data_8Z8L
# 
_entry.id   8Z8L 
# 
_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   8Z8L         pdb_00008z8l 10.2210/pdb8z8l/pdb 
WWPDB D_1300044135 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Z8L 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-22 
_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              gjsong@bio.ecnu.edu.cn 
_pdbx_contact_author.name_first         Gaojie 
_pdbx_contact_author.name_last          Song 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7787-6452 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Song, G.' 1 ? 
'Qiu, W.'  2 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'structure of IL-4Ra in complex with an nanobody 4E9' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Song, G.' 1 ? 
primary 'Qiu, W.'  2 ? 
# 
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 'Interleukin-4 receptor subunit alpha'                                                    24622.545 1 ? C182A ? 
? 
2 polymer     man 'nanobody dAb1'                                                                           13519.990 1 ? ?     ? 
? 
3 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   1 ? ?     ? 
? 
4 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose                                                  221.208   1 ? ?     ? 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IL-4 receptor subunit alpha,IL-4R subunit alpha,IL-4R-alpha,IL-4RA' 
# 
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 
;MKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWA
GQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNYLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLR
IAASTLKSGISYRARVRAWAQAYNTTWSEWSPSTKWHNSYREPFEQHHHHHHHA
;
;MKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWA
GQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNYLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLR
IAASTLKSGISYRARVRAWAQAYNTTWSEWSPSTKWHNSYREPFEQHHHHHHHA
;
B ? 
2 'polypeptide(L)' no no 
;QVQLVESGGGLVQPGGSLRLSCAASGDFYCMAWFRQAPGKEREAVAAIRSGGRSTYYADSVKGRFTISRDNSKNTLYLQM
NSLKAEDTAVYYCAVGVDGNCRNYWGQGTLVTVSSESHHHHHHA
;
;QVQLVESGGGLVQPGGSLRLSCAASGDFYCMAWFRQAPGKEREAVAAIRSGGRSTYYADSVKGRFTISRDNSKNTLYLQM
NSLKAEDTAVYYCAVGVDGNCRNYWGQGTLVTVSSESHHHHHHA
;
A ? 
# 
_pdbx_entity_nonpoly.entity_id   4 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   VAL n 
1 4   LEU n 
1 5   GLN n 
1 6   GLU n 
1 7   PRO n 
1 8   THR n 
1 9   CYS n 
1 10  VAL n 
1 11  SER n 
1 12  ASP n 
1 13  TYR n 
1 14  MET n 
1 15  SER n 
1 16  ILE n 
1 17  SER n 
1 18  THR n 
1 19  CYS n 
1 20  GLU n 
1 21  TRP n 
1 22  LYS n 
1 23  MET n 
1 24  ASN n 
1 25  GLY n 
1 26  PRO n 
1 27  THR n 
1 28  ASN n 
1 29  CYS n 
1 30  SER n 
1 31  THR n 
1 32  GLU n 
1 33  LEU n 
1 34  ARG n 
1 35  LEU n 
1 36  LEU n 
1 37  TYR n 
1 38  GLN n 
1 39  LEU n 
1 40  VAL n 
1 41  PHE n 
1 42  LEU n 
1 43  LEU n 
1 44  SER n 
1 45  GLU n 
1 46  ALA n 
1 47  HIS n 
1 48  THR n 
1 49  CYS n 
1 50  ILE n 
1 51  PRO n 
1 52  GLU n 
1 53  ASN n 
1 54  ASN n 
1 55  GLY n 
1 56  GLY n 
1 57  ALA n 
1 58  GLY n 
1 59  CYS n 
1 60  VAL n 
1 61  CYS n 
1 62  HIS n 
1 63  LEU n 
1 64  LEU n 
1 65  MET n 
1 66  ASP n 
1 67  ASP n 
1 68  VAL n 
1 69  VAL n 
1 70  SER n 
1 71  ALA n 
1 72  ASP n 
1 73  ASN n 
1 74  TYR n 
1 75  THR n 
1 76  LEU n 
1 77  ASP n 
1 78  LEU n 
1 79  TRP n 
1 80  ALA n 
1 81  GLY n 
1 82  GLN n 
1 83  GLN n 
1 84  LEU n 
1 85  LEU n 
1 86  TRP n 
1 87  LYS n 
1 88  GLY n 
1 89  SER n 
1 90  PHE n 
1 91  LYS n 
1 92  PRO n 
1 93  SER n 
1 94  GLU n 
1 95  HIS n 
1 96  VAL n 
1 97  LYS n 
1 98  PRO n 
1 99  ARG n 
1 100 ALA n 
1 101 PRO n 
1 102 GLY n 
1 103 ASN n 
1 104 LEU n 
1 105 THR n 
1 106 VAL n 
1 107 HIS n 
1 108 THR n 
1 109 ASN n 
1 110 VAL n 
1 111 SER n 
1 112 ASP n 
1 113 THR n 
1 114 LEU n 
1 115 LEU n 
1 116 LEU n 
1 117 THR n 
1 118 TRP n 
1 119 SER n 
1 120 ASN n 
1 121 PRO n 
1 122 TYR n 
1 123 PRO n 
1 124 PRO n 
1 125 ASP n 
1 126 ASN n 
1 127 TYR n 
1 128 LEU n 
1 129 TYR n 
1 130 ASN n 
1 131 HIS n 
1 132 LEU n 
1 133 THR n 
1 134 TYR n 
1 135 ALA n 
1 136 VAL n 
1 137 ASN n 
1 138 ILE n 
1 139 TRP n 
1 140 SER n 
1 141 GLU n 
1 142 ASN n 
1 143 ASP n 
1 144 PRO n 
1 145 ALA n 
1 146 ASP n 
1 147 PHE n 
1 148 ARG n 
1 149 ILE n 
1 150 TYR n 
1 151 ASN n 
1 152 VAL n 
1 153 THR n 
1 154 TYR n 
1 155 LEU n 
1 156 GLU n 
1 157 PRO n 
1 158 SER n 
1 159 LEU n 
1 160 ARG n 
1 161 ILE n 
1 162 ALA n 
1 163 ALA n 
1 164 SER n 
1 165 THR n 
1 166 LEU n 
1 167 LYS n 
1 168 SER n 
1 169 GLY n 
1 170 ILE n 
1 171 SER n 
1 172 TYR n 
1 173 ARG n 
1 174 ALA n 
1 175 ARG n 
1 176 VAL n 
1 177 ARG n 
1 178 ALA n 
1 179 TRP n 
1 180 ALA n 
1 181 GLN n 
1 182 ALA n 
1 183 TYR n 
1 184 ASN n 
1 185 THR n 
1 186 THR n 
1 187 TRP n 
1 188 SER n 
1 189 GLU n 
1 190 TRP n 
1 191 SER n 
1 192 PRO n 
1 193 SER n 
1 194 THR n 
1 195 LYS n 
1 196 TRP n 
1 197 HIS n 
1 198 ASN n 
1 199 SER n 
1 200 TYR n 
1 201 ARG n 
1 202 GLU n 
1 203 PRO n 
1 204 PHE n 
1 205 GLU n 
1 206 GLN n 
1 207 HIS n 
1 208 HIS n 
1 209 HIS n 
1 210 HIS n 
1 211 HIS n 
1 212 HIS n 
1 213 HIS n 
1 214 ALA n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  PRO n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  ALA n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  ASP n 
2 28  PHE n 
2 29  TYR n 
2 30  CYS n 
2 31  MET n 
2 32  ALA n 
2 33  TRP n 
2 34  PHE n 
2 35  ARG n 
2 36  GLN n 
2 37  ALA n 
2 38  PRO n 
2 39  GLY n 
2 40  LYS n 
2 41  GLU n 
2 42  ARG n 
2 43  GLU n 
2 44  ALA n 
2 45  VAL n 
2 46  ALA n 
2 47  ALA n 
2 48  ILE n 
2 49  ARG n 
2 50  SER n 
2 51  GLY n 
2 52  GLY n 
2 53  ARG n 
2 54  SER n 
2 55  THR n 
2 56  TYR n 
2 57  TYR n 
2 58  ALA n 
2 59  ASP n 
2 60  SER n 
2 61  VAL n 
2 62  LYS n 
2 63  GLY n 
2 64  ARG n 
2 65  PHE n 
2 66  THR n 
2 67  ILE n 
2 68  SER n 
2 69  ARG n 
2 70  ASP n 
2 71  ASN n 
2 72  SER n 
2 73  LYS n 
2 74  ASN n 
2 75  THR n 
2 76  LEU n 
2 77  TYR n 
2 78  LEU n 
2 79  GLN n 
2 80  MET n 
2 81  ASN n 
2 82  SER n 
2 83  LEU n 
2 84  LYS n 
2 85  ALA n 
2 86  GLU n 
2 87  ASP n 
2 88  THR n 
2 89  ALA n 
2 90  VAL n 
2 91  TYR n 
2 92  TYR n 
2 93  CYS n 
2 94  ALA n 
2 95  VAL n 
2 96  GLY n 
2 97  VAL n 
2 98  ASP n 
2 99  GLY n 
2 100 ASN n 
2 101 CYS n 
2 102 ARG n 
2 103 ASN n 
2 104 TYR n 
2 105 TRP n 
2 106 GLY n 
2 107 GLN n 
2 108 GLY n 
2 109 THR n 
2 110 LEU n 
2 111 VAL n 
2 112 THR n 
2 113 VAL n 
2 114 SER n 
2 115 SER n 
2 116 GLU n 
2 117 SER n 
2 118 HIS n 
2 119 HIS n 
2 120 HIS n 
2 121 HIS n 
2 122 HIS n 
2 123 HIS n 
2 124 ALA 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' 1 214 human ? 'IL4R, IL4RA, 582J2.1' ? ? ? ? ? ? 'Homo sapiens'  9606  ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 124 ?     ? ?                      ? ? ? ? ? ? 'Vicugna pacos' 30538 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_branch.entity_id   3 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 3 DGlcpNAcb1-4DGlcpNAcb1-ROH                            'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
3 3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'       LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  3 
_pdbx_entity_branch_link.entity_branch_list_num_1   2 
_pdbx_entity_branch_link.comp_id_1                  NAG 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   1 
_pdbx_entity_branch_link.comp_id_2                  NAG 
_pdbx_entity_branch_link.atom_id_2                  O4 
_pdbx_entity_branch_link.leaving_atom_id_2          HO4 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   MET 1   1   1   MET MET B . n 
A 1 2   LYS 2   2   2   LYS LYS B . n 
A 1 3   VAL 3   3   3   VAL VAL B . n 
A 1 4   LEU 4   4   4   LEU LEU B . n 
A 1 5   GLN 5   5   5   GLN GLN B . n 
A 1 6   GLU 6   6   6   GLU GLU B . n 
A 1 7   PRO 7   7   7   PRO PRO B . n 
A 1 8   THR 8   8   8   THR THR B . n 
A 1 9   CYS 9   9   9   CYS CYS B . n 
A 1 10  VAL 10  10  10  VAL VAL B . n 
A 1 11  SER 11  11  11  SER SER B . n 
A 1 12  ASP 12  12  12  ASP ASP B . n 
A 1 13  TYR 13  13  13  TYR TYR B . n 
A 1 14  MET 14  14  14  MET MET B . n 
A 1 15  SER 15  15  15  SER SER B . n 
A 1 16  ILE 16  16  16  ILE ILE B . n 
A 1 17  SER 17  17  17  SER SER B . n 
A 1 18  THR 18  18  18  THR THR B . n 
A 1 19  CYS 19  19  19  CYS CYS B . n 
A 1 20  GLU 20  20  20  GLU GLU B . n 
A 1 21  TRP 21  21  21  TRP TRP B . n 
A 1 22  LYS 22  22  22  LYS LYS B . n 
A 1 23  MET 23  23  23  MET MET B . n 
A 1 24  ASN 24  24  24  ASN ASN B . n 
A 1 25  GLY 25  25  25  GLY GLY B . n 
A 1 26  PRO 26  26  26  PRO PRO B . n 
A 1 27  THR 27  27  27  THR THR B . n 
A 1 28  ASN 28  28  28  ASN ASN B . n 
A 1 29  CYS 29  29  29  CYS CYS B . n 
A 1 30  SER 30  30  30  SER SER B . n 
A 1 31  THR 31  31  31  THR THR B . n 
A 1 32  GLU 32  32  32  GLU GLU B . n 
A 1 33  LEU 33  33  33  LEU LEU B . n 
A 1 34  ARG 34  34  34  ARG ARG B . n 
A 1 35  LEU 35  35  35  LEU LEU B . n 
A 1 36  LEU 36  36  36  LEU LEU B . n 
A 1 37  TYR 37  37  37  TYR TYR B . n 
A 1 38  GLN 38  38  38  GLN GLN B . n 
A 1 39  LEU 39  39  39  LEU LEU B . n 
A 1 40  VAL 40  40  40  VAL VAL B . n 
A 1 41  PHE 41  41  41  PHE PHE B . n 
A 1 42  LEU 42  42  42  LEU LEU B . n 
A 1 43  LEU 43  43  43  LEU LEU B . n 
A 1 44  SER 44  44  44  SER SER B . n 
A 1 45  GLU 45  45  45  GLU GLU B . n 
A 1 46  ALA 46  46  46  ALA ALA B . n 
A 1 47  HIS 47  47  47  HIS HIS B . n 
A 1 48  THR 48  48  48  THR THR B . n 
A 1 49  CYS 49  49  49  CYS CYS B . n 
A 1 50  ILE 50  50  50  ILE ILE B . n 
A 1 51  PRO 51  51  51  PRO PRO B . n 
A 1 52  GLU 52  52  52  GLU GLU B . n 
A 1 53  ASN 53  53  53  ASN ASN B . n 
A 1 54  ASN 54  54  54  ASN ASN B . n 
A 1 55  GLY 55  55  55  GLY GLY B . n 
A 1 56  GLY 56  56  56  GLY GLY B . n 
A 1 57  ALA 57  57  57  ALA ALA B . n 
A 1 58  GLY 58  58  58  GLY GLY B . n 
A 1 59  CYS 59  59  59  CYS CYS B . n 
A 1 60  VAL 60  60  60  VAL VAL B . n 
A 1 61  CYS 61  61  61  CYS CYS B . n 
A 1 62  HIS 62  62  62  HIS HIS B . n 
A 1 63  LEU 63  63  63  LEU LEU B . n 
A 1 64  LEU 64  64  64  LEU LEU B . n 
A 1 65  MET 65  65  65  MET MET B . n 
A 1 66  ASP 66  66  66  ASP ASP B . n 
A 1 67  ASP 67  67  67  ASP ASP B . n 
A 1 68  VAL 68  68  68  VAL VAL B . n 
A 1 69  VAL 69  69  69  VAL VAL B . n 
A 1 70  SER 70  70  70  SER SER B . n 
A 1 71  ALA 71  71  71  ALA ALA B . n 
A 1 72  ASP 72  72  72  ASP ASP B . n 
A 1 73  ASN 73  73  73  ASN ASN B . n 
A 1 74  TYR 74  74  74  TYR TYR B . n 
A 1 75  THR 75  75  75  THR THR B . n 
A 1 76  LEU 76  76  76  LEU LEU B . n 
A 1 77  ASP 77  77  77  ASP ASP B . n 
A 1 78  LEU 78  78  78  LEU LEU B . n 
A 1 79  TRP 79  79  79  TRP TRP B . n 
A 1 80  ALA 80  80  80  ALA ALA B . n 
A 1 81  GLY 81  81  81  GLY GLY B . n 
A 1 82  GLN 82  82  82  GLN GLN B . n 
A 1 83  GLN 83  83  83  GLN GLN B . n 
A 1 84  LEU 84  84  84  LEU LEU B . n 
A 1 85  LEU 85  85  85  LEU LEU B . n 
A 1 86  TRP 86  86  86  TRP TRP B . n 
A 1 87  LYS 87  87  87  LYS LYS B . n 
A 1 88  GLY 88  88  88  GLY GLY B . n 
A 1 89  SER 89  89  89  SER SER B . n 
A 1 90  PHE 90  90  90  PHE PHE B . n 
A 1 91  LYS 91  91  91  LYS LYS B . n 
A 1 92  PRO 92  92  92  PRO PRO B . n 
A 1 93  SER 93  93  93  SER SER B . n 
A 1 94  GLU 94  94  94  GLU GLU B . n 
A 1 95  HIS 95  95  95  HIS HIS B . n 
A 1 96  VAL 96  96  96  VAL VAL B . n 
A 1 97  LYS 97  97  97  LYS LYS B . n 
A 1 98  PRO 98  98  98  PRO PRO B . n 
A 1 99  ARG 99  99  99  ARG ARG B . n 
A 1 100 ALA 100 100 100 ALA ALA B . n 
A 1 101 PRO 101 101 101 PRO PRO B . n 
A 1 102 GLY 102 102 102 GLY GLY B . n 
A 1 103 ASN 103 103 103 ASN ASN B . n 
A 1 104 LEU 104 104 104 LEU LEU B . n 
A 1 105 THR 105 105 105 THR THR B . n 
A 1 106 VAL 106 106 106 VAL VAL B . n 
A 1 107 HIS 107 107 107 HIS HIS B . n 
A 1 108 THR 108 108 ?   ?   ?   B . n 
A 1 109 ASN 109 109 ?   ?   ?   B . n 
A 1 110 VAL 110 110 ?   ?   ?   B . n 
A 1 111 SER 111 111 ?   ?   ?   B . n 
A 1 112 ASP 112 112 112 ASP ASP B . n 
A 1 113 THR 113 113 113 THR THR B . n 
A 1 114 LEU 114 114 114 LEU LEU B . n 
A 1 115 LEU 115 115 115 LEU LEU B . n 
A 1 116 LEU 116 116 116 LEU LEU B . n 
A 1 117 THR 117 117 117 THR THR B . n 
A 1 118 TRP 118 118 118 TRP TRP B . n 
A 1 119 SER 119 119 119 SER SER B . n 
A 1 120 ASN 120 120 120 ASN ASN B . n 
A 1 121 PRO 121 121 121 PRO PRO B . n 
A 1 122 TYR 122 122 122 TYR TYR B . n 
A 1 123 PRO 123 123 123 PRO PRO B . n 
A 1 124 PRO 124 124 124 PRO PRO B . n 
A 1 125 ASP 125 125 125 ASP ASP B . n 
A 1 126 ASN 126 126 126 ASN ASN B . n 
A 1 127 TYR 127 127 127 TYR TYR B . n 
A 1 128 LEU 128 128 128 LEU LEU B . n 
A 1 129 TYR 129 129 129 TYR TYR B . n 
A 1 130 ASN 130 130 130 ASN ASN B . n 
A 1 131 HIS 131 131 131 HIS HIS B . n 
A 1 132 LEU 132 132 132 LEU LEU B . n 
A 1 133 THR 133 133 133 THR THR B . n 
A 1 134 TYR 134 134 134 TYR TYR B . n 
A 1 135 ALA 135 135 135 ALA ALA B . n 
A 1 136 VAL 136 136 136 VAL VAL B . n 
A 1 137 ASN 137 137 137 ASN ASN B . n 
A 1 138 ILE 138 138 138 ILE ILE B . n 
A 1 139 TRP 139 139 139 TRP TRP B . n 
A 1 140 SER 140 140 140 SER SER B . n 
A 1 141 GLU 141 141 141 GLU GLU B . n 
A 1 142 ASN 142 142 142 ASN ASN B . n 
A 1 143 ASP 143 143 143 ASP ASP B . n 
A 1 144 PRO 144 144 144 PRO PRO B . n 
A 1 145 ALA 145 145 145 ALA ALA B . n 
A 1 146 ASP 146 146 146 ASP ASP B . n 
A 1 147 PHE 147 147 147 PHE PHE B . n 
A 1 148 ARG 148 148 148 ARG ARG B . n 
A 1 149 ILE 149 149 149 ILE ILE B . n 
A 1 150 TYR 150 150 150 TYR TYR B . n 
A 1 151 ASN 151 151 151 ASN ASN B . n 
A 1 152 VAL 152 152 152 VAL VAL B . n 
A 1 153 THR 153 153 153 THR THR B . n 
A 1 154 TYR 154 154 154 TYR TYR B . n 
A 1 155 LEU 155 155 155 LEU LEU B . n 
A 1 156 GLU 156 156 156 GLU GLU B . n 
A 1 157 PRO 157 157 157 PRO PRO B . n 
A 1 158 SER 158 158 158 SER SER B . n 
A 1 159 LEU 159 159 159 LEU LEU B . n 
A 1 160 ARG 160 160 160 ARG ARG B . n 
A 1 161 ILE 161 161 161 ILE ILE B . n 
A 1 162 ALA 162 162 162 ALA ALA B . n 
A 1 163 ALA 163 163 163 ALA ALA B . n 
A 1 164 SER 164 164 ?   ?   ?   B . n 
A 1 165 THR 165 165 ?   ?   ?   B . n 
A 1 166 LEU 166 166 ?   ?   ?   B . n 
A 1 167 LYS 167 167 ?   ?   ?   B . n 
A 1 168 SER 168 168 ?   ?   ?   B . n 
A 1 169 GLY 169 169 169 GLY GLY B . n 
A 1 170 ILE 170 170 170 ILE ILE B . n 
A 1 171 SER 171 171 171 SER SER B . n 
A 1 172 TYR 172 172 172 TYR TYR B . n 
A 1 173 ARG 173 173 173 ARG ARG B . n 
A 1 174 ALA 174 174 174 ALA ALA B . n 
A 1 175 ARG 175 175 175 ARG ARG B . n 
A 1 176 VAL 176 176 176 VAL VAL B . n 
A 1 177 ARG 177 177 177 ARG ARG B . n 
A 1 178 ALA 178 178 178 ALA ALA B . n 
A 1 179 TRP 179 179 179 TRP TRP B . n 
A 1 180 ALA 180 180 180 ALA ALA B . n 
A 1 181 GLN 181 181 181 GLN GLN B . n 
A 1 182 ALA 182 182 182 ALA ALA B . n 
A 1 183 TYR 183 183 183 TYR TYR B . n 
A 1 184 ASN 184 184 184 ASN ASN B . n 
A 1 185 THR 185 185 185 THR THR B . n 
A 1 186 THR 186 186 186 THR THR B . n 
A 1 187 TRP 187 187 187 TRP TRP B . n 
A 1 188 SER 188 188 188 SER SER B . n 
A 1 189 GLU 189 189 189 GLU GLU B . n 
A 1 190 TRP 190 190 190 TRP TRP B . n 
A 1 191 SER 191 191 191 SER SER B . n 
A 1 192 PRO 192 192 192 PRO PRO B . n 
A 1 193 SER 193 193 193 SER SER B . n 
A 1 194 THR 194 194 194 THR THR B . n 
A 1 195 LYS 195 195 195 LYS LYS B . n 
A 1 196 TRP 196 196 196 TRP TRP B . n 
A 1 197 HIS 197 197 197 HIS HIS B . n 
A 1 198 ASN 198 198 ?   ?   ?   B . n 
A 1 199 SER 199 199 ?   ?   ?   B . n 
A 1 200 TYR 200 200 ?   ?   ?   B . n 
A 1 201 ARG 201 201 ?   ?   ?   B . n 
A 1 202 GLU 202 202 ?   ?   ?   B . n 
A 1 203 PRO 203 203 ?   ?   ?   B . n 
A 1 204 PHE 204 204 ?   ?   ?   B . n 
A 1 205 GLU 205 205 ?   ?   ?   B . n 
A 1 206 GLN 206 206 ?   ?   ?   B . n 
A 1 207 HIS 207 207 ?   ?   ?   B . n 
A 1 208 HIS 208 208 ?   ?   ?   B . n 
A 1 209 HIS 209 209 ?   ?   ?   B . n 
A 1 210 HIS 210 210 ?   ?   ?   B . n 
A 1 211 HIS 211 211 ?   ?   ?   B . n 
A 1 212 HIS 212 212 ?   ?   ?   B . n 
A 1 213 HIS 213 213 ?   ?   ?   B . n 
A 1 214 ALA 214 214 ?   ?   ?   B . n 
B 2 1   GLN 1   1   1   GLN GLN A . n 
B 2 2   VAL 2   2   2   VAL VAL A . n 
B 2 3   GLN 3   3   3   GLN GLN A . n 
B 2 4   LEU 4   4   4   LEU LEU A . n 
B 2 5   VAL 5   5   5   VAL VAL A . n 
B 2 6   GLU 6   6   6   GLU GLU A . n 
B 2 7   SER 7   7   7   SER SER A . n 
B 2 8   GLY 8   8   8   GLY GLY A . n 
B 2 9   GLY 9   9   9   GLY GLY A . n 
B 2 10  GLY 10  10  10  GLY GLY A . n 
B 2 11  LEU 11  11  11  LEU LEU A . n 
B 2 12  VAL 12  12  12  VAL VAL A . n 
B 2 13  GLN 13  13  13  GLN GLN A . n 
B 2 14  PRO 14  14  14  PRO PRO A . n 
B 2 15  GLY 15  15  15  GLY GLY A . n 
B 2 16  GLY 16  16  16  GLY GLY A . n 
B 2 17  SER 17  17  17  SER SER A . n 
B 2 18  LEU 18  18  18  LEU LEU A . n 
B 2 19  ARG 19  19  19  ARG ARG A . n 
B 2 20  LEU 20  20  20  LEU LEU A . n 
B 2 21  SER 21  21  21  SER SER A . n 
B 2 22  CYS 22  22  22  CYS CYS A . n 
B 2 23  ALA 23  23  23  ALA ALA A . n 
B 2 24  ALA 24  24  24  ALA ALA A . n 
B 2 25  SER 25  25  25  SER SER A . n 
B 2 26  GLY 26  26  26  GLY GLY A . n 
B 2 27  ASP 27  27  27  ASP ASP A . n 
B 2 28  PHE 28  28  28  PHE PHE A . n 
B 2 29  TYR 29  29  29  TYR TYR A . n 
B 2 30  CYS 30  30  30  CYS CYS A . n 
B 2 31  MET 31  31  31  MET MET A . n 
B 2 32  ALA 32  32  32  ALA ALA A . n 
B 2 33  TRP 33  33  33  TRP TRP A . n 
B 2 34  PHE 34  34  34  PHE PHE A . n 
B 2 35  ARG 35  35  35  ARG ARG A . n 
B 2 36  GLN 36  36  36  GLN GLN A . n 
B 2 37  ALA 37  37  37  ALA ALA A . n 
B 2 38  PRO 38  38  38  PRO PRO A . n 
B 2 39  GLY 39  39  39  GLY GLY A . n 
B 2 40  LYS 40  40  40  LYS LYS A . n 
B 2 41  GLU 41  41  41  GLU GLU A . n 
B 2 42  ARG 42  42  42  ARG ARG A . n 
B 2 43  GLU 43  43  43  GLU GLU A . n 
B 2 44  ALA 44  44  44  ALA ALA A . n 
B 2 45  VAL 45  45  45  VAL VAL A . n 
B 2 46  ALA 46  46  46  ALA ALA A . n 
B 2 47  ALA 47  47  47  ALA ALA A . n 
B 2 48  ILE 48  48  48  ILE ILE A . n 
B 2 49  ARG 49  49  49  ARG ARG A . n 
B 2 50  SER 50  50  50  SER SER A . n 
B 2 51  GLY 51  51  51  GLY GLY A . n 
B 2 52  GLY 52  52  52  GLY GLY A . n 
B 2 53  ARG 53  53  53  ARG ARG A . n 
B 2 54  SER 54  54  54  SER SER A . n 
B 2 55  THR 55  55  55  THR THR A . n 
B 2 56  TYR 56  56  56  TYR TYR A . n 
B 2 57  TYR 57  57  57  TYR TYR A . n 
B 2 58  ALA 58  58  58  ALA ALA A . n 
B 2 59  ASP 59  59  59  ASP ASP A . n 
B 2 60  SER 60  60  60  SER SER A . n 
B 2 61  VAL 61  61  61  VAL VAL A . n 
B 2 62  LYS 62  62  62  LYS LYS A . n 
B 2 63  GLY 63  63  63  GLY GLY A . n 
B 2 64  ARG 64  64  64  ARG ARG A . n 
B 2 65  PHE 65  65  65  PHE PHE A . n 
B 2 66  THR 66  66  66  THR THR A . n 
B 2 67  ILE 67  67  67  ILE ILE A . n 
B 2 68  SER 68  68  68  SER SER A . n 
B 2 69  ARG 69  69  69  ARG ARG A . n 
B 2 70  ASP 70  70  70  ASP ASP A . n 
B 2 71  ASN 71  71  71  ASN ASN A . n 
B 2 72  SER 72  72  72  SER SER A . n 
B 2 73  LYS 73  73  73  LYS LYS A . n 
B 2 74  ASN 74  74  74  ASN ASN A . n 
B 2 75  THR 75  75  75  THR THR A . n 
B 2 76  LEU 76  76  76  LEU LEU A . n 
B 2 77  TYR 77  77  77  TYR TYR A . n 
B 2 78  LEU 78  78  78  LEU LEU A . n 
B 2 79  GLN 79  79  79  GLN GLN A . n 
B 2 80  MET 80  80  80  MET MET A . n 
B 2 81  ASN 81  81  81  ASN ASN A . n 
B 2 82  SER 82  82  82  SER SER A . n 
B 2 83  LEU 83  83  83  LEU LEU A . n 
B 2 84  LYS 84  84  84  LYS LYS A . n 
B 2 85  ALA 85  85  85  ALA ALA A . n 
B 2 86  GLU 86  86  86  GLU GLU A . n 
B 2 87  ASP 87  87  87  ASP ASP A . n 
B 2 88  THR 88  88  88  THR THR A . n 
B 2 89  ALA 89  89  89  ALA ALA A . n 
B 2 90  VAL 90  90  90  VAL VAL A . n 
B 2 91  TYR 91  91  91  TYR TYR A . n 
B 2 92  TYR 92  92  92  TYR TYR A . n 
B 2 93  CYS 93  93  93  CYS CYS A . n 
B 2 94  ALA 94  94  94  ALA ALA A . n 
B 2 95  VAL 95  95  95  VAL VAL A . n 
B 2 96  GLY 96  96  96  GLY GLY A . n 
B 2 97  VAL 97  97  97  VAL VAL A . n 
B 2 98  ASP 98  98  98  ASP ASP A . n 
B 2 99  GLY 99  99  99  GLY GLY A . n 
B 2 100 ASN 100 100 100 ASN ASN A . n 
B 2 101 CYS 101 101 101 CYS CYS A . n 
B 2 102 ARG 102 102 102 ARG ARG A . n 
B 2 103 ASN 103 103 103 ASN ASN A . n 
B 2 104 TYR 104 104 104 TYR TYR A . n 
B 2 105 TRP 105 105 105 TRP TRP A . n 
B 2 106 GLY 106 106 106 GLY GLY A . n 
B 2 107 GLN 107 107 107 GLN GLN A . n 
B 2 108 GLY 108 108 108 GLY GLY A . n 
B 2 109 THR 109 109 109 THR THR A . n 
B 2 110 LEU 110 110 110 LEU LEU A . n 
B 2 111 VAL 111 111 111 VAL VAL A . n 
B 2 112 THR 112 112 112 THR THR A . n 
B 2 113 VAL 113 113 113 VAL VAL A . n 
B 2 114 SER 114 114 114 SER SER A . n 
B 2 115 SER 115 115 115 SER SER A . n 
B 2 116 GLU 116 116 ?   ?   ?   A . n 
B 2 117 SER 117 117 ?   ?   ?   A . n 
B 2 118 HIS 118 118 ?   ?   ?   A . n 
B 2 119 HIS 119 119 ?   ?   ?   A . n 
B 2 120 HIS 120 120 ?   ?   ?   A . n 
B 2 121 HIS 121 121 ?   ?   ?   A . n 
B 2 122 HIS 122 122 ?   ?   ?   A . n 
B 2 123 HIS 123 123 ?   ?   ?   A . n 
B 2 124 ALA 124 124 ?   ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 3 NAG 1 C NAG 1 B NAG 202 n 
C 3 NAG 2 C NAG 2 B NAG 203 n 
# 
_pdbx_nonpoly_scheme.asym_id         D 
_pdbx_nonpoly_scheme.entity_id       4 
_pdbx_nonpoly_scheme.mon_id          NAG 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     301 
_pdbx_nonpoly_scheme.auth_seq_num    201 
_pdbx_nonpoly_scheme.pdb_mon_id      NAG 
_pdbx_nonpoly_scheme.auth_mon_id     NAG 
_pdbx_nonpoly_scheme.pdb_strand_id   B 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 B LYS 2   ? CG  ? A LYS 2   CG  
2  1 Y 1 B LYS 2   ? CD  ? A LYS 2   CD  
3  1 Y 1 B LYS 2   ? CE  ? A LYS 2   CE  
4  1 Y 1 B LYS 2   ? NZ  ? A LYS 2   NZ  
5  1 Y 1 B LYS 22  ? CG  ? A LYS 22  CG  
6  1 Y 1 B LYS 22  ? CD  ? A LYS 22  CD  
7  1 Y 1 B LYS 22  ? CE  ? A LYS 22  CE  
8  1 Y 1 B LYS 22  ? NZ  ? A LYS 22  NZ  
9  1 Y 1 A ARG 19  ? CG  ? B ARG 19  CG  
10 1 Y 1 A ARG 19  ? CD  ? B ARG 19  CD  
11 1 Y 1 A ARG 19  ? NE  ? B ARG 19  NE  
12 1 Y 1 A ARG 19  ? CZ  ? B ARG 19  CZ  
13 1 Y 1 A ARG 19  ? NH1 ? B ARG 19  NH1 
14 1 Y 1 A ARG 19  ? NH2 ? B ARG 19  NH2 
15 1 Y 1 A LYS 40  ? CG  ? B LYS 40  CG  
16 1 Y 1 A LYS 40  ? CD  ? B LYS 40  CD  
17 1 Y 1 A LYS 40  ? CE  ? B LYS 40  CE  
18 1 Y 1 A LYS 40  ? NZ  ? B LYS 40  NZ  
19 1 Y 1 A ARG 42  ? CG  ? B ARG 42  CG  
20 1 Y 1 A ARG 42  ? CD  ? B ARG 42  CD  
21 1 Y 1 A ARG 42  ? NE  ? B ARG 42  NE  
22 1 Y 1 A ARG 42  ? CZ  ? B ARG 42  CZ  
23 1 Y 1 A ARG 42  ? NH1 ? B ARG 42  NH1 
24 1 Y 1 A ARG 42  ? NH2 ? B ARG 42  NH2 
25 1 Y 1 A ARG 69  ? CG  ? B ARG 69  CG  
26 1 Y 1 A ARG 69  ? CD  ? B ARG 69  CD  
27 1 Y 1 A ARG 69  ? NE  ? B ARG 69  NE  
28 1 Y 1 A ARG 69  ? CZ  ? B ARG 69  CZ  
29 1 Y 1 A ARG 69  ? NH1 ? B ARG 69  NH1 
30 1 Y 1 A ARG 69  ? NH2 ? B ARG 69  NH2 
31 1 Y 1 A LYS 73  ? CG  ? B LYS 73  CG  
32 1 Y 1 A LYS 73  ? CD  ? B LYS 73  CD  
33 1 Y 1 A LYS 73  ? CE  ? B LYS 73  CE  
34 1 Y 1 A LYS 73  ? NZ  ? B LYS 73  NZ  
35 1 Y 1 A LYS 84  ? CG  ? B LYS 84  CG  
36 1 Y 1 A LYS 84  ? CD  ? B LYS 84  CD  
37 1 Y 1 A LYS 84  ? CE  ? B LYS 84  CE  
38 1 Y 1 A LYS 84  ? NZ  ? B LYS 84  NZ  
39 1 Y 1 A ARG 102 ? CG  ? B ARG 102 CG  
40 1 Y 1 A ARG 102 ? CD  ? B ARG 102 CD  
41 1 Y 1 A ARG 102 ? NE  ? B ARG 102 NE  
42 1 Y 1 A ARG 102 ? CZ  ? B ARG 102 CZ  
43 1 Y 1 A ARG 102 ? NH1 ? B ARG 102 NH1 
44 1 Y 1 A ARG 102 ? NH2 ? B ARG 102 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z8L 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     142.936 
_cell.length_a_esd                 ? 
_cell.length_b                     142.936 
_cell.length_b_esd                 ? 
_cell.length_c                     149.087 
_cell.length_c_esd                 ? 
_cell.volume                       2637871.625 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_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                         8Z8L 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
_symmetry.space_group_name_Hall            
;R 3 2"
;
_symmetry.space_group_name_H-M             'H 3 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                   8Z8L 
_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             3.84 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          67.99 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.0 
_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    '1.4 M Sodium malonate dibasic monohydrate pH 6.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     99 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-01-08 
_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   0.9791 
_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                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9791 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          191.38 
_reflns.entry_id                                       8Z8L 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.96 
_reflns.d_resolution_low                               95.2 
_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                                     4534 
_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                           92.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.2 
_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                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    3.96 
_reflns_shell.d_res_low                                     4.21 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             227 
_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                               ? 
_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                                  0.38 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               208.29 
_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                                 8Z8L 
_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                            3.96 
_refine.ls_d_res_low                             19.82 
_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                     4488 
_refine.ls_number_reflns_R_free                  225 
_refine.ls_number_reflns_R_work                  4263 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.16 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.3028 
_refine.ls_R_factor_R_free                       0.3337 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.3011 
_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                          1.35 
_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                 36.9962 
_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                            0.6218 
_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                       3.96 
_refine_hist.d_res_low                        19.82 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2381 
_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        2339 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_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' ? 0.0032 ? 2443 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6724 ? 3341 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0573 ? 374  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0058 ? 425  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 5.4316 ? 347  ? 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' 3.96 4.98  . . 93  1761 72.06 . . . . 0.3833 . . . . . . . . . . . 0.3514 
'X-RAY DIFFRACTION' 4.98 19.82 . . 132 2502 99.92 . . . . 0.2809 . . . . . . . . . . . 0.3297 
# 
_struct.entry_id                     8Z8L 
_struct.title                        'structure of IL-4Ra in complex with an nanobody 4E9' 
_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        8Z8L 
_struct_keywords.text            'inflammation, cytokine, antibody, immune disorder' 
_struct_keywords.pdbx_keywords   CYTOKINE 
# 
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 4 ? 
# 
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 IL4RA_HUMAN P24394 ? 1 
;MKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWA
GQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNYLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLR
IAASTLKSGISYRARVRAWAQCYNTTWSEWSPSTKWHNSYREPFEQH
;
26 
2 PDB 8Z8L        8Z8L   ? 2 ? 1  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8Z8L B 1 ? 207 ? P24394 26 ? 232 ? 1 207 
2 2 8Z8L A 1 ? 124 ? 8Z8L   1  ? 124 ? 1 124 
# 
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 8Z8L ALA B 182 ? UNP P24394 CYS 207 'engineered mutation' 182 1 
1 8Z8L HIS B 208 ? UNP P24394 ?   ?   'expression tag'      208 2 
1 8Z8L HIS B 209 ? UNP P24394 ?   ?   'expression tag'      209 3 
1 8Z8L HIS B 210 ? UNP P24394 ?   ?   'expression tag'      210 4 
1 8Z8L HIS B 211 ? UNP P24394 ?   ?   'expression tag'      211 5 
1 8Z8L HIS B 212 ? UNP P24394 ?   ?   'expression tag'      212 6 
1 8Z8L HIS B 213 ? UNP P24394 ?   ?   'expression tag'      213 7 
1 8Z8L ALA B 214 ? UNP P24394 ?   ?   'expression tag'      214 8 
# 
_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)' 1760  ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  15930 ? 
# 
_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 TYR A 127 ? LEU A 132 ? TYR B 127 LEU B 132 1 ? 6 
HELX_P HELX_P2 AA2 LYS B 84  ? THR B 88  ? LYS A 84  THR A 88  5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 9   SG  ? ? ? 1_555 A CYS 19  SG ? ? B CYS 9   B CYS 19  1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf2 disulf ?    ? A CYS 29  SG  ? ? ? 1_555 A CYS 59  SG ? ? B CYS 29  B CYS 59  1_555 ? ? ? ? ? ? ? 2.027 ? ?               
disulf3 disulf ?    ? A CYS 49  SG  ? ? ? 1_555 A CYS 61  SG ? ? B CYS 49  B CYS 61  1_555 ? ? ? ? ? ? ? 2.027 ? ?               
disulf4 disulf ?    ? B CYS 22  SG  ? ? ? 1_555 B CYS 93  SG ? ? A CYS 22  A CYS 93  1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf5 disulf ?    ? B CYS 30  SG  ? ? ? 1_555 B CYS 101 SG ? ? A CYS 30  A CYS 101 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
covale1 covale one  ? A ASN 73  ND2 ? ? ? 1_555 D NAG .   C1 ? ? B ASN 73  B NAG 301 1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
covale2 covale one  ? A ASN 151 ND2 ? ? ? 1_555 C NAG .   C1 ? ? B ASN 151 C NAG 1   1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale3 covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.441 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG C .  ? ASN A 151 ? NAG C 1   ? 1_555 ASN B 151 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG D .  ? ASN A 73  ? NAG B 301 ? 1_555 ASN B 73  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 CYS A 9  ? CYS A 19  ? CYS B 9   ? 1_555 CYS B 19  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4 CYS A 29 ? CYS A 59  ? CYS B 29  ? 1_555 CYS B 59  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5 CYS A 49 ? CYS A 61  ? CYS B 49  ? 1_555 CYS B 61  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6 CYS B 22 ? CYS B 93  ? CYS A 22  ? 1_555 CYS A 93  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7 CYS B 30 ? CYS B 101 ? CYS A 30  ? 1_555 CYS A 101 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 6 ? 
# 
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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 3   ? SER A 11  ? VAL B 3   SER B 11  
AA1 2 ILE A 16  ? MET A 23  ? ILE B 16  MET B 23  
AA1 3 GLY A 58  ? LEU A 64  ? GLY B 58  LEU B 64  
AA1 4 GLU A 52  ? ASN A 53  ? GLU B 52  ASN B 53  
AA2 1 HIS A 47  ? CYS A 49  ? HIS B 47  CYS B 49  
AA2 2 LEU A 33  ? GLN A 38  ? LEU B 33  GLN B 38  
AA2 3 TYR A 74  ? ALA A 80  ? TYR B 74  ALA B 80  
AA2 4 GLN A 83  ? PHE A 90  ? GLN B 83  PHE B 90  
AA3 1 GLY A 102 ? HIS A 107 ? GLY B 102 HIS B 107 
AA3 2 LEU A 114 ? SER A 119 ? LEU B 114 SER B 119 
AA3 3 SER A 158 ? ILE A 161 ? SER B 158 ILE B 161 
AA4 1 PHE A 147 ? ASN A 151 ? PHE B 147 ASN B 151 
AA4 2 ALA A 135 ? TRP A 139 ? ALA B 135 TRP B 139 
AA4 3 ARG A 173 ? ARG A 177 ? ARG B 173 ARG B 177 
AA4 4 THR A 194 ? LYS A 195 ? THR B 194 LYS B 195 
AA5 1 LEU B 4   ? SER B 7   ? LEU A 4   SER A 7   
AA5 2 SER B 17  ? ALA B 24  ? SER A 17  ALA A 24  
AA5 3 THR B 75  ? ASN B 81  ? THR A 75  ASN A 81  
AA5 4 THR B 66  ? ARG B 69  ? THR A 66  ARG A 69  
AA6 1 GLY B 10  ? VAL B 12  ? GLY A 10  VAL A 12  
AA6 2 THR B 109 ? VAL B 113 ? THR A 109 VAL A 113 
AA6 3 ALA B 89  ? GLY B 96  ? ALA A 89  GLY A 96  
AA6 4 CYS B 30  ? ALA B 37  ? CYS A 30  ALA A 37  
AA6 5 LYS B 40  ? ILE B 48  ? LYS A 40  ILE A 48  
AA6 6 THR B 55  ? TYR B 57  ? THR A 55  TYR A 57  
# 
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 5   ? N GLN B 5   O LYS A 22  ? O LYS B 22  
AA1 2 3 N CYS A 19  ? N CYS B 19  O CYS A 61  ? O CYS B 61  
AA1 3 4 O VAL A 60  ? O VAL B 60  N GLU A 52  ? N GLU B 52  
AA2 1 2 O HIS A 47  ? O HIS B 47  N TYR A 37  ? N TYR B 37  
AA2 2 3 N ARG A 34  ? N ARG B 34  O TRP A 79  ? O TRP B 79  
AA2 3 4 N ALA A 80  ? N ALA B 80  O GLN A 83  ? O GLN B 83  
AA3 1 2 N GLY A 102 ? N GLY B 102 O SER A 119 ? O SER B 119 
AA3 2 3 N LEU A 114 ? N LEU B 114 O ILE A 161 ? O ILE B 161 
AA4 1 2 O ARG A 148 ? O ARG B 148 N ILE A 138 ? N ILE B 138 
AA4 2 3 N TRP A 139 ? N TRP B 139 O ARG A 173 ? O ARG B 173 
AA4 3 4 N ALA A 174 ? N ALA B 174 O THR A 194 ? O THR B 194 
AA5 1 2 N SER B 7   ? N SER A 7   O SER B 21  ? O SER A 21  
AA5 2 3 N LEU B 18  ? N LEU A 18  O MET B 80  ? O MET A 80  
AA5 3 4 O TYR B 77  ? O TYR A 77  N SER B 68  ? N SER A 68  
AA6 1 2 N GLY B 10  ? N GLY A 10  O LEU B 110 ? O LEU A 110 
AA6 2 3 O VAL B 111 ? O VAL A 111 N ALA B 89  ? N ALA A 89  
AA6 3 4 O GLY B 96  ? O GLY A 96  N CYS B 30  ? N CYS A 30  
AA6 4 5 N ARG B 35  ? N ARG A 35  O GLU B 43  ? O GLU A 43  
AA6 5 6 N ALA B 47  ? N ALA A 47  O TYR B 56  ? O TYR A 56  
# 
_pdbx_entry_details.entry_id                   8Z8L 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 MET B 14  ? ? -134.56 -42.11  
2  1 SER B 15  ? ? -148.17 -31.90  
3  1 GLU B 32  ? ? -139.63 -50.98  
4  1 VAL B 40  ? ? -115.03 76.85   
5  1 PHE B 41  ? ? -127.81 -161.24 
6  1 LEU B 43  ? ? -105.57 49.90   
7  1 PRO B 98  ? ? -65.76  -178.68 
8  1 PRO B 121 ? ? -69.25  5.60    
9  1 THR B 153 ? ? -159.69 0.39    
10 1 ALA B 162 ? ? -146.54 48.00   
11 1 LEU A 18  ? ? -165.93 119.61  
12 1 SER A 50  ? ? -66.34  -74.17  
13 1 SER A 54  ? ? -168.02 108.65  
14 1 ARG A 64  ? ? -94.75  -65.74  
15 1 SER A 72  ? ? 55.88   -109.39 
16 1 CYS A 101 ? ? -68.10  68.83   
17 1 TRP A 105 ? ? -141.50 -51.19  
18 1 GLN A 107 ? ? 64.01   -141.24 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z                  
2  -y,x-y,z               
3  -x+y,-x,z              
4  x-y,-y,-z              
5  -x,-x+y,-z             
6  y,x,-z                 
7  x+1/3,y+2/3,z+2/3      
8  -y+1/3,x-y+2/3,z+2/3   
9  -x+y+1/3,-x+2/3,z+2/3  
10 x-y+1/3,-y+2/3,-z+2/3  
11 -x+1/3,-x+y+2/3,-z+2/3 
12 y+1/3,x+2/3,-z+2/3     
13 x+2/3,y+1/3,z+1/3      
14 -y+2/3,x-y+1/3,z+1/3   
15 -x+y+2/3,-x+1/3,z+1/3  
16 x-y+2/3,-y+1/3,-z+1/3  
17 -x+2/3,-x+y+1/3,-z+1/3 
18 y+2/3,x+1/3,-z+1/3     
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 43.511 -35.126 -6.051 2.26507555648 1.38509381819 1.87349169653 -0.204357776096 -0.537848151852  
0.118170621778   8.43870054098 0.926525235178 4.85079508612 1.98259065287  -2.81120135866  1.34728398086  -1.30324651041   
0.452225178083 0.742289696031 0.444067320139  0.288672897375 2.1645221001    -1.75161913489 1.04269640868    -1.28251223902  
'X-RAY DIFFRACTION' 2 ? refined 52.099 -56.626 15.581 1.50805789817 1.41324776621 1.42998607377 -0.218465063545 -0.0943135012765 
-0.0634493629655 11.3605413422 8.08450273407  6.29961740386 -5.46926538684 -0.930776296546 -3.58800775712 0.44672317953    
0.496504171801 -1.0538893179  -0.116347364904 -1.43785714092 -0.743746362878 0.185553470704 0.702756928998   -0.205263007243 
'X-RAY DIFFRACTION' 3 ? refined 40.370 -10.498 11.740 1.55899619114 1.93032377727 2.13111405793 -0.220860448616 -0.21109417224   
0.355518185248   10.6805347861 9.11197014933  9.19470738568 1.41182604312  -2.67413487778  3.22284167976  -0.0361996130557 
-0.44061034831 0.621593381583 1.06883292777   1.4339679825   -0.339919376985 0.279646723365 -0.0924501534763 0.339130719568  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 B 1  B 96  '( CHAIN B AND RESID 1:96 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 A 1  A 115 '( CHAIN A AND RESID 1:115 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 3 3 B 97 B 197 '( CHAIN B AND RESID 97:197 )' ? ? ? ? ? 
# 
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 B THR 108 ? A THR 108 
2  1 Y 1 B ASN 109 ? A ASN 109 
3  1 Y 1 B VAL 110 ? A VAL 110 
4  1 Y 1 B SER 111 ? A SER 111 
5  1 Y 1 B SER 164 ? A SER 164 
6  1 Y 1 B THR 165 ? A THR 165 
7  1 Y 1 B LEU 166 ? A LEU 166 
8  1 Y 1 B LYS 167 ? A LYS 167 
9  1 Y 1 B SER 168 ? A SER 168 
10 1 Y 1 B ASN 198 ? A ASN 198 
11 1 Y 1 B SER 199 ? A SER 199 
12 1 Y 1 B TYR 200 ? A TYR 200 
13 1 Y 1 B ARG 201 ? A ARG 201 
14 1 Y 1 B GLU 202 ? A GLU 202 
15 1 Y 1 B PRO 203 ? A PRO 203 
16 1 Y 1 B PHE 204 ? A PHE 204 
17 1 Y 1 B GLU 205 ? A GLU 205 
18 1 Y 1 B GLN 206 ? A GLN 206 
19 1 Y 1 B HIS 207 ? A HIS 207 
20 1 Y 1 B HIS 208 ? A HIS 208 
21 1 Y 1 B HIS 209 ? A HIS 209 
22 1 Y 1 B HIS 210 ? A HIS 210 
23 1 Y 1 B HIS 211 ? A HIS 211 
24 1 Y 1 B HIS 212 ? A HIS 212 
25 1 Y 1 B HIS 213 ? A HIS 213 
26 1 Y 1 B ALA 214 ? A ALA 214 
27 1 Y 1 A GLU 116 ? B GLU 116 
28 1 Y 1 A SER 117 ? B SER 117 
29 1 Y 1 A HIS 118 ? B HIS 118 
30 1 Y 1 A HIS 119 ? B HIS 119 
31 1 Y 1 A HIS 120 ? B HIS 120 
32 1 Y 1 A HIS 121 ? B HIS 121 
33 1 Y 1 A HIS 122 ? B HIS 122 
34 1 Y 1 A HIS 123 ? B HIS 123 
35 1 Y 1 A ALA 124 ? B ALA 124 
# 
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 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
NAG C1   C N R 247 
NAG C2   C N R 248 
NAG C3   C N R 249 
NAG C4   C N S 250 
NAG C5   C N R 251 
NAG C6   C N N 252 
NAG C7   C N N 253 
NAG C8   C N N 254 
NAG N2   N N N 255 
NAG O1   O N N 256 
NAG O3   O N N 257 
NAG O4   O N N 258 
NAG O5   O N N 259 
NAG O6   O N N 260 
NAG O7   O N N 261 
NAG H1   H N N 262 
NAG H2   H N N 263 
NAG H3   H N N 264 
NAG H4   H N N 265 
NAG H5   H N N 266 
NAG H61  H N N 267 
NAG H62  H N N 268 
NAG H81  H N N 269 
NAG H82  H N N 270 
NAG H83  H N N 271 
NAG HN2  H N N 272 
NAG HO1  H N N 273 
NAG HO3  H N N 274 
NAG HO4  H N N 275 
NAG HO6  H N N 276 
PHE N    N N N 277 
PHE CA   C N S 278 
PHE C    C N N 279 
PHE O    O N N 280 
PHE CB   C N N 281 
PHE CG   C Y N 282 
PHE CD1  C Y N 283 
PHE CD2  C Y N 284 
PHE CE1  C Y N 285 
PHE CE2  C Y N 286 
PHE CZ   C Y N 287 
PHE OXT  O N N 288 
PHE H    H N N 289 
PHE H2   H N N 290 
PHE HA   H N N 291 
PHE HB2  H N N 292 
PHE HB3  H N N 293 
PHE HD1  H N N 294 
PHE HD2  H N N 295 
PHE HE1  H N N 296 
PHE HE2  H N N 297 
PHE HZ   H N N 298 
PHE HXT  H N N 299 
PRO N    N N N 300 
PRO CA   C N S 301 
PRO C    C N N 302 
PRO O    O N N 303 
PRO CB   C N N 304 
PRO CG   C N N 305 
PRO CD   C N N 306 
PRO OXT  O N N 307 
PRO H    H N N 308 
PRO HA   H N N 309 
PRO HB2  H N N 310 
PRO HB3  H N N 311 
PRO HG2  H N N 312 
PRO HG3  H N N 313 
PRO HD2  H N N 314 
PRO HD3  H N N 315 
PRO HXT  H N N 316 
SER N    N N N 317 
SER CA   C N S 318 
SER C    C N N 319 
SER O    O N N 320 
SER CB   C N N 321 
SER OG   O N N 322 
SER OXT  O N N 323 
SER H    H N N 324 
SER H2   H N N 325 
SER HA   H N N 326 
SER HB2  H N N 327 
SER HB3  H N N 328 
SER HG   H N N 329 
SER HXT  H N N 330 
THR N    N N N 331 
THR CA   C N S 332 
THR C    C N N 333 
THR O    O N N 334 
THR CB   C N R 335 
THR OG1  O N N 336 
THR CG2  C N N 337 
THR OXT  O N N 338 
THR H    H N N 339 
THR H2   H N N 340 
THR HA   H N N 341 
THR HB   H N N 342 
THR HG1  H N N 343 
THR HG21 H N N 344 
THR HG22 H N N 345 
THR HG23 H N N 346 
THR HXT  H N N 347 
TRP N    N N N 348 
TRP CA   C N S 349 
TRP C    C N N 350 
TRP O    O N N 351 
TRP CB   C N N 352 
TRP CG   C Y N 353 
TRP CD1  C Y N 354 
TRP CD2  C Y N 355 
TRP NE1  N Y N 356 
TRP CE2  C Y N 357 
TRP CE3  C Y N 358 
TRP CZ2  C Y N 359 
TRP CZ3  C Y N 360 
TRP CH2  C Y N 361 
TRP OXT  O N N 362 
TRP H    H N N 363 
TRP H2   H N N 364 
TRP HA   H N N 365 
TRP HB2  H N N 366 
TRP HB3  H N N 367 
TRP HD1  H N N 368 
TRP HE1  H N N 369 
TRP HE3  H N N 370 
TRP HZ2  H N N 371 
TRP HZ3  H N N 372 
TRP HH2  H N N 373 
TRP HXT  H N N 374 
TYR N    N N N 375 
TYR CA   C N S 376 
TYR C    C N N 377 
TYR O    O N N 378 
TYR CB   C N N 379 
TYR CG   C Y N 380 
TYR CD1  C Y N 381 
TYR CD2  C Y N 382 
TYR CE1  C Y N 383 
TYR CE2  C Y N 384 
TYR CZ   C Y N 385 
TYR OH   O N N 386 
TYR OXT  O N N 387 
TYR H    H N N 388 
TYR H2   H N N 389 
TYR HA   H N N 390 
TYR HB2  H N N 391 
TYR HB3  H N N 392 
TYR HD1  H N N 393 
TYR HD2  H N N 394 
TYR HE1  H N N 395 
TYR HE2  H N N 396 
TYR HH   H N N 397 
TYR HXT  H N N 398 
VAL N    N N N 399 
VAL CA   C N S 400 
VAL C    C N N 401 
VAL O    O N N 402 
VAL CB   C N N 403 
VAL CG1  C N N 404 
VAL CG2  C N N 405 
VAL OXT  O N N 406 
VAL H    H N N 407 
VAL H2   H N N 408 
VAL HA   H N N 409 
VAL HB   H N N 410 
VAL HG11 H N N 411 
VAL HG12 H N N 412 
VAL HG13 H N N 413 
VAL HG21 H N N 414 
VAL HG22 H N N 415 
VAL HG23 H N N 416 
VAL HXT  H N N 417 
# 
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 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
NAG C1  C2   sing N N 235 
NAG C1  O1   sing N N 236 
NAG C1  O5   sing N N 237 
NAG C1  H1   sing N N 238 
NAG C2  C3   sing N N 239 
NAG C2  N2   sing N N 240 
NAG C2  H2   sing N N 241 
NAG C3  C4   sing N N 242 
NAG C3  O3   sing N N 243 
NAG C3  H3   sing N N 244 
NAG C4  C5   sing N N 245 
NAG C4  O4   sing N N 246 
NAG C4  H4   sing N N 247 
NAG C5  C6   sing N N 248 
NAG C5  O5   sing N N 249 
NAG C5  H5   sing N N 250 
NAG C6  O6   sing N N 251 
NAG C6  H61  sing N N 252 
NAG C6  H62  sing N N 253 
NAG C7  C8   sing N N 254 
NAG C7  N2   sing N N 255 
NAG C7  O7   doub N N 256 
NAG C8  H81  sing N N 257 
NAG C8  H82  sing N N 258 
NAG C8  H83  sing N N 259 
NAG N2  HN2  sing N N 260 
NAG O1  HO1  sing N N 261 
NAG O3  HO3  sing N N 262 
NAG O4  HO4  sing N N 263 
NAG O6  HO6  sing N N 264 
PHE N   CA   sing N N 265 
PHE N   H    sing N N 266 
PHE N   H2   sing N N 267 
PHE CA  C    sing N N 268 
PHE CA  CB   sing N N 269 
PHE CA  HA   sing N N 270 
PHE C   O    doub N N 271 
PHE C   OXT  sing N N 272 
PHE CB  CG   sing N N 273 
PHE CB  HB2  sing N N 274 
PHE CB  HB3  sing N N 275 
PHE CG  CD1  doub Y N 276 
PHE CG  CD2  sing Y N 277 
PHE CD1 CE1  sing Y N 278 
PHE CD1 HD1  sing N N 279 
PHE CD2 CE2  doub Y N 280 
PHE CD2 HD2  sing N N 281 
PHE CE1 CZ   doub Y N 282 
PHE CE1 HE1  sing N N 283 
PHE CE2 CZ   sing Y N 284 
PHE CE2 HE2  sing N N 285 
PHE CZ  HZ   sing N N 286 
PHE OXT HXT  sing N N 287 
PRO N   CA   sing N N 288 
PRO N   CD   sing N N 289 
PRO N   H    sing N N 290 
PRO CA  C    sing N N 291 
PRO CA  CB   sing N N 292 
PRO CA  HA   sing N N 293 
PRO C   O    doub N N 294 
PRO C   OXT  sing N N 295 
PRO CB  CG   sing N N 296 
PRO CB  HB2  sing N N 297 
PRO CB  HB3  sing N N 298 
PRO CG  CD   sing N N 299 
PRO CG  HG2  sing N N 300 
PRO CG  HG3  sing N N 301 
PRO CD  HD2  sing N N 302 
PRO CD  HD3  sing N N 303 
PRO OXT HXT  sing N N 304 
SER N   CA   sing N N 305 
SER N   H    sing N N 306 
SER N   H2   sing N N 307 
SER CA  C    sing N N 308 
SER CA  CB   sing N N 309 
SER CA  HA   sing N N 310 
SER C   O    doub N N 311 
SER C   OXT  sing N N 312 
SER CB  OG   sing N N 313 
SER CB  HB2  sing N N 314 
SER CB  HB3  sing N N 315 
SER OG  HG   sing N N 316 
SER OXT HXT  sing N N 317 
THR N   CA   sing N N 318 
THR N   H    sing N N 319 
THR N   H2   sing N N 320 
THR CA  C    sing N N 321 
THR CA  CB   sing N N 322 
THR CA  HA   sing N N 323 
THR C   O    doub N N 324 
THR C   OXT  sing N N 325 
THR CB  OG1  sing N N 326 
THR CB  CG2  sing N N 327 
THR CB  HB   sing N N 328 
THR OG1 HG1  sing N N 329 
THR CG2 HG21 sing N N 330 
THR CG2 HG22 sing N N 331 
THR CG2 HG23 sing N N 332 
THR OXT HXT  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
3 NAG 1 n 
3 NAG 2 n 
# 
_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   1IAR 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'R 3 2 :H' 
_space_group.name_Hall        
;R 3 2"
;
_space_group.IT_number        155 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Z8L 
_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]   0.006996 
_atom_sites.fract_transf_matrix[1][2]   0.004039 
_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]   0.008078 
_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]   0.006707 
_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 ? ? 5.96793  ? ? ? 14.89577 ? ? ? 0.0 
;1-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 ? ? 15.91112 ? ? ? 10.84690 ? ? ? 0.0 
;1-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   . MET A 1 1   ? 40.48019 -33.08653 -22.40977 1.000 264.54950 ? 1   MET B N   1 
ATOM   2    C CA  . MET A 1 1   ? 40.81041 -34.49238 -22.62512 1.000 263.99994 ? 1   MET B CA  1 
ATOM   3    C C   . MET A 1 1   ? 42.21936 -34.81778 -22.13382 1.000 255.61883 ? 1   MET B C   1 
ATOM   4    O O   . MET A 1 1   ? 42.53031 -35.97949 -21.85269 1.000 253.50619 ? 1   MET B O   1 
ATOM   5    C CB  . MET A 1 1   ? 40.68450 -34.85222 -24.10923 1.000 252.47308 ? 1   MET B CB  1 
ATOM   6    C CG  . MET A 1 1   ? 41.89348 -34.46241 -24.95023 1.000 251.44547 ? 1   MET B CG  1 
ATOM   7    S SD  . MET A 1 1   ? 41.44787 -33.92706 -26.61255 1.000 261.78668 ? 1   MET B SD  1 
ATOM   8    C CE  . MET A 1 1   ? 41.15781 -32.18479 -26.32588 1.000 262.00451 ? 1   MET B CE  1 
ATOM   9    N N   . LYS A 1 2   ? 43.06506 -33.79076 -22.03092 1.000 263.43832 ? 2   LYS B N   1 
ATOM   10   C CA  . LYS A 1 2   ? 44.43272 -33.94535 -21.54339 1.000 255.72627 ? 2   LYS B CA  1 
ATOM   11   C C   . LYS A 1 2   ? 44.74409 -32.79133 -20.60094 1.000 252.52694 ? 2   LYS B C   1 
ATOM   12   O O   . LYS A 1 2   ? 44.63708 -31.62833 -21.00004 1.000 256.30129 ? 2   LYS B O   1 
ATOM   13   C CB  . LYS A 1 2   ? 45.43371 -33.98334 -22.70469 1.000 257.19023 ? 2   LYS B CB  1 
ATOM   14   N N   . VAL A 1 3   ? 45.13637 -33.11037 -19.36106 1.000 256.51813 ? 3   VAL B N   1 
ATOM   15   C CA  . VAL A 1 3   ? 45.41373 -32.11113 -18.32796 1.000 254.96981 ? 3   VAL B CA  1 
ATOM   16   C C   . VAL A 1 3   ? 46.58893 -31.23687 -18.75465 1.000 251.50909 ? 3   VAL B C   1 
ATOM   17   O O   . VAL A 1 3   ? 47.74940 -31.65810 -18.67589 1.000 244.98330 ? 3   VAL B O   1 
ATOM   18   C CB  . VAL A 1 3   ? 45.69295 -32.77480 -16.96197 1.000 251.09244 ? 3   VAL B CB  1 
ATOM   19   C CG1 . VAL A 1 3   ? 45.56295 -31.76158 -15.82700 1.000 256.20627 ? 3   VAL B CG1 1 
ATOM   20   C CG2 . VAL A 1 3   ? 44.76754 -33.96491 -16.73264 1.000 252.38236 ? 3   VAL B CG2 1 
ATOM   21   N N   . LEU A 1 4   ? 46.29388 -30.01011 -19.20555 1.000 246.04885 ? 4   LEU B N   1 
ATOM   22   C CA  . LEU A 1 4   ? 47.34987 -29.08294 -19.61107 1.000 243.52824 ? 4   LEU B CA  1 
ATOM   23   C C   . LEU A 1 4   ? 48.11468 -28.54699 -18.40568 1.000 239.11748 ? 4   LEU B C   1 
ATOM   24   O O   . LEU A 1 4   ? 49.34026 -28.39638 -18.45948 1.000 234.39950 ? 4   LEU B O   1 
ATOM   25   C CB  . LEU A 1 4   ? 46.75753 -27.92709 -20.42427 1.000 250.95061 ? 4   LEU B CB  1 
ATOM   26   C CG  . LEU A 1 4   ? 46.13831 -28.26286 -21.78422 1.000 254.12353 ? 4   LEU B CG  1 
ATOM   27   C CD1 . LEU A 1 4   ? 46.12230 -27.03819 -22.69351 1.000 263.68191 ? 4   LEU B CD1 1 
ATOM   28   C CD2 . LEU A 1 4   ? 46.88339 -29.41716 -22.44961 1.000 251.55729 ? 4   LEU B CD2 1 
ATOM   29   N N   . GLN A 1 5   ? 47.41372 -28.24269 -17.31664 1.000 252.55265 ? 5   GLN B N   1 
ATOM   30   C CA  . GLN A 1 5   ? 48.02272 -27.69744 -16.10842 1.000 249.51714 ? 5   GLN B CA  1 
ATOM   31   C C   . GLN A 1 5   ? 48.11233 -28.79108 -15.05324 1.000 247.76533 ? 5   GLN B C   1 
ATOM   32   O O   . GLN A 1 5   ? 47.08179 -29.30121 -14.60343 1.000 255.33094 ? 5   GLN B O   1 
ATOM   33   C CB  . GLN A 1 5   ? 47.21960 -26.50845 -15.58179 1.000 257.98110 ? 5   GLN B CB  1 
ATOM   34   C CG  . GLN A 1 5   ? 47.68803 -25.98041 -14.23981 1.000 254.94101 ? 5   GLN B CG  1 
ATOM   35   C CD  . GLN A 1 5   ? 49.19126 -25.82125 -14.17327 1.000 243.20508 ? 5   GLN B CD  1 
ATOM   36   O OE1 . GLN A 1 5   ? 49.76907 -24.98815 -14.86567 1.000 241.31983 ? 5   GLN B OE1 1 
ATOM   37   N NE2 . GLN A 1 5   ? 49.83150 -26.60679 -13.31401 1.000 234.62221 ? 5   GLN B NE2 1 
ATOM   38   N N   . GLU A 1 6   ? 49.33761 -29.14168 -14.66213 1.000 246.96123 ? 6   GLU B N   1 
ATOM   39   C CA  . GLU A 1 6   ? 49.54804 -30.14286 -13.62187 1.000 244.90328 ? 6   GLU B CA  1 
ATOM   40   C C   . GLU A 1 6   ? 48.76193 -29.76542 -12.37297 1.000 251.67394 ? 6   GLU B C   1 
ATOM   41   O O   . GLU A 1 6   ? 48.77487 -28.59006 -11.97201 1.000 252.93304 ? 6   GLU B O   1 
ATOM   42   C CB  . GLU A 1 6   ? 51.04103 -30.28523 -13.29201 1.000 234.79181 ? 6   GLU B CB  1 
ATOM   43   C CG  . GLU A 1 6   ? 52.00632 -30.44800 -14.48804 1.000 233.07214 ? 6   GLU B CG  1 
ATOM   44   C CD  . GLU A 1 6   ? 52.27961 -29.16199 -15.26667 1.000 234.72151 ? 6   GLU B CD  1 
ATOM   45   O OE1 . GLU A 1 6   ? 51.47495 -28.21276 -15.17031 1.000 238.67153 ? 6   GLU B OE1 1 
ATOM   46   O OE2 . GLU A 1 6   ? 53.29818 -29.10371 -15.98642 1.000 232.15559 ? 6   GLU B OE2 1 
ATOM   47   N N   . PRO A 1 7   ? 48.05990 -30.70680 -11.73464 1.000 219.14599 ? 7   PRO B N   1 
ATOM   48   C CA  . PRO A 1 7   ? 47.20951 -30.37230 -10.58788 1.000 226.57090 ? 7   PRO B CA  1 
ATOM   49   C C   . PRO A 1 7   ? 47.99229 -29.74155 -9.44562  1.000 223.33191 ? 7   PRO B C   1 
ATOM   50   O O   . PRO A 1 7   ? 49.17947 -30.01089 -9.24976  1.000 214.19124 ? 7   PRO B O   1 
ATOM   51   C CB  . PRO A 1 7   ? 46.63127 -31.72993 -10.17418 1.000 229.81429 ? 7   PRO B CB  1 
ATOM   52   C CG  . PRO A 1 7   ? 46.64387 -32.51091 -11.44342 1.000 226.25394 ? 7   PRO B CG  1 
ATOM   53   C CD  . PRO A 1 7   ? 47.95801 -32.13855 -12.06982 1.000 217.18236 ? 7   PRO B CD  1 
ATOM   54   N N   . THR A 1 8   ? 47.29854 -28.90061 -8.68052  1.000 223.83127 ? 8   THR B N   1 
ATOM   55   C CA  . THR A 1 8   ? 47.88616 -28.18196 -7.55746  1.000 219.54717 ? 8   THR B CA  1 
ATOM   56   C C   . THR A 1 8   ? 46.89211 -28.16201 -6.40694  1.000 226.62824 ? 8   THR B C   1 
ATOM   57   O O   . THR A 1 8   ? 45.70543 -27.89343 -6.61709  1.000 233.83348 ? 8   THR B O   1 
ATOM   58   C CB  . THR A 1 8   ? 48.26055 -26.75011 -7.95579  1.000 216.42185 ? 8   THR B CB  1 
ATOM   59   O OG1 . THR A 1 8   ? 47.24092 -26.21119 -8.80714  1.000 224.19023 ? 8   THR B OG1 1 
ATOM   60   C CG2 . THR A 1 8   ? 49.58838 -26.73431 -8.69693  1.000 207.77351 ? 8   THR B CG2 1 
ATOM   61   N N   . CYS A 1 9   ? 47.37409 -28.43893 -5.19569  1.000 212.38824 ? 9   CYS B N   1 
ATOM   62   C CA  . CYS A 1 9   ? 46.51517 -28.51255 -4.02326  1.000 218.56818 ? 9   CYS B CA  1 
ATOM   63   C C   . CYS A 1 9   ? 47.09700 -27.72970 -2.85593  1.000 215.23237 ? 9   CYS B C   1 
ATOM   64   O O   . CYS A 1 9   ? 48.31486 -27.66260 -2.66763  1.000 208.57505 ? 9   CYS B O   1 
ATOM   65   C CB  . CYS A 1 9   ? 46.28427 -29.96068 -3.57503  1.000 221.84961 ? 9   CYS B CB  1 
ATOM   66   S SG  . CYS A 1 9   ? 45.95128 -31.13123 -4.90097  1.000 224.14101 ? 9   CYS B SG  1 
ATOM   67   N N   . VAL A 1 10  ? 46.19605 -27.14332 -2.06994  1.000 208.53119 ? 10  VAL B N   1 
ATOM   68   C CA  . VAL A 1 10  ? 46.50914 -26.60074 -0.75793  1.000 208.14288 ? 10  VAL B CA  1 
ATOM   69   C C   . VAL A 1 10  ? 45.66144 -27.34757 0.26264   1.000 211.46236 ? 10  VAL B C   1 
ATOM   70   O O   . VAL A 1 10  ? 44.62257 -27.92798 -0.06144  1.000 214.71053 ? 10  VAL B O   1 
ATOM   71   C CB  . VAL A 1 10  ? 46.26672 -25.07996 -0.66851  1.000 208.60727 ? 10  VAL B CB  1 
ATOM   72   C CG1 . VAL A 1 10  ? 47.19053 -24.33893 -1.62112  1.000 203.81935 ? 10  VAL B CG1 1 
ATOM   73   C CG2 . VAL A 1 10  ? 44.81193 -24.75533 -0.96670  1.000 213.15733 ? 10  VAL B CG2 1 
ATOM   74   N N   . SER A 1 11  ? 46.12153 -27.33817 1.50874   1.000 200.56035 ? 11  SER B N   1 
ATOM   75   C CA  . SER A 1 11  ? 45.47007 -28.07280 2.58320   1.000 202.54234 ? 11  SER B CA  1 
ATOM   76   C C   . SER A 1 11  ? 45.06380 -27.11269 3.68887   1.000 203.62939 ? 11  SER B C   1 
ATOM   77   O O   . SER A 1 11  ? 45.85346 -26.25211 4.08938   1.000 202.11581 ? 11  SER B O   1 
ATOM   78   C CB  . SER A 1 11  ? 46.39146 -29.15830 3.14454   1.000 200.90949 ? 11  SER B CB  1 
ATOM   79   O OG  . SER A 1 11  ? 45.68438 -30.01430 4.02401   1.000 203.95823 ? 11  SER B OG  1 
ATOM   80   N N   . ASP A 1 12  ? 43.83392 -27.26055 4.18309   1.000 196.91540 ? 12  ASP B N   1 
ATOM   81   C CA  . ASP A 1 12  ? 43.44977 -26.51656 5.37434   1.000 197.34147 ? 12  ASP B CA  1 
ATOM   82   C C   . ASP A 1 12  ? 44.09083 -27.08551 6.63142   1.000 195.82604 ? 12  ASP B C   1 
ATOM   83   O O   . ASP A 1 12  ? 43.98591 -26.47051 7.69817   1.000 196.12474 ? 12  ASP B O   1 
ATOM   84   C CB  . ASP A 1 12  ? 41.92368 -26.47565 5.50434   1.000 199.85804 ? 12  ASP B CB  1 
ATOM   85   C CG  . ASP A 1 12  ? 41.31215 -27.83191 5.81797   1.000 201.96812 ? 12  ASP B CG  1 
ATOM   86   O OD1 . ASP A 1 12  ? 42.04041 -28.84539 5.87532   1.000 201.47337 ? 12  ASP B OD1 1 
ATOM   87   O OD2 . ASP A 1 12  ? 40.07845 -27.88213 6.00062   1.000 204.62821 ? 12  ASP B OD2 1 
ATOM   88   N N   . TYR A 1 13  ? 44.73607 -28.24634 6.51613   1.000 206.86721 ? 13  TYR B N   1 
ATOM   89   C CA  . TYR A 1 13  ? 45.53605 -28.88546 7.55499   1.000 205.38992 ? 13  TYR B CA  1 
ATOM   90   C C   . TYR A 1 13  ? 44.69699 -29.34076 8.74374   1.000 206.89330 ? 13  TYR B C   1 
ATOM   91   O O   . TYR A 1 13  ? 45.21135 -29.45682 9.86089   1.000 205.06212 ? 13  TYR B O   1 
ATOM   92   C CB  . TYR A 1 13  ? 46.67749 -27.97396 8.02387   1.000 202.45531 ? 13  TYR B CB  1 
ATOM   93   C CG  . TYR A 1 13  ? 47.83950 -28.72935 8.62779   1.000 200.80231 ? 13  TYR B CG  1 
ATOM   94   C CD1 . TYR A 1 13  ? 47.96163 -30.09881 8.44965   1.000 200.84872 ? 13  TYR B CD1 1 
ATOM   95   C CD2 . TYR A 1 13  ? 48.82876 -28.07350 9.34391   1.000 198.80242 ? 13  TYR B CD2 1 
ATOM   96   C CE1 . TYR A 1 13  ? 49.01925 -30.79993 8.98704   1.000 199.24893 ? 13  TYR B CE1 1 
ATOM   97   C CE2 . TYR A 1 13  ? 49.89487 -28.76619 9.88496   1.000 196.39170 ? 13  TYR B CE2 1 
ATOM   98   C CZ  . TYR A 1 13  ? 49.98509 -30.13005 9.70230   1.000 196.86163 ? 13  TYR B CZ  1 
ATOM   99   O OH  . TYR A 1 13  ? 51.04407 -30.82736 10.23688  1.000 194.69805 ? 13  TYR B OH  1 
ATOM   100  N N   . MET A 1 14  ? 43.41621 -29.59002 8.52769   1.000 202.27788 ? 14  MET B N   1 
ATOM   101  C CA  . MET A 1 14  ? 42.58836 -30.30531 9.49144   1.000 204.47727 ? 14  MET B CA  1 
ATOM   102  C C   . MET A 1 14  ? 41.72570 -31.37129 8.84049   1.000 209.77592 ? 14  MET B C   1 
ATOM   103  O O   . MET A 1 14  ? 41.60355 -32.46966 9.38853   1.000 213.04112 ? 14  MET B O   1 
ATOM   104  C CB  . MET A 1 14  ? 41.67377 -29.36100 10.28276  1.000 204.29541 ? 14  MET B CB  1 
ATOM   105  C CG  . MET A 1 14  ? 41.08964 -30.02653 11.52289  1.000 204.50730 ? 14  MET B CG  1 
ATOM   106  S SD  . MET A 1 14  ? 39.99477 -28.97138 12.48111  1.000 204.57989 ? 14  MET B SD  1 
ATOM   107  C CE  . MET A 1 14  ? 38.61088 -30.08161 12.74101  1.000 208.08795 ? 14  MET B CE  1 
ATOM   108  N N   . SER A 1 15  ? 41.12171 -31.07822 7.68888   1.000 209.38083 ? 15  SER B N   1 
ATOM   109  C CA  . SER A 1 15  ? 40.15685 -32.00485 7.11373   1.000 214.28276 ? 15  SER B CA  1 
ATOM   110  C C   . SER A 1 15  ? 40.12529 -31.99226 5.58882   1.000 215.59144 ? 15  SER B C   1 
ATOM   111  O O   . SER A 1 15  ? 39.85968 -33.02923 4.97508   1.000 220.85996 ? 15  SER B O   1 
ATOM   112  C CB  . SER A 1 15  ? 38.75803 -31.71188 7.66444   1.000 215.68789 ? 15  SER B CB  1 
ATOM   113  O OG  . SER A 1 15  ? 38.43403 -30.33842 7.54491   1.000 214.36886 ? 15  SER B OG  1 
ATOM   114  N N   . ILE A 1 16  ? 40.39075 -30.84930 4.95968   1.000 209.07360 ? 16  ILE B N   1 
ATOM   115  C CA  . ILE A 1 16  ? 40.14559 -30.67524 3.53134   1.000 210.18390 ? 16  ILE B CA  1 
ATOM   116  C C   . ILE A 1 16  ? 41.43221 -30.26197 2.83015   1.000 205.58897 ? 16  ILE B C   1 
ATOM   117  O O   . ILE A 1 16  ? 42.09208 -29.30099 3.24058   1.000 201.83601 ? 16  ILE B O   1 
ATOM   118  C CB  . ILE A 1 16  ? 39.03463 -29.64109 3.27205   1.000 211.29628 ? 16  ILE B CB  1 
ATOM   119  C CG1 . ILE A 1 16  ? 37.69710 -30.15024 3.81306   1.000 215.56776 ? 16  ILE B CG1 1 
ATOM   120  C CG2 . ILE A 1 16  ? 38.93305 -29.32454 1.78600   1.000 212.29118 ? 16  ILE B CG2 1 
ATOM   121  C CD1 . ILE A 1 16  ? 36.58742 -29.12142 3.76862   1.000 217.29657 ? 16  ILE B CD1 1 
ATOM   122  N N   . SER A 1 17  ? 41.77567 -30.97995 1.76461   1.000 208.73629 ? 17  SER B N   1 
ATOM   123  C CA  . SER A 1 17  ? 42.82224 -30.57434 0.83311   1.000 204.90501 ? 17  SER B CA  1 
ATOM   124  C C   . SER A 1 17  ? 42.15520 -30.31860 -0.51351  1.000 207.51084 ? 17  SER B C   1 
ATOM   125  O O   . SER A 1 17  ? 41.77034 -31.26346 -1.21001  1.000 211.54114 ? 17  SER B O   1 
ATOM   126  C CB  . SER A 1 17  ? 43.91186 -31.63818 0.72282   1.000 203.85903 ? 17  SER B CB  1 
ATOM   127  O OG  . SER A 1 17  ? 44.71908 -31.66554 1.88719   1.000 201.83879 ? 17  SER B OG  1 
ATOM   128  N N   . THR A 1 18  ? 42.00382 -29.04517 -0.86972  1.000 209.97766 ? 18  THR B N   1 
ATOM   129  C CA  . THR A 1 18  ? 41.31987 -28.65696 -2.09717  1.000 212.58722 ? 18  THR B CA  1 
ATOM   130  C C   . THR A 1 18  ? 42.31392 -28.61023 -3.25297  1.000 209.81532 ? 18  THR B C   1 
ATOM   131  O O   . THR A 1 18  ? 43.40374 -28.04477 -3.11865  1.000 205.26694 ? 18  THR B O   1 
ATOM   132  C CB  . THR A 1 18  ? 40.63853 -27.29774 -1.92305  1.000 213.96130 ? 18  THR B CB  1 
ATOM   133  O OG1 . THR A 1 18  ? 39.63562 -27.39059 -0.90266  1.000 217.70354 ? 18  THR B OG1 1 
ATOM   134  C CG2 . THR A 1 18  ? 39.98389 -26.85395 -3.22303  1.000 216.20574 ? 18  THR B CG2 1 
ATOM   135  N N   . CYS A 1 19  ? 41.93611 -29.20467 -4.38291  1.000 227.67422 ? 19  CYS B N   1 
ATOM   136  C CA  . CYS A 1 19  ? 42.79670 -29.31247 -5.55235  1.000 225.48124 ? 19  CYS B CA  1 
ATOM   137  C C   . CYS A 1 19  ? 42.14639 -28.65047 -6.76187  1.000 227.83481 ? 19  CYS B C   1 
ATOM   138  O O   . CYS A 1 19  ? 40.94948 -28.34864 -6.77363  1.000 232.08393 ? 19  CYS B O   1 
ATOM   139  C CB  . CYS A 1 19  ? 43.11495 -30.77964 -5.87185  1.000 226.24808 ? 19  CYS B CB  1 
ATOM   140  S SG  . CYS A 1 19  ? 44.01568 -31.66046 -4.58604  1.000 225.73066 ? 19  CYS B SG  1 
ATOM   141  N N   . GLU A 1 20  ? 42.96311 -28.43275 -7.79180  1.000 236.47357 ? 20  GLU B N   1 
ATOM   142  C CA  . GLU A 1 20  ? 42.48170 -27.93068 -9.07097  1.000 239.87503 ? 20  GLU B CA  1 
ATOM   143  C C   . GLU A 1 20  ? 43.49247 -28.29220 -10.14841 1.000 236.11653 ? 20  GLU B C   1 
ATOM   144  O O   . GLU A 1 20  ? 44.67709 -28.49811 -9.87230  1.000 229.85353 ? 20  GLU B O   1 
ATOM   145  C CB  . GLU A 1 20  ? 42.25544 -26.41475 -9.04980  1.000 241.01921 ? 20  GLU B CB  1 
ATOM   146  C CG  . GLU A 1 20  ? 43.51834 -25.59502 -8.87046  1.000 238.58841 ? 20  GLU B CG  1 
ATOM   147  C CD  . GLU A 1 20  ? 43.39587 -24.21154 -9.47760  1.000 240.91012 ? 20  GLU B CD  1 
ATOM   148  O OE1 . GLU A 1 20  ? 42.39431 -23.52441 -9.18784  1.000 245.60920 ? 20  GLU B OE1 1 
ATOM   149  O OE2 . GLU A 1 20  ? 44.29575 -23.81379 -10.24854 1.000 237.85784 ? 20  GLU B OE2 1 
ATOM   150  N N   . TRP A 1 21  ? 43.00278 -28.36927 -11.38121 1.000 245.04264 ? 21  TRP B N   1 
ATOM   151  C CA  . TRP A 1 21  ? 43.84694 -28.59545 -12.54665 1.000 239.78735 ? 21  TRP B CA  1 
ATOM   152  C C   . TRP A 1 21  ? 43.10090 -28.08867 -13.77396 1.000 244.81058 ? 21  TRP B C   1 
ATOM   153  O O   . TRP A 1 21  ? 41.98414 -27.57329 -13.67637 1.000 250.79583 ? 21  TRP B O   1 
ATOM   154  C CB  . TRP A 1 21  ? 44.24623 -30.07061 -12.67918 1.000 235.18318 ? 21  TRP B CB  1 
ATOM   155  C CG  . TRP A 1 21  ? 43.10776 -31.03080 -12.87087 1.000 240.80738 ? 21  TRP B CG  1 
ATOM   156  C CD1 . TRP A 1 21  ? 42.68473 -31.57613 -14.04769 1.000 241.13845 ? 21  TRP B CD1 1 
ATOM   157  C CD2 . TRP A 1 21  ? 42.27550 -31.59161 -11.84792 1.000 245.96740 ? 21  TRP B CD2 1 
ATOM   158  N NE1 . TRP A 1 21  ? 41.62829 -32.42537 -13.82413 1.000 246.99089 ? 21  TRP B NE1 1 
ATOM   159  C CE2 . TRP A 1 21  ? 41.36058 -32.45640 -12.48091 1.000 249.62434 ? 21  TRP B CE2 1 
ATOM   160  C CE3 . TRP A 1 21  ? 42.21058 -31.44056 -10.46038 1.000 247.03317 ? 21  TRP B CE3 1 
ATOM   161  C CZ2 . TRP A 1 21  ? 40.38927 -33.16295 -11.77444 1.000 254.79023 ? 21  TRP B CZ2 1 
ATOM   162  C CZ3 . TRP A 1 21  ? 41.24882 -32.14285 -9.76224  1.000 251.41265 ? 21  TRP B CZ3 1 
ATOM   163  C CH2 . TRP A 1 21  ? 40.34990 -32.99322 -10.41892 1.000 255.77905 ? 21  TRP B CH2 1 
ATOM   164  N N   . LYS A 1 22  ? 43.73235 -28.23297 -14.93726 1.000 250.58495 ? 22  LYS B N   1 
ATOM   165  C CA  . LYS A 1 22  ? 43.18352 -27.71250 -16.18485 1.000 255.87288 ? 22  LYS B CA  1 
ATOM   166  C C   . LYS A 1 22  ? 43.49830 -28.67847 -17.31413 1.000 251.49734 ? 22  LYS B C   1 
ATOM   167  O O   . LYS A 1 22  ? 44.66724 -28.99770 -17.55076 1.000 241.85648 ? 22  LYS B O   1 
ATOM   168  C CB  . LYS A 1 22  ? 43.74798 -26.32281 -16.49815 1.000 255.61502 ? 22  LYS B CB  1 
ATOM   169  N N   . MET A 1 23  ? 42.46104 -29.13869 -18.00847 1.000 255.32085 ? 23  MET B N   1 
ATOM   170  C CA  . MET A 1 23  ? 42.62353 -29.97084 -19.18968 1.000 252.73814 ? 23  MET B CA  1 
ATOM   171  C C   . MET A 1 23  ? 42.55275 -29.09212 -20.43023 1.000 255.04994 ? 23  MET B C   1 
ATOM   172  O O   . MET A 1 23  ? 42.48237 -27.86401 -20.34326 1.000 259.64680 ? 23  MET B O   1 
ATOM   173  C CB  . MET A 1 23  ? 41.54382 -31.04820 -19.25658 1.000 257.85019 ? 23  MET B CB  1 
ATOM   174  C CG  . MET A 1 23  ? 41.25927 -31.70903 -17.93118 1.000 258.51280 ? 23  MET B CG  1 
ATOM   175  S SD  . MET A 1 23  ? 40.52402 -33.33639 -18.10985 1.000 260.36657 ? 23  MET B SD  1 
ATOM   176  C CE  . MET A 1 23  ? 41.86781 -34.25420 -18.84526 1.000 249.62326 ? 23  MET B CE  1 
ATOM   177  N N   . ASN A 1 24  ? 42.54205 -29.72930 -21.59992 1.000 263.35688 ? 24  ASN B N   1 
ATOM   178  C CA  . ASN A 1 24  ? 42.35998 -29.02303 -22.86116 1.000 266.28756 ? 24  ASN B CA  1 
ATOM   179  C C   . ASN A 1 24  ? 40.91647 -29.20960 -23.31832 1.000 274.89425 ? 24  ASN B C   1 
ATOM   180  O O   . ASN A 1 24  ? 40.45012 -30.34411 -23.45652 1.000 275.21242 ? 24  ASN B O   1 
ATOM   181  C CB  . ASN A 1 24  ? 43.32926 -29.51665 -23.93695 1.000 262.55593 ? 24  ASN B CB  1 
ATOM   182  C CG  . ASN A 1 24  ? 43.49638 -31.02094 -23.94113 1.000 261.21782 ? 24  ASN B CG  1 
ATOM   183  O OD1 . ASN A 1 24  ? 42.69717 -31.75574 -23.36605 1.000 261.76287 ? 24  ASN B OD1 1 
ATOM   184  N ND2 . ASN A 1 24  ? 44.54394 -31.48804 -24.60654 1.000 259.81243 ? 24  ASN B ND2 1 
ATOM   185  N N   . GLY A 1 25  ? 40.20911 -28.09940 -23.53342 1.000 257.30460 ? 25  GLY B N   1 
ATOM   186  C CA  . GLY A 1 25  ? 38.83448 -28.14350 -23.98568 1.000 266.44658 ? 25  GLY B CA  1 
ATOM   187  C C   . GLY A 1 25  ? 37.84945 -28.47077 -22.87615 1.000 267.61634 ? 25  GLY B C   1 
ATOM   188  O O   . GLY A 1 25  ? 38.22993 -28.97684 -21.81570 1.000 264.38260 ? 25  GLY B O   1 
ATOM   189  N N   . PRO A 1 26  ? 36.55914 -28.18915 -23.11039 1.000 265.66674 ? 26  PRO B N   1 
ATOM   190  C CA  . PRO A 1 26  ? 35.53011 -28.41974 -22.08138 1.000 267.21612 ? 26  PRO B CA  1 
ATOM   191  C C   . PRO A 1 26  ? 35.46755 -29.86065 -21.60098 1.000 264.03626 ? 26  PRO B C   1 
ATOM   192  O O   . PRO A 1 26  ? 35.47310 -30.80176 -22.39703 1.000 262.62955 ? 26  PRO B O   1 
ATOM   193  C CB  . PRO A 1 26  ? 34.22345 -28.02502 -22.78815 1.000 275.20889 ? 26  PRO B CB  1 
ATOM   194  C CG  . PRO A 1 26  ? 34.55345 -27.94159 -24.23007 1.000 279.39694 ? 26  PRO B CG  1 
ATOM   195  C CD  . PRO A 1 26  ? 35.99131 -27.53053 -24.29484 1.000 274.11057 ? 26  PRO B CD  1 
ATOM   196  N N   . THR A 1 27  ? 35.39207 -30.02709 -20.27953 1.000 273.40359 ? 27  THR B N   1 
ATOM   197  C CA  . THR A 1 27  ? 35.28927 -31.35432 -19.68147 1.000 271.43891 ? 27  THR B CA  1 
ATOM   198  C C   . THR A 1 27  ? 34.38618 -31.26204 -18.46150 1.000 274.53198 ? 27  THR B C   1 
ATOM   199  O O   . THR A 1 27  ? 34.60828 -30.40878 -17.59806 1.000 273.79633 ? 27  THR B O   1 
ATOM   200  C CB  . THR A 1 27  ? 36.67203 -31.88630 -19.29479 1.000 244.96358 ? 27  THR B CB  1 
ATOM   201  O OG1 . THR A 1 27  ? 37.29141 -30.98801 -18.35898 1.000 238.68333 ? 27  THR B OG1 1 
ATOM   202  C CG2 . THR A 1 27  ? 37.55963 -31.99744 -20.54935 1.000 246.51948 ? 27  THR B CG2 1 
ATOM   203  N N   . ASN A 1 28  ? 33.36727 -32.12064 -18.38922 1.000 264.60304 ? 28  ASN B N   1 
ATOM   204  C CA  . ASN A 1 28  ? 32.56459 -32.24083 -17.17195 1.000 266.86191 ? 28  ASN B CA  1 
ATOM   205  C C   . ASN A 1 28  ? 33.29477 -33.20382 -16.25238 1.000 263.56430 ? 28  ASN B C   1 
ATOM   206  O O   . ASN A 1 28  ? 33.11131 -34.41905 -16.32509 1.000 263.21387 ? 28  ASN B O   1 
ATOM   207  C CB  . ASN A 1 28  ? 31.14857 -32.71291 -17.48079 1.000 270.87694 ? 28  ASN B CB  1 
ATOM   208  C CG  . ASN A 1 28  ? 30.22341 -32.58069 -16.28878 1.000 273.88422 ? 28  ASN B CG  1 
ATOM   209  O OD1 . ASN A 1 28  ? 30.53149 -33.03719 -15.18486 1.000 273.60607 ? 28  ASN B OD1 1 
ATOM   210  N ND2 . ASN A 1 28  ? 29.09790 -31.91268 -16.49601 1.000 277.42316 ? 28  ASN B ND2 1 
ATOM   211  N N   . CYS A 1 29  ? 34.14155 -32.65112 -15.37704 1.000 261.59211 ? 29  CYS B N   1 
ATOM   212  C CA  . CYS A 1 29  ? 34.98511 -33.50026 -14.54234 1.000 258.10059 ? 29  CYS B CA  1 
ATOM   213  C C   . CYS A 1 29  ? 34.13601 -34.43800 -13.69953 1.000 260.88816 ? 29  CYS B C   1 
ATOM   214  O O   . CYS A 1 29  ? 34.53471 -35.57460 -13.42360 1.000 259.35325 ? 29  CYS B O   1 
ATOM   215  C CB  . CYS A 1 29  ? 35.89084 -32.64238 -13.65622 1.000 255.04081 ? 29  CYS B CB  1 
ATOM   216  S SG  . CYS A 1 29  ? 36.14234 -30.99845 -14.33697 1.000 254.94227 ? 29  CYS B SG  1 
ATOM   217  N N   . SER A 1 30  ? 32.93639 -33.99328 -13.32263 1.000 246.08675 ? 30  SER B N   1 
ATOM   218  C CA  . SER A 1 30  ? 32.09744 -34.80653 -12.45142 1.000 249.16515 ? 30  SER B CA  1 
ATOM   219  C C   . SER A 1 30  ? 31.59271 -36.04465 -13.17254 1.000 250.74640 ? 30  SER B C   1 
ATOM   220  O O   . SER A 1 30  ? 31.46700 -37.11295 -12.56372 1.000 251.47531 ? 30  SER B O   1 
ATOM   221  C CB  . SER A 1 30  ? 30.92194 -33.98866 -11.91313 1.000 252.19250 ? 30  SER B CB  1 
ATOM   222  O OG  . SER A 1 30  ? 31.36538 -32.94959 -11.06142 1.000 249.30680 ? 30  SER B OG  1 
ATOM   223  N N   . THR A 1 31  ? 31.31395 -35.92512 -14.47145 1.000 257.92280 ? 31  THR B N   1 
ATOM   224  C CA  . THR A 1 31  ? 30.77409 -37.05258 -15.22044 1.000 258.65992 ? 31  THR B CA  1 
ATOM   225  C C   . THR A 1 31  ? 31.79797 -38.16503 -15.40211 1.000 253.47408 ? 31  THR B C   1 
ATOM   226  O O   . THR A 1 31  ? 31.42084 -39.33988 -15.46465 1.000 253.35904 ? 31  THR B O   1 
ATOM   227  C CB  . THR A 1 31  ? 30.26797 -36.58502 -16.58723 1.000 259.82076 ? 31  THR B CB  1 
ATOM   228  O OG1 . THR A 1 31  ? 31.30120 -35.85113 -17.25784 1.000 256.04389 ? 31  THR B OG1 1 
ATOM   229  C CG2 . THR A 1 31  ? 29.03130 -35.70827 -16.43844 1.000 263.55597 ? 31  THR B CG2 1 
ATOM   230  N N   . GLU A 1 32  ? 33.08727 -37.83200 -15.48387 1.000 268.40659 ? 32  GLU B N   1 
ATOM   231  C CA  . GLU A 1 32  ? 34.03377 -38.82762 -15.96955 1.000 262.74749 ? 32  GLU B CA  1 
ATOM   232  C C   . GLU A 1 32  ? 35.35260 -38.83079 -15.20079 1.000 257.90391 ? 32  GLU B C   1 
ATOM   233  O O   . GLU A 1 32  ? 35.80401 -39.89378 -14.76200 1.000 252.89666 ? 32  GLU B O   1 
ATOM   234  C CB  . GLU A 1 32  ? 34.28469 -38.59864 -17.46279 1.000 261.86807 ? 32  GLU B CB  1 
ATOM   235  C CG  . GLU A 1 32  ? 35.59782 -39.12813 -18.03421 1.000 257.43491 ? 32  GLU B CG  1 
ATOM   236  C CD  . GLU A 1 32  ? 35.80133 -40.63205 -17.86228 1.000 254.63374 ? 32  GLU B CD  1 
ATOM   237  O OE1 . GLU A 1 32  ? 34.99205 -41.31802 -17.20203 1.000 259.34654 ? 32  GLU B OE1 1 
ATOM   238  O OE2 . GLU A 1 32  ? 36.77316 -41.14323 -18.44455 1.000 247.49121 ? 32  GLU B OE2 1 
ATOM   239  N N   . LEU A 1 33  ? 35.98353 -37.66497 -15.04573 1.000 258.37478 ? 33  LEU B N   1 
ATOM   240  C CA  . LEU A 1 33  ? 37.25867 -37.58703 -14.33785 1.000 252.77794 ? 33  LEU B CA  1 
ATOM   241  C C   . LEU A 1 33  ? 37.14933 -38.18315 -12.94210 1.000 255.36798 ? 33  LEU B C   1 
ATOM   242  O O   . LEU A 1 33  ? 36.26196 -37.82557 -12.16315 1.000 260.65790 ? 33  LEU B O   1 
ATOM   243  C CB  . LEU A 1 33  ? 37.74463 -36.13837 -14.24288 1.000 251.25549 ? 33  LEU B CB  1 
ATOM   244  C CG  . LEU A 1 33  ? 38.06582 -35.32941 -15.49793 1.000 248.51419 ? 33  LEU B CG  1 
ATOM   245  C CD1 . LEU A 1 33  ? 39.21013 -34.39083 -15.17387 1.000 244.58116 ? 33  LEU B CD1 1 
ATOM   246  C CD2 . LEU A 1 33  ? 38.44152 -36.23468 -16.65850 1.000 242.78314 ? 33  LEU B CD2 1 
ATOM   247  N N   . ARG A 1 34  ? 38.06167 -39.10002 -12.63488 1.000 240.16229 ? 34  ARG B N   1 
ATOM   248  C CA  . ARG A 1 34  ? 38.07909 -39.80998 -11.36368 1.000 242.72639 ? 34  ARG B CA  1 
ATOM   249  C C   . ARG A 1 34  ? 39.42353 -39.56371 -10.70053 1.000 237.52528 ? 34  ARG B C   1 
ATOM   250  O O   . ARG A 1 34  ? 40.46750 -39.92035 -11.25616 1.000 230.29086 ? 34  ARG B O   1 
ATOM   251  C CB  . ARG A 1 34  ? 37.84597 -41.30649 -11.57187 1.000 242.21827 ? 34  ARG B CB  1 
ATOM   252  C CG  . ARG A 1 34  ? 36.46655 -41.63944 -12.09889 1.000 248.83070 ? 34  ARG B CG  1 
ATOM   253  C CD  . ARG A 1 34  ? 36.28237 -43.13523 -12.25944 1.000 254.04490 ? 34  ARG B CD  1 
ATOM   254  N NE  . ARG A 1 34  ? 34.99077 -43.45626 -12.85402 1.000 258.58496 ? 34  ARG B NE  1 
ATOM   255  C CZ  . ARG A 1 34  ? 34.61518 -44.67478 -13.21749 1.000 258.73025 ? 34  ARG B CZ  1 
ATOM   256  N NH1 . ARG A 1 34  ? 35.41145 -45.71931 -13.05974 1.000 254.25476 ? 34  ARG B NH1 1 
ATOM   257  N NH2 . ARG A 1 34  ? 33.41179 -44.84919 -13.75642 1.000 262.46769 ? 34  ARG B NH2 1 
ATOM   258  N N   . LEU A 1 35  ? 39.40089 -38.94473 -9.52809  1.000 226.26273 ? 35  LEU B N   1 
ATOM   259  C CA  . LEU A 1 35  ? 40.61453 -38.69847 -8.76657  1.000 221.06929 ? 35  LEU B CA  1 
ATOM   260  C C   . LEU A 1 35  ? 40.67605 -39.71866 -7.63771  1.000 223.35584 ? 35  LEU B C   1 
ATOM   261  O O   . LEU A 1 35  ? 39.68588 -39.92392 -6.92866  1.000 231.08542 ? 35  LEU B O   1 
ATOM   262  C CB  . LEU A 1 35  ? 40.63750 -37.26852 -8.21841  1.000 221.18659 ? 35  LEU B CB  1 
ATOM   263  C CG  . LEU A 1 35  ? 41.81751 -36.82468 -7.34272  1.000 215.03932 ? 35  LEU B CG  1 
ATOM   264  C CD1 . LEU A 1 35  ? 41.63742 -37.22430 -5.88361  1.000 212.34355 ? 35  LEU B CD1 1 
ATOM   265  C CD2 . LEU A 1 35  ? 43.14805 -37.33351 -7.89063  1.000 210.44403 ? 35  LEU B CD2 1 
ATOM   266  N N   . LEU A 1 36  ? 41.83510 -40.35313 -7.47643  1.000 219.31586 ? 36  LEU B N   1 
ATOM   267  C CA  . LEU A 1 36  ? 42.04939 -41.39102 -6.47170  1.000 220.09328 ? 36  LEU B CA  1 
ATOM   268  C C   . LEU A 1 36  ? 43.22916 -40.97538 -5.60210  1.000 215.52400 ? 36  LEU B C   1 
ATOM   269  O O   . LEU A 1 36  ? 44.36135 -40.88380 -6.08882  1.000 206.68812 ? 36  LEU B O   1 
ATOM   270  C CB  . LEU A 1 36  ? 42.29995 -42.74752 -7.13307  1.000 214.91066 ? 36  LEU B CB  1 
ATOM   271  C CG  . LEU A 1 36  ? 41.08616 -43.60443 -7.51341  1.000 220.36918 ? 36  LEU B CG  1 
ATOM   272  C CD1 . LEU A 1 36  ? 40.24278 -42.95147 -8.60018  1.000 223.59895 ? 36  LEU B CD1 1 
ATOM   273  C CD2 . LEU A 1 36  ? 41.53725 -44.98697 -7.95866  1.000 213.03755 ? 36  LEU B CD2 1 
ATOM   274  N N   . TYR A 1 37  ? 42.97005 -40.72334 -4.32020  1.000 193.80001 ? 37  TYR B N   1 
ATOM   275  C CA  . TYR A 1 37  ? 43.99405 -40.25868 -3.39326  1.000 190.01102 ? 37  TYR B CA  1 
ATOM   276  C C   . TYR A 1 37  ? 44.09962 -41.21617 -2.21443  1.000 192.18969 ? 37  TYR B C   1 
ATOM   277  O O   . TYR A 1 37  ? 43.08954 -41.54747 -1.58456  1.000 200.70984 ? 37  TYR B O   1 
ATOM   278  C CB  . TYR A 1 37  ? 43.69762 -38.82999 -2.91315  1.000 193.49282 ? 37  TYR B CB  1 
ATOM   279  C CG  . TYR A 1 37  ? 42.42527 -38.65498 -2.10750  1.000 204.12726 ? 37  TYR B CG  1 
ATOM   280  C CD1 . TYR A 1 37  ? 41.19070 -38.53880 -2.73327  1.000 208.07824 ? 37  TYR B CD1 1 
ATOM   281  C CD2 . TYR A 1 37  ? 42.46518 -38.56713 -0.72231  1.000 206.91338 ? 37  TYR B CD2 1 
ATOM   282  C CE1 . TYR A 1 37  ? 40.03052 -38.36361 -2.00296  1.000 213.79129 ? 37  TYR B CE1 1 
ATOM   283  C CE2 . TYR A 1 37  ? 41.30996 -38.39163 0.01674   1.000 214.19431 ? 37  TYR B CE2 1 
ATOM   284  C CZ  . TYR A 1 37  ? 40.09629 -38.28808 -0.62871  1.000 216.34510 ? 37  TYR B CZ  1 
ATOM   285  O OH  . TYR A 1 37  ? 38.94596 -38.11551 0.10657   1.000 220.07982 ? 37  TYR B OH  1 
ATOM   286  N N   . GLN A 1 38  ? 45.32136 -41.66961 -1.93267  1.000 194.35184 ? 38  GLN B N   1 
ATOM   287  C CA  . GLN A 1 38  ? 45.59933 -42.52359 -0.78739  1.000 194.90822 ? 38  GLN B CA  1 
ATOM   288  C C   . GLN A 1 38  ? 46.85531 -42.04145 -0.07971  1.000 189.18016 ? 38  GLN B C   1 
ATOM   289  O O   . GLN A 1 38  ? 47.80038 -41.56099 -0.71040  1.000 181.75068 ? 38  GLN B O   1 
ATOM   290  C CB  . GLN A 1 38  ? 45.79228 -43.99309 -1.17810  1.000 190.89371 ? 38  GLN B CB  1 
ATOM   291  C CG  . GLN A 1 38  ? 44.66097 -44.60893 -1.96441  1.000 194.50722 ? 38  GLN B CG  1 
ATOM   292  C CD  . GLN A 1 38  ? 44.76069 -46.11957 -1.99976  1.000 190.85359 ? 38  GLN B CD  1 
ATOM   293  O OE1 . GLN A 1 38  ? 45.19287 -46.74542 -1.03122  1.000 189.72741 ? 38  GLN B OE1 1 
ATOM   294  N NE2 . GLN A 1 38  ? 44.36100 -46.71483 -3.11635  1.000 188.86262 ? 38  GLN B NE2 1 
ATOM   295  N N   . LEU A 1 39  ? 46.86090 -42.20061 1.24007   1.000 192.53386 ? 39  LEU B N   1 
ATOM   296  C CA  . LEU A 1 39  ? 48.00558 -41.85043 2.06395   1.000 186.69562 ? 39  LEU B CA  1 
ATOM   297  C C   . LEU A 1 39  ? 49.05163 -42.96626 1.98038   1.000 179.91789 ? 39  LEU B C   1 
ATOM   298  O O   . LEU A 1 39  ? 48.88840 -43.94653 1.24976   1.000 178.15250 ? 39  LEU B O   1 
ATOM   299  C CB  . LEU A 1 39  ? 47.53290 -41.56689 3.48948   1.000 192.19930 ? 39  LEU B CB  1 
ATOM   300  C CG  . LEU A 1 39  ? 48.37854 -40.67455 4.39494   1.000 187.58009 ? 39  LEU B CG  1 
ATOM   301  C CD1 . LEU A 1 39  ? 48.94009 -39.53363 3.61638   1.000 181.91306 ? 39  LEU B CD1 1 
ATOM   302  C CD2 . LEU A 1 39  ? 47.52592 -40.14315 5.53951   1.000 193.37881 ? 39  LEU B CD2 1 
ATOM   303  N N   . VAL A 1 40  ? 50.15049 -42.82332 2.72145   1.000 188.10174 ? 40  VAL B N   1 
ATOM   304  C CA  . VAL A 1 40  ? 51.27564 -43.74170 2.56370   1.000 180.37585 ? 40  VAL B CA  1 
ATOM   305  C C   . VAL A 1 40  ? 51.50551 -44.56787 3.82278   1.000 180.58830 ? 40  VAL B C   1 
ATOM   306  O O   . VAL A 1 40  ? 52.43917 -44.31293 4.58900   1.000 176.74055 ? 40  VAL B O   1 
ATOM   307  C CB  . VAL A 1 40  ? 52.56059 -42.98093 2.18280   1.000 173.01542 ? 40  VAL B CB  1 
ATOM   308  C CG1 . VAL A 1 40  ? 52.56454 -42.65461 0.69622   1.000 171.10777 ? 40  VAL B CG1 1 
ATOM   309  C CG2 . VAL A 1 40  ? 52.70390 -41.72036 3.02473   1.000 174.38527 ? 40  VAL B CG2 1 
ATOM   310  N N   . PHE A 1 41  ? 50.66760 -45.58213 4.03662   1.000 182.93563 ? 41  PHE B N   1 
ATOM   311  C CA  . PHE A 1 41  ? 50.90012 -46.56337 5.08887   1.000 182.40944 ? 41  PHE B CA  1 
ATOM   312  C C   . PHE A 1 41  ? 50.82893 -47.96460 4.48466   1.000 180.87472 ? 41  PHE B C   1 
ATOM   313  O O   . PHE A 1 41  ? 50.95498 -48.16508 3.27007   1.000 178.26402 ? 41  PHE B O   1 
ATOM   314  C CB  . PHE A 1 41  ? 49.92155 -46.36710 6.25505   1.000 189.27205 ? 41  PHE B CB  1 
ATOM   315  C CG  . PHE A 1 41  ? 50.48676 -45.55495 7.38788   1.000 186.18689 ? 41  PHE B CG  1 
ATOM   316  C CD1 . PHE A 1 41  ? 51.09182 -44.33663 7.14997   1.000 182.26117 ? 41  PHE B CD1 1 
ATOM   317  C CD2 . PHE A 1 41  ? 50.40302 -46.00726 8.69357   1.000 186.98708 ? 41  PHE B CD2 1 
ATOM   318  C CE1 . PHE A 1 41  ? 51.60312 -43.58767 8.18769   1.000 178.66414 ? 41  PHE B CE1 1 
ATOM   319  C CE2 . PHE A 1 41  ? 50.91665 -45.25905 9.73417   1.000 183.22419 ? 41  PHE B CE2 1 
ATOM   320  C CZ  . PHE A 1 41  ? 51.51751 -44.04666 9.48007   1.000 179.35738 ? 41  PHE B CZ  1 
ATOM   321  N N   . LEU A 1 42  ? 50.63326 -48.95971 5.34644   1.000 183.59829 ? 42  LEU B N   1 
ATOM   322  C CA  . LEU A 1 42  ? 50.69640 -50.36421 4.96304   1.000 180.18499 ? 42  LEU B CA  1 
ATOM   323  C C   . LEU A 1 42  ? 49.32962 -50.95227 4.65091   1.000 186.07512 ? 42  LEU B C   1 
ATOM   324  O O   . LEU A 1 42  ? 49.19345 -51.70797 3.68545   1.000 183.17540 ? 42  LEU B O   1 
ATOM   325  C CB  . LEU A 1 42  ? 51.36743 -51.18202 6.07110   1.000 176.67955 ? 42  LEU B CB  1 
ATOM   326  C CG  . LEU A 1 42  ? 52.67807 -50.60179 6.60610   1.000 170.99644 ? 42  LEU B CG  1 
ATOM   327  C CD1 . LEU A 1 42  ? 52.40666 -49.73588 7.82206   1.000 174.94716 ? 42  LEU B CD1 1 
ATOM   328  C CD2 . LEU A 1 42  ? 53.68188 -51.69629 6.93464   1.000 165.63712 ? 42  LEU B CD2 1 
ATOM   329  N N   . LEU A 1 43  ? 48.31272 -50.62922 5.44594   1.000 171.85760 ? 43  LEU B N   1 
ATOM   330  C CA  . LEU A 1 43  ? 46.95457 -51.01881 5.09729   1.000 177.93829 ? 43  LEU B CA  1 
ATOM   331  C C   . LEU A 1 43  ? 46.20159 -49.79156 4.60857   1.000 184.22173 ? 43  LEU B C   1 
ATOM   332  O O   . LEU A 1 43  ? 45.09668 -49.50371 5.07944   1.000 192.22835 ? 43  LEU B O   1 
ATOM   333  C CB  . LEU A 1 43  ? 46.22669 -51.65935 6.28077   1.000 182.65972 ? 43  LEU B CB  1 
ATOM   334  C CG  . LEU A 1 43  ? 46.53363 -53.11183 6.65943   1.000 182.45033 ? 43  LEU B CG  1 
ATOM   335  C CD1 . LEU A 1 43  ? 46.14092 -54.05894 5.53042   1.000 183.99378 ? 43  LEU B CD1 1 
ATOM   336  C CD2 . LEU A 1 43  ? 47.98410 -53.31715 7.07783   1.000 176.85000 ? 43  LEU B CD2 1 
ATOM   337  N N   . SER A 1 44  ? 46.80768 -49.06011 3.67350   1.000 190.85428 ? 44  SER B N   1 
ATOM   338  C CA  . SER A 1 44  ? 46.19982 -47.85010 3.13993   1.000 195.83690 ? 44  SER B CA  1 
ATOM   339  C C   . SER A 1 44  ? 44.82380 -48.15404 2.56386   1.000 202.12743 ? 44  SER B C   1 
ATOM   340  O O   . SER A 1 44  ? 44.54540 -49.26965 2.11540   1.000 200.00914 ? 44  SER B O   1 
ATOM   341  C CB  . SER A 1 44  ? 47.09568 -47.23601 2.06111   1.000 188.88808 ? 44  SER B CB  1 
ATOM   342  O OG  . SER A 1 44  ? 48.05717 -46.36184 2.62620   1.000 186.53392 ? 44  SER B OG  1 
ATOM   343  N N   . GLU A 1 45  ? 43.95471 -47.14891 2.58353   1.000 206.34127 ? 45  GLU B N   1 
ATOM   344  C CA  . GLU A 1 45  ? 42.59378 -47.28957 2.09374   1.000 212.63342 ? 45  GLU B CA  1 
ATOM   345  C C   . GLU A 1 45  ? 42.37851 -46.34178 0.91934   1.000 212.28609 ? 45  GLU B C   1 
ATOM   346  O O   . GLU A 1 45  ? 43.02825 -45.29670 0.81816   1.000 210.09844 ? 45  GLU B O   1 
ATOM   347  C CB  . GLU A 1 45  ? 41.57974 -47.00821 3.20993   1.000 223.18918 ? 45  GLU B CB  1 
ATOM   348  C CG  . GLU A 1 45  ? 40.29612 -47.81443 3.10582   1.000 230.41911 ? 45  GLU B CG  1 
ATOM   349  C CD  . GLU A 1 45  ? 39.26084 -47.15338 2.22630   1.000 237.71805 ? 45  GLU B CD  1 
ATOM   350  O OE1 . GLU A 1 45  ? 38.83824 -46.02327 2.54960   1.000 245.64259 ? 45  GLU B OE1 1 
ATOM   351  O OE2 . GLU A 1 45  ? 38.86429 -47.77119 1.21651   1.000 236.05254 ? 45  GLU B OE2 1 
ATOM   352  N N   . ALA A 1 46  ? 41.46600 -46.71892 0.02668   1.000 214.83974 ? 46  ALA B N   1 
ATOM   353  C CA  . ALA A 1 46  ? 41.22354 -45.99055 -1.21317  1.000 213.59484 ? 46  ALA B CA  1 
ATOM   354  C C   . ALA A 1 46  ? 40.09796 -44.97987 -1.03208  1.000 223.11767 ? 46  ALA B C   1 
ATOM   355  O O   . ALA A 1 46  ? 38.99525 -45.33901 -0.60554  1.000 230.12791 ? 46  ALA B O   1 
ATOM   356  C CB  . ALA A 1 46  ? 40.87643 -46.95429 -2.34886  1.000 208.60681 ? 46  ALA B CB  1 
ATOM   357  N N   . HIS A 1 47  ? 40.37298 -43.72411 -1.37647  1.000 210.91319 ? 47  HIS B N   1 
ATOM   358  C CA  . HIS A 1 47  ? 39.38081 -42.65821 -1.34712  1.000 218.68402 ? 47  HIS B CA  1 
ATOM   359  C C   . HIS A 1 47  ? 39.29241 -42.02523 -2.72744  1.000 214.90397 ? 47  HIS B C   1 
ATOM   360  O O   . HIS A 1 47  ? 40.32095 -41.72233 -3.34206  1.000 206.95385 ? 47  HIS B O   1 
ATOM   361  C CB  . HIS A 1 47  ? 39.73281 -41.59618 -0.30359  1.000 222.22635 ? 47  HIS B CB  1 
ATOM   362  C CG  . HIS A 1 47  ? 40.45829 -42.13410 0.88897   1.000 221.61372 ? 47  HIS B CG  1 
ATOM   363  N ND1 . HIS A 1 47  ? 39.89516 -43.04667 1.75496   1.000 226.83278 ? 47  HIS B ND1 1 
ATOM   364  C CD2 . HIS A 1 47  ? 41.70299 -41.88690 1.36028   1.000 215.42143 ? 47  HIS B CD2 1 
ATOM   365  C CE1 . HIS A 1 47  ? 40.76215 -43.33863 2.70791   1.000 223.48406 ? 47  HIS B CE1 1 
ATOM   366  N NE2 . HIS A 1 47  ? 41.86733 -42.64839 2.49155   1.000 216.86362 ? 47  HIS B NE2 1 
ATOM   367  N N   . THR A 1 48  ? 38.06975 -41.82480 -3.21005  1.000 224.33989 ? 48  THR B N   1 
ATOM   368  C CA  . THR A 1 48  ? 37.82713 -41.24417 -4.52393  1.000 221.18713 ? 48  THR B CA  1 
ATOM   369  C C   . THR A 1 48  ? 37.14215 -39.89265 -4.37325  1.000 222.96638 ? 48  THR B C   1 
ATOM   370  O O   . THR A 1 48  ? 36.10483 -39.78626 -3.71066  1.000 227.29615 ? 48  THR B O   1 
ATOM   371  C CB  . THR A 1 48  ? 36.97269 -42.17313 -5.38988  1.000 221.88250 ? 48  THR B CB  1 
ATOM   372  O OG1 . THR A 1 48  ? 37.65334 -43.42093 -5.56964  1.000 216.52610 ? 48  THR B OG1 1 
ATOM   373  C CG2 . THR A 1 48  ? 36.71475 -41.54392 -6.75230  1.000 218.64691 ? 48  THR B CG2 1 
ATOM   374  N N   . CYS A 1 49  ? 37.72684 -38.86852 -4.98673  1.000 233.17462 ? 49  CYS B N   1 
ATOM   375  C CA  . CYS A 1 49  ? 37.17958 -37.51806 -4.99081  1.000 232.21184 ? 49  CYS B CA  1 
ATOM   376  C C   . CYS A 1 49  ? 36.38458 -37.27980 -6.26485  1.000 232.95114 ? 49  CYS B C   1 
ATOM   377  O O   . CYS A 1 49  ? 36.86918 -37.55584 -7.36709  1.000 230.36206 ? 49  CYS B O   1 
ATOM   378  C CB  . CYS A 1 49  ? 38.29958 -36.48700 -4.87136  1.000 226.55942 ? 49  CYS B CB  1 
ATOM   379  S SG  . CYS A 1 49  ? 37.94707 -34.79922 -5.45892  1.000 223.72251 ? 49  CYS B SG  1 
ATOM   380  N N   . ILE A 1 50  ? 35.16753 -36.77094 -6.10335  1.000 233.09026 ? 50  ILE B N   1 
ATOM   381  C CA  . ILE A 1 50  ? 34.31766 -36.39773 -7.23544  1.000 234.59247 ? 50  ILE B CA  1 
ATOM   382  C C   . ILE A 1 50  ? 34.66487 -34.96835 -7.61265  1.000 230.76298 ? 50  ILE B C   1 
ATOM   383  O O   . ILE A 1 50  ? 34.40833 -34.04209 -6.81990  1.000 230.02286 ? 50  ILE B O   1 
ATOM   384  C CB  . ILE A 1 50  ? 32.82918 -36.55198 -6.88605  1.000 239.52134 ? 50  ILE B CB  1 
ATOM   385  C CG1 . ILE A 1 50  ? 31.95021 -35.86341 -7.93216  1.000 240.66313 ? 50  ILE B CG1 1 
ATOM   386  C CG2 . ILE A 1 50  ? 32.53647 -36.04738 -5.47473  1.000 240.61378 ? 50  ILE B CG2 1 
ATOM   387  C CD1 . ILE A 1 50  ? 32.06352 -36.47465 -9.30950  1.000 242.41544 ? 50  ILE B CD1 1 
ATOM   388  N N   . PRO A 1 51  ? 35.26412 -34.72591 -8.77385  1.000 246.36557 ? 51  PRO B N   1 
ATOM   389  C CA  . PRO A 1 51  ? 35.71494 -33.38132 -9.13246  1.000 243.58174 ? 51  PRO B CA  1 
ATOM   390  C C   . PRO A 1 51  ? 34.57652 -32.54301 -9.70910  1.000 247.10726 ? 51  PRO B C   1 
ATOM   391  O O   . PRO A 1 51  ? 33.45840 -33.01307 -9.90914  1.000 250.76104 ? 51  PRO B O   1 
ATOM   392  C CB  . PRO A 1 51  ? 36.80462 -33.65537 -10.16923 1.000 239.58005 ? 51  PRO B CB  1 
ATOM   393  C CG  . PRO A 1 51  ? 36.34880 -34.90430 -10.84071 1.000 241.60001 ? 51  PRO B CG  1 
ATOM   394  C CD  . PRO A 1 51  ? 35.66220 -35.72998 -9.77860  1.000 245.23006 ? 51  PRO B CD  1 
ATOM   395  N N   . GLU A 1 52  ? 34.88581 -31.27296 -9.96905  1.000 245.79396 ? 52  GLU B N   1 
ATOM   396  C CA  . GLU A 1 52  ? 33.92239 -30.31994 -10.50106 1.000 249.54201 ? 52  GLU B CA  1 
ATOM   397  C C   . GLU A 1 52  ? 34.61995 -29.42974 -11.51964 1.000 247.86508 ? 52  GLU B C   1 
ATOM   398  O O   . GLU A 1 52  ? 35.84313 -29.45917 -11.66841 1.000 243.73553 ? 52  GLU B O   1 
ATOM   399  C CB  . GLU A 1 52  ? 33.29339 -29.47640 -9.38710  1.000 250.74084 ? 52  GLU B CB  1 
ATOM   400  C CG  . GLU A 1 52  ? 34.30971 -28.69769 -8.57359  1.000 246.80600 ? 52  GLU B CG  1 
ATOM   401  C CD  . GLU A 1 52  ? 34.46865 -29.24610 -7.17131  1.000 245.77430 ? 52  GLU B CD  1 
ATOM   402  O OE1 . GLU A 1 52  ? 34.80551 -30.44155 -7.03376  1.000 246.10560 ? 52  GLU B OE1 1 
ATOM   403  O OE2 . GLU A 1 52  ? 34.25894 -28.48117 -6.20669  1.000 245.41789 ? 52  GLU B OE2 1 
ATOM   404  N N   . ASN A 1 53  ? 33.82755 -28.62026 -12.21583 1.000 259.81903 ? 53  ASN B N   1 
ATOM   405  C CA  . ASN A 1 53  ? 34.30349 -27.81698 -13.34119 1.000 259.88813 ? 53  ASN B CA  1 
ATOM   406  C C   . ASN A 1 53  ? 34.50911 -26.38364 -12.85604 1.000 259.32059 ? 53  ASN B C   1 
ATOM   407  O O   . ASN A 1 53  ? 33.54457 -25.63488 -12.68684 1.000 262.71454 ? 53  ASN B O   1 
ATOM   408  C CB  . ASN A 1 53  ? 33.29898 -27.87938 -14.48948 1.000 264.57112 ? 53  ASN B CB  1 
ATOM   409  C CG  . ASN A 1 53  ? 33.96165 -27.94379 -15.85384 1.000 263.75857 ? 53  ASN B CG  1 
ATOM   410  O OD1 . ASN A 1 53  ? 35.18361 -27.93122 -15.96526 1.000 259.70678 ? 53  ASN B OD1 1 
ATOM   411  N ND2 . ASN A 1 53  ? 33.14830 -28.01476 -16.90315 1.000 266.71781 ? 53  ASN B ND2 1 
ATOM   412  N N   . ASN A 1 54  ? 35.76831 -25.99634 -12.62816 1.000 252.28785 ? 54  ASN B N   1 
ATOM   413  C CA  . ASN A 1 54  ? 36.03785 -24.61819 -12.22328 1.000 251.94471 ? 54  ASN B CA  1 
ATOM   414  C C   . ASN A 1 54  ? 35.90798 -23.65153 -13.39355 1.000 254.56216 ? 54  ASN B C   1 
ATOM   415  O O   . ASN A 1 54  ? 35.33798 -22.56471 -13.24638 1.000 257.98256 ? 54  ASN B O   1 
ATOM   416  C CB  . ASN A 1 54  ? 37.42288 -24.50623 -11.57642 1.000 247.12917 ? 54  ASN B CB  1 
ATOM   417  C CG  . ASN A 1 54  ? 38.56895 -24.77808 -12.54811 1.000 245.62592 ? 54  ASN B CG  1 
ATOM   418  O OD1 . ASN A 1 54  ? 38.65731 -24.18498 -13.62268 1.000 247.92429 ? 54  ASN B OD1 1 
ATOM   419  N ND2 . ASN A 1 54  ? 39.47004 -25.66621 -12.15110 1.000 241.84514 ? 54  ASN B ND2 1 
ATOM   420  N N   . GLY A 1 55  ? 36.44865 -24.02224 -14.55225 1.000 259.79581 ? 55  GLY B N   1 
ATOM   421  C CA  . GLY A 1 55  ? 36.29203 -23.24758 -15.76377 1.000 262.16091 ? 55  GLY B CA  1 
ATOM   422  C C   . GLY A 1 55  ? 35.90717 -24.16502 -16.90532 1.000 264.31463 ? 55  GLY B C   1 
ATOM   423  O O   . GLY A 1 55  ? 35.69987 -25.36332 -16.71024 1.000 264.22539 ? 55  GLY B O   1 
ATOM   424  N N   . GLY A 1 56  ? 35.81575 -23.58317 -18.09918 1.000 274.07836 ? 56  GLY B N   1 
ATOM   425  C CA  . GLY A 1 56  ? 35.47831 -24.34829 -19.28465 1.000 275.26877 ? 56  GLY B CA  1 
ATOM   426  C C   . GLY A 1 56  ? 36.27601 -25.62875 -19.43053 1.000 271.17643 ? 56  GLY B C   1 
ATOM   427  O O   . GLY A 1 56  ? 35.70522 -26.70533 -19.62360 1.000 271.90438 ? 56  GLY B O   1 
ATOM   428  N N   . ALA A 1 57  ? 37.59758 -25.52870 -19.29746 1.000 270.48313 ? 57  ALA B N   1 
ATOM   429  C CA  . ALA A 1 57  ? 38.49105 -26.65909 -19.50162 1.000 265.77111 ? 57  ALA B CA  1 
ATOM   430  C C   . ALA A 1 57  ? 39.20415 -27.11349 -18.23313 1.000 261.22593 ? 57  ALA B C   1 
ATOM   431  O O   . ALA A 1 57  ? 39.91004 -28.12655 -18.27240 1.000 256.76592 ? 57  ALA B O   1 
ATOM   432  C CB  . ALA A 1 57  ? 39.52648 -26.31716 -20.57983 1.000 262.54555 ? 57  ALA B CB  1 
ATOM   433  N N   . GLY A 1 58  ? 39.04228 -26.40313 -17.11540 1.000 254.46186 ? 58  GLY B N   1 
ATOM   434  C CA  . GLY A 1 58  ? 39.72151 -26.74747 -15.87855 1.000 249.77374 ? 58  GLY B CA  1 
ATOM   435  C C   . GLY A 1 58  ? 38.83438 -27.44838 -14.86998 1.000 251.68526 ? 58  GLY B C   1 
ATOM   436  O O   . GLY A 1 58  ? 37.60625 -27.40874 -14.97907 1.000 255.85148 ? 58  GLY B O   1 
ATOM   437  N N   . CYS A 1 59  ? 39.44396 -28.08558 -13.87258 1.000 250.63053 ? 59  CYS B N   1 
ATOM   438  C CA  . CYS A 1 59  ? 38.71919 -28.90892 -12.91517 1.000 252.24942 ? 59  CYS B CA  1 
ATOM   439  C C   . CYS A 1 59  ? 39.19807 -28.61608 -11.49656 1.000 249.47288 ? 59  CYS B C   1 
ATOM   440  O O   . CYS A 1 59  ? 40.24209 -27.99402 -11.28613 1.000 245.52674 ? 59  CYS B O   1 
ATOM   441  C CB  . CYS A 1 59  ? 38.88622 -30.39772 -13.24481 1.000 252.05085 ? 59  CYS B CB  1 
ATOM   442  S SG  . CYS A 1 59  ? 38.11557 -30.91203 -14.79404 1.000 255.09748 ? 59  CYS B SG  1 
ATOM   443  N N   . VAL A 1 60  ? 38.40917 -29.06803 -10.51609 1.000 240.68931 ? 60  VAL B N   1 
ATOM   444  C CA  . VAL A 1 60  ? 38.66877 -28.83322 -9.09706  1.000 238.15632 ? 60  VAL B CA  1 
ATOM   445  C C   . VAL A 1 60  ? 38.26553 -30.06718 -8.29393  1.000 239.73341 ? 60  VAL B C   1 
ATOM   446  O O   . VAL A 1 60  ? 37.29780 -30.75760 -8.62285  1.000 243.41804 ? 60  VAL B O   1 
ATOM   447  C CB  . VAL A 1 60  ? 37.93506 -27.56361 -8.58403  1.000 239.83577 ? 60  VAL B CB  1 
ATOM   448  C CG1 . VAL A 1 60  ? 37.79153 -27.56624 -7.06915  1.000 238.89847 ? 60  VAL B CG1 1 
ATOM   449  C CG2 . VAL A 1 60  ? 38.70227 -26.32820 -8.97639  1.000 237.04189 ? 60  VAL B CG2 1 
ATOM   450  N N   . CYS A 1 61  ? 39.02503 -30.34198 -7.23247  1.000 236.27820 ? 61  CYS B N   1 
ATOM   451  C CA  . CYS A 1 61  ? 38.82835 -31.49455 -6.36046  1.000 238.15793 ? 61  CYS B CA  1 
ATOM   452  C C   . CYS A 1 61  ? 38.96951 -31.06567 -4.90507  1.000 236.14196 ? 61  CYS B C   1 
ATOM   453  O O   . CYS A 1 61  ? 39.52972 -30.00960 -4.60061  1.000 232.36420 ? 61  CYS B O   1 
ATOM   454  C CB  . CYS A 1 61  ? 39.83129 -32.60383 -6.70617  1.000 236.55585 ? 61  CYS B CB  1 
ATOM   455  S SG  . CYS A 1 61  ? 39.84127 -34.12757 -5.72393  1.000 240.21644 ? 61  CYS B SG  1 
ATOM   456  N N   . HIS A 1 62  ? 38.44480 -31.89882 -4.00047  1.000 218.05089 ? 62  HIS B N   1 
ATOM   457  C CA  . HIS A 1 62  ? 38.52387 -31.64544 -2.55733  1.000 216.39042 ? 62  HIS B CA  1 
ATOM   458  C C   . HIS A 1 62  ? 38.77944 -32.96892 -1.84040  1.000 219.17801 ? 62  HIS B C   1 
ATOM   459  O O   . HIS A 1 62  ? 37.84849 -33.74468 -1.60513  1.000 224.26328 ? 62  HIS B O   1 
ATOM   460  C CB  . HIS A 1 62  ? 37.25615 -30.98081 -2.03341  1.000 217.98364 ? 62  HIS B CB  1 
ATOM   461  C CG  . HIS A 1 62  ? 36.77827 -29.84189 -2.87660  1.000 218.04643 ? 62  HIS B CG  1 
ATOM   462  N ND1 . HIS A 1 62  ? 37.09156 -28.52942 -2.60165  1.000 215.67895 ? 62  HIS B ND1 1 
ATOM   463  C CD2 . HIS A 1 62  ? 36.01088 -29.82140 -3.99205  1.000 221.19369 ? 62  HIS B CD2 1 
ATOM   464  C CE1 . HIS A 1 62  ? 36.53771 -27.74705 -3.51130  1.000 217.40339 ? 62  HIS B CE1 1 
ATOM   465  N NE2 . HIS A 1 62  ? 35.87666 -28.50626 -4.36581  1.000 221.38048 ? 62  HIS B NE2 1 
ATOM   466  N N   . LEU A 1 63  ? 40.03762 -33.21349 -1.48738  1.000 212.58922 ? 63  LEU B N   1 
ATOM   467  C CA  . LEU A 1 63  ? 40.39361 -34.38027 -0.69420  1.000 215.65677 ? 63  LEU B CA  1 
ATOM   468  C C   . LEU A 1 63  ? 40.00980 -34.16735 0.76541   1.000 215.98978 ? 63  LEU B C   1 
ATOM   469  O O   . LEU A 1 63  ? 39.99246 -33.03992 1.26712   1.000 211.36962 ? 63  LEU B O   1 
ATOM   470  C CB  . LEU A 1 63  ? 41.89188 -34.67172 -0.80097  1.000 212.34395 ? 63  LEU B CB  1 
ATOM   471  C CG  . LEU A 1 63  ? 42.59870 -34.33173 -2.11483  1.000 208.53925 ? 63  LEU B CG  1 
ATOM   472  C CD1 . LEU A 1 63  ? 44.07734 -34.68487 -2.07821  1.000 203.77208 ? 63  LEU B CD1 1 
ATOM   473  C CD2 . LEU A 1 63  ? 41.93700 -35.08352 -3.22545  1.000 211.96471 ? 63  LEU B CD2 1 
ATOM   474  N N   . LEU A 1 64  ? 39.70838 -35.26863 1.45073   1.000 214.66461 ? 64  LEU B N   1 
ATOM   475  C CA  . LEU A 1 64  ? 39.23962 -35.23717 2.83623   1.000 215.72900 ? 64  LEU B CA  1 
ATOM   476  C C   . LEU A 1 64  ? 40.24666 -35.97704 3.71494   1.000 217.06329 ? 64  LEU B C   1 
ATOM   477  O O   . LEU A 1 64  ? 40.29899 -37.21131 3.70694   1.000 224.16797 ? 64  LEU B O   1 
ATOM   478  C CB  . LEU A 1 64  ? 37.84333 -35.84559 2.94959   1.000 221.98372 ? 64  LEU B CB  1 
ATOM   479  C CG  . LEU A 1 64  ? 36.69421 -35.09572 2.26473   1.000 221.10326 ? 64  LEU B CG  1 
ATOM   480  C CD1 . LEU A 1 64  ? 35.37054 -35.41237 2.94326   1.000 224.51080 ? 64  LEU B CD1 1 
ATOM   481  C CD2 . LEU A 1 64  ? 36.93701 -33.59115 2.24446   1.000 214.33136 ? 64  LEU B CD2 1 
ATOM   482  N N   . MET A 1 65  ? 41.03842 -35.21955 4.47838   1.000 224.31352 ? 65  MET B N   1 
ATOM   483  C CA  . MET A 1 65  ? 42.07237 -35.76907 5.35701   1.000 223.82717 ? 65  MET B CA  1 
ATOM   484  C C   . MET A 1 65  ? 41.54403 -35.73581 6.78734   1.000 224.48054 ? 65  MET B C   1 
ATOM   485  O O   . MET A 1 65  ? 41.51526 -34.67798 7.41863   1.000 218.43986 ? 65  MET B O   1 
ATOM   486  C CB  . MET A 1 65  ? 43.36662 -34.96970 5.24746   1.000 215.80715 ? 65  MET B CB  1 
ATOM   487  C CG  . MET A 1 65  ? 43.70281 -34.46891 3.85642   1.000 212.66962 ? 65  MET B CG  1 
ATOM   488  S SD  . MET A 1 65  ? 43.51457 -35.71002 2.57132   1.000 219.68208 ? 65  MET B SD  1 
ATOM   489  C CE  . MET A 1 65  ? 44.65886 -35.07137 1.35595   1.000 211.46732 ? 65  MET B CE  1 
ATOM   490  N N   . ASP A 1 66  ? 41.15176 -36.90064 7.31048   1.000 220.79648 ? 66  ASP B N   1 
ATOM   491  C CA  . ASP A 1 66  ? 40.53781 -36.94963 8.63669   1.000 221.22320 ? 66  ASP B CA  1 
ATOM   492  C C   . ASP A 1 66  ? 41.46441 -36.37509 9.70608   1.000 212.10913 ? 66  ASP B C   1 
ATOM   493  O O   . ASP A 1 66  ? 41.05135 -35.53875 10.51816  1.000 206.19763 ? 66  ASP B O   1 
ATOM   494  C CB  . ASP A 1 66  ? 40.09138 -38.38846 8.94991   1.000 233.19567 ? 66  ASP B CB  1 
ATOM   495  C CG  . ASP A 1 66  ? 41.24759 -39.34304 9.27012   1.000 236.68304 ? 66  ASP B CG  1 
ATOM   496  O OD1 . ASP A 1 66  ? 42.11846 -39.03231 10.10943  1.000 229.95016 ? 66  ASP B OD1 1 
ATOM   497  O OD2 . ASP A 1 66  ? 41.27753 -40.43356 8.66032   1.000 244.42321 ? 66  ASP B OD2 1 
ATOM   498  N N   . ASP A 1 67  ? 42.72477 -36.79865 9.71023   1.000 223.94238 ? 67  ASP B N   1 
ATOM   499  C CA  . ASP A 1 67  ? 43.73129 -36.23033 10.59552  1.000 214.90489 ? 67  ASP B CA  1 
ATOM   500  C C   . ASP A 1 67  ? 45.07733 -36.35464 9.90564   1.000 212.24468 ? 67  ASP B C   1 
ATOM   501  O O   . ASP A 1 67  ? 45.46325 -37.45101 9.49129   1.000 216.96818 ? 67  ASP B O   1 
ATOM   502  C CB  . ASP A 1 67  ? 43.75694 -36.93275 11.95553  1.000 214.58552 ? 67  ASP B CB  1 
ATOM   503  C CG  . ASP A 1 67  ? 44.44857 -36.10607 13.01812  1.000 205.37719 ? 67  ASP B CG  1 
ATOM   504  O OD1 . ASP A 1 67  ? 44.76369 -34.92904 12.73896  1.000 200.71180 ? 67  ASP B OD1 1 
ATOM   505  O OD2 . ASP A 1 67  ? 44.68056 -36.63154 14.12709  1.000 202.74599 ? 67  ASP B OD2 1 
ATOM   506  N N   . VAL A 1 68  ? 45.78109 -35.23569 9.78224   1.000 197.08048 ? 68  VAL B N   1 
ATOM   507  C CA  . VAL A 1 68  ? 46.99213 -35.15708 8.97974   1.000 193.71909 ? 68  VAL B CA  1 
ATOM   508  C C   . VAL A 1 68  ? 48.11328 -34.54808 9.81053   1.000 187.51863 ? 68  VAL B C   1 
ATOM   509  O O   . VAL A 1 68  ? 47.89407 -33.60073 10.57366  1.000 184.60953 ? 68  VAL B O   1 
ATOM   510  C CB  . VAL A 1 68  ? 46.74040 -34.35520 7.68441   1.000 192.77080 ? 68  VAL B CB  1 
ATOM   511  C CG1 . VAL A 1 68  ? 46.21950 -32.97236 8.00804   1.000 190.14971 ? 68  VAL B CG1 1 
ATOM   512  C CG2 . VAL A 1 68  ? 48.00572 -34.26772 6.85048   1.000 188.09200 ? 68  VAL B CG2 1 
ATOM   513  N N   . VAL A 1 69  ? 49.31391 -35.11216 9.67465   1.000 198.21703 ? 69  VAL B N   1 
ATOM   514  C CA  . VAL A 1 69  ? 50.48717 -34.64707 10.40620  1.000 192.73542 ? 69  VAL B CA  1 
ATOM   515  C C   . VAL A 1 69  ? 51.57904 -34.24965 9.42261   1.000 187.48614 ? 69  VAL B C   1 
ATOM   516  O O   . VAL A 1 69  ? 51.35854 -34.22288 8.20656   1.000 188.36537 ? 69  VAL B O   1 
ATOM   517  C CB  . VAL A 1 69  ? 50.99900 -35.71871 11.38542  1.000 188.28407 ? 69  VAL B CB  1 
ATOM   518  C CG1 . VAL A 1 69  ? 49.92813 -36.05709 12.41066  1.000 190.81938 ? 69  VAL B CG1 1 
ATOM   519  C CG2 . VAL A 1 69  ? 51.43226 -36.96285 10.62652  1.000 188.14894 ? 69  VAL B CG2 1 
ATOM   520  N N   . SER A 1 70  ? 52.77048 -33.95355 9.94498   1.000 197.60511 ? 70  SER B N   1 
ATOM   521  C CA  . SER A 1 70  ? 53.85859 -33.43959 9.12199   1.000 192.33383 ? 70  SER B CA  1 
ATOM   522  C C   . SER A 1 70  ? 54.48469 -34.49149 8.21747   1.000 189.40041 ? 70  SER B C   1 
ATOM   523  O O   . SER A 1 70  ? 55.28949 -34.13172 7.35126   1.000 185.35407 ? 70  SER B O   1 
ATOM   524  C CB  . SER A 1 70  ? 54.94597 -32.83378 10.00976  1.000 185.47740 ? 70  SER B CB  1 
ATOM   525  O OG  . SER A 1 70  ? 56.06052 -32.42653 9.23475   1.000 181.87976 ? 70  SER B OG  1 
ATOM   526  N N   . ALA A 1 71  ? 54.15165 -35.76553 8.39161   1.000 187.90199 ? 71  ALA B N   1 
ATOM   527  C CA  . ALA A 1 71  ? 54.77382 -36.84140 7.63332   1.000 184.76919 ? 71  ALA B CA  1 
ATOM   528  C C   . ALA A 1 71  ? 53.73876 -37.61822 6.83065   1.000 190.76683 ? 71  ALA B C   1 
ATOM   529  O O   . ALA A 1 71  ? 53.81314 -38.84341 6.70269   1.000 190.39303 ? 71  ALA B O   1 
ATOM   530  C CB  . ALA A 1 71  ? 55.55479 -37.77237 8.55474   1.000 179.13210 ? 71  ALA B CB  1 
ATOM   531  N N   . ASP A 1 72  ? 52.76382 -36.90667 6.27113   1.000 176.98009 ? 72  ASP B N   1 
ATOM   532  C CA  . ASP A 1 72  ? 51.74293 -37.49908 5.42221   1.000 182.37662 ? 72  ASP B CA  1 
ATOM   533  C C   . ASP A 1 72  ? 52.00133 -37.13972 3.96289   1.000 180.03299 ? 72  ASP B C   1 
ATOM   534  O O   . ASP A 1 72  ? 52.49688 -36.05466 3.64711   1.000 176.72412 ? 72  ASP B O   1 
ATOM   535  C CB  . ASP A 1 72  ? 50.34205 -37.05536 5.85391   1.000 188.99478 ? 72  ASP B CB  1 
ATOM   536  C CG  . ASP A 1 72  ? 49.89649 -37.72487 7.14232   1.000 192.69932 ? 72  ASP B CG  1 
ATOM   537  O OD1 . ASP A 1 72  ? 50.55985 -38.69064 7.57308   1.000 189.77140 ? 72  ASP B OD1 1 
ATOM   538  O OD2 . ASP A 1 72  ? 48.87306 -37.30243 7.71461   1.000 197.42738 ? 72  ASP B OD2 1 
ATOM   539  N N   . ASN A 1 73  ? 51.64497 -38.06806 3.07840   1.000 192.98205 ? 73  ASN B N   1 
ATOM   540  C CA  . ASN A 1 73  ? 52.06873 -38.05743 1.68151   1.000 189.62085 ? 73  ASN B CA  1 
ATOM   541  C C   . ASN A 1 73  ? 51.03517 -38.83968 0.88753   1.000 193.72342 ? 73  ASN B C   1 
ATOM   542  O O   . ASN A 1 73  ? 50.83922 -40.03021 1.14291   1.000 195.79775 ? 73  ASN B O   1 
ATOM   543  C CB  . ASN A 1 73  ? 53.45166 -38.69702 1.56494   1.000 183.39613 ? 73  ASN B CB  1 
ATOM   544  C CG  . ASN A 1 73  ? 54.03174 -38.66758 0.16351   1.000 179.23189 ? 73  ASN B CG  1 
ATOM   545  O OD1 . ASN A 1 73  ? 53.36433 -38.37265 -0.82923  1.000 181.63946 ? 73  ASN B OD1 1 
ATOM   546  N ND2 . ASN A 1 73  ? 55.31216 -39.01672 0.09842   1.000 173.02181 ? 73  ASN B ND2 1 
ATOM   547  N N   . TYR A 1 74  ? 50.37516 -38.18776 -0.06374  1.000 176.08022 ? 74  TYR B N   1 
ATOM   548  C CA  . TYR A 1 74  ? 49.24988 -38.78522 -0.76842  1.000 180.46719 ? 74  TYR B CA  1 
ATOM   549  C C   . TYR A 1 74  ? 49.61418 -39.10780 -2.21159  1.000 175.05640 ? 74  TYR B C   1 
ATOM   550  O O   . TYR A 1 74  ? 50.37361 -38.37435 -2.84970  1.000 168.85408 ? 74  TYR B O   1 
ATOM   551  C CB  . TYR A 1 74  ? 48.03346 -37.85803 -0.73437  1.000 187.08242 ? 74  TYR B CB  1 
ATOM   552  C CG  . TYR A 1 74  ? 47.37465 -37.78596 0.62225   1.000 193.47263 ? 74  TYR B CG  1 
ATOM   553  C CD1 . TYR A 1 74  ? 47.78896 -36.85724 1.56599   1.000 191.27532 ? 74  TYR B CD1 1 
ATOM   554  C CD2 . TYR A 1 74  ? 46.34340 -38.65142 0.96271   1.000 200.49991 ? 74  TYR B CD2 1 
ATOM   555  C CE1 . TYR A 1 74  ? 47.19255 -36.78864 2.81086   1.000 196.27987 ? 74  TYR B CE1 1 
ATOM   556  C CE2 . TYR A 1 74  ? 45.74022 -38.59014 2.20533   1.000 207.26815 ? 74  TYR B CE2 1 
ATOM   557  C CZ  . TYR A 1 74  ? 46.16963 -37.65691 3.12536   1.000 204.93885 ? 74  TYR B CZ  1 
ATOM   558  O OH  . TYR A 1 74  ? 45.57560 -37.58833 4.36434   1.000 208.59648 ? 74  TYR B OH  1 
ATOM   559  N N   . THR A 1 75  ? 49.06534 -40.21259 -2.71885  1.000 196.01465 ? 75  THR B N   1 
ATOM   560  C CA  . THR A 1 75  ? 49.20378 -40.60241 -4.11913  1.000 191.38575 ? 75  THR B CA  1 
ATOM   561  C C   . THR A 1 75  ? 47.95570 -40.13950 -4.86127  1.000 196.46432 ? 75  THR B C   1 
ATOM   562  O O   . THR A 1 75  ? 46.86404 -40.67413 -4.64448  1.000 204.03159 ? 75  THR B O   1 
ATOM   563  C CB  . THR A 1 75  ? 49.38968 -42.11276 -4.25905  1.000 188.78093 ? 75  THR B CB  1 
ATOM   564  O OG1 . THR A 1 75  ? 50.65738 -42.49630 -3.71363  1.000 184.46926 ? 75  THR B OG1 1 
ATOM   565  C CG2 . THR A 1 75  ? 49.32595 -42.52902 -5.72538  1.000 184.79304 ? 75  THR B CG2 1 
ATOM   566  N N   . LEU A 1 76  ? 48.11574 -39.14969 -5.73484  1.000 190.81805 ? 76  LEU B N   1 
ATOM   567  C CA  . LEU A 1 76  ? 47.00037 -38.56278 -6.46982  1.000 195.64002 ? 76  LEU B CA  1 
ATOM   568  C C   . LEU A 1 76  ? 46.97229 -39.15660 -7.87407  1.000 195.61636 ? 76  LEU B C   1 
ATOM   569  O O   . LEU A 1 76  ? 47.88437 -38.92349 -8.67419  1.000 191.19563 ? 76  LEU B O   1 
ATOM   570  C CB  . LEU A 1 76  ? 47.12000 -37.04145 -6.51294  1.000 194.54318 ? 76  LEU B CB  1 
ATOM   571  C CG  . LEU A 1 76  ? 46.42128 -36.24194 -5.40927  1.000 201.34596 ? 76  LEU B CG  1 
ATOM   572  C CD1 . LEU A 1 76  ? 46.59826 -36.88829 -4.04154  1.000 203.82762 ? 76  LEU B CD1 1 
ATOM   573  C CD2 . LEU A 1 76  ? 46.93544 -34.81323 -5.39546  1.000 197.66249 ? 76  LEU B CD2 1 
ATOM   574  N N   . ASP A 1 77  ? 45.92298 -39.92076 -8.16998  1.000 222.99892 ? 77  ASP B N   1 
ATOM   575  C CA  . ASP A 1 77  ? 45.76497 -40.60256 -9.45107  1.000 219.15238 ? 77  ASP B CA  1 
ATOM   576  C C   . ASP A 1 77  ? 44.49283 -40.09258 -10.11667 1.000 225.88515 ? 77  ASP B C   1 
ATOM   577  O O   . ASP A 1 77  ? 43.38526 -40.39593 -9.65963  1.000 233.56389 ? 77  ASP B O   1 
ATOM   578  C CB  . ASP A 1 77  ? 45.70934 -42.12012 -9.26145  1.000 218.91962 ? 77  ASP B CB  1 
ATOM   579  C CG  . ASP A 1 77  ? 46.97761 -42.68287 -8.64355  1.000 213.32596 ? 77  ASP B CG  1 
ATOM   580  O OD1 . ASP A 1 77  ? 48.07518 -42.20386 -8.99520  1.000 205.76546 ? 77  ASP B OD1 1 
ATOM   581  O OD2 . ASP A 1 77  ? 46.87661 -43.61363 -7.81465  1.000 216.17476 ? 77  ASP B OD2 1 
ATOM   582  N N   . LEU A 1 78  ? 44.64661 -39.32196 -11.19147 1.000 228.35953 ? 78  LEU B N   1 
ATOM   583  C CA  . LEU A 1 78  ? 43.50739 -38.83283 -11.95851 1.000 234.11603 ? 78  LEU B CA  1 
ATOM   584  C C   . LEU A 1 78  ? 43.20327 -39.81507 -13.08396 1.000 232.03568 ? 78  LEU B C   1 
ATOM   585  O O   . LEU A 1 78  ? 44.02915 -40.01524 -13.98188 1.000 223.79993 ? 78  LEU B O   1 
ATOM   586  C CB  . LEU A 1 78  ? 43.77610 -37.43825 -12.52246 1.000 232.17446 ? 78  LEU B CB  1 
ATOM   587  C CG  . LEU A 1 78  ? 42.59154 -36.84459 -13.29084 1.000 239.28988 ? 78  LEU B CG  1 
ATOM   588  C CD1 . LEU A 1 78  ? 41.34969 -36.78185 -12.40709 1.000 248.13527 ? 78  LEU B CD1 1 
ATOM   589  C CD2 . LEU A 1 78  ? 42.93099 -35.47192 -13.84523 1.000 236.92167 ? 78  LEU B CD2 1 
ATOM   590  N N   . TRP A 1 79  ? 42.02202 -40.42005 -13.03660 1.000 250.07491 ? 79  TRP B N   1 
ATOM   591  C CA  . TRP A 1 79  ? 41.59365 -41.38768 -14.03403 1.000 248.11159 ? 79  TRP B CA  1 
ATOM   592  C C   . TRP A 1 79  ? 40.71638 -40.75610 -15.10562 1.000 252.23405 ? 79  TRP B C   1 
ATOM   593  O O   . TRP A 1 79  ? 40.10482 -39.70168 -14.91605 1.000 258.18946 ? 79  TRP B O   1 
ATOM   594  C CB  . TRP A 1 79  ? 40.83294 -42.54621 -13.38467 1.000 251.67726 ? 79  TRP B CB  1 
ATOM   595  C CG  . TRP A 1 79  ? 41.70481 -43.52871 -12.68188 1.000 246.92200 ? 79  TRP B CG  1 
ATOM   596  C CD1 . TRP A 1 79  ? 42.14893 -43.46675 -11.39633 1.000 248.72410 ? 79  TRP B CD1 1 
ATOM   597  C CD2 . TRP A 1 79  ? 42.24307 -44.73423 -13.23744 1.000 238.84507 ? 79  TRP B CD2 1 
ATOM   598  N NE1 . TRP A 1 79  ? 42.93052 -44.56304 -11.11361 1.000 242.48035 ? 79  TRP B NE1 1 
ATOM   599  C CE2 . TRP A 1 79  ? 43.00403 -45.35573 -12.22921 1.000 236.34418 ? 79  TRP B CE2 1 
ATOM   600  C CE3 . TRP A 1 79  ? 42.15416 -45.34702 -14.49118 1.000 239.65446 ? 79  TRP B CE3 1 
ATOM   601  C CZ2 . TRP A 1 79  ? 43.67263 -46.56094 -12.43501 1.000 233.20488 ? 79  TRP B CZ2 1 
ATOM   602  C CZ3 . TRP A 1 79  ? 42.81696 -46.54106 -14.69474 1.000 237.22639 ? 79  TRP B CZ3 1 
ATOM   603  C CH2 . TRP A 1 79  ? 43.56724 -47.13667 -13.67173 1.000 234.83516 ? 79  TRP B CH2 1 
ATOM   604  N N   . ALA A 1 80  ? 40.66327 -41.43898 -16.24705 1.000 241.59006 ? 80  ALA B N   1 
ATOM   605  C CA  . ALA A 1 80  ? 39.68618 -41.18955 -17.30239 1.000 245.69613 ? 80  ALA B CA  1 
ATOM   606  C C   . ALA A 1 80  ? 39.09801 -42.55499 -17.63993 1.000 248.22260 ? 80  ALA B C   1 
ATOM   607  O O   . ALA A 1 80  ? 39.62429 -43.27096 -18.49642 1.000 247.42731 ? 80  ALA B O   1 
ATOM   608  C CB  . ALA A 1 80  ? 40.31322 -40.52087 -18.51582 1.000 244.01993 ? 80  ALA B CB  1 
ATOM   609  N N   . GLY A 1 81  ? 38.00991 -42.90964 -16.95791 1.000 246.95459 ? 81  GLY B N   1 
ATOM   610  C CA  . GLY A 1 81  ? 37.36431 -44.19327 -17.15357 1.000 250.29148 ? 81  GLY B CA  1 
ATOM   611  C C   . GLY A 1 81  ? 38.30110 -45.35284 -16.89254 1.000 247.16408 ? 81  GLY B C   1 
ATOM   612  O O   . GLY A 1 81  ? 38.28647 -45.94638 -15.80972 1.000 247.51990 ? 81  GLY B O   1 
ATOM   613  N N   . GLN A 1 82  ? 39.12089 -45.68787 -17.89407 1.000 250.91052 ? 82  GLN B N   1 
ATOM   614  C CA  . GLN A 1 82  ? 40.19920 -46.65096 -17.70793 1.000 249.26370 ? 82  GLN B CA  1 
ATOM   615  C C   . GLN A 1 82  ? 41.50743 -46.16678 -18.32854 1.000 245.08147 ? 82  GLN B C   1 
ATOM   616  O O   . GLN A 1 82  ? 42.41747 -46.97713 -18.54140 1.000 244.65072 ? 82  GLN B O   1 
ATOM   617  C CB  . GLN A 1 82  ? 39.82885 -48.02304 -18.28390 1.000 257.85244 ? 82  GLN B CB  1 
ATOM   618  C CG  . GLN A 1 82  ? 38.64644 -48.68758 -17.59683 1.000 263.31137 ? 82  GLN B CG  1 
ATOM   619  C CD  . GLN A 1 82  ? 38.62174 -50.18878 -17.80398 1.000 270.01138 ? 82  GLN B CD  1 
ATOM   620  O OE1 . GLN A 1 82  ? 39.56861 -50.76918 -18.33476 1.000 271.01751 ? 82  GLN B OE1 1 
ATOM   621  N NE2 . GLN A 1 82  ? 37.53778 -50.82725 -17.37939 1.000 274.89368 ? 82  GLN B NE2 1 
ATOM   622  N N   . GLN A 1 83  ? 41.62322 -44.87332 -18.62962 1.000 258.11059 ? 83  GLN B N   1 
ATOM   623  C CA  . GLN A 1 83  ? 42.86014 -44.27580 -19.12416 1.000 253.90873 ? 83  GLN B CA  1 
ATOM   624  C C   . GLN A 1 83  ? 43.45078 -43.40768 -18.02006 1.000 245.25385 ? 83  GLN B C   1 
ATOM   625  O O   . GLN A 1 83  ? 42.86371 -42.38700 -17.64479 1.000 245.28105 ? 83  GLN B O   1 
ATOM   626  C CB  . GLN A 1 83  ? 42.62096 -43.44702 -20.38592 1.000 258.19448 ? 83  GLN B CB  1 
ATOM   627  C CG  . GLN A 1 83  ? 41.86644 -44.15599 -21.49860 1.000 268.46177 ? 83  GLN B CG  1 
ATOM   628  C CD  . GLN A 1 83  ? 41.77356 -43.31217 -22.76011 1.000 272.52212 ? 83  GLN B CD  1 
ATOM   629  O OE1 . GLN A 1 83  ? 42.59741 -43.43714 -23.66740 1.000 274.00331 ? 83  GLN B OE1 1 
ATOM   630  N NE2 . GLN A 1 83  ? 40.77131 -42.44263 -22.81879 1.000 274.55200 ? 83  GLN B NE2 1 
ATOM   631  N N   . LEU A 1 84  ? 44.60735 -43.81281 -17.50318 1.000 250.96324 ? 84  LEU B N   1 
ATOM   632  C CA  . LEU A 1 84  ? 45.33644 -42.97860 -16.55923 1.000 244.28426 ? 84  LEU B CA  1 
ATOM   633  C C   . LEU A 1 84  ? 45.84210 -41.72680 -17.26431 1.000 242.23463 ? 84  LEU B C   1 
ATOM   634  O O   . LEU A 1 84  ? 46.49812 -41.81076 -18.30725 1.000 242.46622 ? 84  LEU B O   1 
ATOM   635  C CB  . LEU A 1 84  ? 46.50427 -43.75691 -15.95591 1.000 239.63759 ? 84  LEU B CB  1 
ATOM   636  C CG  . LEU A 1 84  ? 46.45293 -44.08374 -14.46269 1.000 238.79471 ? 84  LEU B CG  1 
ATOM   637  C CD1 . LEU A 1 84  ? 47.84730 -44.39945 -13.94595 1.000 232.70659 ? 84  LEU B CD1 1 
ATOM   638  C CD2 . LEU A 1 84  ? 45.83628 -42.93883 -13.67598 1.000 240.38016 ? 84  LEU B CD2 1 
ATOM   639  N N   . LEU A 1 85  ? 45.52506 -40.56243 -16.70294 1.000 236.82980 ? 85  LEU B N   1 
ATOM   640  C CA  . LEU A 1 85  ? 45.96759 -39.29946 -17.27755 1.000 235.20563 ? 85  LEU B CA  1 
ATOM   641  C C   . LEU A 1 85  ? 47.12366 -38.66386 -16.52336 1.000 229.97394 ? 85  LEU B C   1 
ATOM   642  O O   . LEU A 1 85  ? 47.90748 -37.92573 -17.12997 1.000 228.06443 ? 85  LEU B O   1 
ATOM   643  C CB  . LEU A 1 85  ? 44.80779 -38.30076 -17.33803 1.000 240.11662 ? 85  LEU B CB  1 
ATOM   644  C CG  . LEU A 1 85  ? 43.47350 -38.81574 -17.87334 1.000 246.65535 ? 85  LEU B CG  1 
ATOM   645  C CD1 . LEU A 1 85  ? 42.42857 -37.71894 -17.79279 1.000 252.07619 ? 85  LEU B CD1 1 
ATOM   646  C CD2 . LEU A 1 85  ? 43.63000 -39.30647 -19.30485 1.000 246.65464 ? 85  LEU B CD2 1 
ATOM   647  N N   . TRP A 1 86  ? 47.25412 -38.92926 -15.22474 1.000 226.60270 ? 86  TRP B N   1 
ATOM   648  C CA  . TRP A 1 86  ? 48.29093 -38.28376 -14.43289 1.000 220.83653 ? 86  TRP B CA  1 
ATOM   649  C C   . TRP A 1 86  ? 48.43759 -39.00285 -13.10050 1.000 220.15844 ? 86  TRP B C   1 
ATOM   650  O O   . TRP A 1 86  ? 47.44824 -39.45886 -12.52234 1.000 227.44463 ? 86  TRP B O   1 
ATOM   651  C CB  . TRP A 1 86  ? 47.96431 -36.80115 -14.20900 1.000 221.77287 ? 86  TRP B CB  1 
ATOM   652  C CG  . TRP A 1 86  ? 48.91619 -36.10213 -13.29907 1.000 218.63662 ? 86  TRP B CG  1 
ATOM   653  C CD1 . TRP A 1 86  ? 50.10161 -35.52196 -13.64187 1.000 211.85028 ? 86  TRP B CD1 1 
ATOM   654  C CD2 . TRP A 1 86  ? 48.75617 -35.89098 -11.89306 1.000 222.75365 ? 86  TRP B CD2 1 
ATOM   655  N NE1 . TRP A 1 86  ? 50.69503 -34.96902 -12.53277 1.000 209.24414 ? 86  TRP B NE1 1 
ATOM   656  C CE2 . TRP A 1 86  ? 49.88798 -35.18162 -11.44602 1.000 216.26835 ? 86  TRP B CE2 1 
ATOM   657  C CE3 . TRP A 1 86  ? 47.76718 -36.23654 -10.96794 1.000 231.18667 ? 86  TRP B CE3 1 
ATOM   658  C CZ2 . TRP A 1 86  ? 50.05796 -34.81123 -10.11446 1.000 218.04155 ? 86  TRP B CZ2 1 
ATOM   659  C CZ3 . TRP A 1 86  ? 47.93690 -35.86781 -9.64850  1.000 233.00687 ? 86  TRP B CZ3 1 
ATOM   660  C CH2 . TRP A 1 86  ? 49.07378 -35.16311 -9.23282  1.000 226.35188 ? 86  TRP B CH2 1 
ATOM   661  N N   . LYS A 1 87  ? 49.67802 -39.09187 -12.62523 1.000 220.30736 ? 87  LYS B N   1 
ATOM   662  C CA  . LYS A 1 87  ? 50.01121 -39.72425 -11.35797 1.000 221.02365 ? 87  LYS B CA  1 
ATOM   663  C C   . LYS A 1 87  ? 51.02801 -38.84945 -10.64075 1.000 217.22632 ? 87  LYS B C   1 
ATOM   664  O O   . LYS A 1 87  ? 51.95542 -38.33140 -11.26870 1.000 209.76655 ? 87  LYS B O   1 
ATOM   665  C CB  . LYS A 1 87  ? 50.57254 -41.13816 -11.57692 1.000 216.52472 ? 87  LYS B CB  1 
ATOM   666  C CG  . LYS A 1 87  ? 50.96834 -41.88057 -10.30852 1.000 217.94476 ? 87  LYS B CG  1 
ATOM   667  C CD  . LYS A 1 87  ? 51.33091 -43.33063 -10.61496 1.000 214.28666 ? 87  LYS B CD  1 
ATOM   668  C CE  . LYS A 1 87  ? 51.29399 -44.19977 -9.36476  1.000 217.98315 ? 87  LYS B CE  1 
ATOM   669  N NZ  . LYS A 1 87  ? 49.91763 -44.32421 -8.80684  1.000 226.06941 ? 87  LYS B NZ  1 
ATOM   670  N N   . GLY A 1 88  ? 50.85178 -38.67458 -9.33931  1.000 205.12478 ? 88  GLY B N   1 
ATOM   671  C CA  . GLY A 1 88  ? 51.73657 -37.80933 -8.59530  1.000 201.99789 ? 88  GLY B CA  1 
ATOM   672  C C   . GLY A 1 88  ? 51.68121 -38.02534 -7.10032  1.000 206.30004 ? 88  GLY B C   1 
ATOM   673  O O   . GLY A 1 88  ? 51.22439 -39.06212 -6.61617  1.000 210.15361 ? 88  GLY B O   1 
ATOM   674  N N   . SER A 1 89  ? 52.16342 -37.02128 -6.37006  1.000 193.51409 ? 89  SER B N   1 
ATOM   675  C CA  . SER A 1 89  ? 52.23806 -37.05932 -4.91849  1.000 197.81663 ? 89  SER B CA  1 
ATOM   676  C C   . SER A 1 89  ? 51.68255 -35.76522 -4.34151  1.000 201.26875 ? 89  SER B C   1 
ATOM   677  O O   . SER A 1 89  ? 51.54414 -34.75842 -5.04042  1.000 199.05703 ? 89  SER B O   1 
ATOM   678  C CB  . SER A 1 89  ? 53.67857 -37.26386 -4.43257  1.000 192.01900 ? 89  SER B CB  1 
ATOM   679  O OG  . SER A 1 89  ? 54.47242 -36.12128 -4.69391  1.000 188.03198 ? 89  SER B OG  1 
ATOM   680  N N   . PHE A 1 90  ? 51.36689 -35.79974 -3.04779  1.000 183.88763 ? 90  PHE B N   1 
ATOM   681  C CA  . PHE A 1 90  ? 50.91147 -34.60342 -2.35140  1.000 187.38425 ? 90  PHE B CA  1 
ATOM   682  C C   . PHE A 1 90  ? 51.29418 -34.68832 -0.88295  1.000 189.45279 ? 90  PHE B C   1 
ATOM   683  O O   . PHE A 1 90  ? 50.96808 -35.66923 -0.20808  1.000 193.23223 ? 90  PHE B O   1 
ATOM   684  C CB  . PHE A 1 90  ? 49.39674 -34.41122 -2.48259  1.000 194.25470 ? 90  PHE B CB  1 
ATOM   685  C CG  . PHE A 1 90  ? 48.87259 -33.22717 -1.71586  1.000 197.39549 ? 90  PHE B CG  1 
ATOM   686  C CD1 . PHE A 1 90  ? 49.47847 -31.98626 -1.83696  1.000 191.82498 ? 90  PHE B CD1 1 
ATOM   687  C CD2 . PHE A 1 90  ? 47.78331 -33.35410 -0.86957  1.000 203.52591 ? 90  PHE B CD2 1 
ATOM   688  C CE1 . PHE A 1 90  ? 49.00559 -30.89345 -1.13327  1.000 194.80207 ? 90  PHE B CE1 1 
ATOM   689  C CE2 . PHE A 1 90  ? 47.30501 -32.26317 -0.16313  1.000 204.18291 ? 90  PHE B CE2 1 
ATOM   690  C CZ  . PHE A 1 90  ? 47.91745 -31.03193 -0.29609  1.000 199.76154 ? 90  PHE B CZ  1 
ATOM   691  N N   . LYS A 1 91  ? 51.98057 -33.65422 -0.39949  1.000 187.95828 ? 91  LYS B N   1 
ATOM   692  C CA  . LYS A 1 91  ? 52.30587 -33.50147 1.01468   1.000 188.81542 ? 91  LYS B CA  1 
ATOM   693  C C   . LYS A 1 91  ? 51.47872 -32.35557 1.57889   1.000 190.97203 ? 91  LYS B C   1 
ATOM   694  O O   . LYS A 1 91  ? 51.77596 -31.18269 1.30278   1.000 189.20700 ? 91  LYS B O   1 
ATOM   695  C CB  . LYS A 1 91  ? 53.80048 -33.22999 1.20482   1.000 183.50376 ? 91  LYS B CB  1 
ATOM   696  C CG  . LYS A 1 91  ? 54.21344 -33.01282 2.65128   1.000 185.01588 ? 91  LYS B CG  1 
ATOM   697  C CD  . LYS A 1 91  ? 55.65378 -33.44274 2.88446   1.000 179.98798 ? 91  LYS B CD  1 
ATOM   698  C CE  . LYS A 1 91  ? 55.82362 -34.10687 4.24145   1.000 180.50110 ? 91  LYS B CE  1 
ATOM   699  N NZ  . LYS A 1 91  ? 57.23499 -34.50752 4.50551   1.000 174.87830 ? 91  LYS B NZ  1 
ATOM   700  N N   . PRO A 1 92  ? 50.43309 -32.63322 2.36080   1.000 183.27649 ? 92  PRO B N   1 
ATOM   701  C CA  . PRO A 1 92  ? 49.55288 -31.54952 2.82579   1.000 185.74796 ? 92  PRO B CA  1 
ATOM   702  C C   . PRO A 1 92  ? 50.24388 -30.51749 3.69528   1.000 183.77022 ? 92  PRO B C   1 
ATOM   703  O O   . PRO A 1 92  ? 49.69976 -29.42118 3.87409   1.000 185.14382 ? 92  PRO B O   1 
ATOM   704  C CB  . PRO A 1 92  ? 48.48110 -32.30651 3.61933   1.000 191.19062 ? 92  PRO B CB  1 
ATOM   705  C CG  . PRO A 1 92  ? 48.40113 -33.61225 2.91148   1.000 193.16406 ? 92  PRO B CG  1 
ATOM   706  C CD  . PRO A 1 92  ? 49.85178 -33.95323 2.65850   1.000 187.54112 ? 92  PRO B CD  1 
ATOM   707  N N   . SER A 1 93  ? 51.42276 -30.82273 4.23411   1.000 196.21842 ? 93  SER B N   1 
ATOM   708  C CA  . SER A 1 93  ? 52.01829 -29.99122 5.26978   1.000 195.68594 ? 93  SER B CA  1 
ATOM   709  C C   . SER A 1 93  ? 52.85528 -28.83844 4.73081   1.000 192.68587 ? 93  SER B C   1 
ATOM   710  O O   . SER A 1 93  ? 53.07904 -27.86844 5.46351   1.000 192.66127 ? 93  SER B O   1 
ATOM   711  C CB  . SER A 1 93  ? 52.87797 -30.84994 6.20259   1.000 193.43087 ? 93  SER B CB  1 
ATOM   712  O OG  . SER A 1 93  ? 53.93607 -31.46698 5.49372   1.000 188.83607 ? 93  SER B OG  1 
ATOM   713  N N   . GLU A 1 94  ? 53.32907 -28.90989 3.48598   1.000 204.62267 ? 94  GLU B N   1 
ATOM   714  C CA  . GLU A 1 94  ? 54.09841 -27.80453 2.92610   1.000 199.12506 ? 94  GLU B CA  1 
ATOM   715  C C   . GLU A 1 94  ? 53.23968 -26.78041 2.19985   1.000 200.89870 ? 94  GLU B C   1 
ATOM   716  O O   . GLU A 1 94  ? 53.67912 -25.63769 2.02277   1.000 198.30578 ? 94  GLU B O   1 
ATOM   717  C CB  . GLU A 1 94  ? 55.17270 -28.31555 1.96007   1.000 191.58295 ? 94  GLU B CB  1 
ATOM   718  C CG  . GLU A 1 94  ? 56.23328 -29.20123 2.58994   1.000 190.79478 ? 94  GLU B CG  1 
ATOM   719  C CD  . GLU A 1 94  ? 57.46235 -29.33413 1.70937   1.000 183.81384 ? 94  GLU B CD  1 
ATOM   720  O OE1 . GLU A 1 94  ? 57.40318 -28.90731 0.53526   1.000 181.07569 ? 94  GLU B OE1 1 
ATOM   721  O OE2 . GLU A 1 94  ? 58.48849 -29.85806 2.19194   1.000 179.49006 ? 94  GLU B OE2 1 
ATOM   722  N N   . HIS A 1 95  ? 52.03749 -27.15552 1.77601   1.000 202.26174 ? 95  HIS B N   1 
ATOM   723  C CA  . HIS A 1 95  ? 51.17203 -26.29462 0.97919   1.000 202.80240 ? 95  HIS B CA  1 
ATOM   724  C C   . HIS A 1 95  ? 49.91262 -25.91882 1.75085   1.000 209.34486 ? 95  HIS B C   1 
ATOM   725  O O   . HIS A 1 95  ? 48.81269 -25.88970 1.20012   1.000 212.86094 ? 95  HIS B O   1 
ATOM   726  C CB  . HIS A 1 95  ? 50.81172 -26.97701 -0.33744  1.000 200.86687 ? 95  HIS B CB  1 
ATOM   727  C CG  . HIS A 1 95  ? 52.00269 -27.42795 -1.12334  1.000 193.94957 ? 95  HIS B CG  1 
ATOM   728  N ND1 . HIS A 1 95  ? 52.66759 -26.60571 -2.00849  1.000 188.30457 ? 95  HIS B ND1 1 
ATOM   729  C CD2 . HIS A 1 95  ? 52.65735 -28.61278 -1.14725  1.000 192.16915 ? 95  HIS B CD2 1 
ATOM   730  C CE1 . HIS A 1 95  ? 53.67717 -27.26652 -2.54554  1.000 181.98617 ? 95  HIS B CE1 1 
ATOM   731  N NE2 . HIS A 1 95  ? 53.69316 -28.48722 -2.04015  1.000 184.41111 ? 95  HIS B NE2 1 
ATOM   732  N N   . VAL A 1 96  ? 50.06655 -25.62543 3.04142   1.000 185.67238 ? 96  VAL B N   1 
ATOM   733  C CA  . VAL A 1 96  ? 48.91364 -25.39755 3.90102   1.000 191.46106 ? 96  VAL B CA  1 
ATOM   734  C C   . VAL A 1 96  ? 48.23847 -24.08165 3.53551   1.000 192.12788 ? 96  VAL B C   1 
ATOM   735  O O   . VAL A 1 96  ? 48.90221 -23.07461 3.25523   1.000 188.29322 ? 96  VAL B O   1 
ATOM   736  C CB  . VAL A 1 96  ? 49.34195 -25.41325 5.37877   1.000 192.19923 ? 96  VAL B CB  1 
ATOM   737  C CG1 . VAL A 1 96  ? 48.14942 -25.15424 6.28790   1.000 194.60374 ? 96  VAL B CG1 1 
ATOM   738  C CG2 . VAL A 1 96  ? 50.00697 -26.73547 5.72693   1.000 190.41572 ? 96  VAL B CG2 1 
ATOM   739  N N   . LYS A 1 97  ? 46.90977 -24.09285 3.51791   1.000 198.34691 ? 97  LYS B N   1 
ATOM   740  C CA  . LYS A 1 97  ? 46.10272 -22.87723 3.41242   1.000 191.31346 ? 97  LYS B CA  1 
ATOM   741  C C   . LYS A 1 97  ? 44.99981 -22.94778 4.45702   1.000 187.88936 ? 97  LYS B C   1 
ATOM   742  O O   . LYS A 1 97  ? 44.03427 -23.71811 4.27691   1.000 191.11634 ? 97  LYS B O   1 
ATOM   743  C CB  . LYS A 1 97  ? 45.49561 -22.70385 2.02411   1.000 192.39989 ? 97  LYS B CB  1 
ATOM   744  C CG  . LYS A 1 97  ? 44.55878 -21.50775 1.94632   1.000 186.48077 ? 97  LYS B CG  1 
ATOM   745  C CD  . LYS A 1 97  ? 43.87272 -21.39779 0.59929   1.000 187.58721 ? 97  LYS B CD  1 
ATOM   746  C CE  . LYS A 1 97  ? 42.96182 -20.18027 0.56401   1.000 182.73675 ? 97  LYS B CE  1 
ATOM   747  N NZ  . LYS A 1 97  ? 42.09584 -20.13752 -0.64747  1.000 186.63059 ? 97  LYS B NZ  1 
ATOM   748  N N   . PRO A 1 98  ? 45.07403 -22.16054 5.52841   1.000 181.54173 ? 98  PRO B N   1 
ATOM   749  C CA  . PRO A 1 98  ? 44.11709 -22.31542 6.63320   1.000 178.15255 ? 98  PRO B CA  1 
ATOM   750  C C   . PRO A 1 98  ? 42.68098 -21.97649 6.26424   1.000 175.83060 ? 98  PRO B C   1 
ATOM   751  O O   . PRO A 1 98  ? 42.37481 -21.62491 5.12056   1.000 177.01659 ? 98  PRO B O   1 
ATOM   752  C CB  . PRO A 1 98  ? 44.65952 -21.35213 7.69614   1.000 175.66622 ? 98  PRO B CB  1 
ATOM   753  C CG  . PRO A 1 98  ? 45.41657 -20.33250 6.91892   1.000 176.48951 ? 98  PRO B CG  1 
ATOM   754  C CD  . PRO A 1 98  ? 46.03327 -21.07298 5.77446   1.000 181.01904 ? 98  PRO B CD  1 
ATOM   755  N N   . ARG A 1 99  ? 41.79640 -22.08035 7.24863   1.000 183.54951 ? 99  ARG B N   1 
ATOM   756  C CA  . ARG A 1 99  ? 40.36645 -21.90324 7.06798   1.000 182.75795 ? 99  ARG B CA  1 
ATOM   757  C C   . ARG A 1 99  ? 39.99331 -20.43247 7.22326   1.000 177.24959 ? 99  ARG B C   1 
ATOM   758  O O   . ARG A 1 99  ? 40.77879 -19.61081 7.69922   1.000 173.14236 ? 99  ARG B O   1 
ATOM   759  C CB  . ARG A 1 99  ? 39.61245 -22.75788 8.08420   1.000 183.69632 ? 99  ARG B CB  1 
ATOM   760  C CG  . ARG A 1 99  ? 38.23053 -23.21894 7.67785   1.000 188.25618 ? 99  ARG B CG  1 
ATOM   761  C CD  . ARG A 1 99  ? 37.72372 -24.20081 8.71978   1.000 189.30281 ? 99  ARG B CD  1 
ATOM   762  N NE  . ARG A 1 99  ? 38.45716 -25.45973 8.65180   1.000 196.10819 ? 99  ARG B NE  1 
ATOM   763  C CZ  . ARG A 1 99  ? 37.95371 -26.64447 8.96873   1.000 199.38671 ? 99  ARG B CZ  1 
ATOM   764  N NH1 . ARG A 1 99  ? 36.70974 -26.77407 9.39839   1.000 196.75735 ? 99  ARG B NH1 1 
ATOM   765  N NH2 . ARG A 1 99  ? 38.72210 -27.72543 8.86344   1.000 205.43732 ? 99  ARG B NH2 1 
ATOM   766  N N   . ALA A 1 100 ? 38.77074 -20.10469 6.81962   1.000 184.79331 ? 100 ALA B N   1 
ATOM   767  C CA  . ALA A 1 100 ? 38.46078 -18.70166 7.05656   1.000 180.39419 ? 100 ALA B CA  1 
ATOM   768  C C   . ALA A 1 100 ? 37.93055 -18.50732 8.47434   1.000 176.18484 ? 100 ALA B C   1 
ATOM   769  O O   . ALA A 1 100 ? 37.18754 -19.35375 8.98054   1.000 176.81814 ? 100 ALA B O   1 
ATOM   770  C CB  . ALA A 1 100 ? 37.42774 -18.19672 6.05380   1.000 182.60447 ? 100 ALA B CB  1 
ATOM   771  N N   . PRO A 1 101 ? 38.30764 -17.41851 9.14194   1.000 182.86651 ? 101 PRO B N   1 
ATOM   772  C CA  . PRO A 1 101 ? 37.66920 -17.08681 10.41809  1.000 180.43253 ? 101 PRO B CA  1 
ATOM   773  C C   . PRO A 1 101 ? 36.19350 -16.77784 10.21143  1.000 180.48108 ? 101 PRO B C   1 
ATOM   774  O O   . PRO A 1 101 ? 35.73262 -16.52385 9.09664   1.000 182.23105 ? 101 PRO B O   1 
ATOM   775  C CB  . PRO A 1 101 ? 38.44415 -15.85067 10.89201  1.000 178.50254 ? 101 PRO B CB  1 
ATOM   776  C CG  . PRO A 1 101 ? 39.76889 -15.95375 10.18555  1.000 179.88250 ? 101 PRO B CG  1 
ATOM   777  C CD  . PRO A 1 101 ? 39.41516 -16.49888 8.83246   1.000 182.30137 ? 101 PRO B CD  1 
ATOM   778  N N   . GLY A 1 102 ? 35.44222 -16.81426 11.30661  1.000 191.59688 ? 102 GLY B N   1 
ATOM   779  C CA  . GLY A 1 102 ? 34.01674 -16.56626 11.22121  1.000 192.36634 ? 102 GLY B CA  1 
ATOM   780  C C   . GLY A 1 102 ? 33.42471 -15.99330 12.49023  1.000 190.29755 ? 102 GLY B C   1 
ATOM   781  O O   . GLY A 1 102 ? 34.15951 -15.60044 13.40085  1.000 188.81194 ? 102 GLY B O   1 
ATOM   782  N N   . ASN A 1 103 ? 32.09251 -15.93721 12.55392  1.000 195.74315 ? 103 ASN B N   1 
ATOM   783  C CA  . ASN A 1 103 ? 31.36863 -15.46421 13.73493  1.000 195.81116 ? 103 ASN B CA  1 
ATOM   784  C C   . ASN A 1 103 ? 31.73922 -14.02358 14.08159  1.000 196.04561 ? 103 ASN B C   1 
ATOM   785  O O   . ASN A 1 103 ? 31.75086 -13.63822 15.25363  1.000 195.96116 ? 103 ASN B O   1 
ATOM   786  C CB  . ASN A 1 103 ? 31.61453 -16.38075 14.93921  1.000 194.79118 ? 103 ASN B CB  1 
ATOM   787  C CG  . ASN A 1 103 ? 31.19664 -17.82034 14.67982  1.000 195.31645 ? 103 ASN B CG  1 
ATOM   788  O OD1 . ASN A 1 103 ? 31.68834 -18.74618 15.32802  1.000 195.37118 ? 103 ASN B OD1 1 
ATOM   789  N ND2 . ASN A 1 103 ? 30.29090 -18.01518 13.72892  1.000 196.91422 ? 103 ASN B ND2 1 
ATOM   790  N N   . LEU A 1 104 ? 32.03652 -13.21665 13.06556  1.000 199.74076 ? 104 LEU B N   1 
ATOM   791  C CA  . LEU A 1 104 ? 32.55979 -11.87089 13.26517  1.000 200.15288 ? 104 LEU B CA  1 
ATOM   792  C C   . LEU A 1 104 ? 31.41392 -10.88627 13.47300  1.000 203.52809 ? 104 LEU B C   1 
ATOM   793  O O   . LEU A 1 104 ? 30.58987 -10.68312 12.57367  1.000 207.07966 ? 104 LEU B O   1 
ATOM   794  C CB  . LEU A 1 104 ? 33.42390 -11.45043 12.07682  1.000 200.68112 ? 104 LEU B CB  1 
ATOM   795  C CG  . LEU A 1 104 ? 33.79011 -9.96774  11.97987  1.000 203.31371 ? 104 LEU B CG  1 
ATOM   796  C CD1 . LEU A 1 104 ? 34.76866 -9.57962  13.07164  1.000 200.50799 ? 104 LEU B CD1 1 
ATOM   797  C CD2 . LEU A 1 104 ? 34.37171 -9.65126  10.61418  1.000 205.18077 ? 104 LEU B CD2 1 
ATOM   798  N N   . THR A 1 105 ? 31.36652 -10.28089 14.65508  1.000 206.06999 ? 105 THR B N   1 
ATOM   799  C CA  . THR A 1 105 ? 30.38740 -9.24446  14.97512  1.000 210.20964 ? 105 THR B CA  1 
ATOM   800  C C   . THR A 1 105 ? 31.12568 -8.09930  15.66378  1.000 211.75566 ? 105 THR B C   1 
ATOM   801  O O   . THR A 1 105 ? 32.35926 -8.02334  15.64513  1.000 208.67624 ? 105 THR B O   1 
ATOM   802  C CB  . THR A 1 105 ? 29.23981 -9.80558  15.83191  1.000 210.47506 ? 105 THR B CB  1 
ATOM   803  O OG1 . THR A 1 105 ? 29.77399 -10.42806 17.00758  1.000 207.37139 ? 105 THR B OG1 1 
ATOM   804  C CG2 . THR A 1 105 ? 28.40896 -10.81340 15.04452  1.000 209.75639 ? 105 THR B CG2 1 
ATOM   805  N N   . VAL A 1 106 ? 30.36825 -7.19530  16.28460  1.000 213.83134 ? 106 VAL B N   1 
ATOM   806  C CA  . VAL A 1 106 ? 30.90555 -5.97637  16.88302  1.000 216.44167 ? 106 VAL B CA  1 
ATOM   807  C C   . VAL A 1 106 ? 30.12263 -5.65714  18.15173  1.000 220.55691 ? 106 VAL B C   1 
ATOM   808  O O   . VAL A 1 106 ? 28.90164 -5.83987  18.20265  1.000 224.51644 ? 106 VAL B O   1 
ATOM   809  C CB  . VAL A 1 106 ? 30.84459 -4.79001  15.89248  1.000 220.90045 ? 106 VAL B CB  1 
ATOM   810  C CG1 . VAL A 1 106 ? 31.04176 -3.46431  16.60843  1.000 225.43112 ? 106 VAL B CG1 1 
ATOM   811  C CG2 . VAL A 1 106 ? 31.88365 -4.94521  14.79327  1.000 218.14489 ? 106 VAL B CG2 1 
ATOM   812  N N   . HIS A 1 107 ? 30.82978 -5.19286  19.18054  1.000 225.82006 ? 107 HIS B N   1 
ATOM   813  C CA  . HIS A 1 107 ? 30.18702 -4.64301  20.37212  1.000 231.15940 ? 107 HIS B CA  1 
ATOM   814  C C   . HIS A 1 107 ? 30.34458 -3.12493  20.42496  1.000 235.99363 ? 107 HIS B C   1 
ATOM   815  O O   . HIS A 1 107 ? 31.38632 -2.58321  20.05209  1.000 234.69533 ? 107 HIS B O   1 
ATOM   816  C CB  . HIS A 1 107 ? 30.76098 -5.27362  21.64192  1.000 230.52580 ? 107 HIS B CB  1 
ATOM   817  C CG  . HIS A 1 107 ? 29.91962 -5.05512  22.86211  1.000 236.74352 ? 107 HIS B CG  1 
ATOM   818  N ND1 . HIS A 1 107 ? 30.44951 -5.02153  24.13451  1.000 239.14575 ? 107 HIS B ND1 1 
ATOM   819  C CD2 . HIS A 1 107 ? 28.58898 -4.84821  23.00393  1.000 240.36794 ? 107 HIS B CD2 1 
ATOM   820  C CE1 . HIS A 1 107 ? 29.48053 -4.81231  25.00783  1.000 243.01485 ? 107 HIS B CE1 1 
ATOM   821  N NE2 . HIS A 1 107 ? 28.34180 -4.70244  24.34762  1.000 243.89061 ? 107 HIS B NE2 1 
ATOM   822  N N   . ASP A 1 112 ? 33.41174 5.46594   23.65429  1.000 236.81159 ? 112 ASP B N   1 
ATOM   823  C CA  . ASP A 1 112 ? 34.07963 4.37205   24.35146  1.000 229.71738 ? 112 ASP B CA  1 
ATOM   824  C C   . ASP A 1 112 ? 34.85015 3.47162   23.38789  1.000 222.05929 ? 112 ASP B C   1 
ATOM   825  O O   . ASP A 1 112 ? 34.96760 3.77225   22.19874  1.000 221.28775 ? 112 ASP B O   1 
ATOM   826  C CB  . ASP A 1 112 ? 33.06203 3.55695   25.16773  1.000 230.58660 ? 112 ASP B CB  1 
ATOM   827  C CG  . ASP A 1 112 ? 31.95739 2.94332   24.31099  1.000 230.00733 ? 112 ASP B CG  1 
ATOM   828  O OD1 . ASP A 1 112 ? 32.24263 2.37845   23.23415  1.000 225.79858 ? 112 ASP B OD1 1 
ATOM   829  O OD2 . ASP A 1 112 ? 30.78373 3.02503   24.73099  1.000 234.84565 ? 112 ASP B OD2 1 
ATOM   830  N N   . THR A 1 113 ? 35.37520 2.36770   23.91017  1.000 239.76312 ? 113 THR B N   1 
ATOM   831  C CA  . THR A 1 113 ? 36.12024 1.42764   23.08921  1.000 232.99437 ? 113 THR B CA  1 
ATOM   832  C C   . THR A 1 113 ? 35.17110 0.59813   22.23187  1.000 229.11253 ? 113 THR B C   1 
ATOM   833  O O   . THR A 1 113 ? 34.02162 0.34104   22.60207  1.000 231.73452 ? 113 THR B O   1 
ATOM   834  C CB  . THR A 1 113 ? 36.99099 0.51746   23.96245  1.000 231.13459 ? 113 THR B CB  1 
ATOM   835  O OG1 . THR A 1 113 ? 38.00217 -0.10343  23.15768  1.000 227.26367 ? 113 THR B OG1 1 
ATOM   836  C CG2 . THR A 1 113 ? 36.15356 -0.55513  24.64954  1.000 231.51456 ? 113 THR B CG2 1 
ATOM   837  N N   . LEU A 1 114 ? 35.65679 0.20273   21.06052  1.000 230.98654 ? 114 LEU B N   1 
ATOM   838  C CA  . LEU A 1 114 ? 34.89038 -0.60606  20.12602  1.000 226.86863 ? 114 LEU B CA  1 
ATOM   839  C C   . LEU A 1 114 ? 35.48723 -2.00495  20.07328  1.000 219.83062 ? 114 LEU B C   1 
ATOM   840  O O   . LEU A 1 114 ? 36.71119 -2.16681  20.03157  1.000 216.24950 ? 114 LEU B O   1 
ATOM   841  C CB  . LEU A 1 114 ? 34.87928 0.02702   18.73211  1.000 229.07062 ? 114 LEU B CB  1 
ATOM   842  C CG  . LEU A 1 114 ? 34.25165 -0.78379  17.59997  1.000 226.87972 ? 114 LEU B CG  1 
ATOM   843  C CD1 . LEU A 1 114 ? 32.77318 -0.45978  17.49818  1.000 232.58320 ? 114 LEU B CD1 1 
ATOM   844  C CD2 . LEU A 1 114 ? 34.95477 -0.48775  16.28572  1.000 227.10183 ? 114 LEU B CD2 1 
ATOM   845  N N   . LEU A 1 115 ? 34.61762 -3.01098  20.07791  1.000 221.55836 ? 115 LEU B N   1 
ATOM   846  C CA  . LEU A 1 115 ? 35.01692 -4.40414  20.21677  1.000 217.05337 ? 115 LEU B CA  1 
ATOM   847  C C   . LEU A 1 115 ? 34.71111 -5.17617  18.94206  1.000 213.56533 ? 115 LEU B C   1 
ATOM   848  O O   . LEU A 1 115 ? 33.57464 -5.16432  18.45735  1.000 215.29989 ? 115 LEU B O   1 
ATOM   849  C CB  . LEU A 1 115 ? 34.31051 -5.05044  21.41244  1.000 218.82154 ? 115 LEU B CB  1 
ATOM   850  C CG  . LEU A 1 115 ? 34.62948 -6.50980  21.74382  1.000 216.95008 ? 115 LEU B CG  1 
ATOM   851  C CD1 . LEU A 1 115 ? 36.09209 -6.68576  22.09979  1.000 216.66396 ? 115 LEU B CD1 1 
ATOM   852  C CD2 . LEU A 1 115 ? 33.75164 -6.98408  22.88446  1.000 220.47412 ? 115 LEU B CD2 1 
ATOM   853  N N   . LEU A 1 116 ? 35.72998 -5.84371  18.40793  1.000 216.99740 ? 116 LEU B N   1 
ATOM   854  C CA  . LEU A 1 116 ? 35.58709 -6.78104  17.30575  1.000 214.23210 ? 116 LEU B CA  1 
ATOM   855  C C   . LEU A 1 116 ? 35.95465 -8.17317  17.79735  1.000 212.14472 ? 116 LEU B C   1 
ATOM   856  O O   . LEU A 1 116 ? 36.81434 -8.32840  18.66910  1.000 212.57167 ? 116 LEU B O   1 
ATOM   857  C CB  . LEU A 1 116 ? 36.47957 -6.40191  16.11896  1.000 213.34671 ? 116 LEU B CB  1 
ATOM   858  C CG  . LEU A 1 116 ? 36.01509 -5.29498  15.17205  1.000 216.68876 ? 116 LEU B CG  1 
ATOM   859  C CD1 . LEU A 1 116 ? 35.99638 -3.93806  15.85892  1.000 221.20527 ? 116 LEU B CD1 1 
ATOM   860  C CD2 . LEU A 1 116 ? 36.91311 -5.26442  13.95259  1.000 216.41358 ? 116 LEU B CD2 1 
ATOM   861  N N   . THR A 1 117 ? 35.30234 -9.18810  17.23594  1.000 206.63511 ? 117 THR B N   1 
ATOM   862  C CA  . THR A 1 117 ? 35.56474 -10.55428 17.66546  1.000 205.79708 ? 117 THR B CA  1 
ATOM   863  C C   . THR A 1 117 ? 35.20835 -11.51980 16.54570  1.000 203.36365 ? 117 THR B C   1 
ATOM   864  O O   . THR A 1 117 ? 34.35585 -11.22954 15.70410  1.000 203.60079 ? 117 THR B O   1 
ATOM   865  C CB  . THR A 1 117 ? 34.78522 -10.90450 18.94047  1.000 209.16139 ? 117 THR B CB  1 
ATOM   866  O OG1 . THR A 1 117 ? 35.32055 -12.10239 19.51656  1.000 212.55633 ? 117 THR B OG1 1 
ATOM   867  C CG2 . THR A 1 117 ? 33.30491 -11.10642 18.63704  1.000 208.48997 ? 117 THR B CG2 1 
ATOM   868  N N   . TRP A 1 118 ? 35.88014 -12.66899 16.54826  1.000 198.04494 ? 118 TRP B N   1 
ATOM   869  C CA  . TRP A 1 118 ? 35.62602 -13.73087 15.58619  1.000 197.18940 ? 118 TRP B CA  1 
ATOM   870  C C   . TRP A 1 118 ? 36.01581 -15.05407 16.23474  1.000 197.75547 ? 118 TRP B C   1 
ATOM   871  O O   . TRP A 1 118 ? 36.42709 -15.10021 17.39751  1.000 199.07169 ? 118 TRP B O   1 
ATOM   872  C CB  . TRP A 1 118 ? 36.38543 -13.48133 14.27691  1.000 196.33043 ? 118 TRP B CB  1 
ATOM   873  C CG  . TRP A 1 118 ? 37.87093 -13.40497 14.44407  1.000 196.25541 ? 118 TRP B CG  1 
ATOM   874  C CD1 . TRP A 1 118 ? 38.76733 -14.41138 14.24261  1.000 196.27396 ? 118 TRP B CD1 1 
ATOM   875  C CD2 . TRP A 1 118 ? 38.63426 -12.26596 14.86452  1.000 196.19893 ? 118 TRP B CD2 1 
ATOM   876  N NE1 . TRP A 1 118 ? 40.03945 -13.96951 14.50153  1.000 197.26853 ? 118 TRP B NE1 1 
ATOM   877  C CE2 . TRP A 1 118 ? 39.98661 -12.65681 14.88695  1.000 196.68904 ? 118 TRP B CE2 1 
ATOM   878  C CE3 . TRP A 1 118 ? 38.30584 -10.95421 15.21997  1.000 196.49459 ? 118 TRP B CE3 1 
ATOM   879  C CZ2 . TRP A 1 118 ? 41.00986 -11.78572 15.25081  1.000 198.32026 ? 118 TRP B CZ2 1 
ATOM   880  C CZ3 . TRP A 1 118 ? 39.32384 -10.09049 15.57998  1.000 197.01800 ? 118 TRP B CZ3 1 
ATOM   881  C CH2 . TRP A 1 118 ? 40.65859 -10.51088 15.59551  1.000 198.26527 ? 118 TRP B CH2 1 
ATOM   882  N N   . SER A 1 119 ? 35.87704 -16.13710 15.48035  1.000 198.83494 ? 119 SER B N   1 
ATOM   883  C CA  . SER A 1 119 ? 36.22269 -17.46250 15.96877  1.000 199.90398 ? 119 SER B CA  1 
ATOM   884  C C   . SER A 1 119 ? 37.56675 -17.90380 15.40583  1.000 200.25372 ? 119 SER B C   1 
ATOM   885  O O   . SER A 1 119 ? 37.96793 -17.49634 14.31280  1.000 199.19855 ? 119 SER B O   1 
ATOM   886  C CB  . SER A 1 119 ? 35.14857 -18.48548 15.59173  1.000 200.32340 ? 119 SER B CB  1 
ATOM   887  O OG  . SER A 1 119 ? 33.91323 -18.19031 16.21722  1.000 200.51558 ? 119 SER B OG  1 
ATOM   888  N N   . ASN A 1 120 ? 38.26443 -18.73303 16.16905  1.000 198.09702 ? 120 ASN B N   1 
ATOM   889  C CA  . ASN A 1 120 ? 39.43012 -19.41444 15.63019  1.000 200.37217 ? 120 ASN B CA  1 
ATOM   890  C C   . ASN A 1 120 ? 38.96643 -20.46488 14.62737  1.000 201.67495 ? 120 ASN B C   1 
ATOM   891  O O   . ASN A 1 120 ? 38.08041 -21.26898 14.94126  1.000 202.27968 ? 120 ASN B O   1 
ATOM   892  C CB  . ASN A 1 120 ? 40.25965 -20.04847 16.74523  1.000 202.71623 ? 120 ASN B CB  1 
ATOM   893  C CG  . ASN A 1 120 ? 39.46046 -21.01883 17.59026  1.000 204.37411 ? 120 ASN B CG  1 
ATOM   894  O OD1 . ASN A 1 120 ? 38.23089 -21.01171 17.57364  1.000 204.09885 ? 120 ASN B OD1 1 
ATOM   895  N ND2 . ASN A 1 120 ? 40.15940 -21.87373 18.32475  1.000 207.45189 ? 120 ASN B ND2 1 
ATOM   896  N N   . PRO A 1 121 ? 39.51118 -20.48034 13.41767  1.000 197.07473 ? 121 PRO B N   1 
ATOM   897  C CA  . PRO A 1 121 ? 38.98465 -21.38566 12.38600  1.000 200.48218 ? 121 PRO B CA  1 
ATOM   898  C C   . PRO A 1 121 ? 39.26786 -22.85255 12.67371  1.000 204.43957 ? 121 PRO B C   1 
ATOM   899  O O   . PRO A 1 121 ? 38.96545 -23.71775 11.84617  1.000 208.64934 ? 121 PRO B O   1 
ATOM   900  C CB  . PRO A 1 121 ? 39.70162 -20.91819 11.11162  1.000 201.48121 ? 121 PRO B CB  1 
ATOM   901  C CG  . PRO A 1 121 ? 40.91465 -20.19156 11.59505  1.000 199.02707 ? 121 PRO B CG  1 
ATOM   902  C CD  . PRO A 1 121 ? 40.51821 -19.54975 12.88461  1.000 196.11031 ? 121 PRO B CD  1 
ATOM   903  N N   . TYR A 1 122 ? 39.83381 -23.14708 13.83924  1.000 192.87548 ? 122 TYR B N   1 
ATOM   904  C CA  . TYR A 1 122 ? 40.25599 -24.49698 14.17646  1.000 196.57312 ? 122 TYR B CA  1 
ATOM   905  C C   . TYR A 1 122 ? 40.16332 -24.67551 15.68402  1.000 196.02793 ? 122 TYR B C   1 
ATOM   906  O O   . TYR A 1 122 ? 40.19168 -23.69112 16.43201  1.000 193.61580 ? 122 TYR B O   1 
ATOM   907  C CB  . TYR A 1 122 ? 41.68635 -24.76478 13.68853  1.000 199.58260 ? 122 TYR B CB  1 
ATOM   908  C CG  . TYR A 1 122 ? 41.83574 -24.72761 12.18362  1.000 202.40165 ? 122 TYR B CG  1 
ATOM   909  C CD1 . TYR A 1 122 ? 41.41744 -25.79293 11.39618  1.000 207.22303 ? 122 TYR B CD1 1 
ATOM   910  C CD2 . TYR A 1 122 ? 42.38191 -23.61946 11.54939  1.000 199.75057 ? 122 TYR B CD2 1 
ATOM   911  C CE1 . TYR A 1 122 ? 41.54919 -25.75916 10.01962  1.000 212.07898 ? 122 TYR B CE1 1 
ATOM   912  C CE2 . TYR A 1 122 ? 42.51468 -23.57587 10.17527  1.000 202.78510 ? 122 TYR B CE2 1 
ATOM   913  C CZ  . TYR A 1 122 ? 42.09986 -24.64816 9.41619   1.000 210.01605 ? 122 TYR B CZ  1 
ATOM   914  O OH  . TYR A 1 122 ? 42.23487 -24.60204 8.04845   1.000 215.02356 ? 122 TYR B OH  1 
ATOM   915  N N   . PRO A 1 123 ? 40.04553 -25.91191 16.16095  1.000 197.86046 ? 123 PRO B N   1 
ATOM   916  C CA  . PRO A 1 123 ? 40.03791 -26.15631 17.60367  1.000 198.48889 ? 123 PRO B CA  1 
ATOM   917  C C   . PRO A 1 123 ? 41.44571 -26.06844 18.17364  1.000 201.17424 ? 123 PRO B C   1 
ATOM   918  O O   . PRO A 1 123 ? 42.42671 -26.06038 17.41770  1.000 202.33097 ? 123 PRO B O   1 
ATOM   919  C CB  . PRO A 1 123 ? 39.47533 -27.57925 17.71094  1.000 201.55470 ? 123 PRO B CB  1 
ATOM   920  C CG  . PRO A 1 123 ? 39.92480 -28.23155 16.45808  1.000 203.70956 ? 123 PRO B CG  1 
ATOM   921  C CD  . PRO A 1 123 ? 39.86767 -27.15951 15.39773  1.000 201.40402 ? 123 PRO B CD  1 
ATOM   922  N N   . PRO A 1 124 ? 41.57925 -25.99210 19.50240  1.000 211.52683 ? 124 PRO B N   1 
ATOM   923  C CA  . PRO A 1 124 ? 42.91595 -25.78630 20.08829  1.000 214.95857 ? 124 PRO B CA  1 
ATOM   924  C C   . PRO A 1 124 ? 43.90109 -26.91534 19.83390  1.000 219.59678 ? 124 PRO B C   1 
ATOM   925  O O   . PRO A 1 124 ? 45.09811 -26.64078 19.68196  1.000 221.75391 ? 124 PRO B O   1 
ATOM   926  C CB  . PRO A 1 124 ? 42.61834 -25.63019 21.58620  1.000 217.47807 ? 124 PRO B CB  1 
ATOM   927  C CG  . PRO A 1 124 ? 41.21922 -25.12858 21.63460  1.000 213.58338 ? 124 PRO B CG  1 
ATOM   928  C CD  . PRO A 1 124 ? 40.51028 -25.80311 20.49681  1.000 211.31958 ? 124 PRO B CD  1 
ATOM   929  N N   . ASP A 1 125 ? 43.45085 -28.17174 19.79768  1.000 212.60587 ? 125 ASP B N   1 
ATOM   930  C CA  . ASP A 1 125 ? 44.38269 -29.27448 19.57878  1.000 217.56732 ? 125 ASP B CA  1 
ATOM   931  C C   . ASP A 1 125 ? 45.05111 -29.18083 18.21387  1.000 217.25183 ? 125 ASP B C   1 
ATOM   932  O O   . ASP A 1 125 ? 46.18965 -29.63432 18.04762  1.000 220.94721 ? 125 ASP B O   1 
ATOM   933  C CB  . ASP A 1 125 ? 43.65836 -30.61081 19.72067  1.000 221.40400 ? 125 ASP B CB  1 
ATOM   934  C CG  . ASP A 1 125 ? 42.29316 -30.59782 19.07218  1.000 219.42582 ? 125 ASP B CG  1 
ATOM   935  O OD1 . ASP A 1 125 ? 41.62970 -29.53992 19.10988  1.000 215.31287 ? 125 ASP B OD1 1 
ATOM   936  O OD2 . ASP A 1 125 ? 41.88766 -31.63938 18.51694  1.000 222.18278 ? 125 ASP B OD2 1 
ATOM   937  N N   . ASN A 1 126 ? 44.36118 -28.60338 17.23238  1.000 214.21139 ? 126 ASN B N   1 
ATOM   938  C CA  . ASN A 1 126 ? 44.94576 -28.38848 15.91623  1.000 214.76477 ? 126 ASN B CA  1 
ATOM   939  C C   . ASN A 1 126 ? 46.19068 -27.51437 16.02046  1.000 214.49375 ? 126 ASN B C   1 
ATOM   940  O O   . ASN A 1 126 ? 46.23760 -26.56307 16.80471  1.000 212.29149 ? 126 ASN B O   1 
ATOM   941  C CB  . ASN A 1 126 ? 43.91246 -27.74318 14.99219  1.000 211.14470 ? 126 ASN B CB  1 
ATOM   942  C CG  . ASN A 1 126 ? 44.53841 -27.09621 13.77973  1.000 211.26471 ? 126 ASN B CG  1 
ATOM   943  O OD1 . ASN A 1 126 ? 44.66983 -25.87535 13.71568  1.000 207.69291 ? 126 ASN B OD1 1 
ATOM   944  N ND2 . ASN A 1 126 ? 44.92726 -27.91123 12.80683  1.000 217.58242 ? 126 ASN B ND2 1 
ATOM   945  N N   . TYR A 1 127 ? 47.20798 -27.84618 15.21944  1.000 206.78436 ? 127 TYR B N   1 
ATOM   946  C CA  . TYR A 1 127 ? 48.49984 -27.17278 15.34198  1.000 206.73997 ? 127 TYR B CA  1 
ATOM   947  C C   . TYR A 1 127 ? 48.42239 -25.69912 14.95794  1.000 201.71033 ? 127 TYR B C   1 
ATOM   948  O O   . TYR A 1 127 ? 49.14740 -24.87733 15.53069  1.000 200.42569 ? 127 TYR B O   1 
ATOM   949  C CB  . TYR A 1 127 ? 49.55739 -27.87441 14.48431  1.000 211.23843 ? 127 TYR B CB  1 
ATOM   950  C CG  . TYR A 1 127 ? 49.79002 -29.34133 14.79571  1.000 217.70368 ? 127 TYR B CG  1 
ATOM   951  C CD1 . TYR A 1 127 ? 49.26315 -29.93190 15.93922  1.000 218.45274 ? 127 TYR B CD1 1 
ATOM   952  C CD2 . TYR A 1 127 ? 50.54788 -30.13396 13.94269  1.000 223.70439 ? 127 TYR B CD2 1 
ATOM   953  C CE1 . TYR A 1 127 ? 49.47851 -31.26988 16.21829  1.000 224.53060 ? 127 TYR B CE1 1 
ATOM   954  C CE2 . TYR A 1 127 ? 50.76946 -31.47168 14.21409  1.000 229.97823 ? 127 TYR B CE2 1 
ATOM   955  C CZ  . TYR A 1 127 ? 50.23246 -32.03409 15.35316  1.000 230.22003 ? 127 TYR B CZ  1 
ATOM   956  O OH  . TYR A 1 127 ? 50.45005 -33.36481 15.62786  1.000 235.30557 ? 127 TYR B OH  1 
ATOM   957  N N   . LEU A 1 128 ? 47.56273 -25.34253 13.99952  1.000 214.36255 ? 128 LEU B N   1 
ATOM   958  C CA  . LEU A 1 128 ? 47.50504 -23.96081 13.53009  1.000 209.53161 ? 128 LEU B CA  1 
ATOM   959  C C   . LEU A 1 128 ? 47.03684 -22.99898 14.61496  1.000 205.64174 ? 128 LEU B C   1 
ATOM   960  O O   . LEU A 1 128 ? 47.28255 -21.79317 14.50805  1.000 202.56948 ? 128 LEU B O   1 
ATOM   961  C CB  . LEU A 1 128 ? 46.58840 -23.86020 12.30846  1.000 208.18410 ? 128 LEU B CB  1 
ATOM   962  C CG  . LEU A 1 128 ? 46.75935 -24.93655 11.23282  1.000 214.81034 ? 128 LEU B CG  1 
ATOM   963  C CD1 . LEU A 1 128 ? 45.83142 -24.68354 10.05722  1.000 214.31575 ? 128 LEU B CD1 1 
ATOM   964  C CD2 . LEU A 1 128 ? 48.20092 -24.99460 10.76287  1.000 216.89247 ? 128 LEU B CD2 1 
ATOM   965  N N   . TYR A 1 129 ? 46.38331 -23.50798 15.66074  1.000 217.58100 ? 129 TYR B N   1 
ATOM   966  C CA  . TYR A 1 129 ? 45.87231 -22.66360 16.73376  1.000 216.11494 ? 129 TYR B CA  1 
ATOM   967  C C   . TYR A 1 129 ? 46.98262 -22.03759 17.57224  1.000 218.68022 ? 129 TYR B C   1 
ATOM   968  O O   . TYR A 1 129 ? 46.73512 -21.03718 18.25477  1.000 218.14891 ? 129 TYR B O   1 
ATOM   969  C CB  . TYR A 1 129 ? 44.93472 -23.49227 17.61706  1.000 217.37077 ? 129 TYR B CB  1 
ATOM   970  C CG  . TYR A 1 129 ? 44.39220 -22.78329 18.83796  1.000 216.38533 ? 129 TYR B CG  1 
ATOM   971  C CD1 . TYR A 1 129 ? 43.36973 -21.85059 18.72855  1.000 212.93731 ? 129 TYR B CD1 1 
ATOM   972  C CD2 . TYR A 1 129 ? 44.89192 -23.06175 20.10371  1.000 220.65027 ? 129 TYR B CD2 1 
ATOM   973  C CE1 . TYR A 1 129 ? 42.86633 -21.20827 19.84513  1.000 213.88053 ? 129 TYR B CE1 1 
ATOM   974  C CE2 . TYR A 1 129 ? 44.38862 -22.43366 21.22461  1.000 222.09315 ? 129 TYR B CE2 1 
ATOM   975  C CZ  . TYR A 1 129 ? 43.38000 -21.50303 21.09000  1.000 218.39851 ? 129 TYR B CZ  1 
ATOM   976  O OH  . TYR A 1 129 ? 42.88225 -20.86625 22.20386  1.000 220.39272 ? 129 TYR B OH  1 
ATOM   977  N N   . ASN A 1 130 ? 48.20005 -22.58402 17.52277  1.000 222.10177 ? 130 ASN B N   1 
ATOM   978  C CA  . ASN A 1 130 ? 49.27183 -22.14579 18.41031  1.000 226.11271 ? 130 ASN B CA  1 
ATOM   979  C C   . ASN A 1 130 ? 50.13578 -21.03677 17.82045  1.000 224.39402 ? 130 ASN B C   1 
ATOM   980  O O   . ASN A 1 130 ? 50.73083 -20.26687 18.58383  1.000 227.05844 ? 130 ASN B O   1 
ATOM   981  C CB  . ASN A 1 130 ? 50.13087 -23.35781 18.81901  1.000 233.58355 ? 130 ASN B CB  1 
ATOM   982  C CG  . ASN A 1 130 ? 51.29269 -23.63153 17.86643  1.000 236.91496 ? 130 ASN B CG  1 
ATOM   983  O OD1 . ASN A 1 130 ? 52.25574 -22.86771 17.78887  1.000 238.64164 ? 130 ASN B OD1 1 
ATOM   984  N ND2 . ASN A 1 130 ? 51.19847 -24.73623 17.13342  1.000 239.05183 ? 130 ASN B ND2 1 
ATOM   985  N N   . HIS A 1 131 ? 50.22257 -20.92992 16.49061  1.000 225.94175 ? 131 HIS B N   1 
ATOM   986  C CA  . HIS A 1 131 ? 50.96849 -19.84569 15.86037  1.000 224.06905 ? 131 HIS B CA  1 
ATOM   987  C C   . HIS A 1 131 ? 50.13452 -19.12055 14.80877  1.000 218.64237 ? 131 HIS B C   1 
ATOM   988  O O   . HIS A 1 131 ? 50.69541 -18.52268 13.88342  1.000 217.81017 ? 131 HIS B O   1 
ATOM   989  C CB  . HIS A 1 131 ? 52.27613 -20.35758 15.24882  1.000 227.27814 ? 131 HIS B CB  1 
ATOM   990  C CG  . HIS A 1 131 ? 52.13935 -21.65786 14.52132  1.000 228.93038 ? 131 HIS B CG  1 
ATOM   991  N ND1 . HIS A 1 131 ? 52.55874 -22.85803 15.05257  1.000 234.40092 ? 131 HIS B ND1 1 
ATOM   992  C CD2 . HIS A 1 131 ? 51.64544 -21.94200 13.29367  1.000 227.64611 ? 131 HIS B CD2 1 
ATOM   993  C CE1 . HIS A 1 131 ? 52.31856 -23.82808 14.18807  1.000 235.28924 ? 131 HIS B CE1 1 
ATOM   994  N NE2 . HIS A 1 131 ? 51.76415 -23.29844 13.11299  1.000 231.28766 ? 131 HIS B NE2 1 
ATOM   995  N N   . LEU A 1 132 ? 48.80871 -19.17371 14.93213  1.000 206.60325 ? 132 LEU B N   1 
ATOM   996  C CA  . LEU A 1 132 ? 47.93314 -18.35649 14.10276  1.000 202.44498 ? 132 LEU B CA  1 
ATOM   997  C C   . LEU A 1 132 ? 48.23450 -16.87886 14.31838  1.000 202.12083 ? 132 LEU B C   1 
ATOM   998  O O   . LEU A 1 132 ? 48.54934 -16.44761 15.43106  1.000 204.91081 ? 132 LEU B O   1 
ATOM   999  C CB  . LEU A 1 132 ? 46.46731 -18.64180 14.44186  1.000 200.38848 ? 132 LEU B CB  1 
ATOM   1000 C CG  . LEU A 1 132 ? 45.58333 -19.36551 13.42319  1.000 198.76386 ? 132 LEU B CG  1 
ATOM   1001 C CD1 . LEU A 1 132 ? 44.11434 -19.09344 13.70182  1.000 195.88670 ? 132 LEU B CD1 1 
ATOM   1002 C CD2 . LEU A 1 132 ? 45.93973 -18.95730 12.01188  1.000 198.29225 ? 132 LEU B CD2 1 
ATOM   1003 N N   . THR A 1 133 ? 48.13983 -16.09845 13.24393  1.000 193.03025 ? 133 THR B N   1 
ATOM   1004 C CA  . THR A 1 133 ? 48.35075 -14.65230 13.31489  1.000 192.88996 ? 133 THR B CA  1 
ATOM   1005 C C   . THR A 1 133 ? 47.24306 -13.98667 12.50466  1.000 189.60529 ? 133 THR B C   1 
ATOM   1006 O O   . THR A 1 133 ? 47.35082 -13.85895 11.28143  1.000 188.70973 ? 133 THR B O   1 
ATOM   1007 C CB  . THR A 1 133 ? 49.73238 -14.25713 12.80453  1.000 195.33465 ? 133 THR B CB  1 
ATOM   1008 O OG1 . THR A 1 133 ? 50.08025 -15.07004 11.67673  1.000 195.96215 ? 133 THR B OG1 1 
ATOM   1009 C CG2 . THR A 1 133 ? 50.77944 -14.43257 13.90146  1.000 199.90632 ? 133 THR B CG2 1 
ATOM   1010 N N   . TYR A 1 134 ? 46.18157 -13.57156 13.19107  1.000 194.64190 ? 134 TYR B N   1 
ATOM   1011 C CA  . TYR A 1 134 ? 45.05768 -12.93108 12.52528  1.000 191.64173 ? 134 TYR B CA  1 
ATOM   1012 C C   . TYR A 1 134 ? 45.45698 -11.56705 11.97245  1.000 191.41452 ? 134 TYR B C   1 
ATOM   1013 O O   . TYR A 1 134 ? 46.33803 -10.88582 12.50287  1.000 193.31814 ? 134 TYR B O   1 
ATOM   1014 C CB  . TYR A 1 134 ? 43.88353 -12.76020 13.49046  1.000 189.84937 ? 134 TYR B CB  1 
ATOM   1015 C CG  . TYR A 1 134 ? 43.47197 -14.01136 14.23287  1.000 190.17703 ? 134 TYR B CG  1 
ATOM   1016 C CD1 . TYR A 1 134 ? 42.73178 -14.99964 13.60497  1.000 188.55843 ? 134 TYR B CD1 1 
ATOM   1017 C CD2 . TYR A 1 134 ? 43.81869 -14.20072 15.56368  1.000 193.23542 ? 134 TYR B CD2 1 
ATOM   1018 C CE1 . TYR A 1 134 ? 42.34676 -16.14317 14.27398  1.000 189.12995 ? 134 TYR B CE1 1 
ATOM   1019 C CE2 . TYR A 1 134 ? 43.43974 -15.34446 16.24456  1.000 193.63962 ? 134 TYR B CE2 1 
ATOM   1020 C CZ  . TYR A 1 134 ? 42.70336 -16.31264 15.59308  1.000 191.22947 ? 134 TYR B CZ  1 
ATOM   1021 O OH  . TYR A 1 134 ? 42.32100 -17.45414 16.26029  1.000 192.25503 ? 134 TYR B OH  1 
ATOM   1022 N N   . ALA A 1 135 ? 44.79090 -11.17244 10.89073  1.000 192.11137 ? 135 ALA B N   1 
ATOM   1023 C CA  . ALA A 1 135 ? 44.90191 -9.83073  10.33292  1.000 192.54686 ? 135 ALA B CA  1 
ATOM   1024 C C   . ALA A 1 135 ? 43.49549 -9.34870  10.02310  1.000 191.88098 ? 135 ALA B C   1 
ATOM   1025 O O   . ALA A 1 135 ? 42.76464 -10.01022 9.28046   1.000 191.93226 ? 135 ALA B O   1 
ATOM   1026 C CB  . ALA A 1 135 ? 45.77484 -9.81199  9.07566   1.000 194.17867 ? 135 ALA B CB  1 
ATOM   1027 N N   . VAL A 1 136 ? 43.11049 -8.21348  10.59917  1.000 203.05147 ? 136 VAL B N   1 
ATOM   1028 C CA  . VAL A 1 136 ? 41.75118 -7.69840  10.49013  1.000 202.88253 ? 136 VAL B CA  1 
ATOM   1029 C C   . VAL A 1 136 ? 41.80837 -6.40899  9.68377   1.000 206.83462 ? 136 VAL B C   1 
ATOM   1030 O O   . VAL A 1 136 ? 42.56768 -5.49309  10.02297  1.000 208.06187 ? 136 VAL B O   1 
ATOM   1031 C CB  . VAL A 1 136 ? 41.12682 -7.44344  11.87410  1.000 201.73569 ? 136 VAL B CB  1 
ATOM   1032 C CG1 . VAL A 1 136 ? 39.64756 -7.11570  11.73616  1.000 203.24312 ? 136 VAL B CG1 1 
ATOM   1033 C CG2 . VAL A 1 136 ? 41.37027 -8.60640  12.81272  1.000 200.25151 ? 136 VAL B CG2 1 
ATOM   1034 N N   . ASN A 1 137 ? 41.00767 -6.33137  8.62579   1.000 217.82179 ? 137 ASN B N   1 
ATOM   1035 C CA  . ASN A 1 137 ? 40.94195 -5.14040  7.78854   1.000 223.03441 ? 137 ASN B CA  1 
ATOM   1036 C C   . ASN A 1 137 ? 39.69616 -4.35314  8.17391   1.000 226.42516 ? 137 ASN B C   1 
ATOM   1037 O O   . ASN A 1 137 ? 38.58138 -4.87582  8.09033   1.000 227.44496 ? 137 ASN B O   1 
ATOM   1038 C CB  . ASN A 1 137 ? 40.91188 -5.51070  6.30344   1.000 226.44728 ? 137 ASN B CB  1 
ATOM   1039 C CG  . ASN A 1 137 ? 40.70281 -4.30300  5.39251   1.000 232.98728 ? 137 ASN B CG  1 
ATOM   1040 O OD1 . ASN A 1 137 ? 40.77927 -3.15267  5.82710   1.000 234.07146 ? 137 ASN B OD1 1 
ATOM   1041 N ND2 . ASN A 1 137 ? 40.43725 -4.56710  4.11825   1.000 237.44926 ? 137 ASN B ND2 1 
ATOM   1042 N N   . ILE A 1 138 ? 39.88691 -3.10823  8.60282   1.000 218.53749 ? 138 ILE B N   1 
ATOM   1043 C CA  . ILE A 1 138 ? 38.78766 -2.19542  8.89606   1.000 223.40651 ? 138 ILE B CA  1 
ATOM   1044 C C   . ILE A 1 138 ? 38.82456 -1.09270  7.85026   1.000 230.29553 ? 138 ILE B C   1 
ATOM   1045 O O   . ILE A 1 138 ? 39.73502 -0.25502  7.84640   1.000 230.58346 ? 138 ILE B O   1 
ATOM   1046 C CB  . ILE A 1 138 ? 38.86097 -1.61037  10.31453  1.000 222.28229 ? 138 ILE B CB  1 
ATOM   1047 C CG1 . ILE A 1 138 ? 38.38600 -2.62038  11.35880  1.000 218.00070 ? 138 ILE B CG1 1 
ATOM   1048 C CG2 . ILE A 1 138 ? 38.00305 -0.35552  10.42143  1.000 229.63116 ? 138 ILE B CG2 1 
ATOM   1049 C CD1 . ILE A 1 138 ? 39.35515 -3.71294  11.64700  1.000 212.66009 ? 138 ILE B CD1 1 
ATOM   1050 N N   . TRP A 1 139 ? 37.84517 -1.10090  6.95400   1.000 235.17554 ? 139 TRP B N   1 
ATOM   1051 C CA  . TRP A 1 139 ? 37.66326 -0.04544  5.97226   1.000 242.06294 ? 139 TRP B CA  1 
ATOM   1052 C C   . TRP A 1 139 ? 36.28743 0.56832   6.16778   1.000 248.50734 ? 139 TRP B C   1 
ATOM   1053 O O   . TRP A 1 139 ? 35.32136 -0.13743  6.47376   1.000 247.92100 ? 139 TRP B O   1 
ATOM   1054 C CB  . TRP A 1 139 ? 37.79394 -0.56750  4.53954   1.000 242.52634 ? 139 TRP B CB  1 
ATOM   1055 C CG  . TRP A 1 139 ? 36.68359 -1.48523  4.15979   1.000 242.44512 ? 139 TRP B CG  1 
ATOM   1056 C CD1 . TRP A 1 139 ? 35.60284 -1.18972  3.38153   1.000 247.35751 ? 139 TRP B CD1 1 
ATOM   1057 C CD2 . TRP A 1 139 ? 36.53382 -2.85058  4.55392   1.000 236.64282 ? 139 TRP B CD2 1 
ATOM   1058 N NE1 . TRP A 1 139 ? 34.78974 -2.29040  3.26554   1.000 245.37488 ? 139 TRP B NE1 1 
ATOM   1059 C CE2 . TRP A 1 139 ? 35.34274 -3.32493  3.97340   1.000 238.52754 ? 139 TRP B CE2 1 
ATOM   1060 C CE3 . TRP A 1 139 ? 37.29483 -3.72067  5.33784   1.000 230.24451 ? 139 TRP B CE3 1 
ATOM   1061 C CZ2 . TRP A 1 139 ? 34.89383 -4.62929  4.15613   1.000 234.52562 ? 139 TRP B CZ2 1 
ATOM   1062 C CZ3 . TRP A 1 139 ? 36.84846 -5.01035  5.51691   1.000 225.84755 ? 139 TRP B CZ3 1 
ATOM   1063 C CH2 . TRP A 1 139 ? 35.66056 -5.45542  4.92731   1.000 228.13767 ? 139 TRP B CH2 1 
ATOM   1064 N N   . SER A 1 140 ? 36.19988 1.88156   5.99473   1.000 253.00734 ? 140 SER B N   1 
ATOM   1065 C CA  . SER A 1 140 ? 34.92404 2.55671   6.16982   1.000 260.29802 ? 140 SER B CA  1 
ATOM   1066 C C   . SER A 1 140 ? 34.00730 2.26541   4.98950   1.000 264.68788 ? 140 SER B C   1 
ATOM   1067 O O   . SER A 1 140 ? 34.39761 2.42772   3.82928   1.000 266.37271 ? 140 SER B O   1 
ATOM   1068 C CB  . SER A 1 140 ? 35.13105 4.06032   6.32886   1.000 265.69647 ? 140 SER B CB  1 
ATOM   1069 O OG  . SER A 1 140 ? 33.92547 4.76024   6.08454   1.000 274.97485 ? 140 SER B OG  1 
ATOM   1070 N N   . GLU A 1 141 ? 32.78755 1.81338   5.28937   1.000 258.50417 ? 141 GLU B N   1 
ATOM   1071 C CA  . GLU A 1 141 ? 31.79611 1.62890   4.23568   1.000 263.62249 ? 141 GLU B CA  1 
ATOM   1072 C C   . GLU A 1 141 ? 31.40363 2.96877   3.62690   1.000 272.99638 ? 141 GLU B C   1 
ATOM   1073 O O   . GLU A 1 141 ? 31.17054 3.06441   2.41628   1.000 277.38858 ? 141 GLU B O   1 
ATOM   1074 C CB  . GLU A 1 141 ? 30.57336 0.89347   4.79112   1.000 262.81764 ? 141 GLU B CB  1 
ATOM   1075 C CG  . GLU A 1 141 ? 29.49917 0.54615   3.76305   1.000 265.99356 ? 141 GLU B CG  1 
ATOM   1076 C CD  . GLU A 1 141 ? 28.56442 1.70277   3.45292   1.000 276.38563 ? 141 GLU B CD  1 
ATOM   1077 O OE1 . GLU A 1 141 ? 28.39638 2.58703   4.31925   1.000 281.32046 ? 141 GLU B OE1 1 
ATOM   1078 O OE2 . GLU A 1 141 ? 28.00067 1.72739   2.33970   1.000 280.47191 ? 141 GLU B OE2 1 
ATOM   1079 N N   . ASN A 1 142 ? 31.33463 4.01672   4.45189   1.000 264.32788 ? 142 ASN B N   1 
ATOM   1080 C CA  . ASN A 1 142 ? 31.05017 5.35096   3.93502   1.000 273.92287 ? 142 ASN B CA  1 
ATOM   1081 C C   . ASN A 1 142 ? 32.27037 5.93914   3.23620   1.000 274.20517 ? 142 ASN B C   1 
ATOM   1082 O O   . ASN A 1 142 ? 32.14110 6.58794   2.19152   1.000 281.27581 ? 142 ASN B O   1 
ATOM   1083 C CB  . ASN A 1 142 ? 30.58410 6.26230   5.07224   1.000 279.00217 ? 142 ASN B CB  1 
ATOM   1084 C CG  . ASN A 1 142 ? 30.51262 7.72298   4.66556   1.000 288.66217 ? 142 ASN B CG  1 
ATOM   1085 O OD1 . ASN A 1 142 ? 30.92421 8.60680   5.41736   1.000 290.71889 ? 142 ASN B OD1 1 
ATOM   1086 N ND2 . ASN A 1 142 ? 29.97135 7.98519   3.48101   1.000 295.12817 ? 142 ASN B ND2 1 
ATOM   1087 N N   . ASP A 1 143 ? 33.46340 5.72301   3.79652   1.000 279.58771 ? 143 ASP B N   1 
ATOM   1088 C CA  . ASP A 1 143 ? 34.71713 6.20691   3.22300   1.000 278.83562 ? 143 ASP B CA  1 
ATOM   1089 C C   . ASP A 1 143 ? 35.55485 5.02551   2.74846   1.000 271.34369 ? 143 ASP B C   1 
ATOM   1090 O O   . ASP A 1 143 ? 36.33560 4.45750   3.52586   1.000 264.43435 ? 143 ASP B O   1 
ATOM   1091 C CB  . ASP A 1 143 ? 35.49825 7.04644   4.23872   1.000 278.13639 ? 143 ASP B CB  1 
ATOM   1092 C CG  . ASP A 1 143 ? 34.72426 8.26101   4.71882   1.000 286.65785 ? 143 ASP B CG  1 
ATOM   1093 O OD1 . ASP A 1 143 ? 33.63961 8.53855   4.16611   1.000 293.36797 ? 143 ASP B OD1 1 
ATOM   1094 O OD2 . ASP A 1 143 ? 35.20772 8.94505   5.64646   1.000 287.34326 ? 143 ASP B OD2 1 
ATOM   1095 N N   . PRO A 1 144 ? 35.43506 4.61667   1.48362   1.000 260.14072 ? 144 PRO B N   1 
ATOM   1096 C CA  . PRO A 1 144 ? 36.32056 3.55584   0.97348   1.000 254.17489 ? 144 PRO B CA  1 
ATOM   1097 C C   . PRO A 1 144 ? 37.79430 3.91231   1.05472   1.000 251.31730 ? 144 PRO B C   1 
ATOM   1098 O O   . PRO A 1 144 ? 38.63750 3.00983   1.13460   1.000 245.34315 ? 144 PRO B O   1 
ATOM   1099 C CB  . PRO A 1 144 ? 35.85864 3.38503   -0.48066  1.000 259.89033 ? 144 PRO B CB  1 
ATOM   1100 C CG  . PRO A 1 144 ? 35.10198 4.64092   -0.79856  1.000 268.74241 ? 144 PRO B CG  1 
ATOM   1101 C CD  . PRO A 1 144 ? 34.45964 5.05850   0.47582   1.000 268.70830 ? 144 PRO B CD  1 
ATOM   1102 N N   . ALA A 1 145 ? 38.12888 5.20593   1.03881   1.000 245.82383 ? 145 ALA B N   1 
ATOM   1103 C CA  . ALA A 1 145 ? 39.51664 5.62096   1.21494   1.000 246.97925 ? 145 ALA B CA  1 
ATOM   1104 C C   . ALA A 1 145 ? 40.04158 5.25727   2.59595   1.000 237.77392 ? 145 ALA B C   1 
ATOM   1105 O O   . ALA A 1 145 ? 41.24489 5.02943   2.76205   1.000 235.43667 ? 145 ALA B O   1 
ATOM   1106 C CB  . ALA A 1 145 ? 39.64901 7.12663   0.98539   1.000 259.13166 ? 145 ALA B CB  1 
ATOM   1107 N N   . ASP A 1 146 ? 39.16425 5.21024   3.59475   1.000 263.31258 ? 146 ASP B N   1 
ATOM   1108 C CA  . ASP A 1 146 ? 39.55694 4.85480   4.95228   1.000 256.75548 ? 146 ASP B CA  1 
ATOM   1109 C C   . ASP A 1 146 ? 39.65748 3.33926   5.06564   1.000 249.32002 ? 146 ASP B C   1 
ATOM   1110 O O   . ASP A 1 146 ? 38.66272 2.63301   4.87583   1.000 249.31483 ? 146 ASP B O   1 
ATOM   1111 C CB  . ASP A 1 146 ? 38.54609 5.40740   5.95626   1.000 259.59326 ? 146 ASP B CB  1 
ATOM   1112 C CG  . ASP A 1 146 ? 39.16652 5.71711   7.30825   1.000 257.31822 ? 146 ASP B CG  1 
ATOM   1113 O OD1 . ASP A 1 146 ? 40.00514 4.92180   7.78123   1.000 250.93104 ? 146 ASP B OD1 1 
ATOM   1114 O OD2 . ASP A 1 146 ? 38.80607 6.75561   7.90332   1.000 263.21640 ? 146 ASP B OD2 1 
ATOM   1115 N N   . PHE A 1 147 ? 40.85675 2.84194   5.35969   1.000 248.35100 ? 147 PHE B N   1 
ATOM   1116 C CA  . PHE A 1 147 ? 41.07453 1.41420   5.54513   1.000 241.14631 ? 147 PHE B CA  1 
ATOM   1117 C C   . PHE A 1 147 ? 42.29824 1.22488   6.42723   1.000 235.45048 ? 147 PHE B C   1 
ATOM   1118 O O   . PHE A 1 147 ? 43.23919 2.02123   6.38001   1.000 236.98946 ? 147 PHE B O   1 
ATOM   1119 C CB  . PHE A 1 147 ? 41.25942 0.68022   4.21031   1.000 241.33520 ? 147 PHE B CB  1 
ATOM   1120 C CG  . PHE A 1 147 ? 42.42254 1.17672   3.39368   1.000 243.23693 ? 147 PHE B CG  1 
ATOM   1121 C CD1 . PHE A 1 147 ? 43.69328 0.64920   3.57357   1.000 239.79978 ? 147 PHE B CD1 1 
ATOM   1122 C CD2 . PHE A 1 147 ? 42.24433 2.16489   2.44128   1.000 249.51726 ? 147 PHE B CD2 1 
ATOM   1123 C CE1 . PHE A 1 147 ? 44.76167 1.10357   2.82231   1.000 243.44437 ? 147 PHE B CE1 1 
ATOM   1124 C CE2 . PHE A 1 147 ? 43.30899 2.62387   1.68711   1.000 251.70590 ? 147 PHE B CE2 1 
ATOM   1125 C CZ  . PHE A 1 147 ? 44.56860 2.09192   1.87767   1.000 249.54039 ? 147 PHE B CZ  1 
ATOM   1126 N N   . ARG A 1 148 ? 42.27707 0.16126   7.22827   1.000 240.63697 ? 148 ARG B N   1 
ATOM   1127 C CA  . ARG A 1 148 ? 43.34648 -0.10648  8.18014   1.000 235.85953 ? 148 ARG B CA  1 
ATOM   1128 C C   . ARG A 1 148 ? 43.47197 -1.61141  8.37500   1.000 230.12615 ? 148 ARG B C   1 
ATOM   1129 O O   . ARG A 1 148 ? 42.46470 -2.32304  8.39731   1.000 228.02166 ? 148 ARG B O   1 
ATOM   1130 C CB  . ARG A 1 148 ? 43.07428 0.58062   9.52510   1.000 236.08959 ? 148 ARG B CB  1 
ATOM   1131 C CG  . ARG A 1 148 ? 43.10471 2.09818   9.48713   1.000 242.43582 ? 148 ARG B CG  1 
ATOM   1132 C CD  . ARG A 1 148 ? 42.83703 2.70440   10.85012  1.000 243.37110 ? 148 ARG B CD  1 
ATOM   1133 N NE  . ARG A 1 148 ? 42.78049 4.15939   10.77817  1.000 250.35453 ? 148 ARG B NE  1 
ATOM   1134 C CZ  . ARG A 1 148 ? 42.43678 4.94920   11.78612  1.000 254.22270 ? 148 ARG B CZ  1 
ATOM   1135 N NH1 . ARG A 1 148 ? 42.10233 4.45664   12.96752  1.000 250.86300 ? 148 ARG B NH1 1 
ATOM   1136 N NH2 . ARG A 1 148 ? 42.42163 6.26648   11.60191  1.000 261.87198 ? 148 ARG B NH2 1 
ATOM   1137 N N   . ILE A 1 149 ? 44.70923 -2.08806  8.51657   1.000 226.60876 ? 149 ILE B N   1 
ATOM   1138 C CA  . ILE A 1 149 ? 45.00288 -3.49728  8.76676   1.000 222.88001 ? 149 ILE B CA  1 
ATOM   1139 C C   . ILE A 1 149 ? 45.42104 -3.65113  10.22324  1.000 220.20312 ? 149 ILE B C   1 
ATOM   1140 O O   . ILE A 1 149 ? 46.22775 -2.86387  10.73048  1.000 222.14241 ? 149 ILE B O   1 
ATOM   1141 C CB  . ILE A 1 149 ? 46.10700 -4.02506  7.82890   1.000 224.34196 ? 149 ILE B CB  1 
ATOM   1142 C CG1 . ILE A 1 149 ? 45.58333 -4.17918  6.40319   1.000 226.54904 ? 149 ILE B CG1 1 
ATOM   1143 C CG2 . ILE A 1 149 ? 46.61145 -5.36933  8.31515   1.000 221.58925 ? 149 ILE B CG2 1 
ATOM   1144 C CD1 . ILE A 1 149 ? 44.39344 -5.08940  6.29607   1.000 225.73552 ? 149 ILE B CD1 1 
ATOM   1145 N N   . TYR A 1 150 ? 44.87579 -4.66618  10.89616  1.000 218.42297 ? 150 TYR B N   1 
ATOM   1146 C CA  . TYR A 1 150 ? 45.14106 -4.90384  12.31389  1.000 216.88995 ? 150 TYR B CA  1 
ATOM   1147 C C   . TYR A 1 150 ? 45.72124 -6.30360  12.47797  1.000 215.85422 ? 150 TYR B C   1 
ATOM   1148 O O   . TYR A 1 150 ? 45.03836 -7.29774  12.21199  1.000 213.77116 ? 150 TYR B O   1 
ATOM   1149 C CB  . TYR A 1 150 ? 43.87552 -4.74706  13.16320  1.000 215.25518 ? 150 TYR B CB  1 
ATOM   1150 C CG  . TYR A 1 150 ? 43.21135 -3.38218  13.11154  1.000 217.02244 ? 150 TYR B CG  1 
ATOM   1151 C CD1 . TYR A 1 150 ? 42.74017 -2.85568  11.91722  1.000 218.91928 ? 150 TYR B CD1 1 
ATOM   1152 C CD2 . TYR A 1 150 ? 43.06548 -2.61648  14.26265  1.000 219.33561 ? 150 TYR B CD2 1 
ATOM   1153 C CE1 . TYR A 1 150 ? 42.13842 -1.61758  11.86937  1.000 222.96110 ? 150 TYR B CE1 1 
ATOM   1154 C CE2 . TYR A 1 150 ? 42.46280 -1.36955  14.22273  1.000 221.79754 ? 150 TYR B CE2 1 
ATOM   1155 C CZ  . TYR A 1 150 ? 42.00257 -0.87572  13.02027  1.000 224.56420 ? 150 TYR B CZ  1 
ATOM   1156 O OH  . TYR A 1 150 ? 41.40172 0.36145   12.95699  1.000 230.03519 ? 150 TYR B OH  1 
ATOM   1157 N N   . ASN A 1 151 ? 46.97139 -6.38092  12.92880  1.000 199.86816 ? 151 ASN B N   1 
ATOM   1158 C CA  . ASN A 1 151 ? 47.60570 -7.66438  13.19638  1.000 200.84651 ? 151 ASN B CA  1 
ATOM   1159 C C   . ASN A 1 151 ? 47.15258 -8.20067  14.54775  1.000 201.60175 ? 151 ASN B C   1 
ATOM   1160 O O   . ASN A 1 151 ? 47.18476 -7.48582  15.55356  1.000 203.44821 ? 151 ASN B O   1 
ATOM   1161 C CB  . ASN A 1 151 ? 49.12780 -7.53435  13.17090  1.000 204.40198 ? 151 ASN B CB  1 
ATOM   1162 C CG  . ASN A 1 151 ? 49.65825 -7.05423  11.83425  1.000 205.26898 ? 151 ASN B CG  1 
ATOM   1163 O OD1 . ASN A 1 151 ? 50.30639 -7.81159  11.11067  1.000 206.71941 ? 151 ASN B OD1 1 
ATOM   1164 N ND2 . ASN A 1 151 ? 49.39496 -5.79119  11.50363  1.000 204.40785 ? 151 ASN B ND2 1 
ATOM   1165 N N   . VAL A 1 152 ? 46.72112 -9.46124  14.56674  1.000 195.16266 ? 152 VAL B N   1 
ATOM   1166 C CA  . VAL A 1 152 ? 46.28859 -10.13022 15.78480  1.000 196.99568 ? 152 VAL B CA  1 
ATOM   1167 C C   . VAL A 1 152 ? 46.96951 -11.49030 15.83711  1.000 200.40137 ? 152 VAL B C   1 
ATOM   1168 O O   . VAL A 1 152 ? 47.39209 -12.03835 14.81767  1.000 199.22928 ? 152 VAL B O   1 
ATOM   1169 C CB  . VAL A 1 152 ? 44.75038 -10.29128 15.85736  1.000 193.35657 ? 152 VAL B CB  1 
ATOM   1170 C CG1 . VAL A 1 152 ? 44.30108 -10.67106 17.26525  1.000 196.16132 ? 152 VAL B CG1 1 
ATOM   1171 C CG2 . VAL A 1 152 ? 44.05026 -9.02317  15.39544  1.000 190.11742 ? 152 VAL B CG2 1 
ATOM   1172 N N   . THR A 1 153 ? 47.08238 -12.02922 17.04935  1.000 203.79424 ? 153 THR B N   1 
ATOM   1173 C CA  . THR A 1 153 ? 47.62103 -13.36943 17.23423  1.000 205.17621 ? 153 THR B CA  1 
ATOM   1174 C C   . THR A 1 153 ? 47.19616 -13.93597 18.58087  1.000 207.21136 ? 153 THR B C   1 
ATOM   1175 O O   . THR A 1 153 ? 47.56684 -15.06131 18.93103  1.000 209.10237 ? 153 THR B O   1 
ATOM   1176 C CB  . THR A 1 153 ? 49.14524 -13.36168 17.12844  1.000 209.29176 ? 153 THR B CB  1 
ATOM   1177 O OG1 . THR A 1 153 ? 49.63075 -14.70951 17.16061  1.000 209.70905 ? 153 THR B OG1 1 
ATOM   1178 C CG2 . THR A 1 153 ? 49.74697 -12.58228 18.28545  1.000 215.07475 ? 153 THR B CG2 1 
ATOM   1179 N N   . TYR A 1 154 ? 46.42781 -13.15902 19.34117  1.000 204.90260 ? 154 TYR B N   1 
ATOM   1180 C CA  . TYR A 1 154 ? 45.96162 -13.61103 20.64374  1.000 208.16667 ? 154 TYR B CA  1 
ATOM   1181 C C   . TYR A 1 154 ? 45.13153 -14.88100 20.50909  1.000 206.47011 ? 154 TYR B C   1 
ATOM   1182 O O   . TYR A 1 154 ? 44.44049 -15.09780 19.50955  1.000 201.78996 ? 154 TYR B O   1 
ATOM   1183 C CB  . TYR A 1 154 ? 45.13938 -12.51910 21.32575  1.000 208.40335 ? 154 TYR B CB  1 
ATOM   1184 C CG  . TYR A 1 154 ? 45.92846 -11.27650 21.65839  1.000 209.39013 ? 154 TYR B CG  1 
ATOM   1185 C CD1 . TYR A 1 154 ? 47.21219 -11.36622 22.18018  1.000 214.17096 ? 154 TYR B CD1 1 
ATOM   1186 C CD2 . TYR A 1 154 ? 45.38969 -10.01394 21.45605  1.000 205.70160 ? 154 TYR B CD2 1 
ATOM   1187 C CE1 . TYR A 1 154 ? 47.93732 -10.23229 22.49057  1.000 216.26404 ? 154 TYR B CE1 1 
ATOM   1188 C CE2 . TYR A 1 154 ? 46.10703 -8.87410  21.76273  1.000 207.60179 ? 154 TYR B CE2 1 
ATOM   1189 C CZ  . TYR A 1 154 ? 47.37973 -8.98903  22.27949  1.000 213.18683 ? 154 TYR B CZ  1 
ATOM   1190 O OH  . TYR A 1 154 ? 48.09637 -7.85573  22.58576  1.000 215.09735 ? 154 TYR B OH  1 
ATOM   1191 N N   . LEU A 1 155 ? 45.21354 -15.73082 21.53544  1.000 200.31319 ? 155 LEU B N   1 
ATOM   1192 C CA  . LEU A 1 155 ? 44.48896 -16.99528 21.50211  1.000 198.84463 ? 155 LEU B CA  1 
ATOM   1193 C C   . LEU A 1 155 ? 42.98800 -16.75136 21.43183  1.000 195.76710 ? 155 LEU B C   1 
ATOM   1194 O O   . LEU A 1 155 ? 42.25617 -17.50546 20.77908  1.000 191.58075 ? 155 LEU B O   1 
ATOM   1195 C CB  . LEU A 1 155 ? 44.84154 -17.84243 22.72592  1.000 205.78589 ? 155 LEU B CB  1 
ATOM   1196 C CG  . LEU A 1 155 ? 46.18282 -18.59143 22.77487  1.000 210.12398 ? 155 LEU B CG  1 
ATOM   1197 C CD1 . LEU A 1 155 ? 46.26346 -19.67931 21.70981  1.000 205.96812 ? 155 LEU B CD1 1 
ATOM   1198 C CD2 . LEU A 1 155 ? 47.39360 -17.66052 22.69303  1.000 211.79760 ? 155 LEU B CD2 1 
ATOM   1199 N N   . GLU A 1 156 ? 42.51645 -15.70464 22.10005  1.000 216.65786 ? 156 GLU B N   1 
ATOM   1200 C CA  . GLU A 1 156 ? 41.14474 -15.24790 21.93483  1.000 213.74599 ? 156 GLU B CA  1 
ATOM   1201 C C   . GLU A 1 156 ? 41.03253 -14.42807 20.65643  1.000 207.01290 ? 156 GLU B C   1 
ATOM   1202 O O   . GLU A 1 156 ? 41.65122 -13.36240 20.56080  1.000 207.83013 ? 156 GLU B O   1 
ATOM   1203 C CB  . GLU A 1 156 ? 40.70800 -14.41180 23.13076  1.000 221.86373 ? 156 GLU B CB  1 
ATOM   1204 C CG  . GLU A 1 156 ? 39.25991 -13.93306 23.07262  1.000 219.57910 ? 156 GLU B CG  1 
ATOM   1205 C CD  . GLU A 1 156 ? 38.24590 -15.06226 23.15852  1.000 218.06454 ? 156 GLU B CD  1 
ATOM   1206 O OE1 . GLU A 1 156 ? 38.62790 -16.19410 23.52491  1.000 220.54195 ? 156 GLU B OE1 1 
ATOM   1207 O OE2 . GLU A 1 156 ? 37.05863 -14.80974 22.86463  1.000 214.28813 ? 156 GLU B OE2 1 
ATOM   1208 N N   . PRO A 1 157 ? 40.27324 -14.87663 19.66375  1.000 209.56776 ? 157 PRO B N   1 
ATOM   1209 C CA  . PRO A 1 157 ? 40.19626 -14.15946 18.37320  1.000 204.39916 ? 157 PRO B CA  1 
ATOM   1210 C C   . PRO A 1 157 ? 39.31237 -12.91444 18.43660  1.000 202.33057 ? 157 PRO B C   1 
ATOM   1211 O O   . PRO A 1 157 ? 38.13754 -12.90630 18.06953  1.000 200.06982 ? 157 PRO B O   1 
ATOM   1212 C CB  . PRO A 1 157 ? 39.62053 -15.22316 17.43230  1.000 200.91073 ? 157 PRO B CB  1 
ATOM   1213 C CG  . PRO A 1 157 ? 39.66291 -16.53291 18.19869  1.000 203.19436 ? 157 PRO B CG  1 
ATOM   1214 C CD  . PRO A 1 157 ? 39.53345 -16.14519 19.62560  1.000 208.02422 ? 157 PRO B CD  1 
ATOM   1215 N N   . SER A 1 158 ? 39.89389 -11.81398 18.91002  1.000 218.54077 ? 158 SER B N   1 
ATOM   1216 C CA  . SER A 1 158 ? 39.14503 -10.57578 19.08501  1.000 217.27451 ? 158 SER B CA  1 
ATOM   1217 C C   . SER A 1 158 ? 40.10887 -9.39612  19.02096  1.000 217.62543 ? 158 SER B C   1 
ATOM   1218 O O   . SER A 1 158 ? 41.32930 -9.55640  19.10601  1.000 219.17284 ? 158 SER B O   1 
ATOM   1219 C CB  . SER A 1 158 ? 38.35919 -10.58428 20.40194  1.000 221.21894 ? 158 SER B CB  1 
ATOM   1220 O OG  . SER A 1 158 ? 38.16403 -9.27052  20.89594  1.000 224.16922 ? 158 SER B OG  1 
ATOM   1221 N N   . LEU A 1 159 ? 39.53537 -8.20019  18.88185  1.000 212.58554 ? 159 LEU B N   1 
ATOM   1222 C CA  . LEU A 1 159 ? 40.30296 -6.97195  18.72307  1.000 212.82533 ? 159 LEU B CA  1 
ATOM   1223 C C   . LEU A 1 159 ? 39.53314 -5.81299  19.34276  1.000 214.95036 ? 159 LEU B C   1 
ATOM   1224 O O   . LEU A 1 159 ? 38.29992 -5.78308  19.31027  1.000 214.75927 ? 159 LEU B O   1 
ATOM   1225 C CB  . LEU A 1 159 ? 40.59576 -6.68935  17.24314  1.000 209.50194 ? 159 LEU B CB  1 
ATOM   1226 C CG  . LEU A 1 159 ? 40.98420 -5.26384  16.84284  1.000 210.84215 ? 159 LEU B CG  1 
ATOM   1227 C CD1 . LEU A 1 159 ? 42.40342 -4.93564  17.29447  1.000 213.01753 ? 159 LEU B CD1 1 
ATOM   1228 C CD2 . LEU A 1 159 ? 40.82910 -5.07341  15.34536  1.000 209.63672 ? 159 LEU B CD2 1 
ATOM   1229 N N   . ARG A 1 160 ? 40.27213 -4.85520  19.90581  1.000 211.03222 ? 160 ARG B N   1 
ATOM   1230 C CA  . ARG A 1 160 ? 39.68362 -3.67839  20.53349  1.000 214.27028 ? 160 ARG B CA  1 
ATOM   1231 C C   . ARG A 1 160 ? 40.34123 -2.41722  19.99390  1.000 215.16024 ? 160 ARG B C   1 
ATOM   1232 O O   . ARG A 1 160 ? 41.56917 -2.35187  19.87671  1.000 214.90737 ? 160 ARG B O   1 
ATOM   1233 C CB  . ARG A 1 160 ? 39.81669 -3.74252  22.05929  1.000 218.75963 ? 160 ARG B CB  1 
ATOM   1234 C CG  . ARG A 1 160 ? 38.98123 -4.85023  22.66262  1.000 220.62013 ? 160 ARG B CG  1 
ATOM   1235 C CD  . ARG A 1 160 ? 39.04250 -4.91416  24.17583  1.000 227.52837 ? 160 ARG B CD  1 
ATOM   1236 N NE  . ARG A 1 160 ? 38.26621 -6.05016  24.66002  1.000 230.23497 ? 160 ARG B NE  1 
ATOM   1237 C CZ  . ARG A 1 160 ? 38.21371 -6.45060  25.92273  1.000 236.68671 ? 160 ARG B CZ  1 
ATOM   1238 N NH1 . ARG A 1 160 ? 38.88654 -5.82643  26.87522  1.000 242.09244 ? 160 ARG B NH1 1 
ATOM   1239 N NH2 . ARG A 1 160 ? 37.46455 -7.50367  26.23775  1.000 238.44803 ? 160 ARG B NH2 1 
ATOM   1240 N N   . ILE A 1 161 ? 39.51702 -1.42062  19.66951  1.000 213.86359 ? 161 ILE B N   1 
ATOM   1241 C CA  . ILE A 1 161 ? 39.98554 -0.14119  19.15077  1.000 216.65725 ? 161 ILE B CA  1 
ATOM   1242 C C   . ILE A 1 161 ? 39.01803 0.93669   19.62119  1.000 221.91962 ? 161 ILE B C   1 
ATOM   1243 O O   . ILE A 1 161 ? 37.84812 0.66390   19.90204  1.000 222.81157 ? 161 ILE B O   1 
ATOM   1244 C CB  . ILE A 1 161 ? 40.10658 -0.16418  17.60638  1.000 214.91985 ? 161 ILE B CB  1 
ATOM   1245 C CG1 . ILE A 1 161 ? 40.86451 1.06498   17.09491  1.000 218.92694 ? 161 ILE B CG1 1 
ATOM   1246 C CG2 . ILE A 1 161 ? 38.73056 -0.25936  16.96103  1.000 214.88639 ? 161 ILE B CG2 1 
ATOM   1247 C CD1 . ILE A 1 161 ? 42.31789 1.10986   17.51662  1.000 218.21164 ? 161 ILE B CD1 1 
ATOM   1248 N N   . ALA A 1 162 ? 39.51720 2.17038   19.72098  1.000 210.48185 ? 162 ALA B N   1 
ATOM   1249 C CA  . ALA A 1 162 ? 38.69750 3.28851   20.17715  1.000 216.87882 ? 162 ALA B CA  1 
ATOM   1250 C C   . ALA A 1 162 ? 39.11874 4.57481   19.47469  1.000 221.87073 ? 162 ALA B C   1 
ATOM   1251 O O   . ALA A 1 162 ? 39.30511 5.61599   20.11367  1.000 227.46998 ? 162 ALA B O   1 
ATOM   1252 C CB  . ALA A 1 162 ? 38.77738 3.45587   21.69627  1.000 218.55857 ? 162 ALA B CB  1 
ATOM   1253 N N   . ALA A 1 163 ? 39.26097 4.51605   18.15264  1.000 201.36011 ? 163 ALA B N   1 
ATOM   1254 C CA  . ALA A 1 163 ? 39.74769 5.64151   17.35504  1.000 208.05926 ? 163 ALA B CA  1 
ATOM   1255 C C   . ALA A 1 163 ? 38.93620 6.91684   17.57440  1.000 216.20620 ? 163 ALA B C   1 
ATOM   1256 O O   . ALA A 1 163 ? 37.70643 6.89301   17.57057  1.000 216.19543 ? 163 ALA B O   1 
ATOM   1257 C CB  . ALA A 1 163 ? 39.74687 5.27066   15.87809  1.000 205.78398 ? 163 ALA B CB  1 
ATOM   1258 N N   . GLY A 1 169 ? 31.65581 9.01534   13.87800  1.000 253.20833 ? 169 GLY B N   1 
ATOM   1259 C CA  . GLY A 1 169 ? 30.85654 9.79395   12.95027  1.000 262.77097 ? 169 GLY B CA  1 
ATOM   1260 C C   . GLY A 1 169 ? 30.74003 9.14295   11.58653  1.000 260.62403 ? 169 GLY B C   1 
ATOM   1261 O O   . GLY A 1 169 ? 29.71410 9.26032   10.91708  1.000 266.01072 ? 169 GLY B O   1 
ATOM   1262 N N   . ILE A 1 170 ? 31.80337 8.45396   11.17427  1.000 286.24238 ? 170 ILE B N   1 
ATOM   1263 C CA  . ILE A 1 170 ? 31.82793 7.74116   9.90168   1.000 283.87605 ? 170 ILE B CA  1 
ATOM   1264 C C   . ILE A 1 170 ? 31.25865 6.34732   10.14781  1.000 279.27579 ? 170 ILE B C   1 
ATOM   1265 O O   . ILE A 1 170 ? 30.94083 5.99655   11.28957  1.000 279.12375 ? 170 ILE B O   1 
ATOM   1266 C CB  . ILE A 1 170 ? 33.25784 7.68763   9.32802   1.000 277.95951 ? 170 ILE B CB  1 
ATOM   1267 C CG1 . ILE A 1 170 ? 33.96142 9.03062   9.52471   1.000 281.94192 ? 170 ILE B CG1 1 
ATOM   1268 C CG2 . ILE A 1 170 ? 33.23725 7.40063   7.84093   1.000 279.18115 ? 170 ILE B CG2 1 
ATOM   1269 C CD1 . ILE A 1 170 ? 35.43619 9.00754   9.16895   1.000 275.65569 ? 170 ILE B CD1 1 
ATOM   1270 N N   . SER A 1 171 ? 31.10679 5.54950   9.09055   1.000 283.19434 ? 171 SER B N   1 
ATOM   1271 C CA  . SER A 1 171 ? 30.64692 4.16987   9.20116   1.000 277.71370 ? 171 SER B CA  1 
ATOM   1272 C C   . SER A 1 171 ? 31.68631 3.23968   8.58937   1.000 269.22472 ? 171 SER B C   1 
ATOM   1273 O O   . SER A 1 171 ? 32.06231 3.40490   7.42406   1.000 269.37925 ? 171 SER B O   1 
ATOM   1274 C CB  . SER A 1 171 ? 29.28204 3.97659   8.52444   1.000 282.73973 ? 171 SER B CB  1 
ATOM   1275 O OG  . SER A 1 171 ? 29.34295 4.22262   7.13142   1.000 286.47535 ? 171 SER B OG  1 
ATOM   1276 N N   . TYR A 1 172 ? 32.13843 2.25940   9.37242   1.000 260.84350 ? 172 TYR B N   1 
ATOM   1277 C CA  . TYR A 1 172 ? 33.23078 1.37627   8.98941   1.000 252.34252 ? 172 TYR B CA  1 
ATOM   1278 C C   . TYR A 1 172 ? 32.74602 -0.06158  8.82700   1.000 246.21436 ? 172 TYR B C   1 
ATOM   1279 O O   . TYR A 1 172 ? 31.70871 -0.45967  9.36489   1.000 246.07919 ? 172 TYR B O   1 
ATOM   1280 C CB  . TYR A 1 172 ? 34.36909 1.42928   10.02444  1.000 246.17058 ? 172 TYR B CB  1 
ATOM   1281 C CG  . TYR A 1 172 ? 35.14607 2.73343   10.03851  1.000 248.61423 ? 172 TYR B CG  1 
ATOM   1282 C CD1 . TYR A 1 172 ? 34.68002 3.83720   10.74236  1.000 253.74055 ? 172 TYR B CD1 1 
ATOM   1283 C CD2 . TYR A 1 172 ? 36.35813 2.85195   9.36759   1.000 245.19943 ? 172 TYR B CD2 1 
ATOM   1284 C CE1 . TYR A 1 172 ? 35.38930 5.02803   10.76296  1.000 255.98349 ? 172 TYR B CE1 1 
ATOM   1285 C CE2 . TYR A 1 172 ? 37.07410 4.03895   9.38274   1.000 248.13008 ? 172 TYR B CE2 1 
ATOM   1286 C CZ  . TYR A 1 172 ? 36.58490 5.12263   10.08271  1.000 253.17031 ? 172 TYR B CZ  1 
ATOM   1287 O OH  . TYR A 1 172 ? 37.29135 6.30416   10.10397  1.000 256.59721 ? 172 TYR B OH  1 
ATOM   1288 N N   . ARG A 1 173 ? 33.51556 -0.83761  8.06776   1.000 246.94551 ? 173 ARG B N   1 
ATOM   1289 C CA  . ARG A 1 173 ? 33.34108 -2.27929  7.93153   1.000 239.72929 ? 173 ARG B CA  1 
ATOM   1290 C C   . ARG A 1 173 ? 34.56347 -2.99042  8.51119   1.000 231.25499 ? 173 ARG B C   1 
ATOM   1291 O O   . ARG A 1 173 ? 35.53745 -2.35613  8.92569   1.000 229.67659 ? 173 ARG B O   1 
ATOM   1292 C CB  . ARG A 1 173 ? 33.13240 -2.67913  6.46871   1.000 242.65403 ? 173 ARG B CB  1 
ATOM   1293 C CG  . ARG A 1 173 ? 31.76482 -2.36574  5.89387   1.000 249.82308 ? 173 ARG B CG  1 
ATOM   1294 C CD  . ARG A 1 173 ? 31.52089 -3.23518  4.67140   1.000 250.71518 ? 173 ARG B CD  1 
ATOM   1295 N NE  . ARG A 1 173 ? 30.85920 -2.53868  3.57631   1.000 259.05447 ? 173 ARG B NE  1 
ATOM   1296 C CZ  . ARG A 1 173 ? 30.99579 -2.87049  2.29970   1.000 260.44801 ? 173 ARG B CZ  1 
ATOM   1297 N NH1 . ARG A 1 173 ? 31.76448 -3.88161  1.92725   1.000 255.73116 ? 173 ARG B NH1 1 
ATOM   1298 N NH2 . ARG A 1 173 ? 30.34604 -2.17146  1.37384   1.000 268.26785 ? 173 ARG B NH2 1 
ATOM   1299 N N   . ALA A 1 174 ? 34.50879 -4.32382  8.53493   1.000 233.15876 ? 174 ALA B N   1 
ATOM   1300 C CA  . ALA A 1 174 ? 35.61433 -5.11950  9.05432   1.000 225.81944 ? 174 ALA B CA  1 
ATOM   1301 C C   . ALA A 1 174 ? 35.52608 -6.54816  8.53574   1.000 222.53456 ? 174 ALA B C   1 
ATOM   1302 O O   . ALA A 1 174 ? 34.43120 -7.09175  8.37409   1.000 223.49368 ? 174 ALA B O   1 
ATOM   1303 C CB  . ALA A 1 174 ? 35.63380 -5.12907  10.58648  1.000 222.04743 ? 174 ALA B CB  1 
ATOM   1304 N N   . ARG A 1 175 ? 36.69179 -7.14758  8.29731   1.000 211.67012 ? 175 ARG B N   1 
ATOM   1305 C CA  . ARG A 1 175 ? 36.80852 -8.53541  7.87164   1.000 209.34587 ? 175 ARG B CA  1 
ATOM   1306 C C   . ARG A 1 175 ? 38.20185 -9.01808  8.25272   1.000 205.09260 ? 175 ARG B C   1 
ATOM   1307 O O   . ARG A 1 175 ? 39.16213 -8.24598  8.20037   1.000 204.73051 ? 175 ARG B O   1 
ATOM   1308 C CB  . ARG A 1 175 ? 36.55138 -8.67596  6.36453   1.000 213.91304 ? 175 ARG B CB  1 
ATOM   1309 C CG  . ARG A 1 175 ? 37.70581 -8.25949  5.47275   1.000 216.34569 ? 175 ARG B CG  1 
ATOM   1310 C CD  . ARG A 1 175 ? 37.43470 -8.60449  4.02155   1.000 219.62941 ? 175 ARG B CD  1 
ATOM   1311 N NE  . ARG A 1 175 ? 37.73262 -7.47619  3.14933   1.000 225.31273 ? 175 ARG B NE  1 
ATOM   1312 C CZ  . ARG A 1 175 ? 38.94807 -7.15538  2.72835   1.000 225.50659 ? 175 ARG B CZ  1 
ATOM   1313 N NH1 . ARG A 1 175 ? 40.00290 -7.89104  3.03641   1.000 220.02696 ? 175 ARG B NH1 1 
ATOM   1314 N NH2 . ARG A 1 175 ? 39.11027 -6.06289  1.98833   1.000 231.16431 ? 175 ARG B NH2 1 
ATOM   1315 N N   . VAL A 1 176 ? 38.30185 -10.27911 8.66866   1.000 199.74536 ? 176 VAL B N   1 
ATOM   1316 C CA  . VAL A 1 176 ? 39.53352 -10.82179 9.22943   1.000 196.53363 ? 176 VAL B CA  1 
ATOM   1317 C C   . VAL A 1 176 ? 39.97305 -12.04856 8.44265   1.000 197.94534 ? 176 VAL B C   1 
ATOM   1318 O O   . VAL A 1 176 ? 39.14795 -12.85570 8.00200   1.000 200.10043 ? 176 VAL B O   1 
ATOM   1319 C CB  . VAL A 1 176 ? 39.38003 -11.15060 10.73203  1.000 193.45678 ? 176 VAL B CB  1 
ATOM   1320 C CG1 . VAL A 1 176 ? 38.39906 -12.27033 10.94672  1.000 193.00102 ? 176 VAL B CG1 1 
ATOM   1321 C CG2 . VAL A 1 176 ? 40.71478 -11.56898 11.31251  1.000 192.30279 ? 176 VAL B CG2 1 
ATOM   1322 N N   . ARG A 1 177 ? 41.28243 -12.16580 8.24848   1.000 188.24750 ? 177 ARG B N   1 
ATOM   1323 C CA  . ARG A 1 177 ? 41.90663 -13.36440 7.71633   1.000 189.62067 ? 177 ARG B CA  1 
ATOM   1324 C C   . ARG A 1 177 ? 43.12548 -13.68254 8.56937   1.000 188.63483 ? 177 ARG B C   1 
ATOM   1325 O O   . ARG A 1 177 ? 43.73359 -12.78991 9.16683   1.000 188.66381 ? 177 ARG B O   1 
ATOM   1326 C CB  . ARG A 1 177 ? 42.29435 -13.19433 6.23975   1.000 192.01927 ? 177 ARG B CB  1 
ATOM   1327 C CG  . ARG A 1 177 ? 43.57026 -12.40847 6.00302   1.000 192.22781 ? 177 ARG B CG  1 
ATOM   1328 C CD  . ARG A 1 177 ? 44.13652 -12.68848 4.61888   1.000 194.59536 ? 177 ARG B CD  1 
ATOM   1329 N NE  . ARG A 1 177 ? 45.23447 -11.79046 4.28133   1.000 196.03934 ? 177 ARG B NE  1 
ATOM   1330 C CZ  . ARG A 1 177 ? 45.64303 -11.53758 3.04536   1.000 198.26700 ? 177 ARG B CZ  1 
ATOM   1331 N NH1 . ARG A 1 177 ? 45.07199 -12.10947 1.99761   1.000 199.25267 ? 177 ARG B NH1 1 
ATOM   1332 N NH2 . ARG A 1 177 ? 46.65640 -10.69724 2.85608   1.000 199.23381 ? 177 ARG B NH2 1 
ATOM   1333 N N   . ALA A 1 178 ? 43.46643 -14.96531 8.64140   1.000 187.69348 ? 178 ALA B N   1 
ATOM   1334 C CA  . ALA A 1 178 ? 44.52861 -15.42451 9.52158   1.000 188.52331 ? 178 ALA B CA  1 
ATOM   1335 C C   . ALA A 1 178 ? 45.43105 -16.38860 8.77212   1.000 191.39473 ? 178 ALA B C   1 
ATOM   1336 O O   . ALA A 1 178 ? 45.12576 -16.82142 7.65821   1.000 194.41630 ? 178 ALA B O   1 
ATOM   1337 C CB  . ALA A 1 178 ? 43.96632 -16.10494 10.76936  1.000 187.63731 ? 178 ALA B CB  1 
ATOM   1338 N N   . TRP A 1 179 ? 46.55317 -16.73065 9.40354   1.000 184.80599 ? 179 TRP B N   1 
ATOM   1339 C CA  . TRP A 1 179 ? 47.43886 -17.73814 8.84041   1.000 187.88369 ? 179 TRP B CA  1 
ATOM   1340 C C   . TRP A 1 179 ? 48.43662 -18.19145 9.89288   1.000 188.86584 ? 179 TRP B C   1 
ATOM   1341 O O   . TRP A 1 179 ? 48.94864 -17.38127 10.67124  1.000 187.99866 ? 179 TRP B O   1 
ATOM   1342 C CB  . TRP A 1 179 ? 48.15863 -17.21510 7.58989   1.000 188.85368 ? 179 TRP B CB  1 
ATOM   1343 C CG  . TRP A 1 179 ? 49.42046 -16.43550 7.80896   1.000 189.21081 ? 179 TRP B CG  1 
ATOM   1344 C CD1 . TRP A 1 179 ? 49.53550 -15.18238 8.33218   1.000 188.05436 ? 179 TRP B CD1 1 
ATOM   1345 C CD2 . TRP A 1 179 ? 50.74088 -16.82950 7.42279   1.000 192.23566 ? 179 TRP B CD2 1 
ATOM   1346 N NE1 . TRP A 1 179 ? 50.85330 -14.78861 8.33221   1.000 190.41286 ? 179 TRP B NE1 1 
ATOM   1347 C CE2 . TRP A 1 179 ? 51.61212 -15.78422 7.77448   1.000 192.65180 ? 179 TRP B CE2 1 
ATOM   1348 C CE3 . TRP A 1 179 ? 51.27296 -17.97572 6.83468   1.000 195.81108 ? 179 TRP B CE3 1 
ATOM   1349 C CZ2 . TRP A 1 179 ? 52.98583 -15.85218 7.54442   1.000 196.07709 ? 179 TRP B CZ2 1 
ATOM   1350 C CZ3 . TRP A 1 179 ? 52.63246 -18.03856 6.61098   1.000 198.28308 ? 179 TRP B CZ3 1 
ATOM   1351 C CH2 . TRP A 1 179 ? 53.47411 -16.98790 6.96977   1.000 198.58735 ? 179 TRP B CH2 1 
ATOM   1352 N N   . ALA A 1 180 ? 48.67752 -19.49871 9.91547   1.000 185.38905 ? 180 ALA B N   1 
ATOM   1353 C CA  . ALA A 1 180 ? 49.59819 -20.12295 10.85446  1.000 188.49465 ? 180 ALA B CA  1 
ATOM   1354 C C   . ALA A 1 180 ? 51.02093 -19.76949 10.45012  1.000 191.28446 ? 180 ALA B C   1 
ATOM   1355 O O   . ALA A 1 180 ? 51.48467 -20.16258 9.37481   1.000 194.32365 ? 180 ALA B O   1 
ATOM   1356 C CB  . ALA A 1 180 ? 49.38534 -21.63116 10.86688  1.000 192.80097 ? 180 ALA B CB  1 
ATOM   1357 N N   . GLN A 1 181 ? 51.72611 -19.05117 11.32479  1.000 199.42588 ? 181 GLN B N   1 
ATOM   1358 C CA  . GLN A 1 181 ? 52.99146 -18.44842 10.92415  1.000 201.64604 ? 181 GLN B CA  1 
ATOM   1359 C C   . GLN A 1 181 ? 54.06043 -19.51796 10.74090  1.000 206.14429 ? 181 GLN B C   1 
ATOM   1360 O O   . GLN A 1 181 ? 54.73697 -19.57052 9.70561   1.000 207.44830 ? 181 GLN B O   1 
ATOM   1361 C CB  . GLN A 1 181 ? 53.47791 -17.45622 11.97473  1.000 203.70055 ? 181 GLN B CB  1 
ATOM   1362 C CG  . GLN A 1 181 ? 54.77460 -16.80321 11.51921  1.000 208.56398 ? 181 GLN B CG  1 
ATOM   1363 C CD  . GLN A 1 181 ? 54.53127 -15.77746 10.43226  1.000 208.77723 ? 181 GLN B CD  1 
ATOM   1364 O OE1 . GLN A 1 181 ? 53.41859 -15.28349 10.29556  1.000 203.40306 ? 181 GLN B OE1 1 
ATOM   1365 N NE2 . GLN A 1 181 ? 55.50339 -15.58291 9.56466   1.000 215.02356 ? 181 GLN B NE2 1 
ATOM   1366 N N   . ALA A 1 182 ? 54.22461 -20.37276 11.75523  1.000 205.80845 ? 182 ALA B N   1 
ATOM   1367 C CA  . ALA A 1 182 ? 55.30910 -21.34027 11.78223  1.000 211.52788 ? 182 ALA B CA  1 
ATOM   1368 C C   . ALA A 1 182 ? 55.20031 -22.37481 10.67280  1.000 214.07128 ? 182 ALA B C   1 
ATOM   1369 O O   . ALA A 1 182 ? 56.19646 -23.04308 10.37356  1.000 219.80569 ? 182 ALA B O   1 
ATOM   1370 C CB  . ALA A 1 182 ? 55.36225 -22.04884 13.14258  1.000 214.78493 ? 182 ALA B CB  1 
ATOM   1371 N N   . TYR A 1 183 ? 54.03389 -22.51813 10.04451  1.000 209.19332 ? 183 TYR B N   1 
ATOM   1372 C CA  . TYR A 1 183 ? 53.83554 -23.54095 9.02488   1.000 213.36631 ? 183 TYR B CA  1 
ATOM   1373 C C   . TYR A 1 183 ? 53.92749 -23.00694 7.59927   1.000 212.92251 ? 183 TYR B C   1 
ATOM   1374 O O   . TYR A 1 183 ? 53.79852 -23.79186 6.65191   1.000 218.30590 ? 183 TYR B O   1 
ATOM   1375 C CB  . TYR A 1 183 ? 52.48787 -24.23996 9.23221   1.000 213.02755 ? 183 TYR B CB  1 
ATOM   1376 C CG  . TYR A 1 183 ? 52.61360 -25.58365 9.91723   1.000 218.40855 ? 183 TYR B CG  1 
ATOM   1377 C CD1 . TYR A 1 183 ? 53.15963 -26.67572 9.25494   1.000 226.80737 ? 183 TYR B CD1 1 
ATOM   1378 C CD2 . TYR A 1 183 ? 52.20036 -25.75582 11.23128  1.000 215.56252 ? 183 TYR B CD2 1 
ATOM   1379 C CE1 . TYR A 1 183 ? 53.27983 -27.90403 9.88119   1.000 232.70056 ? 183 TYR B CE1 1 
ATOM   1380 C CE2 . TYR A 1 183 ? 52.31730 -26.97784 11.86637  1.000 221.01585 ? 183 TYR B CE2 1 
ATOM   1381 C CZ  . TYR A 1 183 ? 52.85783 -28.04833 11.18841  1.000 229.50215 ? 183 TYR B CZ  1 
ATOM   1382 O OH  . TYR A 1 183 ? 52.97016 -29.26438 11.82473  1.000 235.86111 ? 183 TYR B OH  1 
ATOM   1383 N N   . ASN A 1 184 ? 54.15393 -21.70563 7.42442   1.000 208.12277 ? 184 ASN B N   1 
ATOM   1384 C CA  . ASN A 1 184 ? 54.33370 -21.08823 6.10919   1.000 207.38777 ? 184 ASN B CA  1 
ATOM   1385 C C   . ASN A 1 184 ? 53.15156 -21.40408 5.18906   1.000 206.97065 ? 184 ASN B C   1 
ATOM   1386 O O   . ASN A 1 184 ? 53.26996 -22.08937 4.17222   1.000 212.03299 ? 184 ASN B O   1 
ATOM   1387 C CB  . ASN A 1 184 ? 55.65713 -21.53488 5.48029   1.000 213.57592 ? 184 ASN B CB  1 
ATOM   1388 C CG  . ASN A 1 184 ? 56.13061 -20.59572 4.38950   1.000 213.56374 ? 184 ASN B CG  1 
ATOM   1389 O OD1 . ASN A 1 184 ? 55.78138 -19.41537 4.38031   1.000 209.61920 ? 184 ASN B OD1 1 
ATOM   1390 N ND2 . ASN A 1 184 ? 56.92839 -21.11446 3.46242   1.000 219.69739 ? 184 ASN B ND2 1 
ATOM   1391 N N   . THR A 1 185 ? 52.00090 -20.87545 5.58391   1.000 206.59135 ? 185 THR B N   1 
ATOM   1392 C CA  . THR A 1 185 ? 50.74160 -21.13512 4.90705   1.000 207.37321 ? 185 THR B CA  1 
ATOM   1393 C C   . THR A 1 185 ? 50.35691 -19.96532 4.00591   1.000 203.76738 ? 185 THR B C   1 
ATOM   1394 O O   . THR A 1 185 ? 50.91087 -18.86771 4.09417   1.000 200.26365 ? 185 THR B O   1 
ATOM   1395 C CB  . THR A 1 185 ? 49.62863 -21.40476 5.92592   1.000 206.10582 ? 185 THR B CB  1 
ATOM   1396 O OG1 . THR A 1 185 ? 49.12817 -20.16331 6.43732   1.000 199.48298 ? 185 THR B OG1 1 
ATOM   1397 C CG2 . THR A 1 185 ? 50.16062 -22.23918 7.08275   1.000 205.93833 ? 185 THR B CG2 1 
ATOM   1398 N N   . THR A 1 186 ? 49.40673 -20.22396 3.11246   1.000 197.93535 ? 186 THR B N   1 
ATOM   1399 C CA  . THR A 1 186 ? 48.87120 -19.17642 2.25498   1.000 195.06628 ? 186 THR B CA  1 
ATOM   1400 C C   . THR A 1 186 ? 47.76940 -18.43315 2.99555   1.000 191.10902 ? 186 THR B C   1 
ATOM   1401 O O   . THR A 1 186 ? 46.90037 -19.05871 3.60892   1.000 192.80221 ? 186 THR B O   1 
ATOM   1402 C CB  . THR A 1 186 ? 48.32950 -19.76780 0.95490   1.000 199.15386 ? 186 THR B CB  1 
ATOM   1403 O OG1 . THR A 1 186 ? 49.39276 -20.41180 0.24220   1.000 205.02601 ? 186 THR B OG1 1 
ATOM   1404 C CG2 . THR A 1 186 ? 47.72554 -18.67688 0.08477   1.000 197.90190 ? 186 THR B CG2 1 
ATOM   1405 N N   . TRP A 1 187 ? 47.81700 -17.10212 2.94467   1.000 190.06898 ? 187 TRP B N   1 
ATOM   1406 C CA  . TRP A 1 187 ? 46.86681 -16.24235 3.63992   1.000 185.76687 ? 187 TRP B CA  1 
ATOM   1407 C C   . TRP A 1 187 ? 45.44148 -16.74328 3.45126   1.000 185.72927 ? 187 TRP B C   1 
ATOM   1408 O O   . TRP A 1 187 ? 44.95509 -16.85491 2.32136   1.000 187.23866 ? 187 TRP B O   1 
ATOM   1409 C CB  . TRP A 1 187 ? 46.98761 -14.80837 3.11506   1.000 184.31707 ? 187 TRP B CB  1 
ATOM   1410 C CG  . TRP A 1 187 ? 47.80435 -13.86144 3.96659   1.000 183.18329 ? 187 TRP B CG  1 
ATOM   1411 C CD1 . TRP A 1 187 ? 48.88123 -13.12612 3.56069   1.000 185.46387 ? 187 TRP B CD1 1 
ATOM   1412 C CD2 . TRP A 1 187 ? 47.60420 -13.54205 5.35257   1.000 180.75998 ? 187 TRP B CD2 1 
ATOM   1413 N NE1 . TRP A 1 187 ? 49.36177 -12.37089 4.60179   1.000 184.83417 ? 187 TRP B NE1 1 
ATOM   1414 C CE2 . TRP A 1 187 ? 48.59736 -12.60842 5.71314   1.000 181.81614 ? 187 TRP B CE2 1 
ATOM   1415 C CE3 . TRP A 1 187 ? 46.68834 -13.95871 6.32395   1.000 178.76177 ? 187 TRP B CE3 1 
ATOM   1416 C CZ2 . TRP A 1 187 ? 48.69662 -12.08236 6.99995   1.000 180.83614 ? 187 TRP B CZ2 1 
ATOM   1417 C CZ3 . TRP A 1 187 ? 46.78526 -13.42965 7.59921   1.000 177.50697 ? 187 TRP B CZ3 1 
ATOM   1418 C CH2 . TRP A 1 187 ? 47.78263 -12.50338 7.92552   1.000 178.53770 ? 187 TRP B CH2 1 
ATOM   1419 N N   . SER A 1 188 ? 44.77637 -17.06747 4.55818   1.000 188.70688 ? 188 SER B N   1 
ATOM   1420 C CA  . SER A 1 188 ? 43.42630 -17.60441 4.48066   1.000 189.85379 ? 188 SER B CA  1 
ATOM   1421 C C   . SER A 1 188 ? 42.46846 -16.57232 3.90019   1.000 188.86272 ? 188 SER B C   1 
ATOM   1422 O O   . SER A 1 188 ? 42.77067 -15.38056 3.81191   1.000 186.48148 ? 188 SER B O   1 
ATOM   1423 C CB  . SER A 1 188 ? 42.92887 -18.03290 5.85830   1.000 188.09550 ? 188 SER B CB  1 
ATOM   1424 O OG  . SER A 1 188 ? 42.39922 -16.92661 6.56940   1.000 183.33229 ? 188 SER B OG  1 
ATOM   1425 N N   . GLU A 1 189 ? 41.29462 -17.04995 3.50070   1.000 201.64801 ? 189 GLU B N   1 
ATOM   1426 C CA  . GLU A 1 189 ? 40.27609 -16.15951 2.96771   1.000 201.94124 ? 189 GLU B CA  1 
ATOM   1427 C C   . GLU A 1 189 ? 39.72872 -15.25947 4.06495   1.000 198.85925 ? 189 GLU B C   1 
ATOM   1428 O O   . GLU A 1 189 ? 39.52319 -15.68921 5.20381   1.000 197.38478 ? 189 GLU B O   1 
ATOM   1429 C CB  . GLU A 1 189 ? 39.14792 -16.96194 2.32390   1.000 206.62314 ? 189 GLU B CB  1 
ATOM   1430 C CG  . GLU A 1 189 ? 39.57235 -17.71986 1.07731   1.000 211.20957 ? 189 GLU B CG  1 
ATOM   1431 C CD  . GLU A 1 189 ? 40.57789 -16.94980 0.23896   1.000 211.42868 ? 189 GLU B CD  1 
ATOM   1432 O OE1 . GLU A 1 189 ? 40.15012 -16.09821 -0.56905  1.000 212.96734 ? 189 GLU B OE1 1 
ATOM   1433 O OE2 . GLU A 1 189 ? 41.79399 -17.19793 0.38230   1.000 210.56190 ? 189 GLU B OE2 1 
ATOM   1434 N N   . TRP A 1 190 ? 39.50472 -13.99762 3.71244   1.000 212.42150 ? 190 TRP B N   1 
ATOM   1435 C CA  . TRP A 1 190 ? 39.02255 -13.02705 4.68060   1.000 210.28948 ? 190 TRP B CA  1 
ATOM   1436 C C   . TRP A 1 190 ? 37.62686 -13.41004 5.15465   1.000 211.05508 ? 190 TRP B C   1 
ATOM   1437 O O   . TRP A 1 190 ? 36.78070 -13.83980 4.36578   1.000 214.85866 ? 190 TRP B O   1 
ATOM   1438 C CB  . TRP A 1 190 ? 39.00633 -11.63164 4.06034   1.000 212.40086 ? 190 TRP B CB  1 
ATOM   1439 C CG  . TRP A 1 190 ? 40.36597 -11.03277 3.84115   1.000 211.54416 ? 190 TRP B CG  1 
ATOM   1440 C CD1 . TRP A 1 190 ? 41.15147 -11.17018 2.73270   1.000 212.51265 ? 190 TRP B CD1 1 
ATOM   1441 C CD2 . TRP A 1 190 ? 41.09889 -10.20200 4.75005   1.000 209.44659 ? 190 TRP B CD2 1 
ATOM   1442 N NE1 . TRP A 1 190 ? 42.32540 -10.47568 2.89460   1.000 211.96827 ? 190 TRP B NE1 1 
ATOM   1443 C CE2 . TRP A 1 190 ? 42.31722 -9.87064  4.12373   1.000 210.20117 ? 190 TRP B CE2 1 
ATOM   1444 C CE3 . TRP A 1 190 ? 40.84280 -9.70384  6.03028   1.000 207.07830 ? 190 TRP B CE3 1 
ATOM   1445 C CZ2 . TRP A 1 190 ? 43.27922 -9.06909  4.73756   1.000 209.81159 ? 190 TRP B CZ2 1 
ATOM   1446 C CZ3 . TRP A 1 190 ? 41.79748 -8.90504  6.63529   1.000 205.87264 ? 190 TRP B CZ3 1 
ATOM   1447 C CH2 . TRP A 1 190 ? 43.00015 -8.59697  5.99006   1.000 207.47768 ? 190 TRP B CH2 1 
ATOM   1448 N N   . SER A 1 191 ? 37.39212 -13.25995 6.45828   1.000 207.83592 ? 191 SER B N   1 
ATOM   1449 C CA  . SER A 1 191 ? 36.09174 -13.57273 7.02264   1.000 208.26085 ? 191 SER B CA  1 
ATOM   1450 C C   . SER A 1 191 ? 35.01891 -12.67438 6.40976   1.000 210.67694 ? 191 SER B C   1 
ATOM   1451 O O   . SER A 1 191 ? 35.33061 -11.65290 5.79089   1.000 212.79534 ? 191 SER B O   1 
ATOM   1452 C CB  . SER A 1 191 ? 36.11741 -13.40315 8.54025   1.000 204.53324 ? 191 SER B CB  1 
ATOM   1453 O OG  . SER A 1 191 ? 35.89267 -12.05235 8.90143   1.000 203.10815 ? 191 SER B OG  1 
ATOM   1454 N N   . PRO A 1 192 ? 33.74702 -13.05605 6.54571   1.000 212.78970 ? 192 PRO B N   1 
ATOM   1455 C CA  . PRO A 1 192 ? 32.65891 -12.18851 6.08167   1.000 217.82645 ? 192 PRO B CA  1 
ATOM   1456 C C   . PRO A 1 192 ? 32.79108 -10.77647 6.63499   1.000 218.24608 ? 192 PRO B C   1 
ATOM   1457 O O   . PRO A 1 192 ? 33.24681 -10.56628 7.76062   1.000 214.95195 ? 192 PRO B O   1 
ATOM   1458 C CB  . PRO A 1 192 ? 31.40625 -12.88346 6.62027   1.000 216.85523 ? 192 PRO B CB  1 
ATOM   1459 C CG  . PRO A 1 192 ? 31.77667 -14.32260 6.62578   1.000 214.75716 ? 192 PRO B CG  1 
ATOM   1460 C CD  . PRO A 1 192 ? 33.25303 -14.38831 6.93832   1.000 211.93040 ? 192 PRO B CD  1 
ATOM   1461 N N   . SER A 1 193 ? 32.38155 -9.80407  5.82648   1.000 219.58922 ? 193 SER B N   1 
ATOM   1462 C CA  . SER A 1 193 ? 32.57139 -8.39350  6.14986   1.000 221.98149 ? 193 SER B CA  1 
ATOM   1463 C C   . SER A 1 193 ? 31.36127 -7.89873  6.93286   1.000 224.23170 ? 193 SER B C   1 
ATOM   1464 O O   . SER A 1 193 ? 30.28093 -7.69932  6.37186   1.000 229.82463 ? 193 SER B O   1 
ATOM   1465 C CB  . SER A 1 193 ? 32.78740 -7.58156  4.87811   1.000 227.13305 ? 193 SER B CB  1 
ATOM   1466 O OG  . SER A 1 193 ? 32.40709 -6.23168  5.06330   1.000 232.13340 ? 193 SER B OG  1 
ATOM   1467 N N   . THR A 1 194 ? 31.54150 -7.69850  8.23581   1.000 222.89696 ? 194 THR B N   1 
ATOM   1468 C CA  . THR A 1 194 ? 30.50713 -7.08140  9.05089   1.000 226.02433 ? 194 THR B CA  1 
ATOM   1469 C C   . THR A 1 194 ? 30.55126 -5.56317  8.89391   1.000 232.23519 ? 194 THR B C   1 
ATOM   1470 O O   . THR A 1 194 ? 31.53186 -4.99086  8.41153   1.000 232.63310 ? 194 THR B O   1 
ATOM   1471 C CB  . THR A 1 194 ? 30.66889 -7.46728  10.52231  1.000 221.41542 ? 194 THR B CB  1 
ATOM   1472 O OG1 . THR A 1 194 ? 29.46974 -7.14786  11.23687  1.000 225.36711 ? 194 THR B OG1 1 
ATOM   1473 C CG2 . THR A 1 194 ? 31.83827 -6.71965  11.14739  1.000 218.51325 ? 194 THR B CG2 1 
ATOM   1474 N N   . LYS A 1 195 ? 29.45889 -4.91084  9.28979   1.000 233.86006 ? 195 LYS B N   1 
ATOM   1475 C CA  . LYS A 1 195 ? 29.29547 -3.48111  9.06957   1.000 241.87256 ? 195 LYS B CA  1 
ATOM   1476 C C   . LYS A 1 195 ? 28.73185 -2.82949  10.32443  1.000 244.99638 ? 195 LYS B C   1 
ATOM   1477 O O   . LYS A 1 195 ? 28.01510 -3.46465  11.10246  1.000 242.93916 ? 195 LYS B O   1 
ATOM   1478 C CB  . LYS A 1 195 ? 28.37057 -3.20245  7.87221   1.000 249.90699 ? 195 LYS B CB  1 
ATOM   1479 C CG  . LYS A 1 195 ? 28.64575 -4.08478  6.65980   1.000 248.56532 ? 195 LYS B CG  1 
ATOM   1480 C CD  . LYS A 1 195 ? 27.76361 -3.73552  5.47451   1.000 256.18092 ? 195 LYS B CD  1 
ATOM   1481 C CE  . LYS A 1 195 ? 27.62118 -2.23812  5.29739   1.000 264.29260 ? 195 LYS B CE  1 
ATOM   1482 N NZ  . LYS A 1 195 ? 27.35381 -1.89396  3.87657   1.000 270.46432 ? 195 LYS B NZ  1 
ATOM   1483 N N   . TRP A 1 196 ? 29.06161 -1.55544  10.50961  1.000 255.63026 ? 196 TRP B N   1 
ATOM   1484 C CA  . TRP A 1 196 ? 28.58273 -0.74982  11.63426  1.000 260.55581 ? 196 TRP B CA  1 
ATOM   1485 C C   . TRP A 1 196 ? 28.91354 0.70869   11.32628  1.000 268.77273 ? 196 TRP B C   1 
ATOM   1486 O O   . TRP A 1 196 ? 29.31248 1.04579   10.20452  1.000 270.19921 ? 196 TRP B O   1 
ATOM   1487 C CB  . TRP A 1 196 ? 29.19921 -1.21787  12.95546  1.000 252.63619 ? 196 TRP B CB  1 
ATOM   1488 C CG  . TRP A 1 196 ? 30.61154 -0.75667  13.16515  1.000 248.91759 ? 196 TRP B CG  1 
ATOM   1489 C CD1 . TRP A 1 196 ? 31.02410 0.33642   13.87097  1.000 252.07756 ? 196 TRP B CD1 1 
ATOM   1490 C CD2 . TRP A 1 196 ? 31.79559 -1.36415  12.64227  1.000 241.73106 ? 196 TRP B CD2 1 
ATOM   1491 N NE1 . TRP A 1 196 ? 32.39254 0.44091   13.82807  1.000 247.16202 ? 196 TRP B NE1 1 
ATOM   1492 C CE2 . TRP A 1 196 ? 32.89067 -0.59194  13.07927  1.000 240.53665 ? 196 TRP B CE2 1 
ATOM   1493 C CE3 . TRP A 1 196 ? 32.03731 -2.48961  11.85168  1.000 235.80327 ? 196 TRP B CE3 1 
ATOM   1494 C CZ2 . TRP A 1 196 ? 34.20562 -0.91032  12.75143  1.000 234.36887 ? 196 TRP B CZ2 1 
ATOM   1495 C CZ3 . TRP A 1 196 ? 33.33875 -2.80279  11.52962  1.000 230.56251 ? 196 TRP B CZ3 1 
ATOM   1496 C CH2 . TRP A 1 196 ? 34.40841 -2.01727  11.97652  1.000 230.10696 ? 196 TRP B CH2 1 
ATOM   1497 N N   . HIS A 1 197 ? 28.74175 1.57859   12.31867  1.000 249.25450 ? 197 HIS B N   1 
ATOM   1498 C CA  . HIS A 1 197 ? 29.14116 2.97697   12.18443  1.000 257.44105 ? 197 HIS B CA  1 
ATOM   1499 C C   . HIS A 1 197 ? 30.61541 3.16894   12.53266  1.000 253.78633 ? 197 HIS B C   1 
ATOM   1500 O O   . HIS A 1 197 ? 30.97032 4.05095   13.31508  1.000 254.89193 ? 197 HIS B O   1 
ATOM   1501 C CB  . HIS A 1 197 ? 28.28045 3.88226   13.06594  1.000 266.80283 ? 197 HIS B CB  1 
ATOM   1502 C CG  . HIS A 1 197 ? 28.13869 5.27656   12.53827  1.000 276.10117 ? 197 HIS B CG  1 
ATOM   1503 N ND1 . HIS A 1 197 ? 27.89672 5.54783   11.20898  1.000 278.52305 ? 197 HIS B ND1 1 
ATOM   1504 C CD2 . HIS A 1 197 ? 28.21828 6.47804   13.15829  1.000 282.50301 ? 197 HIS B CD2 1 
ATOM   1505 C CE1 . HIS A 1 197 ? 27.82446 6.85513   11.03378  1.000 286.04457 ? 197 HIS B CE1 1 
ATOM   1506 N NE2 . HIS A 1 197 ? 28.01709 7.44282   12.20091  1.000 288.12106 ? 197 HIS B NE2 1 
ATOM   1507 N N   . GLN B 2 1   ? 70.44037 -46.16403 17.00969  1.000 208.96955 ? 1   GLN A N   1 
ATOM   1508 C CA  . GLN B 2 1   ? 69.79297 -47.38083 16.53458  1.000 205.54158 ? 1   GLN A CA  1 
ATOM   1509 C C   . GLN B 2 1   ? 68.81258 -47.90343 17.58422  1.000 200.97882 ? 1   GLN A C   1 
ATOM   1510 O O   . GLN B 2 1   ? 69.10446 -47.88652 18.78027  1.000 202.66858 ? 1   GLN A O   1 
ATOM   1511 C CB  . GLN B 2 1   ? 70.84163 -48.44034 16.18871  1.000 210.41126 ? 1   GLN A CB  1 
ATOM   1512 C CG  . GLN B 2 1   ? 70.27161 -49.74055 15.65366  1.000 208.44062 ? 1   GLN A CG  1 
ATOM   1513 C CD  . GLN B 2 1   ? 71.35131 -50.69145 15.17635  1.000 214.16033 ? 1   GLN A CD  1 
ATOM   1514 O OE1 . GLN B 2 1   ? 72.53975 -50.37024 15.21568  1.000 219.30484 ? 1   GLN A OE1 1 
ATOM   1515 N NE2 . GLN B 2 1   ? 70.94245 -51.86770 14.71606  1.000 213.72654 ? 1   GLN A NE2 1 
ATOM   1516 N N   . VAL B 2 2   ? 67.65036 -48.36763 17.13204  1.000 203.44207 ? 2   VAL A N   1 
ATOM   1517 C CA  . VAL B 2 2   ? 66.54148 -48.72861 18.00965  1.000 198.61239 ? 2   VAL A CA  1 
ATOM   1518 C C   . VAL B 2 2   ? 66.37982 -50.24353 18.00540  1.000 198.06634 ? 2   VAL A C   1 
ATOM   1519 O O   . VAL B 2 2   ? 66.12204 -50.84757 16.95642  1.000 197.65798 ? 2   VAL A O   1 
ATOM   1520 C CB  . VAL B 2 2   ? 65.23919 -48.03362 17.58205  1.000 193.51900 ? 2   VAL A CB  1 
ATOM   1521 C CG1 . VAL B 2 2   ? 64.05940 -48.55744 18.38690  1.000 189.01208 ? 2   VAL A CG1 1 
ATOM   1522 C CG2 . VAL B 2 2   ? 65.37015 -46.52638 17.74056  1.000 194.83293 ? 2   VAL A CG2 1 
ATOM   1523 N N   . GLN B 2 3   ? 66.53181 -50.85383 19.17841  1.000 195.48700 ? 3   GLN A N   1 
ATOM   1524 C CA  . GLN B 2 3   ? 66.21435 -52.26442 19.34589  1.000 194.91041 ? 3   GLN A CA  1 
ATOM   1525 C C   . GLN B 2 3   ? 64.70596 -52.46968 19.41907  1.000 188.90193 ? 3   GLN A C   1 
ATOM   1526 O O   . GLN B 2 3   ? 63.95323 -51.58699 19.83912  1.000 185.92833 ? 3   GLN A O   1 
ATOM   1527 C CB  . GLN B 2 3   ? 66.86757 -52.81801 20.61372  1.000 198.88472 ? 3   GLN A CB  1 
ATOM   1528 C CG  . GLN B 2 3   ? 68.35051 -53.12590 20.49091  1.000 205.57309 ? 3   GLN A CG  1 
ATOM   1529 C CD  . GLN B 2 3   ? 68.62733 -54.27873 19.54701  1.000 207.74980 ? 3   GLN A CD  1 
ATOM   1530 O OE1 . GLN B 2 3   ? 69.15863 -54.08777 18.45428  1.000 210.02939 ? 3   GLN A OE1 1 
ATOM   1531 N NE2 . GLN B 2 3   ? 68.26509 -55.48566 19.96595  1.000 208.00534 ? 3   GLN A NE2 1 
ATOM   1532 N N   . LEU B 2 4   ? 64.26840 -53.65511 19.00462  1.000 186.97673 ? 4   LEU A N   1 
ATOM   1533 C CA  . LEU B 2 4   ? 62.88116 -54.07637 19.14024  1.000 182.22591 ? 4   LEU A CA  1 
ATOM   1534 C C   . LEU B 2 4   ? 62.86439 -55.48520 19.70881  1.000 184.39060 ? 4   LEU A C   1 
ATOM   1535 O O   . LEU B 2 4   ? 63.48721 -56.38999 19.14492  1.000 187.84543 ? 4   LEU A O   1 
ATOM   1536 C CB  . LEU B 2 4   ? 62.14501 -54.03445 17.79693  1.000 179.29304 ? 4   LEU A CB  1 
ATOM   1537 C CG  . LEU B 2 4   ? 62.01146 -52.67431 17.11063  1.000 177.96667 ? 4   LEU A CG  1 
ATOM   1538 C CD1 . LEU B 2 4   ? 61.25691 -52.81144 15.80248  1.000 176.70857 ? 4   LEU A CD1 1 
ATOM   1539 C CD2 . LEU B 2 4   ? 61.30684 -51.69376 18.02013  1.000 175.02810 ? 4   LEU A CD2 1 
ATOM   1540 N N   . VAL B 2 5   ? 62.16822 -55.66978 20.82706  1.000 173.58194 ? 5   VAL A N   1 
ATOM   1541 C CA  . VAL B 2 5   ? 62.09836 -56.96202 21.49999  1.000 176.89741 ? 5   VAL A CA  1 
ATOM   1542 C C   . VAL B 2 5   ? 60.63003 -57.27470 21.75725  1.000 174.15496 ? 5   VAL A C   1 
ATOM   1543 O O   . VAL B 2 5   ? 59.99467 -56.63811 22.60726  1.000 174.15096 ? 5   VAL A O   1 
ATOM   1544 C CB  . VAL B 2 5   ? 62.89900 -56.98396 22.81011  1.000 182.48399 ? 5   VAL A CB  1 
ATOM   1545 C CG1 . VAL B 2 5   ? 62.83065 -58.36387 23.44218  1.000 186.98706 ? 5   VAL A CG1 1 
ATOM   1546 C CG2 . VAL B 2 5   ? 64.34726 -56.57611 22.56488  1.000 185.78949 ? 5   VAL A CG2 1 
ATOM   1547 N N   . GLU B 2 6   ? 60.09395 -58.25188 21.02986  1.000 173.76091 ? 6   GLU A N   1 
ATOM   1548 C CA  . GLU B 2 6   ? 58.72599 -58.70687 21.21727  1.000 172.30661 ? 6   GLU A CA  1 
ATOM   1549 C C   . GLU B 2 6   ? 58.63484 -59.67237 22.39763  1.000 178.11181 ? 6   GLU A C   1 
ATOM   1550 O O   . GLU B 2 6   ? 59.64100 -60.14072 22.93685  1.000 182.98354 ? 6   GLU A O   1 
ATOM   1551 C CB  . GLU B 2 6   ? 58.20255 -59.36937 19.94227  1.000 169.71537 ? 6   GLU A CB  1 
ATOM   1552 C CG  . GLU B 2 6   ? 58.17915 -58.45483 18.72860  1.000 165.40876 ? 6   GLU A CG  1 
ATOM   1553 C CD  . GLU B 2 6   ? 59.50857 -58.37216 18.01017  1.000 167.93247 ? 6   GLU A CD  1 
ATOM   1554 O OE1 . GLU B 2 6   ? 60.53966 -58.75637 18.60176  1.000 172.42527 ? 6   GLU A OE1 1 
ATOM   1555 O OE2 . GLU B 2 6   ? 59.52071 -57.90430 16.85319  1.000 166.76222 ? 6   GLU A OE2 1 
ATOM   1556 N N   . SER B 2 7   ? 57.40265 -59.96964 22.79480  1.000 168.21286 ? 7   SER A N   1 
ATOM   1557 C CA  . SER B 2 7   ? 57.12979 -60.86332 23.91537  1.000 174.46385 ? 7   SER A CA  1 
ATOM   1558 C C   . SER B 2 7   ? 55.64041 -61.17992 23.90776  1.000 173.98027 ? 7   SER A C   1 
ATOM   1559 O O   . SER B 2 7   ? 54.89458 -60.74391 23.02493  1.000 169.07455 ? 7   SER A O   1 
ATOM   1560 C CB  . SER B 2 7   ? 57.55697 -60.24361 25.24821  1.000 178.63474 ? 7   SER A CB  1 
ATOM   1561 O OG  . SER B 2 7   ? 56.77972 -59.09721 25.55036  1.000 177.00384 ? 7   SER A OG  1 
ATOM   1562 N N   . GLY B 2 8   ? 55.21154 -61.94676 24.90553  1.000 177.76243 ? 8   GLY A N   1 
ATOM   1563 C CA  . GLY B 2 8   ? 53.79762 -62.20170 25.08065  1.000 177.50494 ? 8   GLY A CA  1 
ATOM   1564 C C   . GLY B 2 8   ? 53.18466 -63.19634 24.12381  1.000 176.64972 ? 8   GLY A C   1 
ATOM   1565 O O   . GLY B 2 8   ? 51.97231 -63.41539 24.18628  1.000 175.57400 ? 8   GLY A O   1 
ATOM   1566 N N   . GLY B 2 9   ? 53.97441 -63.80852 23.24237  1.000 175.23124 ? 9   GLY A N   1 
ATOM   1567 C CA  . GLY B 2 9   ? 53.46047 -64.82087 22.33598  1.000 173.20584 ? 9   GLY A CA  1 
ATOM   1568 C C   . GLY B 2 9   ? 53.19597 -66.14172 23.02726  1.000 177.40046 ? 9   GLY A C   1 
ATOM   1569 O O   . GLY B 2 9   ? 52.96197 -66.16601 24.23913  1.000 180.00060 ? 9   GLY A O   1 
ATOM   1570 N N   . GLY B 2 10  ? 53.22648 -67.24433 22.28121  1.000 186.08892 ? 10  GLY A N   1 
ATOM   1571 C CA  . GLY B 2 10  ? 53.05851 -68.54898 22.89189  1.000 190.31902 ? 10  GLY A CA  1 
ATOM   1572 C C   . GLY B 2 10  ? 51.86682 -69.34856 22.41162  1.000 189.31625 ? 10  GLY A C   1 
ATOM   1573 O O   . GLY B 2 10  ? 51.24365 -69.00829 21.40268  1.000 185.26555 ? 10  GLY A O   1 
ATOM   1574 N N   . LEU B 2 11  ? 51.53901 -70.41265 23.14160  1.000 186.92342 ? 11  LEU A N   1 
ATOM   1575 C CA  . LEU B 2 11  ? 50.48700 -71.33312 22.74334  1.000 188.89829 ? 11  LEU A CA  1 
ATOM   1576 C C   . LEU B 2 11  ? 49.14241 -70.81400 23.23118  1.000 187.21717 ? 11  LEU A C   1 
ATOM   1577 O O   . LEU B 2 11  ? 48.98950 -70.48465 24.41232  1.000 188.11374 ? 11  LEU A O   1 
ATOM   1578 C CB  . LEU B 2 11  ? 50.75440 -72.72540 23.31229  1.000 195.72223 ? 11  LEU A CB  1 
ATOM   1579 C CG  . LEU B 2 11  ? 49.78868 -73.81127 22.85071  1.000 199.28355 ? 11  LEU A CG  1 
ATOM   1580 C CD1 . LEU B 2 11  ? 49.94967 -74.00522 21.35510  1.000 197.75839 ? 11  LEU A CD1 1 
ATOM   1581 C CD2 . LEU B 2 11  ? 50.03427 -75.11849 23.59366  1.000 206.43799 ? 11  LEU A CD2 1 
ATOM   1582 N N   . VAL B 2 12  ? 48.16876 -70.75976 22.32509  1.000 201.97362 ? 12  VAL A N   1 
ATOM   1583 C CA  . VAL B 2 12  ? 46.82978 -70.27352 22.63213  1.000 200.72772 ? 12  VAL A CA  1 
ATOM   1584 C C   . VAL B 2 12  ? 45.80454 -71.26033 22.08877  1.000 202.68014 ? 12  VAL A C   1 
ATOM   1585 O O   . VAL B 2 12  ? 45.92397 -71.73937 20.95580  1.000 202.50934 ? 12  VAL A O   1 
ATOM   1586 C CB  . VAL B 2 12  ? 46.58824 -68.85831 22.05692  1.000 195.72579 ? 12  VAL A CB  1 
ATOM   1587 C CG1 . VAL B 2 12  ? 46.87165 -68.81719 20.56384  1.000 192.91313 ? 12  VAL A CG1 1 
ATOM   1588 C CG2 . VAL B 2 12  ? 45.16388 -68.38852 22.34651  1.000 194.84543 ? 12  VAL A CG2 1 
ATOM   1589 N N   . GLN B 2 13  ? 44.80254 -71.56866 22.89852  1.000 211.82814 ? 13  GLN A N   1 
ATOM   1590 C CA  . GLN B 2 13  ? 43.70053 -72.40458 22.43325  1.000 214.26180 ? 13  GLN A CA  1 
ATOM   1591 C C   . GLN B 2 13  ? 42.84166 -71.59895 21.46671  1.000 210.96017 ? 13  GLN A C   1 
ATOM   1592 O O   . GLN B 2 13  ? 42.54352 -70.42834 21.74320  1.000 207.63889 ? 13  GLN A O   1 
ATOM   1593 C CB  . GLN B 2 13  ? 42.88154 -72.89647 23.62847  1.000 217.80687 ? 13  GLN A CB  1 
ATOM   1594 C CG  . GLN B 2 13  ? 42.18516 -74.23433 23.42128  1.000 223.37552 ? 13  GLN A CG  1 
ATOM   1595 C CD  . GLN B 2 13  ? 43.15574 -75.37590 23.17475  1.000 227.84516 ? 13  GLN A CD  1 
ATOM   1596 O OE1 . GLN B 2 13  ? 44.26080 -75.40145 23.71949  1.000 227.63092 ? 13  GLN A OE1 1 
ATOM   1597 N NE2 . GLN B 2 13  ? 42.75107 -76.31967 22.33446  1.000 232.33019 ? 13  GLN A NE2 1 
ATOM   1598 N N   . PRO B 2 14  ? 42.42167 -72.16360 20.33253  1.000 210.63843 ? 14  PRO A N   1 
ATOM   1599 C CA  . PRO B 2 14  ? 41.69877 -71.36905 19.33765  1.000 207.97035 ? 14  PRO A CA  1 
ATOM   1600 C C   . PRO B 2 14  ? 40.35971 -70.88640 19.86478  1.000 208.21857 ? 14  PRO A C   1 
ATOM   1601 O O   . PRO B 2 14  ? 39.74430 -71.51183 20.73115  1.000 211.72199 ? 14  PRO A O   1 
ATOM   1602 C CB  . PRO B 2 14  ? 41.52483 -72.33836 18.16870  1.000 211.04010 ? 14  PRO A CB  1 
ATOM   1603 C CG  . PRO B 2 14  ? 41.44142 -73.66430 18.81992  1.000 216.94065 ? 14  PRO A CG  1 
ATOM   1604 C CD  . PRO B 2 14  ? 42.38539 -73.60196 20.00286  1.000 215.98912 ? 14  PRO A CD  1 
ATOM   1605 N N   . GLY B 2 15  ? 39.91393 -69.75185 19.32538  1.000 201.31903 ? 15  GLY A N   1 
ATOM   1606 C CA  . GLY B 2 15  ? 38.79671 -69.03134 19.88502  1.000 200.92950 ? 15  GLY A CA  1 
ATOM   1607 C C   . GLY B 2 15  ? 39.12829 -68.23939 21.12527  1.000 198.61430 ? 15  GLY A C   1 
ATOM   1608 O O   . GLY B 2 15  ? 38.28598 -67.45842 21.58245  1.000 197.12470 ? 15  GLY A O   1 
ATOM   1609 N N   . GLY B 2 16  ? 40.32574 -68.40768 21.68503  1.000 202.45517 ? 16  GLY A N   1 
ATOM   1610 C CA  . GLY B 2 16  ? 40.73692 -67.68783 22.87415  1.000 200.95054 ? 16  GLY A CA  1 
ATOM   1611 C C   . GLY B 2 16  ? 41.24694 -66.30204 22.55109  1.000 196.28978 ? 16  GLY A C   1 
ATOM   1612 O O   . GLY B 2 16  ? 40.82937 -65.66904 21.57428  1.000 193.86270 ? 16  GLY A O   1 
ATOM   1613 N N   . SER B 2 17  ? 42.17097 -65.82030 23.37880  1.000 199.16582 ? 17  SER A N   1 
ATOM   1614 C CA  . SER B 2 17  ? 42.72837 -64.48856 23.20252  1.000 195.25672 ? 17  SER A CA  1 
ATOM   1615 C C   . SER B 2 17  ? 44.23460 -64.52891 23.41520  1.000 196.25753 ? 17  SER A C   1 
ATOM   1616 O O   . SER B 2 17  ? 44.78508 -65.49666 23.94697  1.000 199.72843 ? 17  SER A O   1 
ATOM   1617 C CB  . SER B 2 17  ? 42.08189 -63.47916 24.15953  1.000 192.49332 ? 17  SER A CB  1 
ATOM   1618 O OG  . SER B 2 17  ? 40.68324 -63.41115 23.94672  1.000 191.50307 ? 17  SER A OG  1 
ATOM   1619 N N   . LEU B 2 18  ? 44.89688 -63.45235 22.99193  1.000 179.39659 ? 18  LEU A N   1 
ATOM   1620 C CA  . LEU B 2 18  ? 46.34821 -63.35481 23.10201  1.000 180.48276 ? 18  LEU A CA  1 
ATOM   1621 C C   . LEU B 2 18  ? 46.81338 -61.92069 22.87656  1.000 177.69302 ? 18  LEU A C   1 
ATOM   1622 O O   . LEU B 2 18  ? 46.57367 -61.35026 21.80820  1.000 174.35536 ? 18  LEU A O   1 
ATOM   1623 C CB  . LEU B 2 18  ? 47.01959 -64.30447 22.10397  1.000 180.93445 ? 18  LEU A CB  1 
ATOM   1624 C CG  . LEU B 2 18  ? 48.54642 -64.35046 22.05533  1.000 181.80825 ? 18  LEU A CG  1 
ATOM   1625 C CD1 . LEU B 2 18  ? 49.09790 -64.72100 23.41561  1.000 186.40511 ? 18  LEU A CD1 1 
ATOM   1626 C CD2 . LEU B 2 18  ? 49.00106 -65.35490 21.00457  1.000 181.28386 ? 18  LEU A CD2 1 
ATOM   1627 N N   . ARG B 2 19  ? 47.46568 -61.32618 23.87536  1.000 164.74940 ? 19  ARG A N   1 
ATOM   1628 C CA  . ARG B 2 19  ? 47.93459 -59.94554 23.80954  1.000 162.18939 ? 19  ARG A CA  1 
ATOM   1629 C C   . ARG B 2 19  ? 49.44568 -59.93583 23.61704  1.000 164.10171 ? 19  ARG A C   1 
ATOM   1630 O O   . ARG B 2 19  ? 50.18850 -60.42768 24.47386  1.000 167.56177 ? 19  ARG A O   1 
ATOM   1631 C CB  . ARG B 2 19  ? 47.54587 -59.17302 25.07064  1.000 162.52623 ? 19  ARG A CB  1 
ATOM   1632 N N   . LEU B 2 20  ? 49.89266 -59.37918 22.49542  1.000 171.88138 ? 20  LEU A N   1 
ATOM   1633 C CA  . LEU B 2 20  ? 51.30949 -59.30624 22.17562  1.000 170.29338 ? 20  LEU A CA  1 
ATOM   1634 C C   . LEU B 2 20  ? 51.89655 -57.98762 22.65981  1.000 170.46691 ? 20  LEU A C   1 
ATOM   1635 O O   . LEU B 2 20  ? 51.20117 -56.97321 22.75843  1.000 170.42766 ? 20  LEU A O   1 
ATOM   1636 C CB  . LEU B 2 20  ? 51.53621 -59.45357 20.66942  1.000 164.13688 ? 20  LEU A CB  1 
ATOM   1637 C CG  . LEU B 2 20  ? 51.28815 -60.84321 20.07871  1.000 164.51955 ? 20  LEU A CG  1 
ATOM   1638 C CD1 . LEU B 2 20  ? 51.91665 -60.97594 18.69708  1.000 160.99880 ? 20  LEU A CD1 1 
ATOM   1639 C CD2 . LEU B 2 20  ? 51.80143 -61.92264 21.01463  1.000 170.29234 ? 20  LEU A CD2 1 
ATOM   1640 N N   . SER B 2 21  ? 53.19292 -58.01282 22.96079  1.000 174.84607 ? 21  SER A N   1 
ATOM   1641 C CA  . SER B 2 21  ? 53.89459 -56.84163 23.46593  1.000 175.53755 ? 21  SER A CA  1 
ATOM   1642 C C   . SER B 2 21  ? 55.28685 -56.79264 22.86140  1.000 172.52291 ? 21  SER A C   1 
ATOM   1643 O O   . SER B 2 21  ? 56.00522 -57.79666 22.86705  1.000 174.23174 ? 21  SER A O   1 
ATOM   1644 C CB  . SER B 2 21  ? 53.98652 -56.86539 24.99544  1.000 182.70514 ? 21  SER A CB  1 
ATOM   1645 O OG  . SER B 2 21  ? 52.72041 -56.63321 25.58624  1.000 185.46129 ? 21  SER A OG  1 
ATOM   1646 N N   . CYS B 2 22  ? 55.66424 -55.62391 22.34928  1.000 176.50822 ? 22  CYS A N   1 
ATOM   1647 C CA  . CYS B 2 22  ? 56.98665 -55.41916 21.76653  1.000 174.82743 ? 22  CYS A CA  1 
ATOM   1648 C C   . CYS B 2 22  ? 57.45020 -54.01495 22.12116  1.000 175.38473 ? 22  CYS A C   1 
ATOM   1649 O O   . CYS B 2 22  ? 56.91467 -53.03362 21.59652  1.000 172.90916 ? 22  CYS A O   1 
ATOM   1650 C CB  . CYS B 2 22  ? 56.96091 -55.60874 20.25417  1.000 170.51741 ? 22  CYS A CB  1 
ATOM   1651 S SG  . CYS B 2 22  ? 58.32112 -54.78358 19.40940  1.000 169.94259 ? 22  CYS A SG  1 
ATOM   1652 N N   . ALA B 2 23  ? 58.44284 -53.91791 22.99955  1.000 179.97878 ? 23  ALA A N   1 
ATOM   1653 C CA  . ALA B 2 23  ? 58.92246 -52.62194 23.45183  1.000 181.57703 ? 23  ALA A CA  1 
ATOM   1654 C C   . ALA B 2 23  ? 59.92470 -52.03956 22.46468  1.000 179.17044 ? 23  ALA A C   1 
ATOM   1655 O O   . ALA B 2 23  ? 60.73489 -52.76132 21.87549  1.000 179.18251 ? 23  ALA A O   1 
ATOM   1656 C CB  . ALA B 2 23  ? 59.55903 -52.74030 24.83654  1.000 187.81292 ? 23  ALA A CB  1 
ATOM   1657 N N   . ALA B 2 24  ? 59.85432 -50.72381 22.28189  1.000 193.00958 ? 24  ALA A N   1 
ATOM   1658 C CA  . ALA B 2 24  ? 60.81452 -49.97333 21.48756  1.000 192.68766 ? 24  ALA A CA  1 
ATOM   1659 C C   . ALA B 2 24  ? 61.51699 -48.96421 22.38331  1.000 196.93536 ? 24  ALA A C   1 
ATOM   1660 O O   . ALA B 2 24  ? 60.89212 -48.36450 23.26437  1.000 198.64410 ? 24  ALA A O   1 
ATOM   1661 C CB  . ALA B 2 24  ? 60.13504 -49.25437 20.31926  1.000 188.98749 ? 24  ALA A CB  1 
ATOM   1662 N N   . SER B 2 25  ? 62.82110 -48.78083 22.15756  1.000 202.64776 ? 25  SER A N   1 
ATOM   1663 C CA  . SER B 2 25  ? 63.58547 -47.85469 22.98796  1.000 207.61473 ? 25  SER A CA  1 
ATOM   1664 C C   . SER B 2 25  ? 63.10837 -46.41839 22.81318  1.000 207.11606 ? 25  SER A C   1 
ATOM   1665 O O   . SER B 2 25  ? 63.26618 -45.59717 23.72395  1.000 211.26537 ? 25  SER A O   1 
ATOM   1666 C CB  . SER B 2 25  ? 65.07785 -47.96450 22.66941  1.000 211.53890 ? 25  SER A CB  1 
ATOM   1667 O OG  . SER B 2 25  ? 65.29950 -48.11322 21.27895  1.000 209.34806 ? 25  SER A OG  1 
ATOM   1668 N N   . GLY B 2 26  ? 62.52051 -46.09718 21.65665  1.000 205.02658 ? 26  GLY A N   1 
ATOM   1669 C CA  . GLY B 2 26  ? 61.97673 -44.77756 21.42313  1.000 204.89436 ? 26  GLY A CA  1 
ATOM   1670 C C   . GLY B 2 26  ? 60.68377 -44.86082 20.63534  1.000 199.96664 ? 26  GLY A C   1 
ATOM   1671 O O   . GLY B 2 26  ? 60.30900 -45.92208 20.12953  1.000 196.73749 ? 26  GLY A O   1 
ATOM   1672 N N   . ASP B 2 27  ? 60.00405 -43.72006 20.54503  1.000 208.77568 ? 27  ASP A N   1 
ATOM   1673 C CA  . ASP B 2 27  ? 58.73478 -43.65505 19.83682  1.000 205.22027 ? 27  ASP A CA  1 
ATOM   1674 C C   . ASP B 2 27  ? 58.96691 -43.44115 18.34238  1.000 203.73115 ? 27  ASP A C   1 
ATOM   1675 O O   . ASP B 2 27  ? 60.04382 -43.02462 17.90601  1.000 206.10763 ? 27  ASP A O   1 
ATOM   1676 C CB  . ASP B 2 27  ? 57.85339 -42.53981 20.40401  1.000 206.94161 ? 27  ASP A CB  1 
ATOM   1677 C CG  . ASP B 2 27  ? 57.60604 -42.69058 21.89669  1.000 209.76119 ? 27  ASP A CG  1 
ATOM   1678 O OD1 . ASP B 2 27  ? 58.58870 -42.72992 22.66853  1.000 214.10761 ? 27  ASP A OD1 1 
ATOM   1679 O OD2 . ASP B 2 27  ? 56.42619 -42.77973 22.29702  1.000 208.40540 ? 27  ASP A OD2 1 
ATOM   1680 N N   . PHE B 2 28  ? 57.93276 -43.72930 17.55321  1.000 181.97855 ? 28  PHE A N   1 
ATOM   1681 C CA  . PHE B 2 28  ? 58.07515 -43.75333 16.10479  1.000 181.13540 ? 28  PHE A CA  1 
ATOM   1682 C C   . PHE B 2 28  ? 56.80884 -43.24176 15.43298  1.000 179.57524 ? 28  PHE A C   1 
ATOM   1683 O O   . PHE B 2 28  ? 55.71978 -43.25137 16.01167  1.000 178.46704 ? 28  PHE A O   1 
ATOM   1684 C CB  . PHE B 2 28  ? 58.39228 -45.16432 15.59669  1.000 179.61543 ? 28  PHE A CB  1 
ATOM   1685 C CG  . PHE B 2 28  ? 59.85913 -45.46146 15.50068  1.000 182.82630 ? 28  PHE A CG  1 
ATOM   1686 C CD1 . PHE B 2 28  ? 60.58791 -45.81866 16.62321  1.000 184.14232 ? 28  PHE A CD1 1 
ATOM   1687 C CD2 . PHE B 2 28  ? 60.50937 -45.38572 14.28156  1.000 185.37110 ? 28  PHE A CD2 1 
ATOM   1688 C CE1 . PHE B 2 28  ? 61.94043 -46.09452 16.52886  1.000 187.89915 ? 28  PHE A CE1 1 
ATOM   1689 C CE2 . PHE B 2 28  ? 61.85823 -45.65963 14.18056  1.000 189.38801 ? 28  PHE A CE2 1 
ATOM   1690 C CZ  . PHE B 2 28  ? 62.57549 -46.01442 15.30486  1.000 190.61513 ? 28  PHE A CZ  1 
ATOM   1691 N N   . TYR B 2 29  ? 56.97970 -42.79557 14.18694  1.000 188.04691 ? 29  TYR A N   1 
ATOM   1692 C CA  . TYR B 2 29  ? 55.85385 -42.39357 13.34942  1.000 185.19902 ? 29  TYR A CA  1 
ATOM   1693 C C   . TYR B 2 29  ? 55.01410 -43.60519 12.97036  1.000 181.73685 ? 29  TYR A C   1 
ATOM   1694 O O   . TYR B 2 29  ? 53.83457 -43.70490 13.32567  1.000 179.53623 ? 29  TYR A O   1 
ATOM   1695 C CB  . TYR B 2 29  ? 56.39376 -41.67704 12.10613  1.000 185.32850 ? 29  TYR A CB  1 
ATOM   1696 C CG  . TYR B 2 29  ? 55.51505 -41.64683 10.86430  1.000 179.90007 ? 29  TYR A CG  1 
ATOM   1697 C CD1 . TYR B 2 29  ? 54.63360 -40.60310 10.64316  1.000 179.58197 ? 29  TYR A CD1 1 
ATOM   1698 C CD2 . TYR B 2 29  ? 55.61949 -42.62213 9.88194   1.000 175.64925 ? 29  TYR A CD2 1 
ATOM   1699 C CE1 . TYR B 2 29  ? 53.84195 -40.55562 9.51106   1.000 175.05601 ? 29  TYR A CE1 1 
ATOM   1700 C CE2 . TYR B 2 29  ? 54.84672 -42.57557 8.73773   1.000 170.88011 ? 29  TYR A CE2 1 
ATOM   1701 C CZ  . TYR B 2 29  ? 53.95783 -41.53913 8.55743   1.000 170.56016 ? 29  TYR A CZ  1 
ATOM   1702 O OH  . TYR B 2 29  ? 53.17569 -41.48368 7.42589   1.000 166.43889 ? 29  TYR A OH  1 
ATOM   1703 N N   . CYS B 2 30  ? 55.62538 -44.55263 12.27519  1.000 177.02625 ? 30  CYS A N   1 
ATOM   1704 C CA  . CYS B 2 30  ? 54.96426 -45.76362 11.82234  1.000 175.45271 ? 30  CYS A CA  1 
ATOM   1705 C C   . CYS B 2 30  ? 55.25616 -46.89717 12.79594  1.000 176.97017 ? 30  CYS A C   1 
ATOM   1706 O O   . CYS B 2 30  ? 56.41354 -47.12640 13.16243  1.000 179.30110 ? 30  CYS A O   1 
ATOM   1707 C CB  . CYS B 2 30  ? 55.44895 -46.12994 10.42010  1.000 176.48166 ? 30  CYS A CB  1 
ATOM   1708 S SG  . CYS B 2 30  ? 54.37724 -47.22520 9.47489   1.000 175.85124 ? 30  CYS A SG  1 
ATOM   1709 N N   . MET B 2 31  ? 54.20886 -47.60696 13.20706  1.000 160.88755 ? 31  MET A N   1 
ATOM   1710 C CA  . MET B 2 31  ? 54.35662 -48.80536 14.02388  1.000 161.32470 ? 31  MET A CA  1 
ATOM   1711 C C   . MET B 2 31  ? 53.37704 -49.84381 13.50182  1.000 160.91269 ? 31  MET A C   1 
ATOM   1712 O O   . MET B 2 31  ? 52.18257 -49.56016 13.37766  1.000 159.45927 ? 31  MET A O   1 
ATOM   1713 C CB  . MET B 2 31  ? 54.10207 -48.51120 15.50488  1.000 160.94921 ? 31  MET A CB  1 
ATOM   1714 C CG  . MET B 2 31  ? 55.12588 -47.60169 16.16735  1.000 162.53761 ? 31  MET A CG  1 
ATOM   1715 S SD  . MET B 2 31  ? 54.68425 -47.28340 17.88701  1.000 164.13227 ? 31  MET A SD  1 
ATOM   1716 C CE  . MET B 2 31  ? 55.97463 -46.15261 18.38666  1.000 166.73069 ? 31  MET A CE  1 
ATOM   1717 N N   . ALA B 2 32  ? 53.87463 -51.03561 13.17938  1.000 159.82005 ? 32  ALA A N   1 
ATOM   1718 C CA  . ALA B 2 32  ? 53.00906 -52.07423 12.64177  1.000 160.65313 ? 32  ALA A CA  1 
ATOM   1719 C C   . ALA B 2 32  ? 53.53273 -53.44496 13.03609  1.000 161.03288 ? 32  ALA A C   1 
ATOM   1720 O O   . ALA B 2 32  ? 54.69647 -53.60812 13.41045  1.000 161.13545 ? 32  ALA A O   1 
ATOM   1721 C CB  . ALA B 2 32  ? 52.88644 -51.98354 11.11681  1.000 163.72259 ? 32  ALA A CB  1 
ATOM   1722 N N   . TRP B 2 33  ? 52.65093 -54.43308 12.93677  1.000 161.13480 ? 33  TRP A N   1 
ATOM   1723 C CA  . TRP B 2 33  ? 52.98409 -55.82095 13.20558  1.000 160.81327 ? 33  TRP A CA  1 
ATOM   1724 C C   . TRP B 2 33  ? 53.02711 -56.60211 11.89990  1.000 163.49568 ? 33  TRP A C   1 
ATOM   1725 O O   . TRP B 2 33  ? 52.36976 -56.24049 10.92010  1.000 165.39601 ? 33  TRP A O   1 
ATOM   1726 C CB  . TRP B 2 33  ? 51.96888 -56.45814 14.15094  1.000 159.17089 ? 33  TRP A CB  1 
ATOM   1727 C CG  . TRP B 2 33  ? 52.11969 -56.02937 15.56790  1.000 158.07730 ? 33  TRP A CG  1 
ATOM   1728 C CD1 . TRP B 2 33  ? 51.55441 -54.93771 16.15484  1.000 157.70197 ? 33  TRP A CD1 1 
ATOM   1729 C CD2 . TRP B 2 33  ? 52.89052 -56.67944 16.58449  1.000 158.77644 ? 33  TRP A CD2 1 
ATOM   1730 N NE1 . TRP B 2 33  ? 51.91948 -54.86978 17.47580  1.000 158.63598 ? 33  TRP A NE1 1 
ATOM   1731 C CE2 . TRP B 2 33  ? 52.74351 -55.92523 17.76429  1.000 159.37545 ? 33  TRP A CE2 1 
ATOM   1732 C CE3 . TRP B 2 33  ? 53.68988 -57.82615 16.61198  1.000 160.24449 ? 33  TRP A CE3 1 
ATOM   1733 C CZ2 . TRP B 2 33  ? 53.36406 -56.28039 18.95977  1.000 161.83072 ? 33  TRP A CZ2 1 
ATOM   1734 C CZ3 . TRP B 2 33  ? 54.30594 -58.17693 17.79986  1.000 162.27958 ? 33  TRP A CZ3 1 
ATOM   1735 C CH2 . TRP B 2 33  ? 54.13949 -57.40662 18.95694  1.000 163.17652 ? 33  TRP A CH2 1 
ATOM   1736 N N   . PHE B 2 34  ? 53.79873 -57.68716 11.89575  1.000 164.88452 ? 34  PHE A N   1 
ATOM   1737 C CA  . PHE B 2 34  ? 53.99571 -58.48619 10.68892  1.000 168.37701 ? 34  PHE A CA  1 
ATOM   1738 C C   . PHE B 2 34  ? 53.99163 -59.96069 11.06956  1.000 168.64160 ? 34  PHE A C   1 
ATOM   1739 O O   . PHE B 2 34  ? 54.91220 -60.43074 11.74500  1.000 169.15613 ? 34  PHE A O   1 
ATOM   1740 C CB  . PHE B 2 34  ? 55.30148 -58.10547 9.98901   1.000 171.78487 ? 34  PHE A CB  1 
ATOM   1741 C CG  . PHE B 2 34  ? 55.11068 -57.23722 8.77542   1.000 174.38488 ? 34  PHE A CG  1 
ATOM   1742 C CD1 . PHE B 2 34  ? 54.78563 -55.89727 8.90883   1.000 173.70251 ? 34  PHE A CD1 1 
ATOM   1743 C CD2 . PHE B 2 34  ? 55.25838 -57.75899 7.50274   1.000 177.99082 ? 34  PHE A CD2 1 
ATOM   1744 C CE1 . PHE B 2 34  ? 54.61077 -55.09669 7.79432   1.000 176.63519 ? 34  PHE A CE1 1 
ATOM   1745 C CE2 . PHE B 2 34  ? 55.08490 -56.96347 6.38505   1.000 180.63676 ? 34  PHE A CE2 1 
ATOM   1746 C CZ  . PHE B 2 34  ? 54.76062 -55.63157 6.53154   1.000 179.92036 ? 34  PHE A CZ  1 
ATOM   1747 N N   . ARG B 2 35  ? 52.96384 -60.68627 10.63434  1.000 168.54385 ? 35  ARG A N   1 
ATOM   1748 C CA  . ARG B 2 35  ? 52.86796 -62.12101 10.86833  1.000 169.89676 ? 35  ARG A CA  1 
ATOM   1749 C C   . ARG B 2 35  ? 53.46623 -62.88672 9.69596   1.000 173.75811 ? 35  ARG A C   1 
ATOM   1750 O O   . ARG B 2 35  ? 53.17360 -62.59264 8.53253   1.000 175.34911 ? 35  ARG A O   1 
ATOM   1751 C CB  . ARG B 2 35  ? 51.41152 -62.53809 11.07440  1.000 169.45529 ? 35  ARG A CB  1 
ATOM   1752 C CG  . ARG B 2 35  ? 51.04797 -63.89441 10.49980  1.000 172.76274 ? 35  ARG A CG  1 
ATOM   1753 C CD  . ARG B 2 35  ? 49.58912 -64.23833 10.74500  1.000 173.07009 ? 35  ARG A CD  1 
ATOM   1754 N NE  . ARG B 2 35  ? 48.68780 -63.46955 9.89487   1.000 173.35993 ? 35  ARG A NE  1 
ATOM   1755 C CZ  . ARG B 2 35  ? 47.53434 -62.95572 10.29886  1.000 172.36742 ? 35  ARG A CZ  1 
ATOM   1756 N NH1 . ARG B 2 35  ? 47.10591 -63.11169 11.54076  1.000 170.93579 ? 35  ARG A NH1 1 
ATOM   1757 N NH2 . ARG B 2 35  ? 46.79096 -62.27091 9.43441   1.000 173.60474 ? 35  ARG A NH2 1 
ATOM   1758 N N   . GLN B 2 36  ? 54.29994 -63.87712 10.01634  1.000 176.71119 ? 36  GLN A N   1 
ATOM   1759 C CA  . GLN B 2 36  ? 55.02779 -64.66461 9.02606   1.000 181.08222 ? 36  GLN A CA  1 
ATOM   1760 C C   . GLN B 2 36  ? 54.94035 -66.13172 9.41952   1.000 183.59735 ? 36  GLN A C   1 
ATOM   1761 O O   . GLN B 2 36  ? 55.38138 -66.50570 10.51138  1.000 183.71668 ? 36  GLN A O   1 
ATOM   1762 C CB  . GLN B 2 36  ? 56.48600 -64.20480 8.94462   1.000 183.16493 ? 36  GLN A CB  1 
ATOM   1763 C CG  . GLN B 2 36  ? 57.45513 -65.15748 8.28177   1.000 188.53177 ? 36  GLN A CG  1 
ATOM   1764 C CD  . GLN B 2 36  ? 57.73163 -64.83483 6.82626   1.000 191.26178 ? 36  GLN A CD  1 
ATOM   1765 O OE1 . GLN B 2 36  ? 57.87938 -63.67174 6.44279   1.000 190.53397 ? 36  GLN A OE1 1 
ATOM   1766 N NE2 . GLN B 2 36  ? 57.82567 -65.87248 6.00854   1.000 195.03081 ? 36  GLN A NE2 1 
ATOM   1767 N N   . ALA B 2 37  ? 54.39403 -66.97048 8.52362   1.000 188.89861 ? 37  ALA A N   1 
ATOM   1768 C CA  . ALA B 2 37  ? 54.09686 -68.36913 8.84047   1.000 191.71011 ? 37  ALA A CA  1 
ATOM   1769 C C   . ALA B 2 37  ? 54.97009 -69.32875 8.03251   1.000 196.92444 ? 37  ALA A C   1 
ATOM   1770 O O   . ALA B 2 37  ? 55.64798 -68.89032 7.09437   1.000 198.21389 ? 37  ALA A O   1 
ATOM   1771 C CB  . ALA B 2 37  ? 52.61526 -68.64870 8.59143   1.000 191.51189 ? 37  ALA A CB  1 
ATOM   1772 N N   . PRO B 2 38  ? 55.00626 -70.64727 8.37714   1.000 182.36196 ? 38  PRO A N   1 
ATOM   1773 C CA  . PRO B 2 38  ? 55.77585 -71.60504 7.56641   1.000 188.85680 ? 38  PRO A CA  1 
ATOM   1774 C C   . PRO B 2 38  ? 55.46721 -71.55265 6.07763   1.000 193.11136 ? 38  PRO A C   1 
ATOM   1775 O O   . PRO B 2 38  ? 54.38269 -71.94744 5.63782   1.000 197.62929 ? 38  PRO A O   1 
ATOM   1776 C CB  . PRO B 2 38  ? 55.38802 -72.96052 8.17178   1.000 195.68427 ? 38  PRO A CB  1 
ATOM   1777 C CG  . PRO B 2 38  ? 55.11410 -72.65803 9.59144   1.000 189.92513 ? 38  PRO A CG  1 
ATOM   1778 C CD  . PRO B 2 38  ? 54.49961 -71.27541 9.61290   1.000 182.80610 ? 38  PRO A CD  1 
ATOM   1779 N N   . GLY B 2 39  ? 56.43245 -71.07654 5.29223   1.000 192.85753 ? 39  GLY A N   1 
ATOM   1780 C CA  . GLY B 2 39  ? 56.24174 -70.88134 3.87178   1.000 197.18022 ? 39  GLY A CA  1 
ATOM   1781 C C   . GLY B 2 39  ? 55.43491 -69.65804 3.49516   1.000 191.19309 ? 39  GLY A C   1 
ATOM   1782 O O   . GLY B 2 39  ? 55.29556 -69.37446 2.29828   1.000 194.71528 ? 39  GLY A O   1 
ATOM   1783 N N   . LYS B 2 40  ? 54.90262 -68.92363 4.46912   1.000 200.91599 ? 40  LYS A N   1 
ATOM   1784 C CA  . LYS B 2 40  ? 54.08329 -67.74359 4.22206   1.000 197.69848 ? 40  LYS A CA  1 
ATOM   1785 C C   . LYS B 2 40  ? 54.86706 -66.50323 4.62859   1.000 194.63959 ? 40  LYS A C   1 
ATOM   1786 O O   . LYS B 2 40  ? 55.32861 -66.40209 5.77061   1.000 192.22615 ? 40  LYS A O   1 
ATOM   1787 C CB  . LYS B 2 40  ? 52.76208 -67.82471 4.98654   1.000 194.76169 ? 40  LYS A CB  1 
ATOM   1788 N N   . GLU B 2 41  ? 55.00589 -65.56437 3.69647   1.000 200.86113 ? 41  GLU A N   1 
ATOM   1789 C CA  . GLU B 2 41  ? 55.81153 -64.37432 3.92193   1.000 199.33028 ? 41  GLU A CA  1 
ATOM   1790 C C   . GLU B 2 41  ? 55.10791 -63.41991 4.88861   1.000 194.22968 ? 41  GLU A C   1 
ATOM   1791 O O   . GLU B 2 41  ? 53.89139 -63.47659 5.09000   1.000 192.25688 ? 41  GLU A O   1 
ATOM   1792 C CB  . GLU B 2 41  ? 56.14755 -63.71566 2.57398   1.000 202.54931 ? 41  GLU A CB  1 
ATOM   1793 C CG  . GLU B 2 41  ? 55.13032 -62.72779 1.98422   1.000 201.48932 ? 41  GLU A CG  1 
ATOM   1794 C CD  . GLU B 2 41  ? 55.09057 -61.38964 2.69521   1.000 197.91301 ? 41  GLU A CD  1 
ATOM   1795 O OE1 . GLU B 2 41  ? 56.13860 -60.97141 3.22795   1.000 197.10593 ? 41  GLU A OE1 1 
ATOM   1796 O OE2 . GLU B 2 41  ? 54.00974 -60.76320 2.72419   1.000 196.52207 ? 41  GLU A OE2 1 
ATOM   1797 N N   . ARG B 2 42  ? 55.90217 -62.53748 5.49771   1.000 187.06126 ? 42  ARG A N   1 
ATOM   1798 C CA  . ARG B 2 42  ? 55.40870 -61.66730 6.56097   1.000 182.43466 ? 42  ARG A CA  1 
ATOM   1799 C C   . ARG B 2 42  ? 54.38383 -60.67648 6.01769   1.000 181.43944 ? 42  ARG A C   1 
ATOM   1800 O O   . ARG B 2 42  ? 54.71677 -59.79944 5.21384   1.000 183.47991 ? 42  ARG A O   1 
ATOM   1801 C CB  . ARG B 2 42  ? 56.57147 -60.92833 7.21950   1.000 182.43578 ? 42  ARG A CB  1 
ATOM   1802 N N   . GLU B 2 43  ? 53.14333 -60.80031 6.47598   1.000 178.19486 ? 43  GLU A N   1 
ATOM   1803 C CA  . GLU B 2 43  ? 52.05653 -59.94268 6.03207   1.000 177.96487 ? 43  GLU A CA  1 
ATOM   1804 C C   . GLU B 2 43  ? 51.76448 -58.87189 7.07444   1.000 174.47848 ? 43  GLU A C   1 
ATOM   1805 O O   . GLU B 2 43  ? 51.93792 -59.08300 8.27742   1.000 171.64925 ? 43  GLU A O   1 
ATOM   1806 C CB  . GLU B 2 43  ? 50.79248 -60.75997 5.76121   1.000 178.98264 ? 43  GLU A CB  1 
ATOM   1807 C CG  . GLU B 2 43  ? 50.36991 -61.64558 6.92180   1.000 176.80489 ? 43  GLU A CG  1 
ATOM   1808 C CD  . GLU B 2 43  ? 49.35154 -62.69153 6.51618   1.000 179.45435 ? 43  GLU A CD  1 
ATOM   1809 O OE1 . GLU B 2 43  ? 48.97206 -62.72437 5.32667   1.000 182.50045 ? 43  GLU A OE1 1 
ATOM   1810 O OE2 . GLU B 2 43  ? 48.93051 -63.48111 7.38746   1.000 179.01566 ? 43  GLU A OE2 1 
ATOM   1811 N N   . ALA B 2 44  ? 51.31614 -57.71523 6.59592   1.000 163.05256 ? 44  ALA A N   1 
ATOM   1812 C CA  . ALA B 2 44  ? 50.97283 -56.59989 7.46968   1.000 160.48133 ? 44  ALA A CA  1 
ATOM   1813 C C   . ALA B 2 44  ? 49.63752 -56.89347 8.14210   1.000 158.96446 ? 44  ALA A C   1 
ATOM   1814 O O   . ALA B 2 44  ? 48.58905 -56.88871 7.48909   1.000 160.42952 ? 44  ALA A O   1 
ATOM   1815 C CB  . ALA B 2 44  ? 50.92229 -55.29891 6.67536   1.000 161.78843 ? 44  ALA A CB  1 
ATOM   1816 N N   . VAL B 2 45  ? 49.67559 -57.14850 9.44584   1.000 167.84953 ? 45  VAL A N   1 
ATOM   1817 C CA  . VAL B 2 45  ? 48.47397 -57.48343 10.20314  1.000 166.13037 ? 45  VAL A CA  1 
ATOM   1818 C C   . VAL B 2 45  ? 47.78996 -56.23574 10.73993  1.000 164.85424 ? 45  VAL A C   1 
ATOM   1819 O O   . VAL B 2 45  ? 46.57375 -56.07572 10.60985  1.000 165.13264 ? 45  VAL A O   1 
ATOM   1820 C CB  . VAL B 2 45  ? 48.83312 -58.46181 11.34058  1.000 164.09610 ? 45  VAL A CB  1 
ATOM   1821 C CG1 . VAL B 2 45  ? 47.58753 -58.90304 12.08235  1.000 163.85009 ? 45  VAL A CG1 1 
ATOM   1822 C CG2 . VAL B 2 45  ? 49.55837 -59.65568 10.77754  1.000 165.95516 ? 45  VAL A CG2 1 
ATOM   1823 N N   . ALA B 2 46  ? 48.55698 -55.33091 11.34318  1.000 165.15355 ? 46  ALA A N   1 
ATOM   1824 C CA  . ALA B 2 46  ? 47.98844 -54.15361 11.98041  1.000 161.75913 ? 46  ALA A CA  1 
ATOM   1825 C C   . ALA B 2 46  ? 49.01295 -53.03000 11.98152  1.000 160.75113 ? 46  ALA A C   1 
ATOM   1826 O O   . ALA B 2 46  ? 50.19831 -53.26973 12.21627  1.000 161.70769 ? 46  ALA A O   1 
ATOM   1827 C CB  . ALA B 2 46  ? 47.54052 -54.46403 13.41019  1.000 160.05830 ? 46  ALA A CB  1 
ATOM   1828 N N   . ALA B 2 47  ? 48.54572 -51.80770 11.72696  1.000 167.82239 ? 47  ALA A N   1 
ATOM   1829 C CA  . ALA B 2 47  ? 49.39674 -50.62785 11.67299  1.000 166.37430 ? 47  ALA A CA  1 
ATOM   1830 C C   . ALA B 2 47  ? 48.74708 -49.49274 12.45284  1.000 162.05491 ? 47  ALA A C   1 
ATOM   1831 O O   . ALA B 2 47  ? 47.55351 -49.52860 12.76272  1.000 159.78576 ? 47  ALA A O   1 
ATOM   1832 C CB  . ALA B 2 47  ? 49.65827 -50.18689 10.22697  1.000 167.26185 ? 47  ALA A CB  1 
ATOM   1833 N N   . ILE B 2 48  ? 49.54444 -48.47420 12.76747  1.000 173.60987 ? 48  ILE A N   1 
ATOM   1834 C CA  . ILE B 2 48  ? 49.04669 -47.32883 13.52398  1.000 171.29639 ? 48  ILE A CA  1 
ATOM   1835 C C   . ILE B 2 48  ? 49.79951 -46.08103 13.07965  1.000 170.68226 ? 48  ILE A C   1 
ATOM   1836 O O   . ILE B 2 48  ? 51.00539 -46.12235 12.81741  1.000 173.03570 ? 48  ILE A O   1 
ATOM   1837 C CB  . ILE B 2 48  ? 49.17179 -47.55642 15.04799  1.000 173.55763 ? 48  ILE A CB  1 
ATOM   1838 C CG1 . ILE B 2 48  ? 48.70589 -46.32594 15.83105  1.000 173.17400 ? 48  ILE A CG1 1 
ATOM   1839 C CG2 . ILE B 2 48  ? 50.59123 -47.89660 15.43115  1.000 176.94717 ? 48  ILE A CG2 1 
ATOM   1840 C CD1 . ILE B 2 48  ? 47.26438 -45.94565 15.57339  1.000 169.10661 ? 48  ILE A CD1 1 
ATOM   1841 N N   . ARG B 2 49  ? 49.07148 -44.96714 13.01374  1.000 191.26930 ? 49  ARG A N   1 
ATOM   1842 C CA  . ARG B 2 49  ? 49.57868 -43.68456 12.54189  1.000 190.91449 ? 49  ARG A CA  1 
ATOM   1843 C C   . ARG B 2 49  ? 50.67399 -43.14016 13.46719  1.000 195.50337 ? 49  ARG A C   1 
ATOM   1844 O O   . ARG B 2 49  ? 51.01238 -43.72574 14.49943  1.000 198.56391 ? 49  ARG A O   1 
ATOM   1845 C CB  . ARG B 2 49  ? 48.42389 -42.69065 12.43618  1.000 187.58330 ? 49  ARG A CB  1 
ATOM   1846 C CG  . ARG B 2 49  ? 47.86995 -42.54731 11.04416  1.000 183.51239 ? 49  ARG A CG  1 
ATOM   1847 C CD  . ARG B 2 49  ? 48.93009 -42.03116 10.11257  1.000 184.70772 ? 49  ARG A CD  1 
ATOM   1848 N NE  . ARG B 2 49  ? 48.67890 -42.45342 8.74507   1.000 182.42942 ? 49  ARG A NE  1 
ATOM   1849 C CZ  . ARG B 2 49  ? 49.45280 -42.13570 7.71966   1.000 183.25892 ? 49  ARG A CZ  1 
ATOM   1850 N NH1 . ARG B 2 49  ? 50.46939 -41.30004 7.85602   1.000 185.60820 ? 49  ARG A NH1 1 
ATOM   1851 N NH2 . ARG B 2 49  ? 49.22271 -42.69620 6.53714   1.000 182.62378 ? 49  ARG A NH2 1 
ATOM   1852 N N   . SER B 2 50  ? 51.22493 -41.98113 13.08735  1.000 183.42965 ? 50  SER A N   1 
ATOM   1853 C CA  . SER B 2 50  ? 52.16049 -41.22021 13.91318  1.000 189.00151 ? 50  SER A CA  1 
ATOM   1854 C C   . SER B 2 50  ? 51.47647 -40.68891 15.15284  1.000 191.65756 ? 50  SER A C   1 
ATOM   1855 O O   . SER B 2 50  ? 51.70752 -41.17435 16.26389  1.000 195.20204 ? 50  SER A O   1 
ATOM   1856 C CB  . SER B 2 50  ? 52.72882 -40.03669 13.15103  1.000 190.18951 ? 50  SER A CB  1 
ATOM   1857 O OG  . SER B 2 50  ? 53.22727 -39.05846 14.04335  1.000 195.88991 ? 50  SER A OG  1 
ATOM   1858 N N   . GLY B 2 51  ? 50.65677 -39.66453 14.95784  1.000 203.46799 ? 51  GLY A N   1 
ATOM   1859 C CA  . GLY B 2 51  ? 49.79332 -39.17287 16.00158  1.000 205.87111 ? 51  GLY A CA  1 
ATOM   1860 C C   . GLY B 2 51  ? 48.61880 -40.09903 16.24405  1.000 201.10918 ? 51  GLY A C   1 
ATOM   1861 O O   . GLY B 2 51  ? 47.65184 -39.70928 16.90147  1.000 201.22184 ? 51  GLY A O   1 
ATOM   1862 N N   . GLY B 2 52  ? 48.68503 -41.32177 15.71707  1.000 200.55073 ? 52  GLY A N   1 
ATOM   1863 C CA  . GLY B 2 52  ? 47.62758 -42.29368 15.94135  1.000 197.53358 ? 52  GLY A CA  1 
ATOM   1864 C C   . GLY B 2 52  ? 46.30514 -41.84864 15.35064  1.000 192.50614 ? 52  GLY A C   1 
ATOM   1865 O O   . GLY B 2 52  ? 46.23535 -41.31957 14.23514  1.000 189.19882 ? 52  GLY A O   1 
ATOM   1866 N N   . ARG B 2 53  ? 45.23394 -42.06747 16.11844  1.000 203.04334 ? 53  ARG A N   1 
ATOM   1867 C CA  . ARG B 2 53  ? 43.86677 -41.71003 15.73121  1.000 198.37774 ? 53  ARG A CA  1 
ATOM   1868 C C   . ARG B 2 53  ? 43.47267 -42.33386 14.39373  1.000 192.75427 ? 53  ARG A C   1 
ATOM   1869 O O   . ARG B 2 53  ? 42.59981 -41.81843 13.68986  1.000 188.86978 ? 53  ARG A O   1 
ATOM   1870 C CB  . ARG B 2 53  ? 43.67209 -40.18893 15.69233  1.000 199.58753 ? 53  ARG A CB  1 
ATOM   1871 C CG  . ARG B 2 53  ? 44.52281 -39.40287 16.69466  1.000 206.93503 ? 53  ARG A CG  1 
ATOM   1872 C CD  . ARG B 2 53  ? 44.09450 -39.62677 18.13951  1.000 211.37060 ? 53  ARG A CD  1 
ATOM   1873 N NE  . ARG B 2 53  ? 44.81671 -40.72500 18.77466  1.000 214.19417 ? 53  ARG A NE  1 
ATOM   1874 C CZ  . ARG B 2 53  ? 46.05937 -40.64806 19.23404  1.000 219.40740 ? 53  ARG A CZ  1 
ATOM   1875 N NH1 . ARG B 2 53  ? 46.76233 -39.52996 19.14771  1.000 222.94962 ? 53  ARG A NH1 1 
ATOM   1876 N NH2 . ARG B 2 53  ? 46.61287 -41.72207 19.79053  1.000 221.61900 ? 53  ARG A NH2 1 
ATOM   1877 N N   . SER B 2 54  ? 44.11553 -43.44785 14.03905  1.000 179.96408 ? 54  SER A N   1 
ATOM   1878 C CA  . SER B 2 54  ? 43.83082 -44.16125 12.79958  1.000 177.20034 ? 54  SER A CA  1 
ATOM   1879 C C   . SER B 2 54  ? 44.49981 -45.53028 12.81388  1.000 180.41686 ? 54  SER A C   1 
ATOM   1880 O O   . SER B 2 54  ? 45.72669 -45.62814 12.70815  1.000 183.53302 ? 54  SER A O   1 
ATOM   1881 C CB  . SER B 2 54  ? 44.30059 -43.35488 11.58513  1.000 175.81475 ? 54  SER A CB  1 
ATOM   1882 O OG  . SER B 2 54  ? 43.51309 -43.64419 10.44195  1.000 173.00930 ? 54  SER A OG  1 
ATOM   1883 N N   . THR B 2 55  ? 43.70570 -46.58955 12.94192  1.000 165.11925 ? 55  THR A N   1 
ATOM   1884 C CA  . THR B 2 55  ? 44.21441 -47.95304 12.98978  1.000 169.28638 ? 55  THR A CA  1 
ATOM   1885 C C   . THR B 2 55  ? 43.99890 -48.63964 11.64705  1.000 170.95648 ? 55  THR A C   1 
ATOM   1886 O O   . THR B 2 55  ? 42.98323 -48.42174 10.98144  1.000 168.69407 ? 55  THR A O   1 
ATOM   1887 C CB  . THR B 2 55  ? 43.53197 -48.75424 14.10056  1.000 170.11975 ? 55  THR A CB  1 
ATOM   1888 O OG1 . THR B 2 55  ? 42.15927 -48.35710 14.20786  1.000 166.32065 ? 55  THR A OG1 1 
ATOM   1889 C CG2 . THR B 2 55  ? 44.22825 -48.51863 15.43123  1.000 172.02387 ? 55  THR A CG2 1 
ATOM   1890 N N   . TYR B 2 56  ? 44.96458 -49.46806 11.25321  1.000 176.31836 ? 56  TYR A N   1 
ATOM   1891 C CA  . TYR B 2 56  ? 44.95058 -50.14402 9.95815   1.000 180.26265 ? 56  TYR A CA  1 
ATOM   1892 C C   . TYR B 2 56  ? 45.18219 -51.63121 10.18691  1.000 186.30869 ? 56  TYR A C   1 
ATOM   1893 O O   . TYR B 2 56  ? 46.25561 -52.02612 10.64832  1.000 188.18859 ? 56  TYR A O   1 
ATOM   1894 C CB  . TYR B 2 56  ? 46.01640 -49.57612 9.01665   1.000 180.96784 ? 56  TYR A CB  1 
ATOM   1895 C CG  . TYR B 2 56  ? 45.93759 -48.08711 8.74759   1.000 175.11573 ? 56  TYR A CG  1 
ATOM   1896 C CD1 . TYR B 2 56  ? 46.17497 -47.15624 9.75185   1.000 171.86697 ? 56  TYR A CD1 1 
ATOM   1897 C CD2 . TYR B 2 56  ? 45.63567 -47.61406 7.47776   1.000 173.95244 ? 56  TYR A CD2 1 
ATOM   1898 C CE1 . TYR B 2 56  ? 46.10405 -45.80048 9.50120   1.000 167.95202 ? 56  TYR A CE1 1 
ATOM   1899 C CE2 . TYR B 2 56  ? 45.56435 -46.26049 7.21677   1.000 168.94984 ? 56  TYR A CE2 1 
ATOM   1900 C CZ  . TYR B 2 56  ? 45.79933 -45.35844 8.23148   1.000 166.15430 ? 56  TYR A CZ  1 
ATOM   1901 O OH  . TYR B 2 56  ? 45.72891 -44.00921 7.97492   1.000 162.71688 ? 56  TYR A OH  1 
ATOM   1902 N N   . TYR B 2 57  ? 44.19026 -52.45426 9.85198   1.000 169.48434 ? 57  TYR A N   1 
ATOM   1903 C CA  . TYR B 2 57  ? 44.27524 -53.89260 10.04993  1.000 173.28029 ? 57  TYR A CA  1 
ATOM   1904 C C   . TYR B 2 57  ? 44.14337 -54.62060 8.71910   1.000 177.77543 ? 57  TYR A C   1 
ATOM   1905 O O   . TYR B 2 57  ? 43.59256 -54.09486 7.74844   1.000 178.60664 ? 57  TYR A O   1 
ATOM   1906 C CB  . TYR B 2 57  ? 43.18981 -54.39177 11.01112  1.000 172.25034 ? 57  TYR A CB  1 
ATOM   1907 C CG  . TYR B 2 57  ? 43.21793 -53.71866 12.35607  1.000 167.86439 ? 57  TYR A CG  1 
ATOM   1908 C CD1 . TYR B 2 57  ? 44.12314 -54.11104 13.32659  1.000 168.15116 ? 57  TYR A CD1 1 
ATOM   1909 C CD2 . TYR B 2 57  ? 42.33031 -52.69682 12.65963  1.000 162.95847 ? 57  TYR A CD2 1 
ATOM   1910 C CE1 . TYR B 2 57  ? 44.15876 -53.49636 14.55523  1.000 165.15508 ? 57  TYR A CE1 1 
ATOM   1911 C CE2 . TYR B 2 57  ? 42.35167 -52.07914 13.89177  1.000 159.03625 ? 57  TYR A CE2 1 
ATOM   1912 C CZ  . TYR B 2 57  ? 43.26855 -52.48367 14.83805  1.000 160.80731 ? 57  TYR A CZ  1 
ATOM   1913 O OH  . TYR B 2 57  ? 43.29701 -51.86968 16.06939  1.000 158.78171 ? 57  TYR A OH  1 
ATOM   1914 N N   . ALA B 2 58  ? 44.65911 -55.84584 8.68744   1.000 174.06949 ? 58  ALA A N   1 
ATOM   1915 C CA  . ALA B 2 58  ? 44.49512 -56.70502 7.52642   1.000 178.22414 ? 58  ALA A CA  1 
ATOM   1916 C C   . ALA B 2 58  ? 43.08163 -57.26987 7.48690   1.000 179.92681 ? 58  ALA A C   1 
ATOM   1917 O O   . ALA B 2 58  ? 42.45805 -57.50759 8.52477   1.000 178.56971 ? 58  ALA A O   1 
ATOM   1918 C CB  . ALA B 2 58  ? 45.51186 -57.84628 7.54823   1.000 179.38188 ? 58  ALA A CB  1 
ATOM   1919 N N   . ASP B 2 59  ? 42.57903 -57.48721 6.26745   1.000 186.96772 ? 59  ASP A N   1 
ATOM   1920 C CA  . ASP B 2 59  ? 41.22462 -58.00718 6.10063   1.000 189.43511 ? 59  ASP A CA  1 
ATOM   1921 C C   . ASP B 2 59  ? 41.01639 -59.30469 6.86599   1.000 190.31495 ? 59  ASP A C   1 
ATOM   1922 O O   . ASP B 2 59  ? 39.91029 -59.57328 7.34841   1.000 191.08710 ? 59  ASP A O   1 
ATOM   1923 C CB  . ASP B 2 59  ? 40.92415 -58.22455 4.61839   1.000 194.03678 ? 59  ASP A CB  1 
ATOM   1924 C CG  . ASP B 2 59  ? 40.80612 -56.92622 3.85535   1.000 192.96735 ? 59  ASP A CG  1 
ATOM   1925 O OD1 . ASP B 2 59  ? 39.97466 -56.08178 4.24780   1.000 189.95931 ? 59  ASP A OD1 1 
ATOM   1926 O OD2 . ASP B 2 59  ? 41.54817 -56.74748 2.86727   1.000 194.73133 ? 59  ASP A OD2 1 
ATOM   1927 N N   . SER B 2 60  ? 42.06550 -60.11709 6.99409   1.000 194.84433 ? 60  SER A N   1 
ATOM   1928 C CA  . SER B 2 60  ? 41.95751 -61.36435 7.73754   1.000 195.33956 ? 60  SER A CA  1 
ATOM   1929 C C   . SER B 2 60  ? 41.78728 -61.14008 9.23367   1.000 191.66966 ? 60  SER A C   1 
ATOM   1930 O O   . SER B 2 60  ? 41.31848 -62.04458 9.93169   1.000 192.57515 ? 60  SER A O   1 
ATOM   1931 C CB  . SER B 2 60  ? 43.19287 -62.22867 7.48546   1.000 196.12113 ? 60  SER A CB  1 
ATOM   1932 O OG  . SER B 2 60  ? 44.37257 -61.54706 7.87735   1.000 192.50087 ? 60  SER A OG  1 
ATOM   1933 N N   . VAL B 2 61  ? 42.15332 -59.96430 9.74231   1.000 183.69881 ? 61  VAL A N   1 
ATOM   1934 C CA  . VAL B 2 61  ? 42.18774 -59.70713 11.17520  1.000 180.93801 ? 61  VAL A CA  1 
ATOM   1935 C C   . VAL B 2 61  ? 41.33159 -58.51875 11.58196  1.000 180.17102 ? 61  VAL A C   1 
ATOM   1936 O O   . VAL B 2 61  ? 41.31414 -58.16194 12.76361  1.000 177.44088 ? 61  VAL A O   1 
ATOM   1937 C CB  . VAL B 2 61  ? 43.63626 -59.50450 11.66520  1.000 178.10740 ? 61  VAL A CB  1 
ATOM   1938 C CG1 . VAL B 2 61  ? 44.51288 -60.66804 11.22958  1.000 179.03394 ? 61  VAL A CG1 1 
ATOM   1939 C CG2 . VAL B 2 61  ? 44.18865 -58.18624 11.14608  1.000 176.93152 ? 61  VAL A CG2 1 
ATOM   1940 N N   . LYS B 2 62  ? 40.62728 -57.88809 10.64355  1.000 181.15251 ? 62  LYS A N   1 
ATOM   1941 C CA  . LYS B 2 62  ? 39.85491 -56.69460 10.96372  1.000 176.96607 ? 62  LYS A CA  1 
ATOM   1942 C C   . LYS B 2 62  ? 38.69129 -57.04320 11.88407  1.000 176.74985 ? 62  LYS A C   1 
ATOM   1943 O O   . LYS B 2 62  ? 38.05644 -58.09297 11.74330  1.000 181.39683 ? 62  LYS A O   1 
ATOM   1944 C CB  . LYS B 2 62  ? 39.35361 -56.02899 9.68305   1.000 177.55971 ? 62  LYS A CB  1 
ATOM   1945 C CG  . LYS B 2 62  ? 40.41227 -55.20346 8.96701   1.000 176.15558 ? 62  LYS A CG  1 
ATOM   1946 C CD  . LYS B 2 62  ? 39.88420 -54.62582 7.67441   1.000 177.43585 ? 62  LYS A CD  1 
ATOM   1947 C CE  . LYS B 2 62  ? 39.36051 -53.20823 7.87835   1.000 172.52263 ? 62  LYS A CE  1 
ATOM   1948 N NZ  . LYS B 2 62  ? 38.13743 -53.16295 8.73077   1.000 169.97001 ? 62  LYS A NZ  1 
ATOM   1949 N N   . GLY B 2 63  ? 38.42766 -56.16068 12.84895  1.000 175.15615 ? 63  GLY A N   1 
ATOM   1950 C CA  . GLY B 2 63  ? 37.49791 -56.44743 13.91620  1.000 174.08974 ? 63  GLY A CA  1 
ATOM   1951 C C   . GLY B 2 63  ? 37.96169 -57.51074 14.88516  1.000 176.39355 ? 63  GLY A C   1 
ATOM   1952 O O   . GLY B 2 63  ? 37.38342 -57.63864 15.96920  1.000 175.13771 ? 63  GLY A O   1 
ATOM   1953 N N   . ARG B 2 64  ? 39.00130 -58.26409 14.53972  1.000 176.03984 ? 64  ARG A N   1 
ATOM   1954 C CA  . ARG B 2 64  ? 39.52509 -59.31650 15.41520  1.000 178.31141 ? 64  ARG A CA  1 
ATOM   1955 C C   . ARG B 2 64  ? 40.67848 -58.77112 16.24950  1.000 175.17812 ? 64  ARG A C   1 
ATOM   1956 O O   . ARG B 2 64  ? 40.58749 -58.69193 17.47716  1.000 173.86292 ? 64  ARG A O   1 
ATOM   1957 C CB  . ARG B 2 64  ? 39.97091 -60.52744 14.59328  1.000 182.65264 ? 64  ARG A CB  1 
ATOM   1958 C CG  . ARG B 2 64  ? 38.87129 -61.17089 13.77900  1.000 186.32000 ? 64  ARG A CG  1 
ATOM   1959 C CD  . ARG B 2 64  ? 39.24760 -62.58348 13.37801  1.000 188.76013 ? 64  ARG A CD  1 
ATOM   1960 N NE  . ARG B 2 64  ? 40.40999 -62.57235 12.50319  1.000 187.48569 ? 64  ARG A NE  1 
ATOM   1961 C CZ  . ARG B 2 64  ? 41.52203 -63.25370 12.72756  1.000 186.70221 ? 64  ARG A CZ  1 
ATOM   1962 N NH1 . ARG B 2 64  ? 41.66467 -64.00845 13.80507  1.000 187.26502 ? 64  ARG A NH1 1 
ATOM   1963 N NH2 . ARG B 2 64  ? 42.51146 -63.18424 11.84342  1.000 185.90936 ? 64  ARG A NH2 1 
ATOM   1964 N N   . PHE B 2 65  ? 41.77392 -58.41880 15.58470  1.000 174.92776 ? 65  PHE A N   1 
ATOM   1965 C CA  . PHE B 2 65  ? 42.97755 -57.94997 16.25127  1.000 172.97191 ? 65  PHE A CA  1 
ATOM   1966 C C   . PHE B 2 65  ? 42.92817 -56.43843 16.42821  1.000 168.85579 ? 65  PHE A C   1 
ATOM   1967 O O   . PHE B 2 65  ? 42.28031 -55.72200 15.66024  1.000 166.86730 ? 65  PHE A O   1 
ATOM   1968 C CB  . PHE B 2 65  ? 44.23471 -58.33205 15.46155  1.000 173.81807 ? 65  PHE A CB  1 
ATOM   1969 C CG  . PHE B 2 65  ? 44.40648 -59.81648 15.23717  1.000 175.95030 ? 65  PHE A CG  1 
ATOM   1970 C CD1 . PHE B 2 65  ? 43.52121 -60.73954 15.77262  1.000 178.28084 ? 65  PHE A CD1 1 
ATOM   1971 C CD2 . PHE B 2 65  ? 45.48662 -60.28613 14.50937  1.000 175.48663 ? 65  PHE A CD2 1 
ATOM   1972 C CE1 . PHE B 2 65  ? 43.69462 -62.09232 15.56346  1.000 180.31107 ? 65  PHE A CE1 1 
ATOM   1973 C CE2 . PHE B 2 65  ? 45.66650 -61.64024 14.29854  1.000 177.32864 ? 65  PHE A CE2 1 
ATOM   1974 C CZ  . PHE B 2 65  ? 44.76978 -62.54344 14.82724  1.000 179.80685 ? 65  PHE A CZ  1 
ATOM   1975 N N   . THR B 2 66  ? 43.63235 -55.95963 17.45180  1.000 169.75560 ? 66  THR A N   1 
ATOM   1976 C CA  . THR B 2 66  ? 43.73506 -54.53560 17.74007  1.000 166.22581 ? 66  THR A CA  1 
ATOM   1977 C C   . THR B 2 66  ? 45.18319 -54.18489 18.04532  1.000 167.75676 ? 66  THR A C   1 
ATOM   1978 O O   . THR B 2 66  ? 45.84229 -54.87601 18.82866  1.000 170.85578 ? 66  THR A O   1 
ATOM   1979 C CB  . THR B 2 66  ? 42.83370 -54.12740 18.91097  1.000 164.17353 ? 66  THR A CB  1 
ATOM   1980 O OG1 . THR B 2 66  ? 43.00215 -55.04786 19.99553  1.000 167.28855 ? 66  THR A OG1 1 
ATOM   1981 C CG2 . THR B 2 66  ? 41.37331 -54.10722 18.48116  1.000 161.64835 ? 66  THR A CG2 1 
ATOM   1982 N N   . ILE B 2 67  ? 45.67142 -53.11212 17.42776  1.000 155.65265 ? 67  ILE A N   1 
ATOM   1983 C CA  . ILE B 2 67  ? 47.03844 -52.64099 17.61037  1.000 157.43457 ? 67  ILE A CA  1 
ATOM   1984 C C   . ILE B 2 67  ? 47.00171 -51.37842 18.45926  1.000 157.19452 ? 67  ILE A C   1 
ATOM   1985 O O   . ILE B 2 67  ? 46.11040 -50.53609 18.29752  1.000 153.92324 ? 67  ILE A O   1 
ATOM   1986 C CB  . ILE B 2 67  ? 47.73311 -52.38699 16.25711  1.000 156.72879 ? 67  ILE A CB  1 
ATOM   1987 C CG1 . ILE B 2 67  ? 49.15960 -51.87406 16.46242  1.000 157.98407 ? 67  ILE A CG1 1 
ATOM   1988 C CG2 . ILE B 2 67  ? 46.92569 -51.41380 15.40816  1.000 153.43228 ? 67  ILE A CG2 1 
ATOM   1989 C CD1 . ILE B 2 67  ? 49.96579 -51.78939 15.18592  1.000 157.67620 ? 67  ILE A CD1 1 
ATOM   1990 N N   . SER B 2 68  ? 47.96224 -51.25238 19.37160  1.000 167.06946 ? 68  SER A N   1 
ATOM   1991 C CA  . SER B 2 68  ? 47.98492 -50.13026 20.30104  1.000 169.58939 ? 68  SER A CA  1 
ATOM   1992 C C   . SER B 2 68  ? 49.38967 -49.98584 20.87682  1.000 175.34132 ? 68  SER A C   1 
ATOM   1993 O O   . SER B 2 68  ? 50.28929 -50.78103 20.58984  1.000 175.78206 ? 68  SER A O   1 
ATOM   1994 C CB  . SER B 2 68  ? 46.94036 -50.31611 21.40599  1.000 169.91364 ? 68  SER A CB  1 
ATOM   1995 O OG  . SER B 2 68  ? 47.37391 -51.26200 22.36757  1.000 174.09541 ? 68  SER A OG  1 
ATOM   1996 N N   . ARG B 2 69  ? 49.56659 -48.94747 21.69386  1.000 182.35881 ? 69  ARG A N   1 
ATOM   1997 C CA  . ARG B 2 69  ? 50.82223 -48.67374 22.37844  1.000 187.14948 ? 69  ARG A CA  1 
ATOM   1998 C C   . ARG B 2 69  ? 50.51676 -47.91731 23.66344  1.000 190.97086 ? 69  ARG A C   1 
ATOM   1999 O O   . ARG B 2 69  ? 49.60320 -47.08821 23.69864  1.000 190.10972 ? 69  ARG A O   1 
ATOM   2000 C CB  . ARG B 2 69  ? 51.78297 -47.86422 21.49902  1.000 183.97055 ? 69  ARG A CB  1 
ATOM   2001 N N   . ASP B 2 70  ? 51.28463 -48.20611 24.71261  1.000 205.46580 ? 70  ASP A N   1 
ATOM   2002 C CA  . ASP B 2 70  ? 51.04039 -47.62169 26.02248  1.000 209.86344 ? 70  ASP A CA  1 
ATOM   2003 C C   . ASP B 2 70  ? 51.60520 -46.20441 26.09778  1.000 210.26279 ? 70  ASP A C   1 
ATOM   2004 O O   . ASP B 2 70  ? 52.25959 -45.70937 25.17504  1.000 206.77101 ? 70  ASP A O   1 
ATOM   2005 C CB  . ASP B 2 70  ? 51.63631 -48.50134 27.12109  1.000 213.96549 ? 70  ASP A CB  1 
ATOM   2006 C CG  . ASP B 2 70  ? 53.12789 -48.72343 26.94920  1.000 213.10027 ? 70  ASP A CG  1 
ATOM   2007 O OD1 . ASP B 2 70  ? 53.59784 -48.72612 25.79219  1.000 207.98781 ? 70  ASP A OD1 1 
ATOM   2008 O OD2 . ASP B 2 70  ? 53.83071 -48.89367 27.96943  1.000 217.22290 ? 70  ASP A OD2 1 
ATOM   2009 N N   . ASN B 2 71  ? 51.34455 -45.54362 27.22107  1.000 212.17781 ? 71  ASN A N   1 
ATOM   2010 C CA  . ASN B 2 71  ? 51.83897 -44.19931 27.46199  1.000 213.70769 ? 71  ASN A CA  1 
ATOM   2011 C C   . ASN B 2 71  ? 53.23980 -44.25228 28.06653  1.000 216.57104 ? 71  ASN A C   1 
ATOM   2012 O O   . ASN B 2 71  ? 53.74065 -45.31239 28.45016  1.000 217.86212 ? 71  ASN A O   1 
ATOM   2013 C CB  . ASN B 2 71  ? 50.88380 -43.43231 28.37607  1.000 217.08192 ? 71  ASN A CB  1 
ATOM   2014 C CG  . ASN B 2 71  ? 50.07957 -42.38549 27.62942  1.000 214.13677 ? 71  ASN A CG  1 
ATOM   2015 O OD1 . ASN B 2 71  ? 50.61070 -41.66244 26.78623  1.000 211.97790 ? 71  ASN A OD1 1 
ATOM   2016 N ND2 . ASN B 2 71  ? 48.78998 -42.30048 27.93544  1.000 213.76483 ? 71  ASN A ND2 1 
ATOM   2017 N N   . SER B 2 72  ? 53.86610 -43.07642 28.15789  1.000 215.34987 ? 72  SER A N   1 
ATOM   2018 C CA  . SER B 2 72  ? 55.26088 -42.94844 28.56833  1.000 217.98520 ? 72  SER A CA  1 
ATOM   2019 C C   . SER B 2 72  ? 56.14588 -43.79488 27.66333  1.000 213.31078 ? 72  SER A C   1 
ATOM   2020 O O   . SER B 2 72  ? 56.33663 -43.46103 26.48900  1.000 208.65580 ? 72  SER A O   1 
ATOM   2021 C CB  . SER B 2 72  ? 55.44502 -43.34592 30.03583  1.000 224.78338 ? 72  SER A CB  1 
ATOM   2022 O OG  . SER B 2 72  ? 56.80305 -43.23187 30.42483  1.000 227.80592 ? 72  SER A OG  1 
ATOM   2023 N N   . LYS B 2 73  ? 56.69131 -44.88562 28.19798  1.000 217.19754 ? 73  LYS A N   1 
ATOM   2024 C CA  . LYS B 2 73  ? 57.41594 -45.83299 27.36372  1.000 212.76807 ? 73  LYS A CA  1 
ATOM   2025 C C   . LYS B 2 73  ? 56.48831 -46.37760 26.28583  1.000 207.14533 ? 73  LYS A C   1 
ATOM   2026 O O   . LYS B 2 73  ? 55.31863 -46.67323 26.54245  1.000 208.15898 ? 73  LYS A O   1 
ATOM   2027 C CB  . LYS B 2 73  ? 57.97562 -46.97524 28.21317  1.000 216.44810 ? 73  LYS A CB  1 
ATOM   2028 N N   . ASN B 2 74  ? 57.00569 -46.48753 25.06741  1.000 211.12286 ? 74  ASN A N   1 
ATOM   2029 C CA  . ASN B 2 74  ? 56.21204 -46.92183 23.92637  1.000 206.07504 ? 74  ASN A CA  1 
ATOM   2030 C C   . ASN B 2 74  ? 56.44728 -48.40456 23.67246  1.000 204.14117 ? 74  ASN A C   1 
ATOM   2031 O O   . ASN B 2 74  ? 57.59515 -48.86059 23.62948  1.000 203.99293 ? 74  ASN A O   1 
ATOM   2032 C CB  . ASN B 2 74  ? 56.55080 -46.10237 22.68092  1.000 202.25222 ? 74  ASN A CB  1 
ATOM   2033 C CG  . ASN B 2 74  ? 58.02104 -46.14959 22.33667  1.000 201.85533 ? 74  ASN A CG  1 
ATOM   2034 O OD1 . ASN B 2 74  ? 58.86251 -45.63704 23.07518  1.000 205.68603 ? 74  ASN A OD1 1 
ATOM   2035 N ND2 . ASN B 2 74  ? 58.33980 -46.76407 21.20595  1.000 198.24231 ? 74  ASN A ND2 1 
ATOM   2036 N N   . THR B 2 75  ? 55.35633 -49.14900 23.50651  1.000 187.35883 ? 75  THR A N   1 
ATOM   2037 C CA  . THR B 2 75  ? 55.42086 -50.59951 23.34899  1.000 186.39149 ? 75  THR A CA  1 
ATOM   2038 C C   . THR B 2 75  ? 54.29281 -51.02195 22.41953  1.000 183.32725 ? 75  THR A C   1 
ATOM   2039 O O   . THR B 2 75  ? 53.11775 -50.90299 22.77795  1.000 186.35912 ? 75  THR A O   1 
ATOM   2040 C CB  . THR B 2 75  ? 55.31314 -51.30216 24.70104  1.000 192.37561 ? 75  THR A CB  1 
ATOM   2041 O OG1 . THR B 2 75  ? 56.36532 -50.84951 25.56299  1.000 195.87999 ? 75  THR A OG1 1 
ATOM   2042 C CG2 . THR B 2 75  ? 55.39922 -52.81153 24.53696  1.000 191.87647 ? 75  THR A CG2 1 
ATOM   2043 N N   . LEU B 2 76  ? 54.64976 -51.51075 21.23438  1.000 172.74402 ? 76  LEU A N   1 
ATOM   2044 C CA  . LEU B 2 76  ? 53.65050 -51.93221 20.26254  1.000 169.98518 ? 76  LEU A CA  1 
ATOM   2045 C C   . LEU B 2 76  ? 52.87891 -53.13680 20.78576  1.000 172.04214 ? 76  LEU A C   1 
ATOM   2046 O O   . LEU B 2 76  ? 53.47283 -54.11048 21.25842  1.000 173.38973 ? 76  LEU A O   1 
ATOM   2047 C CB  . LEU B 2 76  ? 54.31809 -52.27553 18.93305  1.000 166.35531 ? 76  LEU A CB  1 
ATOM   2048 C CG  . LEU B 2 76  ? 53.47719 -52.09277 17.66843  1.000 164.20828 ? 76  LEU A CG  1 
ATOM   2049 C CD1 . LEU B 2 76  ? 52.50044 -50.93149 17.81437  1.000 164.90128 ? 76  LEU A CD1 1 
ATOM   2050 C CD2 . LEU B 2 76  ? 54.36526 -51.92787 16.44349  1.000 163.39231 ? 76  LEU A CD2 1 
ATOM   2051 N N   . TYR B 2 77  ? 51.55343 -53.06913 20.70044  1.000 168.72173 ? 77  TYR A N   1 
ATOM   2052 C CA  . TYR B 2 77  ? 50.67536 -54.15017 21.12323  1.000 170.97432 ? 77  TYR A CA  1 
ATOM   2053 C C   . TYR B 2 77  ? 49.92644 -54.70591 19.92041  1.000 166.49851 ? 77  TYR A C   1 
ATOM   2054 O O   . TYR B 2 77  ? 49.50638 -53.95148 19.03854  1.000 163.74395 ? 77  TYR A O   1 
ATOM   2055 C CB  . TYR B 2 77  ? 49.66522 -53.67477 22.17663  1.000 175.08962 ? 77  TYR A CB  1 
ATOM   2056 C CG  . TYR B 2 77  ? 50.26957 -53.24683 23.49635  1.000 180.71463 ? 77  TYR A CG  1 
ATOM   2057 C CD1 . TYR B 2 77  ? 51.23789 -54.01858 24.12317  1.000 183.70895 ? 77  TYR A CD1 1 
ATOM   2058 C CD2 . TYR B 2 77  ? 49.85548 -52.07892 24.12503  1.000 181.93730 ? 77  TYR A CD2 1 
ATOM   2059 C CE1 . TYR B 2 77  ? 51.78563 -53.63342 25.33326  1.000 188.34719 ? 77  TYR A CE1 1 
ATOM   2060 C CE2 . TYR B 2 77  ? 50.39711 -51.68618 25.33483  1.000 186.90671 ? 77  TYR A CE2 1 
ATOM   2061 C CZ  . TYR B 2 77  ? 51.36165 -52.46740 25.93407  1.000 189.92652 ? 77  TYR A CZ  1 
ATOM   2062 O OH  . TYR B 2 77  ? 51.90526 -52.08248 27.13808  1.000 194.26769 ? 77  TYR A OH  1 
ATOM   2063 N N   . LEU B 2 78  ? 49.76594 -56.03271 19.88367  1.000 169.02325 ? 78  LEU A N   1 
ATOM   2064 C CA  . LEU B 2 78  ? 48.91171 -56.70609 18.90057  1.000 166.85786 ? 78  LEU A CA  1 
ATOM   2065 C C   . LEU B 2 78  ? 47.94035 -57.58886 19.67282  1.000 169.64624 ? 78  LEU A C   1 
ATOM   2066 O O   . LEU B 2 78  ? 48.12496 -58.80418 19.77762  1.000 171.17076 ? 78  LEU A O   1 
ATOM   2067 C CB  . LEU B 2 78  ? 49.71581 -57.51379 17.89540  1.000 165.00913 ? 78  LEU A CB  1 
ATOM   2068 C CG  . LEU B 2 78  ? 48.86512 -57.96311 16.70314  1.000 164.29314 ? 78  LEU A CG  1 
ATOM   2069 C CD1 . LEU B 2 78  ? 48.08794 -56.79306 16.10913  1.000 163.44235 ? 78  LEU A CD1 1 
ATOM   2070 C CD2 . LEU B 2 78  ? 49.70448 -58.65244 15.64957  1.000 163.86625 ? 78  LEU A CD2 1 
ATOM   2071 N N   . GLN B 2 79  ? 46.89935 -56.96938 20.21515  1.000 179.92763 ? 79  GLN A N   1 
ATOM   2072 C CA  . GLN B 2 79  ? 45.89579 -57.71465 20.95829  1.000 181.08561 ? 79  GLN A CA  1 
ATOM   2073 C C   . GLN B 2 79  ? 45.09141 -58.55756 19.97388  1.000 180.54772 ? 79  GLN A C   1 
ATOM   2074 O O   . GLN B 2 79  ? 44.68675 -58.07252 18.91344  1.000 178.32075 ? 79  GLN A O   1 
ATOM   2075 C CB  . GLN B 2 79  ? 45.01866 -56.73277 21.74945  1.000 178.70615 ? 79  GLN A CB  1 
ATOM   2076 C CG  . GLN B 2 79  ? 43.90931 -57.28980 22.65904  1.000 178.79302 ? 79  GLN A CG  1 
ATOM   2077 C CD  . GLN B 2 79  ? 42.91416 -58.20796 21.98089  1.000 178.72874 ? 79  GLN A CD  1 
ATOM   2078 O OE1 . GLN B 2 79  ? 42.47923 -57.96580 20.84887  1.000 177.05920 ? 79  GLN A OE1 1 
ATOM   2079 N NE2 . GLN B 2 79  ? 42.57317 -59.28989 22.65701  1.000 181.48136 ? 79  GLN A NE2 1 
ATOM   2080 N N   . MET B 2 80  ? 44.86951 -59.82626 20.31807  1.000 180.93860 ? 80  MET A N   1 
ATOM   2081 C CA  . MET B 2 80  ? 44.21948 -60.77081 19.41713  1.000 181.68550 ? 80  MET A CA  1 
ATOM   2082 C C   . MET B 2 80  ? 43.21537 -61.61751 20.18350  1.000 184.24401 ? 80  MET A C   1 
ATOM   2083 O O   . MET B 2 80  ? 43.54660 -62.16918 21.23648  1.000 186.57402 ? 80  MET A O   1 
ATOM   2084 C CB  . MET B 2 80  ? 45.25406 -61.67977 18.74131  1.000 182.22574 ? 80  MET A CB  1 
ATOM   2085 C CG  . MET B 2 80  ? 46.29027 -60.93301 17.92107  1.000 179.19372 ? 80  MET A CG  1 
ATOM   2086 S SD  . MET B 2 80  ? 47.50694 -62.01478 17.15113  1.000 179.23261 ? 80  MET A SD  1 
ATOM   2087 C CE  . MET B 2 80  ? 48.43706 -62.55976 18.57552  1.000 182.19024 ? 80  MET A CE  1 
ATOM   2088 N N   . ASN B 2 81  ? 41.99859 -61.71968 19.65284  1.000 191.79354 ? 81  ASN A N   1 
ATOM   2089 C CA  . ASN B 2 81  ? 40.98465 -62.64559 20.14015  1.000 194.65897 ? 81  ASN A CA  1 
ATOM   2090 C C   . ASN B 2 81  ? 40.58076 -63.61417 19.03808  1.000 197.20967 ? 81  ASN A C   1 
ATOM   2091 O O   . ASN B 2 81  ? 40.90645 -63.42775 17.86206  1.000 196.13846 ? 81  ASN A O   1 
ATOM   2092 C CB  . ASN B 2 81  ? 39.72987 -61.91956 20.64507  1.000 192.57787 ? 81  ASN A CB  1 
ATOM   2093 C CG  . ASN B 2 81  ? 40.03718 -60.61169 21.32357  1.000 188.14591 ? 81  ASN A CG  1 
ATOM   2094 O OD1 . ASN B 2 81  ? 40.11045 -59.56651 20.68077  1.000 184.64107 ? 81  ASN A OD1 1 
ATOM   2095 N ND2 . ASN B 2 81  ? 40.15976 -60.65198 22.64639  1.000 188.43132 ? 81  ASN A ND2 1 
ATOM   2096 N N   . SER B 2 82  ? 39.84064 -64.64990 19.44727  1.000 198.60837 ? 82  SER A N   1 
ATOM   2097 C CA  . SER B 2 82  ? 39.26643 -65.63843 18.53147  1.000 201.70853 ? 82  SER A CA  1 
ATOM   2098 C C   . SER B 2 82  ? 40.30257 -66.12542 17.52427  1.000 201.30273 ? 82  SER A C   1 
ATOM   2099 O O   . SER B 2 82  ? 40.01249 -66.30761 16.33996  1.000 201.93538 ? 82  SER A O   1 
ATOM   2100 C CB  . SER B 2 82  ? 38.04007 -65.07160 17.81674  1.000 201.92375 ? 82  SER A CB  1 
ATOM   2101 O OG  . SER B 2 82  ? 38.42805 -64.16508 16.79959  1.000 199.18869 ? 82  SER A OG  1 
ATOM   2102 N N   . LEU B 2 83  ? 41.52751 -66.32383 18.00477  1.000 198.43145 ? 83  LEU A N   1 
ATOM   2103 C CA  . LEU B 2 83  ? 42.65132 -66.62384 17.12851  1.000 197.39260 ? 83  LEU A CA  1 
ATOM   2104 C C   . LEU B 2 83  ? 42.39087 -67.89898 16.33907  1.000 201.03141 ? 83  LEU A C   1 
ATOM   2105 O O   . LEU B 2 83  ? 42.19512 -68.97161 16.91882  1.000 204.65871 ? 83  LEU A O   1 
ATOM   2106 C CB  . LEU B 2 83  ? 43.92869 -66.75308 17.95456  1.000 196.93834 ? 83  LEU A CB  1 
ATOM   2107 C CG  . LEU B 2 83  ? 44.52226 -65.42350 18.42267  1.000 193.52822 ? 83  LEU A CG  1 
ATOM   2108 C CD1 . LEU B 2 83  ? 44.15806 -65.16293 19.87565  1.000 194.97464 ? 83  LEU A CD1 1 
ATOM   2109 C CD2 . LEU B 2 83  ? 46.02864 -65.40470 18.22937  1.000 192.27387 ? 83  LEU A CD2 1 
ATOM   2110 N N   . LYS B 2 84  ? 42.37059 -67.77198 15.01522  1.000 202.24634 ? 84  LYS A N   1 
ATOM   2111 C CA  . LYS B 2 84  ? 42.16137 -68.91347 14.13906  1.000 206.31601 ? 84  LYS A CA  1 
ATOM   2112 C C   . LYS B 2 84  ? 43.45517 -69.70082 13.97397  1.000 207.00674 ? 84  LYS A C   1 
ATOM   2113 O O   . LYS B 2 84  ? 44.55681 -69.16138 14.10958  1.000 203.80894 ? 84  LYS A O   1 
ATOM   2114 C CB  . LYS B 2 84  ? 41.64968 -68.45570 12.77267  1.000 206.73315 ? 84  LYS A CB  1 
ATOM   2115 N N   . ALA B 2 85  ? 43.30891 -70.99350 13.66879  1.000 203.78932 ? 85  ALA A N   1 
ATOM   2116 C CA  . ALA B 2 85  ? 44.47297 -71.86861 13.56565  1.000 205.46703 ? 85  ALA A CA  1 
ATOM   2117 C C   . ALA B 2 85  ? 45.43578 -71.41251 12.47601  1.000 203.47222 ? 85  ALA A C   1 
ATOM   2118 O O   . ALA B 2 85  ? 46.64801 -71.62778 12.59251  1.000 203.12217 ? 85  ALA A O   1 
ATOM   2119 C CB  . ALA B 2 85  ? 44.02723 -73.30878 13.31077  1.000 212.64545 ? 85  ALA A CB  1 
ATOM   2120 N N   . GLU B 2 86  ? 44.92474 -70.78101 11.41830  1.000 203.19956 ? 86  GLU A N   1 
ATOM   2121 C CA  . GLU B 2 86  ? 45.76663 -70.30025 10.32907  1.000 202.00194 ? 86  GLU A CA  1 
ATOM   2122 C C   . GLU B 2 86  ? 46.51247 -69.01452 10.66886  1.000 196.57544 ? 86  GLU A C   1 
ATOM   2123 O O   . GLU B 2 86  ? 47.22035 -68.48500 9.80589   1.000 195.61154 ? 86  GLU A O   1 
ATOM   2124 C CB  . GLU B 2 86  ? 44.92980 -70.10257 9.05852   1.000 204.49623 ? 86  GLU A CB  1 
ATOM   2125 C CG  . GLU B 2 86  ? 43.76108 -69.14207 9.20279   1.000 202.87355 ? 86  GLU A CG  1 
ATOM   2126 C CD  . GLU B 2 86  ? 42.49119 -69.83272 9.66942   1.000 206.38231 ? 86  GLU A CD  1 
ATOM   2127 O OE1 . GLU B 2 86  ? 42.58241 -70.75918 10.50213  1.000 207.99266 ? 86  GLU A OE1 1 
ATOM   2128 O OE2 . GLU B 2 86  ? 41.39929 -69.45503 9.19555   1.000 208.10233 ? 86  GLU A OE2 1 
ATOM   2129 N N   . ASP B 2 87  ? 46.38147 -68.50515 11.89463  1.000 190.26680 ? 87  ASP A N   1 
ATOM   2130 C CA  . ASP B 2 87  ? 47.18707 -67.37657 12.34612  1.000 184.47781 ? 87  ASP A CA  1 
ATOM   2131 C C   . ASP B 2 87  ? 48.54384 -67.79628 12.89653  1.000 185.03465 ? 87  ASP A C   1 
ATOM   2132 O O   . ASP B 2 87  ? 49.37510 -66.92373 13.17182  1.000 181.13568 ? 87  ASP A O   1 
ATOM   2133 C CB  . ASP B 2 87  ? 46.43403 -66.57882 13.41541  1.000 181.35705 ? 87  ASP A CB  1 
ATOM   2134 C CG  . ASP B 2 87  ? 45.19103 -65.89868 12.87598  1.000 180.25866 ? 87  ASP A CG  1 
ATOM   2135 O OD1 . ASP B 2 87  ? 45.30792 -65.12532 11.90141  1.000 178.07596 ? 87  ASP A OD1 1 
ATOM   2136 O OD2 . ASP B 2 87  ? 44.09911 -66.12295 13.43772  1.000 182.13197 ? 87  ASP A OD2 1 
ATOM   2137 N N   . THR B 2 88  ? 48.77510 -69.10064 13.06200  1.000 190.47585 ? 88  THR A N   1 
ATOM   2138 C CA  . THR B 2 88  ? 50.00615 -69.64514 13.62471  1.000 192.04940 ? 88  THR A CA  1 
ATOM   2139 C C   . THR B 2 88  ? 51.22499 -69.12074 12.88202  1.000 190.79209 ? 88  THR A C   1 
ATOM   2140 O O   . THR B 2 88  ? 51.44054 -69.47490 11.71650  1.000 192.76224 ? 88  THR A O   1 
ATOM   2141 C CB  . THR B 2 88  ? 49.98153 -71.17532 13.58740  1.000 197.33177 ? 88  THR A CB  1 
ATOM   2142 O OG1 . THR B 2 88  ? 48.89924 -71.65263 14.39392  1.000 199.00633 ? 88  THR A OG1 1 
ATOM   2143 C CG2 . THR B 2 88  ? 51.29020 -71.75826 14.11734  1.000 199.80056 ? 88  THR A CG2 1 
ATOM   2144 N N   . ALA B 2 89  ? 52.02984 -68.29431 13.55131  1.000 185.99922 ? 89  ALA A N   1 
ATOM   2145 C CA  . ALA B 2 89  ? 53.15416 -67.63357 12.90633  1.000 185.19927 ? 89  ALA A CA  1 
ATOM   2146 C C   . ALA B 2 89  ? 53.95067 -66.87304 13.95993  1.000 183.83308 ? 89  ALA A C   1 
ATOM   2147 O O   . ALA B 2 89  ? 53.44271 -66.54944 15.03881  1.000 182.61277 ? 89  ALA A O   1 
ATOM   2148 C CB  . ALA B 2 89  ? 52.66294 -66.68903 11.81391  1.000 182.60908 ? 89  ALA A CB  1 
ATOM   2149 N N   . VAL B 2 90  ? 55.20781 -66.58089 13.62844  1.000 181.53026 ? 90  VAL A N   1 
ATOM   2150 C CA  . VAL B 2 90  ? 56.02382 -65.62718 14.37624  1.000 180.53578 ? 90  VAL A CA  1 
ATOM   2151 C C   . VAL B 2 90  ? 55.65430 -64.22313 13.90842  1.000 175.85473 ? 90  VAL A C   1 
ATOM   2152 O O   . VAL B 2 90  ? 56.03222 -63.78990 12.81754  1.000 176.15155 ? 90  VAL A O   1 
ATOM   2153 C CB  . VAL B 2 90  ? 57.51887 -65.90624 14.22183  1.000 185.17185 ? 90  VAL A CB  1 
ATOM   2154 C CG1 . VAL B 2 90  ? 58.30985 -65.07076 15.19217  1.000 185.61565 ? 90  VAL A CG1 1 
ATOM   2155 C CG2 . VAL B 2 90  ? 57.78387 -67.33827 14.56290  1.000 190.16054 ? 90  VAL A CG2 1 
ATOM   2156 N N   . TYR B 2 91  ? 54.89969 -63.51351 14.73971  1.000 173.74698 ? 91  TYR A N   1 
ATOM   2157 C CA  . TYR B 2 91  ? 54.56706 -62.12325 14.48121  1.000 169.89344 ? 91  TYR A CA  1 
ATOM   2158 C C   . TYR B 2 91  ? 55.75359 -61.24428 14.85299  1.000 169.97007 ? 91  TYR A C   1 
ATOM   2159 O O   . TYR B 2 91  ? 56.38113 -61.43889 15.89752  1.000 171.79057 ? 91  TYR A O   1 
ATOM   2160 C CB  . TYR B 2 91  ? 53.33943 -61.71447 15.29618  1.000 167.47543 ? 91  TYR A CB  1 
ATOM   2161 C CG  . TYR B 2 91  ? 52.04368 -62.38182 14.88316  1.000 167.88769 ? 91  TYR A CG  1 
ATOM   2162 C CD1 . TYR B 2 91  ? 51.90506 -63.76467 14.91026  1.000 171.01640 ? 91  TYR A CD1 1 
ATOM   2163 C CD2 . TYR B 2 91  ? 50.95051 -61.62554 14.49183  1.000 166.04088 ? 91  TYR A CD2 1 
ATOM   2164 C CE1 . TYR B 2 91  ? 50.72135 -64.37085 14.54192  1.000 171.99615 ? 91  TYR A CE1 1 
ATOM   2165 C CE2 . TYR B 2 91  ? 49.76174 -62.22171 14.12670  1.000 167.30003 ? 91  TYR A CE2 1 
ATOM   2166 C CZ  . TYR B 2 91  ? 49.65292 -63.59355 14.15248  1.000 170.16106 ? 91  TYR A CZ  1 
ATOM   2167 O OH  . TYR B 2 91  ? 48.46953 -64.18879 13.78660  1.000 171.98276 ? 91  TYR A OH  1 
ATOM   2168 N N   . TYR B 2 92  ? 56.06900 -60.28192 13.99171  1.000 165.81282 ? 92  TYR A N   1 
ATOM   2169 C CA  . TYR B 2 92  ? 57.13363 -59.32592 14.25731  1.000 166.44586 ? 92  TYR A CA  1 
ATOM   2170 C C   . TYR B 2 92  ? 56.54439 -57.93186 14.39917  1.000 163.00756 ? 92  TYR A C   1 
ATOM   2171 O O   . TYR B 2 92  ? 55.69435 -57.52425 13.60214  1.000 162.06816 ? 92  TYR A O   1 
ATOM   2172 C CB  . TYR B 2 92  ? 58.18841 -59.31173 13.14626  1.000 170.88863 ? 92  TYR A CB  1 
ATOM   2173 C CG  . TYR B 2 92  ? 58.50923 -60.66245 12.56161  1.000 174.80261 ? 92  TYR A CG  1 
ATOM   2174 C CD1 . TYR B 2 92  ? 59.24229 -61.59777 13.27788  1.000 178.27151 ? 92  TYR A CD1 1 
ATOM   2175 C CD2 . TYR B 2 92  ? 58.10834 -60.98896 11.27738  1.000 176.04076 ? 92  TYR A CD2 1 
ATOM   2176 C CE1 . TYR B 2 92  ? 59.54388 -62.83109 12.73837  1.000 182.54835 ? 92  TYR A CE1 1 
ATOM   2177 C CE2 . TYR B 2 92  ? 58.40910 -62.21016 10.73065  1.000 179.75220 ? 92  TYR A CE2 1 
ATOM   2178 C CZ  . TYR B 2 92  ? 59.12250 -63.13145 11.46174  1.000 182.82881 ? 92  TYR A CZ  1 
ATOM   2179 O OH  . TYR B 2 92  ? 59.41256 -64.35393 10.90402  1.000 186.86524 ? 92  TYR A OH  1 
ATOM   2180 N N   . CYS B 2 93  ? 56.99928 -57.20535 15.41605  1.000 167.25620 ? 93  CYS A N   1 
ATOM   2181 C CA  . CYS B 2 93  ? 56.64659 -55.80304 15.58051  1.000 165.09026 ? 93  CYS A CA  1 
ATOM   2182 C C   . CYS B 2 93  ? 57.73028 -54.95547 14.92515  1.000 167.30729 ? 93  CYS A C   1 
ATOM   2183 O O   . CYS B 2 93  ? 58.91932 -55.12966 15.20969  1.000 170.13604 ? 93  CYS A O   1 
ATOM   2184 C CB  . CYS B 2 93  ? 56.48346 -55.45309 17.06389  1.000 164.34048 ? 93  CYS A CB  1 
ATOM   2185 S SG  . CYS B 2 93  ? 57.48926 -54.07794 17.69618  1.000 165.27267 ? 93  CYS A SG  1 
ATOM   2186 N N   . ALA B 2 94  ? 57.32097 -54.06819 14.02068  1.000 167.55976 ? 94  ALA A N   1 
ATOM   2187 C CA  . ALA B 2 94  ? 58.24744 -53.25179 13.25075  1.000 171.29006 ? 94  ALA A CA  1 
ATOM   2188 C C   . ALA B 2 94  ? 57.83143 -51.79075 13.32453  1.000 169.46573 ? 94  ALA A C   1 
ATOM   2189 O O   . ALA B 2 94  ? 56.64292 -51.46900 13.39938  1.000 166.48865 ? 94  ALA A O   1 
ATOM   2190 C CB  . ALA B 2 94  ? 58.31141 -53.70115 11.78540  1.000 176.36091 ? 94  ALA A CB  1 
ATOM   2191 N N   . VAL B 2 95  ? 58.82397 -50.90520 13.29086  1.000 165.82315 ? 95  VAL A N   1 
ATOM   2192 C CA  . VAL B 2 95  ? 58.59219 -49.47806 13.45042  1.000 165.45307 ? 95  VAL A CA  1 
ATOM   2193 C C   . VAL B 2 95  ? 59.12601 -48.74294 12.22925  1.000 168.14660 ? 95  VAL A C   1 
ATOM   2194 O O   . VAL B 2 95  ? 59.94927 -49.25879 11.46982  1.000 171.07339 ? 95  VAL A O   1 
ATOM   2195 C CB  . VAL B 2 95  ? 59.24203 -48.93220 14.73424  1.000 166.31336 ? 95  VAL A CB  1 
ATOM   2196 C CG1 . VAL B 2 95  ? 58.60499 -49.56862 15.95779  1.000 164.37362 ? 95  VAL A CG1 1 
ATOM   2197 C CG2 . VAL B 2 95  ? 60.73761 -49.18983 14.70706  1.000 170.01334 ? 95  VAL A CG2 1 
ATOM   2198 N N   . GLY B 2 96  ? 58.64692 -47.51438 12.05244  1.000 176.87338 ? 96  GLY A N   1 
ATOM   2199 C CA  . GLY B 2 96  ? 59.07451 -46.69925 10.93240  1.000 178.00019 ? 96  GLY A CA  1 
ATOM   2200 C C   . GLY B 2 96  ? 58.76934 -45.23689 11.15121  1.000 176.26900 ? 96  GLY A C   1 
ATOM   2201 O O   . GLY B 2 96  ? 58.00181 -44.86501 12.04423  1.000 174.49235 ? 96  GLY A O   1 
ATOM   2202 N N   . VAL B 2 97  ? 59.39320 -44.40309 10.32007  1.000 164.84986 ? 97  VAL A N   1 
ATOM   2203 C CA  . VAL B 2 97  ? 59.15954 -42.96510 10.31715  1.000 165.92129 ? 97  VAL A CA  1 
ATOM   2204 C C   . VAL B 2 97  ? 58.61552 -42.46913 8.98569   1.000 166.18096 ? 97  VAL A C   1 
ATOM   2205 O O   . VAL B 2 97  ? 58.34017 -41.27176 8.84736   1.000 168.28835 ? 97  VAL A O   1 
ATOM   2206 C CB  . VAL B 2 97  ? 60.43630 -42.18753 10.70309  1.000 172.01248 ? 97  VAL A CB  1 
ATOM   2207 C CG1 . VAL B 2 97  ? 61.31768 -41.94922 9.48369   1.000 176.47508 ? 97  VAL A CG1 1 
ATOM   2208 C CG2 . VAL B 2 97  ? 60.08456 -40.87495 11.40315  1.000 174.26049 ? 97  VAL A CG2 1 
ATOM   2209 N N   . ASP B 2 98  ? 58.41124 -43.35914 8.01607   1.000 187.06729 ? 98  ASP A N   1 
ATOM   2210 C CA  . ASP B 2 98  ? 57.89137 -42.98151 6.71009   1.000 184.50563 ? 98  ASP A CA  1 
ATOM   2211 C C   . ASP B 2 98  ? 57.29837 -44.21204 6.03946   1.000 183.74435 ? 98  ASP A C   1 
ATOM   2212 O O   . ASP B 2 98  ? 57.84410 -45.31195 6.16147   1.000 187.17163 ? 98  ASP A O   1 
ATOM   2213 C CB  . ASP B 2 98  ? 58.98984 -42.37743 5.82833   1.000 186.83894 ? 98  ASP A CB  1 
ATOM   2214 C CG  . ASP B 2 98  ? 60.16481 -43.31946 5.63519   1.000 190.76409 ? 98  ASP A CG  1 
ATOM   2215 O OD1 . ASP B 2 98  ? 60.61667 -43.92216 6.63229   1.000 193.18851 ? 98  ASP A OD1 1 
ATOM   2216 O OD2 . ASP B 2 98  ? 60.63766 -43.45720 4.48736   1.000 191.58979 ? 98  ASP A OD2 1 
ATOM   2217 N N   . GLY B 2 99  ? 56.18734 -44.01345 5.33028   1.000 180.00520 ? 99  GLY A N   1 
ATOM   2218 C CA  . GLY B 2 99  ? 55.54775 -45.07564 4.57550   1.000 180.25839 ? 99  GLY A CA  1 
ATOM   2219 C C   . GLY B 2 99  ? 55.28172 -46.32975 5.38194   1.000 182.72247 ? 99  GLY A C   1 
ATOM   2220 O O   . GLY B 2 99  ? 54.50243 -46.30998 6.33921   1.000 180.60412 ? 99  GLY A O   1 
ATOM   2221 N N   . ASN B 2 100 ? 55.92970 -47.42786 5.00257   1.000 191.94901 ? 100 ASN A N   1 
ATOM   2222 C CA  . ASN B 2 100 ? 55.84178 -48.66565 5.76257   1.000 194.49085 ? 100 ASN A CA  1 
ATOM   2223 C C   . ASN B 2 100 ? 56.74406 -48.59428 6.98409   1.000 195.69715 ? 100 ASN A C   1 
ATOM   2224 O O   . ASN B 2 100 ? 57.88049 -48.11985 6.90414   1.000 197.31513 ? 100 ASN A O   1 
ATOM   2225 C CB  . ASN B 2 100 ? 56.24536 -49.85667 4.89543   1.000 199.03916 ? 100 ASN A CB  1 
ATOM   2226 C CG  . ASN B 2 100 ? 55.20388 -50.19580 3.85619   1.000 198.80126 ? 100 ASN A CG  1 
ATOM   2227 O OD1 . ASN B 2 100 ? 54.26391 -49.43261 3.63049   1.000 194.87867 ? 100 ASN A OD1 1 
ATOM   2228 N ND2 . ASN B 2 100 ? 55.36331 -51.34675 3.21390   1.000 203.38400 ? 100 ASN A ND2 1 
ATOM   2229 N N   . CYS B 2 101 ? 56.23992 -49.07752 8.11912   1.000 183.99103 ? 101 CYS A N   1 
ATOM   2230 C CA  . CYS B 2 101 ? 57.05462 -49.09594 9.32729   1.000 185.24166 ? 101 CYS A CA  1 
ATOM   2231 C C   . CYS B 2 101 ? 58.19648 -50.09090 9.17818   1.000 190.33403 ? 101 CYS A C   1 
ATOM   2232 O O   . CYS B 2 101 ? 58.22187 -51.12705 9.84948   1.000 192.18341 ? 101 CYS A O   1 
ATOM   2233 C CB  . CYS B 2 101 ? 56.21285 -49.42707 10.56117  1.000 182.90658 ? 101 CYS A CB  1 
ATOM   2234 S SG  . CYS B 2 101 ? 54.46126 -49.00702 10.44806  1.000 178.52049 ? 101 CYS A SG  1 
ATOM   2235 N N   . ARG B 2 102 ? 59.14889 -49.77509 8.30172   1.000 181.27363 ? 102 ARG A N   1 
ATOM   2236 C CA  . ARG B 2 102 ? 60.27315 -50.64903 7.99948   1.000 186.13921 ? 102 ARG A CA  1 
ATOM   2237 C C   . ARG B 2 102 ? 61.60419 -50.02620 8.40991   1.000 188.08841 ? 102 ARG A C   1 
ATOM   2238 O O   . ARG B 2 102 ? 62.62521 -50.24125 7.75369   1.000 191.61753 ? 102 ARG A O   1 
ATOM   2239 C CB  . ARG B 2 102 ? 60.28479 -51.00396 6.51344   1.000 187.21022 ? 102 ARG A CB  1 
ATOM   2240 N N   . ASN B 2 103 ? 61.60690 -49.24194 9.48884   1.000 189.71481 ? 103 ASN A N   1 
ATOM   2241 C CA  . ASN B 2 103 ? 62.86435 -48.70852 10.00041  1.000 192.18943 ? 103 ASN A CA  1 
ATOM   2242 C C   . ASN B 2 103 ? 63.62175 -49.75488 10.80798  1.000 195.30339 ? 103 ASN A C   1 
ATOM   2243 O O   . ASN B 2 103 ? 64.84080 -49.89360 10.65962  1.000 199.48207 ? 103 ASN A O   1 
ATOM   2244 C CB  . ASN B 2 103 ? 62.60482 -47.46048 10.84413  1.000 189.32095 ? 103 ASN A CB  1 
ATOM   2245 C CG  . ASN B 2 103 ? 62.22094 -46.26028 10.00249  1.000 187.49906 ? 103 ASN A CG  1 
ATOM   2246 O OD1 . ASN B 2 103 ? 61.74255 -46.40517 8.87756   1.000 186.30327 ? 103 ASN A OD1 1 
ATOM   2247 N ND2 . ASN B 2 103 ? 62.40994 -45.06614 10.55227  1.000 187.34607 ? 103 ASN A ND2 1 
ATOM   2248 N N   . TYR B 2 104 ? 62.91941 -50.49773 11.66024  1.000 192.68163 ? 104 TYR A N   1 
ATOM   2249 C CA  . TYR B 2 104 ? 63.51510 -51.58008 12.42707  1.000 194.70810 ? 104 TYR A CA  1 
ATOM   2250 C C   . TYR B 2 104 ? 62.53490 -52.74107 12.48267  1.000 192.89530 ? 104 TYR A C   1 
ATOM   2251 O O   . TYR B 2 104 ? 61.38552 -52.63471 12.04828  1.000 190.12256 ? 104 TYR A O   1 
ATOM   2252 C CB  . TYR B 2 104 ? 63.89601 -51.13333 13.84414  1.000 192.45355 ? 104 TYR A CB  1 
ATOM   2253 C CG  . TYR B 2 104 ? 64.92083 -50.02387 13.88431  1.000 195.02319 ? 104 TYR A CG  1 
ATOM   2254 C CD1 . TYR B 2 104 ? 66.28003 -50.30707 13.85677  1.000 200.39189 ? 104 TYR A CD1 1 
ATOM   2255 C CD2 . TYR B 2 104 ? 64.52943 -48.69339 13.95222  1.000 192.62139 ? 104 TYR A CD2 1 
ATOM   2256 C CE1 . TYR B 2 104 ? 67.21994 -49.29692 13.89634  1.000 203.08283 ? 104 TYR A CE1 1 
ATOM   2257 C CE2 . TYR B 2 104 ? 65.46243 -47.67686 13.99090  1.000 195.57301 ? 104 TYR A CE2 1 
ATOM   2258 C CZ  . TYR B 2 104 ? 66.80643 -47.98416 13.96327  1.000 200.72498 ? 104 TYR A CZ  1 
ATOM   2259 O OH  . TYR B 2 104 ? 67.73862 -46.97249 14.00209  1.000 204.12256 ? 104 TYR A OH  1 
ATOM   2260 N N   . TRP B 2 105 ? 63.00677 -53.86738 13.01320  1.000 190.10078 ? 105 TRP A N   1 
ATOM   2261 C CA  . TRP B 2 105 ? 62.17287 -55.05746 13.11966  1.000 187.92489 ? 105 TRP A CA  1 
ATOM   2262 C C   . TRP B 2 105 ? 62.43649 -55.78817 14.42953  1.000 186.46542 ? 105 TRP A C   1 
ATOM   2263 O O   . TRP B 2 105 ? 61.50084 -56.09841 15.17296  1.000 181.50624 ? 105 TRP A O   1 
ATOM   2264 C CB  . TRP B 2 105 ? 62.40826 -55.98305 11.92349  1.000 194.02623 ? 105 TRP A CB  1 
ATOM   2265 C CG  . TRP B 2 105 ? 62.21811 -55.30662 10.59716  1.000 197.30774 ? 105 TRP A CG  1 
ATOM   2266 C CD1 . TRP B 2 105 ? 61.08274 -55.29707 9.84151   1.000 195.72041 ? 105 TRP A CD1 1 
ATOM   2267 C CD2 . TRP B 2 105 ? 63.18268 -54.52184 9.88158   1.000 200.20694 ? 105 TRP A CD2 1 
ATOM   2268 N NE1 . TRP B 2 105 ? 61.28274 -54.56817 8.69493   1.000 197.55365 ? 105 TRP A NE1 1 
ATOM   2269 C CE2 . TRP B 2 105 ? 62.56254 -54.07931 8.69626   1.000 198.67251 ? 105 TRP A CE2 1 
ATOM   2270 C CE3 . TRP B 2 105 ? 64.50993 -54.15356 10.12660  1.000 202.29207 ? 105 TRP A CE3 1 
ATOM   2271 C CZ2 . TRP B 2 105 ? 63.22316 -53.29047 7.75704   1.000 198.37288 ? 105 TRP A CZ2 1 
ATOM   2272 C CZ3 . TRP B 2 105 ? 65.16407 -53.36772 9.19214   1.000 202.97096 ? 105 TRP A CZ3 1 
ATOM   2273 C CH2 . TRP B 2 105 ? 64.51938 -52.94552 8.02255   1.000 200.77520 ? 105 TRP A CH2 1 
ATOM   2274 N N   . GLY B 2 106 ? 63.70352 -56.06242 14.72138  1.000 189.43225 ? 106 GLY A N   1 
ATOM   2275 C CA  . GLY B 2 106 ? 64.05817 -56.74132 15.96014  1.000 189.74874 ? 106 GLY A CA  1 
ATOM   2276 C C   . GLY B 2 106 ? 63.48912 -58.13708 16.11646  1.000 189.85509 ? 106 GLY A C   1 
ATOM   2277 O O   . GLY B 2 106 ? 63.06472 -58.50694 17.21733  1.000 187.73246 ? 106 GLY A O   1 
ATOM   2278 N N   . GLN B 2 107 ? 63.47083 -58.92172 15.04531  1.000 196.67882 ? 107 GLN A N   1 
ATOM   2279 C CA  . GLN B 2 107 ? 63.05990 -60.34108 15.08680  1.000 198.27701 ? 107 GLN A CA  1 
ATOM   2280 C C   . GLN B 2 107 ? 61.58431 -60.39450 15.49093  1.000 190.80204 ? 107 GLN A C   1 
ATOM   2281 O O   . GLN B 2 107 ? 60.79290 -59.54800 15.04918  1.000 185.77683 ? 107 GLN A O   1 
ATOM   2282 C CB  . GLN B 2 107 ? 63.98598 -61.13249 15.98463  1.000 204.24559 ? 107 GLN A CB  1 
ATOM   2283 C CG  . GLN B 2 107 ? 65.39265 -61.22395 15.44460  1.000 210.03736 ? 107 GLN A CG  1 
ATOM   2284 C CD  . GLN B 2 107 ? 66.35356 -61.92975 16.37653  1.000 212.72988 ? 107 GLN A CD  1 
ATOM   2285 O OE1 . GLN B 2 107 ? 66.15747 -61.97240 17.59246  1.000 210.88363 ? 107 GLN A OE1 1 
ATOM   2286 N NE2 . GLN B 2 107 ? 67.41119 -62.49074 15.80162  1.000 217.14449 ? 107 GLN A NE2 1 
ATOM   2287 N N   . GLY B 2 108 ? 61.18492 -61.36009 16.31047  1.000 187.77619 ? 108 GLY A N   1 
ATOM   2288 C CA  . GLY B 2 108 ? 59.79226 -61.46020 16.70136  1.000 182.51795 ? 108 GLY A CA  1 
ATOM   2289 C C   . GLY B 2 108 ? 59.56419 -62.59119 17.67983  1.000 186.02634 ? 108 GLY A C   1 
ATOM   2290 O O   . GLY B 2 108 ? 60.50501 -63.14977 18.24757  1.000 192.24900 ? 108 GLY A O   1 
ATOM   2291 N N   . THR B 2 109 ? 58.28404 -62.91392 17.87563  1.000 173.90855 ? 109 THR A N   1 
ATOM   2292 C CA  . THR B 2 109 ? 57.86797 -63.97427 18.78395  1.000 178.11120 ? 109 THR A CA  1 
ATOM   2293 C C   . THR B 2 109 ? 56.80519 -64.82751 18.10731  1.000 176.54377 ? 109 THR A C   1 
ATOM   2294 O O   . THR B 2 109 ? 55.96195 -64.31020 17.36841  1.000 171.43037 ? 109 THR A O   1 
ATOM   2295 C CB  . THR B 2 109 ? 57.31887 -63.41546 20.10394  1.000 177.97576 ? 109 THR A CB  1 
ATOM   2296 O OG1 . THR B 2 109 ? 56.75138 -64.48262 20.87300  1.000 183.21261 ? 109 THR A OG1 1 
ATOM   2297 C CG2 . THR B 2 109 ? 56.23968 -62.37090 19.83945  1.000 171.31842 ? 109 THR A CG2 1 
ATOM   2298 N N   . LEU B 2 110 ? 56.84884 -66.13483 18.36341  1.000 175.36178 ? 110 LEU A N   1 
ATOM   2299 C CA  . LEU B 2 110 ? 56.01460 -67.09015 17.64430  1.000 174.60934 ? 110 LEU A CA  1 
ATOM   2300 C C   . LEU B 2 110 ? 54.65236 -67.22586 18.30713  1.000 173.49649 ? 110 LEU A C   1 
ATOM   2301 O O   . LEU B 2 110 ? 54.55871 -67.41069 19.52444  1.000 176.77358 ? 110 LEU A O   1 
ATOM   2302 C CB  . LEU B 2 110 ? 56.69062 -68.46116 17.56036  1.000 180.21992 ? 110 LEU A CB  1 
ATOM   2303 C CG  . LEU B 2 110 ? 55.78137 -69.64881 17.22236  1.000 181.12679 ? 110 LEU A CG  1 
ATOM   2304 C CD1 . LEU B 2 110 ? 55.31529 -69.59796 15.77799  1.000 178.16236 ? 110 LEU A CD1 1 
ATOM   2305 C CD2 . LEU B 2 110 ? 56.51221 -70.95574 17.47238  1.000 187.12795 ? 110 LEU A CD2 1 
ATOM   2306 N N   . VAL B 2 111 ? 53.60217 -67.14054 17.49818  1.000 169.50955 ? 111 VAL A N   1 
ATOM   2307 C CA  . VAL B 2 111 ? 52.23781 -67.39047 17.93961  1.000 169.90549 ? 111 VAL A CA  1 
ATOM   2308 C C   . VAL B 2 111 ? 51.79959 -68.70734 17.31968  1.000 173.82054 ? 111 VAL A C   1 
ATOM   2309 O O   . VAL B 2 111 ? 51.84049 -68.86762 16.09375  1.000 173.36292 ? 111 VAL A O   1 
ATOM   2310 C CB  . VAL B 2 111 ? 51.29069 -66.24982 17.54042  1.000 164.30654 ? 111 VAL A CB  1 
ATOM   2311 C CG1 . VAL B 2 111 ? 49.84697 -66.72704 17.56958  1.000 165.61554 ? 111 VAL A CG1 1 
ATOM   2312 C CG2 . VAL B 2 111 ? 51.49600 -65.05022 18.44990  1.000 161.84435 ? 111 VAL A CG2 1 
ATOM   2313 N N   . THR B 2 112 ? 51.39323 -69.65280 18.16012  1.000 173.57138 ? 112 THR A N   1 
ATOM   2314 C CA  . THR B 2 112 ? 50.93391 -70.96057 17.70616  1.000 178.30451 ? 112 THR A CA  1 
ATOM   2315 C C   . THR B 2 112 ? 49.53113 -71.18704 18.24564  1.000 180.57702 ? 112 THR A C   1 
ATOM   2316 O O   . THR B 2 112 ? 49.35424 -71.44469 19.44080  1.000 182.89695 ? 112 THR A O   1 
ATOM   2317 C CB  . THR B 2 112 ? 51.87366 -72.07319 18.16421  1.000 184.17374 ? 112 THR A CB  1 
ATOM   2318 O OG1 . THR B 2 112 ? 52.32327 -71.80128 19.49699  1.000 185.16453 ? 112 THR A OG1 1 
ATOM   2319 C CG2 . THR B 2 112 ? 53.06998 -72.17405 17.23564  1.000 184.33364 ? 112 THR A CG2 1 
ATOM   2320 N N   . VAL B 2 113 ? 48.53815 -71.08761 17.36914  1.000 193.28328 ? 113 VAL A N   1 
ATOM   2321 C CA  . VAL B 2 113 ? 47.16143 -71.38921 17.73976  1.000 194.93127 ? 113 VAL A CA  1 
ATOM   2322 C C   . VAL B 2 113 ? 46.98678 -72.90333 17.67855  1.000 200.27014 ? 113 VAL A C   1 
ATOM   2323 O O   . VAL B 2 113 ? 46.97184 -73.49318 16.59575  1.000 202.11174 ? 113 VAL A O   1 
ATOM   2324 C CB  . VAL B 2 113 ? 46.16392 -70.67050 16.82798  1.000 192.24496 ? 113 VAL A CB  1 
ATOM   2325 C CG1 . VAL B 2 113 ? 44.80343 -70.63046 17.48475  1.000 193.57295 ? 113 VAL A CG1 1 
ATOM   2326 C CG2 . VAL B 2 113 ? 46.65587 -69.26054 16.52718  1.000 187.12963 ? 113 VAL A CG2 1 
ATOM   2327 N N   . SER B 2 114 ? 46.85905 -73.53339 18.84496  1.000 215.39012 ? 114 SER A N   1 
ATOM   2328 C CA  . SER B 2 114 ? 46.82040 -74.98492 18.93411  1.000 220.89740 ? 114 SER A CA  1 
ATOM   2329 C C   . SER B 2 114 ? 45.56660 -75.54173 18.26392  1.000 223.17002 ? 114 SER A C   1 
ATOM   2330 O O   . SER B 2 114 ? 44.66566 -74.81002 17.84325  1.000 220.70485 ? 114 SER A O   1 
ATOM   2331 C CB  . SER B 2 114 ? 46.87186 -75.43730 20.39366  1.000 224.11400 ? 114 SER A CB  1 
ATOM   2332 O OG  . SER B 2 114 ? 45.69794 -75.06132 21.09327  1.000 223.87577 ? 114 SER A OG  1 
ATOM   2333 N N   . SER B 2 115 ? 45.51978 -76.86632 18.17424  1.000 246.99612 ? 115 SER A N   1 
ATOM   2334 C CA  . SER B 2 115 ? 44.36794 -77.56095 17.61696  1.000 250.69458 ? 115 SER A CA  1 
ATOM   2335 C C   . SER B 2 115 ? 43.29896 -77.77186 18.68409  1.000 253.23347 ? 115 SER A C   1 
ATOM   2336 O O   . SER B 2 115 ? 42.10938 -77.56450 18.44283  1.000 254.02171 ? 115 SER A O   1 
ATOM   2337 C CB  . SER B 2 115 ? 44.79227 -78.90349 17.01894  1.000 256.02792 ? 115 SER A CB  1 
ATOM   2338 O OG  . SER B 2 115 ? 45.20982 -79.80057 18.03298  1.000 259.99019 ? 115 SER A OG  1 
HETATM 2339 C C1  . NAG C 3 .   ? 49.85689 -5.21057  10.26877  1.000 213.10272 ? 1   NAG C C1  1 
HETATM 2340 C C2  . NAG C 3 .   ? 51.31158 -4.76414  10.42653  1.000 213.10272 ? 1   NAG C C2  1 
HETATM 2341 C C3  . NAG C 3 .   ? 51.83446 -4.18012  9.11826   1.000 213.10272 ? 1   NAG C C3  1 
HETATM 2342 C C4  . NAG C 3 .   ? 51.62263 -5.15856  7.97114   1.000 213.10272 ? 1   NAG C C4  1 
HETATM 2343 C C5  . NAG C 3 .   ? 50.15832 -5.58013  7.90737   1.000 213.10272 ? 1   NAG C C5  1 
HETATM 2344 C C6  . NAG C 3 .   ? 49.88700 -6.63801  6.86309   1.000 213.10272 ? 1   NAG C C6  1 
HETATM 2345 C C7  . NAG C 3 .   ? 51.69002 -4.14533  12.77302  1.000 213.10272 ? 1   NAG C C7  1 
HETATM 2346 C C8  . NAG C 3 .   ? 51.80906 -3.01677  13.75168  1.000 213.10272 ? 1   NAG C C8  1 
HETATM 2347 N N2  . NAG C 3 .   ? 51.44945 -3.79801  11.50464  1.000 213.10272 ? 1   NAG C N2  1 
HETATM 2348 O O3  . NAG C 3 .   ? 53.21828 -3.87830  9.25798   1.000 213.10272 ? 1   NAG C O3  1 
HETATM 2349 O O4  . NAG C 3 .   ? 51.96915 -4.53208  6.74170   1.000 213.10272 ? 1   NAG C O4  1 
HETATM 2350 O O5  . NAG C 3 .   ? 49.74880 -6.12807  9.16864   1.000 213.10272 ? 1   NAG C O5  1 
HETATM 2351 O O6  . NAG C 3 .   ? 48.73414 -6.31964  6.09595   1.000 213.10272 ? 1   NAG C O6  1 
HETATM 2352 O O7  . NAG C 3 .   ? 51.80236 -5.31758  13.11558  1.000 213.10272 ? 1   NAG C O7  1 
HETATM 2353 C C1  . NAG C 3 .   ? 53.09718 -5.21694  6.16258   1.000 214.01665 ? 2   NAG C C1  1 
HETATM 2354 C C2  . NAG C 3 .   ? 53.20758 -4.82359  4.68929   1.000 214.01665 ? 2   NAG C C2  1 
HETATM 2355 C C3  . NAG C 3 .   ? 54.41742 -5.50748  4.05463   1.000 214.01665 ? 2   NAG C C3  1 
HETATM 2356 C C4  . NAG C 3 .   ? 55.67614 -5.19885  4.85564   1.000 214.01665 ? 2   NAG C C4  1 
HETATM 2357 C C5  . NAG C 3 .   ? 55.47778 -5.55971  6.32605   1.000 214.01665 ? 2   NAG C C5  1 
HETATM 2358 C C6  . NAG C 3 .   ? 56.64743 -5.14731  7.19038   1.000 214.01665 ? 2   NAG C C6  1 
HETATM 2359 C C7  . NAG C 3 .   ? 50.91565 -4.35513  3.93949   1.000 214.01665 ? 2   NAG C C7  1 
HETATM 2360 C C8  . NAG C 3 .   ? 49.74053 -4.85695  3.15469   1.000 214.01665 ? 2   NAG C C8  1 
HETATM 2361 N N2  . NAG C 3 .   ? 51.98801 -5.15575  3.96895   1.000 214.01665 ? 2   NAG C N2  1 
HETATM 2362 O O3  . NAG C 3 .   ? 54.58029 -5.07035  2.70974   1.000 214.01665 ? 2   NAG C O3  1 
HETATM 2363 O O4  . NAG C 3 .   ? 56.78645 -5.92414  4.33914   1.000 214.01665 ? 2   NAG C O4  1 
HETATM 2364 O O5  . NAG C 3 .   ? 54.32035 -4.88626  6.84482   1.000 214.01665 ? 2   NAG C O5  1 
HETATM 2365 O O6  . NAG C 3 .   ? 56.35698 -5.27331  8.57569   1.000 214.01665 ? 2   NAG C O6  1 
HETATM 2366 O O7  . NAG C 3 .   ? 50.89562 -3.27335  4.52005   1.000 214.01665 ? 2   NAG C O7  1 
HETATM 2367 C C1  . NAG D 4 .   ? 56.26730 -39.15129 -0.98235  1.000 206.09882 ? 301 NAG B C1  1 
HETATM 2368 C C2  . NAG D 4 .   ? 55.89395 -39.88789 -2.26511  1.000 206.09882 ? 301 NAG B C2  1 
HETATM 2369 C C3  . NAG D 4 .   ? 57.17211 -40.29396 -2.99972  1.000 206.09882 ? 301 NAG B C3  1 
HETATM 2370 C C4  . NAG D 4 .   ? 58.09308 -39.09171 -3.18697  1.000 206.09882 ? 301 NAG B C4  1 
HETATM 2371 C C5  . NAG D 4 .   ? 58.27950 -38.31721 -1.87890  1.000 206.09882 ? 301 NAG B C5  1 
HETATM 2372 C C6  . NAG D 4 .   ? 59.03099 -37.01796 -2.05552  1.000 206.09882 ? 301 NAG B C6  1 
HETATM 2373 C C7  . NAG D 4 .   ? 54.06735 -41.47685 -2.75375  1.000 206.09882 ? 301 NAG B C7  1 
HETATM 2374 C C8  . NAG D 4 .   ? 53.79855 -40.67307 -3.99144  1.000 206.09882 ? 301 NAG B C8  1 
HETATM 2375 N N2  . NAG D 4 .   ? 55.07433 -41.05504 -1.97661  1.000 206.09882 ? 301 NAG B N2  1 
HETATM 2376 O O3  . NAG D 4 .   ? 56.86128 -40.87166 -4.26273  1.000 206.09882 ? 301 NAG B O3  1 
HETATM 2377 O O4  . NAG D 4 .   ? 59.36797 -39.53984 -3.63334  1.000 206.09882 ? 301 NAG B O4  1 
HETATM 2378 O O5  . NAG D 4 .   ? 57.00623 -37.98612 -1.30422  1.000 206.09882 ? 301 NAG B O5  1 
HETATM 2379 O O6  . NAG D 4 .   ? 58.58866 -36.31139 -3.20617  1.000 206.09882 ? 301 NAG B O6  1 
HETATM 2380 O O7  . NAG D 4 .   ? 53.40195 -42.46706 -2.46891  1.000 206.09882 ? 301 NAG B O7  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   . MET A 1   ? 3.98243 3.24309 2.82615 -0.81863 -1.35831 0.31253  1   MET B N   
2    C CA  . MET A 1   ? 4.02315 3.23751 2.77014 -0.88313 -1.28971 0.24029  1   MET B CA  
3    C C   . MET A 1   ? 3.99019 3.07095 2.65121 -0.85657 -1.20545 0.21754  1   MET B C   
4    O O   . MET A 1   ? 3.99789 3.01889 2.61529 -0.88267 -1.12796 0.15792  1   MET B O   
5    C CB  . MET A 1   ? 3.89380 3.16742 2.53160 -0.97356 -1.33441 0.23252  1   MET B CB  
6    C CG  . MET A 1   ? 3.93724 3.15908 2.45746 -0.97547 -1.32003 0.25747  1   MET B CG  
7    S SD  . MET A 1   ? 4.02846 3.38248 2.53576 -1.01222 -1.37143 0.30141  1   MET B SD  
8    C CE  . MET A 1   ? 3.98365 3.36962 2.60171 -0.92616 -1.44294 0.40016  1   MET B CE  
9    N N   . LYS A 2   ? 4.11107 3.14702 2.75137 -0.80432 -1.21900 0.26551  2   LYS B N   
10   C CA  . LYS A 2   ? 4.07623 2.99983 2.64037 -0.77257 -1.14472 0.24891  2   LYS B CA  
11   C C   . LYS A 2   ? 4.01322 2.91897 2.66268 -0.68582 -1.14721 0.29155  2   LYS B C   
12   O O   . LYS A 2   ? 4.04177 2.97984 2.71667 -0.66650 -1.21442 0.34878  2   LYS B O   
13   C CB  . LYS A 2   ? 4.16164 3.04482 2.56560 -0.82162 -1.15162 0.25050  2   LYS B CB  
14   N N   . VAL A 3   ? 4.06481 2.92218 2.75954 -0.63519 -1.07205 0.26417  3   VAL B N   
15   C CA  . VAL A 3   ? 4.01724 2.86793 2.80252 -0.55578 -1.06246 0.29127  3   VAL B CA  
16   C C   . VAL A 3   ? 4.02007 2.81748 2.71864 -0.53939 -1.07084 0.32299  3   VAL B C   
17   O O   . VAL A 3   ? 3.99500 2.72122 2.59202 -0.53885 -1.01062 0.29843  3   VAL B O   
18   C CB  . VAL A 3   ? 3.96289 2.78230 2.79518 -0.51359 -0.97368 0.25177  3   VAL B CB  
19   C CG1 . VAL A 3   ? 3.97336 2.82464 2.93667 -0.43921 -0.97262 0.27257  3   VAL B CG1 
20   C CG2 . VAL A 3   ? 3.95681 2.80360 2.82897 -0.54872 -0.94858 0.21161  3   VAL B CG2 
21   N N   . LEU A 4   ? 3.92516 2.75724 2.66634 -0.52517 -1.14414 0.37898  4   LEU B N   
22   C CA  . LEU A 4   ? 3.93484 2.71623 2.60190 -0.51120 -1.15398 0.41334  4   LEU B CA  
23   C C   . LEU A 4   ? 3.87515 2.61718 2.59305 -0.44251 -1.09475 0.40341  4   LEU B C   
24   O O   . LEU A 4   ? 3.86781 2.54868 2.48962 -0.43694 -1.05658 0.39685  4   LEU B O   
25   C CB  . LEU A 4   ? 4.00011 2.82770 2.70717 -0.51435 -1.24762 0.48244  4   LEU B CB  
26   C CG  . LEU A 4   ? 4.03093 2.92334 2.70127 -0.57905 -1.28827 0.49354  4   LEU B CG  
27   C CD1 . LEU A 4   ? 4.12881 3.05656 2.83335 -0.57125 -1.32392 0.55268  4   LEU B CD1 
28   C CD2 . LEU A 4   ? 4.05917 2.91511 2.58376 -0.63999 -1.23731 0.44380  4   LEU B CD2 
29   N N   . GLN A 5   ? 3.98045 2.76610 2.84930 -0.39239 -1.08577 0.39897  5   GLN B N   
30   C CA  . GLN A 5   ? 3.92552 2.69589 2.85910 -0.32936 -1.03048 0.38541  5   GLN B CA  
31   C C   . GLN A 5   ? 3.89693 2.67035 2.84667 -0.31481 -0.95188 0.33258  5   GLN B C   
32   O O   . GLN A 5   ? 3.94540 2.77013 2.98588 -0.31580 -0.95467 0.31783  5   GLN B O   
33   C CB  . GLN A 5   ? 3.95984 2.78301 3.05925 -0.28223 -1.07146 0.41556  5   GLN B CB  
34   C CG  . GLN A 5   ? 3.89061 2.71836 3.07763 -0.22136 -1.01165 0.39136  5   GLN B CG  
35   C CD  . GLN A 5   ? 3.80099 2.56435 2.87534 -0.21371 -0.95768 0.37865  5   GLN B CD  
36   O OE1 . GLN A 5   ? 3.80907 2.53160 2.82838 -0.22039 -0.98506 0.41070  5   GLN B OE1 
37   N NE2 . GLN A 5   ? 3.70439 2.46315 2.74704 -0.19844 -0.87949 0.33361  5   GLN B NE2 
38   N N   . GLU A 6   ? 3.93250 2.65518 2.79572 -0.30096 -0.88203 0.30686  6   GLU B N   
39   C CA  . GLU A 6   ? 3.90186 2.62653 2.77682 -0.28042 -0.80294 0.26561  6   GLU B CA  
40   C C   . GLU A 6   ? 3.90848 2.70509 2.94889 -0.23283 -0.79265 0.25976  6   GLU B C   
41   O O   . GLU A 6   ? 3.88720 2.71213 3.01097 -0.19533 -0.81023 0.27512  6   GLU B O   
42   C CB  . GLU A 6   ? 3.82321 2.49882 2.59899 -0.25870 -0.73396 0.24727  6   GLU B CB  
43   C CG  . GLU A 6   ? 3.87893 2.48588 2.49087 -0.30087 -0.74132 0.25059  6   GLU B CG  
44   C CD  . GLU A 6   ? 3.91152 2.50734 2.49949 -0.30829 -0.80064 0.28800  6   GLU B CD  
45   O OE1 . GLU A 6   ? 3.91113 2.54731 2.61000 -0.29147 -0.85288 0.31815  6   GLU B OE1 
46   O OE2 . GLU A 6   ? 3.93839 2.48418 2.39829 -0.33122 -0.79386 0.28832  6   GLU B OE2 
47   N N   . PRO A 7   ? 3.46739 2.29597 2.56320 -0.23510 -0.76256 0.23596  7   PRO B N   
48   C CA  . PRO A 7   ? 3.48146 2.38937 2.73783 -0.19647 -0.75664 0.22825  7   PRO B CA  
49   C C   . PRO A 7   ? 3.41682 2.34944 2.71934 -0.13949 -0.70356 0.21709  7   PRO B C   
50   O O   . PRO A 7   ? 3.34515 2.23935 2.55379 -0.12716 -0.64818 0.20648  7   PRO B O   
51   C CB  . PRO A 7   ? 3.51623 2.43473 2.78094 -0.21709 -0.71652 0.20214  7   PRO B CB  
52   C CG  . PRO A 7   ? 3.53106 2.39034 2.67522 -0.27854 -0.73865 0.20241  7   PRO B CG  
53   C CD  . PRO A 7   ? 3.48034 2.27365 2.49795 -0.27806 -0.73182 0.21316  7   PRO B CD  
54   N N   . THR A 8   ? 3.34829 2.35461 2.80167 -0.10573 -0.71968 0.21601  8   THR B N   
55   C CA  . THR A 8   ? 3.25686 2.30738 2.77755 -0.05546 -0.67279 0.19907  8   THR B CA  
56   C C   . THR A 8   ? 3.26097 2.40830 2.94158 -0.03109 -0.65974 0.17826  8   THR B C   
57   O O   . THR A 8   ? 3.30674 2.49103 3.08684 -0.04052 -0.71490 0.18655  8   THR B O   
58   C CB  . THR A 8   ? 3.21501 2.24973 2.75830 -0.03982 -0.71021 0.21796  8   THR B CB  
59   O OG1 . THR A 8   ? 3.29432 2.32880 2.89508 -0.05827 -0.79337 0.24987  8   THR B OG1 
60   C CG2 . THR A 8   ? 3.18598 2.13940 2.56907 -0.05415 -0.69517 0.22737  8   THR B CG2 
61   N N   . CYS A 9   ? 3.05540 2.25294 2.76144 -0.00032 -0.58745 0.15162  9   CYS B N   
62   C CA  . CYS A 9   ? 3.05240 2.35078 2.90142 0.01965  -0.56608 0.12860  9   CYS B CA  
63   C C   . CYS A 9   ? 2.95941 2.33451 2.88393 0.06347  -0.51684 0.10253  9   CYS B C   
64   O O   . CYS A 9   ? 2.90882 2.26644 2.74964 0.07895  -0.47071 0.09713  9   CYS B O   
65   C CB  . CYS A 9   ? 3.10366 2.40879 2.91683 0.00459  -0.51923 0.12087  9   CYS B CB  
66   S SG  . CYS A 9   ? 3.20667 2.41219 2.89748 -0.05328 -0.55035 0.13941  9   CYS B SG  
67   N N   . VAL A 10  ? 2.78886 2.25811 2.87626 0.08110  -0.52597 0.08211  10  VAL B N   
68   C CA  . VAL A 10  ? 2.71818 2.29011 2.90019 0.11639  -0.47127 0.04645  10  VAL B CA  
69   C C   . VAL A 10  ? 2.69917 2.36645 2.96898 0.11706  -0.44155 0.02734  10  VAL B C   
70   O O   . VAL A 10  ? 2.73347 2.39328 3.03127 0.09283  -0.47642 0.03735  10  VAL B O   
71   C CB  . VAL A 10  ? 2.66950 2.27568 2.98095 0.13696  -0.50173 0.03122  10  VAL B CB  
72   C CG1 . VAL A 10  ? 2.67153 2.18177 2.89090 0.13506  -0.52340 0.05252  10  VAL B CG1 
73   C CG2 . VAL A 10  ? 2.67653 2.30521 3.11726 0.12925  -0.56832 0.03818  10  VAL B CG2 
74   N N   . SER A 11  ? 2.51470 2.27974 2.82594 0.14222  -0.37500 -0.00102 11  SER B N   
75   C CA  . SER A 11  ? 2.48232 2.34718 2.86619 0.14307  -0.33669 -0.01678 11  SER B CA  
76   C C   . SER A 11  ? 2.39410 2.39658 2.94631 0.16538  -0.32076 -0.06114 11  SER B C   
77   O O   . SER A 11  ? 2.35521 2.39781 2.92646 0.18747  -0.29320 -0.08487 11  SER B O   
78   C CB  . SER A 11  ? 2.49666 2.36822 2.76876 0.15079  -0.26356 -0.00506 11  SER B CB  
79   O OG  . SER A 11  ? 2.49082 2.43990 2.81876 0.14546  -0.23113 -0.00847 11  SER B OG  
80   N N   . ASP A 12  ? 2.24210 2.32124 2.91855 0.15656  -0.33539 -0.07734 12  ASP B N   
81   C CA  . ASP A 12  ? 2.14479 2.37116 2.98213 0.17472  -0.30894 -0.12593 12  ASP B CA  
82   C C   . ASP A 12  ? 2.09612 2.43105 2.91332 0.18641  -0.22654 -0.14120 12  ASP B C   
83   O O   . ASP A 12  ? 2.01419 2.48665 2.95101 0.19981  -0.19348 -0.18631 12  ASP B O   
84   C CB  . ASP A 12  ? 2.11019 2.39292 3.09058 0.16095  -0.35110 -0.14137 12  ASP B CB  
85   C CG  . ASP A 12  ? 2.14047 2.44344 3.08996 0.13632  -0.33231 -0.12697 12  ASP B CG  
86   O OD1 . ASP A 12  ? 2.19250 2.45318 3.00940 0.13127  -0.28822 -0.09961 12  ASP B OD1 
87   O OD2 . ASP A 12  ? 2.11724 2.47774 3.17996 0.12185  -0.36074 -0.14325 12  ASP B OD2 
88   N N   . TYR A 13  ? 2.30246 2.58269 2.97486 0.18142  -0.19245 -0.10409 13  TYR B N   
89   C CA  . TYR A 13  ? 2.27134 2.63790 2.89464 0.19717  -0.11453 -0.10206 13  TYR B CA  
90   C C   . TYR A 13  ? 2.20830 2.71491 2.93779 0.19159  -0.08198 -0.11916 13  TYR B C   
91   O O   . TYR A 13  ? 2.13836 2.77144 2.88162 0.20770  -0.01958 -0.13122 13  TYR B O   
92   C CB  . TYR A 13  ? 2.21319 2.64572 2.83347 0.22358  -0.07692 -0.13064 13  TYR B CB  
93   C CG  . TYR A 13  ? 2.21510 2.69034 2.72413 0.24196  -0.00632 -0.11048 13  TYR B CG  
94   C CD1 . TYR A 13  ? 2.27438 2.68346 2.67350 0.23746  0.01364  -0.06066 13  TYR B CD1 
95   C CD2 . TYR A 13  ? 2.15243 2.73373 2.66743 0.26403  0.04159  -0.14110 13  TYR B CD2 
96   C CE1 . TYR A 13  ? 2.27357 2.72079 2.57619 0.25996  0.07771  -0.03580 13  TYR B CE1 
97   C CE2 . TYR A 13  ? 2.13854 2.77065 2.55280 0.28403  0.10402  -0.11898 13  TYR B CE2 
98   C CZ  . TYR A 13  ? 2.20242 2.76571 2.51172 0.28474  0.12075  -0.06304 13  TYR B CZ  
99   O OH  . TYR A 13  ? 2.18968 2.80361 2.40434 0.31032  0.18291  -0.03505 13  TYR B OH  
100  N N   . MET A 14  ? 2.12826 2.62443 2.93295 0.16724  -0.12298 -0.12090 14  MET B N   
101  C CA  . MET A 14  ? 2.09649 2.69936 2.97336 0.15359  -0.09277 -0.12701 14  MET B CA  
102  C C   . MET A 14  ? 2.20881 2.71683 3.04489 0.12064  -0.12044 -0.09555 14  MET B C   
103  O O   . MET A 14  ? 2.25426 2.78476 3.05557 0.10974  -0.07572 -0.07268 14  MET B O   
104  C CB  . MET A 14  ? 1.98213 2.73207 3.04810 0.15327  -0.10427 -0.18474 14  MET B CB  
105  C CG  . MET A 14  ? 1.91406 2.80790 3.04838 0.14168  -0.05637 -0.19562 14  MET B CG  
106  S SD  . MET A 14  ? 1.77818 2.85574 3.13918 0.13736  -0.06582 -0.27108 14  MET B SD  
107  C CE  . MET A 14  ? 1.79828 2.90511 3.20300 0.09942  -0.07251 -0.25951 14  MET B CE  
108  N N   . SER A 15  ? 2.23587 2.64300 3.07665 0.10291  -0.19111 -0.09318 15  SER B N   
109  C CA  . SER A 15  ? 2.32566 2.66728 3.14883 0.06530  -0.21908 -0.07527 15  SER B CA  
110  C C   . SER A 15  ? 2.41984 2.61171 3.15994 0.04724  -0.28225 -0.05295 15  SER B C   
111  O O   . SER A 15  ? 2.54290 2.64743 3.20134 0.01552  -0.28582 -0.02922 15  SER B O   
112  C CB  . SER A 15  ? 2.24990 2.70643 3.23882 0.04930  -0.24338 -0.11268 15  SER B CB  
113  O OG  . SER A 15  ? 2.17722 2.68180 3.28602 0.06718  -0.29100 -0.14735 15  SER B OG  
114  N N   . ILE A 16  ? 2.34060 2.50315 3.10009 0.06401  -0.32976 -0.06025 16  ILE B N   
115  C CA  . ILE A 16  ? 2.41036 2.45780 3.11788 0.04453  -0.40040 -0.03998 16  ILE B CA  
116  C C   . ILE A 16  ? 2.42436 2.37563 3.01145 0.06153  -0.40136 -0.01867 16  ILE B C   
117  O O   . ILE A 16  ? 2.35157 2.34350 2.97378 0.09320  -0.38715 -0.03422 16  ILE B O   
118  C CB  . ILE A 16  ? 2.35695 2.45713 3.21422 0.04547  -0.47037 -0.06131 16  ILE B CB  
119  C CG1 . ILE A 16  ? 2.34479 2.53454 3.31127 0.02185  -0.47487 -0.08334 16  ILE B CG1 
120  C CG2 . ILE A 16  ? 2.42555 2.41707 3.22348 0.03080  -0.54436 -0.03263 16  ILE B CG2 
121  C CD1 . ILE A 16  ? 2.28466 2.55158 3.42004 0.02971  -0.53570 -0.10967 16  ILE B CD1 
122  N N   . SER A 17  ? 2.55188 2.37945 2.99970 0.03675  -0.41637 0.01228  17  SER B N   
123  C CA  . SER A 17  ? 2.57556 2.30246 2.90743 0.04314  -0.43326 0.03304  17  SER B CA  
124  C C   . SER A 17  ? 2.63617 2.29237 2.95593 0.01347  -0.51555 0.04995  17  SER B C   
125  O O   . SER A 17  ? 2.73053 2.32703 2.98004 -0.02494 -0.52972 0.06295  17  SER B O   
126  C CB  . SER A 17  ? 2.64121 2.29075 2.81376 0.03965  -0.37634 0.05350  17  SER B CB  
127  O OG  . SER A 17  ? 2.59016 2.31204 2.76676 0.07448  -0.30529 0.04440  17  SER B OG  
128  N N   . THR A 18  ? 2.63935 2.30733 3.03151 0.03022  -0.56769 0.04991  18  THR B N   
129  C CA  . THR A 18  ? 2.68629 2.30755 3.08351 0.00776  -0.65079 0.07231  18  THR B CA  
130  C C   . THR A 18  ? 2.74173 2.24677 2.98353 -0.00475 -0.66862 0.10344  18  THR B C   
131  O O   . THR A 18  ? 2.70845 2.18699 2.90376 0.02006  -0.64134 0.10460  18  THR B O   
132  C CB  . THR A 18  ? 2.62694 2.31578 3.18684 0.03547  -0.69794 0.06368  18  THR B CB  
133  O OG1 . THR A 18  ? 2.58737 2.39039 3.29398 0.04200  -0.68406 0.03029  18  THR B OG1 
134  C CG2 . THR A 18  ? 2.66874 2.31455 3.23154 0.01742  -0.78630 0.09720  18  THR B CG2 
135  N N   . CYS A 19  ? 3.01476 2.45881 3.17701 -0.04680 -0.71271 0.12468  19  CYS B N   
136  C CA  . CYS A 19  ? 3.07340 2.41294 3.08092 -0.06859 -0.73035 0.15142  19  CYS B CA  
137  C C   . CYS A 19  ? 3.10343 2.42765 3.12560 -0.08893 -0.82067 0.18166  19  CYS B C   
138  O O   . CYS A 19  ? 3.09529 2.48589 3.23695 -0.09112 -0.86955 0.18238  19  CYS B O   
139  C CB  . CYS A 19  ? 3.14820 2.42526 3.02294 -0.10696 -0.69065 0.14756  19  CYS B CB  
140  S SG  . CYS A 19  ? 3.15256 2.43600 2.98818 -0.08064 -0.58352 0.12695  19  CYS B SG  
141  N N   . GLU A 20  ? 3.28179 2.52378 3.17934 -0.10388 -0.84247 0.20854  20  GLU B N   
142  C CA  . GLU A 20  ? 3.33638 2.55999 3.21779 -0.12923 -0.92665 0.24562  20  GLU B CA  
143  C C   . GLU A 20  ? 3.38059 2.50975 3.08101 -0.16320 -0.92715 0.26378  20  GLU B C   
144  O O   . GLU A 20  ? 3.34924 2.42601 2.95814 -0.15223 -0.86902 0.25214  20  GLU B O   
145  C CB  . GLU A 20  ? 3.30265 2.55489 3.30010 -0.08944 -0.97340 0.27019  20  GLU B CB  
146  C CG  . GLU A 20  ? 3.30403 2.50384 3.25740 -0.05916 -0.94090 0.27529  20  GLU B CG  
147  C CD  . GLU A 20  ? 3.31799 2.50490 3.33060 -0.04017 -1.00240 0.31666  20  GLU B CD  
148  O OE1 . GLU A 20  ? 3.30354 2.55428 3.47422 -0.01529 -1.03973 0.32236  20  GLU B OE1 
149  O OE2 . GLU A 20  ? 3.34043 2.45303 3.24405 -0.04991 -1.01229 0.34466  20  GLU B OE2 
150  N N   . TRP A 21  ? 3.51351 2.63197 3.16503 -0.20580 -0.99363 0.29090  21  TRP B N   
151  C CA  . TRP A 21  ? 3.52759 2.56896 3.01428 -0.24437 -1.00610 0.30965  21  TRP B CA  
152  C C   . TRP A 21  ? 3.58158 2.64800 3.07210 -0.27483 -1.09924 0.35279  21  TRP B C   
153  O O   . TRP A 21  ? 3.58903 2.72918 3.21089 -0.26069 -1.15053 0.36849  21  TRP B O   
154  C CB  . TRP A 21  ? 3.52442 2.52075 2.89071 -0.28622 -0.95130 0.27565  21  TRP B CB  
155  C CG  . TRP A 21  ? 3.57114 2.61070 2.96774 -0.32958 -0.96576 0.25626  21  TRP B CG  
156  C CD1 . TRP A 21  ? 3.60036 2.63835 2.92345 -0.39220 -1.00811 0.25941  21  TRP B CD1 
157  C CD2 . TRP A 21  ? 3.58179 2.67736 3.08649 -0.31869 -0.93300 0.22627  21  TRP B CD2 
158  N NE1 . TRP A 21  ? 3.63811 2.72652 3.01990 -0.42132 -1.00325 0.23086  21  TRP B NE1 
159  C CE2 . TRP A 21  ? 3.62398 2.74449 3.11612 -0.37685 -0.95740 0.21178  21  TRP B CE2 
160  C CE3 . TRP A 21  ? 3.54696 2.68152 3.15765 -0.26901 -0.88452 0.20854  21  TRP B CE3 
161  C CZ2 . TRP A 21  ? 3.64143 2.81650 3.22294 -0.38636 -0.93436 0.18141  21  TRP B CZ2 
162  C CZ3 . TRP A 21  ? 3.55444 2.74618 3.25191 -0.27788 -0.86358 0.18145  21  TRP B CZ3 
163  C CH2 . TRP A 21  ? 3.60954 2.81708 3.29181 -0.33588 -0.88809 0.16866  21  TRP B CH2 
164  N N   . LYS A 22  ? 3.72081 2.73317 3.06711 -0.31659 -1.12109 0.37284  22  LYS B N   
165  C CA  . LYS A 22  ? 3.78384 2.82381 3.11436 -0.34759 -1.20968 0.42156  22  LYS B CA  
166  C C   . LYS A 22  ? 3.79150 2.80222 2.96204 -0.41959 -1.21449 0.41163  22  LYS B C   
167  O O   . LYS A 22  ? 3.73800 2.67295 2.77849 -0.43391 -1.17110 0.39816  22  LYS B O   
168  C CB  . LYS A 22  ? 3.78892 2.79754 3.12574 -0.31433 -1.24390 0.47379  22  LYS B CB  
169  N N   . MET A 23  ? 3.81344 2.89124 2.99635 -0.46640 -1.26546 0.41406  23  MET B N   
170  C CA  . MET A 23  ? 3.83054 2.89957 2.87279 -0.54236 -1.27848 0.40289  23  MET B CA  
171  C C   . MET A 23  ? 3.86394 2.96329 2.86351 -0.56366 -1.36472 0.46664  23  MET B C   
172  O O   . MET A 23  ? 3.89411 3.00325 2.96804 -0.51582 -1.40702 0.52094  23  MET B O   
173  C CB  . MET A 23  ? 3.86270 2.99700 2.93743 -0.59016 -1.27910 0.36201  23  MET B CB  
174  C CG  . MET A 23  ? 3.84409 2.97278 3.00544 -0.56096 -1.20920 0.31385  23  MET B CG  
175  S SD  . MET A 23  ? 3.86843 3.02214 3.00217 -0.63478 -1.17467 0.25015  23  MET B SD  
176  C CE  . MET A 23  ? 3.83334 2.87903 2.77217 -0.68530 -1.11682 0.21944  23  MET B CE  
177  N N   . ASN A 24  ? 4.00153 3.12022 2.88461 -0.63782 -1.38993 0.46049  24  ASN B N   
178  C CA  . ASN A 24  ? 4.02878 3.20235 2.88658 -0.66068 -1.45005 0.51599  24  ASN B CA  
179  C C   . ASN A 24  ? 4.06865 3.36922 3.00686 -0.68935 -1.50919 0.52447  24  ASN B C   
180  O O   . ASN A 24  ? 4.07281 3.40771 2.97629 -0.74732 -1.50068 0.47240  24  ASN B O   
181  C CB  . ASN A 24  ? 4.04486 3.18153 2.74954 -0.71588 -1.40881 0.49682  24  ASN B CB  
182  C CG  . ASN A 24  ? 4.06837 3.17789 2.67883 -0.77671 -1.36243 0.42248  24  ASN B CG  
183  O OD1 . ASN A 24  ? 4.05130 3.18761 2.70689 -0.79356 -1.36965 0.38583  24  ASN B OD1 
184  N ND2 . ASN A 24  ? 4.10964 3.16617 2.59588 -0.81170 -1.30994 0.39622  24  ASN B ND2 
185  N N   . GLY A 25  ? 3.78522 3.15620 2.83499 -0.64866 -1.56374 0.58651  25  GLY B N   
186  C CA  . GLY A 25  ? 3.82856 3.33242 2.96278 -0.66682 -1.62066 0.60073  25  GLY B CA  
187  C C   . GLY A 25  ? 3.78567 3.33426 3.04828 -0.64530 -1.63693 0.57098  25  GLY B C   
188  O O   . GLY A 25  ? 3.76648 3.24430 3.03456 -0.63075 -1.58906 0.52433  25  GLY B O   
189  N N   . PRO A 26  ? 3.68099 3.35582 3.05732 -0.63950 -1.69125 0.59346  26  PRO B N   
190  C CA  . PRO A 26  ? 3.63311 3.36810 3.15179 -0.61770 -1.70770 0.56443  26  PRO B CA  
191  C C   . PRO A 26  ? 3.61358 3.33060 3.08799 -0.67130 -1.64756 0.47705  26  PRO B C   
192  O O   . PRO A 26  ? 3.62557 3.36306 2.99010 -0.75021 -1.64172 0.44239  26  PRO B O   
193  C CB  . PRO A 26  ? 3.65311 3.53928 3.26429 -0.61897 -1.76784 0.59881  26  PRO B CB  
194  C CG  . PRO A 26  ? 3.73774 3.64827 3.22980 -0.66119 -1.77898 0.63112  26  PRO B CG  
195  C CD  . PRO A 26  ? 3.75031 3.52393 3.14070 -0.64480 -1.73996 0.65081  26  PRO B CD  
196  N N   . THR A 27  ? 3.71287 3.39312 3.28211 -0.62547 -1.58645 0.43752  27  THR B N   
197  C CA  . THR A 27  ? 3.70247 3.35950 3.25147 -0.66353 -1.50917 0.35749  27  THR B CA  
198  C C   . THR A 27  ? 3.66732 3.37808 3.38556 -0.61754 -1.49354 0.33481  27  THR B C   
199  O O   . THR A 27  ? 3.63654 3.32052 3.44595 -0.54420 -1.48370 0.35647  27  THR B O   
200  C CB  . THR A 27  ? 3.45342 2.96796 2.88613 -0.66134 -1.42065 0.32717  27  THR B CB  
201  O OG1 . THR A 27  ? 3.37313 2.82829 2.86746 -0.58044 -1.39681 0.35227  27  THR B OG1 
202  C CG2 . THR A 27  ? 3.54496 3.01301 2.80865 -0.71202 -1.43615 0.34415  27  THR B CG2 
203  N N   . ASN A 28  ? 3.49994 3.29132 3.26245 -0.66348 -1.48957 0.28780  28  ASN B N   
204  C CA  . ASN A 28  ? 3.46420 3.30166 3.37368 -0.63030 -1.46068 0.25423  28  ASN B CA  
205  C C   . ASN A 28  ? 3.47515 3.20623 3.33286 -0.63407 -1.35399 0.20068  28  ASN B C   
206  O O   . ASN A 28  ? 3.49258 3.21267 3.29568 -0.69539 -1.30763 0.14813  28  ASN B O   
207  C CB  . ASN A 28  ? 3.44502 3.42020 3.42687 -0.67872 -1.50211 0.22746  28  ASN B CB  
208  C CG  . ASN A 28  ? 3.40392 3.44697 3.55547 -0.63804 -1.48900 0.20262  28  ASN B CG  
209  O OD1 . ASN A 28  ? 3.41371 3.39475 3.58732 -0.61898 -1.41063 0.16475  28  ASN B OD1 
210  N ND2 . ASN A 28  ? 3.36265 3.53983 3.63834 -0.62167 -1.56682 0.22697  28  ASN B ND2 
211  N N   . CYS A 29  ? 3.46927 3.12360 3.34644 -0.56784 -1.31254 0.21505  29  CYS B N   
212  C CA  . CYS A 29  ? 3.47821 3.03273 3.29571 -0.56482 -1.21261 0.17545  29  CYS B CA  
213  C C   . CYS A 29  ? 3.47397 3.07120 3.36739 -0.58577 -1.16493 0.12306  29  CYS B C   
214  O O   . CYS A 29  ? 3.50181 3.03009 3.32234 -0.61809 -1.08878 0.08430  29  CYS B O   
215  C CB  . CYS A 29  ? 3.44811 2.94537 3.29691 -0.48746 -1.18175 0.19862  29  CYS B CB  
216  S SG  . CYS A 29  ? 3.43412 2.94476 3.30777 -0.44211 -1.26712 0.26916  29  CYS B SG  
217  N N   . SER A 30  ? 3.19896 2.91103 3.24019 -0.56986 -1.20893 0.12195  30  SER B N   
218  C CA  . SER A 30  ? 3.19490 2.95495 3.31729 -0.58864 -1.16385 0.07248  30  SER B CA  
219  C C   . SER A 30  ? 3.23565 3.00623 3.28534 -0.67758 -1.15150 0.03074  30  SER B C   
220  O O   . SER A 30  ? 3.25726 2.99747 3.30019 -0.70742 -1.07851 -0.01417 30  SER B O   
221  C CB  . SER A 30  ? 3.13017 3.01948 3.43252 -0.55121 -1.21656 0.07781  30  SER B CB  
222  O OG  . SER A 30  ? 3.07028 2.94831 3.45393 -0.47197 -1.21083 0.10261  30  SER B OG  
223  N N   . THR A 31  ? 3.33006 3.14530 3.32453 -0.72304 -1.21917 0.04482  31  THR B N   
224  C CA  . THR A 31  ? 3.35116 3.19395 3.28278 -0.81445 -1.21025 -0.00170 31  THR B CA  
225  C C   . THR A 31  ? 3.37960 3.08671 3.16455 -0.85684 -1.12617 -0.03349 31  THR B C   
226  O O   . THR A 31  ? 3.39032 3.08862 3.14754 -0.92318 -1.07671 -0.08807 31  THR B O   
227  C CB  . THR A 31  ? 3.34155 3.28210 3.24836 -0.85233 -1.30624 0.02399  31  THR B CB  
228  O OG1 . THR A 31  ? 3.34551 3.22221 3.16077 -0.82588 -1.33686 0.07701  31  THR B OG1 
229  C CG2 . THR A 31  ? 3.28599 3.37775 3.35018 -0.82023 -1.38609 0.04722  31  THR B CG2 
230  N N   . GLU A 32  ? 3.63462 3.23500 3.32860 -0.82055 -1.10562 -0.00282 32  GLU B N   
231  C CA  . GLU A 32  ? 3.65040 3.13603 3.19678 -0.86769 -1.04134 -0.03103 32  GLU B CA  
232  C C   . GLU A 32  ? 3.64876 3.00691 3.14350 -0.80971 -0.97007 -0.01649 32  GLU B C   
233  O O   . GLU A 32  ? 3.63053 2.90138 3.07701 -0.82636 -0.88261 -0.05060 32  GLU B O   
234  C CB  . GLU A 32  ? 3.66813 3.17281 3.10885 -0.91635 -1.10277 -0.01613 32  GLU B CB  
235  C CG  . GLU A 32  ? 3.70566 3.08660 2.98910 -0.94077 -1.05308 -0.02639 32  GLU B CG  
236  C CD  . GLU A 32  ? 3.71735 3.01466 2.94291 -0.99509 -0.95578 -0.09158 32  GLU B CD  
237  O OE1 . GLU A 32  ? 3.74319 3.06479 3.04600 -1.01283 -0.91737 -0.12801 32  GLU B OE1 
238  O OE2 . GLU A 32  ? 3.69860 2.90492 2.80001 -1.02365 -0.91669 -0.10754 32  GLU B OE2 
239  N N   . LEU A 33  ? 3.65460 3.00274 3.15972 -0.74263 -1.00427 0.03398  33  LEU B N   
240  C CA  . LEU A 33  ? 3.63486 2.87845 3.09110 -0.68753 -0.94033 0.04697  33  LEU B CA  
241  C C   . LEU A 33  ? 3.64966 2.87575 3.17741 -0.65716 -0.86139 0.02397  33  LEU B C   
242  O O   . LEU A 33  ? 3.64517 2.95432 3.30433 -0.63140 -0.87714 0.02360  33  LEU B O   
243  C CB  . LEU A 33  ? 3.60089 2.85724 3.08844 -0.61981 -0.99060 0.10002  33  LEU B CB  
244  C CG  . LEU A 33  ? 3.58774 2.85063 3.00403 -0.63351 -1.06643 0.13930  33  LEU B CG  
245  C CD1 . LEU A 33  ? 3.56696 2.76861 2.95740 -0.56942 -1.05758 0.17594  33  LEU B CD1 
246  C CD2 . LEU A 33  ? 3.57855 2.79644 2.84966 -0.71069 -1.05660 0.11462  33  LEU B CD2 
247  N N   . ARG A 34  ? 3.52062 2.64215 2.96230 -0.66006 -0.77567 0.00629  34  ARG B N   
248  C CA  . ARG A 34  ? 3.54540 2.64129 3.03581 -0.63494 -0.69239 -0.00961 34  ARG B CA  
249  C C   . ARG A 34  ? 3.51969 2.54355 2.96164 -0.57026 -0.64020 0.01480  34  ARG B C   
250  O O   . ARG A 34  ? 3.49871 2.43228 2.81901 -0.57933 -0.61100 0.01517  34  ARG B O   
251  C CB  . ARG A 34  ? 3.57484 2.61388 3.01447 -0.70148 -0.62837 -0.05333 34  ARG B CB  
252  C CG  . ARG A 34  ? 3.61243 2.73438 3.10762 -0.76979 -0.66986 -0.08607 34  ARG B CG  
253  C CD  . ARG A 34  ? 3.71593 2.77302 3.16360 -0.83840 -0.59619 -0.13468 34  ARG B CD  
254  N NE  . ARG A 34  ? 3.72922 2.87343 3.22240 -0.91188 -0.63570 -0.17267 34  ARG B NE  
255  C CZ  . ARG A 34  ? 3.75404 2.86279 3.21375 -0.98853 -0.58524 -0.22428 34  ARG B CZ  
256  N NH1 . ARG A 34  ? 3.76581 2.74470 3.15001 -1.00035 -0.49182 -0.24197 34  ARG B NH1 
257  N NH2 . ARG A 34  ? 3.75252 2.96077 3.25929 -1.05506 -0.62757 -0.26021 34  ARG B NH2 
258  N N   . LEU A 35  ? 3.32865 2.40147 2.86683 -0.50717 -0.62837 0.03160  35  LEU B N   
259  C CA  . LEU A 35  ? 3.28902 2.31662 2.79398 -0.44506 -0.57585 0.05151  35  LEU B CA  
260  C C   . LEU A 35  ? 3.31729 2.32484 2.84437 -0.43252 -0.48525 0.04037  35  LEU B C   
261  O O   . LEU A 35  ? 3.35794 2.43312 2.98914 -0.43807 -0.47871 0.02826  35  LEU B O   
262  C CB  . LEU A 35  ? 3.23525 2.33769 2.83114 -0.38437 -0.61952 0.07564  35  LEU B CB  
263  C CG  . LEU A 35  ? 3.16859 2.25301 2.74891 -0.31902 -0.57019 0.09176  35  LEU B CG  
264  C CD1 . LEU A 35  ? 3.09049 2.22361 2.75399 -0.28595 -0.50465 0.08392  35  LEU B CD1 
265  C CD2 . LEU A 35  ? 3.19704 2.17424 2.62463 -0.32317 -0.52868 0.09702  35  LEU B CD2 
266  N N   . LEU A 36  ? 3.32799 2.24639 2.75862 -0.41511 -0.41558 0.04681  36  LEU B N   
267  C CA  . LEU A 36  ? 3.34631 2.23335 2.78288 -0.39973 -0.32408 0.04643  36  LEU B CA  
268  C C   . LEU A 36  ? 3.29415 2.18206 2.71273 -0.32703 -0.28115 0.07384  36  LEU B C   
269  O O   . LEU A 36  ? 3.23782 2.06072 2.55467 -0.31189 -0.27028 0.08297  36  LEU B O   
270  C CB  . LEU A 36  ? 3.35044 2.12595 2.68924 -0.45102 -0.27105 0.02721  36  LEU B CB  
271  C CG  . LEU A 36  ? 3.40765 2.18453 2.78085 -0.52391 -0.27197 -0.00680 36  LEU B CG  
272  C CD1 . LEU A 36  ? 3.42343 2.25943 2.81288 -0.57249 -0.36721 -0.02492 36  LEU B CD1 
273  C CD2 . LEU A 36  ? 3.38626 2.04098 2.66722 -0.56498 -0.19794 -0.02673 36  LEU B CD2 
274  N N   . TYR A 37  ? 2.95854 1.92952 2.47545 -0.28484 -0.25606 0.08392  37  TYR B N   
275  C CA  . TYR A 37  ? 2.90115 1.90265 2.41575 -0.21742 -0.21675 0.10623  37  TYR B CA  
276  C C   . TYR A 37  ? 2.91798 1.92920 2.45515 -0.19508 -0.13039 0.12009  37  TYR B C   
277  O O   . TYR A 37  ? 2.97705 2.04432 2.60469 -0.21118 -0.12093 0.11316  37  TYR B O   
278  C CB  . TYR A 37  ? 2.87345 1.98733 2.49106 -0.18247 -0.27006 0.10576  37  TYR B CB  
279  C CG  . TYR A 37  ? 2.92480 2.14518 2.68592 -0.18718 -0.28434 0.09281  37  TYR B CG  
280  C CD1 . TYR A 37  ? 2.94704 2.19164 2.76735 -0.23314 -0.34657 0.07431  37  TYR B CD1 
281  C CD2 . TYR A 37  ? 2.90440 2.21375 2.74362 -0.14621 -0.23702 0.09761  37  TYR B CD2 
282  C CE1 . TYR A 37  ? 2.94030 2.28812 2.89467 -0.23725 -0.35993 0.05901  37  TYR B CE1 
283  C CE2 . TYR A 37  ? 2.91784 2.33104 2.88953 -0.15298 -0.24924 0.08169  37  TYR B CE2 
284  C CZ  . TYR A 37  ? 2.92033 2.34961 2.95019 -0.19778 -0.31064 0.06143  37  TYR B CZ  
285  O OH  . TYR A 37  ? 2.88666 2.42442 3.05096 -0.20453 -0.32232 0.04230  37  TYR B OH  
286  N N   . GLN A 38  ? 2.99004 1.94989 2.44455 -0.15831 -0.06746 0.14188  38  GLN B N   
287  C CA  . GLN A 38  ? 2.98786 1.96126 2.45650 -0.12673 0.01689  0.16702  38  GLN B CA  
288  C C   . GLN A 38  ? 2.91005 1.92899 2.34895 -0.05915 0.05087  0.19119  38  GLN B C   
289  O O   . GLN A 38  ? 2.85548 1.83534 2.21487 -0.04432 0.03390  0.18951  38  GLN B O   
290  C CB  . GLN A 38  ? 3.00482 1.85183 2.39644 -0.15492 0.07917  0.17374  38  GLN B CB  
291  C CG  . GLN A 38  ? 3.06362 1.85710 2.46967 -0.22935 0.05604  0.14334  38  GLN B CG  
292  C CD  . GLN A 38  ? 3.07017 1.75245 2.42894 -0.25297 0.13628  0.14992  38  GLN B CD  
293  O OE1 . GLN A 38  ? 3.05453 1.73442 2.41982 -0.21298 0.21007  0.18514  38  GLN B OE1 
294  N NE2 . GLN A 38  ? 3.08982 1.68265 2.40345 -0.31889 0.12445  0.11655  38  GLN B NE2 
295  N N   . LEU A 39  ? 2.90158 2.01072 2.40311 -0.02126 0.10109  0.21295  39  LEU B N   
296  C CA  . LEU A 39  ? 2.81231 1.98818 2.29309 0.04213  0.14202  0.23634  39  LEU B CA  
297  C C   . LEU A 39  ? 2.79374 1.87362 2.16870 0.06446  0.21395  0.26884  39  LEU B C   
298  O O   . LEU A 39  ? 2.83072 1.78633 2.15194 0.02890  0.23118  0.26845  39  LEU B O   
299  C CB  . LEU A 39  ? 2.79395 2.12114 2.38761 0.06864  0.16465  0.24485  39  LEU B CB  
300  C CG  . LEU A 39  ? 2.68513 2.14082 2.30124 0.12458  0.18013  0.24952  39  LEU B CG  
301  C CD1 . LEU A 39  ? 2.62960 2.07105 2.21122 0.12892  0.12533  0.22271  39  LEU B CD1 
302  C CD2 . LEU A 39  ? 2.66114 2.27387 2.41251 0.12904  0.17643  0.23705  39  LEU B CD2 
303  N N   . VAL A 40  ? 2.88623 2.02730 2.23348 0.12371  0.25849  0.29495  40  VAL B N   
304  C CA  . VAL A 40  ? 2.85111 1.90603 2.09632 0.15307  0.32132  0.32577  40  VAL B CA  
305  C C   . VAL A 40  ? 2.82532 1.93895 2.09727 0.19718  0.40135  0.37662  40  VAL B C   
306  O O   . VAL A 40  ? 2.75000 1.95621 2.00912 0.25399  0.43524  0.40167  40  VAL B O   
307  C CB  . VAL A 40  ? 2.78072 1.84506 1.94801 0.18683  0.30878  0.31731  40  VAL B CB  
308  C CG1 . VAL A 40  ? 2.81608 1.76922 1.91602 0.14040  0.24954  0.28104  40  VAL B CG1 
309  C CG2 . VAL A 40  ? 2.72189 1.94749 1.95646 0.21872  0.28666  0.30678  40  VAL B CG2 
310  N N   . PHE A 41  ? 2.85984 1.92341 2.16747 0.16996  0.43401  0.39392  41  PHE B N   
311  C CA  . PHE A 41  ? 2.84032 1.92949 2.16093 0.20822  0.51608  0.45203  41  PHE B CA  
312  C C   . PHE A 41  ? 2.89544 1.81207 2.16490 0.18349  0.56575  0.46926  41  PHE B C   
313  O O   . PHE A 41  ? 2.92755 1.71374 2.13193 0.14833  0.54489  0.43667  41  PHE B O   
314  C CB  . PHE A 41  ? 2.84306 2.07077 2.27764 0.20357  0.51851  0.46175  41  PHE B CB  
315  C CG  . PHE A 41  ? 2.72994 2.14149 2.20283 0.25781  0.52740  0.47740  41  PHE B CG  
316  C CD1 . PHE A 41  ? 2.66271 2.14060 2.12178 0.27500  0.48124  0.44224  41  PHE B CD1 
317  C CD2 . PHE A 41  ? 2.68575 2.20926 2.20965 0.28786  0.58403  0.52604  41  PHE B CD2 
318  C CE1 . PHE A 41  ? 2.54589 2.19892 2.04362 0.31894  0.49353  0.44823  41  PHE B CE1 
319  C CE2 . PHE A 41  ? 2.56440 2.27300 2.12428 0.33257  0.59341  0.53517  41  PHE B CE2 
320  C CZ  . PHE A 41  ? 2.49750 2.27167 2.04560 0.34705  0.54913  0.49261  41  PHE B CZ  
321  N N   . LEU A 42  ? 2.91942 1.83636 2.22012 0.20026  0.63591  0.52098  42  LEU B N   
322  C CA  . LEU A 42  ? 2.94393 1.69893 2.20335 0.18749  0.70106  0.54639  42  LEU B CA  
323  C C   . LEU A 42  ? 3.02584 1.70747 2.33670 0.11266  0.69622  0.52004  42  LEU B C   
324  O O   . LEU A 42  ? 3.05492 1.58202 2.32289 0.06913  0.71083  0.49602  42  LEU B O   
325  C CB  . LEU A 42  ? 2.88858 1.67569 2.14875 0.25402  0.78854  0.62786  42  LEU B CB  
326  C CG  . LEU A 42  ? 2.79228 1.69118 2.01362 0.33208  0.79826  0.65886  42  LEU B CG  
327  C CD1 . LEU A 42  ? 2.74650 1.85669 2.04401 0.35556  0.77973  0.67132  42  LEU B CD1 
328  C CD2 . LEU A 42  ? 2.76134 1.59824 1.93387 0.39334  0.88542  0.72987  42  LEU B CD2 
329  N N   . LEU A 43  ? 2.77699 1.57219 2.18062 0.09370  0.67823  0.51931  43  LEU B N   
330  C CA  . LEU A 43  ? 2.85308 1.59837 2.30939 0.01741  0.66214  0.48343  43  LEU B CA  
331  C C   . LEU A 43  ? 2.89126 1.71731 2.39101 -0.02176 0.56399  0.41952  43  LEU B C   
332  O O   . LEU A 43  ? 2.93351 1.84792 2.52238 -0.05317 0.53774  0.40221  43  LEU B O   
333  C CB  . LEU A 43  ? 2.86733 1.67187 2.40103 0.01564  0.71575  0.52655  43  LEU B CB  
334  C CG  . LEU A 43  ? 2.90959 1.60318 2.41951 0.03177  0.81678  0.58943  43  LEU B CG  
335  C CD1 . LEU A 43  ? 3.00514 1.50663 2.47916 -0.03263 0.83744  0.55323  43  LEU B CD1 
336  C CD2 . LEU A 43  ? 2.85809 1.55458 2.30682 0.11685  0.86802  0.65303  43  LEU B CD2 
337  N N   . SER A 44  ? 3.00465 1.80305 2.44389 -0.01837 0.51075  0.38668  44  SER B N   
338  C CA  . SER A 44  ? 3.03245 1.89959 2.50886 -0.04883 0.41698  0.33383  44  SER B CA  
339  C C   . SER A 44  ? 3.10889 1.93802 2.63302 -0.12695 0.38493  0.29221  44  SER B C   
340  O O   . SER A 44  ? 3.13140 1.84135 2.62669 -0.16821 0.42723  0.28870  44  SER B O   
341  C CB  . SER A 44  ? 2.99261 1.80371 2.38056 -0.04120 0.37376  0.31038  44  SER B CB  
342  O OG  . SER A 44  ? 2.93413 1.84159 2.31172 0.02241  0.36853  0.32872  44  SER B OG  
343  N N   . GLU A 45  ? 3.10077 2.03612 2.70313 -0.14754 0.31178  0.25823  45  GLU B N   
344  C CA  . GLU A 45  ? 3.16325 2.09371 2.82215 -0.21856 0.27269  0.21673  45  GLU B CA  
345  C C   . GLU A 45  ? 3.16404 2.09422 2.80764 -0.24687 0.18050  0.17303  45  GLU B C   
346  O O   . GLU A 45  ? 3.12551 2.10296 2.75431 -0.20764 0.13864  0.17466  45  GLU B O   
347  C CB  . GLU A 45  ? 3.20991 2.27883 2.99143 -0.22056 0.26864  0.21686  45  GLU B CB  
348  C CG  . GLU A 45  ? 3.29306 2.33662 3.12520 -0.28984 0.27961  0.19303  45  GLU B CG  
349  C CD  . GLU A 45  ? 3.35898 2.43710 3.23612 -0.34343 0.19180  0.13714  45  GLU B CD  
350  O OE1 . GLU A 45  ? 3.39008 2.59555 3.34767 -0.32597 0.13127  0.12193  45  GLU B OE1 
351  O OE2 . GLU A 45  ? 3.38346 2.36622 3.21924 -0.40320 0.18517  0.10786  45  GLU B OE2 
352  N N   . ALA A 46  ? 3.21196 2.09202 2.85895 -0.31697 0.15089  0.13506  46  ALA B N   
353  C CA  . ALA A 46  ? 3.20671 2.07932 2.82961 -0.35135 0.06614  0.09866  46  ALA B CA  
354  C C   . ALA A 46  ? 3.24546 2.25018 2.98181 -0.36286 -0.01017 0.07595  46  ALA B C   
355  O O   . ALA A 46  ? 3.29022 2.34536 3.10823 -0.39684 -0.00458 0.06039  46  ALA B O   
356  C CB  . ALA A 46  ? 3.20194 1.96064 2.76353 -0.42447 0.07510  0.06664  46  ALA B CB  
357  N N   . HIS A 47  ? 3.07066 2.12881 2.81428 -0.33538 -0.07966 0.07344  47  HIS B N   
358  C CA  . HIS A 47  ? 3.09394 2.26910 2.94595 -0.34097 -0.15777 0.05304  47  HIS B CA  
359  C C   . HIS A 47  ? 3.06924 2.21715 2.87898 -0.36953 -0.23904 0.03683  47  HIS B C   
360  O O   . HIS A 47  ? 3.02066 2.10515 2.73750 -0.35084 -0.24748 0.04971  47  HIS B O   
361  C CB  . HIS A 47  ? 3.07846 2.36160 3.00352 -0.27500 -0.16341 0.06845  47  HIS B CB  
362  C CG  . HIS A 47  ? 3.07066 2.36428 2.98537 -0.23190 -0.07806 0.09772  47  HIS B CG  
363  N ND1 . HIS A 47  ? 3.11372 2.43061 3.07428 -0.24606 -0.01958 0.10428  47  HIS B ND1 
364  C CD2 . HIS A 47  ? 3.00981 2.30190 2.87331 -0.17536 -0.04126 0.12474  47  HIS B CD2 
365  C CE1 . HIS A 47  ? 3.07423 2.40499 3.01215 -0.19783 0.04817  0.13919  47  HIS B CE1 
366  N NE2 . HIS A 47  ? 3.01326 2.33359 2.89297 -0.15400 0.03614  0.15039  47  HIS B NE2 
367  N N   . THR A 48  ? 3.14771 2.35103 3.02516 -0.41507 -0.29875 0.01028  48  THR B N   
368  C CA  . THR A 48  ? 3.12023 2.31699 2.96688 -0.44632 -0.38076 -0.00077 48  THR B CA  
369  C C   . THR A 48  ? 3.06417 2.38038 3.02716 -0.41965 -0.45985 -0.00010 48  THR B C   
370  O O   . THR A 48  ? 3.04765 2.45932 3.12925 -0.42384 -0.46957 -0.01580 48  THR B O   
371  C CB  . THR A 48  ? 3.14746 2.31347 2.96960 -0.52697 -0.38795 -0.03293 48  THR B CB  
372  O OG1 . THR A 48  ? 3.15512 2.19893 2.87296 -0.55156 -0.30962 -0.03645 48  THR B OG1 
373  C CG2 . THR A 48  ? 3.11292 2.29200 2.90267 -0.55983 -0.47626 -0.04035 48  THR B CG2 
374  N N   . CYS A 49  ? 3.20634 2.51523 3.13800 -0.39257 -0.51355 0.01779  49  CYS B N   
375  C CA  . CYS A 49  ? 3.12700 2.53161 3.16438 -0.36428 -0.58994 0.02326  49  CYS B CA  
376  C C   . CYS A 49  ? 3.13129 2.55352 3.16627 -0.41129 -0.67270 0.01869  49  CYS B C   
377  O O   . CYS A 49  ? 3.16245 2.50936 3.08090 -0.44399 -0.68812 0.02487  49  CYS B O   
378  C CB  . CYS A 49  ? 3.07044 2.45684 3.08095 -0.30599 -0.59617 0.04859  49  CYS B CB  
379  S SG  . CYS A 49  ? 2.98670 2.43567 3.07806 -0.27920 -0.69748 0.06535  49  CYS B SG  
380  N N   . ILE A 50  ? 3.05334 2.58436 3.21867 -0.41480 -0.72518 0.00732  50  ILE B N   
381  C CA  . ILE A 50  ? 3.05089 2.62776 3.23479 -0.45136 -0.81182 0.00829  50  ILE B CA  
382  C C   . ILE A 50  ? 2.98705 2.58223 3.19866 -0.40319 -0.87781 0.04373  50  ILE B C   
383  O O   . ILE A 50  ? 2.91307 2.57835 3.24840 -0.35150 -0.89146 0.04789  50  ILE B O   
384  C CB  . ILE A 50  ? 3.03133 2.72303 3.34636 -0.47654 -0.83615 -0.02058 50  ILE B CB  
385  C CG1 . ILE A 50  ? 3.00506 2.77315 3.36589 -0.49589 -0.93596 -0.01113 50  ILE B CG1 
386  C CG2 . ILE A 50  ? 2.97321 2.74355 3.42547 -0.42433 -0.81060 -0.02881 50  ILE B CG2 
387  C CD1 . ILE A 50  ? 3.08693 2.80440 3.31935 -0.56039 -0.96019 -0.01132 50  ILE B CD1 
388  N N   . PRO A 51  ? 3.24079 2.77513 3.34485 -0.41836 -0.91609 0.06886  51  PRO B N   
389  C CA  . PRO A 51  ? 3.19976 2.73547 3.31977 -0.37276 -0.97120 0.10798  51  PRO B CA  
390  C C   . PRO A 51  ? 3.17629 2.81031 3.40235 -0.37369 -1.06500 0.12545  51  PRO B C   
391  O O   . PRO A 51  ? 3.18062 2.88805 3.45910 -0.41292 -1.09114 0.10510  51  PRO B O   
392  C CB  . PRO A 51  ? 3.24125 2.67151 3.19019 -0.39881 -0.96740 0.12587  51  PRO B CB  
393  C CG  . PRO A 51  ? 3.29576 2.71201 3.17193 -0.47301 -0.95703 0.09792  51  PRO B CG  
394  C CD  . PRO A 51  ? 3.30286 2.75641 3.25835 -0.48024 -0.90055 0.06017  51  PRO B CD  
395  N N   . GLU A 52  ? 3.14751 2.78372 3.40782 -0.32848 -1.11400 0.16487  52  GLU B N   
396  C CA  . GLU A 52  ? 3.12994 2.85365 3.49787 -0.31566 -1.20390 0.19357  52  GLU B CA  
397  C C   . GLU A 52  ? 3.15046 2.82128 3.44600 -0.30280 -1.25597 0.24834  52  GLU B C   
398  O O   . GLU A 52  ? 3.17050 2.74298 3.34736 -0.29907 -1.21927 0.25794  52  GLU B O   
399  C CB  . GLU A 52  ? 3.05539 2.86171 3.60991 -0.25735 -1.20603 0.18326  52  GLU B CB  
400  C CG  . GLU A 52  ? 3.01601 2.77188 3.58961 -0.19823 -1.16138 0.18825  52  GLU B CG  
401  C CD  . GLU A 52  ? 2.98341 2.75571 3.59918 -0.18402 -1.07674 0.14146  52  GLU B CD  
402  O OE1 . GLU A 52  ? 3.03613 2.76421 3.55055 -0.22091 -1.02039 0.11964  52  GLU B OE1 
403  O OE2 . GLU A 52  ? 2.91340 2.74532 3.66604 -0.13646 -1.06487 0.12709  52  GLU B OE2 
404  N N   . ASN A 53  ? 3.25332 2.99461 3.62402 -0.29485 -1.34208 0.28686  53  ASN B N   
405  C CA  . ASN A 53  ? 3.28896 2.99369 3.59192 -0.29115 -1.40256 0.34780  53  ASN B CA  
406  C C   . ASN A 53  ? 3.24503 2.94455 3.66343 -0.21657 -1.41891 0.38161  53  ASN B C   
407  O O   . ASN A 53  ? 3.20789 2.99271 3.78136 -0.18233 -1.46847 0.39786  53  ASN B O   
408  C CB  . ASN A 53  ? 3.31767 3.11035 3.62448 -0.33245 -1.48796 0.37557  53  ASN B CB  
409  C CG  . ASN A 53  ? 3.37822 3.12073 3.52267 -0.37569 -1.52308 0.41558  53  ASN B CG  
410  O OD1 . ASN A 53  ? 3.40121 3.03718 3.42928 -0.37447 -1.48413 0.42198  53  ASN B OD1 
411  N ND2 . ASN A 53  ? 3.38915 3.21935 3.52556 -0.41625 -1.59729 0.44115  53  ASN B ND2 
412  N N   . ASN A 54  ? 3.21238 2.81350 3.55991 -0.19177 -1.37457 0.38921  54  ASN B N   
413  C CA  . ASN A 54  ? 3.17790 2.76557 3.62927 -0.12676 -1.38444 0.41758  54  ASN B CA  
414  C C   . ASN A 54  ? 3.21337 2.79700 3.66184 -0.11942 -1.46880 0.49244  54  ASN B C   
415  O O   . ASN A 54  ? 3.19351 2.81880 3.78985 -0.07040 -1.51003 0.52323  54  ASN B O   
416  C CB  . ASN A 54  ? 3.17206 2.66645 3.55127 -0.10557 -1.30690 0.39724  54  ASN B CB  
417  C CG  . ASN A 54  ? 3.25096 2.64662 3.43509 -0.14090 -1.30242 0.42268  54  ASN B CG  
418  O OD1 . ASN A 54  ? 3.30259 2.67664 3.44076 -0.14989 -1.36334 0.47828  54  ASN B OD1 
419  N ND2 . ASN A 54  ? 3.25970 2.59845 3.33087 -0.15950 -1.22838 0.38334  54  ASN B ND2 
420  N N   . GLY A 55  ? 3.35082 2.88542 3.63482 -0.16709 -1.49297 0.52349  55  GLY B N   
421  C CA  . GLY A 55  ? 3.38521 2.92725 3.64846 -0.17011 -1.57593 0.59987  55  GLY B CA  
422  C C   . GLY A 55  ? 3.43714 3.02235 3.58326 -0.24218 -1.61896 0.60820  55  GLY B C   
423  O O   . GLY A 55  ? 3.44588 3.05096 3.54252 -0.28721 -1.58243 0.55121  55  GLY B O   
424  N N   . GLY A 56  ? 3.56911 3.17132 3.67329 -0.25443 -1.69478 0.68001  56  GLY B N   
425  C CA  . GLY A 56  ? 3.60382 3.26018 3.59495 -0.32558 -1.72419 0.68479  56  GLY B CA  
426  C C   . GLY A 56  ? 3.62979 3.22393 3.44975 -0.39139 -1.67660 0.63128  56  GLY B C   
427  O O   . GLY A 56  ? 3.63072 3.28167 3.41873 -0.44654 -1.67102 0.58653  56  GLY B O   
428  N N   . ALA A 57  ? 3.69471 3.17112 3.41129 -0.38409 -1.62321 0.62648  57  ALA B N   
429  C CA  . ALA A 57  ? 3.71349 3.12001 3.26460 -0.43951 -1.56170 0.57620  57  ALA B CA  
430  C C   . ALA A 57  ? 3.67952 3.00987 3.23600 -0.41013 -1.46394 0.51620  57  ALA B C   
431  O O   . ALA A 57  ? 3.68338 2.95531 3.11725 -0.44930 -1.40529 0.47166  57  ALA B O   
432  C CB  . ALA A 57  ? 3.74535 3.08720 3.14298 -0.46709 -1.58133 0.61939  57  ALA B CB  
433  N N   . GLY A 58  ? 3.54534 2.88061 3.24244 -0.34281 -1.44351 0.51355  58  GLY B N   
434  C CA  . GLY A 58  ? 3.50063 2.78143 3.20821 -0.31249 -1.35315 0.46169  58  GLY B CA  
435  C C   . GLY A 58  ? 3.46748 2.81208 3.28334 -0.30681 -1.31945 0.41028  58  GLY B C   
436  O O   . GLY A 58  ? 3.45515 2.89259 3.37345 -0.31278 -1.37001 0.41552  58  GLY B O   
437  N N   . CYS A 59  ? 3.47509 2.77695 3.27078 -0.29484 -1.23393 0.36233  59  CYS B N   
438  C CA  . CYS A 59  ? 3.45156 2.80506 3.32771 -0.29709 -1.19160 0.31323  59  CYS B CA  
439  C C   . CYS A 59  ? 3.39384 2.73922 3.34578 -0.24039 -1.12347 0.28776  59  CYS B C   
440  O O   . CYS A 59  ? 3.37488 2.66393 3.29009 -0.20770 -1.09711 0.29895  59  CYS B O   
441  C CB  . CYS A 59  ? 3.50257 2.81948 3.25473 -0.35925 -1.14855 0.27634  59  CYS B CB  
442  S SG  . CYS A 59  ? 3.55123 2.90941 3.23190 -0.43775 -1.22122 0.28804  59  CYS B SG  
443  N N   . VAL A 60  ? 3.22461 2.63643 3.28405 -0.23226 -1.09430 0.25117  60  VAL B N   
444  C CA  . VAL A 60  ? 3.15541 2.58915 3.30430 -0.18305 -1.03190 0.22323  60  VAL B CA  
445  C C   . VAL A 60  ? 3.16237 2.62421 3.32219 -0.20458 -0.97230 0.17986  60  VAL B C   
446  O O   . VAL A 60  ? 3.18990 2.69185 3.36703 -0.24615 -0.99530 0.16766  60  VAL B O   
447  C CB  . VAL A 60  ? 3.08924 2.60315 3.42027 -0.13352 -1.07224 0.23185  60  VAL B CB  
448  C CG1 . VAL A 60  ? 3.01845 2.59316 3.46545 -0.09817 -1.01051 0.18898  60  VAL B CG1 
449  C CG2 . VAL A 60  ? 3.07388 2.53826 3.39437 -0.09941 -1.09676 0.26901  60  VAL B CG2 
450  N N   . CYS A 61  ? 3.12792 2.57256 3.27702 -0.17722 -0.89362 0.15782  61  CYS B N   
451  C CA  . CYS A 61  ? 3.14472 2.60716 3.29704 -0.19114 -0.82601 0.12460  61  CYS B CA  
452  C C   . CYS A 61  ? 3.06163 2.58912 3.32157 -0.14067 -0.77524 0.10447  61  CYS B C   
453  O O   . CYS A 61  ? 2.99779 2.53426 3.29672 -0.09774 -0.77698 0.11117  61  CYS B O   
454  C CB  . CYS A 61  ? 3.21428 2.57533 3.19844 -0.21908 -0.76997 0.12349  61  CYS B CB  
455  S SG  . CYS A 61  ? 3.27098 2.62348 3.23268 -0.23419 -0.67534 0.09476  61  CYS B SG  
456  N N   . HIS A 62  ? 2.79933 2.37704 3.10856 -0.14980 -0.72747 0.07776  62  HIS B N   
457  C CA  . HIS A 62  ? 2.71902 2.37540 3.12743 -0.10945 -0.67369 0.05570  62  HIS B CA  
458  C C   . HIS A 62  ? 2.77841 2.42110 3.12826 -0.12476 -0.59363 0.04490  62  HIS B C   
459  O O   . HIS A 62  ? 2.81671 2.49518 3.20909 -0.15624 -0.58570 0.02960  62  HIS B O   
460  C CB  . HIS A 62  ? 2.63949 2.41380 3.22910 -0.09832 -0.71193 0.03467  62  HIS B CB  
461  C CG  . HIS A 62  ? 2.61536 2.40000 3.26941 -0.08800 -0.79696 0.05209  62  HIS B CG  
462  N ND1 . HIS A 62  ? 2.54954 2.35910 3.28618 -0.04102 -0.81194 0.05471  62  HIS B ND1 
463  C CD2 . HIS A 62  ? 2.65923 2.43587 3.30926 -0.11849 -0.87008 0.07028  62  HIS B CD2 
464  C CE1 . HIS A 62  ? 2.55663 2.36457 3.33914 -0.03945 -0.89071 0.07925  62  HIS B CE1 
465  N NE2 . HIS A 62  ? 2.62902 2.42370 3.35874 -0.08535 -0.92932 0.09075  62  HIS B NE2 
466  N N   . LEU A 63  ? 2.74278 2.33633 2.99831 -0.10168 -0.53339 0.05454  63  LEU B N   
467  C CA  . LEU A 63  ? 2.80043 2.38557 3.00797 -0.10444 -0.45218 0.05290  63  LEU B CA  
468  C C   . LEU A 63  ? 2.72038 2.43076 3.05549 -0.07626 -0.41333 0.03351  63  LEU B C   
469  O O   . LEU A 63  ? 2.60249 2.39286 3.03574 -0.04262 -0.43019 0.01938  63  LEU B O   
470  C CB  . LEU A 63  ? 2.83214 2.33488 2.90109 -0.08389 -0.40238 0.07225  63  LEU B CB  
471  C CG  . LEU A 63  ? 2.85564 2.25728 2.81062 -0.09502 -0.44376 0.08821  63  LEU B CG  
472  C CD1 . LEU A 63  ? 2.86089 2.19456 2.68696 -0.07294 -0.38635 0.10202  63  LEU B CD1 
473  C CD2 . LEU A 63  ? 2.93916 2.27461 2.83992 -0.15213 -0.47952 0.08935  63  LEU B CD2 
474  N N   . LEU A 64  ? 2.69796 2.42584 3.03248 -0.09249 -0.35769 0.03192  64  LEU B N   
475  C CA  . LEU A 64  ? 2.63036 2.48509 3.08127 -0.07543 -0.31819 0.01451  64  LEU B CA  
476  C C   . LEU A 64  ? 2.67186 2.52432 3.05124 -0.05127 -0.23097 0.03500  64  LEU B C   
477  O O   . LEU A 64  ? 2.80694 2.59660 3.11382 -0.07336 -0.18598 0.05389  64  LEU B O   
478  C CB  . LEU A 64  ? 2.66882 2.56663 3.19892 -0.11819 -0.33144 -0.00305 64  LEU B CB  
479  C CG  . LEU A 64  ? 2.61252 2.54844 3.23996 -0.13789 -0.41717 -0.02473 64  LEU B CG  
480  C CD1 . LEU A 64  ? 2.57973 2.61973 3.33092 -0.16349 -0.41603 -0.05283 64  LEU B CD1 
481  C CD2 . LEU A 64  ? 2.48605 2.46981 3.18776 -0.09541 -0.46219 -0.03226 64  LEU B CD2 
482  N N   . MET A 65  ? 2.73118 2.65644 3.13527 -0.00599 -0.20529 0.03128  65  MET B N   
483  C CA  . MET A 65  ? 2.73819 2.68606 3.08016 0.02417  -0.12574 0.05299  65  MET B CA  
484  C C   . MET A 65  ? 2.65462 2.75918 3.11544 0.03457  -0.08684 0.03732  65  MET B C   
485  O O   . MET A 65  ? 2.50657 2.72675 3.06640 0.05759  -0.09582 0.00726  65  MET B O   
486  C CB  . MET A 65  ? 2.65936 2.59803 2.94230 0.06343  -0.11977 0.05593  65  MET B CB  
487  C CG  . MET A 65  ? 2.68400 2.50422 2.89226 0.05313  -0.17859 0.05896  65  MET B CG  
488  S SD  . MET A 65  ? 2.86856 2.52628 2.95207 0.00624  -0.19281 0.08318  65  MET B SD  
489  C CE  . MET A 65  ? 2.84046 2.39157 2.80277 0.01461  -0.22712 0.09276  65  MET B CE  
490  N N   . ASP A 66  ? 2.60945 2.71904 3.06077 0.01572  -0.03949 0.05671  66  ASP B N   
491  C CA  . ASP A 66  ? 2.52672 2.78892 3.08984 0.01744  -0.00408 0.04354  66  ASP B CA  
492  C C   . ASP A 66  ? 2.36369 2.74975 2.94574 0.06310  0.04142  0.04206  66  ASP B C   
493  O O   . ASP A 66  ? 2.19862 2.73154 2.90441 0.07112  0.03636  0.00398  66  ASP B O   
494  C CB  . ASP A 66  ? 2.70087 2.92842 3.23108 -0.01155 0.04559  0.07396  66  ASP B CB  
495  C CG  . ASP A 66  ? 2.80310 2.97632 3.21345 0.01469  0.12023  0.12740  66  ASP B CG  
496  O OD1 . ASP A 66  ? 2.68876 2.95417 3.09413 0.05705  0.16049  0.14000  66  ASP B OD1 
497  O OD2 . ASP A 66  ? 2.97508 3.01404 3.29784 -0.00792 0.14030  0.15603  66  ASP B OD2 
498  N N   . ASP A 67  ? 2.56964 2.90578 3.03337 0.09231  0.08694  0.07922  67  ASP B N   
499  C CA  . ASP A 67  ? 2.41513 2.86849 2.88179 0.13520  0.12809  0.07692  67  ASP B CA  
500  C C   . ASP A 67  ? 2.46490 2.80916 2.79027 0.16165  0.14065  0.10528  67  ASP B C   
501  O O   . ASP A 67  ? 2.59860 2.82875 2.81645 0.15953  0.16879  0.14896  67  ASP B O   
502  C CB  . ASP A 67  ? 2.35907 2.94233 2.85187 0.14588  0.19957  0.10181  67  ASP B CB  
503  C CG  . ASP A 67  ? 2.16696 2.92701 2.70943 0.18010  0.23217  0.08028  67  ASP B CG  
504  O OD1 . ASP A 67  ? 2.08947 2.87177 2.66489 0.19144  0.19862  0.03758  67  ASP B OD1 
505  O OD2 . ASP A 67  ? 2.09155 2.97130 2.64058 0.19385  0.29301  0.10626  67  ASP B OD2 
506  N N   . VAL A 68  ? 2.26004 2.63854 2.58958 0.18481  0.12254  0.07761  68  VAL B N   
507  C CA  . VAL A 68  ? 2.29492 2.56817 2.49736 0.20441  0.12248  0.09434  68  VAL B CA  
508  C C   . VAL A 68  ? 2.17657 2.57465 2.37363 0.24454  0.16665  0.08431  68  VAL B C   
509  O O   . VAL A 68  ? 2.05527 2.59642 2.36264 0.25030  0.16633  0.04195  68  VAL B O   
510  C CB  . VAL A 68  ? 2.32230 2.48367 2.51844 0.18402  0.04620  0.07057  68  VAL B CB  
511  C CG1 . VAL A 68  ? 2.20897 2.47420 2.54165 0.18559  0.00901  0.02003  68  VAL B CG1 
512  C CG2 . VAL A 68  ? 2.34270 2.39969 2.40425 0.20002  0.04722  0.08606  68  VAL B CG2 
513  N N   . VAL A 69  ? 2.36957 2.72023 2.44154 0.27116  0.20753  0.12009  69  VAL B N   
514  C CA  . VAL A 69  ? 2.26748 2.73825 2.31734 0.30940  0.25306  0.11376  69  VAL B CA  
515  C C   . VAL A 69  ? 2.27293 2.63783 2.21286 0.32074  0.23693  0.11092  69  VAL B C   
516  O O   . VAL A 69  ? 2.35178 2.56129 2.24395 0.29715  0.18653  0.11108  69  VAL B O   
517  C CB  . VAL A 69  ? 2.19770 2.74998 2.20625 0.33825  0.32746  0.16405  69  VAL B CB  
518  C CG1 . VAL A 69  ? 2.15394 2.82376 2.27257 0.32355  0.34526  0.16655  69  VAL B CG1 
519  C CG2 . VAL A 69  ? 2.29469 2.67979 2.17433 0.34362  0.34455  0.22028  69  VAL B CG2 
520  N N   . SER A 70  ? 2.38447 2.84200 2.28162 0.35464  0.28060  0.10787  70  SER B N   
521  C CA  . SER A 70  ? 2.37511 2.75657 2.17613 0.36428  0.26903  0.09697  70  SER B CA  
522  C C   . SER A 70  ? 2.43906 2.66100 2.09629 0.36998  0.27729  0.14348  70  SER B C   
523  O O   . SER A 70  ? 2.44519 2.58170 2.01572 0.37046  0.26031  0.13445  70  SER B O   
524  C CB  . SER A 70  ? 2.23360 2.77868 2.03502 0.39646  0.31795  0.07477  70  SER B CB  
525  O OG  . SER A 70  ? 2.24588 2.71908 1.94565 0.40500  0.31270  0.06556  70  SER B OG  
526  N N   . ALA A 71  ? 2.44272 2.62197 2.07473 0.37253  0.30571  0.19042  71  ALA B N   
527  C CA  . ALA A 71  ? 2.49380 2.52809 1.99850 0.38029  0.32485  0.23223  71  ALA B CA  
528  C C   . ALA A 71  ? 2.62101 2.50483 2.12243 0.33967  0.29346  0.24613  71  ALA B C   
529  O O   . ALA A 71  ? 2.66336 2.46374 2.10697 0.34354  0.32908  0.28727  71  ALA B O   
530  C CB  . ALA A 71  ? 2.40987 2.52277 1.87356 0.42663  0.40155  0.28126  71  ALA B CB  
531  N N   . ASP A 72  ? 2.43593 2.28588 2.00262 0.29993  0.22800  0.21092  72  ASP B N   
532  C CA  . ASP A 72  ? 2.54704 2.26830 2.11413 0.25529  0.19018  0.21521  72  ASP B CA  
533  C C   . ASP A 72  ? 2.59047 2.17325 2.07671 0.22875  0.13601  0.19944  72  ASP B C   
534  O O   . ASP A 72  ? 2.54459 2.14632 2.02380 0.23452  0.10543  0.17444  72  ASP B O   
535  C CB  . ASP A 72  ? 2.56016 2.35574 2.26504 0.22844  0.15423  0.19107  72  ASP B CB  
536  C CG  . ASP A 72  ? 2.54721 2.45371 2.32078 0.24123  0.20799  0.21249  72  ASP B CG  
537  O OD1 . ASP A 72  ? 2.53354 2.43413 2.24279 0.26758  0.27050  0.25492  72  ASP B OD1 
538  O OD2 . ASP A 72  ? 2.53605 2.53607 2.42922 0.22501  0.18829  0.18905  72  ASP B OD2 
539  N N   . ASN A 73  ? 2.81975 2.26610 2.24659 0.19602  0.12674  0.21322  73  ASN B N   
540  C CA  . ASN A 73  ? 2.85706 2.16730 2.18037 0.17020  0.09081  0.20571  73  ASN B CA  
541  C C   . ASN A 73  ? 2.94416 2.15060 2.26585 0.11773  0.06397  0.20526  73  ASN B C   
542  O O   . ASN A 73  ? 2.98867 2.15407 2.29668 0.11333  0.11201  0.22619  73  ASN B O   
543  C CB  . ASN A 73  ? 2.83507 2.09497 2.03817 0.20174  0.14659  0.22679  73  ASN B CB  
544  C CG  . ASN A 73  ? 2.86299 1.99409 1.95292 0.17564  0.11542  0.21518  73  ASN B CG  
545  O OD1 . ASN A 73  ? 2.91652 1.98010 2.00485 0.12871  0.05386  0.19748  73  ASN B OD1 
546  N ND2 . ASN A 73  ? 2.82522 1.93061 1.81821 0.20700  0.16072  0.22667  73  ASN B ND2 
547  N N   . TYR A 74  ? 2.72838 1.89610 2.06577 0.07743  -0.00997 0.18265  74  TYR B N   
548  C CA  . TYR A 74  ? 2.80125 1.90109 2.15459 0.02319  -0.04264 0.17560  74  TYR B CA  
549  C C   . TYR A 74  ? 2.81459 1.78465 2.05211 -0.01507 -0.06875 0.16942  74  TYR B C   
550  O O   . TYR A 74  ? 2.76446 1.71171 1.93951 -0.00943 -0.09757 0.16439  74  TYR B O   
551  C CB  . TYR A 74  ? 2.82017 1.99412 2.29400 0.00317  -0.11026 0.15573  74  TYR B CB  
552  C CG  . TYR A 74  ? 2.81832 2.11627 2.41649 0.02494  -0.08378 0.15470  74  TYR B CG  
553  C CD1 . TYR A 74  ? 2.73112 2.14466 2.39181 0.06868  -0.07185 0.14856  74  TYR B CD1 
554  C CD2 . TYR A 74  ? 2.88668 2.19153 2.53987 -0.00247 -0.06774 0.15604  74  TYR B CD2 
555  C CE1 . TYR A 74  ? 2.71475 2.25338 2.48961 0.08456  -0.04625 0.14351  74  TYR B CE1 
556  C CE2 . TYR A 74  ? 2.89520 2.31986 2.66019 0.01392  -0.04290 0.15445  74  TYR B CE2 
557  C CZ  . TYR A 74  ? 2.80576 2.34989 2.63109 0.05751  -0.03294 0.14812  74  TYR B CZ  
558  O OH  . TYR A 74  ? 2.77127 2.44601 2.70844 0.06999  -0.00713 0.14249  74  TYR B OH  
559  N N   . THR A 75  ? 3.11619 2.00508 2.32640 -0.05789 -0.05581 0.16690  75  THR B N   
560  C CA  . THR A 75  ? 3.12789 1.90420 2.23969 -0.10677 -0.08153 0.15285  75  THR B CA  
561  C C   . THR A 75  ? 3.16845 1.96079 2.33551 -0.15989 -0.16124 0.13376  75  THR B C   
562  O O   . THR A 75  ? 3.23571 2.04524 2.47132 -0.18952 -0.16092 0.12564  75  THR B O   
563  C CB  . THR A 75  ? 3.14790 1.82631 2.19860 -0.12507 -0.01333 0.15544  75  THR B CB  
564  O OG1 . THR A 75  ? 3.11922 1.77993 2.10984 -0.07153 0.05582  0.17753  75  THR B OG1 
565  C CG2 . THR A 75  ? 3.16042 1.73605 2.12482 -0.18788 -0.04216 0.12995  75  THR B CG2 
566  N N   . LEU A 76  ? 3.10712 1.89809 2.24500 -0.17194 -0.22877 0.12876  76  LEU B N   
567  C CA  . LEU A 76  ? 3.14091 1.96016 2.33237 -0.21484 -0.31130 0.11862  76  LEU B CA  
568  C C   . LEU A 76  ? 3.20319 1.93490 2.29444 -0.27772 -0.33496 0.10454  76  LEU B C   
569  O O   . LEU A 76  ? 3.19947 1.87701 2.18808 -0.28300 -0.34568 0.10623  76  LEU B O   
570  C CB  . LEU A 76  ? 3.09222 1.97209 2.32745 -0.18706 -0.37164 0.12806  76  LEU B CB  
571  C CG  . LEU A 76  ? 3.09155 2.08421 2.47447 -0.15078 -0.38390 0.12882  76  LEU B CG  
572  C CD1 . LEU A 76  ? 3.09462 2.13049 2.51941 -0.11488 -0.30476 0.12947  76  LEU B CD1 
573  C CD2 . LEU A 76  ? 3.02451 2.05474 2.43103 -0.11605 -0.42014 0.13622  76  LEU B CD2 
574  N N   . ASP A 77  ? 3.54199 2.26732 2.66364 -0.32913 -0.34137 0.08678  77  ASP B N   
575  C CA  . ASP A 77  ? 3.54449 2.20091 2.58139 -0.39793 -0.35745 0.06453  77  ASP B CA  
576  C C   . ASP A 77  ? 3.58680 2.30910 2.68671 -0.44394 -0.44225 0.05646  77  ASP B C   
577  O O   . ASP A 77  ? 3.63537 2.40971 2.82928 -0.46012 -0.44447 0.04545  77  ASP B O   
578  C CB  . ASP A 77  ? 3.57422 2.15955 2.58418 -0.42490 -0.27783 0.04464  77  ASP B CB  
579  C CG  . ASP A 77  ? 3.54534 2.06627 2.49381 -0.37567 -0.19316 0.05850  77  ASP B CG  
580  O OD1 . ASP A 77  ? 3.48492 1.97933 2.35390 -0.35080 -0.19740 0.06735  77  ASP B OD1 
581  O OD2 . ASP A 77  ? 3.57815 2.07763 2.55788 -0.36206 -0.12178 0.06245  77  ASP B OD2 
582  N N   . LEU A 78  ? 3.63391 2.35984 2.68288 -0.46489 -0.51177 0.06403  78  LEU B N   
583  C CA  . LEU A 78  ? 3.66791 2.46114 2.76630 -0.50823 -0.59677 0.06289  78  LEU B CA  
584  C C   . LEU A 78  ? 3.68111 2.43488 2.70031 -0.58975 -0.59792 0.03038  78  LEU B C   
585  O O   . LEU A 78  ? 3.63738 2.32810 2.53790 -0.61649 -0.59379 0.02374  78  LEU B O   
586  C CB  . LEU A 78  ? 3.63439 2.46043 2.72675 -0.48747 -0.67344 0.09569  78  LEU B CB  
587  C CG  . LEU A 78  ? 3.67763 2.58429 2.83001 -0.52329 -0.76604 0.10526  78  LEU B CG  
588  C CD1 . LEU A 78  ? 3.71023 2.70413 3.01365 -0.50856 -0.77549 0.09857  78  LEU B CD1 
589  C CD2 . LEU A 78  ? 3.64342 2.57039 2.78813 -0.49890 -0.83649 0.14621  78  LEU B CD2 
590  N N   . TRP A 79  ? 3.87290 2.66978 2.95903 -0.63250 -0.60159 0.00553  79  TRP B N   
591  C CA  . TRP A 79  ? 3.87542 2.64961 2.90208 -0.71675 -0.59825 -0.03453 79  TRP B CA  
592  C C   . TRP A 79  ? 3.89280 2.75726 2.93369 -0.76469 -0.69642 -0.03174 79  TRP B C   
593  O O   . TRP A 79  ? 3.90933 2.86177 3.03892 -0.73321 -0.76455 -0.00048 79  TRP B O   
594  C CB  . TRP A 79  ? 3.90386 2.66962 2.98911 -0.74427 -0.53516 -0.06901 79  TRP B CB  
595  C CG  . TRP A 79  ? 3.89335 2.55313 2.93543 -0.72025 -0.43068 -0.07645 79  TRP B CG  
596  C CD1 . TRP A 79  ? 3.90474 2.55261 2.99303 -0.64885 -0.37872 -0.04972 79  TRP B CD1 
597  C CD2 . TRP A 79  ? 3.85748 2.41300 2.80455 -0.76727 -0.36366 -0.11200 79  TRP B CD2 
598  N NE1 . TRP A 79  ? 3.88095 2.42424 2.90795 -0.64455 -0.28549 -0.05937 79  TRP B NE1 
599  C CE2 . TRP A 79  ? 3.85278 2.33155 2.79567 -0.71541 -0.27310 -0.09863 79  TRP B CE2 
600  C CE3 . TRP A 79  ? 3.90396 2.42930 2.77252 -0.84912 -0.36987 -0.15544 79  TRP B CE3 
601  C CZ2 . TRP A 79  ? 3.87640 2.23987 2.74445 -0.73780 -0.18855 -0.12387 79  TRP B CZ2 
602  C CZ3 . TRP A 79  ? 3.93574 2.34727 2.73052 -0.87620 -0.28369 -0.18858 79  TRP B CZ3 
603  C CH2 . TRP A 79  ? 3.93289 2.25958 2.73019 -0.81831 -0.19379 -0.17110 79  TRP B CH2 
604  N N   . ALA A 80  ? 3.79298 2.63892 2.74743 -0.84244 -0.70055 -0.06586 80  ALA B N   
605  C CA  . ALA A 80  ? 3.80911 2.75283 2.77339 -0.90590 -0.78180 -0.07401 80  ALA B CA  
606  C C   . ALA A 80  ? 3.85107 2.78215 2.79811 -0.98832 -0.73297 -0.13823 80  ALA B C   
607  O O   . ALA A 80  ? 3.89536 2.76971 2.73604 -1.04599 -0.70323 -0.17397 80  ALA B O   
608  C CB  . ALA A 80  ? 3.82006 2.76910 2.68249 -0.92577 -0.84230 -0.05086 80  ALA B CB  
609  N N   . GLY A 81  ? 3.78115 2.76622 2.83579 -0.99606 -0.72162 -0.15658 81  GLY B N   
610  C CA  . GLY A 81  ? 3.82728 2.80167 2.88098 -1.07435 -0.66946 -0.21975 81  GLY B CA  
611  C C   . GLY A 81  ? 3.86107 2.68958 2.84046 -1.08174 -0.55973 -0.25040 81  GLY B C   
612  O O   . GLY A 81  ? 3.86661 2.64056 2.89746 -1.05118 -0.48656 -0.25315 81  GLY B O   
613  N N   . GLN A 82  ? 3.96863 2.73657 2.82826 -1.12252 -0.54693 -0.27233 82  GLN B N   
614  C CA  . GLN A 82  ? 4.02080 2.64487 2.80522 -1.11742 -0.44650 -0.29469 82  GLN B CA  
615  C C   . GLN A 82  ? 4.02263 2.59429 2.69505 -1.09383 -0.45942 -0.27367 82  GLN B C   
616  O O   . GLN A 82  ? 4.07988 2.54358 2.67216 -1.10675 -0.38642 -0.30221 82  GLN B O   
617  C CB  . GLN A 82  ? 4.15396 2.73443 2.90883 -1.21202 -0.38314 -0.37036 82  GLN B CB  
618  C CG  . GLN A 82  ? 4.17857 2.78879 3.03728 -1.23922 -0.34956 -0.39741 82  GLN B CG  
619  C CD  . GLN A 82  ? 4.30457 2.81872 3.13591 -1.31086 -0.24977 -0.46664 82  GLN B CD  
620  O OE1 . GLN A 82  ? 4.38094 2.79479 3.12170 -1.32955 -0.19702 -0.49252 82  GLN B OE1 
621  N NE2 . GLN A 82  ? 4.32945 2.87238 3.24288 -1.35224 -0.22015 -0.49934 82  GLN B NE2 
622  N N   . GLN A 83  ? 4.16516 2.80908 2.83278 -1.06028 -0.54801 -0.22519 83  GLN B N   
623  C CA  . GLN A 83  ? 4.15989 2.76013 2.72735 -1.03251 -0.56363 -0.19902 83  GLN B CA  
624  C C   . GLN A 83  ? 4.04094 2.62504 2.65254 -0.92939 -0.56188 -0.14093 83  GLN B C   
625  O O   . GLN A 83  ? 3.98582 2.65365 2.68009 -0.89102 -0.62683 -0.10026 83  GLN B O   
626  C CB  . GLN A 83  ? 4.19974 2.89134 2.71913 -1.07797 -0.66298 -0.18587 83  GLN B CB  
627  C CG  . GLN A 83  ? 4.32172 3.06924 2.80937 -1.18479 -0.67920 -0.24249 83  GLN B CG  
628  C CD  . GLN A 83  ? 4.36100 3.20456 2.78904 -1.22601 -0.77678 -0.22068 83  GLN B CD  
629  O OE1 . GLN A 83  ? 4.42872 3.24017 2.74199 -1.26418 -0.77266 -0.23733 83  GLN B OE1 
630  N NE2 . GLN A 83  ? 4.31931 3.28514 2.82728 -1.21736 -0.86477 -0.18099 83  GLN B NE2 
631  N N   . LEU A 84  ? 4.16406 2.64669 2.72471 -0.88521 -0.48603 -0.13947 84  LEU B N   
632  C CA  . LEU A 84  ? 4.07404 2.54830 2.65935 -0.79291 -0.48161 -0.08983 84  LEU B CA  
633  C C   . LEU A 84  ? 4.05328 2.56428 2.58625 -0.78056 -0.55895 -0.05537 84  LEU B C   
634  O O   . LEU A 84  ? 4.10350 2.58256 2.52655 -0.82154 -0.56832 -0.07037 84  LEU B O   
635  C CB  . LEU A 84  ? 4.06835 2.43523 2.60156 -0.75300 -0.38283 -0.09720 84  LEU B CB  
636  C CG  . LEU A 84  ? 4.03324 2.38722 2.65266 -0.68753 -0.31850 -0.07802 84  LEU B CG  
637  C CD1 . LEU A 84  ? 4.00381 2.27666 2.56132 -0.62988 -0.24385 -0.06590 84  LEU B CD1 
638  C CD2 . LEU A 84  ? 3.98476 2.43769 2.71090 -0.63710 -0.37527 -0.03828 84  LEU B CD2 
639  N N   . LEU A 85  ? 3.93511 2.51370 2.54964 -0.72649 -0.61244 -0.01038 85  LEU B N   
640  C CA  . LEU A 85  ? 3.91656 2.52514 2.49505 -0.70944 -0.68316 0.02869  85  LEU B CA  
641  C C   . LEU A 85  ? 3.86866 2.43759 2.43170 -0.63326 -0.65149 0.05616  85  LEU B C   
642  O O   . LEU A 85  ? 3.87379 2.42934 2.36227 -0.62895 -0.68258 0.07635  85  LEU B O   
643  C CB  . LEU A 85  ? 3.90862 2.62336 2.59136 -0.70519 -0.77253 0.06134  85  LEU B CB  
644  C CG  . LEU A 85  ? 3.95321 2.73732 2.68125 -0.77164 -0.80896 0.03689  85  LEU B CG  
645  C CD1 . LEU A 85  ? 3.94777 2.84002 2.78996 -0.75011 -0.89533 0.07623  85  LEU B CD1 
646  C CD2 . LEU A 85  ? 3.99492 2.77150 2.60534 -0.85529 -0.82907 0.01041  85  LEU B CD2 
647  N N   . TRP A 86  ? 3.80765 2.36473 2.43749 -0.57620 -0.58968 0.05698  86  TRP B N   
648  C CA  . TRP A 86  ? 3.74126 2.28272 2.36680 -0.50410 -0.56001 0.08051  86  TRP B CA  
649  C C   . TRP A 86  ? 3.71942 2.24638 2.39921 -0.45691 -0.47645 0.07310  86  TRP B C   
650  O O   . TRP A 86  ? 3.77004 2.33113 2.54068 -0.46252 -0.46585 0.06538  86  TRP B O   
651  C CB  . TRP A 86  ? 3.70237 2.31618 2.40782 -0.46654 -0.62907 0.11847  86  TRP B CB  
652  C CG  . TRP A 86  ? 3.65887 2.27128 2.37705 -0.39598 -0.59574 0.13543  86  TRP B CG  
653  C CD1 . TRP A 86  ? 3.61429 2.19100 2.24406 -0.37990 -0.59325 0.14569  86  TRP B CD1 
654  C CD2 . TRP A 86  ? 3.65904 2.31885 2.48574 -0.33610 -0.55924 0.14033  86  TRP B CD2 
655  N NE1 . TRP A 86  ? 3.55768 2.15776 2.23488 -0.31397 -0.55599 0.15440  86  TRP B NE1 
656  C CE2 . TRP A 86  ? 3.58826 2.24256 2.38639 -0.28627 -0.53487 0.15137  86  TRP B CE2 
657  C CE3 . TRP A 86  ? 3.70866 2.42224 2.65314 -0.32329 -0.54341 0.13390  86  TRP B CE3 
658  C CZ2 . TRP A 86  ? 3.56443 2.27173 2.44842 -0.22550 -0.49538 0.15452  86  TRP B CZ2 
659  C CZ3 . TRP A 86  ? 3.68719 2.45056 2.71545 -0.26242 -0.50533 0.13965  86  TRP B CZ3 
660  C CH2 . TRP A 86  ? 3.61304 2.37615 2.61116 -0.21461 -0.48161 0.14912  86  TRP B CH2 
661  N N   . LYS A 87  ? 3.75480 2.23817 2.37770 -0.41125 -0.41795 0.07731  87  LYS B N   
662  C CA  . LYS A 87  ? 3.75316 2.22920 2.41553 -0.35949 -0.33642 0.07921  87  LYS B CA  
663  C C   . LYS A 87  ? 3.69637 2.20104 2.35620 -0.29169 -0.32100 0.10077  87  LYS B C   
664  O O   . LYS A 87  ? 3.63990 2.11784 2.21244 -0.29114 -0.33606 0.10271  87  LYS B O   
665  C CB  . LYS A 87  ? 3.75411 2.13757 2.33527 -0.37990 -0.26007 0.05549  87  LYS B CB  
666  C CG  . LYS A 87  ? 3.76458 2.13607 2.38026 -0.32446 -0.17202 0.06639  87  LYS B CG  
667  C CD  . LYS A 87  ? 3.77342 2.04462 2.32388 -0.35002 -0.09872 0.04404  87  LYS B CD  
668  C CE  . LYS A 87  ? 3.80290 2.06649 2.41297 -0.30597 -0.01698 0.06146  87  LYS B CE  
669  N NZ  . LYS A 87  ? 3.85035 2.16659 2.57267 -0.32456 -0.03170 0.06316  87  LYS B NZ  
670  N N   . GLY A 88  ? 3.49094 2.05711 2.24576 -0.23888 -0.29028 0.11395  88  GLY B N   
671  C CA  . GLY A 88  ? 3.43299 2.04491 2.19710 -0.17841 -0.27448 0.12839  88  GLY B CA  
672  C C   . GLY A 88  ? 3.43666 2.11406 2.28774 -0.12451 -0.21697 0.13775  88  GLY B C   
673  O O   . GLY A 88  ? 3.47959 2.14538 2.35991 -0.12843 -0.17202 0.13743  88  GLY B O   
674  N N   . SER A 89  ? 3.23657 1.98704 2.12904 -0.07658 -0.21664 0.14541  89  SER B N   
675  C CA  . SER A 89  ? 3.23603 2.07179 2.20831 -0.02403 -0.16341 0.15301  89  SER B CA  
676  C C   . SER A 89  ? 3.20693 2.14369 2.29668 -0.00496 -0.20582 0.14979  89  SER B C   
677  O O   . SER A 89  ? 3.17881 2.11043 2.27401 -0.02094 -0.26865 0.14678  89  SER B O   
678  C CB  . SER A 89  ? 3.18696 2.02522 2.08366 0.02266  -0.09723 0.15924  89  SER B CB  
679  O OG  . SER A 89  ? 3.14038 2.00007 2.00391 0.03670  -0.12270 0.15240  89  SER B OG  
680  N N   . PHE A 90  ? 2.92292 1.95373 2.11024 0.02933  -0.16856 0.15115  90  PHE B N   
681  C CA  . PHE A 90  ? 2.89140 2.02834 2.20001 0.05097  -0.19623 0.14087  90  PHE B CA  
682  C C   . PHE A 90  ? 2.86319 2.10771 2.22744 0.09883  -0.12955 0.14040  90  PHE B C   
683  O O   . PHE A 90  ? 2.89708 2.16207 2.28279 0.10418  -0.08434 0.15154  90  PHE B O   
684  C CB  . PHE A 90  ? 2.93293 2.09601 2.35185 0.02061  -0.25221 0.13500  90  PHE B CB  
685  C CG  . PHE A 90  ? 2.88951 2.16323 2.44740 0.04464  -0.27588 0.12072  90  PHE B CG  
686  C CD1 . PHE A 90  ? 2.81038 2.10251 2.37559 0.06421  -0.29725 0.11332  90  PHE B CD1 
687  C CD2 . PHE A 90  ? 2.89661 2.25560 2.58084 0.04563  -0.27303 0.11133  90  PHE B CD2 
688  C CE1 . PHE A 90  ? 2.77040 2.15982 2.47138 0.08535  -0.31340 0.09495  90  PHE B CE1 
689  C CE2 . PHE A 90  ? 2.82516 2.28888 2.64397 0.06691  -0.29172 0.09205  90  PHE B CE2 
690  C CZ  . PHE A 90  ? 2.76113 2.23808 2.59081 0.08737  -0.31083 0.08290  90  PHE B CZ  
691  N N   . LYS A 91  ? 2.81220 2.12929 2.20006 0.13069  -0.12227 0.12746  91  LYS B N   
692  C CA  . LYS A 91  ? 2.75714 2.20557 2.21141 0.17295  -0.06562 0.12042  91  LYS B CA  
693  C C   . LYS A 91  ? 2.70140 2.25098 2.30369 0.17550  -0.09895 0.09408  91  LYS B C   
694  O O   . LYS A 91  ? 2.66928 2.22810 2.29162 0.17892  -0.12858 0.07543  91  LYS B O   
695  C CB  . LYS A 91  ? 2.71083 2.18118 2.08030 0.20588  -0.02214 0.11749  91  LYS B CB  
696  C CG  . LYS A 91  ? 2.65681 2.28239 2.09055 0.24766  0.03657  0.10779  91  LYS B CG  
697  C CD  . LYS A 91  ? 2.62440 2.26451 1.94981 0.28130  0.09692  0.11956  91  LYS B CD  
698  C CE  . LYS A 91  ? 2.57655 2.34279 1.93888 0.31838  0.16568  0.13652  91  LYS B CE  
699  N NZ  . LYS A 91  ? 2.52846 2.32469 1.79143 0.35670  0.22413  0.15145  91  LYS B NZ  
700  N N   . PRO A 92  ? 2.54201 2.16731 2.25436 0.17285  -0.09354 0.09011  92  PRO B N   
701  C CA  . PRO A 92  ? 2.49216 2.21032 2.35509 0.17293  -0.12841 0.06051  92  PRO B CA  
702  C C   . PRO A 92  ? 2.41018 2.24362 2.32862 0.20519  -0.09757 0.03064  92  PRO B C   
703  O O   . PRO A 92  ? 2.37004 2.25928 2.40530 0.20512  -0.12898 0.00104  92  PRO B O   
704  C CB  . PRO A 92  ? 2.50980 2.29479 2.45978 0.16468  -0.11113 0.06269  92  PRO B CB  
705  C CG  . PRO A 92  ? 2.60866 2.27592 2.45477 0.14003  -0.10586 0.09422  92  PRO B CG  
706  C CD  . PRO A 92  ? 2.60271 2.21303 2.30997 0.16125  -0.06426 0.11174  92  PRO B CD  
707  N N   . SER A 93  ? 2.57927 2.45408 2.42206 0.23237  -0.03563 0.03529  93  SER B N   
708  C CA  . SER A 93  ? 2.50464 2.52135 2.40918 0.26005  0.00527  0.00177  93  SER B CA  
709  C C   . SER A 93  ? 2.48669 2.47418 2.36031 0.26305  -0.01080 -0.02195 93  SER B C   
710  O O   . SER A 93  ? 2.42105 2.52058 2.37862 0.27598  0.00976  -0.06232 93  SER B O   
711  C CB  . SER A 93  ? 2.46746 2.56890 2.31314 0.28962  0.08200  0.01909  93  SER B CB  
712  O OG  . SER A 93  ? 2.49395 2.49400 2.18696 0.29734  0.09808  0.04775  93  SER B OG  
713  N N   . GLU A 94  ? 2.72427 2.56882 2.48164 0.24821  -0.04362 -0.00104 94  GLU B N   
714  C CA  . GLU A 94  ? 2.67684 2.48669 2.40231 0.24676  -0.05974 -0.02056 94  GLU B CA  
715  C C   . GLU A 94  ? 2.69128 2.44286 2.49910 0.22519  -0.13062 -0.02791 94  GLU B C   
716  O O   . GLU A 94  ? 2.65109 2.40218 2.48144 0.22661  -0.13895 -0.05059 94  GLU B O   
717  C CB  . GLU A 94  ? 2.67674 2.37230 2.23024 0.24127  -0.05586 0.00411  94  GLU B CB  
718  C CG  . GLU A 94  ? 2.67850 2.42748 2.14335 0.26934  0.01565  0.01292  94  GLU B CG  
719  C CD  . GLU A 94  ? 2.67117 2.32982 1.98309 0.26712  0.02254  0.02183  94  GLU B CD  
720  O OE1 . GLU A 94  ? 2.69102 2.23371 1.95532 0.23808  -0.03066 0.02666  94  GLU B OE1 
721  O OE2 . GLU A 94  ? 2.62294 2.33347 1.86340 0.29454  0.08089  0.02502  94  GLU B OE2 
722  N N   . HIS A 95  ? 2.70836 2.41329 2.56337 0.20558  -0.18004 -0.00824 95  HIS B N   
723  C CA  . HIS A 95  ? 2.71046 2.35763 2.63747 0.18726  -0.25326 -0.00458 95  HIS B CA  
724  C C   . HIS A 95  ? 2.70196 2.44571 2.80648 0.19241  -0.26752 -0.02701 95  HIS B C   
725  O O   . HIS A 95  ? 2.73955 2.44599 2.90221 0.17535  -0.32637 -0.01230 95  HIS B O   
726  C CB  . HIS A 95  ? 2.76225 2.27784 2.59194 0.15559  -0.30758 0.03604  95  HIS B CB  
727  C CG  . HIS A 95  ? 2.76350 2.18584 2.41987 0.14690  -0.29286 0.05430  95  HIS B CG  
728  N ND1 . HIS A 95  ? 2.73736 2.08779 2.32957 0.13740  -0.32102 0.06017  95  HIS B ND1 
729  C CD2 . HIS A 95  ? 2.79124 2.18169 2.32862 0.14664  -0.25046 0.06724  95  HIS B CD2 
730  C CE1 . HIS A 95  ? 2.73039 2.01459 2.16966 0.12953  -0.29787 0.07204  95  HIS B CE1 
731  N NE2 . HIS A 95  ? 2.76506 2.07065 2.17107 0.13679  -0.25462 0.07607  95  HIS B NE2 
732  N N   . VAL A 96  ? 2.32710 2.20676 2.52085 0.21472  -0.21296 -0.06541 96  VAL B N   
733  C CA  . VAL A 96  ? 2.30869 2.29668 2.66928 0.21832  -0.21658 -0.09237 96  VAL B CA  
734  C C   . VAL A 96  ? 2.27873 2.25429 2.76696 0.21789  -0.26939 -0.11031 96  VAL B C   
735  O O   . VAL A 96  ? 2.24046 2.18707 2.72676 0.22489  -0.26997 -0.12336 96  VAL B O   
736  C CB  . VAL A 96  ? 2.24558 2.39485 2.66227 0.23906  -0.14072 -0.13113 96  VAL B CB  
737  C CG1 . VAL A 96  ? 2.17683 2.44762 2.76961 0.23914  -0.14255 -0.16459 96  VAL B CG1 
738  C CG2 . VAL A 96  ? 2.26070 2.42081 2.55342 0.24499  -0.08904 -0.10275 96  VAL B CG2 
739  N N   . LYS A 97  ? 2.16209 2.80807 2.56612 -0.01681 0.18809  0.05605  97  LYS B N   
740  C CA  . LYS A 97  ? 2.06800 2.75976 2.44128 -0.05996 0.15318  0.09442  97  LYS B CA  
741  C C   . LYS A 97  ? 2.07675 2.66026 2.40193 -0.07157 0.12325  0.09609  97  LYS B C   
742  O O   . LYS A 97  ? 2.15414 2.68672 2.42069 -0.09134 0.14682  0.04788  97  LYS B O   
743  C CB  . LYS A 97  ? 2.06908 2.85096 2.39028 -0.09917 0.17999  0.07098  97  LYS B CB  
744  C CG  . LYS A 97  ? 1.99234 2.81016 2.28291 -0.13352 0.13885  0.11421  97  LYS B CG  
745  C CD  . LYS A 97  ? 1.99757 2.90573 2.22417 -0.16704 0.15534  0.09430  97  LYS B CD  
746  C CE  . LYS A 97  ? 1.93187 2.87242 2.13887 -0.18887 0.10792  0.14545  97  LYS B CE  
747  N NZ  . LYS A 97  ? 1.97627 3.00329 2.11155 -0.21681 0.11034  0.12630  97  LYS B NZ  
748  N N   . PRO A 98  ? 1.99962 2.55077 2.34737 -0.06621 0.07642  0.14345  98  PRO B N   
749  C CA  . PRO A 98  ? 2.00912 2.45132 2.30855 -0.07605 0.05608  0.14059  98  PRO B CA  
750  C C   . PRO A 98  ? 1.99042 2.44698 2.24336 -0.12022 0.05633  0.12187  98  PRO B C   
751  O O   . PRO A 98  ? 1.97532 2.52633 2.22418 -0.14091 0.06548  0.11461  98  PRO B O   
752  C CB  . PRO A 98  ? 1.96675 2.40156 2.30621 -0.06441 0.00643  0.19253  98  PRO B CB  
753  C CG  . PRO A 98  ? 1.91558 2.47035 2.31986 -0.07026 -0.00108 0.22423  98  PRO B CG  
754  C CD  . PRO A 98  ? 1.94785 2.56362 2.36644 -0.05742 0.04455  0.19575  98  PRO B CD  
755  N N   . ARG A 99  ? 2.12949 2.49783 2.34673 -0.13397 0.04551  0.11416  99  ARG B N   
756  C CA  . ARG A 99  ? 2.12623 2.50502 2.31272 -0.17326 0.04763  0.08624  99  ARG B CA  
757  C C   . ARG A 99  ? 2.02622 2.46238 2.24608 -0.18371 0.00513  0.12877  99  ARG B C   
758  O O   . ARG A 99  ? 1.95987 2.40096 2.21779 -0.16727 -0.02311 0.17556  99  ARG B O   
759  C CB  . ARG A 99  ? 2.19627 2.44983 2.33353 -0.18682 0.06720  0.05342  99  ARG B CB  
760  C CG  . ARG A 99  ? 2.26087 2.52225 2.36977 -0.23033 0.09398  -0.00542 99  ARG B CG  
761  C CD  . ARG A 99  ? 2.33872 2.45749 2.39644 -0.24552 0.12659  -0.03451 99  ARG B CD  
762  N NE  . ARG A 99  ? 2.46354 2.49408 2.49360 -0.22352 0.16444  -0.05162 99  ARG B NE  
763  C CZ  . ARG A 99  ? 2.56010 2.47399 2.54170 -0.24428 0.21304  -0.09523 99  ARG B CZ  
764  N NH1 . ARG A 99  ? 2.54776 2.42551 2.50261 -0.29394 0.23327  -0.13010 99  ARG B NH1 
765  N NH2 . ARG A 99  ? 2.67059 2.49878 2.63631 -0.21471 0.24604  -0.10523 99  ARG B NH2 
766  N N   . ALA A 100 ? 2.10927 2.59018 2.32185 -0.21091 0.00066  0.10842  100 ALA B N   
767  C CA  . ALA A 100 ? 2.02786 2.54574 2.28055 -0.21199 -0.03864 0.15164  100 ALA B CA  
768  C C   . ALA A 100 ? 2.00508 2.43355 2.25559 -0.21926 -0.04753 0.14536  100 ALA B C   
769  O O   . ALA A 100 ? 2.04622 2.41301 2.25904 -0.23732 -0.02222 0.09980  100 ALA B O   
770  C CB  . ALA A 100 ? 2.02081 2.63673 2.28059 -0.22699 -0.05116 0.14493  100 ALA B CB  
771  N N   . PRO A 101 ? 2.08159 2.49819 2.36831 -0.21049 -0.07777 0.18643  101 PRO B N   
772  C CA  . PRO A 101 ? 2.07629 2.42175 2.35758 -0.22235 -0.08441 0.17399  101 PRO B CA  
773  C C   . PRO A 101 ? 2.05836 2.44125 2.35785 -0.24218 -0.08114 0.14279  101 PRO B C   
774  O O   . PRO A 101 ? 2.04194 2.51538 2.36663 -0.24126 -0.08899 0.14459  101 PRO B O   
775  C CB  . PRO A 101 ? 2.03542 2.38322 2.36364 -0.21136 -0.11786 0.21996  101 PRO B CB  
776  C CG  . PRO A 101 ? 2.03215 2.42413 2.37844 -0.19284 -0.12157 0.25281  101 PRO B CG  
777  C CD  . PRO A 101 ? 2.04432 2.50511 2.37719 -0.19445 -0.10070 0.23993  101 PRO B CD  
778  N N   . GLY A 102 ? 2.22505 2.54406 2.51070 -0.25985 -0.06962 0.11246  102 GLY B N   
779  C CA  . GLY A 102 ? 2.20956 2.57130 2.52818 -0.27845 -0.06263 0.07373  102 GLY B CA  
780  C C   . GLY A 102 ? 2.19818 2.50394 2.52832 -0.29131 -0.05769 0.05576  102 GLY B C   
781  O O   . GLY A 102 ? 2.20810 2.44721 2.51869 -0.28552 -0.06765 0.07879  102 GLY B O   
782  N N   . ASN A 103 ? 2.24316 2.58545 2.60874 -0.31044 -0.04174 0.00872  103 ASN B N   
783  C CA  . ASN A 103 ? 2.25385 2.55182 2.63426 -0.32749 -0.02498 -0.02262 103 ASN B CA  
784  C C   . ASN A 103 ? 2.23821 2.53586 2.67477 -0.30329 -0.05876 0.01321  103 ASN B C   
785  O O   . ASN A 103 ? 2.26542 2.49483 2.68539 -0.31502 -0.04785 -0.00110 103 ASN B O   
786  C CB  . ASN A 103 ? 2.31489 2.49108 2.59521 -0.35532 0.01373  -0.04250 103 ASN B CB  
787  C CG  . ASN A 103 ? 2.34805 2.49951 2.57357 -0.38425 0.05700  -0.08042 103 ASN B CG  
788  O OD1 . ASN A 103 ? 2.41554 2.45970 2.54797 -0.39592 0.08328  -0.07659 103 ASN B OD1 
789  N ND2 . ASN A 103 ? 2.31662 2.56544 2.59978 -0.39555 0.06322  -0.11730 103 ASN B ND2 
790  N N   . LEU A 104 ? 2.24097 2.60962 2.73864 -0.27279 -0.09658 0.05855  104 LEU B N   
791  C CA  . LEU A 104 ? 2.23318 2.58788 2.78384 -0.25191 -0.12551 0.09976  104 LEU B CA  
792  C C   . LEU A 104 ? 2.23608 2.62015 2.87691 -0.24206 -0.12787 0.07545  104 LEU B C   
793  O O   . LEU A 104 ? 2.23187 2.70335 2.93287 -0.22311 -0.14229 0.07623  104 LEU B O   
794  C CB  . LEU A 104 ? 2.21697 2.62151 2.78649 -0.22700 -0.15708 0.16540  104 LEU B CB  
795  C CG  . LEU A 104 ? 2.22881 2.62744 2.86874 -0.20697 -0.18392 0.21331  104 LEU B CG  
796  C CD1 . LEU A 104 ? 2.22578 2.54178 2.85083 -0.22132 -0.18302 0.21585  104 LEU B CD1 
797  C CD2 . LEU A 104 ? 2.22869 2.68779 2.87945 -0.18716 -0.20628 0.27828  104 LEU B CD2 
798  N N   . THR A 105 ? 2.28735 2.60365 2.93872 -0.25265 -0.11516 0.05113  105 THR B N   
799  C CA  . THR A 105 ? 2.30244 2.63434 3.05023 -0.23946 -0.11242 0.02339  105 THR B CA  
800  C C   . THR A 105 ? 2.33840 2.59785 3.10949 -0.23562 -0.12309 0.04201  105 THR B C   
801  O O   . THR A 105 ? 2.32558 2.54816 3.05501 -0.23976 -0.14082 0.08395  105 THR B O   
802  C CB  . THR A 105 ? 2.30834 2.63808 3.05068 -0.26851 -0.06680 -0.05632 105 THR B CB  
803  O OG1 . THR A 105 ? 2.33656 2.57180 2.97081 -0.30630 -0.03691 -0.07948 105 THR B OG1 
804  C CG2 . THR A 105 ? 2.27021 2.68464 3.01494 -0.27622 -0.05646 -0.08171 105 THR B CG2 
805  N N   . VAL A 106 ? 2.34481 2.58809 3.19172 -0.22955 -0.10975 0.00358  106 VAL B N   
806  C CA  . VAL A 106 ? 2.38675 2.56199 3.27506 -0.22689 -0.11616 0.00995  106 VAL B CA  
807  C C   . VAL A 106 ? 2.44644 2.58106 3.35266 -0.24675 -0.07637 -0.07063 106 VAL B C   
808  O O   . VAL A 106 ? 2.46441 2.64667 3.41952 -0.24115 -0.05128 -0.11836 106 VAL B O   
809  C CB  . VAL A 106 ? 2.39913 2.59704 3.39704 -0.18184 -0.14721 0.06666  106 VAL B CB  
810  C CG1 . VAL A 106 ? 2.46049 2.57927 3.52559 -0.18070 -0.14077 0.05262  106 VAL B CG1 
811  C CG2 . VAL A 106 ? 2.36831 2.58843 3.33177 -0.17285 -0.17945 0.14820  106 VAL B CG2 
812  N N   . HIS A 107 ? 2.55240 2.60785 3.41988 -0.27327 -0.06894 -0.09155 107 HIS B N   
813  C CA  . HIS A 107 ? 2.62771 2.63933 3.51596 -0.29252 -0.02993 -0.16980 107 HIS B CA  
814  C C   . HIS A 107 ? 2.66675 2.63598 3.66395 -0.27266 -0.03878 -0.16905 107 HIS B C   
815  O O   . HIS A 107 ? 2.65736 2.59667 3.66332 -0.26933 -0.07065 -0.11616 107 HIS B O   
816  C CB  . HIS A 107 ? 2.68712 2.63733 3.43448 -0.34327 -0.01043 -0.20766 107 HIS B CB  
817  C CG  . HIS A 107 ? 2.78057 2.69862 3.51599 -0.37201 0.04212  -0.29644 107 HIS B CG  
818  N ND1 . HIS A 107 ? 2.86847 2.71928 3.49871 -0.41465 0.05633  -0.33744 107 HIS B ND1 
819  C CD2 . HIS A 107 ? 2.78801 2.74017 3.60471 -0.36504 0.08534  -0.35577 107 HIS B CD2 
820  C CE1 . HIS A 107 ? 2.91976 2.75774 3.55596 -0.43616 0.11144  -0.41837 107 HIS B CE1 
821  N NE2 . HIS A 107 ? 2.86989 2.77019 3.62665 -0.40624 0.13218  -0.43268 107 HIS B NE2 
822  N N   . ASP A 112 ? 2.71585 2.12050 4.16141 -0.37445 0.01969  -0.36776 112 ASP B N   
823  C CA  . ASP A 112 ? 2.65955 2.12126 3.94740 -0.42479 0.00078  -0.39032 112 ASP B CA  
824  C C   . ASP A 112 ? 2.55902 2.08996 3.78826 -0.41489 -0.04664 -0.28791 112 ASP B C   
825  O O   . ASP A 112 ? 2.52372 2.05737 3.82683 -0.37858 -0.06334 -0.20224 112 ASP B O   
826  C CB  . ASP A 112 ? 2.68403 2.18457 3.89264 -0.42695 0.03268  -0.46032 112 ASP B CB  
827  C CG  . ASP A 112 ? 2.64259 2.20640 3.89024 -0.36828 0.03740  -0.41563 112 ASP B CG  
828  O OD1 . ASP A 112 ? 2.57529 2.18996 3.81407 -0.34106 0.00035  -0.32336 112 ASP B OD1 
829  O OD2 . ASP A 112 ? 2.68726 2.25785 3.97795 -0.35197 0.08045  -0.48056 112 ASP B OD2 
830  N N   . THR A 113 ? 2.81145 2.39470 3.90376 -0.44578 -0.06631 -0.29673 113 THR B N   
831  C CA  . THR A 113 ? 2.72258 2.37186 3.75829 -0.43574 -0.10629 -0.21162 113 THR B CA  
832  C C   . THR A 113 ? 2.65696 2.36025 3.68802 -0.38635 -0.10219 -0.16506 113 THR B C   
833  O O   . THR A 113 ? 2.68989 2.39882 3.71615 -0.37305 -0.07143 -0.21198 113 THR B O   
834  C CB  . THR A 113 ? 2.73471 2.41574 3.63161 -0.47708 -0.13091 -0.23566 113 THR B CB  
835  O OG1 . THR A 113 ? 2.67405 2.41071 3.55022 -0.46949 -0.17042 -0.15744 113 THR B OG1 
836  C CG2 . THR A 113 ? 2.77255 2.47009 3.55385 -0.47627 -0.11047 -0.27391 113 THR B CG2 
837  N N   . LEU A 114 ? 2.66300 2.41255 3.70089 -0.36284 -0.13061 -0.07769 114 LEU B N   
838  C CA  . LEU A 114 ? 2.59270 2.40416 3.62311 -0.32086 -0.13296 -0.03253 114 LEU B CA  
839  C C   . LEU A 114 ? 2.52561 2.39007 3.43688 -0.33338 -0.15133 -0.01016 114 LEU B C   
840  O O   . LEU A 114 ? 2.48866 2.36165 3.36618 -0.35303 -0.17650 0.01875  114 LEU B O   
841  C CB  . LEU A 114 ? 2.58567 2.40839 3.70958 -0.28044 -0.14831 0.05051  114 LEU B CB  
842  C CG  . LEU A 114 ? 2.53565 2.43768 3.64707 -0.23971 -0.16046 0.10317  114 LEU B CG  
843  C CD1 . LEU A 114 ? 2.57765 2.49309 3.76635 -0.19935 -0.14457 0.07564  114 LEU B CD1 
844  C CD2 . LEU A 114 ? 2.52322 2.44476 3.66085 -0.22174 -0.18496 0.19854  114 LEU B CD2 
845  N N   . LEU A 115 ? 2.55377 2.45370 3.41073 -0.32195 -0.13617 -0.02671 115 LEU B N   
846  C CA  . LEU A 115 ? 2.52735 2.45472 3.26497 -0.33428 -0.14344 -0.01779 115 LEU B CA  
847  C C   . LEU A 115 ? 2.45985 2.45202 3.20264 -0.30325 -0.15075 0.03482  115 LEU B C   
848  O O   . LEU A 115 ? 2.45423 2.47892 3.24726 -0.28076 -0.13584 0.02610  115 LEU B O   
849  C CB  . LEU A 115 ? 2.58888 2.48801 3.23732 -0.35983 -0.11058 -0.08774 115 LEU B CB  
850  C CG  . LEU A 115 ? 2.61036 2.51033 3.12242 -0.37360 -0.11111 -0.08056 115 LEU B CG  
851  C CD1 . LEU A 115 ? 2.63150 2.51942 3.08132 -0.38580 -0.14999 -0.05336 115 LEU B CD1 
852  C CD2 . LEU A 115 ? 2.69569 2.55693 3.12440 -0.40222 -0.06758 -0.14699 115 LEU B CD2 
853  N N   . LEU A 116 ? 2.51013 2.52905 3.20573 -0.30227 -0.17402 0.08336  116 LEU B N   
854  C CA  . LEU A 116 ? 2.46230 2.54046 3.13708 -0.28094 -0.17747 0.12226  116 LEU B CA  
855  C C   . LEU A 116 ? 2.47744 2.54496 3.03813 -0.29500 -0.17168 0.10851  116 LEU B C   
856  O O   . LEU A 116 ? 2.51403 2.54467 3.01805 -0.31234 -0.18317 0.10002  116 LEU B O   
857  C CB  . LEU A 116 ? 2.42263 2.54060 3.14297 -0.26468 -0.20174 0.19250  116 LEU B CB  
858  C CG  . LEU A 116 ? 2.42692 2.56200 3.24427 -0.23967 -0.20782 0.23228  116 LEU B CG  
859  C CD1 . LEU A 116 ? 2.48167 2.55103 3.37209 -0.24833 -0.20441 0.21373  116 LEU B CD1 
860  C CD2 . LEU A 116 ? 2.40637 2.58512 3.23124 -0.23025 -0.22345 0.30448  116 LEU B CD2 
861  N N   . THR A 117 ? 2.40823 2.50697 2.93599 -0.28683 -0.15542 0.10607  117 THR B N   
862  C CA  . THR A 117 ? 2.44294 2.51307 2.86334 -0.29813 -0.14314 0.09519  117 THR B CA  
863  C C   . THR A 117 ? 2.39820 2.51821 2.81048 -0.28545 -0.13250 0.10840  117 THR B C   
864  O O   . THR A 117 ? 2.36061 2.53931 2.83598 -0.27492 -0.12903 0.10646  117 THR B O   
865  C CB  . THR A 117 ? 2.52919 2.53721 2.88078 -0.32601 -0.11020 0.03807  117 THR B CB  
866  O OG1 . THR A 117 ? 2.62901 2.58434 2.86282 -0.33518 -0.10455 0.04219  117 THR B OG1 
867  C CG2 . THR A 117 ? 2.49851 2.53741 2.88575 -0.33145 -0.07412 -0.00137 117 THR B CG2 
868  N N   . TRP A 118 ? 2.36400 2.46151 2.69930 -0.28463 -0.12943 0.11975  118 TRP B N   
869  C CA  . TRP A 118 ? 2.34853 2.47980 2.66397 -0.27831 -0.11295 0.12102  118 TRP B CA  
870  C C   . TRP A 118 ? 2.41548 2.47094 2.62740 -0.28537 -0.09382 0.11176  118 TRP B C   
871  O O   . TRP A 118 ? 2.47559 2.46086 2.62737 -0.29246 -0.09843 0.11002  118 TRP B O   
872  C CB  . TRP A 118 ? 2.29615 2.50183 2.66169 -0.25450 -0.13627 0.16759  118 TRP B CB  
873  C CG  . TRP A 118 ? 2.30098 2.49571 2.66012 -0.24243 -0.15952 0.20423  118 TRP B CG  
874  C CD1 . TRP A 118 ? 2.31710 2.50583 2.63459 -0.22899 -0.15753 0.21674  118 TRP B CD1 
875  C CD2 . TRP A 118 ? 2.28437 2.47847 2.69182 -0.24326 -0.18710 0.22674  118 TRP B CD2 
876  N NE1 . TRP A 118 ? 2.31776 2.51630 2.66124 -0.21885 -0.18543 0.24612  118 TRP B NE1 
877  C CE2 . TRP A 118 ? 2.29137 2.49380 2.68812 -0.23190 -0.20353 0.25112  118 TRP B CE2 
878  C CE3 . TRP A 118 ? 2.27077 2.45767 2.73746 -0.25299 -0.19723 0.22400  118 TRP B CE3 
879  C CZ2 . TRP A 118 ? 2.29187 2.50686 2.73653 -0.23615 -0.23115 0.26983  118 TRP B CZ2 
880  C CZ3 . TRP A 118 ? 2.26526 2.44832 2.77220 -0.25905 -0.22088 0.24273  118 TRP B CZ3 
881  C CH2 . TRP A 118 ? 2.27820 2.48057 2.77440 -0.25371 -0.23837 0.26398  118 TRP B CH2 
882  N N   . SER A 119 ? 2.43417 2.49984 2.62081 -0.28292 -0.07252 0.10572  119 SER B N   
883  C CA  . SER A 119 ? 2.50746 2.48761 2.60037 -0.28461 -0.04971 0.10122  119 SER B CA  
884  C C   . SER A 119 ? 2.50666 2.50094 2.60113 -0.25027 -0.07095 0.14002  119 SER B C   
885  O O   . SER A 119 ? 2.44224 2.52336 2.60304 -0.23505 -0.08617 0.15868  119 SER B O   
886  C CB  . SER A 119 ? 2.52671 2.49231 2.59235 -0.31021 -0.00144 0.05722  119 SER B CB  
887  O OG  . SER A 119 ? 2.53189 2.48678 2.60001 -0.34456 0.02511  0.01482  119 SER B OG  
888  N N   . ASN A 120 ? 2.53230 2.44187 2.55262 -0.23642 -0.07090 0.15352  120 ASN B N   
889  C CA  . ASN A 120 ? 2.55593 2.47478 2.58252 -0.19934 -0.08153 0.18036  120 ASN B CA  
890  C C   . ASN A 120 ? 2.57475 2.49391 2.59408 -0.20328 -0.03861 0.15341  120 ASN B C   
891  O O   . ASN A 120 ? 2.62778 2.47110 2.58682 -0.22859 0.00175  0.12161  120 ASN B O   
892  C CB  . ASN A 120 ? 2.64116 2.46821 2.59293 -0.17481 -0.09843 0.20474  120 ASN B CB  
893  C CG  . ASN A 120 ? 2.74236 2.44066 2.58226 -0.19502 -0.05931 0.18763  120 ASN B CG  
894  O OD1 . ASN A 120 ? 2.74825 2.43234 2.57424 -0.23627 -0.02075 0.15050  120 ASN B OD1 
895  N ND2 . ASN A 120 ? 2.83855 2.44324 2.60044 -0.16536 -0.06788 0.21625  120 ASN B ND2 
896  N N   . PRO A 121 ? 2.46907 2.47259 2.54627 -0.18522 -0.04110 0.15972  121 PRO B N   
897  C CA  . PRO A 121 ? 2.50962 2.52759 2.58020 -0.19631 0.00015  0.12239  121 PRO B CA  
898  C C   . PRO A 121 ? 2.61816 2.52437 2.62524 -0.18267 0.03496  0.10884  121 PRO B C   
899  O O   . PRO A 121 ? 2.67369 2.57914 2.67489 -0.19211 0.07389  0.07120  121 PRO B O   
900  C CB  . PRO A 121 ? 2.45977 2.59729 2.59831 -0.17827 -0.01387 0.13893  121 PRO B CB  
901  C CG  . PRO A 121 ? 2.40975 2.56595 2.58643 -0.14978 -0.05392 0.18644  121 PRO B CG  
902  C CD  . PRO A 121 ? 2.39952 2.49910 2.55269 -0.16380 -0.07706 0.19524  121 PRO B CD  
903  N N   . TYR A 122 ? 2.52153 2.32936 2.47750 -0.16031 0.02102  0.13853  122 TYR B N   
904  C CA  . TYR A 122 ? 2.62881 2.31588 2.52419 -0.13452 0.04765  0.14110  122 TYR B CA  
905  C C   . TYR A 122 ? 2.69426 2.25674 2.49716 -0.13459 0.03828  0.16816  122 TYR B C   
906  O O   . TYR A 122 ? 2.65491 2.24607 2.45553 -0.14205 -0.00014 0.18821  122 TYR B O   
907  C CB  . TYR A 122 ? 2.63572 2.36316 2.58435 -0.07616 0.02695  0.16683  122 TYR B CB  
908  C CG  . TYR A 122 ? 2.60916 2.45056 2.63062 -0.07802 0.04647  0.13813  122 TYR B CG  
909  C CD1 . TYR A 122 ? 2.68739 2.49435 2.69179 -0.08941 0.10087  0.09028  122 TYR B CD1 
910  C CD2 . TYR A 122 ? 2.50320 2.48311 2.60330 -0.07358 0.01418  0.15695  122 TYR B CD2 
911  C CE1 . TYR A 122 ? 2.69496 2.61174 2.75133 -0.09454 0.11897  0.05976  122 TYR B CE1 
912  C CE2 . TYR A 122 ? 2.49148 2.57382 2.63961 -0.07833 0.03472  0.13537  122 TYR B CE2 
913  C CZ  . TYR A 122 ? 2.60077 2.65583 2.72305 -0.08799 0.08532  0.08570  122 TYR B CZ  
914  O OH  . TYR A 122 ? 2.61685 2.77967 2.77339 -0.09570 0.10571  0.06032  122 TYR B OH  
915  N N   . PRO A 123 ? 2.79392 2.21114 2.51274 -0.12862 0.07539  0.16904  123 PRO B N   
916  C CA  . PRO A 123 ? 2.88144 2.16997 2.49026 -0.12550 0.06668  0.20488  123 PRO B CA  
917  C C   . PRO A 123 ? 2.91496 2.20504 2.52371 -0.05834 0.00365  0.26266  123 PRO B C   
918  O O   . PRO A 123 ? 2.87207 2.24521 2.57038 -0.01292 -0.02003 0.27045  123 PRO B O   
919  C CB  . PRO A 123 ? 3.00164 2.12959 2.52693 -0.14075 0.13442  0.18940  123 PRO B CB  
920  C CG  . PRO A 123 ? 2.99190 2.15582 2.59232 -0.11407 0.15563  0.16417  123 PRO B CG  
921  C CD  . PRO A 123 ? 2.86196 2.21589 2.57458 -0.12860 0.13208  0.13553  123 PRO B CD  
922  N N   . PRO A 124 ? 3.10550 2.31544 2.61611 -0.05214 -0.02494 0.30073  124 PRO B N   
923  C CA  . PRO A 124 ? 3.13685 2.37557 2.65502 0.01048  -0.09787 0.35187  124 PRO B CA  
924  C C   . PRO A 124 ? 3.21052 2.39265 2.74050 0.08398  -0.10319 0.38282  124 PRO B C   
925  O O   . PRO A 124 ? 3.17802 2.45595 2.79167 0.13895  -0.15877 0.40480  124 PRO B O   
926  C CB  . PRO A 124 ? 3.24592 2.39192 2.62533 -0.00772 -0.11739 0.37982  124 PRO B CB  
927  C CG  . PRO A 124 ? 3.20649 2.34809 2.56061 -0.08660 -0.06636 0.33256  124 PRO B CG  
928  C CD  . PRO A 124 ? 3.16531 2.29499 2.56888 -0.10889 0.00096  0.29139  124 PRO B CD  
929  N N   . ASP A 125 ? 3.19725 2.22640 2.65441 0.08687  -0.04485 0.38252  125 ASP B N   
930  C CA  . ASP A 125 ? 3.27777 2.23751 2.75128 0.16385  -0.04645 0.41126  125 ASP B CA  
931  C C   . ASP A 125 ? 3.17558 2.27358 2.80542 0.19168  -0.04273 0.37619  125 ASP B C   
932  O O   . ASP A 125 ? 3.19574 2.31186 2.88738 0.26767  -0.07041 0.39981  125 ASP B O   
933  C CB  . ASP A 125 ? 3.42934 2.18418 2.79882 0.15092  0.02831  0.41000  125 ASP B CB  
934  C CG  . ASP A 125 ? 3.40509 2.15705 2.77504 0.06230  0.10461  0.34124  125 ASP B CG  
935  O OD1 . ASP A 125 ? 3.31312 2.16835 2.69944 0.00506  0.09522  0.31457  125 ASP B OD1 
936  O OD2 . ASP A 125 ? 3.47663 2.12717 2.83813 0.05092  0.17300  0.31025  125 ASP B OD2 
937  N N   . ASN A 126 ? 3.08179 2.28166 2.77561 0.13304  -0.00858 0.32039  126 ASN B N   
938  C CA  . ASN A 126 ? 2.99742 2.33905 2.82361 0.14958  -0.00283 0.28795  126 ASN B CA  
939  C C   . ASN A 126 ? 2.91562 2.39954 2.83463 0.19358  -0.07439 0.31926  126 ASN B C   
940  O O   . ASN A 126 ? 2.87827 2.40702 2.78081 0.17745  -0.12572 0.34350  126 ASN B O   
941  C CB  . ASN A 126 ? 2.91113 2.34289 2.76852 0.07610  0.03291  0.23400  126 ASN B CB  
942  C CG  . ASN A 126 ? 2.81453 2.41919 2.79338 0.08418  0.02341  0.21468  126 ASN B CG  
943  O OD1 . ASN A 126 ? 2.71281 2.43724 2.74133 0.06588  -0.01505 0.22626  126 ASN B OD1 
944  N ND2 . ASN A 126 ? 2.87702 2.48920 2.90092 0.10901  0.06386  0.18373  126 ASN B ND2 
945  N N   . TYR A 127 ? 2.75848 2.31705 2.78134 0.24581  -0.07308 0.31164  127 TYR B N   
946  C CA  . TYR A 127 ? 2.67880 2.37300 2.80338 0.29108  -0.13654 0.33802  127 TYR B CA  
947  C C   . TYR A 127 ? 2.54159 2.39139 2.73110 0.23708  -0.15828 0.32668  127 TYR B C   
948  O O   . TYR A 127 ? 2.48209 2.41605 2.71712 0.24772  -0.21894 0.35177  127 TYR B O   
949  C CB  . TYR A 127 ? 2.68097 2.42976 2.91537 0.35529  -0.11789 0.32295  127 TYR B CB  
950  C CG  . TYR A 127 ? 2.82904 2.42124 3.02146 0.42221  -0.09616 0.33554  127 TYR B CG  
951  C CD1 . TYR A 127 ? 2.94307 2.35750 2.99964 0.42980  -0.10617 0.37498  127 TYR B CD1 
952  C CD2 . TYR A 127 ? 2.86554 2.48121 3.15300 0.47830  -0.06097 0.30851  127 TYR B CD2 
953  C CE1 . TYR A 127 ? 3.08821 2.34092 3.10202 0.49290  -0.08363 0.39464  127 TYR B CE1 
954  C CE2 . TYR A 127 ? 3.00712 2.46661 3.26439 0.54484  -0.03826 0.32023  127 TYR B CE2 
955  C CZ  . TYR A 127 ? 3.11862 2.39107 3.23762 0.55285  -0.05092 0.36726  127 TYR B CZ  
956  O OH  . TYR A 127 ? 3.25302 2.35106 3.33646 0.62076  -0.02597 0.38714  127 TYR B OH  
957  N N   . LEU A 128 ? 2.68684 2.57567 2.88229 0.17958  -0.11154 0.28951  128 LEU B N   
958  C CA  . LEU A 128 ? 2.55921 2.58418 2.81786 0.13451  -0.12847 0.28598  128 LEU B CA  
959  C C   . LEU A 128 ? 2.53223 2.53892 2.74230 0.10005  -0.17193 0.30654  128 LEU B C   
960  O O   . LEU A 128 ? 2.43811 2.54740 2.71120 0.07495  -0.19940 0.31286  128 LEU B O   
961  C CB  . LEU A 128 ? 2.53035 2.59090 2.78880 0.08643  -0.07438 0.24755  128 LEU B CB  
962  C CG  . LEU A 128 ? 2.60907 2.66621 2.88653 0.10700  -0.01859 0.21102  128 LEU B CG  
963  C CD1 . LEU A 128 ? 2.58675 2.70093 2.85535 0.05347  0.02289  0.17266  128 LEU B CD1 
964  C CD2 . LEU A 128 ? 2.56708 2.72288 2.95097 0.15770  -0.02664 0.21782  128 LEU B CD2 
965  N N   . TYR A 129 ? 2.76562 2.63841 2.86306 0.09597  -0.17352 0.31530  129 TYR B N   
966  C CA  . TYR A 129 ? 2.77464 2.62300 2.81374 0.06025  -0.20620 0.32597  129 TYR B CA  
967  C C   . TYR A 129 ? 2.77534 2.68414 2.84937 0.08739  -0.27708 0.35494  129 TYR B C   
968  O O   . TYR A 129 ? 2.76694 2.69641 2.82531 0.05154  -0.30645 0.35387  129 TYR B O   
969  C CB  . TYR A 129 ? 2.89093 2.57732 2.79084 0.04703  -0.17989 0.32697  129 TYR B CB  
970  C CG  . TYR A 129 ? 2.91841 2.56488 2.73837 0.01106  -0.20515 0.33345  129 TYR B CG  
971  C CD1 . TYR A 129 ? 2.86033 2.54082 2.68950 -0.04824 -0.18631 0.30291  129 TYR B CD1 
972  C CD2 . TYR A 129 ? 3.02522 2.60085 2.75764 0.03894  -0.24765 0.36857  129 TYR B CD2 
973  C CE1 . TYR A 129 ? 2.90730 2.55134 2.66785 -0.08149 -0.20177 0.29963  129 TYR B CE1 
974  C CE2 . TYR A 129 ? 3.08386 2.62389 2.73079 0.00165  -0.26563 0.36775  129 TYR B CE2 
975  C CZ  . TYR A 129 ? 3.01966 2.59380 2.68469 -0.05994 -0.23896 0.32937  129 TYR B CZ  
976  O OH  . TYR A 129 ? 3.08242 2.62314 2.66836 -0.09735 -0.25023 0.31974  129 TYR B OH  
977  N N   . ASN A 130 ? 2.78753 2.73350 2.91782 0.14928  -0.30505 0.37446  130 ASN B N   
978  C CA  . ASN A 130 ? 2.80726 2.81501 2.96898 0.17949  -0.37932 0.39880  130 ASN B CA  
979  C C   . ASN A 130 ? 2.67877 2.85817 2.98901 0.16570  -0.40341 0.38734  130 ASN B C   
980  O O   . ASN A 130 ? 2.68201 2.92541 3.01977 0.15935  -0.46199 0.39296  130 ASN B O   
981  C CB  . ASN A 130 ? 2.92413 2.88076 3.07023 0.26155  -0.40504 0.42935  130 ASN B CB  
982  C CG  . ASN A 130 ? 2.87654 2.95122 3.17393 0.31290  -0.40382 0.42236  130 ASN B CG  
983  O OD1 . ASN A 130 ? 2.81032 3.03240 3.22457 0.31807  -0.44566 0.41911  130 ASN B OD1 
984  N ND2 . ASN A 130 ? 2.92427 2.93478 3.22383 0.34708  -0.34980 0.41374  130 ASN B ND2 
985  N N   . HIS A 131 ? 2.64285 2.89772 3.04419 0.15594  -0.35744 0.36956  131 HIS B N   
986  C CA  . HIS A 131 ? 2.52443 2.93098 3.05818 0.13271  -0.36742 0.36224  131 HIS B CA  
987  C C   . HIS A 131 ? 2.44334 2.87384 2.99024 0.07550  -0.31639 0.34817  131 HIS B C   
988  O O   . HIS A 131 ? 2.36223 2.90355 3.01001 0.06068  -0.30006 0.34581  131 HIS B O   
989  C CB  . HIS A 131 ? 2.49066 3.00040 3.14447 0.18621  -0.36863 0.36139  131 HIS B CB  
990  C CG  . HIS A 131 ? 2.53795 2.98895 3.17141 0.22854  -0.31681 0.35224  131 HIS B CG  
991  N ND1 . HIS A 131 ? 2.64060 3.01907 3.24649 0.29947  -0.33269 0.36464  131 HIS B ND1 
992  C CD2 . HIS A 131 ? 2.52014 2.97283 3.15655 0.20977  -0.24914 0.32937  131 HIS B CD2 
993  C CE1 . HIS A 131 ? 2.67063 2.99986 3.26943 0.32030  -0.27142 0.34523  131 HIS B CE1 
994  N NE2 . HIS A 131 ? 2.59787 2.97738 3.21262 0.26419  -0.22093 0.32007  131 HIS B NE2 
995  N N   . LEU A 132 ? 2.35703 2.68904 2.80392 0.04402  -0.29078 0.34032  132 LEU B N   
996  C CA  . LEU A 132 ? 2.29256 2.65016 2.74927 -0.00649 -0.25729 0.33124  132 LEU B CA  
997  C C   . LEU A 132 ? 2.24296 2.66975 2.76696 -0.04298 -0.28710 0.34029  132 LEU B C   
998  O O   . LEU A 132 ? 2.28467 2.69913 2.80187 -0.04693 -0.33182 0.34151  132 LEU B O   
999  C CB  . LEU A 132 ? 2.33883 2.58697 2.68805 -0.03153 -0.23387 0.31623  132 LEU B CB  
1000 C CG  . LEU A 132 ? 2.33716 2.56185 2.65311 -0.03963 -0.17923 0.29476  132 LEU B CG  
1001 C CD1 . LEU A 132 ? 2.34251 2.50662 2.59367 -0.08044 -0.16310 0.27650  132 LEU B CD1 
1002 C CD2 . LEU A 132 ? 2.26807 2.60431 2.66182 -0.04640 -0.15730 0.29615  132 LEU B CD2 
1003 N N   . THR A 133 ? 2.08502 2.58046 2.66879 -0.07163 -0.26101 0.34643  133 THR B N   
1004 C CA  . THR A 133 ? 2.04489 2.58886 2.69520 -0.11081 -0.27838 0.35757  133 THR B CA  
1005 C C   . THR A 133 ? 2.01370 2.54350 2.64694 -0.14246 -0.24729 0.36545  133 THR B C   
1006 O O   . THR A 133 ? 1.97196 2.56114 2.63701 -0.14777 -0.21663 0.38096  133 THR B O   
1007 C CB  . THR A 133 ? 1.99900 2.65806 2.76477 -0.11010 -0.28186 0.36859  133 THR B CB  
1008 O OG1 . THR A 133 ? 1.98424 2.69339 2.76803 -0.08552 -0.24189 0.36969  133 THR B OG1 
1009 C CG2 . THR A 133 ? 2.03468 2.72253 2.83832 -0.08791 -0.33319 0.35903  133 THR B CG2 
1010 N N   . TYR A 134 ? 2.11928 2.57517 2.70106 -0.16125 -0.25571 0.35446  134 TYR B N   
1011 C CA  . TYR A 134 ? 2.08737 2.53260 2.66154 -0.18272 -0.23426 0.36106  134 TYR B CA  
1012 C C   . TYR A 134 ? 2.04051 2.53532 2.69705 -0.20781 -0.23552 0.39156  134 TYR B C   
1013 O O   . TYR A 134 ? 2.03845 2.55224 2.75452 -0.22264 -0.25618 0.39460  134 TYR B O   
1014 C CB  . TYR A 134 ? 2.11122 2.47302 2.62917 -0.19529 -0.24078 0.33566  134 TYR B CB  
1015 C CG  . TYR A 134 ? 2.16858 2.46139 2.59589 -0.18009 -0.23544 0.30851  134 TYR B CG  
1016 C CD1 . TYR A 134 ? 2.16943 2.44669 2.54824 -0.17174 -0.20314 0.29508  134 TYR B CD1 
1017 C CD2 . TYR A 134 ? 2.23939 2.47911 2.62356 -0.17754 -0.26152 0.29643  134 TYR B CD2 
1018 C CE1 . TYR A 134 ? 2.23070 2.42922 2.52616 -0.16346 -0.19028 0.27240  134 TYR B CE1 
1019 C CE2 . TYR A 134 ? 2.30271 2.46397 2.59075 -0.16462 -0.25265 0.28137  134 TYR B CE2 
1020 C CZ  . TYR A 134 ? 2.29479 2.42946 2.54160 -0.15871 -0.21365 0.27045  134 TYR B CZ  
1021 O OH  . TYR A 134 ? 2.37068 2.41233 2.52180 -0.15124 -0.19706 0.25728  134 TYR B OH  
1022 N N   . ALA A 135 ? 2.04242 2.55707 2.69986 -0.21412 -0.21348 0.41475  135 ALA B N   
1023 C CA  . ALA A 135 ? 2.02123 2.55529 2.73938 -0.23701 -0.21021 0.45344  135 ALA B CA  
1024 C C   . ALA A 135 ? 2.03345 2.53135 2.72581 -0.23558 -0.20780 0.46158  135 ALA B C   
1025 O O   . ALA A 135 ? 2.04302 2.56325 2.68628 -0.22093 -0.19538 0.45932  135 ALA B O   
1026 C CB  . ALA A 135 ? 2.00444 2.61981 2.75365 -0.24093 -0.18459 0.48961  135 ALA B CB  
1027 N N   . VAL A 136 ? 2.17875 2.62568 2.91060 -0.24979 -0.22020 0.46524  136 VAL B N   
1028 C CA  . VAL A 136 ? 2.19018 2.60212 2.91631 -0.24118 -0.22202 0.46678  136 VAL B CA  
1029 C C   . VAL A 136 ? 2.22214 2.63375 3.00288 -0.24722 -0.21854 0.52557  136 VAL B C   
1030 O O   . VAL A 136 ? 2.22736 2.61113 3.06691 -0.27069 -0.21846 0.53970  136 VAL B O   
1031 C CB  . VAL A 136 ? 2.19901 2.53959 2.92643 -0.24782 -0.23317 0.41754  136 VAL B CB  
1032 C CG1 . VAL A 136 ? 2.22339 2.54484 2.95407 -0.23283 -0.23092 0.40868  136 VAL B CG1 
1033 C CG2 . VAL A 136 ? 2.20578 2.53142 2.87144 -0.24764 -0.23661 0.37132  136 VAL B CG2 
1034 N N   . ASN A 137 ? 2.35876 2.79922 3.11826 -0.22756 -0.21635 0.56021  137 ASN B N   
1035 C CA  . ASN A 137 ? 2.41668 2.84622 3.21139 -0.22588 -0.21485 0.62862  137 ASN B CA  
1036 C C   . ASN A 137 ? 2.46633 2.84019 3.29660 -0.20464 -0.23107 0.62388  137 ASN B C   
1037 O O   . ASN A 137 ? 2.47885 2.87980 3.28322 -0.17993 -0.24212 0.59774  137 ASN B O   
1038 C CB  . ASN A 137 ? 2.45318 2.95798 3.19281 -0.21397 -0.20671 0.67777  137 ASN B CB  
1039 C CG  . ASN A 137 ? 2.53733 3.02281 3.29231 -0.20641 -0.20829 0.76053  137 ASN B CG  
1040 O OD1 . ASN A 137 ? 2.55579 2.96343 3.37443 -0.21372 -0.20884 0.78476  137 ASN B OD1 
1041 N ND2 . ASN A 137 ? 2.59332 3.14472 3.28395 -0.19206 -0.20828 0.80453  137 ASN B ND2 
1042 N N   . ILE A 138 ? 2.36866 2.66745 3.26732 -0.21554 -0.22949 0.64293  138 ILE B N   
1043 C CA  . ILE A 138 ? 2.43315 2.67160 3.38368 -0.19040 -0.24023 0.64326  138 ILE B CA  
1044 C C   . ILE A 138 ? 2.52092 2.73082 3.49844 -0.17667 -0.23932 0.73471  138 ILE B C   
1045 O O   . ILE A 138 ? 2.53027 2.68453 3.54633 -0.20637 -0.22154 0.76962  138 ILE B O   
1046 C CB  . ILE A 138 ? 2.42723 2.58385 3.43464 -0.21185 -0.23509 0.58368  138 ILE B CB  
1047 C CG1 . ILE A 138 ? 2.38090 2.55388 3.34825 -0.21469 -0.23787 0.49923  138 ILE B CG1 
1048 C CG2 . ILE A 138 ? 2.52051 2.60038 3.60404 -0.18731 -0.23672 0.59876  138 ILE B CG2 
1049 C CD1 . ILE A 138 ? 2.31946 2.53412 3.22653 -0.23884 -0.23613 0.47488  138 ILE B CD1 
1050 N N   . TRP A 139 ? 2.57708 2.82633 3.53219 -0.13352 -0.25876 0.77479  139 TRP B N   
1051 C CA  . TRP A 139 ? 2.67120 2.88571 3.64038 -0.10828 -0.26529 0.87026  139 TRP B CA  
1052 C C   . TRP A 139 ? 2.74284 2.92691 3.77240 -0.05469 -0.29145 0.86692  139 TRP B C   
1053 O O   . TRP A 139 ? 2.71490 2.96109 3.74389 -0.03174 -0.30915 0.80631  139 TRP B O   
1054 C CB  . TRP A 139 ? 2.67753 2.98223 3.55514 -0.09885 -0.27174 0.93469  139 TRP B CB  
1055 C CG  . TRP A 139 ? 2.65772 3.06252 3.49156 -0.06332 -0.30222 0.90238  139 TRP B CG  
1056 C CD1 . TRP A 139 ? 2.70895 3.15376 3.53575 -0.01253 -0.33863 0.94615  139 TRP B CD1 
1057 C CD2 . TRP A 139 ? 2.57220 3.05079 3.36836 -0.07742 -0.29952 0.81673  139 TRP B CD2 
1058 N NE1 . TRP A 139 ? 2.65958 3.21059 3.45295 -0.00014 -0.35834 0.88477  139 TRP B NE1 
1059 C CE2 . TRP A 139 ? 2.57573 3.13970 3.34754 -0.04161 -0.33053 0.80584  139 TRP B CE2 
1060 C CE3 . TRP A 139 ? 2.49601 2.97473 3.27750 -0.11540 -0.27514 0.75029  139 TRP B CE3 
1061 C CZ2 . TRP A 139 ? 2.51189 3.15171 3.24730 -0.05092 -0.32983 0.72655  139 TRP B CZ2 
1062 C CZ3 . TRP A 139 ? 2.43353 2.97594 3.17171 -0.11693 -0.27608 0.68137  139 TRP B CZ3 
1063 C CH2 . TRP A 139 ? 2.44474 3.06263 3.16082 -0.08898 -0.29927 0.66784  139 TRP B CH2 
1064 N N   . SER A 140 ? 2.81229 2.89935 3.90148 -0.03500 -0.29043 0.93019  140 SER B N   
1065 C CA  . SER A 140 ? 2.89037 2.94449 4.05527 0.02478  -0.31480 0.92971  140 SER B CA  
1066 C C   . SER A 140 ? 2.92806 3.08032 4.04855 0.08172  -0.35757 0.98591  140 SER B C   
1067 O O   . SER A 140 ? 2.96711 3.13644 4.01741 0.08709  -0.36555 1.07989  140 SER B O   
1068 C CB  . SER A 140 ? 2.98107 2.88685 4.22734 0.03265  -0.29857 0.98235  140 SER B CB  
1069 O OG  . SER A 140 ? 3.08465 2.96612 4.39702 0.10688  -0.32787 1.01429  140 SER B OG  
1070 N N   . GLU A 141 ? 2.81257 3.03818 3.97124 0.12032  -0.38415 0.92426  141 GLU B N   
1071 C CA  . GLU A 141 ? 2.84965 3.18062 3.98619 0.17847  -0.43332 0.96858  141 GLU B CA  
1072 C C   . GLU A 141 ? 2.97631 3.23260 4.16371 0.24148  -0.45950 1.07243  141 GLU B C   
1073 O O   . GLU A 141 ? 3.03406 3.34643 4.15901 0.27880  -0.49743 1.16145  141 GLU B O   
1074 C CB  . GLU A 141 ? 2.78916 3.21875 3.97796 0.19969  -0.45091 0.86860  141 GLU B CB  
1075 C CG  . GLU A 141 ? 2.78699 3.35753 3.96203 0.25342  -0.50670 0.89286  141 GLU B CG  
1076 C CD  . GLU A 141 ? 2.89293 3.44231 4.16615 0.33678  -0.54874 0.95306  141 GLU B CD  
1077 O OE1 . GLU A 141 ? 2.95598 3.39504 4.33788 0.35487  -0.52852 0.93466  141 GLU B OE1 
1078 O OE2 . GLU A 141 ? 2.92392 3.56777 4.16497 0.38640  -0.60330 1.01770  141 GLU B OE2 
1079 N N   . ASN A 142 ? 2.87460 2.99871 4.16994 0.25455  -0.43913 1.06322  142 ASN B N   
1080 C CA  . ASN A 142 ? 3.01213 3.03383 4.36187 0.31516  -0.45671 1.16611  142 ASN B CA  
1081 C C   . ASN A 142 ? 3.07470 2.99670 4.34714 0.27822  -0.43020 1.27375  142 ASN B C   
1082 O O   . ASN A 142 ? 3.18678 3.07825 4.42216 0.32331  -0.45575 1.39413  142 ASN B O   
1083 C CB  . ASN A 142 ? 3.06630 2.97110 4.56342 0.33815  -0.43521 1.10964  142 ASN B CB  
1084 C CG  . ASN A 142 ? 3.21748 2.97299 4.77738 0.39214  -0.43905 1.21497  142 ASN B CG  
1085 O OD1 . ASN A 142 ? 3.26913 2.87141 4.90545 0.37121  -0.39611 1.19703  142 ASN B OD1 
1086 N ND2 . ASN A 142 ? 3.29718 3.09329 4.82306 0.46247  -0.49128 1.32455  142 ASN B ND2 
1087 N N   . ASP A 143 ? 3.16726 3.04154 4.41426 0.19582  -0.37884 1.23361  143 ASP B N   
1088 C CA  . ASP A 143 ? 3.20517 2.99821 4.39111 0.14596  -0.34276 1.31897  143 ASP B CA  
1089 C C   . ASP A 143 ? 3.10945 3.02200 4.17837 0.08929  -0.33053 1.30394  143 ASP B C   
1090 O O   . ASP A 143 ? 3.01555 2.94164 4.09012 0.02769  -0.29843 1.22262  143 ASP B O   
1091 C CB  . ASP A 143 ? 3.21741 2.85989 4.49062 0.09438  -0.29111 1.28279  143 ASP B CB  
1092 C CG  . ASP A 143 ? 3.32953 2.83714 4.72502 0.14842  -0.29384 1.29137  143 ASP B CG  
1093 O OD1 . ASP A 143 ? 3.40182 2.92776 4.81707 0.23246  -0.33784 1.34337  143 ASP B OD1 
1094 O OD2 . ASP A 143 ? 3.35158 2.73805 4.82810 0.10795  -0.25270 1.24269  143 ASP B OD2 
1095 N N   . PRO A 144 ? 2.97345 2.97703 3.93368 0.10968  -0.35578 1.37816  144 PRO B N   
1096 C CA  . PRO A 144 ? 2.89945 3.00632 3.75172 0.05409  -0.33436 1.36364  144 PRO B CA  
1097 C C   . PRO A 144 ? 2.89062 2.92194 3.73635 -0.01927 -0.27405 1.38708  144 PRO B C   
1098 O O   . PRO A 144 ? 2.80352 2.90970 3.60870 -0.07125 -0.24761 1.33532  144 PRO B O   
1099 C CB  . PRO A 144 ? 2.98105 3.17463 3.71897 0.09403  -0.37135 1.45488  144 PRO B CB  
1100 C CG  . PRO A 144 ? 3.11122 3.20736 3.89240 0.16177  -0.40312 1.55113  144 PRO B CG  
1101 C CD  . PRO A 144 ? 3.08452 3.11093 4.01425 0.18716  -0.40799 1.47238  144 PRO B CD  
1102 N N   . ALA A 145 ? 2.85395 2.73893 3.74731 -0.02490 -0.24978 1.46124  145 ALA B N   
1103 C CA  . ALA A 145 ? 2.88677 2.70016 3.79716 -0.10270 -0.18856 1.47231  145 ALA B CA  
1104 C C   . ALA A 145 ? 2.74097 2.55499 3.73836 -0.15021 -0.16947 1.34717  145 ALA B C   
1105 O O   . ALA A 145 ? 2.70438 2.53740 3.70374 -0.21768 -0.12954 1.32227  145 ALA B O   
1106 C CB  . ALA A 145 ? 3.08431 2.72360 4.03791 -0.10025 -0.16405 1.57181  145 ALA B CB  
1107 N N   . ASP A 146 ? 3.04532 2.84452 4.11484 -0.11602 -0.19741 1.26763  146 ASP B N   
1108 C CA  . ASP A 146 ? 2.94047 2.74018 4.07489 -0.15706 -0.18470 1.14975  146 ASP B CA  
1109 C C   . ASP A 146 ? 2.81982 2.76505 3.88816 -0.16615 -0.19854 1.07936  146 ASP B C   
1110 O O   . ASP A 146 ? 2.80657 2.82827 3.83798 -0.11992 -0.23245 1.05865  146 ASP B O   
1111 C CB  . ASP A 146 ? 2.97082 2.69476 4.19777 -0.11908 -0.20154 1.09201  146 ASP B CB  
1112 C CG  . ASP A 146 ? 2.93812 2.59607 4.24273 -0.17363 -0.17480 1.00025  146 ASP B CG  
1113 O OD1 . ASP A 146 ? 2.84276 2.57074 4.12073 -0.22344 -0.16599 0.94011  146 ASP B OD1 
1114 O OD2 . ASP A 146 ? 3.02352 2.56114 4.41637 -0.16432 -0.16430 0.98592  146 ASP B OD2 
1115 N N   . PHE A 147 ? 2.79733 2.78120 3.85768 -0.22498 -0.17170 1.04193  147 PHE B N   
1116 C CA  . PHE A 147 ? 2.68454 2.78764 3.69028 -0.23296 -0.18023 0.97497  147 PHE B CA  
1117 C C   . PHE A 147 ? 2.59713 2.70354 3.64538 -0.29064 -0.15816 0.91423  147 PHE B C   
1118 O O   . PHE A 147 ? 2.61674 2.67492 3.71286 -0.33516 -0.12862 0.94354  147 PHE B O   
1119 C CB  . PHE A 147 ? 2.68636 2.88973 3.59354 -0.22556 -0.17691 1.02885  147 PHE B CB  
1120 C CG  . PHE A 147 ? 2.71808 2.91300 3.61081 -0.26889 -0.13592 1.10108  147 PHE B CG  
1121 C CD1 . PHE A 147 ? 2.65199 2.90289 3.55642 -0.31949 -0.10490 1.06457  147 PHE B CD1 
1122 C CD2 . PHE A 147 ? 2.82631 2.95910 3.69511 -0.25806 -0.12679 1.20732  147 PHE B CD2 
1123 C CE1 . PHE A 147 ? 2.69825 2.95198 3.59955 -0.36475 -0.05962 1.12480  147 PHE B CE1 
1124 C CE2 . PHE A 147 ? 2.86495 2.98499 3.71374 -0.30535 -0.07988 1.27556  147 PHE B CE2 
1125 C CZ  . PHE A 147 ? 2.80898 2.99425 3.67817 -0.36194 -0.04325 1.23026  147 PHE B CZ  
1126 N N   . ARG A 148 ? 2.64899 2.81410 3.68003 -0.29015 -0.17336 0.83048  148 ARG B N   
1127 C CA  . ARG A 148 ? 2.57154 2.75066 3.63939 -0.33440 -0.16571 0.76805  148 ARG B CA  
1128 C C   . ARG A 148 ? 2.48801 2.76122 3.49451 -0.32268 -0.17833 0.71610  148 ARG B C   
1129 O O   . ARG A 148 ? 2.47195 2.76443 3.42740 -0.28642 -0.19575 0.69288  148 ARG B O   
1130 C CB  . ARG A 148 ? 2.58149 2.67445 3.71439 -0.34708 -0.17488 0.70662  148 ARG B CB  
1131 C CG  . ARG A 148 ? 2.67320 2.65551 3.88274 -0.36553 -0.15589 0.74497  148 ARG B CG  
1132 C CD  . ARG A 148 ? 2.69126 2.59365 3.96208 -0.38086 -0.16106 0.66838  148 ARG B CD  
1133 N NE  . ARG A 148 ? 2.79392 2.57528 4.14313 -0.39487 -0.13832 0.70203  148 ARG B NE  
1134 C CZ  . ARG A 148 ? 2.85234 2.54129 4.26568 -0.40586 -0.13400 0.64317  148 ARG B CZ  
1135 N NH1 . ARG A 148 ? 2.80783 2.51586 4.20795 -0.40691 -0.15113 0.54868  148 ARG B NH1 
1136 N NH2 . ARG A 148 ? 2.96492 2.53254 4.45248 -0.41716 -0.10789 0.67985  148 ARG B NH2 
1137 N N   . ILE A 149 ? 2.41984 2.75072 3.43955 -0.35322 -0.16784 0.69655  149 ILE B N   
1138 C CA  . ILE A 149 ? 2.36291 2.77021 3.33531 -0.34000 -0.17770 0.64903  149 ILE B CA  
1139 C C   . ILE A 149 ? 2.32497 2.71378 3.32797 -0.35575 -0.19911 0.57937  149 ILE B C   
1140 O O   . ILE A 149 ? 2.33136 2.70351 3.40553 -0.39359 -0.19757 0.56943  149 ILE B O   
1141 C CB  . ILE A 149 ? 2.35265 2.85098 3.32034 -0.35282 -0.15186 0.67619  149 ILE B CB  
1142 C CG1 . ILE A 149 ? 2.39191 2.92214 3.29378 -0.33337 -0.13386 0.73469  149 ILE B CG1 
1143 C CG2 . ILE A 149 ? 2.30418 2.86579 3.24941 -0.33850 -0.16252 0.62050  149 ILE B CG2 
1144 C CD1 . ILE A 149 ? 2.40315 2.94498 3.22880 -0.29216 -0.15353 0.70986  149 ILE B CD1 
1145 N N   . TYR A 150 ? 2.32100 2.71266 3.26542 -0.33032 -0.21835 0.53063  150 TYR B N   
1146 C CA  . TYR A 150 ? 2.30873 2.67850 3.25360 -0.34055 -0.24239 0.46857  150 TYR B CA  
1147 C C   . TYR A 150 ? 2.29127 2.72139 3.18882 -0.32128 -0.25240 0.44622  150 TYR B C   
1148 O O   . TYR A 150 ? 2.28728 2.72036 3.11469 -0.29168 -0.24778 0.44064  150 TYR B O   
1149 C CB  . TYR A 150 ? 2.32439 2.61862 3.23571 -0.32971 -0.25173 0.43036  150 TYR B CB  
1150 C CG  . TYR A 150 ? 2.35122 2.57587 3.31877 -0.33881 -0.24233 0.44498  150 TYR B CG  
1151 C CD1 . TYR A 150 ? 2.37021 2.59210 3.35562 -0.32261 -0.22736 0.50712  150 TYR B CD1 
1152 C CD2 . TYR A 150 ? 2.39174 2.55033 3.39169 -0.36143 -0.24865 0.39639  150 TYR B CD2 
1153 C CE1 . TYR A 150 ? 2.42757 2.57560 3.46834 -0.32189 -0.22049 0.52678  150 TYR B CE1 
1154 C CE2 . TYR A 150 ? 2.42724 2.51180 3.48826 -0.36531 -0.23581 0.40584  150 TYR B CE2 
1155 C CZ  . TYR A 150 ? 2.45718 2.53303 3.54220 -0.34217 -0.22247 0.47454  150 TYR B CZ  
1156 O OH  . TYR A 150 ? 2.53272 2.52531 3.68226 -0.33694 -0.21132 0.49155  150 TYR B OH  
1157 N N   . ASN A 151 ? 2.05787 2.53576 3.00046 -0.33729 -0.26641 0.43081  151 ASN B N   
1158 C CA  . ASN A 151 ? 2.06384 2.59357 2.97384 -0.31095 -0.28122 0.41080  151 ASN B CA  
1159 C C   . ASN A 151 ? 2.11537 2.58895 2.95562 -0.29882 -0.31191 0.36606  151 ASN B C   
1160 O O   . ASN A 151 ? 2.14548 2.58477 2.99985 -0.32420 -0.33359 0.33688  151 ASN B O   
1161 C CB  . ASN A 151 ? 2.05009 2.66813 3.04813 -0.32737 -0.28918 0.41039  151 ASN B CB  
1162 C CG  . ASN A 151 ? 2.02081 2.69704 3.08143 -0.34590 -0.24904 0.45471  151 ASN B CG  
1163 O OD1 . ASN A 151 ? 2.00985 2.76278 3.08176 -0.32805 -0.23119 0.46463  151 ASN B OD1 
1164 N ND2 . ASN A 151 ? 2.01095 2.64551 3.11011 -0.38181 -0.23068 0.48190  151 ASN B ND2 
1165 N N   . VAL A 152 ? 2.06586 2.52477 2.82467 -0.26384 -0.30937 0.35904  152 VAL B N   
1166 C CA  . VAL A 152 ? 2.13820 2.53550 2.81124 -0.25198 -0.33083 0.32522  152 VAL B CA  
1167 C C   . VAL A 152 ? 2.18494 2.60808 2.82132 -0.21358 -0.34115 0.32758  152 VAL B C   
1168 O O   . VAL A 152 ? 2.14280 2.61927 2.80773 -0.19350 -0.32054 0.34732  152 VAL B O   
1169 C CB  . VAL A 152 ? 2.14148 2.46298 2.74220 -0.25103 -0.30752 0.31189  152 VAL B CB  
1170 C CG1 . VAL A 152 ? 2.22998 2.47964 2.74361 -0.25430 -0.32285 0.27479  152 VAL B CG1 
1171 C CG2 . VAL A 152 ? 2.08606 2.39488 2.74266 -0.27346 -0.29187 0.32101  152 VAL B CG2 
1172 N N   . THR A 153 ? 2.26440 2.64543 2.83342 -0.20183 -0.37224 0.30747  153 THR B N   
1173 C CA  . THR A 153 ? 2.29750 2.67786 2.82040 -0.15705 -0.38445 0.31436  153 THR B CA  
1174 C C   . THR A 153 ? 2.39267 2.68358 2.79684 -0.14921 -0.40735 0.29945  153 THR B C   
1175 O O   . THR A 153 ? 2.44456 2.70868 2.79169 -0.10894 -0.42106 0.31058  153 THR B O   
1176 C CB  . THR A 153 ? 2.28341 2.76757 2.90116 -0.13922 -0.41612 0.32316  153 THR B CB  
1177 O OG1 . THR A 153 ? 2.30063 2.78158 2.88577 -0.08466 -0.42373 0.33301  153 THR B OG1 
1178 C CG2 . THR A 153 ? 2.34135 2.85011 2.98040 -0.16217 -0.46890 0.30335  153 THR B CG2 
1179 N N   . TYR A 154 ? 2.39386 2.63358 2.75792 -0.18655 -0.40849 0.27536  154 TYR B N   
1180 C CA  . TYR A 154 ? 2.50614 2.65962 2.74362 -0.18819 -0.42264 0.25922  154 TYR B CA  
1181 C C   . TYR A 154 ? 2.54612 2.61421 2.68459 -0.16681 -0.38438 0.26828  154 TYR B C   
1182 O O   . TYR A 154 ? 2.47931 2.54532 2.64247 -0.16840 -0.34017 0.26930  154 TYR B O   
1183 C CB  . TYR A 154 ? 2.52731 2.64305 2.74803 -0.23611 -0.41451 0.22249  154 TYR B CB  
1184 C CG  . TYR A 154 ? 2.49007 2.66936 2.79644 -0.26500 -0.45019 0.20379  154 TYR B CG  
1185 C CD1 . TYR A 154 ? 2.52277 2.76616 2.84860 -0.25318 -0.50604 0.20668  154 TYR B CD1 
1186 C CD2 . TYR A 154 ? 2.42181 2.59739 2.79651 -0.30376 -0.42834 0.18072  154 TYR B CD2 
1187 C CE1 . TYR A 154 ? 2.49932 2.80691 2.91082 -0.28832 -0.53673 0.18043  154 TYR B CE1 
1188 C CE2 . TYR A 154 ? 2.40372 2.62439 2.85981 -0.33658 -0.45440 0.15871  154 TYR B CE2 
1189 C CZ  . TYR A 154 ? 2.44551 2.73477 2.91984 -0.33332 -0.50732 0.15531  154 TYR B CZ  
1190 O OH  . TYR A 154 ? 2.42319 2.76359 2.98594 -0.37437 -0.53134 0.12465  154 TYR B OH  
1191 N N   . LEU A 155 ? 2.53122 2.52723 2.55253 -0.14879 -0.40230 0.27509  155 LEU B N   
1192 C CA  . LEU A 155 ? 2.57873 2.47609 2.50037 -0.13284 -0.36171 0.28474  155 LEU B CA  
1193 C C   . LEU A 155 ? 2.56939 2.41261 2.45626 -0.17674 -0.30609 0.25292  155 LEU B C   
1194 O O   . LEU A 155 ? 2.53434 2.34004 2.40481 -0.17601 -0.25872 0.24946  155 LEU B O   
1195 C CB  . LEU A 155 ? 2.73835 2.55343 2.52715 -0.10812 -0.39169 0.30591  155 LEU B CB  
1196 C CG  . LEU A 155 ? 2.77781 2.62317 2.58278 -0.04510 -0.44174 0.34474  155 LEU B CG  
1197 C CD1 . LEU A 155 ? 2.71980 2.54594 2.56011 -0.00534 -0.40371 0.36215  155 LEU B CD1 
1198 C CD2 . LEU A 155 ? 2.71088 2.69602 2.64044 -0.03837 -0.50109 0.34111  155 LEU B CD2 
1199 N N   . GLU A 156 ? 2.83467 2.67915 2.71819 -0.21571 -0.31023 0.22312  156 GLU B N   
1200 C CA  . GLU A 156 ? 2.80286 2.62477 2.69374 -0.25314 -0.26081 0.18752  156 GLU B CA  
1201 C C   . GLU A 156 ? 2.64223 2.55118 2.67214 -0.25415 -0.25348 0.18790  156 GLU B C   
1202 O O   . GLU A 156 ? 2.60516 2.57331 2.71813 -0.25974 -0.28319 0.19028  156 GLU B O   
1203 C CB  . GLU A 156 ? 2.93248 2.72244 2.77489 -0.29064 -0.26396 0.15051  156 GLU B CB  
1204 C CG  . GLU A 156 ? 2.90408 2.67477 2.76415 -0.32527 -0.21063 0.10697  156 GLU B CG  
1205 C CD  . GLU A 156 ? 2.93871 2.63691 2.70985 -0.33559 -0.15621 0.09739  156 GLU B CD  
1206 O OE1 . GLU A 156 ? 3.02649 2.65962 2.69348 -0.32051 -0.15722 0.12493  156 GLU B OE1 
1207 O OE2 . GLU A 156 ? 2.87491 2.58091 2.68615 -0.35882 -0.11155 0.06147  156 GLU B OE2 
1208 N N   . PRO A 157 ? 2.66325 2.58156 2.71781 -0.25139 -0.21519 0.18618  157 PRO B N   
1209 C CA  . PRO A 157 ? 2.53123 2.53411 2.70090 -0.24778 -0.21252 0.19640  157 PRO B CA  
1210 C C   . PRO A 157 ? 2.48099 2.49729 2.70936 -0.27233 -0.20406 0.17234  157 PRO B C   
1211 O O   . PRO A 157 ? 2.44709 2.46576 2.68889 -0.28142 -0.17352 0.15069  157 PRO B O   
1212 C CB  . PRO A 157 ? 2.49229 2.49683 2.64457 -0.23799 -0.17696 0.19515  157 PRO B CB  
1213 C CG  . PRO A 157 ? 2.58889 2.50269 2.62888 -0.23221 -0.16216 0.19086  157 PRO B CG  
1214 C CD  . PRO A 157 ? 2.69274 2.54540 2.66583 -0.25192 -0.17346 0.17693  157 PRO B CD  
1215 N N   . SER A 158 ? 2.66677 2.69549 2.94130 -0.28244 -0.23208 0.17240  158 SER B N   
1216 C CA  . SER A 158 ? 2.63147 2.65701 2.96696 -0.30210 -0.22317 0.14707  158 SER B CA  
1217 C C   . SER A 158 ? 2.59762 2.65437 3.01679 -0.30874 -0.25345 0.16293  158 SER B C   
1218 O O   . SER A 158 ? 2.60752 2.69161 3.02844 -0.30455 -0.28293 0.18294  158 SER B O   
1219 C CB  . SER A 158 ? 2.72895 2.68636 2.99000 -0.32748 -0.20370 0.09577  158 SER B CB  
1220 O OG  . SER A 158 ? 2.74951 2.69842 3.06948 -0.34664 -0.20618 0.06613  158 SER B OG  
1221 N N   . LEU A 159 ? 2.50954 2.56146 3.00628 -0.31930 -0.24395 0.15121  159 LEU B N   
1222 C CA  . LEU A 159 ? 2.47757 2.54411 3.06471 -0.33173 -0.26198 0.16534  159 LEU B CA  
1223 C C   . LEU A 159 ? 2.50629 2.52241 3.13843 -0.35004 -0.24706 0.12314  159 LEU B C   
1224 O O   . LEU A 159 ? 2.50903 2.50598 3.14486 -0.34063 -0.22075 0.10175  159 LEU B O   
1225 C CB  . LEU A 159 ? 2.39259 2.51243 3.05510 -0.31389 -0.26072 0.22406  159 LEU B CB  
1226 C CG  . LEU A 159 ? 2.37655 2.49238 3.14211 -0.32773 -0.26297 0.24676  159 LEU B CG  
1227 C CD1 . LEU A 159 ? 2.38855 2.52329 3.18185 -0.35530 -0.28553 0.24391  159 LEU B CD1 
1228 C CD2 . LEU A 159 ? 2.33324 2.48827 3.14373 -0.30603 -0.25306 0.30869  159 LEU B CD2 
1229 N N   . ARG A 160 ? 2.44766 2.44713 3.12347 -0.37718 -0.26216 0.10504  160 ARG B N   
1230 C CA  . ARG A 160 ? 2.49036 2.43356 3.21737 -0.39710 -0.24514 0.05733  160 ARG B CA  
1231 C C   . ARG A 160 ? 2.46574 2.40237 3.30700 -0.41011 -0.24997 0.08233  160 ARG B C   
1232 O O   . ARG A 160 ? 2.44434 2.41641 3.30475 -0.42869 -0.27309 0.10224  160 ARG B O   
1233 C CB  . ARG A 160 ? 2.58530 2.49404 3.23252 -0.43050 -0.25077 -0.01209 160 ARG B CB  
1234 C CG  . ARG A 160 ? 2.65350 2.54552 3.18354 -0.42362 -0.23277 -0.03744 160 ARG B CG  
1235 C CD  . ARG A 160 ? 2.78763 2.64082 3.21659 -0.45806 -0.23459 -0.10151 160 ARG B CD  
1236 N NE  . ARG A 160 ? 2.87017 2.69939 3.17831 -0.45406 -0.21022 -0.11391 160 ARG B NE  
1237 C CZ  . ARG A 160 ? 3.00728 2.79858 3.18715 -0.48028 -0.20661 -0.15582 160 ARG B CZ  
1238 N NH1 . ARG A 160 ? 3.08829 2.87131 3.23881 -0.51169 -0.23178 -0.19608 160 ARG B NH1 
1239 N NH2 . ARG A 160 ? 3.07544 2.83587 3.14863 -0.47896 -0.17539 -0.15853 160 ARG B NH2 
1240 N N   . ILE A 161 ? 2.43769 2.32799 3.36016 -0.39981 -0.22600 0.08126  161 ILE B N   
1241 C CA  . ILE A 161 ? 2.44810 2.30491 3.47897 -0.41163 -0.22153 0.10927  161 ILE B CA  
1242 C C   . ILE A 161 ? 2.51987 2.29548 3.61658 -0.40927 -0.19397 0.06297  161 ILE B C   
1243 O O   . ILE A 161 ? 2.54036 2.30765 3.61781 -0.38469 -0.17698 0.03054  161 ILE B O   
1244 C CB  . ILE A 161 ? 2.40106 2.29383 3.47109 -0.38108 -0.22246 0.20153  161 ILE B CB  
1245 C CG1 . ILE A 161 ? 2.43306 2.28666 3.59851 -0.40408 -0.21500 0.23993  161 ILE B CG1 
1246 C CG2 . ILE A 161 ? 2.39794 2.28901 3.47775 -0.33232 -0.21008 0.22305  161 ILE B CG2 
1247 C CD1 . ILE A 161 ? 2.41111 2.29529 3.58465 -0.45474 -0.22924 0.22323  161 ILE B CD1 
1248 N N   . ALA A 162 ? 2.36642 2.08149 3.54944 -0.43697 -0.18521 0.05468  162 ALA B N   
1249 C CA  . ALA A 162 ? 2.45189 2.07667 3.71184 -0.43395 -0.15504 0.00631  162 ALA B CA  
1250 C C   . ALA A 162 ? 2.50088 2.05445 3.87474 -0.44002 -0.14228 0.05347  162 ALA B C   
1251 O O   . ALA A 162 ? 2.57745 2.04983 4.01554 -0.47438 -0.12240 -0.00045 162 ALA B O   
1252 C CB  . ALA A 162 ? 2.49599 2.09084 3.71740 -0.48028 -0.14678 -0.10204 162 ALA B CB  
1253 N N   . ALA A 163 ? 2.22653 1.80359 3.62065 -0.40966 -0.14973 0.15343  163 ALA B N   
1254 C CA  . ALA A 163 ? 2.30506 1.81144 3.78881 -0.41770 -0.13488 0.21758  163 ALA B CA  
1255 C C   . ALA A 163 ? 2.41658 1.79855 3.99971 -0.39848 -0.10519 0.19559  163 ALA B C   
1256 O O   . ALA A 163 ? 2.41443 1.78643 4.01358 -0.34337 -0.10079 0.18559  163 ALA B O   
1257 C CB  . ALA A 163 ? 2.26614 1.82116 3.73155 -0.37792 -0.14567 0.33038  163 ALA B CB  
1258 N N   . GLY A 169 ? 2.78535 2.08984 4.74557 0.08465  -0.14308 0.44675  169 GLY B N   
1259 C CA  . GLY A 169 ? 2.89069 2.15729 4.93612 0.17461  -0.16512 0.53502  169 GLY B CA  
1260 C C   . GLY A 169 ? 2.85260 2.22952 4.82040 0.21317  -0.21589 0.64507  169 GLY B C   
1261 O O   . GLY A 169 ? 2.88722 2.31465 4.90532 0.29647  -0.25114 0.69082  169 GLY B O   
1262 N N   . ILE A 170 ? 3.20219 2.62410 5.04962 0.15287  -0.22049 0.68326  170 ILE B N   
1263 C CA  . ILE A 170 ? 3.16649 2.69833 4.92118 0.17560  -0.26178 0.77615  170 ILE B CA  
1264 C C   . ILE A 170 ? 3.07257 2.76652 4.77212 0.17027  -0.27934 0.70078  170 ILE B C   
1265 O O   . ILE A 170 ? 3.05759 2.76468 4.78317 0.14566  -0.25614 0.58895  170 ILE B O   
1266 C CB  . ILE A 170 ? 3.13244 2.63439 4.79436 0.11234  -0.24896 0.84707  170 ILE B CB  
1267 C CG1 . ILE A 170 ? 3.22018 2.54429 4.94804 0.08713  -0.21175 0.88117  170 ILE B CG1 
1268 C CG2 . ILE A 170 ? 3.15124 2.72465 4.73173 0.14742  -0.28499 0.96588  170 ILE B CG2 
1269 C CD1 . ILE A 170 ? 3.17233 2.47121 4.83012 0.00981  -0.18774 0.92788  170 ILE B CD1 
1270 N N   . SER A 171 ? 3.10915 2.92264 4.72830 0.18987  -0.31642 0.75863  171 SER B N   
1271 C CA  . SER A 171 ? 3.01042 2.97118 4.57025 0.17719  -0.32920 0.69217  171 SER B CA  
1272 C C   . SER A 171 ? 2.92731 2.94675 4.35524 0.12606  -0.33096 0.72736  171 SER B C   
1273 O O   . SER A 171 ? 2.94230 2.97499 4.31789 0.14029  -0.35070 0.82687  171 SER B O   
1274 C CB  . SER A 171 ? 3.02172 3.09560 4.62550 0.25205  -0.37338 0.70531  171 SER B CB  
1275 O OG  . SER A 171 ? 3.07418 3.17776 4.63282 0.29301  -0.41482 0.82437  171 SER B OG  
1276 N N   . TYR A 172 ? 2.82850 2.88171 4.20065 0.06908  -0.30871 0.64666  172 TYR B N   
1277 C CA  . TYR A 172 ? 2.74240 2.83968 4.00578 0.01986  -0.30318 0.66531  172 TYR B CA  
1278 C C   . TYR A 172 ? 2.64587 2.86866 3.84050 0.01601  -0.31416 0.61728  172 TYR B C   
1279 O O   . TYR A 172 ? 2.61856 2.88403 3.84730 0.03118  -0.31524 0.54716  172 TYR B O   
1280 C CB  . TYR A 172 ? 2.69222 2.71518 3.94596 -0.04368 -0.27018 0.61885  172 TYR B CB  
1281 C CG  . TYR A 172 ? 2.74435 2.64897 4.05289 -0.05932 -0.25358 0.66790  172 TYR B CG  
1282 C CD1 . TYR A 172 ? 2.81058 2.61200 4.21840 -0.04423 -0.24035 0.64046  172 TYR B CD1 
1283 C CD2 . TYR A 172 ? 2.71857 2.61291 3.98499 -0.09392 -0.24441 0.73469  172 TYR B CD2 
1284 C CE1 . TYR A 172 ? 2.86113 2.54229 4.32278 -0.06450 -0.21959 0.67997  172 TYR B CE1 
1285 C CE2 . TYR A 172 ? 2.77461 2.55753 4.09567 -0.11760 -0.22238 0.77615  172 TYR B CE2 
1286 C CZ  . TYR A 172 ? 2.84344 2.51496 4.26091 -0.10384 -0.21048 0.74884  172 TYR B CZ  
1287 O OH  . TYR A 172 ? 2.90833 2.45733 4.38387 -0.13272 -0.18342 0.78507  172 TYR B OH  
1288 N N   . ARG A 173 ? 2.66714 2.94701 3.76866 -0.00778 -0.31646 0.65197  173 ARG B N   
1289 C CA  . ARG A 173 ? 2.56768 2.94682 3.59411 -0.02394 -0.31724 0.60353  173 ARG B CA  
1290 C C   . ARG A 173 ? 2.48848 2.84332 3.45484 -0.07737 -0.29017 0.57277  173 ARG B C   
1291 O O   . ARG A 173 ? 2.48681 2.76783 3.47202 -0.10257 -0.27595 0.59000  173 ARG B O   
1292 C CB  . ARG A 173 ? 2.59123 3.06977 3.55875 -0.00067 -0.34389 0.66261  173 ARG B CB  
1293 C CG  . ARG A 173 ? 2.64376 3.18928 3.65910 0.05558  -0.38214 0.67640  173 ARG B CG  
1294 C CD  . ARG A 173 ? 2.64013 3.31255 3.57336 0.06208  -0.40683 0.69565  173 ARG B CD  
1295 N NE  . ARG A 173 ? 2.72498 3.44898 3.66893 0.11752  -0.45368 0.77371  173 ARG B NE  
1296 C CZ  . ARG A 173 ? 2.74466 3.55332 3.59786 0.12323  -0.47704 0.82831  173 ARG B CZ  
1297 N NH1 . ARG A 173 ? 2.70350 3.55441 3.45870 0.07698  -0.45267 0.80800  173 ARG B NH1 
1298 N NH2 . ARG A 173 ? 2.82741 3.67955 3.68600 0.17909  -0.52623 0.90467  173 ARG B NH2 
1299 N N   . ALA A 174 ? 2.51354 2.93254 3.41289 -0.09382 -0.28389 0.52530  174 ALA B N   
1300 C CA  . ALA A 174 ? 2.44485 2.84716 3.28810 -0.13322 -0.26332 0.49806  174 ALA B CA  
1301 C C   . ALA A 174 ? 2.40323 2.88267 3.16941 -0.13908 -0.25841 0.47226  174 ALA B C   
1302 O O   . ALA A 174 ? 2.40030 2.93054 3.16090 -0.12693 -0.26347 0.43598  174 ALA B O   
1303 C CB  . ALA A 174 ? 2.41505 2.74676 3.27498 -0.15579 -0.24852 0.42992  174 ALA B CB  
1304 N N   . ARG A 175 ? 2.27890 2.76803 2.99556 -0.15921 -0.24578 0.48503  175 ARG B N   
1305 C CA  . ARG A 175 ? 2.25459 2.79895 2.90064 -0.16657 -0.23357 0.45580  175 ARG B CA  
1306 C C   . ARG A 175 ? 2.21662 2.73670 2.83927 -0.18612 -0.21765 0.45375  175 ARG B C   
1307 O O   . ARG A 175 ? 2.20640 2.70997 2.86246 -0.19433 -0.21820 0.49535  175 ARG B O   
1308 C CB  . ARG A 175 ? 2.29392 2.92676 2.90704 -0.15235 -0.24220 0.49496  175 ARG B CB  
1309 C CG  . ARG A 175 ? 2.32376 2.97561 2.92079 -0.15794 -0.23511 0.56221  175 ARG B CG  
1310 C CD  . ARG A 175 ? 2.35426 3.09883 2.89182 -0.14876 -0.23964 0.59040  175 ARG B CD  
1311 N NE  . ARG A 175 ? 2.42345 3.17330 2.96411 -0.13988 -0.24875 0.67855  175 ARG B NE  
1312 C CZ  . ARG A 175 ? 2.43183 3.17463 2.96176 -0.15924 -0.22470 0.72607  175 ARG B CZ  
1313 N NH1 . ARG A 175 ? 2.36310 3.10956 2.88736 -0.18255 -0.19504 0.69196  175 ARG B NH1 
1314 N NH2 . ARG A 175 ? 2.50763 3.23865 3.03691 -0.15421 -0.22896 0.81115  175 ARG B NH2 
1315 N N   . VAL A 176 ? 2.16690 2.68301 2.73950 -0.19314 -0.20307 0.40446  176 VAL B N   
1316 C CA  . VAL A 176 ? 2.13987 2.63023 2.69728 -0.20194 -0.19435 0.39628  176 VAL B CA  
1317 C C   . VAL A 176 ? 2.15841 2.69635 2.66626 -0.19705 -0.17458 0.38605  176 VAL B C   
1318 O O   . VAL A 176 ? 2.19201 2.75248 2.65842 -0.19532 -0.16338 0.35501  176 VAL B O   
1319 C CB  . VAL A 176 ? 2.13195 2.54608 2.67244 -0.21009 -0.19595 0.34953  176 VAL B CB  
1320 C CG1 . VAL A 176 ? 2.15023 2.54900 2.63393 -0.21125 -0.17865 0.30020  176 VAL B CG1 
1321 C CG2 . VAL A 176 ? 2.12599 2.52286 2.65779 -0.21162 -0.19947 0.35040  176 VAL B CG2 
1322 N N   . ARG A 177 ? 2.02422 2.58270 2.54563 -0.19667 -0.16778 0.40652  177 ARG B N   
1323 C CA  . ARG A 177 ? 2.04182 2.63391 2.52899 -0.18807 -0.14457 0.38845  177 ARG B CA  
1324 C C   . ARG A 177 ? 2.02958 2.59632 2.54136 -0.18063 -0.14898 0.38268  177 ARG B C   
1325 O O   . ARG A 177 ? 2.01587 2.57317 2.57932 -0.18912 -0.16845 0.40329  177 ARG B O   
1326 C CB  . ARG A 177 ? 2.04408 2.72215 2.52964 -0.19013 -0.12712 0.42149  177 ARG B CB  
1327 C CG  . ARG A 177 ? 2.01680 2.72804 2.55894 -0.19821 -0.12292 0.46609  177 ARG B CG  
1328 C CD  . ARG A 177 ? 2.02527 2.82093 2.54754 -0.20145 -0.09065 0.48371  177 ARG B CD  
1329 N NE  . ARG A 177 ? 2.01265 2.84483 2.59112 -0.21821 -0.07896 0.53090  177 ARG B NE  
1330 C CZ  . ARG A 177 ? 2.02389 2.92430 2.58506 -0.23138 -0.04929 0.56622  177 ARG B CZ  
1331 N NH1 . ARG A 177 ? 2.04658 2.99356 2.53055 -0.22751 -0.03323 0.55827  177 ARG B NH1 
1332 N NH2 . ARG A 177 ? 2.00844 2.93380 2.62773 -0.25383 -0.03270 0.60726  177 ARG B NH2 
1333 N N   . ALA A 178 ? 2.03271 2.58808 2.51070 -0.16363 -0.13256 0.35201  178 ALA B N   
1334 C CA  . ALA A 178 ? 2.04535 2.57549 2.54219 -0.14545 -0.14415 0.34592  178 ALA B CA  
1335 C C   . ALA A 178 ? 2.06197 2.64056 2.56960 -0.12249 -0.11723 0.33675  178 ALA B C   
1336 O O   . ALA A 178 ? 2.09497 2.71353 2.57843 -0.12532 -0.08544 0.32584  178 ALA B O   
1337 C CB  . ALA A 178 ? 2.08692 2.51825 2.52419 -0.13841 -0.15484 0.31733  178 ALA B CB  
1338 N N   . TRP A 179 ? 1.96482 2.54541 2.51155 -0.09791 -0.13143 0.33700  179 TRP B N   
1339 C CA  . TRP A 179 ? 1.98309 2.60295 2.55268 -0.06644 -0.10518 0.32173  179 TRP B CA  
1340 C C   . TRP A 179 ? 1.99029 2.59064 2.59511 -0.02916 -0.13586 0.32142  179 TRP B C   
1341 O O   . TRP A 179 ? 1.95813 2.57703 2.60793 -0.03652 -0.17575 0.33920  179 TRP B O   
1342 C CB  . TRP A 179 ? 1.93664 2.67106 2.56788 -0.07970 -0.07724 0.33726  179 TRP B CB  
1343 C CG  . TRP A 179 ? 1.88274 2.69136 2.61506 -0.08266 -0.09402 0.36018  179 TRP B CG  
1344 C CD1 . TRP A 179 ? 1.85202 2.66723 2.62595 -0.11228 -0.12437 0.38732  179 TRP B CD1 
1345 C CD2 . TRP A 179 ? 1.86393 2.76029 2.67986 -0.05998 -0.07518 0.35123  179 TRP B CD2 
1346 N NE1 . TRP A 179 ? 1.81847 2.72048 2.69587 -0.11433 -0.12733 0.39444  179 TRP B NE1 
1347 C CE2 . TRP A 179 ? 1.81707 2.77699 2.72584 -0.08088 -0.09792 0.37312  179 TRP B CE2 
1348 C CE3 . TRP A 179 ? 1.89397 2.82215 2.72381 -0.02396 -0.03851 0.32074  179 TRP B CE3 
1349 C CZ2 . TRP A 179 ? 1.78755 2.85479 2.80770 -0.06856 -0.08621 0.36557  179 TRP B CZ2 
1350 C CZ3 . TRP A 179 ? 1.85449 2.88472 2.79464 -0.00540 -0.02624 0.31439  179 TRP B CZ3 
1351 C CH2 . TRP A 179 ? 1.80130 2.90607 2.83804 -0.02811 -0.05099 0.33675  179 TRP B CH2 
1352 N N   . ALA A 180 ? 1.96706 2.52723 2.54965 0.01162  -0.11850 0.29951  180 ALA B N   
1353 C CA  . ALA A 180 ? 2.00564 2.54183 2.61446 0.06094  -0.15008 0.30340  180 ALA B CA  
1354 C C   . ALA A 180 ? 1.95549 2.62243 2.69002 0.07857  -0.15605 0.30964  180 ALA B C   
1355 O O   . ALA A 180 ? 1.95580 2.69037 2.73725 0.08913  -0.11134 0.29294  180 ALA B O   
1356 C CB  . ALA A 180 ? 2.11068 2.55290 2.66197 0.10179  -0.12177 0.28099  180 ALA B CB  
1357 N N   . GLN A 181 ? 2.02572 2.73433 2.81723 0.07882  -0.20861 0.32712  181 GLN B N   
1358 C CA  . GLN A 181 ? 1.96195 2.81220 2.88749 0.07696  -0.21231 0.32954  181 GLN B CA  
1359 C C   . GLN A 181 ? 1.97662 2.87915 2.97677 0.14215  -0.20433 0.31285  181 GLN B C   
1360 O O   . GLN A 181 ? 1.93092 2.93558 3.01559 0.14358  -0.15975 0.29815  181 GLN B O   
1361 C CB  . GLN A 181 ? 1.96028 2.84567 2.93374 0.05730  -0.27349 0.34198  181 GLN B CB  
1362 C CG  . GLN A 181 ? 1.91996 2.95996 3.04456 0.04488  -0.27097 0.33845  181 GLN B CG  
1363 C CD  . GLN A 181 ? 1.89970 2.98511 3.04777 -0.01838 -0.22149 0.35011  181 GLN B CD  
1364 O OE1 . GLN A 181 ? 1.88703 2.89290 2.94846 -0.05354 -0.21071 0.36445  181 GLN B OE1 
1365 N NE2 . GLN A 181 ? 1.90142 3.11010 3.15839 -0.02767 -0.18486 0.34512  181 GLN B NE2 
1366 N N   . ALA A 182 ? 2.00681 2.83789 2.97508 0.19864  -0.24591 0.31634  182 ALA B N   
1367 C CA  . ALA A 182 ? 2.03586 2.91303 3.08821 0.27356  -0.25237 0.30601  182 ALA B CA  
1368 C C   . ALA A 182 ? 2.07592 2.93198 3.12583 0.30001  -0.17942 0.27764  182 ALA B C   
1369 O O   . ALA A 182 ? 2.09216 3.01576 3.24369 0.35759  -0.16721 0.25986  182 ALA B O   
1370 C CB  . ALA A 182 ? 2.13004 2.90937 3.12144 0.33144  -0.31581 0.32714  182 ALA B CB  
1371 N N   . TYR A 183 ? 2.07664 2.85025 3.02150 0.25963  -0.13057 0.26673  183 TYR B N   
1372 C CA  . TYR A 183 ? 2.14445 2.88998 3.07251 0.27777  -0.06105 0.22988  183 TYR B CA  
1373 C C   . TYR A 183 ? 2.08644 2.94856 3.05508 0.23084  -0.00162 0.20792  183 TYR B C   
1374 O O   . TYR A 183 ? 2.16144 3.01812 3.11507 0.23875  0.06004  0.16882  183 TYR B O   
1375 C CB  . TYR A 183 ? 2.24332 2.82405 3.02671 0.26442  -0.04279 0.22225  183 TYR B CB  
1376 C CG  . TYR A 183 ? 2.36485 2.81731 3.11636 0.33312  -0.04713 0.21999  183 TYR B CG  
1377 C CD1 . TYR A 183 ? 2.45588 2.90305 3.25871 0.38470  0.00166  0.18419  183 TYR B CD1 
1378 C CD2 . TYR A 183 ? 2.39789 2.72800 3.06450 0.34717  -0.09672 0.25484  183 TYR B CD2 
1379 C CE1 . TYR A 183 ? 2.58469 2.89686 3.36001 0.45243  -0.00050 0.18788  183 TYR B CE1 
1380 C CE2 . TYR A 183 ? 2.52493 2.72246 3.15022 0.41114  -0.09974 0.26390  183 TYR B CE2 
1381 C CZ  . TYR A 183 ? 2.61781 2.80162 3.30061 0.46583  -0.05260 0.23285  183 TYR B CZ  
1382 O OH  . TYR A 183 ? 2.76176 2.79577 3.40412 0.53391  -0.05396 0.24744  183 TYR B OH  
1383 N N   . ASN A 184 ? 1.97774 2.93887 2.99110 0.18057  -0.01583 0.23153  184 ASN B N   
1384 C CA  . ASN A 184 ? 1.92088 2.99291 2.96600 0.13381  0.03906  0.22368  184 ASN B CA  
1385 C C   . ASN A 184 ? 1.97451 2.98954 2.89989 0.10087  0.08622  0.20539  184 ASN B C   
1386 O O   . ASN A 184 ? 2.02914 3.07716 2.94999 0.10722  0.14599  0.16629  184 ASN B O   
1387 C CB  . ASN A 184 ? 1.91562 3.11006 3.08922 0.16946  0.07918  0.19315  184 ASN B CB  
1388 C CG  . ASN A 184 ? 1.85289 3.18236 3.07920 0.11366  0.12632  0.19794  184 ASN B CG  
1389 O OD1 . ASN A 184 ? 1.80730 3.14876 3.00851 0.05580  0.11012  0.23660  184 ASN B OD1 
1390 N ND2 . ASN A 184 ? 1.87471 3.30022 3.17257 0.13043  0.18974  0.15894  184 ASN B ND2 
1391 N N   . THR A 185 ? 2.02683 2.96330 2.85940 0.06467  0.05703  0.22911  185 THR B N   
1392 C CA  . THR A 185 ? 2.09121 2.97524 2.81279 0.03373  0.08590  0.21148  185 THR B CA  
1393 C C   . THR A 185 ? 2.02799 2.98700 2.72725 -0.02274 0.09690  0.24005  185 THR B C   
1394 O O   . THR A 185 ? 1.94317 2.96349 2.70245 -0.04366 0.07944  0.27945  185 THR B O   
1395 C CB  . THR A 185 ? 2.14802 2.89773 2.78534 0.03358  0.05033  0.21446  185 THR B CB  
1396 O OG1 . THR A 185 ? 2.06874 2.81617 2.69453 -0.00270 0.00811  0.25510  185 THR B OG1 
1397 C CG2 . THR A 185 ? 2.16536 2.83555 2.82381 0.08904  0.02341  0.21183  185 THR B CG2 
1398 N N   . THR A 186 ? 1.98546 2.93837 2.59681 -0.04772 0.12634  0.21960  186 THR B N   
1399 C CA  . THR A 186 ? 1.94374 2.95492 2.51298 -0.09454 0.12953  0.25380  186 THR B CA  
1400 C C   . THR A 186 ? 1.93070 2.87122 2.45936 -0.11259 0.07881  0.28532  186 THR B C   
1401 O O   . THR A 186 ? 1.99659 2.85155 2.47747 -0.10402 0.06406  0.25826  186 THR B O   
1402 C CB  . THR A 186 ? 2.00853 3.06048 2.49793 -0.11180 0.17588  0.21569  186 THR B CB  
1403 O OG1 . THR A 186 ? 2.04552 3.16759 2.57694 -0.09661 0.23108  0.18029  186 THR B OG1 
1404 C CG2 . THR A 186 ? 1.99229 3.10232 2.42476 -0.15380 0.16978  0.26131  186 THR B CG2 
1405 N N   . TRP A 187 ? 1.89902 2.87132 2.45141 -0.13885 0.05791  0.34016  187 TRP B N   
1406 C CA  . TRP A 187 ? 1.87158 2.78243 2.40429 -0.15343 0.01301  0.37007  187 TRP B CA  
1407 C C   . TRP A 187 ? 1.91280 2.78328 2.36078 -0.15785 0.00887  0.34173  187 TRP B C   
1408 O O   . TRP A 187 ? 1.93187 2.85665 2.32569 -0.17184 0.02925  0.33582  187 TRP B O   
1409 C CB  . TRP A 187 ? 1.83115 2.78691 2.38515 -0.18357 0.00792  0.43168  187 TRP B CB  
1410 C CG  . TRP A 187 ? 1.79083 2.73611 2.43319 -0.19207 -0.01482 0.46256  187 TRP B CG  
1411 C CD1 . TRP A 187 ? 1.77568 2.78558 2.48551 -0.21329 0.00557  0.49472  187 TRP B CD1 
1412 C CD2 . TRP A 187 ? 1.77549 2.64598 2.44658 -0.18651 -0.05869 0.45787  187 TRP B CD2 
1413 N NE1 . TRP A 187 ? 1.75142 2.73392 2.53752 -0.22256 -0.02562 0.50646  187 TRP B NE1 
1414 C CE2 . TRP A 187 ? 1.75052 2.64842 2.50925 -0.20514 -0.06690 0.48372  187 TRP B CE2 
1415 C CE3 . TRP A 187 ? 1.79274 2.57833 2.42106 -0.17258 -0.08747 0.43061  187 TRP B CE3 
1416 C CZ2 . TRP A 187 ? 1.74138 2.58787 2.54169 -0.20905 -0.10754 0.47920  187 TRP B CZ2 
1417 C CZ3 . TRP A 187 ? 1.78364 2.51525 2.44557 -0.17530 -0.12409 0.43119  187 TRP B CZ3 
1418 C CH2 . TRP A 187 ? 1.75827 2.52193 2.50343 -0.19265 -0.13622 0.45339  187 TRP B CH2 
1419 N N   . SER A 188 ? 1.98444 2.76644 2.41912 -0.14900 -0.01630 0.32068  188 SER B N   
1420 C CA  . SER A 188 ? 2.03247 2.77968 2.40143 -0.15813 -0.01573 0.28472  188 SER B CA  
1421 C C   . SER A 188 ? 2.01139 2.80126 2.36327 -0.17863 -0.03675 0.31607  188 SER B C   
1422 O O   . SER A 188 ? 1.96153 2.77463 2.34929 -0.18430 -0.05467 0.37107  188 SER B O   
1423 C CB  . SER A 188 ? 2.04903 2.69020 2.40754 -0.15063 -0.03307 0.26176  188 SER B CB  
1424 O OG  . SER A 188 ? 1.99050 2.60674 2.36855 -0.16193 -0.06848 0.29143  188 SER B OG  
1425 N N   . GLU A 189 ? 2.18699 2.98644 2.48827 -0.18910 -0.03468 0.27950  189 GLU B N   
1426 C CA  . GLU A 189 ? 2.17868 3.02598 2.46819 -0.19951 -0.06220 0.30629  189 GLU B CA  
1427 C C   . GLU A 189 ? 2.14543 2.93140 2.47892 -0.19629 -0.09628 0.32885  189 GLU B C   
1428 O O   . GLU A 189 ? 2.15006 2.85838 2.49128 -0.19552 -0.09621 0.29642  189 GLU B O   
1429 C CB  . GLU A 189 ? 2.24183 3.13057 2.47834 -0.21271 -0.05536 0.25006  189 GLU B CB  
1430 C CG  . GLU A 189 ? 2.29274 3.25494 2.47733 -0.22098 -0.02163 0.22270  189 GLU B CG  
1431 C CD  . GLU A 189 ? 2.27514 3.29967 2.45852 -0.21775 -0.01497 0.28495  189 GLU B CD  
1432 O OE1 . GLU A 189 ? 2.28188 3.37255 2.43736 -0.22258 -0.03796 0.33145  189 GLU B OE1 
1433 O OE2 . GLU A 189 ? 2.25988 3.26898 2.47153 -0.20996 0.01415  0.28885  189 GLU B OE2 
1434 N N   . TRP A 190 ? 2.29936 3.11469 2.65700 -0.19435 -0.12216 0.38569  190 TRP B N   
1435 C CA  . TRP A 190 ? 2.27477 3.03216 2.68311 -0.19007 -0.15016 0.40490  190 TRP B CA  
1436 C C   . TRP A 190 ? 2.29104 3.03442 2.69366 -0.19163 -0.15971 0.35358  190 TRP B C   
1437 O O   . TRP A 190 ? 2.32721 3.13626 2.70018 -0.19431 -0.16190 0.32907  190 TRP B O   
1438 C CB  . TRP A 190 ? 2.28345 3.06774 2.71907 -0.18425 -0.17149 0.47785  190 TRP B CB  
1439 C CG  . TRP A 190 ? 2.26539 3.04757 2.72476 -0.19219 -0.15746 0.52945  190 TRP B CG  
1440 C CD1 . TRP A 190 ? 2.26709 3.11346 2.69396 -0.19983 -0.13346 0.55804  190 TRP B CD1 
1441 C CD2 . TRP A 190 ? 2.23775 2.95801 2.76225 -0.19939 -0.16230 0.55151  190 TRP B CD2 
1442 N NE1 . TRP A 190 ? 2.24927 3.07957 2.72499 -0.21231 -0.12039 0.59805  190 TRP B NE1 
1443 C CE2 . TRP A 190 ? 2.23131 2.98587 2.76951 -0.21300 -0.14040 0.59348  190 TRP B CE2 
1444 C CE3 . TRP A 190 ? 2.21731 2.86158 2.78915 -0.20005 -0.18021 0.53389  190 TRP B CE3 
1445 C CZ2 . TRP A 190 ? 2.21518 2.93454 2.82217 -0.22917 -0.13855 0.61612  190 TRP B CZ2 
1446 C CZ3 . TRP A 190 ? 2.19520 2.80179 2.82523 -0.21467 -0.18101 0.55533  190 TRP B CZ3 
1447 C CH2 . TRP A 190 ? 2.19516 2.84111 2.84694 -0.22994 -0.16171 0.59521  190 TRP B CH2 
1448 N N   . SER A 191 ? 2.26697 2.93166 2.69818 -0.19390 -0.16359 0.33241  191 SER B N   
1449 C CA  . SER A 191 ? 2.27654 2.92599 2.71044 -0.20087 -0.16387 0.28054  191 SER B CA  
1450 C C   . SER A 191 ? 2.27161 2.98729 2.74587 -0.18800 -0.19276 0.29958  191 SER B C   
1451 O O   . SER A 191 ? 2.28184 3.02392 2.77949 -0.17159 -0.21433 0.36306  191 SER B O   
1452 C CB  . SER A 191 ? 2.25598 2.80930 2.70606 -0.20743 -0.16012 0.26112  191 SER B CB  
1453 O OG  . SER A 191 ? 2.22222 2.76179 2.73318 -0.19847 -0.18307 0.29165  191 SER B OG  
1454 N N   . PRO A 192 ? 2.28466 3.02992 2.77045 -0.19447 -0.19287 0.24647  192 PRO B N   
1455 C CA  . PRO A 192 ? 2.30637 3.12194 2.84810 -0.17371 -0.22663 0.26079  192 PRO B CA  
1456 C C   . PRO A 192 ? 2.30784 3.06960 2.91492 -0.15124 -0.24598 0.31066  192 PRO B C   
1457 O O   . PRO A 192 ? 2.29200 2.96294 2.91225 -0.16144 -0.23020 0.30090  192 PRO B O   
1458 C CB  . PRO A 192 ? 2.28092 3.11522 2.84337 -0.19219 -0.21212 0.17934  192 PRO B CB  
1459 C CG  . PRO A 192 ? 2.28621 3.09727 2.77632 -0.22434 -0.17397 0.13058  192 PRO B CG  
1460 C CD  . PRO A 192 ? 2.29173 3.02025 2.74041 -0.22158 -0.16036 0.17082  192 PRO B CD  
1461 N N   . SER A 193 ? 2.29432 3.11021 2.93886 -0.12013 -0.28118 0.36411  193 SER B N   
1462 C CA  . SER A 193 ? 2.32345 3.07960 3.03124 -0.09636 -0.29729 0.42052  193 SER B CA  
1463 C C   . SER A 193 ? 2.32603 3.07406 3.11969 -0.07943 -0.30495 0.37877  193 SER B C   
1464 O O   . SER A 193 ? 2.35478 3.18600 3.19151 -0.05115 -0.33320 0.37580  193 SER B O   
1465 C CB  . SER A 193 ? 2.37717 3.17752 3.07533 -0.06838 -0.32730 0.50932  193 SER B CB  
1466 O OG  . SER A 193 ? 2.42915 3.18534 3.20553 -0.03475 -0.34917 0.55569  193 SER B OG  
1467 N N   . THR A 194 ? 2.33083 2.98694 3.15130 -0.09614 -0.28026 0.34294  194 THR B N   
1468 C CA  . THR A 194 ? 2.34729 2.98582 3.25479 -0.08139 -0.27874 0.30190  194 THR B CA  
1469 C C   . THR A 194 ? 2.41413 3.01091 3.39884 -0.04303 -0.30182 0.36415  194 THR B C   
1470 O O   . THR A 194 ? 2.43968 2.99635 3.40297 -0.04032 -0.31014 0.43531  194 THR B O   
1471 C CB  . THR A 194 ? 2.32268 2.87729 3.21281 -0.11823 -0.23942 0.23586  194 THR B CB  
1472 O OG1 . THR A 194 ? 2.34460 2.90687 3.31145 -0.11061 -0.22757 0.17704  194 THR B OG1 
1473 C CG2 . THR A 194 ? 2.32137 2.77531 3.20583 -0.12834 -0.23479 0.26850  194 THR B CG2 
1474 N N   . LYS A 195 ? 2.39964 3.00467 3.48131 -0.01346 -0.30785 0.33520  195 LYS B N   
1475 C CA  . LYS A 195 ? 2.48601 3.04970 3.65434 0.03322  -0.33036 0.39253  195 LYS B CA  
1476 C C   . LYS A 195 ? 2.51759 3.01417 3.77699 0.03665  -0.30468 0.32981  195 LYS B C   
1477 O O   . LYS A 195 ? 2.47767 3.00326 3.74966 0.01655  -0.27880 0.24378  195 LYS B O   
1478 C CB  . LYS A 195 ? 2.53824 3.20761 3.74948 0.08994  -0.37846 0.43803  195 LYS B CB  
1479 C CG  . LYS A 195 ? 2.52202 3.28819 3.63414 0.08048  -0.40081 0.47251  195 LYS B CG  
1480 C CD  . LYS A 195 ? 2.57130 3.44777 3.71464 0.13764  -0.45685 0.52190  195 LYS B CD  
1481 C CE  . LYS A 195 ? 2.66940 3.47971 3.89281 0.19738  -0.48329 0.60142  195 LYS B CE  
1482 N NZ  . LYS A 195 ? 2.73107 3.62132 3.92402 0.24740  -0.54080 0.69348  195 LYS B NZ  
1483 N N   . TRP A 196 ? 2.66309 3.06558 3.98412 0.05836  -0.30617 0.37070  196 TRP B N   
1484 C CA  . TRP A 196 ? 2.71880 3.04712 4.13401 0.06511  -0.27953 0.31239  196 TRP B CA  
1485 C C   . TRP A 196 ? 2.83052 3.06409 4.31753 0.10218  -0.29196 0.38437  196 TRP B C   
1486 O O   . TRP A 196 ? 2.85436 3.09301 4.31897 0.12711  -0.32290 0.48118  196 TRP B O   
1487 C CB  . TRP A 196 ? 2.66108 2.92204 4.01591 0.00087  -0.23597 0.23878  196 TRP B CB  
1488 C CG  . TRP A 196 ? 2.66156 2.82536 3.97081 -0.03241 -0.23060 0.27814  196 TRP B CG  
1489 C CD1 . TRP A 196 ? 2.71943 2.77577 4.08260 -0.04164 -0.21372 0.26773  196 TRP B CD1 
1490 C CD2 . TRP A 196 ? 2.59939 2.77349 3.81180 -0.06275 -0.24030 0.32754  196 TRP B CD2 
1491 N NE1 . TRP A 196 ? 2.69230 2.69849 4.00024 -0.07988 -0.21463 0.30674  196 TRP B NE1 
1492 C CE2 . TRP A 196 ? 2.61348 2.69368 3.83214 -0.09077 -0.23053 0.34502  196 TRP B CE2 
1493 C CE3 . TRP A 196 ? 2.52491 2.78159 3.65296 -0.07034 -0.25310 0.35160  196 TRP B CE3 
1494 C CZ2 . TRP A 196 ? 2.55820 2.63635 3.71040 -0.12372 -0.23452 0.38699  196 TRP B CZ2 
1495 C CZ3 . TRP A 196 ? 2.48564 2.73068 3.54400 -0.09927 -0.25412 0.39322  196 TRP B CZ3 
1496 C CH2 . TRP A 196 ? 2.50210 2.66413 3.57679 -0.12454 -0.24561 0.41153  196 TRP B CH2 
1497 N N   . HIS A 197 ? 2.58700 2.72761 4.15592 0.10323  -0.26329 0.33617  197 HIS B N   
1498 C CA  . HIS A 197 ? 2.70674 2.72904 4.34580 0.12830  -0.26379 0.39384  197 HIS B CA  
1499 C C   . HIS A 197 ? 2.71483 2.64159 4.28631 0.06511  -0.24317 0.41108  197 HIS B C   
1500 O O   . HIS A 197 ? 2.74861 2.56423 4.37190 0.04585  -0.21572 0.38076  197 HIS B O   
1501 C CB  . HIS A 197 ? 2.80169 2.76341 4.57219 0.15909  -0.23825 0.32625  197 HIS B CB  
1502 C CG  . HIS A 197 ? 2.91556 2.78479 4.79023 0.22017  -0.25159 0.39912  197 HIS B CG  
1503 N ND1 . HIS A 197 ? 2.93107 2.83677 4.81477 0.28195  -0.29955 0.50931  197 HIS B ND1 
1504 C CD2 . HIS A 197 ? 3.01095 2.74345 4.97942 0.22865  -0.22178 0.37949  197 HIS B CD2 
1505 C CE1 . HIS A 197 ? 3.03420 2.82226 5.01193 0.32989  -0.29935 0.56257  197 HIS B CE1 
1506 N NE2 . HIS A 197 ? 3.07740 2.75582 5.11407 0.29795  -0.25020 0.48227  197 HIS B NE2 
1507 N N   . GLN B 1   ? 1.92461 2.37133 3.64395 -0.35250 -0.18660 -0.29184 1   GLN A N   
1508 C CA  . GLN B 1   ? 1.93816 2.36904 3.50245 -0.30085 -0.15052 -0.26573 1   GLN A CA  
1509 C C   . GLN B 1   ? 1.96828 2.33770 3.33030 -0.29511 -0.21218 -0.30315 1   GLN A C   
1510 O O   . GLN B 1   ? 1.98828 2.36661 3.34558 -0.31135 -0.30026 -0.34170 1   GLN A O   
1511 C CB  . GLN B 1   ? 1.94017 2.45190 3.60260 -0.26640 -0.14936 -0.23154 1   GLN A CB  
1512 C CG  . GLN B 1   ? 1.97161 2.45775 3.49044 -0.21255 -0.11448 -0.21071 1   GLN A CG  
1513 C CD  . GLN B 1   ? 1.98461 2.54311 3.60940 -0.17122 -0.09915 -0.17542 1   GLN A CD  
1514 O OE1 . GLN B 1   ? 1.95911 2.59980 3.77367 -0.18203 -0.11048 -0.15819 1   GLN A OE1 
1515 N NE2 . GLN B 1   ? 2.02774 2.55519 3.53770 -0.12290 -0.07327 -0.16426 1   GLN A NE2 
1516 N N   . VAL B 2   ? 2.07249 2.38640 3.27099 -0.26924 -0.16625 -0.28868 2   VAL A N   
1517 C CA  . VAL B 2   ? 2.09346 2.34747 3.10543 -0.26375 -0.20635 -0.31063 2   VAL A CA  
1518 C C   . VAL B 2   ? 2.11115 2.36961 3.04486 -0.22569 -0.21632 -0.28860 2   VAL A C   
1519 O O   . VAL B 2   ? 2.11521 2.36710 3.02779 -0.20026 -0.15725 -0.26073 2   VAL A O   
1520 C CB  . VAL B 2   ? 2.08913 2.27711 2.98660 -0.26839 -0.15027 -0.30748 2   VAL A CB  
1521 C CG1 . VAL B 2   ? 2.11046 2.24809 2.82306 -0.25560 -0.18112 -0.31524 2   VAL A CG1 
1522 C CG2 . VAL B 2   ? 2.08762 2.25572 3.05943 -0.30459 -0.14482 -0.33198 2   VAL A CG2 
1523 N N   . GLN B 3   ? 2.09007 2.35753 2.98001 -0.21859 -0.29180 -0.30188 3   GLN A N   
1524 C CA  . GLN B 3   ? 2.11435 2.37054 2.92081 -0.18371 -0.30322 -0.27758 3   GLN A CA  
1525 C C   . GLN B 3   ? 2.11717 2.30384 2.75641 -0.17904 -0.28225 -0.26933 3   GLN A C   
1526 O O   . GLN B 3   ? 2.11486 2.26919 2.68038 -0.19700 -0.28389 -0.28641 3   GLN A O   
1527 C CB  . GLN B 3   ? 2.14738 2.44427 2.96506 -0.17171 -0.38743 -0.28371 3   GLN A CB  
1528 C CG  . GLN B 3   ? 2.14961 2.52743 3.13379 -0.16342 -0.40962 -0.27559 3   GLN A CG  
1529 C CD  . GLN B 3   ? 2.16533 2.54629 3.18193 -0.12642 -0.36017 -0.23786 3   GLN A CD  
1530 O OE1 . GLN B 3   ? 2.15329 2.55780 3.26907 -0.12263 -0.30366 -0.22627 3   GLN A OE1 
1531 N NE2 . GLN B 3   ? 2.20542 2.55966 3.13818 -0.09453 -0.37862 -0.21695 3   GLN A NE2 
1532 N N   . LEU B 4   ? 2.11804 2.28100 2.70522 -0.15386 -0.26266 -0.24237 4   LEU A N   
1533 C CA  . LEU B 4   ? 2.12213 2.22921 2.57242 -0.15016 -0.25142 -0.22632 4   LEU A CA  
1534 C C   . LEU B 4   ? 2.16220 2.26009 2.58371 -0.12384 -0.28543 -0.19984 4   LEU A C   
1535 O O   . LEU B 4   ? 2.18336 2.28677 2.66714 -0.10344 -0.27601 -0.19021 4   LEU A O   
1536 C CB  . LEU B 4   ? 2.10407 2.18126 2.52698 -0.15178 -0.18369 -0.21958 4   LEU A CB  
1537 C CG  . LEU B 4   ? 2.07754 2.16126 2.52312 -0.17096 -0.13620 -0.23207 4   LEU A CG  
1538 C CD1 . LEU B 4   ? 2.08178 2.14677 2.48558 -0.16170 -0.07477 -0.22031 4   LEU A CD1 
1539 C CD2 . LEU B 4   ? 2.07074 2.13346 2.44607 -0.19094 -0.15424 -0.24290 4   LEU A CD2 
1540 N N   . VAL B 5   ? 2.06098 2.14408 2.39026 -0.11877 -0.32054 -0.18405 5   VAL A N   
1541 C CA  . VAL B 5   ? 2.11355 2.18909 2.41866 -0.09119 -0.35043 -0.14699 5   VAL A CA  
1542 C C   . VAL B 5   ? 2.13066 2.15946 2.32697 -0.09307 -0.33477 -0.11432 5   VAL A C   
1543 O O   . VAL B 5   ? 2.15717 2.18907 2.27071 -0.09374 -0.34777 -0.10948 5   VAL A O   
1544 C CB  . VAL B 5   ? 2.16337 2.29061 2.47958 -0.07112 -0.41552 -0.14524 5   VAL A CB  
1545 C CG1 . VAL B 5   ? 2.22845 2.34973 2.52648 -0.03582 -0.43704 -0.09443 5   VAL A CG1 
1546 C CG2 . VAL B 5   ? 2.14301 2.32911 2.58704 -0.07550 -0.43534 -0.17600 5   VAL A CG2 
1547 N N   . GLU B 6   ? 2.13854 2.12470 2.33889 -0.09219 -0.30795 -0.09269 6   GLU A N   
1548 C CA  . GLU B 6   ? 2.15739 2.10494 2.28454 -0.09785 -0.29557 -0.05405 6   GLU A CA  
1549 C C   . GLU B 6   ? 2.23644 2.18481 2.34619 -0.07048 -0.32860 -0.00047 6   GLU A C   
1550 O O   . GLU B 6   ? 2.27453 2.24914 2.42887 -0.04445 -0.36057 0.00548  6   GLU A O   
1551 C CB  . GLU B 6   ? 2.13270 2.03362 2.28210 -0.11152 -0.26243 -0.05929 6   GLU A CB  
1552 C CG  . GLU B 6   ? 2.07470 1.98172 2.22836 -0.12915 -0.22367 -0.10194 6   GLU A CG  
1553 C CD  . GLU B 6   ? 2.07249 2.00078 2.30740 -0.11554 -0.21446 -0.13677 6   GLU A CD  
1554 O OE1 . GLU B 6   ? 2.10342 2.05423 2.39372 -0.09628 -0.24367 -0.13266 6   GLU A OE1 
1555 O OE2 . GLU B 6   ? 2.05340 1.98409 2.29871 -0.11987 -0.17558 -0.16264 6   GLU A OE2 
1556 N N   . SER B 7   ? 2.13800 2.06464 2.18868 -0.07337 -0.31773 0.04659  7   SER A N   
1557 C CA  . SER B 7   ? 2.22232 2.15181 2.25470 -0.04388 -0.33762 0.11394  7   SER A CA  
1558 C C   . SER B 7   ? 2.23712 2.13819 2.23515 -0.05912 -0.31029 0.16613  7   SER A C   
1559 O O   . SER B 7   ? 2.18394 2.06667 2.17345 -0.09210 -0.28269 0.14467  7   SER A O   
1560 C CB  . SER B 7   ? 2.27792 2.26360 2.24579 -0.01024 -0.37163 0.12061  7   SER A CB  
1561 O OG  . SER B 7   ? 2.28412 2.28090 2.16032 -0.01748 -0.35834 0.10885  7   SER A OG  
1562 N N   . GLY B 8   ? 2.28762 2.19342 2.27312 -0.03226 -0.31721 0.24175  8   GLY A N   
1563 C CA  . GLY B 8   ? 2.29521 2.18939 2.25978 -0.04344 -0.29072 0.30582  8   GLY A CA  
1564 C C   . GLY B 8   ? 2.27469 2.11051 2.32669 -0.08021 -0.27741 0.31908  8   GLY A C   
1565 O O   . GLY B 8   ? 2.26109 2.09243 2.31749 -0.09738 -0.25816 0.37323  8   GLY A O   
1566 N N   . GLY B 9   ? 2.24728 2.03911 2.37160 -0.09099 -0.28844 0.27042  9   GLY A N   
1567 C CA  . GLY B 9   ? 2.21772 1.94227 2.42105 -0.12217 -0.28440 0.26992  9   GLY A CA  
1568 C C   . GLY B 9   ? 2.25955 1.94888 2.53198 -0.10905 -0.29035 0.35103  9   GLY A C   
1569 O O   . GLY B 9   ? 2.28835 2.01882 2.53202 -0.07858 -0.28692 0.42804  9   GLY A O   
1570 N N   . GLY B 10  ? 2.36571 1.97686 2.72796 -0.12716 -0.29755 0.33632  10  GLY A N   
1571 C CA  . GLY B 10  ? 2.40620 1.97124 2.85382 -0.11500 -0.30081 0.41432  10  GLY A CA  
1572 C C   . GLY B 10  ? 2.38570 1.88910 2.91835 -0.16251 -0.29951 0.44223  10  GLY A C   
1573 O O   . GLY B 10  ? 2.34089 1.83019 2.86817 -0.20622 -0.30324 0.38483  10  GLY A O   
1574 N N   . LEU B 11  ? 2.33746 1.80858 2.95620 -0.15354 -0.29556 0.53427  11  LEU A N   
1575 C CA  . LEU B 11  ? 2.34665 1.75016 3.08046 -0.20223 -0.29950 0.56654  11  LEU A CA  
1576 C C   . LEU B 11  ? 2.30527 1.77847 3.02966 -0.22639 -0.28047 0.64259  11  LEU A C   
1577 O O   . LEU B 11  ? 2.30765 1.85364 2.98617 -0.18661 -0.25619 0.73208  11  LEU A O   
1578 C CB  . LEU B 11  ? 2.41745 1.75062 3.26849 -0.18121 -0.29807 0.64093  11  LEU A CB  
1579 C CG  . LEU B 11  ? 2.44332 1.68578 3.44278 -0.23640 -0.30825 0.66682  11  LEU A CG  
1580 C CD1 . LEU B 11  ? 2.44845 1.60366 3.46180 -0.27617 -0.34135 0.53315  11  LEU A CD1 
1581 C CD2 . LEU B 11  ? 2.51485 1.69241 3.63644 -0.20927 -0.29741 0.76122  11  LEU A CD2 
1582 N N   . VAL B 12  ? 2.48414 1.93953 3.25041 -0.28625 -0.29199 0.60840  12  VAL A N   
1583 C CA  . VAL B 12  ? 2.44273 1.96864 3.21537 -0.31312 -0.27382 0.67848  12  VAL A CA  
1584 C C   . VAL B 12  ? 2.43423 1.90210 3.36460 -0.37686 -0.29383 0.70275  12  VAL A C   
1585 O O   . VAL B 12  ? 2.44277 1.83092 3.42074 -0.41531 -0.33088 0.60890  12  VAL A O   
1586 C CB  . VAL B 12  ? 2.39703 1.99193 3.04773 -0.32226 -0.26866 0.61004  12  VAL A CB  
1587 C CG1 . VAL B 12  ? 2.38037 1.92196 3.02749 -0.35714 -0.29997 0.48311  12  VAL A CG1 
1588 C CG2 . VAL B 12  ? 2.35626 2.02609 3.02088 -0.34621 -0.24682 0.68747  12  VAL A CG2 
1589 N N   . GLN B 13  ? 2.50838 2.01751 3.52262 -0.38577 -0.27036 0.82848  13  GLN A N   
1590 C CA  . GLN B 13  ? 2.49565 1.96558 3.67974 -0.45454 -0.29122 0.86113  13  GLN A CA  
1591 C C   . GLN B 13  ? 2.44716 1.96774 3.60062 -0.50425 -0.31089 0.79738  13  GLN A C   
1592 O O   . GLN B 13  ? 2.41020 2.03047 3.44866 -0.48109 -0.28161 0.81416  13  GLN A O   
1593 C CB  . GLN B 13  ? 2.48915 2.00565 3.78087 -0.44450 -0.25166 1.03019  13  GLN A CB  
1594 C CG  . GLN B 13  ? 2.51054 1.94856 4.02815 -0.50479 -0.27260 1.08334  13  GLN A CG  
1595 C CD  . GLN B 13  ? 2.58948 1.88960 4.17800 -0.49982 -0.29791 1.03565  13  GLN A CD  
1596 O OE1 . GLN B 13  ? 2.61966 1.90617 4.12311 -0.43378 -0.27927 1.03636  13  GLN A OE1 
1597 N NE2 . GLN B 13  ? 2.62838 1.82504 4.37407 -0.56836 -0.34364 0.98966  13  GLN A NE2 
1598 N N   . PRO B 14  ? 2.43298 1.88918 3.68113 -0.56841 -0.36122 0.72233  14  PRO A N   
1599 C CA  . PRO B 14  ? 2.39499 1.90744 3.59950 -0.60788 -0.38451 0.65359  14  PRO A CA  
1600 C C   . PRO B 14  ? 2.34345 1.97015 3.59776 -0.62819 -0.35753 0.76633  14  PRO A C   
1601 O O   . PRO B 14  ? 2.34013 1.98192 3.72242 -0.63628 -0.33602 0.89246  14  PRO A O   
1602 C CB  . PRO B 14  ? 2.43090 1.84105 3.74661 -0.66842 -0.45128 0.56049  14  PRO A CB  
1603 C CG  . PRO B 14  ? 2.47535 1.80354 3.96386 -0.68499 -0.45437 0.64137  14  PRO A CG  
1604 C CD  . PRO B 14  ? 2.48432 1.81931 3.90298 -0.61019 -0.39975 0.71377  14  PRO A CD  
1605 N N   . GLY B 15  ? 2.26090 1.97224 3.41606 -0.63143 -0.35358 0.72638  15  GLY A N   
1606 C CA  . GLY B 15  ? 2.21357 2.04635 3.37449 -0.63039 -0.31481 0.83077  15  GLY A CA  
1607 C C   . GLY B 15  ? 2.20516 2.09970 3.24158 -0.55532 -0.24802 0.90898  15  GLY A C   
1608 O O   . GLY B 15  ? 2.16293 2.15888 3.16802 -0.53955 -0.20807 0.98543  15  GLY A O   
1609 N N   . GLY B 16  ? 2.29712 2.13617 3.25908 -0.50492 -0.23668 0.89025  16  GLY A N   
1610 C CA  . GLY B 16  ? 2.30267 2.19566 3.13687 -0.43022 -0.18473 0.95023  16  GLY A CA  
1611 C C   . GLY B 16  ? 2.29157 2.21967 2.94687 -0.39893 -0.17395 0.86215  16  GLY A C   
1612 O O   . GLY B 16  ? 2.26084 2.21328 2.89178 -0.43040 -0.18655 0.79849  16  GLY A O   
1613 N N   . SER B 17  ? 2.36710 2.29947 2.90082 -0.33530 -0.15212 0.85930  17  SER A N   
1614 C CA  . SER B 17  ? 2.36117 2.32056 2.73714 -0.30449 -0.14092 0.78067  17  SER A CA  
1615 C C   . SER B 17  ? 2.41267 2.32191 2.72230 -0.26854 -0.15760 0.71368  17  SER A C   
1616 O O   . SER B 17  ? 2.45181 2.32063 2.81633 -0.25265 -0.16869 0.74711  17  SER A O   
1617 C CB  . SER B 17  ? 2.33082 2.37460 2.60845 -0.25695 -0.09162 0.85426  17  SER A CB  
1618 O OG  . SER B 17  ? 2.27575 2.37759 2.62290 -0.28707 -0.07238 0.92312  17  SER A OG  
1619 N N   . LEU B 18  ? 2.23292 2.14961 2.43372 -0.25497 -0.15758 0.62410  18  LEU A N   
1620 C CA  . LEU B 18  ? 2.27573 2.15803 2.42376 -0.22495 -0.17518 0.55581  18  LEU A CA  
1621 C C   . LEU B 18  ? 2.26952 2.18058 2.30142 -0.20784 -0.16366 0.48371  18  LEU A C   
1622 O O   . LEU B 18  ? 2.22896 2.14207 2.25368 -0.23728 -0.16031 0.42634  18  LEU A O   
1623 C CB  . LEU B 18  ? 2.27793 2.08494 2.51182 -0.25613 -0.20968 0.48913  18  LEU A CB  
1624 C CG  . LEU B 18  ? 2.30933 2.08269 2.51586 -0.22758 -0.22735 0.42137  18  LEU A CG  
1625 C CD1 . LEU B 18  ? 2.36756 2.15486 2.56013 -0.17813 -0.22708 0.48660  18  LEU A CD1 
1626 C CD2 . LEU B 18  ? 2.29990 1.99559 2.59247 -0.25411 -0.25414 0.36286  18  LEU A CD2 
1627 N N   . ARG B 19  ? 2.12734 2.06128 2.07111 -0.15903 -0.15894 0.48688  19  ARG A N   
1628 C CA  . ARG B 19  ? 2.12146 2.07516 1.96584 -0.14280 -0.15026 0.42106  19  ARG A CA  
1629 C C   . ARG B 19  ? 2.15335 2.07993 2.00184 -0.13429 -0.18000 0.34436  19  ARG A C   
1630 O O   . ARG B 19  ? 2.19770 2.12431 2.04457 -0.10181 -0.20147 0.36266  19  ARG A O   
1631 C CB  . ARG B 19  ? 2.14633 2.14427 1.88466 -0.09333 -0.12870 0.46926  19  ARG A CB  
1632 N N   . LEU B 20  ? 2.25340 2.16563 2.11167 -0.15931 -0.17892 0.26598  20  LEU A N   
1633 C CA  . LEU B 20  ? 2.23201 2.12768 2.11068 -0.15292 -0.20039 0.19723  20  LEU A CA  
1634 C C   . LEU B 20  ? 2.24892 2.17185 2.05620 -0.13242 -0.19877 0.15774  20  LEU A C   
1635 O O   . LEU B 20  ? 2.26412 2.20441 2.00694 -0.13150 -0.17328 0.16007  20  LEU A O   
1636 C CB  . LEU B 20  ? 2.14498 2.01349 2.07798 -0.18378 -0.19558 0.13857  20  LEU A CB  
1637 C CG  . LEU B 20  ? 2.13852 1.96193 2.15054 -0.20310 -0.21049 0.14981  20  LEU A CG  
1638 C CD1 . LEU B 20  ? 2.09199 1.88702 2.13822 -0.21445 -0.21121 0.07582  20  LEU A CD1 
1639 C CD2 . LEU B 20  ? 2.20481 2.00689 2.25863 -0.18027 -0.23421 0.19307  20  LEU A CD2 
1640 N N   . SER B 21  ? 2.29691 2.22233 2.12412 -0.11588 -0.22792 0.12076  21  SER A N   
1641 C CA  . SER B 21  ? 2.31381 2.26169 2.09413 -0.10103 -0.23931 0.07565  21  SER A CA  
1642 C C   . SER B 21  ? 2.24967 2.19851 2.10690 -0.10933 -0.25774 0.01626  21  SER A C   
1643 O O   . SER B 21  ? 2.25205 2.19736 2.17060 -0.09988 -0.28044 0.02367  21  SER A O   
1644 C CB  . SER B 21  ? 2.41954 2.39278 2.12964 -0.05824 -0.26794 0.10806  21  SER A CB  
1645 O OG  . SER B 21  ? 2.47933 2.46004 2.10732 -0.04216 -0.24157 0.16233  21  SER A OG  
1646 N N   . CYS B 22  ? 2.29651 2.25143 2.15856 -0.12410 -0.24376 -0.03603 22  CYS A N   
1647 C CA  . CYS B 22  ? 2.24259 2.20949 2.19057 -0.13155 -0.25409 -0.08527 22  CYS A CA  
1648 C C   . CYS B 22  ? 2.24841 2.23058 2.18483 -0.13644 -0.26118 -0.12917 22  CYS A C   
1649 O O   . CYS B 22  ? 2.22878 2.19810 2.14289 -0.15200 -0.22345 -0.14341 22  CYS A O   
1650 C CB  . CYS B 22  ? 2.17443 2.12612 2.17833 -0.15042 -0.21503 -0.10029 22  CYS A CB  
1651 S SG  . CYS B 22  ? 2.12711 2.10417 2.22577 -0.15784 -0.20145 -0.15251 22  CYS A SG  
1652 N N   . ALA B 23  ? 2.29066 2.29976 2.24796 -0.12292 -0.31154 -0.15102 23  ALA A N   
1653 C CA  . ALA B 23  ? 2.30910 2.32658 2.26342 -0.13045 -0.33154 -0.20094 23  ALA A CA  
1654 C C   . ALA B 23  ? 2.23224 2.26321 2.31221 -0.15783 -0.31629 -0.23892 23  ALA A C   
1655 O O   . ALA B 23  ? 2.19340 2.24796 2.36676 -0.15758 -0.31688 -0.23305 23  ALA A O   
1656 C CB  . ALA B 23  ? 2.38806 2.43661 2.31136 -0.10358 -0.40172 -0.21343 23  ALA A CB  
1657 N N   . ALA B 24  ? 2.41104 2.42566 2.49679 -0.17742 -0.29726 -0.27286 24  ALA A N   
1658 C CA  . ALA B 24  ? 2.35823 2.38885 2.57417 -0.20315 -0.28090 -0.30292 24  ALA A CA  
1659 C C   . ALA B 24  ? 2.39999 2.43536 2.64729 -0.21578 -0.33408 -0.35558 24  ALA A C   
1660 O O   . ALA B 24  ? 2.46779 2.46995 2.60983 -0.20724 -0.35430 -0.37670 24  ALA A O   
1661 C CB  . ALA B 24  ? 2.31903 2.32332 2.53832 -0.21717 -0.20432 -0.29198 24  ALA A CB  
1662 N N   . SER B 25  ? 2.40883 2.48663 2.80424 -0.23420 -0.35820 -0.37801 25  SER A N   
1663 C CA  . SER B 25  ? 2.45083 2.53752 2.90007 -0.25308 -0.42096 -0.43497 25  SER A CA  
1664 C C   . SER B 25  ? 2.46640 2.49425 2.90881 -0.27706 -0.38859 -0.46686 25  SER A C   
1665 O O   . SER B 25  ? 2.53407 2.53743 2.95562 -0.28564 -0.44233 -0.52303 25  SER A O   
1666 C CB  . SER B 25  ? 2.41490 2.56984 3.05278 -0.27207 -0.44870 -0.44281 25  SER A CB  
1667 O OG  . SER B 25  ? 2.34854 2.51856 3.08717 -0.27863 -0.37284 -0.40404 25  SER A OG  
1668 N N   . GLY B 26  ? 2.44370 2.44642 2.89995 -0.28406 -0.30252 -0.43352 26  GLY A N   
1669 C CA  . GLY B 26  ? 2.46431 2.40857 2.91217 -0.30022 -0.26027 -0.45135 26  GLY A CA  
1670 C C   . GLY B 26  ? 2.44436 2.36035 2.79311 -0.28218 -0.17939 -0.40240 26  GLY A C   
1671 O O   . GLY B 26  ? 2.40775 2.35058 2.71680 -0.26426 -0.15693 -0.35930 26  GLY A O   
1672 N N   . ASP B 27  ? 2.58618 2.44640 2.89994 -0.28675 -0.13893 -0.41145 27  ASP A N   
1673 C CA  . ASP B 27  ? 2.57788 2.41849 2.80107 -0.26843 -0.06428 -0.36411 27  ASP A CA  
1674 C C   . ASP B 27  ? 2.51361 2.38205 2.84520 -0.27672 0.01041  -0.32523 27  ASP A C   
1675 O O   . ASP B 27  ? 2.48652 2.37568 2.96895 -0.29780 0.01590  -0.33423 27  ASP A O   
1676 C CB  . ASP B 27  ? 2.65379 2.42485 2.78419 -0.25963 -0.04771 -0.38377 27  ASP A CB  
1677 C CG  . ASP B 27  ? 2.73979 2.48478 2.74540 -0.23930 -0.11718 -0.42279 27  ASP A CG  
1678 O OD1 . ASP B 27  ? 2.77687 2.53050 2.82774 -0.25050 -0.19141 -0.47390 27  ASP A OD1 
1679 O OD2 . ASP B 27  ? 2.77738 2.50123 2.63985 -0.20792 -0.09724 -0.39853 27  ASP A OD2 
1680 N N   . PHE B 28  ? 2.26099 2.13692 2.51645 -0.25669 0.06827  -0.27807 28  PHE A N   
1681 C CA  . PHE B 28  ? 2.21328 2.12801 2.54102 -0.25110 0.13577  -0.23795 28  PHE A CA  
1682 C C   . PHE B 28  ? 2.22443 2.12731 2.47131 -0.23249 0.20396  -0.19831 28  PHE A C   
1683 O O   . PHE B 28  ? 2.25931 2.13596 2.38566 -0.22173 0.19718  -0.19273 28  PHE A O   
1684 C CB  . PHE B 28  ? 2.17621 2.14100 2.50736 -0.23878 0.12102  -0.22243 28  PHE A CB  
1685 C CG  . PHE B 28  ? 2.15879 2.16042 2.62736 -0.24868 0.09612  -0.23775 28  PHE A CG  
1686 C CD1 . PHE B 28  ? 2.16659 2.16918 2.66080 -0.26184 0.01913  -0.27353 28  PHE A CD1 
1687 C CD2 . PHE B 28  ? 2.14223 2.18674 2.71429 -0.23869 0.15175  -0.21096 28  PHE A CD2 
1688 C CE1 . PHE B 28  ? 2.15309 2.20121 2.78501 -0.26963 -0.00444 -0.28197 28  PHE A CE1 
1689 C CE2 . PHE B 28  ? 2.13338 2.22081 2.84170 -0.24352 0.13466  -0.21643 28  PHE A CE2 
1690 C CZ  . PHE B 28  ? 2.13601 2.22649 2.88001 -0.26142 0.05520  -0.25179 28  PHE A CZ  
1691 N N   . TYR B 29  ? 2.29818 2.22991 2.61684 -0.22367 0.27283  -0.16421 29  TYR A N   
1692 C CA  . TYR B 29  ? 2.28167 2.22245 2.53260 -0.19946 0.34034  -0.11858 29  TYR A CA  
1693 C C   . TYR B 29  ? 2.26022 2.23799 2.40696 -0.18186 0.32797  -0.09982 29  TYR A C   
1694 O O   . TYR B 29  ? 2.27123 2.23834 2.31200 -0.17487 0.32382  -0.08560 29  TYR A O   
1695 C CB  . TYR B 29  ? 2.23612 2.20933 2.59619 -0.18731 0.41603  -0.08235 29  TYR A CB  
1696 C CG  . TYR B 29  ? 2.17162 2.19050 2.47327 -0.15049 0.48432  -0.02848 29  TYR A CG  
1697 C CD1 . TYR B 29  ? 2.18434 2.18618 2.45278 -0.13547 0.54133  0.00656  29  TYR A CD1 
1698 C CD2 . TYR B 29  ? 2.10371 2.18391 2.38625 -0.12601 0.49209  -0.01419 29  TYR A CD2 
1699 C CE1 . TYR B 29  ? 2.12663 2.18244 2.34225 -0.09794 0.59988  0.05837  29  TYR A CE1 
1700 C CE2 . TYR B 29  ? 2.04685 2.17545 2.27037 -0.08863 0.54676  0.02862  29  TYR A CE2 
1701 C CZ  . TYR B 29  ? 2.05557 2.17779 2.24716 -0.07504 0.59942  0.06722  29  TYR A CZ  
1702 O OH  . TYR B 29  ? 2.00358 2.18575 2.13459 -0.03398 0.64996  0.11271  29  TYR A OH  
1703 N N   . CYS B 30  ? 2.17459 2.19434 2.35726 -0.17427 0.32008  -0.10048 30  CYS A N   
1704 C CA  . CYS B 30  ? 2.17246 2.21923 2.27471 -0.16052 0.30270  -0.09245 30  CYS A CA  
1705 C C   . CYS B 30  ? 2.20379 2.23122 2.28905 -0.17604 0.22770  -0.12183 30  CYS A C   
1706 O O   . CYS B 30  ? 2.20785 2.23369 2.37108 -0.18461 0.19833  -0.14623 30  CYS A O   
1707 C CB  . CYS B 30  ? 2.15619 2.25263 2.29668 -0.13311 0.34210  -0.07990 30  CYS A CB  
1708 S SG  . CYS B 30  ? 2.17289 2.30228 2.20637 -0.10965 0.33718  -0.07159 30  CYS A SG  
1709 N N   . MET B 31  ? 2.03351 2.05259 2.02688 -0.17792 0.19874  -0.11245 31  MET A N   
1710 C CA  . MET B 31  ? 2.04975 2.05382 2.02604 -0.18666 0.13531  -0.12658 31  MET A CA  
1711 C C   . MET B 31  ? 2.05982 2.07575 1.97838 -0.18283 0.12668  -0.10896 31  MET A C   
1712 O O   . MET B 31  ? 2.05813 2.08435 1.91624 -0.18247 0.14534  -0.08117 31  MET A O   
1713 C CB  . MET B 31  ? 2.06985 2.04253 2.00296 -0.19573 0.09936  -0.13001 31  MET A CB  
1714 C CG  . MET B 31  ? 2.07642 2.03096 2.06831 -0.20379 0.08725  -0.16213 31  MET A CG  
1715 S SD  . MET B 31  ? 2.13779 2.05499 2.04350 -0.20140 0.04180  -0.17356 31  MET A SD  
1716 C CE  . MET B 31  ? 2.14865 2.04432 2.14203 -0.21597 0.02179  -0.22661 31  MET A CE  
1717 N N   . ALA B 32  ? 2.03798 2.05215 1.98230 -0.17972 0.09762  -0.12549 32  ALA A N   
1718 C CA  . ALA B 32  ? 2.06164 2.07725 1.96520 -0.18039 0.08155  -0.11884 32  ALA A CA  
1719 C C   . ALA B 32  ? 2.06706 2.05278 1.99868 -0.18337 0.03161  -0.13475 32  ALA A C   
1720 O O   . ALA B 32  ? 2.05326 2.03041 2.03874 -0.17685 0.01748  -0.15211 32  ALA A O   
1721 C CB  . ALA B 32  ? 2.09271 2.13996 1.98804 -0.16015 0.11902  -0.12747 32  ALA A CB  
1722 N N   . TRP B 33  ? 2.08200 2.05361 1.98678 -0.19357 0.00473  -0.12564 33  TRP A N   
1723 C CA  . TRP B 33  ? 2.08057 2.01380 2.01580 -0.19591 -0.03904 -0.13616 33  TRP A CA  
1724 C C   . TRP B 33  ? 2.11745 2.03891 2.05573 -0.18390 -0.04041 -0.17226 33  TRP A C   
1725 O O   . TRP B 33  ? 2.14504 2.09377 2.04549 -0.17993 -0.01929 -0.17963 33  TRP A O   
1726 C CB  . TRP B 33  ? 2.07080 1.98716 1.98981 -0.21738 -0.07127 -0.09587 33  TRP A CB  
1727 C CG  . TRP B 33  ? 2.05977 1.97882 1.96762 -0.21610 -0.07963 -0.06549 33  TRP A CG  
1728 C CD1 . TRP B 33  ? 2.06327 2.00553 1.92315 -0.21621 -0.05807 -0.04105 33  TRP A CD1 
1729 C CD2 . TRP B 33  ? 2.06594 1.96450 2.00233 -0.20717 -0.11301 -0.05850 33  TRP A CD2 
1730 N NE1 . TRP B 33  ? 2.08154 2.01678 1.92913 -0.20671 -0.07921 -0.02579 33  TRP A NE1 
1731 C CE2 . TRP B 33  ? 2.08208 1.99664 1.97682 -0.20105 -0.11411 -0.03360 33  TRP A CE2 
1732 C CE3 . TRP B 33  ? 2.07679 1.94545 2.06632 -0.19836 -0.14144 -0.07026 33  TRP A CE3 
1733 C CZ2 . TRP B 33  ? 2.11312 2.02367 2.01204 -0.18559 -0.14680 -0.02070 33  TRP A CZ2 
1734 C CZ3 . TRP B 33  ? 2.09854 1.96447 2.10288 -0.18463 -0.16979 -0.05004 33  TRP A CZ3 
1735 C CH2 . TRP B 33  ? 2.11740 2.00853 2.07404 -0.17803 -0.17434 -0.02578 33  TRP A CH2 
1736 N N   . PHE B 34  ? 2.13537 2.01611 2.11338 -0.17279 -0.06651 -0.19591 34  PHE A N   
1737 C CA  . PHE B 34  ? 2.18885 2.04565 2.16305 -0.15191 -0.06954 -0.24120 34  PHE A CA  
1738 C C   . PHE B 34  ? 2.20366 1.99252 2.21144 -0.16002 -0.11675 -0.24958 34  PHE A C   
1739 O O   . PHE B 34  ? 2.20222 1.96728 2.25766 -0.14821 -0.12785 -0.24352 34  PHE A O   
1740 C CB  . PHE B 34  ? 2.21737 2.09529 2.21438 -0.11092 -0.03186 -0.26748 34  PHE A CB  
1741 C CG  . PHE B 34  ? 2.24835 2.17562 2.20187 -0.08771 0.01513  -0.27848 34  PHE A CG  
1742 C CD1 . PHE B 34  ? 2.22664 2.20431 2.16896 -0.09731 0.05155  -0.24585 34  PHE A CD1 
1743 C CD2 . PHE B 34  ? 2.30731 2.22894 2.22659 -0.04990 0.02473  -0.32048 34  PHE A CD2 
1744 C CE1 . PHE B 34  ? 2.25924 2.28584 2.16625 -0.07054 0.10022  -0.24547 34  PHE A CE1 
1745 C CE2 . PHE B 34  ? 2.33843 2.31510 2.20984 -0.01908 0.07080  -0.32352 34  PHE A CE2 
1746 C CZ  . PHE B 34  ? 2.31147 2.34329 2.18140 -0.02988 0.11038  -0.28117 34  PHE A CZ  
1747 N N   . ARG B 35  ? 2.21755 1.97680 2.20955 -0.18021 -0.14580 -0.26163 35  ARG A N   
1748 C CA  . ARG B 35  ? 2.24543 1.92841 2.28146 -0.19108 -0.18996 -0.27161 35  ARG A CA  
1749 C C   . ARG B 35  ? 2.31376 1.94764 2.34062 -0.15676 -0.19531 -0.34240 35  ARG A C   
1750 O O   . ARG B 35  ? 2.34546 2.00089 2.31612 -0.14135 -0.18534 -0.38505 35  ARG A O   
1751 C CB  . ARG B 35  ? 2.23987 1.91348 2.28517 -0.23689 -0.22355 -0.24526 35  ARG A CB  
1752 C CG  . ARG B 35  ? 2.29644 1.89196 2.37579 -0.24975 -0.26931 -0.28745 35  ARG A CG  
1753 C CD  . ARG B 35  ? 2.28775 1.88653 2.40160 -0.30212 -0.30374 -0.25243 35  ARG A CD  
1754 N NE  . ARG B 35  ? 2.28699 1.95316 2.34673 -0.31291 -0.30029 -0.26740 35  ARG A NE  
1755 C CZ  . ARG B 35  ? 2.25155 1.97848 2.31914 -0.34650 -0.29980 -0.20974 35  ARG A CZ  
1756 N NH1 . ARG B 35  ? 2.21468 1.94389 2.33621 -0.37087 -0.29982 -0.13242 35  ARG A NH1 
1757 N NH2 . ARG B 35  ? 2.26169 2.05458 2.27992 -0.34917 -0.29612 -0.22498 35  ARG A NH2 
1758 N N   . GLN B 36  ? 2.35618 1.92534 2.43270 -0.13811 -0.20981 -0.35308 36  GLN A N   
1759 C CA  . GLN B 36  ? 2.43339 1.94553 2.50138 -0.09422 -0.21016 -0.41952 36  GLN A CA  
1760 C C   . GLN B 36  ? 2.48003 1.88862 2.60721 -0.10541 -0.25344 -0.42719 36  GLN A C   
1761 O O   . GLN B 36  ? 2.46635 1.85804 2.65601 -0.10896 -0.25814 -0.37772 36  GLN A O   
1762 C CB  . GLN B 36  ? 2.44376 1.99187 2.52380 -0.04283 -0.16569 -0.41991 36  GLN A CB  
1763 C CG  . GLN B 36  ? 2.52915 2.01460 2.61960 0.01186  -0.16075 -0.46993 36  GLN A CG  
1764 C CD  . GLN B 36  ? 2.58061 2.08825 2.59822 0.06355  -0.12668 -0.52676 36  GLN A CD  
1765 O OE1 . GLN B 36  ? 2.55206 2.14660 2.54077 0.07601  -0.08391 -0.51044 36  GLN A OE1 
1766 N NE2 . GLN B 36  ? 2.66573 2.09196 2.65259 0.09943  -0.14324 -0.59290 36  GLN A NE2 
1767 N N   . ALA B 37  ? 2.57676 1.91452 2.68600 -0.10796 -0.28652 -0.49038 37  ALA A N   
1768 C CA  . ALA B 37  ? 2.62639 1.85323 2.80449 -0.12888 -0.33212 -0.49942 37  ALA A CA  
1769 C C   . ALA B 37  ? 2.72696 1.85939 2.89588 -0.07389 -0.33453 -0.57558 37  ALA A C   
1770 O O   . ALA B 37  ? 2.75742 1.91967 2.85413 -0.01931 -0.30216 -0.62459 37  ALA A O   
1771 C CB  . ALA B 37  ? 2.62635 1.83598 2.81425 -0.18784 -0.38025 -0.51014 37  ALA A CB  
1772 N N   . PRO B 38  ? 2.55656 1.57249 2.79987 -0.08035 -0.36675 -0.58266 38  PRO A N   
1773 C CA  . PRO B 38  ? 2.67861 1.58976 2.90732 -0.02311 -0.36917 -0.66250 38  PRO A CA  
1774 C C   . PRO B 38  ? 2.77267 1.66667 2.89801 0.00284  -0.38333 -0.76716 38  PRO A C   
1775 O O   . PRO B 38  ? 2.84642 1.69577 2.96683 -0.04049 -0.43739 -0.81298 38  PRO A O   
1776 C CB  . PRO B 38  ? 2.77248 1.55650 3.10613 -0.05619 -0.41228 -0.65002 38  PRO A CB  
1777 C CG  . PRO B 38  ? 2.65397 1.49867 3.06365 -0.09907 -0.40503 -0.53553 38  PRO A CG  
1778 C CD  . PRO B 38  ? 2.53978 1.51841 2.88760 -0.12898 -0.39107 -0.50620 38  PRO A CD  
1779 N N   . GLY B 39  ? 2.78226 1.71750 2.82795 0.07710  -0.33558 -0.80313 39  GLY A N   
1780 C CA  . GLY B 39  ? 2.87435 1.81590 2.80170 0.11856  -0.33800 -0.89375 39  GLY A CA  
1781 C C   . GLY B 39  ? 2.77933 1.84423 2.64090 0.09146  -0.33180 -0.87748 39  GLY A C   
1782 O O   . GLY B 39  ? 2.85123 1.94248 2.60458 0.13408  -0.32842 -0.94373 39  GLY A O   
1783 N N   . LYS B 40  ? 2.85826 2.00030 2.77533 0.02940  -0.32784 -0.79038 40  LYS A N   
1784 C CA  . LYS B 40  ? 2.79680 2.05282 2.66202 0.00231  -0.31870 -0.76468 40  LYS A CA  
1785 C C   . LYS B 40  ? 2.72262 2.08571 2.58709 0.02537  -0.24872 -0.69551 40  LYS A C   
1786 O O   . LYS B 40  ? 2.66379 2.03481 2.60512 0.00598  -0.23472 -0.62969 40  LYS A O   
1787 C CB  . LYS B 40  ? 2.73694 1.99715 2.66596 -0.08436 -0.36727 -0.71951 40  LYS A CB  
1788 N N   . GLU B 41  ? 2.80161 2.24750 2.58270 0.06766  -0.20712 -0.71002 41  GLU A N   
1789 C CA  . GLU B 41  ? 2.74699 2.28859 2.53806 0.09256  -0.13838 -0.65086 41  GLU A CA  
1790 C C   . GLU B 41  ? 2.64751 2.25619 2.47614 0.02909  -0.13642 -0.57567 41  GLU A C   
1791 O O   . GLU B 41  ? 2.62455 2.23239 2.44795 -0.02303 -0.17681 -0.56823 41  GLU A O   
1792 C CB  . GLU B 41  ? 2.79754 2.40366 2.49475 0.16285  -0.08888 -0.68251 41  GLU A CB  
1793 C CG  . GLU B 41  ? 2.77868 2.47129 2.40571 0.15007  -0.08158 -0.67158 41  GLU A CG  
1794 C CD  . GLU B 41  ? 2.68890 2.47024 2.36065 0.11868  -0.03759 -0.58668 41  GLU A CD  
1795 O OE1 . GLU B 41  ? 2.65063 2.45187 2.38663 0.13203  0.00556  -0.54593 41  GLU A OE1 
1796 O OE2 . GLU B 41  ? 2.66342 2.49343 2.31009 0.08131  -0.04858 -0.56260 41  GLU A OE2 
1797 N N   . ARG B 42  ? 2.52283 2.19026 2.39439 0.03580  -0.08951 -0.52024 42  ARG A N   
1798 C CA  . ARG B 42  ? 2.43617 2.15291 2.34261 -0.01646 -0.08702 -0.45365 42  ARG A CA  
1799 C C   . ARG B 42  ? 2.42134 2.20666 2.26588 -0.03023 -0.07177 -0.44193 42  ARG A C   
1800 O O   . ARG B 42  ? 2.43912 2.28655 2.24572 0.00861  -0.02122 -0.44173 42  ARG A O   
1801 C CB  . ARG B 42  ? 2.40188 2.16250 2.36735 -0.00220 -0.04617 -0.41179 42  ARG A CB  
1802 N N   . GLU B 43  ? 2.38248 2.16272 2.22539 -0.08242 -0.11095 -0.42295 43  GLU A N   
1803 C CA  . GLU B 43  ? 2.37410 2.22221 2.16554 -0.09694 -0.10146 -0.40558 43  GLU A CA  
1804 C C   . GLU B 43  ? 2.30572 2.20138 2.12228 -0.12741 -0.07550 -0.33489 43  GLU A C   
1805 O O   . GLU B 43  ? 2.26227 2.12914 2.13047 -0.15384 -0.09009 -0.30183 43  GLU A O   
1806 C CB  . GLU B 43  ? 2.39946 2.22159 2.17948 -0.13307 -0.16316 -0.43016 43  GLU A CB  
1807 C CG  . GLU B 43  ? 2.36644 2.12752 2.22382 -0.18559 -0.20969 -0.40166 43  GLU A CG  
1808 C CD  . GLU B 43  ? 2.40913 2.12695 2.28236 -0.21965 -0.27559 -0.43781 43  GLU A CD  
1809 O OE1 . GLU B 43  ? 2.46155 2.19815 2.27449 -0.20175 -0.29244 -0.49436 43  GLU A OE1 
1810 O OE2 . GLU B 43  ? 2.39472 2.06229 2.34478 -0.26313 -0.31190 -0.40833 43  GLU A OE2 
1811 N N   . ALA B 44  ? 2.15122 2.11908 1.92495 -0.11737 -0.03577 -0.31220 44  ALA A N   
1812 C CA  . ALA B 44  ? 2.10143 2.10867 1.88746 -0.13948 -0.00683 -0.25184 44  ALA A CA  
1813 C C   . ALA B 44  ? 2.08109 2.08808 1.87076 -0.18572 -0.04536 -0.21868 44  ALA A C   
1814 O O   . ALA B 44  ? 2.09809 2.14185 1.85566 -0.19380 -0.05873 -0.21925 44  ALA A O   
1815 C CB  . ALA B 44  ? 2.10762 2.18552 1.85408 -0.10885 0.05340  -0.23466 44  ALA A CB  
1816 N N   . VAL B 45  ? 2.19055 2.16485 2.02211 -0.21226 -0.06275 -0.18525 45  VAL A N   
1817 C CA  . VAL B 45  ? 2.16274 2.13952 2.00994 -0.25106 -0.09243 -0.14053 45  VAL A CA  
1818 C C   . VAL B 45  ? 2.13784 2.16986 1.95601 -0.25411 -0.05438 -0.08489 45  VAL A C   
1819 O O   . VAL B 45  ? 2.13086 2.20537 1.93805 -0.27081 -0.05820 -0.05254 45  VAL A O   
1820 C CB  . VAL B 45  ? 2.13882 2.05541 2.04067 -0.26767 -0.12588 -0.12412 45  VAL A CB  
1821 C CG1 . VAL B 45  ? 2.12397 2.04695 2.05464 -0.30382 -0.15141 -0.06779 45  VAL A CG1 
1822 C CG2 . VAL B 45  ? 2.17336 2.02695 2.10523 -0.25844 -0.15732 -0.17982 45  VAL A CG2 
1823 N N   . ALA B 46  ? 2.14436 2.17622 1.95450 -0.23707 -0.01873 -0.07443 46  ALA A N   
1824 C CA  . ALA B 46  ? 2.10028 2.16576 1.88007 -0.23570 0.01695  -0.02804 46  ALA A CA  
1825 C C   . ALA B 46  ? 2.08899 2.15418 1.86464 -0.21215 0.05966  -0.04369 46  ALA A C   
1826 O O   . ALA B 46  ? 2.09996 2.13416 1.91003 -0.20536 0.05018  -0.07276 46  ALA A O   
1827 C CB  . ALA B 46  ? 2.08251 2.13012 1.86886 -0.25123 -0.00336 0.01749  46  ALA A CB  
1828 N N   . ALA B 47  ? 2.17687 2.27789 1.92173 -0.20023 0.10663  -0.02056 47  ALA A N   
1829 C CA  . ALA B 47  ? 2.15555 2.25412 1.91180 -0.18186 0.15165  -0.02970 47  ALA A CA  
1830 C C   . ALA B 47  ? 2.11132 2.21146 1.83457 -0.17968 0.18212  0.00660  47  ALA A C   
1831 O O   . ALA B 47  ? 2.08843 2.20900 1.77370 -0.18442 0.18050  0.04524  47  ALA A O   
1832 C CB  . ALA B 47  ? 2.15312 2.28993 1.91214 -0.15657 0.19350  -0.04105 47  ALA A CB  
1833 N N   . ILE B 48  ? 2.25819 2.33556 2.00263 -0.17124 0.21036  -0.00599 48  ILE A N   
1834 C CA  . ILE B 48  ? 2.24544 2.30712 1.95592 -0.16431 0.23975  0.01669  48  ILE A CA  
1835 C C   . ILE B 48  ? 2.22703 2.27733 1.98079 -0.15292 0.28924  0.00449  48  ILE A C   
1836 O O   . ILE B 48  ? 2.23750 2.27823 2.05884 -0.15696 0.28468  -0.02667 48  ILE A O   
1837 C CB  . ILE B 48  ? 2.29605 2.31631 1.98204 -0.17125 0.19867  0.00933  48  ILE A CB  
1838 C CG1 . ILE B 48  ? 2.31607 2.31008 1.95367 -0.15560 0.22939  0.02215  48  ILE A CG1 
1839 C CG2 . ILE B 48  ? 2.32992 2.32155 2.07171 -0.18040 0.16190  -0.03669 48  ILE A CG2 
1840 C CD1 . ILE B 48  ? 2.27111 2.29910 1.85507 -0.14043 0.26937  0.07655  48  ILE A CD1 
1841 N N   . ARG B 49  ? 2.49687 2.54910 2.22139 -0.13735 0.33951  0.03518  49  ARG A N   
1842 C CA  . ARG B 49  ? 2.48100 2.51937 2.25351 -0.12490 0.39706  0.03687  49  ARG A CA  
1843 C C   . ARG B 49  ? 2.54277 2.51745 2.36802 -0.14036 0.37755  -0.00678 49  ARG A C   
1844 O O   . ARG B 49  ? 2.59572 2.54299 2.40582 -0.15500 0.31906  -0.03790 49  ARG A O   
1845 C CB  . ARG B 49  ? 2.45271 2.49914 2.17547 -0.10180 0.45207  0.08336  49  ARG A CB  
1846 C CG  . ARG B 49  ? 2.37847 2.49526 2.09891 -0.07815 0.50026  0.12587  49  ARG A CG  
1847 C CD  . ARG B 49  ? 2.36462 2.48838 2.16505 -0.06754 0.54224  0.12072  49  ARG A CD  
1848 N NE  . ARG B 49  ? 2.31385 2.51637 2.10127 -0.04279 0.56309  0.14501  49  ARG A NE  
1849 C CZ  . ARG B 49  ? 2.29636 2.52793 2.13871 -0.01974 0.60784  0.15442  49  ARG A CZ  
1850 N NH1 . ARG B 49  ? 2.30908 2.50040 2.24278 -0.02310 0.64319  0.15124  49  ARG A NH1 
1851 N NH2 . ARG B 49  ? 2.27529 2.57990 2.08368 0.00874  0.61497  0.16662  49  ARG A NH2 
1852 N N   . SER B 50  ? 2.37387 2.32775 2.26788 -0.13599 0.42644  -0.00660 50  SER A N   
1853 C CA  . SER B 50  ? 2.44455 2.33467 2.40197 -0.15376 0.41019  -0.04932 50  SER A CA  
1854 C C   . SER B 50  ? 2.52612 2.35633 2.39967 -0.14839 0.39346  -0.06452 50  SER A C   
1855 O O   . SER B 50  ? 2.59236 2.39711 2.42732 -0.15764 0.33032  -0.10205 50  SER A O   
1856 C CB  . SER B 50  ? 2.42835 2.30762 2.49036 -0.15053 0.47518  -0.03443 50  SER A CB  
1857 O OG  . SER B 50  ? 2.51064 2.31302 2.61926 -0.16757 0.46329  -0.07393 50  SER A OG  
1858 N N   . GLY B 51  ? 2.69308 2.50209 2.53568 -0.12633 0.45363  -0.03301 51  GLY A N   
1859 C CA  . GLY B 51  ? 2.77349 2.53154 2.51714 -0.10736 0.45161  -0.03698 51  GLY A CA  
1860 C C   . GLY B 51  ? 2.73187 2.54005 2.36931 -0.09085 0.43702  0.00253  51  GLY A C   
1861 O O   . GLY B 51  ? 2.76946 2.55665 2.31940 -0.06390 0.45395  0.02249  51  GLY A O   
1862 N N   . GLY B 52  ? 2.69879 2.57162 2.34961 -0.10518 0.40744  0.01578  52  GLY A N   
1863 C CA  . GLY B 52  ? 2.66961 2.58963 2.24613 -0.09816 0.38684  0.05367  52  GLY A CA  
1864 C C   . GLY B 52  ? 2.60528 2.56863 2.14045 -0.07289 0.44381  0.11686  52  GLY A C   
1865 O O   . GLY B 52  ? 2.54068 2.53429 2.11372 -0.06425 0.49289  0.14019  52  GLY A O   
1866 N N   . ARG B 53  ? 2.76037 2.73536 2.21900 -0.05595 0.43951  0.15188  53  ARG A N   
1867 C CA  . ARG B 53  ? 2.69665 2.72386 2.11693 -0.02948 0.48886  0.22007  53  ARG A CA  
1868 C C   . ARG B 53  ? 2.58277 2.69833 2.04268 -0.04154 0.49148  0.25243  53  ARG A C   
1869 O O   . ARG B 53  ? 2.51874 2.68714 1.97031 -0.01938 0.53855  0.30319  53  ARG A O   
1870 C CB  . ARG B 53  ? 2.73172 2.71349 2.13821 0.00349  0.55755  0.22982  53  ARG A CB  
1871 C CG  . ARG B 53  ? 2.86431 2.73899 2.25929 0.00753  0.54914  0.16729  53  ARG A CG  
1872 C CD  . ARG B 53  ? 2.96316 2.80476 2.26321 0.02856  0.51942  0.15957  53  ARG A CD  
1873 N NE  . ARG B 53  ? 2.99786 2.84009 2.30045 0.00218  0.44448  0.12118  53  ARG A NE  
1874 C CZ  . ARG B 53  ? 3.07291 2.85778 2.40579 -0.01715 0.40039  0.04952  53  ARG A CZ  
1875 N NH1 . ARG B 53  ? 3.12694 2.84349 2.50064 -0.01979 0.41928  0.00311  53  ARG A NH1 
1876 N NH2 . ARG B 53  ? 3.09617 2.89503 2.42931 -0.03482 0.33507  0.02720  53  ARG A NH2 
1877 N N   . SER B 54  ? 2.40214 2.53433 1.90134 -0.07235 0.43903  0.22099  54  SER A N   
1878 C CA  . SER B 54  ? 2.33322 2.53970 1.85988 -0.08228 0.42879  0.23480  54  SER A CA  
1879 C C   . SER B 54  ? 2.36604 2.56577 1.92321 -0.11404 0.36184  0.19377  54  SER A C   
1880 O O   . SER B 54  ? 2.40592 2.56698 2.00051 -0.12253 0.34887  0.14533  54  SER A O   
1881 C CB  . SER B 54  ? 2.29927 2.52377 1.85713 -0.06386 0.47943  0.23269  54  SER A CB  
1882 O OG  . SER B 54  ? 2.23693 2.54975 1.78688 -0.05315 0.48724  0.26650  54  SER A OG  
1883 N N   . THR B 55  ? 2.16139 2.39858 1.71381 -0.13119 0.32083  0.21648  55  THR A N   
1884 C CA  . THR B 55  ? 2.20794 2.43098 1.79319 -0.15989 0.25847  0.18310  55  THR A CA  
1885 C C   . THR B 55  ? 2.20471 2.47904 1.81182 -0.16861 0.23940  0.17084  55  THR A C   
1886 O O   . THR B 55  ? 2.15831 2.49885 1.75245 -0.16123 0.25440  0.20628  55  THR A O   
1887 C CB  . THR B 55  ? 2.22167 2.44169 1.80042 -0.17412 0.22308  0.21721  55  THR A CB  
1888 O OG1 . THR B 55  ? 2.16282 2.43819 1.71842 -0.16278 0.25084  0.28290  55  THR A OG1 
1889 C CG2 . THR B 55  ? 2.27495 2.43185 1.82933 -0.16454 0.21731  0.20213  55  THR A CG2 
1890 N N   . TYR B 56  ? 2.27228 2.51790 1.90911 -0.17984 0.20455  0.11855  56  TYR A N   
1891 C CA  . TYR B 56  ? 2.30809 2.58852 1.95255 -0.17980 0.18339  0.09006  56  TYR A CA  
1892 C C   . TYR B 56  ? 2.38601 2.62933 2.06354 -0.20845 0.11713  0.05801  56  TYR A C   
1893 O O   . TYR B 56  ? 2.42080 2.60775 2.12176 -0.21089 0.10244  0.02570  56  TYR A O   
1894 C CB  . TYR B 56  ? 2.31681 2.59680 1.96234 -0.14995 0.22137  0.05657  56  TYR A CB  
1895 C CG  . TYR B 56  ? 2.23902 2.54528 1.86930 -0.12009 0.29321  0.09074  56  TYR A CG  
1896 C CD1 . TYR B 56  ? 2.20970 2.47312 1.84734 -0.12009 0.32395  0.10765  56  TYR A CD1 
1897 C CD2 . TYR B 56  ? 2.21026 2.58157 1.81757 -0.08786 0.32982  0.10494  56  TYR A CD2 
1898 C CE1 . TYR B 56  ? 2.15795 2.43184 1.79162 -0.09354 0.39071  0.13736  56  TYR A CE1 
1899 C CE2 . TYR B 56  ? 2.14131 2.53388 1.74413 -0.05736 0.40124  0.14466  56  TYR A CE2 
1900 C CZ  . TYR B 56  ? 2.11771 2.45588 1.73952 -0.06267 0.43238  0.16047  56  TYR A CZ  
1901 O OH  . TYR B 56  ? 2.06984 2.41591 1.69676 -0.03314 0.50468  0.19864  56  TYR A OH  
1902 N N   . TYR B 57  ? 2.15843 2.43378 1.84743 -0.23024 0.07612  0.06798  57  TYR A N   
1903 C CA  . TYR B 57  ? 2.20592 2.43882 1.93912 -0.26043 0.01326  0.04198  57  TYR A CA  
1904 C C   . TYR B 57  ? 2.25785 2.50757 1.98924 -0.26151 -0.02374 -0.00944 57  TYR A C   
1905 O O   . TYR B 57  ? 2.25825 2.57430 1.95369 -0.24420 -0.00937 -0.00860 57  TYR A O   
1906 C CB  . TYR B 57  ? 2.17675 2.42061 1.94737 -0.29231 -0.01200 0.10110  57  TYR A CB  
1907 C CG  . TYR B 57  ? 2.13139 2.36156 1.88513 -0.28154 0.02256  0.15113  57  TYR A CG  
1908 C CD1 . TYR B 57  ? 2.15251 2.31959 1.91688 -0.28032 0.01069  0.14016  57  TYR A CD1 
1909 C CD2 . TYR B 57  ? 2.06280 2.34470 1.78418 -0.26679 0.06575  0.20808  57  TYR A CD2 
1910 C CE1 . TYR B 57  ? 2.12828 2.28448 1.86238 -0.26408 0.03588  0.17746  57  TYR A CE1 
1911 C CE2 . TYR B 57  ? 2.02978 2.29204 1.72084 -0.24920 0.09605  0.24541  57  TYR A CE2 
1912 C CZ  . TYR B 57  ? 2.07241 2.27198 1.76556 -0.24775 0.07825  0.22670  57  TYR A CZ  
1913 O OH  . TYR B 57  ? 2.06752 2.24925 1.71622 -0.22418 0.10214  0.25599  57  TYR A OH  
1914 N N   . ALA B 58  ? 2.22007 2.40767 1.98610 -0.27712 -0.07261 -0.05577 58  ALA A N   
1915 C CA  . ALA B 58  ? 2.27451 2.46073 2.03646 -0.27919 -0.11957 -0.11556 58  ALA A CA  
1916 C C   . ALA B 58  ? 2.26932 2.49350 2.07357 -0.32164 -0.17029 -0.09108 58  ALA A C   
1917 O O   . ALA B 58  ? 2.23382 2.45505 2.09596 -0.35546 -0.17982 -0.03216 58  ALA A O   
1918 C CB  . ALA B 58  ? 2.31020 2.40544 2.10005 -0.27913 -0.15329 -0.17396 58  ALA A CB  
1919 N N   . ASP B 59  ? 2.35322 2.61980 2.13090 -0.31679 -0.20392 -0.13494 59  ASP A N   
1920 C CA  . ASP B 59  ? 2.35069 2.66561 2.18137 -0.36049 -0.26109 -0.11738 59  ASP A CA  
1921 C C   . ASP B 59  ? 2.35198 2.59339 2.28573 -0.41416 -0.31741 -0.11410 59  ASP A C   
1922 O O   . ASP B 59  ? 2.32233 2.60236 2.33575 -0.45823 -0.34379 -0.05673 59  ASP A O   
1923 C CB  . ASP B 59  ? 2.41121 2.76956 2.19174 -0.34368 -0.30426 -0.18782 59  ASP A CB  
1924 C CG  . ASP B 59  ? 2.39469 2.85091 2.08628 -0.29139 -0.24843 -0.16769 59  ASP A CG  
1925 O OD1 . ASP B 59  ? 2.32649 2.86037 2.03073 -0.29684 -0.21552 -0.08934 59  ASP A OD1 
1926 O OD2 . ASP B 59  ? 2.44411 2.90022 2.05457 -0.23955 -0.23234 -0.22464 59  ASP A OD2 
1927 N N   . SER B 60  ? 2.44046 2.57936 2.38338 -0.40852 -0.33197 -0.16690 60  SER A N   
1928 C CA  . SER B 60  ? 2.43854 2.49866 2.48481 -0.45382 -0.37854 -0.15817 60  SER A CA  
1929 C C   . SER B 60  ? 2.37387 2.43718 2.47152 -0.46847 -0.34203 -0.05963 60  SER A C   
1930 O O   . SER B 60  ? 2.36314 2.39245 2.56139 -0.50916 -0.37400 -0.02026 60  SER A O   
1931 C CB  . SER B 60  ? 2.48838 2.43863 2.52471 -0.43302 -0.39504 -0.23597 60  SER A CB  
1932 O OG  . SER B 60  ? 2.46600 2.40265 2.44551 -0.38744 -0.33308 -0.22851 60  SER A OG  
1933 N N   . VAL B 61  ? 2.28208 2.38353 2.31410 -0.43338 -0.27588 -0.01877 61  VAL A N   
1934 C CA  . VAL B 61  ? 2.24193 2.33795 2.29494 -0.43272 -0.24059 0.06027  61  VAL A CA  
1935 C C   . VAL B 61  ? 2.21361 2.39862 2.23345 -0.42244 -0.19334 0.13361  61  VAL A C   
1936 O O   . VAL B 61  ? 2.18005 2.36601 2.19588 -0.41168 -0.15953 0.19680  61  VAL A O   
1937 C CB  . VAL B 61  ? 2.24076 2.27642 2.25009 -0.39658 -0.21055 0.03393  61  VAL A CB  
1938 C CG1 . VAL B 61  ? 2.27082 2.21998 2.31168 -0.39812 -0.25078 -0.03547 61  VAL A CG1 
1939 C CG2 . VAL B 61  ? 2.24259 2.31670 2.16330 -0.35614 -0.15968 0.00969  61  VAL A CG2 
1940 N N   . LYS B 62  ? 2.21091 2.47157 2.20048 -0.41881 -0.18891 0.12727  62  LYS A N   
1941 C CA  . LYS B 62  ? 2.14223 2.48494 2.09673 -0.40086 -0.13704 0.19682  62  LYS A CA  
1942 C C   . LYS B 62  ? 2.09990 2.48285 2.13294 -0.43018 -0.14370 0.28850  62  LYS A C   
1943 O O   . LYS B 62  ? 2.12570 2.51202 2.25453 -0.47477 -0.19858 0.29650  62  LYS A O   
1944 C CB  . LYS B 62  ? 2.13794 2.55942 2.04910 -0.38637 -0.13281 0.17425  62  LYS A CB  
1945 C CG  . LYS B 62  ? 2.15510 2.56116 1.97685 -0.33947 -0.09201 0.11912  62  LYS A CG  
1946 C CD  . LYS B 62  ? 2.15768 2.64891 1.93517 -0.31801 -0.08723 0.10484  62  LYS A CD  
1947 C CE  . LYS B 62  ? 2.08581 2.64608 1.82318 -0.28653 -0.01702 0.17374  62  LYS A CE  
1948 N NZ  . LYS B 62  ? 2.01958 2.63026 1.80824 -0.31008 -0.01590 0.25795  62  LYS A NZ  
1949 N N   . GLY B 63  ? 2.08260 2.49341 2.07913 -0.40266 -0.08612 0.35883  63  GLY A N   
1950 C CA  . GLY B 63  ? 2.03698 2.48143 2.09621 -0.41520 -0.07757 0.45558  63  GLY A CA  
1951 C C   . GLY B 63  ? 2.07145 2.44465 2.18606 -0.42974 -0.09964 0.47250  63  GLY A C   
1952 O O   . GLY B 63  ? 2.03664 2.43283 2.18496 -0.42422 -0.07752 0.56145  63  GLY A O   
1953 N N   . ARG B 64  ? 2.09196 2.38246 2.21429 -0.44062 -0.13722 0.39565  64  ARG A N   
1954 C CA  . ARG B 64  ? 2.12595 2.34537 2.30370 -0.44973 -0.15749 0.41200  64  ARG A CA  
1955 C C   . ARG B 64  ? 2.13147 2.30496 2.21954 -0.40315 -0.12231 0.39794  64  ARG A C   
1956 O O   . ARG B 64  ? 2.11736 2.29565 2.19299 -0.38007 -0.09625 0.46559  64  ARG A O   
1957 C CB  . ARG B 64  ? 2.18091 2.33208 2.42698 -0.48540 -0.22016 0.33849  64  ARG A CB  
1958 C CG  . ARG B 64  ? 2.18252 2.37034 2.52645 -0.53687 -0.27051 0.33908  64  ARG A CG  
1959 C CD  . ARG B 64  ? 2.21441 2.31191 2.64570 -0.57283 -0.33380 0.28251  64  ARG A CD  
1960 N NE  . ARG B 64  ? 2.24623 2.28094 2.59643 -0.54790 -0.34577 0.17146  64  ARG A NE  
1961 C CZ  . ARG B 64  ? 2.26767 2.20725 2.61892 -0.53371 -0.35378 0.13085  64  ARG A CZ  
1962 N NH1 . ARG B 64  ? 2.26614 2.15863 2.69045 -0.54095 -0.35276 0.19008  64  ARG A NH1 
1963 N NH2 . ARG B 64  ? 2.29582 2.19240 2.57549 -0.50629 -0.35944 0.03510  64  ARG A NH2 
1964 N N   . PHE B 65  ? 2.16129 2.29487 2.19029 -0.38699 -0.12362 0.31108  65  PHE A N   
1965 C CA  . PHE B 65  ? 2.17236 2.26403 2.13575 -0.34998 -0.10175 0.28602  65  PHE A CA  
1966 C C   . PHE B 65  ? 2.13739 2.26813 2.01023 -0.31658 -0.05029 0.29267  65  PHE A C   
1967 O O   . PHE B 65  ? 2.10254 2.28290 1.95475 -0.31770 -0.02987 0.29235  65  PHE A O   
1968 C CB  . PHE B 65  ? 2.20261 2.23578 2.16591 -0.34793 -0.12516 0.19615  65  PHE A CB  
1969 C CG  . PHE B 65  ? 2.22080 2.19692 2.26759 -0.37463 -0.17460 0.17721  65  PHE A CG  
1970 C CD1 . PHE B 65  ? 2.22301 2.19784 2.35301 -0.40386 -0.19720 0.24113  65  PHE A CD1 
1971 C CD2 . PHE B 65  ? 2.23296 2.15312 2.28162 -0.36699 -0.19440 0.09879  65  PHE A CD2 
1972 C CE1 . PHE B 65  ? 2.24153 2.15098 2.45849 -0.42948 -0.24172 0.22199  65  PHE A CE1 
1973 C CE2 . PHE B 65  ? 2.25366 2.10846 2.37556 -0.38642 -0.23761 0.07626  65  PHE A CE2 
1974 C CZ  . PHE B 65  ? 2.25989 2.10410 2.46786 -0.41978 -0.26284 0.13559  65  PHE A CZ  
1975 N N   . THR B 66  ? 2.17461 2.28078 1.99456 -0.28467 -0.03178 0.29691  66  THR A N   
1976 C CA  . THR B 66  ? 2.15257 2.27414 1.88911 -0.25190 0.01277  0.29253  66  THR A CA  
1977 C C   . THR B 66  ? 2.19845 2.27071 1.90483 -0.23296 0.00741  0.23184  66  THR A C   
1978 O O   . THR B 66  ? 2.24368 2.28460 1.96346 -0.22692 -0.02034 0.23178  66  THR A O   
1979 C CB  . THR B 66  ? 2.13027 2.28323 1.82435 -0.22599 0.04228  0.37085  66  THR A CB  
1980 O OG1 . THR B 66  ? 2.16970 2.30358 1.88292 -0.21861 0.01982  0.41001  66  THR A OG1 
1981 C CG2 . THR B 66  ? 2.06510 2.28528 1.79151 -0.24068 0.05965  0.43366  66  THR A CG2 
1982 N N   . ILE B 67  ? 2.05573 2.12678 1.73158 -0.22294 0.03439  0.18614  67  ILE A N   
1983 C CA  . ILE B 67  ? 2.09352 2.12709 1.76119 -0.21000 0.03077  0.12937  67  ILE A CA  
1984 C C   . ILE B 67  ? 2.11502 2.14245 1.71520 -0.18279 0.06015  0.13435  67  ILE A C   
1985 O O   . ILE B 67  ? 2.07854 2.12908 1.64076 -0.17236 0.10044  0.16221  67  ILE A O   
1986 C CB  . ILE B 67  ? 2.07351 2.10695 1.77452 -0.21754 0.04171  0.07569  67  ILE A CB  
1987 C CG1 . ILE B 67  ? 2.09405 2.09813 1.81050 -0.20698 0.04012  0.02610  67  ILE A CG1 
1988 C CG2 . ILE B 67  ? 2.02755 2.09981 1.70238 -0.21232 0.08761  0.09014  67  ILE A CG2 
1989 C CD1 . ILE B 67  ? 2.07352 2.08225 1.83521 -0.20796 0.05408  -0.01648 67  ILE A CD1 
1990 N N   . SER B 68  ? 2.25576 2.25159 1.84052 -0.16869 0.03741  0.10534  68  SER A N   
1991 C CA  . SER B 68  ? 2.31722 2.29553 1.83088 -0.14062 0.05324  0.09750  68  SER A CA  
1992 C C   . SER B 68  ? 2.39599 2.34313 1.92305 -0.13634 0.01572  0.03936  68  SER A C   
1993 O O   . SER B 68  ? 2.38021 2.32627 1.97244 -0.15166 -0.01688 0.01620  68  SER A O   
1994 C CB  . SER B 68  ? 2.33968 2.33368 1.78258 -0.11265 0.05949  0.16071  68  SER A CB  
1995 O OG  . SER B 68  ? 2.39508 2.38514 1.83461 -0.10120 0.01720  0.17372  68  SER A OG  
1996 N N   . ARG B 69  ? 2.51333 2.43532 1.98015 -0.11352 0.01870  0.01386  69  ARG A N   
1997 C CA  . ARG B 69  ? 2.57887 2.47666 2.05530 -0.10911 -0.02516 -0.04490 69  ARG A CA  
1998 C C   . ARG B 69  ? 2.67153 2.54549 2.03900 -0.07035 -0.03206 -0.05420 69  ARG A C   
1999 O O   . ARG B 69  ? 2.68631 2.54614 1.99086 -0.05220 0.01248  -0.03704 69  ARG A O   
2000 C CB  . ARG B 69  ? 2.51607 2.39757 2.07641 -0.13480 -0.01455 -0.10024 69  ARG A CB  
2001 N N   . ASP B 70  ? 2.86496 2.73661 2.20520 -0.05194 -0.08815 -0.08197 70  ASP A N   
2002 C CA  . ASP B 70  ? 2.96804 2.82004 2.18578 -0.00476 -0.10401 -0.09615 70  ASP A CA  
2003 C C   . ASP B 70  ? 2.99256 2.79141 2.20506 -0.00931 -0.10981 -0.17722 70  ASP A C   
2004 O O   . ASP B 70  ? 2.91824 2.70203 2.23609 -0.05045 -0.10096 -0.21440 70  ASP A O   
2005 C CB  . ASP B 70  ? 3.02253 2.90111 2.20607 0.02333  -0.16576 -0.09302 70  ASP A CB  
2006 C CG  . ASP B 70  ? 2.97589 2.86150 2.25945 -0.00621 -0.22317 -0.15162 70  ASP A CG  
2007 O OD1 . ASP B 70  ? 2.87267 2.75718 2.27274 -0.05152 -0.20741 -0.16649 70  ASP A OD1 
2008 O OD2 . ASP B 70  ? 3.03632 2.93579 2.28138 0.02063  -0.28327 -0.17956 70  ASP A OD2 
2009 N N   . ASN B 71  ? 3.06801 2.83597 2.15781 0.03690  -0.12346 -0.20371 71  ASN A N   
2010 C CA  . ASN B 71  ? 3.11337 2.81671 2.18983 0.03607  -0.13730 -0.28882 71  ASN A CA  
2011 C C   . ASN B 71  ? 3.13529 2.84028 2.25313 0.02396  -0.22440 -0.36490 71  ASN A C   
2012 O O   . ASN B 71  ? 3.12959 2.88798 2.26021 0.02929  -0.27084 -0.34613 71  ASN A O   
2013 C CB  . ASN B 71  ? 3.22395 2.88489 2.13928 0.09766  -0.11249 -0.29078 71  ASN A CB  
2014 C CG  . ASN B 71  ? 3.20044 2.81498 2.12080 0.09323  -0.03572 -0.27991 71  ASN A CG  
2015 O OD1 . ASN B 71  ? 3.14900 2.72873 2.17647 0.04923  -0.02240 -0.31900 71  ASN A OD1 
2016 N ND2 . ASN B 71  ? 3.23038 2.85028 2.04142 0.14276  0.01936  -0.21834 71  ASN A ND2 
2017 N N   . SER B 72  ? 3.12968 2.77582 2.27681 0.00765  -0.24737 -0.44991 72  SER A N   
2018 C CA  . SER B 72  ? 3.13663 2.78679 2.35902 -0.01663 -0.33265 -0.52927 72  SER A CA  
2019 C C   . SER B 72  ? 3.00160 2.71336 2.38988 -0.06620 -0.34177 -0.50280 72  SER A C   
2020 O O   . SER B 72  ? 2.90326 2.60758 2.41713 -0.10992 -0.29519 -0.49312 72  SER A O   
2021 C CB  . SER B 72  ? 3.26052 2.93194 2.34828 0.03825  -0.40813 -0.55703 72  SER A CB  
2022 O OG  . SER B 72  ? 3.26678 2.95402 2.43479 0.01360  -0.49852 -0.63443 72  SER A OG  
2023 N N   . LYS B 73  ? 3.03080 2.80448 2.41724 -0.05270 -0.39749 -0.48748 73  LYS A N   
2024 C CA  . LYS B 73  ? 2.90893 2.73911 2.43618 -0.08771 -0.39851 -0.45315 73  LYS A CA  
2025 C C   . LYS B 73  ? 2.83129 2.66717 2.37211 -0.09648 -0.31676 -0.37558 73  LYS A C   
2026 O O   . LYS B 73  ? 2.88277 2.71379 2.31254 -0.06462 -0.28120 -0.32361 73  LYS A O   
2027 C CB  . LYS B 73  ? 2.94305 2.83474 2.44625 -0.05953 -0.46472 -0.43763 73  LYS A CB  
2028 N N   . ASN B 74  ? 2.83053 2.68126 2.50992 -0.13740 -0.28750 -0.36747 74  ASN A N   
2029 C CA  . ASN B 74  ? 2.75856 2.61585 2.45551 -0.14705 -0.21694 -0.30737 74  ASN A CA  
2030 C C   . ASN B 74  ? 2.70638 2.60899 2.44107 -0.14549 -0.23138 -0.26467 74  ASN A C   
2031 O O   . ASN B 74  ? 2.66398 2.59619 2.49064 -0.15629 -0.27083 -0.28444 74  ASN A O   
2032 C CB  . ASN B 74  ? 2.67676 2.52146 2.48644 -0.18165 -0.16773 -0.32138 74  ASN A CB  
2033 C CG  . ASN B 74  ? 2.61255 2.48618 2.57086 -0.20925 -0.20018 -0.35486 74  ASN A CG  
2034 O OD1 . ASN B 74  ? 2.65032 2.51933 2.64549 -0.21744 -0.25595 -0.40819 74  ASN A OD1 
2035 N ND2 . ASN B 74  ? 2.52631 2.43344 2.57255 -0.22120 -0.16687 -0.32449 74  ASN A ND2 
2036 N N   . THR B 75  ? 2.51308 2.42006 2.18563 -0.13195 -0.19944 -0.20500 75  THR A N   
2037 C CA  . THR B 75  ? 2.48180 2.41626 2.18396 -0.12875 -0.21284 -0.16285 75  THR A CA  
2038 C C   . THR B 75  ? 2.44724 2.37803 2.14033 -0.13848 -0.15957 -0.11420 75  THR A C   
2039 O O   . THR B 75  ? 2.51505 2.44090 2.12485 -0.12380 -0.13597 -0.07535 75  THR A O   
2040 C CB  . THR B 75  ? 2.57829 2.52794 2.20317 -0.09212 -0.25771 -0.13660 75  THR A CB  
2041 O OG1 . THR B 75  ? 2.61838 2.57902 2.24515 -0.08095 -0.31600 -0.18949 75  THR A OG1 
2042 C CG2 . THR B 75  ? 2.55038 2.51896 2.22109 -0.08906 -0.26807 -0.08852 75  THR A CG2 
2043 N N   . LEU B 76  ? 2.28247 2.22034 2.06067 -0.15969 -0.14240 -0.11677 76  LEU A N   
2044 C CA  . LEU B 76  ? 2.24895 2.18716 2.02255 -0.17018 -0.10245 -0.08208 76  LEU A CA  
2045 C C   . LEU B 76  ? 2.28497 2.22503 2.02682 -0.16155 -0.11953 -0.02925 76  LEU A C   
2046 O O   . LEU B 76  ? 2.29208 2.23227 2.06367 -0.15317 -0.15642 -0.02195 76  LEU A O   
2047 C CB  . LEU B 76  ? 2.17201 2.11660 2.03213 -0.18482 -0.08727 -0.10415 76  LEU A CB  
2048 C CG  . LEU B 76  ? 2.14485 2.09583 1.99848 -0.19406 -0.03975 -0.09215 76  LEU A CG  
2049 C CD1 . LEU B 76  ? 2.17448 2.12685 1.96417 -0.19186 -0.00316 -0.07504 76  LEU A CD1 
2050 C CD2 . LEU B 76  ? 2.10648 2.06910 2.03258 -0.19557 -0.01582 -0.12298 76  LEU A CD2 
2051 N N   . TYR B 77  ? 2.25762 2.20266 1.95037 -0.16268 -0.09047 0.01401  77  TYR A N   
2052 C CA  . TYR B 77  ? 2.28754 2.23858 1.97013 -0.15957 -0.09942 0.07524  77  TYR A CA  
2053 C C   . TYR B 77  ? 2.21488 2.16947 1.94184 -0.18714 -0.08208 0.08934  77  TYR A C   
2054 O O   . TYR B 77  ? 2.17876 2.14559 1.89717 -0.19727 -0.04964 0.07527  77  TYR A O   
2055 C CB  . TYR B 77  ? 2.36414 2.32964 1.95882 -0.13372 -0.08303 0.12511  77  TYR A CB  
2056 C CG  . TYR B 77  ? 2.45833 2.42075 1.98726 -0.09743 -0.10807 0.11125  77  TYR A CG  
2057 C CD1 . TYR B 77  ? 2.48777 2.45079 2.04154 -0.08466 -0.15377 0.10386  77  TYR A CD1 
2058 C CD2 . TYR B 77  ? 2.50545 2.46465 1.94268 -0.07113 -0.08816 0.10397  77  TYR A CD2 
2059 C CE1 . TYR B 77  ? 2.56664 2.53631 2.05338 -0.04780 -0.18483 0.08753  77  TYR A CE1 
2060 C CE2 . TYR B 77  ? 2.59425 2.54818 1.95917 -0.03405 -0.11887 0.08050  77  TYR A CE2 
2061 C CZ  . TYR B 77  ? 2.62126 2.58511 2.00997 -0.02302 -0.17012 0.07161  77  TYR A CZ  
2062 O OH  . TYR B 77  ? 2.70092 2.66873 2.01164 0.01725  -0.20865 0.04450  77  TYR A OH  
2063 N N   . LEU B 78  ? 2.23422 2.17726 2.01063 -0.19746 -0.10613 0.11617  78  LEU A N   
2064 C CA  . LEU B 78  ? 2.19256 2.13567 2.01160 -0.22544 -0.10280 0.12968  78  LEU A CA  
2065 C C   . LEU B 78  ? 2.22011 2.16868 2.05700 -0.22943 -0.11296 0.20543  78  LEU A C   
2066 O O   . LEU B 78  ? 2.22840 2.14780 2.12750 -0.23781 -0.14057 0.22036  78  LEU A O   
2067 C CB  . LEU B 78  ? 2.15907 2.07007 2.04045 -0.23738 -0.12325 0.07822  78  LEU A CB  
2068 C CG  . LEU B 78  ? 2.14078 2.05275 2.04887 -0.26374 -0.12362 0.07012  78  LEU A CG  
2069 C CD1 . LEU B 78  ? 2.13046 2.08911 1.99050 -0.26627 -0.08758 0.07215  78  LEU A CD1 
2070 C CD2 . LEU B 78  ? 2.13405 2.00986 2.08226 -0.26411 -0.14010 0.00820  78  LEU A CD2 
2071 N N   . GLN B 79  ? 2.35390 2.33963 2.14291 -0.22030 -0.08588 0.25888  79  GLN A N   
2072 C CA  . GLN B 79  ? 2.35385 2.35809 2.16849 -0.22043 -0.08558 0.34554  79  GLN A CA  
2073 C C   . GLN B 79  ? 2.31709 2.32192 2.22098 -0.26528 -0.09928 0.35727  79  GLN A C   
2074 O O   . GLN B 79  ? 2.28305 2.30684 2.18549 -0.28536 -0.09091 0.32420  79  GLN A O   
2075 C CB  . GLN B 79  ? 2.33540 2.38462 2.07000 -0.19046 -0.04621 0.39908  79  GLN A CB  
2076 C CG  . GLN B 79  ? 2.31875 2.40449 2.07007 -0.17741 -0.03100 0.50589  79  GLN A CG  
2077 C CD  . GLN B 79  ? 2.27451 2.37800 2.13837 -0.22374 -0.03956 0.55220  79  GLN A CD  
2078 O OE1 . GLN B 79  ? 2.23910 2.35614 2.13220 -0.25778 -0.04106 0.51952  79  GLN A OE1 
2079 N NE2 . GLN B 79  ? 2.28568 2.39014 2.21964 -0.22495 -0.04826 0.62839  79  GLN A NE2 
2080 N N   . MET B 80  ? 2.30198 2.28578 2.28709 -0.27976 -0.12281 0.40366  80  MET A N   
2081 C CA  . MET B 80  ? 2.28283 2.25201 2.36838 -0.32722 -0.14903 0.40320  80  MET A CA  
2082 C C   . MET B 80  ? 2.28175 2.26884 2.44984 -0.33989 -0.14880 0.50671  80  MET A C   
2083 O O   . MET B 80  ? 2.31235 2.28359 2.49302 -0.31423 -0.14625 0.56020  80  MET A O   
2084 C CB  . MET B 80  ? 2.29796 2.19410 2.43169 -0.33934 -0.18645 0.33082  80  MET A CB  
2085 C CG  . MET B 80  ? 2.28468 2.16913 2.35473 -0.32427 -0.18217 0.23728  80  MET A CG  
2086 S SD  . MET B 80  ? 2.29464 2.09837 2.41701 -0.32582 -0.21750 0.15960  80  MET A SD  
2087 C CE  . MET B 80  ? 2.33595 2.11434 2.47211 -0.29176 -0.22242 0.20401  80  MET A CE  
2088 N N   . ASN B 81  ? 2.34293 2.37025 2.57409 -0.37732 -0.15105 0.54008  81  ASN A N   
2089 C CA  . ASN B 81  ? 2.33348 2.37914 2.68354 -0.40297 -0.15586 0.63789  81  ASN A CA  
2090 C C   . ASN B 81  ? 2.33625 2.34723 2.80960 -0.46593 -0.20722 0.59904  81  ASN A C   
2091 O O   . ASN B 81  ? 2.33915 2.32842 2.78480 -0.48323 -0.23403 0.50041  81  ASN A O   
2092 C CB  . ASN B 81  ? 2.27983 2.42005 2.61720 -0.39158 -0.11310 0.73096  81  ASN A CB  
2093 C CG  . ASN B 81  ? 2.26359 2.43592 2.44918 -0.33080 -0.06580 0.73182  81  ASN A CG  
2094 O OD1 . ASN B 81  ? 2.23969 2.42960 2.34622 -0.32484 -0.05354 0.67258  81  ASN A OD1 
2095 N ND2 . ASN B 81  ? 2.27771 2.45922 2.42260 -0.28198 -0.03783 0.80317  81  ASN A ND2 
2096 N N   . SER B 82  ? 2.30872 2.31624 2.92125 -0.49743 -0.22029 0.68055  82  SER A N   
2097 C CA  . SER B 82  ? 2.31197 2.28639 3.06564 -0.56407 -0.27551 0.65364  82  SER A CA  
2098 C C   . SER B 82  ? 2.34619 2.22318 3.07922 -0.57393 -0.32145 0.52342  82  SER A C   
2099 O O   . SER B 82  ? 2.34928 2.21365 3.10969 -0.61220 -0.36636 0.44616  82  SER A O   
2100 C CB  . SER B 82  ? 2.27585 2.34006 3.05628 -0.59901 -0.28336 0.66315  82  SER A CB  
2101 O OG  . SER B 82  ? 2.27702 2.35398 2.93726 -0.58657 -0.28893 0.56055  82  SER A OG  
2102 N N   . LEU B 83  ? 2.34877 2.16266 3.02806 -0.53302 -0.30991 0.49981  83  LEU A N   
2103 C CA  . LEU B 83  ? 2.37635 2.10764 3.01603 -0.52570 -0.33944 0.38176  83  LEU A CA  
2104 C C   . LEU B 83  ? 2.40856 2.05703 3.17268 -0.57583 -0.39739 0.33622  83  LEU A C   
2105 O O   . LEU B 83  ? 2.43046 2.02668 3.31896 -0.59547 -0.40936 0.39582  83  LEU A O   
2106 C CB  . LEU B 83  ? 2.40120 2.08925 2.99232 -0.47426 -0.31788 0.38697  83  LEU A CB  
2107 C CG  . LEU B 83  ? 2.38472 2.13368 2.83479 -0.42427 -0.27631 0.38234  83  LEU A CG  
2108 C CD1 . LEU B 83  ? 2.39009 2.19276 2.82530 -0.39439 -0.23980 0.49458  83  LEU A CD1 
2109 C CD2 . LEU B 83  ? 2.40466 2.10314 2.79773 -0.38847 -0.28005 0.30577  83  LEU A CD2 
2110 N N   . LYS B 84  ? 2.43947 2.07520 3.16977 -0.59354 -0.43319 0.23114  84  LYS A N   
2111 C CA  . LYS B 84  ? 2.48728 2.03701 3.31478 -0.63715 -0.49694 0.16316  84  LYS A CA  
2112 C C   . LYS B 84  ? 2.53999 1.97013 3.35520 -0.60641 -0.50689 0.09374  84  LYS A C   
2113 O O   . LYS B 84  ? 2.53459 1.96565 3.24356 -0.55232 -0.47171 0.06765  84  LYS A O   
2114 C CB  . LYS B 84  ? 2.49619 2.08573 3.27300 -0.65699 -0.53402 0.07310  84  LYS A CB  
2115 N N   . ALA B 85  ? 2.49415 1.81979 3.42913 -0.64181 -0.55622 0.06418  85  ALA A N   
2116 C CA  . ALA B 85  ? 2.55500 1.75718 3.49463 -0.61014 -0.56341 0.00725  85  ALA A CA  
2117 C C   . ALA B 85  ? 2.58255 1.76691 3.38156 -0.56448 -0.56425 -0.11667 85  ALA A C   
2118 O O   . ALA B 85  ? 2.61055 1.73934 3.36783 -0.51421 -0.54216 -0.14400 85  ALA A O   
2119 C CB  . ALA B 85  ? 2.63291 1.71590 3.73074 -0.65977 -0.61989 -0.01228 85  ALA A CB  
2120 N N   . GLU B 86  ? 2.58439 1.82353 3.31274 -0.57612 -0.58631 -0.18509 86  GLU A N   
2121 C CA  . GLU B 86  ? 2.61559 1.85096 3.20860 -0.52659 -0.58051 -0.29301 86  GLU A CA  
2122 C C   . GLU B 86  ? 2.55519 1.88040 3.03338 -0.47548 -0.51407 -0.26300 86  GLU A C   
2123 O O   . GLU B 86  ? 2.57349 1.91206 2.94680 -0.43146 -0.49806 -0.33603 86  GLU A O   
2124 C CB  . GLU B 86  ? 2.64861 1.91730 3.20401 -0.55088 -0.62904 -0.37292 86  GLU A CB  
2125 C CG  . GLU B 86  ? 2.58408 1.98647 3.13772 -0.58434 -0.62173 -0.30704 86  GLU A CG  
2126 C CD  . GLU B 86  ? 2.57549 1.97871 3.28740 -0.65822 -0.66600 -0.24344 86  GLU A CD  
2127 O OE1 . GLU B 86  ? 2.58267 1.90837 3.41173 -0.67852 -0.66939 -0.19114 86  GLU A OE1 
2128 O OE2 . GLU B 86  ? 2.56397 2.05079 3.29218 -0.69457 -0.69607 -0.23988 86  GLU A OE2 
2129 N N   . ASP B 87  ? 2.44885 1.83425 2.94617 -0.47748 -0.47519 -0.15835 87  ASP A N   
2130 C CA  . ASP B 87  ? 2.38464 1.83709 2.78758 -0.43115 -0.41921 -0.13479 87  ASP A CA  
2131 C C   . ASP B 87  ? 2.40977 1.80480 2.81590 -0.38754 -0.40041 -0.13591 87  ASP A C   
2132 O O   . ASP B 87  ? 2.36688 1.81085 2.70460 -0.34921 -0.36210 -0.13118 87  ASP A O   
2133 C CB  . ASP B 87  ? 2.31422 1.85712 2.71941 -0.44537 -0.38895 -0.03117 87  ASP A CB  
2134 C CG  . ASP B 87  ? 2.27898 1.90239 2.66764 -0.47701 -0.39520 -0.02286 87  ASP A CG  
2135 O OD1 . ASP B 87  ? 2.26652 1.92997 2.56959 -0.45977 -0.38697 -0.08370 87  ASP A OD1 
2136 O OD2 . ASP B 87  ? 2.26671 1.92100 2.73248 -0.51511 -0.40456 0.05247  87  ASP A OD2 
2137 N N   . THR B 88  ? 2.48339 1.77746 2.97636 -0.39316 -0.42763 -0.14018 88  THR A N   
2138 C CA  . THR B 88  ? 2.51525 1.75443 3.02733 -0.35007 -0.41220 -0.13141 88  THR A CA  
2139 C C   . THR B 88  ? 2.52546 1.77372 2.95005 -0.29724 -0.38921 -0.20674 88  THR A C   
2140 O O   . THR B 88  ? 2.57673 1.77264 2.97472 -0.28413 -0.40513 -0.29578 88  THR A O   
2141 C CB  . THR B 88  ? 2.58802 1.70167 3.20802 -0.36361 -0.44689 -0.14197 88  THR A CB  
2142 O OG1 . THR B 88  ? 2.57496 1.68827 3.29811 -0.41169 -0.46066 -0.05282 88  THR A OG1 
2143 C CG2 . THR B 88  ? 2.63052 1.69010 3.27090 -0.31134 -0.42805 -0.13050 88  THR A CG2 
2144 N N   . ALA B 89  ? 2.45608 1.77163 2.83942 -0.26442 -0.35287 -0.17136 89  ALA A N   
2145 C CA  . ALA B 89  ? 2.45796 1.80286 2.77590 -0.21833 -0.32508 -0.22740 89  ALA A CA  
2146 C C   . ALA B 89  ? 2.42096 1.83516 2.72870 -0.19450 -0.29761 -0.17321 89  ALA A C   
2147 O O   . ALA B 89  ? 2.38936 1.84545 2.70365 -0.21265 -0.29703 -0.10232 89  ALA A O   
2148 C CB  . ALA B 89  ? 2.43306 1.83286 2.67240 -0.22475 -0.31436 -0.27741 89  ALA A CB  
2149 N N   . VAL B 90  ? 2.39177 1.82148 2.68407 -0.15082 -0.27603 -0.20816 90  VAL A N   
2150 C CA  . VAL B 90  ? 2.35692 1.86527 2.63735 -0.13131 -0.25458 -0.17682 90  VAL A CA  
2151 C C   . VAL B 90  ? 2.29456 1.87712 2.51000 -0.14413 -0.22905 -0.19192 90  VAL A C   
2152 O O   . VAL B 90  ? 2.30286 1.90022 2.48987 -0.12522 -0.20583 -0.24259 90  VAL A O   
2153 C CB  . VAL B 90  ? 2.40584 1.90905 2.72080 -0.08234 -0.24283 -0.19991 90  VAL A CB  
2154 C CG1 . VAL B 90  ? 2.38142 1.96470 2.70642 -0.07026 -0.23622 -0.16243 90  VAL A CG1 
2155 C CG2 . VAL B 90  ? 2.47573 1.89562 2.85389 -0.06617 -0.26419 -0.18560 90  VAL A CG2 
2156 N N   . TYR B 91  ? 2.26069 1.88964 2.45127 -0.17038 -0.22886 -0.14304 91  TYR A N   
2157 C CA  . TYR B 91  ? 2.20844 1.90393 2.34281 -0.17953 -0.20137 -0.14780 91  TYR A CA  
2158 C C   . TYR B 91  ? 2.19111 1.93497 2.33201 -0.15559 -0.18328 -0.15199 91  TYR A C   
2159 O O   . TYR B 91  ? 2.20227 1.95290 2.37209 -0.14424 -0.20075 -0.12444 91  TYR A O   
2160 C CB  . TYR B 91  ? 2.17843 1.90060 2.28428 -0.20950 -0.20537 -0.09239 91  TYR A CB  
2161 C CG  . TYR B 91  ? 2.18995 1.88421 2.30481 -0.24134 -0.22244 -0.08194 91  TYR A CG  
2162 C CD1 . TYR B 91  ? 2.23210 1.85754 2.40820 -0.25040 -0.25351 -0.07805 91  TYR A CD1 
2163 C CD2 . TYR B 91  ? 2.16576 1.90374 2.23929 -0.26335 -0.20907 -0.07289 91  TYR A CD2 
2164 C CE1 . TYR B 91  ? 2.24353 1.84397 2.44758 -0.28652 -0.27582 -0.07037 91  TYR A CE1 
2165 C CE2 . TYR B 91  ? 2.17842 1.90326 2.27496 -0.29603 -0.23095 -0.06141 91  TYR A CE2 
2166 C CZ  . TYR B 91  ? 2.21449 1.87034 2.38051 -0.31061 -0.26691 -0.06224 91  TYR A CZ  
2167 O OH  . TYR B 91  ? 2.22798 1.87077 2.43582 -0.34990 -0.29515 -0.05312 91  TYR A OH  
2168 N N   . TYR B 92  ? 2.13238 1.91414 2.25362 -0.14694 -0.14971 -0.18392 92  TYR A N   
2169 C CA  . TYR B 92  ? 2.11551 1.94642 2.26225 -0.13226 -0.13155 -0.18740 92  TYR A CA  
2170 C C   . TYR B 92  ? 2.07201 1.94588 2.17566 -0.15087 -0.10785 -0.17550 92  TYR A C   
2171 O O   . TYR B 92  ? 2.07216 1.95360 2.13209 -0.15931 -0.08373 -0.18088 92  TYR A O   
2172 C CB  . TYR B 92  ? 2.15570 1.99781 2.33947 -0.09990 -0.10204 -0.22487 92  TYR A CB  
2173 C CG  . TYR B 92  ? 2.21753 2.00416 2.42002 -0.07438 -0.11353 -0.24978 92  TYR A CG  
2174 C CD1 . TYR B 92  ? 2.25241 2.01147 2.50963 -0.05894 -0.14089 -0.23702 92  TYR A CD1 
2175 C CD2 . TYR B 92  ? 2.25521 2.01628 2.41725 -0.06001 -0.09728 -0.28857 92  TYR A CD2 
2176 C CE1 . TYR B 92  ? 2.32106 2.01757 2.59738 -0.03161 -0.14791 -0.26136 92  TYR A CE1 
2177 C CE2 . TYR B 92  ? 2.31983 2.01806 2.49187 -0.03270 -0.10964 -0.32161 92  TYR A CE2 
2178 C CZ  . TYR B 92  ? 2.35133 2.01199 2.58334 -0.01923 -0.13285 -0.30776 92  TYR A CZ  
2179 O OH  . TYR B 92  ? 2.42367 2.00969 2.66667 0.01153  -0.14202 -0.34250 92  TYR A OH  
2180 N N   . CYS B 93  ? 2.11296 2.01404 2.22797 -0.15423 -0.11706 -0.16148 93  CYS A N   
2181 C CA  . CYS B 93  ? 2.08605 2.01724 2.16938 -0.16692 -0.09296 -0.15786 93  CYS A CA  
2182 C C   . CYS B 93  ? 2.08289 2.04653 2.22749 -0.15697 -0.06208 -0.18287 93  CYS A C   
2183 O O   . CYS B 93  ? 2.08989 2.06871 2.30580 -0.14620 -0.07864 -0.19310 93  CYS A O   
2184 C CB  . CYS B 93  ? 2.08515 2.02045 2.13859 -0.17300 -0.12345 -0.13610 93  CYS A CB  
2185 S SG  . CYS B 93  ? 2.07529 2.04171 2.16261 -0.17428 -0.12764 -0.16078 93  CYS A SG  
2186 N N   . ALA B 94  ? 2.08648 2.06708 2.21294 -0.15815 -0.01494 -0.18562 94  ALA A N   
2187 C CA  . ALA B 94  ? 2.09995 2.11467 2.29362 -0.14587 0.02682  -0.19676 94  ALA A CA  
2188 C C   . ALA B 94  ? 2.07633 2.10431 2.25829 -0.16027 0.06008  -0.18658 94  ALA A C   
2189 O O   . ALA B 94  ? 2.06819 2.08491 2.17271 -0.16917 0.06949  -0.17148 94  ALA A O   
2190 C CB  . ALA B 94  ? 2.16202 2.18654 2.35235 -0.11704 0.06493  -0.20601 94  ALA A CB  
2191 N N   . VAL B 95  ? 1.99273 2.04473 2.26306 -0.16202 0.07941  -0.19201 95  VAL A N   
2192 C CA  . VAL B 95  ? 1.98473 2.03673 2.26501 -0.17714 0.10892  -0.18592 95  VAL A CA  
2193 C C   . VAL B 95  ? 1.98182 2.06926 2.33772 -0.16130 0.17678  -0.17121 95  VAL A C   
2194 O O   . VAL B 95  ? 1.98848 2.10696 2.40457 -0.13833 0.19448  -0.16930 95  VAL A O   
2195 C CB  . VAL B 95  ? 1.98351 2.02415 2.31149 -0.19984 0.06266  -0.20701 95  VAL A CB  
2196 C CG1 . VAL B 95  ? 1.99937 2.01153 2.23455 -0.20437 0.00440  -0.21186 95  VAL A CG1 
2197 C CG2 . VAL B 95  ? 1.97588 2.05149 2.43237 -0.19854 0.04434  -0.21914 95  VAL A CG2 
2198 N N   . GLY B 96  ? 2.09483 2.17771 2.44784 -0.16796 0.22012  -0.15534 96  GLY A N   
2199 C CA  . GLY B 96  ? 2.07211 2.19039 2.50069 -0.14974 0.29325  -0.12828 96  GLY A CA  
2200 C C   . GLY B 96  ? 2.04804 2.14510 2.50427 -0.16620 0.32845  -0.11444 96  GLY A C   
2201 O O   . GLY B 96  ? 2.06338 2.11632 2.45021 -0.18478 0.30185  -0.12729 96  GLY A O   
2202 N N   . VAL B 97  ? 1.85788 1.98518 2.42049 -0.15459 0.39343  -0.08424 97  VAL A N   
2203 C CA  . VAL B 97  ? 1.86362 1.96736 2.47327 -0.16543 0.44138  -0.06280 97  VAL A CA  
2204 C C   . VAL B 97  ? 1.86128 2.00302 2.44982 -0.12467 0.53103  -0.00648 97  VAL A C   
2205 O O   . VAL B 97  ? 1.88146 2.00461 2.50812 -0.12587 0.58323  0.02278  97  VAL A O   
2206 C CB  . VAL B 97  ? 1.88257 1.98197 2.67115 -0.19567 0.43731  -0.07135 97  VAL A CB  
2207 C CG1 . VAL B 97  ? 1.87344 2.03790 2.79391 -0.16902 0.51174  -0.02006 97  VAL A CG1 
2208 C CG2 . VAL B 97  ? 1.92545 1.95852 2.73713 -0.22490 0.44083  -0.08360 97  VAL A CG2 
2209 N N   . ASP B 98  ? 2.13150 2.32331 2.65289 -0.08481 0.54848  0.00783  98  ASP A N   
2210 C CA  . ASP B 98  ? 2.09532 2.33625 2.57880 -0.03633 0.62770  0.05942  98  ASP A CA  
2211 C C   . ASP B 98  ? 2.11800 2.39130 2.47215 -0.00289 0.60653  0.04506  98  ASP A C   
2212 O O   . ASP B 98  ? 2.16245 2.43528 2.51394 -0.00320 0.55991  0.00945  98  ASP A O   
2213 C CB  . ASP B 98  ? 2.06100 2.35199 2.68604 -0.00848 0.70291  0.10664  98  ASP A CB  
2214 C CG  . ASP B 98  ? 2.07729 2.40272 2.76816 0.00353  0.68243  0.08959  98  ASP A CG  
2215 O OD1 . ASP B 98  ? 2.11124 2.40338 2.82566 -0.03496 0.60706  0.04118  98  ASP A OD1 
2216 O OD2 . ASP B 98  ? 2.05822 2.44765 2.77367 0.05801  0.74446  0.12805  98  ASP A OD2 
2217 N N   . GLY B 99  ? 2.09529 2.39586 2.34822 0.02653  0.63884  0.07186  99  GLY A N   
2218 C CA  . GLY B 99  ? 2.12696 2.46139 2.26065 0.05852  0.61714  0.05511  99  GLY A CA  
2219 C C   . GLY B 99  ? 2.19155 2.48210 2.26896 0.02426  0.52670  -0.00100 99  GLY A C   
2220 O O   . GLY B 99  ? 2.19080 2.44206 2.22928 -0.01403 0.48476  -0.01049 99  GLY A O   
2221 N N   . ASN B 100 ? 2.30735 2.60348 2.38236 0.04298  0.50113  -0.03356 100 ASN A N   
2222 C CA  . ASN B 100 ? 2.36584 2.61471 2.40922 0.01319  0.42026  -0.08149 100 ASN A CA  
2223 C C   . ASN B 100 ? 2.36275 2.57212 2.50073 -0.02543 0.38799  -0.09373 100 ASN A C   
2224 O O   . ASN B 100 ? 2.34224 2.56895 2.58589 -0.01781 0.41923  -0.08216 100 ASN A O   
2225 C CB  . ASN B 100 ? 2.43156 2.69091 2.44011 0.05266  0.40714  -0.11456 100 ASN A CB  
2226 C CG  . ASN B 100 ? 2.45675 2.74626 2.35053 0.08435  0.40900  -0.12232 100 ASN A CG  
2227 O OD1 . ASN B 100 ? 2.41121 2.73168 2.26161 0.08418  0.43291  -0.09104 100 ASN A OD1 
2228 N ND2 . ASN B 100 ? 2.53434 2.81495 2.37838 0.11412  0.38100  -0.16658 100 ASN A ND2 
2229 N N   . CYS B 101 ? 2.24101 2.40446 2.34534 -0.06459 0.32420  -0.11380 101 CYS A N   
2230 C CA  . CYS B 101 ? 2.24312 2.37534 2.41988 -0.09537 0.28357  -0.12934 101 CYS A CA  
2231 C C   . CYS B 101 ? 2.28673 2.42364 2.52145 -0.07946 0.26202  -0.15143 101 CYS A C   
2232 O O   . CYS B 101 ? 2.32676 2.43252 2.54282 -0.09124 0.20437  -0.17334 101 CYS A O   
2233 C CB  . CYS B 101 ? 2.24866 2.33856 2.36240 -0.12861 0.22556  -0.13785 101 CYS A CB  
2234 S SG  . CYS B 101 ? 2.22878 2.32057 2.23362 -0.13296 0.24131  -0.11056 101 CYS A SG  
2235 N N   . ARG B 102 ? 2.13286 2.31129 2.44342 -0.04796 0.31354  -0.13847 102 ARG A N   
2236 C CA  . ARG B 102 ? 2.17003 2.36254 2.53987 -0.02080 0.30748  -0.15200 102 ARG A CA  
2237 C C   . ARG B 102 ? 2.13431 2.35654 2.65565 -0.03126 0.31860  -0.13734 102 ARG A C   
2238 O O   . ARG B 102 ? 2.13903 2.40240 2.73916 0.00403  0.35237  -0.12508 102 ARG A O   
2239 C CB  . ARG B 102 ? 2.18748 2.41318 2.51248 0.03844  0.35967  -0.14783 102 ARG A CB  
2240 N N   . ASN B 103 ? 2.14588 2.35018 2.71223 -0.07752 0.28943  -0.13916 103 ASN A N   
2241 C CA  . ASN B 103 ? 2.11682 2.34829 2.83721 -0.09640 0.28152  -0.13459 103 ASN A CA  
2242 C C   . ASN B 103 ? 2.14520 2.37535 2.90009 -0.10124 0.21395  -0.15893 103 ASN A C   
2243 O O   . ASN B 103 ? 2.14088 2.41744 3.02109 -0.08868 0.22035  -0.14854 103 ASN A O   
2244 C CB  . ASN B 103 ? 2.07847 2.28435 2.83051 -0.14159 0.26897  -0.13843 103 ASN A CB  
2245 C CG  . ASN B 103 ? 2.04520 2.26148 2.81744 -0.13342 0.34797  -0.10242 103 ASN A CG  
2246 O OD1 . ASN B 103 ? 2.04287 2.28184 2.75397 -0.09360 0.40467  -0.07624 103 ASN A OD1 
2247 N ND2 . ASN B 103 ? 2.02179 2.21931 2.87720 -0.16841 0.35016  -0.10225 103 ASN A ND2 
2248 N N   . TYR B 104 ? 2.16142 2.34531 2.81430 -0.11566 0.15289  -0.18318 104 TYR A N   
2249 C CA  . TYR B 104 ? 2.18198 2.36232 2.85372 -0.11322 0.09151  -0.19854 104 TYR A CA  
2250 C C   . TYR B 104 ? 2.21861 2.34941 2.76112 -0.10230 0.06601  -0.20826 104 TYR A C   
2251 O O   . TYR B 104 ? 2.22501 2.32971 2.66906 -0.10382 0.08659  -0.20636 104 TYR A O   
2252 C CB  . TYR B 104 ? 2.13807 2.31910 2.85519 -0.14983 0.02736  -0.21374 104 TYR A CB  
2253 C CG  . TYR B 104 ? 2.10527 2.33151 2.97322 -0.16973 0.03842  -0.21093 104 TYR A CG  
2254 C CD1 . TYR B 104 ? 2.10599 2.39096 3.11703 -0.16059 0.02718  -0.20306 104 TYR A CD1 
2255 C CD2 . TYR B 104 ? 2.07647 2.28630 2.95597 -0.19802 0.06047  -0.21342 104 TYR A CD2 
2256 C CE1 . TYR B 104 ? 2.07063 2.40241 3.24318 -0.18482 0.03379  -0.19692 104 TYR A CE1 
2257 C CE2 . TYR B 104 ? 2.05042 2.29383 3.08663 -0.22191 0.06818  -0.21140 104 TYR A CE2 
2258 C CZ  . TYR B 104 ? 2.04382 2.35100 3.23181 -0.21810 0.05284  -0.20276 104 TYR A CZ  
2259 O OH  . TYR B 104 ? 2.01427 2.36038 3.38108 -0.24770 0.05733  -0.19725 104 TYR A OH  
2260 N N   . TRP B 105 ? 2.18230 2.30312 2.73754 -0.09117 0.02067  -0.21489 105 TRP A N   
2261 C CA  . TRP B 105 ? 2.20444 2.27234 2.66351 -0.08346 -0.00601 -0.22043 105 TRP A CA  
2262 C C   . TRP B 105 ? 2.18724 2.24211 2.65549 -0.09080 -0.07086 -0.21630 105 TRP A C   
2263 O O   . TRP B 105 ? 2.16241 2.18174 2.55226 -0.10660 -0.10220 -0.20867 105 TRP A O   
2264 C CB  . TRP B 105 ? 2.28748 2.34370 2.74093 -0.04145 0.02503  -0.23035 105 TRP A CB  
2265 C CG  . TRP B 105 ? 2.32678 2.40760 2.76242 -0.02121 0.09068  -0.23056 105 TRP A CG  
2266 C CD1 . TRP B 105 ? 2.34744 2.40654 2.68251 -0.01801 0.11048  -0.23879 105 TRP A CD1 
2267 C CD2 . TRP B 105 ? 2.31326 2.45450 2.83919 0.00187  0.14614  -0.21485 105 TRP A CD2 
2268 N NE1 . TRP B 105 ? 2.35329 2.45597 2.69688 0.01143  0.17516  -0.22997 105 TRP A NE1 
2269 C CE2 . TRP B 105 ? 2.31133 2.46311 2.77421 0.02455  0.20229  -0.21151 105 TRP A CE2 
2270 C CE3 . TRP B 105 ? 2.27605 2.47080 2.93933 0.00636  0.15365  -0.19810 105 TRP A CE3 
2271 C CZ2 . TRP B 105 ? 2.26615 2.47727 2.79384 0.05643  0.27257  -0.18604 105 TRP A CZ2 
2272 C CZ3 . TRP B 105 ? 2.23880 2.49186 2.98131 0.03134  0.22208  -0.17309 105 TRP A CZ3 
2273 C CH2 . TRP B 105 ? 2.23233 2.49171 2.90450 0.05844  0.28429  -0.16437 105 TRP A CH2 
2274 N N   . GLY B 106 ? 2.17938 2.27130 2.74688 -0.07514 -0.08875 -0.21414 106 GLY A N   
2275 C CA  . GLY B 106 ? 2.17875 2.27177 2.75907 -0.07393 -0.15035 -0.20491 106 GLY A CA  
2276 C C   . GLY B 106 ? 2.21954 2.25487 2.73923 -0.05664 -0.16902 -0.19384 106 GLY A C   
2277 O O   . GLY B 106 ? 2.21187 2.23195 2.68916 -0.06398 -0.21221 -0.17609 106 GLY A O   
2278 N N   . GLN B 107 ? 2.31874 2.31964 2.83451 -0.03079 -0.13690 -0.20335 107 GLN A N   
2279 C CA  . GLN B 107 ? 2.37259 2.30655 2.85448 -0.01382 -0.15482 -0.19821 107 GLN A CA  
2280 C C   . GLN B 107 ? 2.32377 2.21298 2.71285 -0.04626 -0.17065 -0.18769 107 GLN A C   
2281 O O   . GLN B 107 ? 2.27553 2.17098 2.61216 -0.06893 -0.14746 -0.19718 107 GLN A O   
2282 C CB  . GLN B 107 ? 2.42163 2.36920 2.96957 0.00988  -0.19185 -0.17494 107 GLN A CB  
2283 C CG  . GLN B 107 ? 2.44604 2.43972 3.09470 0.04712  -0.17092 -0.18025 107 GLN A CG  
2284 C CD  . GLN B 107 ? 2.44567 2.46895 3.16815 0.07299  -0.20976 -0.15168 107 GLN A CD  
2285 O OE1 . GLN B 107 ? 2.42372 2.46020 3.12870 0.05967  -0.25712 -0.12795 107 GLN A OE1 
2286 N NE2 . GLN B 107 ? 2.46940 2.50924 3.27186 0.11760  -0.18730 -0.15020 107 GLN A NE2 
2287 N N   . GLY B 108 ? 2.30327 2.15275 2.67862 -0.04619 -0.20525 -0.16051 108 GLY A N   
2288 C CA  . GLY B 108 ? 2.27143 2.08694 2.57649 -0.07487 -0.21597 -0.13922 108 GLY A CA  
2289 C C   . GLY B 108 ? 2.32436 2.10399 2.63981 -0.06723 -0.24941 -0.09550 108 GLY A C   
2290 O O   . GLY B 108 ? 2.38220 2.17247 2.74991 -0.03890 -0.26863 -0.07888 108 GLY A O   
2291 N N   . THR B 109 ? 2.19704 1.94053 2.47017 -0.09115 -0.25386 -0.06939 109 THR A N   
2292 C CA  . THR B 109 ? 2.25649 1.96479 2.54613 -0.08633 -0.27749 -0.01406 109 THR A CA  
2293 C C   . THR B 109 ? 2.25815 1.89418 2.55554 -0.11034 -0.27481 -0.01461 109 THR A C   
2294 O O   . THR B 109 ? 2.20586 1.84303 2.46469 -0.13842 -0.26137 -0.03931 109 THR A O   
2295 C CB  . THR B 109 ? 2.25600 2.01109 2.49518 -0.08984 -0.28981 0.03943  109 THR A CB  
2296 O OG1 . THR B 109 ? 2.32680 2.04904 2.58540 -0.08327 -0.30258 0.10528  109 THR A OG1 
2297 C CG2 . THR B 109 ? 2.18731 1.96278 2.35922 -0.12103 -0.26968 0.03180  109 THR A CG2 
2298 N N   . LEU B 110 ? 2.24483 1.81887 2.59925 -0.09922 -0.28995 0.01333  110 LEU A N   
2299 C CA  . LEU B 110 ? 2.25270 1.74351 2.63816 -0.12312 -0.29572 0.00082  110 LEU A CA  
2300 C C   . LEU B 110 ? 2.23795 1.72970 2.62443 -0.15784 -0.30267 0.06553  110 LEU A C   
2301 O O   . LEU B 110 ? 2.26775 1.78366 2.66519 -0.14523 -0.30616 0.14075  110 LEU A O   
2302 C CB  . LEU B 110 ? 2.32602 1.73517 2.78635 -0.09530 -0.30623 -0.00075 110 LEU A CB  
2303 C CG  . LEU B 110 ? 2.35232 1.66116 2.86851 -0.12255 -0.32224 0.00397  110 LEU A CG  
2304 C CD1 . LEU B 110 ? 2.33820 1.60461 2.82655 -0.14515 -0.32596 -0.08206 110 LEU A CD1 
2305 C CD2 . LEU B 110 ? 2.42848 1.65688 3.02465 -0.08814 -0.32884 0.02132  110 LEU A CD2 
2306 N N   . VAL B 111 ? 2.19683 1.67027 2.57349 -0.19700 -0.30403 0.04015  111 VAL A N   
2307 C CA  . VAL B 111 ? 2.19344 1.66681 2.59538 -0.23429 -0.31053 0.10187  111 VAL A CA  
2308 C C   . VAL B 111 ? 2.24675 1.62226 2.73538 -0.25928 -0.33528 0.08487  111 VAL A C   
2309 O O   . VAL B 111 ? 2.25807 1.59007 2.73886 -0.26874 -0.34728 0.00189  111 VAL A O   
2310 C CB  . VAL B 111 ? 2.12259 1.66046 2.45984 -0.26260 -0.29751 0.09198  111 VAL A CB  
2311 C CG1 . VAL B 111 ? 2.12504 1.65306 2.51454 -0.30701 -0.30931 0.13962  111 VAL A CG1 
2312 C CG2 . VAL B 111 ? 2.08840 1.70893 2.35202 -0.24083 -0.27487 0.12627  111 VAL A CG2 
2313 N N   . THR B 112 ? 2.22814 1.56698 2.79980 -0.26658 -0.34300 0.16270  112 THR A N   
2314 C CA  . THR B 112 ? 2.28768 1.52246 2.96462 -0.29543 -0.36901 0.15456  112 THR A CA  
2315 C C   . THR B 112 ? 2.28690 1.54069 3.03351 -0.34124 -0.37308 0.23979  112 THR A C   
2316 O O   . THR B 112 ? 2.29448 1.57347 3.08130 -0.32728 -0.35582 0.34476  112 THR A O   
2317 C CB  . THR B 112 ? 2.36476 1.52218 3.11082 -0.25792 -0.37008 0.17653  112 THR A CB  
2318 O OG1 . THR B 112 ? 2.36065 1.58642 3.08834 -0.21870 -0.34815 0.26521  112 THR A OG1 
2319 C CG2 . THR B 112 ? 2.39455 1.50521 3.10408 -0.22174 -0.37217 0.07691  112 THR A CG2 
2320 N N   . VAL B 113 ? 2.44343 1.69420 3.20625 -0.39158 -0.39503 0.19962  113 VAL A N   
2321 C CA  . VAL B 113 ? 2.42694 1.69697 3.28259 -0.44145 -0.40301 0.27880  113 VAL A CA  
2322 C C   . VAL B 113 ? 2.48336 1.63550 3.49049 -0.46859 -0.43239 0.29169  113 VAL A C   
2323 O O   . VAL B 113 ? 2.52407 1.58980 3.56545 -0.49458 -0.47258 0.19721  113 VAL A O   
2324 C CB  . VAL B 113 ? 2.38546 1.71038 3.20859 -0.48479 -0.41975 0.23330  113 VAL A CB  
2325 C CG1 . VAL B 113 ? 2.35434 1.74349 3.25706 -0.52373 -0.41256 0.34069  113 VAL A CG1 
2326 C CG2 . VAL B 113 ? 2.34422 1.75085 3.01500 -0.45111 -0.39276 0.18556  113 VAL A CG2 
2327 N N   . SER B 114 ? 2.64719 1.79302 3.74363 -0.45837 -0.41158 0.40882  114 SER A N   
2328 C CA  . SER B 114 ? 2.70462 1.73164 3.95683 -0.47648 -0.43031 0.43611  114 SER A CA  
2329 C C   . SER B 114 ? 2.70419 1.68917 4.08609 -0.55558 -0.47275 0.42286  114 SER A C   
2330 O O   . SER B 114 ? 2.65582 1.71977 4.01019 -0.59361 -0.48476 0.40947  114 SER A O   
2331 C CB  . SER B 114 ? 2.71553 1.76525 4.03453 -0.44271 -0.39055 0.58406  114 SER A CB  
2332 O OG  . SER B 114 ? 2.66782 1.81224 4.02620 -0.46666 -0.36877 0.69494  114 SER A OG  
2333 N N   . SER B 115 ? 2.99759 1.85587 4.53127 -0.58020 -0.49760 0.42767  115 SER A N   
2334 C CA  . SER B 115 ? 3.01027 1.81446 4.70052 -0.66089 -0.54641 0.41758  115 SER A CA  
2335 C C   . SER B 115 ? 2.97195 1.84211 4.80766 -0.69203 -0.51910 0.58294  115 SER A C   
2336 O O   . SER B 115 ? 2.93721 1.86658 4.84788 -0.75300 -0.54112 0.60667  115 SER A O   
2337 C CB  . SER B 115 ? 3.10189 1.72574 4.90027 -0.67497 -0.58769 0.34204  115 SER A CB  
2338 O OG  . SER B 115 ? 3.13639 1.69767 5.04438 -0.64561 -0.55197 0.44965  115 SER A OG  
# 
