data_8XTA
# 
_entry.id   8XTA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8XTA         pdb_00008xta 10.2210/pdb8xta/pdb 
WWPDB D_1300044141 ?            ?                   
# 
_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       2024-11-20 
# 
_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                        8XTA 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-10 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8XT8 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              psy@ssu.ac.kr 
_pdbx_contact_author.name_first         SangYoun 
_pdbx_contact_author.name_last          Park 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9110-7249 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Park, S.' 1 ? 
'Kwon, N.' 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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            280 
_citation.language                  ? 
_citation.page_first                136036 
_citation.page_last                 136036 
_citation.title                     
;Crystal structure of a Clostridioides difficile multiple antibiotic resistance regulator (MarR) CD0473 suggests a potential redox-regulated function.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2024.136036 
_citation.pdbx_database_id_PubMed   39332572 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kwon, N.' 1 ? 
primary 'Rho, S.'  2 ? 
primary 'Ha, S.C.' 3 ? 
primary 'Park, S.' 4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'MarR family transcriptional regulator' 18673.393 1   ? ? ? WP_003434724 
2 polymer man 'MarR family transcriptional regulator' 16784.301 3   ? ? ? WP_003434724 
3 water   nat water                                   18.015    124 ? ? ? ?            
# 
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 
;MGSSHHHHHHSSGLVPRGSHMKDFEKLYEATTKLVSTSLKVKDDLKKMFKQNGYDITTDHYALLRFLWEQDGISQIDLCE
KSCKDKSNTTRILDVMKNKGLIVRKVDVKDRRKFQIFLTDLGRELEEPLNEIASIYATETFKSISDEELPLFTDILDRIG
K
;
;MGSSHHHHHHSSGLVPRGSHMKDFEKLYEATTKLVSTSLKVKDDLKKMFKQNGYDITTDHYALLRFLWEQDGISQIDLCE
KSCKDKSNTTRILDVMKNKGLIVRKVDVKDRRKFQIFLTDLGRELEEPLNEIASIYATETFKSISDEELPLFTDILDRIG
K
;
A     ? 
2 'polypeptide(L)' no no 
;GSHMKDFEKLYEATTKLVSTSLKVKDDLKKMFKQNGYDITTDHYALLRFLWEQDGISQIDLCEKSCKDKSNTTRILDVMK
NKGLIVRKVDVKDRRKFQIFLTDLGRELEEPLNEIASIYATETFKSISDEELPLFTDILDRIGK
;
;GSHMKDFEKLYEATTKLVSTSLKVKDDLKKMFKQNGYDITTDHYALLRFLWEQDGISQIDLCEKSCKDKSNTTRILDVMK
NKGLIVRKVDVKDRRKFQIFLTDLGRELEEPLNEIASIYATETFKSISDEELPLFTDILDRIGK
;
B,C,D ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  LYS n 
1 23  ASP n 
1 24  PHE n 
1 25  GLU n 
1 26  LYS n 
1 27  LEU n 
1 28  TYR n 
1 29  GLU n 
1 30  ALA n 
1 31  THR n 
1 32  THR n 
1 33  LYS n 
1 34  LEU n 
1 35  VAL n 
1 36  SER n 
1 37  THR n 
1 38  SER n 
1 39  LEU n 
1 40  LYS n 
1 41  VAL n 
1 42  LYS n 
1 43  ASP n 
1 44  ASP n 
1 45  LEU n 
1 46  LYS n 
1 47  LYS n 
1 48  MET n 
1 49  PHE n 
1 50  LYS n 
1 51  GLN n 
1 52  ASN n 
1 53  GLY n 
1 54  TYR n 
1 55  ASP n 
1 56  ILE n 
1 57  THR n 
1 58  THR n 
1 59  ASP n 
1 60  HIS n 
1 61  TYR n 
1 62  ALA n 
1 63  LEU n 
1 64  LEU n 
1 65  ARG n 
1 66  PHE n 
1 67  LEU n 
1 68  TRP n 
1 69  GLU n 
1 70  GLN n 
1 71  ASP n 
1 72  GLY n 
1 73  ILE n 
1 74  SER n 
1 75  GLN n 
1 76  ILE n 
1 77  ASP n 
1 78  LEU n 
1 79  CYS n 
1 80  GLU n 
1 81  LYS n 
1 82  SER n 
1 83  CYS n 
1 84  LYS n 
1 85  ASP n 
1 86  LYS n 
1 87  SER n 
1 88  ASN n 
1 89  THR n 
1 90  THR n 
1 91  ARG n 
1 92  ILE n 
1 93  LEU n 
1 94  ASP n 
1 95  VAL n 
1 96  MET n 
1 97  LYS n 
1 98  ASN n 
1 99  LYS n 
1 100 GLY n 
1 101 LEU n 
1 102 ILE n 
1 103 VAL n 
1 104 ARG n 
1 105 LYS n 
1 106 VAL n 
1 107 ASP n 
1 108 VAL n 
1 109 LYS n 
1 110 ASP n 
1 111 ARG n 
1 112 ARG n 
1 113 LYS n 
1 114 PHE n 
1 115 GLN n 
1 116 ILE n 
1 117 PHE n 
1 118 LEU n 
1 119 THR n 
1 120 ASP n 
1 121 LEU n 
1 122 GLY n 
1 123 ARG n 
1 124 GLU n 
1 125 LEU n 
1 126 GLU n 
1 127 GLU n 
1 128 PRO n 
1 129 LEU n 
1 130 ASN n 
1 131 GLU n 
1 132 ILE n 
1 133 ALA n 
1 134 SER n 
1 135 ILE n 
1 136 TYR n 
1 137 ALA n 
1 138 THR n 
1 139 GLU n 
1 140 THR n 
1 141 PHE n 
1 142 LYS n 
1 143 SER n 
1 144 ILE n 
1 145 SER n 
1 146 ASP n 
1 147 GLU n 
1 148 GLU n 
1 149 LEU n 
1 150 PRO n 
1 151 LEU n 
1 152 PHE n 
1 153 THR n 
1 154 ASP n 
1 155 ILE n 
1 156 LEU n 
1 157 ASP n 
1 158 ARG n 
1 159 ILE n 
1 160 GLY n 
1 161 LYS n 
2 1   GLY n 
2 2   SER n 
2 3   HIS n 
2 4   MET n 
2 5   LYS n 
2 6   ASP n 
2 7   PHE n 
2 8   GLU n 
2 9   LYS n 
2 10  LEU n 
2 11  TYR n 
2 12  GLU n 
2 13  ALA n 
2 14  THR n 
2 15  THR n 
2 16  LYS n 
2 17  LEU n 
2 18  VAL n 
2 19  SER n 
2 20  THR n 
2 21  SER n 
2 22  LEU n 
2 23  LYS n 
2 24  VAL n 
2 25  LYS n 
2 26  ASP n 
2 27  ASP n 
2 28  LEU n 
2 29  LYS n 
2 30  LYS n 
2 31  MET n 
2 32  PHE n 
2 33  LYS n 
2 34  GLN n 
2 35  ASN n 
2 36  GLY n 
2 37  TYR n 
2 38  ASP n 
2 39  ILE n 
2 40  THR n 
2 41  THR n 
2 42  ASP n 
2 43  HIS n 
2 44  TYR n 
2 45  ALA n 
2 46  LEU n 
2 47  LEU n 
2 48  ARG n 
2 49  PHE n 
2 50  LEU n 
2 51  TRP n 
2 52  GLU n 
2 53  GLN n 
2 54  ASP n 
2 55  GLY n 
2 56  ILE n 
2 57  SER n 
2 58  GLN n 
2 59  ILE n 
2 60  ASP n 
2 61  LEU n 
2 62  CYS n 
2 63  GLU n 
2 64  LYS n 
2 65  SER n 
2 66  CYS n 
2 67  LYS n 
2 68  ASP n 
2 69  LYS n 
2 70  SER n 
2 71  ASN n 
2 72  THR n 
2 73  THR n 
2 74  ARG n 
2 75  ILE n 
2 76  LEU n 
2 77  ASP n 
2 78  VAL n 
2 79  MET n 
2 80  LYS n 
2 81  ASN n 
2 82  LYS n 
2 83  GLY n 
2 84  LEU n 
2 85  ILE n 
2 86  VAL n 
2 87  ARG n 
2 88  LYS n 
2 89  VAL n 
2 90  ASP n 
2 91  VAL n 
2 92  LYS n 
2 93  ASP n 
2 94  ARG n 
2 95  ARG n 
2 96  LYS n 
2 97  PHE n 
2 98  GLN n 
2 99  ILE n 
2 100 PHE n 
2 101 LEU n 
2 102 THR n 
2 103 ASP n 
2 104 LEU n 
2 105 GLY n 
2 106 ARG n 
2 107 GLU n 
2 108 LEU n 
2 109 GLU n 
2 110 GLU n 
2 111 PRO n 
2 112 LEU n 
2 113 ASN n 
2 114 GLU n 
2 115 ILE n 
2 116 ALA n 
2 117 SER n 
2 118 ILE n 
2 119 TYR n 
2 120 ALA n 
2 121 THR n 
2 122 GLU n 
2 123 THR n 
2 124 PHE n 
2 125 LYS n 
2 126 SER n 
2 127 ILE n 
2 128 SER n 
2 129 ASP n 
2 130 GLU n 
2 131 GLU n 
2 132 LEU n 
2 133 PRO n 
2 134 LEU n 
2 135 PHE n 
2 136 THR n 
2 137 ASP n 
2 138 ILE n 
2 139 LEU n 
2 140 ASP n 
2 141 ARG n 
2 142 ILE n 
2 143 GLY n 
2 144 LYS 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' 1 161 ? ? 'mexR_2, SAMEA897059_03225' ? ? ? ? ? ? 'Clostridioides difficile' 1496 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 144 ? ? 'mexR_2, SAMEA897059_03225' ? ? ? ? ? ? 'Clostridioides difficile' 1496 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  -4  PRO PRO A . n 
A 1 17  ARG 17  -3  -3  ARG ARG A . n 
A 1 18  GLY 18  -2  -2  GLY GLY A . n 
A 1 19  SER 19  -1  -1  SER SER A . n 
A 1 20  HIS 20  0   0   HIS HIS A . n 
A 1 21  MET 21  1   1   MET MET A . n 
A 1 22  LYS 22  2   2   LYS LYS A . n 
A 1 23  ASP 23  3   3   ASP ASP A . n 
A 1 24  PHE 24  4   4   PHE PHE A . n 
A 1 25  GLU 25  5   5   GLU GLU A . n 
A 1 26  LYS 26  6   6   LYS LYS A . n 
A 1 27  LEU 27  7   7   LEU LEU A . n 
A 1 28  TYR 28  8   8   TYR TYR A . n 
A 1 29  GLU 29  9   9   GLU GLU A . n 
A 1 30  ALA 30  10  10  ALA ALA A . n 
A 1 31  THR 31  11  11  THR THR A . n 
A 1 32  THR 32  12  12  THR THR A . n 
A 1 33  LYS 33  13  13  LYS LYS A . n 
A 1 34  LEU 34  14  14  LEU LEU A . n 
A 1 35  VAL 35  15  15  VAL VAL A . n 
A 1 36  SER 36  16  16  SER SER A . n 
A 1 37  THR 37  17  17  THR THR A . n 
A 1 38  SER 38  18  18  SER SER A . n 
A 1 39  LEU 39  19  19  LEU LEU A . n 
A 1 40  LYS 40  20  20  LYS LYS A . n 
A 1 41  VAL 41  21  21  VAL VAL A . n 
A 1 42  LYS 42  22  22  LYS LYS A . n 
A 1 43  ASP 43  23  23  ASP ASP A . n 
A 1 44  ASP 44  24  24  ASP ASP A . n 
A 1 45  LEU 45  25  25  LEU LEU A . n 
A 1 46  LYS 46  26  26  LYS LYS A . n 
A 1 47  LYS 47  27  27  LYS LYS A . n 
A 1 48  MET 48  28  28  MET MET A . n 
A 1 49  PHE 49  29  29  PHE PHE A . n 
A 1 50  LYS 50  30  30  LYS LYS A . n 
A 1 51  GLN 51  31  31  GLN GLN A . n 
A 1 52  ASN 52  32  32  ASN ASN A . n 
A 1 53  GLY 53  33  33  GLY GLY A . n 
A 1 54  TYR 54  34  34  TYR TYR A . n 
A 1 55  ASP 55  35  35  ASP ASP A . n 
A 1 56  ILE 56  36  36  ILE ILE A . n 
A 1 57  THR 57  37  37  THR THR A . n 
A 1 58  THR 58  38  38  THR THR A . n 
A 1 59  ASP 59  39  39  ASP ASP A . n 
A 1 60  HIS 60  40  40  HIS HIS A . n 
A 1 61  TYR 61  41  41  TYR TYR A . n 
A 1 62  ALA 62  42  42  ALA ALA A . n 
A 1 63  LEU 63  43  43  LEU LEU A . n 
A 1 64  LEU 64  44  44  LEU LEU A . n 
A 1 65  ARG 65  45  45  ARG ARG A . n 
A 1 66  PHE 66  46  46  PHE PHE A . n 
A 1 67  LEU 67  47  47  LEU LEU A . n 
A 1 68  TRP 68  48  48  TRP TRP A . n 
A 1 69  GLU 69  49  49  GLU GLU A . n 
A 1 70  GLN 70  50  50  GLN GLN A . n 
A 1 71  ASP 71  51  51  ASP ASP A . n 
A 1 72  GLY 72  52  52  GLY GLY A . n 
A 1 73  ILE 73  53  53  ILE ILE A . n 
A 1 74  SER 74  54  54  SER SER A . n 
A 1 75  GLN 75  55  55  GLN GLN A . n 
A 1 76  ILE 76  56  56  ILE ILE A . n 
A 1 77  ASP 77  57  57  ASP ASP A . n 
A 1 78  LEU 78  58  58  LEU LEU A . n 
A 1 79  CYS 79  59  59  CYS CYS A . n 
A 1 80  GLU 80  60  60  GLU GLU A . n 
A 1 81  LYS 81  61  61  LYS LYS A . n 
A 1 82  SER 82  62  62  SER SER A . n 
A 1 83  CYS 83  63  63  CYS CYS A . n 
A 1 84  LYS 84  64  64  LYS LYS A . n 
A 1 85  ASP 85  65  65  ASP ASP A . n 
A 1 86  LYS 86  66  66  LYS LYS A . n 
A 1 87  SER 87  67  67  SER SER A . n 
A 1 88  ASN 88  68  68  ASN ASN A . n 
A 1 89  THR 89  69  69  THR THR A . n 
A 1 90  THR 90  70  70  THR THR A . n 
A 1 91  ARG 91  71  71  ARG ARG A . n 
A 1 92  ILE 92  72  72  ILE ILE A . n 
A 1 93  LEU 93  73  73  LEU LEU A . n 
A 1 94  ASP 94  74  74  ASP ASP A . n 
A 1 95  VAL 95  75  75  VAL VAL A . n 
A 1 96  MET 96  76  76  MET MET A . n 
A 1 97  LYS 97  77  77  LYS LYS A . n 
A 1 98  ASN 98  78  78  ASN ASN A . n 
A 1 99  LYS 99  79  79  LYS LYS A . n 
A 1 100 GLY 100 80  80  GLY GLY A . n 
A 1 101 LEU 101 81  81  LEU LEU A . n 
A 1 102 ILE 102 82  82  ILE ILE A . n 
A 1 103 VAL 103 83  83  VAL VAL A . n 
A 1 104 ARG 104 84  84  ARG ARG A . n 
A 1 105 LYS 105 85  85  LYS LYS A . n 
A 1 106 VAL 106 86  86  VAL VAL A . n 
A 1 107 ASP 107 87  87  ASP ASP A . n 
A 1 108 VAL 108 88  88  VAL VAL A . n 
A 1 109 LYS 109 89  89  LYS LYS A . n 
A 1 110 ASP 110 90  90  ASP ASP A . n 
A 1 111 ARG 111 91  91  ARG ARG A . n 
A 1 112 ARG 112 92  92  ARG ARG A . n 
A 1 113 LYS 113 93  93  LYS LYS A . n 
A 1 114 PHE 114 94  94  PHE PHE A . n 
A 1 115 GLN 115 95  95  GLN GLN A . n 
A 1 116 ILE 116 96  96  ILE ILE A . n 
A 1 117 PHE 117 97  97  PHE PHE A . n 
A 1 118 LEU 118 98  98  LEU LEU A . n 
A 1 119 THR 119 99  99  THR THR A . n 
A 1 120 ASP 120 100 100 ASP ASP A . n 
A 1 121 LEU 121 101 101 LEU LEU A . n 
A 1 122 GLY 122 102 102 GLY GLY A . n 
A 1 123 ARG 123 103 103 ARG ARG A . n 
A 1 124 GLU 124 104 104 GLU GLU A . n 
A 1 125 LEU 125 105 105 LEU LEU A . n 
A 1 126 GLU 126 106 106 GLU GLU A . n 
A 1 127 GLU 127 107 107 GLU GLU A . n 
A 1 128 PRO 128 108 108 PRO PRO A . n 
A 1 129 LEU 129 109 109 LEU LEU A . n 
A 1 130 ASN 130 110 110 ASN ASN A . n 
A 1 131 GLU 131 111 111 GLU GLU A . n 
A 1 132 ILE 132 112 112 ILE ILE A . n 
A 1 133 ALA 133 113 113 ALA ALA A . n 
A 1 134 SER 134 114 114 SER SER A . n 
A 1 135 ILE 135 115 115 ILE ILE A . n 
A 1 136 TYR 136 116 116 TYR TYR A . n 
A 1 137 ALA 137 117 117 ALA ALA A . n 
A 1 138 THR 138 118 118 THR THR A . n 
A 1 139 GLU 139 119 119 GLU GLU A . n 
A 1 140 THR 140 120 120 THR THR A . n 
A 1 141 PHE 141 121 121 PHE PHE A . n 
A 1 142 LYS 142 122 122 LYS LYS A . n 
A 1 143 SER 143 123 123 SER SER A . n 
A 1 144 ILE 144 124 124 ILE ILE A . n 
A 1 145 SER 145 125 125 SER SER A . n 
A 1 146 ASP 146 126 126 ASP ASP A . n 
A 1 147 GLU 147 127 127 GLU GLU A . n 
A 1 148 GLU 148 128 128 GLU GLU A . n 
A 1 149 LEU 149 129 129 LEU LEU A . n 
A 1 150 PRO 150 130 130 PRO PRO A . n 
A 1 151 LEU 151 131 131 LEU LEU A . n 
A 1 152 PHE 152 132 132 PHE PHE A . n 
A 1 153 THR 153 133 133 THR THR A . n 
A 1 154 ASP 154 134 134 ASP ASP A . n 
A 1 155 ILE 155 135 135 ILE ILE A . n 
A 1 156 LEU 156 136 136 LEU LEU A . n 
A 1 157 ASP 157 137 137 ASP ASP A . n 
A 1 158 ARG 158 138 138 ARG ARG A . n 
A 1 159 ILE 159 139 139 ILE ILE A . n 
A 1 160 GLY 160 140 140 GLY GLY A . n 
A 1 161 LYS 161 141 ?   ?   ?   A . n 
B 2 1   GLY 1   -2  ?   ?   ?   B . n 
B 2 2   SER 2   -1  ?   ?   ?   B . n 
B 2 3   HIS 3   0   ?   ?   ?   B . n 
B 2 4   MET 4   1   ?   ?   ?   B . n 
B 2 5   LYS 5   2   2   LYS LYS B . n 
B 2 6   ASP 6   3   3   ASP ASP B . n 
B 2 7   PHE 7   4   4   PHE PHE B . n 
B 2 8   GLU 8   5   5   GLU GLU B . n 
B 2 9   LYS 9   6   6   LYS LYS B . n 
B 2 10  LEU 10  7   7   LEU LEU B . n 
B 2 11  TYR 11  8   8   TYR TYR B . n 
B 2 12  GLU 12  9   9   GLU GLU B . n 
B 2 13  ALA 13  10  10  ALA ALA B . n 
B 2 14  THR 14  11  11  THR THR B . n 
B 2 15  THR 15  12  12  THR THR B . n 
B 2 16  LYS 16  13  13  LYS LYS B . n 
B 2 17  LEU 17  14  14  LEU LEU B . n 
B 2 18  VAL 18  15  15  VAL VAL B . n 
B 2 19  SER 19  16  16  SER SER B . n 
B 2 20  THR 20  17  17  THR THR B . n 
B 2 21  SER 21  18  18  SER SER B . n 
B 2 22  LEU 22  19  19  LEU LEU B . n 
B 2 23  LYS 23  20  20  LYS LYS B . n 
B 2 24  VAL 24  21  21  VAL VAL B . n 
B 2 25  LYS 25  22  22  LYS LYS B . n 
B 2 26  ASP 26  23  23  ASP ASP B . n 
B 2 27  ASP 27  24  24  ASP ASP B . n 
B 2 28  LEU 28  25  25  LEU LEU B . n 
B 2 29  LYS 29  26  26  LYS LYS B . n 
B 2 30  LYS 30  27  27  LYS LYS B . n 
B 2 31  MET 31  28  28  MET MET B . n 
B 2 32  PHE 32  29  29  PHE PHE B . n 
B 2 33  LYS 33  30  30  LYS LYS B . n 
B 2 34  GLN 34  31  31  GLN GLN B . n 
B 2 35  ASN 35  32  32  ASN ASN B . n 
B 2 36  GLY 36  33  33  GLY GLY B . n 
B 2 37  TYR 37  34  34  TYR TYR B . n 
B 2 38  ASP 38  35  35  ASP ASP B . n 
B 2 39  ILE 39  36  36  ILE ILE B . n 
B 2 40  THR 40  37  37  THR THR B . n 
B 2 41  THR 41  38  38  THR THR B . n 
B 2 42  ASP 42  39  39  ASP ASP B . n 
B 2 43  HIS 43  40  40  HIS HIS B . n 
B 2 44  TYR 44  41  41  TYR TYR B . n 
B 2 45  ALA 45  42  42  ALA ALA B . n 
B 2 46  LEU 46  43  43  LEU LEU B . n 
B 2 47  LEU 47  44  44  LEU LEU B . n 
B 2 48  ARG 48  45  45  ARG ARG B . n 
B 2 49  PHE 49  46  46  PHE PHE B . n 
B 2 50  LEU 50  47  47  LEU LEU B . n 
B 2 51  TRP 51  48  48  TRP TRP B . n 
B 2 52  GLU 52  49  49  GLU GLU B . n 
B 2 53  GLN 53  50  50  GLN GLN B . n 
B 2 54  ASP 54  51  51  ASP ASP B . n 
B 2 55  GLY 55  52  52  GLY GLY B . n 
B 2 56  ILE 56  53  53  ILE ILE B . n 
B 2 57  SER 57  54  54  SER SER B . n 
B 2 58  GLN 58  55  55  GLN GLN B . n 
B 2 59  ILE 59  56  56  ILE ILE B . n 
B 2 60  ASP 60  57  57  ASP ASP B . n 
B 2 61  LEU 61  58  58  LEU LEU B . n 
B 2 62  CYS 62  59  59  CYS CYS B . n 
B 2 63  GLU 63  60  60  GLU GLU B . n 
B 2 64  LYS 64  61  61  LYS LYS B . n 
B 2 65  SER 65  62  62  SER SER B . n 
B 2 66  CYS 66  63  63  CYS CYS B . n 
B 2 67  LYS 67  64  64  LYS LYS B . n 
B 2 68  ASP 68  65  65  ASP ASP B . n 
B 2 69  LYS 69  66  66  LYS LYS B . n 
B 2 70  SER 70  67  67  SER SER B . n 
B 2 71  ASN 71  68  68  ASN ASN B . n 
B 2 72  THR 72  69  69  THR THR B . n 
B 2 73  THR 73  70  70  THR THR B . n 
B 2 74  ARG 74  71  71  ARG ARG B . n 
B 2 75  ILE 75  72  72  ILE ILE B . n 
B 2 76  LEU 76  73  73  LEU LEU B . n 
B 2 77  ASP 77  74  74  ASP ASP B . n 
B 2 78  VAL 78  75  75  VAL VAL B . n 
B 2 79  MET 79  76  76  MET MET B . n 
B 2 80  LYS 80  77  77  LYS LYS B . n 
B 2 81  ASN 81  78  78  ASN ASN B . n 
B 2 82  LYS 82  79  79  LYS LYS B . n 
B 2 83  GLY 83  80  80  GLY GLY B . n 
B 2 84  LEU 84  81  81  LEU LEU B . n 
B 2 85  ILE 85  82  82  ILE ILE B . n 
B 2 86  VAL 86  83  83  VAL VAL B . n 
B 2 87  ARG 87  84  84  ARG ARG B . n 
B 2 88  LYS 88  85  85  LYS LYS B . n 
B 2 89  VAL 89  86  86  VAL VAL B . n 
B 2 90  ASP 90  87  87  ASP ASP B . n 
B 2 91  VAL 91  88  88  VAL VAL B . n 
B 2 92  LYS 92  89  89  LYS LYS B . n 
B 2 93  ASP 93  90  90  ASP ASP B . n 
B 2 94  ARG 94  91  91  ARG ARG B . n 
B 2 95  ARG 95  92  92  ARG ARG B . n 
B 2 96  LYS 96  93  93  LYS LYS B . n 
B 2 97  PHE 97  94  94  PHE PHE B . n 
B 2 98  GLN 98  95  95  GLN GLN B . n 
B 2 99  ILE 99  96  96  ILE ILE B . n 
B 2 100 PHE 100 97  97  PHE PHE B . n 
B 2 101 LEU 101 98  98  LEU LEU B . n 
B 2 102 THR 102 99  99  THR THR B . n 
B 2 103 ASP 103 100 100 ASP ASP B . n 
B 2 104 LEU 104 101 101 LEU LEU B . n 
B 2 105 GLY 105 102 102 GLY GLY B . n 
B 2 106 ARG 106 103 103 ARG ARG B . n 
B 2 107 GLU 107 104 104 GLU GLU B . n 
B 2 108 LEU 108 105 105 LEU LEU B . n 
B 2 109 GLU 109 106 106 GLU GLU B . n 
B 2 110 GLU 110 107 107 GLU GLU B . n 
B 2 111 PRO 111 108 108 PRO PRO B . n 
B 2 112 LEU 112 109 109 LEU LEU B . n 
B 2 113 ASN 113 110 110 ASN ASN B . n 
B 2 114 GLU 114 111 111 GLU GLU B . n 
B 2 115 ILE 115 112 112 ILE ILE B . n 
B 2 116 ALA 116 113 113 ALA ALA B . n 
B 2 117 SER 117 114 114 SER SER B . n 
B 2 118 ILE 118 115 115 ILE ILE B . n 
B 2 119 TYR 119 116 116 TYR TYR B . n 
B 2 120 ALA 120 117 117 ALA ALA B . n 
B 2 121 THR 121 118 118 THR THR B . n 
B 2 122 GLU 122 119 119 GLU GLU B . n 
B 2 123 THR 123 120 120 THR THR B . n 
B 2 124 PHE 124 121 121 PHE PHE B . n 
B 2 125 LYS 125 122 122 LYS LYS B . n 
B 2 126 SER 126 123 123 SER SER B . n 
B 2 127 ILE 127 124 124 ILE ILE B . n 
B 2 128 SER 128 125 125 SER SER B . n 
B 2 129 ASP 129 126 126 ASP ASP B . n 
B 2 130 GLU 130 127 127 GLU GLU B . n 
B 2 131 GLU 131 128 128 GLU GLU B . n 
B 2 132 LEU 132 129 129 LEU LEU B . n 
B 2 133 PRO 133 130 130 PRO PRO B . n 
B 2 134 LEU 134 131 131 LEU LEU B . n 
B 2 135 PHE 135 132 132 PHE PHE B . n 
B 2 136 THR 136 133 133 THR THR B . n 
B 2 137 ASP 137 134 134 ASP ASP B . n 
B 2 138 ILE 138 135 135 ILE ILE B . n 
B 2 139 LEU 139 136 136 LEU LEU B . n 
B 2 140 ASP 140 137 137 ASP ASP B . n 
B 2 141 ARG 141 138 138 ARG ARG B . n 
B 2 142 ILE 142 139 139 ILE ILE B . n 
B 2 143 GLY 143 140 140 GLY GLY B . n 
B 2 144 LYS 144 141 ?   ?   ?   B . n 
C 2 1   GLY 1   -2  ?   ?   ?   C . n 
C 2 2   SER 2   -1  ?   ?   ?   C . n 
C 2 3   HIS 3   0   ?   ?   ?   C . n 
C 2 4   MET 4   1   ?   ?   ?   C . n 
C 2 5   LYS 5   2   2   LYS LYS C . n 
C 2 6   ASP 6   3   3   ASP ASP C . n 
C 2 7   PHE 7   4   4   PHE PHE C . n 
C 2 8   GLU 8   5   5   GLU GLU C . n 
C 2 9   LYS 9   6   6   LYS LYS C . n 
C 2 10  LEU 10  7   7   LEU LEU C . n 
C 2 11  TYR 11  8   8   TYR TYR C . n 
C 2 12  GLU 12  9   9   GLU GLU C . n 
C 2 13  ALA 13  10  10  ALA ALA C . n 
C 2 14  THR 14  11  11  THR THR C . n 
C 2 15  THR 15  12  12  THR THR C . n 
C 2 16  LYS 16  13  13  LYS LYS C . n 
C 2 17  LEU 17  14  14  LEU LEU C . n 
C 2 18  VAL 18  15  15  VAL VAL C . n 
C 2 19  SER 19  16  16  SER SER C . n 
C 2 20  THR 20  17  17  THR THR C . n 
C 2 21  SER 21  18  18  SER SER C . n 
C 2 22  LEU 22  19  19  LEU LEU C . n 
C 2 23  LYS 23  20  20  LYS LYS C . n 
C 2 24  VAL 24  21  21  VAL VAL C . n 
C 2 25  LYS 25  22  22  LYS LYS C . n 
C 2 26  ASP 26  23  23  ASP ASP C . n 
C 2 27  ASP 27  24  24  ASP ASP C . n 
C 2 28  LEU 28  25  25  LEU LEU C . n 
C 2 29  LYS 29  26  26  LYS LYS C . n 
C 2 30  LYS 30  27  27  LYS LYS C . n 
C 2 31  MET 31  28  28  MET MET C . n 
C 2 32  PHE 32  29  29  PHE PHE C . n 
C 2 33  LYS 33  30  30  LYS LYS C . n 
C 2 34  GLN 34  31  31  GLN GLN C . n 
C 2 35  ASN 35  32  32  ASN ASN C . n 
C 2 36  GLY 36  33  33  GLY GLY C . n 
C 2 37  TYR 37  34  34  TYR TYR C . n 
C 2 38  ASP 38  35  35  ASP ASP C . n 
C 2 39  ILE 39  36  36  ILE ILE C . n 
C 2 40  THR 40  37  37  THR THR C . n 
C 2 41  THR 41  38  38  THR THR C . n 
C 2 42  ASP 42  39  39  ASP ASP C . n 
C 2 43  HIS 43  40  40  HIS HIS C . n 
C 2 44  TYR 44  41  41  TYR TYR C . n 
C 2 45  ALA 45  42  42  ALA ALA C . n 
C 2 46  LEU 46  43  43  LEU LEU C . n 
C 2 47  LEU 47  44  44  LEU LEU C . n 
C 2 48  ARG 48  45  45  ARG ARG C . n 
C 2 49  PHE 49  46  46  PHE PHE C . n 
C 2 50  LEU 50  47  47  LEU LEU C . n 
C 2 51  TRP 51  48  48  TRP TRP C . n 
C 2 52  GLU 52  49  49  GLU GLU C . n 
C 2 53  GLN 53  50  50  GLN GLN C . n 
C 2 54  ASP 54  51  51  ASP ASP C . n 
C 2 55  GLY 55  52  52  GLY GLY C . n 
C 2 56  ILE 56  53  53  ILE ILE C . n 
C 2 57  SER 57  54  54  SER SER C . n 
C 2 58  GLN 58  55  55  GLN GLN C . n 
C 2 59  ILE 59  56  56  ILE ILE C . n 
C 2 60  ASP 60  57  57  ASP ASP C . n 
C 2 61  LEU 61  58  58  LEU LEU C . n 
C 2 62  CYS 62  59  59  CYS CYS C . n 
C 2 63  GLU 63  60  60  GLU GLU C . n 
C 2 64  LYS 64  61  61  LYS LYS C . n 
C 2 65  SER 65  62  62  SER SER C . n 
C 2 66  CYS 66  63  63  CYS CYS C . n 
C 2 67  LYS 67  64  64  LYS LYS C . n 
C 2 68  ASP 68  65  65  ASP ASP C . n 
C 2 69  LYS 69  66  66  LYS LYS C . n 
C 2 70  SER 70  67  67  SER SER C . n 
C 2 71  ASN 71  68  68  ASN ASN C . n 
C 2 72  THR 72  69  69  THR THR C . n 
C 2 73  THR 73  70  70  THR THR C . n 
C 2 74  ARG 74  71  71  ARG ARG C . n 
C 2 75  ILE 75  72  72  ILE ILE C . n 
C 2 76  LEU 76  73  73  LEU LEU C . n 
C 2 77  ASP 77  74  74  ASP ASP C . n 
C 2 78  VAL 78  75  75  VAL VAL C . n 
C 2 79  MET 79  76  76  MET MET C . n 
C 2 80  LYS 80  77  77  LYS LYS C . n 
C 2 81  ASN 81  78  78  ASN ASN C . n 
C 2 82  LYS 82  79  79  LYS LYS C . n 
C 2 83  GLY 83  80  80  GLY GLY C . n 
C 2 84  LEU 84  81  81  LEU LEU C . n 
C 2 85  ILE 85  82  82  ILE ILE C . n 
C 2 86  VAL 86  83  83  VAL VAL C . n 
C 2 87  ARG 87  84  84  ARG ARG C . n 
C 2 88  LYS 88  85  85  LYS LYS C . n 
C 2 89  VAL 89  86  86  VAL VAL C . n 
C 2 90  ASP 90  87  87  ASP ASP C . n 
C 2 91  VAL 91  88  88  VAL VAL C . n 
C 2 92  LYS 92  89  89  LYS LYS C . n 
C 2 93  ASP 93  90  90  ASP ASP C . n 
C 2 94  ARG 94  91  91  ARG ARG C . n 
C 2 95  ARG 95  92  92  ARG ARG C . n 
C 2 96  LYS 96  93  93  LYS LYS C . n 
C 2 97  PHE 97  94  94  PHE PHE C . n 
C 2 98  GLN 98  95  95  GLN GLN C . n 
C 2 99  ILE 99  96  96  ILE ILE C . n 
C 2 100 PHE 100 97  97  PHE PHE C . n 
C 2 101 LEU 101 98  98  LEU LEU C . n 
C 2 102 THR 102 99  99  THR THR C . n 
C 2 103 ASP 103 100 100 ASP ASP C . n 
C 2 104 LEU 104 101 101 LEU LEU C . n 
C 2 105 GLY 105 102 102 GLY GLY C . n 
C 2 106 ARG 106 103 103 ARG ARG C . n 
C 2 107 GLU 107 104 104 GLU GLU C . n 
C 2 108 LEU 108 105 105 LEU LEU C . n 
C 2 109 GLU 109 106 106 GLU GLU C . n 
C 2 110 GLU 110 107 107 GLU GLU C . n 
C 2 111 PRO 111 108 108 PRO PRO C . n 
C 2 112 LEU 112 109 109 LEU LEU C . n 
C 2 113 ASN 113 110 110 ASN ASN C . n 
C 2 114 GLU 114 111 111 GLU GLU C . n 
C 2 115 ILE 115 112 112 ILE ILE C . n 
C 2 116 ALA 116 113 113 ALA ALA C . n 
C 2 117 SER 117 114 114 SER SER C . n 
C 2 118 ILE 118 115 115 ILE ILE C . n 
C 2 119 TYR 119 116 116 TYR TYR C . n 
C 2 120 ALA 120 117 117 ALA ALA C . n 
C 2 121 THR 121 118 118 THR THR C . n 
C 2 122 GLU 122 119 119 GLU GLU C . n 
C 2 123 THR 123 120 120 THR THR C . n 
C 2 124 PHE 124 121 121 PHE PHE C . n 
C 2 125 LYS 125 122 122 LYS LYS C . n 
C 2 126 SER 126 123 123 SER SER C . n 
C 2 127 ILE 127 124 124 ILE ILE C . n 
C 2 128 SER 128 125 125 SER SER C . n 
C 2 129 ASP 129 126 126 ASP ASP C . n 
C 2 130 GLU 130 127 127 GLU GLU C . n 
C 2 131 GLU 131 128 128 GLU GLU C . n 
C 2 132 LEU 132 129 129 LEU LEU C . n 
C 2 133 PRO 133 130 130 PRO PRO C . n 
C 2 134 LEU 134 131 131 LEU LEU C . n 
C 2 135 PHE 135 132 132 PHE PHE C . n 
C 2 136 THR 136 133 133 THR THR C . n 
C 2 137 ASP 137 134 134 ASP ASP C . n 
C 2 138 ILE 138 135 135 ILE ILE C . n 
C 2 139 LEU 139 136 136 LEU LEU C . n 
C 2 140 ASP 140 137 137 ASP ASP C . n 
C 2 141 ARG 141 138 138 ARG ARG C . n 
C 2 142 ILE 142 139 139 ILE ILE C . n 
C 2 143 GLY 143 140 140 GLY GLY C . n 
C 2 144 LYS 144 141 ?   ?   ?   C . n 
D 2 1   GLY 1   -2  ?   ?   ?   D . n 
D 2 2   SER 2   -1  ?   ?   ?   D . n 
D 2 3   HIS 3   0   ?   ?   ?   D . n 
D 2 4   MET 4   1   ?   ?   ?   D . n 
D 2 5   LYS 5   2   2   LYS LYS D . n 
D 2 6   ASP 6   3   3   ASP ASP D . n 
D 2 7   PHE 7   4   4   PHE PHE D . n 
D 2 8   GLU 8   5   5   GLU GLU D . n 
D 2 9   LYS 9   6   6   LYS LYS D . n 
D 2 10  LEU 10  7   7   LEU LEU D . n 
D 2 11  TYR 11  8   8   TYR TYR D . n 
D 2 12  GLU 12  9   9   GLU GLU D . n 
D 2 13  ALA 13  10  10  ALA ALA D . n 
D 2 14  THR 14  11  11  THR THR D . n 
D 2 15  THR 15  12  12  THR THR D . n 
D 2 16  LYS 16  13  13  LYS LYS D . n 
D 2 17  LEU 17  14  14  LEU LEU D . n 
D 2 18  VAL 18  15  15  VAL VAL D . n 
D 2 19  SER 19  16  16  SER SER D . n 
D 2 20  THR 20  17  17  THR THR D . n 
D 2 21  SER 21  18  18  SER SER D . n 
D 2 22  LEU 22  19  19  LEU LEU D . n 
D 2 23  LYS 23  20  20  LYS LYS D . n 
D 2 24  VAL 24  21  21  VAL VAL D . n 
D 2 25  LYS 25  22  22  LYS LYS D . n 
D 2 26  ASP 26  23  23  ASP ASP D . n 
D 2 27  ASP 27  24  24  ASP ASP D . n 
D 2 28  LEU 28  25  25  LEU LEU D . n 
D 2 29  LYS 29  26  26  LYS LYS D . n 
D 2 30  LYS 30  27  27  LYS LYS D . n 
D 2 31  MET 31  28  28  MET MET D . n 
D 2 32  PHE 32  29  29  PHE PHE D . n 
D 2 33  LYS 33  30  30  LYS LYS D . n 
D 2 34  GLN 34  31  31  GLN GLN D . n 
D 2 35  ASN 35  32  32  ASN ASN D . n 
D 2 36  GLY 36  33  33  GLY GLY D . n 
D 2 37  TYR 37  34  34  TYR TYR D . n 
D 2 38  ASP 38  35  35  ASP ASP D . n 
D 2 39  ILE 39  36  36  ILE ILE D . n 
D 2 40  THR 40  37  37  THR THR D . n 
D 2 41  THR 41  38  38  THR THR D . n 
D 2 42  ASP 42  39  39  ASP ASP D . n 
D 2 43  HIS 43  40  40  HIS HIS D . n 
D 2 44  TYR 44  41  41  TYR TYR D . n 
D 2 45  ALA 45  42  42  ALA ALA D . n 
D 2 46  LEU 46  43  43  LEU LEU D . n 
D 2 47  LEU 47  44  44  LEU LEU D . n 
D 2 48  ARG 48  45  45  ARG ARG D . n 
D 2 49  PHE 49  46  46  PHE PHE D . n 
D 2 50  LEU 50  47  47  LEU LEU D . n 
D 2 51  TRP 51  48  48  TRP TRP D . n 
D 2 52  GLU 52  49  49  GLU GLU D . n 
D 2 53  GLN 53  50  50  GLN GLN D . n 
D 2 54  ASP 54  51  51  ASP ASP D . n 
D 2 55  GLY 55  52  52  GLY GLY D . n 
D 2 56  ILE 56  53  53  ILE ILE D . n 
D 2 57  SER 57  54  54  SER SER D . n 
D 2 58  GLN 58  55  55  GLN GLN D . n 
D 2 59  ILE 59  56  56  ILE ILE D . n 
D 2 60  ASP 60  57  57  ASP ASP D . n 
D 2 61  LEU 61  58  58  LEU LEU D . n 
D 2 62  CYS 62  59  59  CYS CYS D . n 
D 2 63  GLU 63  60  60  GLU GLU D . n 
D 2 64  LYS 64  61  61  LYS LYS D . n 
D 2 65  SER 65  62  62  SER SER D . n 
D 2 66  CYS 66  63  63  CYS CYS D . n 
D 2 67  LYS 67  64  64  LYS LYS D . n 
D 2 68  ASP 68  65  65  ASP ASP D . n 
D 2 69  LYS 69  66  66  LYS LYS D . n 
D 2 70  SER 70  67  67  SER SER D . n 
D 2 71  ASN 71  68  68  ASN ASN D . n 
D 2 72  THR 72  69  69  THR THR D . n 
D 2 73  THR 73  70  70  THR THR D . n 
D 2 74  ARG 74  71  71  ARG ARG D . n 
D 2 75  ILE 75  72  72  ILE ILE D . n 
D 2 76  LEU 76  73  73  LEU LEU D . n 
D 2 77  ASP 77  74  74  ASP ASP D . n 
D 2 78  VAL 78  75  75  VAL VAL D . n 
D 2 79  MET 79  76  76  MET MET D . n 
D 2 80  LYS 80  77  77  LYS LYS D . n 
D 2 81  ASN 81  78  78  ASN ASN D . n 
D 2 82  LYS 82  79  79  LYS LYS D . n 
D 2 83  GLY 83  80  80  GLY GLY D . n 
D 2 84  LEU 84  81  81  LEU LEU D . n 
D 2 85  ILE 85  82  82  ILE ILE D . n 
D 2 86  VAL 86  83  83  VAL VAL D . n 
D 2 87  ARG 87  84  84  ARG ARG D . n 
D 2 88  LYS 88  85  85  LYS LYS D . n 
D 2 89  VAL 89  86  86  VAL VAL D . n 
D 2 90  ASP 90  87  87  ASP ASP D . n 
D 2 91  VAL 91  88  88  VAL VAL D . n 
D 2 92  LYS 92  89  89  LYS LYS D . n 
D 2 93  ASP 93  90  90  ASP ASP D . n 
D 2 94  ARG 94  91  91  ARG ARG D . n 
D 2 95  ARG 95  92  92  ARG ARG D . n 
D 2 96  LYS 96  93  93  LYS LYS D . n 
D 2 97  PHE 97  94  94  PHE PHE D . n 
D 2 98  GLN 98  95  95  GLN GLN D . n 
D 2 99  ILE 99  96  96  ILE ILE D . n 
D 2 100 PHE 100 97  97  PHE PHE D . n 
D 2 101 LEU 101 98  98  LEU LEU D . n 
D 2 102 THR 102 99  99  THR THR D . n 
D 2 103 ASP 103 100 100 ASP ASP D . n 
D 2 104 LEU 104 101 101 LEU LEU D . n 
D 2 105 GLY 105 102 102 GLY GLY D . n 
D 2 106 ARG 106 103 103 ARG ARG D . n 
D 2 107 GLU 107 104 104 GLU GLU D . n 
D 2 108 LEU 108 105 105 LEU LEU D . n 
D 2 109 GLU 109 106 106 GLU GLU D . n 
D 2 110 GLU 110 107 107 GLU GLU D . n 
D 2 111 PRO 111 108 108 PRO PRO D . n 
D 2 112 LEU 112 109 109 LEU LEU D . n 
D 2 113 ASN 113 110 110 ASN ASN D . n 
D 2 114 GLU 114 111 111 GLU GLU D . n 
D 2 115 ILE 115 112 112 ILE ILE D . n 
D 2 116 ALA 116 113 113 ALA ALA D . n 
D 2 117 SER 117 114 114 SER SER D . n 
D 2 118 ILE 118 115 115 ILE ILE D . n 
D 2 119 TYR 119 116 116 TYR TYR D . n 
D 2 120 ALA 120 117 117 ALA ALA D . n 
D 2 121 THR 121 118 118 THR THR D . n 
D 2 122 GLU 122 119 119 GLU GLU D . n 
D 2 123 THR 123 120 120 THR THR D . n 
D 2 124 PHE 124 121 121 PHE PHE D . n 
D 2 125 LYS 125 122 122 LYS LYS D . n 
D 2 126 SER 126 123 123 SER SER D . n 
D 2 127 ILE 127 124 124 ILE ILE D . n 
D 2 128 SER 128 125 125 SER SER D . n 
D 2 129 ASP 129 126 126 ASP ASP D . n 
D 2 130 GLU 130 127 127 GLU GLU D . n 
D 2 131 GLU 131 128 128 GLU GLU D . n 
D 2 132 LEU 132 129 129 LEU LEU D . n 
D 2 133 PRO 133 130 130 PRO PRO D . n 
D 2 134 LEU 134 131 131 LEU LEU D . n 
D 2 135 PHE 135 132 132 PHE PHE D . n 
D 2 136 THR 136 133 133 THR THR D . n 
D 2 137 ASP 137 134 134 ASP ASP D . n 
D 2 138 ILE 138 135 135 ILE ILE D . n 
D 2 139 LEU 139 136 136 LEU LEU D . n 
D 2 140 ASP 140 137 137 ASP ASP D . n 
D 2 141 ARG 141 138 138 ARG ARG D . n 
D 2 142 ILE 142 139 139 ILE ILE D . n 
D 2 143 GLY 143 140 140 GLY GLY D . n 
D 2 144 LYS 144 141 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 HOH 1  201 71  HOH HOH A . 
E 3 HOH 2  202 61  HOH HOH A . 
E 3 HOH 3  203 41  HOH HOH A . 
E 3 HOH 4  204 39  HOH HOH A . 
E 3 HOH 5  205 83  HOH HOH A . 
E 3 HOH 6  206 93  HOH HOH A . 
E 3 HOH 7  207 19  HOH HOH A . 
E 3 HOH 8  208 35  HOH HOH A . 
E 3 HOH 9  209 22  HOH HOH A . 
E 3 HOH 10 210 57  HOH HOH A . 
E 3 HOH 11 211 58  HOH HOH A . 
E 3 HOH 12 212 54  HOH HOH A . 
E 3 HOH 13 213 14  HOH HOH A . 
E 3 HOH 14 214 20  HOH HOH A . 
E 3 HOH 15 215 60  HOH HOH A . 
E 3 HOH 16 216 109 HOH HOH A . 
E 3 HOH 17 217 103 HOH HOH A . 
E 3 HOH 18 218 44  HOH HOH A . 
E 3 HOH 19 219 3   HOH HOH A . 
E 3 HOH 20 220 1   HOH HOH A . 
E 3 HOH 21 221 67  HOH HOH A . 
E 3 HOH 22 222 26  HOH HOH A . 
E 3 HOH 23 223 49  HOH HOH A . 
E 3 HOH 24 224 38  HOH HOH A . 
E 3 HOH 25 225 56  HOH HOH A . 
E 3 HOH 26 226 21  HOH HOH A . 
E 3 HOH 27 227 16  HOH HOH A . 
E 3 HOH 28 228 113 HOH HOH A . 
E 3 HOH 29 229 117 HOH HOH A . 
E 3 HOH 30 230 104 HOH HOH A . 
E 3 HOH 31 231 50  HOH HOH A . 
E 3 HOH 32 232 118 HOH HOH A . 
E 3 HOH 33 233 99  HOH HOH A . 
E 3 HOH 34 234 116 HOH HOH A . 
E 3 HOH 35 235 48  HOH HOH A . 
F 3 HOH 1  201 95  HOH HOH B . 
F 3 HOH 2  202 66  HOH HOH B . 
F 3 HOH 3  203 40  HOH HOH B . 
F 3 HOH 4  204 102 HOH HOH B . 
F 3 HOH 5  205 92  HOH HOH B . 
F 3 HOH 6  206 10  HOH HOH B . 
F 3 HOH 7  207 36  HOH HOH B . 
F 3 HOH 8  208 51  HOH HOH B . 
F 3 HOH 9  209 11  HOH HOH B . 
F 3 HOH 10 210 68  HOH HOH B . 
F 3 HOH 11 211 55  HOH HOH B . 
F 3 HOH 12 212 96  HOH HOH B . 
F 3 HOH 13 213 17  HOH HOH B . 
F 3 HOH 14 214 8   HOH HOH B . 
F 3 HOH 15 215 5   HOH HOH B . 
F 3 HOH 16 216 62  HOH HOH B . 
F 3 HOH 17 217 97  HOH HOH B . 
F 3 HOH 18 218 78  HOH HOH B . 
F 3 HOH 19 219 89  HOH HOH B . 
F 3 HOH 20 220 65  HOH HOH B . 
F 3 HOH 21 221 23  HOH HOH B . 
F 3 HOH 22 222 70  HOH HOH B . 
F 3 HOH 23 223 46  HOH HOH B . 
F 3 HOH 24 224 37  HOH HOH B . 
F 3 HOH 25 225 64  HOH HOH B . 
F 3 HOH 26 226 13  HOH HOH B . 
F 3 HOH 27 227 72  HOH HOH B . 
F 3 HOH 28 228 12  HOH HOH B . 
F 3 HOH 29 229 27  HOH HOH B . 
F 3 HOH 30 230 53  HOH HOH B . 
F 3 HOH 31 231 76  HOH HOH B . 
F 3 HOH 32 232 6   HOH HOH B . 
F 3 HOH 33 233 7   HOH HOH B . 
F 3 HOH 34 234 31  HOH HOH B . 
F 3 HOH 35 235 9   HOH HOH B . 
F 3 HOH 36 236 15  HOH HOH B . 
F 3 HOH 37 237 63  HOH HOH B . 
F 3 HOH 38 238 52  HOH HOH B . 
F 3 HOH 39 239 101 HOH HOH B . 
F 3 HOH 40 240 112 HOH HOH B . 
F 3 HOH 41 241 4   HOH HOH B . 
F 3 HOH 42 242 98  HOH HOH B . 
F 3 HOH 43 243 34  HOH HOH B . 
F 3 HOH 44 244 45  HOH HOH B . 
F 3 HOH 45 245 111 HOH HOH B . 
F 3 HOH 46 246 94  HOH HOH B . 
F 3 HOH 47 247 25  HOH HOH B . 
F 3 HOH 48 248 28  HOH HOH B . 
F 3 HOH 49 249 18  HOH HOH B . 
F 3 HOH 50 250 24  HOH HOH B . 
F 3 HOH 51 251 100 HOH HOH B . 
F 3 HOH 52 252 115 HOH HOH B . 
F 3 HOH 53 253 32  HOH HOH B . 
G 3 HOH 1  201 82  HOH HOH C . 
G 3 HOH 2  202 59  HOH HOH C . 
G 3 HOH 3  203 87  HOH HOH C . 
G 3 HOH 4  204 119 HOH HOH C . 
G 3 HOH 5  205 106 HOH HOH C . 
G 3 HOH 6  206 43  HOH HOH C . 
G 3 HOH 7  207 91  HOH HOH C . 
G 3 HOH 8  208 85  HOH HOH C . 
G 3 HOH 9  209 47  HOH HOH C . 
G 3 HOH 10 210 74  HOH HOH C . 
G 3 HOH 11 211 84  HOH HOH C . 
G 3 HOH 12 212 105 HOH HOH C . 
G 3 HOH 13 213 114 HOH HOH C . 
G 3 HOH 14 214 90  HOH HOH C . 
G 3 HOH 15 215 73  HOH HOH C . 
G 3 HOH 16 216 79  HOH HOH C . 
G 3 HOH 17 217 69  HOH HOH C . 
G 3 HOH 18 218 88  HOH HOH C . 
G 3 HOH 19 219 125 HOH HOH C . 
G 3 HOH 20 220 108 HOH HOH C . 
G 3 HOH 21 221 123 HOH HOH C . 
G 3 HOH 22 222 124 HOH HOH C . 
G 3 HOH 23 223 120 HOH HOH C . 
H 3 HOH 1  201 81  HOH HOH D . 
H 3 HOH 2  202 33  HOH HOH D . 
H 3 HOH 3  203 29  HOH HOH D . 
H 3 HOH 4  204 30  HOH HOH D . 
H 3 HOH 5  205 75  HOH HOH D . 
H 3 HOH 6  206 86  HOH HOH D . 
H 3 HOH 7  207 80  HOH HOH D . 
H 3 HOH 8  208 2   HOH HOH D . 
H 3 HOH 9  209 77  HOH HOH D . 
H 3 HOH 10 210 122 HOH HOH D . 
H 3 HOH 11 211 121 HOH HOH D . 
H 3 HOH 12 212 110 HOH HOH D . 
H 3 HOH 13 213 42  HOH HOH D . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0049 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XTA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     176.483 
_cell.length_a_esd                 ? 
_cell.length_b                     69.402 
_cell.length_b_esd                 ? 
_cell.length_c                     95.007 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         8XTA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8XTA 
_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             4.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          70.82 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '3.0 M NaCl, 0.1 M sodium acetate pH 4.5, and 10 mM DTT' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 210' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-21 
_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   0.97933 
_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                        'PAL/PLS BEAMLINE 7A (6B, 6C1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97933 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   '7A (6B, 6C1)' 
_diffrn_source.pdbx_synchrotron_site       PAL/PLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XTA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.5 
_reflns.d_resolution_low                               95.01 
_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                                     41080 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          30.1 
_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                                   0.995 
_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                                    2.50 
_reflns_shell.d_res_low                                     2.54 
_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                             1988 
_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                                  0.781 
_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]                            2.50 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -1.70 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.80 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               60.444 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.946 
_refine.correlation_coeff_Fo_to_Fc_free          0.906 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8XTA 
_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                            2.50 
_refine.ls_d_res_low                             95.01 
_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                     38935 
_refine.ls_number_reflns_R_free                  2060 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.77 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21241 
_refine.ls_R_factor_R_free                       0.26019 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20997 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.260 
_refine.pdbx_overall_ESU_R_Free                  0.231 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             7.821 
_refine.overall_SU_ML                            0.170 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        95.01 
_refine_hist.number_atoms_solvent             124 
_refine_hist.number_atoms_total               4726 
_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        4602 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.018  0.020  4664  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  4620  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.027  1.987  6255  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.917  3.000  10697 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.239  5.000  558   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 39.349 24.908 218   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 22.016 15.000 968   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.874 15.000 29    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.106  0.200  721   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  5061  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  978   ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 5.912  5.675  2244  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.912  5.674  2243  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 8.486  8.491  2798  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 8.485  8.492  2799  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.900  6.258  2418  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 6.899  6.259  2419  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 10.475 9.073  3457  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 13.234 44.239 5539  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 13.240 44.211 5520  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.503 
_refine_ls_shell.d_res_low                        2.567 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             155 
_refine_ls_shell.number_reflns_R_work             2786 
_refine_ls_shell.percent_reflns_obs               98.03 
_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                  0.338 
_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   20 
_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                  0.402 
# 
_struct.entry_id                     8XTA 
_struct.title                        'Clostridioides difficile MarR (WP_003434724)' 
_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        8XTA 
_struct_keywords.text            'MarR, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP A0A9X9QLH1_CLODI A0A9X9QLH1 ? 1 
;MKDFEKLYEATTKLVSTSLKVKDDLKKMFKQNGYDITTDHYALLRFLWEQDGISQIDLCEKSCKDKSNTTRILDVMKNKG
LIVRKVDVKDRRKFQIFLTDLGRELEEPLNEIASIYATETFKSISDEELPLFTDILDRIGK
;
13 
2 UNP A0A9X9QLH1_CLODI A0A9X9QLH1 ? 2 
;MKDFEKLYEATTKLVSTSLKVKDDLKKMFKQNGYDITTDHYALLRFLWEQDGISQIDLCEKSCKDKSNTTRILDVMKNKG
LIVRKVDVKDRRKFQIFLTDLGRELEEPLNEIASIYATETFKSISDEELPLFTDILDRIGK
;
13 
# 
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 8XTA A 21 ? 161 ? A0A9X9QLH1 13 ? 153 ? 1 141 
2 2 8XTA B 4  ? 144 ? A0A9X9QLH1 13 ? 153 ? 1 141 
3 2 8XTA C 4  ? 144 ? A0A9X9QLH1 13 ? 153 ? 1 141 
4 2 8XTA D 4  ? 144 ? A0A9X9QLH1 13 ? 153 ? 1 141 
# 
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 8XTA MET A 1  ? UNP A0A9X9QLH1 ? ? 'initiating methionine' -19 1  
1 8XTA GLY A 2  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -18 2  
1 8XTA SER A 3  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -17 3  
1 8XTA SER A 4  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -16 4  
1 8XTA HIS A 5  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -15 5  
1 8XTA HIS A 6  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -14 6  
1 8XTA HIS A 7  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -13 7  
1 8XTA HIS A 8  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -12 8  
1 8XTA HIS A 9  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -11 9  
1 8XTA HIS A 10 ? UNP A0A9X9QLH1 ? ? 'expression tag'        -10 10 
1 8XTA SER A 11 ? UNP A0A9X9QLH1 ? ? 'expression tag'        -9  11 
1 8XTA SER A 12 ? UNP A0A9X9QLH1 ? ? 'expression tag'        -8  12 
1 8XTA GLY A 13 ? UNP A0A9X9QLH1 ? ? 'expression tag'        -7  13 
1 8XTA LEU A 14 ? UNP A0A9X9QLH1 ? ? 'expression tag'        -6  14 
1 8XTA VAL A 15 ? UNP A0A9X9QLH1 ? ? 'expression tag'        -5  15 
1 8XTA PRO A 16 ? UNP A0A9X9QLH1 ? ? 'expression tag'        -4  16 
1 8XTA ARG A 17 ? UNP A0A9X9QLH1 ? ? 'expression tag'        -3  17 
1 8XTA GLY A 18 ? UNP A0A9X9QLH1 ? ? 'expression tag'        -2  18 
1 8XTA SER A 19 ? UNP A0A9X9QLH1 ? ? 'expression tag'        -1  19 
1 8XTA HIS A 20 ? UNP A0A9X9QLH1 ? ? 'expression tag'        0   20 
2 8XTA GLY B 1  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -2  21 
2 8XTA SER B 2  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -1  22 
2 8XTA HIS B 3  ? UNP A0A9X9QLH1 ? ? 'expression tag'        0   23 
3 8XTA GLY C 1  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -2  24 
3 8XTA SER C 2  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -1  25 
3 8XTA HIS C 3  ? UNP A0A9X9QLH1 ? ? 'expression tag'        0   26 
4 8XTA GLY D 1  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -2  27 
4 8XTA SER D 2  ? UNP A0A9X9QLH1 ? ? 'expression tag'        -1  28 
4 8XTA HIS D 3  ? UNP A0A9X9QLH1 ? ? 'expression tag'        0   29 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4920  ? 
1 MORE         -38   ? 
1 'SSA (A^2)'  15990 ? 
2 'ABSA (A^2)' 4730  ? 
2 MORE         -37   ? 
2 'SSA (A^2)'  14980 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F 
2 1 C,D,G,H 
# 
_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 ASP A 23  ? MET A 48  ? ASP A 3   MET A 28  1 ? 26 
HELX_P HELX_P2  AA2 THR A 57  ? GLN A 70  ? THR A 37  GLN A 50  1 ? 14 
HELX_P HELX_P3  AA3 SER A 74  ? SER A 82  ? SER A 54  SER A 62  1 ? 9  
HELX_P HELX_P4  AA4 ASP A 85  ? GLY A 100 ? ASP A 65  GLY A 80  1 ? 16 
HELX_P HELX_P5  AA5 THR A 119 ? LEU A 125 ? THR A 99  LEU A 105 1 ? 7  
HELX_P HELX_P6  AA6 LEU A 125 ? PHE A 141 ? LEU A 105 PHE A 121 1 ? 17 
HELX_P HELX_P7  AA7 GLU A 147 ? ILE A 159 ? GLU A 127 ILE A 139 1 ? 13 
HELX_P HELX_P8  AA8 ASP B 6   ? ASN B 35  ? ASP B 3   ASN B 32  1 ? 30 
HELX_P HELX_P9  AA9 THR B 40  ? GLN B 53  ? THR B 37  GLN B 50  1 ? 14 
HELX_P HELX_P10 AB1 SER B 57  ? SER B 65  ? SER B 54  SER B 62  1 ? 9  
HELX_P HELX_P11 AB2 ASP B 68  ? LYS B 82  ? ASP B 65  LYS B 79  1 ? 15 
HELX_P HELX_P12 AB3 THR B 102 ? LEU B 108 ? THR B 99  LEU B 105 1 ? 7  
HELX_P HELX_P13 AB4 LEU B 108 ? PHE B 124 ? LEU B 105 PHE B 121 1 ? 17 
HELX_P HELX_P14 AB5 SER B 128 ? GLU B 130 ? SER B 125 GLU B 127 5 ? 3  
HELX_P HELX_P15 AB6 GLU B 131 ? ILE B 142 ? GLU B 128 ILE B 139 1 ? 12 
HELX_P HELX_P16 AB7 ASP C 6   ? ASN C 35  ? ASP C 3   ASN C 32  1 ? 30 
HELX_P HELX_P17 AB8 THR C 40  ? GLN C 53  ? THR C 37  GLN C 50  1 ? 14 
HELX_P HELX_P18 AB9 SER C 57  ? SER C 65  ? SER C 54  SER C 62  1 ? 9  
HELX_P HELX_P19 AC1 ASP C 68  ? LYS C 82  ? ASP C 65  LYS C 79  1 ? 15 
HELX_P HELX_P20 AC2 THR C 102 ? LEU C 108 ? THR C 99  LEU C 105 1 ? 7  
HELX_P HELX_P21 AC3 LEU C 108 ? PHE C 124 ? LEU C 105 PHE C 121 1 ? 17 
HELX_P HELX_P22 AC4 GLU C 130 ? ILE C 142 ? GLU C 127 ILE C 139 1 ? 13 
HELX_P HELX_P23 AC5 ASP D 6   ? ASN D 35  ? ASP D 3   ASN D 32  1 ? 30 
HELX_P HELX_P24 AC6 THR D 40  ? GLN D 53  ? THR D 37  GLN D 50  1 ? 14 
HELX_P HELX_P25 AC7 SER D 57  ? SER D 65  ? SER D 54  SER D 62  1 ? 9  
HELX_P HELX_P26 AC8 ASP D 68  ? LYS D 82  ? ASP D 65  LYS D 79  1 ? 15 
HELX_P HELX_P27 AC9 THR D 102 ? LEU D 108 ? THR D 99  LEU D 105 1 ? 7  
HELX_P HELX_P28 AD1 LEU D 108 ? PHE D 124 ? LEU D 105 PHE D 121 1 ? 17 
HELX_P HELX_P29 AD2 SER D 128 ? GLU D 130 ? SER D 125 GLU D 127 5 ? 3  
HELX_P HELX_P30 AD3 GLU D 131 ? ILE D 142 ? GLU D 128 ILE D 139 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? 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 ILE A 102 ? VAL A 106 ? ILE A 82 VAL A 86 
AA1 2 PHE A 114 ? LEU A 118 ? PHE A 94 LEU A 98 
AA2 1 ILE B 85  ? VAL B 89  ? ILE B 82 VAL B 86 
AA2 2 PHE B 97  ? LEU B 101 ? PHE B 94 LEU B 98 
AA3 1 ILE C 85  ? VAL C 89  ? ILE C 82 VAL C 86 
AA3 2 PHE C 97  ? LEU C 101 ? PHE C 94 LEU C 98 
AA4 1 ILE D 85  ? VAL D 89  ? ILE D 82 VAL D 86 
AA4 2 PHE D 97  ? LEU D 101 ? PHE D 94 LEU D 98 
# 
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 LYS A 105 ? N LYS A 85 O GLN A 115 ? O GLN A 95 
AA2 1 2 N VAL B 86  ? N VAL B 83 O PHE B 100 ? O PHE B 97 
AA3 1 2 N VAL C 86  ? N VAL C 83 O PHE C 100 ? O PHE C 97 
AA4 1 2 N LYS D 88  ? N LYS D 85 O GLN D 98  ? O GLN D 95 
# 
_pdbx_entry_details.entry_id                   8XTA 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B HOH 203 ? ? O   B HOH 226 ? ? 2.00 
2 1 OD2 A ASP 65  ? ? ND2 A ASN 68  ? ? 2.15 
3 1 O   A ASP 65  ? ? OG1 A THR 69  ? ? 2.18 
4 1 O   A HOH 234 ? ? O   B HOH 252 ? ? 2.18 
5 1 OG  A SER -1  ? ? O   A HOH 201 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 24  ? ? CG A ASP 24  ? ? OD1 A ASP 24  ? ? 112.37 118.30 -5.93 0.90 N 
2 1 CB A LEU 25  ? ? CG A LEU 25  ? ? CD2 A LEU 25  ? ? 123.76 111.00 12.76 1.70 N 
3 1 NE A ARG 138 ? ? CZ A ARG 138 ? ? NH1 A ARG 138 ? ? 124.22 120.30 3.92  0.50 N 
4 1 NE A ARG 138 ? ? CZ A ARG 138 ? ? NH2 A ARG 138 ? ? 116.87 120.30 -3.43 0.50 N 
5 1 NE B ARG 138 ? ? CZ B ARG 138 ? ? NH1 B ARG 138 ? ? 123.55 120.30 3.25  0.50 N 
6 1 NE D ARG 138 ? ? CZ D ARG 138 ? ? NH2 D ARG 138 ? ? 117.27 120.30 -3.03 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 HIS A 0  ? ? -113.37 72.30   
2  1 MET A 28 ? ? -20.32  -54.50  
3  1 GLN A 31 ? ? -48.13  -18.75  
4  1 HIS A 40 ? ? -28.99  -69.13  
5  1 GLN A 50 ? ? -155.55 80.10   
6  1 GLN A 55 ? ? -54.24  -3.75   
7  1 CYS A 63 ? ? 72.92   -58.94  
8  1 ASP A 90 ? ? 172.79  168.76  
9  1 ARG A 91 ? ? -69.58  -176.92 
10 1 LYS A 93 ? ? -176.19 116.04  
11 1 THR A 99 ? ? -64.15  -178.11 
12 1 CYS B 63 ? ? 60.53   -21.32  
13 1 ASP B 90 ? ? 178.78  -175.64 
14 1 ARG B 92 ? ? 80.52   -20.98  
15 1 ILE C 53 ? ? -31.89  142.17  
16 1 CYS C 63 ? ? 63.74   -12.80  
17 1 ASP C 90 ? ? -177.35 136.41  
18 1 ARG C 92 ? ? 82.47   -46.46  
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       253 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.88 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A LEU -6  ? A LEU 14  
15 1 Y 1 A VAL -5  ? A VAL 15  
16 1 Y 1 A LYS 141 ? A LYS 161 
17 1 Y 1 B GLY -2  ? B GLY 1   
18 1 Y 1 B SER -1  ? B SER 2   
19 1 Y 1 B HIS 0   ? B HIS 3   
20 1 Y 1 B MET 1   ? B MET 4   
21 1 Y 1 B LYS 141 ? B LYS 144 
22 1 Y 1 C GLY -2  ? C GLY 1   
23 1 Y 1 C SER -1  ? C SER 2   
24 1 Y 1 C HIS 0   ? C HIS 3   
25 1 Y 1 C MET 1   ? C MET 4   
26 1 Y 1 C LYS 141 ? C LYS 144 
27 1 Y 1 D GLY -2  ? D GLY 1   
28 1 Y 1 D SER -1  ? D SER 2   
29 1 Y 1 D HIS 0   ? D HIS 3   
30 1 Y 1 D MET 1   ? D MET 4   
31 1 Y 1 D LYS 141 ? D LYS 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'National Research Foundation (NRF, Korea)' 
_pdbx_audit_support.country                'Korea, Republic Of' 
_pdbx_audit_support.grant_number           RS-2023-00243435 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8XT8 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XTA 
_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]   0.005666 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014409 
_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]   0.010526 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . PRO A 1 16  ? 43.058 -2.617  83.451  1.00 86.11  ? -4  PRO A N   1 
ATOM   2    C CA  . PRO A 1 16  ? 42.093 -1.730  82.788  1.00 85.84  ? -4  PRO A CA  1 
ATOM   3    C C   . PRO A 1 16  ? 42.591 -0.244  82.575  1.00 81.20  ? -4  PRO A C   1 
ATOM   4    O O   . PRO A 1 16  ? 43.142 0.313   83.508  1.00 94.31  ? -4  PRO A O   1 
ATOM   5    C CB  . PRO A 1 16  ? 40.885 -1.838  83.728  1.00 86.73  ? -4  PRO A CB  1 
ATOM   6    C CG  . PRO A 1 16  ? 41.016 -3.191  84.411  1.00 74.44  ? -4  PRO A CG  1 
ATOM   7    C CD  . PRO A 1 16  ? 42.379 -3.753  84.106  1.00 74.65  ? -4  PRO A CD  1 
ATOM   8    N N   . ARG A 1 17  ? 42.409 0.384   81.387  1.00 73.01  ? -3  ARG A N   1 
ATOM   9    C CA  . ARG A 1 17  ? 43.180 1.619   81.023  1.00 61.10  ? -3  ARG A CA  1 
ATOM   10   C C   . ARG A 1 17  ? 42.448 2.796   80.261  1.00 58.63  ? -3  ARG A C   1 
ATOM   11   O O   . ARG A 1 17  ? 41.237 2.765   79.996  1.00 55.91  ? -3  ARG A O   1 
ATOM   12   C CB  . ARG A 1 17  ? 44.468 1.227   80.274  1.00 66.04  ? -3  ARG A CB  1 
ATOM   13   C CG  . ARG A 1 17  ? 45.718 1.845   80.892  1.00 78.82  ? -3  ARG A CG  1 
ATOM   14   C CD  . ARG A 1 17  ? 47.003 1.453   80.187  1.00 85.08  ? -3  ARG A CD  1 
ATOM   15   N NE  . ARG A 1 17  ? 47.972 0.894   81.144  1.00 98.36  ? -3  ARG A NE  1 
ATOM   16   C CZ  . ARG A 1 17  ? 47.814 -0.260  81.825  1.00 101.10 ? -3  ARG A CZ  1 
ATOM   17   N NH1 . ARG A 1 17  ? 46.709 -0.987  81.701  1.00 103.61 ? -3  ARG A NH1 1 
ATOM   18   N NH2 . ARG A 1 17  ? 48.760 -0.703  82.661  1.00 92.84  ? -3  ARG A NH2 1 
ATOM   19   N N   . GLY A 1 18  ? 43.224 3.846   79.964  1.00 43.73  ? -2  GLY A N   1 
ATOM   20   C CA  . GLY A 1 18  ? 42.746 5.068   79.416  1.00 48.31  ? -2  GLY A CA  1 
ATOM   21   C C   . GLY A 1 18  ? 43.904 6.042   79.336  1.00 52.25  ? -2  GLY A C   1 
ATOM   22   O O   . GLY A 1 18  ? 44.960 5.836   79.946  1.00 52.40  ? -2  GLY A O   1 
ATOM   23   N N   . SER A 1 19  ? 43.704 7.127   78.599  1.00 50.85  ? -1  SER A N   1 
ATOM   24   C CA  . SER A 1 19  ? 44.798 8.050   78.345  1.00 51.20  ? -1  SER A CA  1 
ATOM   25   C C   . SER A 1 19  ? 44.971 8.974   79.538  1.00 51.52  ? -1  SER A C   1 
ATOM   26   O O   . SER A 1 19  ? 46.040 9.498   79.736  1.00 59.70  ? -1  SER A O   1 
ATOM   27   C CB  . SER A 1 19  ? 44.575 8.802   76.989  1.00 57.84  ? -1  SER A CB  1 
ATOM   28   O OG  . SER A 1 19  ? 43.766 8.020   76.041  1.00 51.22  ? -1  SER A OG  1 
ATOM   29   N N   . HIS A 1 20  ? 43.966 9.107   80.403  1.00 58.10  ? 0   HIS A N   1 
ATOM   30   C CA  . HIS A 1 20  ? 44.043 10.017  81.592  1.00 65.18  ? 0   HIS A CA  1 
ATOM   31   C C   . HIS A 1 20  ? 44.038 9.237   82.954  1.00 57.39  ? 0   HIS A C   1 
ATOM   32   O O   . HIS A 1 20  ? 43.047 9.227   83.664  1.00 52.90  ? 0   HIS A O   1 
ATOM   33   C CB  . HIS A 1 20  ? 42.838 10.987  81.513  1.00 71.60  ? 0   HIS A CB  1 
ATOM   34   C CG  . HIS A 1 20  ? 43.137 12.383  81.937  1.00 83.73  ? 0   HIS A CG  1 
ATOM   35   N ND1 . HIS A 1 20  ? 43.807 12.681  83.109  1.00 101.59 ? 0   HIS A ND1 1 
ATOM   36   C CD2 . HIS A 1 20  ? 42.821 13.568  81.366  1.00 93.47  ? 0   HIS A CD2 1 
ATOM   37   C CE1 . HIS A 1 20  ? 43.914 13.994  83.226  1.00 108.22 ? 0   HIS A CE1 1 
ATOM   38   N NE2 . HIS A 1 20  ? 43.322 14.555  82.182  1.00 108.05 ? 0   HIS A NE2 1 
ATOM   39   N N   . MET A 1 21  ? 45.099 8.551   83.332  1.00 56.46  ? 1   MET A N   1 
ATOM   40   C CA  . MET A 1 21  ? 44.981 7.742   84.570  1.00 56.33  ? 1   MET A CA  1 
ATOM   41   C C   . MET A 1 21  ? 45.152 8.618   85.811  1.00 53.87  ? 1   MET A C   1 
ATOM   42   O O   . MET A 1 21  ? 45.833 9.606   85.754  1.00 45.47  ? 1   MET A O   1 
ATOM   43   C CB  . MET A 1 21  ? 46.006 6.603   84.626  1.00 55.62  ? 1   MET A CB  1 
ATOM   44   C CG  . MET A 1 21  ? 45.860 5.552   83.535  1.00 54.25  ? 1   MET A CG  1 
ATOM   45   S SD  . MET A 1 21  ? 44.264 4.745   83.444  1.00 60.36  ? 1   MET A SD  1 
ATOM   46   C CE  . MET A 1 21  ? 44.592 3.419   84.605  1.00 50.31  ? 1   MET A CE  1 
ATOM   47   N N   . LYS A 1 22  ? 44.521 8.240   86.925  1.00 51.64  ? 2   LYS A N   1 
ATOM   48   C CA  . LYS A 1 22  ? 44.690 8.935   88.197  1.00 39.80  ? 2   LYS A CA  1 
ATOM   49   C C   . LYS A 1 22  ? 45.742 8.215   89.016  1.00 37.54  ? 2   LYS A C   1 
ATOM   50   O O   . LYS A 1 22  ? 46.023 7.051   88.818  1.00 44.60  ? 2   LYS A O   1 
ATOM   51   C CB  . LYS A 1 22  ? 43.404 8.912   88.977  1.00 39.92  ? 2   LYS A CB  1 
ATOM   52   C CG  . LYS A 1 22  ? 42.629 10.194  88.986  1.00 47.87  ? 2   LYS A CG  1 
ATOM   53   C CD  . LYS A 1 22  ? 41.326 10.115  88.219  1.00 49.04  ? 2   LYS A CD  1 
ATOM   54   C CE  . LYS A 1 22  ? 40.292 9.257   88.885  1.00 41.17  ? 2   LYS A CE  1 
ATOM   55   N NZ  . LYS A 1 22  ? 39.269 9.008   87.846  1.00 40.28  ? 2   LYS A NZ  1 
ATOM   56   N N   . ASP A 1 23  ? 46.297 8.886   89.986  1.00 35.23  ? 3   ASP A N   1 
ATOM   57   C CA  . ASP A 1 23  ? 47.390 8.317   90.730  1.00 36.39  ? 3   ASP A CA  1 
ATOM   58   C C   . ASP A 1 23  ? 46.789 7.371   91.797  1.00 40.65  ? 3   ASP A C   1 
ATOM   59   O O   . ASP A 1 23  ? 45.894 7.751   92.552  1.00 35.99  ? 3   ASP A O   1 
ATOM   60   C CB  . ASP A 1 23  ? 48.193 9.429   91.383  1.00 38.18  ? 3   ASP A CB  1 
ATOM   61   C CG  . ASP A 1 23  ? 49.236 8.912   92.294  1.00 46.33  ? 3   ASP A CG  1 
ATOM   62   O OD1 . ASP A 1 23  ? 49.444 7.679   92.377  1.00 70.29  ? 3   ASP A OD1 1 
ATOM   63   O OD2 . ASP A 1 23  ? 49.842 9.725   92.976  1.00 54.69  ? 3   ASP A OD2 1 
ATOM   64   N N   . PHE A 1 24  ? 47.307 6.158   91.861  1.00 38.15  ? 4   PHE A N   1 
ATOM   65   C CA  . PHE A 1 24  ? 46.702 5.176   92.703  1.00 40.64  ? 4   PHE A CA  1 
ATOM   66   C C   . PHE A 1 24  ? 46.765 5.629   94.159  1.00 38.24  ? 4   PHE A C   1 
ATOM   67   O O   . PHE A 1 24  ? 45.830 5.487   94.869  1.00 38.66  ? 4   PHE A O   1 
ATOM   68   C CB  . PHE A 1 24  ? 47.301 3.772   92.501  1.00 36.59  ? 4   PHE A CB  1 
ATOM   69   C CG  . PHE A 1 24  ? 46.910 2.797   93.572  1.00 35.86  ? 4   PHE A CG  1 
ATOM   70   C CD1 . PHE A 1 24  ? 45.623 2.286   93.611  1.00 41.39  ? 4   PHE A CD1 1 
ATOM   71   C CD2 . PHE A 1 24  ? 47.783 2.441   94.565  1.00 35.12  ? 4   PHE A CD2 1 
ATOM   72   C CE1 . PHE A 1 24  ? 45.211 1.448   94.625  1.00 35.56  ? 4   PHE A CE1 1 
ATOM   73   C CE2 . PHE A 1 24  ? 47.398 1.567   95.551  1.00 36.31  ? 4   PHE A CE2 1 
ATOM   74   C CZ  . PHE A 1 24  ? 46.103 1.072   95.577  1.00 33.42  ? 4   PHE A CZ  1 
ATOM   75   N N   . GLU A 1 25  ? 47.836 6.256   94.555  1.00 42.36  ? 5   GLU A N   1 
ATOM   76   C CA  . GLU A 1 25  ? 48.011 6.641   95.932  1.00 42.12  ? 5   GLU A CA  1 
ATOM   77   C C   . GLU A 1 25  ? 46.941 7.643   96.318  1.00 42.05  ? 5   GLU A C   1 
ATOM   78   O O   . GLU A 1 25  ? 46.454 7.608   97.408  1.00 41.50  ? 5   GLU A O   1 
ATOM   79   C CB  . GLU A 1 25  ? 49.406 7.228   96.093  1.00 47.87  ? 5   GLU A CB  1 
ATOM   80   C CG  . GLU A 1 25  ? 49.883 7.407   97.522  1.00 63.32  ? 5   GLU A CG  1 
ATOM   81   C CD  . GLU A 1 25  ? 49.819 6.125   98.371  1.00 79.78  ? 5   GLU A CD  1 
ATOM   82   O OE1 . GLU A 1 25  ? 50.132 5.020   97.791  1.00 79.09  ? 5   GLU A OE1 1 
ATOM   83   O OE2 . GLU A 1 25  ? 49.450 6.246   99.600  1.00 68.19  ? 5   GLU A OE2 1 
ATOM   84   N N   . LYS A 1 26  ? 46.551 8.511   95.395  1.00 39.73  ? 6   LYS A N   1 
ATOM   85   C CA  . LYS A 1 26  ? 45.551 9.496   95.660  1.00 41.80  ? 6   LYS A CA  1 
ATOM   86   C C   . LYS A 1 26  ? 44.173 8.782   95.823  1.00 40.45  ? 6   LYS A C   1 
ATOM   87   O O   . LYS A 1 26  ? 43.396 9.179   96.672  1.00 38.37  ? 6   LYS A O   1 
ATOM   88   C CB  . LYS A 1 26  ? 45.490 10.529  94.513  1.00 47.39  ? 6   LYS A CB  1 
ATOM   89   C CG  . LYS A 1 26  ? 46.073 11.906  94.753  1.00 59.87  ? 6   LYS A CG  1 
ATOM   90   C CD  . LYS A 1 26  ? 47.612 11.966  94.848  1.00 77.72  ? 6   LYS A CD  1 
ATOM   91   C CE  . LYS A 1 26  ? 48.138 12.894  95.978  1.00 90.06  ? 6   LYS A CE  1 
ATOM   92   N NZ  . LYS A 1 26  ? 49.605 12.720  96.259  1.00 94.47  ? 6   LYS A NZ  1 
ATOM   93   N N   . LEU A 1 27  ? 43.858 7.793   94.982  1.00 34.21  ? 7   LEU A N   1 
ATOM   94   C CA  . LEU A 1 27  ? 42.610 7.101   95.066  1.00 35.10  ? 7   LEU A CA  1 
ATOM   95   C C   . LEU A 1 27  ? 42.550 6.301   96.396  1.00 36.22  ? 7   LEU A C   1 
ATOM   96   O O   . LEU A 1 27  ? 41.513 6.222   97.028  1.00 37.41  ? 7   LEU A O   1 
ATOM   97   C CB  . LEU A 1 27  ? 42.432 6.155   93.916  1.00 32.98  ? 7   LEU A CB  1 
ATOM   98   C CG  . LEU A 1 27  ? 42.382 6.752   92.534  1.00 33.02  ? 7   LEU A CG  1 
ATOM   99   C CD1 . LEU A 1 27  ? 42.216 5.736   91.432  1.00 33.10  ? 7   LEU A CD1 1 
ATOM   100  C CD2 . LEU A 1 27  ? 41.271 7.732   92.357  1.00 33.10  ? 7   LEU A CD2 1 
ATOM   101  N N   . TYR A 1 28  ? 43.660 5.774   96.850  1.00 31.33  ? 8   TYR A N   1 
ATOM   102  C CA  . TYR A 1 28  ? 43.679 4.990   98.052  1.00 34.71  ? 8   TYR A CA  1 
ATOM   103  C C   . TYR A 1 28  ? 43.421 5.912   99.248  1.00 35.52  ? 8   TYR A C   1 
ATOM   104  O O   . TYR A 1 28  ? 42.715 5.566   100.153 1.00 37.14  ? 8   TYR A O   1 
ATOM   105  C CB  . TYR A 1 28  ? 45.042 4.271   98.223  1.00 36.20  ? 8   TYR A CB  1 
ATOM   106  C CG  . TYR A 1 28  ? 45.125 3.405   99.468  1.00 38.56  ? 8   TYR A CG  1 
ATOM   107  C CD1 . TYR A 1 28  ? 44.447 2.167   99.556  1.00 39.44  ? 8   TYR A CD1 1 
ATOM   108  C CD2 . TYR A 1 28  ? 45.827 3.848   100.579 1.00 37.28  ? 8   TYR A CD2 1 
ATOM   109  C CE1 . TYR A 1 28  ? 44.486 1.410   100.724 1.00 40.85  ? 8   TYR A CE1 1 
ATOM   110  C CE2 . TYR A 1 28  ? 45.891 3.101   101.743 1.00 37.88  ? 8   TYR A CE2 1 
ATOM   111  C CZ  . TYR A 1 28  ? 45.236 1.871   101.827 1.00 43.43  ? 8   TYR A CZ  1 
ATOM   112  O OH  . TYR A 1 28  ? 45.328 1.151   103.046 1.00 44.77  ? 8   TYR A OH  1 
ATOM   113  N N   . GLU A 1 29  ? 44.063 7.051   99.269  1.00 38.96  ? 9   GLU A N   1 
ATOM   114  C CA  . GLU A 1 29  ? 43.827 8.066   100.290 1.00 42.90  ? 9   GLU A CA  1 
ATOM   115  C C   . GLU A 1 29  ? 42.396 8.565   100.286 1.00 38.70  ? 9   GLU A C   1 
ATOM   116  O O   . GLU A 1 29  ? 41.816 8.772   101.316 1.00 44.39  ? 9   GLU A O   1 
ATOM   117  C CB  . GLU A 1 29  ? 44.826 9.221   100.201 1.00 46.41  ? 9   GLU A CB  1 
ATOM   118  C CG  . GLU A 1 29  ? 46.049 8.998   101.105 1.00 63.40  ? 9   GLU A CG  1 
ATOM   119  C CD  . GLU A 1 29  ? 47.400 9.448   100.487 1.00 83.64  ? 9   GLU A CD  1 
ATOM   120  O OE1 . GLU A 1 29  ? 47.586 10.652  100.150 1.00 79.83  ? 9   GLU A OE1 1 
ATOM   121  O OE2 . GLU A 1 29  ? 48.302 8.578   100.349 1.00 92.50  ? 9   GLU A OE2 1 
ATOM   122  N N   . ALA A 1 30  ? 41.800 8.741   99.141  1.00 34.02  ? 10  ALA A N   1 
ATOM   123  C CA  . ALA A 1 30  ? 40.443 9.174   99.173  1.00 35.77  ? 10  ALA A CA  1 
ATOM   124  C C   . ALA A 1 30  ? 39.586 8.036   99.714  1.00 37.17  ? 10  ALA A C   1 
ATOM   125  O O   . ALA A 1 30  ? 38.619 8.312   100.345 1.00 38.15  ? 10  ALA A O   1 
ATOM   126  C CB  . ALA A 1 30  ? 39.962 9.593   97.787  1.00 35.98  ? 10  ALA A CB  1 
ATOM   127  N N   . THR A 1 31  ? 39.922 6.785   99.402  1.00 34.01  ? 11  THR A N   1 
ATOM   128  C CA  . THR A 1 31  ? 39.112 5.685   99.773  1.00 35.26  ? 11  THR A CA  1 
ATOM   129  C C   . THR A 1 31  ? 39.160 5.521   101.293 1.00 34.18  ? 11  THR A C   1 
ATOM   130  O O   . THR A 1 31  ? 38.181 5.354   101.918 1.00 32.88  ? 11  THR A O   1 
ATOM   131  C CB  . THR A 1 31  ? 39.500 4.419   99.020  1.00 37.29  ? 11  THR A CB  1 
ATOM   132  O OG1 . THR A 1 31  ? 39.179 4.596   97.615  1.00 38.48  ? 11  THR A OG1 1 
ATOM   133  C CG2 . THR A 1 31  ? 38.678 3.288   99.496  1.00 38.21  ? 11  THR A CG2 1 
ATOM   134  N N   . THR A 1 32  ? 40.301 5.714   101.876 1.00 34.28  ? 12  THR A N   1 
ATOM   135  C CA  . THR A 1 32  ? 40.498 5.653   103.293 1.00 33.40  ? 12  THR A CA  1 
ATOM   136  C C   . THR A 1 32  ? 39.806 6.734   104.017 1.00 34.03  ? 12  THR A C   1 
ATOM   137  O O   . THR A 1 32  ? 39.533 6.629   105.175 1.00 36.70  ? 12  THR A O   1 
ATOM   138  C CB  . THR A 1 32  ? 42.020 5.858   103.543 1.00 34.69  ? 12  THR A CB  1 
ATOM   139  O OG1 . THR A 1 32  ? 42.653 4.655   103.165 1.00 40.00  ? 12  THR A OG1 1 
ATOM   140  C CG2 . THR A 1 32  ? 42.358 6.066   104.992 1.00 40.06  ? 12  THR A CG2 1 
ATOM   141  N N   . LYS A 1 33  ? 39.743 7.884   103.387 1.00 38.58  ? 13  LYS A N   1 
ATOM   142  C CA  . LYS A 1 33  ? 39.250 9.048   104.025 1.00 36.12  ? 13  LYS A CA  1 
ATOM   143  C C   . LYS A 1 33  ? 37.724 8.779   104.027 1.00 34.59  ? 13  LYS A C   1 
ATOM   144  O O   . LYS A 1 33  ? 37.043 9.162   104.912 1.00 31.13  ? 13  LYS A O   1 
ATOM   145  C CB  . LYS A 1 33  ? 39.607 10.264  103.211 1.00 40.02  ? 13  LYS A CB  1 
ATOM   146  C CG  . LYS A 1 33  ? 40.196 11.425  103.970 1.00 50.26  ? 13  LYS A CG  1 
ATOM   147  C CD  . LYS A 1 33  ? 39.397 11.826  105.221 1.00 53.70  ? 13  LYS A CD  1 
ATOM   148  C CE  . LYS A 1 33  ? 39.587 13.314  105.557 1.00 56.64  ? 13  LYS A CE  1 
ATOM   149  N NZ  . LYS A 1 33  ? 40.163 13.468  106.910 1.00 63.76  ? 13  LYS A NZ  1 
ATOM   150  N N   . LEU A 1 34  ? 37.232 8.122   103.007 1.00 32.28  ? 14  LEU A N   1 
ATOM   151  C CA  . LEU A 1 34  ? 35.846 7.862   102.904 1.00 38.81  ? 14  LEU A CA  1 
ATOM   152  C C   . LEU A 1 34  ? 35.498 6.919   104.055 1.00 41.54  ? 14  LEU A C   1 
ATOM   153  O O   . LEU A 1 34  ? 34.589 7.177   104.745 1.00 38.25  ? 14  LEU A O   1 
ATOM   154  C CB  . LEU A 1 34  ? 35.513 7.226   101.555 1.00 36.06  ? 14  LEU A CB  1 
ATOM   155  C CG  . LEU A 1 34  ? 34.098 6.681   101.349 1.00 42.87  ? 14  LEU A CG  1 
ATOM   156  C CD1 . LEU A 1 34  ? 33.072 7.766   101.527 1.00 46.94  ? 14  LEU A CD1 1 
ATOM   157  C CD2 . LEU A 1 34  ? 33.900 6.083   99.984  1.00 40.83  ? 14  LEU A CD2 1 
ATOM   158  N N   . VAL A 1 35  ? 36.276 5.878   104.290 1.00 38.65  ? 15  VAL A N   1 
ATOM   159  C CA  . VAL A 1 35  ? 35.909 4.856   105.212 1.00 36.82  ? 15  VAL A CA  1 
ATOM   160  C C   . VAL A 1 35  ? 36.080 5.388   106.617 1.00 39.68  ? 15  VAL A C   1 
ATOM   161  O O   . VAL A 1 35  ? 35.203 5.298   107.428 1.00 42.66  ? 15  VAL A O   1 
ATOM   162  C CB  . VAL A 1 35  ? 36.806 3.625   104.998 1.00 42.28  ? 15  VAL A CB  1 
ATOM   163  C CG1 . VAL A 1 35  ? 36.786 2.607   106.187 1.00 36.34  ? 15  VAL A CG1 1 
ATOM   164  C CG2 . VAL A 1 35  ? 36.404 2.983   103.672 1.00 42.57  ? 15  VAL A CG2 1 
ATOM   165  N N   . SER A 1 36  ? 37.203 5.991   106.908 1.00 41.74  ? 16  SER A N   1 
ATOM   166  C CA  . SER A 1 36  ? 37.364 6.507   108.207 1.00 38.08  ? 16  SER A CA  1 
ATOM   167  C C   . SER A 1 36  ? 36.245 7.474   108.509 1.00 38.55  ? 16  SER A C   1 
ATOM   168  O O   . SER A 1 36  ? 35.800 7.504   109.623 1.00 39.28  ? 16  SER A O   1 
ATOM   169  C CB  . SER A 1 36  ? 38.771 7.079   108.486 1.00 41.89  ? 16  SER A CB  1 
ATOM   170  O OG  . SER A 1 36  ? 39.006 8.286   107.849 1.00 55.50  ? 16  SER A OG  1 
ATOM   171  N N   . THR A 1 37  ? 35.748 8.229   107.540 1.00 38.28  ? 17  THR A N   1 
ATOM   172  C CA  . THR A 1 37  ? 34.737 9.199   107.834 1.00 33.99  ? 17  THR A CA  1 
ATOM   173  C C   . THR A 1 37  ? 33.374 8.537   108.066 1.00 37.03  ? 17  THR A C   1 
ATOM   174  O O   . THR A 1 37  ? 32.611 8.991   108.874 1.00 35.87  ? 17  THR A O   1 
ATOM   175  C CB  . THR A 1 37  ? 34.611 10.243  106.742 1.00 34.32  ? 17  THR A CB  1 
ATOM   176  O OG1 . THR A 1 37  ? 35.835 10.985  106.658 1.00 35.12  ? 17  THR A OG1 1 
ATOM   177  C CG2 . THR A 1 37  ? 33.464 11.190  107.107 1.00 37.14  ? 17  THR A CG2 1 
ATOM   178  N N   . SER A 1 38  ? 33.066 7.474   107.348 1.00 37.67  ? 18  SER A N   1 
ATOM   179  C CA  . SER A 1 38  ? 31.858 6.664   107.608 1.00 39.53  ? 18  SER A CA  1 
ATOM   180  C C   . SER A 1 38  ? 31.877 6.157   109.049 1.00 43.17  ? 18  SER A C   1 
ATOM   181  O O   . SER A 1 38  ? 30.894 6.201   109.748 1.00 48.91  ? 18  SER A O   1 
ATOM   182  C CB  . SER A 1 38  ? 31.856 5.449   106.727 1.00 38.92  ? 18  SER A CB  1 
ATOM   183  O OG  . SER A 1 38  ? 30.597 4.852   106.632 1.00 43.79  ? 18  SER A OG  1 
ATOM   184  N N   . LEU A 1 39  ? 33.026 5.723   109.505 1.00 42.86  ? 19  LEU A N   1 
ATOM   185  C CA  . LEU A 1 39  ? 33.104 5.111   110.798 1.00 50.90  ? 19  LEU A CA  1 
ATOM   186  C C   . LEU A 1 39  ? 32.915 6.178   111.860 1.00 54.94  ? 19  LEU A C   1 
ATOM   187  O O   . LEU A 1 39  ? 32.135 6.002   112.762 1.00 61.48  ? 19  LEU A O   1 
ATOM   188  C CB  . LEU A 1 39  ? 34.472 4.482   111.035 1.00 53.33  ? 19  LEU A CB  1 
ATOM   189  C CG  . LEU A 1 39  ? 34.852 3.176   110.376 1.00 62.01  ? 19  LEU A CG  1 
ATOM   190  C CD1 . LEU A 1 39  ? 36.134 2.707   111.058 1.00 71.07  ? 19  LEU A CD1 1 
ATOM   191  C CD2 . LEU A 1 39  ? 33.760 2.126   110.485 1.00 63.61  ? 19  LEU A CD2 1 
ATOM   192  N N   . LYS A 1 40  ? 33.677 7.257   111.769 1.00 48.44  ? 20  LYS A N   1 
ATOM   193  C CA  . LYS A 1 40  ? 33.550 8.334   112.706 1.00 51.81  ? 20  LYS A CA  1 
ATOM   194  C C   . LYS A 1 40  ? 32.063 8.831   112.734 1.00 55.43  ? 20  LYS A C   1 
ATOM   195  O O   . LYS A 1 40  ? 31.531 9.112   113.817 1.00 47.45  ? 20  LYS A O   1 
ATOM   196  C CB  . LYS A 1 40  ? 34.565 9.400   112.371 1.00 52.98  ? 20  LYS A CB  1 
ATOM   197  C CG  . LYS A 1 40  ? 34.389 10.753  112.989 1.00 67.79  ? 20  LYS A CG  1 
ATOM   198  C CD  . LYS A 1 40  ? 35.419 11.695  112.351 1.00 86.75  ? 20  LYS A CD  1 
ATOM   199  C CE  . LYS A 1 40  ? 34.881 13.109  112.155 1.00 104.81 ? 20  LYS A CE  1 
ATOM   200  N NZ  . LYS A 1 40  ? 34.461 13.734  113.454 1.00 123.97 ? 20  LYS A NZ  1 
ATOM   201  N N   . VAL A 1 41  ? 31.381 8.846   111.584 1.00 41.62  ? 21  VAL A N   1 
ATOM   202  C CA  . VAL A 1 41  ? 30.042 9.331   111.578 1.00 43.69  ? 21  VAL A CA  1 
ATOM   203  C C   . VAL A 1 41  ? 29.092 8.355   112.266 1.00 50.27  ? 21  VAL A C   1 
ATOM   204  O O   . VAL A 1 41  ? 28.267 8.793   113.020 1.00 59.87  ? 21  VAL A O   1 
ATOM   205  C CB  . VAL A 1 41  ? 29.572 9.713   110.180 1.00 44.09  ? 21  VAL A CB  1 
ATOM   206  C CG1 . VAL A 1 41  ? 28.052 9.701   110.059 1.00 43.30  ? 21  VAL A CG1 1 
ATOM   207  C CG2 . VAL A 1 41  ? 30.104 11.086  109.822 1.00 44.49  ? 21  VAL A CG2 1 
ATOM   208  N N   . LYS A 1 42  ? 29.240 7.051   112.060 1.00 57.34  ? 22  LYS A N   1 
ATOM   209  C CA  . LYS A 1 42  ? 28.417 6.044   112.774 1.00 52.70  ? 22  LYS A CA  1 
ATOM   210  C C   . LYS A 1 42  ? 28.614 5.973   114.300 1.00 48.17  ? 22  LYS A C   1 
ATOM   211  O O   . LYS A 1 42  ? 27.688 5.843   115.031 1.00 56.78  ? 22  LYS A O   1 
ATOM   212  C CB  . LYS A 1 42  ? 28.696 4.675   112.217 1.00 54.80  ? 22  LYS A CB  1 
ATOM   213  C CG  . LYS A 1 42  ? 27.882 4.337   110.987 1.00 58.65  ? 22  LYS A CG  1 
ATOM   214  C CD  . LYS A 1 42  ? 28.154 2.874   110.679 1.00 64.97  ? 22  LYS A CD  1 
ATOM   215  C CE  . LYS A 1 42  ? 28.899 2.668   109.373 1.00 75.99  ? 22  LYS A CE  1 
ATOM   216  N NZ  . LYS A 1 42  ? 30.048 1.724   109.546 1.00 82.75  ? 22  LYS A NZ  1 
ATOM   217  N N   . ASP A 1 43  ? 29.842 6.007   114.727 1.00 47.36  ? 23  ASP A N   1 
ATOM   218  C CA  . ASP A 1 43  ? 30.245 6.192   116.092 1.00 61.21  ? 23  ASP A CA  1 
ATOM   219  C C   . ASP A 1 43  ? 29.615 7.467   116.655 1.00 58.32  ? 23  ASP A C   1 
ATOM   220  O O   . ASP A 1 43  ? 28.847 7.345   117.558 1.00 62.13  ? 23  ASP A O   1 
ATOM   221  C CB  . ASP A 1 43  ? 31.827 6.163   116.181 1.00 66.11  ? 23  ASP A CB  1 
ATOM   222  C CG  . ASP A 1 43  ? 32.426 6.865   117.447 1.00 75.31  ? 23  ASP A CG  1 
ATOM   223  O OD1 . ASP A 1 43  ? 32.664 8.119   117.426 1.00 73.62  ? 23  ASP A OD1 1 
ATOM   224  O OD2 . ASP A 1 43  ? 32.734 6.140   118.441 1.00 77.20  ? 23  ASP A OD2 1 
ATOM   225  N N   . ASP A 1 44  ? 29.913 8.665   116.130 1.00 57.18  ? 24  ASP A N   1 
ATOM   226  C CA  . ASP A 1 44  ? 29.320 9.888   116.661 1.00 47.95  ? 24  ASP A CA  1 
ATOM   227  C C   . ASP A 1 44  ? 27.813 9.713   116.867 1.00 50.81  ? 24  ASP A C   1 
ATOM   228  O O   . ASP A 1 44  ? 27.258 10.285  117.808 1.00 45.27  ? 24  ASP A O   1 
ATOM   229  C CB  . ASP A 1 44  ? 29.413 11.096  115.726 1.00 48.57  ? 24  ASP A CB  1 
ATOM   230  C CG  . ASP A 1 44  ? 30.799 11.506  115.443 1.00 55.09  ? 24  ASP A CG  1 
ATOM   231  O OD1 . ASP A 1 44  ? 31.625 10.930  116.181 1.00 57.27  ? 24  ASP A OD1 1 
ATOM   232  O OD2 . ASP A 1 44  ? 31.040 12.335  114.464 1.00 51.22  ? 24  ASP A OD2 1 
ATOM   233  N N   . LEU A 1 45  ? 27.136 9.014   115.951 1.00 45.52  ? 25  LEU A N   1 
ATOM   234  C CA  . LEU A 1 45  ? 25.696 8.992   116.031 1.00 45.55  ? 25  LEU A CA  1 
ATOM   235  C C   . LEU A 1 45  ? 25.159 7.777   116.830 1.00 50.72  ? 25  LEU A C   1 
ATOM   236  O O   . LEU A 1 45  ? 24.048 7.773   117.257 1.00 39.48  ? 25  LEU A O   1 
ATOM   237  C CB  . LEU A 1 45  ? 25.075 9.116   114.674 1.00 40.46  ? 25  LEU A CB  1 
ATOM   238  C CG  . LEU A 1 45  ? 25.439 10.311  113.726 1.00 56.80  ? 25  LEU A CG  1 
ATOM   239  C CD1 . LEU A 1 45  ? 24.741 9.994   112.396 1.00 54.89  ? 25  LEU A CD1 1 
ATOM   240  C CD2 . LEU A 1 45  ? 25.201 11.828  114.095 1.00 57.35  ? 25  LEU A CD2 1 
ATOM   241  N N   . LYS A 1 46  ? 25.969 6.769   117.102 1.00 62.28  ? 26  LYS A N   1 
ATOM   242  C CA  . LYS A 1 46  ? 25.412 5.578   117.699 1.00 69.35  ? 26  LYS A CA  1 
ATOM   243  C C   . LYS A 1 46  ? 24.909 5.980   119.047 1.00 65.12  ? 26  LYS A C   1 
ATOM   244  O O   . LYS A 1 46  ? 23.945 5.472   119.469 1.00 52.83  ? 26  LYS A O   1 
ATOM   245  C CB  . LYS A 1 46  ? 26.440 4.456   117.854 1.00 80.09  ? 26  LYS A CB  1 
ATOM   246  C CG  . LYS A 1 46  ? 25.865 3.024   117.882 1.00 84.56  ? 26  LYS A CG  1 
ATOM   247  C CD  . LYS A 1 46  ? 26.744 2.120   118.772 1.00 93.79  ? 26  LYS A CD  1 
ATOM   248  C CE  . LYS A 1 46  ? 27.292 0.884   118.071 1.00 92.65  ? 26  LYS A CE  1 
ATOM   249  N NZ  . LYS A 1 46  ? 28.618 0.534   118.669 1.00 90.53  ? 26  LYS A NZ  1 
ATOM   250  N N   . LYS A 1 47  ? 25.561 6.902   119.730 1.00 78.19  ? 27  LYS A N   1 
ATOM   251  C CA  . LYS A 1 47  ? 25.040 7.372   121.014 1.00 87.54  ? 27  LYS A CA  1 
ATOM   252  C C   . LYS A 1 47  ? 23.645 8.079   120.930 1.00 88.48  ? 27  LYS A C   1 
ATOM   253  O O   . LYS A 1 47  ? 22.683 7.784   121.669 1.00 66.11  ? 27  LYS A O   1 
ATOM   254  C CB  . LYS A 1 47  ? 26.076 8.309   121.588 1.00 96.24  ? 27  LYS A CB  1 
ATOM   255  C CG  . LYS A 1 47  ? 27.326 7.567   122.069 1.00 109.60 ? 27  LYS A CG  1 
ATOM   256  C CD  . LYS A 1 47  ? 28.519 7.614   121.115 1.00 93.55  ? 27  LYS A CD  1 
ATOM   257  C CE  . LYS A 1 47  ? 29.383 6.368   121.276 1.00 89.97  ? 27  LYS A CE  1 
ATOM   258  N NZ  . LYS A 1 47  ? 30.791 6.600   120.876 1.00 90.24  ? 27  LYS A NZ  1 
ATOM   259  N N   . MET A 1 48  ? 23.572 8.993   119.982 1.00 84.85  ? 28  MET A N   1 
ATOM   260  C CA  . MET A 1 48  ? 22.489 9.925   119.850 1.00 88.21  ? 28  MET A CA  1 
ATOM   261  C C   . MET A 1 48  ? 21.177 9.584   120.521 1.00 83.87  ? 28  MET A C   1 
ATOM   262  O O   . MET A 1 48  ? 20.657 10.413  121.257 1.00 81.17  ? 28  MET A O   1 
ATOM   263  C CB  . MET A 1 48  ? 22.245 10.295  118.354 1.00 99.35  ? 28  MET A CB  1 
ATOM   264  C CG  . MET A 1 48  ? 21.324 9.413   117.480 1.00 84.50  ? 28  MET A CG  1 
ATOM   265  S SD  . MET A 1 48  ? 21.197 9.996   115.748 1.00 71.42  ? 28  MET A SD  1 
ATOM   266  C CE  . MET A 1 48  ? 21.991 8.777   114.709 1.00 78.38  ? 28  MET A CE  1 
ATOM   267  N N   . PHE A 1 49  ? 20.590 8.428   120.261 1.00 79.44  ? 29  PHE A N   1 
ATOM   268  C CA  . PHE A 1 49  ? 19.221 8.235   120.774 1.00 88.34  ? 29  PHE A CA  1 
ATOM   269  C C   . PHE A 1 49  ? 19.187 7.673   122.194 1.00 88.23  ? 29  PHE A C   1 
ATOM   270  O O   . PHE A 1 49  ? 18.329 8.044   122.997 1.00 110.87 ? 29  PHE A O   1 
ATOM   271  C CB  . PHE A 1 49  ? 18.340 7.341   119.864 1.00 92.93  ? 29  PHE A CB  1 
ATOM   272  C CG  . PHE A 1 49  ? 18.328 7.746   118.413 1.00 84.07  ? 29  PHE A CG  1 
ATOM   273  C CD1 . PHE A 1 49  ? 19.280 7.228   117.540 1.00 74.73  ? 29  PHE A CD1 1 
ATOM   274  C CD2 . PHE A 1 49  ? 17.368 8.626   117.927 1.00 70.18  ? 29  PHE A CD2 1 
ATOM   275  C CE1 . PHE A 1 49  ? 19.288 7.573   116.226 1.00 63.17  ? 29  PHE A CE1 1 
ATOM   276  C CE2 . PHE A 1 49  ? 17.375 8.974   116.604 1.00 71.03  ? 29  PHE A CE2 1 
ATOM   277  C CZ  . PHE A 1 49  ? 18.332 8.438   115.754 1.00 69.52  ? 29  PHE A CZ  1 
ATOM   278  N N   . LYS A 1 50  ? 20.089 6.758   122.500 1.00 87.04  ? 30  LYS A N   1 
ATOM   279  C CA  . LYS A 1 50  ? 20.012 6.050   123.765 1.00 94.30  ? 30  LYS A CA  1 
ATOM   280  C C   . LYS A 1 50  ? 20.538 7.024   124.831 1.00 75.40  ? 30  LYS A C   1 
ATOM   281  O O   . LYS A 1 50  ? 19.866 7.325   125.819 1.00 58.17  ? 30  LYS A O   1 
ATOM   282  C CB  . LYS A 1 50  ? 20.794 4.727   123.682 1.00 108.03 ? 30  LYS A CB  1 
ATOM   283  C CG  . LYS A 1 50  ? 20.123 3.555   124.392 1.00 122.22 ? 30  LYS A CG  1 
ATOM   284  C CD  . LYS A 1 50  ? 20.807 2.215   124.106 1.00 128.12 ? 30  LYS A CD  1 
ATOM   285  C CE  . LYS A 1 50  ? 22.213 2.151   124.718 1.00 130.08 ? 30  LYS A CE  1 
ATOM   286  N NZ  . LYS A 1 50  ? 22.598 0.821   125.288 1.00 118.99 ? 30  LYS A NZ  1 
ATOM   287  N N   . GLN A 1 51  ? 21.697 7.596   124.562 1.00 66.70  ? 31  GLN A N   1 
ATOM   288  C CA  . GLN A 1 51  ? 22.190 8.714   125.343 1.00 54.64  ? 31  GLN A CA  1 
ATOM   289  C C   . GLN A 1 51  ? 21.218 9.861   125.605 1.00 51.68  ? 31  GLN A C   1 
ATOM   290  O O   . GLN A 1 51  ? 21.433 10.607  126.591 1.00 50.64  ? 31  GLN A O   1 
ATOM   291  C CB  . GLN A 1 51  ? 23.413 9.256   124.670 1.00 62.42  ? 31  GLN A CB  1 
ATOM   292  C CG  . GLN A 1 51  ? 23.968 10.451  125.377 1.00 62.94  ? 31  GLN A CG  1 
ATOM   293  C CD  . GLN A 1 51  ? 25.290 10.868  124.856 1.00 67.53  ? 31  GLN A CD  1 
ATOM   294  O OE1 . GLN A 1 51  ? 25.467 12.027  124.423 1.00 71.86  ? 31  GLN A OE1 1 
ATOM   295  N NE2 . GLN A 1 51  ? 26.243 9.937   124.879 1.00 72.68  ? 31  GLN A NE2 1 
ATOM   296  N N   . ASN A 1 52  ? 20.132 9.973   124.814 1.00 47.93  ? 32  ASN A N   1 
ATOM   297  C CA  . ASN A 1 52  ? 19.112 11.027  124.976 1.00 47.78  ? 32  ASN A CA  1 
ATOM   298  C C   . ASN A 1 52  ? 17.622 10.655  125.317 1.00 61.38  ? 32  ASN A C   1 
ATOM   299  O O   . ASN A 1 52  ? 16.622 11.433  124.990 1.00 49.27  ? 32  ASN A O   1 
ATOM   300  C CB  . ASN A 1 52  ? 19.050 11.835  123.709 1.00 45.06  ? 32  ASN A CB  1 
ATOM   301  C CG  . ASN A 1 52  ? 20.169 12.775  123.580 1.00 42.43  ? 32  ASN A CG  1 
ATOM   302  O OD1 . ASN A 1 52  ? 20.241 13.702  124.296 1.00 45.84  ? 32  ASN A OD1 1 
ATOM   303  N ND2 . ASN A 1 52  ? 21.015 12.563  122.621 1.00 47.88  ? 32  ASN A ND2 1 
ATOM   304  N N   . GLY A 1 53  ? 17.451 9.516   125.978 1.00 63.84  ? 33  GLY A N   1 
ATOM   305  C CA  . GLY A 1 53  ? 16.110 9.137   126.504 1.00 72.06  ? 33  GLY A CA  1 
ATOM   306  C C   . GLY A 1 53  ? 15.291 8.093   125.726 1.00 75.87  ? 33  GLY A C   1 
ATOM   307  O O   . GLY A 1 53  ? 14.114 7.852   126.086 1.00 69.26  ? 33  GLY A O   1 
ATOM   308  N N   . TYR A 1 54  ? 15.902 7.489   124.681 1.00 76.31  ? 34  TYR A N   1 
ATOM   309  C CA  . TYR A 1 54  ? 15.223 6.540   123.754 1.00 75.10  ? 34  TYR A CA  1 
ATOM   310  C C   . TYR A 1 54  ? 16.120 5.361   123.513 1.00 78.78  ? 34  TYR A C   1 
ATOM   311  O O   . TYR A 1 54  ? 17.178 5.481   122.827 1.00 67.16  ? 34  TYR A O   1 
ATOM   312  C CB  . TYR A 1 54  ? 14.799 7.158   122.398 1.00 58.71  ? 34  TYR A CB  1 
ATOM   313  C CG  . TYR A 1 54  ? 13.733 8.153   122.596 1.00 51.95  ? 34  TYR A CG  1 
ATOM   314  C CD1 . TYR A 1 54  ? 12.403 7.768   122.734 1.00 61.19  ? 34  TYR A CD1 1 
ATOM   315  C CD2 . TYR A 1 54  ? 14.037 9.488   122.742 1.00 53.32  ? 34  TYR A CD2 1 
ATOM   316  C CE1 . TYR A 1 54  ? 11.370 8.699   122.984 1.00 57.18  ? 34  TYR A CE1 1 
ATOM   317  C CE2 . TYR A 1 54  ? 13.037 10.426  122.971 1.00 51.25  ? 34  TYR A CE2 1 
ATOM   318  C CZ  . TYR A 1 54  ? 11.694 10.038  123.085 1.00 62.14  ? 34  TYR A CZ  1 
ATOM   319  O OH  . TYR A 1 54  ? 10.688 11.001  123.319 1.00 64.79  ? 34  TYR A OH  1 
ATOM   320  N N   . ASP A 1 55  ? 15.647 4.229   124.064 1.00 77.66  ? 35  ASP A N   1 
ATOM   321  C CA  . ASP A 1 55  ? 16.324 2.958   123.927 1.00 85.70  ? 35  ASP A CA  1 
ATOM   322  C C   . ASP A 1 55  ? 16.123 2.408   122.527 1.00 83.47  ? 35  ASP A C   1 
ATOM   323  O O   . ASP A 1 55  ? 15.163 1.666   122.256 1.00 74.06  ? 35  ASP A O   1 
ATOM   324  C CB  . ASP A 1 55  ? 15.890 1.941   124.974 1.00 86.91  ? 35  ASP A CB  1 
ATOM   325  C CG  . ASP A 1 55  ? 16.860 0.765   125.066 1.00 94.75  ? 35  ASP A CG  1 
ATOM   326  O OD1 . ASP A 1 55  ? 17.833 0.685   124.242 1.00 80.91  ? 35  ASP A OD1 1 
ATOM   327  O OD2 . ASP A 1 55  ? 16.644 -0.072  125.971 1.00 91.78  ? 35  ASP A OD2 1 
ATOM   328  N N   . ILE A 1 56  ? 17.067 2.804   121.665 1.00 84.08  ? 36  ILE A N   1 
ATOM   329  C CA  . ILE A 1 56  ? 17.040 2.557   120.220 1.00 83.52  ? 36  ILE A CA  1 
ATOM   330  C C   . ILE A 1 56  ? 18.507 2.468   119.806 1.00 69.92  ? 36  ILE A C   1 
ATOM   331  O O   . ILE A 1 56  ? 19.384 2.496   120.664 1.00 86.71  ? 36  ILE A O   1 
ATOM   332  C CB  . ILE A 1 56  ? 16.258 3.698   119.479 1.00 87.88  ? 36  ILE A CB  1 
ATOM   333  C CG1 . ILE A 1 56  ? 14.835 3.869   120.042 1.00 95.31  ? 36  ILE A CG1 1 
ATOM   334  C CG2 . ILE A 1 56  ? 16.126 3.488   117.979 1.00 82.57  ? 36  ILE A CG2 1 
ATOM   335  C CD1 . ILE A 1 56  ? 13.898 2.670   119.892 1.00 97.04  ? 36  ILE A CD1 1 
ATOM   336  N N   . THR A 1 57  ? 18.736 2.274   118.522 1.00 64.06  ? 37  THR A N   1 
ATOM   337  C CA  . THR A 1 57  ? 20.042 2.211   117.873 1.00 67.98  ? 37  THR A CA  1 
ATOM   338  C C   . THR A 1 57  ? 19.866 2.887   116.560 1.00 68.87  ? 37  THR A C   1 
ATOM   339  O O   . THR A 1 57  ? 18.734 3.224   116.191 1.00 71.94  ? 37  THR A O   1 
ATOM   340  C CB  . THR A 1 57  ? 20.347 0.773   117.475 1.00 73.99  ? 37  THR A CB  1 
ATOM   341  O OG1 . THR A 1 57  ? 20.202 -0.045  118.632 1.00 79.09  ? 37  THR A OG1 1 
ATOM   342  C CG2 . THR A 1 57  ? 21.793 0.588   116.861 1.00 83.16  ? 37  THR A CG2 1 
ATOM   343  N N   . THR A 1 58  ? 20.975 3.081   115.857 1.00 71.92  ? 38  THR A N   1 
ATOM   344  C CA  . THR A 1 58  ? 20.995 3.523   114.480 1.00 68.58  ? 38  THR A CA  1 
ATOM   345  C C   . THR A 1 58  ? 20.052 2.719   113.673 1.00 75.74  ? 38  THR A C   1 
ATOM   346  O O   . THR A 1 58  ? 19.084 3.242   113.083 1.00 74.62  ? 38  THR A O   1 
ATOM   347  C CB  . THR A 1 58  ? 22.382 3.293   113.821 1.00 76.01  ? 38  THR A CB  1 
ATOM   348  O OG1 . THR A 1 58  ? 23.261 4.358   114.179 1.00 83.55  ? 38  THR A OG1 1 
ATOM   349  C CG2 . THR A 1 58  ? 22.292 3.155   112.218 1.00 74.17  ? 38  THR A CG2 1 
ATOM   350  N N   . ASP A 1 59  ? 20.374 1.431   113.598 1.00 89.81  ? 39  ASP A N   1 
ATOM   351  C CA  . ASP A 1 59  ? 19.880 0.643   112.501 1.00 79.37  ? 39  ASP A CA  1 
ATOM   352  C C   . ASP A 1 59  ? 18.395 0.542   112.702 1.00 67.59  ? 39  ASP A C   1 
ATOM   353  O O   . ASP A 1 59  ? 17.620 0.910   111.838 1.00 69.35  ? 39  ASP A O   1 
ATOM   354  C CB  . ASP A 1 59  ? 20.650 -0.668  112.363 1.00 88.57  ? 39  ASP A CB  1 
ATOM   355  C CG  . ASP A 1 59  ? 21.906 -0.499  111.497 1.00 92.85  ? 39  ASP A CG  1 
ATOM   356  O OD1 . ASP A 1 59  ? 21.817 -0.326  110.248 1.00 74.28  ? 39  ASP A OD1 1 
ATOM   357  O OD2 . ASP A 1 59  ? 22.995 -0.510  112.081 1.00 96.48  ? 39  ASP A OD2 1 
ATOM   358  N N   . HIS A 1 60  ? 17.983 0.191   113.894 1.00 63.62  ? 40  HIS A N   1 
ATOM   359  C CA  . HIS A 1 60  ? 16.625 0.478   114.231 1.00 75.60  ? 40  HIS A CA  1 
ATOM   360  C C   . HIS A 1 60  ? 16.154 1.776   113.418 1.00 86.82  ? 40  HIS A C   1 
ATOM   361  O O   . HIS A 1 60  ? 15.348 1.694   112.457 1.00 89.49  ? 40  HIS A O   1 
ATOM   362  C CB  . HIS A 1 60  ? 16.497 0.643   115.752 1.00 92.65  ? 40  HIS A CB  1 
ATOM   363  C CG  . HIS A 1 60  ? 16.867 -0.578  116.566 1.00 104.36 ? 40  HIS A CG  1 
ATOM   364  N ND1 . HIS A 1 60  ? 16.192 -0.926  117.724 1.00 96.30  ? 40  HIS A ND1 1 
ATOM   365  C CD2 . HIS A 1 60  ? 17.849 -1.507  116.417 1.00 115.94 ? 40  HIS A CD2 1 
ATOM   366  C CE1 . HIS A 1 60  ? 16.725 -2.019  118.241 1.00 91.04  ? 40  HIS A CE1 1 
ATOM   367  N NE2 . HIS A 1 60  ? 17.728 -2.395  117.465 1.00 119.70 ? 40  HIS A NE2 1 
ATOM   368  N N   . TYR A 1 61  ? 16.697 2.949   113.758 1.00 80.76  ? 41  TYR A N   1 
ATOM   369  C CA  . TYR A 1 61  ? 16.211 4.234   113.201 1.00 64.20  ? 41  TYR A CA  1 
ATOM   370  C C   . TYR A 1 61  ? 16.156 4.214   111.688 1.00 58.57  ? 41  TYR A C   1 
ATOM   371  O O   . TYR A 1 61  ? 15.156 4.633   111.105 1.00 62.79  ? 41  TYR A O   1 
ATOM   372  C CB  . TYR A 1 61  ? 17.049 5.457   113.710 1.00 54.39  ? 41  TYR A CB  1 
ATOM   373  C CG  . TYR A 1 61  ? 16.660 6.816   113.141 1.00 42.83  ? 41  TYR A CG  1 
ATOM   374  C CD1 . TYR A 1 61  ? 15.507 7.425   113.539 1.00 48.84  ? 41  TYR A CD1 1 
ATOM   375  C CD2 . TYR A 1 61  ? 17.441 7.464   112.193 1.00 42.50  ? 41  TYR A CD2 1 
ATOM   376  C CE1 . TYR A 1 61  ? 15.099 8.654   113.023 1.00 50.65  ? 41  TYR A CE1 1 
ATOM   377  C CE2 . TYR A 1 61  ? 17.056 8.705   111.661 1.00 44.35  ? 41  TYR A CE2 1 
ATOM   378  C CZ  . TYR A 1 61  ? 15.875 9.308   112.103 1.00 53.77  ? 41  TYR A CZ  1 
ATOM   379  O OH  . TYR A 1 61  ? 15.378 10.530  111.633 1.00 47.73  ? 41  TYR A OH  1 
ATOM   380  N N   . ALA A 1 62  ? 17.205 3.779   111.028 1.00 48.25  ? 42  ALA A N   1 
ATOM   381  C CA  . ALA A 1 62  ? 17.211 3.894   109.522 1.00 56.92  ? 42  ALA A CA  1 
ATOM   382  C C   . ALA A 1 62  ? 16.091 3.113   108.793 1.00 63.42  ? 42  ALA A C   1 
ATOM   383  O O   . ALA A 1 62  ? 15.669 3.493   107.693 1.00 57.19  ? 42  ALA A O   1 
ATOM   384  C CB  . ALA A 1 62  ? 18.545 3.436   108.955 1.00 58.61  ? 42  ALA A CB  1 
ATOM   385  N N   . LEU A 1 63  ? 15.669 2.004   109.413 1.00 64.82  ? 43  LEU A N   1 
ATOM   386  C CA  . LEU A 1 63  ? 14.588 1.164   108.931 1.00 65.46  ? 43  LEU A CA  1 
ATOM   387  C C   . LEU A 1 63  ? 13.310 1.876   109.193 1.00 60.63  ? 43  LEU A C   1 
ATOM   388  O O   . LEU A 1 63  ? 12.463 2.001   108.288 1.00 62.99  ? 43  LEU A O   1 
ATOM   389  C CB  . LEU A 1 63  ? 14.547 -0.206  109.671 1.00 73.31  ? 43  LEU A CB  1 
ATOM   390  C CG  . LEU A 1 63  ? 15.261 -1.448  109.082 1.00 73.69  ? 43  LEU A CG  1 
ATOM   391  C CD1 . LEU A 1 63  ? 16.173 -1.153  107.884 1.00 66.37  ? 43  LEU A CD1 1 
ATOM   392  C CD2 . LEU A 1 63  ? 15.992 -2.237  110.182 1.00 76.01  ? 43  LEU A CD2 1 
ATOM   393  N N   . LEU A 1 64  ? 13.156 2.334   110.439 1.00 56.68  ? 44  LEU A N   1 
ATOM   394  C CA  . LEU A 1 64  ? 11.959 3.109   110.814 1.00 53.62  ? 44  LEU A CA  1 
ATOM   395  C C   . LEU A 1 64  ? 11.701 4.271   109.852 1.00 43.71  ? 44  LEU A C   1 
ATOM   396  O O   . LEU A 1 64  ? 10.581 4.544   109.527 1.00 53.97  ? 44  LEU A O   1 
ATOM   397  C CB  . LEU A 1 64  ? 12.067 3.622   112.234 1.00 57.58  ? 44  LEU A CB  1 
ATOM   398  C CG  . LEU A 1 64  ? 12.037 2.490   113.249 1.00 60.52  ? 44  LEU A CG  1 
ATOM   399  C CD1 . LEU A 1 64  ? 12.561 2.913   114.617 1.00 69.16  ? 44  LEU A CD1 1 
ATOM   400  C CD2 . LEU A 1 64  ? 10.637 1.991   113.395 1.00 58.12  ? 44  LEU A CD2 1 
ATOM   401  N N   . ARG A 1 65  ? 12.738 4.903   109.342 1.00 41.98  ? 45  ARG A N   1 
ATOM   402  C CA  . ARG A 1 65  ? 12.561 5.970   108.404 1.00 47.66  ? 45  ARG A CA  1 
ATOM   403  C C   . ARG A 1 65  ? 11.761 5.442   107.220 1.00 58.11  ? 45  ARG A C   1 
ATOM   404  O O   . ARG A 1 65  ? 10.825 6.100   106.740 1.00 59.97  ? 45  ARG A O   1 
ATOM   405  C CB  . ARG A 1 65  ? 13.910 6.465   107.897 1.00 48.73  ? 45  ARG A CB  1 
ATOM   406  C CG  . ARG A 1 65  ? 14.751 7.262   108.884 1.00 51.93  ? 45  ARG A CG  1 
ATOM   407  C CD  . ARG A 1 65  ? 14.304 8.693   108.981 1.00 49.47  ? 45  ARG A CD  1 
ATOM   408  N NE  . ARG A 1 65  ? 14.569 9.458   107.776 1.00 50.91  ? 45  ARG A NE  1 
ATOM   409  C CZ  . ARG A 1 65  ? 14.041 10.659  107.551 1.00 60.34  ? 45  ARG A CZ  1 
ATOM   410  N NH1 . ARG A 1 65  ? 13.216 11.208  108.458 1.00 66.16  ? 45  ARG A NH1 1 
ATOM   411  N NH2 . ARG A 1 65  ? 14.325 11.320  106.433 1.00 53.58  ? 45  ARG A NH2 1 
ATOM   412  N N   . PHE A 1 66  ? 12.155 4.257   106.740 1.00 59.05  ? 46  PHE A N   1 
ATOM   413  C CA  . PHE A 1 66  ? 11.476 3.615   105.606 1.00 56.18  ? 46  PHE A CA  1 
ATOM   414  C C   . PHE A 1 66  ? 10.045 3.298   105.986 1.00 53.49  ? 46  PHE A C   1 
ATOM   415  O O   . PHE A 1 66  ? 9.128  3.576   105.205 1.00 46.81  ? 46  PHE A O   1 
ATOM   416  C CB  . PHE A 1 66  ? 12.133 2.306   105.240 1.00 55.52  ? 46  PHE A CB  1 
ATOM   417  C CG  . PHE A 1 66  ? 13.505 2.442   104.658 1.00 53.80  ? 46  PHE A CG  1 
ATOM   418  C CD1 . PHE A 1 66  ? 13.756 3.352   103.623 1.00 51.58  ? 46  PHE A CD1 1 
ATOM   419  C CD2 . PHE A 1 66  ? 14.531 1.599   105.092 1.00 46.93  ? 46  PHE A CD2 1 
ATOM   420  C CE1 . PHE A 1 66  ? 15.008 3.433   103.046 1.00 48.43  ? 46  PHE A CE1 1 
ATOM   421  C CE2 . PHE A 1 66  ? 15.779 1.688   104.524 1.00 42.53  ? 46  PHE A CE2 1 
ATOM   422  C CZ  . PHE A 1 66  ? 16.010 2.595   103.493 1.00 45.42  ? 46  PHE A CZ  1 
ATOM   423  N N   . LEU A 1 67  ? 9.866  2.730   107.182 1.00 42.93  ? 47  LEU A N   1 
ATOM   424  C CA  . LEU A 1 67  ? 8.529  2.456   107.655 1.00 48.42  ? 47  LEU A CA  1 
ATOM   425  C C   . LEU A 1 67  ? 7.648  3.730   107.802 1.00 56.69  ? 47  LEU A C   1 
ATOM   426  O O   . LEU A 1 67  ? 6.515  3.723   107.358 1.00 53.48  ? 47  LEU A O   1 
ATOM   427  C CB  . LEU A 1 67  ? 8.588  1.670   108.956 1.00 52.92  ? 47  LEU A CB  1 
ATOM   428  C CG  . LEU A 1 67  ? 9.215  0.294   108.833 1.00 53.34  ? 47  LEU A CG  1 
ATOM   429  C CD1 . LEU A 1 67  ? 9.094  -0.478  110.123 1.00 59.70  ? 47  LEU A CD1 1 
ATOM   430  C CD2 . LEU A 1 67  ? 8.539  -0.480  107.752 1.00 59.78  ? 47  LEU A CD2 1 
ATOM   431  N N   . TRP A 1 68  ? 8.149  4.839   108.359 1.00 56.18  ? 48  TRP A N   1 
ATOM   432  C CA  . TRP A 1 68  ? 7.301  6.042   108.426 1.00 52.21  ? 48  TRP A CA  1 
ATOM   433  C C   . TRP A 1 68  ? 6.974  6.558   107.036 1.00 51.40  ? 48  TRP A C   1 
ATOM   434  O O   . TRP A 1 68  ? 5.945  7.171   106.845 1.00 56.75  ? 48  TRP A O   1 
ATOM   435  C CB  . TRP A 1 68  ? 7.920  7.185   109.272 1.00 49.72  ? 48  TRP A CB  1 
ATOM   436  C CG  . TRP A 1 68  ? 8.279  6.780   110.661 1.00 45.38  ? 48  TRP A CG  1 
ATOM   437  C CD1 . TRP A 1 68  ? 7.487  6.115   111.531 1.00 47.60  ? 48  TRP A CD1 1 
ATOM   438  C CD2 . TRP A 1 68  ? 9.535  6.976   111.329 1.00 45.04  ? 48  TRP A CD2 1 
ATOM   439  N NE1 . TRP A 1 68  ? 8.163  5.874   112.701 1.00 46.08  ? 48  TRP A NE1 1 
ATOM   440  C CE2 . TRP A 1 68  ? 9.425  6.401   112.597 1.00 45.41  ? 48  TRP A CE2 1 
ATOM   441  C CE3 . TRP A 1 68  ? 10.723 7.622   110.991 1.00 47.64  ? 48  TRP A CE3 1 
ATOM   442  C CZ2 . TRP A 1 68  ? 10.444 6.446   113.520 1.00 47.40  ? 48  TRP A CZ2 1 
ATOM   443  C CZ3 . TRP A 1 68  ? 11.726 7.638   111.889 1.00 51.09  ? 48  TRP A CZ3 1 
ATOM   444  C CH2 . TRP A 1 68  ? 11.588 7.040   113.153 1.00 49.41  ? 48  TRP A CH2 1 
ATOM   445  N N   . GLU A 1 69  ? 7.861  6.375   106.067 1.00 57.57  ? 49  GLU A N   1 
ATOM   446  C CA  . GLU A 1 69  ? 7.559  6.814   104.703 1.00 61.08  ? 49  GLU A CA  1 
ATOM   447  C C   . GLU A 1 69  ? 6.460  5.924   104.134 1.00 61.12  ? 49  GLU A C   1 
ATOM   448  O O   . GLU A 1 69  ? 5.590  6.403   103.395 1.00 63.84  ? 49  GLU A O   1 
ATOM   449  C CB  . GLU A 1 69  ? 8.774  6.729   103.785 1.00 75.13  ? 49  GLU A CB  1 
ATOM   450  C CG  . GLU A 1 69  ? 9.423  8.062   103.432 1.00 93.26  ? 49  GLU A CG  1 
ATOM   451  C CD  . GLU A 1 69  ? 8.919  8.651   102.114 1.00 100.64 ? 49  GLU A CD  1 
ATOM   452  O OE1 . GLU A 1 69  ? 7.770  9.164   102.096 1.00 94.19  ? 49  GLU A OE1 1 
ATOM   453  O OE2 . GLU A 1 69  ? 9.686  8.622   101.108 1.00 95.43  ? 49  GLU A OE2 1 
ATOM   454  N N   . GLN A 1 70  ? 6.463  4.655   104.525 1.00 54.69  ? 50  GLN A N   1 
ATOM   455  C CA  . GLN A 1 70  ? 5.619  3.665   103.874 1.00 66.50  ? 50  GLN A CA  1 
ATOM   456  C C   . GLN A 1 70  ? 5.320  2.481   104.812 1.00 59.28  ? 50  GLN A C   1 
ATOM   457  O O   . GLN A 1 70  ? 5.925  1.437   104.753 1.00 61.25  ? 50  GLN A O   1 
ATOM   458  C CB  . GLN A 1 70  ? 6.348  3.276   102.580 1.00 77.53  ? 50  GLN A CB  1 
ATOM   459  C CG  . GLN A 1 70  ? 6.270  1.842   102.103 1.00 91.25  ? 50  GLN A CG  1 
ATOM   460  C CD  . GLN A 1 70  ? 5.573  1.674   100.783 1.00 96.98  ? 50  GLN A CD  1 
ATOM   461  O OE1 . GLN A 1 70  ? 5.574  0.580   100.233 1.00 84.31  ? 50  GLN A OE1 1 
ATOM   462  N NE2 . GLN A 1 70  ? 4.943  2.736   100.284 1.00 101.56 ? 50  GLN A NE2 1 
ATOM   463  N N   . ASP A 1 71  ? 4.368  2.677   105.704 1.00 65.14  ? 51  ASP A N   1 
ATOM   464  C CA  . ASP A 1 71  ? 4.015  1.662   106.701 1.00 63.76  ? 51  ASP A CA  1 
ATOM   465  C C   . ASP A 1 71  ? 3.314  0.533   105.932 1.00 68.63  ? 51  ASP A C   1 
ATOM   466  O O   . ASP A 1 71  ? 2.445  0.817   105.088 1.00 63.29  ? 51  ASP A O   1 
ATOM   467  C CB  . ASP A 1 71  ? 3.080  2.297   107.747 1.00 56.62  ? 51  ASP A CB  1 
ATOM   468  C CG  . ASP A 1 71  ? 2.981  1.498   109.080 1.00 62.32  ? 51  ASP A CG  1 
ATOM   469  O OD1 . ASP A 1 71  ? 3.767  0.537   109.346 1.00 50.04  ? 51  ASP A OD1 1 
ATOM   470  O OD2 . ASP A 1 71  ? 2.088  1.908   109.890 1.00 68.62  ? 51  ASP A OD2 1 
ATOM   471  N N   . GLY A 1 72  ? 3.700  -0.712  106.199 1.00 64.42  ? 52  GLY A N   1 
ATOM   472  C CA  . GLY A 1 72  ? 3.095  -1.861  105.537 1.00 78.34  ? 52  GLY A CA  1 
ATOM   473  C C   . GLY A 1 72  ? 3.793  -2.305  104.261 1.00 80.20  ? 52  GLY A C   1 
ATOM   474  O O   . GLY A 1 72  ? 3.270  -3.138  103.521 1.00 88.72  ? 52  GLY A O   1 
ATOM   475  N N   . ILE A 1 73  ? 4.958  -1.726  104.003 1.00 74.73  ? 53  ILE A N   1 
ATOM   476  C CA  . ILE A 1 73  ? 5.889  -2.198  102.990 1.00 68.22  ? 53  ILE A CA  1 
ATOM   477  C C   . ILE A 1 73  ? 6.236  -3.704  103.120 1.00 68.63  ? 53  ILE A C   1 
ATOM   478  O O   . ILE A 1 73  ? 6.249  -4.288  104.248 1.00 63.94  ? 53  ILE A O   1 
ATOM   479  C CB  . ILE A 1 73  ? 7.203  -1.357  103.072 1.00 75.59  ? 53  ILE A CB  1 
ATOM   480  C CG1 . ILE A 1 73  ? 7.887  -1.265  101.695 1.00 80.07  ? 53  ILE A CG1 1 
ATOM   481  C CG2 . ILE A 1 73  ? 8.133  -1.873  104.181 1.00 70.63  ? 53  ILE A CG2 1 
ATOM   482  C CD1 . ILE A 1 73  ? 9.266  -0.636  101.691 1.00 81.19  ? 53  ILE A CD1 1 
ATOM   483  N N   . SER A 1 74  ? 6.538  -4.324  101.972 1.00 63.85  ? 54  SER A N   1 
ATOM   484  C CA  . SER A 1 74  ? 6.941  -5.749  101.944 1.00 72.76  ? 54  SER A CA  1 
ATOM   485  C C   . SER A 1 74  ? 8.372  -6.007  102.438 1.00 70.16  ? 54  SER A C   1 
ATOM   486  O O   . SER A 1 74  ? 9.297  -5.345  101.983 1.00 78.79  ? 54  SER A O   1 
ATOM   487  C CB  . SER A 1 74  ? 6.784  -6.329  100.527 1.00 74.83  ? 54  SER A CB  1 
ATOM   488  O OG  . SER A 1 74  ? 7.736  -5.819  99.605  1.00 74.55  ? 54  SER A OG  1 
ATOM   489  N N   . GLN A 1 75  ? 8.554  -7.012  103.307 1.00 70.61  ? 55  GLN A N   1 
ATOM   490  C CA  . GLN A 1 75  ? 9.892  -7.392  103.827 1.00 78.68  ? 55  GLN A CA  1 
ATOM   491  C C   . GLN A 1 75  ? 10.896 -7.673  102.706 1.00 81.49  ? 55  GLN A C   1 
ATOM   492  O O   . GLN A 1 75  ? 12.071 -7.901  102.972 1.00 85.92  ? 55  GLN A O   1 
ATOM   493  C CB  . GLN A 1 75  ? 9.821  -8.557  104.873 1.00 71.52  ? 55  GLN A CB  1 
ATOM   494  C CG  . GLN A 1 75  ? 11.167 -9.090  105.439 1.00 63.95  ? 55  GLN A CG  1 
ATOM   495  C CD  . GLN A 1 75  ? 11.025 -9.840  106.778 1.00 70.69  ? 55  GLN A CD  1 
ATOM   496  O OE1 . GLN A 1 75  ? 12.012 -10.214 107.405 1.00 77.60  ? 55  GLN A OE1 1 
ATOM   497  N NE2 . GLN A 1 75  ? 9.800  -10.045 107.228 1.00 72.76  ? 55  GLN A NE2 1 
ATOM   498  N N   . ILE A 1 76  ? 10.423 -7.617  101.462 1.00 93.16  ? 56  ILE A N   1 
ATOM   499  C CA  . ILE A 1 76  ? 11.273 -7.678  100.272 1.00 100.27 ? 56  ILE A CA  1 
ATOM   500  C C   . ILE A 1 76  ? 11.551 -6.274  99.721  1.00 100.92 ? 56  ILE A C   1 
ATOM   501  O O   . ILE A 1 76  ? 12.710 -5.947  99.482  1.00 112.95 ? 56  ILE A O   1 
ATOM   502  C CB  . ILE A 1 76  ? 10.656 -8.626  99.202  1.00 100.46 ? 56  ILE A CB  1 
ATOM   503  C CG1 . ILE A 1 76  ? 10.385 -10.024 99.830  1.00 100.54 ? 56  ILE A CG1 1 
ATOM   504  C CG2 . ILE A 1 76  ? 11.502 -8.677  97.925  1.00 89.18  ? 56  ILE A CG2 1 
ATOM   505  C CD1 . ILE A 1 76  ? 11.444 -10.559 100.784 1.00 95.28  ? 56  ILE A CD1 1 
ATOM   506  N N   . ASP A 1 77  ? 10.530 -5.433  99.542  1.00 97.68  ? 57  ASP A N   1 
ATOM   507  C CA  . ASP A 1 77  ? 10.802 -4.023  99.207  1.00 101.44 ? 57  ASP A CA  1 
ATOM   508  C C   . ASP A 1 77  ? 11.799 -3.386  100.192 1.00 99.08  ? 57  ASP A C   1 
ATOM   509  O O   . ASP A 1 77  ? 12.630 -2.568  99.782  1.00 90.10  ? 57  ASP A O   1 
ATOM   510  C CB  . ASP A 1 77  ? 9.537  -3.165  99.212  1.00 103.79 ? 57  ASP A CB  1 
ATOM   511  C CG  . ASP A 1 77  ? 8.828  -3.147  97.883  1.00 98.86  ? 57  ASP A CG  1 
ATOM   512  O OD1 . ASP A 1 77  ? 8.253  -4.190  97.549  1.00 85.47  ? 57  ASP A OD1 1 
ATOM   513  O OD2 . ASP A 1 77  ? 8.803  -2.085  97.214  1.00 94.77  ? 57  ASP A OD2 1 
ATOM   514  N N   . LEU A 1 78  ? 11.689 -3.760  101.473 1.00 90.76  ? 58  LEU A N   1 
ATOM   515  C CA  . LEU A 1 78  ? 12.497 -3.185  102.556 1.00 95.11  ? 58  LEU A CA  1 
ATOM   516  C C   . LEU A 1 78  ? 13.957 -3.526  102.307 1.00 102.70 ? 58  LEU A C   1 
ATOM   517  O O   . LEU A 1 78  ? 14.842 -2.660  102.285 1.00 97.94  ? 58  LEU A O   1 
ATOM   518  C CB  . LEU A 1 78  ? 12.084 -3.768  103.928 1.00 90.96  ? 58  LEU A CB  1 
ATOM   519  C CG  . LEU A 1 78  ? 11.792 -2.876  105.162 1.00 86.43  ? 58  LEU A CG  1 
ATOM   520  C CD1 . LEU A 1 78  ? 12.022 -3.607  106.499 1.00 79.17  ? 58  LEU A CD1 1 
ATOM   521  C CD2 . LEU A 1 78  ? 12.581 -1.582  105.118 1.00 87.79  ? 58  LEU A CD2 1 
ATOM   522  N N   . CYS A 1 79  ? 14.188 -4.813  102.095 1.00 105.28 ? 59  CYS A N   1 
ATOM   523  C CA  . CYS A 1 79  ? 15.525 -5.333  101.910 1.00 95.43  ? 59  CYS A CA  1 
ATOM   524  C C   . CYS A 1 79  ? 16.189 -4.729  100.680 1.00 93.58  ? 59  CYS A C   1 
ATOM   525  O O   . CYS A 1 79  ? 17.423 -4.641  100.609 1.00 110.63 ? 59  CYS A O   1 
ATOM   526  C CB  . CYS A 1 79  ? 15.452 -6.854  101.866 1.00 89.00  ? 59  CYS A CB  1 
ATOM   527  S SG  . CYS A 1 79  ? 15.057 -7.553  103.504 1.00 93.60  ? 59  CYS A SG  1 
ATOM   528  N N   . GLU A 1 80  ? 15.363 -4.264  99.743  1.00 91.70  ? 60  GLU A N   1 
ATOM   529  C CA  . GLU A 1 80  ? 15.830 -3.599  98.512  1.00 100.63 ? 60  GLU A CA  1 
ATOM   530  C C   . GLU A 1 80  ? 16.082 -2.093  98.660  1.00 99.30  ? 60  GLU A C   1 
ATOM   531  O O   . GLU A 1 80  ? 16.831 -1.517  97.873  1.00 94.26  ? 60  GLU A O   1 
ATOM   532  C CB  . GLU A 1 80  ? 14.824 -3.812  97.370  1.00 104.11 ? 60  GLU A CB  1 
ATOM   533  C CG  . GLU A 1 80  ? 15.432 -3.744  95.975  1.00 115.42 ? 60  GLU A CG  1 
ATOM   534  C CD  . GLU A 1 80  ? 14.637 -2.858  95.023  1.00 126.08 ? 60  GLU A CD  1 
ATOM   535  O OE1 . GLU A 1 80  ? 13.423 -3.113  94.810  1.00 119.38 ? 60  GLU A OE1 1 
ATOM   536  O OE2 . GLU A 1 80  ? 15.239 -1.900  94.478  1.00 121.85 ? 60  GLU A OE2 1 
ATOM   537  N N   . LYS A 1 81  ? 15.424 -1.451  99.625  1.00 106.10 ? 61  LYS A N   1 
ATOM   538  C CA  . LYS A 1 81  ? 15.745 -0.061  100.001 1.00 93.30  ? 61  LYS A CA  1 
ATOM   539  C C   . LYS A 1 81  ? 16.937 -0.048  100.968 1.00 86.20  ? 61  LYS A C   1 
ATOM   540  O O   . LYS A 1 81  ? 17.800 0.825   100.877 1.00 78.61  ? 61  LYS A O   1 
ATOM   541  C CB  . LYS A 1 81  ? 14.531 0.639   100.616 1.00 93.70  ? 61  LYS A CB  1 
ATOM   542  C CG  . LYS A 1 81  ? 13.593 1.253   99.586  1.00 89.43  ? 61  LYS A CG  1 
ATOM   543  C CD  . LYS A 1 81  ? 12.386 1.898   100.255 1.00 83.01  ? 61  LYS A CD  1 
ATOM   544  C CE  . LYS A 1 81  ? 11.284 2.257   99.265  1.00 86.19  ? 61  LYS A CE  1 
ATOM   545  N NZ  . LYS A 1 81  ? 11.619 3.461   98.444  1.00 89.93  ? 61  LYS A NZ  1 
ATOM   546  N N   . SER A 1 82  ? 16.884 -0.997  101.888 1.00 80.38  ? 62  SER A N   1 
ATOM   547  C CA  . SER A 1 82  ? 17.900 -1.217  102.881 1.00 77.51  ? 62  SER A CA  1 
ATOM   548  C C   . SER A 1 82  ? 19.153 -1.624  102.232 1.00 98.15  ? 62  SER A C   1 
ATOM   549  O O   . SER A 1 82  ? 20.168 -1.599  102.874 1.00 109.15 ? 62  SER A O   1 
ATOM   550  C CB  . SER A 1 82  ? 17.524 -2.328  103.834 1.00 75.08  ? 62  SER A CB  1 
ATOM   551  O OG  . SER A 1 82  ? 18.617 -2.621  104.682 1.00 75.33  ? 62  SER A OG  1 
ATOM   552  N N   . CYS A 1 83  ? 19.041 -2.155  101.026 1.00 109.83 ? 63  CYS A N   1 
ATOM   553  C CA  . CYS A 1 83  ? 20.165 -2.583  100.242 1.00 119.60 ? 63  CYS A CA  1 
ATOM   554  C C   . CYS A 1 83  ? 20.761 -3.863  100.805 1.00 116.18 ? 63  CYS A C   1 
ATOM   555  O O   . CYS A 1 83  ? 20.803 -4.886  100.138 1.00 88.44  ? 63  CYS A O   1 
ATOM   556  C CB  . CYS A 1 83  ? 21.182 -1.439  100.174 1.00 122.06 ? 63  CYS A CB  1 
ATOM   557  S SG  . CYS A 1 83  ? 22.502 -1.379  101.399 1.00 107.33 ? 63  CYS A SG  1 
ATOM   558  N N   . LYS A 1 84  ? 21.181 -3.778  102.059 1.00 124.86 ? 64  LYS A N   1 
ATOM   559  C CA  . LYS A 1 84  ? 21.939 -4.815  102.739 1.00 122.05 ? 64  LYS A CA  1 
ATOM   560  C C   . LYS A 1 84  ? 21.165 -6.014  103.283 1.00 134.93 ? 64  LYS A C   1 
ATOM   561  O O   . LYS A 1 84  ? 19.939 -5.992  103.410 1.00 127.85 ? 64  LYS A O   1 
ATOM   562  C CB  . LYS A 1 84  ? 22.784 -4.193  103.833 1.00 109.77 ? 64  LYS A CB  1 
ATOM   563  C CG  . LYS A 1 84  ? 22.003 -3.296  104.753 1.00 103.64 ? 64  LYS A CG  1 
ATOM   564  C CD  . LYS A 1 84  ? 22.888 -2.752  105.849 1.00 103.28 ? 64  LYS A CD  1 
ATOM   565  C CE  . LYS A 1 84  ? 23.715 -3.840  106.507 1.00 107.44 ? 64  LYS A CE  1 
ATOM   566  N NZ  . LYS A 1 84  ? 24.779 -3.274  107.389 1.00 109.55 ? 64  LYS A NZ  1 
ATOM   567  N N   . ASP A 1 85  ? 21.949 -7.038  103.625 1.00 135.93 ? 65  ASP A N   1 
ATOM   568  C CA  . ASP A 1 85  ? 21.550 -8.414  103.917 1.00 124.28 ? 65  ASP A CA  1 
ATOM   569  C C   . ASP A 1 85  ? 20.421 -8.625  104.902 1.00 113.54 ? 65  ASP A C   1 
ATOM   570  O O   . ASP A 1 85  ? 20.320 -8.009  105.953 1.00 91.81  ? 65  ASP A O   1 
ATOM   571  C CB  . ASP A 1 85  ? 22.799 -9.306  104.222 1.00 122.68 ? 65  ASP A CB  1 
ATOM   572  C CG  . ASP A 1 85  ? 22.829 -9.919  105.655 1.00 120.94 ? 65  ASP A CG  1 
ATOM   573  O OD1 . ASP A 1 85  ? 21.855 -10.583 106.072 1.00 114.03 ? 65  ASP A OD1 1 
ATOM   574  O OD2 . ASP A 1 85  ? 23.840 -9.741  106.349 1.00 97.88  ? 65  ASP A OD2 1 
ATOM   575  N N   . LYS A 1 86  ? 19.632 -9.602  104.510 1.00 109.72 ? 66  LYS A N   1 
ATOM   576  C CA  . LYS A 1 86  ? 18.435 -10.019 105.168 1.00 109.64 ? 66  LYS A CA  1 
ATOM   577  C C   . LYS A 1 86  ? 18.600 -10.622 106.554 1.00 118.08 ? 66  LYS A C   1 
ATOM   578  O O   . LYS A 1 86  ? 17.838 -10.293 107.471 1.00 116.14 ? 66  LYS A O   1 
ATOM   579  C CB  . LYS A 1 86  ? 17.753 -11.007 104.247 1.00 99.47  ? 66  LYS A CB  1 
ATOM   580  C CG  . LYS A 1 86  ? 17.586 -10.487 102.833 1.00 96.52  ? 66  LYS A CG  1 
ATOM   581  C CD  . LYS A 1 86  ? 18.866 -10.444 102.036 1.00 100.11 ? 66  LYS A CD  1 
ATOM   582  C CE  . LYS A 1 86  ? 19.348 -9.018  101.859 1.00 96.04  ? 66  LYS A CE  1 
ATOM   583  N NZ  . LYS A 1 86  ? 18.910 -8.445  100.561 1.00 93.82  ? 66  LYS A NZ  1 
ATOM   584  N N   . SER A 1 87  ? 19.580 -11.496 106.743 1.00 120.38 ? 67  SER A N   1 
ATOM   585  C CA  . SER A 1 87  ? 19.617 -12.136 108.078 1.00 125.18 ? 67  SER A CA  1 
ATOM   586  C C   . SER A 1 87  ? 19.796 -11.105 109.193 1.00 128.08 ? 67  SER A C   1 
ATOM   587  O O   . SER A 1 87  ? 19.235 -11.240 110.272 1.00 122.56 ? 67  SER A O   1 
ATOM   588  C CB  . SER A 1 87  ? 20.757 -13.160 108.152 1.00 117.03 ? 67  SER A CB  1 
ATOM   589  O OG  . SER A 1 87  ? 21.341 -13.335 106.871 1.00 116.24 ? 67  SER A OG  1 
ATOM   590  N N   . ASN A 1 88  ? 20.606 -10.087 108.931 1.00 136.91 ? 68  ASN A N   1 
ATOM   591  C CA  . ASN A 1 88  ? 20.738 -8.958  109.849 1.00 128.82 ? 68  ASN A CA  1 
ATOM   592  C C   . ASN A 1 88  ? 19.467 -8.082  109.719 1.00 123.51 ? 68  ASN A C   1 
ATOM   593  O O   . ASN A 1 88  ? 18.733 -7.870  110.702 1.00 89.06  ? 68  ASN A O   1 
ATOM   594  C CB  . ASN A 1 88  ? 22.020 -8.149  109.546 1.00 122.29 ? 68  ASN A CB  1 
ATOM   595  C CG  . ASN A 1 88  ? 23.286 -9.015  109.486 1.00 117.57 ? 68  ASN A CG  1 
ATOM   596  O OD1 . ASN A 1 88  ? 23.643 -9.693  110.455 1.00 93.15  ? 68  ASN A OD1 1 
ATOM   597  N ND2 . ASN A 1 88  ? 23.985 -8.970  108.346 1.00 114.54 ? 68  ASN A ND2 1 
ATOM   598  N N   . THR A 1 89  ? 19.198 -7.617  108.490 1.00 116.52 ? 69  THR A N   1 
ATOM   599  C CA  . THR A 1 89  ? 17.962 -6.908  108.183 1.00 97.74  ? 69  THR A CA  1 
ATOM   600  C C   . THR A 1 89  ? 16.881 -7.620  109.020 1.00 102.61 ? 69  THR A C   1 
ATOM   601  O O   . THR A 1 89  ? 16.239 -6.999  109.880 1.00 94.12  ? 69  THR A O   1 
ATOM   602  C CB  . THR A 1 89  ? 17.684 -6.861  106.644 1.00 100.48 ? 69  THR A CB  1 
ATOM   603  O OG1 . THR A 1 89  ? 18.847 -6.403  105.926 1.00 92.83  ? 69  THR A OG1 1 
ATOM   604  C CG2 . THR A 1 89  ? 16.560 -5.898  106.301 1.00 99.67  ? 69  THR A CG2 1 
ATOM   605  N N   . THR A 1 90  ? 16.789 -8.942  108.851 1.00 102.06 ? 70  THR A N   1 
ATOM   606  C CA  . THR A 1 90  ? 15.855 -9.813  109.603 1.00 113.97 ? 70  THR A CA  1 
ATOM   607  C C   . THR A 1 90  ? 16.065 -9.865  111.136 1.00 116.06 ? 70  THR A C   1 
ATOM   608  O O   . THR A 1 90  ? 15.095 -9.854  111.908 1.00 89.99  ? 70  THR A O   1 
ATOM   609  C CB  . THR A 1 90  ? 15.930 -11.261 109.045 1.00 120.16 ? 70  THR A CB  1 
ATOM   610  O OG1 . THR A 1 90  ? 15.645 -11.228 107.639 1.00 111.64 ? 70  THR A OG1 1 
ATOM   611  C CG2 . THR A 1 90  ? 14.963 -12.250 109.776 1.00 109.04 ? 70  THR A CG2 1 
ATOM   612  N N   . ARG A 1 91  ? 17.322 -9.961  111.566 1.00 120.39 ? 71  ARG A N   1 
ATOM   613  C CA  . ARG A 1 91  ? 17.650 -10.125 112.991 1.00 124.47 ? 71  ARG A CA  1 
ATOM   614  C C   . ARG A 1 91  ? 17.234 -8.841  113.756 1.00 121.15 ? 71  ARG A C   1 
ATOM   615  O O   . ARG A 1 91  ? 16.610 -8.882  114.835 1.00 97.81  ? 71  ARG A O   1 
ATOM   616  C CB  . ARG A 1 91  ? 19.159 -10.467 113.140 1.00 123.69 ? 71  ARG A CB  1 
ATOM   617  C CG  . ARG A 1 91  ? 19.663 -10.798 114.551 1.00 122.78 ? 71  ARG A CG  1 
ATOM   618  C CD  . ARG A 1 91  ? 21.202 -10.854 114.683 1.00 121.68 ? 71  ARG A CD  1 
ATOM   619  N NE  . ARG A 1 91  ? 22.002 -10.118 113.669 1.00 125.22 ? 71  ARG A NE  1 
ATOM   620  C CZ  . ARG A 1 91  ? 22.307 -8.806  113.680 1.00 120.76 ? 71  ARG A CZ  1 
ATOM   621  N NH1 . ARG A 1 91  ? 21.863 -7.988  114.624 1.00 122.19 ? 71  ARG A NH1 1 
ATOM   622  N NH2 . ARG A 1 91  ? 23.054 -8.286  112.713 1.00 111.35 ? 71  ARG A NH2 1 
ATOM   623  N N   . ILE A 1 92  ? 17.542 -7.697  113.156 1.00 121.46 ? 72  ILE A N   1 
ATOM   624  C CA  . ILE A 1 92  ? 17.227 -6.428  113.775 1.00 114.92 ? 72  ILE A CA  1 
ATOM   625  C C   . ILE A 1 92  ? 15.700 -6.405  113.825 1.00 110.53 ? 72  ILE A C   1 
ATOM   626  O O   . ILE A 1 92  ? 15.104 -6.251  114.914 1.00 87.02  ? 72  ILE A O   1 
ATOM   627  C CB  . ILE A 1 92  ? 17.849 -5.231  112.997 1.00 120.49 ? 72  ILE A CB  1 
ATOM   628  C CG1 . ILE A 1 92  ? 19.389 -5.358  112.863 1.00 102.72 ? 72  ILE A CG1 1 
ATOM   629  C CG2 . ILE A 1 92  ? 17.555 -3.908  113.700 1.00 125.21 ? 72  ILE A CG2 1 
ATOM   630  C CD1 . ILE A 1 92  ? 19.912 -4.861  111.528 1.00 92.70  ? 72  ILE A CD1 1 
ATOM   631  N N   . LEU A 1 93  ? 15.081 -6.653  112.662 1.00 103.60 ? 73  LEU A N   1 
ATOM   632  C CA  . LEU A 1 93  ? 13.608 -6.714  112.540 1.00 96.69  ? 73  LEU A CA  1 
ATOM   633  C C   . LEU A 1 93  ? 12.982 -7.558  113.680 1.00 102.68 ? 73  LEU A C   1 
ATOM   634  O O   . LEU A 1 93  ? 11.955 -7.181  114.306 1.00 82.67  ? 73  LEU A O   1 
ATOM   635  C CB  . LEU A 1 93  ? 13.205 -7.211  111.135 1.00 85.13  ? 73  LEU A CB  1 
ATOM   636  C CG  . LEU A 1 93  ? 13.538 -6.259  109.957 1.00 85.74  ? 73  LEU A CG  1 
ATOM   637  C CD1 . LEU A 1 93  ? 13.543 -6.928  108.610 1.00 82.42  ? 73  LEU A CD1 1 
ATOM   638  C CD2 . LEU A 1 93  ? 12.588 -5.082  109.829 1.00 90.18  ? 73  LEU A CD2 1 
ATOM   639  N N   . ASP A 1 94  ? 13.645 -8.676  113.978 1.00 113.82 ? 74  ASP A N   1 
ATOM   640  C CA  . ASP A 1 94  ? 13.259 -9.533  115.104 1.00 122.51 ? 74  ASP A CA  1 
ATOM   641  C C   . ASP A 1 94  ? 13.373 -8.753  116.422 1.00 118.56 ? 74  ASP A C   1 
ATOM   642  O O   . ASP A 1 94  ? 12.419 -8.683  117.208 1.00 89.77  ? 74  ASP A O   1 
ATOM   643  C CB  . ASP A 1 94  ? 14.129 -10.813 115.144 1.00 129.01 ? 74  ASP A CB  1 
ATOM   644  C CG  . ASP A 1 94  ? 13.644 -11.908 114.179 1.00 123.79 ? 74  ASP A CG  1 
ATOM   645  O OD1 . ASP A 1 94  ? 12.750 -12.689 114.581 1.00 109.51 ? 74  ASP A OD1 1 
ATOM   646  O OD2 . ASP A 1 94  ? 14.165 -11.999 113.039 1.00 118.16 ? 74  ASP A OD2 1 
ATOM   647  N N   . VAL A 1 95  ? 14.540 -8.148  116.641 1.00 128.27 ? 75  VAL A N   1 
ATOM   648  C CA  . VAL A 1 95  ? 14.783 -7.361  117.851 1.00 123.60 ? 75  VAL A CA  1 
ATOM   649  C C   . VAL A 1 95  ? 13.823 -6.174  117.898 1.00 120.05 ? 75  VAL A C   1 
ATOM   650  O O   . VAL A 1 95  ? 13.274 -5.841  118.972 1.00 100.41 ? 75  VAL A O   1 
ATOM   651  C CB  . VAL A 1 95  ? 16.236 -6.851  117.926 1.00 129.67 ? 75  VAL A CB  1 
ATOM   652  C CG1 . VAL A 1 95  ? 16.425 -5.944  119.142 1.00 130.79 ? 75  VAL A CG1 1 
ATOM   653  C CG2 . VAL A 1 95  ? 17.217 -8.019  117.981 1.00 133.74 ? 75  VAL A CG2 1 
ATOM   654  N N   . MET A 1 96  ? 13.624 -5.558  116.724 1.00 109.76 ? 76  MET A N   1 
ATOM   655  C CA  . MET A 1 96  ? 12.689 -4.444  116.560 1.00 103.81 ? 76  MET A CA  1 
ATOM   656  C C   . MET A 1 96  ? 11.304 -4.966  116.964 1.00 111.22 ? 76  MET A C   1 
ATOM   657  O O   . MET A 1 96  ? 10.569 -4.282  117.706 1.00 96.33  ? 76  MET A O   1 
ATOM   658  C CB  . MET A 1 96  ? 12.725 -3.861  115.108 1.00 100.65 ? 76  MET A CB  1 
ATOM   659  C CG  . MET A 1 96  ? 13.972 -3.017  114.739 1.00 93.24  ? 76  MET A CG  1 
ATOM   660  S SD  . MET A 1 96  ? 14.217 -2.371  113.035 1.00 94.32  ? 76  MET A SD  1 
ATOM   661  C CE  . MET A 1 96  ? 12.848 -1.221  112.974 1.00 90.84  ? 76  MET A CE  1 
ATOM   662  N N   . LYS A 1 97  ? 10.980 -6.189  116.510 1.00 114.36 ? 77  LYS A N   1 
ATOM   663  C CA  . LYS A 1 97  ? 9.733  -6.874  116.892 1.00 110.57 ? 77  LYS A CA  1 
ATOM   664  C C   . LYS A 1 97  ? 9.709  -7.235  118.380 1.00 107.00 ? 77  LYS A C   1 
ATOM   665  O O   . LYS A 1 97  ? 8.647  -7.200  119.014 1.00 96.81  ? 77  LYS A O   1 
ATOM   666  C CB  . LYS A 1 97  ? 9.483  -8.130  116.023 1.00 122.32 ? 77  LYS A CB  1 
ATOM   667  C CG  . LYS A 1 97  ? 8.336  -9.036  116.520 1.00 131.58 ? 77  LYS A CG  1 
ATOM   668  C CD  . LYS A 1 97  ? 7.733  -9.976  115.462 1.00 129.59 ? 77  LYS A CD  1 
ATOM   669  C CE  . LYS A 1 97  ? 8.575  -11.227 115.212 1.00 121.86 ? 77  LYS A CE  1 
ATOM   670  N NZ  . LYS A 1 97  ? 8.546  -12.170 116.361 1.00 110.50 ? 77  LYS A NZ  1 
ATOM   671  N N   . ASN A 1 98  ? 10.864 -7.609  118.927 1.00 110.12 ? 78  ASN A N   1 
ATOM   672  C CA  . ASN A 1 98  ? 10.984 -7.850  120.363 1.00 119.72 ? 78  ASN A CA  1 
ATOM   673  C C   . ASN A 1 98  ? 10.646 -6.588  121.148 1.00 121.57 ? 78  ASN A C   1 
ATOM   674  O O   . ASN A 1 98  ? 9.834  -6.627  122.080 1.00 99.72  ? 78  ASN A O   1 
ATOM   675  C CB  . ASN A 1 98  ? 12.404 -8.305  120.743 1.00 123.32 ? 78  ASN A CB  1 
ATOM   676  C CG  . ASN A 1 98  ? 12.582 -9.811  120.698 1.00 124.75 ? 78  ASN A CG  1 
ATOM   677  O OD1 . ASN A 1 98  ? 11.614 -10.583 120.760 1.00 116.73 ? 78  ASN A OD1 1 
ATOM   678  N ND2 . ASN A 1 98  ? 13.839 -10.237 120.607 1.00 115.83 ? 78  ASN A ND2 1 
ATOM   679  N N   . LYS A 1 99  ? 11.274 -5.474  120.763 1.00 121.99 ? 79  LYS A N   1 
ATOM   680  C CA  . LYS A 1 99  ? 11.137 -4.217  121.508 1.00 113.87 ? 79  LYS A CA  1 
ATOM   681  C C   . LYS A 1 99  ? 9.715  -3.645  121.469 1.00 110.06 ? 79  LYS A C   1 
ATOM   682  O O   . LYS A 1 99  ? 9.287  -2.933  122.379 1.00 104.81 ? 79  LYS A O   1 
ATOM   683  C CB  . LYS A 1 99  ? 12.129 -3.163  121.002 1.00 109.34 ? 79  LYS A CB  1 
ATOM   684  C CG  . LYS A 1 99  ? 13.455 -3.085  121.755 1.00 105.22 ? 79  LYS A CG  1 
ATOM   685  C CD  . LYS A 1 99  ? 13.873 -1.632  121.973 1.00 98.76  ? 79  LYS A CD  1 
ATOM   686  C CE  . LYS A 1 99  ? 15.374 -1.483  121.956 1.00 106.39 ? 79  LYS A CE  1 
ATOM   687  N NZ  . LYS A 1 99  ? 16.022 -2.317  122.999 1.00 111.91 ? 79  LYS A NZ  1 
ATOM   688  N N   . GLY A 1 100 ? 8.971  -3.971  120.428 1.00 103.86 ? 80  GLY A N   1 
ATOM   689  C CA  . GLY A 1 100 ? 7.647  -3.402  120.251 1.00 91.90  ? 80  GLY A CA  1 
ATOM   690  C C   . GLY A 1 100 ? 7.747  -2.335  119.200 1.00 83.81  ? 80  GLY A C   1 
ATOM   691  O O   . GLY A 1 100 ? 7.018  -1.367  119.286 1.00 85.93  ? 80  GLY A O   1 
ATOM   692  N N   . LEU A 1 101 ? 8.632  -2.529  118.206 1.00 75.95  ? 81  LEU A N   1 
ATOM   693  C CA  . LEU A 1 101 ? 8.878  -1.537  117.116 1.00 80.71  ? 81  LEU A CA  1 
ATOM   694  C C   . LEU A 1 101 ? 8.227  -1.868  115.775 1.00 79.85  ? 81  LEU A C   1 
ATOM   695  O O   . LEU A 1 101 ? 7.741  -0.999  115.086 1.00 75.41  ? 81  LEU A O   1 
ATOM   696  C CB  . LEU A 1 101 ? 10.375 -1.375  116.834 1.00 76.49  ? 81  LEU A CB  1 
ATOM   697  C CG  . LEU A 1 101 ? 11.304 -0.778  117.904 1.00 68.78  ? 81  LEU A CG  1 
ATOM   698  C CD1 . LEU A 1 101 ? 12.598 -0.352  117.231 1.00 64.71  ? 81  LEU A CD1 1 
ATOM   699  C CD2 . LEU A 1 101 ? 10.650 0.375   118.657 1.00 67.37  ? 81  LEU A CD2 1 
ATOM   700  N N   . ILE A 1 102 ? 8.255  -3.126  115.382 1.00 83.39  ? 82  ILE A N   1 
ATOM   701  C CA  . ILE A 1 102 ? 7.502  -3.525  114.225 1.00 81.78  ? 82  ILE A CA  1 
ATOM   702  C C   . ILE A 1 102 ? 6.881  -4.860  114.480 1.00 87.94  ? 82  ILE A C   1 
ATOM   703  O O   . ILE A 1 102 ? 7.276  -5.559  115.401 1.00 87.92  ? 82  ILE A O   1 
ATOM   704  C CB  . ILE A 1 102 ? 8.407  -3.683  113.024 1.00 83.79  ? 82  ILE A CB  1 
ATOM   705  C CG1 . ILE A 1 102 ? 9.521  -4.679  113.351 1.00 80.06  ? 82  ILE A CG1 1 
ATOM   706  C CG2 . ILE A 1 102 ? 8.988  -2.337  112.631 1.00 84.14  ? 82  ILE A CG2 1 
ATOM   707  C CD1 . ILE A 1 102 ? 10.348 -5.035  112.145 1.00 79.72  ? 82  ILE A CD1 1 
ATOM   708  N N   . VAL A 1 103 ? 5.919  -5.208  113.633 1.00 100.43 ? 83  VAL A N   1 
ATOM   709  C CA  . VAL A 1 103 ? 5.422  -6.585  113.530 1.00 92.73  ? 83  VAL A CA  1 
ATOM   710  C C   . VAL A 1 103 ? 5.335  -7.051  112.073 1.00 96.66  ? 83  VAL A C   1 
ATOM   711  O O   . VAL A 1 103 ? 5.282  -6.236  111.121 1.00 86.92  ? 83  VAL A O   1 
ATOM   712  C CB  . VAL A 1 103 ? 4.048  -6.766  114.186 1.00 77.87  ? 83  VAL A CB  1 
ATOM   713  C CG1 . VAL A 1 103 ? 4.145  -6.519  115.685 1.00 72.54  ? 83  VAL A CG1 1 
ATOM   714  C CG2 . VAL A 1 103 ? 3.016  -5.878  113.500 1.00 76.20  ? 83  VAL A CG2 1 
ATOM   715  N N   . ARG A 1 104 ? 5.349  -8.381  111.931 1.00 109.01 ? 84  ARG A N   1 
ATOM   716  C CA  . ARG A 1 104 ? 5.134  -9.057  110.657 1.00 104.74 ? 84  ARG A CA  1 
ATOM   717  C C   . ARG A 1 104 ? 3.665  -9.423  110.549 1.00 106.49 ? 84  ARG A C   1 
ATOM   718  O O   . ARG A 1 104 ? 3.102  -10.068 111.439 1.00 100.66 ? 84  ARG A O   1 
ATOM   719  C CB  . ARG A 1 104 ? 5.964  -10.336 110.573 1.00 102.75 ? 84  ARG A CB  1 
ATOM   720  C CG  . ARG A 1 104 ? 7.454  -10.150 110.805 1.00 104.18 ? 84  ARG A CG  1 
ATOM   721  C CD  . ARG A 1 104 ? 8.224  -11.454 110.619 1.00 107.86 ? 84  ARG A CD  1 
ATOM   722  N NE  . ARG A 1 104 ? 9.545  -11.244 110.012 1.00 102.28 ? 84  ARG A NE  1 
ATOM   723  C CZ  . ARG A 1 104 ? 10.687 -11.073 110.685 1.00 99.84  ? 84  ARG A CZ  1 
ATOM   724  N NH1 . ARG A 1 104 ? 10.728 -11.110 112.032 1.00 88.40  ? 84  ARG A NH1 1 
ATOM   725  N NH2 . ARG A 1 104 ? 11.813 -10.889 109.994 1.00 91.60  ? 84  ARG A NH2 1 
ATOM   726  N N   . LYS A 1 105 ? 3.024  -8.951  109.493 1.00 111.10 ? 85  LYS A N   1 
ATOM   727  C CA  . LYS A 1 105 ? 1.790  -9.561  109.046 1.00 124.50 ? 85  LYS A CA  1 
ATOM   728  C C   . LYS A 1 105 ? 2.190  -10.269 107.766 1.00 133.14 ? 85  LYS A C   1 
ATOM   729  O O   . LYS A 1 105 ? 3.172  -9.888  107.101 1.00 114.48 ? 85  LYS A O   1 
ATOM   730  C CB  . LYS A 1 105 ? 0.667  -8.545  108.814 1.00 133.23 ? 85  LYS A CB  1 
ATOM   731  C CG  . LYS A 1 105 ? -0.540 -8.692  109.745 1.00 132.37 ? 85  LYS A CG  1 
ATOM   732  C CD  . LYS A 1 105 ? -1.566 -7.569  109.514 1.00 142.17 ? 85  LYS A CD  1 
ATOM   733  C CE  . LYS A 1 105 ? -2.320 -7.658  108.180 1.00 129.37 ? 85  LYS A CE  1 
ATOM   734  N NZ  . LYS A 1 105 ? -3.678 -8.265  108.310 1.00 120.92 ? 85  LYS A NZ  1 
ATOM   735  N N   . VAL A 1 106 ? 1.427  -11.308 107.443 1.00 130.66 ? 86  VAL A N   1 
ATOM   736  C CA  . VAL A 1 106 ? 1.768  -12.223 106.371 1.00 108.78 ? 86  VAL A CA  1 
ATOM   737  C C   . VAL A 1 106 ? 1.036  -11.688 105.155 1.00 101.10 ? 86  VAL A C   1 
ATOM   738  O O   . VAL A 1 106 ? -0.143 -11.431 105.242 1.00 93.58  ? 86  VAL A O   1 
ATOM   739  C CB  . VAL A 1 106 ? 1.336  -13.647 106.741 1.00 103.38 ? 86  VAL A CB  1 
ATOM   740  C CG1 . VAL A 1 106 ? 2.207  -14.656 106.009 1.00 108.31 ? 86  VAL A CG1 1 
ATOM   741  C CG2 . VAL A 1 106 ? 1.418  -13.858 108.261 1.00 99.09  ? 86  VAL A CG2 1 
ATOM   742  N N   . ASP A 1 107 ? 1.736  -11.463 104.045 1.00 109.06 ? 87  ASP A N   1 
ATOM   743  C CA  . ASP A 1 107 ? 1.168  -10.699 102.924 1.00 118.66 ? 87  ASP A CA  1 
ATOM   744  C C   . ASP A 1 107 ? -0.098 -11.356 102.372 1.00 135.04 ? 87  ASP A C   1 
ATOM   745  O O   . ASP A 1 107 ? -0.124 -12.564 102.107 1.00 144.98 ? 87  ASP A O   1 
ATOM   746  C CB  . ASP A 1 107 ? 2.196  -10.516 101.795 1.00 122.61 ? 87  ASP A CB  1 
ATOM   747  C CG  . ASP A 1 107 ? 1.929  -9.273  100.927 1.00 119.86 ? 87  ASP A CG  1 
ATOM   748  O OD1 . ASP A 1 107 ? 0.750  -8.883  100.742 1.00 109.52 ? 87  ASP A OD1 1 
ATOM   749  O OD2 . ASP A 1 107 ? 2.917  -8.685  100.429 1.00 110.30 ? 87  ASP A OD2 1 
ATOM   750  N N   . VAL A 1 108 ? -1.139 -10.542 102.197 1.00 150.55 ? 88  VAL A N   1 
ATOM   751  C CA  . VAL A 1 108 ? -2.438 -11.011 101.701 1.00 155.66 ? 88  VAL A CA  1 
ATOM   752  C C   . VAL A 1 108 ? -2.446 -11.260 100.166 1.00 163.71 ? 88  VAL A C   1 
ATOM   753  O O   . VAL A 1 108 ? -3.392 -11.856 99.645  1.00 151.13 ? 88  VAL A O   1 
ATOM   754  C CB  . VAL A 1 108 ? -3.573 -10.046 102.156 1.00 144.93 ? 88  VAL A CB  1 
ATOM   755  C CG1 . VAL A 1 108 ? -3.599 -8.767  101.312 1.00 139.67 ? 88  VAL A CG1 1 
ATOM   756  C CG2 . VAL A 1 108 ? -4.922 -10.758 102.167 1.00 135.24 ? 88  VAL A CG2 1 
ATOM   757  N N   . LYS A 1 109 ? -1.394 -10.817 99.459  1.00 169.19 ? 89  LYS A N   1 
ATOM   758  C CA  . LYS A 1 109 ? -1.178 -11.169 98.038  1.00 159.14 ? 89  LYS A CA  1 
ATOM   759  C C   . LYS A 1 109 ? -0.958 -12.687 97.932  1.00 168.40 ? 89  LYS A C   1 
ATOM   760  O O   . LYS A 1 109 ? -1.528 -13.335 97.054  1.00 178.92 ? 89  LYS A O   1 
ATOM   761  C CB  . LYS A 1 109 ? 0.011  -10.390 97.427  1.00 147.96 ? 89  LYS A CB  1 
ATOM   762  C CG  . LYS A 1 109 ? -0.265 -9.759  96.059  1.00 141.57 ? 89  LYS A CG  1 
ATOM   763  C CD  . LYS A 1 109 ? 0.010  -10.709 94.890  1.00 140.53 ? 89  LYS A CD  1 
ATOM   764  C CE  . LYS A 1 109 ? -0.706 -10.280 93.607  1.00 130.34 ? 89  LYS A CE  1 
ATOM   765  N NZ  . LYS A 1 109 ? -2.122 -10.748 93.563  1.00 122.75 ? 89  LYS A NZ  1 
ATOM   766  N N   . ASP A 1 110 ? -0.117 -13.219 98.826  1.00 165.71 ? 90  ASP A N   1 
ATOM   767  C CA  . ASP A 1 110 ? -0.017 -14.667 99.162  1.00 157.08 ? 90  ASP A CA  1 
ATOM   768  C C   . ASP A 1 110 ? 1.185  -14.838 100.087 1.00 147.60 ? 90  ASP A C   1 
ATOM   769  O O   . ASP A 1 110 ? 1.964  -13.904 100.236 1.00 142.87 ? 90  ASP A O   1 
ATOM   770  C CB  . ASP A 1 110 ? 0.138  -15.579 97.920  1.00 151.39 ? 90  ASP A CB  1 
ATOM   771  C CG  . ASP A 1 110 ? -1.176 -16.296 97.509  1.00 139.24 ? 90  ASP A CG  1 
ATOM   772  O OD1 . ASP A 1 110 ? -2.200 -16.202 98.219  1.00 120.55 ? 90  ASP A OD1 1 
ATOM   773  O OD2 . ASP A 1 110 ? -1.178 -16.973 96.457  1.00 124.59 ? 90  ASP A OD2 1 
ATOM   774  N N   . ARG A 1 111 ? 1.335  -16.014 100.701 1.00 149.14 ? 91  ARG A N   1 
ATOM   775  C CA  . ARG A 1 111 ? 2.541  -16.338 101.501 1.00 155.69 ? 91  ARG A CA  1 
ATOM   776  C C   . ARG A 1 111 ? 3.772  -16.502 100.580 1.00 167.55 ? 91  ARG A C   1 
ATOM   777  O O   . ARG A 1 111 ? 3.668  -16.307 99.355  1.00 162.72 ? 91  ARG A O   1 
ATOM   778  C CB  . ARG A 1 111 ? 2.309  -17.583 102.383 1.00 150.38 ? 91  ARG A CB  1 
ATOM   779  C CG  . ARG A 1 111 ? 3.179  -17.697 103.646 1.00 139.55 ? 91  ARG A CG  1 
ATOM   780  C CD  . ARG A 1 111 ? 2.409  -18.245 104.851 1.00 139.84 ? 91  ARG A CD  1 
ATOM   781  N NE  . ARG A 1 111 ? 2.521  -19.702 105.059 1.00 137.91 ? 91  ARG A NE  1 
ATOM   782  C CZ  . ARG A 1 111 ? 1.859  -20.658 104.385 1.00 129.71 ? 91  ARG A CZ  1 
ATOM   783  N NH1 . ARG A 1 111 ? 1.018  -20.367 103.395 1.00 135.04 ? 91  ARG A NH1 1 
ATOM   784  N NH2 . ARG A 1 111 ? 2.048  -21.938 104.694 1.00 110.52 ? 91  ARG A NH2 1 
ATOM   785  N N   . ARG A 1 112 ? 4.922  -16.860 101.167 1.00 171.59 ? 92  ARG A N   1 
ATOM   786  C CA  . ARG A 1 112 ? 6.241  -16.632 100.555 1.00 167.81 ? 92  ARG A CA  1 
ATOM   787  C C   . ARG A 1 112 ? 6.444  -15.112 100.342 1.00 168.80 ? 92  ARG A C   1 
ATOM   788  O O   . ARG A 1 112 ? 7.026  -14.680 99.342  1.00 172.75 ? 92  ARG A O   1 
ATOM   789  C CB  . ARG A 1 112 ? 6.421  -17.418 99.236  1.00 157.33 ? 92  ARG A CB  1 
ATOM   790  C CG  . ARG A 1 112 ? 6.360  -18.937 99.368  1.00 147.35 ? 92  ARG A CG  1 
ATOM   791  C CD  . ARG A 1 112 ? 7.141  -19.633 98.252  1.00 142.26 ? 92  ARG A CD  1 
ATOM   792  N NE  . ARG A 1 112 ? 8.600  -19.502 98.415  1.00 143.26 ? 92  ARG A NE  1 
ATOM   793  C CZ  . ARG A 1 112 ? 9.408  -18.668 97.739  1.00 130.86 ? 92  ARG A CZ  1 
ATOM   794  N NH1 . ARG A 1 112 ? 8.950  -17.840 96.800  1.00 123.98 ? 92  ARG A NH1 1 
ATOM   795  N NH2 . ARG A 1 112 ? 10.711 -18.665 98.008  1.00 111.33 ? 92  ARG A NH2 1 
ATOM   796  N N   . LYS A 1 113 ? 5.972  -14.319 101.310 1.00 148.52 ? 93  LYS A N   1 
ATOM   797  C CA  . LYS A 1 113 ? 5.805  -12.863 101.160 1.00 126.40 ? 93  LYS A CA  1 
ATOM   798  C C   . LYS A 1 113 ? 5.334  -12.289 102.504 1.00 119.48 ? 93  LYS A C   1 
ATOM   799  O O   . LYS A 1 113 ? 4.245  -12.633 102.968 1.00 106.80 ? 93  LYS A O   1 
ATOM   800  C CB  . LYS A 1 113 ? 4.761  -12.548 100.060 1.00 117.78 ? 93  LYS A CB  1 
ATOM   801  C CG  . LYS A 1 113 ? 5.290  -12.076 98.710  1.00 117.05 ? 93  LYS A CG  1 
ATOM   802  C CD  . LYS A 1 113 ? 5.068  -10.584 98.460  1.00 121.46 ? 93  LYS A CD  1 
ATOM   803  C CE  . LYS A 1 113 ? 5.638  -9.669  99.554  1.00 132.32 ? 93  LYS A CE  1 
ATOM   804  N NZ  . LYS A 1 113 ? 7.108  -9.761  99.843  1.00 128.50 ? 93  LYS A NZ  1 
ATOM   805  N N   . PHE A 1 114 ? 6.142  -11.434 103.137 1.00 112.50 ? 94  PHE A N   1 
ATOM   806  C CA  . PHE A 1 114 ? 5.732  -10.791 104.394 1.00 111.26 ? 94  PHE A CA  1 
ATOM   807  C C   . PHE A 1 114 ? 5.522  -9.264  104.222 1.00 109.45 ? 94  PHE A C   1 
ATOM   808  O O   . PHE A 1 114 ? 6.072  -8.658  103.297 1.00 98.45  ? 94  PHE A O   1 
ATOM   809  C CB  . PHE A 1 114 ? 6.744  -11.086 105.499 1.00 109.48 ? 94  PHE A CB  1 
ATOM   810  C CG  . PHE A 1 114 ? 6.818  -12.543 105.912 1.00 119.04 ? 94  PHE A CG  1 
ATOM   811  C CD1 . PHE A 1 114 ? 7.186  -13.536 105.001 1.00 122.01 ? 94  PHE A CD1 1 
ATOM   812  C CD2 . PHE A 1 114 ? 6.578  -12.914 107.238 1.00 119.46 ? 94  PHE A CD2 1 
ATOM   813  C CE1 . PHE A 1 114 ? 7.285  -14.861 105.395 1.00 124.06 ? 94  PHE A CE1 1 
ATOM   814  C CE2 . PHE A 1 114 ? 6.677  -14.236 107.637 1.00 114.53 ? 94  PHE A CE2 1 
ATOM   815  C CZ  . PHE A 1 114 ? 7.032  -15.210 106.714 1.00 129.48 ? 94  PHE A CZ  1 
ATOM   816  N N   . GLN A 1 115 ? 4.696  -8.664  105.095 1.00 106.80 ? 95  GLN A N   1 
ATOM   817  C CA  . GLN A 1 115 ? 4.419  -7.199  105.103 1.00 98.01  ? 95  GLN A CA  1 
ATOM   818  C C   . GLN A 1 115 ? 4.839  -6.627  106.451 1.00 96.29  ? 95  GLN A C   1 
ATOM   819  O O   . GLN A 1 115 ? 4.425  -7.183  107.493 1.00 79.35  ? 95  GLN A O   1 
ATOM   820  C CB  . GLN A 1 115 ? 2.919  -6.904  104.903 1.00 89.76  ? 95  GLN A CB  1 
ATOM   821  C CG  . GLN A 1 115 ? 2.516  -6.278  103.560 1.00 85.60  ? 95  GLN A CG  1 
ATOM   822  C CD  . GLN A 1 115 ? 1.038  -5.853  103.523 1.00 80.95  ? 95  GLN A CD  1 
ATOM   823  O OE1 . GLN A 1 115 ? 0.703  -4.737  103.131 1.00 75.07  ? 95  GLN A OE1 1 
ATOM   824  N NE2 . GLN A 1 115 ? 0.156  -6.739  103.967 1.00 88.30  ? 95  GLN A NE2 1 
ATOM   825  N N   . ILE A 1 116 ? 5.629  -5.533  106.444 1.00 87.74  ? 96  ILE A N   1 
ATOM   826  C CA  . ILE A 1 116 ? 6.115  -4.927  107.717 1.00 87.97  ? 96  ILE A CA  1 
ATOM   827  C C   . ILE A 1 116 ? 5.306  -3.715  108.222 1.00 75.17  ? 96  ILE A C   1 
ATOM   828  O O   . ILE A 1 116 ? 5.103  -2.716  107.507 1.00 61.75  ? 96  ILE A O   1 
ATOM   829  C CB  . ILE A 1 116 ? 7.613  -4.560  107.687 1.00 88.36  ? 96  ILE A CB  1 
ATOM   830  C CG1 . ILE A 1 116 ? 8.457  -5.745  107.203 1.00 91.57  ? 96  ILE A CG1 1 
ATOM   831  C CG2 . ILE A 1 116 ? 8.074  -4.167  109.091 1.00 89.09  ? 96  ILE A CG2 1 
ATOM   832  C CD1 . ILE A 1 116 ? 8.446  -6.943  108.137 1.00 92.80  ? 96  ILE A CD1 1 
ATOM   833  N N   . PHE A 1 117 ? 4.856  -3.820  109.469 1.00 59.91  ? 97  PHE A N   1 
ATOM   834  C CA  . PHE A 1 117 ? 3.969  -2.816  110.030 1.00 69.07  ? 97  PHE A CA  1 
ATOM   835  C C   . PHE A 1 117 ? 4.549  -2.285  111.333 1.00 73.24  ? 97  PHE A C   1 
ATOM   836  O O   . PHE A 1 117 ? 5.181  -3.032  112.092 1.00 70.40  ? 97  PHE A O   1 
ATOM   837  C CB  . PHE A 1 117 ? 2.541  -3.381  110.234 1.00 71.41  ? 97  PHE A CB  1 
ATOM   838  C CG  . PHE A 1 117 ? 1.656  -3.236  109.014 1.00 70.39  ? 97  PHE A CG  1 
ATOM   839  C CD1 . PHE A 1 117 ? 1.106  -2.005  108.680 1.00 70.02  ? 97  PHE A CD1 1 
ATOM   840  C CD2 . PHE A 1 117 ? 1.392  -4.316  108.183 1.00 66.61  ? 97  PHE A CD2 1 
ATOM   841  C CE1 . PHE A 1 117 ? 0.315  -1.853  107.543 1.00 70.20  ? 97  PHE A CE1 1 
ATOM   842  C CE2 . PHE A 1 117 ? 0.603  -4.164  107.042 1.00 60.90  ? 97  PHE A CE2 1 
ATOM   843  C CZ  . PHE A 1 117 ? 0.064  -2.941  106.722 1.00 66.06  ? 97  PHE A CZ  1 
ATOM   844  N N   . LEU A 1 118 ? 4.346  -0.983  111.558 1.00 70.79  ? 98  LEU A N   1 
ATOM   845  C CA  . LEU A 1 118 ? 4.763  -0.334  112.793 1.00 66.76  ? 98  LEU A CA  1 
ATOM   846  C C   . LEU A 1 118 ? 3.874  -0.654  113.976 1.00 62.81  ? 98  LEU A C   1 
ATOM   847  O O   . LEU A 1 118 ? 2.641  -0.506  113.914 1.00 53.82  ? 98  LEU A O   1 
ATOM   848  C CB  . LEU A 1 118 ? 4.751  1.190   112.634 1.00 63.35  ? 98  LEU A CB  1 
ATOM   849  C CG  . LEU A 1 118 ? 5.867  1.747   111.777 1.00 60.93  ? 98  LEU A CG  1 
ATOM   850  C CD1 . LEU A 1 118 ? 5.478  3.138   111.343 1.00 55.95  ? 98  LEU A CD1 1 
ATOM   851  C CD2 . LEU A 1 118 ? 7.225  1.671   112.479 1.00 56.52  ? 98  LEU A CD2 1 
ATOM   852  N N   . THR A 1 119 ? 4.528  -0.955  115.092 1.00 63.59  ? 99  THR A N   1 
ATOM   853  C CA  . THR A 1 119 ? 3.868  -1.028  116.413 1.00 73.45  ? 99  THR A CA  1 
ATOM   854  C C   . THR A 1 119 ? 3.321  0.325   116.846 1.00 74.65  ? 99  THR A C   1 
ATOM   855  O O   . THR A 1 119 ? 3.360  1.276   116.088 1.00 87.04  ? 99  THR A O   1 
ATOM   856  C CB  . THR A 1 119 ? 4.872  -1.572  117.419 1.00 84.27  ? 99  THR A CB  1 
ATOM   857  O OG1 . THR A 1 119 ? 6.105  -0.868  117.291 1.00 75.69  ? 99  THR A OG1 1 
ATOM   858  C CG2 . THR A 1 119 ? 5.193  -3.036  117.081 1.00 87.59  ? 99  THR A CG2 1 
ATOM   859  N N   . ASP A 1 120 ? 2.735  0.435   118.022 1.00 90.16  ? 100 ASP A N   1 
ATOM   860  C CA  . ASP A 1 120 ? 2.052  1.702   118.373 1.00 81.04  ? 100 ASP A CA  1 
ATOM   861  C C   . ASP A 1 120 ? 3.106  2.687   118.830 1.00 85.13  ? 100 ASP A C   1 
ATOM   862  O O   . ASP A 1 120 ? 3.011  3.912   118.628 1.00 67.45  ? 100 ASP A O   1 
ATOM   863  C CB  . ASP A 1 120 ? 0.967  1.513   119.430 1.00 74.98  ? 100 ASP A CB  1 
ATOM   864  C CG  . ASP A 1 120 ? -0.419 1.519   118.815 1.00 80.44  ? 100 ASP A CG  1 
ATOM   865  O OD1 . ASP A 1 120 ? -0.541 1.064   117.656 1.00 138.34 ? 100 ASP A OD1 1 
ATOM   866  O OD2 . ASP A 1 120 ? -1.397 1.971   119.455 1.00 69.17  ? 100 ASP A OD2 1 
ATOM   867  N N   . LEU A 1 121 ? 4.133  2.117   119.431 1.00 75.73  ? 101 LEU A N   1 
ATOM   868  C CA  . LEU A 1 121 ? 5.340  2.820   119.670 1.00 69.48  ? 101 LEU A CA  1 
ATOM   869  C C   . LEU A 1 121 ? 5.907  3.369   118.351 1.00 69.71  ? 101 LEU A C   1 
ATOM   870  O O   . LEU A 1 121 ? 5.956  4.583   118.129 1.00 86.36  ? 101 LEU A O   1 
ATOM   871  C CB  . LEU A 1 121 ? 6.320  1.864   120.326 1.00 64.85  ? 101 LEU A CB  1 
ATOM   872  C CG  . LEU A 1 121 ? 7.407  2.555   121.121 1.00 89.47  ? 101 LEU A CG  1 
ATOM   873  C CD1 . LEU A 1 121 ? 6.815  3.451   122.243 1.00 81.09  ? 101 LEU A CD1 1 
ATOM   874  C CD2 . LEU A 1 121 ? 8.401  1.473   121.598 1.00 84.30  ? 101 LEU A CD2 1 
ATOM   875  N N   . GLY A 1 122 ? 6.311  2.481   117.460 1.00 66.56  ? 102 GLY A N   1 
ATOM   876  C CA  . GLY A 1 122 ? 7.074  2.865   116.285 1.00 59.45  ? 102 GLY A CA  1 
ATOM   877  C C   . GLY A 1 122 ? 6.483  4.070   115.566 1.00 58.70  ? 102 GLY A C   1 
ATOM   878  O O   . GLY A 1 122 ? 7.222  4.810   114.977 1.00 63.45  ? 102 GLY A O   1 
ATOM   879  N N   . ARG A 1 123 ? 5.166  4.247   115.579 1.00 50.86  ? 103 ARG A N   1 
ATOM   880  C CA  . ARG A 1 123 ? 4.542  5.424   114.984 1.00 59.97  ? 103 ARG A CA  1 
ATOM   881  C C   . ARG A 1 123 ? 4.786  6.689   115.814 1.00 71.40  ? 103 ARG A C   1 
ATOM   882  O O   . ARG A 1 123 ? 5.006  7.769   115.261 1.00 67.92  ? 103 ARG A O   1 
ATOM   883  C CB  . ARG A 1 123 ? 3.018  5.257   114.746 1.00 55.13  ? 103 ARG A CB  1 
ATOM   884  C CG  . ARG A 1 123 ? 2.701  4.816   113.325 1.00 68.76  ? 103 ARG A CG  1 
ATOM   885  C CD  . ARG A 1 123 ? 1.237  4.850   112.940 1.00 77.89  ? 103 ARG A CD  1 
ATOM   886  N NE  . ARG A 1 123 ? 0.385  4.647   114.103 1.00 87.48  ? 103 ARG A NE  1 
ATOM   887  C CZ  . ARG A 1 123 ? 0.206  3.481   114.716 1.00 86.58  ? 103 ARG A CZ  1 
ATOM   888  N NH1 . ARG A 1 123 ? 0.809  2.369   114.285 1.00 88.46  ? 103 ARG A NH1 1 
ATOM   889  N NH2 . ARG A 1 123 ? -0.569 3.443   115.787 1.00 84.27  ? 103 ARG A NH2 1 
ATOM   890  N N   . GLU A 1 124 ? 4.686  6.553   117.130 1.00 77.54  ? 104 GLU A N   1 
ATOM   891  C CA  . GLU A 1 124 ? 4.875  7.677   118.037 1.00 78.65  ? 104 GLU A CA  1 
ATOM   892  C C   . GLU A 1 124 ? 6.337  8.137   118.080 1.00 71.52  ? 104 GLU A C   1 
ATOM   893  O O   . GLU A 1 124 ? 6.575  9.322   118.180 1.00 68.27  ? 104 GLU A O   1 
ATOM   894  C CB  . GLU A 1 124 ? 4.351  7.342   119.441 1.00 76.25  ? 104 GLU A CB  1 
ATOM   895  C CG  . GLU A 1 124 ? 2.843  7.484   119.515 1.00 76.33  ? 104 GLU A CG  1 
ATOM   896  C CD  . GLU A 1 124 ? 2.210  6.722   120.669 1.00 90.36  ? 104 GLU A CD  1 
ATOM   897  O OE1 . GLU A 1 124 ? 2.935  6.294   121.626 1.00 78.48  ? 104 GLU A OE1 1 
ATOM   898  O OE2 . GLU A 1 124 ? 0.962  6.549   120.593 1.00 88.39  ? 104 GLU A OE2 1 
ATOM   899  N N   . LEU A 1 125 ? 7.279  7.204   117.962 1.00 60.47  ? 105 LEU A N   1 
ATOM   900  C CA  . LEU A 1 125 ? 8.718  7.500   117.867 1.00 57.44  ? 105 LEU A CA  1 
ATOM   901  C C   . LEU A 1 125 ? 9.249  8.382   116.680 1.00 62.02  ? 105 LEU A C   1 
ATOM   902  O O   . LEU A 1 125 ? 10.432 8.779   116.665 1.00 66.78  ? 105 LEU A O   1 
ATOM   903  C CB  . LEU A 1 125 ? 9.477  6.172   117.805 1.00 58.25  ? 105 LEU A CB  1 
ATOM   904  C CG  . LEU A 1 125 ? 10.347 5.951   119.014 1.00 68.46  ? 105 LEU A CG  1 
ATOM   905  C CD1 . LEU A 1 125 ? 9.477  6.142   120.269 1.00 59.95  ? 105 LEU A CD1 1 
ATOM   906  C CD2 . LEU A 1 125 ? 11.116 4.613   118.954 1.00 68.02  ? 105 LEU A CD2 1 
ATOM   907  N N   . GLU A 1 126 ? 8.410  8.671   115.692 1.00 54.12  ? 106 GLU A N   1 
ATOM   908  C CA  . GLU A 1 126 ? 8.857  9.374   114.519 1.00 50.86  ? 106 GLU A CA  1 
ATOM   909  C C   . GLU A 1 126 ? 9.376  10.798  114.873 1.00 50.48  ? 106 GLU A C   1 
ATOM   910  O O   . GLU A 1 126 ? 10.558 11.058  114.702 1.00 47.02  ? 106 GLU A O   1 
ATOM   911  C CB  . GLU A 1 126 ? 7.725  9.440   113.476 1.00 51.37  ? 106 GLU A CB  1 
ATOM   912  C CG  . GLU A 1 126 ? 8.225  9.929   112.130 1.00 47.89  ? 106 GLU A CG  1 
ATOM   913  C CD  . GLU A 1 126 ? 7.181  10.194  111.106 1.00 47.45  ? 106 GLU A CD  1 
ATOM   914  O OE1 . GLU A 1 126 ? 5.948  10.045  111.351 1.00 51.78  ? 106 GLU A OE1 1 
ATOM   915  O OE2 . GLU A 1 126 ? 7.639  10.628  110.044 1.00 43.80  ? 106 GLU A OE2 1 
ATOM   916  N N   . GLU A 1 127 ? 8.484  11.663  115.379 1.00 51.45  ? 107 GLU A N   1 
ATOM   917  C CA  . GLU A 1 127 ? 8.779  13.039  115.847 1.00 57.06  ? 107 GLU A CA  1 
ATOM   918  C C   . GLU A 1 127 ? 9.952  13.105  116.801 1.00 51.61  ? 107 GLU A C   1 
ATOM   919  O O   . GLU A 1 127 ? 10.976 13.689  116.470 1.00 58.37  ? 107 GLU A O   1 
ATOM   920  C CB  . GLU A 1 127 ? 7.510  13.662  116.447 1.00 70.49  ? 107 GLU A CB  1 
ATOM   921  C CG  . GLU A 1 127 ? 7.554  15.140  116.829 1.00 88.26  ? 107 GLU A CG  1 
ATOM   922  C CD  . GLU A 1 127 ? 6.174  15.815  116.673 1.00 101.00 ? 107 GLU A CD  1 
ATOM   923  O OE1 . GLU A 1 127 ? 5.852  16.749  117.464 1.00 99.31  ? 107 GLU A OE1 1 
ATOM   924  O OE2 . GLU A 1 127 ? 5.407  15.405  115.748 1.00 92.90  ? 107 GLU A OE2 1 
ATOM   925  N N   . PRO A 1 128 ? 9.883  12.410  117.936 1.00 58.24  ? 108 PRO A N   1 
ATOM   926  C CA  . PRO A 1 128 ? 11.068 12.472  118.817 1.00 56.80  ? 108 PRO A CA  1 
ATOM   927  C C   . PRO A 1 128 ? 12.340 12.110  118.181 1.00 43.75  ? 108 PRO A C   1 
ATOM   928  O O   . PRO A 1 128 ? 13.273 12.779  118.393 1.00 65.85  ? 108 PRO A O   1 
ATOM   929  C CB  . PRO A 1 128 ? 10.786 11.452  119.902 1.00 55.90  ? 108 PRO A CB  1 
ATOM   930  C CG  . PRO A 1 128 ? 9.302  11.334  119.902 1.00 58.38  ? 108 PRO A CG  1 
ATOM   931  C CD  . PRO A 1 128 ? 8.817  11.584  118.512 1.00 53.15  ? 108 PRO A CD  1 
ATOM   932  N N   . LEU A 1 129 ? 12.423 11.040  117.417 1.00 59.92  ? 109 LEU A N   1 
ATOM   933  C CA  . LEU A 1 129 ? 13.749 10.555  116.920 1.00 50.97  ? 109 LEU A CA  1 
ATOM   934  C C   . LEU A 1 129 ? 14.241 11.391  115.747 1.00 48.46  ? 109 LEU A C   1 
ATOM   935  O O   . LEU A 1 129 ? 15.445 11.577  115.542 1.00 44.23  ? 109 LEU A O   1 
ATOM   936  C CB  . LEU A 1 129 ? 13.643 9.097   116.487 1.00 55.21  ? 109 LEU A CB  1 
ATOM   937  C CG  . LEU A 1 129 ? 13.204 8.095   117.569 1.00 69.71  ? 109 LEU A CG  1 
ATOM   938  C CD1 . LEU A 1 129 ? 13.010 6.724   116.961 1.00 76.87  ? 109 LEU A CD1 1 
ATOM   939  C CD2 . LEU A 1 129 ? 14.220 7.983   118.697 1.00 68.94  ? 109 LEU A CD2 1 
ATOM   940  N N   . ASN A 1 130 ? 13.291 11.853  114.941 1.00 40.00  ? 110 ASN A N   1 
ATOM   941  C CA  . ASN A 1 130 ? 13.612 12.762  113.900 1.00 44.63  ? 110 ASN A CA  1 
ATOM   942  C C   . ASN A 1 130 ? 14.179 14.049  114.533 1.00 50.39  ? 110 ASN A C   1 
ATOM   943  O O   . ASN A 1 130 ? 15.249 14.464  114.157 1.00 54.09  ? 110 ASN A O   1 
ATOM   944  C CB  . ASN A 1 130 ? 12.372 13.040  113.054 1.00 45.10  ? 110 ASN A CB  1 
ATOM   945  C CG  . ASN A 1 130 ? 12.120 11.965  112.014 1.00 45.00  ? 110 ASN A CG  1 
ATOM   946  O OD1 . ASN A 1 130 ? 13.003 11.185  111.643 1.00 49.28  ? 110 ASN A OD1 1 
ATOM   947  N ND2 . ASN A 1 130 ? 10.930 11.961  111.496 1.00 42.70  ? 110 ASN A ND2 1 
ATOM   948  N N   . GLU A 1 131 ? 13.512 14.656  115.511 1.00 46.75  ? 111 GLU A N   1 
ATOM   949  C CA  . GLU A 1 131 ? 14.136 15.797  116.167 1.00 56.07  ? 111 GLU A CA  1 
ATOM   950  C C   . GLU A 1 131 ? 15.571 15.512  116.556 1.00 47.88  ? 111 GLU A C   1 
ATOM   951  O O   . GLU A 1 131 ? 16.489 16.265  116.184 1.00 44.87  ? 111 GLU A O   1 
ATOM   952  C CB  . GLU A 1 131 ? 13.439 16.240  117.430 1.00 57.20  ? 111 GLU A CB  1 
ATOM   953  C CG  . GLU A 1 131 ? 12.198 17.053  117.252 1.00 66.68  ? 111 GLU A CG  1 
ATOM   954  C CD  . GLU A 1 131 ? 11.447 17.121  118.574 1.00 79.59  ? 111 GLU A CD  1 
ATOM   955  O OE1 . GLU A 1 131 ? 11.863 17.974  119.443 1.00 56.99  ? 111 GLU A OE1 1 
ATOM   956  O OE2 . GLU A 1 131 ? 10.482 16.277  118.714 1.00 74.84  ? 111 GLU A OE2 1 
ATOM   957  N N   . ILE A 1 132 ? 15.804 14.451  117.303 1.00 43.25  ? 112 ILE A N   1 
ATOM   958  C CA  . ILE A 1 132 ? 17.233 14.195  117.669 1.00 42.59  ? 112 ILE A CA  1 
ATOM   959  C C   . ILE A 1 132 ? 18.165 14.106  116.501 1.00 39.85  ? 112 ILE A C   1 
ATOM   960  O O   . ILE A 1 132 ? 19.203 14.680  116.502 1.00 53.28  ? 112 ILE A O   1 
ATOM   961  C CB  . ILE A 1 132 ? 17.359 12.950  118.510 1.00 39.32  ? 112 ILE A CB  1 
ATOM   962  C CG1 . ILE A 1 132 ? 16.825 13.278  119.916 1.00 46.76  ? 112 ILE A CG1 1 
ATOM   963  C CG2 . ILE A 1 132 ? 18.783 12.484  118.511 1.00 33.72  ? 112 ILE A CG2 1 
ATOM   964  C CD1 . ILE A 1 132 ? 15.684 12.455  120.521 1.00 44.27  ? 112 ILE A CD1 1 
ATOM   965  N N   . ALA A 1 133 ? 17.751 13.417  115.453 1.00 49.47  ? 113 ALA A N   1 
ATOM   966  C CA  . ALA A 1 133 ? 18.635 13.062  114.342 1.00 48.31  ? 113 ALA A CA  1 
ATOM   967  C C   . ALA A 1 133 ? 19.001 14.244  113.545 1.00 38.90  ? 113 ALA A C   1 
ATOM   968  O O   . ALA A 1 133 ? 20.098 14.372  113.007 1.00 36.95  ? 113 ALA A O   1 
ATOM   969  C CB  . ALA A 1 133 ? 17.902 12.092  113.425 1.00 54.41  ? 113 ALA A CB  1 
ATOM   970  N N   . SER A 1 134 ? 18.006 15.080  113.416 1.00 35.56  ? 114 SER A N   1 
ATOM   971  C CA  . SER A 1 134 ? 18.120 16.329  112.719 1.00 38.18  ? 114 SER A CA  1 
ATOM   972  C C   . SER A 1 134 ? 19.035 17.335  113.414 1.00 40.51  ? 114 SER A C   1 
ATOM   973  O O   . SER A 1 134 ? 19.819 18.036  112.754 1.00 38.66  ? 114 SER A O   1 
ATOM   974  C CB  . SER A 1 134 ? 16.750 16.947  112.624 1.00 39.17  ? 114 SER A CB  1 
ATOM   975  O OG  . SER A 1 134 ? 16.910 18.165  111.960 1.00 46.53  ? 114 SER A OG  1 
ATOM   976  N N   . ILE A 1 135 ? 18.955 17.422  114.741 1.00 40.58  ? 115 ILE A N   1 
ATOM   977  C CA  . ILE A 1 135 ? 19.903 18.280  115.383 1.00 44.41  ? 115 ILE A CA  1 
ATOM   978  C C   . ILE A 1 135 ? 21.303 17.630  115.259 1.00 41.91  ? 115 ILE A C   1 
ATOM   979  O O   . ILE A 1 135 ? 22.281 18.306  114.999 1.00 45.02  ? 115 ILE A O   1 
ATOM   980  C CB  . ILE A 1 135 ? 19.566 18.792  116.822 1.00 40.99  ? 115 ILE A CB  1 
ATOM   981  C CG1 . ILE A 1 135 ? 20.364 18.058  117.813 1.00 49.10  ? 115 ILE A CG1 1 
ATOM   982  C CG2 . ILE A 1 135 ? 18.074 18.938  117.193 1.00 39.17  ? 115 ILE A CG2 1 
ATOM   983  C CD1 . ILE A 1 135 ? 19.966 18.470  119.197 1.00 65.54  ? 115 ILE A CD1 1 
ATOM   984  N N   . TYR A 1 136 ? 21.409 16.321  115.399 1.00 42.92  ? 116 TYR A N   1 
ATOM   985  C CA  . TYR A 1 136 ? 22.708 15.679  115.136 1.00 43.24  ? 116 TYR A CA  1 
ATOM   986  C C   . TYR A 1 136 ? 23.208 15.846  113.688 1.00 44.41  ? 116 TYR A C   1 
ATOM   987  O O   . TYR A 1 136 ? 24.406 16.097  113.487 1.00 46.46  ? 116 TYR A O   1 
ATOM   988  C CB  . TYR A 1 136 ? 22.651 14.230  115.547 1.00 47.95  ? 116 TYR A CB  1 
ATOM   989  C CG  . TYR A 1 136 ? 22.825 13.958  117.071 1.00 54.71  ? 116 TYR A CG  1 
ATOM   990  C CD1 . TYR A 1 136 ? 21.806 14.166  117.985 1.00 57.58  ? 116 TYR A CD1 1 
ATOM   991  C CD2 . TYR A 1 136 ? 24.022 13.461  117.568 1.00 49.21  ? 116 TYR A CD2 1 
ATOM   992  C CE1 . TYR A 1 136 ? 22.002 13.859  119.327 1.00 57.31  ? 116 TYR A CE1 1 
ATOM   993  C CE2 . TYR A 1 136 ? 24.221 13.151  118.867 1.00 43.14  ? 116 TYR A CE2 1 
ATOM   994  C CZ  . TYR A 1 136 ? 23.234 13.348  119.740 1.00 55.19  ? 116 TYR A CZ  1 
ATOM   995  O OH  . TYR A 1 136 ? 23.507 13.030  121.035 1.00 69.31  ? 116 TYR A OH  1 
ATOM   996  N N   . ALA A 1 137 ? 22.320 15.813  112.679 1.00 42.52  ? 117 ALA A N   1 
ATOM   997  C CA  . ALA A 1 137 ? 22.757 16.007  111.275 1.00 42.19  ? 117 ALA A CA  1 
ATOM   998  C C   . ALA A 1 137 ? 23.261 17.437  111.010 1.00 47.79  ? 117 ALA A C   1 
ATOM   999  O O   . ALA A 1 137 ? 24.239 17.698  110.250 1.00 44.69  ? 117 ALA A O   1 
ATOM   1000 C CB  . ALA A 1 137 ? 21.628 15.697  110.345 1.00 44.41  ? 117 ALA A CB  1 
ATOM   1001 N N   . THR A 1 138 ? 22.594 18.366  111.664 1.00 44.28  ? 118 THR A N   1 
ATOM   1002 C CA  . THR A 1 138 ? 22.963 19.766  111.601 1.00 42.57  ? 118 THR A CA  1 
ATOM   1003 C C   . THR A 1 138 ? 24.336 19.995  112.189 1.00 43.06  ? 118 THR A C   1 
ATOM   1004 O O   . THR A 1 138 ? 25.099 20.761  111.639 1.00 44.03  ? 118 THR A O   1 
ATOM   1005 C CB  . THR A 1 138 ? 21.863 20.618  112.305 1.00 47.36  ? 118 THR A CB  1 
ATOM   1006 O OG1 . THR A 1 138 ? 20.823 20.826  111.360 1.00 49.72  ? 118 THR A OG1 1 
ATOM   1007 C CG2 . THR A 1 138 ? 22.322 21.960  112.736 1.00 51.92  ? 118 THR A CG2 1 
ATOM   1008 N N   . GLU A 1 139 ? 24.649 19.384  113.326 1.00 41.83  ? 119 GLU A N   1 
ATOM   1009 C CA  . GLU A 1 139 ? 26.010 19.507  113.853 1.00 49.07  ? 119 GLU A CA  1 
ATOM   1010 C C   . GLU A 1 139 ? 26.965 18.961  112.791 1.00 43.14  ? 119 GLU A C   1 
ATOM   1011 O O   . GLU A 1 139 ? 27.875 19.668  112.367 1.00 43.49  ? 119 GLU A O   1 
ATOM   1012 C CB  . GLU A 1 139 ? 26.250 18.753  115.191 1.00 52.58  ? 119 GLU A CB  1 
ATOM   1013 C CG  . GLU A 1 139 ? 26.203 19.607  116.438 1.00 64.28  ? 119 GLU A CG  1 
ATOM   1014 C CD  . GLU A 1 139 ? 27.483 20.439  116.648 1.00 78.67  ? 119 GLU A CD  1 
ATOM   1015 O OE1 . GLU A 1 139 ? 28.624 19.878  116.549 1.00 69.74  ? 119 GLU A OE1 1 
ATOM   1016 O OE2 . GLU A 1 139 ? 27.351 21.665  116.942 1.00 83.68  ? 119 GLU A OE2 1 
ATOM   1017 N N   . THR A 1 140 ? 26.701 17.731  112.351 1.00 41.49  ? 120 THR A N   1 
ATOM   1018 C CA  . THR A 1 140 ? 27.623 16.930  111.544 1.00 42.83  ? 120 THR A CA  1 
ATOM   1019 C C   . THR A 1 140 ? 28.019 17.664  110.280 1.00 41.95  ? 120 THR A C   1 
ATOM   1020 O O   . THR A 1 140 ? 29.197 17.659  109.864 1.00 40.91  ? 120 THR A O   1 
ATOM   1021 C CB  . THR A 1 140 ? 26.907 15.590  111.221 1.00 46.26  ? 120 THR A CB  1 
ATOM   1022 O OG1 . THR A 1 140 ? 26.631 14.921  112.458 1.00 39.76  ? 120 THR A OG1 1 
ATOM   1023 C CG2 . THR A 1 140 ? 27.722 14.688  110.321 1.00 40.31  ? 120 THR A CG2 1 
ATOM   1024 N N   . PHE A 1 141 ? 27.044 18.371  109.703 1.00 39.24  ? 121 PHE A N   1 
ATOM   1025 C CA  . PHE A 1 141 ? 27.273 19.086  108.475 1.00 36.39  ? 121 PHE A CA  1 
ATOM   1026 C C   . PHE A 1 141 ? 27.456 20.575  108.670 1.00 37.87  ? 121 PHE A C   1 
ATOM   1027 O O   . PHE A 1 141 ? 27.529 21.304  107.702 1.00 38.94  ? 121 PHE A O   1 
ATOM   1028 C CB  . PHE A 1 141 ? 26.160 18.739  107.458 1.00 41.35  ? 121 PHE A CB  1 
ATOM   1029 C CG  . PHE A 1 141 ? 26.284 17.327  106.890 1.00 42.80  ? 121 PHE A CG  1 
ATOM   1030 C CD1 . PHE A 1 141 ? 25.744 16.259  107.551 1.00 41.94  ? 121 PHE A CD1 1 
ATOM   1031 C CD2 . PHE A 1 141 ? 27.018 17.086  105.744 1.00 42.93  ? 121 PHE A CD2 1 
ATOM   1032 C CE1 . PHE A 1 141 ? 25.929 14.970  107.112 1.00 44.49  ? 121 PHE A CE1 1 
ATOM   1033 C CE2 . PHE A 1 141 ? 27.155 15.806  105.258 1.00 47.36  ? 121 PHE A CE2 1 
ATOM   1034 C CZ  . PHE A 1 141 ? 26.613 14.738  105.949 1.00 45.19  ? 121 PHE A CZ  1 
ATOM   1035 N N   . LYS A 1 142 ? 27.650 21.045  109.895 1.00 41.86  ? 122 LYS A N   1 
ATOM   1036 C CA  . LYS A 1 142 ? 27.714 22.520  110.134 1.00 44.53  ? 122 LYS A CA  1 
ATOM   1037 C C   . LYS A 1 142 ? 28.848 23.300  109.450 1.00 46.72  ? 122 LYS A C   1 
ATOM   1038 O O   . LYS A 1 142 ? 28.638 24.464  109.175 1.00 54.14  ? 122 LYS A O   1 
ATOM   1039 C CB  . LYS A 1 142 ? 27.744 22.834  111.618 1.00 46.63  ? 122 LYS A CB  1 
ATOM   1040 C CG  . LYS A 1 142 ? 29.123 22.810  112.220 1.00 53.06  ? 122 LYS A CG  1 
ATOM   1041 C CD  . LYS A 1 142 ? 29.023 22.577  113.712 1.00 53.16  ? 122 LYS A CD  1 
ATOM   1042 C CE  . LYS A 1 142 ? 30.358 22.873  114.383 1.00 56.96  ? 122 LYS A CE  1 
ATOM   1043 N NZ  . LYS A 1 142 ? 30.514 21.973  115.545 1.00 58.63  ? 122 LYS A NZ  1 
ATOM   1044 N N   . SER A 1 143 ? 29.997 22.666  109.137 1.00 44.98  ? 123 SER A N   1 
ATOM   1045 C CA  . SER A 1 143 ? 31.081 23.312  108.354 1.00 41.82  ? 123 SER A CA  1 
ATOM   1046 C C   . SER A 1 143 ? 31.015 22.995  106.893 1.00 44.30  ? 123 SER A C   1 
ATOM   1047 O O   . SER A 1 143 ? 31.995 23.187  106.191 1.00 49.43  ? 123 SER A O   1 
ATOM   1048 C CB  . SER A 1 143 ? 32.504 22.911  108.828 1.00 40.98  ? 123 SER A CB  1 
ATOM   1049 O OG  . SER A 1 143 ? 32.562 22.607  110.231 1.00 44.59  ? 123 SER A OG  1 
ATOM   1050 N N   . ILE A 1 144 ? 29.886 22.514  106.401 1.00 42.17  ? 124 ILE A N   1 
ATOM   1051 C CA  . ILE A 1 144 ? 29.795 22.195  104.983 1.00 43.01  ? 124 ILE A CA  1 
ATOM   1052 C C   . ILE A 1 144 ? 28.763 23.117  104.474 1.00 41.61  ? 124 ILE A C   1 
ATOM   1053 O O   . ILE A 1 144 ? 27.728 23.267  105.103 1.00 43.90  ? 124 ILE A O   1 
ATOM   1054 C CB  . ILE A 1 144 ? 29.295 20.715  104.721 1.00 40.37  ? 124 ILE A CB  1 
ATOM   1055 C CG1 . ILE A 1 144 ? 30.241 19.716  105.341 1.00 41.39  ? 124 ILE A CG1 1 
ATOM   1056 C CG2 . ILE A 1 144 ? 29.134 20.424  103.248 1.00 35.36  ? 124 ILE A CG2 1 
ATOM   1057 C CD1 . ILE A 1 144 ? 31.631 19.775  104.780 1.00 43.08  ? 124 ILE A CD1 1 
ATOM   1058 N N   . SER A 1 145 ? 28.997 23.702  103.319 1.00 43.39  ? 125 SER A N   1 
ATOM   1059 C CA  . SER A 1 145 ? 28.091 24.723  102.819 1.00 43.85  ? 125 SER A CA  1 
ATOM   1060 C C   . SER A 1 145 ? 27.012 24.066  101.995 1.00 48.13  ? 125 SER A C   1 
ATOM   1061 O O   . SER A 1 145 ? 27.088 22.865  101.690 1.00 50.76  ? 125 SER A O   1 
ATOM   1062 C CB  . SER A 1 145 ? 28.852 25.738  102.000 1.00 45.85  ? 125 SER A CB  1 
ATOM   1063 O OG  . SER A 1 145 ? 29.276 25.187  100.759 1.00 61.51  ? 125 SER A OG  1 
ATOM   1064 N N   . ASP A 1 146 ? 26.005 24.867  101.691 1.00 52.23  ? 126 ASP A N   1 
ATOM   1065 C CA  . ASP A 1 146 ? 24.841 24.498  100.890 1.00 56.08  ? 126 ASP A CA  1 
ATOM   1066 C C   . ASP A 1 146 ? 25.204 24.071  99.478  1.00 58.36  ? 126 ASP A C   1 
ATOM   1067 O O   . ASP A 1 146 ? 24.587 23.158  98.987  1.00 69.56  ? 126 ASP A O   1 
ATOM   1068 C CB  . ASP A 1 146 ? 23.864 25.693  100.752 1.00 62.48  ? 126 ASP A CB  1 
ATOM   1069 C CG  . ASP A 1 146 ? 23.144 26.083  102.076 1.00 73.27  ? 126 ASP A CG  1 
ATOM   1070 O OD1 . ASP A 1 146 ? 22.961 25.262  103.004 1.00 78.07  ? 126 ASP A OD1 1 
ATOM   1071 O OD2 . ASP A 1 146 ? 22.712 27.249  102.168 1.00 78.20  ? 126 ASP A OD2 1 
ATOM   1072 N N   . GLU A 1 147 ? 26.133 24.746  98.794  1.00 63.04  ? 127 GLU A N   1 
ATOM   1073 C CA  . GLU A 1 147 ? 26.557 24.296  97.439  1.00 64.23  ? 127 GLU A CA  1 
ATOM   1074 C C   . GLU A 1 147 ? 27.299 22.961  97.505  1.00 67.37  ? 127 GLU A C   1 
ATOM   1075 O O   . GLU A 1 147 ? 27.114 22.141  96.623  1.00 74.81  ? 127 GLU A O   1 
ATOM   1076 C CB  . GLU A 1 147 ? 27.460 25.268  96.641  1.00 77.17  ? 127 GLU A CB  1 
ATOM   1077 C CG  . GLU A 1 147 ? 28.062 26.480  97.351  1.00 94.15  ? 127 GLU A CG  1 
ATOM   1078 C CD  . GLU A 1 147 ? 27.040 27.576  97.596  1.00 106.38 ? 127 GLU A CD  1 
ATOM   1079 O OE1 . GLU A 1 147 ? 26.213 27.821  96.683  1.00 116.19 ? 127 GLU A OE1 1 
ATOM   1080 O OE2 . GLU A 1 147 ? 27.061 28.168  98.703  1.00 98.21  ? 127 GLU A OE2 1 
ATOM   1081 N N   . GLU A 1 148 ? 28.128 22.757  98.533  1.00 58.18  ? 128 GLU A N   1 
ATOM   1082 C CA  . GLU A 1 148 ? 28.965 21.560  98.685  1.00 54.07  ? 128 GLU A CA  1 
ATOM   1083 C C   . GLU A 1 148 ? 28.188 20.235  98.893  1.00 58.69  ? 128 GLU A C   1 
ATOM   1084 O O   . GLU A 1 148 ? 28.615 19.128  98.444  1.00 53.55  ? 128 GLU A O   1 
ATOM   1085 C CB  . GLU A 1 148 ? 29.934 21.744  99.856  1.00 47.50  ? 128 GLU A CB  1 
ATOM   1086 C CG  . GLU A 1 148 ? 31.213 22.497  99.489  1.00 46.54  ? 128 GLU A CG  1 
ATOM   1087 C CD  . GLU A 1 148 ? 32.005 22.932  100.704 1.00 47.39  ? 128 GLU A CD  1 
ATOM   1088 O OE1 . GLU A 1 148 ? 31.341 23.169  101.720 1.00 51.04  ? 128 GLU A OE1 1 
ATOM   1089 O OE2 . GLU A 1 148 ? 33.278 23.044  100.700 1.00 49.69  ? 128 GLU A OE2 1 
ATOM   1090 N N   . LEU A 1 149 ? 27.064 20.345  99.579  1.00 51.40  ? 129 LEU A N   1 
ATOM   1091 C CA  . LEU A 1 149 ? 26.256 19.201  99.867  1.00 52.92  ? 129 LEU A CA  1 
ATOM   1092 C C   . LEU A 1 149 ? 25.834 18.390  98.601  1.00 52.58  ? 129 LEU A C   1 
ATOM   1093 O O   . LEU A 1 149 ? 25.979 17.187  98.566  1.00 56.39  ? 129 LEU A O   1 
ATOM   1094 C CB  . LEU A 1 149 ? 25.050 19.638  100.701 1.00 56.23  ? 129 LEU A CB  1 
ATOM   1095 C CG  . LEU A 1 149 ? 24.641 18.798  101.913 1.00 57.79  ? 129 LEU A CG  1 
ATOM   1096 C CD1 . LEU A 1 149 ? 23.616 17.817  101.475 1.00 55.82  ? 129 LEU A CD1 1 
ATOM   1097 C CD2 . LEU A 1 149 ? 25.800 18.060  102.573 1.00 64.84  ? 129 LEU A CD2 1 
ATOM   1098 N N   . PRO A 1 150 ? 25.327 19.034  97.559  1.00 53.52  ? 130 PRO A N   1 
ATOM   1099 C CA  . PRO A 1 150 ? 24.924 18.188  96.422  1.00 55.33  ? 130 PRO A CA  1 
ATOM   1100 C C   . PRO A 1 150 ? 26.089 17.723  95.553  1.00 45.96  ? 130 PRO A C   1 
ATOM   1101 O O   . PRO A 1 150 ? 25.976 16.780  94.815  1.00 46.01  ? 130 PRO A O   1 
ATOM   1102 C CB  . PRO A 1 150 ? 23.941 19.084  95.636  1.00 53.52  ? 130 PRO A CB  1 
ATOM   1103 C CG  . PRO A 1 150 ? 24.286 20.480  96.049  1.00 53.35  ? 130 PRO A CG  1 
ATOM   1104 C CD  . PRO A 1 150 ? 24.725 20.375  97.487  1.00 56.93  ? 130 PRO A CD  1 
ATOM   1105 N N   . LEU A 1 151 ? 27.187 18.426  95.660  1.00 51.30  ? 131 LEU A N   1 
ATOM   1106 C CA  . LEU A 1 151 ? 28.468 18.048  95.097  1.00 51.04  ? 131 LEU A CA  1 
ATOM   1107 C C   . LEU A 1 151 ? 28.910 16.762  95.762  1.00 43.96  ? 131 LEU A C   1 
ATOM   1108 O O   . LEU A 1 151 ? 29.112 15.755  95.123  1.00 52.65  ? 131 LEU A O   1 
ATOM   1109 C CB  . LEU A 1 151 ? 29.424 19.165  95.430  1.00 58.90  ? 131 LEU A CB  1 
ATOM   1110 C CG  . LEU A 1 151 ? 30.416 19.566  94.381  1.00 75.11  ? 131 LEU A CG  1 
ATOM   1111 C CD1 . LEU A 1 151 ? 30.758 21.056  94.513  1.00 82.08  ? 131 LEU A CD1 1 
ATOM   1112 C CD2 . LEU A 1 151 ? 31.608 18.666  94.580  1.00 79.86  ? 131 LEU A CD2 1 
ATOM   1113 N N   . PHE A 1 152 ? 28.983 16.777  97.082  1.00 42.65  ? 132 PHE A N   1 
ATOM   1114 C CA  . PHE A 1 152 ? 29.360 15.603  97.849  1.00 40.44  ? 132 PHE A CA  1 
ATOM   1115 C C   . PHE A 1 152 ? 28.544 14.417  97.362  1.00 43.16  ? 132 PHE A C   1 
ATOM   1116 O O   . PHE A 1 152 ? 29.039 13.324  97.043  1.00 37.33  ? 132 PHE A O   1 
ATOM   1117 C CB  . PHE A 1 152 ? 29.027 15.858  99.309  1.00 37.39  ? 132 PHE A CB  1 
ATOM   1118 C CG  . PHE A 1 152 ? 29.518 14.811  100.248 1.00 36.03  ? 132 PHE A CG  1 
ATOM   1119 C CD1 . PHE A 1 152 ? 30.832 14.489  100.299 1.00 36.77  ? 132 PHE A CD1 1 
ATOM   1120 C CD2 . PHE A 1 152 ? 28.658 14.188  101.119 1.00 39.34  ? 132 PHE A CD2 1 
ATOM   1121 C CE1 . PHE A 1 152 ? 31.296 13.541  101.183 1.00 37.02  ? 132 PHE A CE1 1 
ATOM   1122 C CE2 . PHE A 1 152 ? 29.105 13.232  101.990 1.00 40.74  ? 132 PHE A CE2 1 
ATOM   1123 C CZ  . PHE A 1 152 ? 30.439 12.921  102.040 1.00 38.21  ? 132 PHE A CZ  1 
ATOM   1124 N N   . THR A 1 153 ? 27.265 14.694  97.298  1.00 42.56  ? 133 THR A N   1 
ATOM   1125 C CA  . THR A 1 153 ? 26.292 13.710  97.015  1.00 42.71  ? 133 THR A CA  1 
ATOM   1126 C C   . THR A 1 153 ? 26.449 13.149  95.631  1.00 36.17  ? 133 THR A C   1 
ATOM   1127 O O   . THR A 1 153 ? 26.388 11.929  95.481  1.00 38.53  ? 133 THR A O   1 
ATOM   1128 C CB  . THR A 1 153 ? 24.901 14.254  97.367  1.00 48.57  ? 133 THR A CB  1 
ATOM   1129 O OG1 . THR A 1 153 ? 24.630 13.790  98.698  1.00 51.79  ? 133 THR A OG1 1 
ATOM   1130 C CG2 . THR A 1 153 ? 23.809 13.804  96.412  1.00 57.20  ? 133 THR A CG2 1 
ATOM   1131 N N   . ASP A 1 154 ? 26.737 13.995  94.657  1.00 35.63  ? 134 ASP A N   1 
ATOM   1132 C CA  . ASP A 1 154 ? 26.893 13.560  93.303  1.00 40.79  ? 134 ASP A CA  1 
ATOM   1133 C C   . ASP A 1 154 ? 28.157 12.708  93.187  1.00 44.04  ? 134 ASP A C   1 
ATOM   1134 O O   . ASP A 1 154 ? 28.136 11.653  92.558  1.00 45.06  ? 134 ASP A O   1 
ATOM   1135 C CB  . ASP A 1 154 ? 26.997 14.736  92.367  1.00 45.78  ? 134 ASP A CB  1 
ATOM   1136 C CG  . ASP A 1 154 ? 27.176 14.314  90.913  1.00 54.96  ? 134 ASP A CG  1 
ATOM   1137 O OD1 . ASP A 1 154 ? 26.439 13.422  90.430  1.00 54.95  ? 134 ASP A OD1 1 
ATOM   1138 O OD2 . ASP A 1 154 ? 28.045 14.906  90.242  1.00 64.05  ? 134 ASP A OD2 1 
ATOM   1139 N N   . ILE A 1 155 ? 29.224 13.144  93.835  1.00 38.55  ? 135 ILE A N   1 
ATOM   1140 C CA  . ILE A 1 155 ? 30.432 12.401  93.785  1.00 39.20  ? 135 ILE A CA  1 
ATOM   1141 C C   . ILE A 1 155 ? 30.195 11.040  94.348  1.00 39.30  ? 135 ILE A C   1 
ATOM   1142 O O   . ILE A 1 155 ? 30.448 10.032  93.674  1.00 45.10  ? 135 ILE A O   1 
ATOM   1143 C CB  . ILE A 1 155 ? 31.572 13.125  94.521  1.00 39.96  ? 135 ILE A CB  1 
ATOM   1144 C CG1 . ILE A 1 155 ? 31.976 14.364  93.717  1.00 39.89  ? 135 ILE A CG1 1 
ATOM   1145 C CG2 . ILE A 1 155 ? 32.741 12.174  94.739  1.00 34.97  ? 135 ILE A CG2 1 
ATOM   1146 C CD1 . ILE A 1 155 ? 32.946 15.269  94.433  1.00 45.69  ? 135 ILE A CD1 1 
ATOM   1147 N N   . LEU A 1 156 ? 29.654 10.964  95.548  1.00 41.55  ? 136 LEU A N   1 
ATOM   1148 C CA  . LEU A 1 156 ? 29.291 9.634   96.087  1.00 42.77  ? 136 LEU A CA  1 
ATOM   1149 C C   . LEU A 1 156 ? 28.391 8.795   95.149  1.00 45.08  ? 136 LEU A C   1 
ATOM   1150 O O   . LEU A 1 156 ? 28.517 7.596   95.100  1.00 44.26  ? 136 LEU A O   1 
ATOM   1151 C CB  . LEU A 1 156 ? 28.567 9.729   97.424  1.00 39.27  ? 136 LEU A CB  1 
ATOM   1152 C CG  . LEU A 1 156 ? 29.319 10.204  98.650  1.00 41.01  ? 136 LEU A CG  1 
ATOM   1153 C CD1 . LEU A 1 156 ? 28.355 10.466  99.785  1.00 46.32  ? 136 LEU A CD1 1 
ATOM   1154 C CD2 . LEU A 1 156 ? 30.357 9.215   99.109  1.00 40.19  ? 136 LEU A CD2 1 
ATOM   1155 N N   . ASP A 1 157 ? 27.431 9.401   94.479  1.00 48.38  ? 137 ASP A N   1 
ATOM   1156 C CA  . ASP A 1 157 ? 26.619 8.629   93.552  1.00 52.88  ? 137 ASP A CA  1 
ATOM   1157 C C   . ASP A 1 157 ? 27.511 7.984   92.455  1.00 58.31  ? 137 ASP A C   1 
ATOM   1158 O O   . ASP A 1 157 ? 27.350 6.801   92.136  1.00 53.79  ? 137 ASP A O   1 
ATOM   1159 C CB  . ASP A 1 157 ? 25.513 9.482   92.908  1.00 55.67  ? 137 ASP A CB  1 
ATOM   1160 C CG  . ASP A 1 157 ? 24.396 9.854   93.896  1.00 60.83  ? 137 ASP A CG  1 
ATOM   1161 O OD1 . ASP A 1 157 ? 24.109 9.049   94.827  1.00 52.52  ? 137 ASP A OD1 1 
ATOM   1162 O OD2 . ASP A 1 157 ? 23.840 10.981  93.757  1.00 64.50  ? 137 ASP A OD2 1 
ATOM   1163 N N   . ARG A 1 158 ? 28.447 8.753   91.905  1.00 51.40  ? 138 ARG A N   1 
ATOM   1164 C CA  . ARG A 1 158 ? 29.301 8.283   90.822  1.00 44.73  ? 138 ARG A CA  1 
ATOM   1165 C C   . ARG A 1 158 ? 30.349 7.229   91.268  1.00 47.96  ? 138 ARG A C   1 
ATOM   1166 O O   . ARG A 1 158 ? 30.860 6.486   90.446  1.00 48.15  ? 138 ARG A O   1 
ATOM   1167 C CB  . ARG A 1 158 ? 29.989 9.463   90.163  1.00 41.55  ? 138 ARG A CB  1 
ATOM   1168 C CG  . ARG A 1 158 ? 29.150 10.187  89.074  1.00 41.43  ? 138 ARG A CG  1 
ATOM   1169 C CD  . ARG A 1 158 ? 29.233 11.730  89.200  1.00 46.28  ? 138 ARG A CD  1 
ATOM   1170 N NE  . ARG A 1 158 ? 30.530 12.208  88.795  1.00 47.38  ? 138 ARG A NE  1 
ATOM   1171 C CZ  . ARG A 1 158 ? 31.187 13.279  89.240  1.00 48.42  ? 138 ARG A CZ  1 
ATOM   1172 N NH1 . ARG A 1 158 ? 30.716 14.116  90.151  1.00 44.18  ? 138 ARG A NH1 1 
ATOM   1173 N NH2 . ARG A 1 158 ? 32.388 13.504  88.722  1.00 51.84  ? 138 ARG A NH2 1 
ATOM   1174 N N   . ILE A 1 159 ? 30.659 7.151   92.557  1.00 42.81  ? 139 ILE A N   1 
ATOM   1175 C CA  . ILE A 1 159 ? 31.633 6.193   92.999  1.00 42.43  ? 139 ILE A CA  1 
ATOM   1176 C C   . ILE A 1 159 ? 31.035 4.809   92.902  1.00 50.24  ? 139 ILE A C   1 
ATOM   1177 O O   . ILE A 1 159 ? 29.992 4.551   93.498  1.00 55.76  ? 139 ILE A O   1 
ATOM   1178 C CB  . ILE A 1 159 ? 32.130 6.481   94.395  1.00 41.40  ? 139 ILE A CB  1 
ATOM   1179 C CG1 . ILE A 1 159 ? 33.110 7.664   94.357  1.00 39.14  ? 139 ILE A CG1 1 
ATOM   1180 C CG2 . ILE A 1 159 ? 32.859 5.303   94.967  1.00 48.26  ? 139 ILE A CG2 1 
ATOM   1181 C CD1 . ILE A 1 159 ? 33.446 8.198   95.725  1.00 38.16  ? 139 ILE A CD1 1 
ATOM   1182 N N   . GLY A 1 160 ? 31.734 3.942   92.146  1.00 56.48  ? 140 GLY A N   1 
ATOM   1183 C CA  . GLY A 1 160 ? 31.269 2.600   91.749  1.00 58.04  ? 140 GLY A CA  1 
ATOM   1184 C C   . GLY A 1 160 ? 30.867 2.527   90.286  1.00 56.40  ? 140 GLY A C   1 
ATOM   1185 O O   . GLY A 1 160 ? 29.982 3.289   89.835  1.00 76.62  ? 140 GLY A O   1 
ATOM   1186 N N   . LYS B 2 5   ? 19.668 22.034  101.927 1.00 80.52  ? 2   LYS B N   1 
ATOM   1187 C CA  . LYS B 2 5   ? 20.395 21.472  103.133 1.00 65.89  ? 2   LYS B CA  1 
ATOM   1188 C C   . LYS B 2 5   ? 19.516 21.286  104.382 1.00 62.66  ? 2   LYS B C   1 
ATOM   1189 O O   . LYS B 2 5   ? 19.960 21.404  105.512 1.00 61.41  ? 2   LYS B O   1 
ATOM   1190 C CB  . LYS B 2 5   ? 21.665 22.307  103.413 1.00 70.19  ? 2   LYS B CB  1 
ATOM   1191 C CG  . LYS B 2 5   ? 22.304 22.209  104.792 1.00 60.24  ? 2   LYS B CG  1 
ATOM   1192 C CD  . LYS B 2 5   ? 23.786 22.572  104.742 1.00 61.82  ? 2   LYS B CD  1 
ATOM   1193 C CE  . LYS B 2 5   ? 24.180 23.314  106.018 1.00 64.98  ? 2   LYS B CE  1 
ATOM   1194 N NZ  . LYS B 2 5   ? 25.467 22.878  106.597 1.00 59.06  ? 2   LYS B NZ  1 
ATOM   1195 N N   . ASP B 2 6   ? 18.262 20.914  104.171 1.00 68.89  ? 3   ASP B N   1 
ATOM   1196 C CA  . ASP B 2 6   ? 17.412 20.595  105.295 1.00 67.53  ? 3   ASP B CA  1 
ATOM   1197 C C   . ASP B 2 6   ? 17.513 19.108  105.623 1.00 63.87  ? 3   ASP B C   1 
ATOM   1198 O O   . ASP B 2 6   ? 18.339 18.394  105.049 1.00 58.64  ? 3   ASP B O   1 
ATOM   1199 C CB  . ASP B 2 6   ? 15.983 21.085  105.070 1.00 80.98  ? 3   ASP B CB  1 
ATOM   1200 C CG  . ASP B 2 6   ? 15.429 20.697  103.747 1.00 82.21  ? 3   ASP B CG  1 
ATOM   1201 O OD1 . ASP B 2 6   ? 15.763 19.586  103.279 1.00 77.31  ? 3   ASP B OD1 1 
ATOM   1202 O OD2 . ASP B 2 6   ? 14.641 21.523  103.205 1.00 80.01  ? 3   ASP B OD2 1 
ATOM   1203 N N   . PHE B 2 7   ? 16.719 18.634  106.575 1.00 51.90  ? 4   PHE B N   1 
ATOM   1204 C CA  . PHE B 2 7   ? 17.062 17.387  107.195 1.00 49.25  ? 4   PHE B CA  1 
ATOM   1205 C C   . PHE B 2 7   ? 17.139 16.269  106.161 1.00 51.04  ? 4   PHE B C   1 
ATOM   1206 O O   . PHE B 2 7   ? 18.029 15.476  106.177 1.00 45.60  ? 4   PHE B O   1 
ATOM   1207 C CB  . PHE B 2 7   ? 16.024 17.024  108.222 1.00 47.66  ? 4   PHE B CB  1 
ATOM   1208 C CG  . PHE B 2 7   ? 16.287 15.725  108.895 1.00 46.66  ? 4   PHE B CG  1 
ATOM   1209 C CD1 . PHE B 2 7   ? 17.555 15.359  109.217 1.00 45.76  ? 4   PHE B CD1 1 
ATOM   1210 C CD2 . PHE B 2 7   ? 15.265 14.905  109.223 1.00 50.60  ? 4   PHE B CD2 1 
ATOM   1211 C CE1 . PHE B 2 7   ? 17.804 14.174  109.856 1.00 51.00  ? 4   PHE B CE1 1 
ATOM   1212 C CE2 . PHE B 2 7   ? 15.503 13.703  109.841 1.00 54.13  ? 4   PHE B CE2 1 
ATOM   1213 C CZ  . PHE B 2 7   ? 16.782 13.343  110.167 1.00 48.10  ? 4   PHE B CZ  1 
ATOM   1214 N N   . GLU B 2 8   ? 16.187 16.255  105.251 1.00 54.40  ? 5   GLU B N   1 
ATOM   1215 C CA  . GLU B 2 8   ? 16.032 15.197  104.309 1.00 61.78  ? 5   GLU B CA  1 
ATOM   1216 C C   . GLU B 2 8   ? 17.338 14.959  103.562 1.00 58.15  ? 5   GLU B C   1 
ATOM   1217 O O   . GLU B 2 8   ? 17.779 13.803  103.483 1.00 49.61  ? 5   GLU B O   1 
ATOM   1218 C CB  . GLU B 2 8   ? 14.899 15.525  103.323 1.00 67.70  ? 5   GLU B CB  1 
ATOM   1219 C CG  . GLU B 2 8   ? 14.392 14.313  102.554 1.00 84.07  ? 5   GLU B CG  1 
ATOM   1220 C CD  . GLU B 2 8   ? 14.074 13.132  103.473 1.00 96.56  ? 5   GLU B CD  1 
ATOM   1221 O OE1 . GLU B 2 8   ? 13.430 13.379  104.560 1.00 79.54  ? 5   GLU B OE1 1 
ATOM   1222 O OE2 . GLU B 2 8   ? 14.502 11.981  103.105 1.00 83.95  ? 5   GLU B OE2 1 
ATOM   1223 N N   . LYS B 2 9   ? 17.937 16.054  103.072 1.00 48.39  ? 6   LYS B N   1 
ATOM   1224 C CA  . LYS B 2 9   ? 19.161 16.011  102.283 1.00 50.77  ? 6   LYS B CA  1 
ATOM   1225 C C   . LYS B 2 9   ? 20.364 15.594  103.107 1.00 52.69  ? 6   LYS B C   1 
ATOM   1226 O O   . LYS B 2 9   ? 21.216 14.884  102.631 1.00 53.21  ? 6   LYS B O   1 
ATOM   1227 C CB  . LYS B 2 9   ? 19.506 17.356  101.694 1.00 54.74  ? 6   LYS B CB  1 
ATOM   1228 C CG  . LYS B 2 9   ? 18.434 18.025  100.845 1.00 69.57  ? 6   LYS B CG  1 
ATOM   1229 C CD  . LYS B 2 9   ? 18.151 17.296  99.533  1.00 80.51  ? 6   LYS B CD  1 
ATOM   1230 C CE  . LYS B 2 9   ? 17.191 18.101  98.661  1.00 90.52  ? 6   LYS B CE  1 
ATOM   1231 N NZ  . LYS B 2 9   ? 16.768 17.315  97.471  1.00 88.78  ? 6   LYS B NZ  1 
ATOM   1232 N N   . LEU B 2 10  ? 20.442 16.066  104.339 1.00 47.78  ? 7   LEU B N   1 
ATOM   1233 C CA  . LEU B 2 10  ? 21.515 15.681  105.188 1.00 41.13  ? 7   LEU B CA  1 
ATOM   1234 C C   . LEU B 2 10  ? 21.403 14.198  105.542 1.00 43.44  ? 7   LEU B C   1 
ATOM   1235 O O   . LEU B 2 10  ? 22.432 13.515  105.771 1.00 40.72  ? 7   LEU B O   1 
ATOM   1236 C CB  . LEU B 2 10  ? 21.522 16.510  106.471 1.00 38.59  ? 7   LEU B CB  1 
ATOM   1237 C CG  . LEU B 2 10  ? 21.613 18.039  106.307 1.00 41.31  ? 7   LEU B CG  1 
ATOM   1238 C CD1 . LEU B 2 10  ? 21.794 18.636  107.688 1.00 38.73  ? 7   LEU B CD1 1 
ATOM   1239 C CD2 . LEU B 2 10  ? 22.700 18.492  105.339 1.00 39.82  ? 7   LEU B CD2 1 
ATOM   1240 N N   . TYR B 2 11  ? 20.176 13.703  105.669 1.00 41.55  ? 8   TYR B N   1 
ATOM   1241 C CA  . TYR B 2 11  ? 20.008 12.309  106.074 1.00 44.41  ? 8   TYR B CA  1 
ATOM   1242 C C   . TYR B 2 11  ? 20.450 11.451  104.885 1.00 47.46  ? 8   TYR B C   1 
ATOM   1243 O O   . TYR B 2 11  ? 21.056 10.448  105.085 1.00 44.26  ? 8   TYR B O   1 
ATOM   1244 C CB  . TYR B 2 11  ? 18.569 11.954  106.443 1.00 41.88  ? 8   TYR B CB  1 
ATOM   1245 C CG  . TYR B 2 11  ? 18.406 10.534  106.884 1.00 39.35  ? 8   TYR B CG  1 
ATOM   1246 C CD1 . TYR B 2 11  ? 18.838 10.127  108.134 1.00 43.29  ? 8   TYR B CD1 1 
ATOM   1247 C CD2 . TYR B 2 11  ? 17.876 9.571   106.008 1.00 46.33  ? 8   TYR B CD2 1 
ATOM   1248 C CE1 . TYR B 2 11  ? 18.742 8.797   108.528 1.00 51.50  ? 8   TYR B CE1 1 
ATOM   1249 C CE2 . TYR B 2 11  ? 17.753 8.229   106.378 1.00 44.83  ? 8   TYR B CE2 1 
ATOM   1250 C CZ  . TYR B 2 11  ? 18.184 7.846   107.628 1.00 51.92  ? 8   TYR B CZ  1 
ATOM   1251 O OH  . TYR B 2 11  ? 18.068 6.533   107.999 1.00 62.77  ? 8   TYR B OH  1 
ATOM   1252 N N   . GLU B 2 12  ? 20.091 11.875  103.679 1.00 51.61  ? 9   GLU B N   1 
ATOM   1253 C CA  . GLU B 2 12  ? 20.450 11.219  102.465 1.00 58.58  ? 9   GLU B CA  1 
ATOM   1254 C C   . GLU B 2 12  ? 21.955 11.094  102.404 1.00 59.84  ? 9   GLU B C   1 
ATOM   1255 O O   . GLU B 2 12  ? 22.497 9.982   102.294 1.00 56.77  ? 9   GLU B O   1 
ATOM   1256 C CB  . GLU B 2 12  ? 19.984 12.037  101.254 1.00 68.04  ? 9   GLU B CB  1 
ATOM   1257 C CG  . GLU B 2 12  ? 18.521 11.832  100.859 1.00 87.80  ? 9   GLU B CG  1 
ATOM   1258 C CD  . GLU B 2 12  ? 18.171 12.520  99.538  1.00 101.38 ? 9   GLU B CD  1 
ATOM   1259 O OE1 . GLU B 2 12  ? 17.091 13.179  99.479  1.00 105.59 ? 9   GLU B OE1 1 
ATOM   1260 O OE2 . GLU B 2 12  ? 18.994 12.402  98.580  1.00 95.57  ? 9   GLU B OE2 1 
ATOM   1261 N N   . ALA B 2 13  ? 22.600 12.255  102.467 1.00 47.79  ? 10  ALA B N   1 
ATOM   1262 C CA  . ALA B 2 13  ? 24.001 12.370  102.375 1.00 41.38  ? 10  ALA B CA  1 
ATOM   1263 C C   . ALA B 2 13  ? 24.680 11.484  103.416 1.00 41.39  ? 10  ALA B C   1 
ATOM   1264 O O   . ALA B 2 13  ? 25.591 10.765  103.070 1.00 39.07  ? 10  ALA B O   1 
ATOM   1265 C CB  . ALA B 2 13  ? 24.395 13.794  102.574 1.00 44.80  ? 10  ALA B CB  1 
ATOM   1266 N N   . THR B 2 14  ? 24.228 11.486  104.660 1.00 37.93  ? 11  THR B N   1 
ATOM   1267 C CA  . THR B 2 14  ? 24.811 10.561  105.643 1.00 43.25  ? 11  THR B CA  1 
ATOM   1268 C C   . THR B 2 14  ? 24.737 9.092   105.254 1.00 45.42  ? 11  THR B C   1 
ATOM   1269 O O   . THR B 2 14  ? 25.563 8.278   105.626 1.00 52.87  ? 11  THR B O   1 
ATOM   1270 C CB  . THR B 2 14  ? 24.148 10.709  106.989 1.00 40.21  ? 11  THR B CB  1 
ATOM   1271 O OG1 . THR B 2 14  ? 24.366 12.054  107.436 1.00 49.34  ? 11  THR B OG1 1 
ATOM   1272 C CG2 . THR B 2 14  ? 24.755 9.789   108.011 1.00 45.21  ? 11  THR B CG2 1 
ATOM   1273 N N   . THR B 2 15  ? 23.763 8.769   104.460 1.00 49.13  ? 12  THR B N   1 
ATOM   1274 C CA  . THR B 2 15  ? 23.358 7.403   104.239 1.00 50.20  ? 12  THR B CA  1 
ATOM   1275 C C   . THR B 2 15  ? 24.069 6.944   102.946 1.00 47.63  ? 12  THR B C   1 
ATOM   1276 O O   . THR B 2 15  ? 24.551 5.838   102.878 1.00 54.05  ? 12  THR B O   1 
ATOM   1277 C CB  . THR B 2 15  ? 21.767 7.342   104.276 1.00 50.41  ? 12  THR B CB  1 
ATOM   1278 O OG1 . THR B 2 15  ? 21.342 6.276   105.112 1.00 52.70  ? 12  THR B OG1 1 
ATOM   1279 C CG2 . THR B 2 15  ? 21.075 7.278   102.914 1.00 44.52  ? 12  THR B CG2 1 
ATOM   1280 N N   . LYS B 2 16  ? 24.177 7.809   101.941 1.00 43.09  ? 13  LYS B N   1 
ATOM   1281 C CA  . LYS B 2 16  ? 25.071 7.531   100.852 1.00 47.55  ? 13  LYS B CA  1 
ATOM   1282 C C   . LYS B 2 16  ? 26.524 7.436   101.365 1.00 51.39  ? 13  LYS B C   1 
ATOM   1283 O O   . LYS B 2 16  ? 27.331 6.608   100.907 1.00 51.70  ? 13  LYS B O   1 
ATOM   1284 C CB  . LYS B 2 16  ? 25.003 8.616   99.833  1.00 48.07  ? 13  LYS B CB  1 
ATOM   1285 C CG  . LYS B 2 16  ? 23.680 8.711   99.146  1.00 51.50  ? 13  LYS B CG  1 
ATOM   1286 C CD  . LYS B 2 16  ? 23.607 9.988   98.337  1.00 61.76  ? 13  LYS B CD  1 
ATOM   1287 C CE  . LYS B 2 16  ? 22.213 10.270  97.784  1.00 63.65  ? 13  LYS B CE  1 
ATOM   1288 N NZ  . LYS B 2 16  ? 22.000 9.566   96.496  1.00 57.38  ? 13  LYS B NZ  1 
ATOM   1289 N N   . LEU B 2 17  ? 26.877 8.272   102.320 1.00 45.95  ? 14  LEU B N   1 
ATOM   1290 C CA  . LEU B 2 17  ? 28.225 8.213   102.753 1.00 47.45  ? 14  LEU B CA  1 
ATOM   1291 C C   . LEU B 2 17  ? 28.444 6.796   103.279 1.00 48.23  ? 14  LEU B C   1 
ATOM   1292 O O   . LEU B 2 17  ? 29.405 6.149   102.891 1.00 45.10  ? 14  LEU B O   1 
ATOM   1293 C CB  . LEU B 2 17  ? 28.561 9.268   103.792 1.00 46.05  ? 14  LEU B CB  1 
ATOM   1294 C CG  . LEU B 2 17  ? 29.759 8.988   104.695 1.00 45.40  ? 14  LEU B CG  1 
ATOM   1295 C CD1 . LEU B 2 17  ? 31.009 9.033   103.868 1.00 42.18  ? 14  LEU B CD1 1 
ATOM   1296 C CD2 . LEU B 2 17  ? 29.837 10.002  105.820 1.00 48.28  ? 14  LEU B CD2 1 
ATOM   1297 N N   . VAL B 2 18  ? 27.567 6.321   104.153 1.00 48.59  ? 15  VAL B N   1 
ATOM   1298 C CA  . VAL B 2 18  ? 27.808 5.063   104.851 1.00 42.98  ? 15  VAL B CA  1 
ATOM   1299 C C   . VAL B 2 18  ? 27.609 3.903   103.913 1.00 44.06  ? 15  VAL B C   1 
ATOM   1300 O O   . VAL B 2 18  ? 28.321 2.951   103.955 1.00 40.16  ? 15  VAL B O   1 
ATOM   1301 C CB  . VAL B 2 18  ? 26.891 4.918   106.071 1.00 48.73  ? 15  VAL B CB  1 
ATOM   1302 C CG1 . VAL B 2 18  ? 26.727 3.460   106.537 1.00 49.88  ? 15  VAL B CG1 1 
ATOM   1303 C CG2 . VAL B 2 18  ? 27.464 5.749   107.237 1.00 43.50  ? 15  VAL B CG2 1 
ATOM   1304 N N   . SER B 2 19  ? 26.672 3.990   103.011 1.00 46.52  ? 16  SER B N   1 
ATOM   1305 C CA  . SER B 2 19  ? 26.498 2.896   102.127 1.00 45.00  ? 16  SER B CA  1 
ATOM   1306 C C   . SER B 2 19  ? 27.656 2.828   101.075 1.00 51.07  ? 16  SER B C   1 
ATOM   1307 O O   . SER B 2 19  ? 28.123 1.728   100.762 1.00 52.46  ? 16  SER B O   1 
ATOM   1308 C CB  . SER B 2 19  ? 25.117 2.968   101.492 1.00 40.42  ? 16  SER B CB  1 
ATOM   1309 O OG  . SER B 2 19  ? 25.152 3.813   100.358 1.00 48.64  ? 16  SER B OG  1 
ATOM   1310 N N   . THR B 2 20  ? 28.111 3.966   100.537 1.00 47.96  ? 17  THR B N   1 
ATOM   1311 C CA  . THR B 2 20  ? 29.212 3.961   99.578  1.00 42.12  ? 17  THR B CA  1 
ATOM   1312 C C   . THR B 2 20  ? 30.502 3.372   100.174 1.00 43.20  ? 17  THR B C   1 
ATOM   1313 O O   . THR B 2 20  ? 31.209 2.572   99.556  1.00 45.07  ? 17  THR B O   1 
ATOM   1314 C CB  . THR B 2 20  ? 29.534 5.334   99.104  1.00 37.57  ? 17  THR B CB  1 
ATOM   1315 O OG1 . THR B 2 20  ? 28.412 5.864   98.423  1.00 39.48  ? 17  THR B OG1 1 
ATOM   1316 C CG2 . THR B 2 20  ? 30.643 5.278   98.135  1.00 38.41  ? 17  THR B CG2 1 
ATOM   1317 N N   . SER B 2 21  ? 30.777 3.740   101.395 1.00 39.95  ? 18  SER B N   1 
ATOM   1318 C CA  . SER B 2 21  ? 31.862 3.139   102.151 1.00 40.73  ? 18  SER B CA  1 
ATOM   1319 C C   . SER B 2 21  ? 31.757 1.632   102.364 1.00 47.61  ? 18  SER B C   1 
ATOM   1320 O O   . SER B 2 21  ? 32.771 0.957   102.457 1.00 55.26  ? 18  SER B O   1 
ATOM   1321 C CB  . SER B 2 21  ? 31.851 3.707   103.540 1.00 33.49  ? 18  SER B CB  1 
ATOM   1322 O OG  . SER B 2 21  ? 32.788 3.044   104.353 1.00 37.49  ? 18  SER B OG  1 
ATOM   1323 N N   . LEU B 2 22  ? 30.552 1.135   102.618 1.00 54.67  ? 19  LEU B N   1 
ATOM   1324 C CA  . LEU B 2 22  ? 30.344 -0.291  102.822 1.00 54.49  ? 19  LEU B CA  1 
ATOM   1325 C C   . LEU B 2 22  ? 30.543 -1.011  101.461 1.00 50.32  ? 19  LEU B C   1 
ATOM   1326 O O   . LEU B 2 22  ? 31.202 -2.007  101.413 1.00 43.99  ? 19  LEU B O   1 
ATOM   1327 C CB  . LEU B 2 22  ? 28.951 -0.595  103.436 1.00 60.76  ? 19  LEU B CB  1 
ATOM   1328 C CG  . LEU B 2 22  ? 28.870 -0.461  104.988 1.00 74.77  ? 19  LEU B CG  1 
ATOM   1329 C CD1 . LEU B 2 22  ? 27.450 -0.523  105.612 1.00 68.59  ? 19  LEU B CD1 1 
ATOM   1330 C CD2 . LEU B 2 22  ? 29.796 -1.469  105.678 1.00 75.97  ? 19  LEU B CD2 1 
ATOM   1331 N N   . LYS B 2 23  ? 30.012 -0.459  100.380 1.00 42.34  ? 20  LYS B N   1 
ATOM   1332 C CA  . LYS B 2 23  ? 30.050 -1.067  99.082  1.00 42.47  ? 20  LYS B CA  1 
ATOM   1333 C C   . LYS B 2 23  ? 31.502 -1.206  98.604  1.00 46.39  ? 20  LYS B C   1 
ATOM   1334 O O   . LYS B 2 23  ? 31.922 -2.257  98.122  1.00 53.85  ? 20  LYS B O   1 
ATOM   1335 C CB  . LYS B 2 23  ? 29.252 -0.198  98.121  1.00 44.44  ? 20  LYS B CB  1 
ATOM   1336 C CG  . LYS B 2 23  ? 28.977 -0.765  96.748  1.00 56.57  ? 20  LYS B CG  1 
ATOM   1337 C CD  . LYS B 2 23  ? 28.831 0.343   95.682  1.00 73.89  ? 20  LYS B CD  1 
ATOM   1338 C CE  . LYS B 2 23  ? 29.087 -0.162  94.237  1.00 77.88  ? 20  LYS B CE  1 
ATOM   1339 N NZ  . LYS B 2 23  ? 28.390 -1.449  93.925  1.00 71.15  ? 20  LYS B NZ  1 
ATOM   1340 N N   . VAL B 2 24  ? 32.239 -0.124  98.714  1.00 44.81  ? 21  VAL B N   1 
ATOM   1341 C CA  . VAL B 2 24  ? 33.639 -0.059  98.338  1.00 44.07  ? 21  VAL B CA  1 
ATOM   1342 C C   . VAL B 2 24  ? 34.463 -1.122  99.091  1.00 41.97  ? 21  VAL B C   1 
ATOM   1343 O O   . VAL B 2 24  ? 35.171 -1.893  98.491  1.00 44.16  ? 21  VAL B O   1 
ATOM   1344 C CB  . VAL B 2 24  ? 34.192 1.369   98.617  1.00 38.76  ? 21  VAL B CB  1 
ATOM   1345 C CG1 . VAL B 2 24  ? 35.649 1.356   98.835  1.00 43.91  ? 21  VAL B CG1 1 
ATOM   1346 C CG2 . VAL B 2 24  ? 33.866 2.296   97.483  1.00 41.88  ? 21  VAL B CG2 1 
ATOM   1347 N N   . LYS B 2 25  ? 34.355 -1.167  100.401 1.00 42.63  ? 22  LYS B N   1 
ATOM   1348 C CA  . LYS B 2 25  ? 35.081 -2.138  101.192 1.00 44.80  ? 22  LYS B CA  1 
ATOM   1349 C C   . LYS B 2 25  ? 34.776 -3.527  100.725 1.00 45.26  ? 22  LYS B C   1 
ATOM   1350 O O   . LYS B 2 25  ? 35.652 -4.390  100.627 1.00 47.45  ? 22  LYS B O   1 
ATOM   1351 C CB  . LYS B 2 25  ? 34.735 -2.010  102.660 1.00 46.18  ? 22  LYS B CB  1 
ATOM   1352 C CG  . LYS B 2 25  ? 35.513 -0.908  103.368 1.00 54.51  ? 22  LYS B CG  1 
ATOM   1353 C CD  . LYS B 2 25  ? 35.126 -0.790  104.862 1.00 64.38  ? 22  LYS B CD  1 
ATOM   1354 C CE  . LYS B 2 25  ? 35.610 -2.015  105.653 1.00 72.81  ? 22  LYS B CE  1 
ATOM   1355 N NZ  . LYS B 2 25  ? 36.154 -1.760  107.031 1.00 79.99  ? 22  LYS B NZ  1 
ATOM   1356 N N   . ASP B 2 26  ? 33.522 -3.727  100.407 1.00 45.10  ? 23  ASP B N   1 
ATOM   1357 C CA  . ASP B 2 26  ? 33.008 -5.041  100.137 1.00 49.88  ? 23  ASP B CA  1 
ATOM   1358 C C   . ASP B 2 26  ? 33.391 -5.508  98.716  1.00 50.94  ? 23  ASP B C   1 
ATOM   1359 O O   . ASP B 2 26  ? 33.837 -6.607  98.520  1.00 51.70  ? 23  ASP B O   1 
ATOM   1360 C CB  . ASP B 2 26  ? 31.490 -5.028  100.342 1.00 52.88  ? 23  ASP B CB  1 
ATOM   1361 C CG  . ASP B 2 26  ? 30.949 -6.398  100.584 1.00 67.30  ? 23  ASP B CG  1 
ATOM   1362 O OD1 . ASP B 2 26  ? 31.255 -6.962  101.679 1.00 77.79  ? 23  ASP B OD1 1 
ATOM   1363 O OD2 . ASP B 2 26  ? 30.294 -6.918  99.646  1.00 59.33  ? 23  ASP B OD2 1 
ATOM   1364 N N   . ASP B 2 27  ? 33.226 -4.632  97.741  1.00 50.91  ? 24  ASP B N   1 
ATOM   1365 C CA  . ASP B 2 27  ? 33.723 -4.860  96.429  1.00 43.54  ? 24  ASP B CA  1 
ATOM   1366 C C   . ASP B 2 27  ? 35.212 -5.177  96.339  1.00 44.01  ? 24  ASP B C   1 
ATOM   1367 O O   . ASP B 2 27  ? 35.585 -6.053  95.564  1.00 47.21  ? 24  ASP B O   1 
ATOM   1368 C CB  . ASP B 2 27  ? 33.372 -3.699  95.554  1.00 42.60  ? 24  ASP B CB  1 
ATOM   1369 C CG  . ASP B 2 27  ? 31.890 -3.673  95.247  1.00 47.75  ? 24  ASP B CG  1 
ATOM   1370 O OD1 . ASP B 2 27  ? 31.193 -4.591  95.688  1.00 49.67  ? 24  ASP B OD1 1 
ATOM   1371 O OD2 . ASP B 2 27  ? 31.410 -2.759  94.558  1.00 56.05  ? 24  ASP B OD2 1 
ATOM   1372 N N   . LEU B 2 28  ? 36.042 -4.528  97.143  1.00 40.37  ? 25  LEU B N   1 
ATOM   1373 C CA  . LEU B 2 28  ? 37.471 -4.737  97.061  1.00 34.90  ? 25  LEU B CA  1 
ATOM   1374 C C   . LEU B 2 28  ? 37.738 -6.111  97.625  1.00 37.11  ? 25  LEU B C   1 
ATOM   1375 O O   . LEU B 2 28  ? 38.572 -6.877  97.123  1.00 37.73  ? 25  LEU B O   1 
ATOM   1376 C CB  . LEU B 2 28  ? 38.274 -3.639  97.770  1.00 34.24  ? 25  LEU B CB  1 
ATOM   1377 C CG  . LEU B 2 28  ? 39.780 -3.902  97.866  1.00 37.56  ? 25  LEU B CG  1 
ATOM   1378 C CD1 . LEU B 2 28  ? 40.352 -4.044  96.466  1.00 40.22  ? 25  LEU B CD1 1 
ATOM   1379 C CD2 . LEU B 2 28  ? 40.503 -2.817  98.586  1.00 38.47  ? 25  LEU B CD2 1 
ATOM   1380 N N   . LYS B 2 29  ? 36.977 -6.496  98.607  1.00 39.18  ? 26  LYS B N   1 
ATOM   1381 C CA  . LYS B 2 29  ? 37.228 -7.781  99.197  1.00 43.31  ? 26  LYS B CA  1 
ATOM   1382 C C   . LYS B 2 29  ? 36.831 -8.861  98.214  1.00 47.33  ? 26  LYS B C   1 
ATOM   1383 O O   . LYS B 2 29  ? 37.545 -9.823  98.033  1.00 41.93  ? 26  LYS B O   1 
ATOM   1384 C CB  . LYS B 2 29  ? 36.424 -7.908  100.438 1.00 48.63  ? 26  LYS B CB  1 
ATOM   1385 C CG  . LYS B 2 29  ? 36.636 -9.171  101.191 1.00 52.65  ? 26  LYS B CG  1 
ATOM   1386 C CD  . LYS B 2 29  ? 35.317 -9.572  101.782 1.00 60.73  ? 26  LYS B CD  1 
ATOM   1387 C CE  . LYS B 2 29  ? 35.280 -9.309  103.256 1.00 62.53  ? 26  LYS B CE  1 
ATOM   1388 N NZ  . LYS B 2 29  ? 33.859 -9.476  103.632 1.00 62.89  ? 26  LYS B NZ  1 
ATOM   1389 N N   . LYS B 2 30  ? 35.698 -8.690  97.565  1.00 48.29  ? 27  LYS B N   1 
ATOM   1390 C CA  . LYS B 2 30  ? 35.276 -9.651  96.566  1.00 54.75  ? 27  LYS B CA  1 
ATOM   1391 C C   . LYS B 2 30  ? 36.369 -9.807  95.534  1.00 49.49  ? 27  LYS B C   1 
ATOM   1392 O O   . LYS B 2 30  ? 36.683 -10.907 95.164  1.00 54.64  ? 27  LYS B O   1 
ATOM   1393 C CB  . LYS B 2 30  ? 33.968 -9.237  95.867  1.00 62.91  ? 27  LYS B CB  1 
ATOM   1394 C CG  . LYS B 2 30  ? 32.702 -9.862  96.442  1.00 77.99  ? 27  LYS B CG  1 
ATOM   1395 C CD  . LYS B 2 30  ? 32.410 -11.218 95.791  1.00 101.90 ? 27  LYS B CD  1 
ATOM   1396 C CE  . LYS B 2 30  ? 31.781 -11.067 94.402  1.00 107.51 ? 27  LYS B CE  1 
ATOM   1397 N NZ  . LYS B 2 30  ? 30.400 -10.498 94.467  1.00 106.72 ? 27  LYS B NZ  1 
ATOM   1398 N N   . MET B 2 31  ? 36.930 -8.706  95.066  1.00 46.44  ? 28  MET B N   1 
ATOM   1399 C CA  . MET B 2 31  ? 38.019 -8.787  94.133  1.00 49.43  ? 28  MET B CA  1 
ATOM   1400 C C   . MET B 2 31  ? 39.231 -9.536  94.672  1.00 45.67  ? 28  MET B C   1 
ATOM   1401 O O   . MET B 2 31  ? 39.797 -10.345 93.994  1.00 51.69  ? 28  MET B O   1 
ATOM   1402 C CB  . MET B 2 31  ? 38.395 -7.429  93.585  1.00 51.40  ? 28  MET B CB  1 
ATOM   1403 C CG  . MET B 2 31  ? 37.640 -7.177  92.280  1.00 62.92  ? 28  MET B CG  1 
ATOM   1404 S SD  . MET B 2 31  ? 38.346 -5.771  91.411  1.00 76.81  ? 28  MET B SD  1 
ATOM   1405 C CE  . MET B 2 31  ? 40.090 -6.112  91.323  1.00 60.65  ? 28  MET B CE  1 
ATOM   1406 N N   . PHE B 2 32  ? 39.614 -9.321  95.903  1.00 40.16  ? 29  PHE B N   1 
ATOM   1407 C CA  . PHE B 2 32  ? 40.682 -10.097 96.390  1.00 38.53  ? 29  PHE B CA  1 
ATOM   1408 C C   . PHE B 2 32  ? 40.324 -11.597 96.272  1.00 43.20  ? 29  PHE B C   1 
ATOM   1409 O O   . PHE B 2 32  ? 41.151 -12.384 95.822  1.00 46.77  ? 29  PHE B O   1 
ATOM   1410 C CB  . PHE B 2 32  ? 41.042 -9.711  97.826  1.00 34.77  ? 29  PHE B CB  1 
ATOM   1411 C CG  . PHE B 2 32  ? 41.791 -8.398  97.952  1.00 34.44  ? 29  PHE B CG  1 
ATOM   1412 C CD1 . PHE B 2 32  ? 42.773 -8.046  97.074  1.00 37.17  ? 29  PHE B CD1 1 
ATOM   1413 C CD2 . PHE B 2 32  ? 41.523 -7.537  98.975  1.00 35.05  ? 29  PHE B CD2 1 
ATOM   1414 C CE1 . PHE B 2 32  ? 43.477 -6.884  97.205  1.00 35.25  ? 29  PHE B CE1 1 
ATOM   1415 C CE2 . PHE B 2 32  ? 42.235 -6.378  99.140  1.00 35.32  ? 29  PHE B CE2 1 
ATOM   1416 C CZ  . PHE B 2 32  ? 43.212 -6.038  98.252  1.00 34.74  ? 29  PHE B CZ  1 
ATOM   1417 N N   . LYS B 2 33  ? 39.108 -11.982 96.655  1.00 46.68  ? 30  LYS B N   1 
ATOM   1418 C CA  . LYS B 2 33  ? 38.721 -13.385 96.790  1.00 49.47  ? 30  LYS B CA  1 
ATOM   1419 C C   . LYS B 2 33  ? 38.600 -14.041 95.441  1.00 44.65  ? 30  LYS B C   1 
ATOM   1420 O O   . LYS B 2 33  ? 38.963 -15.187 95.258  1.00 46.63  ? 30  LYS B O   1 
ATOM   1421 C CB  . LYS B 2 33  ? 37.400 -13.549 97.557  1.00 58.22  ? 30  LYS B CB  1 
ATOM   1422 C CG  . LYS B 2 33  ? 37.525 -13.446 99.079  1.00 69.62  ? 30  LYS B CG  1 
ATOM   1423 C CD  . LYS B 2 33  ? 36.320 -14.062 99.799  1.00 78.92  ? 30  LYS B CD  1 
ATOM   1424 C CE  . LYS B 2 33  ? 35.988 -13.357 101.122 1.00 79.65  ? 30  LYS B CE  1 
ATOM   1425 N NZ  . LYS B 2 33  ? 36.994 -13.613 102.184 1.00 78.42  ? 30  LYS B NZ  1 
ATOM   1426 N N   . GLN B 2 34  ? 38.079 -13.308 94.497  1.00 44.47  ? 31  GLN B N   1 
ATOM   1427 C CA  . GLN B 2 34  ? 38.018 -13.788 93.142  1.00 49.87  ? 31  GLN B CA  1 
ATOM   1428 C C   . GLN B 2 34  ? 39.399 -14.162 92.649  1.00 47.51  ? 31  GLN B C   1 
ATOM   1429 O O   . GLN B 2 34  ? 39.503 -14.991 91.814  1.00 49.79  ? 31  GLN B O   1 
ATOM   1430 C CB  . GLN B 2 34  ? 37.518 -12.702 92.198  1.00 54.14  ? 31  GLN B CB  1 
ATOM   1431 C CG  . GLN B 2 34  ? 36.055 -12.742 91.883  1.00 72.47  ? 31  GLN B CG  1 
ATOM   1432 C CD  . GLN B 2 34  ? 35.682 -11.669 90.847  1.00 91.86  ? 31  GLN B CD  1 
ATOM   1433 O OE1 . GLN B 2 34  ? 36.559 -10.981 90.275  1.00 88.44  ? 31  GLN B OE1 1 
ATOM   1434 N NE2 . GLN B 2 34  ? 34.371 -11.507 90.614  1.00 92.32  ? 31  GLN B NE2 1 
ATOM   1435 N N   . ASN B 2 35  ? 40.433 -13.451 93.071  1.00 43.79  ? 32  ASN B N   1 
ATOM   1436 C CA  . ASN B 2 35  ? 41.771 -13.686 92.584  1.00 40.52  ? 32  ASN B CA  1 
ATOM   1437 C C   . ASN B 2 35  ? 42.529 -14.690 93.422  1.00 41.16  ? 32  ASN B C   1 
ATOM   1438 O O   . ASN B 2 35  ? 43.728 -14.839 93.211  1.00 40.10  ? 32  ASN B O   1 
ATOM   1439 C CB  . ASN B 2 35  ? 42.554 -12.378 92.588  1.00 39.65  ? 32  ASN B CB  1 
ATOM   1440 C CG  . ASN B 2 35  ? 42.223 -11.518 91.410  1.00 45.73  ? 32  ASN B CG  1 
ATOM   1441 O OD1 . ASN B 2 35  ? 42.900 -11.544 90.408  1.00 52.02  ? 32  ASN B OD1 1 
ATOM   1442 N ND2 . ASN B 2 35  ? 41.160 -10.787 91.508  1.00 47.93  ? 32  ASN B ND2 1 
ATOM   1443 N N   . GLY B 2 36  ? 41.880 -15.283 94.442  1.00 38.37  ? 33  GLY B N   1 
ATOM   1444 C CA  . GLY B 2 36  ? 42.509 -16.299 95.303  1.00 36.56  ? 33  GLY B CA  1 
ATOM   1445 C C   . GLY B 2 36  ? 43.009 -15.807 96.628  1.00 42.18  ? 33  GLY B C   1 
ATOM   1446 O O   . GLY B 2 36  ? 43.614 -16.550 97.401  1.00 37.74  ? 33  GLY B O   1 
ATOM   1447 N N   . TYR B 2 37  ? 42.756 -14.547 96.944  1.00 48.31  ? 34  TYR B N   1 
ATOM   1448 C CA  . TYR B 2 37  ? 43.355 -14.011 98.167  1.00 42.71  ? 34  TYR B CA  1 
ATOM   1449 C C   . TYR B 2 37  ? 42.217 -13.842 99.111  1.00 45.58  ? 34  TYR B C   1 
ATOM   1450 O O   . TYR B 2 37  ? 41.210 -13.169 98.820  1.00 46.25  ? 34  TYR B O   1 
ATOM   1451 C CB  . TYR B 2 37  ? 44.095 -12.725 97.917  1.00 39.83  ? 34  TYR B CB  1 
ATOM   1452 C CG  . TYR B 2 37  ? 45.239 -12.858 96.958  1.00 34.24  ? 34  TYR B CG  1 
ATOM   1453 C CD1 . TYR B 2 37  ? 46.423 -13.338 97.372  1.00 35.03  ? 34  TYR B CD1 1 
ATOM   1454 C CD2 . TYR B 2 37  ? 45.121 -12.509 95.628  1.00 35.98  ? 34  TYR B CD2 1 
ATOM   1455 C CE1 . TYR B 2 37  ? 47.518 -13.474 96.526  1.00 31.98  ? 34  TYR B CE1 1 
ATOM   1456 C CE2 . TYR B 2 37  ? 46.197 -12.637 94.764  1.00 36.88  ? 34  TYR B CE2 1 
ATOM   1457 C CZ  . TYR B 2 37  ? 47.410 -13.151 95.241  1.00 34.85  ? 34  TYR B CZ  1 
ATOM   1458 O OH  . TYR B 2 37  ? 48.558 -13.275 94.453  1.00 37.86  ? 34  TYR B OH  1 
ATOM   1459 N N   . ASP B 2 38  ? 42.349 -14.544 100.230 1.00 48.98  ? 35  ASP B N   1 
ATOM   1460 C CA  . ASP B 2 38  ? 41.286 -14.617 101.165 1.00 48.52  ? 35  ASP B CA  1 
ATOM   1461 C C   . ASP B 2 38  ? 41.576 -13.605 102.244 1.00 49.57  ? 35  ASP B C   1 
ATOM   1462 O O   . ASP B 2 38  ? 41.954 -13.955 103.348 1.00 48.85  ? 35  ASP B O   1 
ATOM   1463 C CB  . ASP B 2 38  ? 41.282 -15.998 101.734 1.00 53.94  ? 35  ASP B CB  1 
ATOM   1464 C CG  . ASP B 2 38  ? 40.088 -16.251 102.566 1.00 62.60  ? 35  ASP B CG  1 
ATOM   1465 O OD1 . ASP B 2 38  ? 39.036 -15.577 102.382 1.00 72.32  ? 35  ASP B OD1 1 
ATOM   1466 O OD2 . ASP B 2 38  ? 40.230 -17.123 103.414 1.00 58.45  ? 35  ASP B OD2 1 
ATOM   1467 N N   . ILE B 2 39  ? 41.497 -12.331 101.896 1.00 48.16  ? 36  ILE B N   1 
ATOM   1468 C CA  . ILE B 2 39  ? 41.822 -11.311 102.844 1.00 44.96  ? 36  ILE B CA  1 
ATOM   1469 C C   . ILE B 2 39  ? 40.737 -10.268 102.825 1.00 48.88  ? 36  ILE B C   1 
ATOM   1470 O O   . ILE B 2 39  ? 39.918 -10.235 101.903 1.00 51.01  ? 36  ILE B O   1 
ATOM   1471 C CB  . ILE B 2 39  ? 43.186 -10.676 102.578 1.00 46.50  ? 36  ILE B CB  1 
ATOM   1472 C CG1 . ILE B 2 39  ? 43.102 -9.722  101.430 1.00 48.03  ? 36  ILE B CG1 1 
ATOM   1473 C CG2 . ILE B 2 39  ? 44.303 -11.708 102.330 1.00 45.55  ? 36  ILE B CG2 1 
ATOM   1474 C CD1 . ILE B 2 39  ? 44.381 -8.944  101.323 1.00 49.80  ? 36  ILE B CD1 1 
ATOM   1475 N N   . THR B 2 40  ? 40.744 -9.410  103.836 1.00 43.83  ? 37  THR B N   1 
ATOM   1476 C CA  . THR B 2 40  ? 39.820 -8.309  103.878 1.00 43.67  ? 37  THR B CA  1 
ATOM   1477 C C   . THR B 2 40  ? 40.503 -7.007  103.584 1.00 42.19  ? 37  THR B C   1 
ATOM   1478 O O   . THR B 2 40  ? 41.747 -6.866  103.596 1.00 43.45  ? 37  THR B O   1 
ATOM   1479 C CB  . THR B 2 40  ? 39.219 -8.191  105.263 1.00 47.50  ? 37  THR B CB  1 
ATOM   1480 O OG1 . THR B 2 40  ? 40.279 -7.984  106.203 1.00 50.91  ? 37  THR B OG1 1 
ATOM   1481 C CG2 . THR B 2 40  ? 38.504 -9.491  105.610 1.00 52.06  ? 37  THR B CG2 1 
ATOM   1482 N N   . THR B 2 41  ? 39.665 -6.014  103.398 1.00 38.33  ? 38  THR B N   1 
ATOM   1483 C CA  . THR B 2 41  ? 40.140 -4.674  103.304 1.00 40.86  ? 38  THR B CA  1 
ATOM   1484 C C   . THR B 2 41  ? 40.944 -4.214  104.511 1.00 39.41  ? 38  THR B C   1 
ATOM   1485 O O   . THR B 2 41  ? 41.995 -3.588  104.348 1.00 44.86  ? 38  THR B O   1 
ATOM   1486 C CB  . THR B 2 41  ? 38.959 -3.784  103.039 1.00 44.47  ? 38  THR B CB  1 
ATOM   1487 O OG1 . THR B 2 41  ? 38.532 -4.060  101.691 1.00 49.54  ? 38  THR B OG1 1 
ATOM   1488 C CG2 . THR B 2 41  ? 39.357 -2.382  103.136 1.00 56.70  ? 38  THR B CG2 1 
ATOM   1489 N N   . ASP B 2 42  ? 40.481 -4.534  105.716 1.00 39.47  ? 39  ASP B N   1 
ATOM   1490 C CA  . ASP B 2 42  ? 41.242 -4.244  106.918 1.00 39.82  ? 39  ASP B CA  1 
ATOM   1491 C C   . ASP B 2 42  ? 42.613 -4.856  106.822 1.00 37.47  ? 39  ASP B C   1 
ATOM   1492 O O   . ASP B 2 42  ? 43.567 -4.199  107.113 1.00 42.87  ? 39  ASP B O   1 
ATOM   1493 C CB  . ASP B 2 42  ? 40.551 -4.773  108.180 1.00 51.66  ? 39  ASP B CB  1 
ATOM   1494 C CG  . ASP B 2 42  ? 39.098 -4.244  108.368 1.00 55.71  ? 39  ASP B CG  1 
ATOM   1495 O OD1 . ASP B 2 42  ? 38.769 -3.126  107.894 1.00 54.02  ? 39  ASP B OD1 1 
ATOM   1496 O OD2 . ASP B 2 42  ? 38.291 -4.985  109.002 1.00 56.90  ? 39  ASP B OD2 1 
ATOM   1497 N N   . HIS B 2 43  ? 42.731 -6.110  106.388 1.00 37.29  ? 40  HIS B N   1 
ATOM   1498 C CA  . HIS B 2 43  ? 44.028 -6.736  106.283 1.00 37.36  ? 40  HIS B CA  1 
ATOM   1499 C C   . HIS B 2 43  ? 44.924 -5.979  105.324 1.00 40.04  ? 40  HIS B C   1 
ATOM   1500 O O   . HIS B 2 43  ? 46.127 -5.802  105.596 1.00 37.01  ? 40  HIS B O   1 
ATOM   1501 C CB  . HIS B 2 43  ? 43.915 -8.172  105.810 1.00 38.34  ? 40  HIS B CB  1 
ATOM   1502 C CG  . HIS B 2 43  ? 43.031 -9.021  106.662 1.00 46.39  ? 40  HIS B CG  1 
ATOM   1503 N ND1 . HIS B 2 43  ? 42.389 -10.142 106.188 1.00 52.43  ? 40  HIS B ND1 1 
ATOM   1504 C CD2 . HIS B 2 43  ? 42.684 -8.920  107.962 1.00 48.21  ? 40  HIS B CD2 1 
ATOM   1505 C CE1 . HIS B 2 43  ? 41.684 -10.689 107.156 1.00 50.84  ? 40  HIS B CE1 1 
ATOM   1506 N NE2 . HIS B 2 43  ? 41.836 -9.959  108.239 1.00 47.31  ? 40  HIS B NE2 1 
ATOM   1507 N N   . TYR B 2 44  ? 44.332 -5.528  104.206 1.00 39.34  ? 41  TYR B N   1 
ATOM   1508 C CA  . TYR B 2 44  ? 45.084 -4.793  103.165 1.00 37.36  ? 41  TYR B CA  1 
ATOM   1509 C C   . TYR B 2 44  ? 45.570 -3.470  103.734 1.00 40.87  ? 41  TYR B C   1 
ATOM   1510 O O   . TYR B 2 44  ? 46.761 -3.161  103.674 1.00 42.36  ? 41  TYR B O   1 
ATOM   1511 C CB  . TYR B 2 44  ? 44.257 -4.642  101.894 1.00 35.36  ? 41  TYR B CB  1 
ATOM   1512 C CG  . TYR B 2 44  ? 44.905 -3.850  100.818 1.00 34.18  ? 41  TYR B CG  1 
ATOM   1513 C CD1 . TYR B 2 44  ? 46.080 -4.264  100.278 1.00 37.41  ? 41  TYR B CD1 1 
ATOM   1514 C CD2 . TYR B 2 44  ? 44.328 -2.700  100.341 1.00 34.80  ? 41  TYR B CD2 1 
ATOM   1515 C CE1 . TYR B 2 44  ? 46.707 -3.549  99.307  1.00 41.28  ? 41  TYR B CE1 1 
ATOM   1516 C CE2 . TYR B 2 44  ? 44.922 -1.955  99.341  1.00 40.19  ? 41  TYR B CE2 1 
ATOM   1517 C CZ  . TYR B 2 44  ? 46.121 -2.384  98.817  1.00 43.45  ? 41  TYR B CZ  1 
ATOM   1518 O OH  . TYR B 2 44  ? 46.789 -1.656  97.848  1.00 42.53  ? 41  TYR B OH  1 
ATOM   1519 N N   . ALA B 2 45  ? 44.692 -2.751  104.417 1.00 41.17  ? 42  ALA B N   1 
ATOM   1520 C CA  . ALA B 2 45  ? 45.123 -1.495  105.050 1.00 41.35  ? 42  ALA B CA  1 
ATOM   1521 C C   . ALA B 2 45  ? 46.246 -1.674  106.062 1.00 40.87  ? 42  ALA B C   1 
ATOM   1522 O O   . ALA B 2 45  ? 47.243 -1.010  105.998 1.00 50.79  ? 42  ALA B O   1 
ATOM   1523 C CB  . ALA B 2 45  ? 43.956 -0.797  105.669 1.00 40.44  ? 42  ALA B CB  1 
ATOM   1524 N N   . LEU B 2 46  ? 46.160 -2.642  106.941 1.00 44.18  ? 43  LEU B N   1 
ATOM   1525 C CA  . LEU B 2 46  ? 47.282 -2.878  107.855 1.00 40.50  ? 43  LEU B CA  1 
ATOM   1526 C C   . LEU B 2 46  ? 48.551 -3.297  107.130 1.00 42.21  ? 43  LEU B C   1 
ATOM   1527 O O   . LEU B 2 46  ? 49.646 -2.874  107.499 1.00 42.16  ? 43  LEU B O   1 
ATOM   1528 C CB  . LEU B 2 46  ? 46.892 -3.939  108.873 1.00 41.21  ? 43  LEU B CB  1 
ATOM   1529 C CG  . LEU B 2 46  ? 46.212 -3.487  110.180 1.00 42.82  ? 43  LEU B CG  1 
ATOM   1530 C CD1 . LEU B 2 46  ? 45.885 -1.990  110.321 1.00 42.51  ? 43  LEU B CD1 1 
ATOM   1531 C CD2 . LEU B 2 46  ? 44.988 -4.312  110.395 1.00 40.43  ? 43  LEU B CD2 1 
ATOM   1532 N N   . LEU B 2 47  ? 48.435 -4.136  106.102 1.00 41.69  ? 44  LEU B N   1 
ATOM   1533 C CA  . LEU B 2 47  ? 49.623 -4.497  105.373 1.00 41.12  ? 44  LEU B CA  1 
ATOM   1534 C C   . LEU B 2 47  ? 50.264 -3.258  104.758 1.00 40.26  ? 44  LEU B C   1 
ATOM   1535 O O   . LEU B 2 47  ? 51.487 -3.085  104.832 1.00 41.73  ? 44  LEU B O   1 
ATOM   1536 C CB  . LEU B 2 47  ? 49.327 -5.527  104.286 1.00 42.19  ? 44  LEU B CB  1 
ATOM   1537 C CG  . LEU B 2 47  ? 49.101 -6.962  104.778 1.00 40.53  ? 44  LEU B CG  1 
ATOM   1538 C CD1 . LEU B 2 47  ? 48.521 -7.841  103.695 1.00 39.46  ? 44  LEU B CD1 1 
ATOM   1539 C CD2 . LEU B 2 47  ? 50.380 -7.574  105.281 1.00 41.91  ? 44  LEU B CD2 1 
ATOM   1540 N N   . ARG B 2 48  ? 49.445 -2.387  104.164 1.00 40.78  ? 45  ARG B N   1 
ATOM   1541 C CA  . ARG B 2 48  ? 49.983 -1.137  103.570 1.00 42.13  ? 45  ARG B CA  1 
ATOM   1542 C C   . ARG B 2 48  ? 50.934 -0.422  104.496 1.00 43.52  ? 45  ARG B C   1 
ATOM   1543 O O   . ARG B 2 48  ? 51.949 0.093   104.014 1.00 41.24  ? 45  ARG B O   1 
ATOM   1544 C CB  . ARG B 2 48  ? 48.905 -0.144  103.244 1.00 41.49  ? 45  ARG B CB  1 
ATOM   1545 C CG  . ARG B 2 48  ? 47.998 -0.540  102.113 1.00 46.25  ? 45  ARG B CG  1 
ATOM   1546 C CD  . ARG B 2 48  ? 48.604 -0.233  100.793 1.00 47.45  ? 45  ARG B CD  1 
ATOM   1547 N NE  . ARG B 2 48  ? 48.664 1.210   100.551 1.00 48.76  ? 45  ARG B NE  1 
ATOM   1548 C CZ  . ARG B 2 48  ? 49.110 1.757   99.414  1.00 46.30  ? 45  ARG B CZ  1 
ATOM   1549 N NH1 . ARG B 2 48  ? 49.545 1.022   98.389  1.00 46.86  ? 45  ARG B NH1 1 
ATOM   1550 N NH2 . ARG B 2 48  ? 49.114 3.061   99.296  1.00 51.20  ? 45  ARG B NH2 1 
ATOM   1551 N N   . PHE B 2 49  ? 50.589 -0.381  105.807 1.00 40.49  ? 46  PHE B N   1 
ATOM   1552 C CA  . PHE B 2 49  ? 51.387 0.333   106.794 1.00 37.67  ? 46  PHE B CA  1 
ATOM   1553 C C   . PHE B 2 49  ? 52.683 -0.357  106.907 1.00 39.72  ? 46  PHE B C   1 
ATOM   1554 O O   . PHE B 2 49  ? 53.713 0.297   106.876 1.00 47.49  ? 46  PHE B O   1 
ATOM   1555 C CB  . PHE B 2 49  ? 50.729 0.467   108.193 1.00 38.27  ? 46  PHE B CB  1 
ATOM   1556 C CG  . PHE B 2 49  ? 49.487 1.305   108.222 1.00 33.97  ? 46  PHE B CG  1 
ATOM   1557 C CD1 . PHE B 2 49  ? 49.443 2.554   107.618 1.00 42.01  ? 46  PHE B CD1 1 
ATOM   1558 C CD2 . PHE B 2 49  ? 48.371 0.879   108.874 1.00 36.02  ? 46  PHE B CD2 1 
ATOM   1559 C CE1 . PHE B 2 49  ? 48.282 3.351   107.626 1.00 38.18  ? 46  PHE B CE1 1 
ATOM   1560 C CE2 . PHE B 2 49  ? 47.188 1.676   108.900 1.00 40.16  ? 46  PHE B CE2 1 
ATOM   1561 C CZ  . PHE B 2 49  ? 47.150 2.914   108.261 1.00 36.97  ? 46  PHE B CZ  1 
ATOM   1562 N N   . LEU B 2 50  ? 52.663 -1.677  107.007 1.00 43.09  ? 47  LEU B N   1 
ATOM   1563 C CA  . LEU B 2 50  ? 53.908 -2.411  107.286 1.00 43.60  ? 47  LEU B CA  1 
ATOM   1564 C C   . LEU B 2 50  ? 54.821 -2.484  106.099 1.00 46.42  ? 47  LEU B C   1 
ATOM   1565 O O   . LEU B 2 50  ? 56.035 -2.651  106.262 1.00 49.73  ? 47  LEU B O   1 
ATOM   1566 C CB  . LEU B 2 50  ? 53.612 -3.847  107.765 1.00 49.78  ? 47  LEU B CB  1 
ATOM   1567 C CG  . LEU B 2 50  ? 52.782 -3.941  109.065 1.00 51.23  ? 47  LEU B CG  1 
ATOM   1568 C CD1 . LEU B 2 50  ? 52.091 -5.285  109.279 1.00 47.56  ? 47  LEU B CD1 1 
ATOM   1569 C CD2 . LEU B 2 50  ? 53.646 -3.593  110.257 1.00 53.06  ? 47  LEU B CD2 1 
ATOM   1570 N N   . TRP B 2 51  ? 54.266 -2.445  104.886 1.00 45.71  ? 48  TRP B N   1 
ATOM   1571 C CA  . TRP B 2 51  ? 55.131 -2.366  103.706 1.00 44.27  ? 48  TRP B CA  1 
ATOM   1572 C C   . TRP B 2 51  ? 55.940 -1.065  103.695 1.00 44.79  ? 48  TRP B C   1 
ATOM   1573 O O   . TRP B 2 51  ? 57.002 -1.045  103.140 1.00 44.79  ? 48  TRP B O   1 
ATOM   1574 C CB  . TRP B 2 51  ? 54.340 -2.522  102.385 1.00 49.12  ? 48  TRP B CB  1 
ATOM   1575 C CG  . TRP B 2 51  ? 53.688 -3.899  102.204 1.00 49.22  ? 48  TRP B CG  1 
ATOM   1576 C CD1 . TRP B 2 51  ? 54.217 -5.102  102.552 1.00 47.43  ? 48  TRP B CD1 1 
ATOM   1577 C CD2 . TRP B 2 51  ? 52.404 -4.178  101.674 1.00 43.30  ? 48  TRP B CD2 1 
ATOM   1578 N NE1 . TRP B 2 51  ? 53.359 -6.108  102.264 1.00 41.25  ? 48  TRP B NE1 1 
ATOM   1579 C CE2 . TRP B 2 51  ? 52.237 -5.578  101.704 1.00 42.26  ? 48  TRP B CE2 1 
ATOM   1580 C CE3 . TRP B 2 51  ? 51.399 -3.398  101.147 1.00 40.37  ? 48  TRP B CE3 1 
ATOM   1581 C CZ2 . TRP B 2 51  ? 51.090 -6.207  101.255 1.00 38.23  ? 48  TRP B CZ2 1 
ATOM   1582 C CZ3 . TRP B 2 51  ? 50.265 -4.013  100.697 1.00 41.47  ? 48  TRP B CZ3 1 
ATOM   1583 C CH2 . TRP B 2 51  ? 50.110 -5.419  100.773 1.00 39.35  ? 48  TRP B CH2 1 
ATOM   1584 N N   . GLU B 2 52  ? 55.417 0.003   104.304 1.00 54.17  ? 49  GLU B N   1 
ATOM   1585 C CA  . GLU B 2 52  ? 56.083 1.304   104.441 1.00 57.82  ? 49  GLU B CA  1 
ATOM   1586 C C   . GLU B 2 52  ? 57.163 1.235   105.494 1.00 52.63  ? 49  GLU B C   1 
ATOM   1587 O O   . GLU B 2 52  ? 58.303 1.537   105.228 1.00 56.22  ? 49  GLU B O   1 
ATOM   1588 C CB  . GLU B 2 52  ? 55.069 2.410   104.840 1.00 71.23  ? 49  GLU B CB  1 
ATOM   1589 C CG  . GLU B 2 52  ? 54.690 3.378   103.728 1.00 79.97  ? 49  GLU B CG  1 
ATOM   1590 C CD  . GLU B 2 52  ? 55.894 4.154   103.189 1.00 88.39  ? 49  GLU B CD  1 
ATOM   1591 O OE1 . GLU B 2 52  ? 56.674 4.697   104.009 1.00 79.11  ? 49  GLU B OE1 1 
ATOM   1592 O OE2 . GLU B 2 52  ? 56.070 4.222   101.944 1.00 87.68  ? 49  GLU B OE2 1 
ATOM   1593 N N   . GLN B 2 53  ? 56.781 0.793   106.677 1.00 58.95  ? 50  GLN B N   1 
ATOM   1594 C CA  . GLN B 2 53  ? 57.666 0.626   107.803 1.00 60.24  ? 50  GLN B CA  1 
ATOM   1595 C C   . GLN B 2 53  ? 57.362 -0.694  108.516 1.00 53.37  ? 50  GLN B C   1 
ATOM   1596 O O   . GLN B 2 53  ? 56.365 -0.802  109.221 1.00 54.57  ? 50  GLN B O   1 
ATOM   1597 C CB  . GLN B 2 53  ? 57.465 1.811   108.772 1.00 74.60  ? 50  GLN B CB  1 
ATOM   1598 C CG  . GLN B 2 53  ? 58.532 1.933   109.859 1.00 85.67  ? 50  GLN B CG  1 
ATOM   1599 C CD  . GLN B 2 53  ? 59.955 1.936   109.262 1.00 106.69 ? 50  GLN B CD  1 
ATOM   1600 O OE1 . GLN B 2 53  ? 60.759 1.023   109.525 1.00 98.84  ? 50  GLN B OE1 1 
ATOM   1601 N NE2 . GLN B 2 53  ? 60.258 2.950   108.417 1.00 104.10 ? 50  GLN B NE2 1 
ATOM   1602 N N   . ASP B 2 54  ? 58.235 -1.677  108.332 1.00 52.37  ? 51  ASP B N   1 
ATOM   1603 C CA  . ASP B 2 54  ? 58.168 -2.982  108.994 1.00 54.67  ? 51  ASP B CA  1 
ATOM   1604 C C   . ASP B 2 54  ? 58.422 -2.791  110.472 1.00 58.16  ? 51  ASP B C   1 
ATOM   1605 O O   . ASP B 2 54  ? 58.992 -1.820  110.860 1.00 62.89  ? 51  ASP B O   1 
ATOM   1606 C CB  . ASP B 2 54  ? 59.227 -3.952  108.394 1.00 56.99  ? 51  ASP B CB  1 
ATOM   1607 C CG  . ASP B 2 54  ? 58.857 -5.463  108.589 1.00 69.01  ? 51  ASP B CG  1 
ATOM   1608 O OD1 . ASP B 2 54  ? 57.943 -5.730  109.402 1.00 63.04  ? 51  ASP B OD1 1 
ATOM   1609 O OD2 . ASP B 2 54  ? 59.448 -6.385  107.937 1.00 68.72  ? 51  ASP B OD2 1 
ATOM   1610 N N   . GLY B 2 55  ? 58.004 -3.705  111.329 1.00 68.48  ? 52  GLY B N   1 
ATOM   1611 C CA  . GLY B 2 55  ? 58.412 -3.605  112.739 1.00 64.91  ? 52  GLY B CA  1 
ATOM   1612 C C   . GLY B 2 55  ? 57.750 -2.485  113.509 1.00 66.21  ? 52  GLY B C   1 
ATOM   1613 O O   . GLY B 2 55  ? 58.110 -2.233  114.641 1.00 70.29  ? 52  GLY B O   1 
ATOM   1614 N N   . ILE B 2 56  ? 56.763 -1.824  112.909 1.00 74.11  ? 53  ILE B N   1 
ATOM   1615 C CA  . ILE B 2 56  ? 55.892 -0.890  113.637 1.00 72.08  ? 53  ILE B CA  1 
ATOM   1616 C C   . ILE B 2 56  ? 55.549 -1.587  114.931 1.00 69.61  ? 53  ILE B C   1 
ATOM   1617 O O   . ILE B 2 56  ? 55.397 -2.803  114.947 1.00 68.92  ? 53  ILE B O   1 
ATOM   1618 C CB  . ILE B 2 56  ? 54.516 -0.626  112.946 1.00 78.26  ? 53  ILE B CB  1 
ATOM   1619 C CG1 . ILE B 2 56  ? 54.633 -0.224  111.470 1.00 93.78  ? 53  ILE B CG1 1 
ATOM   1620 C CG2 . ILE B 2 56  ? 53.720 0.441   113.689 1.00 72.89  ? 53  ILE B CG2 1 
ATOM   1621 C CD1 . ILE B 2 56  ? 55.247 1.141   111.216 1.00 112.23 ? 53  ILE B CD1 1 
ATOM   1622 N N   . SER B 2 57  ? 55.397 -0.830  116.010 1.00 70.20  ? 54  SER B N   1 
ATOM   1623 C CA  . SER B 2 57  ? 54.908 -1.409  117.242 1.00 66.48  ? 54  SER B CA  1 
ATOM   1624 C C   . SER B 2 57  ? 53.413 -1.520  117.149 1.00 63.58  ? 54  SER B C   1 
ATOM   1625 O O   . SER B 2 57  ? 52.743 -0.777  116.441 1.00 69.61  ? 54  SER B O   1 
ATOM   1626 C CB  . SER B 2 57  ? 55.334 -0.606  118.493 1.00 70.73  ? 54  SER B CB  1 
ATOM   1627 O OG  . SER B 2 57  ? 54.683 0.649   118.607 1.00 75.03  ? 54  SER B OG  1 
ATOM   1628 N N   . GLN B 2 58  ? 52.902 -2.475  117.885 1.00 61.41  ? 55  GLN B N   1 
ATOM   1629 C CA  . GLN B 2 58  ? 51.483 -2.694  118.022 1.00 62.12  ? 55  GLN B CA  1 
ATOM   1630 C C   . GLN B 2 58  ? 50.669 -1.471  118.386 1.00 70.75  ? 55  GLN B C   1 
ATOM   1631 O O   . GLN B 2 58  ? 49.547 -1.294  117.899 1.00 71.20  ? 55  GLN B O   1 
ATOM   1632 C CB  . GLN B 2 58  ? 51.311 -3.741  119.104 1.00 61.58  ? 55  GLN B CB  1 
ATOM   1633 C CG  . GLN B 2 58  ? 50.805 -5.072  118.629 1.00 70.53  ? 55  GLN B CG  1 
ATOM   1634 C CD  . GLN B 2 58  ? 49.359 -5.203  118.933 1.00 69.09  ? 55  GLN B CD  1 
ATOM   1635 O OE1 . GLN B 2 58  ? 48.619 -4.237  118.748 1.00 74.18  ? 55  GLN B OE1 1 
ATOM   1636 N NE2 . GLN B 2 58  ? 48.944 -6.356  119.449 1.00 63.03  ? 55  GLN B NE2 1 
ATOM   1637 N N   . ILE B 2 59  ? 51.204 -0.641  119.284 1.00 85.66  ? 56  ILE B N   1 
ATOM   1638 C CA  . ILE B 2 59  ? 50.412 0.468   119.836 1.00 90.97  ? 56  ILE B CA  1 
ATOM   1639 C C   . ILE B 2 59  ? 50.302 1.535   118.744 1.00 80.00  ? 56  ILE B C   1 
ATOM   1640 O O   . ILE B 2 59  ? 49.196 2.014   118.436 1.00 62.32  ? 56  ILE B O   1 
ATOM   1641 C CB  . ILE B 2 59  ? 50.963 0.982   121.213 1.00 104.46 ? 56  ILE B CB  1 
ATOM   1642 C CG1 . ILE B 2 59  ? 49.815 1.475   122.109 1.00 110.03 ? 56  ILE B CG1 1 
ATOM   1643 C CG2 . ILE B 2 59  ? 52.046 2.054   121.074 1.00 106.49 ? 56  ILE B CG2 1 
ATOM   1644 C CD1 . ILE B 2 59  ? 48.900 2.525   121.490 1.00 110.37 ? 56  ILE B CD1 1 
ATOM   1645 N N   . ASP B 2 60  ? 51.444 1.819   118.109 1.00 72.90  ? 57  ASP B N   1 
ATOM   1646 C CA  . ASP B 2 60  ? 51.487 2.689   116.938 1.00 73.01  ? 57  ASP B CA  1 
ATOM   1647 C C   . ASP B 2 60  ? 50.520 2.231   115.849 1.00 70.37  ? 57  ASP B C   1 
ATOM   1648 O O   . ASP B 2 60  ? 49.861 3.057   115.244 1.00 71.35  ? 57  ASP B O   1 
ATOM   1649 C CB  . ASP B 2 60  ? 52.900 2.784   116.359 1.00 72.19  ? 57  ASP B CB  1 
ATOM   1650 C CG  . ASP B 2 60  ? 53.829 3.575   117.225 1.00 76.85  ? 57  ASP B CG  1 
ATOM   1651 O OD1 . ASP B 2 60  ? 53.483 3.791   118.397 1.00 87.38  ? 57  ASP B OD1 1 
ATOM   1652 O OD2 . ASP B 2 60  ? 54.911 3.981   116.748 1.00 85.56  ? 57  ASP B OD2 1 
ATOM   1653 N N   . LEU B 2 61  ? 50.435 0.924   115.603 1.00 69.85  ? 58  LEU B N   1 
ATOM   1654 C CA  . LEU B 2 61  ? 49.562 0.417   114.543 1.00 73.81  ? 58  LEU B CA  1 
ATOM   1655 C C   . LEU B 2 61  ? 48.092 0.680   114.870 1.00 71.15  ? 58  LEU B C   1 
ATOM   1656 O O   . LEU B 2 61  ? 47.289 0.982   113.980 1.00 61.72  ? 58  LEU B O   1 
ATOM   1657 C CB  . LEU B 2 61  ? 49.782 -1.076  114.297 1.00 72.84  ? 58  LEU B CB  1 
ATOM   1658 C CG  . LEU B 2 61  ? 50.223 -1.471  112.900 1.00 68.84  ? 58  LEU B CG  1 
ATOM   1659 C CD1 . LEU B 2 61  ? 50.500 -2.954  112.925 1.00 76.57  ? 58  LEU B CD1 1 
ATOM   1660 C CD2 . LEU B 2 61  ? 49.178 -1.160  111.853 1.00 73.82  ? 58  LEU B CD2 1 
ATOM   1661 N N   . CYS B 2 62  ? 47.752 0.592   116.148 1.00 68.38  ? 59  CYS B N   1 
ATOM   1662 C CA  . CYS B 2 62  ? 46.399 0.911   116.560 1.00 75.82  ? 59  CYS B CA  1 
ATOM   1663 C C   . CYS B 2 62  ? 46.088 2.409   116.391 1.00 73.86  ? 59  CYS B C   1 
ATOM   1664 O O   . CYS B 2 62  ? 44.936 2.783   116.007 1.00 69.49  ? 59  CYS B O   1 
ATOM   1665 C CB  . CYS B 2 62  ? 46.178 0.422   117.987 1.00 81.36  ? 59  CYS B CB  1 
ATOM   1666 S SG  . CYS B 2 62  ? 46.074 -1.390  118.090 1.00 78.66  ? 59  CYS B SG  1 
ATOM   1667 N N   . GLU B 2 63  ? 47.121 3.238   116.637 1.00 72.27  ? 60  GLU B N   1 
ATOM   1668 C CA  . GLU B 2 63  ? 47.027 4.692   116.520 1.00 77.29  ? 60  GLU B CA  1 
ATOM   1669 C C   . GLU B 2 63  ? 46.661 4.982   115.084 1.00 71.77  ? 60  GLU B C   1 
ATOM   1670 O O   . GLU B 2 63  ? 45.671 5.651   114.808 1.00 79.36  ? 60  GLU B O   1 
ATOM   1671 C CB  . GLU B 2 63  ? 48.354 5.430   116.852 1.00 95.39  ? 60  GLU B CB  1 
ATOM   1672 C CG  . GLU B 2 63  ? 49.047 5.112   118.193 1.00 109.80 ? 60  GLU B CG  1 
ATOM   1673 C CD  . GLU B 2 63  ? 48.707 6.050   119.353 1.00 117.94 ? 60  GLU B CD  1 
ATOM   1674 O OE1 . GLU B 2 63  ? 47.796 6.897   119.191 1.00 125.68 ? 60  GLU B OE1 1 
ATOM   1675 O OE2 . GLU B 2 63  ? 49.354 5.925   120.437 1.00 98.16  ? 60  GLU B OE2 1 
ATOM   1676 N N   . LYS B 2 64  ? 47.461 4.403   114.191 1.00 72.43  ? 61  LYS B N   1 
ATOM   1677 C CA  . LYS B 2 64  ? 47.404 4.561   112.725 1.00 68.50  ? 61  LYS B CA  1 
ATOM   1678 C C   . LYS B 2 64  ? 46.112 4.027   112.086 1.00 69.71  ? 61  LYS B C   1 
ATOM   1679 O O   . LYS B 2 64  ? 45.698 4.487   111.013 1.00 68.41  ? 61  LYS B O   1 
ATOM   1680 C CB  . LYS B 2 64  ? 48.582 3.772   112.137 1.00 71.52  ? 61  LYS B CB  1 
ATOM   1681 C CG  . LYS B 2 64  ? 49.424 4.487   111.105 1.00 79.91  ? 61  LYS B CG  1 
ATOM   1682 C CD  . LYS B 2 64  ? 50.921 4.388   111.428 1.00 78.14  ? 61  LYS B CD  1 
ATOM   1683 C CE  . LYS B 2 64  ? 51.662 5.483   110.678 1.00 84.96  ? 61  LYS B CE  1 
ATOM   1684 N NZ  . LYS B 2 64  ? 53.132 5.412   110.887 1.00 89.99  ? 61  LYS B NZ  1 
ATOM   1685 N N   . SER B 2 65  ? 45.467 3.100   112.790 1.00 63.76  ? 62  SER B N   1 
ATOM   1686 C CA  . SER B 2 65  ? 44.545 2.169   112.218 1.00 67.77  ? 62  SER B CA  1 
ATOM   1687 C C   . SER B 2 65  ? 43.178 2.682   111.786 1.00 83.36  ? 62  SER B C   1 
ATOM   1688 O O   . SER B 2 65  ? 42.387 1.886   111.259 1.00 108.68 ? 62  SER B O   1 
ATOM   1689 C CB  . SER B 2 65  ? 44.337 0.987   113.181 1.00 65.63  ? 62  SER B CB  1 
ATOM   1690 O OG  . SER B 2 65  ? 43.106 0.285   112.952 1.00 60.38  ? 62  SER B OG  1 
ATOM   1691 N N   . CYS B 2 66  ? 42.858 3.952   111.976 1.00 91.83  ? 63  CYS B N   1 
ATOM   1692 C CA  . CYS B 2 66  ? 41.480 4.415   111.678 1.00 94.87  ? 63  CYS B CA  1 
ATOM   1693 C C   . CYS B 2 66  ? 40.491 3.648   112.561 1.00 88.98  ? 63  CYS B C   1 
ATOM   1694 O O   . CYS B 2 66  ? 39.371 4.097   112.796 1.00 85.21  ? 63  CYS B O   1 
ATOM   1695 C CB  . CYS B 2 66  ? 41.114 4.301   110.169 1.00 97.72  ? 63  CYS B CB  1 
ATOM   1696 S SG  . CYS B 2 66  ? 39.547 3.430   109.791 1.00 96.02  ? 63  CYS B SG  1 
ATOM   1697 N N   . LYS B 2 67  ? 40.904 2.488   113.059 1.00 82.40  ? 64  LYS B N   1 
ATOM   1698 C CA  . LYS B 2 67  ? 40.127 1.819   114.069 1.00 82.14  ? 64  LYS B CA  1 
ATOM   1699 C C   . LYS B 2 67  ? 40.767 1.891   115.466 1.00 84.90  ? 64  LYS B C   1 
ATOM   1700 O O   . LYS B 2 67  ? 41.922 2.426   115.687 1.00 71.13  ? 64  LYS B O   1 
ATOM   1701 C CB  . LYS B 2 67  ? 39.822 0.377   113.649 1.00 75.09  ? 64  LYS B CB  1 
ATOM   1702 C CG  . LYS B 2 67  ? 38.643 0.315   112.713 1.00 76.87  ? 64  LYS B CG  1 
ATOM   1703 C CD  . LYS B 2 67  ? 38.348 -1.095  112.209 1.00 71.66  ? 64  LYS B CD  1 
ATOM   1704 C CE  . LYS B 2 67  ? 37.075 -1.062  111.371 1.00 67.02  ? 64  LYS B CE  1 
ATOM   1705 N NZ  . LYS B 2 67  ? 36.812 -2.311  110.605 1.00 68.02  ? 64  LYS B NZ  1 
ATOM   1706 N N   . ASP B 2 68  ? 39.907 1.389   116.358 1.00 81.76  ? 65  ASP B N   1 
ATOM   1707 C CA  . ASP B 2 68  ? 40.056 1.270   117.800 1.00 91.23  ? 65  ASP B CA  1 
ATOM   1708 C C   . ASP B 2 68  ? 40.923 0.050   118.130 1.00 92.94  ? 65  ASP B C   1 
ATOM   1709 O O   . ASP B 2 68  ? 41.092 -0.856  117.314 1.00 91.72  ? 65  ASP B O   1 
ATOM   1710 C CB  . ASP B 2 68  ? 38.621 1.239   118.426 1.00 90.13  ? 65  ASP B CB  1 
ATOM   1711 C CG  . ASP B 2 68  ? 38.416 0.173   119.485 1.00 95.68  ? 65  ASP B CG  1 
ATOM   1712 O OD1 . ASP B 2 68  ? 39.100 0.199   120.530 1.00 114.38 ? 65  ASP B OD1 1 
ATOM   1713 O OD2 . ASP B 2 68  ? 37.497 -0.648  119.301 1.00 88.35  ? 65  ASP B OD2 1 
ATOM   1714 N N   . LYS B 2 69  ? 41.465 0.085   119.342 1.00 90.42  ? 66  LYS B N   1 
ATOM   1715 C CA  . LYS B 2 69  ? 42.504 -0.809  119.847 1.00 93.92  ? 66  LYS B CA  1 
ATOM   1716 C C   . LYS B 2 69  ? 42.104 -2.306  119.896 1.00 89.65  ? 66  LYS B C   1 
ATOM   1717 O O   . LYS B 2 69  ? 42.898 -3.218  119.570 1.00 77.17  ? 66  LYS B O   1 
ATOM   1718 C CB  . LYS B 2 69  ? 42.860 -0.297  121.256 1.00 101.46 ? 66  LYS B CB  1 
ATOM   1719 C CG  . LYS B 2 69  ? 44.134 -0.822  121.904 1.00 108.82 ? 66  LYS B CG  1 
ATOM   1720 C CD  . LYS B 2 69  ? 44.356 -0.141  123.263 1.00 117.73 ? 66  LYS B CD  1 
ATOM   1721 C CE  . LYS B 2 69  ? 45.317 1.053   123.204 1.00 114.67 ? 66  LYS B CE  1 
ATOM   1722 N NZ  . LYS B 2 69  ? 46.744 0.613   123.108 1.00 115.32 ? 66  LYS B NZ  1 
ATOM   1723 N N   . SER B 2 70  ? 40.878 -2.578  120.319 1.00 85.23  ? 67  SER B N   1 
ATOM   1724 C CA  . SER B 2 70  ? 40.468 -3.971  120.462 1.00 87.94  ? 67  SER B CA  1 
ATOM   1725 C C   . SER B 2 70  ? 40.159 -4.570  119.064 1.00 71.88  ? 67  SER B C   1 
ATOM   1726 O O   . SER B 2 70  ? 40.568 -5.684  118.776 1.00 58.55  ? 67  SER B O   1 
ATOM   1727 C CB  . SER B 2 70  ? 39.323 -4.131  121.489 1.00 80.38  ? 67  SER B CB  1 
ATOM   1728 O OG  . SER B 2 70  ? 38.049 -3.851  120.928 1.00 89.33  ? 67  SER B OG  1 
ATOM   1729 N N   . ASN B 2 71  ? 39.497 -3.811  118.189 1.00 76.09  ? 68  ASN B N   1 
ATOM   1730 C CA  . ASN B 2 71  ? 39.264 -4.274  116.799 1.00 77.56  ? 68  ASN B CA  1 
ATOM   1731 C C   . ASN B 2 71  ? 40.557 -4.476  115.998 1.00 64.47  ? 68  ASN B C   1 
ATOM   1732 O O   . ASN B 2 71  ? 40.802 -5.550  115.493 1.00 59.31  ? 68  ASN B O   1 
ATOM   1733 C CB  . ASN B 2 71  ? 38.352 -3.333  116.036 1.00 80.41  ? 68  ASN B CB  1 
ATOM   1734 C CG  . ASN B 2 71  ? 36.986 -3.207  116.663 1.00 81.60  ? 68  ASN B CG  1 
ATOM   1735 O OD1 . ASN B 2 71  ? 36.165 -4.120  116.594 1.00 57.93  ? 68  ASN B OD1 1 
ATOM   1736 N ND2 . ASN B 2 71  ? 36.724 -2.040  117.254 1.00 95.32  ? 68  ASN B ND2 1 
ATOM   1737 N N   . THR B 2 72  ? 41.399 -3.456  115.931 1.00 58.79  ? 69  THR B N   1 
ATOM   1738 C CA  . THR B 2 72  ? 42.706 -3.594  115.277 1.00 64.82  ? 69  THR B CA  1 
ATOM   1739 C C   . THR B 2 72  ? 43.529 -4.808  115.759 1.00 65.11  ? 69  THR B C   1 
ATOM   1740 O O   . THR B 2 72  ? 44.210 -5.446  114.975 1.00 78.06  ? 69  THR B O   1 
ATOM   1741 C CB  . THR B 2 72  ? 43.547 -2.308  115.446 1.00 59.58  ? 69  THR B CB  1 
ATOM   1742 O OG1 . THR B 2 72  ? 42.773 -1.177  115.030 1.00 63.32  ? 69  THR B OG1 1 
ATOM   1743 C CG2 . THR B 2 72  ? 44.829 -2.356  114.633 1.00 55.16  ? 69  THR B CG2 1 
ATOM   1744 N N   . THR B 2 73  ? 43.479 -5.108  117.044 1.00 68.86  ? 70  THR B N   1 
ATOM   1745 C CA  . THR B 2 73  ? 44.269 -6.202  117.620 1.00 62.00  ? 70  THR B CA  1 
ATOM   1746 C C   . THR B 2 73  ? 43.631 -7.515  117.197 1.00 57.89  ? 70  THR B C   1 
ATOM   1747 O O   . THR B 2 73  ? 44.326 -8.488  116.876 1.00 55.62  ? 70  THR B O   1 
ATOM   1748 C CB  . THR B 2 73  ? 44.321 -6.077  119.169 1.00 65.93  ? 70  THR B CB  1 
ATOM   1749 O OG1 . THR B 2 73  ? 44.752 -4.746  119.529 1.00 68.81  ? 70  THR B OG1 1 
ATOM   1750 C CG2 . THR B 2 73  ? 45.279 -7.106  119.797 1.00 61.76  ? 70  THR B CG2 1 
ATOM   1751 N N   . ARG B 2 74  ? 42.302 -7.533  117.179 1.00 50.72  ? 71  ARG B N   1 
ATOM   1752 C CA  . ARG B 2 74  ? 41.593 -8.715  116.807 1.00 58.15  ? 71  ARG B CA  1 
ATOM   1753 C C   . ARG B 2 74  ? 41.985 -8.966  115.337 1.00 60.00  ? 71  ARG B C   1 
ATOM   1754 O O   . ARG B 2 74  ? 42.434 -10.069 115.008 1.00 63.00  ? 71  ARG B O   1 
ATOM   1755 C CB  . ARG B 2 74  ? 40.048 -8.555  117.039 1.00 68.75  ? 71  ARG B CB  1 
ATOM   1756 C CG  . ARG B 2 74  ? 39.144 -9.713  116.502 1.00 76.33  ? 71  ARG B CG  1 
ATOM   1757 C CD  . ARG B 2 74  ? 37.642 -9.380  116.475 1.00 79.41  ? 71  ARG B CD  1 
ATOM   1758 N NE  . ARG B 2 74  ? 37.379 -7.983  116.045 1.00 96.83  ? 71  ARG B NE  1 
ATOM   1759 C CZ  . ARG B 2 74  ? 37.286 -7.539  114.776 1.00 92.62  ? 71  ARG B CZ  1 
ATOM   1760 N NH1 . ARG B 2 74  ? 37.400 -8.365  113.731 1.00 91.74  ? 71  ARG B NH1 1 
ATOM   1761 N NH2 . ARG B 2 74  ? 37.070 -6.243  114.542 1.00 89.72  ? 71  ARG B NH2 1 
ATOM   1762 N N   . ILE B 2 75  ? 41.865 -7.924  114.485 1.00 58.14  ? 72  ILE B N   1 
ATOM   1763 C CA  . ILE B 2 75  ? 42.156 -8.025  113.057 1.00 53.88  ? 72  ILE B CA  1 
ATOM   1764 C C   . ILE B 2 75  ? 43.592 -8.563  112.907 1.00 49.95  ? 72  ILE B C   1 
ATOM   1765 O O   . ILE B 2 75  ? 43.845 -9.471  112.158 1.00 49.89  ? 72  ILE B O   1 
ATOM   1766 C CB  . ILE B 2 75  ? 42.118 -6.675  112.340 1.00 54.53  ? 72  ILE B CB  1 
ATOM   1767 C CG1 . ILE B 2 75  ? 40.773 -5.951  112.404 1.00 55.81  ? 72  ILE B CG1 1 
ATOM   1768 C CG2 . ILE B 2 75  ? 42.521 -6.858  110.890 1.00 57.82  ? 72  ILE B CG2 1 
ATOM   1769 C CD1 . ILE B 2 75  ? 39.733 -6.498  111.498 1.00 65.26  ? 72  ILE B CD1 1 
ATOM   1770 N N   . LEU B 2 76  ? 44.524 -8.013  113.663 1.00 47.83  ? 73  LEU B N   1 
ATOM   1771 C CA  . LEU B 2 76  ? 45.907 -8.489  113.640 1.00 54.91  ? 73  LEU B CA  1 
ATOM   1772 C C   . LEU B 2 76  ? 46.100 -9.946  114.031 1.00 50.32  ? 73  LEU B C   1 
ATOM   1773 O O   . LEU B 2 76  ? 46.991 -10.579 113.512 1.00 52.23  ? 73  LEU B O   1 
ATOM   1774 C CB  . LEU B 2 76  ? 46.788 -7.636  114.561 1.00 51.89  ? 73  LEU B CB  1 
ATOM   1775 C CG  . LEU B 2 76  ? 47.110 -6.224  114.092 1.00 54.27  ? 73  LEU B CG  1 
ATOM   1776 C CD1 . LEU B 2 76  ? 47.488 -5.352  115.272 1.00 54.55  ? 73  LEU B CD1 1 
ATOM   1777 C CD2 . LEU B 2 76  ? 48.226 -6.261  113.069 1.00 52.58  ? 73  LEU B CD2 1 
ATOM   1778 N N   . ASP B 2 77  ? 45.318 -10.460 114.969 1.00 52.22  ? 74  ASP B N   1 
ATOM   1779 C CA  . ASP B 2 77  ? 45.417 -11.890 115.323 1.00 58.24  ? 74  ASP B CA  1 
ATOM   1780 C C   . ASP B 2 77  ? 45.061 -12.720 114.101 1.00 52.75  ? 74  ASP B C   1 
ATOM   1781 O O   . ASP B 2 77  ? 45.775 -13.672 113.725 1.00 47.03  ? 74  ASP B O   1 
ATOM   1782 C CB  . ASP B 2 77  ? 44.430 -12.269 116.445 1.00 67.31  ? 74  ASP B CB  1 
ATOM   1783 C CG  . ASP B 2 77  ? 44.879 -11.836 117.845 1.00 68.50  ? 74  ASP B CG  1 
ATOM   1784 O OD1 . ASP B 2 77  ? 46.049 -11.453 118.086 1.00 68.92  ? 74  ASP B OD1 1 
ATOM   1785 O OD2 . ASP B 2 77  ? 44.014 -11.903 118.722 1.00 70.78  ? 74  ASP B OD2 1 
ATOM   1786 N N   . VAL B 2 78  ? 43.947 -12.355 113.463 1.00 46.73  ? 75  VAL B N   1 
ATOM   1787 C CA  . VAL B 2 78  ? 43.545 -13.068 112.260 1.00 46.13  ? 75  VAL B CA  1 
ATOM   1788 C C   . VAL B 2 78  ? 44.684 -13.042 111.248 1.00 53.24  ? 75  VAL B C   1 
ATOM   1789 O O   . VAL B 2 78  ? 44.963 -14.070 110.598 1.00 55.98  ? 75  VAL B O   1 
ATOM   1790 C CB  . VAL B 2 78  ? 42.272 -12.493 111.650 1.00 51.84  ? 75  VAL B CB  1 
ATOM   1791 C CG1 . VAL B 2 78  ? 41.981 -13.184 110.340 1.00 53.02  ? 75  VAL B CG1 1 
ATOM   1792 C CG2 . VAL B 2 78  ? 41.088 -12.605 112.614 1.00 49.87  ? 75  VAL B CG2 1 
ATOM   1793 N N   . MET B 2 79  ? 45.384 -11.901 111.136 1.00 44.98  ? 76  MET B N   1 
ATOM   1794 C CA  . MET B 2 79  ? 46.411 -11.783 110.086 1.00 45.39  ? 76  MET B CA  1 
ATOM   1795 C C   . MET B 2 79  ? 47.537 -12.650 110.477 1.00 41.95  ? 76  MET B C   1 
ATOM   1796 O O   . MET B 2 79  ? 48.220 -13.237 109.609 1.00 49.39  ? 76  MET B O   1 
ATOM   1797 C CB  . MET B 2 79  ? 46.897 -10.329 109.863 1.00 43.92  ? 76  MET B CB  1 
ATOM   1798 C CG  . MET B 2 79  ? 45.834 -9.402  109.299 1.00 50.31  ? 76  MET B CG  1 
ATOM   1799 S SD  . MET B 2 79  ? 46.216 -7.625  109.291 1.00 46.91  ? 76  MET B SD  1 
ATOM   1800 C CE  . MET B 2 79  ? 47.694 -7.584  108.311 1.00 43.76  ? 76  MET B CE  1 
ATOM   1801 N N   . LYS B 2 80  ? 47.781 -12.697 111.783 1.00 46.13  ? 77  LYS B N   1 
ATOM   1802 C CA  . LYS B 2 80  ? 48.841 -13.585 112.323 1.00 54.66  ? 77  LYS B CA  1 
ATOM   1803 C C   . LYS B 2 80  ? 48.551 -15.063 111.971 1.00 47.15  ? 77  LYS B C   1 
ATOM   1804 O O   . LYS B 2 80  ? 49.442 -15.786 111.502 1.00 39.09  ? 77  LYS B O   1 
ATOM   1805 C CB  . LYS B 2 80  ? 49.023 -13.443 113.837 1.00 53.43  ? 77  LYS B CB  1 
ATOM   1806 C CG  . LYS B 2 80  ? 50.028 -14.481 114.383 1.00 61.00  ? 77  LYS B CG  1 
ATOM   1807 C CD  . LYS B 2 80  ? 50.248 -14.483 115.895 1.00 58.86  ? 77  LYS B CD  1 
ATOM   1808 C CE  . LYS B 2 80  ? 48.931 -14.630 116.688 1.00 60.43  ? 77  LYS B CE  1 
ATOM   1809 N NZ  . LYS B 2 80  ? 48.114 -15.854 116.373 1.00 57.94  ? 77  LYS B NZ  1 
ATOM   1810 N N   . ASN B 2 81  ? 47.298 -15.468 112.137 1.00 44.76  ? 78  ASN B N   1 
ATOM   1811 C CA  . ASN B 2 81  ? 46.932 -16.863 111.864 1.00 53.45  ? 78  ASN B CA  1 
ATOM   1812 C C   . ASN B 2 81  ? 46.908 -17.191 110.393 1.00 52.39  ? 78  ASN B C   1 
ATOM   1813 O O   . ASN B 2 81  ? 47.071 -18.394 110.023 1.00 65.78  ? 78  ASN B O   1 
ATOM   1814 C CB  . ASN B 2 81  ? 45.598 -17.267 112.517 1.00 51.90  ? 78  ASN B CB  1 
ATOM   1815 C CG  . ASN B 2 81  ? 45.584 -17.003 114.012 1.00 48.38  ? 78  ASN B CG  1 
ATOM   1816 O OD1 . ASN B 2 81  ? 46.619 -16.990 114.666 1.00 45.05  ? 78  ASN B OD1 1 
ATOM   1817 N ND2 . ASN B 2 81  ? 44.420 -16.760 114.544 1.00 42.45  ? 78  ASN B ND2 1 
ATOM   1818 N N   . LYS B 2 82  ? 46.730 -16.167 109.545 1.00 43.94  ? 79  LYS B N   1 
ATOM   1819 C CA  . LYS B 2 82  ? 46.811 -16.399 108.108 1.00 41.25  ? 79  LYS B CA  1 
ATOM   1820 C C   . LYS B 2 82  ? 48.240 -16.441 107.655 1.00 41.95  ? 79  LYS B C   1 
ATOM   1821 O O   . LYS B 2 82  ? 48.487 -16.641 106.472 1.00 47.55  ? 79  LYS B O   1 
ATOM   1822 C CB  . LYS B 2 82  ? 46.078 -15.322 107.335 1.00 49.17  ? 79  LYS B CB  1 
ATOM   1823 C CG  . LYS B 2 82  ? 44.576 -15.227 107.564 1.00 45.54  ? 79  LYS B CG  1 
ATOM   1824 C CD  . LYS B 2 82  ? 43.969 -14.312 106.542 1.00 48.95  ? 79  LYS B CD  1 
ATOM   1825 C CE  . LYS B 2 82  ? 42.446 -14.160 106.708 1.00 60.53  ? 79  LYS B CE  1 
ATOM   1826 N NZ  . LYS B 2 82  ? 41.575 -15.148 105.990 1.00 60.34  ? 79  LYS B NZ  1 
ATOM   1827 N N   . GLY B 2 83  ? 49.191 -16.192 108.567 1.00 40.43  ? 80  GLY B N   1 
ATOM   1828 C CA  . GLY B 2 83  ? 50.624 -16.245 108.244 1.00 42.20  ? 80  GLY B CA  1 
ATOM   1829 C C   . GLY B 2 83  ? 51.274 -14.967 107.695 1.00 53.04  ? 80  GLY B C   1 
ATOM   1830 O O   . GLY B 2 83  ? 52.382 -15.015 107.119 1.00 54.47  ? 80  GLY B O   1 
ATOM   1831 N N   . LEU B 2 84  ? 50.607 -13.820 107.876 1.00 54.21  ? 81  LEU B N   1 
ATOM   1832 C CA  . LEU B 2 84  ? 51.042 -12.547 107.222 1.00 52.04  ? 81  LEU B CA  1 
ATOM   1833 C C   . LEU B 2 84  ? 52.025 -11.784 108.090 1.00 50.07  ? 81  LEU B C   1 
ATOM   1834 O O   . LEU B 2 84  ? 53.022 -11.284 107.624 1.00 44.12  ? 81  LEU B O   1 
ATOM   1835 C CB  . LEU B 2 84  ? 49.837 -11.659 106.964 1.00 46.87  ? 81  LEU B CB  1 
ATOM   1836 C CG  . LEU B 2 84  ? 48.716 -12.311 106.147 1.00 44.75  ? 81  LEU B CG  1 
ATOM   1837 C CD1 . LEU B 2 84  ? 47.465 -11.472 106.134 1.00 42.36  ? 81  LEU B CD1 1 
ATOM   1838 C CD2 . LEU B 2 84  ? 49.235 -12.473 104.723 1.00 51.08  ? 81  LEU B CD2 1 
ATOM   1839 N N   . ILE B 2 85  ? 51.730 -11.718 109.378 1.00 53.63  ? 82  ILE B N   1 
ATOM   1840 C CA  . ILE B 2 85  ? 52.639 -11.108 110.312 1.00 53.27  ? 82  ILE B CA  1 
ATOM   1841 C C   . ILE B 2 85  ? 53.018 -12.059 111.428 1.00 58.51  ? 82  ILE B C   1 
ATOM   1842 O O   . ILE B 2 85  ? 52.409 -13.119 111.606 1.00 66.27  ? 82  ILE B O   1 
ATOM   1843 C CB  . ILE B 2 85  ? 52.027 -9.856  110.934 1.00 49.77  ? 82  ILE B CB  1 
ATOM   1844 C CG1 . ILE B 2 85  ? 50.988 -10.277 111.940 1.00 49.16  ? 82  ILE B CG1 1 
ATOM   1845 C CG2 . ILE B 2 85  ? 51.523 -8.912  109.832 1.00 51.42  ? 82  ILE B CG2 1 
ATOM   1846 C CD1 . ILE B 2 85  ? 49.760 -9.415  112.004 1.00 52.17  ? 82  ILE B CD1 1 
ATOM   1847 N N   . VAL B 2 86  ? 54.062 -11.669 112.153 1.00 61.59  ? 83  VAL B N   1 
ATOM   1848 C CA  . VAL B 2 86  ? 54.349 -12.223 113.461 1.00 59.65  ? 83  VAL B CA  1 
ATOM   1849 C C   . VAL B 2 86  ? 54.398 -11.119 114.506 1.00 65.33  ? 83  VAL B C   1 
ATOM   1850 O O   . VAL B 2 86  ? 54.592 -9.918  114.188 1.00 64.23  ? 83  VAL B O   1 
ATOM   1851 C CB  . VAL B 2 86  ? 55.672 -13.020 113.518 1.00 55.20  ? 83  VAL B CB  1 
ATOM   1852 C CG1 . VAL B 2 86  ? 55.591 -14.311 112.712 1.00 53.17  ? 83  VAL B CG1 1 
ATOM   1853 C CG2 . VAL B 2 86  ? 56.811 -12.175 113.038 1.00 55.62  ? 83  VAL B CG2 1 
ATOM   1854 N N   . ARG B 2 87  ? 54.220 -11.562 115.752 1.00 70.72  ? 84  ARG B N   1 
ATOM   1855 C CA  . ARG B 2 87  ? 54.357 -10.726 116.934 1.00 77.33  ? 84  ARG B CA  1 
ATOM   1856 C C   . ARG B 2 87  ? 55.649 -11.111 117.623 1.00 81.60  ? 84  ARG B C   1 
ATOM   1857 O O   . ARG B 2 87  ? 56.075 -12.267 117.559 1.00 90.29  ? 84  ARG B O   1 
ATOM   1858 C CB  . ARG B 2 87  ? 53.201 -10.995 117.866 1.00 72.73  ? 84  ARG B CB  1 
ATOM   1859 C CG  . ARG B 2 87  ? 52.576 -9.757  118.417 1.00 70.39  ? 84  ARG B CG  1 
ATOM   1860 C CD  . ARG B 2 87  ? 51.398 -10.105 119.303 1.00 66.50  ? 84  ARG B CD  1 
ATOM   1861 N NE  . ARG B 2 87  ? 50.158 -9.483  118.860 1.00 65.88  ? 84  ARG B NE  1 
ATOM   1862 C CZ  . ARG B 2 87  ? 49.087 -10.147 118.437 1.00 62.39  ? 84  ARG B CZ  1 
ATOM   1863 N NH1 . ARG B 2 87  ? 49.080 -11.462 118.380 1.00 68.02  ? 84  ARG B NH1 1 
ATOM   1864 N NH2 . ARG B 2 87  ? 48.019 -9.489  118.051 1.00 59.91  ? 84  ARG B NH2 1 
ATOM   1865 N N   . LYS B 2 88  ? 56.283 -10.144 118.261 1.00 83.94  ? 85  LYS B N   1 
ATOM   1866 C CA  . LYS B 2 88  ? 57.512 -10.389 119.003 1.00 88.97  ? 85  LYS B CA  1 
ATOM   1867 C C   . LYS B 2 88  ? 57.487 -9.539  120.256 1.00 100.66 ? 85  LYS B C   1 
ATOM   1868 O O   . LYS B 2 88  ? 57.172 -8.348  120.196 1.00 102.37 ? 85  LYS B O   1 
ATOM   1869 C CB  . LYS B 2 88  ? 58.757 -10.040 118.173 1.00 88.18  ? 85  LYS B CB  1 
ATOM   1870 C CG  . LYS B 2 88  ? 59.060 -10.978 117.007 1.00 94.95  ? 85  LYS B CG  1 
ATOM   1871 C CD  . LYS B 2 88  ? 59.316 -12.428 117.430 1.00 98.63  ? 85  LYS B CD  1 
ATOM   1872 C CE  . LYS B 2 88  ? 59.379 -13.382 116.237 1.00 98.30  ? 85  LYS B CE  1 
ATOM   1873 N NZ  . LYS B 2 88  ? 60.290 -12.887 115.158 1.00 100.12 ? 85  LYS B NZ  1 
ATOM   1874 N N   . VAL B 2 89  ? 57.773 -10.163 121.395 1.00 109.63 ? 86  VAL B N   1 
ATOM   1875 C CA  . VAL B 2 89  ? 58.121 -9.405  122.591 1.00 115.94 ? 86  VAL B CA  1 
ATOM   1876 C C   . VAL B 2 89  ? 59.297 -8.486  122.240 1.00 111.32 ? 86  VAL B C   1 
ATOM   1877 O O   . VAL B 2 89  ? 60.311 -8.937  121.691 1.00 88.91  ? 86  VAL B O   1 
ATOM   1878 C CB  . VAL B 2 89  ? 58.472 -10.310 123.802 1.00 129.11 ? 86  VAL B CB  1 
ATOM   1879 C CG1 . VAL B 2 89  ? 57.212 -10.602 124.621 1.00 125.17 ? 86  VAL B CG1 1 
ATOM   1880 C CG2 . VAL B 2 89  ? 59.223 -11.588 123.371 1.00 128.02 ? 86  VAL B CG2 1 
ATOM   1881 N N   . ASP B 2 90  ? 59.135 -7.203  122.555 1.00 113.11 ? 87  ASP B N   1 
ATOM   1882 C CA  . ASP B 2 90  ? 60.025 -6.142  122.080 1.00 127.71 ? 87  ASP B CA  1 
ATOM   1883 C C   . ASP B 2 90  ? 61.455 -6.279  122.638 1.00 152.74 ? 87  ASP B C   1 
ATOM   1884 O O   . ASP B 2 90  ? 61.630 -6.685  123.801 1.00 161.89 ? 87  ASP B O   1 
ATOM   1885 C CB  . ASP B 2 90  ? 59.410 -4.790  122.468 1.00 116.25 ? 87  ASP B CB  1 
ATOM   1886 C CG  . ASP B 2 90  ? 60.105 -3.608  121.831 1.00 119.24 ? 87  ASP B CG  1 
ATOM   1887 O OD1 . ASP B 2 90  ? 61.291 -3.719  121.432 1.00 109.58 ? 87  ASP B OD1 1 
ATOM   1888 O OD2 . ASP B 2 90  ? 59.447 -2.546  121.747 1.00 108.58 ? 87  ASP B OD2 1 
ATOM   1889 N N   . VAL B 2 91  ? 62.463 -5.950  121.807 1.00 163.44 ? 88  VAL B N   1 
ATOM   1890 C CA  . VAL B 2 91  ? 63.894 -5.964  122.239 1.00 158.72 ? 88  VAL B CA  1 
ATOM   1891 C C   . VAL B 2 91  ? 64.125 -5.146  123.529 1.00 164.49 ? 88  VAL B C   1 
ATOM   1892 O O   . VAL B 2 91  ? 64.983 -5.509  124.333 1.00 164.52 ? 88  VAL B O   1 
ATOM   1893 C CB  . VAL B 2 91  ? 64.962 -5.551  121.138 1.00 136.87 ? 88  VAL B CB  1 
ATOM   1894 C CG1 . VAL B 2 91  ? 65.645 -6.779  120.534 1.00 122.75 ? 88  VAL B CG1 1 
ATOM   1895 C CG2 . VAL B 2 91  ? 64.410 -4.631  120.044 1.00 123.72 ? 88  VAL B CG2 1 
ATOM   1896 N N   . LYS B 2 92  ? 63.349 -4.076  123.734 1.00 163.96 ? 89  LYS B N   1 
ATOM   1897 C CA  . LYS B 2 92  ? 63.491 -3.213  124.921 1.00 154.83 ? 89  LYS B CA  1 
ATOM   1898 C C   . LYS B 2 92  ? 62.184 -3.057  125.708 1.00 144.06 ? 89  LYS B C   1 
ATOM   1899 O O   . LYS B 2 92  ? 61.686 -1.937  125.856 1.00 142.46 ? 89  LYS B O   1 
ATOM   1900 C CB  . LYS B 2 92  ? 64.068 -1.830  124.526 1.00 155.42 ? 89  LYS B CB  1 
ATOM   1901 C CG  . LYS B 2 92  ? 63.314 -1.054  123.440 1.00 149.62 ? 89  LYS B CG  1 
ATOM   1902 C CD  . LYS B 2 92  ? 64.219 -0.071  122.692 1.00 147.30 ? 89  LYS B CD  1 
ATOM   1903 C CE  . LYS B 2 92  ? 65.170 -0.749  121.709 1.00 141.75 ? 89  LYS B CE  1 
ATOM   1904 N NZ  . LYS B 2 92  ? 64.462 -1.289  120.518 1.00 146.92 ? 89  LYS B NZ  1 
ATOM   1905 N N   . ASP B 2 93  ? 61.639 -4.173  126.216 1.00 139.89 ? 90  ASP B N   1 
ATOM   1906 C CA  . ASP B 2 93  ? 60.368 -4.155  126.996 1.00 131.62 ? 90  ASP B CA  1 
ATOM   1907 C C   . ASP B 2 93  ? 59.884 -5.551  127.474 1.00 125.17 ? 90  ASP B C   1 
ATOM   1908 O O   . ASP B 2 93  ? 60.582 -6.563  127.332 1.00 122.71 ? 90  ASP B O   1 
ATOM   1909 C CB  . ASP B 2 93  ? 59.230 -3.489  126.173 1.00 118.63 ? 90  ASP B CB  1 
ATOM   1910 C CG  . ASP B 2 93  ? 58.426 -2.476  126.978 1.00 107.20 ? 90  ASP B CG  1 
ATOM   1911 O OD1 . ASP B 2 93  ? 57.475 -2.881  127.678 1.00 101.67 ? 90  ASP B OD1 1 
ATOM   1912 O OD2 . ASP B 2 93  ? 58.730 -1.267  126.886 1.00 88.27  ? 90  ASP B OD2 1 
ATOM   1913 N N   . ARG B 2 94  ? 58.700 -5.540  128.092 1.00 119.98 ? 91  ARG B N   1 
ATOM   1914 C CA  . ARG B 2 94  ? 57.791 -6.691  128.236 1.00 126.46 ? 91  ARG B CA  1 
ATOM   1915 C C   . ARG B 2 94  ? 56.367 -6.093  128.143 1.00 126.26 ? 91  ARG B C   1 
ATOM   1916 O O   . ARG B 2 94  ? 56.178 -4.911  128.474 1.00 112.87 ? 91  ARG B O   1 
ATOM   1917 C CB  . ARG B 2 94  ? 58.045 -7.454  129.570 1.00 131.46 ? 91  ARG B CB  1 
ATOM   1918 C CG  . ARG B 2 94  ? 56.804 -7.949  130.340 1.00 121.55 ? 91  ARG B CG  1 
ATOM   1919 C CD  . ARG B 2 94  ? 56.977 -9.347  130.934 1.00 117.31 ? 91  ARG B CD  1 
ATOM   1920 N NE  . ARG B 2 94  ? 55.695 -10.010 131.296 1.00 99.60  ? 91  ARG B NE  1 
ATOM   1921 C CZ  . ARG B 2 94  ? 55.595 -11.253 131.808 1.00 87.35  ? 91  ARG B CZ  1 
ATOM   1922 N NH1 . ARG B 2 94  ? 56.712 -11.978 132.028 1.00 74.58  ? 91  ARG B NH1 1 
ATOM   1923 N NH2 . ARG B 2 94  ? 54.385 -11.780 132.132 1.00 70.67  ? 91  ARG B NH2 1 
ATOM   1924 N N   . ARG B 2 95  ? 55.383 -6.876  127.681 1.00 119.20 ? 92  ARG B N   1 
ATOM   1925 C CA  . ARG B 2 95  ? 54.004 -6.371  127.468 1.00 129.76 ? 92  ARG B CA  1 
ATOM   1926 C C   . ARG B 2 95  ? 53.869 -5.598  126.129 1.00 143.70 ? 92  ARG B C   1 
ATOM   1927 O O   . ARG B 2 95  ? 52.755 -5.481  125.607 1.00 153.07 ? 92  ARG B O   1 
ATOM   1928 C CB  . ARG B 2 95  ? 53.520 -5.498  128.665 1.00 130.21 ? 92  ARG B CB  1 
ATOM   1929 C CG  . ARG B 2 95  ? 52.102 -4.904  128.596 1.00 124.50 ? 92  ARG B CG  1 
ATOM   1930 C CD  . ARG B 2 95  ? 50.961 -5.926  128.591 1.00 118.50 ? 92  ARG B CD  1 
ATOM   1931 N NE  . ARG B 2 95  ? 51.015 -6.865  129.725 1.00 114.73 ? 92  ARG B NE  1 
ATOM   1932 C CZ  . ARG B 2 95  ? 49.958 -7.410  130.342 1.00 104.53 ? 92  ARG B CZ  1 
ATOM   1933 N NH1 . ARG B 2 95  ? 48.711 -7.129  129.968 1.00 103.06 ? 92  ARG B NH1 1 
ATOM   1934 N NH2 . ARG B 2 95  ? 50.149 -8.244  131.361 1.00 94.17  ? 92  ARG B NH2 1 
ATOM   1935 N N   . LYS B 2 96  ? 54.990 -5.107  125.571 1.00 142.24 ? 93  LYS B N   1 
ATOM   1936 C CA  . LYS B 2 96  ? 55.005 -4.263  124.351 1.00 127.25 ? 93  LYS B CA  1 
ATOM   1937 C C   . LYS B 2 96  ? 55.532 -4.990  123.103 1.00 112.55 ? 93  LYS B C   1 
ATOM   1938 O O   . LYS B 2 96  ? 56.686 -5.434  123.065 1.00 96.12  ? 93  LYS B O   1 
ATOM   1939 C CB  . LYS B 2 96  ? 55.835 -2.994  124.591 1.00 121.64 ? 93  LYS B CB  1 
ATOM   1940 C CG  . LYS B 2 96  ? 55.057 -1.908  125.326 1.00 129.74 ? 93  LYS B CG  1 
ATOM   1941 C CD  . LYS B 2 96  ? 54.164 -1.087  124.397 1.00 132.68 ? 93  LYS B CD  1 
ATOM   1942 C CE  . LYS B 2 96  ? 54.824 0.224   123.977 1.00 131.60 ? 93  LYS B CE  1 
ATOM   1943 N NZ  . LYS B 2 96  ? 56.166 0.031   123.357 1.00 125.26 ? 93  LYS B NZ  1 
ATOM   1944 N N   . PHE B 2 97  ? 54.690 -5.075  122.073 1.00 96.54  ? 94  PHE B N   1 
ATOM   1945 C CA  . PHE B 2 97  ? 55.001 -5.868  120.888 1.00 84.69  ? 94  PHE B CA  1 
ATOM   1946 C C   . PHE B 2 97  ? 55.428 -5.019  119.670 1.00 72.75  ? 94  PHE B C   1 
ATOM   1947 O O   . PHE B 2 97  ? 54.905 -3.935  119.452 1.00 72.97  ? 94  PHE B O   1 
ATOM   1948 C CB  . PHE B 2 97  ? 53.777 -6.657  120.467 1.00 84.19  ? 94  PHE B CB  1 
ATOM   1949 C CG  . PHE B 2 97  ? 53.124 -7.470  121.561 1.00 90.34  ? 94  PHE B CG  1 
ATOM   1950 C CD1 . PHE B 2 97  ? 53.660 -8.699  121.957 1.00 86.88  ? 94  PHE B CD1 1 
ATOM   1951 C CD2 . PHE B 2 97  ? 51.906 -7.056  122.130 1.00 88.02  ? 94  PHE B CD2 1 
ATOM   1952 C CE1 . PHE B 2 97  ? 53.014 -9.471  122.925 1.00 88.51  ? 94  PHE B CE1 1 
ATOM   1953 C CE2 . PHE B 2 97  ? 51.261 -7.826  123.101 1.00 87.96  ? 94  PHE B CE2 1 
ATOM   1954 C CZ  . PHE B 2 97  ? 51.809 -9.037  123.495 1.00 83.70  ? 94  PHE B CZ  1 
ATOM   1955 N N   . GLN B 2 98  ? 56.377 -5.533  118.891 1.00 64.72  ? 95  GLN B N   1 
ATOM   1956 C CA  . GLN B 2 98  ? 56.585 -5.118  117.492 1.00 75.50  ? 95  GLN B CA  1 
ATOM   1957 C C   . GLN B 2 98  ? 55.942 -6.093  116.483 1.00 67.09  ? 95  GLN B C   1 
ATOM   1958 O O   . GLN B 2 98  ? 56.104 -7.304  116.584 1.00 67.25  ? 95  GLN B O   1 
ATOM   1959 C CB  . GLN B 2 98  ? 58.066 -5.068  117.143 1.00 80.22  ? 95  GLN B CB  1 
ATOM   1960 C CG  . GLN B 2 98  ? 58.893 -4.108  117.957 1.00 80.49  ? 95  GLN B CG  1 
ATOM   1961 C CD  . GLN B 2 98  ? 60.348 -4.386  117.736 1.00 81.87  ? 95  GLN B CD  1 
ATOM   1962 O OE1 . GLN B 2 98  ? 60.957 -3.816  116.830 1.00 86.60  ? 95  GLN B OE1 1 
ATOM   1963 N NE2 . GLN B 2 98  ? 60.906 -5.312  118.512 1.00 82.92  ? 95  GLN B NE2 1 
ATOM   1964 N N   . ILE B 2 99  ? 55.262 -5.554  115.478 1.00 65.14  ? 96  ILE B N   1 
ATOM   1965 C CA  . ILE B 2 99  ? 54.635 -6.386  114.467 1.00 58.91  ? 96  ILE B CA  1 
ATOM   1966 C C   . ILE B 2 99  ? 55.512 -6.400  113.265 1.00 58.21  ? 96  ILE B C   1 
ATOM   1967 O O   . ILE B 2 99  ? 55.885 -5.345  112.785 1.00 57.22  ? 96  ILE B O   1 
ATOM   1968 C CB  . ILE B 2 99  ? 53.287 -5.848  114.059 1.00 54.77  ? 96  ILE B CB  1 
ATOM   1969 C CG1 . ILE B 2 99  ? 52.348 -5.885  115.257 1.00 57.13  ? 96  ILE B CG1 1 
ATOM   1970 C CG2 . ILE B 2 99  ? 52.742 -6.641  112.894 1.00 61.07  ? 96  ILE B CG2 1 
ATOM   1971 C CD1 . ILE B 2 99  ? 52.287 -7.237  115.931 1.00 57.84  ? 96  ILE B CD1 1 
ATOM   1972 N N   . PHE B 2 100 ? 55.841 -7.605  112.812 1.00 54.77  ? 97  PHE B N   1 
ATOM   1973 C CA  . PHE B 2 100 ? 56.710 -7.803  111.671 1.00 61.54  ? 97  PHE B CA  1 
ATOM   1974 C C   . PHE B 2 100 ? 56.019 -8.616  110.574 1.00 57.73  ? 97  PHE B C   1 
ATOM   1975 O O   . PHE B 2 100 ? 55.201 -9.484  110.835 1.00 62.15  ? 97  PHE B O   1 
ATOM   1976 C CB  . PHE B 2 100 ? 57.975 -8.580  112.064 1.00 63.19  ? 97  PHE B CB  1 
ATOM   1977 C CG  . PHE B 2 100 ? 58.951 -7.811  112.887 1.00 66.36  ? 97  PHE B CG  1 
ATOM   1978 C CD1 . PHE B 2 100 ? 59.946 -7.054  112.269 1.00 71.84  ? 97  PHE B CD1 1 
ATOM   1979 C CD2 . PHE B 2 100 ? 58.929 -7.900  114.271 1.00 72.56  ? 97  PHE B CD2 1 
ATOM   1980 C CE1 . PHE B 2 100 ? 60.879 -6.372  113.014 1.00 64.74  ? 97  PHE B CE1 1 
ATOM   1981 C CE2 . PHE B 2 100 ? 59.856 -7.218  115.026 1.00 68.23  ? 97  PHE B CE2 1 
ATOM   1982 C CZ  . PHE B 2 100 ? 60.826 -6.456  114.392 1.00 68.03  ? 97  PHE B CZ  1 
ATOM   1983 N N   . LEU B 2 101 ? 56.404 -8.335  109.350 1.00 51.40  ? 98  LEU B N   1 
ATOM   1984 C CA  . LEU B 2 101 ? 55.943 -9.062  108.206 1.00 53.51  ? 98  LEU B CA  1 
ATOM   1985 C C   . LEU B 2 101 ? 56.646 -10.386 108.184 1.00 54.84  ? 98  LEU B C   1 
ATOM   1986 O O   . LEU B 2 101 ? 57.833 -10.457 108.500 1.00 64.93  ? 98  LEU B O   1 
ATOM   1987 C CB  . LEU B 2 101 ? 56.300 -8.303  106.904 1.00 49.33  ? 98  LEU B CB  1 
ATOM   1988 C CG  . LEU B 2 101 ? 55.511 -7.022  106.622 1.00 49.26  ? 98  LEU B CG  1 
ATOM   1989 C CD1 . LEU B 2 101 ? 56.206 -6.158  105.586 1.00 47.43  ? 98  LEU B CD1 1 
ATOM   1990 C CD2 . LEU B 2 101 ? 54.075 -7.339  106.203 1.00 45.30  ? 98  LEU B CD2 1 
ATOM   1991 N N   . THR B 2 102 ? 55.928 -11.420 107.765 1.00 47.35  ? 99  THR B N   1 
ATOM   1992 C CA  . THR B 2 102 ? 56.582 -12.646 107.333 1.00 47.08  ? 99  THR B CA  1 
ATOM   1993 C C   . THR B 2 102 ? 56.920 -12.466 105.874 1.00 49.31  ? 99  THR B C   1 
ATOM   1994 O O   . THR B 2 102 ? 56.561 -11.477 105.284 1.00 49.61  ? 99  THR B O   1 
ATOM   1995 C CB  . THR B 2 102 ? 55.629 -13.817 107.316 1.00 45.54  ? 99  THR B CB  1 
ATOM   1996 O OG1 . THR B 2 102 ? 54.618 -13.560 106.305 1.00 44.23  ? 99  THR B OG1 1 
ATOM   1997 C CG2 . THR B 2 102 ? 55.032 -14.023 108.681 1.00 45.90  ? 99  THR B CG2 1 
ATOM   1998 N N   . ASP B 2 103 ? 57.587 -13.458 105.309 1.00 50.20  ? 100 ASP B N   1 
ATOM   1999 C CA  . ASP B 2 103 ? 57.861 -13.522 103.895 1.00 54.55  ? 100 ASP B CA  1 
ATOM   2000 C C   . ASP B 2 103 ? 56.590 -13.529 103.045 1.00 56.71  ? 100 ASP B C   1 
ATOM   2001 O O   . ASP B 2 103 ? 56.556 -12.895 101.978 1.00 56.33  ? 100 ASP B O   1 
ATOM   2002 C CB  . ASP B 2 103 ? 58.693 -14.779 103.594 1.00 61.01  ? 100 ASP B CB  1 
ATOM   2003 C CG  . ASP B 2 103 ? 60.159 -14.620 103.959 1.00 61.38  ? 100 ASP B CG  1 
ATOM   2004 O OD1 . ASP B 2 103 ? 60.545 -13.644 104.629 1.00 67.74  ? 100 ASP B OD1 1 
ATOM   2005 O OD2 . ASP B 2 103 ? 60.925 -15.502 103.580 1.00 70.01  ? 100 ASP B OD2 1 
ATOM   2006 N N   . LEU B 2 104 ? 55.557 -14.237 103.521 1.00 52.74  ? 101 LEU B N   1 
ATOM   2007 C CA  . LEU B 2 104 ? 54.263 -14.215 102.885 1.00 51.77  ? 101 LEU B CA  1 
ATOM   2008 C C   . LEU B 2 104 ? 53.715 -12.739 102.822 1.00 50.71  ? 101 LEU B C   1 
ATOM   2009 O O   . LEU B 2 104 ? 53.278 -12.280 101.757 1.00 46.87  ? 101 LEU B O   1 
ATOM   2010 C CB  . LEU B 2 104 ? 53.308 -15.115 103.650 1.00 53.19  ? 101 LEU B CB  1 
ATOM   2011 C CG  . LEU B 2 104 ? 51.882 -15.133 103.124 1.00 60.52  ? 101 LEU B CG  1 
ATOM   2012 C CD1 . LEU B 2 104 ? 51.936 -15.706 101.738 1.00 62.87  ? 101 LEU B CD1 1 
ATOM   2013 C CD2 . LEU B 2 104 ? 50.916 -15.909 104.002 1.00 64.01  ? 101 LEU B CD2 1 
ATOM   2014 N N   . GLY B 2 105 ? 53.801 -12.029 103.954 1.00 44.00  ? 102 GLY B N   1 
ATOM   2015 C CA  . GLY B 2 105 ? 53.407 -10.624 104.070 1.00 46.77  ? 102 GLY B CA  1 
ATOM   2016 C C   . GLY B 2 105 ? 54.063 -9.720  103.031 1.00 52.42  ? 102 GLY B C   1 
ATOM   2017 O O   . GLY B 2 105 ? 53.369 -8.944  102.377 1.00 46.03  ? 102 GLY B O   1 
ATOM   2018 N N   . ARG B 2 106 ? 55.385 -9.853  102.874 1.00 44.95  ? 103 ARG B N   1 
ATOM   2019 C CA  . ARG B 2 106 ? 56.144 -9.110  101.890 1.00 54.70  ? 103 ARG B CA  1 
ATOM   2020 C C   . ARG B 2 106 ? 55.773 -9.529  100.493 1.00 55.58  ? 103 ARG B C   1 
ATOM   2021 O O   . ARG B 2 106 ? 55.667 -8.671  99.629  1.00 53.01  ? 103 ARG B O   1 
ATOM   2022 C CB  . ARG B 2 106 ? 57.667 -9.361  102.021 1.00 60.22  ? 103 ARG B CB  1 
ATOM   2023 C CG  . ARG B 2 106 ? 58.419 -8.520  103.044 1.00 63.10  ? 103 ARG B CG  1 
ATOM   2024 C CD  . ARG B 2 106 ? 59.899 -8.918  103.062 1.00 68.51  ? 103 ARG B CD  1 
ATOM   2025 N NE  . ARG B 2 106 ? 60.108 -10.080 103.919 1.00 65.14  ? 103 ARG B NE  1 
ATOM   2026 C CZ  . ARG B 2 106 ? 60.198 -10.013 105.246 1.00 71.65  ? 103 ARG B CZ  1 
ATOM   2027 N NH1 . ARG B 2 106 ? 60.143 -8.834  105.893 1.00 68.92  ? 103 ARG B NH1 1 
ATOM   2028 N NH2 . ARG B 2 106 ? 60.341 -11.139 105.935 1.00 78.91  ? 103 ARG B NH2 1 
ATOM   2029 N N   . GLU B 2 107 ? 55.606 -10.839 100.270 1.00 52.94  ? 104 GLU B N   1 
ATOM   2030 C CA  . GLU B 2 107 ? 55.380 -11.361 98.923  1.00 53.26  ? 104 GLU B CA  1 
ATOM   2031 C C   . GLU B 2 107 ? 54.132 -10.759 98.314  1.00 49.62  ? 104 GLU B C   1 
ATOM   2032 O O   . GLU B 2 107 ? 53.958 -10.776 97.118  1.00 53.90  ? 104 GLU B O   1 
ATOM   2033 C CB  . GLU B 2 107 ? 55.192 -12.897 98.931  1.00 61.46  ? 104 GLU B CB  1 
ATOM   2034 C CG  . GLU B 2 107 ? 56.446 -13.762 99.033  1.00 67.93  ? 104 GLU B CG  1 
ATOM   2035 C CD  . GLU B 2 107 ? 56.145 -15.259 99.054  1.00 77.10  ? 104 GLU B CD  1 
ATOM   2036 O OE1 . GLU B 2 107 ? 55.046 -15.666 99.473  1.00 82.03  ? 104 GLU B OE1 1 
ATOM   2037 O OE2 . GLU B 2 107 ? 57.009 -16.053 98.632  1.00 92.28  ? 104 GLU B OE2 1 
ATOM   2038 N N   . LEU B 2 108 ? 53.228 -10.281 99.155  1.00 47.38  ? 105 LEU B N   1 
ATOM   2039 C CA  . LEU B 2 108 ? 51.894 -9.977  98.721  1.00 44.43  ? 105 LEU B CA  1 
ATOM   2040 C C   . LEU B 2 108 ? 51.744 -8.531  98.258  1.00 44.60  ? 105 LEU B C   1 
ATOM   2041 O O   . LEU B 2 108 ? 50.716 -8.185  97.648  1.00 49.06  ? 105 LEU B O   1 
ATOM   2042 C CB  . LEU B 2 108 ? 50.934 -10.288 99.854  1.00 43.74  ? 105 LEU B CB  1 
ATOM   2043 C CG  . LEU B 2 108 ? 50.124 -11.585 99.813  1.00 46.78  ? 105 LEU B CG  1 
ATOM   2044 C CD1 . LEU B 2 108 ? 50.757 -12.679 99.055  1.00 47.32  ? 105 LEU B CD1 1 
ATOM   2045 C CD2 . LEU B 2 108 ? 49.727 -12.059 101.181 1.00 43.89  ? 105 LEU B CD2 1 
ATOM   2046 N N   . GLU B 2 109 ? 52.759 -7.704  98.530  1.00 43.14  ? 106 GLU B N   1 
ATOM   2047 C CA  . GLU B 2 109 ? 52.744 -6.296  98.137  1.00 45.50  ? 106 GLU B CA  1 
ATOM   2048 C C   . GLU B 2 109 ? 52.350 -6.051  96.694  1.00 47.19  ? 106 GLU B C   1 
ATOM   2049 O O   . GLU B 2 109 ? 51.337 -5.352  96.435  1.00 42.29  ? 106 GLU B O   1 
ATOM   2050 C CB  . GLU B 2 109 ? 54.062 -5.619  98.354  1.00 42.75  ? 106 GLU B CB  1 
ATOM   2051 C CG  . GLU B 2 109 ? 53.922 -4.106  98.270  1.00 51.11  ? 106 GLU B CG  1 
ATOM   2052 C CD  . GLU B 2 109 ? 55.108 -3.372  98.843  1.00 47.75  ? 106 GLU B CD  1 
ATOM   2053 O OE1 . GLU B 2 109 ? 56.097 -4.027  98.970  1.00 46.43  ? 106 GLU B OE1 1 
ATOM   2054 O OE2 . GLU B 2 109 ? 55.043 -2.172  99.167  1.00 47.20  ? 106 GLU B OE2 1 
ATOM   2055 N N   . GLU B 2 110 ? 53.134 -6.612  95.775  1.00 47.29  ? 107 GLU B N   1 
ATOM   2056 C CA  . GLU B 2 110 ? 52.886 -6.425  94.353  1.00 51.06  ? 107 GLU B CA  1 
ATOM   2057 C C   . GLU B 2 110 ? 51.501 -6.909  94.045  1.00 42.38  ? 107 GLU B C   1 
ATOM   2058 O O   . GLU B 2 110 ? 50.707 -6.171  93.527  1.00 39.35  ? 107 GLU B O   1 
ATOM   2059 C CB  . GLU B 2 110 ? 53.923 -7.138  93.443  1.00 63.79  ? 107 GLU B CB  1 
ATOM   2060 C CG  . GLU B 2 110 ? 55.094 -6.269  92.975  1.00 83.94  ? 107 GLU B CG  1 
ATOM   2061 C CD  . GLU B 2 110 ? 56.316 -7.061  92.446  1.00 103.31 ? 107 GLU B CD  1 
ATOM   2062 O OE1 . GLU B 2 110 ? 56.168 -8.097  91.734  1.00 104.72 ? 107 GLU B OE1 1 
ATOM   2063 O OE2 . GLU B 2 110 ? 57.459 -6.625  92.733  1.00 115.51 ? 107 GLU B OE2 1 
ATOM   2064 N N   . PRO B 2 111 ? 51.194 -8.166  94.369  1.00 45.47  ? 108 PRO B N   1 
ATOM   2065 C CA  . PRO B 2 111 ? 49.912 -8.660  93.884  1.00 40.49  ? 108 PRO B CA  1 
ATOM   2066 C C   . PRO B 2 111 ? 48.689 -7.970  94.473  1.00 39.93  ? 108 PRO B C   1 
ATOM   2067 O O   . PRO B 2 111 ? 47.722 -7.754  93.755  1.00 41.72  ? 108 PRO B O   1 
ATOM   2068 C CB  . PRO B 2 111 ? 49.921 -10.145 94.286  1.00 40.76  ? 108 PRO B CB  1 
ATOM   2069 C CG  . PRO B 2 111 ? 51.067 -10.318 95.176  1.00 44.05  ? 108 PRO B CG  1 
ATOM   2070 C CD  . PRO B 2 111 ? 52.060 -9.262  94.837  1.00 46.56  ? 108 PRO B CD  1 
ATOM   2071 N N   . LEU B 2 112 ? 48.704 -7.655  95.754  1.00 34.11  ? 109 LEU B N   1 
ATOM   2072 C CA  . LEU B 2 112 ? 47.521 -7.087  96.320  1.00 37.52  ? 109 LEU B CA  1 
ATOM   2073 C C   . LEU B 2 112 ? 47.440 -5.629  95.881  1.00 34.77  ? 109 LEU B C   1 
ATOM   2074 O O   . LEU B 2 112 ? 46.370 -5.166  95.555  1.00 36.51  ? 109 LEU B O   1 
ATOM   2075 C CB  . LEU B 2 112 ? 47.488 -7.215  97.836  1.00 38.68  ? 109 LEU B CB  1 
ATOM   2076 C CG  . LEU B 2 112 ? 47.550 -8.617  98.424  1.00 40.06  ? 109 LEU B CG  1 
ATOM   2077 C CD1 . LEU B 2 112 ? 47.647 -8.544  99.939  1.00 41.16  ? 109 LEU B CD1 1 
ATOM   2078 C CD2 . LEU B 2 112 ? 46.301 -9.375  98.033  1.00 43.34  ? 109 LEU B CD2 1 
ATOM   2079 N N   . ASN B 2 113 ? 48.550 -4.910  95.802  1.00 33.77  ? 110 ASN B N   1 
ATOM   2080 C CA  . ASN B 2 113 ? 48.479 -3.553  95.204  1.00 34.74  ? 110 ASN B CA  1 
ATOM   2081 C C   . ASN B 2 113 ? 48.004 -3.556  93.785  1.00 36.53  ? 110 ASN B C   1 
ATOM   2082 O O   . ASN B 2 113 ? 47.271 -2.637  93.394  1.00 40.61  ? 110 ASN B O   1 
ATOM   2083 C CB  . ASN B 2 113 ? 49.800 -2.849  95.229  1.00 32.44  ? 110 ASN B CB  1 
ATOM   2084 C CG  . ASN B 2 113 ? 50.113 -2.287  96.583  1.00 34.73  ? 110 ASN B CG  1 
ATOM   2085 O OD1 . ASN B 2 113 ? 49.210 -2.024  97.420  1.00 33.80  ? 110 ASN B OD1 1 
ATOM   2086 N ND2 . ASN B 2 113 ? 51.403 -2.105  96.826  1.00 33.03  ? 110 ASN B ND2 1 
ATOM   2087 N N   . GLU B 2 114 ? 48.323 -4.602  93.022  1.00 36.95  ? 111 GLU B N   1 
ATOM   2088 C CA  . GLU B 2 114 ? 47.848 -4.629  91.652  1.00 41.24  ? 111 GLU B CA  1 
ATOM   2089 C C   . GLU B 2 114 ? 46.357 -4.743  91.625  1.00 40.09  ? 111 GLU B C   1 
ATOM   2090 O O   . GLU B 2 114 ? 45.647 -4.049  90.831  1.00 41.49  ? 111 GLU B O   1 
ATOM   2091 C CB  . GLU B 2 114 ? 48.458 -5.734  90.839  1.00 49.42  ? 111 GLU B CB  1 
ATOM   2092 C CG  . GLU B 2 114 ? 48.636 -5.337  89.375  1.00 67.63  ? 111 GLU B CG  1 
ATOM   2093 C CD  . GLU B 2 114 ? 49.476 -6.357  88.596  1.00 87.95  ? 111 GLU B CD  1 
ATOM   2094 O OE1 . GLU B 2 114 ? 48.901 -6.870  87.604  1.00 86.83  ? 111 GLU B OE1 1 
ATOM   2095 O OE2 . GLU B 2 114 ? 50.675 -6.674  88.974  1.00 81.76  ? 111 GLU B OE2 1 
ATOM   2096 N N   . ILE B 2 115 ? 45.842 -5.617  92.475  1.00 35.02  ? 112 ILE B N   1 
ATOM   2097 C CA  . ILE B 2 115 ? 44.401 -5.853  92.430  1.00 33.88  ? 112 ILE B CA  1 
ATOM   2098 C C   . ILE B 2 115 ? 43.679 -4.605  92.903  1.00 33.33  ? 112 ILE B C   1 
ATOM   2099 O O   . ILE B 2 115 ? 42.641 -4.222  92.341  1.00 33.20  ? 112 ILE B O   1 
ATOM   2100 C CB  . ILE B 2 115 ? 44.029 -7.032  93.301  1.00 31.89  ? 112 ILE B CB  1 
ATOM   2101 C CG1 . ILE B 2 115 ? 44.619 -8.275  92.672  1.00 33.28  ? 112 ILE B CG1 1 
ATOM   2102 C CG2 . ILE B 2 115 ? 42.533 -7.120  93.514  1.00 29.24  ? 112 ILE B CG2 1 
ATOM   2103 C CD1 . ILE B 2 115 ? 44.597 -9.457  93.580  1.00 36.53  ? 112 ILE B CD1 1 
ATOM   2104 N N   . ALA B 2 116 ? 44.227 -3.948  93.914  1.00 31.04  ? 113 ALA B N   1 
ATOM   2105 C CA  . ALA B 2 116 ? 43.505 -2.785  94.444  1.00 35.63  ? 113 ALA B CA  1 
ATOM   2106 C C   . ALA B 2 116 ? 43.549 -1.635  93.417  1.00 37.83  ? 113 ALA B C   1 
ATOM   2107 O O   . ALA B 2 116 ? 42.510 -1.005  93.208  1.00 37.18  ? 113 ALA B O   1 
ATOM   2108 C CB  . ALA B 2 116 ? 44.037 -2.393  95.803  1.00 37.62  ? 113 ALA B CB  1 
ATOM   2109 N N   . SER B 2 117 ? 44.698 -1.420  92.729  1.00 37.76  ? 114 SER B N   1 
ATOM   2110 C CA  . SER B 2 117 ? 44.753 -0.539  91.517  1.00 41.23  ? 114 SER B CA  1 
ATOM   2111 C C   . SER B 2 117 ? 43.657 -0.761  90.528  1.00 39.31  ? 114 SER B C   1 
ATOM   2112 O O   . SER B 2 117 ? 43.040 0.178   90.024  1.00 38.01  ? 114 SER B O   1 
ATOM   2113 C CB  . SER B 2 117 ? 45.984 -0.767  90.691  1.00 43.80  ? 114 SER B CB  1 
ATOM   2114 O OG  . SER B 2 117 ? 46.910 0.141   91.111  1.00 60.37  ? 114 SER B OG  1 
ATOM   2115 N N   . ILE B 2 118 ? 43.416 -2.019  90.217  1.00 41.49  ? 115 ILE B N   1 
ATOM   2116 C CA  . ILE B 2 118 ? 42.424 -2.321  89.195  1.00 39.65  ? 115 ILE B CA  1 
ATOM   2117 C C   . ILE B 2 118 ? 41.090 -1.939  89.751  1.00 37.35  ? 115 ILE B C   1 
ATOM   2118 O O   . ILE B 2 118 ? 40.280 -1.308  89.082  1.00 40.08  ? 115 ILE B O   1 
ATOM   2119 C CB  . ILE B 2 118 ? 42.521 -3.790  88.774  1.00 42.19  ? 115 ILE B CB  1 
ATOM   2120 C CG1 . ILE B 2 118 ? 43.791 -3.954  87.929  1.00 46.22  ? 115 ILE B CG1 1 
ATOM   2121 C CG2 . ILE B 2 118 ? 41.314 -4.251  87.986  1.00 39.19  ? 115 ILE B CG2 1 
ATOM   2122 C CD1 . ILE B 2 118 ? 44.225 -5.390  87.792  1.00 48.98  ? 115 ILE B CD1 1 
ATOM   2123 N N   . TYR B 2 119 ? 40.864 -2.312  90.999  1.00 38.34  ? 116 TYR B N   1 
ATOM   2124 C CA  . TYR B 2 119 ? 39.636 -1.911  91.656  1.00 35.75  ? 116 TYR B CA  1 
ATOM   2125 C C   . TYR B 2 119 ? 39.504 -0.378  91.698  1.00 35.54  ? 116 TYR B C   1 
ATOM   2126 O O   . TYR B 2 119 ? 38.456 0.153   91.331  1.00 32.78  ? 116 TYR B O   1 
ATOM   2127 C CB  . TYR B 2 119 ? 39.565 -2.489  93.043  1.00 34.51  ? 116 TYR B CB  1 
ATOM   2128 C CG  . TYR B 2 119 ? 38.355 -1.985  93.735  1.00 40.55  ? 116 TYR B CG  1 
ATOM   2129 C CD1 . TYR B 2 119 ? 37.120 -2.463  93.389  1.00 43.68  ? 116 TYR B CD1 1 
ATOM   2130 C CD2 . TYR B 2 119 ? 38.441 -0.986  94.713  1.00 39.89  ? 116 TYR B CD2 1 
ATOM   2131 C CE1 . TYR B 2 119 ? 36.000 -2.012  94.017  1.00 45.67  ? 116 TYR B CE1 1 
ATOM   2132 C CE2 . TYR B 2 119 ? 37.333 -0.516  95.312  1.00 39.32  ? 116 TYR B CE2 1 
ATOM   2133 C CZ  . TYR B 2 119 ? 36.111 -1.027  94.963  1.00 44.00  ? 116 TYR B CZ  1 
ATOM   2134 O OH  . TYR B 2 119 ? 34.936 -0.547  95.542  1.00 50.69  ? 116 TYR B OH  1 
ATOM   2135 N N   . ALA B 2 120 ? 40.541 0.332   92.132  1.00 32.70  ? 117 ALA B N   1 
ATOM   2136 C CA  . ALA B 2 120 ? 40.412 1.780   92.283  1.00 36.79  ? 117 ALA B CA  1 
ATOM   2137 C C   . ALA B 2 120 ? 40.023 2.471   90.944  1.00 43.58  ? 117 ALA B C   1 
ATOM   2138 O O   . ALA B 2 120 ? 39.085 3.327   90.866  1.00 40.80  ? 117 ALA B O   1 
ATOM   2139 C CB  . ALA B 2 120 ? 41.677 2.353   92.833  1.00 36.12  ? 117 ALA B CB  1 
ATOM   2140 N N   . THR B 2 121 ? 40.666 2.029   89.878  1.00 43.81  ? 118 THR B N   1 
ATOM   2141 C CA  . THR B 2 121 ? 40.533 2.722   88.589  1.00 44.50  ? 118 THR B CA  1 
ATOM   2142 C C   . THR B 2 121 ? 39.178 2.539   88.061  1.00 36.62  ? 118 THR B C   1 
ATOM   2143 O O   . THR B 2 121 ? 38.618 3.447   87.494  1.00 37.56  ? 118 THR B O   1 
ATOM   2144 C CB  . THR B 2 121 ? 41.600 2.310   87.540  1.00 49.14  ? 118 THR B CB  1 
ATOM   2145 O OG1 . THR B 2 121 ? 42.865 2.728   88.066  1.00 66.76  ? 118 THR B OG1 1 
ATOM   2146 C CG2 . THR B 2 121 ? 41.420 3.062   86.250  1.00 42.91  ? 118 THR B CG2 1 
ATOM   2147 N N   . GLU B 2 122 ? 38.625 1.372   88.238  1.00 36.14  ? 119 GLU B N   1 
ATOM   2148 C CA  . GLU B 2 122 ? 37.307 1.152   87.710  1.00 39.60  ? 119 GLU B CA  1 
ATOM   2149 C C   . GLU B 2 122 ? 36.357 1.888   88.618  1.00 39.52  ? 119 GLU B C   1 
ATOM   2150 O O   . GLU B 2 122 ? 35.436 2.482   88.126  1.00 43.55  ? 119 GLU B O   1 
ATOM   2151 C CB  . GLU B 2 122 ? 36.997 -0.329  87.611  1.00 46.00  ? 119 GLU B CB  1 
ATOM   2152 C CG  . GLU B 2 122 ? 37.838 -1.022  86.505  1.00 57.80  ? 119 GLU B CG  1 
ATOM   2153 C CD  . GLU B 2 122 ? 37.457 -0.565  85.063  1.00 61.88  ? 119 GLU B CD  1 
ATOM   2154 O OE1 . GLU B 2 122 ? 36.251 -0.250  84.849  1.00 69.20  ? 119 GLU B OE1 1 
ATOM   2155 O OE2 . GLU B 2 122 ? 38.351 -0.493  84.151  1.00 47.22  ? 119 GLU B OE2 1 
ATOM   2156 N N   . THR B 2 123 ? 36.614 1.915   89.931  1.00 38.18  ? 120 THR B N   1 
ATOM   2157 C CA  . THR B 2 123 ? 35.631 2.421   90.898  1.00 34.65  ? 120 THR B CA  1 
ATOM   2158 C C   . THR B 2 123 ? 35.535 3.931   90.800  1.00 35.43  ? 120 THR B C   1 
ATOM   2159 O O   . THR B 2 123 ? 34.493 4.455   90.981  1.00 34.25  ? 120 THR B O   1 
ATOM   2160 C CB  . THR B 2 123 ? 36.002 2.052   92.337  1.00 36.75  ? 120 THR B CB  1 
ATOM   2161 O OG1 . THR B 2 123 ? 36.083 0.623   92.487  1.00 39.55  ? 120 THR B OG1 1 
ATOM   2162 C CG2 . THR B 2 123 ? 34.996 2.561   93.246  1.00 38.56  ? 120 THR B CG2 1 
ATOM   2163 N N   . PHE B 2 124 ? 36.633 4.602   90.491  1.00 36.18  ? 121 PHE B N   1 
ATOM   2164 C CA  . PHE B 2 124 ? 36.648 6.036   90.381  1.00 39.61  ? 121 PHE B CA  1 
ATOM   2165 C C   . PHE B 2 124 ? 36.600 6.586   88.929  1.00 37.97  ? 121 PHE B C   1 
ATOM   2166 O O   . PHE B 2 124 ? 36.921 7.729   88.682  1.00 29.89  ? 121 PHE B O   1 
ATOM   2167 C CB  . PHE B 2 124 ? 37.897 6.566   91.111  1.00 41.29  ? 121 PHE B CB  1 
ATOM   2168 C CG  . PHE B 2 124 ? 37.747 6.556   92.604  1.00 39.32  ? 121 PHE B CG  1 
ATOM   2169 C CD1 . PHE B 2 124 ? 38.109 5.445   93.346  1.00 39.37  ? 121 PHE B CD1 1 
ATOM   2170 C CD2 . PHE B 2 124 ? 37.242 7.641   93.255  1.00 37.93  ? 121 PHE B CD2 1 
ATOM   2171 C CE1 . PHE B 2 124 ? 38.000 5.450   94.733  1.00 42.01  ? 121 PHE B CE1 1 
ATOM   2172 C CE2 . PHE B 2 124 ? 37.108 7.648   94.630  1.00 43.13  ? 121 PHE B CE2 1 
ATOM   2173 C CZ  . PHE B 2 124 ? 37.477 6.545   95.381  1.00 40.69  ? 121 PHE B CZ  1 
ATOM   2174 N N   . LYS B 2 125 ? 36.172 5.797   87.974  1.00 36.87  ? 122 LYS B N   1 
ATOM   2175 C CA  . LYS B 2 125 ? 36.386 6.216   86.595  1.00 42.99  ? 122 LYS B CA  1 
ATOM   2176 C C   . LYS B 2 125 ? 35.500 7.411   86.205  1.00 45.38  ? 122 LYS B C   1 
ATOM   2177 O O   . LYS B 2 125 ? 35.896 8.171   85.344  1.00 36.64  ? 122 LYS B O   1 
ATOM   2178 C CB  . LYS B 2 125 ? 36.168 5.056   85.597  1.00 43.23  ? 122 LYS B CB  1 
ATOM   2179 C CG  . LYS B 2 125 ? 34.773 4.509   85.636  1.00 43.72  ? 122 LYS B CG  1 
ATOM   2180 C CD  . LYS B 2 125 ? 34.500 3.316   84.730  1.00 48.99  ? 122 LYS B CD  1 
ATOM   2181 C CE  . LYS B 2 125 ? 33.003 3.316   84.491  1.00 52.57  ? 122 LYS B CE  1 
ATOM   2182 N NZ  . LYS B 2 125 ? 32.496 1.989   84.213  1.00 62.22  ? 122 LYS B NZ  1 
ATOM   2183 N N   . SER B 2 126 ? 34.324 7.569   86.825  1.00 44.87  ? 123 SER B N   1 
ATOM   2184 C CA  . SER B 2 126 ? 33.432 8.718   86.538  1.00 46.94  ? 123 SER B CA  1 
ATOM   2185 C C   . SER B 2 126 ? 33.814 10.002  87.261  1.00 50.55  ? 123 SER B C   1 
ATOM   2186 O O   . SER B 2 126 ? 33.076 10.975  87.157  1.00 47.69  ? 123 SER B O   1 
ATOM   2187 C CB  . SER B 2 126 ? 32.017 8.423   87.009  1.00 48.44  ? 123 SER B CB  1 
ATOM   2188 O OG  . SER B 2 126 ? 31.529 7.367   86.261  1.00 63.42  ? 123 SER B OG  1 
ATOM   2189 N N   . ILE B 2 127 ? 34.906 9.967   88.027  1.00 42.39  ? 124 ILE B N   1 
ATOM   2190 C CA  . ILE B 2 127 ? 35.312 11.038  88.867  1.00 45.24  ? 124 ILE B CA  1 
ATOM   2191 C C   . ILE B 2 127 ? 36.569 11.631  88.240  1.00 46.47  ? 124 ILE B C   1 
ATOM   2192 O O   . ILE B 2 127 ? 37.417 10.875  87.827  1.00 52.20  ? 124 ILE B O   1 
ATOM   2193 C CB  . ILE B 2 127 ? 35.701 10.526  90.272  1.00 42.89  ? 124 ILE B CB  1 
ATOM   2194 C CG1 . ILE B 2 127 ? 34.526 9.898   90.952  1.00 46.73  ? 124 ILE B CG1 1 
ATOM   2195 C CG2 . ILE B 2 127 ? 36.185 11.659  91.142  1.00 42.47  ? 124 ILE B CG2 1 
ATOM   2196 C CD1 . ILE B 2 127 ? 33.354 10.805  90.950  1.00 52.86  ? 124 ILE B CD1 1 
ATOM   2197 N N   . SER B 2 128 ? 36.714 12.961  88.260  1.00 41.85  ? 125 SER B N   1 
ATOM   2198 C CA  . SER B 2 128 ? 37.837 13.627  87.666  1.00 39.75  ? 125 SER B CA  1 
ATOM   2199 C C   . SER B 2 128 ? 38.852 13.802  88.706  1.00 42.02  ? 125 SER B C   1 
ATOM   2200 O O   . SER B 2 128 ? 38.507 13.970  89.875  1.00 37.65  ? 125 SER B O   1 
ATOM   2201 C CB  . SER B 2 128 ? 37.478 15.015  87.149  1.00 41.20  ? 125 SER B CB  1 
ATOM   2202 O OG  . SER B 2 128 ? 36.763 14.875  85.924  1.00 56.73  ? 125 SER B OG  1 
ATOM   2203 N N   . ASP B 2 129 ? 40.106 13.823  88.276  1.00 37.25  ? 126 ASP B N   1 
ATOM   2204 C CA  . ASP B 2 129 ? 41.173 14.005  89.166  1.00 42.69  ? 126 ASP B CA  1 
ATOM   2205 C C   . ASP B 2 129 ? 40.952 15.182  90.110  1.00 42.79  ? 126 ASP B C   1 
ATOM   2206 O O   . ASP B 2 129 ? 41.305 15.144  91.300  1.00 47.29  ? 126 ASP B O   1 
ATOM   2207 C CB  . ASP B 2 129 ? 42.460 14.203  88.358  1.00 49.97  ? 126 ASP B CB  1 
ATOM   2208 C CG  . ASP B 2 129 ? 43.694 14.300  89.272  1.00 66.67  ? 126 ASP B CG  1 
ATOM   2209 O OD1 . ASP B 2 129 ? 43.825 13.428  90.177  1.00 69.40  ? 126 ASP B OD1 1 
ATOM   2210 O OD2 . ASP B 2 129 ? 44.512 15.261  89.127  1.00 71.23  ? 126 ASP B OD2 1 
ATOM   2211 N N   . GLU B 2 130 ? 40.380 16.252  89.596  1.00 42.46  ? 127 GLU B N   1 
ATOM   2212 C CA  . GLU B 2 130 ? 40.404 17.498  90.318  1.00 45.59  ? 127 GLU B CA  1 
ATOM   2213 C C   . GLU B 2 130 ? 39.289 17.495  91.346  1.00 46.26  ? 127 GLU B C   1 
ATOM   2214 O O   . GLU B 2 130 ? 39.289 18.330  92.251  1.00 51.10  ? 127 GLU B O   1 
ATOM   2215 C CB  . GLU B 2 130 ? 40.230 18.679  89.356  1.00 52.18  ? 127 GLU B CB  1 
ATOM   2216 C CG  . GLU B 2 130 ? 40.825 18.468  87.959  1.00 54.19  ? 127 GLU B CG  1 
ATOM   2217 C CD  . GLU B 2 130 ? 42.244 18.886  87.878  1.00 60.49  ? 127 GLU B CD  1 
ATOM   2218 O OE1 . GLU B 2 130 ? 42.830 18.758  86.781  1.00 73.37  ? 127 GLU B OE1 1 
ATOM   2219 O OE2 . GLU B 2 130 ? 42.763 19.373  88.898  1.00 65.01  ? 127 GLU B OE2 1 
ATOM   2220 N N   . GLU B 2 131 ? 38.325 16.578  91.215  1.00 43.09  ? 128 GLU B N   1 
ATOM   2221 C CA  . GLU B 2 131 ? 37.268 16.415  92.216  1.00 38.71  ? 128 GLU B CA  1 
ATOM   2222 C C   . GLU B 2 131 ? 37.760 15.735  93.463  1.00 41.93  ? 128 GLU B C   1 
ATOM   2223 O O   . GLU B 2 131 ? 37.169 15.849  94.537  1.00 45.23  ? 128 GLU B O   1 
ATOM   2224 C CB  . GLU B 2 131 ? 36.101 15.662  91.661  1.00 37.34  ? 128 GLU B CB  1 
ATOM   2225 C CG  . GLU B 2 131 ? 35.460 16.409  90.499  1.00 42.65  ? 128 GLU B CG  1 
ATOM   2226 C CD  . GLU B 2 131 ? 34.370 15.637  89.859  1.00 44.61  ? 128 GLU B CD  1 
ATOM   2227 O OE1 . GLU B 2 131 ? 34.733 14.631  89.214  1.00 54.33  ? 128 GLU B OE1 1 
ATOM   2228 O OE2 . GLU B 2 131 ? 33.172 15.975  90.043  1.00 47.72  ? 128 GLU B OE2 1 
ATOM   2229 N N   . LEU B 2 132 ? 38.867 15.043  93.366  1.00 39.18  ? 129 LEU B N   1 
ATOM   2230 C CA  . LEU B 2 132 ? 39.292 14.320  94.546  1.00 39.56  ? 129 LEU B CA  1 
ATOM   2231 C C   . LEU B 2 132 ? 39.564 15.214  95.729  1.00 37.95  ? 129 LEU B C   1 
ATOM   2232 O O   . LEU B 2 132 ? 39.197 14.844  96.798  1.00 36.74  ? 129 LEU B O   1 
ATOM   2233 C CB  . LEU B 2 132 ? 40.520 13.457  94.284  1.00 37.37  ? 129 LEU B CB  1 
ATOM   2234 C CG  . LEU B 2 132 ? 40.191 12.325  93.358  1.00 38.10  ? 129 LEU B CG  1 
ATOM   2235 C CD1 . LEU B 2 132 ? 41.527 11.706  93.057  1.00 45.07  ? 129 LEU B CD1 1 
ATOM   2236 C CD2 . LEU B 2 132 ? 39.199 11.380  93.941  1.00 38.63  ? 129 LEU B CD2 1 
ATOM   2237 N N   . PRO B 2 133 ? 40.250 16.376  95.549  1.00 39.24  ? 130 PRO B N   1 
ATOM   2238 C CA  . PRO B 2 133 ? 40.578 17.136  96.721  1.00 36.71  ? 130 PRO B CA  1 
ATOM   2239 C C   . PRO B 2 133 ? 39.379 17.836  97.258  1.00 40.31  ? 130 PRO B C   1 
ATOM   2240 O O   . PRO B 2 133 ? 39.373 18.260  98.409  1.00 51.34  ? 130 PRO B O   1 
ATOM   2241 C CB  . PRO B 2 133 ? 41.593 18.131  96.211  1.00 40.26  ? 130 PRO B CB  1 
ATOM   2242 C CG  . PRO B 2 133 ? 42.145 17.576  94.993  1.00 35.79  ? 130 PRO B CG  1 
ATOM   2243 C CD  . PRO B 2 133 ? 40.990 16.877  94.389  1.00 38.12  ? 130 PRO B CD  1 
ATOM   2244 N N   . LEU B 2 134 ? 38.362 17.982  96.433  1.00 42.44  ? 131 LEU B N   1 
ATOM   2245 C CA  . LEU B 2 134 ? 37.138 18.574  96.914  1.00 48.44  ? 131 LEU B CA  1 
ATOM   2246 C C   . LEU B 2 134 ? 36.424 17.604  97.868  1.00 47.29  ? 131 LEU B C   1 
ATOM   2247 O O   . LEU B 2 134 ? 36.012 17.953  99.008  1.00 45.53  ? 131 LEU B O   1 
ATOM   2248 C CB  . LEU B 2 134 ? 36.230 18.895  95.726  1.00 54.00  ? 131 LEU B CB  1 
ATOM   2249 C CG  . LEU B 2 134 ? 36.059 20.385  95.630  1.00 63.08  ? 131 LEU B CG  1 
ATOM   2250 C CD1 . LEU B 2 134 ? 35.081 20.628  94.490  1.00 69.21  ? 131 LEU B CD1 1 
ATOM   2251 C CD2 . LEU B 2 134 ? 35.604 20.964  96.987  1.00 60.29  ? 131 LEU B CD2 1 
ATOM   2252 N N   . PHE B 2 135 ? 36.323 16.385  97.354  1.00 34.87  ? 132 PHE B N   1 
ATOM   2253 C CA  . PHE B 2 135 ? 35.670 15.346  97.992  1.00 37.77  ? 132 PHE B CA  1 
ATOM   2254 C C   . PHE B 2 135 ? 36.332 15.137  99.342  1.00 38.26  ? 132 PHE B C   1 
ATOM   2255 O O   . PHE B 2 135 ? 35.748 15.165  100.397 1.00 36.63  ? 132 PHE B O   1 
ATOM   2256 C CB  . PHE B 2 135 ? 35.803 14.126  97.105  1.00 35.90  ? 132 PHE B CB  1 
ATOM   2257 C CG  . PHE B 2 135 ? 35.153 12.918  97.666  1.00 35.06  ? 132 PHE B CG  1 
ATOM   2258 C CD1 . PHE B 2 135 ? 33.789 12.921  97.954  1.00 38.42  ? 132 PHE B CD1 1 
ATOM   2259 C CD2 . PHE B 2 135 ? 35.868 11.795  97.870  1.00 33.36  ? 132 PHE B CD2 1 
ATOM   2260 C CE1 . PHE B 2 135 ? 33.158 11.780  98.430  1.00 35.51  ? 132 PHE B CE1 1 
ATOM   2261 C CE2 . PHE B 2 135 ? 35.280 10.664  98.361  1.00 37.58  ? 132 PHE B CE2 1 
ATOM   2262 C CZ  . PHE B 2 135 ? 33.919 10.655  98.645  1.00 40.45  ? 132 PHE B CZ  1 
ATOM   2263 N N   . THR B 2 136 ? 37.610 15.006  99.272  1.00 39.32  ? 133 THR B N   1 
ATOM   2264 C CA  . THR B 2 136 ? 38.396 14.828  100.426 1.00 40.61  ? 133 THR B CA  1 
ATOM   2265 C C   . THR B 2 136 ? 38.302 15.908  101.480 1.00 40.77  ? 133 THR B C   1 
ATOM   2266 O O   . THR B 2 136 ? 38.352 15.636  102.671 1.00 41.14  ? 133 THR B O   1 
ATOM   2267 C CB  . THR B 2 136 ? 39.818 14.605  99.936  1.00 39.32  ? 133 THR B CB  1 
ATOM   2268 O OG1 . THR B 2 136 ? 39.876 13.195  99.711  1.00 41.03  ? 133 THR B OG1 1 
ATOM   2269 C CG2 . THR B 2 136 ? 40.808 15.013  100.937 1.00 47.79  ? 133 THR B CG2 1 
ATOM   2270 N N   . ASP B 2 137 ? 38.258 17.140  101.050 1.00 40.52  ? 134 ASP B N   1 
ATOM   2271 C CA  . ASP B 2 137 ? 38.258 18.232  101.990 1.00 41.15  ? 134 ASP B CA  1 
ATOM   2272 C C   . ASP B 2 137 ? 36.873 18.341  102.612 1.00 36.88  ? 134 ASP B C   1 
ATOM   2273 O O   . ASP B 2 137 ? 36.776 18.702  103.781 1.00 37.79  ? 134 ASP B O   1 
ATOM   2274 C CB  . ASP B 2 137 ? 38.652 19.546  101.276 1.00 45.63  ? 134 ASP B CB  1 
ATOM   2275 C CG  . ASP B 2 137 ? 38.604 20.720  102.191 1.00 49.30  ? 134 ASP B CG  1 
ATOM   2276 O OD1 . ASP B 2 137 ? 39.539 20.865  103.010 1.00 52.38  ? 134 ASP B OD1 1 
ATOM   2277 O OD2 . ASP B 2 137 ? 37.612 21.480  102.141 1.00 51.27  ? 134 ASP B OD2 1 
ATOM   2278 N N   . ILE B 2 138 ? 35.810 18.068  101.834 1.00 33.75  ? 135 ILE B N   1 
ATOM   2279 C CA  . ILE B 2 138 ? 34.452 17.963  102.388 1.00 33.67  ? 135 ILE B CA  1 
ATOM   2280 C C   . ILE B 2 138 ? 34.419 16.802  103.423 1.00 38.10  ? 135 ILE B C   1 
ATOM   2281 O O   . ILE B 2 138 ? 34.005 16.996  104.536 1.00 36.79  ? 135 ILE B O   1 
ATOM   2282 C CB  . ILE B 2 138 ? 33.405 17.752  101.303 1.00 35.68  ? 135 ILE B CB  1 
ATOM   2283 C CG1 . ILE B 2 138 ? 33.204 19.018  100.448 1.00 33.24  ? 135 ILE B CG1 1 
ATOM   2284 C CG2 . ILE B 2 138 ? 32.079 17.396  101.927 1.00 39.42  ? 135 ILE B CG2 1 
ATOM   2285 C CD1 . ILE B 2 138 ? 32.429 18.801  99.146  1.00 31.32  ? 135 ILE B CD1 1 
ATOM   2286 N N   . LEU B 2 139 ? 34.971 15.639  103.098 1.00 37.17  ? 136 LEU B N   1 
ATOM   2287 C CA  . LEU B 2 139 ? 35.030 14.569  104.064 1.00 37.38  ? 136 LEU B CA  1 
ATOM   2288 C C   . LEU B 2 139 ? 35.698 14.977  105.335 1.00 37.04  ? 136 LEU B C   1 
ATOM   2289 O O   . LEU B 2 139 ? 35.252 14.620  106.428 1.00 44.01  ? 136 LEU B O   1 
ATOM   2290 C CB  . LEU B 2 139 ? 35.777 13.352  103.527 1.00 33.20  ? 136 LEU B CB  1 
ATOM   2291 C CG  . LEU B 2 139 ? 35.066 12.587  102.427 1.00 31.56  ? 136 LEU B CG  1 
ATOM   2292 C CD1 . LEU B 2 139 ? 36.054 11.565  101.928 1.00 31.30  ? 136 LEU B CD1 1 
ATOM   2293 C CD2 . LEU B 2 139 ? 33.775 11.907  102.839 1.00 29.45  ? 136 LEU B CD2 1 
ATOM   2294 N N   . ASP B 2 140 ? 36.782 15.704  105.203 1.00 39.90  ? 137 ASP B N   1 
ATOM   2295 C CA  . ASP B 2 140 ? 37.531 16.224  106.377 1.00 43.67  ? 137 ASP B CA  1 
ATOM   2296 C C   . ASP B 2 140 ? 36.708 17.082  107.286 1.00 39.48  ? 137 ASP B C   1 
ATOM   2297 O O   . ASP B 2 140 ? 36.840 16.969  108.445 1.00 40.37  ? 137 ASP B O   1 
ATOM   2298 C CB  . ASP B 2 140 ? 38.776 17.022  105.980 1.00 53.10  ? 137 ASP B CB  1 
ATOM   2299 C CG  . ASP B 2 140 ? 39.618 17.430  107.202 1.00 66.96  ? 137 ASP B CG  1 
ATOM   2300 O OD1 . ASP B 2 140 ? 40.006 16.516  107.958 1.00 73.60  ? 137 ASP B OD1 1 
ATOM   2301 O OD2 . ASP B 2 140 ? 39.881 18.659  107.420 1.00 77.97  ? 137 ASP B OD2 1 
ATOM   2302 N N   . ARG B 2 141 ? 35.822 17.906  106.749 1.00 40.24  ? 138 ARG B N   1 
ATOM   2303 C CA  . ARG B 2 141 ? 35.093 18.853  107.557 1.00 44.00  ? 138 ARG B CA  1 
ATOM   2304 C C   . ARG B 2 141 ? 33.768 18.284  108.175 1.00 45.85  ? 138 ARG B C   1 
ATOM   2305 O O   . ARG B 2 141 ? 33.066 18.962  108.935 1.00 50.84  ? 138 ARG B O   1 
ATOM   2306 C CB  . ARG B 2 141 ? 34.833 20.121  106.706 1.00 44.42  ? 138 ARG B CB  1 
ATOM   2307 C CG  . ARG B 2 141 ? 36.029 21.062  106.660 1.00 44.84  ? 138 ARG B CG  1 
ATOM   2308 C CD  . ARG B 2 141 ? 36.134 21.810  105.318 1.00 50.67  ? 138 ARG B CD  1 
ATOM   2309 N NE  . ARG B 2 141 ? 34.834 22.280  104.885 1.00 48.02  ? 138 ARG B NE  1 
ATOM   2310 C CZ  . ARG B 2 141 ? 34.394 22.365  103.622 1.00 45.47  ? 138 ARG B CZ  1 
ATOM   2311 N NH1 . ARG B 2 141 ? 35.113 22.013  102.575 1.00 38.12  ? 138 ARG B NH1 1 
ATOM   2312 N NH2 . ARG B 2 141 ? 33.169 22.812  103.414 1.00 47.13  ? 138 ARG B NH2 1 
ATOM   2313 N N   . ILE B 2 142 ? 33.406 17.066  107.819 1.00 45.95  ? 139 ILE B N   1 
ATOM   2314 C CA  . ILE B 2 142 ? 32.265 16.401  108.420 1.00 42.45  ? 139 ILE B CA  1 
ATOM   2315 C C   . ILE B 2 142 ? 32.678 15.812  109.804 1.00 45.68  ? 139 ILE B C   1 
ATOM   2316 O O   . ILE B 2 142 ? 33.693 15.073  109.878 1.00 47.95  ? 139 ILE B O   1 
ATOM   2317 C CB  . ILE B 2 142 ? 31.827 15.300  107.472 1.00 40.52  ? 139 ILE B CB  1 
ATOM   2318 C CG1 . ILE B 2 142 ? 31.264 15.932  106.212 1.00 36.71  ? 139 ILE B CG1 1 
ATOM   2319 C CG2 . ILE B 2 142 ? 30.803 14.407  108.147 1.00 44.52  ? 139 ILE B CG2 1 
ATOM   2320 C CD1 . ILE B 2 142 ? 30.796 14.966  105.152 1.00 36.20  ? 139 ILE B CD1 1 
ATOM   2321 N N   . GLY B 2 143 ? 31.931 16.184  110.863 1.00 43.58  ? 140 GLY B N   1 
ATOM   2322 C CA  . GLY B 2 143 ? 32.148 15.805  112.298 1.00 41.59  ? 140 GLY B CA  1 
ATOM   2323 C C   . GLY B 2 143 ? 33.159 16.619  113.099 1.00 47.63  ? 140 GLY B C   1 
ATOM   2324 O O   . GLY B 2 143 ? 33.769 17.577  112.553 1.00 63.79  ? 140 GLY B O   1 
ATOM   2325 N N   . LYS C 2 5   ? 45.498 30.653  148.119 1.00 78.64  ? 2   LYS C N   1 
ATOM   2326 C CA  . LYS C 2 5   ? 46.295 29.414  147.811 1.00 72.10  ? 2   LYS C CA  1 
ATOM   2327 C C   . LYS C 2 5   ? 47.405 29.951  146.920 1.00 64.14  ? 2   LYS C C   1 
ATOM   2328 O O   . LYS C 2 5   ? 47.775 31.094  147.068 1.00 65.17  ? 2   LYS C O   1 
ATOM   2329 C CB  . LYS C 2 5   ? 45.407 28.358  147.152 1.00 74.77  ? 2   LYS C CB  1 
ATOM   2330 C CG  . LYS C 2 5   ? 44.219 27.869  148.011 1.00 73.63  ? 2   LYS C CG  1 
ATOM   2331 C CD  . LYS C 2 5   ? 43.294 28.971  148.542 1.00 66.36  ? 2   LYS C CD  1 
ATOM   2332 C CE  . LYS C 2 5   ? 41.933 28.461  148.971 1.00 69.40  ? 2   LYS C CE  1 
ATOM   2333 N NZ  . LYS C 2 5   ? 41.131 29.547  149.628 1.00 73.39  ? 2   LYS C NZ  1 
ATOM   2334 N N   . ASP C 2 6   ? 47.965 29.253  145.964 1.00 69.57  ? 3   ASP C N   1 
ATOM   2335 C CA  . ASP C 2 6   ? 48.773 30.100  145.065 1.00 75.12  ? 3   ASP C CA  1 
ATOM   2336 C C   . ASP C 2 6   ? 47.813 31.138  144.394 1.00 57.24  ? 3   ASP C C   1 
ATOM   2337 O O   . ASP C 2 6   ? 46.732 30.799  143.953 1.00 52.38  ? 3   ASP C O   1 
ATOM   2338 C CB  . ASP C 2 6   ? 49.574 29.304  144.015 1.00 78.43  ? 3   ASP C CB  1 
ATOM   2339 C CG  . ASP C 2 6   ? 50.794 30.083  143.503 1.00 93.25  ? 3   ASP C CG  1 
ATOM   2340 O OD1 . ASP C 2 6   ? 51.076 31.205  144.001 1.00 98.08  ? 3   ASP C OD1 1 
ATOM   2341 O OD2 . ASP C 2 6   ? 51.491 29.576  142.607 1.00 101.58 ? 3   ASP C OD2 1 
ATOM   2342 N N   . PHE C 2 7   ? 48.166 32.406  144.375 1.00 42.90  ? 4   PHE C N   1 
ATOM   2343 C CA  . PHE C 2 7   ? 47.496 33.310  143.465 1.00 48.51  ? 4   PHE C CA  1 
ATOM   2344 C C   . PHE C 2 7   ? 47.428 32.672  142.044 1.00 46.98  ? 4   PHE C C   1 
ATOM   2345 O O   . PHE C 2 7   ? 46.350 32.518  141.467 1.00 51.49  ? 4   PHE C O   1 
ATOM   2346 C CB  . PHE C 2 7   ? 48.182 34.657  143.424 1.00 44.08  ? 4   PHE C CB  1 
ATOM   2347 C CG  . PHE C 2 7   ? 47.587 35.602  142.437 1.00 50.53  ? 4   PHE C CG  1 
ATOM   2348 C CD1 . PHE C 2 7   ? 46.217 35.820  142.406 1.00 47.56  ? 4   PHE C CD1 1 
ATOM   2349 C CD2 . PHE C 2 7   ? 48.388 36.323  141.572 1.00 47.45  ? 4   PHE C CD2 1 
ATOM   2350 C CE1 . PHE C 2 7   ? 45.659 36.682  141.488 1.00 46.37  ? 4   PHE C CE1 1 
ATOM   2351 C CE2 . PHE C 2 7   ? 47.825 37.218  140.675 1.00 43.92  ? 4   PHE C CE2 1 
ATOM   2352 C CZ  . PHE C 2 7   ? 46.446 37.374  140.622 1.00 43.62  ? 4   PHE C CZ  1 
ATOM   2353 N N   . GLU C 2 8   ? 48.540 32.178  141.553 1.00 45.35  ? 5   GLU C N   1 
ATOM   2354 C CA  . GLU C 2 8   ? 48.566 31.563  140.246 1.00 49.92  ? 5   GLU C CA  1 
ATOM   2355 C C   . GLU C 2 8   ? 47.507 30.484  140.101 1.00 48.52  ? 5   GLU C C   1 
ATOM   2356 O O   . GLU C 2 8   ? 46.882 30.412  139.085 1.00 45.71  ? 5   GLU C O   1 
ATOM   2357 C CB  . GLU C 2 8   ? 49.958 31.014  139.925 1.00 52.38  ? 5   GLU C CB  1 
ATOM   2358 C CG  . GLU C 2 8   ? 50.392 31.075  138.457 1.00 67.45  ? 5   GLU C CG  1 
ATOM   2359 C CD  . GLU C 2 8   ? 50.166 32.454  137.814 1.00 81.78  ? 5   GLU C CD  1 
ATOM   2360 O OE1 . GLU C 2 8   ? 50.148 33.510  138.553 1.00 74.85  ? 5   GLU C OE1 1 
ATOM   2361 O OE2 . GLU C 2 8   ? 49.990 32.460  136.555 1.00 85.25  ? 5   GLU C OE2 1 
ATOM   2362 N N   . LYS C 2 9   ? 47.291 29.679  141.134 1.00 50.39  ? 6   LYS C N   1 
ATOM   2363 C CA  . LYS C 2 9   ? 46.347 28.606  141.063 1.00 51.13  ? 6   LYS C CA  1 
ATOM   2364 C C   . LYS C 2 9   ? 44.916 29.170  141.055 1.00 44.77  ? 6   LYS C C   1 
ATOM   2365 O O   . LYS C 2 9   ? 44.113 28.717  140.279 1.00 47.39  ? 6   LYS C O   1 
ATOM   2366 C CB  . LYS C 2 9   ? 46.517 27.600  142.200 1.00 54.63  ? 6   LYS C CB  1 
ATOM   2367 C CG  . LYS C 2 9   ? 47.814 26.810  142.175 1.00 78.76  ? 6   LYS C CG  1 
ATOM   2368 C CD  . LYS C 2 9   ? 47.634 25.294  142.088 1.00 98.92  ? 6   LYS C CD  1 
ATOM   2369 C CE  . LYS C 2 9   ? 48.987 24.579  141.983 1.00 108.68 ? 6   LYS C CE  1 
ATOM   2370 N NZ  . LYS C 2 9   ? 48.864 23.113  141.715 1.00 113.45 ? 6   LYS C NZ  1 
ATOM   2371 N N   . LEU C 2 10  ? 44.619 30.157  141.879 1.00 40.84  ? 7   LEU C N   1 
ATOM   2372 C CA  . LEU C 2 10  ? 43.296 30.782  141.884 1.00 44.03  ? 7   LEU C CA  1 
ATOM   2373 C C   . LEU C 2 10  ? 43.041 31.550  140.604 1.00 43.25  ? 7   LEU C C   1 
ATOM   2374 O O   . LEU C 2 10  ? 41.934 31.548  140.132 1.00 39.39  ? 7   LEU C O   1 
ATOM   2375 C CB  . LEU C 2 10  ? 43.106 31.753  143.043 1.00 43.32  ? 7   LEU C CB  1 
ATOM   2376 C CG  . LEU C 2 10  ? 43.492 31.190  144.415 1.00 50.03  ? 7   LEU C CG  1 
ATOM   2377 C CD1 . LEU C 2 10  ? 43.322 32.203  145.549 1.00 45.42  ? 7   LEU C CD1 1 
ATOM   2378 C CD2 . LEU C 2 10  ? 42.691 29.901  144.665 1.00 58.25  ? 7   LEU C CD2 1 
ATOM   2379 N N   . TYR C 2 11  ? 44.061 32.203  140.051 1.00 40.43  ? 8   TYR C N   1 
ATOM   2380 C CA  . TYR C 2 11  ? 43.880 32.904  138.839 1.00 39.39  ? 8   TYR C CA  1 
ATOM   2381 C C   . TYR C 2 11  ? 43.662 31.933  137.678 1.00 43.42  ? 8   TYR C C   1 
ATOM   2382 O O   . TYR C 2 11  ? 42.859 32.204  136.794 1.00 42.43  ? 8   TYR C O   1 
ATOM   2383 C CB  . TYR C 2 11  ? 45.058 33.795  138.530 1.00 43.29  ? 8   TYR C CB  1 
ATOM   2384 C CG  . TYR C 2 11  ? 44.829 34.663  137.320 1.00 44.38  ? 8   TYR C CG  1 
ATOM   2385 C CD1 . TYR C 2 11  ? 44.038 35.810  137.407 1.00 51.14  ? 8   TYR C CD1 1 
ATOM   2386 C CD2 . TYR C 2 11  ? 45.309 34.295  136.087 1.00 44.23  ? 8   TYR C CD2 1 
ATOM   2387 C CE1 . TYR C 2 11  ? 43.773 36.594  136.300 1.00 56.05  ? 8   TYR C CE1 1 
ATOM   2388 C CE2 . TYR C 2 11  ? 45.059 35.071  134.963 1.00 51.03  ? 8   TYR C CE2 1 
ATOM   2389 C CZ  . TYR C 2 11  ? 44.303 36.234  135.080 1.00 56.29  ? 8   TYR C CZ  1 
ATOM   2390 O OH  . TYR C 2 11  ? 44.038 37.021  133.972 1.00 62.79  ? 8   TYR C OH  1 
ATOM   2391 N N   . GLU C 2 12  ? 44.382 30.830  137.638 1.00 47.13  ? 9   GLU C N   1 
ATOM   2392 C CA  . GLU C 2 12  ? 44.085 29.816  136.647 1.00 49.47  ? 9   GLU C CA  1 
ATOM   2393 C C   . GLU C 2 12  ? 42.673 29.235  136.822 1.00 47.80  ? 9   GLU C C   1 
ATOM   2394 O O   . GLU C 2 12  ? 42.027 28.999  135.836 1.00 42.94  ? 9   GLU C O   1 
ATOM   2395 C CB  . GLU C 2 12  ? 45.106 28.705  136.598 1.00 59.55  ? 9   GLU C CB  1 
ATOM   2396 C CG  . GLU C 2 12  ? 45.046 27.935  135.271 1.00 83.13  ? 9   GLU C CG  1 
ATOM   2397 C CD  . GLU C 2 12  ? 46.269 27.040  135.038 1.00 99.82  ? 9   GLU C CD  1 
ATOM   2398 O OE1 . GLU C 2 12  ? 47.313 27.280  135.701 1.00 95.02  ? 9   GLU C OE1 1 
ATOM   2399 O OE2 . GLU C 2 12  ? 46.182 26.105  134.193 1.00 96.69  ? 9   GLU C OE2 1 
ATOM   2400 N N   . ALA C 2 13  ? 42.177 29.071  138.050 1.00 38.97  ? 10  ALA C N   1 
ATOM   2401 C CA  . ALA C 2 13  ? 40.883 28.534  138.232 1.00 39.18  ? 10  ALA C CA  1 
ATOM   2402 C C   . ALA C 2 13  ? 39.835 29.518  137.711 1.00 40.75  ? 10  ALA C C   1 
ATOM   2403 O O   . ALA C 2 13  ? 38.881 29.125  137.073 1.00 43.93  ? 10  ALA C O   1 
ATOM   2404 C CB  . ALA C 2 13  ? 40.624 28.276  139.694 1.00 39.22  ? 10  ALA C CB  1 
ATOM   2405 N N   . THR C 2 14  ? 40.002 30.781  138.050 1.00 37.32  ? 11  THR C N   1 
ATOM   2406 C CA  . THR C 2 14  ? 39.077 31.825  137.710 1.00 39.75  ? 11  THR C CA  1 
ATOM   2407 C C   . THR C 2 14  ? 38.949 32.004  136.187 1.00 37.75  ? 11  THR C C   1 
ATOM   2408 O O   . THR C 2 14  ? 37.887 32.177  135.646 1.00 39.03  ? 11  THR C O   1 
ATOM   2409 C CB  . THR C 2 14  ? 39.556 33.121  138.378 1.00 40.32  ? 11  THR C CB  1 
ATOM   2410 O OG1 . THR C 2 14  ? 39.446 32.930  139.775 1.00 43.87  ? 11  THR C OG1 1 
ATOM   2411 C CG2 . THR C 2 14  ? 38.694 34.303  138.007 1.00 40.64  ? 11  THR C CG2 1 
ATOM   2412 N N   . THR C 2 15  ? 40.070 31.978  135.525 1.00 37.72  ? 12  THR C N   1 
ATOM   2413 C CA  . THR C 2 15  ? 40.159 32.017  134.102 1.00 37.79  ? 12  THR C CA  1 
ATOM   2414 C C   . THR C 2 15  ? 39.427 30.819  133.433 1.00 42.19  ? 12  THR C C   1 
ATOM   2415 O O   . THR C 2 15  ? 38.718 30.996  132.474 1.00 44.95  ? 12  THR C O   1 
ATOM   2416 C CB  . THR C 2 15  ? 41.662 32.041  133.789 1.00 40.19  ? 12  THR C CB  1 
ATOM   2417 O OG1 . THR C 2 15  ? 42.120 33.401  133.964 1.00 42.74  ? 12  THR C OG1 1 
ATOM   2418 C CG2 . THR C 2 15  ? 41.977 31.536  132.411 1.00 39.41  ? 12  THR C CG2 1 
ATOM   2419 N N   . LYS C 2 16  ? 39.629 29.599  133.922 1.00 42.21  ? 13  LYS C N   1 
ATOM   2420 C CA  . LYS C 2 16  ? 39.001 28.429  133.363 1.00 41.45  ? 13  LYS C CA  1 
ATOM   2421 C C   . LYS C 2 16  ? 37.481 28.578  133.609 1.00 43.38  ? 13  LYS C C   1 
ATOM   2422 O O   . LYS C 2 16  ? 36.662 28.064  132.821 1.00 39.81  ? 13  LYS C O   1 
ATOM   2423 C CB  . LYS C 2 16  ? 39.429 27.147  134.085 1.00 47.00  ? 13  LYS C CB  1 
ATOM   2424 C CG  . LYS C 2 16  ? 40.815 26.654  133.837 1.00 54.75  ? 13  LYS C CG  1 
ATOM   2425 C CD  . LYS C 2 16  ? 40.879 25.587  132.766 1.00 74.72  ? 13  LYS C CD  1 
ATOM   2426 C CE  . LYS C 2 16  ? 42.346 25.208  132.512 1.00 71.16  ? 13  LYS C CE  1 
ATOM   2427 N NZ  . LYS C 2 16  ? 42.908 24.834  133.827 1.00 73.63  ? 13  LYS C NZ  1 
ATOM   2428 N N   . LEU C 2 17  ? 37.113 29.204  134.729 1.00 31.04  ? 14  LEU C N   1 
ATOM   2429 C CA  . LEU C 2 17  ? 35.726 29.249  135.092 1.00 35.42  ? 14  LEU C CA  1 
ATOM   2430 C C   . LEU C 2 17  ? 35.050 30.159  134.085 1.00 37.96  ? 14  LEU C C   1 
ATOM   2431 O O   . LEU C 2 17  ? 34.003 29.815  133.566 1.00 41.77  ? 14  LEU C O   1 
ATOM   2432 C CB  . LEU C 2 17  ? 35.519 29.743  136.540 1.00 37.09  ? 14  LEU C CB  1 
ATOM   2433 C CG  . LEU C 2 17  ? 34.187 30.368  136.961 1.00 35.78  ? 14  LEU C CG  1 
ATOM   2434 C CD1 . LEU C 2 17  ? 33.082 29.366  136.763 1.00 38.49  ? 14  LEU C CD1 1 
ATOM   2435 C CD2 . LEU C 2 17  ? 34.199 30.799  138.381 1.00 35.25  ? 14  LEU C CD2 1 
ATOM   2436 N N   . VAL C 2 18  ? 35.666 31.294  133.801 1.00 38.45  ? 15  VAL C N   1 
ATOM   2437 C CA  . VAL C 2 18  ? 35.091 32.271  132.944 1.00 36.69  ? 15  VAL C CA  1 
ATOM   2438 C C   . VAL C 2 18  ? 35.128 31.802  131.496 1.00 42.25  ? 15  VAL C C   1 
ATOM   2439 O O   . VAL C 2 18  ? 34.142 31.967  130.766 1.00 44.16  ? 15  VAL C O   1 
ATOM   2440 C CB  . VAL C 2 18  ? 35.810 33.588  133.088 1.00 39.68  ? 15  VAL C CB  1 
ATOM   2441 C CG1 . VAL C 2 18  ? 35.401 34.590  131.992 1.00 37.10  ? 15  VAL C CG1 1 
ATOM   2442 C CG2 . VAL C 2 18  ? 35.578 34.176  134.487 1.00 41.56  ? 15  VAL C CG2 1 
ATOM   2443 N N   . SER C 2 19  ? 36.237 31.235  131.062 1.00 37.97  ? 16  SER C N   1 
ATOM   2444 C CA  . SER C 2 19  ? 36.307 30.727  129.698 1.00 38.68  ? 16  SER C CA  1 
ATOM   2445 C C   . SER C 2 19  ? 35.257 29.663  129.448 1.00 34.53  ? 16  SER C C   1 
ATOM   2446 O O   . SER C 2 19  ? 34.711 29.600  128.387 1.00 35.75  ? 16  SER C O   1 
ATOM   2447 C CB  . SER C 2 19  ? 37.626 30.003  129.435 1.00 41.38  ? 16  SER C CB  1 
ATOM   2448 O OG  . SER C 2 19  ? 38.576 30.935  129.089 1.00 60.90  ? 16  SER C OG  1 
ATOM   2449 N N   . THR C 2 20  ? 35.070 28.777  130.412 1.00 29.95  ? 17  THR C N   1 
ATOM   2450 C CA  . THR C 2 20  ? 34.121 27.725  130.281 1.00 31.44  ? 17  THR C CA  1 
ATOM   2451 C C   . THR C 2 20  ? 32.687 28.254  130.202 1.00 30.24  ? 17  THR C C   1 
ATOM   2452 O O   . THR C 2 20  ? 31.921 27.812  129.418 1.00 27.84  ? 17  THR C O   1 
ATOM   2453 C CB  . THR C 2 20  ? 34.250 26.699  131.412 1.00 30.63  ? 17  THR C CB  1 
ATOM   2454 O OG1 . THR C 2 20  ? 35.596 26.177  131.420 1.00 29.29  ? 17  THR C OG1 1 
ATOM   2455 C CG2 . THR C 2 20  ? 33.301 25.527  131.166 1.00 28.00  ? 17  THR C CG2 1 
ATOM   2456 N N   . SER C 2 21  ? 32.374 29.254  130.977 1.00 32.93  ? 18  SER C N   1 
ATOM   2457 C CA  . SER C 2 21  ? 31.070 29.888  130.931 1.00 33.57  ? 18  SER C CA  1 
ATOM   2458 C C   . SER C 2 21  ? 30.777 30.498  129.579 1.00 34.42  ? 18  SER C C   1 
ATOM   2459 O O   . SER C 2 21  ? 29.736 30.253  129.013 1.00 36.07  ? 18  SER C O   1 
ATOM   2460 C CB  . SER C 2 21  ? 31.013 30.979  131.973 1.00 32.59  ? 18  SER C CB  1 
ATOM   2461 O OG  . SER C 2 21  ? 29.766 31.616  131.879 1.00 43.08  ? 18  SER C OG  1 
ATOM   2462 N N   . LEU C 2 22  ? 31.709 31.269  129.045 1.00 34.95  ? 19  LEU C N   1 
ATOM   2463 C CA  . LEU C 2 22  ? 31.497 31.896  127.776 1.00 35.00  ? 19  LEU C CA  1 
ATOM   2464 C C   . LEU C 2 22  ? 31.351 30.838  126.710 1.00 40.80  ? 19  LEU C C   1 
ATOM   2465 O O   . LEU C 2 22  ? 30.543 30.993  125.803 1.00 42.61  ? 19  LEU C O   1 
ATOM   2466 C CB  . LEU C 2 22  ? 32.636 32.787  127.405 1.00 35.44  ? 19  LEU C CB  1 
ATOM   2467 C CG  . LEU C 2 22  ? 32.769 33.970  128.336 1.00 46.45  ? 19  LEU C CG  1 
ATOM   2468 C CD1 . LEU C 2 22  ? 34.194 34.531  128.237 1.00 47.55  ? 19  LEU C CD1 1 
ATOM   2469 C CD2 . LEU C 2 22  ? 31.680 35.005  128.049 1.00 42.41  ? 19  LEU C CD2 1 
ATOM   2470 N N   . LYS C 2 23  ? 32.119 29.766  126.815 1.00 40.99  ? 20  LYS C N   1 
ATOM   2471 C CA  . LYS C 2 23  ? 32.089 28.747  125.789 1.00 46.67  ? 20  LYS C CA  1 
ATOM   2472 C C   . LYS C 2 23  ? 30.773 27.937  125.862 1.00 42.58  ? 20  LYS C C   1 
ATOM   2473 O O   . LYS C 2 23  ? 30.169 27.597  124.833 1.00 36.92  ? 20  LYS C O   1 
ATOM   2474 C CB  . LYS C 2 23  ? 33.308 27.858  125.919 1.00 53.90  ? 20  LYS C CB  1 
ATOM   2475 C CG  . LYS C 2 23  ? 33.397 26.696  124.944 1.00 64.00  ? 20  LYS C CG  1 
ATOM   2476 C CD  . LYS C 2 23  ? 34.095 25.510  125.653 1.00 74.81  ? 20  LYS C CD  1 
ATOM   2477 C CE  . LYS C 2 23  ? 33.885 24.161  124.962 1.00 76.49  ? 20  LYS C CE  1 
ATOM   2478 N NZ  . LYS C 2 23  ? 33.901 24.309  123.479 1.00 66.56  ? 20  LYS C NZ  1 
ATOM   2479 N N   . VAL C 2 24  ? 30.312 27.638  127.056 1.00 37.88  ? 21  VAL C N   1 
ATOM   2480 C CA  . VAL C 2 24  ? 29.030 27.024  127.170 1.00 38.53  ? 21  VAL C CA  1 
ATOM   2481 C C   . VAL C 2 24  ? 27.931 27.936  126.565 1.00 36.47  ? 21  VAL C C   1 
ATOM   2482 O O   . VAL C 2 24  ? 27.214 27.500  125.738 1.00 33.67  ? 21  VAL C O   1 
ATOM   2483 C CB  . VAL C 2 24  ? 28.713 26.687  128.608 1.00 42.33  ? 21  VAL C CB  1 
ATOM   2484 C CG1 . VAL C 2 24  ? 27.239 26.435  128.764 1.00 41.81  ? 21  VAL C CG1 1 
ATOM   2485 C CG2 . VAL C 2 24  ? 29.524 25.467  129.011 1.00 46.76  ? 21  VAL C CG2 1 
ATOM   2486 N N   . LYS C 2 25  ? 27.865 29.205  126.922 1.00 40.26  ? 22  LYS C N   1 
ATOM   2487 C CA  . LYS C 2 25  ? 26.840 30.129  126.380 1.00 38.56  ? 22  LYS C CA  1 
ATOM   2488 C C   . LYS C 2 25  ? 26.938 30.179  124.872 1.00 34.04  ? 22  LYS C C   1 
ATOM   2489 O O   . LYS C 2 25  ? 25.957 30.064  124.173 1.00 36.41  ? 22  LYS C O   1 
ATOM   2490 C CB  . LYS C 2 25  ? 26.986 31.560  126.952 1.00 41.68  ? 22  LYS C CB  1 
ATOM   2491 C CG  . LYS C 2 25  ? 26.430 31.723  128.366 1.00 45.78  ? 22  LYS C CG  1 
ATOM   2492 C CD  . LYS C 2 25  ? 26.933 32.970  129.089 1.00 55.06  ? 22  LYS C CD  1 
ATOM   2493 C CE  . LYS C 2 25  ? 26.545 34.306  128.451 1.00 73.29  ? 22  LYS C CE  1 
ATOM   2494 N NZ  . LYS C 2 25  ? 25.291 34.941  128.993 1.00 77.16  ? 22  LYS C NZ  1 
ATOM   2495 N N   . ASP C 2 26  ? 28.128 30.291  124.356 1.00 32.81  ? 23  ASP C N   1 
ATOM   2496 C CA  . ASP C 2 26  ? 28.299 30.575  122.960 1.00 33.82  ? 23  ASP C CA  1 
ATOM   2497 C C   . ASP C 2 26  ? 27.998 29.337  122.122 1.00 39.28  ? 23  ASP C C   1 
ATOM   2498 O O   . ASP C 2 26  ? 27.361 29.446  121.062 1.00 42.71  ? 23  ASP C O   1 
ATOM   2499 C CB  . ASP C 2 26  ? 29.704 31.098  122.733 1.00 38.26  ? 23  ASP C CB  1 
ATOM   2500 C CG  . ASP C 2 26  ? 29.986 31.449  121.283 1.00 51.78  ? 23  ASP C CG  1 
ATOM   2501 O OD1 . ASP C 2 26  ? 29.292 32.340  120.732 1.00 59.10  ? 23  ASP C OD1 1 
ATOM   2502 O OD2 . ASP C 2 26  ? 30.923 30.818  120.702 1.00 63.25  ? 23  ASP C OD2 1 
ATOM   2503 N N   . ASP C 2 27  ? 28.420 28.160  122.576 1.00 33.09  ? 24  ASP C N   1 
ATOM   2504 C CA  . ASP C 2 27  ? 28.105 26.992  121.865 1.00 32.91  ? 24  ASP C CA  1 
ATOM   2505 C C   . ASP C 2 27  ? 26.586 26.717  121.819 1.00 34.26  ? 24  ASP C C   1 
ATOM   2506 O O   . ASP C 2 27  ? 26.099 26.120  120.864 1.00 33.48  ? 24  ASP C O   1 
ATOM   2507 C CB  . ASP C 2 27  ? 28.715 25.779  122.530 1.00 38.39  ? 24  ASP C CB  1 
ATOM   2508 C CG  . ASP C 2 27  ? 30.188 25.657  122.308 1.00 38.96  ? 24  ASP C CG  1 
ATOM   2509 O OD1 . ASP C 2 27  ? 30.772 26.449  121.551 1.00 39.54  ? 24  ASP C OD1 1 
ATOM   2510 O OD2 . ASP C 2 27  ? 30.743 24.754  122.960 1.00 44.13  ? 24  ASP C OD2 1 
ATOM   2511 N N   . LEU C 2 28  ? 25.860 27.065  122.865 1.00 34.24  ? 25  LEU C N   1 
ATOM   2512 C CA  . LEU C 2 28  ? 24.417 26.813  122.904 1.00 33.25  ? 25  LEU C CA  1 
ATOM   2513 C C   . LEU C 2 28  ? 23.744 27.767  121.948 1.00 33.60  ? 25  LEU C C   1 
ATOM   2514 O O   . LEU C 2 28  ? 22.853 27.387  121.212 1.00 32.07  ? 25  LEU C O   1 
ATOM   2515 C CB  . LEU C 2 28  ? 23.855 27.032  124.314 1.00 35.56  ? 25  LEU C CB  1 
ATOM   2516 C CG  . LEU C 2 28  ? 22.336 26.748  124.487 1.00 37.95  ? 25  LEU C CG  1 
ATOM   2517 C CD1 . LEU C 2 28  ? 21.945 25.446  123.810 1.00 33.87  ? 25  LEU C CD1 1 
ATOM   2518 C CD2 . LEU C 2 28  ? 21.912 26.705  125.972 1.00 39.02  ? 25  LEU C CD2 1 
ATOM   2519 N N   . LYS C 2 29  ? 24.228 28.999  121.912 1.00 33.21  ? 26  LYS C N   1 
ATOM   2520 C CA  . LYS C 2 29  ? 23.697 29.967  121.005 1.00 36.25  ? 26  LYS C CA  1 
ATOM   2521 C C   . LYS C 2 29  ? 23.879 29.470  119.592 1.00 39.03  ? 26  LYS C C   1 
ATOM   2522 O O   . LYS C 2 29  ? 22.931 29.561  118.833 1.00 37.82  ? 26  LYS C O   1 
ATOM   2523 C CB  . LYS C 2 29  ? 24.368 31.329  121.180 1.00 42.28  ? 26  LYS C CB  1 
ATOM   2524 C CG  . LYS C 2 29  ? 23.747 32.442  120.331 1.00 45.91  ? 26  LYS C CG  1 
ATOM   2525 C CD  . LYS C 2 29  ? 24.764 33.458  119.870 1.00 52.38  ? 26  LYS C CD  1 
ATOM   2526 C CE  . LYS C 2 29  ? 25.304 34.314  120.986 1.00 62.34  ? 26  LYS C CE  1 
ATOM   2527 N NZ  . LYS C 2 29  ? 26.395 35.141  120.407 1.00 69.84  ? 26  LYS C NZ  1 
ATOM   2528 N N   . LYS C 2 30  ? 25.063 28.937  119.243 1.00 39.10  ? 27  LYS C N   1 
ATOM   2529 C CA  . LYS C 2 30  ? 25.332 28.557  117.854 1.00 42.81  ? 27  LYS C CA  1 
ATOM   2530 C C   . LYS C 2 30  ? 24.446 27.408  117.492 1.00 37.94  ? 27  LYS C C   1 
ATOM   2531 O O   . LYS C 2 30  ? 23.870 27.358  116.455 1.00 40.53  ? 27  LYS C O   1 
ATOM   2532 C CB  . LYS C 2 30  ? 26.802 28.190  117.596 1.00 52.49  ? 27  LYS C CB  1 
ATOM   2533 C CG  . LYS C 2 30  ? 27.749 29.387  117.683 1.00 62.12  ? 27  LYS C CG  1 
ATOM   2534 C CD  . LYS C 2 30  ? 29.138 29.115  117.109 1.00 75.16  ? 27  LYS C CD  1 
ATOM   2535 C CE  . LYS C 2 30  ? 29.999 28.172  117.952 1.00 86.64  ? 27  LYS C CE  1 
ATOM   2536 N NZ  . LYS C 2 30  ? 31.150 28.876  118.599 1.00 93.80  ? 27  LYS C NZ  1 
ATOM   2537 N N   . MET C 2 31  ? 24.305 26.482  118.386 1.00 35.73  ? 28  MET C N   1 
ATOM   2538 C CA  . MET C 2 31  ? 23.420 25.372  118.146 1.00 35.81  ? 28  MET C CA  1 
ATOM   2539 C C   . MET C 2 31  ? 21.933 25.760  117.919 1.00 40.30  ? 28  MET C C   1 
ATOM   2540 O O   . MET C 2 31  ? 21.252 25.150  117.095 1.00 39.02  ? 28  MET C O   1 
ATOM   2541 C CB  . MET C 2 31  ? 23.570 24.440  119.333 1.00 34.22  ? 28  MET C CB  1 
ATOM   2542 C CG  . MET C 2 31  ? 22.902 23.121  119.182 1.00 39.38  ? 28  MET C CG  1 
ATOM   2543 S SD  . MET C 2 31  ? 23.643 21.897  120.257 1.00 49.02  ? 28  MET C SD  1 
ATOM   2544 C CE  . MET C 2 31  ? 22.281 20.805  120.463 1.00 39.76  ? 28  MET C CE  1 
ATOM   2545 N N   . PHE C 2 32  ? 21.414 26.742  118.677 1.00 41.52  ? 29  PHE C N   1 
ATOM   2546 C CA  . PHE C 2 32  ? 20.047 27.224  118.473 1.00 34.64  ? 29  PHE C CA  1 
ATOM   2547 C C   . PHE C 2 32  ? 19.969 27.792  117.055 1.00 35.93  ? 29  PHE C C   1 
ATOM   2548 O O   . PHE C 2 32  ? 19.069 27.482  116.310 1.00 34.09  ? 29  PHE C O   1 
ATOM   2549 C CB  . PHE C 2 32  ? 19.679 28.316  119.479 1.00 34.98  ? 29  PHE C CB  1 
ATOM   2550 C CG  . PHE C 2 32  ? 19.300 27.833  120.883 1.00 31.08  ? 29  PHE C CG  1 
ATOM   2551 C CD1 . PHE C 2 32  ? 18.683 26.678  121.105 1.00 29.52  ? 29  PHE C CD1 1 
ATOM   2552 C CD2 . PHE C 2 32  ? 19.552 28.635  121.969 1.00 32.39  ? 29  PHE C CD2 1 
ATOM   2553 C CE1 . PHE C 2 32  ? 18.319 26.289  122.379 1.00 33.34  ? 29  PHE C CE1 1 
ATOM   2554 C CE2 . PHE C 2 32  ? 19.209 28.265  123.259 1.00 32.15  ? 29  PHE C CE2 1 
ATOM   2555 C CZ  . PHE C 2 32  ? 18.573 27.069  123.470 1.00 29.81  ? 29  PHE C CZ  1 
ATOM   2556 N N   . LYS C 2 33  ? 20.943 28.609  116.684 1.00 37.66  ? 30  LYS C N   1 
ATOM   2557 C CA  . LYS C 2 33  ? 20.949 29.299  115.398 1.00 39.61  ? 30  LYS C CA  1 
ATOM   2558 C C   . LYS C 2 33  ? 21.007 28.310  114.241 1.00 40.80  ? 30  LYS C C   1 
ATOM   2559 O O   . LYS C 2 33  ? 20.232 28.400  113.277 1.00 42.70  ? 30  LYS C O   1 
ATOM   2560 C CB  . LYS C 2 33  ? 22.136 30.223  115.302 1.00 46.60  ? 30  LYS C CB  1 
ATOM   2561 C CG  . LYS C 2 33  ? 22.151 31.442  116.236 1.00 62.47  ? 30  LYS C CG  1 
ATOM   2562 C CD  . LYS C 2 33  ? 22.850 32.636  115.514 1.00 77.41  ? 30  LYS C CD  1 
ATOM   2563 C CE  . LYS C 2 33  ? 23.174 33.858  116.390 1.00 75.36  ? 30  LYS C CE  1 
ATOM   2564 N NZ  . LYS C 2 33  ? 22.076 34.108  117.359 1.00 76.42  ? 30  LYS C NZ  1 
ATOM   2565 N N   . GLN C 2 34  ? 21.905 27.345  114.372 1.00 41.20  ? 31  GLN C N   1 
ATOM   2566 C CA  . GLN C 2 34  ? 22.082 26.266  113.413 1.00 43.36  ? 31  GLN C CA  1 
ATOM   2567 C C   . GLN C 2 34  ? 20.842 25.451  113.165 1.00 43.41  ? 31  GLN C C   1 
ATOM   2568 O O   . GLN C 2 34  ? 20.718 24.891  112.106 1.00 49.35  ? 31  GLN C O   1 
ATOM   2569 C CB  . GLN C 2 34  ? 23.177 25.310  113.881 1.00 45.47  ? 31  GLN C CB  1 
ATOM   2570 C CG  . GLN C 2 34  ? 24.485 25.824  113.376 1.00 62.19  ? 31  GLN C CG  1 
ATOM   2571 C CD  . GLN C 2 34  ? 25.692 25.322  114.154 1.00 67.61  ? 31  GLN C CD  1 
ATOM   2572 O OE1 . GLN C 2 34  ? 25.603 24.323  114.928 1.00 55.73  ? 31  GLN C OE1 1 
ATOM   2573 N NE2 . GLN C 2 34  ? 26.852 26.026  113.943 1.00 49.46  ? 31  GLN C NE2 1 
ATOM   2574 N N   . ASN C 2 35  ? 19.975 25.318  114.153 1.00 39.22  ? 32  ASN C N   1 
ATOM   2575 C CA  . ASN C 2 35  ? 18.732 24.606  113.939 1.00 41.25  ? 32  ASN C CA  1 
ATOM   2576 C C   . ASN C 2 35  ? 17.588 25.581  113.629 1.00 41.61  ? 32  ASN C C   1 
ATOM   2577 O O   . ASN C 2 35  ? 16.439 25.216  113.700 1.00 41.25  ? 32  ASN C O   1 
ATOM   2578 C CB  . ASN C 2 35  ? 18.389 23.742  115.136 1.00 36.25  ? 32  ASN C CB  1 
ATOM   2579 C CG  . ASN C 2 35  ? 19.345 22.588  115.276 1.00 38.17  ? 32  ASN C CG  1 
ATOM   2580 O OD1 . ASN C 2 35  ? 19.095 21.531  114.735 1.00 49.27  ? 32  ASN C OD1 1 
ATOM   2581 N ND2 . ASN C 2 35  ? 20.470 22.787  115.980 1.00 42.49  ? 32  ASN C ND2 1 
ATOM   2582 N N   . GLY C 2 36  ? 17.901 26.830  113.327 1.00 42.77  ? 33  GLY C N   1 
ATOM   2583 C CA  . GLY C 2 36  ? 16.881 27.758  112.875 1.00 44.29  ? 33  GLY C CA  1 
ATOM   2584 C C   . GLY C 2 36  ? 16.275 28.683  113.897 1.00 48.44  ? 33  GLY C C   1 
ATOM   2585 O O   . GLY C 2 36  ? 15.341 29.364  113.567 1.00 47.19  ? 33  GLY C O   1 
ATOM   2586 N N   . TYR C 2 37  ? 16.786 28.737  115.121 1.00 47.10  ? 34  TYR C N   1 
ATOM   2587 C CA  . TYR C 2 37  ? 16.215 29.618  116.128 1.00 42.40  ? 34  TYR C CA  1 
ATOM   2588 C C   . TYR C 2 37  ? 17.217 30.682  116.433 1.00 45.53  ? 34  TYR C C   1 
ATOM   2589 O O   . TYR C 2 37  ? 18.261 30.420  117.047 1.00 46.99  ? 34  TYR C O   1 
ATOM   2590 C CB  . TYR C 2 37  ? 15.858 28.867  117.407 1.00 38.25  ? 34  TYR C CB  1 
ATOM   2591 C CG  . TYR C 2 37  ? 14.912 27.767  117.127 1.00 36.90  ? 34  TYR C CG  1 
ATOM   2592 C CD1 . TYR C 2 37  ? 13.548 28.022  116.950 1.00 36.58  ? 34  TYR C CD1 1 
ATOM   2593 C CD2 . TYR C 2 37  ? 15.362 26.469  116.974 1.00 38.45  ? 34  TYR C CD2 1 
ATOM   2594 C CE1 . TYR C 2 37  ? 12.644 26.991  116.666 1.00 32.21  ? 34  TYR C CE1 1 
ATOM   2595 C CE2 . TYR C 2 37  ? 14.471 25.434  116.681 1.00 38.77  ? 34  TYR C CE2 1 
ATOM   2596 C CZ  . TYR C 2 37  ? 13.129 25.732  116.531 1.00 34.05  ? 34  TYR C CZ  1 
ATOM   2597 O OH  . TYR C 2 37  ? 12.330 24.771  116.239 1.00 37.46  ? 34  TYR C OH  1 
ATOM   2598 N N   . ASP C 2 38  ? 16.883 31.902  116.049 1.00 46.54  ? 35  ASP C N   1 
ATOM   2599 C CA  . ASP C 2 38  ? 17.792 32.997  116.229 1.00 53.32  ? 35  ASP C CA  1 
ATOM   2600 C C   . ASP C 2 38  ? 17.642 33.500  117.677 1.00 48.55  ? 35  ASP C C   1 
ATOM   2601 O O   . ASP C 2 38  ? 17.040 34.519  117.912 1.00 51.97  ? 35  ASP C O   1 
ATOM   2602 C CB  . ASP C 2 38  ? 17.556 34.089  115.146 1.00 55.33  ? 35  ASP C CB  1 
ATOM   2603 C CG  . ASP C 2 38  ? 18.530 35.258  115.274 1.00 64.98  ? 35  ASP C CG  1 
ATOM   2604 O OD1 . ASP C 2 38  ? 19.405 35.206  116.155 1.00 65.83  ? 35  ASP C OD1 1 
ATOM   2605 O OD2 . ASP C 2 38  ? 18.426 36.248  114.518 1.00 80.04  ? 35  ASP C OD2 1 
ATOM   2606 N N   . ILE C 2 39  ? 18.178 32.771  118.656 1.00 53.48  ? 36  ILE C N   1 
ATOM   2607 C CA  . ILE C 2 39  ? 18.067 33.221  120.040 1.00 53.42  ? 36  ILE C CA  1 
ATOM   2608 C C   . ILE C 2 39  ? 19.344 33.069  120.865 1.00 49.79  ? 36  ILE C C   1 
ATOM   2609 O O   . ILE C 2 39  ? 20.135 32.213  120.634 1.00 52.03  ? 36  ILE C O   1 
ATOM   2610 C CB  . ILE C 2 39  ? 16.861 32.571  120.784 1.00 60.76  ? 36  ILE C CB  1 
ATOM   2611 C CG1 . ILE C 2 39  ? 17.232 31.280  121.434 1.00 58.56  ? 36  ILE C CG1 1 
ATOM   2612 C CG2 . ILE C 2 39  ? 15.595 32.347  119.935 1.00 53.76  ? 36  ILE C CG2 1 
ATOM   2613 C CD1 . ILE C 2 39  ? 16.710 31.251  122.835 1.00 60.81  ? 36  ILE C CD1 1 
ATOM   2614 N N   . THR C 2 40  ? 19.556 33.935  121.825 1.00 49.65  ? 37  THR C N   1 
ATOM   2615 C CA  . THR C 2 40  ? 20.715 33.818  122.692 1.00 45.83  ? 37  THR C CA  1 
ATOM   2616 C C   . THR C 2 40  ? 20.366 32.998  123.885 1.00 41.21  ? 37  THR C C   1 
ATOM   2617 O O   . THR C 2 40  ? 19.235 32.640  124.106 1.00 52.31  ? 37  THR C O   1 
ATOM   2618 C CB  . THR C 2 40  ? 21.200 35.170  123.247 1.00 46.18  ? 37  THR C CB  1 
ATOM   2619 O OG1 . THR C 2 40  ? 20.231 35.695  124.164 1.00 52.86  ? 37  THR C OG1 1 
ATOM   2620 C CG2 . THR C 2 40  ? 21.426 36.182  122.136 1.00 45.59  ? 37  THR C CG2 1 
ATOM   2621 N N   . THR C 2 41  ? 21.366 32.750  124.679 1.00 38.15  ? 38  THR C N   1 
ATOM   2622 C CA  . THR C 2 41  ? 21.257 32.007  125.898 1.00 42.00  ? 38  THR C CA  1 
ATOM   2623 C C   . THR C 2 41  ? 20.584 32.789  127.004 1.00 41.16  ? 38  THR C C   1 
ATOM   2624 O O   . THR C 2 41  ? 19.931 32.234  127.882 1.00 47.65  ? 38  THR C O   1 
ATOM   2625 C CB  . THR C 2 41  ? 22.683 31.529  126.313 1.00 43.03  ? 38  THR C CB  1 
ATOM   2626 O OG1 . THR C 2 41  ? 23.052 30.463  125.414 1.00 44.32  ? 38  THR C OG1 1 
ATOM   2627 C CG2 . THR C 2 41  ? 22.709 30.968  127.732 1.00 47.08  ? 38  THR C CG2 1 
ATOM   2628 N N   . ASP C 2 42  ? 20.836 34.080  127.003 1.00 41.79  ? 39  ASP C N   1 
ATOM   2629 C CA  . ASP C 2 42  ? 20.095 35.021  127.798 1.00 42.85  ? 39  ASP C CA  1 
ATOM   2630 C C   . ASP C 2 42  ? 18.620 34.888  127.487 1.00 41.65  ? 39  ASP C C   1 
ATOM   2631 O O   . ASP C 2 42  ? 17.835 34.704  128.398 1.00 42.70  ? 39  ASP C O   1 
ATOM   2632 C CB  . ASP C 2 42  ? 20.540 36.437  127.468 1.00 47.88  ? 39  ASP C CB  1 
ATOM   2633 C CG  . ASP C 2 42  ? 21.968 36.720  127.921 1.00 50.63  ? 39  ASP C CG  1 
ATOM   2634 O OD1 . ASP C 2 42  ? 22.383 36.223  129.021 1.00 45.90  ? 39  ASP C OD1 1 
ATOM   2635 O OD2 . ASP C 2 42  ? 22.639 37.443  127.146 1.00 55.21  ? 39  ASP C OD2 1 
ATOM   2636 N N   . HIS C 2 43  ? 18.246 34.944  126.211 1.00 36.41  ? 40  HIS C N   1 
ATOM   2637 C CA  . HIS C 2 43  ? 16.842 34.811  125.880 1.00 40.90  ? 40  HIS C CA  1 
ATOM   2638 C C   . HIS C 2 43  ? 16.304 33.527  126.470 1.00 45.32  ? 40  HIS C C   1 
ATOM   2639 O O   . HIS C 2 43  ? 15.246 33.530  127.168 1.00 40.35  ? 40  HIS C O   1 
ATOM   2640 C CB  . HIS C 2 43  ? 16.628 34.837  124.379 1.00 38.76  ? 40  HIS C CB  1 
ATOM   2641 C CG  . HIS C 2 43  ? 17.113 36.087  123.768 1.00 34.15  ? 40  HIS C CG  1 
ATOM   2642 N ND1 . HIS C 2 43  ? 17.414 36.186  122.431 1.00 37.74  ? 40  HIS C ND1 1 
ATOM   2643 C CD2 . HIS C 2 43  ? 17.370 37.304  124.319 1.00 33.47  ? 40  HIS C CD2 1 
ATOM   2644 C CE1 . HIS C 2 43  ? 17.836 37.419  122.169 1.00 37.59  ? 40  HIS C CE1 1 
ATOM   2645 N NE2 . HIS C 2 43  ? 17.820 38.116  123.301 1.00 38.90  ? 40  HIS C NE2 1 
ATOM   2646 N N   . TYR C 2 44  ? 17.061 32.451  126.245 1.00 38.53  ? 41  TYR C N   1 
ATOM   2647 C CA  . TYR C 2 44  ? 16.554 31.128  126.601 1.00 36.73  ? 41  TYR C CA  1 
ATOM   2648 C C   . TYR C 2 44  ? 16.419 31.027  128.091 1.00 34.23  ? 41  TYR C C   1 
ATOM   2649 O O   . TYR C 2 44  ? 15.488 30.423  128.572 1.00 40.31  ? 41  TYR C O   1 
ATOM   2650 C CB  . TYR C 2 44  ? 17.486 30.011  126.054 1.00 36.07  ? 41  TYR C CB  1 
ATOM   2651 C CG  . TYR C 2 44  ? 17.190 28.635  126.533 1.00 30.21  ? 41  TYR C CG  1 
ATOM   2652 C CD1 . TYR C 2 44  ? 16.059 28.005  126.130 1.00 30.87  ? 41  TYR C CD1 1 
ATOM   2653 C CD2 . TYR C 2 44  ? 18.061 27.953  127.360 1.00 30.21  ? 41  TYR C CD2 1 
ATOM   2654 C CE1 . TYR C 2 44  ? 15.728 26.754  126.607 1.00 30.45  ? 41  TYR C CE1 1 
ATOM   2655 C CE2 . TYR C 2 44  ? 17.778 26.652  127.796 1.00 32.23  ? 41  TYR C CE2 1 
ATOM   2656 C CZ  . TYR C 2 44  ? 16.599 26.072  127.416 1.00 30.28  ? 41  TYR C CZ  1 
ATOM   2657 O OH  . TYR C 2 44  ? 16.224 24.813  127.834 1.00 30.25  ? 41  TYR C OH  1 
ATOM   2658 N N   . ALA C 2 45  ? 17.289 31.637  128.854 1.00 32.87  ? 42  ALA C N   1 
ATOM   2659 C CA  . ALA C 2 45  ? 17.155 31.460  130.306 1.00 41.90  ? 42  ALA C CA  1 
ATOM   2660 C C   . ALA C 2 45  ? 15.966 32.270  130.890 1.00 41.80  ? 42  ALA C C   1 
ATOM   2661 O O   . ALA C 2 45  ? 15.301 31.841  131.829 1.00 41.10  ? 42  ALA C O   1 
ATOM   2662 C CB  . ALA C 2 45  ? 18.431 31.830  131.004 1.00 42.92  ? 42  ALA C CB  1 
ATOM   2663 N N   . LEU C 2 46  ? 15.705 33.416  130.294 1.00 36.90  ? 43  LEU C N   1 
ATOM   2664 C CA  . LEU C 2 46  ? 14.549 34.200  130.626 1.00 41.16  ? 43  LEU C CA  1 
ATOM   2665 C C   . LEU C 2 46  ? 13.282 33.460  130.213 1.00 40.15  ? 43  LEU C C   1 
ATOM   2666 O O   . LEU C 2 46  ? 12.370 33.289  131.025 1.00 39.39  ? 43  LEU C O   1 
ATOM   2667 C CB  . LEU C 2 46  ? 14.658 35.573  129.966 1.00 46.39  ? 43  LEU C CB  1 
ATOM   2668 C CG  . LEU C 2 46  ? 15.202 36.754  130.804 1.00 46.55  ? 43  LEU C CG  1 
ATOM   2669 C CD1 . LEU C 2 46  ? 15.668 36.454  132.224 1.00 47.95  ? 43  LEU C CD1 1 
ATOM   2670 C CD2 . LEU C 2 46  ? 16.223 37.549  130.042 1.00 46.33  ? 43  LEU C CD2 1 
ATOM   2671 N N   . LEU C 2 47  ? 13.250 32.937  128.996 1.00 38.73  ? 44  LEU C N   1 
ATOM   2672 C CA  . LEU C 2 47  ? 12.150 32.070  128.617 1.00 36.54  ? 44  LEU C CA  1 
ATOM   2673 C C   . LEU C 2 47  ? 11.978 30.871  129.586 1.00 37.65  ? 44  LEU C C   1 
ATOM   2674 O O   . LEU C 2 47  ? 10.887 30.465  129.890 1.00 44.65  ? 44  LEU C O   1 
ATOM   2675 C CB  . LEU C 2 47  ? 12.311 31.618  127.178 1.00 39.31  ? 44  LEU C CB  1 
ATOM   2676 C CG  . LEU C 2 47  ? 12.212 32.655  126.067 1.00 38.79  ? 44  LEU C CG  1 
ATOM   2677 C CD1 . LEU C 2 47  ? 12.762 32.123  124.770 1.00 39.08  ? 44  LEU C CD1 1 
ATOM   2678 C CD2 . LEU C 2 47  ? 10.751 33.016  125.833 1.00 42.90  ? 44  LEU C CD2 1 
ATOM   2679 N N   . ARG C 2 48  ? 13.012 30.299  130.141 1.00 39.54  ? 45  ARG C N   1 
ATOM   2680 C CA  . ARG C 2 48  ? 12.746 29.195  131.124 1.00 40.44  ? 45  ARG C CA  1 
ATOM   2681 C C   . ARG C 2 48  ? 11.946 29.663  132.307 1.00 41.70  ? 45  ARG C C   1 
ATOM   2682 O O   . ARG C 2 48  ? 11.134 28.914  132.826 1.00 40.35  ? 45  ARG C O   1 
ATOM   2683 C CB  . ARG C 2 48  ? 14.045 28.616  131.696 1.00 36.77  ? 45  ARG C CB  1 
ATOM   2684 C CG  . ARG C 2 48  ? 14.861 27.917  130.644 1.00 40.84  ? 45  ARG C CG  1 
ATOM   2685 C CD  . ARG C 2 48  ? 14.354 26.530  130.462 1.00 42.30  ? 45  ARG C CD  1 
ATOM   2686 N NE  . ARG C 2 48  ? 14.697 25.744  131.642 1.00 43.48  ? 45  ARG C NE  1 
ATOM   2687 C CZ  . ARG C 2 48  ? 14.380 24.474  131.779 1.00 40.55  ? 45  ARG C CZ  1 
ATOM   2688 N NH1 . ARG C 2 48  ? 13.747 23.825  130.817 1.00 46.23  ? 45  ARG C NH1 1 
ATOM   2689 N NH2 . ARG C 2 48  ? 14.684 23.868  132.889 1.00 45.14  ? 45  ARG C NH2 1 
ATOM   2690 N N   . PHE C 2 49  ? 12.249 30.870  132.786 1.00 38.60  ? 46  PHE C N   1 
ATOM   2691 C CA  . PHE C 2 49  ? 11.579 31.425  133.955 1.00 38.56  ? 46  PHE C CA  1 
ATOM   2692 C C   . PHE C 2 49  ? 10.099 31.679  133.624 1.00 39.68  ? 46  PHE C C   1 
ATOM   2693 O O   . PHE C 2 49  ? 9.217  31.338  134.391 1.00 40.68  ? 46  PHE C O   1 
ATOM   2694 C CB  . PHE C 2 49  ? 12.227 32.749  134.404 1.00 37.70  ? 46  PHE C CB  1 
ATOM   2695 C CG  . PHE C 2 49  ? 13.553 32.591  135.063 1.00 34.52  ? 46  PHE C CG  1 
ATOM   2696 C CD1 . PHE C 2 49  ? 13.766 31.617  136.008 1.00 40.22  ? 46  PHE C CD1 1 
ATOM   2697 C CD2 . PHE C 2 49  ? 14.608 33.436  134.717 1.00 38.53  ? 46  PHE C CD2 1 
ATOM   2698 C CE1 . PHE C 2 49  ? 15.021 31.482  136.608 1.00 41.54  ? 46  PHE C CE1 1 
ATOM   2699 C CE2 . PHE C 2 49  ? 15.848 33.320  135.315 1.00 39.20  ? 46  PHE C CE2 1 
ATOM   2700 C CZ  . PHE C 2 49  ? 16.055 32.341  136.264 1.00 36.36  ? 46  PHE C CZ  1 
ATOM   2701 N N   . LEU C 2 50  ? 9.854  32.226  132.443 1.00 39.49  ? 47  LEU C N   1 
ATOM   2702 C CA  . LEU C 2 50  ? 8.493  32.449  131.970 1.00 40.02  ? 47  LEU C CA  1 
ATOM   2703 C C   . LEU C 2 50  ? 7.689  31.166  131.723 1.00 43.83  ? 47  LEU C C   1 
ATOM   2704 O O   . LEU C 2 50  ? 6.518  31.167  131.996 1.00 45.69  ? 47  LEU C O   1 
ATOM   2705 C CB  . LEU C 2 50  ? 8.524  33.305  130.720 1.00 37.37  ? 47  LEU C CB  1 
ATOM   2706 C CG  . LEU C 2 50  ? 9.125  34.653  131.076 1.00 39.65  ? 47  LEU C CG  1 
ATOM   2707 C CD1 . LEU C 2 50  ? 9.705  35.375  129.870 1.00 38.97  ? 47  LEU C CD1 1 
ATOM   2708 C CD2 . LEU C 2 50  ? 8.052  35.495  131.735 1.00 41.45  ? 47  LEU C CD2 1 
ATOM   2709 N N   . TRP C 2 51  ? 8.270  30.081  131.191 1.00 44.47  ? 48  TRP C N   1 
ATOM   2710 C CA  . TRP C 2 51  ? 7.474  28.880  131.009 1.00 39.63  ? 48  TRP C CA  1 
ATOM   2711 C C   . TRP C 2 51  ? 7.160  28.372  132.406 1.00 43.42  ? 48  TRP C C   1 
ATOM   2712 O O   . TRP C 2 51  ? 6.174  27.721  132.583 1.00 47.33  ? 48  TRP C O   1 
ATOM   2713 C CB  . TRP C 2 51  ? 8.146  27.760  130.156 1.00 39.30  ? 48  TRP C CB  1 
ATOM   2714 C CG  . TRP C 2 51  ? 8.494  28.186  128.788 1.00 38.23  ? 48  TRP C CG  1 
ATOM   2715 C CD1 . TRP C 2 51  ? 7.710  28.865  127.917 1.00 39.02  ? 48  TRP C CD1 1 
ATOM   2716 C CD2 . TRP C 2 51  ? 9.773  28.052  128.156 1.00 38.90  ? 48  TRP C CD2 1 
ATOM   2717 N NE1 . TRP C 2 51  ? 8.410  29.149  126.757 1.00 37.68  ? 48  TRP C NE1 1 
ATOM   2718 C CE2 . TRP C 2 51  ? 9.680  28.647  126.885 1.00 38.61  ? 48  TRP C CE2 1 
ATOM   2719 C CE3 . TRP C 2 51  ? 10.975 27.448  128.527 1.00 39.39  ? 48  TRP C CE3 1 
ATOM   2720 C CZ2 . TRP C 2 51  ? 10.748 28.674  125.993 1.00 39.61  ? 48  TRP C CZ2 1 
ATOM   2721 C CZ3 . TRP C 2 51  ? 12.046 27.459  127.600 1.00 44.34  ? 48  TRP C CZ3 1 
ATOM   2722 C CH2 . TRP C 2 51  ? 11.919 28.099  126.374 1.00 39.24  ? 48  TRP C CH2 1 
ATOM   2723 N N   . GLU C 2 52  ? 7.980  28.652  133.416 1.00 48.54  ? 49  GLU C N   1 
ATOM   2724 C CA  . GLU C 2 52  ? 7.607  28.235  134.807 1.00 53.42  ? 49  GLU C CA  1 
ATOM   2725 C C   . GLU C 2 52  ? 6.522  29.113  135.426 1.00 50.23  ? 49  GLU C C   1 
ATOM   2726 O O   . GLU C 2 52  ? 5.637  28.619  136.083 1.00 51.81  ? 49  GLU C O   1 
ATOM   2727 C CB  . GLU C 2 52  ? 8.793  28.295  135.757 1.00 55.19  ? 49  GLU C CB  1 
ATOM   2728 C CG  . GLU C 2 52  ? 9.438  26.959  135.975 1.00 72.97  ? 49  GLU C CG  1 
ATOM   2729 C CD  . GLU C 2 52  ? 9.110  26.400  137.327 1.00 81.25  ? 49  GLU C CD  1 
ATOM   2730 O OE1 . GLU C 2 52  ? 9.509  27.075  138.300 1.00 84.53  ? 49  GLU C OE1 1 
ATOM   2731 O OE2 . GLU C 2 52  ? 8.496  25.297  137.401 1.00 89.60  ? 49  GLU C OE2 1 
ATOM   2732 N N   . GLN C 2 53  ? 6.637  30.413  135.207 1.00 48.08  ? 50  GLN C N   1 
ATOM   2733 C CA  . GLN C 2 53  ? 5.749  31.380  135.772 1.00 51.41  ? 50  GLN C CA  1 
ATOM   2734 C C   . GLN C 2 53  ? 5.403  32.440  134.725 1.00 43.17  ? 50  GLN C C   1 
ATOM   2735 O O   . GLN C 2 53  ? 5.896  33.545  134.766 1.00 38.37  ? 50  GLN C O   1 
ATOM   2736 C CB  . GLN C 2 53  ? 6.429  32.022  136.976 1.00 57.65  ? 50  GLN C CB  1 
ATOM   2737 C CG  . GLN C 2 53  ? 5.471  32.538  138.053 1.00 73.05  ? 50  GLN C CG  1 
ATOM   2738 C CD  . GLN C 2 53  ? 6.164  33.356  139.153 1.00 78.54  ? 50  GLN C CD  1 
ATOM   2739 O OE1 . GLN C 2 53  ? 5.682  34.419  139.534 1.00 82.77  ? 50  GLN C OE1 1 
ATOM   2740 N NE2 . GLN C 2 53  ? 7.303  32.866  139.648 1.00 77.29  ? 50  GLN C NE2 1 
ATOM   2741 N N   . ASP C 2 54  ? 4.532  32.123  133.787 1.00 39.71  ? 51  ASP C N   1 
ATOM   2742 C CA  . ASP C 2 54  ? 4.090  33.135  132.828 1.00 39.68  ? 51  ASP C CA  1 
ATOM   2743 C C   . ASP C 2 54  ? 3.306  34.169  133.640 1.00 45.17  ? 51  ASP C C   1 
ATOM   2744 O O   . ASP C 2 54  ? 2.488  33.798  134.462 1.00 47.30  ? 51  ASP C O   1 
ATOM   2745 C CB  . ASP C 2 54  ? 3.237  32.469  131.769 1.00 38.57  ? 51  ASP C CB  1 
ATOM   2746 C CG  . ASP C 2 54  ? 3.067  33.315  130.525 1.00 40.41  ? 51  ASP C CG  1 
ATOM   2747 O OD1 . ASP C 2 54  ? 3.673  34.418  130.403 1.00 42.54  ? 51  ASP C OD1 1 
ATOM   2748 O OD2 . ASP C 2 54  ? 2.347  32.821  129.627 1.00 48.87  ? 51  ASP C OD2 1 
ATOM   2749 N N   . GLY C 2 55  ? 3.606  35.439  133.461 1.00 49.39  ? 52  GLY C N   1 
ATOM   2750 C CA  . GLY C 2 55  ? 2.978  36.482  134.240 1.00 62.84  ? 52  GLY C CA  1 
ATOM   2751 C C   . GLY C 2 55  ? 3.804  37.126  135.351 1.00 65.90  ? 52  GLY C C   1 
ATOM   2752 O O   . GLY C 2 55  ? 3.495  38.215  135.804 1.00 64.15  ? 52  GLY C O   1 
ATOM   2753 N N   . ILE C 2 56  ? 4.860  36.462  135.786 1.00 66.43  ? 53  ILE C N   1 
ATOM   2754 C CA  . ILE C 2 56  ? 5.843  37.054  136.682 1.00 53.76  ? 53  ILE C CA  1 
ATOM   2755 C C   . ILE C 2 56  ? 6.056  38.576  136.501 1.00 53.98  ? 53  ILE C C   1 
ATOM   2756 O O   . ILE C 2 56  ? 6.035  39.139  135.354 1.00 54.33  ? 53  ILE C O   1 
ATOM   2757 C CB  . ILE C 2 56  ? 7.194  36.297  136.563 1.00 56.02  ? 53  ILE C CB  1 
ATOM   2758 C CG1 . ILE C 2 56  ? 7.949  36.393  137.889 1.00 61.96  ? 53  ILE C CG1 1 
ATOM   2759 C CG2 . ILE C 2 56  ? 8.063  36.793  135.381 1.00 46.30  ? 53  ILE C CG2 1 
ATOM   2760 C CD1 . ILE C 2 56  ? 9.017  35.351  138.088 1.00 57.43  ? 53  ILE C CD1 1 
ATOM   2761 N N   . SER C 2 57  ? 6.249  39.250  137.635 1.00 53.99  ? 54  SER C N   1 
ATOM   2762 C CA  . SER C 2 57  ? 6.545  40.703  137.637 1.00 63.37  ? 54  SER C CA  1 
ATOM   2763 C C   . SER C 2 57  ? 7.984  40.911  137.182 1.00 60.72  ? 54  SER C C   1 
ATOM   2764 O O   . SER C 2 57  ? 8.805  40.044  137.481 1.00 59.96  ? 54  SER C O   1 
ATOM   2765 C CB  . SER C 2 57  ? 6.413  41.278  139.042 1.00 64.27  ? 54  SER C CB  1 
ATOM   2766 O OG  . SER C 2 57  ? 7.081  40.444  139.994 1.00 63.91  ? 54  SER C OG  1 
ATOM   2767 N N   . GLN C 2 58  ? 8.275  42.037  136.503 1.00 48.92  ? 55  GLN C N   1 
ATOM   2768 C CA  . GLN C 2 58  ? 9.630  42.391  136.113 1.00 53.02  ? 55  GLN C CA  1 
ATOM   2769 C C   . GLN C 2 58  ? 10.576 42.368  137.273 1.00 66.33  ? 55  GLN C C   1 
ATOM   2770 O O   . GLN C 2 58  ? 11.640 41.761  137.202 1.00 72.30  ? 55  GLN C O   1 
ATOM   2771 C CB  . GLN C 2 58  ? 9.729  43.765  135.512 1.00 50.91  ? 55  GLN C CB  1 
ATOM   2772 C CG  . GLN C 2 58  ? 9.928  43.770  134.018 1.00 50.46  ? 55  GLN C CG  1 
ATOM   2773 C CD  . GLN C 2 58  ? 10.673 44.966  133.512 1.00 52.33  ? 55  GLN C CD  1 
ATOM   2774 O OE1 . GLN C 2 58  ? 11.043 45.839  134.260 1.00 72.94  ? 55  GLN C OE1 1 
ATOM   2775 N NE2 . GLN C 2 58  ? 10.887 45.020  132.238 1.00 56.27  ? 55  GLN C NE2 1 
ATOM   2776 N N   . ILE C 2 59  ? 10.196 43.063  138.327 1.00 67.06  ? 56  ILE C N   1 
ATOM   2777 C CA  . ILE C 2 59  ? 10.976 43.026  139.538 1.00 80.64  ? 56  ILE C CA  1 
ATOM   2778 C C   . ILE C 2 59  ? 11.326 41.543  139.826 1.00 72.00  ? 56  ILE C C   1 
ATOM   2779 O O   . ILE C 2 59  ? 12.506 41.193  139.793 1.00 73.44  ? 56  ILE C O   1 
ATOM   2780 C CB  . ILE C 2 59  ? 10.331 43.855  140.729 1.00 85.64  ? 56  ILE C CB  1 
ATOM   2781 C CG1 . ILE C 2 59  ? 11.172 43.767  142.013 1.00 90.69  ? 56  ILE C CG1 1 
ATOM   2782 C CG2 . ILE C 2 59  ? 8.877  43.464  141.033 1.00 93.48  ? 56  ILE C CG2 1 
ATOM   2783 C CD1 . ILE C 2 59  ? 10.708 42.743  143.049 1.00 93.94  ? 56  ILE C CD1 1 
ATOM   2784 N N   . ASP C 2 60  ? 10.343 40.663  140.036 1.00 64.15  ? 57  ASP C N   1 
ATOM   2785 C CA  . ASP C 2 60  ? 10.661 39.261  140.391 1.00 56.04  ? 57  ASP C CA  1 
ATOM   2786 C C   . ASP C 2 60  ? 11.546 38.494  139.367 1.00 54.47  ? 57  ASP C C   1 
ATOM   2787 O O   . ASP C 2 60  ? 12.183 37.528  139.726 1.00 54.13  ? 57  ASP C O   1 
ATOM   2788 C CB  . ASP C 2 60  ? 9.389  38.450  140.566 1.00 62.53  ? 57  ASP C CB  1 
ATOM   2789 C CG  . ASP C 2 60  ? 8.781  38.569  141.940 1.00 63.79  ? 57  ASP C CG  1 
ATOM   2790 O OD1 . ASP C 2 60  ? 8.928  39.630  142.574 1.00 71.89  ? 57  ASP C OD1 1 
ATOM   2791 O OD2 . ASP C 2 60  ? 8.141  37.582  142.373 1.00 67.44  ? 57  ASP C OD2 1 
ATOM   2792 N N   . LEU C 2 61  ? 11.563 38.891  138.104 1.00 46.78  ? 58  LEU C N   1 
ATOM   2793 C CA  . LEU C 2 61  ? 12.323 38.179  137.122 1.00 52.05  ? 58  LEU C CA  1 
ATOM   2794 C C   . LEU C 2 61  ? 13.775 38.622  137.205 1.00 56.90  ? 58  LEU C C   1 
ATOM   2795 O O   . LEU C 2 61  ? 14.704 37.809  137.047 1.00 54.79  ? 58  LEU C O   1 
ATOM   2796 C CB  . LEU C 2 61  ? 11.832 38.519  135.725 1.00 52.71  ? 58  LEU C CB  1 
ATOM   2797 C CG  . LEU C 2 61  ? 11.596 37.416  134.709 1.00 47.76  ? 58  LEU C CG  1 
ATOM   2798 C CD1 . LEU C 2 61  ? 11.748 37.980  133.313 1.00 51.53  ? 58  LEU C CD1 1 
ATOM   2799 C CD2 . LEU C 2 61  ? 12.439 36.183  134.897 1.00 49.57  ? 58  LEU C CD2 1 
ATOM   2800 N N   . CYS C 2 62  ? 13.941 39.933  137.394 1.00 54.96  ? 59  CYS C N   1 
ATOM   2801 C CA  . CYS C 2 62  ? 15.235 40.565  137.565 1.00 52.70  ? 59  CYS C CA  1 
ATOM   2802 C C   . CYS C 2 62  ? 15.970 39.998  138.796 1.00 57.20  ? 59  CYS C C   1 
ATOM   2803 O O   . CYS C 2 62  ? 17.187 39.844  138.782 1.00 65.99  ? 59  CYS C O   1 
ATOM   2804 C CB  . CYS C 2 62  ? 15.031 42.050  137.683 1.00 46.56  ? 59  CYS C CB  1 
ATOM   2805 S SG  . CYS C 2 62  ? 14.766 42.844  136.091 1.00 55.92  ? 59  CYS C SG  1 
ATOM   2806 N N   . GLU C 2 63  ? 15.207 39.684  139.836 1.00 62.27  ? 60  GLU C N   1 
ATOM   2807 C CA  . GLU C 2 63  ? 15.684 38.953  141.002 1.00 72.29  ? 60  GLU C CA  1 
ATOM   2808 C C   . GLU C 2 63  ? 16.168 37.583  140.578 1.00 68.77  ? 60  GLU C C   1 
ATOM   2809 O O   . GLU C 2 63  ? 17.291 37.205  140.874 1.00 65.86  ? 60  GLU C O   1 
ATOM   2810 C CB  . GLU C 2 63  ? 14.552 38.775  142.037 1.00 87.12  ? 60  GLU C CB  1 
ATOM   2811 C CG  . GLU C 2 63  ? 14.592 39.682  143.263 1.00 104.90 ? 60  GLU C CG  1 
ATOM   2812 C CD  . GLU C 2 63  ? 14.752 38.890  144.554 1.00 114.09 ? 60  GLU C CD  1 
ATOM   2813 O OE1 . GLU C 2 63  ? 13.879 39.002  145.458 1.00 112.08 ? 60  GLU C OE1 1 
ATOM   2814 O OE2 . GLU C 2 63  ? 15.748 38.137  144.646 1.00 103.78 ? 60  GLU C OE2 1 
ATOM   2815 N N   . LYS C 2 64  ? 15.305 36.842  139.887 1.00 64.36  ? 61  LYS C N   1 
ATOM   2816 C CA  . LYS C 2 64  ? 15.651 35.502  139.418 1.00 70.55  ? 61  LYS C CA  1 
ATOM   2817 C C   . LYS C 2 64  ? 16.845 35.434  138.437 1.00 61.11  ? 61  LYS C C   1 
ATOM   2818 O O   . LYS C 2 64  ? 17.521 34.455  138.444 1.00 60.78  ? 61  LYS C O   1 
ATOM   2819 C CB  . LYS C 2 64  ? 14.430 34.809  138.805 1.00 68.85  ? 61  LYS C CB  1 
ATOM   2820 C CG  . LYS C 2 64  ? 13.565 34.114  139.843 1.00 66.18  ? 61  LYS C CG  1 
ATOM   2821 C CD  . LYS C 2 64  ? 12.426 33.358  139.186 1.00 71.06  ? 61  LYS C CD  1 
ATOM   2822 C CE  . LYS C 2 64  ? 11.911 32.206  140.027 1.00 72.20  ? 61  LYS C CE  1 
ATOM   2823 N NZ  . LYS C 2 64  ? 10.844 32.706  140.922 1.00 69.67  ? 61  LYS C NZ  1 
ATOM   2824 N N   . SER C 2 65  ? 17.110 36.519  137.717 1.00 55.15  ? 62  SER C N   1 
ATOM   2825 C CA  . SER C 2 65  ? 17.898 36.587  136.498 1.00 57.40  ? 62  SER C CA  1 
ATOM   2826 C C   . SER C 2 65  ? 19.441 36.526  136.560 1.00 74.09  ? 62  SER C C   1 
ATOM   2827 O O   . SER C 2 65  ? 20.109 36.429  135.504 1.00 87.81  ? 62  SER C O   1 
ATOM   2828 C CB  . SER C 2 65  ? 17.551 37.890  135.777 1.00 54.68  ? 62  SER C CB  1 
ATOM   2829 O OG  . SER C 2 65  ? 18.551 38.307  134.844 1.00 57.53  ? 62  SER C OG  1 
ATOM   2830 N N   . CYS C 2 66  ? 20.043 36.623  137.730 1.00 68.70  ? 63  CYS C N   1 
ATOM   2831 C CA  . CYS C 2 66  ? 21.533 36.496  137.796 1.00 75.88  ? 63  CYS C CA  1 
ATOM   2832 C C   . CYS C 2 66  ? 22.242 37.598  137.052 1.00 66.78  ? 63  CYS C C   1 
ATOM   2833 O O   . CYS C 2 66  ? 23.430 37.729  137.198 1.00 82.60  ? 63  CYS C O   1 
ATOM   2834 C CB  . CYS C 2 66  ? 22.081 35.131  137.292 1.00 77.30  ? 63  CYS C CB  1 
ATOM   2835 S SG  . CYS C 2 66  ? 22.970 35.183  135.702 1.00 76.16  ? 63  CYS C SG  1 
ATOM   2836 N N   . LYS C 2 67  ? 21.544 38.372  136.236 1.00 63.18  ? 64  LYS C N   1 
ATOM   2837 C CA  . LYS C 2 67  ? 22.011 39.716  135.924 1.00 59.16  ? 64  LYS C CA  1 
ATOM   2838 C C   . LYS C 2 67  ? 21.212 40.799  136.666 1.00 57.72  ? 64  LYS C C   1 
ATOM   2839 O O   . LYS C 2 67  ? 20.174 40.526  137.315 1.00 63.27  ? 64  LYS C O   1 
ATOM   2840 C CB  . LYS C 2 67  ? 21.971 39.954  134.426 1.00 61.21  ? 64  LYS C CB  1 
ATOM   2841 C CG  . LYS C 2 67  ? 22.888 39.040  133.689 1.00 60.18  ? 64  LYS C CG  1 
ATOM   2842 C CD  . LYS C 2 67  ? 22.654 39.092  132.196 1.00 65.27  ? 64  LYS C CD  1 
ATOM   2843 C CE  . LYS C 2 67  ? 23.821 39.720  131.449 1.00 72.20  ? 64  LYS C CE  1 
ATOM   2844 N NZ  . LYS C 2 67  ? 24.152 38.866  130.272 1.00 68.21  ? 64  LYS C NZ  1 
ATOM   2845 N N   . ASP C 2 68  ? 21.705 42.033  136.571 1.00 65.08  ? 65  ASP C N   1 
ATOM   2846 C CA  . ASP C 2 68  ? 21.116 43.169  137.317 1.00 73.31  ? 65  ASP C CA  1 
ATOM   2847 C C   . ASP C 2 68  ? 19.883 43.699  136.579 1.00 76.25  ? 65  ASP C C   1 
ATOM   2848 O O   . ASP C 2 68  ? 19.586 43.222  135.474 1.00 88.63  ? 65  ASP C O   1 
ATOM   2849 C CB  . ASP C 2 68  ? 22.174 44.269  137.584 1.00 66.81  ? 65  ASP C CB  1 
ATOM   2850 C CG  . ASP C 2 68  ? 22.700 44.918  136.316 1.00 67.82  ? 65  ASP C CG  1 
ATOM   2851 O OD1 . ASP C 2 68  ? 22.109 44.740  135.234 1.00 78.66  ? 65  ASP C OD1 1 
ATOM   2852 O OD2 . ASP C 2 68  ? 23.705 45.647  136.392 1.00 74.70  ? 65  ASP C OD2 1 
ATOM   2853 N N   . LYS C 2 69  ? 19.166 44.658  137.179 1.00 73.90  ? 66  LYS C N   1 
ATOM   2854 C CA  . LYS C 2 69  ? 17.985 45.289  136.528 1.00 74.15  ? 66  LYS C CA  1 
ATOM   2855 C C   . LYS C 2 69  ? 18.253 45.793  135.125 1.00 64.58  ? 66  LYS C C   1 
ATOM   2856 O O   . LYS C 2 69  ? 17.544 45.469  134.182 1.00 65.96  ? 66  LYS C O   1 
ATOM   2857 C CB  . LYS C 2 69  ? 17.453 46.481  137.341 1.00 86.83  ? 66  LYS C CB  1 
ATOM   2858 C CG  . LYS C 2 69  ? 16.244 46.185  138.219 1.00 97.14  ? 66  LYS C CG  1 
ATOM   2859 C CD  . LYS C 2 69  ? 15.590 47.473  138.722 1.00 102.46 ? 66  LYS C CD  1 
ATOM   2860 C CE  . LYS C 2 69  ? 14.081 47.304  138.919 1.00 105.49 ? 66  LYS C CE  1 
ATOM   2861 N NZ  . LYS C 2 69  ? 13.667 46.079  139.678 1.00 98.57  ? 66  LYS C NZ  1 
ATOM   2862 N N   . SER C 2 70  ? 19.286 46.606  135.002 1.00 63.81  ? 67  SER C N   1 
ATOM   2863 C CA  . SER C 2 70  ? 19.530 47.371  133.780 1.00 66.21  ? 67  SER C CA  1 
ATOM   2864 C C   . SER C 2 70  ? 19.859 46.518  132.500 1.00 65.01  ? 67  SER C C   1 
ATOM   2865 O O   . SER C 2 70  ? 19.607 46.964  131.360 1.00 62.62  ? 67  SER C O   1 
ATOM   2866 C CB  . SER C 2 70  ? 20.649 48.396  134.074 1.00 62.95  ? 67  SER C CB  1 
ATOM   2867 O OG  . SER C 2 70  ? 21.336 48.791  132.874 1.00 82.86  ? 67  SER C OG  1 
ATOM   2868 N N   . ASN C 2 71  ? 20.496 45.353  132.680 1.00 58.66  ? 68  ASN C N   1 
ATOM   2869 C CA  . ASN C 2 71  ? 20.819 44.489  131.531 1.00 61.97  ? 68  ASN C CA  1 
ATOM   2870 C C   . ASN C 2 71  ? 19.670 43.512  131.298 1.00 58.31  ? 68  ASN C C   1 
ATOM   2871 O O   . ASN C 2 71  ? 19.388 43.212  130.167 1.00 52.89  ? 68  ASN C O   1 
ATOM   2872 C CB  . ASN C 2 71  ? 22.143 43.705  131.681 1.00 63.90  ? 68  ASN C CB  1 
ATOM   2873 C CG  . ASN C 2 71  ? 23.385 44.605  131.649 1.00 67.01  ? 68  ASN C CG  1 
ATOM   2874 O OD1 . ASN C 2 71  ? 23.638 45.332  130.677 1.00 72.47  ? 68  ASN C OD1 1 
ATOM   2875 N ND2 . ASN C 2 71  ? 24.167 44.548  132.704 1.00 57.99  ? 68  ASN C ND2 1 
ATOM   2876 N N   . THR C 2 72  ? 19.037 43.031  132.371 1.00 50.43  ? 69  THR C N   1 
ATOM   2877 C CA  . THR C 2 72  ? 17.925 42.106  132.291 1.00 53.65  ? 69  THR C CA  1 
ATOM   2878 C C   . THR C 2 72  ? 16.805 42.780  131.534 1.00 57.05  ? 69  THR C C   1 
ATOM   2879 O O   . THR C 2 72  ? 16.287 42.262  130.540 1.00 62.97  ? 69  THR C O   1 
ATOM   2880 C CB  . THR C 2 72  ? 17.469 41.698  133.711 1.00 53.61  ? 69  THR C CB  1 
ATOM   2881 O OG1 . THR C 2 72  ? 18.567 41.087  134.406 1.00 50.07  ? 69  THR C OG1 1 
ATOM   2882 C CG2 . THR C 2 72  ? 16.315 40.727  133.678 1.00 48.15  ? 69  THR C CG2 1 
ATOM   2883 N N   . THR C 2 73  ? 16.517 44.001  131.947 1.00 64.53  ? 70  THR C N   1 
ATOM   2884 C CA  . THR C 2 73  ? 15.501 44.817  131.319 1.00 58.94  ? 70  THR C CA  1 
ATOM   2885 C C   . THR C 2 73  ? 15.853 45.106  129.867 1.00 57.37  ? 70  THR C C   1 
ATOM   2886 O O   . THR C 2 73  ? 14.998 45.080  128.996 1.00 56.80  ? 70  THR C O   1 
ATOM   2887 C CB  . THR C 2 73  ? 15.312 46.110  132.145 1.00 66.94  ? 70  THR C CB  1 
ATOM   2888 O OG1 . THR C 2 73  ? 14.688 45.779  133.407 1.00 62.92  ? 70  THR C OG1 1 
ATOM   2889 C CG2 . THR C 2 73  ? 14.481 47.160  131.387 1.00 71.16  ? 70  THR C CG2 1 
ATOM   2890 N N   . ARG C 2 74  ? 17.112 45.375  129.585 1.00 59.34  ? 71  ARG C N   1 
ATOM   2891 C CA  . ARG C 2 74  ? 17.484 45.631  128.204 1.00 60.27  ? 71  ARG C CA  1 
ATOM   2892 C C   . ARG C 2 74  ? 17.278 44.371  127.345 1.00 59.88  ? 71  ARG C C   1 
ATOM   2893 O O   . ARG C 2 74  ? 16.962 44.482  126.159 1.00 59.67  ? 71  ARG C O   1 
ATOM   2894 C CB  . ARG C 2 74  ? 18.949 46.107  128.122 1.00 70.47  ? 71  ARG C CB  1 
ATOM   2895 C CG  . ARG C 2 74  ? 19.491 46.347  126.690 1.00 77.74  ? 71  ARG C CG  1 
ATOM   2896 C CD  . ARG C 2 74  ? 21.003 46.667  126.670 1.00 93.49  ? 71  ARG C CD  1 
ATOM   2897 N NE  . ARG C 2 74  ? 21.822 45.808  127.557 1.00 102.75 ? 71  ARG C NE  1 
ATOM   2898 C CZ  . ARG C 2 74  ? 22.214 44.547  127.298 1.00 97.26  ? 71  ARG C CZ  1 
ATOM   2899 N NH1 . ARG C 2 74  ? 21.894 43.925  126.160 1.00 97.59  ? 71  ARG C NH1 1 
ATOM   2900 N NH2 . ARG C 2 74  ? 22.920 43.884  128.203 1.00 85.20  ? 71  ARG C NH2 1 
ATOM   2901 N N   . ILE C 2 75  ? 17.487 43.174  127.906 1.00 54.13  ? 72  ILE C N   1 
ATOM   2902 C CA  . ILE C 2 75  ? 17.254 42.004  127.092 1.00 57.39  ? 72  ILE C CA  1 
ATOM   2903 C C   . ILE C 2 75  ? 15.773 41.680  127.034 1.00 57.96  ? 72  ILE C C   1 
ATOM   2904 O O   . ILE C 2 75  ? 15.307 41.297  125.969 1.00 39.49  ? 72  ILE C O   1 
ATOM   2905 C CB  . ILE C 2 75  ? 18.173 40.769  127.309 1.00 63.32  ? 72  ILE C CB  1 
ATOM   2906 C CG1 . ILE C 2 75  ? 18.481 40.461  128.761 1.00 61.99  ? 72  ILE C CG1 1 
ATOM   2907 C CG2 . ILE C 2 75  ? 19.459 40.998  126.483 1.00 74.44  ? 72  ILE C CG2 1 
ATOM   2908 C CD1 . ILE C 2 75  ? 20.002 40.490  129.089 1.00 56.95  ? 72  ILE C CD1 1 
ATOM   2909 N N   . LEU C 2 76  ? 15.027 41.894  128.119 1.00 51.26  ? 73  LEU C N   1 
ATOM   2910 C CA  . LEU C 2 76  ? 13.585 41.887  127.978 1.00 50.34  ? 73  LEU C CA  1 
ATOM   2911 C C   . LEU C 2 76  ? 13.138 42.783  126.796 1.00 49.96  ? 73  LEU C C   1 
ATOM   2912 O O   . LEU C 2 76  ? 12.272 42.351  125.969 1.00 47.13  ? 73  LEU C O   1 
ATOM   2913 C CB  . LEU C 2 76  ? 12.913 42.267  129.273 1.00 48.28  ? 73  LEU C CB  1 
ATOM   2914 C CG  . LEU C 2 76  ? 13.129 41.161  130.300 1.00 53.74  ? 73  LEU C CG  1 
ATOM   2915 C CD1 . LEU C 2 76  ? 12.708 41.648  131.700 1.00 51.63  ? 73  LEU C CD1 1 
ATOM   2916 C CD2 . LEU C 2 76  ? 12.410 39.863  129.898 1.00 48.80  ? 73  LEU C CD2 1 
ATOM   2917 N N   . ASP C 2 77  ? 13.761 43.961  126.648 1.00 45.91  ? 74  ASP C N   1 
ATOM   2918 C CA  . ASP C 2 77  ? 13.370 44.838  125.528 1.00 53.54  ? 74  ASP C CA  1 
ATOM   2919 C C   . ASP C 2 77  ? 13.637 44.130  124.225 1.00 45.88  ? 74  ASP C C   1 
ATOM   2920 O O   . ASP C 2 77  ? 12.806 44.124  123.381 1.00 54.73  ? 74  ASP C O   1 
ATOM   2921 C CB  . ASP C 2 77  ? 14.049 46.228  125.500 1.00 58.65  ? 74  ASP C CB  1 
ATOM   2922 C CG  . ASP C 2 77  ? 13.676 47.140  126.710 1.00 67.86  ? 74  ASP C CG  1 
ATOM   2923 O OD1 . ASP C 2 77  ? 12.838 46.794  127.589 1.00 63.37  ? 74  ASP C OD1 1 
ATOM   2924 O OD2 . ASP C 2 77  ? 14.270 48.237  126.781 1.00 79.05  ? 74  ASP C OD2 1 
ATOM   2925 N N   . VAL C 2 78  ? 14.792 43.514  124.064 1.00 48.97  ? 75  VAL C N   1 
ATOM   2926 C CA  . VAL C 2 78  ? 15.119 42.825  122.803 1.00 47.25  ? 75  VAL C CA  1 
ATOM   2927 C C   . VAL C 2 78  ? 14.140 41.677  122.510 1.00 47.93  ? 75  VAL C C   1 
ATOM   2928 O O   . VAL C 2 78  ? 13.742 41.428  121.363 1.00 48.38  ? 75  VAL C O   1 
ATOM   2929 C CB  . VAL C 2 78  ? 16.561 42.285  122.835 1.00 48.45  ? 75  VAL C CB  1 
ATOM   2930 C CG1 . VAL C 2 78  ? 16.870 41.413  121.619 1.00 51.29  ? 75  VAL C CG1 1 
ATOM   2931 C CG2 . VAL C 2 78  ? 17.537 43.440  122.886 1.00 46.54  ? 75  VAL C CG2 1 
ATOM   2932 N N   . MET C 2 79  ? 13.764 41.004  123.577 1.00 43.74  ? 76  MET C N   1 
ATOM   2933 C CA  . MET C 2 79  ? 12.859 39.893  123.537 1.00 49.65  ? 76  MET C CA  1 
ATOM   2934 C C   . MET C 2 79  ? 11.445 40.342  123.139 1.00 59.33  ? 76  MET C C   1 
ATOM   2935 O O   . MET C 2 79  ? 10.761 39.600  122.401 1.00 54.89  ? 76  MET C O   1 
ATOM   2936 C CB  . MET C 2 79  ? 12.834 39.151  124.905 1.00 45.16  ? 76  MET C CB  1 
ATOM   2937 C CG  . MET C 2 79  ? 14.074 38.305  125.217 1.00 43.33  ? 76  MET C CG  1 
ATOM   2938 S SD  . MET C 2 79  ? 13.971 37.465  126.804 1.00 45.63  ? 76  MET C SD  1 
ATOM   2939 C CE  . MET C 2 79  ? 12.783 36.186  126.428 1.00 42.08  ? 76  MET C CE  1 
ATOM   2940 N N   . LYS C 2 80  ? 11.003 41.510  123.650 1.00 65.28  ? 77  LYS C N   1 
ATOM   2941 C CA  . LYS C 2 80  ? 9.773  42.178  123.154 1.00 59.87  ? 77  LYS C CA  1 
ATOM   2942 C C   . LYS C 2 80  ? 9.886  42.521  121.660 1.00 51.10  ? 77  LYS C C   1 
ATOM   2943 O O   . LYS C 2 80  ? 9.071  42.110  120.868 1.00 56.48  ? 77  LYS C O   1 
ATOM   2944 C CB  . LYS C 2 80  ? 9.447  43.427  123.952 1.00 70.74  ? 77  LYS C CB  1 
ATOM   2945 C CG  . LYS C 2 80  ? 8.308  44.258  123.352 1.00 84.97  ? 77  LYS C CG  1 
ATOM   2946 C CD  . LYS C 2 80  ? 7.384  44.878  124.404 1.00 100.12 ? 77  LYS C CD  1 
ATOM   2947 C CE  . LYS C 2 80  ? 7.976  46.095  125.112 1.00 104.10 ? 77  LYS C CE  1 
ATOM   2948 N NZ  . LYS C 2 80  ? 7.619  47.363  124.423 1.00 99.84  ? 77  LYS C NZ  1 
ATOM   2949 N N   . ASN C 2 81  ? 10.928 43.187  121.230 1.00 47.46  ? 78  ASN C N   1 
ATOM   2950 C CA  . ASN C 2 81  ? 11.045 43.417  119.789 1.00 55.85  ? 78  ASN C CA  1 
ATOM   2951 C C   . ASN C 2 81  ? 11.144 42.212  118.948 1.00 49.27  ? 78  ASN C C   1 
ATOM   2952 O O   . ASN C 2 81  ? 10.876 42.312  117.788 1.00 59.25  ? 78  ASN C O   1 
ATOM   2953 C CB  . ASN C 2 81  ? 12.232 44.309  119.434 1.00 64.49  ? 78  ASN C CB  1 
ATOM   2954 C CG  . ASN C 2 81  ? 12.100 45.687  120.025 1.00 76.32  ? 78  ASN C CG  1 
ATOM   2955 O OD1 . ASN C 2 81  ? 10.991 46.185  120.266 1.00 81.70  ? 78  ASN C OD1 1 
ATOM   2956 N ND2 . ASN C 2 81  ? 13.228 46.303  120.295 1.00 88.99  ? 78  ASN C ND2 1 
ATOM   2957 N N   . LYS C 2 82  ? 11.576 41.074  119.477 1.00 56.34  ? 79  LYS C N   1 
ATOM   2958 C CA  . LYS C 2 82  ? 11.643 39.850  118.650 1.00 53.66  ? 79  LYS C CA  1 
ATOM   2959 C C   . LYS C 2 82  ? 10.318 39.146  118.686 1.00 53.53  ? 79  LYS C C   1 
ATOM   2960 O O   . LYS C 2 82  ? 10.157 38.087  118.073 1.00 53.16  ? 79  LYS C O   1 
ATOM   2961 C CB  . LYS C 2 82  ? 12.655 38.864  119.198 1.00 60.42  ? 79  LYS C CB  1 
ATOM   2962 C CG  . LYS C 2 82  ? 14.112 39.098  118.891 1.00 65.39  ? 79  LYS C CG  1 
ATOM   2963 C CD  . LYS C 2 82  ? 14.938 38.091  119.701 1.00 66.34  ? 79  LYS C CD  1 
ATOM   2964 C CE  . LYS C 2 82  ? 16.173 37.653  118.955 1.00 64.90  ? 79  LYS C CE  1 
ATOM   2965 N NZ  . LYS C 2 82  ? 15.809 37.036  117.665 1.00 60.68  ? 79  LYS C NZ  1 
ATOM   2966 N N   . GLY C 2 83  ? 9.429  39.645  119.541 1.00 52.88  ? 80  GLY C N   1 
ATOM   2967 C CA  . GLY C 2 83  ? 8.079  39.135  119.633 1.00 51.30  ? 80  GLY C CA  1 
ATOM   2968 C C   . GLY C 2 83  ? 7.951  37.849  120.404 1.00 50.18  ? 80  GLY C C   1 
ATOM   2969 O O   . GLY C 2 83  ? 7.136  36.987  120.054 1.00 53.68  ? 80  GLY C O   1 
ATOM   2970 N N   . LEU C 2 84  ? 8.709  37.764  121.481 1.00 39.94  ? 81  LEU C N   1 
ATOM   2971 C CA  . LEU C 2 84  ? 8.699  36.612  122.356 1.00 43.34  ? 81  LEU C CA  1 
ATOM   2972 C C   . LEU C 2 84  ? 7.916  36.915  123.614 1.00 43.41  ? 81  LEU C C   1 
ATOM   2973 O O   . LEU C 2 84  ? 7.369  36.016  124.256 1.00 42.03  ? 81  LEU C O   1 
ATOM   2974 C CB  . LEU C 2 84  ? 10.151 36.261  122.735 1.00 44.63  ? 81  LEU C CB  1 
ATOM   2975 C CG  . LEU C 2 84  ? 11.041 35.945  121.520 1.00 45.57  ? 81  LEU C CG  1 
ATOM   2976 C CD1 . LEU C 2 84  ? 12.503 36.061  121.830 1.00 47.54  ? 81  LEU C CD1 1 
ATOM   2977 C CD2 . LEU C 2 84  ? 10.757 34.547  121.061 1.00 48.25  ? 81  LEU C CD2 1 
ATOM   2978 N N   . ILE C 2 85  ? 7.876  38.187  123.995 1.00 45.55  ? 82  ILE C N   1 
ATOM   2979 C CA  . ILE C 2 85  ? 7.148  38.567  125.179 1.00 51.83  ? 82  ILE C CA  1 
ATOM   2980 C C   . ILE C 2 85  ? 6.347  39.838  124.954 1.00 51.47  ? 82  ILE C C   1 
ATOM   2981 O O   . ILE C 2 85  ? 6.554  40.572  123.962 1.00 50.20  ? 82  ILE C O   1 
ATOM   2982 C CB  . ILE C 2 85  ? 8.099  38.819  126.360 1.00 51.51  ? 82  ILE C CB  1 
ATOM   2983 C CG1 . ILE C 2 85  ? 9.180  39.811  125.946 1.00 56.44  ? 82  ILE C CG1 1 
ATOM   2984 C CG2 . ILE C 2 85  ? 8.738  37.540  126.845 1.00 50.94  ? 82  ILE C CG2 1 
ATOM   2985 C CD1 . ILE C 2 85  ? 9.660  40.601  127.139 1.00 60.33  ? 82  ILE C CD1 1 
ATOM   2986 N N   . VAL C 2 86  ? 5.464  40.106  125.920 1.00 47.44  ? 83  VAL C N   1 
ATOM   2987 C CA  . VAL C 2 86  ? 4.935  41.464  126.114 1.00 47.46  ? 83  VAL C CA  1 
ATOM   2988 C C   . VAL C 2 86  ? 4.920  41.781  127.620 1.00 48.24  ? 83  VAL C C   1 
ATOM   2989 O O   . VAL C 2 86  ? 4.867  40.864  128.456 1.00 45.46  ? 83  VAL C O   1 
ATOM   2990 C CB  . VAL C 2 86  ? 3.509  41.661  125.487 1.00 46.35  ? 83  VAL C CB  1 
ATOM   2991 C CG1 . VAL C 2 86  ? 3.485  41.383  123.983 1.00 40.72  ? 83  VAL C CG1 1 
ATOM   2992 C CG2 . VAL C 2 86  ? 2.462  40.804  126.171 1.00 46.08  ? 83  VAL C CG2 1 
ATOM   2993 N N   . ARG C 2 87  ? 5.022  43.085  127.923 1.00 63.60  ? 84  ARG C N   1 
ATOM   2994 C CA  . ARG C 2 87  ? 4.858  43.686  129.275 1.00 66.95  ? 84  ARG C CA  1 
ATOM   2995 C C   . ARG C 2 87  ? 3.476  44.239  129.368 1.00 73.26  ? 84  ARG C C   1 
ATOM   2996 O O   . ARG C 2 87  ? 3.110  45.083  128.552 1.00 72.82  ? 84  ARG C O   1 
ATOM   2997 C CB  . ARG C 2 87  ? 5.726  44.946  129.478 1.00 71.20  ? 84  ARG C CB  1 
ATOM   2998 C CG  . ARG C 2 87  ? 7.224  44.812  129.441 1.00 75.27  ? 84  ARG C CG  1 
ATOM   2999 C CD  . ARG C 2 87  ? 7.914  46.010  130.107 1.00 75.23  ? 84  ARG C CD  1 
ATOM   3000 N NE  . ARG C 2 87  ? 9.369  45.798  130.247 1.00 68.96  ? 84  ARG C NE  1 
ATOM   3001 C CZ  . ARG C 2 87  ? 10.257 45.870  129.251 1.00 62.17  ? 84  ARG C CZ  1 
ATOM   3002 N NH1 . ARG C 2 87  ? 9.914  46.233  128.014 1.00 62.63  ? 84  ARG C NH1 1 
ATOM   3003 N NH2 . ARG C 2 87  ? 11.534 45.645  129.500 1.00 70.19  ? 84  ARG C NH2 1 
ATOM   3004 N N   . LYS C 2 88  ? 2.709  43.824  130.354 1.00 79.11  ? 85  LYS C N   1 
ATOM   3005 C CA  . LYS C 2 88  ? 1.481  44.519  130.644 1.00 85.75  ? 85  LYS C CA  1 
ATOM   3006 C C   . LYS C 2 88  ? 1.687  45.256  131.955 1.00 89.57  ? 85  LYS C C   1 
ATOM   3007 O O   . LYS C 2 88  ? 2.269  44.701  132.894 1.00 80.32  ? 85  LYS C O   1 
ATOM   3008 C CB  . LYS C 2 88  ? 0.299  43.548  130.689 1.00 98.97  ? 85  LYS C CB  1 
ATOM   3009 C CG  . LYS C 2 88  ? -0.573 43.613  129.424 1.00 110.46 ? 85  LYS C CG  1 
ATOM   3010 C CD  . LYS C 2 88  ? -1.751 44.597  129.574 1.00 119.38 ? 85  LYS C CD  1 
ATOM   3011 C CE  . LYS C 2 88  ? -2.063 45.384  128.300 1.00 117.48 ? 85  LYS C CE  1 
ATOM   3012 N NZ  . LYS C 2 88  ? -2.057 44.549  127.064 1.00 110.11 ? 85  LYS C NZ  1 
ATOM   3013 N N   . VAL C 2 89  ? 1.240  46.516  132.014 1.00 86.90  ? 86  VAL C N   1 
ATOM   3014 C CA  . VAL C 2 89  ? 1.299  47.271  133.268 1.00 76.73  ? 86  VAL C CA  1 
ATOM   3015 C C   . VAL C 2 89  ? 0.554  46.467  134.329 1.00 77.29  ? 86  VAL C C   1 
ATOM   3016 O O   . VAL C 2 89  ? -0.512 45.933  134.054 1.00 69.22  ? 86  VAL C O   1 
ATOM   3017 C CB  . VAL C 2 89  ? 0.713  48.688  133.141 1.00 73.25  ? 86  VAL C CB  1 
ATOM   3018 C CG1 . VAL C 2 89  ? 0.793  49.408  134.486 1.00 75.16  ? 86  VAL C CG1 1 
ATOM   3019 C CG2 . VAL C 2 89  ? 1.454  49.471  132.062 1.00 68.22  ? 86  VAL C CG2 1 
ATOM   3020 N N   . ASP C 2 90  ? 1.134  46.341  135.522 1.00 84.28  ? 87  ASP C N   1 
ATOM   3021 C CA  . ASP C 2 90  ? 0.564  45.463  136.549 1.00 97.85  ? 87  ASP C CA  1 
ATOM   3022 C C   . ASP C 2 90  ? -0.812 46.036  136.913 1.00 109.16 ? 87  ASP C C   1 
ATOM   3023 O O   . ASP C 2 90  ? -0.935 47.244  137.165 1.00 103.68 ? 87  ASP C O   1 
ATOM   3024 C CB  . ASP C 2 90  ? 1.510  45.333  137.774 1.00 95.33  ? 87  ASP C CB  1 
ATOM   3025 C CG  . ASP C 2 90  ? 1.314  44.027  138.556 1.00 94.18  ? 87  ASP C CG  1 
ATOM   3026 O OD1 . ASP C 2 90  ? 0.151  43.593  138.735 1.00 82.62  ? 87  ASP C OD1 1 
ATOM   3027 O OD2 . ASP C 2 90  ? 2.337  43.440  138.997 1.00 97.46  ? 87  ASP C OD2 1 
ATOM   3028 N N   . VAL C 2 91  ? -1.837 45.174  136.888 1.00 120.98 ? 88  VAL C N   1 
ATOM   3029 C CA  . VAL C 2 91  ? -3.239 45.585  137.126 1.00 126.16 ? 88  VAL C CA  1 
ATOM   3030 C C   . VAL C 2 91  ? -3.425 46.003  138.592 1.00 132.54 ? 88  VAL C C   1 
ATOM   3031 O O   . VAL C 2 91  ? -4.187 46.932  138.885 1.00 118.68 ? 88  VAL C O   1 
ATOM   3032 C CB  . VAL C 2 91  ? -4.272 44.467  136.769 1.00 120.10 ? 88  VAL C CB  1 
ATOM   3033 C CG1 . VAL C 2 91  ? -5.690 45.031  136.750 1.00 109.21 ? 88  VAL C CG1 1 
ATOM   3034 C CG2 . VAL C 2 91  ? -3.946 43.802  135.431 1.00 121.80 ? 88  VAL C CG2 1 
ATOM   3035 N N   . LYS C 2 92  ? -2.692 45.321  139.485 1.00 144.37 ? 89  LYS C N   1 
ATOM   3036 C CA  . LYS C 2 92  ? -2.757 45.517  140.942 1.00 139.47 ? 89  LYS C CA  1 
ATOM   3037 C C   . LYS C 2 92  ? -1.502 46.255  141.488 1.00 129.71 ? 89  LYS C C   1 
ATOM   3038 O O   . LYS C 2 92  ? -1.107 46.066  142.638 1.00 131.39 ? 89  LYS C O   1 
ATOM   3039 C CB  . LYS C 2 92  ? -2.953 44.145  141.624 1.00 139.67 ? 89  LYS C CB  1 
ATOM   3040 C CG  . LYS C 2 92  ? -4.190 44.032  142.519 1.00 141.20 ? 89  LYS C CG  1 
ATOM   3041 C CD  . LYS C 2 92  ? -4.041 44.773  143.844 1.00 143.82 ? 89  LYS C CD  1 
ATOM   3042 C CE  . LYS C 2 92  ? -4.829 44.107  144.975 1.00 139.41 ? 89  LYS C CE  1 
ATOM   3043 N NZ  . LYS C 2 92  ? -4.179 44.315  146.304 1.00 134.62 ? 89  LYS C NZ  1 
ATOM   3044 N N   . ASP C 2 93  ? -0.876 47.078  140.644 1.00 124.40 ? 90  ASP C N   1 
ATOM   3045 C CA  . ASP C 2 93  ? 0.149  48.047  141.065 1.00 118.97 ? 90  ASP C CA  1 
ATOM   3046 C C   . ASP C 2 93  ? 0.584  48.858  139.813 1.00 119.21 ? 90  ASP C C   1 
ATOM   3047 O O   . ASP C 2 93  ? 0.764  48.306  138.733 1.00 109.23 ? 90  ASP C O   1 
ATOM   3048 C CB  . ASP C 2 93  ? 1.345  47.344  141.745 1.00 121.63 ? 90  ASP C CB  1 
ATOM   3049 C CG  . ASP C 2 93  ? 2.001  48.185  142.881 1.00 123.36 ? 90  ASP C CG  1 
ATOM   3050 O OD1 . ASP C 2 93  ? 2.457  49.331  142.635 1.00 115.50 ? 90  ASP C OD1 1 
ATOM   3051 O OD2 . ASP C 2 93  ? 2.127  47.660  144.012 1.00 110.87 ? 90  ASP C OD2 1 
ATOM   3052 N N   . ARG C 2 94  ? 0.723  50.170  139.948 1.00 126.76 ? 91  ARG C N   1 
ATOM   3053 C CA  . ARG C 2 94  ? 1.148  51.017  138.828 1.00 135.61 ? 91  ARG C CA  1 
ATOM   3054 C C   . ARG C 2 94  ? 2.674  51.194  138.860 1.00 134.47 ? 91  ARG C C   1 
ATOM   3055 O O   . ARG C 2 94  ? 3.280  51.205  139.945 1.00 130.44 ? 91  ARG C O   1 
ATOM   3056 C CB  . ARG C 2 94  ? 0.434  52.373  138.910 1.00 148.81 ? 91  ARG C CB  1 
ATOM   3057 C CG  . ARG C 2 94  ? 0.358  53.149  137.603 1.00 145.08 ? 91  ARG C CG  1 
ATOM   3058 C CD  . ARG C 2 94  ? -0.686 54.260  137.671 1.00 138.50 ? 91  ARG C CD  1 
ATOM   3059 N NE  . ARG C 2 94  ? -0.292 55.389  138.529 1.00 139.31 ? 91  ARG C NE  1 
ATOM   3060 C CZ  . ARG C 2 94  ? -0.835 55.715  139.712 1.00 136.71 ? 91  ARG C CZ  1 
ATOM   3061 N NH1 . ARG C 2 94  ? -1.823 55.005  140.251 1.00 135.70 ? 91  ARG C NH1 1 
ATOM   3062 N NH2 . ARG C 2 94  ? -0.383 56.781  140.372 1.00 123.84 ? 91  ARG C NH2 1 
ATOM   3063 N N   . ARG C 2 95  ? 3.279  51.319  137.672 1.00 133.45 ? 92  ARG C N   1 
ATOM   3064 C CA  . ARG C 2 95  ? 4.763  51.357  137.474 1.00 138.24 ? 92  ARG C CA  1 
ATOM   3065 C C   . ARG C 2 95  ? 5.403  49.931  137.440 1.00 120.07 ? 92  ARG C C   1 
ATOM   3066 O O   . ARG C 2 95  ? 6.227  49.635  136.564 1.00 105.64 ? 92  ARG C O   1 
ATOM   3067 C CB  . ARG C 2 95  ? 5.480  52.283  138.498 1.00 140.38 ? 92  ARG C CB  1 
ATOM   3068 C CG  . ARG C 2 95  ? 6.557  53.206  137.905 1.00 133.20 ? 92  ARG C CG  1 
ATOM   3069 C CD  . ARG C 2 95  ? 7.642  53.617  138.910 1.00 131.40 ? 92  ARG C CD  1 
ATOM   3070 N NE  . ARG C 2 95  ? 7.130  53.870  140.264 1.00 131.29 ? 92  ARG C NE  1 
ATOM   3071 C CZ  . ARG C 2 95  ? 7.885  53.980  141.363 1.00 124.61 ? 92  ARG C CZ  1 
ATOM   3072 N NH1 . ARG C 2 95  ? 9.216  53.875  141.295 1.00 117.76 ? 92  ARG C NH1 1 
ATOM   3073 N NH2 . ARG C 2 95  ? 7.302  54.193  142.546 1.00 110.16 ? 92  ARG C NH2 1 
ATOM   3074 N N   . LYS C 2 96  ? 5.028  49.068  138.390 1.00 100.45 ? 93  LYS C N   1 
ATOM   3075 C CA  . LYS C 2 96  ? 5.314  47.633  138.298 1.00 86.66  ? 93  LYS C CA  1 
ATOM   3076 C C   . LYS C 2 96  ? 4.720  47.039  137.021 1.00 82.69  ? 93  LYS C C   1 
ATOM   3077 O O   . LYS C 2 96  ? 3.603  47.381  136.645 1.00 71.19  ? 93  LYS C O   1 
ATOM   3078 C CB  . LYS C 2 96  ? 4.734  46.889  139.485 1.00 86.85  ? 93  LYS C CB  1 
ATOM   3079 C CG  . LYS C 2 96  ? 5.402  47.230  140.804 1.00 93.17  ? 93  LYS C CG  1 
ATOM   3080 C CD  . LYS C 2 96  ? 4.720  46.597  142.014 1.00 95.63  ? 93  LYS C CD  1 
ATOM   3081 C CE  . LYS C 2 96  ? 4.379  45.122  141.828 1.00 101.22 ? 93  LYS C CE  1 
ATOM   3082 N NZ  . LYS C 2 96  ? 5.601  44.287  141.637 1.00 105.08 ? 93  LYS C NZ  1 
ATOM   3083 N N   . PHE C 2 97  ? 5.486  46.181  136.342 1.00 77.30  ? 94  PHE C N   1 
ATOM   3084 C CA  . PHE C 2 97  ? 5.001  45.488  135.151 1.00 66.57  ? 94  PHE C CA  1 
ATOM   3085 C C   . PHE C 2 97  ? 4.915  43.988  135.347 1.00 61.77  ? 94  PHE C C   1 
ATOM   3086 O O   . PHE C 2 97  ? 5.523  43.413  136.233 1.00 66.54  ? 94  PHE C O   1 
ATOM   3087 C CB  . PHE C 2 97  ? 5.918  45.681  133.990 1.00 69.41  ? 94  PHE C CB  1 
ATOM   3088 C CG  . PHE C 2 97  ? 6.077  47.095  133.526 1.00 78.34  ? 94  PHE C CG  1 
ATOM   3089 C CD1 . PHE C 2 97  ? 5.141  47.667  132.668 1.00 77.76  ? 94  PHE C CD1 1 
ATOM   3090 C CD2 . PHE C 2 97  ? 7.244  47.813  133.824 1.00 77.53  ? 94  PHE C CD2 1 
ATOM   3091 C CE1 . PHE C 2 97  ? 5.331  48.951  132.155 1.00 80.77  ? 94  PHE C CE1 1 
ATOM   3092 C CE2 . PHE C 2 97  ? 7.436  49.092  133.314 1.00 81.87  ? 94  PHE C CE2 1 
ATOM   3093 C CZ  . PHE C 2 97  ? 6.476  49.667  132.483 1.00 83.84  ? 94  PHE C CZ  1 
ATOM   3094 N N   . GLN C 2 98  ? 4.134  43.349  134.498 1.00 67.55  ? 95  GLN C N   1 
ATOM   3095 C CA  . GLN C 2 98  ? 4.106  41.887  134.433 1.00 66.94  ? 95  GLN C CA  1 
ATOM   3096 C C   . GLN C 2 98  ? 4.656  41.428  133.075 1.00 63.55  ? 95  GLN C C   1 
ATOM   3097 O O   . GLN C 2 98  ? 4.560  42.174  132.098 1.00 51.49  ? 95  GLN C O   1 
ATOM   3098 C CB  . GLN C 2 98  ? 2.712  41.378  134.649 1.00 60.87  ? 95  GLN C CB  1 
ATOM   3099 C CG  . GLN C 2 98  ? 2.406  40.902  136.045 1.00 59.91  ? 95  GLN C CG  1 
ATOM   3100 C CD  . GLN C 2 98  ? 0.930  40.561  136.151 1.00 67.97  ? 95  GLN C CD  1 
ATOM   3101 O OE1 . GLN C 2 98  ? 0.520  39.401  136.371 1.00 52.97  ? 95  GLN C OE1 1 
ATOM   3102 N NE2 . GLN C 2 98  ? 0.104  41.589  135.930 1.00 78.96  ? 95  GLN C NE2 1 
ATOM   3103 N N   . ILE C 2 99  ? 5.303  40.255  133.033 1.00 59.09  ? 96  ILE C N   1 
ATOM   3104 C CA  . ILE C 2 99  ? 5.868  39.756  131.749 1.00 53.69  ? 96  ILE C CA  1 
ATOM   3105 C C   . ILE C 2 99  ? 5.102  38.524  131.259 1.00 47.00  ? 96  ILE C C   1 
ATOM   3106 O O   . ILE C 2 99  ? 4.905  37.517  132.013 1.00 45.38  ? 96  ILE C O   1 
ATOM   3107 C CB  . ILE C 2 99  ? 7.387  39.470  131.878 1.00 48.35  ? 96  ILE C CB  1 
ATOM   3108 C CG1 . ILE C 2 99  ? 8.087  40.707  132.461 1.00 48.15  ? 96  ILE C CG1 1 
ATOM   3109 C CG2 . ILE C 2 99  ? 8.006  39.138  130.526 1.00 43.74  ? 96  ILE C CG2 1 
ATOM   3110 C CD1 . ILE C 2 99  ? 8.198  41.854  131.466 1.00 52.02  ? 96  ILE C CD1 1 
ATOM   3111 N N   . PHE C 2 100 ? 4.640  38.593  130.019 1.00 35.42  ? 97  PHE C N   1 
ATOM   3112 C CA  . PHE C 2 100 ? 3.868  37.433  129.518 1.00 40.79  ? 97  PHE C CA  1 
ATOM   3113 C C   . PHE C 2 100 ? 4.403  36.956  128.184 1.00 39.31  ? 97  PHE C C   1 
ATOM   3114 O O   . PHE C 2 100 ? 4.822  37.753  127.312 1.00 43.81  ? 97  PHE C O   1 
ATOM   3115 C CB  . PHE C 2 100 ? 2.351  37.776  129.300 1.00 47.50  ? 97  PHE C CB  1 
ATOM   3116 C CG  . PHE C 2 100 ? 1.518  37.834  130.547 1.00 38.69  ? 97  PHE C CG  1 
ATOM   3117 C CD1 . PHE C 2 100 ? 0.987  36.725  131.056 1.00 45.42  ? 97  PHE C CD1 1 
ATOM   3118 C CD2 . PHE C 2 100 ? 1.207  39.045  131.126 1.00 46.17  ? 97  PHE C CD2 1 
ATOM   3119 C CE1 . PHE C 2 100 ? 0.201  36.746  132.211 1.00 54.27  ? 97  PHE C CE1 1 
ATOM   3120 C CE2 . PHE C 2 100 ? 0.421  39.113  132.271 1.00 48.27  ? 97  PHE C CE2 1 
ATOM   3121 C CZ  . PHE C 2 100 ? -0.095 37.949  132.820 1.00 50.73  ? 97  PHE C CZ  1 
ATOM   3122 N N   . LEU C 2 101 ? 4.335  35.652  127.988 1.00 37.62  ? 98  LEU C N   1 
ATOM   3123 C CA  . LEU C 2 101 ? 4.731  35.096  126.709 1.00 37.06  ? 98  LEU C CA  1 
ATOM   3124 C C   . LEU C 2 101 ? 3.767  35.383  125.584 1.00 41.84  ? 98  LEU C C   1 
ATOM   3125 O O   . LEU C 2 101 ? 2.523  35.229  125.726 1.00 38.21  ? 98  LEU C O   1 
ATOM   3126 C CB  . LEU C 2 101 ? 4.790  33.568  126.843 1.00 40.65  ? 98  LEU C CB  1 
ATOM   3127 C CG  . LEU C 2 101 ? 5.852  33.048  127.846 1.00 39.37  ? 98  LEU C CG  1 
ATOM   3128 C CD1 . LEU C 2 101 ? 5.531  31.630  128.213 1.00 37.63  ? 98  LEU C CD1 1 
ATOM   3129 C CD2 . LEU C 2 101 ? 7.264  33.196  127.320 1.00 38.75  ? 98  LEU C CD2 1 
ATOM   3130 N N   . THR C 2 102 ? 4.325  35.700  124.424 1.00 39.25  ? 99  THR C N   1 
ATOM   3131 C CA  . THR C 2 102 ? 3.537  35.628  123.224 1.00 36.79  ? 99  THR C CA  1 
ATOM   3132 C C   . THR C 2 102 ? 3.273  34.161  122.857 1.00 37.76  ? 99  THR C C   1 
ATOM   3133 O O   . THR C 2 102 ? 3.603  33.295  123.619 1.00 40.83  ? 99  THR C O   1 
ATOM   3134 C CB  . THR C 2 102 ? 4.199  36.328  122.041 1.00 39.96  ? 99  THR C CB  1 
ATOM   3135 O OG1 . THR C 2 102 ? 5.408  35.652  121.705 1.00 39.20  ? 99  THR C OG1 1 
ATOM   3136 C CG2 . THR C 2 102 ? 4.469  37.772  122.352 1.00 37.30  ? 99  THR C CG2 1 
ATOM   3137 N N   . ASP C 2 103 ? 2.594  33.903  121.741 1.00 37.22  ? 100 ASP C N   1 
ATOM   3138 C CA  . ASP C 2 103 ? 2.280  32.579  121.287 1.00 40.10  ? 100 ASP C CA  1 
ATOM   3139 C C   . ASP C 2 103 ? 3.609  31.975  120.854 1.00 39.55  ? 100 ASP C C   1 
ATOM   3140 O O   . ASP C 2 103 ? 3.914  30.845  121.164 1.00 38.18  ? 100 ASP C O   1 
ATOM   3141 C CB  . ASP C 2 103 ? 1.349  32.617  120.044 1.00 44.39  ? 100 ASP C CB  1 
ATOM   3142 C CG  . ASP C 2 103 ? -0.122 33.037  120.356 1.00 53.36  ? 100 ASP C CG  1 
ATOM   3143 O OD1 . ASP C 2 103 ? -0.581 33.118  121.534 1.00 53.11  ? 100 ASP C OD1 1 
ATOM   3144 O OD2 . ASP C 2 103 ? -0.847 33.269  119.367 1.00 56.36  ? 100 ASP C OD2 1 
ATOM   3145 N N   . LEU C 2 104 ? 4.393  32.750  120.118 1.00 40.82  ? 101 LEU C N   1 
ATOM   3146 C CA  . LEU C 2 104 ? 5.733  32.329  119.724 1.00 44.61  ? 101 LEU C CA  1 
ATOM   3147 C C   . LEU C 2 104 ? 6.546  31.898  120.963 1.00 40.97  ? 101 LEU C C   1 
ATOM   3148 O O   . LEU C 2 104 ? 7.119  30.832  120.993 1.00 42.12  ? 101 LEU C O   1 
ATOM   3149 C CB  . LEU C 2 104 ? 6.449  33.464  118.988 1.00 45.22  ? 101 LEU C CB  1 
ATOM   3150 C CG  . LEU C 2 104 ? 7.862  33.104  118.481 1.00 53.29  ? 101 LEU C CG  1 
ATOM   3151 C CD1 . LEU C 2 104 ? 7.939  31.715  117.791 1.00 47.21  ? 101 LEU C CD1 1 
ATOM   3152 C CD2 . LEU C 2 104 ? 8.324  34.216  117.535 1.00 45.67  ? 101 LEU C CD2 1 
ATOM   3153 N N   . GLY C 2 105 ? 6.506  32.694  122.009 1.00 37.84  ? 102 GLY C N   1 
ATOM   3154 C CA  . GLY C 2 105 ? 7.224  32.388  123.216 1.00 40.44  ? 102 GLY C CA  1 
ATOM   3155 C C   . GLY C 2 105 ? 6.768  31.091  123.811 1.00 43.90  ? 102 GLY C C   1 
ATOM   3156 O O   . GLY C 2 105 ? 7.570  30.349  124.352 1.00 52.09  ? 102 GLY C O   1 
ATOM   3157 N N   . ARG C 2 106 ? 5.479  30.817  123.764 1.00 42.44  ? 103 ARG C N   1 
ATOM   3158 C CA  . ARG C 2 106 ? 4.965  29.573  124.362 1.00 46.00  ? 103 ARG C CA  1 
ATOM   3159 C C   . ARG C 2 106 ? 5.370  28.404  123.467 1.00 44.51  ? 103 ARG C C   1 
ATOM   3160 O O   . ARG C 2 106 ? 5.764  27.387  123.990 1.00 45.51  ? 103 ARG C O   1 
ATOM   3161 C CB  . ARG C 2 106 ? 3.420  29.538  124.574 1.00 42.99  ? 103 ARG C CB  1 
ATOM   3162 C CG  . ARG C 2 106 ? 2.966  29.915  125.989 1.00 54.21  ? 103 ARG C CG  1 
ATOM   3163 C CD  . ARG C 2 106 ? 1.470  29.633  126.319 1.00 53.91  ? 103 ARG C CD  1 
ATOM   3164 N NE  . ARG C 2 106 ? 0.695  29.842  125.115 1.00 48.51  ? 103 ARG C NE  1 
ATOM   3165 C CZ  . ARG C 2 106 ? 0.236  31.014  124.683 1.00 44.04  ? 103 ARG C CZ  1 
ATOM   3166 N NH1 . ARG C 2 106 ? 0.369  32.132  125.397 1.00 46.86  ? 103 ARG C NH1 1 
ATOM   3167 N NH2 . ARG C 2 106 ? -0.390 31.053  123.507 1.00 48.25  ? 103 ARG C NH2 1 
ATOM   3168 N N   . GLU C 2 107 ? 5.282  28.564  122.146 1.00 39.48  ? 104 GLU C N   1 
ATOM   3169 C CA  . GLU C 2 107 ? 5.550  27.455  121.228 1.00 43.34  ? 104 GLU C CA  1 
ATOM   3170 C C   . GLU C 2 107 ? 7.000  26.993  121.246 1.00 42.28  ? 104 GLU C C   1 
ATOM   3171 O O   . GLU C 2 107 ? 7.264  25.845  120.952 1.00 48.22  ? 104 GLU C O   1 
ATOM   3172 C CB  . GLU C 2 107 ? 5.172  27.826  119.810 1.00 42.64  ? 104 GLU C CB  1 
ATOM   3173 C CG  . GLU C 2 107 ? 3.681  27.871  119.636 1.00 57.94  ? 104 GLU C CG  1 
ATOM   3174 C CD  . GLU C 2 107 ? 3.265  28.679  118.429 1.00 70.87  ? 104 GLU C CD  1 
ATOM   3175 O OE1 . GLU C 2 107 ? 4.151  29.082  117.606 1.00 66.79  ? 104 GLU C OE1 1 
ATOM   3176 O OE2 . GLU C 2 107 ? 2.033  28.896  118.327 1.00 77.69  ? 104 GLU C OE2 1 
ATOM   3177 N N   . LEU C 2 108 ? 7.902  27.912  121.564 1.00 37.58  ? 105 LEU C N   1 
ATOM   3178 C CA  . LEU C 2 108 ? 9.311  27.669  121.631 1.00 38.70  ? 105 LEU C CA  1 
ATOM   3179 C C   . LEU C 2 108 ? 9.760  26.742  122.759 1.00 43.01  ? 105 LEU C C   1 
ATOM   3180 O O   . LEU C 2 108 ? 10.901 26.254  122.721 1.00 45.69  ? 105 LEU C O   1 
ATOM   3181 C CB  . LEU C 2 108 ? 10.018 28.992  121.757 1.00 36.62  ? 105 LEU C CB  1 
ATOM   3182 C CG  . LEU C 2 108 ? 10.587 29.609  120.499 1.00 43.56  ? 105 LEU C CG  1 
ATOM   3183 C CD1 . LEU C 2 108 ? 10.154 28.953  119.212 1.00 49.59  ? 105 LEU C CD1 1 
ATOM   3184 C CD2 . LEU C 2 108 ? 10.391 31.108  120.446 1.00 41.81  ? 105 LEU C CD2 1 
ATOM   3185 N N   . GLU C 2 109 ? 8.893  26.489  123.750 1.00 38.19  ? 106 GLU C N   1 
ATOM   3186 C CA  . GLU C 2 109 ? 9.288  25.680  124.877 1.00 39.25  ? 106 GLU C CA  1 
ATOM   3187 C C   . GLU C 2 109 ? 9.897  24.279  124.537 1.00 41.17  ? 106 GLU C C   1 
ATOM   3188 O O   . GLU C 2 109 ? 11.039 23.949  124.944 1.00 37.18  ? 106 GLU C O   1 
ATOM   3189 C CB  . GLU C 2 109 ? 8.161  25.493  125.848 1.00 37.83  ? 106 GLU C CB  1 
ATOM   3190 C CG  . GLU C 2 109 ? 8.578  24.749  127.113 1.00 40.16  ? 106 GLU C CG  1 
ATOM   3191 C CD  . GLU C 2 109 ? 7.521  24.707  128.198 1.00 40.70  ? 106 GLU C CD  1 
ATOM   3192 O OE1 . GLU C 2 109 ? 6.307  24.943  127.913 1.00 45.81  ? 106 GLU C OE1 1 
ATOM   3193 O OE2 . GLU C 2 109 ? 7.929  24.386  129.331 1.00 36.59  ? 106 GLU C OE2 1 
ATOM   3194 N N   . GLU C 2 110 ? 9.121  23.482  123.833 1.00 36.36  ? 107 GLU C N   1 
ATOM   3195 C CA  . GLU C 2 110 ? 9.512  22.169  123.421 1.00 37.95  ? 107 GLU C CA  1 
ATOM   3196 C C   . GLU C 2 110 ? 10.789 22.209  122.500 1.00 40.61  ? 107 GLU C C   1 
ATOM   3197 O O   . GLU C 2 110 ? 11.765 21.578  122.774 1.00 36.93  ? 107 GLU C O   1 
ATOM   3198 C CB  . GLU C 2 110 ? 8.299  21.494  122.789 1.00 38.75  ? 107 GLU C CB  1 
ATOM   3199 C CG  . GLU C 2 110 ? 8.533  20.761  121.475 1.00 59.27  ? 107 GLU C CG  1 
ATOM   3200 C CD  . GLU C 2 110 ? 9.462  19.588  121.572 1.00 59.91  ? 107 GLU C CD  1 
ATOM   3201 O OE1 . GLU C 2 110 ? 10.327 19.479  120.707 1.00 68.80  ? 107 GLU C OE1 1 
ATOM   3202 O OE2 . GLU C 2 110 ? 9.321  18.772  122.499 1.00 92.73  ? 107 GLU C OE2 1 
ATOM   3203 N N   . PRO C 2 111 ? 10.769 22.963  121.410 1.00 38.74  ? 108 PRO C N   1 
ATOM   3204 C CA  . PRO C 2 111 ? 11.916 22.788  120.574 1.00 35.11  ? 108 PRO C CA  1 
ATOM   3205 C C   . PRO C 2 111 ? 13.187 23.319  121.199 1.00 37.14  ? 108 PRO C C   1 
ATOM   3206 O O   . PRO C 2 111 ? 14.219 22.651  121.216 1.00 38.68  ? 108 PRO C O   1 
ATOM   3207 C CB  . PRO C 2 111 ? 11.550 23.588  119.288 1.00 39.23  ? 108 PRO C CB  1 
ATOM   3208 C CG  . PRO C 2 111 ? 10.398 24.485  119.680 1.00 39.33  ? 108 PRO C CG  1 
ATOM   3209 C CD  . PRO C 2 111 ? 9.691  23.781  120.798 1.00 39.11  ? 108 PRO C CD  1 
ATOM   3210 N N   . LEU C 2 112 ? 13.144 24.520  121.741 1.00 40.88  ? 109 LEU C N   1 
ATOM   3211 C CA  . LEU C 2 112 ? 14.331 24.992  122.440 1.00 36.23  ? 109 LEU C CA  1 
ATOM   3212 C C   . LEU C 2 112 ? 14.768 24.051  123.584 1.00 35.40  ? 109 LEU C C   1 
ATOM   3213 O O   . LEU C 2 112 ? 15.936 23.837  123.751 1.00 42.09  ? 109 LEU C O   1 
ATOM   3214 C CB  . LEU C 2 112 ? 14.128 26.381  122.934 1.00 33.34  ? 109 LEU C CB  1 
ATOM   3215 C CG  . LEU C 2 112 ? 13.831 27.431  121.881 1.00 32.70  ? 109 LEU C CG  1 
ATOM   3216 C CD1 . LEU C 2 112 ? 13.896 28.766  122.618 1.00 33.29  ? 109 LEU C CD1 1 
ATOM   3217 C CD2 . LEU C 2 112 ? 14.798 27.404  120.745 1.00 29.84  ? 109 LEU C CD2 1 
ATOM   3218 N N   . ASN C 2 113 ? 13.868 23.453  124.349 1.00 34.69  ? 110 ASN C N   1 
ATOM   3219 C CA  . ASN C 2 113 ? 14.320 22.558  125.415 1.00 35.34  ? 110 ASN C CA  1 
ATOM   3220 C C   . ASN C 2 113 ? 14.925 21.274  124.866 1.00 39.74  ? 110 ASN C C   1 
ATOM   3221 O O   . ASN C 2 113 ? 15.821 20.691  125.495 1.00 37.10  ? 110 ASN C O   1 
ATOM   3222 C CB  . ASN C 2 113 ? 13.192 22.182  126.362 1.00 32.21  ? 110 ASN C CB  1 
ATOM   3223 C CG  . ASN C 2 113 ? 12.933 23.248  127.439 1.00 39.68  ? 110 ASN C CG  1 
ATOM   3224 O OD1 . ASN C 2 113 ? 13.762 24.178  127.708 1.00 40.82  ? 110 ASN C OD1 1 
ATOM   3225 N ND2 . ASN C 2 113 ? 11.780 23.119  128.072 1.00 35.44  ? 110 ASN C ND2 1 
ATOM   3226 N N   . GLU C 2 114 ? 14.434 20.837  123.708 1.00 40.16  ? 111 GLU C N   1 
ATOM   3227 C CA  . GLU C 2 114 ? 14.992 19.688  123.044 1.00 43.86  ? 111 GLU C CA  1 
ATOM   3228 C C   . GLU C 2 114 ? 16.433 19.947  122.668 1.00 39.56  ? 111 GLU C C   1 
ATOM   3229 O O   . GLU C 2 114 ? 17.297 19.100  122.914 1.00 33.57  ? 111 GLU C O   1 
ATOM   3230 C CB  . GLU C 2 114 ? 14.217 19.267  121.778 1.00 52.88  ? 111 GLU C CB  1 
ATOM   3231 C CG  . GLU C 2 114 ? 14.488 17.799  121.367 1.00 54.47  ? 111 GLU C CG  1 
ATOM   3232 C CD  . GLU C 2 114 ? 14.178 16.861  122.510 1.00 69.05  ? 111 GLU C CD  1 
ATOM   3233 O OE1 . GLU C 2 114 ? 15.110 16.174  123.055 1.00 64.12  ? 111 GLU C OE1 1 
ATOM   3234 O OE2 . GLU C 2 114 ? 12.979 16.887  122.912 1.00 103.45 ? 111 GLU C OE2 1 
ATOM   3235 N N   . ILE C 2 115 ? 16.696 21.102  122.092 1.00 33.64  ? 112 ILE C N   1 
ATOM   3236 C CA  . ILE C 2 115 ? 18.054 21.423  121.686 1.00 33.10  ? 112 ILE C CA  1 
ATOM   3237 C C   . ILE C 2 115 ? 18.944 21.617  122.908 1.00 35.80  ? 112 ILE C C   1 
ATOM   3238 O O   . ILE C 2 115 ? 20.088 21.126  122.930 1.00 38.76  ? 112 ILE C O   1 
ATOM   3239 C CB  . ILE C 2 115 ? 18.061 22.662  120.820 1.00 33.73  ? 112 ILE C CB  1 
ATOM   3240 C CG1 . ILE C 2 115 ? 17.431 22.359  119.482 1.00 34.10  ? 112 ILE C CG1 1 
ATOM   3241 C CG2 . ILE C 2 115 ? 19.429 23.213  120.640 1.00 33.89  ? 112 ILE C CG2 1 
ATOM   3242 C CD1 . ILE C 2 115 ? 17.053 23.589  118.727 1.00 34.91  ? 112 ILE C CD1 1 
ATOM   3243 N N   . ALA C 2 116 ? 18.448 22.280  123.947 1.00 33.27  ? 113 ALA C N   1 
ATOM   3244 C CA  . ALA C 2 116 ? 19.273 22.456  125.171 1.00 32.50  ? 113 ALA C CA  1 
ATOM   3245 C C   . ALA C 2 116 ? 19.542 21.190  125.915 1.00 30.43  ? 113 ALA C C   1 
ATOM   3246 O O   . ALA C 2 116 ? 20.549 21.032  126.547 1.00 38.86  ? 113 ALA C O   1 
ATOM   3247 C CB  . ALA C 2 116 ? 18.588 23.385  126.146 1.00 33.94  ? 113 ALA C CB  1 
ATOM   3248 N N   . SER C 2 117 ? 18.561 20.339  125.967 1.00 30.77  ? 114 SER C N   1 
ATOM   3249 C CA  . SER C 2 117 ? 18.729 19.057  126.560 1.00 33.18  ? 114 SER C CA  1 
ATOM   3250 C C   . SER C 2 117 ? 19.796 18.203  125.849 1.00 34.67  ? 114 SER C C   1 
ATOM   3251 O O   . SER C 2 117 ? 20.584 17.561  126.496 1.00 37.14  ? 114 SER C O   1 
ATOM   3252 C CB  . SER C 2 117 ? 17.421 18.309  126.511 1.00 34.87  ? 114 SER C CB  1 
ATOM   3253 O OG  . SER C 2 117 ? 17.509 17.168  127.372 1.00 42.31  ? 114 SER C OG  1 
ATOM   3254 N N   . ILE C 2 118 ? 19.797 18.175  124.532 1.00 33.83  ? 115 ILE C N   1 
ATOM   3255 C CA  . ILE C 2 118 ? 20.730 17.363  123.836 1.00 38.01  ? 115 ILE C CA  1 
ATOM   3256 C C   . ILE C 2 118 ? 22.075 18.040  123.956 1.00 37.54  ? 115 ILE C C   1 
ATOM   3257 O O   . ILE C 2 118 ? 23.078 17.380  124.028 1.00 41.79  ? 115 ILE C O   1 
ATOM   3258 C CB  . ILE C 2 118 ? 20.331 17.245  122.375 1.00 39.85  ? 115 ILE C CB  1 
ATOM   3259 C CG1 . ILE C 2 118 ? 19.225 16.259  122.286 1.00 39.71  ? 115 ILE C CG1 1 
ATOM   3260 C CG2 . ILE C 2 118 ? 21.489 16.878  121.440 1.00 38.09  ? 115 ILE C CG2 1 
ATOM   3261 C CD1 . ILE C 2 118 ? 18.427 16.608  121.031 1.00 41.08  ? 115 ILE C CD1 1 
ATOM   3262 N N   . TYR C 2 119 ? 22.091 19.351  123.983 1.00 37.79  ? 116 TYR C N   1 
ATOM   3263 C CA  . TYR C 2 119 ? 23.345 20.054  124.168 1.00 38.91  ? 116 TYR C CA  1 
ATOM   3264 C C   . TYR C 2 119 ? 23.919 19.763  125.572 1.00 43.37  ? 116 TYR C C   1 
ATOM   3265 O O   . TYR C 2 119 ? 25.133 19.475  125.735 1.00 43.98  ? 116 TYR C O   1 
ATOM   3266 C CB  . TYR C 2 119 ? 23.153 21.546  123.929 1.00 40.48  ? 116 TYR C CB  1 
ATOM   3267 C CG  . TYR C 2 119 ? 24.306 22.335  124.411 1.00 40.52  ? 116 TYR C CG  1 
ATOM   3268 C CD1 . TYR C 2 119 ? 25.421 22.442  123.645 1.00 39.48  ? 116 TYR C CD1 1 
ATOM   3269 C CD2 . TYR C 2 119 ? 24.305 22.920  125.674 1.00 39.67  ? 116 TYR C CD2 1 
ATOM   3270 C CE1 . TYR C 2 119 ? 26.521 23.126  124.085 1.00 42.46  ? 116 TYR C CE1 1 
ATOM   3271 C CE2 . TYR C 2 119 ? 25.395 23.610  126.121 1.00 45.09  ? 116 TYR C CE2 1 
ATOM   3272 C CZ  . TYR C 2 119 ? 26.504 23.714  125.309 1.00 48.15  ? 116 TYR C CZ  1 
ATOM   3273 O OH  . TYR C 2 119 ? 27.636 24.355  125.703 1.00 54.02  ? 116 TYR C OH  1 
ATOM   3274 N N   . ALA C 2 120 ? 23.053 19.781  126.573 1.00 38.82  ? 117 ALA C N   1 
ATOM   3275 C CA  . ALA C 2 120 ? 23.502 19.551  127.950 1.00 44.26  ? 117 ALA C CA  1 
ATOM   3276 C C   . ALA C 2 120 ? 24.036 18.135  128.153 1.00 44.77  ? 117 ALA C C   1 
ATOM   3277 O O   . ALA C 2 120 ? 25.041 17.941  128.778 1.00 44.59  ? 117 ALA C O   1 
ATOM   3278 C CB  . ALA C 2 120 ? 22.349 19.788  128.922 1.00 42.53  ? 117 ALA C CB  1 
ATOM   3279 N N   . THR C 2 121 ? 23.329 17.143  127.635 1.00 41.35  ? 118 THR C N   1 
ATOM   3280 C CA  . THR C 2 121 ? 23.787 15.792  127.710 1.00 41.63  ? 118 THR C CA  1 
ATOM   3281 C C   . THR C 2 121 ? 25.133 15.608  126.998 1.00 41.45  ? 118 THR C C   1 
ATOM   3282 O O   . THR C 2 121 ? 25.973 15.015  127.572 1.00 45.46  ? 118 THR C O   1 
ATOM   3283 C CB  . THR C 2 121 ? 22.741 14.824  127.189 1.00 48.51  ? 118 THR C CB  1 
ATOM   3284 O OG1 . THR C 2 121 ? 21.757 14.654  128.220 1.00 48.31  ? 118 THR C OG1 1 
ATOM   3285 C CG2 . THR C 2 121 ? 23.322 13.479  126.912 1.00 49.14  ? 118 THR C CG2 1 
ATOM   3286 N N   . GLU C 2 122 ? 25.361 16.165  125.818 1.00 39.88  ? 119 GLU C N   1 
ATOM   3287 C CA  . GLU C 2 122 ? 26.712 16.131  125.172 1.00 45.53  ? 119 GLU C CA  1 
ATOM   3288 C C   . GLU C 2 122 ? 27.760 16.831  126.012 1.00 45.58  ? 119 GLU C C   1 
ATOM   3289 O O   . GLU C 2 122 ? 28.838 16.321  126.228 1.00 46.95  ? 119 GLU C O   1 
ATOM   3290 C CB  . GLU C 2 122 ? 26.744 16.849  123.808 1.00 47.30  ? 119 GLU C CB  1 
ATOM   3291 C CG  . GLU C 2 122 ? 26.564 15.983  122.580 1.00 64.13  ? 119 GLU C CG  1 
ATOM   3292 C CD  . GLU C 2 122 ? 27.311 14.642  122.667 1.00 78.40  ? 119 GLU C CD  1 
ATOM   3293 O OE1 . GLU C 2 122 ? 28.582 14.668  122.826 1.00 65.02  ? 119 GLU C OE1 1 
ATOM   3294 O OE2 . GLU C 2 122 ? 26.600 13.581  122.574 1.00 74.52  ? 119 GLU C OE2 1 
ATOM   3295 N N   . THR C 2 123 ? 27.417 18.020  126.479 1.00 42.58  ? 120 THR C N   1 
ATOM   3296 C CA  . THR C 2 123 ? 28.349 18.843  127.168 1.00 42.20  ? 120 THR C CA  1 
ATOM   3297 C C   . THR C 2 123 ? 28.816 18.217  128.489 1.00 42.91  ? 120 THR C C   1 
ATOM   3298 O O   . THR C 2 123 ? 29.914 18.537  128.951 1.00 48.46  ? 120 THR C O   1 
ATOM   3299 C CB  . THR C 2 123 ? 27.722 20.216  127.401 1.00 44.09  ? 120 THR C CB  1 
ATOM   3300 O OG1 . THR C 2 123 ? 27.531 20.852  126.130 1.00 43.81  ? 120 THR C OG1 1 
ATOM   3301 C CG2 . THR C 2 123 ? 28.563 21.087  128.296 1.00 43.26  ? 120 THR C CG2 1 
ATOM   3302 N N   . PHE C 2 124 ? 27.999 17.357  129.092 1.00 40.54  ? 121 PHE C N   1 
ATOM   3303 C CA  . PHE C 2 124 ? 28.294 16.799  130.402 1.00 42.59  ? 121 PHE C CA  1 
ATOM   3304 C C   . PHE C 2 124 ? 28.508 15.244  130.326 1.00 47.11  ? 121 PHE C C   1 
ATOM   3305 O O   . PHE C 2 124 ? 28.494 14.555  131.344 1.00 36.22  ? 121 PHE C O   1 
ATOM   3306 C CB  . PHE C 2 124 ? 27.170 17.152  131.365 1.00 42.87  ? 121 PHE C CB  1 
ATOM   3307 C CG  . PHE C 2 124 ? 27.206 18.605  131.903 1.00 46.13  ? 121 PHE C CG  1 
ATOM   3308 C CD1 . PHE C 2 124 ? 26.529 19.634  131.250 1.00 44.29  ? 121 PHE C CD1 1 
ATOM   3309 C CD2 . PHE C 2 124 ? 27.813 18.915  133.130 1.00 43.20  ? 121 PHE C CD2 1 
ATOM   3310 C CE1 . PHE C 2 124 ? 26.514 20.930  131.759 1.00 45.80  ? 121 PHE C CE1 1 
ATOM   3311 C CE2 . PHE C 2 124 ? 27.811 20.223  133.633 1.00 43.21  ? 121 PHE C CE2 1 
ATOM   3312 C CZ  . PHE C 2 124 ? 27.168 21.226  132.947 1.00 45.50  ? 121 PHE C CZ  1 
ATOM   3313 N N   . LYS C 2 125 ? 28.738 14.698  129.125 1.00 47.65  ? 122 LYS C N   1 
ATOM   3314 C CA  . LYS C 2 125 ? 28.804 13.244  128.974 1.00 52.54  ? 122 LYS C CA  1 
ATOM   3315 C C   . LYS C 2 125 ? 30.019 12.603  129.680 1.00 53.79  ? 122 LYS C C   1 
ATOM   3316 O O   . LYS C 2 125 ? 29.907 11.535  130.240 1.00 60.92  ? 122 LYS C O   1 
ATOM   3317 C CB  . LYS C 2 125 ? 28.813 12.901  127.504 1.00 52.96  ? 122 LYS C CB  1 
ATOM   3318 C CG  . LYS C 2 125 ? 30.098 13.282  126.821 1.00 57.36  ? 122 LYS C CG  1 
ATOM   3319 C CD  . LYS C 2 125 ? 29.977 13.223  125.316 1.00 59.37  ? 122 LYS C CD  1 
ATOM   3320 C CE  . LYS C 2 125 ? 31.356 13.131  124.709 1.00 68.22  ? 122 LYS C CE  1 
ATOM   3321 N NZ  . LYS C 2 125 ? 31.353 13.564  123.289 1.00 77.21  ? 122 LYS C NZ  1 
ATOM   3322 N N   . SER C 2 126 ? 31.150 13.290  129.655 1.00 52.19  ? 123 SER C N   1 
ATOM   3323 C CA  . SER C 2 126 ? 32.333 12.954  130.441 1.00 56.10  ? 123 SER C CA  1 
ATOM   3324 C C   . SER C 2 126 ? 32.306 13.264  131.928 1.00 59.22  ? 123 SER C C   1 
ATOM   3325 O O   . SER C 2 126 ? 33.296 13.008  132.595 1.00 71.71  ? 123 SER C O   1 
ATOM   3326 C CB  . SER C 2 126 ? 33.536 13.695  129.876 1.00 53.27  ? 123 SER C CB  1 
ATOM   3327 O OG  . SER C 2 126 ? 33.558 13.497  128.461 1.00 63.52  ? 123 SER C OG  1 
ATOM   3328 N N   . ILE C 2 127 ? 31.229 13.817  132.470 1.00 51.82  ? 124 ILE C N   1 
ATOM   3329 C CA  . ILE C 2 127 ? 31.222 14.182  133.898 1.00 48.70  ? 124 ILE C CA  1 
ATOM   3330 C C   . ILE C 2 127 ? 30.343 13.149  134.565 1.00 50.62  ? 124 ILE C C   1 
ATOM   3331 O O   . ILE C 2 127 ? 29.222 12.909  134.143 1.00 51.85  ? 124 ILE C O   1 
ATOM   3332 C CB  . ILE C 2 127 ? 30.589 15.592  134.193 1.00 48.56  ? 124 ILE C CB  1 
ATOM   3333 C CG1 . ILE C 2 127 ? 31.215 16.747  133.396 1.00 47.67  ? 124 ILE C CG1 1 
ATOM   3334 C CG2 . ILE C 2 127 ? 30.572 15.888  135.676 1.00 43.00  ? 124 ILE C CG2 1 
ATOM   3335 C CD1 . ILE C 2 127 ? 32.700 16.712  133.334 1.00 56.28  ? 124 ILE C CD1 1 
ATOM   3336 N N   . SER C 2 128 ? 30.809 12.570  135.643 1.00 56.06  ? 125 SER C N   1 
ATOM   3337 C CA  . SER C 2 128 ? 30.085 11.453  136.245 1.00 54.51  ? 125 SER C CA  1 
ATOM   3338 C C   . SER C 2 128 ? 28.916 12.066  136.975 1.00 51.96  ? 125 SER C C   1 
ATOM   3339 O O   . SER C 2 128 ? 28.936 13.256  137.245 1.00 50.64  ? 125 SER C O   1 
ATOM   3340 C CB  . SER C 2 128 ? 31.000 10.684  137.204 1.00 46.83  ? 125 SER C CB  1 
ATOM   3341 O OG  . SER C 2 128 ? 31.094 11.426  138.416 1.00 53.39  ? 125 SER C OG  1 
ATOM   3342 N N   . ASP C 2 129 ? 27.942 11.245  137.361 1.00 58.09  ? 126 ASP C N   1 
ATOM   3343 C CA  . ASP C 2 129 ? 26.751 11.728  138.105 1.00 65.18  ? 126 ASP C CA  1 
ATOM   3344 C C   . ASP C 2 129 ? 27.137 12.153  139.475 1.00 59.66  ? 126 ASP C C   1 
ATOM   3345 O O   . ASP C 2 129 ? 26.346 12.814  140.153 1.00 65.80  ? 126 ASP C O   1 
ATOM   3346 C CB  . ASP C 2 129 ? 25.671 10.616  138.248 1.00 73.05  ? 126 ASP C CB  1 
ATOM   3347 C CG  . ASP C 2 129 ? 25.241 10.010  136.895 1.00 86.17  ? 126 ASP C CG  1 
ATOM   3348 O OD1 . ASP C 2 129 ? 26.093 9.735   136.015 1.00 89.37  ? 126 ASP C OD1 1 
ATOM   3349 O OD2 . ASP C 2 129 ? 24.035 9.779   136.711 1.00 109.11 ? 126 ASP C OD2 1 
ATOM   3350 N N   . GLU C 2 130 ? 28.324 11.675  139.888 1.00 65.38  ? 127 GLU C N   1 
ATOM   3351 C CA  . GLU C 2 130 ? 28.888 11.780  141.241 1.00 69.30  ? 127 GLU C CA  1 
ATOM   3352 C C   . GLU C 2 130 ? 29.575 13.145  141.414 1.00 63.62  ? 127 GLU C C   1 
ATOM   3353 O O   . GLU C 2 130 ? 29.353 13.877  142.400 1.00 60.17  ? 127 GLU C O   1 
ATOM   3354 C CB  . GLU C 2 130 ? 29.978 10.696  141.460 1.00 85.57  ? 127 GLU C CB  1 
ATOM   3355 C CG  . GLU C 2 130 ? 29.679 9.263   141.039 1.00 90.28  ? 127 GLU C CG  1 
ATOM   3356 C CD  . GLU C 2 130 ? 28.633 8.628   141.926 1.00 104.43 ? 127 GLU C CD  1 
ATOM   3357 O OE1 . GLU C 2 130 ? 28.909 7.575   142.536 1.00 122.07 ? 127 GLU C OE1 1 
ATOM   3358 O OE2 . GLU C 2 130 ? 27.527 9.193   142.029 1.00 118.93 ? 127 GLU C OE2 1 
ATOM   3359 N N   . GLU C 2 131 ? 30.420 13.446  140.432 1.00 54.10  ? 128 GLU C N   1 
ATOM   3360 C CA  . GLU C 2 131 ? 31.085 14.749  140.272 1.00 57.25  ? 128 GLU C CA  1 
ATOM   3361 C C   . GLU C 2 131 ? 30.184 15.968  140.247 1.00 56.81  ? 128 GLU C C   1 
ATOM   3362 O O   . GLU C 2 131 ? 30.551 17.026  140.775 1.00 64.41  ? 128 GLU C O   1 
ATOM   3363 C CB  . GLU C 2 131 ? 31.916 14.724  138.991 1.00 57.74  ? 128 GLU C CB  1 
ATOM   3364 C CG  . GLU C 2 131 ? 33.231 13.968  139.157 1.00 61.57  ? 128 GLU C CG  1 
ATOM   3365 C CD  . GLU C 2 131 ? 33.863 13.608  137.850 1.00 59.32  ? 128 GLU C CD  1 
ATOM   3366 O OE1 . GLU C 2 131 ? 33.206 12.956  137.038 1.00 62.13  ? 128 GLU C OE1 1 
ATOM   3367 O OE2 . GLU C 2 131 ? 35.019 14.003  137.620 1.00 63.98  ? 128 GLU C OE2 1 
ATOM   3368 N N   . LEU C 2 132 ? 28.990 15.813  139.686 1.00 55.08  ? 129 LEU C N   1 
ATOM   3369 C CA  . LEU C 2 132 ? 28.129 16.966  139.464 1.00 57.63  ? 129 LEU C CA  1 
ATOM   3370 C C   . LEU C 2 132 ? 27.854 17.764  140.766 1.00 53.95  ? 129 LEU C C   1 
ATOM   3371 O O   . LEU C 2 132 ? 28.101 18.994  140.812 1.00 58.22  ? 129 LEU C O   1 
ATOM   3372 C CB  . LEU C 2 132 ? 26.853 16.534  138.734 1.00 61.12  ? 129 LEU C CB  1 
ATOM   3373 C CG  . LEU C 2 132 ? 26.148 17.393  137.678 1.00 62.27  ? 129 LEU C CG  1 
ATOM   3374 C CD1 . LEU C 2 132 ? 24.914 18.030  138.267 1.00 70.47  ? 129 LEU C CD1 1 
ATOM   3375 C CD2 . LEU C 2 132 ? 27.048 18.445  137.077 1.00 61.93  ? 129 LEU C CD2 1 
ATOM   3376 N N   . PRO C 2 133 ? 27.364 17.097  141.824 1.00 46.97  ? 130 PRO C N   1 
ATOM   3377 C CA  . PRO C 2 133 ? 27.086 17.877  143.032 1.00 45.95  ? 130 PRO C CA  1 
ATOM   3378 C C   . PRO C 2 133 ? 28.336 18.408  143.773 1.00 47.64  ? 130 PRO C C   1 
ATOM   3379 O O   . PRO C 2 133 ? 28.235 19.404  144.516 1.00 48.92  ? 130 PRO C O   1 
ATOM   3380 C CB  . PRO C 2 133 ? 26.229 16.932  143.902 1.00 48.34  ? 130 PRO C CB  1 
ATOM   3381 C CG  . PRO C 2 133 ? 26.256 15.582  143.268 1.00 49.88  ? 130 PRO C CG  1 
ATOM   3382 C CD  . PRO C 2 133 ? 26.624 15.811  141.829 1.00 59.19  ? 130 PRO C CD  1 
ATOM   3383 N N   . LEU C 2 134 ? 29.497 17.821  143.512 1.00 44.31  ? 131 LEU C N   1 
ATOM   3384 C CA  . LEU C 2 134 ? 30.726 18.373  144.072 1.00 53.55  ? 131 LEU C CA  1 
ATOM   3385 C C   . LEU C 2 134 ? 30.959 19.742  143.419 1.00 52.57  ? 131 LEU C C   1 
ATOM   3386 O O   . LEU C 2 134 ? 31.231 20.771  144.132 1.00 45.85  ? 131 LEU C O   1 
ATOM   3387 C CB  . LEU C 2 134 ? 31.946 17.423  143.855 1.00 54.86  ? 131 LEU C CB  1 
ATOM   3388 C CG  . LEU C 2 134 ? 31.627 15.954  144.249 1.00 57.71  ? 131 LEU C CG  1 
ATOM   3389 C CD1 . LEU C 2 134 ? 32.714 14.947  143.868 1.00 61.40  ? 131 LEU C CD1 1 
ATOM   3390 C CD2 . LEU C 2 134 ? 31.276 15.872  145.731 1.00 53.89  ? 131 LEU C CD2 1 
ATOM   3391 N N   . PHE C 2 135 ? 30.827 19.726  142.074 1.00 43.85  ? 132 PHE C N   1 
ATOM   3392 C CA  . PHE C 2 135 ? 31.094 20.872  141.205 1.00 39.54  ? 132 PHE C CA  1 
ATOM   3393 C C   . PHE C 2 135 ? 30.185 22.001  141.579 1.00 41.20  ? 132 PHE C C   1 
ATOM   3394 O O   . PHE C 2 135 ? 30.589 23.115  141.815 1.00 43.29  ? 132 PHE C O   1 
ATOM   3395 C CB  . PHE C 2 135 ? 30.892 20.429  139.762 1.00 44.13  ? 132 PHE C CB  1 
ATOM   3396 C CG  . PHE C 2 135 ? 31.025 21.511  138.753 1.00 41.44  ? 132 PHE C CG  1 
ATOM   3397 C CD1 . PHE C 2 135 ? 32.204 22.193  138.607 1.00 45.70  ? 132 PHE C CD1 1 
ATOM   3398 C CD2 . PHE C 2 135 ? 29.968 21.820  137.926 1.00 44.64  ? 132 PHE C CD2 1 
ATOM   3399 C CE1 . PHE C 2 135 ? 32.320 23.191  137.671 1.00 42.80  ? 132 PHE C CE1 1 
ATOM   3400 C CE2 . PHE C 2 135 ? 30.076 22.801  136.984 1.00 43.62  ? 132 PHE C CE2 1 
ATOM   3401 C CZ  . PHE C 2 135 ? 31.259 23.473  136.847 1.00 45.24  ? 132 PHE C CZ  1 
ATOM   3402 N N   . THR C 2 136 ? 28.936 21.676  141.725 1.00 45.88  ? 133 THR C N   1 
ATOM   3403 C CA  . THR C 2 136 ? 27.947 22.651  142.111 1.00 46.36  ? 133 THR C CA  1 
ATOM   3404 C C   . THR C 2 136 ? 28.164 23.184  143.517 1.00 45.61  ? 133 THR C C   1 
ATOM   3405 O O   . THR C 2 136 ? 27.901 24.367  143.783 1.00 48.78  ? 133 THR C O   1 
ATOM   3406 C CB  . THR C 2 136 ? 26.611 21.924  141.932 1.00 53.58  ? 133 THR C CB  1 
ATOM   3407 O OG1 . THR C 2 136 ? 26.354 21.927  140.529 1.00 54.48  ? 133 THR C OG1 1 
ATOM   3408 C CG2 . THR C 2 136 ? 25.499 22.557  142.682 1.00 55.58  ? 133 THR C CG2 1 
ATOM   3409 N N   . ASP C 2 137 ? 28.653 22.347  144.439 1.00 47.94  ? 134 ASP C N   1 
ATOM   3410 C CA  . ASP C 2 137 ? 28.850 22.828  145.838 1.00 50.36  ? 134 ASP C CA  1 
ATOM   3411 C C   . ASP C 2 137 ? 30.015 23.787  145.899 1.00 42.36  ? 134 ASP C C   1 
ATOM   3412 O O   . ASP C 2 137 ? 29.973 24.755  146.629 1.00 40.86  ? 134 ASP C O   1 
ATOM   3413 C CB  . ASP C 2 137 ? 29.045 21.687  146.871 1.00 54.88  ? 134 ASP C CB  1 
ATOM   3414 C CG  . ASP C 2 137 ? 29.101 22.207  148.348 1.00 62.90  ? 134 ASP C CG  1 
ATOM   3415 O OD1 . ASP C 2 137 ? 28.338 23.120  148.793 1.00 57.24  ? 134 ASP C OD1 1 
ATOM   3416 O OD2 . ASP C 2 137 ? 29.952 21.695  149.087 1.00 74.19  ? 134 ASP C OD2 1 
ATOM   3417 N N   . ILE C 2 138 ? 31.052 23.512  145.120 1.00 40.73  ? 135 ILE C N   1 
ATOM   3418 C CA  . ILE C 2 138 ? 32.154 24.449  144.986 1.00 44.03  ? 135 ILE C CA  1 
ATOM   3419 C C   . ILE C 2 138 ? 31.623 25.770  144.313 1.00 40.80  ? 135 ILE C C   1 
ATOM   3420 O O   . ILE C 2 138 ? 31.867 26.884  144.798 1.00 37.85  ? 135 ILE C O   1 
ATOM   3421 C CB  . ILE C 2 138 ? 33.315 23.794  144.194 1.00 48.76  ? 135 ILE C CB  1 
ATOM   3422 C CG1 . ILE C 2 138 ? 33.867 22.570  144.930 1.00 48.74  ? 135 ILE C CG1 1 
ATOM   3423 C CG2 . ILE C 2 138 ? 34.431 24.794  143.922 1.00 47.68  ? 135 ILE C CG2 1 
ATOM   3424 C CD1 . ILE C 2 138 ? 34.690 21.616  144.066 1.00 49.15  ? 135 ILE C CD1 1 
ATOM   3425 N N   . LEU C 2 139 ? 30.816 25.663  143.266 1.00 36.51  ? 136 LEU C N   1 
ATOM   3426 C CA  . LEU C 2 139 ? 30.314 26.902  142.651 1.00 41.62  ? 136 LEU C CA  1 
ATOM   3427 C C   . LEU C 2 139 ? 29.562 27.786  143.677 1.00 41.77  ? 136 LEU C C   1 
ATOM   3428 O O   . LEU C 2 139 ? 29.767 29.012  143.706 1.00 39.26  ? 136 LEU C O   1 
ATOM   3429 C CB  . LEU C 2 139 ? 29.465 26.609  141.417 1.00 37.78  ? 136 LEU C CB  1 
ATOM   3430 C CG  . LEU C 2 139 ? 30.205 26.100  140.200 1.00 42.55  ? 136 LEU C CG  1 
ATOM   3431 C CD1 . LEU C 2 139 ? 29.204 25.587  139.179 1.00 45.41  ? 136 LEU C CD1 1 
ATOM   3432 C CD2 . LEU C 2 139 ? 31.093 27.150  139.567 1.00 40.62  ? 136 LEU C CD2 1 
ATOM   3433 N N   . ASP C 2 140 ? 28.718 27.156  144.504 1.00 47.58  ? 137 ASP C N   1 
ATOM   3434 C CA  . ASP C 2 140 ? 27.917 27.876  145.555 1.00 53.32  ? 137 ASP C CA  1 
ATOM   3435 C C   . ASP C 2 140 ? 28.857 28.520  146.546 1.00 52.11  ? 137 ASP C C   1 
ATOM   3436 O O   . ASP C 2 140 ? 28.613 29.627  146.977 1.00 56.62  ? 137 ASP C O   1 
ATOM   3437 C CB  . ASP C 2 140 ? 26.931 26.968  146.333 1.00 55.93  ? 137 ASP C CB  1 
ATOM   3438 C CG  . ASP C 2 140 ? 25.810 26.337  145.426 1.00 64.21  ? 137 ASP C CG  1 
ATOM   3439 O OD1 . ASP C 2 140 ? 25.438 26.924  144.393 1.00 68.17  ? 137 ASP C OD1 1 
ATOM   3440 O OD2 . ASP C 2 140 ? 25.264 25.260  145.753 1.00 65.36  ? 137 ASP C OD2 1 
ATOM   3441 N N   . ARG C 2 141 ? 29.973 27.877  146.861 1.00 50.83  ? 138 ARG C N   1 
ATOM   3442 C CA  . ARG C 2 141 ? 30.937 28.491  147.811 1.00 53.53  ? 138 ARG C CA  1 
ATOM   3443 C C   . ARG C 2 141 ? 31.859 29.561  147.249 1.00 48.75  ? 138 ARG C C   1 
ATOM   3444 O O   . ARG C 2 141 ? 32.357 30.386  147.996 1.00 54.39  ? 138 ARG C O   1 
ATOM   3445 C CB  . ARG C 2 141 ? 31.768 27.412  148.533 1.00 51.13  ? 138 ARG C CB  1 
ATOM   3446 C CG  . ARG C 2 141 ? 30.856 26.449  149.298 1.00 54.91  ? 138 ARG C CG  1 
ATOM   3447 C CD  . ARG C 2 141 ? 31.515 25.550  150.324 1.00 51.20  ? 138 ARG C CD  1 
ATOM   3448 N NE  . ARG C 2 141 ? 32.795 24.882  149.981 1.00 45.10  ? 138 ARG C NE  1 
ATOM   3449 C CZ  . ARG C 2 141 ? 32.875 23.834  149.223 1.00 47.27  ? 138 ARG C CZ  1 
ATOM   3450 N NH1 . ARG C 2 141 ? 31.789 23.375  148.635 1.00 55.42  ? 138 ARG C NH1 1 
ATOM   3451 N NH2 . ARG C 2 141 ? 34.029 23.268  149.030 1.00 50.34  ? 138 ARG C NH2 1 
ATOM   3452 N N   . ILE C 2 142 ? 32.091 29.574  145.950 1.00 50.40  ? 139 ILE C N   1 
ATOM   3453 C CA  . ILE C 2 142 ? 32.810 30.698  145.338 1.00 48.84  ? 139 ILE C CA  1 
ATOM   3454 C C   . ILE C 2 142 ? 32.046 32.040  145.409 1.00 44.90  ? 139 ILE C C   1 
ATOM   3455 O O   . ILE C 2 142 ? 30.882 32.112  145.128 1.00 54.32  ? 139 ILE C O   1 
ATOM   3456 C CB  . ILE C 2 142 ? 33.217 30.354  143.905 1.00 51.00  ? 139 ILE C CB  1 
ATOM   3457 C CG1 . ILE C 2 142 ? 34.288 29.275  143.990 1.00 54.30  ? 139 ILE C CG1 1 
ATOM   3458 C CG2 . ILE C 2 142 ? 33.777 31.577  143.187 1.00 54.12  ? 139 ILE C CG2 1 
ATOM   3459 C CD1 . ILE C 2 142 ? 34.569 28.577  142.696 1.00 51.66  ? 139 ILE C CD1 1 
ATOM   3460 N N   . GLY C 2 143 ? 32.743 33.090  145.803 1.00 56.79  ? 140 GLY C N   1 
ATOM   3461 C CA  . GLY C 2 143 ? 32.146 34.347  146.233 1.00 58.70  ? 140 GLY C CA  1 
ATOM   3462 C C   . GLY C 2 143 ? 32.363 34.510  147.721 1.00 56.02  ? 140 GLY C C   1 
ATOM   3463 O O   . GLY C 2 143 ? 31.922 35.502  148.282 1.00 74.18  ? 140 GLY C O   1 
ATOM   3464 N N   . LYS D 2 5   ? 22.292 11.593  134.942 1.00 114.84 ? 2   LYS D N   1 
ATOM   3465 C CA  . LYS D 2 5   ? 21.850 13.015  134.947 1.00 102.07 ? 2   LYS D CA  1 
ATOM   3466 C C   . LYS D 2 5   ? 20.381 13.116  134.556 1.00 99.72  ? 2   LYS D C   1 
ATOM   3467 O O   . LYS D 2 5   ? 19.683 12.122  134.316 1.00 107.52 ? 2   LYS D O   1 
ATOM   3468 C CB  . LYS D 2 5   ? 22.637 13.869  133.947 1.00 92.90  ? 2   LYS D CB  1 
ATOM   3469 C CG  . LYS D 2 5   ? 24.003 13.378  133.513 1.00 86.34  ? 2   LYS D CG  1 
ATOM   3470 C CD  . LYS D 2 5   ? 25.080 13.575  134.572 1.00 82.26  ? 2   LYS D CD  1 
ATOM   3471 C CE  . LYS D 2 5   ? 26.434 13.699  133.892 1.00 75.90  ? 2   LYS D CE  1 
ATOM   3472 N NZ  . LYS D 2 5   ? 26.603 12.762  132.733 1.00 69.88  ? 2   LYS D NZ  1 
ATOM   3473 N N   . ASP D 2 6   ? 19.942 14.352  134.459 1.00 76.43  ? 3   ASP D N   1 
ATOM   3474 C CA  . ASP D 2 6   ? 18.585 14.667  134.175 1.00 63.39  ? 3   ASP D CA  1 
ATOM   3475 C C   . ASP D 2 6   ? 18.698 16.119  133.749 1.00 57.23  ? 3   ASP D C   1 
ATOM   3476 O O   . ASP D 2 6   ? 19.609 16.836  134.146 1.00 57.30  ? 3   ASP D O   1 
ATOM   3477 C CB  . ASP D 2 6   ? 17.727 14.427  135.420 1.00 66.69  ? 3   ASP D CB  1 
ATOM   3478 C CG  . ASP D 2 6   ? 16.802 15.565  135.723 1.00 80.03  ? 3   ASP D CG  1 
ATOM   3479 O OD1 . ASP D 2 6   ? 15.739 15.718  135.055 1.00 98.41  ? 3   ASP D OD1 1 
ATOM   3480 O OD2 . ASP D 2 6   ? 17.148 16.333  136.640 1.00 73.59  ? 3   ASP D OD2 1 
ATOM   3481 N N   . PHE D 2 7   ? 17.833 16.543  132.858 1.00 50.68  ? 4   PHE D N   1 
ATOM   3482 C CA  . PHE D 2 7   ? 18.037 17.804  132.260 1.00 42.52  ? 4   PHE D CA  1 
ATOM   3483 C C   . PHE D 2 7   ? 18.017 18.905  133.334 1.00 41.82  ? 4   PHE D C   1 
ATOM   3484 O O   . PHE D 2 7   ? 18.880 19.757  133.386 1.00 41.94  ? 4   PHE D O   1 
ATOM   3485 C CB  . PHE D 2 7   ? 16.993 18.064  131.201 1.00 41.29  ? 4   PHE D CB  1 
ATOM   3486 C CG  . PHE D 2 7   ? 17.193 19.362  130.508 1.00 40.86  ? 4   PHE D CG  1 
ATOM   3487 C CD1 . PHE D 2 7   ? 18.461 19.763  130.137 1.00 35.49  ? 4   PHE D CD1 1 
ATOM   3488 C CD2 . PHE D 2 7   ? 16.146 20.170  130.245 1.00 43.66  ? 4   PHE D CD2 1 
ATOM   3489 C CE1 . PHE D 2 7   ? 18.678 20.972  129.527 1.00 41.40  ? 4   PHE D CE1 1 
ATOM   3490 C CE2 . PHE D 2 7   ? 16.337 21.389  129.600 1.00 47.42  ? 4   PHE D CE2 1 
ATOM   3491 C CZ  . PHE D 2 7   ? 17.609 21.801  129.252 1.00 44.22  ? 4   PHE D CZ  1 
ATOM   3492 N N   . GLU D 2 8   ? 17.081 18.850  134.249 1.00 45.48  ? 5   GLU D N   1 
ATOM   3493 C CA  . GLU D 2 8   ? 17.012 19.873  135.264 1.00 49.59  ? 5   GLU D CA  1 
ATOM   3494 C C   . GLU D 2 8   ? 18.335 20.047  136.020 1.00 49.73  ? 5   GLU D C   1 
ATOM   3495 O O   . GLU D 2 8   ? 18.702 21.162  136.389 1.00 50.74  ? 5   GLU D O   1 
ATOM   3496 C CB  . GLU D 2 8   ? 15.879 19.576  136.237 1.00 54.91  ? 5   GLU D CB  1 
ATOM   3497 C CG  . GLU D 2 8   ? 15.613 20.727  137.182 1.00 70.24  ? 5   GLU D CG  1 
ATOM   3498 C CD  . GLU D 2 8   ? 15.389 22.030  136.419 1.00 85.32  ? 5   GLU D CD  1 
ATOM   3499 O OE1 . GLU D 2 8   ? 14.800 21.951  135.292 1.00 89.85  ? 5   GLU D OE1 1 
ATOM   3500 O OE2 . GLU D 2 8   ? 15.816 23.102  136.932 1.00 79.09  ? 5   GLU D OE2 1 
ATOM   3501 N N   . LYS D 2 9   ? 19.060 18.964  136.246 1.00 46.82  ? 6   LYS D N   1 
ATOM   3502 C CA  . LYS D 2 9   ? 20.270 19.081  137.057 1.00 55.51  ? 6   LYS D CA  1 
ATOM   3503 C C   . LYS D 2 9   ? 21.396 19.622  136.228 1.00 45.52  ? 6   LYS D C   1 
ATOM   3504 O O   . LYS D 2 9   ? 22.193 20.380  136.712 1.00 42.87  ? 6   LYS D O   1 
ATOM   3505 C CB  . LYS D 2 9   ? 20.671 17.755  137.757 1.00 64.34  ? 6   LYS D CB  1 
ATOM   3506 C CG  . LYS D 2 9   ? 19.593 17.282  138.733 1.00 77.08  ? 6   LYS D CG  1 
ATOM   3507 C CD  . LYS D 2 9   ? 20.084 16.524  139.953 1.00 88.92  ? 6   LYS D CD  1 
ATOM   3508 C CE  . LYS D 2 9   ? 18.906 16.200  140.879 1.00 92.48  ? 6   LYS D CE  1 
ATOM   3509 N NZ  . LYS D 2 9   ? 19.172 14.961  141.669 1.00 91.15  ? 6   LYS D NZ  1 
ATOM   3510 N N   . LEU D 2 10  ? 21.427 19.271  134.963 1.00 40.15  ? 7   LEU D N   1 
ATOM   3511 C CA  . LEU D 2 10  ? 22.447 19.792  134.129 1.00 39.37  ? 7   LEU D CA  1 
ATOM   3512 C C   . LEU D 2 10  ? 22.175 21.247  133.911 1.00 41.32  ? 7   LEU D C   1 
ATOM   3513 O O   . LEU D 2 10  ? 23.129 22.036  133.891 1.00 41.51  ? 7   LEU D O   1 
ATOM   3514 C CB  . LEU D 2 10  ? 22.489 19.067  132.814 1.00 39.98  ? 7   LEU D CB  1 
ATOM   3515 C CG  . LEU D 2 10  ? 22.779 17.585  133.017 1.00 41.42  ? 7   LEU D CG  1 
ATOM   3516 C CD1 . LEU D 2 10  ? 22.934 16.861  131.670 1.00 38.60  ? 7   LEU D CD1 1 
ATOM   3517 C CD2 . LEU D 2 10  ? 24.034 17.417  133.881 1.00 44.41  ? 7   LEU D CD2 1 
ATOM   3518 N N   . TYR D 2 11  ? 20.888 21.607  133.776 1.00 40.88  ? 8   TYR D N   1 
ATOM   3519 C CA  . TYR D 2 11  ? 20.529 22.992  133.508 1.00 38.21  ? 8   TYR D CA  1 
ATOM   3520 C C   . TYR D 2 11  ? 20.843 23.875  134.710 1.00 37.97  ? 8   TYR D C   1 
ATOM   3521 O O   . TYR D 2 11  ? 21.317 24.967  134.552 1.00 37.13  ? 8   TYR D O   1 
ATOM   3522 C CB  . TYR D 2 11  ? 19.055 23.178  133.089 1.00 38.89  ? 8   TYR D CB  1 
ATOM   3523 C CG  . TYR D 2 11  ? 18.733 24.644  132.781 1.00 35.92  ? 8   TYR D CG  1 
ATOM   3524 C CD1 . TYR D 2 11  ? 19.138 25.219  131.589 1.00 35.60  ? 8   TYR D CD1 1 
ATOM   3525 C CD2 . TYR D 2 11  ? 18.167 25.496  133.765 1.00 39.23  ? 8   TYR D CD2 1 
ATOM   3526 C CE1 . TYR D 2 11  ? 18.909 26.575  131.323 1.00 43.06  ? 8   TYR D CE1 1 
ATOM   3527 C CE2 . TYR D 2 11  ? 17.936 26.871  133.502 1.00 40.96  ? 8   TYR D CE2 1 
ATOM   3528 C CZ  . TYR D 2 11  ? 18.290 27.383  132.273 1.00 43.40  ? 8   TYR D CZ  1 
ATOM   3529 O OH  . TYR D 2 11  ? 18.085 28.707  132.003 1.00 56.56  ? 8   TYR D OH  1 
ATOM   3530 N N   . GLU D 2 12  ? 20.561 23.392  135.905 1.00 45.48  ? 9   GLU D N   1 
ATOM   3531 C CA  . GLU D 2 12  ? 20.878 24.092  137.136 1.00 48.23  ? 9   GLU D CA  1 
ATOM   3532 C C   . GLU D 2 12  ? 22.438 24.243  137.281 1.00 46.03  ? 9   GLU D C   1 
ATOM   3533 O O   . GLU D 2 12  ? 22.982 25.285  137.661 1.00 40.54  ? 9   GLU D O   1 
ATOM   3534 C CB  . GLU D 2 12  ? 20.227 23.310  138.281 1.00 57.09  ? 9   GLU D CB  1 
ATOM   3535 C CG  . GLU D 2 12  ? 20.295 23.977  139.653 1.00 79.72  ? 9   GLU D CG  1 
ATOM   3536 C CD  . GLU D 2 12  ? 20.074 23.010  140.832 1.00 84.77  ? 9   GLU D CD  1 
ATOM   3537 O OE1 . GLU D 2 12  ? 19.656 23.496  141.904 1.00 89.70  ? 9   GLU D OE1 1 
ATOM   3538 O OE2 . GLU D 2 12  ? 20.331 21.788  140.717 1.00 71.87  ? 9   GLU D OE2 1 
ATOM   3539 N N   . ALA D 2 13  ? 23.183 23.238  136.875 1.00 43.62  ? 10  ALA D N   1 
ATOM   3540 C CA  . ALA D 2 13  ? 24.608 23.315  137.066 1.00 40.14  ? 10  ALA D CA  1 
ATOM   3541 C C   . ALA D 2 13  ? 25.169 24.371  136.119 1.00 42.89  ? 10  ALA D C   1 
ATOM   3542 O O   . ALA D 2 13  ? 26.048 25.156  136.500 1.00 35.54  ? 10  ALA D O   1 
ATOM   3543 C CB  . ALA D 2 13  ? 25.198 21.956  136.809 1.00 39.79  ? 10  ALA D CB  1 
ATOM   3544 N N   . THR D 2 14  ? 24.635 24.390  134.892 1.00 37.72  ? 11  THR D N   1 
ATOM   3545 C CA  . THR D 2 14  ? 25.055 25.338  133.888 1.00 39.49  ? 11  THR D CA  1 
ATOM   3546 C C   . THR D 2 14  ? 24.736 26.763  134.322 1.00 39.99  ? 11  THR D C   1 
ATOM   3547 O O   . THR D 2 14  ? 25.505 27.686  134.132 1.00 40.08  ? 11  THR D O   1 
ATOM   3548 C CB  . THR D 2 14  ? 24.353 25.063  132.561 1.00 39.67  ? 11  THR D CB  1 
ATOM   3549 O OG1 . THR D 2 14  ? 24.718 23.771  132.110 1.00 34.10  ? 11  THR D OG1 1 
ATOM   3550 C CG2 . THR D 2 14  ? 24.759 26.073  131.507 1.00 42.51  ? 11  THR D CG2 1 
ATOM   3551 N N   . THR D 2 15  ? 23.593 26.916  134.935 1.00 42.21  ? 12  THR D N   1 
ATOM   3552 C CA  . THR D 2 15  ? 23.145 28.198  135.438 1.00 44.29  ? 12  THR D CA  1 
ATOM   3553 C C   . THR D 2 15  ? 24.056 28.694  136.539 1.00 39.77  ? 12  THR D C   1 
ATOM   3554 O O   . THR D 2 15  ? 24.361 29.899  136.613 1.00 39.57  ? 12  THR D O   1 
ATOM   3555 C CB  . THR D 2 15  ? 21.677 28.102  135.983 1.00 47.09  ? 12  THR D CB  1 
ATOM   3556 O OG1 . THR D 2 15  ? 20.780 28.074  134.885 1.00 50.57  ? 12  THR D OG1 1 
ATOM   3557 C CG2 . THR D 2 15  ? 21.306 29.321  136.738 1.00 54.23  ? 12  THR D CG2 1 
ATOM   3558 N N   . LYS D 2 16  ? 24.421 27.796  137.447 1.00 36.08  ? 13  LYS D N   1 
ATOM   3559 C CA  . LYS D 2 16  ? 25.275 28.187  138.551 1.00 39.59  ? 13  LYS D CA  1 
ATOM   3560 C C   . LYS D 2 16  ? 26.663 28.597  137.997 1.00 41.12  ? 13  LYS D C   1 
ATOM   3561 O O   . LYS D 2 16  ? 27.271 29.555  138.469 1.00 44.03  ? 13  LYS D O   1 
ATOM   3562 C CB  . LYS D 2 16  ? 25.496 27.050  139.551 1.00 47.09  ? 13  LYS D CB  1 
ATOM   3563 C CG  . LYS D 2 16  ? 24.304 26.504  140.271 1.00 50.09  ? 13  LYS D CG  1 
ATOM   3564 C CD  . LYS D 2 16  ? 24.307 27.009  141.697 1.00 72.33  ? 13  LYS D CD  1 
ATOM   3565 C CE  . LYS D 2 16  ? 23.135 26.454  142.517 1.00 70.07  ? 13  LYS D CE  1 
ATOM   3566 N NZ  . LYS D 2 16  ? 23.448 25.036  142.704 1.00 68.20  ? 13  LYS D NZ  1 
ATOM   3567 N N   . LEU D 2 17  ? 27.156 27.842  137.023 1.00 35.52  ? 14  LEU D N   1 
ATOM   3568 C CA  . LEU D 2 17  ? 28.411 28.152  136.367 1.00 38.66  ? 14  LEU D CA  1 
ATOM   3569 C C   . LEU D 2 17  ? 28.415 29.586  135.839 1.00 37.99  ? 14  LEU D C   1 
ATOM   3570 O O   . LEU D 2 17  ? 29.257 30.370  136.205 1.00 36.83  ? 14  LEU D O   1 
ATOM   3571 C CB  . LEU D 2 17  ? 28.645 27.150  135.220 1.00 42.04  ? 14  LEU D CB  1 
ATOM   3572 C CG  . LEU D 2 17  ? 29.729 27.386  134.179 1.00 41.56  ? 14  LEU D CG  1 
ATOM   3573 C CD1 . LEU D 2 17  ? 30.996 27.650  134.883 1.00 45.70  ? 14  LEU D CD1 1 
ATOM   3574 C CD2 . LEU D 2 17  ? 29.954 26.190  133.300 1.00 45.81  ? 14  LEU D CD2 1 
ATOM   3575 N N   . VAL D 2 18  ? 27.478 29.904  134.958 1.00 39.88  ? 15  VAL D N   1 
ATOM   3576 C CA  . VAL D 2 18  ? 27.343 31.244  134.434 1.00 38.23  ? 15  VAL D CA  1 
ATOM   3577 C C   . VAL D 2 18  ? 27.138 32.282  135.509 1.00 36.61  ? 15  VAL D C   1 
ATOM   3578 O O   . VAL D 2 18  ? 27.806 33.284  135.485 1.00 37.90  ? 15  VAL D O   1 
ATOM   3579 C CB  . VAL D 2 18  ? 26.219 31.332  133.386 1.00 41.07  ? 15  VAL D CB  1 
ATOM   3580 C CG1 . VAL D 2 18  ? 25.892 32.767  133.041 1.00 39.08  ? 15  VAL D CG1 1 
ATOM   3581 C CG2 . VAL D 2 18  ? 26.688 30.657  132.114 1.00 43.82  ? 15  VAL D CG2 1 
ATOM   3582 N N   . SER D 2 19  ? 26.260 32.091  136.472 1.00 34.79  ? 16  SER D N   1 
ATOM   3583 C CA  . SER D 2 19  ? 26.118 33.177  137.436 1.00 36.47  ? 16  SER D CA  1 
ATOM   3584 C C   . SER D 2 19  ? 27.380 33.368  138.296 1.00 35.34  ? 16  SER D C   1 
ATOM   3585 O O   . SER D 2 19  ? 27.723 34.470  138.625 1.00 41.70  ? 16  SER D O   1 
ATOM   3586 C CB  . SER D 2 19  ? 24.904 33.005  138.313 1.00 36.06  ? 16  SER D CB  1 
ATOM   3587 O OG  . SER D 2 19  ? 25.009 31.827  139.026 1.00 46.95  ? 16  SER D OG  1 
ATOM   3588 N N   . THR D 2 20  ? 28.060 32.296  138.649 1.00 32.59  ? 17  THR D N   1 
ATOM   3589 C CA  . THR D 2 20  ? 29.309 32.375  139.390 1.00 37.98  ? 17  THR D CA  1 
ATOM   3590 C C   . THR D 2 20  ? 30.422 33.133  138.595 1.00 38.43  ? 17  THR D C   1 
ATOM   3591 O O   . THR D 2 20  ? 31.128 34.002  139.097 1.00 35.45  ? 17  THR D O   1 
ATOM   3592 C CB  . THR D 2 20  ? 29.770 30.946  139.785 1.00 41.15  ? 17  THR D CB  1 
ATOM   3593 O OG1 . THR D 2 20  ? 28.745 30.317  140.592 1.00 42.43  ? 17  THR D OG1 1 
ATOM   3594 C CG2 . THR D 2 20  ? 31.028 31.012  140.579 1.00 39.03  ? 17  THR D CG2 1 
ATOM   3595 N N   . SER D 2 21  ? 30.518 32.829  137.329 1.00 34.58  ? 18  SER D N   1 
ATOM   3596 C CA  . SER D 2 21  ? 31.375 33.569  136.456 1.00 35.73  ? 18  SER D CA  1 
ATOM   3597 C C   . SER D 2 21  ? 31.081 35.063  136.447 1.00 36.43  ? 18  SER D C   1 
ATOM   3598 O O   . SER D 2 21  ? 31.995 35.872  136.529 1.00 35.55  ? 18  SER D O   1 
ATOM   3599 C CB  . SER D 2 21  ? 31.218 33.047  135.038 1.00 35.65  ? 18  SER D CB  1 
ATOM   3600 O OG  . SER D 2 21  ? 32.102 33.701  134.186 1.00 34.85  ? 18  SER D OG  1 
ATOM   3601 N N   . LEU D 2 22  ? 29.816 35.430  136.330 1.00 37.64  ? 19  LEU D N   1 
ATOM   3602 C CA  . LEU D 2 22  ? 29.476 36.815  136.325 1.00 38.64  ? 19  LEU D CA  1 
ATOM   3603 C C   . LEU D 2 22  ? 29.787 37.492  137.668 1.00 43.03  ? 19  LEU D C   1 
ATOM   3604 O O   . LEU D 2 22  ? 30.255 38.609  137.661 1.00 45.66  ? 19  LEU D O   1 
ATOM   3605 C CB  . LEU D 2 22  ? 28.024 37.020  135.938 1.00 45.96  ? 19  LEU D CB  1 
ATOM   3606 C CG  . LEU D 2 22  ? 27.823 36.785  134.426 1.00 53.47  ? 19  LEU D CG  1 
ATOM   3607 C CD1 . LEU D 2 22  ? 26.366 36.503  134.065 1.00 58.79  ? 19  LEU D CD1 1 
ATOM   3608 C CD2 . LEU D 2 22  ? 28.326 37.973  133.622 1.00 51.99  ? 19  LEU D CD2 1 
ATOM   3609 N N   . LYS D 2 23  ? 29.598 36.808  138.802 1.00 42.82  ? 20  LYS D N   1 
ATOM   3610 C CA  . LYS D 2 23  ? 29.795 37.413  140.098 1.00 43.07  ? 20  LYS D CA  1 
ATOM   3611 C C   . LYS D 2 23  ? 31.297 37.615  140.315 1.00 45.78  ? 20  LYS D C   1 
ATOM   3612 O O   . LYS D 2 23  ? 31.768 38.618  140.824 1.00 46.85  ? 20  LYS D O   1 
ATOM   3613 C CB  . LYS D 2 23  ? 29.197 36.501  141.153 1.00 49.38  ? 20  LYS D CB  1 
ATOM   3614 C CG  . LYS D 2 23  ? 29.143 37.117  142.543 1.00 57.20  ? 20  LYS D CG  1 
ATOM   3615 C CD  . LYS D 2 23  ? 29.003 36.038  143.634 1.00 69.79  ? 20  LYS D CD  1 
ATOM   3616 C CE  . LYS D 2 23  ? 29.488 36.481  145.030 1.00 75.46  ? 20  LYS D CE  1 
ATOM   3617 N NZ  . LYS D 2 23  ? 28.885 37.771  145.467 1.00 73.07  ? 20  LYS D NZ  1 
ATOM   3618 N N   . VAL D 2 24  ? 32.075 36.666  139.863 1.00 40.65  ? 21  VAL D N   1 
ATOM   3619 C CA  . VAL D 2 24  ? 33.476 36.783  140.041 1.00 39.12  ? 21  VAL D CA  1 
ATOM   3620 C C   . VAL D 2 24  ? 34.038 37.923  139.232 1.00 38.74  ? 21  VAL D C   1 
ATOM   3621 O O   . VAL D 2 24  ? 34.860 38.641  139.723 1.00 41.62  ? 21  VAL D O   1 
ATOM   3622 C CB  . VAL D 2 24  ? 34.141 35.440  139.758 1.00 39.53  ? 21  VAL D CB  1 
ATOM   3623 C CG1 . VAL D 2 24  ? 35.608 35.583  139.519 1.00 43.75  ? 21  VAL D CG1 1 
ATOM   3624 C CG2 . VAL D 2 24  ? 33.880 34.523  140.947 1.00 39.37  ? 21  VAL D CG2 1 
ATOM   3625 N N   . LYS D 2 25  ? 33.601 38.107  137.997 1.00 41.57  ? 22  LYS D N   1 
ATOM   3626 C CA  . LYS D 2 25  ? 34.154 39.184  137.185 1.00 40.38  ? 22  LYS D CA  1 
ATOM   3627 C C   . LYS D 2 25  ? 33.731 40.506  137.756 1.00 40.55  ? 22  LYS D C   1 
ATOM   3628 O O   . LYS D 2 25  ? 34.483 41.445  137.814 1.00 46.60  ? 22  LYS D O   1 
ATOM   3629 C CB  . LYS D 2 25  ? 33.695 39.080  135.737 1.00 40.79  ? 22  LYS D CB  1 
ATOM   3630 C CG  . LYS D 2 25  ? 34.258 37.878  135.007 1.00 47.78  ? 22  LYS D CG  1 
ATOM   3631 C CD  . LYS D 2 25  ? 33.932 37.880  133.502 1.00 53.68  ? 22  LYS D CD  1 
ATOM   3632 C CE  . LYS D 2 25  ? 32.796 36.921  133.192 1.00 62.20  ? 22  LYS D CE  1 
ATOM   3633 N NZ  . LYS D 2 25  ? 31.837 37.391  132.161 1.00 71.65  ? 22  LYS D NZ  1 
ATOM   3634 N N   . ASP D 2 26  ? 32.495 40.576  138.182 1.00 43.61  ? 23  ASP D N   1 
ATOM   3635 C CA  . ASP D 2 26  ? 31.897 41.817  138.568 1.00 46.94  ? 23  ASP D CA  1 
ATOM   3636 C C   . ASP D 2 26  ? 32.408 42.262  139.931 1.00 47.71  ? 23  ASP D C   1 
ATOM   3637 O O   . ASP D 2 26  ? 32.678 43.461  140.162 1.00 49.02  ? 23  ASP D O   1 
ATOM   3638 C CB  . ASP D 2 26  ? 30.365 41.668  138.563 1.00 55.58  ? 23  ASP D CB  1 
ATOM   3639 C CG  . ASP D 2 26  ? 29.658 42.978  138.806 1.00 66.17  ? 23  ASP D CG  1 
ATOM   3640 O OD1 . ASP D 2 26  ? 29.633 43.824  137.874 1.00 74.41  ? 23  ASP D OD1 1 
ATOM   3641 O OD2 . ASP D 2 26  ? 29.158 43.162  139.943 1.00 64.59  ? 23  ASP D OD2 1 
ATOM   3642 N N   . ASP D 2 27  ? 32.537 41.319  140.843 1.00 40.45  ? 24  ASP D N   1 
ATOM   3643 C CA  . ASP D 2 27  ? 33.196 41.640  142.090 1.00 40.89  ? 24  ASP D CA  1 
ATOM   3644 C C   . ASP D 2 27  ? 34.631 42.139  141.922 1.00 42.13  ? 24  ASP D C   1 
ATOM   3645 O O   . ASP D 2 27  ? 35.013 43.024  142.666 1.00 47.63  ? 24  ASP D O   1 
ATOM   3646 C CB  . ASP D 2 27  ? 33.185 40.458  143.066 1.00 40.13  ? 24  ASP D CB  1 
ATOM   3647 C CG  . ASP D 2 27  ? 31.802 40.194  143.643 1.00 45.36  ? 24  ASP D CG  1 
ATOM   3648 O OD1 . ASP D 2 27  ? 30.856 41.023  143.371 1.00 47.61  ? 24  ASP D OD1 1 
ATOM   3649 O OD2 . ASP D 2 27  ? 31.670 39.136  144.325 1.00 47.87  ? 24  ASP D OD2 1 
ATOM   3650 N N   . LEU D 2 28  ? 35.417 41.612  140.971 1.00 37.74  ? 25  LEU D N   1 
ATOM   3651 C CA  . LEU D 2 28  ? 36.800 42.047  140.848 1.00 35.16  ? 25  LEU D CA  1 
ATOM   3652 C C   . LEU D 2 28  ? 36.783 43.449  140.269 1.00 36.42  ? 25  LEU D C   1 
ATOM   3653 O O   . LEU D 2 28  ? 37.640 44.292  140.576 1.00 37.85  ? 25  LEU D O   1 
ATOM   3654 C CB  . LEU D 2 28  ? 37.623 41.111  139.986 1.00 34.93  ? 25  LEU D CB  1 
ATOM   3655 C CG  . LEU D 2 28  ? 39.051 41.484  139.554 1.00 39.95  ? 25  LEU D CG  1 
ATOM   3656 C CD1 . LEU D 2 28  ? 39.896 41.867  140.750 1.00 45.03  ? 25  LEU D CD1 1 
ATOM   3657 C CD2 . LEU D 2 28  ? 39.758 40.340  138.854 1.00 41.11  ? 25  LEU D CD2 1 
ATOM   3658 N N   . LYS D 2 29  ? 35.801 43.725  139.443 1.00 37.15  ? 26  LYS D N   1 
ATOM   3659 C CA  . LYS D 2 29  ? 35.708 45.041  138.885 1.00 44.25  ? 26  LYS D CA  1 
ATOM   3660 C C   . LYS D 2 29  ? 35.451 46.027  140.036 1.00 45.70  ? 26  LYS D C   1 
ATOM   3661 O O   . LYS D 2 29  ? 36.170 46.995  140.149 1.00 46.78  ? 26  LYS D O   1 
ATOM   3662 C CB  . LYS D 2 29  ? 34.591 45.098  137.882 1.00 51.42  ? 26  LYS D CB  1 
ATOM   3663 C CG  . LYS D 2 29  ? 34.451 46.433  137.176 1.00 55.18  ? 26  LYS D CG  1 
ATOM   3664 C CD  . LYS D 2 29  ? 32.984 46.692  136.850 1.00 62.40  ? 26  LYS D CD  1 
ATOM   3665 C CE  . LYS D 2 29  ? 32.585 46.067  135.539 1.00 71.95  ? 26  LYS D CE  1 
ATOM   3666 N NZ  . LYS D 2 29  ? 31.690 46.998  134.791 1.00 80.23  ? 26  LYS D NZ  1 
ATOM   3667 N N   . LYS D 2 30  ? 34.460 45.739  140.885 1.00 45.90  ? 27  LYS D N   1 
ATOM   3668 C CA  . LYS D 2 30  ? 34.150 46.550  142.074 1.00 51.65  ? 27  LYS D CA  1 
ATOM   3669 C C   . LYS D 2 30  ? 35.384 46.727  142.963 1.00 50.67  ? 27  LYS D C   1 
ATOM   3670 O O   . LYS D 2 30  ? 35.665 47.797  143.467 1.00 47.81  ? 27  LYS D O   1 
ATOM   3671 C CB  . LYS D 2 30  ? 33.046 45.928  142.909 1.00 53.21  ? 27  LYS D CB  1 
ATOM   3672 C CG  . LYS D 2 30  ? 31.649 46.010  142.280 1.00 64.59  ? 27  LYS D CG  1 
ATOM   3673 C CD  . LYS D 2 30  ? 30.621 45.547  143.307 1.00 73.36  ? 27  LYS D CD  1 
ATOM   3674 C CE  . LYS D 2 30  ? 29.561 44.613  142.748 1.00 80.25  ? 27  LYS D CE  1 
ATOM   3675 N NZ  . LYS D 2 30  ? 28.706 45.288  141.741 1.00 85.96  ? 27  LYS D NZ  1 
ATOM   3676 N N   . MET D 2 31  ? 36.160 45.688  143.127 1.00 43.33  ? 28  MET D N   1 
ATOM   3677 C CA  . MET D 2 31  ? 37.257 45.862  143.958 1.00 43.42  ? 28  MET D CA  1 
ATOM   3678 C C   . MET D 2 31  ? 38.291 46.757  143.305 1.00 46.97  ? 28  MET D C   1 
ATOM   3679 O O   . MET D 2 31  ? 38.794 47.649  143.956 1.00 49.19  ? 28  MET D O   1 
ATOM   3680 C CB  . MET D 2 31  ? 37.804 44.537  144.350 1.00 50.47  ? 28  MET D CB  1 
ATOM   3681 C CG  . MET D 2 31  ? 38.904 44.694  145.356 1.00 58.10  ? 28  MET D CG  1 
ATOM   3682 S SD  . MET D 2 31  ? 38.976 43.298  146.467 1.00 70.91  ? 28  MET D SD  1 
ATOM   3683 C CE  . MET D 2 31  ? 40.675 43.538  147.039 1.00 61.78  ? 28  MET D CE  1 
ATOM   3684 N N   . PHE D 2 32  ? 38.581 46.595  142.016 1.00 49.37  ? 29  PHE D N   1 
ATOM   3685 C CA  . PHE D 2 32  ? 39.441 47.577  141.360 1.00 48.28  ? 29  PHE D CA  1 
ATOM   3686 C C   . PHE D 2 32  ? 38.883 49.023  141.499 1.00 48.43  ? 29  PHE D C   1 
ATOM   3687 O O   . PHE D 2 32  ? 39.645 49.951  141.622 1.00 47.97  ? 29  PHE D O   1 
ATOM   3688 C CB  . PHE D 2 32  ? 39.602 47.312  139.868 1.00 44.61  ? 29  PHE D CB  1 
ATOM   3689 C CG  . PHE D 2 32  ? 40.483 46.157  139.520 1.00 45.65  ? 29  PHE D CG  1 
ATOM   3690 C CD1 . PHE D 2 32  ? 41.732 46.042  140.024 1.00 43.80  ? 29  PHE D CD1 1 
ATOM   3691 C CD2 . PHE D 2 32  ? 40.061 45.214  138.562 1.00 47.60  ? 29  PHE D CD2 1 
ATOM   3692 C CE1 . PHE D 2 32  ? 42.516 44.962  139.669 1.00 47.72  ? 29  PHE D CE1 1 
ATOM   3693 C CE2 . PHE D 2 32  ? 40.848 44.141  138.202 1.00 38.50  ? 29  PHE D CE2 1 
ATOM   3694 C CZ  . PHE D 2 32  ? 42.067 44.011  138.758 1.00 40.60  ? 29  PHE D CZ  1 
ATOM   3695 N N   . LYS D 2 33  ? 37.573 49.214  141.441 1.00 46.72  ? 30  LYS D N   1 
ATOM   3696 C CA  . LYS D 2 33  ? 37.035 50.582  141.462 1.00 59.46  ? 30  LYS D CA  1 
ATOM   3697 C C   . LYS D 2 33  ? 37.164 51.213  142.860 1.00 50.35  ? 30  LYS D C   1 
ATOM   3698 O O   . LYS D 2 33  ? 37.541 52.324  142.974 1.00 37.06  ? 30  LYS D O   1 
ATOM   3699 C CB  . LYS D 2 33  ? 35.586 50.619  140.981 1.00 65.37  ? 30  LYS D CB  1 
ATOM   3700 C CG  . LYS D 2 33  ? 34.940 52.008  140.984 1.00 82.27  ? 30  LYS D CG  1 
ATOM   3701 C CD  . LYS D 2 33  ? 34.061 52.311  142.232 1.00 91.28  ? 30  LYS D CD  1 
ATOM   3702 C CE  . LYS D 2 33  ? 32.549 52.315  141.939 1.00 93.83  ? 30  LYS D CE  1 
ATOM   3703 N NZ  . LYS D 2 33  ? 32.149 53.291  140.865 1.00 90.10  ? 30  LYS D NZ  1 
ATOM   3704 N N   . GLN D 2 34  ? 36.873 50.456  143.901 1.00 53.42  ? 31  GLN D N   1 
ATOM   3705 C CA  . GLN D 2 34  ? 37.086 50.869  145.273 1.00 53.53  ? 31  GLN D CA  1 
ATOM   3706 C C   . GLN D 2 34  ? 38.522 51.286  145.570 1.00 51.96  ? 31  GLN D C   1 
ATOM   3707 O O   . GLN D 2 34  ? 38.708 52.174  146.355 1.00 54.03  ? 31  GLN D O   1 
ATOM   3708 C CB  . GLN D 2 34  ? 36.679 49.745  146.233 1.00 60.08  ? 31  GLN D CB  1 
ATOM   3709 C CG  . GLN D 2 34  ? 35.169 49.640  146.352 1.00 80.30  ? 31  GLN D CG  1 
ATOM   3710 C CD  . GLN D 2 34  ? 34.661 48.220  146.624 1.00 103.56 ? 31  GLN D CD  1 
ATOM   3711 O OE1 . GLN D 2 34  ? 35.348 47.375  147.228 1.00 108.44 ? 31  GLN D OE1 1 
ATOM   3712 N NE2 . GLN D 2 34  ? 33.434 47.953  146.171 1.00 115.69 ? 31  GLN D NE2 1 
ATOM   3713 N N   . ASN D 2 35  ? 39.534 50.659  144.979 1.00 44.89  ? 32  ASN D N   1 
ATOM   3714 C CA  . ASN D 2 35  ? 40.894 51.131  145.177 1.00 38.63  ? 32  ASN D CA  1 
ATOM   3715 C C   . ASN D 2 35  ? 41.253 52.223  144.196 1.00 37.83  ? 32  ASN D C   1 
ATOM   3716 O O   . ASN D 2 35  ? 42.407 52.568  144.055 1.00 41.43  ? 32  ASN D O   1 
ATOM   3717 C CB  . ASN D 2 35  ? 41.888 50.003  145.058 1.00 41.39  ? 32  ASN D CB  1 
ATOM   3718 C CG  . ASN D 2 35  ? 41.781 49.014  146.207 1.00 47.86  ? 32  ASN D CG  1 
ATOM   3719 O OD1 . ASN D 2 35  ? 42.698 48.890  147.021 1.00 67.10  ? 32  ASN D OD1 1 
ATOM   3720 N ND2 . ASN D 2 35  ? 40.681 48.310  146.280 1.00 50.12  ? 32  ASN D ND2 1 
ATOM   3721 N N   . GLY D 2 36  ? 40.283 52.771  143.486 1.00 35.91  ? 33  GLY D N   1 
ATOM   3722 C CA  . GLY D 2 36  ? 40.581 53.889  142.568 1.00 42.12  ? 33  GLY D CA  1 
ATOM   3723 C C   . GLY D 2 36  ? 41.080 53.588  141.167 1.00 43.51  ? 33  GLY D C   1 
ATOM   3724 O O   . GLY D 2 36  ? 41.514 54.483  140.439 1.00 44.91  ? 33  GLY D O   1 
ATOM   3725 N N   . TYR D 2 37  ? 41.049 52.328  140.773 1.00 46.42  ? 34  TYR D N   1 
ATOM   3726 C CA  . TYR D 2 37  ? 41.392 51.964  139.397 1.00 45.85  ? 34  TYR D CA  1 
ATOM   3727 C C   . TYR D 2 37  ? 40.142 51.897  138.545 1.00 49.75  ? 34  TYR D C   1 
ATOM   3728 O O   . TYR D 2 37  ? 39.226 51.158  138.898 1.00 60.12  ? 34  TYR D O   1 
ATOM   3729 C CB  . TYR D 2 37  ? 42.058 50.596  139.446 1.00 39.62  ? 34  TYR D CB  1 
ATOM   3730 C CG  . TYR D 2 37  ? 43.377 50.653  140.125 1.00 36.75  ? 34  TYR D CG  1 
ATOM   3731 C CD1 . TYR D 2 37  ? 44.439 51.194  139.495 1.00 34.79  ? 34  TYR D CD1 1 
ATOM   3732 C CD2 . TYR D 2 37  ? 43.531 50.257  141.426 1.00 40.43  ? 34  TYR D CD2 1 
ATOM   3733 C CE1 . TYR D 2 37  ? 45.668 51.234  140.076 1.00 36.31  ? 34  TYR D CE1 1 
ATOM   3734 C CE2 . TYR D 2 37  ? 44.762 50.342  142.041 1.00 42.86  ? 34  TYR D CE2 1 
ATOM   3735 C CZ  . TYR D 2 37  ? 45.829 50.822  141.349 1.00 40.68  ? 34  TYR D CZ  1 
ATOM   3736 O OH  . TYR D 2 37  ? 47.076 50.963  141.943 1.00 51.11  ? 34  TYR D OH  1 
ATOM   3737 N N   . ASP D 2 38  ? 40.054 52.651  137.454 1.00 57.08  ? 35  ASP D N   1 
ATOM   3738 C CA  . ASP D 2 38  ? 38.851 52.511  136.617 1.00 69.85  ? 35  ASP D CA  1 
ATOM   3739 C C   . ASP D 2 38  ? 39.118 51.502  135.468 1.00 67.23  ? 35  ASP D C   1 
ATOM   3740 O O   . ASP D 2 38  ? 39.127 51.821  134.287 1.00 61.47  ? 35  ASP D O   1 
ATOM   3741 C CB  . ASP D 2 38  ? 38.229 53.880  136.230 1.00 84.63  ? 35  ASP D CB  1 
ATOM   3742 C CG  . ASP D 2 38  ? 37.286 54.485  137.408 1.00 103.42 ? 35  ASP D CG  1 
ATOM   3743 O OD1 . ASP D 2 38  ? 36.345 53.797  137.912 1.00 89.71  ? 35  ASP D OD1 1 
ATOM   3744 O OD2 . ASP D 2 38  ? 37.488 55.654  137.847 1.00 100.36 ? 35  ASP D OD2 1 
ATOM   3745 N N   . ILE D 2 39  ? 39.383 50.266  135.873 1.00 55.87  ? 36  ILE D N   1 
ATOM   3746 C CA  . ILE D 2 39  ? 39.623 49.213  134.947 1.00 52.96  ? 36  ILE D CA  1 
ATOM   3747 C C   . ILE D 2 39  ? 38.705 48.036  135.251 1.00 53.53  ? 36  ILE D C   1 
ATOM   3748 O O   . ILE D 2 39  ? 38.201 47.890  136.353 1.00 50.11  ? 36  ILE D O   1 
ATOM   3749 C CB  . ILE D 2 39  ? 41.100 48.716  134.934 1.00 52.08  ? 36  ILE D CB  1 
ATOM   3750 C CG1 . ILE D 2 39  ? 41.388 47.843  136.113 1.00 46.74  ? 36  ILE D CG1 1 
ATOM   3751 C CG2 . ILE D 2 39  ? 42.159 49.810  134.853 1.00 47.92  ? 36  ILE D CG2 1 
ATOM   3752 C CD1 . ILE D 2 39  ? 42.522 46.952  135.769 1.00 48.79  ? 36  ILE D CD1 1 
ATOM   3753 N N   . THR D 2 40  ? 38.529 47.175  134.260 1.00 52.50  ? 37  THR D N   1 
ATOM   3754 C CA  . THR D 2 40  ? 37.647 46.038  134.363 1.00 47.28  ? 37  THR D CA  1 
ATOM   3755 C C   . THR D 2 40  ? 38.467 44.804  134.379 1.00 41.68  ? 37  THR D C   1 
ATOM   3756 O O   . THR D 2 40  ? 39.672 44.812  134.121 1.00 42.85  ? 37  THR D O   1 
ATOM   3757 C CB  . THR D 2 40  ? 36.777 45.909  133.101 1.00 58.70  ? 37  THR D CB  1 
ATOM   3758 O OG1 . THR D 2 40  ? 37.626 45.599  131.975 1.00 55.28  ? 37  THR D OG1 1 
ATOM   3759 C CG2 . THR D 2 40  ? 36.022 47.218  132.831 1.00 58.06  ? 37  THR D CG2 1 
ATOM   3760 N N   . THR D 2 41  ? 37.786 43.709  134.618 1.00 41.04  ? 38  THR D N   1 
ATOM   3761 C CA  . THR D 2 41  ? 38.405 42.436  134.579 1.00 43.21  ? 38  THR D CA  1 
ATOM   3762 C C   . THR D 2 41  ? 38.974 42.124  133.216 1.00 46.87  ? 38  THR D C   1 
ATOM   3763 O O   . THR D 2 41  ? 40.040 41.510  133.126 1.00 47.93  ? 38  THR D O   1 
ATOM   3764 C CB  . THR D 2 41  ? 37.389 41.403  134.988 1.00 47.72  ? 38  THR D CB  1 
ATOM   3765 O OG1 . THR D 2 41  ? 36.788 41.866  136.204 1.00 51.18  ? 38  THR D OG1 1 
ATOM   3766 C CG2 . THR D 2 41  ? 38.053 40.080  135.258 1.00 53.65  ? 38  THR D CG2 1 
ATOM   3767 N N   . ASP D 2 42  ? 38.310 42.556  132.147 1.00 45.97  ? 39  ASP D N   1 
ATOM   3768 C CA  . ASP D 2 42  ? 38.773 42.173  130.828 1.00 45.44  ? 39  ASP D CA  1 
ATOM   3769 C C   . ASP D 2 42  ? 40.103 42.861  130.619 1.00 43.89  ? 39  ASP D C   1 
ATOM   3770 O O   . ASP D 2 42  ? 41.098 42.200  130.208 1.00 43.44  ? 39  ASP D O   1 
ATOM   3771 C CB  . ASP D 2 42  ? 37.784 42.512  129.714 1.00 50.11  ? 39  ASP D CB  1 
ATOM   3772 C CG  . ASP D 2 42  ? 36.575 41.586  129.676 1.00 54.07  ? 39  ASP D CG  1 
ATOM   3773 O OD1 . ASP D 2 42  ? 36.685 40.384  129.978 1.00 55.49  ? 39  ASP D OD1 1 
ATOM   3774 O OD2 . ASP D 2 42  ? 35.505 42.099  129.322 1.00 54.69  ? 39  ASP D OD2 1 
ATOM   3775 N N   . HIS D 2 43  ? 40.170 44.144  131.006 1.00 36.29  ? 40  HIS D N   1 
ATOM   3776 C CA  . HIS D 2 43  ? 41.416 44.856  130.830 1.00 35.83  ? 40  HIS D CA  1 
ATOM   3777 C C   . HIS D 2 43  ? 42.536 44.168  131.611 1.00 36.44  ? 40  HIS D C   1 
ATOM   3778 O O   . HIS D 2 43  ? 43.663 44.069  131.139 1.00 31.73  ? 40  HIS D O   1 
ATOM   3779 C CB  . HIS D 2 43  ? 41.359 46.290  131.259 1.00 42.32  ? 40  HIS D CB  1 
ATOM   3780 C CG  . HIS D 2 43  ? 40.222 47.071  130.694 1.00 49.20  ? 40  HIS D CG  1 
ATOM   3781 N ND1 . HIS D 2 43  ? 39.605 48.086  131.399 1.00 59.79  ? 40  HIS D ND1 1 
ATOM   3782 C CD2 . HIS D 2 43  ? 39.581 46.993  129.517 1.00 51.98  ? 40  HIS D CD2 1 
ATOM   3783 C CE1 . HIS D 2 43  ? 38.634 48.602  130.675 1.00 55.22  ? 40  HIS D CE1 1 
ATOM   3784 N NE2 . HIS D 2 43  ? 38.594 47.955  129.529 1.00 54.80  ? 40  HIS D NE2 1 
ATOM   3785 N N   . TYR D 2 44  ? 42.210 43.666  132.795 1.00 34.94  ? 41  TYR D N   1 
ATOM   3786 C CA  . TYR D 2 44  ? 43.206 43.098  133.656 1.00 32.40  ? 41  TYR D CA  1 
ATOM   3787 C C   . TYR D 2 44  ? 43.642 41.844  132.985 1.00 32.32  ? 41  TYR D C   1 
ATOM   3788 O O   . TYR D 2 44  ? 44.873 41.542  132.868 1.00 32.19  ? 41  TYR D O   1 
ATOM   3789 C CB  . TYR D 2 44  ? 42.643 42.842  135.077 1.00 32.93  ? 41  TYR D CB  1 
ATOM   3790 C CG  . TYR D 2 44  ? 43.579 42.079  135.985 1.00 30.41  ? 41  TYR D CG  1 
ATOM   3791 C CD1 . TYR D 2 44  ? 44.825 42.562  136.280 1.00 34.83  ? 41  TYR D CD1 1 
ATOM   3792 C CD2 . TYR D 2 44  ? 43.238 40.849  136.462 1.00 32.12  ? 41  TYR D CD2 1 
ATOM   3793 C CE1 . TYR D 2 44  ? 45.706 41.850  137.072 1.00 38.68  ? 41  TYR D CE1 1 
ATOM   3794 C CE2 . TYR D 2 44  ? 44.100 40.113  137.282 1.00 36.44  ? 41  TYR D CE2 1 
ATOM   3795 C CZ  . TYR D 2 44  ? 45.322 40.626  137.595 1.00 37.37  ? 41  TYR D CZ  1 
ATOM   3796 O OH  . TYR D 2 44  ? 46.162 39.905  138.375 1.00 36.26  ? 41  TYR D OH  1 
ATOM   3797 N N   . ALA D 2 45  ? 42.666 41.126  132.474 1.00 31.81  ? 42  ALA D N   1 
ATOM   3798 C CA  . ALA D 2 45  ? 42.985 39.869  131.795 1.00 35.55  ? 42  ALA D CA  1 
ATOM   3799 C C   . ALA D 2 45  ? 43.923 40.114  130.650 1.00 35.10  ? 42  ALA D C   1 
ATOM   3800 O O   . ALA D 2 45  ? 44.881 39.412  130.515 1.00 42.51  ? 42  ALA D O   1 
ATOM   3801 C CB  . ALA D 2 45  ? 41.736 39.159  131.298 1.00 36.84  ? 42  ALA D CB  1 
ATOM   3802 N N   . LEU D 2 46  ? 43.719 41.166  129.878 1.00 36.55  ? 43  LEU D N   1 
ATOM   3803 C CA  . LEU D 2 46  ? 44.559 41.347  128.683 1.00 39.56  ? 43  LEU D CA  1 
ATOM   3804 C C   . LEU D 2 46  ? 45.945 41.856  129.065 1.00 38.65  ? 43  LEU D C   1 
ATOM   3805 O O   . LEU D 2 46  ? 46.974 41.454  128.474 1.00 40.18  ? 43  LEU D O   1 
ATOM   3806 C CB  . LEU D 2 46  ? 43.863 42.312  127.722 1.00 42.33  ? 43  LEU D CB  1 
ATOM   3807 C CG  . LEU D 2 46  ? 42.913 41.856  126.611 1.00 43.15  ? 43  LEU D CG  1 
ATOM   3808 C CD1 . LEU D 2 46  ? 42.713 40.382  126.511 1.00 44.20  ? 43  LEU D CD1 1 
ATOM   3809 C CD2 . LEU D 2 46  ? 41.592 42.565  126.758 1.00 47.96  ? 43  LEU D CD2 1 
ATOM   3810 N N   . LEU D 2 47  ? 45.969 42.730  130.068 1.00 37.34  ? 44  LEU D N   1 
ATOM   3811 C CA  . LEU D 2 47  ? 47.215 43.223  130.627 1.00 38.12  ? 44  LEU D CA  1 
ATOM   3812 C C   . LEU D 2 47  ? 48.083 42.063  131.106 1.00 37.02  ? 44  LEU D C   1 
ATOM   3813 O O   . LEU D 2 47  ? 49.327 42.073  130.918 1.00 35.80  ? 44  LEU D O   1 
ATOM   3814 C CB  . LEU D 2 47  ? 46.959 44.199  131.794 1.00 37.10  ? 44  LEU D CB  1 
ATOM   3815 C CG  . LEU D 2 47  ? 46.519 45.625  131.469 1.00 35.10  ? 44  LEU D CG  1 
ATOM   3816 C CD1 . LEU D 2 47  ? 46.202 46.424  132.701 1.00 37.69  ? 44  LEU D CD1 1 
ATOM   3817 C CD2 . LEU D 2 47  ? 47.560 46.389  130.715 1.00 36.48  ? 44  LEU D CD2 1 
ATOM   3818 N N   . ARG D 2 48  ? 47.457 41.070  131.726 1.00 36.13  ? 45  ARG D N   1 
ATOM   3819 C CA  . ARG D 2 48  ? 48.224 39.859  132.163 1.00 42.43  ? 45  ARG D CA  1 
ATOM   3820 C C   . ARG D 2 48  ? 48.953 39.165  131.021 1.00 41.80  ? 45  ARG D C   1 
ATOM   3821 O O   . ARG D 2 48  ? 50.154 38.817  131.137 1.00 39.46  ? 45  ARG D O   1 
ATOM   3822 C CB  . ARG D 2 48  ? 47.309 38.822  132.772 1.00 43.90  ? 45  ARG D CB  1 
ATOM   3823 C CG  . ARG D 2 48  ? 46.706 39.272  134.078 1.00 43.38  ? 45  ARG D CG  1 
ATOM   3824 C CD  . ARG D 2 48  ? 47.665 39.007  135.163 1.00 43.48  ? 45  ARG D CD  1 
ATOM   3825 N NE  . ARG D 2 48  ? 47.866 37.565  135.359 1.00 52.38  ? 45  ARG D NE  1 
ATOM   3826 C CZ  . ARG D 2 48  ? 48.445 37.028  136.432 1.00 50.83  ? 45  ARG D CZ  1 
ATOM   3827 N NH1 . ARG D 2 48  ? 48.827 37.773  137.461 1.00 54.30  ? 45  ARG D NH1 1 
ATOM   3828 N NH2 . ARG D 2 48  ? 48.603 35.739  136.484 1.00 51.96  ? 45  ARG D NH2 1 
ATOM   3829 N N   . PHE D 2 49  ? 48.243 38.999  129.902 1.00 36.60  ? 46  PHE D N   1 
ATOM   3830 C CA  . PHE D 2 49  ? 48.906 38.479  128.719 1.00 35.34  ? 46  PHE D CA  1 
ATOM   3831 C C   . PHE D 2 49  ? 50.110 39.326  128.330 1.00 35.44  ? 46  PHE D C   1 
ATOM   3832 O O   . PHE D 2 49  ? 51.190 38.820  128.081 1.00 35.71  ? 46  PHE D O   1 
ATOM   3833 C CB  . PHE D 2 49  ? 47.943 38.348  127.553 1.00 35.43  ? 46  PHE D CB  1 
ATOM   3834 C CG  . PHE D 2 49  ? 46.898 37.293  127.746 1.00 33.20  ? 46  PHE D CG  1 
ATOM   3835 C CD1 . PHE D 2 49  ? 47.233 36.011  128.175 1.00 35.44  ? 46  PHE D CD1 1 
ATOM   3836 C CD2 . PHE D 2 49  ? 45.564 37.570  127.447 1.00 36.69  ? 46  PHE D CD2 1 
ATOM   3837 C CE1 . PHE D 2 49  ? 46.244 35.033  128.324 1.00 36.31  ? 46  PHE D CE1 1 
ATOM   3838 C CE2 . PHE D 2 49  ? 44.558 36.601  127.631 1.00 33.84  ? 46  PHE D CE2 1 
ATOM   3839 C CZ  . PHE D 2 49  ? 44.891 35.349  128.078 1.00 33.05  ? 46  PHE D CZ  1 
ATOM   3840 N N   . LEU D 2 50  ? 49.920 40.631  128.294 1.00 37.25  ? 47  LEU D N   1 
ATOM   3841 C CA  . LEU D 2 50  ? 50.994 41.546  127.896 1.00 37.04  ? 47  LEU D CA  1 
ATOM   3842 C C   . LEU D 2 50  ? 52.165 41.612  128.869 1.00 42.02  ? 47  LEU D C   1 
ATOM   3843 O O   . LEU D 2 50  ? 53.268 41.883  128.434 1.00 49.20  ? 47  LEU D O   1 
ATOM   3844 C CB  . LEU D 2 50  ? 50.415 42.933  127.692 1.00 37.93  ? 47  LEU D CB  1 
ATOM   3845 C CG  . LEU D 2 50  ? 49.479 42.921  126.487 1.00 39.06  ? 47  LEU D CG  1 
ATOM   3846 C CD1 . LEU D 2 50  ? 48.566 44.111  126.385 1.00 39.71  ? 47  LEU D CD1 1 
ATOM   3847 C CD2 . LEU D 2 50  ? 50.316 42.873  125.228 1.00 41.99  ? 47  LEU D CD2 1 
ATOM   3848 N N   . TRP D 2 51  ? 51.938 41.362  130.169 1.00 42.32  ? 48  TRP D N   1 
ATOM   3849 C CA  . TRP D 2 51  ? 53.037 41.297  131.125 1.00 38.61  ? 48  TRP D CA  1 
ATOM   3850 C C   . TRP D 2 51  ? 53.804 40.011  130.943 1.00 38.65  ? 48  TRP D C   1 
ATOM   3851 O O   . TRP D 2 51  ? 54.965 40.002  131.196 1.00 42.41  ? 48  TRP D O   1 
ATOM   3852 C CB  . TRP D 2 51  ? 52.589 41.470  132.610 1.00 40.04  ? 48  TRP D CB  1 
ATOM   3853 C CG  . TRP D 2 51  ? 51.879 42.809  132.973 1.00 35.76  ? 48  TRP D CG  1 
ATOM   3854 C CD1 . TRP D 2 51  ? 52.229 44.070  132.552 1.00 33.58  ? 48  TRP D CD1 1 
ATOM   3855 C CD2 . TRP D 2 51  ? 50.689 42.980  133.772 1.00 33.29  ? 48  TRP D CD2 1 
ATOM   3856 N NE1 . TRP D 2 51  ? 51.374 45.002  133.079 1.00 31.03  ? 48  TRP D NE1 1 
ATOM   3857 C CE2 . TRP D 2 51  ? 50.401 44.362  133.799 1.00 31.25  ? 48  TRP D CE2 1 
ATOM   3858 C CE3 . TRP D 2 51  ? 49.869 42.108  134.475 1.00 30.65  ? 48  TRP D CE3 1 
ATOM   3859 C CZ2 . TRP D 2 51  ? 49.334 44.883  134.486 1.00 35.16  ? 48  TRP D CZ2 1 
ATOM   3860 C CZ3 . TRP D 2 51  ? 48.820 42.618  135.154 1.00 39.05  ? 48  TRP D CZ3 1 
ATOM   3861 C CH2 . TRP D 2 51  ? 48.553 44.006  135.174 1.00 39.60  ? 48  TRP D CH2 1 
ATOM   3862 N N   . GLU D 2 52  ? 53.178 38.914  130.507 1.00 52.61  ? 49  GLU D N   1 
ATOM   3863 C CA  . GLU D 2 52  ? 53.949 37.741  130.028 1.00 52.13  ? 49  GLU D CA  1 
ATOM   3864 C C   . GLU D 2 52  ? 54.752 38.093  128.759 1.00 54.65  ? 49  GLU D C   1 
ATOM   3865 O O   . GLU D 2 52  ? 55.968 37.931  128.743 1.00 50.77  ? 49  GLU D O   1 
ATOM   3866 C CB  . GLU D 2 52  ? 53.078 36.522  129.728 1.00 59.19  ? 49  GLU D CB  1 
ATOM   3867 C CG  . GLU D 2 52  ? 53.019 35.445  130.803 1.00 77.27  ? 49  GLU D CG  1 
ATOM   3868 C CD  . GLU D 2 52  ? 54.330 35.306  131.590 1.00 96.01  ? 49  GLU D CD  1 
ATOM   3869 O OE1 . GLU D 2 52  ? 55.270 34.604  131.118 1.00 87.23  ? 49  GLU D OE1 1 
ATOM   3870 O OE2 . GLU D 2 52  ? 54.412 35.918  132.688 1.00 100.33 ? 49  GLU D OE2 1 
ATOM   3871 N N   . GLN D 2 53  ? 54.077 38.577  127.715 1.00 50.41  ? 50  GLN D N   1 
ATOM   3872 C CA  . GLN D 2 53  ? 54.735 38.889  126.456 1.00 55.55  ? 50  GLN D CA  1 
ATOM   3873 C C   . GLN D 2 53  ? 54.179 40.172  125.883 1.00 53.79  ? 50  GLN D C   1 
ATOM   3874 O O   . GLN D 2 53  ? 53.034 40.227  125.450 1.00 61.87  ? 50  GLN D O   1 
ATOM   3875 C CB  . GLN D 2 53  ? 54.509 37.761  125.428 1.00 58.78  ? 50  GLN D CB  1 
ATOM   3876 C CG  . GLN D 2 53  ? 55.338 37.865  124.138 1.00 67.34  ? 50  GLN D CG  1 
ATOM   3877 C CD  . GLN D 2 53  ? 56.847 37.583  124.344 1.00 79.53  ? 50  GLN D CD  1 
ATOM   3878 O OE1 . GLN D 2 53  ? 57.714 38.388  123.960 1.00 69.11  ? 50  GLN D OE1 1 
ATOM   3879 N NE2 . GLN D 2 53  ? 57.159 36.439  124.974 1.00 88.38  ? 50  GLN D NE2 1 
ATOM   3880 N N   . ASP D 2 54  ? 55.012 41.189  125.850 1.00 49.39  ? 51  ASP D N   1 
ATOM   3881 C CA  . ASP D 2 54  ? 54.724 42.449  125.170 1.00 46.61  ? 51  ASP D CA  1 
ATOM   3882 C C   . ASP D 2 54  ? 54.814 42.289  123.664 1.00 46.00  ? 51  ASP D C   1 
ATOM   3883 O O   . ASP D 2 54  ? 55.533 41.456  123.177 1.00 65.60  ? 51  ASP D O   1 
ATOM   3884 C CB  . ASP D 2 54  ? 55.802 43.408  125.578 1.00 44.13  ? 51  ASP D CB  1 
ATOM   3885 C CG  . ASP D 2 54  ? 55.422 44.830  125.408 1.00 49.52  ? 51  ASP D CG  1 
ATOM   3886 O OD1 . ASP D 2 54  ? 54.216 45.146  125.462 1.00 50.37  ? 51  ASP D OD1 1 
ATOM   3887 O OD2 . ASP D 2 54  ? 56.378 45.640  125.292 1.00 56.74  ? 51  ASP D OD2 1 
ATOM   3888 N N   . GLY D 2 55  ? 54.128 43.107  122.912 1.00 50.47  ? 52  GLY D N   1 
ATOM   3889 C CA  . GLY D 2 55  ? 54.301 43.085  121.475 1.00 51.81  ? 52  GLY D CA  1 
ATOM   3890 C C   . GLY D 2 55  ? 53.482 41.997  120.795 1.00 52.74  ? 52  GLY D C   1 
ATOM   3891 O O   . GLY D 2 55  ? 53.685 41.736  119.610 1.00 59.17  ? 52  GLY D O   1 
ATOM   3892 N N   . ILE D 2 56  ? 52.531 41.393  121.506 1.00 50.56  ? 53  ILE D N   1 
ATOM   3893 C CA  . ILE D 2 56  ? 51.691 40.343  120.925 1.00 49.20  ? 53  ILE D CA  1 
ATOM   3894 C C   . ILE D 2 56  ? 50.895 41.017  119.815 1.00 49.41  ? 53  ILE D C   1 
ATOM   3895 O O   . ILE D 2 56  ? 50.479 42.174  119.946 1.00 53.12  ? 53  ILE D O   1 
ATOM   3896 C CB  . ILE D 2 56  ? 50.662 39.748  121.945 1.00 55.81  ? 53  ILE D CB  1 
ATOM   3897 C CG1 . ILE D 2 56  ? 51.332 39.269  123.223 1.00 64.19  ? 53  ILE D CG1 1 
ATOM   3898 C CG2 . ILE D 2 56  ? 49.927 38.552  121.372 1.00 58.69  ? 53  ILE D CG2 1 
ATOM   3899 C CD1 . ILE D 2 56  ? 50.433 38.470  124.152 1.00 67.52  ? 53  ILE D CD1 1 
ATOM   3900 N N   . SER D 2 57  ? 50.623 40.282  118.749 1.00 48.58  ? 54  SER D N   1 
ATOM   3901 C CA  . SER D 2 57  ? 49.845 40.797  117.637 1.00 47.44  ? 54  SER D CA  1 
ATOM   3902 C C   . SER D 2 57  ? 48.397 40.869  118.087 1.00 45.66  ? 54  SER D C   1 
ATOM   3903 O O   . SER D 2 57  ? 48.006 40.114  118.946 1.00 42.84  ? 54  SER D O   1 
ATOM   3904 C CB  . SER D 2 57  ? 49.982 39.899  116.416 1.00 50.26  ? 54  SER D CB  1 
ATOM   3905 O OG  . SER D 2 57  ? 49.146 38.765  116.478 1.00 54.21  ? 54  SER D OG  1 
ATOM   3906 N N   . GLN D 2 58  ? 47.612 41.780  117.524 1.00 39.00  ? 55  GLN D N   1 
ATOM   3907 C CA  . GLN D 2 58  ? 46.291 41.974  117.992 1.00 37.09  ? 55  GLN D CA  1 
ATOM   3908 C C   . GLN D 2 58  ? 45.445 40.742  117.771 1.00 46.79  ? 55  GLN D C   1 
ATOM   3909 O O   . GLN D 2 58  ? 44.549 40.408  118.578 1.00 57.27  ? 55  GLN D O   1 
ATOM   3910 C CB  . GLN D 2 58  ? 45.666 43.150  117.289 1.00 36.78  ? 55  GLN D CB  1 
ATOM   3911 C CG  . GLN D 2 58  ? 44.200 43.294  117.587 1.00 38.58  ? 55  GLN D CG  1 
ATOM   3912 C CD  . GLN D 2 58  ? 43.656 44.639  117.183 1.00 43.55  ? 55  GLN D CD  1 
ATOM   3913 O OE1 . GLN D 2 58  ? 43.040 44.773  116.149 1.00 47.17  ? 55  GLN D OE1 1 
ATOM   3914 N NE2 . GLN D 2 58  ? 43.845 45.632  118.020 1.00 50.26  ? 55  GLN D NE2 1 
ATOM   3915 N N   . ILE D 2 59  ? 45.690 40.058  116.671 1.00 48.59  ? 56  ILE D N   1 
ATOM   3916 C CA  . ILE D 2 59  ? 44.855 38.881  116.348 1.00 51.21  ? 56  ILE D CA  1 
ATOM   3917 C C   . ILE D 2 59  ? 45.217 37.680  117.272 1.00 46.55  ? 56  ILE D C   1 
ATOM   3918 O O   . ILE D 2 59  ? 44.343 36.949  117.703 1.00 43.38  ? 56  ILE D O   1 
ATOM   3919 C CB  . ILE D 2 59  ? 44.865 38.538  114.831 1.00 46.05  ? 56  ILE D CB  1 
ATOM   3920 C CG1 . ILE D 2 59  ? 43.599 37.744  114.530 1.00 57.89  ? 56  ILE D CG1 1 
ATOM   3921 C CG2 . ILE D 2 59  ? 46.182 37.892  114.426 1.00 42.42  ? 56  ILE D CG2 1 
ATOM   3922 C CD1 . ILE D 2 59  ? 43.528 37.064  113.177 1.00 66.96  ? 56  ILE D CD1 1 
ATOM   3923 N N   . ASP D 2 60  ? 46.483 37.540  117.608 1.00 40.75  ? 57  ASP D N   1 
ATOM   3924 C CA  . ASP D 2 60  ? 46.887 36.626  118.654 1.00 51.21  ? 57  ASP D CA  1 
ATOM   3925 C C   . ASP D 2 60  ? 46.201 36.958  119.995 1.00 56.02  ? 57  ASP D C   1 
ATOM   3926 O O   . ASP D 2 60  ? 45.599 36.098  120.584 1.00 60.19  ? 57  ASP D O   1 
ATOM   3927 C CB  . ASP D 2 60  ? 48.392 36.621  118.799 1.00 47.77  ? 57  ASP D CB  1 
ATOM   3928 C CG  . ASP D 2 60  ? 49.061 35.679  117.837 1.00 57.01  ? 57  ASP D CG  1 
ATOM   3929 O OD1 . ASP D 2 60  ? 48.377 35.020  116.981 1.00 58.61  ? 57  ASP D OD1 1 
ATOM   3930 O OD2 . ASP D 2 60  ? 50.305 35.573  117.962 1.00 74.22  ? 57  ASP D OD2 1 
ATOM   3931 N N   . LEU D 2 61  ? 46.197 38.207  120.430 1.00 52.34  ? 58  LEU D N   1 
ATOM   3932 C CA  . LEU D 2 61  ? 45.470 38.528  121.645 1.00 52.73  ? 58  LEU D CA  1 
ATOM   3933 C C   . LEU D 2 61  ? 44.046 38.200  121.502 1.00 51.09  ? 58  LEU D C   1 
ATOM   3934 O O   . LEU D 2 61  ? 43.402 37.853  122.475 1.00 50.74  ? 58  LEU D O   1 
ATOM   3935 C CB  . LEU D 2 61  ? 45.485 40.015  121.975 1.00 52.97  ? 58  LEU D CB  1 
ATOM   3936 C CG  . LEU D 2 61  ? 46.581 40.460  122.863 1.00 47.99  ? 58  LEU D CG  1 
ATOM   3937 C CD1 . LEU D 2 61  ? 46.440 41.966  123.006 1.00 54.44  ? 58  LEU D CD1 1 
ATOM   3938 C CD2 . LEU D 2 61  ? 46.466 39.759  124.182 1.00 48.19  ? 58  LEU D CD2 1 
ATOM   3939 N N   . CYS D 2 62  ? 43.503 38.392  120.316 1.00 54.09  ? 59  CYS D N   1 
ATOM   3940 C CA  . CYS D 2 62  ? 42.130 37.945  120.117 1.00 55.70  ? 59  CYS D CA  1 
ATOM   3941 C C   . CYS D 2 62  ? 41.975 36.408  120.306 1.00 57.03  ? 59  CYS D C   1 
ATOM   3942 O O   . CYS D 2 62  ? 40.939 36.008  120.800 1.00 51.97  ? 59  CYS D O   1 
ATOM   3943 C CB  . CYS D 2 62  ? 41.605 38.441  118.795 1.00 54.71  ? 59  CYS D CB  1 
ATOM   3944 S SG  . CYS D 2 62  ? 41.210 40.211  118.883 1.00 57.70  ? 59  CYS D SG  1 
ATOM   3945 N N   . GLU D 2 63  ? 43.015 35.604  119.970 1.00 61.14  ? 60  GLU D N   1 
ATOM   3946 C CA  . GLU D 2 63  ? 43.028 34.130  120.092 1.00 69.69  ? 60  GLU D CA  1 
ATOM   3947 C C   . GLU D 2 63  ? 42.933 33.693  121.530 1.00 72.67  ? 60  GLU D C   1 
ATOM   3948 O O   . GLU D 2 63  ? 42.107 32.850  121.882 1.00 77.62  ? 60  GLU D O   1 
ATOM   3949 C CB  . GLU D 2 63  ? 44.336 33.476  119.580 1.00 77.14  ? 60  GLU D CB  1 
ATOM   3950 C CG  . GLU D 2 63  ? 44.648 33.565  118.094 1.00 95.70  ? 60  GLU D CG  1 
ATOM   3951 C CD  . GLU D 2 63  ? 43.496 33.113  117.220 1.00 103.10 ? 60  GLU D CD  1 
ATOM   3952 O OE1 . GLU D 2 63  ? 42.804 32.145  117.604 1.00 116.86 ? 60  GLU D OE1 1 
ATOM   3953 O OE2 . GLU D 2 63  ? 43.280 33.731  116.156 1.00 90.89  ? 60  GLU D OE2 1 
ATOM   3954 N N   . LYS D 2 64  ? 43.838 34.261  122.325 1.00 65.02  ? 61  LYS D N   1 
ATOM   3955 C CA  . LYS D 2 64  ? 44.003 33.993  123.742 1.00 58.27  ? 61  LYS D CA  1 
ATOM   3956 C C   . LYS D 2 64  ? 42.813 34.501  124.541 1.00 56.82  ? 61  LYS D C   1 
ATOM   3957 O O   . LYS D 2 64  ? 42.398 33.923  125.526 1.00 53.07  ? 61  LYS D O   1 
ATOM   3958 C CB  . LYS D 2 64  ? 45.227 34.728  124.225 1.00 56.52  ? 61  LYS D CB  1 
ATOM   3959 C CG  . LYS D 2 64  ? 46.483 34.338  123.477 1.00 62.10  ? 61  LYS D CG  1 
ATOM   3960 C CD  . LYS D 2 64  ? 47.682 34.955  124.165 1.00 67.90  ? 61  LYS D CD  1 
ATOM   3961 C CE  . LYS D 2 64  ? 48.949 34.611  123.415 1.00 83.41  ? 61  LYS D CE  1 
ATOM   3962 N NZ  . LYS D 2 64  ? 49.936 34.033  124.363 1.00 90.18  ? 61  LYS D NZ  1 
ATOM   3963 N N   . SER D 2 65  ? 42.300 35.638  124.130 1.00 59.28  ? 62  SER D N   1 
ATOM   3964 C CA  . SER D 2 65  ? 41.097 36.149  124.714 1.00 62.84  ? 62  SER D CA  1 
ATOM   3965 C C   . SER D 2 65  ? 40.051 35.074  124.477 1.00 68.23  ? 62  SER D C   1 
ATOM   3966 O O   . SER D 2 65  ? 39.844 34.587  123.343 1.00 74.96  ? 62  SER D O   1 
ATOM   3967 C CB  . SER D 2 65  ? 40.717 37.484  124.065 1.00 63.17  ? 62  SER D CB  1 
ATOM   3968 O OG  . SER D 2 65  ? 39.344 37.746  124.156 1.00 61.22  ? 62  SER D OG  1 
ATOM   3969 N N   . CYS D 2 66  ? 39.415 34.672  125.563 1.00 68.01  ? 63  CYS D N   1 
ATOM   3970 C CA  . CYS D 2 66  ? 38.298 33.744  125.464 1.00 72.36  ? 63  CYS D CA  1 
ATOM   3971 C C   . CYS D 2 66  ? 37.120 34.537  124.961 1.00 69.24  ? 63  CYS D C   1 
ATOM   3972 O O   . CYS D 2 66  ? 36.053 33.974  124.748 1.00 84.80  ? 63  CYS D O   1 
ATOM   3973 C CB  . CYS D 2 66  ? 37.970 33.111  126.806 1.00 71.25  ? 63  CYS D CB  1 
ATOM   3974 S SG  . CYS D 2 66  ? 37.850 34.326  128.149 1.00 76.57  ? 63  CYS D SG  1 
ATOM   3975 N N   . LYS D 2 67  ? 37.292 35.847  124.789 1.00 61.12  ? 64  LYS D N   1 
ATOM   3976 C CA  . LYS D 2 67  ? 36.403 36.551  123.890 1.00 63.04  ? 64  LYS D CA  1 
ATOM   3977 C C   . LYS D 2 67  ? 36.853 36.444  122.415 1.00 75.31  ? 64  LYS D C   1 
ATOM   3978 O O   . LYS D 2 67  ? 38.012 35.995  122.063 1.00 65.84  ? 64  LYS D O   1 
ATOM   3979 C CB  . LYS D 2 67  ? 36.106 37.991  124.327 1.00 62.21  ? 64  LYS D CB  1 
ATOM   3980 C CG  . LYS D 2 67  ? 35.153 37.997  125.518 1.00 66.84  ? 64  LYS D CG  1 
ATOM   3981 C CD  . LYS D 2 67  ? 34.814 39.393  126.019 1.00 70.52  ? 64  LYS D CD  1 
ATOM   3982 C CE  . LYS D 2 67  ? 34.100 39.331  127.363 1.00 61.66  ? 64  LYS D CE  1 
ATOM   3983 N NZ  . LYS D 2 67  ? 33.470 40.627  127.728 1.00 55.83  ? 64  LYS D NZ  1 
ATOM   3984 N N   . ASP D 2 68  ? 35.851 36.804  121.599 1.00 67.81  ? 65  ASP D N   1 
ATOM   3985 C CA  . ASP D 2 68  ? 35.880 36.818  120.149 1.00 73.72  ? 65  ASP D CA  1 
ATOM   3986 C C   . ASP D 2 68  ? 36.537 38.101  119.670 1.00 78.48  ? 65  ASP D C   1 
ATOM   3987 O O   . ASP D 2 68  ? 36.725 39.025  120.460 1.00 79.68  ? 65  ASP D O   1 
ATOM   3988 C CB  . ASP D 2 68  ? 34.435 36.763  119.597 1.00 73.04  ? 65  ASP D CB  1 
ATOM   3989 C CG  . ASP D 2 68  ? 33.566 37.890  120.131 1.00 77.30  ? 65  ASP D CG  1 
ATOM   3990 O OD1 . ASP D 2 68  ? 33.081 37.782  121.300 1.00 82.78  ? 65  ASP D OD1 1 
ATOM   3991 O OD2 . ASP D 2 68  ? 33.425 38.896  119.411 1.00 76.82  ? 65  ASP D OD2 1 
ATOM   3992 N N   . LYS D 2 69  ? 36.839 38.135  118.367 1.00 81.70  ? 66  LYS D N   1 
ATOM   3993 C CA  . LYS D 2 69  ? 37.540 39.230  117.681 1.00 81.03  ? 66  LYS D CA  1 
ATOM   3994 C C   . LYS D 2 69  ? 36.992 40.629  117.997 1.00 74.46  ? 66  LYS D C   1 
ATOM   3995 O O   . LYS D 2 69  ? 37.743 41.553  118.390 1.00 78.93  ? 66  LYS D O   1 
ATOM   3996 C CB  . LYS D 2 69  ? 37.492 39.001  116.150 1.00 89.49  ? 66  LYS D CB  1 
ATOM   3997 C CG  . LYS D 2 69  ? 38.329 39.959  115.294 1.00 96.71  ? 66  LYS D CG  1 
ATOM   3998 C CD  . LYS D 2 69  ? 39.770 39.479  115.101 1.00 102.02 ? 66  LYS D CD  1 
ATOM   3999 C CE  . LYS D 2 69  ? 40.783 40.629  115.029 1.00 107.30 ? 66  LYS D CE  1 
ATOM   4000 N NZ  . LYS D 2 69  ? 40.398 41.770  114.149 1.00 110.09 ? 66  LYS D NZ  1 
ATOM   4001 N N   . SER D 2 70  ? 35.694 40.799  117.823 1.00 61.54  ? 67  SER D N   1 
ATOM   4002 C CA  . SER D 2 70  ? 35.158 42.149  117.761 1.00 61.95  ? 67  SER D CA  1 
ATOM   4003 C C   . SER D 2 70  ? 35.111 42.810  119.141 1.00 64.38  ? 67  SER D C   1 
ATOM   4004 O O   . SER D 2 70  ? 35.419 43.983  119.271 1.00 63.39  ? 67  SER D O   1 
ATOM   4005 C CB  . SER D 2 70  ? 33.763 42.145  117.122 1.00 64.08  ? 67  SER D CB  1 
ATOM   4006 O OG  . SER D 2 70  ? 33.365 43.476  116.795 1.00 68.71  ? 67  SER D OG  1 
ATOM   4007 N N   . ASN D 2 71  ? 34.722 42.054  120.169 1.00 64.95  ? 68  ASN D N   1 
ATOM   4008 C CA  . ASN D 2 71  ? 34.719 42.581  121.540 1.00 63.50  ? 68  ASN D CA  1 
ATOM   4009 C C   . ASN D 2 71  ? 36.139 42.831  122.066 1.00 57.59  ? 68  ASN D C   1 
ATOM   4010 O O   . ASN D 2 71  ? 36.480 43.927  122.539 1.00 54.89  ? 68  ASN D O   1 
ATOM   4011 C CB  . ASN D 2 71  ? 33.931 41.660  122.467 1.00 67.65  ? 68  ASN D CB  1 
ATOM   4012 C CG  . ASN D 2 71  ? 32.433 41.735  122.203 1.00 66.86  ? 68  ASN D CG  1 
ATOM   4013 O OD1 . ASN D 2 71  ? 31.901 42.815  122.007 1.00 59.55  ? 68  ASN D OD1 1 
ATOM   4014 N ND2 . ASN D 2 71  ? 31.759 40.587  122.172 1.00 64.19  ? 68  ASN D ND2 1 
ATOM   4015 N N   . THR D 2 72  ? 36.992 41.846  121.907 1.00 47.15  ? 69  THR D N   1 
ATOM   4016 C CA  . THR D 2 72  ? 38.347 42.059  122.247 1.00 53.78  ? 69  THR D CA  1 
ATOM   4017 C C   . THR D 2 72  ? 38.896 43.331  121.634 1.00 54.98  ? 69  THR D C   1 
ATOM   4018 O O   . THR D 2 72  ? 39.661 44.030  122.280 1.00 59.47  ? 69  THR D O   1 
ATOM   4019 C CB  . THR D 2 72  ? 39.177 40.893  121.767 1.00 52.28  ? 69  THR D CB  1 
ATOM   4020 O OG1 . THR D 2 72  ? 38.457 39.717  122.057 1.00 46.20  ? 69  THR D OG1 1 
ATOM   4021 C CG2 . THR D 2 72  ? 40.544 40.847  122.460 1.00 51.15  ? 69  THR D CG2 1 
ATOM   4022 N N   . THR D 2 73  ? 38.492 43.633  120.405 1.00 55.12  ? 70  THR D N   1 
ATOM   4023 C CA  . THR D 2 73  ? 39.071 44.738  119.678 1.00 50.20  ? 70  THR D CA  1 
ATOM   4024 C C   . THR D 2 73  ? 38.567 46.031  120.257 1.00 54.20  ? 70  THR D C   1 
ATOM   4025 O O   . THR D 2 73  ? 39.329 47.016  120.346 1.00 61.42  ? 70  THR D O   1 
ATOM   4026 C CB  . THR D 2 73  ? 38.813 44.594  118.145 1.00 51.27  ? 70  THR D CB  1 
ATOM   4027 O OG1 . THR D 2 73  ? 39.646 43.537  117.630 1.00 64.02  ? 70  THR D OG1 1 
ATOM   4028 C CG2 . THR D 2 73  ? 39.221 45.825  117.399 1.00 44.84  ? 70  THR D CG2 1 
ATOM   4029 N N   . ARG D 2 74  ? 37.301 46.044  120.678 1.00 53.54  ? 71  ARG D N   1 
ATOM   4030 C CA  . ARG D 2 74  ? 36.718 47.237  121.355 1.00 65.19  ? 71  ARG D CA  1 
ATOM   4031 C C   . ARG D 2 74  ? 37.330 47.471  122.756 1.00 58.19  ? 71  ARG D C   1 
ATOM   4032 O O   . ARG D 2 74  ? 37.543 48.633  123.164 1.00 46.95  ? 71  ARG D O   1 
ATOM   4033 C CB  . ARG D 2 74  ? 35.187 47.073  121.491 1.00 76.67  ? 71  ARG D CB  1 
ATOM   4034 C CG  . ARG D 2 74  ? 34.452 48.156  122.298 1.00 92.06  ? 71  ARG D CG  1 
ATOM   4035 C CD  . ARG D 2 74  ? 33.017 47.734  122.646 1.00 99.15  ? 71  ARG D CD  1 
ATOM   4036 N NE  . ARG D 2 74  ? 32.900 46.306  123.014 1.00 104.98 ? 71  ARG D NE  1 
ATOM   4037 C CZ  . ARG D 2 74  ? 32.908 45.806  124.258 1.00 107.33 ? 71  ARG D CZ  1 
ATOM   4038 N NH1 . ARG D 2 74  ? 33.020 46.601  125.321 1.00 112.00 ? 71  ARG D NH1 1 
ATOM   4039 N NH2 . ARG D 2 74  ? 32.803 44.487  124.445 1.00 92.96  ? 71  ARG D NH2 1 
ATOM   4040 N N   . ILE D 2 75  ? 37.586 46.356  123.461 1.00 47.54  ? 72  ILE D N   1 
ATOM   4041 C CA  . ILE D 2 75  ? 38.185 46.358  124.797 1.00 48.32  ? 72  ILE D CA  1 
ATOM   4042 C C   . ILE D 2 75  ? 39.594 46.909  124.683 1.00 44.19  ? 72  ILE D C   1 
ATOM   4043 O O   . ILE D 2 75  ? 39.978 47.846  125.398 1.00 38.19  ? 72  ILE D O   1 
ATOM   4044 C CB  . ILE D 2 75  ? 38.141 44.957  125.414 1.00 52.69  ? 72  ILE D CB  1 
ATOM   4045 C CG1 . ILE D 2 75  ? 36.671 44.611  125.699 1.00 49.36  ? 72  ILE D CG1 1 
ATOM   4046 C CG2 . ILE D 2 75  ? 38.952 44.919  126.689 1.00 54.12  ? 72  ILE D CG2 1 
ATOM   4047 C CD1 . ILE D 2 75  ? 36.385 43.162  125.966 1.00 48.45  ? 72  ILE D CD1 1 
ATOM   4048 N N   . LEU D 2 76  ? 40.325 46.434  123.692 1.00 41.92  ? 73  LEU D N   1 
ATOM   4049 C CA  . LEU D 2 76  ? 41.618 47.049  123.421 1.00 45.55  ? 73  LEU D CA  1 
ATOM   4050 C C   . LEU D 2 76  ? 41.495 48.533  123.063 1.00 49.21  ? 73  LEU D C   1 
ATOM   4051 O O   . LEU D 2 76  ? 42.441 49.278  123.242 1.00 51.43  ? 73  LEU D O   1 
ATOM   4052 C CB  . LEU D 2 76  ? 42.383 46.317  122.321 1.00 41.58  ? 73  LEU D CB  1 
ATOM   4053 C CG  . LEU D 2 76  ? 42.885 44.907  122.670 1.00 44.60  ? 73  LEU D CG  1 
ATOM   4054 C CD1 . LEU D 2 76  ? 43.199 44.180  121.379 1.00 42.23  ? 73  LEU D CD1 1 
ATOM   4055 C CD2 . LEU D 2 76  ? 44.126 44.870  123.577 1.00 41.90  ? 73  LEU D CD2 1 
ATOM   4056 N N   . ASP D 2 77  ? 40.375 48.976  122.498 1.00 54.36  ? 74  ASP D N   1 
ATOM   4057 C CA  . ASP D 2 77  ? 40.320 50.400  122.072 1.00 54.07  ? 74  ASP D CA  1 
ATOM   4058 C C   . ASP D 2 77  ? 40.191 51.254  123.292 1.00 48.85  ? 74  ASP D C   1 
ATOM   4059 O O   . ASP D 2 77  ? 40.923 52.217  123.431 1.00 40.99  ? 74  ASP D O   1 
ATOM   4060 C CB  . ASP D 2 77  ? 39.165 50.686  121.113 1.00 58.66  ? 74  ASP D CB  1 
ATOM   4061 C CG  . ASP D 2 77  ? 39.396 50.095  119.729 1.00 60.77  ? 74  ASP D CG  1 
ATOM   4062 O OD1 . ASP D 2 77  ? 40.579 50.011  119.279 1.00 50.48  ? 74  ASP D OD1 1 
ATOM   4063 O OD2 . ASP D 2 77  ? 38.382 49.699  119.124 1.00 55.58  ? 74  ASP D OD2 1 
ATOM   4064 N N   . VAL D 2 78  ? 39.288 50.843  124.197 1.00 52.91  ? 75  VAL D N   1 
ATOM   4065 C CA  . VAL D 2 78  ? 39.207 51.434  125.535 1.00 51.73  ? 75  VAL D CA  1 
ATOM   4066 C C   . VAL D 2 78  ? 40.596 51.462  126.222 1.00 53.41  ? 75  VAL D C   1 
ATOM   4067 O O   . VAL D 2 78  ? 40.999 52.479  126.769 1.00 62.01  ? 75  VAL D O   1 
ATOM   4068 C CB  . VAL D 2 78  ? 38.205 50.704  126.464 1.00 56.28  ? 75  VAL D CB  1 
ATOM   4069 C CG1 . VAL D 2 78  ? 38.150 51.411  127.802 1.00 57.20  ? 75  VAL D CG1 1 
ATOM   4070 C CG2 . VAL D 2 78  ? 36.788 50.615  125.893 1.00 53.61  ? 75  VAL D CG2 1 
ATOM   4071 N N   . MET D 2 79  ? 41.360 50.380  126.148 1.00 44.65  ? 76  MET D N   1 
ATOM   4072 C CA  . MET D 2 79  ? 42.627 50.372  126.825 1.00 41.58  ? 76  MET D CA  1 
ATOM   4073 C C   . MET D 2 79  ? 43.616 51.342  126.172 1.00 44.81  ? 76  MET D C   1 
ATOM   4074 O O   . MET D 2 79  ? 44.432 51.977  126.890 1.00 52.84  ? 76  MET D O   1 
ATOM   4075 C CB  . MET D 2 79  ? 43.200 48.923  126.931 1.00 40.84  ? 76  MET D CB  1 
ATOM   4076 C CG  . MET D 2 79  ? 42.327 47.926  127.714 1.00 41.61  ? 76  MET D CG  1 
ATOM   4077 S SD  . MET D 2 79  ? 42.854 46.201  127.501 1.00 39.93  ? 76  MET D SD  1 
ATOM   4078 C CE  . MET D 2 79  ? 44.629 46.281  127.712 1.00 37.85  ? 76  MET D CE  1 
ATOM   4079 N N   . LYS D 2 80  ? 43.593 51.457  124.839 1.00 53.56  ? 77  LYS D N   1 
ATOM   4080 C CA  . LYS D 2 80  ? 44.509 52.399  124.151 1.00 60.96  ? 77  LYS D CA  1 
ATOM   4081 C C   . LYS D 2 80  ? 44.259 53.795  124.660 1.00 57.05  ? 77  LYS D C   1 
ATOM   4082 O O   . LYS D 2 80  ? 45.211 54.581  124.830 1.00 49.53  ? 77  LYS D O   1 
ATOM   4083 C CB  . LYS D 2 80  ? 44.323 52.512  122.631 1.00 65.47  ? 77  LYS D CB  1 
ATOM   4084 C CG  . LYS D 2 80  ? 45.237 53.639  122.074 1.00 73.53  ? 77  LYS D CG  1 
ATOM   4085 C CD  . LYS D 2 80  ? 45.006 54.125  120.648 1.00 86.57  ? 77  LYS D CD  1 
ATOM   4086 C CE  . LYS D 2 80  ? 43.535 54.293  120.248 1.00 91.33  ? 77  LYS D CE  1 
ATOM   4087 N NZ  . LYS D 2 80  ? 42.702 55.120  121.161 1.00 89.28  ? 77  LYS D NZ  1 
ATOM   4088 N N   . ASN D 2 81  ? 42.964 54.066  124.792 1.00 44.91  ? 78  ASN D N   1 
ATOM   4089 C CA  . ASN D 2 81  ? 42.436 55.319  125.236 1.00 55.18  ? 78  ASN D CA  1 
ATOM   4090 C C   . ASN D 2 81  ? 42.937 55.728  126.573 1.00 60.60  ? 78  ASN D C   1 
ATOM   4091 O O   . ASN D 2 81  ? 43.204 56.919  126.783 1.00 58.18  ? 78  ASN D O   1 
ATOM   4092 C CB  . ASN D 2 81  ? 40.902 55.250  125.333 1.00 56.58  ? 78  ASN D CB  1 
ATOM   4093 C CG  . ASN D 2 81  ? 40.214 55.424  123.979 1.00 64.11  ? 78  ASN D CG  1 
ATOM   4094 O OD1 . ASN D 2 81  ? 40.845 55.800  122.949 1.00 55.30  ? 78  ASN D OD1 1 
ATOM   4095 N ND2 . ASN D 2 81  ? 38.893 55.191  123.977 1.00 63.57  ? 78  ASN D ND2 1 
ATOM   4096 N N   . LYS D 2 82  ? 43.004 54.750  127.484 1.00 58.49  ? 79  LYS D N   1 
ATOM   4097 C CA  . LYS D 2 82  ? 43.367 55.012  128.856 1.00 48.69  ? 79  LYS D CA  1 
ATOM   4098 C C   . LYS D 2 82  ? 44.881 54.967  129.114 1.00 47.47  ? 79  LYS D C   1 
ATOM   4099 O O   . LYS D 2 82  ? 45.304 54.869  130.242 1.00 52.06  ? 79  LYS D O   1 
ATOM   4100 C CB  . LYS D 2 82  ? 42.722 54.007  129.751 1.00 51.46  ? 79  LYS D CB  1 
ATOM   4101 C CG  . LYS D 2 82  ? 41.233 53.813  129.634 1.00 47.56  ? 79  LYS D CG  1 
ATOM   4102 C CD  . LYS D 2 82  ? 40.903 52.786  130.713 1.00 50.02  ? 79  LYS D CD  1 
ATOM   4103 C CE  . LYS D 2 82  ? 39.444 52.478  130.827 1.00 60.01  ? 79  LYS D CE  1 
ATOM   4104 N NZ  . LYS D 2 82  ? 38.785 53.274  131.871 1.00 64.97  ? 79  LYS D NZ  1 
ATOM   4105 N N   . GLY D 2 83  ? 45.714 55.020  128.100 1.00 40.47  ? 80  GLY D N   1 
ATOM   4106 C CA  . GLY D 2 83  ? 47.138 55.082  128.371 1.00 40.71  ? 80  GLY D CA  1 
ATOM   4107 C C   . GLY D 2 83  ? 47.785 53.714  128.553 1.00 42.09  ? 80  GLY D C   1 
ATOM   4108 O O   . GLY D 2 83  ? 49.028 53.601  128.630 1.00 37.26  ? 80  GLY D O   1 
ATOM   4109 N N   . LEU D 2 84  ? 46.997 52.641  128.554 1.00 40.51  ? 81  LEU D N   1 
ATOM   4110 C CA  . LEU D 2 84  ? 47.610 51.335  128.955 1.00 38.72  ? 81  LEU D CA  1 
ATOM   4111 C C   . LEU D 2 84  ? 48.469 50.693  127.899 1.00 37.29  ? 81  LEU D C   1 
ATOM   4112 O O   . LEU D 2 84  ? 49.427 50.027  128.222 1.00 33.77  ? 81  LEU D O   1 
ATOM   4113 C CB  . LEU D 2 84  ? 46.554 50.362  129.352 1.00 34.42  ? 81  LEU D CB  1 
ATOM   4114 C CG  . LEU D 2 84  ? 45.658 50.966  130.398 1.00 32.64  ? 81  LEU D CG  1 
ATOM   4115 C CD1 . LEU D 2 84  ? 44.513 50.024  130.701 1.00 36.32  ? 81  LEU D CD1 1 
ATOM   4116 C CD2 . LEU D 2 84  ? 46.443 51.228  131.640 1.00 32.25  ? 81  LEU D CD2 1 
ATOM   4117 N N   . ILE D 2 85  ? 48.133 50.936  126.625 1.00 42.37  ? 82  ILE D N   1 
ATOM   4118 C CA  . ILE D 2 85  ? 48.785 50.298  125.483 1.00 38.46  ? 82  ILE D CA  1 
ATOM   4119 C C   . ILE D 2 85  ? 48.735 51.194  124.292 1.00 38.36  ? 82  ILE D C   1 
ATOM   4120 O O   . ILE D 2 85  ? 48.004 52.169  124.274 1.00 46.26  ? 82  ILE D O   1 
ATOM   4121 C CB  . ILE D 2 85  ? 48.046 49.033  125.056 1.00 37.20  ? 82  ILE D CB  1 
ATOM   4122 C CG1 . ILE D 2 85  ? 46.589 49.376  124.757 1.00 40.99  ? 82  ILE D CG1 1 
ATOM   4123 C CG2 . ILE D 2 85  ? 48.089 47.977  126.140 1.00 38.65  ? 82  ILE D CG2 1 
ATOM   4124 C CD1 . ILE D 2 85  ? 45.841 48.314  124.007 1.00 41.71  ? 82  ILE D CD1 1 
ATOM   4125 N N   . VAL D 2 86  ? 49.490 50.821  123.272 1.00 44.11  ? 83  VAL D N   1 
ATOM   4126 C CA  . VAL D 2 86  ? 49.368 51.414  121.939 1.00 46.11  ? 83  VAL D CA  1 
ATOM   4127 C C   . VAL D 2 86  ? 49.368 50.290  120.858 1.00 50.77  ? 83  VAL D C   1 
ATOM   4128 O O   . VAL D 2 86  ? 49.897 49.175  121.124 1.00 44.58  ? 83  VAL D O   1 
ATOM   4129 C CB  . VAL D 2 86  ? 50.551 52.377  121.704 1.00 48.53  ? 83  VAL D CB  1 
ATOM   4130 C CG1 . VAL D 2 86  ? 50.490 53.600  122.648 1.00 49.20  ? 83  VAL D CG1 1 
ATOM   4131 C CG2 . VAL D 2 86  ? 51.872 51.667  121.913 1.00 45.43  ? 83  VAL D CG2 1 
ATOM   4132 N N   . ARG D 2 87  ? 48.767 50.562  119.678 1.00 52.31  ? 84  ARG D N   1 
ATOM   4133 C CA  . ARG D 2 87  ? 48.984 49.747  118.450 1.00 51.88  ? 84  ARG D CA  1 
ATOM   4134 C C   . ARG D 2 87  ? 50.047 50.315  117.512 1.00 49.85  ? 84  ARG D C   1 
ATOM   4135 O O   . ARG D 2 87  ? 50.015 51.474  117.182 1.00 54.06  ? 84  ARG D O   1 
ATOM   4136 C CB  . ARG D 2 87  ? 47.788 49.677  117.552 1.00 50.98  ? 84  ARG D CB  1 
ATOM   4137 C CG  . ARG D 2 87  ? 46.449 49.717  118.185 1.00 57.05  ? 84  ARG D CG  1 
ATOM   4138 C CD  . ARG D 2 87  ? 45.449 49.241  117.124 1.00 55.85  ? 84  ARG D CD  1 
ATOM   4139 N NE  . ARG D 2 87  ? 44.422 48.464  117.785 1.00 50.10  ? 84  ARG D NE  1 
ATOM   4140 C CZ  . ARG D 2 87  ? 43.405 49.012  118.409 1.00 42.07  ? 84  ARG D CZ  1 
ATOM   4141 N NH1 . ARG D 2 87  ? 43.308 50.303  118.414 1.00 39.84  ? 84  ARG D NH1 1 
ATOM   4142 N NH2 . ARG D 2 87  ? 42.479 48.266  119.003 1.00 47.14  ? 84  ARG D NH2 1 
ATOM   4143 N N   . LYS D 2 88  ? 50.935 49.470  117.047 1.00 45.92  ? 85  LYS D N   1 
ATOM   4144 C CA  . LYS D 2 88  ? 51.848 49.815  116.006 1.00 50.11  ? 85  LYS D CA  1 
ATOM   4145 C C   . LYS D 2 88  ? 51.618 48.848  114.859 1.00 53.46  ? 85  LYS D C   1 
ATOM   4146 O O   . LYS D 2 88  ? 51.467 47.642  115.060 1.00 53.33  ? 85  LYS D O   1 
ATOM   4147 C CB  . LYS D 2 88  ? 53.291 49.642  116.463 1.00 54.45  ? 85  LYS D CB  1 
ATOM   4148 C CG  . LYS D 2 88  ? 53.632 50.322  117.775 1.00 63.05  ? 85  LYS D CG  1 
ATOM   4149 C CD  . LYS D 2 88  ? 53.757 51.834  117.713 1.00 65.72  ? 85  LYS D CD  1 
ATOM   4150 C CE  . LYS D 2 88  ? 54.501 52.389  118.937 1.00 69.83  ? 85  LYS D CE  1 
ATOM   4151 N NZ  . LYS D 2 88  ? 55.843 51.746  119.114 1.00 68.55  ? 85  LYS D NZ  1 
ATOM   4152 N N   . VAL D 2 89  ? 51.605 49.380  113.650 1.00 55.17  ? 86  VAL D N   1 
ATOM   4153 C CA  . VAL D 2 89  ? 51.554 48.546  112.478 1.00 48.18  ? 86  VAL D CA  1 
ATOM   4154 C C   . VAL D 2 89  ? 52.791 47.710  112.502 1.00 43.91  ? 86  VAL D C   1 
ATOM   4155 O O   . VAL D 2 89  ? 53.854 48.231  112.714 1.00 43.76  ? 86  VAL D O   1 
ATOM   4156 C CB  . VAL D 2 89  ? 51.526 49.382  111.189 1.00 46.43  ? 86  VAL D CB  1 
ATOM   4157 C CG1 . VAL D 2 89  ? 51.886 48.520  109.981 1.00 48.33  ? 86  VAL D CG1 1 
ATOM   4158 C CG2 . VAL D 2 89  ? 50.150 50.029  111.034 1.00 41.81  ? 86  VAL D CG2 1 
ATOM   4159 N N   . ASP D 2 90  ? 52.636 46.402  112.302 1.00 44.78  ? 87  ASP D N   1 
ATOM   4160 C CA  . ASP D 2 90  ? 53.790 45.491  112.116 1.00 50.92  ? 87  ASP D CA  1 
ATOM   4161 C C   . ASP D 2 90  ? 54.418 45.825  110.734 1.00 55.17  ? 87  ASP D C   1 
ATOM   4162 O O   . ASP D 2 90  ? 53.719 45.885  109.732 1.00 58.06  ? 87  ASP D O   1 
ATOM   4163 C CB  . ASP D 2 90  ? 53.255 44.062  112.175 1.00 51.01  ? 87  ASP D CB  1 
ATOM   4164 C CG  . ASP D 2 90  ? 54.337 42.982  112.333 1.00 56.28  ? 87  ASP D CG  1 
ATOM   4165 O OD1 . ASP D 2 90  ? 55.502 43.148  111.890 1.00 59.93  ? 87  ASP D OD1 1 
ATOM   4166 O OD2 . ASP D 2 90  ? 53.965 41.911  112.898 1.00 54.47  ? 87  ASP D OD2 1 
ATOM   4167 N N   . VAL D 2 91  ? 55.716 46.061  110.673 1.00 55.44  ? 88  VAL D N   1 
ATOM   4168 C CA  . VAL D 2 91  ? 56.348 46.484  109.418 1.00 57.30  ? 88  VAL D CA  1 
ATOM   4169 C C   . VAL D 2 91  ? 56.634 45.284  108.526 1.00 57.75  ? 88  VAL D C   1 
ATOM   4170 O O   . VAL D 2 91  ? 56.659 45.371  107.276 1.00 54.96  ? 88  VAL D O   1 
ATOM   4171 C CB  . VAL D 2 91  ? 57.646 47.282  109.697 1.00 61.97  ? 88  VAL D CB  1 
ATOM   4172 C CG1 . VAL D 2 91  ? 58.267 47.767  108.389 1.00 67.88  ? 88  VAL D CG1 1 
ATOM   4173 C CG2 . VAL D 2 91  ? 57.346 48.475  110.618 1.00 60.10  ? 88  VAL D CG2 1 
ATOM   4174 N N   . LYS D 2 92  ? 56.869 44.158  109.169 1.00 60.09  ? 89  LYS D N   1 
ATOM   4175 C CA  . LYS D 2 92  ? 57.175 42.951  108.441 1.00 66.71  ? 89  LYS D CA  1 
ATOM   4176 C C   . LYS D 2 92  ? 55.876 42.315  107.958 1.00 60.33  ? 89  LYS D C   1 
ATOM   4177 O O   . LYS D 2 92  ? 55.915 41.495  107.051 1.00 60.81  ? 89  LYS D O   1 
ATOM   4178 C CB  . LYS D 2 92  ? 58.000 41.982  109.300 1.00 82.63  ? 89  LYS D CB  1 
ATOM   4179 C CG  . LYS D 2 92  ? 59.433 42.468  109.607 1.00 100.71 ? 89  LYS D CG  1 
ATOM   4180 C CD  . LYS D 2 92  ? 59.841 42.274  111.083 1.00 112.46 ? 89  LYS D CD  1 
ATOM   4181 C CE  . LYS D 2 92  ? 59.181 43.294  112.030 1.00 119.60 ? 89  LYS D CE  1 
ATOM   4182 N NZ  . LYS D 2 92  ? 58.515 42.682  113.229 1.00 118.31 ? 89  LYS D NZ  1 
ATOM   4183 N N   . ASP D 2 93  ? 54.728 42.715  108.513 1.00 53.32  ? 90  ASP D N   1 
ATOM   4184 C CA  . ASP D 2 93  ? 53.482 42.085  108.124 1.00 47.53  ? 90  ASP D CA  1 
ATOM   4185 C C   . ASP D 2 93  ? 52.380 43.072  108.318 1.00 47.82  ? 90  ASP D C   1 
ATOM   4186 O O   . ASP D 2 93  ? 51.766 43.161  109.392 1.00 52.57  ? 90  ASP D O   1 
ATOM   4187 C CB  . ASP D 2 93  ? 53.265 40.784  108.898 1.00 43.22  ? 90  ASP D CB  1 
ATOM   4188 C CG  . ASP D 2 93  ? 51.974 40.048  108.501 1.00 46.27  ? 90  ASP D CG  1 
ATOM   4189 O OD1 . ASP D 2 93  ? 51.082 40.602  107.800 1.00 36.34  ? 90  ASP D OD1 1 
ATOM   4190 O OD2 . ASP D 2 93  ? 51.850 38.870  108.928 1.00 44.12  ? 90  ASP D OD2 1 
ATOM   4191 N N   . ARG D 2 94  ? 52.092 43.814  107.245 1.00 44.90  ? 91  ARG D N   1 
ATOM   4192 C CA  . ARG D 2 94  ? 51.243 45.018  107.351 1.00 38.59  ? 91  ARG D CA  1 
ATOM   4193 C C   . ARG D 2 94  ? 49.823 44.647  107.623 1.00 37.87  ? 91  ARG D C   1 
ATOM   4194 O O   . ARG D 2 94  ? 48.973 45.518  107.803 1.00 37.83  ? 91  ARG D O   1 
ATOM   4195 C CB  . ARG D 2 94  ? 51.316 45.889  106.101 1.00 42.73  ? 91  ARG D CB  1 
ATOM   4196 C CG  . ARG D 2 94  ? 52.715 46.139  105.557 1.00 51.71  ? 91  ARG D CG  1 
ATOM   4197 C CD  . ARG D 2 94  ? 53.546 47.219  106.223 1.00 54.78  ? 91  ARG D CD  1 
ATOM   4198 N NE  . ARG D 2 94  ? 54.164 48.117  105.209 1.00 57.84  ? 91  ARG D NE  1 
ATOM   4199 C CZ  . ARG D 2 94  ? 55.457 48.188  104.931 1.00 58.61  ? 91  ARG D CZ  1 
ATOM   4200 N NH1 . ARG D 2 94  ? 56.333 47.449  105.582 1.00 69.58  ? 91  ARG D NH1 1 
ATOM   4201 N NH2 . ARG D 2 94  ? 55.885 49.018  104.001 1.00 69.92  ? 91  ARG D NH2 1 
ATOM   4202 N N   . ARG D 2 95  ? 49.521 43.348  107.597 1.00 43.85  ? 92  ARG D N   1 
ATOM   4203 C CA  . ARG D 2 95  ? 48.193 42.908  107.980 1.00 43.80  ? 92  ARG D CA  1 
ATOM   4204 C C   . ARG D 2 95  ? 47.982 43.043  109.509 1.00 42.41  ? 92  ARG D C   1 
ATOM   4205 O O   . ARG D 2 95  ? 46.862 43.045  109.947 1.00 44.20  ? 92  ARG D O   1 
ATOM   4206 C CB  . ARG D 2 95  ? 47.931 41.450  107.604 1.00 43.80  ? 92  ARG D CB  1 
ATOM   4207 C CG  . ARG D 2 95  ? 48.037 41.059  106.147 1.00 46.82  ? 92  ARG D CG  1 
ATOM   4208 C CD  . ARG D 2 95  ? 49.182 40.053  106.031 1.00 49.64  ? 92  ARG D CD  1 
ATOM   4209 N NE  . ARG D 2 95  ? 48.684 38.715  105.886 1.00 46.85  ? 92  ARG D NE  1 
ATOM   4210 C CZ  . ARG D 2 95  ? 49.326 37.613  106.181 1.00 40.26  ? 92  ARG D CZ  1 
ATOM   4211 N NH1 . ARG D 2 95  ? 50.500 37.600  106.759 1.00 42.48  ? 92  ARG D NH1 1 
ATOM   4212 N NH2 . ARG D 2 95  ? 48.724 36.487  105.933 1.00 49.92  ? 92  ARG D NH2 1 
ATOM   4213 N N   . LYS D 2 96  ? 49.040 43.105  110.305 1.00 43.87  ? 93  LYS D N   1 
ATOM   4214 C CA  . LYS D 2 96  ? 48.912 42.970  111.740 1.00 50.41  ? 93  LYS D CA  1 
ATOM   4215 C C   . LYS D 2 96  ? 49.218 44.274  112.499 1.00 51.69  ? 93  LYS D C   1 
ATOM   4216 O O   . LYS D 2 96  ? 50.055 45.050  112.075 1.00 52.50  ? 93  LYS D O   1 
ATOM   4217 C CB  . LYS D 2 96  ? 49.909 41.944  112.210 1.00 55.41  ? 93  LYS D CB  1 
ATOM   4218 C CG  . LYS D 2 96  ? 49.625 40.526  111.764 1.00 62.09  ? 93  LYS D CG  1 
ATOM   4219 C CD  . LYS D 2 96  ? 50.797 39.629  112.186 1.00 64.26  ? 93  LYS D CD  1 
ATOM   4220 C CE  . LYS D 2 96  ? 50.516 38.130  112.057 1.00 63.77  ? 93  LYS D CE  1 
ATOM   4221 N NZ  . LYS D 2 96  ? 49.677 37.824  110.863 1.00 63.07  ? 93  LYS D NZ  1 
ATOM   4222 N N   . PHE D 2 97  ? 48.544 44.479  113.624 1.00 51.74  ? 94  PHE D N   1 
ATOM   4223 C CA  . PHE D 2 97  ? 48.995 45.408  114.650 1.00 49.76  ? 94  PHE D CA  1 
ATOM   4224 C C   . PHE D 2 97  ? 49.668 44.661  115.802 1.00 50.96  ? 94  PHE D C   1 
ATOM   4225 O O   . PHE D 2 97  ? 49.164 43.615  116.254 1.00 53.20  ? 94  PHE D O   1 
ATOM   4226 C CB  . PHE D 2 97  ? 47.826 46.152  115.254 1.00 48.54  ? 94  PHE D CB  1 
ATOM   4227 C CG  . PHE D 2 97  ? 47.034 46.909  114.287 1.00 47.23  ? 94  PHE D CG  1 
ATOM   4228 C CD1 . PHE D 2 97  ? 47.583 47.970  113.623 1.00 52.23  ? 94  PHE D CD1 1 
ATOM   4229 C CD2 . PHE D 2 97  ? 45.698 46.612  114.091 1.00 51.47  ? 94  PHE D CD2 1 
ATOM   4230 C CE1 . PHE D 2 97  ? 46.826 48.677  112.703 1.00 58.87  ? 94  PHE D CE1 1 
ATOM   4231 C CE2 . PHE D 2 97  ? 44.921 47.319  113.196 1.00 53.85  ? 94  PHE D CE2 1 
ATOM   4232 C CZ  . PHE D 2 97  ? 45.492 48.345  112.481 1.00 61.08  ? 94  PHE D CZ  1 
ATOM   4233 N N   . GLN D 2 98  ? 50.767 45.214  116.306 1.00 46.51  ? 95  GLN D N   1 
ATOM   4234 C CA  . GLN D 2 98  ? 51.376 44.711  117.536 1.00 47.30  ? 95  GLN D CA  1 
ATOM   4235 C C   . GLN D 2 98  ? 50.833 45.586  118.696 1.00 50.25  ? 95  GLN D C   1 
ATOM   4236 O O   . GLN D 2 98  ? 50.635 46.826  118.550 1.00 50.99  ? 95  GLN D O   1 
ATOM   4237 C CB  . GLN D 2 98  ? 52.894 44.727  117.435 1.00 52.47  ? 95  GLN D CB  1 
ATOM   4238 C CG  . GLN D 2 98  ? 53.446 43.708  116.419 1.00 58.48  ? 95  GLN D CG  1 
ATOM   4239 C CD  . GLN D 2 98  ? 54.935 43.833  116.028 1.00 62.31  ? 95  GLN D CD  1 
ATOM   4240 O OE1 . GLN D 2 98  ? 55.519 42.891  115.497 1.00 72.39  ? 95  GLN D OE1 1 
ATOM   4241 N NE2 . GLN D 2 98  ? 55.526 45.000  116.224 1.00 70.84  ? 95  GLN D NE2 1 
ATOM   4242 N N   . ILE D 2 99  ? 50.485 44.927  119.806 1.00 49.12  ? 96  ILE D N   1 
ATOM   4243 C CA  . ILE D 2 99  ? 49.987 45.607  121.009 1.00 44.05  ? 96  ILE D CA  1 
ATOM   4244 C C   . ILE D 2 99  ? 51.151 45.716  121.967 1.00 43.36  ? 96  ILE D C   1 
ATOM   4245 O O   . ILE D 2 99  ? 51.776 44.709  122.289 1.00 45.31  ? 96  ILE D O   1 
ATOM   4246 C CB  . ILE D 2 99  ? 48.837 44.861  121.647 1.00 46.73  ? 96  ILE D CB  1 
ATOM   4247 C CG1 . ILE D 2 99  ? 47.734 44.565  120.617 1.00 52.64  ? 96  ILE D CG1 1 
ATOM   4248 C CG2 . ILE D 2 99  ? 48.255 45.661  122.808 1.00 48.53  ? 96  ILE D CG2 1 
ATOM   4249 C CD1 . ILE D 2 99  ? 47.121 45.796  119.970 1.00 58.62  ? 96  ILE D CD1 1 
ATOM   4250 N N   . PHE D 2 100 ? 51.521 46.950  122.319 1.00 42.24  ? 97  PHE D N   1 
ATOM   4251 C CA  . PHE D 2 100 ? 52.665 47.197  123.232 1.00 42.60  ? 97  PHE D CA  1 
ATOM   4252 C C   . PHE D 2 100 ? 52.137 47.877  124.483 1.00 42.44  ? 97  PHE D C   1 
ATOM   4253 O O   . PHE D 2 100 ? 51.248 48.767  124.402 1.00 42.07  ? 97  PHE D O   1 
ATOM   4254 C CB  . PHE D 2 100 ? 53.710 48.108  122.593 1.00 39.27  ? 97  PHE D CB  1 
ATOM   4255 C CG  . PHE D 2 100 ? 54.497 47.462  121.500 1.00 40.62  ? 97  PHE D CG  1 
ATOM   4256 C CD1 . PHE D 2 100 ? 55.593 46.662  121.795 1.00 41.95  ? 97  PHE D CD1 1 
ATOM   4257 C CD2 . PHE D 2 100 ? 54.157 47.661  120.177 1.00 44.69  ? 97  PHE D CD2 1 
ATOM   4258 C CE1 . PHE D 2 100 ? 56.308 46.044  120.788 1.00 44.01  ? 97  PHE D CE1 1 
ATOM   4259 C CE2 . PHE D 2 100 ? 54.880 47.046  119.145 1.00 46.82  ? 97  PHE D CE2 1 
ATOM   4260 C CZ  . PHE D 2 100 ? 55.956 46.230  119.454 1.00 42.46  ? 97  PHE D CZ  1 
ATOM   4261 N N   . LEU D 2 101 ? 52.633 47.450  125.635 1.00 39.89  ? 98  LEU D N   1 
ATOM   4262 C CA  . LEU D 2 101 ? 52.371 48.194  126.894 1.00 39.58  ? 98  LEU D CA  1 
ATOM   4263 C C   . LEU D 2 101 ? 52.916 49.629  126.822 1.00 39.11  ? 98  LEU D C   1 
ATOM   4264 O O   . LEU D 2 101 ? 54.028 49.835  126.403 1.00 31.43  ? 98  LEU D O   1 
ATOM   4265 C CB  . LEU D 2 101 ? 53.095 47.489  128.028 1.00 39.05  ? 98  LEU D CB  1 
ATOM   4266 C CG  . LEU D 2 101 ? 52.367 46.208  128.411 1.00 42.52  ? 98  LEU D CG  1 
ATOM   4267 C CD1 . LEU D 2 101 ? 53.318 45.304  129.170 1.00 42.96  ? 98  LEU D CD1 1 
ATOM   4268 C CD2 . LEU D 2 101 ? 51.073 46.506  129.168 1.00 41.35  ? 98  LEU D CD2 1 
ATOM   4269 N N   . THR D 2 102 ? 52.167 50.621  127.245 1.00 39.79  ? 99  THR D N   1 
ATOM   4270 C CA  . THR D 2 102 ? 52.853 51.882  127.602 1.00 46.07  ? 99  THR D CA  1 
ATOM   4271 C C   . THR D 2 102 ? 53.640 51.717  128.923 1.00 47.59  ? 99  THR D C   1 
ATOM   4272 O O   . THR D 2 102 ? 53.543 50.674  129.607 1.00 44.46  ? 99  THR D O   1 
ATOM   4273 C CB  . THR D 2 102 ? 51.854 53.003  127.828 1.00 43.74  ? 99  THR D CB  1 
ATOM   4274 O OG1 . THR D 2 102 ? 51.035 52.674  128.963 1.00 37.22  ? 99  THR D OG1 1 
ATOM   4275 C CG2 . THR D 2 102 ? 51.023 53.097  126.608 1.00 45.21  ? 99  THR D CG2 1 
ATOM   4276 N N   . ASP D 2 103 ? 54.378 52.761  129.293 1.00 44.95  ? 100 ASP D N   1 
ATOM   4277 C CA  . ASP D 2 103 ? 55.066 52.801  130.595 1.00 45.45  ? 100 ASP D CA  1 
ATOM   4278 C C   . ASP D 2 103 ? 54.040 52.633  131.704 1.00 41.71  ? 100 ASP D C   1 
ATOM   4279 O O   . ASP D 2 103 ? 54.270 51.871  132.612 1.00 39.23  ? 100 ASP D O   1 
ATOM   4280 C CB  . ASP D 2 103 ? 55.812 54.121  130.797 1.00 48.94  ? 100 ASP D CB  1 
ATOM   4281 C CG  . ASP D 2 103 ? 57.159 54.147  130.094 1.00 53.17  ? 100 ASP D CG  1 
ATOM   4282 O OD1 . ASP D 2 103 ? 57.601 53.098  129.570 1.00 61.86  ? 100 ASP D OD1 1 
ATOM   4283 O OD2 . ASP D 2 103 ? 57.782 55.212  130.084 1.00 60.31  ? 100 ASP D OD2 1 
ATOM   4284 N N   . LEU D 2 104 ? 52.883 53.283  131.552 1.00 35.98  ? 101 LEU D N   1 
ATOM   4285 C CA  . LEU D 2 104 ? 51.825 53.180  132.490 1.00 35.70  ? 101 LEU D CA  1 
ATOM   4286 C C   . LEU D 2 104 ? 51.320 51.722  132.621 1.00 46.37  ? 101 LEU D C   1 
ATOM   4287 O O   . LEU D 2 104 ? 51.133 51.223  133.733 1.00 43.28  ? 101 LEU D O   1 
ATOM   4288 C CB  . LEU D 2 104 ? 50.690 54.078  132.089 1.00 34.19  ? 101 LEU D CB  1 
ATOM   4289 C CG  . LEU D 2 104 ? 49.421 53.841  132.899 1.00 41.05  ? 101 LEU D CG  1 
ATOM   4290 C CD1 . LEU D 2 104 ? 49.696 54.052  134.373 1.00 44.67  ? 101 LEU D CD1 1 
ATOM   4291 C CD2 . LEU D 2 104 ? 48.394 54.858  132.450 1.00 40.51  ? 101 LEU D CD2 1 
ATOM   4292 N N   . GLY D 2 105 ? 51.139 51.044  131.488 1.00 46.97  ? 102 GLY D N   1 
ATOM   4293 C CA  . GLY D 2 105 ? 50.736 49.644  131.492 1.00 40.76  ? 102 GLY D CA  1 
ATOM   4294 C C   . GLY D 2 105 ? 51.747 48.763  132.155 1.00 37.03  ? 102 GLY D C   1 
ATOM   4295 O O   . GLY D 2 105 ? 51.375 47.876  132.833 1.00 39.54  ? 102 GLY D O   1 
ATOM   4296 N N   . ARG D 2 106 ? 53.026 49.011  131.985 1.00 43.59  ? 103 ARG D N   1 
ATOM   4297 C CA  . ARG D 2 106 ? 54.067 48.193  132.647 1.00 48.41  ? 103 ARG D CA  1 
ATOM   4298 C C   . ARG D 2 106 ? 54.020 48.283  134.187 1.00 46.88  ? 103 ARG D C   1 
ATOM   4299 O O   . ARG D 2 106 ? 54.152 47.329  134.917 1.00 50.60  ? 103 ARG D O   1 
ATOM   4300 C CB  . ARG D 2 106 ? 55.444 48.620  132.178 1.00 49.32  ? 103 ARG D CB  1 
ATOM   4301 C CG  . ARG D 2 106 ? 56.110 47.591  131.282 1.00 64.68  ? 103 ARG D CG  1 
ATOM   4302 C CD  . ARG D 2 106 ? 57.547 47.959  131.001 1.00 68.15  ? 103 ARG D CD  1 
ATOM   4303 N NE  . ARG D 2 106 ? 57.540 49.122  130.129 1.00 79.47  ? 103 ARG D NE  1 
ATOM   4304 C CZ  . ARG D 2 106 ? 57.456 49.049  128.814 1.00 81.52  ? 103 ARG D CZ  1 
ATOM   4305 N NH1 . ARG D 2 106 ? 57.406 47.851  128.231 1.00 88.05  ? 103 ARG D NH1 1 
ATOM   4306 N NH2 . ARG D 2 106 ? 57.426 50.174  128.093 1.00 83.49  ? 103 ARG D NH2 1 
ATOM   4307 N N   . GLU D 2 107 ? 53.769 49.466  134.645 1.00 45.49  ? 104 GLU D N   1 
ATOM   4308 C CA  . GLU D 2 107 ? 53.912 49.790  136.020 1.00 48.49  ? 104 GLU D CA  1 
ATOM   4309 C C   . GLU D 2 107 ? 52.740 49.259  136.844 1.00 46.55  ? 104 GLU D C   1 
ATOM   4310 O O   . GLU D 2 107 ? 52.912 48.905  138.011 1.00 59.90  ? 104 GLU D O   1 
ATOM   4311 C CB  . GLU D 2 107 ? 54.095 51.328  136.072 1.00 49.30  ? 104 GLU D CB  1 
ATOM   4312 C CG  . GLU D 2 107 ? 53.526 52.084  137.241 1.00 60.86  ? 104 GLU D CG  1 
ATOM   4313 C CD  . GLU D 2 107 ? 53.695 53.587  137.068 1.00 69.23  ? 104 GLU D CD  1 
ATOM   4314 O OE1 . GLU D 2 107 ? 53.874 54.241  138.119 1.00 63.00  ? 104 GLU D OE1 1 
ATOM   4315 O OE2 . GLU D 2 107 ? 53.652 54.102  135.897 1.00 73.84  ? 104 GLU D OE2 1 
ATOM   4316 N N   . LEU D 2 108 ? 51.550 49.199  136.252 1.00 40.24  ? 105 LEU D N   1 
ATOM   4317 C CA  . LEU D 2 108 ? 50.365 48.694  136.944 1.00 35.51  ? 105 LEU D CA  1 
ATOM   4318 C C   . LEU D 2 108 ? 50.355 47.204  137.319 1.00 33.88  ? 105 LEU D C   1 
ATOM   4319 O O   . LEU D 2 108 ? 49.496 46.790  138.068 1.00 40.09  ? 105 LEU D O   1 
ATOM   4320 C CB  . LEU D 2 108 ? 49.175 48.996  136.106 1.00 40.35  ? 105 LEU D CB  1 
ATOM   4321 C CG  . LEU D 2 108 ? 48.377 50.281  136.376 1.00 45.89  ? 105 LEU D CG  1 
ATOM   4322 C CD1 . LEU D 2 108 ? 49.145 51.326  137.168 1.00 45.55  ? 105 LEU D CD1 1 
ATOM   4323 C CD2 . LEU D 2 108 ? 47.858 50.801  135.039 1.00 44.66  ? 105 LEU D CD2 1 
ATOM   4324 N N   . GLU D 2 109 ? 51.330 46.438  136.822 1.00 38.36  ? 106 GLU D N   1 
ATOM   4325 C CA  . GLU D 2 109 ? 51.520 45.028  137.125 1.00 46.32  ? 106 GLU D CA  1 
ATOM   4326 C C   . GLU D 2 109 ? 51.486 44.738  138.601 1.00 46.13  ? 106 GLU D C   1 
ATOM   4327 O O   . GLU D 2 109 ? 50.654 43.959  139.041 1.00 48.92  ? 106 GLU D O   1 
ATOM   4328 C CB  . GLU D 2 109 ? 52.837 44.464  136.530 1.00 44.64  ? 106 GLU D CB  1 
ATOM   4329 C CG  . GLU D 2 109 ? 52.900 42.941  136.627 1.00 44.26  ? 106 GLU D CG  1 
ATOM   4330 C CD  . GLU D 2 109 ? 54.096 42.268  135.899 1.00 45.58  ? 106 GLU D CD  1 
ATOM   4331 O OE1 . GLU D 2 109 ? 54.964 42.924  135.293 1.00 51.20  ? 106 GLU D OE1 1 
ATOM   4332 O OE2 . GLU D 2 109 ? 54.202 41.032  135.962 1.00 47.42  ? 106 GLU D OE2 1 
ATOM   4333 N N   . GLU D 2 110 ? 52.394 45.348  139.354 1.00 50.15  ? 107 GLU D N   1 
ATOM   4334 C CA  . GLU D 2 110 ? 52.522 45.042  140.796 1.00 51.32  ? 107 GLU D CA  1 
ATOM   4335 C C   . GLU D 2 110 ? 51.207 45.350  141.527 1.00 43.95  ? 107 GLU D C   1 
ATOM   4336 O O   . GLU D 2 110 ? 50.609 44.449  142.139 1.00 55.63  ? 107 GLU D O   1 
ATOM   4337 C CB  . GLU D 2 110 ? 53.776 45.743  141.430 1.00 56.47  ? 107 GLU D CB  1 
ATOM   4338 C CG  . GLU D 2 110 ? 54.144 45.326  142.870 1.00 63.48  ? 107 GLU D CG  1 
ATOM   4339 C CD  . GLU D 2 110 ? 53.329 46.059  143.954 1.00 71.34  ? 107 GLU D CD  1 
ATOM   4340 O OE1 . GLU D 2 110 ? 52.935 47.243  143.744 1.00 68.08  ? 107 GLU D OE1 1 
ATOM   4341 O OE2 . GLU D 2 110 ? 53.064 45.446  145.025 1.00 78.56  ? 107 GLU D OE2 1 
ATOM   4342 N N   . PRO D 2 111 ? 50.726 46.595  141.442 1.00 36.18  ? 108 PRO D N   1 
ATOM   4343 C CA  . PRO D 2 111 ? 49.499 46.918  142.175 1.00 37.56  ? 108 PRO D CA  1 
ATOM   4344 C C   . PRO D 2 111 ? 48.256 46.244  141.719 1.00 38.45  ? 108 PRO D C   1 
ATOM   4345 O O   . PRO D 2 111 ? 47.380 45.943  142.551 1.00 47.49  ? 108 PRO D O   1 
ATOM   4346 C CB  . PRO D 2 111 ? 49.321 48.449  141.931 1.00 41.40  ? 108 PRO D CB  1 
ATOM   4347 C CG  . PRO D 2 111 ? 50.152 48.775  140.728 1.00 38.20  ? 108 PRO D CG  1 
ATOM   4348 C CD  . PRO D 2 111 ? 51.297 47.778  140.752 1.00 37.19  ? 108 PRO D CD  1 
ATOM   4349 N N   . LEU D 2 112 ? 48.108 46.035  140.410 1.00 37.87  ? 109 LEU D N   1 
ATOM   4350 C CA  . LEU D 2 112 ? 46.872 45.370  139.992 1.00 37.67  ? 109 LEU D CA  1 
ATOM   4351 C C   . LEU D 2 112 ? 46.937 43.916  140.422 1.00 30.52  ? 109 LEU D C   1 
ATOM   4352 O O   . LEU D 2 112 ? 45.936 43.374  140.868 1.00 29.45  ? 109 LEU D O   1 
ATOM   4353 C CB  . LEU D 2 112 ? 46.538 45.559  138.518 1.00 37.29  ? 109 LEU D CB  1 
ATOM   4354 C CG  . LEU D 2 112 ? 46.151 46.998  138.081 1.00 37.90  ? 109 LEU D CG  1 
ATOM   4355 C CD1 . LEU D 2 112 ? 45.907 47.030  136.564 1.00 37.84  ? 109 LEU D CD1 1 
ATOM   4356 C CD2 . LEU D 2 112 ? 44.906 47.467  138.809 1.00 35.40  ? 109 LEU D CD2 1 
ATOM   4357 N N   . ASN D 2 113 ? 48.105 43.306  140.380 1.00 32.17  ? 110 ASN D N   1 
ATOM   4358 C CA  . ASN D 2 113 ? 48.215 41.921  140.865 1.00 36.66  ? 110 ASN D CA  1 
ATOM   4359 C C   . ASN D 2 113 ? 47.997 41.839  142.390 1.00 40.15  ? 110 ASN D C   1 
ATOM   4360 O O   . ASN D 2 113 ? 47.413 40.878  142.881 1.00 42.64  ? 110 ASN D O   1 
ATOM   4361 C CB  . ASN D 2 113 ? 49.536 41.335  140.471 1.00 33.65  ? 110 ASN D CB  1 
ATOM   4362 C CG  . ASN D 2 113 ? 49.556 40.874  139.010 1.00 37.98  ? 110 ASN D CG  1 
ATOM   4363 O OD1 . ASN D 2 113 ? 48.509 40.601  138.341 1.00 35.56  ? 110 ASN D OD1 1 
ATOM   4364 N ND2 . ASN D 2 113 ? 50.743 40.733  138.516 1.00 35.83  ? 110 ASN D ND2 1 
ATOM   4365 N N   . GLU D 2 114 ? 48.374 42.893  143.116 1.00 42.13  ? 111 GLU D N   1 
ATOM   4366 C CA  . GLU D 2 114 ? 48.161 42.928  144.552 1.00 44.19  ? 111 GLU D CA  1 
ATOM   4367 C C   . GLU D 2 114 ? 46.702 42.889  144.809 1.00 41.97  ? 111 GLU D C   1 
ATOM   4368 O O   . GLU D 2 114 ? 46.234 42.058  145.600 1.00 42.08  ? 111 GLU D O   1 
ATOM   4369 C CB  . GLU D 2 114 ? 48.791 44.164  145.210 1.00 55.53  ? 111 GLU D CB  1 
ATOM   4370 C CG  . GLU D 2 114 ? 49.988 43.884  146.094 1.00 67.36  ? 111 GLU D CG  1 
ATOM   4371 C CD  . GLU D 2 114 ? 49.548 43.273  147.408 1.00 77.86  ? 111 GLU D CD  1 
ATOM   4372 O OE1 . GLU D 2 114 ? 49.966 42.131  147.731 1.00 74.26  ? 111 GLU D OE1 1 
ATOM   4373 O OE2 . GLU D 2 114 ? 48.740 43.929  148.090 1.00 82.18  ? 111 GLU D OE2 1 
ATOM   4374 N N   . ILE D 2 115 ? 45.955 43.765  144.144 1.00 41.11  ? 112 ILE D N   1 
ATOM   4375 C CA  . ILE D 2 115 ? 44.501 43.789  144.396 1.00 41.45  ? 112 ILE D CA  1 
ATOM   4376 C C   . ILE D 2 115 ? 43.826 42.489  143.962 1.00 41.16  ? 112 ILE D C   1 
ATOM   4377 O O   . ILE D 2 115 ? 42.965 41.998  144.659 1.00 48.12  ? 112 ILE D O   1 
ATOM   4378 C CB  . ILE D 2 115 ? 43.839 44.972  143.688 1.00 42.72  ? 112 ILE D CB  1 
ATOM   4379 C CG1 . ILE D 2 115 ? 44.300 46.254  144.328 1.00 45.23  ? 112 ILE D CG1 1 
ATOM   4380 C CG2 . ILE D 2 115 ? 42.323 44.875  143.745 1.00 37.29  ? 112 ILE D CG2 1 
ATOM   4381 C CD1 . ILE D 2 115 ? 44.193 47.468  143.456 1.00 54.19  ? 112 ILE D CD1 1 
ATOM   4382 N N   . ALA D 2 116 ? 44.236 41.899  142.846 1.00 40.80  ? 113 ALA D N   1 
ATOM   4383 C CA  . ALA D 2 116 ? 43.545 40.676  142.380 1.00 44.09  ? 113 ALA D CA  1 
ATOM   4384 C C   . ALA D 2 116 ? 43.815 39.509  143.321 1.00 41.78  ? 113 ALA D C   1 
ATOM   4385 O O   . ALA D 2 116 ? 42.957 38.684  143.558 1.00 38.76  ? 113 ALA D O   1 
ATOM   4386 C CB  . ALA D 2 116 ? 43.963 40.289  140.972 1.00 43.84  ? 113 ALA D CB  1 
ATOM   4387 N N   . SER D 2 117 ? 45.018 39.472  143.851 1.00 40.72  ? 114 SER D N   1 
ATOM   4388 C CA  . SER D 2 117 ? 45.416 38.471  144.800 1.00 41.93  ? 114 SER D CA  1 
ATOM   4389 C C   . SER D 2 117 ? 44.614 38.560  146.069 1.00 42.24  ? 114 SER D C   1 
ATOM   4390 O O   . SER D 2 117 ? 44.104 37.572  146.587 1.00 51.21  ? 114 SER D O   1 
ATOM   4391 C CB  . SER D 2 117 ? 46.879 38.713  145.160 1.00 47.54  ? 114 SER D CB  1 
ATOM   4392 O OG  . SER D 2 117 ? 47.438 37.565  145.728 1.00 51.75  ? 114 SER D OG  1 
ATOM   4393 N N   . ILE D 2 118 ? 44.508 39.753  146.606 1.00 44.12  ? 115 ILE D N   1 
ATOM   4394 C CA  . ILE D 2 118 ? 43.689 39.955  147.799 1.00 43.36  ? 115 ILE D CA  1 
ATOM   4395 C C   . ILE D 2 118 ? 42.269 39.549  147.467 1.00 44.28  ? 115 ILE D C   1 
ATOM   4396 O O   . ILE D 2 118 ? 41.637 38.818  148.201 1.00 48.36  ? 115 ILE D O   1 
ATOM   4397 C CB  . ILE D 2 118 ? 43.720 41.454  148.206 1.00 44.23  ? 115 ILE D CB  1 
ATOM   4398 C CG1 . ILE D 2 118 ? 45.085 41.800  148.820 1.00 42.56  ? 115 ILE D CG1 1 
ATOM   4399 C CG2 . ILE D 2 118 ? 42.555 41.830  149.094 1.00 40.22  ? 115 ILE D CG2 1 
ATOM   4400 C CD1 . ILE D 2 118 ? 45.328 43.278  148.815 1.00 45.57  ? 115 ILE D CD1 1 
ATOM   4401 N N   . TYR D 2 119 ? 41.766 40.050  146.346 1.00 48.35  ? 116 TYR D N   1 
ATOM   4402 C CA  . TYR D 2 119 ? 40.461 39.598  145.801 1.00 46.67  ? 116 TYR D CA  1 
ATOM   4403 C C   . TYR D 2 119 ? 40.271 38.093  145.716 1.00 47.35  ? 116 TYR D C   1 
ATOM   4404 O O   . TYR D 2 119 ? 39.195 37.583  146.073 1.00 41.25  ? 116 TYR D O   1 
ATOM   4405 C CB  . TYR D 2 119 ? 40.280 40.114  144.386 1.00 47.49  ? 116 TYR D CB  1 
ATOM   4406 C CG  . TYR D 2 119 ? 38.997 39.650  143.836 1.00 50.01  ? 116 TYR D CG  1 
ATOM   4407 C CD1 . TYR D 2 119 ? 37.806 40.143  144.343 1.00 54.74  ? 116 TYR D CD1 1 
ATOM   4408 C CD2 . TYR D 2 119 ? 38.943 38.667  142.856 1.00 49.23  ? 116 TYR D CD2 1 
ATOM   4409 C CE1 . TYR D 2 119 ? 36.588 39.681  143.863 1.00 59.65  ? 116 TYR D CE1 1 
ATOM   4410 C CE2 . TYR D 2 119 ? 37.735 38.189  142.382 1.00 45.81  ? 116 TYR D CE2 1 
ATOM   4411 C CZ  . TYR D 2 119 ? 36.565 38.700  142.870 1.00 49.31  ? 116 TYR D CZ  1 
ATOM   4412 O OH  . TYR D 2 119 ? 35.360 38.254  142.406 1.00 52.67  ? 116 TYR D OH  1 
ATOM   4413 N N   . ALA D 2 120 ? 41.289 37.382  145.212 1.00 41.37  ? 117 ALA D N   1 
ATOM   4414 C CA  . ALA D 2 120 ? 41.138 35.948  144.962 1.00 47.88  ? 117 ALA D CA  1 
ATOM   4415 C C   . ALA D 2 120 ? 41.029 35.173  146.277 1.00 53.41  ? 117 ALA D C   1 
ATOM   4416 O O   . ALA D 2 120 ? 40.144 34.329  146.457 1.00 59.45  ? 117 ALA D O   1 
ATOM   4417 C CB  . ALA D 2 120 ? 42.286 35.399  144.104 1.00 47.99  ? 117 ALA D CB  1 
ATOM   4418 N N   . THR D 2 121 ? 41.950 35.460  147.178 1.00 53.82  ? 118 THR D N   1 
ATOM   4419 C CA  . THR D 2 121 ? 41.877 35.038  148.574 1.00 45.98  ? 118 THR D CA  1 
ATOM   4420 C C   . THR D 2 121 ? 40.521 35.316  149.194 1.00 47.45  ? 118 THR D C   1 
ATOM   4421 O O   . THR D 2 121 ? 39.927 34.421  149.737 1.00 54.56  ? 118 THR D O   1 
ATOM   4422 C CB  . THR D 2 121 ? 43.013 35.742  149.337 1.00 49.11  ? 118 THR D CB  1 
ATOM   4423 O OG1 . THR D 2 121 ? 44.273 35.243  148.842 1.00 48.62  ? 118 THR D OG1 1 
ATOM   4424 C CG2 . THR D 2 121 ? 42.940 35.544  150.800 1.00 46.08  ? 118 THR D CG2 1 
ATOM   4425 N N   . GLU D 2 122 ? 39.975 36.518  149.099 1.00 50.82  ? 119 GLU D N   1 
ATOM   4426 C CA  . GLU D 2 122 ? 38.624 36.740  149.667 1.00 54.52  ? 119 GLU D CA  1 
ATOM   4427 C C   . GLU D 2 122 ? 37.592 35.875  148.943 1.00 60.98  ? 119 GLU D C   1 
ATOM   4428 O O   . GLU D 2 122 ? 36.719 35.262  149.573 1.00 56.07  ? 119 GLU D O   1 
ATOM   4429 C CB  . GLU D 2 122 ? 38.203 38.216  149.603 1.00 62.57  ? 119 GLU D CB  1 
ATOM   4430 C CG  . GLU D 2 122 ? 38.459 39.040  150.873 1.00 80.49  ? 119 GLU D CG  1 
ATOM   4431 C CD  . GLU D 2 122 ? 37.572 38.632  152.085 1.00 99.80  ? 119 GLU D CD  1 
ATOM   4432 O OE1 . GLU D 2 122 ? 36.386 38.229  151.899 1.00 101.31 ? 119 GLU D OE1 1 
ATOM   4433 O OE2 . GLU D 2 122 ? 38.061 38.716  153.247 1.00 102.99 ? 119 GLU D OE2 1 
ATOM   4434 N N   . THR D 2 123 ? 37.719 35.805  147.612 1.00 54.42  ? 120 THR D N   1 
ATOM   4435 C CA  . THR D 2 123 ? 36.723 35.151  146.786 1.00 50.42  ? 120 THR D CA  1 
ATOM   4436 C C   . THR D 2 123 ? 36.733 33.625  147.001 1.00 51.84  ? 120 THR D C   1 
ATOM   4437 O O   . THR D 2 123 ? 35.660 32.955  147.055 1.00 43.16  ? 120 THR D O   1 
ATOM   4438 C CB  . THR D 2 123 ? 36.900 35.527  145.277 1.00 55.50  ? 120 THR D CB  1 
ATOM   4439 O OG1 . THR D 2 123 ? 36.554 36.912  145.072 1.00 47.82  ? 120 THR D OG1 1 
ATOM   4440 C CG2 . THR D 2 123 ? 36.011 34.650  144.377 1.00 51.04  ? 120 THR D CG2 1 
ATOM   4441 N N   . PHE D 2 124 ? 37.919 33.065  147.147 1.00 45.71  ? 121 PHE D N   1 
ATOM   4442 C CA  . PHE D 2 124 ? 38.012 31.636  147.346 1.00 51.99  ? 121 PHE D CA  1 
ATOM   4443 C C   . PHE D 2 124 ? 38.127 31.166  148.834 1.00 54.28  ? 121 PHE D C   1 
ATOM   4444 O O   . PHE D 2 124 ? 38.404 30.001  149.125 1.00 55.45  ? 121 PHE D O   1 
ATOM   4445 C CB  . PHE D 2 124 ? 39.164 31.106  146.503 1.00 50.23  ? 121 PHE D CB  1 
ATOM   4446 C CG  . PHE D 2 124 ? 38.794 30.888  145.083 1.00 56.39  ? 121 PHE D CG  1 
ATOM   4447 C CD1 . PHE D 2 124 ? 38.912 31.907  144.164 1.00 58.40  ? 121 PHE D CD1 1 
ATOM   4448 C CD2 . PHE D 2 124 ? 38.323 29.662  144.662 1.00 55.54  ? 121 PHE D CD2 1 
ATOM   4449 C CE1 . PHE D 2 124 ? 38.565 31.711  142.838 1.00 58.36  ? 121 PHE D CE1 1 
ATOM   4450 C CE2 . PHE D 2 124 ? 37.973 29.461  143.344 1.00 55.08  ? 121 PHE D CE2 1 
ATOM   4451 C CZ  . PHE D 2 124 ? 38.096 30.486  142.423 1.00 55.29  ? 121 PHE D CZ  1 
ATOM   4452 N N   . LYS D 2 125 ? 37.839 32.027  149.780 1.00 55.20  ? 122 LYS D N   1 
ATOM   4453 C CA  . LYS D 2 125 ? 38.201 31.681  151.165 1.00 64.53  ? 122 LYS D CA  1 
ATOM   4454 C C   . LYS D 2 125 ? 37.483 30.466  151.755 1.00 52.15  ? 122 LYS D C   1 
ATOM   4455 O O   . LYS D 2 125 ? 38.041 29.839  152.611 1.00 58.70  ? 122 LYS D O   1 
ATOM   4456 C CB  . LYS D 2 125 ? 38.133 32.929  152.060 1.00 70.36  ? 122 LYS D CB  1 
ATOM   4457 C CG  . LYS D 2 125 ? 37.422 32.826  153.380 1.00 86.41  ? 122 LYS D CG  1 
ATOM   4458 C CD  . LYS D 2 125 ? 36.521 34.042  153.583 1.00 97.61  ? 122 LYS D CD  1 
ATOM   4459 C CE  . LYS D 2 125 ? 35.243 33.954  152.745 1.00 97.84  ? 122 LYS D CE  1 
ATOM   4460 N NZ  . LYS D 2 125 ? 34.629 35.301  152.607 1.00 93.64  ? 122 LYS D NZ  1 
ATOM   4461 N N   . SER D 2 126 ? 36.310 30.112  151.246 1.00 48.06  ? 123 SER D N   1 
ATOM   4462 C CA  . SER D 2 126 ? 35.550 28.900  151.631 1.00 47.91  ? 123 SER D CA  1 
ATOM   4463 C C   . SER D 2 126 ? 35.816 27.681  150.751 1.00 51.15  ? 123 SER D C   1 
ATOM   4464 O O   . SER D 2 126 ? 35.046 26.712  150.736 1.00 57.64  ? 123 SER D O   1 
ATOM   4465 C CB  . SER D 2 126 ? 34.068 29.196  151.581 1.00 50.11  ? 123 SER D CB  1 
ATOM   4466 O OG  . SER D 2 126 ? 33.851 30.457  152.207 1.00 64.33  ? 123 SER D OG  1 
ATOM   4467 N N   . ILE D 2 127 ? 36.907 27.715  150.013 1.00 42.40  ? 124 ILE D N   1 
ATOM   4468 C CA  . ILE D 2 127 ? 37.248 26.642  149.174 1.00 43.00  ? 124 ILE D CA  1 
ATOM   4469 C C   . ILE D 2 127 ? 38.626 26.250  149.620 1.00 44.24  ? 124 ILE D C   1 
ATOM   4470 O O   . ILE D 2 127 ? 39.444 27.143  149.847 1.00 48.39  ? 124 ILE D O   1 
ATOM   4471 C CB  . ILE D 2 127 ? 37.395 27.158  147.710 1.00 46.72  ? 124 ILE D CB  1 
ATOM   4472 C CG1 . ILE D 2 127 ? 36.123 27.820  147.222 1.00 47.02  ? 124 ILE D CG1 1 
ATOM   4473 C CG2 . ILE D 2 127 ? 37.776 26.027  146.769 1.00 45.69  ? 124 ILE D CG2 1 
ATOM   4474 C CD1 . ILE D 2 127 ? 34.893 27.002  147.385 1.00 46.71  ? 124 ILE D CD1 1 
ATOM   4475 N N   . SER D 2 128 ? 38.964 24.965  149.599 1.00 47.57  ? 125 SER D N   1 
ATOM   4476 C CA  . SER D 2 128 ? 40.351 24.569  149.864 1.00 51.94  ? 125 SER D CA  1 
ATOM   4477 C C   . SER D 2 128 ? 41.140 24.425  148.624 1.00 53.65  ? 125 SER D C   1 
ATOM   4478 O O   . SER D 2 128 ? 40.620 24.060  147.569 1.00 51.46  ? 125 SER D O   1 
ATOM   4479 C CB  . SER D 2 128 ? 40.424 23.236  150.577 1.00 52.55  ? 125 SER D CB  1 
ATOM   4480 O OG  . SER D 2 128 ? 39.695 23.376  151.774 1.00 75.08  ? 125 SER D OG  1 
ATOM   4481 N N   . ASP D 2 129 ? 42.432 24.595  148.803 1.00 55.38  ? 126 ASP D N   1 
ATOM   4482 C CA  . ASP D 2 129 ? 43.398 24.403  147.756 1.00 61.05  ? 126 ASP D CA  1 
ATOM   4483 C C   . ASP D 2 129 ? 43.201 23.018  147.134 1.00 57.21  ? 126 ASP D C   1 
ATOM   4484 O O   . ASP D 2 129 ? 43.334 22.843  145.914 1.00 62.86  ? 126 ASP D O   1 
ATOM   4485 C CB  . ASP D 2 129 ? 44.807 24.558  148.363 1.00 77.86  ? 126 ASP D CB  1 
ATOM   4486 C CG  . ASP D 2 129 ? 45.899 24.851  147.317 1.00 101.22 ? 126 ASP D CG  1 
ATOM   4487 O OD1 . ASP D 2 129 ? 45.589 25.296  146.178 1.00 115.24 ? 126 ASP D OD1 1 
ATOM   4488 O OD2 . ASP D 2 129 ? 47.092 24.646  147.658 1.00 105.53 ? 126 ASP D OD2 1 
ATOM   4489 N N   . GLU D 2 130 ? 42.868 22.030  147.958 1.00 53.00  ? 127 GLU D N   1 
ATOM   4490 C CA  . GLU D 2 130 ? 42.786 20.660  147.482 1.00 51.30  ? 127 GLU D CA  1 
ATOM   4491 C C   . GLU D 2 130 ? 41.512 20.429  146.663 1.00 50.92  ? 127 GLU D C   1 
ATOM   4492 O O   . GLU D 2 130 ? 41.397 19.378  146.039 1.00 50.13  ? 127 GLU D O   1 
ATOM   4493 C CB  . GLU D 2 130 ? 42.763 19.637  148.640 1.00 64.20  ? 127 GLU D CB  1 
ATOM   4494 C CG  . GLU D 2 130 ? 43.770 19.828  149.773 1.00 68.46  ? 127 GLU D CG  1 
ATOM   4495 C CD  . GLU D 2 130 ? 45.118 19.190  149.532 1.00 77.90  ? 127 GLU D CD  1 
ATOM   4496 O OE1 . GLU D 2 130 ? 45.824 19.035  150.554 1.00 95.27  ? 127 GLU D OE1 1 
ATOM   4497 O OE2 . GLU D 2 130 ? 45.479 18.855  148.368 1.00 77.00  ? 127 GLU D OE2 1 
ATOM   4498 N N   . GLU D 2 131 ? 40.539 21.353  146.684 1.00 46.57  ? 128 GLU D N   1 
ATOM   4499 C CA  . GLU D 2 131 ? 39.364 21.217  145.789 1.00 48.70  ? 128 GLU D CA  1 
ATOM   4500 C C   . GLU D 2 131 ? 39.539 21.847  144.422 1.00 47.69  ? 128 GLU D C   1 
ATOM   4501 O O   . GLU D 2 131 ? 38.743 21.548  143.562 1.00 45.72  ? 128 GLU D O   1 
ATOM   4502 C CB  . GLU D 2 131 ? 38.114 21.834  146.328 1.00 44.92  ? 128 GLU D CB  1 
ATOM   4503 C CG  . GLU D 2 131 ? 37.978 21.692  147.778 1.00 48.42  ? 128 GLU D CG  1 
ATOM   4504 C CD  . GLU D 2 131 ? 36.646 22.158  148.253 1.00 49.40  ? 128 GLU D CD  1 
ATOM   4505 O OE1 . GLU D 2 131 ? 36.651 23.274  148.806 1.00 46.53  ? 128 GLU D OE1 1 
ATOM   4506 O OE2 . GLU D 2 131 ? 35.639 21.408  148.107 1.00 46.87  ? 128 GLU D OE2 1 
ATOM   4507 N N   . LEU D 2 132 ? 40.553 22.698  144.232 1.00 44.01  ? 129 LEU D N   1 
ATOM   4508 C CA  . LEU D 2 132 ? 40.802 23.272  142.925 1.00 44.17  ? 129 LEU D CA  1 
ATOM   4509 C C   . LEU D 2 132 ? 41.019 22.264  141.815 1.00 51.66  ? 129 LEU D C   1 
ATOM   4510 O O   . LEU D 2 132 ? 40.599 22.482  140.667 1.00 61.05  ? 129 LEU D O   1 
ATOM   4511 C CB  . LEU D 2 132 ? 41.978 24.195  142.966 1.00 44.34  ? 129 LEU D CB  1 
ATOM   4512 C CG  . LEU D 2 132 ? 41.636 25.350  143.918 1.00 53.98  ? 129 LEU D CG  1 
ATOM   4513 C CD1 . LEU D 2 132 ? 42.824 26.288  143.962 1.00 55.39  ? 129 LEU D CD1 1 
ATOM   4514 C CD2 . LEU D 2 132 ? 40.352 26.110  143.546 1.00 55.46  ? 129 LEU D CD2 1 
ATOM   4515 N N   . PRO D 2 133 ? 41.666 21.141  142.129 1.00 57.59  ? 130 PRO D N   1 
ATOM   4516 C CA  . PRO D 2 133 ? 41.936 20.229  141.006 1.00 49.68  ? 130 PRO D CA  1 
ATOM   4517 C C   . PRO D 2 133 ? 40.694 19.551  140.475 1.00 48.14  ? 130 PRO D C   1 
ATOM   4518 O O   . PRO D 2 133 ? 40.604 19.249  139.286 1.00 47.54  ? 130 PRO D O   1 
ATOM   4519 C CB  . PRO D 2 133 ? 42.884 19.189  141.634 1.00 54.56  ? 130 PRO D CB  1 
ATOM   4520 C CG  . PRO D 2 133 ? 43.562 19.955  142.728 1.00 55.02  ? 130 PRO D CG  1 
ATOM   4521 C CD  . PRO D 2 133 ? 42.480 20.818  143.320 1.00 53.10  ? 130 PRO D CD  1 
ATOM   4522 N N   . LEU D 2 134 ? 39.751 19.270  141.365 1.00 50.19  ? 131 LEU D N   1 
ATOM   4523 C CA  . LEU D 2 134 ? 38.495 18.626  140.967 1.00 48.49  ? 131 LEU D CA  1 
ATOM   4524 C C   . LEU D 2 134 ? 37.706 19.616  140.120 1.00 45.81  ? 131 LEU D C   1 
ATOM   4525 O O   . LEU D 2 134 ? 37.279 19.303  138.988 1.00 42.08  ? 131 LEU D O   1 
ATOM   4526 C CB  . LEU D 2 134 ? 37.681 18.208  142.201 1.00 50.62  ? 131 LEU D CB  1 
ATOM   4527 C CG  . LEU D 2 134 ? 36.677 17.073  142.047 1.00 53.44  ? 131 LEU D CG  1 
ATOM   4528 C CD1 . LEU D 2 134 ? 35.328 17.506  142.534 1.00 53.50  ? 131 LEU D CD1 1 
ATOM   4529 C CD2 . LEU D 2 134 ? 36.603 16.439  140.629 1.00 58.64  ? 131 LEU D CD2 1 
ATOM   4530 N N   . PHE D 2 135 ? 37.557 20.810  140.687 1.00 38.77  ? 132 PHE D N   1 
ATOM   4531 C CA  . PHE D 2 135 ? 36.877 21.919  140.051 1.00 38.76  ? 132 PHE D CA  1 
ATOM   4532 C C   . PHE D 2 135 ? 37.372 22.190  138.652 1.00 41.13  ? 132 PHE D C   1 
ATOM   4533 O O   . PHE D 2 135 ? 36.637 22.105  137.648 1.00 49.82  ? 132 PHE D O   1 
ATOM   4534 C CB  . PHE D 2 135 ? 37.119 23.142  140.858 1.00 38.16  ? 132 PHE D CB  1 
ATOM   4535 C CG  . PHE D 2 135 ? 36.353 24.333  140.385 1.00 42.28  ? 132 PHE D CG  1 
ATOM   4536 C CD1 . PHE D 2 135 ? 34.977 24.292  140.301 1.00 41.85  ? 132 PHE D CD1 1 
ATOM   4537 C CD2 . PHE D 2 135 ? 37.001 25.519  140.093 1.00 39.35  ? 132 PHE D CD2 1 
ATOM   4538 C CE1 . PHE D 2 135 ? 34.265 25.423  139.935 1.00 41.96  ? 132 PHE D CE1 1 
ATOM   4539 C CE2 . PHE D 2 135 ? 36.296 26.640  139.727 1.00 40.80  ? 132 PHE D CE2 1 
ATOM   4540 C CZ  . PHE D 2 135 ? 34.926 26.592  139.641 1.00 41.82  ? 132 PHE D CZ  1 
ATOM   4541 N N   . THR D 2 136 ? 38.635 22.505  138.602 1.00 41.45  ? 133 THR D N   1 
ATOM   4542 C CA  . THR D 2 136 ? 39.379 22.683  137.353 1.00 42.82  ? 133 THR D CA  1 
ATOM   4543 C C   . THR D 2 136 ? 39.311 21.547  136.343 1.00 40.71  ? 133 THR D C   1 
ATOM   4544 O O   . THR D 2 136 ? 39.332 21.771  135.106 1.00 36.29  ? 133 THR D O   1 
ATOM   4545 C CB  . THR D 2 136 ? 40.826 22.903  137.784 1.00 40.84  ? 133 THR D CB  1 
ATOM   4546 O OG1 . THR D 2 136 ? 40.965 24.312  137.930 1.00 43.57  ? 133 THR D OG1 1 
ATOM   4547 C CG2 . THR D 2 136 ? 41.804 22.287  136.835 1.00 48.68  ? 133 THR D CG2 1 
ATOM   4548 N N   . ASP D 2 137 ? 39.234 20.318  136.854 1.00 39.48  ? 134 ASP D N   1 
ATOM   4549 C CA  . ASP D 2 137 ? 39.302 19.184  135.959 1.00 42.88  ? 134 ASP D CA  1 
ATOM   4550 C C   . ASP D 2 137 ? 37.893 19.038  135.336 1.00 46.39  ? 134 ASP D C   1 
ATOM   4551 O O   . ASP D 2 137 ? 37.754 18.819  134.109 1.00 43.39  ? 134 ASP D O   1 
ATOM   4552 C CB  . ASP D 2 137 ? 39.817 17.935  136.680 1.00 45.13  ? 134 ASP D CB  1 
ATOM   4553 C CG  . ASP D 2 137 ? 39.785 16.697  135.795 1.00 51.82  ? 134 ASP D CG  1 
ATOM   4554 O OD1 . ASP D 2 137 ? 40.404 16.649  134.719 1.00 57.84  ? 134 ASP D OD1 1 
ATOM   4555 O OD2 . ASP D 2 137 ? 39.099 15.746  136.171 1.00 65.09  ? 134 ASP D OD2 1 
ATOM   4556 N N   . ILE D 2 138 ? 36.852 19.227  136.160 1.00 43.71  ? 135 ILE D N   1 
ATOM   4557 C CA  . ILE D 2 138 ? 35.498 19.243  135.650 1.00 45.03  ? 135 ILE D CA  1 
ATOM   4558 C C   . ILE D 2 138 ? 35.354 20.353  134.601 1.00 41.95  ? 135 ILE D C   1 
ATOM   4559 O O   . ILE D 2 138 ? 34.876 20.118  133.497 1.00 37.65  ? 135 ILE D O   1 
ATOM   4560 C CB  . ILE D 2 138 ? 34.496 19.387  136.779 1.00 50.39  ? 135 ILE D CB  1 
ATOM   4561 C CG1 . ILE D 2 138 ? 34.524 18.111  137.622 1.00 53.07  ? 135 ILE D CG1 1 
ATOM   4562 C CG2 . ILE D 2 138 ? 33.100 19.561  136.202 1.00 51.18  ? 135 ILE D CG2 1 
ATOM   4563 C CD1 . ILE D 2 138 ? 33.692 18.168  138.880 1.00 54.10  ? 135 ILE D CD1 1 
ATOM   4564 N N   . LEU D 2 139 ? 35.864 21.539  134.895 1.00 39.48  ? 136 LEU D N   1 
ATOM   4565 C CA  . LEU D 2 139 ? 35.771 22.593  133.909 1.00 36.98  ? 136 LEU D CA  1 
ATOM   4566 C C   . LEU D 2 139 ? 36.442 22.165  132.648 1.00 41.75  ? 136 LEU D C   1 
ATOM   4567 O O   . LEU D 2 139 ? 35.911 22.416  131.592 1.00 45.53  ? 136 LEU D O   1 
ATOM   4568 C CB  . LEU D 2 139 ? 36.329 23.905  134.402 1.00 34.30  ? 136 LEU D CB  1 
ATOM   4569 C CG  . LEU D 2 139 ? 35.511 24.508  135.551 1.00 33.46  ? 136 LEU D CG  1 
ATOM   4570 C CD1 . LEU D 2 139 ? 36.317 25.555  136.311 1.00 35.48  ? 136 LEU D CD1 1 
ATOM   4571 C CD2 . LEU D 2 139 ? 34.213 25.132  135.089 1.00 36.36  ? 136 LEU D CD2 1 
ATOM   4572 N N   . ASP D 2 140 ? 37.576 21.480  132.728 1.00 45.61  ? 137 ASP D N   1 
ATOM   4573 C CA  . ASP D 2 140 ? 38.239 21.039  131.495 1.00 47.86  ? 137 ASP D CA  1 
ATOM   4574 C C   . ASP D 2 140 ? 37.398 20.070  130.754 1.00 44.68  ? 137 ASP D C   1 
ATOM   4575 O O   . ASP D 2 140 ? 37.400 20.107  129.563 1.00 45.71  ? 137 ASP D O   1 
ATOM   4576 C CB  . ASP D 2 140 ? 39.664 20.459  131.693 1.00 56.80  ? 137 ASP D CB  1 
ATOM   4577 C CG  . ASP D 2 140 ? 40.666 21.514  132.211 1.00 60.96  ? 137 ASP D CG  1 
ATOM   4578 O OD1 . ASP D 2 140 ? 40.568 22.691  131.796 1.00 67.57  ? 137 ASP D OD1 1 
ATOM   4579 O OD2 . ASP D 2 140 ? 41.525 21.186  133.057 1.00 68.17  ? 137 ASP D OD2 1 
ATOM   4580 N N   . ARG D 2 141 ? 36.638 19.232  131.430 1.00 46.39  ? 138 ARG D N   1 
ATOM   4581 C CA  . ARG D 2 141 ? 35.845 18.257  130.691 1.00 54.56  ? 138 ARG D CA  1 
ATOM   4582 C C   . ARG D 2 141 ? 34.552 18.834  130.070 1.00 54.89  ? 138 ARG D C   1 
ATOM   4583 O O   . ARG D 2 141 ? 34.096 18.387  129.018 1.00 49.13  ? 138 ARG D O   1 
ATOM   4584 C CB  . ARG D 2 141 ? 35.635 17.000  131.538 1.00 53.56  ? 138 ARG D CB  1 
ATOM   4585 C CG  . ARG D 2 141 ? 36.914 16.132  131.491 1.00 52.08  ? 138 ARG D CG  1 
ATOM   4586 C CD  . ARG D 2 141 ? 37.262 15.487  132.849 1.00 55.44  ? 138 ARG D CD  1 
ATOM   4587 N NE  . ARG D 2 141 ? 36.165 14.719  133.382 1.00 47.78  ? 138 ARG D NE  1 
ATOM   4588 C CZ  . ARG D 2 141 ? 35.817 14.624  134.658 1.00 54.43  ? 138 ARG D CZ  1 
ATOM   4589 N NH1 . ARG D 2 141 ? 36.490 15.236  135.648 1.00 47.78  ? 138 ARG D NH1 1 
ATOM   4590 N NH2 . ARG D 2 141 ? 34.739 13.886  134.946 1.00 60.40  ? 138 ARG D NH2 1 
ATOM   4591 N N   . ILE D 2 142 ? 34.023 19.884  130.675 1.00 57.95  ? 139 ILE D N   1 
ATOM   4592 C CA  . ILE D 2 142 ? 32.857 20.554  130.128 1.00 53.08  ? 139 ILE D CA  1 
ATOM   4593 C C   . ILE D 2 142 ? 33.130 21.069  128.735 1.00 53.41  ? 139 ILE D C   1 
ATOM   4594 O O   . ILE D 2 142 ? 34.049 21.845  128.531 1.00 60.52  ? 139 ILE D O   1 
ATOM   4595 C CB  . ILE D 2 142 ? 32.355 21.634  131.079 1.00 44.85  ? 139 ILE D CB  1 
ATOM   4596 C CG1 . ILE D 2 142 ? 31.693 20.952  132.259 1.00 41.88  ? 139 ILE D CG1 1 
ATOM   4597 C CG2 . ILE D 2 142 ? 31.348 22.503  130.404 1.00 49.71  ? 139 ILE D CG2 1 
ATOM   4598 C CD1 . ILE D 2 142 ? 31.215 21.863  133.340 1.00 39.93  ? 139 ILE D CD1 1 
ATOM   4599 N N   . GLY D 2 143 ? 32.315 20.576  127.788 1.00 67.60  ? 140 GLY D N   1 
ATOM   4600 C CA  . GLY D 2 143 ? 32.352 20.922  126.343 1.00 66.83  ? 140 GLY D CA  1 
ATOM   4601 C C   . GLY D 2 143 ? 32.545 19.696  125.456 1.00 73.12  ? 140 GLY D C   1 
ATOM   4602 O O   . GLY D 2 143 ? 33.585 19.005  125.538 1.00 77.68  ? 140 GLY D O   1 
HETATM 4603 O O   . HOH E 3 .   ? 41.741 7.177   76.017  1.00 21.53  ? 201 HOH A O   1 
HETATM 4604 O O   . HOH E 3 .   ? 32.892 20.935  111.764 1.00 48.95  ? 202 HOH A O   1 
HETATM 4605 O O   . HOH E 3 .   ? 44.612 5.147   88.532  1.00 47.31  ? 203 HOH A O   1 
HETATM 4606 O O   . HOH E 3 .   ? 8.262  10.936  123.304 1.00 69.06  ? 204 HOH A O   1 
HETATM 4607 O O   . HOH E 3 .   ? 19.346 0.411   110.140 1.00 61.88  ? 205 HOH A O   1 
HETATM 4608 O O   . HOH E 3 .   ? 1.396  0.273   111.727 1.00 49.47  ? 206 HOH A O   1 
HETATM 4609 O O   . HOH E 3 .   ? 10.114 10.374  109.367 1.00 48.15  ? 207 HOH A O   1 
HETATM 4610 O O   . HOH E 3 .   ? 23.690 -2.299  110.352 1.00 56.39  ? 208 HOH A O   1 
HETATM 4611 O O   . HOH E 3 .   ? 14.419 -2.706  92.084  1.00 74.38  ? 209 HOH A O   1 
HETATM 4612 O O   . HOH E 3 .   ? 23.642 14.573  123.194 1.00 70.22  ? 210 HOH A O   1 
HETATM 4613 O O   . HOH E 3 .   ? 22.627 20.811  115.984 1.00 53.32  ? 211 HOH A O   1 
HETATM 4614 O O   . HOH E 3 .   ? 43.095 11.715  97.666  1.00 48.76  ? 212 HOH A O   1 
HETATM 4615 O O   . HOH E 3 .   ? 5.527  10.727  116.069 1.00 62.44  ? 213 HOH A O   1 
HETATM 4616 O O   . HOH E 3 .   ? 15.221 13.781  124.517 1.00 56.19  ? 214 HOH A O   1 
HETATM 4617 O O   . HOH E 3 .   ? 24.476 21.892  109.145 1.00 45.89  ? 215 HOH A O   1 
HETATM 4618 O O   . HOH E 3 .   ? 23.992 4.662   111.472 1.00 58.85  ? 216 HOH A O   1 
HETATM 4619 O O   . HOH E 3 .   ? 43.357 9.626   103.705 1.00 65.01  ? 217 HOH A O   1 
HETATM 4620 O O   . HOH E 3 .   ? 7.976  16.527  120.355 1.00 71.84  ? 218 HOH A O   1 
HETATM 4621 O O   . HOH E 3 .   ? 40.540 10.059  85.263  1.00 40.83  ? 219 HOH A O   1 
HETATM 4622 O O   . HOH E 3 .   ? 9.098  14.275  112.373 1.00 43.80  ? 220 HOH A O   1 
HETATM 4623 O O   . HOH E 3 .   ? 42.437 5.954   87.168  1.00 20.19  ? 221 HOH A O   1 
HETATM 4624 O O   . HOH E 3 .   ? 48.066 8.903   82.489  1.00 47.51  ? 222 HOH A O   1 
HETATM 4625 O O   . HOH E 3 .   ? 42.287 16.395  84.487  1.00 55.32  ? 223 HOH A O   1 
HETATM 4626 O O   . HOH E 3 .   ? 3.432  17.585  119.279 1.00 74.15  ? 224 HOH A O   1 
HETATM 4627 O O   . HOH E 3 .   ? 9.440  0.966   96.813  1.00 65.54  ? 225 HOH A O   1 
HETATM 4628 O O   . HOH E 3 .   ? 22.819 10.740  129.414 1.00 73.04  ? 226 HOH A O   1 
HETATM 4629 O O   . HOH E 3 .   ? 49.402 4.882   89.793  1.00 44.20  ? 227 HOH A O   1 
HETATM 4630 O O   . HOH E 3 .   ? 27.878 21.890  120.134 1.00 63.94  ? 228 HOH A O   1 
HETATM 4631 O O   . HOH E 3 .   ? 19.510 0.481   105.489 1.00 54.20  ? 229 HOH A O   1 
HETATM 4632 O O   . HOH E 3 .   ? 42.192 8.686   106.856 1.00 57.91  ? 230 HOH A O   1 
HETATM 4633 O O   . HOH E 3 .   ? 45.664 6.815   103.396 1.00 78.28  ? 231 HOH A O   1 
HETATM 4634 O O   . HOH E 3 .   ? 22.227 0.206   105.514 1.00 76.52  ? 232 HOH A O   1 
HETATM 4635 O O   . HOH E 3 .   ? 45.886 -5.293  84.287  1.00 56.37  ? 233 HOH A O   1 
HETATM 4636 O O   . HOH E 3 .   ? 40.250 1.090   105.649 1.00 52.37  ? 234 HOH A O   1 
HETATM 4637 O O   . HOH E 3 .   ? 55.039 4.651   95.269  1.00 72.57  ? 235 HOH A O   1 
HETATM 4638 O O   . HOH F 3 .   ? 33.009 -0.568  94.329  1.00 53.08  ? 201 HOH B O   1 
HETATM 4639 O O   . HOH F 3 .   ? 44.118 17.752  89.952  1.00 46.11  ? 202 HOH B O   1 
HETATM 4640 O O   . HOH F 3 .   ? 37.448 1.466   115.882 1.00 68.46  ? 203 HOH B O   1 
HETATM 4641 O O   . HOH F 3 .   ? 47.913 -12.927 91.994  1.00 46.94  ? 204 HOH B O   1 
HETATM 4642 O O   . HOH F 3 .   ? 44.466 17.688  85.114  1.00 74.59  ? 205 HOH B O   1 
HETATM 4643 O O   . HOH F 3 .   ? 49.605 -8.872  89.830  1.00 62.49  ? 206 HOH B O   1 
HETATM 4644 O O   . HOH F 3 .   ? 52.414 0.796   101.473 1.00 43.42  ? 207 HOH B O   1 
HETATM 4645 O O   . HOH F 3 .   ? 44.518 15.405  86.438  1.00 65.60  ? 208 HOH B O   1 
HETATM 4646 O O   . HOH F 3 .   ? 52.800 -4.976  89.047  1.00 65.65  ? 209 HOH B O   1 
HETATM 4647 O O   . HOH F 3 .   ? 39.318 6.066   87.876  1.00 46.04  ? 210 HOH B O   1 
HETATM 4648 O O   . HOH F 3 .   ? 12.712 14.175  107.088 1.00 55.86  ? 211 HOH B O   1 
HETATM 4649 O O   . HOH F 3 .   ? 44.206 -13.420 88.884  1.00 56.68  ? 212 HOH B O   1 
HETATM 4650 O O   . HOH F 3 .   ? 52.748 -0.639  99.285  1.00 39.10  ? 213 HOH B O   1 
HETATM 4651 O O   . HOH F 3 .   ? 52.194 -16.007 111.371 1.00 46.24  ? 214 HOH B O   1 
HETATM 4652 O O   . HOH F 3 .   ? 33.470 6.334   89.180  1.00 49.65  ? 215 HOH B O   1 
HETATM 4653 O O   . HOH F 3 .   ? 36.015 13.606  109.288 1.00 71.44  ? 216 HOH B O   1 
HETATM 4654 O O   . HOH F 3 .   ? 45.197 -14.008 90.961  1.00 55.38  ? 217 HOH B O   1 
HETATM 4655 O O   . HOH F 3 .   ? 41.589 18.035  100.153 1.00 53.49  ? 218 HOH B O   1 
HETATM 4656 O O   . HOH F 3 .   ? 15.031 20.545  107.828 1.00 43.80  ? 219 HOH B O   1 
HETATM 4657 O O   . HOH F 3 .   ? 38.886 -7.764  108.811 1.00 51.75  ? 220 HOH B O   1 
HETATM 4658 O O   . HOH F 3 .   ? 46.244 -10.276 120.726 1.00 79.84  ? 221 HOH B O   1 
HETATM 4659 O O   . HOH F 3 .   ? 40.887 12.839  85.653  1.00 44.85  ? 222 HOH B O   1 
HETATM 4660 O O   . HOH F 3 .   ? 30.241 2.876   82.599  1.00 73.86  ? 223 HOH B O   1 
HETATM 4661 O O   . HOH F 3 .   ? 62.826 -8.592  125.691 1.00 69.56  ? 224 HOH B O   1 
HETATM 4662 O O   . HOH F 3 .   ? 31.868 2.096   107.041 1.00 28.58  ? 225 HOH B O   1 
HETATM 4663 O O   . HOH F 3 .   ? 36.032 0.167   115.324 1.00 59.21  ? 226 HOH B O   1 
HETATM 4664 O O   . HOH F 3 .   ? 39.796 -9.858  110.477 1.00 39.39  ? 227 HOH B O   1 
HETATM 4665 O O   . HOH F 3 .   ? 53.327 -2.736  94.571  1.00 39.80  ? 228 HOH B O   1 
HETATM 4666 O O   . HOH F 3 .   ? 51.037 2.425   96.100  1.00 54.69  ? 229 HOH B O   1 
HETATM 4667 O O   . HOH F 3 .   ? 60.978 -11.862 112.326 1.00 58.57  ? 230 HOH B O   1 
HETATM 4668 O O   . HOH F 3 .   ? 47.862 -15.785 119.466 1.00 36.87  ? 231 HOH B O   1 
HETATM 4669 O O   . HOH F 3 .   ? 13.766 18.303  105.626 1.00 52.41  ? 232 HOH B O   1 
HETATM 4670 O O   . HOH F 3 .   ? 43.727 -9.171  88.465  1.00 65.01  ? 233 HOH B O   1 
HETATM 4671 O O   . HOH F 3 .   ? 39.166 -13.132 106.512 1.00 53.38  ? 234 HOH B O   1 
HETATM 4672 O O   . HOH F 3 .   ? 61.216 -1.627  107.185 1.00 57.96  ? 235 HOH B O   1 
HETATM 4673 O O   . HOH F 3 .   ? 41.840 -17.729 107.908 1.00 63.04  ? 236 HOH B O   1 
HETATM 4674 O O   . HOH F 3 .   ? 36.506 -5.765  104.139 1.00 31.40  ? 237 HOH B O   1 
HETATM 4675 O O   . HOH F 3 .   ? 60.043 -12.620 109.659 1.00 54.86  ? 238 HOH B O   1 
HETATM 4676 O O   . HOH F 3 .   ? 49.950 -1.157  91.197  1.00 55.25  ? 239 HOH B O   1 
HETATM 4677 O O   . HOH F 3 .   ? 52.518 -2.523  121.673 1.00 37.74  ? 240 HOH B O   1 
HETATM 4678 O O   . HOH F 3 .   ? 47.372 -9.569  90.995  1.00 60.57  ? 241 HOH B O   1 
HETATM 4679 O O   . HOH F 3 .   ? 42.100 23.025  102.881 1.00 65.43  ? 242 HOH B O   1 
HETATM 4680 O O   . HOH F 3 .   ? 41.267 -8.193  89.286  1.00 55.69  ? 243 HOH B O   1 
HETATM 4681 O O   . HOH F 3 .   ? 51.573 -9.504  90.982  1.00 61.69  ? 244 HOH B O   1 
HETATM 4682 O O   . HOH F 3 .   ? 42.096 -1.300  109.597 1.00 64.87  ? 245 HOH B O   1 
HETATM 4683 O O   . HOH F 3 .   ? 53.409 -15.094 115.947 1.00 51.09  ? 246 HOH B O   1 
HETATM 4684 O O   . HOH F 3 .   ? 41.605 3.168   121.327 1.00 55.76  ? 247 HOH B O   1 
HETATM 4685 O O   . HOH F 3 .   ? 61.593 5.940   106.368 1.00 67.57  ? 248 HOH B O   1 
HETATM 4686 O O   . HOH F 3 .   ? 53.320 1.288   97.555  1.00 48.05  ? 249 HOH B O   1 
HETATM 4687 O O   . HOH F 3 .   ? 32.033 -3.643  105.082 1.00 62.85  ? 250 HOH B O   1 
HETATM 4688 O O   . HOH F 3 .   ? 46.763 -0.640  86.790  1.00 55.27  ? 251 HOH B O   1 
HETATM 4689 O O   . HOH F 3 .   ? 39.996 0.654   103.528 1.00 50.12  ? 252 HOH B O   1 
HETATM 4690 O O   . HOH F 3 .   ? 60.338 4.162   123.687 1.00 65.00  ? 253 HOH B O   1 
HETATM 4691 O O   . HOH G 3 .   ? 19.247 38.558  138.462 1.00 53.44  ? 201 HOH C O   1 
HETATM 4692 O O   . HOH G 3 .   ? 24.909 22.206  115.410 1.00 44.10  ? 202 HOH C O   1 
HETATM 4693 O O   . HOH G 3 .   ? 1.352  34.217  127.586 1.00 36.03  ? 203 HOH C O   1 
HETATM 4694 O O   . HOH G 3 .   ? 19.582 34.857  133.478 1.00 46.60  ? 204 HOH C O   1 
HETATM 4695 O O   . HOH G 3 .   ? 11.052 26.310  132.396 1.00 42.32  ? 205 HOH C O   1 
HETATM 4696 O O   . HOH G 3 .   ? 11.313 19.655  124.588 1.00 57.30  ? 206 HOH C O   1 
HETATM 4697 O O   . HOH G 3 .   ? 16.543 30.278  133.633 1.00 60.98  ? 207 HOH C O   1 
HETATM 4698 O O   . HOH G 3 .   ? 34.655 31.335  149.142 1.00 53.06  ? 208 HOH C O   1 
HETATM 4699 O O   . HOH G 3 .   ? 28.220 8.098   135.408 1.00 57.80  ? 209 HOH C O   1 
HETATM 4700 O O   . HOH G 3 .   ? 21.471 38.143  124.706 1.00 53.35  ? 210 HOH C O   1 
HETATM 4701 O O   . HOH G 3 .   ? -3.489 34.069  118.822 1.00 41.85  ? 211 HOH C O   1 
HETATM 4702 O O   . HOH G 3 .   ? 10.516 24.592  130.454 1.00 35.99  ? 212 HOH C O   1 
HETATM 4703 O O   . HOH G 3 .   ? 27.563 24.278  118.971 1.00 55.15  ? 213 HOH C O   1 
HETATM 4704 O O   . HOH G 3 .   ? 7.678  44.992  138.259 1.00 38.85  ? 214 HOH C O   1 
HETATM 4705 O O   . HOH G 3 .   ? 19.695 40.635  123.834 1.00 35.00  ? 215 HOH C O   1 
HETATM 4706 O O   . HOH G 3 .   ? 9.793  20.808  127.082 1.00 29.84  ? 216 HOH C O   1 
HETATM 4707 O O   . HOH G 3 .   ? 24.571 33.695  124.390 1.00 24.24  ? 217 HOH C O   1 
HETATM 4708 O O   . HOH G 3 .   ? 18.021 24.461  110.141 1.00 49.79  ? 218 HOH C O   1 
HETATM 4709 O O   . HOH G 3 .   ? 25.717 29.562  114.387 1.00 49.51  ? 219 HOH C O   1 
HETATM 4710 O O   . HOH G 3 .   ? 19.910 36.401  131.676 1.00 53.29  ? 220 HOH C O   1 
HETATM 4711 O O   . HOH G 3 .   ? 33.832 31.304  122.905 1.00 57.23  ? 221 HOH C O   1 
HETATM 4712 O O   . HOH G 3 .   ? 26.481 33.130  116.938 1.00 51.80  ? 222 HOH C O   1 
HETATM 4713 O O   . HOH G 3 .   ? 22.211 30.879  131.339 1.00 50.24  ? 223 HOH C O   1 
HETATM 4714 O O   . HOH H 3 .   ? 54.704 47.126  138.244 1.00 48.46  ? 201 HOH D O   1 
HETATM 4715 O O   . HOH H 3 .   ? 46.912 50.563  144.557 1.00 53.85  ? 202 HOH D O   1 
HETATM 4716 O O   . HOH H 3 .   ? 57.962 50.618  102.748 1.00 64.43  ? 203 HOH D O   1 
HETATM 4717 O O   . HOH H 3 .   ? 45.646 22.549  144.071 1.00 46.35  ? 204 HOH D O   1 
HETATM 4718 O O   . HOH H 3 .   ? 34.537 42.851  134.532 1.00 42.10  ? 205 HOH D O   1 
HETATM 4719 O O   . HOH H 3 .   ? 30.442 34.616  131.834 1.00 37.98  ? 206 HOH D O   1 
HETATM 4720 O O   . HOH H 3 .   ? 36.095 47.798  127.787 1.00 36.84  ? 207 HOH D O   1 
HETATM 4721 O O   . HOH H 3 .   ? 55.553 54.827  127.350 1.00 54.92  ? 208 HOH D O   1 
HETATM 4722 O O   . HOH H 3 .   ? 44.952 52.869  117.763 1.00 44.39  ? 209 HOH D O   1 
HETATM 4723 O O   . HOH H 3 .   ? 47.901 35.165  133.079 1.00 55.65  ? 210 HOH D O   1 
HETATM 4724 O O   . HOH H 3 .   ? 39.905 37.517  128.115 1.00 58.14  ? 211 HOH D O   1 
HETATM 4725 O O   . HOH H 3 .   ? 38.944 36.788  132.007 1.00 49.87  ? 212 HOH D O   1 
HETATM 4726 O O   . HOH H 3 .   ? 35.836 56.844  130.724 1.00 74.06  ? 213 HOH D O   1 
# 
