1 B HIS 228 ? B HIS 195 
79 1 Y 1 B HIS 229 ? B HIS 196 
80 1 Y 1 B HIS 230 ? B HIS 197 
81 1 Y 1 B HIS 231 ? B HIS 198 
82 1 Y 1 B HIS 232 ? B HIS 199 
83 1 Y 1 B HIS 233 ? B HIS 200 
84 1 Y 1 B HIS 234 ? B HIS 201 
85 1 Y 1 B HIS 235 ? B HIS 202 
86 1 Y 1 B HIS 236 ? B HIS 203 
87 1 Y 1 B GLU 237 ? B GLU 204 
88 1 Y 1 B LEU 238 ? B LEU 205 
# 
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 
ACE C    C N N 1   
ACE O    O N N 2   
ACE CH3  C N N 3   
ACE H    H N N 4   
ACE H1   H N N 5   
ACE H2   H N N 6   
ACE H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
CYS N    N N N 81  
CYS CA   C N R 82  
CYS C    C N N 83  
CYS O    O N N 84  
CYS CB   C N N 85  
CYS SG   S N N 86  
CYS OXT  O N N 87  
CYS H    H N N 88  
CYS H2   H N N 89  
CYS HA   H N N 90  
CYS HB2  H N N 91  
CYS HB3  H N N 92  
CYS HG   H N N 93  
CYS HXT  H N N 94  
DTY N    N N N 95  
DTY CA   C N R 96  
DTY C    C N N 97  
DTY O    O N N 98  
DTY CB   C N N 99  
DTY CG   C Y N 100 
DTY CD1  C Y N 101 
DTY CD2  C Y N 102 
DTY CE1  C Y N 103 
DTY CE2  C Y N 104 
DTY CZ   C Y N 105 
DTY OH   O N N 106 
DTY OXT  O N N 107 
DTY H    H N N 108 
DTY H2   H N N 109 
DTY HA   H N N 110 
DTY HB2  H N N 111 
DTY HB3  H N N 112 
DTY HD1  H N N 113 
DTY HD2  H N N 114 
DTY HE1  H N N 115 
DTY HE2  H N N 116 
DTY HH   H N N 117 
DTY HXT  H N N 118 
GLN N    N N N 119 
GLN CA   C N S 120 
GLN C    C N N 121 
GLN O    O N N 122 
GLN CB   C N N 123 
GLN CG   C N N 124 
GLN CD   C N N 125 
GLN OE1  O N N 126 
GLN NE2  N N N 127 
GLN OXT  O N N 128 
GLN H    H N N 129 
GLN H2   H N N 130 
GLN HA   H N N 131 
GLN HB2  H N N 132 
GLN HB3  H N N 133 
GLN HG2  H N N 134 
GLN HG3  H N N 135 
GLN HE21 H N N 136 
GLN HE22 H N N 137 
GLN HXT  H N N 138 
GLU N    N N N 139 
GLU CA   C N S 140 
GLU C    C N N 141 
GLU O    O N N 142 
GLU CB   C N N 143 
GLU CG   C N N 144 
GLU CD   C N N 145 
GLU OE1  O N N 146 
GLU OE2  O N N 147 
GLU OXT  O N N 148 
GLU H    H N N 149 
GLU H2   H N N 150 
GLU HA   H N N 151 
GLU HB2  H N N 152 
GLU HB3  H N N 153 
GLU HG2  H N N 154 
GLU HG3  H N N 155 
GLU HE2  H N N 156 
GLU HXT  H N N 157 
GLY N    N N N 158 
GLY CA   C N N 159 
GLY C    C N N 160 
GLY O    O N N 161 
GLY OXT  O N N 162 
GLY H    H N N 163 
GLY H2   H N N 164 
GLY HA2  H N N 165 
GLY HA3  H N N 166 
GLY HXT  H N N 167 
HIS N    N N N 168 
HIS CA   C N S 169 
HIS C    C N N 170 
HIS O    O N N 171 
HIS CB   C N N 172 
HIS CG   C Y N 173 
HIS ND1  N Y N 174 
HIS CD2  C Y N 175 
HIS CE1  C Y N 176 
HIS NE2  N Y N 177 
HIS OXT  O N N 178 
HIS H    H N N 179 
HIS H2   H N N 180 
HIS HA   H N N 181 
HIS HB2  H N N 182 
HIS HB3  H N N 183 
HIS HD1  H N N 184 
HIS HD2  H N N 185 
HIS HE1  H N N 186 
HIS HE2  H N N 187 
HIS HXT  H N N 188 
HOH O    O N N 189 
HOH H1   H N N 190 
HOH H2   H N N 191 
ILE N    N N N 192 
ILE CA   C N S 193 
ILE C    C N N 194 
ILE O    O N N 195 
ILE CB   C N S 196 
ILE CG1  C N N 197 
ILE CG2  C N N 198 
ILE CD1  C N N 199 
ILE OXT  O N N 200 
ILE H    H N N 201 
ILE H2   H N N 202 
ILE HA   H N N 203 
ILE HB   H N N 204 
ILE HG12 H N N 205 
ILE HG13 H N N 206 
ILE HG21 H N N 207 
ILE HG22 H N N 208 
ILE HG23 H N N 209 
ILE HD11 H N N 210 
ILE HD12 H N N 211 
ILE HD13 H N N 212 
ILE HXT  H N N 213 
LEU N    N N N 214 
LEU CA   C N S 215 
LEU C    C N N 216 
LEU O    O N N 217 
LEU CB   C N N 218 
LEU CG   C N N 219 
LEU CD1  C N N 220 
LEU CD2  C N N 221 
LEU OXT  O N N 222 
LEU H    H N N 223 
LEU H2   H N N 224 
LEU HA   H N N 225 
LEU HB2  H N N 226 
LEU HB3  H N N 227 
LEU HG   H N N 228 
LEU HD11 H N N 229 
LEU HD12 H N N 230 
LEU HD13 H N N 231 
LEU HD21 H N N 232 
LEU HD22 H N N 233 
LEU HD23 H N N 234 
LEU HXT  H N N 235 
LYS N    N N N 236 
LYS CA   C N S 237 
LYS C    C N N 238 
LYS O    O N N 239 
LYS CB   C N N 240 
LYS CG   C N N 241 
LYS CD   C N N 242 
LYS CE   C N N 243 
LYS NZ   N N N 244 
LYS OXT  O N N 245 
LYS H    H N N 246 
LYS H2   H N N 247 
LYS HA   H N N 248 
LYS HB2  H N N 249 
LYS HB3  H N N 250 
LYS HG2  H N N 251 
LYS HG3  H N N 252 
LYS HD2  H N N 253 
LYS HD3  H N N 254 
LYS HE2  H N N 255 
LYS HE3  H N N 256 
LYS HZ1  H N N 257 
LYS HZ2  H N N 258 
LYS HZ3  H N N 259 
LYS HXT  H N N 260 
MET N    N N N 261 
MET CA   C N S 262 
MET C    C N N 263 
MET O    O N N 264 
MET CB   C N N 265 
MET CG   C N N 266 
MET SD   S N N 267 
MET CE   C N N 268 
MET OXT  O N N 269 
MET H    H N N 270 
MET H2   H N N 271 
MET HA   H N N 272 
MET HB2  H N N 273 
MET HB3  H N N 274 
MET HG2  H N N 275 
MET HG3  H N N 276 
MET HE1  H N N 277 
MET HE2  H N N 278 
MET HE3  H N N 279 
MET HXT  H N N 280 
PHE N    N N N 281 
PHE CA   C N S 282 
PHE C    C N N 283 
PHE O    O N N 284 
PHE CB   C N N 285 
PHE CG   C Y N 286 
PHE CD1  C Y N 287 
PHE CD2  C Y N 288 
PHE CE1  C Y N 289 
PHE CE2  C Y N 290 
PHE CZ   C Y N 291 
PHE OXT  O N N 292 
PHE H    H N N 293 
PHE H2   H N N 294 
PHE HA   H N N 295 
PHE HB2  H N N 296 
PHE HB3  H N N 297 
PHE HD1  H N N 298 
PHE HD2  H N N 299 
PHE HE1  H N N 300 
PHE HE2  H N N 301 
PHE HZ   H N N 302 
PHE HXT  H N N 303 
PRO N    N N N 304 
PRO CA   C N S 305 
PRO C    C N N 306 
PRO O    O N N 307 
PRO CB   C N N 308 
PRO CG   C N N 309 
PRO CD   C N N 310 
PRO OXT  O N N 311 
PRO H    H N N 312 
PRO HA   H N N 313 
PRO HB2  H N N 314 
PRO HB3  H N N 315 
PRO HG2  H N N 316 
PRO HG3  H N N 317 
PRO HD2  H N N 318 
PRO HD3  H N N 319 
PRO HXT  H N N 320 
SER N    N N N 321 
SER CA   C N S 322 
SER C    C N N 323 
SER O    O N N 324 
SER CB   C N N 325 
SER OG   O N N 326 
SER OXT  O N N 327 
SER H    H N N 328 
SER H2   H N N 329 
SER HA   H N N 330 
SER HB2  H N N 331 
SER HB3  H N N 332 
SER HG   H N N 333 
SER HXT  H N N 334 
THR N    N N N 335 
THR CA   C N S 336 
THR C    C N N 337 
THR O    O N N 338 
THR CB   C N R 339 
THR OG1  O N N 340 
THR CG2  C N N 341 
THR OXT  O N N 342 
THR H    H N N 343 
THR H2   H N N 344 
THR HA   H N N 345 
THR HB   H N N 346 
THR HG1  H N N 347 
THR HG21 H N N 348 
THR HG22 H N N 349 
THR HG23 H N N 350 
THR HXT  H N N 351 
TRP N    N N N 352 
TRP CA   C N S 353 
TRP C    C N N 354 
TRP O    O N N 355 
TRP CB   C N N 356 
TRP CG   C Y N 357 
TRP CD1  C Y N 358 
TRP CD2  C Y N 359 
TRP NE1  N Y N 360 
TRP CE2  C Y N 361 
TRP CE3  C Y N 362 
TRP CZ2  C Y N 363 
TRP CZ3  C Y N 364 
TRP CH2  C Y N 365 
TRP OXT  O N N 366 
TRP H    H N N 367 
TRP H2   H N N 368 
TRP HA   H N N 369 
TRP HB2  H N N 370 
TRP HB3  H N N 371 
TRP HD1  H N N 372 
TRP HE1  H N N 373 
TRP HE3  H N N 374 
TRP HZ2  H N N 375 
TRP HZ3  H N N 376 
TRP HH2  H N N 377 
TRP HXT  H N N 378 
TYR N    N N N 379 
TYR CA   C N S 380 
TYR C    C N N 381 
TYR O    O N N 382 
TYR CB   C N N 383 
TYR CG   C Y N 384 
TYR CD1  C Y N 385 
TYR CD2  C Y N 386 
TYR CE1  C Y N 387 
TYR CE2  C Y N 388 
TYR CZ   C Y N 389 
TYR OH   O N N 390 
TYR OXT  O N N 391 
TYR H    H N N 392 
TYR H2   H N N 393 
TYR HA   H N N 394 
TYR HB2  H N N 395 
TYR HB3  H N N 396 
TYR HD1  H N N 397 
TYR HD2  H N N 398 
TYR HE1  H N N 399 
TYR HE2  H N N 400 
TYR HH   H N N 401 
TYR HXT  H N N 402 
VAL N    N N N 403 
VAL CA   C N S 404 
VAL C    C N N 405 
VAL O    O N N 406 
VAL CB   C N N 407 
VAL CG1  C N N 408 
VAL CG2  C N N 409 
VAL OXT  O N N 410 
VAL H    H N N 411 
VAL H2   H N N 412 
VAL HA   H N N 413 
VAL HB   H N N 414 
VAL HG11 H N N 415 
VAL HG12 H N N 416 
VAL HG13 H N N 417 
VAL HG21 H N N 418 
VAL HG22 H N N 419 
VAL HG23 H N N 420 
VAL HXT  H N N 421 
# 
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 
ACE C   O    doub N N 1   
ACE C   CH3  sing N N 2   
ACE C   H    sing N N 3   
ACE CH3 H1   sing N N 4   
ACE CH3 H2   sing N N 5   
ACE CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
DTY N   CA   sing N N 89  
DTY N   H    sing N N 90  
DTY N   H2   sing N N 91  
DTY CA  C    sing N N 92  
DTY CA  CB   sing N N 93  
DTY CA  HA   sing N N 94  
DTY C   O    doub N N 95  
DTY C   OXT  sing N N 96  
DTY CB  CG   sing N N 97  
DTY CB  HB2  sing N N 98  
DTY CB  HB3  sing N N 99  
DTY CG  CD1  doub Y N 100 
DTY CG  CD2  sing Y N 101 
DTY CD1 CE1  sing Y N 102 
DTY CD1 HD1  sing N N 103 
DTY CD2 CE2  doub Y N 104 
DTY CD2 HD2  sing N N 105 
DTY CE1 CZ   doub Y N 106 
DTY CE1 HE1  sing N N 107 
DTY CE2 CZ   sing Y N 108 
DTY CE2 HE2  sing N N 109 
DTY CZ  OH   sing N N 110 
DTY OH  HH   sing N N 111 
DTY OXT HXT  sing N N 112 
GLN N   CA   sing N N 113 
GLN N   H    sing N N 114 
GLN N   H2   sing N N 115 
GLN CA  C    sing N N 116 
GLN CA  CB   sing N N 117 
GLN CA  HA   sing N N 118 
GLN C   O    doub N N 119 
GLN C   OXT  sing N N 120 
GLN CB  CG   sing N N 121 
GLN CB  HB2  sing N N 122 
GLN CB  HB3  sing N N 123 
GLN CG  CD   sing N N 124 
GLN CG  HG2  sing N N 125 
GLN CG  HG3  sing N N 126 
GLN CD  OE1  doub N N 127 
GLN CD  NE2  sing N N 128 
GLN NE2 HE21 sing N N 129 
GLN NE2 HE22 sing N N 130 
GLN OXT HXT  sing N N 131 
GLU N   CA   sing N N 132 
GLU N   H    sing N N 133 
GLU N   H2   sing N N 134 
GLU CA  C    sing N N 135 
GLU CA  CB   sing N N 136 
GLU CA  HA   sing N N 137 
GLU C   O    doub N N 138 
GLU C   OXT  sing N N 139 
GLU CB  CG   sing N N 140 
GLU CB  HB2  sing N N 141 
GLU CB  HB3  sing N N 142 
GLU CG  CD   sing N N 143 
GLU CG  HG2  sing N N 144 
GLU CG  HG3  sing N N 145 
GLU CD  OE1  doub N N 146 
GLU CD  OE2  sing N N 147 
GLU OE2 HE2  sing N N 148 
GLU OXT HXT  sing N N 149 
GLY N   CA   sing N N 150 
GLY N   H    sing N N 151 
GLY N   H2   sing N N 152 
GLY CA  C    sing N N 153 
GLY CA  HA2  sing N N 154 
GLY CA  HA3  sing N N 155 
GLY C   O    doub N N 156 
GLY C   OXT  sing N N 157 
GLY OXT HXT  sing N N 158 
HIS N   CA   sing N N 159 
HIS N   H    sing N N 160 
HIS N   H2   sing N N 161 
HIS CA  C    sing N N 162 
HIS CA  CB   sing N N 163 
HIS CA  HA   sing N N 164 
HIS C   O    doub N N 165 
HIS C   OXT  sing N N 166 
HIS CB  CG   sing N N 167 
HIS CB  HB2  sing N N 168 
HIS CB  HB3  sing N N 169 
HIS CG  ND1  sing Y N 170 
HIS CG  CD2  doub Y N 171 
HIS ND1 CE1  doub Y N 172 
HIS ND1 HD1  sing N N 173 
HIS CD2 NE2  sing Y N 174 
HIS CD2 HD2  sing N N 175 
HIS CE1 NE2  sing Y N 176 
HIS CE1 HE1  sing N N 177 
HIS NE2 HE2  sing N N 178 
HIS OXT HXT  sing N N 179 
HOH O   H1   sing N N 180 
HOH O   H2   sing N N 181 
ILE N   CA   sing N N 182 
ILE N   H    sing N N 183 
ILE N   H2   sing N N 184 
ILE CA  C    sing N N 185 
ILE CA  CB   sing N N 186 
ILE CA  HA   sing N N 187 
ILE C   O    doub N N 188 
ILE C   OXT  sing N N 189 
ILE CB  CG1  sing N N 190 
ILE CB  CG2  sing N N 191 
ILE CB  HB   sing N N 192 
ILE CG1 CD1  sing N N 193 
ILE CG1 HG12 sing N N 194 
ILE CG1 HG13 sing N N 195 
ILE CG2 HG21 sing N N 196 
ILE CG2 HG22 sing N N 197 
ILE CG2 HG23 sing N N 198 
ILE CD1 HD11 sing N N 199 
ILE CD1 HD12 sing N N 200 
ILE CD1 HD13 sing N N 201 
ILE OXT HXT  sing N N 202 
LEU N   CA   sing N N 203 
LEU N   H    sing N N 204 
LEU N   H2   sing N N 205 
LEU CA  C    sing N N 206 
LEU CA  CB   sing N N 207 
LEU CA  HA   sing N N 208 
LEU C   O    doub N N 209 
LEU C   OXT  sing N N 210 
LEU CB  CG   sing N N 211 
LEU CB  HB2  sing N N 212 
LEU CB  HB3  sing N N 213 
LEU CG  CD1  sing N N 214 
LEU CG  CD2  sing N N 215 
LEU CG  HG   sing N N 216 
LEU CD1 HD11 sing N N 217 
LEU CD1 HD12 sing N N 218 
LEU CD1 HD13 sing N N 219 
LEU CD2 HD21 sing N N 220 
LEU CD2 HD22 sing N N 221 
LEU CD2 HD23 sing N N 222 
LEU OXT HXT  sing N N 223 
LYS N   CA   sing N N 224 
LYS N   H    sing N N 225 
LYS N   H2   sing N N 226 
LYS CA  C    sing N N 227 
LYS CA  CB   sing N N 228 
LYS CA  HA   sing N N 229 
LYS C   O    doub N N 230 
LYS C   OXT  sing N N 231 
LYS CB  CG   sing N N 232 
LYS CB  HB2  sing N N 233 
LYS CB  HB3  sing N N 234 
LYS CG  CD   sing N N 235 
LYS CG  HG2  sing N N 236 
LYS CG  HG3  sing N N 237 
LYS CD  CE   sing N N 238 
LYS CD  HD2  sing N N 239 
LYS CD  HD3  sing N N 240 
LYS CE  NZ   sing N N 241 
LYS CE  HE2  sing N N 242 
LYS CE  HE3  sing N N 243 
LYS NZ  HZ1  sing N N 244 
LYS NZ  HZ2  sing N N 245 
LYS NZ  HZ3  sing N N 246 
LYS OXT HXT  sing N N 247 
MET N   CA   sing N N 248 
MET N   H    sing N N 249 
MET N   H2   sing N N 250 
MET CA  C    sing N N 251 
MET CA  CB   sing N N 252 
MET CA  HA   sing N N 253 
MET C   O    doub N N 254 
MET C   OXT  sing N N 255 
MET CB  CG   sing N N 256 
MET CB  HB2  sing N N 257 
MET CB  HB3  sing N N 258 
MET CG  SD   sing N N 259 
MET CG  HG2  sing N N 260 
MET CG  HG3  sing N N 261 
MET SD  CE   sing N N 262 
MET CE  HE1  sing N N 263 
MET CE  HE2  sing N N 264 
MET CE  HE3  sing N N 265 
MET OXT HXT  sing N N 266 
PHE N   CA   sing N N 267 
PHE N   H    sing N N 268 
PHE N   H2   sing N N 269 
PHE CA  C    sing N N 270 
PHE CA  CB   sing N N 271 
PHE CA  HA   sing N N 272 
PHE C   O    doub N N 273 
PHE C   OXT  sing N N 274 
PHE CB  CG   sing N N 275 
PHE CB  HB2  sing N N 276 
PHE CB  HB3  sing N N 277 
PHE CG  CD1  doub Y N 278 
PHE CG  CD2  sing Y N 279 
PHE CD1 CE1  sing Y N 280 
PHE CD1 HD1  sing N N 281 
PHE CD2 CE2  doub Y N 282 
PHE CD2 HD2  sing N N 283 
PHE CE1 CZ   doub Y N 284 
PHE CE1 HE1  sing N N 285 
PHE CE2 CZ   sing Y N 286 
PHE CE2 HE2  sing N N 287 
PHE CZ  HZ   sing N N 288 
PHE OXT HXT  sing N N 289 
PRO N   CA   sing N N 290 
PRO N   CD   sing N N 291 
PRO N   H    sing N N 292 
PRO CA  C    sing N N 293 
PRO CA  CB   sing N N 294 
PRO CA  HA   sing N N 295 
PRO C   O    doub N N 296 
PRO C   OXT  sing N N 297 
PRO CB  CG   sing N N 298 
PRO CB  HB2  sing N N 299 
PRO CB  HB3  sing N N 300 
PRO CG  CD   sing N N 301 
PRO CG  HG2  sing N N 302 
PRO CG  HG3  sing N N 303 
PRO CD  HD2  sing N N 304 
PRO CD  HD3  sing N N 305 
PRO OXT HXT  sing N N 306 
SER N   CA   sing N N 307 
SER N   H    sing N N 308 
SER N   H2   sing N N 309 
SER CA  C    sing N N 310 
SER CA  CB   sing N N 311 
SER CA  HA   sing N N 312 
SER C   O    doub N N 313 
SER C   OXT  sing N N 314 
SER CB  OG   sing N N 315 
SER CB  HB2  sing N N 316 
SER CB  HB3  sing N N 317 
SER OG  HG   sing N N 318 
SER OXT HXT  sing N N 319 
THR N   CA   sing N N 320 
THR N   H    sing N N 321 
THR N   H2   sing N N 322 
THR CA  C    sing N N 323 
THR CA  CB   sing N N 324 
THR CA  HA   sing N N 325 
THR C   O    doub N N 326 
THR C   OXT  sing N N 327 
THR CB  OG1  sing N N 328 
THR CB  CG2  sing N N 329 
THR CB  HB   sing N N 330 
THR OG1 HG1  sing N N 331 
THR CG2 HG21 sing N N 332 
THR CG2 HG22 sing N N 333 
THR CG2 HG23 sing N N 334 
THR OXT HXT  sing N N 335 
TRP N   CA   sing N N 336 
TRP N   H    sing N N 337 
TRP N   H2   sing N N 338 
TRP CA  C    sing N N 339 
TRP CA  CB   sing N N 340 
TRP CA  HA   sing N N 341 
TRP C   O    doub N N 342 
TRP C   OXT  sing N N 343 
TRP CB  CG   sing N N 344 
TRP CB  HB2  sing N N 345 
TRP CB  HB3  sing N N 346 
TRP CG  CD1  doub Y N 347 
TRP CG  CD2  sing Y N 348 
TRP CD1 NE1  sing Y N 349 
TRP CD1 HD1  sing N N 350 
TRP CD2 CE2  doub Y N 351 
TRP CD2 CE3  sing Y N 352 
TRP NE1 CE2  sing Y N 353 
TRP NE1 HE1  sing N N 354 
TRP CE2 CZ2  sing Y N 355 
TRP CE3 CZ3  doub Y N 356 
TRP CE3 HE3  sing N N 357 
TRP CZ2 CH2  doub Y N 358 
TRP CZ2 HZ2  sing N N 359 
TRP CZ3 CH2  sing Y N 360 
TRP CZ3 HZ3  sing N N 361 
TRP CH2 HH2  sing N N 362 
TRP OXT HXT  sing N N 363 
TYR N   CA   sing N N 364 
TYR N   H    sing N N 365 
TYR N   H2   sing N N 366 
TYR CA  C    sing N N 367 
TYR CA  CB   sing N N 368 
TYR CA  HA   sing N N 369 
TYR C   O    doub N N 370 
TYR C   OXT  sing N N 371 
TYR CB  CG   sing N N 372 
TYR CB  HB2  sing N N 373 
TYR CB  HB3  sing N N 374 
TYR CG  CD1  doub Y N 375 
TYR CG  CD2  sing Y N 376 
TYR CD1 CE1  sing Y N 377 
TYR CD1 HD1  sing N N 378 
TYR CD2 CE2  doub Y N 379 
TYR CD2 HD2  sing N N 380 
TYR CE1 CZ   doub Y N 381 
TYR CE1 HE1  sing N N 382 
TYR CE2 CZ   sing Y N 383 
TYR CE2 HE2  sing N N 384 
TYR CZ  OH   sing N N 385 
TYR OH  HH   sing N N 386 
TYR OXT HXT  sing N N 387 
VAL N   CA   sing N N 388 
VAL N   H    sing N N 389 
VAL N   H2   sing N N 390 
VAL CA  C    sing N N 391 
VAL CA  CB   sing N N 392 
VAL CA  HA   sing N N 393 
VAL C   O    doub N N 394 
VAL C   OXT  sing N N 395 
VAL CB  CG1  sing N N 396 
VAL CB  CG2  sing N N 397 
VAL CB  HB   sing N N 398 
VAL CG1 HG11 sing N N 399 
VAL CG1 HG12 sing N N 400 
VAL CG1 HG13 sing N N 401 
VAL CG2 HG21 sing N N 402 
VAL CG2 HG22 sing N N 403 
VAL CG2 HG23 sing N N 404 
VAL OXT HXT  sing N N 405 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/Office of the Director'                                           'United States' S10OD030394  1 
'National Institutes of Health/National Center for Advancing Translational Sciences (NIH/NCATS)' 'United States' 1ZIATR000053 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2F6L 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BT7 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.014248 
_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]   0.014064 
_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]   0.013966 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . THR A 1 3   ? 7.134  43.375  -6.878 1.00 49.59 ? 36  THR A N   1 
ATOM   2    C CA  . THR A 1 3   ? 8.201  42.883  -6.011 1.00 44.09 ? 36  THR A CA  1 
ATOM   3    C C   . THR A 1 3   ? 7.936  43.225  -4.546 1.00 33.69 ? 36  THR A C   1 
ATOM   4    O O   . THR A 1 3   ? 7.592  44.361  -4.206 1.00 38.04 ? 36  THR A O   1 
ATOM   5    C CB  . THR A 1 3   ? 9.567  43.449  -6.439 1.00 36.79 ? 36  THR A CB  1 
ATOM   6    O OG1 . THR A 1 3   ? 9.929  42.884  -7.704 1.00 58.07 ? 36  THR A OG1 1 
ATOM   7    C CG2 . THR A 1 3   ? 10.648 43.109  -5.419 1.00 44.49 ? 36  THR A CG2 1 
ATOM   8    N N   . SER A 1 4   ? 8.102  42.230  -3.681 1.00 28.88 ? 37  SER A N   1 
ATOM   9    C CA  . SER A 1 4   ? 7.784  42.405  -2.273 1.00 24.60 ? 37  SER A CA  1 
ATOM   10   C C   . SER A 1 4   ? 8.818  43.283  -1.581 1.00 21.26 ? 37  SER A C   1 
ATOM   11   O O   . SER A 1 4   ? 10.023 43.146  -1.798 1.00 19.09 ? 37  SER A O   1 
ATOM   12   C CB  . SER A 1 4   ? 7.707  41.045  -1.580 1.00 21.15 ? 37  SER A CB  1 
ATOM   13   O OG  . SER A 1 4   ? 7.572  41.196  -0.177 1.00 18.52 ? 37  SER A OG  1 
ATOM   14   N N   A GLN A 1 5   ? 8.331  44.192  -0.737 0.48 20.27 ? 38  GLN A N   1 
ATOM   15   N N   B GLN A 1 5   ? 8.331  44.196  -0.739 0.52 20.26 ? 38  GLN A N   1 
ATOM   16   C CA  A GLN A 1 5   ? 9.202  44.965  0.138  0.48 19.71 ? 38  GLN A CA  1 
ATOM   17   C CA  B GLN A 1 5   ? 9.209  44.966  0.132  0.52 19.71 ? 38  GLN A CA  1 
ATOM   18   C C   A GLN A 1 5   ? 9.937  44.091  1.151  0.48 17.17 ? 38  GLN A C   1 
ATOM   19   C C   B GLN A 1 5   ? 9.951  44.085  1.137  0.52 17.15 ? 38  GLN A C   1 
ATOM   20   O O   A GLN A 1 5   ? 10.900 44.557  1.772  0.48 18.48 ? 38  GLN A O   1 
ATOM   21   O O   B GLN A 1 5   ? 10.930 44.537  1.743  0.52 18.48 ? 38  GLN A O   1 
ATOM   22   C CB  A GLN A 1 5   ? 8.383  46.033  0.868  0.48 20.31 ? 38  GLN A CB  1 
ATOM   23   C CB  B GLN A 1 5   ? 8.393  46.023  0.875  0.52 20.30 ? 38  GLN A CB  1 
ATOM   24   C CG  A GLN A 1 5   ? 7.793  47.109  -0.045 0.48 22.15 ? 38  GLN A CG  1 
ATOM   25   C CG  B GLN A 1 5   ? 7.935  47.183  -0.001 0.52 22.10 ? 38  GLN A CG  1 
ATOM   26   C CD  A GLN A 1 5   ? 6.682  47.905  0.626  0.48 23.20 ? 38  GLN A CD  1 
ATOM   27   C CD  B GLN A 1 5   ? 9.092  48.029  -0.474 0.52 24.37 ? 38  GLN A CD  1 
ATOM   28   O OE1 A GLN A 1 5   ? 6.549  47.903  1.853  0.48 24.51 ? 38  GLN A OE1 1 
ATOM   29   O OE1 B GLN A 1 5   ? 9.370  48.108  -1.670 0.52 30.33 ? 38  GLN A OE1 1 
ATOM   30   N NE2 A GLN A 1 5   ? 5.872  48.579  -0.179 0.48 28.82 ? 38  GLN A NE2 1 
ATOM   31   N NE2 B GLN A 1 5   ? 9.780  48.670  0.466  0.52 26.33 ? 38  GLN A NE2 1 
ATOM   32   N N   . LEU A 1 6   ? 9.504  42.850  1.346  1.00 15.34 ? 39  LEU A N   1 
ATOM   33   C CA  . LEU A 1 6   ? 10.159 41.947  2.286  1.00 14.58 ? 39  LEU A CA  1 
ATOM   34   C C   . LEU A 1 6   ? 11.182 41.031  1.612  1.00 15.54 ? 39  LEU A C   1 
ATOM   35   O O   . LEU A 1 6   ? 11.733 40.148  2.270  1.00 13.51 ? 39  LEU A O   1 
ATOM   36   C CB  . LEU A 1 6   ? 9.112  41.115  3.044  1.00 14.46 ? 39  LEU A CB  1 
ATOM   37   C CG  . LEU A 1 6   ? 8.160  41.909  3.935  1.00 15.39 ? 39  LEU A CG  1 
ATOM   38   C CD1 . LEU A 1 6   ? 7.170  41.000  4.669  1.00 17.55 ? 39  LEU A CD1 1 
ATOM   39   C CD2 . LEU A 1 6   ? 8.946  42.754  4.932  1.00 15.90 ? 39  LEU A CD2 1 
ATOM   40   N N   . ALA A 1 7   ? 11.459 41.231  0.322  1.00 15.23 ? 40  ALA A N   1 
ATOM   41   C CA  . ALA A 1 7   ? 12.301 40.288  -0.407 1.00 15.37 ? 40  ALA A CA  1 
ATOM   42   C C   . ALA A 1 7   ? 13.745 40.322  0.074  1.00 15.00 ? 40  ALA A C   1 
ATOM   43   O O   . ALA A 1 7   ? 14.399 39.280  0.123  1.00 16.49 ? 40  ALA A O   1 
ATOM   44   C CB  . ALA A 1 7   ? 12.230 40.567  -1.906 1.00 16.08 ? 40  ALA A CB  1 
ATOM   45   N N   . GLU A 1 8   ? 14.272 41.496  0.424  1.00 15.34 ? 41  GLU A N   1 
ATOM   46   C CA  . GLU A 1 8   ? 15.662 41.554  0.879  1.00 17.60 ? 41  GLU A CA  1 
ATOM   47   C C   . GLU A 1 8   ? 15.834 40.821  2.206  1.00 16.70 ? 41  GLU A C   1 
ATOM   48   O O   . GLU A 1 8   ? 16.813 40.084  2.405  1.00 15.51 ? 41  GLU A O   1 
ATOM   49   C CB  . GLU A 1 8   ? 16.114 43.013  0.993  1.00 19.20 ? 41  GLU A CB  1 
ATOM   50   C CG  . GLU A 1 8   ? 17.596 43.172  1.229  1.00 17.29 ? 41  GLU A CG  1 
ATOM   51   C CD  . GLU A 1 8   ? 18.052 44.623  1.149  1.00 27.68 ? 41  GLU A CD  1 
ATOM   52   O OE1 . GLU A 1 8   ? 17.225 45.505  0.832  1.00 27.39 ? 41  GLU A OE1 1 
ATOM   53   O OE2 . GLU A 1 8   ? 19.248 44.880  1.409  1.00 34.08 ? 41  GLU A OE2 1 
ATOM   54   N N   . LEU A 1 9   ? 14.866 40.989  3.110  1.00 14.00 ? 42  LEU A N   1 
ATOM   55   C CA  . LEU A 1 9   ? 14.878 40.272  4.380  1.00 15.28 ? 42  LEU A CA  1 
ATOM   56   C C   . LEU A 1 9   ? 14.785 38.763  4.162  1.00 13.36 ? 42  LEU A C   1 
ATOM   57   O O   . LEU A 1 9   ? 15.545 37.983  4.753  1.00 13.54 ? 42  LEU A O   1 
ATOM   58   C CB  . LEU A 1 9   ? 13.717 40.767  5.249  1.00 14.97 ? 42  LEU A CB  1 
ATOM   59   C CG  . LEU A 1 9   ? 13.385 39.991  6.533  1.00 15.77 ? 42  LEU A CG  1 
ATOM   60   C CD1 . LEU A 1 9   ? 14.584 39.949  7.471  1.00 14.91 ? 42  LEU A CD1 1 
ATOM   61   C CD2 . LEU A 1 9   ? 12.171 40.610  7.235  1.00 13.66 ? 42  LEU A CD2 1 
ATOM   62   N N   . VAL A 1 10  ? 13.851 38.331  3.318  1.00 13.20 ? 43  VAL A N   1 
ATOM   63   C CA  . VAL A 1 10  ? 13.672 36.897  3.099  1.00 13.69 ? 43  VAL A CA  1 
ATOM   64   C C   . VAL A 1 10  ? 14.892 36.314  2.397  1.00 12.86 ? 43  VAL A C   1 
ATOM   65   O O   . VAL A 1 10  ? 15.301 35.179  2.666  1.00 12.55 ? 43  VAL A O   1 
ATOM   66   C CB  . VAL A 1 10  ? 12.370 36.642  2.316  1.00 15.94 ? 43  VAL A CB  1 
ATOM   67   C CG1 . VAL A 1 10  ? 12.237 35.142  1.933  1.00 14.78 ? 43  VAL A CG1 1 
ATOM   68   C CG2 . VAL A 1 10  ? 11.163 37.111  3.136  1.00 12.38 ? 43  VAL A CG2 1 
ATOM   69   N N   . ASP A 1 11  ? 15.482 37.073  1.473  1.00 13.59 ? 44  ASP A N   1 
ATOM   70   C CA  . ASP A 1 11  ? 16.720 36.648  0.835  1.00 16.91 ? 44  ASP A CA  1 
ATOM   71   C C   . ASP A 1 11  ? 17.818 36.433  1.865  1.00 15.23 ? 44  ASP A C   1 
ATOM   72   O O   . ASP A 1 11  ? 18.566 35.448  1.792  1.00 14.99 ? 44  ASP A O   1 
ATOM   73   C CB  . ASP A 1 11  ? 17.157 37.695  -0.185 1.00 15.07 ? 44  ASP A CB  1 
ATOM   74   C CG  . ASP A 1 11  ? 18.405 37.284  -0.948 1.00 18.64 ? 44  ASP A CG  1 
ATOM   75   O OD1 . ASP A 1 11  ? 18.347 36.279  -1.694 1.00 19.89 ? 44  ASP A OD1 1 
ATOM   76   O OD2 . ASP A 1 11  ? 19.433 37.984  -0.813 1.00 21.55 ? 44  ASP A OD2 1 
ATOM   77   N N   . ALA A 1 12  ? 17.941 37.360  2.823  1.00 13.67 ? 45  ALA A N   1 
ATOM   78   C CA  . ALA A 1 12  ? 18.958 37.226  3.863  1.00 14.85 ? 45  ALA A CA  1 
ATOM   79   C C   . ALA A 1 12  ? 18.690 36.018  4.755  1.00 15.25 ? 45  ALA A C   1 
ATOM   80   O O   . ALA A 1 12  ? 19.619 35.295  5.139  1.00 12.72 ? 45  ALA A O   1 
ATOM   81   C CB  . ALA A 1 12  ? 19.015 38.499  4.702  1.00 13.77 ? 45  ALA A CB  1 
ATOM   82   N N   . ALA A 1 13  ? 17.426 35.789  5.101  1.00 13.34 ? 46  ALA A N   1 
ATOM   83   C CA  . ALA A 1 13  ? 17.095 34.626  5.918  1.00 13.47 ? 46  ALA A CA  1 
ATOM   84   C C   . ALA A 1 13  ? 17.420 33.323  5.181  1.00 14.01 ? 46  ALA A C   1 
ATOM   85   O O   . ALA A 1 13  ? 17.934 32.369  5.779  1.00 13.12 ? 46  ALA A O   1 
ATOM   86   C CB  . ALA A 1 13  ? 15.622 34.689  6.309  1.00 11.56 ? 46  ALA A CB  1 
ATOM   87   N N   . ALA A 1 14  ? 17.130 33.267  3.878  1.00 11.99 ? 47  ALA A N   1 
ATOM   88   C CA  . ALA A 1 14  ? 17.462 32.068  3.108  1.00 14.06 ? 47  ALA A CA  1 
ATOM   89   C C   . ALA A 1 14  ? 18.972 31.882  2.997  1.00 14.06 ? 47  ALA A C   1 
ATOM   90   O O   . ALA A 1 14  ? 19.483 30.752  3.106  1.00 12.77 ? 47  ALA A O   1 
ATOM   91   C CB  . ALA A 1 14  ? 16.816 32.138  1.723  1.00 12.68 ? 47  ALA A CB  1 
ATOM   92   N N   . GLU A 1 15  ? 19.708 32.972  2.771  1.00 12.97 ? 48  GLU A N   1 
ATOM   93   C CA  . GLU A 1 15  ? 21.157 32.844  2.722  1.00 14.51 ? 48  GLU A CA  1 
ATOM   94   C C   . GLU A 1 15  ? 21.687 32.336  4.055  1.00 13.45 ? 48  GLU A C   1 
ATOM   95   O O   . GLU A 1 15  ? 22.622 31.529  4.094  1.00 13.07 ? 48  GLU A O   1 
ATOM   96   C CB  . GLU A 1 15  ? 21.807 34.178  2.345  1.00 14.19 ? 48  GLU A CB  1 
ATOM   97   C CG  . GLU A 1 15  ? 23.293 34.031  2.060  1.00 15.00 ? 48  GLU A CG  1 
ATOM   98   C CD  . GLU A 1 15  ? 23.976 35.326  1.650  1.00 23.94 ? 48  GLU A CD  1 
ATOM   99   O OE1 . GLU A 1 15  ? 23.287 36.286  1.233  1.00 22.63 ? 48  GLU A OE1 1 
ATOM   100  O OE2 . GLU A 1 15  ? 25.217 35.383  1.762  1.00 26.24 ? 48  GLU A OE2 1 
ATOM   101  N N   . ARG A 1 16  ? 21.084 32.785  5.163  1.00 12.50 ? 49  ARG A N   1 
ATOM   102  C CA  . ARG A 1 16  ? 21.519 32.311  6.475  1.00 14.00 ? 49  ARG A CA  1 
ATOM   103  C C   . ARG A 1 16  ? 21.185 30.836  6.660  1.00 16.54 ? 49  ARG A C   1 
ATOM   104  O O   . ARG A 1 16  ? 21.960 30.090  7.274  1.00 14.91 ? 49  ARG A O   1 
ATOM   105  C CB  . ARG A 1 16  ? 20.884 33.168  7.575  1.00 13.37 ? 49  ARG A CB  1 
ATOM   106  C CG  . ARG A 1 16  ? 21.618 33.132  8.924  1.00 18.83 ? 49  ARG A CG  1 
ATOM   107  C CD  . ARG A 1 16  ? 20.697 33.683  10.011 1.00 17.85 ? 49  ARG A CD  1 
ATOM   108  N NE  . ARG A 1 16  ? 21.330 33.823  11.319 1.00 17.65 ? 49  ARG A NE  1 
ATOM   109  C CZ  . ARG A 1 16  ? 21.407 32.849  12.218 1.00 20.40 ? 49  ARG A CZ  1 
ATOM   110  N NH1 . ARG A 1 16  ? 21.023 31.612  11.932 1.00 18.71 ? 49  ARG A NH1 1 
ATOM   111  N NH2 . ARG A 1 16  ? 21.874 33.123  13.433 1.00 18.77 ? 49  ARG A NH2 1 
ATOM   112  N N   . LEU A 1 17  ? 20.043 30.392  6.118  1.00 11.90 ? 50  LEU A N   1 
ATOM   113  C CA  . LEU A 1 17  ? 19.717 28.966  6.167  1.00 12.86 ? 50  LEU A CA  1 
ATOM   114  C C   . LEU A 1 17  ? 20.793 28.141  5.485  1.00 16.88 ? 50  LEU A C   1 
ATOM   115  O O   . LEU A 1 17  ? 21.072 27.009  5.901  1.00 13.14 ? 50  LEU A O   1 
ATOM   116  C CB  . LEU A 1 17  ? 18.364 28.686  5.499  1.00 11.08 ? 50  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 17  ? 17.082 29.112  6.205  1.00 11.35 ? 50  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 17  ? 15.921 28.750  5.286  1.00 16.31 ? 50  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 17  ? 16.952 28.430  7.572  1.00 10.79 ? 50  LEU A CD2 1 
ATOM   120  N N   . GLU A 1 18  ? 21.385 28.683  4.409  1.00 12.03 ? 51  GLU A N   1 
ATOM   121  C CA  . GLU A 1 18  ? 22.382 27.918  3.665  1.00 14.00 ? 51  GLU A CA  1 
ATOM   122  C C   . GLU A 1 18  ? 23.630 27.584  4.488  1.00 14.12 ? 51  GLU A C   1 
ATOM   123  O O   . GLU A 1 18  ? 24.355 26.649  4.126  1.00 14.51 ? 51  GLU A O   1 
ATOM   124  C CB  . GLU A 1 18  ? 22.744 28.670  2.369  1.00 14.07 ? 51  GLU A CB  1 
ATOM   125  C CG  . GLU A 1 18  ? 21.507 28.811  1.496  1.00 18.33 ? 51  GLU A CG  1 
ATOM   126  C CD  . GLU A 1 18  ? 21.722 29.577  0.194  1.00 24.14 ? 51  GLU A CD  1 
ATOM   127  O OE1 . GLU A 1 18  ? 22.877 29.914  -0.148 1.00 32.40 ? 51  GLU A OE1 1 
ATOM   128  O OE2 . GLU A 1 18  ? 20.708 29.852  -0.479 1.00 29.34 ? 51  GLU A OE2 1 
ATOM   129  N N   . VAL A 1 19  ? 23.889 28.294  5.594  1.00 14.42 ? 52  VAL A N   1 
ATOM   130  C CA  . VAL A 1 19  ? 25.048 27.978  6.426  1.00 16.08 ? 52  VAL A CA  1 
ATOM   131  C C   . VAL A 1 19  ? 24.883 26.615  7.096  1.00 12.89 ? 52  VAL A C   1 
ATOM   132  O O   . VAL A 1 19  ? 25.867 26.018  7.556  1.00 16.61 ? 52  VAL A O   1 
ATOM   133  C CB  . VAL A 1 19  ? 25.287 29.099  7.467  1.00 18.47 ? 52  VAL A CB  1 
ATOM   134  C CG1 . VAL A 1 19  ? 26.533 28.821  8.312  1.00 20.70 ? 52  VAL A CG1 1 
ATOM   135  C CG2 . VAL A 1 19  ? 25.430 30.462  6.774  1.00 17.95 ? 52  VAL A CG2 1 
ATOM   136  N N   . ALA A 1 20  ? 23.660 26.088  7.137  1.00 12.44 ? 53  ALA A N   1 
ATOM   137  C CA  . ALA A 1 20  ? 23.447 24.766  7.719  1.00 13.54 ? 53  ALA A CA  1 
ATOM   138  C C   . ALA A 1 20  ? 24.276 23.695  7.027  1.00 15.69 ? 53  ALA A C   1 
ATOM   139  O O   . ALA A 1 20  ? 24.698 22.723  7.670  1.00 15.58 ? 53  ALA A O   1 
ATOM   140  C CB  . ALA A 1 20  ? 21.974 24.395  7.642  1.00 14.94 ? 53  ALA A CB  1 
ATOM   141  N N   . ASP A 1 21  ? 24.497 23.822  5.715  1.00 13.05 ? 54  ASP A N   1 
ATOM   142  C CA  . ASP A 1 21  ? 25.167 22.730  5.012  1.00 13.03 ? 54  ASP A CA  1 
ATOM   143  C C   . ASP A 1 21  ? 26.639 22.621  5.391  1.00 16.27 ? 54  ASP A C   1 
ATOM   144  O O   . ASP A 1 21  ? 27.058 21.529  5.819  1.00 18.89 ? 54  ASP A O   1 
ATOM   145  C CB  . ASP A 1 21  ? 24.938 22.854  3.501  1.00 18.18 ? 54  ASP A CB  1 
ATOM   146  C CG  . ASP A 1 21  ? 23.760 22.018  3.043  1.00 24.60 ? 54  ASP A CG  1 
ATOM   147  O OD1 . ASP A 1 21  ? 23.804 20.785  3.256  1.00 28.66 ? 54  ASP A OD1 1 
ATOM   148  O OD2 . ASP A 1 21  ? 22.787 22.586  2.509  1.00 20.58 ? 54  ASP A OD2 1 
ATOM   149  N N   . PRO A 1 22  ? 27.464 23.676  5.297  1.00 15.49 ? 55  PRO A N   1 
ATOM   150  C CA  . PRO A 1 22  ? 28.845 23.537  5.788  1.00 17.48 ? 55  PRO A CA  1 
ATOM   151  C C   . PRO A 1 22  ? 28.923 23.204  7.260  1.00 14.90 ? 55  PRO A C   1 
ATOM   152  O O   . PRO A 1 22  ? 29.802 22.431  7.660  1.00 14.30 ? 55  PRO A O   1 
ATOM   153  C CB  . PRO A 1 22  ? 29.477 24.906  5.482  1.00 15.11 ? 55  PRO A CB  1 
ATOM   154  C CG  . PRO A 1 22  ? 28.344 25.820  5.293  1.00 20.67 ? 55  PRO A CG  1 
ATOM   155  C CD  . PRO A 1 22  ? 27.250 25.000  4.688  1.00 16.11 ? 55  PRO A CD  1 
ATOM   156  N N   . VAL A 1 23  ? 28.022 23.751  8.083  1.00 14.37 ? 56  VAL A N   1 
ATOM   157  C CA  . VAL A 1 23  ? 28.073 23.441  9.510  1.00 14.41 ? 56  VAL A CA  1 
ATOM   158  C C   . VAL A 1 23  ? 27.758 21.969  9.753  1.00 17.47 ? 56  VAL A C   1 
ATOM   159  O O   . VAL A 1 23  ? 28.431 21.305  10.556 1.00 14.48 ? 56  VAL A O   1 
ATOM   160  C CB  . VAL A 1 23  ? 27.133 24.371  10.297 1.00 19.30 ? 56  VAL A CB  1 
ATOM   161  C CG1 . VAL A 1 23  ? 26.981 23.876  11.744 1.00 19.17 ? 56  VAL A CG1 1 
ATOM   162  C CG2 . VAL A 1 23  ? 27.687 25.783  10.271 1.00 14.28 ? 56  VAL A CG2 1 
ATOM   163  N N   . ALA A 1 24  ? 26.739 21.435  9.068  1.00 12.88 ? 57  ALA A N   1 
ATOM   164  C CA  . ALA A 1 24  ? 26.423 20.015  9.197  1.00 14.96 ? 57  ALA A CA  1 
ATOM   165  C C   . ALA A 1 24  ? 27.598 19.151  8.757  1.00 14.79 ? 57  ALA A C   1 
ATOM   166  O O   . ALA A 1 24  ? 27.963 18.195  9.444  1.00 16.11 ? 57  ALA A O   1 
ATOM   167  C CB  . ALA A 1 24  ? 25.177 19.661  8.384  1.00 14.76 ? 57  ALA A CB  1 
ATOM   168  N N   . ALA A 1 25  ? 28.198 19.468  7.605  1.00 13.76 ? 58  ALA A N   1 
ATOM   169  C CA  . ALA A 1 25  ? 29.332 18.680  7.131  1.00 14.75 ? 58  ALA A CA  1 
ATOM   170  C C   . ALA A 1 25  ? 30.470 18.685  8.146  1.00 15.27 ? 58  ALA A C   1 
ATOM   171  O O   . ALA A 1 25  ? 31.091 17.640  8.415  1.00 15.24 ? 58  ALA A O   1 
ATOM   172  C CB  . ALA A 1 25  ? 29.819 19.217  5.787  1.00 16.72 ? 58  ALA A CB  1 
ATOM   173  N N   . PHE A 1 26  ? 30.745 19.857  8.730  1.00 14.65 ? 59  PHE A N   1 
ATOM   174  C CA  . PHE A 1 26  ? 31.816 19.971  9.709  1.00 14.15 ? 59  PHE A CA  1 
ATOM   175  C C   . PHE A 1 26  ? 31.507 19.166  10.968 1.00 15.44 ? 59  PHE A C   1 
ATOM   176  O O   . PHE A 1 26  ? 32.359 18.415  11.458 1.00 15.26 ? 59  PHE A O   1 
ATOM   177  C CB  . PHE A 1 26  ? 32.039 21.443  10.054 1.00 15.30 ? 59  PHE A CB  1 
ATOM   178  C CG  . PHE A 1 26  ? 33.198 21.667  10.973 1.00 16.64 ? 59  PHE A CG  1 
ATOM   179  C CD1 . PHE A 1 26  ? 33.022 21.649  12.350 1.00 15.76 ? 59  PHE A CD1 1 
ATOM   180  C CD2 . PHE A 1 26  ? 34.471 21.880  10.460 1.00 22.53 ? 59  PHE A CD2 1 
ATOM   181  C CE1 . PHE A 1 26  ? 34.090 21.859  13.205 1.00 17.03 ? 59  PHE A CE1 1 
ATOM   182  C CE2 . PHE A 1 26  ? 35.546 22.089  11.306 1.00 23.65 ? 59  PHE A CE2 1 
ATOM   183  C CZ  . PHE A 1 26  ? 35.361 22.071  12.678 1.00 21.14 ? 59  PHE A CZ  1 
ATOM   184  N N   . LYS A 1 27  ? 30.293 19.311  11.502 1.00 13.41 ? 60  LYS A N   1 
ATOM   185  C CA  . LYS A 1 27  ? 29.925 18.602  12.728 1.00 15.25 ? 60  LYS A CA  1 
ATOM   186  C C   . LYS A 1 27  ? 29.933 17.091  12.514 1.00 14.23 ? 60  LYS A C   1 
ATOM   187  O O   . LYS A 1 27  ? 30.294 16.334  13.422 1.00 15.06 ? 60  LYS A O   1 
ATOM   188  C CB  . LYS A 1 27  ? 28.546 19.060  13.213 1.00 15.79 ? 60  LYS A CB  1 
ATOM   189  C CG  . LYS A 1 27  ? 28.497 20.457  13.862 1.00 18.95 ? 60  LYS A CG  1 
ATOM   190  C CD  . LYS A 1 27  ? 27.041 20.857  14.157 1.00 20.29 ? 60  LYS A CD  1 
ATOM   191  C CE  . LYS A 1 27  ? 26.926 22.034  15.110 1.00 26.48 ? 60  LYS A CE  1 
ATOM   192  N NZ  . LYS A 1 27  ? 25.513 22.575  15.148 1.00 29.19 ? 60  LYS A NZ  1 
ATOM   193  N N   . TRP A 1 28  ? 29.521 16.632  11.325 1.00 13.37 ? 61  TRP A N   1 
ATOM   194  C CA  . TRP A 1 28  ? 29.589 15.202  11.020 1.00 13.30 ? 61  TRP A CA  1 
ATOM   195  C C   . TRP A 1 28  ? 31.025 14.703  11.072 1.00 16.37 ? 61  TRP A C   1 
ATOM   196  O O   . TRP A 1 28  ? 31.328 13.709  11.749 1.00 14.11 ? 61  TRP A O   1 
ATOM   197  C CB  . TRP A 1 28  ? 28.985 14.928  9.640  1.00 13.17 ? 61  TRP A CB  1 
ATOM   198  C CG  . TRP A 1 28  ? 28.943 13.475  9.256  1.00 13.99 ? 61  TRP A CG  1 
ATOM   199  C CD1 . TRP A 1 28  ? 29.897 12.777  8.565  1.00 15.50 ? 61  TRP A CD1 1 
ATOM   200  C CD2 . TRP A 1 28  ? 27.880 12.549  9.518  1.00 13.36 ? 61  TRP A CD2 1 
ATOM   201  N NE1 . TRP A 1 28  ? 29.492 11.474  8.384  1.00 14.97 ? 61  TRP A NE1 1 
ATOM   202  C CE2 . TRP A 1 28  ? 28.262 11.307  8.966  1.00 14.64 ? 61  TRP A CE2 1 
ATOM   203  C CE3 . TRP A 1 28  ? 26.638 12.653  10.159 1.00 13.09 ? 61  TRP A CE3 1 
ATOM   204  C CZ2 . TRP A 1 28  ? 27.451 10.175  9.041  1.00 15.63 ? 61  TRP A CZ2 1 
ATOM   205  C CZ3 . TRP A 1 28  ? 25.838 11.528  10.238 1.00 14.90 ? 61  TRP A CZ3 1 
ATOM   206  C CH2 . TRP A 1 28  ? 26.249 10.302  9.677  1.00 15.34 ? 61  TRP A CH2 1 
ATOM   207  N N   . ARG A 1 29  ? 31.932 15.383  10.357 1.00 14.15 ? 62  ARG A N   1 
ATOM   208  C CA  . ARG A 1 29  ? 33.309 14.889  10.303 1.00 14.79 ? 62  ARG A CA  1 
ATOM   209  C C   . ARG A 1 29  ? 33.989 15.016  11.664 1.00 15.95 ? 62  ARG A C   1 
ATOM   210  O O   . ARG A 1 29  ? 34.770 14.140  12.063 1.00 16.52 ? 62  ARG A O   1 
ATOM   211  C CB  . ARG A 1 29  ? 34.092 15.633  9.219  1.00 19.60 ? 62  ARG A CB  1 
ATOM   212  C CG  . ARG A 1 29  ? 35.548 15.221  9.105  1.00 23.63 ? 62  ARG A CG  1 
ATOM   213  N N   . ALA A 1 30  ? 33.675 16.071  12.408 1.00 15.05 ? 63  ALA A N   1 
ATOM   214  C CA  . ALA A 1 30  ? 34.280 16.312  13.711 1.00 16.32 ? 63  ALA A CA  1 
ATOM   215  C C   . ALA A 1 30  ? 33.570 15.584  14.842 1.00 15.44 ? 63  ALA A C   1 
ATOM   216  O O   . ALA A 1 30  ? 33.987 15.724  15.997 1.00 15.97 ? 63  ALA A O   1 
ATOM   217  C CB  . ALA A 1 30  ? 34.302 17.810  14.020 1.00 15.71 ? 63  ALA A CB  1 
ATOM   218  N N   . GLN A 1 31  ? 32.497 14.851  14.544 1.00 14.89 ? 64  GLN A N   1 
ATOM   219  C CA  . GLN A 1 31  ? 31.761 14.077  15.551 1.00 14.90 ? 64  GLN A CA  1 
ATOM   220  C C   . GLN A 1 31  ? 31.240 14.968  16.672 1.00 16.03 ? 64  GLN A C   1 
ATOM   221  O O   . GLN A 1 31  ? 31.275 14.605  17.852 1.00 17.78 ? 64  GLN A O   1 
ATOM   222  C CB  . GLN A 1 31  ? 32.627 12.936  16.091 1.00 15.53 ? 64  GLN A CB  1 
ATOM   223  C CG  . GLN A 1 31  ? 33.038 11.989  14.961 1.00 15.50 ? 64  GLN A CG  1 
ATOM   224  C CD  . GLN A 1 31  ? 33.921 10.828  15.417 1.00 26.96 ? 64  GLN A CD  1 
ATOM   225  O OE1 . GLN A 1 31  ? 33.500 9.678   15.413 1.00 28.24 ? 64  GLN A OE1 1 
ATOM   226  N NE2 . GLN A 1 31  ? 35.155 11.131  15.782 1.00 24.53 ? 64  GLN A NE2 1 
ATOM   227  N N   . LEU A 1 32  ? 30.729 16.138  16.293 1.00 14.55 ? 65  LEU A N   1 
ATOM   228  C CA  . LEU A 1 32  ? 30.125 17.096  17.209 1.00 19.70 ? 65  LEU A CA  1 
ATOM   229  C C   . LEU A 1 32  ? 28.607 16.989  17.176 1.00 17.30 ? 65  LEU A C   1 
ATOM   230  O O   . LEU A 1 32  ? 28.029 16.756  16.112 1.00 15.91 ? 65  LEU A O   1 
ATOM   231  C CB  . LEU A 1 32  ? 30.521 18.522  16.832 1.00 16.11 ? 65  LEU A CB  1 
ATOM   232  C CG  . LEU A 1 32  ? 32.017 18.803  16.845 1.00 20.26 ? 65  LEU A CG  1 
ATOM   233  C CD1 . LEU A 1 32  ? 32.291 20.215  16.335 1.00 20.33 ? 65  LEU A CD1 1 
ATOM   234  C CD2 . LEU A 1 32  ? 32.537 18.617  18.251 1.00 21.89 ? 65  LEU A CD2 1 
ATOM   235  N N   . PRO A 1 33  ? 27.926 17.180  18.305 1.00 18.61 ? 66  PRO A N   1 
ATOM   236  C CA  . PRO A 1 33  ? 26.459 17.207  18.275 1.00 22.41 ? 66  PRO A CA  1 
ATOM   237  C C   . PRO A 1 33  ? 25.936 18.384  17.459 1.00 19.43 ? 66  PRO A C   1 
ATOM   238  O O   . PRO A 1 33  ? 26.523 19.471  17.449 1.00 16.77 ? 66  PRO A O   1 
ATOM   239  C CB  . PRO A 1 33  ? 26.077 17.346  19.756 1.00 20.09 ? 66  PRO A CB  1 
ATOM   240  C CG  . PRO A 1 33  ? 27.273 18.015  20.388 1.00 26.85 ? 66  PRO A CG  1 
ATOM   241  C CD  . PRO A 1 33  ? 28.460 17.425  19.657 1.00 18.80 ? 66  PRO A CD  1 
ATOM   242  N N   . ILE A 1 34  ? 24.803 18.163  16.782 1.00 14.41 ? 67  ILE A N   1 
ATOM   243  C CA  . ILE A 1 34  ? 24.078 19.285  16.184 1.00 14.29 ? 67  ILE A CA  1 
ATOM   244  C C   . ILE A 1 34  ? 23.545 20.195  17.275 1.00 18.16 ? 67  ILE A C   1 
ATOM   245  O O   . ILE A 1 34  ? 23.719 21.417  17.232 1.00 17.88 ? 67  ILE A O   1 
ATOM   246  C CB  . ILE A 1 34  ? 22.922 18.798  15.297 1.00 17.02 ? 67  ILE A CB  1 
ATOM   247  C CG1 . ILE A 1 34  ? 23.434 18.134  14.026 1.00 19.14 ? 67  ILE A CG1 1 
ATOM   248  C CG2 . ILE A 1 34  ? 22.012 19.983  14.946 1.00 17.02 ? 67  ILE A CG2 1 
ATOM   249  C CD1 . ILE A 1 34  ? 22.362 17.287  13.337 1.00 17.91 ? 67  ILE A CD1 1 
ATOM   250  N N   . GLU A 1 35  ? 22.892 19.601  18.270 1.00 15.19 ? 68  GLU A N   1 
ATOM   251  C CA  . GLU A 1 35  ? 22.184 20.368  19.279 1.00 17.07 ? 68  GLU A CA  1 
ATOM   252  C C   . GLU A 1 35  ? 23.184 21.014  20.225 1.00 18.26 ? 68  GLU A C   1 
ATOM   253  O O   . GLU A 1 35  ? 24.155 20.375  20.638 1.00 17.34 ? 68  GLU A O   1 
ATOM   254  C CB  . GLU A 1 35  ? 21.223 19.460  20.050 1.00 14.77 ? 68  GLU A CB  1 
ATOM   255  C CG  . GLU A 1 35  ? 20.088 20.217  20.730 1.00 13.67 ? 68  GLU A CG  1 
ATOM   256  C CD  . GLU A 1 35  ? 18.957 20.544  19.793 1.00 18.70 ? 68  GLU A CD  1 
ATOM   257  O OE1 . GLU A 1 35  ? 19.022 20.151  18.598 1.00 18.41 ? 68  GLU A OE1 1 
ATOM   258  O OE2 . GLU A 1 35  ? 17.993 21.191  20.255 1.00 19.76 ? 68  GLU A OE2 1 
ATOM   259  N N   . ASP A 1 36  ? 22.974 22.295  20.533 1.00 19.16 ? 69  ASP A N   1 
ATOM   260  C CA  . ASP A 1 36  ? 23.810 22.993  21.513 1.00 23.18 ? 69  ASP A CA  1 
ATOM   261  C C   . ASP A 1 36  ? 22.933 24.066  22.169 1.00 17.99 ? 69  ASP A C   1 
ATOM   262  O O   . ASP A 1 36  ? 22.938 25.229  21.752 1.00 19.09 ? 69  ASP A O   1 
ATOM   263  C CB  . ASP A 1 36  ? 25.022 23.584  20.808 1.00 24.93 ? 69  ASP A CB  1 
ATOM   264  C CG  . ASP A 1 36  ? 26.037 24.185  21.761 1.00 30.28 ? 69  ASP A CG  1 
ATOM   265  O OD1 . ASP A 1 36  ? 25.736 24.358  22.959 1.00 28.88 ? 69  ASP A OD1 1 
ATOM   266  O OD2 . ASP A 1 36  ? 27.145 24.503  21.283 1.00 37.38 ? 69  ASP A OD2 1 
ATOM   267  N N   . SER A 1 37  ? 22.224 23.674  23.232 1.00 19.13 ? 70  SER A N   1 
ATOM   268  C CA  . SER A 1 37  ? 21.213 24.563  23.800 1.00 17.61 ? 70  SER A CA  1 
ATOM   269  C C   . SER A 1 37  ? 21.848 25.775  24.464 1.00 19.32 ? 70  SER A C   1 
ATOM   270  O O   . SER A 1 37  ? 21.261 26.864  24.457 1.00 18.66 ? 70  SER A O   1 
ATOM   271  C CB  . SER A 1 37  ? 20.339 23.813  24.806 1.00 17.74 ? 70  SER A CB  1 
ATOM   272  O OG  . SER A 1 37  ? 21.108 23.380  25.918 1.00 21.43 ? 70  SER A OG  1 
ATOM   273  N N   . GLY A 1 38  ? 23.040 25.613  25.039 1.00 18.91 ? 71  GLY A N   1 
ATOM   274  C CA  . GLY A 1 38  ? 23.700 26.754  25.655 1.00 21.50 ? 71  GLY A CA  1 
ATOM   275  C C   . GLY A 1 38  ? 24.124 27.791  24.634 1.00 21.59 ? 71  GLY A C   1 
ATOM   276  O O   . GLY A 1 38  ? 24.003 29.001  24.869 1.00 20.46 ? 71  GLY A O   1 
ATOM   277  N N   . ARG A 1 39  ? 24.633 27.333  23.484 1.00 20.54 ? 72  ARG A N   1 
ATOM   278  C CA  . ARG A 1 39  ? 25.004 28.259  22.420 1.00 19.76 ? 72  ARG A CA  1 
ATOM   279  C C   . ARG A 1 39  ? 23.784 28.992  21.875 1.00 21.81 ? 72  ARG A C   1 
ATOM   280  O O   . ARG A 1 39  ? 23.855 30.193  21.590 1.00 20.72 ? 72  ARG A O   1 
ATOM   281  C CB  . ARG A 1 39  ? 25.734 27.525  21.302 1.00 23.43 ? 72  ARG A CB  1 
ATOM   282  C CG  . ARG A 1 39  ? 26.074 28.422  20.120 1.00 30.47 ? 72  ARG A CG  1 
ATOM   283  C CD  . ARG A 1 39  ? 26.923 27.701  19.083 1.00 42.04 ? 72  ARG A CD  1 
ATOM   284  N NE  . ARG A 1 39  ? 27.961 28.590  18.576 1.00 47.99 ? 72  ARG A NE  1 
ATOM   285  C CZ  . ARG A 1 39  ? 27.994 29.098  17.352 1.00 56.58 ? 72  ARG A CZ  1 
ATOM   286  N NH1 . ARG A 1 39  ? 27.112 28.740  16.431 1.00 59.23 ? 72  ARG A NH1 1 
ATOM   287  N NH2 . ARG A 1 39  ? 28.937 29.985  17.045 1.00 43.37 ? 72  ARG A NH2 1 
ATOM   288  N N   . VAL A 1 40  ? 22.657 28.289  21.727 1.00 17.63 ? 73  VAL A N   1 
ATOM   289  C CA  . VAL A 1 40  ? 21.418 28.937  21.293 1.00 16.67 ? 73  VAL A CA  1 
ATOM   290  C C   . VAL A 1 40  ? 20.995 30.018  22.287 1.00 18.98 ? 73  VAL A C   1 
ATOM   291  O O   . VAL A 1 40  ? 20.607 31.132  21.901 1.00 18.04 ? 73  VAL A O   1 
ATOM   292  C CB  . VAL A 1 40  ? 20.310 27.885  21.106 1.00 16.24 ? 73  VAL A CB  1 
ATOM   293  C CG1 . VAL A 1 40  ? 18.958 28.560  20.867 1.00 17.31 ? 73  VAL A CG1 1 
ATOM   294  C CG2 . VAL A 1 40  ? 20.669 26.933  19.976 1.00 16.74 ? 73  VAL A CG2 1 
ATOM   295  N N   . GLU A 1 41  ? 21.024 29.697  23.582 1.00 16.72 ? 74  GLU A N   1 
ATOM   296  C CA  . GLU A 1 41  ? 20.643 30.706  24.571 1.00 16.85 ? 74  GLU A CA  1 
ATOM   297  C C   . GLU A 1 41  ? 21.536 31.934  24.463 1.00 17.34 ? 74  GLU A C   1 
ATOM   298  O O   . GLU A 1 41  ? 21.046 33.073  24.477 1.00 18.36 ? 74  GLU A O   1 
ATOM   299  C CB  . GLU A 1 41  ? 20.704 30.116  25.983 1.00 17.57 ? 74  GLU A CB  1 
ATOM   300  C CG  . GLU A 1 41  ? 20.581 31.153  27.123 1.00 21.89 ? 74  GLU A CG  1 
ATOM   301  C CD  . GLU A 1 41  ? 19.172 31.720  27.301 1.00 26.29 ? 74  GLU A CD  1 
ATOM   302  O OE1 . GLU A 1 41  ? 18.225 31.267  26.612 1.00 20.70 ? 74  GLU A OE1 1 
ATOM   303  O OE2 . GLU A 1 41  ? 19.010 32.628  28.149 1.00 29.30 ? 74  GLU A OE2 1 
ATOM   304  N N   . GLN A 1 42  ? 22.854 31.727  24.335 1.00 18.19 ? 75  GLN A N   1 
ATOM   305  C CA  . GLN A 1 42  ? 23.753 32.875  24.240 1.00 18.97 ? 75  GLN A CA  1 
ATOM   306  C C   . GLN A 1 42  ? 23.510 33.680  22.963 1.00 18.35 ? 75  GLN A C   1 
ATOM   307  O O   . GLN A 1 42  ? 23.500 34.920  22.996 1.00 19.07 ? 75  GLN A O   1 
ATOM   308  C CB  . GLN A 1 42  ? 25.202 32.410  24.338 1.00 25.11 ? 75  GLN A CB  1 
ATOM   309  C CG  . GLN A 1 42  ? 25.578 32.107  25.772 1.00 29.80 ? 75  GLN A CG  1 
ATOM   310  C CD  . GLN A 1 42  ? 26.857 31.320  25.893 1.00 46.69 ? 75  GLN A CD  1 
ATOM   311  O OE1 . GLN A 1 42  ? 27.309 30.702  24.930 1.00 48.19 ? 75  GLN A OE1 1 
ATOM   312  N NE2 . GLN A 1 42  ? 27.451 31.335  27.084 1.00 53.39 ? 75  GLN A NE2 1 
ATOM   313  N N   . GLN A 1 43  ? 23.287 33.001  21.833 1.00 17.85 ? 76  GLN A N   1 
ATOM   314  C CA  . GLN A 1 43  ? 23.031 33.719  20.585 1.00 17.99 ? 76  GLN A CA  1 
ATOM   315  C C   . GLN A 1 43  ? 21.760 34.551  20.689 1.00 20.22 ? 76  GLN A C   1 
ATOM   316  O O   . GLN A 1 43  ? 21.737 35.730  20.301 1.00 17.33 ? 76  GLN A O   1 
ATOM   317  C CB  . GLN A 1 43  ? 22.928 32.738  19.415 1.00 19.52 ? 76  GLN A CB  1 
ATOM   318  C CG  . GLN A 1 43  ? 24.238 32.104  19.020 1.00 25.32 ? 76  GLN A CG  1 
ATOM   319  C CD  . GLN A 1 43  ? 24.066 30.921  18.072 1.00 42.71 ? 76  GLN A CD  1 
ATOM   320  O OE1 . GLN A 1 43  ? 22.950 30.467  17.804 1.00 38.35 ? 76  GLN A OE1 1 
ATOM   321  N NE2 . GLN A 1 43  ? 25.181 30.414  17.567 1.00 49.23 ? 76  GLN A NE2 1 
ATOM   322  N N   . LEU A 1 44  ? 20.680 33.946  21.202 1.00 16.71 ? 77  LEU A N   1 
ATOM   323  C CA  . LEU A 1 44  ? 19.411 34.667  21.270 1.00 17.91 ? 77  LEU A CA  1 
ATOM   324  C C   . LEU A 1 44  ? 19.482 35.826  22.254 1.00 17.36 ? 77  LEU A C   1 
ATOM   325  O O   . LEU A 1 44  ? 18.898 36.892  22.009 1.00 15.66 ? 77  LEU A O   1 
ATOM   326  C CB  . LEU A 1 44  ? 18.272 33.717  21.639 1.00 17.90 ? 77  LEU A CB  1 
ATOM   327  C CG  . LEU A 1 44  ? 17.953 32.648  20.585 1.00 14.82 ? 77  LEU A CG  1 
ATOM   328  C CD1 . LEU A 1 44  ? 16.923 31.680  21.128 1.00 15.59 ? 77  LEU A CD1 1 
ATOM   329  C CD2 . LEU A 1 44  ? 17.447 33.288  19.284 1.00 14.66 ? 77  LEU A CD2 1 
ATOM   330  N N   . ALA A 1 45  ? 20.175 35.638  23.381 1.00 16.48 ? 78  ALA A N   1 
ATOM   331  C CA  . ALA A 1 45  ? 20.341 36.737  24.324 1.00 17.24 ? 78  ALA A CA  1 
ATOM   332  C C   . ALA A 1 45  ? 21.082 37.898  23.669 1.00 17.55 ? 78  ALA A C   1 
ATOM   333  O O   . ALA A 1 45  ? 20.697 39.069  23.838 1.00 17.73 ? 78  ALA A O   1 
ATOM   334  C CB  . ALA A 1 45  ? 21.083 36.245  25.571 1.00 18.31 ? 78  ALA A CB  1 
ATOM   335  N N   . LYS A 1 46  ? 22.136 37.586  22.894 1.00 17.81 ? 79  LYS A N   1 
ATOM   336  C CA  . LYS A 1 46  ? 22.899 38.641  22.231 1.00 18.37 ? 79  LYS A CA  1 
ATOM   337  C C   . LYS A 1 46  ? 22.046 39.372  21.207 1.00 17.53 ? 79  LYS A C   1 
ATOM   338  O O   . LYS A 1 46  ? 22.108 40.603  21.102 1.00 17.86 ? 79  LYS A O   1 
ATOM   339  C CB  . LYS A 1 46  ? 24.146 38.067  21.558 1.00 19.15 ? 79  LYS A CB  1 
ATOM   340  C CG  . LYS A 1 46  ? 24.839 39.086  20.653 1.00 31.41 ? 79  LYS A CG  1 
ATOM   341  C CD  . LYS A 1 46  ? 26.140 38.573  20.061 1.00 45.80 ? 79  LYS A CD  1 
ATOM   342  C CE  . LYS A 1 46  ? 26.661 39.527  18.985 1.00 45.69 ? 79  LYS A CE  1 
ATOM   343  N NZ  . LYS A 1 46  ? 26.696 40.943  19.460 1.00 51.14 ? 79  LYS A NZ  1 
ATOM   344  N N   . LEU A 1 47  ? 21.248 38.628  20.436 1.00 16.64 ? 80  LEU A N   1 
ATOM   345  C CA  . LEU A 1 47  ? 20.397 39.265  19.432 1.00 17.49 ? 80  LEU A CA  1 
ATOM   346  C C   . LEU A 1 47  ? 19.318 40.125  20.089 1.00 15.83 ? 80  LEU A C   1 
ATOM   347  O O   . LEU A 1 47  ? 18.964 41.195  19.575 1.00 15.82 ? 80  LEU A O   1 
ATOM   348  C CB  . LEU A 1 47  ? 19.786 38.196  18.518 1.00 17.29 ? 80  LEU A CB  1 
ATOM   349  C CG  . LEU A 1 47  ? 20.808 37.493  17.615 1.00 23.48 ? 80  LEU A CG  1 
ATOM   350  C CD1 . LEU A 1 47  ? 20.342 36.089  17.161 1.00 18.40 ? 80  LEU A CD1 1 
ATOM   351  C CD2 . LEU A 1 47  ? 21.147 38.368  16.411 1.00 19.15 ? 80  LEU A CD2 1 
ATOM   352  N N   . GLY A 1 48  ? 18.784 39.680  21.226 1.00 15.83 ? 81  GLY A N   1 
ATOM   353  C CA  . GLY A 1 48  ? 17.848 40.520  21.960 1.00 16.04 ? 81  GLY A CA  1 
ATOM   354  C C   . GLY A 1 48  ? 18.488 41.820  22.411 1.00 17.93 ? 81  GLY A C   1 
ATOM   355  O O   . GLY A 1 48  ? 17.849 42.879  22.395 1.00 17.02 ? 81  GLY A O   1 
ATOM   356  N N   . GLU A 1 49  ? 19.768 41.761  22.804 1.00 17.53 ? 82  GLU A N   1 
ATOM   357  C CA  . GLU A 1 49  ? 20.461 42.991  23.194 1.00 18.57 ? 82  GLU A CA  1 
ATOM   358  C C   . GLU A 1 49  ? 20.789 43.873  21.989 1.00 18.60 ? 82  GLU A C   1 
ATOM   359  O O   . GLU A 1 49  ? 20.754 45.100  22.103 1.00 19.35 ? 82  GLU A O   1 
ATOM   360  C CB  . GLU A 1 49  ? 21.722 42.662  23.990 1.00 23.15 ? 82  GLU A CB  1 
ATOM   361  C CG  . GLU A 1 49  ? 21.432 42.164  25.410 1.00 25.03 ? 82  GLU A CG  1 
ATOM   362  C CD  . GLU A 1 49  ? 20.889 43.256  26.349 1.00 36.43 ? 82  GLU A CD  1 
ATOM   363  O OE1 . GLU A 1 49  ? 19.692 43.610  26.248 1.00 29.72 ? 82  GLU A OE1 1 
ATOM   364  O OE2 . GLU A 1 49  ? 21.663 43.760  27.198 1.00 39.07 ? 82  GLU A OE2 1 
ATOM   365  N N   . ASP A 1 50  ? 21.106 43.278  20.831 1.00 17.90 ? 83  ASP A N   1 
ATOM   366  C CA  . ASP A 1 50  ? 21.279 44.083  19.618 1.00 21.79 ? 83  ASP A CA  1 
ATOM   367  C C   . ASP A 1 50  ? 19.992 44.818  19.271 1.00 21.03 ? 83  ASP A C   1 
ATOM   368  O O   . ASP A 1 50  ? 20.006 46.018  18.930 1.00 21.45 ? 83  ASP A O   1 
ATOM   369  C CB  . ASP A 1 50  ? 21.709 43.198  18.449 1.00 17.97 ? 83  ASP A CB  1 
ATOM   370  C CG  . ASP A 1 50  ? 23.092 42.603  18.646 1.00 28.86 ? 83  ASP A CG  1 
ATOM   371  O OD1 . ASP A 1 50  ? 23.856 43.149  19.474 1.00 28.12 ? 83  ASP A OD1 1 
ATOM   372  O OD2 . ASP A 1 50  ? 23.413 41.601  17.965 1.00 29.64 ? 83  ASP A OD2 1 
ATOM   373  N N   . ALA A 1 51  ? 18.862 44.114  19.385 1.00 16.57 ? 84  ALA A N   1 
ATOM   374  C CA  . ALA A 1 51  ? 17.570 44.745  19.152 1.00 20.42 ? 84  ALA A CA  1 
ATOM   375  C C   . ALA A 1 51  ? 17.338 45.894  20.131 1.00 17.00 ? 84  ALA A C   1 
ATOM   376  O O   . ALA A 1 51  ? 16.966 47.003  19.728 1.00 17.78 ? 84  ALA A O   1 
ATOM   377  C CB  . ALA A 1 51  ? 16.452 43.708  19.254 1.00 16.05 ? 84  ALA A CB  1 
ATOM   378  N N   . ARG A 1 52  ? 17.569 45.652  21.422 1.00 17.55 ? 85  ARG A N   1 
ATOM   379  C CA  . ARG A 1 52  ? 17.340 46.711  22.402 1.00 19.03 ? 85  ARG A CA  1 
ATOM   380  C C   . ARG A 1 52  ? 18.250 47.912  22.150 1.00 22.26 ? 85  ARG A C   1 
ATOM   381  O O   . ARG A 1 52  ? 17.833 49.066  22.324 1.00 19.93 ? 85  ARG A O   1 
ATOM   382  C CB  . ARG A 1 52  ? 17.533 46.181  23.820 1.00 24.40 ? 85  ARG A CB  1 
ATOM   383  C CG  . ARG A 1 52  ? 17.082 47.182  24.874 1.00 25.53 ? 85  ARG A CG  1 
ATOM   384  C CD  . ARG A 1 52  ? 16.992 46.524  26.220 1.00 36.57 ? 85  ARG A CD  1 
ATOM   385  N NE  . ARG A 1 52  ? 18.313 46.253  26.773 1.00 42.83 ? 85  ARG A NE  1 
ATOM   386  C CZ  . ARG A 1 52  ? 18.892 46.993  27.709 1.00 43.08 ? 85  ARG A CZ  1 
ATOM   387  N NH1 . ARG A 1 52  ? 18.289 48.057  28.220 1.00 42.13 ? 85  ARG A NH1 1 
ATOM   388  N NH2 . ARG A 1 52  ? 20.102 46.653  28.147 1.00 40.52 ? 85  ARG A NH2 1 
ATOM   389  N N   . SER A 1 53  ? 19.493 47.663  21.734 1.00 20.27 ? 86  SER A N   1 
ATOM   390  C CA  . SER A 1 53  ? 20.386 48.763  21.388 1.00 20.24 ? 86  SER A CA  1 
ATOM   391  C C   . SER A 1 53  ? 19.783 49.639  20.300 1.00 22.68 ? 86  SER A C   1 
ATOM   392  O O   . SER A 1 53  ? 19.955 50.866  20.318 1.00 20.64 ? 86  SER A O   1 
ATOM   393  C CB  . SER A 1 53  ? 21.746 48.226  20.940 1.00 22.44 ? 86  SER A CB  1 
ATOM   394  O OG  . SER A 1 53  ? 22.498 47.797  22.062 1.00 32.43 ? 86  SER A OG  1 
ATOM   395  N N   . GLN A 1 54  ? 19.081 49.028  19.339 1.00 18.73 ? 87  GLN A N   1 
ATOM   396  C CA  . GLN A 1 54  ? 18.446 49.806  18.274 1.00 18.54 ? 87  GLN A CA  1 
ATOM   397  C C   . GLN A 1 54  ? 17.018 50.257  18.606 1.00 21.16 ? 87  GLN A C   1 
ATOM   398  O O   . GLN A 1 54  ? 16.336 50.810  17.726 1.00 19.41 ? 87  GLN A O   1 
ATOM   399  C CB  . GLN A 1 54  ? 18.454 49.003  16.974 1.00 17.86 ? 87  GLN A CB  1 
ATOM   400  C CG  . GLN A 1 54  ? 19.825 48.473  16.603 1.00 21.68 ? 87  GLN A CG  1 
ATOM   401  C CD  . GLN A 1 54  ? 20.813 49.581  16.321 1.00 21.52 ? 87  GLN A CD  1 
ATOM   402  O OE1 . GLN A 1 54  ? 20.424 50.719  16.042 1.00 19.59 ? 87  GLN A OE1 1 
ATOM   403  N NE2 . GLN A 1 54  ? 22.098 49.257  16.384 1.00 20.15 ? 87  GLN A NE2 1 
ATOM   404  N N   . HIS A 1 55  ? 16.563 50.039  19.848 1.00 21.92 ? 88  HIS A N   1 
ATOM   405  C CA  . HIS A 1 55  ? 15.205 50.364  20.299 1.00 19.94 ? 88  HIS A CA  1 
ATOM   406  C C   . HIS A 1 55  ? 14.147 49.521  19.586 1.00 24.57 ? 88  HIS A C   1 
ATOM   407  O O   . HIS A 1 55  ? 13.001 49.950  19.418 1.00 24.50 ? 88  HIS A O   1 
ATOM   408  C CB  . HIS A 1 55  ? 14.924 51.866  20.152 1.00 24.78 ? 88  HIS A CB  1 
ATOM   409  C CG  . HIS A 1 55  ? 16.022 52.725  20.708 1.00 24.79 ? 88  HIS A CG  1 
ATOM   410  N ND1 . HIS A 1 55  ? 16.862 53.471  19.909 1.00 30.87 ? 88  HIS A ND1 1 
ATOM   411  C CD2 . HIS A 1 55  ? 16.457 52.903  21.977 1.00 31.37 ? 88  HIS A CD2 1 
ATOM   412  C CE1 . HIS A 1 55  ? 17.745 54.098  20.665 1.00 26.72 ? 88  HIS A CE1 1 
ATOM   413  N NE2 . HIS A 1 55  ? 17.522 53.771  21.925 1.00 33.99 ? 88  HIS A NE2 1 
ATOM   414  N N   . ILE A 1 56  ? 14.532 48.290  19.167 1.00 20.25 ? 89  ILE A N   1 
ATOM   415  C CA  . ILE A 1 56  ? 13.624 47.294  18.609 1.00 20.10 ? 89  ILE A CA  1 
ATOM   416  C C   . ILE A 1 56  ? 13.154 46.371  19.728 1.00 22.88 ? 89  ILE A C   1 
ATOM   417  O O   . ILE A 1 56  ? 13.904 46.069  20.662 1.00 21.85 ? 89  ILE A O   1 
ATOM   418  C CB  . ILE A 1 56  ? 14.324 46.497  17.492 1.00 19.85 ? 89  ILE A CB  1 
ATOM   419  C CG1 . ILE A 1 56  ? 15.048 47.444  16.528 1.00 24.33 ? 89  ILE A CG1 1 
ATOM   420  C CG2 . ILE A 1 56  ? 13.333 45.605  16.767 1.00 20.34 ? 89  ILE A CG2 1 
ATOM   421  C CD1 . ILE A 1 56  ? 15.895 46.730  15.491 1.00 19.96 ? 89  ILE A CD1 1 
ATOM   422  N N   . ASP A 1 57  ? 11.902 45.917  19.646 1.00 17.33 ? 90  ASP A N   1 
ATOM   423  C CA  . ASP A 1 57  ? 11.325 45.033  20.661 1.00 18.52 ? 90  ASP A CA  1 
ATOM   424  C C   . ASP A 1 57  ? 12.122 43.729  20.724 1.00 18.91 ? 90  ASP A C   1 
ATOM   425  O O   . ASP A 1 57  ? 12.110 42.955  19.761 1.00 17.37 ? 90  ASP A O   1 
ATOM   426  C CB  . ASP A 1 57  ? 9.846  44.773  20.339 1.00 21.02 ? 90  ASP A CB  1 
ATOM   427  C CG  . ASP A 1 57  ? 9.250  43.585  21.109 1.00 29.62 ? 90  ASP A CG  1 
ATOM   428  O OD1 . ASP A 1 57  ? 9.814  43.140  22.127 1.00 37.89 ? 90  ASP A OD1 1 
ATOM   429  O OD2 . ASP A 1 57  ? 8.188  43.083  20.681 1.00 42.98 ? 90  ASP A OD2 1 
ATOM   430  N N   . PRO A 1 58  ? 12.823 43.456  21.835 1.00 20.01 ? 91  PRO A N   1 
ATOM   431  C CA  . PRO A 1 58  ? 13.692 42.266  21.877 1.00 17.73 ? 91  PRO A CA  1 
ATOM   432  C C   . PRO A 1 58  ? 12.948 40.951  21.757 1.00 18.32 ? 91  PRO A C   1 
ATOM   433  O O   . PRO A 1 58  ? 13.488 40.020  21.153 1.00 15.09 ? 91  PRO A O   1 
ATOM   434  C CB  . PRO A 1 58  ? 14.401 42.390  23.237 1.00 20.96 ? 91  PRO A CB  1 
ATOM   435  C CG  . PRO A 1 58  ? 13.626 43.381  24.003 1.00 25.37 ? 91  PRO A CG  1 
ATOM   436  C CD  . PRO A 1 58  ? 13.003 44.309  23.018 1.00 20.12 ? 91  PRO A CD  1 
ATOM   437  N N   . ASP A 1 59  ? 11.741 40.833  22.330 1.00 16.59 ? 92  ASP A N   1 
ATOM   438  C CA  . ASP A 1 59  ? 11.031 39.550  22.299 1.00 20.67 ? 92  ASP A CA  1 
ATOM   439  C C   . ASP A 1 59  ? 10.578 39.183  20.885 1.00 20.03 ? 92  ASP A C   1 
ATOM   440  O O   . ASP A 1 59  ? 10.621 38.005  20.497 1.00 18.75 ? 92  ASP A O   1 
ATOM   441  C CB  . ASP A 1 59  ? 9.836  39.585  23.250 1.00 19.93 ? 92  ASP A CB  1 
ATOM   442  C CG  . ASP A 1 59  ? 10.251 39.635  24.714 1.00 37.08 ? 92  ASP A CG  1 
ATOM   443  O OD1 . ASP A 1 59  ? 11.376 39.186  25.046 1.00 28.39 ? 92  ASP A OD1 1 
ATOM   444  O OD2 . ASP A 1 59  ? 9.442  40.118  25.536 1.00 46.41 ? 92  ASP A OD2 1 
ATOM   445  N N   . TYR A 1 60  ? 10.144 40.173  20.094 1.00 17.75 ? 93  TYR A N   1 
ATOM   446  C CA  . TYR A 1 60  ? 9.830  39.902  18.692 1.00 17.47 ? 93  TYR A CA  1 
ATOM   447  C C   . TYR A 1 60  ? 11.053 39.361  17.961 1.00 16.55 ? 93  TYR A C   1 
ATOM   448  O O   . TYR A 1 60  ? 10.975 38.355  17.241 1.00 15.25 ? 93  TYR A O   1 
ATOM   449  C CB  . TYR A 1 60  ? 9.330  41.181  18.016 1.00 19.66 ? 93  TYR A CB  1 
ATOM   450  C CG  . TYR A 1 60  ? 9.158  41.052  16.518 1.00 16.69 ? 93  TYR A CG  1 
ATOM   451  C CD1 . TYR A 1 60  ? 10.211 41.332  15.649 1.00 14.80 ? 93  TYR A CD1 1 
ATOM   452  C CD2 . TYR A 1 60  ? 7.945  40.654  15.971 1.00 19.85 ? 93  TYR A CD2 1 
ATOM   453  C CE1 . TYR A 1 60  ? 10.068 41.210  14.281 1.00 15.83 ? 93  TYR A CE1 1 
ATOM   454  C CE2 . TYR A 1 60  ? 7.791  40.530  14.605 1.00 16.06 ? 93  TYR A CE2 1 
ATOM   455  C CZ  . TYR A 1 60  ? 8.854  40.814  13.764 1.00 19.77 ? 93  TYR A CZ  1 
ATOM   456  O OH  . TYR A 1 60  ? 8.699  40.693  12.408 1.00 16.70 ? 93  TYR A OH  1 
ATOM   457  N N   . VAL A 1 61  ? 12.203 39.990  18.192 1.00 14.40 ? 94  VAL A N   1 
ATOM   458  C CA  . VAL A 1 61  ? 13.446 39.599  17.535 1.00 14.00 ? 94  VAL A CA  1 
ATOM   459  C C   . VAL A 1 61  ? 13.882 38.201  17.968 1.00 14.53 ? 94  VAL A C   1 
ATOM   460  O O   . VAL A 1 61  ? 14.276 37.378  17.131 1.00 15.35 ? 94  VAL A O   1 
ATOM   461  C CB  . VAL A 1 61  ? 14.528 40.656  17.808 1.00 14.13 ? 94  VAL A CB  1 
ATOM   462  C CG1 . VAL A 1 61  ? 15.888 40.171  17.402 1.00 13.86 ? 94  VAL A CG1 1 
ATOM   463  C CG2 . VAL A 1 61  ? 14.166 41.946  17.036 1.00 17.15 ? 94  VAL A CG2 1 
ATOM   464  N N   . THR A 1 62  ? 13.827 37.905  19.275 1.00 13.92 ? 95  THR A N   1 
ATOM   465  C CA  . THR A 1 62  ? 14.306 36.596  19.704 1.00 16.35 ? 95  THR A CA  1 
ATOM   466  C C   . THR A 1 62  ? 13.365 35.489  19.253 1.00 14.05 ? 95  THR A C   1 
ATOM   467  O O   . THR A 1 62  ? 13.827 34.385  18.973 1.00 15.94 ? 95  THR A O   1 
ATOM   468  C CB  . THR A 1 62  ? 14.543 36.529  21.224 1.00 17.92 ? 95  THR A CB  1 
ATOM   469  O OG1 . THR A 1 62  ? 13.350 36.835  21.953 1.00 15.94 ? 95  THR A OG1 1 
ATOM   470  C CG2 . THR A 1 62  ? 15.672 37.470  21.646 1.00 18.95 ? 95  THR A CG2 1 
ATOM   471  N N   . ARG A 1 63  ? 12.059 35.755  19.142 1.00 15.47 ? 96  ARG A N   1 
ATOM   472  C CA  . ARG A 1 63  ? 11.189 34.741  18.549 1.00 15.87 ? 96  ARG A CA  1 
ATOM   473  C C   . ARG A 1 63  ? 11.544 34.502  17.080 1.00 16.62 ? 96  ARG A C   1 
ATOM   474  O O   . ARG A 1 63  ? 11.644 33.346  16.626 1.00 14.63 ? 96  ARG A O   1 
ATOM   475  C CB  . ARG A 1 63  ? 9.725  35.159  18.699 1.00 15.33 ? 96  ARG A CB  1 
ATOM   476  C CG  . ARG A 1 63  ? 8.735  34.233  18.024 1.00 17.26 ? 96  ARG A CG  1 
ATOM   477  C CD  . ARG A 1 63  ? 8.919  32.808  18.468 1.00 25.91 ? 96  ARG A CD  1 
ATOM   478  N NE  . ARG A 1 63  ? 8.153  31.884  17.639 1.00 28.71 ? 96  ARG A NE  1 
ATOM   479  C CZ  . ARG A 1 63  ? 6.945  31.433  17.943 1.00 39.44 ? 96  ARG A CZ  1 
ATOM   480  N NH1 . ARG A 1 63  ? 6.331  31.795  19.064 1.00 29.91 ? 96  ARG A NH1 1 
ATOM   481  N NH2 . ARG A 1 63  ? 6.340  30.594  17.105 1.00 35.89 ? 96  ARG A NH2 1 
ATOM   482  N N   . VAL A 1 64  ? 11.756 35.580  16.322 1.00 13.42 ? 97  VAL A N   1 
ATOM   483  C CA  . VAL A 1 64  ? 12.128 35.413  14.913 1.00 15.44 ? 97  VAL A CA  1 
ATOM   484  C C   . VAL A 1 64  ? 13.406 34.588  14.782 1.00 12.93 ? 97  VAL A C   1 
ATOM   485  O O   . VAL A 1 64  ? 13.498 33.663  13.960 1.00 14.48 ? 97  VAL A O   1 
ATOM   486  C CB  . VAL A 1 64  ? 12.281 36.783  14.236 1.00 14.94 ? 97  VAL A CB  1 
ATOM   487  C CG1 . VAL A 1 64  ? 13.042 36.627  12.923 1.00 18.64 ? 97  VAL A CG1 1 
ATOM   488  C CG2 . VAL A 1 64  ? 10.897 37.393  14.007 1.00 17.95 ? 97  VAL A CG2 1 
ATOM   489  N N   . PHE A 1 65  ? 14.418 34.915  15.579 1.00 13.42 ? 98  PHE A N   1 
ATOM   490  C CA  . PHE A 1 65  ? 15.673 34.192  15.425 1.00 12.56 ? 98  PHE A CA  1 
ATOM   491  C C   . PHE A 1 65  ? 15.619 32.786  16.005 1.00 12.41 ? 98  PHE A C   1 
ATOM   492  O O   . PHE A 1 65  ? 16.337 31.911  15.518 1.00 12.35 ? 98  PHE A O   1 
ATOM   493  C CB  . PHE A 1 65  ? 16.831 34.991  16.008 1.00 12.69 ? 98  PHE A CB  1 
ATOM   494  C CG  . PHE A 1 65  ? 17.347 36.032  15.058 1.00 15.04 ? 98  PHE A CG  1 
ATOM   495  C CD1 . PHE A 1 65  ? 18.262 35.696  14.070 1.00 17.91 ? 98  PHE A CD1 1 
ATOM   496  C CD2 . PHE A 1 65  ? 16.877 37.332  15.116 1.00 14.56 ? 98  PHE A CD2 1 
ATOM   497  C CE1 . PHE A 1 65  ? 18.727 36.647  13.187 1.00 16.36 ? 98  PHE A CE1 1 
ATOM   498  C CE2 . PHE A 1 65  ? 17.337 38.288  14.226 1.00 17.38 ? 98  PHE A CE2 1 
ATOM   499  C CZ  . PHE A 1 65  ? 18.259 37.945  13.263 1.00 18.32 ? 98  PHE A CZ  1 
ATOM   500  N N   . ASP A 1 66  ? 14.773 32.526  17.006 1.00 13.13 ? 99  ASP A N   1 
ATOM   501  C CA  . ASP A 1 66  ? 14.579 31.140  17.435 1.00 14.46 ? 99  ASP A CA  1 
ATOM   502  C C   . ASP A 1 66  ? 13.969 30.308  16.319 1.00 14.78 ? 99  ASP A C   1 
ATOM   503  O O   . ASP A 1 66  ? 14.372 29.153  16.108 1.00 12.81 ? 99  ASP A O   1 
ATOM   504  C CB  . ASP A 1 66  ? 13.696 31.075  18.680 1.00 16.00 ? 99  ASP A CB  1 
ATOM   505  C CG  . ASP A 1 66  ? 13.643 29.678  19.279 1.00 19.48 ? 99  ASP A CG  1 
ATOM   506  O OD1 . ASP A 1 66  ? 14.724 29.107  19.561 1.00 17.81 ? 99  ASP A OD1 1 
ATOM   507  O OD2 . ASP A 1 66  ? 12.527 29.154  19.468 1.00 23.57 ? 99  ASP A OD2 1 
ATOM   508  N N   . ASP A 1 67  ? 12.989 30.877  15.602 1.00 14.41 ? 100 ASP A N   1 
ATOM   509  C CA  . ASP A 1 67  ? 12.445 30.218  14.411 1.00 12.39 ? 100 ASP A CA  1 
ATOM   510  C C   . ASP A 1 67  ? 13.545 29.946  13.389 1.00 12.28 ? 100 ASP A C   1 
ATOM   511  O O   . ASP A 1 67  ? 13.636 28.846  12.821 1.00 11.99 ? 100 ASP A O   1 
ATOM   512  C CB  . ASP A 1 67  ? 11.358 31.082  13.754 1.00 12.70 ? 100 ASP A CB  1 
ATOM   513  C CG  . ASP A 1 67  ? 10.120 31.295  14.627 1.00 21.86 ? 100 ASP A CG  1 
ATOM   514  O OD1 . ASP A 1 67  ? 9.900  30.551  15.609 1.00 22.87 ? 100 ASP A OD1 1 
ATOM   515  O OD2 . ASP A 1 67  ? 9.331  32.208  14.282 1.00 17.74 ? 100 ASP A OD2 1 
ATOM   516  N N   . GLN A 1 68  ? 14.361 30.966  13.105 1.00 13.03 ? 101 GLN A N   1 
ATOM   517  C CA  . GLN A 1 68  ? 15.431 30.812  12.120 1.00 13.19 ? 101 GLN A CA  1 
ATOM   518  C C   . GLN A 1 68  ? 16.398 29.709  12.528 1.00 13.63 ? 101 GLN A C   1 
ATOM   519  O O   . GLN A 1 68  ? 16.826 28.903  11.694 1.00 12.03 ? 101 GLN A O   1 
ATOM   520  C CB  . GLN A 1 68  ? 16.183 32.133  11.954 1.00 14.56 ? 101 GLN A CB  1 
ATOM   521  C CG  . GLN A 1 68  ? 17.402 32.074  11.029 1.00 13.24 ? 101 GLN A CG  1 
ATOM   522  C CD  . GLN A 1 68  ? 17.003 32.229  9.571  1.00 14.41 ? 101 GLN A CD  1 
ATOM   523  O OE1 . GLN A 1 68  ? 15.973 32.833  9.255  1.00 14.34 ? 101 GLN A OE1 1 
ATOM   524  N NE2 . GLN A 1 68  ? 17.807 31.677  8.681  1.00 12.30 ? 101 GLN A NE2 1 
ATOM   525  N N   . ILE A 1 69  ? 16.777 29.678  13.805 1.00 11.81 ? 102 ILE A N   1 
ATOM   526  C CA  . ILE A 1 69  ? 17.730 28.679  14.270 1.00 11.70 ? 102 ILE A CA  1 
ATOM   527  C C   . ILE A 1 69  ? 17.116 27.287  14.216 1.00 14.90 ? 102 ILE A C   1 
ATOM   528  O O   . ILE A 1 69  ? 17.782 26.333  13.809 1.00 11.49 ? 102 ILE A O   1 
ATOM   529  C CB  . ILE A 1 69  ? 18.230 29.025  15.683 1.00 12.04 ? 102 ILE A CB  1 
ATOM   530  C CG1 . ILE A 1 69  ? 19.058 30.314  15.632 1.00 13.84 ? 102 ILE A CG1 1 
ATOM   531  C CG2 . ILE A 1 69  ? 19.061 27.884  16.256 1.00 15.80 ? 102 ILE A CG2 1 
ATOM   532  C CD1 . ILE A 1 69  ? 19.314 30.933  17.023 1.00 18.83 ? 102 ILE A CD1 1 
ATOM   533  N N   . ARG A 1 70  ? 15.850 27.141  14.639 1.00 11.64 ? 103 ARG A N   1 
ATOM   534  C CA  . ARG A 1 70  ? 15.187 25.848  14.511 1.00 12.33 ? 103 ARG A CA  1 
ATOM   535  C C   . ARG A 1 70  ? 15.197 25.378  13.060 1.00 12.78 ? 103 ARG A C   1 
ATOM   536  O O   . ARG A 1 70  ? 15.431 24.195  12.786 1.00 12.21 ? 103 ARG A O   1 
ATOM   537  C CB  . ARG A 1 70  ? 13.735 25.924  14.992 1.00 14.00 ? 103 ARG A CB  1 
ATOM   538  C CG  . ARG A 1 70  ? 13.511 25.988  16.492 1.00 18.64 ? 103 ARG A CG  1 
ATOM   539  C CD  . ARG A 1 70  ? 12.030 25.756  16.808 1.00 19.88 ? 103 ARG A CD  1 
ATOM   540  N NE  . ARG A 1 70  ? 11.166 26.854  16.382 1.00 17.23 ? 103 ARG A NE  1 
ATOM   541  C CZ  . ARG A 1 70  ? 10.240 26.771  15.436 1.00 21.75 ? 103 ARG A CZ  1 
ATOM   542  N NH1 . ARG A 1 70  ? 10.055 25.662  14.744 1.00 17.73 ? 103 ARG A NH1 1 
ATOM   543  N NH2 . ARG A 1 70  ? 9.458  27.824  15.195 1.00 20.14 ? 103 ARG A NH2 1 
ATOM   544  N N   . ALA A 1 71  ? 14.903 26.284  12.123 1.00 12.04 ? 104 ALA A N   1 
ATOM   545  C CA  . ALA A 1 71  ? 14.890 25.907  10.709 1.00 11.63 ? 104 ALA A CA  1 
ATOM   546  C C   . ALA A 1 71  ? 16.276 25.466  10.225 1.00 13.45 ? 104 ALA A C   1 
ATOM   547  O O   . ALA A 1 71  ? 16.412 24.504  9.442  1.00 14.45 ? 104 ALA A O   1 
ATOM   548  C CB  . ALA A 1 71  ? 14.367 27.079  9.883  1.00 11.84 ? 104 ALA A CB  1 
ATOM   549  N N   . THR A 1 72  ? 17.316 26.177  10.664 1.00 13.35 ? 105 THR A N   1 
ATOM   550  C CA  . THR A 1 72  ? 18.688 25.799  10.326 1.00 12.05 ? 105 THR A CA  1 
ATOM   551  C C   . THR A 1 72  ? 19.025 24.409  10.879 1.00 14.41 ? 105 THR A C   1 
ATOM   552  O O   . THR A 1 72  ? 19.589 23.549  10.179 1.00 14.84 ? 105 THR A O   1 
ATOM   553  C CB  . THR A 1 72  ? 19.647 26.854  10.899 1.00 13.66 ? 105 THR A CB  1 
ATOM   554  O OG1 . THR A 1 72  ? 19.195 28.172  10.532 1.00 13.17 ? 105 THR A OG1 1 
ATOM   555  C CG2 . THR A 1 72  ? 21.053 26.653  10.379 1.00 14.48 ? 105 THR A CG2 1 
ATOM   556  N N   . GLU A 1 73  ? 18.703 24.184  12.157 1.00 13.52 ? 106 GLU A N   1 
ATOM   557  C CA  . GLU A 1 73  ? 18.943 22.878  12.766 1.00 12.84 ? 106 GLU A CA  1 
ATOM   558  C C   . GLU A 1 73  ? 18.166 21.786  12.034 1.00 11.19 ? 106 GLU A C   1 
ATOM   559  O O   . GLU A 1 73  ? 18.647 20.656  11.898 1.00 13.55 ? 106 GLU A O   1 
ATOM   560  C CB  . GLU A 1 73  ? 18.570 22.923  14.261 1.00 13.82 ? 106 GLU A CB  1 
ATOM   561  C CG  . GLU A 1 73  ? 19.528 23.785  15.092 1.00 14.92 ? 106 GLU A CG  1 
ATOM   562  C CD  . GLU A 1 73  ? 19.036 24.076  16.501 1.00 17.92 ? 106 GLU A CD  1 
ATOM   563  O OE1 . GLU A 1 73  ? 17.807 24.039  16.738 1.00 16.18 ? 106 GLU A OE1 1 
ATOM   564  O OE2 . GLU A 1 73  ? 19.896 24.344  17.365 1.00 19.27 ? 106 GLU A OE2 1 
ATOM   565  N N   . ALA A 1 74  ? 16.958 22.099  11.561 1.00 12.83 ? 107 ALA A N   1 
ATOM   566  C CA  . ALA A 1 74  ? 16.174 21.089  10.853 1.00 14.62 ? 107 ALA A CA  1 
ATOM   567  C C   . ALA A 1 74  ? 16.898 20.617  9.596  1.00 11.35 ? 107 ALA A C   1 
ATOM   568  O O   . ALA A 1 74  ? 16.896 19.415  9.275  1.00 12.32 ? 107 ALA A O   1 
ATOM   569  C CB  . ALA A 1 74  ? 14.802 21.648  10.488 1.00 11.91 ? 107 ALA A CB  1 
ATOM   570  N N   . ILE A 1 75  ? 17.525 21.556  8.877  1.00 12.95 ? 108 ILE A N   1 
ATOM   571  C CA  . ILE A 1 75  ? 18.335 21.166  7.712  1.00 11.54 ? 108 ILE A CA  1 
ATOM   572  C C   . ILE A 1 75  ? 19.491 20.261  8.134  1.00 12.28 ? 108 ILE A C   1 
ATOM   573  O O   . ILE A 1 75  ? 19.796 19.252  7.471  1.00 11.68 ? 108 ILE A O   1 
ATOM   574  C CB  . ILE A 1 75  ? 18.861 22.411  6.974  1.00 11.74 ? 108 ILE A CB  1 
ATOM   575  C CG1 . ILE A 1 75  ? 17.687 23.255  6.466  1.00 13.15 ? 108 ILE A CG1 1 
ATOM   576  C CG2 . ILE A 1 75  ? 19.831 21.988  5.837  1.00 15.02 ? 108 ILE A CG2 1 
ATOM   577  C CD1 . ILE A 1 75  ? 18.071 24.659  6.032  1.00 13.86 ? 108 ILE A CD1 1 
ATOM   578  N N   . GLU A 1 76  ? 20.180 20.624  9.216  1.00 11.44 ? 109 GLU A N   1 
ATOM   579  C CA  . GLU A 1 76  ? 21.291 19.778  9.670  1.00 11.49 ? 109 GLU A CA  1 
ATOM   580  C C   . GLU A 1 76  ? 20.824 18.359  10.027 1.00 12.93 ? 109 GLU A C   1 
ATOM   581  O O   . GLU A 1 76  ? 21.496 17.371  9.701  1.00 11.48 ? 109 GLU A O   1 
ATOM   582  C CB  . GLU A 1 76  ? 21.986 20.419  10.871 1.00 11.52 ? 109 GLU A CB  1 
ATOM   583  C CG  . GLU A 1 76  ? 22.529 21.810  10.600 1.00 11.69 ? 109 GLU A CG  1 
ATOM   584  C CD  . GLU A 1 76  ? 23.116 22.439  11.853 1.00 23.78 ? 109 GLU A CD  1 
ATOM   585  O OE1 . GLU A 1 76  ? 23.993 21.815  12.485 1.00 22.34 ? 109 GLU A OE1 1 
ATOM   586  O OE2 . GLU A 1 76  ? 22.691 23.547  12.214 1.00 25.80 ? 109 GLU A OE2 1 
ATOM   587  N N   . TYR A 1 77  ? 19.691 18.236  10.730 1.00 11.22 ? 110 TYR A N   1 
ATOM   588  C CA  . TYR A 1 77  ? 19.185 16.906  11.077 1.00 13.03 ? 110 TYR A CA  1 
ATOM   589  C C   . TYR A 1 77  ? 18.816 16.106  9.829  1.00 13.14 ? 110 TYR A C   1 
ATOM   590  O O   . TYR A 1 77  ? 19.039 14.885  9.772  1.00 12.15 ? 110 TYR A O   1 
ATOM   591  C CB  . TYR A 1 77  ? 17.980 17.007  12.018 1.00 11.11 ? 110 TYR A CB  1 
ATOM   592  C CG  . TYR A 1 77  ? 18.372 17.224  13.463 1.00 12.19 ? 110 TYR A CG  1 
ATOM   593  C CD1 . TYR A 1 77  ? 18.669 16.149  14.294 1.00 13.89 ? 110 TYR A CD1 1 
ATOM   594  C CD2 . TYR A 1 77  ? 18.445 18.501  13.995 1.00 14.93 ? 110 TYR A CD2 1 
ATOM   595  C CE1 . TYR A 1 77  ? 19.035 16.344  15.616 1.00 16.67 ? 110 TYR A CE1 1 
ATOM   596  C CE2 . TYR A 1 77  ? 18.806 18.710  15.326 1.00 13.09 ? 110 TYR A CE2 1 
ATOM   597  C CZ  . TYR A 1 77  ? 19.104 17.621  16.127 1.00 15.88 ? 110 TYR A CZ  1 
ATOM   598  O OH  . TYR A 1 77  ? 19.461 17.809  17.440 1.00 14.48 ? 110 TYR A OH  1 
ATOM   599  N N   . SER A 1 78  ? 18.234 16.769  8.825  1.00 11.34 ? 111 SER A N   1 
ATOM   600  C CA  . SER A 1 78  ? 17.909 16.077  7.577  1.00 11.52 ? 111 SER A CA  1 
ATOM   601  C C   . SER A 1 78  ? 19.167 15.547  6.892  1.00 11.95 ? 111 SER A C   1 
ATOM   602  O O   . SER A 1 78  ? 19.203 14.397  6.410  1.00 12.31 ? 111 SER A O   1 
ATOM   603  C CB  . SER A 1 78  ? 17.155 17.021  6.637  1.00 11.68 ? 111 SER A CB  1 
ATOM   604  O OG  . SER A 1 78  ? 16.813 16.347  5.434  1.00 14.35 ? 111 SER A OG  1 
ATOM   605  N N   . ARG A 1 79  ? 20.213 16.382  6.819  1.00 11.74 ? 112 ARG A N   1 
ATOM   606  C CA  . ARG A 1 79  ? 21.480 15.897  6.270  1.00 12.31 ? 112 ARG A CA  1 
ATOM   607  C C   . ARG A 1 79  ? 22.006 14.704  7.059  1.00 13.76 ? 112 ARG A C   1 
ATOM   608  O O   . ARG A 1 79  ? 22.519 13.747  6.472  1.00 12.16 ? 112 ARG A O   1 
ATOM   609  C CB  . ARG A 1 79  ? 22.543 16.995  6.262  1.00 13.28 ? 112 ARG A CB  1 
ATOM   610  C CG  . ARG A 1 79  ? 22.186 18.242  5.504  1.00 12.99 ? 112 ARG A CG  1 
ATOM   611  C CD  . ARG A 1 79  ? 21.638 17.923  4.124  1.00 15.96 ? 112 ARG A CD  1 
ATOM   612  N NE  . ARG A 1 79  ? 21.595 19.127  3.301  1.00 19.82 ? 112 ARG A NE  1 
ATOM   613  C CZ  . ARG A 1 79  ? 20.737 19.335  2.313  1.00 18.16 ? 112 ARG A CZ  1 
ATOM   614  N NH1 . ARG A 1 79  ? 19.801 18.447  2.011  1.00 17.33 ? 112 ARG A NH1 1 
ATOM   615  N NH2 . ARG A 1 79  ? 20.823 20.460  1.607  1.00 19.57 ? 112 ARG A NH2 1 
ATOM   616  N N   . PHE A 1 80  ? 21.957 14.769  8.394  1.00 11.72 ? 113 PHE A N   1 
ATOM   617  C CA  . PHE A 1 80  ? 22.480 13.650  9.164  1.00 11.74 ? 113 PHE A CA  1 
ATOM   618  C C   . PHE A 1 80  ? 21.688 12.384  8.873  1.00 14.67 ? 113 PHE A C   1 
ATOM   619  O O   . PHE A 1 80  ? 22.256 11.292  8.837  1.00 13.35 ? 113 PHE A O   1 
ATOM   620  C CB  . PHE A 1 80  ? 22.471 13.952  10.673 1.00 11.60 ? 113 PHE A CB  1 
ATOM   621  C CG  . PHE A 1 80  ? 23.689 14.697  11.157 1.00 12.92 ? 113 PHE A CG  1 
ATOM   622  C CD1 . PHE A 1 80  ? 24.260 15.706  10.393 1.00 15.15 ? 113 PHE A CD1 1 
ATOM   623  C CD2 . PHE A 1 80  ? 24.248 14.405  12.393 1.00 12.71 ? 113 PHE A CD2 1 
ATOM   624  C CE1 . PHE A 1 80  ? 25.373 16.398  10.839 1.00 14.34 ? 113 PHE A CE1 1 
ATOM   625  C CE2 . PHE A 1 80  ? 25.366 15.102  12.854 1.00 14.29 ? 113 PHE A CE2 1 
ATOM   626  C CZ  . PHE A 1 80  ? 25.920 16.104  12.081 1.00 12.54 ? 113 PHE A CZ  1 
ATOM   627  N N   . SER A 1 81  ? 20.377 12.510  8.657  1.00 13.41 ? 114 SER A N   1 
ATOM   628  C CA  . SER A 1 81  ? 19.581 11.335  8.294  1.00 14.22 ? 114 SER A CA  1 
ATOM   629  C C   . SER A 1 81  ? 20.087 10.720  6.989  1.00 17.78 ? 114 SER A C   1 
ATOM   630  O O   . SER A 1 81  ? 20.343 9.504   6.905  1.00 15.37 ? 114 SER A O   1 
ATOM   631  C CB  . SER A 1 81  ? 18.104 11.720  8.174  1.00 14.81 ? 114 SER A CB  1 
ATOM   632  O OG  . SER A 1 81  ? 17.325 10.633  7.696  1.00 13.51 ? 114 SER A OG  1 
ATOM   633  N N   . ASP A 1 82  ? 20.296 11.570  5.972  1.00 12.06 ? 115 ASP A N   1 
ATOM   634  C CA  . ASP A 1 82  ? 20.849 11.087  4.701  1.00 13.62 ? 115 ASP A CA  1 
ATOM   635  C C   . ASP A 1 82  ? 22.204 10.408  4.894  1.00 13.96 ? 115 ASP A C   1 
ATOM   636  O O   . ASP A 1 82  ? 22.474 9.352   4.303  1.00 13.22 ? 115 ASP A O   1 
ATOM   637  C CB  . ASP A 1 82  ? 21.007 12.243  3.706  1.00 14.05 ? 115 ASP A CB  1 
ATOM   638  C CG  . ASP A 1 82  ? 19.686 12.803  3.212  1.00 20.30 ? 115 ASP A CG  1 
ATOM   639  O OD1 . ASP A 1 82  ? 18.644 12.116  3.332  1.00 15.86 ? 115 ASP A OD1 1 
ATOM   640  O OD2 . ASP A 1 82  ? 19.708 13.946  2.680  1.00 17.83 ? 115 ASP A OD2 1 
ATOM   641  N N   . TRP A 1 83  ? 23.087 11.019  5.686  1.00 12.76 ? 116 TRP A N   1 
ATOM   642  C CA  . TRP A 1 83  ? 24.440 10.484  5.837  1.00 12.99 ? 116 TRP A CA  1 
ATOM   643  C C   . TRP A 1 83  ? 24.467 9.234   6.723  1.00 12.74 ? 116 TRP A C   1 
ATOM   644  O O   . TRP A 1 83  ? 25.352 8.390   6.565  1.00 14.45 ? 116 TRP A O   1 
ATOM   645  C CB  . TRP A 1 83  ? 25.373 11.578  6.370  1.00 13.27 ? 116 TRP A CB  1 
ATOM   646  C CG  . TRP A 1 83  ? 25.385 12.816  5.469  1.00 13.07 ? 116 TRP A CG  1 
ATOM   647  C CD1 . TRP A 1 83  ? 25.077 12.863  4.123  1.00 15.46 ? 116 TRP A CD1 1 
ATOM   648  C CD2 . TRP A 1 83  ? 25.722 14.166  5.847  1.00 13.05 ? 116 TRP A CD2 1 
ATOM   649  N NE1 . TRP A 1 83  ? 25.208 14.159  3.653  1.00 19.27 ? 116 TRP A NE1 1 
ATOM   650  C CE2 . TRP A 1 83  ? 25.593 14.974  4.690  1.00 16.84 ? 116 TRP A CE2 1 
ATOM   651  C CE3 . TRP A 1 83  ? 26.100 14.771  7.053  1.00 12.92 ? 116 TRP A CE3 1 
ATOM   652  C CZ2 . TRP A 1 83  ? 25.843 16.351  4.707  1.00 13.35 ? 116 TRP A CZ2 1 
ATOM   653  C CZ3 . TRP A 1 83  ? 26.358 16.143  7.066  1.00 12.99 ? 116 TRP A CZ3 1 
ATOM   654  C CH2 . TRP A 1 83  ? 26.230 16.914  5.893  1.00 16.27 ? 116 TRP A CH2 1 
ATOM   655  N N   . LYS A 1 84  ? 23.512 9.086   7.641  1.00 14.41 ? 117 LYS A N   1 
ATOM   656  C CA  . LYS A 1 84  ? 23.377 7.828   8.366  1.00 15.95 ? 117 LYS A CA  1 
ATOM   657  C C   . LYS A 1 84  ? 23.042 6.705   7.406  1.00 16.82 ? 117 LYS A C   1 
ATOM   658  O O   . LYS A 1 84  ? 23.566 5.590   7.539  1.00 15.21 ? 117 LYS A O   1 
ATOM   659  C CB  . LYS A 1 84  ? 22.292 7.927   9.449  1.00 12.96 ? 117 LYS A CB  1 
ATOM   660  C CG  . LYS A 1 84  ? 22.697 8.675   10.708 1.00 16.46 ? 117 LYS A CG  1 
ATOM   661  C CD  . LYS A 1 84  ? 23.545 7.810   11.628 1.00 15.98 ? 117 LYS A CD  1 
ATOM   662  C CE  . LYS A 1 84  ? 23.898 8.549   12.915 1.00 16.98 ? 117 LYS A CE  1 
ATOM   663  N NZ  . LYS A 1 84  ? 24.605 7.641   13.872 1.00 17.80 ? 117 LYS A NZ  1 
ATOM   664  N N   . LEU A 1 85  ? 22.148 6.980   6.440  1.00 15.00 ? 118 LEU A N   1 
ATOM   665  C CA  . LEU A 1 85  ? 21.820 5.959   5.444  1.00 16.80 ? 118 LEU A CA  1 
ATOM   666  C C   . LEU A 1 85  ? 23.005 5.640   4.532  1.00 23.40 ? 118 LEU A C   1 
ATOM   667  O O   . LEU A 1 85  ? 23.163 4.485   4.111  1.00 22.97 ? 118 LEU A O   1 
ATOM   668  C CB  . LEU A 1 85  ? 20.603 6.394   4.609  1.00 13.85 ? 118 LEU A CB  1 
ATOM   669  C CG  . LEU A 1 85  ? 19.333 6.465   5.463  1.00 16.46 ? 118 LEU A CG  1 
ATOM   670  C CD1 . LEU A 1 85  ? 18.179 7.137   4.751  1.00 20.50 ? 118 LEU A CD1 1 
ATOM   671  C CD2 . LEU A 1 85  ? 18.941 5.050   5.961  1.00 17.05 ? 118 LEU A CD2 1 
ATOM   672  N N   . ASN A 1 86  ? 23.843 6.629   4.222  1.00 19.83 ? 119 ASN A N   1 
ATOM   673  C CA  . ASN A 1 86  ? 24.984 6.433   3.324  1.00 21.17 ? 119 ASN A CA  1 
ATOM   674  C C   . ASN A 1 86  ? 26.140 7.335   3.750  1.00 19.30 ? 119 ASN A C   1 
ATOM   675  O O   . ASN A 1 86  ? 26.307 8.452   3.228  1.00 18.97 ? 119 ASN A O   1 
ATOM   676  C CB  . ASN A 1 86  ? 24.598 6.705   1.872  1.00 23.01 ? 119 ASN A CB  1 
ATOM   677  C CG  . ASN A 1 86  ? 25.748 6.476   0.914  1.00 28.83 ? 119 ASN A CG  1 
ATOM   678  O OD1 . ASN A 1 86  ? 26.775 5.913   1.284  1.00 30.52 ? 119 ASN A OD1 1 
ATOM   679  N ND2 . ASN A 1 86  ? 25.577 6.911   -0.331 1.00 30.74 ? 119 ASN A ND2 1 
ATOM   680  N N   . PRO A 1 87  ? 26.971 6.877   4.692  1.00 19.31 ? 120 PRO A N   1 
ATOM   681  C CA  . PRO A 1 87  ? 28.061 7.733   5.196  1.00 17.78 ? 120 PRO A CA  1 
ATOM   682  C C   . PRO A 1 87  ? 29.057 8.156   4.125  1.00 22.27 ? 120 PRO A C   1 
ATOM   683  O O   . PRO A 1 87  ? 29.706 9.199   4.279  1.00 22.38 ? 120 PRO A O   1 
ATOM   684  C CB  . PRO A 1 87  ? 28.719 6.858   6.272  1.00 21.35 ? 120 PRO A CB  1 
ATOM   685  C CG  . PRO A 1 87  ? 27.603 5.962   6.747  1.00 20.60 ? 120 PRO A CG  1 
ATOM   686  C CD  . PRO A 1 87  ? 26.833 5.639   5.484  1.00 21.97 ? 120 PRO A CD  1 
ATOM   687  N N   . ALA A 1 88  ? 29.182 7.394   3.036  1.00 23.89 ? 121 ALA A N   1 
ATOM   688  C CA  . ALA A 1 88  ? 30.076 7.783   1.946  1.00 25.04 ? 121 ALA A CA  1 
ATOM   689  C C   . ALA A 1 88  ? 29.639 9.063   1.251  1.00 25.86 ? 121 ALA A C   1 
ATOM   690  O O   . ALA A 1 88  ? 30.432 9.651   0.511  1.00 26.72 ? 121 ALA A O   1 
ATOM   691  C CB  . ALA A 1 88  ? 30.168 6.663   0.903  1.00 23.99 ? 121 ALA A CB  1 
ATOM   692  N N   . SER A 1 89  ? 28.394 9.488   1.433  1.00 22.79 ? 122 SER A N   1 
ATOM   693  C CA  . SER A 1 89  ? 27.899 10.680  0.765  1.00 24.60 ? 122 SER A CA  1 
ATOM   694  C C   . SER A 1 89  ? 28.108 11.947  1.578  1.00 24.11 ? 122 SER A C   1 
ATOM   695  O O   . SER A 1 89  ? 27.800 13.033  1.081  1.00 22.96 ? 122 SER A O   1 
ATOM   696  C CB  . SER A 1 89  ? 26.413 10.523  0.431  1.00 23.13 ? 122 SER A CB  1 
ATOM   697  O OG  . SER A 1 89  ? 25.634 10.419  1.602  1.00 23.44 ? 122 SER A OG  1 
ATOM   698  N N   . ALA A 1 90  ? 28.616 11.841  2.806  1.00 18.36 ? 123 ALA A N   1 
ATOM   699  C CA  . ALA A 1 90  ? 28.898 13.036  3.589  1.00 18.71 ? 123 ALA A CA  1 
ATOM   700  C C   . ALA A 1 90  ? 29.968 13.859  2.876  1.00 26.24 ? 123 ALA A C   1 
ATOM   701  O O   . ALA A 1 90  ? 31.045 13.332  2.570  1.00 23.25 ? 123 ALA A O   1 
ATOM   702  C CB  . ALA A 1 90  ? 29.351 12.662  5.003  1.00 20.58 ? 123 ALA A CB  1 
ATOM   703  N N   . PRO A 1 91  ? 29.719 15.134  2.594  1.00 23.62 ? 124 PRO A N   1 
ATOM   704  C CA  . PRO A 1 91  ? 30.567 15.873  1.652  1.00 29.40 ? 124 PRO A CA  1 
ATOM   705  C C   . PRO A 1 91  ? 31.767 16.484  2.352  1.00 30.08 ? 124 PRO A C   1 
ATOM   706  O O   . PRO A 1 91  ? 31.784 16.591  3.586  1.00 27.52 ? 124 PRO A O   1 
ATOM   707  C CB  . PRO A 1 91  ? 29.620 16.960  1.127  1.00 25.01 ? 124 PRO A CB  1 
ATOM   708  C CG  . PRO A 1 91  ? 28.778 17.271  2.329  1.00 26.82 ? 124 PRO A CG  1 
ATOM   709  C CD  . PRO A 1 91  ? 28.585 15.951  3.054  1.00 24.00 ? 124 PRO A CD  1 
ATOM   710  N N   . PRO A 1 92  ? 32.784 16.911  1.597  1.00 30.22 ? 125 PRO A N   1 
ATOM   711  C CA  . PRO A 1 92  ? 33.930 17.583  2.221  1.00 30.59 ? 125 PRO A CA  1 
ATOM   712  C C   . PRO A 1 92  ? 33.496 18.804  3.022  1.00 31.14 ? 125 PRO A C   1 
ATOM   713  O O   . PRO A 1 92  ? 32.681 19.619  2.579  1.00 28.44 ? 125 PRO A O   1 
ATOM   714  C CB  . PRO A 1 92  ? 34.805 17.971  1.025  1.00 32.64 ? 125 PRO A CB  1 
ATOM   715  C CG  . PRO A 1 92  ? 34.463 16.957  -0.021 1.00 34.96 ? 125 PRO A CG  1 
ATOM   716  C CD  . PRO A 1 92  ? 32.999 16.672  0.157  1.00 32.63 ? 125 PRO A CD  1 
ATOM   717  N N   . GLU A 1 93  ? 34.041 18.914  4.200  1.00 29.12 ? 126 GLU A N   1 
ATOM   718  C CA  . GLU A 1 93  ? 33.636 19.950  5.123  1.00 28.16 ? 126 GLU A CA  1 
ATOM   719  C C   . GLU A 1 93  ? 34.592 21.127  5.032  1.00 33.62 ? 126 GLU A C   1 
ATOM   720  O O   . GLU A 1 93  ? 35.710 20.997  4.524  1.00 31.05 ? 126 GLU A O   1 
ATOM   721  C CB  . GLU A 1 93  ? 33.610 19.397  6.554  1.00 26.67 ? 126 GLU A CB  1 
ATOM   722  C CG  . GLU A 1 93  ? 34.979 19.306  7.216  1.00 30.52 ? 126 GLU A CG  1 
ATOM   723  C CD  . GLU A 1 93  ? 35.811 18.160  6.694  1.00 38.31 ? 126 GLU A CD  1 
ATOM   724  O OE1 . GLU A 1 93  ? 35.301 17.391  5.846  1.00 42.96 ? 126 GLU A OE1 1 
ATOM   725  O OE2 . GLU A 1 93  ? 36.977 18.024  7.134  1.00 41.79 ? 126 GLU A OE2 1 
ATOM   726  N N   . PRO A 1 94  ? 34.181 22.305  5.489  1.00 22.01 ? 127 PRO A N   1 
ATOM   727  C CA  . PRO A 1 94  ? 35.104 23.445  5.505  1.00 28.24 ? 127 PRO A CA  1 
ATOM   728  C C   . PRO A 1 94  ? 36.240 23.193  6.479  1.00 26.14 ? 127 PRO A C   1 
ATOM   729  O O   . PRO A 1 94  ? 36.098 22.385  7.414  1.00 27.70 ? 127 PRO A O   1 
ATOM   730  C CB  . PRO A 1 94  ? 34.216 24.616  5.956  1.00 24.08 ? 127 PRO A CB  1 
ATOM   731  C CG  . PRO A 1 94  ? 33.098 23.974  6.711  1.00 24.00 ? 127 PRO A CG  1 
ATOM   732  C CD  . PRO A 1 94  ? 32.855 22.651  6.041  1.00 20.61 ? 127 PRO A CD  1 
ATOM   733  N N   . PRO A 1 95  ? 37.397 23.838  6.281  1.00 28.31 ? 128 PRO A N   1 
ATOM   734  C CA  . PRO A 1 95  ? 38.522 23.612  7.208  1.00 30.49 ? 128 PRO A CA  1 
ATOM   735  C C   . PRO A 1 95  ? 38.213 24.028  8.637  1.00 34.96 ? 128 PRO A C   1 
ATOM   736  O O   . PRO A 1 95  ? 38.769 23.450  9.579  1.00 27.41 ? 128 PRO A O   1 
ATOM   737  C CB  . PRO A 1 95  ? 39.652 24.453  6.604  1.00 28.79 ? 128 PRO A CB  1 
ATOM   738  C CG  . PRO A 1 95  ? 38.951 25.509  5.809  1.00 32.52 ? 128 PRO A CG  1 
ATOM   739  C CD  . PRO A 1 95  ? 37.702 24.867  5.270  1.00 26.49 ? 128 PRO A CD  1 
ATOM   740  N N   . ASP A 1 96  ? 37.336 25.008  8.823  1.00 22.35 ? 129 ASP A N   1 
ATOM   741  C CA  . ASP A 1 96  ? 36.890 25.434  10.143 1.00 26.96 ? 129 ASP A CA  1 
ATOM   742  C C   . ASP A 1 96  ? 35.598 26.214  9.948  1.00 26.90 ? 129 ASP A C   1 
ATOM   743  O O   . ASP A 1 96  ? 35.116 26.372  8.825  1.00 24.18 ? 129 ASP A O   1 
ATOM   744  C CB  . ASP A 1 96  ? 37.956 26.266  10.866 1.00 26.09 ? 129 ASP A CB  1 
ATOM   745  C CG  . ASP A 1 96  ? 38.395 27.479  10.068 1.00 32.53 ? 129 ASP A CG  1 
ATOM   746  O OD1 . ASP A 1 96  ? 37.558 28.382  9.847  1.00 31.52 ? 129 ASP A OD1 1 
ATOM   747  O OD2 . ASP A 1 96  ? 39.582 27.532  9.667  1.00 32.48 ? 129 ASP A OD2 1 
ATOM   748  N N   . LEU A 1 97  ? 35.029 26.697  11.050 1.00 19.97 ? 130 LEU A N   1 
ATOM   749  C CA  . LEU A 1 97  ? 33.758 27.408  10.985 1.00 21.34 ? 130 LEU A CA  1 
ATOM   750  C C   . LEU A 1 97  ? 33.916 28.910  11.176 1.00 20.00 ? 130 LEU A C   1 
ATOM   751  O O   . LEU A 1 97  ? 32.918 29.606  11.399 1.00 18.26 ? 130 LEU A O   1 
ATOM   752  C CB  . LEU A 1 97  ? 32.781 26.836  12.009 1.00 20.91 ? 130 LEU A CB  1 
ATOM   753  C CG  . LEU A 1 97  ? 32.335 25.400  11.737 1.00 24.91 ? 130 LEU A CG  1 
ATOM   754  C CD1 . LEU A 1 97  ? 31.255 24.997  12.725 1.00 24.60 ? 130 LEU A CD1 1 
ATOM   755  C CD2 . LEU A 1 97  ? 31.849 25.234  10.294 1.00 22.31 ? 130 LEU A CD2 1 
ATOM   756  N N   . SER A 1 98  ? 35.141 29.433  11.073 1.00 20.08 ? 131 SER A N   1 
ATOM   757  C CA  . SER A 1 98  ? 35.332 30.875  11.211 1.00 19.76 ? 131 SER A CA  1 
ATOM   758  C C   . SER A 1 98  ? 34.570 31.636  10.130 1.00 20.15 ? 131 SER A C   1 
ATOM   759  O O   . SER A 1 98  ? 33.908 32.643  10.415 1.00 19.78 ? 131 SER A O   1 
ATOM   760  C CB  . SER A 1 98  ? 36.827 31.212  11.168 1.00 18.90 ? 131 SER A CB  1 
ATOM   761  O OG  . SER A 1 98  ? 37.048 32.602  11.411 1.00 22.12 ? 131 SER A OG  1 
ATOM   762  N N   . ALA A 1 99  ? 34.635 31.161  8.884  1.00 18.53 ? 132 ALA A N   1 
ATOM   763  C CA  . ALA A 1 99  ? 33.906 31.825  7.808  1.00 20.82 ? 132 ALA A CA  1 
ATOM   764  C C   . ALA A 1 99  ? 32.400 31.741  8.028  1.00 19.20 ? 132 ALA A C   1 
ATOM   765  O O   . ALA A 1 99  ? 31.670 32.704  7.755  1.00 17.23 ? 132 ALA A O   1 
ATOM   766  C CB  . ALA A 1 99  ? 34.290 31.218  6.454  1.00 21.45 ? 132 ALA A CB  1 
ATOM   767  N N   . SER A 1 100 ? 31.914 30.594  8.515  1.00 17.89 ? 133 SER A N   1 
ATOM   768  C CA  . SER A 1 100 ? 30.489 30.462  8.825  1.00 16.68 ? 133 SER A CA  1 
ATOM   769  C C   . SER A 1 100 ? 30.083 31.389  9.966  1.00 17.81 ? 133 SER A C   1 
ATOM   770  O O   . SER A 1 100 ? 28.997 31.977  9.941  1.00 15.37 ? 133 SER A O   1 
ATOM   771  C CB  . SER A 1 100 ? 30.157 29.006  9.176  1.00 19.71 ? 133 SER A CB  1 
ATOM   772  O OG  . SER A 1 100 ? 30.346 28.143  8.059  1.00 20.59 ? 133 SER A OG  1 
ATOM   773  N N   . ARG A 1 101 ? 30.924 31.512  10.994 1.00 15.36 ? 134 ARG A N   1 
ATOM   774  C CA  . ARG A 1 101 ? 30.612 32.452  12.068 1.00 15.28 ? 134 ARG A CA  1 
ATOM   775  C C   . ARG A 1 101 ? 30.535 33.884  11.540 1.00 16.51 ? 134 ARG A C   1 
ATOM   776  O O   . ARG A 1 101 ? 29.637 34.654  11.921 1.00 15.63 ? 134 ARG A O   1 
ATOM   777  C CB  . ARG A 1 101 ? 31.655 32.338  13.184 1.00 17.17 ? 134 ARG A CB  1 
ATOM   778  C CG  . ARG A 1 101 ? 31.542 31.055  14.027 1.00 18.09 ? 134 ARG A CG  1 
ATOM   779  C CD  . ARG A 1 101 ? 32.486 31.081  15.237 1.00 21.11 ? 134 ARG A CD  1 
ATOM   780  N NE  . ARG A 1 101 ? 33.808 30.542  14.926 1.00 25.84 ? 134 ARG A NE  1 
ATOM   781  C CZ  . ARG A 1 101 ? 34.915 31.260  14.777 1.00 27.63 ? 134 ARG A CZ  1 
ATOM   782  N NH1 . ARG A 1 101 ? 34.917 32.583  14.920 1.00 18.53 ? 134 ARG A NH1 1 
ATOM   783  N NH2 . ARG A 1 101 ? 36.057 30.635  14.491 1.00 25.25 ? 134 ARG A NH2 1 
ATOM   784  N N   . SER A 1 102 ? 31.482 34.266  10.677 1.00 16.58 ? 135 SER A N   1 
ATOM   785  C CA  . SER A 1 102 ? 31.442 35.605  10.093 1.00 15.06 ? 135 SER A CA  1 
ATOM   786  C C   . SER A 1 102 ? 30.171 35.807  9.281  1.00 17.87 ? 135 SER A C   1 
ATOM   787  O O   . SER A 1 102 ? 29.509 36.854  9.386  1.00 15.07 ? 135 SER A O   1 
ATOM   788  C CB  . SER A 1 102 ? 32.675 35.839  9.217  1.00 19.60 ? 135 SER A CB  1 
ATOM   789  O OG  . SER A 1 102 ? 32.624 37.119  8.592  1.00 18.95 ? 135 SER A OG  1 
ATOM   790  N N   . ALA A 1 103 ? 29.816 34.813  8.464  1.00 15.65 ? 136 ALA A N   1 
ATOM   791  C CA  . ALA A 1 103 ? 28.619 34.929  7.640  1.00 15.65 ? 136 ALA A CA  1 
ATOM   792  C C   . ALA A 1 103 ? 27.375 35.067  8.502  1.00 17.71 ? 136 ALA A C   1 
ATOM   793  O O   . ALA A 1 103 ? 26.516 35.906  8.219  1.00 14.30 ? 136 ALA A O   1 
ATOM   794  C CB  . ALA A 1 103 ? 28.492 33.728  6.704  1.00 15.21 ? 136 ALA A CB  1 
ATOM   795  N N   . ILE A 1 104 ? 27.263 34.257  9.559  1.00 16.15 ? 137 ILE A N   1 
ATOM   796  C CA  . ILE A 1 104 ? 26.111 34.359  10.448 1.00 16.07 ? 137 ILE A CA  1 
ATOM   797  C C   . ILE A 1 104 ? 26.037 35.743  11.087 1.00 17.71 ? 137 ILE A C   1 
ATOM   798  O O   . ILE A 1 104 ? 24.960 36.333  11.167 1.00 15.82 ? 137 ILE A O   1 
ATOM   799  C CB  . ILE A 1 104 ? 26.144 33.238  11.505 1.00 15.05 ? 137 ILE A CB  1 
ATOM   800  C CG1 . ILE A 1 104 ? 25.822 31.893  10.832 1.00 16.83 ? 137 ILE A CG1 1 
ATOM   801  C CG2 . ILE A 1 104 ? 25.144 33.519  12.618 1.00 16.74 ? 137 ILE A CG2 1 
ATOM   802  C CD1 . ILE A 1 104 ? 25.961 30.695  11.729 1.00 36.18 ? 137 ILE A CD1 1 
ATOM   803  N N   . ASP A 1 105 ? 27.164 36.281  11.566 1.00 13.60 ? 138 ASP A N   1 
ATOM   804  C CA  . ASP A 1 105 ? 27.133 37.619  12.161 1.00 15.12 ? 138 ASP A CA  1 
ATOM   805  C C   . ASP A 1 105 ? 26.654 38.662  11.149 1.00 16.63 ? 138 ASP A C   1 
ATOM   806  O O   . ASP A 1 105 ? 25.788 39.508  11.453 1.00 16.52 ? 138 ASP A O   1 
ATOM   807  C CB  . ASP A 1 105 ? 28.523 37.978  12.698 1.00 18.83 ? 138 ASP A CB  1 
ATOM   808  C CG  . ASP A 1 105 ? 28.583 39.373  13.301 1.00 23.33 ? 138 ASP A CG  1 
ATOM   809  O OD1 . ASP A 1 105 ? 28.120 39.549  14.447 1.00 24.67 ? 138 ASP A OD1 1 
ATOM   810  O OD2 . ASP A 1 105 ? 29.093 40.293  12.630 1.00 24.92 ? 138 ASP A OD2 1 
ATOM   811  N N   A SER A 1 106 ? 27.191 38.597  9.925  0.56 14.63 ? 139 SER A N   1 
ATOM   812  N N   B SER A 1 106 ? 27.188 38.604  9.924  0.44 14.60 ? 139 SER A N   1 
ATOM   813  C CA  A SER A 1 106 ? 26.792 39.533  8.878  0.56 16.98 ? 139 SER A CA  1 
ATOM   814  C CA  B SER A 1 106 ? 26.780 39.557  8.895  0.44 16.96 ? 139 SER A CA  1 
ATOM   815  C C   A SER A 1 106 ? 25.306 39.407  8.558  0.56 15.88 ? 139 SER A C   1 
ATOM   816  C C   B SER A 1 106 ? 25.299 39.413  8.557  0.44 15.87 ? 139 SER A C   1 
ATOM   817  O O   A SER A 1 106 ? 24.599 40.415  8.416  0.56 14.40 ? 139 SER A O   1 
ATOM   818  O O   B SER A 1 106 ? 24.586 40.414  8.401  0.44 14.36 ? 139 SER A O   1 
ATOM   819  C CB  A SER A 1 106 ? 27.629 39.288  7.618  0.56 16.85 ? 139 SER A CB  1 
ATOM   820  C CB  B SER A 1 106 ? 27.638 39.376  7.640  0.44 16.88 ? 139 SER A CB  1 
ATOM   821  O OG  A SER A 1 106 ? 27.218 40.127  6.558  0.56 18.91 ? 139 SER A OG  1 
ATOM   822  O OG  B SER A 1 106 ? 28.992 39.704  7.908  0.44 18.26 ? 139 SER A OG  1 
ATOM   823  N N   . LEU A 1 107 ? 24.812 38.175  8.453  1.00 13.23 ? 140 LEU A N   1 
ATOM   824  C CA  . LEU A 1 107 ? 23.420 37.962  8.080  1.00 12.25 ? 140 LEU A CA  1 
ATOM   825  C C   . LEU A 1 107 ? 22.466 38.261  9.227  1.00 12.46 ? 140 LEU A C   1 
ATOM   826  O O   . LEU A 1 107 ? 21.350 38.720  8.983  1.00 12.92 ? 140 LEU A O   1 
ATOM   827  C CB  . LEU A 1 107 ? 23.229 36.532  7.563  1.00 13.35 ? 140 LEU A CB  1 
ATOM   828  C CG  . LEU A 1 107 ? 23.858 36.291  6.188  1.00 15.57 ? 140 LEU A CG  1 
ATOM   829  C CD1 . LEU A 1 107 ? 24.043 34.808  5.905  1.00 13.02 ? 140 LEU A CD1 1 
ATOM   830  C CD2 . LEU A 1 107 ? 22.980 36.931  5.123  1.00 15.89 ? 140 LEU A CD2 1 
ATOM   831  N N   . ASN A 1 108 ? 22.878 38.013  10.473 1.00 13.66 ? 141 ASN A N   1 
ATOM   832  C CA  . ASN A 1 108 ? 22.130 38.507  11.626 1.00 12.99 ? 141 ASN A CA  1 
ATOM   833  C C   . ASN A 1 108 ? 21.892 39.994  11.490 1.00 15.22 ? 141 ASN A C   1 
ATOM   834  O O   . ASN A 1 108 ? 20.763 40.479  11.650 1.00 14.26 ? 141 ASN A O   1 
ATOM   835  C CB  . ASN A 1 108 ? 22.918 38.281  12.923 1.00 14.41 ? 141 ASN A CB  1 
ATOM   836  C CG  . ASN A 1 108 ? 22.922 36.852  13.392 1.00 17.92 ? 141 ASN A CG  1 
ATOM   837  O OD1 . ASN A 1 108 ? 22.167 36.004  12.912 1.00 16.16 ? 141 ASN A OD1 1 
ATOM   838  N ND2 . ASN A 1 108 ? 23.769 36.582  14.382 1.00 16.95 ? 141 ASN A ND2 1 
ATOM   839  N N   . ASN A 1 109 ? 22.976 40.739  11.228 1.00 13.61 ? 142 ASN A N   1 
ATOM   840  C CA  . ASN A 1 109 ? 22.863 42.194  11.135 1.00 16.59 ? 142 ASN A CA  1 
ATOM   841  C C   . ASN A 1 109 ? 21.989 42.608  9.954  1.00 16.07 ? 142 ASN A C   1 
ATOM   842  O O   . ASN A 1 109 ? 21.175 43.536  10.067 1.00 15.91 ? 142 ASN A O   1 
ATOM   843  C CB  . ASN A 1 109 ? 24.251 42.820  11.028 1.00 17.83 ? 142 ASN A CB  1 
ATOM   844  C CG  . ASN A 1 109 ? 24.209 44.336  11.049 1.00 31.55 ? 142 ASN A CG  1 
ATOM   845  O OD1 . ASN A 1 109 ? 24.171 44.953  12.115 1.00 40.70 ? 142 ASN A OD1 1 
ATOM   846  N ND2 . ASN A 1 109 ? 24.207 44.947  9.866  1.00 40.90 ? 142 ASN A ND2 1 
ATOM   847  N N   . ARG A 1 110 ? 22.136 41.924  8.813  1.00 12.38 ? 143 ARG A N   1 
ATOM   848  C CA  . ARG A 1 110 ? 21.305 42.251  7.658  1.00 15.87 ? 143 ARG A CA  1 
ATOM   849  C C   . ARG A 1 110 ? 19.826 42.017  7.961  1.00 14.39 ? 143 ARG A C   1 
ATOM   850  O O   . ARG A 1 110 ? 18.975 42.863  7.641  1.00 13.70 ? 143 ARG A O   1 
ATOM   851  C CB  . ARG A 1 110 ? 21.772 41.449  6.430  1.00 14.37 ? 143 ARG A CB  1 
ATOM   852  C CG  . ARG A 1 110 ? 20.884 41.605  5.181  1.00 24.85 ? 143 ARG A CG  1 
ATOM   853  C CD  . ARG A 1 110 ? 21.648 41.617  3.836  1.00 34.52 ? 143 ARG A CD  1 
ATOM   854  N NE  . ARG A 1 110 ? 22.858 40.800  3.777  1.00 39.76 ? 143 ARG A NE  1 
ATOM   855  C CZ  . ARG A 1 110 ? 23.017 39.731  3.002  1.00 42.95 ? 143 ARG A CZ  1 
ATOM   856  N NH1 . ARG A 1 110 ? 22.026 39.253  2.258  1.00 33.84 ? 143 ARG A NH1 1 
ATOM   857  N NH2 . ARG A 1 110 ? 24.203 39.125  2.969  1.00 35.39 ? 143 ARG A NH2 1 
ATOM   858  N N   . MET A 1 111 ? 19.500 40.891  8.607  1.00 11.80 ? 144 MET A N   1 
ATOM   859  C CA  . MET A 1 111 ? 18.105 40.604  8.934  1.00 12.59 ? 144 MET A CA  1 
ATOM   860  C C   . MET A 1 111 ? 17.543 41.620  9.914  1.00 13.33 ? 144 MET A C   1 
ATOM   861  O O   . MET A 1 111 ? 16.430 42.122  9.731  1.00 13.92 ? 144 MET A O   1 
ATOM   862  C CB  . MET A 1 111 ? 17.975 39.192  9.512  1.00 11.64 ? 144 MET A CB  1 
ATOM   863  C CG  . MET A 1 111 ? 18.171 38.110  8.457  1.00 13.36 ? 144 MET A CG  1 
ATOM   864  S SD  . MET A 1 111 ? 18.274 36.461  9.190  1.00 16.55 ? 144 MET A SD  1 
ATOM   865  C CE  . MET A 1 111 ? 16.643 36.309  9.902  1.00 14.99 ? 144 MET A CE  1 
ATOM   866  N N   . LEU A 1 112 ? 18.281 41.910  10.986 1.00 12.17 ? 145 LEU A N   1 
ATOM   867  C CA  . LEU A 1 112 ? 17.757 42.832  11.991 1.00 13.29 ? 145 LEU A CA  1 
ATOM   868  C C   . LEU A 1 112 ? 17.551 44.230  11.402 1.00 17.05 ? 145 LEU A C   1 
ATOM   869  O O   . LEU A 1 112 ? 16.537 44.896  11.682 1.00 13.19 ? 145 LEU A O   1 
ATOM   870  C CB  . LEU A 1 112 ? 18.690 42.850  13.208 1.00 14.48 ? 145 LEU A CB  1 
ATOM   871  C CG  . LEU A 1 112 ? 18.225 43.568  14.480 1.00 25.01 ? 145 LEU A CG  1 
ATOM   872  C CD1 . LEU A 1 112 ? 16.961 42.924  15.040 1.00 21.62 ? 145 LEU A CD1 1 
ATOM   873  C CD2 . LEU A 1 112 ? 19.331 43.582  15.532 1.00 19.99 ? 145 LEU A CD2 1 
ATOM   874  N N   . SER A 1 113 ? 18.483 44.684  10.561 1.00 14.93 ? 146 SER A N   1 
ATOM   875  C CA  . SER A 1 113 ? 18.306 46.000  9.954  1.00 13.55 ? 146 SER A CA  1 
ATOM   876  C C   . SER A 1 113 ? 17.141 46.000  8.966  1.00 15.60 ? 146 SER A C   1 
ATOM   877  O O   . SER A 1 113 ? 16.411 46.995  8.872  1.00 16.21 ? 146 SER A O   1 
ATOM   878  C CB  . SER A 1 113 ? 19.609 46.467  9.306  1.00 17.04 ? 146 SER A CB  1 
ATOM   879  O OG  . SER A 1 113 ? 20.026 45.622  8.245  1.00 21.34 ? 146 SER A OG  1 
ATOM   880  N N   . GLN A 1 114 ? 16.915 44.886  8.248  1.00 12.73 ? 147 GLN A N   1 
ATOM   881  C CA  . GLN A 1 114 ? 15.753 44.830  7.359  1.00 14.98 ? 147 GLN A CA  1 
ATOM   882  C C   . GLN A 1 114 ? 14.456 44.799  8.151  1.00 18.13 ? 147 GLN A C   1 
ATOM   883  O O   . GLN A 1 114 ? 13.450 45.387  7.735  1.00 17.10 ? 147 GLN A O   1 
ATOM   884  C CB  . GLN A 1 114 ? 15.826 43.610  6.437  1.00 14.68 ? 147 GLN A CB  1 
ATOM   885  C CG  . GLN A 1 114 ? 16.781 43.806  5.263  1.00 15.74 ? 147 GLN A CG  1 
ATOM   886  C CD  . GLN A 1 114 ? 16.397 45.009  4.440  1.00 18.29 ? 147 GLN A CD  1 
ATOM   887  O OE1 . GLN A 1 114 ? 15.290 45.080  3.904  1.00 21.06 ? 147 GLN A OE1 1 
ATOM   888  N NE2 . GLN A 1 114 ? 17.297 45.983  4.359  1.00 23.08 ? 147 GLN A NE2 1 
ATOM   889  N N   . ILE A 1 115 ? 14.462 44.098  9.284  1.00 14.71 ? 148 ILE A N   1 
ATOM   890  C CA  . ILE A 1 115 ? 13.303 44.054  10.165 1.00 13.73 ? 148 ILE A CA  1 
ATOM   891  C C   . ILE A 1 115 ? 12.921 45.455  10.607 1.00 17.39 ? 148 ILE A C   1 
ATOM   892  O O   . ILE A 1 115 ? 11.756 45.850  10.511 1.00 16.24 ? 148 ILE A O   1 
ATOM   893  C CB  . ILE A 1 115 ? 13.583 43.149  11.381 1.00 12.94 ? 148 ILE A CB  1 
ATOM   894  C CG1 . ILE A 1 115 ? 13.539 41.672  10.970 1.00 14.20 ? 148 ILE A CG1 1 
ATOM   895  C CG2 . ILE A 1 115 ? 12.581 43.447  12.506 1.00 14.60 ? 148 ILE A CG2 1 
ATOM   896  C CD1 . ILE A 1 115 ? 14.046 40.700  12.072 1.00 15.43 ? 148 ILE A CD1 1 
ATOM   897  N N   . TRP A 1 116 ? 13.890 46.228  11.111 1.00 14.57 ? 149 TRP A N   1 
ATOM   898  C CA  . TRP A 1 116 ? 13.543 47.591  11.508 1.00 14.55 ? 149 TRP A CA  1 
ATOM   899  C C   . TRP A 1 116 ? 13.145 48.442  10.305 1.00 17.28 ? 149 TRP A C   1 
ATOM   900  O O   . TRP A 1 116 ? 12.211 49.249  10.396 1.00 15.37 ? 149 TRP A O   1 
ATOM   901  C CB  . TRP A 1 116 ? 14.681 48.259  12.273 1.00 14.98 ? 149 TRP A CB  1 
ATOM   902  C CG  . TRP A 1 116 ? 14.200 49.489  12.943 1.00 18.04 ? 149 TRP A CG  1 
ATOM   903  C CD1 . TRP A 1 116 ? 14.624 50.775  12.724 1.00 16.68 ? 149 TRP A CD1 1 
ATOM   904  C CD2 . TRP A 1 116 ? 13.155 49.569  13.922 1.00 22.99 ? 149 TRP A CD2 1 
ATOM   905  N NE1 . TRP A 1 116 ? 13.925 51.645  13.533 1.00 20.69 ? 149 TRP A NE1 1 
ATOM   906  C CE2 . TRP A 1 116 ? 13.016 50.930  14.275 1.00 24.52 ? 149 TRP A CE2 1 
ATOM   907  C CE3 . TRP A 1 116 ? 12.328 48.622  14.542 1.00 19.29 ? 149 TRP A CE3 1 
ATOM   908  C CZ2 . TRP A 1 116 ? 12.084 51.369  15.227 1.00 26.29 ? 149 TRP A CZ2 1 
ATOM   909  C CZ3 . TRP A 1 116 ? 11.401 49.062  15.495 1.00 21.16 ? 149 TRP A CZ3 1 
ATOM   910  C CH2 . TRP A 1 116 ? 11.292 50.424  15.823 1.00 24.72 ? 149 TRP A CH2 1 
ATOM   911  N N   . SER A 1 117 ? 13.839 48.280  9.173  1.00 17.97 ? 150 SER A N   1 
ATOM   912  C CA  . SER A 1 117 ? 13.561 49.110  8.004  1.00 16.48 ? 150 SER A CA  1 
ATOM   913  C C   . SER A 1 117 ? 12.130 48.942  7.510  1.00 18.84 ? 150 SER A C   1 
ATOM   914  O O   . SER A 1 117 ? 11.547 49.885  6.956  1.00 17.93 ? 150 SER A O   1 
ATOM   915  C CB  . SER A 1 117 ? 14.540 48.779  6.875  1.00 15.80 ? 150 SER A CB  1 
ATOM   916  O OG  . SER A 1 117 ? 15.847 49.236  7.186  1.00 19.83 ? 150 SER A OG  1 
ATOM   917  N N   . HIS A 1 118 ? 11.549 47.765  7.713  1.00 15.51 ? 151 HIS A N   1 
ATOM   918  C CA  . HIS A 1 118 ? 10.222 47.432  7.217  1.00 14.69 ? 151 HIS A CA  1 
ATOM   919  C C   . HIS A 1 118 ? 9.254  47.173  8.361  1.00 18.76 ? 151 HIS A C   1 
ATOM   920  O O   . HIS A 1 118 ? 8.262  46.460  8.199  1.00 17.44 ? 151 HIS A O   1 
ATOM   921  C CB  . HIS A 1 118 ? 10.308 46.233  6.269  1.00 16.75 ? 151 HIS A CB  1 
ATOM   922  C CG  . HIS A 1 118 ? 11.117 46.518  5.044  1.00 17.82 ? 151 HIS A CG  1 
ATOM   923  N ND1 . HIS A 1 118 ? 10.606 47.196  3.957  1.00 18.48 ? 151 HIS A ND1 1 
ATOM   924  C CD2 . HIS A 1 118 ? 12.412 46.256  4.748  1.00 18.98 ? 151 HIS A CD2 1 
ATOM   925  C CE1 . HIS A 1 118 ? 11.546 47.327  3.040  1.00 18.32 ? 151 HIS A CE1 1 
ATOM   926  N NE2 . HIS A 1 118 ? 12.653 46.764  3.494  1.00 21.44 ? 151 HIS A NE2 1 
ATOM   927  N N   . TRP A 1 119 ? 9.525  47.781  9.520  1.00 15.10 ? 152 TRP A N   1 
ATOM   928  C CA  . TRP A 1 119 ? 8.731  47.499  10.706 1.00 20.19 ? 152 TRP A CA  1 
ATOM   929  C C   . TRP A 1 119 ? 7.269  47.874  10.495 1.00 20.88 ? 152 TRP A C   1 
ATOM   930  O O   . TRP A 1 119 ? 6.365  47.178  10.976 1.00 21.47 ? 152 TRP A O   1 
ATOM   931  C CB  . TRP A 1 119 ? 9.316  48.241  11.910 1.00 16.53 ? 152 TRP A CB  1 
ATOM   932  C CG  . TRP A 1 119 ? 8.658  47.875  13.196 1.00 23.51 ? 152 TRP A CG  1 
ATOM   933  C CD1 . TRP A 1 119 ? 7.670  48.565  13.839 1.00 21.55 ? 152 TRP A CD1 1 
ATOM   934  C CD2 . TRP A 1 119 ? 8.920  46.714  13.990 1.00 22.29 ? 152 TRP A CD2 1 
ATOM   935  N NE1 . TRP A 1 119 ? 7.305  47.909  14.987 1.00 28.72 ? 152 TRP A NE1 1 
ATOM   936  C CE2 . TRP A 1 119 ? 8.054  46.767  15.103 1.00 26.08 ? 152 TRP A CE2 1 
ATOM   937  C CE3 . TRP A 1 119 ? 9.802  45.632  13.870 1.00 23.36 ? 152 TRP A CE3 1 
ATOM   938  C CZ2 . TRP A 1 119 ? 8.045  45.784  16.092 1.00 30.04 ? 152 TRP A CZ2 1 
ATOM   939  C CZ3 . TRP A 1 119 ? 9.793  44.658  14.857 1.00 22.12 ? 152 TRP A CZ3 1 
ATOM   940  C CH2 . TRP A 1 119 ? 8.919  44.740  15.950 1.00 24.98 ? 152 TRP A CH2 1 
ATOM   941  N N   . SER A 1 120 ? 7.015  48.971  9.778  1.00 21.11 ? 153 SER A N   1 
ATOM   942  C CA  . SER A 1 120 ? 5.635  49.382  9.539  1.00 26.45 ? 153 SER A CA  1 
ATOM   943  C C   . SER A 1 120 ? 4.875  48.328  8.743  1.00 24.23 ? 153 SER A C   1 
ATOM   944  O O   . SER A 1 120 ? 3.711  48.035  9.039  1.00 23.74 ? 153 SER A O   1 
ATOM   945  C CB  . SER A 1 120 ? 5.609  50.726  8.815  1.00 28.83 ? 153 SER A CB  1 
ATOM   946  O OG  . SER A 1 120 ? 6.073  51.752  9.679  1.00 40.88 ? 153 SER A OG  1 
ATOM   947  N N   . LEU A 1 121 ? 5.522  47.742  7.735  1.00 20.95 ? 154 LEU A N   1 
ATOM   948  C CA  . LEU A 1 121 ? 4.883  46.686  6.955  1.00 19.92 ? 154 LEU A CA  1 
ATOM   949  C C   . LEU A 1 121 ? 4.716  45.413  7.773  1.00 18.85 ? 154 LEU A C   1 
ATOM   950  O O   . LEU A 1 121 ? 3.660  44.776  7.718  1.00 20.58 ? 154 LEU A O   1 
ATOM   951  C CB  . LEU A 1 121 ? 5.690  46.407  5.693  1.00 18.96 ? 154 LEU A CB  1 
ATOM   952  C CG  . LEU A 1 121 ? 5.262  45.209  4.847  1.00 20.13 ? 154 LEU A CG  1 
ATOM   953  C CD1 . LEU A 1 121 ? 3.790  45.320  4.470  1.00 20.24 ? 154 LEU A CD1 1 
ATOM   954  C CD2 . LEU A 1 121 ? 6.156  45.133  3.615  1.00 17.38 ? 154 LEU A CD2 1 
ATOM   955  N N   . LEU A 1 122 ? 5.746  45.025  8.538  1.00 17.31 ? 155 LEU A N   1 
ATOM   956  C CA  . LEU A 1 122 ? 5.653  43.806  9.338  1.00 17.83 ? 155 LEU A CA  1 
ATOM   957  C C   . LEU A 1 122 ? 4.515  43.881  10.354 1.00 21.82 ? 155 LEU A C   1 
ATOM   958  O O   . LEU A 1 122 ? 3.961  42.844  10.739 1.00 22.09 ? 155 LEU A O   1 
ATOM   959  C CB  . LEU A 1 122 ? 6.989  43.531  10.038 1.00 15.84 ? 155 LEU A CB  1 
ATOM   960  C CG  . LEU A 1 122 ? 8.142  43.117  9.109  1.00 16.38 ? 155 LEU A CG  1 
ATOM   961  C CD1 . LEU A 1 122 ? 9.468  43.148  9.850  1.00 16.84 ? 155 LEU A CD1 1 
ATOM   962  C CD2 . LEU A 1 122 ? 7.888  41.727  8.536  1.00 14.81 ? 155 LEU A CD2 1 
ATOM   963  N N   . SER A 1 123 ? 4.140  45.087  10.790 1.00 18.91 ? 156 SER A N   1 
ATOM   964  C CA  . SER A 1 123 ? 3.014  45.241  11.703 1.00 22.74 ? 156 SER A CA  1 
ATOM   965  C C   . SER A 1 123 ? 1.698  45.525  10.985 1.00 27.43 ? 156 SER A C   1 
ATOM   966  O O   . SER A 1 123 ? 0.673  45.697  11.649 1.00 23.63 ? 156 SER A O   1 
ATOM   967  C CB  . SER A 1 123 ? 3.296  46.346  12.731 1.00 27.45 ? 156 SER A CB  1 
ATOM   968  O OG  . SER A 1 123 ? 4.117  47.367  12.201 1.00 34.55 ? 156 SER A OG  1 
ATOM   969  N N   . ALA A 1 124 ? 1.690  45.537  9.663  1.00 21.51 ? 157 ALA A N   1 
ATOM   970  C CA  . ALA A 1 124 ? 0.536  45.969  8.895  1.00 24.99 ? 157 ALA A CA  1 
ATOM   971  C C   . ALA A 1 124 ? -0.243 44.776  8.363  1.00 19.31 ? 157 ALA A C   1 
ATOM   972  O O   . ALA A 1 124 ? 0.304  43.677  8.222  1.00 19.71 ? 157 ALA A O   1 
ATOM   973  C CB  . ALA A 1 124 ? 0.990  46.861  7.733  1.00 26.94 ? 157 ALA A CB  1 
ATOM   974  N N   . PRO A 1 125 ? -1.526 44.964  8.031  1.00 21.76 ? 158 PRO A N   1 
ATOM   975  C CA  . PRO A 1 125 ? -2.329 43.832  7.534  1.00 22.20 ? 158 PRO A CA  1 
ATOM   976  C C   . PRO A 1 125 ? -1.797 43.196  6.258  1.00 21.14 ? 158 PRO A C   1 
ATOM   977  O O   . PRO A 1 125 ? -2.002 41.993  6.050  1.00 22.79 ? 158 PRO A O   1 
ATOM   978  C CB  . PRO A 1 125 ? -3.718 44.455  7.318  1.00 24.77 ? 158 PRO A CB  1 
ATOM   979  C CG  . PRO A 1 125 ? -3.502 45.910  7.258  1.00 21.39 ? 158 PRO A CG  1 
ATOM   980  C CD  . PRO A 1 125 ? -2.329 46.196  8.143  1.00 22.30 ? 158 PRO A CD  1 
ATOM   981  N N   . SER A 1 126 ? -1.123 43.954  5.392  1.00 19.92 ? 159 SER A N   1 
ATOM   982  C CA  . SER A 1 126 ? -0.610 43.384  4.148  1.00 18.79 ? 159 SER A CA  1 
ATOM   983  C C   . SER A 1 126 ? 0.645  42.534  4.347  1.00 18.53 ? 159 SER A C   1 
ATOM   984  O O   . SER A 1 126 ? 1.112  41.905  3.379  1.00 19.66 ? 159 SER A O   1 
ATOM   985  C CB  . SER A 1 126 ? -0.326 44.497  3.141  1.00 26.07 ? 159 SER A CB  1 
ATOM   986  O OG  . SER A 1 126 ? 0.694  45.349  3.625  1.00 24.66 ? 159 SER A OG  1 
ATOM   987  N N   . CYS A 1 127 ? 1.175  42.461  5.575  1.00 17.20 ? 160 CYS A N   1 
ATOM   988  C CA  . CYS A 1 127 ? 2.422  41.730  5.803  1.00 17.58 ? 160 CYS A CA  1 
ATOM   989  C C   . CYS A 1 127 ? 2.356  40.313  5.240  1.00 16.46 ? 160 CYS A C   1 
ATOM   990  O O   . CYS A 1 127 ? 3.229  39.897  4.465  1.00 17.67 ? 160 CYS A O   1 
ATOM   991  C CB  . CYS A 1 127 ? 2.742  41.686  7.298  1.00 16.71 ? 160 CYS A CB  1 
ATOM   992  S SG  . CYS A 1 127 ? 4.257  40.768  7.705  1.00 18.84 ? 160 CYS A SG  1 
ATOM   993  N N   . ALA A 1 128 ? 1.305  39.565  5.594  1.00 18.92 ? 161 ALA A N   1 
ATOM   994  C CA  . ALA A 1 128 ? 1.219  38.167  5.170  1.00 15.73 ? 161 ALA A CA  1 
ATOM   995  C C   . ALA A 1 128 ? 1.309  38.049  3.652  1.00 16.97 ? 161 ALA A C   1 
ATOM   996  O O   . ALA A 1 128 ? 2.098  37.249  3.125  1.00 19.01 ? 161 ALA A O   1 
ATOM   997  C CB  . ALA A 1 128 ? -0.076 37.532  5.682  1.00 18.13 ? 161 ALA A CB  1 
ATOM   998  N N   . ALA A 1 129 ? 0.551  38.877  2.929  1.00 19.47 ? 162 ALA A N   1 
ATOM   999  C CA  . ALA A 1 129 ? 0.602  38.791  1.473  1.00 23.80 ? 162 ALA A CA  1 
ATOM   1000 C C   . ALA A 1 129 ? 2.003  39.123  0.982  1.00 20.62 ? 162 ALA A C   1 
ATOM   1001 O O   . ALA A 1 129 ? 2.601  38.369  0.196  1.00 20.97 ? 162 ALA A O   1 
ATOM   1002 C CB  . ALA A 1 129 ? -0.433 39.727  0.850  1.00 24.14 ? 162 ALA A CB  1 
ATOM   1003 N N   . GLN A 1 130 ? 2.584  40.197  1.531  1.00 17.38 ? 163 GLN A N   1 
ATOM   1004 C CA  . GLN A 1 130 ? 3.914  40.605  1.101  1.00 19.39 ? 163 GLN A CA  1 
ATOM   1005 C C   . GLN A 1 130 ? 4.936  39.532  1.423  1.00 19.24 ? 163 GLN A C   1 
ATOM   1006 O O   . GLN A 1 130 ? 5.913  39.365  0.683  1.00 18.64 ? 163 GLN A O   1 
ATOM   1007 C CB  . GLN A 1 130 ? 4.315  41.927  1.760  1.00 17.28 ? 163 GLN A CB  1 
ATOM   1008 C CG  . GLN A 1 130 ? 3.631  43.136  1.171  1.00 19.01 ? 163 GLN A CG  1 
ATOM   1009 C CD  . GLN A 1 130 ? 4.206  43.491  -0.179 1.00 32.62 ? 163 GLN A CD  1 
ATOM   1010 O OE1 . GLN A 1 130 ? 5.280  44.086  -0.267 1.00 33.26 ? 163 GLN A OE1 1 
ATOM   1011 N NE2 . GLN A 1 130 ? 3.508  43.105  -1.247 1.00 33.03 ? 163 GLN A NE2 1 
ATOM   1012 N N   . LEU A 1 131 ? 4.720  38.788  2.508  1.00 16.79 ? 164 LEU A N   1 
ATOM   1013 C CA  . LEU A 1 131 ? 5.689  37.762  2.860  1.00 14.06 ? 164 LEU A CA  1 
ATOM   1014 C C   . LEU A 1 131 ? 5.561  36.571  1.927  1.00 16.62 ? 164 LEU A C   1 
ATOM   1015 O O   . LEU A 1 131 ? 6.573  36.027  1.454  1.00 15.16 ? 164 LEU A O   1 
ATOM   1016 C CB  . LEU A 1 131 ? 5.499  37.349  4.318  1.00 15.31 ? 164 LEU A CB  1 
ATOM   1017 C CG  . LEU A 1 131 ? 6.336  36.170  4.803  1.00 16.09 ? 164 LEU A CG  1 
ATOM   1018 C CD1 . LEU A 1 131 ? 7.824  36.461  4.625  1.00 17.77 ? 164 LEU A CD1 1 
ATOM   1019 C CD2 . LEU A 1 131 ? 5.998  35.850  6.273  1.00 14.70 ? 164 LEU A CD2 1 
ATOM   1020 N N   . ASP A 1 132 ? 4.321  36.205  1.589  1.00 18.91 ? 165 ASP A N   1 
ATOM   1021 C CA  . ASP A 1 132 ? 4.105  35.105  0.654  1.00 20.71 ? 165 ASP A CA  1 
ATOM   1022 C C   . ASP A 1 132 ? 4.795  35.395  -0.670 1.00 18.78 ? 165 ASP A C   1 
ATOM   1023 O O   . ASP A 1 132 ? 5.596  34.587  -1.169 1.00 19.46 ? 165 ASP A O   1 
ATOM   1024 C CB  . ASP A 1 132 ? 2.606  34.893  0.450  1.00 20.41 ? 165 ASP A CB  1 
ATOM   1025 C CG  . ASP A 1 132 ? 2.292  33.614  -0.308 1.00 37.69 ? 165 ASP A CG  1 
ATOM   1026 O OD1 . ASP A 1 132 ? 3.057  32.634  -0.166 1.00 48.11 ? 165 ASP A OD1 1 
ATOM   1027 O OD2 . ASP A 1 132 ? 1.284  33.587  -1.048 1.00 51.46 ? 165 ASP A OD2 1 
ATOM   1028 N N   . ARG A 1 133 ? 4.563  36.597  -1.201 1.00 17.75 ? 166 ARG A N   1 
ATOM   1029 C CA  . ARG A 1 133 ? 5.211  37.006  -2.441 1.00 18.06 ? 166 ARG A CA  1 
ATOM   1030 C C   . ARG A 1 133 ? 6.725  36.899  -2.313 1.00 21.20 ? 166 ARG A C   1 
ATOM   1031 O O   . ARG A 1 133 ? 7.395  36.303  -3.173 1.00 19.02 ? 166 ARG A O   1 
ATOM   1032 C CB  . ARG A 1 133 ? 4.787  38.433  -2.789 1.00 22.69 ? 166 ARG A CB  1 
ATOM   1033 C CG  . ARG A 1 133 ? 5.644  39.089  -3.849 1.00 32.40 ? 166 ARG A CG  1 
ATOM   1034 C CD  . ARG A 1 133 ? 4.947  40.311  -4.411 1.00 41.62 ? 166 ARG A CD  1 
ATOM   1035 N NE  . ARG A 1 133 ? 3.795  39.913  -5.208 1.00 57.08 ? 166 ARG A NE  1 
ATOM   1036 C CZ  . ARG A 1 133 ? 3.862  39.547  -6.481 1.00 60.30 ? 166 ARG A CZ  1 
ATOM   1037 N NH1 . ARG A 1 133 ? 5.007  39.559  -7.145 1.00 59.80 ? 166 ARG A NH1 1 
ATOM   1038 N NH2 . ARG A 1 133 ? 2.754  39.155  -7.102 1.00 60.90 ? 166 ARG A NH2 1 
ATOM   1039 N N   . ALA A 1 134 ? 7.276  37.411  -1.201 1.00 16.71 ? 167 ALA A N   1 
ATOM   1040 C CA  . ALA A 1 134 ? 8.723  37.412  -1.057 1.00 14.81 ? 167 ALA A CA  1 
ATOM   1041 C C   . ALA A 1 134 ? 9.252  35.991  -1.045 1.00 18.27 ? 167 ALA A C   1 
ATOM   1042 O O   . ALA A 1 134 ? 10.211 35.677  -1.763 1.00 16.42 ? 167 ALA A O   1 
ATOM   1043 C CB  . ALA A 1 134 ? 9.144  38.149  0.215  1.00 14.33 ? 167 ALA A CB  1 
ATOM   1044 N N   . LYS A 1 135 ? 8.584  35.094  -0.301 1.00 15.43 ? 168 LYS A N   1 
ATOM   1045 C CA  . LYS A 1 135 ? 9.085  33.725  -0.252 1.00 16.29 ? 168 LYS A CA  1 
ATOM   1046 C C   . LYS A 1 135 ? 9.075  33.121  -1.645 1.00 18.58 ? 168 LYS A C   1 
ATOM   1047 O O   . LYS A 1 135 ? 10.074 32.532  -2.087 1.00 20.67 ? 168 LYS A O   1 
ATOM   1048 C CB  . LYS A 1 135 ? 8.257  32.878  0.721  1.00 14.54 ? 168 LYS A CB  1 
ATOM   1049 C CG  . LYS A 1 135 ? 8.413  33.284  2.195  1.00 15.49 ? 168 LYS A CG  1 
ATOM   1050 C CD  . LYS A 1 135 ? 7.251  32.778  3.062  1.00 26.22 ? 168 LYS A CD  1 
ATOM   1051 C CE  . LYS A 1 135 ? 7.139  31.263  3.061  1.00 29.44 ? 168 LYS A CE  1 
ATOM   1052 N NZ  . LYS A 1 135 ? 5.853  30.824  3.701  1.00 27.51 ? 168 LYS A NZ  1 
ATOM   1053 N N   . ARG A 1 136 ? 7.990  33.350  -2.393 1.00 14.91 ? 169 ARG A N   1 
ATOM   1054 C CA  . ARG A 1 136 ? 7.915  32.773  -3.730 1.00 18.07 ? 169 ARG A CA  1 
ATOM   1055 C C   . ARG A 1 136 ? 9.111  33.228  -4.560 1.00 21.49 ? 169 ARG A C   1 
ATOM   1056 O O   . ARG A 1 136 ? 9.843  32.402  -5.140 1.00 19.66 ? 169 ARG A O   1 
ATOM   1057 C CB  . ARG A 1 136 ? 6.594  33.170  -4.392 1.00 21.84 ? 169 ARG A CB  1 
ATOM   1058 C CG  . ARG A 1 136 ? 6.290  32.421  -5.677 1.00 38.05 ? 169 ARG A CG  1 
ATOM   1059 C CD  . ARG A 1 136 ? 5.323  33.187  -6.581 1.00 51.20 ? 169 ARG A CD  1 
ATOM   1060 N NE  . ARG A 1 136 ? 5.849  34.502  -6.935 1.00 53.48 ? 169 ARG A NE  1 
ATOM   1061 C CZ  . ARG A 1 136 ? 5.338  35.655  -6.519 1.00 53.21 ? 169 ARG A CZ  1 
ATOM   1062 N NH1 . ARG A 1 136 ? 4.246  35.700  -5.770 1.00 54.33 ? 169 ARG A NH1 1 
ATOM   1063 N NH2 . ARG A 1 136 ? 5.935  36.792  -6.868 1.00 52.09 ? 169 ARG A NH2 1 
ATOM   1064 N N   . ASP A 1 137 ? 9.402  34.533  -4.524 1.00 19.61 ? 170 ASP A N   1 
ATOM   1065 C CA  . ASP A 1 137 ? 10.458 35.044  -5.386 1.00 16.48 ? 170 ASP A CA  1 
ATOM   1066 C C   . ASP A 1 137 ? 11.808 34.509  -4.937 1.00 17.23 ? 170 ASP A C   1 
ATOM   1067 O O   . ASP A 1 137 ? 12.624 34.089  -5.771 1.00 17.37 ? 170 ASP A O   1 
ATOM   1068 C CB  . ASP A 1 137 ? 10.427 36.576  -5.423 1.00 18.95 ? 170 ASP A CB  1 
ATOM   1069 C CG  . ASP A 1 137 ? 9.211  37.120  -6.188 1.00 31.20 ? 170 ASP A CG  1 
ATOM   1070 O OD1 . ASP A 1 137 ? 8.612  36.365  -6.982 1.00 29.31 ? 170 ASP A OD1 1 
ATOM   1071 O OD2 . ASP A 1 137 ? 8.849  38.301  -6.002 1.00 38.09 ? 170 ASP A OD2 1 
ATOM   1072 N N   . ILE A 1 138 ? 12.017 34.418  -3.616 1.00 14.97 ? 171 ILE A N   1 
ATOM   1073 C CA  . ILE A 1 138 ? 13.324 33.996  -3.128 1.00 13.32 ? 171 ILE A CA  1 
ATOM   1074 C C   . ILE A 1 138 ? 13.486 32.506  -3.372 1.00 16.96 ? 171 ILE A C   1 
ATOM   1075 O O   . ILE A 1 138 ? 14.593 32.035  -3.696 1.00 12.46 ? 171 ILE A O   1 
ATOM   1076 C CB  . ILE A 1 138 ? 13.507 34.380  -1.641 1.00 12.38 ? 171 ILE A CB  1 
ATOM   1077 C CG1 . ILE A 1 138 ? 13.616 35.900  -1.488 1.00 15.58 ? 171 ILE A CG1 1 
ATOM   1078 C CG2 . ILE A 1 138 ? 14.719 33.690  -1.028 1.00 14.60 ? 171 ILE A CG2 1 
ATOM   1079 C CD1 . ILE A 1 138 ? 14.478 36.580  -2.522 1.00 17.68 ? 171 ILE A CD1 1 
ATOM   1080 N N   . VAL A 1 139 ? 12.376 31.753  -3.308 1.00 14.23 ? 172 VAL A N   1 
ATOM   1081 C CA  . VAL A 1 139 ? 12.474 30.327  -3.607 1.00 15.63 ? 172 VAL A CA  1 
ATOM   1082 C C   . VAL A 1 139 ? 12.957 30.152  -5.037 1.00 22.54 ? 172 VAL A C   1 
ATOM   1083 O O   . VAL A 1 139 ? 13.768 29.257  -5.337 1.00 17.01 ? 172 VAL A O   1 
ATOM   1084 C CB  . VAL A 1 139 ? 11.127 29.616  -3.353 1.00 14.17 ? 172 VAL A CB  1 
ATOM   1085 C CG1 . VAL A 1 139 ? 11.076 28.280  -4.075 1.00 15.96 ? 172 VAL A CG1 1 
ATOM   1086 C CG2 . VAL A 1 139 ? 10.900 29.421  -1.832 1.00 15.27 ? 172 VAL A CG2 1 
ATOM   1087 N N   . ARG A 1 140 ? 12.515 31.043  -5.935 1.00 16.81 ? 173 ARG A N   1 
ATOM   1088 C CA  . ARG A 1 140 ? 12.990 30.969  -7.308 1.00 18.50 ? 173 ARG A CA  1 
ATOM   1089 C C   . ARG A 1 140 ? 14.430 31.436  -7.419 1.00 20.86 ? 173 ARG A C   1 
ATOM   1090 O O   . ARG A 1 140 ? 15.254 30.770  -8.054 1.00 18.51 ? 173 ARG A O   1 
ATOM   1091 C CB  . ARG A 1 140 ? 12.102 31.797  -8.237 1.00 19.64 ? 173 ARG A CB  1 
ATOM   1092 C CG  . ARG A 1 140 ? 10.759 31.188  -8.499 1.00 21.35 ? 173 ARG A CG  1 
ATOM   1093 C CD  . ARG A 1 140 ? 10.135 31.795  -9.748 1.00 28.07 ? 173 ARG A CD  1 
ATOM   1094 N NE  . ARG A 1 140 ? 8.737  31.399  -9.855 1.00 45.18 ? 173 ARG A NE  1 
ATOM   1095 C CZ  . ARG A 1 140 ? 7.740  32.016  -9.237 1.00 47.51 ? 173 ARG A CZ  1 
ATOM   1096 N NH1 . ARG A 1 140 ? 7.951  33.081  -8.481 1.00 43.97 ? 173 ARG A NH1 1 
ATOM   1097 N NH2 . ARG A 1 140 ? 6.501  31.556  -9.383 1.00 59.98 ? 173 ARG A NH2 1 
ATOM   1098 N N   . SER A 1 141 ? 14.762 32.582  -6.812 1.00 16.24 ? 174 SER A N   1 
ATOM   1099 C CA  . SER A 1 141 ? 16.054 33.162  -7.161 1.00 16.65 ? 174 SER A CA  1 
ATOM   1100 C C   . SER A 1 141 ? 17.196 32.398  -6.506 1.00 18.64 ? 174 SER A C   1 
ATOM   1101 O O   . SER A 1 141 ? 18.311 32.388  -7.032 1.00 20.19 ? 174 SER A O   1 
ATOM   1102 C CB  . SER A 1 141 ? 16.116 34.646  -6.796 1.00 16.78 ? 174 SER A CB  1 
ATOM   1103 O OG  . SER A 1 141 ? 15.656 34.868  -5.479 1.00 20.87 ? 174 SER A OG  1 
ATOM   1104 N N   . ARG A 1 142 ? 16.927 31.722  -5.393 1.00 16.53 ? 175 ARG A N   1 
ATOM   1105 C CA  . ARG A 1 142 ? 17.942 30.944  -4.700 1.00 14.31 ? 175 ARG A CA  1 
ATOM   1106 C C   . ARG A 1 142 ? 17.817 29.440  -4.946 1.00 17.03 ? 175 ARG A C   1 
ATOM   1107 O O   . ARG A 1 142 ? 18.563 28.665  -4.339 1.00 19.00 ? 175 ARG A O   1 
ATOM   1108 C CB  . ARG A 1 142 ? 17.897 31.259  -3.200 1.00 15.63 ? 175 ARG A CB  1 
ATOM   1109 C CG  . ARG A 1 142 ? 18.045 32.758  -2.927 1.00 17.12 ? 175 ARG A CG  1 
ATOM   1110 C CD  . ARG A 1 142 ? 18.435 33.042  -1.492 1.00 22.94 ? 175 ARG A CD  1 
ATOM   1111 N NE  . ARG A 1 142 ? 19.777 32.560  -1.211 1.00 23.29 ? 175 ARG A NE  1 
ATOM   1112 C CZ  . ARG A 1 142 ? 20.862 33.320  -1.213 1.00 20.75 ? 175 ARG A CZ  1 
ATOM   1113 N NH1 . ARG A 1 142 ? 20.794 34.620  -1.437 1.00 18.89 ? 175 ARG A NH1 1 
ATOM   1114 N NH2 . ARG A 1 142 ? 22.044 32.764  -0.966 1.00 19.72 ? 175 ARG A NH2 1 
ATOM   1115 N N   . HIS A 1 143 ? 16.906 29.012  -5.826 1.00 18.05 ? 176 HIS A N   1 
ATOM   1116 C CA  . HIS A 1 143 ? 16.797 27.605  -6.243 1.00 18.02 ? 176 HIS A CA  1 
ATOM   1117 C C   . HIS A 1 143 ? 16.516 26.671  -5.063 1.00 18.68 ? 176 HIS A C   1 
ATOM   1118 O O   . HIS A 1 143 ? 17.112 25.598  -4.941 1.00 16.56 ? 176 HIS A O   1 
ATOM   1119 C CB  . HIS A 1 143 ? 18.062 27.147  -6.976 1.00 19.83 ? 176 HIS A CB  1 
ATOM   1120 C CG  . HIS A 1 143 ? 18.581 28.141  -7.965 1.00 23.25 ? 176 HIS A CG  1 
ATOM   1121 N ND1 . HIS A 1 143 ? 17.877 28.508  -9.089 1.00 26.63 ? 176 HIS A ND1 1 
ATOM   1122 C CD2 . HIS A 1 143 ? 19.737 28.848  -7.995 1.00 27.49 ? 176 HIS A CD2 1 
ATOM   1123 C CE1 . HIS A 1 143 ? 18.576 29.397  -9.772 1.00 29.19 ? 176 HIS A CE1 1 
ATOM   1124 N NE2 . HIS A 1 143 ? 19.708 29.622  -9.129 1.00 23.41 ? 176 HIS A NE2 1 
ATOM   1125 N N   . LEU A 1 144 ? 15.613 27.075  -4.180 1.00 15.88 ? 177 LEU A N   1 
ATOM   1126 C CA  . LEU A 1 144 ? 15.374 26.311  -2.958 1.00 15.68 ? 177 LEU A CA  1 
ATOM   1127 C C   . LEU A 1 144 ? 14.524 25.081  -3.240 1.00 18.67 ? 177 LEU A C   1 
ATOM   1128 O O   . LEU A 1 144 ? 13.445 25.192  -3.834 1.00 18.32 ? 177 LEU A O   1 
ATOM   1129 C CB  . LEU A 1 144 ? 14.694 27.202  -1.919 1.00 13.93 ? 177 LEU A CB  1 
ATOM   1130 C CG  . LEU A 1 144 ? 15.538 28.399  -1.501 1.00 15.15 ? 177 LEU A CG  1 
ATOM   1131 C CD1 . LEU A 1 144 ? 14.885 29.039  -0.298 1.00 14.66 ? 177 LEU A CD1 1 
ATOM   1132 C CD2 . LEU A 1 144 ? 16.981 27.988  -1.179 1.00 15.25 ? 177 LEU A CD2 1 
ATOM   1133 N N   . ASP A 1 145 ? 15.009 23.915  -2.787 1.00 18.59 ? 178 ASP A N   1 
ATOM   1134 C CA  . ASP A 1 145 ? 14.321 22.637  -2.924 1.00 19.37 ? 178 ASP A CA  1 
ATOM   1135 C C   . ASP A 1 145 ? 13.295 22.482  -1.796 1.00 20.94 ? 178 ASP A C   1 
ATOM   1136 O O   . ASP A 1 145 ? 13.100 23.381  -0.975 1.00 17.56 ? 178 ASP A O   1 
ATOM   1137 C CB  . ASP A 1 145 ? 15.335 21.482  -2.961 1.00 19.14 ? 178 ASP A CB  1 
ATOM   1138 C CG  . ASP A 1 145 ? 16.126 21.290  -1.629 1.00 28.23 ? 178 ASP A CG  1 
ATOM   1139 O OD1 . ASP A 1 145 ? 15.765 21.829  -0.557 1.00 18.04 ? 178 ASP A OD1 1 
ATOM   1140 O OD2 . ASP A 1 145 ? 17.144 20.563  -1.658 1.00 31.50 ? 178 ASP A OD2 1 
ATOM   1141 N N   . SER A 1 146 ? 12.659 21.306  -1.712 1.00 18.77 ? 179 SER A N   1 
ATOM   1142 C CA  A SER A 1 146 ? 11.557 21.128  -0.770 0.61 17.95 ? 179 SER A CA  1 
ATOM   1143 C CA  B SER A 1 146 ? 11.558 21.131  -0.770 0.39 17.99 ? 179 SER A CA  1 
ATOM   1144 C C   . SER A 1 146 ? 12.011 21.345  0.670  1.00 17.95 ? 179 SER A C   1 
ATOM   1145 O O   . SER A 1 146 ? 11.297 21.972  1.468  1.00 16.82 ? 179 SER A O   1 
ATOM   1146 C CB  A SER A 1 146 ? 10.952 19.736  -0.924 0.61 24.25 ? 179 SER A CB  1 
ATOM   1147 C CB  B SER A 1 146 ? 10.947 19.743  -0.932 0.39 24.19 ? 179 SER A CB  1 
ATOM   1148 O OG  A SER A 1 146 ? 11.722 18.774  -0.223 0.61 25.56 ? 179 SER A OG  1 
ATOM   1149 O OG  B SER A 1 146 ? 10.036 19.484  0.118  0.39 21.85 ? 179 SER A OG  1 
ATOM   1150 N N   . LEU A 1 147 ? 13.194 20.833  1.022  1.00 14.02 ? 180 LEU A N   1 
ATOM   1151 C CA  . LEU A 1 147 ? 13.681 20.986  2.391  1.00 14.99 ? 180 LEU A CA  1 
ATOM   1152 C C   . LEU A 1 147 ? 13.882 22.459  2.749  1.00 16.14 ? 180 LEU A C   1 
ATOM   1153 O O   . LEU A 1 147 ? 13.440 22.922  3.807  1.00 13.97 ? 180 LEU A O   1 
ATOM   1154 C CB  . LEU A 1 147 ? 14.984 20.209  2.566  1.00 15.07 ? 180 LEU A CB  1 
ATOM   1155 C CG  . LEU A 1 147 ? 15.656 20.371  3.932  1.00 16.41 ? 180 LEU A CG  1 
ATOM   1156 C CD1 . LEU A 1 147 ? 14.743 19.852  5.042  1.00 19.60 ? 180 LEU A CD1 1 
ATOM   1157 C CD2 . LEU A 1 147 ? 17.003 19.662  3.964  1.00 15.22 ? 180 LEU A CD2 1 
ATOM   1158 N N   . TYR A 1 148 ? 14.558 23.212  1.878  1.00 14.49 ? 181 TYR A N   1 
ATOM   1159 C CA  . TYR A 1 148 ? 14.792 24.626  2.158  1.00 15.16 ? 181 TYR A CA  1 
ATOM   1160 C C   . TYR A 1 148 ? 13.506 25.442  2.082  1.00 14.87 ? 181 TYR A C   1 
ATOM   1161 O O   . TYR A 1 148 ? 13.374 26.444  2.790  1.00 14.58 ? 181 TYR A O   1 
ATOM   1162 C CB  . TYR A 1 148 ? 15.848 25.197  1.203  1.00 13.31 ? 181 TYR A CB  1 
ATOM   1163 C CG  . TYR A 1 148 ? 17.252 25.023  1.728  1.00 18.24 ? 181 TYR A CG  1 
ATOM   1164 C CD1 . TYR A 1 148 ? 17.899 23.795  1.647  1.00 18.00 ? 181 TYR A CD1 1 
ATOM   1165 C CD2 . TYR A 1 148 ? 17.919 26.082  2.337  1.00 17.59 ? 181 TYR A CD2 1 
ATOM   1166 C CE1 . TYR A 1 148 ? 19.193 23.628  2.150  1.00 15.92 ? 181 TYR A CE1 1 
ATOM   1167 C CE2 . TYR A 1 148 ? 19.207 25.926  2.843  1.00 14.61 ? 181 TYR A CE2 1 
ATOM   1168 C CZ  . TYR A 1 148 ? 19.838 24.700  2.741  1.00 18.02 ? 181 TYR A CZ  1 
ATOM   1169 O OH  . TYR A 1 148 ? 21.113 24.549  3.245  1.00 17.32 ? 181 TYR A OH  1 
ATOM   1170 N N   . GLN A 1 149 ? 12.544 25.035  1.255  1.00 13.32 ? 182 GLN A N   1 
ATOM   1171 C CA  . GLN A 1 149 ? 11.262 25.735  1.244  1.00 14.46 ? 182 GLN A CA  1 
ATOM   1172 C C   . GLN A 1 149 ? 10.548 25.583  2.581  1.00 19.36 ? 182 GLN A C   1 
ATOM   1173 O O   . GLN A 1 149 ? 10.058 26.569  3.154  1.00 13.32 ? 182 GLN A O   1 
ATOM   1174 C CB  . GLN A 1 149 ? 10.382 25.222  0.104  1.00 14.13 ? 182 GLN A CB  1 
ATOM   1175 C CG  . GLN A 1 149 ? 10.894 25.590  -1.285 1.00 14.98 ? 182 GLN A CG  1 
ATOM   1176 C CD  . GLN A 1 149 ? 10.110 24.891  -2.376 1.00 23.06 ? 182 GLN A CD  1 
ATOM   1177 O OE1 . GLN A 1 149 ? 8.917  24.640  -2.224 1.00 25.90 ? 182 GLN A OE1 1 
ATOM   1178 N NE2 . GLN A 1 149 ? 10.778 24.559  -3.473 1.00 24.28 ? 182 GLN A NE2 1 
ATOM   1179 N N   . ARG A 1 150 ? 10.505 24.352  3.113  1.00 14.32 ? 183 ARG A N   1 
ATOM   1180 C CA  . ARG A 1 150 ? 9.916  24.151  4.436  1.00 13.79 ? 183 ARG A CA  1 
ATOM   1181 C C   . ARG A 1 150 ? 10.681 24.928  5.509  1.00 13.62 ? 183 ARG A C   1 
ATOM   1182 O O   . ARG A 1 150 ? 10.080 25.506  6.434  1.00 14.40 ? 183 ARG A O   1 
ATOM   1183 C CB  . ARG A 1 150 ? 9.890  22.655  4.769  1.00 14.16 ? 183 ARG A CB  1 
ATOM   1184 C CG  . ARG A 1 150 ? 9.072  21.818  3.771  1.00 16.76 ? 183 ARG A CG  1 
ATOM   1185 C CD  . ARG A 1 150 ? 9.400  20.334  3.927  1.00 17.68 ? 183 ARG A CD  1 
ATOM   1186 N NE  . ARG A 1 150 ? 9.065  19.859  5.262  1.00 18.00 ? 183 ARG A NE  1 
ATOM   1187 C CZ  . ARG A 1 150 ? 9.670  18.846  5.863  1.00 23.53 ? 183 ARG A CZ  1 
ATOM   1188 N NH1 . ARG A 1 150 ? 10.698 18.226  5.302  1.00 20.81 ? 183 ARG A NH1 1 
ATOM   1189 N NH2 . ARG A 1 150 ? 9.241  18.453  7.062  1.00 18.34 ? 183 ARG A NH2 1 
ATOM   1190 N N   . ALA A 1 151 ? 12.011 24.941  5.409  1.00 12.04 ? 184 ALA A N   1 
ATOM   1191 C CA  . ALA A 1 151 ? 12.809 25.663  6.393  1.00 15.33 ? 184 ALA A CA  1 
ATOM   1192 C C   . ALA A 1 151 ? 12.527 27.157  6.330  1.00 13.78 ? 184 ALA A C   1 
ATOM   1193 O O   . ALA A 1 151 ? 12.466 27.824  7.364  1.00 14.15 ? 184 ALA A O   1 
ATOM   1194 C CB  . ALA A 1 151 ? 14.301 25.386  6.180  1.00 11.67 ? 184 ALA A CB  1 
ATOM   1195 N N   . LEU A 1 152 ? 12.355 27.698  5.121  1.00 14.13 ? 185 LEU A N   1 
ATOM   1196 C CA  . LEU A 1 152 ? 12.070 29.122  4.973  1.00 12.61 ? 185 LEU A CA  1 
ATOM   1197 C C   . LEU A 1 152 ? 10.708 29.457  5.570  1.00 14.02 ? 185 LEU A C   1 
ATOM   1198 O O   . LEU A 1 152 ? 10.539 30.505  6.210  1.00 11.72 ? 185 LEU A O   1 
ATOM   1199 C CB  . LEU A 1 152 ? 12.138 29.516  3.492  1.00 12.54 ? 185 LEU A CB  1 
ATOM   1200 C CG  . LEU A 1 152 ? 12.119 31.013  3.157  1.00 12.68 ? 185 LEU A CG  1 
ATOM   1201 C CD1 . LEU A 1 152 ? 13.335 31.710  3.810  1.00 13.75 ? 185 LEU A CD1 1 
ATOM   1202 C CD2 . LEU A 1 152 ? 12.099 31.240  1.643  1.00 15.80 ? 185 LEU A CD2 1 
ATOM   1203 N N   . THR A 1 153 ? 9.731  28.568  5.381  1.00 12.87 ? 186 THR A N   1 
ATOM   1204 C CA  . THR A 1 153 ? 8.426  28.789  5.998  1.00 13.58 ? 186 THR A CA  1 
ATOM   1205 C C   . THR A 1 153 ? 8.543  28.838  7.517  1.00 12.67 ? 186 THR A C   1 
ATOM   1206 O O   . THR A 1 153 ? 7.977  29.720  8.171  1.00 13.70 ? 186 THR A O   1 
ATOM   1207 C CB  . THR A 1 153 ? 7.444  27.704  5.558  1.00 16.19 ? 186 THR A CB  1 
ATOM   1208 O OG1 . THR A 1 153 ? 7.186  27.867  4.163  1.00 16.50 ? 186 THR A OG1 1 
ATOM   1209 C CG2 . THR A 1 153 ? 6.134  27.828  6.313  1.00 16.56 ? 186 THR A CG2 1 
ATOM   1210 N N   . THR A 1 154 ? 9.281  27.895  8.096  1.00 12.57 ? 187 THR A N   1 
ATOM   1211 C CA  . THR A 1 154 ? 9.464  27.908  9.546  1.00 12.85 ? 187 THR A CA  1 
ATOM   1212 C C   . THR A 1 154 ? 10.197 29.164  9.999  1.00 12.55 ? 187 THR A C   1 
ATOM   1213 O O   . THR A 1 154 ? 9.804  29.810  10.975 1.00 14.01 ? 187 THR A O   1 
ATOM   1214 C CB  . THR A 1 154 ? 10.231 26.660  9.977  1.00 13.11 ? 187 THR A CB  1 
ATOM   1215 O OG1 . THR A 1 154 ? 9.409  25.509  9.750  1.00 15.52 ? 187 THR A OG1 1 
ATOM   1216 C CG2 . THR A 1 154 ? 10.620 26.739  11.462 1.00 13.27 ? 187 THR A CG2 1 
ATOM   1217 N N   . ALA A 1 155 ? 11.265 29.526  9.291  1.00 11.96 ? 188 ALA A N   1 
ATOM   1218 C CA  . ALA A 1 155 ? 12.094 30.655  9.702  1.00 12.97 ? 188 ALA A CA  1 
ATOM   1219 C C   . ALA A 1 155 ? 11.335 31.977  9.682  1.00 11.99 ? 188 ALA A C   1 
ATOM   1220 O O   . ALA A 1 155 ? 11.669 32.890  10.454 1.00 13.80 ? 188 ALA A O   1 
ATOM   1221 C CB  . ALA A 1 155 ? 13.316 30.764  8.788  1.00 14.31 ? 188 ALA A CB  1 
ATOM   1222 N N   . THR A 1 156 ? 10.350 32.116  8.794  1.00 14.75 ? 189 THR A N   1 
ATOM   1223 C CA  . THR A 1 156 ? 9.638  33.383  8.617  1.00 14.36 ? 189 THR A CA  1 
ATOM   1224 C C   . THR A 1 156 ? 8.255  33.403  9.270  1.00 15.95 ? 189 THR A C   1 
ATOM   1225 O O   . THR A 1 156 ? 7.527  34.396  9.131  1.00 16.75 ? 189 THR A O   1 
ATOM   1226 C CB  . THR A 1 156 ? 9.507  33.704  7.119  1.00 12.24 ? 189 THR A CB  1 
ATOM   1227 O OG1 . THR A 1 156 ? 8.748  32.679  6.465  1.00 14.05 ? 189 THR A OG1 1 
ATOM   1228 C CG2 . THR A 1 156 ? 10.892 33.801  6.463  1.00 13.06 ? 189 THR A CG2 1 
ATOM   1229 N N   . GLN A 1 157 ? 7.888  32.353  10.005 1.00 16.39 ? 190 GLN A N   1 
ATOM   1230 C CA  . GLN A 1 157 ? 6.510  32.196  10.452 1.00 15.86 ? 190 GLN A CA  1 
ATOM   1231 C C   . GLN A 1 157 ? 6.074  33.256  11.464 1.00 17.12 ? 190 GLN A C   1 
ATOM   1232 O O   . GLN A 1 157 ? 4.870  33.416  11.669 1.00 19.55 ? 190 GLN A O   1 
ATOM   1233 C CB  . GLN A 1 157 ? 6.317  30.804  11.051 1.00 19.25 ? 190 GLN A CB  1 
ATOM   1234 C CG  . GLN A 1 157 ? 6.869  30.684  12.453 1.00 22.72 ? 190 GLN A CG  1 
ATOM   1235 C CD  . GLN A 1 157 ? 6.837  29.264  12.995 1.00 29.80 ? 190 GLN A CD  1 
ATOM   1236 O OE1 . GLN A 1 157 ? 6.634  28.303  12.256 1.00 32.81 ? 190 GLN A OE1 1 
ATOM   1237 N NE2 . GLN A 1 157 ? 7.040  29.133  14.299 1.00 37.85 ? 190 GLN A NE2 1 
ATOM   1238 N N   . SER A 1 158 ? 7.004  33.969  12.109 1.00 18.34 ? 191 SER A N   1 
ATOM   1239 C CA  . SER A 1 158 ? 6.654  34.977  13.110 1.00 19.27 ? 191 SER A CA  1 
ATOM   1240 C C   . SER A 1 158 ? 6.906  36.409  12.638 1.00 18.91 ? 191 SER A C   1 
ATOM   1241 O O   . SER A 1 158 ? 6.835  37.342  13.453 1.00 18.61 ? 191 SER A O   1 
ATOM   1242 C CB  . SER A 1 158 ? 7.415  34.720  14.422 1.00 19.61 ? 191 SER A CB  1 
ATOM   1243 O OG  . SER A 1 158 ? 7.105  33.438  14.969 1.00 17.69 ? 191 SER A OG  1 
ATOM   1244 N N   . TYR A 1 159 ? 7.186  36.615  11.347 1.00 15.06 ? 192 TYR A N   1 
ATOM   1245 C CA  . TYR A 1 159 ? 7.438  37.971  10.862 1.00 17.71 ? 192 TYR A CA  1 
ATOM   1246 C C   . TYR A 1 159 ? 6.226  38.863  11.079 1.00 19.27 ? 192 TYR A C   1 
ATOM   1247 O O   . TYR A 1 159 ? 6.350  40.009  11.536 1.00 16.80 ? 192 TYR A O   1 
ATOM   1248 C CB  . TYR A 1 159 ? 7.779  37.961  9.371  1.00 15.91 ? 192 TYR A CB  1 
ATOM   1249 C CG  . TYR A 1 159 ? 9.185  37.545  9.002  1.00 17.64 ? 192 TYR A CG  1 
ATOM   1250 C CD1 . TYR A 1 159 ? 10.050 36.975  9.942  1.00 19.65 ? 192 TYR A CD1 1 
ATOM   1251 C CD2 . TYR A 1 159 ? 9.649  37.724  7.699  1.00 15.57 ? 192 TYR A CD2 1 
ATOM   1252 C CE1 . TYR A 1 159 ? 11.349 36.589  9.582  1.00 14.80 ? 192 TYR A CE1 1 
ATOM   1253 C CE2 . TYR A 1 159 ? 10.927 37.352  7.338  1.00 16.11 ? 192 TYR A CE2 1 
ATOM   1254 C CZ  . TYR A 1 159 ? 11.772 36.782  8.279  1.00 13.83 ? 192 TYR A CZ  1 
ATOM   1255 O OH  . TYR A 1 159 ? 13.047 36.411  7.898  1.00 17.10 ? 192 TYR A OH  1 
ATOM   1256 N N   . CYS A 1 160 ? 5.047  38.369  10.715 1.00 16.91 ? 193 CYS A N   1 
ATOM   1257 C CA  . CYS A 1 160 ? 3.849  39.201  10.727 1.00 21.80 ? 193 CYS A CA  1 
ATOM   1258 C C   . CYS A 1 160 ? 3.193  39.177  12.101 1.00 33.49 ? 193 CYS A C   1 
ATOM   1259 O O   . CYS A 1 160 ? 1.987  39.001  12.249 1.00 36.89 ? 193 CYS A O   1 
ATOM   1260 C CB  . CYS A 1 160 ? 2.897  38.745  9.629  1.00 18.72 ? 193 CYS A CB  1 
ATOM   1261 S SG  . CYS A 1 160 ? 3.679  38.812  7.960  1.00 24.48 ? 193 CYS A SG  1 
ATOM   1262 N N   . GLN A 1 161 ? 4.043  39.390  13.114 1.00 31.08 ? 194 GLN A N   1 
ATOM   1263 C CA  . GLN A 1 161 ? 3.664  39.524  14.515 1.00 35.48 ? 194 GLN A CA  1 
ATOM   1264 C C   . GLN A 1 161 ? 4.112  40.851  15.109 1.00 31.57 ? 194 GLN A C   1 
ATOM   1265 O O   . GLN A 1 161 ? 3.932  41.061  16.316 1.00 32.69 ? 194 GLN A O   1 
ATOM   1266 C CB  . GLN A 1 161 ? 4.269  38.385  15.354 1.00 29.83 ? 194 GLN A CB  1 
ATOM   1267 C CG  . GLN A 1 161 ? 3.713  37.001  15.048 1.00 33.18 ? 194 GLN A CG  1 
ATOM   1268 C CD  . GLN A 1 161 ? 2.252  36.870  15.427 1.00 43.24 ? 194 GLN A CD  1 
ATOM   1269 O OE1 . GLN A 1 161 ? 1.880  37.086  16.579 1.00 56.80 ? 194 GLN A OE1 1 
ATOM   1270 N NE2 . GLN A 1 161 ? 1.415  36.520  14.457 1.00 45.32 ? 194 GLN A NE2 1 
ATOM   1271 N N   . ALA A 1 162 ? 4.718  41.734  14.313 1.00 27.00 ? 195 ALA A N   1 
ATOM   1272 C CA  . ALA A 1 162 ? 5.235  42.989  14.848 1.00 31.05 ? 195 ALA A CA  1 
ATOM   1273 C C   . ALA A 1 162 ? 4.095  43.890  15.301 1.00 31.98 ? 195 ALA A C   1 
ATOM   1274 O O   . ALA A 1 162 ? 3.056  43.977  14.643 1.00 34.09 ? 195 ALA A O   1 
ATOM   1275 C CB  . ALA A 1 162 ? 6.079  43.715  13.797 1.00 29.84 ? 195 ALA A CB  1 
ATOM   1276 N N   . LEU A 1 163 ? 4.291  44.562  16.432 1.00 33.66 ? 196 LEU A N   1 
ATOM   1277 C CA  . LEU A 1 163 ? 3.295  45.517  16.919 1.00 35.40 ? 196 LEU A CA  1 
ATOM   1278 C C   . LEU A 1 163 ? 3.849  46.939  16.921 1.00 43.42 ? 196 LEU A C   1 
ATOM   1279 O O   . LEU A 1 163 ? 5.021  47.159  16.602 1.00 40.21 ? 196 LEU A O   1 
ATOM   1280 C CB  . LEU A 1 163 ? 2.811  45.138  18.325 1.00 43.40 ? 196 LEU A CB  1 
ATOM   1281 C CG  . LEU A 1 163 ? 2.039  43.822  18.505 1.00 47.82 ? 196 LEU A CG  1 
ATOM   1282 C CD1 . LEU A 1 163 ? 1.893  43.483  19.986 1.00 55.57 ? 196 LEU A CD1 1 
ATOM   1283 C CD2 . LEU A 1 163 ? 0.672  43.857  17.829 1.00 54.69 ? 196 LEU A CD2 1 
ATOM   1284 N N   . THR B 1 3   ? 7.094  -16.363 -2.588 1.00 44.08 ? 36  THR B N   1 
ATOM   1285 C CA  . THR B 1 3   ? 7.479  -16.019 -1.223 1.00 49.98 ? 36  THR B CA  1 
ATOM   1286 C C   . THR B 1 3   ? 8.971  -16.232 -1.014 1.00 39.85 ? 36  THR B C   1 
ATOM   1287 O O   . THR B 1 3   ? 9.477  -17.342 -1.165 1.00 32.97 ? 36  THR B O   1 
ATOM   1288 C CB  . THR B 1 3   ? 6.706  -16.851 -0.178 1.00 48.80 ? 36  THR B CB  1 
ATOM   1289 O OG1 . THR B 1 3   ? 5.302  -16.600 -0.305 1.00 60.74 ? 36  THR B OG1 1 
ATOM   1290 C CG2 . THR B 1 3   ? 7.157  -16.491 1.236  1.00 41.89 ? 36  THR B CG2 1 
ATOM   1291 N N   . SER B 1 4   ? 9.671  -15.160 -0.662 1.00 29.45 ? 37  SER B N   1 
ATOM   1292 C CA  . SER B 1 4   ? 11.104 -15.253 -0.438 1.00 29.31 ? 37  SER B CA  1 
ATOM   1293 C C   . SER B 1 4   ? 11.411 -16.084 0.800  1.00 22.23 ? 37  SER B C   1 
ATOM   1294 O O   . SER B 1 4   ? 10.728 -15.983 1.825  1.00 21.84 ? 37  SER B O   1 
ATOM   1295 C CB  . SER B 1 4   ? 11.710 -13.860 -0.273 1.00 19.51 ? 37  SER B CB  1 
ATOM   1296 O OG  . SER B 1 4   ? 13.079 -13.979 0.075  1.00 19.49 ? 37  SER B OG  1 
ATOM   1297 N N   . GLN B 1 5   ? 12.478 -16.874 0.719  1.00 19.76 ? 38  GLN B N   1 
ATOM   1298 C CA  . GLN B 1 5   ? 12.998 -17.527 1.912  1.00 22.39 ? 38  GLN B CA  1 
ATOM   1299 C C   . GLN B 1 5   ? 13.544 -16.535 2.926  1.00 20.40 ? 38  GLN B C   1 
ATOM   1300 O O   . GLN B 1 5   ? 13.752 -16.910 4.084  1.00 18.42 ? 38  GLN B O   1 
ATOM   1301 C CB  . GLN B 1 5   ? 14.092 -18.528 1.539  1.00 24.07 ? 38  GLN B CB  1 
ATOM   1302 C CG  . GLN B 1 5   ? 13.669 -19.533 0.473  1.00 33.10 ? 38  GLN B CG  1 
ATOM   1303 C CD  . GLN B 1 5   ? 14.790 -20.489 0.101  1.00 47.90 ? 38  GLN B CD  1 
ATOM   1304 O OE1 . GLN B 1 5   ? 15.605 -20.865 0.945  1.00 53.24 ? 38  GLN B OE1 1 
ATOM   1305 N NE2 . GLN B 1 5   ? 14.838 -20.883 -1.170 1.00 50.87 ? 38  GLN B NE2 1 
ATOM   1306 N N   . LEU B 1 6   ? 13.778 -15.282 2.536  1.00 18.02 ? 39  LEU B N   1 
ATOM   1307 C CA  . LEU B 1 6   ? 14.237 -14.279 3.484  1.00 17.24 ? 39  LEU B CA  1 
ATOM   1308 C C   . LEU B 1 6   ? 13.115 -13.363 3.954  1.00 17.31 ? 39  LEU B C   1 
ATOM   1309 O O   . LEU B 1 6   ? 13.397 -12.317 4.546  1.00 18.47 ? 39  LEU B O   1 
ATOM   1310 C CB  . LEU B 1 6   ? 15.379 -13.452 2.876  1.00 16.73 ? 39  LEU B CB  1 
ATOM   1311 C CG  . LEU B 1 6   ? 16.615 -14.270 2.481  1.00 16.79 ? 39  LEU B CG  1 
ATOM   1312 C CD1 . LEU B 1 6   ? 17.729 -13.391 1.889  1.00 17.44 ? 39  LEU B CD1 1 
ATOM   1313 C CD2 . LEU B 1 6   ? 17.157 -15.075 3.649  1.00 16.68 ? 39  LEU B CD2 1 
ATOM   1314 N N   . ALA B 1 7   ? 11.854 -13.730 3.696  1.00 18.07 ? 40  ALA B N   1 
ATOM   1315 C CA  . ALA B 1 7   ? 10.739 -12.869 4.073  1.00 19.54 ? 40  ALA B CA  1 
ATOM   1316 C C   . ALA B 1 7   ? 10.685 -12.659 5.580  1.00 20.47 ? 40  ALA B C   1 
ATOM   1317 O O   . ALA B 1 7   ? 10.438 -11.543 6.043  1.00 17.64 ? 40  ALA B O   1 
ATOM   1318 C CB  . ALA B 1 7   ? 9.415  -13.454 3.574  1.00 19.50 ? 40  ALA B CB  1 
ATOM   1319 N N   . GLU B 1 8   ? 10.926 -13.707 6.362  1.00 19.30 ? 41  GLU B N   1 
ATOM   1320 C CA  . GLU B 1 8   ? 10.773 -13.523 7.827  1.00 18.08 ? 41  GLU B CA  1 
ATOM   1321 C C   . GLU B 1 8   ? 11.922 -12.652 8.369  1.00 18.48 ? 41  GLU B C   1 
ATOM   1322 O O   . GLU B 1 8   ? 11.679 -11.842 9.256  1.00 17.25 ? 41  GLU B O   1 
ATOM   1323 C CB  . GLU B 1 8   ? 10.729 -14.875 8.532  1.00 18.79 ? 41  GLU B CB  1 
ATOM   1324 C CG  . GLU B 1 8   ? 9.447  -15.642 8.280  1.00 26.13 ? 41  GLU B CG  1 
ATOM   1325 C CD  . GLU B 1 8   ? 9.522  -17.134 8.547  1.00 39.52 ? 41  GLU B CD  1 
ATOM   1326 O OE1 . GLU B 1 8   ? 10.644 -17.662 8.635  1.00 49.20 ? 41  GLU B OE1 1 
ATOM   1327 O OE2 . GLU B 1 8   ? 8.459  -17.761 8.662  1.00 40.43 ? 41  GLU B OE2 1 
ATOM   1328 N N   . LEU B 1 9   ? 13.126 -12.862 7.852  1.00 16.57 ? 42  LEU B N   1 
ATOM   1329 C CA  . LEU B 1 9   ? 14.246 -12.037 8.296  1.00 16.74 ? 42  LEU B CA  1 
ATOM   1330 C C   . LEU B 1 9   ? 13.998 -10.570 7.967  1.00 15.57 ? 42  LEU B C   1 
ATOM   1331 O O   . LEU B 1 9   ? 14.146 -9.691  8.824  1.00 14.94 ? 42  LEU B O   1 
ATOM   1332 C CB  . LEU B 1 9   ? 15.548 -12.523 7.645  1.00 15.74 ? 42  LEU B CB  1 
ATOM   1333 C CG  . LEU B 1 9   ? 16.832 -11.712 7.857  1.00 14.98 ? 42  LEU B CG  1 
ATOM   1334 C CD1 . LEU B 1 9   ? 17.107 -11.448 9.335  1.00 16.31 ? 42  LEU B CD1 1 
ATOM   1335 C CD2 . LEU B 1 9   ? 18.024 -12.427 7.217  1.00 16.25 ? 42  LEU B CD2 1 
ATOM   1336 N N   . VAL B 1 10  ? 13.606 -10.288 6.723  1.00 15.54 ? 43  VAL B N   1 
ATOM   1337 C CA  . VAL B 1 10  ? 13.416 -8.894  6.329  1.00 15.30 ? 43  VAL B CA  1 
ATOM   1338 C C   . VAL B 1 10  ? 12.224 -8.290  7.052  1.00 15.51 ? 43  VAL B C   1 
ATOM   1339 O O   . VAL B 1 10  ? 12.239 -7.104  7.397  1.00 15.16 ? 43  VAL B O   1 
ATOM   1340 C CB  . VAL B 1 10  ? 13.283 -8.775  4.802  1.00 15.69 ? 43  VAL B CB  1 
ATOM   1341 C CG1 . VAL B 1 10  ? 13.034 -7.336  4.405  1.00 15.65 ? 43  VAL B CG1 1 
ATOM   1342 C CG2 . VAL B 1 10  ? 14.559 -9.290  4.142  1.00 15.54 ? 43  VAL B CG2 1 
ATOM   1343 N N   . ASP B 1 11  ? 11.181 -9.083  7.306  1.00 16.21 ? 44  ASP B N   1 
ATOM   1344 C CA  . ASP B 1 11  ? 10.036 -8.569  8.044  1.00 16.62 ? 44  ASP B CA  1 
ATOM   1345 C C   . ASP B 1 11  ? 10.421 -8.215  9.475  1.00 17.69 ? 44  ASP B C   1 
ATOM   1346 O O   . ASP B 1 11  ? 9.969  -7.191  10.008 1.00 18.61 ? 44  ASP B O   1 
ATOM   1347 C CB  . ASP B 1 11  ? 8.902  -9.588  8.021  1.00 19.61 ? 44  ASP B CB  1 
ATOM   1348 C CG  . ASP B 1 11  ? 7.638  -9.071  8.666  1.00 26.89 ? 44  ASP B CG  1 
ATOM   1349 O OD1 . ASP B 1 11  ? 7.005  -8.145  8.107  1.00 23.04 ? 44  ASP B OD1 1 
ATOM   1350 O OD2 . ASP B 1 11  ? 7.274  -9.602  9.734  1.00 36.35 ? 44  ASP B OD2 1 
ATOM   1351 N N   . ALA B 1 12  ? 11.258 -9.040  10.112 1.00 15.94 ? 45  ALA B N   1 
ATOM   1352 C CA  . ALA B 1 12  ? 11.727 -8.702  11.457 1.00 15.61 ? 45  ALA B CA  1 
ATOM   1353 C C   . ALA B 1 12  ? 12.580 -7.448  11.435 1.00 14.77 ? 45  ALA B C   1 
ATOM   1354 O O   . ALA B 1 12  ? 12.482 -6.606  12.332 1.00 15.38 ? 45  ALA B O   1 
ATOM   1355 C CB  . ALA B 1 12  ? 12.533 -9.846  12.060 1.00 15.74 ? 45  ALA B CB  1 
ATOM   1356 N N   . ALA B 1 13  ? 13.439 -7.316  10.425 1.00 14.46 ? 46  ALA B N   1 
ATOM   1357 C CA  . ALA B 1 13  ? 14.265 -6.117  10.334 1.00 13.79 ? 46  ALA B CA  1 
ATOM   1358 C C   . ALA B 1 13  ? 13.402 -4.869  10.154 1.00 14.79 ? 46  ALA B C   1 
ATOM   1359 O O   . ALA B 1 13  ? 13.668 -3.829  10.769 1.00 13.46 ? 46  ALA B O   1 
ATOM   1360 C CB  . ALA B 1 13  ? 15.271 -6.264  9.192  1.00 14.38 ? 46  ALA B CB  1 
ATOM   1361 N N   . ALA B 1 14  ? 12.357 -4.958  9.319  1.00 15.20 ? 47  ALA B N   1 
ATOM   1362 C CA  . ALA B 1 14  ? 11.436 -3.832  9.136  1.00 16.55 ? 47  ALA B CA  1 
ATOM   1363 C C   . ALA B 1 14  ? 10.695 -3.499  10.432 1.00 15.10 ? 47  ALA B C   1 
ATOM   1364 O O   . ALA B 1 14  ? 10.552 -2.317  10.807 1.00 16.23 ? 47  ALA B O   1 
ATOM   1365 C CB  . ALA B 1 14  ? 10.442 -4.157  8.015  1.00 15.38 ? 47  ALA B CB  1 
ATOM   1366 N N   . GLU B 1 15  ? 10.230 -4.531  11.142 1.00 15.13 ? 48  GLU B N   1 
ATOM   1367 C CA  . GLU B 1 15  ? 9.549  -4.288  12.408 1.00 16.81 ? 48  GLU B CA  1 
ATOM   1368 C C   . GLU B 1 15  ? 10.492 -3.631  13.405 1.00 14.75 ? 48  GLU B C   1 
ATOM   1369 O O   . GLU B 1 15  ? 10.087 -2.741  14.162 1.00 15.95 ? 48  GLU B O   1 
ATOM   1370 C CB  . GLU B 1 15  ? 8.982  -5.589  12.975 1.00 16.20 ? 48  GLU B CB  1 
ATOM   1371 C CG  . GLU B 1 15  ? 8.010  -5.358  14.118 1.00 23.90 ? 48  GLU B CG  1 
ATOM   1372 C CD  . GLU B 1 15  ? 7.415  -6.646  14.652 1.00 27.05 ? 48  GLU B CD  1 
ATOM   1373 O OE1 . GLU B 1 15  ? 7.314  -7.621  13.881 1.00 34.12 ? 48  GLU B OE1 1 
ATOM   1374 O OE2 . GLU B 1 15  ? 7.058  -6.681  15.850 1.00 32.04 ? 48  GLU B OE2 1 
ATOM   1375 N N   . ARG B 1 16  ? 11.758 -4.046  13.407 1.00 14.22 ? 49  ARG B N   1 
ATOM   1376 C CA  . ARG B 1 16  ? 12.741 -3.439  14.300 1.00 15.86 ? 49  ARG B CA  1 
ATOM   1377 C C   . ARG B 1 16  ? 12.987 -1.978  13.936 1.00 13.66 ? 49  ARG B C   1 
ATOM   1378 O O   . ARG B 1 16  ? 13.170 -1.143  14.824 1.00 14.49 ? 49  ARG B O   1 
ATOM   1379 C CB  . ARG B 1 16  ? 14.048 -4.232  14.257 1.00 15.16 ? 49  ARG B CB  1 
ATOM   1380 C CG  . ARG B 1 16  ? 14.898 -4.159  15.527 1.00 14.26 ? 49  ARG B CG  1 
ATOM   1381 C CD  . ARG B 1 16  ? 16.328 -4.553  15.199 1.00 19.86 ? 49  ARG B CD  1 
ATOM   1382 N NE  . ARG B 1 16  ? 17.215 -4.628  16.357 1.00 18.04 ? 49  ARG B NE  1 
ATOM   1383 C CZ  . ARG B 1 16  ? 17.968 -3.631  16.803 1.00 18.04 ? 49  ARG B CZ  1 
ATOM   1384 N NH1 . ARG B 1 16  ? 17.876 -2.410  16.301 1.00 16.47 ? 49  ARG B NH1 1 
ATOM   1385 N NH2 . ARG B 1 16  ? 18.847 -3.870  17.771 1.00 21.41 ? 49  ARG B NH2 1 
ATOM   1386 N N   . LEU B 1 17  ? 13.033 -1.660  12.631 1.00 13.20 ? 50  LEU B N   1 
ATOM   1387 C CA  . LEU B 1 17  ? 13.149 -0.261  12.209 1.00 13.67 ? 50  LEU B CA  1 
ATOM   1388 C C   . LEU B 1 17  ? 12.027 0.590   12.779 1.00 15.52 ? 50  LEU B C   1 
ATOM   1389 O O   . LEU B 1 17  ? 12.236 1.763   13.125 1.00 16.13 ? 50  LEU B O   1 
ATOM   1390 C CB  . LEU B 1 17  ? 13.121 -0.152  10.683 1.00 15.93 ? 50  LEU B CB  1 
ATOM   1391 C CG  . LEU B 1 17  ? 14.363 -0.599  9.936  1.00 15.90 ? 50  LEU B CG  1 
ATOM   1392 C CD1 . LEU B 1 17  ? 14.116 -0.472  8.441  1.00 13.66 ? 50  LEU B CD1 1 
ATOM   1393 C CD2 . LEU B 1 17  ? 15.564 0.230   10.378 1.00 17.69 ? 50  LEU B CD2 1 
ATOM   1394 N N   . GLU B 1 18  ? 10.816 0.034   12.829 1.00 13.90 ? 51  GLU B N   1 
ATOM   1395 C CA  . GLU B 1 18  ? 9.671  0.820   13.290 1.00 15.38 ? 51  GLU B CA  1 
ATOM   1396 C C   . GLU B 1 18  ? 9.779  1.241   14.757 1.00 16.53 ? 51  GLU B C   1 
ATOM   1397 O O   . GLU B 1 18  ? 9.034  2.131   15.180 1.00 16.62 ? 51  GLU B O   1 
ATOM   1398 C CB  . GLU B 1 18  ? 8.383  0.035   13.041 1.00 18.83 ? 51  GLU B CB  1 
ATOM   1399 C CG  . GLU B 1 18  ? 8.151  -0.204  11.551 1.00 22.59 ? 51  GLU B CG  1 
ATOM   1400 C CD  . GLU B 1 18  ? 6.968  -1.108  11.263 1.00 32.91 ? 51  GLU B CD  1 
ATOM   1401 O OE1 . GLU B 1 18  ? 6.310  -1.547  12.228 1.00 35.10 ? 51  GLU B OE1 1 
ATOM   1402 O OE2 . GLU B 1 18  ? 6.703  -1.383  10.068 1.00 32.68 ? 51  GLU B OE2 1 
ATOM   1403 N N   . VAL B 1 19  ? 10.693 0.654   15.536 1.00 14.09 ? 52  VAL B N   1 
ATOM   1404 C CA  . VAL B 1 19  ? 10.908 1.141   16.897 1.00 18.15 ? 52  VAL B CA  1 
ATOM   1405 C C   . VAL B 1 19  ? 11.526 2.539   16.901 1.00 17.53 ? 52  VAL B C   1 
ATOM   1406 O O   . VAL B 1 19  ? 11.479 3.239   17.919 1.00 17.90 ? 52  VAL B O   1 
ATOM   1407 C CB  . VAL B 1 19  ? 11.775 0.139   17.685 1.00 19.39 ? 52  VAL B CB  1 
ATOM   1408 C CG1 . VAL B 1 19  ? 11.854 0.519   19.150 1.00 26.55 ? 52  VAL B CG1 1 
ATOM   1409 C CG2 . VAL B 1 19  ? 11.188 -1.272  17.562 1.00 23.85 ? 52  VAL B CG2 1 
ATOM   1410 N N   . ALA B 1 20  ? 12.103 2.972   15.780 1.00 14.09 ? 53  ALA B N   1 
ATOM   1411 C CA  . ALA B 1 20  ? 12.657 4.322   15.707 1.00 14.82 ? 53  ALA B CA  1 
ATOM   1412 C C   . ALA B 1 20  ? 11.614 5.378   16.057 1.00 15.82 ? 53  ALA B C   1 
ATOM   1413 O O   . ALA B 1 20  ? 11.940 6.402   16.666 1.00 15.78 ? 53  ALA B O   1 
ATOM   1414 C CB  . ALA B 1 20  ? 13.216 4.583   14.307 1.00 12.97 ? 53  ALA B CB  1 
ATOM   1415 N N   . ASP B 1 21  ? 10.353 5.172   15.651 1.00 13.62 ? 54  ASP B N   1 
ATOM   1416 C CA  . ASP B 1 21  ? 9.362  6.227   15.877 1.00 14.36 ? 54  ASP B CA  1 
ATOM   1417 C C   . ASP B 1 21  ? 9.102  6.464   17.366 1.00 15.79 ? 54  ASP B C   1 
ATOM   1418 O O   . ASP B 1 21  ? 9.271  7.607   17.831 1.00 17.06 ? 54  ASP B O   1 
ATOM   1419 C CB  . ASP B 1 21  ? 8.091  5.930   15.076 1.00 17.61 ? 54  ASP B CB  1 
ATOM   1420 C CG  . ASP B 1 21  ? 8.082  6.641   13.736 1.00 22.09 ? 54  ASP B CG  1 
ATOM   1421 O OD1 . ASP B 1 21  ? 8.097  7.885   13.745 1.00 26.39 ? 54  ASP B OD1 1 
ATOM   1422 O OD2 . ASP B 1 21  ? 8.086  5.966   12.685 1.00 21.07 ? 54  ASP B OD2 1 
ATOM   1423 N N   . PRO B 1 22  ? 8.696  5.465   18.164 1.00 15.50 ? 55  PRO B N   1 
ATOM   1424 C CA  . PRO B 1 22  ? 8.518  5.746   19.604 1.00 17.98 ? 55  PRO B CA  1 
ATOM   1425 C C   . PRO B 1 22  ? 9.801  6.171   20.294 1.00 16.49 ? 55  PRO B C   1 
ATOM   1426 O O   . PRO B 1 22  ? 9.759  7.015   21.205 1.00 15.81 ? 55  PRO B O   1 
ATOM   1427 C CB  . PRO B 1 22  ? 7.977  4.424   20.168 1.00 23.01 ? 55  PRO B CB  1 
ATOM   1428 C CG  . PRO B 1 22  ? 8.374  3.387   19.181 1.00 24.07 ? 55  PRO B CG  1 
ATOM   1429 C CD  . PRO B 1 22  ? 8.329  4.074   17.840 1.00 18.87 ? 55  PRO B CD  1 
ATOM   1430 N N   . VAL B 1 23  ? 10.947 5.631   19.868 1.00 14.28 ? 56  VAL B N   1 
ATOM   1431 C CA  . VAL B 1 23  ? 12.214 6.031   20.467 1.00 13.89 ? 56  VAL B CA  1 
ATOM   1432 C C   . VAL B 1 23  ? 12.504 7.498   20.170 1.00 17.59 ? 56  VAL B C   1 
ATOM   1433 O O   . VAL B 1 23  ? 12.899 8.260   21.062 1.00 13.79 ? 56  VAL B O   1 
ATOM   1434 C CB  . VAL B 1 23  ? 13.352 5.111   19.987 1.00 15.62 ? 56  VAL B CB  1 
ATOM   1435 C CG1 . VAL B 1 23  ? 14.693 5.707   20.339 1.00 15.21 ? 56  VAL B CG1 1 
ATOM   1436 C CG2 . VAL B 1 23  ? 13.219 3.712   20.633 1.00 14.42 ? 56  VAL B CG2 1 
ATOM   1437 N N   . ALA B 1 24  ? 12.312 7.919   18.915 1.00 13.65 ? 57  ALA B N   1 
ATOM   1438 C CA  . ALA B 1 24  ? 12.553 9.321   18.587 1.00 13.29 ? 57  ALA B CA  1 
ATOM   1439 C C   . ALA B 1 24  ? 11.601 10.231  19.355 1.00 16.26 ? 57  ALA B C   1 
ATOM   1440 O O   . ALA B 1 24  ? 12.018 11.269  19.879 1.00 14.12 ? 57  ALA B O   1 
ATOM   1441 C CB  . ALA B 1 24  ? 12.427 9.550   17.077 1.00 14.46 ? 57  ALA B CB  1 
ATOM   1442 N N   . ALA B 1 25  ? 10.324 9.851   19.454 1.00 14.75 ? 58  ALA B N   1 
ATOM   1443 C CA  . ALA B 1 25  ? 9.381  10.698  20.182 1.00 16.43 ? 58  ALA B CA  1 
ATOM   1444 C C   . ALA B 1 25  ? 9.781  10.840  21.649 1.00 14.53 ? 58  ALA B C   1 
ATOM   1445 O O   . ALA B 1 25  ? 9.700  11.938  22.229 1.00 17.16 ? 58  ALA B O   1 
ATOM   1446 C CB  . ALA B 1 25  ? 7.967  10.135  20.059 1.00 15.03 ? 58  ALA B CB  1 
ATOM   1447 N N   . PHE B 1 26  ? 10.230 9.742   22.260 1.00 15.52 ? 59  PHE B N   1 
ATOM   1448 C CA  . PHE B 1 26  ? 10.692 9.810   23.641 1.00 16.74 ? 59  PHE B CA  1 
ATOM   1449 C C   . PHE B 1 26  ? 11.935 10.681  23.764 1.00 15.81 ? 59  PHE B C   1 
ATOM   1450 O O   . PHE B 1 26  ? 12.040 11.511  24.678 1.00 16.02 ? 59  PHE B O   1 
ATOM   1451 C CB  . PHE B 1 26  ? 10.976 8.404   24.174 1.00 14.43 ? 59  PHE B CB  1 
ATOM   1452 C CG  . PHE B 1 26  ? 11.309 8.386   25.640 1.00 14.77 ? 59  PHE B CG  1 
ATOM   1453 C CD1 . PHE B 1 26  ? 10.302 8.316   26.583 1.00 17.21 ? 59  PHE B CD1 1 
ATOM   1454 C CD2 . PHE B 1 26  ? 12.622 8.472   26.068 1.00 15.12 ? 59  PHE B CD2 1 
ATOM   1455 C CE1 . PHE B 1 26  ? 10.605 8.309   27.943 1.00 22.28 ? 59  PHE B CE1 1 
ATOM   1456 C CE2 . PHE B 1 26  ? 12.934 8.463   27.421 1.00 15.86 ? 59  PHE B CE2 1 
ATOM   1457 C CZ  . PHE B 1 26  ? 11.919 8.382   28.358 1.00 16.03 ? 59  PHE B CZ  1 
ATOM   1458 N N   . LYS B 1 27  ? 12.905 10.491  22.867 1.00 15.20 ? 60  LYS B N   1 
ATOM   1459 C CA  . LYS B 1 27  ? 14.127 11.282  22.959 1.00 14.62 ? 60  LYS B CA  1 
ATOM   1460 C C   . LYS B 1 27  ? 13.823 12.757  22.773 1.00 13.18 ? 60  LYS B C   1 
ATOM   1461 O O   . LYS B 1 27  ? 14.415 13.605  23.442 1.00 13.81 ? 60  LYS B O   1 
ATOM   1462 C CB  . LYS B 1 27  ? 15.156 10.820  21.930 1.00 13.03 ? 60  LYS B CB  1 
ATOM   1463 C CG  . LYS B 1 27  ? 15.833 9.483   22.249 1.00 14.63 ? 60  LYS B CG  1 
ATOM   1464 C CD  . LYS B 1 27  ? 16.810 9.130   21.119 1.00 17.29 ? 60  LYS B CD  1 
ATOM   1465 C CE  . LYS B 1 27  ? 17.669 7.934   21.467 1.00 22.32 ? 60  LYS B CE  1 
ATOM   1466 N NZ  . LYS B 1 27  ? 18.561 7.604   20.312 1.00 26.44 ? 60  LYS B NZ  1 
ATOM   1467 N N   . TRP B 1 28  ? 12.903 13.079  21.862 1.00 13.31 ? 61  TRP B N   1 
ATOM   1468 C CA  . TRP B 1 28  ? 12.552 14.475  21.603 1.00 13.60 ? 61  TRP B CA  1 
ATOM   1469 C C   . TRP B 1 28  ? 11.945 15.117  22.839 1.00 14.95 ? 61  TRP B C   1 
ATOM   1470 O O   . TRP B 1 28  ? 12.385 16.189  23.275 1.00 14.09 ? 61  TRP B O   1 
ATOM   1471 C CB  . TRP B 1 28  ? 11.574 14.563  20.429 1.00 14.24 ? 61  TRP B CB  1 
ATOM   1472 C CG  . TRP B 1 28  ? 11.131 15.961  20.136 1.00 14.63 ? 61  TRP B CG  1 
ATOM   1473 C CD1 . TRP B 1 28  ? 10.068 16.633  20.693 1.00 14.98 ? 61  TRP B CD1 1 
ATOM   1474 C CD2 . TRP B 1 28  ? 11.739 16.869  19.208 1.00 14.70 ? 61  TRP B CD2 1 
ATOM   1475 N NE1 . TRP B 1 28  ? 9.988  17.907  20.167 1.00 15.71 ? 61  TRP B NE1 1 
ATOM   1476 C CE2 . TRP B 1 28  ? 11.000 18.073  19.251 1.00 15.89 ? 61  TRP B CE2 1 
ATOM   1477 C CE3 . TRP B 1 28  ? 12.842 16.779  18.342 1.00 17.15 ? 61  TRP B CE3 1 
ATOM   1478 C CZ2 . TRP B 1 28  ? 11.332 19.182  18.469 1.00 15.58 ? 61  TRP B CZ2 1 
ATOM   1479 C CZ3 . TRP B 1 28  ? 13.167 17.877  17.565 1.00 14.80 ? 61  TRP B CZ3 1 
ATOM   1480 C CH2 . TRP B 1 28  ? 12.411 19.064  17.630 1.00 17.95 ? 61  TRP B CH2 1 
ATOM   1481 N N   . ARG B 1 29  ? 10.933 14.465  23.424 1.00 14.31 ? 62  ARG B N   1 
ATOM   1482 C CA  . ARG B 1 29  ? 10.235 15.054  24.566 1.00 16.88 ? 62  ARG B CA  1 
ATOM   1483 C C   . ARG B 1 29  ? 11.112 15.072  25.816 1.00 16.57 ? 62  ARG B C   1 
ATOM   1484 O O   . ARG B 1 29  ? 11.106 16.048  26.571 1.00 18.18 ? 62  ARG B O   1 
ATOM   1485 C CB  . ARG B 1 29  ? 8.932  14.293  24.823 1.00 18.36 ? 62  ARG B CB  1 
ATOM   1486 C CG  . ARG B 1 29  ? 7.995  14.914  25.866 1.00 27.20 ? 62  ARG B CG  1 
ATOM   1487 C CD  . ARG B 1 29  ? 7.983  16.434  25.784 1.00 39.24 ? 62  ARG B CD  1 
ATOM   1488 N NE  . ARG B 1 29  ? 6.724  17.030  26.226 1.00 51.57 ? 62  ARG B NE  1 
ATOM   1489 C CZ  . ARG B 1 29  ? 6.322  17.108  27.489 1.00 57.20 ? 62  ARG B CZ  1 
ATOM   1490 N NH1 . ARG B 1 29  ? 7.021  16.569  28.474 1.00 58.91 ? 62  ARG B NH1 1 
ATOM   1491 N NH2 . ARG B 1 29  ? 5.185  17.739  27.770 1.00 57.03 ? 62  ARG B NH2 1 
ATOM   1492 N N   . ALA B 1 30  ? 11.868 14.016  26.057 1.00 14.51 ? 63  ALA B N   1 
ATOM   1493 C CA  . ALA B 1 30  ? 12.680 13.920  27.261 1.00 14.67 ? 63  ALA B CA  1 
ATOM   1494 C C   . ALA B 1 30  ? 14.056 14.550  27.103 1.00 14.55 ? 63  ALA B C   1 
ATOM   1495 O O   . ALA B 1 30  ? 14.842 14.542  28.058 1.00 16.30 ? 63  ALA B O   1 
ATOM   1496 C CB  . ALA B 1 30  ? 12.820 12.456  27.677 1.00 15.20 ? 63  ALA B CB  1 
ATOM   1497 N N   . GLN B 1 31  ? 14.360 15.085  25.921 1.00 14.01 ? 64  GLN B N   1 
ATOM   1498 C CA  . GLN B 1 31  ? 15.607 15.796  25.646 1.00 13.92 ? 64  GLN B CA  1 
ATOM   1499 C C   . GLN B 1 31  ? 16.832 14.902  25.790 1.00 17.04 ? 64  GLN B C   1 
ATOM   1500 O O   . GLN B 1 31  ? 17.896 15.354  26.227 1.00 16.91 ? 64  GLN B O   1 
ATOM   1501 C CB  . GLN B 1 31  ? 15.728 17.050  26.521 1.00 16.09 ? 64  GLN B CB  1 
ATOM   1502 C CG  . GLN B 1 31  ? 14.599 18.041  26.219 1.00 14.53 ? 64  GLN B CG  1 
ATOM   1503 C CD  . GLN B 1 31  ? 14.812 19.401  26.851 1.00 17.53 ? 64  GLN B CD  1 
ATOM   1504 O OE1 . GLN B 1 31  ? 15.942 19.854  27.002 1.00 17.58 ? 64  GLN B OE1 1 
ATOM   1505 N NE2 . GLN B 1 31  ? 13.727 20.064  27.203 1.00 16.57 ? 64  GLN B NE2 1 
ATOM   1506 N N   A LEU B 1 32  ? 16.691 13.629  25.427 0.31 13.58 ? 65  LEU B N   1 
ATOM   1507 N N   B LEU B 1 32  ? 16.693 13.630  25.424 0.69 13.58 ? 65  LEU B N   1 
ATOM   1508 C CA  A LEU B 1 32  ? 17.838 12.737  25.372 0.31 13.54 ? 65  LEU B CA  1 
ATOM   1509 C CA  B LEU B 1 32  ? 17.845 12.741  25.372 0.69 13.54 ? 65  LEU B CA  1 
ATOM   1510 C C   A LEU B 1 32  ? 18.685 13.048  24.140 0.31 15.69 ? 65  LEU B C   1 
ATOM   1511 C C   B LEU B 1 32  ? 18.688 13.056  24.142 0.69 15.67 ? 65  LEU B C   1 
ATOM   1512 O O   A LEU B 1 32  ? 18.141 13.378  23.081 0.31 15.89 ? 65  LEU B O   1 
ATOM   1513 O O   B LEU B 1 32  ? 18.138 13.364  23.080 0.69 15.88 ? 65  LEU B O   1 
ATOM   1514 C CB  A LEU B 1 32  ? 17.382 11.279  25.322 0.31 14.84 ? 65  LEU B CB  1 
ATOM   1515 C CB  B LEU B 1 32  ? 17.422 11.271  25.302 0.69 14.74 ? 65  LEU B CB  1 
ATOM   1516 C CG  A LEU B 1 32  ? 16.962 10.591  26.622 0.31 14.61 ? 65  LEU B CG  1 
ATOM   1517 C CG  B LEU B 1 32  ? 17.190 10.468  26.582 0.69 14.52 ? 65  LEU B CG  1 
ATOM   1518 C CD1 A LEU B 1 32  ? 16.161 9.339   26.312 0.31 15.29 ? 65  LEU B CD1 1 
ATOM   1519 C CD1 B LEU B 1 32  ? 15.929 10.920  27.245 0.69 14.17 ? 65  LEU B CD1 1 
ATOM   1520 C CD2 A LEU B 1 32  ? 18.185 10.232  27.429 0.31 17.57 ? 65  LEU B CD2 1 
ATOM   1521 C CD2 B LEU B 1 32  ? 17.099 8.987   26.257 0.69 18.03 ? 65  LEU B CD2 1 
ATOM   1522 N N   . PRO B 1 33  ? 20.011 12.942  24.239 1.00 19.00 ? 66  PRO B N   1 
ATOM   1523 C CA  . PRO B 1 33  ? 20.840 13.035  23.033 1.00 19.52 ? 66  PRO B CA  1 
ATOM   1524 C C   . PRO B 1 33  ? 20.433 11.965  22.035 1.00 16.58 ? 66  PRO B C   1 
ATOM   1525 O O   . PRO B 1 33  ? 20.200 10.801  22.378 1.00 19.86 ? 66  PRO B O   1 
ATOM   1526 C CB  . PRO B 1 33  ? 22.267 12.826  23.554 1.00 23.52 ? 66  PRO B CB  1 
ATOM   1527 C CG  . PRO B 1 33  ? 22.110 12.213  24.915 1.00 32.07 ? 66  PRO B CG  1 
ATOM   1528 C CD  . PRO B 1 33  ? 20.795 12.675  25.457 1.00 21.15 ? 66  PRO B CD  1 
ATOM   1529 N N   . ILE B 1 34  ? 20.315 12.377  20.783 1.00 17.70 ? 67  ILE B N   1 
ATOM   1530 C CA  . ILE B 1 34  ? 19.866 11.442  19.774 1.00 16.00 ? 67  ILE B CA  1 
ATOM   1531 C C   . ILE B 1 34  ? 20.955 10.407  19.489 1.00 20.45 ? 67  ILE B C   1 
ATOM   1532 O O   . ILE B 1 34  ? 20.671 9.218   19.338 1.00 18.99 ? 67  ILE B O   1 
ATOM   1533 C CB  . ILE B 1 34  ? 19.417 12.218  18.521 1.00 20.21 ? 67  ILE B CB  1 
ATOM   1534 C CG1 . ILE B 1 34  ? 18.839 11.279  17.475 1.00 16.30 ? 67  ILE B CG1 1 
ATOM   1535 C CG2 . ILE B 1 34  ? 20.547 13.087  17.969 1.00 26.38 ? 67  ILE B CG2 1 
ATOM   1536 C CD1 . ILE B 1 34  ? 17.989 12.012  16.452 1.00 16.35 ? 67  ILE B CD1 1 
ATOM   1537 N N   . GLU B 1 35  ? 22.215 10.831  19.474 1.00 18.70 ? 68  GLU B N   1 
ATOM   1538 C CA  . GLU B 1 35  ? 23.347 9.939   19.240 1.00 17.02 ? 68  GLU B CA  1 
ATOM   1539 C C   . GLU B 1 35  ? 23.878 9.414   20.575 1.00 18.17 ? 68  GLU B C   1 
ATOM   1540 O O   . GLU B 1 35  ? 24.042 10.187  21.526 1.00 19.42 ? 68  GLU B O   1 
ATOM   1541 C CB  . GLU B 1 35  ? 24.443 10.700  18.486 1.00 19.21 ? 68  GLU B CB  1 
ATOM   1542 C CG  . GLU B 1 35  ? 25.563 9.840   17.919 1.00 14.66 ? 68  GLU B CG  1 
ATOM   1543 C CD  . GLU B 1 35  ? 25.251 9.338   16.549 1.00 18.58 ? 68  GLU B CD  1 
ATOM   1544 O OE1 . GLU B 1 35  ? 24.140 9.634   16.055 1.00 21.31 ? 68  GLU B OE1 1 
ATOM   1545 O OE2 . GLU B 1 35  ? 26.118 8.647   15.963 1.00 18.42 ? 68  GLU B OE2 1 
ATOM   1546 N N   . ASP B 1 36  ? 24.136 8.099   20.654 1.00 18.12 ? 69  ASP B N   1 
ATOM   1547 C CA  . ASP B 1 36  ? 24.664 7.502   21.893 1.00 20.24 ? 69  ASP B CA  1 
ATOM   1548 C C   . ASP B 1 36  ? 25.611 6.358   21.513 1.00 16.01 ? 69  ASP B C   1 
ATOM   1549 O O   . ASP B 1 36  ? 25.198 5.197   21.444 1.00 15.97 ? 69  ASP B O   1 
ATOM   1550 C CB  . ASP B 1 36  ? 23.514 7.019   22.759 1.00 21.76 ? 69  ASP B CB  1 
ATOM   1551 C CG  . ASP B 1 36  ? 23.955 6.518   24.123 1.00 31.57 ? 69  ASP B CG  1 
ATOM   1552 O OD1 . ASP B 1 36  ? 25.169 6.365   24.382 1.00 24.48 ? 69  ASP B OD1 1 
ATOM   1553 O OD2 . ASP B 1 36  ? 23.051 6.274   24.943 1.00 33.15 ? 69  ASP B OD2 1 
ATOM   1554 N N   . SER B 1 37  ? 26.893 6.688   21.324 1.00 13.88 ? 70  SER B N   1 
ATOM   1555 C CA  . SER B 1 37  ? 27.820 5.685   20.805 1.00 14.13 ? 70  SER B CA  1 
ATOM   1556 C C   . SER B 1 37  ? 28.118 4.602   21.839 1.00 18.13 ? 70  SER B C   1 
ATOM   1557 O O   . SER B 1 37  ? 28.386 3.450   21.464 1.00 14.68 ? 70  SER B O   1 
ATOM   1558 C CB  . SER B 1 37  ? 29.118 6.337   20.317 1.00 14.47 ? 70  SER B CB  1 
ATOM   1559 O OG  . SER B 1 37  ? 29.901 6.828   21.393 1.00 18.13 ? 70  SER B OG  1 
ATOM   1560 N N   . GLY B 1 38  ? 28.061 4.941   23.134 1.00 17.10 ? 71  GLY B N   1 
ATOM   1561 C CA  . GLY B 1 38  ? 28.295 3.934   24.166 1.00 17.80 ? 71  GLY B CA  1 
ATOM   1562 C C   . GLY B 1 38  ? 27.232 2.846   24.176 1.00 21.01 ? 71  GLY B C   1 
ATOM   1563 O O   . GLY B 1 38  ? 27.541 1.655   24.325 1.00 17.48 ? 71  GLY B O   1 
ATOM   1564 N N   . ARG B 1 39  ? 25.965 3.239   24.006 1.00 17.14 ? 72  ARG B N   1 
ATOM   1565 C CA  . ARG B 1 39  ? 24.895 2.255   23.875 1.00 19.87 ? 72  ARG B CA  1 
ATOM   1566 C C   . ARG B 1 39  ? 25.060 1.408   22.616 1.00 17.40 ? 72  ARG B C   1 
ATOM   1567 O O   . ARG B 1 39  ? 24.828 0.195   22.648 1.00 18.01 ? 72  ARG B O   1 
ATOM   1568 C CB  . ARG B 1 39  ? 23.528 2.942   23.884 1.00 21.99 ? 72  ARG B CB  1 
ATOM   1569 C CG  . ARG B 1 39  ? 22.974 3.168   25.298 1.00 34.52 ? 72  ARG B CG  1 
ATOM   1570 C CD  . ARG B 1 39  ? 21.449 3.246   25.322 1.00 39.65 ? 72  ARG B CD  1 
ATOM   1571 N NE  . ARG B 1 39  ? 20.913 3.153   26.678 1.00 38.49 ? 72  ARG B NE  1 
ATOM   1572 C CZ  . ARG B 1 39  ? 20.627 4.198   27.447 1.00 43.63 ? 72  ARG B CZ  1 
ATOM   1573 N NH1 . ARG B 1 39  ? 20.803 5.439   27.021 1.00 39.79 ? 72  ARG B NH1 1 
ATOM   1574 N NH2 . ARG B 1 39  ? 20.145 3.993   28.671 1.00 37.38 ? 72  ARG B NH2 1 
ATOM   1575 N N   . VAL B 1 40  ? 25.439 2.025   21.492 1.00 14.82 ? 73  VAL B N   1 
ATOM   1576 C CA  . VAL B 1 40  ? 25.669 1.240   20.277 1.00 14.21 ? 73  VAL B CA  1 
ATOM   1577 C C   . VAL B 1 40  ? 26.762 0.203   20.512 1.00 15.20 ? 73  VAL B C   1 
ATOM   1578 O O   . VAL B 1 40  ? 26.631 -0.959  20.109 1.00 14.28 ? 73  VAL B O   1 
ATOM   1579 C CB  . VAL B 1 40  ? 26.015 2.158   19.089 1.00 15.30 ? 73  VAL B CB  1 
ATOM   1580 C CG1 . VAL B 1 40  ? 26.480 1.316   17.895 1.00 14.02 ? 73  VAL B CG1 1 
ATOM   1581 C CG2 . VAL B 1 40  ? 24.815 3.027   18.719 1.00 14.76 ? 73  VAL B CG2 1 
ATOM   1582 N N   . GLU B 1 41  ? 27.860 0.605   21.161 1.00 12.18 ? 74  GLU B N   1 
ATOM   1583 C CA  . GLU B 1 41  ? 28.922 -0.355  21.434 1.00 14.33 ? 74  GLU B CA  1 
ATOM   1584 C C   . GLU B 1 41  ? 28.430 -1.480  22.341 1.00 16.87 ? 74  GLU B C   1 
ATOM   1585 O O   . GLU B 1 41  ? 28.738 -2.649  22.099 1.00 14.59 ? 74  GLU B O   1 
ATOM   1586 C CB  . GLU B 1 41  ? 30.140 0.353   22.039 1.00 14.64 ? 74  GLU B CB  1 
ATOM   1587 C CG  . GLU B 1 41  ? 31.222 -0.579  22.606 1.00 17.31 ? 74  GLU B CG  1 
ATOM   1588 C CD  . GLU B 1 41  ? 31.972 -1.379  21.537 1.00 18.03 ? 74  GLU B CD  1 
ATOM   1589 O OE1 . GLU B 1 41  ? 31.892 -1.039  20.338 1.00 15.82 ? 74  GLU B OE1 1 
ATOM   1590 O OE2 . GLU B 1 41  ? 32.646 -2.369  21.907 1.00 19.26 ? 74  GLU B OE2 1 
ATOM   1591 N N   A GLN B 1 42  ? 27.670 -1.151  23.392 0.50 17.80 ? 75  GLN B N   1 
ATOM   1592 N N   B GLN B 1 42  ? 27.662 -1.155  23.388 0.50 17.80 ? 75  GLN B N   1 
ATOM   1593 C CA  A GLN B 1 42  ? 27.167 -2.210  24.268 0.50 18.23 ? 75  GLN B CA  1 
ATOM   1594 C CA  B GLN B 1 42  ? 27.177 -2.221  24.267 0.50 18.22 ? 75  GLN B CA  1 
ATOM   1595 C C   A GLN B 1 42  ? 26.265 -3.179  23.505 0.50 17.69 ? 75  GLN B C   1 
ATOM   1596 C C   B GLN B 1 42  ? 26.258 -3.182  23.513 0.50 17.69 ? 75  GLN B C   1 
ATOM   1597 O O   A GLN B 1 42  ? 26.378 -4.404  23.665 0.50 18.67 ? 75  GLN B O   1 
ATOM   1598 O O   B GLN B 1 42  ? 26.361 -4.408  23.674 0.50 18.66 ? 75  GLN B O   1 
ATOM   1599 C CB  A GLN B 1 42  ? 26.424 -1.605  25.460 0.50 22.45 ? 75  GLN B CB  1 
ATOM   1600 C CB  B GLN B 1 42  ? 26.477 -1.632  25.499 0.50 22.46 ? 75  GLN B CB  1 
ATOM   1601 C CG  A GLN B 1 42  ? 27.328 -0.886  26.457 0.50 23.09 ? 75  GLN B CG  1 
ATOM   1602 C CG  B GLN B 1 42  ? 24.975 -1.409  25.384 0.50 25.46 ? 75  GLN B CG  1 
ATOM   1603 C CD  A GLN B 1 42  ? 26.578 -0.410  27.686 0.50 27.81 ? 75  GLN B CD  1 
ATOM   1604 C CD  B GLN B 1 42  ? 24.344 -1.000  26.702 0.50 26.48 ? 75  GLN B CD  1 
ATOM   1605 O OE1 A GLN B 1 42  ? 26.098 0.724   27.734 0.50 32.27 ? 75  GLN B OE1 1 
ATOM   1606 O OE1 B GLN B 1 42  ? 25.039 -0.612  27.638 0.50 32.31 ? 75  GLN B OE1 1 
ATOM   1607 N NE2 A GLN B 1 42  ? 26.470 -1.279  28.690 0.50 25.88 ? 75  GLN B NE2 1 
ATOM   1608 N NE2 B GLN B 1 42  ? 23.022 -1.091  26.780 0.50 25.73 ? 75  GLN B NE2 1 
ATOM   1609 N N   . GLN B 1 43  ? 25.381 -2.647  22.653 1.00 16.40 ? 76  GLN B N   1 
ATOM   1610 C CA  . GLN B 1 43  ? 24.482 -3.496  21.869 1.00 18.15 ? 76  GLN B CA  1 
ATOM   1611 C C   . GLN B 1 43  ? 25.251 -4.373  20.892 1.00 14.53 ? 76  GLN B C   1 
ATOM   1612 O O   . GLN B 1 43  ? 24.973 -5.570  20.765 1.00 13.77 ? 76  GLN B O   1 
ATOM   1613 C CB  . GLN B 1 43  ? 23.479 -2.651  21.085 1.00 17.62 ? 76  GLN B CB  1 
ATOM   1614 C CG  . GLN B 1 43  ? 22.446 -1.886  21.885 1.00 26.39 ? 76  GLN B CG  1 
ATOM   1615 C CD  . GLN B 1 43  ? 21.518 -1.119  20.961 1.00 39.79 ? 76  GLN B CD  1 
ATOM   1616 O OE1 . GLN B 1 43  ? 20.713 -1.712  20.228 1.00 42.20 ? 76  GLN B OE1 1 
ATOM   1617 N NE2 . GLN B 1 43  ? 21.656 0.202   20.955 1.00 36.42 ? 76  GLN B NE2 1 
ATOM   1618 N N   . LEU B 1 44  ? 26.212 -3.789  20.173 1.00 14.49 ? 77  LEU B N   1 
ATOM   1619 C CA  . LEU B 1 44  ? 26.965 -4.561  19.190 1.00 13.52 ? 77  LEU B CA  1 
ATOM   1620 C C   . LEU B 1 44  ? 27.832 -5.624  19.859 1.00 14.27 ? 77  LEU B C   1 
ATOM   1621 O O   . LEU B 1 44  ? 27.970 -6.739  19.332 1.00 14.34 ? 77  LEU B O   1 
ATOM   1622 C CB  . LEU B 1 44  ? 27.813 -3.632  18.325 1.00 11.46 ? 77  LEU B CB  1 
ATOM   1623 C CG  . LEU B 1 44  ? 26.987 -2.759  17.361 1.00 11.50 ? 77  LEU B CG  1 
ATOM   1624 C CD1 . LEU B 1 44  ? 27.914 -1.899  16.500 1.00 12.69 ? 77  LEU B CD1 1 
ATOM   1625 C CD2 . LEU B 1 44  ? 26.077 -3.612  16.465 1.00 14.03 ? 77  LEU B CD2 1 
ATOM   1626 N N   . ALA B 1 45  ? 28.437 -5.307  21.008 1.00 14.17 ? 78  ALA B N   1 
ATOM   1627 C CA  . ALA B 1 45  ? 29.224 -6.322  21.705 1.00 16.19 ? 78  ALA B CA  1 
ATOM   1628 C C   . ALA B 1 45  ? 28.336 -7.479  22.148 1.00 16.98 ? 78  ALA B C   1 
ATOM   1629 O O   . ALA B 1 45  ? 28.684 -8.664  21.963 1.00 17.10 ? 78  ALA B O   1 
ATOM   1630 C CB  . ALA B 1 45  ? 29.944 -5.704  22.906 1.00 19.82 ? 78  ALA B CB  1 
ATOM   1631 N N   . LYS B 1 46  ? 27.167 -7.157  22.728 1.00 17.35 ? 79  LYS B N   1 
ATOM   1632 C CA  . LYS B 1 46  ? 26.259 -8.228  23.127 1.00 16.05 ? 79  LYS B CA  1 
ATOM   1633 C C   . LYS B 1 46  ? 25.813 -9.056  21.925 1.00 18.00 ? 79  LYS B C   1 
ATOM   1634 O O   . LYS B 1 46  ? 25.744 -10.286 22.003 1.00 16.30 ? 79  LYS B O   1 
ATOM   1635 C CB  . LYS B 1 46  ? 25.044 -7.660  23.859 1.00 18.05 ? 79  LYS B CB  1 
ATOM   1636 C CG  . LYS B 1 46  ? 24.082 -8.731  24.357 1.00 25.03 ? 79  LYS B CG  1 
ATOM   1637 C CD  . LYS B 1 46  ? 22.834 -8.109  24.958 1.00 29.48 ? 79  LYS B CD  1 
ATOM   1638 C CE  . LYS B 1 46  ? 22.025 -9.134  25.744 1.00 34.21 ? 79  LYS B CE  1 
ATOM   1639 N NZ  . LYS B 1 46  ? 21.808 -10.402 24.988 1.00 45.15 ? 79  LYS B NZ  1 
ATOM   1640 N N   . LEU B 1 47  ? 25.507 -8.402  20.801 1.00 15.21 ? 80  LEU B N   1 
ATOM   1641 C CA  . LEU B 1 47  ? 25.039 -9.149  19.638 1.00 15.38 ? 80  LEU B CA  1 
ATOM   1642 C C   . LEU B 1 47  ? 26.134 -10.040 19.068 1.00 16.37 ? 80  LEU B C   1 
ATOM   1643 O O   . LEU B 1 47  ? 25.850 -11.136 18.571 1.00 17.07 ? 80  LEU B O   1 
ATOM   1644 C CB  . LEU B 1 47  ? 24.520 -8.198  18.569 1.00 13.21 ? 80  LEU B CB  1 
ATOM   1645 C CG  . LEU B 1 47  ? 23.163 -7.601  18.920 1.00 16.50 ? 80  LEU B CG  1 
ATOM   1646 C CD1 . LEU B 1 47  ? 22.943 -6.357  18.082 1.00 16.30 ? 80  LEU B CD1 1 
ATOM   1647 C CD2 . LEU B 1 47  ? 22.059 -8.631  18.688 1.00 18.26 ? 80  LEU B CD2 1 
ATOM   1648 N N   . GLY B 1 48  ? 27.389 -9.588  19.118 1.00 13.40 ? 81  GLY B N   1 
ATOM   1649 C CA  . GLY B 1 48  ? 28.477 -10.460 18.706 1.00 16.80 ? 81  GLY B CA  1 
ATOM   1650 C C   . GLY B 1 48  ? 28.536 -11.726 19.541 1.00 20.18 ? 81  GLY B C   1 
ATOM   1651 O O   . GLY B 1 48  ? 28.735 -12.830 19.014 1.00 20.11 ? 81  GLY B O   1 
ATOM   1652 N N   . GLU B 1 49  ? 28.342 -11.591 20.857 1.00 15.19 ? 82  GLU B N   1 
ATOM   1653 C CA  . GLU B 1 49  ? 28.409 -12.797 21.687 1.00 16.36 ? 82  GLU B CA  1 
ATOM   1654 C C   . GLU B 1 49  ? 27.162 -13.680 21.563 1.00 17.47 ? 82  GLU B C   1 
ATOM   1655 O O   . GLU B 1 49  ? 27.262 -14.911 21.680 1.00 17.49 ? 82  GLU B O   1 
ATOM   1656 C CB  . GLU B 1 49  ? 28.669 -12.407 23.135 1.00 20.76 ? 82  GLU B CB  1 
ATOM   1657 C CG  . GLU B 1 49  ? 30.009 -11.709 23.286 1.00 24.29 ? 82  GLU B CG  1 
ATOM   1658 C CD  . GLU B 1 49  ? 31.139 -12.438 22.558 1.00 27.28 ? 82  GLU B CD  1 
ATOM   1659 O OE1 . GLU B 1 49  ? 31.272 -13.671 22.734 1.00 25.19 ? 82  GLU B OE1 1 
ATOM   1660 O OE2 . GLU B 1 49  ? 31.889 -11.777 21.800 1.00 19.99 ? 82  GLU B OE2 1 
ATOM   1661 N N   . ASP B 1 50  ? 25.990 -13.083 21.322 1.00 16.21 ? 83  ASP B N   1 
ATOM   1662 C CA  . ASP B 1 50  ? 24.809 -13.884 21.003 1.00 16.78 ? 83  ASP B CA  1 
ATOM   1663 C C   . ASP B 1 50  ? 25.010 -14.660 19.709 1.00 16.30 ? 83  ASP B C   1 
ATOM   1664 O O   . ASP B 1 50  ? 24.642 -15.838 19.615 1.00 19.19 ? 83  ASP B O   1 
ATOM   1665 C CB  . ASP B 1 50  ? 23.570 -12.995 20.900 1.00 16.61 ? 83  ASP B CB  1 
ATOM   1666 C CG  . ASP B 1 50  ? 23.216 -12.329 22.219 1.00 31.65 ? 83  ASP B CG  1 
ATOM   1667 O OD1 . ASP B 1 50  ? 23.657 -12.830 23.283 1.00 26.65 ? 83  ASP B OD1 1 
ATOM   1668 O OD2 . ASP B 1 50  ? 22.489 -11.306 22.190 1.00 32.58 ? 83  ASP B OD2 1 
ATOM   1669 N N   . ALA B 1 51  ? 25.603 -14.012 18.701 1.00 17.66 ? 84  ALA B N   1 
ATOM   1670 C CA  . ALA B 1 51  ? 25.937 -14.698 17.459 1.00 19.73 ? 84  ALA B CA  1 
ATOM   1671 C C   . ALA B 1 51  ? 26.845 -15.885 17.732 1.00 18.64 ? 84  ALA B C   1 
ATOM   1672 O O   . ALA B 1 51  ? 26.594 -17.001 17.254 1.00 18.65 ? 84  ALA B O   1 
ATOM   1673 C CB  . ALA B 1 51  ? 26.605 -13.719 16.489 1.00 18.05 ? 84  ALA B CB  1 
ATOM   1674 N N   . ARG B 1 52  ? 27.896 -15.668 18.532 1.00 16.93 ? 85  ARG B N   1 
ATOM   1675 C CA  . ARG B 1 52  ? 28.794 -16.771 18.876 1.00 19.65 ? 85  ARG B CA  1 
ATOM   1676 C C   . ARG B 1 52  ? 28.031 -17.897 19.561 1.00 19.52 ? 85  ARG B C   1 
ATOM   1677 O O   . ARG B 1 52  ? 28.278 -19.081 19.297 1.00 20.36 ? 85  ARG B O   1 
ATOM   1678 C CB  . ARG B 1 52  ? 29.926 -16.261 19.770 1.00 17.91 ? 85  ARG B CB  1 
ATOM   1679 C CG  . ARG B 1 52  ? 31.133 -17.175 19.832 1.00 24.02 ? 85  ARG B CG  1 
ATOM   1680 C CD  . ARG B 1 52  ? 32.137 -16.688 20.879 1.00 24.45 ? 85  ARG B CD  1 
ATOM   1681 N NE  . ARG B 1 52  ? 32.414 -15.262 20.727 1.00 23.55 ? 85  ARG B NE  1 
ATOM   1682 C CZ  . ARG B 1 52  ? 33.233 -14.747 19.821 1.00 26.18 ? 85  ARG B CZ  1 
ATOM   1683 N NH1 . ARG B 1 52  ? 33.887 -15.514 18.963 1.00 24.34 ? 85  ARG B NH1 1 
ATOM   1684 N NH2 . ARG B 1 52  ? 33.396 -13.426 19.769 1.00 26.00 ? 85  ARG B NH2 1 
ATOM   1685 N N   . SER B 1 53  ? 27.087 -17.540 20.437 1.00 19.48 ? 86  SER B N   1 
ATOM   1686 C CA  . SER B 1 53  ? 26.252 -18.526 21.121 1.00 19.54 ? 86  SER B CA  1 
ATOM   1687 C C   . SER B 1 53  ? 25.388 -19.328 20.151 1.00 20.97 ? 86  SER B C   1 
ATOM   1688 O O   . SER B 1 53  ? 25.050 -20.487 20.430 1.00 21.66 ? 86  SER B O   1 
ATOM   1689 C CB  . SER B 1 53  ? 25.366 -17.813 22.145 1.00 19.83 ? 86  SER B CB  1 
ATOM   1690 O OG  . SER B 1 53  ? 24.398 -18.688 22.677 1.00 46.18 ? 86  SER B OG  1 
ATOM   1691 N N   . GLN B 1 54  ? 24.993 -18.726 19.030 1.00 19.13 ? 87  GLN B N   1 
ATOM   1692 C CA  . GLN B 1 54  ? 24.164 -19.395 18.033 1.00 18.74 ? 87  GLN B CA  1 
ATOM   1693 C C   . GLN B 1 54  ? 24.977 -19.877 16.835 1.00 18.91 ? 87  GLN B C   1 
ATOM   1694 O O   . GLN B 1 54  ? 24.401 -20.173 15.778 1.00 22.77 ? 87  GLN B O   1 
ATOM   1695 C CB  . GLN B 1 54  ? 23.029 -18.467 17.590 1.00 18.25 ? 87  GLN B CB  1 
ATOM   1696 C CG  . GLN B 1 54  ? 22.089 -18.125 18.743 1.00 19.88 ? 87  GLN B CG  1 
ATOM   1697 C CD  . GLN B 1 54  ? 20.863 -17.348 18.305 1.00 20.32 ? 87  GLN B CD  1 
ATOM   1698 O OE1 . GLN B 1 54  ? 20.205 -17.691 17.312 1.00 19.29 ? 87  GLN B OE1 1 
ATOM   1699 N NE2 . GLN B 1 54  ? 20.546 -16.302 19.041 1.00 18.76 ? 87  GLN B NE2 1 
ATOM   1700 N N   . HIS B 1 55  ? 26.305 -19.959 16.991 1.00 18.84 ? 88  HIS B N   1 
ATOM   1701 C CA  . HIS B 1 55  ? 27.210 -20.515 15.982 1.00 20.16 ? 88  HIS B CA  1 
ATOM   1702 C C   . HIS B 1 55  ? 27.109 -19.754 14.663 1.00 22.73 ? 88  HIS B C   1 
ATOM   1703 O O   . HIS B 1 55  ? 27.104 -20.348 13.581 1.00 23.20 ? 88  HIS B O   1 
ATOM   1704 C CB  . HIS B 1 55  ? 26.952 -22.012 15.775 1.00 24.35 ? 88  HIS B CB  1 
ATOM   1705 C CG  . HIS B 1 55  ? 26.721 -22.757 17.052 1.00 31.04 ? 88  HIS B CG  1 
ATOM   1706 N ND1 . HIS B 1 55  ? 25.459 -23.070 17.514 1.00 34.77 ? 88  HIS B ND1 1 
ATOM   1707 C CD2 . HIS B 1 55  ? 27.587 -23.223 17.982 1.00 31.41 ? 88  HIS B CD2 1 
ATOM   1708 C CE1 . HIS B 1 55  ? 25.559 -23.706 18.668 1.00 35.35 ? 88  HIS B CE1 1 
ATOM   1709 N NE2 . HIS B 1 55  ? 26.840 -23.815 18.973 1.00 36.96 ? 88  HIS B NE2 1 
ATOM   1710 N N   . ILE B 1 56  ? 27.012 -18.428 14.765 1.00 18.52 ? 89  ILE B N   1 
ATOM   1711 C CA  . ILE B 1 56  ? 27.061 -17.510 13.631 1.00 19.64 ? 89  ILE B CA  1 
ATOM   1712 C C   . ILE B 1 56  ? 28.362 -16.727 13.726 1.00 21.27 ? 89  ILE B C   1 
ATOM   1713 O O   . ILE B 1 56  ? 28.805 -16.384 14.829 1.00 19.94 ? 89  ILE B O   1 
ATOM   1714 C CB  . ILE B 1 56  ? 25.877 -16.523 13.626 1.00 21.53 ? 89  ILE B CB  1 
ATOM   1715 C CG1 . ILE B 1 56  ? 24.535 -17.224 13.852 1.00 20.72 ? 89  ILE B CG1 1 
ATOM   1716 C CG2 . ILE B 1 56  ? 25.869 -15.714 12.339 1.00 21.34 ? 89  ILE B CG2 1 
ATOM   1717 C CD1 . ILE B 1 56  ? 23.384 -16.235 14.074 1.00 21.75 ? 89  ILE B CD1 1 
ATOM   1718 N N   . ASP B 1 57  ? 28.950 -16.414 12.582 1.00 17.22 ? 90  ASP B N   1 
ATOM   1719 C CA  . ASP B 1 57  ? 30.162 -15.600 12.563 1.00 20.33 ? 90  ASP B CA  1 
ATOM   1720 C C   . ASP B 1 57  ? 29.877 -14.253 13.218 1.00 19.32 ? 90  ASP B C   1 
ATOM   1721 O O   . ASP B 1 57  ? 28.989 -13.521 12.752 1.00 19.18 ? 90  ASP B O   1 
ATOM   1722 C CB  . ASP B 1 57  ? 30.650 -15.396 11.130 1.00 23.66 ? 90  ASP B CB  1 
ATOM   1723 C CG  . ASP B 1 57  ? 31.821 -14.432 11.047 1.00 29.97 ? 90  ASP B CG  1 
ATOM   1724 O OD1 . ASP B 1 57  ? 32.801 -14.615 11.796 1.00 41.30 ? 90  ASP B OD1 1 
ATOM   1725 O OD2 . ASP B 1 57  ? 31.764 -13.497 10.229 1.00 37.00 ? 90  ASP B OD2 1 
ATOM   1726 N N   . PRO B 1 58  ? 30.569 -13.904 14.307 1.00 18.27 ? 91  PRO B N   1 
ATOM   1727 C CA  . PRO B 1 58  ? 30.252 -12.643 14.996 1.00 18.64 ? 91  PRO B CA  1 
ATOM   1728 C C   . PRO B 1 58  ? 30.455 -11.403 14.148 1.00 18.45 ? 91  PRO B C   1 
ATOM   1729 O O   . PRO B 1 58  ? 29.710 -10.428 14.320 1.00 13.58 ? 91  PRO B O   1 
ATOM   1730 C CB  . PRO B 1 58  ? 31.199 -12.656 16.206 1.00 17.01 ? 91  PRO B CB  1 
ATOM   1731 C CG  . PRO B 1 58  ? 31.489 -14.123 16.432 1.00 16.46 ? 91  PRO B CG  1 
ATOM   1732 C CD  . PRO B 1 58  ? 31.546 -14.715 15.052 1.00 19.70 ? 91  PRO B CD  1 
ATOM   1733 N N   . ASP B 1 59  ? 31.444 -11.399 13.253 1.00 14.10 ? 92  ASP B N   1 
ATOM   1734 C CA  . ASP B 1 59  ? 31.737 -10.189 12.479 1.00 19.91 ? 92  ASP B CA  1 
ATOM   1735 C C   . ASP B 1 59  ? 30.646 -9.908  11.455 1.00 18.33 ? 92  ASP B C   1 
ATOM   1736 O O   . ASP B 1 59  ? 30.290 -8.742  11.213 1.00 18.86 ? 92  ASP B O   1 
ATOM   1737 C CB  . ASP B 1 59  ? 33.099 -10.329 11.804 1.00 23.55 ? 92  ASP B CB  1 
ATOM   1738 C CG  . ASP B 1 59  ? 34.240 -10.332 12.806 1.00 32.75 ? 92  ASP B CG  1 
ATOM   1739 O OD1 . ASP B 1 59  ? 34.152 -9.592  13.815 1.00 33.81 ? 92  ASP B OD1 1 
ATOM   1740 O OD2 . ASP B 1 59  ? 35.217 -11.076 12.593 1.00 36.36 ? 92  ASP B OD2 1 
ATOM   1741 N N   . TYR B 1 60  ? 30.090 -10.965 10.860 1.00 17.43 ? 93  TYR B N   1 
ATOM   1742 C CA  . TYR B 1 60  ? 28.928 -10.813 9.984  1.00 15.91 ? 93  TYR B CA  1 
ATOM   1743 C C   . TYR B 1 60  ? 27.772 -10.171 10.734 1.00 15.37 ? 93  TYR B C   1 
ATOM   1744 O O   . TYR B 1 60  ? 27.146 -9.212  10.252 1.00 15.64 ? 93  TYR B O   1 
ATOM   1745 C CB  . TYR B 1 60  ? 28.508 -12.181 9.439  1.00 14.97 ? 93  TYR B CB  1 
ATOM   1746 C CG  . TYR B 1 60  ? 27.238 -12.163 8.621  1.00 18.75 ? 93  TYR B CG  1 
ATOM   1747 C CD1 . TYR B 1 60  ? 27.276 -11.956 7.243  1.00 16.45 ? 93  TYR B CD1 1 
ATOM   1748 C CD2 . TYR B 1 60  ? 25.997 -12.349 9.221  1.00 14.36 ? 93  TYR B CD2 1 
ATOM   1749 C CE1 . TYR B 1 60  ? 26.110 -11.944 6.486  1.00 18.33 ? 93  TYR B CE1 1 
ATOM   1750 C CE2 . TYR B 1 60  ? 24.827 -12.326 8.474  1.00 15.65 ? 93  TYR B CE2 1 
ATOM   1751 C CZ  . TYR B 1 60  ? 24.893 -12.121 7.106  1.00 20.28 ? 93  TYR B CZ  1 
ATOM   1752 O OH  . TYR B 1 60  ? 23.730 -12.113 6.368  1.00 15.97 ? 93  TYR B OH  1 
ATOM   1753 N N   . VAL B 1 61  ? 27.486 -10.685 11.934 1.00 14.07 ? 94  VAL B N   1 
ATOM   1754 C CA  . VAL B 1 61  ? 26.355 -10.184 12.707 1.00 14.11 ? 94  VAL B CA  1 
ATOM   1755 C C   . VAL B 1 61  ? 26.576 -8.741  13.139 1.00 14.92 ? 94  VAL B C   1 
ATOM   1756 O O   . VAL B 1 61  ? 25.652 -7.923  13.062 1.00 13.12 ? 94  VAL B O   1 
ATOM   1757 C CB  . VAL B 1 61  ? 26.067 -11.100 13.905 1.00 13.94 ? 94  VAL B CB  1 
ATOM   1758 C CG1 . VAL B 1 61  ? 25.121 -10.388 14.910 1.00 14.78 ? 94  VAL B CG1 1 
ATOM   1759 C CG2 . VAL B 1 61  ? 25.459 -12.402 13.402 1.00 14.00 ? 94  VAL B CG2 1 
ATOM   1760 N N   . THR B 1 62  ? 27.780 -8.395  13.621 1.00 13.18 ? 95  THR B N   1 
ATOM   1761 C CA  . THR B 1 62  ? 27.967 -7.015  14.067 1.00 13.23 ? 95  THR B CA  1 
ATOM   1762 C C   . THR B 1 62  ? 27.924 -6.037  12.900 1.00 14.85 ? 95  THR B C   1 
ATOM   1763 O O   . THR B 1 62  ? 27.428 -4.917  13.066 1.00 14.09 ? 95  THR B O   1 
ATOM   1764 C CB  . THR B 1 62  ? 29.267 -6.834  14.875 1.00 13.08 ? 95  THR B CB  1 
ATOM   1765 O OG1 . THR B 1 62  ? 30.403 -7.293  14.129 1.00 16.46 ? 95  THR B OG1 1 
ATOM   1766 C CG2 . THR B 1 62  ? 29.175 -7.586  16.209 1.00 14.19 ? 95  THR B CG2 1 
ATOM   1767 N N   . ARG B 1 63  ? 28.382 -6.440  11.708 1.00 16.77 ? 96  ARG B N   1 
ATOM   1768 C CA  . ARG B 1 63  ? 28.220 -5.544  10.562 1.00 16.53 ? 96  ARG B CA  1 
ATOM   1769 C C   . ARG B 1 63  ? 26.746 -5.349  10.220 1.00 15.35 ? 96  ARG B C   1 
ATOM   1770 O O   . ARG B 1 63  ? 26.300 -4.216  9.970  1.00 15.75 ? 96  ARG B O   1 
ATOM   1771 C CB  . ARG B 1 63  ? 28.982 -6.084  9.349  1.00 13.48 ? 96  ARG B CB  1 
ATOM   1772 C CG  . ARG B 1 63  ? 28.773 -5.225  8.101  1.00 22.43 ? 96  ARG B CG  1 
ATOM   1773 C CD  . ARG B 1 63  ? 29.523 -5.748  6.879  1.00 27.39 ? 96  ARG B CD  1 
ATOM   1774 N NE  . ARG B 1 63  ? 30.974 -5.634  7.005  1.00 32.88 ? 96  ARG B NE  1 
ATOM   1775 C CZ  . ARG B 1 63  ? 31.679 -4.556  6.681  1.00 33.90 ? 96  ARG B CZ  1 
ATOM   1776 N NH1 . ARG B 1 63  ? 31.094 -3.439  6.262  1.00 27.27 ? 96  ARG B NH1 1 
ATOM   1777 N NH2 . ARG B 1 63  ? 33.006 -4.598  6.781  1.00 32.92 ? 96  ARG B NH2 1 
ATOM   1778 N N   . VAL B 1 64  ? 25.980 -6.446  10.204 1.00 14.17 ? 97  VAL B N   1 
ATOM   1779 C CA  . VAL B 1 64  ? 24.558 -6.373  9.876  1.00 15.26 ? 97  VAL B CA  1 
ATOM   1780 C C   . VAL B 1 64  ? 23.816 -5.498  10.884 1.00 14.37 ? 97  VAL B C   1 
ATOM   1781 O O   . VAL B 1 64  ? 22.996 -4.647  10.512 1.00 12.88 ? 97  VAL B O   1 
ATOM   1782 C CB  . VAL B 1 64  ? 23.963 -7.795  9.786  1.00 14.30 ? 97  VAL B CB  1 
ATOM   1783 C CG1 . VAL B 1 64  ? 22.457 -7.787  9.981  1.00 17.38 ? 97  VAL B CG1 1 
ATOM   1784 C CG2 . VAL B 1 64  ? 24.312 -8.408  8.428  1.00 15.54 ? 97  VAL B CG2 1 
ATOM   1785 N N   . PHE B 1 65  ? 24.083 -5.685  12.181 1.00 12.85 ? 98  PHE B N   1 
ATOM   1786 C CA  . PHE B 1 65  ? 23.374 -4.853  13.141 1.00 12.87 ? 98  PHE B CA  1 
ATOM   1787 C C   . PHE B 1 65  ? 23.905 -3.429  13.194 1.00 12.78 ? 98  PHE B C   1 
ATOM   1788 O O   . PHE B 1 65  ? 23.151 -2.518  13.544 1.00 12.42 ? 98  PHE B O   1 
ATOM   1789 C CB  . PHE B 1 65  ? 23.370 -5.505  14.534 1.00 12.87 ? 98  PHE B CB  1 
ATOM   1790 C CG  . PHE B 1 65  ? 22.313 -6.582  14.660 1.00 15.09 ? 98  PHE B CG  1 
ATOM   1791 C CD1 . PHE B 1 65  ? 21.025 -6.267  15.079 1.00 14.69 ? 98  PHE B CD1 1 
ATOM   1792 C CD2 . PHE B 1 65  ? 22.581 -7.881  14.255 1.00 15.77 ? 98  PHE B CD2 1 
ATOM   1793 C CE1 . PHE B 1 65  ? 20.035 -7.256  15.161 1.00 15.12 ? 98  PHE B CE1 1 
ATOM   1794 C CE2 . PHE B 1 65  ? 21.606 -8.882  14.340 1.00 16.23 ? 98  PHE B CE2 1 
ATOM   1795 C CZ  . PHE B 1 65  ? 20.328 -8.566  14.799 1.00 14.51 ? 98  PHE B CZ  1 
ATOM   1796 N N   . ASP B 1 66  ? 25.155 -3.184  12.823 1.00 12.45 ? 99  ASP B N   1 
ATOM   1797 C CA  . ASP B 1 66  ? 25.555 -1.789  12.693 1.00 13.05 ? 99  ASP B CA  1 
ATOM   1798 C C   . ASP B 1 66  ? 24.782 -1.107  11.571 1.00 15.71 ? 99  ASP B C   1 
ATOM   1799 O O   . ASP B 1 66  ? 24.335 0.033   11.734 1.00 15.45 ? 99  ASP B O   1 
ATOM   1800 C CB  . ASP B 1 66  ? 27.057 -1.677  12.467 1.00 15.36 ? 99  ASP B CB  1 
ATOM   1801 C CG  . ASP B 1 66  ? 27.539 -0.248  12.558 1.00 18.68 ? 99  ASP B CG  1 
ATOM   1802 O OD1 . ASP B 1 66  ? 27.340 0.381   13.620 1.00 20.68 ? 99  ASP B OD1 1 
ATOM   1803 O OD2 . ASP B 1 66  ? 28.089 0.257   11.562 1.00 23.04 ? 99  ASP B OD2 1 
ATOM   1804 N N   . ASP B 1 67  ? 24.589 -1.794  10.434 1.00 13.52 ? 100 ASP B N   1 
ATOM   1805 C CA  . ASP B 1 67  ? 23.736 -1.242  9.379  1.00 13.77 ? 100 ASP B CA  1 
ATOM   1806 C C   . ASP B 1 67  ? 22.306 -1.020  9.874  1.00 15.83 ? 100 ASP B C   1 
ATOM   1807 O O   . ASP B 1 67  ? 21.693 0.024   9.600  1.00 14.45 ? 100 ASP B O   1 
ATOM   1808 C CB  . ASP B 1 67  ? 23.701 -2.180  8.171  1.00 12.80 ? 100 ASP B CB  1 
ATOM   1809 C CG  . ASP B 1 67  ? 25.067 -2.442  7.576  1.00 21.28 ? 100 ASP B CG  1 
ATOM   1810 O OD1 . ASP B 1 67  ? 25.998 -1.622  7.757  1.00 24.00 ? 100 ASP B OD1 1 
ATOM   1811 O OD2 . ASP B 1 67  ? 25.195 -3.484  6.906  1.00 17.03 ? 100 ASP B OD2 1 
ATOM   1812 N N   . GLN B 1 68  ? 21.756 -2.005  10.592 1.00 12.56 ? 101 GLN B N   1 
ATOM   1813 C CA  . GLN B 1 68  ? 20.404 -1.881  11.140 1.00 12.65 ? 101 GLN B CA  1 
ATOM   1814 C C   . GLN B 1 68  ? 20.289 -0.677  12.071 1.00 16.31 ? 101 GLN B C   1 
ATOM   1815 O O   . GLN B 1 68  ? 19.304 0.073   12.017 1.00 12.99 ? 101 GLN B O   1 
ATOM   1816 C CB  . GLN B 1 68  ? 20.030 -3.165  11.882 1.00 13.23 ? 101 GLN B CB  1 
ATOM   1817 C CG  . GLN B 1 68  ? 18.682 -3.135  12.587 1.00 13.13 ? 101 GLN B CG  1 
ATOM   1818 C CD  . GLN B 1 68  ? 17.529 -3.422  11.647 1.00 16.03 ? 101 GLN B CD  1 
ATOM   1819 O OE1 . GLN B 1 68  ? 17.699 -4.117  10.642 1.00 15.71 ? 101 GLN B OE1 1 
ATOM   1820 N NE2 . GLN B 1 68  ? 16.346 -2.898  11.969 1.00 15.00 ? 101 GLN B NE2 1 
ATOM   1821 N N   . ILE B 1 69  ? 21.282 -0.480  12.937 1.00 12.30 ? 102 ILE B N   1 
ATOM   1822 C CA  . ILE B 1 69  ? 21.229 0.633   13.871 1.00 14.29 ? 102 ILE B CA  1 
ATOM   1823 C C   . ILE B 1 69  ? 21.417 1.964   13.140 1.00 12.01 ? 102 ILE B C   1 
ATOM   1824 O O   . ILE B 1 69  ? 20.729 2.945   13.442 1.00 13.38 ? 102 ILE B O   1 
ATOM   1825 C CB  . ILE B 1 69  ? 22.257 0.417   14.994 1.00 13.69 ? 102 ILE B CB  1 
ATOM   1826 C CG1 . ILE B 1 69  ? 21.819 -0.803  15.844 1.00 16.77 ? 102 ILE B CG1 1 
ATOM   1827 C CG2 . ILE B 1 69  ? 22.400 1.673   15.812 1.00 12.41 ? 102 ILE B CG2 1 
ATOM   1828 C CD1 . ILE B 1 69  ? 22.799 -1.219  16.943 1.00 16.82 ? 102 ILE B CD1 1 
ATOM   1829 N N   . ARG B 1 70  ? 22.337 2.029   12.171 1.00 11.96 ? 103 ARG B N   1 
ATOM   1830 C CA  . ARG B 1 70  ? 22.470 3.255   11.381 1.00 15.07 ? 103 ARG B CA  1 
ATOM   1831 C C   . ARG B 1 70  ? 21.147 3.616   10.733 1.00 14.47 ? 103 ARG B C   1 
ATOM   1832 O O   . ARG B 1 70  ? 20.761 4.788   10.706 1.00 13.40 ? 103 ARG B O   1 
ATOM   1833 C CB  . ARG B 1 70  ? 23.533 3.118   10.280 1.00 12.91 ? 103 ARG B CB  1 
ATOM   1834 C CG  . ARG B 1 70  ? 24.977 3.162   10.728 1.00 22.25 ? 103 ARG B CG  1 
ATOM   1835 C CD  . ARG B 1 70  ? 25.910 3.289   9.519  1.00 19.96 ? 103 ARG B CD  1 
ATOM   1836 N NE  . ARG B 1 70  ? 25.937 2.100   8.667  1.00 16.38 ? 103 ARG B NE  1 
ATOM   1837 C CZ  . ARG B 1 70  ? 25.531 2.071   7.404  1.00 20.50 ? 103 ARG B CZ  1 
ATOM   1838 N NH1 . ARG B 1 70  ? 24.984 3.131   6.828  1.00 17.77 ? 103 ARG B NH1 1 
ATOM   1839 N NH2 . ARG B 1 70  ? 25.700 0.959   6.692  1.00 20.22 ? 103 ARG B NH2 1 
ATOM   1840 N N   . ALA B 1 71  ? 20.450 2.621   10.181 1.00 12.99 ? 104 ALA B N   1 
ATOM   1841 C CA  . ALA B 1 71  ? 19.181 2.893   9.506  1.00 14.83 ? 104 ALA B CA  1 
ATOM   1842 C C   . ALA B 1 71  ? 18.123 3.380   10.495 1.00 14.89 ? 104 ALA B C   1 
ATOM   1843 O O   . ALA B 1 71  ? 17.347 4.308   10.200 1.00 12.92 ? 104 ALA B O   1 
ATOM   1844 C CB  . ALA B 1 71  ? 18.711 1.631   8.780  1.00 14.30 ? 104 ALA B CB  1 
ATOM   1845 N N   . THR B 1 72  ? 18.079 2.760   11.675 1.00 12.31 ? 105 THR B N   1 
ATOM   1846 C CA  . THR B 1 72  ? 17.167 3.207   12.728 1.00 12.41 ? 105 THR B CA  1 
ATOM   1847 C C   . THR B 1 72  ? 17.441 4.661   13.125 1.00 13.01 ? 105 THR B C   1 
ATOM   1848 O O   . THR B 1 72  ? 16.522 5.495   13.229 1.00 12.28 ? 105 THR B O   1 
ATOM   1849 C CB  . THR B 1 72  ? 17.338 2.282   13.933 1.00 12.55 ? 105 THR B CB  1 
ATOM   1850 O OG1 . THR B 1 72  ? 17.253 0.901   13.504 1.00 14.00 ? 105 THR B OG1 1 
ATOM   1851 C CG2 . THR B 1 72  ? 16.308 2.568   14.985 1.00 13.30 ? 105 THR B CG2 1 
ATOM   1852 N N   . GLU B 1 73  ? 18.711 4.979   13.359 1.00 14.26 ? 106 GLU B N   1 
ATOM   1853 C CA  . GLU B 1 73  ? 19.081 6.347   13.711 1.00 13.30 ? 106 GLU B CA  1 
ATOM   1854 C C   . GLU B 1 73  ? 18.734 7.313   12.587 1.00 14.00 ? 106 GLU B C   1 
ATOM   1855 O O   . GLU B 1 73  ? 18.346 8.453   12.845 1.00 12.23 ? 106 GLU B O   1 
ATOM   1856 C CB  . GLU B 1 73  ? 20.574 6.417   14.043 1.00 13.42 ? 106 GLU B CB  1 
ATOM   1857 C CG  . GLU B 1 73  ? 20.943 5.586   15.270 1.00 16.69 ? 106 GLU B CG  1 
ATOM   1858 C CD  . GLU B 1 73  ? 22.447 5.458   15.487 1.00 20.59 ? 106 GLU B CD  1 
ATOM   1859 O OE1 . GLU B 1 73  ? 23.207 5.380   14.489 1.00 17.37 ? 106 GLU B OE1 1 
ATOM   1860 O OE2 . GLU B 1 73  ? 22.864 5.415   16.670 1.00 20.09 ? 106 GLU B OE2 1 
ATOM   1861 N N   . ALA B 1 74  ? 18.888 6.881   11.332 1.00 12.62 ? 107 ALA B N   1 
ATOM   1862 C CA  . ALA B 1 74  ? 18.518 7.745   10.211 1.00 11.83 ? 107 ALA B CA  1 
ATOM   1863 C C   . ALA B 1 74  ? 17.043 8.126   10.265 1.00 11.96 ? 107 ALA B C   1 
ATOM   1864 O O   . ALA B 1 74  ? 16.670 9.281   9.981  1.00 12.77 ? 107 ALA B O   1 
ATOM   1865 C CB  . ALA B 1 74  ? 18.822 7.045   8.898  1.00 11.97 ? 107 ALA B CB  1 
ATOM   1866 N N   . ILE B 1 75  ? 16.192 7.172   10.632 1.00 12.16 ? 108 ILE B N   1 
ATOM   1867 C CA  . ILE B 1 75  ? 14.776 7.503   10.809 1.00 13.01 ? 108 ILE B CA  1 
ATOM   1868 C C   . ILE B 1 75  ? 14.602 8.527   11.922 1.00 12.84 ? 108 ILE B C   1 
ATOM   1869 O O   . ILE B 1 75  ? 13.835 9.500   11.788 1.00 13.90 ? 108 ILE B O   1 
ATOM   1870 C CB  . ILE B 1 75  ? 13.950 6.234   11.083 1.00 13.06 ? 108 ILE B CB  1 
ATOM   1871 C CG1 . ILE B 1 75  ? 13.957 5.333   9.845  1.00 15.09 ? 108 ILE B CG1 1 
ATOM   1872 C CG2 . ILE B 1 75  ? 12.525 6.622   11.470 1.00 15.08 ? 108 ILE B CG2 1 
ATOM   1873 C CD1 . ILE B 1 75  ? 13.528 3.892   10.138 1.00 15.95 ? 108 ILE B CD1 1 
ATOM   1874 N N   . GLU B 1 76  ? 15.297 8.318   13.045 1.00 12.22 ? 109 GLU B N   1 
ATOM   1875 C CA  . GLU B 1 76  ? 15.158 9.251   14.165 1.00 12.25 ? 109 GLU B CA  1 
ATOM   1876 C C   . GLU B 1 76  ? 15.596 10.661  13.774 1.00 16.18 ? 109 GLU B C   1 
ATOM   1877 O O   . GLU B 1 76  ? 14.931 11.652  14.120 1.00 12.13 ? 109 GLU B O   1 
ATOM   1878 C CB  . GLU B 1 76  ? 15.965 8.758   15.363 1.00 12.26 ? 109 GLU B CB  1 
ATOM   1879 C CG  . GLU B 1 76  ? 15.519 7.391   15.856 1.00 13.48 ? 109 GLU B CG  1 
ATOM   1880 C CD  . GLU B 1 76  ? 16.391 6.894   16.984 1.00 18.07 ? 109 GLU B CD  1 
ATOM   1881 O OE1 . GLU B 1 76  ? 16.749 7.712   17.847 1.00 18.71 ? 109 GLU B OE1 1 
ATOM   1882 O OE2 . GLU B 1 76  ? 16.731 5.693   16.995 1.00 25.47 ? 109 GLU B OE2 1 
ATOM   1883 N N   . TYR B 1 77  ? 16.716 10.774  13.056 1.00 11.82 ? 110 TYR B N   1 
ATOM   1884 C CA  . TYR B 1 77  ? 17.171 12.092  12.612 1.00 12.63 ? 110 TYR B CA  1 
ATOM   1885 C C   . TYR B 1 77  ? 16.161 12.751  11.673 1.00 13.54 ? 110 TYR B C   1 
ATOM   1886 O O   . TYR B 1 77  ? 15.942 13.971  11.743 1.00 11.77 ? 110 TYR B O   1 
ATOM   1887 C CB  . TYR B 1 77  ? 18.543 11.985  11.935 1.00 11.60 ? 110 TYR B CB  1 
ATOM   1888 C CG  . TYR B 1 77  ? 19.683 11.987  12.930 1.00 15.14 ? 110 TYR B CG  1 
ATOM   1889 C CD1 . TYR B 1 77  ? 20.275 13.175  13.332 1.00 13.41 ? 110 TYR B CD1 1 
ATOM   1890 C CD2 . TYR B 1 77  ? 20.146 10.803  13.492 1.00 15.55 ? 110 TYR B CD2 1 
ATOM   1891 C CE1 . TYR B 1 77  ? 21.308 13.187  14.257 1.00 16.69 ? 110 TYR B CE1 1 
ATOM   1892 C CE2 . TYR B 1 77  ? 21.177 10.802  14.413 1.00 17.97 ? 110 TYR B CE2 1 
ATOM   1893 C CZ  . TYR B 1 77  ? 21.755 11.997  14.793 1.00 16.60 ? 110 TYR B CZ  1 
ATOM   1894 O OH  . TYR B 1 77  ? 22.778 12.001  15.709 1.00 14.04 ? 110 TYR B OH  1 
ATOM   1895 N N   . SER B 1 78  ? 15.548 11.969  10.774 1.00 11.90 ? 111 SER B N   1 
ATOM   1896 C CA  . SER B 1 78  ? 14.539 12.540  9.884  1.00 12.06 ? 111 SER B CA  1 
ATOM   1897 C C   . SER B 1 78  ? 13.347 13.085  10.669 1.00 12.54 ? 111 SER B C   1 
ATOM   1898 O O   . SER B 1 78  ? 12.822 14.174  10.363 1.00 12.70 ? 111 SER B O   1 
ATOM   1899 C CB  . SER B 1 78  ? 14.082 11.487  8.869  1.00 13.41 ? 111 SER B CB  1 
ATOM   1900 O OG  . SER B 1 78  ? 13.131 12.031  7.961  1.00 16.79 ? 111 SER B OG  1 
ATOM   1901 N N   . ARG B 1 79  ? 12.884 12.328  11.672 1.00 12.38 ? 112 ARG B N   1 
ATOM   1902 C CA  . ARG B 1 79  ? 11.790 12.830  12.506 1.00 12.88 ? 112 ARG B CA  1 
ATOM   1903 C C   . ARG B 1 79  ? 12.198 14.116  13.210 1.00 12.50 ? 112 ARG B C   1 
ATOM   1904 O O   . ARG B 1 79  ? 11.396 15.052  13.329 1.00 12.66 ? 112 ARG B O   1 
ATOM   1905 C CB  . ARG B 1 79  ? 11.372 11.792  13.548 1.00 13.12 ? 112 ARG B CB  1 
ATOM   1906 C CG  . ARG B 1 79  ? 10.828 10.478  13.008 1.00 17.40 ? 112 ARG B CG  1 
ATOM   1907 C CD  . ARG B 1 79  ? 9.723  10.657  11.986 1.00 19.04 ? 112 ARG B CD  1 
ATOM   1908 N NE  . ARG B 1 79  ? 9.085  9.374   11.699 1.00 16.18 ? 112 ARG B NE  1 
ATOM   1909 C CZ  . ARG B 1 79  ? 8.610  9.024   10.515 1.00 21.48 ? 112 ARG B CZ  1 
ATOM   1910 N NH1 . ARG B 1 79  ? 8.795  9.786   9.445  1.00 20.31 ? 112 ARG B NH1 1 
ATOM   1911 N NH2 . ARG B 1 79  ? 7.937  7.884   10.400 1.00 20.03 ? 112 ARG B NH2 1 
ATOM   1912 N N   . PHE B 1 80  ? 13.427 14.159  13.732 1.00 12.26 ? 113 PHE B N   1 
ATOM   1913 C CA  . PHE B 1 80  ? 13.877 15.369  14.415 1.00 12.21 ? 113 PHE B CA  1 
ATOM   1914 C C   . PHE B 1 80  ? 13.882 16.561  13.465 1.00 15.33 ? 113 PHE B C   1 
ATOM   1915 O O   . PHE B 1 80  ? 13.582 17.687  13.872 1.00 12.50 ? 113 PHE B O   1 
ATOM   1916 C CB  . PHE B 1 80  ? 15.265 15.164  15.028 1.00 12.08 ? 113 PHE B CB  1 
ATOM   1917 C CG  . PHE B 1 80  ? 15.230 14.611  16.445 1.00 14.66 ? 113 PHE B CG  1 
ATOM   1918 C CD1 . PHE B 1 80  ? 14.337 13.607  16.791 1.00 13.76 ? 113 PHE B CD1 1 
ATOM   1919 C CD2 . PHE B 1 80  ? 16.093 15.101  17.419 1.00 12.39 ? 113 PHE B CD2 1 
ATOM   1920 C CE1 . PHE B 1 80  ? 14.296 13.093  18.088 1.00 12.85 ? 113 PHE B CE1 1 
ATOM   1921 C CE2 . PHE B 1 80  ? 16.076 14.570  18.717 1.00 12.69 ? 113 PHE B CE2 1 
ATOM   1922 C CZ  . PHE B 1 80  ? 15.164 13.578  19.047 1.00 12.92 ? 113 PHE B CZ  1 
ATOM   1923 N N   . SER B 1 81  ? 14.244 16.339  12.201 1.00 12.55 ? 114 SER B N   1 
ATOM   1924 C CA  . SER B 1 81  ? 14.172 17.433  11.236 1.00 12.94 ? 114 SER B CA  1 
ATOM   1925 C C   . SER B 1 81  ? 12.734 17.929  11.085 1.00 13.58 ? 114 SER B C   1 
ATOM   1926 O O   . SER B 1 81  ? 12.462 19.144  11.154 1.00 12.82 ? 114 SER B O   1 
ATOM   1927 C CB  . SER B 1 81  ? 14.738 16.969  9.893  1.00 15.35 ? 114 SER B CB  1 
ATOM   1928 O OG  . SER B 1 81  ? 14.517 17.931  8.903  1.00 12.27 ? 114 SER B OG  1 
ATOM   1929 N N   . ASP B 1 82  ? 11.790 16.991  10.918 1.00 12.37 ? 115 ASP B N   1 
ATOM   1930 C CA  . ASP B 1 82  ? 10.379 17.377  10.822 1.00 13.15 ? 115 ASP B CA  1 
ATOM   1931 C C   . ASP B 1 82  ? 9.932  18.159  12.054 1.00 13.32 ? 115 ASP B C   1 
ATOM   1932 O O   . ASP B 1 82  ? 9.182  19.141  11.949 1.00 14.20 ? 115 ASP B O   1 
ATOM   1933 C CB  . ASP B 1 82  ? 9.485  16.150  10.669 1.00 13.29 ? 115 ASP B CB  1 
ATOM   1934 C CG  . ASP B 1 82  ? 9.676  15.431  9.347  1.00 18.57 ? 115 ASP B CG  1 
ATOM   1935 O OD1 . ASP B 1 82  ? 10.195 16.038  8.381  1.00 17.61 ? 115 ASP B OD1 1 
ATOM   1936 O OD2 . ASP B 1 82  ? 9.280  14.245  9.283  1.00 19.44 ? 115 ASP B OD2 1 
ATOM   1937 N N   . TRP B 1 83  ? 10.341 17.709  13.231 1.00 13.09 ? 116 TRP B N   1 
ATOM   1938 C CA  . TRP B 1 83  ? 9.828  18.309  14.450 1.00 13.75 ? 116 TRP B CA  1 
ATOM   1939 C C   . TRP B 1 83  ? 10.538 19.616  14.765 1.00 13.74 ? 116 TRP B C   1 
ATOM   1940 O O   . TRP B 1 83  ? 9.964  20.457  15.461 1.00 14.12 ? 116 TRP B O   1 
ATOM   1941 C CB  . TRP B 1 83  ? 9.937  17.317  15.622 1.00 14.09 ? 116 TRP B CB  1 
ATOM   1942 C CG  . TRP B 1 83  ? 9.171  16.030  15.384 1.00 15.23 ? 116 TRP B CG  1 
ATOM   1943 C CD1 . TRP B 1 83  ? 8.071  15.857  14.575 1.00 15.67 ? 116 TRP B CD1 1 
ATOM   1944 C CD2 . TRP B 1 83  ? 9.472  14.738  15.929 1.00 14.00 ? 116 TRP B CD2 1 
ATOM   1945 N NE1 . TRP B 1 83  ? 7.665  14.534  14.602 1.00 16.50 ? 116 TRP B NE1 1 
ATOM   1946 C CE2 . TRP B 1 83  ? 8.510  13.829  15.423 1.00 15.80 ? 116 TRP B CE2 1 
ATOM   1947 C CE3 . TRP B 1 83  ? 10.457 14.262  16.803 1.00 14.61 ? 116 TRP B CE3 1 
ATOM   1948 C CZ2 . TRP B 1 83  ? 8.512  12.470  15.758 1.00 17.19 ? 116 TRP B CZ2 1 
ATOM   1949 C CZ3 . TRP B 1 83  ? 10.455 12.910  17.141 1.00 13.67 ? 116 TRP B CZ3 1 
ATOM   1950 C CH2 . TRP B 1 83  ? 9.486  12.030  16.618 1.00 15.93 ? 116 TRP B CH2 1 
ATOM   1951 N N   . LYS B 1 84  ? 11.769 19.804  14.267 1.00 12.93 ? 117 LYS B N   1 
ATOM   1952 C CA  . LYS B 1 84  ? 12.391 21.121  14.346 1.00 14.08 ? 117 LYS B CA  1 
ATOM   1953 C C   . LYS B 1 84  ? 11.608 22.118  13.510 1.00 15.15 ? 117 LYS B C   1 
ATOM   1954 O O   . LYS B 1 84  ? 11.420 23.273  13.915 1.00 16.61 ? 117 LYS B O   1 
ATOM   1955 C CB  . LYS B 1 84  ? 13.854 21.076  13.882 1.00 12.23 ? 117 LYS B CB  1 
ATOM   1956 C CG  . LYS B 1 84  ? 14.838 20.465  14.904 1.00 13.65 ? 117 LYS B CG  1 
ATOM   1957 C CD  . LYS B 1 84  ? 15.166 21.462  16.025 1.00 16.47 ? 117 LYS B CD  1 
ATOM   1958 C CE  . LYS B 1 84  ? 16.233 20.913  16.990 1.00 14.76 ? 117 LYS B CE  1 
ATOM   1959 N NZ  . LYS B 1 84  ? 16.672 21.981  17.943 1.00 17.39 ? 117 LYS B NZ  1 
ATOM   1960 N N   . LEU B 1 85  ? 11.133 21.681  12.342 1.00 12.53 ? 118 LEU B N   1 
ATOM   1961 C CA  . LEU B 1 85  ? 10.331 22.576  11.523 1.00 15.67 ? 118 LEU B CA  1 
ATOM   1962 C C   . LEU B 1 85  ? 8.985  22.868  12.180 1.00 18.48 ? 118 LEU B C   1 
ATOM   1963 O O   . LEU B 1 85  ? 8.478  23.987  12.060 1.00 14.21 ? 118 LEU B O   1 
ATOM   1964 C CB  . LEU B 1 85  ? 10.150 21.985  10.115 1.00 13.88 ? 118 LEU B CB  1 
ATOM   1965 C CG  . LEU B 1 85  ? 11.454 21.848  9.310  1.00 15.84 ? 118 LEU B CG  1 
ATOM   1966 C CD1 . LEU B 1 85  ? 11.308 21.022  8.034  1.00 18.96 ? 118 LEU B CD1 1 
ATOM   1967 C CD2 . LEU B 1 85  ? 12.031 23.225  8.960  1.00 14.68 ? 118 LEU B CD2 1 
ATOM   1968 N N   . ASN B 1 86  ? 8.412  21.910  12.911 1.00 14.64 ? 119 ASN B N   1 
ATOM   1969 C CA  . ASN B 1 86  ? 7.093  22.095  13.520 1.00 17.53 ? 119 ASN B CA  1 
ATOM   1970 C C   . ASN B 1 86  ? 7.010  21.303  14.818 1.00 20.71 ? 119 ASN B C   1 
ATOM   1971 O O   . ASN B 1 86  ? 6.560  20.146  14.832 1.00 17.23 ? 119 ASN B O   1 
ATOM   1972 C CB  . ASN B 1 86  ? 5.976  21.684  12.559 1.00 17.47 ? 119 ASN B CB  1 
ATOM   1973 C CG  . ASN B 1 86  ? 4.589  21.858  13.156 1.00 28.29 ? 119 ASN B CG  1 
ATOM   1974 O OD1 . ASN B 1 86  ? 4.425  22.456  14.224 1.00 28.40 ? 119 ASN B OD1 1 
ATOM   1975 N ND2 . ASN B 1 86  ? 3.577  21.336  12.460 1.00 31.78 ? 119 ASN B ND2 1 
ATOM   1976 N N   . PRO B 1 87  ? 7.434  21.896  15.939 1.00 18.58 ? 120 PRO B N   1 
ATOM   1977 C CA  . PRO B 1 87  ? 7.457  21.123  17.197 1.00 14.28 ? 120 PRO B CA  1 
ATOM   1978 C C   . PRO B 1 87  ? 6.096  20.629  17.650 1.00 20.84 ? 120 PRO B C   1 
ATOM   1979 O O   . PRO B 1 87  ? 6.029  19.600  18.334 1.00 21.05 ? 120 PRO B O   1 
ATOM   1980 C CB  . PRO B 1 87  ? 8.077  22.101  18.204 1.00 17.98 ? 120 PRO B CB  1 
ATOM   1981 C CG  . PRO B 1 87  ? 8.952  23.002  17.342 1.00 19.11 ? 120 PRO B CG  1 
ATOM   1982 C CD  . PRO B 1 87  ? 8.160  23.175  16.059 1.00 19.96 ? 120 PRO B CD  1 
ATOM   1983 N N   . ALA B 1 88  ? 5.005  21.313  17.285 1.00 17.97 ? 121 ALA B N   1 
ATOM   1984 C CA  . ALA B 1 88  ? 3.689  20.832  17.691 1.00 19.53 ? 121 ALA B CA  1 
ATOM   1985 C C   . ALA B 1 88  ? 3.336  19.505  17.034 1.00 19.92 ? 121 ALA B C   1 
ATOM   1986 O O   . ALA B 1 88  ? 2.426  18.816  17.508 1.00 23.18 ? 121 ALA B O   1 
ATOM   1987 C CB  . ALA B 1 88  ? 2.624  21.878  17.374 1.00 23.68 ? 121 ALA B CB  1 
ATOM   1988 N N   . SER B 1 89  ? 4.036  19.116  15.966 1.00 16.48 ? 122 SER B N   1 
ATOM   1989 C CA  . SER B 1 89  ? 3.728  17.845  15.325 1.00 21.16 ? 122 SER B CA  1 
ATOM   1990 C C   . SER B 1 89  ? 4.424  16.655  15.986 1.00 19.77 ? 122 SER B C   1 
ATOM   1991 O O   . SER B 1 89  ? 4.133  15.514  15.624 1.00 19.39 ? 122 SER B O   1 
ATOM   1992 C CB  . SER B 1 89  ? 4.069  17.899  13.828 1.00 21.80 ? 122 SER B CB  1 
ATOM   1993 O OG  . SER B 1 89  ? 5.459  17.991  13.598 1.00 21.71 ? 122 SER B OG  1 
ATOM   1994 N N   . ALA B 1 90  ? 5.312  16.875  16.945 1.00 18.11 ? 123 ALA B N   1 
ATOM   1995 C CA  . ALA B 1 90  ? 5.959  15.746  17.610 1.00 16.86 ? 123 ALA B CA  1 
ATOM   1996 C C   . ALA B 1 90  ? 4.916  14.978  18.416 1.00 20.46 ? 123 ALA B C   1 
ATOM   1997 O O   . ALA B 1 90  ? 4.213  15.580  19.231 1.00 25.57 ? 123 ALA B O   1 
ATOM   1998 C CB  . ALA B 1 90  ? 7.096  16.219  18.521 1.00 22.60 ? 123 ALA B CB  1 
ATOM   1999 N N   . PRO B 1 91  ? 4.789  13.670  18.222 1.00 24.45 ? 124 PRO B N   1 
ATOM   2000 C CA  . PRO B 1 91  ? 3.680  12.928  18.815 1.00 28.63 ? 124 PRO B CA  1 
ATOM   2001 C C   . PRO B 1 91  ? 3.946  12.623  20.277 1.00 24.40 ? 124 PRO B C   1 
ATOM   2002 O O   . PRO B 1 91  ? 5.092  12.714  20.743 1.00 22.44 ? 124 PRO B O   1 
ATOM   2003 C CB  . PRO B 1 91  ? 3.635  11.637  17.982 1.00 23.85 ? 124 PRO B CB  1 
ATOM   2004 C CG  . PRO B 1 91  ? 4.948  11.609  17.186 1.00 28.05 ? 124 PRO B CG  1 
ATOM   2005 C CD  . PRO B 1 91  ? 5.780  12.762  17.633 1.00 27.00 ? 124 PRO B CD  1 
ATOM   2006 N N   . PRO B 1 92  ? 2.917  12.257  21.036 1.00 28.06 ? 125 PRO B N   1 
ATOM   2007 C CA  . PRO B 1 92  ? 3.148  11.890  22.437 1.00 29.15 ? 125 PRO B CA  1 
ATOM   2008 C C   . PRO B 1 92  ? 4.068  10.681  22.538 1.00 27.37 ? 125 PRO B C   1 
ATOM   2009 O O   . PRO B 1 92  ? 4.012  9.753   21.724 1.00 24.93 ? 125 PRO B O   1 
ATOM   2010 C CB  . PRO B 1 92  ? 1.741  11.592  22.969 1.00 32.21 ? 125 PRO B CB  1 
ATOM   2011 C CG  . PRO B 1 92  ? 0.904  11.346  21.752 1.00 41.24 ? 125 PRO B CG  1 
ATOM   2012 C CD  . PRO B 1 92  ? 1.495  12.169  20.658 1.00 28.28 ? 125 PRO B CD  1 
ATOM   2013 N N   . GLU B 1 93  ? 4.923  10.717  23.528 1.00 23.75 ? 126 GLU B N   1 
ATOM   2014 C CA  . GLU B 1 93  ? 5.974  9.734   23.711 1.00 26.30 ? 126 GLU B CA  1 
ATOM   2015 C C   . GLU B 1 93  ? 5.498  8.608   24.619 1.00 20.12 ? 126 GLU B C   1 
ATOM   2016 O O   . GLU B 1 93  ? 4.530  8.765   25.365 1.00 22.98 ? 126 GLU B O   1 
ATOM   2017 C CB  . GLU B 1 93  ? 7.211  10.413  24.299 1.00 25.22 ? 126 GLU B CB  1 
ATOM   2018 C CG  . GLU B 1 93  ? 7.128  10.716  25.803 1.00 25.61 ? 126 GLU B CG  1 
ATOM   2019 C CD  . GLU B 1 93  ? 6.293  11.928  26.144 1.00 29.34 ? 126 GLU B CD  1 
ATOM   2020 O OE1 . GLU B 1 93  ? 5.621  12.488  25.249 1.00 29.05 ? 126 GLU B OE1 1 
ATOM   2021 O OE2 . GLU B 1 93  ? 6.313  12.333  27.330 1.00 33.13 ? 126 GLU B OE2 1 
ATOM   2022 N N   . PRO B 1 94  ? 6.138  7.442   24.556 1.00 22.50 ? 127 PRO B N   1 
ATOM   2023 C CA  . PRO B 1 94  ? 5.829  6.372   25.507 1.00 24.99 ? 127 PRO B CA  1 
ATOM   2024 C C   . PRO B 1 94  ? 6.253  6.769   26.909 1.00 25.98 ? 127 PRO B C   1 
ATOM   2025 O O   . PRO B 1 94  ? 7.090  7.669   27.076 1.00 29.18 ? 127 PRO B O   1 
ATOM   2026 C CB  . PRO B 1 94  ? 6.658  5.186   24.986 1.00 22.33 ? 127 PRO B CB  1 
ATOM   2027 C CG  . PRO B 1 94  ? 7.773  5.820   24.202 1.00 22.51 ? 127 PRO B CG  1 
ATOM   2028 C CD  . PRO B 1 94  ? 7.158  7.038   23.571 1.00 21.46 ? 127 PRO B CD  1 
ATOM   2029 N N   . PRO B 1 95  ? 5.675  6.150   27.944 1.00 25.59 ? 128 PRO B N   1 
ATOM   2030 C CA  . PRO B 1 95  ? 6.089  6.485   29.324 1.00 25.87 ? 128 PRO B CA  1 
ATOM   2031 C C   . PRO B 1 95  ? 7.553  6.194   29.599 1.00 28.93 ? 128 PRO B C   1 
ATOM   2032 O O   . PRO B 1 95  ? 8.164  6.863   30.443 1.00 27.25 ? 128 PRO B O   1 
ATOM   2033 C CB  . PRO B 1 95  ? 5.167  5.612   30.191 1.00 25.92 ? 128 PRO B CB  1 
ATOM   2034 C CG  . PRO B 1 95  ? 4.794  4.453   29.293 1.00 26.23 ? 128 PRO B CG  1 
ATOM   2035 C CD  . PRO B 1 95  ? 4.702  5.040   27.904 1.00 29.16 ? 128 PRO B CD  1 
ATOM   2036 N N   . ASP B 1 96  ? 8.127  5.206   28.918 1.00 25.98 ? 129 ASP B N   1 
ATOM   2037 C CA  . ASP B 1 96  ? 9.540  4.870   29.031 1.00 26.07 ? 129 ASP B CA  1 
ATOM   2038 C C   . ASP B 1 96  ? 9.911  4.039   27.807 1.00 30.50 ? 129 ASP B C   1 
ATOM   2039 O O   . ASP B 1 96  ? 9.091  3.826   26.908 1.00 28.06 ? 129 ASP B O   1 
ATOM   2040 C CB  . ASP B 1 96  ? 9.833  4.128   30.339 1.00 30.02 ? 129 ASP B CB  1 
ATOM   2041 C CG  . ASP B 1 96  ? 8.916  2.950   30.547 1.00 37.66 ? 129 ASP B CG  1 
ATOM   2042 O OD1 . ASP B 1 96  ? 8.888  2.062   29.668 1.00 35.98 ? 129 ASP B OD1 1 
ATOM   2043 O OD2 . ASP B 1 96  ? 8.213  2.916   31.579 1.00 38.35 ? 129 ASP B OD2 1 
ATOM   2044 N N   . LEU B 1 97  ? 11.153 3.558   27.778 1.00 24.06 ? 130 LEU B N   1 
ATOM   2045 C CA  . LEU B 1 97  ? 11.635 2.769   26.653 1.00 23.99 ? 130 LEU B CA  1 
ATOM   2046 C C   . LEU B 1 97  ? 11.695 1.272   26.952 1.00 26.11 ? 130 LEU B C   1 
ATOM   2047 O O   . LEU B 1 97  ? 12.291 0.520   26.171 1.00 24.65 ? 130 LEU B O   1 
ATOM   2048 C CB  . LEU B 1 97  ? 13.005 3.284   26.195 1.00 26.65 ? 130 LEU B CB  1 
ATOM   2049 C CG  . LEU B 1 97  ? 12.989 4.720   25.635 1.00 25.89 ? 130 LEU B CG  1 
ATOM   2050 C CD1 . LEU B 1 97  ? 14.383 5.201   25.218 1.00 24.92 ? 130 LEU B CD1 1 
ATOM   2051 C CD2 . LEU B 1 97  ? 12.004 4.857   24.470 1.00 26.38 ? 130 LEU B CD2 1 
ATOM   2052 N N   . SER B 1 98  ? 11.074 0.821   28.047 1.00 31.24 ? 131 SER B N   1 
ATOM   2053 C CA  . SER B 1 98  ? 11.099 -0.603  28.386 1.00 27.73 ? 131 SER B CA  1 
ATOM   2054 C C   . SER B 1 98  ? 10.403 -1.449  27.318 1.00 27.03 ? 131 SER B C   1 
ATOM   2055 O O   . SER B 1 98  ? 10.924 -2.491  26.901 1.00 27.86 ? 131 SER B O   1 
ATOM   2056 C CB  . SER B 1 98  ? 10.463 -0.825  29.764 1.00 31.35 ? 131 SER B CB  1 
ATOM   2057 O OG  . SER B 1 98  ? 9.089  -0.481  29.760 1.00 38.76 ? 131 SER B OG  1 
ATOM   2058 N N   . ALA B 1 99  ? 9.222  -1.019  26.862 1.00 27.60 ? 132 ALA B N   1 
ATOM   2059 C CA  . ALA B 1 99  ? 8.528  -1.763  25.809 1.00 23.35 ? 132 ALA B CA  1 
ATOM   2060 C C   . ALA B 1 99  ? 9.358  -1.825  24.527 1.00 26.24 ? 132 ALA B C   1 
ATOM   2061 O O   . ALA B 1 99  ? 9.435  -2.875  23.871 1.00 26.96 ? 132 ALA B O   1 
ATOM   2062 C CB  . ALA B 1 99  ? 7.166  -1.129  25.530 1.00 26.11 ? 132 ALA B CB  1 
ATOM   2063 N N   . SER B 1 100 ? 9.979  -0.704  24.150 1.00 21.40 ? 133 SER B N   1 
ATOM   2064 C CA  . SER B 1 100 ? 10.829 -0.678  22.962 1.00 19.55 ? 133 SER B CA  1 
ATOM   2065 C C   . SER B 1 100 ? 12.046 -1.581  23.128 1.00 25.52 ? 133 SER B C   1 
ATOM   2066 O O   . SER B 1 100 ? 12.444 -2.280  22.187 1.00 19.21 ? 133 SER B O   1 
ATOM   2067 C CB  . SER B 1 100 ? 11.273 0.757   22.666 1.00 25.39 ? 133 SER B CB  1 
ATOM   2068 O OG  . SER B 1 100 ? 10.168 1.611   22.425 1.00 26.67 ? 133 SER B OG  1 
ATOM   2069 N N   A ARG B 1 101 ? 12.673 -1.551  24.301 0.32 24.00 ? 134 ARG B N   1 
ATOM   2070 N N   B ARG B 1 101 ? 12.674 -1.545  24.301 0.68 23.94 ? 134 ARG B N   1 
ATOM   2071 C CA  A ARG B 1 101 ? 13.827 -2.463  24.550 0.32 25.91 ? 134 ARG B CA  1 
ATOM   2072 C CA  B ARG B 1 101 ? 13.825 -2.460  24.543 0.68 25.94 ? 134 ARG B CA  1 
ATOM   2073 C C   A ARG B 1 101 ? 13.387 -3.931  24.443 0.32 23.97 ? 134 ARG B C   1 
ATOM   2074 C C   B ARG B 1 101 ? 13.366 -3.920  24.409 0.68 23.95 ? 134 ARG B C   1 
ATOM   2075 O O   A ARG B 1 101 ? 14.136 -4.718  23.865 0.32 23.34 ? 134 ARG B O   1 
ATOM   2076 O O   B ARG B 1 101 ? 14.158 -4.727  23.903 0.68 23.32 ? 134 ARG B O   1 
ATOM   2077 C CB  A ARG B 1 101 ? 14.479 -2.219  25.909 0.32 27.21 ? 134 ARG B CB  1 
ATOM   2078 C CB  B ARG B 1 101 ? 14.493 -2.174  25.889 0.68 27.20 ? 134 ARG B CB  1 
ATOM   2079 C CG  A ARG B 1 101 ? 15.719 -1.342  25.870 0.32 31.15 ? 134 ARG B CG  1 
ATOM   2080 C CG  B ARG B 1 101 ? 15.126 -0.793  25.970 0.68 29.97 ? 134 ARG B CG  1 
ATOM   2081 C CD  A ARG B 1 101 ? 15.341 0.119   25.783 0.32 31.06 ? 134 ARG B CD  1 
ATOM   2082 C CD  B ARG B 1 101 ? 15.976 -0.595  27.208 0.68 33.13 ? 134 ARG B CD  1 
ATOM   2083 N NE  A ARG B 1 101 ? 15.698 0.940   26.932 0.32 36.14 ? 134 ARG B NE  1 
ATOM   2084 N NE  B ARG B 1 101 ? 16.662 0.687   27.167 0.68 38.56 ? 134 ARG B NE  1 
ATOM   2085 C CZ  A ARG B 1 101 ? 15.229 0.780   28.166 0.32 35.16 ? 134 ARG B CZ  1 
ATOM   2086 C CZ  B ARG B 1 101 ? 16.248 1.779   27.795 0.68 36.93 ? 134 ARG B CZ  1 
ATOM   2087 N NH1 A ARG B 1 101 ? 14.390 -0.202  28.446 0.32 29.85 ? 134 ARG B NH1 1 
ATOM   2088 N NH1 B ARG B 1 101 ? 15.144 1.744   28.521 0.68 36.40 ? 134 ARG B NH1 1 
ATOM   2089 N NH2 A ARG B 1 101 ? 15.610 1.604   29.122 0.32 36.10 ? 134 ARG B NH2 1 
ATOM   2090 N NH2 B ARG B 1 101 ? 16.938 2.900   27.695 0.68 34.92 ? 134 ARG B NH2 1 
ATOM   2091 N N   . SER B 1 102 ? 12.242 -4.274  25.039 1.00 25.52 ? 135 SER B N   1 
ATOM   2092 C CA  . SER B 1 102 ? 11.795 -5.664  24.972 1.00 26.58 ? 135 SER B CA  1 
ATOM   2093 C C   . SER B 1 102 ? 11.523 -6.079  23.532 1.00 24.78 ? 135 SER B C   1 
ATOM   2094 O O   . SER B 1 102 ? 11.893 -7.187  23.113 1.00 24.21 ? 135 SER B O   1 
ATOM   2095 C CB  A SER B 1 102 ? 10.550 -5.859  25.833 0.41 26.84 ? 135 SER B CB  1 
ATOM   2096 C CB  B SER B 1 102 ? 10.545 -5.864  25.831 0.59 26.85 ? 135 SER B CB  1 
ATOM   2097 O OG  A SER B 1 102 ? 9.554  -4.919  25.483 0.41 30.49 ? 135 SER B OG  1 
ATOM   2098 O OG  B SER B 1 102 ? 10.795 -5.550  27.190 0.59 29.32 ? 135 SER B OG  1 
ATOM   2099 N N   . ALA B 1 103 ? 10.875 -5.198  22.764 1.00 20.94 ? 136 ALA B N   1 
ATOM   2100 C CA  . ALA B 1 103 ? 10.662 -5.458  21.347 1.00 21.49 ? 136 ALA B CA  1 
ATOM   2101 C C   . ALA B 1 103 ? 11.985 -5.671  20.629 1.00 20.49 ? 136 ALA B C   1 
ATOM   2102 O O   . ALA B 1 103 ? 12.125 -6.601  19.826 1.00 19.29 ? 136 ALA B O   1 
ATOM   2103 C CB  . ALA B 1 103 ? 9.886  -4.300  20.716 1.00 25.31 ? 136 ALA B CB  1 
ATOM   2104 N N   . ILE B 1 104 ? 12.970 -4.809  20.902 1.00 17.85 ? 137 ILE B N   1 
ATOM   2105 C CA  . ILE B 1 104 ? 14.270 -4.934  20.253 1.00 17.08 ? 137 ILE B CA  1 
ATOM   2106 C C   . ILE B 1 104 ? 14.937 -6.248  20.642 1.00 18.93 ? 137 ILE B C   1 
ATOM   2107 O O   . ILE B 1 104 ? 15.502 -6.937  19.796 1.00 20.66 ? 137 ILE B O   1 
ATOM   2108 C CB  . ILE B 1 104 ? 15.158 -3.724  20.586 1.00 21.02 ? 137 ILE B CB  1 
ATOM   2109 C CG1 . ILE B 1 104 ? 14.662 -2.484  19.836 1.00 21.58 ? 137 ILE B CG1 1 
ATOM   2110 C CG2 . ILE B 1 104 ? 16.616 -4.016  20.251 1.00 20.06 ? 137 ILE B CG2 1 
ATOM   2111 C CD1 . ILE B 1 104 ? 15.218 -1.189  20.384 1.00 25.44 ? 137 ILE B CD1 1 
ATOM   2112 N N   . ASP B 1 105 ? 14.883 -6.622  21.918 1.00 18.96 ? 138 ASP B N   1 
ATOM   2113 C CA  . ASP B 1 105 ? 15.478 -7.900  22.319 1.00 21.87 ? 138 ASP B CA  1 
ATOM   2114 C C   . ASP B 1 105 ? 14.823 -9.077  21.591 1.00 19.77 ? 138 ASP B C   1 
ATOM   2115 O O   . ASP B 1 105 ? 15.518 -9.980  21.087 1.00 19.43 ? 138 ASP B O   1 
ATOM   2116 C CB  . ASP B 1 105 ? 15.362 -8.065  23.835 1.00 24.63 ? 138 ASP B CB  1 
ATOM   2117 C CG  . ASP B 1 105 ? 16.080 -9.291  24.337 1.00 29.11 ? 138 ASP B CG  1 
ATOM   2118 O OD1 . ASP B 1 105 ? 17.326 -9.327  24.246 1.00 35.21 ? 138 ASP B OD1 1 
ATOM   2119 O OD2 . ASP B 1 105 ? 15.397 -10.227 24.810 1.00 37.59 ? 138 ASP B OD2 1 
ATOM   2120 N N   A SER B 1 106 ? 13.487 -9.079  21.508 0.55 18.35 ? 139 SER B N   1 
ATOM   2121 N N   B SER B 1 106 ? 13.488 -9.076  21.508 0.45 18.37 ? 139 SER B N   1 
ATOM   2122 C CA  A SER B 1 106 ? 12.800 -10.170 20.818 0.55 19.01 ? 139 SER B CA  1 
ATOM   2123 C CA  B SER B 1 106 ? 12.794 -10.166 20.825 0.45 19.01 ? 139 SER B CA  1 
ATOM   2124 C C   A SER B 1 106 ? 13.153 -10.199 19.336 0.55 17.49 ? 139 SER B C   1 
ATOM   2125 C C   B SER B 1 106 ? 13.142 -10.199 19.340 0.45 17.49 ? 139 SER B C   1 
ATOM   2126 O O   A SER B 1 106 ? 13.411 -11.270 18.765 0.55 16.35 ? 139 SER B O   1 
ATOM   2127 O O   B SER B 1 106 ? 13.395 -11.272 18.770 0.45 16.36 ? 139 SER B O   1 
ATOM   2128 C CB  A SER B 1 106 ? 11.290 -10.040 20.997 0.55 21.86 ? 139 SER B CB  1 
ATOM   2129 C CB  B SER B 1 106 ? 11.285 -10.025 21.021 0.45 21.85 ? 139 SER B CB  1 
ATOM   2130 O OG  A SER B 1 106 ? 10.912 -10.345 22.323 0.55 22.75 ? 139 SER B OG  1 
ATOM   2131 O OG  B SER B 1 106 ? 10.590 -11.112 20.436 0.45 18.70 ? 139 SER B OG  1 
ATOM   2132 N N   . LEU B 1 107 ? 13.174 -9.031  18.697 1.00 15.06 ? 140 LEU B N   1 
ATOM   2133 C CA  . LEU B 1 107 ? 13.483 -8.971  17.270 1.00 13.81 ? 140 LEU B CA  1 
ATOM   2134 C C   . LEU B 1 107 ? 14.946 -9.313  16.995 1.00 18.18 ? 140 LEU B C   1 
ATOM   2135 O O   . LEU B 1 107 ? 15.254 -9.945  15.981 1.00 15.99 ? 140 LEU B O   1 
ATOM   2136 C CB  . LEU B 1 107 ? 13.114 -7.588  16.727 1.00 14.09 ? 140 LEU B CB  1 
ATOM   2137 C CG  . LEU B 1 107 ? 11.594 -7.366  16.708 1.00 18.86 ? 140 LEU B CG  1 
ATOM   2138 C CD1 . LEU B 1 107 ? 11.223 -5.896  16.557 1.00 17.20 ? 140 LEU B CD1 1 
ATOM   2139 C CD2 . LEU B 1 107 ? 10.920 -8.218  15.627 1.00 19.81 ? 140 LEU B CD2 1 
ATOM   2140 N N   . ASN B 1 108 ? 15.862 -8.914  17.889 1.00 15.33 ? 141 ASN B N   1 
ATOM   2141 C CA  . ASN B 1 108 ? 17.252 -9.358  17.808 1.00 15.75 ? 141 ASN B CA  1 
ATOM   2142 C C   . ASN B 1 108 ? 17.322 -10.876 17.739 1.00 17.35 ? 141 ASN B C   1 
ATOM   2143 O O   . ASN B 1 108 ? 17.980 -11.446 16.859 1.00 16.14 ? 141 ASN B O   1 
ATOM   2144 C CB  . ASN B 1 108 ? 18.051 -8.893  19.037 1.00 15.18 ? 141 ASN B CB  1 
ATOM   2145 C CG  . ASN B 1 108 ? 18.414 -7.417  19.012 1.00 19.94 ? 141 ASN B CG  1 
ATOM   2146 O OD1 . ASN B 1 108 ? 18.273 -6.732  17.997 1.00 17.88 ? 141 ASN B OD1 1 
ATOM   2147 N ND2 . ASN B 1 108 ? 18.913 -6.924  20.147 1.00 17.90 ? 141 ASN B ND2 1 
ATOM   2148 N N   . ASN B 1 109 ? 16.670 -11.544 18.691 1.00 14.96 ? 142 ASN B N   1 
ATOM   2149 C CA  . ASN B 1 109 ? 16.737 -13.007 18.731 1.00 18.08 ? 142 ASN B CA  1 
ATOM   2150 C C   . ASN B 1 109 ? 16.078 -13.629 17.503 1.00 16.84 ? 142 ASN B C   1 
ATOM   2151 O O   . ASN B 1 109 ? 16.564 -14.639 16.965 1.00 17.40 ? 142 ASN B O   1 
ATOM   2152 C CB  . ASN B 1 109 ? 16.088 -13.520 20.009 1.00 18.13 ? 142 ASN B CB  1 
ATOM   2153 C CG  . ASN B 1 109 ? 16.933 -13.242 21.227 1.00 24.76 ? 142 ASN B CG  1 
ATOM   2154 O OD1 . ASN B 1 109 ? 18.157 -13.197 21.139 1.00 28.61 ? 142 ASN B OD1 1 
ATOM   2155 N ND2 . ASN B 1 109 ? 16.287 -13.036 22.367 1.00 30.72 ? 142 ASN B ND2 1 
ATOM   2156 N N   . ARG B 1 110 ? 14.968 -13.042 17.050 1.00 14.23 ? 143 ARG B N   1 
ATOM   2157 C CA  . ARG B 1 110 ? 14.326 -13.530 15.834 1.00 15.41 ? 143 ARG B CA  1 
ATOM   2158 C C   . ARG B 1 110 ? 15.261 -13.419 14.633 1.00 15.42 ? 143 ARG B C   1 
ATOM   2159 O O   . ARG B 1 110 ? 15.386 -14.361 13.839 1.00 15.14 ? 143 ARG B O   1 
ATOM   2160 C CB  . ARG B 1 110 ? 13.037 -12.752 15.576 1.00 16.83 ? 143 ARG B CB  1 
ATOM   2161 C CG  . ARG B 1 110 ? 11.996 -13.547 14.822 1.00 30.28 ? 143 ARG B CG  1 
ATOM   2162 C CD  . ARG B 1 110 ? 10.924 -12.658 14.224 1.00 30.60 ? 143 ARG B CD  1 
ATOM   2163 N NE  . ARG B 1 110 ? 10.025 -12.094 15.223 1.00 36.61 ? 143 ARG B NE  1 
ATOM   2164 C CZ  . ARG B 1 110 ? 9.131  -11.146 14.966 1.00 42.77 ? 143 ARG B CZ  1 
ATOM   2165 N NH1 . ARG B 1 110 ? 8.996  -10.630 13.749 1.00 37.90 ? 143 ARG B NH1 1 
ATOM   2166 N NH2 . ARG B 1 110 ? 8.361  -10.697 15.952 1.00 33.88 ? 143 ARG B NH2 1 
ATOM   2167 N N   . MET B 1 111 ? 15.934 -12.277 14.496 1.00 13.80 ? 144 MET B N   1 
ATOM   2168 C CA  . MET B 1 111 ? 16.827 -12.058 13.361 1.00 13.57 ? 144 MET B CA  1 
ATOM   2169 C C   . MET B 1 111 ? 18.033 -12.983 13.430 1.00 13.87 ? 144 MET B C   1 
ATOM   2170 O O   . MET B 1 111 ? 18.476 -13.511 12.406 1.00 16.42 ? 144 MET B O   1 
ATOM   2171 C CB  . MET B 1 111 ? 17.274 -10.592 13.314 1.00 12.40 ? 144 MET B CB  1 
ATOM   2172 C CG  . MET B 1 111 ? 16.183 -9.636  12.869 1.00 13.67 ? 144 MET B CG  1 
ATOM   2173 S SD  . MET B 1 111 ? 16.642 -7.884  13.098 1.00 15.49 ? 144 MET B SD  1 
ATOM   2174 C CE  . MET B 1 111 ? 17.899 -7.726  11.838 1.00 16.32 ? 144 MET B CE  1 
ATOM   2175 N N   . LEU B 1 112 ? 18.582 -13.182 14.625 1.00 12.42 ? 145 LEU B N   1 
ATOM   2176 C CA  . LEU B 1 112 ? 19.714 -14.091 14.760 1.00 12.80 ? 145 LEU B CA  1 
ATOM   2177 C C   . LEU B 1 112 ? 19.339 -15.506 14.333 1.00 13.12 ? 145 LEU B C   1 
ATOM   2178 O O   . LEU B 1 112 ? 20.089 -16.165 13.598 1.00 13.83 ? 145 LEU B O   1 
ATOM   2179 C CB  . LEU B 1 112 ? 20.218 -14.085 16.203 1.00 13.77 ? 145 LEU B CB  1 
ATOM   2180 C CG  . LEU B 1 112 ? 20.968 -12.829 16.627 1.00 15.06 ? 145 LEU B CG  1 
ATOM   2181 C CD1 . LEU B 1 112 ? 21.362 -12.955 18.083 1.00 19.25 ? 145 LEU B CD1 1 
ATOM   2182 C CD2 . LEU B 1 112 ? 22.195 -12.578 15.763 1.00 19.80 ? 145 LEU B CD2 1 
ATOM   2183 N N   . SER B 1 113 ? 18.191 -16.004 14.808 1.00 13.54 ? 146 SER B N   1 
ATOM   2184 C CA  . SER B 1 113 ? 17.802 -17.362 14.427 1.00 14.31 ? 146 SER B CA  1 
ATOM   2185 C C   . SER B 1 113 ? 17.507 -17.467 12.936 1.00 14.14 ? 146 SER B C   1 
ATOM   2186 O O   . SER B 1 113 ? 17.779 -18.511 12.326 1.00 14.74 ? 146 SER B O   1 
ATOM   2187 C CB  . SER B 1 113 ? 16.602 -17.814 15.251 1.00 15.10 ? 146 SER B CB  1 
ATOM   2188 O OG  . SER B 1 113 ? 16.993 -17.954 16.600 1.00 18.41 ? 146 SER B OG  1 
ATOM   2189 N N   . GLN B 1 114 ? 16.963 -16.404 12.329 1.00 13.54 ? 147 GLN B N   1 
ATOM   2190 C CA  . GLN B 1 114 ? 16.796 -16.395 10.874 1.00 13.84 ? 147 GLN B CA  1 
ATOM   2191 C C   . GLN B 1 114 ? 18.140 -16.431 10.148 1.00 15.73 ? 147 GLN B C   1 
ATOM   2192 O O   . GLN B 1 114 ? 18.279 -17.097 9.115  1.00 15.60 ? 147 GLN B O   1 
ATOM   2193 C CB  . GLN B 1 114 ? 16.007 -15.154 10.441 1.00 13.84 ? 147 GLN B CB  1 
ATOM   2194 C CG  . GLN B 1 114 ? 14.540 -15.189 10.810 1.00 19.21 ? 147 GLN B CG  1 
ATOM   2195 C CD  . GLN B 1 114 ? 13.819 -16.361 10.189 1.00 23.59 ? 147 GLN B CD  1 
ATOM   2196 O OE1 . GLN B 1 114 ? 14.008 -16.666 9.009  1.00 20.64 ? 147 GLN B OE1 1 
ATOM   2197 N NE2 . GLN B 1 114 ? 12.995 -17.036 10.985 1.00 22.56 ? 147 GLN B NE2 1 
ATOM   2198 N N   . ILE B 1 115 ? 19.127 -15.678 10.641 1.00 14.56 ? 148 ILE B N   1 
ATOM   2199 C CA  . ILE B 1 115 ? 20.441 -15.649 9.996  1.00 14.20 ? 148 ILE B CA  1 
ATOM   2200 C C   . ILE B 1 115 ? 21.106 -17.022 10.081 1.00 15.65 ? 148 ILE B C   1 
ATOM   2201 O O   . ILE B 1 115 ? 21.638 -17.538 9.093  1.00 13.91 ? 148 ILE B O   1 
ATOM   2202 C CB  . ILE B 1 115 ? 21.319 -14.549 10.622 1.00 12.68 ? 148 ILE B CB  1 
ATOM   2203 C CG1 . ILE B 1 115 ? 20.829 -13.159 10.201 1.00 14.22 ? 148 ILE B CG1 1 
ATOM   2204 C CG2 . ILE B 1 115 ? 22.783 -14.731 10.250 1.00 12.87 ? 148 ILE B CG2 1 
ATOM   2205 C CD1 . ILE B 1 115 ? 21.358 -12.004 11.125 1.00 14.29 ? 148 ILE B CD1 1 
ATOM   2206 N N   . TRP B 1 116 ? 21.076 -17.638 11.264 1.00 13.90 ? 149 TRP B N   1 
ATOM   2207 C CA  . TRP B 1 116 ? 21.599 -18.994 11.388 1.00 15.87 ? 149 TRP B CA  1 
ATOM   2208 C C   . TRP B 1 116 ? 20.865 -19.956 10.451 1.00 15.41 ? 149 TRP B C   1 
ATOM   2209 O O   . TRP B 1 116 ? 21.490 -20.657 9.644  1.00 17.88 ? 149 TRP B O   1 
ATOM   2210 C CB  . TRP B 1 116 ? 21.499 -19.463 12.845 1.00 15.36 ? 149 TRP B CB  1 
ATOM   2211 C CG  . TRP B 1 116 ? 21.787 -20.920 12.988 1.00 17.42 ? 149 TRP B CG  1 
ATOM   2212 C CD1 . TRP B 1 116 ? 23.015 -21.509 13.051 1.00 21.81 ? 149 TRP B CD1 1 
ATOM   2213 C CD2 . TRP B 1 116 ? 20.827 -21.981 13.058 1.00 17.50 ? 149 TRP B CD2 1 
ATOM   2214 N NE1 . TRP B 1 116 ? 22.879 -22.873 13.159 1.00 24.61 ? 149 TRP B NE1 1 
ATOM   2215 C CE2 . TRP B 1 116 ? 21.545 -23.187 13.162 1.00 20.61 ? 149 TRP B CE2 1 
ATOM   2216 C CE3 . TRP B 1 116 ? 19.428 -22.024 13.036 1.00 17.61 ? 149 TRP B CE3 1 
ATOM   2217 C CZ2 . TRP B 1 116 ? 20.916 -24.426 13.253 1.00 23.56 ? 149 TRP B CZ2 1 
ATOM   2218 C CZ3 . TRP B 1 116 ? 18.803 -23.263 13.121 1.00 23.14 ? 149 TRP B CZ3 1 
ATOM   2219 C CH2 . TRP B 1 116 ? 19.548 -24.440 13.232 1.00 20.25 ? 149 TRP B CH2 1 
ATOM   2220 N N   . SER B 1 117 ? 19.531 -19.972 10.504 1.00 15.73 ? 150 SER B N   1 
ATOM   2221 C CA  . SER B 1 117 ? 18.814 -21.005 9.760  1.00 16.47 ? 150 SER B CA  1 
ATOM   2222 C C   . SER B 1 117 ? 18.920 -20.807 8.256  1.00 16.83 ? 150 SER B C   1 
ATOM   2223 O O   . SER B 1 117 ? 18.807 -21.785 7.511  1.00 17.44 ? 150 SER B O   1 
ATOM   2224 C CB  . SER B 1 117 ? 17.343 -21.071 10.193 1.00 18.99 ? 150 SER B CB  1 
ATOM   2225 O OG  . SER B 1 117 ? 16.617 -19.920 9.806  1.00 22.67 ? 150 SER B OG  1 
ATOM   2226 N N   . HIS B 1 118 ? 19.189 -19.578 7.810  1.00 15.46 ? 151 HIS B N   1 
ATOM   2227 C CA  . HIS B 1 118 ? 19.295 -19.298 6.349  1.00 19.43 ? 151 HIS B CA  1 
ATOM   2228 C C   . HIS B 1 118 ? 20.755 -19.101 5.916  1.00 16.74 ? 151 HIS B C   1 
ATOM   2229 O O   . HIS B 1 118 ? 20.968 -18.562 4.842  1.00 16.66 ? 151 HIS B O   1 
ATOM   2230 C CB  . HIS B 1 118 ? 18.416 -18.098 5.967  1.00 15.11 ? 151 HIS B CB  1 
ATOM   2231 C CG  . HIS B 1 118 ? 16.961 -18.324 6.168  1.00 16.66 ? 151 HIS B CG  1 
ATOM   2232 N ND1 . HIS B 1 118 ? 16.143 -18.792 5.165  1.00 20.65 ? 151 HIS B ND1 1 
ATOM   2233 C CD2 . HIS B 1 118 ? 16.174 -18.142 7.245  1.00 15.70 ? 151 HIS B CD2 1 
ATOM   2234 C CE1 . HIS B 1 118 ? 14.915 -18.895 5.622  1.00 18.89 ? 151 HIS B CE1 1 
ATOM   2235 N NE2 . HIS B 1 118 ? 14.907 -18.494 6.888  1.00 16.40 ? 151 HIS B NE2 1 
ATOM   2236 N N   . TRP B 1 119 ? 21.709 -19.564 6.714  1.00 16.72 ? 152 TRP B N   1 
ATOM   2237 C CA  . TRP B 1 119 ? 23.108 -19.280 6.406  1.00 17.09 ? 152 TRP B CA  1 
ATOM   2238 C C   . TRP B 1 119 ? 23.498 -19.821 5.034  1.00 21.06 ? 152 TRP B C   1 
ATOM   2239 O O   . TRP B 1 119 ? 24.252 -19.171 4.295  1.00 19.36 ? 152 TRP B O   1 
ATOM   2240 C CB  . TRP B 1 119 ? 24.042 -19.865 7.468  1.00 18.46 ? 152 TRP B CB  1 
ATOM   2241 C CG  . TRP B 1 119 ? 25.434 -19.378 7.239  1.00 22.20 ? 152 TRP B CG  1 
ATOM   2242 C CD1 . TRP B 1 119 ? 26.461 -20.049 6.627  1.00 25.70 ? 152 TRP B CD1 1 
ATOM   2243 C CD2 . TRP B 1 119 ? 25.937 -18.076 7.555  1.00 24.63 ? 152 TRP B CD2 1 
ATOM   2244 N NE1 . TRP B 1 119 ? 27.580 -19.248 6.566  1.00 21.10 ? 152 TRP B NE1 1 
ATOM   2245 C CE2 . TRP B 1 119 ? 27.283 -18.031 7.128  1.00 24.98 ? 152 TRP B CE2 1 
ATOM   2246 C CE3 . TRP B 1 119 ? 25.382 -16.946 8.172  1.00 21.92 ? 152 TRP B CE3 1 
ATOM   2247 C CZ2 . TRP B 1 119 ? 28.084 -16.902 7.303  1.00 25.53 ? 152 TRP B CZ2 1 
ATOM   2248 C CZ3 . TRP B 1 119 ? 26.181 -15.819 8.341  1.00 19.89 ? 152 TRP B CZ3 1 
ATOM   2249 C CH2 . TRP B 1 119 ? 27.517 -15.810 7.912  1.00 22.98 ? 152 TRP B CH2 1 
ATOM   2250 N N   . SER B 1 120 ? 22.997 -21.007 4.677  1.00 20.45 ? 153 SER B N   1 
ATOM   2251 C CA  . SER B 1 120 ? 23.324 -21.579 3.371  1.00 21.40 ? 153 SER B CA  1 
ATOM   2252 C C   . SER B 1 120 ? 22.851 -20.677 2.243  1.00 24.78 ? 153 SER B C   1 
ATOM   2253 O O   . SER B 1 120 ? 23.515 -20.564 1.208  1.00 24.25 ? 153 SER B O   1 
ATOM   2254 C CB  . SER B 1 120 ? 22.703 -22.965 3.217  1.00 22.01 ? 153 SER B CB  1 
ATOM   2255 O OG  . SER B 1 120 ? 23.426 -23.923 3.964  1.00 33.35 ? 153 SER B OG  1 
ATOM   2256 N N   . LEU B 1 121 ? 21.683 -20.065 2.406  1.00 19.48 ? 154 LEU B N   1 
ATOM   2257 C CA  . LEU B 1 121 ? 21.190 -19.144 1.391  1.00 20.08 ? 154 LEU B CA  1 
ATOM   2258 C C   . LEU B 1 121 ? 21.942 -17.821 1.431  1.00 20.03 ? 154 LEU B C   1 
ATOM   2259 O O   . LEU B 1 121 ? 22.319 -17.287 0.379  1.00 20.88 ? 154 LEU B O   1 
ATOM   2260 C CB  . LEU B 1 121 ? 19.689 -18.918 1.578  1.00 24.33 ? 154 LEU B CB  1 
ATOM   2261 C CG  . LEU B 1 121 ? 19.027 -17.831 0.725  1.00 23.01 ? 154 LEU B CG  1 
ATOM   2262 C CD1 . LEU B 1 121 ? 19.368 -18.005 -0.753 1.00 27.45 ? 154 LEU B CD1 1 
ATOM   2263 C CD2 . LEU B 1 121 ? 17.532 -17.903 0.938  1.00 24.60 ? 154 LEU B CD2 1 
ATOM   2264 N N   . LEU B 1 122 ? 22.170 -17.279 2.635  1.00 18.97 ? 155 LEU B N   1 
ATOM   2265 C CA  . LEU B 1 122 ? 22.840 -15.983 2.744  1.00 20.19 ? 155 LEU B CA  1 
ATOM   2266 C C   . LEU B 1 122 ? 24.234 -16.020 2.143  1.00 22.36 ? 155 LEU B C   1 
ATOM   2267 O O   . LEU B 1 122 ? 24.731 -14.993 1.670  1.00 22.53 ? 155 LEU B O   1 
ATOM   2268 C CB  . LEU B 1 122 ? 22.932 -15.540 4.210  1.00 16.99 ? 155 LEU B CB  1 
ATOM   2269 C CG  . LEU B 1 122 ? 21.585 -15.157 4.827  1.00 17.21 ? 155 LEU B CG  1 
ATOM   2270 C CD1 . LEU B 1 122 ? 21.725 -15.013 6.340  1.00 18.49 ? 155 LEU B CD1 1 
ATOM   2271 C CD2 . LEU B 1 122 ? 21.043 -13.886 4.229  1.00 16.29 ? 155 LEU B CD2 1 
ATOM   2272 N N   . SER B 1 123 ? 24.880 -17.183 2.156  1.00 18.73 ? 156 SER B N   1 
ATOM   2273 C CA  . SER B 1 123 ? 26.208 -17.339 1.582  1.00 19.12 ? 156 SER B CA  1 
ATOM   2274 C C   . SER B 1 123 ? 26.161 -17.876 0.158  1.00 23.78 ? 156 SER B C   1 
ATOM   2275 O O   . SER B 1 123 ? 27.210 -18.192 -0.406 1.00 24.85 ? 156 SER B O   1 
ATOM   2276 C CB  . SER B 1 123 ? 27.068 -18.248 2.464  1.00 22.77 ? 156 SER B CB  1 
ATOM   2277 O OG  . SER B 1 123 ? 26.490 -19.533 2.620  1.00 23.88 ? 156 SER B OG  1 
ATOM   2278 N N   . ALA B 1 124 ? 24.975 -17.977 -0.436 1.00 22.60 ? 157 ALA B N   1 
ATOM   2279 C CA  . ALA B 1 124 ? 24.788 -18.553 -1.762 1.00 22.68 ? 157 ALA B CA  1 
ATOM   2280 C C   . ALA B 1 124 ? 24.641 -17.465 -2.816 1.00 22.64 ? 157 ALA B C   1 
ATOM   2281 O O   . ALA B 1 124 ? 24.279 -16.324 -2.507 1.00 24.68 ? 157 ALA B O   1 
ATOM   2282 C CB  . ALA B 1 124 ? 23.552 -19.464 -1.780 1.00 27.80 ? 157 ALA B CB  1 
ATOM   2283 N N   . PRO B 1 125 ? 24.911 -17.796 -4.088 1.00 27.44 ? 158 PRO B N   1 
ATOM   2284 C CA  . PRO B 1 125 ? 24.778 -16.781 -5.149 1.00 27.79 ? 158 PRO B CA  1 
ATOM   2285 C C   . PRO B 1 125 ? 23.395 -16.153 -5.226 1.00 18.70 ? 158 PRO B C   1 
ATOM   2286 O O   . PRO B 1 125 ? 23.280 -14.949 -5.461 1.00 25.27 ? 158 PRO B O   1 
ATOM   2287 C CB  . PRO B 1 125 ? 25.113 -17.570 -6.426 1.00 29.76 ? 158 PRO B CB  1 
ATOM   2288 C CG  . PRO B 1 125 ? 25.965 -18.711 -5.963 1.00 35.19 ? 158 PRO B CG  1 
ATOM   2289 C CD  . PRO B 1 125 ? 25.430 -19.081 -4.605 1.00 29.34 ? 158 PRO B CD  1 
ATOM   2290 N N   . SER B 1 126 ? 22.341 -16.926 -4.996 1.00 22.04 ? 159 SER B N   1 
ATOM   2291 C CA  . SER B 1 126 ? 20.989 -16.431 -5.205 1.00 22.02 ? 159 SER B CA  1 
ATOM   2292 C C   . SER B 1 126 ? 20.472 -15.588 -4.050 1.00 15.49 ? 159 SER B C   1 
ATOM   2293 O O   . SER B 1 126 ? 19.327 -15.124 -4.111 1.00 19.61 ? 159 SER B O   1 
ATOM   2294 C CB  . SER B 1 126 ? 20.052 -17.610 -5.458 1.00 22.45 ? 159 SER B CB  1 
ATOM   2295 O OG  . SER B 1 126 ? 20.073 -18.480 -4.349 1.00 26.29 ? 159 SER B OG  1 
ATOM   2296 N N   . CYS B 1 127 ? 21.294 -15.342 -3.027 1.00 16.61 ? 160 CYS B N   1 
ATOM   2297 C CA  . CYS B 1 127 ? 20.874 -14.497 -1.911 1.00 16.82 ? 160 CYS B CA  1 
ATOM   2298 C C   . CYS B 1 127 ? 20.292 -13.170 -2.397 1.00 19.53 ? 160 CYS B C   1 
ATOM   2299 O O   . CYS B 1 127 ? 19.208 -12.756 -1.964 1.00 17.68 ? 160 CYS B O   1 
ATOM   2300 C CB  . CYS B 1 127 ? 22.063 -14.250 -0.974 1.00 19.25 ? 160 CYS B CB  1 
ATOM   2301 S SG  . CYS B 1 127 ? 21.694 -13.154 0.427  1.00 18.54 ? 160 CYS B SG  1 
ATOM   2302 N N   . ALA B 1 128 ? 20.981 -12.507 -3.329 1.00 14.72 ? 161 ALA B N   1 
ATOM   2303 C CA  . ALA B 1 128 ? 20.503 -11.212 -3.796 1.00 19.93 ? 161 ALA B CA  1 
ATOM   2304 C C   . ALA B 1 128 ? 19.083 -11.315 -4.350 1.00 18.42 ? 161 ALA B C   1 
ATOM   2305 O O   . ALA B 1 128 ? 18.213 -10.495 -4.007 1.00 17.87 ? 161 ALA B O   1 
ATOM   2306 C CB  . ALA B 1 128 ? 21.470 -10.638 -4.834 1.00 18.33 ? 161 ALA B CB  1 
ATOM   2307 N N   . ALA B 1 129 ? 18.805 -12.356 -5.144 1.00 15.51 ? 162 ALA B N   1 
ATOM   2308 C CA  . ALA B 1 129 ? 17.457 -12.503 -5.683 1.00 16.87 ? 162 ALA B CA  1 
ATOM   2309 C C   . ALA B 1 129 ? 16.454 -12.668 -4.558 1.00 17.48 ? 162 ALA B C   1 
ATOM   2310 O O   . ALA B 1 129 ? 15.434 -11.965 -4.511 1.00 18.65 ? 162 ALA B O   1 
ATOM   2311 C CB  . ALA B 1 129 ? 17.377 -13.684 -6.656 1.00 17.75 ? 162 ALA B CB  1 
ATOM   2312 N N   . GLN B 1 130 ? 16.773 -13.535 -3.584 1.00 15.97 ? 163 GLN B N   1 
ATOM   2313 C CA  . GLN B 1 130 ? 15.853 -13.731 -2.469 1.00 17.36 ? 163 GLN B CA  1 
ATOM   2314 C C   . GLN B 1 130 ? 15.691 -12.435 -1.687 1.00 18.89 ? 163 GLN B C   1 
ATOM   2315 O O   . GLN B 1 130 ? 14.563 -12.024 -1.363 1.00 19.51 ? 163 GLN B O   1 
ATOM   2316 C CB  . GLN B 1 130 ? 16.347 -14.857 -1.556 1.00 15.06 ? 163 GLN B CB  1 
ATOM   2317 C CG  . GLN B 1 130 ? 16.347 -16.229 -2.224 1.00 19.03 ? 163 GLN B CG  1 
ATOM   2318 C CD  . GLN B 1 130 ? 14.956 -16.810 -2.363 1.00 24.83 ? 163 GLN B CD  1 
ATOM   2319 O OE1 . GLN B 1 130 ? 14.091 -16.578 -1.528 1.00 26.92 ? 163 GLN B OE1 1 
ATOM   2320 N NE2 . GLN B 1 130 ? 14.737 -17.571 -3.417 1.00 32.40 ? 163 GLN B NE2 1 
ATOM   2321 N N   . LEU B 1 131 ? 16.802 -11.722 -1.472 1.00 15.99 ? 164 LEU B N   1 
ATOM   2322 C CA  . LEU B 1 131 ? 16.706 -10.490 -0.707 1.00 15.47 ? 164 LEU B CA  1 
ATOM   2323 C C   . LEU B 1 131 ? 15.804 -9.500  -1.433 1.00 21.31 ? 164 LEU B C   1 
ATOM   2324 O O   . LEU B 1 131 ? 14.884 -8.924  -0.829 1.00 19.04 ? 164 LEU B O   1 
ATOM   2325 C CB  . LEU B 1 131 ? 18.105 -9.916  -0.450 1.00 14.31 ? 164 LEU B CB  1 
ATOM   2326 C CG  . LEU B 1 131 ? 18.131 -8.552  0.255  1.00 15.89 ? 164 LEU B CG  1 
ATOM   2327 C CD1 . LEU B 1 131 ? 17.277 -8.586  1.534  1.00 17.40 ? 164 LEU B CD1 1 
ATOM   2328 C CD2 . LEU B 1 131 ? 19.558 -8.128  0.580  1.00 22.92 ? 164 LEU B CD2 1 
ATOM   2329 N N   . ASP B 1 132 ? 15.972 -9.387  -2.759 1.00 17.06 ? 165 ASP B N   1 
ATOM   2330 C CA  . ASP B 1 132 ? 15.195 -8.393  -3.489 1.00 19.40 ? 165 ASP B CA  1 
ATOM   2331 C C   . ASP B 1 132 ? 13.711 -8.702  -3.377 1.00 20.31 ? 165 ASP B C   1 
ATOM   2332 O O   . ASP B 1 132 ? 12.902 -7.819  -3.047 1.00 21.34 ? 165 ASP B O   1 
ATOM   2333 C CB  . ASP B 1 132 ? 15.643 -8.347  -4.952 1.00 16.08 ? 165 ASP B CB  1 
ATOM   2334 C CG  . ASP B 1 132 ? 15.074 -7.150  -5.704 1.00 30.75 ? 165 ASP B CG  1 
ATOM   2335 O OD1 . ASP B 1 132 ? 15.410 -5.998  -5.348 1.00 30.12 ? 165 ASP B OD1 1 
ATOM   2336 O OD2 . ASP B 1 132 ? 14.296 -7.363  -6.655 1.00 31.38 ? 165 ASP B OD2 1 
ATOM   2337 N N   . ARG B 1 133 ? 13.351 -9.981  -3.536 1.00 20.00 ? 166 ARG B N   1 
ATOM   2338 C CA  . ARG B 1 133 ? 11.939 -10.330 -3.483 1.00 18.56 ? 166 ARG B CA  1 
ATOM   2339 C C   . ARG B 1 133 ? 11.394 -10.043 -2.097 1.00 19.90 ? 166 ARG B C   1 
ATOM   2340 O O   . ARG B 1 133 ? 10.341 -9.403  -1.949 1.00 20.43 ? 166 ARG B O   1 
ATOM   2341 C CB  . ARG B 1 133 ? 11.748 -11.798 -3.871 1.00 20.55 ? 166 ARG B CB  1 
ATOM   2342 C CG  . ARG B 1 133 ? 10.356 -12.326 -3.630 1.00 24.85 ? 166 ARG B CG  1 
ATOM   2343 C CD  . ARG B 1 133 ? 9.319  -11.615 -4.481 1.00 37.12 ? 166 ARG B CD  1 
ATOM   2344 N NE  . ARG B 1 133 ? 7.983  -12.123 -4.194 1.00 45.56 ? 166 ARG B NE  1 
ATOM   2345 C CZ  . ARG B 1 133 ? 7.424  -13.158 -4.806 1.00 50.66 ? 166 ARG B CZ  1 
ATOM   2346 N NH1 . ARG B 1 133 ? 8.041  -13.796 -5.790 1.00 50.58 ? 166 ARG B NH1 1 
ATOM   2347 N NH2 . ARG B 1 133 ? 6.216  -13.562 -4.422 1.00 54.06 ? 166 ARG B NH2 1 
ATOM   2348 N N   . ALA B 1 134 ? 12.172 -10.398 -1.068 1.00 19.90 ? 167 ALA B N   1 
ATOM   2349 C CA  . ALA B 1 134 ? 11.733 -10.160 0.300  1.00 20.09 ? 167 ALA B CA  1 
ATOM   2350 C C   . ALA B 1 134 ? 11.491 -8.676  0.528  1.00 18.31 ? 167 ALA B C   1 
ATOM   2351 O O   . ALA B 1 134 ? 10.420 -8.274  1.013  1.00 22.02 ? 167 ALA B O   1 
ATOM   2352 C CB  . ALA B 1 134 ? 12.773 -10.696 1.284  1.00 18.93 ? 167 ALA B CB  1 
ATOM   2353 N N   . LYS B 1 135 ? 12.431 -7.834  0.081  1.00 20.52 ? 168 LYS B N   1 
ATOM   2354 C CA  . LYS B 1 135 ? 12.269 -6.408  0.338  1.00 16.64 ? 168 LYS B CA  1 
ATOM   2355 C C   . LYS B 1 135 ? 10.993 -5.912  -0.320 1.00 20.57 ? 168 LYS B C   1 
ATOM   2356 O O   . LYS B 1 135 ? 10.143 -5.286  0.329  1.00 19.51 ? 168 LYS B O   1 
ATOM   2357 C CB  . LYS B 1 135 ? 13.488 -5.629  -0.157 1.00 13.41 ? 168 LYS B CB  1 
ATOM   2358 C CG  . LYS B 1 135 ? 14.714 -5.805  0.720  1.00 17.07 ? 168 LYS B CG  1 
ATOM   2359 C CD  . LYS B 1 135 ? 15.963 -5.306  0.019  1.00 28.31 ? 168 LYS B CD  1 
ATOM   2360 C CE  . LYS B 1 135 ? 15.810 -3.866  -0.443 1.00 28.69 ? 168 LYS B CE  1 
ATOM   2361 N NZ  . LYS B 1 135 ? 17.072 -3.366  -1.064 1.00 30.93 ? 168 LYS B NZ  1 
ATOM   2362 N N   . ARG B 1 136 ? 10.797 -6.276  -1.574 1.00 19.35 ? 169 ARG B N   1 
ATOM   2363 C CA  . ARG B 1 136 ? 9.608  -5.790  -2.315 1.00 23.07 ? 169 ARG B CA  1 
ATOM   2364 C C   . ARG B 1 136 ? 8.337  -6.217  -1.566 1.00 24.36 ? 169 ARG B C   1 
ATOM   2365 O O   . ARG B 1 136 ? 7.459  -5.376  -1.385 1.00 21.71 ? 169 ARG B O   1 
ATOM   2366 C CB  . ARG B 1 136 ? 9.658  -6.262  -3.773 1.00 22.57 ? 169 ARG B CB  1 
ATOM   2367 C CG  . ARG B 1 136 ? 11.051 -6.236  -4.380 1.00 38.18 ? 169 ARG B CG  1 
ATOM   2368 C CD  . ARG B 1 136 ? 11.299 -5.298  -5.539 1.00 39.72 ? 169 ARG B CD  1 
ATOM   2369 N NE  . ARG B 1 136 ? 10.300 -5.407  -6.586 1.00 36.31 ? 169 ARG B NE  1 
ATOM   2370 C CZ  . ARG B 1 136 ? 10.532 -5.910  -7.788 1.00 39.47 ? 169 ARG B CZ  1 
ATOM   2371 N NH1 . ARG B 1 136 ? 11.732 -6.369  -8.091 1.00 36.22 ? 169 ARG B NH1 1 
ATOM   2372 N NH2 . ARG B 1 136 ? 9.561  -5.953  -8.683 1.00 35.72 ? 169 ARG B NH2 1 
ATOM   2373 N N   . ASP B 1 137 ? 8.285  -7.476  -1.125 1.00 24.49 ? 170 ASP B N   1 
ATOM   2374 C CA  . ASP B 1 137 ? 7.067  -7.949  -0.484 1.00 23.75 ? 170 ASP B CA  1 
ATOM   2375 C C   . ASP B 1 137 ? 6.861  -7.246  0.849  1.00 20.06 ? 170 ASP B C   1 
ATOM   2376 O O   . ASP B 1 137 ? 5.743  -6.809  1.164  1.00 18.84 ? 170 ASP B O   1 
ATOM   2377 C CB  . ASP B 1 137 ? 7.115  -9.465  -0.310 1.00 28.76 ? 170 ASP B CB  1 
ATOM   2378 C CG  . ASP B 1 137 ? 6.988  -10.203 -1.633 1.00 37.66 ? 170 ASP B CG  1 
ATOM   2379 O OD1 . ASP B 1 137 ? 6.722  -9.544  -2.664 1.00 34.86 ? 170 ASP B OD1 1 
ATOM   2380 O OD2 . ASP B 1 137 ? 7.158  -11.440 -1.643 1.00 37.66 ? 170 ASP B OD2 1 
ATOM   2381 N N   . ILE B 1 138 ? 7.939  -7.066  1.614  1.00 17.25 ? 171 ILE B N   1 
ATOM   2382 C CA  . ILE B 1 138 ? 7.771  -6.441  2.918  1.00 19.71 ? 171 ILE B CA  1 
ATOM   2383 C C   . ILE B 1 138 ? 7.369  -4.989  2.738  1.00 21.06 ? 171 ILE B C   1 
ATOM   2384 O O   . ILE B 1 138 ? 6.489  -4.479  3.453  1.00 22.02 ? 171 ILE B O   1 
ATOM   2385 C CB  . ILE B 1 138 ? 9.048  -6.593  3.766  1.00 20.39 ? 171 ILE B CB  1 
ATOM   2386 C CG1 . ILE B 1 138 ? 9.310  -8.067  4.063  1.00 17.30 ? 171 ILE B CG1 1 
ATOM   2387 C CG2 . ILE B 1 138 ? 8.924  -5.833  5.066  1.00 19.87 ? 171 ILE B CG2 1 
ATOM   2388 C CD1 . ILE B 1 138 ? 8.065  -8.844  4.465  1.00 20.32 ? 171 ILE B CD1 1 
ATOM   2389 N N   . VAL B 1 139 ? 7.933  -4.326  1.721  1.00 16.42 ? 172 VAL B N   1 
ATOM   2390 C CA  . VAL B 1 139 ? 7.586  -2.924  1.518  1.00 16.68 ? 172 VAL B CA  1 
ATOM   2391 C C   . VAL B 1 139 ? 6.099  -2.816  1.249  1.00 25.22 ? 172 VAL B C   1 
ATOM   2392 O O   . VAL B 1 139 ? 5.423  -1.902  1.745  1.00 19.52 ? 172 VAL B O   1 
ATOM   2393 C CB  . VAL B 1 139 ? 8.428  -2.317  0.381  1.00 18.33 ? 172 VAL B CB  1 
ATOM   2394 C CG1 . VAL B 1 139 ? 7.796  -1.021  -0.136 1.00 23.30 ? 172 VAL B CG1 1 
ATOM   2395 C CG2 . VAL B 1 139 ? 9.859  -2.064  0.865  1.00 16.53 ? 172 VAL B CG2 1 
ATOM   2396 N N   . ARG B 1 140 ? 5.556  -3.797  0.517  1.00 20.18 ? 173 ARG B N   1 
ATOM   2397 C CA  . ARG B 1 140 ? 4.138  -3.780  0.195  1.00 24.19 ? 173 ARG B CA  1 
ATOM   2398 C C   . ARG B 1 140 ? 3.307  -4.140  1.417  1.00 25.67 ? 173 ARG B C   1 
ATOM   2399 O O   . ARG B 1 140 ? 2.308  -3.475  1.711  1.00 26.53 ? 173 ARG B O   1 
ATOM   2400 C CB  . ARG B 1 140 ? 3.863  -4.744  -0.966 1.00 25.17 ? 173 ARG B CB  1 
ATOM   2401 C CG  . ARG B 1 140 ? 2.437  -4.721  -1.505 1.00 37.56 ? 173 ARG B CG  1 
ATOM   2402 C CD  . ARG B 1 140 ? 2.186  -5.859  -2.497 1.00 44.57 ? 173 ARG B CD  1 
ATOM   2403 N NE  . ARG B 1 140 ? 3.304  -6.047  -3.415 1.00 52.24 ? 173 ARG B NE  1 
ATOM   2404 C CZ  . ARG B 1 140 ? 4.163  -7.058  -3.357 1.00 51.65 ? 173 ARG B CZ  1 
ATOM   2405 N NH1 . ARG B 1 140 ? 4.031  -8.028  -2.465 1.00 43.53 ? 173 ARG B NH1 1 
ATOM   2406 N NH2 . ARG B 1 140 ? 5.184  -7.093  -4.210 1.00 50.48 ? 173 ARG B NH2 1 
ATOM   2407 N N   . SER B 1 141 ? 3.740  -5.152  2.179  1.00 24.39 ? 174 SER B N   1 
ATOM   2408 C CA  . SER B 1 141 ? 2.862  -5.672  3.221  1.00 23.57 ? 174 SER B CA  1 
ATOM   2409 C C   . SER B 1 141 ? 2.824  -4.753  4.436  1.00 25.87 ? 174 SER B C   1 
ATOM   2410 O O   . SER B 1 141 ? 1.816  -4.712  5.145  1.00 24.37 ? 174 SER B O   1 
ATOM   2411 C CB  . SER B 1 141 ? 3.294  -7.083  3.630  1.00 25.22 ? 174 SER B CB  1 
ATOM   2412 O OG  . SER B 1 141 ? 4.580  -7.060  4.223  1.00 31.27 ? 174 SER B OG  1 
ATOM   2413 N N   . ARG B 1 142 ? 3.898  -4.013  4.692  1.00 23.14 ? 175 ARG B N   1 
ATOM   2414 C CA  . ARG B 1 142 ? 3.936  -3.069  5.797  1.00 22.42 ? 175 ARG B CA  1 
ATOM   2415 C C   . ARG B 1 142 ? 3.712  -1.634  5.344  1.00 21.16 ? 175 ARG B C   1 
ATOM   2416 O O   . ARG B 1 142 ? 3.764  -0.727  6.174  1.00 23.79 ? 175 ARG B O   1 
ATOM   2417 C CB  . ARG B 1 142 ? 5.265  -3.198  6.556  1.00 23.85 ? 175 ARG B CB  1 
ATOM   2418 C CG  . ARG B 1 142 ? 5.552  -4.637  6.980  1.00 27.08 ? 175 ARG B CG  1 
ATOM   2419 C CD  . ARG B 1 142 ? 6.776  -4.757  7.868  1.00 27.99 ? 175 ARG B CD  1 
ATOM   2420 N NE  . ARG B 1 142 ? 6.501  -4.237  9.198  1.00 31.11 ? 175 ARG B NE  1 
ATOM   2421 C CZ  . ARG B 1 142 ? 6.074  -4.967  10.219 1.00 30.57 ? 175 ARG B CZ  1 
ATOM   2422 N NH1 . ARG B 1 142 ? 5.959  -6.283  10.133 1.00 27.44 ? 175 ARG B NH1 1 
ATOM   2423 N NH2 . ARG B 1 142 ? 5.745  -4.358  11.351 1.00 28.42 ? 175 ARG B NH2 1 
ATOM   2424 N N   . HIS B 1 143 ? 3.457  -1.414  4.055  1.00 21.59 ? 176 HIS B N   1 
ATOM   2425 C CA  . HIS B 1 143 ? 3.126  -0.097  3.522  1.00 24.74 ? 176 HIS B CA  1 
ATOM   2426 C C   . HIS B 1 143 ? 4.205  0.925   3.879  1.00 24.34 ? 176 HIS B C   1 
ATOM   2427 O O   . HIS B 1 143 ? 3.925  2.011   4.390  1.00 25.89 ? 176 HIS B O   1 
ATOM   2428 C CB  . HIS B 1 143 ? 1.749  0.354   4.020  1.00 28.28 ? 176 HIS B CB  1 
ATOM   2429 C CG  . HIS B 1 143 ? 0.692  -0.699  3.905  1.00 37.18 ? 176 HIS B CG  1 
ATOM   2430 N ND1 . HIS B 1 143 ? -0.002 -0.936  2.737  1.00 47.34 ? 176 HIS B ND1 1 
ATOM   2431 C CD2 . HIS B 1 143 ? 0.216  -1.586  4.811  1.00 45.15 ? 176 HIS B CD2 1 
ATOM   2432 C CE1 . HIS B 1 143 ? -0.860 -1.922  2.928  1.00 45.60 ? 176 HIS B CE1 1 
ATOM   2433 N NE2 . HIS B 1 143 ? -0.750 -2.333  4.179  1.00 44.54 ? 176 HIS B NE2 1 
ATOM   2434 N N   . LEU B 1 144 ? 5.459  0.560   3.614  1.00 21.92 ? 177 LEU B N   1 
ATOM   2435 C CA  . LEU B 1 144 ? 6.591  1.398   4.000  1.00 23.90 ? 177 LEU B CA  1 
ATOM   2436 C C   . LEU B 1 144 ? 6.717  2.580   3.050  1.00 18.36 ? 177 LEU B C   1 
ATOM   2437 O O   . LEU B 1 144 ? 6.676  2.408   1.828  1.00 20.60 ? 177 LEU B O   1 
ATOM   2438 C CB  . LEU B 1 144 ? 7.893  0.589   3.996  1.00 16.75 ? 177 LEU B CB  1 
ATOM   2439 C CG  . LEU B 1 144 ? 7.952  -0.586  4.966  1.00 20.73 ? 177 LEU B CG  1 
ATOM   2440 C CD1 . LEU B 1 144 ? 9.326  -1.230  4.954  1.00 20.81 ? 177 LEU B CD1 1 
ATOM   2441 C CD2 . LEU B 1 144 ? 7.569  -0.144  6.380  1.00 21.76 ? 177 LEU B CD2 1 
ATOM   2442 N N   . ASP B 1 145 ? 6.880  3.776   3.606  1.00 19.15 ? 178 ASP B N   1 
ATOM   2443 C CA  . ASP B 1 145 ? 7.009  4.964   2.777  1.00 20.44 ? 178 ASP B CA  1 
ATOM   2444 C C   . ASP B 1 145 ? 8.464  5.084   2.319  1.00 23.45 ? 178 ASP B C   1 
ATOM   2445 O O   . ASP B 1 145 ? 9.282  4.186   2.541  1.00 22.11 ? 178 ASP B O   1 
ATOM   2446 C CB  . ASP B 1 145 ? 6.476  6.193   3.519  1.00 19.15 ? 178 ASP B CB  1 
ATOM   2447 C CG  . ASP B 1 145 ? 7.266  6.543   4.773  1.00 28.65 ? 178 ASP B CG  1 
ATOM   2448 O OD1 . ASP B 1 145 ? 8.356  5.982   5.011  1.00 22.49 ? 178 ASP B OD1 1 
ATOM   2449 O OD2 . ASP B 1 145 ? 6.782  7.415   5.529  1.00 28.66 ? 178 ASP B OD2 1 
ATOM   2450 N N   . SER B 1 146 ? 8.805  6.193   1.654  1.00 19.16 ? 179 SER B N   1 
ATOM   2451 C CA  . SER B 1 146 ? 10.129 6.299   1.048  1.00 20.82 ? 179 SER B CA  1 
ATOM   2452 C C   . SER B 1 146 ? 11.233 6.258   2.100  1.00 20.66 ? 179 SER B C   1 
ATOM   2453 O O   . SER B 1 146 ? 12.286 5.642   1.885  1.00 19.24 ? 179 SER B O   1 
ATOM   2454 C CB  . SER B 1 146 ? 10.233 7.580   0.223  1.00 23.83 ? 179 SER B CB  1 
ATOM   2455 O OG  . SER B 1 146 ? 10.224 8.710   1.076  1.00 36.79 ? 179 SER B OG  1 
ATOM   2456 N N   . LEU B 1 147 ? 11.024 6.923   3.237  1.00 19.20 ? 180 LEU B N   1 
ATOM   2457 C CA  . LEU B 1 147 ? 12.064 6.923   4.263  1.00 15.40 ? 180 LEU B CA  1 
ATOM   2458 C C   . LEU B 1 147 ? 12.307 5.516   4.797  1.00 14.86 ? 180 LEU B C   1 
ATOM   2459 O O   . LEU B 1 147 ? 13.463 5.098   4.961  1.00 15.75 ? 180 LEU B O   1 
ATOM   2460 C CB  . LEU B 1 147 ? 11.694 7.874   5.398  1.00 19.56 ? 180 LEU B CB  1 
ATOM   2461 C CG  . LEU B 1 147 ? 12.606 7.854   6.631  1.00 15.41 ? 180 LEU B CG  1 
ATOM   2462 C CD1 . LEU B 1 147 ? 14.000 8.398   6.285  1.00 17.32 ? 180 LEU B CD1 1 
ATOM   2463 C CD2 . LEU B 1 147 ? 11.963 8.663   7.754  1.00 19.64 ? 180 LEU B CD2 1 
ATOM   2464 N N   . TYR B 1 148 ? 11.237 4.764   5.078  1.00 16.46 ? 181 TYR B N   1 
ATOM   2465 C CA  . TYR B 1 148 ? 11.439 3.397   5.559  1.00 16.36 ? 181 TYR B CA  1 
ATOM   2466 C C   . TYR B 1 148 ? 11.999 2.499   4.459  1.00 15.77 ? 181 TYR B C   1 
ATOM   2467 O O   . TYR B 1 148 ? 12.761 1.577   4.755  1.00 15.90 ? 181 TYR B O   1 
ATOM   2468 C CB  . TYR B 1 148 ? 10.139 2.827   6.147  1.00 13.95 ? 181 TYR B CB  1 
ATOM   2469 C CG  . TYR B 1 148 ? 9.987  3.104   7.639  1.00 15.62 ? 181 TYR B CG  1 
ATOM   2470 C CD1 . TYR B 1 148 ? 9.563  4.348   8.096  1.00 18.48 ? 181 TYR B CD1 1 
ATOM   2471 C CD2 . TYR B 1 148 ? 10.295 2.133   8.586  1.00 20.00 ? 181 TYR B CD2 1 
ATOM   2472 C CE1 . TYR B 1 148 ? 9.435  4.615   9.461  1.00 18.44 ? 181 TYR B CE1 1 
ATOM   2473 C CE2 . TYR B 1 148 ? 10.167 2.392   9.957  1.00 20.02 ? 181 TYR B CE2 1 
ATOM   2474 C CZ  . TYR B 1 148 ? 9.737  3.641   10.382 1.00 22.27 ? 181 TYR B CZ  1 
ATOM   2475 O OH  . TYR B 1 148 ? 9.608  3.923   11.732 1.00 17.87 ? 181 TYR B OH  1 
ATOM   2476 N N   . GLN B 1 149 ? 11.688 2.775   3.188  1.00 15.43 ? 182 GLN B N   1 
ATOM   2477 C CA  . GLN B 1 149 ? 12.288 1.990   2.107  1.00 17.21 ? 182 GLN B CA  1 
ATOM   2478 C C   . GLN B 1 149 ? 13.801 2.190   2.061  1.00 16.06 ? 182 GLN B C   1 
ATOM   2479 O O   . GLN B 1 149 ? 14.564 1.221   1.932  1.00 15.75 ? 182 GLN B O   1 
ATOM   2480 C CB  . GLN B 1 149 ? 11.649 2.358   0.760  1.00 18.61 ? 182 GLN B CB  1 
ATOM   2481 C CG  . GLN B 1 149 ? 10.218 1.858   0.613  1.00 20.59 ? 182 GLN B CG  1 
ATOM   2482 C CD  . GLN B 1 149 ? 9.555  2.342   -0.655 1.00 26.83 ? 182 GLN B CD  1 
ATOM   2483 O OE1 . GLN B 1 149 ? 10.175 2.372   -1.716 1.00 27.06 ? 182 GLN B OE1 1 
ATOM   2484 N NE2 . GLN B 1 149 ? 8.296  2.743   -0.548 1.00 22.48 ? 182 GLN B NE2 1 
ATOM   2485 N N   . ARG B 1 150 ? 14.254 3.443   2.177  1.00 14.69 ? 183 ARG B N   1 
ATOM   2486 C CA  . ARG B 1 150 ? 15.690 3.711   2.198  1.00 14.90 ? 183 ARG B CA  1 
ATOM   2487 C C   . ARG B 1 150 ? 16.348 3.098   3.432  1.00 14.53 ? 183 ARG B C   1 
ATOM   2488 O O   . ARG B 1 150 ? 17.456 2.545   3.357  1.00 15.26 ? 183 ARG B O   1 
ATOM   2489 C CB  . ARG B 1 150 ? 15.935 5.217   2.161  1.00 15.55 ? 183 ARG B CB  1 
ATOM   2490 C CG  . ARG B 1 150 ? 15.391 5.893   0.920  1.00 17.52 ? 183 ARG B CG  1 
ATOM   2491 C CD  . ARG B 1 150 ? 15.316 7.399   1.135  1.00 23.35 ? 183 ARG B CD  1 
ATOM   2492 N NE  . ARG B 1 150 ? 16.634 7.967   1.386  1.00 23.82 ? 183 ARG B NE  1 
ATOM   2493 C CZ  . ARG B 1 150 ? 16.849 9.066   2.097  1.00 29.83 ? 183 ARG B CZ  1 
ATOM   2494 N NH1 . ARG B 1 150 ? 15.856 9.702   2.699  1.00 23.72 ? 183 ARG B NH1 1 
ATOM   2495 N NH2 . ARG B 1 150 ? 18.089 9.541   2.203  1.00 21.00 ? 183 ARG B NH2 1 
ATOM   2496 N N   . ALA B 1 151 ? 15.681 3.199   4.581  1.00 14.18 ? 184 ALA B N   1 
ATOM   2497 C CA  . ALA B 1 151 ? 16.234 2.597   5.788  1.00 13.42 ? 184 ALA B CA  1 
ATOM   2498 C C   . ALA B 1 151 ? 16.331 1.083   5.651  1.00 13.45 ? 184 ALA B C   1 
ATOM   2499 O O   . ALA B 1 151 ? 17.313 0.472   6.088  1.00 12.91 ? 184 ALA B O   1 
ATOM   2500 C CB  . ALA B 1 151 ? 15.389 2.986   7.003  1.00 13.27 ? 184 ALA B CB  1 
ATOM   2501 N N   . LEU B 1 152 ? 15.317 0.453   5.062  1.00 12.95 ? 185 LEU B N   1 
ATOM   2502 C CA  . LEU B 1 152 ? 15.356 -0.999  4.930  1.00 13.78 ? 185 LEU B CA  1 
ATOM   2503 C C   . LEU B 1 152 ? 16.461 -1.420  3.973  1.00 15.72 ? 185 LEU B C   1 
ATOM   2504 O O   . LEU B 1 152 ? 17.129 -2.437  4.196  1.00 14.38 ? 185 LEU B O   1 
ATOM   2505 C CB  . LEU B 1 152 ? 13.998 -1.525  4.478  1.00 13.06 ? 185 LEU B CB  1 
ATOM   2506 C CG  . LEU B 1 152 ? 13.882 -3.057  4.436  1.00 14.50 ? 185 LEU B CG  1 
ATOM   2507 C CD1 . LEU B 1 152 ? 13.843 -3.642  5.848  1.00 15.53 ? 185 LEU B CD1 1 
ATOM   2508 C CD2 . LEU B 1 152 ? 12.656 -3.451  3.637  1.00 19.80 ? 185 LEU B CD2 1 
ATOM   2509 N N   . THR B 1 153 ? 16.680 -0.645  2.906  1.00 14.64 ? 186 THR B N   1 
ATOM   2510 C CA  . THR B 1 153 ? 17.824 -0.919  2.035  1.00 15.23 ? 186 THR B CA  1 
ATOM   2511 C C   . THR B 1 153 ? 19.137 -0.839  2.805  1.00 16.34 ? 186 THR B C   1 
ATOM   2512 O O   . THR B 1 153 ? 19.986 -1.734  2.703  1.00 15.46 ? 186 THR B O   1 
ATOM   2513 C CB  . THR B 1 153 ? 17.825 0.047   0.851  1.00 18.03 ? 186 THR B CB  1 
ATOM   2514 O OG1 . THR B 1 153 ? 16.645 -0.178  0.099  1.00 17.83 ? 186 THR B OG1 1 
ATOM   2515 C CG2 . THR B 1 153 ? 19.020 -0.193  -0.053 1.00 21.90 ? 186 THR B CG2 1 
ATOM   2516 N N   . THR B 1 154 ? 19.317 0.215   3.606  1.00 15.26 ? 187 THR B N   1 
ATOM   2517 C CA  . THR B 1 154 ? 20.561 0.321   4.361  1.00 15.49 ? 187 THR B CA  1 
ATOM   2518 C C   . THR B 1 154 ? 20.697 -0.840  5.347  1.00 15.15 ? 187 THR B C   1 
ATOM   2519 O O   . THR B 1 154 ? 21.778 -1.425  5.500  1.00 13.86 ? 187 THR B O   1 
ATOM   2520 C CB  . THR B 1 154 ? 20.615 1.677   5.080  1.00 14.35 ? 187 THR B CB  1 
ATOM   2521 O OG1 . THR B 1 154 ? 20.716 2.726   4.107  1.00 15.10 ? 187 THR B OG1 1 
ATOM   2522 C CG2 . THR B 1 154 ? 21.815 1.743   6.034  1.00 14.60 ? 187 THR B CG2 1 
ATOM   2523 N N   . ALA B 1 155 ? 19.591 -1.208  5.997  1.00 13.06 ? 188 ALA B N   1 
ATOM   2524 C CA  . ALA B 1 155 ? 19.627 -2.205  7.060  1.00 12.71 ? 188 ALA B CA  1 
ATOM   2525 C C   . ALA B 1 155 ? 19.985 -3.588  6.530  1.00 15.87 ? 188 ALA B C   1 
ATOM   2526 O O   . ALA B 1 155 ? 20.607 -4.378  7.245  1.00 14.91 ? 188 ALA B O   1 
ATOM   2527 C CB  . ALA B 1 155 ? 18.277 -2.253  7.773  1.00 12.64 ? 188 ALA B CB  1 
ATOM   2528 N N   . THR B 1 156 ? 19.601 -3.897  5.292  1.00 12.96 ? 189 THR B N   1 
ATOM   2529 C CA  . THR B 1 156 ? 19.802 -5.217  4.716  1.00 13.18 ? 189 THR B CA  1 
ATOM   2530 C C   . THR B 1 156 ? 20.988 -5.297  3.753  1.00 13.86 ? 189 THR B C   1 
ATOM   2531 O O   . THR B 1 156 ? 21.204 -6.352  3.146  1.00 15.72 ? 189 THR B O   1 
ATOM   2532 C CB  . THR B 1 156 ? 18.529 -5.649  3.993  1.00 13.21 ? 189 THR B CB  1 
ATOM   2533 O OG1 . THR B 1 156 ? 18.218 -4.689  2.972  1.00 14.42 ? 189 THR B OG1 1 
ATOM   2534 C CG2 . THR B 1 156 ? 17.370 -5.731  4.970  1.00 18.96 ? 189 THR B CG2 1 
ATOM   2535 N N   . GLN B 1 157 ? 21.774 -4.229  3.609  1.00 14.19 ? 190 GLN B N   1 
ATOM   2536 C CA  . GLN B 1 157 ? 22.736 -4.189  2.507  1.00 15.07 ? 190 GLN B CA  1 
ATOM   2537 C C   . GLN B 1 157 ? 23.880 -5.181  2.662  1.00 16.84 ? 190 GLN B C   1 
ATOM   2538 O O   . GLN B 1 157 ? 24.533 -5.504  1.661  1.00 17.84 ? 190 GLN B O   1 
ATOM   2539 C CB  . GLN B 1 157 ? 23.308 -2.782  2.360  1.00 19.31 ? 190 GLN B CB  1 
ATOM   2540 C CG  . GLN B 1 157 ? 24.202 -2.386  3.509  1.00 16.69 ? 190 GLN B CG  1 
ATOM   2541 C CD  . GLN B 1 157 ? 24.696 -0.954  3.392  1.00 31.43 ? 190 GLN B CD  1 
ATOM   2542 O OE1 . GLN B 1 157 ? 25.589 -0.658  2.601  1.00 39.29 ? 190 GLN B OE1 1 
ATOM   2543 N NE2 . GLN B 1 157 ? 24.113 -0.061  4.177  1.00 29.64 ? 190 GLN B NE2 1 
ATOM   2544 N N   . SER B 1 158 ? 24.157 -5.660  3.877  1.00 15.06 ? 191 SER B N   1 
ATOM   2545 C CA  . SER B 1 158 ? 25.255 -6.591  4.109  1.00 19.18 ? 191 SER B CA  1 
ATOM   2546 C C   . SER B 1 158 ? 24.796 -8.039  4.242  1.00 18.40 ? 191 SER B C   1 
ATOM   2547 O O   . SER B 1 158 ? 25.618 -8.909  4.553  1.00 19.34 ? 191 SER B O   1 
ATOM   2548 C CB  . SER B 1 158 ? 26.039 -6.178  5.359  1.00 15.60 ? 191 SER B CB  1 
ATOM   2549 O OG  . SER B 1 158 ? 26.573 -4.881  5.189  1.00 15.91 ? 191 SER B OG  1 
ATOM   2550 N N   . TYR B 1 159 ? 23.508 -8.320  4.010  1.00 16.82 ? 192 TYR B N   1 
ATOM   2551 C CA  . TYR B 1 159 ? 22.998 -9.676  4.194  1.00 15.21 ? 192 TYR B CA  1 
ATOM   2552 C C   . TYR B 1 159 ? 23.754 -10.682 3.337  1.00 19.11 ? 192 TYR B C   1 
ATOM   2553 O O   . TYR B 1 159 ? 24.104 -11.773 3.803  1.00 17.52 ? 192 TYR B O   1 
ATOM   2554 C CB  . TYR B 1 159 ? 21.513 -9.741  3.845  1.00 14.55 ? 192 TYR B CB  1 
ATOM   2555 C CG  . TYR B 1 159 ? 20.577 -9.266  4.917  1.00 17.13 ? 192 TYR B CG  1 
ATOM   2556 C CD1 . TYR B 1 159 ? 21.045 -8.588  6.030  1.00 16.73 ? 192 TYR B CD1 1 
ATOM   2557 C CD2 . TYR B 1 159 ? 19.211 -9.509  4.812  1.00 17.44 ? 192 TYR B CD2 1 
ATOM   2558 C CE1 . TYR B 1 159 ? 20.167 -8.158  7.025  1.00 14.22 ? 192 TYR B CE1 1 
ATOM   2559 C CE2 . TYR B 1 159 ? 18.336 -9.083  5.782  1.00 17.34 ? 192 TYR B CE2 1 
ATOM   2560 C CZ  . TYR B 1 159 ? 18.820 -8.415  6.886  1.00 13.17 ? 192 TYR B CZ  1 
ATOM   2561 O OH  . TYR B 1 159 ? 17.933 -7.991  7.841  1.00 19.77 ? 192 TYR B OH  1 
ATOM   2562 N N   . CYS B 1 160 ? 23.959 -10.361 2.060  1.00 16.67 ? 193 CYS B N   1 
ATOM   2563 C CA  . CYS B 1 160 ? 24.486 -11.345 1.129  1.00 19.89 ? 193 CYS B CA  1 
ATOM   2564 C C   . CYS B 1 160 ? 26.014 -11.382 1.115  1.00 21.50 ? 193 CYS B C   1 
ATOM   2565 O O   . CYS B 1 160 ? 26.608 -11.904 0.165  1.00 34.66 ? 193 CYS B O   1 
ATOM   2566 C CB  . CYS B 1 160 ? 23.899 -11.097 -0.262 1.00 20.39 ? 193 CYS B CB  1 
ATOM   2567 S SG  . CYS B 1 160 ? 22.069 -11.263 -0.286 1.00 25.01 ? 193 CYS B SG  1 
ATOM   2568 N N   . GLN B 1 161 ? 26.656 -10.883 2.172  1.00 28.28 ? 194 GLN B N   1 
ATOM   2569 C CA  . GLN B 1 161 ? 28.100 -10.987 2.360  1.00 27.83 ? 194 GLN B CA  1 
ATOM   2570 C C   . GLN B 1 161 ? 28.517 -12.255 3.098  1.00 29.54 ? 194 GLN B C   1 
ATOM   2571 O O   . GLN B 1 161 ? 29.713 -12.439 3.350  1.00 28.55 ? 194 GLN B O   1 
ATOM   2572 C CB  . GLN B 1 161 ? 28.635 -9.782  3.149  1.00 32.68 ? 194 GLN B CB  1 
ATOM   2573 C CG  . GLN B 1 161 ? 28.108 -8.429  2.718  1.00 30.72 ? 194 GLN B CG  1 
ATOM   2574 C CD  . GLN B 1 161 ? 28.812 -7.883  1.510  1.00 42.30 ? 194 GLN B CD  1 
ATOM   2575 O OE1 . GLN B 1 161 ? 29.826 -8.427  1.067  1.00 49.24 ? 194 GLN B OE1 1 
ATOM   2576 N NE2 . GLN B 1 161 ? 28.283 -6.792  0.963  1.00 50.02 ? 194 GLN B NE2 1 
ATOM   2577 N N   . ALA B 1 162 ? 27.569 -13.104 3.487  1.00 26.76 ? 195 ALA B N   1 
ATOM   2578 C CA  . ALA B 1 162 ? 27.893 -14.262 4.311  1.00 26.08 ? 195 ALA B CA  1 
ATOM   2579 C C   . ALA B 1 162 ? 28.886 -15.164 3.593  1.00 34.74 ? 195 ALA B C   1 
ATOM   2580 O O   . ALA B 1 162 ? 28.702 -15.494 2.418  1.00 38.19 ? 195 ALA B O   1 
ATOM   2581 C CB  . ALA B 1 162 ? 26.617 -15.033 4.650  1.00 25.55 ? 195 ALA B CB  1 
ATOM   2582 N N   . LEU B 1 163 ? 29.900 -15.607 4.322  1.00 33.22 ? 196 LEU B N   1 
ATOM   2583 C CA  . LEU B 1 163 ? 30.941 -16.473 3.710  1.00 39.01 ? 196 LEU B CA  1 
ATOM   2584 C C   . LEU B 1 163 ? 30.574 -17.958 3.856  1.00 38.07 ? 196 LEU B C   1 
ATOM   2585 O O   . LEU B 1 163 ? 30.046 -18.324 4.906  1.00 39.43 ? 196 LEU B O   1 
ATOM   2586 C CB  . LEU B 1 163 ? 32.282 -16.151 4.378  1.00 47.16 ? 196 LEU B CB  1 
ATOM   2587 C CG  . LEU B 1 163 ? 32.926 -14.853 3.893  1.00 50.77 ? 196 LEU B CG  1 
ATOM   2588 C CD1 . LEU B 1 163 ? 34.167 -14.517 4.700  1.00 58.49 ? 196 LEU B CD1 1 
ATOM   2589 C CD2 . LEU B 1 163 ? 33.256 -14.937 2.412  1.00 44.06 ? 196 LEU B CD2 1 
HETATM 2590 C C   . ACE C 2 1   ? 27.891 7.414   11.720 1.00 18.10 ? 0   ACE C C   1 
HETATM 2591 O O   . ACE C 2 1   ? 26.761 7.258   12.188 1.00 18.59 ? 0   ACE C O   1 
HETATM 2592 C CH3 . ACE C 2 1   ? 28.412 6.590   10.580 1.00 20.05 ? 0   ACE C CH3 1 
HETATM 2593 N N   . DTY C 2 2   ? 28.762 8.300   12.189 1.00 14.49 ? 1   DTY C N   1 
HETATM 2594 C CA  . DTY C 2 2   ? 28.388 9.231   13.284 1.00 14.76 ? 1   DTY C CA  1 
HETATM 2595 C C   . DTY C 2 2   ? 29.469 9.241   14.371 1.00 16.69 ? 1   DTY C C   1 
HETATM 2596 O O   . DTY C 2 2   ? 30.660 9.359   14.024 1.00 15.50 ? 1   DTY C O   1 
HETATM 2597 C CB  . DTY C 2 2   ? 28.243 10.636  12.698 1.00 17.64 ? 1   DTY C CB  1 
HETATM 2598 C CG  . DTY C 2 2   ? 27.773 11.679  13.672 1.00 15.63 ? 1   DTY C CG  1 
HETATM 2599 C CD1 . DTY C 2 2   ? 28.546 12.799  13.946 1.00 16.39 ? 1   DTY C CD1 1 
HETATM 2600 C CD2 . DTY C 2 2   ? 26.551 11.554  14.314 1.00 15.42 ? 1   DTY C CD2 1 
HETATM 2601 C CE1 . DTY C 2 2   ? 28.120 13.766  14.839 1.00 16.90 ? 1   DTY C CE1 1 
HETATM 2602 C CE2 . DTY C 2 2   ? 26.110 12.518  15.208 1.00 15.91 ? 1   DTY C CE2 1 
HETATM 2603 C CZ  . DTY C 2 2   ? 26.900 13.621  15.478 1.00 16.64 ? 1   DTY C CZ  1 
HETATM 2604 O OH  . DTY C 2 2   ? 26.481 14.586  16.361 1.00 18.45 ? 1   DTY C OH  1 
ATOM   2605 N N   . GLN C 2 3   ? 29.068 9.187   15.637 1.00 15.15 ? 2   GLN C N   1 
ATOM   2606 C CA  . GLN C 2 3   ? 30.024 9.228   16.737 1.00 15.61 ? 2   GLN C CA  1 
ATOM   2607 C C   . GLN C 2 3   ? 30.459 7.824   17.114 1.00 15.28 ? 2   GLN C C   1 
ATOM   2608 O O   . GLN C 2 3   ? 29.637 6.909   17.154 1.00 15.18 ? 2   GLN C O   1 
ATOM   2609 C CB  . GLN C 2 3   ? 29.418 9.931   17.957 1.00 16.00 ? 2   GLN C CB  1 
ATOM   2610 C CG  . GLN C 2 3   ? 29.105 11.423  17.700 1.00 16.53 ? 2   GLN C CG  1 
ATOM   2611 C CD  . GLN C 2 3   ? 28.573 12.143  18.935 1.00 20.60 ? 2   GLN C CD  1 
ATOM   2612 O OE1 . GLN C 2 3   ? 27.767 11.592  19.691 1.00 20.15 ? 2   GLN C OE1 1 
ATOM   2613 N NE2 . GLN C 2 3   ? 29.034 13.374  19.152 1.00 23.42 ? 2   GLN C NE2 1 
ATOM   2614 N N   . PHE C 2 4   ? 31.751 7.666   17.396 1.00 15.68 ? 3   PHE C N   1 
ATOM   2615 C CA  . PHE C 2 4   ? 32.284 6.401   17.890 1.00 16.12 ? 3   PHE C CA  1 
ATOM   2616 C C   . PHE C 2 4   ? 33.690 6.649   18.424 1.00 21.03 ? 3   PHE C C   1 
ATOM   2617 O O   . PHE C 2 4   ? 34.366 7.578   17.982 1.00 16.82 ? 3   PHE C O   1 
ATOM   2618 C CB  . PHE C 2 4   ? 32.306 5.330   16.785 1.00 15.68 ? 3   PHE C CB  1 
ATOM   2619 C CG  . PHE C 2 4   ? 33.058 5.747   15.553 1.00 18.66 ? 3   PHE C CG  1 
ATOM   2620 C CD1 . PHE C 2 4   ? 32.412 6.426   14.530 1.00 15.13 ? 3   PHE C CD1 1 
ATOM   2621 C CD2 . PHE C 2 4   ? 34.404 5.444   15.411 1.00 18.96 ? 3   PHE C CD2 1 
ATOM   2622 C CE1 . PHE C 2 4   ? 33.100 6.817   13.390 1.00 16.76 ? 3   PHE C CE1 1 
ATOM   2623 C CE2 . PHE C 2 4   ? 35.097 5.830   14.272 1.00 20.32 ? 3   PHE C CE2 1 
ATOM   2624 C CZ  . PHE C 2 4   ? 34.442 6.518   13.263 1.00 25.77 ? 3   PHE C CZ  1 
ATOM   2625 N N   . GLU C 2 5   ? 34.118 5.822   19.377 1.00 16.39 ? 4   GLU C N   1 
ATOM   2626 C CA  . GLU C 2 5   ? 35.507 5.839   19.821 1.00 20.90 ? 4   GLU C CA  1 
ATOM   2627 C C   . GLU C 2 5   ? 36.345 4.956   18.909 1.00 22.08 ? 4   GLU C C   1 
ATOM   2628 O O   . GLU C 2 5   ? 35.823 4.116   18.176 1.00 18.04 ? 4   GLU C O   1 
ATOM   2629 C CB  . GLU C 2 5   ? 35.641 5.363   21.271 1.00 18.66 ? 4   GLU C CB  1 
ATOM   2630 C CG  . GLU C 2 5   ? 34.827 6.172   22.261 1.00 23.36 ? 4   GLU C CG  1 
ATOM   2631 C CD  . GLU C 2 5   ? 35.294 7.606   22.349 1.00 32.13 ? 4   GLU C CD  1 
ATOM   2632 O OE1 . GLU C 2 5   ? 36.503 7.821   22.562 1.00 33.14 ? 4   GLU C OE1 1 
ATOM   2633 O OE2 . GLU C 2 5   ? 34.455 8.516   22.193 1.00 34.02 ? 4   GLU C OE2 1 
ATOM   2634 N N   . GLN C 2 6   ? 37.665 5.161   18.962 1.00 21.02 ? 5   GLN C N   1 
ATOM   2635 C CA  . GLN C 2 6   ? 38.562 4.443   18.062 1.00 27.39 ? 5   GLN C CA  1 
ATOM   2636 C C   . GLN C 2 6   ? 38.491 2.939   18.282 1.00 23.59 ? 5   GLN C C   1 
ATOM   2637 O O   . GLN C 2 6   ? 38.733 2.168   17.350 1.00 24.95 ? 5   GLN C O   1 
ATOM   2638 C CB  . GLN C 2 6   ? 40.004 4.926   18.247 1.00 30.23 ? 5   GLN C CB  1 
ATOM   2639 C CG  . GLN C 2 6   ? 40.206 6.417   18.056 1.00 44.79 ? 5   GLN C CG  1 
ATOM   2640 C CD  . GLN C 2 6   ? 40.549 6.787   16.629 1.00 59.61 ? 5   GLN C CD  1 
ATOM   2641 O OE1 . GLN C 2 6   ? 40.161 6.098   15.682 1.00 50.98 ? 5   GLN C OE1 1 
ATOM   2642 N NE2 . GLN C 2 6   ? 41.293 7.881   16.467 1.00 61.86 ? 5   GLN C NE2 1 
ATOM   2643 N N   . TRP C 2 7   ? 38.164 2.500   19.496 1.00 18.01 ? 6   TRP C N   1 
ATOM   2644 C CA  . TRP C 2 7   ? 38.121 1.078   19.810 1.00 17.26 ? 6   TRP C CA  1 
ATOM   2645 C C   . TRP C 2 7   ? 36.737 0.451   19.619 1.00 18.06 ? 6   TRP C C   1 
ATOM   2646 O O   . TRP C 2 7   ? 36.589 -0.759  19.834 1.00 17.85 ? 6   TRP C O   1 
ATOM   2647 C CB  . TRP C 2 7   ? 38.610 0.862   21.254 1.00 19.59 ? 6   TRP C CB  1 
ATOM   2648 C CG  . TRP C 2 7   ? 37.817 1.641   22.265 1.00 19.24 ? 6   TRP C CG  1 
ATOM   2649 C CD1 . TRP C 2 7   ? 38.029 2.932   22.671 1.00 19.30 ? 6   TRP C CD1 1 
ATOM   2650 C CD2 . TRP C 2 7   ? 36.660 1.181   22.971 1.00 17.37 ? 6   TRP C CD2 1 
ATOM   2651 N NE1 . TRP C 2 7   ? 37.079 3.291   23.608 1.00 18.43 ? 6   TRP C NE1 1 
ATOM   2652 C CE2 . TRP C 2 7   ? 36.229 2.234   23.803 1.00 17.72 ? 6   TRP C CE2 1 
ATOM   2653 C CE3 . TRP C 2 7   ? 35.963 -0.031  23.000 1.00 16.89 ? 6   TRP C CE3 1 
ATOM   2654 C CZ2 . TRP C 2 7   ? 35.122 2.117   24.642 1.00 19.99 ? 6   TRP C CZ2 1 
ATOM   2655 C CZ3 . TRP C 2 7   ? 34.858 -0.142  23.828 1.00 16.77 ? 6   TRP C CZ3 1 
ATOM   2656 C CH2 . TRP C 2 7   ? 34.448 0.925   24.635 1.00 17.91 ? 6   TRP C CH2 1 
ATOM   2657 N N   . HIS C 2 8   ? 35.730 1.232   19.221 1.00 15.92 ? 7   HIS C N   1 
ATOM   2658 C CA  . HIS C 2 8   ? 34.370 0.719   19.081 1.00 15.28 ? 7   HIS C CA  1 
ATOM   2659 C C   . HIS C 2 8   ? 34.221 -0.165  17.847 1.00 17.45 ? 7   HIS C C   1 
ATOM   2660 O O   . HIS C 2 8   ? 34.869 0.050   16.824 1.00 15.79 ? 7   HIS C O   1 
ATOM   2661 C CB  . HIS C 2 8   ? 33.367 1.871   18.953 1.00 15.59 ? 7   HIS C CB  1 
ATOM   2662 C CG  . HIS C 2 8   ? 32.998 2.514   20.252 1.00 16.54 ? 7   HIS C CG  1 
ATOM   2663 N ND1 . HIS C 2 8   ? 32.167 3.613   20.322 1.00 17.41 ? 7   HIS C ND1 1 
ATOM   2664 C CD2 . HIS C 2 8   ? 33.341 2.218   21.529 1.00 17.75 ? 7   HIS C CD2 1 
ATOM   2665 C CE1 . HIS C 2 8   ? 32.009 3.963   21.586 1.00 20.21 ? 7   HIS C CE1 1 
ATOM   2666 N NE2 . HIS C 2 8   ? 32.701 3.126   22.339 1.00 19.40 ? 7   HIS C NE2 1 
ATOM   2667 N N   . ILE C 2 9   ? 33.286 -1.117  17.930 1.00 14.86 ? 8   ILE C N   1 
ATOM   2668 C CA  . ILE C 2 9   ? 32.943 -1.946  16.774 1.00 16.07 ? 8   ILE C CA  1 
ATOM   2669 C C   . ILE C 2 9   ? 32.451 -1.083  15.614 1.00 16.49 ? 8   ILE C C   1 
ATOM   2670 O O   . ILE C 2 9   ? 32.784 -1.332  14.449 1.00 17.95 ? 8   ILE C O   1 
ATOM   2671 C CB  . ILE C 2 9   ? 31.895 -3.001  17.170 1.00 15.17 ? 8   ILE C CB  1 
ATOM   2672 C CG1 . ILE C 2 9   ? 32.473 -3.939  18.236 1.00 17.43 ? 8   ILE C CG1 1 
ATOM   2673 C CG2 . ILE C 2 9   ? 31.415 -3.758  15.914 1.00 14.65 ? 8   ILE C CG2 1 
ATOM   2674 C CD1 . ILE C 2 9   ? 31.434 -4.800  18.952 1.00 17.24 ? 8   ILE C CD1 1 
ATOM   2675 N N   . ARG C 2 10  ? 31.648 -0.061  15.909 1.00 14.58 ? 9   ARG C N   1 
ATOM   2676 C CA  . ARG C 2 10  ? 31.126 0.802   14.848 1.00 13.74 ? 9   ARG C CA  1 
ATOM   2677 C C   . ARG C 2 10  ? 32.246 1.428   14.013 1.00 17.90 ? 9   ARG C C   1 
ATOM   2678 O O   . ARG C 2 10  ? 32.054 1.688   12.818 1.00 18.18 ? 9   ARG C O   1 
ATOM   2679 C CB  . ARG C 2 10  ? 30.236 1.886   15.462 1.00 13.80 ? 9   ARG C CB  1 
ATOM   2680 C CG  . ARG C 2 10  ? 29.925 3.059   14.556 1.00 14.10 ? 9   ARG C CG  1 
ATOM   2681 C CD  . ARG C 2 10  ? 28.602 3.703   14.972 1.00 16.90 ? 9   ARG C CD  1 
ATOM   2682 N NE  . ARG C 2 10  ? 27.465 2.874   14.596 1.00 16.00 ? 9   ARG C NE  1 
ATOM   2683 C CZ  . ARG C 2 10  ? 26.199 3.266   14.652 1.00 19.27 ? 9   ARG C CZ  1 
ATOM   2684 N NH1 . ARG C 2 10  ? 25.864 4.441   15.150 1.00 15.99 ? 9   ARG C NH1 1 
ATOM   2685 N NH2 . ARG C 2 10  ? 25.247 2.462   14.178 1.00 18.39 ? 9   ARG C NH2 1 
ATOM   2686 N N   . GLY C 2 11  ? 33.427 1.633   14.601 1.00 15.85 ? 10  GLY C N   1 
ATOM   2687 C CA  . GLY C 2 11  ? 34.538 2.193   13.848 1.00 14.99 ? 10  GLY C CA  1 
ATOM   2688 C C   . GLY C 2 11  ? 35.041 1.314   12.715 1.00 18.37 ? 10  GLY C C   1 
ATOM   2689 O O   . GLY C 2 11  ? 35.787 1.800   11.856 1.00 20.55 ? 10  GLY C O   1 
ATOM   2690 N N   . ARG C 2 12  ? 34.655 0.030   12.693 1.00 18.60 ? 11  ARG C N   1 
ATOM   2691 C CA  . ARG C 2 12  ? 35.120 -0.935  11.694 1.00 20.16 ? 11  ARG C CA  1 
ATOM   2692 C C   . ARG C 2 12  ? 34.357 -0.881  10.376 1.00 21.68 ? 11  ARG C C   1 
ATOM   2693 O O   . ARG C 2 12  ? 34.843 -1.415  9.372  1.00 19.69 ? 11  ARG C O   1 
ATOM   2694 C CB  . ARG C 2 12  ? 34.997 -2.367  12.227 1.00 16.28 ? 11  ARG C CB  1 
ATOM   2695 C CG  . ARG C 2 12  ? 35.781 -2.665  13.501 1.00 23.31 ? 11  ARG C CG  1 
ATOM   2696 C CD  . ARG C 2 12  ? 35.428 -4.069  13.964 1.00 29.94 ? 11  ARG C CD  1 
ATOM   2697 N NE  . ARG C 2 12  ? 35.889 -4.354  15.317 1.00 34.63 ? 11  ARG C NE  1 
ATOM   2698 C CZ  . ARG C 2 12  ? 35.600 -5.467  15.980 1.00 39.70 ? 11  ARG C CZ  1 
ATOM   2699 N NH1 . ARG C 2 12  ? 34.853 -6.418  15.442 1.00 33.24 ? 11  ARG C NH1 1 
ATOM   2700 N NH2 . ARG C 2 12  ? 36.075 -5.631  17.212 1.00 31.45 ? 11  ARG C NH2 1 
ATOM   2701 N N   . TYR C 2 13  ? 33.202 -0.234  10.338 1.00 14.50 ? 12  TYR C N   1 
ATOM   2702 C CA  . TYR C 2 13  ? 32.246 -0.436  9.254  1.00 16.10 ? 12  TYR C CA  1 
ATOM   2703 C C   . TYR C 2 13  ? 31.993 0.899   8.568  1.00 18.71 ? 12  TYR C C   1 
ATOM   2704 O O   . TYR C 2 13  ? 32.918 1.709   8.461  1.00 18.49 ? 12  TYR C O   1 
ATOM   2705 C CB  . TYR C 2 13  ? 30.960 -1.091  9.767  1.00 18.55 ? 12  TYR C CB  1 
ATOM   2706 C CG  . TYR C 2 13  ? 31.211 -2.417  10.461 1.00 18.78 ? 12  TYR C CG  1 
ATOM   2707 C CD1 . TYR C 2 13  ? 32.046 -3.372  9.887  1.00 15.78 ? 12  TYR C CD1 1 
ATOM   2708 C CD2 . TYR C 2 13  ? 30.652 -2.700  11.705 1.00 14.88 ? 12  TYR C CD2 1 
ATOM   2709 C CE1 . TYR C 2 13  ? 32.299 -4.584  10.526 1.00 19.77 ? 12  TYR C CE1 1 
ATOM   2710 C CE2 . TYR C 2 13  ? 30.902 -3.907  12.348 1.00 18.33 ? 12  TYR C CE2 1 
ATOM   2711 C CZ  . TYR C 2 13  ? 31.728 -4.844  11.749 1.00 19.15 ? 12  TYR C CZ  1 
ATOM   2712 O OH  . TYR C 2 13  ? 31.986 -6.046  12.376 1.00 23.23 ? 12  TYR C OH  1 
ATOM   2713 N N   . ALA C 2 14  ? 30.814 1.056   7.961  1.00 18.73 ? 13  ALA C N   1 
ATOM   2714 C CA  . ALA C 2 14  ? 30.537 2.203   7.092  1.00 18.33 ? 13  ALA C CA  1 
ATOM   2715 C C   . ALA C 2 14  ? 30.947 3.543   7.699  1.00 23.15 ? 13  ALA C C   1 
ATOM   2716 O O   . ALA C 2 14  ? 31.316 4.466   6.959  1.00 17.39 ? 13  ALA C O   1 
ATOM   2717 C CB  . ALA C 2 14  ? 29.050 2.233   6.741  1.00 20.20 ? 13  ALA C CB  1 
ATOM   2718 N N   . CYS C 2 15  ? 30.887 3.678   9.027  1.00 18.43 ? 14  CYS C N   1 
ATOM   2719 C CA  . CYS C 2 15  ? 31.185 4.951   9.693  1.00 19.70 ? 14  CYS C CA  1 
ATOM   2720 C C   . CYS C 2 15  ? 32.672 5.249   9.767  1.00 22.06 ? 14  CYS C C   1 
ATOM   2721 O O   . CYS C 2 15  ? 33.486 4.344   9.565  1.00 25.87 ? 14  CYS C O   1 
ATOM   2722 C CB  . CYS C 2 15  ? 30.599 4.962   11.108 1.00 20.01 ? 14  CYS C CB  1 
ATOM   2723 S SG  . CYS C 2 15  ? 28.795 4.898   11.112 1.00 19.35 ? 14  CYS C SG  1 
ATOM   2724 O OXT . CYS C 2 15  ? 33.075 6.395   10.035 1.00 21.31 ? 14  CYS C OXT 1 
HETATM 2725 C C   . ACE D 2 1   ? 13.372 21.985  19.877 1.00 16.95 ? 0   ACE D C   1 
HETATM 2726 O O   . ACE D 2 1   ? 14.332 22.160  19.137 1.00 22.21 ? 0   ACE D O   1 
HETATM 2727 C CH3 . ACE D 2 1   ? 12.084 22.742  19.696 1.00 16.75 ? 0   ACE D CH3 1 
HETATM 2728 N N   . DTY D 2 2   ? 13.437 21.110  20.891 1.00 14.33 ? 1   DTY D N   1 
HETATM 2729 C CA  . DTY D 2 2   ? 14.677 20.318  21.087 1.00 14.24 ? 1   DTY D CA  1 
HETATM 2730 C C   . DTY D 2 2   ? 15.141 20.396  22.543 1.00 15.88 ? 1   DTY D C   1 
HETATM 2731 O O   . DTY D 2 2   ? 14.303 20.140  23.430 1.00 16.29 ? 1   DTY D O   1 
HETATM 2732 C CB  . DTY D 2 2   ? 14.395 18.846  20.782 1.00 15.12 ? 1   DTY D CB  1 
HETATM 2733 C CG  . DTY D 2 2   ? 15.574 17.927  20.972 1.00 14.55 ? 1   DTY D CG  1 
HETATM 2734 C CD1 . DTY D 2 2   ? 15.527 16.882  21.884 1.00 15.63 ? 1   DTY D CD1 1 
HETATM 2735 C CD2 . DTY D 2 2   ? 16.731 18.088  20.225 1.00 14.35 ? 1   DTY D CD2 1 
HETATM 2736 C CE1 . DTY D 2 2   ? 16.598 16.019  22.045 1.00 16.06 ? 1   DTY D CE1 1 
HETATM 2737 C CE2 . DTY D 2 2   ? 17.814 17.238  20.381 1.00 14.69 ? 1   DTY D CE2 1 
HETATM 2738 C CZ  . DTY D 2 2   ? 17.744 16.194  21.287 1.00 15.40 ? 1   DTY D CZ  1 
HETATM 2739 O OH  . DTY D 2 2   ? 18.811 15.339  21.443 1.00 15.99 ? 1   DTY D OH  1 
ATOM   2740 N N   . GLN D 2 3   ? 16.422 20.679  22.779 1.00 16.05 ? 2   GLN D N   1 
ATOM   2741 C CA  . GLN D 2 3   ? 16.940 20.780  24.148 1.00 16.83 ? 2   GLN D CA  1 
ATOM   2742 C C   . GLN D 2 3   ? 16.963 22.232  24.612 1.00 17.05 ? 2   GLN D C   1 
ATOM   2743 O O   . GLN D 2 3   ? 17.324 23.129  23.858 1.00 16.36 ? 2   GLN D O   1 
ATOM   2744 C CB  . GLN D 2 3   ? 18.338 20.172  24.250 1.00 17.25 ? 2   GLN D CB  1 
ATOM   2745 C CG  . GLN D 2 3   ? 18.389 18.667  23.919 1.00 17.28 ? 2   GLN D CG  1 
ATOM   2746 C CD  . GLN D 2 3   ? 19.787 18.090  24.070 1.00 19.69 ? 2   GLN D CD  1 
ATOM   2747 O OE1 . GLN D 2 3   ? 20.768 18.711  23.671 1.00 21.87 ? 2   GLN D OE1 1 
ATOM   2748 N NE2 . GLN D 2 3   ? 19.884 16.916  24.686 1.00 23.21 ? 2   GLN D NE2 1 
ATOM   2749 N N   . PHE D 2 4   ? 16.556 22.455  25.858 1.00 18.18 ? 3   PHE D N   1 
ATOM   2750 C CA  . PHE D 2 4   ? 16.525 23.788  26.444 1.00 18.59 ? 3   PHE D CA  1 
ATOM   2751 C C   . PHE D 2 4   ? 16.189 23.629  27.916 1.00 20.85 ? 3   PHE D C   1 
ATOM   2752 O O   . PHE D 2 4   ? 15.490 22.688  28.293 1.00 20.69 ? 3   PHE D O   1 
ATOM   2753 C CB  . PHE D 2 4   ? 15.482 24.685  25.755 1.00 17.79 ? 3   PHE D CB  1 
ATOM   2754 C CG  . PHE D 2 4   ? 14.071 24.137  25.823 1.00 18.21 ? 3   PHE D CG  1 
ATOM   2755 C CD1 . PHE D 2 4   ? 13.621 23.230  24.874 1.00 17.48 ? 3   PHE D CD1 1 
ATOM   2756 C CD2 . PHE D 2 4   ? 13.208 24.515  26.850 1.00 19.02 ? 3   PHE D CD2 1 
ATOM   2757 C CE1 . PHE D 2 4   ? 12.330 22.710  24.939 1.00 22.52 ? 3   PHE D CE1 1 
ATOM   2758 C CE2 . PHE D 2 4   ? 11.916 24.006  26.929 1.00 22.52 ? 3   PHE D CE2 1 
ATOM   2759 C CZ  . PHE D 2 4   ? 11.474 23.097  25.967 1.00 25.11 ? 3   PHE D CZ  1 
ATOM   2760 N N   . GLU D 2 5   ? 16.705 24.542  28.736 1.00 24.53 ? 4   GLU D N   1 
ATOM   2761 C CA  . GLU D 2 5   ? 16.288 24.644  30.129 1.00 28.18 ? 4   GLU D CA  1 
ATOM   2762 C C   . GLU D 2 5   ? 14.984 25.426  30.218 1.00 26.09 ? 4   GLU D C   1 
ATOM   2763 O O   . GLU D 2 5   ? 14.672 26.236  29.346 1.00 24.07 ? 4   GLU D O   1 
ATOM   2764 C CB  . GLU D 2 5   ? 17.366 25.334  30.960 1.00 27.87 ? 4   GLU D CB  1 
ATOM   2765 C CG  . GLU D 2 5   ? 18.755 24.763  30.762 1.00 29.85 ? 4   GLU D CG  1 
ATOM   2766 C CD  . GLU D 2 5   ? 19.178 23.866  31.897 1.00 55.07 ? 4   GLU D CD  1 
ATOM   2767 O OE1 . GLU D 2 5   ? 18.520 23.905  32.961 1.00 58.93 ? 4   GLU D OE1 1 
ATOM   2768 O OE2 . GLU D 2 5   ? 20.169 23.124  31.728 1.00 66.72 ? 4   GLU D OE2 1 
ATOM   2769 N N   . GLN D 2 6   ? 14.222 25.196  31.297 1.00 27.36 ? 5   GLN D N   1 
ATOM   2770 C CA  . GLN D 2 6   ? 12.892 25.801  31.368 1.00 31.95 ? 5   GLN D CA  1 
ATOM   2771 C C   . GLN D 2 6   ? 12.937 27.324  31.496 1.00 29.15 ? 5   GLN D C   1 
ATOM   2772 O O   . GLN D 2 6   ? 11.945 27.990  31.171 1.00 30.00 ? 5   GLN D O   1 
ATOM   2773 C CB  . GLN D 2 6   ? 12.094 25.176  32.516 1.00 38.93 ? 5   GLN D CB  1 
ATOM   2774 C CG  . GLN D 2 6   ? 11.823 23.692  32.275 1.00 52.62 ? 5   GLN D CG  1 
ATOM   2775 C CD  . GLN D 2 6   ? 10.598 23.181  33.004 1.00 58.75 ? 5   GLN D CD  1 
ATOM   2776 O OE1 . GLN D 2 6   ? 9.532  23.017  32.406 1.00 61.88 ? 5   GLN D OE1 1 
ATOM   2777 N NE2 . GLN D 2 6   ? 10.745 22.913  34.299 1.00 56.69 ? 5   GLN D NE2 1 
ATOM   2778 N N   . TRP D 2 7   ? 14.061 27.892  31.928 1.00 24.23 ? 6   TRP D N   1 
ATOM   2779 C CA  . TRP D 2 7   ? 14.233 29.339  31.986 1.00 24.22 ? 6   TRP D CA  1 
ATOM   2780 C C   . TRP D 2 7   ? 14.863 29.924  30.720 1.00 26.87 ? 6   TRP D C   1 
ATOM   2781 O O   . TRP D 2 7   ? 14.991 31.150  30.622 1.00 22.76 ? 6   TRP D O   1 
ATOM   2782 C CB  . TRP D 2 7   ? 15.080 29.719  33.215 1.00 27.54 ? 6   TRP D CB  1 
ATOM   2783 C CG  . TRP D 2 7   ? 16.449 29.109  33.169 1.00 28.78 ? 6   TRP D CG  1 
ATOM   2784 C CD1 . TRP D 2 7   ? 16.815 27.874  33.623 1.00 30.52 ? 6   TRP D CD1 1 
ATOM   2785 C CD2 . TRP D 2 7   ? 17.631 29.702  32.621 1.00 25.27 ? 6   TRP D CD2 1 
ATOM   2786 N NE1 . TRP D 2 7   ? 18.155 27.662  33.388 1.00 30.69 ? 6   TRP D NE1 1 
ATOM   2787 C CE2 . TRP D 2 7   ? 18.677 28.770  32.773 1.00 28.72 ? 6   TRP D CE2 1 
ATOM   2788 C CE3 . TRP D 2 7   ? 17.905 30.929  32.009 1.00 31.79 ? 6   TRP D CE3 1 
ATOM   2789 C CZ2 . TRP D 2 7   ? 19.975 29.025  32.334 1.00 30.23 ? 6   TRP D CZ2 1 
ATOM   2790 C CZ3 . TRP D 2 7   ? 19.192 31.179  31.570 1.00 34.93 ? 6   TRP D CZ3 1 
ATOM   2791 C CH2 . TRP D 2 7   ? 20.210 30.227  31.730 1.00 32.15 ? 6   TRP D CH2 1 
ATOM   2792 N N   . HIS D 2 8   ? 15.247 29.090  29.748 1.00 22.18 ? 7   HIS D N   1 
ATOM   2793 C CA  . HIS D 2 8   ? 15.854 29.584  28.518 1.00 20.81 ? 7   HIS D CA  1 
ATOM   2794 C C   . HIS D 2 8   ? 14.837 30.335  27.660 1.00 22.14 ? 7   HIS D C   1 
ATOM   2795 O O   . HIS D 2 8   ? 13.628 30.099  27.717 1.00 21.53 ? 7   HIS D O   1 
ATOM   2796 C CB  . HIS D 2 8   ? 16.438 28.442  27.673 1.00 20.48 ? 7   HIS D CB  1 
ATOM   2797 C CG  . HIS D 2 8   ? 17.783 27.962  28.130 1.00 25.28 ? 7   HIS D CG  1 
ATOM   2798 N ND1 . HIS D 2 8   ? 18.463 26.939  27.498 1.00 20.85 ? 7   HIS D ND1 1 
ATOM   2799 C CD2 . HIS D 2 8   ? 18.576 28.369  29.149 1.00 22.59 ? 7   HIS D CD2 1 
ATOM   2800 C CE1 . HIS D 2 8   ? 19.619 26.742  28.105 1.00 25.19 ? 7   HIS D CE1 1 
ATOM   2801 N NE2 . HIS D 2 8   ? 19.710 27.592  29.114 1.00 26.59 ? 7   HIS D NE2 1 
ATOM   2802 N N   . ILE D 2 9   ? 15.365 31.224  26.820 1.00 19.20 ? 8   ILE D N   1 
ATOM   2803 C CA  . ILE D 2 9   ? 14.536 31.943  25.855 1.00 19.76 ? 8   ILE D CA  1 
ATOM   2804 C C   . ILE D 2 9   ? 13.786 30.968  24.948 1.00 20.48 ? 8   ILE D C   1 
ATOM   2805 O O   . ILE D 2 9   ? 12.591 31.136  24.679 1.00 19.88 ? 8   ILE D O   1 
ATOM   2806 C CB  . ILE D 2 9   ? 15.408 32.897  25.027 1.00 18.29 ? 8   ILE D CB  1 
ATOM   2807 C CG1 . ILE D 2 9   ? 16.035 33.963  25.922 1.00 22.19 ? 8   ILE D CG1 1 
ATOM   2808 C CG2 . ILE D 2 9   ? 14.580 33.522  23.933 1.00 18.87 ? 8   ILE D CG2 1 
ATOM   2809 C CD1 . ILE D 2 9   ? 17.214 34.672  25.267 1.00 23.32 ? 8   ILE D CD1 1 
ATOM   2810 N N   . ARG D 2 10  ? 14.490 29.945  24.449 1.00 17.07 ? 9   ARG D N   1 
ATOM   2811 C CA  . ARG D 2 10  ? 13.871 28.932  23.592 1.00 16.29 ? 9   ARG D CA  1 
ATOM   2812 C C   . ARG D 2 10  ? 12.667 28.274  24.266 1.00 20.02 ? 9   ARG D C   1 
ATOM   2813 O O   . ARG D 2 10  ? 11.725 27.857  23.583 1.00 18.72 ? 9   ARG D O   1 
ATOM   2814 C CB  . ARG D 2 10  ? 14.929 27.887  23.198 1.00 19.03 ? 9   ARG D CB  1 
ATOM   2815 C CG  . ARG D 2 10  ? 14.407 26.645  22.481 1.00 19.29 ? 9   ARG D CG  1 
ATOM   2816 C CD  . ARG D 2 10  ? 15.484 25.986  21.602 1.00 20.75 ? 9   ARG D CD  1 
ATOM   2817 N NE  . ARG D 2 10  ? 15.636 26.718  20.347 1.00 21.58 ? 9   ARG D NE  1 
ATOM   2818 C CZ  . ARG D 2 10  ? 16.334 26.297  19.301 1.00 22.23 ? 9   ARG D CZ  1 
ATOM   2819 N NH1 . ARG D 2 10  ? 17.039 25.178  19.348 1.00 16.05 ? 9   ARG D NH1 1 
ATOM   2820 N NH2 . ARG D 2 10  ? 16.314 27.013  18.174 1.00 16.70 ? 9   ARG D NH2 1 
ATOM   2821 N N   . GLY D 2 11  ? 12.657 28.197  25.598 1.00 20.87 ? 10  GLY D N   1 
ATOM   2822 C CA  . GLY D 2 11  ? 11.514 27.609  26.280 1.00 21.51 ? 10  GLY D CA  1 
ATOM   2823 C C   . GLY D 2 11  ? 10.231 28.406  26.153 1.00 21.34 ? 10  GLY D C   1 
ATOM   2824 O O   . GLY D 2 11  ? 9.153  27.863  26.423 1.00 24.85 ? 10  GLY D O   1 
ATOM   2825 N N   . ARG D 2 12  ? 10.316 29.658  25.724 1.00 18.70 ? 11  ARG D N   1 
ATOM   2826 C CA  . ARG D 2 12  ? 9.144  30.518  25.636 1.00 22.55 ? 11  ARG D CA  1 
ATOM   2827 C C   . ARG D 2 12  ? 8.400  30.390  24.322 1.00 20.14 ? 11  ARG D C   1 
ATOM   2828 O O   . ARG D 2 12  ? 7.293  30.921  24.199 1.00 19.90 ? 11  ARG D O   1 
ATOM   2829 C CB  . ARG D 2 12  ? 9.547  31.982  25.836 1.00 23.12 ? 11  ARG D CB  1 
ATOM   2830 C CG  . ARG D 2 12  ? 9.994  32.271  27.252 1.00 28.86 ? 11  ARG D CG  1 
ATOM   2831 C CD  . ARG D 2 12  ? 9.953  33.743  27.577 1.00 38.70 ? 11  ARG D CD  1 
ATOM   2832 N NE  . ARG D 2 12  ? 11.259 34.367  27.422 1.00 41.98 ? 11  ARG D NE  1 
ATOM   2833 C CZ  . ARG D 2 12  ? 11.561 35.234  26.468 1.00 38.24 ? 11  ARG D CZ  1 
ATOM   2834 N NH1 . ARG D 2 12  ? 10.662 35.621  25.577 1.00 34.35 ? 11  ARG D NH1 1 
ATOM   2835 N NH2 . ARG D 2 12  ? 12.794 35.731  26.412 1.00 36.43 ? 11  ARG D NH2 1 
ATOM   2836 N N   . TYR D 2 13  ? 8.956  29.672  23.357 1.00 18.71 ? 12  TYR D N   1 
ATOM   2837 C CA  . TYR D 2 13  ? 8.518  29.764  21.969 1.00 17.96 ? 12  TYR D CA  1 
ATOM   2838 C C   . TYR D 2 13  ? 8.085  28.366  21.528 1.00 16.46 ? 12  TYR D C   1 
ATOM   2839 O O   . TYR D 2 13  ? 7.578  27.603  22.357 1.00 19.17 ? 12  TYR D O   1 
ATOM   2840 C CB  . TYR D 2 13  ? 9.616  30.383  21.093 1.00 16.03 ? 12  TYR D CB  1 
ATOM   2841 C CG  . TYR D 2 13  ? 10.016 31.807  21.507 1.00 21.26 ? 12  TYR D CG  1 
ATOM   2842 C CD1 . TYR D 2 13  ? 9.071  32.709  21.996 1.00 19.29 ? 12  TYR D CD1 1 
ATOM   2843 C CD2 . TYR D 2 13  ? 11.335 32.244  21.398 1.00 19.98 ? 12  TYR D CD2 1 
ATOM   2844 C CE1 . TYR D 2 13  ? 9.432  34.004  22.377 1.00 21.46 ? 12  TYR D CE1 1 
ATOM   2845 C CE2 . TYR D 2 13  ? 11.702 33.536  21.773 1.00 18.23 ? 12  TYR D CE2 1 
ATOM   2846 C CZ  . TYR D 2 13  ? 10.747 34.408  22.256 1.00 21.64 ? 12  TYR D CZ  1 
ATOM   2847 O OH  . TYR D 2 13  ? 11.116 35.681  22.624 1.00 21.18 ? 12  TYR D OH  1 
ATOM   2848 N N   . ALA D 2 14  ? 8.141  28.068  20.224 1.00 16.89 ? 13  ALA D N   1 
ATOM   2849 C CA  . ALA D 2 14  ? 7.538  26.841  19.700 1.00 21.61 ? 13  ALA D CA  1 
ATOM   2850 C C   . ALA D 2 14  ? 8.026  25.576  20.398 1.00 22.38 ? 13  ALA D C   1 
ATOM   2851 O O   . ALA D 2 14  ? 7.294  24.578  20.436 1.00 20.92 ? 13  ALA D O   1 
ATOM   2852 C CB  . ALA D 2 14  ? 7.806  26.715  18.196 1.00 15.32 ? 13  ALA D CB  1 
ATOM   2853 N N   . CYS D 2 15  ? 9.249  25.571  20.932 1.00 17.43 ? 14  CYS D N   1 
ATOM   2854 C CA  . CYS D 2 15  ? 9.776  24.358  21.569 1.00 21.75 ? 14  CYS D CA  1 
ATOM   2855 C C   . CYS D 2 15  ? 9.136  24.070  22.916 1.00 24.44 ? 14  CYS D C   1 
ATOM   2856 O O   . CYS D 2 15  ? 8.538  24.942  23.557 1.00 27.63 ? 14  CYS D O   1 
ATOM   2857 C CB  . CYS D 2 15  ? 11.288 24.450  21.755 1.00 17.62 ? 14  CYS D CB  1 
ATOM   2858 S SG  . CYS D 2 15  ? 12.161 24.486  20.196 1.00 20.05 ? 14  CYS D SG  1 
ATOM   2859 O OXT . CYS D 2 15  ? 9.237  22.941  23.388 1.00 20.71 ? 14  CYS D OXT 1 
HETATM 2860 O O   . HOH E 3 .   ? 1.550  41.881  -1.737 1.00 40.04 ? 301 HOH A O   1 
HETATM 2861 O O   . HOH E 3 .   ? 5.964  33.651  20.607 1.00 33.12 ? 302 HOH A O   1 
HETATM 2862 O O   . HOH E 3 .   ? 20.287 30.190  9.630  1.00 15.09 ? 303 HOH A O   1 
HETATM 2863 O O   . HOH E 3 .   ? 11.258 27.550  20.881 1.00 19.20 ? 304 HOH A O   1 
HETATM 2864 O O   . HOH E 3 .   ? 22.118 45.163  29.210 1.00 35.32 ? 305 HOH A O   1 
HETATM 2865 O O   . HOH E 3 .   ? 19.970 45.890  5.738  1.00 26.54 ? 306 HOH A O   1 
HETATM 2866 O O   . HOH E 3 .   ? 27.467 41.772  15.452 1.00 40.10 ? 307 HOH A O   1 
HETATM 2867 O O   . HOH E 3 .   ? 31.065 39.435  9.326  1.00 31.11 ? 308 HOH A O   1 
HETATM 2868 O O   . HOH E 3 .   ? 12.251 52.321  6.916  1.00 31.79 ? 309 HOH A O   1 
HETATM 2869 O O   . HOH E 3 .   ? 10.427 29.178  18.045 1.00 20.29 ? 310 HOH A O   1 
HETATM 2870 O O   . HOH E 3 .   ? 20.497 23.618  19.726 1.00 17.80 ? 311 HOH A O   1 
HETATM 2871 O O   . HOH E 3 .   ? 36.727 29.464  7.698  1.00 25.53 ? 312 HOH A O   1 
HETATM 2872 O O   . HOH E 3 .   ? 18.528 16.152  3.295  1.00 16.93 ? 313 HOH A O   1 
HETATM 2873 O O   . HOH E 3 .   ? 22.455 24.217  17.007 1.00 30.06 ? 314 HOH A O   1 
HETATM 2874 O O   . HOH E 3 .   ? 19.408 21.452  -0.751 1.00 30.78 ? 315 HOH A O   1 
HETATM 2875 O O   . HOH E 3 .   ? 25.575 46.617  13.544 1.00 27.75 ? 316 HOH A O   1 
HETATM 2876 O O   . HOH E 3 .   ? 21.764 15.107  1.575  1.00 33.99 ? 317 HOH A O   1 
HETATM 2877 O O   . HOH E 3 .   ? 14.297 15.664  5.501  1.00 20.89 ? 318 HOH A O   1 
HETATM 2878 O O   . HOH E 3 .   ? 20.938 33.754  29.552 1.00 27.32 ? 319 HOH A O   1 
HETATM 2879 O O   . HOH E 3 .   ? 4.681  33.149  15.977 1.00 37.97 ? 320 HOH A O   1 
HETATM 2880 O O   . HOH E 3 .   ? 41.705 25.937  9.720  1.00 35.43 ? 321 HOH A O   1 
HETATM 2881 O O   . HOH E 3 .   ? 8.282  48.494  4.087  1.00 28.49 ? 322 HOH A O   1 
HETATM 2882 O O   . HOH E 3 .   ? 12.929 39.678  27.165 1.00 38.48 ? 323 HOH A O   1 
HETATM 2883 O O   . HOH E 3 .   ? 17.462 29.753  24.534 1.00 18.12 ? 324 HOH A O   1 
HETATM 2884 O O   . HOH E 3 .   ? 21.050 29.436  -3.118 1.00 33.18 ? 325 HOH A O   1 
HETATM 2885 O O   . HOH E 3 .   ? 17.598 19.551  -4.115 1.00 38.64 ? 326 HOH A O   1 
HETATM 2886 O O   . HOH E 3 .   ? -0.706 40.200  7.596  1.00 24.72 ? 327 HOH A O   1 
HETATM 2887 O O   . HOH E 3 .   ? 18.500 39.601  25.317 1.00 19.56 ? 328 HOH A O   1 
HETATM 2888 O O   . HOH E 3 .   ? 23.694 27.984  17.020 1.00 39.48 ? 329 HOH A O   1 
HETATM 2889 O O   . HOH E 3 .   ? 9.990  34.033  12.251 1.00 16.21 ? 330 HOH A O   1 
HETATM 2890 O O   . HOH E 3 .   ? 13.893 34.556  9.696  1.00 15.79 ? 331 HOH A O   1 
HETATM 2891 O O   . HOH E 3 .   ? 28.297 27.343  14.418 1.00 47.06 ? 332 HOH A O   1 
HETATM 2892 O O   . HOH E 3 .   ? 16.406 13.075  2.115  1.00 30.87 ? 333 HOH A O   1 
HETATM 2893 O O   . HOH E 3 .   ? 11.544 18.077  2.410  1.00 18.46 ? 334 HOH A O   1 
HETATM 2894 O O   . HOH E 3 .   ? 19.261 47.612  1.346  1.00 28.93 ? 335 HOH A O   1 
HETATM 2895 O O   . HOH E 3 .   ? 16.735 11.135  5.074  1.00 21.14 ? 336 HOH A O   1 
HETATM 2896 O O   . HOH E 3 .   ? 33.176 27.872  7.612  1.00 20.26 ? 337 HOH A O   1 
HETATM 2897 O O   . HOH E 3 .   ? 13.639 37.693  24.557 1.00 28.94 ? 338 HOH A O   1 
HETATM 2898 O O   . HOH E 3 .   ? -1.914 40.223  3.938  1.00 19.03 ? 339 HOH A O   1 
HETATM 2899 O O   . HOH E 3 .   ? 6.096  31.899  6.630  1.00 22.12 ? 340 HOH A O   1 
HETATM 2900 O O   . HOH E 3 .   ? 21.270 8.819   1.862  1.00 20.91 ? 341 HOH A O   1 
HETATM 2901 O O   . HOH E 3 .   ? 36.132 16.983  17.227 1.00 22.09 ? 342 HOH A O   1 
HETATM 2902 O O   . HOH E 3 .   ? 16.665 33.219  29.558 1.00 20.11 ? 343 HOH A O   1 
HETATM 2903 O O   . HOH E 3 .   ? 6.569  25.392  3.005  1.00 32.62 ? 344 HOH A O   1 
HETATM 2904 O O   . HOH E 3 .   ? 7.823  24.230  7.814  1.00 21.64 ? 345 HOH A O   1 
HETATM 2905 O O   . HOH E 3 .   ? 18.046 35.990  -4.505 1.00 24.92 ? 346 HOH A O   1 
HETATM 2906 O O   . HOH E 3 .   ? 22.454 46.609  17.269 1.00 28.44 ? 347 HOH A O   1 
HETATM 2907 O O   . HOH E 3 .   ? 31.160 15.561  6.131  1.00 22.56 ? 348 HOH A O   1 
HETATM 2908 O O   . HOH E 3 .   ? 13.685 47.917  22.776 1.00 30.32 ? 349 HOH A O   1 
HETATM 2909 O O   . HOH E 3 .   ? 10.241 49.399  19.605 1.00 40.56 ? 350 HOH A O   1 
HETATM 2910 O O   . HOH E 3 .   ? 19.456 40.018  1.149  1.00 22.73 ? 351 HOH A O   1 
HETATM 2911 O O   . HOH E 3 .   ? 26.542 19.829  3.618  1.00 24.49 ? 352 HOH A O   1 
HETATM 2912 O O   . HOH E 3 .   ? 40.402 30.189  9.066  1.00 38.62 ? 353 HOH A O   1 
HETATM 2913 O O   . HOH E 3 .   ? 37.294 20.405  9.071  1.00 35.64 ? 354 HOH A O   1 
HETATM 2914 O O   . HOH E 3 .   ? 23.000 41.408  15.147 1.00 31.76 ? 355 HOH A O   1 
HETATM 2915 O O   . HOH E 3 .   ? 23.511 24.670  14.708 1.00 36.04 ? 356 HOH A O   1 
HETATM 2916 O O   . HOH E 3 .   ? 25.392 38.670  15.466 1.00 27.32 ? 357 HOH A O   1 
HETATM 2917 O O   . HOH E 3 .   ? 27.521 31.446  15.029 1.00 40.01 ? 358 HOH A O   1 
HETATM 2918 O O   . HOH E 3 .   ? 31.068 9.708   6.769  1.00 21.08 ? 359 HOH A O   1 
HETATM 2919 O O   . HOH E 3 .   ? 14.675 46.722  1.330  1.00 35.97 ? 360 HOH A O   1 
HETATM 2920 O O   . HOH E 3 .   ? 1.239  41.981  10.439 1.00 28.45 ? 361 HOH A O   1 
HETATM 2921 O O   . HOH E 3 .   ? 13.161 43.306  3.073  1.00 13.42 ? 362 HOH A O   1 
HETATM 2922 O O   . HOH E 3 .   ? 28.539 21.204  18.545 1.00 29.67 ? 363 HOH A O   1 
HETATM 2923 O O   . HOH E 3 .   ? 30.854 21.722  3.310  1.00 29.40 ? 364 HOH A O   1 
HETATM 2924 O O   . HOH E 3 .   ? 8.770  28.629  1.596  1.00 28.23 ? 365 HOH A O   1 
HETATM 2925 O O   . HOH E 3 .   ? 26.782 33.565  3.372  1.00 30.82 ? 366 HOH A O   1 
HETATM 2926 O O   . HOH E 3 .   ? 36.778 27.849  14.199 1.00 27.12 ? 367 HOH A O   1 
HETATM 2927 O O   . HOH E 3 .   ? 12.456 44.321  -2.868 1.00 34.40 ? 368 HOH A O   1 
HETATM 2928 O O   . HOH E 3 .   ? 25.403 31.226  3.288  1.00 29.49 ? 369 HOH A O   1 
HETATM 2929 O O   . HOH E 3 .   ? 3.131  35.763  11.647 1.00 33.80 ? 370 HOH A O   1 
HETATM 2930 O O   . HOH E 3 .   ? 6.312  43.565  18.294 1.00 35.97 ? 371 HOH A O   1 
HETATM 2931 O O   . HOH E 3 .   ? 22.085 16.745  18.172 1.00 18.25 ? 372 HOH A O   1 
HETATM 2932 O O   . HOH E 3 .   ? 8.463  29.907  -5.822 1.00 25.46 ? 373 HOH A O   1 
HETATM 2933 O O   . HOH E 3 .   ? 23.941 36.009  18.385 1.00 28.35 ? 374 HOH A O   1 
HETATM 2934 O O   . HOH E 3 .   ? -1.165 47.291  4.806  1.00 21.08 ? 375 HOH A O   1 
HETATM 2935 O O   . HOH E 3 .   ? 0.915  37.299  -1.961 1.00 31.81 ? 376 HOH A O   1 
HETATM 2936 O O   . HOH E 3 .   ? 35.198 18.659  10.706 1.00 27.20 ? 377 HOH A O   1 
HETATM 2937 O O   . HOH E 3 .   ? 24.972 33.049  -1.156 1.00 34.95 ? 378 HOH A O   1 
HETATM 2938 O O   . HOH E 3 .   ? 24.247 45.676  20.953 1.00 40.72 ? 379 HOH A O   1 
HETATM 2939 O O   . HOH E 3 .   ? 24.369 44.764  6.918  1.00 38.38 ? 380 HOH A O   1 
HETATM 2940 O O   . HOH E 3 .   ? 28.570 34.149  14.639 1.00 26.00 ? 381 HOH A O   1 
HETATM 2941 O O   . HOH E 3 .   ? 20.535 49.103  29.847 1.00 38.52 ? 382 HOH A O   1 
HETATM 2942 O O   . HOH E 3 .   ? 32.025 10.811  11.529 1.00 28.03 ? 383 HOH A O   1 
HETATM 2943 O O   . HOH E 3 .   ? 24.006 34.150  16.107 1.00 21.59 ? 384 HOH A O   1 
HETATM 2944 O O   . HOH E 3 .   ? 8.225  37.570  16.337 1.00 16.33 ? 385 HOH A O   1 
HETATM 2945 O O   . HOH E 3 .   ? 2.306  34.750  4.772  1.00 23.73 ? 386 HOH A O   1 
HETATM 2946 O O   . HOH E 3 .   ? 27.282 24.193  18.288 1.00 36.26 ? 387 HOH A O   1 
HETATM 2947 O O   . HOH E 3 .   ? 21.295 44.714  3.625  1.00 36.46 ? 388 HOH A O   1 
HETATM 2948 O O   . HOH E 3 .   ? 17.882 23.873  -1.839 1.00 26.97 ? 389 HOH A O   1 
HETATM 2949 O O   . HOH E 3 .   ? 21.697 46.964  24.863 1.00 39.27 ? 390 HOH A O   1 
HETATM 2950 O O   . HOH E 3 .   ? 13.049 44.129  -0.448 1.00 24.40 ? 391 HOH A O   1 
HETATM 2951 O O   . HOH E 3 .   ? 19.007 33.014  -9.934 1.00 25.75 ? 392 HOH A O   1 
HETATM 2952 O O   . HOH E 3 .   ? 29.856 29.342  5.298  1.00 32.55 ? 393 HOH A O   1 
HETATM 2953 O O   . HOH E 3 .   ? 7.480  49.533  6.230  1.00 30.09 ? 394 HOH A O   1 
HETATM 2954 O O   . HOH E 3 .   ? 7.778  36.936  20.837 1.00 24.62 ? 395 HOH A O   1 
HETATM 2955 O O   . HOH E 3 .   ? 4.724  35.600  9.387  1.00 20.77 ? 396 HOH A O   1 
HETATM 2956 O O   . HOH E 3 .   ? 27.932 36.894  15.976 1.00 37.91 ? 397 HOH A O   1 
HETATM 2957 O O   . HOH E 3 .   ? 12.473 36.285  -7.957 1.00 35.65 ? 398 HOH A O   1 
HETATM 2958 O O   . HOH E 3 .   ? 3.390  32.793  2.928  1.00 43.74 ? 399 HOH A O   1 
HETATM 2959 O O   . HOH E 3 .   ? 7.775  21.626  0.470  1.00 38.07 ? 400 HOH A O   1 
HETATM 2960 O O   . HOH E 3 .   ? 1.406  49.094  10.904 1.00 38.44 ? 401 HOH A O   1 
HETATM 2961 O O   . HOH E 3 .   ? 1.937  46.786  1.064  1.00 34.12 ? 402 HOH A O   1 
HETATM 2962 O O   . HOH E 3 .   ? 26.273 25.869  14.985 1.00 43.80 ? 403 HOH A O   1 
HETATM 2963 O O   . HOH E 3 .   ? 12.633 50.694  3.921  1.00 33.09 ? 404 HOH A O   1 
HETATM 2964 O O   . HOH E 3 .   ? 27.351 36.558  4.171  1.00 35.01 ? 405 HOH A O   1 
HETATM 2965 O O   . HOH E 3 .   ? 22.984 2.493   1.308  1.00 36.51 ? 406 HOH A O   1 
HETATM 2966 O O   . HOH E 3 .   ? 28.375 21.205  2.191  1.00 31.52 ? 407 HOH A O   1 
HETATM 2967 O O   . HOH E 3 .   ? 12.460 39.643  -5.557 1.00 36.32 ? 408 HOH A O   1 
HETATM 2968 O O   . HOH E 3 .   ? 13.684 16.135  2.937  1.00 27.53 ? 409 HOH A O   1 
HETATM 2969 O O   . HOH E 3 .   ? 6.003  24.177  5.199  1.00 33.86 ? 410 HOH A O   1 
HETATM 2970 O O   . HOH E 3 .   ? 27.486 29.182  3.828  1.00 33.28 ? 411 HOH A O   1 
HETATM 2971 O O   . HOH E 3 .   ? 21.833 31.224  -5.191 1.00 30.81 ? 412 HOH A O   1 
HETATM 2972 O O   . HOH E 3 .   ? 37.374 17.605  11.240 1.00 34.35 ? 413 HOH A O   1 
HETATM 2973 O O   . HOH E 3 .   ? -2.913 41.886  1.930  1.00 29.52 ? 414 HOH A O   1 
HETATM 2974 O O   . HOH E 3 .   ? 33.297 27.859  4.836  1.00 32.05 ? 415 HOH A O   1 
HETATM 2975 O O   . HOH E 3 .   ? 24.551 20.509  25.228 1.00 29.33 ? 416 HOH A O   1 
HETATM 2976 O O   . HOH E 3 .   ? -0.958 49.370  9.674  1.00 41.06 ? 417 HOH A O   1 
HETATM 2977 O O   . HOH E 3 .   ? 6.530  37.889  18.454 1.00 23.83 ? 418 HOH A O   1 
HETATM 2978 O O   . HOH F 3 .   ? 8.232  -12.581 0.066  1.00 27.00 ? 301 HOH B O   1 
HETATM 2979 O O   . HOH F 3 .   ? 23.230 -20.701 23.179 1.00 41.39 ? 302 HOH B O   1 
HETATM 2980 O O   . HOH F 3 .   ? 18.991 -8.961  22.477 1.00 29.62 ? 303 HOH B O   1 
HETATM 2981 O O   . HOH F 3 .   ? 18.316 5.099   18.806 1.00 27.98 ? 304 HOH B O   1 
HETATM 2982 O O   . HOH F 3 .   ? 4.532  8.425   5.223  1.00 36.93 ? 305 HOH B O   1 
HETATM 2983 O O   . HOH F 3 .   ? 8.804  2.242   25.011 1.00 29.51 ? 306 HOH B O   1 
HETATM 2984 O O   . HOH F 3 .   ? 7.927  9.349   6.610  1.00 32.98 ? 307 HOH B O   1 
HETATM 2985 O O   . HOH F 3 .   ? 27.884 0.002   9.083  1.00 23.11 ? 308 HOH B O   1 
HETATM 2986 O O   . HOH F 3 .   ? 8.865  -20.230 8.555  1.00 26.06 ? 309 HOH B O   1 
HETATM 2987 O O   . HOH F 3 .   ? 3.508  -8.478  -0.054 1.00 35.90 ? 310 HOH B O   1 
HETATM 2988 O O   . HOH F 3 .   ? 14.188 12.672  5.770  1.00 26.36 ? 311 HOH B O   1 
HETATM 2989 O O   . HOH F 3 .   ? 31.038 -15.220 24.708 1.00 28.87 ? 312 HOH B O   1 
HETATM 2990 O O   . HOH F 3 .   ? 24.619 6.406   18.191 1.00 20.88 ? 313 HOH B O   1 
HETATM 2991 O O   . HOH F 3 .   ? 28.791 -2.356  6.306  1.00 28.83 ? 314 HOH B O   1 
HETATM 2992 O O   . HOH F 3 .   ? 10.468 12.068  8.573  1.00 21.40 ? 315 HOH B O   1 
HETATM 2993 O O   . HOH F 3 .   ? 6.827  6.810   8.038  1.00 32.43 ? 316 HOH B O   1 
HETATM 2994 O O   . HOH F 3 .   ? 7.412  1.148   27.738 1.00 32.76 ? 317 HOH B O   1 
HETATM 2995 O O   . HOH F 3 .   ? 20.145 -10.928 21.120 1.00 31.00 ? 318 HOH B O   1 
HETATM 2996 O O   . HOH F 3 .   ? 26.989 6.425   17.045 1.00 18.34 ? 319 HOH B O   1 
HETATM 2997 O O   . HOH F 3 .   ? 7.314  25.862  13.496 1.00 28.88 ? 320 HOH B O   1 
HETATM 2998 O O   . HOH F 3 .   ? 9.895  -12.379 11.118 1.00 28.58 ? 321 HOH B O   1 
HETATM 2999 O O   . HOH F 3 .   ? 11.363 -19.331 10.547 1.00 29.89 ? 322 HOH B O   1 
HETATM 3000 O O   . HOH F 3 .   ? 7.306  13.285  10.755 1.00 29.62 ? 323 HOH B O   1 
HETATM 3001 O O   . HOH F 3 .   ? 27.611 7.400   24.528 1.00 26.42 ? 324 HOH B O   1 
HETATM 3002 O O   . HOH F 3 .   ? 12.582 17.035  7.309  1.00 20.09 ? 325 HOH B O   1 
HETATM 3003 O O   . HOH F 3 .   ? 15.883 -1.177  14.486 1.00 15.07 ? 326 HOH B O   1 
HETATM 3004 O O   . HOH F 3 .   ? 20.360 9.071   24.429 1.00 28.23 ? 327 HOH B O   1 
HETATM 3005 O O   . HOH F 3 .   ? 20.391 -4.286  20.947 1.00 23.45 ? 328 HOH B O   1 
HETATM 3006 O O   . HOH F 3 .   ? 24.955 10.802  23.987 1.00 36.30 ? 329 HOH B O   1 
HETATM 3007 O O   . HOH F 3 .   ? 25.649 -14.648 -0.879 1.00 25.95 ? 330 HOH B O   1 
HETATM 3008 O O   . HOH F 3 .   ? 19.163 -6.025  9.252  1.00 16.07 ? 331 HOH B O   1 
HETATM 3009 O O   . HOH F 3 .   ? 25.194 2.424   3.935  1.00 26.61 ? 332 HOH B O   1 
HETATM 3010 O O   . HOH F 3 .   ? 7.359  9.017   16.497 1.00 25.72 ? 333 HOH B O   1 
HETATM 3011 O O   . HOH F 3 .   ? 13.803 -9.553  -8.218 1.00 34.98 ? 334 HOH B O   1 
HETATM 3012 O O   . HOH F 3 .   ? 31.267 -9.298  20.817 1.00 22.46 ? 335 HOH B O   1 
HETATM 3013 O O   . HOH F 3 .   ? 20.037 5.830   21.796 1.00 38.68 ? 336 HOH B O   1 
HETATM 3014 O O   . HOH F 3 .   ? 23.039 -5.392  6.479  1.00 14.11 ? 337 HOH B O   1 
HETATM 3015 O O   . HOH F 3 .   ? 7.418  -4.658  17.671 1.00 37.02 ? 338 HOH B O   1 
HETATM 3016 O O   . HOH F 3 .   ? 27.672 9.321   21.311 1.00 22.64 ? 339 HOH B O   1 
HETATM 3017 O O   . HOH F 3 .   ? 4.551  -7.778  6.879  1.00 35.19 ? 340 HOH B O   1 
HETATM 3018 O O   . HOH F 3 .   ? 30.378 0.310   18.478 1.00 15.94 ? 341 HOH B O   1 
HETATM 3019 O O   . HOH F 3 .   ? 20.973 -22.778 6.132  1.00 27.73 ? 342 HOH B O   1 
HETATM 3020 O O   . HOH F 3 .   ? 11.049 18.772  26.152 1.00 23.52 ? 343 HOH B O   1 
HETATM 3021 O O   . HOH F 3 .   ? 5.235  7.568   20.545 1.00 34.54 ? 344 HOH B O   1 
HETATM 3022 O O   . HOH F 3 .   ? 32.398 -8.570  15.697 1.00 25.49 ? 345 HOH B O   1 
HETATM 3023 O O   . HOH F 3 .   ? 35.049 -13.781 17.133 1.00 34.23 ? 346 HOH B O   1 
HETATM 3024 O O   . HOH F 3 .   ? 7.594  13.785  21.290 1.00 24.95 ? 347 HOH B O   1 
HETATM 3025 O O   . HOH F 3 .   ? 7.621  19.378  9.652  1.00 18.81 ? 348 HOH B O   1 
HETATM 3026 O O   . HOH F 3 .   ? 13.783 -1.009  0.452  1.00 29.48 ? 349 HOH B O   1 
HETATM 3027 O O   . HOH F 3 .   ? 20.329 6.422   24.333 1.00 37.22 ? 350 HOH B O   1 
HETATM 3028 O O   . HOH F 3 .   ? 30.293 -20.085 17.641 1.00 33.93 ? 351 HOH B O   1 
HETATM 3029 O O   . HOH F 3 .   ? 19.327 -3.974  0.505  1.00 24.13 ? 352 HOH B O   1 
HETATM 3030 O O   . HOH F 3 .   ? 21.636 -18.920 22.280 1.00 26.46 ? 353 HOH B O   1 
HETATM 3031 O O   . HOH F 3 .   ? 28.841 -16.367 23.481 1.00 27.17 ? 354 HOH B O   1 
HETATM 3032 O O   . HOH F 3 .   ? 13.759 -15.423 6.498  1.00 18.48 ? 355 HOH B O   1 
HETATM 3033 O O   . HOH F 3 .   ? 8.122  -2.240  16.113 1.00 29.98 ? 356 HOH B O   1 
HETATM 3034 O O   . HOH F 3 .   ? 27.305 -5.490  26.101 1.00 29.01 ? 357 HOH B O   1 
HETATM 3035 O O   . HOH F 3 .   ? 4.508  1.394   0.315  1.00 36.23 ? 358 HOH B O   1 
HETATM 3036 O O   . HOH F 3 .   ? 11.210 -16.623 5.313  1.00 26.81 ? 359 HOH B O   1 
HETATM 3037 O O   . HOH F 3 .   ? 7.438  -3.182  -3.191 1.00 29.77 ? 360 HOH B O   1 
HETATM 3038 O O   . HOH F 3 .   ? 18.992 -0.503  18.312 1.00 25.52 ? 361 HOH B O   1 
HETATM 3039 O O   . HOH F 3 .   ? 27.921 -20.020 -2.468 1.00 41.93 ? 362 HOH B O   1 
HETATM 3040 O O   . HOH F 3 .   ? 9.970  14.732  5.846  1.00 26.79 ? 363 HOH B O   1 
HETATM 3041 O O   . HOH F 3 .   ? 14.084 -11.853 -7.039 1.00 21.18 ? 364 HOH B O   1 
HETATM 3042 O O   . HOH F 3 .   ? 6.785  7.905   0.541  1.00 37.90 ? 365 HOH B O   1 
HETATM 3043 O O   . HOH F 3 .   ? 22.415 -6.046  22.008 1.00 24.38 ? 366 HOH B O   1 
HETATM 3044 O O   . HOH F 3 .   ? 17.650 -5.707  -3.550 1.00 28.64 ? 367 HOH B O   1 
HETATM 3045 O O   . HOH F 3 .   ? 8.742  9.318   3.479  1.00 31.27 ? 368 HOH B O   1 
HETATM 3046 O O   . HOH F 3 .   ? 19.629 -21.674 3.655  1.00 29.59 ? 369 HOH B O   1 
HETATM 3047 O O   . HOH F 3 .   ? 13.459 -16.517 13.966 1.00 20.79 ? 370 HOH B O   1 
HETATM 3048 O O   . HOH F 3 .   ? 1.852  7.958   24.620 1.00 29.85 ? 371 HOH B O   1 
HETATM 3049 O O   . HOH F 3 .   ? 28.942 -13.726 0.130  1.00 42.33 ? 372 HOH B O   1 
HETATM 3050 O O   . HOH F 3 .   ? 27.401 -8.804  7.375  1.00 26.68 ? 373 HOH B O   1 
HETATM 3051 O O   . HOH F 3 .   ? 30.049 1.245   25.757 1.00 28.22 ? 374 HOH B O   1 
HETATM 3052 O O   . HOH F 3 .   ? 7.728  19.629  20.836 1.00 25.91 ? 375 HOH B O   1 
HETATM 3053 O O   . HOH F 3 .   ? 22.419 4.966   20.560 1.00 29.07 ? 376 HOH B O   1 
HETATM 3054 O O   . HOH F 3 .   ? 34.249 -10.069 22.133 1.00 28.05 ? 377 HOH B O   1 
HETATM 3055 O O   . HOH F 3 .   ? 30.631 -14.498 6.938  1.00 33.07 ? 378 HOH B O   1 
HETATM 3056 O O   . HOH F 3 .   ? 30.844 -18.309 15.722 1.00 32.32 ? 379 HOH B O   1 
HETATM 3057 O O   . HOH F 3 .   ? 31.684 -8.014  8.593  1.00 30.87 ? 380 HOH B O   1 
HETATM 3058 O O   . HOH F 3 .   ? 12.819 9.651   2.125  1.00 23.69 ? 381 HOH B O   1 
HETATM 3059 O O   . HOH F 3 .   ? 5.168  24.474  16.248 1.00 29.70 ? 382 HOH B O   1 
HETATM 3060 O O   . HOH F 3 .   ? 10.472 8.067   31.844 1.00 40.49 ? 383 HOH B O   1 
HETATM 3061 O O   . HOH F 3 .   ? 22.856 -7.926  0.794  1.00 27.75 ? 384 HOH B O   1 
HETATM 3062 O O   . HOH F 3 .   ? 8.337  19.512  26.111 1.00 40.54 ? 385 HOH B O   1 
HETATM 3063 O O   . HOH F 3 .   ? 28.044 -17.968 10.220 1.00 28.02 ? 386 HOH B O   1 
HETATM 3064 O O   . HOH F 3 .   ? 12.094 -9.649  24.966 1.00 34.26 ? 387 HOH B O   1 
HETATM 3065 O O   . HOH F 3 .   ? 21.189 6.299   19.057 1.00 38.40 ? 388 HOH B O   1 
HETATM 3066 O O   . HOH F 3 .   ? 19.397 -7.794  -3.456 1.00 22.38 ? 389 HOH B O   1 
HETATM 3067 O O   . HOH F 3 .   ? 13.141 4.445   29.875 1.00 29.38 ? 390 HOH B O   1 
HETATM 3068 O O   . HOH F 3 .   ? 19.577 3.746   1.491  1.00 26.79 ? 391 HOH B O   1 
HETATM 3069 O O   . HOH F 3 .   ? 15.779 2.286   -1.447 1.00 34.74 ? 392 HOH B O   1 
HETATM 3070 O O   . HOH F 3 .   ? 23.134 -23.224 9.074  1.00 26.83 ? 393 HOH B O   1 
HETATM 3071 O O   . HOH F 3 .   ? 6.776  -4.544  -8.180 1.00 42.72 ? 394 HOH B O   1 
HETATM 3072 O O   . HOH F 3 .   ? 31.102 -11.644 6.101  1.00 36.67 ? 395 HOH B O   1 
HETATM 3073 O O   . HOH F 3 .   ? 4.980  13.494  13.210 1.00 40.61 ? 396 HOH B O   1 
HETATM 3074 O O   . HOH F 3 .   ? 31.084 6.336   24.327 1.00 34.12 ? 397 HOH B O   1 
HETATM 3075 O O   . HOH F 3 .   ? 23.484 13.767  19.801 1.00 26.23 ? 398 HOH B O   1 
HETATM 3076 O O   . HOH F 3 .   ? 7.376  18.008  23.091 1.00 36.07 ? 399 HOH B O   1 
HETATM 3077 O O   . HOH F 3 .   ? 29.179 -18.946 22.858 1.00 30.68 ? 400 HOH B O   1 
HETATM 3078 O O   . HOH F 3 .   ? 5.492  10.164  13.109 1.00 41.54 ? 401 HOH B O   1 
HETATM 3079 O O   . HOH F 3 .   ? 30.190 -9.188  6.608  1.00 28.42 ? 402 HOH B O   1 
HETATM 3080 O O   . HOH F 3 .   ? 6.102  15.798  22.486 1.00 36.90 ? 403 HOH B O   1 
HETATM 3081 O O   . HOH F 3 .   ? 7.391  -0.059  17.706 1.00 35.40 ? 404 HOH B O   1 
HETATM 3082 O O   . HOH F 3 .   ? 10.072 11.481  5.879  1.00 29.72 ? 405 HOH B O   1 
HETATM 3083 O O   . HOH F 3 .   ? 35.870 -10.492 20.282 1.00 32.65 ? 406 HOH B O   1 
HETATM 3084 O O   . HOH F 3 .   ? 12.193 11.644  4.180  1.00 35.61 ? 407 HOH B O   1 
HETATM 3085 O O   . HOH F 3 .   ? 5.334  7.728   17.619 1.00 28.80 ? 408 HOH B O   1 
HETATM 3086 O O   . HOH F 3 .   ? 2.249  -6.901  8.417  1.00 41.86 ? 409 HOH B O   1 
HETATM 3087 O O   . HOH F 3 .   ? 20.236 6.310   0.879  1.00 40.05 ? 410 HOH B O   1 
HETATM 3088 O O   . HOH F 3 .   ? 24.840 -5.781  27.206 1.00 36.43 ? 411 HOH B O   1 
HETATM 3089 O O   . HOH F 3 .   ? 0.722  -7.573  0.339  1.00 37.79 ? 412 HOH B O   1 
HETATM 3090 O O   . HOH F 3 .   ? 7.380  -1.047  20.533 1.00 46.36 ? 413 HOH B O   1 
HETATM 3091 O O   . HOH F 3 .   ? 32.412 -9.420  18.140 1.00 31.66 ? 414 HOH B O   1 
HETATM 3092 O O   . HOH F 3 .   ? 6.261  -3.240  20.056 1.00 48.21 ? 415 HOH B O   1 
HETATM 3093 O O   . HOH G 3 .   ? 30.184 1.768   11.035 1.00 18.36 ? 101 HOH C O   1 
HETATM 3094 O O   . HOH G 3 .   ? 37.237 0.554   15.778 1.00 29.78 ? 102 HOH C O   1 
HETATM 3095 O O   . HOH G 3 .   ? 34.471 -6.921  12.770 1.00 39.73 ? 103 HOH C O   1 
HETATM 3096 O O   . HOH G 3 .   ? 38.561 7.231   20.545 1.00 33.57 ? 104 HOH C O   1 
HETATM 3097 O O   . HOH G 3 .   ? 32.053 3.776   24.981 1.00 26.57 ? 105 HOH C O   1 
HETATM 3098 O O   . HOH G 3 .   ? 29.756 2.967   19.031 1.00 16.10 ? 106 HOH C O   1 
HETATM 3099 O O   . HOH G 3 .   ? 32.044 8.653   20.719 1.00 24.57 ? 107 HOH C O   1 
HETATM 3100 O O   . HOH G 3 .   ? 23.693 14.970  16.699 1.00 26.63 ? 108 HOH C O   1 
HETATM 3101 O O   . HOH G 3 .   ? 36.504 4.347   10.791 1.00 37.98 ? 109 HOH C O   1 
HETATM 3102 O O   . HOH G 3 .   ? 37.217 5.943   24.678 1.00 32.59 ? 110 HOH C O   1 
HETATM 3103 O O   . HOH G 3 .   ? 36.960 8.359   16.897 1.00 34.69 ? 111 HOH C O   1 
HETATM 3104 O O   . HOH G 3 .   ? 31.133 8.565   10.429 1.00 20.72 ? 112 HOH C O   1 
HETATM 3105 O O   . HOH G 3 .   ? 25.772 13.195  21.247 1.00 26.16 ? 113 HOH C O   1 
HETATM 3106 O O   . HOH G 3 .   ? 28.862 14.629  21.893 1.00 29.34 ? 114 HOH C O   1 
HETATM 3107 O O   . HOH G 3 .   ? 32.493 7.341   6.528  1.00 35.20 ? 115 HOH C O   1 
HETATM 3108 O O   . HOH G 3 .   ? 32.717 10.369  18.937 1.00 29.03 ? 116 HOH C O   1 
HETATM 3109 O O   . HOH H 3 .   ? 11.718 30.070  29.325 1.00 28.06 ? 101 HOH D O   1 
HETATM 3110 O O   . HOH H 3 .   ? 14.184 33.024  32.206 1.00 36.60 ? 102 HOH D O   1 
HETATM 3111 O O   . HOH H 3 .   ? 22.171 20.914  23.973 1.00 22.79 ? 103 HOH D O   1 
HETATM 3112 O O   . HOH H 3 .   ? 18.333 23.601  21.424 1.00 19.69 ? 104 HOH D O   1 
HETATM 3113 O O   . HOH H 3 .   ? 11.876 18.947  23.674 1.00 16.16 ? 105 HOH D O   1 
HETATM 3114 O O   . HOH H 3 .   ? 9.181  22.049  36.360 1.00 35.41 ? 106 HOH D O   1 
HETATM 3115 O O   . HOH H 3 .   ? 18.458 27.063  24.700 1.00 21.34 ? 107 HOH D O   1 
HETATM 3116 O O   . HOH H 3 .   ? 10.565 20.862  22.004 1.00 23.30 ? 108 HOH D O   1 
HETATM 3117 O O   . HOH H 3 .   ? 23.042 17.117  22.714 1.00 25.88 ? 109 HOH D O   1 
HETATM 3118 O O   . HOH H 3 .   ? 8.078  25.053  26.503 1.00 30.12 ? 110 HOH D O   1 
HETATM 3119 O O   . HOH H 3 .   ? 21.725 15.701  20.689 1.00 21.66 ? 111 HOH D O   1 
HETATM 3120 O O   . HOH H 3 .   ? 22.665 16.187  25.865 1.00 35.73 ? 112 HOH D O   1 
HETATM 3121 O O   . HOH H 3 .   ? 24.880 15.937  24.051 1.00 42.26 ? 113 HOH D 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   . THR A 3   ? 0.7067 0.6653 0.5121 0.1073  -0.0051 0.0324  36  THR A N   
2    C CA  . THR A 3   ? 0.6302 0.5902 0.4549 0.0927  0.0006  0.0321  36  THR A CA  
3    C C   . THR A 3   ? 0.4893 0.4513 0.3394 0.0766  -0.0019 0.0291  36  THR A C   
4    O O   . THR A 3   ? 0.5444 0.5015 0.3995 0.0755  0.0015  0.0348  36  THR A O   
5    C CB  . THR A 3   ? 0.5408 0.4931 0.3639 0.0951  0.0182  0.0462  36  THR A CB  
6    O OG1 . THR A 3   ? 0.8189 0.7698 0.6176 0.1102  0.0211  0.0482  36  THR A OG1 
7    C CG2 . THR A 3   ? 0.6296 0.5838 0.4771 0.0792  0.0230  0.0459  36  THR A CG2 
8    N N   . SER A 4   ? 0.4215 0.3898 0.2860 0.0654  -0.0075 0.0203  37  SER A N   
9    C CA  . SER A 4   ? 0.3600 0.3301 0.2447 0.0525  -0.0106 0.0165  37  SER A CA  
10   C C   . SER A 4   ? 0.3155 0.2788 0.2133 0.0445  -0.0003 0.0243  37  SER A C   
11   O O   . SER A 4   ? 0.2879 0.2491 0.1884 0.0429  0.0076  0.0292  37  SER A O   
12   C CB  . SER A 4   ? 0.3101 0.2882 0.2053 0.0446  -0.0184 0.0060  37  SER A CB  
13   O OG  . SER A 4   ? 0.2709 0.2495 0.1833 0.0337  -0.0192 0.0038  37  SER A OG  
14   N N   A GLN A 5   ? 0.3010 0.2608 0.2083 0.0399  -0.0009 0.0250  38  GLN A N   
15   N N   B GLN A 5   ? 0.3009 0.2607 0.2081 0.0399  -0.0009 0.0250  38  GLN A N   
16   C CA  A GLN A 5   ? 0.2909 0.2442 0.2139 0.0312  0.0052  0.0289  38  GLN A CA  
17   C CA  B GLN A 5   ? 0.2908 0.2441 0.2138 0.0312  0.0053  0.0290  38  GLN A CA  
18   C C   A GLN A 5   ? 0.2529 0.2103 0.1891 0.0208  0.0024  0.0225  38  GLN A C   
19   C C   B GLN A 5   ? 0.2527 0.2101 0.1889 0.0209  0.0025  0.0226  38  GLN A C   
20   O O   A GLN A 5   ? 0.2664 0.2192 0.2164 0.0142  0.0065  0.0248  38  GLN A O   
21   O O   B GLN A 5   ? 0.2664 0.2193 0.2163 0.0143  0.0067  0.0249  38  GLN A O   
22   C CB  A GLN A 5   ? 0.2985 0.2467 0.2265 0.0298  0.0032  0.0288  38  GLN A CB  
23   C CB  B GLN A 5   ? 0.2983 0.2466 0.2265 0.0297  0.0032  0.0288  38  GLN A CB  
24   C CG  A GLN A 5   ? 0.3274 0.2697 0.2445 0.0399  0.0074  0.0368  38  GLN A CG  
25   C CG  B GLN A 5   ? 0.3266 0.2680 0.2452 0.0391  0.0084  0.0375  38  GLN A CG  
26   C CD  A GLN A 5   ? 0.3407 0.2803 0.2603 0.0399  0.0031  0.0347  38  GLN A CD  
27   C CD  B GLN A 5   ? 0.3563 0.2889 0.2807 0.0397  0.0205  0.0484  38  GLN A CD  
28   O OE1 A GLN A 5   ? 0.3538 0.2932 0.2843 0.0322  -0.0007 0.0288  38  GLN A OE1 
29   O OE1 B GLN A 5   ? 0.4364 0.3672 0.3488 0.0491  0.0277  0.0566  38  GLN A OE1 
30   N NE2 A GLN A 5   ? 0.4166 0.3539 0.3246 0.0500  0.0039  0.0396  38  GLN A NE2 
31   N NE2 B GLN A 5   ? 0.3768 0.3032 0.3204 0.0305  0.0229  0.0487  38  GLN A NE2 
32   N N   . LEU A 6   ? 0.2278 0.1934 0.1616 0.0197  -0.0047 0.0145  39  LEU A N   
33   C CA  . LEU A 6   ? 0.2134 0.1828 0.1579 0.0112  -0.0070 0.0091  39  LEU A CA  
34   C C   . LEU A 6   ? 0.2251 0.1977 0.1676 0.0118  -0.0037 0.0099  39  LEU A C   
35   O O   . LEU A 6   ? 0.1956 0.1720 0.1459 0.0059  -0.0058 0.0055  39  LEU A O   
36   C CB  . LEU A 6   ? 0.2092 0.1846 0.1556 0.0092  -0.0152 0.0008  39  LEU A CB  
37   C CG  . LEU A 6   ? 0.2208 0.1934 0.1707 0.0084  -0.0176 -0.0002 39  LEU A CG  
38   C CD1 . LEU A 6   ? 0.2444 0.2235 0.1987 0.0071  -0.0232 -0.0065 39  LEU A CD1 
39   C CD2 . LEU A 6   ? 0.2271 0.1921 0.1851 0.0031  -0.0148 0.0013  39  LEU A CD2 
40   N N   . ALA A 7   ? 0.2256 0.1964 0.1568 0.0200  0.0020  0.0161  40  ALA A N   
41   C CA  . ALA A 7   ? 0.2280 0.2018 0.1541 0.0229  0.0052  0.0167  40  ALA A CA  
42   C C   . ALA A 7   ? 0.2184 0.1911 0.1603 0.0157  0.0121  0.0206  40  ALA A C   
43   O O   . ALA A 7   ? 0.2349 0.2122 0.1794 0.0135  0.0117  0.0174  40  ALA A O   
44   C CB  . ALA A 7   ? 0.2444 0.2153 0.1514 0.0360  0.0106  0.0231  40  ALA A CB  
45   N N   . GLU A 8   ? 0.2204 0.1872 0.1750 0.0121  0.0179  0.0270  41  GLU A N   
46   C CA  . GLU A 8   ? 0.2427 0.2091 0.2167 0.0052  0.0231  0.0300  41  GLU A CA  
47   C C   . GLU A 8   ? 0.2264 0.1972 0.2111 -0.0038 0.0143  0.0204  41  GLU A C   
48   O O   . GLU A 8   ? 0.2070 0.1819 0.2006 -0.0073 0.0153  0.0193  41  GLU A O   
49   C CB  . GLU A 8   ? 0.2606 0.2191 0.2497 0.0031  0.0299  0.0379  41  GLU A CB  
50   C CG  . GLU A 8   ? 0.2286 0.1868 0.2417 -0.0028 0.0361  0.0422  41  GLU A CG  
51   C CD  . GLU A 8   ? 0.3568 0.3065 0.3884 -0.0042 0.0441  0.0510  41  GLU A CD  
52   O OE1 . GLU A 8   ? 0.3582 0.3015 0.3809 0.0005  0.0458  0.0547  41  GLU A OE1 
53   O OE2 . GLU A 8   ? 0.4293 0.3787 0.4868 -0.0099 0.0484  0.0542  41  GLU A OE2 
54   N N   . LEU A 9   ? 0.1931 0.1631 0.1759 -0.0063 0.0062  0.0140  42  LEU A N   
55   C CA  . LEU A 9   ? 0.2061 0.1795 0.1950 -0.0123 -0.0015 0.0057  42  LEU A CA  
56   C C   . LEU A 9   ? 0.1817 0.1625 0.1636 -0.0112 -0.0039 0.0014  42  LEU A C   
57   O O   . LEU A 9   ? 0.1803 0.1644 0.1697 -0.0153 -0.0055 -0.0017 42  LEU A O   
58   C CB  . LEU A 9   ? 0.2044 0.1749 0.1896 -0.0125 -0.0075 0.0014  42  LEU A CB  
59   C CG  . LEU A 9   ? 0.2133 0.1865 0.1993 -0.0155 -0.0143 -0.0062 42  LEU A CG  
60   C CD1 . LEU A 9   ? 0.1989 0.1708 0.1969 -0.0205 -0.0163 -0.0087 42  LEU A CD1 
61   C CD2 . LEU A 9   ? 0.1894 0.1590 0.1706 -0.0136 -0.0178 -0.0084 42  LEU A CD2 
62   N N   . VAL A 10  ? 0.1833 0.1664 0.1516 -0.0053 -0.0051 0.0005  43  VAL A N   
63   C CA  . VAL A 10  ? 0.1891 0.1783 0.1529 -0.0042 -0.0086 -0.0049 43  VAL A CA  
64   C C   . VAL A 10  ? 0.1780 0.1688 0.1419 -0.0029 -0.0030 -0.0020 43  VAL A C   
65   O O   . VAL A 10  ? 0.1716 0.1666 0.1388 -0.0052 -0.0048 -0.0061 43  VAL A O   
66   C CB  . VAL A 10  ? 0.2209 0.2120 0.1727 0.0024  -0.0130 -0.0079 43  VAL A CB  
67   C CG1 . VAL A 10  ? 0.2054 0.2017 0.1545 0.0040  -0.0172 -0.0143 43  VAL A CG1 
68   C CG2 . VAL A 10  ? 0.1749 0.1656 0.1300 0.0007  -0.0179 -0.0106 43  VAL A CG2 
69   N N   . ASP A 11  ? 0.1894 0.1768 0.1503 0.0015  0.0049  0.0059  44  ASP A N   
70   C CA  . ASP A 11  ? 0.2303 0.2189 0.1934 0.0035  0.0125  0.0105  44  ASP A CA  
71   C C   . ASP A 11  ? 0.2018 0.1927 0.1844 -0.0052 0.0126  0.0096  44  ASP A C   
72   O O   . ASP A 11  ? 0.1964 0.1914 0.1817 -0.0057 0.0139  0.0083  44  ASP A O   
73   C CB  . ASP A 11  ? 0.2098 0.1933 0.1694 0.0099  0.0232  0.0213  44  ASP A CB  
74   C CG  . ASP A 11  ? 0.2540 0.2387 0.2155 0.0138  0.0334  0.0278  44  ASP A CG  
75   O OD1 . ASP A 11  ? 0.2742 0.2611 0.2203 0.0207  0.0330  0.0250  44  ASP A OD1 
76   O OD2 . ASP A 11  ? 0.2853 0.2684 0.2649 0.0103  0.0418  0.0357  44  ASP A OD2 
77   N N   . ALA A 12  ? 0.1784 0.1664 0.1746 -0.0113 0.0107  0.0099  45  ALA A N   
78   C CA  . ALA A 12  ? 0.1866 0.1765 0.2013 -0.0185 0.0084  0.0076  45  ALA A CA  
79   C C   . ALA A 12  ? 0.1912 0.1855 0.2029 -0.0210 0.0005  -0.0007 45  ALA A C   
80   O O   . ALA A 12  ? 0.1548 0.1530 0.1755 -0.0236 0.0001  -0.0022 45  ALA A O   
81   C CB  . ALA A 12  ? 0.1703 0.1547 0.1981 -0.0230 0.0057  0.0077  45  ALA A CB  
82   N N   . ALA A 13  ? 0.1707 0.1645 0.1714 -0.0198 -0.0051 -0.0055 46  ALA A N   
83   C CA  . ALA A 13  ? 0.1718 0.1692 0.1709 -0.0213 -0.0106 -0.0117 46  ALA A CA  
84   C C   . ALA A 13  ? 0.1784 0.1803 0.1736 -0.0190 -0.0085 -0.0127 46  ALA A C   
85   O O   . ALA A 13  ? 0.1644 0.1693 0.1646 -0.0212 -0.0102 -0.0155 46  ALA A O   
86   C CB  . ALA A 13  ? 0.1507 0.1468 0.1419 -0.0198 -0.0149 -0.0150 46  ALA A CB  
87   N N   . ALA A 14  ? 0.1563 0.1581 0.1413 -0.0136 -0.0053 -0.0107 47  ALA A N   
88   C CA  . ALA A 14  ? 0.1833 0.1881 0.1629 -0.0100 -0.0038 -0.0126 47  ALA A CA  
89   C C   . ALA A 14  ? 0.1797 0.1863 0.1681 -0.0111 0.0024  -0.0083 47  ALA A C   
90   O O   . ALA A 14  ? 0.1615 0.1713 0.1523 -0.0115 0.0020  -0.0111 47  ALA A O   
91   C CB  . ALA A 14  ? 0.1716 0.1748 0.1354 -0.0016 -0.0028 -0.0122 47  ALA A CB  
92   N N   . GLU A 15  ? 0.1641 0.1688 0.1600 -0.0116 0.0086  -0.0012 48  GLU A N   
93   C CA  . GLU A 15  ? 0.1781 0.1854 0.1877 -0.0131 0.0147  0.0033  48  GLU A CA  
94   C C   . GLU A 15  ? 0.1590 0.1697 0.1824 -0.0198 0.0085  -0.0016 48  GLU A C   
95   O O   . GLU A 15  ? 0.1504 0.1651 0.1810 -0.0202 0.0104  -0.0015 48  GLU A O   
96   C CB  . GLU A 15  ? 0.1712 0.1757 0.1922 -0.0132 0.0226  0.0122  48  GLU A CB  
97   C CG  . GLU A 15  ? 0.1748 0.1827 0.2125 -0.0136 0.0310  0.0184  48  GLU A CG  
98   C CD  . GLU A 15  ? 0.2835 0.2886 0.3377 -0.0138 0.0405  0.0285  48  GLU A CD  
99   O OE1 . GLU A 15  ? 0.2712 0.2706 0.3180 -0.0111 0.0431  0.0324  48  GLU A OE1 
100  O OE2 . GLU A 15  ? 0.3037 0.3123 0.3808 -0.0167 0.0457  0.0329  48  GLU A OE2 
101  N N   . ARG A 16  ? 0.1468 0.1555 0.1726 -0.0238 0.0011  -0.0058 49  ARG A N   
102  C CA  . ARG A 16  ? 0.1621 0.1729 0.1968 -0.0277 -0.0054 -0.0105 49  ARG A CA  
103  C C   . ARG A 16  ? 0.1961 0.2097 0.2226 -0.0261 -0.0075 -0.0148 49  ARG A C   
104  O O   . ARG A 16  ? 0.1720 0.1888 0.2057 -0.0273 -0.0092 -0.0165 49  ARG A O   
105  C CB  . ARG A 16  ? 0.1556 0.1620 0.1906 -0.0299 -0.0122 -0.0139 49  ARG A CB  
106  C CG  . ARG A 16  ? 0.2210 0.2281 0.2665 -0.0323 -0.0192 -0.0181 49  ARG A CG  
107  C CD  . ARG A 16  ? 0.2129 0.2146 0.2506 -0.0315 -0.0259 -0.0225 49  ARG A CD  
108  N NE  . ARG A 16  ? 0.2087 0.2092 0.2527 -0.0315 -0.0339 -0.0275 49  ARG A NE  
109  C CZ  . ARG A 16  ? 0.2450 0.2470 0.2832 -0.0287 -0.0377 -0.0307 49  ARG A CZ  
110  N NH1 . ARG A 16  ? 0.2251 0.2304 0.2556 -0.0272 -0.0334 -0.0292 49  ARG A NH1 
111  N NH2 . ARG A 16  ? 0.2244 0.2240 0.2646 -0.0266 -0.0462 -0.0359 49  ARG A NH2 
112  N N   . LEU A 17  ? 0.1421 0.1545 0.1555 -0.0232 -0.0078 -0.0167 50  LEU A N   
113  C CA  . LEU A 17  ? 0.1549 0.1694 0.1642 -0.0218 -0.0094 -0.0208 50  LEU A CA  
114  C C   . LEU A 17  ? 0.2040 0.2215 0.2159 -0.0200 -0.0049 -0.0195 50  LEU A C   
115  O O   . LEU A 17  ? 0.1551 0.1745 0.1697 -0.0202 -0.0060 -0.0221 50  LEU A O   
116  C CB  . LEU A 17  ? 0.1364 0.1494 0.1353 -0.0188 -0.0112 -0.0238 50  LEU A CB  
117  C CG  . LEU A 17  ? 0.1408 0.1519 0.1384 -0.0199 -0.0154 -0.0257 50  LEU A CG  
118  C CD1 . LEU A 17  ? 0.2059 0.2169 0.1969 -0.0164 -0.0176 -0.0290 50  LEU A CD1 
119  C CD2 . LEU A 17  ? 0.1318 0.1432 0.1350 -0.0219 -0.0175 -0.0274 50  LEU A CD2 
120  N N   . GLU A 18  ? 0.1430 0.1604 0.1536 -0.0172 0.0013  -0.0147 51  GLU A N   
121  C CA  . GLU A 18  ? 0.1669 0.1868 0.1784 -0.0138 0.0070  -0.0128 51  GLU A CA  
122  C C   . GLU A 18  ? 0.1614 0.1857 0.1893 -0.0175 0.0074  -0.0116 51  GLU A C   
123  O O   . GLU A 18  ? 0.1650 0.1918 0.1944 -0.0150 0.0109  -0.0113 51  GLU A O   
124  C CB  . GLU A 18  ? 0.1700 0.1883 0.1761 -0.0083 0.0156  -0.0061 51  GLU A CB  
125  C CG  . GLU A 18  ? 0.2317 0.2459 0.2188 -0.0025 0.0137  -0.0085 51  GLU A CG  
126  C CD  . GLU A 18  ? 0.3097 0.3209 0.2864 0.0054  0.0224  -0.0012 51  GLU A CD  
127  O OE1 . GLU A 18  ? 0.4112 0.4235 0.3965 0.0068  0.0320  0.0067  51  GLU A OE1 
128  O OE2 . GLU A 18  ? 0.3822 0.3899 0.3428 0.0111  0.0199  -0.0031 51  GLU A OE2 
129  N N   . VAL A 19  ? 0.1611 0.1859 0.2008 -0.0225 0.0030  -0.0116 52  VAL A N   
130  C CA  . VAL A 19  ? 0.1755 0.2047 0.2309 -0.0250 0.0010  -0.0118 52  VAL A CA  
131  C C   . VAL A 19  ? 0.1363 0.1666 0.1869 -0.0240 -0.0029 -0.0165 52  VAL A C   
132  O O   . VAL A 19  ? 0.1788 0.2131 0.2393 -0.0241 -0.0035 -0.0165 52  VAL A O   
133  C CB  . VAL A 19  ? 0.2019 0.2303 0.2697 -0.0292 -0.0051 -0.0127 52  VAL A CB  
134  C CG1 . VAL A 19  ? 0.2225 0.2559 0.3078 -0.0308 -0.0092 -0.0141 52  VAL A CG1 
135  C CG2 . VAL A 19  ? 0.1934 0.2197 0.2688 -0.0304 -0.0003 -0.0074 52  VAL A CG2 
136  N N   . ALA A 20  ? 0.1361 0.1630 0.1736 -0.0228 -0.0051 -0.0199 53  ALA A N   
137  C CA  . ALA A 20  ? 0.1507 0.1777 0.1859 -0.0216 -0.0072 -0.0232 53  ALA A CA  
138  C C   . ALA A 20  ? 0.1764 0.2059 0.2138 -0.0191 -0.0026 -0.0227 53  ALA A C   
139  O O   . ALA A 20  ? 0.1733 0.2041 0.2146 -0.0184 -0.0037 -0.0238 53  ALA A O   
140  C CB  . ALA A 20  ? 0.1731 0.1962 0.1986 -0.0208 -0.0089 -0.0263 53  ALA A CB  
141  N N   . ASP A 21  ? 0.1444 0.1739 0.1776 -0.0163 0.0028  -0.0209 54  ASP A N   
142  C CA  . ASP A 21  ? 0.1441 0.1748 0.1764 -0.0123 0.0074  -0.0211 54  ASP A CA  
143  C C   . ASP A 21  ? 0.1783 0.2146 0.2254 -0.0129 0.0102  -0.0173 54  ASP A C   
144  O O   . ASP A 21  ? 0.2099 0.2476 0.2603 -0.0119 0.0095  -0.0190 54  ASP A O   
145  C CB  . ASP A 21  ? 0.2143 0.2424 0.2341 -0.0066 0.0124  -0.0206 54  ASP A CB  
146  C CG  . ASP A 21  ? 0.3014 0.3247 0.3087 -0.0036 0.0081  -0.0278 54  ASP A CG  
147  O OD1 . ASP A 21  ? 0.3524 0.3749 0.3618 -0.0029 0.0065  -0.0318 54  ASP A OD1 
148  O OD2 . ASP A 21  ? 0.2547 0.2751 0.2523 -0.0020 0.0057  -0.0296 54  ASP A OD2 
149  N N   . PRO A 22  ? 0.1633 0.2031 0.2221 -0.0146 0.0133  -0.0121 55  PRO A N   
150  C CA  . PRO A 22  ? 0.1801 0.2263 0.2578 -0.0156 0.0142  -0.0093 55  PRO A CA  
151  C C   . PRO A 22  ? 0.1450 0.1927 0.2286 -0.0182 0.0050  -0.0133 55  PRO A C   
152  O O   . PRO A 22  ? 0.1330 0.1849 0.2254 -0.0168 0.0046  -0.0133 55  PRO A O   
153  C CB  . PRO A 22  ? 0.1442 0.1930 0.2369 -0.0179 0.0180  -0.0035 55  PRO A CB  
154  C CG  . PRO A 22  ? 0.2204 0.2635 0.3013 -0.0191 0.0163  -0.0042 55  PRO A CG  
155  C CD  . PRO A 22  ? 0.1719 0.2101 0.2302 -0.0151 0.0166  -0.0080 55  PRO A CD  
156  N N   . VAL A 23  ? 0.1415 0.1854 0.2189 -0.0206 -0.0019 -0.0164 56  VAL A N   
157  C CA  . VAL A 23  ? 0.1414 0.1856 0.2205 -0.0205 -0.0100 -0.0197 56  VAL A CA  
158  C C   . VAL A 23  ? 0.1837 0.2261 0.2541 -0.0172 -0.0090 -0.0213 56  VAL A C   
159  O O   . VAL A 23  ? 0.1434 0.1882 0.2187 -0.0149 -0.0119 -0.0217 56  VAL A O   
160  C CB  . VAL A 23  ? 0.2073 0.2467 0.2794 -0.0221 -0.0163 -0.0222 56  VAL A CB  
161  C CG1 . VAL A 23  ? 0.2079 0.2457 0.2749 -0.0190 -0.0233 -0.0252 56  VAL A CG1 
162  C CG2 . VAL A 23  ? 0.1386 0.1797 0.2241 -0.0254 -0.0187 -0.0213 56  VAL A CG2 
163  N N   . ALA A 24  ? 0.1310 0.1688 0.1895 -0.0164 -0.0054 -0.0224 57  ALA A N   
164  C CA  . ALA A 24  ? 0.1596 0.1949 0.2137 -0.0137 -0.0040 -0.0240 57  ALA A CA  
165  C C   . ALA A 24  ? 0.1538 0.1929 0.2150 -0.0111 0.0000  -0.0227 57  ALA A C   
166  O O   . ALA A 24  ? 0.1697 0.2090 0.2335 -0.0087 -0.0007 -0.0226 57  ALA A O   
167  C CB  . ALA A 24  ? 0.1619 0.1921 0.2066 -0.0136 -0.0021 -0.0267 57  ALA A CB  
168  N N   . ALA A 25  ? 0.1392 0.1808 0.2029 -0.0105 0.0052  -0.0208 58  ALA A N   
169  C CA  . ALA A 25  ? 0.1481 0.1935 0.2187 -0.0072 0.0103  -0.0190 58  ALA A CA  
170  C C   . ALA A 25  ? 0.1475 0.1994 0.2333 -0.0075 0.0070  -0.0169 58  ALA A C   
171  O O   . ALA A 25  ? 0.1454 0.1988 0.2350 -0.0044 0.0079  -0.0168 58  ALA A O   
172  C CB  . ALA A 25  ? 0.1726 0.2196 0.2432 -0.0051 0.0179  -0.0156 58  ALA A CB  
173  N N   . PHE A 26  ? 0.1355 0.1907 0.2305 -0.0108 0.0022  -0.0160 59  PHE A N   
174  C CA  . PHE A 26  ? 0.1218 0.1833 0.2325 -0.0106 -0.0037 -0.0158 59  PHE A CA  
175  C C   . PHE A 26  ? 0.1417 0.2005 0.2445 -0.0074 -0.0101 -0.0185 59  PHE A C   
176  O O   . PHE A 26  ? 0.1357 0.1984 0.2456 -0.0038 -0.0117 -0.0181 59  PHE A O   
177  C CB  . PHE A 26  ? 0.1316 0.1957 0.2541 -0.0146 -0.0091 -0.0159 59  PHE A CB  
178  C CG  . PHE A 26  ? 0.1397 0.2108 0.2819 -0.0141 -0.0171 -0.0172 59  PHE A CG  
179  C CD1 . PHE A 26  ? 0.1309 0.2002 0.2677 -0.0117 -0.0283 -0.0220 59  PHE A CD1 
180  C CD2 . PHE A 26  ? 0.2033 0.2828 0.3700 -0.0151 -0.0134 -0.0137 59  PHE A CD2 
181  C CE1 . PHE A 26  ? 0.1391 0.2146 0.2932 -0.0099 -0.0380 -0.0248 59  PHE A CE1 
182  C CE2 . PHE A 26  ? 0.2078 0.2946 0.3963 -0.0147 -0.0225 -0.0159 59  PHE A CE2 
183  C CZ  . PHE A 26  ? 0.1789 0.2637 0.3605 -0.0119 -0.0359 -0.0222 59  PHE A CZ  
184  N N   . LYS A 27  ? 0.1231 0.1751 0.2114 -0.0077 -0.0131 -0.0206 60  LYS A N   
185  C CA  . LYS A 27  ? 0.1506 0.1989 0.2300 -0.0031 -0.0172 -0.0215 60  LYS A CA  
186  C C   . LYS A 27  ? 0.1393 0.1855 0.2159 0.0003  -0.0112 -0.0200 60  LYS A C   
187  O O   . LYS A 27  ? 0.1502 0.1960 0.2259 0.0055  -0.0133 -0.0189 60  LYS A O   
188  C CB  . LYS A 27  ? 0.1644 0.2056 0.2300 -0.0037 -0.0189 -0.0226 60  LYS A CB  
189  C CG  . LYS A 27  ? 0.2043 0.2458 0.2701 -0.0049 -0.0266 -0.0248 60  LYS A CG  
190  C CD  . LYS A 27  ? 0.2283 0.2626 0.2800 -0.0052 -0.0261 -0.0252 60  LYS A CD  
191  C CE  . LYS A 27  ? 0.3087 0.3410 0.3565 -0.0037 -0.0345 -0.0279 60  LYS A CE  
192  N NZ  . LYS A 27  ? 0.3489 0.3751 0.3852 -0.0047 -0.0325 -0.0277 60  LYS A NZ  
193  N N   . TRP A 28  ? 0.1299 0.1736 0.2043 -0.0016 -0.0044 -0.0202 61  TRP A N   
194  C CA  . TRP A 28  ? 0.1303 0.1711 0.2040 0.0016  0.0008  -0.0199 61  TRP A CA  
195  C C   . TRP A 28  ? 0.1634 0.2106 0.2478 0.0049  0.0016  -0.0180 61  TRP A C   
196  O O   . TRP A 28  ? 0.1351 0.1811 0.2201 0.0095  0.0017  -0.0167 61  TRP A O   
197  C CB  . TRP A 28  ? 0.1314 0.1684 0.2006 0.0001  0.0060  -0.0224 61  TRP A CB  
198  C CG  . TRP A 28  ? 0.1433 0.1757 0.2123 0.0034  0.0102  -0.0239 61  TRP A CG  
199  C CD1 . TRP A 28  ? 0.1606 0.1949 0.2335 0.0067  0.0145  -0.0237 61  TRP A CD1 
200  C CD2 . TRP A 28  ? 0.1389 0.1634 0.2054 0.0039  0.0109  -0.0257 61  TRP A CD2 
201  N NE1 . TRP A 28  ? 0.1566 0.1840 0.2283 0.0092  0.0170  -0.0263 61  TRP A NE1 
202  C CE2 . TRP A 28  ? 0.1552 0.1765 0.2247 0.0072  0.0148  -0.0274 61  TRP A CE2 
203  C CE3 . TRP A 28  ? 0.1379 0.1576 0.2021 0.0020  0.0093  -0.0257 61  TRP A CE3 
204  C CZ2 . TRP A 28  ? 0.1695 0.1827 0.2417 0.0080  0.0164  -0.0297 61  TRP A CZ2 
205  C CZ3 . TRP A 28  ? 0.1618 0.1743 0.2299 0.0029  0.0119  -0.0268 61  TRP A CZ3 
206  C CH2 . TRP A 28  ? 0.1670 0.1761 0.2399 0.0056  0.0151  -0.0291 61  TRP A CH2 
207  N N   . ARG A 29  ? 0.1297 0.1838 0.2241 0.0032  0.0030  -0.0170 62  ARG A N   
208  C CA  . ARG A 29  ? 0.1310 0.1921 0.2388 0.0065  0.0048  -0.0147 62  ARG A CA  
209  C C   . ARG A 29  ? 0.1414 0.2074 0.2571 0.0089  -0.0039 -0.0145 62  ARG A C   
210  O O   . ARG A 29  ? 0.1458 0.2148 0.2671 0.0138  -0.0041 -0.0132 62  ARG A O   
211  C CB  . ARG A 29  ? 0.1860 0.2535 0.3053 0.0046  0.0100  -0.0122 62  ARG A CB  
212  C CG  . ARG A 29  ? 0.2283 0.3043 0.3653 0.0079  0.0129  -0.0090 62  ARG A CG  
213  N N   . ALA A 30  ? 0.1302 0.1966 0.2450 0.0068  -0.0118 -0.0164 63  ALA A N   
214  C CA  . ALA A 30  ? 0.1434 0.2135 0.2633 0.0106  -0.0223 -0.0179 63  ALA A CA  
215  C C   . ALA A 30  ? 0.1405 0.2032 0.2427 0.0169  -0.0250 -0.0179 63  ALA A C   
216  O O   . ALA A 30  ? 0.1471 0.2114 0.2483 0.0226  -0.0342 -0.0195 63  ALA A O   
217  C CB  . ALA A 30  ? 0.1324 0.2051 0.2592 0.0067  -0.0305 -0.0209 63  ALA A CB  
218  N N   . GLN A 31  ? 0.1407 0.1951 0.2299 0.0167  -0.0174 -0.0163 64  GLN A N   
219  C CA  . GLN A 31  ? 0.1481 0.1948 0.2232 0.0230  -0.0168 -0.0142 64  GLN A CA  
220  C C   . GLN A 31  ? 0.1670 0.2108 0.2311 0.0260  -0.0244 -0.0155 64  GLN A C   
221  O O   . GLN A 31  ? 0.1935 0.2343 0.2478 0.0349  -0.0278 -0.0139 64  GLN A O   
222  C CB  . GLN A 31  ? 0.1547 0.2029 0.2325 0.0307  -0.0163 -0.0115 64  GLN A CB  
223  C CG  . GLN A 31  ? 0.1510 0.2002 0.2378 0.0285  -0.0079 -0.0104 64  GLN A CG  
224  C CD  . GLN A 31  ? 0.2944 0.3450 0.3851 0.0362  -0.0067 -0.0074 64  GLN A CD  
225  O OE1 . GLN A 31  ? 0.3144 0.3578 0.4008 0.0392  0.0003  -0.0047 64  GLN A OE1 
226  N NE2 . GLN A 31  ? 0.2569 0.3169 0.3582 0.0393  -0.0137 -0.0081 64  GLN A NE2 
227  N N   . LEU A 32  ? 0.1483 0.1923 0.2124 0.0197  -0.0267 -0.0183 65  LEU A N   
228  C CA  . LEU A 32  ? 0.2185 0.2587 0.2716 0.0220  -0.0334 -0.0204 65  LEU A CA  
229  C C   . LEU A 32  ? 0.1949 0.2267 0.2355 0.0209  -0.0265 -0.0180 65  LEU A C   
230  O O   . LEU A 32  ? 0.1764 0.2072 0.2210 0.0146  -0.0195 -0.0174 65  LEU A O   
231  C CB  . LEU A 32  ? 0.1678 0.2130 0.2313 0.0158  -0.0403 -0.0248 65  LEU A CB  
232  C CG  . LEU A 32  ? 0.2109 0.2655 0.2932 0.0158  -0.0476 -0.0274 65  LEU A CG  
233  C CD1 . LEU A 32  ? 0.2058 0.2642 0.3025 0.0085  -0.0519 -0.0306 65  LEU A CD1 
234  C CD2 . LEU A 32  ? 0.2337 0.2882 0.3098 0.0260  -0.0583 -0.0299 65  LEU A CD2 
235  N N   . PRO A 33  ? 0.2186 0.2443 0.2444 0.0278  -0.0284 -0.0167 66  PRO A N   
236  C CA  . PRO A 33  ? 0.2717 0.2904 0.2892 0.0264  -0.0214 -0.0140 66  PRO A CA  
237  C C   . PRO A 33  ? 0.2324 0.2525 0.2534 0.0176  -0.0232 -0.0177 66  PRO A C   
238  O O   . PRO A 33  ? 0.1963 0.2201 0.2207 0.0154  -0.0311 -0.0220 66  PRO A O   
239  C CB  . PRO A 33  ? 0.2503 0.2628 0.2502 0.0377  -0.0237 -0.0116 66  PRO A CB  
240  C CG  . PRO A 33  ? 0.3349 0.3517 0.3335 0.0424  -0.0367 -0.0170 66  PRO A CG  
241  C CD  . PRO A 33  ? 0.2247 0.2495 0.2402 0.0383  -0.0374 -0.0180 66  PRO A CD  
242  N N   . ILE A 34  ? 0.1696 0.1865 0.1915 0.0130  -0.0159 -0.0161 67  ILE A N   
243  C CA  . ILE A 34  ? 0.1681 0.1849 0.1898 0.0069  -0.0172 -0.0187 67  ILE A CA  
244  C C   . ILE A 34  ? 0.2226 0.2351 0.2322 0.0118  -0.0214 -0.0188 67  ILE A C   
245  O O   . ILE A 34  ? 0.2188 0.2325 0.2279 0.0093  -0.0278 -0.0226 67  ILE A O   
246  C CB  . ILE A 34  ? 0.2023 0.2167 0.2278 0.0023  -0.0102 -0.0178 67  ILE A CB  
247  C CG1 . ILE A 34  ? 0.2248 0.2425 0.2598 -0.0021 -0.0077 -0.0197 67  ILE A CG1 
248  C CG2 . ILE A 34  ? 0.2037 0.2170 0.2261 -0.0017 -0.0118 -0.0196 67  ILE A CG2 
249  C CD1 . ILE A 34  ? 0.2089 0.2230 0.2485 -0.0042 -0.0023 -0.0201 67  ILE A CD1 
250  N N   . GLU A 35  ? 0.1902 0.1970 0.1900 0.0197  -0.0170 -0.0143 68  GLU A N   
251  C CA  . GLU A 35  ? 0.2205 0.2218 0.2061 0.0261  -0.0186 -0.0135 68  GLU A CA  
252  C C   . GLU A 35  ? 0.2387 0.2400 0.2149 0.0332  -0.0295 -0.0177 68  GLU A C   
253  O O   . GLU A 35  ? 0.2264 0.2298 0.2026 0.0383  -0.0326 -0.0177 68  GLU A O   
254  C CB  . GLU A 35  ? 0.1959 0.1908 0.1746 0.0339  -0.0084 -0.0057 68  GLU A CB  
255  C CG  . GLU A 35  ? 0.1878 0.1769 0.1549 0.0388  -0.0059 -0.0034 68  GLU A CG  
256  C CD  . GLU A 35  ? 0.2474 0.2377 0.2255 0.0297  -0.0014 -0.0035 68  GLU A CD  
257  O OE1 . GLU A 35  ? 0.2372 0.2321 0.2302 0.0202  -0.0006 -0.0058 68  GLU A OE1 
258  O OE2 . GLU A 35  ? 0.2646 0.2509 0.2354 0.0330  0.0012  -0.0015 68  GLU A OE2 
259  N N   . ASP A 36  ? 0.2530 0.2522 0.2226 0.0337  -0.0364 -0.0222 69  ASP A N   
260  C CA  . ASP A 36  ? 0.3074 0.3053 0.2682 0.0415  -0.0489 -0.0281 69  ASP A CA  
261  C C   . ASP A 36  ? 0.2491 0.2396 0.1947 0.0464  -0.0515 -0.0302 69  ASP A C   
262  O O   . ASP A 36  ? 0.2608 0.2520 0.2126 0.0400  -0.0575 -0.0356 69  ASP A O   
263  C CB  . ASP A 36  ? 0.3208 0.3263 0.3002 0.0331  -0.0582 -0.0346 69  ASP A CB  
264  C CG  . ASP A 36  ? 0.3895 0.3949 0.3661 0.0405  -0.0732 -0.0422 69  ASP A CG  
265  O OD1 . ASP A 36  ? 0.3809 0.3792 0.3370 0.0528  -0.0780 -0.0439 69  ASP A OD1 
266  O OD2 . ASP A 36  ? 0.4704 0.4831 0.4666 0.0345  -0.0803 -0.0467 69  ASP A OD2 
267  N N   . SER A 37  ? 0.2191 0.2531 0.2547 0.0294  -0.0586 -0.0359 70  SER A N   
268  C CA  . SER A 37  ? 0.2089 0.2389 0.2215 0.0254  -0.0591 -0.0315 70  SER A CA  
269  C C   . SER A 37  ? 0.2294 0.2599 0.2445 0.0239  -0.0649 -0.0318 70  SER A C   
270  O O   . SER A 37  ? 0.2264 0.2556 0.2270 0.0212  -0.0597 -0.0305 70  SER A O   
271  C CB  . SER A 37  ? 0.2209 0.2384 0.2148 0.0264  -0.0656 -0.0249 70  SER A CB  
272  O OG  . SER A 37  ? 0.2703 0.2787 0.2652 0.0291  -0.0793 -0.0243 70  SER A OG  
273  N N   . GLY A 38  ? 0.2178 0.2481 0.2527 0.0252  -0.0777 -0.0326 71  GLY A N   
274  C CA  . GLY A 38  ? 0.2509 0.2770 0.2890 0.0221  -0.0888 -0.0321 71  GLY A CA  
275  C C   . GLY A 38  ? 0.2396 0.2818 0.2989 0.0190  -0.0777 -0.0341 71  GLY A C   
276  O O   . GLY A 38  ? 0.2309 0.2679 0.2786 0.0152  -0.0803 -0.0337 71  GLY A O   
277  N N   . ARG A 39  ? 0.2117 0.2698 0.2989 0.0212  -0.0639 -0.0360 72  ARG A N   
278  C CA  . ARG A 39  ? 0.1923 0.2628 0.2958 0.0189  -0.0492 -0.0368 72  ARG A CA  
279  C C   . ARG A 39  ? 0.2310 0.2968 0.3007 0.0156  -0.0387 -0.0381 72  ARG A C   
280  O O   . ARG A 39  ? 0.2157 0.2849 0.2866 0.0114  -0.0353 -0.0374 72  ARG A O   
281  C CB  . ARG A 39  ? 0.2265 0.3067 0.3571 0.0244  -0.0319 -0.0381 72  ARG A CB  
282  C CG  . ARG A 39  ? 0.3094 0.3977 0.4504 0.0229  -0.0120 -0.0378 72  ARG A CG  
283  C CD  . ARG A 39  ? 0.4467 0.5385 0.6119 0.0309  0.0097  -0.0379 72  ARG A CD  
284  N NE  . ARG A 39  ? 0.5042 0.6104 0.7089 0.0302  0.0227  -0.0323 72  ARG A NE  
285  C CZ  . ARG A 39  ? 0.6172 0.7201 0.8124 0.0311  0.0476  -0.0323 72  ARG A CZ  
286  N NH1 . ARG A 39  ? 0.6746 0.7564 0.8196 0.0332  0.0604  -0.0384 72  ARG A NH1 
287  N NH2 . ARG A 39  ? 0.4314 0.5492 0.6675 0.0294  0.0581  -0.0249 72  ARG A NH2 
288  N N   . VAL A 40  ? 0.1896 0.2473 0.2329 0.0169  -0.0354 -0.0384 73  VAL A N   
289  C CA  . VAL A 40  ? 0.1872 0.2408 0.2055 0.0135  -0.0289 -0.0368 73  VAL A CA  
290  C C   . VAL A 40  ? 0.2229 0.2708 0.2276 0.0117  -0.0354 -0.0339 73  VAL A C   
291  O O   . VAL A 40  ? 0.2130 0.2617 0.2109 0.0086  -0.0299 -0.0332 73  VAL A O   
292  C CB  . VAL A 40  ? 0.1899 0.2356 0.1916 0.0144  -0.0288 -0.0345 73  VAL A CB  
293  C CG1 . VAL A 40  ? 0.2099 0.2526 0.1952 0.0106  -0.0258 -0.0293 73  VAL A CG1 
294  C CG2 . VAL A 40  ? 0.1968 0.2386 0.2009 0.0163  -0.0224 -0.0387 73  VAL A CG2 
295  N N   . GLU A 41  ? 0.2011 0.2380 0.1962 0.0143  -0.0468 -0.0321 74  GLU A N   
296  C CA  . GLU A 41  ? 0.2159 0.2371 0.1872 0.0144  -0.0514 -0.0299 74  GLU A CA  
297  C C   . GLU A 41  ? 0.2182 0.2405 0.2001 0.0104  -0.0569 -0.0326 74  GLU A C   
298  O O   . GLU A 41  ? 0.2388 0.2541 0.2049 0.0091  -0.0530 -0.0320 74  GLU A O   
299  C CB  . GLU A 41  ? 0.2389 0.2391 0.1898 0.0183  -0.0635 -0.0279 74  GLU A CB  
300  C CG  . GLU A 41  ? 0.3149 0.2863 0.2306 0.0198  -0.0703 -0.0270 74  GLU A CG  
301  C CD  . GLU A 41  ? 0.3833 0.3442 0.2712 0.0241  -0.0529 -0.0221 74  GLU A CD  
302  O OE1 . GLU A 41  ? 0.3028 0.2806 0.2033 0.0247  -0.0388 -0.0176 74  GLU A OE1 
303  O OE2 . GLU A 41  ? 0.4423 0.3750 0.2961 0.0273  -0.0541 -0.0218 74  GLU A OE2 
304  N N   . GLN A 42  ? 0.2154 0.2469 0.2287 0.0084  -0.0660 -0.0342 75  GLN A N   
305  C CA  . GLN A 42  ? 0.2183 0.2522 0.2501 0.0032  -0.0732 -0.0340 75  GLN A CA  
306  C C   . GLN A 42  ? 0.2029 0.2514 0.2430 0.0001  -0.0554 -0.0344 75  GLN A C   
307  O O   . GLN A 42  ? 0.2159 0.2588 0.2499 -0.0038 -0.0579 -0.0339 75  GLN A O   
308  C CB  . GLN A 42  ? 0.2781 0.3222 0.3538 0.0018  -0.0857 -0.0321 75  GLN A CB  
309  C CG  . GLN A 42  ? 0.3495 0.3702 0.4125 0.0020  -0.1123 -0.0306 75  GLN A CG  
310  C CD  . GLN A 42  ? 0.5436 0.5756 0.6547 0.0018  -0.1260 -0.0269 75  GLN A CD  
311  O OE1 . GLN A 42  ? 0.5412 0.5985 0.6913 0.0047  -0.1098 -0.0261 75  GLN A OE1 
312  N NE2 . GLN A 42  ? 0.6374 0.6466 0.7444 -0.0009 -0.1562 -0.0240 75  GLN A NE2 
313  N N   . GLN A 43  ? 0.1893 0.2512 0.2377 0.0019  -0.0387 -0.0354 76  GLN A N   
314  C CA  . GLN A 43  ? 0.1890 0.2577 0.2369 -0.0011 -0.0230 -0.0353 76  GLN A CA  
315  C C   . GLN A 43  ? 0.2309 0.2896 0.2479 -0.0026 -0.0218 -0.0343 76  GLN A C   
316  O O   . GLN A 43  ? 0.1947 0.2533 0.2105 -0.0066 -0.0187 -0.0334 76  GLN A O   
317  C CB  . GLN A 43  ? 0.2069 0.2795 0.2551 0.0018  -0.0078 -0.0370 76  GLN A CB  
318  C CG  . GLN A 43  ? 0.2659 0.3481 0.3479 0.0052  -0.0007 -0.0370 76  GLN A CG  
319  C CD  . GLN A 43  ? 0.4923 0.5677 0.5627 0.0105  0.0132  -0.0399 76  GLN A CD  
320  O OE1 . GLN A 43  ? 0.4519 0.5150 0.4901 0.0102  0.0119  -0.0417 76  GLN A OE1 
321  N NE2 . GLN A 43  ? 0.5638 0.6446 0.6620 0.0158  0.0261  -0.0394 76  GLN A NE2 
322  N N   . LEU A 44  ? 0.1962 0.2468 0.1918 0.0009  -0.0231 -0.0330 77  LEU A N   
323  C CA  . LEU A 44  ? 0.2207 0.2639 0.1957 0.0011  -0.0188 -0.0293 77  LEU A CA  
324  C C   . LEU A 44  ? 0.2231 0.2522 0.1843 0.0019  -0.0249 -0.0292 77  LEU A C   
325  O O   . LEU A 44  ? 0.2058 0.2308 0.1582 0.0009  -0.0198 -0.0274 77  LEU A O   
326  C CB  . LEU A 44  ? 0.2255 0.2647 0.1899 0.0051  -0.0171 -0.0246 77  LEU A CB  
327  C CG  . LEU A 44  ? 0.1821 0.2277 0.1533 0.0033  -0.0143 -0.0240 77  LEU A CG  
328  C CD1 . LEU A 44  ? 0.1945 0.2363 0.1617 0.0061  -0.0160 -0.0175 77  LEU A CD1 
329  C CD2 . LEU A 44  ? 0.1806 0.2271 0.1493 -0.0017 -0.0092 -0.0224 77  LEU A CD2 
330  N N   . ALA A 45  ? 0.2181 0.2347 0.1735 0.0038  -0.0374 -0.0311 78  ALA A N   
331  C CA  . ALA A 45  ? 0.2429 0.2359 0.1763 0.0043  -0.0469 -0.0319 78  ALA A CA  
332  C C   . ALA A 45  ? 0.2387 0.2383 0.1899 -0.0028 -0.0503 -0.0333 78  ALA A C   
333  O O   . ALA A 45  ? 0.2521 0.2368 0.1847 -0.0030 -0.0499 -0.0331 78  ALA A O   
334  C CB  . ALA A 45  ? 0.2673 0.2397 0.1886 0.0059  -0.0653 -0.0334 78  ALA A CB  
335  N N   . LYS A 46  ? 0.2223 0.2434 0.2109 -0.0079 -0.0514 -0.0335 79  LYS A N   
336  C CA  . LYS A 46  ? 0.2191 0.2483 0.2306 -0.0149 -0.0521 -0.0323 79  LYS A CA  
337  C C   . LYS A 46  ? 0.2100 0.2443 0.2119 -0.0162 -0.0360 -0.0313 79  LYS A C   
338  O O   . LYS A 46  ? 0.2174 0.2448 0.2163 -0.0203 -0.0385 -0.0303 79  LYS A O   
339  C CB  . LYS A 46  ? 0.2062 0.2577 0.2636 -0.0179 -0.0498 -0.0301 79  LYS A CB  
340  C CG  . LYS A 46  ? 0.3485 0.4116 0.4335 -0.0246 -0.0432 -0.0262 79  LYS A CG  
341  C CD  . LYS A 46  ? 0.5064 0.5907 0.6429 -0.0258 -0.0366 -0.0213 79  LYS A CD  
342  C CE  . LYS A 46  ? 0.4932 0.5887 0.6540 -0.0314 -0.0220 -0.0156 79  LYS A CE  
343  N NZ  . LYS A 46  ? 0.5677 0.6513 0.7242 -0.0390 -0.0384 -0.0135 79  LYS A NZ  
344  N N   . LEU A 47  ? 0.1975 0.2409 0.1940 -0.0135 -0.0223 -0.0309 80  LEU A N   
345  C CA  . LEU A 47  ? 0.2110 0.2558 0.1977 -0.0156 -0.0113 -0.0287 80  LEU A CA  
346  C C   . LEU A 47  ? 0.2029 0.2324 0.1662 -0.0126 -0.0131 -0.0268 80  LEU A C   
347  O O   . LEU A 47  ? 0.2051 0.2316 0.1645 -0.0154 -0.0098 -0.0248 80  LEU A O   
348  C CB  . LEU A 47  ? 0.2077 0.2583 0.1909 -0.0144 -0.0022 -0.0280 80  LEU A CB  
349  C CG  . LEU A 47  ? 0.2778 0.3370 0.2772 -0.0156 0.0056  -0.0299 80  LEU A CG  
350  C CD1 . LEU A 47  ? 0.2176 0.2741 0.2073 -0.0123 0.0091  -0.0311 80  LEU A CD1 
351  C CD2 . LEU A 47  ? 0.2228 0.2817 0.2233 -0.0207 0.0163  -0.0281 80  LEU A CD2 
352  N N   . GLY A 48  ? 0.2123 0.2299 0.1593 -0.0058 -0.0162 -0.0265 81  GLY A N   
353  C CA  . GLY A 48  ? 0.2294 0.2276 0.1526 -0.0001 -0.0134 -0.0239 81  GLY A CA  
354  C C   . GLY A 48  ? 0.2631 0.2431 0.1750 -0.0024 -0.0223 -0.0271 81  GLY A C   
355  O O   . GLY A 48  ? 0.2599 0.2279 0.1587 -0.0003 -0.0176 -0.0252 81  GLY A O   
356  N N   . GLU A 49  ? 0.2565 0.2331 0.1764 -0.0071 -0.0373 -0.0309 82  GLU A N   
357  C CA  . GLU A 49  ? 0.2786 0.2357 0.1913 -0.0115 -0.0511 -0.0327 82  GLU A CA  
358  C C   . GLU A 49  ? 0.2649 0.2393 0.2028 -0.0199 -0.0468 -0.0305 82  GLU A C   
359  O O   . GLU A 49  ? 0.2839 0.2413 0.2099 -0.0220 -0.0518 -0.0304 82  GLU A O   
360  C CB  . GLU A 49  ? 0.3374 0.2845 0.2578 -0.0155 -0.0732 -0.0346 82  GLU A CB  
361  C CG  . GLU A 49  ? 0.3863 0.2996 0.2653 -0.0076 -0.0823 -0.0370 82  GLU A CG  
362  C CD  . GLU A 49  ? 0.5639 0.4303 0.3900 -0.0019 -0.0864 -0.0392 82  GLU A CD  
363  O OE1 . GLU A 49  ? 0.4875 0.3486 0.2933 0.0064  -0.0658 -0.0377 82  GLU A OE1 
364  O OE2 . GLU A 49  ? 0.6162 0.4475 0.4208 -0.0053 -0.1111 -0.0417 82  GLU A OE2 
365  N N   . ASP A 50  ? 0.2364 0.2397 0.2042 -0.0241 -0.0366 -0.0284 83  ASP A N   
366  C CA  . ASP A 50  ? 0.2766 0.2913 0.2599 -0.0310 -0.0284 -0.0252 83  ASP A CA  
367  C C   . ASP A 50  ? 0.2774 0.2833 0.2382 -0.0282 -0.0205 -0.0235 83  ASP A C   
368  O O   . ASP A 50  ? 0.2857 0.2845 0.2448 -0.0325 -0.0217 -0.0217 83  ASP A O   
369  C CB  . ASP A 50  ? 0.2132 0.2506 0.2192 -0.0333 -0.0152 -0.0235 83  ASP A CB  
370  C CG  . ASP A 50  ? 0.3358 0.3851 0.3755 -0.0355 -0.0199 -0.0228 83  ASP A CG  
371  O OD1 . ASP A 50  ? 0.3246 0.3666 0.3770 -0.0390 -0.0368 -0.0218 83  ASP A OD1 
372  O OD2 . ASP A 50  ? 0.3364 0.3995 0.3901 -0.0336 -0.0077 -0.0224 83  ASP A OD2 
373  N N   . ALA A 51  ? 0.2254 0.2314 0.1729 -0.0212 -0.0133 -0.0225 84  ALA A N   
374  C CA  . ALA A 51  ? 0.2806 0.2796 0.2156 -0.0176 -0.0066 -0.0182 84  ALA A CA  
375  C C   . ALA A 51  ? 0.2527 0.2264 0.1671 -0.0126 -0.0105 -0.0192 84  ALA A C   
376  O O   . ALA A 51  ? 0.2658 0.2325 0.1771 -0.0140 -0.0089 -0.0167 84  ALA A O   
377  C CB  . ALA A 51  ? 0.2240 0.2283 0.1576 -0.0111 0.0001  -0.0142 84  ALA A CB  
378  N N   . ARG A 52  ? 0.2724 0.2268 0.1675 -0.0065 -0.0163 -0.0230 85  ARG A N   
379  C CA  . ARG A 52  ? 0.3134 0.2327 0.1767 -0.0002 -0.0196 -0.0249 85  ARG A CA  
380  C C   . ARG A 52  ? 0.3567 0.2663 0.2228 -0.0094 -0.0332 -0.0273 85  ARG A C   
381  O O   . ARG A 52  ? 0.3412 0.2278 0.1883 -0.0064 -0.0326 -0.0271 85  ARG A O   
382  C CB  . ARG A 52  ? 0.4013 0.2926 0.2333 0.0073  -0.0256 -0.0288 85  ARG A CB  
383  C CG  . ARG A 52  ? 0.4470 0.2908 0.2322 0.0173  -0.0245 -0.0307 85  ARG A CG  
384  C CD  . ARG A 52  ? 0.6113 0.4220 0.3561 0.0272  -0.0247 -0.0329 85  ARG A CD  
385  N NE  . ARG A 52  ? 0.6981 0.4944 0.4350 0.0189  -0.0516 -0.0387 85  ARG A NE  
386  C CZ  . ARG A 52  ? 0.7321 0.4786 0.4261 0.0189  -0.0714 -0.0438 85  ARG A CZ  
387  N NH1 . ARG A 52  ? 0.7499 0.4527 0.3983 0.0280  -0.0647 -0.0454 85  ARG A NH1 
388  N NH2 . ARG A 52  ? 0.7019 0.4388 0.3987 0.0097  -0.0999 -0.0466 85  ARG A NH2 
389  N N   . SER A 53  ? 0.3168 0.2435 0.2101 -0.0203 -0.0445 -0.0282 86  SER A N   
390  C CA  . SER A 53  ? 0.3135 0.2357 0.2200 -0.0306 -0.0566 -0.0274 86  SER A CA  
391  C C   . SER A 53  ? 0.3393 0.2703 0.2521 -0.0332 -0.0451 -0.0232 86  SER A C   
392  O O   . SER A 53  ? 0.3217 0.2348 0.2276 -0.0370 -0.0529 -0.0226 86  SER A O   
393  C CB  . SER A 53  ? 0.3194 0.2662 0.2671 -0.0408 -0.0642 -0.0251 86  SER A CB  
394  O OG  . SER A 53  ? 0.4524 0.3833 0.3963 -0.0409 -0.0837 -0.0278 86  SER A OG  
395  N N   . GLN A 54  ? 0.2778 0.2323 0.2016 -0.0320 -0.0294 -0.0198 87  GLN A N   
396  C CA  . GLN A 54  ? 0.2729 0.2318 0.1995 -0.0350 -0.0215 -0.0148 87  GLN A CA  
397  C C   . GLN A 54  ? 0.3175 0.2614 0.2250 -0.0247 -0.0149 -0.0124 87  GLN A C   
398  O O   . GLN A 54  ? 0.2925 0.2401 0.2050 -0.0265 -0.0101 -0.0068 87  GLN A O   
399  C CB  . GLN A 54  ? 0.2506 0.2340 0.1939 -0.0401 -0.0116 -0.0112 87  GLN A CB  
400  C CG  . GLN A 54  ? 0.2866 0.2851 0.2522 -0.0473 -0.0115 -0.0119 87  GLN A CG  
401  C CD  . GLN A 54  ? 0.2803 0.2761 0.2613 -0.0565 -0.0164 -0.0088 87  GLN A CD  
402  O OE1 . GLN A 54  ? 0.2629 0.2468 0.2346 -0.0591 -0.0182 -0.0062 87  GLN A OE1 
403  N NE2 . GLN A 54  ? 0.2495 0.2569 0.2591 -0.0617 -0.0188 -0.0075 87  GLN A NE2 
404  N N   . HIS A 55  ? 0.3405 0.2653 0.2269 -0.0134 -0.0136 -0.0152 88  HIS A N   
405  C CA  . HIS A 55  ? 0.3251 0.2351 0.1977 -0.0005 -0.0016 -0.0108 88  HIS A CA  
406  C C   . HIS A 55  ? 0.3677 0.3028 0.2631 0.0016  0.0090  -0.0025 88  HIS A C   
407  O O   . HIS A 55  ? 0.3651 0.2980 0.2677 0.0082  0.0177  0.0056  88  HIS A O   
408  C CB  . HIS A 55  ? 0.3963 0.2859 0.2594 0.0004  -0.0026 -0.0093 88  HIS A CB  
409  C CG  . HIS A 55  ? 0.4118 0.2751 0.2550 -0.0048 -0.0182 -0.0165 88  HIS A CG  
410  N ND1 . HIS A 55  ? 0.4814 0.3515 0.3401 -0.0183 -0.0292 -0.0160 88  HIS A ND1 
411  C CD2 . HIS A 55  ? 0.5186 0.3459 0.3275 0.0007  -0.0269 -0.0232 88  HIS A CD2 
412  C CE1 . HIS A 55  ? 0.4437 0.2862 0.2851 -0.0217 -0.0456 -0.0212 88  HIS A CE1 
413  N NE2 . HIS A 55  ? 0.5567 0.3702 0.3645 -0.0105 -0.0463 -0.0263 88  HIS A NE2 
414  N N   . ILE A 56  ? 0.3011 0.2582 0.2102 -0.0040 0.0069  -0.0034 89  ILE A N   
415  C CA  . ILE A 56  ? 0.2870 0.2626 0.2141 -0.0031 0.0121  0.0040  89  ILE A CA  
416  C C   . ILE A 56  ? 0.3249 0.2972 0.2472 0.0076  0.0197  0.0052  89  ILE A C   
417  O O   . ILE A 56  ? 0.3216 0.2827 0.2258 0.0102  0.0172  -0.0022 89  ILE A O   
418  C CB  . ILE A 56  ? 0.2745 0.2680 0.2115 -0.0144 0.0062  0.0018  89  ILE A CB  
419  C CG1 . ILE A 56  ? 0.3323 0.3241 0.2682 -0.0243 0.0022  0.0004  89  ILE A CG1 
420  C CG2 . ILE A 56  ? 0.2729 0.2770 0.2228 -0.0153 0.0062  0.0098  89  ILE A CG2 
421  C CD1 . ILE A 56  ? 0.2721 0.2747 0.2115 -0.0331 0.0022  -0.0019 89  ILE A CD1 
422  N N   . ASP A 57  ? 0.2459 0.2263 0.1862 0.0133  0.0277  0.0161  90  ASP A N   
423  C CA  . ASP A 57  ? 0.2620 0.2399 0.2018 0.0237  0.0384  0.0206  90  ASP A CA  
424  C C   . ASP A 57  ? 0.2644 0.2526 0.2015 0.0184  0.0308  0.0140  90  ASP A C   
425  O O   . ASP A 57  ? 0.2329 0.2392 0.1877 0.0100  0.0235  0.0159  90  ASP A O   
426  C CB  . ASP A 57  ? 0.2782 0.2686 0.2520 0.0282  0.0465  0.0372  90  ASP A CB  
427  C CG  . ASP A 57  ? 0.3821 0.3773 0.3661 0.0357  0.0566  0.0449  90  ASP A CG  
428  O OD1 . ASP A 57  ? 0.5003 0.4822 0.4573 0.0413  0.0616  0.0377  90  ASP A OD1 
429  O OD2 . ASP A 57  ? 0.5335 0.5446 0.5548 0.0353  0.0577  0.0598  90  ASP A OD2 
430  N N   . PRO A 58  ? 0.3280 0.2269 0.2055 0.0235  -0.0038 -0.0073 91  PRO A N   
431  C CA  . PRO A 58  ? 0.2943 0.2012 0.1780 0.0187  -0.0062 -0.0070 91  PRO A CA  
432  C C   . PRO A 58  ? 0.2926 0.2128 0.1907 0.0201  -0.0005 -0.0067 91  PRO A C   
433  O O   . PRO A 58  ? 0.2442 0.1761 0.1529 0.0161  -0.0029 -0.0064 91  PRO A O   
434  C CB  . PRO A 58  ? 0.3468 0.2369 0.2125 0.0182  -0.0083 -0.0074 91  PRO A CB  
435  C CG  . PRO A 58  ? 0.4131 0.2873 0.2636 0.0240  -0.0042 -0.0076 91  PRO A CG  
436  C CD  . PRO A 58  ? 0.3431 0.2218 0.1997 0.0258  -0.0039 -0.0076 91  PRO A CD  
437  N N   . ASP A 59  ? 0.2710 0.1893 0.1699 0.0257  0.0074  -0.0066 92  ASP A N   
438  C CA  . ASP A 59  ? 0.3139 0.2443 0.2271 0.0266  0.0132  -0.0061 92  ASP A CA  
439  C C   . ASP A 59  ? 0.2935 0.2411 0.2266 0.0254  0.0111  -0.0060 92  ASP A C   
440  O O   . ASP A 59  ? 0.2696 0.2286 0.2141 0.0229  0.0112  -0.0056 92  ASP A O   
441  C CB  . ASP A 59  ? 0.3075 0.2313 0.2184 0.0326  0.0233  -0.0060 92  ASP A CB  
442  C CG  . ASP A 59  ? 0.5386 0.4430 0.4274 0.0338  0.0262  -0.0060 92  ASP A CG  
443  O OD1 . ASP A 59  ? 0.4329 0.3328 0.3128 0.0296  0.0204  -0.0062 92  ASP A OD1 
444  O OD2 . ASP A 59  ? 0.6635 0.5563 0.5437 0.0392  0.0343  -0.0060 92  ASP A OD2 
445  N N   . TYR A 60  ? 0.2636 0.2115 0.1993 0.0273  0.0086  -0.0062 93  TYR A N   
446  C CA  . TYR A 60  ? 0.2509 0.2113 0.2014 0.0261  0.0048  -0.0062 93  TYR A CA  
447  C C   . TYR A 60  ? 0.2378 0.2029 0.1880 0.0198  -0.0009 -0.0060 93  TYR A C   
448  O O   . TYR A 60  ? 0.2139 0.1899 0.1757 0.0178  -0.0018 -0.0057 93  TYR A O   
449  C CB  . TYR A 60  ? 0.2808 0.2367 0.2296 0.0292  0.0017  -0.0066 93  TYR A CB  
450  C CG  . TYR A 60  ? 0.2371 0.2011 0.1958 0.0277  -0.0041 -0.0067 93  TYR A CG  
451  C CD1 . TYR A 60  ? 0.2167 0.1778 0.1678 0.0229  -0.0098 -0.0066 93  TYR A CD1 
452  C CD2 . TYR A 60  ? 0.2686 0.2416 0.2439 0.0312  -0.0038 -0.0068 93  TYR A CD2 
453  C CE1 . TYR A 60  ? 0.2268 0.1917 0.1830 0.0218  -0.0146 -0.0066 93  TYR A CE1 
454  C CE2 . TYR A 60  ? 0.2173 0.1945 0.1987 0.0301  -0.0103 -0.0070 93  TYR A CE2 
455  C CZ  . TYR A 60  ? 0.2698 0.2417 0.2398 0.0255  -0.0155 -0.0068 93  TYR A CZ  
456  O OH  . TYR A 60  ? 0.2297 0.2025 0.2023 0.0247  -0.0215 -0.0069 93  TYR A OH  
457  N N   . VAL A 61  ? 0.2177 0.1741 0.1552 0.0166  -0.0045 -0.0061 94  VAL A N   
458  C CA  . VAL A 61  ? 0.2111 0.1713 0.1496 0.0106  -0.0089 -0.0059 94  VAL A CA  
459  C C   . VAL A 61  ? 0.2135 0.1808 0.1577 0.0084  -0.0075 -0.0057 94  VAL A C   
460  O O   . VAL A 61  ? 0.2180 0.1945 0.1707 0.0054  -0.0089 -0.0055 94  VAL A O   
461  C CB  . VAL A 61  ? 0.2206 0.1697 0.1465 0.0077  -0.0128 -0.0061 94  VAL A CB  
462  C CG1 . VAL A 61  ? 0.2147 0.1681 0.1440 0.0016  -0.0161 -0.0059 94  VAL A CG1 
463  C CG2 . VAL A 61  ? 0.2627 0.2055 0.1834 0.0090  -0.0147 -0.0062 94  VAL A CG2 
464  N N   . THR A 62  ? 0.2099 0.1713 0.1477 0.0101  -0.0047 -0.0058 95  THR A N   
465  C CA  . THR A 62  ? 0.2379 0.2040 0.1792 0.0081  -0.0042 -0.0057 95  THR A CA  
466  C C   . THR A 62  ? 0.2004 0.1782 0.1551 0.0094  -0.0001 -0.0053 95  THR A C   
467  O O   . THR A 62  ? 0.2199 0.2050 0.1807 0.0067  -0.0011 -0.0051 95  THR A O   
468  C CB  . THR A 62  ? 0.2665 0.2200 0.1943 0.0095  -0.0029 -0.0059 95  THR A CB  
469  O OG1 . THR A 62  ? 0.2454 0.1922 0.1682 0.0147  0.0039  -0.0058 95  THR A OG1 
470  C CG2 . THR A 62  ? 0.2875 0.2294 0.2031 0.0071  -0.0092 -0.0064 95  THR A CG2 
471  N N   . ARG A 63  ? 0.2159 0.1956 0.1763 0.0134  0.0040  -0.0052 96  ARG A N   
472  C CA  . ARG A 63  ? 0.2119 0.2034 0.1876 0.0140  0.0063  -0.0048 96  ARG A CA  
473  C C   . ARG A 63  ? 0.2163 0.2158 0.1993 0.0110  0.0007  -0.0048 96  ARG A C   
474  O O   . ARG A 63  ? 0.1860 0.1934 0.1766 0.0089  0.0001  -0.0045 96  ARG A O   
475  C CB  . ARG A 63  ? 0.2022 0.1947 0.1857 0.0190  0.0112  -0.0047 96  ARG A CB  
476  C CG  . ARG A 63  ? 0.2163 0.2212 0.2184 0.0194  0.0123  -0.0044 96  ARG A CG  
477  C CD  . ARG A 63  ? 0.3233 0.3325 0.3286 0.0170  0.0153  -0.0039 96  ARG A CD  
478  N NE  . ARG A 63  ? 0.3492 0.3699 0.3718 0.0163  0.0143  -0.0036 96  ARG A NE  
479  C CZ  . ARG A 63  ? 0.4786 0.5047 0.5153 0.0185  0.0198  -0.0033 96  ARG A CZ  
480  N NH1 . ARG A 63  ? 0.3602 0.3809 0.3954 0.0219  0.0284  -0.0031 96  ARG A NH1 
481  N NH2 . ARG A 63  ? 0.4250 0.4611 0.4777 0.0172  0.0170  -0.0031 96  ARG A NH2 
482  N N   . VAL A 64  ? 0.1785 0.1742 0.1573 0.0108  -0.0033 -0.0050 97  VAL A N   
483  C CA  . VAL A 64  ? 0.2017 0.2014 0.1836 0.0081  -0.0078 -0.0049 97  VAL A CA  
484  C C   . VAL A 64  ? 0.1694 0.1718 0.1500 0.0035  -0.0088 -0.0047 97  VAL A C   
485  O O   . VAL A 64  ? 0.1850 0.1935 0.1716 0.0018  -0.0098 -0.0045 97  VAL A O   
486  C CB  . VAL A 64  ? 0.2006 0.1924 0.1746 0.0084  -0.0112 -0.0051 97  VAL A CB  
487  C CG1 . VAL A 64  ? 0.2481 0.2401 0.2203 0.0047  -0.0145 -0.0049 97  VAL A CG1 
488  C CG2 . VAL A 64  ? 0.2373 0.2285 0.2162 0.0134  -0.0116 -0.0054 97  VAL A CG2 
489  N N   . PHE A 65  ? 0.1799 0.1771 0.1529 0.0016  -0.0089 -0.0049 98  PHE A N   
490  C CA  . PHE A 65  ? 0.1674 0.1678 0.1418 -0.0025 -0.0103 -0.0048 98  PHE A CA  
491  C C   . PHE A 65  ? 0.1619 0.1680 0.1414 -0.0024 -0.0085 -0.0048 98  PHE A C   
492  O O   . PHE A 65  ? 0.1580 0.1693 0.1420 -0.0049 -0.0093 -0.0047 98  PHE A O   
493  C CB  . PHE A 65  ? 0.1738 0.1672 0.1410 -0.0049 -0.0126 -0.0051 98  PHE A CB  
494  C CG  . PHE A 65  ? 0.2058 0.1954 0.1701 -0.0073 -0.0144 -0.0050 98  PHE A CG  
495  C CD1 . PHE A 65  ? 0.2394 0.2329 0.2083 -0.0110 -0.0145 -0.0047 98  PHE A CD1 
496  C CD2 . PHE A 65  ? 0.2052 0.1865 0.1616 -0.0055 -0.0151 -0.0051 98  PHE A CD2 
497  C CE1 . PHE A 65  ? 0.2227 0.2111 0.1877 -0.0134 -0.0148 -0.0044 98  PHE A CE1 
498  C CE2 . PHE A 65  ? 0.2440 0.2203 0.1962 -0.0079 -0.0165 -0.0049 98  PHE A CE2 
499  C CZ  . PHE A 65  ? 0.2534 0.2330 0.2098 -0.0120 -0.0160 -0.0045 98  PHE A CZ  
500  N N   . ASP A 66  ? 0.1720 0.1763 0.1505 0.0006  -0.0053 -0.0048 99  ASP A N   
501  C CA  . ASP A 66  ? 0.1858 0.1948 0.1689 0.0006  -0.0030 -0.0046 99  ASP A CA  
502  C C   . ASP A 66  ? 0.1831 0.2014 0.1769 0.0002  -0.0030 -0.0042 99  ASP A C   
503  O O   . ASP A 66  ? 0.1554 0.1783 0.1528 -0.0016 -0.0033 -0.0041 99  ASP A O   
504  C CB  . ASP A 66  ? 0.2084 0.2120 0.1876 0.0039  0.0020  -0.0045 99  ASP A CB  
505  C CG  . ASP A 66  ? 0.2513 0.2567 0.2320 0.0034  0.0046  -0.0042 99  ASP A CG  
506  O OD1 . ASP A 66  ? 0.2321 0.2359 0.2086 0.0013  0.0015  -0.0045 99  ASP A OD1 
507  O OD2 . ASP A 66  ? 0.3001 0.3084 0.2870 0.0052  0.0097  -0.0037 99  ASP A OD2 
508  N N   . ASP A 67  ? 0.1764 0.1961 0.1748 0.0021  -0.0032 -0.0041 100 ASP A N   
509  C CA  . ASP A 67  ? 0.1459 0.1720 0.1530 0.0017  -0.0053 -0.0039 100 ASP A CA  
510  C C   . ASP A 67  ? 0.1455 0.1716 0.1492 -0.0015 -0.0084 -0.0039 100 ASP A C   
511  O O   . ASP A 67  ? 0.1392 0.1694 0.1468 -0.0028 -0.0091 -0.0037 100 ASP A O   
512  C CB  . ASP A 67  ? 0.1487 0.1740 0.1598 0.0044  -0.0072 -0.0040 100 ASP A CB  
513  C CG  . ASP A 67  ? 0.2620 0.2885 0.2802 0.0081  -0.0031 -0.0039 100 ASP A CG  
514  O OD1 . ASP A 67  ? 0.2732 0.3016 0.2941 0.0083  0.0019  -0.0037 100 ASP A OD1 
515  O OD2 . ASP A 67  ? 0.2092 0.2342 0.2305 0.0110  -0.0046 -0.0042 100 ASP A OD2 
516  N N   . GLN A 68  ? 0.1592 0.1800 0.1557 -0.0027 -0.0098 -0.0040 101 GLN A N   
517  C CA  . GLN A 68  ? 0.1625 0.1824 0.1563 -0.0058 -0.0109 -0.0040 101 GLN A CA  
518  C C   . GLN A 68  ? 0.1657 0.1900 0.1623 -0.0078 -0.0097 -0.0040 101 GLN A C   
519  O O   . GLN A 68  ? 0.1442 0.1707 0.1424 -0.0092 -0.0095 -0.0038 101 GLN A O   
520  C CB  . GLN A 68  ? 0.1844 0.1977 0.1711 -0.0072 -0.0115 -0.0040 101 GLN A CB  
521  C CG  . GLN A 68  ? 0.1688 0.1806 0.1536 -0.0107 -0.0107 -0.0038 101 GLN A CG  
522  C CD  . GLN A 68  ? 0.1870 0.1937 0.1669 -0.0105 -0.0115 -0.0035 101 GLN A CD  
523  O OE1 . GLN A 68  ? 0.1886 0.1911 0.1653 -0.0080 -0.0140 -0.0036 101 GLN A OE1 
524  N NE2 . GLN A 68  ? 0.1611 0.1666 0.1396 -0.0127 -0.0094 -0.0032 101 GLN A NE2 
525  N N   . ILE A 69  ? 0.1429 0.1669 0.1388 -0.0077 -0.0091 -0.0043 102 ILE A N   
526  C CA  . ILE A 69  ? 0.1398 0.1668 0.1381 -0.0093 -0.0091 -0.0045 102 ILE A CA  
527  C C   . ILE A 69  ? 0.1773 0.2091 0.1798 -0.0084 -0.0080 -0.0043 102 ILE A C   
528  O O   . ILE A 69  ? 0.1321 0.1671 0.1374 -0.0096 -0.0081 -0.0043 102 ILE A O   
529  C CB  . ILE A 69  ? 0.1470 0.1694 0.1410 -0.0090 -0.0103 -0.0050 102 ILE A CB  
530  C CG1 . ILE A 69  ? 0.1724 0.1901 0.1634 -0.0108 -0.0124 -0.0052 102 ILE A CG1 
531  C CG2 . ILE A 69  ? 0.1932 0.2176 0.1895 -0.0098 -0.0115 -0.0053 102 ILE A CG2 
532  C CD1 . ILE A 69  ? 0.2406 0.2503 0.2244 -0.0102 -0.0148 -0.0057 102 ILE A CD1 
533  N N   . ARG A 70  ? 0.1355 0.1675 0.1393 -0.0062 -0.0065 -0.0040 103 ARG A N   
534  C CA  . ARG A 70  ? 0.1410 0.1774 0.1500 -0.0059 -0.0054 -0.0037 103 ARG A CA  
535  C C   . ARG A 70  ? 0.1451 0.1839 0.1566 -0.0070 -0.0074 -0.0035 103 ARG A C   
536  O O   . ARG A 70  ? 0.1364 0.1776 0.1497 -0.0078 -0.0075 -0.0034 103 ARG A O   
537  C CB  . ARG A 70  ? 0.1606 0.1977 0.1738 -0.0037 -0.0029 -0.0034 103 ARG A CB  
538  C CG  . ARG A 70  ? 0.2222 0.2549 0.2312 -0.0023 0.0010  -0.0034 103 ARG A CG  
539  C CD  . ARG A 70  ? 0.2346 0.2694 0.2512 -0.0004 0.0053  -0.0028 103 ARG A CD  
540  N NE  . ARG A 70  ? 0.1992 0.2348 0.2207 0.0017  0.0051  -0.0029 103 ARG A NE  
541  C CZ  . ARG A 70  ? 0.2510 0.2922 0.2835 0.0022  0.0030  -0.0027 103 ARG A CZ  
542  N NH1 . ARG A 70  ? 0.1961 0.2422 0.2352 0.0004  0.0007  -0.0024 103 ARG A NH1 
543  N NH2 . ARG A 70  ? 0.2292 0.2701 0.2660 0.0047  0.0025  -0.0029 103 ARG A NH2 
544  N N   . ALA A 71  ? 0.1370 0.1734 0.1471 -0.0067 -0.0091 -0.0035 104 ALA A N   
545  C CA  . ALA A 71  ? 0.1327 0.1675 0.1415 -0.0074 -0.0113 -0.0033 104 ALA A CA  
546  C C   . ALA A 71  ? 0.1574 0.1912 0.1626 -0.0094 -0.0100 -0.0034 104 ALA A C   
547  O O   . ALA A 71  ? 0.1706 0.2038 0.1747 -0.0099 -0.0103 -0.0032 104 ALA A O   
548  C CB  . ALA A 71  ? 0.1384 0.1678 0.1436 -0.0064 -0.0138 -0.0033 104 ALA A CB  
549  N N   . THR A 72  ? 0.1569 0.1899 0.1605 -0.0105 -0.0085 -0.0036 105 THR A N   
550  C CA  . THR A 72  ? 0.1401 0.1737 0.1441 -0.0124 -0.0065 -0.0037 105 THR A CA  
551  C C   . THR A 72  ? 0.1670 0.2054 0.1753 -0.0122 -0.0063 -0.0039 105 THR A C   
552  O O   . THR A 72  ? 0.1722 0.2109 0.1809 -0.0126 -0.0049 -0.0039 105 THR A O   
553  C CB  . THR A 72  ? 0.1605 0.1933 0.1652 -0.0139 -0.0060 -0.0040 105 THR A CB  
554  O OG1 . THR A 72  ? 0.1579 0.1853 0.1573 -0.0139 -0.0066 -0.0038 105 THR A OG1 
555  C CG2 . THR A 72  ? 0.1693 0.2031 0.1776 -0.0160 -0.0034 -0.0040 105 THR A CG2 
556  N N   . GLU A 73  ? 0.1544 0.1949 0.1646 -0.0113 -0.0072 -0.0042 106 GLU A N   
557  C CA  . GLU A 73  ? 0.1442 0.1872 0.1564 -0.0109 -0.0073 -0.0044 106 GLU A CA  
558  C C   . GLU A 73  ? 0.1230 0.1668 0.1353 -0.0105 -0.0072 -0.0040 106 GLU A C   
559  O O   . GLU A 73  ? 0.1524 0.1972 0.1653 -0.0105 -0.0070 -0.0041 106 GLU A O   
560  C CB  . GLU A 73  ? 0.1577 0.1992 0.1682 -0.0099 -0.0079 -0.0046 106 GLU A CB  
561  C CG  . GLU A 73  ? 0.1731 0.2118 0.1821 -0.0104 -0.0097 -0.0052 106 GLU A CG  
562  C CD  . GLU A 73  ? 0.2150 0.2481 0.2179 -0.0090 -0.0100 -0.0053 106 GLU A CD  
563  O OE1 . GLU A 73  ? 0.1939 0.2259 0.1950 -0.0076 -0.0074 -0.0048 106 GLU A OE1 
564  O OE2 . GLU A 73  ? 0.2345 0.2633 0.2345 -0.0091 -0.0130 -0.0060 106 GLU A OE2 
565  N N   . ALA A 74  ? 0.1441 0.1869 0.1563 -0.0100 -0.0080 -0.0035 107 ALA A N   
566  C CA  . ALA A 74  ? 0.1666 0.2093 0.1797 -0.0099 -0.0093 -0.0032 107 ALA A CA  
567  C C   . ALA A 74  ? 0.1279 0.1671 0.1362 -0.0104 -0.0094 -0.0032 107 ALA A C   
568  O O   . ALA A 74  ? 0.1407 0.1792 0.1481 -0.0104 -0.0099 -0.0031 107 ALA A O   
569  C CB  . ALA A 74  ? 0.1316 0.1737 0.1474 -0.0091 -0.0114 -0.0029 107 ALA A CB  
570  N N   . ILE A 75  ? 0.1508 0.1863 0.1551 -0.0108 -0.0084 -0.0032 108 ILE A N   
571  C CA  . ILE A 75  ? 0.1366 0.1669 0.1351 -0.0111 -0.0064 -0.0032 108 ILE A CA  
572  C C   . ILE A 75  ? 0.1434 0.1775 0.1455 -0.0112 -0.0036 -0.0036 108 ILE A C   
573  O O   . ILE A 75  ? 0.1379 0.1691 0.1367 -0.0107 -0.0025 -0.0035 108 ILE A O   
574  C CB  . ILE A 75  ? 0.1427 0.1673 0.1360 -0.0118 -0.0043 -0.0031 108 ILE A CB  
575  C CG1 . ILE A 75  ? 0.1640 0.1832 0.1524 -0.0112 -0.0082 -0.0028 108 ILE A CG1 
576  C CG2 . ILE A 75  ? 0.1886 0.2067 0.1755 -0.0122 0.0000  -0.0029 108 ILE A CG2 
577  C CD1 . ILE A 75  ? 0.1768 0.1902 0.1598 -0.0119 -0.0066 -0.0027 108 ILE A CD1 
578  N N   . GLU A 76  ? 0.1288 0.1684 0.1373 -0.0116 -0.0030 -0.0040 109 GLU A N   
579  C CA  . GLU A 76  ? 0.1266 0.1698 0.1402 -0.0113 -0.0018 -0.0045 109 GLU A CA  
580  C C   . GLU A 76  ? 0.1450 0.1888 0.1575 -0.0102 -0.0035 -0.0046 109 GLU A C   
581  O O   . GLU A 76  ? 0.1266 0.1701 0.1394 -0.0094 -0.0022 -0.0049 109 GLU A O   
582  C CB  . GLU A 76  ? 0.1235 0.1707 0.1434 -0.0118 -0.0031 -0.0051 109 GLU A CB  
583  C CG  . GLU A 76  ? 0.1254 0.1718 0.1470 -0.0133 -0.0017 -0.0050 109 GLU A CG  
584  C CD  . GLU A 76  ? 0.2760 0.3247 0.3029 -0.0139 -0.0046 -0.0056 109 GLU A CD  
585  O OE1 . GLU A 76  ? 0.2546 0.3063 0.2877 -0.0135 -0.0063 -0.0063 109 GLU A OE1 
586  O OE2 . GLU A 76  ? 0.3034 0.3498 0.3273 -0.0146 -0.0059 -0.0055 109 GLU A OE2 
587  N N   . TYR A 77  ? 0.1234 0.1677 0.1352 -0.0101 -0.0058 -0.0043 110 TYR A N   
588  C CA  . TYR A 77  ? 0.1468 0.1908 0.1575 -0.0096 -0.0070 -0.0042 110 TYR A CA  
589  C C   . TYR A 77  ? 0.1510 0.1910 0.1573 -0.0096 -0.0073 -0.0039 110 TYR A C   
590  O O   . TYR A 77  ? 0.1396 0.1781 0.1439 -0.0090 -0.0075 -0.0040 110 TYR A O   
591  C CB  . TYR A 77  ? 0.1219 0.1667 0.1337 -0.0099 -0.0079 -0.0039 110 TYR A CB  
592  C CG  . TYR A 77  ? 0.1355 0.1804 0.1472 -0.0094 -0.0077 -0.0043 110 TYR A CG  
593  C CD1 . TYR A 77  ? 0.1584 0.2015 0.1679 -0.0089 -0.0082 -0.0046 110 TYR A CD1 
594  C CD2 . TYR A 77  ? 0.1701 0.2149 0.1821 -0.0094 -0.0076 -0.0044 110 TYR A CD2 
595  C CE1 . TYR A 77  ? 0.1956 0.2356 0.2021 -0.0081 -0.0089 -0.0051 110 TYR A CE1 
596  C CE2 . TYR A 77  ? 0.1487 0.1907 0.1580 -0.0088 -0.0082 -0.0049 110 TYR A CE2 
597  C CZ  . TYR A 77  ? 0.1861 0.2251 0.1921 -0.0081 -0.0091 -0.0052 110 TYR A CZ  
598  O OH  . TYR A 77  ? 0.1722 0.2053 0.1727 -0.0072 -0.0107 -0.0057 110 TYR A OH  
599  N N   . SER A 78  ? 0.1304 0.1668 0.1335 -0.0100 -0.0081 -0.0035 111 SER A N   
600  C CA  . SER A 78  ? 0.1374 0.1667 0.1334 -0.0098 -0.0095 -0.0032 111 SER A CA  
601  C C   . SER A 78  ? 0.1458 0.1712 0.1370 -0.0088 -0.0058 -0.0035 111 SER A C   
602  O O   . SER A 78  ? 0.1537 0.1743 0.1396 -0.0081 -0.0062 -0.0035 111 SER A O   
603  C CB  . SER A 78  ? 0.1428 0.1665 0.1344 -0.0100 -0.0119 -0.0028 111 SER A CB  
604  O OG  . SER A 78  ? 0.1830 0.1969 0.1654 -0.0097 -0.0145 -0.0026 111 SER A OG  
605  N N   . ARG A 79  ? 0.1419 0.1688 0.1352 -0.0088 -0.0018 -0.0037 112 ARG A N   
606  C CA  . ARG A 79  ? 0.1503 0.1750 0.1426 -0.0077 0.0032  -0.0040 112 ARG A CA  
607  C C   . ARG A 79  ? 0.1652 0.1947 0.1628 -0.0065 0.0028  -0.0046 112 ARG A C   
608  O O   . ARG A 79  ? 0.1477 0.1729 0.1414 -0.0049 0.0051  -0.0048 112 ARG A O   
609  C CB  . ARG A 79  ? 0.1597 0.1873 0.1578 -0.0084 0.0077  -0.0042 112 ARG A CB  
610  C CG  . ARG A 79  ? 0.1600 0.1816 0.1519 -0.0096 0.0088  -0.0036 112 ARG A CG  
611  C CD  . ARG A 79  ? 0.2071 0.2154 0.1839 -0.0089 0.0090  -0.0031 112 ARG A CD  
612  N NE  . ARG A 79  ? 0.2615 0.2614 0.2303 -0.0097 0.0110  -0.0027 112 ARG A NE  
613  C CZ  . ARG A 79  ? 0.2493 0.2365 0.2040 -0.0093 0.0079  -0.0023 112 ARG A CZ  
614  N NH1 . ARG A 79  ? 0.2425 0.2248 0.1910 -0.0084 0.0021  -0.0023 112 ARG A NH1 
615  N NH2 . ARG A 79  ? 0.2730 0.2512 0.2192 -0.0100 0.0101  -0.0019 112 ARG A NH2 
616  N N   . PHE A 80  ? 0.1345 0.1713 0.1396 -0.0068 0.0000  -0.0050 113 PHE A N   
617  C CA  . PHE A 80  ? 0.1329 0.1721 0.1411 -0.0054 -0.0011 -0.0056 113 PHE A CA  
618  C C   . PHE A 80  ? 0.1743 0.2082 0.1748 -0.0050 -0.0030 -0.0053 113 PHE A C   
619  O O   . PHE A 80  ? 0.1586 0.1907 0.1578 -0.0033 -0.0025 -0.0057 113 PHE A O   
620  C CB  . PHE A 80  ? 0.1276 0.1716 0.1413 -0.0058 -0.0043 -0.0060 113 PHE A CB  
621  C CG  . PHE A 80  ? 0.1399 0.1885 0.1626 -0.0055 -0.0040 -0.0068 113 PHE A CG  
622  C CD1 . PHE A 80  ? 0.1663 0.2162 0.1930 -0.0065 -0.0005 -0.0066 113 PHE A CD1 
623  C CD2 . PHE A 80  ? 0.1353 0.1857 0.1621 -0.0046 -0.0077 -0.0077 113 PHE A CD2 
624  C CE1 . PHE A 80  ? 0.1510 0.2056 0.1882 -0.0068 -0.0005 -0.0073 113 PHE A CE1 
625  C CE2 . PHE A 80  ? 0.1508 0.2050 0.1873 -0.0046 -0.0090 -0.0085 113 PHE A CE2 
626  C CZ  . PHE A 80  ? 0.1255 0.1826 0.1684 -0.0059 -0.0054 -0.0083 113 PHE A CZ  
627  N N   . SER A 81  ? 0.1605 0.1919 0.1569 -0.0065 -0.0055 -0.0045 114 SER A N   
628  C CA  . SER A 81  ? 0.1748 0.2007 0.1650 -0.0067 -0.0080 -0.0041 114 SER A CA  
629  C C   . SER A 81  ? 0.2256 0.2431 0.2070 -0.0053 -0.0063 -0.0042 114 SER A C   
630  O O   . SER A 81  ? 0.1978 0.2114 0.1749 -0.0040 -0.0065 -0.0044 114 SER A O   
631  C CB  . SER A 81  ? 0.1824 0.2075 0.1729 -0.0088 -0.0114 -0.0034 114 SER A CB  
632  O OG  . SER A 81  ? 0.1695 0.1888 0.1552 -0.0095 -0.0147 -0.0030 114 SER A OG  
633  N N   . ASP A 82  ? 0.1561 0.1691 0.1332 -0.0051 -0.0040 -0.0040 115 ASP A N   
634  C CA  . ASP A 82  ? 0.1830 0.1853 0.1492 -0.0034 -0.0008 -0.0040 115 ASP A CA  
635  C C   . ASP A 82  ? 0.1853 0.1899 0.1552 -0.0010 0.0043  -0.0047 115 ASP A C   
636  O O   . ASP A 82  ? 0.1813 0.1780 0.1430 0.0010  0.0057  -0.0048 115 ASP A O   
637  C CB  . ASP A 82  ? 0.1925 0.1885 0.1529 -0.0036 0.0023  -0.0037 115 ASP A CB  
638  C CG  . ASP A 82  ? 0.2758 0.2658 0.2298 -0.0052 -0.0037 -0.0031 115 ASP A CG  
639  O OD1 . ASP A 82  ? 0.2204 0.2090 0.1734 -0.0060 -0.0100 -0.0029 115 ASP A OD1 
640  O OD2 . ASP A 82  ? 0.2468 0.2331 0.1975 -0.0056 -0.0023 -0.0029 115 ASP A OD2 
641  N N   . TRP A 83  ? 0.1626 0.1773 0.1451 -0.0008 0.0069  -0.0052 116 TRP A N   
642  C CA  . TRP A 83  ? 0.1620 0.1800 0.1515 0.0017  0.0113  -0.0060 116 TRP A CA  
643  C C   . TRP A 83  ? 0.1576 0.1778 0.1489 0.0032  0.0073  -0.0066 116 TRP A C   
644  O O   . TRP A 83  ? 0.1792 0.1981 0.1719 0.0061  0.0101  -0.0073 116 TRP A O   
645  C CB  . TRP A 83  ? 0.1576 0.1852 0.1616 0.0011  0.0139  -0.0064 116 TRP A CB  
646  C CG  . TRP A 83  ? 0.1572 0.1812 0.1582 -0.0005 0.0185  -0.0058 116 TRP A CG  
647  C CD1 . TRP A 83  ? 0.1964 0.2080 0.1831 -0.0003 0.0222  -0.0050 116 TRP A CD1 
648  C CD2 . TRP A 83  ? 0.1517 0.1821 0.1621 -0.0026 0.0194  -0.0057 116 TRP A CD2 
649  N NE1 . TRP A 83  ? 0.2454 0.2552 0.2317 -0.0021 0.0258  -0.0046 116 TRP A NE1 
650  C CE2 . TRP A 83  ? 0.2054 0.2274 0.2069 -0.0036 0.0242  -0.0049 116 TRP A CE2 
651  C CE3 . TRP A 83  ? 0.1422 0.1828 0.1659 -0.0037 0.0161  -0.0063 116 TRP A CE3 
652  C CZ2 . TRP A 83  ? 0.1588 0.1831 0.1651 -0.0059 0.0262  -0.0047 116 TRP A CZ2 
653  C CZ3 . TRP A 83  ? 0.1405 0.1837 0.1695 -0.0059 0.0177  -0.0060 116 TRP A CZ3 
654  C CH2 . TRP A 83  ? 0.1873 0.2228 0.2081 -0.0071 0.0230  -0.0052 116 TRP A CH2 
655  N N   . LYS A 84  ? 0.1780 0.2005 0.1689 0.0014  0.0016  -0.0064 117 LYS A N   
656  C CA  . LYS A 84  ? 0.1988 0.2199 0.1874 0.0024  -0.0019 -0.0068 117 LYS A CA  
657  C C   . LYS A 84  ? 0.2173 0.2282 0.1938 0.0035  -0.0017 -0.0065 117 LYS A C   
658  O O   . LYS A 84  ? 0.1987 0.2065 0.1728 0.0059  -0.0017 -0.0071 117 LYS A O   
659  C CB  . LYS A 84  ? 0.1600 0.1835 0.1489 -0.0001 -0.0065 -0.0063 117 LYS A CB  
660  C CG  . LYS A 84  ? 0.1993 0.2296 0.1966 -0.0003 -0.0078 -0.0069 117 LYS A CG  
661  C CD  . LYS A 84  ? 0.1928 0.2228 0.1918 0.0022  -0.0100 -0.0079 117 LYS A CD  
662  C CE  . LYS A 84  ? 0.2022 0.2360 0.2069 0.0020  -0.0128 -0.0085 117 LYS A CE  
663  N NZ  . LYS A 84  ? 0.2139 0.2446 0.2178 0.0046  -0.0167 -0.0096 117 LYS A NZ  
664  N N   . LEU A 85  ? 0.1993 0.2034 0.1672 0.0017  -0.0023 -0.0056 118 LEU A N   
665  C CA  . LEU A 85  ? 0.2307 0.2224 0.1850 0.0026  -0.0031 -0.0053 118 LEU A CA  
666  C C   . LEU A 85  ? 0.3182 0.3035 0.2674 0.0063  0.0033  -0.0058 118 LEU A C   
667  O O   . LEU A 85  ? 0.3190 0.2952 0.2586 0.0085  0.0035  -0.0060 118 LEU A O   
668  C CB  . LEU A 85  ? 0.1986 0.1830 0.1449 0.0001  -0.0069 -0.0044 118 LEU A CB  
669  C CG  . LEU A 85  ? 0.2274 0.2177 0.1802 -0.0033 -0.0127 -0.0039 118 LEU A CG  
670  C CD1 . LEU A 85  ? 0.2809 0.2670 0.2310 -0.0056 -0.0170 -0.0032 118 LEU A CD1 
671  C CD2 . LEU A 85  ? 0.2369 0.2241 0.1868 -0.0039 -0.0159 -0.0038 118 LEU A CD2 
672  N N   . ASN A 86  ? 0.2697 0.2588 0.2251 0.0071  0.0093  -0.0060 119 ASN A N   
673  C CA  . ASN A 86  ? 0.2896 0.2726 0.2419 0.0105  0.0175  -0.0063 119 ASN A CA  
674  C C   . ASN A 86  ? 0.2562 0.2512 0.2260 0.0111  0.0231  -0.0068 119 ASN A C   
675  O O   . ASN A 86  ? 0.2517 0.2464 0.2227 0.0097  0.0275  -0.0064 119 ASN A O   
676  C CB  . ASN A 86  ? 0.3243 0.2913 0.2588 0.0105  0.0204  -0.0055 119 ASN A CB  
677  C CG  . ASN A 86  ? 0.4027 0.3610 0.3318 0.0142  0.0308  -0.0057 119 ASN A CG  
678  O OD1 . ASN A 86  ? 0.4186 0.3829 0.3580 0.0172  0.0353  -0.0065 119 ASN A OD1 
679  N ND2 . ASN A 86  ? 0.4377 0.3803 0.3500 0.0143  0.0350  -0.0050 119 ASN A ND2 
680  N N   . PRO A 87  ? 0.2484 0.2532 0.2321 0.0130  0.0225  -0.0079 120 PRO A N   
681  C CA  . PRO A 87  ? 0.2186 0.2354 0.2217 0.0132  0.0258  -0.0085 120 PRO A CA  
682  C C   . PRO A 87  ? 0.2754 0.2892 0.2817 0.0148  0.0367  -0.0083 120 PRO A C   
683  O O   . PRO A 87  ? 0.2693 0.2913 0.2898 0.0133  0.0402  -0.0084 120 PRO A O   
684  C CB  . PRO A 87  ? 0.2578 0.2815 0.2719 0.0159  0.0216  -0.0098 120 PRO A CB  
685  C CG  . PRO A 87  ? 0.2546 0.2727 0.2555 0.0151  0.0142  -0.0095 120 PRO A CG  
686  C CD  . PRO A 87  ? 0.2823 0.2873 0.2650 0.0146  0.0168  -0.0085 120 PRO A CD  
687  N N   . ALA A 88  ? 0.3047 0.3057 0.2974 0.0176  0.0428  -0.0081 121 ALA A N   
688  C CA  . ALA A 88  ? 0.3211 0.3163 0.3140 0.0192  0.0551  -0.0078 121 ALA A CA  
689  C C   . ALA A 88  ? 0.3361 0.3255 0.3209 0.0157  0.0583  -0.0067 121 ALA A C   
690  O O   . ALA A 88  ? 0.3471 0.3332 0.3347 0.0161  0.0692  -0.0063 121 ALA A O   
691  C CB  . ALA A 88  ? 0.3193 0.2980 0.2942 0.0232  0.0608  -0.0077 121 ALA A CB  
692  N N   . SER A 89  ? 0.3014 0.2884 0.2760 0.0125  0.0497  -0.0061 122 SER A N   
693  C CA  . SER A 89  ? 0.3299 0.3098 0.2951 0.0096  0.0515  -0.0051 122 SER A CA  
694  C C   . SER A 89  ? 0.3131 0.3073 0.2958 0.0064  0.0499  -0.0052 122 SER A C   
695  O O   . SER A 89  ? 0.3023 0.2914 0.2788 0.0040  0.0517  -0.0044 122 SER A O   
696  C CB  . SER A 89  ? 0.3214 0.2902 0.2671 0.0081  0.0426  -0.0045 122 SER A CB  
697  O OG  . SER A 89  ? 0.3185 0.2990 0.2730 0.0062  0.0325  -0.0048 122 SER A OG  
698  N N   . ALA A 90  ? 0.2282 0.2384 0.2310 0.0064  0.0461  -0.0061 123 ALA A N   
699  C CA  . ALA A 90  ? 0.2234 0.2454 0.2419 0.0035  0.0442  -0.0062 123 ALA A CA  
700  C C   . ALA A 90  ? 0.3163 0.3378 0.3428 0.0028  0.0552  -0.0058 123 ALA A C   
701  O O   . ALA A 90  ? 0.2748 0.2978 0.3109 0.0053  0.0630  -0.0062 123 ALA A O   
702  C CB  . ALA A 90  ? 0.2366 0.2725 0.2728 0.0041  0.0376  -0.0073 123 ALA A CB  
703  N N   . PRO A 91  ? 0.2850 0.3041 0.3085 -0.0004 0.0568  -0.0051 124 PRO A N   
704  C CA  . PRO A 91  ? 0.3594 0.3731 0.3846 -0.0014 0.0689  -0.0044 124 PRO A CA  
705  C C   . PRO A 91  ? 0.3539 0.3826 0.4066 -0.0030 0.0716  -0.0049 124 PRO A C   
706  O O   . PRO A 91  ? 0.3123 0.3540 0.3793 -0.0038 0.0623  -0.0058 124 PRO A O   
707  C CB  . PRO A 91  ? 0.3132 0.3163 0.3210 -0.0042 0.0671  -0.0034 124 PRO A CB  
708  C CG  . PRO A 91  ? 0.3309 0.3442 0.3439 -0.0058 0.0546  -0.0038 124 PRO A CG  
709  C CD  . PRO A 91  ? 0.2919 0.3113 0.3085 -0.0032 0.0482  -0.0047 124 PRO A CD  
710  N N   . PRO A 92  ? 0.3537 0.3803 0.4143 -0.0035 0.0843  -0.0044 125 PRO A N   
711  C CA  . PRO A 92  ? 0.3439 0.3851 0.4334 -0.0058 0.0865  -0.0049 125 PRO A CA  
712  C C   . PRO A 92  ? 0.3476 0.3946 0.4407 -0.0101 0.0777  -0.0048 125 PRO A C   
713  O O   . PRO A 92  ? 0.3227 0.3598 0.3979 -0.0123 0.0774  -0.0038 125 PRO A O   
714  C CB  . PRO A 92  ? 0.3719 0.4052 0.4630 -0.0063 0.1034  -0.0039 125 PRO A CB  
715  C CG  . PRO A 92  ? 0.4145 0.4316 0.4824 -0.0022 0.1100  -0.0035 125 PRO A CG  
716  C CD  . PRO A 92  ? 0.3954 0.4050 0.4394 -0.0018 0.0975  -0.0035 125 PRO A CD  
717  N N   . GLU A 93  ? 0.3098 0.3714 0.4251 -0.0108 0.0701  -0.0059 126 GLU A N   
718  C CA  . GLU A 93  ? 0.2952 0.3615 0.4132 -0.0143 0.0605  -0.0060 126 GLU A CA  
719  C C   . GLU A 93  ? 0.3568 0.4277 0.4927 -0.0184 0.0661  -0.0056 126 GLU A C   
720  O O   . GLU A 93  ? 0.3174 0.3920 0.4705 -0.0184 0.0761  -0.0055 126 GLU A O   
721  C CB  . GLU A 93  ? 0.2697 0.3460 0.3978 -0.0127 0.0474  -0.0074 126 GLU A CB  
722  C CG  . GLU A 93  ? 0.3043 0.3932 0.4622 -0.0126 0.0458  -0.0086 126 GLU A CG  
723  C CD  . GLU A 93  ? 0.3983 0.4900 0.5672 -0.0087 0.0532  -0.0091 126 GLU A CD  
724  O OE1 . GLU A 93  ? 0.4663 0.5489 0.6171 -0.0060 0.0592  -0.0085 126 GLU A OE1 
725  O OE2 . GLU A 93  ? 0.4299 0.5324 0.6257 -0.0082 0.0524  -0.0102 126 GLU A OE2 
726  N N   . PRO A 94  ? 0.2110 0.2813 0.3438 -0.0221 0.0605  -0.0053 127 PRO A N   
727  C CA  . PRO A 94  ? 0.2824 0.3572 0.4333 -0.0266 0.0645  -0.0049 127 PRO A CA  
728  C C   . PRO A 94  ? 0.2406 0.3303 0.4223 -0.0267 0.0589  -0.0063 127 PRO A C   
729  O O   . PRO A 94  ? 0.2576 0.3527 0.4422 -0.0236 0.0484  -0.0076 127 PRO A O   
730  C CB  . PRO A 94  ? 0.2360 0.3057 0.3731 -0.0296 0.0568  -0.0045 127 PRO A CB  
731  C CG  . PRO A 94  ? 0.2400 0.3090 0.3627 -0.0264 0.0457  -0.0052 127 PRO A CG  
732  C CD  . PRO A 94  ? 0.2014 0.2669 0.3150 -0.0222 0.0503  -0.0052 127 PRO A CD  
733  N N   . PRO A 95  ? 0.2581 0.3539 0.4636 -0.0301 0.0655  -0.0061 128 PRO A N   
734  C CA  . PRO A 95  ? 0.2701 0.3803 0.5080 -0.0302 0.0586  -0.0076 128 PRO A CA  
735  C C   . PRO A 95  ? 0.3254 0.4387 0.5641 -0.0312 0.0410  -0.0087 128 PRO A C   
736  O O   . PRO A 95  ? 0.2215 0.3430 0.4772 -0.0292 0.0309  -0.0103 128 PRO A O   
737  C CB  . PRO A 95  ? 0.2393 0.3538 0.5009 -0.0348 0.0700  -0.0068 128 PRO A CB  
738  C CG  . PRO A 95  ? 0.2988 0.4001 0.5369 -0.0384 0.0774  -0.0050 128 PRO A CG  
739  C CD  . PRO A 95  ? 0.2377 0.3268 0.4419 -0.0344 0.0784  -0.0045 128 PRO A CD  
740  N N   . ASP A 96  ? 0.1749 0.2801 0.3942 -0.0339 0.0369  -0.0079 129 ASP A N   
741  C CA  . ASP A 96  ? 0.2353 0.3397 0.4496 -0.0344 0.0214  -0.0088 129 ASP A CA  
742  C C   . ASP A 96  ? 0.2478 0.3409 0.4335 -0.0356 0.0214  -0.0077 129 ASP A C   
743  O O   . ASP A 96  ? 0.2204 0.3066 0.3917 -0.0359 0.0319  -0.0064 129 ASP A O   
744  C CB  . ASP A 96  ? 0.2134 0.3247 0.4534 -0.0385 0.0146  -0.0096 129 ASP A CB  
745  C CG  . ASP A 96  ? 0.2930 0.4028 0.5401 -0.0442 0.0245  -0.0082 129 ASP A CG  
746  O OD1 . ASP A 96  ? 0.2906 0.3906 0.5163 -0.0463 0.0255  -0.0071 129 ASP A OD1 
747  O OD2 . ASP A 96  ? 0.2804 0.3986 0.5553 -0.0465 0.0314  -0.0081 129 ASP A OD2 
748  N N   . LEU A 97  ? 0.1641 0.2539 0.3407 -0.0358 0.0094  -0.0083 130 LEU A N   
749  C CA  . LEU A 97  ? 0.1933 0.2730 0.3445 -0.0362 0.0086  -0.0074 130 LEU A CA  
750  C C   . LEU A 97  ? 0.1773 0.2531 0.3294 -0.0409 0.0066  -0.0070 130 LEU A C   
751  O O   . LEU A 97  ? 0.1645 0.2320 0.2972 -0.0409 0.0035  -0.0066 130 LEU A O   
752  C CB  . LEU A 97  ? 0.1941 0.2706 0.3300 -0.0325 -0.0012 -0.0082 130 LEU A CB  
753  C CG  . LEU A 97  ? 0.2465 0.3242 0.3759 -0.0281 0.0011  -0.0084 130 LEU A CG  
754  C CD1 . LEU A 97  ? 0.2496 0.3226 0.3625 -0.0252 -0.0072 -0.0089 130 LEU A CD1 
755  C CD2 . LEU A 97  ? 0.2185 0.2923 0.3371 -0.0277 0.0125  -0.0071 130 LEU A CD2 
756  N N   . SER A 98  ? 0.1793 0.2867 0.2967 0.0335  -0.0562 -0.0168 131 SER A N   
757  C CA  . SER A 98  ? 0.1749 0.2885 0.2872 0.0232  -0.0524 -0.0141 131 SER A CA  
758  C C   . SER A 98  ? 0.1823 0.2953 0.2882 0.0201  -0.0430 -0.0156 131 SER A C   
759  O O   . SER A 98  ? 0.1844 0.2878 0.2792 0.0119  -0.0402 -0.0127 131 SER A O   
760  C CB  . SER A 98  ? 0.1511 0.2877 0.2792 0.0227  -0.0545 -0.0143 131 SER A CB  
761  O OG  . SER A 98  ? 0.1912 0.3317 0.3177 0.0116  -0.0526 -0.0114 131 SER A OG  
762  N N   . ALA A 99  ? 0.1564 0.2795 0.2683 0.0277  -0.0385 -0.0207 132 ALA A N   
763  C CA  . ALA A 99  ? 0.1878 0.3114 0.2919 0.0264  -0.0302 -0.0217 132 ALA A CA  
764  C C   . ALA A 99  ? 0.1791 0.2803 0.2701 0.0246  -0.0305 -0.0218 132 ALA A C   
765  O O   . ALA A 99  ? 0.1591 0.2550 0.2405 0.0189  -0.0254 -0.0195 132 ALA A O   
766  C CB  . ALA A 99  ? 0.1880 0.3285 0.2987 0.0373  -0.0262 -0.0283 132 ALA A CB  
767  N N   . SER A 100 ? 0.1664 0.2547 0.2587 0.0293  -0.0363 -0.0238 133 SER A N   
768  C CA  . SER A 100 ? 0.1605 0.2293 0.2441 0.0268  -0.0364 -0.0225 133 SER A CA  
769  C C   . SER A 100 ? 0.1817 0.2406 0.2542 0.0174  -0.0356 -0.0154 133 SER A C   
770  O O   . SER A 100 ? 0.1571 0.2064 0.2205 0.0134  -0.0318 -0.0141 133 SER A O   
771  C CB  . SER A 100 ? 0.2000 0.2575 0.2914 0.0329  -0.0431 -0.0240 133 SER A CB  
772  O OG  . SER A 100 ? 0.2059 0.2696 0.3069 0.0427  -0.0448 -0.0333 133 SER A OG  
773  N N   . ARG A 101 ? 0.1497 0.2112 0.2227 0.0147  -0.0399 -0.0116 134 ARG A N   
774  C CA  . ARG A 101 ? 0.1555 0.2089 0.2163 0.0072  -0.0400 -0.0071 134 ARG A CA  
775  C C   . ARG A 101 ? 0.1713 0.2280 0.2278 0.0007  -0.0345 -0.0080 134 ARG A C   
776  O O   . ARG A 101 ? 0.1678 0.2133 0.2130 -0.0037 -0.0319 -0.0066 134 ARG A O   
777  C CB  . ARG A 101 ? 0.1774 0.2354 0.2396 0.0066  -0.0473 -0.0045 134 ARG A CB  
778  C CG  . ARG A 101 ? 0.1917 0.2418 0.2539 0.0122  -0.0530 -0.0004 134 ARG A CG  
779  C CD  . ARG A 101 ? 0.2294 0.2838 0.2890 0.0121  -0.0611 0.0029  134 ARG A CD  
780  N NE  . ARG A 101 ? 0.2788 0.3483 0.3547 0.0169  -0.0664 0.0005  134 ARG A NE  
781  C CZ  . ARG A 101 ? 0.2933 0.3788 0.3777 0.0139  -0.0685 -0.0025 134 ARG A CZ  
782  N NH1 . ARG A 101 ? 0.1795 0.2663 0.2581 0.0054  -0.0667 -0.0038 134 ARG A NH1 
783  N NH2 . ARG A 101 ? 0.2525 0.3533 0.3537 0.0196  -0.0729 -0.0043 134 ARG A NH2 
784  N N   . SER A 102 ? 0.1636 0.2362 0.2301 0.0005  -0.0324 -0.0094 135 SER A N   
785  C CA  . SER A 102 ? 0.1440 0.2195 0.2087 -0.0058 -0.0269 -0.0080 135 SER A CA  
786  C C   . SER A 102 ? 0.1853 0.2522 0.2415 -0.0042 -0.0210 -0.0086 135 SER A C   
787  O O   . SER A 102 ? 0.1556 0.2132 0.2039 -0.0095 -0.0183 -0.0067 135 SER A O   
788  C CB  . SER A 102 ? 0.1897 0.2865 0.2687 -0.0056 -0.0241 -0.0072 135 SER A CB  
789  O OG  . SER A 102 ? 0.1807 0.2799 0.2595 -0.0120 -0.0182 -0.0033 135 SER A OG  
790  N N   . ALA A 103 ? 0.1554 0.2252 0.2140 0.0037  -0.0200 -0.0121 136 ALA A N   
791  C CA  . ALA A 103 ? 0.1598 0.2233 0.2116 0.0061  -0.0160 -0.0139 136 ALA A CA  
792  C C   . ALA A 103 ? 0.1947 0.2402 0.2380 0.0028  -0.0169 -0.0125 136 ALA A C   
793  O O   . ALA A 103 ? 0.1560 0.1952 0.1922 0.0004  -0.0132 -0.0114 136 ALA A O   
794  C CB  . ALA A 103 ? 0.1506 0.2199 0.2076 0.0158  -0.0173 -0.0203 136 ALA A CB  
795  N N   . ILE A 104 ? 0.1773 0.2152 0.2212 0.0033  -0.0213 -0.0116 137 ILE A N   
796  C CA  . ILE A 104 ? 0.1836 0.2074 0.2196 0.0007  -0.0207 -0.0089 137 ILE A CA  
797  C C   . ILE A 104 ? 0.2093 0.2284 0.2350 -0.0055 -0.0186 -0.0069 137 ILE A C   
798  O O   . ILE A 104 ? 0.1905 0.2013 0.2094 -0.0068 -0.0152 -0.0065 137 ILE A O   
799  C CB  . ILE A 104 ? 0.1717 0.1902 0.2101 0.0026  -0.0252 -0.0058 137 ILE A CB  
800  C CG1 . ILE A 104 ? 0.1905 0.2082 0.2408 0.0085  -0.0276 -0.0085 137 ILE A CG1 
801  C CG2 . ILE A 104 ? 0.2001 0.2077 0.2283 -0.0004 -0.0230 -0.0010 137 ILE A CG2 
802  C CD1 . ILE A 104 ? 0.4355 0.4474 0.4917 0.0108  -0.0325 -0.0040 137 ILE A CD1 
803  N N   . ASP A 105 ? 0.1554 0.1798 0.1816 -0.0090 -0.0215 -0.0064 138 ASP A N   
804  C CA  . ASP A 105 ? 0.1793 0.1976 0.1975 -0.0148 -0.0213 -0.0063 138 ASP A CA  
805  C C   . ASP A 105 ? 0.1990 0.2156 0.2171 -0.0169 -0.0161 -0.0063 138 ASP A C   
806  O O   . ASP A 105 ? 0.2041 0.2098 0.2139 -0.0186 -0.0141 -0.0067 138 ASP A O   
807  C CB  . ASP A 105 ? 0.2222 0.2480 0.2453 -0.0186 -0.0269 -0.0068 138 ASP A CB  
808  C CG  . ASP A 105 ? 0.2835 0.3019 0.3011 -0.0247 -0.0288 -0.0086 138 ASP A CG  
809  O OD1 . ASP A 105 ? 0.3077 0.3167 0.3129 -0.0242 -0.0315 -0.0106 138 ASP A OD1 
810  O OD2 . ASP A 105 ? 0.2996 0.3218 0.3255 -0.0297 -0.0276 -0.0080 138 ASP A OD2 
811  N N   A SER A 106 ? 0.1671 0.1951 0.1938 -0.0157 -0.0136 -0.0054 139 SER A N   
812  N N   B SER A 106 ? 0.1668 0.1947 0.1934 -0.0157 -0.0136 -0.0053 139 SER A N   
813  C CA  A SER A 106 ? 0.1971 0.2251 0.2229 -0.0168 -0.0085 -0.0032 139 SER A CA  
814  C CA  B SER A 106 ? 0.1970 0.2246 0.2227 -0.0169 -0.0085 -0.0032 139 SER A CA  
815  C C   A SER A 106 ? 0.1886 0.2075 0.2072 -0.0126 -0.0059 -0.0045 139 SER A C   
816  C C   B SER A 106 ? 0.1886 0.2073 0.2071 -0.0127 -0.0059 -0.0045 139 SER A C   
817  O O   A SER A 106 ? 0.1744 0.1849 0.1879 -0.0144 -0.0035 -0.0031 139 SER A O   
818  O O   B SER A 106 ? 0.1739 0.1844 0.1873 -0.0143 -0.0034 -0.0031 139 SER A O   
819  C CB  A SER A 106 ? 0.1869 0.2320 0.2212 -0.0141 -0.0055 -0.0013 139 SER A CB  
820  C CB  B SER A 106 ? 0.1874 0.2322 0.2217 -0.0146 -0.0054 -0.0010 139 SER A CB  
821  O OG  A SER A 106 ? 0.2136 0.2598 0.2453 -0.0140 -0.0002 0.0026  139 SER A OG  
822  O OG  B SER A 106 ? 0.1983 0.2531 0.2425 -0.0196 -0.0071 0.0013  139 SER A OG  
823  N N   . LEU A 107 ? 0.1542 0.1743 0.1743 -0.0072 -0.0071 -0.0073 140 LEU A N   
824  C CA  . LEU A 107 ? 0.1447 0.1587 0.1622 -0.0036 -0.0055 -0.0089 140 LEU A CA  
825  C C   . LEU A 107 ? 0.1534 0.1551 0.1650 -0.0058 -0.0049 -0.0082 140 LEU A C   
826  O O   . LEU A 107 ? 0.1618 0.1582 0.1708 -0.0045 -0.0025 -0.0084 140 LEU A O   
827  C CB  . LEU A 107 ? 0.1545 0.1734 0.1792 0.0025  -0.0082 -0.0129 140 LEU A CB  
828  C CG  . LEU A 107 ? 0.1772 0.2094 0.2051 0.0077  -0.0079 -0.0157 140 LEU A CG  
829  C CD1 . LEU A 107 ? 0.1405 0.1771 0.1770 0.0140  -0.0124 -0.0216 140 LEU A CD1 
830  C CD2 . LEU A 107 ? 0.1828 0.2156 0.2053 0.0106  -0.0053 -0.0161 140 LEU A CD2 
831  N N   . ASN A 108 ? 0.1705 0.1691 0.1795 -0.0080 -0.0071 -0.0072 141 ASN A N   
832  C CA  . ASN A 108 ? 0.1680 0.1572 0.1682 -0.0093 -0.0056 -0.0065 141 ASN A CA  
833  C C   . ASN A 108 ? 0.2003 0.1833 0.1946 -0.0116 -0.0037 -0.0077 141 ASN A C   
834  O O   . ASN A 108 ? 0.1917 0.1682 0.1818 -0.0099 -0.0006 -0.0084 141 ASN A O   
835  C CB  . ASN A 108 ? 0.1879 0.1767 0.1827 -0.0109 -0.0092 -0.0056 141 ASN A CB  
836  C CG  . ASN A 108 ? 0.2302 0.2215 0.2291 -0.0082 -0.0109 -0.0023 141 ASN A CG  
837  O OD1 . ASN A 108 ? 0.2053 0.1967 0.2120 -0.0057 -0.0093 -0.0011 141 ASN A OD1 
838  N ND2 . ASN A 108 ? 0.2190 0.2117 0.2135 -0.0086 -0.0151 -0.0007 141 ASN A ND2 
839  N N   . ASN A 109 ? 0.1786 0.1637 0.1747 -0.0155 -0.0058 -0.0077 142 ASN A N   
840  C CA  . ASN A 109 ? 0.2201 0.1970 0.2133 -0.0185 -0.0052 -0.0082 142 ASN A CA  
841  C C   . ASN A 109 ? 0.2134 0.1890 0.2081 -0.0158 -0.0011 -0.0061 142 ASN A C   
842  O O   . ASN A 109 ? 0.2161 0.1817 0.2066 -0.0150 0.0003  -0.0069 142 ASN A O   
843  C CB  . ASN A 109 ? 0.2324 0.2129 0.2320 -0.0245 -0.0085 -0.0070 142 ASN A CB  
844  C CG  . ASN A 109 ? 0.4100 0.3793 0.4095 -0.0287 -0.0092 -0.0073 142 ASN A CG  
845  O OD1 . ASN A 109 ? 0.5311 0.4904 0.5249 -0.0302 -0.0131 -0.0124 142 ASN A OD1 
846  N ND2 . ASN A 109 ? 0.5261 0.4967 0.5314 -0.0298 -0.0059 -0.0018 142 ASN A ND2 
847  N N   . ARG A 110 ? 0.1614 0.1475 0.1616 -0.0131 0.0001  -0.0040 143 ARG A N   
848  C CA  . ARG A 110 ? 0.2055 0.1921 0.2054 -0.0092 0.0028  -0.0023 143 ARG A CA  
849  C C   . ARG A 110 ? 0.1895 0.1701 0.1872 -0.0051 0.0037  -0.0051 143 ARG A C   
850  O O   . ARG A 110 ? 0.1836 0.1581 0.1789 -0.0031 0.0052  -0.0043 143 ARG A O   
851  C CB  . ARG A 110 ? 0.1804 0.1812 0.1844 -0.0055 0.0032  -0.0015 143 ARG A CB  
852  C CG  . ARG A 110 ? 0.3129 0.3166 0.3145 0.0005  0.0046  -0.0007 143 ARG A CG  
853  C CD  . ARG A 110 ? 0.4310 0.4485 0.4321 0.0036  0.0065  0.0029  143 ARG A CD  
854  N NE  . ARG A 110 ? 0.4916 0.5215 0.4976 0.0035  0.0062  0.0015  143 ARG A NE  
855  C CZ  . ARG A 110 ? 0.5276 0.5695 0.5347 0.0105  0.0050  -0.0034 143 ARG A CZ  
856  N NH1 . ARG A 110 ? 0.4129 0.4560 0.4169 0.0178  0.0027  -0.0083 143 ARG A NH1 
857  N NH2 . ARG A 110 ? 0.4262 0.4798 0.4387 0.0109  0.0051  -0.0043 143 ARG A NH2 
858  N N   . MET A 111 ? 0.1553 0.1379 0.1552 -0.0037 0.0029  -0.0075 144 MET A N   
859  C CA  . MET A 111 ? 0.1658 0.1453 0.1673 -0.0006 0.0045  -0.0088 144 MET A CA  
860  C C   . MET A 111 ? 0.1807 0.1507 0.1751 -0.0012 0.0071  -0.0093 144 MET A C   
861  O O   . MET A 111 ? 0.1889 0.1560 0.1840 0.0021  0.0092  -0.0099 144 MET A O   
862  C CB  . MET A 111 ? 0.1505 0.1337 0.1582 -0.0002 0.0035  -0.0089 144 MET A CB  
863  C CG  . MET A 111 ? 0.1665 0.1575 0.1836 0.0025  0.0001  -0.0110 144 MET A CG  
864  S SD  . MET A 111 ? 0.2033 0.1954 0.2302 0.0021  -0.0025 -0.0102 144 MET A SD  
865  C CE  . MET A 111 ? 0.1827 0.1712 0.2156 0.0020  0.0012  -0.0074 144 MET A CE  
866  N N   . LEU A 112 ? 0.1695 0.1354 0.1573 -0.0043 0.0062  -0.0099 145 LEU A N   
867  C CA  . LEU A 112 ? 0.1895 0.1467 0.1688 -0.0032 0.0080  -0.0127 145 LEU A CA  
868  C C   . LEU A 112 ? 0.2404 0.1888 0.2188 -0.0029 0.0077  -0.0138 145 LEU A C   
869  O O   . LEU A 112 ? 0.1943 0.1367 0.1700 0.0012  0.0101  -0.0162 145 LEU A O   
870  C CB  . LEU A 112 ? 0.2080 0.1631 0.1790 -0.0059 0.0052  -0.0146 145 LEU A CB  
871  C CG  . LEU A 112 ? 0.3478 0.2958 0.3067 -0.0030 0.0063  -0.0193 145 LEU A CG  
872  C CD1 . LEU A 112 ? 0.3038 0.2567 0.2612 0.0021  0.0127  -0.0173 145 LEU A CD1 
873  C CD2 . LEU A 112 ? 0.2875 0.2346 0.2376 -0.0054 0.0011  -0.0222 145 LEU A CD2 
874  N N   . SER A 113 ? 0.2125 0.1607 0.1942 -0.0066 0.0052  -0.0112 146 SER A N   
875  C CA  . SER A 113 ? 0.1978 0.1367 0.1803 -0.0066 0.0049  -0.0098 146 SER A CA  
876  C C   . SER A 113 ? 0.2221 0.1633 0.2074 -0.0008 0.0074  -0.0075 146 SER A C   
877  O O   . SER A 113 ? 0.2332 0.1651 0.2176 0.0023  0.0078  -0.0079 146 SER A O   
878  C CB  . SER A 113 ? 0.2400 0.1801 0.2274 -0.0127 0.0027  -0.0051 146 SER A CB  
879  O OG  . SER A 113 ? 0.2884 0.2423 0.2801 -0.0123 0.0041  -0.0004 146 SER A OG  
880  N N   . GLN A 114 ? 0.1804 0.1336 0.1697 0.0014  0.0079  -0.0061 147 GLN A N   
881  C CA  . GLN A 114 ? 0.2067 0.1633 0.1993 0.0075  0.0085  -0.0054 147 GLN A CA  
882  C C   . GLN A 114 ? 0.2468 0.2009 0.2411 0.0114  0.0107  -0.0092 147 GLN A C   
883  O O   . GLN A 114 ? 0.2337 0.1857 0.2303 0.0164  0.0110  -0.0092 147 GLN A O   
884  C CB  . GLN A 114 ? 0.1970 0.1667 0.1943 0.0095  0.0069  -0.0055 147 GLN A CB  
885  C CG  . GLN A 114 ? 0.2092 0.1848 0.2041 0.0092  0.0060  -0.0011 147 GLN A CG  
886  C CD  . GLN A 114 ? 0.2442 0.2149 0.2357 0.0120  0.0065  0.0041  147 GLN A CD  
887  O OE1 . GLN A 114 ? 0.2787 0.2504 0.2709 0.0181  0.0052  0.0032  147 GLN A OE1 
888  N NE2 . GLN A 114 ? 0.3075 0.2725 0.2969 0.0075  0.0077  0.0102  147 GLN A NE2 
889  N N   . ILE A 115 ? 0.2030 0.1591 0.1968 0.0097  0.0125  -0.0115 148 ILE A N   
890  C CA  . ILE A 115 ? 0.1900 0.1465 0.1853 0.0134  0.0164  -0.0137 148 ILE A CA  
891  C C   . ILE A 115 ? 0.2420 0.1876 0.2310 0.0167  0.0176  -0.0166 148 ILE A C   
892  O O   . ILE A 115 ? 0.2259 0.1719 0.2192 0.0224  0.0198  -0.0179 148 ILE A O   
893  C CB  . ILE A 115 ? 0.1794 0.1400 0.1723 0.0110  0.0187  -0.0134 148 ILE A CB  
894  C CG1 . ILE A 115 ? 0.1885 0.1589 0.1923 0.0094  0.0176  -0.0105 148 ILE A CG1 
895  C CG2 . ILE A 115 ? 0.2015 0.1622 0.1913 0.0153  0.0245  -0.0151 148 ILE A CG2 
896  C CD1 . ILE A 115 ? 0.2037 0.1769 0.2055 0.0065  0.0189  -0.0078 148 ILE A CD1 
897  N N   . TRP A 116 ? 0.2126 0.1480 0.1930 0.0134  0.0155  -0.0186 149 TRP A N   
898  C CA  . TRP A 116 ? 0.2182 0.1406 0.1940 0.0170  0.0151  -0.0230 149 TRP A CA  
899  C C   . TRP A 116 ? 0.2528 0.1693 0.2343 0.0196  0.0132  -0.0196 149 TRP A C   
900  O O   . TRP A 116 ? 0.2304 0.1405 0.2130 0.0260  0.0141  -0.0224 149 TRP A O   
901  C CB  . TRP A 116 ? 0.2299 0.1415 0.1979 0.0125  0.0112  -0.0270 149 TRP A CB  
902  C CG  . TRP A 116 ? 0.2748 0.1729 0.2379 0.0176  0.0103  -0.0345 149 TRP A CG  
903  C CD1 . TRP A 116 ? 0.2626 0.1441 0.2272 0.0162  0.0052  -0.0365 149 TRP A CD1 
904  C CD2 . TRP A 116 ? 0.3388 0.2387 0.2959 0.0259  0.0149  -0.0409 149 TRP A CD2 
905  N NE1 . TRP A 116 ? 0.3186 0.1897 0.2780 0.0236  0.0051  -0.0458 149 TRP A NE1 
906  C CE2 . TRP A 116 ? 0.3648 0.2483 0.3186 0.0302  0.0116  -0.0488 149 TRP A CE2 
907  C CE3 . TRP A 116 ? 0.2877 0.2021 0.2432 0.0302  0.0218  -0.0403 149 TRP A CE3 
908  C CZ2 . TRP A 116 ? 0.3900 0.2722 0.3368 0.0401  0.0151  -0.0577 149 TRP A CZ2 
909  C CZ3 . TRP A 116 ? 0.3133 0.2282 0.2625 0.0392  0.0265  -0.0470 149 TRP A CZ3 
910  C CH2 . TRP A 116 ? 0.3653 0.2648 0.3093 0.0447  0.0232  -0.0564 149 TRP A CH2 
911  N N   . SER A 117 ? 0.2595 0.1790 0.2442 0.0156  0.0108  -0.0132 150 SER A N   
912  C CA  . SER A 117 ? 0.2413 0.1557 0.2290 0.0184  0.0090  -0.0079 150 SER A CA  
913  C C   . SER A 117 ? 0.2674 0.1882 0.2602 0.0266  0.0101  -0.0083 150 SER A C   
914  O O   . SER A 117 ? 0.2579 0.1712 0.2523 0.0317  0.0086  -0.0059 150 SER A O   
915  C CB  . SER A 117 ? 0.2300 0.1515 0.2186 0.0140  0.0076  -0.0002 150 SER A CB  
916  O OG  . SER A 117 ? 0.2836 0.1987 0.2713 0.0063  0.0063  0.0017  150 SER A OG  
917  N N   . HIS A 118 ? 0.2194 0.1536 0.2164 0.0279  0.0120  -0.0108 151 HIS A N   
918  C CA  . HIS A 118 ? 0.2030 0.1464 0.2089 0.0346  0.0121  -0.0115 151 HIS A CA  
919  C C   . HIS A 118 ? 0.2514 0.1991 0.2622 0.0376  0.0169  -0.0164 151 HIS A C   
920  O O   . HIS A 118 ? 0.2269 0.1868 0.2490 0.0406  0.0179  -0.0169 151 HIS A O   
921  C CB  . HIS A 118 ? 0.2228 0.1799 0.2338 0.0335  0.0093  -0.0099 151 HIS A CB  
922  C CG  . HIS A 118 ? 0.2385 0.1950 0.2435 0.0330  0.0057  -0.0048 151 HIS A CG  
923  N ND1 . HIS A 118 ? 0.2473 0.2034 0.2514 0.0391  0.0027  -0.0009 151 HIS A ND1 
924  C CD2 . HIS A 118 ? 0.2547 0.2124 0.2540 0.0277  0.0054  -0.0018 151 HIS A CD2 
925  C CE1 . HIS A 118 ? 0.2472 0.2047 0.2442 0.0376  0.0014  0.0050  151 HIS A CE1 
926  N NE2 . HIS A 118 ? 0.2869 0.2460 0.2818 0.0306  0.0033  0.0043  151 HIS A NE2 
927  N N   . TRP A 119 ? 0.2108 0.1493 0.2136 0.0373  0.0199  -0.0200 152 TRP A N   
928  C CA  . TRP A 119 ? 0.2726 0.2175 0.2769 0.0409  0.0260  -0.0239 152 TRP A CA  
929  C C   . TRP A 119 ? 0.2758 0.2265 0.2910 0.0495  0.0282  -0.0253 152 TRP A C   
930  O O   . TRP A 119 ? 0.2754 0.2402 0.3002 0.0518  0.0335  -0.0253 152 TRP A O   
931  C CB  . TRP A 119 ? 0.2346 0.1682 0.2253 0.0410  0.0274  -0.0294 152 TRP A CB  
932  C CG  . TRP A 119 ? 0.3209 0.2634 0.3089 0.0453  0.0347  -0.0326 152 TRP A CG  
933  C CD1 . TRP A 119 ? 0.2961 0.2392 0.2836 0.0544  0.0394  -0.0380 152 TRP A CD1 
934  C CD2 . TRP A 119 ? 0.3027 0.2561 0.2881 0.0414  0.0388  -0.0296 152 TRP A CD2 
935  N NE1 . TRP A 119 ? 0.3840 0.3396 0.3678 0.0566  0.0472  -0.0381 152 TRP A NE1 
936  C CE2 . TRP A 119 ? 0.3490 0.3104 0.3314 0.0483  0.0468  -0.0321 152 TRP A CE2 
937  C CE3 . TRP A 119 ? 0.3148 0.2723 0.3004 0.0335  0.0366  -0.0245 152 TRP A CE3 
938  C CZ2 . TRP A 119 ? 0.3963 0.3697 0.3752 0.0470  0.0531  -0.0278 152 TRP A CZ2 
939  C CZ3 . TRP A 119 ? 0.2967 0.2640 0.2798 0.0322  0.0417  -0.0211 152 TRP A CZ3 
940  C CH2 . TRP A 119 ? 0.3315 0.3067 0.3110 0.0386  0.0500  -0.0218 152 TRP A CH2 
941  N N   . SER A 120 ? 0.2819 0.2227 0.2975 0.0545  0.0242  -0.0256 153 SER A N   
942  C CA  . SER A 120 ? 0.3438 0.2904 0.3708 0.0638  0.0253  -0.0271 153 SER A CA  
943  C C   . SER A 120 ? 0.3045 0.2691 0.3471 0.0637  0.0239  -0.0239 153 SER A C   
944  O O   . SER A 120 ? 0.2890 0.2671 0.3457 0.0685  0.0277  -0.0253 153 SER A O   
945  C CB  . SER A 120 ? 0.3800 0.3109 0.4045 0.0692  0.0199  -0.0265 153 SER A CB  
946  O OG  . SER A 120 ? 0.5418 0.4554 0.5561 0.0706  0.0206  -0.0317 153 SER A OG  
947  N N   . LEU A 121 ? 0.2627 0.2288 0.3044 0.0585  0.0182  -0.0200 154 LEU A N   
948  C CA  . LEU A 121 ? 0.2394 0.2215 0.2958 0.0584  0.0147  -0.0191 154 LEU A CA  
949  C C   . LEU A 121 ? 0.2186 0.2127 0.2850 0.0530  0.0195  -0.0195 154 LEU A C   
950  O O   . LEU A 121 ? 0.2294 0.2377 0.3147 0.0546  0.0200  -0.0199 154 LEU A O   
951  C CB  . LEU A 121 ? 0.2300 0.2106 0.2800 0.0558  0.0074  -0.0164 154 LEU A CB  
952  C CG  . LEU A 121 ? 0.2355 0.2311 0.2983 0.0555  0.0017  -0.0180 154 LEU A CG  
953  C CD1 . LEU A 121 ? 0.2276 0.2339 0.3075 0.0629  -0.0014 -0.0202 154 LEU A CD1 
954  C CD2 . LEU A 121 ? 0.2051 0.1989 0.2563 0.0553  -0.0047 -0.0161 154 LEU A CD2 
955  N N   . LEU A 122 ? 0.2046 0.1933 0.2599 0.0464  0.0228  -0.0185 155 LEU A N   
956  C CA  . LEU A 122 ? 0.2049 0.2037 0.2688 0.0414  0.0274  -0.0166 155 LEU A CA  
957  C C   . LEU A 122 ? 0.2489 0.2575 0.3227 0.0455  0.0360  -0.0162 155 LEU A C   
958  O O   . LEU A 122 ? 0.2427 0.2643 0.3323 0.0425  0.0397  -0.0126 155 LEU A O   
959  C CB  . LEU A 122 ? 0.1876 0.1783 0.2358 0.0352  0.0289  -0.0153 155 LEU A CB  
960  C CG  . LEU A 122 ? 0.1978 0.1840 0.2405 0.0305  0.0218  -0.0148 155 LEU A CG  
961  C CD1 . LEU A 122 ? 0.2114 0.1895 0.2390 0.0255  0.0230  -0.0140 155 LEU A CD1 
962  C CD2 . LEU A 122 ? 0.1691 0.1659 0.2279 0.0278  0.0180  -0.0142 155 LEU A CD2 
963  N N   . SER A 123 ? 0.2165 0.2197 0.2825 0.0526  0.0396  -0.0195 156 SER A N   
964  C CA  . SER A 123 ? 0.2581 0.2731 0.3331 0.0586  0.0486  -0.0199 156 SER A CA  
965  C C   . SER A 123 ? 0.3070 0.3327 0.4025 0.0654  0.0468  -0.0211 156 SER A C   
966  O O   . SER A 123 ? 0.2511 0.2893 0.3573 0.0714  0.0546  -0.0214 156 SER A O   
967  C CB  . SER A 123 ? 0.3278 0.3323 0.3831 0.0645  0.0537  -0.0250 156 SER A CB  
968  O OG  . SER A 123 ? 0.4290 0.4137 0.4700 0.0651  0.0463  -0.0289 156 SER A OG  
969  N N   . ALA A 124 ? 0.2309 0.2541 0.3322 0.0652  0.0368  -0.0215 157 ALA A N   
970  C CA  . ALA A 124 ? 0.2668 0.2983 0.3846 0.0730  0.0327  -0.0233 157 ALA A CA  
971  C C   . ALA A 124 ? 0.1798 0.2299 0.3241 0.0694  0.0291  -0.0216 157 ALA A C   
972  O O   . ALA A 124 ? 0.1834 0.2350 0.3306 0.0609  0.0266  -0.0196 157 ALA A O   
973  C CB  . ALA A 124 ? 0.3004 0.3173 0.4061 0.0767  0.0230  -0.0244 157 ALA A CB  
974  N N   . PRO A 125 ? 0.2388 0.2710 0.3170 0.0376  0.0054  0.0272  158 PRO A N   
975  C CA  . PRO A 125 ? 0.2300 0.2857 0.3279 0.0418  -0.0072 0.0216  158 PRO A CA  
976  C C   . PRO A 125 ? 0.2181 0.2783 0.3069 0.0438  -0.0149 0.0184  158 PRO A C   
977  O O   . PRO A 125 ? 0.2244 0.3050 0.3365 0.0395  -0.0212 0.0092  158 PRO A O   
978  C CB  . PRO A 125 ? 0.2588 0.3213 0.3611 0.0577  -0.0132 0.0202  158 PRO A CB  
979  C CG  . PRO A 125 ? 0.2353 0.2698 0.3077 0.0658  -0.0033 0.0306  158 PRO A CG  
980  C CD  . PRO A 125 ? 0.2530 0.2715 0.3226 0.0486  0.0104  0.0320  158 PRO A CD  
981  N N   . SER A 126 ? 0.2201 0.2595 0.2772 0.0509  -0.0110 0.0253  159 SER A N   
982  C CA  . SER A 126 ? 0.2091 0.2519 0.2530 0.0564  -0.0177 0.0235  159 SER A CA  
983  C C   . SER A 126 ? 0.2043 0.2462 0.2536 0.0373  -0.0139 0.0219  159 SER A C   
984  O O   . SER A 126 ? 0.2197 0.2659 0.2613 0.0394  -0.0196 0.0196  159 SER A O   
985  C CB  . SER A 126 ? 0.3241 0.3388 0.3278 0.0757  -0.0085 0.0352  159 SER A CB  
986  O OG  . SER A 126 ? 0.3204 0.3023 0.3144 0.0630  0.0135  0.0426  159 SER A OG  
987  N N   . CYS A 127 ? 0.1839 0.2248 0.2450 0.0225  -0.0055 0.0216  160 CYS A N   
988  C CA  . CYS A 127 ? 0.1873 0.2313 0.2494 0.0099  -0.0020 0.0192  160 CYS A CA  
989  C C   . CYS A 127 ? 0.1636 0.2237 0.2381 0.0085  -0.0102 0.0155  160 CYS A C   
990  O O   . CYS A 127 ? 0.1835 0.2407 0.2472 0.0053  -0.0116 0.0152  160 CYS A O   
991  C CB  . CYS A 127 ? 0.1698 0.2226 0.2424 0.0039  0.0048  0.0165  160 CYS A CB  
992  S SG  . CYS A 127 ? 0.1933 0.2590 0.2636 -0.0032 0.0080  0.0115  160 CYS A SG  
993  N N   . ALA A 128 ? 0.1804 0.2566 0.2820 0.0102  -0.0128 0.0108  161 ALA A N   
994  C CA  . ALA A 128 ? 0.1278 0.2181 0.2518 0.0061  -0.0143 0.0030  161 ALA A CA  
995  C C   . ALA A 128 ? 0.1446 0.2413 0.2589 0.0118  -0.0273 -0.0046 161 ALA A C   
996  O O   . ALA A 128 ? 0.1708 0.2687 0.2828 0.0062  -0.0275 -0.0065 161 ALA A O   
997  C CB  . ALA A 128 ? 0.1401 0.2446 0.3042 0.0064  -0.0093 -0.0059 161 ALA A CB  
998  N N   . ALA A 129 ? 0.1785 0.2796 0.2818 0.0272  -0.0377 -0.0081 162 ALA A N   
999  C CA  . ALA A 129 ? 0.2356 0.3465 0.3225 0.0415  -0.0503 -0.0153 162 ALA A CA  
1000 C C   . ALA A 129 ? 0.2165 0.3008 0.2664 0.0395  -0.0433 -0.0011 162 ALA A C   
1001 O O   . ALA A 129 ? 0.2203 0.3102 0.2664 0.0382  -0.0477 -0.0056 162 ALA A O   
1002 C CB  . ALA A 129 ? 0.2415 0.3623 0.3136 0.0676  -0.0607 -0.0188 162 ALA A CB  
1003 N N   . GLN A 130 ? 0.1917 0.2477 0.2209 0.0361  -0.0297 0.0132  163 GLN A N   
1004 C CA  . GLN A 130 ? 0.2344 0.2647 0.2375 0.0321  -0.0177 0.0224  163 GLN A CA  
1005 C C   . GLN A 130 ? 0.2254 0.2637 0.2420 0.0134  -0.0169 0.0183  163 GLN A C   
1006 O O   . GLN A 130 ? 0.2265 0.2547 0.2271 0.0118  -0.0134 0.0207  163 GLN A O   
1007 C CB  . GLN A 130 ? 0.2203 0.2230 0.2134 0.0280  0.0009  0.0302  163 GLN A CB  
1008 C CG  . GLN A 130 ? 0.2577 0.2389 0.2256 0.0505  0.0087  0.0400  163 GLN A CG  
1009 C CD  . GLN A 130 ? 0.4505 0.4065 0.3824 0.0683  0.0195  0.0505  163 GLN A CD  
1010 O OE1 . GLN A 130 ? 0.4721 0.3964 0.3952 0.0599  0.0432  0.0561  163 GLN A OE1 
1011 N NE2 . GLN A 130 ? 0.4564 0.4291 0.3696 0.0948  0.0037  0.0503  163 GLN A NE2 
1012 N N   . LEU A 131 ? 0.1801 0.2347 0.2232 0.0027  -0.0176 0.0136  164 LEU A N   
1013 C CA  . LEU A 131 ? 0.1409 0.2021 0.1911 -0.0087 -0.0140 0.0122  164 LEU A CA  
1014 C C   . LEU A 131 ? 0.1664 0.2393 0.2259 -0.0080 -0.0217 0.0062  164 LEU A C   
1015 O O   . LEU A 131 ? 0.1519 0.2220 0.2020 -0.0130 -0.0204 0.0070  164 LEU A O   
1016 C CB  . LEU A 131 ? 0.1475 0.2188 0.2155 -0.0120 -0.0071 0.0126  164 LEU A CB  
1017 C CG  . LEU A 131 ? 0.1534 0.2328 0.2253 -0.0153 -0.0004 0.0138  164 LEU A CG  
1018 C CD1 . LEU A 131 ? 0.1815 0.2592 0.2343 -0.0199 0.0007  0.0121  164 LEU A CD1 
1019 C CD2 . LEU A 131 ? 0.1302 0.2168 0.2114 -0.0086 0.0104  0.0180  164 LEU A CD2 
1020 N N   . ASP A 132 ? 0.1830 0.2718 0.2638 -0.0016 -0.0298 -0.0039 165 ASP A N   
1021 C CA  . ASP A 132 ? 0.1940 0.3005 0.2923 -0.0010 -0.0373 -0.0181 165 ASP A CA  
1022 C C   . ASP A 132 ? 0.1825 0.2834 0.2477 0.0086  -0.0459 -0.0163 165 ASP A C   
1023 O O   . ASP A 132 ? 0.1916 0.2929 0.2548 0.0027  -0.0454 -0.0180 165 ASP A O   
1024 C CB  . ASP A 132 ? 0.1701 0.3028 0.3026 0.0062  -0.0457 -0.0378 165 ASP A CB  
1025 C CG  . ASP A 132 ? 0.3686 0.5269 0.5364 0.0030  -0.0500 -0.0620 165 ASP A CG  
1026 O OD1 . ASP A 132 ? 0.5005 0.6505 0.6770 -0.0097 -0.0385 -0.0593 165 ASP A OD1 
1027 O OD2 . ASP A 132 ? 0.5256 0.7155 0.7142 0.0149  -0.0644 -0.0865 165 ASP A OD2 
1028 N N   . ARG A 133 ? 0.1828 0.2736 0.2181 0.0257  -0.0497 -0.0097 166 ARG A N   
1029 C CA  . ARG A 133 ? 0.2039 0.2815 0.2007 0.0410  -0.0511 -0.0031 166 ARG A CA  
1030 C C   . ARG A 133 ? 0.2558 0.3099 0.2396 0.0250  -0.0376 0.0082  166 ARG A C   
1031 O O   . ARG A 133 ? 0.2318 0.2863 0.2046 0.0265  -0.0401 0.0068  166 ARG A O   
1032 C CB  . ARG A 133 ? 0.2799 0.3389 0.2431 0.0643  -0.0465 0.0086  166 ARG A CB  
1033 C CG  . ARG A 133 ? 0.4282 0.4570 0.3457 0.0814  -0.0347 0.0238  166 ARG A CG  
1034 C CD  . ARG A 133 ? 0.5623 0.5757 0.4435 0.1156  -0.0287 0.0350  166 ARG A CD  
1035 N NE  . ARG A 133 ? 0.7453 0.8000 0.6234 0.1456  -0.0533 0.0188  166 ARG A NE  
1036 C CZ  . ARG A 133 ? 0.7900 0.8598 0.6412 0.1734  -0.0637 0.0135  166 ARG A CZ  
1037 N NH1 . ARG A 133 ? 0.8038 0.8435 0.6247 0.1755  -0.0491 0.0282  166 ARG A NH1 
1038 N NH2 . ARG A 133 ? 0.7789 0.8937 0.6414 0.1935  -0.0836 -0.0118 166 ARG A NH2 
1039 N N   . ALA A 134 ? 0.2023 0.2417 0.1911 0.0099  -0.0243 0.0153  167 ALA A N   
1040 C CA  . ALA A 134 ? 0.1854 0.2105 0.1668 -0.0035 -0.0121 0.0194  167 ALA A CA  
1041 C C   . ALA A 134 ? 0.2189 0.2611 0.2143 -0.0136 -0.0177 0.0138  167 ALA A C   
1042 O O   . ALA A 134 ? 0.2021 0.2374 0.1843 -0.0157 -0.0151 0.0155  167 ALA A O   
1043 C CB  . ALA A 134 ? 0.1777 0.1976 0.1693 -0.0153 -0.0001 0.0187  167 ALA A CB  
1044 N N   . LYS A 135 ? 0.1676 0.2290 0.1897 -0.0179 -0.0218 0.0081  168 LYS A N   
1045 C CA  . LYS A 135 ? 0.1708 0.2422 0.2060 -0.0254 -0.0201 0.0050  168 LYS A CA  
1046 C C   . LYS A 135 ? 0.1996 0.2756 0.2306 -0.0208 -0.0292 -0.0019 168 LYS A C   
1047 O O   . LYS A 135 ? 0.2303 0.3028 0.2523 -0.0255 -0.0269 -0.0001 168 LYS A O   
1048 C CB  . LYS A 135 ? 0.1344 0.2175 0.2006 -0.0277 -0.0141 0.0017  168 LYS A CB  
1049 C CG  . LYS A 135 ? 0.1473 0.2288 0.2124 -0.0272 -0.0041 0.0094  168 LYS A CG  
1050 C CD  . LYS A 135 ? 0.2724 0.3588 0.3651 -0.0242 0.0049  0.0087  168 LYS A CD  
1051 C CE  . LYS A 135 ? 0.3049 0.3921 0.4215 -0.0262 0.0189  0.0067  168 LYS A CE  
1052 N NZ  . LYS A 135 ? 0.2684 0.3559 0.4208 -0.0250 0.0332  0.0026  168 LYS A NZ  
1053 N N   . ARG A 136 ? 0.1483 0.2354 0.1828 -0.0082 -0.0410 -0.0115 169 ARG A N   
1054 C CA  . ARG A 136 ? 0.1851 0.2857 0.2156 0.0016  -0.0525 -0.0235 169 ARG A CA  
1055 C C   . ARG A 136 ? 0.2492 0.3282 0.2390 0.0072  -0.0491 -0.0104 169 ARG A C   
1056 O O   . ARG A 136 ? 0.2263 0.3070 0.2137 0.0029  -0.0497 -0.0130 169 ARG A O   
1057 C CB  . ARG A 136 ? 0.2239 0.3475 0.2585 0.0222  -0.0679 -0.0390 169 ARG A CB  
1058 C CG  . ARG A 136 ? 0.4173 0.5705 0.4577 0.0360  -0.0836 -0.0618 169 ARG A CG  
1059 C CD  . ARG A 136 ? 0.5830 0.7590 0.6034 0.0698  -0.1009 -0.0731 169 ARG A CD  
1060 N NE  . ARG A 136 ? 0.6430 0.7842 0.6049 0.0898  -0.0932 -0.0450 169 ARG A NE  
1061 C CZ  . ARG A 136 ? 0.6499 0.7766 0.5952 0.1013  -0.0879 -0.0323 169 ARG A CZ  
1062 N NH1 . ARG A 136 ? 0.6458 0.7936 0.6250 0.0969  -0.0939 -0.0449 169 ARG A NH1 
1063 N NH2 . ARG A 136 ? 0.6653 0.7527 0.5612 0.1177  -0.0724 -0.0065 169 ARG A NH2 
1064 N N   . ASP A 137 ? 0.2432 0.2974 0.2044 0.0145  -0.0404 0.0043  170 ASP A N   
1065 C CA  . ASP A 137 ? 0.2239 0.2523 0.1500 0.0216  -0.0301 0.0162  170 ASP A CA  
1066 C C   . ASP A 137 ? 0.2329 0.2543 0.1673 -0.0005 -0.0201 0.0186  170 ASP A C   
1067 O O   . ASP A 137 ? 0.2417 0.2568 0.1614 0.0009  -0.0182 0.0206  170 ASP A O   
1068 C CB  . ASP A 137 ? 0.2741 0.2717 0.1741 0.0341  -0.0142 0.0302  170 ASP A CB  
1069 C CG  . ASP A 137 ? 0.4347 0.4383 0.3123 0.0669  -0.0236 0.0307  170 ASP A CG  
1070 O OD1 . ASP A 137 ? 0.4010 0.4345 0.2781 0.0830  -0.0434 0.0175  170 ASP A OD1 
1071 O OD2 . ASP A 137 ? 0.5345 0.5164 0.3962 0.0788  -0.0109 0.0416  170 ASP A OD2 
1072 N N   . ILE A 138 ? 0.1945 0.2224 0.1519 -0.0174 -0.0151 0.0167  171 ILE A N   
1073 C CA  . ILE A 138 ? 0.1715 0.2003 0.1343 -0.0322 -0.0067 0.0162  171 ILE A CA  
1074 C C   . ILE A 138 ? 0.2092 0.2536 0.1815 -0.0355 -0.0138 0.0123  171 ILE A C   
1075 O O   . ILE A 138 ? 0.1554 0.1975 0.1207 -0.0409 -0.0097 0.0133  171 ILE A O   
1076 C CB  . ILE A 138 ? 0.1509 0.1890 0.1304 -0.0411 -0.0004 0.0126  171 ILE A CB  
1077 C CG1 . ILE A 138 ? 0.1991 0.2190 0.1737 -0.0416 0.0117  0.0124  171 ILE A CG1 
1078 C CG2 . ILE A 138 ? 0.1718 0.2250 0.1578 -0.0491 0.0036  0.0076  171 ILE A CG2 
1079 C CD1 . ILE A 138 ? 0.2403 0.2331 0.1982 -0.0412 0.0270  0.0157  171 ILE A CD1 
1080 N N   . VAL A 139 ? 0.1631 0.2226 0.1549 -0.0324 -0.0221 0.0058  172 VAL A N   
1081 C CA  . VAL A 139 ? 0.1720 0.2426 0.1793 -0.0365 -0.0231 -0.0006 172 VAL A CA  
1082 C C   . VAL A 139 ? 0.2672 0.3343 0.2549 -0.0306 -0.0300 -0.0031 172 VAL A C   
1083 O O   . VAL A 139 ? 0.1972 0.2645 0.1847 -0.0364 -0.0267 -0.0033 172 VAL A O   
1084 C CB  . VAL A 139 ? 0.1365 0.2231 0.1790 -0.0362 -0.0250 -0.0134 172 VAL A CB  
1085 C CG1 . VAL A 139 ? 0.1484 0.2459 0.2120 -0.0396 -0.0249 -0.0271 172 VAL A CG1 
1086 C CG2 . VAL A 139 ? 0.1449 0.2303 0.2051 -0.0408 -0.0108 -0.0066 172 VAL A CG2 
1087 N N   . ARG A 140 ? 0.2036 0.2657 0.1695 -0.0150 -0.0375 -0.0030 173 ARG A N   
1088 C CA  . ARG A 140 ? 0.2356 0.2925 0.1746 -0.0024 -0.0419 -0.0028 173 ARG A CA  
1089 C C   . ARG A 140 ? 0.2824 0.3126 0.1976 -0.0086 -0.0268 0.0120  173 ARG A C   
1090 O O   . ARG A 140 ? 0.2559 0.2841 0.1631 -0.0109 -0.0258 0.0122  173 ARG A O   
1091 C CB  . ARG A 140 ? 0.2574 0.3168 0.1719 0.0255  -0.0514 -0.0048 173 ARG A CB  
1092 C CG  . ARG A 140 ? 0.2576 0.3549 0.1986 0.0355  -0.0702 -0.0291 173 ARG A CG  
1093 C CD  . ARG A 140 ? 0.3502 0.4592 0.2570 0.0729  -0.0832 -0.0345 173 ARG A CD  
1094 N NE  . ARG A 140 ? 0.5417 0.6914 0.4834 0.0814  -0.0987 -0.0629 173 ARG A NE  
1095 C CZ  . ARG A 140 ? 0.5641 0.7227 0.5185 0.0858  -0.1017 -0.0663 173 ARG A CZ  
1096 N NH1 . ARG A 140 ? 0.5359 0.6649 0.4697 0.0835  -0.0907 -0.0424 173 ARG A NH1 
1097 N NH2 . ARG A 140 ? 0.6984 0.8904 0.6903 0.0900  -0.1095 -0.0944 173 ARG A NH2 
1098 N N   . SER A 141 ? 0.2324 0.2433 0.1412 -0.0124 -0.0132 0.0212  174 SER A N   
1099 C CA  . SER A 141 ? 0.2517 0.2373 0.1436 -0.0165 0.0051  0.0294  174 SER A CA  
1100 C C   . SER A 141 ? 0.2668 0.2642 0.1773 -0.0363 0.0086  0.0240  174 SER A C   
1101 O O   . SER A 141 ? 0.2935 0.2789 0.1948 -0.0402 0.0192  0.0260  174 SER A O   
1102 C CB  . SER A 141 ? 0.2633 0.2238 0.1504 -0.0156 0.0244  0.0353  174 SER A CB  
1103 O OG  . SER A 141 ? 0.3013 0.2775 0.2141 -0.0268 0.0209  0.0284  174 SER A OG  
1104 N N   . ARG A 142 ? 0.2417 0.2331 0.1534 0.0296  0.0174  0.0218  175 ARG A N   
1105 C CA  . ARG A 142 ? 0.2088 0.1997 0.1354 0.0271  0.0205  0.0193  175 ARG A CA  
1106 C C   . ARG A 142 ? 0.2441 0.2343 0.1686 0.0273  0.0190  0.0106  175 ARG A C   
1107 O O   . ARG A 142 ? 0.2653 0.2539 0.2025 0.0260  0.0199  0.0082  175 ARG A O   
1108 C CB  . ARG A 142 ? 0.2209 0.2111 0.1618 0.0233  0.0155  0.0215  175 ARG A CB  
1109 C CG  . ARG A 142 ? 0.2398 0.2281 0.1825 0.0232  0.0165  0.0290  175 ARG A CG  
1110 C CD  . ARG A 142 ? 0.3100 0.2955 0.2660 0.0191  0.0133  0.0305  175 ARG A CD  
1111 N NE  . ARG A 142 ? 0.3099 0.2956 0.2793 0.0171  0.0161  0.0310  175 ARG A NE  
1112 C CZ  . ARG A 142 ? 0.2748 0.2601 0.2536 0.0157  0.0202  0.0363  175 ARG A CZ  
1113 N NH1 . ARG A 142 ? 0.2537 0.2356 0.2284 0.0155  0.0219  0.0420  175 ARG A NH1 
1114 N NH2 . ARG A 142 ? 0.2556 0.2437 0.2501 0.0144  0.0220  0.0361  175 ARG A NH2 
1115 N N   . HIS A 143 ? 0.2622 0.2525 0.1711 0.0287  0.0158  0.0058  176 HIS A N   
1116 C CA  . HIS A 143 ? 0.2646 0.2516 0.1687 0.0287  0.0144  -0.0034 176 HIS A CA  
1117 C C   . HIS A 143 ? 0.2690 0.2541 0.1865 0.0242  0.0081  -0.0069 176 HIS A C   
1118 O O   . HIS A 143 ? 0.2422 0.2217 0.1651 0.0242  0.0092  -0.0118 176 HIS A O   
1119 C CB  . HIS A 143 ? 0.2889 0.2729 0.1916 0.0325  0.0246  -0.0062 176 HIS A CB  
1120 C CG  . HIS A 143 ? 0.3355 0.3213 0.2268 0.0356  0.0335  -0.0007 176 HIS A CG  
1121 N ND1 . HIS A 143 ? 0.3866 0.3710 0.2543 0.0375  0.0324  -0.0007 176 HIS A ND1 
1122 C CD2 . HIS A 143 ? 0.3854 0.3738 0.2854 0.0365  0.0433  0.0056  176 HIS A CD2 
1123 C CE1 . HIS A 143 ? 0.4215 0.4061 0.2815 0.0394  0.0419  0.0060  176 HIS A CE1 
1124 N NE2 . HIS A 143 ? 0.3403 0.3281 0.2209 0.0384  0.0492  0.0098  176 HIS A NE2 
1125 N N   . LEU A 144 ? 0.2307 0.2194 0.1533 0.0204  0.0019  -0.0041 177 LEU A N   
1126 C CA  . LEU A 144 ? 0.2254 0.2116 0.1588 0.0150  -0.0029 -0.0055 177 LEU A CA  
1127 C C   . LEU A 144 ? 0.2657 0.2493 0.1942 0.0116  -0.0085 -0.0130 177 LEU A C   
1128 O O   . LEU A 144 ? 0.2621 0.2511 0.1829 0.0110  -0.0127 -0.0155 177 LEU A O   
1129 C CB  . LEU A 144 ? 0.1997 0.1909 0.1387 0.0120  -0.0057 -0.0005 177 LEU A CB  
1130 C CG  . LEU A 144 ? 0.2136 0.2045 0.1577 0.0141  -0.0016 0.0063  177 LEU A CG  
1131 C CD1 . LEU A 144 ? 0.2052 0.1980 0.1538 0.0109  -0.0045 0.0090  177 LEU A CD1 
1132 C CD2 . LEU A 144 ? 0.2136 0.1990 0.1668 0.0143  0.0016  0.0075  177 LEU A CD2 
1133 N N   . ASP A 145 ? 0.2659 0.2405 0.1999 0.0093  -0.0096 -0.0163 178 ASP A N   
1134 C CA  . ASP A 145 ? 0.2788 0.2473 0.2096 0.0048  -0.0152 -0.0233 178 ASP A CA  
1135 C C   . ASP A 145 ? 0.2956 0.2671 0.2329 -0.0036 -0.0207 -0.0208 178 ASP A C   
1136 O O   . ASP A 145 ? 0.2489 0.2271 0.1912 -0.0048 -0.0195 -0.0148 178 ASP A O   
1137 C CB  . ASP A 145 ? 0.2794 0.2347 0.2133 0.0068  -0.0139 -0.0276 178 ASP A CB  
1138 C CG  . ASP A 145 ? 0.3919 0.3414 0.3395 0.0051  -0.0146 -0.0218 178 ASP A CG  
1139 O OD1 . ASP A 145 ? 0.2600 0.2134 0.2121 0.0003  -0.0169 -0.0155 178 ASP A OD1 
1140 O OD2 . ASP A 145 ? 0.4343 0.3748 0.3878 0.0090  -0.0133 -0.0240 178 ASP A OD2 
1141 N N   . SER A 146 ? 0.2703 0.2356 0.2072 -0.0099 -0.0259 -0.0257 179 SER A N   
1142 C CA  A SER A 146 ? 0.2565 0.2265 0.1991 -0.0191 -0.0297 -0.0236 179 SER A CA  
1143 C CA  B SER A 146 ? 0.2571 0.2271 0.1996 -0.0191 -0.0297 -0.0236 179 SER A CA  
1144 C C   . SER A 146 ? 0.2557 0.2220 0.2044 -0.0221 -0.0277 -0.0163 179 SER A C   
1145 O O   . SER A 146 ? 0.2373 0.2127 0.1893 -0.0261 -0.0267 -0.0125 179 SER A O   
1146 C CB  A SER A 146 ? 0.3396 0.3008 0.2811 -0.0267 -0.0355 -0.0296 179 SER A CB  
1147 C CB  B SER A 146 ? 0.3388 0.3001 0.2803 -0.0266 -0.0355 -0.0296 179 SER A CB  
1148 O OG  A SER A 146 ? 0.3611 0.3053 0.3048 -0.0290 -0.0362 -0.0283 179 SER A OG  
1149 O OG  B SER A 146 ? 0.3057 0.2705 0.2540 -0.0368 -0.0373 -0.0263 179 SER A OG  
1150 N N   . LEU A 147 ? 0.2097 0.1629 0.1600 -0.0198 -0.0273 -0.0148 180 LEU A N   
1151 C CA  . LEU A 147 ? 0.2225 0.1704 0.1765 -0.0228 -0.0276 -0.0077 180 LEU A CA  
1152 C C   . LEU A 147 ? 0.2333 0.1915 0.1886 -0.0192 -0.0236 -0.0029 180 LEU A C   
1153 O O   . LEU A 147 ? 0.2052 0.1659 0.1598 -0.0240 -0.0233 0.0012  180 LEU A O   
1154 C CB  . LEU A 147 ? 0.2273 0.1603 0.1850 -0.0193 -0.0296 -0.0070 180 LEU A CB  
1155 C CG  . LEU A 147 ? 0.2455 0.1718 0.2062 -0.0216 -0.0320 0.0006  180 LEU A CG  
1156 C CD1 . LEU A 147 ? 0.2898 0.2102 0.2446 -0.0325 -0.0352 0.0042  180 LEU A CD1 
1157 C CD2 . LEU A 147 ? 0.2320 0.1460 0.2001 -0.0161 -0.0351 0.0011  180 LEU A CD2 
1158 N N   . TYR A 148 ? 0.2105 0.1736 0.1666 -0.0111 -0.0200 -0.0035 181 TYR A N   
1159 C CA  . TYR A 148 ? 0.2161 0.1865 0.1735 -0.0080 -0.0167 0.0011  181 TYR A CA  
1160 C C   . TYR A 148 ? 0.2095 0.1915 0.1639 -0.0091 -0.0158 0.0008  181 TYR A C   
1161 O O   . TYR A 148 ? 0.2045 0.1899 0.1597 -0.0091 -0.0142 0.0043  181 TYR A O   
1162 C CB  . TYR A 148 ? 0.1915 0.1635 0.1507 -0.0002 -0.0124 0.0015  181 TYR A CB  
1163 C CG  . TYR A 148 ? 0.2532 0.2184 0.2215 0.0014  -0.0125 0.0046  181 TYR A CG  
1164 C CD1 . TYR A 148 ? 0.2514 0.2081 0.2243 0.0024  -0.0145 0.0018  181 TYR A CD1 
1165 C CD2 . TYR A 148 ? 0.2427 0.2096 0.2162 0.0019  -0.0116 0.0100  181 TYR A CD2 
1166 C CE1 . TYR A 148 ? 0.2227 0.1748 0.2074 0.0047  -0.0158 0.0048  181 TYR A CE1 
1167 C CE2 . TYR A 148 ? 0.2027 0.1652 0.1872 0.0029  -0.0133 0.0129  181 TYR A CE2 
1168 C CZ  . TYR A 148 ? 0.2458 0.2019 0.2368 0.0046  -0.0155 0.0105  181 TYR A CZ  
1169 O OH  . TYR A 148 ? 0.2332 0.1866 0.2382 0.0065  -0.0183 0.0135  181 TYR A OH  
1170 N N   . GLN A 149 ? 0.1888 0.1768 0.1406 -0.0098 -0.0175 -0.0039 182 GLN A N   
1171 C CA  . GLN A 149 ? 0.1985 0.1995 0.1515 -0.0105 -0.0178 -0.0043 182 GLN A CA  
1172 C C   . GLN A 149 ? 0.2584 0.2615 0.2155 -0.0180 -0.0174 -0.0027 182 GLN A C   
1173 O O   . GLN A 149 ? 0.1787 0.1892 0.1380 -0.0169 -0.0146 -0.0008 182 GLN A O   
1174 C CB  . GLN A 149 ? 0.1928 0.2003 0.1436 -0.0106 -0.0218 -0.0098 182 GLN A CB  
1175 C CG  . GLN A 149 ? 0.2068 0.2133 0.1490 -0.0028 -0.0214 -0.0112 182 GLN A CG  
1176 C CD  . GLN A 149 ? 0.3100 0.3196 0.2466 -0.0038 -0.0270 -0.0176 182 GLN A CD  
1177 O OE1 . GLN A 149 ? 0.3410 0.3598 0.2834 -0.0088 -0.0317 -0.0199 182 GLN A OE1 
1178 N NE2 . GLN A 149 ? 0.3316 0.3339 0.2571 0.0005  -0.0263 -0.0209 182 GLN A NE2 
1179 N N   . ARG A 150 ? 0.1973 0.1925 0.1543 -0.0257 -0.0195 -0.0035 183 ARG A N   
1180 C CA  . ARG A 150 ? 0.1903 0.1855 0.1481 -0.0340 -0.0178 -0.0010 183 ARG A CA  
1181 C C   . ARG A 150 ? 0.1917 0.1804 0.1454 -0.0326 -0.0152 0.0039  183 ARG A C   
1182 O O   . ARG A 150 ? 0.2003 0.1940 0.1527 -0.0355 -0.0115 0.0053  183 ARG A O   
1183 C CB  . ARG A 150 ? 0.1993 0.1830 0.1556 -0.0428 -0.0212 -0.0013 183 ARG A CB  
1184 C CG  . ARG A 150 ? 0.2295 0.2178 0.1895 -0.0460 -0.0249 -0.0071 183 ARG A CG  
1185 C CD  . ARG A 150 ? 0.2480 0.2188 0.2052 -0.0527 -0.0291 -0.0076 183 ARG A CD  
1186 N NE  . ARG A 150 ? 0.2545 0.2193 0.2100 -0.0631 -0.0278 -0.0024 183 ARG A NE  
1187 C CZ  . ARG A 150 ? 0.3329 0.2779 0.2832 -0.0679 -0.0311 0.0010  183 ARG A CZ  
1188 N NH1 . ARG A 150 ? 0.3038 0.2340 0.2527 -0.0622 -0.0356 -0.0010 183 ARG A NH1 
1189 N NH2 . ARG A 150 ? 0.2704 0.2100 0.2164 -0.0784 -0.0295 0.0066  183 ARG A NH2 
1190 N N   . ALA A 151 ? 0.1759 0.1537 0.1278 -0.0283 -0.0172 0.0061  184 ALA A N   
1191 C CA  . ALA A 151 ? 0.2208 0.1920 0.1695 -0.0276 -0.0167 0.0105  184 ALA A CA  
1192 C C   . ALA A 151 ? 0.1981 0.1782 0.1473 -0.0224 -0.0128 0.0104  184 ALA A C   
1193 O O   . ALA A 151 ? 0.2052 0.1829 0.1497 -0.0242 -0.0112 0.0120  184 ALA A O   
1194 C CB  . ALA A 151 ? 0.1770 0.1378 0.1285 -0.0237 -0.0202 0.0126  184 ALA A CB  
1195 N N   . LEU A 152 ? 0.1984 0.1870 0.1515 -0.0157 -0.0117 0.0084  185 LEU A N   
1196 C CA  . LEU A 152 ? 0.1768 0.1717 0.1306 -0.0100 -0.0088 0.0089  185 LEU A CA  
1197 C C   . LEU A 152 ? 0.1911 0.1957 0.1460 -0.0121 -0.0060 0.0066  185 LEU A C   
1198 O O   . LEU A 152 ? 0.1624 0.1671 0.1158 -0.0097 -0.0032 0.0069  185 LEU A O   
1199 C CB  . LEU A 152 ? 0.1736 0.1739 0.1289 -0.0029 -0.0089 0.0083  185 LEU A CB  
1200 C CG  . LEU A 152 ? 0.1748 0.1773 0.1298 0.0038  -0.0070 0.0105  185 LEU A CG  
1201 C CD1 . LEU A 152 ? 0.1921 0.1838 0.1464 0.0038  -0.0061 0.0144  185 LEU A CD1 
1202 C CD2 . LEU A 152 ? 0.2137 0.2202 0.1665 0.0097  -0.0077 0.0108  185 LEU A CD2 
1203 N N   . THR A 153 ? 0.1725 0.1855 0.1311 -0.0165 -0.0065 0.0038  186 THR A N   
1204 C CA  . THR A 153 ? 0.1759 0.2011 0.1392 -0.0193 -0.0026 0.0015  186 THR A CA  
1205 C C   . THR A 153 ? 0.1693 0.1869 0.1251 -0.0251 0.0016  0.0031  186 THR A C   
1206 O O   . THR A 153 ? 0.1807 0.2034 0.1365 -0.0231 0.0068  0.0015  186 THR A O   
1207 C CB  . THR A 153 ? 0.2031 0.2385 0.1735 -0.0252 -0.0044 -0.0014 186 THR A CB  
1208 O OG1 . THR A 153 ? 0.2029 0.2461 0.1780 -0.0190 -0.0089 -0.0036 186 THR A OG1 
1209 C CG2 . THR A 153 ? 0.2003 0.2503 0.1787 -0.0295 0.0011  -0.0034 186 THR A CG2 
1210 N N   . THR A 154 ? 0.1752 0.1793 0.1233 -0.0319 -0.0009 0.0059  187 THR A N   
1211 C CA  . THR A 154 ? 0.1857 0.1800 0.1224 -0.0379 0.0017  0.0082  187 THR A CA  
1212 C C   . THR A 154 ? 0.1864 0.1733 0.1170 -0.0322 0.0020  0.0088  187 THR A C   
1213 O O   . THR A 154 ? 0.2077 0.1938 0.1307 -0.0334 0.0069  0.0074  187 THR A O   
1214 C CB  . THR A 154 ? 0.1966 0.1755 0.1261 -0.0451 -0.0035 0.0123  187 THR A CB  
1215 O OG1 . THR A 154 ? 0.2241 0.2077 0.1579 -0.0522 -0.0031 0.0116  187 THR A OG1 
1216 C CG2 . THR A 154 ? 0.2083 0.1738 0.1220 -0.0508 -0.0031 0.0158  187 THR A CG2 
1217 N N   . ALA A 155 ? 0.1799 0.1611 0.1134 -0.0264 -0.0028 0.0105  188 ALA A N   
1218 C CA  . ALA A 155 ? 0.1971 0.1696 0.1261 -0.0227 -0.0039 0.0116  188 ALA A CA  
1219 C C   . ALA A 155 ? 0.1820 0.1613 0.1124 -0.0166 0.0013  0.0081  188 ALA A C   
1220 O O   . ALA A 155 ? 0.2103 0.1808 0.1332 -0.0158 0.0018  0.0075  188 ALA A O   
1221 C CB  . ALA A 155 ? 0.2132 0.1816 0.1489 -0.0182 -0.0086 0.0143  188 ALA A CB  
1222 N N   . THR A 156 ? 0.2088 0.2027 0.1490 -0.0120 0.0040  0.0057  189 THR A N   
1223 C CA  . THR A 156 ? 0.2002 0.2006 0.1446 -0.0043 0.0076  0.0028  189 THR A CA  
1224 C C   . THR A 156 ? 0.2153 0.2280 0.1627 -0.0053 0.0145  -0.0018 189 THR A C   
1225 O O   . THR A 156 ? 0.2209 0.2409 0.1748 0.0023  0.0177  -0.0050 189 THR A O   
1226 C CB  . THR A 156 ? 0.1677 0.1760 0.1215 0.0032  0.0047  0.0039  189 THR A CB  
1227 O OG1 . THR A 156 ? 0.1840 0.2051 0.1447 0.0008  0.0036  0.0026  189 THR A OG1 
1228 C CG2 . THR A 156 ? 0.1826 0.1798 0.1337 0.0044  0.0005  0.0084  189 THR A CG2 
1229 N N   . GLN A 157 ? 0.2215 0.2363 0.1651 -0.0145 0.0172  -0.0020 190 GLN A N   
1230 C CA  . GLN A 157 ? 0.2072 0.2379 0.1575 -0.0167 0.0250  -0.0060 190 GLN A CA  
1231 C C   . GLN A 157 ? 0.2254 0.2551 0.1701 -0.0132 0.0331  -0.0105 190 GLN A C   
1232 O O   . GLN A 157 ? 0.2471 0.2935 0.2021 -0.0117 0.0409  -0.0148 190 GLN A O   
1233 C CB  . GLN A 157 ? 0.2520 0.2823 0.1973 -0.0291 0.0266  -0.0040 190 GLN A CB  
1234 C CG  . GLN A 157 ? 0.3081 0.3218 0.2331 -0.0360 0.0293  -0.0022 190 GLN A CG  
1235 C CD  . GLN A 157 ? 0.4021 0.4107 0.3195 -0.0485 0.0290  0.0019  190 GLN A CD  
1236 O OE1 . GLN A 157 ? 0.4350 0.4492 0.3624 -0.0520 0.0253  0.0034  190 GLN A OE1 
1237 N NE2 . GLN A 157 ? 0.5148 0.5107 0.4126 -0.0555 0.0325  0.0036  190 GLN A NE2 
1238 N N   . SER A 158 ? 0.2520 0.2631 0.1816 -0.0119 0.0317  -0.0102 191 SER A N   
1239 C CA  . SER A 158 ? 0.2684 0.2748 0.1892 -0.0085 0.0391  -0.0157 191 SER A CA  
1240 C C   . SER A 158 ? 0.2645 0.2647 0.1893 0.0030  0.0367  -0.0180 191 SER A C   
1241 O O   . SER A 158 ? 0.2670 0.2579 0.1823 0.0064  0.0413  -0.0232 191 SER A O   
1242 C CB  . SER A 158 ? 0.2872 0.2743 0.1836 -0.0172 0.0391  -0.0147 191 SER A CB  
1243 O OG  . SER A 158 ? 0.2639 0.2542 0.1539 -0.0282 0.0421  -0.0119 191 SER A OG  
1244 N N   . TYR A 159 ? 0.2105 0.2141 0.1476 0.0089  0.0297  -0.0144 192 TYR A N   
1245 C CA  . TYR A 159 ? 0.2458 0.2413 0.1857 0.0190  0.0271  -0.0151 192 TYR A CA  
1246 C C   . TYR A 159 ? 0.2595 0.2645 0.2081 0.0284  0.0343  -0.0218 192 TYR A C   
1247 O O   . TYR A 159 ? 0.2345 0.2265 0.1772 0.0344  0.0360  -0.0257 192 TYR A O   
1248 C CB  . TYR A 159 ? 0.2183 0.2176 0.1685 0.0234  0.0197  -0.0093 192 TYR A CB  
1249 C CG  . TYR A 159 ? 0.2465 0.2335 0.1901 0.0180  0.0131  -0.0032 192 TYR A CG  
1250 C CD1 . TYR A 159 ? 0.2797 0.2553 0.2116 0.0091  0.0119  -0.0022 192 TYR A CD1 
1251 C CD2 . TYR A 159 ? 0.2183 0.2055 0.1676 0.0221  0.0082  0.0018  192 TYR A CD2 
1252 C CE1 . TYR A 159 ? 0.2217 0.1886 0.1520 0.0051  0.0056  0.0032  192 TYR A CE1 
1253 C CE2 . TYR A 159 ? 0.2292 0.2077 0.1751 0.0177  0.0039  0.0069  192 TYR A CE2 
1254 C CZ  . TYR A 159 ? 0.2059 0.1752 0.1444 0.0096  0.0026  0.0073  192 TYR A CZ  
1255 O OH  . TYR A 159 ? 0.2491 0.2121 0.1885 0.0062  -0.0017 0.0121  192 TYR A OH  
1256 N N   . CYS A 160 ? 0.2167 0.2444 0.1813 0.0300  0.0380  -0.0236 193 CYS A N   
1257 C CA  . CYS A 160 ? 0.2693 0.3102 0.2486 0.0408  0.0439  -0.0298 193 CYS A CA  
1258 C C   . CYS A 160 ? 0.4179 0.4628 0.3918 0.0378  0.0566  -0.0373 193 CYS A C   
1259 O O   . CYS A 160 ? 0.4483 0.5151 0.4382 0.0400  0.0645  -0.0418 193 CYS A O   
1260 C CB  . CYS A 160 ? 0.2147 0.2800 0.2166 0.0443  0.0405  -0.0282 193 CYS A CB  
1261 S SG  . CYS A 160 ? 0.2897 0.3481 0.2924 0.0480  0.0263  -0.0195 193 CYS A SG  
1262 N N   . GLN A 161 ? 0.4025 0.4254 0.3529 0.0326  0.0583  -0.0387 194 GLN A N   
1263 C CA  . GLN A 161 ? 0.4643 0.4834 0.4005 0.0296  0.0701  -0.0460 194 GLN A CA  
1264 C C   . GLN A 161 ? 0.4271 0.4237 0.3489 0.0368  0.0707  -0.0520 194 GLN A C   
1265 O O   . GLN A 161 ? 0.4495 0.4383 0.3542 0.0345  0.0800  -0.0591 194 GLN A O   
1266 C CB  . GLN A 161 ? 0.4024 0.4133 0.3178 0.0143  0.0705  -0.0422 194 GLN A CB  
1267 C CG  . GLN A 161 ? 0.4345 0.4651 0.3611 0.0054  0.0721  -0.0376 194 GLN A CG  
1268 C CD  . GLN A 161 ? 0.5490 0.6038 0.4900 0.0063  0.0861  -0.0435 194 GLN A CD  
1269 O OE1 . GLN A 161 ? 0.7261 0.7784 0.6537 0.0042  0.0982  -0.0493 194 GLN A OE1 
1270 N NE2 . GLN A 161 ? 0.5581 0.6372 0.5266 0.0093  0.0847  -0.0424 194 GLN A NE2 
1271 N N   . ALA A 162 ? 0.3719 0.3560 0.2981 0.0444  0.0612  -0.0494 195 ALA A N   
1272 C CA  . ALA A 162 ? 0.4361 0.3954 0.3483 0.0499  0.0602  -0.0547 195 ALA A CA  
1273 C C   . ALA A 162 ? 0.4437 0.4084 0.3630 0.0619  0.0713  -0.0656 195 ALA A C   
1274 O O   . ALA A 162 ? 0.4551 0.4414 0.3988 0.0711  0.0745  -0.0665 195 ALA A O   
1275 C CB  . ALA A 162 ? 0.4235 0.3691 0.3411 0.0546  0.0481  -0.0481 195 ALA A CB  
1276 N N   . LEU A 163 ? 0.4785 0.4235 0.3769 0.0623  0.0767  -0.0743 196 LEU A N   
1277 C CA  . LEU A 163 ? 0.4982 0.4449 0.4018 0.0751  0.0881  -0.0863 196 LEU A CA  
1278 C C   . LEU A 163 ? 0.6124 0.5297 0.5078 0.0839  0.0820  -0.0908 196 LEU A C   
1279 O O   . LEU A 163 ? 0.5818 0.4786 0.4673 0.0785  0.0695  -0.0842 196 LEU A O   
1280 C CB  . LEU A 163 ? 0.6051 0.5541 0.4897 0.0693  0.1032  -0.0956 196 LEU A CB  
1281 C CG  . LEU A 163 ? 0.6487 0.6266 0.5415 0.0606  0.1129  -0.0928 196 LEU A CG  
1282 C CD1 . LEU A 163 ? 0.7585 0.7301 0.6227 0.0519  0.1264  -0.0999 196 LEU A CD1 
1283 C CD2 . LEU A 163 ? 0.7128 0.7233 0.6419 0.0715  0.1204  -0.0951 196 LEU A CD2 
1284 N N   . THR B 3   ? 0.5367 0.4776 0.6606 0.0363  -0.1433 -0.1096 36  THR B N   
1285 C CA  . THR B 3   ? 0.6081 0.5555 0.7353 0.0270  -0.1242 -0.0969 36  THR B CA  
1286 C C   . THR B 3   ? 0.4935 0.4328 0.5880 0.0271  -0.1131 -0.0819 36  THR B C   
1287 O O   . THR B 3   ? 0.4105 0.3426 0.4997 0.0263  -0.1101 -0.0813 36  THR B O   
1288 C CB  . THR B 3   ? 0.5786 0.5329 0.7427 0.0147  -0.1117 -0.1016 36  THR B CB  
1289 O OG1 . THR B 3   ? 0.7137 0.6796 0.9146 0.0137  -0.1205 -0.1179 36  THR B OG1 
1290 C CG2 . THR B 3   ? 0.4916 0.4481 0.6520 0.0066  -0.0922 -0.0879 36  THR B CG2 
1291 N N   . SER B 4   ? 0.3679 0.3088 0.4424 0.0282  -0.1075 -0.0711 37  SER B N   
1292 C CA  . SER B 4   ? 0.3764 0.3128 0.4242 0.0285  -0.0975 -0.0591 37  SER B CA  
1293 C C   . SER B 4   ? 0.2831 0.2205 0.3411 0.0209  -0.0830 -0.0531 37  SER B C   
1294 O O   . SER B 4   ? 0.2698 0.2121 0.3479 0.0138  -0.0753 -0.0524 37  SER B O   
1295 C CB  . SER B 4   ? 0.2582 0.1969 0.2864 0.0302  -0.0941 -0.0506 37  SER B CB  
1296 O OG  . SER B 4   ? 0.2644 0.2024 0.2739 0.0295  -0.0835 -0.0413 37  SER B OG  
1297 N N   . GLN B 5   ? 0.2594 0.1903 0.3009 0.0230  -0.0790 -0.0487 38  GLN B N   
1298 C CA  . GLN B 5   ? 0.2938 0.2213 0.3356 0.0186  -0.0666 -0.0415 38  GLN B CA  
1299 C C   . GLN B 5   ? 0.2690 0.2029 0.3033 0.0168  -0.0578 -0.0319 38  GLN B C   
1300 O O   . GLN B 5   ? 0.2451 0.1747 0.2799 0.0133  -0.0481 -0.0262 38  GLN B O   
1301 C CB  . GLN B 5   ? 0.3233 0.2428 0.3483 0.0237  -0.0667 -0.0405 38  GLN B CB  
1302 C CG  . GLN B 5   ? 0.4387 0.3508 0.4682 0.0264  -0.0760 -0.0502 38  GLN B CG  
1303 C CD  . GLN B 5   ? 0.6344 0.5388 0.6468 0.0323  -0.0761 -0.0496 38  GLN B CD  
1304 O OE1 . GLN B 5   ? 0.7056 0.6068 0.7104 0.0328  -0.0685 -0.0434 38  GLN B OE1 
1305 N NE2 . GLN B 5   ? 0.6756 0.5762 0.6811 0.0379  -0.0857 -0.0572 38  GLN B NE2 
1306 N N   . LEU B 6   ? 0.2395 0.1807 0.2645 0.0194  -0.0610 -0.0301 39  LEU B N   
1307 C CA  . LEU B 6   ? 0.2292 0.1768 0.2491 0.0173  -0.0532 -0.0222 39  LEU B CA  
1308 C C   . LEU B 6   ? 0.2228 0.1762 0.2587 0.0131  -0.0530 -0.0232 39  LEU B C   
1309 O O   . LEU B 6   ? 0.2374 0.1962 0.2681 0.0121  -0.0487 -0.0177 39  LEU B O   
1310 C CB  . LEU B 6   ? 0.2289 0.1796 0.2273 0.0218  -0.0540 -0.0192 39  LEU B CB  
1311 C CG  . LEU B 6   ? 0.2349 0.1831 0.2198 0.0261  -0.0526 -0.0195 39  LEU B CG  
1312 C CD1 . LEU B 6   ? 0.2477 0.2003 0.2147 0.0285  -0.0503 -0.0184 39  LEU B CD1 
1313 C CD2 . LEU B 6   ? 0.2331 0.1799 0.2207 0.0258  -0.0460 -0.0157 39  LEU B CD2 
1314 N N   . ALA B 7   ? 0.2254 0.1788 0.2826 0.0107  -0.0579 -0.0317 40  ALA B N   
1315 C CA  . ALA B 7   ? 0.2350 0.1961 0.3114 0.0076  -0.0586 -0.0354 40  ALA B CA  
1316 C C   . ALA B 7   ? 0.2439 0.2072 0.3266 0.0008  -0.0444 -0.0287 40  ALA B C   
1317 O O   . ALA B 7   ? 0.2050 0.1750 0.2901 0.0001  -0.0428 -0.0267 40  ALA B O   
1318 C CB  . ALA B 7   ? 0.2247 0.1876 0.3285 0.0060  -0.0660 -0.0486 40  ALA B CB  
1319 N N   . GLU B 8   ? 0.2321 0.1869 0.3141 -0.0034 -0.0343 -0.0252 41  GLU B N   
1320 C CA  . GLU B 8   ? 0.2169 0.1692 0.3010 -0.0094 -0.0204 -0.0192 41  GLU B CA  
1321 C C   . GLU B 8   ? 0.2288 0.1831 0.2902 -0.0053 -0.0183 -0.0094 41  GLU B C   
1322 O O   . GLU B 8   ? 0.2113 0.1692 0.2749 -0.0081 -0.0120 -0.0061 41  GLU B O   
1323 C CB  . GLU B 8   ? 0.2314 0.1678 0.3146 -0.0143 -0.0099 -0.0177 41  GLU B CB  
1324 C CG  . GLU B 8   ? 0.3157 0.2504 0.4266 -0.0216 -0.0078 -0.0284 41  GLU B CG  
1325 C CD  . GLU B 8   ? 0.4933 0.4086 0.5997 -0.0255 -0.0002 -0.0280 41  GLU B CD  
1326 O OE1 . GLU B 8   ? 0.6285 0.5320 0.7087 -0.0197 -0.0012 -0.0205 41  GLU B OE1 
1327 O OE2 . GLU B 8   ? 0.4984 0.4098 0.6280 -0.0342 0.0066  -0.0362 41  GLU B OE2 
1328 N N   . LEU B 9   ? 0.2116 0.1642 0.2538 0.0008  -0.0230 -0.0062 42  LEU B N   
1329 C CA  . LEU B 9   ? 0.2179 0.1749 0.2431 0.0042  -0.0213 0.0005  42  LEU B CA  
1330 C C   . LEU B 9   ? 0.1989 0.1663 0.2264 0.0041  -0.0250 0.0000  42  LEU B C   
1331 O O   . LEU B 9   ? 0.1905 0.1616 0.2153 0.0028  -0.0202 0.0044  42  LEU B O   
1332 C CB  . LEU B 9   ? 0.2108 0.1669 0.2202 0.0103  -0.0255 0.0008  42  LEU B CB  
1333 C CG  . LEU B 9   ? 0.2032 0.1668 0.1991 0.0138  -0.0246 0.0043  42  LEU B CG  
1334 C CD1 . LEU B 9   ? 0.2219 0.1837 0.2139 0.0133  -0.0181 0.0097  42  LEU B CD1 
1335 C CD2 . LEU B 9   ? 0.2227 0.1863 0.2084 0.0195  -0.0275 0.0018  42  LEU B CD2 
1336 N N   . VAL B 10  ? 0.1970 0.1666 0.2269 0.0064  -0.0343 -0.0055 43  VAL B N   
1337 C CA  . VAL B 10  ? 0.1935 0.1678 0.2198 0.0077  -0.0388 -0.0057 43  VAL B CA  
1338 C C   . VAL B 10  ? 0.1885 0.1674 0.2335 0.0041  -0.0370 -0.0078 43  VAL B C   
1339 O O   . VAL B 10  ? 0.1840 0.1665 0.2254 0.0040  -0.0362 -0.0051 43  VAL B O   
1340 C CB  . VAL B 10  ? 0.2028 0.1726 0.2209 0.0126  -0.0501 -0.0113 43  VAL B CB  
1341 C CG1 . VAL B 10  ? 0.2055 0.1742 0.2151 0.0147  -0.0552 -0.0112 43  VAL B CG1 
1342 C CG2 . VAL B 10  ? 0.2087 0.1744 0.2074 0.0155  -0.0492 -0.0094 43  VAL B CG2 
1343 N N   . ASP B 11  ? 0.1902 0.1692 0.2566 0.0005  -0.0353 -0.0136 44  ASP B N   
1344 C CA  . ASP B 11  ? 0.1861 0.1713 0.2740 -0.0038 -0.0314 -0.0174 44  ASP B CA  
1345 C C   . ASP B 11  ? 0.2020 0.1866 0.2836 -0.0076 -0.0184 -0.0092 44  ASP B C   
1346 O O   . ASP B 11  ? 0.2096 0.2000 0.2974 -0.0086 -0.0164 -0.0094 44  ASP B O   
1347 C CB  . ASP B 11  ? 0.2149 0.2006 0.3296 -0.0084 -0.0297 -0.0269 44  ASP B CB  
1348 C CG  . ASP B 11  ? 0.2949 0.2896 0.4371 -0.0132 -0.0251 -0.0341 44  ASP B CG  
1349 O OD1 . ASP B 11  ? 0.2400 0.2428 0.3925 -0.0087 -0.0360 -0.0412 44  ASP B OD1 
1350 O OD2 . ASP B 11  ? 0.4125 0.4042 0.5647 -0.0210 -0.0102 -0.0333 44  ASP B OD2 
1351 N N   . ALA B 12  ? 0.1874 0.1634 0.2549 -0.0086 -0.0107 -0.0027 45  ALA B N   
1352 C CA  . ALA B 12  ? 0.1882 0.1606 0.2444 -0.0101 -0.0005 0.0048  45  ALA B CA  
1353 C C   . ALA B 12  ? 0.1799 0.1590 0.2224 -0.0062 -0.0046 0.0091  45  ALA B C   
1354 O O   . ALA B 12  ? 0.1872 0.1685 0.2286 -0.0075 0.0004  0.0119  45  ALA B O   
1355 C CB  . ALA B 12  ? 0.1997 0.1586 0.2397 -0.0092 0.0054  0.0100  45  ALA B CB  
1356 N N   . ALA B 13  ? 0.1789 0.1602 0.2102 -0.0018 -0.0126 0.0092  46  ALA B N   
1357 C CA  . ALA B 13  ? 0.1729 0.1592 0.1918 0.0003  -0.0147 0.0123  46  ALA B CA  
1358 C C   . ALA B 13  ? 0.1817 0.1721 0.2081 -0.0005 -0.0181 0.0100  46  ALA B C   
1359 O O   . ALA B 13  ? 0.1657 0.1588 0.1871 -0.0011 -0.0154 0.0131  46  ALA B O   
1360 C CB  . ALA B 13  ? 0.1847 0.1709 0.1909 0.0037  -0.0200 0.0114  46  ALA B CB  
1361 N N   . ALA B 14  ? 0.1828 0.1732 0.2215 0.0003  -0.0252 0.0035  47  ALA B N   
1362 C CA  . ALA B 14  ? 0.1963 0.1894 0.2432 0.0015  -0.0307 -0.0006 47  ALA B CA  
1363 C C   . ALA B 14  ? 0.1709 0.1695 0.2335 -0.0024 -0.0224 -0.0008 47  ALA B C   
1364 O O   . ALA B 14  ? 0.1849 0.1859 0.2460 -0.0018 -0.0226 0.0002  47  ALA B O   
1365 C CB  . ALA B 14  ? 0.1777 0.1699 0.2368 0.0049  -0.0421 -0.0099 47  ALA B CB  
1366 N N   . GLU B 15  ? 0.1668 0.1653 0.2428 -0.0069 -0.0137 -0.0022 48  GLU B N   
1367 C CA  . GLU B 15  ? 0.1833 0.1841 0.2712 -0.0115 -0.0028 -0.0025 48  GLU B CA  
1368 C C   . GLU B 15  ? 0.1647 0.1627 0.2329 -0.0111 0.0034  0.0064  48  GLU B C   
1369 O O   . GLU B 15  ? 0.1775 0.1787 0.2497 -0.0122 0.0075  0.0063  48  GLU B O   
1370 C CB  . GLU B 15  ? 0.1731 0.1690 0.2735 -0.0175 0.0080  -0.0048 48  GLU B CB  
1371 C CG  . GLU B 15  ? 0.2648 0.2623 0.3810 -0.0235 0.0209  -0.0079 48  GLU B CG  
1372 C CD  . GLU B 15  ? 0.3041 0.2929 0.4309 -0.0312 0.0345  -0.0107 48  GLU B CD  
1373 O OE1 . GLU B 15  ? 0.3920 0.3785 0.5258 -0.0319 0.0304  -0.0146 48  GLU B OE1 
1374 O OE2 . GLU B 15  ? 0.3697 0.3517 0.4958 -0.0367 0.0500  -0.0090 48  GLU B OE2 
1375 N N   . ARG B 16  ? 0.1665 0.1592 0.2145 -0.0090 0.0032  0.0126  49  ARG B N   
1376 C CA  . ARG B 16  ? 0.1935 0.1848 0.2244 -0.0075 0.0068  0.0189  49  ARG B CA  
1377 C C   . ARG B 16  ? 0.1648 0.1623 0.1921 -0.0058 0.0009  0.0189  49  ARG B C   
1378 O O   . ARG B 16  ? 0.1766 0.1750 0.1991 -0.0061 0.0046  0.0213  49  ARG B O   
1379 C CB  . ARG B 16  ? 0.1917 0.1782 0.2062 -0.0044 0.0059  0.0226  49  ARG B CB  
1380 C CG  . ARG B 16  ? 0.1871 0.1686 0.1861 -0.0022 0.0107  0.0272  49  ARG B CG  
1381 C CD  . ARG B 16  ? 0.2616 0.2444 0.2486 0.0026  0.0055  0.0276  49  ARG B CD  
1382 N NE  . ARG B 16  ? 0.2451 0.2227 0.2178 0.0071  0.0069  0.0299  49  ARG B NE  
1383 C CZ  . ARG B 16  ? 0.2442 0.2287 0.2125 0.0089  0.0049  0.0294  49  ARG B CZ  
1384 N NH1 . ARG B 16  ? 0.2186 0.2132 0.1942 0.0055  0.0035  0.0281  49  ARG B NH1 
1385 N NH2 . ARG B 16  ? 0.2929 0.2723 0.2483 0.0148  0.0034  0.0296  49  ARG B NH2 
1386 N N   . LEU B 17  ? 0.1588 0.1576 0.1851 -0.0039 -0.0080 0.0163  50  LEU B N   
1387 C CA  . LEU B 17  ? 0.1670 0.1661 0.1864 -0.0025 -0.0130 0.0162  50  LEU B CA  
1388 C C   . LEU B 17  ? 0.1853 0.1871 0.2174 -0.0028 -0.0127 0.0133  50  LEU B C   
1389 O O   . LEU B 17  ? 0.1954 0.1969 0.2207 -0.0025 -0.0128 0.0151  50  LEU B O   
1390 C CB  . LEU B 17  ? 0.1995 0.1936 0.2123 0.0003  -0.0224 0.0133  50  LEU B CB  
1391 C CG  . LEU B 17  ? 0.2055 0.1964 0.2024 0.0006  -0.0223 0.0155  50  LEU B CG  
1392 C CD1 . LEU B 17  ? 0.1833 0.1651 0.1706 0.0038  -0.0311 0.0123  50  LEU B CD1 
1393 C CD2 . LEU B 17  ? 0.2317 0.2241 0.2163 -0.0015 -0.0171 0.0193  50  LEU B CD2 
1394 N N   . GLU B 18  ? 0.1569 0.1619 0.2092 -0.0036 -0.0124 0.0075  51  GLU B N   
1395 C CA  . GLU B 18  ? 0.1685 0.1784 0.2374 -0.0034 -0.0123 0.0021  51  GLU B CA  
1396 C C   . GLU B 18  ? 0.1833 0.1944 0.2503 -0.0063 -0.0011 0.0059  51  GLU B C   
1397 O O   . GLU B 18  ? 0.1798 0.1948 0.2568 -0.0057 -0.0008 0.0020  51  GLU B O   
1398 C CB  . GLU B 18  ? 0.2014 0.2169 0.2972 -0.0045 -0.0130 -0.0075 51  GLU B CB  
1399 C CG  . GLU B 18  ? 0.2492 0.2626 0.3463 0.0004  -0.0273 -0.0131 51  GLU B CG  
1400 C CD  . GLU B 18  ? 0.3679 0.3882 0.4944 -0.0009 -0.0289 -0.0243 51  GLU B CD  
1401 O OE1 . GLU B 18  ? 0.3870 0.4133 0.5336 -0.0070 -0.0168 -0.0277 51  GLU B OE1 
1402 O OE2 . GLU B 18  ? 0.3649 0.3833 0.4936 0.0039  -0.0418 -0.0304 51  GLU B OE2 
1403 N N   . VAL B 19  ? 0.1585 0.1652 0.2116 -0.0083 0.0070  0.0126  52  VAL B N   
1404 C CA  . VAL B 19  ? 0.2132 0.2178 0.2587 -0.0094 0.0156  0.0162  52  VAL B CA  
1405 C C   . VAL B 19  ? 0.2086 0.2146 0.2430 -0.0070 0.0103  0.0182  52  VAL B C   
1406 O O   . VAL B 19  ? 0.2145 0.2200 0.2457 -0.0071 0.0152  0.0192  52  VAL B O   
1407 C CB  . VAL B 19  ? 0.2370 0.2333 0.2666 -0.0098 0.0227  0.0219  52  VAL B CB  
1408 C CG1 . VAL B 19  ? 0.3331 0.3235 0.3522 -0.0099 0.0315  0.0248  52  VAL B CG1 
1409 C CG2 . VAL B 19  ? 0.2923 0.2835 0.3304 -0.0128 0.0282  0.0201  52  VAL B CG2 
1410 N N   . ALA B 20  ? 0.1676 0.1731 0.1945 -0.0051 0.0013  0.0186  53  ALA B N   
1411 C CA  . ALA B 20  ? 0.1812 0.1850 0.1971 -0.0042 -0.0024 0.0201  53  ALA B CA  
1412 C C   . ALA B 20  ? 0.1904 0.1951 0.2155 -0.0028 -0.0038 0.0163  53  ALA B C   
1413 O O   . ALA B 20  ? 0.1929 0.1961 0.2107 -0.0028 -0.0026 0.0178  53  ALA B O   
1414 C CB  . ALA B 20  ? 0.1630 0.1617 0.1680 -0.0033 -0.0099 0.0203  53  ALA B CB  
1415 N N   . ASP B 21  ? 0.1557 0.1633 0.1986 -0.0012 -0.0072 0.0100  54  ASP B N   
1416 C CA  . ASP B 21  ? 0.1608 0.1703 0.2145 0.0016  -0.0103 0.0044  54  ASP B CA  
1417 C C   . ASP B 21  ? 0.1758 0.1894 0.2350 -0.0007 0.0008  0.0046  54  ASP B C   
1418 O O   . ASP B 21  ? 0.1951 0.2063 0.2468 0.0007  0.0000  0.0055  54  ASP B O   
1419 C CB  . ASP B 21  ? 0.1935 0.2073 0.2685 0.0050  -0.0182 -0.0051 54  ASP B CB  
1420 C CG  . ASP B 21  ? 0.2574 0.2614 0.3206 0.0114  -0.0335 -0.0071 54  ASP B CG  
1421 O OD1 . ASP B 21  ? 0.3177 0.3146 0.3705 0.0147  -0.0383 -0.0068 54  ASP B OD1 
1422 O OD2 . ASP B 21  ? 0.2463 0.2469 0.3075 0.0133  -0.0404 -0.0087 54  ASP B OD2 
1423 N N   . PRO B 22  ? 0.1676 0.1845 0.2369 -0.0045 0.0121  0.0038  55  PRO B N   
1424 C CA  . PRO B 22  ? 0.1997 0.2159 0.2675 -0.0063 0.0238  0.0045  55  PRO B CA  
1425 C C   . PRO B 22  ? 0.1915 0.2009 0.2343 -0.0056 0.0250  0.0123  55  PRO B C   
1426 O O   . PRO B 22  ? 0.1850 0.1930 0.2229 -0.0047 0.0286  0.0122  55  PRO B O   
1427 C CB  . PRO B 22  ? 0.2606 0.2758 0.3378 -0.0112 0.0367  0.0032  55  PRO B CB  
1428 C CG  . PRO B 22  ? 0.2748 0.2888 0.3510 -0.0118 0.0314  0.0050  55  PRO B CG  
1429 C CD  . PRO B 22  ? 0.2058 0.2244 0.2866 -0.0074 0.0157  0.0017  55  PRO B CD  
1430 N N   . VAL B 23  ? 0.1693 0.1754 0.1977 -0.0056 0.0215  0.0177  56  VAL B N   
1431 C CA  . VAL B 23  ? 0.1722 0.1745 0.1812 -0.0045 0.0210  0.0223  56  VAL B CA  
1432 C C   . VAL B 23  ? 0.2198 0.2230 0.2253 -0.0034 0.0142  0.0214  56  VAL B C   
1433 O O   . VAL B 23  ? 0.1751 0.1765 0.1724 -0.0026 0.0159  0.0219  56  VAL B O   
1434 C CB  . VAL B 23  ? 0.1977 0.1988 0.1968 -0.0043 0.0182  0.0257  56  VAL B CB  
1435 C CG1 . VAL B 23  ? 0.1972 0.1983 0.1825 -0.0029 0.0151  0.0272  56  VAL B CG1 
1436 C CG2 . VAL B 23  ? 0.1858 0.1806 0.1814 -0.0044 0.0258  0.0276  56  VAL B CG2 
1437 N N   . ALA B 24  ? 0.1688 0.1720 0.1780 -0.0031 0.0063  0.0197  57  ALA B N   
1438 C CA  . ALA B 24  ? 0.1682 0.1668 0.1700 -0.0023 0.0006  0.0192  57  ALA B CA  
1439 C C   . ALA B 24  ? 0.2031 0.2022 0.2124 -0.0001 0.0018  0.0155  57  ALA B C   
1440 O O   . ALA B 24  ? 0.1801 0.1757 0.1809 0.0000  0.0015  0.0160  57  ALA B O   
1441 C CB  . ALA B 24  ? 0.1862 0.1786 0.1847 -0.0013 -0.0080 0.0183  57  ALA B CB  
1442 N N   . ALA B 25  ? 0.1765 0.1805 0.2035 0.0014  0.0035  0.0106  58  ALA B N   
1443 C CA  . ALA B 25  ? 0.1937 0.1999 0.2307 0.0038  0.0054  0.0054  58  ALA B CA  
1444 C C   . ALA B 25  ? 0.1728 0.1781 0.2012 0.0023  0.0153  0.0079  58  ALA B C   
1445 O O   . ALA B 25  ? 0.2080 0.2111 0.2328 0.0043  0.0147  0.0062  58  ALA B O   
1446 C CB  . ALA B 25  ? 0.1647 0.1793 0.2272 0.0047  0.0074  -0.0027 58  ALA B CB  
1447 N N   . PHE B 26  ? 0.1876 0.1923 0.2099 -0.0002 0.0235  0.0117  59  PHE B N   
1448 C CA  . PHE B 26  ? 0.2094 0.2090 0.2175 0.0002  0.0313  0.0141  59  PHE B CA  
1449 C C   . PHE B 26  ? 0.2041 0.2006 0.1962 0.0014  0.0245  0.0167  59  PHE B C   
1450 O O   . PHE B 26  ? 0.2101 0.2035 0.1949 0.0032  0.0260  0.0155  59  PHE B O   
1451 C CB  . PHE B 26  ? 0.1848 0.1791 0.1844 -0.0013 0.0396  0.0178  59  PHE B CB  
1452 C CG  . PHE B 26  ? 0.1988 0.1830 0.1793 0.0007  0.0474  0.0198  59  PHE B CG  
1453 C CD1 . PHE B 26  ? 0.2308 0.2100 0.2132 -0.0003 0.0601  0.0172  59  PHE B CD1 
1454 C CD2 . PHE B 26  ? 0.2116 0.1907 0.1723 0.0040  0.0419  0.0230  59  PHE B CD2 
1455 C CE1 . PHE B 26  ? 0.3073 0.2728 0.2664 0.0023  0.0675  0.0193  59  PHE B CE1 
1456 C CE2 . PHE B 26  ? 0.2319 0.1991 0.1717 0.0077  0.0468  0.0240  59  PHE B CE2 
1457 C CZ  . PHE B 26  ? 0.2380 0.1965 0.1744 0.0071  0.0597  0.0229  59  PHE B CZ  
1458 N N   . LYS B 27  ? 0.1976 0.1949 0.1849 0.0001  0.0179  0.0192  60  LYS B N   
1459 C CA  . LYS B 27  ? 0.1945 0.1905 0.1706 -0.0003 0.0132  0.0196  60  LYS B CA  
1460 C C   . LYS B 27  ? 0.1769 0.1699 0.1541 -0.0003 0.0092  0.0171  60  LYS B C   
1461 O O   . LYS B 27  ? 0.1880 0.1787 0.1578 -0.0001 0.0084  0.0158  60  LYS B O   
1462 C CB  . LYS B 27  ? 0.1743 0.1726 0.1481 -0.0028 0.0090  0.0212  60  LYS B CB  
1463 C CG  . LYS B 27  ? 0.1952 0.1956 0.1649 -0.0015 0.0110  0.0228  60  LYS B CG  
1464 C CD  . LYS B 27  ? 0.2275 0.2319 0.1977 -0.0041 0.0072  0.0228  60  LYS B CD  
1465 C CE  . LYS B 27  ? 0.2917 0.2985 0.2577 -0.0014 0.0072  0.0228  60  LYS B CE  
1466 N NZ  . LYS B 27  ? 0.3411 0.3533 0.3101 -0.0041 0.0046  0.0215  60  LYS B NZ  
1467 N N   . TRP B 28  ? 0.1763 0.1677 0.1617 0.0002  0.0056  0.0157  61  TRP B N   
1468 C CA  . TRP B 28  ? 0.1829 0.1674 0.1664 0.0016  0.0003  0.0132  61  TRP B CA  
1469 C C   . TRP B 28  ? 0.1987 0.1841 0.1851 0.0045  0.0040  0.0099  61  TRP B C   
1470 O O   . TRP B 28  ? 0.1924 0.1725 0.1706 0.0046  0.0022  0.0089  61  TRP B O   
1471 C CB  . TRP B 28  ? 0.1899 0.1708 0.1805 0.0044  -0.0064 0.0109  61  TRP B CB  
1472 C CG  . TRP B 28  ? 0.2001 0.1701 0.1858 0.0078  -0.0134 0.0080  61  TRP B CG  
1473 C CD1 . TRP B 28  ? 0.2008 0.1720 0.1964 0.0129  -0.0148 0.0024  61  TRP B CD1 
1474 C CD2 . TRP B 28  ? 0.2124 0.1659 0.1802 0.0065  -0.0193 0.0101  61  TRP B CD2 
1475 N NE1 . TRP B 28  ? 0.2189 0.1750 0.2032 0.0160  -0.0232 0.0011  61  TRP B NE1 
1476 C CE2 . TRP B 28  ? 0.2317 0.1749 0.1971 0.0117  -0.0255 0.0063  61  TRP B CE2 
1477 C CE3 . TRP B 28  ? 0.2513 0.1963 0.2040 0.0011  -0.0188 0.0144  61  TRP B CE3 
1478 C CZ2 . TRP B 28  ? 0.2420 0.1632 0.1869 0.0118  -0.0314 0.0077  61  TRP B CZ2 
1479 C CZ3 . TRP B 28  ? 0.2349 0.1590 0.1684 -0.0001 -0.0226 0.0154  61  TRP B CZ3 
1480 C CH2 . TRP B 28  ? 0.2811 0.1917 0.2091 0.0053  -0.0290 0.0126  61  TRP B CH2 
1481 N N   . ARG B 29  ? 0.1847 0.1761 0.1830 0.0064  0.0103  0.0074  62  ARG B N   
1482 C CA  . ARG B 29  ? 0.2159 0.2078 0.2176 0.0091  0.0157  0.0032  62  ARG B CA  
1483 C C   . ARG B 29  ? 0.2187 0.2069 0.2041 0.0088  0.0209  0.0057  62  ARG B C   
1484 O O   . ARG B 29  ? 0.2422 0.2267 0.2221 0.0110  0.0208  0.0031  62  ARG B O   
1485 C CB  . ARG B 29  ? 0.2261 0.2252 0.2462 0.0096  0.0238  -0.0014 62  ARG B CB  
1486 C CG  . ARG B 29  ? 0.3350 0.3357 0.3627 0.0121  0.0311  -0.0078 62  ARG B CG  
1487 C CD  . ARG B 29  ? 0.4900 0.4865 0.5146 0.0162  0.0219  -0.0109 62  ARG B CD  
1488 N NE  . ARG B 29  ? 0.6387 0.6402 0.6804 0.0202  0.0250  -0.0202 62  ARG B NE  
1489 C CZ  . ARG B 29  ? 0.7099 0.7122 0.7514 0.0204  0.0369  -0.0234 62  ARG B CZ  
1490 N NH1 . ARG B 29  ? 0.7400 0.7360 0.7624 0.0177  0.0465  -0.0178 62  ARG B NH1 
1491 N NH2 . ARG B 29  ? 0.6996 0.7080 0.7594 0.0242  0.0391  -0.0335 62  ARG B NH2 
1492 N N   . ALA B 30  ? 0.1956 0.1836 0.1723 0.0074  0.0241  0.0098  63  ALA B N   
1493 C CA  . ALA B 30  ? 0.2052 0.1877 0.1646 0.0094  0.0268  0.0109  63  ALA B CA  
1494 C C   . ALA B 30  ? 0.2065 0.1889 0.1575 0.0088  0.0181  0.0108  63  ALA B C   
1495 O O   . ALA B 30  ? 0.2341 0.2130 0.1719 0.0117  0.0173  0.0098  63  ALA B O   
1496 C CB  . ALA B 30  ? 0.2158 0.1947 0.1671 0.0098  0.0335  0.0144  63  ALA B CB  
1497 N N   . GLN B 31  ? 0.1966 0.1815 0.1542 0.0052  0.0119  0.0108  64  GLN B N   
1498 C CA  . GLN B 31  ? 0.1971 0.1817 0.1502 0.0023  0.0061  0.0092  64  GLN B CA  
1499 C C   . GLN B 31  ? 0.2362 0.2258 0.1853 0.0022  0.0048  0.0091  64  GLN B C   
1500 O O   . GLN B 31  ? 0.2350 0.2264 0.1809 0.0020  0.0012  0.0049  64  GLN B O   
1501 C CB  . GLN B 31  ? 0.2279 0.2079 0.1756 0.0039  0.0045  0.0051  64  GLN B CB  
1502 C CG  . GLN B 31  ? 0.2085 0.1829 0.1607 0.0047  0.0040  0.0041  64  GLN B CG  
1503 C CD  . GLN B 31  ? 0.2504 0.2185 0.1972 0.0054  0.0012  0.0000  64  GLN B CD  
1504 O OE1 . GLN B 31  ? 0.2528 0.2202 0.1951 0.0023  -0.0016 -0.0024 64  GLN B OE1 
1505 N NE2 . GLN B 31  ? 0.2388 0.2030 0.1879 0.0093  0.0021  -0.0022 64  GLN B NE2 
1506 N N   A LEU B 32  ? 0.1909 0.1832 0.1417 0.0028  0.0071  0.0125  65  LEU B N   
1507 N N   B LEU B 32  ? 0.1909 0.1832 0.1417 0.0027  0.0071  0.0125  65  LEU B N   
1508 C CA  A LEU B 32  ? 0.1897 0.1867 0.1380 0.0034  0.0046  0.0117  65  LEU B CA  
1509 C CA  B LEU B 32  ? 0.1897 0.1867 0.1380 0.0034  0.0046  0.0117  65  LEU B CA  
1510 C C   A LEU B 32  ? 0.2125 0.2151 0.1685 -0.0027 0.0018  0.0100  65  LEU B C   
1511 C C   B LEU B 32  ? 0.2123 0.2149 0.1682 -0.0028 0.0018  0.0100  65  LEU B C   
1512 O O   A LEU B 32  ? 0.2147 0.2145 0.1744 -0.0067 0.0027  0.0124  65  LEU B O   
1513 O O   B LEU B 32  ? 0.2147 0.2144 0.1744 -0.0067 0.0027  0.0125  65  LEU B O   
1514 C CB  A LEU B 32  ? 0.2072 0.2027 0.1538 0.0058  0.0083  0.0159  65  LEU B CB  
1515 C CB  B LEU B 32  ? 0.2060 0.2017 0.1526 0.0057  0.0081  0.0159  65  LEU B CB  
1516 C CG  A LEU B 32  ? 0.2120 0.1981 0.1450 0.0117  0.0130  0.0175  65  LEU B CG  
1517 C CG  B LEU B 32  ? 0.2109 0.1977 0.1433 0.0120  0.0119  0.0172  65  LEU B CG  
1518 C CD1 A LEU B 32  ? 0.2213 0.2038 0.1559 0.0109  0.0195  0.0218  65  LEU B CD1 
1519 C CD1 B LEU B 32  ? 0.2091 0.1894 0.1400 0.0123  0.0192  0.0182  65  LEU B CD1 
1520 C CD2 A LEU B 32  ? 0.2547 0.2384 0.1744 0.0177  0.0071  0.0144  65  LEU B CD2 
1521 C CD2 B LEU B 32  ? 0.2568 0.2410 0.1872 0.0128  0.0146  0.0209  65  LEU B CD2 
1522 N N   . PRO B 33  ? 0.2515 0.2610 0.2093 -0.0033 -0.0015 0.0049  66  PRO B N   
1523 C CA  . PRO B 33  ? 0.2537 0.2687 0.2193 -0.0102 -0.0010 0.0026  66  PRO B CA  
1524 C C   . PRO B 33  ? 0.2162 0.2311 0.1828 -0.0107 0.0010  0.0076  66  PRO B C   
1525 O O   . PRO B 33  ? 0.2581 0.2740 0.2226 -0.0055 0.0006  0.0100  66  PRO B O   
1526 C CB  . PRO B 33  ? 0.2990 0.3246 0.2702 -0.0086 -0.0050 -0.0061 66  PRO B CB  
1527 C CG  . PRO B 33  ? 0.4112 0.4343 0.3730 0.0015  -0.0094 -0.0062 66  PRO B CG  
1528 C CD  . PRO B 33  ? 0.2798 0.2917 0.2323 0.0032  -0.0060 -0.0003 66  PRO B CD  
1529 N N   . ILE B 34  ? 0.2316 0.2423 0.1988 -0.0168 0.0033  0.0093  67  ILE B N   
1530 C CA  . ILE B 34  ? 0.2106 0.2198 0.1777 -0.0167 0.0041  0.0135  67  ILE B CA  
1531 C C   . ILE B 34  ? 0.2620 0.2811 0.2339 -0.0168 0.0043  0.0103  67  ILE B C   
1532 O O   . ILE B 34  ? 0.2428 0.2635 0.2151 -0.0131 0.0035  0.0129  67  ILE B O   
1533 C CB  . ILE B 34  ? 0.2698 0.2673 0.2310 -0.0215 0.0051  0.0158  67  ILE B CB  
1534 C CG1 . ILE B 34  ? 0.2215 0.2162 0.1815 -0.0201 0.0042  0.0193  67  ILE B CG1 
1535 C CG2 . ILE B 34  ? 0.3497 0.3444 0.3081 -0.0294 0.0090  0.0117  67  ILE B CG2 
1536 C CD1 . ILE B 34  ? 0.2305 0.2097 0.1811 -0.0206 0.0018  0.0216  67  ILE B CD1 
1537 N N   . GLU B 35  ? 0.2356 0.2620 0.2130 -0.0207 0.0052  0.0033  68  GLU B N   
1538 C CA  . GLU B 35  ? 0.2076 0.2459 0.1931 -0.0202 0.0049  -0.0025 68  GLU B CA  
1539 C C   . GLU B 35  ? 0.2186 0.2649 0.2070 -0.0118 -0.0016 -0.0074 68  GLU B C   
1540 O O   . GLU B 35  ? 0.2343 0.2810 0.2225 -0.0103 -0.0043 -0.0111 68  GLU B O   
1541 C CB  . GLU B 35  ? 0.2314 0.2742 0.2242 -0.0296 0.0105  -0.0099 68  GLU B CB  
1542 C CG  . GLU B 35  ? 0.1656 0.2216 0.1696 -0.0307 0.0124  -0.0172 68  GLU B CG  
1543 C CD  . GLU B 35  ? 0.2203 0.2687 0.2170 -0.0343 0.0176  -0.0121 68  GLU B CD  
1544 O OE1 . GLU B 35  ? 0.2646 0.2975 0.2476 -0.0349 0.0181  -0.0032 68  GLU B OE1 
1545 O OE2 . GLU B 35  ? 0.2123 0.2704 0.2173 -0.0357 0.0204  -0.0180 68  GLU B OE2 
1546 N N   . ASP B 36  ? 0.2167 0.2668 0.2051 -0.0053 -0.0049 -0.0078 69  ASP B N   
1547 C CA  . ASP B 36  ? 0.2436 0.2963 0.2291 0.0049  -0.0127 -0.0126 69  ASP B CA  
1548 C C   . ASP B 36  ? 0.1846 0.2467 0.1771 0.0092  -0.0165 -0.0186 69  ASP B C   
1549 O O   . ASP B 36  ? 0.1892 0.2442 0.1732 0.0145  -0.0176 -0.0132 69  ASP B O   
1550 C CB  . ASP B 36  ? 0.2735 0.3112 0.2422 0.0113  -0.0130 -0.0038 69  ASP B CB  
1551 C CG  . ASP B 36  ? 0.4034 0.4358 0.3602 0.0227  -0.0207 -0.0074 69  ASP B CG  
1552 O OD1 . ASP B 36  ? 0.3082 0.3503 0.2715 0.0278  -0.0285 -0.0176 69  ASP B OD1 
1553 O OD2 . ASP B 36  ? 0.4341 0.4513 0.3742 0.0269  -0.0186 -0.0007 69  ASP B OD2 
1554 N N   . SER B 37  ? 0.1539 0.2102 0.1632 -0.0002 -0.0230 -0.0134 70  SER B N   
1555 C CA  . SER B 37  ? 0.1552 0.2192 0.1623 -0.0001 -0.0279 -0.0038 70  SER B CA  
1556 C C   . SER B 37  ? 0.2134 0.2699 0.2056 -0.0054 -0.0230 -0.0007 70  SER B C   
1557 O O   . SER B 37  ? 0.1657 0.2288 0.1633 -0.0039 -0.0234 0.0033  70  SER B O   
1558 C CB  . SER B 37  ? 0.1602 0.2260 0.1636 -0.0009 -0.0383 0.0051  70  SER B CB  
1559 O OG  . SER B 37  ? 0.2152 0.2702 0.2033 -0.0067 -0.0429 0.0089  70  SER B OG  
1560 N N   . GLY B 38  ? 0.2143 0.2522 0.1834 -0.0120 -0.0191 -0.0028 71  GLY B N   
1561 C CA  . GLY B 38  ? 0.2368 0.2579 0.1817 -0.0190 -0.0168 0.0008  71  GLY B CA  
1562 C C   . GLY B 38  ? 0.2747 0.2976 0.2261 -0.0196 -0.0022 -0.0048 71  GLY B C   
1563 O O   . GLY B 38  ? 0.2335 0.2524 0.1781 -0.0216 -0.0043 0.0009  71  GLY B O   
1564 N N   . ARG B 39  ? 0.2175 0.2465 0.1872 -0.0178 0.0118  -0.0166 72  ARG B N   
1565 C CA  . ARG B 39  ? 0.2445 0.2792 0.2314 -0.0184 0.0253  -0.0229 72  ARG B CA  
1566 C C   . ARG B 39  ? 0.1989 0.2531 0.2092 -0.0111 0.0150  -0.0181 72  ARG B C   
1567 O O   . ARG B 39  ? 0.2066 0.2599 0.2177 -0.0132 0.0194  -0.0169 72  ARG B O   
1568 C CB  . ARG B 39  ? 0.2603 0.3004 0.2750 -0.0171 0.0404  -0.0378 72  ARG B CB  
1569 C CG  . ARG B 39  ? 0.4349 0.4508 0.4260 -0.0278 0.0635  -0.0465 72  ARG B CG  
1570 C CD  . ARG B 39  ? 0.4834 0.5080 0.5151 -0.0279 0.0857  -0.0631 72  ARG B CD  
1571 N NE  . ARG B 39  ? 0.4864 0.4843 0.4916 -0.0408 0.1150  -0.0721 72  ARG B NE  
1572 C CZ  . ARG B 39  ? 0.5609 0.5421 0.5547 -0.0445 0.1305  -0.0827 72  ARG B CZ  
1573 N NH1 . ARG B 39  ? 0.5038 0.4940 0.5142 -0.0355 0.1175  -0.0854 72  ARG B NH1 
1574 N NH2 . ARG B 39  ? 0.5026 0.4535 0.4643 -0.0585 0.1610  -0.0913 72  ARG B NH2 
1575 N N   . VAL B 40  ? 0.1567 0.2243 0.1819 -0.0034 0.0021  -0.0158 73  VAL B N   
1576 C CA  . VAL B 40  ? 0.1410 0.2201 0.1788 0.0022  -0.0060 -0.0120 73  VAL B CA  
1577 C C   . VAL B 40  ? 0.1596 0.2350 0.1829 0.0004  -0.0092 -0.0026 73  VAL B C   
1578 O O   . VAL B 40  ? 0.1449 0.2231 0.1744 0.0018  -0.0082 -0.0019 73  VAL B O   
1579 C CB  . VAL B 40  ? 0.1508 0.2357 0.1948 0.0079  -0.0175 -0.0104 73  VAL B CB  
1580 C CG1 . VAL B 40  ? 0.1329 0.2218 0.1778 0.0115  -0.0227 -0.0061 73  VAL B CG1 
1581 C CG2 . VAL B 40  ? 0.1370 0.2231 0.2007 0.0111  -0.0196 -0.0197 73  VAL B CG2 
1582 N N   . GLU B 41  ? 0.1292 0.1973 0.1363 -0.0025 -0.0152 0.0044  74  GLU B N   
1583 C CA  . GLU B 41  ? 0.1597 0.2237 0.1611 -0.0035 -0.0220 0.0128  74  GLU B CA  
1584 C C   . GLU B 41  ? 0.2020 0.2506 0.1884 -0.0092 -0.0168 0.0130  74  GLU B C   
1585 O O   . GLU B 41  ? 0.1711 0.2202 0.1630 -0.0073 -0.0199 0.0167  74  GLU B O   
1586 C CB  . GLU B 41  ? 0.1689 0.2261 0.1612 -0.0063 -0.0335 0.0199  74  GLU B CB  
1587 C CG  . GLU B 41  ? 0.2066 0.2547 0.1965 -0.0080 -0.0455 0.0285  74  GLU B CG  
1588 C CD  . GLU B 41  ? 0.2000 0.2653 0.2197 -0.0007 -0.0473 0.0308  74  GLU B CD  
1589 O OE1 . GLU B 41  ? 0.1615 0.2428 0.1967 0.0043  -0.0399 0.0271  74  GLU B OE1 
1590 O OE2 . GLU B 41  ? 0.2159 0.2748 0.2412 -0.0003 -0.0563 0.0360  74  GLU B OE2 
1591 N N   A GLN B 42  ? 0.2263 0.2582 0.1919 -0.0170 -0.0072 0.0086  75  GLN B N   
1592 N N   B GLN B 42  ? 0.2263 0.2582 0.1920 -0.0170 -0.0071 0.0085  75  GLN B N   
1593 C CA  A GLN B 42  ? 0.2454 0.2569 0.1903 -0.0252 0.0010  0.0088  75  GLN B CA  
1594 C CA  B GLN B 42  ? 0.2453 0.2569 0.1902 -0.0252 0.0008  0.0089  75  GLN B CA  
1595 C C   A GLN B 42  ? 0.2258 0.2510 0.1952 -0.0221 0.0098  0.0038  75  GLN B C   
1596 C C   B GLN B 42  ? 0.2259 0.2509 0.1952 -0.0222 0.0099  0.0038  75  GLN B C   
1597 O O   A GLN B 42  ? 0.2436 0.2596 0.2063 -0.0245 0.0081  0.0082  75  GLN B O   
1598 O O   B GLN B 42  ? 0.2436 0.2594 0.2062 -0.0246 0.0084  0.0081  75  GLN B O   
1599 C CB  A GLN B 42  ? 0.3162 0.3044 0.2323 -0.0357 0.0162  0.0025  75  GLN B CB  
1600 C CB  B GLN B 42  ? 0.3174 0.3044 0.2318 -0.0360 0.0155  0.0031  75  GLN B CB  
1601 C CG  A GLN B 42  ? 0.3455 0.3079 0.2238 -0.0419 0.0053  0.0084  75  GLN B CG  
1602 C CG  B GLN B 42  ? 0.3455 0.3412 0.2805 -0.0374 0.0384  -0.0104 75  GLN B CG  
1603 C CD  A GLN B 42  ? 0.4289 0.3595 0.2683 -0.0542 0.0238  0.0010  75  GLN B CD  
1604 C CD  B GLN B 42  ? 0.3793 0.3457 0.2813 -0.0500 0.0589  -0.0175 75  GLN B CD  
1605 O OE1 A GLN B 42  ? 0.4819 0.4168 0.3275 -0.0533 0.0340  -0.0081 75  GLN B OE1 
1606 O OE1 B GLN B 42  ? 0.4772 0.4149 0.3353 -0.0571 0.0533  -0.0125 75  GLN B OE1 
1607 N NE2 A GLN B 42  ? 0.4306 0.3255 0.2273 -0.0664 0.0292  0.0044  75  GLN B NE2 
1608 N NE2 B GLN B 42  ? 0.3610 0.3321 0.2846 -0.0536 0.0832  -0.0301 75  GLN B NE2 
1609 N N   . GLN B 43  ? 0.1933 0.2381 0.1919 -0.0168 0.0159  -0.0051 76  GLN B N   
1610 C CA  . GLN B 43  ? 0.2030 0.2592 0.2274 -0.0141 0.0202  -0.0104 76  GLN B CA  
1611 C C   . GLN B 43  ? 0.1529 0.2161 0.1832 -0.0072 0.0077  -0.0042 76  GLN B C   
1612 O O   . GLN B 43  ? 0.1432 0.2031 0.1770 -0.0084 0.0093  -0.0038 76  GLN B O   
1613 C CB  . GLN B 43  ? 0.1804 0.2526 0.2365 -0.0090 0.0219  -0.0205 76  GLN B CB  
1614 C CG  . GLN B 43  ? 0.2893 0.3584 0.3551 -0.0144 0.0380  -0.0308 76  GLN B CG  
1615 C CD  . GLN B 43  ? 0.4400 0.5255 0.5465 -0.0071 0.0330  -0.0404 76  GLN B CD  
1616 O OE1 . GLN B 43  ? 0.4573 0.5520 0.5939 -0.0046 0.0295  -0.0451 76  GLN B OE1 
1617 N NE2 . GLN B 43  ? 0.3967 0.4831 0.5040 -0.0037 0.0289  -0.0426 76  GLN B NE2 
1618 N N   . LEU B 44  ? 0.1490 0.2205 0.1811 -0.0005 -0.0027 -0.0002 77  LEU B N   
1619 C CA  . LEU B 44  ? 0.1327 0.2094 0.1715 0.0057  -0.0096 0.0034  77  LEU B CA  
1620 C C   . LEU B 44  ? 0.1487 0.2149 0.1786 0.0039  -0.0135 0.0107  77  LEU B C   
1621 O O   . LEU B 44  ? 0.1473 0.2131 0.1845 0.0072  -0.0148 0.0110  77  LEU B O   
1622 C CB  . LEU B 44  ? 0.1029 0.1878 0.1447 0.0108  -0.0149 0.0051  77  LEU B CB  
1623 C CG  . LEU B 44  ? 0.1000 0.1892 0.1476 0.0134  -0.0160 -0.0012 77  LEU B CG  
1624 C CD1 . LEU B 44  ? 0.1163 0.2072 0.1588 0.0161  -0.0196 0.0018  77  LEU B CD1 
1625 C CD2 . LEU B 44  ? 0.1299 0.2176 0.1856 0.0157  -0.0173 -0.0068 77  LEU B CD2 
1626 N N   . ALA B 45  ? 0.1569 0.2112 0.1702 -0.0012 -0.0179 0.0166  78  ALA B N   
1627 C CA  . ALA B 45  ? 0.1908 0.2294 0.1949 -0.0033 -0.0272 0.0244  78  ALA B CA  
1628 C C   . ALA B 45  ? 0.2097 0.2333 0.2021 -0.0091 -0.0209 0.0234  78  ALA B C   
1629 O O   . ALA B 45  ? 0.2112 0.2293 0.2091 -0.0066 -0.0267 0.0266  78  ALA B O   
1630 C CB  . ALA B 45  ? 0.2501 0.2710 0.2321 -0.0094 -0.0376 0.0312  78  ALA B CB  
1631 N N   . LYS B 46  ? 0.2213 0.2374 0.2005 -0.0173 -0.0072 0.0180  79  LYS B N   
1632 C CA  . LYS B 46  ? 0.2122 0.2142 0.1833 -0.0249 0.0026  0.0163  79  LYS B CA  
1633 C C   . LYS B 46  ? 0.2217 0.2404 0.2219 -0.0179 0.0031  0.0117  79  LYS B C   
1634 O O   . LYS B 46  ? 0.2052 0.2122 0.2020 -0.0202 0.0016  0.0143  79  LYS B O   
1635 C CB  . LYS B 46  ? 0.2434 0.2379 0.2047 -0.0352 0.0224  0.0086  79  LYS B CB  
1636 C CG  . LYS B 46  ? 0.3396 0.3178 0.2936 -0.0458 0.0369  0.0063  79  LYS B CG  
1637 C CD  . LYS B 46  ? 0.3962 0.3715 0.3523 -0.0557 0.0619  -0.0044 79  LYS B CD  
1638 C CE  . LYS B 46  ? 0.4700 0.4206 0.4093 -0.0707 0.0806  -0.0056 79  LYS B CE  
1639 N NZ  . LYS B 46  ? 0.5980 0.5570 0.5604 -0.0675 0.0738  -0.0039 79  LYS B NZ  
1640 N N   . LEU B 47  ? 0.1707 0.2119 0.1953 -0.0101 0.0034  0.0050  80  LEU B N   
1641 C CA  . LEU B 47  ? 0.1631 0.2132 0.2079 -0.0047 0.0016  0.0002  80  LEU B CA  
1642 C C   . LEU B 47  ? 0.1767 0.2240 0.2212 0.0023  -0.0079 0.0051  80  LEU B C   
1643 O O   . LEU B 47  ? 0.1850 0.2280 0.2356 0.0036  -0.0089 0.0032  80  LEU B O   
1644 C CB  . LEU B 47  ? 0.1245 0.1905 0.1870 0.0010  -0.0003 -0.0070 80  LEU B CB  
1645 C CG  . LEU B 47  ? 0.1591 0.2299 0.2378 -0.0044 0.0084  -0.0151 80  LEU B CG  
1646 C CD1 . LEU B 47  ? 0.1486 0.2306 0.2401 0.0018  0.0015  -0.0198 80  LEU B CD1 
1647 C CD2 . LEU B 47  ? 0.1753 0.2451 0.2736 -0.0081 0.0118  -0.0208 80  LEU B CD2 
1648 N N   . GLY B 48  ? 0.1393 0.1890 0.1810 0.0068  -0.0143 0.0105  81  GLY B N   
1649 C CA  . GLY B 48  ? 0.1803 0.2277 0.2302 0.0135  -0.0210 0.0137  81  GLY B CA  
1650 C C   . GLY B 48  ? 0.2323 0.2603 0.2740 0.0094  -0.0264 0.0190  81  GLY B C   
1651 O O   . GLY B 48  ? 0.2297 0.2534 0.2809 0.0141  -0.0288 0.0178  81  GLY B O   
1652 N N   . GLU B 49  ? 0.1822 0.1933 0.2015 -0.0001 -0.0281 0.0247  82  GLU B N   
1653 C CA  . GLU B 49  ? 0.2112 0.1959 0.2144 -0.0059 -0.0350 0.0312  82  GLU B CA  
1654 C C   . GLU B 49  ? 0.2285 0.2064 0.2288 -0.0121 -0.0243 0.0267  82  GLU B C   
1655 O O   . GLU B 49  ? 0.2355 0.1965 0.2325 -0.0131 -0.0303 0.0301  82  GLU B O   
1656 C CB  . GLU B 49  ? 0.2867 0.2457 0.2562 -0.0163 -0.0415 0.0394  82  GLU B CB  
1657 C CG  . GLU B 49  ? 0.3274 0.2905 0.3049 -0.0103 -0.0577 0.0448  82  GLU B CG  
1658 C CD  . GLU B 49  ? 0.3503 0.3234 0.3630 0.0020  -0.0705 0.0462  82  GLU B CD  
1659 O OE1 . GLU B 49  ? 0.3298 0.2851 0.3421 0.0024  -0.0792 0.0496  82  GLU B OE1 
1660 O OE2 . GLU B 49  ? 0.2400 0.2373 0.2821 0.0108  -0.0701 0.0430  82  GLU B OE2 
1661 N N   . ASP B 50  ? 0.2065 0.1969 0.2127 -0.0163 -0.0098 0.0188  83  ASP B N   
1662 C CA  . ASP B 50  ? 0.2107 0.2000 0.2270 -0.0211 -0.0009 0.0129  83  ASP B CA  
1663 C C   . ASP B 50  ? 0.1949 0.1929 0.2315 -0.0107 -0.0086 0.0092  83  ASP B C   
1664 O O   . ASP B 50  ? 0.2351 0.2211 0.2731 -0.0135 -0.0095 0.0090  83  ASP B O   
1665 C CB  . ASP B 50  ? 0.1985 0.2028 0.2298 -0.0257 0.0131  0.0037  83  ASP B CB  
1666 C CG  . ASP B 50  ? 0.4006 0.3918 0.4101 -0.0377 0.0266  0.0048  83  ASP B CG  
1667 O OD1 . ASP B 50  ? 0.3584 0.3210 0.3333 -0.0463 0.0259  0.0131  83  ASP B OD1 
1668 O OD2 . ASP B 50  ? 0.4026 0.4080 0.4272 -0.0389 0.0372  -0.0031 83  ASP B OD2 
1669 N N   . ALA B 51  ? 0.2025 0.2175 0.2511 0.0001  -0.0129 0.0059  84  ALA B N   
1670 C CA  . ALA B 51  ? 0.2245 0.2414 0.2838 0.0092  -0.0176 0.0015  84  ALA B CA  
1671 C C   . ALA B 51  ? 0.2162 0.2180 0.2740 0.0125  -0.0245 0.0067  84  ALA B C   
1672 O O   . ALA B 51  ? 0.2185 0.2103 0.2798 0.0139  -0.0263 0.0037  84  ALA B O   
1673 C CB  . ALA B 51  ? 0.1970 0.2280 0.2607 0.0178  -0.0176 -0.0018 84  ALA B CB  
1674 N N   . ARG B 52  ? 0.1972 0.1948 0.2513 0.0137  -0.0309 0.0145  85  ARG B N   
1675 C CA  . ARG B 52  ? 0.2358 0.2169 0.2940 0.0174  -0.0421 0.0199  85  ARG B CA  
1676 C C   . ARG B 52  ? 0.2477 0.2044 0.2896 0.0081  -0.0444 0.0237  85  ARG B C   
1677 O O   . ARG B 52  ? 0.2604 0.2041 0.3092 0.0120  -0.0508 0.0235  85  ARG B O   
1678 C CB  . ARG B 52  ? 0.2151 0.1923 0.2732 0.0183  -0.0537 0.0285  85  ARG B CB  
1679 C CG  . ARG B 52  ? 0.2890 0.2560 0.3677 0.0267  -0.0686 0.0321  85  ARG B CG  
1680 C CD  . ARG B 52  ? 0.2974 0.2555 0.3761 0.0254  -0.0863 0.0418  85  ARG B CD  
1681 N NE  . ARG B 52  ? 0.2769 0.2570 0.3610 0.0261  -0.0800 0.0401  85  ARG B NE  
1682 C CZ  . ARG B 52  ? 0.2908 0.2952 0.4086 0.0357  -0.0741 0.0343  85  ARG B CZ  
1683 N NH1 . ARG B 52  ? 0.2544 0.2653 0.4052 0.0461  -0.0710 0.0282  85  ARG B NH1 
1684 N NH2 . ARG B 52  ? 0.2832 0.3037 0.4008 0.0341  -0.0689 0.0338  85  ARG B NH2 
1685 N N   . SER B 53  ? 0.2571 0.2055 0.2775 -0.0052 -0.0372 0.0263  86  SER B N   
1686 C CA  . SER B 53  ? 0.2723 0.1957 0.2747 -0.0175 -0.0344 0.0294  86  SER B CA  
1687 C C   . SER B 53  ? 0.2824 0.2117 0.3027 -0.0162 -0.0290 0.0211  86  SER B C   
1688 O O   . SER B 53  ? 0.3009 0.2083 0.3137 -0.0225 -0.0313 0.0238  86  SER B O   
1689 C CB  . SER B 53  ? 0.2862 0.2019 0.2653 -0.0327 -0.0205 0.0307  86  SER B CB  
1690 O OG  . SER B 53  ? 0.6318 0.5256 0.5970 -0.0466 -0.0111 0.0314  86  SER B OG  
1691 N N   . GLN B 54  ? 0.2440 0.1982 0.2846 -0.0095 -0.0238 0.0114  87  GLN B N   
1692 C CA  . GLN B 54  ? 0.2334 0.1899 0.2888 -0.0086 -0.0229 0.0030  87  GLN B CA  
1693 C C   . GLN B 54  ? 0.2327 0.1899 0.2958 0.0051  -0.0304 -0.0018 87  GLN B C   
1694 O O   . GLN B 54  ? 0.2791 0.2372 0.3490 0.0075  -0.0313 -0.0102 87  GLN B O   
1695 C CB  . GLN B 54  ? 0.2159 0.1916 0.2860 -0.0121 -0.0154 -0.0050 87  GLN B CB  
1696 C CG  . GLN B 54  ? 0.2376 0.2114 0.3063 -0.0266 -0.0024 -0.0034 87  GLN B CG  
1697 C CD  . GLN B 54  ? 0.2275 0.2207 0.3239 -0.0297 0.0039  -0.0132 87  GLN B CD  
1698 O OE1 . GLN B 54  ? 0.2058 0.2039 0.3232 -0.0272 -0.0033 -0.0204 87  GLN B OE1 
1699 N NE2 . GLN B 54  ? 0.2046 0.2063 0.3021 -0.0350 0.0155  -0.0139 87  GLN B NE2 
1700 N N   . HIS B 55  ? 0.2328 0.1872 0.2959 0.0136  -0.0357 0.0026  88  HIS B N   
1701 C CA  . HIS B 55  ? 0.2465 0.1989 0.3205 0.0262  -0.0381 -0.0031 88  HIS B CA  
1702 C C   . HIS B 55  ? 0.2744 0.2401 0.3490 0.0318  -0.0308 -0.0130 88  HIS B C   
1703 O O   . HIS B 55  ? 0.2842 0.2405 0.3568 0.0369  -0.0294 -0.0215 88  HIS B O   
1704 C CB  . HIS B 55  ? 0.3067 0.2374 0.3811 0.0261  -0.0433 -0.0052 88  HIS B CB  
1705 C CG  . HIS B 55  ? 0.4013 0.3121 0.4661 0.0165  -0.0505 0.0051  88  HIS B CG  
1706 N ND1 . HIS B 55  ? 0.4549 0.3569 0.5094 0.0027  -0.0469 0.0066  88  HIS B ND1 
1707 C CD2 . HIS B 55  ? 0.4123 0.3065 0.4745 0.0173  -0.0616 0.0146  88  HIS B CD2 
1708 C CE1 . HIS B 55  ? 0.4753 0.3534 0.5143 -0.0058 -0.0525 0.0168  88  HIS B CE1 
1709 N NE2 . HIS B 55  ? 0.4975 0.3684 0.5384 0.0031  -0.0641 0.0224  88  HIS B NE2 
1710 N N   . ILE B 56  ? 0.2164 0.1989 0.2886 0.0298  -0.0269 -0.0118 89  ILE B N   
1711 C CA  . ILE B 56  ? 0.2293 0.2204 0.2964 0.0340  -0.0218 -0.0188 89  ILE B CA  
1712 C C   . ILE B 56  ? 0.2438 0.2465 0.3180 0.0399  -0.0168 -0.0160 89  ILE B C   
1713 O O   . ILE B 56  ? 0.2223 0.2319 0.3036 0.0380  -0.0203 -0.0078 89  ILE B O   
1714 C CB  . ILE B 56  ? 0.2515 0.2518 0.3147 0.0270  -0.0232 -0.0199 89  ILE B CB  
1715 C CG1 . ILE B 56  ? 0.2417 0.2351 0.3103 0.0190  -0.0277 -0.0218 89  ILE B CG1 
1716 C CG2 . ILE B 56  ? 0.2533 0.2529 0.3044 0.0306  -0.0227 -0.0266 89  ILE B CG2 
1717 C CD1 . ILE B 56  ? 0.2475 0.2533 0.3257 0.0123  -0.0281 -0.0236 89  ILE B CD1 
1718 N N   . ASP B 57  ? 0.1941 0.1960 0.2642 0.0456  -0.0084 -0.0230 90  ASP B N   
1719 C CA  . ASP B 57  ? 0.2255 0.2399 0.3072 0.0499  -0.0007 -0.0215 90  ASP B CA  
1720 C C   . ASP B 57  ? 0.2090 0.2382 0.2869 0.0445  -0.0041 -0.0151 90  ASP B C   
1721 O O   . ASP B 57  ? 0.2129 0.2419 0.2741 0.0404  -0.0048 -0.0175 90  ASP B O   
1722 C CB  . ASP B 57  ? 0.2745 0.2805 0.3442 0.0535  0.0138  -0.0313 90  ASP B CB  
1723 C CG  . ASP B 57  ? 0.3450 0.3648 0.4287 0.0556  0.0251  -0.0304 90  ASP B CG  
1724 O OD1 . ASP B 57  ? 0.4734 0.5052 0.5905 0.0598  0.0239  -0.0264 90  ASP B OD1 
1725 O OD2 . ASP B 57  ? 0.4426 0.4586 0.5045 0.0525  0.0334  -0.0335 90  ASP B OD2 
1726 N N   . PRO B 58  ? 0.2388 0.2155 0.2399 0.0051  -0.0228 -0.0207 91  PRO B N   
1727 C CA  . PRO B 58  ? 0.2408 0.2223 0.2450 0.0032  -0.0203 -0.0191 91  PRO B CA  
1728 C C   . PRO B 58  ? 0.2346 0.2231 0.2433 0.0030  -0.0172 -0.0197 91  PRO B C   
1729 O O   . PRO B 58  ? 0.1713 0.1629 0.1817 0.0006  -0.0154 -0.0181 91  PRO B O   
1730 C CB  . PRO B 58  ? 0.2208 0.2009 0.2244 0.0055  -0.0220 -0.0200 91  PRO B CB  
1731 C CG  . PRO B 58  ? 0.2180 0.1908 0.2167 0.0073  -0.0253 -0.0208 91  PRO B CG  
1732 C CD  . PRO B 58  ? 0.2587 0.2318 0.2579 0.0079  -0.0254 -0.0222 91  PRO B CD  
1733 N N   . ASP B 59  ? 0.1780 0.1689 0.1889 0.0058  -0.0160 -0.0217 92  ASP B N   
1734 C CA  . ASP B 59  ? 0.2480 0.2449 0.2635 0.0060  -0.0120 -0.0215 92  ASP B CA  
1735 C C   . ASP B 59  ? 0.2301 0.2254 0.2410 0.0047  -0.0108 -0.0206 92  ASP B C   
1736 O O   . ASP B 59  ? 0.2347 0.2340 0.2480 0.0032  -0.0083 -0.0196 92  ASP B O   
1737 C CB  . ASP B 59  ? 0.2920 0.2911 0.3117 0.0101  -0.0095 -0.0229 92  ASP B CB  
1738 C CG  . ASP B 59  ? 0.4047 0.4067 0.4328 0.0113  -0.0114 -0.0241 92  ASP B CG  
1739 O OD1 . ASP B 59  ? 0.4164 0.4203 0.4480 0.0094  -0.0134 -0.0237 92  ASP B OD1 
1740 O OD2 . ASP B 59  ? 0.4499 0.4512 0.4804 0.0147  -0.0116 -0.0255 92  ASP B OD2 
1741 N N   . TYR B 60  ? 0.2231 0.2117 0.2275 0.0055  -0.0137 -0.0213 93  TYR B N   
1742 C CA  . TYR B 60  ? 0.2063 0.1915 0.2067 0.0044  -0.0150 -0.0210 93  TYR B CA  
1743 C C   . TYR B 60  ? 0.1970 0.1850 0.2020 -0.0003 -0.0154 -0.0188 93  TYR B C   
1744 O O   . TYR B 60  ? 0.1994 0.1896 0.2051 -0.0015 -0.0142 -0.0182 93  TYR B O   
1745 C CB  . TYR B 60  ? 0.1995 0.1755 0.1937 0.0058  -0.0202 -0.0223 93  TYR B CB  
1746 C CG  . TYR B 60  ? 0.2500 0.2209 0.2415 0.0048  -0.0241 -0.0225 93  TYR B CG  
1747 C CD1 . TYR B 60  ? 0.2256 0.1909 0.2084 0.0089  -0.0246 -0.0243 93  TYR B CD1 
1748 C CD2 . TYR B 60  ? 0.1923 0.1629 0.1903 0.0002  -0.0274 -0.0206 93  TYR B CD2 
1749 C CE1 . TYR B 60  ? 0.2526 0.2115 0.2324 0.0085  -0.0301 -0.0251 93  TYR B CE1 
1750 C CE2 . TYR B 60  ? 0.2101 0.1760 0.2086 -0.0009 -0.0321 -0.0210 93  TYR B CE2 
1751 C CZ  . TYR B 60  ? 0.2738 0.2336 0.2630 0.0033  -0.0343 -0.0236 93  TYR B CZ  
1752 O OH  . TYR B 60  ? 0.2213 0.1750 0.2107 0.0029  -0.0408 -0.0246 93  TYR B OH  
1753 N N   . VAL B 61  ? 0.1799 0.1673 0.1873 -0.0023 -0.0166 -0.0173 94  VAL B N   
1754 C CA  . VAL B 61  ? 0.1784 0.1677 0.1899 -0.0058 -0.0158 -0.0145 94  VAL B CA  
1755 C C   . VAL B 61  ? 0.1859 0.1815 0.1996 -0.0063 -0.0122 -0.0140 94  VAL B C   
1756 O O   . VAL B 61  ? 0.1613 0.1595 0.1776 -0.0083 -0.0110 -0.0126 94  VAL B O   
1757 C CB  . VAL B 61  ? 0.1776 0.1630 0.1893 -0.0068 -0.0164 -0.0124 94  VAL B CB  
1758 C CG1 . VAL B 61  ? 0.1864 0.1740 0.2013 -0.0091 -0.0131 -0.0089 94  VAL B CG1 
1759 C CG2 . VAL B 61  ? 0.1803 0.1593 0.1925 -0.0076 -0.0204 -0.0122 94  VAL B CG2 
1760 N N   . THR B 62  ? 0.1629 0.1610 0.1768 -0.0043 -0.0112 -0.0151 95  THR B N   
1761 C CA  . THR B 62  ? 0.1609 0.1641 0.1778 -0.0047 -0.0092 -0.0147 95  THR B CA  
1762 C C   . THR B 62  ? 0.1795 0.1865 0.1983 -0.0050 -0.0070 -0.0152 95  THR B C   
1763 O O   . THR B 62  ? 0.1682 0.1784 0.1889 -0.0065 -0.0056 -0.0142 95  THR B O   
1764 C CB  . THR B 62  ? 0.1580 0.1621 0.1768 -0.0024 -0.0103 -0.0162 95  THR B CB  
1765 O OG1 . THR B 62  ? 0.1996 0.2046 0.2212 -0.0002 -0.0102 -0.0181 95  THR B OG1 
1766 C CG2 . THR B 62  ? 0.1757 0.1740 0.1896 -0.0014 -0.0125 -0.0155 95  THR B CG2 
1767 N N   . ARG B 63  ? 0.2050 0.2105 0.2219 -0.0031 -0.0064 -0.0164 96  ARG B N   
1768 C CA  . ARG B 63  ? 0.2018 0.2085 0.2176 -0.0026 -0.0039 -0.0164 96  ARG B CA  
1769 C C   . ARG B 63  ? 0.1884 0.1930 0.2018 -0.0048 -0.0058 -0.0157 96  ARG B C   
1770 O O   . ARG B 63  ? 0.1923 0.1995 0.2067 -0.0059 -0.0043 -0.0150 96  ARG B O   
1771 C CB  . ARG B 63  ? 0.1659 0.1691 0.1772 0.0014  -0.0022 -0.0175 96  ARG B CB  
1772 C CG  . ARG B 63  ? 0.2813 0.2830 0.2881 0.0030  0.0009  -0.0171 96  ARG B CG  
1773 C CD  . ARG B 63  ? 0.3485 0.3446 0.3477 0.0084  0.0038  -0.0178 96  ARG B CD  
1774 N NE  . ARG B 63  ? 0.4140 0.4149 0.4206 0.0106  0.0091  -0.0171 96  ARG B NE  
1775 C CZ  . ARG B 63  ? 0.4234 0.4287 0.4360 0.0114  0.0154  -0.0152 96  ARG B CZ  
1776 N NH1 . ARG B 63  ? 0.3400 0.3455 0.3507 0.0102  0.0172  -0.0139 96  ARG B NH1 
1777 N NH2 . ARG B 63  ? 0.4063 0.4159 0.4286 0.0135  0.0198  -0.0143 96  ARG B NH2 
1778 N N   . VAL B 64  ? 0.1757 0.1753 0.1872 -0.0055 -0.0096 -0.0158 97  VAL B N   
1779 C CA  . VAL B 64  ? 0.1898 0.1873 0.2026 -0.0076 -0.0125 -0.0152 97  VAL B CA  
1780 C C   . VAL B 64  ? 0.1747 0.1776 0.1937 -0.0107 -0.0105 -0.0128 97  VAL B C   
1781 O O   . VAL B 64  ? 0.1547 0.1591 0.1754 -0.0119 -0.0106 -0.0124 97  VAL B O   
1782 C CB  . VAL B 64  ? 0.1797 0.1709 0.1927 -0.0080 -0.0174 -0.0155 97  VAL B CB  
1783 C CG1 . VAL B 64  ? 0.2163 0.2073 0.2369 -0.0114 -0.0201 -0.0137 97  VAL B CG1 
1784 C CG2 . VAL B 64  ? 0.2008 0.1844 0.2052 -0.0041 -0.0208 -0.0183 97  VAL B CG2 
1785 N N   . PHE B 65  ? 0.1542 0.1589 0.1751 -0.0113 -0.0088 -0.0114 98  PHE B N   
1786 C CA  . PHE B 65  ? 0.1523 0.1603 0.1765 -0.0129 -0.0064 -0.0090 98  PHE B CA  
1787 C C   . PHE B 65  ? 0.1499 0.1622 0.1734 -0.0122 -0.0043 -0.0097 98  PHE B C   
1788 O O   . PHE B 65  ? 0.1439 0.1587 0.1693 -0.0133 -0.0029 -0.0084 98  PHE B O   
1789 C CB  . PHE B 65  ? 0.1532 0.1590 0.1768 -0.0126 -0.0050 -0.0069 98  PHE B CB  
1790 C CG  . PHE B 65  ? 0.1811 0.1834 0.2090 -0.0144 -0.0056 -0.0045 98  PHE B CG  
1791 C CD1 . PHE B 65  ? 0.1734 0.1772 0.2077 -0.0162 -0.0031 -0.0011 98  PHE B CD1 
1792 C CD2 . PHE B 65  ? 0.1914 0.1892 0.2187 -0.0142 -0.0089 -0.0054 98  PHE B CD2 
1793 C CE1 . PHE B 65  ? 0.1770 0.1782 0.2193 -0.0182 -0.0035 0.0017  98  PHE B CE1 
1794 C CE2 . PHE B 65  ? 0.1963 0.1906 0.2298 -0.0163 -0.0101 -0.0030 98  PHE B CE2 
1795 C CZ  . PHE B 65  ? 0.1710 0.1673 0.2133 -0.0185 -0.0073 0.0008  98  PHE B CZ  
1796 N N   . ASP B 66  ? 0.1458 0.1593 0.1680 -0.0105 -0.0039 -0.0115 99  ASP B N   
1797 C CA  . ASP B 66  ? 0.1515 0.1688 0.1753 -0.0104 -0.0022 -0.0118 99  ASP B CA  
1798 C C   . ASP B 66  ? 0.1854 0.2031 0.2084 -0.0112 -0.0017 -0.0117 99  ASP B C   
1799 O O   . ASP B 66  ? 0.1807 0.2010 0.2052 -0.0122 -0.0008 -0.0111 99  ASP B O   
1800 C CB  . ASP B 66  ? 0.1795 0.1984 0.2057 -0.0085 -0.0014 -0.0131 99  ASP B CB  
1801 C CG  . ASP B 66  ? 0.2188 0.2416 0.2495 -0.0087 -0.0001 -0.0129 99  ASP B CG  
1802 O OD1 . ASP B 66  ? 0.2436 0.2669 0.2751 -0.0091 -0.0016 -0.0126 99  ASP B OD1 
1803 O OD2 . ASP B 66  ? 0.2727 0.2969 0.3056 -0.0081 0.0026  -0.0128 99  ASP B OD2 
1804 N N   . ASP B 67  ? 0.1602 0.1739 0.1797 -0.0103 -0.0030 -0.0127 100 ASP B N   
1805 C CA  . ASP B 67  ? 0.1649 0.1765 0.1818 -0.0103 -0.0040 -0.0130 100 ASP B CA  
1806 C C   . ASP B 67  ? 0.1890 0.2019 0.2105 -0.0129 -0.0060 -0.0119 100 ASP B C   
1807 O O   . ASP B 67  ? 0.1709 0.1852 0.1930 -0.0135 -0.0058 -0.0117 100 ASP B O   
1808 C CB  . ASP B 67  ? 0.1573 0.1616 0.1675 -0.0078 -0.0067 -0.0147 100 ASP B CB  
1809 C CG  . ASP B 67  ? 0.2671 0.2694 0.2723 -0.0043 -0.0035 -0.0154 100 ASP B CG  
1810 O OD1 . ASP B 67  ? 0.2989 0.3059 0.3071 -0.0039 0.0011  -0.0144 100 ASP B OD1 
1811 O OD2 . ASP B 67  ? 0.2173 0.2132 0.2164 -0.0016 -0.0057 -0.0167 100 ASP B OD2 
1812 N N   . GLN B 68  ? 0.1465 0.1587 0.1720 -0.0142 -0.0074 -0.0108 101 GLN B N   
1813 C CA  . GLN B 68  ? 0.1447 0.1586 0.1774 -0.0165 -0.0078 -0.0088 101 GLN B CA  
1814 C C   . GLN B 68  ? 0.1890 0.2078 0.2230 -0.0168 -0.0040 -0.0072 101 GLN B C   
1815 O O   . GLN B 68  ? 0.1450 0.1658 0.1829 -0.0177 -0.0039 -0.0064 101 GLN B O   
1816 C CB  . GLN B 68  ? 0.1511 0.1631 0.1885 -0.0175 -0.0082 -0.0069 101 GLN B CB  
1817 C CG  . GLN B 68  ? 0.1458 0.1600 0.1931 -0.0196 -0.0066 -0.0035 101 GLN B CG  
1818 C CD  . GLN B 68  ? 0.1803 0.1927 0.2362 -0.0212 -0.0117 -0.0040 101 GLN B CD  
1819 O OE1 . GLN B 68  ? 0.1788 0.1860 0.2321 -0.0205 -0.0173 -0.0066 101 GLN B OE1 
1820 N NE2 . GLN B 68  ? 0.1626 0.1786 0.2289 -0.0227 -0.0103 -0.0016 101 GLN B NE2 
1821 N N   . ILE B 69  ? 0.1390 0.1587 0.1694 -0.0155 -0.0017 -0.0071 102 ILE B N   
1822 C CA  . ILE B 69  ? 0.1636 0.1858 0.1934 -0.0149 0.0006  -0.0061 102 ILE B CA  
1823 C C   . ILE B 69  ? 0.1342 0.1588 0.1632 -0.0150 0.0003  -0.0074 102 ILE B C   
1824 O O   . ILE B 69  ? 0.1507 0.1770 0.1807 -0.0151 0.0012  -0.0066 102 ILE B O   
1825 C CB  . ILE B 69  ? 0.1581 0.1785 0.1837 -0.0129 0.0012  -0.0062 102 ILE B CB  
1826 C CG1 . ILE B 69  ? 0.1984 0.2153 0.2234 -0.0125 0.0024  -0.0040 102 ILE B CG1 
1827 C CG2 . ILE B 69  ? 0.1424 0.1635 0.1655 -0.0114 0.0018  -0.0061 102 ILE B CG2 
1828 C CD1 . ILE B 69  ? 0.2025 0.2152 0.2213 -0.0098 0.0020  -0.0043 102 ILE B CD1 
1829 N N   . ARG B 70  ? 0.1345 0.1585 0.1615 -0.0145 -0.0003 -0.0092 103 ARG B N   
1830 C CA  . ARG B 70  ? 0.1738 0.1988 0.1999 -0.0144 0.0003  -0.0097 103 ARG B CA  
1831 C C   . ARG B 70  ? 0.1664 0.1907 0.1927 -0.0152 -0.0011 -0.0096 103 ARG B C   
1832 O O   . ARG B 70  ? 0.1523 0.1781 0.1788 -0.0155 -0.0008 -0.0094 103 ARG B O   
1833 C CB  . ARG B 70  ? 0.1479 0.1712 0.1715 -0.0130 0.0014  -0.0107 103 ARG B CB  
1834 C CG  . ARG B 70  ? 0.2644 0.2897 0.2913 -0.0122 0.0031  -0.0108 103 ARG B CG  
1835 C CD  . ARG B 70  ? 0.2362 0.2601 0.2622 -0.0104 0.0062  -0.0107 103 ARG B CD  
1836 N NE  . ARG B 70  ? 0.1943 0.2136 0.2145 -0.0085 0.0063  -0.0114 103 ARG B NE  
1837 C CZ  . ARG B 70  ? 0.2509 0.2647 0.2632 -0.0065 0.0067  -0.0117 103 ARG B CZ  
1838 N NH1 . ARG B 70  ? 0.2179 0.2303 0.2271 -0.0066 0.0073  -0.0112 103 ARG B NH1 
1839 N NH2 . ARG B 70  ? 0.2514 0.2596 0.2572 -0.0038 0.0061  -0.0127 103 ARG B NH2 
1840 N N   . ALA B 71  ? 0.1485 0.1698 0.1754 -0.0155 -0.0037 -0.0100 104 ALA B N   
1841 C CA  . ALA B 71  ? 0.1715 0.1913 0.2006 -0.0161 -0.0067 -0.0104 104 ALA B CA  
1842 C C   . ALA B 71  ? 0.1684 0.1926 0.2049 -0.0175 -0.0055 -0.0084 104 ALA B C   
1843 O O   . ALA B 71  ? 0.1425 0.1677 0.1808 -0.0176 -0.0065 -0.0086 104 ALA B O   
1844 C CB  . ALA B 71  ? 0.1664 0.1810 0.1961 -0.0158 -0.0112 -0.0115 104 ALA B CB  
1845 N N   . THR B 72  ? 0.1338 0.1599 0.1740 -0.0179 -0.0030 -0.0064 105 THR B N   
1846 C CA  . THR B 72  ? 0.1323 0.1616 0.1778 -0.0181 0.0001  -0.0037 105 THR B CA  
1847 C C   . THR B 72  ? 0.1409 0.1720 0.1816 -0.0168 0.0018  -0.0041 105 THR B C   
1848 O O   . THR B 72  ? 0.1297 0.1629 0.1738 -0.0166 0.0025  -0.0033 105 THR B O   
1849 C CB  . THR B 72  ? 0.1342 0.1626 0.1801 -0.0175 0.0035  -0.0013 105 THR B CB  
1850 O OG1 . THR B 72  ? 0.1520 0.1780 0.2019 -0.0188 0.0012  -0.0012 105 THR B OG1 
1851 C CG2 . THR B 72  ? 0.1415 0.1716 0.1922 -0.0167 0.0081  0.0023  105 THR B CG2 
1852 N N   . GLU B 73  ? 0.1591 0.1893 0.1933 -0.0157 0.0021  -0.0053 106 GLU B N   
1853 C CA  . GLU B 73  ? 0.1478 0.1788 0.1785 -0.0146 0.0025  -0.0059 106 GLU B CA  
1854 C C   . GLU B 73  ? 0.1564 0.1881 0.1875 -0.0154 0.0009  -0.0070 106 GLU B C   
1855 O O   . GLU B 73  ? 0.1338 0.1665 0.1642 -0.0148 0.0010  -0.0069 106 GLU B O   
1856 C CB  . GLU B 73  ? 0.1509 0.1807 0.1782 -0.0136 0.0018  -0.0071 106 GLU B CB  
1857 C CG  . GLU B 73  ? 0.1939 0.2214 0.2187 -0.0119 0.0025  -0.0063 106 GLU B CG  
1858 C CD  . GLU B 73  ? 0.2442 0.2702 0.2679 -0.0110 0.0004  -0.0079 106 GLU B CD  
1859 O OE1 . GLU B 73  ? 0.2019 0.2295 0.2286 -0.0123 0.0000  -0.0090 106 GLU B OE1 
1860 O OE2 . GLU B 73  ? 0.2404 0.2630 0.2601 -0.0085 -0.0007 -0.0081 106 GLU B OE2 
1861 N N   . ALA B 74  ? 0.1398 0.1695 0.1700 -0.0161 -0.0009 -0.0082 107 ALA B N   
1862 C CA  . ALA B 74  ? 0.1311 0.1592 0.1591 -0.0160 -0.0026 -0.0093 107 ALA B CA  
1863 C C   . ALA B 74  ? 0.1308 0.1601 0.1635 -0.0164 -0.0042 -0.0090 107 ALA B C   
1864 O O   . ALA B 74  ? 0.1416 0.1709 0.1729 -0.0159 -0.0050 -0.0094 107 ALA B O   
1865 C CB  . ALA B 74  ? 0.1361 0.1592 0.1596 -0.0153 -0.0043 -0.0106 107 ALA B CB  
1866 N N   . ILE B 75  ? 0.1305 0.1611 0.1704 -0.0171 -0.0047 -0.0079 108 ILE B N   
1867 C CA  . ILE B 75  ? 0.1377 0.1706 0.1860 -0.0173 -0.0055 -0.0070 108 ILE B CA  
1868 C C   . ILE B 75  ? 0.1345 0.1708 0.1824 -0.0161 -0.0015 -0.0054 108 ILE B C   
1869 O O   . ILE B 75  ? 0.1469 0.1844 0.1969 -0.0155 -0.0023 -0.0056 108 ILE B O   
1870 C CB  . ILE B 75  ? 0.1343 0.1683 0.1936 -0.0185 -0.0058 -0.0053 108 ILE B CB  
1871 C CG1 . ILE B 75  ? 0.1618 0.1907 0.2210 -0.0191 -0.0119 -0.0076 108 ILE B CG1 
1872 C CG2 . ILE B 75  ? 0.1545 0.1924 0.2261 -0.0187 -0.0049 -0.0033 108 ILE B CG2 
1873 C CD1 . ILE B 75  ? 0.1694 0.1981 0.2385 -0.0206 -0.0127 -0.0060 108 ILE B CD1 
1874 N N   . GLU B 76  ? 0.1280 0.1645 0.1720 -0.0151 0.0022  -0.0040 109 GLU B N   
1875 C CA  . GLU B 76  ? 0.1291 0.1663 0.1700 -0.0126 0.0052  -0.0028 109 GLU B CA  
1876 C C   . GLU B 76  ? 0.1811 0.2174 0.2162 -0.0121 0.0029  -0.0049 109 GLU B C   
1877 O O   . GLU B 76  ? 0.1296 0.1667 0.1646 -0.0105 0.0035  -0.0046 109 GLU B O   
1878 C CB  . GLU B 76  ? 0.1321 0.1669 0.1670 -0.0107 0.0079  -0.0017 109 GLU B CB  
1879 C CG  . GLU B 76  ? 0.1459 0.1806 0.1856 -0.0109 0.0111  0.0010  109 GLU B CG  
1880 C CD  . GLU B 76  ? 0.2083 0.2387 0.2396 -0.0083 0.0130  0.0018  109 GLU B CD  
1881 O OE1 . GLU B 76  ? 0.2203 0.2475 0.2431 -0.0049 0.0134  0.0014  109 GLU B OE1 
1882 O OE2 . GLU B 76  ? 0.3020 0.3312 0.3346 -0.0094 0.0132  0.0024  109 GLU B OE2 
1883 N N   . TYR B 77  ? 0.1279 0.1624 0.1589 -0.0133 0.0007  -0.0067 110 TYR B N   
1884 C CA  . TYR B 77  ? 0.1398 0.1731 0.1670 -0.0131 -0.0010 -0.0080 110 TYR B CA  
1885 C C   . TYR B 77  ? 0.1508 0.1841 0.1794 -0.0135 -0.0029 -0.0086 110 TYR B C   
1886 O O   . TYR B 77  ? 0.1294 0.1621 0.1558 -0.0126 -0.0037 -0.0090 110 TYR B O   
1887 C CB  . TYR B 77  ? 0.1281 0.1597 0.1531 -0.0142 -0.0015 -0.0088 110 TYR B CB  
1888 C CG  . TYR B 77  ? 0.1731 0.2044 0.1976 -0.0134 -0.0014 -0.0088 110 TYR B CG  
1889 C CD1 . TYR B 77  ? 0.1519 0.1819 0.1756 -0.0126 -0.0032 -0.0093 110 TYR B CD1 
1890 C CD2 . TYR B 77  ? 0.1782 0.2094 0.2032 -0.0131 -0.0007 -0.0085 110 TYR B CD2 
1891 C CE1 . TYR B 77  ? 0.1939 0.2223 0.2181 -0.0115 -0.0050 -0.0099 110 TYR B CE1 
1892 C CE2 . TYR B 77  ? 0.2096 0.2393 0.2339 -0.0118 -0.0019 -0.0090 110 TYR B CE2 
1893 C CZ  . TYR B 77  ? 0.1927 0.2209 0.2169 -0.0109 -0.0046 -0.0098 110 TYR B CZ  
1894 O OH  . TYR B 77  ? 0.1612 0.1867 0.1857 -0.0092 -0.0076 -0.0109 110 TYR B OH  
1895 N N   . SER B 78  ? 0.1292 0.1619 0.1609 -0.0144 -0.0046 -0.0091 111 SER B N   
1896 C CA  . SER B 78  ? 0.1313 0.1625 0.1643 -0.0142 -0.0078 -0.0102 111 SER B CA  
1897 C C   . SER B 78  ? 0.1339 0.1689 0.1736 -0.0132 -0.0070 -0.0092 111 SER B C   
1898 O O   . SER B 78  ? 0.1365 0.1709 0.1751 -0.0123 -0.0089 -0.0101 111 SER B O   
1899 C CB  . SER B 78  ? 0.1486 0.1768 0.1840 -0.0147 -0.0115 -0.0113 111 SER B CB  
1900 O OG  . SER B 78  ? 0.1924 0.2174 0.2283 -0.0139 -0.0162 -0.0129 111 SER B OG  
1901 N N   . ARG B 79  ? 0.1283 0.1669 0.1749 -0.0130 -0.0037 -0.0070 112 ARG B N   
1902 C CA  . ARG B 79  ? 0.1315 0.1735 0.1845 -0.0111 -0.0010 -0.0052 112 ARG B CA  
1903 C C   . ARG B 79  ? 0.1300 0.1708 0.1740 -0.0087 0.0004  -0.0055 112 ARG B C   
1904 O O   . ARG B 79  ? 0.1312 0.1729 0.1768 -0.0069 0.0004  -0.0055 112 ARG B O   
1905 C CB  . ARG B 79  ? 0.1312 0.1758 0.1913 -0.0105 0.0043  -0.0018 112 ARG B CB  
1906 C CG  . ARG B 79  ? 0.1811 0.2270 0.2531 -0.0130 0.0027  -0.0011 112 ARG B CG  
1907 C CD  . ARG B 79  ? 0.1979 0.2448 0.2809 -0.0141 -0.0027 -0.0025 112 ARG B CD  
1908 N NE  . ARG B 79  ? 0.1566 0.2044 0.2537 -0.0161 -0.0046 -0.0014 112 ARG B NE  
1909 C CZ  . ARG B 79  ? 0.2226 0.2677 0.3259 -0.0174 -0.0126 -0.0040 112 ARG B CZ  
1910 N NH1 . ARG B 79  ? 0.2125 0.2528 0.3063 -0.0167 -0.0188 -0.0079 112 ARG B NH1 
1911 N NH2 . ARG B 79  ? 0.1988 0.2447 0.3177 -0.0192 -0.0149 -0.0027 112 ARG B NH2 
1912 N N   . PHE B 80  ? 0.1308 0.1690 0.1662 -0.0082 0.0011  -0.0058 113 PHE B N   
1913 C CA  . PHE B 80  ? 0.1337 0.1693 0.1610 -0.0057 0.0007  -0.0065 113 PHE B CA  
1914 C C   . PHE B 80  ? 0.1743 0.2085 0.1996 -0.0066 -0.0031 -0.0084 113 PHE B C   
1915 O O   . PHE B 80  ? 0.1400 0.1729 0.1619 -0.0043 -0.0039 -0.0088 113 PHE B O   
1916 C CB  . PHE B 80  ? 0.1352 0.1676 0.1560 -0.0053 0.0002  -0.0069 113 PHE B CB  
1917 C CG  . PHE B 80  ? 0.1699 0.2002 0.1868 -0.0017 0.0037  -0.0052 113 PHE B CG  
1918 C CD1 . PHE B 80  ? 0.1560 0.1886 0.1781 -0.0012 0.0084  -0.0025 113 PHE B CD1 
1919 C CD2 . PHE B 80  ? 0.1460 0.1707 0.1539 0.0015  0.0017  -0.0062 113 PHE B CD2 
1920 C CE1 . PHE B 80  ? 0.1475 0.1766 0.1642 0.0028  0.0128  -0.0003 113 PHE B CE1 
1921 C CE2 . PHE B 80  ? 0.1537 0.1739 0.1546 0.0059  0.0046  -0.0047 113 PHE B CE2 
1922 C CZ  . PHE B 80  ? 0.1547 0.1770 0.1592 0.0068  0.0109  -0.0015 113 PHE B CZ  
1923 N N   . SER B 81  ? 0.1393 0.1725 0.1651 -0.0093 -0.0055 -0.0095 114 SER B N   
1924 C CA  . SER B 81  ? 0.1462 0.1767 0.1687 -0.0097 -0.0085 -0.0109 114 SER B CA  
1925 C C   . SER B 81  ? 0.1525 0.1843 0.1791 -0.0083 -0.0100 -0.0113 114 SER B C   
1926 O O   . SER B 81  ? 0.1445 0.1748 0.1679 -0.0068 -0.0115 -0.0120 114 SER B O   
1927 C CB  . SER B 81  ? 0.1787 0.2059 0.1987 -0.0115 -0.0097 -0.0115 114 SER B CB  
1928 O OG  . SER B 81  ? 0.1426 0.1655 0.1580 -0.0111 -0.0122 -0.0125 114 SER B OG  
1929 N N   . ASP B 82  ? 0.1334 0.1681 0.1684 -0.0087 -0.0099 -0.0108 115 ASP B N   
1930 C CA  . ASP B 82  ? 0.1400 0.1769 0.1829 -0.0073 -0.0114 -0.0110 115 ASP B CA  
1931 C C   . ASP B 82  ? 0.1411 0.1806 0.1843 -0.0042 -0.0077 -0.0096 115 ASP B C   
1932 O O   . ASP B 82  ? 0.1519 0.1914 0.1961 -0.0024 -0.0094 -0.0104 115 ASP B O   
1933 C CB  . ASP B 82  ? 0.1362 0.1766 0.1923 -0.0084 -0.0116 -0.0101 115 ASP B CB  
1934 C CG  . ASP B 82  ? 0.2049 0.2407 0.2599 -0.0102 -0.0171 -0.0122 115 ASP B CG  
1935 O OD1 . ASP B 82  ? 0.1984 0.2281 0.2426 -0.0100 -0.0206 -0.0143 115 ASP B OD1 
1936 O OD2 . ASP B 82  ? 0.2122 0.2496 0.2767 -0.0114 -0.0178 -0.0115 115 ASP B OD2 
1937 N N   . TRP B 83  ? 0.1385 0.1791 0.1799 -0.0029 -0.0028 -0.0076 116 TRP B N   
1938 C CA  . TRP B 83  ? 0.1473 0.1883 0.1869 0.0015  0.0014  -0.0059 116 TRP B CA  
1939 C C   . TRP B 83  ? 0.1529 0.1889 0.1801 0.0036  -0.0012 -0.0077 116 TRP B C   
1940 O O   . TRP B 83  ? 0.1591 0.1940 0.1833 0.0078  0.0002  -0.0074 116 TRP B O   
1941 C CB  . TRP B 83  ? 0.1513 0.1929 0.1911 0.0034  0.0077  -0.0029 116 TRP B CB  
1942 C CG  . TRP B 83  ? 0.1592 0.2058 0.2136 0.0012  0.0105  -0.0005 116 TRP B CG  
1943 C CD1 . TRP B 83  ? 0.1586 0.2094 0.2276 -0.0006 0.0084  -0.0005 116 TRP B CD1 
1944 C CD2 . TRP B 83  ? 0.1430 0.1897 0.1994 0.0006  0.0146  0.0020  116 TRP B CD2 
1945 N NE1 . TRP B 83  ? 0.1638 0.2177 0.2453 -0.0025 0.0109  0.0020  116 TRP B NE1 
1946 C CE2 . TRP B 83  ? 0.1583 0.2099 0.2319 -0.0019 0.0152  0.0037  116 TRP B CE2 
1947 C CE3 . TRP B 83  ? 0.1555 0.1982 0.2013 0.0021  0.0171  0.0028  116 TRP B CE3 
1948 C CZ2 . TRP B 83  ? 0.1734 0.2260 0.2537 -0.0033 0.0188  0.0066  116 TRP B CZ2 
1949 C CZ3 . TRP B 83  ? 0.1417 0.1852 0.1927 0.0011  0.0210  0.0056  116 TRP B CZ3 
1950 C CH2 . TRP B 83  ? 0.1629 0.2114 0.2311 -0.0017 0.0221  0.0076  116 TRP B CH2 
1951 N N   . LYS B 84  ? 0.1460 0.1786 0.1669 0.0010  -0.0049 -0.0094 117 LYS B N   
1952 C CA  . LYS B 84  ? 0.1648 0.1926 0.1774 0.0021  -0.0086 -0.0111 117 LYS B CA  
1953 C C   . LYS B 84  ? 0.1781 0.2056 0.1919 0.0021  -0.0115 -0.0124 117 LYS B C   
1954 O O   . LYS B 84  ? 0.1993 0.2239 0.2080 0.0049  -0.0133 -0.0132 117 LYS B O   
1955 C CB  . LYS B 84  ? 0.1434 0.1684 0.1531 -0.0011 -0.0111 -0.0119 117 LYS B CB  
1956 C CG  . LYS B 84  ? 0.1628 0.1862 0.1698 -0.0001 -0.0102 -0.0115 117 LYS B CG  
1957 C CD  . LYS B 84  ? 0.2030 0.2206 0.2021 0.0042  -0.0131 -0.0125 117 LYS B CD  
1958 C CE  . LYS B 84  ? 0.1839 0.1976 0.1793 0.0057  -0.0143 -0.0128 117 LYS B CE  
1959 N NZ  . LYS B 84  ? 0.2226 0.2284 0.2098 0.0101  -0.0196 -0.0145 117 LYS B NZ  
1960 N N   . LEU B 85  ? 0.1424 0.1717 0.1618 -0.0006 -0.0129 -0.0128 118 LEU B N   
1961 C CA  . LEU B 85  ? 0.1826 0.2104 0.2025 -0.0001 -0.0165 -0.0143 118 LEU B CA  
1962 C C   . LEU B 85  ? 0.2148 0.2464 0.2411 0.0035  -0.0149 -0.0138 118 LEU B C   
1963 O O   . LEU B 85  ? 0.1621 0.1917 0.1859 0.0056  -0.0174 -0.0150 118 LEU B O   
1964 C CB  . LEU B 85  ? 0.1595 0.1860 0.1819 -0.0026 -0.0195 -0.0153 118 LEU B CB  
1965 C CG  . LEU B 85  ? 0.1886 0.2101 0.2033 -0.0051 -0.0200 -0.0154 118 LEU B CG  
1966 C CD1 . LEU B 85  ? 0.2291 0.2475 0.2436 -0.0063 -0.0223 -0.0162 118 LEU B CD1 
1967 C CD2 . LEU B 85  ? 0.1784 0.1943 0.1849 -0.0049 -0.0218 -0.0158 118 LEU B CD2 
1968 N N   . ASN B 86  ? 0.1617 0.1983 0.1964 0.0045  -0.0100 -0.0116 119 ASN B N   
1969 C CA  . ASN B 86  ? 0.1939 0.2348 0.2375 0.0082  -0.0067 -0.0101 119 ASN B CA  
1970 C C   . ASN B 86  ? 0.2327 0.2761 0.2783 0.0109  0.0012  -0.0066 119 ASN B C   
1971 O O   . ASN B 86  ? 0.1831 0.2311 0.2406 0.0093  0.0046  -0.0044 119 ASN B O   
1972 C CB  . ASN B 86  ? 0.1868 0.2317 0.2454 0.0065  -0.0097 -0.0107 119 ASN B CB  
1973 C CG  . ASN B 86  ? 0.3174 0.3679 0.3895 0.0101  -0.0057 -0.0087 119 ASN B CG  
1974 O OD1 . ASN B 86  ? 0.3205 0.3709 0.3877 0.0147  -0.0004 -0.0071 119 ASN B OD1 
1975 N ND2 . ASN B 86  ? 0.3544 0.4090 0.4440 0.0086  -0.0085 -0.0088 119 ASN B ND2 
1976 N N   . PRO B 87  ? 0.2112 0.2502 0.2446 0.0154  0.0040  -0.0061 120 PRO B N   
1977 C CA  . PRO B 87  ? 0.1576 0.1962 0.1888 0.0190  0.0117  -0.0027 120 PRO B CA  
1978 C C   . PRO B 87  ? 0.2341 0.2784 0.2793 0.0218  0.0196  0.0013  120 PRO B C   
1979 O O   . PRO B 87  ? 0.2353 0.2807 0.2838 0.0228  0.0264  0.0050  120 PRO B O   
1980 C CB  . PRO B 87  ? 0.2133 0.2435 0.2265 0.0246  0.0110  -0.0038 120 PRO B CB  
1981 C CG  . PRO B 87  ? 0.2306 0.2575 0.2381 0.0209  0.0020  -0.0078 120 PRO B CG  
1982 C CD  . PRO B 87  ? 0.2356 0.2679 0.2549 0.0171  -0.0008 -0.0087 120 PRO B CD  
1983 N N   . ALA B 88  ? 0.1933 0.2415 0.2482 0.0232  0.0191  0.0011  121 ALA B N   
1984 C CA  . ALA B 88  ? 0.2050 0.2597 0.2774 0.0258  0.0271  0.0055  121 ALA B CA  
1985 C C   . ALA B 88  ? 0.2012 0.2623 0.2932 0.0201  0.0271  0.0071  121 ALA B C   
1986 O O   . ALA B 88  ? 0.2353 0.3017 0.3438 0.0215  0.0349  0.0119  121 ALA B O   
1987 C CB  . ALA B 88  ? 0.2539 0.3115 0.3343 0.0284  0.0255  0.0044  121 ALA B CB  
1988 N N   . SER B 89  ? 0.1584 0.2185 0.2492 0.0141  0.0186  0.0037  122 SER B N   
1989 C CA  . SER B 89  ? 0.2106 0.2751 0.3184 0.0093  0.0172  0.0047  122 SER B CA  
1990 C C   . SER B 89  ? 0.1945 0.2578 0.2987 0.0083  0.0226  0.0076  122 SER B C   
1991 O O   . SER B 89  ? 0.1837 0.2503 0.3026 0.0048  0.0223  0.0091  122 SER B O   
1992 C CB  . SER B 89  ? 0.2197 0.2819 0.3266 0.0045  0.0058  -0.0003 122 SER B CB  
1993 O OG  . SER B 89  ? 0.2268 0.2831 0.3149 0.0028  0.0027  -0.0027 122 SER B OG  
1994 N N   . ALA B 90  ? 0.1816 0.2394 0.2672 0.0116  0.0266  0.0082  123 ALA B N   
1995 C CA  . ALA B 90  ? 0.1678 0.2236 0.2492 0.0113  0.0314  0.0109  123 ALA B CA  
1996 C C   . ALA B 90  ? 0.2071 0.2668 0.3033 0.0138  0.0419  0.0172  123 ALA B C   
1997 O O   . ALA B 90  ? 0.2721 0.3316 0.3680 0.0197  0.0492  0.0202  123 ALA B O   
1998 C CB  . ALA B 90  ? 0.2510 0.2985 0.3091 0.0152  0.0322  0.0099  123 ALA B CB  
1999 N N   . PRO B 91  ? 0.2524 0.3149 0.3618 0.0100  0.0433  0.0196  124 PRO B N   
2000 C CA  . PRO B 91  ? 0.2972 0.3644 0.4263 0.0115  0.0532  0.0262  124 PRO B CA  
2001 C C   . PRO B 91  ? 0.2501 0.3115 0.3656 0.0177  0.0650  0.0313  124 PRO B C   
2002 O O   . PRO B 91  ? 0.2357 0.2891 0.3279 0.0196  0.0633  0.0291  124 PRO B O   
2003 C CB  . PRO B 91  ? 0.2297 0.3004 0.3759 0.0048  0.0482  0.0261  124 PRO B CB  
2004 C CG  . PRO B 91  ? 0.2902 0.3561 0.4193 0.0011  0.0379  0.0199  124 PRO B CG  
2005 C CD  . PRO B 91  ? 0.2867 0.3471 0.3919 0.0050  0.0373  0.0171  124 PRO B CD  
2006 N N   . PRO B 92  ? 0.2909 0.3550 0.4203 0.0213  0.0770  0.0384  125 PRO B N   
2007 C CA  . PRO B 92  ? 0.3124 0.3686 0.4265 0.0282  0.0891  0.0439  125 PRO B CA  
2008 C C   . PRO B 92  ? 0.2936 0.3454 0.4009 0.0250  0.0877  0.0441  125 PRO B C   
2009 O O   . PRO B 92  ? 0.2551 0.3124 0.3798 0.0178  0.0827  0.0436  125 PRO B O   
2010 C CB  . PRO B 92  ? 0.3417 0.4035 0.4788 0.0315  0.1028  0.0522  125 PRO B CB  
2011 C CG  . PRO B 92  ? 0.4413 0.5148 0.6108 0.0238  0.0957  0.0510  125 PRO B CG  
2012 C CD  . PRO B 92  ? 0.2800 0.3538 0.4404 0.0198  0.0803  0.0419  125 PRO B CD  
2013 N N   . GLU B 93  ? 0.2601 0.3010 0.3411 0.0308  0.0910  0.0444  126 GLU B N   
2014 C CA  . GLU B 93  ? 0.2982 0.3331 0.3678 0.0288  0.0884  0.0435  126 GLU B CA  
2015 C C   . GLU B 93  ? 0.2193 0.2510 0.2940 0.0319  0.1015  0.0518  126 GLU B C   
2016 O O   . GLU B 93  ? 0.2540 0.2853 0.3339 0.0378  0.1141  0.0584  126 GLU B O   
2017 C CB  . GLU B 93  ? 0.2987 0.3223 0.3375 0.0338  0.0832  0.0388  126 GLU B CB  
2018 C CG  . GLU B 93  ? 0.3150 0.3262 0.3320 0.0451  0.0935  0.0430  126 GLU B CG  
2019 C CD  . GLU B 93  ? 0.3631 0.3740 0.3776 0.0515  0.0983  0.0441  126 GLU B CD  
2020 O OE1 . GLU B 93  ? 0.3497 0.3714 0.3828 0.0469  0.0948  0.0424  126 GLU B OE1 
2021 O OE2 . GLU B 93  ? 0.4227 0.4212 0.4150 0.0619  0.1052  0.0465  126 GLU B OE2 
2022 N N   . PRO B 94  ? 0.2504 0.2798 0.3246 0.0281  0.0995  0.0521  127 PRO B N   
2023 C CA  . PRO B 94  ? 0.2835 0.3074 0.3585 0.0316  0.1120  0.0601  127 PRO B CA  
2024 C C   . PRO B 94  ? 0.3115 0.3204 0.3554 0.0427  0.1198  0.0623  127 PRO B C   
2025 O O   . PRO B 94  ? 0.3619 0.3640 0.3827 0.0463  0.1121  0.0562  127 PRO B O   
2026 C CB  . PRO B 94  ? 0.2492 0.2729 0.3264 0.0249  0.1045  0.0577  127 PRO B CB  
2027 C CG  . PRO B 94  ? 0.2556 0.2795 0.3203 0.0215  0.0896  0.0482  127 PRO B CG  
2028 C CD  . PRO B 94  ? 0.2370 0.2683 0.3102 0.0207  0.0861  0.0454  127 PRO B CD  
2029 N N   . PRO B 95  ? 0.3093 0.3117 0.3514 0.0490  0.1351  0.0711  128 PRO B N   
2030 C CA  . PRO B 95  ? 0.3300 0.3147 0.3382 0.0613  0.1424  0.0732  128 PRO B CA  
2031 C C   . PRO B 95  ? 0.3815 0.3544 0.3632 0.0624  0.1321  0.0673  128 PRO B C   
2032 O O   . PRO B 95  ? 0.3752 0.3337 0.3267 0.0716  0.1304  0.0647  128 PRO B O   
2033 C CB  . PRO B 95  ? 0.3295 0.3102 0.3452 0.0663  0.1614  0.0848  128 PRO B CB  
2034 C CG  . PRO B 95  ? 0.3178 0.3116 0.3674 0.0549  0.1598  0.0871  128 PRO B CG  
2035 C CD  . PRO B 95  ? 0.3430 0.3520 0.4131 0.0455  0.1457  0.0797  128 PRO B CD  
2036 N N   . ASP B 96  ? 0.3389 0.3169 0.3314 0.0538  0.1247  0.0650  129 ASP B N   
2037 C CA  . ASP B 96  ? 0.3497 0.3187 0.3219 0.0536  0.1140  0.0590  129 ASP B CA  
2038 C C   . ASP B 96  ? 0.3950 0.3757 0.3883 0.0418  0.1047  0.0556  129 ASP B C   
2039 O O   . ASP B 96  ? 0.3504 0.3444 0.3712 0.0346  0.1052  0.0572  129 ASP B O   
2040 C CB  . ASP B 96  ? 0.4134 0.3649 0.3624 0.0626  0.1227  0.0641  129 ASP B CB  
2041 C CG  . ASP B 96  ? 0.5034 0.4574 0.4700 0.0611  0.1366  0.0738  129 ASP B CG  
2042 O OD1 . ASP B 96  ? 0.4708 0.4356 0.4607 0.0512  0.1325  0.0735  129 ASP B OD1 
2043 O OD2 . ASP B 96  ? 0.5183 0.4629 0.4758 0.0702  0.1519  0.0818  129 ASP B OD2 
2044 N N   . LEU B 97  ? 0.3196 0.2945 0.3000 0.0405  0.0956  0.0507  130 LEU B N   
2045 C CA  . LEU B 97  ? 0.3104 0.2944 0.3068 0.0307  0.0866  0.0471  130 LEU B CA  
2046 C C   . LEU B 97  ? 0.3375 0.3173 0.3372 0.0294  0.0912  0.0516  130 LEU B C   
2047 O O   . LEU B 97  ? 0.3150 0.2991 0.3226 0.0228  0.0832  0.0482  130 LEU B O   
2048 C CB  . LEU B 97  ? 0.3485 0.3313 0.3329 0.0290  0.0726  0.0382  130 LEU B CB  
2049 C CG  . LEU B 97  ? 0.3366 0.3251 0.3220 0.0283  0.0665  0.0334  130 LEU B CG  
2050 C CD1 . LEU B 97  ? 0.3280 0.3150 0.3039 0.0266  0.0538  0.0256  130 LEU B CD1 
2051 C CD2 . LEU B 97  ? 0.3296 0.3323 0.3404 0.0211  0.0666  0.0340  130 LEU B CD2 
2052 N N   . SER B 98  ? 0.4619 0.3735 0.3517 0.0472  0.0804  -0.0399 131 SER B N   
2053 C CA  . SER B 98  ? 0.4177 0.3373 0.2984 0.0458  0.0790  -0.0314 131 SER B CA  
2054 C C   . SER B 98  ? 0.3932 0.3319 0.3018 0.0396  0.0834  -0.0173 131 SER B C   
2055 O O   . SER B 98  ? 0.4003 0.3447 0.3135 0.0331  0.0755  -0.0126 131 SER B O   
2056 C CB  . SER B 98  ? 0.4773 0.3873 0.3264 0.0562  0.0906  -0.0304 131 SER B CB  
2057 O OG  . SER B 98  ? 0.5657 0.4821 0.4247 0.0613  0.1086  -0.0235 131 SER B OG  
2058 N N   . ALA B 99  ? 0.3906 0.3401 0.3181 0.0424  0.0952  -0.0117 132 ALA B N   
2059 C CA  . ALA B 99  ? 0.3199 0.2910 0.2763 0.0363  0.0971  -0.0013 132 ALA B CA  
2060 C C   . ALA B 99  ? 0.3492 0.3249 0.3228 0.0292  0.0832  -0.0018 132 ALA B C   
2061 O O   . ALA B 99  ? 0.3510 0.3373 0.3362 0.0219  0.0783  0.0039  132 ALA B O   
2062 C CB  . ALA B 99  ? 0.3435 0.3296 0.3189 0.0432  0.1098  0.0023  132 ALA B CB  
2063 N N   . SER B 100 ? 0.2909 0.2566 0.2655 0.0310  0.0782  -0.0086 133 SER B N   
2064 C CA  . SER B 100 ? 0.2620 0.2299 0.2508 0.0248  0.0678  -0.0086 133 SER B CA  
2065 C C   . SER B 100 ? 0.3410 0.3067 0.3218 0.0176  0.0563  -0.0115 133 SER B C   
2066 O O   . SER B 100 ? 0.2541 0.2287 0.2471 0.0123  0.0495  -0.0072 133 SER B O   
2067 C CB  . SER B 100 ? 0.3410 0.2935 0.3303 0.0274  0.0686  -0.0152 133 SER B CB  
2068 O OG  . SER B 100 ? 0.3551 0.3079 0.3504 0.0372  0.0791  -0.0115 133 SER B OG  
2069 N N   A ARG B 101 ? 0.3330 0.2870 0.2918 0.0192  0.0531  -0.0195 134 ARG B N   
2070 N N   B ARG B 101 ? 0.3323 0.2862 0.2910 0.0192  0.0531  -0.0195 134 ARG B N   
2071 C CA  A ARG B 101 ? 0.3603 0.3146 0.3097 0.0158  0.0410  -0.0224 134 ARG B CA  
2072 C CA  B ARG B 101 ? 0.3606 0.3149 0.3102 0.0158  0.0410  -0.0224 134 ARG B CA  
2073 C C   A ARG B 101 ? 0.3341 0.2949 0.2819 0.0147  0.0427  -0.0113 134 ARG B C   
2074 C C   B ARG B 101 ? 0.3335 0.2946 0.2820 0.0146  0.0429  -0.0112 134 ARG B C   
2075 O O   A ARG B 101 ? 0.3229 0.2881 0.2759 0.0110  0.0339  -0.0096 134 ARG B O   
2076 O O   B ARG B 101 ? 0.3231 0.2879 0.2752 0.0111  0.0337  -0.0098 134 ARG B O   
2077 C CB  A ARG B 101 ? 0.3894 0.3322 0.3122 0.0208  0.0358  -0.0336 134 ARG B CB  
2078 C CB  B ARG B 101 ? 0.3891 0.3319 0.3125 0.0207  0.0357  -0.0340 134 ARG B CB  
2079 C CG  A ARG B 101 ? 0.4384 0.3787 0.3665 0.0166  0.0249  -0.0484 134 ARG B CG  
2080 C CG  B ARG B 101 ? 0.4256 0.3603 0.3527 0.0185  0.0321  -0.0482 134 ARG B CG  
2081 C CD  A ARG B 101 ? 0.4390 0.3680 0.3733 0.0159  0.0327  -0.0550 134 ARG B CD  
2082 C CD  B ARG B 101 ? 0.4758 0.4033 0.3795 0.0222  0.0222  -0.0633 134 ARG B CD  
2083 N NE  A ARG B 101 ? 0.5145 0.4298 0.4290 0.0191  0.0298  -0.0710 134 ARG B NE  
2084 N NE  B ARG B 101 ? 0.5439 0.4642 0.4568 0.0163  0.0182  -0.0791 134 ARG B NE  
2085 C CZ  A ARG B 101 ? 0.5145 0.4219 0.3996 0.0289  0.0325  -0.0735 134 ARG B CZ  
2086 C CZ  B ARG B 101 ? 0.5328 0.4363 0.4339 0.0196  0.0246  -0.0884 134 ARG B CZ  
2087 N NH1 A ARG B 101 ? 0.4497 0.3612 0.3233 0.0352  0.0400  -0.0600 134 ARG B NH1 
2088 N NH1 B ARG B 101 ? 0.5361 0.4313 0.4158 0.0301  0.0355  -0.0830 134 ARG B NH1 
2089 N NH2 A ARG B 101 ? 0.5369 0.4312 0.4036 0.0319  0.0284  -0.0903 134 ARG B NH2 
2090 N NH2 B ARG B 101 ? 0.5071 0.4012 0.4184 0.0119  0.0215  -0.1035 134 ARG B NH2 
2091 N N   . SER B 102 ? 0.3565 0.3164 0.2967 0.0178  0.0550  -0.0047 135 SER B N   
2092 C CA  . SER B 102 ? 0.3692 0.3316 0.3089 0.0144  0.0591  0.0052  135 SER B CA  
2093 C C   . SER B 102 ? 0.3320 0.3092 0.3005 0.0067  0.0562  0.0099  135 SER B C   
2094 O O   . SER B 102 ? 0.3248 0.3011 0.2939 0.0022  0.0512  0.0136  135 SER B O   
2095 C CB  A SER B 102 ? 0.3760 0.3366 0.3074 0.0172  0.0761  0.0112  135 SER B CB  
2096 C CB  B SER B 102 ? 0.3760 0.3366 0.3075 0.0172  0.0762  0.0112  135 SER B CB  
2097 O OG  A SER B 102 ? 0.4114 0.3844 0.3627 0.0185  0.0844  0.0107  135 SER B OG  
2098 O OG  B SER B 102 ? 0.4235 0.3682 0.3224 0.0264  0.0793  0.0071  135 SER B OG  
2099 N N   . ALA B 103 ? 0.2722 0.2615 0.2618 0.0069  0.0590  0.0094  136 ALA B N   
2100 C CA  . ALA B 103 ? 0.2665 0.2702 0.2799 0.0023  0.0542  0.0124  136 ALA B CA  
2101 C C   . ALA B 103 ? 0.2555 0.2549 0.2679 -0.0001 0.0417  0.0098  136 ALA B C   
2102 O O   . ALA B 103 ? 0.2363 0.2407 0.2559 -0.0045 0.0366  0.0127  136 ALA B O   
2103 C CB  . ALA B 103 ? 0.3057 0.3203 0.3356 0.0076  0.0581  0.0122  136 ALA B CB  
2104 N N   . ILE B 104 ? 0.2276 0.2184 0.2323 0.0024  0.0372  0.0032  137 ILE B N   
2105 C CA  . ILE B 104 ? 0.2170 0.2073 0.2248 -0.0003 0.0272  0.0000  137 ILE B CA  
2106 C C   . ILE B 104 ? 0.2455 0.2327 0.2410 -0.0010 0.0207  0.0009  137 ILE B C   
2107 O O   . ILE B 104 ? 0.2640 0.2551 0.2658 -0.0030 0.0146  0.0027  137 ILE B O   
2108 C CB  . ILE B 104 ? 0.2698 0.2530 0.2758 0.0002  0.0251  -0.0091 137 ILE B CB  
2109 C CG1 . ILE B 104 ? 0.2734 0.2548 0.2916 0.0015  0.0321  -0.0080 137 ILE B CG1 
2110 C CG2 . ILE B 104 ? 0.2554 0.2417 0.2651 -0.0031 0.0151  -0.0141 137 ILE B CG2 
2111 C CD1 . ILE B 104 ? 0.3279 0.2962 0.3425 0.0010  0.0341  -0.0177 137 ILE B CD1 
2112 N N   . ASP B 105 ? 0.2559 0.2339 0.2307 0.0025  0.0225  0.0002  138 ASP B N   
2113 C CA  . ASP B 105 ? 0.3005 0.2715 0.2589 0.0049  0.0173  0.0027  138 ASP B CA  
2114 C C   . ASP B 105 ? 0.2718 0.2425 0.2371 0.0000  0.0212  0.0113  138 ASP B C   
2115 O O   . ASP B 105 ? 0.2689 0.2369 0.2324 0.0002  0.0145  0.0125  138 ASP B O   
2116 C CB  . ASP B 105 ? 0.3494 0.3073 0.2791 0.0119  0.0209  0.0024  138 ASP B CB  
2117 C CG  . ASP B 105 ? 0.4173 0.3644 0.3245 0.0182  0.0153  0.0054  138 ASP B CG  
2118 O OD1 . ASP B 105 ? 0.4934 0.4454 0.3992 0.0225  0.0022  -0.0010 138 ASP B OD1 
2119 O OD2 . ASP B 105 ? 0.5346 0.4679 0.4259 0.0193  0.0249  0.0145  138 ASP B OD2 
2120 N N   A SER B 106 ? 0.2492 0.2238 0.2242 -0.0044 0.0319  0.0159  139 SER B N   
2121 N N   B SER B 106 ? 0.2494 0.2240 0.2244 -0.0044 0.0318  0.0159  139 SER B N   
2122 C CA  A SER B 106 ? 0.2536 0.2297 0.2389 -0.0115 0.0351  0.0212  139 SER B CA  
2123 C CA  B SER B 106 ? 0.2537 0.2298 0.2390 -0.0115 0.0352  0.0212  139 SER B CA  
2124 C C   A SER B 106 ? 0.2247 0.2118 0.2281 -0.0142 0.0260  0.0190  139 SER B C   
2125 C C   B SER B 106 ? 0.2247 0.2118 0.2281 -0.0142 0.0261  0.0190  139 SER B C   
2126 O O   A SER B 106 ? 0.2123 0.1941 0.2147 -0.0171 0.0221  0.0203  139 SER B O   
2127 O O   B SER B 106 ? 0.2125 0.1943 0.2150 -0.0172 0.0223  0.0203  139 SER B O   
2128 C CB  A SER B 106 ? 0.2822 0.2675 0.2810 -0.0164 0.0478  0.0243  139 SER B CB  
2129 C CB  B SER B 106 ? 0.2822 0.2673 0.2807 -0.0163 0.0480  0.0243  139 SER B CB  
2130 O OG  A SER B 106 ? 0.3044 0.2763 0.2837 -0.0146 0.0593  0.0284  139 SER B OG  
2131 O OG  B SER B 106 ? 0.2371 0.2250 0.2485 -0.0256 0.0512  0.0271  139 SER B OG  
2132 N N   . LEU B 107 ? 0.1854 0.1846 0.2023 -0.0121 0.0235  0.0160  140 LEU B N   
2133 C CA  . LEU B 107 ? 0.1621 0.1703 0.1921 -0.0125 0.0166  0.0150  140 LEU B CA  
2134 C C   . LEU B 107 ? 0.2223 0.2241 0.2443 -0.0100 0.0085  0.0128  140 LEU B C   
2135 O O   . LEU B 107 ? 0.1928 0.1964 0.2184 -0.0105 0.0037  0.0131  140 LEU B O   
2136 C CB  . LEU B 107 ? 0.1584 0.1765 0.2004 -0.0087 0.0187  0.0142  140 LEU B CB  
2137 C CG  . LEU B 107 ? 0.2104 0.2412 0.2649 -0.0088 0.0251  0.0162  140 LEU B CG  
2138 C CD1 . LEU B 107 ? 0.1861 0.2212 0.2461 -0.0014 0.0292  0.0161  140 LEU B CD1 
2139 C CD2 . LEU B 107 ? 0.2137 0.2575 0.2816 -0.0125 0.0206  0.0164  140 LEU B CD2 
2140 N N   . ASN B 108 ? 0.1915 0.1878 0.2032 -0.0067 0.0065  0.0094  141 ASN B N   
2141 C CA  . ASN B 108 ? 0.1991 0.1939 0.2054 -0.0034 -0.0015 0.0064  141 ASN B CA  
2142 C C   . ASN B 108 ? 0.2262 0.2116 0.2213 -0.0023 -0.0038 0.0100  141 ASN B C   
2143 O O   . ASN B 108 ? 0.2096 0.1963 0.2074 -0.0006 -0.0087 0.0097  141 ASN B O   
2144 C CB  . ASN B 108 ? 0.1963 0.1888 0.1918 0.0006  -0.0049 0.0004  141 ASN B CB  
2145 C CG  . ASN B 108 ? 0.2504 0.2495 0.2579 -0.0016 -0.0042 -0.0063 141 ASN B CG  
2146 O OD1 . ASN B 108 ? 0.2175 0.2213 0.2404 -0.0047 -0.0005 -0.0051 141 ASN B OD1 
2147 N ND2 . ASN B 108 ? 0.2281 0.2254 0.2265 0.0007  -0.0075 -0.0140 141 ASN B ND2 
2148 N N   . ASN B 109 ? 0.2051 0.1779 0.1854 -0.0025 0.0012  0.0138  142 ASN B N   
2149 C CA  . ASN B 109 ? 0.2547 0.2114 0.2208 -0.0014 0.0013  0.0180  142 ASN B CA  
2150 C C   . ASN B 109 ? 0.2342 0.1922 0.2136 -0.0088 0.0023  0.0189  142 ASN B C   
2151 O O   . ASN B 109 ? 0.2467 0.1947 0.2196 -0.0070 -0.0014 0.0191  142 ASN B O   
2152 C CB  . ASN B 109 ? 0.2677 0.2072 0.2140 -0.0009 0.0102  0.0233  142 ASN B CB  
2153 C CG  . ASN B 109 ? 0.3608 0.2949 0.2851 0.0102  0.0062  0.0216  142 ASN B CG  
2154 O OD1 . ASN B 109 ? 0.4085 0.3483 0.3302 0.0179  -0.0047 0.0169  142 ASN B OD1 
2155 N ND2 . ASN B 109 ? 0.4442 0.3696 0.3532 0.0117  0.0147  0.0245  142 ASN B ND2 
2156 N N   . ARG B 110 ? 0.1909 0.1618 0.1882 -0.0158 0.0066  0.0185  143 ARG B N   
2157 C CA  . ARG B 110 ? 0.1992 0.1762 0.2103 -0.0219 0.0047  0.0167  143 ARG B CA  
2158 C C   . ARG B 110 ? 0.1966 0.1793 0.2101 -0.0165 -0.0040 0.0137  143 ARG B C   
2159 O O   . ARG B 110 ? 0.1961 0.1722 0.2068 -0.0174 -0.0078 0.0118  143 ARG B O   
2160 C CB  . ARG B 110 ? 0.2043 0.2000 0.2353 -0.0268 0.0088  0.0159  143 ARG B CB  
2161 C CG  . ARG B 110 ? 0.3678 0.3697 0.4129 -0.0357 0.0085  0.0129  143 ARG B CG  
2162 C CD  . ARG B 110 ? 0.3559 0.3838 0.4230 -0.0360 0.0079  0.0104  143 ARG B CD  
2163 N NE  . ARG B 110 ? 0.4267 0.4625 0.5019 -0.0380 0.0181  0.0130  143 ARG B NE  
2164 C CZ  . ARG B 110 ? 0.4913 0.5497 0.5840 -0.0348 0.0192  0.0119  143 ARG B CZ  
2165 N NH1 . ARG B 110 ? 0.4212 0.4955 0.5231 -0.0286 0.0103  0.0090  143 ARG B NH1 
2166 N NH2 . ARG B 110 ? 0.3749 0.4391 0.4734 -0.0355 0.0301  0.0143  143 ARG B NH2 
2167 N N   . MET B 111 ? 0.1712 0.1642 0.1891 -0.0112 -0.0059 0.0129  144 MET B N   
2168 C CA  . MET B 111 ? 0.1652 0.1641 0.1863 -0.0061 -0.0107 0.0112  144 MET B CA  
2169 C C   . MET B 111 ? 0.1760 0.1654 0.1855 -0.0009 -0.0149 0.0102  144 MET B C   
2170 O O   . MET B 111 ? 0.2091 0.1977 0.2170 0.0024  -0.0181 0.0089  144 MET B O   
2171 C CB  . MET B 111 ? 0.1443 0.1531 0.1739 -0.0036 -0.0084 0.0109  144 MET B CB  
2172 C CG  . MET B 111 ? 0.1543 0.1715 0.1936 -0.0044 -0.0045 0.0126  144 MET B CG  
2173 S SD  . MET B 111 ? 0.1747 0.1938 0.2202 -0.0022 0.0014  0.0127  144 MET B SD  
2174 C CE  . MET B 111 ? 0.1840 0.2046 0.2314 0.0016  0.0012  0.0132  144 MET B CE  
2175 N N   . LEU B 112 ? 0.1633 0.1459 0.1627 0.0020  -0.0153 0.0105  145 LEU B N   
2176 C CA  . LEU B 112 ? 0.1746 0.1495 0.1620 0.0102  -0.0201 0.0098  145 LEU B CA  
2177 C C   . LEU B 112 ? 0.1890 0.1450 0.1643 0.0099  -0.0199 0.0115  145 LEU B C   
2178 O O   . LEU B 112 ? 0.2007 0.1532 0.1716 0.0163  -0.0234 0.0099  145 LEU B O   
2179 C CB  . LEU B 112 ? 0.1926 0.1632 0.1674 0.0157  -0.0219 0.0097  145 LEU B CB  
2180 C CG  . LEU B 112 ? 0.1991 0.1879 0.1853 0.0170  -0.0248 0.0043  145 LEU B CG  
2181 C CD1 . LEU B 112 ? 0.2593 0.2432 0.2287 0.0240  -0.0287 0.0026  145 LEU B CD1 
2182 C CD2 . LEU B 112 ? 0.2489 0.2538 0.2497 0.0206  -0.0288 0.0000  145 LEU B CD2 
2183 N N   . SER B 113 ? 0.2004 0.1432 0.1708 0.0021  -0.0145 0.0142  146 SER B N   
2184 C CA  . SER B 113 ? 0.2206 0.1421 0.1811 -0.0009 -0.0130 0.0144  146 SER B CA  
2185 C C   . SER B 113 ? 0.2121 0.1415 0.1838 -0.0046 -0.0169 0.0091  146 SER B C   
2186 O O   . SER B 113 ? 0.2284 0.1418 0.1900 -0.0023 -0.0191 0.0065  146 SER B O   
2187 C CB  . SER B 113 ? 0.2365 0.1437 0.1937 -0.0112 -0.0038 0.0179  146 SER B CB  
2188 O OG  . SER B 113 ? 0.2894 0.1828 0.2272 -0.0042 0.0001  0.0236  146 SER B OG  
2189 N N   . GLN B 114 ? 0.1911 0.1428 0.1804 -0.0083 -0.0180 0.0072  147 GLN B N   
2190 C CA  . GLN B 114 ? 0.1901 0.1505 0.1854 -0.0076 -0.0230 0.0023  147 GLN B CA  
2191 C C   . GLN B 114 ? 0.2165 0.1772 0.2040 0.0039  -0.0263 0.0017  147 GLN B C   
2192 O O   . GLN B 114 ? 0.2191 0.1738 0.1998 0.0072  -0.0298 -0.0026 147 GLN B O   
2193 C CB  . GLN B 114 ? 0.1770 0.1600 0.1887 -0.0098 -0.0229 0.0022  147 GLN B CB  
2194 C CG  . GLN B 114 ? 0.2389 0.2280 0.2631 -0.0204 -0.0205 0.0008  147 GLN B CG  
2195 C CD  . GLN B 114 ? 0.2961 0.2784 0.3217 -0.0283 -0.0241 -0.0062 147 GLN B CD  
2196 O OE1 . GLN B 114 ? 0.2597 0.2432 0.2812 -0.0243 -0.0313 -0.0118 147 GLN B OE1 
2197 N NE2 . GLN B 114 ? 0.2843 0.2580 0.3150 -0.0400 -0.0181 -0.0066 147 GLN B NE2 
2198 N N   . ILE B 115 ? 0.1978 0.1675 0.1880 0.0100  -0.0248 0.0046  148 ILE B N   
2199 C CA  . ILE B 115 ? 0.1920 0.1671 0.1804 0.0202  -0.0260 0.0038  148 ILE B CA  
2200 C C   . ILE B 115 ? 0.2218 0.1789 0.1940 0.0276  -0.0285 0.0024  148 ILE B C   
2201 O O   . ILE B 115 ? 0.2030 0.1569 0.1688 0.0348  -0.0297 -0.0002 148 ILE B O   
2202 C CB  . ILE B 115 ? 0.1636 0.1546 0.1634 0.0224  -0.0239 0.0051  148 ILE B CB  
2203 C CG1 . ILE B 115 ? 0.1743 0.1785 0.1876 0.0175  -0.0196 0.0066  148 ILE B CG1 
2204 C CG2 . ILE B 115 ? 0.1629 0.1617 0.1644 0.0322  -0.0244 0.0034  148 ILE B CG2 
2205 C CD1 . ILE B 115 ? 0.1677 0.1823 0.1929 0.0150  -0.0168 0.0062  148 ILE B CD1 
2206 N N   . TRP B 116 ? 0.2079 0.1503 0.1699 0.0277  -0.0284 0.0046  149 TRP B N   
2207 C CA  . TRP B 116 ? 0.2471 0.1663 0.1896 0.0363  -0.0296 0.0045  149 TRP B CA  
2208 C C   . TRP B 116 ? 0.2507 0.1502 0.1848 0.0313  -0.0295 0.0006  149 TRP B C   
2209 O O   . TRP B 116 ? 0.2884 0.1788 0.2124 0.0403  -0.0313 -0.0027 149 TRP B O   
2210 C CB  . TRP B 116 ? 0.2510 0.1532 0.1795 0.0377  -0.0278 0.0093  149 TRP B CB  
2211 C CG  . TRP B 116 ? 0.2959 0.1659 0.2001 0.0462  -0.0269 0.0109  149 TRP B CG  
2212 C CD1 . TRP B 116 ? 0.3573 0.2225 0.2488 0.0640  -0.0305 0.0112  149 TRP B CD1 
2213 C CD2 . TRP B 116 ? 0.3126 0.1494 0.2029 0.0376  -0.0212 0.0120  149 TRP B CD2 
2214 N NE1 . TRP B 116 ? 0.4137 0.2408 0.2803 0.0688  -0.0271 0.0134  149 TRP B NE1 
2215 C CE2 . TRP B 116 ? 0.3699 0.1775 0.2357 0.0513  -0.0208 0.0137  149 TRP B CE2 
2216 C CE3 . TRP B 116 ? 0.3136 0.1436 0.2121 0.0193  -0.0158 0.0110  149 TRP B CE3 
2217 C CZ2 . TRP B 116 ? 0.4272 0.1937 0.2741 0.0461  -0.0138 0.0149  149 TRP B CZ2 
2218 C CZ3 . TRP B 116 ? 0.4004 0.1944 0.2846 0.0123  -0.0092 0.0111  149 TRP B CZ3 
2219 C CH2 . TRP B 116 ? 0.3840 0.1441 0.2415 0.0251  -0.0077 0.0132  149 TRP B CH2 
2220 N N   . SER B 117 ? 0.2543 0.1492 0.1941 0.0169  -0.0275 -0.0006 150 SER B N   
2221 C CA  . SER B 117 ? 0.2724 0.1476 0.2056 0.0101  -0.0283 -0.0069 150 SER B CA  
2222 C C   . SER B 117 ? 0.2719 0.1595 0.2080 0.0139  -0.0340 -0.0139 150 SER B C   
2223 O O   . SER B 117 ? 0.2898 0.1587 0.2142 0.0141  -0.0365 -0.0211 150 SER B O   
2224 C CB  . SER B 117 ? 0.3015 0.1741 0.2457 -0.0075 -0.0245 -0.0080 150 SER B CB  
2225 O OG  . SER B 117 ? 0.3310 0.2341 0.2963 -0.0133 -0.0270 -0.0097 150 SER B OG  
2226 N N   . HIS B 118 ? 0.2414 0.1566 0.1896 0.0181  -0.0351 -0.0120 151 HIS B N   
2227 C CA  . HIS B 118 ? 0.2886 0.2146 0.2351 0.0242  -0.0389 -0.0169 151 HIS B CA  
2228 C C   . HIS B 118 ? 0.2547 0.1862 0.1952 0.0394  -0.0362 -0.0141 151 HIS B C   
2229 O O   . HIS B 118 ? 0.2501 0.1933 0.1897 0.0457  -0.0359 -0.0149 151 HIS B O   
2230 C CB  . HIS B 118 ? 0.2209 0.1705 0.1825 0.0192  -0.0402 -0.0161 151 HIS B CB  
2231 C CG  . HIS B 118 ? 0.2370 0.1877 0.2083 0.0057  -0.0434 -0.0210 151 HIS B CG  
2232 N ND1 . HIS B 118 ? 0.2878 0.2395 0.2575 0.0025  -0.0510 -0.0310 151 HIS B ND1 
2233 C CD2 . HIS B 118 ? 0.2197 0.1730 0.2038 -0.0054 -0.0399 -0.0181 151 HIS B CD2 
2234 C CE1 . HIS B 118 ? 0.2582 0.2158 0.2436 -0.0112 -0.0521 -0.0347 151 HIS B CE1 
2235 N NE2 . HIS B 118 ? 0.2236 0.1818 0.2176 -0.0160 -0.0442 -0.0261 151 HIS B NE2 
2236 N N   . TRP B 119 ? 0.2587 0.1823 0.1945 0.0461  -0.0341 -0.0109 152 TRP B N   
2237 C CA  . TRP B 119 ? 0.2585 0.1950 0.1960 0.0596  -0.0311 -0.0090 152 TRP B CA  
2238 C C   . TRP B 119 ? 0.3154 0.2456 0.2391 0.0700  -0.0307 -0.0137 152 TRP B C   
2239 O O   . TRP B 119 ? 0.2865 0.2339 0.2152 0.0780  -0.0258 -0.0120 152 TRP B O   
2240 C CB  . TRP B 119 ? 0.2791 0.2096 0.2127 0.0680  -0.0313 -0.0066 152 TRP B CB  
2241 C CG  . TRP B 119 ? 0.3151 0.2687 0.2597 0.0798  -0.0284 -0.0058 152 TRP B CG  
2242 C CD1 . TRP B 119 ? 0.3623 0.3149 0.2994 0.0952  -0.0268 -0.0080 152 TRP B CD1 
2243 C CD2 . TRP B 119 ? 0.3283 0.3111 0.2964 0.0763  -0.0254 -0.0037 152 TRP B CD2 
2244 N NE1 . TRP B 119 ? 0.2870 0.2701 0.2446 0.1008  -0.0226 -0.0071 152 TRP B NE1 
2245 C CE2 . TRP B 119 ? 0.3237 0.3246 0.3009 0.0883  -0.0218 -0.0049 152 TRP B CE2 
2246 C CE3 . TRP B 119 ? 0.2851 0.2797 0.2681 0.0640  -0.0247 -0.0015 152 TRP B CE3 
2247 C CZ2 . TRP B 119 ? 0.3119 0.3427 0.3153 0.0858  -0.0173 -0.0048 152 TRP B CZ2 
2248 C CZ3 . TRP B 119 ? 0.2435 0.2636 0.2487 0.0626  -0.0208 -0.0015 152 TRP B CZ3 
2249 C CH2 . TRP B 119 ? 0.2728 0.3111 0.2893 0.0722  -0.0170 -0.0034 152 TRP B CH2 
2250 N N   . SER B 120 ? 0.3227 0.2265 0.2280 0.0698  -0.0347 -0.0202 153 SER B N   
2251 C CA  . SER B 120 ? 0.3436 0.2382 0.2314 0.0806  -0.0351 -0.0266 153 SER B CA  
2252 C C   . SER B 120 ? 0.3799 0.2918 0.2699 0.0799  -0.0355 -0.0278 153 SER B C   
2253 O O   . SER B 120 ? 0.3751 0.2916 0.2548 0.0927  -0.0317 -0.0285 153 SER B O   
2254 C CB  . SER B 120 ? 0.3692 0.2296 0.2374 0.0773  -0.0399 -0.0355 153 SER B CB  
2255 O OG  . SER B 120 ? 0.5238 0.3622 0.3810 0.0854  -0.0374 -0.0335 153 SER B OG  
2256 N N   . LEU B 121 ? 0.3063 0.2267 0.2070 0.0670  -0.0396 -0.0280 154 LEU B N   
2257 C CA  . LEU B 121 ? 0.3087 0.2452 0.2090 0.0692  -0.0406 -0.0279 154 LEU B CA  
2258 C C   . LEU B 121 ? 0.2968 0.2543 0.2098 0.0740  -0.0307 -0.0172 154 LEU B C   
2259 O O   . LEU B 121 ? 0.3085 0.2724 0.2124 0.0845  -0.0255 -0.0148 154 LEU B O   
2260 C CB  . LEU B 121 ? 0.3576 0.2994 0.2675 0.0556  -0.0485 -0.0320 154 LEU B CB  
2261 C CG  . LEU B 121 ? 0.3342 0.2950 0.2451 0.0593  -0.0508 -0.0305 154 LEU B CG  
2262 C CD1 . LEU B 121 ? 0.3999 0.3569 0.2860 0.0748  -0.0524 -0.0350 154 LEU B CD1 
2263 C CD2 . LEU B 121 ? 0.3482 0.3158 0.2706 0.0469  -0.0605 -0.0375 154 LEU B CD2 
2264 N N   . LEU B 122 ? 0.2740 0.2402 0.2065 0.0665  -0.0272 -0.0112 155 LEU B N   
2265 C CA  . LEU B 122 ? 0.2783 0.2630 0.2259 0.0678  -0.0176 -0.0031 155 LEU B CA  
2266 C C   . LEU B 122 ? 0.3047 0.2948 0.2502 0.0799  -0.0085 -0.0012 155 LEU B C   
2267 O O   . LEU B 122 ? 0.3003 0.3026 0.2532 0.0825  0.0019  0.0047  155 LEU B O   
2268 C CB  . LEU B 122 ? 0.2289 0.2206 0.1960 0.0581  -0.0171 0.0000  155 LEU B CB  
2269 C CG  . LEU B 122 ? 0.2298 0.2210 0.2029 0.0465  -0.0219 0.0001  155 LEU B CG  
2270 C CD1 . LEU B 122 ? 0.2414 0.2345 0.2266 0.0391  -0.0218 0.0018  155 LEU B CD1 
2271 C CD2 . LEU B 122 ? 0.2132 0.2150 0.1910 0.0464  -0.0179 0.0045  155 LEU B CD2 
2272 N N   . SER B 123 ? 0.2653 0.2455 0.2010 0.0876  -0.0108 -0.0057 156 SER B N   
2273 C CA  . SER B 123 ? 0.2680 0.2557 0.2030 0.1009  -0.0018 -0.0048 156 SER B CA  
2274 C C   . SER B 123 ? 0.3399 0.3153 0.2485 0.1132  -0.0003 -0.0084 156 SER B C   
2275 O O   . SER B 123 ? 0.3539 0.3326 0.2577 0.1263  0.0079  -0.0084 156 SER B O   
2276 C CB  . SER B 123 ? 0.3132 0.2994 0.2526 0.1063  -0.0047 -0.0075 156 SER B CB  
2277 O OG  . SER B 123 ? 0.3433 0.3023 0.2618 0.1077  -0.0138 -0.0132 156 SER B OG  
2278 N N   . ALA B 124 ? 0.3346 0.2979 0.2263 0.1102  -0.0081 -0.0123 157 ALA B N   
2279 C CA  . ALA B 124 ? 0.3496 0.2997 0.2123 0.1221  -0.0101 -0.0185 157 ALA B CA  
2280 C C   . ALA B 124 ? 0.3489 0.3086 0.2029 0.1288  -0.0025 -0.0123 157 ALA B C   
2281 O O   . ALA B 124 ? 0.3656 0.3374 0.2347 0.1213  0.0010  -0.0046 157 ALA B O   
2282 C CB  . ALA B 124 ? 0.4251 0.3566 0.2744 0.1148  -0.0256 -0.0299 157 ALA B CB  
2283 N N   . PRO B 125 ? 0.4284 0.3208 0.2935 0.0269  0.0014  -0.0321 158 PRO B N   
2284 C CA  . PRO B 125 ? 0.4233 0.3414 0.2911 0.0272  -0.0017 -0.0269 158 PRO B CA  
2285 C C   . PRO B 125 ? 0.3049 0.2306 0.1749 0.0206  -0.0069 -0.0289 158 PRO B C   
2286 O O   . PRO B 125 ? 0.3819 0.3215 0.2567 0.0218  -0.0094 -0.0182 158 PRO B O   
2287 C CB  . PRO B 125 ? 0.4492 0.3762 0.3054 0.0333  0.0018  -0.0355 158 PRO B CB  
2288 C CG  . PRO B 125 ? 0.5253 0.4335 0.3783 0.0370  0.0070  -0.0403 158 PRO B CG  
2289 C CD  . PRO B 125 ? 0.4584 0.3421 0.3142 0.0318  0.0076  -0.0416 158 PRO B CD  
2290 N N   . SER B 126 ? 0.3505 0.2667 0.2203 0.0138  -0.0070 -0.0425 159 SER B N   
2291 C CA  . SER B 126 ? 0.3443 0.2730 0.2192 0.0083  -0.0125 -0.0483 159 SER B CA  
2292 C C   . SER B 126 ? 0.2613 0.1822 0.1453 0.0030  -0.0144 -0.0389 159 SER B C   
2293 O O   . SER B 126 ? 0.3079 0.2392 0.1979 -0.0012 -0.0187 -0.0431 159 SER B O   
2294 C CB  . SER B 126 ? 0.3494 0.2744 0.2290 0.0017  -0.0107 -0.0707 159 SER B CB  
2295 O OG  . SER B 126 ? 0.4068 0.3011 0.2911 -0.0042 -0.0011 -0.0725 159 SER B OG  
2296 N N   . CYS B 127 ? 0.2800 0.1860 0.1652 0.0051  -0.0123 -0.0278 160 CYS B N   
2297 C CA  . CYS B 127 ? 0.2824 0.1821 0.1745 0.0025  -0.0150 -0.0203 160 CYS B CA  
2298 C C   . CYS B 127 ? 0.3080 0.2275 0.2067 0.0017  -0.0210 -0.0139 160 CYS B C   
2299 O O   . CYS B 127 ? 0.2826 0.2029 0.1864 -0.0029 -0.0234 -0.0154 160 CYS B O   
2300 C CB  . CYS B 127 ? 0.3162 0.2062 0.2092 0.0091  -0.0154 -0.0121 160 CYS B CB  
2301 S SG  . CYS B 127 ? 0.3063 0.1910 0.2069 0.0092  -0.0207 -0.0058 160 CYS B SG  
2302 N N   . ALA B 128 ? 0.2420 0.1768 0.1406 0.0075  -0.0212 -0.0058 161 ALA B N   
2303 C CA  . ALA B 128 ? 0.3017 0.2510 0.2044 0.0099  -0.0235 0.0037  161 ALA B CA  
2304 C C   . ALA B 128 ? 0.2801 0.2424 0.1772 0.0093  -0.0285 -0.0056 161 ALA B C   
2305 O O   . ALA B 128 ? 0.2700 0.2362 0.1729 0.0079  -0.0322 -0.0025 161 ALA B O   
2306 C CB  . ALA B 128 ? 0.2783 0.2387 0.1795 0.0183  -0.0177 0.0153  161 ALA B CB  
2307 N N   . ALA B 129 ? 0.2435 0.2137 0.1321 0.0106  -0.0294 -0.0201 162 ALA B N   
2308 C CA  . ALA B 129 ? 0.2546 0.2427 0.1436 0.0106  -0.0361 -0.0347 162 ALA B CA  
2309 C C   . ALA B 129 ? 0.2607 0.2383 0.1651 -0.0011 -0.0364 -0.0423 162 ALA B C   
2310 O O   . ALA B 129 ? 0.2691 0.2595 0.1799 -0.0009 -0.0418 -0.0433 162 ALA B O   
2311 C CB  . ALA B 129 ? 0.2643 0.2634 0.1468 0.0133  -0.0377 -0.0545 162 ALA B CB  
2312 N N   . GLN B 130 ? 0.2484 0.2009 0.1574 -0.0092 -0.0291 -0.0452 163 GLN B N   
2313 C CA  . GLN B 130 ? 0.2664 0.2053 0.1878 -0.0185 -0.0251 -0.0498 163 GLN B CA  
2314 C C   . GLN B 130 ? 0.2855 0.2232 0.2089 -0.0167 -0.0283 -0.0349 163 GLN B C   
2315 O O   . GLN B 130 ? 0.2877 0.2322 0.2212 -0.0204 -0.0302 -0.0386 163 GLN B O   
2316 C CB  . GLN B 130 ? 0.2481 0.1563 0.1678 -0.0224 -0.0134 -0.0511 163 GLN B CB  
2317 C CG  . GLN B 130 ? 0.2986 0.2033 0.2211 -0.0259 -0.0076 -0.0684 163 GLN B CG  
2318 C CD  . GLN B 130 ? 0.3626 0.2741 0.3069 -0.0365 -0.0041 -0.0893 163 GLN B CD  
2319 O OE1 . GLN B 130 ? 0.3872 0.2921 0.3436 -0.0427 0.0008  -0.0884 163 GLN B OE1 
2320 N NE2 . GLN B 130 ? 0.4511 0.3772 0.4030 -0.0384 -0.0065 -0.1102 163 GLN B NE2 
2321 N N   . LEU B 131 ? 0.2527 0.1850 0.1699 -0.0107 -0.0294 -0.0198 164 LEU B N   
2322 C CA  . LEU B 131 ? 0.2450 0.1751 0.1676 -0.0093 -0.0324 -0.0086 164 LEU B CA  
2323 C C   . LEU B 131 ? 0.3108 0.2619 0.2371 -0.0065 -0.0379 -0.0064 164 LEU B C   
2324 O O   . LEU B 131 ? 0.2793 0.2312 0.2128 -0.0086 -0.0400 -0.0063 164 LEU B O   
2325 C CB  . LEU B 131 ? 0.2322 0.1562 0.1554 -0.0043 -0.0324 0.0024  164 LEU B CB  
2326 C CG  . LEU B 131 ? 0.2488 0.1719 0.1830 -0.0029 -0.0357 0.0110  164 LEU B CG  
2327 C CD1 . LEU B 131 ? 0.2720 0.1832 0.2060 -0.0053 -0.0366 0.0070  164 LEU B CD1 
2328 C CD2 . LEU B 131 ? 0.3361 0.2552 0.2794 0.0005  -0.0356 0.0158  164 LEU B CD2 
2329 N N   . ASP B 132 ? 0.2535 0.2224 0.1724 0.0006  -0.0399 -0.0055 165 ASP B N   
2330 C CA  . ASP B 132 ? 0.2772 0.2658 0.1942 0.0088  -0.0447 -0.0008 165 ASP B CA  
2331 C C   . ASP B 132 ? 0.2817 0.2836 0.2065 0.0050  -0.0504 -0.0166 165 ASP B C   
2332 O O   . ASP B 132 ? 0.2908 0.2983 0.2218 0.0069  -0.0536 -0.0127 165 ASP B O   
2333 C CB  . ASP B 132 ? 0.2348 0.2399 0.1364 0.0216  -0.0444 0.0031  165 ASP B CB  
2334 C CG  . ASP B 132 ? 0.4178 0.4391 0.3114 0.0362  -0.0465 0.0142  165 ASP B CG  
2335 O OD1 . ASP B 132 ? 0.4117 0.4218 0.3108 0.0383  -0.0409 0.0320  165 ASP B OD1 
2336 O OD2 . ASP B 132 ? 0.4215 0.4670 0.3038 0.0470  -0.0536 0.0041  165 ASP B OD2 
2337 N N   . ARG B 133 ? 0.2752 0.2803 0.2043 -0.0017 -0.0502 -0.0358 166 ARG B N   
2338 C CA  . ARG B 133 ? 0.2464 0.2673 0.1915 -0.0069 -0.0541 -0.0547 166 ARG B CA  
2339 C C   . ARG B 133 ? 0.2648 0.2685 0.2230 -0.0159 -0.0487 -0.0505 166 ARG B C   
2340 O O   . ARG B 133 ? 0.2632 0.2813 0.2317 -0.0148 -0.0530 -0.0533 166 ARG B O   
2341 C CB  . ARG B 133 ? 0.2675 0.2917 0.2217 -0.0144 -0.0518 -0.0782 166 ARG B CB  
2342 C CG  . ARG B 133 ? 0.3086 0.3453 0.2901 -0.0243 -0.0518 -0.1012 166 ARG B CG  
2343 C CD  . ARG B 133 ? 0.4491 0.5256 0.4357 -0.0137 -0.0661 -0.1120 166 ARG B CD  
2344 N NE  . ARG B 133 ? 0.5396 0.6313 0.5601 -0.0245 -0.0657 -0.1369 166 ARG B NE  
2345 C CZ  . ARG B 133 ? 0.5924 0.6983 0.6341 -0.0281 -0.0640 -0.1590 166 ARG B CZ  
2346 N NH1 . ARG B 133 ? 0.5933 0.7049 0.6235 -0.0216 -0.0671 -0.1653 166 ARG B NH1 
2347 N NH2 . ARG B 133 ? 0.6209 0.7356 0.6976 -0.0375 -0.0578 -0.1741 166 ARG B NH2 
2348 N N   . ALA B 134 ? 0.2759 0.2498 0.2306 -0.0215 -0.0397 -0.0419 167 ALA B N   
2349 C CA  . ALA B 134 ? 0.2819 0.2381 0.2432 -0.0263 -0.0336 -0.0372 167 ALA B CA  
2350 C C   . ALA B 134 ? 0.2571 0.2206 0.2179 -0.0198 -0.0403 -0.0249 167 ALA B C   
2351 O O   . ALA B 134 ? 0.2985 0.2678 0.2702 -0.0216 -0.0404 -0.0281 167 ALA B O   
2352 C CB  . ALA B 134 ? 0.2810 0.2066 0.2314 -0.0266 -0.0251 -0.0291 167 ALA B CB  
2353 N N   . LYS B 135 ? 0.2880 0.2524 0.2392 -0.0119 -0.0446 -0.0116 168 LYS B N   
2354 C CA  . LYS B 135 ? 0.2373 0.2037 0.1911 -0.0061 -0.0482 0.0003  168 LYS B CA  
2355 C C   . LYS B 135 ? 0.2774 0.2681 0.2362 -0.0012 -0.0539 -0.0044 168 LYS B C   
2356 O O   . LYS B 135 ? 0.2608 0.2527 0.2279 -0.0012 -0.0549 -0.0041 168 LYS B O   
2357 C CB  . LYS B 135 ? 0.1993 0.1620 0.1484 0.0005  -0.0478 0.0145  168 LYS B CB  
2358 C CG  . LYS B 135 ? 0.2519 0.1944 0.2025 -0.0026 -0.0446 0.0175  168 LYS B CG  
2359 C CD  . LYS B 135 ? 0.3935 0.3364 0.3459 0.0017  -0.0419 0.0275  168 LYS B CD  
2360 C CE  . LYS B 135 ? 0.3943 0.3418 0.3541 0.0080  -0.0401 0.0400  168 LYS B CE  
2361 N NZ  . LYS B 135 ? 0.4211 0.3658 0.3881 0.0112  -0.0324 0.0509  168 LYS B NZ  
2362 N N   . ARG B 136 ? 0.2566 0.2688 0.2099 0.0046  -0.0583 -0.0113 169 ARG B N   
2363 C CA  . ARG B 136 ? 0.2932 0.3344 0.2490 0.0142  -0.0665 -0.0179 169 ARG B CA  
2364 C C   . ARG B 136 ? 0.3001 0.3486 0.2768 0.0044  -0.0668 -0.0345 169 ARG B C   
2365 O O   . ARG B 136 ? 0.2605 0.3204 0.2439 0.0100  -0.0707 -0.0329 169 ARG B O   
2366 C CB  . ARG B 136 ? 0.2826 0.3485 0.2263 0.0250  -0.0727 -0.0265 169 ARG B CB  
2367 C CG  . ARG B 136 ? 0.4905 0.5444 0.4158 0.0309  -0.0674 -0.0119 169 ARG B CG  
2368 C CD  . ARG B 136 ? 0.5127 0.5788 0.4176 0.0521  -0.0679 0.0037  169 ARG B CD  
2369 N NE  . ARG B 136 ? 0.4611 0.5620 0.3567 0.0681  -0.0791 -0.0101 169 ARG B NE  
2370 C CZ  . ARG B 136 ? 0.5009 0.6190 0.3798 0.0807  -0.0816 -0.0168 169 ARG B CZ  
2371 N NH1 . ARG B 136 ? 0.4681 0.5735 0.3346 0.0799  -0.0748 -0.0098 169 ARG B NH1 
2372 N NH2 . ARG B 136 ? 0.4443 0.5889 0.3239 0.0928  -0.0878 -0.0309 169 ARG B NH2 
2373 N N   . ASP B 137 ? 0.3010 0.3406 0.2889 -0.0091 -0.0603 -0.0488 170 ASP B N   
2374 C CA  . ASP B 137 ? 0.2813 0.3272 0.2938 -0.0191 -0.0561 -0.0648 170 ASP B CA  
2375 C C   . ASP B 137 ? 0.2409 0.2665 0.2551 -0.0213 -0.0495 -0.0519 170 ASP B C   
2376 O O   . ASP B 137 ? 0.2155 0.2550 0.2453 -0.0211 -0.0504 -0.0575 170 ASP B O   
2377 C CB  . ASP B 137 ? 0.3441 0.3791 0.3695 -0.0328 -0.0457 -0.0809 170 ASP B CB  
2378 C CG  . ASP B 137 ? 0.4458 0.5078 0.4771 -0.0311 -0.0539 -0.1018 170 ASP B CG  
2379 O OD1 . ASP B 137 ? 0.4027 0.4953 0.4264 -0.0171 -0.0683 -0.1046 170 ASP B OD1 
2380 O OD2 . ASP B 137 ? 0.4458 0.4976 0.4877 -0.0416 -0.0453 -0.1156 170 ASP B OD2 
2381 N N   . ILE B 138 ? 0.2203 0.2162 0.2187 -0.0212 -0.0442 -0.0360 171 ILE B N   
2382 C CA  . ILE B 138 ? 0.2578 0.2356 0.2557 -0.0208 -0.0391 -0.0268 171 ILE B CA  
2383 C C   . ILE B 138 ? 0.2704 0.2612 0.2688 -0.0112 -0.0479 -0.0185 171 ILE B C   
2384 O O   . ILE B 138 ? 0.2789 0.2714 0.2863 -0.0106 -0.0462 -0.0193 171 ILE B O   
2385 C CB  . ILE B 138 ? 0.2818 0.2296 0.2633 -0.0198 -0.0342 -0.0158 171 ILE B CB  
2386 C CG1 . ILE B 138 ? 0.2489 0.1803 0.2282 -0.0267 -0.0227 -0.0226 171 ILE B CG1 
2387 C CG2 . ILE B 138 ? 0.2814 0.2141 0.2595 -0.0154 -0.0320 -0.0086 171 ILE B CG2 
2388 C CD1 . ILE B 138 ? 0.2809 0.2130 0.2782 -0.0352 -0.0103 -0.0343 171 ILE B CD1 
2389 N N   . VAL B 139 ? 0.2115 0.2117 0.2006 -0.0024 -0.0556 -0.0103 172 VAL B N   
2390 C CA  . VAL B 139 ? 0.2125 0.2203 0.2010 0.0087  -0.0608 0.0000  172 VAL B CA  
2391 C C   . VAL B 139 ? 0.3074 0.3425 0.3085 0.0122  -0.0656 -0.0114 172 VAL B C   
2392 O O   . VAL B 139 ? 0.2328 0.2694 0.2396 0.0173  -0.0666 -0.0073 172 VAL B O   
2393 C CB  . VAL B 139 ? 0.2366 0.2476 0.2123 0.0194  -0.0633 0.0128  172 VAL B CB  
2394 C CG1 . VAL B 139 ? 0.2962 0.3190 0.2700 0.0345  -0.0668 0.0226  172 VAL B CG1 
2395 C CG2 . VAL B 139 ? 0.2238 0.2083 0.1960 0.0159  -0.0579 0.0242  172 VAL B CG2 
2396 N N   . ARG B 140 ? 0.2332 0.2914 0.2422 0.0092  -0.0687 -0.0288 173 ARG B N   
2397 C CA  . ARG B 140 ? 0.2670 0.3579 0.2942 0.0127  -0.0749 -0.0451 173 ARG B CA  
2398 C C   . ARG B 140 ? 0.2806 0.3646 0.3302 0.0000  -0.0653 -0.0539 173 ARG B C   
2399 O O   . ARG B 140 ? 0.2825 0.3809 0.3445 0.0049  -0.0675 -0.0565 173 ARG B O   
2400 C CB  . ARG B 140 ? 0.2674 0.3879 0.3010 0.0135  -0.0821 -0.0659 173 ARG B CB  
2401 C CG  . ARG B 140 ? 0.4026 0.5663 0.4582 0.0202  -0.0925 -0.0881 173 ARG B CG  
2402 C CD  . ARG B 140 ? 0.4772 0.6704 0.5458 0.0182  -0.0997 -0.1159 173 ARG B CD  
2403 N NE  . ARG B 140 ? 0.5866 0.7727 0.6257 0.0268  -0.1027 -0.1068 173 ARG B NE  
2404 C CZ  . ARG B 140 ? 0.5864 0.7528 0.6232 0.0141  -0.0955 -0.1100 173 ARG B CZ  
2405 N NH1 . ARG B 140 ? 0.4818 0.6298 0.5422 -0.0070 -0.0827 -0.1205 173 ARG B NH1 
2406 N NH2 . ARG B 140 ? 0.5822 0.7446 0.5913 0.0242  -0.0985 -0.1005 173 ARG B NH2 
2407 N N   . SER B 141 ? 0.2715 0.3310 0.3242 -0.0140 -0.0528 -0.0564 174 SER B N   
2408 C CA  . SER B 141 ? 0.2559 0.3094 0.3303 -0.0247 -0.0394 -0.0653 174 SER B CA  
2409 C C   . SER B 141 ? 0.2950 0.3278 0.3602 -0.0201 -0.0343 -0.0499 174 SER B C   
2410 O O   . SER B 141 ? 0.2687 0.3058 0.3515 -0.0229 -0.0261 -0.0555 174 SER B O   
2411 C CB  . SER B 141 ? 0.2831 0.3139 0.3613 -0.0380 -0.0240 -0.0711 174 SER B CB  
2412 O OG  . SER B 141 ? 0.3804 0.3773 0.4303 -0.0352 -0.0202 -0.0532 174 SER B OG  
2413 N N   . ARG B 142 ? 0.2513 0.2804 0.3475 -0.0068 -0.0509 -0.0508 175 ARG B N   
2414 C CA  . ARG B 142 ? 0.2446 0.2715 0.3358 -0.0065 -0.0408 -0.0450 175 ARG B CA  
2415 C C   . ARG B 142 ? 0.2329 0.2573 0.3137 0.0008  -0.0440 -0.0443 175 ARG B C   
2416 O O   . ARG B 142 ? 0.2697 0.2898 0.3443 0.0022  -0.0371 -0.0409 175 ARG B O   
2417 C CB  . ARG B 142 ? 0.2719 0.2888 0.3457 -0.0107 -0.0334 -0.0400 175 ARG B CB  
2418 C CG  . ARG B 142 ? 0.3095 0.3270 0.3924 -0.0171 -0.0308 -0.0397 175 ARG B CG  
2419 C CD  . ARG B 142 ? 0.3288 0.3378 0.3966 -0.0205 -0.0240 -0.0343 175 ARG B CD  
2420 N NE  . ARG B 142 ? 0.3692 0.3774 0.4355 -0.0211 -0.0150 -0.0300 175 ARG B NE  
2421 C CZ  . ARG B 142 ? 0.3579 0.3691 0.4346 -0.0246 -0.0075 -0.0267 175 ARG B CZ  
2422 N NH1 . ARG B 142 ? 0.3124 0.3262 0.4038 -0.0292 -0.0081 -0.0263 175 ARG B NH1 
2423 N NH2 . ARG B 142 ? 0.3324 0.3432 0.4041 -0.0229 0.0010  -0.0234 175 ARG B NH2 
2424 N N   . HIS B 143 ? 0.2389 0.2648 0.3166 0.0061  -0.0547 -0.0477 176 HIS B N   
2425 C CA  . HIS B 143 ? 0.2825 0.3058 0.3519 0.0138  -0.0590 -0.0462 176 HIS B CA  
2426 C C   . HIS B 143 ? 0.2892 0.2992 0.3365 0.0139  -0.0530 -0.0398 176 HIS B C   
2427 O O   . HIS B 143 ? 0.3108 0.3163 0.3565 0.0172  -0.0500 -0.0375 176 HIS B O   
2428 C CB  . HIS B 143 ? 0.3167 0.3498 0.4081 0.0173  -0.0581 -0.0478 176 HIS B CB  
2429 C CG  . HIS B 143 ? 0.4150 0.4630 0.5349 0.0149  -0.0625 -0.0529 176 HIS B CG  
2430 N ND1 . HIS B 143 ? 0.5382 0.5933 0.6674 0.0190  -0.0766 -0.0584 176 HIS B ND1 
2431 C CD2 . HIS B 143 ? 0.5055 0.5623 0.6478 0.0086  -0.0553 -0.0530 176 HIS B CD2 
2432 C CE1 . HIS B 143 ? 0.5021 0.5697 0.6608 0.0144  -0.0788 -0.0624 176 HIS B CE1 
2433 N NE2 . HIS B 143 ? 0.4852 0.5543 0.6530 0.0079  -0.0651 -0.0584 176 HIS B NE2 
2434 N N   . LEU B 144 ? 0.2658 0.2693 0.2976 0.0103  -0.0517 -0.0372 177 LEU B N   
2435 C CA  . LEU B 144 ? 0.3002 0.2923 0.3154 0.0085  -0.0465 -0.0308 177 LEU B CA  
2436 C C   . LEU B 144 ? 0.2367 0.2220 0.2390 0.0145  -0.0513 -0.0264 177 LEU B C   
2437 O O   . LEU B 144 ? 0.2664 0.2542 0.2620 0.0190  -0.0575 -0.0266 177 LEU B O   
2438 C CB  . LEU B 144 ? 0.2132 0.2032 0.2201 0.0030  -0.0434 -0.0286 177 LEU B CB  
2439 C CG  . LEU B 144 ? 0.2588 0.2527 0.2762 -0.0031 -0.0387 -0.0311 177 LEU B CG  
2440 C CD1 . LEU B 144 ? 0.2636 0.2546 0.2726 -0.0071 -0.0362 -0.0282 177 LEU B CD1 
2441 C CD2 . LEU B 144 ? 0.2709 0.2626 0.2931 -0.0051 -0.0323 -0.0301 177 LEU B CD2 
2442 N N   . ASP B 145 ? 0.2516 0.2270 0.2491 0.0151  -0.0486 -0.0223 178 ASP B N   
2443 C CA  . ASP B 145 ? 0.2744 0.2411 0.2610 0.0204  -0.0527 -0.0164 178 ASP B CA  
2444 C C   . ASP B 145 ? 0.3194 0.2797 0.2920 0.0163  -0.0501 -0.0086 178 ASP B C   
2445 O O   . ASP B 145 ? 0.3012 0.2655 0.2734 0.0107  -0.0463 -0.0091 178 ASP B O   
2446 C CB  . ASP B 145 ? 0.2602 0.2176 0.2499 0.0235  -0.0519 -0.0161 178 ASP B CB  
2447 C CG  . ASP B 145 ? 0.3849 0.3322 0.3714 0.0172  -0.0459 -0.0154 178 ASP B CG  
2448 O OD1 . ASP B 145 ? 0.3086 0.2556 0.2905 0.0101  -0.0429 -0.0132 178 ASP B OD1 
2449 O OD2 . ASP B 145 ? 0.3871 0.3263 0.3754 0.0204  -0.0451 -0.0176 178 ASP B OD2 
2450 N N   . SER B 146 ? 0.2716 0.2224 0.2342 0.0193  -0.0518 -0.0005 179 SER B N   
2451 C CA  . SER B 146 ? 0.2972 0.2448 0.2490 0.0161  -0.0483 0.0086  179 SER B CA  
2452 C C   . SER B 146 ? 0.2950 0.2387 0.2513 0.0066  -0.0428 0.0105  179 SER B C   
2453 O O   . SER B 146 ? 0.2760 0.2246 0.2302 0.0025  -0.0388 0.0139  179 SER B O   
2454 C CB  . SER B 146 ? 0.3420 0.2790 0.2843 0.0205  -0.0503 0.0190  179 SER B CB  
2455 O OG  . SER B 146 ? 0.5089 0.4323 0.4566 0.0179  -0.0506 0.0210  179 SER B OG  
2456 N N   . LEU B 147 ? 0.2777 0.2122 0.2395 0.0039  -0.0431 0.0078  180 LEU B N   
2457 C CA  . LEU B 147 ? 0.2302 0.1600 0.1948 -0.0046 -0.0403 0.0087  180 LEU B CA  
2458 C C   . LEU B 147 ? 0.2184 0.1595 0.1869 -0.0082 -0.0372 0.0033  180 LEU B C   
2459 O O   . LEU B 147 ? 0.2285 0.1719 0.1979 -0.0140 -0.0348 0.0068  180 LEU B O   
2460 C CB  . LEU B 147 ? 0.2869 0.2033 0.2531 -0.0050 -0.0423 0.0047  180 LEU B CB  
2461 C CG  . LEU B 147 ? 0.2361 0.1464 0.2032 -0.0127 -0.0418 0.0030  180 LEU B CG  
2462 C CD1 . LEU B 147 ? 0.2616 0.1662 0.2302 -0.0197 -0.0429 0.0126  180 LEU B CD1 
2463 C CD2 . LEU B 147 ? 0.2948 0.1920 0.2596 -0.0100 -0.0439 -0.0041 180 LEU B CD2 
2464 N N   . TYR B 148 ? 0.2346 0.1832 0.2078 -0.0049 -0.0372 -0.0046 181 TYR B N   
2465 C CA  . TYR B 148 ? 0.2287 0.1864 0.2066 -0.0085 -0.0343 -0.0086 181 TYR B CA  
2466 C C   . TYR B 148 ? 0.2191 0.1851 0.1949 -0.0078 -0.0341 -0.0068 181 TYR B C   
2467 O O   . TYR B 148 ? 0.2186 0.1889 0.1965 -0.0117 -0.0315 -0.0069 181 TYR B O   
2468 C CB  . TYR B 148 ? 0.1933 0.1569 0.1799 -0.0060 -0.0335 -0.0161 181 TYR B CB  
2469 C CG  . TYR B 148 ? 0.2163 0.1741 0.2032 -0.0081 -0.0301 -0.0184 181 TYR B CG  
2470 C CD1 . TYR B 148 ? 0.2570 0.2049 0.2403 -0.0047 -0.0309 -0.0194 181 TYR B CD1 
2471 C CD2 . TYR B 148 ? 0.2701 0.2310 0.2588 -0.0125 -0.0262 -0.0197 181 TYR B CD2 
2472 C CE1 . TYR B 148 ? 0.2598 0.2013 0.2395 -0.0050 -0.0277 -0.0228 181 TYR B CE1 
2473 C CE2 . TYR B 148 ? 0.2737 0.2288 0.2582 -0.0130 -0.0228 -0.0216 181 TYR B CE2 
2474 C CZ  . TYR B 148 ? 0.3073 0.2527 0.2863 -0.0089 -0.0235 -0.0237 181 TYR B CZ  
2475 O OH  . TYR B 148 ? 0.2565 0.1949 0.2277 -0.0078 -0.0203 -0.0268 181 TYR B OH  
2476 N N   . GLN B 149 ? 0.2162 0.1840 0.1861 -0.0019 -0.0369 -0.0049 182 GLN B N   
2477 C CA  . GLN B 149 ? 0.2386 0.2131 0.2023 0.0005  -0.0362 -0.0036 182 GLN B CA  
2478 C C   . GLN B 149 ? 0.2254 0.1989 0.1859 -0.0038 -0.0309 0.0050  182 GLN B C   
2479 O O   . GLN B 149 ? 0.2191 0.1990 0.1804 -0.0048 -0.0278 0.0044  182 GLN B O   
2480 C CB  . GLN B 149 ? 0.2594 0.2347 0.2131 0.0090  -0.0408 -0.0029 182 GLN B CB  
2481 C CG  . GLN B 149 ? 0.2806 0.2609 0.2410 0.0135  -0.0477 -0.0125 182 GLN B CG  
2482 C CD  . GLN B 149 ? 0.3631 0.3434 0.3130 0.0226  -0.0545 -0.0118 182 GLN B CD  
2483 O OE1 . GLN B 149 ? 0.3715 0.3514 0.3054 0.0271  -0.0540 -0.0072 182 GLN B OE1 
2484 N NE2 . GLN B 149 ? 0.3049 0.2860 0.2631 0.0262  -0.0607 -0.0159 182 GLN B NE2 
2485 N N   . ARG B 150 ? 0.2113 0.1766 0.1703 -0.0063 -0.0301 0.0131  183 ARG B N   
2486 C CA  . ARG B 150 ? 0.2130 0.1786 0.1744 -0.0116 -0.0255 0.0222  183 ARG B CA  
2487 C C   . ARG B 150 ? 0.2046 0.1718 0.1758 -0.0187 -0.0248 0.0191  183 ARG B C   
2488 O O   . ARG B 150 ? 0.2100 0.1842 0.1855 -0.0214 -0.0211 0.0229  183 ARG B O   
2489 C CB  . ARG B 150 ? 0.2249 0.1795 0.1864 -0.0140 -0.0264 0.0312  183 ARG B CB  
2490 C CG  . ARG B 150 ? 0.2546 0.2062 0.2051 -0.0066 -0.0270 0.0368  183 ARG B CG  
2491 C CD  . ARG B 150 ? 0.3326 0.2694 0.2851 -0.0088 -0.0297 0.0437  183 ARG B CD  
2492 N NE  . ARG B 150 ? 0.3367 0.2702 0.2981 -0.0174 -0.0264 0.0537  183 ARG B NE  
2493 C CZ  . ARG B 150 ? 0.4150 0.3343 0.3841 -0.0233 -0.0302 0.0565  183 ARG B CZ  
2494 N NH1 . ARG B 150 ? 0.3424 0.2492 0.3097 -0.0207 -0.0363 0.0494  183 ARG B NH1 
2495 N NH2 . ARG B 150 ? 0.3000 0.2175 0.2803 -0.0317 -0.0282 0.0664  183 ARG B NH2 
2496 N N   . ALA B 151 ? 0.2012 0.1624 0.1753 -0.0210 -0.0280 0.0125  184 ALA B N   
2497 C CA  . ALA B 151 ? 0.1895 0.1513 0.1693 -0.0265 -0.0280 0.0098  184 ALA B CA  
2498 C C   . ALA B 151 ? 0.1856 0.1576 0.1678 -0.0251 -0.0256 0.0061  184 ALA B C   
2499 O O   . ALA B 151 ? 0.1759 0.1517 0.1630 -0.0286 -0.0243 0.0080  184 ALA B O   
2500 C CB  . ALA B 151 ? 0.1908 0.1440 0.1693 -0.0272 -0.0307 0.0036  184 ALA B CB  
2501 N N   . LEU B 152 ? 0.1786 0.1545 0.1588 -0.0198 -0.0259 0.0004  185 LEU B N   
2502 C CA  . LEU B 152 ? 0.1857 0.1687 0.1694 -0.0185 -0.0248 -0.0041 185 LEU B CA  
2503 C C   . LEU B 152 ? 0.2089 0.1981 0.1903 -0.0162 -0.0218 -0.0001 185 LEU B C   
2504 O O   . LEU B 152 ? 0.1889 0.1823 0.1750 -0.0170 -0.0200 -0.0011 185 LEU B O   
2505 C CB  . LEU B 152 ? 0.1754 0.1606 0.1602 -0.0140 -0.0277 -0.0117 185 LEU B CB  
2506 C CG  . LEU B 152 ? 0.1901 0.1798 0.1810 -0.0136 -0.0280 -0.0175 185 LEU B CG  
2507 C CD1 . LEU B 152 ? 0.2010 0.1888 0.2001 -0.0191 -0.0260 -0.0178 185 LEU B CD1 
2508 C CD2 . LEU B 152 ? 0.2557 0.2479 0.2486 -0.0089 -0.0329 -0.0248 185 LEU B CD2 
2509 N N   . THR B 153 ? 0.1975 0.1874 0.1714 -0.0126 -0.0204 0.0052  186 THR B N   
2510 C CA  . THR B 153 ? 0.2035 0.2005 0.1748 -0.0098 -0.0151 0.0108  186 THR B CA  
2511 C C   . THR B 153 ? 0.2128 0.2127 0.1954 -0.0164 -0.0121 0.0175  186 THR B C   
2512 O O   . THR B 153 ? 0.1975 0.2049 0.1848 -0.0151 -0.0087 0.0178  186 THR B O   
2513 C CB  . THR B 153 ? 0.2427 0.2393 0.2031 -0.0050 -0.0130 0.0179  186 THR B CB  
2514 O OG1 . THR B 153 ? 0.2442 0.2393 0.1939 0.0022  -0.0175 0.0107  186 THR B OG1 
2515 C CG2 . THR B 153 ? 0.2898 0.2952 0.2471 -0.0013 -0.0050 0.0252  186 THR B CG2 
2516 N N   . THR B 154 ? 0.1995 0.1930 0.1873 -0.0232 -0.0145 0.0220  187 THR B N   
2517 C CA  . THR B 154 ? 0.1974 0.1936 0.1974 -0.0299 -0.0142 0.0276  187 THR B CA  
2518 C C   . THR B 154 ? 0.1908 0.1889 0.1959 -0.0313 -0.0164 0.0216  187 THR B C   
2519 O O   . THR B 154 ? 0.1688 0.1746 0.1832 -0.0324 -0.0146 0.0249  187 THR B O   
2520 C CB  . THR B 154 ? 0.1853 0.1712 0.1888 -0.0366 -0.0188 0.0314  187 THR B CB  
2521 O OG1 . THR B 154 ? 0.1961 0.1802 0.1975 -0.0358 -0.0161 0.0398  187 THR B OG1 
2522 C CG2 . THR B 154 ? 0.1834 0.1710 0.2004 -0.0441 -0.0219 0.0351  187 THR B CG2 
2523 N N   . ALA B 155 ? 0.1683 0.1599 0.1682 -0.0307 -0.0197 0.0138  188 ALA B N   
2524 C CA  . ALA B 155 ? 0.1628 0.1538 0.1662 -0.0326 -0.0215 0.0098  188 ALA B CA  
2525 C C   . ALA B 155 ? 0.1991 0.1976 0.2061 -0.0282 -0.0186 0.0078  188 ALA B C   
2526 O O   . ALA B 155 ? 0.1844 0.1845 0.1976 -0.0297 -0.0194 0.0084  188 ALA B O   
2527 C CB  . ALA B 155 ? 0.1662 0.1499 0.1642 -0.0324 -0.0235 0.0035  188 ALA B CB  
2528 N N   . THR B 156 ? 0.1628 0.1648 0.1649 -0.0221 -0.0160 0.0050  189 THR B N   
2529 C CA  . THR B 156 ? 0.1637 0.1700 0.1671 -0.0165 -0.0141 0.0007  189 THR B CA  
2530 C C   . THR B 156 ? 0.1689 0.1846 0.1731 -0.0117 -0.0085 0.0055  189 THR B C   
2531 O O   . THR B 156 ? 0.1918 0.2105 0.1950 -0.0051 -0.0065 0.0010  189 THR B O   
2532 C CB  . THR B 156 ? 0.1674 0.1705 0.1639 -0.0117 -0.0165 -0.0078 189 THR B CB  
2533 O OG1 . THR B 156 ? 0.1857 0.1898 0.1723 -0.0082 -0.0158 -0.0061 189 THR B OG1 
2534 C CG2 . THR B 156 ? 0.2411 0.2379 0.2413 -0.0162 -0.0202 -0.0118 189 THR B CG2 
2535 N N   . GLN B 157 ? 0.1706 0.1908 0.1778 -0.0145 -0.0055 0.0147  190 GLN B N   
2536 C CA  . GLN B 157 ? 0.1783 0.2089 0.1855 -0.0090 0.0022  0.0206  190 GLN B CA  
2537 C C   . GLN B 157 ? 0.1936 0.2334 0.2127 -0.0064 0.0056  0.0218  190 GLN B C   
2538 O O   . GLN B 157 ? 0.2037 0.2528 0.2211 0.0014  0.0133  0.0239  190 GLN B O   
2539 C CB  . GLN B 157 ? 0.2295 0.2629 0.2412 -0.0140 0.0050  0.0321  190 GLN B CB  
2540 C CG  . GLN B 157 ? 0.1899 0.2250 0.2193 -0.0232 0.0017  0.0379  190 GLN B CG  
2541 C CD  . GLN B 157 ? 0.3742 0.4095 0.4107 -0.0295 0.0027  0.0486  190 GLN B CD  
2542 O OE1 . GLN B 157 ? 0.4676 0.5137 0.5117 -0.0282 0.0106  0.0584  190 GLN B OE1 
2543 N NE2 . GLN B 157 ? 0.3562 0.3791 0.3909 -0.0361 -0.0048 0.0472  190 GLN B NE2 
2544 N N   . SER B 158 ? 0.1680 0.2058 0.1982 -0.0115 0.0006  0.0208  191 SER B N   
2545 C CA  . SER B 158 ? 0.2132 0.2593 0.2564 -0.0087 0.0025  0.0225  191 SER B CA  
2546 C C   . SER B 158 ? 0.2063 0.2463 0.2464 -0.0033 0.0001  0.0130  191 SER B C   
2547 O O   . SER B 158 ? 0.2131 0.2576 0.2640 -0.0003 0.0006  0.0137  191 SER B O   
2548 C CB  . SER B 158 ? 0.1620 0.2102 0.2205 -0.0173 -0.0028 0.0289  191 SER B CB  
2549 O OG  . SER B 158 ? 0.1618 0.2154 0.2271 -0.0228 -0.0013 0.0377  191 SER B OG  
2550 N N   . TYR B 159 ? 0.1938 0.2235 0.2216 -0.0019 -0.0029 0.0046  192 TYR B N   
2551 C CA  . TYR B 159 ? 0.1760 0.1980 0.2038 0.0015  -0.0062 -0.0040 192 TYR B CA  
2552 C C   . TYR B 159 ? 0.2233 0.2502 0.2526 0.0119  -0.0019 -0.0075 192 TYR B C   
2553 O O   . TYR B 159 ? 0.2015 0.2252 0.2392 0.0141  -0.0037 -0.0098 192 TYR B O   
2554 C CB  . TYR B 159 ? 0.1742 0.1869 0.1918 0.0015  -0.0102 -0.0124 192 TYR B CB  
2555 C CG  . TYR B 159 ? 0.2087 0.2145 0.2276 -0.0071 -0.0146 -0.0114 192 TYR B CG  
2556 C CD1 . TYR B 159 ? 0.2019 0.2085 0.2253 -0.0139 -0.0153 -0.0039 192 TYR B CD1 
2557 C CD2 . TYR B 159 ? 0.2159 0.2150 0.2319 -0.0077 -0.0183 -0.0185 192 TYR B CD2 
2558 C CE1 . TYR B 159 ? 0.1731 0.1728 0.1945 -0.0200 -0.0183 -0.0038 192 TYR B CE1 
2559 C CE2 . TYR B 159 ? 0.2156 0.2100 0.2334 -0.0144 -0.0204 -0.0172 192 TYR B CE2 
2560 C CZ  . TYR B 159 ? 0.1623 0.1568 0.1812 -0.0199 -0.0197 -0.0100 192 TYR B CZ  
2561 O OH  . TYR B 159 ? 0.2479 0.2374 0.2657 -0.0248 -0.0208 -0.0094 192 TYR B OH  
2562 N N   . CYS B 160 ? 0.1935 0.2268 0.2130 0.0195  0.0041  -0.0084 193 CYS B N   
2563 C CA  . CYS B 160 ? 0.2346 0.2706 0.2504 0.0317  0.0086  -0.0144 193 CYS B CA  
2564 C C   . CYS B 160 ? 0.2456 0.2964 0.2748 0.0357  0.0167  -0.0058 193 CYS B C   
2565 O O   . CYS B 160 ? 0.4117 0.4687 0.4365 0.0475  0.0239  -0.0087 193 CYS B O   
2566 C CB  . CYS B 160 ? 0.2484 0.2832 0.2433 0.0401  0.0108  -0.0205 193 CYS B CB  
2567 S SG  . CYS B 160 ? 0.3157 0.3346 0.3001 0.0365  -0.0010 -0.0323 193 CYS B SG  
2568 N N   . GLN B 161 ? 0.3240 0.3806 0.3698 0.0266  0.0153  0.0040  194 GLN B N   
2569 C CA  . GLN B 161 ? 0.3070 0.3787 0.3717 0.0289  0.0206  0.0123  194 GLN B CA  
2570 C C   . GLN B 161 ? 0.3258 0.3939 0.4025 0.0321  0.0160  0.0090  194 GLN B C   
2571 O O   . GLN B 161 ? 0.3029 0.3838 0.3979 0.0345  0.0189  0.0156  194 GLN B O   
2572 C CB  . GLN B 161 ? 0.3612 0.4408 0.4398 0.0173  0.0187  0.0242  194 GLN B CB  
2573 C CG  . GLN B 161 ? 0.3399 0.4186 0.4085 0.0115  0.0205  0.0285  194 GLN B CG  
2574 C CD  . GLN B 161 ? 0.4817 0.5749 0.5506 0.0175  0.0328  0.0360  194 GLN B CD  
2575 O OE1 . GLN B 161 ? 0.5615 0.6683 0.6410 0.0255  0.0409  0.0389  194 GLN B OE1 
2576 N NE2 . GLN B 161 ? 0.5842 0.6748 0.6414 0.0144  0.0350  0.0399  194 GLN B NE2 
2577 N N   . ALA B 162 ? 0.2987 0.3500 0.3679 0.0316  0.0087  0.0001  195 ALA B N   
2578 C CA  . ALA B 162 ? 0.2885 0.3335 0.3690 0.0334  0.0036  -0.0013 195 ALA B CA  
2579 C C   . ALA B 162 ? 0.3931 0.4458 0.4811 0.0471  0.0099  -0.0039 195 ALA B C   
2580 O O   . ALA B 162 ? 0.4411 0.4927 0.5171 0.0572  0.0153  -0.0121 195 ALA B O   
2581 C CB  . ALA B 162 ? 0.2913 0.3165 0.3630 0.0310  -0.0036 -0.0099 195 ALA B CB  
2582 N N   . LEU B 163 ? 0.3654 0.4248 0.4721 0.0484  0.0084  0.0023  196 LEU B N   
2583 C CA  . LEU B 163 ? 0.4322 0.5006 0.5495 0.0627  0.0149  0.0005  196 LEU B CA  
2584 C C   . LEU B 163 ? 0.4271 0.4768 0.5424 0.0699  0.0094  -0.0093 196 LEU B C   
2585 O O   . LEU B 163 ? 0.4484 0.4844 0.5656 0.0621  0.0001  -0.0079 196 LEU B O   
2586 C CB  . LEU B 163 ? 0.5207 0.6080 0.6630 0.0610  0.0155  0.0127  196 LEU B CB  
2587 C CG  . LEU B 163 ? 0.5569 0.6656 0.7067 0.0573  0.0238  0.0222  196 LEU B CG  
2588 C CD1 . LEU B 163 ? 0.6390 0.7656 0.8176 0.0531  0.0211  0.0341  196 LEU B CD1 
2589 C CD2 . LEU B 163 ? 0.4706 0.5898 0.6135 0.0706  0.0383  0.0189  196 LEU B CD2 
2590 C C   . ACE C 1   ? 0.2348 0.2156 0.2371 0.0050  0.0004  -0.0061 0   ACE C C   
2591 O O   . ACE C 1   ? 0.2423 0.2246 0.2395 0.0086  -0.0014 -0.0074 0   ACE C O   
2592 C CH3 . ACE C 1   ? 0.2564 0.2415 0.2637 0.0060  0.0036  -0.0040 0   ACE C CH3 
2593 N N   . DTY C 2   ? 0.1903 0.1659 0.1946 0.0002  -0.0005 -0.0063 1   DTY C N   
2594 C CA  . DTY C 2   ? 0.1988 0.1666 0.1954 0.0003  -0.0045 -0.0093 1   DTY C CA  
2595 C C   . DTY C 2   ? 0.2203 0.1899 0.2240 -0.0053 -0.0096 -0.0108 1   DTY C C   
2596 O O   . DTY C 2   ? 0.2009 0.1723 0.2155 -0.0111 -0.0092 -0.0089 1   DTY C O   
2597 C CB  . DTY C 2   ? 0.2431 0.1961 0.2309 0.0006  -0.0028 -0.0091 1   DTY C CB  
2598 C CG  . DTY C 2   ? 0.2254 0.1668 0.2018 0.0025  -0.0073 -0.0128 1   DTY C CG  
2599 C CD1 . DTY C 2   ? 0.2398 0.1679 0.2151 -0.0027 -0.0106 -0.0138 1   DTY C CD1 
2600 C CD2 . DTY C 2   ? 0.2253 0.1686 0.1920 0.0099  -0.0084 -0.0151 1   DTY C CD2 
2601 C CE1 . DTY C 2   ? 0.2552 0.1695 0.2173 0.0004  -0.0159 -0.0183 1   DTY C CE1 
2602 C CE2 . DTY C 2   ? 0.2396 0.1717 0.1933 0.0139  -0.0121 -0.0189 1   DTY C CE2 
2603 C CZ  . DTY C 2   ? 0.2554 0.1716 0.2054 0.0096  -0.0164 -0.0210 1   DTY C CZ  
2604 O OH  . DTY C 2   ? 0.2881 0.1903 0.2227 0.0147  -0.0213 -0.0257 1   DTY C OH  
2605 N N   . GLN C 3   ? 0.2029 0.1723 0.2005 -0.0030 -0.0144 -0.0138 2   GLN C N   
2606 C CA  . GLN C 3   ? 0.2072 0.1769 0.2089 -0.0069 -0.0208 -0.0161 2   GLN C CA  
2607 C C   . GLN C 3   ? 0.1953 0.1789 0.2064 -0.0073 -0.0217 -0.0146 2   GLN C C   
2608 O O   . GLN C 3   ? 0.1928 0.1828 0.2013 -0.0030 -0.0193 -0.0130 2   GLN C O   
2609 C CB  . GLN C 3   ? 0.2204 0.1806 0.2069 -0.0023 -0.0260 -0.0204 2   GLN C CB  
2610 C CG  . GLN C 3   ? 0.2365 0.1793 0.2121 -0.0015 -0.0269 -0.0227 2   GLN C CG  
2611 C CD  . GLN C 3   ? 0.2977 0.2293 0.2559 0.0048  -0.0327 -0.0279 2   GLN C CD  
2612 O OE1 . GLN C 3   ? 0.2924 0.2305 0.2425 0.0121  -0.0317 -0.0282 2   GLN C OE1 
2613 N NE2 . GLN C 3   ? 0.3413 0.2553 0.2932 0.0022  -0.0387 -0.0317 2   GLN C NE2 
2614 N N   . PHE C 4   ? 0.1951 0.1831 0.2176 -0.0125 -0.0255 -0.0147 3   PHE C N   
2615 C CA  . PHE C 4   ? 0.1942 0.1938 0.2244 -0.0121 -0.0276 -0.0138 3   PHE C CA  
2616 C C   . PHE C 4   ? 0.2516 0.2542 0.2932 -0.0176 -0.0341 -0.0152 3   PHE C C   
2617 O O   . PHE C 4   ? 0.1970 0.1960 0.2460 -0.0233 -0.0346 -0.0151 3   PHE C O   
2618 C CB  . PHE C 4   ? 0.1830 0.1915 0.2212 -0.0110 -0.0216 -0.0100 3   PHE C CB  
2619 C CG  . PHE C 4   ? 0.2172 0.2270 0.2649 -0.0144 -0.0169 -0.0077 3   PHE C CG  
2620 C CD1 . PHE C 4   ? 0.1770 0.1795 0.2184 -0.0133 -0.0114 -0.0064 3   PHE C CD1 
2621 C CD2 . PHE C 4   ? 0.2128 0.2320 0.2757 -0.0179 -0.0175 -0.0060 3   PHE C CD2 
2622 C CE1 . PHE C 4   ? 0.1950 0.1984 0.2436 -0.0156 -0.0060 -0.0031 3   PHE C CE1 
2623 C CE2 . PHE C 4   ? 0.2258 0.2481 0.2980 -0.0204 -0.0115 -0.0024 3   PHE C CE2 
2624 C CZ  . PHE C 4   ? 0.3003 0.3141 0.3646 -0.0192 -0.0055 -0.0007 3   PHE C CZ  
2625 N N   . GLU C 5   ? 0.1901 0.1992 0.2335 -0.0160 -0.0393 -0.0162 4   GLU C N   
2626 C CA  . GLU C 5   ? 0.2406 0.2559 0.2976 -0.0206 -0.0461 -0.0173 4   GLU C CA  
2627 C C   . GLU C 5   ? 0.2452 0.2745 0.3193 -0.0219 -0.0414 -0.0132 4   GLU C C   
2628 O O   . GLU C 5   ? 0.1936 0.2261 0.2656 -0.0180 -0.0347 -0.0104 4   GLU C O   
2629 C CB  . GLU C 5   ? 0.2146 0.2301 0.2643 -0.0169 -0.0546 -0.0204 4   GLU C CB  
2630 C CG  . GLU C 5   ? 0.2853 0.2871 0.3152 -0.0131 -0.0592 -0.0247 4   GLU C CG  
2631 C CD  . GLU C 5   ? 0.3999 0.3905 0.4305 -0.0184 -0.0656 -0.0289 4   GLU C CD  
2632 O OE1 . GLU C 5   ? 0.4068 0.4012 0.4513 -0.0243 -0.0731 -0.0304 4   GLU C OE1 
2633 O OE2 . GLU C 5   ? 0.4323 0.4103 0.4502 -0.0168 -0.0635 -0.0304 4   GLU C OE2 
2634 N N   . GLN C 6   ? 0.2232 0.2610 0.3145 -0.0271 -0.0455 -0.0129 5   GLN C N   
2635 C CA  . GLN C 6   ? 0.2931 0.3459 0.4016 -0.0273 -0.0403 -0.0085 5   GLN C CA  
2636 C C   . GLN C 6   ? 0.2437 0.3032 0.3494 -0.0202 -0.0401 -0.0079 5   GLN C C   
2637 O O   . GLN C 6   ? 0.2564 0.3234 0.3680 -0.0169 -0.0337 -0.0047 5   GLN C O   
2638 C CB  . GLN C 6   ? 0.3184 0.3819 0.4485 -0.0342 -0.0456 -0.0079 5   GLN C CB  
2639 C CG  . GLN C 6   ? 0.5036 0.5592 0.6389 -0.0429 -0.0471 -0.0078 5   GLN C CG  
2640 C CD  . GLN C 6   ? 0.6854 0.7468 0.8328 -0.0463 -0.0361 -0.0011 5   GLN C CD  
2641 O OE1 . GLN C 6   ? 0.5764 0.6413 0.7192 -0.0403 -0.0263 0.0021  5   GLN C OE1 
2642 N NE2 . GLN C 6   ? 0.7087 0.7703 0.8712 -0.0558 -0.0380 0.0012  5   GLN C NE2 
2643 N N   . TRP C 7   ? 0.1778 0.2333 0.2731 -0.0169 -0.0470 -0.0107 6   TRP C N   
2644 C CA  . TRP C 7   ? 0.1679 0.2277 0.2600 -0.0106 -0.0476 -0.0095 6   TRP C CA  
2645 C C   . TRP C 7   ? 0.1861 0.2374 0.2628 -0.0063 -0.0427 -0.0080 6   TRP C C   
2646 O O   . TRP C 7   ? 0.1842 0.2365 0.2576 -0.0018 -0.0431 -0.0063 6   TRP C O   
2647 C CB  . TRP C 7   ? 0.1980 0.2587 0.2875 -0.0090 -0.0579 -0.0122 6   TRP C CB  
2648 C CG  . TRP C 7   ? 0.2033 0.2516 0.2760 -0.0088 -0.0625 -0.0155 6   TRP C CG  
2649 C CD1 . TRP C 7   ? 0.2063 0.2486 0.2784 -0.0132 -0.0681 -0.0195 6   TRP C CD1 
2650 C CD2 . TRP C 7   ? 0.1887 0.2289 0.2425 -0.0033 -0.0614 -0.0148 6   TRP C CD2 
2651 N NE1 . TRP C 7   ? 0.2063 0.2364 0.2577 -0.0092 -0.0708 -0.0221 6   TRP C NE1 
2652 C CE2 . TRP C 7   ? 0.2007 0.2309 0.2414 -0.0031 -0.0659 -0.0187 6   TRP C CE2 
2653 C CE3 . TRP C 7   ? 0.1849 0.2250 0.2318 0.0015  -0.0572 -0.0108 6   TRP C CE3 
2654 C CZ2 . TRP C 7   ? 0.2387 0.2612 0.2598 0.0029  -0.0648 -0.0182 6   TRP C CZ2 
2655 C CZ3 . TRP C 7   ? 0.1915 0.2244 0.2213 0.0055  -0.0563 -0.0095 6   TRP C CZ3 
2656 C CH2 . TRP C 7   ? 0.2127 0.2380 0.2297 0.0068  -0.0594 -0.0129 6   TRP C CH2 
2657 N N   . HIS C 8   ? 0.1646 0.2076 0.2327 -0.0078 -0.0384 -0.0084 7   HIS C N   
2658 C CA  . HIS C 8   ? 0.1625 0.1994 0.2186 -0.0044 -0.0345 -0.0067 7   HIS C CA  
2659 C C   . HIS C 8   ? 0.1880 0.2270 0.2481 -0.0023 -0.0292 -0.0043 7   HIS C C   
2660 O O   . HIS C 8   ? 0.1629 0.2057 0.2313 -0.0031 -0.0256 -0.0039 7   HIS C O   
2661 C CB  . HIS C 8   ? 0.1724 0.2010 0.2191 -0.0055 -0.0318 -0.0080 7   HIS C CB  
2662 C CG  . HIS C 8   ? 0.1900 0.2129 0.2255 -0.0044 -0.0366 -0.0105 7   HIS C CG  
2663 N ND1 . HIS C 8   ? 0.2072 0.2218 0.2325 -0.0038 -0.0353 -0.0123 7   HIS C ND1 
2664 C CD2 . HIS C 8   ? 0.2067 0.2301 0.2375 -0.0022 -0.0429 -0.0116 7   HIS C CD2 
2665 C CE1 . HIS C 8   ? 0.2480 0.2580 0.2621 -0.0009 -0.0403 -0.0147 7   HIS C CE1 
2666 N NE2 . HIS C 8   ? 0.2351 0.2502 0.2519 0.0002  -0.0450 -0.0142 7   HIS C NE2 
2667 N N   . ILE C 9   ? 0.1585 0.1941 0.2119 0.0005  -0.0287 -0.0024 8   ILE C N   
2668 C CA  . ILE C 9   ? 0.1741 0.2081 0.2284 0.0029  -0.0255 -0.0011 8   ILE C CA  
2669 C C   . ILE C 9   ? 0.1810 0.2120 0.2336 0.0021  -0.0204 -0.0020 8   ILE C C   
2670 O O   . ILE C 9   ? 0.1985 0.2298 0.2536 0.0044  -0.0174 -0.0019 8   ILE C O   
2671 C CB  . ILE C 9   ? 0.1661 0.1957 0.2145 0.0043  -0.0272 0.0014  8   ILE C CB  
2672 C CG1 . ILE C 9   ? 0.1941 0.2251 0.2429 0.0059  -0.0318 0.0031  8   ILE C CG1 
2673 C CG2 . ILE C 9   ? 0.1610 0.1861 0.2093 0.0063  -0.0258 0.0017  8   ILE C CG2 
2674 C CD1 . ILE C 9   ? 0.1952 0.2218 0.2380 0.0061  -0.0331 0.0073  8   ILE C CD1 
2675 N N   . ARG C 10  ? 0.1601 0.1874 0.2067 0.0002  -0.0194 -0.0027 9   ARG C N   
2676 C CA  . ARG C 10  ? 0.1519 0.1750 0.1953 0.0002  -0.0150 -0.0033 9   ARG C CA  
2677 C C   . ARG C 10  ? 0.2017 0.2269 0.2516 -0.0010 -0.0117 -0.0032 9   ARG C C   
2678 O O   . ARG C 10  ? 0.2070 0.2294 0.2546 0.0009  -0.0072 -0.0026 9   ARG C O   
2679 C CB  . ARG C 10  ? 0.1568 0.1754 0.1923 -0.0007 -0.0151 -0.0043 9   ARG C CB  
2680 C CG  . ARG C 10  ? 0.1638 0.1767 0.1953 -0.0007 -0.0113 -0.0051 9   ARG C CG  
2681 C CD  . ARG C 10  ? 0.2039 0.2124 0.2257 0.0013  -0.0112 -0.0058 9   ARG C CD  
2682 N NE  . ARG C 10  ? 0.1920 0.2031 0.2128 0.0041  -0.0106 -0.0042 9   ARG C NE  
2683 C CZ  . ARG C 10  ? 0.2354 0.2460 0.2507 0.0067  -0.0097 -0.0039 9   ARG C CZ  
2684 N NH1 . ARG C 10  ? 0.1978 0.2042 0.2055 0.0083  -0.0090 -0.0054 9   ARG C NH1 
2685 N NH2 . ARG C 10  ? 0.2222 0.2363 0.2402 0.0081  -0.0101 -0.0022 9   ARG C NH2 
2686 N N   . GLY C 11  ? 0.1709 0.2019 0.2296 -0.0039 -0.0139 -0.0033 10  GLY C N   
2687 C CA  . GLY C 11  ? 0.1551 0.1910 0.2237 -0.0059 -0.0101 -0.0017 10  GLY C CA  
2688 C C   . GLY C 11  ? 0.1948 0.2359 0.2673 -0.0010 -0.0055 0.0003  10  GLY C C   
2689 O O   . GLY C 11  ? 0.2188 0.2643 0.2978 -0.0013 0.0001  0.0029  10  GLY C O   
2690 N N   . ARG C 12  ? 0.1995 0.2396 0.2675 0.0040  -0.0076 -0.0005 11  ARG C N   
2691 C CA  . ARG C 12  ? 0.2182 0.2608 0.2868 0.0106  -0.0047 0.0003  11  ARG C CA  
2692 C C   . ARG C 12  ? 0.2436 0.2782 0.3018 0.0152  -0.0005 0.0000  11  ARG C C   
2693 O O   . ARG C 12  ? 0.2186 0.2543 0.2752 0.0218  0.0031  0.0006  11  ARG C O   
2694 C CB  . ARG C 12  ? 0.1703 0.2114 0.2368 0.0143  -0.0104 -0.0009 11  ARG C CB  
2695 C CG  . ARG C 12  ? 0.2542 0.3025 0.3288 0.0121  -0.0154 -0.0007 11  ARG C CG  
2696 C CD  . ARG C 12  ? 0.3418 0.3848 0.4111 0.0159  -0.0207 -0.0010 11  ARG C CD  
2697 N NE  . ARG C 12  ? 0.3986 0.4456 0.4715 0.0143  -0.0262 -0.0006 11  ARG C NE  
2698 C CZ  . ARG C 12  ? 0.4662 0.5080 0.5342 0.0166  -0.0309 0.0003  11  ARG C CZ  
2699 N NH1 . ARG C 12  ? 0.3899 0.4221 0.4510 0.0194  -0.0317 0.0007  11  ARG C NH1 
2700 N NH2 . ARG C 12  ? 0.3600 0.4053 0.4297 0.0161  -0.0357 0.0009  11  ARG C NH2 
2701 N N   . TYR C 13  ? 0.1581 0.1847 0.2081 0.0129  -0.0009 -0.0009 12  TYR C N   
2702 C CA  . TYR C 13  ? 0.1849 0.2029 0.2237 0.0179  0.0001  -0.0021 12  TYR C CA  
2703 C C   . TYR C 13  ? 0.2208 0.2352 0.2549 0.0171  0.0055  -0.0009 12  TYR C C   
2704 O O   . TYR C 13  ? 0.2144 0.2333 0.2548 0.0145  0.0105  0.0019  12  TYR C O   
2705 C CB  . TYR C 13  ? 0.2194 0.2320 0.2536 0.0171  -0.0063 -0.0040 12  TYR C CB  
2706 C CG  . TYR C 13  ? 0.2204 0.2345 0.2586 0.0175  -0.0116 -0.0041 12  TYR C CG  
2707 C CD1 . TYR C 13  ? 0.1824 0.1965 0.2209 0.0232  -0.0118 -0.0047 12  TYR C CD1 
2708 C CD2 . TYR C 13  ? 0.1700 0.1850 0.2104 0.0131  -0.0159 -0.0032 12  TYR C CD2 
2709 C CE1 . TYR C 13  ? 0.2323 0.2456 0.2731 0.0242  -0.0170 -0.0047 12  TYR C CE1 
2710 C CE2 . TYR C 13  ? 0.2129 0.2278 0.2559 0.0136  -0.0204 -0.0024 12  TYR C CE2 
2711 C CZ  . TYR C 13  ? 0.2237 0.2370 0.2669 0.0190  -0.0214 -0.0033 12  TYR C CZ  
2712 O OH  . TYR C 13  ? 0.2757 0.2868 0.3202 0.0201  -0.0264 -0.0025 12  TYR C OH  
2713 N N   . ALA C 14  ? 0.2273 0.2335 0.2509 0.0199  0.0046  -0.0024 13  ALA C N   
2714 C CA  . ALA C 14  ? 0.2267 0.2271 0.2427 0.0215  0.0097  -0.0012 13  ALA C CA  
2715 C C   . ALA C 14  ? 0.2858 0.2870 0.3067 0.0149  0.0126  0.0011  13  ALA C C   
2716 O O   . ALA C 14  ? 0.2149 0.2128 0.2332 0.0152  0.0186  0.0040  13  ALA C O   
2717 C CB  . ALA C 14  ? 0.2562 0.2491 0.2621 0.0244  0.0059  -0.0037 13  ALA C CB  
2718 N N   . CYS C 15  ? 0.2232 0.2272 0.2499 0.0092  0.0081  -0.0002 14  CYS C N   
2719 C CA  . CYS C 15  ? 0.2392 0.2409 0.2685 0.0033  0.0085  0.0006  14  CYS C CA  
2720 C C   . CYS C 15  ? 0.2626 0.2709 0.3046 -0.0014 0.0110  0.0035  14  CYS C C   
2721 O O   . CYS C 15  ? 0.3051 0.3226 0.3551 0.0004  0.0121  0.0047  14  CYS C O   
2722 C CB  . CYS C 15  ? 0.2433 0.2449 0.2719 0.0007  0.0023  -0.0022 14  CYS C CB  
2723 S SG  . CYS C 15  ? 0.2405 0.2372 0.2575 0.0053  0.0003  -0.0042 14  CYS C SG  
2724 O OXT . CYS C 15  ? 0.2533 0.2580 0.2985 -0.0069 0.0115  0.0048  14  CYS C OXT 
2725 C C   . ACE D 1   ? 0.2071 0.2258 0.2111 0.0233  0.0119  0.0081  0   ACE D C   
2726 O O   . ACE D 1   ? 0.2677 0.2957 0.2805 0.0208  0.0014  0.0039  0   ACE D O   
2727 C CH3 . ACE D 1   ? 0.2017 0.2226 0.2122 0.0253  0.0238  0.0075  0   ACE D CH3 
2728 N N   . DTY D 2   ? 0.1844 0.1889 0.1713 0.0248  0.0135  0.0126  1   DTY D N   
2729 C CA  . DTY D 2   ? 0.1866 0.1877 0.1667 0.0256  -0.0007 0.0119  1   DTY D CA  
2730 C C   . DTY D 2   ? 0.2282 0.2042 0.1711 0.0301  -0.0041 0.0128  1   DTY D C   
2731 O O   . DTY D 2   ? 0.2461 0.2039 0.1688 0.0318  0.0083  0.0189  1   DTY D O   
2732 C CB  . DTY D 2   ? 0.1927 0.1963 0.1855 0.0250  0.0007  0.0167  1   DTY D CB  
2733 C CG  . DTY D 2   ? 0.1894 0.1881 0.1754 0.0278  -0.0147 0.0156  1   DTY D CG  
2734 C CD1 . DTY D 2   ? 0.2185 0.1940 0.1815 0.0315  -0.0143 0.0218  1   DTY D CD1 
2735 C CD2 . DTY D 2   ? 0.1757 0.1917 0.1779 0.0271  -0.0293 0.0074  1   DTY D CD2 
2736 C CE1 . DTY D 2   ? 0.2285 0.1976 0.1843 0.0364  -0.0308 0.0197  1   DTY D CE1 
2737 C CE2 . DTY D 2   ? 0.1812 0.1956 0.1813 0.0311  -0.0446 0.0038  1   DTY D CE2 
2738 C CZ  . DTY D 2   ? 0.2059 0.1967 0.1826 0.0367  -0.0468 0.0099  1   DTY D CZ  
2739 O OH  . DTY D 2   ? 0.2158 0.2029 0.1889 0.0429  -0.0643 0.0054  1   DTY D OH  
2740 N N   . GLN D 3   ? 0.2334 0.2084 0.1680 0.0322  -0.0199 0.0060  2   GLN D N   
2741 C CA  . GLN D 3   ? 0.2637 0.2143 0.1616 0.0386  -0.0267 0.0050  2   GLN D CA  
2742 C C   . GLN D 3   ? 0.2722 0.2182 0.1573 0.0384  -0.0249 -0.0004 2   GLN D C   
2743 O O   . GLN D 3   ? 0.2517 0.2138 0.1562 0.0335  -0.0276 -0.0072 2   GLN D O   
2744 C CB  . GLN D 3   ? 0.2689 0.2208 0.1657 0.0431  -0.0477 -0.0021 2   GLN D CB  
2745 C CG  . GLN D 3   ? 0.2668 0.2184 0.1714 0.0451  -0.0516 0.0029  2   GLN D CG  
2746 C CD  . GLN D 3   ? 0.2972 0.2500 0.2008 0.0519  -0.0744 -0.0062 2   GLN D CD  
2747 O OE1 . GLN D 3   ? 0.3122 0.2844 0.2343 0.0502  -0.0858 -0.0186 2   GLN D OE1 
2748 N NE2 . GLN D 3   ? 0.3568 0.2871 0.2378 0.0598  -0.0809 -0.0010 2   GLN D NE2 
2749 N N   . PHE D 4   ? 0.3066 0.2277 0.1565 0.0435  -0.0192 0.0027  3   PHE D N   
2750 C CA  . PHE D 4   ? 0.3198 0.2330 0.1536 0.0445  -0.0175 -0.0026 3   PHE D CA  
2751 C C   . PHE D 4   ? 0.3736 0.2556 0.1630 0.0519  -0.0128 0.0016  3   PHE D C   
2752 O O   . PHE D 4   ? 0.3809 0.2490 0.1565 0.0531  -0.0019 0.0109  3   PHE D O   
2753 C CB  . PHE D 4   ? 0.2994 0.2244 0.1522 0.0395  -0.0023 -0.0015 3   PHE D CB  
2754 C CG  . PHE D 4   ? 0.3051 0.2272 0.1595 0.0393  0.0166  0.0071  3   PHE D CG  
2755 C CD1 . PHE D 4   ? 0.2809 0.2192 0.1638 0.0356  0.0210  0.0113  3   PHE D CD1 
2756 C CD2 . PHE D 4   ? 0.3299 0.2339 0.1587 0.0425  0.0306  0.0093  3   PHE D CD2 
2757 C CE1 . PHE D 4   ? 0.3429 0.2807 0.2319 0.0344  0.0388  0.0168  3   PHE D CE1 
2758 C CE2 . PHE D 4   ? 0.3725 0.2762 0.2068 0.0408  0.0500  0.0149  3   PHE D CE2 
2759 C CZ  . PHE D 4   ? 0.3890 0.3102 0.2549 0.0364  0.0541  0.0182  3   PHE D CZ  
2760 N N   . GLU D 5   ? 0.4322 0.3018 0.1981 0.0563  -0.0206 -0.0057 4   GLU D N   
2761 C CA  . GLU D 5   ? 0.5040 0.3425 0.2241 0.0635  -0.0142 -0.0026 4   GLU D CA  
2762 C C   . GLU D 5   ? 0.4777 0.3157 0.1980 0.0604  0.0077  0.0005  4   GLU D C   
2763 O O   . GLU D 5   ? 0.4351 0.2938 0.1857 0.0550  0.0118  -0.0030 4   GLU D O   
2764 C CB  . GLU D 5   ? 0.5122 0.3385 0.2081 0.0705  -0.0330 -0.0137 4   GLU D CB  
2765 C CG  . GLU D 5   ? 0.5316 0.3656 0.2368 0.0740  -0.0574 -0.0219 4   GLU D CG  
2766 C CD  . GLU D 5   ? 0.8762 0.6790 0.5371 0.0865  -0.0692 -0.0199 4   GLU D CD  
2767 O OE1 . GLU D 5   ? 0.9499 0.7221 0.5671 0.0922  -0.0589 -0.0135 4   GLU D OE1 
2768 O OE2 . GLU D 5   ? 1.0199 0.8274 0.6878 0.0913  -0.0888 -0.0254 4   GLU D OE2 
2769 N N   . GLN D 6   ? 0.5145 0.3266 0.1985 0.0644  0.0221  0.0063  5   GLN D N   
2770 C CA  . GLN D 6   ? 0.5703 0.3849 0.2589 0.0615  0.0448  0.0079  5   GLN D CA  
2771 C C   . GLN D 6   ? 0.5339 0.3518 0.2221 0.0633  0.0420  -0.0014 5   GLN D C   
2772 O O   . GLN D 6   ? 0.5354 0.3639 0.2406 0.0612  0.0564  -0.0029 5   GLN D O   
2773 C CB  . GLN D 6   ? 0.6815 0.4669 0.3307 0.0640  0.0635  0.0153  5   GLN D CB  
2774 C CG  . GLN D 6   ? 0.8550 0.6361 0.5082 0.0600  0.0710  0.0251  5   GLN D CG  
2775 C CD  . GLN D 6   ? 0.9463 0.7078 0.5783 0.0569  0.0993  0.0319  5   GLN D CD  
2776 O OE1 . GLN D 6   ? 0.9682 0.7492 0.6339 0.0493  0.1179  0.0325  5   GLN D OE1 
2777 N NE2 . GLN D 6   ? 0.9465 0.6741 0.5333 0.0615  0.1003  0.0349  5   GLN D NE2 
2778 N N   . TRP D 7   ? 0.4799 0.2895 0.1515 0.0676  0.0231  -0.0092 6   TRP D N   
2779 C CA  . TRP D 7   ? 0.4785 0.2902 0.1514 0.0681  0.0188  -0.0190 6   TRP D CA  
2780 C C   . TRP D 7   ? 0.4907 0.3270 0.2033 0.0611  0.0079  -0.0250 6   TRP D C   
2781 O O   . TRP D 7   ? 0.4374 0.2741 0.1532 0.0600  0.0054  -0.0327 6   TRP D O   
2782 C CB  . TRP D 7   ? 0.5421 0.3298 0.1746 0.0762  0.0048  -0.0263 6   TRP D CB  
2783 C CG  . TRP D 7   ? 0.5570 0.3464 0.1901 0.0782  -0.0184 -0.0308 6   TRP D CG  
2784 C CD1 . TRP D 7   ? 0.5907 0.3663 0.2028 0.0839  -0.0253 -0.0255 6   TRP D CD1 
2785 C CD2 . TRP D 7   ? 0.4987 0.3048 0.1564 0.0746  -0.0374 -0.0431 6   TRP D CD2 
2786 N NE1 . TRP D 7   ? 0.5858 0.3707 0.2098 0.0856  -0.0495 -0.0348 6   TRP D NE1 
2787 C CE2 . TRP D 7   ? 0.5440 0.3494 0.1980 0.0791  -0.0561 -0.0462 6   TRP D CE2 
2788 C CE3 . TRP D 7   ? 0.5686 0.3885 0.2507 0.0677  -0.0396 -0.0523 6   TRP D CE3 
2789 C CZ2 . TRP D 7   ? 0.5490 0.3719 0.2278 0.0764  -0.0762 -0.0600 6   TRP D CZ2 
2790 C CZ3 . TRP D 7   ? 0.5964 0.4304 0.3002 0.0633  -0.0576 -0.0645 6   TRP D CZ3 
2791 C CH2 . TRP D 7   ? 0.5597 0.3976 0.2643 0.0673  -0.0753 -0.0691 6   TRP D CH2 
2792 N N   . HIS D 8   ? 0.4159 0.2702 0.1564 0.0561  0.0026  -0.0217 7   HIS D N   
2793 C CA  . HIS D 8   ? 0.3801 0.2555 0.1550 0.0486  -0.0054 -0.0271 7   HIS D CA  
2794 C C   . HIS D 8   ? 0.3872 0.2719 0.1821 0.0453  0.0077  -0.0251 7   HIS D C   
2795 O O   . HIS D 8   ? 0.3792 0.2638 0.1749 0.0478  0.0226  -0.0192 7   HIS D O   
2796 C CB  . HIS D 8   ? 0.3622 0.2548 0.1613 0.0447  -0.0130 -0.0242 7   HIS D CB  
2797 C CG  . HIS D 8   ? 0.4265 0.3166 0.2175 0.0474  -0.0322 -0.0312 7   HIS D CG  
2798 N ND1 . HIS D 8   ? 0.3589 0.2635 0.1699 0.0456  -0.0417 -0.0312 7   HIS D ND1 
2799 C CD2 . HIS D 8   ? 0.4054 0.2811 0.1718 0.0530  -0.0451 -0.0403 7   HIS D CD2 
2800 C CE1 . HIS D 8   ? 0.4189 0.3190 0.2193 0.0503  -0.0599 -0.0405 7   HIS D CE1 
2801 N NE2 . HIS D 8   ? 0.4515 0.3340 0.2247 0.0550  -0.0628 -0.0463 7   HIS D NE2 
2802 N N   . ILE D 9   ? 0.3419 0.2341 0.1536 0.0396  0.0018  -0.0313 8   ILE D N   
2803 C CA  . ILE D 9   ? 0.3415 0.2393 0.1699 0.0377  0.0107  -0.0299 8   ILE D CA  
2804 C C   . ILE D 9   ? 0.3372 0.2518 0.1894 0.0372  0.0176  -0.0222 8   ILE D C   
2805 O O   . ILE D 9   ? 0.3262 0.2435 0.1858 0.0409  0.0284  -0.0197 8   ILE D O   
2806 C CB  . ILE D 9   ? 0.3192 0.2179 0.1578 0.0302  0.0030  -0.0368 8   ILE D CB  
2807 C CG1 . ILE D 9   ? 0.3812 0.2631 0.1989 0.0302  -0.0029 -0.0462 8   ILE D CG1 
2808 C CG2 . ILE D 9   ? 0.3218 0.2220 0.1730 0.0299  0.0104  -0.0343 8   ILE D CG2 
2809 C CD1 . ILE D 9   ? 0.3914 0.2746 0.2202 0.0198  -0.0109 -0.0550 8   ILE D CD1 
2810 N N   . ARG D 10  ? 0.2850 0.2121 0.1516 0.0331  0.0106  -0.0200 9   ARG D N   
2811 C CA  . ARG D 10  ? 0.2620 0.2052 0.1519 0.0323  0.0157  -0.0135 9   ARG D CA  
2812 C C   . ARG D 10  ? 0.3122 0.2521 0.1965 0.0373  0.0289  -0.0079 9   ARG D C   
2813 O O   . ARG D 10  ? 0.2845 0.2369 0.1900 0.0376  0.0371  -0.0050 9   ARG D O   
2814 C CB  . ARG D 10  ? 0.2890 0.2433 0.1908 0.0282  0.0049  -0.0132 9   ARG D CB  
2815 C CG  . ARG D 10  ? 0.2804 0.2492 0.2036 0.0277  0.0088  -0.0068 9   ARG D CG  
2816 C CD  . ARG D 10  ? 0.2875 0.2712 0.2298 0.0228  -0.0025 -0.0091 9   ARG D CD  
2817 N NE  . ARG D 10  ? 0.2893 0.2825 0.2482 0.0178  -0.0030 -0.0125 9   ARG D NE  
2818 C CZ  . ARG D 10  ? 0.2862 0.2939 0.2644 0.0127  -0.0086 -0.0147 9   ARG D CZ  
2819 N NH1 . ARG D 10  ? 0.2020 0.2191 0.1890 0.0122  -0.0163 -0.0154 9   ARG D NH1 
2820 N NH2 . ARG D 10  ? 0.2123 0.2230 0.1991 0.0087  -0.0064 -0.0166 9   ARG D NH2 
2821 N N   . GLY D 11  ? 0.3382 0.2608 0.1938 0.0410  0.0321  -0.0072 10  GLY D N   
2822 C CA  . GLY D 11  ? 0.3509 0.2677 0.1987 0.0438  0.0483  -0.0024 10  GLY D CA  
2823 C C   . GLY D 11  ? 0.3441 0.2653 0.2015 0.0467  0.0618  -0.0056 10  GLY D C   
2824 O O   . GLY D 11  ? 0.3856 0.3097 0.2489 0.0473  0.0774  -0.0035 10  GLY D O   
2825 N N   . ARG D 12  ? 0.3095 0.2310 0.1700 0.0484  0.0565  -0.0114 11  ARG D N   
2826 C CA  . ARG D 12  ? 0.3552 0.2788 0.2229 0.0536  0.0666  -0.0162 11  ARG D CA  
2827 C C   . ARG D 12  ? 0.3066 0.2500 0.2087 0.0545  0.0675  -0.0172 11  ARG D C   
2828 O O   . ARG D 12  ? 0.2982 0.2466 0.2113 0.0605  0.0753  -0.0225 11  ARG D O   
2829 C CB  . ARG D 12  ? 0.3729 0.2821 0.2233 0.0565  0.0597  -0.0224 11  ARG D CB  
2830 C CG  . ARG D 12  ? 0.4638 0.3531 0.2796 0.0583  0.0601  -0.0242 11  ARG D CG  
2831 C CD  . ARG D 12  ? 0.5981 0.4733 0.3989 0.0626  0.0580  -0.0318 11  ARG D CD  
2832 N NE  . ARG D 12  ? 0.6455 0.5120 0.4376 0.0581  0.0428  -0.0352 11  ARG D NE  
2833 C CZ  . ARG D 12  ? 0.5949 0.4607 0.3976 0.0552  0.0362  -0.0384 11  ARG D CZ  
2834 N NH1 . ARG D 12  ? 0.5385 0.4095 0.3573 0.0588  0.0408  -0.0382 11  ARG D NH1 
2835 N NH2 . ARG D 12  ? 0.5767 0.4348 0.3728 0.0489  0.0248  -0.0427 11  ARG D NH2 
2836 N N   . TYR D 13  ? 0.2788 0.2339 0.1983 0.0498  0.0592  -0.0134 12  TYR D N   
2837 C CA  . TYR D 13  ? 0.2554 0.2252 0.2018 0.0515  0.0553  -0.0152 12  TYR D CA  
2838 C C   . TYR D 13  ? 0.2220 0.2100 0.1935 0.0489  0.0596  -0.0118 12  TYR D C   
2839 O O   . TYR D 13  ? 0.2566 0.2450 0.2270 0.0476  0.0712  -0.0099 12  TYR D O   
2840 C CB  . TYR D 13  ? 0.2342 0.1986 0.1761 0.0479  0.0418  -0.0153 12  TYR D CB  
2841 C CG  . TYR D 13  ? 0.3151 0.2594 0.2332 0.0492  0.0386  -0.0196 12  TYR D CG  
2842 C CD1 . TYR D 13  ? 0.2957 0.2313 0.2058 0.0573  0.0449  -0.0243 12  TYR D CD1 
2843 C CD2 . TYR D 13  ? 0.3062 0.2409 0.2122 0.0421  0.0295  -0.0204 12  TYR D CD2 
2844 C CE1 . TYR D 13  ? 0.3375 0.2527 0.2252 0.0586  0.0415  -0.0286 12  TYR D CE1 
2845 C CE2 . TYR D 13  ? 0.2973 0.2126 0.1829 0.0421  0.0271  -0.0252 12  TYR D CE2 
2846 C CZ  . TYR D 13  ? 0.3475 0.2519 0.2229 0.0505  0.0328  -0.0287 12  TYR D CZ  
2847 O OH  . TYR D 13  ? 0.3556 0.2390 0.2103 0.0506  0.0299  -0.0338 12  TYR D OH  
2848 N N   . ALA D 14  ? 0.2156 0.2171 0.2092 0.0484  0.0521  -0.0119 13  ALA D N   
2849 C CA  . ALA D 14  ? 0.2599 0.2800 0.2814 0.0472  0.0560  -0.0109 13  ALA D CA  
2850 C C   . ALA D 14  ? 0.2719 0.2902 0.2882 0.0404  0.0598  -0.0044 13  ALA D C   
2851 O O   . ALA D 14  ? 0.2442 0.2723 0.2785 0.0386  0.0689  -0.0038 13  ALA D O   
2852 C CB  . ALA D 14  ? 0.1705 0.2017 0.2099 0.0477  0.0446  -0.0116 13  ALA D CB  
2853 N N   . CYS D 15  ? 0.2216 0.2266 0.2141 0.0369  0.0523  -0.0005 14  CYS D N   
2854 C CA  . CYS D 15  ? 0.2811 0.2805 0.2648 0.0328  0.0528  0.0053  14  CYS D CA  
2855 C C   . CYS D 15  ? 0.3269 0.3112 0.2906 0.0334  0.0675  0.0078  14  CYS D C   
2856 O O   . CYS D 15  ? 0.3737 0.3506 0.3254 0.0366  0.0761  0.0045  14  CYS D O   
2857 C CB  . CYS D 15  ? 0.2377 0.2284 0.2033 0.0309  0.0383  0.0060  14  CYS D CB  
2858 S SG  . CYS D 15  ? 0.2550 0.2630 0.2437 0.0275  0.0244  0.0031  14  CYS D SG  
2859 O OXT . CYS D 15  ? 0.2845 0.2614 0.2411 0.0305  0.0714  0.0132  14  CYS D OXT 
# 
