data_8YNX
# 
_entry.id   8YNX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8YNX         pdb_00008ynx 10.2210/pdb8ynx/pdb 
WWPDB D_1300046013 ?            ?                   
# 
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 2025-03-19 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.journal_volume'          
7  2 'Structure model' '_citation.page_first'              
8  2 'Structure model' '_citation.page_last'               
9  2 'Structure model' '_citation.pdbx_database_id_DOI'    
10 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
11 2 'Structure model' '_citation.title'                   
12 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YNX 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              shannon-au@cuhk.edu.hk 
_pdbx_contact_author.name_first         'Shannon Wing Ngor' 
_pdbx_contact_author.name_last          Au 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3573-9273 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mok, C.Y.'  1 0009-0001-9314-9431 
'Au, S.W.N.' 2 0000-0002-3573-9273 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            32 
_citation.language                  ? 
_citation.page_first                1725 
_citation.page_last                 1736.e4 
_citation.title                     
'Structural insights into the assembly pathway of the Helicobacter pylori CagT4SS outer membrane core complex.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2024.06.019 
_citation.pdbx_database_id_PubMed   39032488 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mok, C.Y.'   1 ? 
primary 'Chu, H.Y.'   2 ? 
primary 'Lam, W.W.L.' 3 ? 
primary 'Au, S.W.N.'  4 ? 
# 
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 'Cag pathogenicity island protein 3' 24692.014 1  ? ? ? ? 
2 polymer man 'Cag pathogenicity island protein T' 13754.686 1  ? ? ? ? 
3 water   nat water                                18.015    22 ? ? ? ? 
# 
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 
;GPLGSKEISEADKVIKATKETKETKKEVKRLKKEAKQRQQIPDHKKPQYASVDDTKTQALFDIYDTLNVNDKSFGDWFGN
SALKDKTYLYAMDLLDYNNYLSIENPIIKTRAMGTYADLIIITGSLEQVNGYYNILKALNKRNAKFVLKINENMPYAQAT
FLRVPKRSDPNAHTLDKGASIDENKLFEQQKRAYFNYANDVICRPNDEVCSPLRD
;
;GPLGSKEISEADKVIKATKETKETKKEVKRLKKEAKQRQQIPDHKKPQYASVDDTKTQALFDIYDTLNVNDKSFGDWFGN
SALKDKTYLYAMDLLDYNNYLSIENPIIKTRAMGTYADLIIITGSLEQVNGYYNILKALNKRNAKFVLKINENMPYAQAT
FLRVPKRSDPNAHTLDKGASIDENKLFEQQKRAYFNYANDVICRPNDEVCSPLRD
;
A ? 
2 'polypeptide(L)' no no 
;HHHHHHMDKLKDTPFMVQVKLPNYKDYLLDNKQVVLTFKLVHHSKKITLIGDANKILQYKNYFQANGARSDIDFYLQPTL
NQKGVVMIASNYNDNPNSKEKPQTFDVLQGSQPMLGANT
;
;HHHHHHMDKLKDTPFMVQVKLPNYKDYLLDNKQVVLTFKLVHHSKKITLIGDANKILQYKNYFQANGARSDIDFYLQPTL
NQKGVVMIASNYNDNPNSKEKPQTFDVLQGSQPMLGANT
;
B ? 
# 
_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   GLY n 
1 2   PRO n 
1 3   LEU n 
1 4   GLY n 
1 5   SER n 
1 6   LYS n 
1 7   GLU n 
1 8   ILE n 
1 9   SER n 
1 10  GLU n 
1 11  ALA n 
1 12  ASP n 
1 13  LYS n 
1 14  VAL n 
1 15  ILE n 
1 16  LYS n 
1 17  ALA n 
1 18  THR n 
1 19  LYS n 
1 20  GLU n 
1 21  THR n 
1 22  LYS n 
1 23  GLU n 
1 24  THR n 
1 25  LYS n 
1 26  LYS n 
1 27  GLU n 
1 28  VAL n 
1 29  LYS n 
1 30  ARG n 
1 31  LEU n 
1 32  LYS n 
1 33  LYS n 
1 34  GLU n 
1 35  ALA n 
1 36  LYS n 
1 37  GLN n 
1 38  ARG n 
1 39  GLN n 
1 40  GLN n 
1 41  ILE n 
1 42  PRO n 
1 43  ASP n 
1 44  HIS n 
1 45  LYS n 
1 46  LYS n 
1 47  PRO n 
1 48  GLN n 
1 49  TYR n 
1 50  ALA n 
1 51  SER n 
1 52  VAL n 
1 53  ASP n 
1 54  ASP n 
1 55  THR n 
1 56  LYS n 
1 57  THR n 
1 58  GLN n 
1 59  ALA n 
1 60  LEU n 
1 61  PHE n 
1 62  ASP n 
1 63  ILE n 
1 64  TYR n 
1 65  ASP n 
1 66  THR n 
1 67  LEU n 
1 68  ASN n 
1 69  VAL n 
1 70  ASN n 
1 71  ASP n 
1 72  LYS n 
1 73  SER n 
1 74  PHE n 
1 75  GLY n 
1 76  ASP n 
1 77  TRP n 
1 78  PHE n 
1 79  GLY n 
1 80  ASN n 
1 81  SER n 
1 82  ALA n 
1 83  LEU n 
1 84  LYS n 
1 85  ASP n 
1 86  LYS n 
1 87  THR n 
1 88  TYR n 
1 89  LEU n 
1 90  TYR n 
1 91  ALA n 
1 92  MET n 
1 93  ASP n 
1 94  LEU n 
1 95  LEU n 
1 96  ASP n 
1 97  TYR n 
1 98  ASN n 
1 99  ASN n 
1 100 TYR n 
1 101 LEU n 
1 102 SER n 
1 103 ILE n 
1 104 GLU n 
1 105 ASN n 
1 106 PRO n 
1 107 ILE n 
1 108 ILE n 
1 109 LYS n 
1 110 THR n 
1 111 ARG n 
1 112 ALA n 
1 113 MET n 
1 114 GLY n 
1 115 THR n 
1 116 TYR n 
1 117 ALA n 
1 118 ASP n 
1 119 LEU n 
1 120 ILE n 
1 121 ILE n 
1 122 ILE n 
1 123 THR n 
1 124 GLY n 
1 125 SER n 
1 126 LEU n 
1 127 GLU n 
1 128 GLN n 
1 129 VAL n 
1 130 ASN n 
1 131 GLY n 
1 132 TYR n 
1 133 TYR n 
1 134 ASN n 
1 135 ILE n 
1 136 LEU n 
1 137 LYS n 
1 138 ALA n 
1 139 LEU n 
1 140 ASN n 
1 141 LYS n 
1 142 ARG n 
1 143 ASN n 
1 144 ALA n 
1 145 LYS n 
1 146 PHE n 
1 147 VAL n 
1 148 LEU n 
1 149 LYS n 
1 150 ILE n 
1 151 ASN n 
1 152 GLU n 
1 153 ASN n 
1 154 MET n 
1 155 PRO n 
1 156 TYR n 
1 157 ALA n 
1 158 GLN n 
1 159 ALA n 
1 160 THR n 
1 161 PHE n 
1 162 LEU n 
1 163 ARG n 
1 164 VAL n 
1 165 PRO n 
1 166 LYS n 
1 167 ARG n 
1 168 SER n 
1 169 ASP n 
1 170 PRO n 
1 171 ASN n 
1 172 ALA n 
1 173 HIS n 
1 174 THR n 
1 175 LEU n 
1 176 ASP n 
1 177 LYS n 
1 178 GLY n 
1 179 ALA n 
1 180 SER n 
1 181 ILE n 
1 182 ASP n 
1 183 GLU n 
1 184 ASN n 
1 185 LYS n 
1 186 LEU n 
1 187 PHE n 
1 188 GLU n 
1 189 GLN n 
1 190 GLN n 
1 191 LYS n 
1 192 ARG n 
1 193 ALA n 
1 194 TYR n 
1 195 PHE n 
1 196 ASN n 
1 197 TYR n 
1 198 ALA n 
1 199 ASN n 
1 200 ASP n 
1 201 VAL n 
1 202 ILE n 
1 203 CYS n 
1 204 ARG n 
1 205 PRO n 
1 206 ASN n 
1 207 ASP n 
1 208 GLU n 
1 209 VAL n 
1 210 CYS n 
1 211 SER n 
1 212 PRO n 
1 213 LEU n 
1 214 ARG n 
1 215 ASP n 
2 1   HIS n 
2 2   HIS n 
2 3   HIS n 
2 4   HIS n 
2 5   HIS n 
2 6   HIS n 
2 7   MET n 
2 8   ASP n 
2 9   LYS n 
2 10  LEU n 
2 11  LYS n 
2 12  ASP n 
2 13  THR n 
2 14  PRO n 
2 15  PHE n 
2 16  MET n 
2 17  VAL n 
2 18  GLN n 
2 19  VAL n 
2 20  LYS n 
2 21  LEU n 
2 22  PRO n 
2 23  ASN n 
2 24  TYR n 
2 25  LYS n 
2 26  ASP n 
2 27  TYR n 
2 28  LEU n 
2 29  LEU n 
2 30  ASP n 
2 31  ASN n 
2 32  LYS n 
2 33  GLN n 
2 34  VAL n 
2 35  VAL n 
2 36  LEU n 
2 37  THR n 
2 38  PHE n 
2 39  LYS n 
2 40  LEU n 
2 41  VAL n 
2 42  HIS n 
2 43  HIS n 
2 44  SER n 
2 45  LYS n 
2 46  LYS n 
2 47  ILE n 
2 48  THR n 
2 49  LEU n 
2 50  ILE n 
2 51  GLY n 
2 52  ASP n 
2 53  ALA n 
2 54  ASN n 
2 55  LYS n 
2 56  ILE n 
2 57  LEU n 
2 58  GLN n 
2 59  TYR n 
2 60  LYS n 
2 61  ASN n 
2 62  TYR n 
2 63  PHE n 
2 64  GLN n 
2 65  ALA n 
2 66  ASN n 
2 67  GLY n 
2 68  ALA n 
2 69  ARG n 
2 70  SER n 
2 71  ASP n 
2 72  ILE n 
2 73  ASP n 
2 74  PHE n 
2 75  TYR n 
2 76  LEU n 
2 77  GLN n 
2 78  PRO n 
2 79  THR n 
2 80  LEU n 
2 81  ASN n 
2 82  GLN n 
2 83  LYS n 
2 84  GLY n 
2 85  VAL n 
2 86  VAL n 
2 87  MET n 
2 88  ILE n 
2 89  ALA n 
2 90  SER n 
2 91  ASN n 
2 92  TYR n 
2 93  ASN n 
2 94  ASP n 
2 95  ASN n 
2 96  PRO n 
2 97  ASN n 
2 98  SER n 
2 99  LYS n 
2 100 GLU n 
2 101 LYS n 
2 102 PRO n 
2 103 GLN n 
2 104 THR n 
2 105 PHE n 
2 106 ASP n 
2 107 VAL n 
2 108 LEU n 
2 109 GLN n 
2 110 GLY n 
2 111 SER n 
2 112 GLN n 
2 113 PRO n 
2 114 MET n 
2 115 LEU n 
2 116 GLY n 
2 117 ALA n 
2 118 ASN n 
2 119 THR n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 215 ? ? 'cag3, HPG27_481' ? G27 ? ? ? ? 'Helicobacter pylori (strain G27)' 563041 ? ? ? ? ? ? ? 
? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 119 ? ? 'cagT, HPG27_491' ? G27 ? ? ? ? 'Helicobacter pylori (strain G27)' 563041 ? ? ? ? ? ? ? 
? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
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   GLY 1   18  ?   ?   ?   A . n 
A 1 2   PRO 2   19  ?   ?   ?   A . n 
A 1 3   LEU 3   20  ?   ?   ?   A . n 
A 1 4   GLY 4   21  ?   ?   ?   A . n 
A 1 5   SER 5   22  ?   ?   ?   A . n 
A 1 6   LYS 6   23  ?   ?   ?   A . n 
A 1 7   GLU 7   24  ?   ?   ?   A . n 
A 1 8   ILE 8   25  ?   ?   ?   A . n 
A 1 9   SER 9   26  ?   ?   ?   A . n 
A 1 10  GLU 10  27  ?   ?   ?   A . n 
A 1 11  ALA 11  28  ?   ?   ?   A . n 
A 1 12  ASP 12  29  ?   ?   ?   A . n 
A 1 13  LYS 13  30  ?   ?   ?   A . n 
A 1 14  VAL 14  31  ?   ?   ?   A . n 
A 1 15  ILE 15  32  ?   ?   ?   A . n 
A 1 16  LYS 16  33  ?   ?   ?   A . n 
A 1 17  ALA 17  34  ?   ?   ?   A . n 
A 1 18  THR 18  35  ?   ?   ?   A . n 
A 1 19  LYS 19  36  ?   ?   ?   A . n 
A 1 20  GLU 20  37  ?   ?   ?   A . n 
A 1 21  THR 21  38  ?   ?   ?   A . n 
A 1 22  LYS 22  39  ?   ?   ?   A . n 
A 1 23  GLU 23  40  ?   ?   ?   A . n 
A 1 24  THR 24  41  ?   ?   ?   A . n 
A 1 25  LYS 25  42  ?   ?   ?   A . n 
A 1 26  LYS 26  43  ?   ?   ?   A . n 
A 1 27  GLU 27  44  ?   ?   ?   A . n 
A 1 28  VAL 28  45  ?   ?   ?   A . n 
A 1 29  LYS 29  46  ?   ?   ?   A . n 
A 1 30  ARG 30  47  ?   ?   ?   A . n 
A 1 31  LEU 31  48  ?   ?   ?   A . n 
A 1 32  LYS 32  49  ?   ?   ?   A . n 
A 1 33  LYS 33  50  ?   ?   ?   A . n 
A 1 34  GLU 34  51  ?   ?   ?   A . n 
A 1 35  ALA 35  52  ?   ?   ?   A . n 
A 1 36  LYS 36  53  ?   ?   ?   A . n 
A 1 37  GLN 37  54  ?   ?   ?   A . n 
A 1 38  ARG 38  55  ?   ?   ?   A . n 
A 1 39  GLN 39  56  ?   ?   ?   A . n 
A 1 40  GLN 40  57  57  GLN GLN A . n 
A 1 41  ILE 41  58  58  ILE ILE A . n 
A 1 42  PRO 42  59  59  PRO PRO A . n 
A 1 43  ASP 43  60  60  ASP ASP A . n 
A 1 44  HIS 44  61  61  HIS HIS A . n 
A 1 45  LYS 45  62  62  LYS LYS A . n 
A 1 46  LYS 46  63  63  LYS LYS A . n 
A 1 47  PRO 47  64  64  PRO PRO A . n 
A 1 48  GLN 48  65  65  GLN GLN A . n 
A 1 49  TYR 49  66  66  TYR TYR A . n 
A 1 50  ALA 50  67  67  ALA ALA A . n 
A 1 51  SER 51  68  68  SER SER A . n 
A 1 52  VAL 52  69  69  VAL VAL A . n 
A 1 53  ASP 53  70  70  ASP ASP A . n 
A 1 54  ASP 54  71  71  ASP ASP A . n 
A 1 55  THR 55  72  72  THR THR A . n 
A 1 56  LYS 56  73  73  LYS LYS A . n 
A 1 57  THR 57  74  74  THR THR A . n 
A 1 58  GLN 58  75  75  GLN GLN A . n 
A 1 59  ALA 59  76  76  ALA ALA A . n 
A 1 60  LEU 60  77  77  LEU LEU A . n 
A 1 61  PHE 61  78  78  PHE PHE A . n 
A 1 62  ASP 62  79  79  ASP ASP A . n 
A 1 63  ILE 63  80  80  ILE ILE A . n 
A 1 64  TYR 64  81  81  TYR TYR A . n 
A 1 65  ASP 65  82  82  ASP ASP A . n 
A 1 66  THR 66  83  83  THR THR A . n 
A 1 67  LEU 67  84  84  LEU LEU A . n 
A 1 68  ASN 68  85  85  ASN ASN A . n 
A 1 69  VAL 69  86  86  VAL VAL A . n 
A 1 70  ASN 70  87  87  ASN ASN A . n 
A 1 71  ASP 71  88  88  ASP ASP A . n 
A 1 72  LYS 72  89  89  LYS LYS A . n 
A 1 73  SER 73  90  90  SER SER A . n 
A 1 74  PHE 74  91  91  PHE PHE A . n 
A 1 75  GLY 75  92  92  GLY GLY A . n 
A 1 76  ASP 76  93  93  ASP ASP A . n 
A 1 77  TRP 77  94  94  TRP TRP A . n 
A 1 78  PHE 78  95  95  PHE PHE A . n 
A 1 79  GLY 79  96  96  GLY GLY A . n 
A 1 80  ASN 80  97  97  ASN ASN A . n 
A 1 81  SER 81  98  98  SER SER A . n 
A 1 82  ALA 82  99  99  ALA ALA A . n 
A 1 83  LEU 83  100 100 LEU LEU A . n 
A 1 84  LYS 84  101 101 LYS LYS A . n 
A 1 85  ASP 85  102 102 ASP ASP A . n 
A 1 86  LYS 86  103 103 LYS LYS A . n 
A 1 87  THR 87  104 104 THR THR A . n 
A 1 88  TYR 88  105 105 TYR TYR A . n 
A 1 89  LEU 89  106 106 LEU LEU A . n 
A 1 90  TYR 90  107 107 TYR TYR A . n 
A 1 91  ALA 91  108 108 ALA ALA A . n 
A 1 92  MET 92  109 109 MET MET A . n 
A 1 93  ASP 93  110 110 ASP ASP A . n 
A 1 94  LEU 94  111 111 LEU LEU A . n 
A 1 95  LEU 95  112 112 LEU LEU A . n 
A 1 96  ASP 96  113 113 ASP ASP A . n 
A 1 97  TYR 97  114 114 TYR TYR A . n 
A 1 98  ASN 98  115 115 ASN ASN A . n 
A 1 99  ASN 99  116 116 ASN ASN A . n 
A 1 100 TYR 100 117 117 TYR TYR A . n 
A 1 101 LEU 101 118 118 LEU LEU A . n 
A 1 102 SER 102 119 119 SER SER A . n 
A 1 103 ILE 103 120 120 ILE ILE A . n 
A 1 104 GLU 104 121 121 GLU GLU A . n 
A 1 105 ASN 105 122 122 ASN ASN A . n 
A 1 106 PRO 106 123 123 PRO PRO A . n 
A 1 107 ILE 107 124 124 ILE ILE A . n 
A 1 108 ILE 108 125 125 ILE ILE A . n 
A 1 109 LYS 109 126 126 LYS LYS A . n 
A 1 110 THR 110 127 127 THR THR A . n 
A 1 111 ARG 111 128 128 ARG ARG A . n 
A 1 112 ALA 112 129 129 ALA ALA A . n 
A 1 113 MET 113 130 130 MET MET A . n 
A 1 114 GLY 114 131 131 GLY GLY A . n 
A 1 115 THR 115 132 132 THR THR A . n 
A 1 116 TYR 116 133 133 TYR TYR A . n 
A 1 117 ALA 117 134 134 ALA ALA A . n 
A 1 118 ASP 118 135 135 ASP ASP A . n 
A 1 119 LEU 119 136 136 LEU LEU A . n 
A 1 120 ILE 120 137 137 ILE ILE A . n 
A 1 121 ILE 121 138 138 ILE ILE A . n 
A 1 122 ILE 122 139 139 ILE ILE A . n 
A 1 123 THR 123 140 140 THR THR A . n 
A 1 124 GLY 124 141 141 GLY GLY A . n 
A 1 125 SER 125 142 142 SER SER A . n 
A 1 126 LEU 126 143 143 LEU LEU A . n 
A 1 127 GLU 127 144 144 GLU GLU A . n 
A 1 128 GLN 128 145 145 GLN GLN A . n 
A 1 129 VAL 129 146 146 VAL VAL A . n 
A 1 130 ASN 130 147 147 ASN ASN A . n 
A 1 131 GLY 131 148 148 GLY GLY A . n 
A 1 132 TYR 132 149 149 TYR TYR A . n 
A 1 133 TYR 133 150 150 TYR TYR A . n 
A 1 134 ASN 134 151 151 ASN ASN A . n 
A 1 135 ILE 135 152 152 ILE ILE A . n 
A 1 136 LEU 136 153 153 LEU LEU A . n 
A 1 137 LYS 137 154 154 LYS LYS A . n 
A 1 138 ALA 138 155 155 ALA ALA A . n 
A 1 139 LEU 139 156 156 LEU LEU A . n 
A 1 140 ASN 140 157 157 ASN ASN A . n 
A 1 141 LYS 141 158 158 LYS LYS A . n 
A 1 142 ARG 142 159 159 ARG ARG A . n 
A 1 143 ASN 143 160 160 ASN ASN A . n 
A 1 144 ALA 144 161 161 ALA ALA A . n 
A 1 145 LYS 145 162 162 LYS LYS A . n 
A 1 146 PHE 146 163 163 PHE PHE A . n 
A 1 147 VAL 147 164 164 VAL VAL A . n 
A 1 148 LEU 148 165 165 LEU LEU A . n 
A 1 149 LYS 149 166 166 LYS LYS A . n 
A 1 150 ILE 150 167 167 ILE ILE A . n 
A 1 151 ASN 151 168 168 ASN ASN A . n 
A 1 152 GLU 152 169 169 GLU GLU A . n 
A 1 153 ASN 153 170 170 ASN ASN A . n 
A 1 154 MET 154 171 171 MET MET A . n 
A 1 155 PRO 155 172 172 PRO PRO A . n 
A 1 156 TYR 156 173 173 TYR TYR A . n 
A 1 157 ALA 157 174 174 ALA ALA A . n 
A 1 158 GLN 158 175 175 GLN GLN A . n 
A 1 159 ALA 159 176 176 ALA ALA A . n 
A 1 160 THR 160 177 177 THR THR A . n 
A 1 161 PHE 161 178 178 PHE PHE A . n 
A 1 162 LEU 162 179 179 LEU LEU A . n 
A 1 163 ARG 163 180 180 ARG ARG A . n 
A 1 164 VAL 164 181 181 VAL VAL A . n 
A 1 165 PRO 165 182 182 PRO PRO A . n 
A 1 166 LYS 166 183 183 LYS LYS A . n 
A 1 167 ARG 167 184 ?   ?   ?   A . n 
A 1 168 SER 168 185 ?   ?   ?   A . n 
A 1 169 ASP 169 186 ?   ?   ?   A . n 
A 1 170 PRO 170 187 ?   ?   ?   A . n 
A 1 171 ASN 171 188 ?   ?   ?   A . n 
A 1 172 ALA 172 189 ?   ?   ?   A . n 
A 1 173 HIS 173 190 ?   ?   ?   A . n 
A 1 174 THR 174 191 ?   ?   ?   A . n 
A 1 175 LEU 175 192 ?   ?   ?   A . n 
A 1 176 ASP 176 193 ?   ?   ?   A . n 
A 1 177 LYS 177 194 ?   ?   ?   A . n 
A 1 178 GLY 178 195 ?   ?   ?   A . n 
A 1 179 ALA 179 196 ?   ?   ?   A . n 
A 1 180 SER 180 197 ?   ?   ?   A . n 
A 1 181 ILE 181 198 ?   ?   ?   A . n 
A 1 182 ASP 182 199 199 ASP ASP A . n 
A 1 183 GLU 183 200 200 GLU GLU A . n 
A 1 184 ASN 184 201 201 ASN ASN A . n 
A 1 185 LYS 185 202 202 LYS LYS A . n 
A 1 186 LEU 186 203 203 LEU LEU A . n 
A 1 187 PHE 187 204 204 PHE PHE A . n 
A 1 188 GLU 188 205 205 GLU GLU A . n 
A 1 189 GLN 189 206 206 GLN GLN A . n 
A 1 190 GLN 190 207 207 GLN GLN A . n 
A 1 191 LYS 191 208 208 LYS LYS A . n 
A 1 192 ARG 192 209 209 ARG ARG A . n 
A 1 193 ALA 193 210 210 ALA ALA A . n 
A 1 194 TYR 194 211 211 TYR TYR A . n 
A 1 195 PHE 195 212 212 PHE PHE A . n 
A 1 196 ASN 196 213 213 ASN ASN A . n 
A 1 197 TYR 197 214 214 TYR TYR A . n 
A 1 198 ALA 198 215 215 ALA ALA A . n 
A 1 199 ASN 199 216 216 ASN ASN A . n 
A 1 200 ASP 200 217 217 ASP ASP A . n 
A 1 201 VAL 201 218 218 VAL VAL A . n 
A 1 202 ILE 202 219 219 ILE ILE A . n 
A 1 203 CYS 203 220 220 CYS CYS A . n 
A 1 204 ARG 204 221 221 ARG ARG A . n 
A 1 205 PRO 205 222 222 PRO PRO A . n 
A 1 206 ASN 206 223 223 ASN ASN A . n 
A 1 207 ASP 207 224 224 ASP ASP A . n 
A 1 208 GLU 208 225 225 GLU GLU A . n 
A 1 209 VAL 209 226 226 VAL VAL A . n 
A 1 210 CYS 210 227 227 CYS CYS A . n 
A 1 211 SER 211 228 228 SER SER A . n 
A 1 212 PRO 212 229 229 PRO PRO A . n 
A 1 213 LEU 213 230 230 LEU LEU A . n 
A 1 214 ARG 214 231 231 ARG ARG A . n 
A 1 215 ASP 215 232 232 ASP ASP A . n 
B 2 1   HIS 1   47  ?   ?   ?   B . n 
B 2 2   HIS 2   48  ?   ?   ?   B . n 
B 2 3   HIS 3   49  ?   ?   ?   B . n 
B 2 4   HIS 4   50  ?   ?   ?   B . n 
B 2 5   HIS 5   51  ?   ?   ?   B . n 
B 2 6   HIS 6   52  52  HIS HIS B . n 
B 2 7   MET 7   53  53  MET MET B . n 
B 2 8   ASP 8   54  54  ASP ASP B . n 
B 2 9   LYS 9   55  55  LYS LYS B . n 
B 2 10  LEU 10  56  56  LEU LEU B . n 
B 2 11  LYS 11  57  57  LYS LYS B . n 
B 2 12  ASP 12  58  58  ASP ASP B . n 
B 2 13  THR 13  59  59  THR THR B . n 
B 2 14  PRO 14  60  60  PRO PRO B . n 
B 2 15  PHE 15  61  61  PHE PHE B . n 
B 2 16  MET 16  62  62  MET MET B . n 
B 2 17  VAL 17  63  63  VAL VAL B . n 
B 2 18  GLN 18  64  64  GLN GLN B . n 
B 2 19  VAL 19  65  65  VAL VAL B . n 
B 2 20  LYS 20  66  66  LYS LYS B . n 
B 2 21  LEU 21  67  67  LEU LEU B . n 
B 2 22  PRO 22  68  68  PRO PRO B . n 
B 2 23  ASN 23  69  69  ASN ASN B . n 
B 2 24  TYR 24  70  70  TYR TYR B . n 
B 2 25  LYS 25  71  71  LYS LYS B . n 
B 2 26  ASP 26  72  72  ASP ASP B . n 
B 2 27  TYR 27  73  73  TYR TYR B . n 
B 2 28  LEU 28  74  74  LEU LEU B . n 
B 2 29  LEU 29  75  75  LEU LEU B . n 
B 2 30  ASP 30  76  76  ASP ASP B . n 
B 2 31  ASN 31  77  77  ASN ASN B . n 
B 2 32  LYS 32  78  78  LYS LYS B . n 
B 2 33  GLN 33  79  79  GLN GLN B . n 
B 2 34  VAL 34  80  80  VAL VAL B . n 
B 2 35  VAL 35  81  81  VAL VAL B . n 
B 2 36  LEU 36  82  82  LEU LEU B . n 
B 2 37  THR 37  83  83  THR THR B . n 
B 2 38  PHE 38  84  84  PHE PHE B . n 
B 2 39  LYS 39  85  85  LYS LYS B . n 
B 2 40  LEU 40  86  86  LEU LEU B . n 
B 2 41  VAL 41  87  87  VAL VAL B . n 
B 2 42  HIS 42  88  88  HIS HIS B . n 
B 2 43  HIS 43  89  89  HIS HIS B . n 
B 2 44  SER 44  90  90  SER SER B . n 
B 2 45  LYS 45  91  91  LYS LYS B . n 
B 2 46  LYS 46  92  92  LYS LYS B . n 
B 2 47  ILE 47  93  93  ILE ILE B . n 
B 2 48  THR 48  94  94  THR THR B . n 
B 2 49  LEU 49  95  95  LEU LEU B . n 
B 2 50  ILE 50  96  96  ILE ILE B . n 
B 2 51  GLY 51  97  97  GLY GLY B . n 
B 2 52  ASP 52  98  98  ASP ASP B . n 
B 2 53  ALA 53  99  99  ALA ALA B . n 
B 2 54  ASN 54  100 100 ASN ASN B . n 
B 2 55  LYS 55  101 101 LYS LYS B . n 
B 2 56  ILE 56  102 102 ILE ILE B . n 
B 2 57  LEU 57  103 103 LEU LEU B . n 
B 2 58  GLN 58  104 104 GLN GLN B . n 
B 2 59  TYR 59  105 105 TYR TYR B . n 
B 2 60  LYS 60  106 106 LYS LYS B . n 
B 2 61  ASN 61  107 107 ASN ASN B . n 
B 2 62  TYR 62  108 108 TYR TYR B . n 
B 2 63  PHE 63  109 109 PHE PHE B . n 
B 2 64  GLN 64  110 110 GLN GLN B . n 
B 2 65  ALA 65  111 111 ALA ALA B . n 
B 2 66  ASN 66  112 112 ASN ASN B . n 
B 2 67  GLY 67  113 113 GLY GLY B . n 
B 2 68  ALA 68  114 114 ALA ALA B . n 
B 2 69  ARG 69  115 115 ARG ARG B . n 
B 2 70  SER 70  116 116 SER SER B . n 
B 2 71  ASP 71  117 117 ASP ASP B . n 
B 2 72  ILE 72  118 118 ILE ILE B . n 
B 2 73  ASP 73  119 119 ASP ASP B . n 
B 2 74  PHE 74  120 120 PHE PHE B . n 
B 2 75  TYR 75  121 121 TYR TYR B . n 
B 2 76  LEU 76  122 122 LEU LEU B . n 
B 2 77  GLN 77  123 123 GLN GLN B . n 
B 2 78  PRO 78  124 124 PRO PRO B . n 
B 2 79  THR 79  125 125 THR THR B . n 
B 2 80  LEU 80  126 126 LEU LEU B . n 
B 2 81  ASN 81  127 127 ASN ASN B . n 
B 2 82  GLN 82  128 128 GLN GLN B . n 
B 2 83  LYS 83  129 129 LYS LYS B . n 
B 2 84  GLY 84  130 130 GLY GLY B . n 
B 2 85  VAL 85  131 131 VAL VAL B . n 
B 2 86  VAL 86  132 132 VAL VAL B . n 
B 2 87  MET 87  133 133 MET MET B . n 
B 2 88  ILE 88  134 134 ILE ILE B . n 
B 2 89  ALA 89  135 135 ALA ALA B . n 
B 2 90  SER 90  136 136 SER SER B . n 
B 2 91  ASN 91  137 137 ASN ASN B . n 
B 2 92  TYR 92  138 138 TYR TYR B . n 
B 2 93  ASN 93  139 139 ASN ASN B . n 
B 2 94  ASP 94  140 ?   ?   ?   B . n 
B 2 95  ASN 95  141 ?   ?   ?   B . n 
B 2 96  PRO 96  142 ?   ?   ?   B . n 
B 2 97  ASN 97  143 ?   ?   ?   B . n 
B 2 98  SER 98  144 ?   ?   ?   B . n 
B 2 99  LYS 99  145 ?   ?   ?   B . n 
B 2 100 GLU 100 146 ?   ?   ?   B . n 
B 2 101 LYS 101 147 ?   ?   ?   B . n 
B 2 102 PRO 102 148 ?   ?   ?   B . n 
B 2 103 GLN 103 149 ?   ?   ?   B . n 
B 2 104 THR 104 150 ?   ?   ?   B . n 
B 2 105 PHE 105 151 ?   ?   ?   B . n 
B 2 106 ASP 106 152 ?   ?   ?   B . n 
B 2 107 VAL 107 153 ?   ?   ?   B . n 
B 2 108 LEU 108 154 ?   ?   ?   B . n 
B 2 109 GLN 109 155 ?   ?   ?   B . n 
B 2 110 GLY 110 156 ?   ?   ?   B . n 
B 2 111 SER 111 157 ?   ?   ?   B . n 
B 2 112 GLN 112 158 ?   ?   ?   B . n 
B 2 113 PRO 113 159 ?   ?   ?   B . n 
B 2 114 MET 114 160 ?   ?   ?   B . n 
B 2 115 LEU 115 161 ?   ?   ?   B . n 
B 2 116 GLY 116 162 ?   ?   ?   B . n 
B 2 117 ALA 117 163 ?   ?   ?   B . n 
B 2 118 ASN 118 164 ?   ?   ?   B . n 
B 2 119 THR 119 165 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 HOH 1  301 11 HOH HOH A . 
C 3 HOH 2  302 10 HOH HOH A . 
C 3 HOH 3  303 2  HOH HOH A . 
C 3 HOH 4  304 6  HOH HOH A . 
C 3 HOH 5  305 21 HOH HOH A . 
C 3 HOH 6  306 4  HOH HOH A . 
C 3 HOH 7  307 22 HOH HOH A . 
C 3 HOH 8  308 16 HOH HOH A . 
C 3 HOH 9  309 3  HOH HOH A . 
C 3 HOH 10 310 14 HOH HOH A . 
C 3 HOH 11 311 19 HOH HOH A . 
C 3 HOH 12 312 9  HOH HOH A . 
C 3 HOH 13 313 13 HOH HOH A . 
C 3 HOH 14 314 12 HOH HOH A . 
D 3 HOH 1  201 18 HOH HOH B . 
D 3 HOH 2  202 1  HOH HOH B . 
D 3 HOH 3  203 17 HOH HOH B . 
D 3 HOH 4  204 20 HOH HOH B . 
D 3 HOH 5  205 7  HOH HOH B . 
D 3 HOH 6  206 8  HOH HOH B . 
D 3 HOH 7  207 15 HOH HOH B . 
D 3 HOH 8  208 5  HOH HOH B . 
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA    ? ? ? .           2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YNX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     112.621 
_cell.length_a_esd                 ? 
_cell.length_b                     112.621 
_cell.length_b_esd                 ? 
_cell.length_c                     128.204 
_cell.length_c_esd                 ? 
_cell.volume                       1626074.106 
_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                         8YNX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            'P 4abw 2nw' 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   8YNX 
_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             5.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          76.73 
_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              8.5 
_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    'Morpheus I A10 0.06M divalents mix, 0.1M buffer system 3, 30% v/v precipitant mix 2' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX300-HS' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-03-12 
_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                    ? 
_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   0.99984 
_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                        'NSRRC BEAMLINE TPS 05A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.99984 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'TPS 05A' 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          67.82 
_reflns.entry_id                                       8YNX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.25 
_reflns.d_resolution_low                               29.13 
_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                                     13523 
_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                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.974 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.132 
_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                                    3.25 
_reflns_shell.d_res_low                                     3.37 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1313 
_reflns_shell.percent_possible_obs                          ? 
_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                               3.6 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.748 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.500 
_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                               69.64 
_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                                 8YNX 
_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                            3.25 
_refine.ls_d_res_low                             29.13 
_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                     13268 
_refine.ls_number_reflns_R_free                  664 
_refine.ls_number_reflns_R_work                  12604 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.01 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1759 
_refine.ls_R_factor_R_free                       0.2043 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1744 
_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                          1.36 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 18.5993 
_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                            0.3223 
_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                       3.25 
_refine_hist.d_res_low                        29.13 
_refine_hist.number_atoms_solvent             22 
_refine_hist.number_atoms_total               2060 
_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        2038 
_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' ? 0.0112 ? 2080 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1555 ? 2812 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0609 ? 308  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0083 ? 362  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.4290 ? 271  ? f_dihedral_angle_d ? ? 
# 
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' 3.25 3.50  . . 125 2371 94.47 . . . . 0.2361 . . . . . . . . . . . 0.2443 
'X-RAY DIFFRACTION' 3.50 3.85  . . 131 2489 98.98 . . . . 0.1981 . . . . . . . . . . . 0.2564 
'X-RAY DIFFRACTION' 3.85 4.40  . . 133 2527 99.18 . . . . 0.1714 . . . . . . . . . . . 0.1894 
'X-RAY DIFFRACTION' 4.41 5.54  . . 135 2560 99.45 . . . . 0.1454 . . . . . . . . . . . 0.1871 
'X-RAY DIFFRACTION' 5.54 29.13 . . 140 2657 97.90 . . . . 0.1659 . . . . . . . . . . . 0.1892 
# 
_struct.entry_id                     8YNX 
_struct.title                        'Crystal structure of Cag3-CagT complex from Helicobacter pylori' 
_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        8YNX 
_struct_keywords.text            'Type IV secretion system, Helicobacter pylori, STRUCTURAL PROTEIN' 
_struct_keywords.pdbx_keywords   'STRUCTURAL PROTEIN' 
# 
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 2 ? 
C N N 3 ? 
D 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 B5Z6P5_HELPG B5Z6P5 ? 1 
;KEISEADKVIKATKETKETKKEVKRLKKEAKQRQQIPDHKKPQYASVDDTKTQALFDIYDTLNVNDKSFGDWFGNSALKD
KTYLYAMDLLDYNNYLSIENPIIKTRAMGTYADLIIITGSLEQVNGYYNILKALNKRNAKFVLKINENMPYAQATFLRVP
KRSDPNAHTLDKGASIDENKLFEQQKRAYFNYANDVICRPNDEVCSPLRD
;
23 
2 UNP B5Z6Q4_HELPG B5Z6Q4 ? 2 
;DKLKDTPFMVQVKLPNYKDYLLDNKQVVLTFKLVHHSKKITLIGDANKILQYKNYFQANGARSDIDFYLQPTLNQKGVVM
IASNYNDNPNSKEKPQTFDVLQGSQPMLGANT
;
54 
# 
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 8YNX A 6 ? 215 ? B5Z6P5 23 ? 232 ? 23 232 
2 2 8YNX B 8 ? 119 ? B5Z6Q4 54 ? 165 ? 54 165 
# 
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 8YNX GLY A 1 ? UNP B5Z6P5 ? ? 'expression tag' 18 1  
1 8YNX PRO A 2 ? UNP B5Z6P5 ? ? 'expression tag' 19 2  
1 8YNX LEU A 3 ? UNP B5Z6P5 ? ? 'expression tag' 20 3  
1 8YNX GLY A 4 ? UNP B5Z6P5 ? ? 'expression tag' 21 4  
1 8YNX SER A 5 ? UNP B5Z6P5 ? ? 'expression tag' 22 5  
2 8YNX HIS B 1 ? UNP B5Z6Q4 ? ? 'expression tag' 47 6  
2 8YNX HIS B 2 ? UNP B5Z6Q4 ? ? 'expression tag' 48 7  
2 8YNX HIS B 3 ? UNP B5Z6Q4 ? ? 'expression tag' 49 8  
2 8YNX HIS B 4 ? UNP B5Z6Q4 ? ? 'expression tag' 50 9  
2 8YNX HIS B 5 ? UNP B5Z6Q4 ? ? 'expression tag' 51 10 
2 8YNX HIS B 6 ? UNP B5Z6Q4 ? ? 'expression tag' 52 11 
2 8YNX MET B 7 ? UNP B5Z6Q4 ? ? 'expression tag' 53 12 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     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)' 6690  ? 
1 MORE         -41   ? 
1 'SSA (A^2)'  13030 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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 PRO A 42  ? LYS A 46  ? PRO A 59  LYS A 63  5 ? 5  
HELX_P HELX_P2 AA2 ASP A 96  ? ALA A 117 ? ASP A 113 ALA A 134 1 ? 22 
HELX_P HELX_P3 AA3 SER A 125 ? ASN A 140 ? SER A 142 ASN A 157 1 ? 16 
HELX_P HELX_P4 AA4 GLU A 183 ? VAL A 201 ? GLU A 200 VAL A 218 1 ? 19 
HELX_P HELX_P5 AA5 ASP A 207 ? ARG A 214 ? ASP A 224 ARG A 231 5 ? 8  
HELX_P HELX_P6 AA6 ASN B 23  ? SER B 44  ? ASN B 69  SER B 90  1 ? 22 
HELX_P HELX_P7 AA7 ALA B 53  ? ALA B 65  ? ALA B 99  ALA B 111 1 ? 13 
HELX_P HELX_P8 AA8 ASN B 66  ? ALA B 68  ? ASN B 112 ALA B 114 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            203 
_struct_conn.ptnr1_label_atom_id           SG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            210 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             220 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             227 
_struct_conn.ptnr2_symmetry                1_555 
_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               2.059 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       203 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      210 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        220 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       227 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 48  ? ALA A 50  ? GLN A 65  ALA A 67  
AA1 2 ALA A 59  ? ASP A 62  ? ALA A 76  ASP A 79  
AA1 3 PHE B 15  ? LYS B 20  ? PHE B 61  LYS B 66  
AA1 4 GLN A 158 ? ARG A 163 ? GLN A 175 ARG A 180 
AA1 5 LEU A 119 ? GLY A 124 ? LEU A 136 GLY A 141 
AA1 6 LYS A 145 ? ILE A 150 ? LYS A 162 ILE A 167 
AA2 1 TYR A 88  ? ASP A 93  ? TYR A 105 ASP A 110 
AA2 2 VAL B 85  ? ASN B 91  ? VAL B 131 ASN B 137 
AA2 3 LYS B 46  ? ASP B 52  ? LYS B 92  ASP B 98  
AA2 4 ASP B 73  ? THR B 79  ? ASP B 119 THR B 125 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 48  ? N GLN A 65  O PHE A 61  ? O PHE A 78  
AA1 2 3 N ASP A 62  ? N ASP A 79  O MET B 16  ? O MET B 62  
AA1 3 4 O VAL B 17  ? O VAL B 63  N PHE A 161 ? N PHE A 178 
AA1 4 5 O GLN A 158 ? O GLN A 175 N THR A 123 ? N THR A 140 
AA1 5 6 N ILE A 122 ? N ILE A 139 O LYS A 149 ? O LYS A 166 
AA2 1 2 N MET A 92  ? N MET A 109 O MET B 87  ? O MET B 133 
AA2 2 3 O VAL B 86  ? O VAL B 132 N ILE B 50  ? N ILE B 96  
AA2 3 4 N LEU B 49  ? N LEU B 95  O TYR B 75  ? O TYR B 121 
# 
_pdbx_entry_details.entry_id                   8YNX 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE1 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    GLN 
_pdbx_validate_symm_contact.auth_seq_id_1     123 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    NE2 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    GLN 
_pdbx_validate_symm_contact.auth_seq_id_2     123 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   7_555 
_pdbx_validate_symm_contact.dist              2.11 
# 
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 70  ? ? -174.01 -178.91 
2 1 ASP A 79  ? ? -115.02 66.51   
3 1 LYS B 57  ? ? -89.12  30.08   
4 1 LEU B 126 ? ? -119.61 -88.48  
5 1 ASN B 127 ? ? -67.38  68.17   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     309 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+1/4  
3 y+1/2,-x+1/2,z+3/4  
4 x+1/2,-y+1/2,-z+3/4 
5 -x+1/2,y+1/2,-z+1/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
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 34.6384608119 -11.3964818391 19.6248734178 0.562469503291 ? 0.197403572027    ? 0.144645031492     
? 0.592677575295 ? 0.186638661215   ? 0.685325833729 ? 8.00048622542  ? -3.12978519717  ? -3.04696118893  ? 5.11251160941 ? 
0.752854982343 ? 9.28785266459 ? -0.0567009516649 ? 0.345271433366    ? -0.458833533106 ? -0.171542097847 ? -0.520806693327  ? 
-0.744376008    ? 0.73889913796    ? 0.622532770054   ? 0.491513221873  ? 
2 'X-RAY DIFFRACTION' ? refined 28.1649048687 -1.5855519629  7.25205421169 0.994222794822 ? 0.00612236212852  ? 0.0979599493568    
? 0.753167192261 ? 0.0519185536019  ? 0.560507333875 ? 2.73307982923  ? -3.57199469695  ? 0.974981029737  ? 7.7035550852  ? 
-4.5193200801  ? 5.24719615503 ? 0.106242807323   ? 0.602877973495    ? -0.528100928149 ? -1.52311833572  ? -0.918284700624  ? 
0.105695526312  ? 1.44769830871    ? 1.48568086787    ? 0.634780455324  ? 
3 'X-RAY DIFFRACTION' ? refined 21.2385863738 6.78050114351  13.1814364995 0.35369185764  ? -0.0106285047575  ? -0.000798677573822 
? 0.389552113799 ? -0.033343708976  ? 0.372533508964 ? 2.52069560437  ? -1.24240193676  ? -1.27903674006  ? 8.20846737957 ? 
-6.87809753998 ? 7.92696893953 ? -0.0413941989123 ? -0.00677747328338 ? 0.290040274082  ? 0.233813995984  ? 0.248820611173   ? 
0.538117648612  ? -0.0588782985193 ? -0.07411874996   ? -0.158197521714 ? 
4 'X-RAY DIFFRACTION' ? refined 15.4323753583 -8.67833726617 25.0088531667 0.52548717976  ? -0.0840495063748  ? -0.0195188742123   
? 0.385684094189 ? 0.0133045445539  ? 0.261588334538 ? 7.32269327842  ? -0.911315465925 ? -1.09838129424  ? 5.02760746642 ? 
-4.24627617384 ? 3.9467666893  ? 0.205677931889   ? 0.106430012577    ? 0.223723202433  ? -0.615806574013 ? -0.0878727228434 ? 
-0.121498868498 ? -0.173902381584  ? -0.361571234729  ? -0.149413780859 ? 
5 'X-RAY DIFFRACTION' ? refined 23.9263911119 -23.2892770954 23.7788010532 0.847044646872 ? 0.176797182703    ? 0.0915047313118    
? 0.456894441301 ? 0.175410730254   ? 0.810785882101 ? 7.57991377995  ? 6.1547730729    ? -0.612196313888 ? 6.61281777428 ? 
2.02621360139  ? 4.21252335476 ? -0.417357060242  ? -0.582922723721   ? -0.704029262546 ? -0.101723476683 ? -0.154330895164  ? 
0.0394090073627 ? 0.348082864278   ? -0.127182815836  ? 0.402052136763  ? 
6 'X-RAY DIFFRACTION' ? refined 30.4750515218 -11.4180555271 33.4215723585 0.910833214742 ? -0.00534100109181 ? -0.0351080051426   
? 0.892703683301 ? 0.0869414416724  ? 0.880665350336 ? 2.3510159994   ? -2.29767690712  ? 2.25665070844   ? 2.32334576041 ? 
-2.45295502684 ? 7.46589875652 ? -0.0494145327185 ? -1.77803560064    ? -1.1150817495   ? 0.995628889455  ? -0.371406761365  ? 
-0.94767301618  ? -0.18300195028   ? 0.970773955614   ? 0.344176332425  ? 
7 'X-RAY DIFFRACTION' ? refined 23.105503754  -6.96287031421 6.16529228468 2.04322907656  ? -0.160226438378   ? -0.442746021437    
? 0.871647853446 ? 0.0622779959948  ? 1.20654826141  ? 0.321923568032 ? 0.253024928646  ? 1.16412714172   ? 0.3421415711  ? 
0.963445289792 ? 4.29275104639 ? -0.566069074956  ? -0.157159915834   ? -0.145715012047 ? -0.600440160421 ? -1.07955991671   ? 
1.38461568454   ? -2.99713203838   ? -0.0084375031579 ? 1.82779997521   ? 
8 'X-RAY DIFFRACTION' ? refined 20.3917599225 1.67241986923  15.3563477936 0.490938088636 ? -0.0616220988499  ? -0.0308175509005   
? 0.309811955874 ? -0.0265561919461 ? 0.412272337464 ? 3.29963668477  ? 0.404420697673  ? -1.22220947785  ? 5.75217623156 ? 
-4.39891481801 ? 3.8615405177  ? 0.145544271324   ? 0.131210050997    ? 0.257995353755  ? -0.286851520358 ? 0.0521180472696  ? 
-0.151800091516 ? 0.180240788446   ? -0.304956881753  ? -0.18185156982  ? 
9 'X-RAY DIFFRACTION' ? refined 28.5640251632 17.615214525   6.67941000417 0.439154530878 ? -0.0113880898139  ? 0.0274232660888    
? 0.382135762123 ? 0.0374942137195  ? 0.377448408566 ? 9.63842257379  ? 3.4031935649    ? 0.538887692617  ? 4.78939177304 ? 
-1.6624947813  ? 8.52641226331 ? 0.341254600195   ? 0.0238283635846   ? 0.228645364863  ? -0.239679320797 ? 0.0478560967981  ? 
-0.342004395182 ? 0.300666713763   ? 0.657639644315   ? -0.399174817107 ? 
# 
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 A 1   A 57  ? A 27  A 83  ? ? 
;chain 'A' and (resid 57 through 83 )
;
2 'X-RAY DIFFRACTION' 2 A 28  A 84  ? A 47  A 103 ? ? 
;chain 'A' and (resid 84 through 103 )
;
3 'X-RAY DIFFRACTION' 3 A 48  A 104 ? A 77  A 133 ? ? 
;chain 'A' and (resid 104 through 133 )
;
4 'X-RAY DIFFRACTION' 4 A 78  A 134 ? A 128 A 199 ? ? 
;chain 'A' and (resid 134 through 199 )
;
5 'X-RAY DIFFRACTION' 5 A 129 A 200 ? A 146 A 217 ? ? 
;chain 'A' and (resid 200 through 217 )
;
6 'X-RAY DIFFRACTION' 6 A 147 A 218 ? A 161 A 232 ? ? 
;chain 'A' and (resid 218 through 232 )
;
7 'X-RAY DIFFRACTION' 7 B 1   B 52  ? B 5   B 56  ? ? 
;chain 'B' and (resid 52 through 56 )
;
8 'X-RAY DIFFRACTION' 8 B 6   B 57  ? B 40  B 91  ? ? 
;chain 'B' and (resid 57 through 91 )
;
9 'X-RAY DIFFRACTION' 9 B 41  B 92  ? B 88  B 139 ? ? 
;chain 'B' and (resid 92 through 139 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       314 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.87 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 GLY 18  ? A GLY 1   
2  1 Y 1 A PRO 19  ? A PRO 2   
3  1 Y 1 A LEU 20  ? A LEU 3   
4  1 Y 1 A GLY 21  ? A GLY 4   
5  1 Y 1 A SER 22  ? A SER 5   
6  1 Y 1 A LYS 23  ? A LYS 6   
7  1 Y 1 A GLU 24  ? A GLU 7   
8  1 Y 1 A ILE 25  ? A ILE 8   
9  1 Y 1 A SER 26  ? A SER 9   
10 1 Y 1 A GLU 27  ? A GLU 10  
11 1 Y 1 A ALA 28  ? A ALA 11  
12 1 Y 1 A ASP 29  ? A ASP 12  
13 1 Y 1 A LYS 30  ? A LYS 13  
14 1 Y 1 A VAL 31  ? A VAL 14  
15 1 Y 1 A ILE 32  ? A ILE 15  
16 1 Y 1 A LYS 33  ? A LYS 16  
17 1 Y 1 A ALA 34  ? A ALA 17  
18 1 Y 1 A THR 35  ? A THR 18  
19 1 Y 1 A LYS 36  ? A LYS 19  
20 1 Y 1 A GLU 37  ? A GLU 20  
21 1 Y 1 A THR 38  ? A THR 21  
22 1 Y 1 A LYS 39  ? A LYS 22  
23 1 Y 1 A GLU 40  ? A GLU 23  
24 1 Y 1 A THR 41  ? A THR 24  
25 1 Y 1 A LYS 42  ? A LYS 25  
26 1 Y 1 A LYS 43  ? A LYS 26  
27 1 Y 1 A GLU 44  ? A GLU 27  
28 1 Y 1 A VAL 45  ? A VAL 28  
29 1 Y 1 A LYS 46  ? A LYS 29  
30 1 Y 1 A ARG 47  ? A ARG 30  
31 1 Y 1 A LEU 48  ? A LEU 31  
32 1 Y 1 A LYS 49  ? A LYS 32  
33 1 Y 1 A LYS 50  ? A LYS 33  
34 1 Y 1 A GLU 51  ? A GLU 34  
35 1 Y 1 A ALA 52  ? A ALA 35  
36 1 Y 1 A LYS 53  ? A LYS 36  
37 1 Y 1 A GLN 54  ? A GLN 37  
38 1 Y 1 A ARG 55  ? A ARG 38  
39 1 Y 1 A GLN 56  ? A GLN 39  
40 1 Y 1 A ARG 184 ? A ARG 167 
41 1 Y 1 A SER 185 ? A SER 168 
42 1 Y 1 A ASP 186 ? A ASP 169 
43 1 Y 1 A PRO 187 ? A PRO 170 
44 1 Y 1 A ASN 188 ? A ASN 171 
45 1 Y 1 A ALA 189 ? A ALA 172 
46 1 Y 1 A HIS 190 ? A HIS 173 
47 1 Y 1 A THR 191 ? A THR 174 
48 1 Y 1 A LEU 192 ? A LEU 175 
49 1 Y 1 A ASP 193 ? A ASP 176 
50 1 Y 1 A LYS 194 ? A LYS 177 
51 1 Y 1 A GLY 195 ? A GLY 178 
52 1 Y 1 A ALA 196 ? A ALA 179 
53 1 Y 1 A SER 197 ? A SER 180 
54 1 Y 1 A ILE 198 ? A ILE 181 
55 1 Y 1 B HIS 47  ? B HIS 1   
56 1 Y 1 B HIS 48  ? B HIS 2   
57 1 Y 1 B HIS 49  ? B HIS 3   
58 1 Y 1 B HIS 50  ? B HIS 4   
59 1 Y 1 B HIS 51  ? B HIS 5   
60 1 Y 1 B ASP 140 ? B ASP 94  
61 1 Y 1 B ASN 141 ? B ASN 95  
62 1 Y 1 B PRO 142 ? B PRO 96  
63 1 Y 1 B ASN 143 ? B ASN 97  
64 1 Y 1 B SER 144 ? B SER 98  
65 1 Y 1 B LYS 145 ? B LYS 99  
66 1 Y 1 B GLU 146 ? B GLU 100 
67 1 Y 1 B LYS 147 ? B LYS 101 
68 1 Y 1 B PRO 148 ? B PRO 102 
69 1 Y 1 B GLN 149 ? B GLN 103 
70 1 Y 1 B THR 150 ? B THR 104 
71 1 Y 1 B PHE 151 ? B PHE 105 
72 1 Y 1 B ASP 152 ? B ASP 106 
73 1 Y 1 B VAL 153 ? B VAL 107 
74 1 Y 1 B LEU 154 ? B LEU 108 
75 1 Y 1 B GLN 155 ? B GLN 109 
76 1 Y 1 B GLY 156 ? B GLY 110 
77 1 Y 1 B SER 157 ? B SER 111 
78 1 Y 1 B GLN 158 ? B GLN 112 
79 1 Y 1 B PRO 159 ? B PRO 113 
80 1 Y 1 B MET 160 ? B MET 114 
81 1 Y 1 B LEU 161 ? B LEU 115 
82 1 Y 1 B GLY 162 ? B GLY 116 
83 1 Y 1 B ALA 163 ? B ALA 117 
84 1 Y 1 B ASN 164 ? B ASN 118 
85 1 Y 1 B THR 165 ? B THR 119 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'The University Grants Committee, Research Grants Council (RGC)' 
_pdbx_audit_support.country                'Hong Kong' 
_pdbx_audit_support.grant_number           14121619 
_pdbx_audit_support.ordinal                1 
# 
_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   6x6s 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 41 21 2' 
_space_group.name_Hall        'P 4abw 2nw' 
_space_group.IT_number        92 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8YNX 
_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]   0.008879 
_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]   0.008879 
_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]   0.007800 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 6.96715 ?       ? ? 11.43723 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLN A 1 40  ? 42.46613 2.99169   24.95132  1.000 123.70620 ? 57  GLN A N   1 
ATOM   2    C CA  . GLN A 1 40  ? 41.12645 3.42236   25.35605  1.000 124.56795 ? 57  GLN A CA  1 
ATOM   3    C C   . GLN A 1 40  ? 40.19566 2.25108   25.70553  1.000 114.78376 ? 57  GLN A C   1 
ATOM   4    O O   . GLN A 1 40  ? 39.56802 2.25793   26.76493  1.000 113.65507 ? 57  GLN A O   1 
ATOM   5    C CB  . GLN A 1 40  ? 40.48619 4.28182   24.25751  1.000 126.44396 ? 57  GLN A CB  1 
ATOM   6    C CG  . GLN A 1 40  ? 39.41691 5.27136   24.74902  1.000 128.38963 ? 57  GLN A CG  1 
ATOM   7    C CD  . GLN A 1 40  ? 39.94749 6.32668   25.71970  1.000 134.89358 ? 57  GLN A CD  1 
ATOM   8    O OE1 . GLN A 1 40  ? 41.14268 6.63206   25.74087  1.000 136.10932 ? 57  GLN A OE1 1 
ATOM   9    N NE2 . GLN A 1 40  ? 39.04800 6.89983   26.51760  1.000 130.35161 ? 57  GLN A NE2 1 
ATOM   10   N N   . ILE A 1 41  ? 40.08862 1.26040   24.82587  1.000 107.75857 ? 58  ILE A N   1 
ATOM   11   C CA  . ILE A 1 41  ? 39.28079 0.06697   25.07057  1.000 104.35235 ? 58  ILE A CA  1 
ATOM   12   C C   . ILE A 1 41  ? 40.21322 -1.05746  25.50633  1.000 101.23102 ? 58  ILE A C   1 
ATOM   13   O O   . ILE A 1 41  ? 41.08583 -1.46102  24.71394  1.000 99.93680  ? 58  ILE A O   1 
ATOM   14   C CB  . ILE A 1 41  ? 38.46512 -0.35260  23.83510  1.000 98.75746  ? 58  ILE A CB  1 
ATOM   15   C CG1 . ILE A 1 41  ? 37.34441 0.64132   23.55081  1.000 95.34780  ? 58  ILE A CG1 1 
ATOM   16   C CG2 . ILE A 1 41  ? 37.85820 -1.73858  24.02913  1.000 81.44936  ? 58  ILE A CG2 1 
ATOM   17   C CD1 . ILE A 1 41  ? 36.57873 0.32046   22.29104  1.000 87.98647  ? 58  ILE A CD1 1 
ATOM   18   N N   . PRO A 1 42  ? 40.08222 -1.58479  26.72529  1.000 95.55005  ? 59  PRO A N   1 
ATOM   19   C CA  . PRO A 1 42  ? 40.90632 -2.72705  27.12963  1.000 93.75044  ? 59  PRO A CA  1 
ATOM   20   C C   . PRO A 1 42  ? 40.84331 -3.83604  26.09004  1.000 91.60271  ? 59  PRO A C   1 
ATOM   21   O O   . PRO A 1 42  ? 39.86500 -3.97023  25.35804  1.000 88.53534  ? 59  PRO A O   1 
ATOM   22   C CB  . PRO A 1 42  ? 40.28869 -3.15415  28.46441  1.000 89.44946  ? 59  PRO A CB  1 
ATOM   23   C CG  . PRO A 1 42  ? 39.71837 -1.88411  29.02333  1.000 88.95246  ? 59  PRO A CG  1 
ATOM   24   C CD  . PRO A 1 42  ? 39.24223 -1.08564  27.83291  1.000 92.87389  ? 59  PRO A CD  1 
ATOM   25   N N   . ASP A 1 43  ? 41.91551 -4.62210  26.01216  1.000 101.74992 ? 60  ASP A N   1 
ATOM   26   C CA  . ASP A 1 43  ? 42.02944 -5.56648  24.90828  1.000 99.22853  ? 60  ASP A CA  1 
ATOM   27   C C   . ASP A 1 43  ? 41.06100 -6.73696  25.04589  1.000 97.07675  ? 60  ASP A C   1 
ATOM   28   O O   . ASP A 1 43  ? 40.58569 -7.25350  24.03047  1.000 95.25188  ? 60  ASP A O   1 
ATOM   29   C CB  . ASP A 1 43  ? 43.46775 -6.05445  24.79124  1.000 100.83509 ? 60  ASP A CB  1 
ATOM   30   C CG  . ASP A 1 43  ? 44.39111 -4.98746  24.23708  1.000 107.66534 ? 60  ASP A CG  1 
ATOM   31   O OD1 . ASP A 1 43  ? 44.48573 -4.86478  22.99799  1.000 108.51676 ? 60  ASP A OD1 1 
ATOM   32   O OD2 . ASP A 1 43  ? 45.01566 -4.26073  25.04072  1.000 113.32661 ? 60  ASP A OD2 1 
ATOM   33   N N   . HIS A 1 44  ? 40.73712 -7.16996  26.26919  1.000 87.09707  ? 61  HIS A N   1 
ATOM   34   C CA  . HIS A 1 44  ? 39.76671 -8.25441  26.36796  1.000 82.14613  ? 61  HIS A CA  1 
ATOM   35   C C   . HIS A 1 44  ? 38.34408 -7.77840  26.13645  1.000 80.92698  ? 61  HIS A C   1 
ATOM   36   O O   . HIS A 1 44  ? 37.45260 -8.61282  25.94075  1.000 80.87511  ? 61  HIS A O   1 
ATOM   37   C CB  . HIS A 1 44  ? 39.85106 -8.98925  27.71690  1.000 83.40075  ? 61  HIS A CB  1 
ATOM   38   C CG  . HIS A 1 44  ? 39.47870 -8.15648  28.89896  1.000 87.11733  ? 61  HIS A CG  1 
ATOM   39   N ND1 . HIS A 1 44  ? 40.08923 -6.95541  29.18981  1.000 89.62753  ? 61  HIS A ND1 1 
ATOM   40   C CD2 . HIS A 1 44  ? 38.55073 -8.35154  29.86575  1.000 90.85576  ? 61  HIS A CD2 1 
ATOM   41   C CE1 . HIS A 1 44  ? 39.54987 -6.44347  30.28352  1.000 91.16363  ? 61  HIS A CE1 1 
ATOM   42   N NE2 . HIS A 1 44  ? 38.61152 -7.26902  30.71188  1.000 91.95528  ? 61  HIS A NE2 1 
ATOM   43   N N   . LYS A 1 45  ? 38.11144 -6.47057  26.12527  1.000 78.24203  ? 62  LYS A N   1 
ATOM   44   C CA  . LYS A 1 45  ? 36.77766 -5.95220  25.87660  1.000 73.22035  ? 62  LYS A CA  1 
ATOM   45   C C   . LYS A 1 45  ? 36.52146 -5.65967  24.40099  1.000 72.14462  ? 62  LYS A C   1 
ATOM   46   O O   . LYS A 1 45  ? 35.37228 -5.38792  24.03413  1.000 71.22594  ? 62  LYS A O   1 
ATOM   47   C CB  . LYS A 1 45  ? 36.54938 -4.69237  26.71668  1.000 71.62016  ? 62  LYS A CB  1 
ATOM   48   C CG  . LYS A 1 45  ? 36.88983 -4.85406  28.19195  1.000 71.22186  ? 62  LYS A CG  1 
ATOM   49   C CD  . LYS A 1 45  ? 36.10876 -3.86761  29.02483  1.000 66.82301  ? 62  LYS A CD  1 
ATOM   50   C CE  . LYS A 1 45  ? 36.14958 -4.19910  30.49996  1.000 72.78387  ? 62  LYS A CE  1 
ATOM   51   N NZ  . LYS A 1 45  ? 35.34107 -3.19544  31.24767  1.000 66.70630  ? 62  LYS A NZ  1 
ATOM   52   N N   . LYS A 1 46  ? 37.55166 -5.71494  23.55187  1.000 71.27287  ? 63  LYS A N   1 
ATOM   53   C CA  . LYS A 1 46  ? 37.35621 -5.50659  22.12882  1.000 66.03078  ? 63  LYS A CA  1 
ATOM   54   C C   . LYS A 1 46  ? 36.52672 -6.64520  21.54557  1.000 65.17420  ? 63  LYS A C   1 
ATOM   55   O O   . LYS A 1 46  ? 36.68237 -7.80112  21.95144  1.000 66.32413  ? 63  LYS A O   1 
ATOM   56   C CB  . LYS A 1 46  ? 38.69089 -5.42802  21.38406  1.000 68.97922  ? 63  LYS A CB  1 
ATOM   57   C CG  . LYS A 1 46  ? 39.64232 -4.28610  21.73337  1.000 71.47960  ? 63  LYS A CG  1 
ATOM   58   C CD  . LYS A 1 46  ? 40.41369 -3.92854  20.46511  1.000 75.49050  ? 63  LYS A CD  1 
ATOM   59   C CE  . LYS A 1 46  ? 41.93860 -3.88501  20.62101  1.000 86.70198  ? 63  LYS A CE  1 
ATOM   60   N NZ  . LYS A 1 46  ? 42.39116 -2.97225  21.70878  1.000 93.79342  ? 63  LYS A NZ  1 
ATOM   61   N N   . PRO A 1 47  ? 35.65959 -6.35142  20.57154  1.000 63.09157  ? 64  PRO A N   1 
ATOM   62   C CA  . PRO A 1 47  ? 34.83375 -7.41037  19.97781  1.000 63.78250  ? 64  PRO A CA  1 
ATOM   63   C C   . PRO A 1 47  ? 35.71318 -8.42155  19.26512  1.000 66.13277  ? 64  PRO A C   1 
ATOM   64   O O   . PRO A 1 47  ? 36.74744 -8.07655  18.69050  1.000 71.05889  ? 64  PRO A O   1 
ATOM   65   C CB  . PRO A 1 47  ? 33.94227 -6.66089  18.98217  1.000 61.58921  ? 64  PRO A CB  1 
ATOM   66   C CG  . PRO A 1 47  ? 34.27872 -5.21781  19.12663  1.000 60.95735  ? 64  PRO A CG  1 
ATOM   67   C CD  . PRO A 1 47  ? 35.60217 -5.11593  19.78148  1.000 61.59098  ? 64  PRO A CD  1 
ATOM   68   N N   . GLN A 1 48  ? 35.29944 -9.68104  19.29025  1.000 61.17275  ? 65  GLN A N   1 
ATOM   69   C CA  . GLN A 1 48  ? 36.17208 -10.71666 18.76745  1.000 65.65914  ? 65  GLN A CA  1 
ATOM   70   C C   . GLN A 1 48  ? 35.37514 -11.79091 18.03881  1.000 69.54017  ? 65  GLN A C   1 
ATOM   71   O O   . GLN A 1 48  ? 34.23228 -12.10207 18.39983  1.000 66.20890  ? 65  GLN A O   1 
ATOM   72   C CB  . GLN A 1 48  ? 36.98076 -11.35756 19.88299  1.000 66.66871  ? 65  GLN A CB  1 
ATOM   73   C CG  . GLN A 1 48  ? 36.23134 -12.45819 20.58523  1.000 68.79242  ? 65  GLN A CG  1 
ATOM   74   C CD  . GLN A 1 48  ? 36.76670 -12.74425 21.96065  1.000 74.37812  ? 65  GLN A CD  1 
ATOM   75   O OE1 . GLN A 1 48  ? 36.52419 -11.98268 22.90397  1.000 75.42905  ? 65  GLN A OE1 1 
ATOM   76   N NE2 . GLN A 1 48  ? 37.50447 -13.85009 22.09167  1.000 80.04721  ? 65  GLN A NE2 1 
ATOM   77   N N   . TYR A 1 49  ? 36.00366 -12.35793 17.00509  1.000 70.96401  ? 66  TYR A N   1 
ATOM   78   C CA  . TYR A 1 49  ? 35.47007 -13.51734 16.30591  1.000 73.84472  ? 66  TYR A CA  1 
ATOM   79   C C   . TYR A 1 49  ? 36.03479 -14.78138 16.94873  1.000 77.95373  ? 66  TYR A C   1 
ATOM   80   O O   . TYR A 1 49  ? 37.10657 -14.75579 17.55975  1.000 81.24414  ? 66  TYR A O   1 
ATOM   81   C CB  . TYR A 1 49  ? 35.84063 -13.48715 14.82595  1.000 72.70640  ? 66  TYR A CB  1 
ATOM   82   C CG  . TYR A 1 49  ? 34.93522 -12.65750 13.94839  1.000 70.60002  ? 66  TYR A CG  1 
ATOM   83   C CD1 . TYR A 1 49  ? 33.67466 -13.10214 13.59315  1.000 72.21286  ? 66  TYR A CD1 1 
ATOM   84   C CD2 . TYR A 1 49  ? 35.38120 -11.46067 13.40451  1.000 72.39520  ? 66  TYR A CD2 1 
ATOM   85   C CE1 . TYR A 1 49  ? 32.86089 -12.34173 12.76409  1.000 75.28481  ? 66  TYR A CE1 1 
ATOM   86   C CE2 . TYR A 1 49  ? 34.58275 -10.70047 12.57254  1.000 72.62307  ? 66  TYR A CE2 1 
ATOM   87   C CZ  . TYR A 1 49  ? 33.32496 -11.13946 12.25729  1.000 74.59000  ? 66  TYR A CZ  1 
ATOM   88   O OH  . TYR A 1 49  ? 32.52502 -10.37749 11.43341  1.000 79.33702  ? 66  TYR A OH  1 
ATOM   89   N N   . ALA A 1 50  ? 35.32257 -15.89643 16.79785  1.000 77.58098  ? 67  ALA A N   1 
ATOM   90   C CA  . ALA A 1 50  ? 35.74596 -17.09888 17.50154  1.000 87.15901  ? 67  ALA A CA  1 
ATOM   91   C C   . ALA A 1 50  ? 35.11530 -18.32533 16.86068  1.000 96.83403  ? 67  ALA A C   1 
ATOM   92   O O   . ALA A 1 50  ? 33.88472 -18.41584 16.78721  1.000 94.58327  ? 67  ALA A O   1 
ATOM   93   C CB  . ALA A 1 50  ? 35.36909 -16.99742 18.97941  1.000 86.32732  ? 67  ALA A CB  1 
ATOM   94   N N   . SER A 1 51  ? 35.95416 -19.27755 16.43325  1.000 100.38123 ? 68  SER A N   1 
ATOM   95   C CA  . SER A 1 51  ? 35.49437 -20.39645 15.60465  1.000 105.76868 ? 68  SER A CA  1 
ATOM   96   C C   . SER A 1 51  ? 34.59671 -21.31564 16.42554  1.000 112.19555 ? 68  SER A C   1 
ATOM   97   O O   . SER A 1 51  ? 35.06397 -22.11860 17.23730  1.000 111.74839 ? 68  SER A O   1 
ATOM   98   C CB  . SER A 1 51  ? 36.67389 -21.16292 15.01609  1.000 111.77252 ? 68  SER A CB  1 
ATOM   99   O OG  . SER A 1 51  ? 37.61486 -21.49620 16.01317  1.000 120.84353 ? 68  SER A OG  1 
ATOM   100  N N   . VAL A 1 52  ? 33.28775 -21.22298 16.17858  1.000 110.25788 ? 69  VAL A N   1 
ATOM   101  C CA  . VAL A 1 52  ? 32.30744 -21.94753 16.97840  1.000 107.68463 ? 69  VAL A CA  1 
ATOM   102  C C   . VAL A 1 52  ? 32.12923 -23.38753 16.54794  1.000 117.45734 ? 69  VAL A C   1 
ATOM   103  O O   . VAL A 1 52  ? 31.28785 -24.09094 17.11786  1.000 118.90756 ? 69  VAL A O   1 
ATOM   104  C CB  . VAL A 1 52  ? 30.94852 -21.23783 16.88731  1.000 105.01374 ? 69  VAL A CB  1 
ATOM   105  C CG1 . VAL A 1 52  ? 31.07260 -19.86179 17.49188  1.000 95.88799  ? 69  VAL A CG1 1 
ATOM   106  C CG2 . VAL A 1 52  ? 30.48313 -21.18337 15.43999  1.000 107.94336 ? 69  VAL A CG2 1 
ATOM   107  N N   . ASP A 1 53  ? 32.87901 -23.84663 15.56194  1.000 133.99334 ? 70  ASP A N   1 
ATOM   108  C CA  . ASP A 1 53  ? 32.67732 -25.16996 14.99008  1.000 140.16126 ? 70  ASP A CA  1 
ATOM   109  C C   . ASP A 1 53  ? 33.80208 -25.40815 13.99907  1.000 143.69431 ? 70  ASP A C   1 
ATOM   110  O O   . ASP A 1 53  ? 34.68660 -24.56345 13.81837  1.000 139.90833 ? 70  ASP A O   1 
ATOM   111  C CB  . ASP A 1 53  ? 31.30992 -25.28389 14.31480  1.000 142.26054 ? 70  ASP A CB  1 
ATOM   112  C CG  . ASP A 1 53  ? 30.91157 -24.00622 13.59432  1.000 140.48553 ? 70  ASP A CG  1 
ATOM   113  O OD1 . ASP A 1 53  ? 31.80828 -23.20889 13.23124  1.000 138.18329 ? 70  ASP A OD1 1 
ATOM   114  O OD2 . ASP A 1 53  ? 29.69626 -23.78956 13.40414  1.000 140.88740 ? 70  ASP A OD2 1 
ATOM   115  N N   . ASP A 1 54  ? 33.76422 -26.57275 13.35752  1.000 143.19029 ? 71  ASP A N   1 
ATOM   116  C CA  . ASP A 1 54  ? 34.66830 -26.81044 12.24318  1.000 142.50688 ? 71  ASP A CA  1 
ATOM   117  C C   . ASP A 1 54  ? 34.25591 -26.06533 10.97097  1.000 144.30935 ? 71  ASP A C   1 
ATOM   118  O O   . ASP A 1 54  ? 34.98168 -26.15036 9.97108   1.000 144.07766 ? 71  ASP A O   1 
ATOM   119  C CB  . ASP A 1 54  ? 34.78720 -28.31384 11.98230  1.000 144.32367 ? 71  ASP A CB  1 
ATOM   120  C CG  . ASP A 1 54  ? 33.46267 -29.03530 12.10630  1.000 149.01086 ? 71  ASP A CG  1 
ATOM   121  O OD1 . ASP A 1 54  ? 32.42664 -28.44033 11.74035  1.000 148.38402 ? 71  ASP A OD1 1 
ATOM   122  O OD2 . ASP A 1 54  ? 33.46387 -30.20518 12.55258  1.000 153.68129 ? 71  ASP A OD2 1 
ATOM   123  N N   . THR A 1 55  ? 33.13526 -25.33765 10.97788  1.000 141.51628 ? 72  THR A N   1 
ATOM   124  C CA  . THR A 1 55  ? 32.80966 -24.46307 9.85706   1.000 133.50386 ? 72  THR A CA  1 
ATOM   125  C C   . THR A 1 55  ? 33.81655 -23.32697 9.77239   1.000 126.08467 ? 72  THR A C   1 
ATOM   126  O O   . THR A 1 55  ? 34.38919 -22.89482 10.77803  1.000 125.16358 ? 72  THR A O   1 
ATOM   127  C CB  . THR A 1 55  ? 31.39931 -23.87237 9.98978   1.000 128.92608 ? 72  THR A CB  1 
ATOM   128  O OG1 . THR A 1 55  ? 30.48463 -24.89097 10.40564  1.000 138.31740 ? 72  THR A OG1 1 
ATOM   129  C CG2 . THR A 1 55  ? 30.92015 -23.26839 8.65809   1.000 120.45815 ? 72  THR A CG2 1 
ATOM   130  N N   . LYS A 1 56  ? 34.03373 -22.85040 8.54680   1.000 120.76417 ? 73  LYS A N   1 
ATOM   131  C CA  . LYS A 1 56  ? 34.82201 -21.64600 8.34606   1.000 117.20781 ? 73  LYS A CA  1 
ATOM   132  C C   . LYS A 1 56  ? 34.13893 -20.39764 8.91462   1.000 112.58788 ? 73  LYS A C   1 
ATOM   133  O O   . LYS A 1 56  ? 34.82736 -19.41591 9.21785   1.000 105.49365 ? 73  LYS A O   1 
ATOM   134  C CB  . LYS A 1 56  ? 35.11862 -21.49084 6.85356   1.000 111.72102 ? 73  LYS A CB  1 
ATOM   135  C CG  . LYS A 1 56  ? 33.91142 -21.04968 6.02956   1.000 118.20029 ? 73  LYS A CG  1 
ATOM   136  C CD  . LYS A 1 56  ? 33.96221 -21.63133 4.63006   1.000 113.85906 ? 73  LYS A CD  1 
ATOM   137  C CE  . LYS A 1 56  ? 33.70007 -23.13244 4.63476   1.000 120.88892 ? 73  LYS A CE  1 
ATOM   138  N NZ  . LYS A 1 56  ? 33.82543 -23.74916 3.26390   1.000 117.80132 ? 73  LYS A NZ  1 
ATOM   139  N N   . THR A 1 57  ? 32.81550 -20.41544 9.09705   1.000 111.97542 ? 74  THR A N   1 
ATOM   140  C CA  . THR A 1 57  ? 32.08888 -19.24309 9.59064   1.000 106.17874 ? 74  THR A CA  1 
ATOM   141  C C   . THR A 1 57  ? 32.30657 -19.09704 11.09488  1.000 97.65673  ? 74  THR A C   1 
ATOM   142  O O   . THR A 1 57  ? 31.80141 -19.90030 11.88837  1.000 101.47074 ? 74  THR A O   1 
ATOM   143  C CB  . THR A 1 57  ? 30.60022 -19.35764 9.27622   1.000 108.77164 ? 74  THR A CB  1 
ATOM   144  O OG1 . THR A 1 57  ? 30.01827 -20.37904 10.10020  1.000 115.01723 ? 74  THR A OG1 1 
ATOM   145  C CG2 . THR A 1 57  ? 30.39273 -19.72015 7.80221   1.000 108.90095 ? 74  THR A CG2 1 
ATOM   146  N N   . GLN A 1 58  ? 33.05870 -18.07441 11.48371  1.000 87.99716  ? 75  GLN A N   1 
ATOM   147  C CA  . GLN A 1 58  ? 33.29217 -17.74927 12.88034  1.000 85.47523  ? 75  GLN A CA  1 
ATOM   148  C C   . GLN A 1 58  ? 32.13010 -16.90132 13.39324  1.000 81.49196  ? 75  GLN A C   1 
ATOM   149  O O   . GLN A 1 58  ? 31.34265 -16.36379 12.61288  1.000 85.37439  ? 75  GLN A O   1 
ATOM   150  C CB  . GLN A 1 58  ? 34.61360 -16.99843 13.01843  1.000 83.56421  ? 75  GLN A CB  1 
ATOM   151  C CG  . GLN A 1 58  ? 35.83652 -17.87285 12.79842  1.000 88.47999  ? 75  GLN A CG  1 
ATOM   152  C CD  . GLN A 1 58  ? 37.13752 -17.18684 13.18302  1.000 91.11651  ? 75  GLN A CD  1 
ATOM   153  O OE1 . GLN A 1 58  ? 37.86245 -17.64712 14.06715  1.000 95.53365  ? 75  GLN A OE1 1 
ATOM   154  N NE2 . GLN A 1 58  ? 37.44277 -16.07617 12.50918  1.000 85.17771  ? 75  GLN A NE2 1 
ATOM   155  N N   . ALA A 1 59  ? 32.00907 -16.78458 14.71249  1.000 80.31549  ? 76  ALA A N   1 
ATOM   156  C CA  . ALA A 1 59  ? 30.91504 -16.01522 15.28748  1.000 72.47571  ? 76  ALA A CA  1 
ATOM   157  C C   . ALA A 1 59  ? 31.44515 -14.77895 16.00653  1.000 69.42551  ? 76  ALA A C   1 
ATOM   158  O O   . ALA A 1 59  ? 32.54104 -14.78805 16.56865  1.000 71.90903  ? 76  ALA A O   1 
ATOM   159  C CB  . ALA A 1 59  ? 30.07851 -16.86617 16.23749  1.000 68.28612  ? 76  ALA A CB  1 
ATOM   160  N N   . LEU A 1 60  ? 30.66336 -13.70432 15.96874  1.000 63.50741  ? 77  LEU A N   1 
ATOM   161  C CA  . LEU A 1 60  ? 31.08099 -12.43445 16.54266  1.000 63.43327  ? 77  LEU A CA  1 
ATOM   162  C C   . LEU A 1 60  ? 30.67278 -12.36534 18.01057  1.000 61.39071  ? 77  LEU A C   1 
ATOM   163  O O   . LEU A 1 60  ? 29.49212 -12.50688 18.33868  1.000 57.34351  ? 77  LEU A O   1 
ATOM   164  C CB  . LEU A 1 60  ? 30.46655 -11.26090 15.77171  1.000 62.02400  ? 77  LEU A CB  1 
ATOM   165  C CG  . LEU A 1 60  ? 30.97529 -9.86966  16.18805  1.000 61.87821  ? 77  LEU A CG  1 
ATOM   166  C CD1 . LEU A 1 60  ? 32.49555 -9.77829  16.18106  1.000 65.47344  ? 77  LEU A CD1 1 
ATOM   167  C CD2 . LEU A 1 60  ? 30.38464 -8.77161  15.36348  1.000 63.01599  ? 77  LEU A CD2 1 
ATOM   168  N N   . PHE A 1 61  ? 31.63774 -12.12301 18.89001  1.000 58.70492  ? 78  PHE A N   1 
ATOM   169  C CA  . PHE A 1 61  ? 31.35430 -11.92299 20.30545  1.000 58.83786  ? 78  PHE A CA  1 
ATOM   170  C C   . PHE A 1 61  ? 31.64251 -10.47360 20.69128  1.000 62.00193  ? 78  PHE A C   1 
ATOM   171  O O   . PHE A 1 61  ? 32.80398 -10.06635 20.77370  1.000 62.50360  ? 78  PHE A O   1 
ATOM   172  C CB  . PHE A 1 61  ? 32.17230 -12.87899 21.15394  1.000 61.79409  ? 78  PHE A CB  1 
ATOM   173  C CG  . PHE A 1 61  ? 31.61269 -14.26264 21.20518  1.000 66.67364  ? 78  PHE A CG  1 
ATOM   174  C CD1 . PHE A 1 61  ? 31.99512 -15.21326 20.26153  1.000 64.85268  ? 78  PHE A CD1 1 
ATOM   175  C CD2 . PHE A 1 61  ? 30.70253 -14.62376 22.19983  1.000 66.00398  ? 78  PHE A CD2 1 
ATOM   176  C CE1 . PHE A 1 61  ? 31.48449 -16.49900 20.30667  1.000 67.14711  ? 78  PHE A CE1 1 
ATOM   177  C CE2 . PHE A 1 61  ? 30.18667 -15.91567 22.25550  1.000 65.16325  ? 78  PHE A CE2 1 
ATOM   178  C CZ  . PHE A 1 61  ? 30.57728 -16.85147 21.30671  1.000 67.44454  ? 78  PHE A CZ  1 
ATOM   179  N N   . ASP A 1 62  ? 30.58340 -9.69637  20.93005  1.000 60.22657  ? 79  ASP A N   1 
ATOM   180  C CA  . ASP A 1 62  ? 30.73148 -8.34742  21.45887  1.000 57.01361  ? 79  ASP A CA  1 
ATOM   181  C C   . ASP A 1 62  ? 30.10909 -8.27326  22.85072  1.000 57.22674  ? 79  ASP A C   1 
ATOM   182  O O   . ASP A 1 62  ? 29.09526 -7.59842  23.05777  1.000 55.92298  ? 79  ASP A O   1 
ATOM   183  C CB  . ASP A 1 62  ? 30.09325 -7.33219  20.50855  1.000 57.05984  ? 79  ASP A CB  1 
ATOM   184  C CG  . ASP A 1 62  ? 30.37551 -5.89545  20.92339  1.000 60.56937  ? 79  ASP A CG  1 
ATOM   185  O OD1 . ASP A 1 62  ? 31.40620 -5.70506  21.61871  1.000 61.46898  ? 79  ASP A OD1 1 
ATOM   186  O OD2 . ASP A 1 62  ? 29.58066 -4.97565  20.57070  1.000 58.13087  ? 79  ASP A OD2 1 
ATOM   187  N N   . ILE A 1 63  ? 30.70057 -8.98098  23.81628  1.000 60.47959  ? 80  ILE A N   1 
ATOM   188  C CA  . ILE A 1 63  ? 30.04823 -9.11299  25.11374  1.000 56.45685  ? 80  ILE A CA  1 
ATOM   189  C C   . ILE A 1 63  ? 30.07852 -7.81531  25.89049  1.000 56.42363  ? 80  ILE A C   1 
ATOM   190  O O   . ILE A 1 63  ? 29.25642 -7.62168  26.79138  1.000 55.80915  ? 80  ILE A O   1 
ATOM   191  C CB  . ILE A 1 63  ? 30.68554 -10.26240 25.91293  1.000 56.19268  ? 80  ILE A CB  1 
ATOM   192  C CG1 . ILE A 1 63  ? 30.51127 -11.55550 25.13356  1.000 60.57330  ? 80  ILE A CG1 1 
ATOM   193  C CG2 . ILE A 1 63  ? 30.04647 -10.41896 27.26622  1.000 55.78105  ? 80  ILE A CG2 1 
ATOM   194  C CD1 . ILE A 1 63  ? 29.07110 -11.78287 24.74864  1.000 57.66014  ? 80  ILE A CD1 1 
ATOM   195  N N   . TYR A 1 64  ? 30.96551 -6.89053  25.53172  1.000 60.02967  ? 81  TYR A N   1 
ATOM   196  C CA  . TYR A 1 64  ? 31.20403 -5.70893  26.34608  1.000 61.25134  ? 81  TYR A CA  1 
ATOM   197  C C   . TYR A 1 64  ? 30.59878 -4.43717  25.76421  1.000 57.23308  ? 81  TYR A C   1 
ATOM   198  O O   . TYR A 1 64  ? 30.89522 -3.34667  26.25908  1.000 57.53375  ? 81  TYR A O   1 
ATOM   199  C CB  . TYR A 1 64  ? 32.70481 -5.53347  26.55431  1.000 62.50579  ? 81  TYR A CB  1 
ATOM   200  C CG  . TYR A 1 64  ? 33.32352 -6.54561  27.49155  1.000 62.42401  ? 81  TYR A CG  1 
ATOM   201  C CD1 . TYR A 1 64  ? 33.31196 -6.36151  28.85935  1.000 59.85662  ? 81  TYR A CD1 1 
ATOM   202  C CD2 . TYR A 1 64  ? 33.92226 -7.68848  26.99501  1.000 69.34868  ? 81  TYR A CD2 1 
ATOM   203  C CE1 . TYR A 1 64  ? 33.89010 -7.28478  29.69805  1.000 71.85913  ? 81  TYR A CE1 1 
ATOM   204  C CE2 . TYR A 1 64  ? 34.49737 -8.62619  27.82765  1.000 69.23398  ? 81  TYR A CE2 1 
ATOM   205  C CZ  . TYR A 1 64  ? 34.48536 -8.42115  29.17244  1.000 74.08935  ? 81  TYR A CZ  1 
ATOM   206  O OH  . TYR A 1 64  ? 35.06908 -9.37081  29.98163  1.000 81.09605  ? 81  TYR A OH  1 
ATOM   207  N N   . ASP A 1 65  ? 29.74892 -4.55685  24.74520  1.000 60.67741  ? 82  ASP A N   1 
ATOM   208  C CA  . ASP A 1 65  ? 29.19426 -3.43416  23.97952  1.000 58.91956  ? 82  ASP A CA  1 
ATOM   209  C C   . ASP A 1 65  ? 30.28712 -2.45277  23.55615  1.000 61.01199  ? 82  ASP A C   1 
ATOM   210  O O   . ASP A 1 65  ? 30.28197 -1.28352  23.93100  1.000 63.05730  ? 82  ASP A O   1 
ATOM   211  C CB  . ASP A 1 65  ? 28.09486 -2.71348  24.76350  1.000 57.14618  ? 82  ASP A CB  1 
ATOM   212  C CG  . ASP A 1 65  ? 27.36604 -1.66490  23.92466  1.000 58.43115  ? 82  ASP A CG  1 
ATOM   213  O OD1 . ASP A 1 65  ? 27.50062 -1.68931  22.68158  1.000 66.58099  ? 82  ASP A OD1 1 
ATOM   214  O OD2 . ASP A 1 65  ? 26.65843 -0.79980  24.48885  1.000 59.08467  ? 82  ASP A OD2 1 
ATOM   215  N N   . THR A 1 66  ? 31.24328 -2.94599  22.76419  1.000 59.44327  ? 83  THR A N   1 
ATOM   216  C CA  . THR A 1 66  ? 32.33391 -2.10485  22.29508  1.000 58.44208  ? 83  THR A CA  1 
ATOM   217  C C   . THR A 1 66  ? 32.51710 -2.13643  20.78917  1.000 61.19883  ? 83  THR A C   1 
ATOM   218  O O   . THR A 1 66  ? 33.42620 -1.46442  20.28274  1.000 61.57650  ? 83  THR A O   1 
ATOM   219  C CB  . THR A 1 66  ? 33.65347 -2.49075  22.95750  1.000 56.87341  ? 83  THR A CB  1 
ATOM   220  O OG1 . THR A 1 66  ? 33.89439 -3.87993  22.74421  1.000 64.49775  ? 83  THR A OG1 1 
ATOM   221  C CG2 . THR A 1 66  ? 33.57277 -2.23595  24.42480  1.000 58.92172  ? 83  THR A CG2 1 
ATOM   222  N N   . LEU A 1 67  ? 31.68205 -2.87935  20.06108  1.000 56.23118  ? 84  LEU A N   1 
ATOM   223  C CA  . LEU A 1 67  ? 31.67783 -2.80651  18.60404  1.000 57.13750  ? 84  LEU A CA  1 
ATOM   224  C C   . LEU A 1 67  ? 31.09389 -1.47469  18.18004  1.000 53.39930  ? 84  LEU A C   1 
ATOM   225  O O   . LEU A 1 67  ? 29.88494 -1.25702  18.30277  1.000 53.70845  ? 84  LEU A O   1 
ATOM   226  C CB  . LEU A 1 67  ? 30.86776 -3.94440  17.99257  1.000 58.13493  ? 84  LEU A CB  1 
ATOM   227  C CG  . LEU A 1 67  ? 30.86490 -3.88517  16.46711  1.000 56.59332  ? 84  LEU A CG  1 
ATOM   228  C CD1 . LEU A 1 67  ? 32.29588 -3.76418  15.93177  1.000 58.91333  ? 84  LEU A CD1 1 
ATOM   229  C CD2 . LEU A 1 67  ? 30.21031 -5.11849  15.93931  1.000 57.41182  ? 84  LEU A CD2 1 
ATOM   230  N N   . ASN A 1 68  ? 31.93641 -0.58722  17.66973  1.000 54.92289  ? 85  ASN A N   1 
ATOM   231  C CA  . ASN A 1 68  ? 31.43633 0.67409   17.15116  1.000 54.99220  ? 85  ASN A CA  1 
ATOM   232  C C   . ASN A 1 68  ? 30.81308 0.46530   15.78408  1.000 54.85441  ? 85  ASN A C   1 
ATOM   233  O O   . ASN A 1 68  ? 31.33116 -0.27279  14.94360  1.000 57.93434  ? 85  ASN A O   1 
ATOM   234  C CB  . ASN A 1 68  ? 32.53922 1.70936   17.05386  1.000 55.08054  ? 85  ASN A CB  1 
ATOM   235  C CG  . ASN A 1 68  ? 32.02095 3.03171   16.62702  1.000 53.39991  ? 85  ASN A CG  1 
ATOM   236  O OD1 . ASN A 1 68  ? 31.54148 3.18167   15.52014  1.000 58.96894  ? 85  ASN A OD1 1 
ATOM   237  N ND2 . ASN A 1 68  ? 32.11218 4.01063   17.49746  1.000 58.07536  ? 85  ASN A ND2 1 
ATOM   238  N N   . VAL A 1 69  ? 29.69270 1.13356   15.57173  1.000 54.05589  ? 86  VAL A N   1 
ATOM   239  C CA  . VAL A 1 69  ? 28.89201 0.90330   14.38437  1.000 52.58331  ? 86  VAL A CA  1 
ATOM   240  C C   . VAL A 1 69  ? 29.60264 1.39752   13.12900  1.000 59.18192  ? 86  VAL A C   1 
ATOM   241  O O   . VAL A 1 69  ? 29.55725 0.74833   12.07542  1.000 60.93068  ? 86  VAL A O   1 
ATOM   242  C CB  . VAL A 1 69  ? 27.52592 1.55941   14.60961  1.000 53.28796  ? 86  VAL A CB  1 
ATOM   243  C CG1 . VAL A 1 69  ? 26.92808 1.92223   13.35421  1.000 58.25070  ? 86  VAL A CG1 1 
ATOM   244  C CG2 . VAL A 1 69  ? 26.62307 0.56583   15.30672  1.000 52.42527  ? 86  VAL A CG2 1 
ATOM   245  N N   . ASN A 1 70  ? 30.29353 2.53388   13.22368  1.000 61.45420  ? 87  ASN A N   1 
ATOM   246  C CA  . ASN A 1 70  ? 31.03211 3.09635   12.09785  1.000 61.65120  ? 87  ASN A CA  1 
ATOM   247  C C   . ASN A 1 70  ? 32.25324 2.26973   11.71017  1.000 65.91507  ? 87  ASN A C   1 
ATOM   248  O O   . ASN A 1 70  ? 32.81037 2.48525   10.62510  1.000 72.46011  ? 87  ASN A O   1 
ATOM   249  C CB  . ASN A 1 70  ? 31.43828 4.52922   12.42729  1.000 58.68208  ? 87  ASN A CB  1 
ATOM   250  C CG  . ASN A 1 70  ? 30.24823 5.38492   12.83592  1.000 59.68081  ? 87  ASN A CG  1 
ATOM   251  O OD1 . ASN A 1 70  ? 29.54299 5.96696   11.99581  1.000 58.45077  ? 87  ASN A OD1 1 
ATOM   252  N ND2 . ASN A 1 70  ? 30.01286 5.45948   14.13825  1.000 61.94210  ? 87  ASN A ND2 1 
ATOM   253  N N   . ASP A 1 71  ? 32.63954 1.30778   12.54688  1.000 70.12345  ? 88  ASP A N   1 
ATOM   254  C CA  . ASP A 1 71  ? 33.82142 0.47106   12.34893  1.000 72.78940  ? 88  ASP A CA  1 
ATOM   255  C C   . ASP A 1 71  ? 33.57358 -0.59504  11.28903  1.000 76.27915  ? 88  ASP A C   1 
ATOM   256  O O   . ASP A 1 71  ? 32.70868 -1.46391  11.46790  1.000 76.04533  ? 88  ASP A O   1 
ATOM   257  C CB  . ASP A 1 71  ? 34.20450 -0.18940  13.67188  1.000 71.38131  ? 88  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 71  ? 35.54036 -0.86556  13.60897  1.000 77.01974  ? 88  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 71  ? 36.21159 -0.69256  12.57268  1.000 85.75463  ? 88  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 71  ? 35.92384 -1.56288  14.57731  1.000 75.57693  ? 88  ASP A OD2 1 
ATOM   261  N N   . LYS A 1 72  ? 34.36226 -0.55893  10.20950  1.000 77.69147  ? 89  LYS A N   1 
ATOM   262  C CA  . LYS A 1 72  ? 34.23713 -1.54576  9.14384   1.000 79.38739  ? 89  LYS A CA  1 
ATOM   263  C C   . LYS A 1 72  ? 35.08611 -2.79204  9.38350   1.000 83.11501  ? 89  LYS A C   1 
ATOM   264  O O   . LYS A 1 72  ? 35.01289 -3.72570  8.57827   1.000 82.80324  ? 89  LYS A O   1 
ATOM   265  C CB  . LYS A 1 72  ? 34.60928 -0.94002  7.78452   1.000 79.62545  ? 89  LYS A CB  1 
ATOM   266  C CG  . LYS A 1 72  ? 34.37488 0.57198   7.61180   1.000 93.60651  ? 89  LYS A CG  1 
ATOM   267  C CD  . LYS A 1 72  ? 33.03492 0.94746   6.93898   1.000 89.54356  ? 89  LYS A CD  1 
ATOM   268  C CE  . LYS A 1 72  ? 33.08268 2.41072   6.40253   1.000 90.12206  ? 89  LYS A CE  1 
ATOM   269  N NZ  . LYS A 1 72  ? 31.75172 3.08946   6.11258   1.000 76.10239  ? 89  LYS A NZ  1 
ATOM   270  N N   . SER A 1 73  ? 35.86680 -2.83594  10.47336  1.000 83.47761  ? 90  SER A N   1 
ATOM   271  C CA  . SER A 1 73  ? 36.82671 -3.92162  10.69251  1.000 77.03450  ? 90  SER A CA  1 
ATOM   272  C C   . SER A 1 73  ? 36.16038 -5.28366  10.61759  1.000 80.41806  ? 90  SER A C   1 
ATOM   273  O O   . SER A 1 73  ? 36.66410 -6.19970  9.95717   1.000 86.43662  ? 90  SER A O   1 
ATOM   274  C CB  . SER A 1 73  ? 37.52181 -3.78480  12.05566  1.000 79.14413  ? 90  SER A CB  1 
ATOM   275  O OG  . SER A 1 73  ? 37.94341 -2.46560  12.35621  1.000 81.28132  ? 90  SER A OG  1 
ATOM   276  N N   . PHE A 1 74  ? 35.03402 -5.44498  11.30486  1.000 81.30586  ? 91  PHE A N   1 
ATOM   277  C CA  . PHE A 1 74  ? 34.43785 -6.76212  11.46723  1.000 79.52784  ? 91  PHE A CA  1 
ATOM   278  C C   . PHE A 1 74  ? 33.40895 -7.08336  10.39790  1.000 81.80919  ? 91  PHE A C   1 
ATOM   279  O O   . PHE A 1 74  ? 32.65372 -8.05088  10.55370  1.000 79.35589  ? 91  PHE A O   1 
ATOM   280  C CB  . PHE A 1 74  ? 33.79093 -6.88318  12.83666  1.000 73.59037  ? 91  PHE A CB  1 
ATOM   281  C CG  . PHE A 1 74  ? 34.71264 -6.57391  13.95776  1.000 74.00752  ? 91  PHE A CG  1 
ATOM   282  C CD1 . PHE A 1 74  ? 34.99411 -5.26165  14.29167  1.000 73.98508  ? 91  PHE A CD1 1 
ATOM   283  C CD2 . PHE A 1 74  ? 35.30378 -7.59686  14.68611  1.000 73.99115  ? 91  PHE A CD2 1 
ATOM   284  C CE1 . PHE A 1 74  ? 35.83876 -4.97110  15.33629  1.000 76.77760  ? 91  PHE A CE1 1 
ATOM   285  C CE2 . PHE A 1 74  ? 36.15644 -7.31937  15.73768  1.000 72.76992  ? 91  PHE A CE2 1 
ATOM   286  C CZ  . PHE A 1 74  ? 36.42511 -6.00672  16.06665  1.000 74.11697  ? 91  PHE A CZ  1 
ATOM   287  N N   . GLY A 1 75  ? 33.36132 -6.30538  9.32409   1.000 80.67028  ? 92  GLY A N   1 
ATOM   288  C CA  . GLY A 1 75  ? 32.40053 -6.51983  8.26726   1.000 74.96458  ? 92  GLY A CA  1 
ATOM   289  C C   . GLY A 1 75  ? 31.24499 -5.54182  8.35069   1.000 75.79909  ? 92  GLY A C   1 
ATOM   290  O O   . GLY A 1 75  ? 31.07781 -4.78681  9.31934   1.000 71.82456  ? 92  GLY A O   1 
ATOM   291  N N   . ASP A 1 76  ? 30.43027 -5.58896  7.29525   1.000 72.87789  ? 93  ASP A N   1 
ATOM   292  C CA  . ASP A 1 76  ? 29.33696 -4.64249  7.08022   1.000 75.70551  ? 93  ASP A CA  1 
ATOM   293  C C   . ASP A 1 76  ? 28.08761 -5.14828  7.79903   1.000 77.26848  ? 93  ASP A C   1 
ATOM   294  O O   . ASP A 1 76  ? 27.08606 -5.53697  7.19792   1.000 81.63095  ? 93  ASP A O   1 
ATOM   295  C CB  . ASP A 1 76  ? 29.10713 -4.45090  5.58402   1.000 80.95669  ? 93  ASP A CB  1 
ATOM   296  C CG  . ASP A 1 76  ? 28.33537 -3.16559  5.23837   1.000 86.20859  ? 93  ASP A CG  1 
ATOM   297  O OD1 . ASP A 1 76  ? 28.42959 -2.14363  5.96769   1.000 76.35035  ? 93  ASP A OD1 1 
ATOM   298  O OD2 . ASP A 1 76  ? 27.64930 -3.18022  4.18806   1.000 94.29904  ? 93  ASP A OD2 1 
ATOM   299  N N   . TRP A 1 77  ? 28.17619 -5.14989  9.12940   1.000 71.98443  ? 94  TRP A N   1 
ATOM   300  C CA  . TRP A 1 77  ? 27.04862 -5.58862  9.94559   1.000 69.48344  ? 94  TRP A CA  1 
ATOM   301  C C   . TRP A 1 77  ? 25.89873 -4.60624  9.84255   1.000 70.86368  ? 94  TRP A C   1 
ATOM   302  O O   . TRP A 1 77  ? 24.73977 -4.99134  9.65930   1.000 75.07711  ? 94  TRP A O   1 
ATOM   303  C CB  . TRP A 1 77  ? 27.48179 -5.73465  11.40059  1.000 66.39619  ? 94  TRP A CB  1 
ATOM   304  C CG  . TRP A 1 77  ? 28.30732 -6.91329  11.63916  1.000 63.70570  ? 94  TRP A CG  1 
ATOM   305  C CD1 . TRP A 1 77  ? 29.66676 -6.97732  11.64310  1.000 68.33607  ? 94  TRP A CD1 1 
ATOM   306  C CD2 . TRP A 1 77  ? 27.83582 -8.22753  11.90675  1.000 65.84469  ? 94  TRP A CD2 1 
ATOM   307  N NE1 . TRP A 1 77  ? 30.07963 -8.26204  11.89213  1.000 72.55948  ? 94  TRP A NE1 1 
ATOM   308  C CE2 . TRP A 1 77  ? 28.97137 -9.05383  12.05938  1.000 73.18879  ? 94  TRP A CE2 1 
ATOM   309  C CE3 . TRP A 1 77  ? 26.56470 -8.79149  12.02935  1.000 66.24499  ? 94  TRP A CE3 1 
ATOM   310  C CZ2 . TRP A 1 77  ? 28.87038 -10.42009 12.33503  1.000 71.28420  ? 94  TRP A CZ2 1 
ATOM   311  C CZ3 . TRP A 1 77  ? 26.46388 -10.13022 12.29764  1.000 69.18446  ? 94  TRP A CZ3 1 
ATOM   312  C CH2 . TRP A 1 77  ? 27.61004 -10.93610 12.45051  1.000 71.56441  ? 94  TRP A CH2 1 
ATOM   313  N N   . PHE A 1 78  ? 26.21217 -3.33294  9.95629   1.000 68.86353  ? 95  PHE A N   1 
ATOM   314  C CA  . PHE A 1 78  ? 25.23816 -2.26610  9.95651   1.000 71.81947  ? 95  PHE A CA  1 
ATOM   315  C C   . PHE A 1 78  ? 25.29476 -1.59930  8.60354   1.000 75.21099  ? 95  PHE A C   1 
ATOM   316  O O   . PHE A 1 78  ? 26.36327 -1.52636  7.99682   1.000 79.07489  ? 95  PHE A O   1 
ATOM   317  C CB  . PHE A 1 78  ? 25.56683 -1.30177  11.08214  1.000 67.28122  ? 95  PHE A CB  1 
ATOM   318  C CG  . PHE A 1 78  ? 26.20762 -1.98730  12.24231  1.000 61.13959  ? 95  PHE A CG  1 
ATOM   319  C CD1 . PHE A 1 78  ? 25.44128 -2.70238  13.13384  1.000 58.42053  ? 95  PHE A CD1 1 
ATOM   320  C CD2 . PHE A 1 78  ? 27.56909 -1.94385  12.42333  1.000 59.51650  ? 95  PHE A CD2 1 
ATOM   321  C CE1 . PHE A 1 78  ? 26.02292 -3.34842  14.17559  1.000 60.75625  ? 95  PHE A CE1 1 
ATOM   322  C CE2 . PHE A 1 78  ? 28.15573 -2.58787  13.47104  1.000 54.86972  ? 95  PHE A CE2 1 
ATOM   323  C CZ  . PHE A 1 78  ? 27.39079 -3.28994  14.34132  1.000 59.47664  ? 95  PHE A CZ  1 
ATOM   324  N N   . GLY A 1 79  ? 24.14248 -1.16459  8.11026   1.000 89.65846  ? 96  GLY A N   1 
ATOM   325  C CA  . GLY A 1 79  ? 24.05257 -0.67784  6.74622   1.000 93.44312  ? 96  GLY A CA  1 
ATOM   326  C C   . GLY A 1 79  ? 23.86225 -1.78053  5.72048   1.000 94.64127  ? 96  GLY A C   1 
ATOM   327  O O   . GLY A 1 79  ? 24.62637 -2.74112  5.68575   1.000 87.24771  ? 96  GLY A O   1 
ATOM   328  N N   . ASN A 1 80  ? 22.84995 -1.64406  4.87142   1.000 113.79413 ? 97  ASN A N   1 
ATOM   329  C CA  . ASN A 1 80  ? 22.52154 -2.66665  3.89385   1.000 121.88072 ? 97  ASN A CA  1 
ATOM   330  C C   . ASN A 1 80  ? 23.33121 -2.44793  2.61459   1.000 115.93226 ? 97  ASN A C   1 
ATOM   331  O O   . ASN A 1 80  ? 24.12508 -1.51119  2.50003   1.000 111.16481 ? 97  ASN A O   1 
ATOM   332  C CB  . ASN A 1 80  ? 21.01020 -2.67483  3.62698   1.000 126.06629 ? 97  ASN A CB  1 
ATOM   333  C CG  . ASN A 1 80  ? 20.49157 -1.34939  3.10284   1.000 120.08807 ? 97  ASN A CG  1 
ATOM   334  O OD1 . ASN A 1 80  ? 20.70960 -1.01269  1.94551   1.000 118.94167 ? 97  ASN A OD1 1 
ATOM   335  N ND2 . ASN A 1 80  ? 19.83527 -0.57303  3.96732   1.000 116.10960 ? 97  ASN A ND2 1 
ATOM   336  N N   . SER A 1 81  ? 23.15295 -3.34129  1.64422   1.000 119.88481 ? 98  SER A N   1 
ATOM   337  C CA  . SER A 1 81  ? 23.70758 -3.14138  0.31454   1.000 119.03457 ? 98  SER A CA  1 
ATOM   338  C C   . SER A 1 81  ? 22.60907 -2.81022  -0.69766  1.000 124.14843 ? 98  SER A C   1 
ATOM   339  O O   . SER A 1 81  ? 22.88720 -2.71011  -1.90267  1.000 117.64494 ? 98  SER A O   1 
ATOM   340  C CB  . SER A 1 81  ? 24.52311 -4.37001  -0.10338  1.000 114.89399 ? 98  SER A CB  1 
ATOM   341  O OG  . SER A 1 81  ? 24.86192 -4.32850  -1.47541  1.000 110.33304 ? 98  SER A OG  1 
ATOM   342  N N   . ALA A 1 82  ? 21.36156 -2.61989  -0.21985  1.000 133.58475 ? 99  ALA A N   1 
ATOM   343  C CA  . ALA A 1 82  ? 20.20656 -2.11826  -0.97348  1.000 131.97479 ? 99  ALA A CA  1 
ATOM   344  C C   . ALA A 1 82  ? 20.26300 -0.61356  -1.21143  1.000 129.44056 ? 99  ALA A C   1 
ATOM   345  O O   . ALA A 1 82  ? 19.34824 -0.05997  -1.83663  1.000 126.35690 ? 99  ALA A O   1 
ATOM   346  C CB  . ALA A 1 82  ? 18.90706 -2.46409  -0.23731  1.000 130.90923 ? 99  ALA A CB  1 
ATOM   347  N N   . LEU A 1 83  ? 21.29897 0.04661   -0.68802  1.000 118.89626 ? 100 LEU A N   1 
ATOM   348  C CA  . LEU A 1 83  ? 21.59303 1.44327   -0.94703  1.000 103.51843 ? 100 LEU A CA  1 
ATOM   349  C C   . LEU A 1 83  ? 23.01867 1.65195   -1.41066  1.000 102.07128 ? 100 LEU A C   1 
ATOM   350  O O   . LEU A 1 83  ? 23.35264 2.76245   -1.82765  1.000 105.24335 ? 100 LEU A O   1 
ATOM   351  C CB  . LEU A 1 83  ? 21.38102 2.28800   0.31480   1.000 93.37233  ? 100 LEU A CB  1 
ATOM   352  C CG  . LEU A 1 83  ? 20.01184 2.87989   0.61003   1.000 95.45734  ? 100 LEU A CG  1 
ATOM   353  C CD1 . LEU A 1 83  ? 19.03574 1.80318   1.08632   1.000 112.12931 ? 100 LEU A CD1 1 
ATOM   354  C CD2 . LEU A 1 83  ? 20.16385 3.96877   1.64127   1.000 80.46358  ? 100 LEU A CD2 1 
ATOM   355  N N   . LYS A 1 84  ? 23.86009 0.62140   -1.35117  1.000 105.42655 ? 101 LYS A N   1 
ATOM   356  C CA  . LYS A 1 84  ? 25.29753 0.77089   -1.55097  1.000 110.26625 ? 101 LYS A CA  1 
ATOM   357  C C   . LYS A 1 84  ? 25.62622 1.49070   -2.85424  1.000 113.86642 ? 101 LYS A C   1 
ATOM   358  O O   . LYS A 1 84  ? 26.46217 2.40217   -2.87341  1.000 111.90903 ? 101 LYS A O   1 
ATOM   359  C CB  . LYS A 1 84  ? 25.93622 -0.61963  -1.49694  1.000 117.94052 ? 101 LYS A CB  1 
ATOM   360  C CG  . LYS A 1 84  ? 27.44309 -0.69593  -1.62388  1.000 117.54310 ? 101 LYS A CG  1 
ATOM   361  C CD  . LYS A 1 84  ? 27.89398 -2.16522  -1.56147  1.000 117.35435 ? 101 LYS A CD  1 
ATOM   362  C CE  . LYS A 1 84  ? 27.40051 -2.96133  -2.78148  1.000 117.90231 ? 101 LYS A CE  1 
ATOM   363  N NZ  . LYS A 1 84  ? 27.95562 -2.49932  -4.09130  1.000 111.02690 ? 101 LYS A NZ  1 
ATOM   364  N N   . ASP A 1 85  ? 24.96027 1.11935   -3.94863  1.000 122.52420 ? 102 ASP A N   1 
ATOM   365  C CA  . ASP A 1 85  ? 25.21292 1.74708   -5.23974  1.000 123.29845 ? 102 ASP A CA  1 
ATOM   366  C C   . ASP A 1 85  ? 23.95654 2.31629   -5.88155  1.000 122.18631 ? 102 ASP A C   1 
ATOM   367  O O   . ASP A 1 85  ? 24.00832 2.74622   -7.04342  1.000 122.51907 ? 102 ASP A O   1 
ATOM   368  C CB  . ASP A 1 85  ? 25.87320 0.75409   -6.19405  1.000 128.78328 ? 102 ASP A CB  1 
ATOM   369  C CG  . ASP A 1 85  ? 27.28926 0.43385   -5.79055  1.000 129.25754 ? 102 ASP A CG  1 
ATOM   370  O OD1 . ASP A 1 85  ? 27.84784 1.19677   -4.97241  1.000 124.20750 ? 102 ASP A OD1 1 
ATOM   371  O OD2 . ASP A 1 85  ? 27.83102 -0.58822  -6.26777  1.000 132.45107 ? 102 ASP A OD2 1 
ATOM   372  N N   . LYS A 1 86  ? 22.83315 2.31083   -5.17149  1.000 109.21417 ? 103 LYS A N   1 
ATOM   373  C CA  . LYS A 1 86  ? 21.66170 3.02535   -5.64271  1.000 97.44792  ? 103 LYS A CA  1 
ATOM   374  C C   . LYS A 1 86  ? 21.99708 4.50408   -5.73981  1.000 87.90429  ? 103 LYS A C   1 
ATOM   375  O O   . LYS A 1 86  ? 22.60051 5.07274   -4.82778  1.000 84.10841  ? 103 LYS A O   1 
ATOM   376  C CB  . LYS A 1 86  ? 20.47988 2.79274   -4.69622  1.000 97.97800  ? 103 LYS A CB  1 
ATOM   377  C CG  . LYS A 1 86  ? 19.13773 2.52920   -5.40182  1.000 102.92341 ? 103 LYS A CG  1 
ATOM   378  C CD  . LYS A 1 86  ? 17.97264 2.48155   -4.40637  1.000 102.71939 ? 103 LYS A CD  1 
ATOM   379  C CE  . LYS A 1 86  ? 17.73794 3.83860   -3.73869  1.000 98.39715  ? 103 LYS A CE  1 
ATOM   380  N NZ  . LYS A 1 86  ? 16.43987 3.93025   -3.00202  1.000 92.55738  ? 103 LYS A NZ  1 
ATOM   381  N N   . THR A 1 87  ? 21.66111 5.10585   -6.87783  1.000 86.90705  ? 104 THR A N   1 
ATOM   382  C CA  . THR A 1 87  ? 21.75399 6.55127   -7.04218  1.000 75.79768  ? 104 THR A CA  1 
ATOM   383  C C   . THR A 1 87  ? 20.66216 7.23091   -6.23696  1.000 71.67717  ? 104 THR A C   1 
ATOM   384  O O   . THR A 1 87  ? 19.47790 6.94250   -6.42865  1.000 74.58930  ? 104 THR A O   1 
ATOM   385  C CB  . THR A 1 87  ? 21.61955 6.91540   -8.51213  1.000 71.58668  ? 104 THR A CB  1 
ATOM   386  O OG1 . THR A 1 87  ? 22.79723 6.49975   -9.21531  1.000 84.70211  ? 104 THR A OG1 1 
ATOM   387  C CG2 . THR A 1 87  ? 21.40543 8.39080   -8.67477  1.000 68.94492  ? 104 THR A CG2 1 
ATOM   388  N N   . TYR A 1 88  ? 21.04495 8.13171   -5.33590  1.000 70.12958  ? 105 TYR A N   1 
ATOM   389  C CA  . TYR A 1 88  ? 20.04316 8.76932   -4.49820  1.000 62.81439  ? 105 TYR A CA  1 
ATOM   390  C C   . TYR A 1 88  ? 20.49348 10.17365  -4.12206  1.000 61.50208  ? 105 TYR A C   1 
ATOM   391  O O   . TYR A 1 88  ? 21.65944 10.54093  -4.28086  1.000 62.46815  ? 105 TYR A O   1 
ATOM   392  C CB  . TYR A 1 88  ? 19.73479 7.91952   -3.26510  1.000 54.74613  ? 105 TYR A CB  1 
ATOM   393  C CG  . TYR A 1 88  ? 20.82066 7.81634   -2.21770  1.000 57.40072  ? 105 TYR A CG  1 
ATOM   394  C CD1 . TYR A 1 88  ? 21.11985 8.88166   -1.39438  1.000 55.38788  ? 105 TYR A CD1 1 
ATOM   395  C CD2 . TYR A 1 88  ? 21.52669 6.62426   -2.01930  1.000 67.29705  ? 105 TYR A CD2 1 
ATOM   396  C CE1 . TYR A 1 88  ? 22.10028 8.77698   -0.41132  1.000 58.43229  ? 105 TYR A CE1 1 
ATOM   397  C CE2 . TYR A 1 88  ? 22.51352 6.51430   -1.03370  1.000 61.54759  ? 105 TYR A CE2 1 
ATOM   398  C CZ  . TYR A 1 88  ? 22.79122 7.60281   -0.24059  1.000 58.02676  ? 105 TYR A CZ  1 
ATOM   399  O OH  . TYR A 1 88  ? 23.75439 7.54466   0.73195   1.000 59.25249  ? 105 TYR A OH  1 
ATOM   400  N N   . LEU A 1 89  ? 19.52377 10.95291  -3.63671  1.000 57.22417  ? 106 LEU A N   1 
ATOM   401  C CA  . LEU A 1 89  ? 19.66704 12.36356  -3.26588  1.000 51.28723  ? 106 LEU A CA  1 
ATOM   402  C C   . LEU A 1 89  ? 18.61757 12.66300  -2.20529  1.000 51.92874  ? 106 LEU A C   1 
ATOM   403  O O   . LEU A 1 89  ? 17.41834 12.70372  -2.51356  1.000 59.11789  ? 106 LEU A O   1 
ATOM   404  C CB  . LEU A 1 89  ? 19.46801 13.29188  -4.46260  1.000 49.64524  ? 106 LEU A CB  1 
ATOM   405  C CG  . LEU A 1 89  ? 19.66552 14.75601  -4.05990  1.000 50.10033  ? 106 LEU A CG  1 
ATOM   406  C CD1 . LEU A 1 89  ? 20.92263 14.91359  -3.22497  1.000 53.84095  ? 106 LEU A CD1 1 
ATOM   407  C CD2 . LEU A 1 89  ? 19.63530 15.73635  -5.19778  1.000 47.34862  ? 106 LEU A CD2 1 
ATOM   408  N N   . TYR A 1 90  ? 19.04589 12.91099  -0.97708  1.000 48.80560  ? 107 TYR A N   1 
ATOM   409  C CA  . TYR A 1 90  ? 18.08454 13.05653  0.09835   1.000 48.83405  ? 107 TYR A CA  1 
ATOM   410  C C   . TYR A 1 90  ? 18.51468 14.19067  1.02085   1.000 49.37307  ? 107 TYR A C   1 
ATOM   411  O O   . TYR A 1 90  ? 19.70854 14.45147  1.18241   1.000 49.86260  ? 107 TYR A O   1 
ATOM   412  C CB  . TYR A 1 90  ? 17.94760 11.71218  0.79661   1.000 45.06124  ? 107 TYR A CB  1 
ATOM   413  C CG  . TYR A 1 90  ? 16.75647 11.59438  1.69486   1.000 47.77556  ? 107 TYR A CG  1 
ATOM   414  C CD1 . TYR A 1 90  ? 16.78891 12.10300  2.98709   1.000 50.60041  ? 107 TYR A CD1 1 
ATOM   415  C CD2 . TYR A 1 90  ? 15.58283 11.01438  1.24706   1.000 45.37296  ? 107 TYR A CD2 1 
ATOM   416  C CE1 . TYR A 1 90  ? 15.70141 11.99023  3.83519   1.000 52.98326  ? 107 TYR A CE1 1 
ATOM   417  C CE2 . TYR A 1 90  ? 14.47214 10.91699  2.07389   1.000 50.11748  ? 107 TYR A CE2 1 
ATOM   418  C CZ  . TYR A 1 90  ? 14.53521 11.40139  3.37753   1.000 55.95741  ? 107 TYR A CZ  1 
ATOM   419  O OH  . TYR A 1 90  ? 13.43719 11.31180  4.23074   1.000 58.56733  ? 107 TYR A OH  1 
ATOM   420  N N   . ALA A 1 91  ? 17.53427 14.90433  1.58156   1.000 54.58678  ? 108 ALA A N   1 
ATOM   421  C CA  . ALA A 1 91  ? 17.80128 16.06108  2.43536   1.000 53.50901  ? 108 ALA A CA  1 
ATOM   422  C C   . ALA A 1 91  ? 17.06803 15.90618  3.76072   1.000 55.47316  ? 108 ALA A C   1 
ATOM   423  O O   . ALA A 1 91  ? 15.85704 15.63362  3.77572   1.000 57.76997  ? 108 ALA A O   1 
ATOM   424  C CB  . ALA A 1 91  ? 17.38036 17.37077  1.76333   1.000 52.92280  ? 108 ALA A CB  1 
ATOM   425  N N   . MET A 1 92  ? 17.79376 16.09715  4.86838   1.000 46.41118  ? 109 MET A N   1 
ATOM   426  C CA  . MET A 1 92  ? 17.21151 15.85867  6.17504   1.000 44.66129  ? 109 MET A CA  1 
ATOM   427  C C   . MET A 1 92  ? 17.76835 16.82831  7.20371   1.000 48.49264  ? 109 MET A C   1 
ATOM   428  O O   . MET A 1 92  ? 18.89151 17.32100  7.08205   1.000 48.94234  ? 109 MET A O   1 
ATOM   429  C CB  . MET A 1 92  ? 17.45782 14.42616  6.64827   1.000 46.77963  ? 109 MET A CB  1 
ATOM   430  C CG  . MET A 1 92  ? 18.89026 14.10530  7.03598   1.000 48.77328  ? 109 MET A CG  1 
ATOM   431  S SD  . MET A 1 92  ? 18.96682 12.60649  8.05695   1.000 51.36557  ? 109 MET A SD  1 
ATOM   432  C CE  . MET A 1 92  ? 17.50833 12.76711  9.07624   1.000 48.54958  ? 109 MET A CE  1 
ATOM   433  N N   . ASP A 1 93  ? 16.95907 17.07341  8.23052   1.000 55.70008  ? 110 ASP A N   1 
ATOM   434  C CA  . ASP A 1 93  ? 17.36247 17.79606  9.42773   1.000 56.55140  ? 110 ASP A CA  1 
ATOM   435  C C   . ASP A 1 93  ? 18.11848 16.87395  10.37694  1.000 58.54226  ? 110 ASP A C   1 
ATOM   436  O O   . ASP A 1 93  ? 17.58314 15.85247  10.81712  1.000 58.41770  ? 110 ASP A O   1 
ATOM   437  C CB  . ASP A 1 93  ? 16.11644 18.32966  10.10967  1.000 61.46029  ? 110 ASP A CB  1 
ATOM   438  C CG  . ASP A 1 93  ? 15.52568 19.49798  9.38559   1.000 68.77405  ? 110 ASP A CG  1 
ATOM   439  O OD1 . ASP A 1 93  ? 16.29079 20.12494  8.62249   1.000 72.48832  ? 110 ASP A OD1 1 
ATOM   440  O OD2 . ASP A 1 93  ? 14.29320 19.75278  9.51866   1.000 74.69192  ? 110 ASP A OD2 1 
ATOM   441  N N   . LEU A 1 94  ? 19.34870 17.23280  10.71227  1.000 53.33078  ? 111 LEU A N   1 
ATOM   442  C CA  . LEU A 1 94  ? 20.11026 16.41892  11.64188  1.000 48.81600  ? 111 LEU A CA  1 
ATOM   443  C C   . LEU A 1 94  ? 19.60478 16.63464  13.06414  1.000 54.28371  ? 111 LEU A C   1 
ATOM   444  O O   . LEU A 1 94  ? 19.29024 17.75677  13.46875  1.000 56.69375  ? 111 LEU A O   1 
ATOM   445  C CB  . LEU A 1 94  ? 21.58782 16.76920  11.55191  1.000 44.13168  ? 111 LEU A CB  1 
ATOM   446  C CG  . LEU A 1 94  ? 22.28316 16.42678  10.24894  1.000 43.03285  ? 111 LEU A CG  1 
ATOM   447  C CD1 . LEU A 1 94  ? 23.76204 16.57053  10.43656  1.000 43.71034  ? 111 LEU A CD1 1 
ATOM   448  C CD2 . LEU A 1 94  ? 21.92035 15.03052  9.79597   1.000 41.81649  ? 111 LEU A CD2 1 
ATOM   449  N N   . LEU A 1 95  ? 19.51756 15.54507  13.82186  1.000 55.97906  ? 112 LEU A N   1 
ATOM   450  C CA  . LEU A 1 95  ? 19.30341 15.60439  15.26004  1.000 51.92511  ? 112 LEU A CA  1 
ATOM   451  C C   . LEU A 1 95  ? 20.33911 16.49148  15.93117  1.000 54.75666  ? 112 LEU A C   1 
ATOM   452  O O   . LEU A 1 95  ? 21.40989 16.72131  15.36742  1.000 55.22230  ? 112 LEU A O   1 
ATOM   453  C CB  . LEU A 1 95  ? 19.37941 14.19975  15.83927  1.000 52.93207  ? 112 LEU A CB  1 
ATOM   454  C CG  . LEU A 1 95  ? 18.07246 13.58473  16.27917  1.000 50.90657  ? 112 LEU A CG  1 
ATOM   455  C CD1 . LEU A 1 95  ? 18.37072 12.24915  16.91380  1.000 49.23910  ? 112 LEU A CD1 1 
ATOM   456  C CD2 . LEU A 1 95  ? 17.40680 14.52451  17.27856  1.000 60.46389  ? 112 LEU A CD2 1 
ATOM   457  N N   . ASP A 1 96  ? 20.05534 16.97533  17.13734  1.000 64.00577  ? 113 ASP A N   1 
ATOM   458  C CA  . ASP A 1 96  ? 21.05559 17.74980  17.85181  1.000 63.76699  ? 113 ASP A CA  1 
ATOM   459  C C   . ASP A 1 96  ? 22.28880 16.89885  18.09283  1.000 62.91262  ? 113 ASP A C   1 
ATOM   460  O O   . ASP A 1 96  ? 22.19495 15.70461  18.37543  1.000 62.95013  ? 113 ASP A O   1 
ATOM   461  C CB  . ASP A 1 96  ? 20.50848 18.25434  19.16837  1.000 66.63961  ? 113 ASP A CB  1 
ATOM   462  C CG  . ASP A 1 96  ? 21.59639 18.81054  20.06317  1.000 74.50120  ? 113 ASP A CG  1 
ATOM   463  O OD1 . ASP A 1 96  ? 21.91947 20.03228  19.94603  1.000 75.51003  ? 113 ASP A OD1 1 
ATOM   464  O OD2 . ASP A 1 96  ? 22.11155 18.01789  20.89357  1.000 73.55896  ? 113 ASP A OD2 1 
ATOM   465  N N   . TYR A 1 97  ? 23.45424 17.51999  17.96852  1.000 57.78661  ? 114 TYR A N   1 
ATOM   466  C CA  . TYR A 1 97  ? 24.68420 16.75457  17.83250  1.000 55.00218  ? 114 TYR A CA  1 
ATOM   467  C C   . TYR A 1 97  ? 24.97067 15.91932  19.07727  1.000 57.97913  ? 114 TYR A C   1 
ATOM   468  O O   . TYR A 1 97  ? 25.17058 14.70279  18.97771  1.000 57.20200  ? 114 TYR A O   1 
ATOM   469  C CB  . TYR A 1 97  ? 25.83762 17.69812  17.50313  1.000 57.63775  ? 114 TYR A CB  1 
ATOM   470  C CG  . TYR A 1 97  ? 27.20095 17.05908  17.61335  1.000 60.20080  ? 114 TYR A CG  1 
ATOM   471  C CD1 . TYR A 1 97  ? 27.63623 16.12428  16.68566  1.000 57.24053  ? 114 TYR A CD1 1 
ATOM   472  C CD2 . TYR A 1 97  ? 28.04821 17.37915  18.67508  1.000 60.67106  ? 114 TYR A CD2 1 
ATOM   473  C CE1 . TYR A 1 97  ? 28.87747 15.54171  16.80859  1.000 57.02286  ? 114 TYR A CE1 1 
ATOM   474  C CE2 . TYR A 1 97  ? 29.27647 16.80657  18.80003  1.000 57.53826  ? 114 TYR A CE2 1 
ATOM   475  C CZ  . TYR A 1 97  ? 29.68470 15.89071  17.87025  1.000 57.17254  ? 114 TYR A CZ  1 
ATOM   476  O OH  . TYR A 1 97  ? 30.92064 15.32411  18.00150  1.000 65.73160  ? 114 TYR A OH  1 
ATOM   477  N N   . ASN A 1 98  ? 24.99342 16.54316  20.26252  1.000 59.96202  ? 115 ASN A N   1 
ATOM   478  C CA  . ASN A 1 98  ? 25.26143 15.77133  21.47834  1.000 59.01485  ? 115 ASN A CA  1 
ATOM   479  C C   . ASN A 1 98  ? 24.24734 14.66160  21.65338  1.000 60.39213  ? 115 ASN A C   1 
ATOM   480  O O   . ASN A 1 98  ? 24.60534 13.52789  21.99285  1.000 61.02152  ? 115 ASN A O   1 
ATOM   481  C CB  . ASN A 1 98  ? 25.22883 16.65313  22.70969  1.000 62.36472  ? 115 ASN A CB  1 
ATOM   482  C CG  . ASN A 1 98  ? 26.14330 17.80278  22.59770  1.000 66.68238  ? 115 ASN A CG  1 
ATOM   483  O OD1 . ASN A 1 98  ? 25.79932 18.82256  22.00241  1.000 73.23426  ? 115 ASN A OD1 1 
ATOM   484  N ND2 . ASN A 1 98  ? 27.33553 17.66139  23.15457  1.000 71.08188  ? 115 ASN A ND2 1 
ATOM   485  N N   . ASN A 1 99  ? 22.96996 14.98068  21.45230  1.000 62.24378  ? 116 ASN A N   1 
ATOM   486  C CA  . ASN A 1 99  ? 21.93126 13.97016  21.55797  1.000 60.62303  ? 116 ASN A CA  1 
ATOM   487  C C   . ASN A 1 99  ? 22.19803 12.83213  20.59128  1.000 56.59114  ? 116 ASN A C   1 
ATOM   488  O O   . ASN A 1 99  ? 22.19777 11.65970  20.98544  1.000 55.66037  ? 116 ASN A O   1 
ATOM   489  C CB  . ASN A 1 99  ? 20.56741 14.62422  21.33184  1.000 64.31234  ? 116 ASN A CB  1 
ATOM   490  C CG  . ASN A 1 99  ? 19.43486 13.61780  21.23933  1.000 69.64525  ? 116 ASN A CG  1 
ATOM   491  O OD1 . ASN A 1 99  ? 18.51044 13.81041  20.44095  1.000 73.86361  ? 116 ASN A OD1 1 
ATOM   492  N ND2 . ASN A 1 99  ? 19.51137 12.52090  22.01819  1.000 63.57449  ? 116 ASN A ND2 1 
ATOM   493  N N   . TYR A 1 100 ? 22.49377 13.16593  19.33090  1.000 56.11103  ? 117 TYR A N   1 
ATOM   494  C CA  . TYR A 1 100 ? 22.76367 12.13803  18.32775  1.000 52.95965  ? 117 TYR A CA  1 
ATOM   495  C C   . TYR A 1 100 ? 23.93702 11.25426  18.73606  1.000 49.77942  ? 117 TYR A C   1 
ATOM   496  O O   . TYR A 1 100 ? 23.86640 10.02788  18.61642  1.000 44.23883  ? 117 TYR A O   1 
ATOM   497  C CB  . TYR A 1 100 ? 23.01751 12.78069  16.96259  1.000 48.53125  ? 117 TYR A CB  1 
ATOM   498  C CG  . TYR A 1 100 ? 23.33313 11.76571  15.89516  1.000 44.63263  ? 117 TYR A CG  1 
ATOM   499  C CD1 . TYR A 1 100 ? 22.31824 11.10144  15.23998  1.000 44.90483  ? 117 TYR A CD1 1 
ATOM   500  C CD2 . TYR A 1 100 ? 24.64324 11.46686  15.54625  1.000 43.98079  ? 117 TYR A CD2 1 
ATOM   501  C CE1 . TYR A 1 100 ? 22.58027 10.15555  14.27559  1.000 41.87951  ? 117 TYR A CE1 1 
ATOM   502  C CE2 . TYR A 1 100 ? 24.91254 10.53110  14.57211  1.000 45.44559  ? 117 TYR A CE2 1 
ATOM   503  C CZ  . TYR A 1 100 ? 23.86350 9.88225   13.94068  1.000 39.99110  ? 117 TYR A CZ  1 
ATOM   504  O OH  . TYR A 1 100 ? 24.07625 8.94222   12.97727  1.000 41.39983  ? 117 TYR A OH  1 
ATOM   505  N N   . LEU A 1 101 ? 25.02252 11.86791  19.22794  1.000 50.06299  ? 118 LEU A N   1 
ATOM   506  C CA  . LEU A 1 101 ? 26.22890 11.12292  19.57967  1.000 48.69065  ? 118 LEU A CA  1 
ATOM   507  C C   . LEU A 1 101 ? 25.93027 10.01975  20.57271  1.000 52.24627  ? 118 LEU A C   1 
ATOM   508  O O   . LEU A 1 101 ? 26.47257 8.90758   20.47241  1.000 52.25067  ? 118 LEU A O   1 
ATOM   509  C CB  . LEU A 1 101 ? 27.27387 12.04085  20.20413  1.000 49.81582  ? 118 LEU A CB  1 
ATOM   510  C CG  . LEU A 1 101 ? 28.34463 12.76645  19.39951  1.000 54.83220  ? 118 LEU A CG  1 
ATOM   511  C CD1 . LEU A 1 101 ? 29.51279 13.05962  20.29816  1.000 55.85737  ? 118 LEU A CD1 1 
ATOM   512  C CD2 . LEU A 1 101 ? 28.79132 11.97716  18.23097  1.000 56.51865  ? 118 LEU A CD2 1 
ATOM   513  N N   . SER A 1 102 ? 25.08993 10.31582  21.55658  1.000 48.18776  ? 119 SER A N   1 
ATOM   514  C CA  . SER A 1 102 ? 24.93060 9.41799   22.67863  1.000 44.95623  ? 119 SER A CA  1 
ATOM   515  C C   . SER A 1 102 ? 23.93678 8.30216   22.41288  1.000 44.95777  ? 119 SER A C   1 
ATOM   516  O O   . SER A 1 102 ? 23.77359 7.43553   23.28189  1.000 49.06972  ? 119 SER A O   1 
ATOM   517  C CB  . SER A 1 102 ? 24.50863 10.20124  23.91392  1.000 48.25867  ? 119 SER A CB  1 
ATOM   518  O OG  . SER A 1 102 ? 23.26184 10.80608  23.67896  1.000 51.83795  ? 119 SER A OG  1 
ATOM   519  N N   . ILE A 1 103 ? 23.26048 8.29526   21.26137  1.000 45.34421  ? 120 ILE A N   1 
ATOM   520  C CA  . ILE A 1 103 ? 22.29962 7.24666   20.94538  1.000 44.11028  ? 120 ILE A CA  1 
ATOM   521  C C   . ILE A 1 103 ? 22.55690 6.58601   19.61139  1.000 39.78201  ? 120 ILE A C   1 
ATOM   522  O O   . ILE A 1 103 ? 21.89556 5.60662   19.29095  1.000 39.03004  ? 120 ILE A O   1 
ATOM   523  C CB  . ILE A 1 103 ? 20.83218 7.73840   21.01990  1.000 42.66377  ? 120 ILE A CB  1 
ATOM   524  C CG1 . ILE A 1 103 ? 20.54387 8.81087   19.96991  1.000 48.10912  ? 120 ILE A CG1 1 
ATOM   525  C CG2 . ILE A 1 103 ? 20.49553 8.22840   22.40723  1.000 41.16708  ? 120 ILE A CG2 1 
ATOM   526  C CD1 . ILE A 1 103 ? 19.20990 9.50489   20.14766  1.000 45.86672  ? 120 ILE A CD1 1 
ATOM   527  N N   . GLU A 1 104 ? 23.51716 7.07441   18.81866  1.000 42.54816  ? 121 GLU A N   1 
ATOM   528  C CA  . GLU A 1 104 ? 23.74079 6.50279   17.49346  1.000 41.70481  ? 121 GLU A CA  1 
ATOM   529  C C   . GLU A 1 104 ? 24.13429 5.03293   17.59060  1.000 47.62282  ? 121 GLU A C   1 
ATOM   530  O O   . GLU A 1 104 ? 23.50580 4.17025   16.95900  1.000 46.76708  ? 121 GLU A O   1 
ATOM   531  C CB  . GLU A 1 104 ? 24.81140 7.28195   16.73114  1.000 41.81333  ? 121 GLU A CB  1 
ATOM   532  C CG  . GLU A 1 104 ? 25.01740 6.75031   15.30234  1.000 48.20672  ? 121 GLU A CG  1 
ATOM   533  C CD  . GLU A 1 104 ? 26.39549 7.10134   14.71520  1.000 54.01254  ? 121 GLU A CD  1 
ATOM   534  O OE1 . GLU A 1 104 ? 27.40283 6.59715   15.28373  1.000 54.01065  ? 121 GLU A OE1 1 
ATOM   535  O OE2 . GLU A 1 104 ? 26.47047 7.81538   13.67202  1.000 52.67727  ? 121 GLU A OE2 1 
ATOM   536  N N   . ASN A 1 105 ? 25.18092 4.72265   18.37950  1.000 47.92849  ? 122 ASN A N   1 
ATOM   537  C CA  . ASN A 1 105 ? 25.61829 3.33064   18.49011  1.000 45.00921  ? 122 ASN A CA  1 
ATOM   538  C C   . ASN A 1 105 ? 24.53205 2.41992   19.04027  1.000 46.60147  ? 122 ASN A C   1 
ATOM   539  O O   . ASN A 1 105 ? 24.27940 1.36439   18.42965  1.000 50.07956  ? 122 ASN A O   1 
ATOM   540  C CB  . ASN A 1 105 ? 26.86221 3.19352   19.36643  1.000 44.96777  ? 122 ASN A CB  1 
ATOM   541  C CG  . ASN A 1 105 ? 27.91967 2.30018   18.74128  1.000 48.97431  ? 122 ASN A CG  1 
ATOM   542  O OD1 . ASN A 1 105 ? 28.14829 2.35241   17.54194  1.000 50.59735  ? 122 ASN A OD1 1 
ATOM   543  N ND2 . ASN A 1 105 ? 28.44339 1.36218   19.52754  1.000 53.51988  ? 122 ASN A ND2 1 
ATOM   544  N N   . PRO A 1 106 ? 23.88146 2.72075   20.17672  1.000 45.04473  ? 123 PRO A N   1 
ATOM   545  C CA  . PRO A 1 106 ? 22.88202 1.77482   20.68567  1.000 40.78170  ? 123 PRO A CA  1 
ATOM   546  C C   . PRO A 1 106 ? 21.78669 1.53375   19.67599  1.000 44.20247  ? 123 PRO A C   1 
ATOM   547  O O   . PRO A 1 106 ? 21.44009 0.37805   19.42092  1.000 47.00294  ? 123 PRO A O   1 
ATOM   548  C CB  . PRO A 1 106 ? 22.35024 2.47417   21.93960  1.000 39.99343  ? 123 PRO A CB  1 
ATOM   549  C CG  . PRO A 1 106 ? 23.40871 3.31917   22.36834  1.000 40.85503  ? 123 PRO A CG  1 
ATOM   550  C CD  . PRO A 1 106 ? 24.02759 3.85478   21.10289  1.000 42.60036  ? 123 PRO A CD  1 
ATOM   551  N N   . ILE A 1 107 ? 21.25514 2.60594   19.06960  1.000 42.83502  ? 124 ILE A N   1 
ATOM   552  C CA  . ILE A 1 107 ? 20.08826 2.48727   18.20140  1.000 43.79085  ? 124 ILE A CA  1 
ATOM   553  C C   . ILE A 1 107 ? 20.43876 1.71712   16.93055  1.000 49.08213  ? 124 ILE A C   1 
ATOM   554  O O   . ILE A 1 107 ? 19.67282 0.85435   16.47594  1.000 48.80799  ? 124 ILE A O   1 
ATOM   555  C CB  . ILE A 1 107 ? 19.51689 3.88343   17.89212  1.000 42.47244  ? 124 ILE A CB  1 
ATOM   556  C CG1 . ILE A 1 107 ? 18.96474 4.53439   19.15318  1.000 44.93704  ? 124 ILE A CG1 1 
ATOM   557  C CG2 . ILE A 1 107 ? 18.41232 3.80782   16.86675  1.000 42.37325  ? 124 ILE A CG2 1 
ATOM   558  C CD1 . ILE A 1 107 ? 18.08234 5.74581   18.86755  1.000 45.65344  ? 124 ILE A CD1 1 
ATOM   559  N N   . ILE A 1 108 ? 21.60591 1.99169   16.34541  1.000 48.58432  ? 125 ILE A N   1 
ATOM   560  C CA  . ILE A 1 108 ? 21.96865 1.29839   15.11468  1.000 53.74180  ? 125 ILE A CA  1 
ATOM   561  C C   . ILE A 1 108 ? 22.28512 -0.16471  15.40293  1.000 55.14714  ? 125 ILE A C   1 
ATOM   562  O O   . ILE A 1 108 ? 21.81654 -1.06833  14.69877  1.000 59.66181  ? 125 ILE A O   1 
ATOM   563  C CB  . ILE A 1 108 ? 23.13795 2.00572   14.41031  1.000 51.02240  ? 125 ILE A CB  1 
ATOM   564  C CG1 . ILE A 1 108 ? 22.72975 3.41667   14.00203  1.000 51.95996  ? 125 ILE A CG1 1 
ATOM   565  C CG2 . ILE A 1 108 ? 23.49540 1.24797   13.17776  1.000 54.96081  ? 125 ILE A CG2 1 
ATOM   566  C CD1 . ILE A 1 108 ? 21.40647 3.47368   13.24822  1.000 52.98828  ? 125 ILE A CD1 1 
ATOM   567  N N   . LYS A 1 109 ? 23.08603 -0.41974  16.44300  1.000 51.19927  ? 126 LYS A N   1 
ATOM   568  C CA  . LYS A 1 109 ? 23.45488 -1.79233  16.77343  1.000 50.99818  ? 126 LYS A CA  1 
ATOM   569  C C   . LYS A 1 109 ? 22.22590 -2.62351  17.14788  1.000 51.36344  ? 126 LYS A C   1 
ATOM   570  O O   . LYS A 1 109 ? 22.04756 -3.73312  16.64233  1.000 53.58695  ? 126 LYS A O   1 
ATOM   571  C CB  . LYS A 1 109 ? 24.48614 -1.82070  17.90254  1.000 47.19722  ? 126 LYS A CB  1 
ATOM   572  C CG  . LYS A 1 109 ? 25.21815 -3.12123  17.90044  1.000 49.86468  ? 126 LYS A CG  1 
ATOM   573  C CD  . LYS A 1 109 ? 26.63972 -3.06387  18.36192  1.000 51.61005  ? 126 LYS A CD  1 
ATOM   574  C CE  . LYS A 1 109 ? 26.72605 -2.45547  19.71688  1.000 52.37704  ? 126 LYS A CE  1 
ATOM   575  N NZ  . LYS A 1 109 ? 28.07702 -2.70433  20.27224  1.000 57.20771  ? 126 LYS A NZ  1 
ATOM   576  N N   . THR A 1 110 ? 21.37704 -2.10678  18.04733  1.000 47.99175  ? 127 THR A N   1 
ATOM   577  C CA  . THR A 1 110 ? 20.11886 -2.76499  18.39017  1.000 43.54924  ? 127 THR A CA  1 
ATOM   578  C C   . THR A 1 110 ? 19.32473 -3.13863  17.15776  1.000 50.15905  ? 127 THR A C   1 
ATOM   579  O O   . THR A 1 110 ? 18.74861 -4.22716  17.07784  1.000 50.33649  ? 127 THR A O   1 
ATOM   580  C CB  . THR A 1 110 ? 19.26421 -1.84524  19.25934  1.000 44.87511  ? 127 THR A CB  1 
ATOM   581  O OG1 . THR A 1 110 ? 19.89240 -1.66717  20.52186  1.000 46.17742  ? 127 THR A OG1 1 
ATOM   582  C CG2 . THR A 1 110 ? 17.85787 -2.39673  19.46607  1.000 47.96080  ? 127 THR A CG2 1 
ATOM   583  N N   . ARG A 1 111 ? 19.25614 -2.23521  16.19120  1.000 56.27761  ? 128 ARG A N   1 
ATOM   584  C CA  . ARG A 1 111 ? 18.36186 -2.46575  15.07008  1.000 56.49774  ? 128 ARG A CA  1 
ATOM   585  C C   . ARG A 1 111 ? 18.88284 -3.59309  14.18546  1.000 59.05786  ? 128 ARG A C   1 
ATOM   586  O O   . ARG A 1 111 ? 18.11836 -4.46236  13.76356  1.000 57.88503  ? 128 ARG A O   1 
ATOM   587  C CB  . ARG A 1 111 ? 18.18961 -1.17155  14.28591  1.000 63.58127  ? 128 ARG A CB  1 
ATOM   588  C CG  . ARG A 1 111 ? 17.09146 -1.26405  13.29411  1.000 71.57742  ? 128 ARG A CG  1 
ATOM   589  C CD  . ARG A 1 111 ? 16.86744 0.02251   12.56624  1.000 77.73859  ? 128 ARG A CD  1 
ATOM   590  N NE  . ARG A 1 111 ? 15.72014 -0.12400  11.68721  1.000 75.88725  ? 128 ARG A NE  1 
ATOM   591  C CZ  . ARG A 1 111 ? 14.48141 0.01596   12.13273  1.000 78.18883  ? 128 ARG A CZ  1 
ATOM   592  N NH1 . ARG A 1 111 ? 14.24413 0.34035   13.40141  1.000 76.00416  ? 128 ARG A NH1 1 
ATOM   593  N NH2 . ARG A 1 111 ? 13.45989 -0.20228  11.30210  1.000 81.17385  ? 128 ARG A NH2 1 
ATOM   594  N N   . ALA A 1 112 ? 20.18558 -3.61155  13.91836  1.000 62.17724  ? 129 ALA A N   1 
ATOM   595  C CA  . ALA A 1 112 ? 20.77458 -4.70750  13.16386  1.000 62.03769  ? 129 ALA A CA  1 
ATOM   596  C C   . ALA A 1 112 ? 20.68838 -6.01263  13.93796  1.000 56.57539  ? 129 ALA A C   1 
ATOM   597  O O   . ALA A 1 112 ? 20.06687 -6.97681  13.48162  1.000 64.15852  ? 129 ALA A O   1 
ATOM   598  C CB  . ALA A 1 112 ? 22.22513 -4.38081  12.82620  1.000 69.67933  ? 129 ALA A CB  1 
ATOM   599  N N   . MET A 1 113 ? 21.29877 -6.05718  15.12712  1.000 54.68960  ? 130 MET A N   1 
ATOM   600  C CA  . MET A 1 113 ? 21.40681 -7.30501  15.88767  1.000 50.80846  ? 130 MET A CA  1 
ATOM   601  C C   . MET A 1 113 ? 20.03453 -7.81320  16.32001  1.000 49.83302  ? 130 MET A C   1 
ATOM   602  O O   . MET A 1 113 ? 19.72633 -8.99914  16.17758  1.000 53.91379  ? 130 MET A O   1 
ATOM   603  C CB  . MET A 1 113 ? 22.27187 -7.09911  17.12977  1.000 48.08815  ? 130 MET A CB  1 
ATOM   604  C CG  . MET A 1 113 ? 23.66717 -6.58913  16.87521  1.000 50.47650  ? 130 MET A CG  1 
ATOM   605  S SD  . MET A 1 113 ? 24.67413 -7.63215  15.83838  1.000 55.88241  ? 130 MET A SD  1 
ATOM   606  C CE  . MET A 1 113 ? 24.62942 -6.70669  14.32466  1.000 66.75391  ? 130 MET A CE  1 
ATOM   607  N N   . GLY A 1 114 ? 19.20699 -6.93539  16.88381  1.000 48.37788  ? 131 GLY A N   1 
ATOM   608  C CA  . GLY A 1 114 ? 17.90808 -7.34870  17.37120  1.000 48.51956  ? 131 GLY A CA  1 
ATOM   609  C C   . GLY A 1 114 ? 16.93644 -7.78882  16.29774  1.000 50.64514  ? 131 GLY A C   1 
ATOM   610  O O   . GLY A 1 114 ? 15.95500 -8.46288  16.61468  1.000 48.26421  ? 131 GLY A O   1 
ATOM   611  N N   . THR A 1 115 ? 17.17278 -7.42298  15.03539  1.000 55.92880  ? 132 THR A N   1 
ATOM   612  C CA  . THR A 1 115 ? 16.28597 -7.89776  13.97540  1.000 54.06534  ? 132 THR A CA  1 
ATOM   613  C C   . THR A 1 115 ? 16.44400 -9.39046  13.73095  1.000 57.20692  ? 132 THR A C   1 
ATOM   614  O O   . THR A 1 115 ? 15.45356 -10.07315 13.45101  1.000 56.81387  ? 132 THR A O   1 
ATOM   615  C CB  . THR A 1 115 ? 16.52257 -7.11610  12.69069  1.000 50.98852  ? 132 THR A CB  1 
ATOM   616  O OG1 . THR A 1 115 ? 16.15442 -5.75395  12.90656  1.000 55.25516  ? 132 THR A OG1 1 
ATOM   617  C CG2 . THR A 1 115 ? 15.70535 -7.66020  11.57648  1.000 55.24373  ? 132 THR A CG2 1 
ATOM   618  N N   . TYR A 1 116 ? 17.65583 -9.92805  13.90190  1.000 58.44726  ? 133 TYR A N   1 
ATOM   619  C CA  . TYR A 1 116 ? 17.97380 -11.27973 13.46391  1.000 54.77496  ? 133 TYR A CA  1 
ATOM   620  C C   . TYR A 1 116 ? 18.22271 -12.27615 14.59232  1.000 55.12427  ? 133 TYR A C   1 
ATOM   621  O O   . TYR A 1 116 ? 18.33543 -13.47483 14.32056  1.000 58.88421  ? 133 TYR A O   1 
ATOM   622  C CB  . TYR A 1 116 ? 19.18415 -11.20670 12.52853  1.000 60.16877  ? 133 TYR A CB  1 
ATOM   623  C CG  . TYR A 1 116 ? 18.78971 -10.50867 11.25771  1.000 68.80317  ? 133 TYR A CG  1 
ATOM   624  C CD1 . TYR A 1 116 ? 17.80311 -11.05222 10.43914  1.000 66.79232  ? 133 TYR A CD1 1 
ATOM   625  C CD2 . TYR A 1 116 ? 19.32163 -9.27057  10.91825  1.000 69.60408  ? 133 TYR A CD2 1 
ATOM   626  C CE1 . TYR A 1 116 ? 17.39180 -10.41491 9.29147   1.000 68.85079  ? 133 TYR A CE1 1 
ATOM   627  C CE2 . TYR A 1 116 ? 18.91009 -8.62541  9.77170   1.000 77.80921  ? 133 TYR A CE2 1 
ATOM   628  C CZ  . TYR A 1 116 ? 17.93994 -9.20739  8.96384   1.000 80.22677  ? 133 TYR A CZ  1 
ATOM   629  O OH  . TYR A 1 116 ? 17.50276 -8.60057  7.81263   1.000 99.29397  ? 133 TYR A OH  1 
ATOM   630  N N   . ALA A 1 117 ? 18.25629 -11.83205 15.84121  1.000 49.98823  ? 134 ALA A N   1 
ATOM   631  C CA  . ALA A 1 117 ? 18.58542 -12.71018 16.95161  1.000 49.78988  ? 134 ALA A CA  1 
ATOM   632  C C   . ALA A 1 117 ? 17.52000 -13.79339 17.15182  1.000 53.05665  ? 134 ALA A C   1 
ATOM   633  O O   . ALA A 1 117 ? 16.35550 -13.62358 16.77037  1.000 53.69942  ? 134 ALA A O   1 
ATOM   634  C CB  . ALA A 1 117 ? 18.74476 -11.88124 18.21936  1.000 46.17236  ? 134 ALA A CB  1 
ATOM   635  N N   . ASP A 1 118 ? 17.93798 -14.93282 17.74382  1.000 48.26350  ? 135 ASP A N   1 
ATOM   636  C CA  . ASP A 1 118 ? 17.00927 -15.98922 18.14605  1.000 48.10695  ? 135 ASP A CA  1 
ATOM   637  C C   . ASP A 1 118 ? 16.71568 -15.98697 19.63394  1.000 48.52915  ? 135 ASP A C   1 
ATOM   638  O O   . ASP A 1 118 ? 15.76253 -16.65309 20.06653  1.000 51.38621  ? 135 ASP A O   1 
ATOM   639  C CB  . ASP A 1 118 ? 17.53943 -17.38839 17.81948  1.000 50.83696  ? 135 ASP A CB  1 
ATOM   640  C CG  . ASP A 1 118 ? 18.08719 -17.50163 16.44588  1.000 61.50150  ? 135 ASP A CG  1 
ATOM   641  O OD1 . ASP A 1 118 ? 17.30097 -17.76376 15.48886  1.000 63.86863  ? 135 ASP A OD1 1 
ATOM   642  O OD2 . ASP A 1 118 ? 19.32896 -17.34842 16.34853  1.000 62.44027  ? 135 ASP A OD2 1 
ATOM   643  N N   . LEU A 1 119 ? 17.55758 -15.33053 20.42497  1.000 46.50137  ? 136 LEU A N   1 
ATOM   644  C CA  . LEU A 1 119 ? 17.32104 -15.16466 21.84488  1.000 46.14695  ? 136 LEU A CA  1 
ATOM   645  C C   . LEU A 1 119 ? 17.63224 -13.71601 22.14916  1.000 43.85445  ? 136 LEU A C   1 
ATOM   646  O O   . LEU A 1 119 ? 18.67862 -13.21004 21.73254  1.000 41.21868  ? 136 LEU A O   1 
ATOM   647  C CB  . LEU A 1 119 ? 18.20344 -16.08708 22.69128  1.000 48.40391  ? 136 LEU A CB  1 
ATOM   648  C CG  . LEU A 1 119 ? 17.93753 -16.12332 24.20129  1.000 46.63934  ? 136 LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 119 ? 16.54450 -16.65631 24.51417  1.000 50.82846  ? 136 LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 119 ? 18.98337 -16.92305 24.86939  1.000 48.22650  ? 136 LEU A CD2 1 
ATOM   651  N N   . ILE A 1 120 ? 16.70851 -13.04705 22.82957  1.000 43.88246  ? 137 ILE A N   1 
ATOM   652  C CA  . ILE A 1 120 ? 16.91187 -11.69159 23.32437  1.000 44.26888  ? 137 ILE A CA  1 
ATOM   653  C C   . ILE A 1 120 ? 16.67293 -11.67223 24.82645  1.000 44.42647  ? 137 ILE A C   1 
ATOM   654  O O   . ILE A 1 120 ? 15.61073 -12.09909 25.29815  1.000 46.67265  ? 137 ILE A O   1 
ATOM   655  C CB  . ILE A 1 120 ? 16.00556 -10.67659 22.60675  1.000 42.38218  ? 137 ILE A CB  1 
ATOM   656  C CG1 . ILE A 1 120 ? 16.27519 -10.72394 21.09815  1.000 41.19242  ? 137 ILE A CG1 1 
ATOM   657  C CG2 . ILE A 1 120 ? 16.16212 -9.30215  23.23620  1.000 41.20888  ? 137 ILE A CG2 1 
ATOM   658  C CD1 . ILE A 1 120 ? 15.72345 -9.57158  20.32430  1.000 39.11338  ? 137 ILE A CD1 1 
ATOM   659  N N   . ILE A 1 121 ? 17.66250 -11.19234 25.57344  1.000 39.57169  ? 138 ILE A N   1 
ATOM   660  C CA  . ILE A 1 121 ? 17.53064 -10.95236 27.00233  1.000 44.04215  ? 138 ILE A CA  1 
ATOM   661  C C   . ILE A 1 121 ? 17.49672 -9.44878  27.22619  1.000 45.83592  ? 138 ILE A C   1 
ATOM   662  O O   . ILE A 1 121 ? 18.33264 -8.71970  26.68129  1.000 48.30555  ? 138 ILE A O   1 
ATOM   663  C CB  . ILE A 1 121 ? 18.69199 -11.58161 27.77989  1.000 47.48966  ? 138 ILE A CB  1 
ATOM   664  C CG1 . ILE A 1 121 ? 18.91296 -13.01974 27.33167  1.000 45.33317  ? 138 ILE A CG1 1 
ATOM   665  C CG2 . ILE A 1 121 ? 18.41754 -11.49677 29.26439  1.000 47.20324  ? 138 ILE A CG2 1 
ATOM   666  C CD1 . ILE A 1 121 ? 19.79269 -13.79163 28.27348  1.000 47.24015  ? 138 ILE A CD1 1 
ATOM   667  N N   . ILE A 1 122 ? 16.54349 -8.97434  28.01926  1.000 42.85018  ? 139 ILE A N   1 
ATOM   668  C CA  . ILE A 1 122 ? 16.48929 -7.55952  28.36626  1.000 44.42165  ? 139 ILE A CA  1 
ATOM   669  C C   . ILE A 1 122 ? 16.58948 -7.46494  29.87084  1.000 46.08597  ? 139 ILE A C   1 
ATOM   670  O O   . ILE A 1 122 ? 15.80361 -8.09091  30.59061  1.000 45.39208  ? 139 ILE A O   1 
ATOM   671  C CB  . ILE A 1 122 ? 15.21999 -6.87371  27.85398  1.000 43.44477  ? 139 ILE A CB  1 
ATOM   672  C CG1 . ILE A 1 122 ? 14.85263 -7.42814  26.47620  1.000 41.29522  ? 139 ILE A CG1 1 
ATOM   673  C CG2 . ILE A 1 122 ? 15.44655 -5.37976  27.80596  1.000 41.43907  ? 139 ILE A CG2 1 
ATOM   674  C CD1 . ILE A 1 122 ? 13.61420 -6.86913  25.90676  1.000 40.88101  ? 139 ILE A CD1 1 
ATOM   675  N N   . THR A 1 123 ? 17.57256 -6.71155  30.34218  1.000 47.73788  ? 140 THR A N   1 
ATOM   676  C CA  . THR A 1 123 ? 17.93963 -6.66618  31.74945  1.000 49.21459  ? 140 THR A CA  1 
ATOM   677  C C   . THR A 1 123 ? 17.79662 -5.22638  32.20848  1.000 51.30879  ? 140 THR A C   1 
ATOM   678  O O   . THR A 1 123 ? 18.25735 -4.30647  31.52112  1.000 52.14401  ? 140 THR A O   1 
ATOM   679  C CB  . THR A 1 123 ? 19.37871 -7.15435  31.96354  1.000 50.78964  ? 140 THR A CB  1 
ATOM   680  O OG1 . THR A 1 123 ? 19.51818 -8.48441  31.45488  1.000 55.11017  ? 140 THR A OG1 1 
ATOM   681  C CG2 . THR A 1 123 ? 19.73032 -7.16232  33.40927  1.000 49.67520  ? 140 THR A CG2 1 
ATOM   682  N N   . GLY A 1 124 ? 17.14668 -5.02818  33.34034  1.000 48.23406  ? 141 GLY A N   1 
ATOM   683  C CA  . GLY A 1 124 ? 16.97834 -3.69871  33.87467  1.000 49.66570  ? 141 GLY A CA  1 
ATOM   684  C C   . GLY A 1 124 ? 15.67567 -3.60516  34.63273  1.000 51.95180  ? 141 GLY A C   1 
ATOM   685  O O   . GLY A 1 124 ? 15.09569 -4.61569  35.00175  1.000 51.76751  ? 141 GLY A O   1 
ATOM   686  N N   . SER A 1 125 ? 15.25608 -2.36471  34.86192  1.000 53.12287  ? 142 SER A N   1 
ATOM   687  C CA  . SER A 1 125 ? 14.02471 -2.06672  35.57052  1.000 51.33525  ? 142 SER A CA  1 
ATOM   688  C C   . SER A 1 125 ? 12.81480 -2.66990  34.86763  1.000 56.98063  ? 142 SER A C   1 
ATOM   689  O O   . SER A 1 125 ? 12.84538 -2.96598  33.66760  1.000 57.56377  ? 142 SER A O   1 
ATOM   690  C CB  . SER A 1 125 ? 13.86522 -0.56361  35.66091  1.000 58.73288  ? 142 SER A CB  1 
ATOM   691  O OG  . SER A 1 125 ? 13.41734 -0.06855  34.41547  1.000 57.67456  ? 142 SER A OG  1 
ATOM   692  N N   . LEU A 1 126 ? 11.72397 -2.84272  35.63060  1.000 59.17016  ? 143 LEU A N   1 
ATOM   693  C CA  . LEU A 1 126 ? 10.48948 -3.36424  35.04241  1.000 53.20949  ? 143 LEU A CA  1 
ATOM   694  C C   . LEU A 1 126 ? 9.96965  -2.40825  33.97708  1.000 56.80318  ? 143 LEU A C   1 
ATOM   695  O O   . LEU A 1 126 ? 9.60920  -2.81902  32.86785  1.000 54.31758  ? 143 LEU A O   1 
ATOM   696  C CB  . LEU A 1 126 ? 9.44314  -3.59940  36.13697  1.000 46.06134  ? 143 LEU A CB  1 
ATOM   697  C CG  . LEU A 1 126 ? 8.18009  -4.42495  35.84432  1.000 45.17666  ? 143 LEU A CG  1 
ATOM   698  C CD1 . LEU A 1 126 ? 8.51721  -5.85764  35.48279  1.000 46.81609  ? 143 LEU A CD1 1 
ATOM   699  C CD2 . LEU A 1 126 ? 7.24291  -4.44646  37.02506  1.000 48.20793  ? 143 LEU A CD2 1 
ATOM   700  N N   . GLU A 1 127 ? 9.98620  -1.11229  34.29038  1.000 63.64985  ? 144 GLU A N   1 
ATOM   701  C CA  . GLU A 1 127 ? 9.52188  -0.07539  33.37418  1.000 65.65697  ? 144 GLU A CA  1 
ATOM   702  C C   . GLU A 1 127 ? 10.24154 -0.13873  32.03010  1.000 65.00915  ? 144 GLU A C   1 
ATOM   703  O O   . GLU A 1 127 ? 9.62597  0.07504   30.97993  1.000 68.15981  ? 144 GLU A O   1 
ATOM   704  C CB  . GLU A 1 127 ? 9.71146  1.27479   34.06684  1.000 66.60094  ? 144 GLU A CB  1 
ATOM   705  C CG  . GLU A 1 127 ? 8.83730  2.40801   33.59707  1.000 74.81739  ? 144 GLU A CG  1 
ATOM   706  C CD  . GLU A 1 127 ? 9.63777  3.53267   32.95720  1.000 86.58834  ? 144 GLU A CD  1 
ATOM   707  O OE1 . GLU A 1 127 ? 10.86992 3.62612   33.23503  1.000 83.27880  ? 144 GLU A OE1 1 
ATOM   708  O OE2 . GLU A 1 127 ? 9.03175  4.31905   32.17533  1.000 86.28443  ? 144 GLU A OE2 1 
ATOM   709  N N   . GLN A 1 128 ? 11.53268 -0.48052  32.04217  1.000 58.87960  ? 145 GLN A N   1 
ATOM   710  C CA  . GLN A 1 128 ? 12.41581 -0.45479  30.87468  1.000 55.32330  ? 145 GLN A CA  1 
ATOM   711  C C   . GLN A 1 128 ? 12.39797 -1.74405  30.06776  1.000 50.16159  ? 145 GLN A C   1 
ATOM   712  O O   . GLN A 1 128 ? 12.28591 -1.69974  28.84110  1.000 47.58144  ? 145 GLN A O   1 
ATOM   713  C CB  . GLN A 1 128 ? 13.84889 -0.16941  31.30487  1.000 51.58954  ? 145 GLN A CB  1 
ATOM   714  C CG  . GLN A 1 128 ? 14.03840 1.26368   31.66275  1.000 58.62687  ? 145 GLN A CG  1 
ATOM   715  C CD  . GLN A 1 128 ? 13.87163 2.16908   30.47648  1.000 53.04312  ? 145 GLN A CD  1 
ATOM   716  O OE1 . GLN A 1 128 ? 14.58337 2.03245   29.47765  1.000 50.16892  ? 145 GLN A OE1 1 
ATOM   717  N NE2 . GLN A 1 128 ? 12.92572 3.09753   30.57040  1.000 51.85608  ? 145 GLN A NE2 1 
ATOM   718  N N   . VAL A 1 129 ? 12.55192 -2.89363  30.73013  1.000 50.82201  ? 146 VAL A N   1 
ATOM   719  C CA  . VAL A 1 129 ? 12.48534 -4.16190  30.01083  1.000 47.23010  ? 146 VAL A CA  1 
ATOM   720  C C   . VAL A 1 129 ? 11.12888 -4.31939  29.33707  1.000 48.90227  ? 146 VAL A C   1 
ATOM   721  O O   . VAL A 1 129 ? 11.02947 -4.87285  28.23446  1.000 48.38265  ? 146 VAL A O   1 
ATOM   722  C CB  . VAL A 1 129 ? 12.80548 -5.33136  30.95589  1.000 43.17700  ? 146 VAL A CB  1 
ATOM   723  C CG1 . VAL A 1 129 ? 14.17581 -5.11713  31.56515  1.000 45.49725  ? 146 VAL A CG1 1 
ATOM   724  C CG2 . VAL A 1 129 ? 11.75892 -5.44680  32.03494  1.000 45.64446  ? 146 VAL A CG2 1 
ATOM   725  N N   . ASN A 1 130 ? 10.06967 -3.80103  29.95498  1.000 52.50365  ? 147 ASN A N   1 
ATOM   726  C CA  . ASN A 1 130 ? 8.77326  -3.81058  29.29422  1.000 48.71892  ? 147 ASN A CA  1 
ATOM   727  C C   . ASN A 1 130 ? 8.79836  -2.92632  28.06058  1.000 48.23503  ? 147 ASN A C   1 
ATOM   728  O O   . ASN A 1 130 ? 8.40463  -3.36044  26.97346  1.000 47.06262  ? 147 ASN A O   1 
ATOM   729  C CB  . ASN A 1 130 ? 7.69302  -3.35684  30.26382  1.000 49.11470  ? 147 ASN A CB  1 
ATOM   730  C CG  . ASN A 1 130 ? 7.00553  -4.51447  30.94345  1.000 48.92126  ? 147 ASN A CG  1 
ATOM   731  O OD1 . ASN A 1 130 ? 6.12174  -5.16050  30.36465  1.000 51.30541  ? 147 ASN A OD1 1 
ATOM   732  N ND2 . ASN A 1 130 ? 7.39130  -4.77725  32.18997  1.000 47.43783  ? 147 ASN A ND2 1 
ATOM   733  N N   . GLY A 1 131 ? 9.28050  -1.68148  28.21512  1.000 51.88124  ? 148 GLY A N   1 
ATOM   734  C CA  . GLY A 1 131 ? 9.34783  -0.76445  27.08832  1.000 47.48113  ? 148 GLY A CA  1 
ATOM   735  C C   . GLY A 1 131 ? 10.10530 -1.34357  25.91473  1.000 45.91842  ? 148 GLY A C   1 
ATOM   736  O O   . GLY A 1 131 ? 9.68237  -1.21614  24.76427  1.000 46.03376  ? 148 GLY A O   1 
ATOM   737  N N   . TYR A 1 132 ? 11.22056 -2.02013  26.19333  1.000 48.73703  ? 149 TYR A N   1 
ATOM   738  C CA  . TYR A 1 132 ? 12.04889 -2.59004  25.13983  1.000 46.40267  ? 149 TYR A CA  1 
ATOM   739  C C   . TYR A 1 132 ? 11.55306 -3.94805  24.66936  1.000 48.25822  ? 149 TYR A C   1 
ATOM   740  O O   . TYR A 1 132 ? 11.88922 -4.35435  23.54756  1.000 47.53717  ? 149 TYR A O   1 
ATOM   741  C CB  . TYR A 1 132 ? 13.50285 -2.69911  25.60895  1.000 43.46997  ? 149 TYR A CB  1 
ATOM   742  C CG  . TYR A 1 132 ? 14.28939 -1.44175  25.30723  1.000 43.37748  ? 149 TYR A CG  1 
ATOM   743  C CD1 . TYR A 1 132 ? 14.52988 -1.04324  24.00337  1.000 39.33939  ? 149 TYR A CD1 1 
ATOM   744  C CD2 . TYR A 1 132 ? 14.76439 -0.63649  26.33333  1.000 43.75548  ? 149 TYR A CD2 1 
ATOM   745  C CE1 . TYR A 1 132 ? 15.23402 0.10625   23.74285  1.000 41.31412  ? 149 TYR A CE1 1 
ATOM   746  C CE2 . TYR A 1 132 ? 15.46700 0.51410   26.07680  1.000 41.92897  ? 149 TYR A CE2 1 
ATOM   747  C CZ  . TYR A 1 132 ? 15.69690 0.88130   24.78926  1.000 42.60494  ? 149 TYR A CZ  1 
ATOM   748  O OH  . TYR A 1 132 ? 16.38843 2.04161   24.54694  1.000 45.15197  ? 149 TYR A OH  1 
ATOM   749  N N   . TYR A 1 133 ? 10.77208 -4.66848  25.48516  1.000 47.04651  ? 150 TYR A N   1 
ATOM   750  C CA  . TYR A 1 133 ? 10.18550 -5.88824  24.95646  1.000 44.16439  ? 150 TYR A CA  1 
ATOM   751  C C   . TYR A 1 133 ? 9.23600  -5.55595  23.82688  1.000 46.01786  ? 150 TYR A C   1 
ATOM   752  O O   . TYR A 1 133 ? 9.24396  -6.21770  22.78733  1.000 50.17575  ? 150 TYR A O   1 
ATOM   753  C CB  . TYR A 1 133 ? 9.45397  -6.69754  26.01662  1.000 42.15705  ? 150 TYR A CB  1 
ATOM   754  C CG  . TYR A 1 133 ? 8.61942  -7.80383  25.37516  1.000 45.32894  ? 150 TYR A CG  1 
ATOM   755  C CD1 . TYR A 1 133 ? 9.19986  -8.99838  24.97757  1.000 43.55800  ? 150 TYR A CD1 1 
ATOM   756  C CD2 . TYR A 1 133 ? 7.25752  -7.63424  25.12470  1.000 48.02952  ? 150 TYR A CD2 1 
ATOM   757  C CE1 . TYR A 1 133 ? 8.44131  -10.00484 24.37662  1.000 46.39591  ? 150 TYR A CE1 1 
ATOM   758  C CE2 . TYR A 1 133 ? 6.49345  -8.64142  24.51691  1.000 48.08929  ? 150 TYR A CE2 1 
ATOM   759  C CZ  . TYR A 1 133 ? 7.08554  -9.82822  24.14736  1.000 45.90918  ? 150 TYR A CZ  1 
ATOM   760  O OH  . TYR A 1 133 ? 6.32009  -10.83037 23.55543  1.000 47.14057  ? 150 TYR A OH  1 
ATOM   761  N N   . ASN A 1 134 ? 8.42104  -4.52436  23.99756  1.000 48.06643  ? 151 ASN A N   1 
ATOM   762  C CA  . ASN A 1 134 ? 7.51546  -4.16153  22.91834  1.000 49.75630  ? 151 ASN A CA  1 
ATOM   763  C C   . ASN A 1 134 ? 8.28271  -3.64140  21.70422  1.000 50.74790  ? 151 ASN A C   1 
ATOM   764  O O   . ASN A 1 134 ? 7.91105  -3.94151  20.55838  1.000 48.45962  ? 151 ASN A O   1 
ATOM   765  C CB  . ASN A 1 134 ? 6.49867  -3.14918  23.42654  1.000 50.54942  ? 151 ASN A CB  1 
ATOM   766  C CG  . ASN A 1 134 ? 5.57858  -3.74606  24.46444  1.000 53.17500  ? 151 ASN A CG  1 
ATOM   767  O OD1 . ASN A 1 134 ? 5.60903  -3.35366  25.63702  1.000 56.41798  ? 151 ASN A OD1 1 
ATOM   768  N ND2 . ASN A 1 134 ? 4.75406  -4.71849  24.04603  1.000 56.26541  ? 151 ASN A ND2 1 
ATOM   769  N N   . ILE A 1 135 ? 9.37574  -2.89407  21.93442  1.000 49.42785  ? 152 ILE A N   1 
ATOM   770  C CA  . ILE A 1 135 ? 10.17234 -2.37869  20.82130  1.000 46.89851  ? 152 ILE A CA  1 
ATOM   771  C C   . ILE A 1 135 ? 10.78479 -3.52394  20.03741  1.000 47.31995  ? 152 ILE A C   1 
ATOM   772  O O   . ILE A 1 135 ? 10.75762 -3.54007  18.80182  1.000 50.64337  ? 152 ILE A O   1 
ATOM   773  C CB  . ILE A 1 135 ? 11.26127 -1.41169  21.31402  1.000 43.03136  ? 152 ILE A CB  1 
ATOM   774  C CG1 . ILE A 1 135 ? 10.66131 -0.07896  21.73078  1.000 44.69693  ? 152 ILE A CG1 1 
ATOM   775  C CG2 . ILE A 1 135 ? 12.23438 -1.14736  20.20802  1.000 43.17093  ? 152 ILE A CG2 1 
ATOM   776  C CD1 . ILE A 1 135 ? 11.66784 0.88241   22.30056  1.000 44.88094  ? 152 ILE A CD1 1 
ATOM   777  N N   . LEU A 1 136 ? 11.32756 -4.50701  20.74780  1.000 45.76248  ? 153 LEU A N   1 
ATOM   778  C CA  . LEU A 1 136 ? 12.11362 -5.55003  20.10703  1.000 46.61064  ? 153 LEU A CA  1 
ATOM   779  C C   . LEU A 1 136 ? 11.24984 -6.69473  19.57774  1.000 49.82624  ? 153 LEU A C   1 
ATOM   780  O O   . LEU A 1 136 ? 11.58203 -7.25721  18.53098  1.000 50.68565  ? 153 LEU A O   1 
ATOM   781  C CB  . LEU A 1 136 ? 13.18367 -6.05222  21.07915  1.000 46.09845  ? 153 LEU A CB  1 
ATOM   782  C CG  . LEU A 1 136 ? 14.52860 -5.32532  21.03512  1.000 44.41102  ? 153 LEU A CG  1 
ATOM   783  C CD1 . LEU A 1 136 ? 14.32742 -3.93008  21.41333  1.000 53.26398  ? 153 LEU A CD1 1 
ATOM   784  C CD2 . LEU A 1 136 ? 15.43605 -5.90165  22.06965  1.000 41.98942  ? 153 LEU A CD2 1 
ATOM   785  N N   . LYS A 1 137 ? 10.15584 -7.07274  20.27265  1.000 49.63339  ? 154 LYS A N   1 
ATOM   786  C CA  . LYS A 1 137 ? 9.20573  -8.02397  19.68457  1.000 45.86868  ? 154 LYS A CA  1 
ATOM   787  C C   . LYS A 1 137 ? 8.80702  -7.56206  18.29498  1.000 49.28746  ? 154 LYS A C   1 
ATOM   788  O O   . LYS A 1 137 ? 8.79762  -8.35507  17.33977  1.000 53.13577  ? 154 LYS A O   1 
ATOM   789  C CB  . LYS A 1 137 ? 7.94658  -8.18379  20.54759  1.000 43.58387  ? 154 LYS A CB  1 
ATOM   790  C CG  . LYS A 1 137 ? 7.02267  -9.40185  20.21505  1.000 44.08346  ? 154 LYS A CG  1 
ATOM   791  C CD  . LYS A 1 137 ? 7.64287  -10.75119 20.61953  1.000 51.53080  ? 154 LYS A CD  1 
ATOM   792  C CE  . LYS A 1 137 ? 6.89668  -11.99656 20.09557  1.000 52.15848  ? 154 LYS A CE  1 
ATOM   793  N NZ  . LYS A 1 137 ? 7.83332  -13.06985 19.53096  1.000 60.16100  ? 154 LYS A NZ  1 
ATOM   794  N N   . ALA A 1 138 ? 8.49665  -6.26818  18.16624  1.000 45.90686  ? 155 ALA A N   1 
ATOM   795  C CA  . ALA A 1 138 ? 8.17658  -5.68902  16.87091  1.000 49.17717  ? 155 ALA A CA  1 
ATOM   796  C C   . ALA A 1 138 ? 9.33757  -5.84474  15.90081  1.000 54.11683  ? 155 ALA A C   1 
ATOM   797  O O   . ALA A 1 138 ? 9.17604  -6.35611  14.78387  1.000 58.48679  ? 155 ALA A O   1 
ATOM   798  C CB  . ALA A 1 138 ? 7.83668  -4.21821  17.05168  1.000 49.82091  ? 155 ALA A CB  1 
ATOM   799  N N   . LEU A 1 139 ? 10.52764 -5.42427  16.32923  1.000 53.33158  ? 156 LEU A N   1 
ATOM   800  C CA  . LEU A 1 139 ? 11.67923 -5.36364  15.43964  1.000 49.64187  ? 156 LEU A CA  1 
ATOM   801  C C   . LEU A 1 139 ? 12.07200 -6.74803  14.92992  1.000 49.59868  ? 156 LEU A C   1 
ATOM   802  O O   . LEU A 1 139 ? 12.41037 -6.89848  13.75361  1.000 52.44970  ? 156 LEU A O   1 
ATOM   803  C CB  . LEU A 1 139 ? 12.84378 -4.70544  16.18045  1.000 49.85928  ? 156 LEU A CB  1 
ATOM   804  C CG  . LEU A 1 139 ? 14.19284 -4.58066  15.47749  1.000 50.57630  ? 156 LEU A CG  1 
ATOM   805  C CD1 . LEU A 1 139 ? 14.05330 -3.66516  14.32456  1.000 54.89332  ? 156 LEU A CD1 1 
ATOM   806  C CD2 . LEU A 1 139 ? 15.32849 -4.16068  16.41448  1.000 52.09695  ? 156 LEU A CD2 1 
ATOM   807  N N   . ASN A 1 140 ? 12.01027 -7.77049  15.79482  1.000 50.64509  ? 157 ASN A N   1 
ATOM   808  C CA  . ASN A 1 140 ? 12.58848 -9.08619  15.51412  1.000 50.32017  ? 157 ASN A CA  1 
ATOM   809  C C   . ASN A 1 140 ? 11.84321 -9.84300  14.42397  1.000 57.21702  ? 157 ASN A C   1 
ATOM   810  O O   . ASN A 1 140 ? 10.63129 -10.07334 14.51534  1.000 59.52517  ? 157 ASN A O   1 
ATOM   811  C CB  . ASN A 1 140 ? 12.60965 -9.95190  16.76629  1.000 49.13035  ? 157 ASN A CB  1 
ATOM   812  C CG  . ASN A 1 140 ? 13.56299 -11.12068 16.63730  1.000 51.52299  ? 157 ASN A CG  1 
ATOM   813  O OD1 . ASN A 1 140 ? 13.15339 -12.26235 16.44413  1.000 50.95685  ? 157 ASN A OD1 1 
ATOM   814  N ND2 . ASN A 1 140 ? 14.84043 -10.84127 16.74746  1.000 55.51863  ? 157 ASN A ND2 1 
ATOM   815  N N   . LYS A 1 141 ? 12.61201 -10.30568 13.44024  1.000 58.38528  ? 158 LYS A N   1 
ATOM   816  C CA  . LYS A 1 141 ? 12.14063 -10.91845 12.20834  1.000 59.52611  ? 158 LYS A CA  1 
ATOM   817  C C   . LYS A 1 141 ? 12.42633 -12.42574 12.20159  1.000 62.24880  ? 158 LYS A C   1 
ATOM   818  O O   . LYS A 1 141 ? 12.25030 -13.08177 11.16412  1.000 65.73617  ? 158 LYS A O   1 
ATOM   819  C CB  . LYS A 1 141 ? 12.82072 -10.19765 11.02541  1.000 62.37326  ? 158 LYS A CB  1 
ATOM   820  C CG  . LYS A 1 141 ? 12.15445 -10.26919 9.66250   1.000 76.38102  ? 158 LYS A CG  1 
ATOM   821  C CD  . LYS A 1 141 ? 13.14164 -10.08597 8.44906   1.000 85.45920  ? 158 LYS A CD  1 
ATOM   822  C CE  . LYS A 1 141 ? 12.66807 -10.87580 7.16875   1.000 87.93179  ? 158 LYS A CE  1 
ATOM   823  N NZ  . LYS A 1 141 ? 13.68259 -11.03128 6.07101   1.000 82.86705  ? 158 LYS A NZ  1 
ATOM   824  N N   . ARG A 1 142 ? 12.88805 -12.99100 13.34113  1.000 57.32830  ? 159 ARG A N   1 
ATOM   825  C CA  . ARG A 1 142 ? 13.25687 -14.40186 13.43307  1.000 58.64032  ? 159 ARG A CA  1 
ATOM   826  C C   . ARG A 1 142 ? 12.60685 -15.08975 14.63006  1.000 59.63129  ? 159 ARG A C   1 
ATOM   827  O O   . ARG A 1 142 ? 13.16019 -16.07351 15.13710  1.000 60.07789  ? 159 ARG A O   1 
ATOM   828  C CB  . ARG A 1 142 ? 14.77745 -14.61009 13.50941  1.000 57.61063  ? 159 ARG A CB  1 
ATOM   829  C CG  . ARG A 1 142 ? 15.60160 -14.03628 12.36910  1.000 60.23291  ? 159 ARG A CG  1 
ATOM   830  C CD  . ARG A 1 142 ? 15.23727 -14.66755 11.04692  1.000 66.28878  ? 159 ARG A CD  1 
ATOM   831  N NE  . ARG A 1 142 ? 16.19410 -14.46471 9.95566   1.000 75.59654  ? 159 ARG A NE  1 
ATOM   832  C CZ  . ARG A 1 142 ? 15.88128 -13.97885 8.75083   1.000 82.71281  ? 159 ARG A CZ  1 
ATOM   833  N NH1 . ARG A 1 142 ? 14.67813 -13.47975 8.48930   1.000 79.65326  ? 159 ARG A NH1 1 
ATOM   834  N NH2 . ARG A 1 142 ? 16.79467 -14.00072 7.77657   1.000 78.13073  ? 159 ARG A NH2 1 
ATOM   835  N N   . ASN A 1 143 ? 11.45427 -14.60201 15.09822  1.000 58.01371  ? 160 ASN A N   1 
ATOM   836  C CA  . ASN A 1 143 ? 10.71956 -15.22869 16.20854  1.000 60.04805  ? 160 ASN A CA  1 
ATOM   837  C C   . ASN A 1 143 ? 11.59255 -15.54495 17.41090  1.000 57.04406  ? 160 ASN A C   1 
ATOM   838  O O   . ASN A 1 143 ? 11.63163 -16.67654 17.89105  1.000 56.85916  ? 160 ASN A O   1 
ATOM   839  C CB  . ASN A 1 143 ? 10.00416 -16.49349 15.75787  1.000 63.77177  ? 160 ASN A CB  1 
ATOM   840  C CG  . ASN A 1 143 ? 8.53965  -16.26370 15.55285  1.000 79.00073  ? 160 ASN A CG  1 
ATOM   841  O OD1 . ASN A 1 143 ? 7.76911  -16.28461 16.53465  1.000 80.16854  ? 160 ASN A OD1 1 
ATOM   842  N ND2 . ASN A 1 143 ? 8.12605  -16.02545 14.29569  1.000 78.34230  ? 160 ASN A ND2 1 
ATOM   843  N N   . ALA A 1 144 ? 12.28174 -14.53262 17.91264  1.000 54.51960  ? 161 ALA A N   1 
ATOM   844  C CA  . ALA A 1 144 ? 13.19236 -14.76924 19.01314  1.000 48.14768  ? 161 ALA A CA  1 
ATOM   845  C C   . ALA A 1 144 ? 12.39470 -15.09222 20.26144  1.000 49.87411  ? 161 ALA A C   1 
ATOM   846  O O   . ALA A 1 144 ? 11.21119 -14.75199 20.36526  1.000 54.00142  ? 161 ALA A O   1 
ATOM   847  C CB  . ALA A 1 144 ? 14.08430 -13.55542 19.24361  1.000 48.29386  ? 161 ALA A CB  1 
ATOM   848  N N   . LYS A 1 145 ? 13.03580 -15.82138 21.17623  1.000 46.87196  ? 162 LYS A N   1 
ATOM   849  C CA  . LYS A 1 145 ? 12.51886 -16.00769 22.52225  1.000 45.48484  ? 162 LYS A CA  1 
ATOM   850  C C   . LYS A 1 145 ? 12.98517 -14.84267 23.36514  1.000 47.53257  ? 162 LYS A C   1 
ATOM   851  O O   . LYS A 1 145 ? 14.15859 -14.45544 23.30217  1.000 46.06469  ? 162 LYS A O   1 
ATOM   852  C CB  . LYS A 1 145 ? 13.03218 -17.30599 23.15060  1.000 51.07777  ? 162 LYS A CB  1 
ATOM   853  C CG  . LYS A 1 145 ? 12.69309 -18.59182 22.44304  1.000 55.64923  ? 162 LYS A CG  1 
ATOM   854  C CD  . LYS A 1 145 ? 12.86100 -19.78813 23.37300  1.000 63.20717  ? 162 LYS A CD  1 
ATOM   855  C CE  . LYS A 1 145 ? 11.92775 -20.94630 22.97730  1.000 74.99669  ? 162 LYS A CE  1 
ATOM   856  N NZ  . LYS A 1 145 ? 12.48270 -21.90767 21.92864  1.000 80.30458  ? 162 LYS A NZ  1 
ATOM   857  N N   . PHE A 1 146 ? 12.07843 -14.28308 24.16171  1.000 46.55624  ? 163 PHE A N   1 
ATOM   858  C CA  . PHE A 1 146 ? 12.42898 -13.16139 25.02631  1.000 45.72446  ? 163 PHE A CA  1 
ATOM   859  C C   . PHE A 1 146 ? 12.51668 -13.60711 26.47920  1.000 44.65297  ? 163 PHE A C   1 
ATOM   860  O O   . PHE A 1 146 ? 11.61756 -14.28794 26.98937  1.000 44.92944  ? 163 PHE A O   1 
ATOM   861  C CB  . PHE A 1 146 ? 11.43377 -12.01627 24.87396  1.000 39.69932  ? 163 PHE A CB  1 
ATOM   862  C CG  . PHE A 1 146 ? 11.62593 -11.23160 23.61805  1.000 44.56480  ? 163 PHE A CG  1 
ATOM   863  C CD1 . PHE A 1 146 ? 11.11560 -11.69954 22.40449  1.000 46.23602  ? 163 PHE A CD1 1 
ATOM   864  C CD2 . PHE A 1 146 ? 12.31645 -10.03419 23.63218  1.000 44.42319  ? 163 PHE A CD2 1 
ATOM   865  C CE1 . PHE A 1 146 ? 11.27786 -10.97891 21.23106  1.000 44.75346  ? 163 PHE A CE1 1 
ATOM   866  C CE2 . PHE A 1 146 ? 12.48528 -9.30079  22.45925  1.000 46.40635  ? 163 PHE A CE2 1 
ATOM   867  C CZ  . PHE A 1 146 ? 11.96196 -9.77205  21.25429  1.000 45.76647  ? 163 PHE A CZ  1 
ATOM   868  N N   . VAL A 1 147 ? 13.60383 -13.22401 27.13788  1.000 42.02879  ? 164 VAL A N   1 
ATOM   869  C CA  . VAL A 1 147 ? 13.74707 -13.38722 28.57861  1.000 44.79180  ? 164 VAL A CA  1 
ATOM   870  C C   . VAL A 1 147 ? 13.96784 -12.00679 29.19057  1.000 44.91299  ? 164 VAL A C   1 
ATOM   871  O O   . VAL A 1 147 ? 14.90521 -11.29161 28.80468  1.000 46.70291  ? 164 VAL A O   1 
ATOM   872  C CB  . VAL A 1 147 ? 14.89613 -14.34177 28.92960  1.000 41.86852  ? 164 VAL A CB  1 
ATOM   873  C CG1 . VAL A 1 147 ? 15.19948 -14.25231 30.38685  1.000 41.61744  ? 164 VAL A CG1 1 
ATOM   874  C CG2 . VAL A 1 147 ? 14.51520 -15.74049 28.57015  1.000 48.14078  ? 164 VAL A CG2 1 
ATOM   875  N N   . LEU A 1 148 ? 13.11085 -11.63002 30.13867  1.000 40.22806  ? 165 LEU A N   1 
ATOM   876  C CA  . LEU A 1 148 ? 13.21307 -10.33920 30.81718  1.000 42.60815  ? 165 LEU A CA  1 
ATOM   877  C C   . LEU A 1 148 ? 13.80276 -10.55287 32.21104  1.000 43.42131  ? 165 LEU A C   1 
ATOM   878  O O   . LEU A 1 148 ? 13.17758 -11.18502 33.07006  1.000 45.38810  ? 165 LEU A O   1 
ATOM   879  C CB  . LEU A 1 148 ? 11.84641 -9.66365  30.89896  1.000 42.07737  ? 165 LEU A CB  1 
ATOM   880  C CG  . LEU A 1 148 ? 11.09917 -9.57628  29.58005  1.000 39.59355  ? 165 LEU A CG  1 
ATOM   881  C CD1 . LEU A 1 148 ? 9.80507  -8.84189  29.79193  1.000 40.07650  ? 165 LEU A CD1 1 
ATOM   882  C CD2 . LEU A 1 148 ? 11.94746 -8.88592  28.52610  1.000 39.84110  ? 165 LEU A CD2 1 
ATOM   883  N N   . LYS A 1 149 ? 15.00522 -10.03808 32.43817  1.000 45.14156  ? 166 LYS A N   1 
ATOM   884  C CA  . LYS A 1 149 ? 15.68515 -10.19068 33.71920  1.000 43.15490  ? 166 LYS A CA  1 
ATOM   885  C C   . LYS A 1 149 ? 15.57496 -8.86439  34.45847  1.000 46.74429  ? 166 LYS A C   1 
ATOM   886  O O   . LYS A 1 149 ? 16.12667 -7.85331  34.01184  1.000 47.92042  ? 166 LYS A O   1 
ATOM   887  C CB  . LYS A 1 149 ? 17.13431 -10.62383 33.51754  1.000 41.90460  ? 166 LYS A CB  1 
ATOM   888  C CG  . LYS A 1 149 ? 17.25586 -12.05271 32.95739  1.000 44.78509  ? 166 LYS A CG  1 
ATOM   889  C CD  . LYS A 1 149 ? 18.69327 -12.50328 32.69359  1.000 49.60790  ? 166 LYS A CD  1 
ATOM   890  C CE  . LYS A 1 149 ? 18.99915 -13.80227 33.39863  1.000 60.14247  ? 166 LYS A CE  1 
ATOM   891  N NZ  . LYS A 1 149 ? 19.69680 -14.78748 32.52232  1.000 67.13530  ? 166 LYS A NZ  1 
ATOM   892  N N   . ILE A 1 150 ? 14.83722 -8.86814  35.57304  1.000 47.55848  ? 167 ILE A N   1 
ATOM   893  C CA  . ILE A 1 150 ? 14.52646 -7.64612  36.31048  1.000 45.32607  ? 167 ILE A CA  1 
ATOM   894  C C   . ILE A 1 150 ? 15.68448 -7.31009  37.23285  1.000 47.57495  ? 167 ILE A C   1 
ATOM   895  O O   . ILE A 1 150 ? 16.12162 -8.15236  38.02468  1.000 48.22742  ? 167 ILE A O   1 
ATOM   896  C CB  . ILE A 1 150 ? 13.22315 -7.80766  37.10325  1.000 41.19106  ? 167 ILE A CB  1 
ATOM   897  C CG1 . ILE A 1 150 ? 12.15625 -8.36317  36.17907  1.000 44.33823  ? 167 ILE A CG1 1 
ATOM   898  C CG2 . ILE A 1 150 ? 12.77412 -6.49359  37.69066  1.000 41.90752  ? 167 ILE A CG2 1 
ATOM   899  C CD1 . ILE A 1 150 ? 11.71602 -7.38372  35.13628  1.000 45.19066  ? 167 ILE A CD1 1 
ATOM   900  N N   . ASN A 1 151 ? 16.19436 -6.08221  37.11634  1.000 47.63528  ? 168 ASN A N   1 
ATOM   901  C CA  . ASN A 1 151 ? 17.21444 -5.54575  38.01685  1.000 50.79631  ? 168 ASN A CA  1 
ATOM   902  C C   . ASN A 1 151 ? 16.83642 -4.09544  38.27927  1.000 60.52133  ? 168 ASN A C   1 
ATOM   903  O O   . ASN A 1 151 ? 17.09469 -3.22923  37.43957  1.000 62.95938  ? 168 ASN A O   1 
ATOM   904  C CB  . ASN A 1 151 ? 18.60582 -5.62112  37.41509  1.000 55.19307  ? 168 ASN A CB  1 
ATOM   905  C CG  . ASN A 1 151 ? 19.71310 -5.36617  38.44297  1.000 62.95402  ? 168 ASN A CG  1 
ATOM   906  O OD1 . ASN A 1 151 ? 19.64825 -4.43899  39.27513  1.000 61.96875  ? 168 ASN A OD1 1 
ATOM   907  N ND2 . ASN A 1 151 ? 20.77475 -6.15577  38.33685  1.000 65.64815  ? 168 ASN A ND2 1 
ATOM   908  N N   . GLU A 1 152 ? 16.24758 -3.81544  39.43672  1.000 68.42463  ? 169 GLU A N   1 
ATOM   909  C CA  . GLU A 1 152 ? 15.78037 -2.45082  39.61275  1.000 69.95932  ? 169 GLU A CA  1 
ATOM   910  C C   . GLU A 1 152 ? 16.89033 -1.46954  39.96962  1.000 70.69384  ? 169 GLU A C   1 
ATOM   911  O O   . GLU A 1 152 ? 16.59320 -0.28352  40.09989  1.000 72.54945  ? 169 GLU A O   1 
ATOM   912  C CB  . GLU A 1 152 ? 14.65480 -2.39500  40.65139  1.000 70.33378  ? 169 GLU A CB  1 
ATOM   913  C CG  . GLU A 1 152 ? 13.30705 -2.97405  40.15732  1.000 73.35378  ? 169 GLU A CG  1 
ATOM   914  C CD  . GLU A 1 152 ? 12.61021 -2.10419  39.06833  1.000 76.25082  ? 169 GLU A CD  1 
ATOM   915  O OE1 . GLU A 1 152 ? 13.13566 -1.01152  38.72857  1.000 76.44388  ? 169 GLU A OE1 1 
ATOM   916  O OE2 . GLU A 1 152 ? 11.52876 -2.51059  38.55867  1.000 73.76058  ? 169 GLU A OE2 1 
ATOM   917  N N   . ASN A 1 153 ? 18.14839 -1.90823  40.10709  1.000 63.90165  ? 170 ASN A N   1 
ATOM   918  C CA  . ASN A 1 153 ? 19.26638 -0.99514  40.34477  1.000 66.35903  ? 170 ASN A CA  1 
ATOM   919  C C   . ASN A 1 153 ? 19.93247 -0.50283  39.06898  1.000 70.95229  ? 170 ASN A C   1 
ATOM   920  O O   . ASN A 1 153 ? 20.87161 0.29820   39.15113  1.000 67.96241  ? 170 ASN A O   1 
ATOM   921  C CB  . ASN A 1 153 ? 20.37023 -1.64167  41.17486  1.000 73.20316  ? 170 ASN A CB  1 
ATOM   922  C CG  . ASN A 1 153 ? 19.85208 -2.50195  42.27621  1.000 80.13243  ? 170 ASN A CG  1 
ATOM   923  O OD1 . ASN A 1 153 ? 19.37110 -2.00530  43.31265  1.000 83.15246  ? 170 ASN A OD1 1 
ATOM   924  N ND2 . ASN A 1 153 ? 19.98099 -3.82039  42.09010  1.000 80.69700  ? 170 ASN A ND2 1 
ATOM   925  N N   . MET A 1 154 ? 19.51315 -0.99344  37.90442  1.000 68.76021  ? 171 MET A N   1 
ATOM   926  C CA  . MET A 1 154 ? 20.16372 -0.64213  36.65406  1.000 64.03993  ? 171 MET A CA  1 
ATOM   927  C C   . MET A 1 154 ? 19.48584 0.59145   36.07669  1.000 69.49900  ? 171 MET A C   1 
ATOM   928  O O   . MET A 1 154 ? 18.33469 0.49140   35.60325  1.000 66.70747  ? 171 MET A O   1 
ATOM   929  C CB  . MET A 1 154 ? 20.07533 -1.78958  35.68060  1.000 58.31489  ? 171 MET A CB  1 
ATOM   930  C CG  . MET A 1 154 ? 21.03039 -2.87286  35.97867  1.000 54.01462  ? 171 MET A CG  1 
ATOM   931  S SD  . MET A 1 154 ? 20.91058 -4.15132  34.74037  1.000 53.67272  ? 171 MET A SD  1 
ATOM   932  C CE  . MET A 1 154 ? 20.68553 -3.20838  33.23689  1.000 52.95647  ? 171 MET A CE  1 
ATOM   933  N N   . PRO A 1 155 ? 20.14911 1.75276   36.06381  1.000 67.62985  ? 172 PRO A N   1 
ATOM   934  C CA  . PRO A 1 155 ? 19.48355 2.96876   35.57795  1.000 68.29631  ? 172 PRO A CA  1 
ATOM   935  C C   . PRO A 1 155 ? 19.14707 2.92945   34.08575  1.000 73.41130  ? 172 PRO A C   1 
ATOM   936  O O   . PRO A 1 155 ? 18.22645 3.65451   33.66687  1.000 72.37047  ? 172 PRO A O   1 
ATOM   937  C CB  . PRO A 1 155 ? 20.49240 4.07607   35.91304  1.000 71.11452  ? 172 PRO A CB  1 
ATOM   938  C CG  . PRO A 1 155 ? 21.81212 3.36148   35.95832  1.000 70.06028  ? 172 PRO A CG  1 
ATOM   939  C CD  . PRO A 1 155 ? 21.52821 2.01027   36.50995  1.000 66.68821  ? 172 PRO A CD  1 
ATOM   940  N N   . TYR A 1 156 ? 19.83944 2.10000   33.27991  1.000 67.62945  ? 173 TYR A N   1 
ATOM   941  C CA  . TYR A 1 156 ? 19.51453 1.90564   31.87058  1.000 61.15915  ? 173 TYR A CA  1 
ATOM   942  C C   . TYR A 1 156 ? 19.43232 0.41943   31.58912  1.000 55.07889  ? 173 TYR A C   1 
ATOM   943  O O   . TYR A 1 156 ? 20.19792 -0.35441  32.15846  1.000 53.32917  ? 173 TYR A O   1 
ATOM   944  C CB  . TYR A 1 156 ? 20.55154 2.57951   30.95813  1.000 59.60565  ? 173 TYR A CB  1 
ATOM   945  C CG  . TYR A 1 156 ? 20.50089 4.08207   31.06504  1.000 61.35096  ? 173 TYR A CG  1 
ATOM   946  C CD1 . TYR A 1 156 ? 19.61468 4.82030   30.28421  1.000 62.74104  ? 173 TYR A CD1 1 
ATOM   947  C CD2 . TYR A 1 156 ? 21.30446 4.76783   31.96902  1.000 64.37268  ? 173 TYR A CD2 1 
ATOM   948  C CE1 . TYR A 1 156 ? 19.53381 6.21861   30.38499  1.000 66.45926  ? 173 TYR A CE1 1 
ATOM   949  C CE2 . TYR A 1 156 ? 21.24073 6.17126   32.08061  1.000 68.86479  ? 173 TYR A CE2 1 
ATOM   950  C CZ  . TYR A 1 156 ? 20.35242 6.89337   31.28387  1.000 71.90847  ? 173 TYR A CZ  1 
ATOM   951  O OH  . TYR A 1 156 ? 20.27425 8.27448   31.38325  1.000 72.53835  ? 173 TYR A OH  1 
ATOM   952  N N   . ALA A 1 157 ? 18.50013 0.02235   30.72140  1.000 56.22218  ? 174 ALA A N   1 
ATOM   953  C CA  . ALA A 1 157 ? 18.33109 -1.39622  30.41510  1.000 48.35774  ? 174 ALA A CA  1 
ATOM   954  C C   . ALA A 1 157 ? 19.51331 -1.91283  29.61111  1.000 48.14345  ? 174 ALA A C   1 
ATOM   955  O O   . ALA A 1 157 ? 20.30491 -1.14714  29.05459  1.000 49.35434  ? 174 ALA A O   1 
ATOM   956  C CB  . ALA A 1 157 ? 17.03993 -1.65537  29.63524  1.000 42.01153  ? 174 ALA A CB  1 
ATOM   957  N N   . GLN A 1 158 ? 19.62363 -3.23479  29.53833  1.000 47.00658  ? 175 GLN A N   1 
ATOM   958  C CA  . GLN A 1 158 ? 20.69406 -3.85948  28.77412  1.000 43.89136  ? 175 GLN A CA  1 
ATOM   959  C C   . GLN A 1 158 ? 20.14563 -5.03115  27.98338  1.000 46.35225  ? 175 GLN A C   1 
ATOM   960  O O   . GLN A 1 158 ? 19.63045 -5.99444  28.56491  1.000 47.11871  ? 175 GLN A O   1 
ATOM   961  C CB  . GLN A 1 158 ? 21.80644 -4.33080  29.69186  1.000 46.02648  ? 175 GLN A CB  1 
ATOM   962  C CG  . GLN A 1 158 ? 22.79544 -5.21433  28.99862  1.000 48.60720  ? 175 GLN A CG  1 
ATOM   963  C CD  . GLN A 1 158 ? 24.06700 -5.34062  29.78839  1.000 50.88724  ? 175 GLN A CD  1 
ATOM   964  O OE1 . GLN A 1 158 ? 24.48788 -4.38340  30.44680  1.000 53.19564  ? 175 GLN A OE1 1 
ATOM   965  N NE2 . GLN A 1 158 ? 24.70137 -6.51102  29.72573  1.000 49.25077  ? 175 GLN A NE2 1 
ATOM   966  N N   . ALA A 1 159 ? 20.28091 -4.96545  26.66525  1.000 45.55344  ? 176 ALA A N   1 
ATOM   967  C CA  . ALA A 1 159 ? 19.86523 -6.06410  25.80860  1.000 44.18144  ? 176 ALA A CA  1 
ATOM   968  C C   . ALA A 1 159 ? 21.05088 -6.94328  25.44242  1.000 43.75410  ? 176 ALA A C   1 
ATOM   969  O O   . ALA A 1 159 ? 22.18497 -6.48278  25.30877  1.000 42.34640  ? 176 ALA A O   1 
ATOM   970  C CB  . ALA A 1 159 ? 19.18916 -5.56854  24.53488  1.000 43.49580  ? 176 ALA A CB  1 
ATOM   971  N N   . THR A 1 160 ? 20.75185 -8.22634  25.27907  1.000 47.83479  ? 177 THR A N   1 
ATOM   972  C CA  . THR A 1 160 ? 21.70588 -9.28186  24.96644  1.000 47.97010  ? 177 THR A CA  1 
ATOM   973  C C   . THR A 1 160 ? 21.13728 -10.03986 23.77768  1.000 46.59733  ? 177 THR A C   1 
ATOM   974  O O   . THR A 1 160 ? 20.02639 -10.56617 23.86251  1.000 47.80772  ? 177 THR A O   1 
ATOM   975  C CB  . THR A 1 160 ? 21.89472 -10.20939 26.17685  1.000 50.69237  ? 177 THR A CB  1 
ATOM   976  O OG1 . THR A 1 160 ? 21.94914 -9.43386  27.40588  1.000 53.40746  ? 177 THR A OG1 1 
ATOM   977  C CG2 . THR A 1 160 ? 23.11722 -11.10023 26.00228  1.000 48.62380  ? 177 THR A CG2 1 
ATOM   978  N N   . PHE A 1 161 ? 21.86665 -10.06272 22.66480  1.000 44.48704  ? 178 PHE A N   1 
ATOM   979  C CA  . PHE A 1 161 ? 21.35936 -10.56441 21.38904  1.000 44.28813  ? 178 PHE A CA  1 
ATOM   980  C C   . PHE A 1 161 ? 22.16843 -11.78604 20.96839  1.000 47.70154  ? 178 PHE A C   1 
ATOM   981  O O   . PHE A 1 161 ? 23.35621 -11.65565 20.64980  1.000 47.16880  ? 178 PHE A O   1 
ATOM   982  C CB  . PHE A 1 161 ? 21.45638 -9.49189  20.30725  1.000 44.59971  ? 178 PHE A CB  1 
ATOM   983  C CG  . PHE A 1 161 ? 20.67742 -8.24840  20.60393  1.000 45.21157  ? 178 PHE A CG  1 
ATOM   984  C CD1 . PHE A 1 161 ? 19.29205 -8.27559  20.65236  1.000 44.25645  ? 178 PHE A CD1 1 
ATOM   985  C CD2 . PHE A 1 161 ? 21.33520 -7.03430  20.79363  1.000 44.20050  ? 178 PHE A CD2 1 
ATOM   986  C CE1 . PHE A 1 161 ? 18.57261 -7.11802  20.91460  1.000 44.16672  ? 178 PHE A CE1 1 
ATOM   987  C CE2 . PHE A 1 161 ? 20.62339 -5.87973  21.06518  1.000 42.97837  ? 178 PHE A CE2 1 
ATOM   988  C CZ  . PHE A 1 161 ? 19.23580 -5.91883  21.11824  1.000 41.08089  ? 178 PHE A CZ  1 
ATOM   989  N N   . LEU A 1 162 ? 21.52678 -12.96078 20.92219  1.000 47.08131  ? 179 LEU A N   1 
ATOM   990  C CA  . LEU A 1 162 ? 22.18144 -14.19528 20.49155  1.000 47.62282  ? 179 LEU A CA  1 
ATOM   991  C C   . LEU A 1 162 ? 21.58217 -14.71760 19.19441  1.000 47.82796  ? 179 LEU A C   1 
ATOM   992  O O   . LEU A 1 162 ? 20.36417 -14.87811 19.08958  1.000 50.35579  ? 179 LEU A O   1 
ATOM   993  C CB  . LEU A 1 162 ? 22.08887 -15.27867 21.56388  1.000 46.21442  ? 179 LEU A CB  1 
ATOM   994  C CG  . LEU A 1 162 ? 22.72587 -16.62437 21.22394  1.000 48.54126  ? 179 LEU A CG  1 
ATOM   995  C CD1 . LEU A 1 162 ? 24.18871 -16.48166 20.77907  1.000 57.49532  ? 179 LEU A CD1 1 
ATOM   996  C CD2 . LEU A 1 162 ? 22.62716 -17.54462 22.42181  1.000 50.40729  ? 179 LEU A CD2 1 
ATOM   997  N N   . ARG A 1 163 ? 22.43694 -14.98542 18.20971  1.000 49.44557  ? 180 ARG A N   1 
ATOM   998  C CA  . ARG A 1 163 ? 22.03661 -15.70056 17.00645  1.000 53.63890  ? 180 ARG A CA  1 
ATOM   999  C C   . ARG A 1 163 ? 22.96665 -16.87838 16.80611  1.000 59.83944  ? 180 ARG A C   1 
ATOM   1000 O O   . ARG A 1 163 ? 24.18932 -16.71063 16.71215  1.000 60.45147  ? 180 ARG A O   1 
ATOM   1001 C CB  . ARG A 1 163 ? 22.05374 -14.85006 15.73645  1.000 56.87385  ? 180 ARG A CB  1 
ATOM   1002 C CG  . ARG A 1 163 ? 22.06379 -15.73664 14.49980  1.000 61.87050  ? 180 ARG A CG  1 
ATOM   1003 C CD  . ARG A 1 163 ? 21.03624 -15.30461 13.49183  1.000 64.49144  ? 180 ARG A CD  1 
ATOM   1004 N NE  . ARG A 1 163 ? 21.52572 -14.17089 12.72323  1.000 72.67902  ? 180 ARG A NE  1 
ATOM   1005 C CZ  . ARG A 1 163 ? 22.37243 -14.27368 11.70811  1.000 81.10894  ? 180 ARG A CZ  1 
ATOM   1006 N NH1 . ARG A 1 163 ? 22.75562 -15.45463 11.25409  1.000 86.07190  ? 180 ARG A NH1 1 
ATOM   1007 N NH2 . ARG A 1 163 ? 22.83451 -13.16490 11.12688  1.000 81.54404  ? 180 ARG A NH2 1 
ATOM   1008 N N   . VAL A 1 164 ? 22.35949 -18.05128 16.70118  1.000 63.15002  ? 181 VAL A N   1 
ATOM   1009 C CA  . VAL A 1 164 ? 22.99814 -19.34859 16.57930  1.000 66.11126  ? 181 VAL A CA  1 
ATOM   1010 C C   . VAL A 1 164 ? 23.11198 -19.70307 15.09819  1.000 76.62383  ? 181 VAL A C   1 
ATOM   1011 O O   . VAL A 1 164 ? 22.28218 -19.25267 14.28895  1.000 77.04183  ? 181 VAL A O   1 
ATOM   1012 C CB  . VAL A 1 164 ? 22.18737 -20.35943 17.39971  1.000 70.35290  ? 181 VAL A CB  1 
ATOM   1013 C CG1 . VAL A 1 164 ? 22.48068 -21.78125 17.02242  1.000 76.81035  ? 181 VAL A CG1 1 
ATOM   1014 C CG2 . VAL A 1 164 ? 22.49693 -20.13559 18.85724  1.000 69.54146  ? 181 VAL A CG2 1 
ATOM   1015 N N   . PRO A 1 165 ? 24.15618 -20.47199 14.68554  1.000 80.64336  ? 182 PRO A N   1 
ATOM   1016 C CA  . PRO A 1 165 ? 24.29647 -20.86893 13.27344  1.000 81.25186  ? 182 PRO A CA  1 
ATOM   1017 C C   . PRO A 1 165 ? 23.08015 -21.53991 12.63067  1.000 87.86721  ? 182 PRO A C   1 
ATOM   1018 O O   . PRO A 1 165 ? 22.11525 -21.90282 13.31345  1.000 88.21853  ? 182 PRO A O   1 
ATOM   1019 C CB  . PRO A 1 165 ? 25.50012 -21.83176 13.30767  1.000 79.28857  ? 182 PRO A CB  1 
ATOM   1020 C CG  . PRO A 1 165 ? 25.88448 -22.01329 14.76438  1.000 75.36674  ? 182 PRO A CG  1 
ATOM   1021 C CD  . PRO A 1 165 ? 25.37722 -20.78519 15.45030  1.000 79.13418  ? 182 PRO A CD  1 
ATOM   1022 N N   . LYS A 1 166 ? 23.15237 -21.69576 11.29903  1.000 97.11971  ? 183 LYS A N   1 
ATOM   1023 C CA  . LYS A 1 166 ? 22.16260 -22.35098 10.41536  1.000 102.88422 ? 183 LYS A CA  1 
ATOM   1024 C C   . LYS A 1 166 ? 20.71954 -22.24994 10.94449  1.000 107.08884 ? 183 LYS A C   1 
ATOM   1025 O O   . LYS A 1 166 ? 20.04336 -23.25376 11.19950  1.000 110.39609 ? 183 LYS A O   1 
ATOM   1026 C CB  . LYS A 1 166 ? 22.56030 -23.82789 10.16829  1.000 97.29911  ? 183 LYS A CB  1 
ATOM   1027 C CG  . LYS A 1 166 ? 21.68338 -24.56349 9.14829   1.000 102.96521 ? 183 LYS A CG  1 
ATOM   1028 C CD  . LYS A 1 166 ? 22.16335 -25.97621 8.87016   1.000 110.97050 ? 183 LYS A CD  1 
ATOM   1029 C CE  . LYS A 1 166 ? 21.26584 -26.67609 7.85536   1.000 114.41027 ? 183 LYS A CE  1 
ATOM   1030 N NZ  . LYS A 1 166 ? 21.71999 -28.06084 7.53174   1.000 121.82604 ? 183 LYS A NZ  1 
ATOM   1031 N N   . ASP A 1 182 ? 13.33276 -32.84859 18.09294  1.000 117.26316 ? 199 ASP A N   1 
ATOM   1032 C CA  . ASP A 1 182 ? 14.73530 -33.22856 18.22567  1.000 117.34216 ? 199 ASP A CA  1 
ATOM   1033 C C   . ASP A 1 182 ? 15.65393 -32.07551 17.85424  1.000 113.41287 ? 199 ASP A C   1 
ATOM   1034 O O   . ASP A 1 182 ? 16.47460 -31.64990 18.65760  1.000 114.60547 ? 199 ASP A O   1 
ATOM   1035 C CB  . ASP A 1 182 ? 15.07494 -34.43238 17.35434  1.000 126.07272 ? 199 ASP A CB  1 
ATOM   1036 C CG  . ASP A 1 182 ? 16.56879 -34.65663 17.25269  1.000 126.74135 ? 199 ASP A CG  1 
ATOM   1037 O OD1 . ASP A 1 182 ? 17.16025 -35.10974 18.25739  1.000 125.43488 ? 199 ASP A OD1 1 
ATOM   1038 O OD2 . ASP A 1 182 ? 17.15524 -34.34752 16.19166  1.000 127.90443 ? 199 ASP A OD2 1 
ATOM   1039 N N   . GLU A 1 183 ? 15.52072 -31.55621 16.63359  1.000 110.79018 ? 200 GLU A N   1 
ATOM   1040 C CA  . GLU A 1 183 ? 16.29057 -30.37468 16.26968  1.000 105.32707 ? 200 GLU A CA  1 
ATOM   1041 C C   . GLU A 1 183 ? 16.02123 -29.21689 17.22439  1.000 98.26922  ? 200 GLU A C   1 
ATOM   1042 O O   . GLU A 1 183 ? 16.77312 -28.23353 17.24180  1.000 90.93128  ? 200 GLU A O   1 
ATOM   1043 C CB  . GLU A 1 183 ? 15.96801 -29.95785 14.83928  1.000 111.33639 ? 200 GLU A CB  1 
ATOM   1044 C CG  . GLU A 1 183 ? 16.72659 -28.71640 14.39503  1.000 116.34711 ? 200 GLU A CG  1 
ATOM   1045 C CD  . GLU A 1 183 ? 15.94479 -27.85965 13.42739  1.000 127.43580 ? 200 GLU A CD  1 
ATOM   1046 O OE1 . GLU A 1 183 ? 15.94150 -28.16926 12.21227  1.000 133.18154 ? 200 GLU A OE1 1 
ATOM   1047 O OE2 . GLU A 1 183 ? 15.32357 -26.87625 13.89406  1.000 128.31978 ? 200 GLU A OE2 1 
ATOM   1048 N N   . ASN A 1 184 ? 14.96160 -29.30858 18.02473  1.000 101.26751 ? 201 ASN A N   1 
ATOM   1049 C CA  . ASN A 1 184 ? 14.79361 -28.32824 19.08048  1.000 97.13581  ? 201 ASN A CA  1 
ATOM   1050 C C   . ASN A 1 184 ? 15.77750 -28.56724 20.22110  1.000 93.13025  ? 201 ASN A C   1 
ATOM   1051 O O   . ASN A 1 184 ? 16.18203 -27.60416 20.88527  1.000 89.46024  ? 201 ASN A O   1 
ATOM   1052 C CB  . ASN A 1 184 ? 13.35540 -28.33838 19.58285  1.000 101.58743 ? 201 ASN A CB  1 
ATOM   1053 C CG  . ASN A 1 184 ? 13.09409 -27.22818 20.57546  1.000 109.69571 ? 201 ASN A CG  1 
ATOM   1054 O OD1 . ASN A 1 184 ? 13.39907 -26.06127 20.30497  1.000 105.86612 ? 201 ASN A OD1 1 
ATOM   1055 N ND2 . ASN A 1 184 ? 12.52568 -27.57777 21.73330  1.000 111.11600 ? 201 ASN A ND2 1 
ATOM   1056 N N   . LYS A 1 185 ? 16.18521 -29.83077 20.45455  1.000 92.11609  ? 202 LYS A N   1 
ATOM   1057 C CA  . LYS A 1 185 ? 17.20625 -30.10214 21.46791  1.000 82.09149  ? 202 LYS A CA  1 
ATOM   1058 C C   . LYS A 1 185 ? 18.56268 -29.55774 21.04779  1.000 78.53565  ? 202 LYS A C   1 
ATOM   1059 O O   . LYS A 1 185 ? 19.30054 -29.03465 21.88581  1.000 79.58696  ? 202 LYS A O   1 
ATOM   1060 C CB  . LYS A 1 185 ? 17.34916 -31.59765 21.77708  1.000 87.76331  ? 202 LYS A CB  1 
ATOM   1061 C CG  . LYS A 1 185 ? 16.08288 -32.47396 21.85265  1.000 101.06723 ? 202 LYS A CG  1 
ATOM   1062 C CD  . LYS A 1 185 ? 16.48242 -33.98220 21.87496  1.000 102.80989 ? 202 LYS A CD  1 
ATOM   1063 C CE  . LYS A 1 185 ? 15.28260 -34.94793 21.97022  1.000 103.18898 ? 202 LYS A CE  1 
ATOM   1064 N NZ  . LYS A 1 185 ? 15.33106 -35.93109 23.11419  1.000 90.29158  ? 202 LYS A NZ  1 
ATOM   1065 N N   . LEU A 1 186 ? 18.92993 -29.69496 19.76990  1.000 79.06733  ? 203 LEU A N   1 
ATOM   1066 C CA  . LEU A 1 186 ? 20.15745 -29.06207 19.28772  1.000 73.15671  ? 203 LEU A CA  1 
ATOM   1067 C C   . LEU A 1 186 ? 20.16928 -27.57883 19.60795  1.000 74.58600  ? 203 LEU A C   1 
ATOM   1068 O O   . LEU A 1 186 ? 21.14402 -27.05478 20.15654  1.000 75.09201  ? 203 LEU A O   1 
ATOM   1069 C CB  . LEU A 1 186 ? 20.31707 -29.26506 17.78181  1.000 72.97294  ? 203 LEU A CB  1 
ATOM   1070 C CG  . LEU A 1 186 ? 21.31943 -28.34539 17.05999  1.000 70.20332  ? 203 LEU A CG  1 
ATOM   1071 C CD1 . LEU A 1 186 ? 22.72626 -28.37405 17.63729  1.000 74.97219  ? 203 LEU A CD1 1 
ATOM   1072 C CD2 . LEU A 1 186 ? 21.35712 -28.70328 15.60374  1.000 72.89723  ? 203 LEU A CD2 1 
ATOM   1073 N N   . PHE A 1 187 ? 19.09118 -26.88790 19.24247  1.000 74.83006  ? 204 PHE A N   1 
ATOM   1074 C CA  . PHE A 1 187 ? 18.96328 -25.46154 19.49497  1.000 73.83915  ? 204 PHE A CA  1 
ATOM   1075 C C   . PHE A 1 187 ? 19.32829 -25.11786 20.93988  1.000 75.99241  ? 204 PHE A C   1 
ATOM   1076 O O   . PHE A 1 187 ? 20.10121 -24.18394 21.19755  1.000 72.77740  ? 204 PHE A O   1 
ATOM   1077 C CB  . PHE A 1 187 ? 17.52903 -25.05181 19.16664  1.000 78.01396  ? 204 PHE A CB  1 
ATOM   1078 C CG  . PHE A 1 187 ? 17.36487 -23.59809 18.81007  1.000 81.20172  ? 204 PHE A CG  1 
ATOM   1079 C CD1 . PHE A 1 187 ? 18.28761 -22.65027 19.22557  1.000 81.27549  ? 204 PHE A CD1 1 
ATOM   1080 C CD2 . PHE A 1 187 ? 16.26896 -23.18411 18.05760  1.000 76.78898  ? 204 PHE A CD2 1 
ATOM   1081 C CE1 . PHE A 1 187 ? 18.12556 -21.33030 18.88638  1.000 83.21907  ? 204 PHE A CE1 1 
ATOM   1082 C CE2 . PHE A 1 187 ? 16.10366 -21.87969 17.71231  1.000 74.35085  ? 204 PHE A CE2 1 
ATOM   1083 C CZ  . PHE A 1 187 ? 17.02123 -20.94129 18.12992  1.000 81.19265  ? 204 PHE A CZ  1 
ATOM   1084 N N   . GLU A 1 188 ? 18.79565 -25.88889 21.89666  1.000 76.27835  ? 205 GLU A N   1 
ATOM   1085 C CA  . GLU A 1 188 ? 19.01454 -25.58967 23.30701  1.000 73.25032  ? 205 GLU A CA  1 
ATOM   1086 C C   . GLU A 1 188 ? 20.47209 -25.76759 23.68627  1.000 69.95843  ? 205 GLU A C   1 
ATOM   1087 O O   . GLU A 1 188 ? 21.02763 -24.94495 24.42033  1.000 73.31124  ? 205 GLU A O   1 
ATOM   1088 C CB  . GLU A 1 188 ? 18.13958 -26.48000 24.17839  1.000 80.13757  ? 205 GLU A CB  1 
ATOM   1089 C CG  . GLU A 1 188 ? 16.65971 -26.17166 24.09959  1.000 89.25685  ? 205 GLU A CG  1 
ATOM   1090 C CD  . GLU A 1 188 ? 15.80088 -27.32492 24.62417  1.000 102.58564 ? 205 GLU A CD  1 
ATOM   1091 O OE1 . GLU A 1 188 ? 16.37744 -28.35029 25.09998  1.000 94.93409  ? 205 GLU A OE1 1 
ATOM   1092 O OE2 . GLU A 1 188 ? 14.54919 -27.20092 24.55003  1.000 105.89037 ? 205 GLU A OE2 1 
ATOM   1093 N N   . GLN A 1 189 ? 21.10916 -26.83197 23.18901  1.000 70.53562  ? 206 GLN A N   1 
ATOM   1094 C CA  . GLN A 1 189 ? 22.51383 -27.08588 23.50785  1.000 68.94179  ? 206 GLN A CA  1 
ATOM   1095 C C   . GLN A 1 189 ? 23.42879 -26.02170 22.91825  1.000 69.36138  ? 206 GLN A C   1 
ATOM   1096 O O   . GLN A 1 189 ? 24.37471 -25.57162 23.57428  1.000 68.26996  ? 206 GLN A O   1 
ATOM   1097 C CB  . GLN A 1 189 ? 22.91987 -28.46636 23.01072  1.000 66.41634  ? 206 GLN A CB  1 
ATOM   1098 C CG  . GLN A 1 189 ? 22.05545 -29.54865 23.57180  1.000 64.72122  ? 206 GLN A CG  1 
ATOM   1099 C CD  . GLN A 1 189 ? 22.31071 -29.76996 25.03191  1.000 66.30934  ? 206 GLN A CD  1 
ATOM   1100 O OE1 . GLN A 1 189 ? 23.44273 -29.96292 25.45204  1.000 67.50761  ? 206 GLN A OE1 1 
ATOM   1101 N NE2 . GLN A 1 189 ? 21.25936 -29.70355 25.82792  1.000 75.34053  ? 206 GLN A NE2 1 
ATOM   1102 N N   . GLN A 1 190 ? 23.17013 -25.61205 21.67924  1.000 70.43722  ? 207 GLN A N   1 
ATOM   1103 C CA  . GLN A 1 190 ? 23.91042 -24.49723 21.10357  1.000 71.24848  ? 207 GLN A CA  1 
ATOM   1104 C C   . GLN A 1 190 ? 23.84285 -23.26418 21.98934  1.000 71.07055  ? 207 GLN A C   1 
ATOM   1105 O O   . GLN A 1 190 ? 24.87560 -22.68268 22.34620  1.000 70.17278  ? 207 GLN A O   1 
ATOM   1106 C CB  . GLN A 1 190 ? 23.37249 -24.21256 19.71617  1.000 69.25344  ? 207 GLN A CB  1 
ATOM   1107 C CG  . GLN A 1 190 ? 23.99868 -25.11836 18.72678  1.000 73.80543  ? 207 GLN A CG  1 
ATOM   1108 C CD  . GLN A 1 190 ? 23.44550 -24.91964 17.35981  1.000 85.88119  ? 207 GLN A CD  1 
ATOM   1109 O OE1 . GLN A 1 190 ? 22.22449 -24.95816 17.16696  1.000 85.91721  ? 207 GLN A OE1 1 
ATOM   1110 N NE2 . GLN A 1 190 ? 24.32367 -24.60961 16.40286  1.000 89.59939  ? 207 GLN A NE2 1 
ATOM   1111 N N   . LYS A 1 191 ? 22.62853 -22.87378 22.38010  1.000 70.51906  ? 208 LYS A N   1 
ATOM   1112 C CA  . LYS A 1 191 ? 22.46137 -21.72302 23.25723  1.000 70.74617  ? 208 LYS A CA  1 
ATOM   1113 C C   . LYS A 1 191 ? 23.26389 -21.88069 24.54971  1.000 71.68445  ? 208 LYS A C   1 
ATOM   1114 O O   . LYS A 1 191 ? 23.85653 -20.91527 25.04589  1.000 70.01863  ? 208 LYS A O   1 
ATOM   1115 C CB  . LYS A 1 191 ? 20.97027 -21.51455 23.53766  1.000 74.61816  ? 208 LYS A CB  1 
ATOM   1116 C CG  . LYS A 1 191 ? 20.14305 -21.14519 22.27598  1.000 78.18239  ? 208 LYS A CG  1 
ATOM   1117 C CD  . LYS A 1 191 ? 18.67131 -21.48069 22.45076  1.000 79.65179  ? 208 LYS A CD  1 
ATOM   1118 C CE  . LYS A 1 191 ? 17.77445 -20.35082 21.99915  1.000 77.67456  ? 208 LYS A CE  1 
ATOM   1119 N NZ  . LYS A 1 191 ? 16.36786 -20.81697 21.79402  1.000 83.25096  ? 208 LYS A NZ  1 
ATOM   1120 N N   . ARG A 1 192 ? 23.32807 -23.09430 25.09582  1.000 71.03624  ? 209 ARG A N   1 
ATOM   1121 C CA  . ARG A 1 192 ? 24.06721 -23.26052 26.33977  1.000 72.70468  ? 209 ARG A CA  1 
ATOM   1122 C C   . ARG A 1 192 ? 25.56671 -23.14174 26.11947  1.000 73.92145  ? 209 ARG A C   1 
ATOM   1123 O O   . ARG A 1 192 ? 26.30304 -22.78516 27.04653  1.000 74.98915  ? 209 ARG A O   1 
ATOM   1124 C CB  . ARG A 1 192 ? 23.72292 -24.59804 26.99943  1.000 74.80197  ? 209 ARG A CB  1 
ATOM   1125 C CG  . ARG A 1 192 ? 24.45000 -24.83790 28.32727  1.000 82.36997  ? 209 ARG A CG  1 
ATOM   1126 C CD  . ARG A 1 192 ? 23.93527 -23.96213 29.48530  1.000 93.08412  ? 209 ARG A CD  1 
ATOM   1127 N NE  . ARG A 1 192 ? 22.71442 -24.47070 30.11088  1.000 106.55505 ? 209 ARG A NE  1 
ATOM   1128 C CZ  . ARG A 1 192 ? 22.68864 -25.36933 31.09516  1.000 113.41298 ? 209 ARG A CZ  1 
ATOM   1129 N NH1 . ARG A 1 192 ? 23.79914 -25.95497 31.53113  1.000 111.11572 ? 209 ARG A NH1 1 
ATOM   1130 N NH2 . ARG A 1 192 ? 21.51966 -25.69760 31.65284  1.000 106.92460 ? 209 ARG A NH2 1 
ATOM   1131 N N   . ALA A 1 193 ? 26.04409 -23.42383 24.90844  1.000 76.24699  ? 210 ALA A N   1 
ATOM   1132 C CA  . ALA A 1 193 ? 27.48407 -23.37368 24.68256  1.000 73.93865  ? 210 ALA A CA  1 
ATOM   1133 C C   . ALA A 1 193 ? 27.96381 -21.95224 24.46680  1.000 75.10376  ? 210 ALA A C   1 
ATOM   1134 O O   . ALA A 1 193 ? 29.07649 -21.60624 24.88462  1.000 75.26380  ? 210 ALA A O   1 
ATOM   1135 C CB  . ALA A 1 193 ? 27.86297 -24.23710 23.48849  1.000 71.71979  ? 210 ALA A CB  1 
ATOM   1136 N N   . TYR A 1 194 ? 27.13681 -21.12804 23.81849  1.000 72.22156  ? 211 TYR A N   1 
ATOM   1137 C CA  . TYR A 1 194 ? 27.45152 -19.71519 23.68453  1.000 67.11260  ? 211 TYR A CA  1 
ATOM   1138 C C   . TYR A 1 194 ? 27.46331 -19.02489 25.03379  1.000 67.30883  ? 211 TYR A C   1 
ATOM   1139 O O   . TYR A 1 194 ? 28.35381 -18.21982 25.31970  1.000 69.27793  ? 211 TYR A O   1 
ATOM   1140 C CB  . TYR A 1 194 ? 26.44855 -19.05403 22.76360  1.000 63.72431  ? 211 TYR A CB  1 
ATOM   1141 C CG  . TYR A 1 194 ? 26.80731 -19.26765 21.33744  1.000 71.06456  ? 211 TYR A CG  1 
ATOM   1142 C CD1 . TYR A 1 194 ? 27.76792 -18.48250 20.71752  1.000 75.61488  ? 211 TYR A CD1 1 
ATOM   1143 C CD2 . TYR A 1 194 ? 26.22863 -20.28837 20.61569  1.000 73.87084  ? 211 TYR A CD2 1 
ATOM   1144 C CE1 . TYR A 1 194 ? 28.11789 -18.69463 19.39569  1.000 77.75871  ? 211 TYR A CE1 1 
ATOM   1145 C CE2 . TYR A 1 194 ? 26.56173 -20.50385 19.30028  1.000 77.98208  ? 211 TYR A CE2 1 
ATOM   1146 C CZ  . TYR A 1 194 ? 27.50660 -19.71259 18.69183  1.000 78.97140  ? 211 TYR A CZ  1 
ATOM   1147 O OH  . TYR A 1 194 ? 27.82335 -19.94738 17.37326  1.000 80.77259  ? 211 TYR A OH  1 
ATOM   1148 N N   . PHE A 1 195 ? 26.48784 -19.32039 25.88430  1.000 67.81854  ? 212 PHE A N   1 
ATOM   1149 C CA  . PHE A 1 195 ? 26.52197 -18.69500 27.19540  1.000 66.45633  ? 212 PHE A CA  1 
ATOM   1150 C C   . PHE A 1 195 ? 27.67658 -19.21645 28.03642  1.000 72.50603  ? 212 PHE A C   1 
ATOM   1151 O O   . PHE A 1 195 ? 28.14566 -18.50881 28.93416  1.000 75.55811  ? 212 PHE A O   1 
ATOM   1152 C CB  . PHE A 1 195 ? 25.18457 -18.88125 27.91133  1.000 61.30208  ? 212 PHE A CB  1 
ATOM   1153 C CG  . PHE A 1 195 ? 24.15067 -17.89677 27.48110  1.000 58.61807  ? 212 PHE A CG  1 
ATOM   1154 C CD1 . PHE A 1 195 ? 24.19524 -16.58661 27.92700  1.000 62.92593  ? 212 PHE A CD1 1 
ATOM   1155 C CD2 . PHE A 1 195 ? 23.16156 -18.25902 26.59359  1.000 62.07123  ? 212 PHE A CD2 1 
ATOM   1156 C CE1 . PHE A 1 195 ? 23.26365 -15.64301 27.50059  1.000 59.99070  ? 212 PHE A CE1 1 
ATOM   1157 C CE2 . PHE A 1 195 ? 22.22844 -17.32950 26.16748  1.000 61.51136  ? 212 PHE A CE2 1 
ATOM   1158 C CZ  . PHE A 1 195 ? 22.27933 -16.01744 26.62744  1.000 57.54086  ? 212 PHE A CZ  1 
ATOM   1159 N N   . ASN A 1 196 ? 28.16613 -20.42053 27.75795  1.000 71.15005  ? 213 ASN A N   1 
ATOM   1160 C CA  . ASN A 1 196 ? 29.32458 -20.88022 28.50219  1.000 76.21999  ? 213 ASN A CA  1 
ATOM   1161 C C   . ASN A 1 196 ? 30.59584 -20.25287 27.95532  1.000 77.82304  ? 213 ASN A C   1 
ATOM   1162 O O   . ASN A 1 196 ? 31.45447 -19.80274 28.72321  1.000 82.39756  ? 213 ASN A O   1 
ATOM   1163 C CB  . ASN A 1 196 ? 29.39205 -22.40681 28.47562  1.000 82.88565  ? 213 ASN A CB  1 
ATOM   1164 C CG  . ASN A 1 196 ? 28.34765 -23.04764 29.37570  1.000 84.86153  ? 213 ASN A CG  1 
ATOM   1165 O OD1 . ASN A 1 196 ? 27.84567 -22.41631 30.31496  1.000 82.37078  ? 213 ASN A OD1 1 
ATOM   1166 N ND2 . ASN A 1 196 ? 28.00710 -24.30168 29.08840  1.000 83.28707  ? 213 ASN A ND2 1 
ATOM   1167 N N   . TYR A 1 197 ? 30.72041 -20.18774 26.63292  1.000 74.34679  ? 214 TYR A N   1 
ATOM   1168 C CA  . TYR A 1 197 ? 31.90225 -19.56972 26.05383  1.000 74.31007  ? 214 TYR A CA  1 
ATOM   1169 C C   . TYR A 1 197 ? 32.03400 -18.11547 26.48843  1.000 74.56502  ? 214 TYR A C   1 
ATOM   1170 O O   . TYR A 1 197 ? 33.14975 -17.61034 26.62255  1.000 79.96824  ? 214 TYR A O   1 
ATOM   1171 C CB  . TYR A 1 197 ? 31.85825 -19.68629 24.52887  1.000 74.10327  ? 214 TYR A CB  1 
ATOM   1172 C CG  . TYR A 1 197 ? 33.10400 -19.18947 23.83017  1.000 73.15017  ? 214 TYR A CG  1 
ATOM   1173 C CD1 . TYR A 1 197 ? 34.21521 -19.99590 23.70255  1.000 72.79255  ? 214 TYR A CD1 1 
ATOM   1174 C CD2 . TYR A 1 197 ? 33.16718 -17.90933 23.30804  1.000 75.84049  ? 214 TYR A CD2 1 
ATOM   1175 C CE1 . TYR A 1 197 ? 35.35447 -19.56102 23.07121  1.000 75.50271  ? 214 TYR A CE1 1 
ATOM   1176 C CE2 . TYR A 1 197 ? 34.30911 -17.45582 22.67344  1.000 78.90985  ? 214 TYR A CE2 1 
ATOM   1177 C CZ  . TYR A 1 197 ? 35.40656 -18.29494 22.55490  1.000 83.54699  ? 214 TYR A CZ  1 
ATOM   1178 O OH  . TYR A 1 197 ? 36.55721 -17.85950 21.91469  1.000 89.53576  ? 214 TYR A OH  1 
ATOM   1179 N N   . ALA A 1 198 ? 30.92118 -17.42721 26.73552  1.000 76.08913  ? 215 ALA A N   1 
ATOM   1180 C CA  . ALA A 1 198 ? 31.03622 -16.04085 27.17337  1.000 75.63616  ? 215 ALA A CA  1 
ATOM   1181 C C   . ALA A 1 198 ? 31.45739 -15.95078 28.63541  1.000 81.67494  ? 215 ALA A C   1 
ATOM   1182 O O   . ALA A 1 198 ? 32.30011 -15.12265 28.98387  1.000 82.57603  ? 215 ALA A O   1 
ATOM   1183 C CB  . ALA A 1 198 ? 29.72257 -15.29792 26.94025  1.000 66.16185  ? 215 ALA A CB  1 
ATOM   1184 N N   . ASN A 1 199 ? 30.89619 -16.80262 29.49867  1.000 81.90771  ? 216 ASN A N   1 
ATOM   1185 C CA  . ASN A 1 199 ? 31.23833 -16.77693 30.91889  1.000 84.51168  ? 216 ASN A CA  1 
ATOM   1186 C C   . ASN A 1 199 ? 32.66261 -17.25054 31.16800  1.000 95.36643  ? 216 ASN A C   1 
ATOM   1187 O O   . ASN A 1 199 ? 33.44043 -16.57636 31.85364  1.000 97.70150  ? 216 ASN A O   1 
ATOM   1188 C CB  . ASN A 1 199 ? 30.27262 -17.65027 31.70506  1.000 84.00775  ? 216 ASN A CB  1 
ATOM   1189 C CG  . ASN A 1 199 ? 28.96930 -16.97365 31.96027  1.000 85.61851  ? 216 ASN A CG  1 
ATOM   1190 O OD1 . ASN A 1 199 ? 28.92238 -15.92377 32.61450  1.000 90.32119  ? 216 ASN A OD1 1 
ATOM   1191 N ND2 . ASN A 1 199 ? 27.88607 -17.56575 31.45910  1.000 78.31558  ? 216 ASN A ND2 1 
ATOM   1192 N N   . ASP A 1 200 ? 33.01258 -18.42805 30.64869  1.000 115.72613 ? 217 ASP A N   1 
ATOM   1193 C CA  . ASP A 1 200 ? 34.28453 -19.04263 31.00630  1.000 117.43447 ? 217 ASP A CA  1 
ATOM   1194 C C   . ASP A 1 200 ? 35.45219 -18.33198 30.33436  1.000 119.49181 ? 217 ASP A C   1 
ATOM   1195 O O   . ASP A 1 200 ? 36.42317 -17.94855 30.99794  1.000 123.56069 ? 217 ASP A O   1 
ATOM   1196 C CB  . ASP A 1 200 ? 34.26826 -20.52618 30.62947  1.000 114.82779 ? 217 ASP A CB  1 
ATOM   1197 C CG  . ASP A 1 200 ? 33.11939 -21.28482 31.28423  1.000 115.51005 ? 217 ASP A CG  1 
ATOM   1198 O OD1 . ASP A 1 200 ? 32.07323 -20.65187 31.55641  1.000 115.02738 ? 217 ASP A OD1 1 
ATOM   1199 O OD2 . ASP A 1 200 ? 33.25929 -22.50637 31.52877  1.000 113.49327 ? 217 ASP A OD2 1 
ATOM   1200 N N   . VAL A 1 201 ? 35.35315 -18.12955 29.02167  1.000 95.40560  ? 218 VAL A N   1 
ATOM   1201 C CA  . VAL A 1 201 ? 36.42685 -17.61213 28.17693  1.000 85.94183  ? 218 VAL A CA  1 
ATOM   1202 C C   . VAL A 1 201 ? 36.51380 -16.08801 28.19146  1.000 87.65768  ? 218 VAL A C   1 
ATOM   1203 O O   . VAL A 1 201 ? 37.56766 -15.52314 28.51130  1.000 85.16207  ? 218 VAL A O   1 
ATOM   1204 C CB  . VAL A 1 201 ? 36.24005 -18.11811 26.73628  1.000 79.05775  ? 218 VAL A CB  1 
ATOM   1205 C CG1 . VAL A 1 201 ? 37.41920 -17.76001 25.90171  1.000 80.36506  ? 218 VAL A CG1 1 
ATOM   1206 C CG2 . VAL A 1 201 ? 36.04343 -19.60506 26.74100  1.000 81.64593  ? 218 VAL A CG2 1 
ATOM   1207 N N   . ILE A 1 202 ? 35.41816 -15.41457 27.83082  1.000 82.38816  ? 219 ILE A N   1 
ATOM   1208 C CA  . ILE A 1 202 ? 35.45263 -13.98020 27.54747  1.000 76.55427  ? 219 ILE A CA  1 
ATOM   1209 C C   . ILE A 1 202 ? 35.32087 -13.12797 28.81005  1.000 82.64449  ? 219 ILE A C   1 
ATOM   1210 O O   . ILE A 1 202 ? 36.01298 -12.11641 28.95768  1.000 86.52615  ? 219 ILE A O   1 
ATOM   1211 C CB  . ILE A 1 202 ? 34.35958 -13.63749 26.52084  1.000 70.51080  ? 219 ILE A CB  1 
ATOM   1212 C CG1 . ILE A 1 202 ? 34.73266 -14.19154 25.14808  1.000 68.34357  ? 219 ILE A CG1 1 
ATOM   1213 C CG2 . ILE A 1 202 ? 34.10890 -12.13516 26.48433  1.000 72.24044  ? 219 ILE A CG2 1 
ATOM   1214 C CD1 . ILE A 1 202 ? 33.63387 -14.08462 24.13847  1.000 65.63958  ? 219 ILE A CD1 1 
ATOM   1215 N N   . CYS A 1 203 ? 34.43803 -13.49989 29.73100  1.000 83.85923  ? 220 CYS A N   1 
ATOM   1216 C CA  . CYS A 1 203 ? 34.13322 -12.65942 30.88081  1.000 82.61412  ? 220 CYS A CA  1 
ATOM   1217 C C   . CYS A 1 203 ? 35.16931 -12.82246 31.97812  1.000 89.34192  ? 220 CYS A C   1 
ATOM   1218 O O   . CYS A 1 203 ? 35.56592 -13.94271 32.31791  1.000 92.65013  ? 220 CYS A O   1 
ATOM   1219 C CB  . CYS A 1 203 ? 32.75750 -13.00807 31.44766  1.000 87.69351  ? 220 CYS A CB  1 
ATOM   1220 S SG  . CYS A 1 203 ? 31.36223 -12.47443 30.44839  1.000 84.65340  ? 220 CYS A SG  1 
ATOM   1221 N N   . ARG A 1 204 ? 35.59072 -11.69687 32.54574  1.000 94.28665  ? 221 ARG A N   1 
ATOM   1222 C CA  . ARG A 1 204 ? 36.39737 -11.73706 33.75097  1.000 98.58571  ? 221 ARG A CA  1 
ATOM   1223 C C   . ARG A 1 204 ? 35.47355 -11.91974 34.94981  1.000 98.14077  ? 221 ARG A C   1 
ATOM   1224 O O   . ARG A 1 204 ? 34.28495 -11.59662 34.87529  1.000 96.41461  ? 221 ARG A O   1 
ATOM   1225 C CB  . ARG A 1 204 ? 37.22645 -10.46158 33.88411  1.000 99.05639  ? 221 ARG A CB  1 
ATOM   1226 C CG  . ARG A 1 204 ? 38.17883 -10.21104 32.73277  1.000 93.56383  ? 221 ARG A CG  1 
ATOM   1227 C CD  . ARG A 1 204 ? 39.58896 -10.32001 33.21822  1.000 104.05518 ? 221 ARG A CD  1 
ATOM   1228 N NE  . ARG A 1 204 ? 40.57954 -10.10996 32.16868  1.000 109.38468 ? 221 ARG A NE  1 
ATOM   1229 C CZ  . ARG A 1 204 ? 41.49707 -9.14964  32.19014  1.000 108.77136 ? 221 ARG A CZ  1 
ATOM   1230 N NH1 . ARG A 1 204 ? 41.58677 -8.29920  33.20380  1.000 107.11003 ? 221 ARG A NH1 1 
ATOM   1231 N NH2 . ARG A 1 204 ? 42.35796 -9.05013  31.17927  1.000 105.28281 ? 221 ARG A NH2 1 
ATOM   1232 N N   . PRO A 1 205 ? 35.98949 -12.45897 36.06144  1.000 100.94282 ? 222 PRO A N   1 
ATOM   1233 C CA  . PRO A 1 205 ? 35.09197 -12.84016 37.17062  1.000 102.49851 ? 222 PRO A CA  1 
ATOM   1234 C C   . PRO A 1 205 ? 34.17211 -11.72845 37.65358  1.000 103.37291 ? 222 PRO A C   1 
ATOM   1235 O O   . PRO A 1 205 ? 32.97000 -11.95128 37.85370  1.000 101.95021 ? 222 PRO A O   1 
ATOM   1236 C CB  . PRO A 1 205 ? 36.07703 -13.28764 38.25753  1.000 96.33541  ? 222 PRO A CB  1 
ATOM   1237 C CG  . PRO A 1 205 ? 37.24619 -13.81843 37.49671  1.000 97.71124  ? 222 PRO A CG  1 
ATOM   1238 C CD  . PRO A 1 205 ? 37.36763 -12.93938 36.27613  1.000 100.22471 ? 222 PRO A CD  1 
ATOM   1239 N N   . ASN A 1 206 ? 34.70081 -10.52595 37.82080  1.000 103.42252 ? 223 ASN A N   1 
ATOM   1240 C CA  . ASN A 1 206 ? 33.95696 -9.42193  38.40183  1.000 104.49501 ? 223 ASN A CA  1 
ATOM   1241 C C   . ASN A 1 206 ? 33.48556 -8.38920  37.37295  1.000 105.27578 ? 223 ASN A C   1 
ATOM   1242 O O   . ASN A 1 206 ? 32.97913 -7.33123  37.76353  1.000 104.59483 ? 223 ASN A O   1 
ATOM   1243 C CB  . ASN A 1 206 ? 34.81739 -8.76899  39.48089  1.000 111.01465 ? 223 ASN A CB  1 
ATOM   1244 C CG  . ASN A 1 206 ? 36.27321 -8.66929  39.06304  1.000 114.88273 ? 223 ASN A CG  1 
ATOM   1245 O OD1 . ASN A 1 206 ? 36.57666 -8.65059  37.86734  1.000 115.41905 ? 223 ASN A OD1 1 
ATOM   1246 N ND2 . ASN A 1 206 ? 37.17977 -8.58903  40.03831  1.000 113.69634 ? 223 ASN A ND2 1 
ATOM   1247 N N   . ASP A 1 207 ? 33.62966 -8.66932  36.07574  1.000 103.10442 ? 224 ASP A N   1 
ATOM   1248 C CA  . ASP A 1 207 ? 33.05400 -7.80584  35.04507  1.000 98.79654  ? 224 ASP A CA  1 
ATOM   1249 C C   . ASP A 1 207 ? 31.53696 -7.75008  35.18195  1.000 89.76350  ? 224 ASP A C   1 
ATOM   1250 O O   . ASP A 1 207 ? 30.86567 -8.78597  35.14532  1.000 92.33567  ? 224 ASP A O   1 
ATOM   1251 C CB  . ASP A 1 207 ? 33.43963 -8.31110  33.65515  1.000 94.82959  ? 224 ASP A CB  1 
ATOM   1252 C CG  . ASP A 1 207 ? 34.75422 -7.73143  33.15902  1.000 95.12302  ? 224 ASP A CG  1 
ATOM   1253 O OD1 . ASP A 1 207 ? 35.16118 -6.62979  33.61056  1.000 98.00954  ? 224 ASP A OD1 1 
ATOM   1254 O OD2 . ASP A 1 207 ? 35.38200 -8.39138  32.30665  1.000 96.02920  ? 224 ASP A OD2 1 
ATOM   1255 N N   . GLU A 1 208 ? 30.99067 -6.53857  35.31973  1.000 85.43275  ? 225 GLU A N   1 
ATOM   1256 C CA  . GLU A 1 208 ? 29.58052 -6.39924  35.66187  1.000 83.37736  ? 225 GLU A CA  1 
ATOM   1257 C C   . GLU A 1 208 ? 28.65072 -6.41186  34.46224  1.000 76.41728  ? 225 GLU A C   1 
ATOM   1258 O O   . GLU A 1 208 ? 27.47029 -6.72461  34.62524  1.000 79.32046  ? 225 GLU A O   1 
ATOM   1259 C CB  . GLU A 1 208 ? 29.34324 -5.12140  36.46463  1.000 92.28665  ? 225 GLU A CB  1 
ATOM   1260 C CG  . GLU A 1 208 ? 27.89965 -4.99357  36.93716  1.000 100.15686 ? 225 GLU A CG  1 
ATOM   1261 C CD  . GLU A 1 208 ? 27.68922 -3.96898  38.05438  1.000 124.99192 ? 225 GLU A CD  1 
ATOM   1262 O OE1 . GLU A 1 208 ? 28.67992 -3.41415  38.60221  1.000 125.02298 ? 225 GLU A OE1 1 
ATOM   1263 O OE2 . GLU A 1 208 ? 26.50485 -3.72284  38.38548  1.000 134.52635 ? 225 GLU A OE2 1 
ATOM   1264 N N   . VAL A 1 209 ? 29.14675 -6.09268  33.26622  1.000 78.50145  ? 226 VAL A N   1 
ATOM   1265 C CA  . VAL A 1 209 ? 28.34289 -6.22341  32.05318  1.000 68.13068  ? 226 VAL A CA  1 
ATOM   1266 C C   . VAL A 1 209 ? 27.85211 -7.65394  31.87448  1.000 71.09513  ? 226 VAL A C   1 
ATOM   1267 O O   . VAL A 1 209 ? 26.80968 -7.89163  31.25264  1.000 65.88051  ? 226 VAL A O   1 
ATOM   1268 C CB  . VAL A 1 209 ? 29.16725 -5.76705  30.83507  1.000 64.75860  ? 226 VAL A CB  1 
ATOM   1269 C CG1 . VAL A 1 209 ? 30.21725 -6.81907  30.46986  1.000 67.53282  ? 226 VAL A CG1 1 
ATOM   1270 C CG2 . VAL A 1 209 ? 28.27070 -5.46580  29.65063  1.000 64.11002  ? 226 VAL A CG2 1 
ATOM   1271 N N   . CYS A 1 210 ? 28.58714 -8.62428  32.41791  1.000 74.58865  ? 227 CYS A N   1 
ATOM   1272 C CA  . CYS A 1 210 ? 28.34130 -10.03386 32.17476  1.000 79.48937  ? 227 CYS A CA  1 
ATOM   1273 C C   . CYS A 1 210 ? 27.28130 -10.61925 33.07841  1.000 78.79051  ? 227 CYS A C   1 
ATOM   1274 O O   . CYS A 1 210 ? 26.94534 -11.79390 32.91175  1.000 78.12089  ? 227 CYS A O   1 
ATOM   1275 C CB  . CYS A 1 210 ? 29.62970 -10.83247 32.36356  1.000 85.69092  ? 227 CYS A CB  1 
ATOM   1276 S SG  . CYS A 1 210 ? 30.93083 -10.57146 31.10473  1.000 95.25839  ? 227 CYS A SG  1 
ATOM   1277 N N   . SER A 1 211 ? 26.76468 -9.84428  34.02835  1.000 74.93777  ? 228 SER A N   1 
ATOM   1278 C CA  . SER A 1 211 ? 25.84856 -10.40231 35.01735  1.000 74.60263  ? 228 SER A CA  1 
ATOM   1279 C C   . SER A 1 211 ? 24.56046 -10.98134 34.43189  1.000 72.09131  ? 228 SER A C   1 
ATOM   1280 O O   . SER A 1 211 ? 24.06024 -11.96469 35.00813  1.000 75.69044  ? 228 SER A O   1 
ATOM   1281 C CB  . SER A 1 211 ? 25.52746 -9.34406  36.08756  1.000 71.80764  ? 228 SER A CB  1 
ATOM   1282 O OG  . SER A 1 211 ? 25.19339 -8.09091  35.51156  1.000 73.41545  ? 228 SER A OG  1 
ATOM   1283 N N   . PRO A 1 212 ? 23.96665 -10.45301 33.35846  1.000 69.31113  ? 229 PRO A N   1 
ATOM   1284 C CA  . PRO A 1 212 ? 22.78954 -11.11776 32.79994  1.000 65.88208  ? 229 PRO A CA  1 
ATOM   1285 C C   . PRO A 1 212 ? 23.10134 -12.37094 31.99823  1.000 66.09955  ? 229 PRO A C   1 
ATOM   1286 O O   . PRO A 1 212 ? 22.16351 -13.00846 31.51410  1.000 65.79351  ? 229 PRO A O   1 
ATOM   1287 C CB  . PRO A 1 212 ? 22.16126 -10.02232 31.92821  1.000 61.88392  ? 229 PRO A CB  1 
ATOM   1288 C CG  . PRO A 1 212 ? 23.25374 -9.14397  31.59463  1.000 61.90039  ? 229 PRO A CG  1 
ATOM   1289 C CD  . PRO A 1 212 ? 24.10596 -9.09640  32.79985  1.000 64.42906  ? 229 PRO A CD  1 
ATOM   1290 N N   . LEU A 1 213 ? 24.36444 -12.77725 31.87979  1.000 69.73179  ? 230 LEU A N   1 
ATOM   1291 C CA  . LEU A 1 213 ? 24.72406 -14.02750 31.21571  1.000 68.74186  ? 230 LEU A CA  1 
ATOM   1292 C C   . LEU A 1 213 ? 24.88997 -15.20474 32.16898  1.000 79.75896  ? 230 LEU A C   1 
ATOM   1293 O O   . LEU A 1 213 ? 25.23826 -16.29776 31.71681  1.000 81.33264  ? 230 LEU A O   1 
ATOM   1294 C CB  . LEU A 1 213 ? 26.03282 -13.87261 30.44358  1.000 65.84589  ? 230 LEU A CB  1 
ATOM   1295 C CG  . LEU A 1 213 ? 26.20480 -12.68469 29.51853  1.000 67.90495  ? 230 LEU A CG  1 
ATOM   1296 C CD1 . LEU A 1 213 ? 27.41383 -12.89530 28.64231  1.000 63.94515  ? 230 LEU A CD1 1 
ATOM   1297 C CD2 . LEU A 1 213 ? 24.95373 -12.53140 28.69043  1.000 69.41089  ? 230 LEU A CD2 1 
ATOM   1298 N N   . ARG A 1 214 ? 24.67319 -15.02331 33.47001  1.000 86.46249  ? 231 ARG A N   1 
ATOM   1299 C CA  . ARG A 1 214 ? 25.13201 -16.00896 34.44116  1.000 91.35363  ? 231 ARG A CA  1 
ATOM   1300 C C   . ARG A 1 214 ? 24.13845 -16.03925 35.60057  1.000 102.79849 ? 231 ARG A C   1 
ATOM   1301 O O   . ARG A 1 214 ? 24.36857 -15.53277 36.69017  1.000 110.41498 ? 231 ARG A O   1 
ATOM   1302 C CB  . ARG A 1 214 ? 26.55717 -15.69726 34.91351  1.000 94.17522  ? 231 ARG A CB  1 
ATOM   1303 C CG  . ARG A 1 214 ? 26.77906 -14.26070 35.43437  1.000 88.78274  ? 231 ARG A CG  1 
ATOM   1304 C CD  . ARG A 1 214 ? 28.02133 -14.12848 36.30797  1.000 91.69591  ? 231 ARG A CD  1 
ATOM   1305 N NE  . ARG A 1 214 ? 29.16816 -13.59481 35.57746  1.000 97.06670  ? 231 ARG A NE  1 
ATOM   1306 C CZ  . ARG A 1 214 ? 29.73700 -12.41425 35.81215  1.000 99.74809  ? 231 ARG A CZ  1 
ATOM   1307 N NH1 . ARG A 1 214 ? 29.28037 -11.59413 36.75052  1.000 93.95885  ? 231 ARG A NH1 1 
ATOM   1308 N NH2 . ARG A 1 214 ? 30.79557 -12.04815 35.09088  1.000 96.18658  ? 231 ARG A NH2 1 
ATOM   1309 N N   . ASP A 1 215 ? 22.99411 -16.66142 35.37506  1.000 127.29317 ? 232 ASP A N   1 
ATOM   1310 C CA  . ASP A 1 215 ? 21.95305 -16.66486 36.39387  1.000 128.52970 ? 232 ASP A CA  1 
ATOM   1311 C C   . ASP A 1 215 ? 22.24502 -17.60127 37.57940  1.000 130.29254 ? 232 ASP A C   1 
ATOM   1312 O O   . ASP A 1 215 ? 22.01281 -17.24278 38.74125  1.000 132.65326 ? 232 ASP A O   1 
ATOM   1313 C CB  . ASP A 1 215 ? 20.61853 -17.02027 35.74743  1.000 124.22670 ? 232 ASP A CB  1 
ATOM   1314 C CG  . ASP A 1 215 ? 19.47197 -16.20223 36.30255  1.000 123.07562 ? 232 ASP A CG  1 
ATOM   1315 O OD1 . ASP A 1 215 ? 19.56729 -15.69928 37.45728  1.000 127.09021 ? 232 ASP A OD1 1 
ATOM   1316 O OD2 . ASP A 1 215 ? 18.48336 -16.04334 35.55988  1.000 118.11637 ? 232 ASP A OD2 1 
ATOM   1317 N N   . HIS B 2 6   ? 18.46905 -3.44369  9.91909   1.000 141.25457 ? 52  HIS B N   1 
ATOM   1318 C CA  . HIS B 2 6   ? 19.59031 -3.46648  8.98301   1.000 139.99069 ? 52  HIS B CA  1 
ATOM   1319 C C   . HIS B 2 6   ? 19.69152 -4.85385  8.36093   1.000 142.56469 ? 52  HIS B C   1 
ATOM   1320 O O   . HIS B 2 6   ? 19.40048 -5.84287  9.03043   1.000 141.01448 ? 52  HIS B O   1 
ATOM   1321 C CB  . HIS B 2 6   ? 20.89700 -3.09603  9.67864   1.000 138.18330 ? 52  HIS B CB  1 
ATOM   1322 C CG  . HIS B 2 6   ? 20.92953 -1.68911  10.18609  1.000 137.56260 ? 52  HIS B CG  1 
ATOM   1323 N ND1 . HIS B 2 6   ? 21.49474 -0.65199  9.47456   1.000 135.45946 ? 52  HIS B ND1 1 
ATOM   1324 C CD2 . HIS B 2 6   ? 20.48035 -1.14840  11.34337  1.000 138.36649 ? 52  HIS B CD2 1 
ATOM   1325 C CE1 . HIS B 2 6   ? 21.37698 0.47003   10.16206  1.000 135.18992 ? 52  HIS B CE1 1 
ATOM   1326 N NE2 . HIS B 2 6   ? 20.76920 0.19509   11.30275  1.000 136.98620 ? 52  HIS B NE2 1 
ATOM   1327 N N   . MET B 2 7   ? 20.10399 -4.93133  7.08765   1.000 146.36945 ? 53  MET B N   1 
ATOM   1328 C CA  . MET B 2 7   ? 19.92827 -6.14403  6.27434   1.000 142.75302 ? 53  MET B CA  1 
ATOM   1329 C C   . MET B 2 7   ? 21.13237 -6.33840  5.34109   1.000 148.65586 ? 53  MET B C   1 
ATOM   1330 O O   . MET B 2 7   ? 21.21371 -5.68453  4.29628   1.000 142.44045 ? 53  MET B O   1 
ATOM   1331 C CB  . MET B 2 7   ? 18.61681 -6.05442  5.48228   1.000 143.07338 ? 53  MET B CB  1 
ATOM   1332 C CG  . MET B 2 7   ? 17.32669 -5.72947  6.30105   1.000 140.86796 ? 53  MET B CG  1 
ATOM   1333 S SD  . MET B 2 7   ? 16.82070 -3.97963  6.47707   1.000 147.90450 ? 53  MET B SD  1 
ATOM   1334 C CE  . MET B 2 7   ? 15.88669 -4.01380  8.01951   1.000 140.35730 ? 53  MET B CE  1 
ATOM   1335 N N   . ASP B 2 8   ? 22.04466 -7.26564  5.68613   1.000 160.97363 ? 54  ASP B N   1 
ATOM   1336 C CA  . ASP B 2 8   ? 23.30008 -7.45667  4.95320   1.000 154.62687 ? 54  ASP B CA  1 
ATOM   1337 C C   . ASP B 2 8   ? 23.57618 -8.92935  4.64102   1.000 152.57382 ? 54  ASP B C   1 
ATOM   1338 O O   . ASP B 2 8   ? 23.01828 -9.83323  5.26580   1.000 155.79358 ? 54  ASP B O   1 
ATOM   1339 C CB  . ASP B 2 8   ? 24.49422 -6.89636  5.73791   1.000 147.60785 ? 54  ASP B CB  1 
ATOM   1340 C CG  . ASP B 2 8   ? 25.77777 -6.91178  4.92570   1.000 138.10713 ? 54  ASP B CG  1 
ATOM   1341 O OD1 . ASP B 2 8   ? 25.94386 -6.03477  4.03860   1.000 136.82403 ? 54  ASP B OD1 1 
ATOM   1342 O OD2 . ASP B 2 8   ? 26.59590 -7.83715  5.14112   1.000 131.38572 ? 54  ASP B OD2 1 
ATOM   1343 N N   . LYS B 2 9   ? 24.47760 -9.16490  3.66719   1.000 135.14591 ? 55  LYS B N   1 
ATOM   1344 C CA  . LYS B 2 9   ? 24.96892 -10.50483 3.33400   1.000 131.45025 ? 55  LYS B CA  1 
ATOM   1345 C C   . LYS B 2 9   ? 25.94539 -11.06219 4.37106   1.000 126.49357 ? 55  LYS B C   1 
ATOM   1346 O O   . LYS B 2 9   ? 26.47588 -12.16680 4.16773   1.000 121.95440 ? 55  LYS B O   1 
ATOM   1347 C CB  . LYS B 2 9   ? 25.62243 -10.51038 1.94712   1.000 131.09221 ? 55  LYS B CB  1 
ATOM   1348 C CG  . LYS B 2 9   ? 24.82343 -9.78248  0.87512   1.000 132.47658 ? 55  LYS B CG  1 
ATOM   1349 C CD  . LYS B 2 9   ? 25.62989 -9.57115  -0.39948  1.000 131.46572 ? 55  LYS B CD  1 
ATOM   1350 C CE  . LYS B 2 9   ? 26.65056 -8.45960  -0.23943  1.000 126.66508 ? 55  LYS B CE  1 
ATOM   1351 N NZ  . LYS B 2 9   ? 27.89705 -8.78256  -0.98179  1.000 124.85898 ? 55  LYS B NZ  1 
ATOM   1352 N N   . LEU B 2 10  ? 26.19577 -10.32812 5.46021   1.000 126.01687 ? 56  LEU B N   1 
ATOM   1353 C CA  . LEU B 2 10  ? 26.83810 -10.86372 6.65610   1.000 113.14016 ? 56  LEU B CA  1 
ATOM   1354 C C   . LEU B 2 10  ? 25.83960 -11.47366 7.63293   1.000 108.95755 ? 56  LEU B C   1 
ATOM   1355 O O   . LEU B 2 10  ? 26.24330 -11.89552 8.71990   1.000 97.08998  ? 56  LEU B O   1 
ATOM   1356 C CB  . LEU B 2 10  ? 27.64390 -9.77335  7.37482   1.000 95.87564  ? 56  LEU B CB  1 
ATOM   1357 C CG  . LEU B 2 10  ? 28.80587 -10.24064 8.24934   1.000 93.32873  ? 56  LEU B CG  1 
ATOM   1358 C CD1 . LEU B 2 10  ? 29.45228 -11.44713 7.65130   1.000 92.30555  ? 56  LEU B CD1 1 
ATOM   1359 C CD2 . LEU B 2 10  ? 29.82989 -9.16800  8.43920   1.000 94.90299  ? 56  LEU B CD2 1 
ATOM   1360 N N   . LYS B 2 11  ? 24.54739 -11.52811 7.28083   1.000 113.83199 ? 57  LYS B N   1 
ATOM   1361 C CA  . LYS B 2 11  ? 23.53114 -12.14936 8.12557   1.000 108.34505 ? 57  LYS B CA  1 
ATOM   1362 C C   . LYS B 2 11  ? 23.37173 -13.63510 7.83540   1.000 100.59831 ? 57  LYS B C   1 
ATOM   1363 O O   . LYS B 2 11  ? 22.27706 -14.20175 7.97909   1.000 91.53824  ? 57  LYS B O   1 
ATOM   1364 C CB  . LYS B 2 11  ? 22.20319 -11.42203 7.97859   1.000 98.17192  ? 57  LYS B CB  1 
ATOM   1365 C CG  . LYS B 2 11  ? 22.33739 -9.95943  8.26476   1.000 104.73930 ? 57  LYS B CG  1 
ATOM   1366 C CD  . LYS B 2 11  ? 22.76393 -9.61211  9.66694   1.000 88.32184  ? 57  LYS B CD  1 
ATOM   1367 C CE  . LYS B 2 11  ? 22.70303 -8.09640  9.75002   1.000 92.02694  ? 57  LYS B CE  1 
ATOM   1368 N NZ  . LYS B 2 11  ? 23.02583 -7.50434  11.05457  1.000 78.42642  ? 57  LYS B NZ  1 
ATOM   1369 N N   . ASP B 2 12  ? 24.44716 -14.27055 7.41104   1.000 96.61934  ? 58  ASP B N   1 
ATOM   1370 C CA  . ASP B 2 12  ? 24.58460 -15.70165 7.54195   1.000 94.82860  ? 58  ASP B CA  1 
ATOM   1371 C C   . ASP B 2 12  ? 25.33243 -16.08911 8.82107   1.000 91.73343  ? 58  ASP B C   1 
ATOM   1372 O O   . ASP B 2 12  ? 25.31210 -17.26484 9.20282   1.000 89.20356  ? 58  ASP B O   1 
ATOM   1373 C CB  . ASP B 2 12  ? 25.30930 -16.23405 6.30197   1.000 111.58137 ? 58  ASP B CB  1 
ATOM   1374 C CG  . ASP B 2 12  ? 25.50714 -17.75724 6.31850   1.000 117.66059 ? 58  ASP B CG  1 
ATOM   1375 O OD1 . ASP B 2 12  ? 26.50419 -18.23611 6.91668   1.000 117.73771 ? 58  ASP B OD1 1 
ATOM   1376 O OD2 . ASP B 2 12  ? 24.68891 -18.47538 5.68601   1.000 112.80795 ? 58  ASP B OD2 1 
ATOM   1377 N N   . THR B 2 13  ? 25.96996 -15.11221 9.52149   1.000 90.82003  ? 59  THR B N   1 
ATOM   1378 C CA  . THR B 2 13  ? 27.01112 -15.15870 10.55593  1.000 80.80686  ? 59  THR B CA  1 
ATOM   1379 C C   . THR B 2 13  ? 26.41217 -15.17397 11.96281  1.000 78.45744  ? 59  THR B C   1 
ATOM   1380 O O   . THR B 2 13  ? 25.53934 -14.34054 12.27590  1.000 74.89035  ? 59  THR B O   1 
ATOM   1381 C CB  . THR B 2 13  ? 27.94473 -13.95057 10.43348  1.000 75.34500  ? 59  THR B CB  1 
ATOM   1382 O OG1 . THR B 2 13  ? 28.62824 -14.00218 9.18508   1.000 91.26517  ? 59  THR B OG1 1 
ATOM   1383 C CG2 . THR B 2 13  ? 29.00225 -13.98346 11.51270  1.000 71.30547  ? 59  THR B CG2 1 
ATOM   1384 N N   . PRO B 2 14  ? 26.89497 -16.07693 12.82964  1.000 76.16862  ? 60  PRO B N   1 
ATOM   1385 C CA  . PRO B 2 14  ? 26.44315 -16.10174 14.22826  1.000 69.18524  ? 60  PRO B CA  1 
ATOM   1386 C C   . PRO B 2 14  ? 27.03947 -14.97033 15.05358  1.000 63.30700  ? 60  PRO B C   1 
ATOM   1387 O O   . PRO B 2 14  ? 28.18705 -14.55944 14.87209  1.000 63.91107  ? 60  PRO B O   1 
ATOM   1388 C CB  . PRO B 2 14  ? 26.96300 -17.45153 14.73959  1.000 69.01540  ? 60  PRO B CB  1 
ATOM   1389 C CG  . PRO B 2 14  ? 27.44486 -18.17513 13.53191  1.000 72.83816  ? 60  PRO B CG  1 
ATOM   1390 C CD  . PRO B 2 14  ? 27.87677 -17.13786 12.57964  1.000 71.81051  ? 60  PRO B CD  1 
ATOM   1391 N N   . PHE B 2 15  ? 26.26055 -14.48512 16.00945  1.000 58.63294  ? 61  PHE B N   1 
ATOM   1392 C CA  . PHE B 2 15  ? 26.78181 -13.41275 16.84544  1.000 56.87765  ? 61  PHE B CA  1 
ATOM   1393 C C   . PHE B 2 15  ? 26.23598 -13.52128 18.26350  1.000 53.13940  ? 61  PHE B C   1 
ATOM   1394 O O   . PHE B 2 15  ? 25.28218 -14.25694 18.53899  1.000 53.95668  ? 61  PHE B O   1 
ATOM   1395 C CB  . PHE B 2 15  ? 26.48214 -12.03631 16.23823  1.000 53.01427  ? 61  PHE B CB  1 
ATOM   1396 C CG  . PHE B 2 15  ? 25.03195 -11.72117 16.13625  1.000 47.57679  ? 61  PHE B CG  1 
ATOM   1397 C CD1 . PHE B 2 15  ? 24.33905 -11.24044 17.21119  1.000 48.23211  ? 61  PHE B CD1 1 
ATOM   1398 C CD2 . PHE B 2 15  ? 24.36020 -11.92042 14.96124  1.000 54.86180  ? 61  PHE B CD2 1 
ATOM   1399 C CE1 . PHE B 2 15  ? 23.00665 -10.95669 17.11997  1.000 49.42477  ? 61  PHE B CE1 1 
ATOM   1400 C CE2 . PHE B 2 15  ? 23.02746 -11.64172 14.86567  1.000 54.69185  ? 61  PHE B CE2 1 
ATOM   1401 C CZ  . PHE B 2 15  ? 22.35156 -11.15342 15.94673  1.000 50.27832  ? 61  PHE B CZ  1 
ATOM   1402 N N   . MET B 2 16  ? 26.89508 -12.79670 19.16863  1.000 49.00255  ? 62  MET B N   1 
ATOM   1403 C CA  . MET B 2 16  ? 26.44771 -12.65998 20.55225  1.000 48.48233  ? 62  MET B CA  1 
ATOM   1404 C C   . MET B 2 16  ? 26.89682 -11.27199 21.02107  1.000 50.42887  ? 62  MET B C   1 
ATOM   1405 O O   . MET B 2 16  ? 28.07112 -11.05658 21.32964  1.000 52.44536  ? 62  MET B O   1 
ATOM   1406 C CB  . MET B 2 16  ? 26.99511 -13.77971 21.42352  1.000 48.71999  ? 62  MET B CB  1 
ATOM   1407 C CG  . MET B 2 16  ? 26.62062 -13.61203 22.85724  1.000 53.80595  ? 62  MET B CG  1 
ATOM   1408 S SD  . MET B 2 16  ? 26.85863 -15.02082 23.93693  1.000 61.83466  ? 62  MET B SD  1 
ATOM   1409 C CE  . MET B 2 16  ? 25.20697 -15.20823 24.58487  1.000 58.57485  ? 62  MET B CE  1 
ATOM   1410 N N   . VAL B 2 17  ? 25.95482 -10.33474 21.05626  1.000 46.95133  ? 63  VAL B N   1 
ATOM   1411 C CA  . VAL B 2 17  ? 26.23507 -8.91258  21.20162  1.000 49.75749  ? 63  VAL B CA  1 
ATOM   1412 C C   . VAL B 2 17  ? 25.40706 -8.36199  22.35798  1.000 50.69749  ? 63  VAL B C   1 
ATOM   1413 O O   . VAL B 2 17  ? 24.20256 -8.62241  22.43708  1.000 51.39175  ? 63  VAL B O   1 
ATOM   1414 C CB  . VAL B 2 17  ? 25.91324 -8.15351  19.89672  1.000 44.04398  ? 63  VAL B CB  1 
ATOM   1415 C CG1 . VAL B 2 17  ? 26.10578 -6.66606  20.07258  1.000 47.39050  ? 63  VAL B CG1 1 
ATOM   1416 C CG2 . VAL B 2 17  ? 26.79302 -8.64855  18.80758  1.000 45.88570  ? 63  VAL B CG2 1 
ATOM   1417 N N   . GLN B 2 18  ? 26.03512 -7.59136  23.24297  1.000 47.26793  ? 64  GLN B N   1 
ATOM   1418 C CA  . GLN B 2 18  ? 25.30398 -6.89479  24.28613  1.000 45.83905  ? 64  GLN B CA  1 
ATOM   1419 C C   . GLN B 2 18  ? 25.27561 -5.41146  23.94672  1.000 48.32785  ? 64  GLN B C   1 
ATOM   1420 O O   . GLN B 2 18  ? 26.23140 -4.88598  23.36618  1.000 49.28763  ? 64  GLN B O   1 
ATOM   1421 C CB  . GLN B 2 18  ? 25.94775 -7.11644  25.64755  1.000 49.31030  ? 64  GLN B CB  1 
ATOM   1422 C CG  . GLN B 2 18  ? 25.95859 -8.55955  26.06690  1.000 52.78589  ? 64  GLN B CG  1 
ATOM   1423 C CD  . GLN B 2 18  ? 25.71004 -8.76175  27.54013  1.000 55.67910  ? 64  GLN B CD  1 
ATOM   1424 O OE1 . GLN B 2 18  ? 24.59237 -9.07777  27.94203  1.000 55.78019  ? 64  GLN B OE1 1 
ATOM   1425 N NE2 . GLN B 2 18  ? 26.73893 -8.55067  28.35904  1.000 56.06068  ? 64  GLN B NE2 1 
ATOM   1426 N N   . VAL B 2 19  ? 24.16421 -4.74744  24.27819  1.000 48.53637  ? 65  VAL B N   1 
ATOM   1427 C CA  . VAL B 2 19  ? 23.97449 -3.31808  24.03390  1.000 44.93289  ? 65  VAL B CA  1 
ATOM   1428 C C   . VAL B 2 19  ? 23.46682 -2.66138  25.31383  1.000 46.40838  ? 65  VAL B C   1 
ATOM   1429 O O   . VAL B 2 19  ? 22.47306 -3.10721  25.90125  1.000 47.95506  ? 65  VAL B O   1 
ATOM   1430 C CB  . VAL B 2 19  ? 22.99255 -3.03770  22.87755  1.000 41.37340  ? 65  VAL B CB  1 
ATOM   1431 C CG1 . VAL B 2 19  ? 22.73631 -1.55203  22.77156  1.000 41.05096  ? 65  VAL B CG1 1 
ATOM   1432 C CG2 . VAL B 2 19  ? 23.52167 -3.57518  21.54480  1.000 43.31480  ? 65  VAL B CG2 1 
ATOM   1433 N N   . LYS B 2 20  ? 24.15712 -1.61330  25.74909  1.000 46.60387  ? 66  LYS B N   1 
ATOM   1434 C CA  . LYS B 2 20  ? 23.67637 -0.72607  26.79680  1.000 43.75446  ? 66  LYS B CA  1 
ATOM   1435 C C   . LYS B 2 20  ? 22.78239 0.30699   26.12126  1.000 45.83568  ? 66  LYS B C   1 
ATOM   1436 O O   . LYS B 2 20  ? 23.26798 1.16678   25.37144  1.000 42.10659  ? 66  LYS B O   1 
ATOM   1437 C CB  . LYS B 2 20  ? 24.84936 -0.06550  27.50788  1.000 45.93868  ? 66  LYS B CB  1 
ATOM   1438 C CG  . LYS B 2 20  ? 25.74038 -1.04181  28.20096  1.000 54.40376  ? 66  LYS B CG  1 
ATOM   1439 C CD  . LYS B 2 20  ? 27.02797 -0.41340  28.73617  1.000 61.55689  ? 66  LYS B CD  1 
ATOM   1440 C CE  . LYS B 2 20  ? 27.91720 -1.50312  29.37803  1.000 64.89984  ? 66  LYS B CE  1 
ATOM   1441 N NZ  . LYS B 2 20  ? 29.24400 -0.98556  29.83974  1.000 72.00887  ? 66  LYS B NZ  1 
ATOM   1442 N N   . LEU B 2 21  ? 21.47115 0.21355   26.39013  1.000 46.35773  ? 67  LEU B N   1 
ATOM   1443 C CA  . LEU B 2 21  ? 20.37686 0.95473   25.79220  1.000 43.74474  ? 67  LEU B CA  1 
ATOM   1444 C C   . LEU B 2 21  ? 20.16205 2.28539   26.50151  1.000 48.43348  ? 67  LEU B C   1 
ATOM   1445 O O   . LEU B 2 21  ? 20.52385 2.45545   27.67273  1.000 52.08107  ? 67  LEU B O   1 
ATOM   1446 C CB  . LEU B 2 21  ? 19.10727 0.11634   25.86071  1.000 46.53666  ? 67  LEU B CB  1 
ATOM   1447 C CG  . LEU B 2 21  ? 19.17463 -1.20838  25.10138  1.000 42.57227  ? 67  LEU B CG  1 
ATOM   1448 C CD1 . LEU B 2 21  ? 17.95877 -2.02653  25.38785  1.000 38.53218  ? 67  LEU B CD1 1 
ATOM   1449 C CD2 . LEU B 2 21  ? 19.30005 -0.94759  23.61580  1.000 39.25501  ? 67  LEU B CD2 1 
ATOM   1450 N N   . PRO B 2 22  ? 19.60524 3.26879   25.80934  1.000 48.40100  ? 68  PRO B N   1 
ATOM   1451 C CA  . PRO B 2 22  ? 19.13692 4.47508   26.48034  1.000 49.25559  ? 68  PRO B CA  1 
ATOM   1452 C C   . PRO B 2 22  ? 17.73737 4.21459   27.03342  1.000 51.74604  ? 68  PRO B C   1 
ATOM   1453 O O   . PRO B 2 22  ? 17.22036 3.09205   26.99240  1.000 49.94825  ? 68  PRO B O   1 
ATOM   1454 C CB  . PRO B 2 22  ? 19.13974 5.50617   25.35333  1.000 47.93804  ? 68  PRO B CB  1 
ATOM   1455 C CG  . PRO B 2 22  ? 18.77050 4.71740   24.17600  1.000 44.56831  ? 68  PRO B CG  1 
ATOM   1456 C CD  . PRO B 2 22  ? 19.49498 3.40431   24.34505  1.000 47.64996  ? 68  PRO B CD  1 
ATOM   1457 N N   . ASN B 2 23  ? 17.14196 5.26487   27.59600  1.000 52.71052  ? 69  ASN B N   1 
ATOM   1458 C CA  . ASN B 2 23  ? 15.74911 5.19419   28.00380  1.000 50.87166  ? 69  ASN B CA  1 
ATOM   1459 C C   . ASN B 2 23  ? 14.88587 4.87036   26.79367  1.000 49.99119  ? 69  ASN B C   1 
ATOM   1460 O O   . ASN B 2 23  ? 15.01008 5.52068   25.75606  1.000 51.82109  ? 69  ASN B O   1 
ATOM   1461 C CB  . ASN B 2 23  ? 15.34598 6.51729   28.63326  1.000 52.14623  ? 69  ASN B CB  1 
ATOM   1462 C CG  . ASN B 2 23  ? 13.92229 6.51875   29.11504  1.000 54.80219  ? 69  ASN B CG  1 
ATOM   1463 O OD1 . ASN B 2 23  ? 13.21272 5.52025   29.00225  1.000 54.92105  ? 69  ASN B OD1 1 
ATOM   1464 N ND2 . ASN B 2 23  ? 13.49770 7.63899   29.68915  1.000 59.62342  ? 69  ASN B ND2 1 
ATOM   1465 N N   . TYR B 2 24  ? 14.02645 3.84463   26.91231  1.000 48.93599  ? 70  TYR B N   1 
ATOM   1466 C CA  . TYR B 2 24  ? 13.30472 3.38451   25.72914  1.000 47.23926  ? 70  TYR B CA  1 
ATOM   1467 C C   . TYR B 2 24  ? 12.42167 4.48667   25.16737  1.000 50.52246  ? 70  TYR B C   1 
ATOM   1468 O O   . TYR B 2 24  ? 12.10030 4.47486   23.97281  1.000 49.21735  ? 70  TYR B O   1 
ATOM   1469 C CB  . TYR B 2 24  ? 12.44464 2.15403   26.01712  1.000 45.12584  ? 70  TYR B CB  1 
ATOM   1470 C CG  . TYR B 2 24  ? 11.13875 2.45591   26.70576  1.000 49.74647  ? 70  TYR B CG  1 
ATOM   1471 C CD1 . TYR B 2 24  ? 11.05861 2.52148   28.08751  1.000 54.56623  ? 70  TYR B CD1 1 
ATOM   1472 C CD2 . TYR B 2 24  ? 9.98140  2.71586   25.96726  1.000 48.89728  ? 70  TYR B CD2 1 
ATOM   1473 C CE1 . TYR B 2 24  ? 9.85549  2.81043   28.72533  1.000 57.03837  ? 70  TYR B CE1 1 
ATOM   1474 C CE2 . TYR B 2 24  ? 8.78717  3.03176   26.59021  1.000 50.23014  ? 70  TYR B CE2 1 
ATOM   1475 C CZ  . TYR B 2 24  ? 8.72711  3.07040   27.97231  1.000 55.38167  ? 70  TYR B CZ  1 
ATOM   1476 O OH  . TYR B 2 24  ? 7.54167  3.35898   28.61178  1.000 58.34707  ? 70  TYR B OH  1 
ATOM   1477 N N   . LYS B 2 25  ? 12.01331 5.43861   26.01731  1.000 52.44545  ? 71  LYS B N   1 
ATOM   1478 C CA  . LYS B 2 25  ? 11.22009 6.57086   25.55555  1.000 49.02791  ? 71  LYS B CA  1 
ATOM   1479 C C   . LYS B 2 25  ? 12.02546 7.44119   24.60725  1.000 53.38636  ? 71  LYS B C   1 
ATOM   1480 O O   . LYS B 2 25  ? 11.47382 8.00756   23.65575  1.000 54.31362  ? 71  LYS B O   1 
ATOM   1481 C CB  . LYS B 2 25  ? 10.73821 7.38147   26.74848  1.000 50.57803  ? 71  LYS B CB  1 
ATOM   1482 C CG  . LYS B 2 25  ? 9.80353  6.60543   27.61712  1.000 52.06664  ? 71  LYS B CG  1 
ATOM   1483 C CD  . LYS B 2 25  ? 9.33306  7.40520   28.80303  1.000 58.87630  ? 71  LYS B CD  1 
ATOM   1484 C CE  . LYS B 2 25  ? 8.38363  6.59448   29.65905  1.000 63.71689  ? 71  LYS B CE  1 
ATOM   1485 N NZ  . LYS B 2 25  ? 7.88488  7.37139   30.82674  1.000 76.36620  ? 71  LYS B NZ  1 
ATOM   1486 N N   . ASP B 2 26  ? 13.33851 7.55567   24.85628  1.000 55.96987  ? 72  ASP B N   1 
ATOM   1487 C CA  . ASP B 2 26  ? 14.24007 8.25553   23.94082  1.000 54.47160  ? 72  ASP B CA  1 
ATOM   1488 C C   . ASP B 2 26  ? 14.42818 7.47809   22.64188  1.000 54.73616  ? 72  ASP B C   1 
ATOM   1489 O O   . ASP B 2 26  ? 14.39908 8.06275   21.55499  1.000 56.05270  ? 72  ASP B O   1 
ATOM   1490 C CB  . ASP B 2 26  ? 15.58812 8.48767   24.61481  1.000 55.37537  ? 72  ASP B CB  1 
ATOM   1491 C CG  . ASP B 2 26  ? 15.52667 9.55866   25.68083  1.000 60.94321  ? 72  ASP B CG  1 
ATOM   1492 O OD1 . ASP B 2 26  ? 14.74010 10.52823  25.53059  1.000 64.49757  ? 72  ASP B OD1 1 
ATOM   1493 O OD2 . ASP B 2 26  ? 16.25967 9.42029   26.68532  1.000 64.83412  ? 72  ASP B OD2 1 
ATOM   1494 N N   . TYR B 2 27  ? 14.64771 6.16093   22.73820  1.000 51.43144  ? 73  TYR B N   1 
ATOM   1495 C CA  . TYR B 2 27  ? 14.67931 5.30199   21.55659  1.000 47.77826  ? 73  TYR B CA  1 
ATOM   1496 C C   . TYR B 2 27  ? 13.45008 5.53062   20.69205  1.000 48.28067  ? 73  TYR B C   1 
ATOM   1497 O O   . TYR B 2 27  ? 13.55651 5.80116   19.49599  1.000 49.16002  ? 73  TYR B O   1 
ATOM   1498 C CB  . TYR B 2 27  ? 14.77229 3.81938   21.96548  1.000 47.82954  ? 73  TYR B CB  1 
ATOM   1499 C CG  . TYR B 2 27  ? 14.83058 2.85402   20.78187  1.000 47.66997  ? 73  TYR B CG  1 
ATOM   1500 C CD1 . TYR B 2 27  ? 13.70598 2.61765   19.99140  1.000 47.17620  ? 73  TYR B CD1 1 
ATOM   1501 C CD2 . TYR B 2 27  ? 16.00937 2.18802   20.44842  1.000 45.78375  ? 73  TYR B CD2 1 
ATOM   1502 C CE1 . TYR B 2 27  ? 13.75130 1.76665   18.90866  1.000 46.32482  ? 73  TYR B CE1 1 
ATOM   1503 C CE2 . TYR B 2 27  ? 16.06113 1.31544   19.35986  1.000 45.25090  ? 73  TYR B CE2 1 
ATOM   1504 C CZ  . TYR B 2 27  ? 14.92081 1.11001   18.59296  1.000 47.85405  ? 73  TYR B CZ  1 
ATOM   1505 O OH  . TYR B 2 27  ? 14.93121 0.25820   17.49394  1.000 54.31990  ? 73  TYR B OH  1 
ATOM   1506 N N   . LEU B 2 28  ? 12.26524 5.38419   21.28250  1.000 51.34834  ? 74  LEU B N   1 
ATOM   1507 C CA  . LEU B 2 28  ? 11.03022 5.58811   20.53260  1.000 51.57369  ? 74  LEU B CA  1 
ATOM   1508 C C   . LEU B 2 28  ? 11.01838 6.94178   19.84680  1.000 52.49630  ? 74  LEU B C   1 
ATOM   1509 O O   . LEU B 2 28  ? 10.62458 7.06131   18.68359  1.000 55.58290  ? 74  LEU B O   1 
ATOM   1510 C CB  . LEU B 2 28  ? 9.83369  5.48076   21.46727  1.000 48.21769  ? 74  LEU B CB  1 
ATOM   1511 C CG  . LEU B 2 28  ? 9.44492  4.09717   21.92441  1.000 43.70718  ? 74  LEU B CG  1 
ATOM   1512 C CD1 . LEU B 2 28  ? 8.46030  4.19099   23.04745  1.000 46.22243  ? 74  LEU B CD1 1 
ATOM   1513 C CD2 . LEU B 2 28  ? 8.85782  3.40856   20.76492  1.000 43.71417  ? 74  LEU B CD2 1 
ATOM   1514 N N   . LEU B 2 29  ? 11.48155 7.96686   20.54969  1.000 52.22963  ? 75  LEU B N   1 
ATOM   1515 C CA  . LEU B 2 29  ? 11.34445 9.33255   20.06782  1.000 55.15231  ? 75  LEU B CA  1 
ATOM   1516 C C   . LEU B 2 29  ? 12.24979 9.61243   18.87227  1.000 56.54905  ? 75  LEU B C   1 
ATOM   1517 O O   . LEU B 2 29  ? 11.86076 10.35776  17.96664  1.000 60.69040  ? 75  LEU B O   1 
ATOM   1518 C CB  . LEU B 2 29  ? 11.65169 10.29818  21.20773  1.000 57.22373  ? 75  LEU B CB  1 
ATOM   1519 C CG  . LEU B 2 29  ? 11.70717 11.76463  20.83082  1.000 54.91117  ? 75  LEU B CG  1 
ATOM   1520 C CD1 . LEU B 2 29  ? 10.32419 12.16102  20.45122  1.000 56.56799  ? 75  LEU B CD1 1 
ATOM   1521 C CD2 . LEU B 2 29  ? 12.18431 12.57230  22.00659  1.000 59.28645  ? 75  LEU B CD2 1 
ATOM   1522 N N   . ASP B 2 30  ? 13.46339 9.03099   18.85021  1.000 56.21046  ? 76  ASP B N   1 
ATOM   1523 C CA  . ASP B 2 30  ? 14.49603 9.40724   17.88696  1.000 51.86391  ? 76  ASP B CA  1 
ATOM   1524 C C   . ASP B 2 30  ? 15.07698 8.26871   17.05477  1.000 48.90316  ? 76  ASP B C   1 
ATOM   1525 O O   . ASP B 2 30  ? 16.00243 8.52212   16.27604  1.000 47.05288  ? 76  ASP B O   1 
ATOM   1526 C CB  . ASP B 2 30  ? 15.68176 10.09645  18.58627  1.000 49.85783  ? 76  ASP B CB  1 
ATOM   1527 C CG  . ASP B 2 30  ? 15.31261 11.40972  19.25160  1.000 58.46370  ? 76  ASP B CG  1 
ATOM   1528 O OD1 . ASP B 2 30  ? 14.51402 12.19450  18.66793  1.000 58.44749  ? 76  ASP B OD1 1 
ATOM   1529 O OD2 . ASP B 2 30  ? 15.87543 11.67623  20.35007  1.000 63.56101  ? 76  ASP B OD2 1 
ATOM   1530 N N   . ASN B 2 31  ? 14.59154 7.03266   17.18700  1.000 51.33194  ? 77  ASN B N   1 
ATOM   1531 C CA  . ASN B 2 31  ? 15.25468 5.93779   16.47528  1.000 49.58243  ? 77  ASN B CA  1 
ATOM   1532 C C   . ASN B 2 31  ? 15.11290 6.08054   14.96607  1.000 49.48158  ? 77  ASN B C   1 
ATOM   1533 O O   . ASN B 2 31  ? 16.08610 5.86062   14.23299  1.000 49.11636  ? 77  ASN B O   1 
ATOM   1534 C CB  . ASN B 2 31  ? 14.73280 4.57584   16.93587  1.000 47.84814  ? 77  ASN B CB  1 
ATOM   1535 C CG  . ASN B 2 31  ? 13.43902 4.19481   16.26867  1.000 49.05961  ? 77  ASN B CG  1 
ATOM   1536 O OD1 . ASN B 2 31  ? 13.41855 3.42977   15.30770  1.000 52.61659  ? 77  ASN B OD1 1 
ATOM   1537 N ND2 . ASN B 2 31  ? 12.34033 4.72099   16.78619  1.000 50.76208  ? 77  ASN B ND2 1 
ATOM   1538 N N   . LYS B 2 32  ? 13.92522 6.47678   14.48102  1.000 52.39716  ? 78  LYS B N   1 
ATOM   1539 C CA  . LYS B 2 32  ? 13.72585 6.56820   13.03732  1.000 46.68316  ? 78  LYS B CA  1 
ATOM   1540 C C   . LYS B 2 32  ? 14.67338 7.58382   12.42359  1.000 45.50916  ? 78  LYS B C   1 
ATOM   1541 O O   . LYS B 2 32  ? 15.28894 7.31653   11.38638  1.000 45.05544  ? 78  LYS B O   1 
ATOM   1542 C CB  . LYS B 2 32  ? 12.27860 6.91341   12.70739  1.000 49.77720  ? 78  LYS B CB  1 
ATOM   1543 C CG  . LYS B 2 32  ? 11.24903 5.79247   12.95241  1.000 54.55369  ? 78  LYS B CG  1 
ATOM   1544 C CD  . LYS B 2 32  ? 9.83684  6.41261   12.89771  1.000 64.86698  ? 78  LYS B CD  1 
ATOM   1545 C CE  . LYS B 2 32  ? 8.75792  5.58831   13.59538  1.000 73.91454  ? 78  LYS B CE  1 
ATOM   1546 N NZ  . LYS B 2 32  ? 8.30495  4.39345   12.82484  1.000 88.83669  ? 78  LYS B NZ  1 
ATOM   1547 N N   . GLN B 2 33  ? 14.84668 8.73575   13.07694  1.000 48.27872  ? 79  GLN B N   1 
ATOM   1548 C CA  . GLN B 2 33  ? 15.70698 9.76759   12.50903  1.000 45.51525  ? 79  GLN B CA  1 
ATOM   1549 C C   . GLN B 2 33  ? 17.17550 9.41567   12.64928  1.000 46.65300  ? 79  GLN B C   1 
ATOM   1550 O O   . GLN B 2 33  ? 17.96371 9.74271   11.75073  1.000 48.24257  ? 79  GLN B O   1 
ATOM   1551 C CB  . GLN B 2 33  ? 15.43221 11.11320  13.15726  1.000 47.26921  ? 79  GLN B CB  1 
ATOM   1552 C CG  . GLN B 2 33  ? 16.37449 12.20984  12.72652  1.000 46.94859  ? 79  GLN B CG  1 
ATOM   1553 C CD  . GLN B 2 33  ? 15.87927 13.60201  13.12990  1.000 53.00401  ? 79  GLN B CD  1 
ATOM   1554 O OE1 . GLN B 2 33  ? 15.56072 13.85623  14.29878  1.000 50.73543  ? 79  GLN B OE1 1 
ATOM   1555 N NE2 . GLN B 2 33  ? 15.84084 14.51686  12.16689  1.000 59.86538  ? 79  GLN B NE2 1 
ATOM   1556 N N   . VAL B 2 34  ? 17.56645 8.75974   13.75608  1.000 47.86218  ? 80  VAL B N   1 
ATOM   1557 C CA  . VAL B 2 34  ? 18.95307 8.28980   13.89739  1.000 49.55517  ? 80  VAL B CA  1 
ATOM   1558 C C   . VAL B 2 34  ? 19.30568 7.31153   12.77510  1.000 48.56141  ? 80  VAL B C   1 
ATOM   1559 O O   . VAL B 2 34  ? 20.40294 7.37499   12.19372  1.000 47.14183  ? 80  VAL B O   1 
ATOM   1560 C CB  . VAL B 2 34  ? 19.19379 7.67786   15.29845  1.000 45.42913  ? 80  VAL B CB  1 
ATOM   1561 C CG1 . VAL B 2 34  ? 20.30308 6.64993   15.27598  1.000 45.63396  ? 80  VAL B CG1 1 
ATOM   1562 C CG2 . VAL B 2 34  ? 19.55863 8.75920   16.28584  1.000 43.14974  ? 80  VAL B CG2 1 
ATOM   1563 N N   . VAL B 2 35  ? 18.36457 6.43548   12.41208  1.000 46.04204  ? 81  VAL B N   1 
ATOM   1564 C CA  . VAL B 2 35  ? 18.63492 5.45683   11.36433  1.000 49.61927  ? 81  VAL B CA  1 
ATOM   1565 C C   . VAL B 2 35  ? 18.84683 6.13536   10.01000  1.000 48.21840  ? 81  VAL B C   1 
ATOM   1566 O O   . VAL B 2 35  ? 19.80619 5.81355   9.30134   1.000 47.19666  ? 81  VAL B O   1 
ATOM   1567 C CB  . VAL B 2 35  ? 17.52250 4.40308   11.30995  1.000 48.66748  ? 81  VAL B CB  1 
ATOM   1568 C CG1 . VAL B 2 35  ? 17.62729 3.63427   10.02934  1.000 51.43019  ? 81  VAL B CG1 1 
ATOM   1569 C CG2 . VAL B 2 35  ? 17.66053 3.48889   12.49009  1.000 51.68709  ? 81  VAL B CG2 1 
ATOM   1570 N N   . LEU B 2 36  ? 17.96008 7.06651   9.61875   1.000 47.41752  ? 82  LEU B N   1 
ATOM   1571 C CA  . LEU B 2 36  ? 18.22652 7.89264   8.43387   1.000 46.53966  ? 82  LEU B CA  1 
ATOM   1572 C C   . LEU B 2 36  ? 19.64428 8.43148   8.39632   1.000 48.37075  ? 82  LEU B C   1 
ATOM   1573 O O   . LEU B 2 36  ? 20.38858 8.19104   7.43651   1.000 46.28122  ? 82  LEU B O   1 
ATOM   1574 C CB  . LEU B 2 36  ? 17.29332 9.08776   8.33408   1.000 44.50805  ? 82  LEU B CB  1 
ATOM   1575 C CG  . LEU B 2 36  ? 16.34092 9.04709   7.17387   1.000 44.75066  ? 82  LEU B CG  1 
ATOM   1576 C CD1 . LEU B 2 36  ? 15.57818 10.35616  7.13446   1.000 47.21515  ? 82  LEU B CD1 1 
ATOM   1577 C CD2 . LEU B 2 36  ? 17.20158 8.91566   5.95903   1.000 43.31462  ? 82  LEU B CD2 1 
ATOM   1578 N N   . THR B 2 37  ? 19.98936 9.24939   9.39817   1.000 48.10938  ? 83  THR B N   1 
ATOM   1579 C CA  . THR B 2 37  ? 21.31318 9.85135   9.46530   1.000 45.06698  ? 83  THR B CA  1 
ATOM   1580 C C   . THR B 2 37  ? 22.40199 8.82266   9.20138   1.000 47.42169  ? 83  THR B C   1 
ATOM   1581 O O   . THR B 2 37  ? 23.26453 9.02414   8.33675   1.000 48.91579  ? 83  THR B O   1 
ATOM   1582 C CB  . THR B 2 37  ? 21.51234 10.49949  10.82333  1.000 41.80104  ? 83  THR B CB  1 
ATOM   1583 O OG1 . THR B 2 37  ? 20.29565 11.14905  11.20118  1.000 43.64999  ? 83  THR B OG1 1 
ATOM   1584 C CG2 . THR B 2 37  ? 22.64046 11.52749  10.73760  1.000 39.83531  ? 83  THR B CG2 1 
ATOM   1585 N N   . PHE B 2 38  ? 22.36825 7.69626   9.91917   1.000 46.69334  ? 84  PHE B N   1 
ATOM   1586 C CA  . PHE B 2 38  ? 23.43087 6.71767   9.73461   1.000 48.24953  ? 84  PHE B CA  1 
ATOM   1587 C C   . PHE B 2 38  ? 23.36559 6.09776   8.34079   1.000 49.92666  ? 84  PHE B C   1 
ATOM   1588 O O   . PHE B 2 38  ? 24.37315 6.04491   7.62859   1.000 50.68546  ? 84  PHE B O   1 
ATOM   1589 C CB  . PHE B 2 38  ? 23.37191 5.64246   10.81455  1.000 47.95982  ? 84  PHE B CB  1 
ATOM   1590 C CG  . PHE B 2 38  ? 24.43474 4.62241   10.65550  1.000 48.88897  ? 84  PHE B CG  1 
ATOM   1591 C CD1 . PHE B 2 38  ? 25.73915 4.93102   10.95913  1.000 54.71997  ? 84  PHE B CD1 1 
ATOM   1592 C CD2 . PHE B 2 38  ? 24.15002 3.37991   10.14127  1.000 51.21969  ? 84  PHE B CD2 1 
ATOM   1593 C CE1 . PHE B 2 38  ? 26.73377 3.99581   10.77805  1.000 56.99972  ? 84  PHE B CE1 1 
ATOM   1594 C CE2 . PHE B 2 38  ? 25.13523 2.44870   9.96100   1.000 52.13412  ? 84  PHE B CE2 1 
ATOM   1595 C CZ  . PHE B 2 38  ? 26.42152 2.75219   10.27243  1.000 51.51953  ? 84  PHE B CZ  1 
ATOM   1596 N N   . LYS B 2 39  ? 22.17725 5.63420   7.93709   1.000 50.80544  ? 85  LYS B N   1 
ATOM   1597 C CA  . LYS B 2 39  ? 21.95003 5.11347   6.58874   1.000 47.18255  ? 85  LYS B CA  1 
ATOM   1598 C C   . LYS B 2 39  ? 22.49895 6.05446   5.52228   1.000 51.39367  ? 85  LYS B C   1 
ATOM   1599 O O   . LYS B 2 39  ? 23.13444 5.61788   4.55658   1.000 53.54948  ? 85  LYS B O   1 
ATOM   1600 C CB  . LYS B 2 39  ? 20.44223 4.89231   6.39255   1.000 50.42289  ? 85  LYS B CB  1 
ATOM   1601 C CG  . LYS B 2 39  ? 20.02418 3.88654   5.33444   1.000 59.04166  ? 85  LYS B CG  1 
ATOM   1602 C CD  . LYS B 2 39  ? 18.49124 3.78630   5.16842   1.000 63.16777  ? 85  LYS B CD  1 
ATOM   1603 C CE  . LYS B 2 39  ? 17.76103 3.37887   6.46257   1.000 59.96542  ? 85  LYS B CE  1 
ATOM   1604 N NZ  . LYS B 2 39  ? 16.28968 3.07561   6.28286   1.000 63.95864  ? 85  LYS B NZ  1 
ATOM   1605 N N   . LEU B 2 40  ? 22.27890 7.35657   5.68916   1.000 50.70747  ? 86  LEU B N   1 
ATOM   1606 C CA  . LEU B 2 40  ? 22.67705 8.30757   4.66475   1.000 47.64937  ? 86  LEU B CA  1 
ATOM   1607 C C   . LEU B 2 40  ? 24.17000 8.59410   4.66835   1.000 48.51306  ? 86  LEU B C   1 
ATOM   1608 O O   . LEU B 2 40  ? 24.72945 8.84986   3.60199   1.000 49.74633  ? 86  LEU B O   1 
ATOM   1609 C CB  . LEU B 2 40  ? 21.90527 9.60818   4.83460   1.000 49.00340  ? 86  LEU B CB  1 
ATOM   1610 C CG  . LEU B 2 40  ? 20.47641 9.55757   4.30936   1.000 45.07685  ? 86  LEU B CG  1 
ATOM   1611 C CD1 . LEU B 2 40  ? 19.83472 10.91418  4.46256   1.000 43.43902  ? 86  LEU B CD1 1 
ATOM   1612 C CD2 . LEU B 2 40  ? 20.51542 9.14229   2.86318   1.000 46.96838  ? 86  LEU B CD2 1 
ATOM   1613 N N   . VAL B 2 41  ? 24.83409 8.58962   5.82996   1.000 48.61215  ? 87  VAL B N   1 
ATOM   1614 C CA  . VAL B 2 41  ? 26.25914 8.91442   5.79992   1.000 49.26348  ? 87  VAL B CA  1 
ATOM   1615 C C   . VAL B 2 41  ? 27.06453 7.66820   5.49420   1.000 54.63341  ? 87  VAL B C   1 
ATOM   1616 O O   . VAL B 2 41  ? 28.13744 7.75445   4.88412   1.000 57.73931  ? 87  VAL B O   1 
ATOM   1617 C CB  . VAL B 2 41  ? 26.74938 9.58011   7.10241   1.000 43.02259  ? 87  VAL B CB  1 
ATOM   1618 C CG1 . VAL B 2 41  ? 25.85773 10.72764  7.48819   1.000 45.85568  ? 87  VAL B CG1 1 
ATOM   1619 C CG2 . VAL B 2 41  ? 26.82764 8.61273   8.20109   1.000 51.92037  ? 87  VAL B CG2 1 
ATOM   1620 N N   . HIS B 2 42  ? 26.55296 6.49507   5.88072   1.000 55.64541  ? 88  HIS B N   1 
ATOM   1621 C CA  . HIS B 2 42  ? 27.29342 5.25311   5.69238   1.000 55.22798  ? 88  HIS B CA  1 
ATOM   1622 C C   . HIS B 2 42  ? 27.50007 4.97121   4.21619   1.000 60.68327  ? 88  HIS B C   1 
ATOM   1623 O O   . HIS B 2 42  ? 28.60589 4.62212   3.78531   1.000 65.23983  ? 88  HIS B O   1 
ATOM   1624 C CB  . HIS B 2 42  ? 26.54706 4.10446   6.35517   1.000 53.25243  ? 88  HIS B CB  1 
ATOM   1625 C CG  . HIS B 2 42  ? 27.40159 2.91656   6.63807   1.000 57.66938  ? 88  HIS B CG  1 
ATOM   1626 N ND1 . HIS B 2 42  ? 28.62684 3.01367   7.26334   1.000 63.64187  ? 88  HIS B ND1 1 
ATOM   1627 C CD2 . HIS B 2 42  ? 27.20161 1.60100   6.40596   1.000 57.73392  ? 88  HIS B CD2 1 
ATOM   1628 C CE1 . HIS B 2 42  ? 29.14522 1.80731   7.40075   1.000 60.00679  ? 88  HIS B CE1 1 
ATOM   1629 N NE2 . HIS B 2 42  ? 28.30346 0.93222   6.88109   1.000 55.20375  ? 88  HIS B NE2 1 
ATOM   1630 N N   . HIS B 2 43  ? 26.44816 5.16895   3.41991   1.000 59.31822  ? 89  HIS B N   1 
ATOM   1631 C CA  . HIS B 2 43  ? 26.43426 4.80280   2.01532   1.000 60.97099  ? 89  HIS B CA  1 
ATOM   1632 C C   . HIS B 2 43  ? 26.73609 5.95525   1.07728   1.000 62.09676  ? 89  HIS B C   1 
ATOM   1633 O O   . HIS B 2 43  ? 27.10514 5.71651   -0.07848  1.000 69.83979  ? 89  HIS B O   1 
ATOM   1634 C CB  . HIS B 2 43  ? 25.07865 4.20002   1.67671   1.000 63.16993  ? 89  HIS B CB  1 
ATOM   1635 C CG  . HIS B 2 43  ? 24.77031 2.98292   2.48681   1.000 70.63801  ? 89  HIS B CG  1 
ATOM   1636 N ND1 . HIS B 2 43  ? 23.88367 2.99013   3.53961   1.000 68.11310  ? 89  HIS B ND1 1 
ATOM   1637 C CD2 . HIS B 2 43  ? 25.24814 1.72011   2.40875   1.000 75.03393  ? 89  HIS B CD2 1 
ATOM   1638 C CE1 . HIS B 2 43  ? 23.82205 1.78333   4.06995   1.000 70.04699  ? 89  HIS B CE1 1 
ATOM   1639 N NE2 . HIS B 2 43  ? 24.63968 0.99367   3.40043   1.000 73.24579  ? 89  HIS B NE2 1 
ATOM   1640 N N   . SER B 2 44  ? 26.64368 7.18368   1.55025   1.000 61.05587  ? 90  SER B N   1 
ATOM   1641 C CA  . SER B 2 44  ? 26.74015 8.30854   0.64900   1.000 61.67850  ? 90  SER B CA  1 
ATOM   1642 C C   . SER B 2 44  ? 28.17691 8.58332   0.21246   1.000 63.14200  ? 90  SER B C   1 
ATOM   1643 O O   . SER B 2 44  ? 29.13590 8.33194   0.94358   1.000 67.47528  ? 90  SER B O   1 
ATOM   1644 C CB  . SER B 2 44  ? 26.17225 9.53485   1.31563   1.000 59.35872  ? 90  SER B CB  1 
ATOM   1645 O OG  . SER B 2 44  ? 26.12736 10.57020  0.37132   1.000 69.46627  ? 90  SER B OG  1 
ATOM   1646 N N   . LYS B 2 45  ? 28.30956 9.13244   -0.99357  1.000 58.75379  ? 91  LYS B N   1 
ATOM   1647 C CA  . LYS B 2 45  ? 29.58170 9.59188   -1.53890  1.000 59.12375  ? 91  LYS B CA  1 
ATOM   1648 C C   . LYS B 2 45  ? 29.77389 11.09793  -1.43773  1.000 62.97782  ? 91  LYS B C   1 
ATOM   1649 O O   . LYS B 2 45  ? 30.91914 11.55575  -1.41183  1.000 68.16049  ? 91  LYS B O   1 
ATOM   1650 C CB  . LYS B 2 45  ? 29.70905 9.17082   -3.01018  1.000 67.88668  ? 91  LYS B CB  1 
ATOM   1651 C CG  . LYS B 2 45  ? 29.73478 7.66048   -3.18795  1.000 74.69785  ? 91  LYS B CG  1 
ATOM   1652 C CD  . LYS B 2 45  ? 29.64245 7.19629   -4.63291  1.000 74.45953  ? 91  LYS B CD  1 
ATOM   1653 C CE  . LYS B 2 45  ? 29.86001 5.68775   -4.69101  1.000 84.07007  ? 91  LYS B CE  1 
ATOM   1654 N NZ  . LYS B 2 45  ? 28.80841 4.91194   -3.94315  1.000 90.71504  ? 91  LYS B NZ  1 
ATOM   1655 N N   . LYS B 2 46  ? 28.69371 11.88138  -1.40128  1.000 56.43674  ? 92  LYS B N   1 
ATOM   1656 C CA  . LYS B 2 46  ? 28.76319 13.31664  -1.16954  1.000 53.00804  ? 92  LYS B CA  1 
ATOM   1657 C C   . LYS B 2 46  ? 27.82197 13.64104  -0.02996  1.000 55.41663  ? 92  LYS B C   1 
ATOM   1658 O O   . LYS B 2 46  ? 26.63581 13.30210  -0.10663  1.000 55.11609  ? 92  LYS B O   1 
ATOM   1659 C CB  . LYS B 2 46  ? 28.33420 14.13274  -2.39400  1.000 55.60565  ? 92  LYS B CB  1 
ATOM   1660 C CG  . LYS B 2 46  ? 29.12236 13.87917  -3.64429  1.000 65.93008  ? 92  LYS B CG  1 
ATOM   1661 C CD  . LYS B 2 46  ? 29.27314 15.13569  -4.48481  1.000 70.40862  ? 92  LYS B CD  1 
ATOM   1662 C CE  . LYS B 2 46  ? 30.47509 15.02799  -5.45347  1.000 79.31233  ? 92  LYS B CE  1 
ATOM   1663 N NZ  . LYS B 2 46  ? 31.52160 14.01211  -5.06269  1.000 69.39063  ? 92  LYS B NZ  1 
ATOM   1664 N N   . ILE B 2 47  ? 28.33746 14.31338  1.00618   1.000 54.53814  ? 93  ILE B N   1 
ATOM   1665 C CA  . ILE B 2 47  ? 27.53283 14.89303  2.08120   1.000 49.95178  ? 93  ILE B CA  1 
ATOM   1666 C C   . ILE B 2 47  ? 27.71214 16.40947  2.05293   1.000 50.07849  ? 93  ILE B C   1 
ATOM   1667 O O   . ILE B 2 47  ? 28.82492 16.91071  1.87620   1.000 52.47855  ? 93  ILE B O   1 
ATOM   1668 C CB  . ILE B 2 47  ? 27.93843 14.33473  3.46043   1.000 51.21440  ? 93  ILE B CB  1 
ATOM   1669 C CG1 . ILE B 2 47  ? 27.80939 12.81230  3.48377   1.000 48.85289  ? 93  ILE B CG1 1 
ATOM   1670 C CG2 . ILE B 2 47  ? 27.15670 15.01165  4.58792   1.000 46.24359  ? 93  ILE B CG2 1 
ATOM   1671 C CD1 . ILE B 2 47  ? 26.49936 12.35167  3.84425   1.000 49.34168  ? 93  ILE B CD1 1 
ATOM   1672 N N   . THR B 2 48  ? 26.61990 17.14225  2.21544   1.000 50.78888  ? 94  THR B N   1 
ATOM   1673 C CA  . THR B 2 48  ? 26.65351 18.59220  2.35146   1.000 49.48380  ? 94  THR B CA  1 
ATOM   1674 C C   . THR B 2 48  ? 25.98059 18.94881  3.66096   1.000 46.12328  ? 94  THR B C   1 
ATOM   1675 O O   . THR B 2 48  ? 24.90483 18.43100  3.95943   1.000 45.46485  ? 94  THR B O   1 
ATOM   1676 C CB  . THR B 2 48  ? 25.93319 19.27809  1.19268   1.000 52.07124  ? 94  THR B CB  1 
ATOM   1677 O OG1 . THR B 2 48  ? 26.42157 18.73036  -0.03345  1.000 59.51510  ? 94  THR B OG1 1 
ATOM   1678 C CG2 . THR B 2 48  ? 26.15674 20.79484  1.20712   1.000 47.87670  ? 94  THR B CG2 1 
ATOM   1679 N N   . LEU B 2 49  ? 26.61008 19.82022  4.43827   1.000 46.78554  ? 95  LEU B N   1 
ATOM   1680 C CA  . LEU B 2 49  ? 26.09744 20.20368  5.74143   1.000 46.70143  ? 95  LEU B CA  1 
ATOM   1681 C C   . LEU B 2 49  ? 25.86700 21.70273  5.74301   1.000 50.23716  ? 95  LEU B C   1 
ATOM   1682 O O   . LEU B 2 49  ? 26.77652 22.46530  5.41163   1.000 54.11504  ? 95  LEU B O   1 
ATOM   1683 C CB  . LEU B 2 49  ? 27.06590 19.80472  6.84882   1.000 45.38334  ? 95  LEU B CB  1 
ATOM   1684 C CG  . LEU B 2 49  ? 27.04229 18.30261  7.06885   1.000 41.47542  ? 95  LEU B CG  1 
ATOM   1685 C CD1 . LEU B 2 49  ? 28.32705 17.82588  7.70973   1.000 43.32110  ? 95  LEU B CD1 1 
ATOM   1686 C CD2 . LEU B 2 49  ? 25.82320 17.92524  7.85657   1.000 44.48827  ? 95  LEU B CD2 1 
ATOM   1687 N N   . ILE B 2 50  ? 24.65613 22.12485  6.10608   1.000 52.26846  ? 96  ILE B N   1 
ATOM   1688 C CA  . ILE B 2 50  ? 24.27679 23.54073  6.10551   1.000 57.55595  ? 96  ILE B CA  1 
ATOM   1689 C C   . ILE B 2 50  ? 23.76940 23.91517  7.48509   1.000 54.75183  ? 96  ILE B C   1 
ATOM   1690 O O   . ILE B 2 50  ? 22.73442 23.40605  7.93490   1.000 56.47419  ? 96  ILE B O   1 
ATOM   1691 C CB  . ILE B 2 50  ? 23.20826 23.85815  5.05379   1.000 52.14430  ? 96  ILE B CB  1 
ATOM   1692 C CG1 . ILE B 2 50  ? 23.45826 23.04624  3.78923   1.000 46.50405  ? 96  ILE B CG1 1 
ATOM   1693 C CG2 . ILE B 2 50  ? 23.19295 25.32765  4.79766   1.000 53.75453  ? 96  ILE B CG2 1 
ATOM   1694 C CD1 . ILE B 2 50  ? 22.43461 23.23426  2.80447   1.000 41.19463  ? 96  ILE B CD1 1 
ATOM   1695 N N   . GLY B 2 51  ? 24.47481 24.81595  8.14569   1.000 54.76007  ? 97  GLY B N   1 
ATOM   1696 C CA  . GLY B 2 51  ? 24.05647 25.20410  9.46851   1.000 60.80679  ? 97  GLY B CA  1 
ATOM   1697 C C   . GLY B 2 51  ? 25.14653 25.99556  10.14374  1.000 60.29976  ? 97  GLY B C   1 
ATOM   1698 O O   . GLY B 2 51  ? 26.14729 26.35374  9.52948   1.000 56.59098  ? 97  GLY B O   1 
ATOM   1699 N N   . ASP B 2 52  ? 24.91041 26.26167  11.42379  1.000 63.29381  ? 98  ASP B N   1 
ATOM   1700 C CA  . ASP B 2 52  ? 25.81671 27.07088  12.21243  1.000 62.55207  ? 98  ASP B CA  1 
ATOM   1701 C C   . ASP B 2 52  ? 27.23779 26.58736  11.99322  1.000 59.46799  ? 98  ASP B C   1 
ATOM   1702 O O   . ASP B 2 52  ? 27.49057 25.38466  11.96365  1.000 57.04413  ? 98  ASP B O   1 
ATOM   1703 C CB  . ASP B 2 52  ? 25.43509 26.98055  13.68663  1.000 70.01739  ? 98  ASP B CB  1 
ATOM   1704 C CG  . ASP B 2 52  ? 26.32024 27.83529  14.57511  1.000 82.67405  ? 98  ASP B CG  1 
ATOM   1705 O OD1 . ASP B 2 52  ? 26.51986 29.03162  14.24168  1.000 89.50399  ? 98  ASP B OD1 1 
ATOM   1706 O OD2 . ASP B 2 52  ? 26.81955 27.31430  15.60089  1.000 78.76133  ? 98  ASP B OD2 1 
ATOM   1707 N N   . ALA B 2 53  ? 28.15282 27.54009  11.77714  1.000 67.80682  ? 99  ALA B N   1 
ATOM   1708 C CA  . ALA B 2 53  ? 29.53643 27.21000  11.44047  1.000 61.69230  ? 99  ALA B CA  1 
ATOM   1709 C C   . ALA B 2 53  ? 30.11776 26.19840  12.40599  1.000 62.67769  ? 99  ALA B C   1 
ATOM   1710 O O   . ALA B 2 53  ? 30.89993 25.32825  12.01936  1.000 59.04918  ? 99  ALA B O   1 
ATOM   1711 C CB  . ALA B 2 53  ? 30.38130 28.47464  11.44416  1.000 64.00514  ? 99  ALA B CB  1 
ATOM   1712 N N   . ASN B 2 54  ? 29.72792 26.28646  13.67065  1.000 75.98734  ? 100 ASN B N   1 
ATOM   1713 C CA  . ASN B 2 54  ? 30.21389 25.33886  14.66005  1.000 75.02542  ? 100 ASN B CA  1 
ATOM   1714 C C   . ASN B 2 54  ? 29.63532 23.94427  14.43416  1.000 72.42124  ? 100 ASN B C   1 
ATOM   1715 O O   . ASN B 2 54  ? 30.37954 22.98270  14.21529  1.000 71.27959  ? 100 ASN B O   1 
ATOM   1716 C CB  . ASN B 2 54  ? 29.87061 25.84087  16.05283  1.000 78.38427  ? 100 ASN B CB  1 
ATOM   1717 C CG  . ASN B 2 54  ? 30.75094 25.23778  17.08855  1.000 85.22544  ? 100 ASN B CG  1 
ATOM   1718 O OD1 . ASN B 2 54  ? 31.34801 24.18750  16.85810  1.000 82.64872  ? 100 ASN B OD1 1 
ATOM   1719 N ND2 . ASN B 2 54  ? 30.84681 25.88462  18.24383  1.000 97.91836  ? 100 ASN B ND2 1 
ATOM   1720 N N   . LYS B 2 55  ? 28.30024 23.82201  14.48084  1.000 68.63244  ? 101 LYS B N   1 
ATOM   1721 C CA  . LYS B 2 55  ? 27.64824 22.51323  14.49368  1.000 58.72393  ? 101 LYS B CA  1 
ATOM   1722 C C   . LYS B 2 55  ? 28.03206 21.67320  13.28903  1.000 55.82223  ? 101 LYS B C   1 
ATOM   1723 O O   . LYS B 2 55  ? 28.21614 20.46282  13.41384  1.000 55.44060  ? 101 LYS B O   1 
ATOM   1724 C CB  . LYS B 2 55  ? 26.13293 22.68233  14.56272  1.000 55.52807  ? 101 LYS B CB  1 
ATOM   1725 C CG  . LYS B 2 55  ? 25.68277 23.70691  15.59045  1.000 59.42493  ? 101 LYS B CG  1 
ATOM   1726 C CD  . LYS B 2 55  ? 24.21860 24.01787  15.47731  1.000 61.97978  ? 101 LYS B CD  1 
ATOM   1727 C CE  . LYS B 2 55  ? 23.53106 23.94097  16.81743  1.000 65.58130  ? 101 LYS B CE  1 
ATOM   1728 N NZ  . LYS B 2 55  ? 22.12697 24.41964  16.69881  1.000 73.55060  ? 101 LYS B NZ  1 
ATOM   1729 N N   . ILE B 2 56  ? 28.19056 22.29352  12.11736  1.000 55.14162  ? 102 ILE B N   1 
ATOM   1730 C CA  . ILE B 2 56  ? 28.50753 21.50493  10.92949  1.000 51.99117  ? 102 ILE B CA  1 
ATOM   1731 C C   . ILE B 2 56  ? 29.94677 21.01251  10.95455  1.000 53.46998  ? 102 ILE B C   1 
ATOM   1732 O O   . ILE B 2 56  ? 30.24637 19.93059  10.43703  1.000 53.09799  ? 102 ILE B O   1 
ATOM   1733 C CB  . ILE B 2 56  ? 28.21073 22.29539  9.64307   1.000 51.07460  ? 102 ILE B CB  1 
ATOM   1734 C CG1 . ILE B 2 56  ? 29.12938 23.50941  9.50517   1.000 48.44010  ? 102 ILE B CG1 1 
ATOM   1735 C CG2 . ILE B 2 56  ? 26.74097 22.67266  9.59261   1.000 53.93889  ? 102 ILE B CG2 1 
ATOM   1736 C CD1 . ILE B 2 56  ? 28.93019 24.25268  8.21775   1.000 48.27753  ? 102 ILE B CD1 1 
ATOM   1737 N N   . LEU B 2 57  ? 30.86503 21.77196  11.54309  1.000 54.64662  ? 103 LEU B N   1 
ATOM   1738 C CA  . LEU B 2 57  ? 32.22116 21.25218  11.67109  1.000 52.06484  ? 103 LEU B CA  1 
ATOM   1739 C C   . LEU B 2 57  ? 32.27655 20.05280  12.61715  1.000 53.79225  ? 103 LEU B C   1 
ATOM   1740 O O   . LEU B 2 57  ? 33.03225 19.10817  12.37315  1.000 53.63363  ? 103 LEU B O   1 
ATOM   1741 C CB  . LEU B 2 57  ? 33.15566 22.35287  12.14223  1.000 52.61124  ? 103 LEU B CB  1 
ATOM   1742 C CG  . LEU B 2 57  ? 33.72647 23.25144  11.06153  1.000 46.87049  ? 103 LEU B CG  1 
ATOM   1743 C CD1 . LEU B 2 57  ? 34.25726 24.51040  11.67747  1.000 52.41249  ? 103 LEU B CD1 1 
ATOM   1744 C CD2 . LEU B 2 57  ? 34.80676 22.51377  10.37142  1.000 52.50793  ? 103 LEU B CD2 1 
ATOM   1745 N N   . GLN B 2 58  ? 31.48526 20.06580  13.70098  1.000 53.09050  ? 104 GLN B N   1 
ATOM   1746 C CA  . GLN B 2 58  ? 31.46461 18.92366  14.61434  1.000 52.43382  ? 104 GLN B CA  1 
ATOM   1747 C C   . GLN B 2 58  ? 30.93427 17.67685  13.92768  1.000 53.76190  ? 104 GLN B C   1 
ATOM   1748 O O   . GLN B 2 58  ? 31.42347 16.56766  14.17245  1.000 56.14517  ? 104 GLN B O   1 
ATOM   1749 C CB  . GLN B 2 58  ? 30.56386 19.16770  15.81567  1.000 55.03773  ? 104 GLN B CB  1 
ATOM   1750 C CG  . GLN B 2 58  ? 30.61435 20.45370  16.53056  1.000 58.57192  ? 104 GLN B CG  1 
ATOM   1751 C CD  . GLN B 2 58  ? 29.74973 20.35929  17.77972  1.000 62.60940  ? 104 GLN B CD  1 
ATOM   1752 O OE1 . GLN B 2 58  ? 28.51121 20.36869  17.70958  1.000 64.74543  ? 104 GLN B OE1 1 
ATOM   1753 N NE2 . GLN B 2 58  ? 30.39999 20.28165  18.93432  1.000 64.35892  ? 104 GLN B NE2 1 
ATOM   1754 N N   . TYR B 2 59  ? 29.85867 17.83203  13.15126  1.000 51.42365  ? 105 TYR B N   1 
ATOM   1755 C CA  . TYR B 2 59  ? 29.26510 16.70333  12.45527  1.000 48.04488  ? 105 TYR B CA  1 
ATOM   1756 C C   . TYR B 2 59  ? 30.20481 16.17667  11.38749  1.000 52.10091  ? 105 TYR B C   1 
ATOM   1757 O O   . TYR B 2 59  ? 30.38855 14.96206  11.26185  1.000 55.44135  ? 105 TYR B O   1 
ATOM   1758 C CB  . TYR B 2 59  ? 27.93356 17.11483  11.83755  1.000 47.60231  ? 105 TYR B CB  1 
ATOM   1759 C CG  . TYR B 2 59  ? 26.73393 16.67260  12.63468  1.000 48.91776  ? 105 TYR B CG  1 
ATOM   1760 C CD1 . TYR B 2 59  ? 26.48854 15.32754  12.86840  1.000 50.20462  ? 105 TYR B CD1 1 
ATOM   1761 C CD2 . TYR B 2 59  ? 25.84511 17.59415  13.15979  1.000 48.09852  ? 105 TYR B CD2 1 
ATOM   1762 C CE1 . TYR B 2 59  ? 25.38464 14.91580  13.59580  1.000 46.52051  ? 105 TYR B CE1 1 
ATOM   1763 C CE2 . TYR B 2 59  ? 24.75417 17.18829  13.90213  1.000 48.82394  ? 105 TYR B CE2 1 
ATOM   1764 C CZ  . TYR B 2 59  ? 24.52690 15.85047  14.10936  1.000 44.75910  ? 105 TYR B CZ  1 
ATOM   1765 O OH  . TYR B 2 59  ? 23.43499 15.44922  14.82696  1.000 46.28134  ? 105 TYR B OH  1 
ATOM   1766 N N   . LYS B 2 60  ? 30.81761 17.07160  10.61089  1.000 51.73729  ? 106 LYS B N   1 
ATOM   1767 C CA  . LYS B 2 60  ? 31.76828 16.60586  9.61782   1.000 48.98275  ? 106 LYS B CA  1 
ATOM   1768 C C   . LYS B 2 60  ? 32.85369 15.77381  10.26538  1.000 53.49080  ? 106 LYS B C   1 
ATOM   1769 O O   . LYS B 2 60  ? 33.33717 14.81832  9.65859   1.000 60.30836  ? 106 LYS B O   1 
ATOM   1770 C CB  . LYS B 2 60  ? 32.38867 17.77186  8.84261   1.000 51.42156  ? 106 LYS B CB  1 
ATOM   1771 C CG  . LYS B 2 60  ? 33.61127 17.33286  8.01284   1.000 53.90547  ? 106 LYS B CG  1 
ATOM   1772 C CD  . LYS B 2 60  ? 34.04964 18.30917  6.94104   1.000 51.39916  ? 106 LYS B CD  1 
ATOM   1773 C CE  . LYS B 2 60  ? 35.56787 18.39346  6.91423   1.000 54.36404  ? 106 LYS B CE  1 
ATOM   1774 N NZ  . LYS B 2 60  ? 36.19705 17.94811  5.62942   1.000 58.06237  ? 106 LYS B NZ  1 
ATOM   1775 N N   . ASN B 2 61  ? 33.23089 16.07954  11.50147  1.000 57.71045  ? 107 ASN B N   1 
ATOM   1776 C CA  . ASN B 2 61  ? 34.32028 15.30471  12.07600  1.000 60.57748  ? 107 ASN B CA  1 
ATOM   1777 C C   . ASN B 2 61  ? 33.83898 13.99507  12.65923  1.000 60.98474  ? 107 ASN B C   1 
ATOM   1778 O O   . ASN B 2 61  ? 34.49181 12.96097  12.47333  1.000 62.86118  ? 107 ASN B O   1 
ATOM   1779 C CB  . ASN B 2 61  ? 35.05643 16.11963  13.11044  1.000 60.89190  ? 107 ASN B CB  1 
ATOM   1780 C CG  . ASN B 2 61  ? 35.96752 17.10816  12.46560  1.000 71.37837  ? 107 ASN B CG  1 
ATOM   1781 O OD1 . ASN B 2 61  ? 35.82084 18.30801  12.66168  1.000 77.26449  ? 107 ASN B OD1 1 
ATOM   1782 N ND2 . ASN B 2 61  ? 36.91112 16.61506  11.64767  1.000 76.92410  ? 107 ASN B ND2 1 
ATOM   1783 N N   . TYR B 2 62  ? 32.70853 14.01288  13.36184  1.000 57.21412  ? 108 TYR B N   1 
ATOM   1784 C CA  . TYR B 2 62  ? 32.13332 12.75739  13.81005  1.000 53.45279  ? 108 TYR B CA  1 
ATOM   1785 C C   . TYR B 2 62  ? 31.90348 11.84516  12.61864  1.000 55.47753  ? 108 TYR B C   1 
ATOM   1786 O O   . TYR B 2 62  ? 32.29305 10.67035  12.63130  1.000 60.26610  ? 108 TYR B O   1 
ATOM   1787 C CB  . TYR B 2 62  ? 30.82917 12.99757  14.57080  1.000 53.99955  ? 108 TYR B CB  1 
ATOM   1788 C CG  . TYR B 2 62  ? 30.23714 11.71573  15.10196  1.000 56.32157  ? 108 TYR B CG  1 
ATOM   1789 C CD1 . TYR B 2 62  ? 30.95049 10.93617  15.99233  1.000 53.85210  ? 108 TYR B CD1 1 
ATOM   1790 C CD2 . TYR B 2 62  ? 28.99123 11.24781  14.66809  1.000 59.46101  ? 108 TYR B CD2 1 
ATOM   1791 C CE1 . TYR B 2 62  ? 30.44236 9.74319   16.47153  1.000 57.17252  ? 108 TYR B CE1 1 
ATOM   1792 C CE2 . TYR B 2 62  ? 28.46122 10.04182  15.15375  1.000 55.61924  ? 108 TYR B CE2 1 
ATOM   1793 C CZ  . TYR B 2 62  ? 29.20098 9.29870   16.06163  1.000 57.92614  ? 108 TYR B CZ  1 
ATOM   1794 O OH  . TYR B 2 62  ? 28.73184 8.09263   16.56159  1.000 64.27452  ? 108 TYR B OH  1 
ATOM   1795 N N   . PHE B 2 63  ? 31.31638 12.38842  11.55318  1.000 54.77574  ? 109 PHE B N   1 
ATOM   1796 C CA  . PHE B 2 63  ? 30.99147 11.56113  10.39987  1.000 55.35498  ? 109 PHE B CA  1 
ATOM   1797 C C   . PHE B 2 63  ? 32.24233 10.97036  9.75973   1.000 59.48998  ? 109 PHE B C   1 
ATOM   1798 O O   . PHE B 2 63  ? 32.18378 9.88164   9.18769   1.000 66.36679  ? 109 PHE B O   1 
ATOM   1799 C CB  . PHE B 2 63  ? 30.18850 12.37489  9.39049   1.000 46.89158  ? 109 PHE B CB  1 
ATOM   1800 C CG  . PHE B 2 63  ? 28.75588 12.55772  9.77099   1.000 48.38228  ? 109 PHE B CG  1 
ATOM   1801 C CD1 . PHE B 2 63  ? 28.16801 11.73906  10.72292  1.000 51.51067  ? 109 PHE B CD1 1 
ATOM   1802 C CD2 . PHE B 2 63  ? 27.99373 13.57885  9.20612   1.000 49.42903  ? 109 PHE B CD2 1 
ATOM   1803 C CE1 . PHE B 2 63  ? 26.82939 11.90866  11.09348  1.000 47.73362  ? 109 PHE B CE1 1 
ATOM   1804 C CE2 . PHE B 2 63  ? 26.65172 13.75926  9.56795   1.000 46.61451  ? 109 PHE B CE2 1 
ATOM   1805 C CZ  . PHE B 2 63  ? 26.06965 12.91729  10.51455  1.000 45.91150  ? 109 PHE B CZ  1 
ATOM   1806 N N   . GLN B 2 64  ? 33.38480 11.63779  9.87381   1.000 57.79784  ? 110 GLN B N   1 
ATOM   1807 C CA  . GLN B 2 64  ? 34.57288 11.16666  9.17939   1.000 63.23075  ? 110 GLN B CA  1 
ATOM   1808 C C   . GLN B 2 64  ? 35.29164 10.02941  9.90392   1.000 76.94395  ? 110 GLN B C   1 
ATOM   1809 O O   . GLN B 2 64  ? 36.15383 9.38570   9.29626   1.000 81.40718  ? 110 GLN B O   1 
ATOM   1810 C CB  . GLN B 2 64  ? 35.52160 12.33294  8.94782   1.000 62.34486  ? 110 GLN B CB  1 
ATOM   1811 C CG  . GLN B 2 64  ? 35.29426 12.98847  7.61517   1.000 63.05263  ? 110 GLN B CG  1 
ATOM   1812 C CD  . GLN B 2 64  ? 36.11050 14.24511  7.43336   1.000 63.61870  ? 110 GLN B CD  1 
ATOM   1813 O OE1 . GLN B 2 64  ? 36.41082 14.95781  8.40319   1.000 63.20506  ? 110 GLN B OE1 1 
ATOM   1814 N NE2 . GLN B 2 64  ? 36.49870 14.51952  6.18231   1.000 61.58853  ? 110 GLN B NE2 1 
ATOM   1815 N N   . ALA B 2 65  ? 34.98922 9.79732   11.18889  1.000 79.29776  ? 111 ALA B N   1 
ATOM   1816 C CA  . ALA B 2 65  ? 35.23002 8.50996   11.85566  1.000 80.30583  ? 111 ALA B CA  1 
ATOM   1817 C C   . ALA B 2 65  ? 36.70969 8.17361   11.97487  1.000 88.67411  ? 111 ALA B C   1 
ATOM   1818 O O   . ALA B 2 65  ? 37.09055 7.00623   11.89408  1.000 90.90766  ? 111 ALA B O   1 
ATOM   1819 C CB  . ALA B 2 65  ? 34.49130 7.36980   11.14123  1.000 73.07479  ? 111 ALA B CB  1 
ATOM   1820 N N   . ASN B 2 66  ? 37.54667 9.19078   12.19978  1.000 93.05343  ? 112 ASN B N   1 
ATOM   1821 C CA  . ASN B 2 66  ? 39.00913 9.03186   12.14993  1.000 97.58951  ? 112 ASN B CA  1 
ATOM   1822 C C   . ASN B 2 66  ? 39.46371 8.50477   10.79353  1.000 100.03616 ? 112 ASN B C   1 
ATOM   1823 O O   . ASN B 2 66  ? 40.39577 7.70361   10.69879  1.000 102.64360 ? 112 ASN B O   1 
ATOM   1824 C CB  . ASN B 2 66  ? 39.54352 8.11574   13.25573  1.000 98.99403  ? 112 ASN B CB  1 
ATOM   1825 C CG  . ASN B 2 66  ? 38.85243 8.31864   14.56253  1.000 103.97114 ? 112 ASN B CG  1 
ATOM   1826 O OD1 . ASN B 2 66  ? 39.21207 9.21147   15.32630  1.000 107.62935 ? 112 ASN B OD1 1 
ATOM   1827 N ND2 . ASN B 2 66  ? 37.84896 7.49422   14.83972  1.000 105.55536 ? 112 ASN B ND2 1 
ATOM   1828 N N   . GLY B 2 67  ? 38.79923 8.94188   9.73356   1.000 92.38994  ? 113 GLY B N   1 
ATOM   1829 C CA  . GLY B 2 67  ? 39.19488 8.49929   8.41885   1.000 91.02344  ? 113 GLY B CA  1 
ATOM   1830 C C   . GLY B 2 67  ? 38.60807 7.18375   7.96367   1.000 90.88065  ? 113 GLY B C   1 
ATOM   1831 O O   . GLY B 2 67  ? 39.01449 6.68376   6.91081   1.000 96.25889  ? 113 GLY B O   1 
ATOM   1832 N N   . ALA B 2 68  ? 37.66966 6.59606   8.70890   1.000 88.82714  ? 114 ALA B N   1 
ATOM   1833 C CA  . ALA B 2 68  ? 36.93374 5.47122   8.14364   1.000 88.67227  ? 114 ALA B CA  1 
ATOM   1834 C C   . ALA B 2 68  ? 35.99154 5.90827   7.03394   1.000 86.76043  ? 114 ALA B C   1 
ATOM   1835 O O   . ALA B 2 68  ? 35.46430 5.04812   6.32455   1.000 90.95593  ? 114 ALA B O   1 
ATOM   1836 C CB  . ALA B 2 68  ? 36.14522 4.72543   9.22512   1.000 91.96127  ? 114 ALA B CB  1 
ATOM   1837 N N   . ARG B 2 69  ? 35.76498 7.21219   6.88010   1.000 80.80636  ? 115 ARG B N   1 
ATOM   1838 C CA  . ARG B 2 69  ? 34.99483 7.80988   5.79725   1.000 76.93969  ? 115 ARG B CA  1 
ATOM   1839 C C   . ARG B 2 69  ? 35.77565 8.95281   5.15867   1.000 81.22495  ? 115 ARG B C   1 
ATOM   1840 O O   . ARG B 2 69  ? 35.21569 9.98010   4.75950   1.000 77.87286  ? 115 ARG B O   1 
ATOM   1841 C CB  . ARG B 2 69  ? 33.64013 8.29285   6.29621   1.000 70.00711  ? 115 ARG B CB  1 
ATOM   1842 C CG  . ARG B 2 69  ? 32.89995 7.24556   7.07558   1.000 72.02369  ? 115 ARG B CG  1 
ATOM   1843 C CD  . ARG B 2 69  ? 31.49330 7.05675   6.55694   1.000 70.91694  ? 115 ARG B CD  1 
ATOM   1844 N NE  . ARG B 2 69  ? 30.76728 6.04459   7.31352   1.000 66.69885  ? 115 ARG B NE  1 
ATOM   1845 C CZ  . ARG B 2 69  ? 30.38568 6.18481   8.57612   1.000 63.80754  ? 115 ARG B CZ  1 
ATOM   1846 N NH1 . ARG B 2 69  ? 30.66760 7.27766   9.26986   1.000 64.01913  ? 115 ARG B NH1 1 
ATOM   1847 N NH2 . ARG B 2 69  ? 29.70437 5.20256   9.15920   1.000 62.96205  ? 115 ARG B NH2 1 
ATOM   1848 N N   . SER B 2 70  ? 37.09422 8.79089   5.04942   1.000 85.20541  ? 116 SER B N   1 
ATOM   1849 C CA  . SER B 2 70  ? 37.91746 9.79453   4.39345   1.000 79.24237  ? 116 SER B CA  1 
ATOM   1850 C C   . SER B 2 70  ? 37.66992 9.85494   2.90020   1.000 80.39573  ? 116 SER B C   1 
ATOM   1851 O O   . SER B 2 70  ? 38.21851 10.73966  2.23580   1.000 87.11477  ? 116 SER B O   1 
ATOM   1852 C CB  . SER B 2 70  ? 39.38724 9.51447   4.66541   1.000 84.59089  ? 116 SER B CB  1 
ATOM   1853 O OG  . SER B 2 70  ? 39.67256 8.13771   4.50272   1.000 93.14390  ? 116 SER B OG  1 
ATOM   1854 N N   . ASP B 2 71  ? 36.85591 8.94285   2.37102   1.000 83.85450  ? 117 ASP B N   1 
ATOM   1855 C CA  . ASP B 2 71  ? 36.43433 8.92621   0.97585   1.000 85.52884  ? 117 ASP B CA  1 
ATOM   1856 C C   . ASP B 2 71  ? 35.14731 9.70564   0.70766   1.000 82.41553  ? 117 ASP B C   1 
ATOM   1857 O O   . ASP B 2 71  ? 34.79915 9.90541   -0.46165  1.000 79.72688  ? 117 ASP B O   1 
ATOM   1858 C CB  . ASP B 2 71  ? 36.25273 7.47812   0.49921   1.000 90.89980  ? 117 ASP B CB  1 
ATOM   1859 C CG  . ASP B 2 71  ? 35.22971 6.69223   1.32635   1.000 88.09179  ? 117 ASP B CG  1 
ATOM   1860 O OD1 . ASP B 2 71  ? 34.71118 7.20767   2.33979   1.000 83.56820  ? 117 ASP B OD1 1 
ATOM   1861 O OD2 . ASP B 2 71  ? 34.94103 5.53687   0.94702   1.000 92.88555  ? 117 ASP B OD2 1 
ATOM   1862 N N   . ILE B 2 72  ? 34.42142 10.12529  1.74634   1.000 78.38556  ? 118 ILE B N   1 
ATOM   1863 C CA  . ILE B 2 72  ? 33.26464 10.98381  1.54498   1.000 69.20550  ? 118 ILE B CA  1 
ATOM   1864 C C   . ILE B 2 72  ? 33.75869 12.36413  1.15156   1.000 73.13252  ? 118 ILE B C   1 
ATOM   1865 O O   . ILE B 2 72  ? 34.78310 12.84023  1.66363   1.000 78.11961  ? 118 ILE B O   1 
ATOM   1866 C CB  . ILE B 2 72  ? 32.39863 11.03823  2.81599   1.000 65.56392  ? 118 ILE B CB  1 
ATOM   1867 C CG1 . ILE B 2 72  ? 31.80036 9.67631   3.11519   1.000 66.20491  ? 118 ILE B CG1 1 
ATOM   1868 C CG2 . ILE B 2 72  ? 31.26594 12.02085  2.67131   1.000 61.20325  ? 118 ILE B CG2 1 
ATOM   1869 C CD1 . ILE B 2 72  ? 30.68388 9.73866   4.08001   1.000 61.53647  ? 118 ILE B CD1 1 
ATOM   1870 N N   . ASP B 2 73  ? 33.05272 13.00277  0.21162   1.000 68.50953  ? 119 ASP B N   1 
ATOM   1871 C CA  . ASP B 2 73  ? 33.30841 14.38856  -0.16777  1.000 66.78024  ? 119 ASP B CA  1 
ATOM   1872 C C   . ASP B 2 73  ? 32.37181 15.28628  0.62199   1.000 64.05854  ? 119 ASP B C   1 
ATOM   1873 O O   . ASP B 2 73  ? 31.17251 15.32822  0.33858   1.000 63.57701  ? 119 ASP B O   1 
ATOM   1874 C CB  . ASP B 2 73  ? 33.11266 14.59391  -1.66348  1.000 67.85620  ? 119 ASP B CB  1 
ATOM   1875 C CG  . ASP B 2 73  ? 34.35148 14.26699  -2.45019  1.000 77.53941  ? 119 ASP B CG  1 
ATOM   1876 O OD1 . ASP B 2 73  ? 35.46200 14.30832  -1.86220  1.000 83.09404  ? 119 ASP B OD1 1 
ATOM   1877 O OD2 . ASP B 2 73  ? 34.21606 13.96113  -3.65157  1.000 81.04291  ? 119 ASP B OD2 1 
ATOM   1878 N N   . PHE B 2 74  ? 32.91928 16.00386  1.60477   1.000 57.91141  ? 120 PHE B N   1 
ATOM   1879 C CA  . PHE B 2 74  ? 32.13400 16.88476  2.45528   1.000 53.71706  ? 120 PHE B CA  1 
ATOM   1880 C C   . PHE B 2 74  ? 32.14217 18.30626  1.93039   1.000 57.02778  ? 120 PHE B C   1 
ATOM   1881 O O   . PHE B 2 74  ? 33.15649 18.80168  1.44082   1.000 67.39954  ? 120 PHE B O   1 
ATOM   1882 C CB  . PHE B 2 74  ? 32.66187 16.89019  3.87915   1.000 52.21729  ? 120 PHE B CB  1 
ATOM   1883 C CG  . PHE B 2 74  ? 32.19909 15.73583  4.68453   1.000 55.09312  ? 120 PHE B CG  1 
ATOM   1884 C CD1 . PHE B 2 74  ? 32.92774 14.55295  4.70404   1.000 59.47253  ? 120 PHE B CD1 1 
ATOM   1885 C CD2 . PHE B 2 74  ? 31.03207 15.81545  5.41391   1.000 50.95213  ? 120 PHE B CD2 1 
ATOM   1886 C CE1 . PHE B 2 74  ? 32.51146 13.47333  5.45735   1.000 58.62650  ? 120 PHE B CE1 1 
ATOM   1887 C CE2 . PHE B 2 74  ? 30.60313 14.74164  6.16976   1.000 53.25135  ? 120 PHE B CE2 1 
ATOM   1888 C CZ  . PHE B 2 74  ? 31.34691 13.56054  6.18893   1.000 54.65619  ? 120 PHE B CZ  1 
ATOM   1889 N N   . TYR B 2 75  ? 31.00827 18.97286  2.05970   1.000 55.83547  ? 121 TYR B N   1 
ATOM   1890 C CA  . TYR B 2 75  ? 30.87736 20.35455  1.62422   1.000 53.75864  ? 121 TYR B CA  1 
ATOM   1891 C C   . TYR B 2 75  ? 30.12093 21.11108  2.70588   1.000 54.12239  ? 121 TYR B C   1 
ATOM   1892 O O   . TYR B 2 75  ? 28.93384 20.85264  2.91562   1.000 54.03378  ? 121 TYR B O   1 
ATOM   1893 C CB  . TYR B 2 75  ? 30.15737 20.42242  0.28441   1.000 55.47009  ? 121 TYR B CB  1 
ATOM   1894 C CG  . TYR B 2 75  ? 30.83409 19.66700  -0.85817  1.000 64.91738  ? 121 TYR B CG  1 
ATOM   1895 C CD1 . TYR B 2 75  ? 32.04425 20.11660  -1.40404  1.000 75.14466  ? 121 TYR B CD1 1 
ATOM   1896 C CD2 . TYR B 2 75  ? 30.24240 18.54317  -1.43237  1.000 61.72935  ? 121 TYR B CD2 1 
ATOM   1897 C CE1 . TYR B 2 75  ? 32.65016 19.45164  -2.47583  1.000 75.23174  ? 121 TYR B CE1 1 
ATOM   1898 C CE2 . TYR B 2 75  ? 30.84166 17.87378  -2.50168  1.000 61.96575  ? 121 TYR B CE2 1 
ATOM   1899 C CZ  . TYR B 2 75  ? 32.03802 18.33461  -3.02184  1.000 69.56747  ? 121 TYR B CZ  1 
ATOM   1900 O OH  . TYR B 2 75  ? 32.63042 17.67281  -4.07836  1.000 74.23923  ? 121 TYR B OH  1 
ATOM   1901 N N   . LEU B 2 76  ? 30.80453 22.02714  3.39643   1.000 57.44977  ? 122 LEU B N   1 
ATOM   1902 C CA  . LEU B 2 76  ? 30.23158 22.79872  4.49048   1.000 52.06263  ? 122 LEU B CA  1 
ATOM   1903 C C   . LEU B 2 76  ? 29.75755 24.15788  4.00637   1.000 57.00275  ? 122 LEU B C   1 
ATOM   1904 O O   . LEU B 2 76  ? 30.37685 24.76871  3.13726   1.000 63.97507  ? 122 LEU B O   1 
ATOM   1905 C CB  . LEU B 2 76  ? 31.24183 23.00229  5.60662   1.000 48.59329  ? 122 LEU B CB  1 
ATOM   1906 C CG  . LEU B 2 76  ? 31.89278 21.75527  6.17843   1.000 47.94674  ? 122 LEU B CG  1 
ATOM   1907 C CD1 . LEU B 2 76  ? 32.67863 22.17102  7.38889   1.000 48.17375  ? 122 LEU B CD1 1 
ATOM   1908 C CD2 . LEU B 2 76  ? 30.87898 20.66472  6.50952   1.000 46.81705  ? 122 LEU B CD2 1 
ATOM   1909 N N   . GLN B 2 77  ? 28.64379 24.61822  4.56364   1.000 69.55793  ? 123 GLN B N   1 
ATOM   1910 C CA  . GLN B 2 77  ? 28.08971 25.93912  4.26664   1.000 72.89353  ? 123 GLN B CA  1 
ATOM   1911 C C   . GLN B 2 77  ? 27.66288 26.58994  5.56343   1.000 73.42379  ? 123 GLN B C   1 
ATOM   1912 O O   . GLN B 2 77  ? 26.55924 26.32073  6.06771   1.000 72.97151  ? 123 GLN B O   1 
ATOM   1913 C CB  . GLN B 2 77  ? 26.92543 25.84537  3.29869   1.000 72.88083  ? 123 GLN B CB  1 
ATOM   1914 C CG  . GLN B 2 77  ? 27.18023 24.75086  2.32013   1.000 78.55027  ? 123 GLN B CG  1 
ATOM   1915 C CD  . GLN B 2 77  ? 26.22281 24.76336  1.16603   1.000 87.92997  ? 123 GLN B CD  1 
ATOM   1916 O OE1 . GLN B 2 77  ? 25.07823 25.23724  1.30741   1.000 82.58330  ? 123 GLN B OE1 1 
ATOM   1917 N NE2 . GLN B 2 77  ? 26.66758 24.24079  -0.00293  1.000 82.55932  ? 123 GLN B NE2 1 
ATOM   1918 N N   . PRO B 2 78  ? 28.51528 27.43482  6.13956   1.000 64.41211  ? 124 PRO B N   1 
ATOM   1919 C CA  . PRO B 2 78  ? 28.17250 28.13207  7.36963   1.000 62.46628  ? 124 PRO B CA  1 
ATOM   1920 C C   . PRO B 2 78  ? 26.95863 29.01086  7.16752   1.000 66.09254  ? 124 PRO B C   1 
ATOM   1921 O O   . PRO B 2 78  ? 26.82733 29.67706  6.14088   1.000 71.00046  ? 124 PRO B O   1 
ATOM   1922 C CB  . PRO B 2 78  ? 29.40914 28.98669  7.61773   1.000 63.85298  ? 124 PRO B CB  1 
ATOM   1923 C CG  . PRO B 2 78  ? 30.47574 28.25349  7.01838   1.000 62.77875  ? 124 PRO B CG  1 
ATOM   1924 C CD  . PRO B 2 78  ? 29.91654 27.68127  5.77346   1.000 61.96170  ? 124 PRO B CD  1 
ATOM   1925 N N   . THR B 2 79  ? 26.07876 29.03304  8.16131   1.000 62.61586  ? 125 THR B N   1 
ATOM   1926 C CA  . THR B 2 79  ? 25.01216 30.02233  8.18844   1.000 68.29475  ? 125 THR B CA  1 
ATOM   1927 C C   . THR B 2 79  ? 25.01230 30.77534  9.51306   1.000 74.17101  ? 125 THR B C   1 
ATOM   1928 O O   . THR B 2 79  ? 25.84013 30.54609  10.40660  1.000 72.99668  ? 125 THR B O   1 
ATOM   1929 C CB  . THR B 2 79  ? 23.63353 29.39984  7.95235   1.000 66.73823  ? 125 THR B CB  1 
ATOM   1930 O OG1 . THR B 2 79  ? 23.21465 28.69300  9.13504   1.000 72.08475  ? 125 THR B OG1 1 
ATOM   1931 C CG2 . THR B 2 79  ? 23.60851 28.54062  6.70620   1.000 61.31092  ? 125 THR B CG2 1 
ATOM   1932 N N   . LEU B 2 80  ? 24.06038 31.69584  9.61301   1.000 79.09254  ? 126 LEU B N   1 
ATOM   1933 C CA  . LEU B 2 80  ? 23.80658 32.40193  10.84978  1.000 84.39886  ? 126 LEU B CA  1 
ATOM   1934 C C   . LEU B 2 80  ? 22.37967 32.13251  11.30555  1.000 91.11122  ? 126 LEU B C   1 
ATOM   1935 O O   . LEU B 2 80  ? 22.13887 31.16345  12.02924  1.000 98.10541  ? 126 LEU B O   1 
ATOM   1936 C CB  . LEU B 2 80  ? 24.09870 33.88084  10.64940  1.000 78.94991  ? 126 LEU B CB  1 
ATOM   1937 C CG  . LEU B 2 80  ? 25.36390 34.34099  11.34339  1.000 75.85414  ? 126 LEU B CG  1 
ATOM   1938 C CD1 . LEU B 2 80  ? 26.46531 33.66637  10.71967  1.000 73.23854  ? 126 LEU B CD1 1 
ATOM   1939 C CD2 . LEU B 2 80  ? 25.54397 35.78984  11.05382  1.000 83.03476  ? 126 LEU B CD2 1 
ATOM   1940 N N   . ASN B 2 81  ? 21.42857 32.94174  10.85360  1.000 95.86530  ? 127 ASN B N   1 
ATOM   1941 C CA  . ASN B 2 81  ? 20.06474 32.90918  11.37086  1.000 98.58802  ? 127 ASN B CA  1 
ATOM   1942 C C   . ASN B 2 81  ? 19.39224 31.60397  10.98825  1.000 101.85887 ? 127 ASN B C   1 
ATOM   1943 O O   . ASN B 2 81  ? 18.45802 31.58797  10.18427  1.000 108.76730 ? 127 ASN B O   1 
ATOM   1944 C CB  . ASN B 2 81  ? 19.24413 34.09290  10.83579  1.000 106.36247 ? 127 ASN B CB  1 
ATOM   1945 C CG  . ASN B 2 81  ? 19.01764 35.18534  11.88229  1.000 111.72543 ? 127 ASN B CG  1 
ATOM   1946 O OD1 . ASN B 2 81  ? 19.63021 35.18081  12.94736  1.000 112.53592 ? 127 ASN B OD1 1 
ATOM   1947 N ND2 . ASN B 2 81  ? 18.16441 36.14754  11.55830  1.000 117.90003 ? 127 ASN B ND2 1 
ATOM   1948 N N   . GLN B 2 82  ? 19.85738 30.50392  11.55968  1.000 98.22047  ? 128 GLN B N   1 
ATOM   1949 C CA  . GLN B 2 82  ? 19.33991 29.19392  11.21053  1.000 85.51074  ? 128 GLN B CA  1 
ATOM   1950 C C   . GLN B 2 82  ? 19.64252 28.28828  12.38375  1.000 89.00442  ? 128 GLN B C   1 
ATOM   1951 O O   . GLN B 2 82  ? 20.79320 28.20449  12.82623  1.000 96.45156  ? 128 GLN B O   1 
ATOM   1952 C CB  . GLN B 2 82  ? 19.99036 28.68070  9.93431   1.000 82.11855  ? 128 GLN B CB  1 
ATOM   1953 C CG  . GLN B 2 82  ? 20.22612 27.18710  9.90801   1.000 85.61560  ? 128 GLN B CG  1 
ATOM   1954 C CD  . GLN B 2 82  ? 20.34297 26.64054  8.48723   1.000 81.70079  ? 128 GLN B CD  1 
ATOM   1955 O OE1 . GLN B 2 82  ? 20.16228 27.38497  7.51193   1.000 83.25237  ? 128 GLN B OE1 1 
ATOM   1956 N NE2 . GLN B 2 82  ? 20.62542 25.33169  8.36232   1.000 71.46974  ? 128 GLN B NE2 1 
ATOM   1957 N N   . LYS B 2 83  ? 18.62021 27.64679  12.91314  1.000 89.01957  ? 129 LYS B N   1 
ATOM   1958 C CA  . LYS B 2 83  ? 18.80108 26.79751  14.07424  1.000 90.05660  ? 129 LYS B CA  1 
ATOM   1959 C C   . LYS B 2 83  ? 18.64858 25.37985  13.56599  1.000 81.69788  ? 129 LYS B C   1 
ATOM   1960 O O   . LYS B 2 83  ? 17.64902 25.05919  12.92009  1.000 78.45505  ? 129 LYS B O   1 
ATOM   1961 C CB  . LYS B 2 83  ? 17.78703 27.12885  15.16864  1.000 101.70241 ? 129 LYS B CB  1 
ATOM   1962 C CG  . LYS B 2 83  ? 17.71973 28.64870  15.44667  1.000 112.58519 ? 129 LYS B CG  1 
ATOM   1963 C CD  . LYS B 2 83  ? 19.08537 29.27329  15.77961  1.000 116.43352 ? 129 LYS B CD  1 
ATOM   1964 C CE  . LYS B 2 83  ? 18.95658 30.78169  15.95781  1.000 115.31841 ? 129 LYS B CE  1 
ATOM   1965 N NZ  . LYS B 2 83  ? 20.27808 31.43390  16.11934  1.000 118.98642 ? 129 LYS B NZ  1 
ATOM   1966 N N   . GLY B 2 84  ? 19.65656 24.56015  13.79294  1.000 75.20301  ? 130 GLY B N   1 
ATOM   1967 C CA  . GLY B 2 84  ? 19.69096 23.24026  13.20510  1.000 67.86805  ? 130 GLY B CA  1 
ATOM   1968 C C   . GLY B 2 84  ? 20.78236 23.12217  12.15939  1.000 64.79158  ? 130 GLY B C   1 
ATOM   1969 O O   . GLY B 2 84  ? 21.48076 24.08539  11.82287  1.000 62.15834  ? 130 GLY B O   1 
ATOM   1970 N N   . VAL B 2 85  ? 20.93617 21.87967  11.68058  1.000 61.62978  ? 131 VAL B N   1 
ATOM   1971 C CA  . VAL B 2 85  ? 21.86316 21.53092  10.60690  1.000 51.59867  ? 131 VAL B CA  1 
ATOM   1972 C C   . VAL B 2 85  ? 21.11127 20.70245  9.57981   1.000 47.62423  ? 131 VAL B C   1 
ATOM   1973 O O   . VAL B 2 85  ? 20.42998 19.73835  9.94037   1.000 51.05743  ? 131 VAL B O   1 
ATOM   1974 C CB  . VAL B 2 85  ? 23.07820 20.74735  11.12704  1.000 49.38406  ? 131 VAL B CB  1 
ATOM   1975 C CG1 . VAL B 2 85  ? 23.95267 20.33315  9.97036   1.000 47.21730  ? 131 VAL B CG1 1 
ATOM   1976 C CG2 . VAL B 2 85  ? 23.85294 21.57471  12.13163  1.000 50.17192  ? 131 VAL B CG2 1 
ATOM   1977 N N   . VAL B 2 86  ? 21.21740 21.08229  8.30937   1.000 49.72213  ? 132 VAL B N   1 
ATOM   1978 C CA  . VAL B 2 86  ? 20.60741 20.34299  7.19928   1.000 50.97886  ? 132 VAL B CA  1 
ATOM   1979 C C   . VAL B 2 86  ? 21.67459 19.53376  6.46835   1.000 47.14888  ? 132 VAL B C   1 
ATOM   1980 O O   . VAL B 2 86  ? 22.69378 20.08375  6.03057   1.000 45.27346  ? 132 VAL B O   1 
ATOM   1981 C CB  . VAL B 2 86  ? 19.87375 21.28984  6.23270   1.000 40.09506  ? 132 VAL B CB  1 
ATOM   1982 C CG1 . VAL B 2 86  ? 19.45632 20.56681  5.01941   1.000 38.06109  ? 132 VAL B CG1 1 
ATOM   1983 C CG2 . VAL B 2 86  ? 18.65007 21.76300  6.86881   1.000 39.97329  ? 132 VAL B CG2 1 
ATOM   1984 N N   . MET B 2 87  ? 21.44763 18.22930  6.34525   1.000 39.26270  ? 133 MET B N   1 
ATOM   1985 C CA  . MET B 2 87  ? 22.32611 17.35674  5.58832   1.000 43.15082  ? 133 MET B CA  1 
ATOM   1986 C C   . MET B 2 87  ? 21.69333 17.02712  4.24864   1.000 48.85929  ? 133 MET B C   1 
ATOM   1987 O O   . MET B 2 87  ? 20.48548 16.78221  4.17050   1.000 49.37416  ? 133 MET B O   1 
ATOM   1988 C CB  . MET B 2 87  ? 22.62892 16.07380  6.34855   1.000 42.34732  ? 133 MET B CB  1 
ATOM   1989 C CG  . MET B 2 87  ? 23.85279 15.34666  5.86425   1.000 40.52186  ? 133 MET B CG  1 
ATOM   1990 S SD  . MET B 2 87  ? 24.09836 13.73158  6.64864   1.000 48.32772  ? 133 MET B SD  1 
ATOM   1991 C CE  . MET B 2 87  ? 22.45036 13.01790  6.71068   1.000 47.56788  ? 133 MET B CE  1 
ATOM   1992 N N   . ILE B 2 88  ? 22.50691 17.05504  3.19221   1.000 46.94474  ? 134 ILE B N   1 
ATOM   1993 C CA  . ILE B 2 88  ? 22.10241 16.58159  1.87923   1.000 44.49277  ? 134 ILE B CA  1 
ATOM   1994 C C   . ILE B 2 88  ? 23.09932 15.51652  1.47371   1.000 48.24533  ? 134 ILE B C   1 
ATOM   1995 O O   . ILE B 2 88  ? 24.28271 15.81618  1.28032   1.000 51.40234  ? 134 ILE B O   1 
ATOM   1996 C CB  . ILE B 2 88  ? 22.07623 17.69567  0.82952   1.000 48.84645  ? 134 ILE B CB  1 
ATOM   1997 C CG1 . ILE B 2 88  ? 21.07435 18.78514  1.18869   1.000 51.21807  ? 134 ILE B CG1 1 
ATOM   1998 C CG2 . ILE B 2 88  ? 21.63015 17.11930  -0.49750  1.000 50.39557  ? 134 ILE B CG2 1 
ATOM   1999 C CD1 . ILE B 2 88  ? 21.66672 19.87670  2.00166   1.000 47.66324  ? 134 ILE B CD1 1 
ATOM   2000 N N   . ALA B 2 89  ? 22.63037 14.28491  1.32560   1.000 51.82032  ? 135 ALA B N   1 
ATOM   2001 C CA  . ALA B 2 89  ? 23.47964 13.16381  0.95115   1.000 50.78271  ? 135 ALA B CA  1 
ATOM   2002 C C   . ALA B 2 89  ? 23.13997 12.73595  -0.47028  1.000 50.44689  ? 135 ALA B C   1 
ATOM   2003 O O   . ALA B 2 89  ? 21.95805 12.65342  -0.82011  1.000 51.30496  ? 135 ALA B O   1 
ATOM   2004 C CB  . ALA B 2 89  ? 23.29039 12.00171  1.93045   1.000 48.66754  ? 135 ALA B CB  1 
ATOM   2005 N N   . SER B 2 90  ? 24.16245 12.48599  -1.29971  1.000 50.62828  ? 136 SER B N   1 
ATOM   2006 C CA  . SER B 2 90  ? 23.91284 11.92493  -2.62168  1.000 56.42366  ? 136 SER B CA  1 
ATOM   2007 C C   . SER B 2 90  ? 24.88734 10.79083  -2.91126  1.000 59.78439  ? 136 SER B C   1 
ATOM   2008 O O   . SER B 2 90  ? 26.01682 10.77565  -2.42105  1.000 61.55511  ? 136 SER B O   1 
ATOM   2009 C CB  . SER B 2 90  ? 23.99159 12.97997  -3.74961  1.000 56.72740  ? 136 SER B CB  1 
ATOM   2010 O OG  . SER B 2 90  ? 25.30786 13.15542  -4.23204  1.000 62.79520  ? 136 SER B OG  1 
ATOM   2011 N N   . ASN B 2 91  ? 24.42136 9.83817   -3.71511  1.000 61.42314  ? 137 ASN B N   1 
ATOM   2012 C CA  . ASN B 2 91  ? 25.17863 8.66402   -4.11716  1.000 68.30374  ? 137 ASN B CA  1 
ATOM   2013 C C   . ASN B 2 91  ? 25.00861 8.45998   -5.62086  1.000 80.74294  ? 137 ASN B C   1 
ATOM   2014 O O   . ASN B 2 91  ? 24.11442 9.04205   -6.24084  1.000 79.24102  ? 137 ASN B O   1 
ATOM   2015 C CB  . ASN B 2 91  ? 24.70200 7.43442   -3.35457  1.000 64.11892  ? 137 ASN B CB  1 
ATOM   2016 C CG  . ASN B 2 91  ? 25.68107 6.31191   -3.40506  1.000 75.84822  ? 137 ASN B CG  1 
ATOM   2017 O OD1 . ASN B 2 91  ? 26.44948 6.20413   -4.34637  1.000 86.01930  ? 137 ASN B OD1 1 
ATOM   2018 N ND2 . ASN B 2 91  ? 25.65635 5.45031   -2.40222  1.000 81.34390  ? 137 ASN B ND2 1 
ATOM   2019 N N   . TYR B 2 92  ? 25.87190 7.62274   -6.20646  1.000 87.13923  ? 138 TYR B N   1 
ATOM   2020 C CA  . TYR B 2 92  ? 25.87173 7.38529   -7.64968  1.000 88.18802  ? 138 TYR B CA  1 
ATOM   2021 C C   . TYR B 2 92  ? 26.79794 6.22112   -7.97921  1.000 98.80904  ? 138 TYR B C   1 
ATOM   2022 O O   . TYR B 2 92  ? 27.79100 5.98046   -7.28629  1.000 98.37310  ? 138 TYR B O   1 
ATOM   2023 C CB  . TYR B 2 92  ? 26.31412 8.63236   -8.42705  1.000 90.83295  ? 138 TYR B CB  1 
ATOM   2024 C CG  . TYR B 2 92  ? 27.55466 9.32915   -7.88427  1.000 98.39664  ? 138 TYR B CG  1 
ATOM   2025 C CD1 . TYR B 2 92  ? 28.84125 8.95035   -8.32461  1.000 95.62036  ? 138 TYR B CD1 1 
ATOM   2026 C CD2 . TYR B 2 92  ? 27.44904 10.33125  -6.89289  1.000 89.12491  ? 138 TYR B CD2 1 
ATOM   2027 C CE1 . TYR B 2 92  ? 29.98402 9.58497   -7.83199  1.000 92.56147  ? 138 TYR B CE1 1 
ATOM   2028 C CE2 . TYR B 2 92  ? 28.58297 10.96254  -6.38678  1.000 89.00846  ? 138 TYR B CE2 1 
ATOM   2029 C CZ  . TYR B 2 92  ? 29.84928 10.58567  -6.86086  1.000 93.68063  ? 138 TYR B CZ  1 
ATOM   2030 O OH  . TYR B 2 92  ? 30.97766 11.21228  -6.36707  1.000 93.05432  ? 138 TYR B OH  1 
ATOM   2031 N N   . ASN B 2 93  ? 26.48118 5.52096   -9.05705  1.000 109.33209 ? 139 ASN B N   1 
ATOM   2032 C CA  . ASN B 2 93  ? 27.25739 4.35120   -9.41009  1.000 114.11047 ? 139 ASN B CA  1 
ATOM   2033 C C   . ASN B 2 93  ? 28.31008 4.64634   -10.47773 1.000 118.33413 ? 139 ASN B C   1 
ATOM   2034 O O   . ASN B 2 93  ? 29.49933 4.38780   -10.27667 1.000 121.24334 ? 139 ASN B O   1 
ATOM   2035 C CB  . ASN B 2 93  ? 26.33122 3.24428   -9.87948  1.000 121.89605 ? 139 ASN B CB  1 
ATOM   2036 C CG  . ASN B 2 93  ? 26.87407 1.88105   -9.56085  1.000 131.45047 ? 139 ASN B CG  1 
ATOM   2037 O OD1 . ASN B 2 93  ? 28.02558 1.74702   -9.14195  1.000 130.65399 ? 139 ASN B OD1 1 
ATOM   2038 N ND2 . ASN B 2 93  ? 26.05830 0.85435   -9.76220  1.000 137.46329 ? 139 ASN B ND2 1 
HETATM 2039 O O   . HOH C 3 .   ? 36.60520 1.05783   10.16005  1.000 73.55670  ? 301 HOH A O   1 
HETATM 2040 O O   . HOH C 3 .   ? 34.56930 -1.39469  17.04247  1.000 58.12355  ? 302 HOH A O   1 
HETATM 2041 O O   . HOH C 3 .   ? 25.00448 -1.72955  31.24435  1.000 50.45178  ? 303 HOH A O   1 
HETATM 2042 O O   . HOH C 3 .   ? 33.00181 -28.29279 15.50066  1.000 110.65974 ? 304 HOH A O   1 
HETATM 2043 O O   . HOH C 3 .   ? 11.17581 -7.66019  11.20538  1.000 65.20879  ? 305 HOH A O   1 
HETATM 2044 O O   . HOH C 3 .   ? 11.11125 -1.35124  9.70708   1.000 61.01076  ? 306 HOH A O   1 
HETATM 2045 O O   . HOH C 3 .   ? 37.50624 -13.36690 10.80511  1.000 65.05045  ? 307 HOH A O   1 
HETATM 2046 O O   . HOH C 3 .   ? 23.83196 20.23843  16.23523  1.000 52.16440  ? 308 HOH A O   1 
HETATM 2047 O O   . HOH C 3 .   ? 14.69984 14.69984  0.00000   0.50  46.32394  ? 309 HOH A O   1 
HETATM 2048 O O   . HOH C 3 .   ? 39.59793 -6.25242  8.28938   1.000 57.73817  ? 310 HOH A O   1 
HETATM 2049 O O   . HOH C 3 .   ? 37.24130 -6.79282  6.66725   1.000 66.41779  ? 311 HOH A O   1 
HETATM 2050 O O   . HOH C 3 .   ? 21.64010 7.96755   25.94765  1.000 49.20419  ? 312 HOH A O   1 
HETATM 2051 O O   . HOH C 3 .   ? 36.05256 -11.19566 9.45803   1.000 62.98504  ? 313 HOH A O   1 
HETATM 2052 O O   . HOH C 3 .   ? 43.15973 -8.57815  14.16104  1.000 59.95379  ? 314 HOH A O   1 
HETATM 2053 O O   . HOH D 3 .   ? 18.43052 8.24529   27.45316  1.000 54.87057  ? 201 HOH B O   1 
HETATM 2054 O O   . HOH D 3 .   ? 38.58689 17.22110  4.58425   1.000 42.08180  ? 202 HOH B O   1 
HETATM 2055 O O   . HOH D 3 .   ? 15.67363 9.89762   29.35398  1.000 55.86453  ? 203 HOH B O   1 
HETATM 2056 O O   . HOH D 3 .   ? 31.33566 3.95807   -8.14931  1.000 80.41153  ? 204 HOH B O   1 
HETATM 2057 O O   . HOH D 3 .   ? 16.28560 12.19891  27.52977  1.000 57.19520  ? 205 HOH B O   1 
HETATM 2058 O O   . HOH D 3 .   ? 23.14801 4.29926   26.01077  1.000 50.94686  ? 206 HOH B O   1 
HETATM 2059 O O   . HOH D 3 .   ? 39.06160 7.87189   -0.46653  1.000 75.99609  ? 207 HOH B O   1 
HETATM 2060 O O   . HOH D 3 .   ? 11.84743 3.51616   6.15054   1.000 60.05135  ? 208 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLN A 40  ? 1.23908 1.50335 1.95784 -0.25429 0.01960  0.12094  57  GLN A N   
2    C CA  . GLN A 40  ? 1.31950 1.47283 1.94069 -0.23736 0.01257  0.10488  57  GLN A CA  
3    C C   . GLN A 40  ? 1.22140 1.38123 1.75863 -0.17707 -0.01026 0.11217  57  GLN A C   
4    O O   . GLN A 40  ? 1.23014 1.37251 1.71572 -0.16947 -0.04378 0.08139  57  GLN A O   
5    C CB  . GLN A 40  ? 1.39319 1.43053 1.98057 -0.23519 0.06616  0.13454  57  GLN A CB  
6    C CG  . GLN A 40  ? 1.48054 1.39973 1.99795 -0.23754 0.06445  0.10906  57  GLN A CG  
7    C CD  . GLN A 40  ? 1.55463 1.45370 2.11701 -0.29970 0.04492  0.05612  57  GLN A CD  
8    O OE1 . GLN A 40  ? 1.51853 1.47542 2.17759 -0.35346 0.04660  0.04376  57  GLN A OE1 
9    N NE2 . GLN A 40  ? 1.54613 1.36624 2.04040 -0.29340 0.02742  0.02096  57  GLN A NE2 
10   N N   . ILE A 41  ? 1.13033 1.31130 1.65271 -0.13593 0.01090  0.15074  58  ILE A N   
11   C CA  . ILE A 41  ? 1.10875 1.29331 1.56286 -0.08583 -0.00381 0.15774  58  ILE A CA  
12   C C   . ILE A 41  ? 1.02163 1.30866 1.51603 -0.06969 -0.02612 0.16283  58  ILE A C   
13   O O   . ILE A 41  ? 0.96907 1.30999 1.51808 -0.06457 -0.00514 0.18736  58  ILE A O   
14   C CB  . ILE A 41  ? 1.07058 1.20644 1.47532 -0.04947 0.03263  0.18900  58  ILE A CB  
15   C CG1 . ILE A 41  ? 1.07756 1.11894 1.42628 -0.04919 0.04886  0.18527  58  ILE A CG1 
16   C CG2 . ILE A 41  ? 0.86278 1.01368 1.21825 -0.00740 0.02123  0.19341  58  ILE A CG2 
17   C CD1 . ILE A 41  ? 1.00995 1.02078 1.31236 -0.01183 0.08092  0.21276  58  ILE A CD1 
18   N N   . PRO A 42  ? 0.94867 1.26671 1.41509 -0.05536 -0.06492 0.14397  59  PRO A N   
19   C CA  . PRO A 42  ? 0.88650 1.29622 1.37936 -0.02639 -0.08312 0.15628  59  PRO A CA  
20   C C   . PRO A 42  ? 0.86592 1.26762 1.34694 0.01387  -0.04972 0.19318  59  PRO A C   
21   O O   . PRO A 42  ? 0.86974 1.19562 1.29859 0.02656  -0.02356 0.20287  59  PRO A O   
22   C CB  . PRO A 42  ? 0.85564 1.26060 1.28243 -0.00432 -0.11802 0.13968  59  PRO A CB  
23   C CG  . PRO A 42  ? 0.87403 1.22732 1.27844 -0.04110 -0.13206 0.10244  59  PRO A CG  
24   C CD  . PRO A 42  ? 0.94894 1.22276 1.35709 -0.06170 -0.09231 0.11155  59  PRO A CD  
25   N N   . ASP A 43  ? 0.94950 1.43584 1.48070 0.03583  -0.05128 0.21044  60  ASP A N   
26   C CA  . ASP A 43  ? 0.92114 1.39985 1.44924 0.07165  -0.01515 0.24094  60  ASP A CA  
27   C C   . ASP A 43  ? 0.94256 1.35699 1.38892 0.11358  -0.00942 0.24926  60  ASP A C   
28   O O   . ASP A 43  ? 0.94540 1.31058 1.36315 0.13126  0.02273  0.26045  60  ASP A O   
29   C CB  . ASP A 43  ? 0.87848 1.46764 1.48515 0.08822  -0.01522 0.25705  60  ASP A CB  
30   C CG  . ASP A 43  ? 0.91483 1.56296 1.61300 0.04250  -0.00279 0.25439  60  ASP A CG  
31   O OD1 . ASP A 43  ? 0.92781 1.55543 1.63990 0.04215  0.03962  0.27448  60  ASP A OD1 
32   O OD2 . ASP A 43  ? 0.94495 1.66033 1.70061 0.00531  -0.03376 0.23074  60  ASP A OD2 
33   N N   . HIS A 44  ? 0.82986 1.24294 1.23648 0.12870  -0.03759 0.24270  61  HIS A N   
34   C CA  . HIS A 44  ? 0.81503 1.15721 1.14894 0.16081  -0.02358 0.25229  61  HIS A CA  
35   C C   . HIS A 44  ? 0.84516 1.10444 1.12526 0.13929  -0.01372 0.23561  61  HIS A C   
36   O O   . HIS A 44  ? 0.88007 1.08156 1.11125 0.15592  0.00475  0.23906  61  HIS A O   
37   C CB  . HIS A 44  ? 0.83527 1.19709 1.13649 0.19145  -0.04753 0.26030  61  HIS A CB  
38   C CG  . HIS A 44  ? 0.88668 1.25876 1.16462 0.16953  -0.08243 0.23726  61  HIS A CG  
39   N ND1 . HIS A 44  ? 0.88279 1.31299 1.20966 0.13323  -0.11030 0.21197  61  HIS A ND1 
40   C CD2 . HIS A 44  ? 0.97098 1.30065 1.18047 0.17835  -0.09118 0.23323  61  HIS A CD2 
41   C CE1 . HIS A 44  ? 0.91975 1.33997 1.20408 0.12308  -0.13746 0.18931  61  HIS A CE1 
42   N NE2 . HIS A 44  ? 0.97307 1.33619 1.18462 0.15241  -0.12584 0.20410  61  HIS A NE2 
43   N N   . LYS A 45  ? 0.80978 1.06233 1.10073 0.10336  -0.02318 0.21675  62  LYS A N   
44   C CA  . LYS A 45  ? 0.78579 0.96890 1.02734 0.09099  -0.01353 0.20296  62  LYS A CA  
45   C C   . LYS A 45  ? 0.77936 0.93573 1.02608 0.08848  0.01763  0.20936  62  LYS A C   
46   O O   . LYS A 45  ? 0.79773 0.90677 1.00176 0.08808  0.02727  0.20036  62  LYS A O   
47   C CB  . LYS A 45  ? 0.76958 0.94560 1.00606 0.06244  -0.03776 0.17894  62  LYS A CB  
48   C CG  . LYS A 45  ? 0.75455 0.96979 0.98176 0.06666  -0.07270 0.16801  62  LYS A CG  
49   C CD  . LYS A 45  ? 0.72333 0.90426 0.91138 0.04882  -0.09026 0.13905  62  LYS A CD  
50   C CE  . LYS A 45  ? 0.79969 1.01277 0.95299 0.06370  -0.12143 0.12903  62  LYS A CE  
51   N NZ  . LYS A 45  ? 0.74986 0.92521 0.85946 0.04910  -0.13488 0.09706  62  LYS A NZ  
52   N N   . LYS A 46  ? 0.73938 0.93334 1.03532 0.09122  0.03413  0.22558  63  LYS A N   
53   C CA  . LYS A 46  ? 0.68125 0.85490 0.97272 0.09674  0.06627  0.23530  63  LYS A CA  
54   C C   . LYS A 46  ? 0.69723 0.83975 0.93935 0.12507  0.08141  0.23201  63  LYS A C   
55   O O   . LYS A 46  ? 0.71273 0.85865 0.94863 0.14355  0.07904  0.23342  63  LYS A O   
56   C CB  . LYS A 46  ? 0.67938 0.90737 1.03414 0.09698  0.08536  0.25577  63  LYS A CB  
57   C CG  . LYS A 46  ? 0.67540 0.94313 1.09737 0.05968  0.07789  0.25693  63  LYS A CG  
58   C CD  . LYS A 46  ? 0.70365 0.99596 1.16869 0.05787  0.11647  0.28148  63  LYS A CD  
59   C CE  . LYS A 46  ? 0.78318 1.16867 1.34243 0.04239  0.11690  0.29153  63  LYS A CE  
60   N NZ  . LYS A 46  ? 0.84618 1.26063 1.45691 -0.00426 0.08648  0.27012  63  LYS A NZ  
61   N N   . PRO A 47  ? 0.69269 0.80518 0.89933 0.13016  0.09831  0.22661  64  PRO A N   
62   C CA  . PRO A 47  ? 0.72250 0.81366 0.88728 0.15038  0.11000  0.21300  64  PRO A CA  
63   C C   . PRO A 47  ? 0.74056 0.85017 0.92201 0.17384  0.13018  0.22203  64  PRO A C   
64   O O   . PRO A 47  ? 0.77927 0.92369 0.99696 0.17955  0.14421  0.24151  64  PRO A O   
65   C CB  . PRO A 47  ? 0.71014 0.78898 0.84099 0.15483  0.12076  0.20662  64  PRO A CB  
66   C CG  . PRO A 47  ? 0.69657 0.77284 0.84669 0.13909  0.11923  0.22235  64  PRO A CG  
67   C CD  . PRO A 47  ? 0.67601 0.77998 0.88418 0.12234  0.11280  0.23584  64  PRO A CD  
68   N N   . GLN A 48  ? 0.69502 0.77820 0.85107 0.18738  0.13587  0.20742  65  GLN A N   
69   C CA  . GLN A 48  ? 0.74564 0.83519 0.91391 0.21473  0.15612  0.21443  65  GLN A CA  
70   C C   . GLN A 48  ? 0.82329 0.87038 0.94854 0.22641  0.17312  0.18542  65  GLN A C   
71   O O   . GLN A 48  ? 0.80220 0.81451 0.89893 0.20969  0.16608  0.16191  65  GLN A O   
72   C CB  . GLN A 48  ? 0.74720 0.84445 0.94146 0.22503  0.14694  0.23190  65  GLN A CB  
73   C CG  . GLN A 48  ? 0.80567 0.84446 0.96367 0.22866  0.14794  0.22048  65  GLN A CG  
74   C CD  . GLN A 48  ? 0.86945 0.91724 1.03935 0.23795  0.13188  0.24258  65  GLN A CD  
75   O OE1 . GLN A 48  ? 0.87640 0.94173 1.04783 0.21811  0.10645  0.24451  65  GLN A OE1 
76   N NE2 . GLN A 48  ? 0.94413 0.98028 1.11701 0.27398  0.14707  0.25920  65  GLN A NE2 
77   N N   . TYR A 49  ? 0.83946 0.89364 0.96321 0.25378  0.19714  0.18410  66  TYR A N   
78   C CA  . TYR A 49  ? 0.90305 0.91378 0.98893 0.26638  0.21509  0.15018  66  TYR A CA  
79   C C   . TYR A 49  ? 0.96775 0.93384 1.06030 0.28480  0.22779  0.15700  66  TYR A C   
80   O O   . TYR A 49  ? 0.98895 0.98144 1.11652 0.30238  0.22594  0.19142  66  TYR A O   
81   C CB  . TYR A 49  ? 0.88524 0.92263 0.95464 0.29293  0.23663  0.14170  66  TYR A CB  
82   C CG  . TYR A 49  ? 0.86117 0.92398 0.89732 0.28566  0.23043  0.12376  66  TYR A CG  
83   C CD1 . TYR A 49  ? 0.90116 0.94492 0.89768 0.27418  0.22322  0.07723  66  TYR A CD1 
84   C CD2 . TYR A 49  ? 0.86537 0.97498 0.91034 0.29366  0.23520  0.15403  66  TYR A CD2 
85   C CE1 . TYR A 49  ? 0.93815 1.02039 0.90194 0.27722  0.21496  0.06221  66  TYR A CE1 
86   C CE2 . TYR A 49  ? 0.87425 1.00483 0.88026 0.29842  0.23291  0.14491  66  TYR A CE2 
87   C CZ  . TYR A 49  ? 0.91594 1.03846 0.87968 0.29403  0.22030  0.09931  66  TYR A CZ  
88   O OH  . TYR A 49  ? 0.97807 1.13534 0.90103 0.30721  0.21493  0.09148  66  TYR A OH  
89   N N   . ALA A 50  ? 0.99608 0.89554 1.05610 0.28210  0.24220  0.12359  67  ALA A N   
90   C CA  . ALA A 50  ? 1.13871 0.97541 1.19753 0.30123  0.25952  0.13482  67  ALA A CA  
91   C C   . ALA A 50  ? 1.29990 1.05639 1.32297 0.29978  0.28628  0.08948  67  ALA A C   
92   O O   . ALA A 50  ? 1.28515 1.01754 1.29105 0.26165  0.28158  0.05154  67  ALA A O   
93   C CB  . ALA A 50  ? 1.13188 0.95132 1.19684 0.28142  0.24268  0.15704  67  ALA A CB  
94   N N   . SER A 51  ? 1.36072 1.07747 1.37584 0.34059  0.31511  0.09074  68  SER A N   
95   C CA  . SER A 51  ? 1.46706 1.10545 1.44621 0.34162  0.34334  0.03870  68  SER A CA  
96   C C   . SER A 51  ? 1.58605 1.12436 1.55251 0.30972  0.35683  0.02259  68  SER A C   
97   O O   . SER A 51  ? 1.60475 1.07226 1.56891 0.33308  0.37846  0.05384  68  SER A O   
98   C CB  . SER A 51  ? 1.55374 1.16800 1.52511 0.39966  0.37439  0.04664  68  SER A CB  
99   O OG  . SER A 51  ? 1.66592 1.26694 1.65865 0.43594  0.38202  0.10113  68  SER A OG  
100  N N   . VAL A 52  ? 1.56534 1.10024 1.52372 0.25807  0.34728  -0.02578 69  VAL A N   
101  C CA  . VAL A 52  ? 1.56011 1.01441 1.51701 0.21601  0.36158  -0.04083 69  VAL A CA  
102  C C   . VAL A 52  ? 1.73074 1.06639 1.66571 0.21168  0.40299  -0.08501 69  VAL A C   
103  O O   . VAL A 52  ? 1.77478 1.03151 1.71166 0.17047  0.42360  -0.10179 69  VAL A O   
104  C CB  . VAL A 52  ? 1.50251 1.01750 1.47003 0.16064  0.33490  -0.07744 69  VAL A CB  
105  C CG1 . VAL A 52  ? 1.35041 0.95736 1.33554 0.16459  0.29976  -0.03200 69  VAL A CG1 
106  C CG2 . VAL A 52  ? 1.53054 1.08774 1.48308 0.15166  0.32700  -0.14361 69  VAL A CG2 
107  N N   . ASP A 53  ? 1.95335 1.27004 1.86774 0.25135  0.41951  -0.10579 70  ASP A N   
108  C CA  . ASP A 53  ? 2.07914 1.27879 1.96756 0.24620  0.45870  -0.16127 70  ASP A CA  
109  C C   . ASP A 53  ? 2.13065 1.33466 1.99442 0.30936  0.47276  -0.16651 70  ASP A C   
110  O O   . ASP A 53  ? 2.04711 1.34768 1.92109 0.35103  0.45429  -0.12375 70  ASP A O   
111  C CB  . ASP A 53  ? 2.10258 1.31161 1.99106 0.18009  0.44916  -0.24539 70  ASP A CB  
112  C CG  . ASP A 53  ? 2.02849 1.38707 1.92225 0.17148  0.40227  -0.26264 70  ASP A CG  
113  O OD1 . ASP A 53  ? 1.97580 1.41069 1.86384 0.21948  0.38698  -0.22418 70  ASP A OD1 
114  O OD2 . ASP A 53  ? 2.01514 1.41707 1.92087 0.11781  0.38307  -0.31224 70  ASP A OD2 
115  N N   . ASP A 54  ? 2.16242 1.27913 1.99902 0.30773  0.49771  -0.21642 71  ASP A N   
116  C CA  . ASP A 54  ? 2.15325 1.29706 1.96431 0.35745  0.50065  -0.23214 71  ASP A CA  
117  C C   . ASP A 54  ? 2.15192 1.38786 1.94332 0.35324  0.48136  -0.29091 71  ASP A C   
118  O O   . ASP A 54  ? 2.14454 1.41801 1.91174 0.39603  0.48294  -0.30318 71  ASP A O   
119  C CB  . ASP A 54  ? 2.22421 1.24895 2.01047 0.35887  0.52908  -0.26518 71  ASP A CB  
120  C CG  . ASP A 54  ? 2.31251 1.25009 2.09913 0.28597  0.53886  -0.32746 71  ASP A CG  
121  O OD1 . ASP A 54  ? 2.28370 1.27573 2.07849 0.23730  0.51858  -0.38083 71  ASP A OD1 
122  O OD2 . ASP A 54  ? 2.41197 1.23442 2.19280 0.27653  0.56746  -0.32268 71  ASP A OD2 
123  N N   . THR A 55  ? 2.09434 1.38646 1.89618 0.30262  0.45683  -0.32158 72  THR A N   
124  C CA  . THR A 55  ? 1.95831 1.37304 1.74119 0.30390  0.42515  -0.35641 72  THR A CA  
125  C C   . THR A 55  ? 1.82672 1.34465 1.61926 0.35380  0.41193  -0.28336 72  THR A C   
126  O O   . THR A 55  ? 1.79953 1.32712 1.62900 0.36338  0.40906  -0.21096 72  THR A O   
127  C CB  . THR A 55  ? 1.87204 1.35257 1.67399 0.23899  0.38875  -0.39042 72  THR A CB  
128  O OG1 . THR A 55  ? 2.01876 1.40308 1.83359 0.18089  0.40498  -0.44382 72  THR A OG1 
129  C CG2 . THR A 55  ? 1.73941 1.33069 1.50676 0.24556  0.36071  -0.44432 72  THR A CG2 
130  N N   . LYS A 56  ? 1.74432 1.34160 1.50256 0.38496  0.40549  -0.30483 73  LYS A N   
131  C CA  . LYS A 56  ? 1.66037 1.36257 1.43043 0.42133  0.39526  -0.23995 73  LYS A CA  
132  C C   . LYS A 56  ? 1.56621 1.34489 1.36672 0.38391  0.35792  -0.20723 73  LYS A C   
133  O O   . LYS A 56  ? 1.44701 1.28565 1.27561 0.40090  0.35202  -0.14153 73  LYS A O   
134  C CB  . LYS A 56  ? 1.58871 1.35048 1.30570 0.46428  0.40337  -0.27098 73  LYS A CB  
135  C CG  . LYS A 56  ? 1.66200 1.48888 1.34019 0.43985  0.37353  -0.33024 73  LYS A CG  
136  C CD  . LYS A 56  ? 1.62118 1.46144 1.24351 0.46263  0.38055  -0.39270 73  LYS A CD  
137  C CE  . LYS A 56  ? 1.75256 1.47871 1.36196 0.44411  0.39965  -0.46884 73  LYS A CE  
138  N NZ  . LYS A 56  ? 1.72573 1.46331 1.28687 0.46013  0.40707  -0.53069 73  LYS A NZ  
139  N N   . THR A 57  ? 1.55898 1.33675 1.35883 0.33259  0.33465  -0.25268 74  THR A N   
140  C CA  . THR A 57  ? 1.45380 1.30345 1.27705 0.30324  0.30106  -0.22621 74  THR A CA  
141  C C   . THR A 57  ? 1.34234 1.15366 1.21451 0.28225  0.29928  -0.16974 74  THR A C   
142  O O   . THR A 57  ? 1.41024 1.14813 1.29706 0.24866  0.30654  -0.18645 74  THR A O   
143  C CB  . THR A 57  ? 1.48186 1.35813 1.29284 0.25991  0.27769  -0.29583 74  THR A CB  
144  O OG1 . THR A 57  ? 1.58158 1.37032 1.41823 0.21233  0.28829  -0.32621 74  THR A OG1 
145  C CG2 . THR A 57  ? 1.49014 1.40135 1.24625 0.28230  0.27808  -0.36421 74  THR A CG2 
146  N N   . GLN A 58  ? 1.19549 1.05651 1.09149 0.30136  0.29155  -0.10420 75  GLN A N   
147  C CA  . GLN A 58  ? 1.15490 1.00037 1.09240 0.28518  0.28299  -0.05289 75  GLN A CA  
148  C C   . GLN A 58  ? 1.08926 0.97175 1.03531 0.24505  0.25327  -0.05729 75  GLN A C   
149  O O   . GLN A 58  ? 1.12775 1.06380 1.05228 0.23920  0.23832  -0.08723 75  GLN A O   
150  C CB  . GLN A 58  ? 1.10603 0.99816 1.07087 0.31837  0.28603  0.00902  75  GLN A CB  
151  C CG  . GLN A 58  ? 1.17709 1.03917 1.14558 0.36199  0.31634  0.02283  75  GLN A CG  
152  C CD  . GLN A 58  ? 1.17572 1.09649 1.18980 0.38692  0.31722  0.08450  75  GLN A CD  
153  O OE1 . GLN A 58  ? 1.22862 1.13009 1.27113 0.40202  0.32212  0.11501  75  GLN A OE1 
154  N NE2 . GLN A 58  ? 1.07243 1.06909 1.09485 0.39197  0.31393  0.10346  75  GLN A NE2 
155  N N   . ALA A 59  ? 1.07319 0.93185 1.04659 0.22315  0.24508  -0.02713 76  ALA A N   
156  C CA  . ALA A 59  ? 0.96060 0.85166 0.94149 0.18909  0.22047  -0.03067 76  ALA A CA  
157  C C   . ALA A 59  ? 0.90164 0.83222 0.90400 0.19550  0.20297  0.02286  76  ALA A C   
158  O O   . ALA A 59  ? 0.92958 0.85004 0.95259 0.21259  0.20806  0.06254  76  ALA A O   
159  C CB  . ALA A 59  ? 0.92436 0.75639 0.91381 0.15218  0.22731  -0.04866 76  ALA A CB  
160  N N   . LEU A 60  ? 0.81203 0.79075 0.81021 0.18312  0.18216  0.02069  77  LEU A N   
161  C CA  . LEU A 60  ? 0.79587 0.80363 0.81068 0.18593  0.16725  0.06293  77  LEU A CA  
162  C C   . LEU A 60  ? 0.77274 0.75830 0.80152 0.16149  0.15476  0.07477  77  LEU A C   
163  O O   . LEU A 60  ? 0.72503 0.70841 0.74535 0.13912  0.14902  0.04983  77  LEU A O   
164  C CB  . LEU A 60  ? 0.76767 0.82593 0.76303 0.19327  0.15606  0.05911  77  LEU A CB  
165  C CG  . LEU A 60  ? 0.75567 0.82922 0.76620 0.19625  0.14770  0.10100  77  LEU A CG  
166  C CD1 . LEU A 60  ? 0.79114 0.86456 0.83200 0.20806  0.16051  0.13644  77  LEU A CD1 
167  C CD2 . LEU A 60  ? 0.76785 0.87537 0.75110 0.21199  0.14449  0.10298  77  LEU A CD2 
168  N N   . PHE A 61  ? 0.73341 0.71293 0.78418 0.16691  0.15030  0.11136  78  PHE A N   
169  C CA  . PHE A 61  ? 0.73769 0.70465 0.79324 0.15063  0.13627  0.12489  78  PHE A CA  
170  C C   . PHE A 61  ? 0.76246 0.76340 0.82993 0.14736  0.11580  0.14447  78  PHE A C   
171  O O   . PHE A 61  ? 0.75370 0.77385 0.84731 0.15625  0.11241  0.16847  78  PHE A O   
172  C CB  . PHE A 61  ? 0.78315 0.71726 0.84749 0.16245  0.14472  0.14701  78  PHE A CB  
173  C CG  . PHE A 61  ? 0.87039 0.74524 0.91767 0.15768  0.16816  0.12947  78  PHE A CG  
174  C CD1 . PHE A 61  ? 0.85855 0.70368 0.90188 0.17334  0.19148  0.11463  78  PHE A CD1 
175  C CD2 . PHE A 61  ? 0.87663 0.72002 0.91121 0.13662  0.17142  0.12693  78  PHE A CD2 
176  C CE1 . PHE A 61  ? 0.91577 0.69100 0.94452 0.16429  0.21735  0.09420  78  PHE A CE1 
177  C CE2 . PHE A 61  ? 0.89134 0.66948 0.91508 0.12581  0.20031  0.11205  78  PHE A CE2 
178  C CZ  . PHE A 61  ? 0.93391 0.67305 0.95563 0.13764  0.22310  0.09391  78  PHE A CZ  
179  N N   . ASP A 62  ? 0.74255 0.75161 0.79417 0.13392  0.10396  0.13187  79  ASP A N   
180  C CA  . ASP A 62  ? 0.69582 0.71775 0.75269 0.12911  0.08710  0.14557  79  ASP A CA  
181  C C   . ASP A 62  ? 0.70663 0.71651 0.75122 0.11617  0.07356  0.14227  79  ASP A C   
182  O O   . ASP A 62  ? 0.69486 0.70890 0.72105 0.11118  0.06717  0.12962  79  ASP A O   
183  C CB  . ASP A 62  ? 0.69661 0.73411 0.73729 0.13622  0.08849  0.13856  79  ASP A CB  
184  C CG  . ASP A 62  ? 0.74116 0.77303 0.78717 0.13219  0.07864  0.15394  79  ASP A CG  
185  O OD1 . ASP A 62  ? 0.74409 0.77341 0.81804 0.12156  0.07113  0.16811  79  ASP A OD1 
186  O OD2 . ASP A 62  ? 0.71837 0.74897 0.74138 0.14075  0.07862  0.14999  79  ASP A OD2 
187  N N   . ILE A 63  ? 0.74978 0.74813 0.80004 0.11690  0.07095  0.15561  80  ILE A N   
188  C CA  . ILE A 63  ? 0.71010 0.69651 0.73849 0.10990  0.06404  0.15474  80  ILE A CA  
189  C C   . ILE A 63  ? 0.70725 0.70707 0.72952 0.10519  0.04121  0.15393  80  ILE A C   
190  O O   . ILE A 63  ? 0.70989 0.70468 0.70593 0.10142  0.03649  0.14666  80  ILE A O   
191  C CB  . ILE A 63  ? 0.71376 0.68168 0.73963 0.12123  0.07064  0.17495  80  ILE A CB  
192  C CG1 . ILE A 63  ? 0.77971 0.71493 0.80687 0.12396  0.09890  0.16997  80  ILE A CG1 
193  C CG2 . ILE A 63  ? 0.72276 0.67866 0.71801 0.11906  0.06818  0.18028  80  ILE A CG2 
194  C CD1 . ILE A 63  ? 0.75017 0.67486 0.76579 0.10254  0.11263  0.14154  80  ILE A CD1 
195  N N   . TYR A 64  ? 0.74017 0.75431 0.78637 0.10364  0.03049  0.15877  81  TYR A N   
196  C CA  . TYR A 64  ? 0.75480 0.77259 0.79988 0.09443  0.00913  0.15317  81  TYR A CA  
197  C C   . TYR A 64  ? 0.71255 0.71310 0.74895 0.09009  0.01215  0.14217  81  TYR A C   
198  O O   . TYR A 64  ? 0.71914 0.70882 0.75806 0.07988  -0.00086 0.13480  81  TYR A O   
199  C CB  . TYR A 64  ? 0.74741 0.79412 0.83341 0.08971  -0.00463 0.16382  81  TYR A CB  
200  C CG  . TYR A 64  ? 0.73869 0.80880 0.82434 0.10327  -0.01508 0.17605  81  TYR A CG  
201  C CD1 . TYR A 64  ? 0.71023 0.79233 0.77172 0.10502  -0.03828 0.16966  81  TYR A CD1 
202  C CD2 . TYR A 64  ? 0.81779 0.89645 0.92070 0.12090  0.00002  0.19505  81  TYR A CD2 
203  C CE1 . TYR A 64  ? 0.85670 0.96364 0.90998 0.12676  -0.04674 0.18671  81  TYR A CE1 
204  C CE2 . TYR A 64  ? 0.81287 0.90753 0.91017 0.14294  -0.00584 0.21240  81  TYR A CE2 
205  C CZ  . TYR A 64  ? 0.87730 0.98855 0.94920 0.14726  -0.02948 0.21067  81  TYR A CZ  
206  O OH  . TYR A 64  ? 0.96410 1.09429 1.02289 0.17840  -0.03398 0.23381  81  TYR A OH  
207  N N   . ASP A 65  ? 0.76151 0.75876 0.78519 0.09992  0.02913  0.13921  82  ASP A N   
208  C CA  . ASP A 65  ? 0.74814 0.73207 0.75847 0.10851  0.03640  0.13667  82  ASP A CA  
209  C C   . ASP A 65  ? 0.77124 0.73896 0.80798 0.10055  0.03998  0.15100  82  ASP A C   
210  O O   . ASP A 65  ? 0.80966 0.74573 0.84051 0.09407  0.03624  0.14685  82  ASP A O   
211  C CB  . ASP A 65  ? 0.74159 0.71151 0.71820 0.11385  0.02896  0.12091  82  ASP A CB  
212  C CG  . ASP A 65  ? 0.76949 0.72569 0.72494 0.13490  0.03977  0.12170  82  ASP A CG  
213  O OD1 . ASP A 65  ? 0.86801 0.83382 0.82794 0.14752  0.05337  0.13390  82  ASP A OD1 
214  O OD2 . ASP A 65  ? 0.79351 0.72900 0.72243 0.14502  0.03640  0.11175  82  ASP A OD2 
215  N N   . THR A 66  ? 0.73450 0.72147 0.80260 0.09988  0.05116  0.16711  83  THR A N   
216  C CA  . THR A 66  ? 0.71210 0.69268 0.81576 0.08804  0.06136  0.18390  83  THR A CA  
217  C C   . THR A 66  ? 0.74457 0.73214 0.84857 0.10630  0.08932  0.20438  83  THR A C   
218  O O   . THR A 66  ? 0.74042 0.72343 0.87578 0.09676  0.10634  0.22420  83  THR A O   
219  C CB  . THR A 66  ? 0.66424 0.67817 0.81852 0.06805  0.04824  0.18683  83  THR A CB  
220  O OG1 . THR A 66  ? 0.74853 0.79424 0.90785 0.08368  0.05111  0.19279  83  THR A OG1 
221  C CG2 . THR A 66  ? 0.69327 0.70422 0.84127 0.05285  0.01939  0.16637  83  THR A CG2 
222  N N   . LEU A 67  ? 0.73010 0.80507 0.60135 0.01835  0.14911  0.24304  84  LEU A N   
223  C CA  . LEU A 67  ? 0.73942 0.82020 0.61134 0.01161  0.15429  0.23366  84  LEU A CA  
224  C C   . LEU A 67  ? 0.69121 0.76922 0.56851 -0.03244 0.11774  0.21834  84  LEU A C   
225  O O   . LEU A 67  ? 0.71768 0.73577 0.58722 -0.04965 0.11066  0.18971  84  LEU A O   
226  C CB  . LEU A 67  ? 0.78454 0.79009 0.63423 0.03175  0.18525  0.20539  84  LEU A CB  
227  C CG  . LEU A 67  ? 0.77409 0.77105 0.60515 0.03097  0.18671  0.19296  84  LEU A CG  
228  C CD1 . LEU A 67  ? 0.77516 0.85344 0.60984 0.05317  0.19804  0.23130  84  LEU A CD1 
229  C CD2 . LEU A 67  ? 0.82343 0.73539 0.62257 0.05416  0.20982  0.16642  84  LEU A CD2 
230  N N   . ASN A 68  ? 0.68219 0.82666 0.57798 -0.04968 0.09614  0.24163  85  ASN A N   
231  C CA  . ASN A 68  ? 0.68337 0.82390 0.58218 -0.08995 0.06333  0.22880  85  ASN A CA  
232  C C   . ASN A 68  ? 0.69851 0.80517 0.58053 -0.08809 0.07805  0.20423  85  ASN A C   
233  O O   . ASN A 68  ? 0.73765 0.85564 0.60795 -0.05825 0.10578  0.21238  85  ASN A O   
234  C CB  . ASN A 68  ? 0.64722 0.86775 0.57784 -0.11199 0.03292  0.26612  85  ASN A CB  
235  C CG  . ASN A 68  ? 0.62967 0.83903 0.56026 -0.15355 -0.00189 0.25375  85  ASN A CG  
236  O OD1 . ASN A 68  ? 0.70828 0.90212 0.63016 -0.15809 0.00694  0.23754  85  ASN A OD1 
237  N ND2 . ASN A 68  ? 0.68816 0.89774 0.62070 -0.18219 -0.04414 0.26072  85  ASN A ND2 
238  N N   . VAL A 69  ? 0.70645 0.76656 0.58086 -0.11665 0.05807  0.17514  86  VAL A N   
239  C CA  . VAL A 69  ? 0.70985 0.72335 0.56473 -0.11699 0.06397  0.14665  86  VAL A CA  
240  C C   . VAL A 69  ? 0.78162 0.83815 0.62887 -0.11569 0.06282  0.16122  86  VAL A C   
241  O O   . VAL A 69  ? 0.82417 0.85238 0.63854 -0.09124 0.08102  0.14994  86  VAL A O   
242  C CB  . VAL A 69  ? 0.73421 0.69725 0.59325 -0.14768 0.04149  0.11934  86  VAL A CB  
243  C CG1 . VAL A 69  ? 0.80898 0.74901 0.65527 -0.16100 0.02987  0.09893  86  VAL A CG1 
244  C CG2 . VAL A 69  ? 0.74117 0.64545 0.60530 -0.13451 0.05881  0.10361  86  VAL A CG2 
245  N N   . ASN A 70  ? 0.78045 0.90062 0.65391 -0.13910 0.04111  0.18912  87  ASN A N   
246  C CA  . ASN A 70  ? 0.76432 0.93604 0.64210 -0.13778 0.04316  0.21373  87  ASN A CA  
247  C C   . ASN A 70  ? 0.80020 1.02391 0.68036 -0.09382 0.07979  0.25059  87  ASN A C   
248  O O   . ASN A 70  ? 0.87394 1.13153 0.74769 -0.07771 0.09486  0.27298  87  ASN A O   
249  C CB  . ASN A 70  ? 0.69679 0.92035 0.61252 -0.17904 0.00635  0.23873  87  ASN A CB  
250  C CG  . ASN A 70  ? 0.73251 0.89910 0.63598 -0.21557 -0.02629 0.20487  87  ASN A CG  
251  O OD1 . ASN A 70  ? 0.73111 0.87083 0.61893 -0.23023 -0.03528 0.18549  87  ASN A OD1 
252  N ND2 . ASN A 70  ? 0.76770 0.91290 0.67292 -0.22532 -0.04231 0.19966  87  ASN A ND2 
253  N N   . ASP A 71  ? 0.85074 1.07795 0.73568 -0.06877 0.09846  0.25917  88  ASP A N   
254  C CA  . ASP A 71  ? 0.86563 1.14464 0.75539 -0.02233 0.13607  0.29877  88  ASP A CA  
255  C C   . ASP A 71  ? 0.95316 1.16887 0.77622 0.02521  0.17373  0.27767  88  ASP A C   
256  O O   . ASP A 71  ? 0.99195 1.12138 0.77604 0.03463  0.17875  0.23659  88  ASP A O   
257  C CB  . ASP A 71  ? 0.83565 1.12966 0.74685 -0.01162 0.14023  0.31125  88  ASP A CB  
258  C CG  . ASP A 71  ? 0.87612 1.24262 0.80766 0.03244  0.17442  0.36246  88  ASP A CG  
259  O OD1 . ASP A 71  ? 0.96985 1.38298 0.90545 0.05293  0.19492  0.39410  88  ASP A OD1 
260  O OD2 . ASP A 71  ? 0.84997 1.22851 0.79310 0.05050  0.18366  0.37494  88  ASP A OD2 
261  N N   . LYS A 72  ? 0.96320 1.21763 0.77109 0.05823  0.20013  0.30943  89  LYS A N   
262  C CA  . LYS A 72  ? 1.03635 1.21947 0.76054 0.11241  0.23501  0.29142  89  LYS A CA  
263  C C   . LYS A 72  ? 1.08735 1.27841 0.79224 0.17139  0.27999  0.31744  89  LYS A C   
264  O O   . LYS A 72  ? 1.13635 1.25228 0.75752 0.22292  0.30941  0.30112  89  LYS A O   
265  C CB  . LYS A 72  ? 1.04137 1.24655 0.73749 0.13173  0.24803  0.31263  89  LYS A CB  
266  C CG  . LYS A 72  ? 1.18637 1.43849 0.93177 0.07653  0.21121  0.31947  89  LYS A CG  
267  C CD  . LYS A 72  ? 1.18323 1.34327 0.87575 0.05134  0.18119  0.26139  89  LYS A CD  
268  C CE  . LYS A 72  ? 1.16184 1.37435 0.88804 0.01606  0.15960  0.28116  89  LYS A CE  
269  N NZ  . LYS A 72  ? 1.01403 1.15939 0.71813 -0.02544 0.11943  0.23050  89  LYS A NZ  
270  N N   . SER A 73  ? 1.04246 1.31407 0.81524 0.16688  0.28300  0.35621  90  SER A N   
271  C CA  . SER A 73  ? 0.95473 1.25304 0.71919 0.22585  0.32839  0.39218  90  SER A CA  
272  C C   . SER A 73  ? 1.06645 1.24272 0.74635 0.26270  0.34931  0.34580  90  SER A C   
273  O O   . SER A 73  ? 1.17435 1.31844 0.79141 0.32688  0.39188  0.35724  90  SER A O   
274  C CB  . SER A 73  ? 0.92393 1.30921 0.77398 0.20605  0.31361  0.42767  90  SER A CB  
275  O OG  . SER A 73  ? 0.89323 1.37011 0.82498 0.15619  0.27447  0.45932  90  SER A OG  
276  N N   . PHE A 74  ? 1.10232 1.20593 0.78100 0.22457  0.31935  0.29593  91  PHE A N   
277  C CA  . PHE A 74  ? 1.13516 1.13076 0.75578 0.25183  0.33470  0.25967  91  PHE A CA  
278  C C   . PHE A 74  ? 1.23167 1.10428 0.77242 0.25393  0.32171  0.20718  91  PHE A C   
279  O O   . PHE A 74  ? 1.24740 1.01733 0.75043 0.25966  0.31901  0.17065  91  PHE A O   
280  C CB  . PHE A 74  ? 1.04794 1.03164 0.71652 0.21532  0.31424  0.24272  91  PHE A CB  
281  C CG  . PHE A 74  ? 0.99595 1.08447 0.73152 0.21176  0.31678  0.28837  91  PHE A CG  
282  C CD1 . PHE A 74  ? 0.94675 1.12082 0.74353 0.16830  0.28366  0.31035  91  PHE A CD1 
283  C CD2 . PHE A 74  ? 0.99383 1.08956 0.72794 0.25184  0.34793  0.30965  91  PHE A CD2 
284  C CE1 . PHE A 74  ? 0.93412 1.19499 0.78809 0.16235  0.27514  0.35120  91  PHE A CE1 
285  C CE2 . PHE A 74  ? 0.92689 1.11729 0.72075 0.24877  0.34381  0.35217  91  PHE A CE2 
286  C CZ  . PHE A 74  ? 0.89722 1.16849 0.75040 0.20296  0.30428  0.37241  91  PHE A CZ  
287  N N   . GLY A 75  ? 1.22383 1.10189 0.73938 0.24890  0.31058  0.20460  92  GLY A N   
288  C CA  . GLY A 75  ? 1.21714 0.97844 0.65273 0.25006  0.29011  0.15525  92  GLY A CA  
289  C C   . GLY A 75  ? 1.21616 0.96848 0.69539 0.18173  0.23952  0.12281  92  GLY A C   
290  O O   . GLY A 75  ? 1.11545 0.93545 0.67810 0.13507  0.22151  0.13313  92  GLY A O   
291  N N   . ASP A 76  ? 1.23277 0.89127 0.64499 0.18071  0.21526  0.08301  93  ASP A N   
292  C CA  . ASP A 76  ? 1.26313 0.90875 0.70458 0.12427  0.16852  0.05417  93  ASP A CA  
293  C C   . ASP A 76  ? 1.29396 0.87109 0.77080 0.08614  0.13887  0.01890  93  ASP A C   
294  O O   . ASP A 76  ? 1.39458 0.87243 0.83459 0.07546  0.10698  -0.02011 93  ASP A O   
295  C CB  . ASP A 76  ? 1.38077 0.96206 0.73315 0.14498  0.15499  0.03300  93  ASP A CB  
296  C CG  . ASP A 76  ? 1.42792 1.03253 0.81509 0.09367  0.11521  0.01957  93  ASP A CG  
297  O OD1 . ASP A 76  ? 1.24318 0.94174 0.71605 0.05296  0.10963  0.04203  93  ASP A OD1 
298  O OD2 . ASP A 76  ? 1.58097 1.10192 0.90005 0.09741  0.08733  -0.01385 93  ASP A OD2 
299  N N   . TRP A 77  ? 1.18354 0.81602 0.73552 0.06714  0.14914  0.03759  94  TRP A N   
300  C CA  . TRP A 77  ? 1.15325 0.73540 0.75140 0.03524  0.13044  0.01620  94  TRP A CA  
301  C C   . TRP A 77  ? 1.15695 0.73743 0.79812 -0.01701 0.08986  -0.00242 94  TRP A C   
302  O O   . TRP A 77  ? 1.23219 0.73763 0.88277 -0.03858 0.06207  -0.02976 94  TRP A O   
303  C CB  . TRP A 77  ? 1.07404 0.71740 0.73131 0.03525  0.15493  0.04477  94  TRP A CB  
304  C CG  . TRP A 77  ? 1.05639 0.68391 0.68022 0.08377  0.19205  0.05918  94  TRP A CG  
305  C CD1 . TRP A 77  ? 1.09845 0.79308 0.70493 0.12317  0.22520  0.09425  94  TRP A CD1 
306  C CD2 . TRP A 77  ? 1.11863 0.65727 0.72590 0.09981  0.20074  0.04320  94  TRP A CD2 
307  N NE1 . TRP A 77  ? 1.17733 0.82926 0.75035 0.16708  0.25688  0.09963  94  TRP A NE1 
308  C CE2 . TRP A 77  ? 1.22004 0.77127 0.78953 0.15296  0.24196  0.06678  94  TRP A CE2 
309  C CE3 . TRP A 77  ? 1.14615 0.59728 0.77358 0.07382  0.17710  0.01573  94  TRP A CE3 
310  C CZ2 . TRP A 77  ? 1.23217 0.70296 0.77335 0.18194  0.26077  0.05943  94  TRP A CZ2 
311  C CZ3 . TRP A 77  ? 1.21550 0.58969 0.82350 0.09796  0.19266  0.01068  94  TRP A CZ3 
312  C CH2 . TRP A 77  ? 1.25969 0.63970 0.81973 0.15225  0.23453  0.03026  94  TRP A CH2 
313  N N   . PHE A 78  ? 1.09430 0.75683 0.76536 -0.03789 0.08449  0.01543  95  PHE A N   
314  C CA  . PHE A 78  ? 1.11550 0.78680 0.82651 -0.08342 0.05123  0.00383  95  PHE A CA  
315  C C   . PHE A 78  ? 1.17621 0.84178 0.83968 -0.08295 0.03339  -0.00686 95  PHE A C   
316  O O   . PHE A 78  ? 1.22888 0.92633 0.84927 -0.05162 0.05396  0.01086  95  PHE A O   
317  C CB  . PHE A 78  ? 1.01269 0.76564 0.77806 -0.10421 0.05562  0.03074  95  PHE A CB  
318  C CG  . PHE A 78  ? 0.92084 0.69776 0.70443 -0.08346 0.08405  0.05238  95  PHE A CG  
319  C CD1 . PHE A 78  ? 0.89042 0.62570 0.70359 -0.08603 0.09035  0.04614  95  PHE A CD1 
320  C CD2 . PHE A 78  ? 0.88101 0.72387 0.65648 -0.05966 0.10499  0.08327  95  PHE A CD2 
321  C CE1 . PHE A 78  ? 0.91055 0.66393 0.73398 -0.06318 0.11747  0.06623  95  PHE A CE1 
322  C CE2 . PHE A 78  ? 0.80991 0.67453 0.60036 -0.03903 0.12814  0.10367  95  PHE A CE2 
323  C CZ  . PHE A 78  ? 0.87799 0.69513 0.68672 -0.03947 0.13480  0.09320  95  PHE A CZ  
324  N N   . GLY A 79  ? 1.37007 0.99477 1.04176 -0.11341 -0.00259 -0.03199 96  GLY A N   
325  C CA  . GLY A 79  ? 1.44482 1.04548 1.06012 -0.10903 -0.02296 -0.04709 96  GLY A CA  
326  C C   . GLY A 79  ? 1.52152 1.01952 1.05490 -0.07792 -0.03380 -0.07587 96  GLY A C   
327  O O   . GLY A 79  ? 1.45230 0.92492 0.93779 -0.03627 -0.00576 -0.07063 96  GLY A O   
328  N N   . ASN A 80  ? 1.79346 1.22601 1.30419 -0.09579 -0.07727 -0.10605 97  ASN A N   
329  C CA  . ASN A 80  ? 1.96397 1.27845 1.38849 -0.07088 -0.10211 -0.13883 97  ASN A CA  
330  C C   . ASN A 80  ? 1.93273 1.22772 1.24445 -0.02366 -0.09138 -0.14019 97  ASN A C   
331  O O   . ASN A 80  ? 1.84173 1.22374 1.15828 -0.01439 -0.06337 -0.11132 97  ASN A O   
332  C CB  . ASN A 80  ? 2.02678 1.27694 1.48623 -0.11428 -0.16175 -0.16775 97  ASN A CB  
333  C CG  . ASN A 80  ? 1.93111 1.22251 1.40917 -0.14218 -0.18776 -0.16888 97  ASN A CG  
334  O OD1 . ASN A 80  ? 1.95489 1.21624 1.34811 -0.12012 -0.20082 -0.18138 97  ASN A OD1 
335  N ND2 . ASN A 80  ? 1.82360 1.18205 1.40599 -0.18530 -0.19128 -0.15325 97  ASN A ND2 
336  N N   . SER A 81  ? 2.05867 1.23264 1.26377 0.00967  -0.11369 -0.17119 98  SER A N   
337  C CA  . SER A 81  ? 2.10280 1.23604 1.18394 0.05981  -0.10874 -0.17623 98  SER A CA  
338  C C   . SER A 81  ? 2.20983 1.26161 1.24563 0.03963  -0.17336 -0.21368 98  SER A C   
339  O O   . SER A 81  ? 2.18728 1.18018 1.10251 0.08388  -0.17850 -0.22472 98  SER A O   
340  C CB  . SER A 81  ? 2.11820 1.16588 1.08137 0.12970  -0.07953 -0.18009 98  SER A CB  
341  O OG  . SER A 81  ? 2.13170 1.10744 0.95301 0.18567  -0.08056 -0.19072 98  SER A OG  
342  N N   . ALA A 82  ? 2.29792 1.34803 1.42967 -0.02354 -0.22164 -0.22923 99  ALA A N   
343  C CA  . ALA A 82  ? 2.26695 1.31404 1.43346 -0.05237 -0.27396 -0.24100 99  ALA A CA  
344  C C   . ALA A 82  ? 2.20288 1.32784 1.38743 -0.06894 -0.26937 -0.22761 99  ALA A C   
345  O O   . ALA A 82  ? 2.14195 1.28909 1.36994 -0.08693 -0.30065 -0.22825 99  ALA A O   
346  C CB  . ALA A 82  ? 2.19110 1.27661 1.50625 -0.10321 -0.30045 -0.23518 99  ALA A CB  
347  N N   . LEU A 83  ? 2.03816 1.24740 1.23196 -0.06009 -0.21851 -0.19840 100 LEU A N   
348  C CA  . LEU A 83  ? 1.80767 1.10443 1.02113 -0.06845 -0.20392 -0.17466 100 LEU A CA  
349  C C   . LEU A 83  ? 1.79685 1.13694 0.94446 -0.01437 -0.14898 -0.14292 100 LEU A C   
350  O O   . LEU A 83  ? 1.81539 1.21755 0.96583 -0.01458 -0.13666 -0.12036 100 LEU A O   
351  C CB  . LEU A 83  ? 1.59925 1.00203 0.94644 -0.12008 -0.19237 -0.14942 100 LEU A CB  
352  C CG  . LEU A 83  ? 1.59842 1.00392 1.02461 -0.17407 -0.23664 -0.16207 100 LEU A CG  
353  C CD1 . LEU A 83  ? 1.79704 1.17078 1.29258 -0.18473 -0.25425 -0.17293 100 LEU A CD1 
354  C CD2 . LEU A 83  ? 1.34356 0.85251 0.86117 -0.20551 -0.21293 -0.13095 100 LEU A CD2 
355  N N   . LYS A 84  ? 1.86718 1.17809 0.96045 0.03306  -0.11415 -0.13596 101 LYS A N   
356  C CA  . LYS A 84  ? 1.91798 1.29358 0.97806 0.08419  -0.05254 -0.09190 101 LYS A CA  
357  C C   . LYS A 84  ? 1.99451 1.36350 0.96839 0.12199  -0.04450 -0.08101 101 LYS A C   
358  O O   . LYS A 84  ? 1.92252 1.39433 0.93518 0.12744  -0.00701 -0.03404 101 LYS A O   
359  C CB  . LYS A 84  ? 2.05919 1.37257 1.04945 0.13858  -0.02320 -0.09385 101 LYS A CB  
360  C CG  . LYS A 84  ? 2.04162 1.42119 1.00330 0.19911  0.04565  -0.04220 101 LYS A CG  
361  C CD  . LYS A 84  ? 2.09199 1.39096 0.97598 0.25441  0.07016  -0.05030 101 LYS A CD  
362  C CE  . LYS A 84  ? 2.20997 1.34036 0.92942 0.30330  0.04105  -0.09684 101 LYS A CE  
363  N NZ  . LYS A 84  ? 2.16766 1.27916 0.77169 0.36687  0.06537  -0.07967 101 LYS A NZ  
364  N N   . ASP A 85  ? 2.18359 1.43010 1.04167 0.14725  -0.08272 -0.12191 102 ASP A N   
365  C CA  . ASP A 85  ? 2.23339 1.45902 0.99237 0.19088  -0.07560 -0.11369 102 ASP A CA  
366  C C   . ASP A 85  ? 2.24540 1.41246 0.98467 0.15608  -0.14206 -0.15314 102 ASP A C   
367  O O   . ASP A 85  ? 2.28055 1.42346 0.95116 0.19191  -0.14198 -0.14974 102 ASP A O   
368  C CB  . ASP A 85  ? 2.39264 1.51354 0.98700 0.28143  -0.04890 -0.11824 102 ASP A CB  
369  C CG  . ASP A 85  ? 2.36754 1.56705 0.97661 0.32923  0.02883  -0.06346 102 ASP A CG  
370  O OD1 . ASP A 85  ? 2.21128 1.55457 0.95347 0.29313  0.05953  -0.01708 102 ASP A OD1 
371  O OD2 . ASP A 85  ? 2.46062 1.58894 0.98298 0.39623  0.05439  -0.06326 102 ASP A OD2 
372  N N   . LYS A 86  ? 2.05216 1.21384 0.88363 0.08810  -0.19337 -0.18142 103 LYS A N   
373  C CA  . LYS A 86  ? 1.88461 1.04769 0.77028 0.04779  -0.24378 -0.19748 103 LYS A CA  
374  C C   . LYS A 86  ? 1.72690 0.97961 0.63344 0.03438  -0.22385 -0.16789 103 LYS A C   
375  O O   . LYS A 86  ? 1.61410 0.97213 0.60951 0.01045  -0.18664 -0.13196 103 LYS A O   
376  C CB  . LYS A 86  ? 1.83946 1.02148 0.86178 -0.01812 -0.28237 -0.21128 103 LYS A CB  
377  C CG  . LYS A 86  ? 1.90305 1.04483 0.96274 -0.03248 -0.33380 -0.22901 103 LYS A CG  
378  C CD  . LYS A 86  ? 1.83033 1.02835 1.04418 -0.09012 -0.35360 -0.22465 103 LYS A CD  
379  C CE  . LYS A 86  ? 1.70660 1.01170 1.02035 -0.12772 -0.33715 -0.20223 103 LYS A CE  
380  N NZ  . LYS A 86  ? 1.56775 0.92916 1.01985 -0.16681 -0.34878 -0.19306 103 LYS A NZ  
381  N N   . THR A 87  ? 1.62321 0.99547 0.68339 0.04179  -0.17521 0.03982  104 THR A N   
382  C CA  . THR A 87  ? 1.42797 0.88955 0.56245 0.06097  -0.16820 0.06558  104 THR A CA  
383  C C   . THR A 87  ? 1.28494 0.86763 0.57083 0.01548  -0.20357 0.07277  104 THR A C   
384  O O   . THR A 87  ? 1.32823 0.90508 0.60074 -0.03282 -0.26184 0.07591  104 THR A O   
385  C CB  . THR A 87  ? 1.40900 0.83050 0.48047 0.07238  -0.17530 0.07437  104 THR A CB  
386  O OG1 . THR A 87  ? 1.62882 0.97079 0.61868 0.12562  -0.12060 0.07121  104 THR A OG1 
387  C CG2 . THR A 87  ? 1.31559 0.83192 0.47208 0.08203  -0.17912 0.10409  104 THR A CG2 
388  N N   . TYR A 88  ? 1.18206 0.87162 0.61093 0.03016  -0.16824 0.07981  105 TYR A N   
389  C CA  . TYR A 88  ? 1.01095 0.80208 0.57363 -0.00292 -0.18922 0.08836  105 TYR A CA  
390  C C   . TYR A 88  ? 0.92622 0.80503 0.60555 0.02216  -0.15067 0.10213  105 TYR A C   
391  O O   . TYR A 88  ? 0.94194 0.81477 0.61679 0.05792  -0.11020 0.10421  105 TYR A O   
392  C CB  . TYR A 88  ? 0.89534 0.69454 0.49023 -0.02893 -0.19648 0.07218  105 TYR A CB  
393  C CG  . TYR A 88  ? 0.91077 0.72645 0.54375 -0.00334 -0.14945 0.05816  105 TYR A CG  
394  C CD1 . TYR A 88  ? 0.81983 0.71815 0.56650 0.00770  -0.12161 0.06413  105 TYR A CD1 
395  C CD2 . TYR A 88  ? 1.08866 0.83100 0.63732 0.00768  -0.13504 0.04135  105 TYR A CD2 
396  C CE1 . TYR A 88  ? 0.84275 0.75664 0.62077 0.02310  -0.08869 0.05452  105 TYR A CE1 
397  C CE2 . TYR A 88  ? 0.99259 0.76202 0.58392 0.02951  -0.09566 0.03599  105 TYR A CE2 
398  C CZ  . TYR A 88  ? 0.87954 0.73814 0.58707 0.03391  -0.07694 0.04305  105 TYR A CZ  
399  O OH  . TYR A 88  ? 0.87203 0.75927 0.62003 0.04806  -0.04766 0.04122  105 TYR A OH  
400  N N   . LEU A 89  ? 0.81189 0.76842 0.59394 0.00258  -0.16345 0.11687  106 LEU A N   
401  C CA  . LEU A 89  ? 0.67957 0.70530 0.56380 0.02009  -0.13203 0.13109  106 LEU A CA  
402  C C   . LEU A 89  ? 0.63669 0.72273 0.61363 -0.00066 -0.13837 0.13936  106 LEU A C   
403  O O   . LEU A 89  ? 0.70885 0.82681 0.71055 -0.02008 -0.16911 0.16391  106 LEU A O   
404  C CB  . LEU A 89  ? 0.65563 0.69410 0.53657 0.03521  -0.13438 0.15675  106 LEU A CB  
405  C CG  . LEU A 89  ? 0.61013 0.70500 0.58845 0.05352  -0.09790 0.17091  106 LEU A CG  
406  C CD1 . LEU A 89  ? 0.65287 0.74019 0.65265 0.06632  -0.06134 0.15297  106 LEU A CD1 
407  C CD2 . LEU A 89  ? 0.57067 0.67790 0.55047 0.07442  -0.09097 0.19762  106 LEU A CD2 
408  N N   . TYR A 90  ? 0.57477 0.67736 0.60225 0.00494  -0.10903 0.12527  107 TYR A N   
409  C CA  . TYR A 90  ? 0.53849 0.68187 0.63510 -0.00742 -0.10790 0.13324  107 TYR A CA  
410  C C   . TYR A 90  ? 0.52321 0.67979 0.67295 0.01057  -0.06746 0.12910  107 TYR A C   
411  O O   . TYR A 90  ? 0.54271 0.67597 0.67588 0.02032  -0.04857 0.11188  107 TYR A O   
412  C CB  . TYR A 90  ? 0.50722 0.62899 0.57591 -0.02796 -0.12471 0.11546  107 TYR A CB  
413  C CG  . TYR A 90  ? 0.50591 0.67028 0.63907 -0.04227 -0.13001 0.13340  107 TYR A CG  
414  C CD1 . TYR A 90  ? 0.52076 0.70005 0.70177 -0.02819 -0.09519 0.12827  107 TYR A CD1 
415  C CD2 . TYR A 90  ? 0.46383 0.65172 0.60841 -0.06980 -0.17003 0.16121  107 TYR A CD2 
416  C CE1 . TYR A 90  ? 0.52038 0.73544 0.75730 -0.03228 -0.09084 0.15072  107 TYR A CE1 
417  C CE2 . TYR A 90  ? 0.48188 0.72135 0.70101 -0.07988 -0.17075 0.18994  107 TYR A CE2 
418  C CZ  . TYR A 90  ? 0.53598 0.78885 0.80129 -0.05629 -0.12609 0.18525  107 TYR A CZ  
419  O OH  . TYR A 90  ? 0.52948 0.83009 0.86572 -0.05691 -0.11708 0.21956  107 TYR A OH  
420  N N   . ALA A 91  ? 0.55815 0.74783 0.76807 0.01521  -0.05410 0.15048  108 ALA A N   
421  C CA  . ALA A 91  ? 0.53879 0.71680 0.77751 0.03268  -0.01503 0.14711  108 ALA A CA  
422  C C   . ALA A 91  ? 0.55453 0.73509 0.81811 0.03441  0.00067  0.14889  108 ALA A C   
423  O O   . ALA A 91  ? 0.55665 0.77855 0.85979 0.03363  -0.00621 0.18010  108 ALA A O   
424  C CB  . ALA A 91  ? 0.51457 0.70941 0.78684 0.05202  0.00331  0.17721  108 ALA A CB  
425  N N   . MET A 92  ? 0.46166 0.59935 0.70241 0.03668  0.02095  0.12107  109 MET A N   
426  C CA  . MET A 92  ? 0.44143 0.56820 0.68729 0.04229  0.03837  0.11950  109 MET A CA  
427  C C   . MET A 92  ? 0.52201 0.58480 0.73569 0.05332  0.06959  0.10045  109 MET A C   
428  O O   . MET A 92  ? 0.54788 0.57761 0.73410 0.04340  0.06570  0.08010  109 MET A O   
429  C CB  . MET A 92  ? 0.47423 0.60390 0.69928 0.02372  0.01591  0.09915  109 MET A CB  
430  C CG  . MET A 92  ? 0.52685 0.62064 0.70567 0.01326  0.01019  0.06296  109 MET A CG  
431  S SD  . MET A 92  ? 0.56844 0.65800 0.72522 0.00242  0.00037  0.04449  109 MET A SD  
432  C CE  . MET A 92  ? 0.51857 0.61709 0.70900 0.01795  0.02498  0.06736  109 MET A CE  
433  N N   . ASP A 93  ? 0.62081 0.66181 0.83373 0.07311  0.09987  0.11122  110 ASP A N   
434  C CA  . ASP A 93  ? 0.67920 0.63567 0.83383 0.08265  0.12769  0.08958  110 ASP A CA  
435  C C   . ASP A 93  ? 0.72538 0.66011 0.83885 0.06315  0.10935  0.05560  110 ASP A C   
436  O O   . ASP A 93  ? 0.70835 0.67422 0.83703 0.06533  0.10626  0.06078  110 ASP A O   
437  C CB  . ASP A 93  ? 0.74670 0.68226 0.90625 0.12129  0.17472  0.12093  110 ASP A CB  
438  C CG  . ASP A 93  ? 0.82992 0.76699 1.01619 0.14673  0.20300  0.15541  110 ASP A CG  
439  O OD1 . ASP A 93  ? 0.88455 0.80753 1.06215 0.13237  0.18958  0.14275  110 ASP A OD1 
440  O OD2 . ASP A 93  ? 0.88374 0.84575 1.10846 0.18258  0.23944  0.20200  110 ASP A OD2 
441  N N   . LEU A 94  ? 0.69189 0.57676 0.75768 0.04261  0.09606  0.02620  111 LEU A N   
442  C CA  . LEU A 94  ? 0.65228 0.52163 0.68087 0.02450  0.07753  -0.00006 111 LEU A CA  
443  C C   . LEU A 94  ? 0.76515 0.56285 0.73453 0.04213  0.10485  -0.00822 111 LEU A C   
444  O O   . LEU A 94  ? 0.83682 0.55734 0.75995 0.05864  0.13361  -0.00651 111 LEU A O   
445  C CB  . LEU A 94  ? 0.60685 0.45672 0.61323 -0.00620 0.05057  -0.01745 111 LEU A CB  
446  C CG  . LEU A 94  ? 0.55471 0.47048 0.60985 -0.01771 0.02886  -0.00672 111 LEU A CG  
447  C CD1 . LEU A 94  ? 0.56945 0.47851 0.61284 -0.04628 0.00456  -0.01373 111 LEU A CD1 
448  C CD2 . LEU A 94  ? 0.51026 0.48638 0.59220 -0.01133 0.01961  -0.00151 111 LEU A CD2 
449  N N   . LEU A 95  ? 0.78385 0.59765 0.74545 0.04242  0.09980  -0.01573 112 LEU A N   
450  C CA  . LEU A 95  ? 0.78104 0.52085 0.67102 0.05745  0.12142  -0.02756 112 LEU A CA  
451  C C   . LEU A 95  ? 0.87860 0.52235 0.67956 0.03552  0.10796  -0.05572 112 LEU A C   
452  O O   . LEU A 95  ? 0.87484 0.53491 0.68845 0.00157  0.07361  -0.06438 112 LEU A O   
453  C CB  . LEU A 95  ? 0.77697 0.55804 0.67617 0.05299  0.10849  -0.03353 112 LEU A CB  
454  C CG  . LEU A 95  ? 0.73358 0.53892 0.66171 0.08511  0.14065  -0.00769 112 LEU A CG  
455  C CD1 . LEU A 95  ? 0.70443 0.53654 0.62989 0.07591  0.12536  -0.01833 112 LEU A CD1 
456  C CD2 . LEU A 95  ? 0.90772 0.62148 0.76815 0.12262  0.18854  -0.00058 112 LEU A CD2 
457  N N   . ASP A 96  ? 1.06218 0.60145 0.76830 0.05296  0.13294  -0.06672 113 ASP A N   
458  C CA  . ASP A 96  ? 1.12861 0.56178 0.73247 0.02234  0.10943  -0.09499 113 ASP A CA  
459  C C   . ASP A 96  ? 1.09774 0.58060 0.71206 -0.02044 0.05628  -0.10971 113 ASP A C   
460  O O   . ASP A 96  ? 1.06624 0.61293 0.71265 -0.01262 0.05313  -0.10719 113 ASP A O   
461  C CB  . ASP A 96  ? 1.25275 0.54951 0.72974 0.05148  0.14544  -0.10590 113 ASP A CB  
462  C CG  . ASP A 96  ? 1.43276 0.61224 0.78570 0.00954  0.10711  -0.13836 113 ASP A CG  
463  O OD1 . ASP A 96  ? 1.50118 0.58018 0.78768 -0.00897 0.10243  -0.14770 113 ASP A OD1 
464  O OD2 . ASP A 96  ? 1.42996 0.61531 0.74963 -0.00697 0.07965  -0.15198 113 ASP A OD2 
465  N N   . TYR A 97  ? 1.04887 0.50547 0.64129 -0.06580 0.01534  -0.11897 114 TYR A N   
466  C CA  . TYR A 97  ? 0.97038 0.50904 0.61041 -0.10416 -0.03315 -0.11571 114 TYR A CA  
467  C C   . TYR A 97  ? 1.03146 0.55526 0.61622 -0.10907 -0.04850 -0.12779 114 TYR A C   
468  O O   . TYR A 97  ? 0.97100 0.58737 0.61505 -0.10321 -0.05463 -0.11856 114 TYR A O   
469  C CB  . TYR A 97  ? 1.01286 0.52880 0.64832 -0.15354 -0.07366 -0.11213 114 TYR A CB  
470  C CG  . TYR A 97  ? 1.00729 0.59788 0.68219 -0.19467 -0.12427 -0.09885 114 TYR A CG  
471  C CD1 . TYR A 97  ? 0.89139 0.61073 0.67276 -0.18679 -0.12660 -0.07429 114 TYR A CD1 
472  C CD2 . TYR A 97  ? 1.06032 0.58684 0.65807 -0.24001 -0.16930 -0.10646 114 TYR A CD2 
473  C CE1 . TYR A 97  ? 0.85185 0.64238 0.67239 -0.21583 -0.16414 -0.05227 114 TYR A CE1 
474  C CE2 . TYR A 97  ? 0.97788 0.58553 0.62279 -0.27668 -0.21570 -0.08336 114 TYR A CE2 
475  C CZ  . TYR A 97  ? 0.88905 0.63280 0.65045 -0.26087 -0.20890 -0.05372 114 TYR A CZ  
476  O OH  . TYR A 97  ? 0.95203 0.78073 0.76475 -0.28988 -0.24743 -0.02096 114 TYR A OH  
477  N N   . ASN A 98  ? 1.13999 0.53802 0.60027 -0.11817 -0.05364 -0.14813 115 ASN A N   
478  C CA  . ASN A 98  ? 1.15497 0.53423 0.55309 -0.12139 -0.06921 -0.15854 115 ASN A CA  
479  C C   . ASN A 98  ? 1.14216 0.57450 0.57797 -0.07013 -0.02516 -0.15231 115 ASN A C   
480  O O   . ASN A 98  ? 1.11759 0.61794 0.58301 -0.07152 -0.03877 -0.14754 115 ASN A O   
481  C CB  . ASN A 98  ? 1.30247 0.52239 0.54471 -0.12923 -0.07326 -0.18020 115 ASN A CB  
482  C CG  . ASN A 98  ? 1.37861 0.55664 0.59837 -0.17877 -0.11490 -0.17650 115 ASN A CG  
483  O OD1 . ASN A 98  ? 1.48159 0.60768 0.69330 -0.17452 -0.09551 -0.17681 115 ASN A OD1 
484  N ND2 . ASN A 98  ? 1.42735 0.63146 0.64198 -0.22592 -0.17172 -0.16785 115 ASN A ND2 
485  N N   . ASN A 99  ? 1.17515 0.57744 0.61239 -0.02473 0.02856  -0.14672 116 ASN A N   
486  C CA  . ASN A 99  ? 1.11868 0.57852 0.60619 0.01930  0.06829  -0.13149 116 ASN A CA  
487  C C   . ASN A 99  ? 0.98044 0.57896 0.59081 0.00814  0.04977  -0.11667 116 ASN A C   
488  O O   . ASN A 99  ? 0.94552 0.59251 0.57681 0.01546  0.04906  -0.11303 116 ASN A O   
489  C CB  . ASN A 99  ? 1.17712 0.59928 0.66717 0.06590  0.12570  -0.11421 116 ASN A CB  
490  C CG  . ASN A 99  ? 1.19086 0.69376 0.76158 0.10422  0.16160  -0.08576 116 ASN A CG  
491  O OD1 . ASN A 99  ? 1.20428 0.75327 0.84893 0.12591  0.18853  -0.05782 116 ASN A OD1 
492  N ND2 . ASN A 99  ? 1.10860 0.63498 0.67195 0.10904  0.15846  -0.08806 116 ASN A ND2 
493  N N   . TYR A 100 ? 0.93318 0.58524 0.61354 -0.00902 0.03527  -0.10812 117 TYR A N   
494  C CA  . TYR A 100 ? 0.82557 0.58669 0.59997 -0.01609 0.02084  -0.09462 117 TYR A CA  
495  C C   . TYR A 100 ? 0.77345 0.57246 0.54548 -0.03804 -0.01106 -0.09768 117 TYR A C   
496  O O   . TYR A 100 ? 0.67150 0.52801 0.48136 -0.02783 -0.00723 -0.08998 117 TYR A O   
497  C CB  . TYR A 100 ? 0.74001 0.53508 0.56888 -0.02884 0.01110  -0.08485 117 TYR A CB  
498  C CG  . TYR A 100 ? 0.63706 0.52131 0.53747 -0.03219 -0.00094 -0.07176 117 TYR A CG  
499  C CD1 . TYR A 100 ? 0.61300 0.53572 0.55746 -0.01350 0.01523  -0.05992 117 TYR A CD1 
500  C CD2 . TYR A 100 ? 0.60980 0.53359 0.52768 -0.05368 -0.02810 -0.06647 117 TYR A CD2 
501  C CE1 . TYR A 100 ? 0.54379 0.52101 0.52643 -0.01709 0.00366  -0.05135 117 TYR A CE1 
502  C CE2 . TYR A 100 ? 0.59288 0.57790 0.55594 -0.04779 -0.03000 -0.05311 117 TYR A CE2 
503  C CZ  . TYR A 100 ? 0.51137 0.51214 0.49597 -0.03000 -0.01458 -0.04975 117 TYR A CZ  
504  O OH  . TYR A 100 ? 0.51145 0.54663 0.51493 -0.02519 -0.01745 -0.04012 117 TYR A OH  
505  N N   . LEU A 101 ? 0.80330 0.56866 0.53020 -0.06988 -0.04381 -0.10447 118 LEU A N   
506  C CA  . LEU A 101 ? 0.76594 0.58139 0.50270 -0.09229 -0.07690 -0.09567 118 LEU A CA  
507  C C   . LEU A 101 ? 0.81930 0.63765 0.52817 -0.07183 -0.06466 -0.09981 118 LEU A C   
508  O O   . LEU A 101 ? 0.78250 0.67054 0.53225 -0.06909 -0.07037 -0.08547 118 LEU A O   
509  C CB  . LEU A 101 ? 0.81435 0.58205 0.49638 -0.13565 -0.11992 -0.09803 118 LEU A CB  
510  C CG  . LEU A 101 ? 0.85029 0.65307 0.58001 -0.17385 -0.15378 -0.07819 118 LEU A CG  
511  C CD1 . LEU A 101 ? 0.88283 0.66897 0.57052 -0.22203 -0.20717 -0.06940 118 LEU A CD1 
512  C CD2 . LEU A 101 ? 0.80062 0.71436 0.63247 -0.16134 -0.14614 -0.05002 118 LEU A CD2 
513  N N   . SER A 102 ? 0.81982 0.55725 0.45384 -0.05304 -0.04313 -0.11600 119 SER A N   
514  C CA  . SER A 102 ? 0.79585 0.52367 0.38861 -0.03551 -0.03387 -0.11887 119 SER A CA  
515  C C   . SER A 102 ? 0.76002 0.53750 0.41067 0.00000  0.00400  -0.10830 119 SER A C   
516  O O   . SER A 102 ? 0.81956 0.59742 0.44744 0.01715  0.01578  -0.10669 119 SER A O   
517  C CB  . SER A 102 ? 0.91843 0.52525 0.38993 -0.02646 -0.02396 -0.13754 119 SER A CB  
518  O OG  . SER A 102 ? 0.98214 0.54059 0.44687 0.00675  0.02135  -0.13815 119 SER A OG  
519  N N   . ILE A 103 ? 0.72845 0.54460 0.44983 0.00849  0.02022  -0.09873 120 ILE A N   
520  C CA  . ILE A 103 ? 0.68004 0.53967 0.45628 0.03116  0.04622  -0.08488 120 ILE A CA  
521  C C   . ILE A 103 ? 0.57978 0.50599 0.42576 0.01933  0.03348  -0.07487 120 ILE A C   
522  O O   . ILE A 103 ? 0.54882 0.50320 0.43094 0.02850  0.04533  -0.06417 120 ILE A O   
523  C CB  . ILE A 103 ? 0.66889 0.49950 0.45264 0.05867  0.08355  -0.07396 120 ILE A CB  
524  C CG1 . ILE A 103 ? 0.72836 0.55798 0.54159 0.05245  0.08281  -0.06965 120 ILE A CG1 
525  C CG2 . ILE A 103 ? 0.70583 0.45501 0.40333 0.08271  0.10823  -0.08039 120 ILE A CG2 
526  C CD1 . ILE A 103 ? 0.70998 0.50768 0.52507 0.08419  0.12343  -0.05122 120 ILE A CD1 
527  N N   . GLU A 104 ? 0.60409 0.54911 0.46344 -0.00118 0.00958  -0.07558 121 GLU A N   
528  C CA  . GLU A 104 ? 0.56158 0.55350 0.46951 -0.00514 0.00364  -0.06484 121 GLU A CA  
529  C C   . GLU A 104 ? 0.62695 0.64540 0.53710 0.00230  0.00651  -0.05789 121 GLU A C   
530  O O   . GLU A 104 ? 0.60838 0.63303 0.53553 0.00839  0.01523  -0.05281 121 GLU A O   
531  C CB  . GLU A 104 ? 0.55325 0.56151 0.47395 -0.02249 -0.01663 -0.05994 121 GLU A CB  
532  C CG  . GLU A 104 ? 0.61139 0.65392 0.56633 -0.01860 -0.01616 -0.04719 121 GLU A CG  
533  C CD  . GLU A 104 ? 0.66895 0.74265 0.64063 -0.02761 -0.02990 -0.03051 121 GLU A CD  
534  O OE1 . GLU A 104 ? 0.66124 0.76060 0.63032 -0.02915 -0.03662 -0.01761 121 GLU A OE1 
535  O OE2 . GLU A 104 ? 0.64309 0.72236 0.63605 -0.03074 -0.03208 -0.02373 121 GLU A OE2 
536  N N   . ASN A 105 ? 0.63411 0.66408 0.52288 0.00004  -0.00257 -0.05462 122 ASN A N   
537  C CA  . ASN A 105 ? 0.58946 0.64262 0.47807 0.01287  0.00628  -0.04335 122 ASN A CA  
538  C C   . ASN A 105 ? 0.61925 0.65201 0.49938 0.02722  0.02707  -0.04808 122 ASN A C   
539  O O   . ASN A 105 ? 0.66072 0.69358 0.54850 0.03365  0.03718  -0.04191 122 ASN A O   
540  C CB  . ASN A 105 ? 0.58537 0.66412 0.45908 0.00924  -0.00735 -0.03102 122 ASN A CB  
541  C CG  . ASN A 105 ? 0.61440 0.73720 0.50920 0.02073  -0.00175 -0.00391 122 ASN A CG  
542  O OD1 . ASN A 105 ? 0.62518 0.75709 0.54021 0.02410  0.00284  0.00546  122 ASN A OD1 
543  N ND2 . ASN A 105 ? 0.66926 0.81171 0.55254 0.03421  0.00562  0.01087  122 ASN A ND2 
544  N N   . PRO A 106 ? 0.61523 0.62285 0.47342 0.03359  0.03577  -0.05570 123 PRO A N   
545  C CA  . PRO A 106 ? 0.56315 0.56104 0.42534 0.04919  0.05885  -0.05079 123 PRO A CA  
546  C C   . PRO A 106 ? 0.59175 0.59224 0.49551 0.04364  0.06350  -0.04340 123 PRO A C   
547  O O   . PRO A 106 ? 0.62356 0.62465 0.53770 0.04327  0.06908  -0.03499 123 PRO A O   
548  C CB  . PRO A 106 ? 0.57644 0.53980 0.40334 0.06191  0.07163  -0.05629 123 PRO A CB  
549  C CG  . PRO A 106 ? 0.60634 0.55589 0.39008 0.04990  0.04919  -0.06706 123 PRO A CG  
550  C CD  . PRO A 106 ? 0.60848 0.58408 0.42606 0.02904  0.02770  -0.06640 123 PRO A CD  
551  N N   . ILE A 107 ? 0.56818 0.56684 0.49252 0.03644  0.05833  -0.04392 124 ILE A N   
552  C CA  . ILE A 107 ? 0.56210 0.57082 0.53093 0.02853  0.05803  -0.02951 124 ILE A CA  
553  C C   . ILE A 107 ? 0.62817 0.63929 0.59743 0.01185  0.03919  -0.02988 124 ILE A C   
554  O O   . ILE A 107 ? 0.62162 0.62771 0.60516 0.00012  0.03389  -0.01839 124 ILE A O   
555  C CB  . ILE A 107 ? 0.53903 0.54728 0.52745 0.02992  0.06034  -0.02532 124 ILE A CB  
556  C CG1 . ILE A 107 ? 0.58467 0.56785 0.55488 0.05389  0.08835  -0.02092 124 ILE A CG1 
557  C CG2 . ILE A 107 ? 0.51204 0.54432 0.55363 0.01804  0.05276  -0.00333 124 ILE A CG2 
558  C CD1 . ILE A 107 ? 0.58820 0.56542 0.58100 0.06432  0.10316  -0.00596 124 ILE A CD1 
559  N N   . ILE A 108 ? 0.62904 0.64072 0.57622 0.01033  0.02899  -0.03956 125 ILE A N   
560  C CA  . ILE A 108 ? 0.70509 0.70276 0.63408 0.00357  0.01907  -0.03802 125 ILE A CA  
561  C C   . ILE A 108 ? 0.74210 0.71601 0.63723 0.01112  0.02972  -0.03601 125 ILE A C   
562  O O   . ILE A 108 ? 0.81913 0.75625 0.69150 0.00094  0.02417  -0.03342 125 ILE A O   
563  C CB  . ILE A 108 ? 0.67004 0.67851 0.59007 0.00733  0.01342  -0.03941 125 ILE A CB  
564  C CG1 . ILE A 108 ? 0.66748 0.68929 0.61748 -0.00148 0.00398  -0.04070 125 ILE A CG1 
565  C CG2 . ILE A 108 ? 0.74130 0.72102 0.62593 0.01004  0.01202  -0.03512 125 ILE A CG2 
566  C CD1 . ILE A 108 ? 0.67534 0.69162 0.64635 -0.01334 -0.00496 -0.03419 125 ILE A CD1 
567  N N   . LYS A 109 ? 0.69109 0.67885 0.57540 0.02735  0.04332  -0.03563 126 LYS A N   
568  C CA  . LYS A 109 ? 0.70626 0.67282 0.55862 0.04028  0.05924  -0.02984 126 LYS A CA  
569  C C   . LYS A 109 ? 0.71690 0.65900 0.57567 0.03098  0.06341  -0.02735 126 LYS A C   
570  O O   . LYS A 109 ? 0.77110 0.66762 0.59735 0.02585  0.06559  -0.02450 126 LYS A O   
571  C CB  . LYS A 109 ? 0.64917 0.64721 0.49690 0.05840  0.06974  -0.02373 126 LYS A CB  
572  C CG  . LYS A 109 ? 0.69955 0.68142 0.51366 0.07881  0.09008  -0.01044 126 LYS A CG  
573  C CD  . LYS A 109 ? 0.70636 0.73286 0.52173 0.09712  0.09579  0.00899  126 LYS A CD  
574  C CE  . LYS A 109 ? 0.69905 0.76151 0.52953 0.09181  0.08402  0.00658  126 LYS A CE  
575  N NZ  . LYS A 109 ? 0.74407 0.85372 0.57584 0.10625  0.08556  0.03397  126 LYS A NZ  
576  N N   . THR A 110 ? 0.65412 0.61936 0.54999 0.02975  0.06662  -0.02456 127 THR A N   
577  C CA  . THR A 110 ? 0.59192 0.54882 0.51394 0.02061  0.07154  -0.01082 127 THR A CA  
578  C C   . THR A 110 ? 0.68113 0.61403 0.61066 -0.00990 0.04813  -0.00362 127 THR A C   
579  O O   . THR A 110 ? 0.69560 0.59790 0.61906 -0.02597 0.04433  0.00698  127 THR A O   
580  C CB  . THR A 110 ? 0.58476 0.57138 0.54891 0.02945  0.08250  -0.00104 127 THR A CB  
581  O OG1 . THR A 110 ? 0.60946 0.59883 0.54624 0.05480  0.10131  -0.00806 127 THR A OG1 
582  C CG2 . THR A 110 ? 0.60481 0.59939 0.61809 0.01982  0.08819  0.02703  127 THR A CG2 
583  N N   . ARG A 111 ? 0.75224 0.69449 0.69156 -0.02167 0.02884  -0.00736 128 ARG A N   
584  C CA  . ARG A 111 ? 0.75862 0.68227 0.70577 -0.05476 -0.00034 0.00354  128 ARG A CA  
585  C C   . ARG A 111 ? 0.84251 0.69144 0.70998 -0.06616 -0.01123 -0.00744 128 ARG A C   
586  O O   . ARG A 111 ? 0.84731 0.65345 0.69860 -0.09724 -0.03241 0.00233  128 ARG A O   
587  C CB  . ARG A 111 ? 0.82950 0.78266 0.80364 -0.05979 -0.01544 0.00433  128 ARG A CB  
588  C CG  . ARG A 111 ? 0.92412 0.87502 0.92047 -0.09542 -0.04930 0.02397  128 ARG A CG  
589  C CD  . ARG A 111 ? 0.97997 0.96578 1.00796 -0.09644 -0.06072 0.02969  128 ARG A CD  
590  N NE  . ARG A 111 ? 0.94427 0.93819 1.00091 -0.13391 -0.09810 0.05690  128 ARG A NE  
591  C CZ  . ARG A 111 ? 0.92698 0.97619 1.06765 -0.14532 -0.10102 0.09630  128 ARG A CZ  
592  N NH1 . ARG A 111 ? 0.86978 0.95786 1.06017 -0.11563 -0.06269 0.10862  128 ARG A NH1 
593  N NH2 . ARG A 111 ? 0.94937 1.01325 1.12161 -0.18675 -0.14327 0.12894  128 ARG A NH2 
594  N N   . ALA A 112 ? 0.90774 0.73429 0.72043 -0.04087 0.00429  -0.02323 129 ALA A N   
595  C CA  . ALA A 112 ? 0.96465 0.70646 0.68604 -0.03807 0.00779  -0.02998 129 ALA A CA  
596  C C   . ALA A 112 ? 0.91727 0.61962 0.61272 -0.03492 0.02520  -0.02580 129 ALA A C   
597  O O   . ALA A 112 ? 1.05378 0.68175 0.70220 -0.06224 0.00935  -0.02401 129 ALA A O   
598  C CB  . ALA A 112 ? 1.07295 0.81644 0.75811 -0.00205 0.03048  -0.03466 129 ALA A CB  
599  N N   . MET A 113 ? 0.86986 0.61678 0.59132 -0.00466 0.05502  -0.02271 130 MET A N   
600  C CA  . MET A 113 ? 0.84209 0.55341 0.53499 0.00708  0.07867  -0.01664 130 MET A CA  
601  C C   . MET A 113 ? 0.81887 0.52412 0.55044 -0.02531 0.06425  -0.00513 130 MET A C   
602  O O   . MET A 113 ? 0.91062 0.54238 0.59548 -0.04062 0.06402  -0.00109 130 MET A O   
603  C CB  . MET A 113 ? 0.77769 0.55132 0.49812 0.04369  0.10749  -0.01156 130 MET A CB  
604  C CG  . MET A 113 ? 0.80445 0.60515 0.50828 0.07230  0.11917  -0.01027 130 MET A CG  
605  S SD  . MET A 113 ? 0.93213 0.64993 0.54122 0.09869  0.14472  -0.00248 130 MET A SD  
606  C CE  . MET A 113 ? 1.08127 0.78091 0.67417 0.08304  0.11985  -0.01226 130 MET A CE  
607  N N   . GLY A 114 ? 0.74769 0.52654 0.56392 -0.03408 0.05546  0.00534  131 GLY A N   
608  C CA  . GLY A 114 ? 0.72658 0.51840 0.59854 -0.05895 0.04768  0.02928  131 GLY A CA  
609  C C   . GLY A 114 ? 0.77005 0.51740 0.63683 -0.11117 0.00589  0.04116  131 GLY A C   
610  O O   . GLY A 114 ? 0.72803 0.47276 0.63303 -0.13915 -0.00422 0.06731  131 GLY A O   
611  N N   . THR A 115 ? 0.86428 0.57645 0.68431 -0.12753 -0.02153 0.02654  132 THR A N   
612  C CA  . THR A 115 ? 0.86743 0.52363 0.66318 -0.18303 -0.06979 0.03732  132 THR A CA  
613  C C   . THR A 115 ? 0.98060 0.51647 0.67653 -0.20196 -0.07354 0.02974  132 THR A C   
614  O O   . THR A 115 ? 0.98828 0.48424 0.68615 -0.25549 -0.11149 0.04956  132 THR A O   
615  C CB  . THR A 115 ? 0.84644 0.48715 0.60374 -0.19191 -0.09687 0.02329  132 THR A CB  
616  O OG1 . THR A 115 ? 0.83266 0.57917 0.68761 -0.18113 -0.09606 0.03617  132 THR A OG1 
617  C CG2 . THR A 115 ? 0.94044 0.50873 0.64984 -0.25136 -0.15228 0.03241  132 THR A CG2 
618  N N   . TYR A 116 ? 1.04344 0.52161 0.65568 -0.15917 -0.03347 0.00731  133 TYR A N   
619  C CA  . TYR A 116 ? 1.08531 0.42315 0.57274 -0.16763 -0.02938 -0.00301 133 TYR A CA  
620  C C   . TYR A 116 ? 1.09526 0.41787 0.58134 -0.14367 0.01143  0.00470  133 TYR A C   
621  O O   . TYR A 116 ? 1.21862 0.41610 0.60261 -0.15366 0.01670  0.00012  133 TYR A O   
622  C CB  . TYR A 116 ? 1.21658 0.47993 0.58963 -0.13155 -0.00984 -0.02663 133 TYR A CB  
623  C CG  . TYR A 116 ? 1.34116 0.58471 0.68834 -0.16389 -0.05559 -0.03331 133 TYR A CG  
624  C CD1 . TYR A 116 ? 1.36478 0.51792 0.65510 -0.22794 -0.11073 -0.03025 133 TYR A CD1 
625  C CD2 . TYR A 116 ? 1.31229 0.63308 0.69926 -0.13649 -0.04943 -0.03855 133 TYR A CD2 
626  C CE1 . TYR A 116 ? 1.40368 0.54256 0.66977 -0.26003 -0.15758 -0.03278 133 TYR A CE1 
627  C CE2 . TYR A 116 ? 1.42772 0.73420 0.79447 -0.16476 -0.09038 -0.04168 133 TYR A CE2 
628  C CZ  . TYR A 116 ? 1.50857 0.72576 0.81392 -0.22532 -0.14449 -0.03863 133 TYR A CZ  
629  O OH  . TYR A 116 ? 1.76385 0.96563 1.04325 -0.25592 -0.19017 -0.03874 133 TYR A OH  
630  N N   . ALA A 117 ? 0.96495 0.60991 0.32446 -0.00770 0.05894  -0.00224 134 ALA A N   
631  C CA  . ALA A 117 ? 0.94758 0.58595 0.35826 -0.02249 0.06046  -0.01267 134 ALA A CA  
632  C C   . ALA A 117 ? 0.99747 0.62466 0.39378 -0.04466 0.02723  -0.04249 134 ALA A C   
633  O O   . ALA A 117 ? 1.01025 0.65092 0.37916 -0.05531 -0.00562 -0.05033 134 ALA A O   
634  C CB  . ALA A 117 ? 0.86074 0.53963 0.35398 -0.03216 0.05796  0.00761  134 ALA A CB  
635  N N   . ASP A 118 ? 0.93543 0.54048 0.35788 -0.05207 0.03613  -0.05419 135 ASP A N   
636  C CA  . ASP A 118 ? 0.93253 0.52979 0.36552 -0.07567 0.00615  -0.07614 135 ASP A CA  
637  C C   . ASP A 118 ? 0.89323 0.53775 0.41291 -0.09145 -0.00593 -0.06040 135 ASP A C   
638  O O   . ASP A 118 ? 0.91869 0.57294 0.46081 -0.11119 -0.03427 -0.06883 135 ASP A O   
639  C CB  . ASP A 118 ? 0.99532 0.53210 0.40415 -0.07352 0.02414  -0.09950 135 ASP A CB  
640  C CG  . ASP A 118 ? 1.17842 0.66189 0.49647 -0.05127 0.04755  -0.11630 135 ASP A CG  
641  O OD1 . ASP A 118 ? 1.24324 0.69839 0.48508 -0.05864 0.02227  -0.14517 135 ASP A OD1 
642  O OD2 . ASP A 118 ? 1.19174 0.66489 0.51582 -0.02626 0.09146  -0.09820 135 ASP A OD2 
643  N N   . LEU A 119 ? 0.84152 0.51528 0.41004 -0.08377 0.01503  -0.03701 136 LEU A N   
644  C CA  . LEU A 119 ? 0.79732 0.52041 0.43564 -0.09613 0.00425  -0.02278 136 LEU A CA  
645  C C   . LEU A 119 ? 0.75393 0.50564 0.40669 -0.08895 0.01021  -0.00646 136 LEU A C   
646  O O   . LEU A 119 ? 0.72729 0.46573 0.37310 -0.07626 0.03480  0.00437  136 LEU A O   
647  C CB  . LEU A 119 ? 0.80752 0.53478 0.49683 -0.09860 0.02334  -0.01257 136 LEU A CB  
648  C CG  . LEU A 119 ? 0.74403 0.52790 0.50015 -0.11129 0.01118  0.00283  136 LEU A CG  
649  C CD1 . LEU A 119 ? 0.78758 0.58794 0.55573 -0.12511 -0.01904 -0.00425 136 LEU A CD1 
650  C CD2 . LEU A 119 ? 0.74517 0.53826 0.54895 -0.11068 0.03345  0.02036  136 LEU A CD2 
651  N N   . ILE A 120 ? 0.73515 0.52285 0.40934 -0.09589 -0.01063 -0.00346 137 ILE A N   
652  C CA  . ILE A 120 ? 0.72653 0.53529 0.42019 -0.09125 -0.00585 0.00720  137 ILE A CA  
653  C C   . ILE A 120 ? 0.69957 0.54858 0.43986 -0.10119 -0.01470 0.00989  137 ILE A C   
654  O O   . ILE A 120 ? 0.71652 0.58900 0.46783 -0.10664 -0.03263 0.00817  137 ILE A O   
655  C CB  . ILE A 120 ? 0.71184 0.52051 0.37798 -0.08294 -0.01595 0.00916  137 ILE A CB  
656  C CG1 . ILE A 120 ? 0.72557 0.50162 0.33794 -0.07158 -0.00726 0.00890  137 ILE A CG1 
657  C CG2 . ILE A 120 ? 0.68352 0.50542 0.37682 -0.07840 -0.00905 0.01742  137 ILE A CG2 
658  C CD1 . ILE A 120 ? 0.70442 0.48582 0.29588 -0.05980 -0.00997 0.02103  137 ILE A CD1 
659  N N   . ILE A 121 ? 0.62519 0.48566 0.39270 -0.10390 -0.00311 0.01639  138 ILE A N   
660  C CA  . ILE A 121 ? 0.65837 0.55771 0.45732 -0.11204 -0.01128 0.01644  138 ILE A CA  
661  C C   . ILE A 121 ? 0.68455 0.57813 0.47888 -0.10861 -0.01066 0.01072  138 ILE A C   
662  O O   . ILE A 121 ? 0.72444 0.59351 0.51743 -0.10701 0.00062  0.01491  138 ILE A O   
663  C CB  . ILE A 121 ? 0.68346 0.60428 0.51665 -0.12194 -0.00329 0.02774  138 ILE A CB  
664  C CG1 . ILE A 121 ? 0.65691 0.56801 0.49753 -0.12133 0.00472  0.03533  138 ILE A CG1 
665  C CG2 . ILE A 121 ? 0.65636 0.62501 0.51214 -0.12998 -0.01496 0.02746  138 ILE A CG2 
666  C CD1 . ILE A 121 ? 0.65424 0.60007 0.54060 -0.12934 0.01197  0.05412  138 ILE A CD1 
667  N N   . ILE A 122 ? 0.63971 0.55346 0.43494 -0.10583 -0.02005 0.00319  139 ILE A N   
668  C CA  . ILE A 122 ? 0.66544 0.56557 0.45681 -0.10154 -0.01655 -0.00659 139 ILE A CA  
669  C C   . ILE A 122 ? 0.67367 0.60321 0.47418 -0.10919 -0.02212 -0.01749 139 ILE A C   
670  O O   . ILE A 122 ? 0.65196 0.61759 0.45513 -0.10546 -0.02830 -0.01538 139 ILE A O   
671  C CB  . ILE A 122 ? 0.66102 0.55164 0.43804 -0.08482 -0.01656 -0.00544 139 ILE A CB  
672  C CG1 . ILE A 122 ? 0.64242 0.52315 0.40346 -0.07996 -0.01955 0.00702  139 ILE A CG1 
673  C CG2 . ILE A 122 ? 0.64628 0.50455 0.42367 -0.07863 -0.00572 -0.01210 139 ILE A CG2 
674  C CD1 . ILE A 122 ? 0.63928 0.52272 0.39129 -0.06597 -0.02335 0.01632  139 ILE A CD1 
675  N N   . THR A 123 ? 0.69688 0.61420 0.50275 -0.12090 -0.02127 -0.02704 140 THR A N   
676  C CA  . THR A 123 ? 0.70534 0.65221 0.51239 -0.13335 -0.03032 -0.03909 140 THR A CA  
677  C C   . THR A 123 ? 0.74926 0.66241 0.53782 -0.13208 -0.02942 -0.06529 140 THR A C   
678  O O   . THR A 123 ? 0.77224 0.64096 0.56804 -0.13480 -0.02394 -0.06790 140 THR A O   
679  C CB  . THR A 123 ? 0.71041 0.67590 0.54347 -0.15489 -0.03523 -0.02621 140 THR A CB  
680  O OG1 . THR A 123 ? 0.75230 0.73783 0.60380 -0.15216 -0.02987 -0.00241 140 THR A OG1 
681  C CG2 . THR A 123 ? 0.68351 0.68962 0.51430 -0.16977 -0.04907 -0.03564 140 THR A CG2 
682  N N   . GLY A 124 ? 0.71190 0.64337 0.47741 -0.12581 -0.03211 -0.08344 141 GLY A N   
683  C CA  . GLY A 124 ? 0.75175 0.64283 0.49249 -0.12268 -0.02850 -0.11464 141 GLY A CA  
684  C C   . GLY A 124 ? 0.78514 0.69173 0.49706 -0.09722 -0.01879 -0.12487 141 GLY A C   
685  O O   . GLY A 124 ? 0.76389 0.72418 0.47886 -0.08845 -0.02022 -0.10701 141 GLY A O   
686  N N   . SER A 125 ? 0.82410 0.68128 0.51304 -0.08443 -0.00649 -0.15122 142 SER A N   
687  C CA  . SER A 125 ? 0.80922 0.67206 0.46922 -0.05414 0.01033  -0.16088 142 SER A CA  
688  C C   . SER A 125 ? 0.86217 0.75650 0.54633 -0.02925 0.02086  -0.12351 142 SER A C   
689  O O   . SER A 125 ? 0.86091 0.75133 0.57492 -0.03351 0.01717  -0.09905 142 SER A O   
690  C CB  . SER A 125 ? 0.93452 0.72297 0.57409 -0.04320 0.02692  -0.19314 142 SER A CB  
691  O OG  . SER A 125 ? 0.92094 0.67698 0.59345 -0.02895 0.04128  -0.17072 142 SER A OG  
692  N N   . LEU A 126 ? 0.88341 0.81160 0.55318 -0.00284 0.03355  -0.11769 143 LEU A N   
693  C CA  . LEU A 126 ? 0.78616 0.74957 0.48598 0.01892  0.04066  -0.07820 143 LEU A CA  
694  C C   . LEU A 126 ? 0.84202 0.75915 0.55710 0.03421  0.05503  -0.06898 143 LEU A C   
695  O O   . LEU A 126 ? 0.79598 0.72676 0.54108 0.03229  0.04724  -0.03819 143 LEU A O   
696  C CB  . LEU A 126 ? 0.68399 0.69469 0.37144 0.04741  0.05555  -0.06858 143 LEU A CB  
697  C CG  . LEU A 126 ? 0.63918 0.70950 0.36783 0.06519  0.05708  -0.01995 143 LEU A CG  
698  C CD1 . LEU A 126 ? 0.63317 0.74948 0.39614 0.03878  0.03049  0.00384  143 LEU A CD1 
699  C CD2 . LEU A 126 ? 0.66709 0.78126 0.38332 0.09797  0.07829  -0.00924 143 LEU A CD2 
700  N N   . GLU A 127 ? 0.95510 0.81471 0.64859 0.04802  0.07535  -0.09650 144 GLU A N   
701  C CA  . GLU A 127 ? 0.98894 0.80294 0.70279 0.06575  0.09407  -0.08490 144 GLU A CA  
702  C C   . GLU A 127 ? 0.97692 0.77532 0.71782 0.04368  0.07892  -0.06948 144 GLU A C   
703  O O   . GLU A 127 ? 1.00696 0.80840 0.77440 0.05658  0.08480  -0.03707 144 GLU A O   
704  C CB  . GLU A 127 ? 1.03415 0.77689 0.71950 0.07781  0.11711  -0.12592 144 GLU A CB  
705  C CG  . GLU A 127 ? 1.14561 0.84633 0.85077 0.11171  0.14999  -0.11213 144 GLU A CG  
706  C CD  . GLU A 127 ? 1.31494 0.93883 1.03619 0.09958  0.15530  -0.12863 144 GLU A CD  
707  O OE1 . GLU A 127 ? 1.28854 0.88124 0.99443 0.06626  0.13612  -0.16323 144 GLU A OE1 
708  O OE2 . GLU A 127 ? 1.30741 0.90732 1.06368 0.12312  0.17839  -0.10140 144 GLU A OE2 
709  N N   . GLN A 128 ? 0.90438 0.69365 0.63912 0.01184  0.05977  -0.08752 145 GLN A N   
710  C CA  . GLN A 128 ? 0.85880 0.62851 0.61472 -0.00693 0.05047  -0.07537 145 GLN A CA  
711  C C   . GLN A 128 ? 0.77449 0.59097 0.54045 -0.01648 0.03337  -0.04702 145 GLN A C   
712  O O   . GLN A 128 ? 0.73906 0.55111 0.51771 -0.01297 0.03368  -0.02321 145 GLN A O   
713  C CB  . GLN A 128 ? 0.82341 0.56231 0.57445 -0.03563 0.04020  -0.10363 145 GLN A CB  
714  C CG  . GLN A 128 ? 0.93540 0.60826 0.68389 -0.03235 0.05436  -0.13132 145 GLN A CG  
715  C CD  . GLN A 128 ? 0.86631 0.50079 0.64830 -0.01902 0.07123  -0.10819 145 GLN A CD  
716  O OE1 . GLN A 128 ? 0.82116 0.45706 0.62797 -0.03141 0.06502  -0.08554 145 GLN A OE1 
717  N NE2 . GLN A 128 ? 0.86094 0.46388 0.64548 0.00957  0.09598  -0.10944 145 GLN A NE2 
718  N N   . VAL A 129 ? 0.77094 0.63008 0.52998 -0.02875 0.01885  -0.04973 146 VAL A N   
719  C CA  . VAL A 129 ? 0.71047 0.60449 0.47957 -0.03777 0.00404  -0.02691 146 VAL A CA  
720  C C   . VAL A 129 ? 0.72112 0.63737 0.49957 -0.02012 0.00357  0.00007  146 VAL A C   
721  O O   . VAL A 129 ? 0.71181 0.63374 0.49278 -0.02590 -0.00733 0.01732  146 VAL A O   
722  C CB  . VAL A 129 ? 0.64466 0.58104 0.41483 -0.05149 -0.00795 -0.03052 146 VAL A CB  
723  C CG1 . VAL A 129 ? 0.68075 0.60255 0.44539 -0.07120 -0.01065 -0.05128 146 VAL A CG1 
724  C CG2 . VAL A 129 ? 0.66420 0.63824 0.43184 -0.03474 -0.00358 -0.02826 146 VAL A CG2 
725  N N   . ASN A 130 ? 0.76116 0.69030 0.54343 0.00214  0.01561  0.00536  147 ASN A N   
726  C CA  . ASN A 130 ? 0.69832 0.65382 0.49896 0.01893  0.01507  0.03869  147 ASN A CA  
727  C C   . ASN A 130 ? 0.70154 0.62550 0.50567 0.02553  0.02174  0.05170  147 ASN A C   
728  O O   . ASN A 130 ? 0.67867 0.62202 0.48747 0.02114  0.00685  0.07610  147 ASN A O   
729  C CB  . ASN A 130 ? 0.69352 0.67025 0.50237 0.04653  0.03347  0.04688  147 ASN A CB  
730  C CG  . ASN A 130 ? 0.66527 0.70383 0.48968 0.04578  0.02175  0.06462  147 ASN A CG  
731  O OD1 . ASN A 130 ? 0.67267 0.75154 0.52516 0.04451  0.00656  0.09870  147 ASN A OD1 
732  N ND2 . ASN A 130 ? 0.64780 0.69787 0.45675 0.04553  0.02718  0.04438  147 ASN A ND2 
733  N N   . GLY A 131 ? 0.76485 0.63982 0.56658 0.03496  0.04310  0.03578  148 GLY A N   
734  C CA  . GLY A 131 ? 0.71434 0.56146 0.52827 0.04366  0.05340  0.05387  148 GLY A CA  
735  C C   . GLY A 131 ? 0.69723 0.54584 0.50162 0.02499  0.03680  0.06247  148 GLY A C   
736  O O   . GLY A 131 ? 0.69310 0.55473 0.50124 0.03214  0.03381  0.09193  148 GLY A O   
737  N N   . TYR A 132 ? 0.74087 0.58014 0.53078 0.00260  0.02685  0.03937  149 TYR A N   
738  C CA  . TYR A 132 ? 0.71690 0.55202 0.49418 -0.01095 0.01772  0.04591  149 TYR A CA  
739  C C   . TYR A 132 ? 0.73415 0.60487 0.49458 -0.01976 -0.00414 0.05427  149 TYR A C   
740  O O   . TYR A 132 ? 0.73313 0.59973 0.47333 -0.02409 -0.01019 0.06292  149 TYR A O   
741  C CB  . TYR A 132 ? 0.68787 0.49848 0.46531 -0.02927 0.01989  0.02407  149 TYR A CB  
742  C CG  . TYR A 132 ? 0.69450 0.46336 0.49029 -0.02675 0.03656  0.02591  149 TYR A CG  
743  C CD1 . TYR A 132 ? 0.64522 0.40465 0.44484 -0.01802 0.04518  0.05212  149 TYR A CD1 
744  C CD2 . TYR A 132 ? 0.70453 0.44376 0.51422 -0.03353 0.04288  0.00228  149 TYR A CD2 
745  C CE1 . TYR A 132 ? 0.67249 0.39668 0.50058 -0.01559 0.06141  0.06004  149 TYR A CE1 
746  C CE2 . TYR A 132 ? 0.68707 0.38385 0.52219 -0.03501 0.05557  0.00418  149 TYR A CE2 
747  C CZ  . TYR A 132 ? 0.69275 0.38332 0.54273 -0.02565 0.06574  0.03572  149 TYR A CZ  
748  O OH  . TYR A 132 ? 0.72617 0.37661 0.61279 -0.02697 0.07950  0.04344  149 TYR A OH  
749  N N   . TYR A 133 ? 0.70541 0.60906 0.47309 -0.02228 -0.01556 0.05203  150 TYR A N   
750  C CA  . TYR A 133 ? 0.66173 0.59459 0.42172 -0.03295 -0.03889 0.06219  150 TYR A CA  
751  C C   . TYR A 133 ? 0.68161 0.62991 0.43695 -0.02407 -0.04789 0.08929  150 TYR A C   
752  O O   . TYR A 133 ? 0.74255 0.69197 0.47194 -0.03463 -0.06524 0.09279  150 TYR A O   
753  C CB  . TYR A 133 ? 0.61638 0.58769 0.39771 -0.03692 -0.04942 0.06359  150 TYR A CB  
754  C CG  . TYR A 133 ? 0.64610 0.64597 0.43023 -0.04941 -0.07689 0.07907  150 TYR A CG  
755  C CD1 . TYR A 133 ? 0.63299 0.61992 0.40210 -0.06965 -0.09109 0.06559  150 TYR A CD1 
756  C CD2 . TYR A 133 ? 0.66119 0.69838 0.46533 -0.04179 -0.08891 0.10835  150 TYR A CD2 
757  C CE1 . TYR A 133 ? 0.66343 0.66639 0.43301 -0.08500 -0.11921 0.07398  150 TYR A CE1 
758  C CE2 . TYR A 133 ? 0.65145 0.71472 0.46100 -0.05938 -0.12064 0.12225  150 TYR A CE2 
759  C CZ  . TYR A 133 ? 0.63744 0.67959 0.42731 -0.08252 -0.13715 0.10159  150 TYR A CZ  
760  O OH  . TYR A 133 ? 0.64608 0.70501 0.44004 -0.10369 -0.17149 0.10993  150 TYR A OH  
761  N N   . ASN A 134 ? 0.69604 0.65621 0.47405 -0.00384 -0.03553 0.10937  151 ASN A N   
762  C CA  . ASN A 134 ? 0.70844 0.69335 0.48873 0.00515  -0.04432 0.14350  151 ASN A CA  
763  C C   . ASN A 134 ? 0.73847 0.69703 0.49269 0.00770  -0.03741 0.14804  151 ASN A C   
764  O O   . ASN A 134 ? 0.71043 0.68948 0.44133 0.00356  -0.05600 0.16624  151 ASN A O   
765  C CB  . ASN A 134 ? 0.69917 0.70346 0.51802 0.03079  -0.02606 0.16977  151 ASN A CB  
766  C CG  . ASN A 134 ? 0.71094 0.75411 0.55535 0.03225  -0.03289 0.17610  151 ASN A CG  
767  O OD1 . ASN A 134 ? 0.75178 0.78423 0.60762 0.04601  -0.01070 0.16245  151 ASN A OD1 
768  N ND2 . ASN A 134 ? 0.73189 0.82133 0.58461 0.01735  -0.06464 0.19729  151 ASN A ND2 
769  N N   . ILE A 135 ? 0.73506 0.65087 0.49211 0.01319  -0.01251 0.13289  152 ILE A N   
770  C CA  . ILE A 135 ? 0.71545 0.61013 0.45636 0.01817  -0.00188 0.14371  152 ILE A CA  
771  C C   . ILE A 135 ? 0.73723 0.62946 0.43126 0.00240  -0.01822 0.13142  152 ILE A C   
772  O O   . ILE A 135 ? 0.78687 0.68790 0.44944 0.00708  -0.02327 0.14892  152 ILE A O   
773  C CB  . ILE A 135 ? 0.67364 0.52342 0.43793 0.02268  0.02524  0.13167  152 ILE A CB  
774  C CG1 . ILE A 135 ? 0.68468 0.52397 0.48963 0.04300  0.04639  0.14628  152 ILE A CG1 
775  C CG2 . ILE A 135 ? 0.68517 0.51868 0.43645 0.02537  0.03546  0.14538  152 ILE A CG2 
776  C CD1 . ILE A 135 ? 0.69589 0.48348 0.52590 0.04237  0.06845  0.12891  152 ILE A CD1 
777  N N   . LEU A 136 ? 0.72380 0.60444 0.41052 -0.01449 -0.02493 0.10215  153 LEU A N   
778  C CA  . LEU A 136 ? 0.75336 0.61813 0.39950 -0.02588 -0.03109 0.08740  153 LEU A CA  
779  C C   . LEU A 136 ? 0.79827 0.68264 0.41226 -0.03863 -0.06151 0.08351  153 LEU A C   
780  O O   . LEU A 136 ? 0.83044 0.70066 0.39473 -0.04116 -0.06703 0.07787  153 LEU A O   
781  C CB  . LEU A 136 ? 0.74877 0.59273 0.41003 -0.03711 -0.02125 0.06379  153 LEU A CB  
782  C CG  . LEU A 136 ? 0.73245 0.54842 0.40655 -0.03195 0.00400  0.06632  153 LEU A CG  
783  C CD1 . LEU A 136 ? 0.83443 0.64604 0.54332 -0.02184 0.01602  0.07706  153 LEU A CD1 
784  C CD2 . LEU A 136 ? 0.69764 0.50655 0.39122 -0.04635 0.00728  0.04814  153 LEU A CD2 
785  N N   . LYS A 137 ? 0.77665 0.69193 0.41726 -0.04700 -0.08146 0.08641  154 LYS A N   
786  C CA  . LYS A 137 ? 0.72867 0.66593 0.34821 -0.06269 -0.11585 0.08864  154 LYS A CA  
787  C C   . LYS A 137 ? 0.78090 0.73051 0.36128 -0.05612 -0.12625 0.10868  154 LYS A C   
788  O O   . LYS A 137 ? 0.85086 0.79085 0.37720 -0.06866 -0.14717 0.09638  154 LYS A O   
789  C CB  . LYS A 137 ? 0.66868 0.65008 0.33724 -0.06783 -0.13339 0.10493  154 LYS A CB  
790  C CG  . LYS A 137 ? 0.66894 0.67290 0.33313 -0.09277 -0.17422 0.10559  154 LYS A CG  
791  C CD  . LYS A 137 ? 0.77531 0.74895 0.43368 -0.11233 -0.17997 0.07396  154 LYS A CD  
792  C CE  . LYS A 137 ? 0.78532 0.76315 0.43332 -0.14096 -0.22128 0.06754  154 LYS A CE  
793  N NZ  . LYS A 137 ? 0.92352 0.84172 0.52061 -0.15432 -0.22151 0.02882  154 LYS A NZ  
794  N N   . ALA A 138 ? 0.72323 0.69268 0.32834 -0.03551 -0.11048 0.13955  155 ALA A N   
795  C CA  . ALA A 138 ? 0.76780 0.75803 0.34268 -0.02524 -0.11600 0.16765  155 ALA A CA  
796  C C   . ALA A 138 ? 0.86221 0.81710 0.37688 -0.02038 -0.10254 0.15330  155 ALA A C   
797  O O   . ALA A 138 ? 0.93618 0.89733 0.38872 -0.02633 -0.12275 0.15151  155 ALA A O   
798  C CB  . ALA A 138 ? 0.75268 0.76216 0.37813 -0.00008 -0.09134 0.20498  155 ALA A CB  
799  N N   . LEU A 139 ? 0.85899 0.77743 0.38994 -0.00967 -0.06863 0.14344  156 LEU A N   
800  C CA  . LEU A 139 ? 0.83567 0.72680 0.32370 0.00182  -0.04728 0.14195  156 LEU A CA  
801  C C   . LEU A 139 ? 0.86630 0.73109 0.28713 -0.01133 -0.06020 0.10877  156 LEU A C   
802  O O   . LEU A 139 ? 0.92620 0.78393 0.28271 -0.00164 -0.05660 0.11099  156 LEU A O   
803  C CB  . LEU A 139 ? 0.83288 0.69425 0.36729 0.01029  -0.01287 0.14051  156 LEU A CB  
804  C CG  . LEU A 139 ? 0.85809 0.69370 0.36988 0.02352  0.01544  0.14631  156 LEU A CG  
805  C CD1 . LEU A 139 ? 0.91008 0.76758 0.40804 0.04538  0.02627  0.18522  156 LEU A CD1 
806  C CD2 . LEU A 139 ? 0.86773 0.67715 0.43457 0.02171  0.03994  0.14184  156 LEU A CD2 
807  N N   . ASN A 140 ? 0.88042 0.72965 0.31420 -0.03141 -0.07331 0.07885  157 ASN A N   
808  C CA  . ASN A 140 ? 0.90575 0.71609 0.29010 -0.04194 -0.07613 0.04505  157 ASN A CA  
809  C C   . ASN A 140 ? 1.01670 0.82756 0.32973 -0.05324 -0.10850 0.03149  157 ASN A C   
810  O O   . ASN A 140 ? 1.02672 0.87287 0.36209 -0.06976 -0.14312 0.03435  157 ASN A O   
811  C CB  . ASN A 140 ? 0.87893 0.67947 0.30833 -0.06036 -0.08222 0.02383  157 ASN A CB  
812  C CG  . ASN A 140 ? 0.93550 0.68887 0.33327 -0.06401 -0.06920 -0.00453 157 ASN A CG  
813  O OD1 . ASN A 140 ? 0.94397 0.67814 0.31402 -0.08084 -0.09077 -0.02862 157 ASN A OD1 
814  N ND2 . ASN A 140 ? 0.98948 0.72294 0.39703 -0.04847 -0.03311 0.00066  157 ASN A ND2 
815  N N   . LYS A 141 ? 1.05882 0.84232 0.31723 -0.04137 -0.09199 0.01419  158 LYS A N   
816  C CA  . LYS A 141 ? 1.08780 0.88040 0.29351 -0.04415 -0.11206 -0.00355 158 LYS A CA  
817  C C   . LYS A 141 ? 1.14789 0.88946 0.32782 -0.05884 -0.11694 -0.04884 158 LYS A C   
818  O O   . LYS A 141 ? 1.21314 0.94568 0.33886 -0.06078 -0.12864 -0.07262 158 LYS A O   
819  C CB  . LYS A 141 ? 1.13560 0.93915 0.29515 -0.01573 -0.08487 0.01526  158 LYS A CB  
820  C CG  . LYS A 141 ? 1.31810 1.15992 0.42411 -0.01424 -0.10672 0.01406  158 LYS A CG  
821  C CD  . LYS A 141 ? 1.45484 1.29163 0.50059 0.01026  -0.07380 0.01826  158 LYS A CD  
822  C CE  . LYS A 141 ? 1.50759 1.35665 0.47678 0.00334  -0.09744 -0.01143 158 LYS A CE  
823  N NZ  . LYS A 141 ? 1.47280 1.30170 0.37407 0.02394  -0.06409 -0.01897 158 LYS A NZ  
824  N N   . ARG A 142 ? 1.08490 0.79197 0.30134 -0.06869 -0.10682 -0.06050 159 ARG A N   
825  C CA  . ARG A 142 ? 1.12508 0.77802 0.32496 -0.07996 -0.10504 -0.09764 159 ARG A CA  
826  C C   . ARG A 142 ? 1.11697 0.77196 0.37679 -0.10821 -0.12984 -0.10365 159 ARG A C   
827  O O   . ARG A 142 ? 1.13531 0.74497 0.40241 -0.11498 -0.11799 -0.12383 159 ARG A O   
828  C CB  . ARG A 142 ? 1.13545 0.73805 0.31544 -0.05777 -0.05641 -0.10246 159 ARG A CB  
829  C CG  . ARG A 142 ? 1.18677 0.78649 0.31532 -0.02595 -0.02418 -0.09164 159 ARG A CG  
830  C CD  . ARG A 142 ? 1.28919 0.87916 0.35033 -0.02502 -0.03822 -0.11891 159 ARG A CD  
831  N NE  . ARG A 142 ? 1.42986 1.00718 0.43529 0.00691  -0.00153 -0.11474 159 ARG A NE  
832  C CZ  . ARG A 142 ? 1.52442 1.13719 0.48110 0.01708  -0.00872 -0.10830 159 ARG A CZ  
833  N NH1 . ARG A 142 ? 1.46577 1.13425 0.42644 0.00043  -0.04887 -0.09878 159 ARG A NH1 
834  N NH2 . ARG A 142 ? 1.48934 1.08585 0.39342 0.04566  0.02649  -0.10767 159 ARG A NH2 
835  N N   . ASN A 143 ? 1.06278 0.77187 0.36961 -0.12266 -0.16106 -0.08225 160 ASN A N   
836  C CA  . ASN A 143 ? 1.06226 0.78612 0.43318 -0.14778 -0.18549 -0.08052 160 ASN A CA  
837  C C   . ASN A 143 ? 1.01978 0.72098 0.42666 -0.14767 -0.16094 -0.08200 160 ASN A C   
838  O O   . ASN A 143 ? 1.01684 0.69371 0.44984 -0.16304 -0.16558 -0.09776 160 ASN A O   
839  C CB  . ASN A 143 ? 1.11714 0.82298 0.48292 -0.17146 -0.21646 -0.10590 160 ASN A CB  
840  C CG  . ASN A 143 ? 1.28126 1.04408 0.67633 -0.18746 -0.25703 -0.08666 160 ASN A CG  
841  O OD1 . ASN A 143 ? 1.25994 1.06103 0.72507 -0.20116 -0.27404 -0.06374 160 ASN A OD1 
842  N ND2 . ASN A 143 ? 1.28562 1.06081 0.63022 -0.18448 -0.27195 -0.09146 160 ASN A ND2 
843  N N   . ALA A 144 ? 0.97088 0.69363 0.40699 -0.12609 -0.12955 -0.06042 161 ALA A N   
844  C CA  . ALA A 144 ? 0.87282 0.59274 0.36383 -0.12098 -0.10121 -0.05669 161 ALA A CA  
845  C C   . ALA A 144 ? 0.85656 0.61789 0.42054 -0.13699 -0.12029 -0.04499 161 ALA A C   
846  O O   . ALA A 144 ? 0.89015 0.69022 0.47144 -0.14540 -0.14800 -0.03152 161 ALA A O   
847  C CB  . ALA A 144 ? 0.86538 0.59897 0.37060 -0.09934 -0.06957 -0.03727 161 ALA A CB  
848  N N   . LYS A 145 ? 0.80517 0.56199 0.41376 -0.13976 -0.10422 -0.04566 162 LYS A N   
849  C CA  . LYS A 145 ? 0.74743 0.55232 0.42846 -0.14814 -0.11274 -0.02791 162 LYS A CA  
850  C C   . LYS A 145 ? 0.75364 0.59280 0.45958 -0.13308 -0.09291 -0.01147 162 LYS A C   
851  O O   . LYS A 145 ? 0.74485 0.56566 0.43974 -0.12205 -0.06663 -0.01306 162 LYS A O   
852  C CB  . LYS A 145 ? 0.80949 0.60067 0.53057 -0.15676 -0.10325 -0.03069 162 LYS A CB  
853  C CG  . LYS A 145 ? 0.88896 0.63266 0.59280 -0.17357 -0.11956 -0.05173 162 LYS A CG  
854  C CD  . LYS A 145 ? 0.96028 0.70851 0.73279 -0.18310 -0.11355 -0.04231 162 LYS A CD  
855  C CE  . LYS A 145 ? 1.11562 0.83540 0.89851 -0.20852 -0.14522 -0.05579 162 LYS A CE  
856  N NZ  . LYS A 145 ? 1.23050 0.86081 0.95990 -0.21247 -0.13652 -0.09292 162 LYS A NZ  
857  N N   . PHE A 146 ? 0.71368 0.60105 0.45419 -0.13256 -0.10489 0.00483  163 PHE A N   
858  C CA  . PHE A 146 ? 0.68891 0.60139 0.44702 -0.11941 -0.08774 0.01383  163 PHE A CA  
859  C C   . PHE A 146 ? 0.64565 0.59712 0.45384 -0.12254 -0.08368 0.02347  163 PHE A C   
860  O O   . PHE A 146 ? 0.62714 0.61084 0.46914 -0.12917 -0.09889 0.03569  163 PHE A O   
861  C CB  . PHE A 146 ? 0.60741 0.54097 0.36001 -0.10918 -0.09554 0.02478  163 PHE A CB  
862  C CG  . PHE A 146 ? 0.69373 0.59803 0.40149 -0.10067 -0.09138 0.02208  163 PHE A CG  
863  C CD1 . PHE A 146 ? 0.73191 0.62196 0.40289 -0.10764 -0.11067 0.01918  163 PHE A CD1 
864  C CD2 . PHE A 146 ? 0.69782 0.58993 0.40013 -0.08682 -0.06968 0.02358  163 PHE A CD2 
865  C CE1 . PHE A 146 ? 0.73417 0.60598 0.36028 -0.09734 -0.10619 0.02134  163 PHE A CE1 
866  C CE2 . PHE A 146 ? 0.74119 0.61247 0.40956 -0.07662 -0.06349 0.02864  163 PHE A CE2 
867  C CZ  . PHE A 146 ? 0.74857 0.61344 0.37691 -0.08006 -0.08064 0.02928  163 PHE A CZ  
868  N N   . VAL A 147 ? 0.60937 0.56287 0.42466 -0.11855 -0.06454 0.02171  164 VAL A N   
869  C CA  . VAL A 147 ? 0.61674 0.61539 0.46976 -0.11954 -0.06075 0.03168  164 VAL A CA  
870  C C   . VAL A 147 ? 0.61975 0.62638 0.46035 -0.11046 -0.05227 0.02545  164 VAL A C   
871  O O   . VAL A 147 ? 0.65835 0.63508 0.48107 -0.11014 -0.04167 0.01648  164 VAL A O   
872  C CB  . VAL A 147 ? 0.57131 0.57093 0.44858 -0.12748 -0.04938 0.03723  164 VAL A CB  
873  C CG1 . VAL A 147 ? 0.54067 0.59291 0.44770 -0.12795 -0.04594 0.04892  164 VAL A CG1 
874  C CG2 . VAL A 147 ? 0.64669 0.63745 0.54499 -0.13570 -0.05651 0.04269  164 VAL A CG2 
875  N N   . LEU A 148 ? 0.54432 0.58856 0.39560 -0.10238 -0.05552 0.03076  165 LEU A N   
876  C CA  . LEU A 148 ? 0.58015 0.62424 0.41452 -0.09272 -0.04649 0.01893  165 LEU A CA  
877  C C   . LEU A 148 ? 0.57390 0.65641 0.41951 -0.09741 -0.04394 0.01834  165 LEU A C   
878  O O   . LEU A 148 ? 0.57588 0.70718 0.44148 -0.09281 -0.04676 0.03315  165 LEU A O   
879  C CB  . LEU A 148 ? 0.57094 0.62654 0.40127 -0.07492 -0.04640 0.02461  165 LEU A CB  
880  C CG  . LEU A 148 ? 0.54813 0.58333 0.37292 -0.07187 -0.05414 0.03369  165 LEU A CG  
881  C CD1 . LEU A 148 ? 0.54554 0.60085 0.37633 -0.05219 -0.05081 0.04713  165 LEU A CD1 
882  C CD2 . LEU A 148 ? 0.57679 0.56165 0.37534 -0.07414 -0.04755 0.02150  165 LEU A CD2 
883  N N   . LYS A 149 ? 0.60430 0.67084 0.44003 -0.10729 -0.04001 0.00545  166 LYS A N   
884  C CA  . LYS A 149 ? 0.56360 0.67059 0.40550 -0.11591 -0.04227 0.00534  166 LYS A CA  
885  C C   . LYS A 149 ? 0.62444 0.71984 0.43179 -0.11040 -0.04060 -0.02043 166 LYS A C   
886  O O   . LYS A 149 ? 0.66015 0.70805 0.45256 -0.11583 -0.03864 -0.03855 166 LYS A O   
887  C CB  . LYS A 149 ? 0.54234 0.64622 0.40362 -0.13420 -0.04229 0.01334  166 LYS A CB  
888  C CG  . LYS A 149 ? 0.56474 0.67730 0.45958 -0.13644 -0.03881 0.03721  166 LYS A CG  
889  C CD  . LYS A 149 ? 0.61940 0.72759 0.53788 -0.14865 -0.03155 0.05103  166 LYS A CD  
890  C CE  . LYS A 149 ? 0.72103 0.88067 0.68344 -0.15301 -0.02937 0.07932  166 LYS A CE  
891  N NZ  . LYS A 149 ? 0.80934 0.94304 0.79846 -0.15313 -0.01425 0.09612  166 LYS A NZ  
892  N N   . ILE A 150 ? 0.62523 0.76131 0.42047 -0.09792 -0.03934 -0.02135 167 ILE A N   
893  C CA  . ILE A 150 ? 0.61696 0.73524 0.36999 -0.08677 -0.03339 -0.05024 167 ILE A CA  
894  C C   . ILE A 150 ? 0.64936 0.77650 0.38177 -0.10732 -0.04419 -0.07021 167 ILE A C   
895  O O   . ILE A 150 ? 0.63398 0.82069 0.37775 -0.11681 -0.05276 -0.05417 167 ILE A O   
896  C CB  . ILE A 150 ? 0.55366 0.71360 0.29781 -0.05986 -0.02326 -0.04026 167 ILE A CB  
897  C CG1 . ILE A 150 ? 0.58045 0.74512 0.35908 -0.04731 -0.02020 -0.01148 167 ILE A CG1 
898  C CG2 . ILE A 150 ? 0.58987 0.71680 0.28562 -0.04120 -0.00960 -0.07213 167 ILE A CG2 
899  C CD1 . ILE A 150 ? 0.61368 0.72018 0.38317 -0.03793 -0.01284 -0.02122 167 ILE A CD1 
900  N N   . ASN A 151 ? 0.67756 0.74760 0.38477 -0.11615 -0.04551 -0.10213 168 ASN A N   
901  C CA  . ASN A 151 ? 0.72581 0.79620 0.40803 -0.13969 -0.06101 -0.12769 168 ASN A CA  
902  C C   . ASN A 151 ? 0.88570 0.89169 0.52214 -0.13068 -0.05341 -0.17117 168 ASN A C   
903  O O   . ASN A 151 ? 0.93434 0.87575 0.58208 -0.13578 -0.04948 -0.18227 168 ASN A O   
904  C CB  . ASN A 151 ? 0.77336 0.83223 0.49150 -0.17050 -0.07471 -0.11687 168 ASN A CB  
905  C CG  . ASN A 151 ? 0.86805 0.95137 0.57255 -0.20119 -0.09839 -0.13149 168 ASN A CG  
906  O OD1 . ASN A 151 ? 0.87943 0.94019 0.53491 -0.20621 -0.10653 -0.17132 168 ASN A OD1 
907  N ND2 . ASN A 151 ? 0.87334 0.99930 0.62169 -0.22287 -0.10980 -0.09920 168 ASN A ND2 
908  N N   . GLU A 152 ? 0.99775 1.01894 0.58313 -0.11542 -0.04860 -0.19466 169 GLU A N   
909  C CA  . GLU A 152 ? 1.05601 1.00442 0.59770 -0.10103 -0.03444 -0.23718 169 GLU A CA  
910  C C   . GLU A 152 ? 1.09090 0.98710 0.60805 -0.13443 -0.05443 -0.27988 169 GLU A C   
911  O O   . GLU A 152 ? 1.15003 0.97304 0.63348 -0.12546 -0.04267 -0.31960 169 GLU A O   
912  C CB  . GLU A 152 ? 1.07022 1.04214 0.56000 -0.06553 -0.01470 -0.24915 169 GLU A CB  
913  C CG  . GLU A 152 ? 1.08747 1.09087 0.60877 -0.02820 0.00961  -0.20805 169 GLU A CG  
914  C CD  . GLU A 152 ? 1.13962 1.07566 0.68190 -0.00845 0.03102  -0.20656 169 GLU A CD  
915  O OE1 . GLU A 152 ? 1.17030 1.03096 0.70327 -0.02000 0.03149  -0.23799 169 GLU A OE1 
916  O OE2 . GLU A 152 ? 1.08901 1.05130 0.66225 0.01767  0.04629  -0.17007 169 GLU A OE2 
917  N N   . ASN A 153 ? 0.98651 0.91592 0.52554 -0.17299 -0.08375 -0.27049 170 ASN A N   
918  C CA  . ASN A 153 ? 1.03119 0.91678 0.57338 -0.20370 -0.10756 -0.29731 170 ASN A CA  
919  C C   . ASN A 153 ? 1.09038 0.92188 0.68361 -0.22677 -0.10868 -0.28798 170 ASN A C   
920  O O   . ASN A 153 ? 1.05782 0.85399 0.67045 -0.25185 -0.12788 -0.30313 170 ASN A O   
921  C CB  . ASN A 153 ? 1.08994 1.04425 0.64719 -0.22910 -0.13863 -0.27998 170 ASN A CB  
922  C CG  . ASN A 153 ? 1.16446 1.19153 0.68867 -0.20859 -0.13678 -0.26825 170 ASN A CG  
923  O OD1 . ASN A 153 ? 1.22760 1.24150 0.69032 -0.19049 -0.13558 -0.30000 170 ASN A OD1 
924  N ND2 . ASN A 153 ? 1.13212 1.23569 0.69830 -0.21036 -0.13556 -0.21981 170 ASN A ND2 
925  N N   . MET A 154 ? 1.04685 0.88231 0.68342 -0.20677 -0.08853 -0.24952 171 MET A N   
926  C CA  . MET A 154 ? 0.98104 0.77865 0.67353 -0.21801 -0.08592 -0.22752 171 MET A CA  
927  C C   . MET A 154 ? 1.07857 0.79482 0.76726 -0.19809 -0.06413 -0.24744 171 MET A C   
928  O O   . MET A 154 ? 1.04617 0.75921 0.72919 -0.16239 -0.03937 -0.23579 171 MET A O   
929  C CB  . MET A 154 ? 0.88086 0.72184 0.61300 -0.20487 -0.07514 -0.17855 171 MET A CB  
930  C CG  . MET A 154 ? 0.79598 0.70296 0.55337 -0.22701 -0.09233 -0.15111 171 MET A CG  
931  S SD  . MET A 154 ? 0.76839 0.70435 0.56658 -0.20919 -0.07481 -0.10169 171 MET A SD  
932  C CE  . MET A 154 ? 0.77815 0.64217 0.59178 -0.19435 -0.05547 -0.09772 171 MET A CE  
933  N N   . PRO A 155 ? 1.07270 0.72455 0.77237 -0.22043 -0.07248 -0.27233 172 PRO A N   
934  C CA  . PRO A 155 ? 1.10723 0.67845 0.80926 -0.19928 -0.04802 -0.28948 172 PRO A CA  
935  C C   . PRO A 155 ? 1.15694 0.72337 0.90898 -0.17641 -0.02489 -0.24348 172 PRO A C   
936  O O   . PRO A 155 ? 1.15829 0.68119 0.91027 -0.14670 0.00141  -0.24538 172 PRO A O   
937  C CB  . PRO A 155 ? 1.15973 0.66799 0.87431 -0.23727 -0.06841 -0.32224 172 PRO A CB  
938  C CG  . PRO A 155 ? 1.11588 0.68134 0.86474 -0.27706 -0.10063 -0.29693 172 PRO A CG  
939  C CD  . PRO A 155 ? 1.05485 0.70641 0.77259 -0.26745 -0.10559 -0.28234 172 PRO A CD  
940  N N   . TYR A 156 ? 1.05554 0.66702 0.84705 -0.18688 -0.03198 -0.20102 173 TYR A N   
941  C CA  . TYR A 156 ? 0.96139 0.57696 0.78542 -0.16421 -0.01190 -0.15864 173 TYR A CA  
942  C C   . TYR A 156 ? 0.86318 0.54741 0.68216 -0.15830 -0.01542 -0.12990 173 TYR A C   
943  O O   . TYR A 156 ? 0.82692 0.55214 0.64721 -0.18010 -0.03329 -0.12775 173 TYR A O   
944  C CB  . TYR A 156 ? 0.93348 0.51751 0.81375 -0.18029 -0.01093 -0.13493 173 TYR A CB  
945  C CG  . TYR A 156 ? 0.97555 0.48338 0.87213 -0.18307 -0.00348 -0.15860 173 TYR A CG  
946  C CD1 . TYR A 156 ? 1.00108 0.47232 0.91047 -0.15110 0.02484  -0.14564 173 TYR A CD1 
947  C CD2 . TYR A 156 ? 1.02473 0.49614 0.92500 -0.21834 -0.02546 -0.19388 173 TYR A CD2 
948  C CE1 . TYR A 156 ? 1.06631 0.46110 0.99773 -0.15078 0.03649  -0.16561 173 TYR A CE1 
949  C CE2 . TYR A 156 ? 1.10373 0.49245 1.02037 -0.22228 -0.01809 -0.22063 173 TYR A CE2 
950  C CZ  . TYR A 156 ? 1.14975 0.49789 1.08456 -0.18667 0.01559  -0.20570 173 TYR A CZ  
951  O OH  . TYR A 156 ? 1.17869 0.44037 1.13707 -0.18791 0.02743  -0.22938 173 TYR A OH  
952  N N   . ALA A 157 ? 0.87471 0.57121 0.69027 -0.13005 0.00063  -0.10693 174 ALA A N   
953  C CA  . ALA A 157 ? 0.75888 0.50983 0.56866 -0.12530 -0.00320 -0.08415 174 ALA A CA  
954  C C   . ALA A 157 ? 0.74298 0.50425 0.58200 -0.13935 -0.00503 -0.05659 174 ALA A C   
955  O O   . ALA A 157 ? 0.75872 0.48980 0.62672 -0.14731 -0.00035 -0.04605 174 ALA A O   
956  C CB  . ALA A 157 ? 0.67944 0.43867 0.47813 -0.09643 0.00909  -0.06753 174 ALA A CB  
957  N N   . GLN A 158 ? 0.71565 0.51919 0.55119 -0.14017 -0.00886 -0.04164 175 GLN A N   
958  C CA  . GLN A 158 ? 0.66505 0.47813 0.52449 -0.14715 -0.00415 -0.01384 175 GLN A CA  
959  C C   . GLN A 158 ? 0.69650 0.52618 0.53850 -0.13055 0.00315  0.00089  175 GLN A C   
960  O O   . GLN A 158 ? 0.69929 0.56011 0.53090 -0.13061 -0.00446 -0.00420 175 GLN A O   
961  C CB  . GLN A 158 ? 0.67375 0.51914 0.55590 -0.17260 -0.01728 -0.01066 175 GLN A CB  
962  C CG  . GLN A 158 ? 0.69179 0.55476 0.60030 -0.17385 -0.00709 0.02292  175 GLN A CG  
963  C CD  . GLN A 158 ? 0.69744 0.59194 0.64410 -0.20071 -0.01919 0.03609  175 GLN A CD  
964  O OE1 . GLN A 158 ? 0.72525 0.61139 0.68456 -0.22235 -0.03551 0.02261  175 GLN A OE1 
965  N NE2 . GLN A 158 ? 0.65792 0.58785 0.62553 -0.20062 -0.01187 0.06354  175 GLN A NE2 
966  N N   . ALA A 159 ? 0.69435 0.50334 0.53314 -0.11715 0.01736  0.01964  176 ALA A N   
967  C CA  . ALA A 159 ? 0.68316 0.49857 0.49696 -0.10414 0.02248  0.02861  176 ALA A CA  
968  C C   . ALA A 159 ? 0.67165 0.49226 0.49854 -0.10745 0.03420  0.04712  176 ALA A C   
969  O O   . ALA A 159 ? 0.64569 0.46141 0.50187 -0.11287 0.04397  0.06467  176 ALA A O   
970  C CB  . ALA A 159 ? 0.69009 0.48369 0.47886 -0.08459 0.03068  0.03710  176 ALA A CB  
971  N N   . THR A 160 ? 0.72607 0.55566 0.53578 -0.10350 0.03436  0.04544  177 THR A N   
972  C CA  . THR A 160 ? 0.72429 0.55485 0.54351 -0.10179 0.05001  0.06126  177 THR A CA  
973  C C   . THR A 160 ? 0.73158 0.53507 0.50383 -0.08537 0.05768  0.05551  177 THR A C   
974  O O   . THR A 160 ? 0.75303 0.55920 0.50425 -0.08715 0.04150  0.03871  177 THR A O   
975  C CB  . THR A 160 ? 0.73667 0.60338 0.58603 -0.11620 0.04134  0.06175  177 THR A CB  
976  O OG1 . THR A 160 ? 0.75394 0.64862 0.62667 -0.13296 0.02431  0.05542  177 THR A OG1 
977  C CG2 . THR A 160 ? 0.69975 0.57129 0.57644 -0.11417 0.06231  0.08678  177 THR A CG2 
978  N N   . PHE A 161 ? 0.71918 0.49772 0.47340 -0.06965 0.08115  0.07000  178 PHE A N   
979  C CA  . PHE A 161 ? 0.74717 0.49474 0.44084 -0.05285 0.08782  0.06075  178 PHE A CA  
980  C C   . PHE A 161 ? 0.80128 0.52714 0.48401 -0.04270 0.11241  0.06503  178 PHE A C   
981  O O   . PHE A 161 ? 0.78990 0.51208 0.49023 -0.03058 0.14086  0.09040  178 PHE A O   
982  C CB  . PHE A 161 ? 0.76356 0.49851 0.43252 -0.03600 0.09948  0.07491  178 PHE A CB  
983  C CG  . PHE A 161 ? 0.76192 0.51084 0.44508 -0.04149 0.08168  0.07403  178 PHE A CG  
984  C CD1 . PHE A 161 ? 0.75562 0.51147 0.41446 -0.04517 0.05776  0.05638  178 PHE A CD1 
985  C CD2 . PHE A 161 ? 0.73356 0.48667 0.45919 -0.04223 0.09053  0.09392  178 PHE A CD2 
986  C CE1 . PHE A 161 ? 0.74532 0.51219 0.42063 -0.04523 0.04766  0.05948  178 PHE A CE1 
987  C CE2 . PHE A 161 ? 0.71212 0.46840 0.45246 -0.04491 0.07868  0.09149  178 PHE A CE2 
988  C CZ  . PHE A 161 ? 0.69471 0.45766 0.40851 -0.04393 0.05980  0.07489  178 PHE A CZ  
989  N N   . LEU A 162 ? 0.80762 0.51657 0.46468 -0.04626 0.10365  0.04277  179 LEU A N   
990  C CA  . LEU A 162 ? 0.83034 0.50609 0.47303 -0.03468 0.12957  0.04142  179 LEU A CA  
991  C C   . LEU A 162 ? 0.87734 0.50368 0.43622 -0.02250 0.13007  0.01452  179 LEU A C   
992  O O   . LEU A 162 ? 0.91990 0.54329 0.45010 -0.03585 0.09797  -0.00974 179 LEU A O   
993  C CB  . LEU A 162 ? 0.79195 0.48197 0.48202 -0.05009 0.12228  0.03868  179 LEU A CB  
994  C CG  . LEU A 162 ? 0.83572 0.48658 0.52205 -0.03764 0.15205  0.03829  179 LEU A CG  
995  C CD1 . LEU A 162 ? 0.94778 0.59093 0.64585 -0.01422 0.19582  0.06945  179 LEU A CD1 
996  C CD2 . LEU A 162 ? 0.82891 0.50673 0.57961 -0.05363 0.14419  0.04548  179 LEU A CD2 
997  N N   . ARG A 163 ? 0.92346 0.51332 0.44193 0.00293  0.16606  0.02029  180 ARG A N   
998  C CA  . ARG A 163 ? 1.02516 0.55952 0.45335 0.01568  0.17061  -0.01069 180 ARG A CA  
999  C C   . ARG A 163 ? 1.12110 0.60922 0.54330 0.03375  0.21094  -0.01262 180 ARG A C   
1000 O O   . ARG A 163 ? 1.11880 0.61144 0.56664 0.05654  0.25218  0.02045  180 ARG A O   
1001 C CB  . ARG A 163 ? 1.09193 0.61905 0.44997 0.03768  0.18021  -0.00564 180 ARG A CB  
1002 C CG  . ARG A 163 ? 1.20968 0.67383 0.46729 0.05738  0.19754  -0.03581 180 ARG A CG  
1003 C CD  . ARG A 163 ? 1.27185 0.73385 0.44469 0.05555  0.16810  -0.05623 180 ARG A CD  
1004 N NE  . ARG A 163 ? 1.36901 0.86144 0.53103 0.08127  0.18802  -0.02221 180 ARG A NE  
1005 C CZ  . ARG A 163 ? 1.48998 0.96960 0.62218 0.11338  0.22239  -0.01257 180 ARG A CZ  
1006 N NH1 . ARG A 163 ? 1.58462 1.01145 0.67426 0.12556  0.24208  -0.03914 180 ARG A NH1 
1007 N NH2 . ARG A 163 ? 1.47658 0.99637 0.62536 0.13423  0.23780  0.02569  180 ARG A NH2 
1008 N N   . VAL A 164 ? 1.18862 0.63094 0.57986 0.02394  0.19953  -0.04921 181 VAL A N   
1009 C CA  . VAL A 164 ? 1.24641 0.63226 0.63326 0.03802  0.23465  -0.05943 181 VAL A CA  
1010 C C   . VAL A 164 ? 1.44195 0.75578 0.71363 0.06479  0.25820  -0.09047 181 VAL A C   
1011 O O   . VAL A 164 ? 1.47542 0.78268 0.66914 0.05939  0.22922  -0.11560 181 VAL A O   
1012 C CB  . VAL A 164 ? 1.28897 0.66649 0.71763 0.00840  0.20503  -0.08078 181 VAL A CB  
1013 C CG1 . VAL A 164 ? 1.40522 0.70351 0.80971 0.01933  0.23326  -0.10617 181 VAL A CG1 
1014 C CG2 . VAL A 164 ? 1.21791 0.66634 0.75801 -0.00583 0.20038  -0.04116 181 VAL A CG2 
1015 N N   . PRO A 165 ? 1.51581 0.77749 0.77078 0.09697  0.31329  -0.08656 182 PRO A N   
1016 C CA  . PRO A 165 ? 1.58166 0.77818 0.72736 0.12465  0.33545  -0.11678 182 PRO A CA  
1017 C C   . PRO A 165 ? 1.69737 0.85980 0.78139 0.09889  0.28523  -0.17289 182 PRO A C   
1018 O O   . PRO A 165 ? 1.69307 0.85521 0.80362 0.06274  0.24352  -0.19506 182 PRO A O   
1019 C CB  . PRO A 165 ? 1.56071 0.71534 0.73656 0.15551  0.39606  -0.09959 182 PRO A CB  
1020 C CG  . PRO A 165 ? 1.45832 0.65127 0.75401 0.14206  0.40510  -0.06398 182 PRO A CG  
1021 C CD  . PRO A 165 ? 1.45905 0.74084 0.80685 0.11269  0.35752  -0.04059 182 PRO A CD  
1022 N N   . LYS A 166 ? 1.84777 0.98747 0.85487 0.11786  0.28974  -0.19247 183 LYS A N   
1023 C CA  . LYS A 166 ? 1.95315 1.06322 0.89276 0.09924  0.24890  -0.24594 183 LYS A CA  
1024 C C   . LYS A 166 ? 1.98862 1.12912 0.95116 0.05233  0.18222  -0.26589 183 LYS A C   
1025 O O   . LYS A 166 ? 2.03706 1.14432 1.01317 0.02552  0.15527  -0.29951 183 LYS A O   
1026 C CB  . LYS A 166 ? 1.91420 0.94498 0.83774 0.10854  0.27573  -0.27849 183 LYS A CB  
1027 C CG  . LYS A 166 ? 2.02294 1.01717 0.87210 0.09222  0.23895  -0.33763 183 LYS A CG  
1028 C CD  . LYS A 166 ? 2.15763 1.06844 0.99030 0.10499  0.27019  -0.37069 183 LYS A CD  
1029 C CE  . LYS A 166 ? 2.23844 1.11274 0.99589 0.08594  0.23055  -0.43448 183 LYS A CE  
1030 N NZ  . LYS A 166 ? 2.36854 1.15418 1.10612 0.09917  0.26113  -0.47245 183 LYS A NZ  
1031 N N   . ASP A 182 ? 1.89802 0.89005 1.66739 -0.27227 -0.09323 -0.35951 199 ASP A N   
1032 C CA  . ASP A 182 ? 1.91995 0.85565 1.68287 -0.23247 -0.03632 -0.34960 199 ASP A CA  
1033 C C   . ASP A 182 ? 1.89622 0.84764 1.56531 -0.19948 -0.00031 -0.34255 199 ASP A C   
1034 O O   . ASP A 182 ? 1.88931 0.87131 1.59387 -0.17995 0.03912  -0.29784 199 ASP A O   
1035 C CB  . ASP A 182 ? 2.07483 0.90898 1.80638 -0.22141 -0.02362 -0.39885 199 ASP A CB  
1036 C CG  . ASP A 182 ? 2.11089 0.89539 1.80931 -0.17459 0.04586  -0.38847 199 ASP A CG  
1037 O OD1 . ASP A 182 ? 2.06208 0.85599 1.84788 -0.16316 0.07952  -0.33962 199 ASP A OD1 
1038 O OD2 . ASP A 182 ? 2.17354 0.92253 1.76371 -0.14868 0.07089  -0.42209 199 ASP A OD2 
1039 N N   . GLU A 183 ? 1.58188 1.07117 1.55647 -0.08425 0.25977  -0.01514 200 GLU A N   
1040 C CA  . GLU A 183 ? 1.51863 1.01090 1.47242 -0.06947 0.22210  -0.00295 200 GLU A CA  
1041 C C   . GLU A 183 ? 1.40994 0.94127 1.38257 -0.03041 0.17923  0.01514  200 GLU A C   
1042 O O   . GLU A 183 ? 1.32143 0.85096 1.28258 -0.01031 0.15245  0.02961  200 GLU A O   
1043 C CB  . GLU A 183 ? 1.60643 1.10481 1.51904 -0.11253 0.19585  -0.02068 200 GLU A CB  
1044 C CG  . GLU A 183 ? 1.68165 1.17599 1.56301 -0.10510 0.15495  -0.00611 200 GLU A CG  
1045 C CD  . GLU A 183 ? 1.82454 1.34263 1.67481 -0.13489 0.09779  -0.00688 200 GLU A CD  
1046 O OE1 . GLU A 183 ? 1.91823 1.42261 1.71945 -0.18999 0.10188  -0.02204 200 GLU A OE1 
1047 O OE2 . GLU A 183 ? 1.81535 1.36630 1.69391 -0.10572 0.04798  0.00756  200 GLU A OE2 
1048 N N   . ASN A 184 ? 1.42571 0.99309 1.42891 -0.02338 0.17663  0.00942  201 ASN A N   
1049 C CA  . ASN A 184 ? 1.35305 0.95612 1.38154 0.01019  0.15013  0.01894  201 ASN A CA  
1050 C C   . ASN A 184 ? 1.30927 0.89333 1.33592 0.03471  0.17425  0.04413  201 ASN A C   
1051 O O   . ASN A 184 ? 1.25541 0.85737 1.28630 0.05981  0.15261  0.05556  201 ASN A O   
1052 C CB  . ASN A 184 ? 1.37941 1.03312 1.44733 0.00403  0.14508  -0.00341 201 ASN A CB  
1053 C CG  . ASN A 184 ? 1.45627 1.15200 1.55967 0.03261  0.12105  -0.00560 201 ASN A CG  
1054 O OD1 . ASN A 184 ? 1.40383 1.10515 1.51344 0.05145  0.08211  0.00002  201 ASN A OD1 
1055 N ND2 . ASN A 184 ? 1.45776 1.18118 1.58296 0.03080  0.14696  -0.01643 201 ASN A ND2 
1056 N N   . LYS A 185 ? 1.30995 0.85692 1.33312 0.02612  0.21656  0.05463  202 LYS A N   
1057 C CA  . LYS A 185 ? 1.18907 0.71594 1.21409 0.04813  0.23074  0.08753  202 LYS A CA  
1058 C C   . LYS A 185 ? 1.15296 0.66048 1.17056 0.06648  0.21898  0.10157  202 LYS A C   
1059 O O   . LYS A 185 ? 1.16249 0.68068 1.18077 0.08980  0.20648  0.12513  202 LYS A O   
1060 C CB  . LYS A 185 ? 1.27213 0.75594 1.30654 0.03660  0.27313  0.10139  202 LYS A CB  
1061 C CG  . LYS A 185 ? 1.43910 0.92540 1.47560 0.00654  0.29773  0.08187  202 LYS A CG  
1062 C CD  . LYS A 185 ? 1.47821 0.90155 1.52655 -0.00489 0.34163  0.09700  202 LYS A CD  
1063 C CE  . LYS A 185 ? 1.48584 0.90347 1.53140 -0.03963 0.37176  0.07799  202 LYS A CE  
1064 N NZ  . LYS A 185 ? 1.33491 0.71579 1.37998 -0.04484 0.39513  0.11239  202 LYS A NZ  
1065 N N   . LEU A 186 ? 1.17162 0.65330 1.17928 0.05019  0.22566  0.08489  203 LEU A N   
1066 C CA  . LEU A 186 ? 1.10450 0.57333 1.10179 0.06035  0.21553  0.09025  203 LEU A CA  
1067 C C   . LEU A 186 ? 1.11677 0.61906 1.09809 0.07834  0.17137  0.09655  203 LEU A C   
1068 O O   . LEU A 186 ? 1.12144 0.62752 1.10419 0.10054  0.16346  0.11463  203 LEU A O   
1069 C CB  . LEU A 186 ? 1.11781 0.56156 1.09326 0.02565  0.22769  0.06256  203 LEU A CB  
1070 C CG  . LEU A 186 ? 1.09417 0.53128 1.04196 0.02182  0.21084  0.05901  203 LEU A CG  
1071 C CD1 . LEU A 186 ? 1.14834 0.57604 1.12422 0.05020  0.22521  0.07616  203 LEU A CD1 
1072 C CD2 . LEU A 186 ? 1.14664 0.55975 1.06337 -0.02680 0.22950  0.02800  203 LEU A CD2 
1073 N N   . PHE A 187 ? 1.11447 0.64143 1.08730 0.06819  0.14150  0.08077  204 PHE A N   
1074 C CA  . PHE A 187 ? 1.09372 0.64721 1.06462 0.08530  0.09940  0.08314  204 PHE A CA  
1075 C C   . PHE A 187 ? 1.10777 0.68446 1.09514 0.11296  0.10220  0.09874  204 PHE A C   
1076 O O   . PHE A 187 ? 1.06895 0.64947 1.04679 0.12850  0.08508  0.10784  204 PHE A O   
1077 C CB  . PHE A 187 ? 1.13104 0.71349 1.11964 0.07519  0.07074  0.06479  204 PHE A CB  
1078 C CG  . PHE A 187 ? 1.16734 0.76027 1.15769 0.08439  0.02024  0.06499  204 PHE A CG  
1079 C CD1 . PHE A 187 ? 1.17396 0.76016 1.15398 0.10520  0.00801  0.07741  204 PHE A CD1 
1080 C CD2 . PHE A 187 ? 1.10055 0.70941 1.10767 0.07106  -0.01771 0.05449  204 PHE A CD2 
1081 C CE1 . PHE A 187 ? 1.19704 0.78358 1.18133 0.11246  -0.03741 0.07855  204 PHE A CE1 
1082 C CE2 . PHE A 187 ? 1.06563 0.67632 1.08304 0.08059  -0.06895 0.06041  204 PHE A CE2 
1083 C CZ  . PHE A 187 ? 1.16113 0.75685 1.16698 0.10165  -0.07759 0.07196  204 PHE A CZ  
1084 N N   . GLU A 188 ? 1.10037 0.69222 1.10564 0.11251  0.12519  0.10179  205 GLU A N   
1085 C CA  . GLU A 188 ? 1.05145 0.67032 1.06141 0.12600  0.12750  0.11562  205 GLU A CA  
1086 C C   . GLU A 188 ? 1.01998 0.62068 1.01744 0.13904  0.13430  0.14683  205 GLU A C   
1087 O O   . GLU A 188 ? 1.05733 0.68065 1.04751 0.15058  0.12061  0.15629  205 GLU A O   
1088 C CB  . GLU A 188 ? 1.13050 0.76434 1.15003 0.11121  0.15215  0.11395  205 GLU A CB  
1089 C CG  . GLU A 188 ? 1.22526 0.89514 1.27096 0.09939  0.14602  0.07787  205 GLU A CG  
1090 C CD  . GLU A 188 ? 1.39143 1.06578 1.44058 0.07533  0.17804  0.07203  205 GLU A CD  
1091 O OE1 . GLU A 188 ? 1.31236 0.95460 1.34010 0.06856  0.20229  0.10192  205 GLU A OE1 
1092 O OE2 . GLU A 188 ? 1.41189 1.12123 1.49023 0.06260  0.17732  0.03815  205 GLU A OE2 
1093 N N   . GLN A 189 ? 1.03819 0.60079 1.04105 0.13629  0.15632  0.16004  206 GLN A N   
1094 C CA  . GLN A 189 ? 1.01958 0.56860 1.03129 0.15157  0.16150  0.18892  206 GLN A CA  
1095 C C   . GLN A 189 ? 1.02777 0.58008 1.02756 0.16045  0.14297  0.18130  206 GLN A C   
1096 O O   . GLN A 189 ? 1.00792 0.57728 1.00875 0.17461  0.13296  0.20062  206 GLN A O   
1097 C CB  . GLN A 189 ? 0.99258 0.49792 1.03302 0.14761  0.19267  0.19656  206 GLN A CB  
1098 C CG  . GLN A 189 ? 0.97260 0.46572 1.02079 0.13548  0.21227  0.20623  206 GLN A CG  
1099 C CD  . GLN A 189 ? 0.98842 0.49579 1.03525 0.14223  0.20452  0.24766  206 GLN A CD  
1100 O OE1 . GLN A 189 ? 0.99877 0.49955 1.06666 0.15892  0.19799  0.28126  206 GLN A OE1 
1101 N NE2 . GLN A 189 ? 1.10283 0.63486 1.12491 0.12502  0.20350  0.24457  206 GLN A NE2 
1102 N N   . GLN A 190 ? 1.05211 0.58864 1.03554 0.14696  0.13685  0.15470  207 GLN A N   
1103 C CA  . GLN A 190 ? 1.07043 0.60598 1.03070 0.14772  0.11674  0.14724  207 GLN A CA  
1104 C C   . GLN A 190 ? 1.06031 0.62902 1.01102 0.16223  0.08931  0.15249  207 GLN A C   
1105 O O   . GLN A 190 ? 1.04771 0.62619 0.99235 0.17207  0.08327  0.16246  207 GLN A O   
1106 C CB  . GLN A 190 ? 1.06173 0.57536 0.99423 0.12182  0.10664  0.12314  207 GLN A CB  
1107 C CG  . GLN A 190 ? 1.13028 0.61135 1.06264 0.10035  0.13833  0.11086  207 GLN A CG  
1108 C CD  . GLN A 190 ? 1.30306 0.76493 1.19510 0.06249  0.12876  0.08836  207 GLN A CD  
1109 O OE1 . GLN A 190 ? 1.30252 0.77248 1.18946 0.05168  0.11304  0.08288  207 GLN A OE1 
1110 N NE2 . GLN A 190 ? 1.36792 0.80861 1.22783 0.03747  0.13409  0.07527  207 GLN A NE2 
1111 N N   . LYS A 191 ? 1.04445 0.63416 1.00079 0.16167  0.07602  0.14136  208 LYS A N   
1112 C CA  . LYS A 191 ? 1.03594 0.65782 0.99427 0.17204  0.05748  0.13692  208 LYS A CA  
1113 C C   . LYS A 191 ? 1.03985 0.68753 0.99630 0.17900  0.06940  0.15860  208 LYS A C   
1114 O O   . LYS A 191 ? 1.01615 0.68236 0.96188 0.18405  0.05804  0.15886  208 LYS A O   
1115 C CB  . LYS A 191 ? 1.06823 0.71393 1.05299 0.16881  0.05057  0.11484  208 LYS A CB  
1116 C CG  . LYS A 191 ? 1.11670 0.74476 1.10911 0.16196  0.02510  0.09797  208 LYS A CG  
1117 C CD  . LYS A 191 ? 1.11323 0.76805 1.14512 0.15643  0.02622  0.07746  208 LYS A CD  
1118 C CE  . LYS A 191 ? 1.07183 0.73821 1.14125 0.16277  -0.01277 0.05831  208 LYS A CE  
1119 N NZ  . LYS A 191 ? 1.11906 0.81124 1.23286 0.15402  -0.01577 0.03777  208 LYS A NZ  
1120 N N   . ARG A 192 ? 1.02897 0.67627 0.99381 0.17600  0.08999  0.17976  209 ARG A N   
1121 C CA  . ARG A 192 ? 1.04343 0.71639 1.00262 0.17738  0.09243  0.20886  209 ARG A CA  
1122 C C   . ARG A 192 ? 1.05986 0.72706 1.02175 0.18956  0.08655  0.22815  209 ARG A C   
1123 O O   . ARG A 192 ? 1.06575 0.76427 1.01923 0.19028  0.07750  0.24760  209 ARG A O   
1124 C CB  . ARG A 192 ? 1.06946 0.73675 1.03593 0.16803  0.10985  0.23415  209 ARG A CB  
1125 C CG  . ARG A 192 ? 1.16087 0.85384 1.11497 0.16246  0.10424  0.27440  209 ARG A CG  
1126 C CD  . ARG A 192 ? 1.29066 1.03296 1.21316 0.14126  0.09984  0.26145  209 ARG A CD  
1127 N NE  . ARG A 192 ? 1.46167 1.21368 1.37326 0.11553  0.11668  0.25159  209 ARG A NE  
1128 C CZ  . ARG A 192 ? 1.55524 1.31018 1.44376 0.09183  0.12235  0.28752  209 ARG A CZ  
1129 N NH1 . ARG A 192 ? 1.53061 1.27663 1.41465 0.09583  0.10740  0.34197  209 ARG A NH1 
1130 N NH2 . ARG A 192 ? 1.47430 1.24153 1.34682 0.06114  0.14150  0.26977  209 ARG A NH2 
1131 N N   . ALA A 193 ? 1.09685 0.72947 1.07072 0.19403  0.09309  0.21962  210 ALA A N   
1132 C CA  . ALA A 193 ? 1.06304 0.69525 1.05104 0.20322  0.09310  0.23090  210 ALA A CA  
1133 C C   . ALA A 193 ? 1.08314 0.72869 1.04177 0.20118  0.07586  0.21344  210 ALA A C   
1134 O O   . ALA A 193 ? 1.07577 0.74481 1.03910 0.20665  0.07025  0.22553  210 ALA A O   
1135 C CB  . ALA A 193 ? 1.03902 0.63161 1.05439 0.20115  0.11534  0.21972  210 ALA A CB  
1136 N N   . TYR A 194 ? 1.06055 0.69074 0.99280 0.19244  0.06498  0.18698  211 TYR A N   
1137 C CA  . TYR A 194 ? 1.00366 0.63805 0.90827 0.18939  0.04620  0.17269  211 TYR A CA  
1138 C C   . TYR A 194 ? 0.99298 0.67038 0.89406 0.19295  0.03883  0.17769  211 TYR A C   
1139 O O   . TYR A 194 ? 1.01730 0.71097 0.90398 0.19152  0.03246  0.17734  211 TYR A O   
1140 C CB  . TYR A 194 ? 0.97613 0.58116 0.86395 0.18044  0.02921  0.15102  211 TYR A CB  
1141 C CG  . TYR A 194 ? 1.08959 0.65408 0.95647 0.16347  0.03145  0.14320  211 TYR A CG  
1142 C CD1 . TYR A 194 ? 1.16349 0.71103 0.99850 0.15097  0.02505  0.13694  211 TYR A CD1 
1143 C CD2 . TYR A 194 ? 1.12944 0.67369 1.00363 0.15258  0.04443  0.13889  211 TYR A CD2 
1144 C CE1 . TYR A 194 ? 1.21205 0.72377 1.01865 0.12402  0.03169  0.12554  211 TYR A CE1 
1145 C CE2 . TYR A 194 ? 1.20157 0.71160 1.04980 0.12645  0.05138  0.12646  211 TYR A CE2 
1146 C CZ  . TYR A 194 ? 1.23122 0.72546 1.04387 0.11034  0.04549  0.11945  211 TYR A CZ  
1147 O OH  . TYR A 194 ? 1.27639 0.73797 1.05464 0.07343  0.05660  0.10291  211 TYR A OH  
1148 N N   . PHE A 195 ? 0.98897 0.68783 0.89999 0.19125  0.04300  0.17823  212 PHE A N   
1149 C CA  . PHE A 195 ? 0.95999 0.70347 0.86158 0.18381  0.04202  0.17754  212 PHE A CA  
1150 C C   . PHE A 195 ? 1.02831 0.80221 0.92437 0.18120  0.04365  0.21218  212 PHE A C   
1151 O O   . PHE A 195 ? 1.06039 0.87268 0.93779 0.16983  0.03912  0.21271  212 PHE A O   
1152 C CB  . PHE A 195 ? 0.88458 0.64772 0.79690 0.17387  0.05122  0.16296  212 PHE A CB  
1153 C CG  . PHE A 195 ? 0.84687 0.60147 0.77888 0.17666  0.04329  0.12408  212 PHE A CG  
1154 C CD1 . PHE A 195 ? 0.89515 0.66664 0.82911 0.17328  0.03851  0.09911  212 PHE A CD1 
1155 C CD2 . PHE A 195 ? 0.89138 0.62030 0.84674 0.18235  0.03848  0.11276  212 PHE A CD2 
1156 C CE1 . PHE A 195 ? 0.85032 0.60879 0.82027 0.18053  0.02700  0.06529  212 PHE A CE1 
1157 C CE2 . PHE A 195 ? 0.87588 0.59863 0.86265 0.18781  0.02249  0.08225  212 PHE A CE2 
1158 C CZ  . PHE A 195 ? 0.81708 0.55251 0.81669 0.18941  0.01577  0.05949  212 PHE A CZ  
1159 N N   . ASN A 196 ? 1.00907 0.76760 0.92670 0.19018  0.04871  0.24075  213 ASN A N   
1160 C CA  . ASN A 196 ? 1.05992 0.84803 0.98807 0.19172  0.04183  0.27846  213 ASN A CA  
1161 C C   . ASN A 196 ? 1.07608 0.86946 1.01139 0.19937  0.03569  0.27206  213 ASN A C   
1162 O O   . ASN A 196 ? 1.12214 0.95858 1.05001 0.19321  0.02389  0.28619  213 ASN A O   
1163 C CB  . ASN A 196 ? 1.13890 0.90598 1.10440 0.20105  0.04839  0.31262  213 ASN A CB  
1164 C CG  . ASN A 196 ? 1.16792 0.93998 1.11645 0.18481  0.05239  0.32876  213 ASN A CG  
1165 O OD1 . ASN A 196 ? 1.13731 0.94449 1.04791 0.16281  0.04924  0.32124  213 ASN A OD1 
1166 N ND2 . ASN A 196 ? 1.15073 0.88685 1.12695 0.19054  0.06380  0.34619  213 ASN A ND2 
1167 N N   . TYR A 197 ? 1.04249 0.79552 0.98683 0.20606  0.04433  0.24851  214 TYR A N   
1168 C CA  . TYR A 197 ? 1.04036 0.79698 0.98611 0.20580  0.04323  0.23627  214 TYR A CA  
1169 C C   . TYR A 197 ? 1.05032 0.82946 0.95335 0.19333  0.03137  0.21923  214 TYR A C   
1170 O O   . TYR A 197 ? 1.11014 0.91588 1.01241 0.18929  0.02759  0.21906  214 TYR A O   
1171 C CB  . TYR A 197 ? 1.05454 0.76068 1.00036 0.20187  0.05705  0.20923  214 TYR A CB  
1172 C CG  . TYR A 197 ? 1.04195 0.74904 0.98838 0.19385  0.06287  0.19202  214 TYR A CG  
1173 C CD1 . TYR A 197 ? 1.01224 0.73592 1.01762 0.20233  0.07692  0.19879  214 TYR A CD1 
1174 C CD2 . TYR A 197 ? 1.09889 0.78959 0.99312 0.17629  0.05482  0.16770  214 TYR A CD2 
1175 C CE1 . TYR A 197 ? 1.04171 0.77284 1.05421 0.19114  0.08718  0.17597  214 TYR A CE1 
1176 C CE2 . TYR A 197 ? 1.13988 0.83088 1.02746 0.16186  0.06324  0.14958  214 TYR A CE2 
1177 C CZ  . TYR A 197 ? 1.17075 0.88584 1.11782 0.16809  0.08172  0.15076  214 TYR A CZ  
1178 O OH  . TYR A 197 ? 1.24429 0.96613 1.19153 0.14986  0.09520  0.12528  214 TYR A OH  
1179 N N   . ALA A 198 ? 1.08145 0.85251 0.95708 0.18640  0.02732  0.20164  215 ALA A N   
1180 C CA  . ALA A 198 ? 1.08018 0.86788 0.92577 0.17424  0.02046  0.18109  215 ALA A CA  
1181 C C   . ALA A 198 ? 1.13839 0.98830 0.97658 0.16192  0.01884  0.19682  215 ALA A C   
1182 O O   . ALA A 198 ? 1.14658 1.02398 0.96695 0.15012  0.01552  0.18992  215 ALA A O   
1183 C CB  . ALA A 198 ? 0.97223 0.73113 0.81049 0.17268  0.01698  0.15305  215 ALA A CB  
1184 N N   . ASN A 199 ? 1.13127 1.00434 0.97652 0.15813  0.02085  0.21868  216 ASN A N   
1185 C CA  . ASN A 199 ? 1.15079 1.08401 0.97626 0.13532  0.01629  0.23818  216 ASN A CA  
1186 C C   . ASN A 199 ? 1.27157 1.23899 1.11293 0.13866  0.00084  0.27652  216 ASN A C   
1187 O O   . ASN A 199 ? 1.29213 1.30739 1.11270 0.11968  -0.00723 0.27799  216 ASN A O   
1188 C CB  . ASN A 199 ? 1.14257 1.08551 0.96384 0.12326  0.02137  0.25542  216 ASN A CB  
1189 C CG  . ASN A 199 ? 1.16800 1.10807 0.97705 0.10848  0.03793  0.21200  216 ASN A CG  
1190 O OD1 . ASN A 199 ? 1.22450 1.19504 1.01225 0.08558  0.04523  0.18258  216 ASN A OD1 
1191 N ND2 . ASN A 199 ? 1.07970 0.98613 0.90980 0.11971  0.04627  0.20334  216 ASN A ND2 
1192 N N   . ASP A 200 ? 1.52132 1.46811 1.40764 0.16146  -0.00301 0.30623  217 ASP A N   
1193 C CA  . ASP A 200 ? 1.51777 1.50169 1.44251 0.16843  -0.02119 0.34733  217 ASP A CA  
1194 C C   . ASP A 200 ? 1.53433 1.52980 1.47601 0.17460  -0.02052 0.32555  217 ASP A C   
1195 O O   . ASP A 200 ? 1.56685 1.61903 1.50887 0.16285  -0.03646 0.33941  217 ASP A O   
1196 C CB  . ASP A 200 ? 1.47539 1.42769 1.45986 0.19275  -0.02128 0.38030  217 ASP A CB  
1197 C CG  . ASP A 200 ? 1.49623 1.43319 1.45944 0.18207  -0.02027 0.40275  217 ASP A CG  
1198 O OD1 . ASP A 200 ? 1.50826 1.44288 1.41938 0.16215  -0.00883 0.37384  217 ASP A OD1 
1199 O OD2 . ASP A 200 ? 1.46068 1.38697 1.46457 0.19234  -0.02981 0.44741  217 ASP A OD2 
1200 N N   . VAL A 201 ? 1.06222 1.06932 1.49344 0.24186  -0.00400 0.26618  218 VAL A N   
1201 C CA  . VAL A 201 ? 0.90743 0.97522 1.38275 0.25882  -0.00042 0.25909  218 VAL A CA  
1202 C C   . VAL A 201 ? 0.91905 1.03303 1.37851 0.20756  -0.00387 0.22605  218 VAL A C   
1203 O O   . VAL A 201 ? 0.84829 1.05667 1.33081 0.19212  -0.02274 0.24435  218 VAL A O   
1204 C CB  . VAL A 201 ? 0.83635 0.83372 1.33376 0.30605  0.02421  0.23764  218 VAL A CB  
1205 C CG1 . VAL A 201 ? 0.81174 0.88325 1.35852 0.33373  0.02949  0.24157  218 VAL A CG1 
1206 C CG2 . VAL A 201 ? 0.89212 0.82039 1.38967 0.35344  0.02185  0.26668  218 VAL A CG2 
1207 N N   . ILE A 202 ? 0.88869 0.93502 1.30667 0.18082  0.01197  0.17852  219 ILE A N   
1208 C CA  . ILE A 202 ? 0.81518 0.88108 1.21246 0.14053  0.01176  0.14039  219 ILE A CA  
1209 C C   . ILE A 202 ? 0.90056 0.99749 1.24207 0.08992  -0.01453 0.13910  219 ILE A C   
1210 O O   . ILE A 202 ? 0.93360 1.08382 1.27018 0.05725  -0.03391 0.13364  219 ILE A O   
1211 C CB  . ILE A 202 ? 0.77644 0.75314 1.14951 0.14213  0.04105  0.08837  219 ILE A CB  
1212 C CG1 . ILE A 202 ? 0.73831 0.69466 1.16377 0.19141  0.06292  0.08451  219 ILE A CG1 
1213 C CG2 . ILE A 202 ? 0.81372 0.79034 1.14075 0.09605  0.03833  0.04659  219 ILE A CG2 
1214 C CD1 . ILE A 202 ? 0.74234 0.60533 1.14633 0.20032  0.09026  0.03716  219 ILE A CD1 
1215 N N   . CYS A 203 ? 0.94260 1.00586 1.23781 0.08252  -0.01769 0.14531  220 CYS A N   
1216 C CA  . CYS A 203 ? 0.94424 1.02366 1.17106 0.04225  -0.03976 0.13772  220 CYS A CA  
1217 C C   . CYS A 203 ? 0.99815 1.16057 1.23586 0.03448  -0.07433 0.18256  220 CYS A C   
1218 O O   . CYS A 203 ? 1.01851 1.20689 1.29489 0.06357  -0.07735 0.22667  220 CYS A O   
1219 C CB  . CYS A 203 ? 1.04522 1.06831 1.21842 0.04191  -0.02711 0.13173  220 CYS A CB  
1220 S SG  . CYS A 203 ? 1.04792 0.98366 1.18486 0.03888  0.00692  0.07367  220 CYS A SG  
1221 N N   . ARG A 204 ? 1.06220 1.26043 1.25983 -0.00474 -0.10322 0.17082  221 ARG A N   
1222 C CA  . ARG A 204 ? 1.09479 1.36539 1.28563 -0.01786 -0.14082 0.20876  221 ARG A CA  
1223 C C   . ARG A 204 ? 1.12257 1.36568 1.24065 -0.02029 -0.14630 0.21351  221 ARG A C   
1224 O O   . ARG A 204 ? 1.14139 1.31894 1.20299 -0.02394 -0.12714 0.18014  221 ARG A O   
1225 C CB  . ARG A 204 ? 1.09236 1.40616 1.26517 -0.06228 -0.17590 0.19561  221 ARG A CB  
1226 C CG  . ARG A 204 ? 0.98361 1.34021 1.23118 -0.06395 -0.17110 0.19765  221 ARG A CG  
1227 C CD  . ARG A 204 ? 1.06219 1.52938 1.36205 -0.07341 -0.20597 0.24533  221 ARG A CD  
1228 N NE  . ARG A 204 ? 1.08282 1.61269 1.46061 -0.07337 -0.20165 0.25709  221 ARG A NE  
1229 C CZ  . ARG A 204 ? 1.04921 1.64388 1.43972 -0.11964 -0.23555 0.26444  221 ARG A CZ  
1230 N NH1 . ARG A 204 ? 1.04959 1.64514 1.37496 -0.16989 -0.28059 0.25782  221 ARG A NH1 
1231 N NH2 . ARG A 204 ? 0.95686 1.61803 1.42538 -0.11503 -0.22625 0.28143  221 ARG A NH2 
1232 N N   . PRO A 205 ? 1.13947 1.43779 1.25811 -0.01499 -0.17089 0.25742  222 PRO A N   
1233 C CA  . PRO A 205 ? 1.18635 1.46431 1.24382 -0.00889 -0.17068 0.27099  222 PRO A CA  
1234 C C   . PRO A 205 ? 1.24507 1.48125 1.20139 -0.03312 -0.17616 0.22947  222 PRO A C   
1235 O O   . PRO A 205 ? 1.25552 1.44839 1.16974 -0.02230 -0.15277 0.22193  222 PRO A O   
1236 C CB  . PRO A 205 ? 1.07795 1.43355 1.14880 -0.00500 -0.20452 0.32030  222 PRO A CB  
1237 C CG  . PRO A 205 ? 1.04737 1.45331 1.21191 0.01205  -0.20497 0.34514  222 PRO A CG  
1238 C CD  . PRO A 205 ? 1.07968 1.46509 1.26331 -0.00576 -0.19425 0.30264  222 PRO A CD  
1239 N N   . ASN A 206 ? 1.25637 1.50343 1.16979 -0.06490 -0.20789 0.20342  223 ASN A N   
1240 C CA  . ASN A 206 ? 1.32200 1.52515 1.12318 -0.08284 -0.22153 0.16465  223 ASN A CA  
1241 C C   . ASN A 206 ? 1.36370 1.50180 1.13450 -0.09895 -0.20755 0.10762  223 ASN A C   
1242 O O   . ASN A 206 ? 1.40350 1.49767 1.07296 -0.11299 -0.22322 0.07065  223 ASN A O   
1243 C CB  . ASN A 206 ? 1.40733 1.65199 1.15873 -0.10724 -0.27580 0.17479  223 ASN A CB  
1244 C CG  . ASN A 206 ? 1.40970 1.71596 1.23935 -0.12989 -0.30284 0.19368  223 ASN A CG  
1245 O OD1 . ASN A 206 ? 1.39461 1.69872 1.29206 -0.13308 -0.28307 0.18358  223 ASN A OD1 
1246 N ND2 . ASN A 206 ? 1.37746 1.74461 1.19788 -0.14465 -0.34845 0.22280  223 ASN A ND2 
1247 N N   . ASP A 207 ? 1.31393 1.44072 1.16284 -0.09294 -0.17909 0.09923  224 ASP A N   
1248 C CA  . ASP A 207 ? 1.29017 1.35165 1.11200 -0.10234 -0.15942 0.04634  224 ASP A CA  
1249 C C   . ASP A 207 ? 1.21910 1.22138 0.97012 -0.08442 -0.13078 0.01965  224 ASP A C   
1250 O O   . ASP A 207 ? 1.24020 1.24248 1.02565 -0.05851 -0.10119 0.04131  224 ASP A O   
1251 C CB  . ASP A 207 ? 1.20543 1.27029 1.12738 -0.08969 -0.13050 0.04796  224 ASP A CB  
1252 C CG  . ASP A 207 ? 1.17854 1.28843 1.14727 -0.11565 -0.15504 0.05260  224 ASP A CG  
1253 O OD1 . ASP A 207 ? 1.23409 1.34456 1.14526 -0.15354 -0.19275 0.03739  224 ASP A OD1 
1254 O OD2 . ASP A 207 ? 1.14744 1.29231 1.20892 -0.09717 -0.13794 0.07361  224 ASP A OD2 
1255 N N   . GLU A 208 ? 1.21490 1.16621 0.86494 -0.09789 -0.14093 -0.02580 225 GLU A N   
1256 C CA  . GLU A 208 ? 1.22903 1.14024 0.79868 -0.07716 -0.11822 -0.04671 225 GLU A CA  
1257 C C   . GLU A 208 ? 1.15105 1.01295 0.73950 -0.06366 -0.07441 -0.07958 225 GLU A C   
1258 O O   . GLU A 208 ? 1.20170 1.05162 0.76049 -0.04236 -0.04732 -0.08129 225 GLU A O   
1259 C CB  . GLU A 208 ? 1.39862 1.27395 0.83391 -0.08708 -0.15035 -0.08014 225 GLU A CB  
1260 C CG  . GLU A 208 ? 1.53661 1.38620 0.88269 -0.05715 -0.12664 -0.09587 225 GLU A CG  
1261 C CD  . GLU A 208 ? 1.90751 1.73173 1.10988 -0.05311 -0.16212 -0.11673 225 GLU A CD  
1262 O OE1 . GLU A 208 ? 1.91903 1.74311 1.08816 -0.07742 -0.21103 -0.11609 225 GLU A OE1 
1263 O OE2 . GLU A 208 ? 2.06245 1.86759 1.18135 -0.02323 -0.14204 -0.13294 225 GLU A OE2 
1264 N N   . VAL A 209 ? 1.16842 1.00749 0.80679 -0.07507 -0.06694 -0.10280 226 VAL A N   
1265 C CA  . VAL A 209 ? 1.04252 0.83718 0.70896 -0.05942 -0.02542 -0.13154 226 VAL A CA  
1266 C C   . VAL A 209 ? 1.04859 0.86185 0.79085 -0.03495 0.00401  -0.09656 226 VAL A C   
1267 O O   . VAL A 209 ? 0.99338 0.77209 0.73769 -0.01970 0.03635  -0.11432 226 VAL A O   
1268 C CB  . VAL A 209 ? 0.98753 0.76686 0.70615 -0.07346 -0.02457 -0.15255 226 VAL A CB  
1269 C CG1 . VAL A 209 ? 0.96546 0.79997 0.80051 -0.06696 -0.02424 -0.10836 226 VAL A CG1 
1270 C CG2 . VAL A 209 ? 1.00180 0.72067 0.71341 -0.05981 0.01199  -0.19677 226 VAL A CG2 
1271 N N   . CYS A 210 ? 1.05577 0.92036 0.85790 -0.03165 -0.00943 -0.04567 227 CYS A N   
1272 C CA  . CYS A 210 ? 1.09040 0.96200 0.96784 -0.01034 0.01145  -0.00904 227 CYS A CA  
1273 C C   . CYS A 210 ? 1.09032 0.97014 0.93322 -0.00187 0.02039  0.01661  227 CYS A C   
1274 O O   . CYS A 210 ? 1.06481 0.94081 0.96262 0.01112  0.03525  0.04870  227 CYS A O   
1275 C CB  . CYS A 210 ? 1.12774 1.04888 1.07925 -0.00580 -0.00779 0.03650  227 CYS A CB  
1276 S SG  . CYS A 210 ? 1.22057 1.15247 1.24634 -0.00580 -0.01032 0.02445  227 CYS A SG  
1277 N N   . SER A 211 ? 1.06886 0.95886 0.81957 -0.00769 0.01000  0.00577  228 SER A N   
1278 C CA  . SER A 211 ? 1.06675 0.98302 0.78479 0.00236  0.01745  0.03928  228 SER A CA  
1279 C C   . SER A 211 ? 1.03582 0.92876 0.77456 0.01183  0.05309  0.03950  228 SER A C   
1280 O O   . SER A 211 ? 1.06534 0.98487 0.82568 0.01629  0.05959  0.08699  228 SER A O   
1281 C CB  . SER A 211 ? 1.06542 0.99502 0.66792 0.00231  -0.00008 0.02256  228 SER A CB  
1282 O OG  . SER A 211 ? 1.12384 1.00564 0.65997 -0.00054 0.00326  -0.03715 228 SER A OG  
1283 N N   . PRO A 212 ? 1.01783 0.86501 0.75066 0.01339  0.07492  -0.00714 229 PRO A N   
1284 C CA  . PRO A 212 ? 0.97027 0.80065 0.73230 0.01943  0.10467  -0.00140 229 PRO A CA  
1285 C C   . PRO A 212 ? 0.94837 0.75274 0.81037 0.02088  0.11014  0.02399  229 PRO A C   
1286 O O   . PRO A 212 ? 0.94231 0.72565 0.83190 0.02160  0.12896  0.03169  229 PRO A O   
1287 C CB  . PRO A 212 ? 0.94913 0.73840 0.66377 0.02320  0.12261  -0.06392 229 PRO A CB  
1288 C CG  . PRO A 212 ? 0.96105 0.72873 0.66216 0.01643  0.10422  -0.09762 229 PRO A CG  
1289 C CD  . PRO A 212 ? 0.98667 0.79762 0.66372 0.00911  0.07235  -0.06686 229 PRO A CD  
1290 N N   . LEU A 213 ? 0.97674 0.78278 0.88997 0.02305  0.09212  0.04014  230 LEU A N   
1291 C CA  . LEU A 213 ? 0.94616 0.72331 0.94241 0.03339  0.09383  0.06750  230 LEU A CA  
1292 C C   . LEU A 213 ? 1.06831 0.87253 1.08964 0.03473  0.07981  0.13240  230 LEU A C   
1293 O O   . LEU A 213 ? 1.07905 0.85162 1.15960 0.04661  0.07653  0.15864  230 LEU A O   
1294 C CB  . LEU A 213 ? 0.89793 0.66575 0.93817 0.04372  0.08472  0.05148  230 LEU A CB  
1295 C CG  . LEU A 213 ? 0.93745 0.68376 0.95887 0.04100  0.09365  -0.00662 230 LEU A CG  
1296 C CD1 . LEU A 213 ? 0.86742 0.61034 0.95187 0.05595  0.08908  -0.00774 230 LEU A CD1 
1297 C CD2 . LEU A 213 ? 0.97837 0.67396 0.98497 0.04353  0.12061  -0.04198 230 LEU A CD2 
1298 N N   . ARG A 214 ? 1.15174 1.00900 1.12444 0.02652  0.07026  0.15940  231 ARG A N   
1299 C CA  . ARG A 214 ? 1.19597 1.08544 1.18960 0.02957  0.05287  0.22073  231 ARG A CA  
1300 C C   . ARG A 214 ? 1.34372 1.27672 1.28543 0.02107  0.05715  0.25215  231 ARG A C   
1301 O O   . ARG A 214 ? 1.44081 1.42524 1.32921 0.02151  0.04384  0.26255  231 ARG A O   
1302 C CB  . ARG A 214 ? 1.21805 1.14610 1.21409 0.03470  0.02691  0.22626  231 ARG A CB  
1303 C CG  . ARG A 214 ? 1.16273 1.12399 1.08662 0.02388  0.01502  0.18996  231 ARG A CG  
1304 C CD  . ARG A 214 ? 1.18386 1.19722 1.10295 0.02282  -0.01750 0.21293  231 ARG A CD  
1305 N NE  . ARG A 214 ? 1.24062 1.25502 1.19246 0.01926  -0.03030 0.18694  231 ARG A NE  
1306 C CZ  . ARG A 214 ? 1.28320 1.31672 1.19005 0.00247  -0.05196 0.15803  231 ARG A CZ  
1307 N NH1 . ARG A 214 ? 1.23669 1.27974 1.05358 -0.00740 -0.06492 0.14509  231 ARG A NH1 
1308 N NH2 . ARG A 214 ? 1.22079 1.26333 1.17053 -0.00378 -0.06288 0.14373  231 ARG A NH2 
1309 N N   . ASP A 215 ? 1.65494 1.57034 1.61128 0.01376  0.07491  0.27058  232 ASP A N   
1310 C CA  . ASP A 215 ? 1.66816 1.63671 1.57868 0.00677  0.08339  0.30368  232 ASP A CA  
1311 C C   . ASP A 215 ? 1.67425 1.68299 1.59329 0.00661  0.06779  0.37390  232 ASP A C   
1312 O O   . ASP A 215 ? 1.70214 1.77389 1.56419 0.01053  0.06515  0.39531  232 ASP A O   
1313 C CB  . ASP A 215 ? 1.61423 1.56201 1.54381 -0.00563 0.10619  0.30570  232 ASP A CB  
1314 C CG  . ASP A 215 ? 1.60319 1.60899 1.46413 -0.00503 0.12472  0.29804  232 ASP A CG  
1315 O OD1 . ASP A 215 ? 1.65520 1.72040 1.45325 0.00557  0.11858  0.31171  232 ASP A OD1 
1316 O OD2 . ASP A 215 ? 1.54331 1.53523 1.40935 -0.01127 0.14478  0.27689  232 ASP A OD2 
1317 N N   . HIS B 6   ? 2.56605 1.15886 1.64212 0.06901  -0.54281 -0.17309 52  HIS B N   
1318 C CA  . HIS B 6   ? 2.58862 1.13973 1.59067 0.01496  -0.55261 -0.11706 52  HIS B CA  
1319 C C   . HIS B 6   ? 2.53014 1.21441 1.67227 0.00748  -0.50943 -0.10731 52  HIS B C   
1320 O O   . HIS B 6   ? 2.42099 1.23477 1.70215 0.01089  -0.45588 -0.11636 52  HIS B O   
1321 C CB  . HIS B 6   ? 2.60759 1.12525 1.51750 -0.06286 -0.53620 -0.05083 52  HIS B CB  
1322 C CG  . HIS B 6   ? 2.70038 1.07241 1.45396 -0.06295 -0.58264 -0.05367 52  HIS B CG  
1323 N ND1 . HIS B 6   ? 2.78014 1.00359 1.36311 -0.08641 -0.63820 -0.03006 52  HIS B ND1 
1324 C CD2 . HIS B 6   ? 2.72321 1.07298 1.46111 -0.04388 -0.58230 -0.07680 52  HIS B CD2 
1325 C CE1 . HIS B 6   ? 2.85309 0.96399 1.31952 -0.08046 -0.67155 -0.03904 52  HIS B CE1 
1326 N NE2 . HIS B 6   ? 2.82001 1.00619 1.37866 -0.05365 -0.63838 -0.06748 52  HIS B NE2 
1327 N N   . MET B 7   ? 2.60268 1.25327 1.70542 -0.00342 -0.53315 -0.08891 53  MET B N   
1328 C CA  . MET B 7   ? 2.47825 1.23744 1.70828 0.00845  -0.50597 -0.09473 53  MET B CA  
1329 C C   . MET B 7   ? 2.57687 1.32186 1.74952 -0.04768 -0.50816 -0.03678 53  MET B C   
1330 O O   . MET B 7   ? 2.56511 1.20953 1.63745 -0.04125 -0.55893 -0.03736 53  MET B O   
1331 C CB  . MET B 7   ? 2.47639 1.21575 1.74400 0.08681  -0.54322 -0.16251 53  MET B CB  
1332 C CG  . MET B 7   ? 2.43078 1.17779 1.74377 0.15018  -0.55017 -0.22803 53  MET B CG  
1333 S SD  . MET B 7   ? 2.63608 1.20443 1.77919 0.19044  -0.62461 -0.26252 53  MET B SD  
1334 C CE  . MET B 7   ? 2.48795 1.12845 1.71654 0.22679  -0.59494 -0.30886 53  MET B CE  
1335 N N   . ASP B 8   ? 2.67656 1.52537 1.91434 -0.10072 -0.45374 0.01124  54  ASP B N   
1336 C CA  . ASP B 8   ? 2.61477 1.46298 1.79737 -0.15946 -0.45098 0.06968  54  ASP B CA  
1337 C C   . ASP B 8   ? 2.49485 1.48604 1.81622 -0.16959 -0.40008 0.08544  54  ASP B C   
1338 O O   . ASP B 8   ? 2.45627 1.55191 1.91127 -0.14748 -0.35725 0.06355  54  ASP B O   
1339 C CB  . ASP B 8   ? 2.57189 1.38456 1.65198 -0.22935 -0.44100 0.12648  54  ASP B CB  
1340 C CG  . ASP B 8   ? 2.48107 1.28221 1.48417 -0.29019 -0.44629 0.18379  54  ASP B CG  
1341 O OD1 . ASP B 8   ? 2.54481 1.23156 1.42232 -0.29577 -0.49928 0.18762  54  ASP B OD1 
1342 O OD2 . ASP B 8   ? 2.33733 1.24709 1.40763 -0.33058 -0.39789 0.22307  54  ASP B OD2 
1343 N N   . LYS B 9   ? 2.28575 1.27982 1.56935 -0.20552 -0.40556 0.12480  55  LYS B N   
1344 C CA  . LYS B 9   ? 2.15983 1.28110 1.55358 -0.22283 -0.35998 0.14867  55  LYS B CA  
1345 C C   . LYS B 9   ? 2.05874 1.26423 1.48321 -0.27722 -0.30638 0.19642  55  LYS B C   
1346 O O   . LYS B 9   ? 1.93937 1.24870 1.44564 -0.29506 -0.26807 0.22069  55  LYS B O   
1347 C CB  . LYS B 9   ? 2.18314 1.27844 1.51933 -0.24211 -0.38619 0.17368  55  LYS B CB  
1348 C CG  . LYS B 9   ? 2.25533 1.24682 1.53135 -0.19630 -0.44589 0.13352  55  LYS B CG  
1349 C CD  . LYS B 9   ? 2.28610 1.23402 1.47497 -0.22733 -0.47555 0.16564  55  LYS B CD  
1350 C CE  . LYS B 9   ? 2.31347 1.16304 1.33618 -0.28798 -0.50184 0.21045  55  LYS B CE  
1351 N NZ  . LYS B 9   ? 2.29160 1.17727 1.27520 -0.34506 -0.49417 0.26325  55  LYS B NZ  
1352 N N   . LEU B 10  ? 2.08930 1.25085 1.44791 -0.30229 -0.30416 0.20981  56  LEU B N   
1353 C CA  . LEU B 10  ? 1.88307 1.12737 1.28836 -0.34157 -0.25120 0.24284  56  LEU B CA  
1354 C C   . LEU B 10  ? 1.76479 1.07956 1.29554 -0.30227 -0.21627 0.20282  56  LEU B C   
1355 O O   . LEU B 10  ? 1.57923 0.95827 1.15148 -0.33036 -0.17270 0.22502  56  LEU B O   
1356 C CB  . LEU B 10  ? 1.73632 0.90013 1.00638 -0.39191 -0.26485 0.27911  56  LEU B CB  
1357 C CG  . LEU B 10  ? 1.67514 0.91589 0.95503 -0.45241 -0.21718 0.33312  56  LEU B CG  
1358 C CD1 . LEU B 10  ? 1.59888 0.94964 0.95867 -0.46875 -0.18420 0.35970  56  LEU B CD1 
1359 C CD2 . LEU B 10  ? 1.75791 0.94063 0.90734 -0.49775 -0.23687 0.36189  56  LEU B CD2 
1360 N N   . LYS B 11  ? 1.97402 1.09285 1.25823 -0.04348 0.14089  -0.10270 57  LYS B N   
1361 C CA  . LYS B 11  ? 1.88958 1.03354 1.19350 -0.07421 0.10090  -0.10817 57  LYS B CA  
1362 C C   . LYS B 11  ? 1.82965 0.91330 1.07932 -0.08280 0.10890  -0.11472 57  LYS B C   
1363 O O   . LYS B 11  ? 1.71978 0.80569 0.95256 -0.11515 0.07207  -0.12074 57  LYS B O   
1364 C CB  . LYS B 11  ? 1.75021 0.93453 1.04535 -0.10869 0.04987  -0.11291 57  LYS B CB  
1365 C CG  . LYS B 11  ? 1.78474 1.04758 1.14730 -0.09765 0.04307  -0.10086 57  LYS B CG  
1366 C CD  . LYS B 11  ? 1.51446 0.85671 0.98465 -0.08326 0.04337  -0.08581 57  LYS B CD  
1367 C CE  . LYS B 11  ? 1.51846 0.93494 1.04321 -0.07754 0.03233  -0.07484 57  LYS B CE  
1368 N NZ  . LYS B 11  ? 1.29059 0.78136 0.90790 -0.06852 0.02726  -0.06246 57  LYS B NZ  
1369 N N   . ASP B 12  ? 1.80549 0.83542 1.03018 -0.05367 0.15828  -0.11047 58  ASP B N   
1370 C CA  . ASP B 12  ? 1.80747 0.78751 1.00807 -0.05304 0.17575  -0.11247 58  ASP B CA  
1371 C C   . ASP B 12  ? 1.72573 0.74241 1.01732 -0.03080 0.19573  -0.09615 58  ASP B C   
1372 O O   . ASP B 12  ? 1.70378 0.69260 0.99295 -0.03299 0.20379  -0.09616 58  ASP B O   
1373 C CB  . ASP B 12  ? 2.07614 0.97151 1.19194 -0.03388 0.22176  -0.11362 58  ASP B CB  
1374 C CG  . ASP B 12  ? 2.18698 1.01711 1.26648 -0.03156 0.24647  -0.11619 58  ASP B CG  
1375 O OD1 . ASP B 12  ? 2.16816 1.00420 1.30114 -0.00042 0.28706  -0.09986 58  ASP B OD1 
1376 O OD2 . ASP B 12  ? 2.17252 0.94385 1.16982 -0.06088 0.22640  -0.13197 58  ASP B OD2 
1377 N N   . THR B 13  ? 1.66548 0.74508 1.04018 -0.01122 0.20147  -0.07949 59  THR B N   
1378 C CA  . THR B 13  ? 1.49333 0.61489 0.96207 0.01667  0.22650  -0.05286 59  THR B CA  
1379 C C   . THR B 13  ? 1.42409 0.59922 0.95772 -0.00291 0.18957  -0.04868 59  THR B C   
1380 O O   . THR B 13  ? 1.35787 0.58292 0.90470 -0.02696 0.14697  -0.05714 59  THR B O   
1381 C CB  . THR B 13  ? 1.39385 0.55541 0.91351 0.04271  0.24597  -0.03308 59  THR B CB  
1382 O OG1 . THR B 13  ? 1.62938 0.74325 1.09504 0.06546  0.28750  -0.03062 59  THR B OG1 
1383 C CG2 . THR B 13  ? 1.28912 0.50580 0.91436 0.06647  0.26438  0.00245  59  THR B CG2 
1384 N N   . PRO B 14  ? 1.37637 0.55878 0.95891 0.00854  0.20529  -0.03081 60  PRO B N   
1385 C CA  . PRO B 14  ? 1.24323 0.49142 0.89407 -0.00730 0.17218  -0.02044 60  PRO B CA  
1386 C C   . PRO B 14  ? 1.10332 0.45618 0.84588 0.00215  0.15910  0.00281  60  PRO B C   
1387 O O   . PRO B 14  ? 1.09304 0.46168 0.87361 0.02824  0.18749  0.02464  60  PRO B O   
1388 C CB  . PRO B 14  ? 1.24526 0.46092 0.91609 0.00704  0.20126  -0.00390 60  PRO B CB  
1389 C CG  . PRO B 14  ? 1.33771 0.48545 0.94436 0.02424  0.24038  -0.01253 60  PRO B CG  
1390 C CD  . PRO B 14  ? 1.33329 0.47932 0.91587 0.03686  0.25341  -0.01560 60  PRO B CD  
1391 N N   . PHE B 15  ? 1.00896 0.43149 0.78733 -0.01994 0.11629  0.00045  61  PHE B N   
1392 C CA  . PHE B 15  ? 0.93302 0.44304 0.78503 -0.01551 0.10132  0.01869  61  PHE B CA  
1393 C C   . PHE B 15  ? 0.85136 0.42157 0.74613 -0.03176 0.06945  0.02540  61  PHE B C   
1394 O O   . PHE B 15  ? 0.87515 0.42858 0.74638 -0.04781 0.05516  0.01524  61  PHE B O   
1395 C CB  . PHE B 15  ? 0.88205 0.41303 0.71922 -0.02145 0.08617  0.00513  61  PHE B CB  
1396 C CG  . PHE B 15  ? 0.82520 0.35920 0.62331 -0.04751 0.05256  -0.01803 61  PHE B CG  
1397 C CD1 . PHE B 15  ? 0.80163 0.39658 0.63440 -0.06232 0.02128  -0.01686 61  PHE B CD1 
1398 C CD2 . PHE B 15  ? 0.96165 0.43613 0.68672 -0.05731 0.05316  -0.03761 61  PHE B CD2 
1399 C CE1 . PHE B 15  ? 0.82293 0.42533 0.62965 -0.08292 -0.00524 -0.03041 61  PHE B CE1 
1400 C CE2 . PHE B 15  ? 0.96446 0.44985 0.66373 -0.08285 0.02002  -0.05068 61  PHE B CE2 
1401 C CZ  . PHE B 15  ? 0.87068 0.42311 0.61656 -0.09389 -0.00743 -0.04487 61  PHE B CZ  
1402 N N   . MET B 16  ? 0.75573 0.39397 0.71218 -0.02818 0.05877  0.04499  62  MET B N   
1403 C CA  . MET B 16  ? 0.71878 0.41559 0.70774 -0.04299 0.02836  0.05101  62  MET B CA  
1404 C C   . MET B 16  ? 0.71448 0.46610 0.73549 -0.04627 0.01082  0.05623  62  MET B C   
1405 O O   . MET B 16  ? 0.71503 0.49457 0.78308 -0.03753 0.01712  0.08141  62  MET B O   
1406 C CB  . MET B 16  ? 0.70489 0.41323 0.73302 -0.03628 0.03748  0.07754  62  MET B CB  
1407 C CG  . MET B 16  ? 0.74021 0.50821 0.79596 -0.05048 0.00750  0.08594  62  MET B CG  
1408 S SD  . MET B 16  ? 0.82434 0.60755 0.91754 -0.04723 0.01236  0.11542  62  MET B SD  
1409 C CE  . MET B 16  ? 0.79127 0.58186 0.85244 -0.06779 -0.01432 0.09563  62  MET B CE  
1410 N N   . VAL B 17  ? 0.67419 0.43884 0.67090 -0.05976 -0.01080 0.03506  63  VAL B N   
1411 C CA  . VAL B 17  ? 0.69463 0.49056 0.70537 -0.06330 -0.02333 0.03259  63  VAL B CA  
1412 C C   . VAL B 17  ? 0.69693 0.52628 0.70307 -0.07841 -0.04963 0.02446  63  VAL B C   
1413 O O   . VAL B 17  ? 0.71694 0.53935 0.69636 -0.08502 -0.05640 0.01203  63  VAL B O   
1414 C CB  . VAL B 17  ? 0.64199 0.41005 0.62143 -0.05966 -0.01484 0.01541  63  VAL B CB  
1415 C CG1 . VAL B 17  ? 0.66974 0.46641 0.66448 -0.06388 -0.02699 0.01254  63  VAL B CG1 
1416 C CG2 . VAL B 17  ? 0.67888 0.40933 0.65524 -0.04214 0.01535  0.02439  63  VAL B CG2 
1417 N N   . GLN B 18  ? 0.63477 0.49712 0.66407 -0.08464 -0.06393 0.03317  64  GLN B N   
1418 C CA  . GLN B 18  ? 0.61640 0.49776 0.62751 -0.09695 -0.08377 0.02250  64  GLN B CA  
1419 C C   . GLN B 18  ? 0.65288 0.53009 0.65326 -0.09993 -0.08753 0.00842  64  GLN B C   
1420 O O   . GLN B 18  ? 0.65806 0.53423 0.68041 -0.09719 -0.08318 0.01542  64  GLN B O   
1421 C CB  . GLN B 18  ? 0.64428 0.55592 0.67337 -0.10625 -0.10005 0.04026  64  GLN B CB  
1422 C CG  . GLN B 18  ? 0.68061 0.59974 0.72527 -0.10226 -0.09529 0.05774  64  GLN B CG  
1423 C CD  . GLN B 18  ? 0.71080 0.65686 0.74789 -0.11280 -0.11328 0.06582  64  GLN B CD  
1424 O OE1 . GLN B 18  ? 0.72119 0.66453 0.73367 -0.11301 -0.11329 0.05680  64  GLN B OE1 
1425 N NE2 . GLN B 18  ? 0.69971 0.67318 0.75717 -0.12287 -0.12985 0.08573  64  GLN B NE2 
1426 N N   . VAL B 19  ? 0.66656 0.54071 0.63689 -0.10357 -0.09226 -0.00807 65  VAL B N   
1427 C CA  . VAL B 19  ? 0.62813 0.49337 0.58575 -0.10484 -0.09234 -0.02146 65  VAL B CA  
1428 C C   . VAL B 19  ? 0.65578 0.52216 0.58537 -0.11275 -0.10188 -0.02994 65  VAL B C   
1429 O O   . VAL B 19  ? 0.68012 0.55063 0.59132 -0.11035 -0.09980 -0.03119 65  VAL B O   
1430 C CB  . VAL B 19  ? 0.59174 0.44326 0.53700 -0.09636 -0.07990 -0.03091 65  VAL B CB  
1431 C CG1 . VAL B 19  ? 0.59318 0.43727 0.52930 -0.09578 -0.07745 -0.04120 65  VAL B CG1 
1432 C CG2 . VAL B 19  ? 0.61720 0.45533 0.57323 -0.08906 -0.06866 -0.02581 65  VAL B CG2 
1433 N N   . LYS B 20  ? 0.66294 0.52146 0.58633 -0.12269 -0.11136 -0.03454 66  LYS B N   
1434 C CA  . LYS B 20  ? 0.64706 0.48769 0.52772 -0.12970 -0.11558 -0.04828 66  LYS B CA  
1435 C C   . LYS B 20  ? 0.68466 0.50449 0.55240 -0.11837 -0.09738 -0.06176 66  LYS B C   
1436 O O   . LYS B 20  ? 0.63637 0.44537 0.51812 -0.11896 -0.09503 -0.06508 66  LYS B O   
1437 C CB  . LYS B 20  ? 0.67947 0.51241 0.55358 -0.15046 -0.13711 -0.04728 66  LYS B CB  
1438 C CG  . LYS B 20  ? 0.77086 0.63182 0.66442 -0.16251 -0.15681 -0.02668 66  LYS B CG  
1439 C CD  . LYS B 20  ? 0.85924 0.72089 0.75875 -0.18803 -0.18439 -0.01736 66  LYS B CD  
1440 C CE  . LYS B 20  ? 0.87797 0.77871 0.80923 -0.19864 -0.20391 0.01276  66  LYS B CE  
1441 N NZ  . LYS B 20  ? 0.95784 0.87023 0.90794 -0.22717 -0.23603 0.03180  66  LYS B NZ  
1442 N N   . LEU B 21  ? 0.69874 0.51681 0.54584 -0.10709 -0.08333 -0.06449 67  LEU B N   
1443 C CA  . LEU B 21  ? 0.66966 0.47886 0.51358 -0.09294 -0.06331 -0.06762 67  LEU B CA  
1444 C C   . LEU B 21  ? 0.75424 0.52657 0.55944 -0.09151 -0.05217 -0.08140 67  LEU B C   
1445 O O   . LEU B 21  ? 0.82087 0.57151 0.58646 -0.10170 -0.05967 -0.09031 67  LEU B O   
1446 C CB  . LEU B 21  ? 0.69653 0.52677 0.54488 -0.08285 -0.05455 -0.05559 67  LEU B CB  
1447 C CG  . LEU B 21  ? 0.62864 0.48273 0.50618 -0.08615 -0.06427 -0.04429 67  LEU B CG  
1448 C CD1 . LEU B 21  ? 0.56995 0.44291 0.45118 -0.08178 -0.06050 -0.03072 67  LEU B CD1 
1449 C CD2 . LEU B 21  ? 0.58071 0.43324 0.47756 -0.08410 -0.06200 -0.04382 67  LEU B CD2 
1450 N N   . PRO B 22  ? 0.75622 0.51555 0.56725 -0.07982 -0.03379 -0.08303 68  PRO B N   
1451 C CA  . PRO B 22  ? 0.79471 0.51123 0.56555 -0.07280 -0.01385 -0.09439 68  PRO B CA  
1452 C C   . PRO B 22  ? 0.82862 0.55137 0.58613 -0.05386 0.00960  -0.08345 68  PRO B C   
1453 O O   . PRO B 22  ? 0.78561 0.54695 0.56524 -0.05110 0.00446  -0.06787 68  PRO B O   
1454 C CB  . PRO B 22  ? 0.77197 0.48046 0.56900 -0.06562 -0.00205 -0.09351 68  PRO B CB  
1455 C CG  . PRO B 22  ? 0.69838 0.45304 0.54198 -0.05951 -0.00563 -0.07562 68  PRO B CG  
1456 C CD  . PRO B 22  ? 0.72731 0.50480 0.57838 -0.07300 -0.02951 -0.07414 68  PRO B CD  
1457 N N   . ASN B 23  ? 0.86729 0.54772 0.58775 -0.04048 0.03757  -0.08987 69  ASN B N   
1458 C CA  . ASN B 23  ? 0.84276 0.53010 0.56003 -0.01648 0.06843  -0.07224 69  ASN B CA  
1459 C C   . ASN B 23  ? 0.79154 0.53228 0.57562 -0.00521 0.07272  -0.04408 69  ASN B C   
1460 O O   . ASN B 23  ? 0.80427 0.54806 0.61664 -0.00389 0.07400  -0.04171 69  ASN B O   
1461 C CB  . ASN B 23  ? 0.89691 0.52049 0.56392 -0.00050 0.10457  -0.08294 69  ASN B CB  
1462 C CG  . ASN B 23  ? 0.92948 0.55767 0.59508 0.02939  0.14431  -0.05944 69  ASN B CG  
1463 O OD1 . ASN B 23  ? 0.89877 0.58284 0.60514 0.03530  0.14079  -0.03339 69  ASN B OD1 
1464 N ND2 . ASN B 23  ? 1.02739 0.59286 0.64516 0.04872  0.18448  -0.06650 69  ASN B ND2 
1465 N N   . TYR B 24  ? 0.75570 0.53908 0.56457 0.00011  0.07197  -0.02072 70  TYR B N   
1466 C CA  . TYR B 24  ? 0.69744 0.53180 0.56564 0.00119  0.06482  0.00647  70  TYR B CA  
1467 C C   . TYR B 24  ? 0.73014 0.56614 0.62335 0.02131  0.09356  0.02654  70  TYR B C   
1468 O O   . TYR B 24  ? 0.68787 0.55771 0.62446 0.01809  0.08385  0.04491  70  TYR B O   
1469 C CB  . TYR B 24  ? 0.64863 0.52531 0.54063 0.00067  0.05833  0.03164  70  TYR B CB  
1470 C CG  . TYR B 24  ? 0.70145 0.58714 0.60155 0.02500  0.09253  0.06002  70  TYR B CG  
1471 C CD1 . TYR B 24  ? 0.78787 0.64369 0.64171 0.03733  0.11423  0.05292  70  TYR B CD1 
1472 C CD2 . TYR B 24  ? 0.66000 0.58406 0.61381 0.03669  0.10508  0.09797  70  TYR B CD2 
1473 C CE1 . TYR B 24  ? 0.81547 0.67617 0.67555 0.06466  0.15307  0.08236  70  TYR B CE1 
1474 C CE2 . TYR B 24  ? 0.66732 0.60327 0.63793 0.06280  0.14160  0.13148  70  TYR B CE2 
1475 C CZ  . TYR B 24  ? 0.75956 0.66195 0.68274 0.07875  0.16834  0.12323  70  TYR B CZ  
1476 O OH  . TYR B 24  ? 0.78920 0.70036 0.72736 0.10909  0.21115  0.15952  70  TYR B OH  
1477 N N   . LYS B 25  ? 0.77775 0.57429 0.64065 0.04254  0.13057  0.02504  71  LYS B N   
1478 C CA  . LYS B 25  ? 0.72755 0.51975 0.61554 0.06575  0.16478  0.04642  71  LYS B CA  
1479 C C   . LYS B 25  ? 0.78720 0.56029 0.68095 0.05775  0.15659  0.03006  71  LYS B C   
1480 O O   . LYS B 25  ? 0.77572 0.57334 0.71462 0.06808  0.16731  0.05510  71  LYS B O   
1481 C CB  . LYS B 25  ? 0.78099 0.51858 0.62217 0.09181  0.21156  0.04378  71  LYS B CB  
1482 C CG  . LYS B 25  ? 0.79126 0.55268 0.63436 0.10569  0.22721  0.06858  71  LYS B CG  
1483 C CD  . LYS B 25  ? 0.91753 0.61604 0.70347 0.13503  0.27977  0.06591  71  LYS B CD  
1484 C CE  . LYS B 25  ? 0.96722 0.69433 0.75940 0.15173  0.29849  0.09597  71  LYS B CE  
1485 N NZ  . LYS B 25  ? 1.17181 0.83036 0.89940 0.18494  0.35721  0.09504  71  LYS B NZ  
1486 N N   . ASP B 26  ? 0.84689 0.58018 0.69953 0.03868  0.13673  -0.00743 72  ASP B N   
1487 C CA  . ASP B 26  ? 0.82862 0.54874 0.69231 0.02835  0.12497  -0.02084 72  ASP B CA  
1488 C C   . ASP B 26  ? 0.79807 0.57336 0.70829 0.01530  0.09508  -0.00739 72  ASP B C   
1489 O O   . ASP B 26  ? 0.80007 0.58831 0.74137 0.01877  0.09752  0.00428  72  ASP B O   
1490 C CB  . ASP B 26  ? 0.87350 0.54293 0.68758 0.00850  0.10829  -0.05749 72  ASP B CB  
1491 C CG  . ASP B 26  ? 0.98829 0.58411 0.74316 0.01721  0.13732  -0.07580 72  ASP B CG  
1492 O OD1 . ASP B 26  ? 1.03871 0.61244 0.79947 0.04077  0.17510  -0.06366 72  ASP B OD1 
1493 O OD2 . ASP B 26  ? 1.06932 0.62597 0.76812 0.00004  0.12298  -0.10101 72  ASP B OD2 
1494 N N   . TYR B 27  ? 0.74728 0.54968 0.65720 0.00026  0.06818  -0.00919 73  TYR B N   
1495 C CA  . TYR B 27  ? 0.67688 0.52057 0.61791 -0.01165 0.04342  0.00320  73  TYR B CA  
1496 C C   . TYR B 27  ? 0.65761 0.53879 0.63804 -0.00166 0.05227  0.03780  73  TYR B C   
1497 O O   . TYR B 27  ? 0.65758 0.55291 0.65737 -0.00526 0.04457  0.04650  73  TYR B O   
1498 C CB  . TYR B 27  ? 0.67409 0.53560 0.60762 -0.02535 0.02111  0.00107  73  TYR B CB  
1499 C CG  . TYR B 27  ? 0.65736 0.54544 0.60844 -0.03953 -0.00297 0.00969  73  TYR B CG  
1500 C CD1 . TYR B 27  ? 0.63118 0.55301 0.60829 -0.04050 -0.00727 0.03791  73  TYR B CD1 
1501 C CD2 . TYR B 27  ? 0.64174 0.51742 0.58042 -0.05258 -0.02061 -0.00801 73  TYR B CD2 
1502 C CE1 . TYR B 27  ? 0.61638 0.54980 0.59395 -0.05714 -0.03069 0.04269  73  TYR B CE1 
1503 C CE2 . TYR B 27  ? 0.63093 0.51626 0.57214 -0.06370 -0.03706 -0.00267 73  TYR B CE2 
1504 C CZ  . TYR B 27  ? 0.65136 0.56122 0.60566 -0.06761 -0.04335 0.02004  73  TYR B CZ  
1505 O OH  . TYR B 27  ? 0.73774 0.64617 0.68000 -0.08269 -0.06181 0.02307  73  TYR B OH  
1506 N N   . LEU B 28  ? 0.68498 0.58634 0.67968 0.01040  0.06767  0.06237  74  LEU B N   
1507 C CA  . LEU B 28  ? 0.65716 0.60308 0.69932 0.01853  0.07429  0.10465  74  LEU B CA  
1508 C C   . LEU B 28  ? 0.66590 0.60297 0.72575 0.03282  0.09511  0.11331  74  LEU B C   
1509 O O   . LEU B 28  ? 0.68217 0.65453 0.77520 0.02833  0.08424  0.13878  74  LEU B O   
1510 C CB  . LEU B 28  ? 0.60270 0.56688 0.66248 0.03596  0.09814  0.13368  74  LEU B CB  
1511 C CG  . LEU B 28  ? 0.53510 0.52704 0.59853 0.02246  0.07720  0.14274  74  LEU B CG  
1512 C CD1 . LEU B 28  ? 0.56111 0.56018 0.63496 0.04552  0.10997  0.16777  74  LEU B CD1 
1513 C CD2 . LEU B 28  ? 0.50583 0.54726 0.60786 0.00256  0.04593  0.17194  74  LEU B CD2 
1514 N N   . LEU B 29  ? 0.68823 0.57434 0.72192 0.04787  0.12353  0.09202  75  LEU B N   
1515 C CA  . LEU B 29  ? 0.72392 0.59511 0.77651 0.06547  0.15114  0.10317  75  LEU B CA  
1516 C C   . LEU B 29  ? 0.73862 0.61168 0.79830 0.05178  0.13036  0.09260  75  LEU B C   
1517 O O   . LEU B 29  ? 0.77257 0.66552 0.86787 0.06123  0.14076  0.11835  75  LEU B O   
1518 C CB  . LEU B 29  ? 0.78762 0.58900 0.79762 0.08145  0.18614  0.07835  75  LEU B CB  
1519 C CG  . LEU B 29  ? 0.76617 0.53378 0.78642 0.09839  0.21713  0.08207  75  LEU B CG  
1520 C CD1 . LEU B 29  ? 0.75502 0.56375 0.83056 0.12407  0.24702  0.13351  75  LEU B CD1 
1521 C CD2 . LEU B 29  ? 0.87032 0.55281 0.82948 0.10566  0.24444  0.04823  75  LEU B CD2 
1522 N N   . ASP B 30  ? 0.75061 0.60524 0.77989 0.03138  0.10338  0.05925  76  ASP B N   
1523 C CA  . ASP B 30  ? 0.69747 0.54368 0.72945 0.02243  0.09123  0.04751  76  ASP B CA  
1524 C C   . ASP B 30  ? 0.65403 0.52335 0.68072 0.00281  0.05796  0.04260  76  ASP B C   
1525 O O   . ASP B 30  ? 0.63344 0.49408 0.66028 -0.00215 0.05141  0.03430  76  ASP B O   
1526 C CB  . ASP B 30  ? 0.70045 0.49059 0.70333 0.01877  0.09710  0.01400  76  ASP B CB  
1527 C CG  . ASP B 30  ? 0.82653 0.57299 0.82183 0.03657  0.13267  0.01277  76  ASP B CG  
1528 O OD1 . ASP B 30  ? 0.81075 0.57072 0.83928 0.05500  0.15650  0.04015  76  ASP B OD1 
1529 O OD2 . ASP B 30  ? 0.92281 0.61680 0.87541 0.03097  0.13674  -0.01528 76  ASP B OD2 
1530 N N   . ASN B 31  ? 0.67886 0.57221 0.69931 -0.00759 0.03957  0.04825  77  ASN B N   
1531 C CA  . ASN B 31  ? 0.66056 0.55867 0.66467 -0.02536 0.01284  0.03858  77  ASN B CA  
1532 C C   . ASN B 31  ? 0.65032 0.56696 0.66279 -0.02890 0.00479  0.05630  77  ASN B C   
1533 O O   . ASN B 31  ? 0.65638 0.55778 0.65204 -0.03472 -0.00267 0.04374  77  ASN B O   
1534 C CB  . ASN B 31  ? 0.63716 0.55006 0.63079 -0.03726 -0.00456 0.04097  77  ASN B CB  
1535 C CG  . ASN B 31  ? 0.63331 0.58489 0.64584 -0.04339 -0.01567 0.07363  77  ASN B CG  
1536 O OD1 . ASN B 31  ? 0.68085 0.63879 0.67955 -0.06013 -0.03811 0.07793  77  ASN B OD1 
1537 N ND2 . ASN B 31  ? 0.63708 0.61215 0.67949 -0.03063 0.00041  0.09929  77  ASN B ND2 
1538 N N   . LYS B 32  ? 0.66734 0.61747 0.70604 -0.02453 0.00769  0.08910  78  LYS B N   
1539 C CA  . LYS B 32  ? 0.58774 0.55777 0.62823 -0.03151 -0.00455 0.10917  78  LYS B CA  
1540 C C   . LYS B 32  ? 0.57837 0.52926 0.62151 -0.02068 0.01052  0.10101  78  LYS B C   
1541 O O   . LYS B 32  ? 0.58255 0.52621 0.60314 -0.02803 0.00016  0.09712  78  LYS B O   
1542 C CB  . LYS B 32  ? 0.59880 0.61570 0.67681 -0.02941 -0.00519 0.15338  78  LYS B CB  
1543 C CG  . LYS B 32  ? 0.64856 0.69457 0.72966 -0.04670 -0.02848 0.17226  78  LYS B CG  
1544 C CD  . LYS B 32  ? 0.74289 0.84124 0.88052 -0.03791 -0.02025 0.22421  78  LYS B CD  
1545 C CE  . LYS B 32  ? 0.83909 0.96947 0.99985 -0.04618 -0.03093 0.24884  78  LYS B CE  
1546 N NZ  . LYS B 32  ? 1.02709 1.17759 1.17071 -0.08157 -0.07596 0.26246  78  LYS B NZ  
1547 N N   . GLN B 33  ? 0.61068 0.54680 0.67689 -0.00327 0.03670  0.09758  79  GLN B N   
1548 C CA  . GLN B 33  ? 0.57827 0.49685 0.65425 0.00569  0.05077  0.09357  79  GLN B CA  
1549 C C   . GLN B 33  ? 0.61123 0.49717 0.66420 -0.00158 0.04449  0.06266  79  GLN B C   
1550 O O   . GLN B 33  ? 0.63232 0.51333 0.68735 0.00012  0.04650  0.06427  79  GLN B O   
1551 C CB  . GLN B 33  ? 0.59622 0.49958 0.70022 0.02421  0.08099  0.09919  79  GLN B CB  
1552 C CG  . GLN B 33  ? 0.59603 0.47501 0.71279 0.03122  0.09530  0.09347  79  GLN B CG  
1553 C CD  . GLN B 33  ? 0.66928 0.53065 0.81398 0.05045  0.12819  0.10572  79  GLN B CD  
1554 O OE1 . GLN B 33  ? 0.65403 0.48558 0.78811 0.05680  0.14438  0.09394  79  GLN B OE1 
1555 N NE2 . GLN B 33  ? 0.74144 0.61554 0.91763 0.06094  0.14106  0.12954  79  GLN B NE2 
1556 N N   . VAL B 34  ? 0.63885 0.50585 0.67384 -0.00878 0.03794  0.03930  80  VAL B N   
1557 C CA  . VAL B 34  ? 0.67242 0.51708 0.69337 -0.01683 0.02968  0.01772  80  VAL B CA  
1558 C C   . VAL B 34  ? 0.66389 0.51588 0.66535 -0.02277 0.01770  0.02155  80  VAL B C   
1559 O O   . VAL B 34  ? 0.64965 0.48969 0.65184 -0.02062 0.02164  0.01879  80  VAL B O   
1560 C CB  . VAL B 34  ? 0.63048 0.45982 0.63580 -0.02483 0.02221  -0.00236 80  VAL B CB  
1561 C CG1 . VAL B 34  ? 0.63937 0.46200 0.63251 -0.03462 0.00852  -0.01383 80  VAL B CG1 
1562 C CG2 . VAL B 34  ? 0.60990 0.41015 0.61944 -0.02262 0.03378  -0.01447 80  VAL B CG2 
1563 N N   . VAL B 35  ? 0.63307 0.50119 0.61513 -0.03033 0.00456  0.03038  81  VAL B N   
1564 C CA  . VAL B 35  ? 0.69264 0.55292 0.63974 -0.03841 -0.00628 0.03040  81  VAL B CA  
1565 C C   . VAL B 35  ? 0.67513 0.53760 0.61935 -0.03161 0.00159  0.04524  81  VAL B C   
1566 O O   . VAL B 35  ? 0.67671 0.51766 0.59889 -0.02863 0.00743  0.03975  81  VAL B O   
1567 C CB  . VAL B 35  ? 0.68473 0.55629 0.60812 -0.05376 -0.02653 0.03691  81  VAL B CB  
1568 C CG1 . VAL B 35  ? 0.74149 0.59543 0.61720 -0.06415 -0.03718 0.03855  81  VAL B CG1 
1569 C CG2 . VAL B 35  ? 0.72743 0.58977 0.64667 -0.05960 -0.03250 0.02046  81  VAL B CG2 
1570 N N   . LEU B 36  ? 0.64842 0.53742 0.61581 -0.02701 0.00467  0.06787  82  LEU B N   
1571 C CA  . LEU B 36  ? 0.63402 0.52822 0.60606 -0.01815 0.01483  0.08472  82  LEU B CA  
1572 C C   . LEU B 36  ? 0.65966 0.53188 0.64633 -0.00613 0.03323  0.07408  82  LEU B C   
1573 O O   . LEU B 36  ? 0.64571 0.50414 0.60863 -0.00254 0.03864  0.07595  82  LEU B O   
1574 C CB  . LEU B 36  ? 0.58365 0.50954 0.59791 -0.00927 0.02341  0.11199  82  LEU B CB  
1575 C CG  . LEU B 36  ? 0.58091 0.53655 0.58286 -0.01683 0.00952  0.14268  82  LEU B CG  
1576 C CD1 . LEU B 36  ? 0.58260 0.57154 0.63982 -0.00275 0.02483  0.17459  82  LEU B CD1 
1577 C CD2 . LEU B 36  ? 0.58201 0.51838 0.54537 -0.01631 0.01108  0.14060  82  LEU B CD2 
1578 N N   . THR B 37  ? 0.64504 0.51241 0.67048 -0.00004 0.04404  0.06640  83  THR B N   
1579 C CA  . THR B 37  ? 0.60450 0.45449 0.65335 0.00649  0.05678  0.06078  83  THR B CA  
1580 C C   . THR B 37  ? 0.64722 0.48128 0.67331 0.00419  0.05442  0.05154  83  THR B C   
1581 O O   . THR B 37  ? 0.66629 0.49530 0.69699 0.01331  0.06700  0.06195  83  THR B O   
1582 C CB  . THR B 37  ? 0.55930 0.39508 0.63387 0.00381  0.05940  0.04678  83  THR B CB  
1583 O OG1 . THR B 37  ? 0.57664 0.42089 0.66097 0.00836  0.06558  0.05425  83  THR B OG1 
1584 C CG2 . THR B 37  ? 0.52752 0.34938 0.63666 0.00760  0.07077  0.05000  83  THR B CG2 
1585 N N   . PHE B 38  ? 0.64838 0.47418 0.65157 -0.00553 0.04192  0.03550  84  PHE B N   
1586 C CA  . PHE B 38  ? 0.67931 0.48763 0.66632 -0.00452 0.04489  0.03013  84  PHE B CA  
1587 C C   . PHE B 38  ? 0.72046 0.51567 0.66086 0.00070  0.05155  0.03779  84  PHE B C   
1588 O O   . PHE B 38  ? 0.73551 0.51672 0.67358 0.01275  0.06932  0.04583  84  PHE B O   
1589 C CB  . PHE B 38  ? 0.68185 0.48405 0.65636 -0.01532 0.03143  0.01395  84  PHE B CB  
1590 C CG  . PHE B 38  ? 0.70324 0.48760 0.66672 -0.01166 0.03840  0.01280  84  PHE B CG  
1591 C CD1 . PHE B 38  ? 0.76298 0.54914 0.76699 -0.00632 0.04716  0.02073  84  PHE B CD1 
1592 C CD2 . PHE B 38  ? 0.75622 0.51964 0.67025 -0.01353 0.03778  0.00753  84  PHE B CD2 
1593 C CE1 . PHE B 38  ? 0.79670 0.56999 0.79904 0.00111  0.05881  0.02726  84  PHE B CE1 
1594 C CE2 . PHE B 38  ? 0.77926 0.51939 0.68221 -0.00584 0.05149  0.00867  84  PHE B CE2 
1595 C CZ  . PHE B 38  ? 0.75315 0.50098 0.70337 0.00366  0.06406  0.02056  84  PHE B CZ  
1596 N N   . LYS B 39  ? 0.74408 0.54163 0.64467 -0.00923 0.03747  0.03769  85  LYS B N   
1597 C CA  . LYS B 39  ? 0.72424 0.50273 0.56575 -0.01035 0.03827  0.04391  85  LYS B CA  
1598 C C   . LYS B 39  ? 0.77413 0.55516 0.62344 0.00540  0.05781  0.06185  85  LYS B C   
1599 O O   . LYS B 39  ? 0.82584 0.57720 0.63160 0.01407  0.07311  0.06438  85  LYS B O   
1600 C CB  . LYS B 39  ? 0.76843 0.56312 0.58429 -0.02845 0.01335  0.04986  85  LYS B CB  
1601 C CG  . LYS B 39  ? 0.91450 0.67833 0.65048 -0.04274 0.00088  0.04849  85  LYS B CG  
1602 C CD  . LYS B 39  ? 0.96182 0.75246 0.68581 -0.06573 -0.03021 0.06281  85  LYS B CD  
1603 C CE  . LYS B 39  ? 0.90205 0.71506 0.66130 -0.07648 -0.04597 0.05795  85  LYS B CE  
1604 N NZ  . LYS B 39  ? 0.94654 0.78642 0.69718 -0.10077 -0.07725 0.07747  85  LYS B NZ  
1605 N N   . LEU B 40  ? 0.73717 0.54924 0.64024 0.01110  0.06114  0.07553  86  LEU B N   
1606 C CA  . LEU B 40  ? 0.69193 0.51101 0.60752 0.02555  0.07884  0.09647  86  LEU B CA  
1607 C C   . LEU B 40  ? 0.69572 0.50314 0.64441 0.04135  0.10231  0.09973  86  LEU B C   
1608 O O   . LEU B 40  ? 0.71760 0.51804 0.65450 0.05548  0.12144  0.11604  86  LEU B O   
1609 C CB  . LEU B 40  ? 0.68103 0.53438 0.64649 0.02719  0.07714  0.11296  86  LEU B CB  
1610 C CG  . LEU B 40  ? 0.63203 0.50805 0.57264 0.01649  0.05927  0.12807  86  LEU B CG  
1611 C CD1 . LEU B 40  ? 0.58047 0.48980 0.58021 0.02437  0.06628  0.15036  86  LEU B CD1 
1612 C CD2 . LEU B 40  ? 0.68105 0.54446 0.55908 0.01540  0.05839  0.13955  86  LEU B CD2 
1613 N N   . VAL B 41  ? 0.68259 0.49016 0.67429 0.03862  0.10077  0.08884  87  VAL B N   
1614 C CA  . VAL B 41  ? 0.67786 0.48222 0.71171 0.05063  0.11957  0.10045  87  VAL B CA  
1615 C C   . VAL B 41  ? 0.76574 0.54462 0.76546 0.05852  0.13243  0.09859  87  VAL B C   
1616 O O   . VAL B 41  ? 0.80145 0.57466 0.81772 0.07567  0.15707  0.11764  87  VAL B O   
1617 C CB  . VAL B 41  ? 0.57433 0.38938 0.67095 0.04101  0.11007  0.09559  87  VAL B CB  
1618 C CG1 . VAL B 41  ? 0.59914 0.42541 0.71776 0.03491  0.10242  0.09370  87  VAL B CG1 
1619 C CG2 . VAL B 41  ? 0.69277 0.50054 0.77943 0.02858  0.09459  0.07661  87  VAL B CG2 
1620 N N   . HIS B 42  ? 0.79989 0.56126 0.75312 0.04811  0.11953  0.07884  88  HIS B N   
1621 C CA  . HIS B 42  ? 0.81618 0.54586 0.73637 0.05659  0.13505  0.07626  88  HIS B CA  
1622 C C   . HIS B 42  ? 0.91632 0.61320 0.77617 0.07338  0.16090  0.08633  88  HIS B C   
1623 O O   . HIS B 42  ? 0.98004 0.65697 0.84180 0.09386  0.19174  0.10048  88  HIS B O   
1624 C CB  . HIS B 42  ? 0.80990 0.52414 0.68931 0.04016  0.11494  0.05308  88  HIS B CB  
1625 C CG  . HIS B 42  ? 0.87797 0.56545 0.74776 0.04757  0.12947  0.05096  88  HIS B CG  
1626 N ND1 . HIS B 42  ? 0.92655 0.63042 0.86113 0.05690  0.14120  0.06652  88  HIS B ND1 
1627 C CD2 . HIS B 42  ? 0.91424 0.55914 0.72024 0.04615  0.13409  0.03807  88  HIS B CD2 
1628 C CE1 . HIS B 42  ? 0.89558 0.57275 0.81165 0.06413  0.15521  0.06615  88  HIS B CE1 
1629 N NE2 . HIS B 42  ? 0.87518 0.51171 0.71060 0.05870  0.15313  0.04691  88  HIS B NE2 
1630 N N   . HIS B 43  ? 0.91846 0.61035 0.72501 0.06545  0.14978  0.08311  89  HIS B N   
1631 C CA  . HIS B 43  ? 0.97972 0.63183 0.70507 0.07519  0.16794  0.08827  89  HIS B CA  
1632 C C   . HIS B 43  ? 0.98133 0.65192 0.72614 0.09149  0.18605  0.11402  89  HIS B C   
1633 O O   . HIS B 43  ? 1.11171 0.74663 0.79526 0.10699  0.21149  0.12320  89  HIS B O   
1634 C CB  . HIS B 43  ? 1.03968 0.67369 0.68679 0.05068  0.13862  0.07228  89  HIS B CB  
1635 C CG  . HIS B 43  ? 1.15023 0.76086 0.77283 0.03475  0.12266  0.04887  89  HIS B CG  
1636 N ND1 . HIS B 43  ? 1.09485 0.73963 0.75351 0.01412  0.09073  0.03964  89  HIS B ND1 
1637 C CD2 . HIS B 43  ? 1.24305 0.79752 0.81038 0.03858  0.13788  0.03507  89  HIS B CD2 
1638 C CE1 . HIS B 43  ? 1.13922 0.75415 0.76809 0.00437  0.08410  0.02168  89  HIS B CE1 
1639 N NE2 . HIS B 43  ? 1.21682 0.77558 0.79060 0.01844  0.11209  0.01805  89  HIS B NE2 
1640 N N   . SER B 44  ? 0.92503 0.64452 0.75029 0.08987  0.17708  0.12637  90  SER B N   
1641 C CA  . SER B 44  ? 0.91995 0.65914 0.76442 0.10290  0.19120  0.15211  90  SER B CA  
1642 C C   . SER B 44  ? 0.92845 0.66213 0.80852 0.12975  0.22905  0.17538  90  SER B C   
1643 O O   . SER B 44  ? 0.96596 0.70132 0.89647 0.13535  0.23852  0.17720  90  SER B O   
1644 C CB  . SER B 44  ? 0.85042 0.63568 0.76926 0.09341  0.17315  0.15829  90  SER B CB  
1645 O OG  . SER B 44  ? 0.96756 0.77109 0.90074 0.10533  0.18616  0.18480  90  SER B OG  
1646 N N   . LYS B 45  ? 0.88089 0.61264 0.73884 0.14612  0.25020  0.19829  91  LYS B N   
1647 C CA  . LYS B 45  ? 0.87078 0.60514 0.77051 0.17408  0.28880  0.22903  91  LYS B CA  
1648 C C   . LYS B 45  ? 0.87208 0.65437 0.86642 0.17674  0.28827  0.25447  91  LYS B C   
1649 O O   . LYS B 45  ? 0.91003 0.70602 0.97374 0.19266  0.31136  0.28028  91  LYS B O   
1650 C CB  . LYS B 45  ? 1.02729 0.72000 0.83209 0.19439  0.31960  0.24036  91  LYS B CB  
1651 C CG  . LYS B 45  ? 1.16828 0.79680 0.87310 0.19521  0.32925  0.21634  91  LYS B CG  
1652 C CD  . LYS B 45  ? 1.22516 0.79619 0.80777 0.20903  0.35484  0.21962  91  LYS B CD  
1653 C CE  . LYS B 45  ? 1.40352 0.89858 0.89219 0.21231  0.37149  0.19513  91  LYS B CE  
1654 N NZ  . LYS B 45  ? 1.50329 0.98742 0.95605 0.17655  0.32615  0.15868  91  LYS B NZ  
1655 N N   . LYS B 46  ? 0.90604 0.69545 0.54284 0.03886  0.04765  -0.07087 92  LYS B N   
1656 C CA  . LYS B 46  ? 0.82723 0.67998 0.50685 0.02388  0.05497  -0.03529 92  LYS B CA  
1657 C C   . LYS B 46  ? 0.85547 0.68741 0.56270 0.01222  0.03000  -0.00409 92  LYS B C   
1658 O O   . LYS B 46  ? 0.87332 0.67106 0.54978 -0.00841 0.00887  0.00836  92  LYS B O   
1659 C CB  . LYS B 46  ? 0.85890 0.74925 0.50461 -0.00945 0.06355  -0.01645 92  LYS B CB  
1660 C CG  . LYS B 46  ? 0.99231 0.91592 0.59682 -0.00853 0.09092  -0.04652 92  LYS B CG  
1661 C CD  . LYS B 46  ? 1.02599 1.01911 0.63011 -0.03813 0.10555  -0.01391 92  LYS B CD  
1662 C CE  . LYS B 46  ? 1.12559 1.17923 0.70868 -0.03240 0.14263  -0.04490 92  LYS B CE  
1663 N NZ  . LYS B 46  ? 0.99556 1.04136 0.59960 0.01489  0.16175  -0.09724 92  LYS B NZ  
1664 N N   . ILE B 47  ? 0.81615 0.67649 0.57956 0.02149  0.03363  0.00697  93  ILE B N   
1665 C CA  . ILE B 47  ? 0.74980 0.60641 0.54173 0.00844  0.01928  0.03174  93  ILE B CA  
1666 C C   . ILE B 47  ? 0.72479 0.62349 0.55448 -0.00427 0.03538  0.05020  93  ILE B C   
1667 O O   . ILE B 47  ? 0.73561 0.67095 0.58738 0.00041  0.05355  0.04315  93  ILE B O   
1668 C CB  . ILE B 47  ? 0.76051 0.60746 0.57794 0.02411  0.00741  0.02537  93  ILE B CB  
1669 C CG1 . ILE B 47  ? 0.76007 0.55155 0.54456 0.03744  -0.01111 0.01232  93  ILE B CG1 
1670 C CG2 . ILE B 47  ? 0.68679 0.54189 0.52837 0.00717  -0.00079 0.04416  93  ILE B CG2 
1671 C CD1 . ILE B 47  ? 0.78764 0.54057 0.54655 0.01564  -0.03451 0.02856  93  ILE B CD1 
1672 N N   . THR B 48  ? 0.73161 0.62505 0.57308 -0.02040 0.02893  0.07480  94  THR B N   
1673 C CA  . THR B 48  ? 0.69445 0.60746 0.57825 -0.02992 0.04206  0.09227  94  THR B CA  
1674 C C   . THR B 48  ? 0.64492 0.54754 0.56002 -0.02990 0.03754  0.09251  94  THR B C   
1675 O O   . THR B 48  ? 0.64437 0.53438 0.54870 -0.03135 0.02333  0.09972  94  THR B O   
1676 C CB  . THR B 48  ? 0.72762 0.64609 0.60476 -0.04484 0.04161  0.12468  94  THR B CB  
1677 O OG1 . THR B 48  ? 0.83240 0.76544 0.66347 -0.05008 0.04501  0.11991  94  THR B OG1 
1678 C CG2 . THR B 48  ? 0.65624 0.58242 0.58044 -0.05319 0.05551  0.14543  94  THR B CG2 
1679 N N   . LEU B 49  ? 0.63807 0.55072 0.58885 -0.03252 0.05061  0.08253  95  LEU B N   
1680 C CA  . LEU B 49  ? 0.63073 0.53859 0.60512 -0.03514 0.05194  0.07269  95  LEU B CA  
1681 C C   . LEU B 49  ? 0.66551 0.56226 0.68102 -0.04185 0.06902  0.07923  95  LEU B C   
1682 O O   . LEU B 49  ? 0.70911 0.60746 0.73955 -0.05125 0.08019  0.07880  95  LEU B O   
1683 C CB  . LEU B 49  ? 0.60827 0.53425 0.58184 -0.03657 0.04968  0.04840  95  LEU B CB  
1684 C CG  . LEU B 49  ? 0.57048 0.49361 0.51178 -0.02635 0.02909  0.04743  95  LEU B CG  
1685 C CD1 . LEU B 49  ? 0.58354 0.53251 0.52995 -0.02114 0.02357  0.03441  95  LEU B CD1 
1686 C CD2 . LEU B 49  ? 0.61488 0.52907 0.54640 -0.03289 0.01838  0.05308  95  LEU B CD2 
1687 N N   . ILE B 50  ? 0.68749 0.57298 0.72550 -0.03685 0.07162  0.08622  96  ILE B N   
1688 C CA  . ILE B 50  ? 0.74621 0.60831 0.83235 -0.03512 0.08844  0.09262  96  ILE B CA  
1689 C C   . ILE B 50  ? 0.70460 0.56341 0.81231 -0.03241 0.10254  0.06124  96  ILE B C   
1690 O O   . ILE B 50  ? 0.72012 0.59805 0.82759 -0.02393 0.09917  0.06209  96  ILE B O   
1691 C CB  . ILE B 50  ? 0.67215 0.53005 0.77905 -0.02480 0.08161  0.13528  96  ILE B CB  
1692 C CG1 . ILE B 50  ? 0.60957 0.48506 0.67231 -0.03241 0.06395  0.16026  96  ILE B CG1 
1693 C CG2 . ILE B 50  ? 0.68678 0.51028 0.84537 -0.02204 0.09592  0.15007  96  ILE B CG2 
1694 C CD1 . ILE B 50  ? 0.53586 0.41991 0.60944 -0.02992 0.05158  0.20396  96  ILE B CD1 
1695 N N   . GLY B 51  ? 0.70591 0.54485 0.82988 -0.04399 0.11945  0.03224  97  GLY B N   
1696 C CA  . GLY B 51  ? 0.77917 0.61671 0.91449 -0.04581 0.13681  -0.00661 97  GLY B CA  
1697 C C   . GLY B 51  ? 0.77926 0.59798 0.91387 -0.07055 0.14962  -0.04308 97  GLY B C   
1698 O O   . GLY B 51  ? 0.73593 0.54249 0.87177 -0.08496 0.14572  -0.03259 97  GLY B O   
1699 N N   . ASP B 52  ? 0.81712 0.64060 0.94715 -0.07987 0.16558  -0.08682 98  ASP B N   
1700 C CA  . ASP B 52  ? 0.81575 0.62119 0.93975 -0.11065 0.17833  -0.12951 98  ASP B CA  
1701 C C   . ASP B 52  ? 0.77461 0.61257 0.87233 -0.13551 0.15705  -0.11821 98  ASP B C   
1702 O O   . ASP B 52  ? 0.73655 0.62398 0.80689 -0.13093 0.13558  -0.09938 98  ASP B O   
1703 C CB  . ASP B 52  ? 0.90932 0.74244 1.00857 -0.12410 0.19235  -0.17797 98  ASP B CB  
1704 C CG  . ASP B 52  ? 1.08036 0.89654 1.16434 -0.16375 0.20515  -0.22915 98  ASP B CG  
1705 O OD1 . ASP B 52  ? 1.17920 0.92649 1.29505 -0.16855 0.22174  -0.24357 98  ASP B OD1 
1706 O OD2 . ASP B 52  ? 1.02769 0.89825 1.06663 -0.19403 0.19604  -0.25220 98  ASP B OD2 
1707 N N   . ALA B 53  ? 0.88516 0.69370 0.99749 -0.16054 0.16319  -0.12689 99  ALA B N   
1708 C CA  . ALA B 53  ? 0.79740 0.64832 0.89830 -0.18337 0.14614  -0.11224 99  ALA B CA  
1709 C C   . ALA B 53  ? 0.79746 0.72000 0.86400 -0.19615 0.12828  -0.12532 99  ALA B C   
1710 O O   . ALA B 53  ? 0.73635 0.71010 0.79715 -0.19092 0.10925  -0.10070 99  ALA B O   
1711 C CB  . ALA B 53  ? 0.83265 0.64779 0.95146 -0.22158 0.15667  -0.12889 99  ALA B CB  
1712 N N   . ASN B 54  ? 0.97091 0.90064 1.01562 -0.21166 0.13462  -0.16289 100 ASN B N   
1713 C CA  . ASN B 54  ? 0.94642 0.94792 0.95629 -0.22792 0.11359  -0.16758 100 ASN B CA  
1714 C C   . ASN B 54  ? 0.90909 0.93685 0.90573 -0.19422 0.09504  -0.13278 100 ASN B C   
1715 O O   . ASN B 54  ? 0.88188 0.95181 0.87461 -0.18653 0.07076  -0.10550 100 ASN B O   
1716 C CB  . ASN B 54  ? 0.99694 1.00323 0.97808 -0.25949 0.12731  -0.21751 100 ASN B CB  
1717 C CG  . ASN B 54  ? 1.06895 1.15428 1.01494 -0.29483 0.10267  -0.22175 100 ASN B CG  
1718 O OD1 . ASN B 54  ? 1.01886 1.15534 0.96608 -0.28264 0.07374  -0.18173 100 ASN B OD1 
1719 N ND2 . ASN B 54  ? 1.23615 1.33340 1.15090 -0.33888 0.11319  -0.27030 100 ASN B ND2 
1720 N N   . LYS B 55  ? 0.87047 0.87297 0.86427 -0.17381 0.10658  -0.13358 101 LYS B N   
1721 C CA  . LYS B 55  ? 0.74377 0.76966 0.71781 -0.15417 0.08784  -0.10477 101 LYS B CA  
1722 C C   . LYS B 55  ? 0.70652 0.72616 0.68830 -0.12810 0.06880  -0.06574 101 LYS B C   
1723 O O   . LYS B 55  ? 0.70026 0.74348 0.66275 -0.12049 0.04454  -0.04438 101 LYS B O   
1724 C CB  . LYS B 55  ? 0.70773 0.71377 0.68831 -0.13884 0.10618  -0.10950 101 LYS B CB  
1725 C CG  . LYS B 55  ? 0.75760 0.76143 0.73884 -0.15688 0.13636  -0.15823 101 LYS B CG  
1726 C CD  . LYS B 55  ? 0.78612 0.77524 0.79359 -0.13210 0.15988  -0.16184 101 LYS B CD  
1727 C CE  . LYS B 55  ? 0.82486 0.86055 0.80638 -0.14981 0.17697  -0.19553 101 LYS B CE  
1728 N NZ  . LYS B 55  ? 0.91409 0.94398 0.93652 -0.12103 0.20678  -0.20380 101 LYS B NZ  
1729 N N   . ILE B 56  ? 0.70015 0.68673 0.70825 -0.11580 0.07967  -0.05643 102 ILE B N   
1730 C CA  . ILE B 56  ? 0.66088 0.64614 0.66841 -0.09341 0.06652  -0.02624 102 ILE B CA  
1731 C C   . ILE B 56  ? 0.66492 0.69285 0.67385 -0.09678 0.05315  -0.02347 102 ILE B C   
1732 O O   . ILE B 56  ? 0.65961 0.69722 0.66066 -0.07491 0.03849  -0.00629 102 ILE B O   
1733 C CB  . ILE B 56  ? 0.65402 0.60305 0.68353 -0.08414 0.08106  -0.01171 102 ILE B CB  
1734 C CG1 . ILE B 56  ? 0.61400 0.55811 0.66840 -0.10555 0.09560  -0.02218 102 ILE B CG1 
1735 C CG2 . ILE B 56  ? 0.69735 0.61506 0.73702 -0.07366 0.09037  -0.00672 102 ILE B CG2 
1736 C CD1 . ILE B 56  ? 0.61611 0.52764 0.69057 -0.10090 0.10568  0.00240  102 ILE B CD1 
1737 N N   . LEU B 57  ? 0.66619 0.72193 0.68820 -0.12364 0.05796  -0.04124 103 LEU B N   
1738 C CA  . LEU B 57  ? 0.61004 0.72556 0.64263 -0.12614 0.04257  -0.03423 103 LEU B CA  
1739 C C   . LEU B 57  ? 0.62673 0.77581 0.64132 -0.11913 0.01587  -0.02468 103 LEU B C   
1740 O O   . LEU B 57  ? 0.60991 0.79102 0.63691 -0.09666 -0.00089 -0.00606 103 LEU B O   
1741 C CB  . LEU B 57  ? 0.60126 0.74662 0.65111 -0.16554 0.04995  -0.05309 103 LEU B CB  
1742 C CG  . LEU B 57  ? 0.52252 0.65882 0.59953 -0.17431 0.06736  -0.04781 103 LEU B CG  
1743 C CD1 . LEU B 57  ? 0.58942 0.72647 0.67555 -0.22286 0.07583  -0.07183 103 LEU B CD1 
1744 C CD2 . LEU B 57  ? 0.56627 0.76493 0.66386 -0.15602 0.05964  -0.02726 103 LEU B CD2 
1745 N N   . GLN B 58  ? 0.62861 0.77250 0.61609 -0.13741 0.01227  -0.03555 104 GLN B N   
1746 C CA  . GLN B 58  ? 0.61691 0.79233 0.58300 -0.13690 -0.01615 -0.01749 104 GLN B CA  
1747 C C   . GLN B 58  ? 0.64827 0.78701 0.60743 -0.10024 -0.02982 0.00989  104 GLN B C   
1748 O O   . GLN B 58  ? 0.67221 0.82853 0.63252 -0.08529 -0.05675 0.03426  104 GLN B O   
1749 C CB  . GLN B 58  ? 0.65958 0.84066 0.59094 -0.16702 -0.01288 -0.03374 104 GLN B CB  
1750 C CG  . GLN B 58  ? 0.70283 0.89528 0.62736 -0.20501 0.00863  -0.07435 104 GLN B CG  
1751 C CD  . GLN B 58  ? 0.76068 0.97425 0.64394 -0.23136 0.01060  -0.08925 104 GLN B CD  
1752 O OE1 . GLN B 58  ? 0.80046 0.98369 0.67589 -0.22022 0.02763  -0.09477 104 GLN B OE1 
1753 N NE2 . GLN B 58  ? 0.77043 1.04751 0.62741 -0.26955 -0.00665 -0.09441 104 GLN B NE2 
1754 N N   . TYR B 59  ? 0.63898 0.72465 0.59023 -0.08839 -0.01395 0.00735  105 TYR B N   
1755 C CA  . TYR B 59  ? 0.61431 0.65973 0.55144 -0.06266 -0.02693 0.02852  105 TYR B CA  
1756 C C   . TYR B 59  ? 0.66172 0.70142 0.61645 -0.03225 -0.02959 0.03446  105 TYR B C   
1757 O O   . TYR B 59  ? 0.71189 0.73439 0.66024 -0.01025 -0.04962 0.04944  105 TYR B O   
1758 C CB  . TYR B 59  ? 0.62490 0.63039 0.55338 -0.06255 -0.01051 0.02597  105 TYR B CB  
1759 C CG  . TYR B 59  ? 0.65009 0.65407 0.55449 -0.07732 -0.01873 0.03446  105 TYR B CG  
1760 C CD1 . TYR B 59  ? 0.67905 0.66974 0.55875 -0.07557 -0.04656 0.05889  105 TYR B CD1 
1761 C CD2 . TYR B 59  ? 0.63400 0.65033 0.54320 -0.09338 0.00263  0.01825  105 TYR B CD2 
1762 C CE1 . TYR B 59  ? 0.63760 0.63550 0.49447 -0.09632 -0.05439 0.07157  105 TYR B CE1 
1763 C CE2 . TYR B 59  ? 0.64432 0.67622 0.53455 -0.10834 -0.00097 0.02569  105 TYR B CE2 
1764 C CZ  . TYR B 59  ? 0.60384 0.63051 0.46629 -0.11306 -0.03026 0.05472  105 TYR B CZ  
1765 O OH  . TYR B 59  ? 0.62188 0.67156 0.46505 -0.13457 -0.03400 0.06683  105 TYR B OH  
1766 N N   . LYS B 60  ? 0.64498 0.69812 0.62269 -0.03113 -0.00812 0.02222  106 LYS B N   
1767 C CA  . LYS B 60  ? 0.60048 0.66525 0.59540 -0.00384 -0.00492 0.02405  106 LYS B CA  
1768 C C   . LYS B 60  ? 0.63529 0.74405 0.65307 0.01221  -0.02535 0.03306  106 LYS B C   
1769 O O   . LYS B 60  ? 0.72083 0.82221 0.74841 0.04741  -0.02995 0.03659  106 LYS B O   
1770 C CB  . LYS B 60  ? 0.61513 0.70564 0.63302 -0.01473 0.02048  0.01485  106 LYS B CB  
1771 C CG  . LYS B 60  ? 0.62435 0.75704 0.66677 0.00990  0.02748  0.01431  106 LYS B CG  
1772 C CD  . LYS B 60  ? 0.58125 0.73576 0.63593 -0.00256 0.05374  0.01172  106 LYS B CD  
1773 C CE  . LYS B 60  ? 0.57608 0.81497 0.67454 0.00021  0.06017  0.01037  106 LYS B CE  
1774 N NZ  . LYS B 60  ? 0.61045 0.87989 0.71576 0.02648  0.07989  0.00625  106 LYS B NZ  
1775 N N   . ASN B 61  ? 0.67017 0.82540 0.69716 -0.01207 -0.03868 0.03694  107 ASN B N   
1776 C CA  . ASN B 61  ? 0.67838 0.88756 0.73572 0.00428  -0.06255 0.05451  107 ASN B CA  
1777 C C   . ASN B 61  ? 0.70153 0.87529 0.74033 0.02022  -0.09329 0.07911  107 ASN B C   
1778 O O   . ASN B 61  ? 0.71609 0.89058 0.78177 0.05851  -0.10934 0.09527  107 ASN B O   
1779 C CB  . ASN B 61  ? 0.65143 0.93700 0.72519 -0.03346 -0.06921 0.05297  107 ASN B CB  
1780 C CG  . ASN B 61  ? 0.75770 1.08897 0.86538 -0.04348 -0.04629 0.03789  107 ASN B CG  
1781 O OD1 . ASN B 61  ? 0.83530 1.16716 0.93324 -0.08336 -0.03076 0.01890  107 ASN B OD1 
1782 N ND2 . ASN B 61  ? 0.80188 1.16966 0.95123 -0.00727 -0.04165 0.04509  107 ASN B ND2 
1783 N N   . TYR B 62  ? 0.67810 0.82092 0.67486 -0.00800 -0.10098 0.08336  108 TYR B N   
1784 C CA  . TYR B 62  ? 0.65181 0.75310 0.62605 0.00033  -0.13027 0.11149  108 TYR B CA  
1785 C C   . TYR B 62  ? 0.70309 0.72972 0.67508 0.03976  -0.12778 0.10959  108 TYR B C   
1786 O O   . TYR B 62  ? 0.76892 0.76721 0.75371 0.06993  -0.15107 0.12958  108 TYR B O   
1787 C CB  . TYR B 62  ? 0.67877 0.76571 0.60726 -0.03934 -0.13113 0.11321  108 TYR B CB  
1788 C CG  . TYR B 62  ? 0.72892 0.77922 0.63182 -0.04122 -0.16384 0.14896  108 TYR B CG  
1789 C CD1 . TYR B 62  ? 0.68378 0.76435 0.59801 -0.03987 -0.19948 0.18528  108 TYR B CD1 
1790 C CD2 . TYR B 62  ? 0.80087 0.78686 0.67151 -0.04614 -0.16263 0.15224  108 TYR B CD2 
1791 C CE1 . TYR B 62  ? 0.74699 0.78614 0.63917 -0.04429 -0.23295 0.22557  108 TYR B CE1 
1792 C CE2 . TYR B 62  ? 0.77326 0.72067 0.61935 -0.05496 -0.19520 0.18897  108 TYR B CE2 
1793 C CZ  . TYR B 62  ? 0.79169 0.76121 0.64803 -0.05396 -0.23021 0.22636  108 TYR B CZ  
1794 O OH  . TYR B 62  ? 0.89443 0.81935 0.72837 -0.06519 -0.26630 0.27058  108 TYR B OH  
1795 N N   . PHE B 63  ? 0.71045 0.70369 0.66709 0.03986  -0.09996 0.08505  109 PHE B N   
1796 C CA  . PHE B 63  ? 0.74633 0.66993 0.68697 0.06734  -0.09690 0.07768  109 PHE B CA  
1797 C C   . PHE B 63  ? 0.78350 0.71588 0.76097 0.11296  -0.09290 0.06907  109 PHE B C   
1798 O O   . PHE B 63  ? 0.89523 0.76369 0.86272 0.14193  -0.09999 0.06507  109 PHE B O   
1799 C CB  . PHE B 63  ? 0.65287 0.55790 0.57089 0.05333  -0.07011 0.05832  109 PHE B CB  
1800 C CG  . PHE B 63  ? 0.69055 0.57157 0.57618 0.02158  -0.07548 0.06797  109 PHE B CG  
1801 C CD1 . PHE B 63  ? 0.74296 0.60511 0.60910 0.00719  -0.10242 0.09050  109 PHE B CD1 
1802 C CD2 . PHE B 63  ? 0.70416 0.58948 0.58444 0.00547  -0.05381 0.05907  109 PHE B CD2 
1803 C CE1 . PHE B 63  ? 0.70534 0.56191 0.54641 -0.02376 -0.10422 0.09990  109 PHE B CE1 
1804 C CE2 . PHE B 63  ? 0.67729 0.55397 0.53987 -0.01879 -0.05663 0.06899  109 PHE B CE2 
1805 C CZ  . PHE B 63  ? 0.67811 0.54537 0.52095 -0.03399 -0.08007 0.08732  109 PHE B CZ  
1806 N N   . GLN B 64  ? 0.72061 0.73250 0.74294 0.11949  -0.08121 0.06456  110 GLN B N   
1807 C CA  . GLN B 64  ? 0.76596 0.80444 0.83207 0.16527  -0.07040 0.05384  110 GLN B CA  
1808 C C   . GLN B 64  ? 0.92465 0.96785 1.03102 0.20124  -0.10099 0.07901  110 GLN B C   
1809 O O   . GLN B 64  ? 0.96546 1.01514 1.11251 0.25103  -0.09214 0.06848  110 GLN B O   
1810 C CB  . GLN B 64  ? 0.71101 0.84317 0.81464 0.15430  -0.04576 0.04321  110 GLN B CB  
1811 C CG  . GLN B 64  ? 0.73070 0.85233 0.81269 0.14831  -0.01041 0.01758  110 GLN B CG  
1812 C CD  . GLN B 64  ? 0.69897 0.90546 0.81280 0.12520  0.01161  0.01355  110 GLN B CD  
1813 O OE1 . GLN B 64  ? 0.67136 0.92574 0.80441 0.09494  0.00100  0.02490  110 GLN B OE1 
1814 N NE2 . GLN B 64  ? 0.66556 0.89319 0.78133 0.13412  0.04234  -0.00308 110 GLN B NE2 
1815 N N   . ALA B 65  ? 0.95548 1.00260 1.05488 0.17789  -0.13569 0.11345  111 ALA B N   
1816 C CA  . ALA B 65  ? 0.97180 0.98731 1.09215 0.20625  -0.17373 0.14890  111 ALA B CA  
1817 C C   . ALA B 65  ? 1.02605 1.11553 1.22763 0.25324  -0.18091 0.16280  111 ALA B C   
1818 O O   . ALA B 65  ? 1.05784 1.10260 1.29364 0.30358  -0.19816 0.17774  111 ALA B O   
1819 C CB  . ALA B 65  ? 0.93289 0.82367 1.01995 0.23066  -0.17747 0.13968  111 ALA B CB  
1820 N N   . ASN B 66  ? 1.03160 1.23504 1.26896 0.23638  -0.16922 0.15984  112 ASN B N   
1821 C CA  . ASN B 66  ? 1.02832 1.32723 1.35240 0.27912  -0.16968 0.17007  112 ASN B CA  
1822 C C   . ASN B 66  ? 1.05867 1.32848 1.41377 0.34082  -0.13529 0.13456  112 ASN B C   
1823 O O   . ASN B 66  ? 1.05821 1.35610 1.48569 0.40110  -0.14084 0.14501  112 ASN B O   
1824 C CB  . ASN B 66  ? 1.02084 1.34789 1.39258 0.30083  -0.21909 0.22576  112 ASN B CB  
1825 C CG  . ASN B 66  ? 1.09957 1.43040 1.42045 0.23984  -0.25515 0.26086  112 ASN B CG  
1826 O OD1 . ASN B 66  ? 1.11277 1.54201 1.43464 0.19302  -0.26271 0.26981  112 ASN B OD1 
1827 N ND2 . ASN B 66  ? 1.17067 1.39706 1.44289 0.23483  -0.27685 0.27918  112 ASN B ND2 
1828 N N   . GLY B 67  ? 0.99735 1.21432 1.29873 0.32696  -0.09901 0.09230  113 GLY B N   
1829 C CA  . GLY B 67  ? 0.98164 1.17825 1.29858 0.37672  -0.06267 0.05274  113 GLY B CA  
1830 C C   . GLY B 67  ? 1.03316 1.09808 1.32181 0.41616  -0.06871 0.03803  113 GLY B C   
1831 O O   . GLY B 67  ? 1.10340 1.14843 1.40557 0.46275  -0.03750 -0.00119 113 GLY B O   
1832 N N   . ALA B 68  ? 1.05119 1.02549 1.29834 0.39578  -0.10633 0.06570  114 ALA B N   
1833 C CA  . ALA B 68  ? 1.11018 0.94493 1.31404 0.41707  -0.11016 0.04647  114 ALA B CA  
1834 C C   . ALA B 68  ? 1.12917 0.91331 1.25402 0.38384  -0.07946 0.00315  114 ALA B C   
1835 O O   . ALA B 68  ? 1.23186 0.90862 1.31542 0.39795  -0.07560 -0.02469 114 ALA B O   
1836 C CB  . ALA B 68  ? 1.18684 0.94197 1.36530 0.39524  -0.16033 0.09357  114 ALA B CB  
1837 N N   . ARG B 69  ? 1.03698 0.89289 1.14040 0.33823  -0.06036 -0.00096 115 ARG B N   
1838 C CA  . ARG B 69  ? 1.01670 0.84970 1.05696 0.30668  -0.03201 -0.03279 115 ARG B CA  
1839 C C   . ARG B 69  ? 1.02682 0.96683 1.09253 0.30124  0.00522  -0.04900 115 ARG B C   
1840 O O   . ARG B 69  ? 0.98983 0.94921 1.01977 0.25794  0.01936  -0.05096 115 ARG B O   
1841 C CB  . ARG B 69  ? 0.95933 0.75655 0.94408 0.24854  -0.05165 -0.01079 115 ARG B CB  
1842 C CG  . ARG B 69  ? 1.02125 0.73129 0.98403 0.24343  -0.09063 0.01452  115 ARG B CG  
1843 C CD  . ARG B 69  ? 1.05808 0.68813 0.94831 0.20651  -0.09496 0.00635  115 ARG B CD  
1844 N NE  . ARG B 69  ? 1.03888 0.58823 0.90713 0.19362  -0.13335 0.03461  115 ARG B NE  
1845 C CZ  . ARG B 69  ? 0.99205 0.56659 0.86575 0.16470  -0.16040 0.07678  115 ARG B CZ  
1846 N NH1 . ARG B 69  ? 0.95394 0.62541 0.85309 0.14741  -0.15326 0.08976  115 ARG B NH1 
1847 N NH2 . ARG B 69  ? 1.01441 0.51451 0.86336 0.14827  -0.19500 0.10538  115 ARG B NH2 
1848 N N   . SER B 70  ? 1.02975 1.04432 1.16335 0.34516  0.02088  -0.05688 116 SER B N   
1849 C CA  . SER B 70  ? 0.90894 1.03234 1.06957 0.33751  0.05724  -0.07033 116 SER B CA  
1850 C C   . SER B 70  ? 0.94720 1.05093 1.05654 0.33579  0.09566  -0.11149 116 SER B C   
1851 O O   . SER B 70  ? 1.00006 1.19064 1.11927 0.31963  0.12681  -0.11913 116 SER B O   
1852 C CB  . SER B 70  ? 0.91298 1.13466 1.16643 0.38593  0.06380  -0.06595 116 SER B CB  
1853 O OG  . SER B 70  ? 1.03238 1.19575 1.31091 0.45100  0.06131  -0.08291 116 SER B OG  
1854 N N   . ASP B 71  ? 1.04691 1.04130 1.09787 0.34548  0.09220  -0.13588 117 ASP B N   
1855 C CA  . ASP B 71  ? 1.09959 1.06646 1.08366 0.33361  0.12273  -0.17528 117 ASP B CA  
1856 C C   . ASP B 71  ? 1.09473 1.02865 1.00803 0.27046  0.11221  -0.15821 117 ASP B C   
1857 O O   . ASP B 71  ? 1.08007 1.01223 0.93696 0.24997  0.13447  -0.18077 117 ASP B O   
1858 C CB  . ASP B 71  ? 1.21250 1.07423 1.16705 0.37415  0.12413  -0.21675 117 ASP B CB  
1859 C CG  . ASP B 71  ? 1.22643 0.96779 1.15287 0.36345  0.07798  -0.19464 117 ASP B CG  
1860 O OD1 . ASP B 71  ? 1.16369 0.91350 1.09802 0.33012  0.04673  -0.14802 117 ASP B OD1 
1861 O OD2 . ASP B 71  ? 1.33300 0.96954 1.22668 0.38593  0.07452  -0.22652 117 ASP B OD2 
1862 N N   . ILE B 72  ? 1.04985 0.96293 0.96551 0.24000  0.07936  -0.11887 118 ILE B N   
1863 C CA  . ILE B 72  ? 0.95453 0.85269 0.82228 0.18713  0.07228  -0.09954 118 ILE B CA  
1864 C C   . ILE B 72  ? 0.96709 0.95619 0.85542 0.16293  0.09649  -0.08805 118 ILE B C   
1865 O O   . ILE B 72  ? 0.98629 1.04851 0.93340 0.17252  0.10414  -0.07985 118 ILE B O   
1866 C CB  . ILE B 72  ? 0.92004 0.77993 0.79116 0.16571  0.03631  -0.06572 118 ILE B CB  
1867 C CG1 . ILE B 72  ? 0.96928 0.73378 0.81242 0.17902  0.00987  -0.07022 118 ILE B CG1 
1868 C CG2 . ILE B 72  ? 0.87567 0.73401 0.71577 0.11930  0.03290  -0.04529 118 ILE B CG2 
1869 C CD1 . ILE B 72  ? 0.92640 0.65738 0.75432 0.14597  -0.02106 -0.03787 118 ILE B CD1 
1870 N N   . ASP B 73  ? 0.92505 0.91212 0.76588 0.12824  0.10629  -0.08373 119 ASP B N   
1871 C CA  . ASP B 73  ? 0.87553 0.93093 0.73089 0.09684  0.12335  -0.06236 119 ASP B CA  
1872 C C   . ASP B 73  ? 0.84632 0.87769 0.70992 0.06534  0.10170  -0.02779 119 ASP B C   
1873 O O   . ASP B 73  ? 0.86849 0.85380 0.69335 0.04559  0.08836  -0.01530 119 ASP B O   
1874 C CB  . ASP B 73  ? 0.90132 0.97392 0.70299 0.07678  0.14469  -0.07028 119 ASP B CB  
1875 C CG  . ASP B 73  ? 0.99915 1.13843 0.80856 0.09986  0.18020  -0.10235 119 ASP B CG  
1876 O OD1 . ASP B 73  ? 1.02927 1.22522 0.90271 0.12459  0.19011  -0.10606 119 ASP B OD1 
1877 O OD2 . ASP B 73  ? 1.06134 1.20476 0.81317 0.09188  0.19874  -0.12448 119 ASP B OD2 
1878 N N   . PHE B 74  ? 0.73924 0.80659 0.65455 0.06001  0.09924  -0.01461 120 PHE B N   
1879 C CA  . PHE B 74  ? 0.68952 0.73486 0.61662 0.03378  0.08469  0.00815  120 PHE B CA  
1880 C C   . PHE B 74  ? 0.71926 0.79009 0.65745 0.00204  0.09961  0.02835  120 PHE B C   
1881 O O   . PHE B 74  ? 0.82541 0.95264 0.78283 -0.00552 0.11869  0.02875  120 PHE B O   
1882 C CB  . PHE B 74  ? 0.65080 0.71469 0.61853 0.03851  0.07230  0.00727  120 PHE B CB  
1883 C CG  . PHE B 74  ? 0.70557 0.72685 0.66088 0.05738  0.04793  0.00400  120 PHE B CG  
1884 C CD1 . PHE B 74  ? 0.75729 0.78099 0.72141 0.09280  0.04251  -0.00842 120 PHE B CD1 
1885 C CD2 . PHE B 74  ? 0.67259 0.65230 0.61106 0.04053  0.03099  0.01540  120 PHE B CD2 
1886 C CE1 . PHE B 74  ? 0.76608 0.74158 0.71988 0.10732  0.01618  -0.00411 120 PHE B CE1 
1887 C CE2 . PHE B 74  ? 0.71816 0.66255 0.64259 0.05062  0.00701  0.01855  120 PHE B CE2 
1888 C CZ  . PHE B 74  ? 0.73649 0.67331 0.66689 0.08234  -0.00263 0.01136  120 PHE B CZ  
1889 N N   . TYR B 75  ? 0.71969 0.75053 0.65127 -0.01654 0.09052  0.04813  121 TYR B N   
1890 C CA  . TYR B 75  ? 0.68588 0.72265 0.63406 -0.04411 0.10046  0.07345  121 TYR B CA  
1891 C C   . TYR B 75  ? 0.69377 0.69322 0.66942 -0.05265 0.09208  0.07942  121 TYR B C   
1892 O O   . TYR B 75  ? 0.70837 0.67232 0.67235 -0.04642 0.07978  0.08564  121 TYR B O   
1893 C CB  . TYR B 75  ? 0.72247 0.75137 0.63377 -0.05430 0.10074  0.09619  121 TYR B CB  
1894 C CG  . TYR B 75  ? 0.84226 0.90975 0.71456 -0.04930 0.11395  0.08216  121 TYR B CG  
1895 C CD1 . TYR B 75  ? 0.94672 1.07638 0.83204 -0.05986 0.13676  0.08202  121 TYR B CD1 
1896 C CD2 . TYR B 75  ? 0.82684 0.87134 0.64725 -0.03829 0.10582  0.06712  121 TYR B CD2 
1897 C CE1 . TYR B 75  ? 0.94486 1.11966 0.79395 -0.05434 0.15537  0.06390  121 TYR B CE1 
1898 C CE2 . TYR B 75  ? 0.83310 0.90898 0.61234 -0.03410 0.12279  0.04489  121 TYR B CE2 
1899 C CZ  . TYR B 75  ? 0.90155 1.04589 0.69581 -0.03987 0.14962  0.04209  121 TYR B CZ  
1900 O OH  . TYR B 75  ? 0.96089 1.14564 0.71422 -0.03415 0.17244  0.01432  121 TYR B OH  
1901 N N   . LEU B 76  ? 0.71997 0.73144 0.73143 -0.06896 0.10015  0.07441  122 LEU B N   
1902 C CA  . LEU B 76  ? 0.65546 0.63183 0.69086 -0.07836 0.09832  0.06802  122 LEU B CA  
1903 C C   . LEU B 76  ? 0.72212 0.66286 0.78086 -0.09548 0.10732  0.09182  122 LEU B C   
1904 O O   . LEU B 76  ? 0.80359 0.75851 0.86866 -0.11344 0.11547  0.11231  122 LEU B O   
1905 C CB  . LEU B 76  ? 0.59543 0.60008 0.65081 -0.09183 0.09983  0.04358  122 LEU B CB  
1906 C CG  . LEU B 76  ? 0.57665 0.62300 0.62211 -0.07442 0.08760  0.02806  122 LEU B CG  
1907 C CD1 . LEU B 76  ? 0.56228 0.63945 0.62866 -0.09588 0.08467  0.01036  122 LEU B CD1 
1908 C CD2 . LEU B 76  ? 0.58129 0.59860 0.59895 -0.05162 0.07193  0.02677  122 LEU B CD2 
1909 N N   . GLN B 77  ? 0.89044 0.78713 0.96532 -0.08895 0.10621  0.09166  123 GLN B N   
1910 C CA  . GLN B 77  ? 0.93636 0.78683 1.04644 -0.09672 0.11408  0.11382  123 GLN B CA  
1911 C C   . GLN B 77  ? 0.94651 0.75916 1.08410 -0.09585 0.12374  0.08209  123 GLN B C   
1912 O O   . GLN B 77  ? 0.94236 0.74522 1.08501 -0.07525 0.12275  0.07492  123 GLN B O   
1913 C CB  . GLN B 77  ? 0.93991 0.78047 1.04875 -0.08133 0.10445  0.15349  123 GLN B CB  
1914 C CG  . GLN B 77  ? 1.01318 0.89676 1.07462 -0.08044 0.09421  0.16534  123 GLN B CG  
1915 C CD  . GLN B 77  ? 1.13475 1.01957 1.18661 -0.07854 0.08206  0.20944  123 GLN B CD  
1916 O OE1 . GLN B 77  ? 1.06409 0.92519 1.14851 -0.06677 0.07622  0.23011  123 GLN B OE1 
1917 N NE2 . GLN B 77  ? 1.06942 0.99002 1.07745 -0.09051 0.07861  0.22427  123 GLN B NE2 
1918 N N   . PRO B 78  ? 0.83264 0.62885 0.98587 -0.12153 0.13449  0.05962  124 PRO B N   
1919 C CA  . PRO B 78  ? 0.81514 0.57127 0.98702 -0.12616 0.14758  0.01991  124 PRO B CA  
1920 C C   . PRO B 78  ? 0.86799 0.56178 1.08145 -0.10453 0.15791  0.03369  124 PRO B C   
1921 O O   . PRO B 78  ? 0.93207 0.59437 1.17125 -0.10362 0.15576  0.07603  124 PRO B O   
1922 C CB  . PRO B 78  ? 0.83398 0.57900 1.01314 -0.16680 0.15412  0.00347  124 PRO B CB  
1923 C CG  . PRO B 78  ? 0.80473 0.61766 0.96292 -0.17788 0.14292  0.02126  124 PRO B CG  
1924 C CD  . PRO B 78  ? 0.79311 0.61839 0.94276 -0.15228 0.13561  0.06365  124 PRO B CD  
1925 N N   . THR B 79  ? 0.82460 0.50628 1.04824 -0.08700 0.16961  0.00026  125 THR B N   
1926 C CA  . THR B 79  ? 0.89845 0.52059 1.17584 -0.06228 0.18599  0.00235  125 THR B CA  
1927 C C   . THR B 79  ? 0.98322 0.56447 1.27047 -0.07129 0.21199  -0.06246 125 THR B C   
1928 O O   . THR B 79  ? 0.97400 0.57826 1.22128 -0.10305 0.21378  -0.10528 125 THR B O   
1929 C CB  . THR B 79  ? 0.86258 0.51735 1.15582 -0.02417 0.18076  0.02714  125 THR B CB  
1930 O OG1 . THR B 79  ? 0.92440 0.62061 1.19389 -0.02040 0.18883  -0.01562 125 THR B OG1 
1931 C CG2 . THR B 79  ? 0.78750 0.48510 1.05694 -0.02220 0.15412  0.08228  125 THR B CG2 
1932 N N   . LEU B 80  ? 1.04656 0.56898 1.38962 -0.04241 0.23223  -0.06912 126 LEU B N   
1933 C CA  . LEU B 80  ? 1.12368 0.60470 1.47838 -0.04258 0.26373  -0.13842 126 LEU B CA  
1934 C C   . LEU B 80  ? 1.18772 0.70089 1.57320 0.00235  0.28123  -0.14997 126 LEU B C   
1935 O O   . LEU B 80  ? 1.26485 0.85346 1.60924 -0.00228 0.28056  -0.17104 126 LEU B O   
1936 C CB  . LEU B 80  ? 1.07142 0.47254 1.45577 -0.04790 0.26782  -0.14064 126 LEU B CB  
1937 C CG  . LEU B 80  ? 1.05396 0.43442 1.39374 -0.10097 0.26875  -0.18633 126 LEU B CG  
1938 C CD1 . LEU B 80  ? 1.01864 0.43739 1.32670 -0.13694 0.24596  -0.15326 126 LEU B CD1 
1939 C CD2 . LEU B 80  ? 1.16341 0.46144 1.53009 -0.10402 0.26755  -0.18059 126 LEU B CD2 
1940 N N   . ASN B 81  ? 1.23741 0.71185 1.69318 0.04428  0.29081  -0.12702 127 ASN B N   
1941 C CA  . ASN B 81  ? 1.24574 0.75491 1.74525 0.08841  0.31328  -0.14338 127 ASN B CA  
1942 C C   . ASN B 81  ? 1.25956 0.86086 1.74976 0.10175  0.29465  -0.10033 127 ASN B C   
1943 O O   . ASN B 81  ? 1.32158 0.94397 1.86711 0.13726  0.28425  -0.04557 127 ASN B O   
1944 C CB  . ASN B 81  ? 1.33326 0.80195 1.90608 0.12850  0.31433  -0.11390 127 ASN B CB  
1945 C CG  . ASN B 81  ? 1.41206 0.83437 1.99863 0.13731  0.34602  -0.18142 127 ASN B CG  
1946 O OD1 . ASN B 81  ? 1.44175 0.85883 1.97527 0.10443  0.36352  -0.24801 127 ASN B OD1 
1947 N ND2 . ASN B 81  ? 1.47878 0.86723 2.13365 0.17973  0.35105  -0.16278 127 ASN B ND2 
1948 N N   . GLN B 82  ? 1.21718 0.88318 1.63157 0.06861  0.28293  -0.11898 128 GLN B N   
1949 C CA  . GLN B 82  ? 1.03684 0.78742 1.42475 0.07000  0.25683  -0.07723 128 GLN B CA  
1950 C C   . GLN B 82  ? 1.08497 0.89211 1.40468 0.03943  0.25899  -0.11963 128 GLN B C   
1951 O O   . GLN B 82  ? 1.20109 0.99430 1.46933 0.00424  0.25364  -0.14692 128 GLN B O   
1952 C CB  . GLN B 82  ? 1.00366 0.75171 1.36477 0.05542  0.21918  -0.01853 128 GLN B CB  
1953 C CG  . GLN B 82  ? 1.04902 0.86092 1.34307 0.03365  0.19198  -0.00436 128 GLN B CG  
1954 C CD  . GLN B 82  ? 1.00124 0.82100 1.28201 0.03215  0.16009  0.05547  128 GLN B CD  
1955 O OE1 . GLN B 82  ? 1.01735 0.80679 1.33907 0.04548  0.15638  0.09345  128 GLN B OE1 
1956 N NE2 . GLN B 82  ? 0.87822 0.73708 1.10023 0.01483  0.13673  0.06441  128 GLN B NE2 
1957 N N   . LYS B 83  ? 1.06110 0.93792 1.38332 0.04983  0.26575  -0.12154 129 LYS B N   
1958 C CA  . LYS B 83  ? 1.07611 1.01133 1.33431 0.01797  0.26677  -0.15439 129 LYS B CA  
1959 C C   . LYS B 83  ? 0.96573 0.95155 1.18687 0.00635  0.22796  -0.10177 129 LYS B C   
1960 O O   . LYS B 83  ? 0.90337 0.91928 1.15828 0.02672  0.21899  -0.06108 129 LYS B O   
1961 C CB  . LYS B 83  ? 1.20046 1.18112 1.48264 0.03057  0.30721  -0.20022 129 LYS B CB  
1962 C CG  . LYS B 83  ? 1.34300 1.25492 1.67981 0.05528  0.34997  -0.25286 129 LYS B CG  
1963 C CD  . LYS B 83  ? 1.42982 1.26968 1.72445 0.02072  0.35154  -0.29523 129 LYS B CD  
1964 C CE  . LYS B 83  ? 1.42602 1.17872 1.77684 0.04406  0.39199  -0.34589 129 LYS B CE  
1965 N NZ  . LYS B 83  ? 1.50999 1.18799 1.82297 0.00390  0.38719  -0.37777 129 LYS B NZ  
1966 N N   . GLY B 84  ? 0.90326 0.89457 1.05954 -0.02586 0.20330  -0.10078 130 GLY B N   
1967 C CA  . GLY B 84  ? 0.81450 0.82903 0.93515 -0.03509 0.16567  -0.05466 130 GLY B CA  
1968 C C   . GLY B 84  ? 0.79532 0.76506 0.90140 -0.03677 0.14258  -0.03192 130 GLY B C   
1969 O O   . GLY B 84  ? 0.76979 0.69574 0.89620 -0.03364 0.15356  -0.04391 130 GLY B O   
1970 N N   . VAL B 85  ? 0.76377 0.74584 0.83204 -0.04460 0.11128  -0.00055 131 VAL B N   
1971 C CA  . VAL B 85  ? 0.65250 0.60499 0.70303 -0.04360 0.09097  0.02055  131 VAL B CA  
1972 C C   . VAL B 85  ? 0.60405 0.56016 0.64530 -0.03733 0.06919  0.05970  131 VAL B C   
1973 O O   . VAL B 85  ? 0.64676 0.62741 0.66579 -0.04674 0.05488  0.07024  131 VAL B O   
1974 C CB  . VAL B 85  ? 0.63645 0.59569 0.64422 -0.06014 0.07498  0.00911  131 VAL B CB  
1975 C CG1 . VAL B 85  ? 0.62000 0.55840 0.61564 -0.05316 0.05968  0.02738  131 VAL B CG1 
1976 C CG2 . VAL B 85  ? 0.64316 0.60803 0.65511 -0.07529 0.09237  -0.02852 131 VAL B CG2 
1977 N N   . VAL B 86  ? 0.63360 0.56770 0.68791 -0.02769 0.06541  0.08261  132 VAL B N   
1978 C CA  . VAL B 86  ? 0.65419 0.59249 0.69029 -0.02869 0.04308  0.11728  132 VAL B CA  
1979 C C   . VAL B 86  ? 0.62879 0.54588 0.61677 -0.03500 0.02787  0.11624  132 VAL B C   
1980 O O   . VAL B 86  ? 0.60816 0.51207 0.59995 -0.03220 0.03733  0.10960  132 VAL B O   
1981 C CB  . VAL B 86  ? 0.50065 0.44110 0.58169 -0.01638 0.04717  0.14893  132 VAL B CB  
1982 C CG1 . VAL B 86  ? 0.48201 0.43127 0.53287 -0.02606 0.02190  0.18246  132 VAL B CG1 
1983 C CG2 . VAL B 86  ? 0.47206 0.44289 0.60385 -0.00414 0.05925  0.15284  132 VAL B CG2 
1984 N N   . MET B 87  ? 0.54437 0.45806 0.48937 -0.04407 0.00595  0.12135  133 MET B N   
1985 C CA  . MET B 87  ? 0.61640 0.50538 0.51775 -0.04439 -0.00592 0.11551  133 MET B CA  
1986 C C   . MET B 87  ? 0.69885 0.58313 0.57446 -0.05309 -0.01929 0.13704  133 MET B C   
1987 O O   . MET B 87  ? 0.70074 0.59885 0.57640 -0.06530 -0.03294 0.15780  133 MET B O   
1988 C CB  . MET B 87  ? 0.62263 0.49501 0.49137 -0.04793 -0.02244 0.10332  133 MET B CB  
1989 C CG  . MET B 87  ? 0.61673 0.46374 0.45917 -0.03599 -0.02628 0.08728  133 MET B CG  
1990 S SD  . MET B 87  ? 0.73774 0.54967 0.54883 -0.03518 -0.05192 0.08280  133 MET B SD  
1991 C CE  . MET B 87  ? 0.74205 0.53907 0.52624 -0.06379 -0.07451 0.10585  133 MET B CE  
1992 N N   . ILE B 88  ? 0.68502 0.56032 0.53835 -0.05068 -0.01480 0.13267  134 ILE B N   
1993 C CA  . ILE B 88  ? 0.66924 0.54137 0.47992 -0.06498 -0.02780 0.14533  134 ILE B CA  
1994 C C   . ILE B 88  ? 0.74322 0.58525 0.50463 -0.05981 -0.02782 0.11349  134 ILE B C   
1995 O O   . ILE B 88  ? 0.77827 0.62824 0.54654 -0.04589 -0.00928 0.09694  134 ILE B O   
1996 C CB  . ILE B 88  ? 0.71028 0.60896 0.53670 -0.06982 -0.01937 0.17231  134 ILE B CB  
1997 C CG1 . ILE B 88  ? 0.71229 0.63392 0.59984 -0.06638 -0.01866 0.20547  134 ILE B CG1 
1998 C CG2 . ILE B 88  ? 0.74642 0.65132 0.51707 -0.09228 -0.03576 0.18486  134 ILE B CG2 
1999 C CD1 . ILE B 88  ? 0.65142 0.56728 0.59229 -0.04983 0.00434  0.19574  134 ILE B CD1 
2000 N N   . ALA B 89  ? 0.81519 0.62315 0.53059 -0.07109 -0.04758 0.10439  135 ALA B N   
2001 C CA  . ALA B 89  ? 0.83105 0.59619 0.50227 -0.06101 -0.04717 0.06941  135 ALA B CA  
2002 C C   . ALA B 89  ? 0.85052 0.60593 0.46030 -0.08288 -0.05251 0.06239  135 ALA B C   
2003 O O   . ALA B 89  ? 0.86626 0.62753 0.45557 -0.11312 -0.07304 0.08533  135 ALA B O   
2004 C CB  . ALA B 89  ? 0.82386 0.53957 0.48572 -0.05889 -0.06691 0.06097  135 ALA B CB  
2005 N N   . SER B 90  ? 0.86412 0.61515 0.44437 -0.07046 -0.03331 0.03054  136 SER B N   
2006 C CA  . SER B 90  ? 0.96591 0.70438 0.47356 -0.09450 -0.03602 0.01247  136 SER B CA  
2007 C C   . SER B 90  ? 1.03788 0.72472 0.50894 -0.07088 -0.02165 -0.04368 136 SER B C   
2008 O O   . SER B 90  ? 1.04564 0.73683 0.55634 -0.03228 -0.00189 -0.06218 136 SER B O   
2009 C CB  . SER B 90  ? 0.95102 0.75634 0.44802 -0.11279 -0.02226 0.03363  136 SER B CB  
2010 O OG  . SER B 90  ? 1.02036 0.85036 0.51520 -0.09256 0.01008  0.00573  136 SER B OG  
2011 N N   . ASN B 91  ? 1.09913 0.73814 0.49653 -0.09486 -0.03226 -0.07139 137 ASN B N   
2012 C CA  . ASN B 91  ? 1.22202 0.79595 0.57727 -0.07332 -0.01803 -0.13240 137 ASN B CA  
2013 C C   . ASN B 91  ? 1.40558 0.98837 0.67392 -0.10703 -0.00804 -0.16366 137 ASN B C   
2014 O O   . ASN B 91  ? 1.38121 1.01075 0.61884 -0.15324 -0.02378 -0.12991 137 ASN B O   
2015 C CB  . ASN B 91  ? 1.20572 0.67965 0.55085 -0.07277 -0.04618 -0.14299 137 ASN B CB  
2016 C CG  . ASN B 91  ? 1.38335 0.78050 0.71803 -0.03121 -0.03025 -0.19995 137 ASN B CG  
2017 O OD1 . ASN B 91  ? 1.51769 0.92718 0.82347 -0.01490 0.00175  -0.24613 137 ASN B OD1 
2018 N ND2 . ASN B 91  ? 1.47066 0.78965 0.83039 -0.01312 -0.05180 -0.19605 137 ASN B ND2 
2019 N N   . TYR B 92  ? 1.51302 1.05518 0.74269 -0.08327 0.01856  -0.22871 138 TYR B N   
2020 C CA  . TYR B 92  ? 1.55253 1.10754 0.69068 -0.11458 0.03584  -0.27124 138 TYR B CA  
2021 C C   . TYR B 92  ? 1.72102 1.20406 0.82922 -0.07552 0.06617  -0.35394 138 TYR B C   
2022 O O   . TYR B 92  ? 1.69790 1.16573 0.87410 -0.01473 0.08516  -0.36981 138 TYR B O   
2023 C CB  . TYR B 92  ? 1.54481 1.22010 0.68633 -0.12674 0.06128  -0.24610 138 TYR B CB  
2024 C CG  . TYR B 92  ? 1.59264 1.32631 0.81967 -0.07624 0.09266  -0.23732 138 TYR B CG  
2025 C CD1 . TYR B 92  ? 1.55133 1.30409 0.77772 -0.03734 0.13743  -0.29472 138 TYR B CD1 
2026 C CD2 . TYR B 92  ? 1.43477 1.20587 0.74569 -0.06763 0.07851  -0.17548 138 TYR B CD2 
2027 C CE1 . TYR B 92  ? 1.46292 1.28242 0.77157 0.00342  0.16368  -0.28311 138 TYR B CE1 
2028 C CE2 . TYR B 92  ? 1.39103 1.21544 0.77545 -0.03028 0.10397  -0.16877 138 TYR B CE2 
2029 C CZ  . TYR B 92  ? 1.44074 1.29349 0.82521 0.00322  0.14454  -0.21934 138 TYR B CZ  
2030 O OH  . TYR B 92  ? 1.38527 1.30395 0.84642 0.03493  0.16741  -0.20901 138 TYR B OH  
2031 N N   . ASN B 93  ? 1.88371 1.34775 0.92266 -0.10509 0.06784  -0.39769 139 ASN B N   
2032 C CA  . ASN B 93  ? 1.96284 1.37029 1.00255 -0.06341 0.09252  -0.47327 139 ASN B CA  
2033 C C   . ASN B 93  ? 1.98919 1.48837 1.01860 -0.04074 0.14019  -0.51462 139 ASN B C   
2034 O O   . ASN B 93  ? 2.00674 1.51294 1.08702 0.02223  0.17494  -0.55268 139 ASN B O   
2035 C CB  . ASN B 93  ? 2.10522 1.43387 1.09241 -0.10230 0.06413  -0.50026 139 ASN B CB  
2036 C CG  . ASN B 93  ? 2.25234 1.47363 1.26855 -0.05533 0.07143  -0.55992 139 ASN B CG  
2037 O OD1 . ASN B 93  ? 2.22152 1.44161 1.30113 0.01071  0.10112  -0.58509 139 ASN B OD1 
2038 N ND2 . ASN B 93  ? 2.36947 1.50518 1.34833 -0.08948 0.04418  -0.57954 139 ASN B ND2 
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