data_7NXX
# 
_entry.id   7NXX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.361 
_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   7NXX         pdb_00007nxx 10.2210/pdb7nxx/pdb 
WWPDB D_1292114770 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7NXX 
_pdbx_database_status.recvd_initial_deposition_date   2021-03-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gallardo, R.'    1 0000-0003-1584-3564 
'Rousseau, F.'    2 0000-0002-9189-7399 
'Schymkowitz, J.' 3 0000-0003-2020-0168 
'Ulens, C.'       4 0000-0002-8202-5281 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Identification and rational improvement of a nanobody that suppresses aggregation of mutant SOD1' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'van der Kant, R.'  1  0000-0003-3639-9749 
primary 'Gallardo, R.'      2  0000-0003-1584-3564 
primary 'Michiels, E.'      3  0000-0001-6065-5576 
primary 'Wilkinson, H.'     4  ?                   
primary 'Claes, F.'         5  ?                   
primary 'Laird, A.'         6  ?                   
primary 'Van Den Bosch, L.' 7  ?                   
primary 'Robberecht, W.'    8  ?                   
primary 'Ghassabeh, G.H.'   9  ?                   
primary 'Oliveberg, M.'     10 ?                   
primary 'Ulens, C.'         11 0000-0002-8202-5281 
primary 'Schymkowitz, J.'   12 0000-0003-2020-0168 
primary 'Rousseau, F.'      13 0000-0002-9189-7399 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7NXX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     115.830 
_cell.length_a_esd                 ? 
_cell.length_b                     115.830 
_cell.length_b_esd                 ? 
_cell.length_c                     83.790 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         7NXX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'Superoxide dismutase [Cu-Zn]' 15827.561 1 1.15.1.1 ? ? ? 
2 polymer     man 'nanobody 2'                   14752.282 1 ?        ? ? ? 
3 non-polymer syn 'COPPER (II) ION'              63.546    1 ?        ? ? ? 
4 non-polymer syn 'ZINC ION'                     65.409    1 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
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 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
A ? 
2 'polypeptide(L)' no no 
;MAQVQLQESGGGSVQAGGSLRLACVASGGDTRPYITYWMGWYRQAPGKEREGVATIYTGGSGTYYSDSVEGRFTISQDKA
QRTVYLQMNDLKPEDTAMYYCAAGNGALPPGRRLSPQNMDTWGPGTQVTVSSHHHH
;
;MAQVQLQESGGGSVQAGGSLRLACVASGGDTRPYITYWMGWYRQAPGKEREGVATIYTGGSGTYYSDSVEGRFTISQDKA
QRTVYLQMNDLKPEDTAMYYCAAGNGALPPGRRLSPQNMDTWGPGTQVTVSSHHHH
;
B ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
2 1   MET n 
2 2   ALA n 
2 3   GLN n 
2 4   VAL n 
2 5   GLN n 
2 6   LEU n 
2 7   GLN n 
2 8   GLU n 
2 9   SER n 
2 10  GLY n 
2 11  GLY n 
2 12  GLY n 
2 13  SER n 
2 14  VAL n 
2 15  GLN n 
2 16  ALA n 
2 17  GLY n 
2 18  GLY n 
2 19  SER n 
2 20  LEU n 
2 21  ARG n 
2 22  LEU n 
2 23  ALA n 
2 24  CYS n 
2 25  VAL n 
2 26  ALA n 
2 27  SER n 
2 28  GLY n 
2 29  GLY n 
2 30  ASP n 
2 31  THR n 
2 32  ARG n 
2 33  PRO n 
2 34  TYR n 
2 35  ILE n 
2 36  THR n 
2 37  TYR n 
2 38  TRP n 
2 39  MET n 
2 40  GLY n 
2 41  TRP n 
2 42  TYR n 
2 43  ARG n 
2 44  GLN n 
2 45  ALA n 
2 46  PRO n 
2 47  GLY n 
2 48  LYS n 
2 49  GLU n 
2 50  ARG n 
2 51  GLU n 
2 52  GLY n 
2 53  VAL n 
2 54  ALA n 
2 55  THR n 
2 56  ILE n 
2 57  TYR n 
2 58  THR n 
2 59  GLY n 
2 60  GLY n 
2 61  SER n 
2 62  GLY n 
2 63  THR n 
2 64  TYR n 
2 65  TYR n 
2 66  SER n 
2 67  ASP n 
2 68  SER n 
2 69  VAL n 
2 70  GLU n 
2 71  GLY n 
2 72  ARG n 
2 73  PHE n 
2 74  THR n 
2 75  ILE n 
2 76  SER n 
2 77  GLN n 
2 78  ASP n 
2 79  LYS n 
2 80  ALA n 
2 81  GLN n 
2 82  ARG n 
2 83  THR n 
2 84  VAL n 
2 85  TYR n 
2 86  LEU n 
2 87  GLN n 
2 88  MET n 
2 89  ASN n 
2 90  ASP n 
2 91  LEU n 
2 92  LYS n 
2 93  PRO n 
2 94  GLU n 
2 95  ASP n 
2 96  THR n 
2 97  ALA n 
2 98  MET n 
2 99  TYR n 
2 100 TYR n 
2 101 CYS n 
2 102 ALA n 
2 103 ALA n 
2 104 GLY n 
2 105 ASN n 
2 106 GLY n 
2 107 ALA n 
2 108 LEU n 
2 109 PRO n 
2 110 PRO n 
2 111 GLY n 
2 112 ARG n 
2 113 ARG n 
2 114 LEU n 
2 115 SER n 
2 116 PRO n 
2 117 GLN n 
2 118 ASN n 
2 119 MET n 
2 120 ASP n 
2 121 THR n 
2 122 TRP n 
2 123 GLY n 
2 124 PRO n 
2 125 GLY n 
2 126 THR n 
2 127 GLN n 
2 128 VAL n 
2 129 THR n 
2 130 VAL n 
2 131 SER n 
2 132 SER n 
2 133 HIS n 
2 134 HIS n 
2 135 HIS n 
2 136 HIS 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' 1 153 Human ? SOD1 ? ? ? ? ? ? 'Homo sapiens'        9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 136 ?     ? ?    ? ? ? ? ? ? 'Camelus dromedarius' 9838 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 SODC_HUMAN P00441 ? 1 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
2 
2 PDB 7NXX       7NXX   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7NXX A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 2 7NXX B 1 ? 136 ? 7NXX   1 ? 136 ? 1 136 
# 
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 
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE        ? 'C5 H11 N O2 S'  149.211 
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 
ZN  non-polymer         . 'ZINC ION'        ? 'Zn 2'           65.409  
# 
_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                   7NXX 
_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            2.32 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         47 
_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_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            273 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Hepes,1.5 M Lithium sulphate, pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'PSI JUNGFRAU 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-02-07 
_diffrn_detector.pdbx_frequency               ? 
# 
_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   0.97923 
_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                        'ESRF BEAMLINE ID29' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97923 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7NXX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1890 
_reflns.d_resolution_low                               58.57 
_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                                     29792 
_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                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.8 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_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                                    2.19 
_reflns_shell.d_res_low                                     2.26 
_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                             2455 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_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_Rsym_value                               ? 
_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                                  0.825 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                137.230 
_refine.B_iso_mean                               53.2605 
_refine.B_iso_min                                18.280 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 7NXX 
_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                            2.1890 
_refine.ls_d_res_low                             57.9150 
_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                     20091 
_refine.ls_number_reflns_R_free                  1008 
_refine.ls_number_reflns_R_work                  19083 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    67.1400 
_refine.ls_percent_reflns_R_free                 5.0200 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2042 
_refine.ls_R_factor_R_free                       0.2455 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2020 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.350 
_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                      2v0a 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.1300 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2400 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.1890 
_refine_hist.d_res_low                        57.9150 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2145 
_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       289 
_refine_hist.pdbx_B_iso_mean_ligand           47.58 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2143 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_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' ? 0.007  ? 2189 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.915  ? 2962 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.057  ? 314  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 396  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.273 ? 1281 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 2.1894 2.3048  . . 39  767  19.0000  . . . 0.4727 0.0000 0.3553 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.3048 2.4492  . . 81  1483 37.0000  . . . 0.3542 0.0000 0.3208 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.4492 2.6384  . . 103 2100 52.0000  . . . 0.3108 0.0000 0.3020 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.6384 2.9039  . . 156 2751 69.0000  . . . 0.3314 0.0000 0.3024 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.9039 3.3240  . . 204 3611 89.0000  . . . 0.2881 0.0000 0.2650 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.3240 4.1877  . . 215 4084 100.0000 . . . 0.2559 0.0000 0.1871 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.1877 57.9150 . . 210 4287 100.0000 . . . 0.1704 0.0000 0.1440 . . . . . . . . . . . 
# 
_struct.entry_id                     7NXX 
_struct.title                        'Structure of Superoxide Dismutase 1 (SOD1) in complex with nanobody 2 (Nb2).' 
_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        7NXX 
_struct_keywords.text            
;Cu/Zn superoxide dismutase metalloenzyme binding catalysing the dismutation of superoxides into hydrogen peroxide, METAL BINDING PROTEIN
;
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
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 CYS A 57  ? GLY A 61  ? CYS A 57  GLY A 61  5 ? 5 
HELX_P HELX_P2 AA2 GLU A 132 ? LYS A 136 ? GLU A 132 LYS A 136 5 ? 5 
HELX_P HELX_P3 AA3 ASP B 67  ? GLU B 70  ? ASP B 67  GLU B 70  5 ? 4 
HELX_P HELX_P4 AA4 LYS B 79  ? GLN B 81  ? LYS B 79  GLN B 81  5 ? 3 
HELX_P HELX_P5 AA5 LYS B 92  ? THR B 96  ? LYS B 92  THR B 96  5 ? 5 
HELX_P HELX_P6 AA6 SER B 115 ? MET B 119 ? SER B 115 MET B 119 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
disulf2 disulf ? ? B CYS 24  SG  ? ? ? 1_555 B CYS 101 SG ? ? B CYS 24  B CYS 101 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc1 metalc ? ? A HIS 46  ND1 ? ? ? 1_555 C CU  .   CU A ? A HIS 46  A CU  201 1_555 ? ? ? ? ? ? ? 2.116 ? ? 
metalc2 metalc ? ? A HIS 48  NE2 ? ? ? 1_555 C CU  .   CU A ? A HIS 48  A CU  201 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc3 metalc ? ? A HIS 71  ND1 ? ? ? 1_555 D ZN  .   ZN A ? A HIS 71  A ZN  202 1_555 ? ? ? ? ? ? ? 1.920 ? ? 
metalc4 metalc ? ? A HIS 80  ND1 ? ? ? 1_555 D ZN  .   ZN A ? A HIS 80  A ZN  202 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc5 metalc ? ? A ASP 83  OD1 ? ? ? 1_555 D ZN  .   ZN A ? A ASP 83  A ZN  202 1_555 ? ? ? ? ? ? ? 2.224 ? ? 
metalc6 metalc ? ? A HIS 120 NE2 ? ? ? 1_555 C CU  .   CU A ? A HIS 120 A CU  201 1_555 ? ? ? ? ? ? ? 2.149 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 6 ? 
AA5 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? 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 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
AA1 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA1 3 GLN A 15  ? GLU A 21  ? GLN A 15  GLU A 21  
AA1 4 LYS A 3   ? LEU A 8   ? LYS A 3   LEU A 8   
AA1 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
AA2 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
AA2 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
AA2 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
AA2 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
AA3 1 GLN B 5   ? SER B 9   ? GLN B 5   SER B 9   
AA3 2 LEU B 20  ? SER B 27  ? LEU B 20  SER B 27  
AA3 3 THR B 83  ? MET B 88  ? THR B 83  MET B 88  
AA3 4 PHE B 73  ? ASP B 78  ? PHE B 73  ASP B 78  
AA4 1 SER B 13  ? GLN B 15  ? SER B 13  GLN B 15  
AA4 2 THR B 126 ? SER B 131 ? THR B 126 SER B 131 
AA4 3 ALA B 97  ? ASN B 105 ? ALA B 97  ASN B 105 
AA4 4 TYR B 37  ? GLN B 44  ? TYR B 37  GLN B 44  
AA4 5 GLU B 51  ? TYR B 57  ? GLU B 51  TYR B 57  
AA4 6 THR B 63  ? TYR B 65  ? THR B 63  TYR B 65  
AA5 1 SER B 13  ? GLN B 15  ? SER B 13  GLN B 15  
AA5 2 THR B 126 ? SER B 131 ? THR B 126 SER B 131 
AA5 3 ALA B 97  ? ASN B 105 ? ALA B 97  ASN B 105 
AA5 4 THR B 121 ? TRP B 122 ? THR B 121 TRP B 122 
# 
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 O ASP A 101 ? O ASP A 101 N VAL A 29  ? N VAL A 29  
AA1 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
AA1 3 4 O PHE A 20  ? O PHE A 20  N ALA A 4   ? N ALA A 4   
AA1 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
AA2 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
AA2 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
AA2 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
AA3 1 2 N GLN B 7   ? N GLN B 7   O VAL B 25  ? O VAL B 25  
AA3 2 3 N LEU B 20  ? N LEU B 20  O MET B 88  ? O MET B 88  
AA3 3 4 O GLN B 87  ? O GLN B 87  N THR B 74  ? N THR B 74  
AA4 1 2 N VAL B 14  ? N VAL B 14  O SER B 131 ? O SER B 131 
AA4 2 3 O THR B 126 ? O THR B 126 N TYR B 99  ? N TYR B 99  
AA4 3 4 O TYR B 100 ? O TYR B 100 N TYR B 42  ? N TYR B 42  
AA4 4 5 N TRP B 41  ? N TRP B 41  O VAL B 53  ? O VAL B 53  
AA4 5 6 N THR B 55  ? N THR B 55  O TYR B 64  ? O TYR B 64  
AA5 1 2 N VAL B 14  ? N VAL B 14  O SER B 131 ? O SER B 131 
AA5 2 3 O THR B 126 ? O THR B 126 N TYR B 99  ? N TYR B 99  
AA5 3 4 N ALA B 103 ? N ALA B 103 O THR B 121 ? O THR B 121 
# 
_atom_sites.entry_id                    7NXX 
_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.fract_transf_matrix[1][1]   0.008633 
_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]   0.008633 
_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]   0.011935 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
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   . ALA A 1 1   ? 59.356 66.338  19.896 0.90 100.06 ?  1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 59.366 67.789  19.730 0.90 96.85  ?  1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 60.012 68.488  20.932 0.90 90.23  ?  1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 60.054 67.943  22.039 0.90 83.82  ?  1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 57.948 68.307  19.506 0.90 93.50  ?  1   ALA A CB  1 
ATOM   6    N  N   A THR A 1 2   ? 60.522 69.698  20.703 0.99 88.03  ?  2   THR A N   1 
ATOM   7    C  CA  A THR A 1 2   ? 61.160 70.478  21.753 0.99 88.05  ?  2   THR A CA  1 
ATOM   8    C  C   A THR A 1 2   ? 60.420 71.773  22.097 0.99 78.27  ?  2   THR A C   1 
ATOM   9    O  O   A THR A 1 2   ? 60.788 72.424  23.084 0.99 67.86  ?  2   THR A O   1 
ATOM   10   C  CB  A THR A 1 2   ? 62.616 70.793  21.360 0.99 84.46  ?  2   THR A CB  1 
ATOM   11   O  OG1 A THR A 1 2   ? 62.646 71.410  20.064 0.99 77.46  ?  2   THR A OG1 1 
ATOM   12   C  CG2 A THR A 1 2   ? 63.453 69.509  21.331 0.99 83.53  ?  2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 59.374 72.141  21.342 1.00 72.00  ?  3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 58.601 73.368  21.542 1.00 66.32  ?  3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 57.108 73.066  21.476 1.00 67.06  ?  3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 56.651 72.439  20.513 1.00 63.57  ?  3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 58.942 74.420  20.474 1.00 63.91  ?  3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 59.744 75.598  20.967 1.00 67.67  ?  3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 60.043 76.603  19.851 1.00 72.38  ?  3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 60.768 77.821  20.431 1.00 78.85  ?  3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 61.375 78.726  19.410 1.00 80.83  1  3   LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 56.342 73.543  22.470 1.00 65.28  ?  4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 54.886 73.386  22.477 1.00 54.34  ?  4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 54.203 74.655  22.978 1.00 60.48  ?  4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 54.821 75.515  23.617 1.00 59.25  ?  4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 54.434 72.205  23.340 1.00 46.00  ?  4   ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 52.895 74.740  22.703 1.00 60.01  ?  5   VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 52.115 75.952  22.940 1.00 54.49  ?  5   VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 50.654 75.593  23.180 1.00 48.47  ?  5   VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 50.157 74.553  22.742 1.00 43.96  ?  5   VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 52.230 76.931  21.752 1.00 48.87  ?  5   VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 51.522 76.351  20.554 1.00 46.13  ?  5   VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 51.691 78.302  22.117 1.00 38.94  ?  5   VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? 49.945 76.489  23.851 1.00 51.87  ?  6   CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? 48.620 76.157  24.348 1.00 50.60  ?  6   CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? 47.803 77.436  24.442 1.00 49.81  ?  6   CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? 48.291 78.431  24.990 1.00 45.91  ?  6   CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? 48.738 75.473  25.715 1.00 47.90  ?  6   CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? 47.186 75.055  26.464 1.00 54.14  ?  6   CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? 46.588 77.417  23.886 1.00 48.50  ?  7   VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? 45.631 78.513  24.029 1.00 48.29  ?  7   VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? 44.581 78.082  25.038 1.00 48.39  ?  7   VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? 43.861 77.106  24.805 1.00 52.14  ?  7   VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? 44.960 78.891  22.701 1.00 37.10  ?  7   VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? 44.119 80.117  22.906 1.00 38.35  ?  7   VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? 45.987 79.172  21.654 1.00 49.51  ?  7   VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? 44.474 78.823  26.142 1.00 46.50  ?  8   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? 43.519 78.525  27.200 1.00 45.74  ?  8   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? 42.293 79.415  27.044 1.00 49.20  ?  8   LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? 42.406 80.643  27.082 1.00 55.04  ?  8   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? 44.151 78.742  28.565 1.00 41.82  ?  8   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? 45.401 77.928  28.791 1.00 44.73  ?  8   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 8   ? 46.559 78.880  28.878 1.00 46.06  ?  8   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 8   ? 45.252 77.142  30.056 1.00 46.82  ?  8   LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 9   ? 41.124 78.795  26.881 1.00 46.69  ?  9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 39.852 79.503  26.874 1.00 40.48  ?  9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 38.854 78.728  27.728 1.00 46.23  ?  9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 39.046 77.538  27.999 1.00 49.90  ?  9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 39.312 79.709  25.440 1.00 43.57  ?  9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 40.317 80.272  24.420 1.00 67.22  ?  9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 40.016 81.769  24.132 1.00 80.26  ?  9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 41.185 82.537  23.466 1.00 79.14  ?  9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 42.385 82.737  24.359 1.00 79.37  1  9   LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 10  ? 37.795 79.419  28.166 1.00 49.98  ?  10  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 10  ? 36.778 78.817  29.007 1.00 50.91  ?  10  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 10  ? 35.481 79.614  29.036 1.00 50.49  ?  10  GLY A C   1 
ATOM   67   O  O   . GLY A 1 10  ? 35.246 80.476  28.190 1.00 49.83  ?  10  GLY A O   1 
ATOM   68   N  N   . ASP A 1 11  ? 34.641 79.316  30.041 1.00 52.83  ?  11  ASP A N   1 
ATOM   69   C  CA  . ASP A 1 11  ? 33.325 79.954  30.150 1.00 47.45  ?  11  ASP A CA  1 
ATOM   70   C  C   . ASP A 1 11  ? 33.437 81.448  30.403 1.00 47.25  ?  11  ASP A C   1 
ATOM   71   O  O   . ASP A 1 11  ? 32.835 82.258  29.691 1.00 56.71  ?  11  ASP A O   1 
ATOM   72   C  CB  . ASP A 1 11  ? 32.515 79.312  31.274 1.00 51.16  ?  11  ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 11  ? 31.814 78.079  30.833 1.00 68.11  ?  11  ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 11  ? 32.182 77.558  29.761 1.00 85.41  ?  11  ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 11  ? 30.901 77.624  31.552 1.00 77.43  -1 11  ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 12  ? 34.173 81.830  31.436 1.00 45.57  ?  12  GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? 34.267 83.214  31.820 1.00 26.79  ?  12  GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? 35.286 83.968  31.001 1.00 39.75  ?  12  GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? 35.605 83.610  29.862 1.00 53.18  ?  12  GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? 35.831 85.034  31.586 1.00 38.54  ?  13  PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? 36.757 85.898  30.848 1.00 41.54  ?  13  PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? 38.181 85.388  30.817 1.00 41.07  ?  13  PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? 39.036 86.046  30.218 1.00 46.01  ?  13  PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? 36.686 87.206  31.636 1.00 42.30  ?  13  PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? 36.549 86.718  33.075 1.00 35.81  ?  13  PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? 35.695 85.449  32.998 1.00 30.88  ?  13  PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? 38.481 84.261  31.459 1.00 44.12  ?  14  VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? 39.877 83.879  31.612 1.00 45.57  ?  14  VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? 40.387 83.352  30.281 1.00 47.29  ?  14  VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? 39.724 82.542  29.617 1.00 45.79  ?  14  VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? 40.049 82.857  32.749 1.00 37.85  ?  14  VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? 41.470 82.379  32.820 1.00 30.61  ?  14  VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? 39.682 83.485  34.088 1.00 37.79  ?  14  VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? 41.551 83.848  29.865 1.00 42.28  ?  15  GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? 42.191 83.398  28.641 1.00 39.72  ?  15  GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? 43.691 83.637  28.754 1.00 47.02  ?  15  GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? 44.155 84.430  29.584 1.00 44.83  ?  15  GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? 41.610 84.108  27.411 1.00 41.81  ?  15  GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? 41.508 85.599  27.560 1.00 44.73  ?  15  GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? 41.626 86.321  26.239 1.00 50.78  ?  15  GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? 42.725 86.650  25.812 1.00 56.47  ?  15  GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? 40.496 86.579  25.589 1.00 57.70  ?  15  GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 16  ? 44.450 82.921  27.930 1.00 48.38  ?  16  GLY A N   1 
ATOM   104  C  CA  . GLY A 1 16  ? 45.877 83.169  27.861 1.00 47.97  ?  16  GLY A CA  1 
ATOM   105  C  C   . GLY A 1 16  ? 46.552 82.239  26.876 1.00 38.65  ?  16  GLY A C   1 
ATOM   106  O  O   . GLY A 1 16  ? 45.909 81.436  26.199 1.00 41.05  ?  16  GLY A O   1 
ATOM   107  N  N   . ILE A 1 17  ? 47.876 82.379  26.812 1.00 48.12  ?  17  ILE A N   1 
ATOM   108  C  CA  . ILE A 1 17  ? 48.752 81.581  25.961 1.00 47.01  ?  17  ILE A CA  1 
ATOM   109  C  C   . ILE A 1 17  ? 49.937 81.121  26.803 1.00 47.46  ?  17  ILE A C   1 
ATOM   110  O  O   . ILE A 1 17  ? 50.535 81.925  27.524 1.00 48.38  ?  17  ILE A O   1 
ATOM   111  C  CB  . ILE A 1 17  ? 49.233 82.395  24.747 1.00 38.69  ?  17  ILE A CB  1 
ATOM   112  C  CG1 . ILE A 1 17  ? 48.038 82.804  23.894 1.00 34.45  ?  17  ILE A CG1 1 
ATOM   113  C  CG2 . ILE A 1 17  ? 50.198 81.599  23.913 1.00 45.08  ?  17  ILE A CG2 1 
ATOM   114  C  CD1 . ILE A 1 17  ? 48.354 83.965  22.992 1.00 35.34  ?  17  ILE A CD1 1 
ATOM   115  N  N   . ILE A 1 18  ? 50.270 79.833  26.727 1.00 48.63  ?  18  ILE A N   1 
ATOM   116  C  CA  . ILE A 1 18  ? 51.414 79.281  27.446 1.00 43.05  ?  18  ILE A CA  1 
ATOM   117  C  C   . ILE A 1 18  ? 52.340 78.586  26.452 1.00 53.17  ?  18  ILE A C   1 
ATOM   118  O  O   . ILE A 1 18  ? 51.874 77.819  25.598 1.00 52.84  ?  18  ILE A O   1 
ATOM   119  C  CB  . ILE A 1 18  ? 50.970 78.307  28.552 1.00 38.07  ?  18  ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 18  ? 50.174 79.047  29.617 1.00 39.61  ?  18  ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 18  ? 52.162 77.625  29.179 1.00 44.97  ?  18  ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 18  ? 50.963 80.119  30.324 1.00 45.94  ?  18  ILE A CD1 1 
ATOM   123  N  N   . ASN A 1 19  ? 53.649 78.852  26.565 1.00 47.80  ?  19  ASN A N   1 
ATOM   124  C  CA  . ASN A 1 19  ? 54.655 78.181  25.752 1.00 41.59  ?  19  ASN A CA  1 
ATOM   125  C  C   . ASN A 1 19  ? 55.436 77.170  26.579 1.00 51.72  ?  19  ASN A C   1 
ATOM   126  O  O   . ASN A 1 19  ? 55.586 77.317  27.800 1.00 50.45  ?  19  ASN A O   1 
ATOM   127  C  CB  . ASN A 1 19  ? 55.642 79.164  25.113 1.00 34.64  ?  19  ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 19  ? 54.959 80.176  24.221 1.00 41.93  ?  19  ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 19  ? 54.447 81.191  24.680 1.00 48.04  ?  19  ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 19  ? 54.861 79.847  22.941 1.00 42.37  ?  19  ASN A ND2 1 
ATOM   131  N  N   . PHE A 1 20  ? 55.943 76.142  25.886 1.00 52.40  ?  20  PHE A N   1 
ATOM   132  C  CA  . PHE A 1 20  ? 56.763 75.094  26.480 1.00 55.76  ?  20  PHE A CA  1 
ATOM   133  C  C   . PHE A 1 20  ? 58.048 74.926  25.686 1.00 63.78  ?  20  PHE A C   1 
ATOM   134  O  O   . PHE A 1 20  ? 58.043 75.039  24.453 1.00 64.94  ?  20  PHE A O   1 
ATOM   135  C  CB  . PHE A 1 20  ? 56.043 73.752  26.502 1.00 55.61  ?  20  PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 20  ? 54.767 73.758  27.280 1.00 55.27  ?  20  PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 20  ? 54.755 73.369  28.606 1.00 48.39  ?  20  PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 20  ? 53.569 74.134  26.676 1.00 53.50  ?  20  PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 20  ? 53.577 73.361  29.318 1.00 48.60  ?  20  PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 20  ? 52.381 74.124  27.381 1.00 45.64  ?  20  PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 20  ? 52.381 73.739  28.701 1.00 49.20  ?  20  PHE A CZ  1 
ATOM   142  N  N   . GLU A 1 21  ? 59.139 74.633  26.401 1.00 64.59  ?  21  GLU A N   1 
ATOM   143  C  CA  . GLU A 1 21  ? 60.425 74.302  25.795 1.00 61.72  ?  21  GLU A CA  1 
ATOM   144  C  C   . GLU A 1 21  ? 61.187 73.351  26.706 1.00 63.58  ?  21  GLU A C   1 
ATOM   145  O  O   . GLU A 1 21  ? 61.363 73.631  27.899 1.00 63.02  ?  21  GLU A O   1 
ATOM   146  C  CB  . GLU A 1 21  ? 61.265 75.555  25.543 1.00 66.01  ?  21  GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 21  ? 61.415 75.957  24.083 1.00 79.82  ?  21  GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 21  ? 62.565 76.939  23.873 1.00 95.94  ?  21  GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 21  ? 63.730 76.536  24.099 1.00 101.98 ?  21  GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 21  ? 62.309 78.111  23.502 1.00 95.95  -1 21  GLU A OE2 1 
ATOM   151  N  N   . GLN A 1 22  ? 61.612 72.218  26.150 1.00 59.84  ?  22  GLN A N   1 
ATOM   152  C  CA  . GLN A 1 22  ? 62.741 71.462  26.682 1.00 75.32  ?  22  GLN A CA  1 
ATOM   153  C  C   . GLN A 1 22  ? 63.733 71.329  25.532 1.00 81.65  ?  22  GLN A C   1 
ATOM   154  O  O   . GLN A 1 22  ? 63.457 70.660  24.527 1.00 69.11  ?  22  GLN A O   1 
ATOM   155  C  CB  . GLN A 1 22  ? 62.328 70.107  27.278 1.00 69.51  ?  22  GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 22  ? 61.806 69.045  26.333 1.00 66.91  ?  22  GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 22  ? 61.692 67.693  27.009 1.00 68.57  ?  22  GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 22  ? 61.911 67.570  28.223 1.00 62.59  ?  22  GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 22  ? 61.390 66.659  26.221 1.00 69.58  ?  22  GLN A NE2 1 
ATOM   160  N  N   . LYS A 1 23  ? 64.859 72.027  25.653 1.00 94.28  ?  23  LYS A N   1 
ATOM   161  C  CA  . LYS A 1 23  ? 65.822 72.092  24.565 1.00 98.04  ?  23  LYS A CA  1 
ATOM   162  C  C   . LYS A 1 23  ? 66.704 70.853  24.481 1.00 93.48  ?  23  LYS A C   1 
ATOM   163  O  O   . LYS A 1 23  ? 67.561 70.787  23.595 1.00 91.62  ?  23  LYS A O   1 
ATOM   164  C  CB  . LYS A 1 23  ? 66.682 73.358  24.689 1.00 99.13  ?  23  LYS A CB  1 
ATOM   165  C  CG  . LYS A 1 23  ? 67.326 73.580  26.046 1.00 106.15 ?  23  LYS A CG  1 
ATOM   166  C  CD  . LYS A 1 23  ? 67.621 75.067  26.271 1.00 108.67 ?  23  LYS A CD  1 
ATOM   167  C  CE  . LYS A 1 23  ? 67.608 75.450  27.758 1.00 105.01 ?  23  LYS A CE  1 
ATOM   168  N  NZ  . LYS A 1 23  ? 68.618 76.512  28.103 1.00 98.26  1  23  LYS A NZ  1 
ATOM   169  N  N   . GLU A 1 24  ? 66.514 69.869  25.357 1.00 88.42  ?  24  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 24  ? 67.194 68.592  25.203 1.00 97.53  ?  24  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 24  ? 66.378 67.503  25.882 1.00 90.06  ?  24  GLU A C   1 
ATOM   172  O  O   . GLU A 1 24  ? 65.820 67.719  26.962 1.00 81.22  ?  24  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 24  ? 68.623 68.628  25.765 1.00 107.53 ?  24  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 24  ? 68.740 69.064  27.214 1.00 114.31 ?  24  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 24  ? 69.906 68.395  27.932 1.00 116.81 ?  24  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 24  ? 69.751 67.227  28.366 1.00 117.58 ?  24  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 24  ? 70.976 69.034  28.054 1.00 114.18 -1 24  GLU A OE2 1 
ATOM   178  N  N   . SER A 1 25  ? 66.333 66.335  25.231 1.00 86.45  ?  25  SER A N   1 
ATOM   179  C  CA  . SER A 1 25  ? 65.527 65.194  25.655 1.00 85.96  ?  25  SER A CA  1 
ATOM   180  C  C   . SER A 1 25  ? 65.650 64.918  27.148 1.00 88.97  ?  25  SER A C   1 
ATOM   181  O  O   . SER A 1 25  ? 66.743 64.979  27.720 1.00 100.85 ?  25  SER A O   1 
ATOM   182  C  CB  . SER A 1 25  ? 65.953 63.955  24.864 1.00 86.78  ?  25  SER A CB  1 
ATOM   183  O  OG  . SER A 1 25  ? 65.516 62.766  25.498 1.00 90.27  ?  25  SER A OG  1 
ATOM   184  N  N   . ASN A 1 26  ? 64.506 64.611  27.772 1.00 83.69  ?  26  ASN A N   1 
ATOM   185  C  CA  . ASN A 1 26  ? 64.412 64.266  29.197 1.00 93.75  ?  26  ASN A CA  1 
ATOM   186  C  C   . ASN A 1 26  ? 65.012 65.340  30.106 1.00 87.59  ?  26  ASN A C   1 
ATOM   187  O  O   . ASN A 1 26  ? 65.361 65.069  31.263 1.00 79.43  ?  26  ASN A O   1 
ATOM   188  C  CB  . ASN A 1 26  ? 65.055 62.904  29.490 1.00 109.12 ?  26  ASN A CB  1 
ATOM   189  C  CG  . ASN A 1 26  ? 64.117 61.741  29.193 1.00 119.37 ?  26  ASN A CG  1 
ATOM   190  O  OD1 . ASN A 1 26  ? 62.992 61.938  28.725 1.00 126.78 ?  26  ASN A OD1 1 
ATOM   191  N  ND2 . ASN A 1 26  ? 64.571 60.524  29.479 1.00 117.03 ?  26  ASN A ND2 1 
ATOM   192  N  N   . GLY A 1 27  ? 65.128 66.564  29.603 1.00 83.44  ?  27  GLY A N   1 
ATOM   193  C  CA  . GLY A 1 27  ? 65.588 67.670  30.400 1.00 81.38  ?  27  GLY A CA  1 
ATOM   194  C  C   . GLY A 1 27  ? 64.441 68.458  31.000 1.00 82.59  ?  27  GLY A C   1 
ATOM   195  O  O   . GLY A 1 27  ? 63.273 68.039  30.978 1.00 82.97  ?  27  GLY A O   1 
ATOM   196  N  N   . PRO A 1 28  ? 64.764 69.622  31.558 1.00 78.60  ?  28  PRO A N   1 
ATOM   197  C  CA  . PRO A 1 28  ? 63.735 70.451  32.196 1.00 82.12  ?  28  PRO A CA  1 
ATOM   198  C  C   . PRO A 1 28  ? 62.871 71.181  31.178 1.00 75.34  ?  28  PRO A C   1 
ATOM   199  O  O   . PRO A 1 28  ? 63.334 71.613  30.117 1.00 68.45  ?  28  PRO A O   1 
ATOM   200  C  CB  . PRO A 1 28  ? 64.549 71.444  33.041 1.00 78.30  ?  28  PRO A CB  1 
ATOM   201  C  CG  . PRO A 1 28  ? 65.938 70.870  33.105 1.00 80.80  ?  28  PRO A CG  1 
ATOM   202  C  CD  . PRO A 1 28  ? 66.117 70.132  31.817 1.00 78.67  ?  28  PRO A CD  1 
ATOM   203  N  N   . VAL A 1 29  ? 61.594 71.318  31.526 1.00 72.79  ?  29  VAL A N   1 
ATOM   204  C  CA  . VAL A 1 29  ? 60.612 72.018  30.706 1.00 70.60  ?  29  VAL A CA  1 
ATOM   205  C  C   . VAL A 1 29  ? 60.466 73.440  31.235 1.00 67.19  ?  29  VAL A C   1 
ATOM   206  O  O   . VAL A 1 29  ? 60.218 73.641  32.433 1.00 54.63  ?  29  VAL A O   1 
ATOM   207  C  CB  . VAL A 1 29  ? 59.260 71.280  30.710 1.00 68.49  ?  29  VAL A CB  1 
ATOM   208  C  CG1 . VAL A 1 29  ? 58.332 71.854  29.652 1.00 63.96  ?  29  VAL A CG1 1 
ATOM   209  C  CG2 . VAL A 1 29  ? 59.475 69.799  30.457 1.00 62.87  ?  29  VAL A CG2 1 
ATOM   210  N  N   . LYS A 1 30  ? 60.654 74.426  30.349 1.00 68.58  ?  30  LYS A N   1 
ATOM   211  C  CA  . LYS A 1 30  ? 60.403 75.834  30.648 1.00 70.81  ?  30  LYS A CA  1 
ATOM   212  C  C   . LYS A 1 30  ? 59.007 76.185  30.151 1.00 68.34  ?  30  LYS A C   1 
ATOM   213  O  O   . LYS A 1 30  ? 58.722 76.066  28.954 1.00 64.23  ?  30  LYS A O   1 
ATOM   214  C  CB  . LYS A 1 30  ? 61.441 76.748  29.993 1.00 76.83  ?  30  LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 30  ? 62.869 76.646  30.570 1.00 87.67  ?  30  LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 30  ? 62.914 76.853  32.093 1.00 79.64  ?  30  LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 30  ? 64.247 77.457  32.554 1.00 69.44  ?  30  LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 30  ? 65.448 76.642  32.174 1.00 59.53  1  30  LYS A NZ  1 
ATOM   219  N  N   . VAL A 1 31  ? 58.139 76.609  31.067 1.00 70.44  ?  31  VAL A N   1 
ATOM   220  C  CA  . VAL A 1 31  ? 56.764 76.985  30.748 1.00 67.22  ?  31  VAL A CA  1 
ATOM   221  C  C   . VAL A 1 31  ? 56.618 78.482  31.005 1.00 59.52  ?  31  VAL A C   1 
ATOM   222  O  O   . VAL A 1 31  ? 56.989 78.978  32.074 1.00 56.75  ?  31  VAL A O   1 
ATOM   223  C  CB  . VAL A 1 31  ? 55.739 76.148  31.552 1.00 70.06  ?  31  VAL A CB  1 
ATOM   224  C  CG1 . VAL A 1 31  ? 56.150 74.683  31.544 1.00 65.78  ?  31  VAL A CG1 1 
ATOM   225  C  CG2 . VAL A 1 31  ? 55.565 76.613  33.005 1.00 73.70  ?  31  VAL A CG2 1 
ATOM   226  N  N   . TRP A 1 32  ? 56.112 79.208  30.012 1.00 53.56  ?  32  TRP A N   1 
ATOM   227  C  CA  . TRP A 1 32  ? 56.055 80.661  30.102 1.00 47.11  ?  32  TRP A CA  1 
ATOM   228  C  C   . TRP A 1 32  ? 54.968 81.196  29.178 1.00 49.70  ?  32  TRP A C   1 
ATOM   229  O  O   . TRP A 1 32  ? 54.696 80.637  28.110 1.00 52.51  ?  32  TRP A O   1 
ATOM   230  C  CB  . TRP A 1 32  ? 57.413 81.289  29.760 1.00 43.92  ?  32  TRP A CB  1 
ATOM   231  C  CG  . TRP A 1 32  ? 57.910 80.979  28.357 1.00 52.73  ?  32  TRP A CG  1 
ATOM   232  C  CD1 . TRP A 1 32  ? 58.616 79.869  27.944 1.00 58.30  ?  32  TRP A CD1 1 
ATOM   233  C  CD2 . TRP A 1 32  ? 57.742 81.796  27.193 1.00 48.47  ?  32  TRP A CD2 1 
ATOM   234  N  NE1 . TRP A 1 32  ? 58.879 79.948  26.591 1.00 51.82  ?  32  TRP A NE1 1 
ATOM   235  C  CE2 . TRP A 1 32  ? 58.354 81.121  26.110 1.00 53.80  ?  32  TRP A CE2 1 
ATOM   236  C  CE3 . TRP A 1 32  ? 57.118 83.022  26.957 1.00 43.56  ?  32  TRP A CE3 1 
ATOM   237  C  CZ2 . TRP A 1 32  ? 58.365 81.641  24.820 1.00 57.70  ?  32  TRP A CZ2 1 
ATOM   238  C  CZ3 . TRP A 1 32  ? 57.125 83.533  25.674 1.00 46.28  ?  32  TRP A CZ3 1 
ATOM   239  C  CH2 . TRP A 1 32  ? 57.748 82.847  24.624 1.00 54.32  ?  32  TRP A CH2 1 
ATOM   240  N  N   . GLY A 1 33  ? 54.355 82.287  29.614 1.00 50.82  ?  33  GLY A N   1 
ATOM   241  C  CA  . GLY A 1 33  ? 53.198 82.864  28.955 1.00 44.92  ?  33  GLY A CA  1 
ATOM   242  C  C   . GLY A 1 33  ? 52.503 83.788  29.942 1.00 49.48  ?  33  GLY A C   1 
ATOM   243  O  O   . GLY A 1 33  ? 53.073 84.146  30.972 1.00 48.33  ?  33  GLY A O   1 
ATOM   244  N  N   . SER A 1 34  ? 51.260 84.149  29.626 1.00 49.01  ?  34  SER A N   1 
ATOM   245  C  CA  . SER A 1 34  ? 50.489 84.930  30.590 1.00 50.15  ?  34  SER A CA  1 
ATOM   246  C  C   . SER A 1 34  ? 48.997 84.690  30.400 1.00 45.63  ?  34  SER A C   1 
ATOM   247  O  O   . SER A 1 34  ? 48.518 84.452  29.287 1.00 51.33  ?  34  SER A O   1 
ATOM   248  C  CB  . SER A 1 34  ? 50.802 86.429  30.507 1.00 48.93  ?  34  SER A CB  1 
ATOM   249  O  OG  . SER A 1 34  ? 50.108 87.039  29.447 1.00 52.37  ?  34  SER A OG  1 
ATOM   250  N  N   . ILE A 1 35  ? 48.270 84.764  31.514 1.00 48.87  ?  35  ILE A N   1 
ATOM   251  C  CA  . ILE A 1 35  ? 46.840 84.484  31.579 1.00 43.28  ?  35  ILE A CA  1 
ATOM   252  C  C   . ILE A 1 35  ? 46.156 85.707  32.182 1.00 39.94  ?  35  ILE A C   1 
ATOM   253  O  O   . ILE A 1 35  ? 46.622 86.235  33.197 1.00 34.48  ?  35  ILE A O   1 
ATOM   254  C  CB  . ILE A 1 35  ? 46.581 83.216  32.415 1.00 44.32  ?  35  ILE A CB  1 
ATOM   255  C  CG1 . ILE A 1 35  ? 47.622 82.157  32.046 1.00 36.66  ?  35  ILE A CG1 1 
ATOM   256  C  CG2 . ILE A 1 35  ? 45.197 82.653  32.155 1.00 44.88  ?  35  ILE A CG2 1 
ATOM   257  C  CD1 . ILE A 1 35  ? 47.544 80.881  32.866 1.00 37.11  ?  35  ILE A CD1 1 
ATOM   258  N  N   . LYS A 1 36  ? 45.093 86.189  31.531 1.00 39.47  ?  36  LYS A N   1 
ATOM   259  C  CA  . LYS A 1 36  ? 44.357 87.379  31.944 1.00 36.55  ?  36  LYS A CA  1 
ATOM   260  C  C   . LYS A 1 36  ? 42.973 87.001  32.473 1.00 38.21  ?  36  LYS A C   1 
ATOM   261  O  O   . LYS A 1 36  ? 42.443 85.918  32.203 1.00 44.63  ?  36  LYS A O   1 
ATOM   262  C  CB  . LYS A 1 36  ? 44.159 88.374  30.777 1.00 41.60  ?  36  LYS A CB  1 
ATOM   263  C  CG  . LYS A 1 36  ? 45.106 88.289  29.607 1.00 44.98  ?  36  LYS A CG  1 
ATOM   264  C  CD  . LYS A 1 36  ? 46.451 88.875  29.970 1.00 54.02  ?  36  LYS A CD  1 
ATOM   265  C  CE  . LYS A 1 36  ? 47.439 88.849  28.808 1.00 48.07  ?  36  LYS A CE  1 
ATOM   266  N  NZ  . LYS A 1 36  ? 48.817 89.250  29.276 1.00 54.54  1  36  LYS A NZ  1 
ATOM   267  N  N   . GLY A 1 37  ? 42.346 87.948  33.171 1.00 31.04  ?  37  GLY A N   1 
ATOM   268  C  CA  . GLY A 1 37  ? 40.959 87.772  33.568 1.00 27.81  ?  37  GLY A CA  1 
ATOM   269  C  C   . GLY A 1 37  ? 40.761 86.964  34.826 1.00 34.29  ?  37  GLY A C   1 
ATOM   270  O  O   . GLY A 1 37  ? 39.618 86.613  35.148 1.00 36.93  ?  37  GLY A O   1 
ATOM   271  N  N   . LEU A 1 38  ? 41.840 86.642  35.531 1.00 37.66  ?  38  LEU A N   1 
ATOM   272  C  CA  . LEU A 1 38  ? 41.777 85.903  36.778 1.00 38.18  ?  38  LEU A CA  1 
ATOM   273  C  C   . LEU A 1 38  ? 41.526 86.841  37.948 1.00 44.87  ?  38  LEU A C   1 
ATOM   274  O  O   . LEU A 1 38  ? 41.781 88.047  37.886 1.00 52.79  ?  38  LEU A O   1 
ATOM   275  C  CB  . LEU A 1 38  ? 43.077 85.131  37.030 1.00 30.20  ?  38  LEU A CB  1 
ATOM   276  C  CG  . LEU A 1 38  ? 43.450 84.009  36.069 1.00 33.18  ?  38  LEU A CG  1 
ATOM   277  C  CD1 . LEU A 1 38  ? 44.953 83.789  36.043 1.00 36.83  ?  38  LEU A CD1 1 
ATOM   278  C  CD2 . LEU A 1 38  ? 42.737 82.740  36.465 1.00 35.99  ?  38  LEU A CD2 1 
ATOM   279  N  N   . THR A 1 39  ? 41.022 86.262  39.028 1.00 44.58  ?  39  THR A N   1 
ATOM   280  C  CA  . THR A 1 39  ? 40.939 86.979  40.287 1.00 39.60  ?  39  THR A CA  1 
ATOM   281  C  C   . THR A 1 39  ? 42.336 87.080  40.890 1.00 43.59  ?  39  THR A C   1 
ATOM   282  O  O   . THR A 1 39  ? 43.111 86.118  40.850 1.00 54.36  ?  39  THR A O   1 
ATOM   283  C  CB  . THR A 1 39  ? 39.975 86.255  41.228 1.00 39.72  ?  39  THR A CB  1 
ATOM   284  O  OG1 . THR A 1 39  ? 40.259 84.849  41.212 1.00 50.03  ?  39  THR A OG1 1 
ATOM   285  C  CG2 . THR A 1 39  ? 38.538 86.460  40.777 1.00 31.89  ?  39  THR A CG2 1 
ATOM   286  N  N   . GLU A 1 40  ? 42.670 88.260  41.415 1.00 43.68  ?  40  GLU A N   1 
ATOM   287  C  CA  . GLU A 1 40  ? 43.984 88.481  42.019 1.00 42.87  ?  40  GLU A CA  1 
ATOM   288  C  C   . GLU A 1 40  ? 44.274 87.408  43.058 1.00 40.35  ?  40  GLU A C   1 
ATOM   289  O  O   . GLU A 1 40  ? 43.403 87.060  43.857 1.00 51.40  ?  40  GLU A O   1 
ATOM   290  C  CB  . GLU A 1 40  ? 44.028 89.874  42.652 1.00 41.08  ?  40  GLU A CB  1 
ATOM   291  C  CG  . GLU A 1 40  ? 45.251 90.167  43.501 1.00 47.11  ?  40  GLU A CG  1 
ATOM   292  C  CD  . GLU A 1 40  ? 45.275 91.623  43.979 1.00 54.56  ?  40  GLU A CD  1 
ATOM   293  O  OE1 . GLU A 1 40  ? 44.192 92.252  44.047 1.00 56.01  ?  40  GLU A OE1 1 
ATOM   294  O  OE2 . GLU A 1 40  ? 46.373 92.139  44.287 1.00 63.99  -1 40  GLU A OE2 1 
ATOM   295  N  N   . GLY A 1 41  ? 45.482 86.840  43.008 1.00 40.16  ?  41  GLY A N   1 
ATOM   296  C  CA  . GLY A 1 41  ? 45.853 85.762  43.909 1.00 34.41  ?  41  GLY A CA  1 
ATOM   297  C  C   . GLY A 1 41  ? 46.259 84.469  43.221 1.00 47.66  ?  41  GLY A C   1 
ATOM   298  O  O   . GLY A 1 41  ? 46.546 84.473  42.019 1.00 54.98  ?  41  GLY A O   1 
ATOM   299  N  N   . LEU A 1 42  ? 46.257 83.352  43.958 1.00 42.55  ?  42  LEU A N   1 
ATOM   300  C  CA  . LEU A 1 42  ? 46.799 82.084  43.468 1.00 48.40  ?  42  LEU A CA  1 
ATOM   301  C  C   . LEU A 1 42  ? 45.743 81.222  42.781 1.00 46.01  ?  42  LEU A C   1 
ATOM   302  O  O   . LEU A 1 42  ? 44.586 81.177  43.206 1.00 49.17  ?  42  LEU A O   1 
ATOM   303  C  CB  . LEU A 1 42  ? 47.409 81.288  44.618 1.00 51.85  ?  42  LEU A CB  1 
ATOM   304  C  CG  . LEU A 1 42  ? 48.863 81.562  44.986 1.00 46.01  ?  42  LEU A CG  1 
ATOM   305  C  CD1 . LEU A 1 42  ? 49.072 82.981  45.498 1.00 59.22  ?  42  LEU A CD1 1 
ATOM   306  C  CD2 . LEU A 1 42  ? 49.243 80.572  46.030 1.00 40.64  ?  42  LEU A CD2 1 
ATOM   307  N  N   . HIS A 1 43  ? 46.166 80.495  41.744 1.00 44.24  ?  43  HIS A N   1 
ATOM   308  C  CA  . HIS A 1 43  ? 45.270 79.633  40.979 1.00 44.70  ?  43  HIS A CA  1 
ATOM   309  C  C   . HIS A 1 43  ? 45.973 78.338  40.592 1.00 52.74  ?  43  HIS A C   1 
ATOM   310  O  O   . HIS A 1 43  ? 47.095 78.366  40.073 1.00 48.24  ?  43  HIS A O   1 
ATOM   311  C  CB  . HIS A 1 43  ? 44.771 80.349  39.721 1.00 40.80  ?  43  HIS A CB  1 
ATOM   312  C  CG  . HIS A 1 43  ? 43.900 81.525  40.014 1.00 38.92  ?  43  HIS A CG  1 
ATOM   313  N  ND1 . HIS A 1 43  ? 42.546 81.405  40.241 1.00 41.36  ?  43  HIS A ND1 1 
ATOM   314  C  CD2 . HIS A 1 43  ? 44.191 82.840  40.154 1.00 36.81  ?  43  HIS A CD2 1 
ATOM   315  C  CE1 . HIS A 1 43  ? 42.036 82.599  40.483 1.00 45.51  ?  43  HIS A CE1 1 
ATOM   316  N  NE2 . HIS A 1 43  ? 43.014 83.487  40.441 1.00 43.46  ?  43  HIS A NE2 1 
ATOM   317  N  N   . GLY A 1 44  ? 45.296 77.212  40.821 1.00 52.06  ?  44  GLY A N   1 
ATOM   318  C  CA  . GLY A 1 44  ? 45.878 75.925  40.485 1.00 54.43  ?  44  GLY A CA  1 
ATOM   319  C  C   . GLY A 1 44  ? 46.146 75.782  38.999 1.00 53.70  ?  44  GLY A C   1 
ATOM   320  O  O   . GLY A 1 44  ? 45.451 76.351  38.155 1.00 62.19  ?  44  GLY A O   1 
ATOM   321  N  N   . PHE A 1 45  ? 47.141 74.952  38.682 1.00 52.15  ?  45  PHE A N   1 
ATOM   322  C  CA  . PHE A 1 45  ? 47.776 74.952  37.365 1.00 48.90  ?  45  PHE A CA  1 
ATOM   323  C  C   . PHE A 1 45  ? 48.331 73.553  37.117 1.00 52.59  ?  45  PHE A C   1 
ATOM   324  O  O   . PHE A 1 45  ? 49.414 73.227  37.608 1.00 58.81  ?  45  PHE A O   1 
ATOM   325  C  CB  . PHE A 1 45  ? 48.878 75.999  37.335 1.00 44.89  ?  45  PHE A CB  1 
ATOM   326  C  CG  . PHE A 1 45  ? 49.344 76.365  35.959 1.00 49.43  ?  45  PHE A CG  1 
ATOM   327  C  CD1 . PHE A 1 45  ? 48.440 76.741  34.978 1.00 50.06  ?  45  PHE A CD1 1 
ATOM   328  C  CD2 . PHE A 1 45  ? 50.697 76.383  35.658 1.00 48.31  ?  45  PHE A CD2 1 
ATOM   329  C  CE1 . PHE A 1 45  ? 48.877 77.099  33.706 1.00 41.62  ?  45  PHE A CE1 1 
ATOM   330  C  CE2 . PHE A 1 45  ? 51.138 76.749  34.398 1.00 36.91  ?  45  PHE A CE2 1 
ATOM   331  C  CZ  . PHE A 1 45  ? 50.222 77.102  33.418 1.00 41.28  ?  45  PHE A CZ  1 
ATOM   332  N  N   . HIS A 1 46  ? 47.601 72.729  36.366 1.00 46.67  ?  46  HIS A N   1 
ATOM   333  C  CA  . HIS A 1 46  ? 48.058 71.369  36.119 1.00 46.44  ?  46  HIS A CA  1 
ATOM   334  C  C   . HIS A 1 46  ? 47.800 70.968  34.674 1.00 47.72  ?  46  HIS A C   1 
ATOM   335  O  O   . HIS A 1 46  ? 47.027 71.605  33.955 1.00 53.45  ?  46  HIS A O   1 
ATOM   336  C  CB  . HIS A 1 46  ? 47.370 70.366  37.050 1.00 49.92  ?  46  HIS A CB  1 
ATOM   337  C  CG  . HIS A 1 46  ? 46.855 70.975  38.314 1.00 48.77  ?  46  HIS A CG  1 
ATOM   338  N  ND1 . HIS A 1 46  ? 45.533 71.335  38.480 1.00 48.96  ?  46  HIS A ND1 1 
ATOM   339  C  CD2 . HIS A 1 46  ? 47.484 71.293  39.471 1.00 49.48  ?  46  HIS A CD2 1 
ATOM   340  C  CE1 . HIS A 1 46  ? 45.371 71.846  39.688 1.00 53.12  ?  46  HIS A CE1 1 
ATOM   341  N  NE2 . HIS A 1 46  ? 46.540 71.833  40.309 1.00 49.76  ?  46  HIS A NE2 1 
ATOM   342  N  N   . VAL A 1 47  ? 48.467 69.887  34.268 1.00 53.56  ?  47  VAL A N   1 
ATOM   343  C  CA  . VAL A 1 47  ? 48.222 69.209  32.997 1.00 51.26  ?  47  VAL A CA  1 
ATOM   344  C  C   . VAL A 1 47  ? 47.301 68.026  33.266 1.00 48.60  ?  47  VAL A C   1 
ATOM   345  O  O   . VAL A 1 47  ? 47.659 67.126  34.037 1.00 60.51  ?  47  VAL A O   1 
ATOM   346  C  CB  . VAL A 1 47  ? 49.536 68.735  32.354 1.00 46.48  ?  47  VAL A CB  1 
ATOM   347  C  CG1 . VAL A 1 47  ? 49.237 67.914  31.105 1.00 42.27  ?  47  VAL A CG1 1 
ATOM   348  C  CG2 . VAL A 1 47  ? 50.436 69.918  32.019 1.00 43.97  ?  47  VAL A CG2 1 
ATOM   349  N  N   . HIS A 1 48  ? 46.112 68.026  32.651 1.00 47.65  ?  48  HIS A N   1 
ATOM   350  C  CA  . HIS A 1 48  ? 45.161 66.927  32.778 1.00 44.91  ?  48  HIS A CA  1 
ATOM   351  C  C   . HIS A 1 48  ? 45.348 65.934  31.631 1.00 50.97  ?  48  HIS A C   1 
ATOM   352  O  O   . HIS A 1 48  ? 46.026 66.219  30.638 1.00 53.55  ?  48  HIS A O   1 
ATOM   353  C  CB  . HIS A 1 48  ? 43.720 67.444  32.824 1.00 40.25  ?  48  HIS A CB  1 
ATOM   354  C  CG  . HIS A 1 48  ? 43.406 68.230  34.058 1.00 40.24  ?  48  HIS A CG  1 
ATOM   355  N  ND1 . HIS A 1 48  ? 42.312 67.979  34.860 1.00 47.39  ?  48  HIS A ND1 1 
ATOM   356  C  CD2 . HIS A 1 48  ? 44.076 69.247  34.646 1.00 46.59  ?  48  HIS A CD2 1 
ATOM   357  C  CE1 . HIS A 1 48  ? 42.312 68.826  35.879 1.00 46.86  ?  48  HIS A CE1 1 
ATOM   358  N  NE2 . HIS A 1 48  ? 43.371 69.608  35.770 1.00 48.21  ?  48  HIS A NE2 1 
ATOM   359  N  N   . GLU A 1 49  ? 44.728 64.754  31.781 1.00 50.50  ?  49  GLU A N   1 
ATOM   360  C  CA  . GLU A 1 49  ? 45.173 63.576  31.034 1.00 48.40  ?  49  GLU A CA  1 
ATOM   361  C  C   . GLU A 1 49  ? 44.789 63.636  29.555 1.00 51.00  ?  49  GLU A C   1 
ATOM   362  O  O   . GLU A 1 49  ? 45.559 63.197  28.692 1.00 59.18  ?  49  GLU A O   1 
ATOM   363  C  CB  . GLU A 1 49  ? 44.610 62.298  31.669 1.00 47.63  ?  49  GLU A CB  1 
ATOM   364  C  CG  . GLU A 1 49  ? 44.965 61.040  30.884 1.00 48.06  ?  49  GLU A CG  1 
ATOM   365  C  CD  . GLU A 1 49  ? 44.542 59.750  31.564 1.00 55.69  ?  49  GLU A CD  1 
ATOM   366  O  OE1 . GLU A 1 49  ? 43.678 59.825  32.466 1.00 64.15  ?  49  GLU A OE1 1 
ATOM   367  O  OE2 . GLU A 1 49  ? 45.060 58.680  31.166 1.00 52.16  -1 49  GLU A OE2 1 
ATOM   368  N  N   . PHE A 1 50  ? 43.604 64.135  29.236 1.00 46.98  ?  50  PHE A N   1 
ATOM   369  C  CA  . PHE A 1 50  ? 43.100 64.068  27.874 1.00 49.43  ?  50  PHE A CA  1 
ATOM   370  C  C   . PHE A 1 50  ? 43.018 65.446  27.232 1.00 48.85  ?  50  PHE A C   1 
ATOM   371  O  O   . PHE A 1 50  ? 42.540 66.403  27.845 1.00 59.17  ?  50  PHE A O   1 
ATOM   372  C  CB  . PHE A 1 50  ? 41.725 63.417  27.842 1.00 44.25  ?  50  PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 50  ? 41.681 62.084  28.507 1.00 53.81  ?  50  PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 50  ? 41.075 61.923  29.742 1.00 51.31  ?  50  PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 50  ? 42.276 60.986  27.895 1.00 58.71  ?  50  PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 50  ? 41.034 60.678  30.339 1.00 54.72  ?  50  PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 50  ? 42.251 59.732  28.485 1.00 57.58  ?  50  PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 50  ? 41.632 59.575  29.708 1.00 57.37  ?  50  PHE A CZ  1 
ATOM   379  N  N   . GLY A 1 51  ? 43.475 65.529  25.986 1.00 48.54  ?  51  GLY A N   1 
ATOM   380  C  CA  . GLY A 1 51  ? 43.304 66.713  25.173 1.00 47.74  ?  51  GLY A CA  1 
ATOM   381  C  C   . GLY A 1 51  ? 42.023 66.619  24.376 1.00 55.52  ?  51  GLY A C   1 
ATOM   382  O  O   . GLY A 1 51  ? 42.017 66.725  23.145 1.00 60.88  ?  51  GLY A O   1 
ATOM   383  N  N   . ASP A 1 52  ? 40.926 66.379  25.080 1.00 55.47  ?  52  ASP A N   1 
ATOM   384  C  CA  . ASP A 1 52  ? 39.594 66.375  24.495 1.00 51.26  ?  52  ASP A CA  1 
ATOM   385  C  C   . ASP A 1 52  ? 38.862 67.543  25.134 1.00 44.57  ?  52  ASP A C   1 
ATOM   386  O  O   . ASP A 1 52  ? 38.552 67.502  26.331 1.00 50.81  ?  52  ASP A O   1 
ATOM   387  C  CB  . ASP A 1 52  ? 38.880 65.049  24.762 1.00 56.92  ?  52  ASP A CB  1 
ATOM   388  C  CG  . ASP A 1 52  ? 37.447 65.038  24.256 1.00 65.61  ?  52  ASP A CG  1 
ATOM   389  O  OD1 . ASP A 1 52  ? 37.137 64.264  23.324 1.00 61.54  ?  52  ASP A OD1 1 
ATOM   390  O  OD2 . ASP A 1 52  ? 36.628 65.819  24.775 1.00 69.01  -1 52  ASP A OD2 1 
ATOM   391  N  N   . ASN A 1 53  ? 38.617 68.596  24.362 1.00 45.71  ?  53  ASN A N   1 
ATOM   392  C  CA  . ASN A 1 53  ? 37.845 69.733  24.848 1.00 54.71  ?  53  ASN A CA  1 
ATOM   393  C  C   . ASN A 1 53  ? 36.481 69.818  24.177 1.00 55.92  ?  53  ASN A C   1 
ATOM   394  O  O   . ASN A 1 53  ? 35.944 70.910  24.003 1.00 54.29  ?  53  ASN A O   1 
ATOM   395  C  CB  . ASN A 1 53  ? 38.597 71.051  24.661 1.00 64.01  ?  53  ASN A CB  1 
ATOM   396  C  CG  . ASN A 1 53  ? 39.804 71.184  25.594 1.00 81.86  ?  53  ASN A CG  1 
ATOM   397  O  OD1 . ASN A 1 53  ? 40.009 70.373  26.507 1.00 84.48  ?  53  ASN A OD1 1 
ATOM   398  N  ND2 . ASN A 1 53  ? 40.599 72.224  25.371 1.00 86.91  ?  53  ASN A ND2 1 
ATOM   399  N  N   . THR A 1 54  ? 35.908 68.674  23.801 1.00 58.53  ?  54  THR A N   1 
ATOM   400  C  CA  . THR A 1 54  ? 34.598 68.688  23.160 1.00 46.18  ?  54  THR A CA  1 
ATOM   401  C  C   . THR A 1 54  ? 33.522 69.177  24.124 1.00 50.57  ?  54  THR A C   1 
ATOM   402  O  O   . THR A 1 54  ? 32.668 69.996  23.755 1.00 58.15  ?  54  THR A O   1 
ATOM   403  C  CB  . THR A 1 54  ? 34.263 67.293  22.634 1.00 47.72  ?  54  THR A CB  1 
ATOM   404  O  OG1 . THR A 1 54  ? 34.441 66.340  23.683 1.00 54.59  ?  54  THR A OG1 1 
ATOM   405  C  CG2 . THR A 1 54  ? 35.184 66.922  21.493 1.00 47.69  ?  54  THR A CG2 1 
ATOM   406  N  N   . ALA A 1 55  ? 33.546 68.685  25.364 1.00 48.62  ?  55  ALA A N   1 
ATOM   407  C  CA  . ALA A 1 55  ? 32.667 69.152  26.430 1.00 43.14  ?  55  ALA A CA  1 
ATOM   408  C  C   . ALA A 1 55  ? 33.344 70.196  27.316 1.00 55.28  ?  55  ALA A C   1 
ATOM   409  O  O   . ALA A 1 55  ? 33.162 70.187  28.541 1.00 67.48  ?  55  ALA A O   1 
ATOM   410  C  CB  . ALA A 1 55  ? 32.189 67.972  27.275 1.00 43.91  ?  55  ALA A CB  1 
ATOM   411  N  N   . GLY A 1 56  ? 34.140 71.087  26.721 1.00 46.32  ?  56  GLY A N   1 
ATOM   412  C  CA  . GLY A 1 56  ? 34.825 72.086  27.510 1.00 47.58  ?  56  GLY A CA  1 
ATOM   413  C  C   . GLY A 1 56  ? 35.972 71.464  28.278 1.00 56.78  ?  56  GLY A C   1 
ATOM   414  O  O   . GLY A 1 56  ? 36.569 70.465  27.862 1.00 61.56  ?  56  GLY A O   1 
ATOM   415  N  N   . CYS A 1 57  ? 36.286 72.061  29.426 1.00 53.65  ?  57  CYS A N   1 
ATOM   416  C  CA  . CYS A 1 57  ? 37.357 71.518  30.250 1.00 48.71  ?  57  CYS A CA  1 
ATOM   417  C  C   . CYS A 1 57  ? 36.946 70.251  30.975 1.00 51.01  ?  57  CYS A C   1 
ATOM   418  O  O   . CYS A 1 57  ? 37.812 69.563  31.521 1.00 54.16  ?  57  CYS A O   1 
ATOM   419  C  CB  . CYS A 1 57  ? 37.833 72.567  31.260 1.00 55.61  ?  57  CYS A CB  1 
ATOM   420  S  SG  . CYS A 1 57  ? 38.318 74.134  30.485 1.00 60.85  ?  57  CYS A SG  1 
ATOM   421  N  N   . THR A 1 58  ? 35.655 69.916  30.970 1.00 53.19  ?  58  THR A N   1 
ATOM   422  C  CA  . THR A 1 58  ? 35.183 68.780  31.753 1.00 53.87  ?  58  THR A CA  1 
ATOM   423  C  C   . THR A 1 58  ? 35.694 67.462  31.182 1.00 49.78  ?  58  THR A C   1 
ATOM   424  O  O   . THR A 1 58  ? 36.067 66.548  31.932 1.00 59.66  ?  58  THR A O   1 
ATOM   425  C  CB  . THR A 1 58  ? 33.658 68.788  31.794 1.00 55.65  ?  58  THR A CB  1 
ATOM   426  O  OG1 . THR A 1 58  ? 33.213 69.851  32.650 1.00 54.61  ?  58  THR A OG1 1 
ATOM   427  C  CG2 . THR A 1 58  ? 33.140 67.449  32.306 1.00 53.37  ?  58  THR A CG2 1 
ATOM   428  N  N   . SER A 1 59  ? 35.737 67.354  29.855 1.00 42.48  ?  59  SER A N   1 
ATOM   429  C  CA  . SER A 1 59  ? 36.165 66.143  29.165 1.00 54.53  ?  59  SER A CA  1 
ATOM   430  C  C   . SER A 1 59  ? 37.680 65.946  29.155 1.00 58.81  ?  59  SER A C   1 
ATOM   431  O  O   . SER A 1 59  ? 38.162 65.008  28.508 1.00 52.83  ?  59  SER A O   1 
ATOM   432  C  CB  . SER A 1 59  ? 35.625 66.160  27.736 1.00 60.58  ?  59  SER A CB  1 
ATOM   433  O  OG  . SER A 1 59  ? 35.771 67.444  27.156 1.00 59.78  ?  59  SER A OG  1 
ATOM   434  N  N   . ALA A 1 60  ? 38.442 66.791  29.848 1.00 58.39  ?  60  ALA A N   1 
ATOM   435  C  CA  . ALA A 1 60  ? 39.886 66.612  29.912 1.00 55.43  ?  60  ALA A CA  1 
ATOM   436  C  C   . ALA A 1 60  ? 40.305 65.528  30.902 1.00 57.16  ?  60  ALA A C   1 
ATOM   437  O  O   . ALA A 1 60  ? 41.471 65.112  30.892 1.00 49.81  ?  60  ALA A O   1 
ATOM   438  C  CB  . ALA A 1 60  ? 40.566 67.938  30.271 1.00 54.16  ?  60  ALA A CB  1 
ATOM   439  N  N   . GLY A 1 61  ? 39.388 65.054  31.742 1.00 62.85  ?  61  GLY A N   1 
ATOM   440  C  CA  . GLY A 1 61  ? 39.711 64.046  32.719 1.00 65.33  ?  61  GLY A CA  1 
ATOM   441  C  C   . GLY A 1 61  ? 40.524 64.605  33.867 1.00 65.09  ?  61  GLY A C   1 
ATOM   442  O  O   . GLY A 1 61  ? 40.630 65.824  34.055 1.00 61.95  ?  61  GLY A O   1 
ATOM   443  N  N   . PRO A 1 62  ? 41.126 63.710  34.663 1.00 62.24  ?  62  PRO A N   1 
ATOM   444  C  CA  . PRO A 1 62  ? 41.861 64.163  35.846 1.00 56.29  ?  62  PRO A CA  1 
ATOM   445  C  C   . PRO A 1 62  ? 43.305 64.491  35.528 1.00 58.77  ?  62  PRO A C   1 
ATOM   446  O  O   . PRO A 1 62  ? 43.756 64.346  34.382 1.00 55.25  ?  62  PRO A O   1 
ATOM   447  C  CB  . PRO A 1 62  ? 41.754 62.967  36.793 1.00 54.97  ?  62  PRO A CB  1 
ATOM   448  C  CG  . PRO A 1 62  ? 41.791 61.784  35.851 1.00 55.84  ?  62  PRO A CG  1 
ATOM   449  C  CD  . PRO A 1 62  ? 41.111 62.238  34.562 1.00 56.01  ?  62  PRO A CD  1 
ATOM   450  N  N   . HIS A 1 63  ? 44.018 64.943  36.563 1.00 56.93  ?  63  HIS A N   1 
ATOM   451  C  CA  . HIS A 1 63  ? 45.450 65.206  36.491 1.00 60.87  ?  63  HIS A CA  1 
ATOM   452  C  C   . HIS A 1 63  ? 46.210 64.088  35.782 1.00 64.49  ?  63  HIS A C   1 
ATOM   453  O  O   . HIS A 1 63  ? 46.000 62.903  36.056 1.00 72.34  ?  63  HIS A O   1 
ATOM   454  C  CB  . HIS A 1 63  ? 46.011 65.359  37.906 1.00 61.99  ?  63  HIS A CB  1 
ATOM   455  C  CG  . HIS A 1 63  ? 45.431 66.503  38.676 1.00 65.64  ?  63  HIS A CG  1 
ATOM   456  N  ND1 . HIS A 1 63  ? 44.604 67.441  38.100 1.00 73.13  ?  63  HIS A ND1 1 
ATOM   457  C  CD2 . HIS A 1 63  ? 45.585 66.880  39.969 1.00 68.55  ?  63  HIS A CD2 1 
ATOM   458  C  CE1 . HIS A 1 63  ? 44.257 68.334  39.009 1.00 72.25  ?  63  HIS A CE1 1 
ATOM   459  N  NE2 . HIS A 1 63  ? 44.841 68.020  40.152 1.00 61.27  ?  63  HIS A NE2 1 
ATOM   460  N  N   . PHE A 1 64  ? 47.138 64.473  34.902 1.00 49.90  ?  64  PHE A N   1 
ATOM   461  C  CA  . PHE A 1 64  ? 48.024 63.492  34.278 1.00 48.83  ?  64  PHE A CA  1 
ATOM   462  C  C   . PHE A 1 64  ? 48.854 62.792  35.342 1.00 66.73  ?  64  PHE A C   1 
ATOM   463  O  O   . PHE A 1 64  ? 49.687 63.416  36.013 1.00 66.17  ?  64  PHE A O   1 
ATOM   464  C  CB  . PHE A 1 64  ? 48.939 64.164  33.261 1.00 55.83  ?  64  PHE A CB  1 
ATOM   465  C  CG  . PHE A 1 64  ? 49.793 63.203  32.468 1.00 65.32  ?  64  PHE A CG  1 
ATOM   466  C  CD1 . PHE A 1 64  ? 49.274 62.005  31.990 1.00 74.19  ?  64  PHE A CD1 1 
ATOM   467  C  CD2 . PHE A 1 64  ? 51.107 63.522  32.162 1.00 67.85  ?  64  PHE A CD2 1 
ATOM   468  C  CE1 . PHE A 1 64  ? 50.063 61.132  31.241 1.00 78.33  ?  64  PHE A CE1 1 
ATOM   469  C  CE2 . PHE A 1 64  ? 51.897 62.658  31.409 1.00 75.66  ?  64  PHE A CE2 1 
ATOM   470  C  CZ  . PHE A 1 64  ? 51.375 61.461  30.950 1.00 77.65  ?  64  PHE A CZ  1 
ATOM   471  N  N   . ASN A 1 65  ? 48.634 61.494  35.484 1.00 71.61  ?  65  ASN A N   1 
ATOM   472  C  CA  . ASN A 1 65  ? 49.179 60.764  36.612 1.00 72.94  ?  65  ASN A CA  1 
ATOM   473  C  C   . ASN A 1 65  ? 49.556 59.366  36.125 1.00 71.16  ?  65  ASN A C   1 
ATOM   474  O  O   . ASN A 1 65  ? 48.812 58.412  36.374 1.00 73.15  ?  65  ASN A O   1 
ATOM   475  C  CB  . ASN A 1 65  ? 48.117 60.719  37.724 1.00 72.06  ?  65  ASN A CB  1 
ATOM   476  C  CG  . ASN A 1 65  ? 48.593 60.027  38.990 1.00 71.28  ?  65  ASN A CG  1 
ATOM   477  O  OD1 . ASN A 1 65  ? 49.664 59.432  39.018 1.00 84.13  ?  65  ASN A OD1 1 
ATOM   478  N  ND2 . ASN A 1 65  ? 47.764 60.065  40.038 1.00 60.27  ?  65  ASN A ND2 1 
ATOM   479  N  N   . PRO A 1 66  ? 50.661 59.183  35.403 1.00 62.56  ?  66  PRO A N   1 
ATOM   480  C  CA  . PRO A 1 66  ? 51.002 57.813  34.994 1.00 70.52  ?  66  PRO A CA  1 
ATOM   481  C  C   . PRO A 1 66  ? 51.585 56.964  36.121 1.00 69.38  ?  66  PRO A C   1 
ATOM   482  O  O   . PRO A 1 66  ? 51.461 55.735  36.074 1.00 71.22  ?  66  PRO A O   1 
ATOM   483  C  CB  . PRO A 1 66  ? 51.993 58.019  33.843 1.00 70.43  ?  66  PRO A CB  1 
ATOM   484  C  CG  . PRO A 1 66  ? 52.453 59.422  33.960 1.00 64.36  ?  66  PRO A CG  1 
ATOM   485  C  CD  . PRO A 1 66  ? 51.414 60.204  34.656 1.00 58.96  ?  66  PRO A CD  1 
ATOM   486  N  N   . LEU A 1 67  ? 52.173 57.578  37.150 1.00 69.97  ?  67  LEU A N   1 
ATOM   487  C  CA  . LEU A 1 67  ? 52.762 56.854  38.272 1.00 68.86  ?  67  LEU A CA  1 
ATOM   488  C  C   . LEU A 1 67  ? 51.756 56.443  39.340 1.00 69.03  ?  67  LEU A C   1 
ATOM   489  O  O   . LEU A 1 67  ? 52.169 55.853  40.338 1.00 81.27  ?  67  LEU A O   1 
ATOM   490  C  CB  . LEU A 1 67  ? 53.851 57.699  38.937 1.00 74.11  ?  67  LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 67  ? 55.289 57.549  38.451 1.00 78.45  ?  67  LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 67  ? 55.400 57.795  36.936 1.00 68.81  ?  67  LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 67  ? 56.205 58.478  39.276 1.00 75.36  ?  67  LEU A CD2 1 
ATOM   494  N  N   . SER A 1 68  ? 50.470 56.749  39.176 1.00 74.60  ?  68  SER A N   1 
ATOM   495  C  CA  . SER A 1 68  ? 49.435 56.441  40.176 1.00 80.87  ?  68  SER A CA  1 
ATOM   496  C  C   . SER A 1 68  ? 49.820 56.935  41.576 1.00 79.41  ?  68  SER A C   1 
ATOM   497  O  O   . SER A 1 68  ? 49.772 56.198  42.562 1.00 75.20  ?  68  SER A O   1 
ATOM   498  C  CB  . SER A 1 68  ? 49.113 54.943  40.186 1.00 82.11  ?  68  SER A CB  1 
ATOM   499  O  OG  . SER A 1 68  ? 48.869 54.466  38.871 1.00 83.92  ?  68  SER A OG  1 
ATOM   500  N  N   . ARG A 1 69  ? 50.191 58.205  41.663 1.00 83.71  ?  69  ARG A N   1 
ATOM   501  C  CA  . ARG A 1 69  ? 50.576 58.808  42.928 1.00 80.45  ?  69  ARG A CA  1 
ATOM   502  C  C   . ARG A 1 69  ? 49.500 59.768  43.418 1.00 79.14  ?  69  ARG A C   1 
ATOM   503  O  O   . ARG A 1 69  ? 48.565 60.115  42.692 1.00 77.22  ?  69  ARG A O   1 
ATOM   504  C  CB  . ARG A 1 69  ? 51.908 59.530  42.779 1.00 74.27  ?  69  ARG A CB  1 
ATOM   505  C  CG  . ARG A 1 69  ? 52.575 59.747  44.083 1.00 68.72  ?  69  ARG A CG  1 
ATOM   506  C  CD  . ARG A 1 69  ? 53.508 58.601  44.368 1.00 65.15  ?  69  ARG A CD  1 
ATOM   507  N  NE  . ARG A 1 69  ? 54.345 58.996  45.464 1.00 73.98  ?  69  ARG A NE  1 
ATOM   508  C  CZ  . ARG A 1 69  ? 55.660 58.864  45.458 1.00 82.00  ?  69  ARG A CZ  1 
ATOM   509  N  NH1 . ARG A 1 69  ? 56.251 58.361  44.382 1.00 90.10  1  69  ARG A NH1 1 
ATOM   510  N  NH2 . ARG A 1 69  ? 56.388 59.249  46.510 1.00 87.78  ?  69  ARG A NH2 1 
ATOM   511  N  N   . LYS A 1 70  ? 49.633 60.180  44.680 1.00 75.79  ?  70  LYS A N   1 
ATOM   512  C  CA  . LYS A 1 70  ? 48.744 61.172  45.259 1.00 81.25  ?  70  LYS A CA  1 
ATOM   513  C  C   . LYS A 1 70  ? 49.087 62.572  44.741 1.00 89.39  ?  70  LYS A C   1 
ATOM   514  O  O   . LYS A 1 70  ? 50.113 62.796  44.086 1.00 90.46  ?  70  LYS A O   1 
ATOM   515  C  CB  . LYS A 1 70  ? 48.816 61.137  46.787 1.00 76.59  ?  70  LYS A CB  1 
ATOM   516  C  CG  . LYS A 1 70  ? 48.197 59.905  47.442 1.00 80.71  ?  70  LYS A CG  1 
ATOM   517  C  CD  . LYS A 1 70  ? 47.688 60.231  48.853 1.00 87.37  ?  70  LYS A CD  1 
ATOM   518  C  CE  . LYS A 1 70  ? 48.197 59.245  49.904 1.00 93.38  ?  70  LYS A CE  1 
ATOM   519  N  NZ  . LYS A 1 70  ? 48.264 59.874  51.259 1.00 94.27  1  70  LYS A NZ  1 
ATOM   520  N  N   . HIS A 1 71  ? 48.204 63.525  45.044 1.00 83.22  ?  71  HIS A N   1 
ATOM   521  C  CA  . HIS A 1 71  ? 48.407 64.908  44.644 1.00 74.37  ?  71  HIS A CA  1 
ATOM   522  C  C   . HIS A 1 71  ? 49.487 65.550  45.504 1.00 74.50  ?  71  HIS A C   1 
ATOM   523  O  O   . HIS A 1 71  ? 49.574 65.289  46.706 1.00 79.00  ?  71  HIS A O   1 
ATOM   524  C  CB  . HIS A 1 71  ? 47.102 65.696  44.773 1.00 71.47  ?  71  HIS A CB  1 
ATOM   525  C  CG  . HIS A 1 71  ? 47.196 67.098  44.262 1.00 65.27  ?  71  HIS A CG  1 
ATOM   526  N  ND1 . HIS A 1 71  ? 47.612 67.395  42.983 1.00 68.60  ?  71  HIS A ND1 1 
ATOM   527  C  CD2 . HIS A 1 71  ? 46.968 68.286  44.867 1.00 65.31  ?  71  HIS A CD2 1 
ATOM   528  C  CE1 . HIS A 1 71  ? 47.619 68.704  42.815 1.00 59.15  ?  71  HIS A CE1 1 
ATOM   529  N  NE2 . HIS A 1 71  ? 47.226 69.269  43.942 1.00 60.13  ?  71  HIS A NE2 1 
ATOM   530  N  N   . GLY A 1 72  ? 50.318 66.386  44.880 1.00 73.24  ?  72  GLY A N   1 
ATOM   531  C  CA  . GLY A 1 72  ? 51.276 67.199  45.606 1.00 73.60  ?  72  GLY A CA  1 
ATOM   532  C  C   . GLY A 1 72  ? 51.628 68.457  44.831 1.00 73.41  ?  72  GLY A C   1 
ATOM   533  O  O   . GLY A 1 72  ? 51.085 68.717  43.758 1.00 75.92  ?  72  GLY A O   1 
ATOM   534  N  N   . GLY A 1 73  ? 52.546 69.246  45.380 1.00 71.68  ?  73  GLY A N   1 
ATOM   535  C  CA  . GLY A 1 73  ? 53.106 70.369  44.658 1.00 69.37  ?  73  GLY A CA  1 
ATOM   536  C  C   . GLY A 1 73  ? 54.225 69.954  43.727 1.00 63.37  ?  73  GLY A C   1 
ATOM   537  O  O   . GLY A 1 73  ? 54.667 68.797  43.691 1.00 64.22  ?  73  GLY A O   1 
ATOM   538  N  N   . PRO A 1 74  ? 54.718 70.919  42.945 1.00 51.48  ?  74  PRO A N   1 
ATOM   539  C  CA  . PRO A 1 74  ? 55.746 70.589  41.945 1.00 55.55  ?  74  PRO A CA  1 
ATOM   540  C  C   . PRO A 1 74  ? 57.075 70.202  42.552 1.00 68.35  ?  74  PRO A C   1 
ATOM   541  O  O   . PRO A 1 74  ? 57.775 69.353  41.986 1.00 68.28  ?  74  PRO A O   1 
ATOM   542  C  CB  . PRO A 1 74  ? 55.888 71.878  41.114 1.00 51.00  ?  74  PRO A CB  1 
ATOM   543  C  CG  . PRO A 1 74  ? 54.742 72.731  41.511 1.00 56.35  ?  74  PRO A CG  1 
ATOM   544  C  CD  . PRO A 1 74  ? 54.383 72.341  42.909 1.00 52.71  ?  74  PRO A CD  1 
ATOM   545  N  N   . LYS A 1 75  ? 57.452 70.824  43.673 1.00 74.87  ?  75  LYS A N   1 
ATOM   546  C  CA  . LYS A 1 75  ? 58.698 70.485  44.348 1.00 68.74  ?  75  LYS A CA  1 
ATOM   547  C  C   . LYS A 1 75  ? 58.605 69.149  45.083 1.00 67.71  ?  75  LYS A C   1 
ATOM   548  O  O   . LYS A 1 75  ? 59.626 68.486  45.268 1.00 74.49  ?  75  LYS A O   1 
ATOM   549  C  CB  . LYS A 1 75  ? 59.091 71.603  45.326 1.00 67.11  ?  75  LYS A CB  1 
ATOM   550  C  CG  . LYS A 1 75  ? 59.474 72.940  44.675 1.00 71.39  ?  75  LYS A CG  1 
ATOM   551  C  CD  . LYS A 1 75  ? 60.284 73.850  45.632 1.00 82.80  ?  75  LYS A CD  1 
ATOM   552  C  CE  . LYS A 1 75  ? 59.496 75.098  46.073 1.00 84.18  ?  75  LYS A CE  1 
ATOM   553  N  NZ  . LYS A 1 75  ? 60.033 76.395  45.539 1.00 79.50  1  75  LYS A NZ  1 
ATOM   554  N  N   . ASP A 1 76  ? 57.401 68.735  45.482 1.00 65.34  ?  76  ASP A N   1 
ATOM   555  C  CA  . ASP A 1 76  ? 57.203 67.512  46.249 1.00 60.63  ?  76  ASP A CA  1 
ATOM   556  C  C   . ASP A 1 76  ? 57.632 66.274  45.472 1.00 68.53  ?  76  ASP A C   1 
ATOM   557  O  O   . ASP A 1 76  ? 57.646 66.238  44.240 1.00 68.87  ?  76  ASP A O   1 
ATOM   558  C  CB  . ASP A 1 76  ? 55.737 67.327  46.652 1.00 66.03  ?  76  ASP A CB  1 
ATOM   559  C  CG  . ASP A 1 76  ? 55.247 68.388  47.615 1.00 85.99  ?  76  ASP A CG  1 
ATOM   560  O  OD1 . ASP A 1 76  ? 54.262 68.101  48.323 1.00 88.41  ?  76  ASP A OD1 1 
ATOM   561  O  OD2 . ASP A 1 76  ? 55.837 69.488  47.654 1.00 101.16 -1 76  ASP A OD2 1 
ATOM   562  N  N   . GLU A 1 77  ? 57.958 65.234  46.228 1.00 71.50  ?  77  GLU A N   1 
ATOM   563  C  CA  . GLU A 1 77  ? 58.286 63.952  45.641 1.00 69.52  ?  77  GLU A CA  1 
ATOM   564  C  C   . GLU A 1 77  ? 57.043 63.101  45.420 1.00 68.75  ?  77  GLU A C   1 
ATOM   565  O  O   . GLU A 1 77  ? 56.986 62.334  44.451 1.00 59.33  ?  77  GLU A O   1 
ATOM   566  C  CB  . GLU A 1 77  ? 59.299 63.253  46.543 1.00 78.43  ?  77  GLU A CB  1 
ATOM   567  C  CG  . GLU A 1 77  ? 59.816 61.937  46.031 1.00 84.11  ?  77  GLU A CG  1 
ATOM   568  C  CD  . GLU A 1 77  ? 58.961 60.779  46.478 1.00 91.65  ?  77  GLU A CD  1 
ATOM   569  O  OE1 . GLU A 1 77  ? 58.782 59.829  45.680 1.00 104.87 ?  77  GLU A OE1 1 
ATOM   570  O  OE2 . GLU A 1 77  ? 58.454 60.853  47.621 1.00 85.14  -1 77  GLU A OE2 1 
ATOM   571  N  N   . GLU A 1 78  ? 56.038 63.242  46.287 1.00 72.38  ?  78  GLU A N   1 
ATOM   572  C  CA  . GLU A 1 78  ? 54.731 62.618  46.099 1.00 75.29  ?  78  GLU A CA  1 
ATOM   573  C  C   . GLU A 1 78  ? 53.849 63.618  45.359 1.00 75.51  ?  78  GLU A C   1 
ATOM   574  O  O   . GLU A 1 78  ? 53.453 64.645  45.923 1.00 69.77  ?  78  GLU A O   1 
ATOM   575  C  CB  . GLU A 1 78  ? 54.116 62.211  47.438 1.00 86.64  ?  78  GLU A CB  1 
ATOM   576  C  CG  . GLU A 1 78  ? 52.815 61.410  47.316 1.00 96.88  ?  78  GLU A CG  1 
ATOM   577  C  CD  . GLU A 1 78  ? 52.295 60.907  48.656 1.00 97.33  ?  78  GLU A CD  1 
ATOM   578  O  OE1 . GLU A 1 78  ? 52.005 61.753  49.531 1.00 98.37  ?  78  GLU A OE1 1 
ATOM   579  O  OE2 . GLU A 1 78  ? 52.170 59.670  48.827 1.00 91.77  -1 78  GLU A OE2 1 
ATOM   580  N  N   . ARG A 1 79  ? 53.506 63.290  44.114 1.00 75.14  ?  79  ARG A N   1 
ATOM   581  C  CA  . ARG A 1 79  ? 53.124 64.277  43.118 1.00 70.38  ?  79  ARG A CA  1 
ATOM   582  C  C   . ARG A 1 79  ? 52.458 63.550  41.960 1.00 76.29  ?  79  ARG A C   1 
ATOM   583  O  O   . ARG A 1 79  ? 52.708 62.364  41.730 1.00 84.20  ?  79  ARG A O   1 
ATOM   584  C  CB  . ARG A 1 79  ? 54.372 65.036  42.654 1.00 63.07  ?  79  ARG A CB  1 
ATOM   585  C  CG  . ARG A 1 79  ? 54.170 66.187  41.721 1.00 61.83  ?  79  ARG A CG  1 
ATOM   586  C  CD  . ARG A 1 79  ? 55.526 66.783  41.374 1.00 73.18  ?  79  ARG A CD  1 
ATOM   587  N  NE  . ARG A 1 79  ? 55.464 67.826  40.350 1.00 84.73  ?  79  ARG A NE  1 
ATOM   588  C  CZ  . ARG A 1 79  ? 55.835 67.608  39.101 1.00 80.28  ?  79  ARG A CZ  1 
ATOM   589  N  NH1 . ARG A 1 79  ? 56.240 66.403  38.808 1.00 74.76  1  79  ARG A NH1 1 
ATOM   590  N  NH2 . ARG A 1 79  ? 55.778 68.549  38.168 1.00 82.04  ?  79  ARG A NH2 1 
ATOM   591  N  N   . HIS A 1 80  ? 51.593 64.262  41.244 1.00 72.55  ?  80  HIS A N   1 
ATOM   592  C  CA  . HIS A 1 80  ? 51.217 63.847  39.898 1.00 66.13  ?  80  HIS A CA  1 
ATOM   593  C  C   . HIS A 1 80  ? 52.195 64.459  38.902 1.00 59.98  ?  80  HIS A C   1 
ATOM   594  O  O   . HIS A 1 80  ? 52.683 65.574  39.101 1.00 63.51  ?  80  HIS A O   1 
ATOM   595  C  CB  . HIS A 1 80  ? 49.792 64.277  39.530 1.00 66.93  ?  80  HIS A CB  1 
ATOM   596  C  CG  . HIS A 1 80  ? 48.740 63.841  40.505 1.00 72.94  ?  80  HIS A CG  1 
ATOM   597  N  ND1 . HIS A 1 80  ? 47.674 64.641  40.861 1.00 67.97  ?  80  HIS A ND1 1 
ATOM   598  C  CD2 . HIS A 1 80  ? 48.593 62.690  41.204 1.00 73.52  ?  80  HIS A CD2 1 
ATOM   599  C  CE1 . HIS A 1 80  ? 46.911 63.996  41.728 1.00 60.75  ?  80  HIS A CE1 1 
ATOM   600  N  NE2 . HIS A 1 80  ? 47.446 62.809  41.953 1.00 60.97  ?  80  HIS A NE2 1 
ATOM   601  N  N   . VAL A 1 81  ? 52.472 63.728  37.818 1.00 59.32  ?  81  VAL A N   1 
ATOM   602  C  CA  . VAL A 1 81  ? 53.351 64.274  36.781 1.00 63.82  ?  81  VAL A CA  1 
ATOM   603  C  C   . VAL A 1 81  ? 52.858 65.637  36.331 1.00 66.81  ?  81  VAL A C   1 
ATOM   604  O  O   . VAL A 1 81  ? 53.656 66.521  35.991 1.00 65.57  ?  81  VAL A O   1 
ATOM   605  C  CB  . VAL A 1 81  ? 53.464 63.306  35.584 1.00 64.97  ?  81  VAL A CB  1 
ATOM   606  C  CG1 . VAL A 1 81  ? 54.202 63.990  34.427 1.00 47.77  ?  81  VAL A CG1 1 
ATOM   607  C  CG2 . VAL A 1 81  ? 54.176 62.011  36.007 1.00 50.53  ?  81  VAL A CG2 1 
ATOM   608  N  N   . GLY A 1 82  ? 51.545 65.847  36.357 1.00 68.75  ?  82  GLY A N   1 
ATOM   609  C  CA  . GLY A 1 82  ? 50.944 67.077  35.903 1.00 63.39  ?  82  GLY A CA  1 
ATOM   610  C  C   . GLY A 1 82  ? 50.788 68.152  36.944 1.00 62.52  ?  82  GLY A C   1 
ATOM   611  O  O   . GLY A 1 82  ? 50.228 69.209  36.642 1.00 64.08  ?  82  GLY A O   1 
ATOM   612  N  N   . ASP A 1 83  ? 51.265 67.932  38.163 1.00 59.46  ?  83  ASP A N   1 
ATOM   613  C  CA  . ASP A 1 83  ? 51.134 68.953  39.199 1.00 61.39  ?  83  ASP A CA  1 
ATOM   614  C  C   . ASP A 1 83  ? 52.149 70.071  38.964 1.00 60.82  ?  83  ASP A C   1 
ATOM   615  O  O   . ASP A 1 83  ? 53.353 69.871  39.143 1.00 72.63  ?  83  ASP A O   1 
ATOM   616  C  CB  . ASP A 1 83  ? 51.303 68.320  40.578 1.00 59.32  ?  83  ASP A CB  1 
ATOM   617  C  CG  . ASP A 1 83  ? 50.119 67.437  40.973 1.00 63.53  ?  83  ASP A CG  1 
ATOM   618  O  OD1 . ASP A 1 83  ? 49.140 67.398  40.215 1.00 52.98  ?  83  ASP A OD1 1 
ATOM   619  O  OD2 . ASP A 1 83  ? 50.174 66.771  42.033 1.00 70.96  -1 83  ASP A OD2 1 
ATOM   620  N  N   . LEU A 1 84  ? 51.670 71.250  38.555 1.00 52.86  ?  84  LEU A N   1 
ATOM   621  C  CA  . LEU A 1 84  ? 52.522 72.422  38.357 1.00 49.93  ?  84  LEU A CA  1 
ATOM   622  C  C   . LEU A 1 84  ? 52.220 73.521  39.367 1.00 51.62  ?  84  LEU A C   1 
ATOM   623  O  O   . LEU A 1 84  ? 52.650 74.668  39.183 1.00 52.05  ?  84  LEU A O   1 
ATOM   624  C  CB  . LEU A 1 84  ? 52.382 72.950  36.928 1.00 41.47  ?  84  LEU A CB  1 
ATOM   625  C  CG  . LEU A 1 84  ? 52.739 71.906  35.866 1.00 49.98  ?  84  LEU A CG  1 
ATOM   626  C  CD1 . LEU A 1 84  ? 52.748 72.497  34.487 1.00 46.49  ?  84  LEU A CD1 1 
ATOM   627  C  CD2 . LEU A 1 84  ? 54.084 71.261  36.150 1.00 50.92  ?  84  LEU A CD2 1 
ATOM   628  N  N   . GLY A 1 85  ? 51.478 73.197  40.419 1.00 58.46  ?  85  GLY A N   1 
ATOM   629  C  CA  . GLY A 1 85  ? 51.320 74.122  41.528 1.00 64.33  ?  85  GLY A CA  1 
ATOM   630  C  C   . GLY A 1 85  ? 50.392 75.261  41.189 1.00 62.45  ?  85  GLY A C   1 
ATOM   631  O  O   . GLY A 1 85  ? 49.291 75.057  40.668 1.00 68.10  ?  85  GLY A O   1 
ATOM   632  N  N   . ASN A 1 86  ? 50.836 76.476  41.491 1.00 53.66  ?  86  ASN A N   1 
ATOM   633  C  CA  . ASN A 1 86  ? 49.997 77.649  41.371 1.00 51.33  ?  86  ASN A CA  1 
ATOM   634  C  C   . ASN A 1 86  ? 50.662 78.686  40.485 1.00 50.31  ?  86  ASN A C   1 
ATOM   635  O  O   . ASN A 1 86  ? 51.889 78.731  40.350 1.00 50.17  ?  86  ASN A O   1 
ATOM   636  C  CB  . ASN A 1 86  ? 49.700 78.275  42.738 1.00 54.97  ?  86  ASN A CB  1 
ATOM   637  C  CG  . ASN A 1 86  ? 48.732 77.450  43.560 1.00 60.15  ?  86  ASN A CG  1 
ATOM   638  O  OD1 . ASN A 1 86  ? 47.528 77.412  43.291 1.00 57.06  ?  86  ASN A OD1 1 
ATOM   639  N  ND2 . ASN A 1 86  ? 49.256 76.785  44.578 1.00 68.85  ?  86  ASN A ND2 1 
ATOM   640  N  N   . VAL A 1 87  ? 49.818 79.498  39.869 1.00 53.61  ?  87  VAL A N   1 
ATOM   641  C  CA  . VAL A 1 87  ? 50.204 80.755  39.250 1.00 48.61  ?  87  VAL A CA  1 
ATOM   642  C  C   . VAL A 1 87  ? 49.535 81.862  40.052 1.00 45.45  ?  87  VAL A C   1 
ATOM   643  O  O   . VAL A 1 87  ? 48.468 81.656  40.646 1.00 41.84  ?  87  VAL A O   1 
ATOM   644  C  CB  . VAL A 1 87  ? 49.798 80.789  37.762 1.00 43.77  ?  87  VAL A CB  1 
ATOM   645  C  CG1 . VAL A 1 87  ? 50.443 79.618  37.032 1.00 39.08  ?  87  VAL A CG1 1 
ATOM   646  C  CG2 . VAL A 1 87  ? 48.285 80.701  37.616 1.00 46.14  ?  87  VAL A CG2 1 
ATOM   647  N  N   . THR A 1 88  ? 50.187 83.028  40.111 1.00 41.77  ?  88  THR A N   1 
ATOM   648  C  CA  . THR A 1 88  ? 49.735 84.146  40.934 1.00 44.56  ?  88  THR A CA  1 
ATOM   649  C  C   . THR A 1 88  ? 49.321 85.310  40.046 1.00 44.86  ?  88  THR A C   1 
ATOM   650  O  O   . THR A 1 88  ? 50.138 85.824  39.273 1.00 47.62  ?  88  THR A O   1 
ATOM   651  C  CB  . THR A 1 88  ? 50.832 84.600  41.898 1.00 51.35  ?  88  THR A CB  1 
ATOM   652  O  OG1 . THR A 1 88  ? 51.219 83.503  42.739 1.00 55.25  ?  88  THR A OG1 1 
ATOM   653  C  CG2 . THR A 1 88  ? 50.320 85.762  42.758 1.00 51.38  ?  88  THR A CG2 1 
ATOM   654  N  N   . ALA A 1 89  ? 48.066 85.747  40.181 1.00 49.74  ?  89  ALA A N   1 
ATOM   655  C  CA  . ALA A 1 89  ? 47.515 86.824  39.364 1.00 40.94  ?  89  ALA A CA  1 
ATOM   656  C  C   . ALA A 1 89  ? 47.684 88.158  40.080 1.00 45.78  ?  89  ALA A C   1 
ATOM   657  O  O   . ALA A 1 89  ? 47.393 88.264  41.280 1.00 58.05  ?  89  ALA A O   1 
ATOM   658  C  CB  . ALA A 1 89  ? 46.035 86.571  39.068 1.00 34.13  ?  89  ALA A CB  1 
ATOM   659  N  N   . ASP A 1 90  ? 48.126 89.183  39.342 1.00 39.83  ?  90  ASP A N   1 
ATOM   660  C  CA  . ASP A 1 90  ? 48.383 90.483  39.952 1.00 42.04  ?  90  ASP A CA  1 
ATOM   661  C  C   . ASP A 1 90  ? 47.072 91.236  40.168 1.00 38.78  ?  90  ASP A C   1 
ATOM   662  O  O   . ASP A 1 90  ? 45.974 90.696  39.999 1.00 38.18  ?  90  ASP A O   1 
ATOM   663  C  CB  . ASP A 1 90  ? 49.396 91.277  39.130 1.00 42.95  ?  90  ASP A CB  1 
ATOM   664  C  CG  . ASP A 1 90  ? 48.871 91.725  37.781 1.00 42.70  ?  90  ASP A CG  1 
ATOM   665  O  OD1 . ASP A 1 90  ? 47.647 91.659  37.507 1.00 44.36  ?  90  ASP A OD1 1 
ATOM   666  O  OD2 . ASP A 1 90  ? 49.725 92.167  36.978 1.00 42.40  -1 90  ASP A OD2 1 
ATOM   667  N  N   . LYS A 1 91  ? 47.176 92.511  40.548 1.00 44.78  ?  91  LYS A N   1 
ATOM   668  C  CA  . LYS A 1 91  ? 45.991 93.273  40.929 1.00 36.54  ?  91  LYS A CA  1 
ATOM   669  C  C   . LYS A 1 91  ? 45.117 93.635  39.747 1.00 32.04  ?  91  LYS A C   1 
ATOM   670  O  O   . LYS A 1 91  ? 44.020 94.167  39.962 1.00 33.27  ?  91  LYS A O   1 
ATOM   671  C  CB  . LYS A 1 91  ? 46.396 94.548  41.671 1.00 36.85  ?  91  LYS A CB  1 
ATOM   672  C  CG  . LYS A 1 91  ? 47.430 95.383  40.956 1.00 39.63  ?  91  LYS A CG  1 
ATOM   673  C  CD  . LYS A 1 91  ? 47.499 96.784  41.543 1.00 50.72  ?  91  LYS A CD  1 
ATOM   674  C  CE  . LYS A 1 91  ? 48.592 97.584  40.842 1.00 64.00  ?  91  LYS A CE  1 
ATOM   675  N  NZ  . LYS A 1 91  ? 48.418 97.600  39.348 1.00 59.70  1  91  LYS A NZ  1 
ATOM   676  N  N   . ASP A 1 92  ? 45.597 93.398  38.521 1.00 39.78  ?  92  ASP A N   1 
ATOM   677  C  CA  . ASP A 1 92  ? 44.845 93.567  37.282 1.00 32.58  ?  92  ASP A CA  1 
ATOM   678  C  C   . ASP A 1 92  ? 44.306 92.243  36.746 1.00 38.22  ?  92  ASP A C   1 
ATOM   679  O  O   . ASP A 1 92  ? 43.735 92.214  35.649 1.00 37.61  ?  92  ASP A O   1 
ATOM   680  C  CB  . ASP A 1 92  ? 45.730 94.197  36.204 1.00 38.09  ?  92  ASP A CB  1 
ATOM   681  C  CG  . ASP A 1 92  ? 46.181 95.616  36.527 1.00 39.83  ?  92  ASP A CG  1 
ATOM   682  O  OD1 . ASP A 1 92  ? 45.575 96.319  37.373 1.00 40.75  ?  92  ASP A OD1 1 
ATOM   683  O  OD2 . ASP A 1 92  ? 47.164 96.033  35.885 1.00 42.92  -1 92  ASP A OD2 1 
ATOM   684  N  N   . GLY A 1 93  ? 44.515 91.142  37.462 1.00 33.86  ?  93  GLY A N   1 
ATOM   685  C  CA  . GLY A 1 93  ? 44.029 89.862  37.001 1.00 26.82  ?  93  GLY A CA  1 
ATOM   686  C  C   . GLY A 1 93  ? 44.923 89.175  36.003 1.00 30.59  ?  93  GLY A C   1 
ATOM   687  O  O   . GLY A 1 93  ? 44.494 88.199  35.378 1.00 36.91  ?  93  GLY A O   1 
ATOM   688  N  N   . VAL A 1 94  ? 46.145 89.658  35.828 1.00 32.02  ?  94  VAL A N   1 
ATOM   689  C  CA  . VAL A 1 94  ? 47.113 89.068  34.910 1.00 37.56  ?  94  VAL A CA  1 
ATOM   690  C  C   . VAL A 1 94  ? 48.133 88.260  35.703 1.00 47.15  ?  94  VAL A C   1 
ATOM   691  O  O   . VAL A 1 94  ? 48.707 88.752  36.686 1.00 52.82  ?  94  VAL A O   1 
ATOM   692  C  CB  . VAL A 1 94  ? 47.822 90.153  34.082 1.00 33.11  ?  94  VAL A CB  1 
ATOM   693  C  CG1 . VAL A 1 94  ? 48.816 89.499  33.127 1.00 35.82  ?  94  VAL A CG1 1 
ATOM   694  C  CG2 . VAL A 1 94  ? 46.810 91.020  33.359 1.00 26.90  ?  94  VAL A CG2 1 
ATOM   695  N  N   . ALA A 1 95  ? 48.379 87.029  35.275 1.00 45.60  ?  95  ALA A N   1 
ATOM   696  C  CA  . ALA A 1 95  ? 49.413 86.199  35.878 1.00 48.73  ?  95  ALA A CA  1 
ATOM   697  C  C   . ALA A 1 95  ? 50.449 85.901  34.809 1.00 43.25  ?  95  ALA A C   1 
ATOM   698  O  O   . ALA A 1 95  ? 50.171 85.170  33.853 1.00 41.95  ?  95  ALA A O   1 
ATOM   699  C  CB  . ALA A 1 95  ? 48.833 84.909  36.450 1.00 49.24  ?  95  ALA A CB  1 
ATOM   700  N  N   . ASP A 1 96  ? 51.635 86.466  34.964 1.00 47.17  ?  96  ASP A N   1 
ATOM   701  C  CA  . ASP A 1 96  ? 52.747 86.150  34.085 1.00 46.95  ?  96  ASP A CA  1 
ATOM   702  C  C   . ASP A 1 96  ? 53.456 84.930  34.647 1.00 55.39  ?  96  ASP A C   1 
ATOM   703  O  O   . ASP A 1 96  ? 53.911 84.941  35.797 1.00 60.38  ?  96  ASP A O   1 
ATOM   704  C  CB  . ASP A 1 96  ? 53.682 87.346  33.954 1.00 45.84  ?  96  ASP A CB  1 
ATOM   705  C  CG  . ASP A 1 96  ? 52.987 88.537  33.347 1.00 58.01  ?  96  ASP A CG  1 
ATOM   706  O  OD1 . ASP A 1 96  ? 52.409 88.382  32.245 1.00 60.30  ?  96  ASP A OD1 1 
ATOM   707  O  OD2 . ASP A 1 96  ? 52.974 89.610  33.994 1.00 62.75  -1 96  ASP A OD2 1 
ATOM   708  N  N   . VAL A 1 97  ? 53.510 83.869  33.849 1.00 55.71  ?  97  VAL A N   1 
ATOM   709  C  CA  . VAL A 1 97  ? 54.066 82.600  34.275 1.00 55.31  ?  97  VAL A CA  1 
ATOM   710  C  C   . VAL A 1 97  ? 55.447 82.456  33.662 1.00 52.76  ?  97  VAL A C   1 
ATOM   711  O  O   . VAL A 1 97  ? 55.642 82.719  32.469 1.00 53.38  ?  97  VAL A O   1 
ATOM   712  C  CB  . VAL A 1 97  ? 53.154 81.431  33.874 1.00 53.54  ?  97  VAL A CB  1 
ATOM   713  C  CG1 . VAL A 1 97  ? 53.661 80.136  34.496 1.00 54.29  ?  97  VAL A CG1 1 
ATOM   714  C  CG2 . VAL A 1 97  ? 51.745 81.706  34.313 1.00 40.78  ?  97  VAL A CG2 1 
ATOM   715  N  N   . SER A 1 98  ? 56.409 82.084  34.493 1.00 51.34  ?  98  SER A N   1 
ATOM   716  C  CA  . SER A 1 98  ? 57.725 81.674  34.026 1.00 48.24  ?  98  SER A CA  1 
ATOM   717  C  C   . SER A 1 98  ? 58.227 80.659  35.037 1.00 58.00  ?  98  SER A C   1 
ATOM   718  O  O   . SER A 1 98  ? 58.628 81.040  36.140 1.00 65.29  ?  98  SER A O   1 
ATOM   719  C  CB  . SER A 1 98  ? 58.676 82.852  33.904 1.00 39.95  ?  98  SER A CB  1 
ATOM   720  O  OG  . SER A 1 98  ? 59.926 82.411  33.400 1.00 48.82  ?  98  SER A OG  1 
ATOM   721  N  N   . ILE A 1 99  ? 58.203 79.380  34.655 1.00 60.33  ?  99  ILE A N   1 
ATOM   722  C  CA  . ILE A 1 99  ? 58.365 78.258  35.569 1.00 55.94  ?  99  ILE A CA  1 
ATOM   723  C  C   . ILE A 1 99  ? 59.250 77.219  34.891 1.00 60.51  ?  99  ILE A C   1 
ATOM   724  O  O   . ILE A 1 99  ? 59.255 77.096  33.662 1.00 63.66  ?  99  ILE A O   1 
ATOM   725  C  CB  . ILE A 1 99  ? 56.971 77.672  35.960 1.00 63.91  ?  99  ILE A CB  1 
ATOM   726  C  CG1 . ILE A 1 99  ? 56.188 78.633  36.876 1.00 81.54  ?  99  ILE A CG1 1 
ATOM   727  C  CG2 . ILE A 1 99  ? 57.063 76.309  36.590 1.00 61.43  ?  99  ILE A CG2 1 
ATOM   728  C  CD1 . ILE A 1 99  ? 56.889 79.026  38.190 1.00 88.26  ?  99  ILE A CD1 1 
ATOM   729  N  N   . GLU A 1 100 ? 60.022 76.483  35.701 1.00 55.10  ?  100 GLU A N   1 
ATOM   730  C  CA  . GLU A 1 100 ? 60.783 75.323  35.245 1.00 59.85  ?  100 GLU A CA  1 
ATOM   731  C  C   . GLU A 1 100 ? 60.294 74.053  35.946 1.00 63.30  ?  100 GLU A C   1 
ATOM   732  O  O   . GLU A 1 100 ? 60.114 74.037  37.168 1.00 62.95  ?  100 GLU A O   1 
ATOM   733  C  CB  . GLU A 1 100 ? 62.280 75.527  35.495 1.00 62.92  ?  100 GLU A CB  1 
ATOM   734  C  CG  . GLU A 1 100 ? 63.168 74.367  35.037 1.00 79.70  ?  100 GLU A CG  1 
ATOM   735  C  CD  . GLU A 1 100 ? 64.652 74.718  35.064 1.00 82.01  ?  100 GLU A CD  1 
ATOM   736  O  OE1 . GLU A 1 100 ? 64.983 75.840  35.505 1.00 92.95  ?  100 GLU A OE1 1 
ATOM   737  O  OE2 . GLU A 1 100 ? 65.486 73.875  34.658 1.00 73.53  -1 100 GLU A OE2 1 
ATOM   738  N  N   . ASP A 1 101 ? 60.076 72.988  35.176 1.00 62.98  ?  101 ASP A N   1 
ATOM   739  C  CA  . ASP A 1 101 ? 59.734 71.688  35.733 1.00 63.54  ?  101 ASP A CA  1 
ATOM   740  C  C   . ASP A 1 101 ? 60.486 70.619  34.955 1.00 71.56  ?  101 ASP A C   1 
ATOM   741  O  O   . ASP A 1 101 ? 60.681 70.739  33.743 1.00 80.98  ?  101 ASP A O   1 
ATOM   742  C  CB  . ASP A 1 101 ? 58.220 71.430  35.683 1.00 56.70  ?  101 ASP A CB  1 
ATOM   743  C  CG  . ASP A 1 101 ? 57.768 70.376  36.683 1.00 64.71  ?  101 ASP A CG  1 
ATOM   744  O  OD1 . ASP A 1 101 ? 57.539 70.748  37.857 1.00 67.38  ?  101 ASP A OD1 1 
ATOM   745  O  OD2 . ASP A 1 101 ? 57.608 69.195  36.291 1.00 67.11  -1 101 ASP A OD2 1 
ATOM   746  N  N   . SER A 1 102 ? 60.908 69.569  35.656 1.00 70.04  ?  102 SER A N   1 
ATOM   747  C  CA  . SER A 1 102 ? 61.680 68.507  35.024 1.00 76.10  ?  102 SER A CA  1 
ATOM   748  C  C   . SER A 1 102 ? 60.971 67.162  34.998 1.00 74.01  ?  102 SER A C   1 
ATOM   749  O  O   . SER A 1 102 ? 61.490 66.214  34.392 1.00 71.50  ?  102 SER A O   1 
ATOM   750  C  CB  . SER A 1 102 ? 63.037 68.370  35.713 1.00 75.34  ?  102 SER A CB  1 
ATOM   751  O  OG  . SER A 1 102 ? 63.813 69.517  35.417 1.00 78.40  ?  102 SER A OG  1 
ATOM   752  N  N   . VAL A 1 103 ? 59.791 67.059  35.607 1.00 69.88  ?  103 VAL A N   1 
ATOM   753  C  CA  . VAL A 1 103 ? 59.031 65.818  35.561 1.00 71.26  ?  103 VAL A CA  1 
ATOM   754  C  C   . VAL A 1 103 ? 58.100 65.760  34.355 1.00 71.45  ?  103 VAL A C   1 
ATOM   755  O  O   . VAL A 1 103 ? 57.876 64.681  33.797 1.00 81.43  ?  103 VAL A O   1 
ATOM   756  C  CB  . VAL A 1 103 ? 58.246 65.624  36.862 1.00 65.23  ?  103 VAL A CB  1 
ATOM   757  C  CG1 . VAL A 1 103 ? 57.356 64.384  36.761 1.00 71.13  ?  103 VAL A CG1 1 
ATOM   758  C  CG2 . VAL A 1 103 ? 59.194 65.516  38.055 1.00 65.96  ?  103 VAL A CG2 1 
ATOM   759  N  N   . ILE A 1 104 ? 57.543 66.892  33.933 1.00 66.38  ?  104 ILE A N   1 
ATOM   760  C  CA  . ILE A 1 104 ? 56.863 66.888  32.649 1.00 67.66  ?  104 ILE A CA  1 
ATOM   761  C  C   . ILE A 1 104 ? 57.899 66.814  31.524 1.00 65.47  ?  104 ILE A C   1 
ATOM   762  O  O   . ILE A 1 104 ? 59.096 67.045  31.726 1.00 78.01  ?  104 ILE A O   1 
ATOM   763  C  CB  . ILE A 1 104 ? 55.950 68.118  32.516 1.00 63.81  ?  104 ILE A CB  1 
ATOM   764  C  CG1 . ILE A 1 104 ? 56.718 69.394  32.848 1.00 48.10  ?  104 ILE A CG1 1 
ATOM   765  C  CG2 . ILE A 1 104 ? 54.742 67.979  33.439 1.00 61.04  ?  104 ILE A CG2 1 
ATOM   766  C  CD1 . ILE A 1 104 ? 55.974 70.650  32.466 1.00 42.52  ?  104 ILE A CD1 1 
ATOM   767  N  N   . SER A 1 105 ? 57.437 66.437  30.330 1.00 58.65  ?  105 SER A N   1 
ATOM   768  C  CA  . SER A 1 105 ? 58.327 66.311  29.181 1.00 59.11  ?  105 SER A CA  1 
ATOM   769  C  C   . SER A 1 105 ? 57.539 66.471  27.885 1.00 60.26  ?  105 SER A C   1 
ATOM   770  O  O   . SER A 1 105 ? 56.307 66.361  27.860 1.00 58.11  ?  105 SER A O   1 
ATOM   771  C  CB  . SER A 1 105 ? 59.061 64.963  29.180 1.00 70.45  ?  105 SER A CB  1 
ATOM   772  O  OG  . SER A 1 105 ? 59.807 64.794  27.983 1.00 77.82  ?  105 SER A OG  1 
ATOM   773  N  N   . LEU A 1 106 ? 58.277 66.750  26.807 1.00 58.04  ?  106 LEU A N   1 
ATOM   774  C  CA  . LEU A 1 106 ? 57.735 66.875  25.459 1.00 51.80  ?  106 LEU A CA  1 
ATOM   775  C  C   . LEU A 1 106 ? 58.003 65.634  24.610 1.00 65.50  ?  106 LEU A C   1 
ATOM   776  O  O   . LEU A 1 106 ? 57.828 65.678  23.384 1.00 67.72  ?  106 LEU A O   1 
ATOM   777  C  CB  . LEU A 1 106 ? 58.320 68.114  24.779 1.00 47.47  ?  106 LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 106 ? 57.959 69.479  25.359 1.00 57.30  ?  106 LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 106 ? 58.298 70.568  24.382 1.00 64.15  ?  106 LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 106 ? 56.485 69.542  25.703 1.00 61.36  ?  106 LEU A CD2 1 
ATOM   781  N  N   . SER A 1 107 ? 58.436 64.539  25.236 1.00 69.52  ?  107 SER A N   1 
ATOM   782  C  CA  . SER A 1 107 ? 58.619 63.253  24.573 1.00 70.79  ?  107 SER A CA  1 
ATOM   783  C  C   . SER A 1 107 ? 58.633 62.173  25.646 1.00 67.48  ?  107 SER A C   1 
ATOM   784  O  O   . SER A 1 107 ? 58.724 62.457  26.844 1.00 63.17  ?  107 SER A O   1 
ATOM   785  C  CB  . SER A 1 107 ? 59.906 63.219  23.743 1.00 66.28  ?  107 SER A CB  1 
ATOM   786  O  OG  . SER A 1 107 ? 61.047 63.459  24.554 1.00 69.88  ?  107 SER A OG  1 
ATOM   787  N  N   . GLY A 1 108 ? 58.534 60.933  25.210 1.00 64.58  ?  108 GLY A N   1 
ATOM   788  C  CA  . GLY A 1 108 ? 58.642 59.853  26.163 1.00 68.46  ?  108 GLY A CA  1 
ATOM   789  C  C   . GLY A 1 108 ? 57.343 59.612  26.904 1.00 70.03  ?  108 GLY A C   1 
ATOM   790  O  O   . GLY A 1 108 ? 56.274 60.118  26.546 1.00 72.37  ?  108 GLY A O   1 
ATOM   791  N  N   . ASP A 1 109 ? 57.457 58.820  27.976 1.00 73.97  ?  109 ASP A N   1 
ATOM   792  C  CA  . ASP A 1 109 ? 56.276 58.279  28.650 1.00 78.05  ?  109 ASP A CA  1 
ATOM   793  C  C   . ASP A 1 109 ? 55.440 59.361  29.315 1.00 74.44  ?  109 ASP A C   1 
ATOM   794  O  O   . ASP A 1 109 ? 54.213 59.221  29.412 1.00 69.65  ?  109 ASP A O   1 
ATOM   795  C  CB  . ASP A 1 109 ? 56.697 57.244  29.694 1.00 79.45  ?  109 ASP A CB  1 
ATOM   796  C  CG  . ASP A 1 109 ? 56.965 55.893  29.096 1.00 81.33  ?  109 ASP A CG  1 
ATOM   797  O  OD1 . ASP A 1 109 ? 56.650 55.701  27.903 1.00 79.63  ?  109 ASP A OD1 1 
ATOM   798  O  OD2 . ASP A 1 109 ? 57.495 55.025  29.821 1.00 87.19  -1 109 ASP A OD2 1 
ATOM   799  N  N   . HIS A 1 110 ? 56.090 60.419  29.803 1.00 79.59  ?  110 HIS A N   1 
ATOM   800  C  CA  . HIS A 1 110 ? 55.434 61.535  30.465 1.00 81.94  ?  110 HIS A CA  1 
ATOM   801  C  C   . HIS A 1 110 ? 55.301 62.747  29.542 1.00 71.49  ?  110 HIS A C   1 
ATOM   802  O  O   . HIS A 1 110 ? 55.211 63.883  30.024 1.00 72.23  ?  110 HIS A O   1 
ATOM   803  C  CB  . HIS A 1 110 ? 56.176 61.896  31.763 1.00 81.72  ?  110 HIS A CB  1 
ATOM   804  C  CG  . HIS A 1 110 ? 56.400 60.732  32.694 1.00 82.44  ?  110 HIS A CG  1 
ATOM   805  N  ND1 . HIS A 1 110 ? 57.185 60.818  33.830 1.00 72.33  ?  110 HIS A ND1 1 
ATOM   806  C  CD2 . HIS A 1 110 ? 55.927 59.460  32.667 1.00 93.68  ?  110 HIS A CD2 1 
ATOM   807  C  CE1 . HIS A 1 110 ? 57.181 59.656  34.463 1.00 73.07  ?  110 HIS A CE1 1 
ATOM   808  N  NE2 . HIS A 1 110 ? 56.430 58.813  33.776 1.00 87.21  ?  110 HIS A NE2 1 
ATOM   809  N  N   . CYS A 1 111 ? 55.326 62.517  28.226 1.00 64.52  ?  111 CYS A N   1 
ATOM   810  C  CA  . CYS A 1 111 ? 55.003 63.544  27.245 1.00 59.61  ?  111 CYS A CA  1 
ATOM   811  C  C   . CYS A 1 111 ? 53.643 64.160  27.553 1.00 68.99  ?  111 CYS A C   1 
ATOM   812  O  O   . CYS A 1 111 ? 52.674 63.445  27.823 1.00 70.63  ?  111 CYS A O   1 
ATOM   813  C  CB  . CYS A 1 111 ? 54.995 62.916  25.852 1.00 58.06  ?  111 CYS A CB  1 
ATOM   814  S  SG  . CYS A 1 111 ? 54.877 64.077  24.495 1.00 62.06  ?  111 CYS A SG  1 
ATOM   815  N  N   . ILE A 1 112 ? 53.569 65.493  27.514 1.00 69.00  ?  112 ILE A N   1 
ATOM   816  C  CA  . ILE A 1 112 ? 52.316 66.201  27.756 1.00 59.85  ?  112 ILE A CA  1 
ATOM   817  C  C   . ILE A 1 112 ? 51.696 66.744  26.478 1.00 58.02  ?  112 ILE A C   1 
ATOM   818  O  O   . ILE A 1 112 ? 50.667 67.429  26.542 1.00 54.69  ?  112 ILE A O   1 
ATOM   819  C  CB  . ILE A 1 112 ? 52.506 67.353  28.762 1.00 55.44  ?  112 ILE A CB  1 
ATOM   820  C  CG1 . ILE A 1 112 ? 53.470 68.401  28.188 1.00 50.11  ?  112 ILE A CG1 1 
ATOM   821  C  CG2 . ILE A 1 112 ? 53.005 66.810  30.089 1.00 53.38  ?  112 ILE A CG2 1 
ATOM   822  C  CD1 . ILE A 1 112 ? 53.437 69.735  28.911 1.00 40.50  ?  112 ILE A CD1 1 
ATOM   823  N  N   . ILE A 1 113 ? 52.290 66.470  25.319 1.00 59.63  ?  113 ILE A N   1 
ATOM   824  C  CA  . ILE A 1 113 ? 51.734 66.971  24.071 1.00 55.87  ?  113 ILE A CA  1 
ATOM   825  C  C   . ILE A 1 113 ? 50.442 66.230  23.766 1.00 54.88  ?  113 ILE A C   1 
ATOM   826  O  O   . ILE A 1 113 ? 50.354 65.005  23.922 1.00 60.70  ?  113 ILE A O   1 
ATOM   827  C  CB  . ILE A 1 113 ? 52.757 66.838  22.936 1.00 54.67  ?  113 ILE A CB  1 
ATOM   828  C  CG1 . ILE A 1 113 ? 53.995 67.675  23.269 1.00 60.33  ?  113 ILE A CG1 1 
ATOM   829  C  CG2 . ILE A 1 113 ? 52.139 67.254  21.602 1.00 50.49  ?  113 ILE A CG2 1 
ATOM   830  C  CD1 . ILE A 1 113 ? 54.840 68.048  22.058 1.00 65.18  ?  113 ILE A CD1 1 
ATOM   831  N  N   . GLY A 1 114 ? 49.426 66.974  23.349 1.00 50.69  ?  114 GLY A N   1 
ATOM   832  C  CA  . GLY A 1 114 ? 48.124 66.389  23.124 1.00 51.08  ?  114 GLY A CA  1 
ATOM   833  C  C   . GLY A 1 114 ? 47.276 66.242  24.364 1.00 47.02  ?  114 GLY A C   1 
ATOM   834  O  O   . GLY A 1 114 ? 46.206 65.627  24.302 1.00 46.55  ?  114 GLY A O   1 
ATOM   835  N  N   . ARG A 1 115 ? 47.719 66.762  25.491 1.00 50.61  ?  115 ARG A N   1 
ATOM   836  C  CA  . ARG A 1 115 ? 46.907 66.765  26.693 1.00 53.01  ?  115 ARG A CA  1 
ATOM   837  C  C   . ARG A 1 115 ? 46.474 68.197  26.984 1.00 53.57  ?  115 ARG A C   1 
ATOM   838  O  O   . ARG A 1 115 ? 46.772 69.125  26.221 1.00 57.35  ?  115 ARG A O   1 
ATOM   839  C  CB  . ARG A 1 115 ? 47.673 66.117  27.846 1.00 49.07  ?  115 ARG A CB  1 
ATOM   840  C  CG  . ARG A 1 115 ? 48.208 64.738  27.460 1.00 52.29  ?  115 ARG A CG  1 
ATOM   841  C  CD  . ARG A 1 115 ? 48.749 63.980  28.653 1.00 58.30  ?  115 ARG A CD  1 
ATOM   842  N  NE  . ARG A 1 115 ? 49.494 62.798  28.239 1.00 68.34  ?  115 ARG A NE  1 
ATOM   843  C  CZ  . ARG A 1 115 ? 49.009 61.564  28.241 1.00 72.02  ?  115 ARG A CZ  1 
ATOM   844  N  NH1 . ARG A 1 115 ? 47.769 61.339  28.645 1.00 72.76  1  115 ARG A NH1 1 
ATOM   845  N  NH2 . ARG A 1 115 ? 49.774 60.553  27.852 1.00 74.30  ?  115 ARG A NH2 1 
ATOM   846  N  N   . THR A 1 116 ? 45.746 68.378  28.082 1.00 51.42  ?  116 THR A N   1 
ATOM   847  C  CA  . THR A 1 116 ? 45.074 69.641  28.356 1.00 47.79  ?  116 THR A CA  1 
ATOM   848  C  C   . THR A 1 116 ? 45.719 70.342  29.542 1.00 46.79  ?  116 THR A C   1 
ATOM   849  O  O   . THR A 1 116 ? 45.916 69.735  30.597 1.00 52.88  ?  116 THR A O   1 
ATOM   850  C  CB  . THR A 1 116 ? 43.588 69.422  28.628 1.00 52.61  ?  116 THR A CB  1 
ATOM   851  O  OG1 . THR A 1 116 ? 42.954 68.905  27.450 1.00 53.40  ?  116 THR A OG1 1 
ATOM   852  C  CG2 . THR A 1 116 ? 42.936 70.738  28.978 1.00 51.74  ?  116 THR A CG2 1 
ATOM   853  N  N   . LEU A 1 117 ? 46.047 71.616  29.364 1.00 44.86  ?  117 LEU A N   1 
ATOM   854  C  CA  . LEU A 1 117 ? 46.500 72.457  30.462 1.00 43.76  ?  117 LEU A CA  1 
ATOM   855  C  C   . LEU A 1 117 ? 45.302 73.220  31.007 1.00 43.92  ?  117 LEU A C   1 
ATOM   856  O  O   . LEU A 1 117 ? 44.450 73.676  30.236 1.00 42.09  ?  117 LEU A O   1 
ATOM   857  C  CB  . LEU A 1 117 ? 47.580 73.431  29.986 1.00 46.36  ?  117 LEU A CB  1 
ATOM   858  C  CG  . LEU A 1 117 ? 48.133 74.421  31.007 1.00 47.10  ?  117 LEU A CG  1 
ATOM   859  C  CD1 . LEU A 1 117 ? 48.937 73.663  32.054 1.00 46.04  ?  117 LEU A CD1 1 
ATOM   860  C  CD2 . LEU A 1 117 ? 48.998 75.455  30.332 1.00 39.36  ?  117 LEU A CD2 1 
ATOM   861  N  N   . VAL A 1 118 ? 45.236 73.368  32.333 1.00 41.20  ?  118 VAL A N   1 
ATOM   862  C  CA  . VAL A 1 118 ? 44.046 73.906  32.989 1.00 44.59  ?  118 VAL A CA  1 
ATOM   863  C  C   . VAL A 1 118 ? 44.453 74.900  34.082 1.00 49.92  ?  118 VAL A C   1 
ATOM   864  O  O   . VAL A 1 118 ? 45.344 74.607  34.888 1.00 60.81  ?  118 VAL A O   1 
ATOM   865  C  CB  . VAL A 1 118 ? 43.182 72.767  33.573 1.00 40.90  ?  118 VAL A CB  1 
ATOM   866  C  CG1 . VAL A 1 118 ? 41.951 73.315  34.269 1.00 40.19  ?  118 VAL A CG1 1 
ATOM   867  C  CG2 . VAL A 1 118 ? 42.786 71.769  32.492 1.00 35.61  ?  118 VAL A CG2 1 
ATOM   868  N  N   . VAL A 1 119 ? 43.788 76.082  34.108 1.00 43.45  ?  119 VAL A N   1 
ATOM   869  C  CA  . VAL A 1 119 ? 43.871 77.061  35.199 1.00 43.65  ?  119 VAL A CA  1 
ATOM   870  C  C   . VAL A 1 119 ? 42.628 76.928  36.070 1.00 49.22  ?  119 VAL A C   1 
ATOM   871  O  O   . VAL A 1 119 ? 41.515 76.745  35.560 1.00 55.39  ?  119 VAL A O   1 
ATOM   872  C  CB  . VAL A 1 119 ? 43.973 78.510  34.676 1.00 46.78  ?  119 VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 119 ? 44.561 79.418  35.745 1.00 48.88  ?  119 VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 119 ? 44.784 78.572  33.428 1.00 56.67  ?  119 VAL A CG2 1 
ATOM   875  N  N   . HIS A 1 120 ? 42.797 77.085  37.376 1.00 45.38  ?  120 HIS A N   1 
ATOM   876  C  CA  . HIS A 1 120 ? 41.744 76.753  38.320 1.00 43.19  ?  120 HIS A CA  1 
ATOM   877  C  C   . HIS A 1 120 ? 41.215 77.976  39.063 1.00 46.07  ?  120 HIS A C   1 
ATOM   878  O  O   . HIS A 1 120 ? 41.895 78.997  39.221 1.00 44.29  ?  120 HIS A O   1 
ATOM   879  C  CB  . HIS A 1 120 ? 42.252 75.707  39.315 1.00 50.75  ?  120 HIS A CB  1 
ATOM   880  C  CG  . HIS A 1 120 ? 42.119 74.303  38.816 1.00 53.48  ?  120 HIS A CG  1 
ATOM   881  N  ND1 . HIS A 1 120 ? 40.981 73.557  39.022 1.00 56.27  ?  120 HIS A ND1 1 
ATOM   882  C  CD2 . HIS A 1 120 ? 42.966 73.515  38.110 1.00 50.06  ?  120 HIS A CD2 1 
ATOM   883  C  CE1 . HIS A 1 120 ? 41.130 72.370  38.462 1.00 60.31  ?  120 HIS A CE1 1 
ATOM   884  N  NE2 . HIS A 1 120 ? 42.330 72.315  37.910 1.00 51.89  ?  120 HIS A NE2 1 
ATOM   885  N  N   . GLU A 1 121 ? 39.982 77.823  39.554 1.00 43.73  ?  121 GLU A N   1 
ATOM   886  C  CA  . GLU A 1 121 ? 39.286 78.895  40.260 1.00 43.74  ?  121 GLU A CA  1 
ATOM   887  C  C   . GLU A 1 121 ? 39.986 79.273  41.564 1.00 50.15  ?  121 GLU A C   1 
ATOM   888  O  O   . GLU A 1 121 ? 40.084 80.459  41.905 1.00 49.53  ?  121 GLU A O   1 
ATOM   889  C  CB  . GLU A 1 121 ? 37.855 78.442  40.532 1.00 44.28  ?  121 GLU A CB  1 
ATOM   890  C  CG  . GLU A 1 121 ? 37.083 79.267  41.531 1.00 51.29  ?  121 GLU A CG  1 
ATOM   891  C  CD  . GLU A 1 121 ? 35.757 78.616  41.850 1.00 59.86  ?  121 GLU A CD  1 
ATOM   892  O  OE1 . GLU A 1 121 ? 35.728 77.365  41.891 1.00 70.26  ?  121 GLU A OE1 1 
ATOM   893  O  OE2 . GLU A 1 121 ? 34.751 79.337  42.041 1.00 61.07  -1 121 GLU A OE2 1 
ATOM   894  N  N   . LYS A 1 122 ? 40.471 78.282  42.306 1.00 58.36  ?  122 LYS A N   1 
ATOM   895  C  CA  . LYS A 1 122 ? 41.008 78.468  43.648 1.00 49.03  ?  122 LYS A CA  1 
ATOM   896  C  C   . LYS A 1 122 ? 42.473 78.064  43.690 1.00 51.60  ?  122 LYS A C   1 
ATOM   897  O  O   . LYS A 1 122 ? 43.017 77.488  42.743 1.00 49.70  ?  122 LYS A O   1 
ATOM   898  C  CB  . LYS A 1 122 ? 40.209 77.651  44.675 1.00 50.69  ?  122 LYS A CB  1 
ATOM   899  C  CG  . LYS A 1 122 ? 39.044 78.418  45.305 1.00 57.43  ?  122 LYS A CG  1 
ATOM   900  C  CD  . LYS A 1 122 ? 37.958 77.505  45.874 1.00 51.57  ?  122 LYS A CD  1 
ATOM   901  C  CE  . LYS A 1 122 ? 37.315 76.662  44.802 1.00 66.59  ?  122 LYS A CE  1 
ATOM   902  N  NZ  . LYS A 1 122 ? 36.831 75.353  45.338 1.00 81.62  1  122 LYS A NZ  1 
ATOM   903  N  N   . ALA A 1 123 ? 43.117 78.368  44.813 1.00 56.74  ?  123 ALA A N   1 
ATOM   904  C  CA  . ALA A 1 123 ? 44.501 77.960  44.994 1.00 55.03  ?  123 ALA A CA  1 
ATOM   905  C  C   . ALA A 1 123 ? 44.598 76.453  45.211 1.00 65.78  ?  123 ALA A C   1 
ATOM   906  O  O   . ALA A 1 123 ? 43.742 75.837  45.856 1.00 68.26  ?  123 ALA A O   1 
ATOM   907  C  CB  . ALA A 1 123 ? 45.126 78.701  46.174 1.00 46.86  ?  123 ALA A CB  1 
ATOM   908  N  N   . ASP A 1 124 ? 45.643 75.859  44.644 1.00 64.68  ?  124 ASP A N   1 
ATOM   909  C  CA  . ASP A 1 124 ? 45.990 74.468  44.901 1.00 61.58  ?  124 ASP A CA  1 
ATOM   910  C  C   . ASP A 1 124 ? 46.650 74.395  46.277 1.00 68.33  ?  124 ASP A C   1 
ATOM   911  O  O   . ASP A 1 124 ? 47.586 75.156  46.554 1.00 59.49  ?  124 ASP A O   1 
ATOM   912  C  CB  . ASP A 1 124 ? 46.944 73.974  43.812 1.00 50.90  ?  124 ASP A CB  1 
ATOM   913  C  CG  . ASP A 1 124 ? 47.261 72.500  43.916 1.00 54.30  ?  124 ASP A CG  1 
ATOM   914  O  OD1 . ASP A 1 124 ? 46.881 71.847  44.914 1.00 65.36  ?  124 ASP A OD1 1 
ATOM   915  O  OD2 . ASP A 1 124 ? 47.899 71.982  42.976 1.00 53.70  -1 124 ASP A OD2 1 
ATOM   916  N  N   . ASP A 1 125 ? 46.176 73.501  47.152 1.00 75.85  ?  125 ASP A N   1 
ATOM   917  C  CA  . ASP A 1 125 ? 46.864 73.354  48.434 1.00 72.64  ?  125 ASP A CA  1 
ATOM   918  C  C   . ASP A 1 125 ? 48.017 72.354  48.370 1.00 62.37  ?  125 ASP A C   1 
ATOM   919  O  O   . ASP A 1 125 ? 48.641 72.077  49.400 1.00 54.64  ?  125 ASP A O   1 
ATOM   920  C  CB  . ASP A 1 125 ? 45.868 73.002  49.560 1.00 68.40  ?  125 ASP A CB  1 
ATOM   921  C  CG  . ASP A 1 125 ? 45.152 71.676  49.358 1.00 68.53  ?  125 ASP A CG  1 
ATOM   922  O  OD1 . ASP A 1 125 ? 45.726 70.719  48.785 1.00 72.79  ?  125 ASP A OD1 1 
ATOM   923  O  OD2 . ASP A 1 125 ? 43.992 71.602  49.817 1.00 64.60  -1 125 ASP A OD2 1 
ATOM   924  N  N   . LEU A 1 126 ? 48.322 71.847  47.175 1.00 68.51  ?  126 LEU A N   1 
ATOM   925  C  CA  . LEU A 1 126 ? 49.482 70.993  46.909 1.00 68.70  ?  126 LEU A CA  1 
ATOM   926  C  C   . LEU A 1 126 ? 49.441 69.696  47.708 1.00 71.73  ?  126 LEU A C   1 
ATOM   927  O  O   . LEU A 1 126 ? 50.487 69.121  48.008 1.00 67.84  ?  126 LEU A O   1 
ATOM   928  C  CB  . LEU A 1 126 ? 50.807 71.726  47.150 1.00 57.90  ?  126 LEU A CB  1 
ATOM   929  C  CG  . LEU A 1 126 ? 51.093 72.981  46.313 1.00 57.36  ?  126 LEU A CG  1 
ATOM   930  C  CD1 . LEU A 1 126 ? 50.347 74.167  46.842 1.00 56.70  ?  126 LEU A CD1 1 
ATOM   931  C  CD2 . LEU A 1 126 ? 52.567 73.326  46.198 1.00 65.81  ?  126 LEU A CD2 1 
ATOM   932  N  N   . GLY A 1 127 ? 48.232 69.222  48.045 1.00 81.68  ?  127 GLY A N   1 
ATOM   933  C  CA  . GLY A 1 127 ? 48.040 67.949  48.715 1.00 80.75  ?  127 GLY A CA  1 
ATOM   934  C  C   . GLY A 1 127 ? 48.065 67.980  50.232 1.00 79.17  ?  127 GLY A C   1 
ATOM   935  O  O   . GLY A 1 127 ? 47.890 66.926  50.861 1.00 79.67  ?  127 GLY A O   1 
ATOM   936  N  N   . LYS A 1 128 ? 48.252 69.148  50.844 1.00 74.08  ?  128 LYS A N   1 
ATOM   937  C  CA  . LYS A 1 128 ? 48.397 69.257  52.289 1.00 70.08  ?  128 LYS A CA  1 
ATOM   938  C  C   . LYS A 1 128 ? 47.131 69.765  52.968 1.00 70.19  ?  128 LYS A C   1 
ATOM   939  O  O   . LYS A 1 128 ? 47.213 70.354  54.051 1.00 72.33  ?  128 LYS A O   1 
ATOM   940  C  CB  . LYS A 1 128 ? 49.565 70.178  52.639 1.00 69.11  ?  128 LYS A CB  1 
ATOM   941  C  CG  . LYS A 1 128 ? 50.622 70.310  51.558 1.00 71.06  ?  128 LYS A CG  1 
ATOM   942  C  CD  . LYS A 1 128 ? 51.316 69.000  51.285 1.00 72.19  ?  128 LYS A CD  1 
ATOM   943  C  CE  . LYS A 1 128 ? 52.567 69.248  50.500 1.00 74.48  ?  128 LYS A CE  1 
ATOM   944  N  NZ  . LYS A 1 128 ? 53.535 70.059  51.275 1.00 77.65  1  128 LYS A NZ  1 
ATOM   945  N  N   . GLY A 1 129 ? 45.966 69.570  52.350 1.00 71.31  ?  129 GLY A N   1 
ATOM   946  C  CA  . GLY A 1 129 ? 44.744 70.112  52.919 1.00 78.43  ?  129 GLY A CA  1 
ATOM   947  C  C   . GLY A 1 129 ? 44.293 69.389  54.171 1.00 85.45  ?  129 GLY A C   1 
ATOM   948  O  O   . GLY A 1 129 ? 43.658 69.990  55.044 1.00 84.24  ?  129 GLY A O   1 
ATOM   949  N  N   . GLY A 1 130 ? 44.611 68.102  54.283 1.00 87.67  ?  130 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 130 ? 44.153 67.300  55.393 1.00 84.71  ?  130 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 130 ? 42.886 66.521  55.134 1.00 86.39  ?  130 GLY A C   1 
ATOM   952  O  O   . GLY A 1 130 ? 42.434 65.797  56.030 1.00 90.42  ?  130 GLY A O   1 
ATOM   953  N  N   . ASN A 1 131 ? 42.293 66.651  53.952 1.00 85.25  ?  131 ASN A N   1 
ATOM   954  C  CA  . ASN A 1 131 ? 41.155 65.840  53.544 1.00 83.92  ?  131 ASN A CA  1 
ATOM   955  C  C   . ASN A 1 131 ? 41.536 65.000  52.327 1.00 77.35  ?  131 ASN A C   1 
ATOM   956  O  O   . ASN A 1 131 ? 42.671 65.049  51.835 1.00 65.91  ?  131 ASN A O   1 
ATOM   957  C  CB  . ASN A 1 131 ? 39.924 66.709  53.263 1.00 80.65  ?  131 ASN A CB  1 
ATOM   958  C  CG  . ASN A 1 131 ? 40.208 67.824  52.286 1.00 82.81  ?  131 ASN A CG  1 
ATOM   959  O  OD1 . ASN A 1 131 ? 40.526 67.588  51.119 1.00 83.27  ?  131 ASN A OD1 1 
ATOM   960  N  ND2 . ASN A 1 131 ? 40.104 69.055  52.761 1.00 87.02  ?  131 ASN A ND2 1 
ATOM   961  N  N   . GLU A 1 132 ? 40.555 64.216  51.856 1.00 88.18  ?  132 GLU A N   1 
ATOM   962  C  CA  . GLU A 1 132 ? 40.792 63.261  50.774 1.00 95.24  ?  132 GLU A CA  1 
ATOM   963  C  C   . GLU A 1 132 ? 40.866 63.962  49.424 1.00 89.39  ?  132 GLU A C   1 
ATOM   964  O  O   . GLU A 1 132 ? 41.676 63.581  48.570 1.00 81.68  ?  132 GLU A O   1 
ATOM   965  C  CB  . GLU A 1 132 ? 39.696 62.180  50.745 1.00 105.43 ?  132 GLU A CB  1 
ATOM   966  C  CG  . GLU A 1 132 ? 39.200 61.655  52.128 1.00 117.75 ?  132 GLU A CG  1 
ATOM   967  C  CD  . GLU A 1 132 ? 38.120 62.557  52.789 1.00 125.07 ?  132 GLU A CD  1 
ATOM   968  O  OE1 . GLU A 1 132 ? 38.431 63.709  53.188 1.00 121.99 ?  132 GLU A OE1 1 
ATOM   969  O  OE2 . GLU A 1 132 ? 36.957 62.094  52.902 1.00 129.64 -1 132 GLU A OE2 1 
ATOM   970  N  N   . GLU A 1 133 ? 40.017 64.975  49.204 1.00 91.24  ?  133 GLU A N   1 
ATOM   971  C  CA  . GLU A 1 133 ? 40.045 65.689  47.931 1.00 84.02  ?  133 GLU A CA  1 
ATOM   972  C  C   . GLU A 1 133 ? 41.379 66.392  47.729 1.00 78.35  ?  133 GLU A C   1 
ATOM   973  O  O   . GLU A 1 133 ? 41.869 66.476  46.599 1.00 84.40  ?  133 GLU A O   1 
ATOM   974  C  CB  . GLU A 1 133 ? 38.891 66.689  47.855 1.00 74.67  ?  133 GLU A CB  1 
ATOM   975  C  CG  . GLU A 1 133 ? 38.728 67.353  46.499 1.00 71.70  ?  133 GLU A CG  1 
ATOM   976  C  CD  . GLU A 1 133 ? 37.879 66.514  45.544 1.00 80.64  ?  133 GLU A CD  1 
ATOM   977  O  OE1 . GLU A 1 133 ? 37.040 65.721  46.018 1.00 90.22  ?  133 GLU A OE1 1 
ATOM   978  O  OE2 . GLU A 1 133 ? 38.042 66.644  44.311 1.00 80.24  -1 133 GLU A OE2 1 
ATOM   979  N  N   . SER A 1 134 ? 41.997 66.862  48.815 1.00 67.69  ?  134 SER A N   1 
ATOM   980  C  CA  . SER A 1 134 ? 43.307 67.492  48.711 1.00 62.91  ?  134 SER A CA  1 
ATOM   981  C  C   . SER A 1 134 ? 44.346 66.548  48.120 1.00 67.47  ?  134 SER A C   1 
ATOM   982  O  O   . SER A 1 134 ? 45.303 66.998  47.476 1.00 64.62  ?  134 SER A O   1 
ATOM   983  C  CB  . SER A 1 134 ? 43.756 67.982  50.084 1.00 65.49  ?  134 SER A CB  1 
ATOM   984  O  OG  . SER A 1 134 ? 45.129 68.332  50.055 1.00 69.11  ?  134 SER A OG  1 
ATOM   985  N  N   . THR A 1 135 ? 44.190 65.246  48.340 1.00 78.47  ?  135 THR A N   1 
ATOM   986  C  CA  . THR A 1 135 ? 45.101 64.269  47.761 1.00 78.74  ?  135 THR A CA  1 
ATOM   987  C  C   . THR A 1 135 ? 44.725 63.913  46.332 1.00 77.56  ?  135 THR A C   1 
ATOM   988  O  O   . THR A 1 135 ? 45.465 63.172  45.676 1.00 74.51  ?  135 THR A O   1 
ATOM   989  C  CB  . THR A 1 135 ? 45.135 63.008  48.625 1.00 74.54  ?  135 THR A CB  1 
ATOM   990  O  OG1 . THR A 1 135 ? 43.854 62.363  48.575 1.00 82.47  ?  135 THR A OG1 1 
ATOM   991  C  CG2 . THR A 1 135 ? 45.458 63.376  50.071 1.00 62.78  ?  135 THR A CG2 1 
ATOM   992  N  N   . LYS A 1 136 ? 43.602 64.434  45.842 1.00 76.50  ?  136 LYS A N   1 
ATOM   993  C  CA  . LYS A 1 136 ? 43.179 64.285  44.458 1.00 82.22  ?  136 LYS A CA  1 
ATOM   994  C  C   . LYS A 1 136 ? 43.419 65.542  43.635 1.00 82.01  ?  136 LYS A C   1 
ATOM   995  O  O   . LYS A 1 136 ? 44.023 65.470  42.562 1.00 74.32  ?  136 LYS A O   1 
ATOM   996  C  CB  . LYS A 1 136 ? 41.683 63.925  44.398 1.00 85.66  ?  136 LYS A CB  1 
ATOM   997  C  CG  . LYS A 1 136 ? 41.284 62.581  44.997 1.00 88.42  ?  136 LYS A CG  1 
ATOM   998  C  CD  . LYS A 1 136 ? 39.775 62.338  44.829 1.00 89.83  ?  136 LYS A CD  1 
ATOM   999  C  CE  . LYS A 1 136 ? 39.019 62.437  46.162 1.00 93.29  ?  136 LYS A CE  1 
ATOM   1000 N  NZ  . LYS A 1 136 ? 37.661 63.066  46.055 1.00 85.71  1  136 LYS A NZ  1 
ATOM   1001 N  N   . THR A 1 137 ? 42.942 66.697  44.118 1.00 81.35  ?  137 THR A N   1 
ATOM   1002 C  CA  . THR A 1 137 ? 42.854 67.915  43.328 1.00 69.20  ?  137 THR A CA  1 
ATOM   1003 C  C   . THR A 1 137 ? 43.562 69.107  43.944 1.00 63.33  ?  137 THR A C   1 
ATOM   1004 O  O   . THR A 1 137 ? 43.695 70.131  43.271 1.00 70.27  ?  137 THR A O   1 
ATOM   1005 C  CB  . THR A 1 137 ? 41.385 68.302  43.090 1.00 71.51  ?  137 THR A CB  1 
ATOM   1006 O  OG1 . THR A 1 137 ? 40.773 68.610  44.340 1.00 78.39  ?  137 THR A OG1 1 
ATOM   1007 C  CG2 . THR A 1 137 ? 40.602 67.190  42.396 1.00 66.64  ?  137 THR A CG2 1 
ATOM   1008 N  N   . GLY A 1 138 ? 44.036 69.005  45.182 1.00 63.20  ?  138 GLY A N   1 
ATOM   1009 C  CA  . GLY A 1 138 ? 44.518 70.180  45.872 1.00 62.72  ?  138 GLY A CA  1 
ATOM   1010 C  C   . GLY A 1 138 ? 43.417 71.136  46.248 1.00 63.15  ?  138 GLY A C   1 
ATOM   1011 O  O   . GLY A 1 138 ? 43.694 72.292  46.575 1.00 68.89  ?  138 GLY A O   1 
ATOM   1012 N  N   . ASN A 1 139 ? 42.167 70.671  46.218 1.00 62.70  ?  139 ASN A N   1 
ATOM   1013 C  CA  . ASN A 1 139 ? 40.992 71.514  46.448 1.00 67.27  ?  139 ASN A CA  1 
ATOM   1014 C  C   . ASN A 1 139 ? 41.037 72.774  45.582 1.00 67.27  ?  139 ASN A C   1 
ATOM   1015 O  O   . ASN A 1 139 ? 40.602 73.851  45.997 1.00 64.20  ?  139 ASN A O   1 
ATOM   1016 C  CB  . ASN A 1 139 ? 40.847 71.868  47.933 1.00 68.42  ?  139 ASN A CB  1 
ATOM   1017 C  CG  . ASN A 1 139 ? 40.452 70.670  48.791 1.00 69.38  ?  139 ASN A CG  1 
ATOM   1018 O  OD1 . ASN A 1 139 ? 39.512 69.940  48.472 1.00 71.60  ?  139 ASN A OD1 1 
ATOM   1019 N  ND2 . ASN A 1 139 ? 41.179 70.461  49.883 1.00 72.51  ?  139 ASN A ND2 1 
ATOM   1020 N  N   . ALA A 1 140 ? 41.563 72.639  44.360 1.00 63.55  ?  140 ALA A N   1 
ATOM   1021 C  CA  . ALA A 1 140 ? 41.776 73.798  43.503 1.00 59.34  ?  140 ALA A CA  1 
ATOM   1022 C  C   . ALA A 1 140 ? 40.488 74.332  42.885 1.00 60.60  ?  140 ALA A C   1 
ATOM   1023 O  O   . ALA A 1 140 ? 40.482 75.462  42.384 1.00 61.33  ?  140 ALA A O   1 
ATOM   1024 C  CB  . ALA A 1 140 ? 42.784 73.459  42.401 1.00 53.11  ?  140 ALA A CB  1 
ATOM   1025 N  N   . GLY A 1 141 ? 39.406 73.569  42.904 1.00 64.45  ?  141 GLY A N   1 
ATOM   1026 C  CA  . GLY A 1 141 ? 38.135 74.093  42.441 1.00 61.55  ?  141 GLY A CA  1 
ATOM   1027 C  C   . GLY A 1 141 ? 37.928 73.950  40.945 1.00 51.73  ?  141 GLY A C   1 
ATOM   1028 O  O   . GLY A 1 141 ? 38.588 73.167  40.259 1.00 53.34  ?  141 GLY A O   1 
ATOM   1029 N  N   . SER A 1 142 ? 36.987 74.735  40.434 1.00 56.48  ?  142 SER A N   1 
ATOM   1030 C  CA  . SER A 1 142 ? 36.543 74.520  39.067 1.00 57.55  ?  142 SER A CA  1 
ATOM   1031 C  C   . SER A 1 142 ? 37.579 75.021  38.067 1.00 55.56  ?  142 SER A C   1 
ATOM   1032 O  O   . SER A 1 142 ? 38.470 75.822  38.387 1.00 51.88  ?  142 SER A O   1 
ATOM   1033 C  CB  . SER A 1 142 ? 35.192 75.198  38.807 1.00 55.46  ?  142 SER A CB  1 
ATOM   1034 O  OG  . SER A 1 142 ? 35.286 76.609  38.903 1.00 60.17  ?  142 SER A OG  1 
ATOM   1035 N  N   . ARG A 1 143 ? 37.427 74.537  36.831 1.00 58.76  ?  143 ARG A N   1 
ATOM   1036 C  CA  . ARG A 1 143 ? 38.367 74.780  35.741 1.00 50.99  ?  143 ARG A CA  1 
ATOM   1037 C  C   . ARG A 1 143 ? 37.897 76.000  34.951 1.00 47.49  ?  143 ARG A C   1 
ATOM   1038 O  O   . ARG A 1 143 ? 36.870 75.944  34.270 1.00 55.86  ?  143 ARG A O   1 
ATOM   1039 C  CB  . ARG A 1 143 ? 38.469 73.530  34.864 1.00 45.04  ?  143 ARG A CB  1 
ATOM   1040 C  CG  . ARG A 1 143 ? 38.324 72.221  35.656 1.00 45.53  ?  143 ARG A CG  1 
ATOM   1041 C  CD  . ARG A 1 143 ? 38.502 70.931  34.799 1.00 46.09  ?  143 ARG A CD  1 
ATOM   1042 N  NE  . ARG A 1 143 ? 38.618 69.776  35.667 1.00 52.85  ?  143 ARG A NE  1 
ATOM   1043 C  CZ  . ARG A 1 143 ? 38.776 68.519  35.247 1.00 56.75  ?  143 ARG A CZ  1 
ATOM   1044 N  NH1 . ARG A 1 143 ? 38.849 68.233  33.946 1.00 47.09  1  143 ARG A NH1 1 
ATOM   1045 N  NH2 . ARG A 1 143 ? 38.885 67.522  36.132 1.00 58.47  ?  143 ARG A NH2 1 
ATOM   1046 N  N   . LEU A 1 144 ? 38.640 77.113  35.055 1.00 44.02  ?  144 LEU A N   1 
ATOM   1047 C  CA  . LEU A 1 144 ? 38.207 78.356  34.421 1.00 38.27  ?  144 LEU A CA  1 
ATOM   1048 C  C   . LEU A 1 144 ? 38.573 78.401  32.939 1.00 45.93  ?  144 LEU A C   1 
ATOM   1049 O  O   . LEU A 1 144 ? 37.823 78.958  32.127 1.00 45.33  ?  144 LEU A O   1 
ATOM   1050 C  CB  . LEU A 1 144 ? 38.813 79.560  35.144 1.00 34.34  ?  144 LEU A CB  1 
ATOM   1051 C  CG  . LEU A 1 144 ? 38.559 79.690  36.645 1.00 38.12  ?  144 LEU A CG  1 
ATOM   1052 C  CD1 . LEU A 1 144 ? 39.111 81.005  37.140 1.00 41.84  ?  144 LEU A CD1 1 
ATOM   1053 C  CD2 . LEU A 1 144 ? 37.083 79.578  36.951 1.00 41.15  ?  144 LEU A CD2 1 
ATOM   1054 N  N   . ALA A 1 145 ? 39.717 77.833  32.566 1.00 48.65  ?  145 ALA A N   1 
ATOM   1055 C  CA  . ALA A 1 145 ? 40.155 77.889  31.177 1.00 43.89  ?  145 ALA A CA  1 
ATOM   1056 C  C   . ALA A 1 145 ? 41.100 76.732  30.911 1.00 48.57  ?  145 ALA A C   1 
ATOM   1057 O  O   . ALA A 1 145 ? 41.818 76.274  31.813 1.00 44.70  ?  145 ALA A O   1 
ATOM   1058 C  CB  . ALA A 1 145 ? 40.843 79.222  30.857 1.00 32.49  ?  145 ALA A CB  1 
ATOM   1059 N  N   . CYS A 1 146 ? 41.113 76.277  29.659 1.00 48.39  ?  146 CYS A N   1 
ATOM   1060 C  CA  . CYS A 1 146 ? 41.944 75.135  29.309 1.00 43.76  ?  146 CYS A CA  1 
ATOM   1061 C  C   . CYS A 1 146 ? 42.211 75.126  27.814 1.00 41.80  ?  146 CYS A C   1 
ATOM   1062 O  O   . CYS A 1 146 ? 41.536 75.802  27.031 1.00 42.16  ?  146 CYS A O   1 
ATOM   1063 C  CB  . CYS A 1 146 ? 41.285 73.822  29.733 1.00 42.65  ?  146 CYS A CB  1 
ATOM   1064 S  SG  . CYS A 1 146 ? 39.664 73.611  29.023 1.00 54.78  ?  146 CYS A SG  1 
ATOM   1065 N  N   . GLY A 1 147 ? 43.208 74.339  27.429 1.00 41.40  ?  147 GLY A N   1 
ATOM   1066 C  CA  . GLY A 1 147 ? 43.492 74.139  26.021 1.00 46.28  ?  147 GLY A CA  1 
ATOM   1067 C  C   . GLY A 1 147 ? 44.324 72.896  25.817 1.00 47.66  ?  147 GLY A C   1 
ATOM   1068 O  O   . GLY A 1 147 ? 44.943 72.377  26.751 1.00 51.09  ?  147 GLY A O   1 
ATOM   1069 N  N   . VAL A 1 148 ? 44.325 72.417  24.585 1.00 46.08  ?  148 VAL A N   1 
ATOM   1070 C  CA  . VAL A 1 148 ? 45.128 71.259  24.215 1.00 46.06  ?  148 VAL A CA  1 
ATOM   1071 C  C   . VAL A 1 148 ? 46.531 71.749  23.898 1.00 47.48  ?  148 VAL A C   1 
ATOM   1072 O  O   . VAL A 1 148 ? 46.712 72.842  23.351 1.00 54.96  ?  148 VAL A O   1 
ATOM   1073 C  CB  . VAL A 1 148 ? 44.507 70.506  23.023 1.00 42.22  ?  148 VAL A CB  1 
ATOM   1074 C  CG1 . VAL A 1 148 ? 45.336 69.270  22.686 1.00 38.61  ?  148 VAL A CG1 1 
ATOM   1075 C  CG2 . VAL A 1 148 ? 43.077 70.104  23.337 1.00 39.43  ?  148 VAL A CG2 1 
ATOM   1076 N  N   . ILE A 1 149 ? 47.526 70.963  24.279 1.00 44.96  ?  149 ILE A N   1 
ATOM   1077 C  CA  . ILE A 1 149 ? 48.926 71.313  24.074 1.00 48.42  ?  149 ILE A CA  1 
ATOM   1078 C  C   . ILE A 1 149 ? 49.363 70.786  22.714 1.00 48.41  ?  149 ILE A C   1 
ATOM   1079 O  O   . ILE A 1 149 ? 49.348 69.574  22.483 1.00 52.61  ?  149 ILE A O   1 
ATOM   1080 C  CB  . ILE A 1 149 ? 49.803 70.732  25.191 1.00 44.55  ?  149 ILE A CB  1 
ATOM   1081 C  CG1 . ILE A 1 149 ? 49.375 71.310  26.542 1.00 44.76  ?  149 ILE A CG1 1 
ATOM   1082 C  CG2 . ILE A 1 149 ? 51.259 71.046  24.907 1.00 46.06  ?  149 ILE A CG2 1 
ATOM   1083 C  CD1 . ILE A 1 149 ? 49.987 70.604  27.729 1.00 51.32  ?  149 ILE A CD1 1 
ATOM   1084 N  N   . GLY A 1 150 ? 49.742 71.690  21.807 1.00 45.51  ?  150 GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 150 ? 50.140 71.269  20.472 1.00 50.23  ?  150 GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 150 ? 51.621 71.432  20.173 1.00 59.46  ?  150 GLY A C   1 
ATOM   1087 O  O   . GLY A 1 150 ? 52.321 72.143  20.898 1.00 71.83  ?  150 GLY A O   1 
ATOM   1088 N  N   . ILE A 1 151 ? 52.116 70.768  19.119 1.00 58.33  ?  151 ILE A N   1 
ATOM   1089 C  CA  . ILE A 1 151 ? 53.481 71.009  18.649 1.00 64.35  ?  151 ILE A CA  1 
ATOM   1090 C  C   . ILE A 1 151 ? 53.579 72.447  18.151 1.00 68.57  ?  151 ILE A C   1 
ATOM   1091 O  O   . ILE A 1 151 ? 52.766 72.895  17.328 1.00 63.59  ?  151 ILE A O   1 
ATOM   1092 C  CB  . ILE A 1 151 ? 53.869 70.000  17.548 1.00 64.21  ?  151 ILE A CB  1 
ATOM   1093 C  CG1 . ILE A 1 151 ? 53.978 68.567  18.094 1.00 62.30  ?  151 ILE A CG1 1 
ATOM   1094 C  CG2 . ILE A 1 151 ? 55.187 70.398  16.887 1.00 70.83  ?  151 ILE A CG2 1 
ATOM   1095 C  CD1 . ILE A 1 151 ? 53.974 67.435  16.989 1.00 50.46  ?  151 ILE A CD1 1 
ATOM   1096 N  N   . ALA A 1 152 ? 54.565 73.186  18.659 1.00 69.16  ?  152 ALA A N   1 
ATOM   1097 C  CA  . ALA A 1 152 ? 54.723 74.598  18.336 1.00 66.41  ?  152 ALA A CA  1 
ATOM   1098 C  C   . ALA A 1 152 ? 55.915 74.824  17.410 1.00 63.45  ?  152 ALA A C   1 
ATOM   1099 O  O   . ALA A 1 152 ? 56.877 74.049  17.397 1.00 68.48  ?  152 ALA A O   1 
ATOM   1100 C  CB  . ALA A 1 152 ? 54.891 75.441  19.609 1.00 59.45  ?  152 ALA A CB  1 
ATOM   1101 N  N   . GLN A 1 153 ? 55.842 75.904  16.640 1.00 58.50  ?  153 GLN A N   1 
ATOM   1102 C  CA  . GLN A 1 153 ? 56.945 76.325  15.782 1.00 63.03  ?  153 GLN A CA  1 
ATOM   1103 C  C   . GLN A 1 153 ? 57.821 77.381  16.461 1.00 61.96  ?  153 GLN A C   1 
ATOM   1104 O  O   . GLN A 1 153 ? 59.041 77.224  16.545 1.00 62.34  ?  153 GLN A O   1 
ATOM   1105 C  CB  . GLN A 1 153 ? 56.408 76.877  14.469 1.00 55.21  ?  153 GLN A CB  1 
ATOM   1106 C  CG  . GLN A 1 153 ? 57.472 77.338  13.506 1.00 47.67  ?  153 GLN A CG  1 
ATOM   1107 C  CD  . GLN A 1 153 ? 56.860 77.966  12.269 1.00 54.62  ?  153 GLN A CD  1 
ATOM   1108 O  OE1 . GLN A 1 153 ? 55.698 78.388  12.272 1.00 60.97  ?  153 GLN A OE1 1 
ATOM   1109 N  NE2 . GLN A 1 153 ? 57.632 78.018  11.198 1.00 58.51  ?  153 GLN A NE2 1 
ATOM   1110 N  N   . MET B 2 1   ? 19.099 87.482  38.045 1.00 112.07 ?  1   MET B N   1 
ATOM   1111 C  CA  . MET B 2 1   ? 20.311 87.416  37.231 1.00 116.65 ?  1   MET B CA  1 
ATOM   1112 C  C   . MET B 2 1   ? 19.986 87.161  35.757 1.00 104.83 ?  1   MET B C   1 
ATOM   1113 O  O   . MET B 2 1   ? 20.321 86.110  35.198 1.00 107.19 ?  1   MET B O   1 
ATOM   1114 C  CB  . MET B 2 1   ? 21.281 86.338  37.765 1.00 127.33 ?  1   MET B CB  1 
ATOM   1115 C  CG  . MET B 2 1   ? 20.677 84.962  38.089 1.00 132.18 ?  1   MET B CG  1 
ATOM   1116 S  SD  . MET B 2 1   ? 21.897 83.766  38.712 1.00 126.97 ?  1   MET B SD  1 
ATOM   1117 C  CE  . MET B 2 1   ? 21.739 83.982  40.488 1.00 120.70 ?  1   MET B CE  1 
ATOM   1118 N  N   . ALA B 2 2   ? 19.336 88.134  35.123 1.00 87.92  ?  2   ALA B N   1 
ATOM   1119 C  CA  . ALA B 2 2   ? 19.094 88.033  33.691 1.00 96.06  ?  2   ALA B CA  1 
ATOM   1120 C  C   . ALA B 2 2   ? 20.373 88.371  32.923 1.00 102.86 ?  2   ALA B C   1 
ATOM   1121 O  O   . ALA B 2 2   ? 21.178 87.481  32.614 1.00 103.33 ?  2   ALA B O   1 
ATOM   1122 C  CB  . ALA B 2 2   ? 17.933 88.946  33.281 1.00 95.17  ?  2   ALA B CB  1 
ATOM   1123 N  N   . GLN B 2 3   ? 20.552 89.654  32.606 1.00 98.52  ?  3   GLN B N   1 
ATOM   1124 C  CA  . GLN B 2 3   ? 21.767 90.221  32.034 1.00 78.71  ?  3   GLN B CA  1 
ATOM   1125 C  C   . GLN B 2 3   ? 22.272 91.287  32.993 1.00 65.59  ?  3   GLN B C   1 
ATOM   1126 O  O   . GLN B 2 3   ? 21.540 91.727  33.887 1.00 64.10  ?  3   GLN B O   1 
ATOM   1127 C  CB  . GLN B 2 3   ? 21.527 90.833  30.642 1.00 73.69  ?  3   GLN B CB  1 
ATOM   1128 C  CG  . GLN B 2 3   ? 20.324 91.778  30.545 1.00 90.71  ?  3   GLN B CG  1 
ATOM   1129 C  CD  . GLN B 2 3   ? 18.979 91.068  30.711 1.00 107.19 ?  3   GLN B CD  1 
ATOM   1130 O  OE1 . GLN B 2 3   ? 18.827 89.906  30.321 1.00 113.87 ?  3   GLN B OE1 1 
ATOM   1131 N  NE2 . GLN B 2 3   ? 18.005 91.760  31.310 1.00 108.53 ?  3   GLN B NE2 1 
ATOM   1132 N  N   . VAL B 2 4   ? 23.536 91.693  32.828 1.00 54.27  ?  4   VAL B N   1 
ATOM   1133 C  CA  . VAL B 2 4   ? 24.113 92.670  33.749 1.00 48.47  ?  4   VAL B CA  1 
ATOM   1134 C  C   . VAL B 2 4   ? 23.413 94.012  33.576 1.00 48.25  ?  4   VAL B C   1 
ATOM   1135 O  O   . VAL B 2 4   ? 23.123 94.444  32.448 1.00 53.46  ?  4   VAL B O   1 
ATOM   1136 C  CB  . VAL B 2 4   ? 25.630 92.804  33.537 1.00 49.97  ?  4   VAL B CB  1 
ATOM   1137 C  CG1 . VAL B 2 4   ? 26.194 93.867  34.451 1.00 40.13  ?  4   VAL B CG1 1 
ATOM   1138 C  CG2 . VAL B 2 4   ? 26.315 91.482  33.801 1.00 62.49  ?  4   VAL B CG2 1 
ATOM   1139 N  N   . GLN B 2 5   ? 23.112 94.669  34.707 1.00 42.22  ?  5   GLN B N   1 
ATOM   1140 C  CA  . GLN B 2 5   ? 22.453 95.973  34.721 1.00 40.72  ?  5   GLN B CA  1 
ATOM   1141 C  C   . GLN B 2 5   ? 23.098 96.884  35.760 1.00 38.72  ?  5   GLN B C   1 
ATOM   1142 O  O   . GLN B 2 5   ? 23.344 96.474  36.901 1.00 39.55  ?  5   GLN B O   1 
ATOM   1143 C  CB  . GLN B 2 5   ? 20.946 95.830  34.991 1.00 46.50  ?  5   GLN B CB  1 
ATOM   1144 C  CG  . GLN B 2 5   ? 20.155 95.422  33.747 1.00 59.67  ?  5   GLN B CG  1 
ATOM   1145 C  CD  . GLN B 2 5   ? 18.665 95.275  34.000 1.00 72.14  ?  5   GLN B CD  1 
ATOM   1146 O  OE1 . GLN B 2 5   ? 18.020 96.190  34.519 1.00 79.63  ?  5   GLN B OE1 1 
ATOM   1147 N  NE2 . GLN B 2 5   ? 18.108 94.117  33.625 1.00 73.79  ?  5   GLN B NE2 1 
ATOM   1148 N  N   . LEU B 2 6   ? 23.363 98.123  35.356 1.00 36.72  ?  6   LEU B N   1 
ATOM   1149 C  CA  . LEU B 2 6   ? 24.092 99.075  36.173 1.00 37.29  ?  6   LEU B CA  1 
ATOM   1150 C  C   . LEU B 2 6   ? 23.196 100.259 36.492 1.00 38.83  ?  6   LEU B C   1 
ATOM   1151 O  O   . LEU B 2 6   ? 22.434 100.723 35.638 1.00 39.40  ?  6   LEU B O   1 
ATOM   1152 C  CB  . LEU B 2 6   ? 25.343 99.553  35.455 1.00 34.62  ?  6   LEU B CB  1 
ATOM   1153 C  CG  . LEU B 2 6   ? 26.178 98.421  34.876 1.00 30.93  ?  6   LEU B CG  1 
ATOM   1154 C  CD1 . LEU B 2 6   ? 27.161 98.986  33.870 1.00 29.74  ?  6   LEU B CD1 1 
ATOM   1155 C  CD2 . LEU B 2 6   ? 26.905 97.649  35.986 1.00 28.42  ?  6   LEU B CD2 1 
ATOM   1156 N  N   . GLN B 2 7   ? 23.292 100.749 37.724 1.00 37.91  ?  7   GLN B N   1 
ATOM   1157 C  CA  . GLN B 2 7   ? 22.486 101.876 38.166 1.00 38.47  ?  7   GLN B CA  1 
ATOM   1158 C  C   . GLN B 2 7   ? 23.397 102.863 38.867 1.00 40.09  ?  7   GLN B C   1 
ATOM   1159 O  O   . GLN B 2 7   ? 24.033 102.516 39.868 1.00 42.62  ?  7   GLN B O   1 
ATOM   1160 C  CB  . GLN B 2 7   ? 21.365 101.439 39.104 1.00 41.32  ?  7   GLN B CB  1 
ATOM   1161 C  CG  . GLN B 2 7   ? 20.567 102.611 39.628 1.00 45.45  ?  7   GLN B CG  1 
ATOM   1162 C  CD  . GLN B 2 7   ? 19.783 103.278 38.527 1.00 48.18  ?  7   GLN B CD  1 
ATOM   1163 O  OE1 . GLN B 2 7   ? 18.944 102.645 37.886 1.00 54.83  ?  7   GLN B OE1 1 
ATOM   1164 N  NE2 . GLN B 2 7   ? 20.058 104.557 38.285 1.00 49.99  ?  7   GLN B NE2 1 
ATOM   1165 N  N   . GLU B 2 8   ? 23.470 104.077 38.333 1.00 34.24  ?  8   GLU B N   1 
ATOM   1166 C  CA  . GLU B 2 8   ? 24.245 105.120 38.974 1.00 41.06  ?  8   GLU B CA  1 
ATOM   1167 C  C   . GLU B 2 8   ? 23.364 105.897 39.942 1.00 43.97  ?  8   GLU B C   1 
ATOM   1168 O  O   . GLU B 2 8   ? 22.130 105.889 39.861 1.00 41.04  ?  8   GLU B O   1 
ATOM   1169 C  CB  . GLU B 2 8   ? 24.861 106.081 37.951 1.00 41.42  ?  8   GLU B CB  1 
ATOM   1170 C  CG  . GLU B 2 8   ? 25.725 105.433 36.888 1.00 48.38  ?  8   GLU B CG  1 
ATOM   1171 C  CD  . GLU B 2 8   ? 24.947 105.102 35.625 1.00 44.77  ?  8   GLU B CD  1 
ATOM   1172 O  OE1 . GLU B 2 8   ? 25.575 104.921 34.559 1.00 41.18  ?  8   GLU B OE1 1 
ATOM   1173 O  OE2 . GLU B 2 8   ? 23.705 105.039 35.699 1.00 40.77  -1 8   GLU B OE2 1 
ATOM   1174 N  N   . SER B 2 9   ? 24.025 106.582 40.863 1.00 37.77  ?  9   SER B N   1 
ATOM   1175 C  CA  . SER B 2 9   ? 23.336 107.424 41.819 1.00 44.04  ?  9   SER B CA  1 
ATOM   1176 C  C   . SER B 2 9   ? 24.346 108.423 42.354 1.00 48.38  ?  9   SER B C   1 
ATOM   1177 O  O   . SER B 2 9   ? 25.559 108.224 42.241 1.00 43.25  ?  9   SER B O   1 
ATOM   1178 C  CB  . SER B 2 9   ? 22.741 106.594 42.951 1.00 37.08  ?  9   SER B CB  1 
ATOM   1179 O  OG  . SER B 2 9   ? 23.789 105.950 43.645 1.00 48.67  ?  9   SER B OG  1 
ATOM   1180 N  N   . GLY B 2 10  ? 23.832 109.506 42.922 1.00 45.87  ?  10  GLY B N   1 
ATOM   1181 C  CA  . GLY B 2 10  ? 24.661 110.422 43.668 1.00 44.06  ?  10  GLY B CA  1 
ATOM   1182 C  C   . GLY B 2 10  ? 25.039 111.680 42.937 1.00 45.52  ?  10  GLY B C   1 
ATOM   1183 O  O   . GLY B 2 10  ? 25.750 112.515 43.508 1.00 44.57  ?  10  GLY B O   1 
ATOM   1184 N  N   . GLY B 2 11  ? 24.599 111.847 41.696 1.00 44.25  ?  11  GLY B N   1 
ATOM   1185 C  CA  . GLY B 2 11  ? 24.883 113.077 40.994 1.00 40.80  ?  11  GLY B CA  1 
ATOM   1186 C  C   . GLY B 2 11  ? 24.060 114.230 41.537 1.00 43.01  ?  11  GLY B C   1 
ATOM   1187 O  O   . GLY B 2 11  ? 22.964 114.061 42.076 1.00 47.10  ?  11  GLY B O   1 
ATOM   1188 N  N   . GLY B 2 12  ? 24.595 115.428 41.385 1.00 40.28  ?  12  GLY B N   1 
ATOM   1189 C  CA  . GLY B 2 12  ? 23.862 116.584 41.853 1.00 45.01  ?  12  GLY B CA  1 
ATOM   1190 C  C   . GLY B 2 12  ? 24.477 117.872 41.371 1.00 42.25  ?  12  GLY B C   1 
ATOM   1191 O  O   . GLY B 2 12  ? 25.037 117.918 40.266 1.00 47.95  ?  12  GLY B O   1 
ATOM   1192 N  N   . SER B 2 13  ? 24.373 118.918 42.195 1.00 39.96  ?  13  SER B N   1 
ATOM   1193 C  CA  . SER B 2 13  ? 24.913 120.237 41.889 1.00 50.13  ?  13  SER B CA  1 
ATOM   1194 C  C   . SER B 2 13  ? 25.824 120.677 43.028 1.00 48.84  ?  13  SER B C   1 
ATOM   1195 O  O   . SER B 2 13  ? 25.468 120.543 44.207 1.00 51.71  ?  13  SER B O   1 
ATOM   1196 C  CB  . SER B 2 13  ? 23.784 121.252 41.661 1.00 55.96  ?  13  SER B CB  1 
ATOM   1197 O  OG  . SER B 2 13  ? 22.866 120.776 40.676 1.00 65.63  ?  13  SER B OG  1 
ATOM   1198 N  N   . VAL B 2 14  ? 27.004 121.184 42.673 1.00 39.75  ?  14  VAL B N   1 
ATOM   1199 C  CA  . VAL B 2 14  ? 28.007 121.587 43.654 1.00 45.49  ?  14  VAL B CA  1 
ATOM   1200 C  C   . VAL B 2 14  ? 28.791 122.750 43.061 1.00 46.65  ?  14  VAL B C   1 
ATOM   1201 O  O   . VAL B 2 14  ? 28.913 122.880 41.839 1.00 52.97  ?  14  VAL B O   1 
ATOM   1202 C  CB  . VAL B 2 14  ? 28.934 120.401 44.032 1.00 44.48  ?  14  VAL B CB  1 
ATOM   1203 C  CG1 . VAL B 2 14  ? 29.759 119.992 42.827 1.00 53.85  ?  14  VAL B CG1 1 
ATOM   1204 C  CG2 . VAL B 2 14  ? 29.846 120.747 45.215 1.00 33.82  ?  14  VAL B CG2 1 
ATOM   1205 N  N   . GLN B 2 15  ? 29.304 123.614 43.931 1.00 44.94  ?  15  GLN B N   1 
ATOM   1206 C  CA  . GLN B 2 15  ? 30.121 124.726 43.468 1.00 49.74  ?  15  GLN B CA  1 
ATOM   1207 C  C   . GLN B 2 15  ? 31.561 124.279 43.250 1.00 50.82  ?  15  GLN B C   1 
ATOM   1208 O  O   . GLN B 2 15  ? 32.048 123.347 43.900 1.00 51.59  ?  15  GLN B O   1 
ATOM   1209 C  CB  . GLN B 2 15  ? 30.081 125.880 44.466 1.00 58.80  ?  15  GLN B CB  1 
ATOM   1210 C  CG  . GLN B 2 15  ? 30.724 127.144 43.936 1.00 66.09  ?  15  GLN B CG  1 
ATOM   1211 C  CD  . GLN B 2 15  ? 30.792 128.240 44.965 1.00 69.98  ?  15  GLN B CD  1 
ATOM   1212 O  OE1 . GLN B 2 15  ? 31.581 128.177 45.915 1.00 73.73  ?  15  GLN B OE1 1 
ATOM   1213 N  NE2 . GLN B 2 15  ? 29.973 129.266 44.779 1.00 76.10  ?  15  GLN B NE2 1 
ATOM   1214 N  N   . ALA B 2 16  ? 32.234 124.949 42.312 1.00 51.67  ?  16  ALA B N   1 
ATOM   1215 C  CA  . ALA B 2 16  ? 33.631 124.661 42.005 1.00 42.27  ?  16  ALA B CA  1 
ATOM   1216 C  C   . ALA B 2 16  ? 34.467 124.574 43.274 1.00 42.31  ?  16  ALA B C   1 
ATOM   1217 O  O   . ALA B 2 16  ? 34.274 125.342 44.224 1.00 43.04  ?  16  ALA B O   1 
ATOM   1218 C  CB  . ALA B 2 16  ? 34.196 125.739 41.080 1.00 30.83  ?  16  ALA B CB  1 
ATOM   1219 N  N   . GLY B 2 17  ? 35.400 123.621 43.281 1.00 38.85  ?  17  GLY B N   1 
ATOM   1220 C  CA  . GLY B 2 17  ? 36.177 123.289 44.451 1.00 35.78  ?  17  GLY B CA  1 
ATOM   1221 C  C   . GLY B 2 17  ? 35.542 122.262 45.368 1.00 36.57  ?  17  GLY B C   1 
ATOM   1222 O  O   . GLY B 2 17  ? 36.244 121.685 46.208 1.00 39.88  ?  17  GLY B O   1 
ATOM   1223 N  N   . GLY B 2 18  ? 34.248 122.000 45.215 1.00 40.91  ?  18  GLY B N   1 
ATOM   1224 C  CA  . GLY B 2 18  ? 33.537 121.066 46.062 1.00 45.69  ?  18  GLY B CA  1 
ATOM   1225 C  C   . GLY B 2 18  ? 33.831 119.614 45.722 1.00 43.98  ?  18  GLY B C   1 
ATOM   1226 O  O   . GLY B 2 18  ? 34.653 119.283 44.868 1.00 42.11  ?  18  GLY B O   1 
ATOM   1227 N  N   . SER B 2 19  ? 33.129 118.727 46.437 1.00 45.63  ?  19  SER B N   1 
ATOM   1228 C  CA  . SER B 2 19  ? 33.264 117.285 46.293 1.00 40.25  ?  19  SER B CA  1 
ATOM   1229 C  C   . SER B 2 19  ? 31.917 116.657 45.963 1.00 42.93  ?  19  SER B C   1 
ATOM   1230 O  O   . SER B 2 19  ? 30.857 117.282 46.080 1.00 46.07  ?  19  SER B O   1 
ATOM   1231 C  CB  . SER B 2 19  ? 33.814 116.633 47.561 1.00 28.36  ?  19  SER B CB  1 
ATOM   1232 O  OG  . SER B 2 19  ? 34.914 117.371 48.038 1.00 59.06  ?  19  SER B OG  1 
ATOM   1233 N  N   . LEU B 2 20  ? 31.993 115.391 45.562 1.00 34.97  ?  20  LEU B N   1 
ATOM   1234 C  CA  . LEU B 2 20  ? 30.853 114.572 45.178 1.00 37.70  ?  20  LEU B CA  1 
ATOM   1235 C  C   . LEU B 2 20  ? 31.302 113.123 45.196 1.00 42.87  ?  20  LEU B C   1 
ATOM   1236 O  O   . LEU B 2 20  ? 32.462 112.813 44.898 1.00 49.39  ?  20  LEU B O   1 
ATOM   1237 C  CB  . LEU B 2 20  ? 30.335 114.929 43.785 1.00 36.54  ?  20  LEU B CB  1 
ATOM   1238 C  CG  . LEU B 2 20  ? 28.984 115.597 43.715 1.00 49.68  ?  20  LEU B CG  1 
ATOM   1239 C  CD1 . LEU B 2 20  ? 28.684 115.989 42.271 1.00 46.05  ?  20  LEU B CD1 1 
ATOM   1240 C  CD2 . LEU B 2 20  ? 27.958 114.626 44.267 1.00 56.37  ?  20  LEU B CD2 1 
ATOM   1241 N  N   . ARG B 2 21  ? 30.383 112.239 45.561 1.00 37.13  ?  21  ARG B N   1 
ATOM   1242 C  CA  . ARG B 2 21  ? 30.624 110.808 45.472 1.00 36.33  ?  21  ARG B CA  1 
ATOM   1243 C  C   . ARG B 2 21  ? 29.504 110.211 44.641 1.00 44.32  ?  21  ARG B C   1 
ATOM   1244 O  O   . ARG B 2 21  ? 28.326 110.487 44.902 1.00 46.53  ?  21  ARG B O   1 
ATOM   1245 C  CB  . ARG B 2 21  ? 30.671 110.148 46.848 1.00 29.49  ?  21  ARG B CB  1 
ATOM   1246 C  CG  . ARG B 2 21  ? 31.383 108.810 46.870 1.00 29.44  ?  21  ARG B CG  1 
ATOM   1247 C  CD  . ARG B 2 21  ? 31.051 108.055 48.138 1.00 39.39  ?  21  ARG B CD  1 
ATOM   1248 N  NE  . ARG B 2 21  ? 32.156 107.197 48.562 1.00 70.60  ?  21  ARG B NE  1 
ATOM   1249 C  CZ  . ARG B 2 21  ? 32.048 106.187 49.431 1.00 80.54  ?  21  ARG B CZ  1 
ATOM   1250 N  NH1 . ARG B 2 21  ? 30.865 105.900 49.986 1.00 82.28  1  21  ARG B NH1 1 
ATOM   1251 N  NH2 . ARG B 2 21  ? 33.127 105.458 49.742 1.00 65.62  ?  21  ARG B NH2 1 
ATOM   1252 N  N   . LEU B 2 22  ? 29.874 109.435 43.618 1.00 33.05  ?  22  LEU B N   1 
ATOM   1253 C  CA  . LEU B 2 22  ? 28.912 108.702 42.815 1.00 27.35  ?  22  LEU B CA  1 
ATOM   1254 C  C   . LEU B 2 22  ? 29.059 107.223 43.102 1.00 27.53  ?  22  LEU B C   1 
ATOM   1255 O  O   . LEU B 2 22  ? 30.147 106.751 43.435 1.00 31.88  ?  22  LEU B O   1 
ATOM   1256 C  CB  . LEU B 2 22  ? 29.082 108.937 41.309 1.00 34.01  ?  22  LEU B CB  1 
ATOM   1257 C  CG  . LEU B 2 22  ? 29.283 110.327 40.736 1.00 38.16  ?  22  LEU B CG  1 
ATOM   1258 C  CD1 . LEU B 2 22  ? 29.453 110.232 39.233 1.00 42.81  ?  22  LEU B CD1 1 
ATOM   1259 C  CD2 . LEU B 2 22  ? 28.113 111.234 41.089 1.00 36.76  ?  22  LEU B CD2 1 
ATOM   1260 N  N   . ALA B 2 23  ? 27.955 106.495 42.951 1.00 29.45  ?  23  ALA B N   1 
ATOM   1261 C  CA  . ALA B 2 23  ? 27.948 105.062 43.167 1.00 28.64  ?  23  ALA B CA  1 
ATOM   1262 C  C   . ALA B 2 23  ? 27.311 104.374 41.981 1.00 36.36  ?  23  ALA B C   1 
ATOM   1263 O  O   . ALA B 2 23  ? 26.364 104.893 41.384 1.00 45.03  ?  23  ALA B O   1 
ATOM   1264 C  CB  . ALA B 2 23  ? 27.186 104.687 44.423 1.00 32.80  ?  23  ALA B CB  1 
ATOM   1265 N  N   . CYS B 2 24  ? 27.827 103.198 41.654 1.00 40.07  ?  24  CYS B N   1 
ATOM   1266 C  CA  . CYS B 2 24  ? 27.295 102.397 40.561 1.00 42.99  ?  24  CYS B CA  1 
ATOM   1267 C  C   . CYS B 2 24  ? 27.064 100.987 41.068 1.00 39.09  ?  24  CYS B C   1 
ATOM   1268 O  O   . CYS B 2 24  ? 28.025 100.277 41.383 1.00 40.51  ?  24  CYS B O   1 
ATOM   1269 C  CB  . CYS B 2 24  ? 28.249 102.379 39.382 1.00 49.06  ?  24  CYS B CB  1 
ATOM   1270 S  SG  . CYS B 2 24  ? 27.803 101.126 38.214 1.00 50.37  ?  24  CYS B SG  1 
ATOM   1271 N  N   . VAL B 2 25  ? 25.799 100.580 41.120 1.00 35.09  ?  25  VAL B N   1 
ATOM   1272 C  CA  . VAL B 2 25  ? 25.414 99.269  41.618 1.00 33.38  ?  25  VAL B CA  1 
ATOM   1273 C  C   . VAL B 2 25  ? 25.168 98.337  40.446 1.00 38.29  ?  25  VAL B C   1 
ATOM   1274 O  O   . VAL B 2 25  ? 24.419 98.678  39.519 1.00 38.29  ?  25  VAL B O   1 
ATOM   1275 C  CB  . VAL B 2 25  ? 24.164 99.361  42.497 1.00 35.50  ?  25  VAL B CB  1 
ATOM   1276 C  CG1 . VAL B 2 25  ? 23.774 97.969  42.923 1.00 39.27  ?  25  VAL B CG1 1 
ATOM   1277 C  CG2 . VAL B 2 25  ? 24.452 100.257 43.698 1.00 36.93  ?  25  VAL B CG2 1 
ATOM   1278 N  N   . ALA B 2 26  ? 25.778 97.156  40.488 1.00 30.14  ?  26  ALA B N   1 
ATOM   1279 C  CA  . ALA B 2 26  ? 25.588 96.153  39.451 1.00 35.82  ?  26  ALA B CA  1 
ATOM   1280 C  C   . ALA B 2 26  ? 24.660 95.053  39.950 1.00 39.55  ?  26  ALA B C   1 
ATOM   1281 O  O   . ALA B 2 26  ? 24.776 94.602  41.093 1.00 45.03  ?  26  ALA B O   1 
ATOM   1282 C  CB  . ALA B 2 26  ? 26.930 95.562  39.030 1.00 42.34  ?  26  ALA B CB  1 
ATOM   1283 N  N   . SER B 2 27  ? 23.731 94.629  39.093 1.00 44.47  ?  27  SER B N   1 
ATOM   1284 C  CA  . SER B 2 27  ? 22.798 93.562  39.438 1.00 47.82  ?  27  SER B CA  1 
ATOM   1285 C  C   . SER B 2 27  ? 22.664 92.611  38.260 1.00 53.21  ?  27  SER B C   1 
ATOM   1286 O  O   . SER B 2 27  ? 22.878 92.985  37.104 1.00 51.23  ?  27  SER B O   1 
ATOM   1287 C  CB  . SER B 2 27  ? 21.410 94.096  39.798 1.00 45.56  ?  27  SER B CB  1 
ATOM   1288 O  OG  . SER B 2 27  ? 20.866 94.809  38.700 1.00 52.01  ?  27  SER B OG  1 
ATOM   1289 N  N   . GLY B 2 28  ? 22.290 91.373  38.562 1.00 54.55  ?  28  GLY B N   1 
ATOM   1290 C  CA  . GLY B 2 28  ? 22.038 90.443  37.485 1.00 37.98  ?  28  GLY B CA  1 
ATOM   1291 C  C   . GLY B 2 28  ? 23.304 89.918  36.817 1.00 44.53  ?  28  GLY B C   1 
ATOM   1292 O  O   . GLY B 2 28  ? 24.430 90.107  37.279 1.00 48.65  ?  28  GLY B O   1 
ATOM   1293 N  N   . GLY B 2 29  ? 23.083 89.236  35.689 1.00 43.96  ?  29  GLY B N   1 
ATOM   1294 C  CA  . GLY B 2 29  ? 24.160 88.632  34.930 1.00 40.32  ?  29  GLY B CA  1 
ATOM   1295 C  C   . GLY B 2 29  ? 24.658 87.336  35.550 1.00 46.28  ?  29  GLY B C   1 
ATOM   1296 O  O   . GLY B 2 29  ? 24.136 86.830  36.554 1.00 41.24  ?  29  GLY B O   1 
ATOM   1297 N  N   . ASP B 2 30  ? 25.704 86.789  34.930 1.00 42.28  ?  30  ASP B N   1 
ATOM   1298 C  CA  . ASP B 2 30  ? 26.364 85.615  35.486 1.00 34.96  ?  30  ASP B CA  1 
ATOM   1299 C  C   . ASP B 2 30  ? 26.969 85.970  36.835 1.00 45.97  ?  30  ASP B C   1 
ATOM   1300 O  O   . ASP B 2 30  ? 27.893 86.787  36.918 1.00 49.65  ?  30  ASP B O   1 
ATOM   1301 C  CB  . ASP B 2 30  ? 27.440 85.124  34.526 1.00 35.45  ?  30  ASP B CB  1 
ATOM   1302 C  CG  . ASP B 2 30  ? 28.058 83.803  34.951 1.00 45.53  ?  30  ASP B CG  1 
ATOM   1303 O  OD1 . ASP B 2 30  ? 27.920 83.385  36.129 1.00 48.74  ?  30  ASP B OD1 1 
ATOM   1304 O  OD2 . ASP B 2 30  ? 28.679 83.168  34.074 1.00 47.63  -1 30  ASP B OD2 1 
ATOM   1305 N  N   . THR B 2 31  ? 26.450 85.357  37.893 1.00 52.00  ?  31  THR B N   1 
ATOM   1306 C  CA  . THR B 2 31  ? 26.847 85.720  39.245 1.00 53.45  ?  31  THR B CA  1 
ATOM   1307 C  C   . THR B 2 31  ? 27.909 84.794  39.831 1.00 51.70  ?  31  THR B C   1 
ATOM   1308 O  O   . THR B 2 31  ? 28.244 84.925  41.014 1.00 51.00  ?  31  THR B O   1 
ATOM   1309 C  CB  . THR B 2 31  ? 25.613 85.766  40.147 1.00 52.97  ?  31  THR B CB  1 
ATOM   1310 O  OG1 . THR B 2 31  ? 24.828 84.583  39.942 1.00 62.15  ?  31  THR B OG1 1 
ATOM   1311 C  CG2 . THR B 2 31  ? 24.771 86.995  39.799 1.00 49.76  ?  31  THR B CG2 1 
ATOM   1312 N  N   . ARG B 2 32  ? 28.461 83.884  39.034 1.00 50.48  ?  32  ARG B N   1 
ATOM   1313 C  CA  . ARG B 2 32  ? 29.592 83.094  39.500 1.00 48.42  ?  32  ARG B CA  1 
ATOM   1314 C  C   . ARG B 2 32  ? 30.733 84.025  39.900 1.00 50.56  ?  32  ARG B C   1 
ATOM   1315 O  O   . ARG B 2 32  ? 30.962 85.046  39.242 1.00 57.58  ?  32  ARG B O   1 
ATOM   1316 C  CB  . ARG B 2 32  ? 30.042 82.114  38.412 1.00 39.96  ?  32  ARG B CB  1 
ATOM   1317 C  CG  . ARG B 2 32  ? 28.938 81.159  37.978 1.00 32.40  ?  32  ARG B CG  1 
ATOM   1318 C  CD  . ARG B 2 32  ? 29.418 80.164  36.942 1.00 41.45  ?  32  ARG B CD  1 
ATOM   1319 N  NE  . ARG B 2 32  ? 29.536 80.747  35.606 1.00 61.35  ?  32  ARG B NE  1 
ATOM   1320 C  CZ  . ARG B 2 32  ? 30.208 80.189  34.594 1.00 66.67  ?  32  ARG B CZ  1 
ATOM   1321 N  NH1 . ARG B 2 32  ? 30.845 79.040  34.768 1.00 68.33  1  32  ARG B NH1 1 
ATOM   1322 N  NH2 . ARG B 2 32  ? 30.261 80.787  33.405 1.00 60.36  ?  32  ARG B NH2 1 
ATOM   1323 N  N   . PRO B 2 33  ? 31.463 83.722  40.975 1.00 52.91  ?  33  PRO B N   1 
ATOM   1324 C  CA  . PRO B 2 33  ? 32.374 84.726  41.558 1.00 46.69  ?  33  PRO B CA  1 
ATOM   1325 C  C   . PRO B 2 33  ? 33.652 84.962  40.764 1.00 46.51  ?  33  PRO B C   1 
ATOM   1326 O  O   . PRO B 2 33  ? 34.349 85.951  41.033 1.00 48.11  ?  33  PRO B O   1 
ATOM   1327 C  CB  . PRO B 2 33  ? 32.688 84.146  42.939 1.00 45.84  ?  33  PRO B CB  1 
ATOM   1328 C  CG  . PRO B 2 33  ? 32.602 82.669  42.723 1.00 55.54  ?  33  PRO B CG  1 
ATOM   1329 C  CD  . PRO B 2 33  ? 31.516 82.440  41.696 1.00 56.53  ?  33  PRO B CD  1 
ATOM   1330 N  N   . TYR B 2 34  ? 33.996 84.104  39.808 1.00 45.45  ?  34  TYR B N   1 
ATOM   1331 C  CA  . TYR B 2 34  ? 35.188 84.334  39.007 1.00 39.15  ?  34  TYR B CA  1 
ATOM   1332 C  C   . TYR B 2 34  ? 34.925 85.169  37.751 1.00 43.08  ?  34  TYR B C   1 
ATOM   1333 O  O   . TYR B 2 34  ? 35.855 85.363  36.956 1.00 45.28  ?  34  TYR B O   1 
ATOM   1334 C  CB  . TYR B 2 34  ? 35.828 83.002  38.642 1.00 34.66  ?  34  TYR B CB  1 
ATOM   1335 C  CG  . TYR B 2 34  ? 34.859 81.937  38.206 1.00 44.34  ?  34  TYR B CG  1 
ATOM   1336 C  CD1 . TYR B 2 34  ? 34.503 81.800  36.868 1.00 47.04  ?  34  TYR B CD1 1 
ATOM   1337 C  CD2 . TYR B 2 34  ? 34.311 81.051  39.129 1.00 57.00  ?  34  TYR B CD2 1 
ATOM   1338 C  CE1 . TYR B 2 34  ? 33.633 80.812  36.455 1.00 53.56  ?  34  TYR B CE1 1 
ATOM   1339 C  CE2 . TYR B 2 34  ? 33.431 80.059  38.728 1.00 61.60  ?  34  TYR B CE2 1 
ATOM   1340 C  CZ  . TYR B 2 34  ? 33.099 79.944  37.389 1.00 63.14  ?  34  TYR B CZ  1 
ATOM   1341 O  OH  . TYR B 2 34  ? 32.235 78.953  36.982 1.00 69.77  ?  34  TYR B OH  1 
ATOM   1342 N  N   . ILE B 2 35  ? 33.702 85.679  37.574 1.00 32.97  ?  35  ILE B N   1 
ATOM   1343 C  CA  . ILE B 2 35  ? 33.324 86.552  36.455 1.00 31.84  ?  35  ILE B CA  1 
ATOM   1344 C  C   . ILE B 2 35  ? 33.779 87.974  36.774 1.00 32.99  ?  35  ILE B C   1 
ATOM   1345 O  O   . ILE B 2 35  ? 33.112 88.688  37.520 1.00 40.03  ?  35  ILE B O   1 
ATOM   1346 C  CB  . ILE B 2 35  ? 31.818 86.514  36.182 1.00 35.58  ?  35  ILE B CB  1 
ATOM   1347 C  CG1 . ILE B 2 35  ? 31.326 85.082  35.927 1.00 31.01  ?  35  ILE B CG1 1 
ATOM   1348 C  CG2 . ILE B 2 35  ? 31.465 87.448  35.038 1.00 36.46  ?  35  ILE B CG2 1 
ATOM   1349 C  CD1 . ILE B 2 35  ? 32.174 84.299  34.958 1.00 30.31  ?  35  ILE B CD1 1 
ATOM   1350 N  N   . THR B 2 36  ? 34.880 88.412  36.169 1.00 34.70  ?  36  THR B N   1 
ATOM   1351 C  CA  . THR B 2 36  ? 35.508 89.685  36.483 1.00 26.74  ?  36  THR B CA  1 
ATOM   1352 C  C   . THR B 2 36  ? 35.198 90.740  35.424 1.00 28.42  ?  36  THR B C   1 
ATOM   1353 O  O   . THR B 2 36  ? 34.982 90.428  34.247 1.00 38.90  ?  36  THR B O   1 
ATOM   1354 C  CB  . THR B 2 36  ? 37.019 89.495  36.611 1.00 35.43  ?  36  THR B CB  1 
ATOM   1355 O  OG1 . THR B 2 36  ? 37.527 88.910  35.402 1.00 34.38  ?  36  THR B OG1 1 
ATOM   1356 C  CG2 . THR B 2 36  ? 37.342 88.575  37.812 1.00 29.12  ?  36  THR B CG2 1 
ATOM   1357 N  N   . TYR B 2 37  ? 35.176 92.002  35.853 1.00 26.35  ?  37  TYR B N   1 
ATOM   1358 C  CA  . TYR B 2 37  ? 34.912 93.122  34.958 1.00 22.75  ?  37  TYR B CA  1 
ATOM   1359 C  C   . TYR B 2 37  ? 35.937 94.222  35.180 1.00 22.29  ?  37  TYR B C   1 
ATOM   1360 O  O   . TYR B 2 37  ? 36.531 94.338  36.252 1.00 25.88  ?  37  TYR B O   1 
ATOM   1361 C  CB  . TYR B 2 37  ? 33.517 93.729  35.151 1.00 18.28  ?  37  TYR B CB  1 
ATOM   1362 C  CG  . TYR B 2 37  ? 32.365 92.745  35.120 1.00 25.43  ?  37  TYR B CG  1 
ATOM   1363 C  CD1 . TYR B 2 37  ? 31.674 92.475  33.937 1.00 27.73  ?  37  TYR B CD1 1 
ATOM   1364 C  CD2 . TYR B 2 37  ? 31.927 92.119  36.292 1.00 29.69  ?  37  TYR B CD2 1 
ATOM   1365 C  CE1 . TYR B 2 37  ? 30.585 91.582  33.920 1.00 30.91  ?  37  TYR B CE1 1 
ATOM   1366 C  CE2 . TYR B 2 37  ? 30.848 91.227  36.288 1.00 33.43  ?  37  TYR B CE2 1 
ATOM   1367 C  CZ  . TYR B 2 37  ? 30.180 90.959  35.103 1.00 34.19  ?  37  TYR B CZ  1 
ATOM   1368 O  OH  . TYR B 2 37  ? 29.112 90.070  35.110 1.00 38.57  ?  37  TYR B OH  1 
ATOM   1369 N  N   . TRP B 2 38  ? 36.163 95.009  34.137 1.00 26.35  ?  38  TRP B N   1 
ATOM   1370 C  CA  . TRP B 2 38  ? 36.713 96.343  34.291 1.00 21.78  ?  38  TRP B CA  1 
ATOM   1371 C  C   . TRP B 2 38  ? 35.516 97.259  34.389 1.00 26.80  ?  38  TRP B C   1 
ATOM   1372 O  O   . TRP B 2 38  ? 34.775 97.437  33.416 1.00 27.84  ?  38  TRP B O   1 
ATOM   1373 C  CB  . TRP B 2 38  ? 37.639 96.715  33.141 1.00 21.54  ?  38  TRP B CB  1 
ATOM   1374 C  CG  . TRP B 2 38  ? 38.896 95.957  33.281 1.00 24.85  ?  38  TRP B CG  1 
ATOM   1375 C  CD1 . TRP B 2 38  ? 39.180 94.728  32.750 1.00 23.43  ?  38  TRP B CD1 1 
ATOM   1376 C  CD2 . TRP B 2 38  ? 40.023 96.323  34.076 1.00 25.45  ?  38  TRP B CD2 1 
ATOM   1377 N  NE1 . TRP B 2 38  ? 40.436 94.318  33.153 1.00 23.32  ?  38  TRP B NE1 1 
ATOM   1378 C  CE2 . TRP B 2 38  ? 40.971 95.279  33.970 1.00 27.16  ?  38  TRP B CE2 1 
ATOM   1379 C  CE3 . TRP B 2 38  ? 40.321 97.426  34.880 1.00 31.36  ?  38  TRP B CE3 1 
ATOM   1380 C  CZ2 . TRP B 2 38  ? 42.201 95.320  34.622 1.00 28.15  ?  38  TRP B CZ2 1 
ATOM   1381 C  CZ3 . TRP B 2 38  ? 41.541 97.461  35.529 1.00 27.90  ?  38  TRP B CZ3 1 
ATOM   1382 C  CH2 . TRP B 2 38  ? 42.465 96.416  35.396 1.00 25.78  ?  38  TRP B CH2 1 
ATOM   1383 N  N   . MET B 2 39  ? 35.284 97.767  35.587 1.00 30.66  ?  39  MET B N   1 
ATOM   1384 C  CA  . MET B 2 39  ? 34.103 98.555  35.877 1.00 24.19  ?  39  MET B CA  1 
ATOM   1385 C  C   . MET B 2 39  ? 34.559 100.011 35.902 1.00 27.08  ?  39  MET B C   1 
ATOM   1386 O  O   . MET B 2 39  ? 35.508 100.359 36.618 1.00 31.91  ?  39  MET B O   1 
ATOM   1387 C  CB  . MET B 2 39  ? 33.470 98.061  37.183 1.00 27.40  ?  39  MET B CB  1 
ATOM   1388 C  CG  . MET B 2 39  ? 32.132 98.661  37.447 1.00 35.36  ?  39  MET B CG  1 
ATOM   1389 S  SD  . MET B 2 39  ? 30.824 97.795  36.570 1.00 42.31  ?  39  MET B SD  1 
ATOM   1390 C  CE  . MET B 2 39  ? 31.191 96.089  36.978 1.00 30.24  ?  39  MET B CE  1 
ATOM   1391 N  N   . GLY B 2 40  ? 33.964 100.832 35.039 1.00 27.67  ?  40  GLY B N   1 
ATOM   1392 C  CA  . GLY B 2 40  ? 34.092 101.203 35.821 1.00 19.16  ?  40  GLY B CA  1 
ATOM   1393 C  C   . GLY B 2 40  ? 33.515 103.250 34.768 1.00 28.44  ?  40  GLY B C   1 
ATOM   1394 O  O   . GLY B 2 40  ? 32.330 103.049 34.519 1.00 32.26  ?  40  GLY B O   1 
ATOM   1395 N  N   . TRP B 2 41  ? 34.020 104.443 35.096 1.00 33.14  ?  41  TRP B N   1 
ATOM   1396 C  CA  . TRP B 2 41  ? 33.238 105.678 35.079 1.00 31.07  ?  41  TRP B CA  1 
ATOM   1397 C  C   . TRP B 2 41  ? 33.581 106.496 33.838 1.00 34.25  ?  41  TRP B C   1 
ATOM   1398 O  O   . TRP B 2 41  ? 34.765 106.704 33.535 1.00 30.35  ?  41  TRP B O   1 
ATOM   1399 C  CB  . TRP B 2 41  ? 33.498 106.494 36.345 1.00 24.37  ?  41  TRP B CB  1 
ATOM   1400 C  CG  . TRP B 2 41  ? 32.690 105.973 37.482 1.00 28.89  ?  41  TRP B CG  1 
ATOM   1401 C  CD1 . TRP B 2 41  ? 33.115 105.143 38.483 1.00 24.79  ?  41  TRP B CD1 1 
ATOM   1402 C  CD2 . TRP B 2 41  ? 31.289 106.203 37.717 1.00 29.48  ?  41  TRP B CD2 1 
ATOM   1403 N  NE1 . TRP B 2 41  ? 32.065 104.849 39.337 1.00 30.26  ?  41  TRP B NE1 1 
ATOM   1404 C  CE2 . TRP B 2 41  ? 30.937 105.492 38.890 1.00 30.53  ?  41  TRP B CE2 1 
ATOM   1405 C  CE3 . TRP B 2 41  ? 30.301 106.940 37.054 1.00 29.01  ?  41  TRP B CE3 1 
ATOM   1406 C  CZ2 . TRP B 2 41  ? 29.645 105.506 39.416 1.00 32.92  ?  41  TRP B CZ2 1 
ATOM   1407 C  CZ3 . TRP B 2 41  ? 29.011 106.956 37.576 1.00 32.60  ?  41  TRP B CZ3 1 
ATOM   1408 C  CH2 . TRP B 2 41  ? 28.696 106.244 38.749 1.00 33.37  ?  41  TRP B CH2 1 
ATOM   1409 N  N   . TYR B 2 42  ? 32.541 106.951 33.125 1.00 32.16  ?  42  TYR B N   1 
ATOM   1410 C  CA  . TYR B 2 42  ? 32.666 107.689 31.871 1.00 27.94  ?  42  TYR B CA  1 
ATOM   1411 C  C   . TYR B 2 42  ? 31.865 108.982 31.956 1.00 28.91  ?  42  TYR B C   1 
ATOM   1412 O  O   . TYR B 2 42  ? 30.933 109.095 32.753 1.00 32.82  ?  42  TYR B O   1 
ATOM   1413 C  CB  . TYR B 2 42  ? 32.177 106.850 30.670 1.00 32.82  ?  42  TYR B CB  1 
ATOM   1414 C  CG  . TYR B 2 42  ? 33.025 105.632 30.431 1.00 32.58  ?  42  TYR B CG  1 
ATOM   1415 C  CD1 . TYR B 2 42  ? 32.868 104.493 31.201 1.00 34.25  ?  42  TYR B CD1 1 
ATOM   1416 C  CD2 . TYR B 2 42  ? 33.996 105.627 29.447 1.00 38.41  ?  42  TYR B CD2 1 
ATOM   1417 C  CE1 . TYR B 2 42  ? 33.661 103.385 31.002 1.00 31.02  ?  42  TYR B CE1 1 
ATOM   1418 C  CE2 . TYR B 2 42  ? 34.800 104.531 29.245 1.00 20.99  ?  42  TYR B CE2 1 
ATOM   1419 C  CZ  . TYR B 2 42  ? 34.630 103.413 30.021 1.00 32.97  ?  42  TYR B CZ  1 
ATOM   1420 O  OH  . TYR B 2 42  ? 35.430 102.303 29.809 1.00 36.72  ?  42  TYR B OH  1 
ATOM   1421 N  N   . ARG B 2 43  ? 32.234 109.957 31.111 1.00 40.44  ?  43  ARG B N   1 
ATOM   1422 C  CA  . ARG B 2 43  ? 31.592 111.268 31.017 1.00 39.41  ?  43  ARG B CA  1 
ATOM   1423 C  C   . ARG B 2 43  ? 31.107 111.531 29.608 1.00 46.24  ?  43  ARG B C   1 
ATOM   1424 O  O   . ARG B 2 43  ? 31.711 111.067 28.635 1.00 55.06  ?  43  ARG B O   1 
ATOM   1425 C  CB  . ARG B 2 43  ? 32.540 112.431 31.338 1.00 38.77  ?  43  ARG B CB  1 
ATOM   1426 C  CG  . ARG B 2 43  ? 32.898 112.564 32.759 1.00 46.46  ?  43  ARG B CG  1 
ATOM   1427 C  CD  . ARG B 2 43  ? 33.611 113.885 33.051 1.00 41.63  ?  43  ARG B CD  1 
ATOM   1428 N  NE  . ARG B 2 43  ? 34.897 114.096 32.406 1.00 31.98  ?  43  ARG B NE  1 
ATOM   1429 C  CZ  . ARG B 2 43  ? 35.808 114.890 32.963 1.00 34.34  ?  43  ARG B CZ  1 
ATOM   1430 N  NH1 . ARG B 2 43  ? 35.526 115.455 34.140 1.00 36.11  1  43  ARG B NH1 1 
ATOM   1431 N  NH2 . ARG B 2 43  ? 36.996 115.116 32.395 1.00 41.96  ?  43  ARG B NH2 1 
ATOM   1432 N  N   . GLN B 2 44  ? 30.049 112.335 29.505 1.00 41.89  ?  44  GLN B N   1 
ATOM   1433 C  CA  . GLN B 2 44  ? 29.706 112.987 28.244 1.00 53.67  ?  44  GLN B CA  1 
ATOM   1434 C  C   . GLN B 2 44  ? 29.263 114.411 28.546 1.00 56.94  ?  44  GLN B C   1 
ATOM   1435 O  O   . GLN B 2 44  ? 28.199 114.629 29.143 1.00 52.46  ?  44  GLN B O   1 
ATOM   1436 C  CB  . GLN B 2 44  ? 28.627 112.228 27.477 1.00 61.73  ?  44  GLN B CB  1 
ATOM   1437 C  CG  . GLN B 2 44  ? 28.556 112.598 26.002 1.00 62.67  ?  44  GLN B CG  1 
ATOM   1438 C  CD  . GLN B 2 44  ? 27.651 111.665 25.247 1.00 71.86  ?  44  GLN B CD  1 
ATOM   1439 O  OE1 . GLN B 2 44  ? 26.455 111.577 25.537 1.00 76.67  ?  44  GLN B OE1 1 
ATOM   1440 N  NE2 . GLN B 2 44  ? 28.215 110.937 24.288 1.00 75.93  ?  44  GLN B NE2 1 
ATOM   1441 N  N   . ALA B 2 45  ? 30.096 115.371 28.151 1.00 57.51  ?  45  ALA B N   1 
ATOM   1442 C  CA  . ALA B 2 45  ? 29.822 116.794 28.262 1.00 63.15  ?  45  ALA B CA  1 
ATOM   1443 C  C   . ALA B 2 45  ? 29.053 117.268 27.035 1.00 73.60  ?  45  ALA B C   1 
ATOM   1444 O  O   . ALA B 2 45  ? 28.998 116.566 26.015 1.00 73.65  ?  45  ALA B O   1 
ATOM   1445 C  CB  . ALA B 2 45  ? 31.133 117.565 28.409 1.00 53.17  ?  45  ALA B CB  1 
ATOM   1446 N  N   . PRO B 2 46  ? 28.426 118.445 27.101 1.00 77.16  ?  46  PRO B N   1 
ATOM   1447 C  CA  . PRO B 2 46  ? 27.692 118.947 25.930 1.00 77.03  ?  46  PRO B CA  1 
ATOM   1448 C  C   . PRO B 2 46  ? 28.608 119.078 24.719 1.00 71.86  ?  46  PRO B C   1 
ATOM   1449 O  O   . PRO B 2 46  ? 29.687 119.674 24.798 1.00 69.47  ?  46  PRO B O   1 
ATOM   1450 C  CB  . PRO B 2 46  ? 27.167 120.310 26.397 1.00 77.24  ?  46  PRO B CB  1 
ATOM   1451 C  CG  . PRO B 2 46  ? 27.102 120.202 27.887 1.00 76.11  ?  46  PRO B CG  1 
ATOM   1452 C  CD  . PRO B 2 46  ? 28.252 119.318 28.279 1.00 73.86  ?  46  PRO B CD  1 
ATOM   1453 N  N   . GLY B 2 47  ? 28.185 118.477 23.606 1.00 69.20  ?  47  GLY B N   1 
ATOM   1454 C  CA  . GLY B 2 47  ? 28.901 118.604 22.351 1.00 68.77  ?  47  GLY B CA  1 
ATOM   1455 C  C   . GLY B 2 47  ? 30.222 117.871 22.238 1.00 79.77  ?  47  GLY B C   1 
ATOM   1456 O  O   . GLY B 2 47  ? 30.928 118.057 21.244 1.00 86.29  ?  47  GLY B O   1 
ATOM   1457 N  N   . LYS B 2 48  ? 30.594 117.042 23.206 1.00 82.33  ?  48  LYS B N   1 
ATOM   1458 C  CA  . LYS B 2 48  ? 31.840 116.300 23.101 1.00 73.07  ?  48  LYS B CA  1 
ATOM   1459 C  C   . LYS B 2 48  ? 31.573 114.808 23.184 1.00 63.37  ?  48  LYS B C   1 
ATOM   1460 O  O   . LYS B 2 48  ? 30.490 114.362 23.580 1.00 57.36  ?  48  LYS B O   1 
ATOM   1461 C  CB  . LYS B 2 48  ? 32.845 116.705 24.184 1.00 71.55  ?  48  LYS B CB  1 
ATOM   1462 C  CG  . LYS B 2 48  ? 32.787 118.153 24.558 1.00 70.68  ?  48  LYS B CG  1 
ATOM   1463 C  CD  . LYS B 2 48  ? 33.947 118.498 25.441 1.00 72.11  ?  48  LYS B CD  1 
ATOM   1464 C  CE  . LYS B 2 48  ? 33.893 119.957 25.831 1.00 79.38  ?  48  LYS B CE  1 
ATOM   1465 N  NZ  . LYS B 2 48  ? 34.330 120.093 27.251 1.00 80.05  1  48  LYS B NZ  1 
ATOM   1466 N  N   . GLU B 2 49  ? 32.590 114.047 22.796 1.00 68.42  ?  49  GLU B N   1 
ATOM   1467 C  CA  . GLU B 2 49  ? 32.486 112.599 22.779 1.00 73.01  ?  49  GLU B CA  1 
ATOM   1468 C  C   . GLU B 2 49  ? 32.501 112.043 24.196 1.00 71.58  ?  49  GLU B C   1 
ATOM   1469 O  O   . GLU B 2 49  ? 32.993 112.678 25.134 1.00 75.89  ?  49  GLU B O   1 
ATOM   1470 C  CB  . GLU B 2 49  ? 33.629 111.995 21.959 1.00 75.59  ?  49  GLU B CB  1 
ATOM   1471 C  CG  . GLU B 2 49  ? 33.403 112.092 20.466 1.00 79.86  ?  49  GLU B CG  1 
ATOM   1472 C  CD  . GLU B 2 49  ? 31.996 111.656 20.080 1.00 89.78  ?  49  GLU B CD  1 
ATOM   1473 O  OE1 . GLU B 2 49  ? 31.611 110.515 20.430 1.00 87.08  ?  49  GLU B OE1 1 
ATOM   1474 O  OE2 . GLU B 2 49  ? 31.265 112.463 19.456 1.00 96.09  -1 49  GLU B OE2 1 
ATOM   1475 N  N   . ARG B 2 50  ? 31.949 110.842 24.344 1.00 65.26  ?  50  ARG B N   1 
ATOM   1476 C  CA  . ARG B 2 50  ? 31.996 110.154 25.628 1.00 54.31  ?  50  ARG B CA  1 
ATOM   1477 C  C   . ARG B 2 50  ? 33.431 109.739 25.947 1.00 52.24  ?  50  ARG B C   1 
ATOM   1478 O  O   . ARG B 2 50  ? 34.129 109.186 25.091 1.00 56.03  ?  50  ARG B O   1 
ATOM   1479 C  CB  . ARG B 2 50  ? 31.073 108.943 25.600 1.00 46.52  ?  50  ARG B CB  1 
ATOM   1480 C  CG  . ARG B 2 50  ? 30.801 108.375 26.956 1.00 42.80  ?  50  ARG B CG  1 
ATOM   1481 C  CD  . ARG B 2 50  ? 29.685 107.363 26.910 1.00 47.13  ?  50  ARG B CD  1 
ATOM   1482 N  NE  . ARG B 2 50  ? 28.386 107.994 26.724 1.00 50.18  ?  50  ARG B NE  1 
ATOM   1483 C  CZ  . ARG B 2 50  ? 27.236 107.327 26.651 1.00 53.26  ?  50  ARG B CZ  1 
ATOM   1484 N  NH1 . ARG B 2 50  ? 27.224 106.001 26.751 1.00 46.58  1  50  ARG B NH1 1 
ATOM   1485 N  NH2 . ARG B 2 50  ? 26.097 107.988 26.483 1.00 63.17  ?  50  ARG B NH2 1 
ATOM   1486 N  N   . GLU B 2 51  ? 33.883 110.023 27.173 1.00 48.03  ?  51  GLU B N   1 
ATOM   1487 C  CA  . GLU B 2 51  ? 35.270 109.789 27.553 1.00 47.54  ?  51  GLU B CA  1 
ATOM   1488 C  C   . GLU B 2 51  ? 35.361 109.058 28.886 1.00 42.81  ?  51  GLU B C   1 
ATOM   1489 O  O   . GLU B 2 51  ? 34.536 109.260 29.781 1.00 44.05  ?  51  GLU B O   1 
ATOM   1490 C  CB  . GLU B 2 51  ? 36.060 111.107 27.634 1.00 53.95  ?  51  GLU B CB  1 
ATOM   1491 C  CG  . GLU B 2 51  ? 35.457 112.166 28.539 1.00 68.73  ?  51  GLU B CG  1 
ATOM   1492 C  CD  . GLU B 2 51  ? 36.435 113.307 28.844 1.00 73.96  ?  51  GLU B CD  1 
ATOM   1493 O  OE1 . GLU B 2 51  ? 37.210 113.690 27.945 1.00 78.17  ?  51  GLU B OE1 1 
ATOM   1494 O  OE2 . GLU B 2 51  ? 36.436 113.820 29.984 1.00 72.76  -1 51  GLU B OE2 1 
ATOM   1495 N  N   . GLY B 2 52  ? 36.388 108.216 29.015 1.00 41.04  ?  52  GLY B N   1 
ATOM   1496 C  CA  . GLY B 2 52  ? 36.586 107.453 30.240 1.00 38.82  ?  52  GLY B CA  1 
ATOM   1497 C  C   . GLY B 2 52  ? 37.280 108.287 31.304 1.00 42.65  ?  52  GLY B C   1 
ATOM   1498 O  O   . GLY B 2 52  ? 38.127 109.126 31.010 1.00 53.27  ?  52  GLY B O   1 
ATOM   1499 N  N   . VAL B 2 53  ? 36.918 108.042 32.558 1.00 36.39  ?  53  VAL B N   1 
ATOM   1500 C  CA  . VAL B 2 53  ? 37.432 108.815 33.681 1.00 36.29  ?  53  VAL B CA  1 
ATOM   1501 C  C   . VAL B 2 53  ? 38.275 107.952 34.617 1.00 31.78  ?  53  VAL B C   1 
ATOM   1502 O  O   . VAL B 2 53  ? 39.381 108.330 35.006 1.00 32.52  ?  53  VAL B O   1 
ATOM   1503 C  CB  . VAL B 2 53  ? 36.277 109.506 34.441 1.00 30.42  ?  53  VAL B CB  1 
ATOM   1504 C  CG1 . VAL B 2 53  ? 36.821 110.393 35.501 1.00 46.22  ?  53  VAL B CG1 1 
ATOM   1505 C  CG2 . VAL B 2 53  ? 35.500 110.363 33.499 1.00 29.39  ?  53  VAL B CG2 1 
ATOM   1506 N  N   . ALA B 2 54  ? 37.771 106.777 34.970 1.00 29.82  ?  54  ALA B N   1 
ATOM   1507 C  CA  . ALA B 2 54  ? 38.430 105.906 35.923 1.00 27.24  ?  54  ALA B CA  1 
ATOM   1508 C  C   . ALA B 2 54  ? 37.895 104.504 35.712 1.00 30.62  ?  54  ALA B C   1 
ATOM   1509 O  O   . ALA B 2 54  ? 36.753 104.318 35.277 1.00 32.43  ?  54  ALA B O   1 
ATOM   1510 C  CB  . ALA B 2 54  ? 38.176 106.374 37.354 1.00 30.61  ?  54  ALA B CB  1 
ATOM   1511 N  N   . THR B 2 55  ? 38.724 103.515 36.011 1.00 30.41  ?  55  THR B N   1 
ATOM   1512 C  CA  . THR B 2 55  ? 38.281 102.137 35.887 1.00 27.60  ?  55  THR B CA  1 
ATOM   1513 C  C   . THR B 2 55  ? 38.925 101.315 36.993 1.00 28.34  ?  55  THR B C   1 
ATOM   1514 O  O   . THR B 2 55  ? 39.987 101.667 37.516 1.00 28.28  ?  55  THR B O   1 
ATOM   1515 C  CB  . THR B 2 55  ? 38.628 101.551 34.516 1.00 26.78  ?  55  THR B CB  1 
ATOM   1516 O  OG1 . THR B 2 55  ? 38.001 100.269 34.373 1.00 33.66  ?  55  THR B OG1 1 
ATOM   1517 C  CG2 . THR B 2 55  ? 40.134 101.372 34.394 1.00 21.40  ?  55  THR B CG2 1 
ATOM   1518 N  N   . ILE B 2 56  ? 38.274 100.211 37.349 1.00 22.92  ?  56  ILE B N   1 
ATOM   1519 C  CA  . ILE B 2 56  ? 38.767 99.382  38.443 1.00 28.91  ?  56  ILE B CA  1 
ATOM   1520 C  C   . ILE B 2 56  ? 38.445 97.932  38.127 1.00 29.27  ?  56  ILE B C   1 
ATOM   1521 O  O   . ILE B 2 56  ? 37.414 97.627  37.521 1.00 34.26  ?  56  ILE B O   1 
ATOM   1522 C  CB  . ILE B 2 56  ? 38.166 99.836  39.791 1.00 32.84  ?  56  ILE B CB  1 
ATOM   1523 C  CG1 . ILE B 2 56  ? 38.908 99.201  40.962 1.00 25.01  ?  56  ILE B CG1 1 
ATOM   1524 C  CG2 . ILE B 2 56  ? 36.684 99.519  39.864 1.00 29.79  ?  56  ILE B CG2 1 
ATOM   1525 C  CD1 . ILE B 2 56  ? 38.396 99.722  42.300 1.00 28.78  ?  56  ILE B CD1 1 
ATOM   1526 N  N   . TYR B 2 57  ? 39.349 97.037  38.512 1.00 33.05  ?  57  TYR B N   1 
ATOM   1527 C  CA  . TYR B 2 57  ? 39.203 95.618  38.213 1.00 29.82  ?  57  TYR B CA  1 
ATOM   1528 C  C   . TYR B 2 57  ? 38.448 94.969  39.364 1.00 27.97  ?  57  TYR B C   1 
ATOM   1529 O  O   . TYR B 2 57  ? 38.956 94.900  40.488 1.00 28.06  ?  57  TYR B O   1 
ATOM   1530 C  CB  . TYR B 2 57  ? 40.566 94.972  38.008 1.00 26.64  ?  57  TYR B CB  1 
ATOM   1531 C  CG  . TYR B 2 57  ? 40.497 93.530  37.576 1.00 27.07  ?  57  TYR B CG  1 
ATOM   1532 C  CD1 . TYR B 2 57  ? 41.125 92.538  38.312 1.00 29.09  ?  57  TYR B CD1 1 
ATOM   1533 C  CD2 . TYR B 2 57  ? 39.813 93.163  36.413 1.00 31.31  ?  57  TYR B CD2 1 
ATOM   1534 C  CE1 . TYR B 2 57  ? 41.070 91.211  37.915 1.00 31.68  ?  57  TYR B CE1 1 
ATOM   1535 C  CE2 . TYR B 2 57  ? 39.756 91.840  35.995 1.00 29.44  ?  57  TYR B CE2 1 
ATOM   1536 C  CZ  . TYR B 2 57  ? 40.386 90.866  36.750 1.00 34.36  ?  57  TYR B CZ  1 
ATOM   1537 O  OH  . TYR B 2 57  ? 40.328 89.542  36.338 1.00 31.89  ?  57  TYR B OH  1 
ATOM   1538 N  N   . THR B 2 58  ? 37.231 94.501  39.090 1.00 30.03  ?  58  THR B N   1 
ATOM   1539 C  CA  . THR B 2 58  ? 36.403 93.902  40.130 1.00 25.78  ?  58  THR B CA  1 
ATOM   1540 C  C   . THR B 2 58  ? 36.952 92.581  40.645 1.00 34.49  ?  58  THR B C   1 
ATOM   1541 O  O   . THR B 2 58  ? 36.550 92.147  41.731 1.00 45.71  ?  58  THR B O   1 
ATOM   1542 C  CB  . THR B 2 58  ? 34.977 93.699  39.633 1.00 27.18  ?  58  THR B CB  1 
ATOM   1543 O  OG1 . THR B 2 58  ? 34.932 92.597  38.714 1.00 28.71  ?  58  THR B OG1 1 
ATOM   1544 C  CG2 . THR B 2 58  ? 34.453 94.953  39.003 1.00 21.49  ?  58  THR B CG2 1 
ATOM   1545 N  N   . GLY B 2 59  ? 37.851 91.937  39.906 1.00 38.63  ?  59  GLY B N   1 
ATOM   1546 C  CA  . GLY B 2 59  ? 38.511 90.733  40.360 1.00 35.98  ?  59  GLY B CA  1 
ATOM   1547 C  C   . GLY B 2 59  ? 39.811 90.960  41.099 1.00 38.90  ?  59  GLY B C   1 
ATOM   1548 O  O   . GLY B 2 59  ? 40.555 90.000  41.315 1.00 37.04  ?  59  GLY B O   1 
ATOM   1549 N  N   . GLY B 2 60  ? 40.112 92.199  41.496 1.00 46.77  ?  60  GLY B N   1 
ATOM   1550 C  CA  . GLY B 2 60  ? 41.364 92.516  42.164 1.00 36.34  ?  60  GLY B CA  1 
ATOM   1551 C  C   . GLY B 2 60  ? 41.391 93.909  42.757 1.00 37.76  ?  60  GLY B C   1 
ATOM   1552 O  O   . GLY B 2 60  ? 40.538 94.250  43.585 1.00 38.97  ?  60  GLY B O   1 
ATOM   1553 N  N   . SER B 2 61  ? 42.355 94.738  42.336 1.00 35.14  ?  61  SER B N   1 
ATOM   1554 C  CA  . SER B 2 61  ? 42.450 96.076  42.913 1.00 33.65  ?  61  SER B CA  1 
ATOM   1555 C  C   . SER B 2 61  ? 43.043 97.126  41.986 1.00 32.42  ?  61  SER B C   1 
ATOM   1556 O  O   . SER B 2 61  ? 43.109 98.292  42.389 1.00 35.92  ?  61  SER B O   1 
ATOM   1557 C  CB  . SER B 2 61  ? 43.276 96.036  44.211 1.00 39.25  ?  61  SER B CB  1 
ATOM   1558 O  OG  . SER B 2 61  ? 44.620 95.668  43.940 1.00 52.97  ?  61  SER B OG  1 
ATOM   1559 N  N   . GLY B 2 62  ? 43.486 96.776  40.781 1.00 32.39  ?  62  GLY B N   1 
ATOM   1560 C  CA  . GLY B 2 62  ? 44.111 97.773  39.924 1.00 35.70  ?  62  GLY B CA  1 
ATOM   1561 C  C   . GLY B 2 62  ? 43.121 98.852  39.521 1.00 34.78  ?  62  GLY B C   1 
ATOM   1562 O  O   . GLY B 2 62  ? 41.940 98.583  39.292 1.00 29.19  ?  62  GLY B O   1 
ATOM   1563 N  N   . THR B 2 63  ? 43.610 100.094 39.459 1.00 32.56  ?  63  THR B N   1 
ATOM   1564 C  CA  . THR B 2 63  ? 42.808 101.248 39.076 1.00 26.34  ?  63  THR B CA  1 
ATOM   1565 C  C   . THR B 2 63  ? 43.587 102.084 38.070 1.00 28.83  ?  63  THR B C   1 
ATOM   1566 O  O   . THR B 2 63  ? 44.820 102.107 38.090 1.00 29.51  ?  63  THR B O   1 
ATOM   1567 C  CB  . THR B 2 63  ? 42.439 102.131 40.292 1.00 29.11  ?  63  THR B CB  1 
ATOM   1568 O  OG1 . THR B 2 63  ? 43.626 102.504 41.020 1.00 31.11  ?  63  THR B OG1 1 
ATOM   1569 C  CG2 . THR B 2 63  ? 41.513 101.397 41.216 1.00 24.65  ?  63  THR B CG2 1 
ATOM   1570 N  N   . TYR B 2 64  ? 42.858 102.766 37.182 1.00 32.95  ?  64  TYR B N   1 
ATOM   1571 C  CA  . TYR B 2 64  ? 43.472 103.612 36.165 1.00 25.98  ?  64  TYR B CA  1 
ATOM   1572 C  C   . TYR B 2 64  ? 42.555 104.788 35.901 1.00 26.07  ?  64  TYR B C   1 
ATOM   1573 O  O   . TYR B 2 64  ? 41.332 104.632 35.904 1.00 30.08  ?  64  TYR B O   1 
ATOM   1574 C  CB  . TYR B 2 64  ? 43.736 102.852 34.864 1.00 20.42  ?  64  TYR B CB  1 
ATOM   1575 C  CG  . TYR B 2 64  ? 44.677 101.701 35.051 1.00 21.93  ?  64  TYR B CG  1 
ATOM   1576 C  CD1 . TYR B 2 64  ? 44.201 100.430 35.326 1.00 30.53  ?  64  TYR B CD1 1 
ATOM   1577 C  CD2 . TYR B 2 64  ? 46.044 101.885 34.985 1.00 30.03  ?  64  TYR B CD2 1 
ATOM   1578 C  CE1 . TYR B 2 64  ? 45.061 99.367  35.513 1.00 38.41  ?  64  TYR B CE1 1 
ATOM   1579 C  CE2 . TYR B 2 64  ? 46.917 100.826 35.169 1.00 33.51  ?  64  TYR B CE2 1 
ATOM   1580 C  CZ  . TYR B 2 64  ? 46.421 99.571  35.437 1.00 37.32  ?  64  TYR B CZ  1 
ATOM   1581 O  OH  . TYR B 2 64  ? 47.281 98.511  35.632 1.00 46.02  ?  64  TYR B OH  1 
ATOM   1582 N  N   . TYR B 2 65  ? 43.161 105.952 35.658 1.00 31.89  ?  65  TYR B N   1 
ATOM   1583 C  CA  . TYR B 2 65  ? 42.457 107.223 35.556 1.00 36.80  ?  65  TYR B CA  1 
ATOM   1584 C  C   . TYR B 2 65  ? 42.863 107.953 34.283 1.00 35.76  ?  65  TYR B C   1 
ATOM   1585 O  O   . TYR B 2 65  ? 43.989 107.809 33.792 1.00 40.10  ?  65  TYR B O   1 
ATOM   1586 C  CB  . TYR B 2 65  ? 42.768 108.133 36.761 1.00 28.24  ?  65  TYR B CB  1 
ATOM   1587 C  CG  . TYR B 2 65  ? 42.443 107.515 38.104 1.00 29.60  ?  65  TYR B CG  1 
ATOM   1588 C  CD1 . TYR B 2 65  ? 43.332 106.663 38.720 1.00 27.39  ?  65  TYR B CD1 1 
ATOM   1589 C  CD2 . TYR B 2 65  ? 41.247 107.795 38.754 1.00 32.54  ?  65  TYR B CD2 1 
ATOM   1590 C  CE1 . TYR B 2 65  ? 43.040 106.099 39.930 1.00 30.66  ?  65  TYR B CE1 1 
ATOM   1591 C  CE2 . TYR B 2 65  ? 40.945 107.237 39.972 1.00 23.39  ?  65  TYR B CE2 1 
ATOM   1592 C  CZ  . TYR B 2 65  ? 41.840 106.383 40.556 1.00 28.96  ?  65  TYR B CZ  1 
ATOM   1593 O  OH  . TYR B 2 65  ? 41.553 105.807 41.788 1.00 36.67  ?  65  TYR B OH  1 
ATOM   1594 N  N   . SER B 2 66  ? 41.940 108.757 33.763 1.00 33.51  ?  66  SER B N   1 
ATOM   1595 C  CA  . SER B 2 66  ? 42.289 109.677 32.690 1.00 33.83  ?  66  SER B CA  1 
ATOM   1596 C  C   . SER B 2 66  ? 43.207 110.771 33.215 1.00 35.76  ?  66  SER B C   1 
ATOM   1597 O  O   . SER B 2 66  ? 43.207 111.088 34.408 1.00 46.19  ?  66  SER B O   1 
ATOM   1598 C  CB  . SER B 2 66  ? 41.038 110.296 32.090 1.00 30.72  ?  66  SER B CB  1 
ATOM   1599 O  OG  . SER B 2 66  ? 40.475 111.245 32.972 1.00 31.75  ?  66  SER B OG  1 
ATOM   1600 N  N   . ASP B 2 67  ? 44.008 111.345 32.312 1.00 43.50  ?  67  ASP B N   1 
ATOM   1601 C  CA  . ASP B 2 67  ? 44.885 112.454 32.690 1.00 39.04  ?  67  ASP B CA  1 
ATOM   1602 C  C   . ASP B 2 67  ? 44.100 113.607 33.300 1.00 38.91  ?  67  ASP B C   1 
ATOM   1603 O  O   . ASP B 2 67  ? 44.525 114.206 34.298 1.00 41.81  ?  67  ASP B O   1 
ATOM   1604 C  CB  . ASP B 2 67  ? 45.655 112.958 31.474 1.00 51.34  ?  67  ASP B CB  1 
ATOM   1605 C  CG  . ASP B 2 67  ? 46.878 112.134 31.170 1.00 60.42  ?  67  ASP B CG  1 
ATOM   1606 O  OD1 . ASP B 2 67  ? 47.242 111.267 32.000 1.00 60.23  ?  67  ASP B OD1 1 
ATOM   1607 O  OD2 . ASP B 2 67  ? 47.469 112.361 30.087 1.00 67.42  -1 67  ASP B OD2 1 
ATOM   1608 N  N   . SER B 2 68  ? 42.953 113.939 32.705 1.00 41.01  ?  68  SER B N   1 
ATOM   1609 C  CA  . SER B 2 68  ? 42.193 115.107 33.137 1.00 40.15  ?  68  SER B CA  1 
ATOM   1610 C  C   . SER B 2 68  ? 41.721 115.012 34.583 1.00 42.69  ?  68  SER B C   1 
ATOM   1611 O  O   . SER B 2 68  ? 41.403 116.049 35.183 1.00 48.76  ?  68  SER B O   1 
ATOM   1612 C  CB  . SER B 2 68  ? 40.995 115.308 32.215 1.00 41.92  ?  68  SER B CB  1 
ATOM   1613 O  OG  . SER B 2 68  ? 40.439 114.053 31.861 1.00 56.75  ?  68  SER B OG  1 
ATOM   1614 N  N   . VAL B 2 69  ? 41.666 113.808 35.161 1.00 34.25  ?  69  VAL B N   1 
ATOM   1615 C  CA  . VAL B 2 69  ? 41.136 113.625 36.508 1.00 34.14  ?  69  VAL B CA  1 
ATOM   1616 C  C   . VAL B 2 69  ? 42.122 112.971 37.463 1.00 39.90  ?  69  VAL B C   1 
ATOM   1617 O  O   . VAL B 2 69  ? 41.778 112.776 38.636 1.00 49.92  ?  69  VAL B O   1 
ATOM   1618 C  CB  . VAL B 2 69  ? 39.809 112.832 36.514 1.00 34.92  ?  69  VAL B CB  1 
ATOM   1619 C  CG1 . VAL B 2 69  ? 38.775 113.425 35.542 1.00 25.32  ?  69  VAL B CG1 1 
ATOM   1620 C  CG2 . VAL B 2 69  ? 40.065 111.337 36.259 1.00 28.33  ?  69  VAL B CG2 1 
ATOM   1621 N  N   . GLU B 2 70  ? 43.327 112.615 37.015 1.00 45.02  ?  70  GLU B N   1 
ATOM   1622 C  CA  . GLU B 2 70  ? 44.299 112.022 37.934 1.00 51.46  ?  70  GLU B CA  1 
ATOM   1623 C  C   . GLU B 2 70  ? 44.618 112.989 39.075 1.00 45.55  ?  70  GLU B C   1 
ATOM   1624 O  O   . GLU B 2 70  ? 44.786 114.195 38.866 1.00 48.84  ?  70  GLU B O   1 
ATOM   1625 C  CB  . GLU B 2 70  ? 45.580 111.634 37.184 1.00 62.53  ?  70  GLU B CB  1 
ATOM   1626 C  CG  . GLU B 2 70  ? 46.633 110.925 38.037 1.00 75.41  ?  70  GLU B CG  1 
ATOM   1627 C  CD  . GLU B 2 70  ? 46.417 109.416 38.121 1.00 84.24  ?  70  GLU B CD  1 
ATOM   1628 O  OE1 . GLU B 2 70  ? 46.451 108.755 37.060 1.00 81.54  ?  70  GLU B OE1 1 
ATOM   1629 O  OE2 . GLU B 2 70  ? 46.226 108.895 39.248 1.00 87.13  -1 70  GLU B OE2 1 
ATOM   1630 N  N   . GLY B 2 71  ? 44.677 112.460 40.295 1.00 34.25  ?  71  GLY B N   1 
ATOM   1631 C  CA  . GLY B 2 71  ? 44.919 113.280 41.458 1.00 32.40  ?  71  GLY B CA  1 
ATOM   1632 C  C   . GLY B 2 71  ? 43.669 113.793 42.147 1.00 33.49  ?  71  GLY B C   1 
ATOM   1633 O  O   . GLY B 2 71  ? 43.665 113.931 43.377 1.00 46.06  ?  71  GLY B O   1 
ATOM   1634 N  N   . ARG B 2 72  ? 42.596 114.049 41.395 1.00 32.81  ?  72  ARG B N   1 
ATOM   1635 C  CA  . ARG B 2 72  ? 41.362 114.586 41.958 1.00 26.92  ?  72  ARG B CA  1 
ATOM   1636 C  C   . ARG B 2 72  ? 40.262 113.558 42.165 1.00 31.45  ?  72  ARG B C   1 
ATOM   1637 O  O   . ARG B 2 72  ? 39.480 113.697 43.107 1.00 36.00  ?  72  ARG B O   1 
ATOM   1638 C  CB  . ARG B 2 72  ? 40.816 115.697 41.064 1.00 21.46  ?  72  ARG B CB  1 
ATOM   1639 C  CG  . ARG B 2 72  ? 41.865 116.699 40.682 1.00 26.45  ?  72  ARG B CG  1 
ATOM   1640 C  CD  . ARG B 2 72  ? 41.274 117.835 39.860 1.00 30.57  ?  72  ARG B CD  1 
ATOM   1641 N  NE  . ARG B 2 72  ? 40.726 117.414 38.573 1.00 36.70  ?  72  ARG B NE  1 
ATOM   1642 C  CZ  . ARG B 2 72  ? 39.481 117.660 38.175 1.00 40.72  ?  72  ARG B CZ  1 
ATOM   1643 N  NH1 . ARG B 2 72  ? 38.653 118.333 38.965 1.00 36.83  1  72  ARG B NH1 1 
ATOM   1644 N  NH2 . ARG B 2 72  ? 39.067 117.256 36.972 1.00 37.44  ?  72  ARG B NH2 1 
ATOM   1645 N  N   . PHE B 2 73  ? 40.150 112.553 41.302 1.00 30.44  ?  73  PHE B N   1 
ATOM   1646 C  CA  . PHE B 2 73  ? 39.120 111.540 41.439 1.00 27.85  ?  73  PHE B CA  1 
ATOM   1647 C  C   . PHE B 2 73  ? 39.761 110.262 41.946 1.00 35.26  ?  73  PHE B C   1 
ATOM   1648 O  O   . PHE B 2 73  ? 40.927 109.975 41.644 1.00 35.44  ?  73  PHE B O   1 
ATOM   1649 C  CB  . PHE B 2 73  ? 38.401 111.248 40.110 1.00 28.64  ?  73  PHE B CB  1 
ATOM   1650 C  CG  . PHE B 2 73  ? 37.600 112.412 39.554 1.00 33.67  ?  73  PHE B CG  1 
ATOM   1651 C  CD1 . PHE B 2 73  ? 37.636 113.671 40.141 1.00 35.77  ?  73  PHE B CD1 1 
ATOM   1652 C  CD2 . PHE B 2 73  ? 36.817 112.237 38.419 1.00 32.67  ?  73  PHE B CD2 1 
ATOM   1653 C  CE1 . PHE B 2 73  ? 36.895 114.732 39.605 1.00 26.96  ?  73  PHE B CE1 1 
ATOM   1654 C  CE2 . PHE B 2 73  ? 36.077 113.280 37.887 1.00 29.29  ?  73  PHE B CE2 1 
ATOM   1655 C  CZ  . PHE B 2 73  ? 36.113 114.527 38.482 1.00 33.66  ?  73  PHE B CZ  1 
ATOM   1656 N  N   . THR B 2 74  ? 38.988 109.491 42.708 1.00 34.64  ?  74  THR B N   1 
ATOM   1657 C  CA  . THR B 2 74  ? 39.423 108.169 43.127 1.00 32.49  ?  74  THR B CA  1 
ATOM   1658 C  C   . THR B 2 74  ? 38.289 107.174 42.985 1.00 32.09  ?  74  THR B C   1 
ATOM   1659 O  O   . THR B 2 74  ? 37.144 107.479 43.333 1.00 36.80  ?  74  THR B O   1 
ATOM   1660 C  CB  . THR B 2 74  ? 39.904 108.177 44.554 1.00 26.07  ?  74  THR B CB  1 
ATOM   1661 O  OG1 . THR B 2 74  ? 40.791 109.282 44.718 1.00 35.99  ?  74  THR B OG1 1 
ATOM   1662 C  CG2 . THR B 2 74  ? 40.634 106.909 44.830 1.00 21.13  ?  74  THR B CG2 1 
ATOM   1663 N  N   . ILE B 2 75  ? 38.616 105.984 42.483 1.00 30.47  ?  75  ILE B N   1 
ATOM   1664 C  CA  . ILE B 2 75  ? 37.632 104.939 42.236 1.00 30.60  ?  75  ILE B CA  1 
ATOM   1665 C  C   . ILE B 2 75  ? 37.912 103.775 43.180 1.00 35.13  ?  75  ILE B C   1 
ATOM   1666 O  O   . ILE B 2 75  ? 39.069 103.391 43.383 1.00 36.98  ?  75  ILE B O   1 
ATOM   1667 C  CB  . ILE B 2 75  ? 37.635 104.481 40.765 1.00 28.62  ?  75  ILE B CB  1 
ATOM   1668 C  CG1 . ILE B 2 75  ? 36.448 103.545 40.501 1.00 23.07  ?  75  ILE B CG1 1 
ATOM   1669 C  CG2 . ILE B 2 75  ? 38.948 103.818 40.405 1.00 19.59  ?  75  ILE B CG2 1 
ATOM   1670 C  CD1 . ILE B 2 75  ? 36.340 103.067 39.075 1.00 24.91  ?  75  ILE B CD1 1 
ATOM   1671 N  N   . SER B 2 76  ? 36.851 103.229 43.762 1.00 34.51  ?  76  SER B N   1 
ATOM   1672 C  CA  . SER B 2 76  ? 36.950 102.145 44.724 1.00 34.11  ?  76  SER B CA  1 
ATOM   1673 C  C   . SER B 2 76  ? 35.721 101.259 44.576 1.00 32.95  ?  76  SER B C   1 
ATOM   1674 O  O   . SER B 2 76  ? 34.786 101.576 43.835 1.00 43.79  ?  76  SER B O   1 
ATOM   1675 C  CB  . SER B 2 76  ? 37.062 102.694 46.146 1.00 35.29  ?  76  SER B CB  1 
ATOM   1676 O  OG  . SER B 2 76  ? 35.990 103.596 46.384 1.00 42.85  ?  76  SER B OG  1 
ATOM   1677 N  N   . GLN B 2 77  ? 35.712 100.139 45.292 1.00 32.66  ?  77  GLN B N   1 
ATOM   1678 C  CA  . GLN B 2 77  ? 34.594 99.220  45.175 1.00 32.71  ?  77  GLN B CA  1 
ATOM   1679 C  C   . GLN B 2 77  ? 34.350 98.509  46.496 1.00 40.49  ?  77  GLN B C   1 
ATOM   1680 O  O   . GLN B 2 77  ? 35.262 98.327  47.317 1.00 38.15  ?  77  GLN B O   1 
ATOM   1681 C  CB  . GLN B 2 77  ? 34.847 98.177  44.095 1.00 29.38  ?  77  GLN B CB  1 
ATOM   1682 C  CG  . GLN B 2 77  ? 36.114 97.394  44.354 1.00 28.93  ?  77  GLN B CG  1 
ATOM   1683 C  CD  . GLN B 2 77  ? 36.453 96.438  43.250 1.00 32.77  ?  77  GLN B CD  1 
ATOM   1684 O  OE1 . GLN B 2 77  ? 35.567 95.993  42.510 1.00 42.07  ?  77  GLN B OE1 1 
ATOM   1685 N  NE2 . GLN B 2 77  ? 37.745 96.114  43.116 1.00 34.41  ?  77  GLN B NE2 1 
ATOM   1686 N  N   . ASP B 2 78  ? 33.103 98.105  46.676 1.00 34.40  ?  78  ASP B N   1 
ATOM   1687 C  CA  . ASP B 2 78  ? 32.671 97.218  47.744 1.00 36.28  ?  78  ASP B CA  1 
ATOM   1688 C  C   . ASP B 2 78  ? 32.201 95.958  47.027 1.00 36.30  ?  78  ASP B C   1 
ATOM   1689 O  O   . ASP B 2 78  ? 31.043 95.861  46.612 1.00 41.96  ?  78  ASP B O   1 
ATOM   1690 C  CB  . ASP B 2 78  ? 31.580 97.881  48.566 1.00 49.71  ?  78  ASP B CB  1 
ATOM   1691 C  CG  . ASP B 2 78  ? 30.908 96.936  49.539 1.00 60.33  ?  78  ASP B CG  1 
ATOM   1692 O  OD1 . ASP B 2 78  ? 31.429 95.823  49.795 1.00 60.50  ?  78  ASP B OD1 1 
ATOM   1693 O  OD2 . ASP B 2 78  ? 29.846 97.340  50.057 1.00 64.32  -1 78  ASP B OD2 1 
ATOM   1694 N  N   . LYS B 2 79  ? 33.124 95.005  46.847 1.00 34.02  ?  79  LYS B N   1 
ATOM   1695 C  CA  . LYS B 2 79  ? 32.868 93.897  45.931 1.00 31.56  ?  79  LYS B CA  1 
ATOM   1696 C  C   . LYS B 2 79  ? 31.660 93.091  46.377 1.00 44.13  ?  79  LYS B C   1 
ATOM   1697 O  O   . LYS B 2 79  ? 30.874 92.620  45.543 1.00 44.38  ?  79  LYS B O   1 
ATOM   1698 C  CB  . LYS B 2 79  ? 34.091 92.986  45.841 1.00 26.25  ?  79  LYS B CB  1 
ATOM   1699 C  CG  . LYS B 2 79  ? 35.410 93.661  45.520 1.00 31.14  ?  79  LYS B CG  1 
ATOM   1700 C  CD  . LYS B 2 79  ? 36.447 92.597  45.153 1.00 25.65  ?  79  LYS B CD  1 
ATOM   1701 C  CE  . LYS B 2 79  ? 37.855 92.982  45.592 1.00 36.18  ?  79  LYS B CE  1 
ATOM   1702 N  NZ  . LYS B 2 79  ? 38.875 92.805  44.503 1.00 43.59  1  79  LYS B NZ  1 
ATOM   1703 N  N   . ALA B 2 80  ? 31.501 92.923  47.696 1.00 55.66  ?  80  ALA B N   1 
ATOM   1704 C  CA  . ALA B 2 80  ? 30.380 92.156  48.228 1.00 49.66  ?  80  ALA B CA  1 
ATOM   1705 C  C   . ALA B 2 80  ? 29.038 92.754  47.825 1.00 47.55  ?  80  ALA B C   1 
ATOM   1706 O  O   . ALA B 2 80  ? 28.060 92.019  47.636 1.00 48.74  ?  80  ALA B O   1 
ATOM   1707 C  CB  . ALA B 2 80  ? 30.493 92.077  49.747 1.00 53.64  ?  80  ALA B CB  1 
ATOM   1708 N  N   . GLN B 2 81  ? 28.970 94.076  47.678 1.00 44.55  ?  81  GLN B N   1 
ATOM   1709 C  CA  . GLN B 2 81  ? 27.750 94.747  47.259 1.00 44.06  ?  81  GLN B CA  1 
ATOM   1710 C  C   . GLN B 2 81  ? 27.749 95.147  45.783 1.00 47.42  ?  81  GLN B C   1 
ATOM   1711 O  O   . GLN B 2 81  ? 26.797 95.794  45.335 1.00 49.30  ?  81  GLN B O   1 
ATOM   1712 C  CB  . GLN B 2 81  ? 27.509 95.981  48.137 1.00 50.32  ?  81  GLN B CB  1 
ATOM   1713 C  CG  . GLN B 2 81  ? 27.391 95.662  49.616 1.00 62.03  ?  81  GLN B CG  1 
ATOM   1714 C  CD  . GLN B 2 81  ? 26.110 94.924  49.975 1.00 72.70  ?  81  GLN B CD  1 
ATOM   1715 O  OE1 . GLN B 2 81  ? 26.147 93.781  50.434 1.00 81.59  ?  81  GLN B OE1 1 
ATOM   1716 N  NE2 . GLN B 2 81  ? 24.973 95.584  49.788 1.00 73.81  ?  81  GLN B NE2 1 
ATOM   1717 N  N   . ARG B 2 82  ? 28.772 94.775  45.010 1.00 49.59  ?  82  ARG B N   1 
ATOM   1718 C  CA  . ARG B 2 82  ? 28.803 95.074  43.576 1.00 42.08  ?  82  ARG B CA  1 
ATOM   1719 C  C   . ARG B 2 82  ? 28.611 96.561  43.307 1.00 35.83  ?  82  ARG B C   1 
ATOM   1720 O  O   . ARG B 2 82  ? 27.923 96.963  42.370 1.00 38.88  ?  82  ARG B O   1 
ATOM   1721 C  CB  . ARG B 2 82  ? 27.754 94.264  42.822 1.00 36.61  ?  82  ARG B CB  1 
ATOM   1722 C  CG  . ARG B 2 82  ? 27.929 92.786  42.955 1.00 34.54  ?  82  ARG B CG  1 
ATOM   1723 C  CD  . ARG B 2 82  ? 28.046 92.167  41.576 1.00 35.00  ?  82  ARG B CD  1 
ATOM   1724 N  NE  . ARG B 2 82  ? 26.771 91.694  41.069 1.00 35.76  ?  82  ARG B NE  1 
ATOM   1725 C  CZ  . ARG B 2 82  ? 26.471 91.567  39.779 1.00 42.76  ?  82  ARG B CZ  1 
ATOM   1726 N  NH1 . ARG B 2 82  ? 27.353 91.896  38.847 1.00 47.87  1  82  ARG B NH1 1 
ATOM   1727 N  NH2 . ARG B 2 82  ? 25.283 91.100  39.422 1.00 48.26  ?  82  ARG B NH2 1 
ATOM   1728 N  N   . THR B 2 83  ? 29.204 97.390  44.151 1.00 37.34  ?  83  THR B N   1 
ATOM   1729 C  CA  . THR B 2 83  ? 29.102 98.829  44.010 1.00 36.55  ?  83  THR B CA  1 
ATOM   1730 C  C   . THR B 2 83  ? 30.491 99.415  43.803 1.00 42.73  ?  83  THR B C   1 
ATOM   1731 O  O   . THR B 2 83  ? 31.442 99.060  44.513 1.00 40.82  ?  83  THR B O   1 
ATOM   1732 C  CB  . THR B 2 83  ? 28.437 99.449  45.227 1.00 41.96  ?  83  THR B CB  1 
ATOM   1733 O  OG1 . THR B 2 83  ? 27.235 98.728  45.515 1.00 51.16  ?  83  THR B OG1 1 
ATOM   1734 C  CG2 . THR B 2 83  ? 28.081 100.888 44.930 1.00 38.63  ?  83  THR B CG2 1 
ATOM   1735 N  N   . VAL B 2 84  ? 30.600 100.300 42.819 1.00 36.26  ?  84  VAL B N   1 
ATOM   1736 C  CA  . VAL B 2 84  ? 31.843 100.971 42.479 1.00 35.74  ?  84  VAL B CA  1 
ATOM   1737 C  C   . VAL B 2 84  ? 31.621 102.460 42.679 1.00 36.58  ?  84  VAL B C   1 
ATOM   1738 O  O   . VAL B 2 84  ? 30.684 103.029 42.105 1.00 32.24  ?  84  VAL B O   1 
ATOM   1739 C  CB  . VAL B 2 84  ? 32.270 100.661 41.033 1.00 29.95  ?  84  VAL B CB  1 
ATOM   1740 C  CG1 . VAL B 2 84  ? 33.407 101.557 40.633 1.00 27.66  ?  84  VAL B CG1 1 
ATOM   1741 C  CG2 . VAL B 2 84  ? 32.683 99.200  40.911 1.00 29.12  ?  84  VAL B CG2 1 
ATOM   1742 N  N   . TYR B 2 85  ? 32.477 103.081 43.493 1.00 39.47  ?  85  TYR B N   1 
ATOM   1743 C  CA  . TYR B 2 85  ? 32.329 104.470 43.913 1.00 36.30  ?  85  TYR B CA  1 
ATOM   1744 C  C   . TYR B 2 85  ? 33.325 105.350 43.181 1.00 33.80  ?  85  TYR B C   1 
ATOM   1745 O  O   . TYR B 2 85  ? 34.489 104.975 43.022 1.00 33.82  ?  85  TYR B O   1 
ATOM   1746 C  CB  . TYR B 2 85  ? 32.570 104.620 45.417 1.00 37.20  ?  85  TYR B CB  1 
ATOM   1747 C  CG  . TYR B 2 85  ? 31.629 103.814 46.271 1.00 38.39  ?  85  TYR B CG  1 
ATOM   1748 C  CD1 . TYR B 2 85  ? 30.327 104.243 46.479 1.00 35.39  ?  85  TYR B CD1 1 
ATOM   1749 C  CD2 . TYR B 2 85  ? 32.040 102.626 46.873 1.00 42.44  ?  85  TYR B CD2 1 
ATOM   1750 C  CE1 . TYR B 2 85  ? 29.446 103.516 47.257 1.00 38.60  ?  85  TYR B CE1 1 
ATOM   1751 C  CE2 . TYR B 2 85  ? 31.161 101.883 47.658 1.00 43.78  ?  85  TYR B CE2 1 
ATOM   1752 C  CZ  . TYR B 2 85  ? 29.865 102.339 47.842 1.00 45.97  ?  85  TYR B CZ  1 
ATOM   1753 O  OH  . TYR B 2 85  ? 28.974 101.628 48.611 1.00 56.77  ?  85  TYR B OH  1 
ATOM   1754 N  N   . LEU B 2 86  ? 32.878 106.542 42.785 1.00 34.86  ?  86  LEU B N   1 
ATOM   1755 C  CA  . LEU B 2 86  ? 33.759 107.577 42.252 1.00 27.83  ?  86  LEU B CA  1 
ATOM   1756 C  C   . LEU B 2 86  ? 33.755 108.747 43.220 1.00 32.44  ?  86  LEU B C   1 
ATOM   1757 O  O   . LEU B 2 86  ? 32.783 109.506 43.269 1.00 40.38  ?  86  LEU B O   1 
ATOM   1758 C  CB  . LEU B 2 86  ? 33.319 108.052 40.868 1.00 29.01  ?  86  LEU B CB  1 
ATOM   1759 C  CG  . LEU B 2 86  ? 34.371 108.921 40.159 1.00 29.06  ?  86  LEU B CG  1 
ATOM   1760 C  CD1 . LEU B 2 86  ? 35.638 108.114 39.877 1.00 21.52  ?  86  LEU B CD1 1 
ATOM   1761 C  CD2 . LEU B 2 86  ? 33.816 109.504 38.882 1.00 29.10  ?  86  LEU B CD2 1 
ATOM   1762 N  N   . GLN B 2 87  ? 34.845 108.907 43.974 1.00 33.31  ?  87  GLN B N   1 
ATOM   1763 C  CA  . GLN B 2 87  ? 35.013 110.050 44.860 1.00 30.43  ?  87  GLN B CA  1 
ATOM   1764 C  C   . GLN B 2 87  ? 35.659 111.165 44.053 1.00 35.47  ?  87  GLN B C   1 
ATOM   1765 O  O   . GLN B 2 87  ? 36.826 111.053 43.660 1.00 34.88  ?  87  GLN B O   1 
ATOM   1766 C  CB  . GLN B 2 87  ? 35.861 109.688 46.073 1.00 39.37  ?  87  GLN B CB  1 
ATOM   1767 C  CG  . GLN B 2 87  ? 36.121 110.874 47.003 1.00 43.63  ?  87  GLN B CG  1 
ATOM   1768 C  CD  . GLN B 2 87  ? 34.860 111.372 47.678 1.00 39.97  ?  87  GLN B CD  1 
ATOM   1769 O  OE1 . GLN B 2 87  ? 34.028 110.581 48.112 1.00 55.18  ?  87  GLN B OE1 1 
ATOM   1770 N  NE2 . GLN B 2 87  ? 34.716 112.688 47.774 1.00 40.81  ?  87  GLN B NE2 1 
ATOM   1771 N  N   . MET B 2 88  ? 34.889 112.232 43.794 1.00 30.47  ?  88  MET B N   1 
ATOM   1772 C  CA  . MET B 2 88  ? 35.311 113.355 42.957 1.00 26.69  ?  88  MET B CA  1 
ATOM   1773 C  C   . MET B 2 88  ? 35.599 114.553 43.853 1.00 32.21  ?  88  MET B C   1 
ATOM   1774 O  O   . MET B 2 88  ? 34.680 115.094 44.478 1.00 39.96  ?  88  MET B O   1 
ATOM   1775 C  CB  . MET B 2 88  ? 34.238 113.722 41.932 1.00 29.13  ?  88  MET B CB  1 
ATOM   1776 C  CG  . MET B 2 88  ? 33.592 112.556 41.216 1.00 29.65  ?  88  MET B CG  1 
ATOM   1777 S  SD  . MET B 2 88  ? 32.520 113.187 39.895 1.00 41.63  ?  88  MET B SD  1 
ATOM   1778 C  CE  . MET B 2 88  ? 31.004 113.187 40.793 1.00 50.99  ?  88  MET B CE  1 
ATOM   1779 N  N   . ASN B 2 89  ? 36.861 114.980 43.895 1.00 37.94  ?  89  ASN B N   1 
ATOM   1780 C  CA  . ASN B 2 89  ? 37.284 116.126 44.689 1.00 34.84  ?  89  ASN B CA  1 
ATOM   1781 C  C   . ASN B 2 89  ? 37.792 117.235 43.780 1.00 32.68  ?  89  ASN B C   1 
ATOM   1782 O  O   . ASN B 2 89  ? 38.024 117.037 42.585 1.00 40.87  ?  89  ASN B O   1 
ATOM   1783 C  CB  . ASN B 2 89  ? 38.392 115.750 45.683 1.00 33.60  ?  89  ASN B CB  1 
ATOM   1784 C  CG  . ASN B 2 89  ? 37.957 114.722 46.701 1.00 35.78  ?  89  ASN B CG  1 
ATOM   1785 O  OD1 . ASN B 2 89  ? 36.826 114.745 47.202 1.00 44.89  ?  89  ASN B OD1 1 
ATOM   1786 N  ND2 . ASN B 2 89  ? 38.856 113.804 47.007 1.00 45.35  ?  89  ASN B ND2 1 
ATOM   1787 N  N   . ASP B 2 90  ? 38.017 118.397 44.394 1.00 34.83  ?  90  ASP B N   1 
ATOM   1788 C  CA  . ASP B 2 90  ? 38.429 119.613 43.696 1.00 35.32  ?  90  ASP B CA  1 
ATOM   1789 C  C   . ASP B 2 90  ? 37.735 119.728 42.330 1.00 34.76  ?  90  ASP B C   1 
ATOM   1790 O  O   . ASP B 2 90  ? 38.374 119.729 41.277 1.00 50.90  ?  90  ASP B O   1 
ATOM   1791 C  CB  . ASP B 2 90  ? 39.957 119.688 43.575 1.00 37.84  ?  90  ASP B CB  1 
ATOM   1792 C  CG  . ASP B 2 90  ? 40.417 121.046 43.041 1.00 79.10  ?  90  ASP B CG  1 
ATOM   1793 O  OD1 . ASP B 2 90  ? 41.026 121.086 41.943 1.00 93.92  ?  90  ASP B OD1 1 
ATOM   1794 O  OD2 . ASP B 2 90  ? 40.104 122.083 43.701 1.00 88.88  -1 90  ASP B OD2 1 
ATOM   1795 N  N   . LEU B 2 91  ? 36.398 119.801 42.352 1.00 38.11  ?  91  LEU B N   1 
ATOM   1796 C  CA  . LEU B 2 91  ? 35.624 119.792 41.114 1.00 35.03  ?  91  LEU B CA  1 
ATOM   1797 C  C   . LEU B 2 91  ? 35.800 121.106 40.353 1.00 40.75  ?  91  LEU B C   1 
ATOM   1798 O  O   . LEU B 2 91  ? 35.803 122.184 40.948 1.00 45.80  ?  91  LEU B O   1 
ATOM   1799 C  CB  . LEU B 2 91  ? 34.149 119.514 41.419 1.00 32.60  ?  91  LEU B CB  1 
ATOM   1800 C  CG  . LEU B 2 91  ? 33.858 118.034 41.708 1.00 36.37  ?  91  LEU B CG  1 
ATOM   1801 C  CD1 . LEU B 2 91  ? 32.458 117.765 42.217 1.00 32.26  ?  91  LEU B CD1 1 
ATOM   1802 C  CD2 . LEU B 2 91  ? 34.104 117.226 40.439 1.00 33.05  ?  91  LEU B CD2 1 
ATOM   1803 N  N   . LYS B 2 92  ? 35.988 121.012 39.033 1.00 43.12  ?  92  LYS B N   1 
ATOM   1804 C  CA  . LYS B 2 92  ? 36.053 122.177 38.160 1.00 38.69  ?  92  LYS B CA  1 
ATOM   1805 C  C   . LYS B 2 92  ? 34.760 122.299 37.371 1.00 50.38  ?  92  LYS B C   1 
ATOM   1806 O  O   . LYS B 2 92  ? 33.995 121.334 37.262 1.00 53.09  ?  92  LYS B O   1 
ATOM   1807 C  CB  . LYS B 2 92  ? 37.232 122.061 37.190 1.00 37.08  ?  92  LYS B CB  1 
ATOM   1808 C  CG  . LYS B 2 92  ? 38.577 121.900 37.872 1.00 42.34  ?  92  LYS B CG  1 
ATOM   1809 C  CD  . LYS B 2 92  ? 39.657 121.438 36.897 1.00 48.13  ?  92  LYS B CD  1 
ATOM   1810 C  CE  . LYS B 2 92  ? 41.043 121.725 37.460 1.00 48.98  ?  92  LYS B CE  1 
ATOM   1811 N  NZ  . LYS B 2 92  ? 42.062 120.833 36.843 1.00 58.78  1  92  LYS B NZ  1 
ATOM   1812 N  N   . PRO B 2 93  ? 34.467 123.478 36.811 1.00 46.82  ?  93  PRO B N   1 
ATOM   1813 C  CA  . PRO B 2 93  ? 33.245 123.596 36.001 1.00 43.73  ?  93  PRO B CA  1 
ATOM   1814 C  C   . PRO B 2 93  ? 33.208 122.636 34.822 1.00 47.58  ?  93  PRO B C   1 
ATOM   1815 O  O   . PRO B 2 93  ? 32.135 122.116 34.488 1.00 52.69  ?  93  PRO B O   1 
ATOM   1816 C  CB  . PRO B 2 93  ? 33.275 125.061 35.558 1.00 46.38  ?  93  PRO B CB  1 
ATOM   1817 C  CG  . PRO B 2 93  ? 34.005 125.747 36.658 1.00 42.14  ?  93  PRO B CG  1 
ATOM   1818 C  CD  . PRO B 2 93  ? 35.098 124.789 37.033 1.00 42.07  ?  93  PRO B CD  1 
ATOM   1819 N  N   . GLU B 2 94  ? 34.357 122.352 34.204 1.00 47.15  ?  94  GLU B N   1 
ATOM   1820 C  CA  . GLU B 2 94  ? 34.408 121.458 33.048 1.00 49.28  ?  94  GLU B CA  1 
ATOM   1821 C  C   . GLU B 2 94  ? 34.205 119.985 33.405 1.00 46.16  ?  94  GLU B C   1 
ATOM   1822 O  O   . GLU B 2 94  ? 34.063 119.157 32.493 1.00 46.69  ?  94  GLU B O   1 
ATOM   1823 C  CB  . GLU B 2 94  ? 35.738 121.640 32.318 1.00 56.58  ?  94  GLU B CB  1 
ATOM   1824 C  CG  . GLU B 2 94  ? 36.958 121.409 33.200 1.00 67.45  ?  94  GLU B CG  1 
ATOM   1825 C  CD  . GLU B 2 94  ? 37.526 122.697 33.784 1.00 73.70  ?  94  GLU B CD  1 
ATOM   1826 O  OE1 . GLU B 2 94  ? 36.762 123.678 33.969 1.00 72.60  ?  94  GLU B OE1 1 
ATOM   1827 O  OE2 . GLU B 2 94  ? 38.747 122.715 34.060 1.00 77.27  -1 94  GLU B OE2 1 
ATOM   1828 N  N   . ASP B 2 95  ? 34.197 119.626 34.692 1.00 42.71  ?  95  ASP B N   1 
ATOM   1829 C  CA  . ASP B 2 95  ? 33.730 118.290 35.042 1.00 45.57  ?  95  ASP B CA  1 
ATOM   1830 C  C   . ASP B 2 95  ? 32.216 118.136 34.886 1.00 45.87  ?  95  ASP B C   1 
ATOM   1831 O  O   . ASP B 2 95  ? 31.701 117.043 35.150 1.00 42.48  ?  95  ASP B O   1 
ATOM   1832 C  CB  . ASP B 2 95  ? 34.104 117.922 36.483 1.00 45.63  ?  95  ASP B CB  1 
ATOM   1833 C  CG  . ASP B 2 95  ? 35.581 118.039 36.768 1.00 45.07  ?  95  ASP B CG  1 
ATOM   1834 O  OD1 . ASP B 2 95  ? 36.404 117.665 35.892 1.00 42.61  ?  95  ASP B OD1 1 
ATOM   1835 O  OD2 . ASP B 2 95  ? 35.906 118.477 37.899 1.00 43.32  -1 95  ASP B OD2 1 
ATOM   1836 N  N   . THR B 2 96  ? 31.489 119.188 34.510 1.00 47.07  ?  96  THR B N   1 
ATOM   1837 C  CA  . THR B 2 96  ? 30.054 119.056 34.291 1.00 43.54  ?  96  THR B CA  1 
ATOM   1838 C  C   . THR B 2 96  ? 29.801 118.143 33.097 1.00 49.90  ?  96  THR B C   1 
ATOM   1839 O  O   . THR B 2 96  ? 30.391 118.323 32.024 1.00 50.26  ?  96  THR B O   1 
ATOM   1840 C  CB  . THR B 2 96  ? 29.412 120.431 34.066 1.00 43.82  ?  96  THR B CB  1 
ATOM   1841 O  OG1 . THR B 2 96  ? 29.324 121.148 35.314 1.00 44.25  ?  96  THR B OG1 1 
ATOM   1842 C  CG2 . THR B 2 96  ? 28.008 120.284 33.472 1.00 43.82  ?  96  THR B CG2 1 
ATOM   1843 N  N   . ALA B 2 97  ? 28.936 117.148 33.299 1.00 51.34  ?  97  ALA B N   1 
ATOM   1844 C  CA  . ALA B 2 97  ? 28.598 116.149 32.288 1.00 44.63  ?  97  ALA B CA  1 
ATOM   1845 C  C   . ALA B 2 97  ? 27.576 115.187 32.879 1.00 47.94  ?  97  ALA B C   1 
ATOM   1846 O  O   . ALA B 2 97  ? 27.332 115.166 34.091 1.00 42.40  ?  97  ALA B O   1 
ATOM   1847 C  CB  . ALA B 2 97  ? 29.813 115.356 31.814 1.00 36.50  ?  97  ALA B CB  1 
ATOM   1848 N  N   . MET B 2 98  ? 26.976 114.390 31.997 1.00 44.41  ?  98  MET B N   1 
ATOM   1849 C  CA  . MET B 2 98  ? 26.294 113.180 32.424 1.00 45.39  ?  98  MET B CA  1 
ATOM   1850 C  C   . MET B 2 98  ? 27.343 112.094 32.620 1.00 45.49  ?  98  MET B C   1 
ATOM   1851 O  O   . MET B 2 98  ? 28.158 111.844 31.720 1.00 41.21  ?  98  MET B O   1 
ATOM   1852 C  CB  . MET B 2 98  ? 25.250 112.753 31.390 1.00 48.31  ?  98  MET B CB  1 
ATOM   1853 C  CG  . MET B 2 98  ? 24.425 111.529 31.793 1.00 50.99  ?  98  MET B CG  1 
ATOM   1854 S  SD  . MET B 2 98  ? 23.342 111.716 33.248 1.00 50.18  ?  98  MET B SD  1 
ATOM   1855 C  CE  . MET B 2 98  ? 22.171 112.961 32.722 1.00 43.27  ?  98  MET B CE  1 
ATOM   1856 N  N   . TYR B 2 99  ? 27.349 111.481 33.809 1.00 40.35  ?  99  TYR B N   1 
ATOM   1857 C  CA  . TYR B 2 99  ? 28.336 110.474 34.192 1.00 30.95  ?  99  TYR B CA  1 
ATOM   1858 C  C   . TYR B 2 99  ? 27.729 109.078 34.072 1.00 43.57  ?  99  TYR B C   1 
ATOM   1859 O  O   . TYR B 2 99  ? 26.638 108.827 34.595 1.00 41.91  ?  99  TYR B O   1 
ATOM   1860 C  CB  . TYR B 2 99  ? 28.842 110.737 35.618 1.00 30.42  ?  99  TYR B CB  1 
ATOM   1861 C  CG  . TYR B 2 99  ? 29.900 111.841 35.694 1.00 34.69  ?  99  TYR B CG  1 
ATOM   1862 C  CD1 . TYR B 2 99  ? 31.219 111.554 36.062 1.00 37.83  ?  99  TYR B CD1 1 
ATOM   1863 C  CD2 . TYR B 2 99  ? 29.590 113.163 35.361 1.00 34.04  ?  99  TYR B CD2 1 
ATOM   1864 C  CE1 . TYR B 2 99  ? 32.203 112.574 36.121 1.00 35.07  ?  99  TYR B CE1 1 
ATOM   1865 C  CE2 . TYR B 2 99  ? 30.554 114.170 35.404 1.00 31.26  ?  99  TYR B CE2 1 
ATOM   1866 C  CZ  . TYR B 2 99  ? 31.853 113.873 35.788 1.00 38.41  ?  99  TYR B CZ  1 
ATOM   1867 O  OH  . TYR B 2 99  ? 32.807 114.879 35.829 1.00 43.37  ?  99  TYR B OH  1 
ATOM   1868 N  N   . TYR B 2 100 ? 28.425 108.174 33.368 1.00 44.76  ?  100 TYR B N   1 
ATOM   1869 C  CA  . TYR B 2 100 ? 27.924 106.825 33.129 1.00 38.72  ?  100 TYR B CA  1 
ATOM   1870 C  C   . TYR B 2 100 ? 28.829 105.778 33.749 1.00 35.36  ?  100 TYR B C   1 
ATOM   1871 O  O   . TYR B 2 100 ? 30.057 105.913 33.751 1.00 41.03  ?  100 TYR B O   1 
ATOM   1872 C  CB  . TYR B 2 100 ? 27.801 106.498 31.646 1.00 41.91  ?  100 TYR B CB  1 
ATOM   1873 C  CG  . TYR B 2 100 ? 26.889 107.408 30.891 1.00 46.16  ?  100 TYR B CG  1 
ATOM   1874 C  CD1 . TYR B 2 100 ? 25.538 107.112 30.741 1.00 48.36  ?  100 TYR B CD1 1 
ATOM   1875 C  CD2 . TYR B 2 100 ? 27.377 108.566 30.322 1.00 47.71  ?  100 TYR B CD2 1 
ATOM   1876 C  CE1 . TYR B 2 100 ? 24.700 107.954 30.046 1.00 44.01  ?  100 TYR B CE1 1 
ATOM   1877 C  CE2 . TYR B 2 100 ? 26.552 109.414 29.620 1.00 54.73  ?  100 TYR B CE2 1 
ATOM   1878 C  CZ  . TYR B 2 100 ? 25.218 109.108 29.482 1.00 54.49  ?  100 TYR B CZ  1 
ATOM   1879 O  OH  . TYR B 2 100 ? 24.421 109.980 28.774 1.00 60.55  ?  100 TYR B OH  1 
ATOM   1880 N  N   . CYS B 2 101 ? 28.195 104.729 34.247 1.00 39.37  ?  101 CYS B N   1 
ATOM   1881 C  CA  . CYS B 2 101 ? 28.843 103.496 34.641 1.00 33.37  ?  101 CYS B CA  1 
ATOM   1882 C  C   . CYS B 2 101 ? 28.848 102.526 33.461 1.00 39.12  ?  101 CYS B C   1 
ATOM   1883 O  O   . CYS B 2 101 ? 27.924 102.503 32.642 1.00 39.59  ?  101 CYS B O   1 
ATOM   1884 C  CB  . CYS B 2 101 ? 28.096 102.884 35.818 1.00 31.32  ?  101 CYS B CB  1 
ATOM   1885 S  SG  . CYS B 2 101 ? 28.992 101.587 36.634 1.00 53.62  ?  101 CYS B SG  1 
ATOM   1886 N  N   . ALA B 2 102 ? 29.895 101.716 33.378 1.00 44.86  ?  102 ALA B N   1 
ATOM   1887 C  CA  . ALA B 2 102 ? 30.046 100.825 32.243 1.00 21.00  ?  102 ALA B CA  1 
ATOM   1888 C  C   . ALA B 2 102 ? 30.867 99.625  32.664 1.00 29.71  ?  102 ALA B C   1 
ATOM   1889 O  O   . ALA B 2 102 ? 31.815 99.759  33.440 1.00 41.34  ?  102 ALA B O   1 
ATOM   1890 C  CB  . ALA B 2 102 ? 30.731 101.538 31.085 1.00 30.32  ?  102 ALA B CB  1 
ATOM   1891 N  N   . ALA B 2 103 ? 30.508 98.455  32.154 1.00 30.45  ?  103 ALA B N   1 
ATOM   1892 C  CA  . ALA B 2 103 ? 31.220 97.229  32.480 1.00 27.94  ?  103 ALA B CA  1 
ATOM   1893 C  C   . ALA B 2 103 ? 31.835 96.650  31.219 1.00 29.77  ?  103 ALA B C   1 
ATOM   1894 O  O   . ALA B 2 103 ? 31.156 96.530  30.187 1.00 32.36  ?  103 ALA B O   1 
ATOM   1895 C  CB  . ALA B 2 103 ? 30.289 96.209  33.137 1.00 25.20  ?  103 ALA B CB  1 
ATOM   1896 N  N   . GLY B 2 104 ? 33.117 96.303  31.308 1.00 29.92  ?  104 GLY B N   1 
ATOM   1897 C  CA  . GLY B 2 104 ? 33.832 95.665  30.218 1.00 33.95  ?  104 GLY B CA  1 
ATOM   1898 C  C   . GLY B 2 104 ? 34.435 94.329  30.612 1.00 35.14  ?  104 GLY B C   1 
ATOM   1899 O  O   . GLY B 2 104 ? 34.611 94.033  31.804 1.00 27.49  ?  104 GLY B O   1 
ATOM   1900 N  N   . ASN B 2 105 ? 34.759 93.510  29.610 1.00 32.42  ?  105 ASN B N   1 
ATOM   1901 C  CA  . ASN B 2 105 ? 35.258 92.170  29.870 1.00 29.23  ?  105 ASN B CA  1 
ATOM   1902 C  C   . ASN B 2 105 ? 36.501 92.198  30.755 1.00 37.85  ?  105 ASN B C   1 
ATOM   1903 O  O   . ASN B 2 105 ? 37.396 93.024  30.577 1.00 43.12  ?  105 ASN B O   1 
ATOM   1904 C  CB  . ASN B 2 105 ? 35.564 91.474  28.554 1.00 28.65  ?  105 ASN B CB  1 
ATOM   1905 C  CG  . ASN B 2 105 ? 35.868 90.016  28.739 1.00 30.07  ?  105 ASN B CG  1 
ATOM   1906 O  OD1 . ASN B 2 105 ? 37.007 89.639  29.004 1.00 43.44  ?  105 ASN B OD1 1 
ATOM   1907 N  ND2 . ASN B 2 105 ? 34.852 89.178  28.593 1.00 39.15  ?  105 ASN B ND2 1 
ATOM   1908 N  N   . GLY B 2 106 ? 36.551 91.281  31.725 1.00 31.90  ?  106 GLY B N   1 
ATOM   1909 C  CA  . GLY B 2 106 ? 37.662 91.264  32.664 1.00 24.60  ?  106 GLY B CA  1 
ATOM   1910 C  C   . GLY B 2 106 ? 39.008 90.957  32.045 1.00 26.82  ?  106 GLY B C   1 
ATOM   1911 O  O   . GLY B 2 106 ? 40.042 91.247  32.655 1.00 33.78  ?  106 GLY B O   1 
ATOM   1912 N  N   . ALA B 2 107 ? 39.025 90.366  30.861 1.00 32.55  ?  107 ALA B N   1 
ATOM   1913 C  CA  . ALA B 2 107 ? 40.270 90.128  30.153 1.00 37.78  ?  107 ALA B CA  1 
ATOM   1914 C  C   . ALA B 2 107 ? 40.692 91.300  29.274 1.00 38.32  ?  107 ALA B C   1 
ATOM   1915 O  O   . ALA B 2 107 ? 41.645 91.149  28.504 1.00 43.34  ?  107 ALA B O   1 
ATOM   1916 C  CB  . ALA B 2 107 ? 40.164 88.846  29.307 1.00 40.43  ?  107 ALA B CB  1 
ATOM   1917 N  N   . LEU B 2 108 ? 40.005 92.435  29.357 1.00 33.79  ?  108 LEU B N   1 
ATOM   1918 C  CA  . LEU B 2 108 ? 40.346 93.564  28.508 1.00 29.11  ?  108 LEU B CA  1 
ATOM   1919 C  C   . LEU B 2 108 ? 41.813 93.898  28.688 1.00 33.57  ?  108 LEU B C   1 
ATOM   1920 O  O   . LEU B 2 108 ? 42.339 93.865  29.812 1.00 38.11  ?  108 LEU B O   1 
ATOM   1921 C  CB  . LEU B 2 108 ? 39.493 94.793  28.837 1.00 26.66  ?  108 LEU B CB  1 
ATOM   1922 C  CG  . LEU B 2 108 ? 38.095 94.887  28.216 1.00 28.61  ?  108 LEU B CG  1 
ATOM   1923 C  CD1 . LEU B 2 108 ? 37.353 96.121  28.714 1.00 23.69  ?  108 LEU B CD1 1 
ATOM   1924 C  CD2 . LEU B 2 108 ? 38.256 94.933  26.743 1.00 30.22  ?  108 LEU B CD2 1 
ATOM   1925 N  N   . PRO B 2 109 ? 42.509 94.237  27.608 1.00 37.45  ?  109 PRO B N   1 
ATOM   1926 C  CA  . PRO B 2 109 ? 43.941 94.473  27.708 1.00 38.43  ?  109 PRO B CA  1 
ATOM   1927 C  C   . PRO B 2 109 ? 44.229 95.934  28.039 1.00 42.13  ?  109 PRO B C   1 
ATOM   1928 O  O   . PRO B 2 109 ? 43.359 96.798  27.892 1.00 39.00  ?  109 PRO B O   1 
ATOM   1929 C  CB  . PRO B 2 109 ? 44.458 94.124  26.305 1.00 30.33  ?  109 PRO B CB  1 
ATOM   1930 C  CG  . PRO B 2 109 ? 43.310 94.423  25.427 1.00 33.41  ?  109 PRO B CG  1 
ATOM   1931 C  CD  . PRO B 2 109 ? 42.041 94.246  26.219 1.00 34.72  ?  109 PRO B CD  1 
ATOM   1932 N  N   . PRO B 2 110 ? 45.442 96.240  28.502 1.00 36.06  ?  110 PRO B N   1 
ATOM   1933 C  CA  . PRO B 2 110 ? 45.774 97.641  28.812 1.00 35.52  ?  110 PRO B CA  1 
ATOM   1934 C  C   . PRO B 2 110 ? 45.518 98.510  27.604 1.00 42.43  ?  110 PRO B C   1 
ATOM   1935 O  O   . PRO B 2 110 ? 45.955 98.197  26.493 1.00 56.44  ?  110 PRO B O   1 
ATOM   1936 C  CB  . PRO B 2 110 ? 47.268 97.585  29.156 1.00 31.96  ?  110 PRO B CB  1 
ATOM   1937 C  CG  . PRO B 2 110 ? 47.502 96.160  29.587 1.00 31.66  ?  110 PRO B CG  1 
ATOM   1938 C  CD  . PRO B 2 110 ? 46.559 95.329  28.775 1.00 36.09  ?  110 PRO B CD  1 
ATOM   1939 N  N   . GLY B 2 111 ? 44.776 99.588  27.817 1.00 43.64  ?  111 GLY B N   1 
ATOM   1940 C  CA  . GLY B 2 111 ? 44.476 100.514 26.750 1.00 43.55  ?  111 GLY B CA  1 
ATOM   1941 C  C   . GLY B 2 111 ? 43.119 100.330 26.113 1.00 38.54  ?  111 GLY B C   1 
ATOM   1942 O  O   . GLY B 2 111 ? 42.683 101.215 25.365 1.00 41.40  ?  111 GLY B O   1 
ATOM   1943 N  N   . ARG B 2 112 ? 42.450 99.201  26.366 1.00 38.38  ?  112 ARG B N   1 
ATOM   1944 C  CA  . ARG B 2 112 ? 41.029 99.062  26.080 1.00 38.87  ?  112 ARG B CA  1 
ATOM   1945 C  C   . ARG B 2 112 ? 40.163 99.109  27.331 1.00 36.84  ?  112 ARG B C   1 
ATOM   1946 O  O   . ARG B 2 112 ? 38.939 99.240  27.212 1.00 31.05  ?  112 ARG B O   1 
ATOM   1947 C  CB  . ARG B 2 112 ? 40.759 97.751  25.330 1.00 39.33  ?  112 ARG B CB  1 
ATOM   1948 C  CG  . ARG B 2 112 ? 41.584 97.627  24.079 1.00 45.61  ?  112 ARG B CG  1 
ATOM   1949 C  CD  . ARG B 2 112 ? 41.074 96.545  23.153 1.00 56.63  ?  112 ARG B CD  1 
ATOM   1950 N  NE  . ARG B 2 112 ? 41.752 96.614  21.859 1.00 65.08  ?  112 ARG B NE  1 
ATOM   1951 C  CZ  . ARG B 2 112 ? 41.512 95.793  20.843 1.00 71.58  ?  112 ARG B CZ  1 
ATOM   1952 N  NH1 . ARG B 2 112 ? 40.605 94.831  20.968 1.00 78.54  1  112 ARG B NH1 1 
ATOM   1953 N  NH2 . ARG B 2 112 ? 42.181 95.934  19.704 1.00 74.98  ?  112 ARG B NH2 1 
ATOM   1954 N  N   . ARG B 2 113 ? 40.765 99.021  28.523 1.00 38.03  ?  113 ARG B N   1 
ATOM   1955 C  CA  . ARG B 2 113 ? 39.983 98.920  29.751 1.00 29.67  ?  113 ARG B CA  1 
ATOM   1956 C  C   . ARG B 2 113 ? 39.139 100.158 29.991 1.00 36.23  ?  113 ARG B C   1 
ATOM   1957 O  O   . ARG B 2 113 ? 38.053 100.068 30.579 1.00 40.55  ?  113 ARG B O   1 
ATOM   1958 C  CB  . ARG B 2 113 ? 40.919 98.665  30.925 1.00 25.95  ?  113 ARG B CB  1 
ATOM   1959 C  CG  . ARG B 2 113 ? 41.588 97.303  30.859 1.00 27.79  ?  113 ARG B CG  1 
ATOM   1960 C  CD  . ARG B 2 113 ? 42.885 97.315  31.628 1.00 30.51  ?  113 ARG B CD  1 
ATOM   1961 N  NE  . ARG B 2 113 ? 43.503 96.001  31.681 1.00 37.03  ?  113 ARG B NE  1 
ATOM   1962 C  CZ  . ARG B 2 113 ? 44.684 95.752  32.238 1.00 39.85  ?  113 ARG B CZ  1 
ATOM   1963 N  NH1 . ARG B 2 113 ? 45.394 96.733  32.793 1.00 38.93  1  113 ARG B NH1 1 
ATOM   1964 N  NH2 . ARG B 2 113 ? 45.154 94.514  32.245 1.00 43.73  ?  113 ARG B NH2 1 
ATOM   1965 N  N   . LEU B 2 114 ? 39.594 101.309 29.529 1.00 45.63  ?  114 LEU B N   1 
ATOM   1966 C  CA  . LEU B 2 114 ? 38.891 102.557 29.769 1.00 35.00  ?  114 LEU B CA  1 
ATOM   1967 C  C   . LEU B 2 114 ? 38.462 103.197 28.447 1.00 41.29  ?  114 LEU B C   1 
ATOM   1968 O  O   . LEU B 2 114 ? 38.420 104.420 28.319 1.00 51.60  ?  114 LEU B O   1 
ATOM   1969 C  CB  . LEU B 2 114 ? 39.783 103.473 30.601 1.00 28.18  ?  114 LEU B CB  1 
ATOM   1970 C  CG  . LEU B 2 114 ? 39.296 104.751 31.257 1.00 28.16  ?  114 LEU B CG  1 
ATOM   1971 C  CD1 . LEU B 2 114 ? 38.119 104.454 32.154 1.00 28.33  ?  114 LEU B CD1 1 
ATOM   1972 C  CD2 . LEU B 2 114 ? 40.449 105.240 32.080 1.00 21.54  ?  114 LEU B CD2 1 
ATOM   1973 N  N   . SER B 2 115 ? 38.128 102.373 27.443 1.00 42.23  ?  115 SER B N   1 
ATOM   1974 C  CA  . SER B 2 115 ? 37.646 102.896 26.180 1.00 45.71  ?  115 SER B CA  1 
ATOM   1975 C  C   . SER B 2 115 ? 36.173 102.560 26.009 1.00 42.25  ?  115 SER B C   1 
ATOM   1976 O  O   . SER B 2 115 ? 35.765 101.403 26.184 1.00 39.48  ?  115 SER B O   1 
ATOM   1977 C  CB  . SER B 2 115 ? 38.457 102.337 25.002 1.00 51.25  ?  115 SER B CB  1 
ATOM   1978 O  OG  . SER B 2 115 ? 37.886 101.137 24.523 1.00 60.11  ?  115 SER B OG  1 
ATOM   1979 N  N   . PRO B 2 116 ? 35.342 103.549 25.682 1.00 39.05  ?  116 PRO B N   1 
ATOM   1980 C  CA  . PRO B 2 116 ? 33.895 103.286 25.614 1.00 31.69  ?  116 PRO B CA  1 
ATOM   1981 C  C   . PRO B 2 116 ? 33.525 102.224 24.605 1.00 38.16  ?  116 PRO B C   1 
ATOM   1982 O  O   . PRO B 2 116 ? 32.538 101.499 24.800 1.00 38.97  ?  116 PRO B O   1 
ATOM   1983 C  CB  . PRO B 2 116 ? 33.280 104.650 25.233 1.00 31.02  ?  116 PRO B CB  1 
ATOM   1984 C  CG  . PRO B 2 116 ? 34.379 105.656 25.308 1.00 24.15  ?  116 PRO B CG  1 
ATOM   1985 C  CD  . PRO B 2 116 ? 35.659 104.985 25.670 1.00 27.10  ?  116 PRO B CD  1 
ATOM   1986 N  N   . GLN B 2 117 ? 34.289 102.100 23.521 1.00 47.84  ?  117 GLN B N   1 
ATOM   1987 C  CA  . GLN B 2 117 ? 33.889 101.161 22.484 1.00 48.74  ?  117 GLN B CA  1 
ATOM   1988 C  C   . GLN B 2 117 ? 33.977 99.725  22.968 1.00 45.06  ?  117 GLN B C   1 
ATOM   1989 O  O   . GLN B 2 117 ? 33.286 98.859  22.428 1.00 51.32  ?  117 GLN B O   1 
ATOM   1990 C  CB  . GLN B 2 117 ? 34.747 101.356 21.226 1.00 64.40  ?  117 GLN B CB  1 
ATOM   1991 C  CG  . GLN B 2 117 ? 35.212 102.802 20.998 1.00 76.79  ?  117 GLN B CG  1 
ATOM   1992 C  CD  . GLN B 2 117 ? 36.693 103.020 21.341 1.00 84.75  ?  117 GLN B CD  1 
ATOM   1993 O  OE1 . GLN B 2 117 ? 37.567 102.275 20.878 1.00 89.92  ?  117 GLN B OE1 1 
ATOM   1994 N  NE2 . GLN B 2 117 ? 36.976 104.038 22.166 1.00 75.23  ?  117 GLN B NE2 1 
ATOM   1995 N  N   . ASN B 2 118 ? 34.801 99.448  23.975 1.00 40.32  ?  118 ASN B N   1 
ATOM   1996 C  CA  . ASN B 2 118 ? 34.975 98.092  24.472 1.00 37.48  ?  118 ASN B CA  1 
ATOM   1997 C  C   . ASN B 2 118 ? 34.093 97.790  25.670 1.00 33.28  ?  118 ASN B C   1 
ATOM   1998 O  O   . ASN B 2 118 ? 34.233 96.724  26.281 1.00 37.42  ?  118 ASN B O   1 
ATOM   1999 C  CB  . ASN B 2 118 ? 36.436 97.844  24.829 1.00 37.51  ?  118 ASN B CB  1 
ATOM   2000 C  CG  . ASN B 2 118 ? 37.320 97.798  23.616 1.00 40.92  ?  118 ASN B CG  1 
ATOM   2001 O  OD1 . ASN B 2 118 ? 37.517 96.741  23.015 1.00 49.26  ?  118 ASN B OD1 1 
ATOM   2002 N  ND2 . ASN B 2 118 ? 37.860 98.950  23.241 1.00 38.47  ?  118 ASN B ND2 1 
ATOM   2003 N  N   . MET B 2 119 ? 33.198 98.705  26.018 1.00 36.87  ?  119 MET B N   1 
ATOM   2004 C  CA  . MET B 2 119 ? 32.248 98.486  27.097 1.00 36.75  ?  119 MET B CA  1 
ATOM   2005 C  C   . MET B 2 119 ? 31.092 97.639  26.588 1.00 42.39  ?  119 MET B C   1 
ATOM   2006 O  O   . MET B 2 119 ? 30.634 97.819  25.456 1.00 45.96  ?  119 MET B O   1 
ATOM   2007 C  CB  . MET B 2 119 ? 31.745 99.835  27.605 1.00 29.45  ?  119 MET B CB  1 
ATOM   2008 C  CG  . MET B 2 119 ? 32.815 100.591 28.387 1.00 25.61  ?  119 MET B CG  1 
ATOM   2009 S  SD  . MET B 2 119 ? 33.685 99.546  29.560 1.00 32.76  ?  119 MET B SD  1 
ATOM   2010 C  CE  . MET B 2 119 ? 35.331 99.444  28.863 1.00 30.73  ?  119 MET B CE  1 
ATOM   2011 N  N   . ASP B 2 120 ? 30.621 96.708  27.421 1.00 38.10  ?  120 ASP B N   1 
ATOM   2012 C  CA  . ASP B 2 120 ? 29.484 95.866  27.055 1.00 29.06  ?  120 ASP B CA  1 
ATOM   2013 C  C   . ASP B 2 120 ? 28.154 96.369  27.599 1.00 35.88  ?  120 ASP B C   1 
ATOM   2014 O  O   . ASP B 2 120 ? 27.121 96.233  26.937 1.00 41.83  ?  120 ASP B O   1 
ATOM   2015 C  CB  . ASP B 2 120 ? 29.689 94.436  27.553 1.00 33.40  ?  120 ASP B CB  1 
ATOM   2016 C  CG  . ASP B 2 120 ? 30.923 93.783  26.982 1.00 40.83  ?  120 ASP B CG  1 
ATOM   2017 O  OD1 . ASP B 2 120 ? 30.999 93.608  25.739 1.00 40.27  ?  120 ASP B OD1 1 
ATOM   2018 O  OD2 . ASP B 2 120 ? 31.805 93.417  27.792 1.00 45.10  -1 120 ASP B OD2 1 
ATOM   2019 N  N   . THR B 2 121 ? 28.147 96.925  28.800 1.00 40.47  ?  121 THR B N   1 
ATOM   2020 C  CA  . THR B 2 121 ? 26.929 97.361  29.455 1.00 30.88  ?  121 THR B CA  1 
ATOM   2021 C  C   . THR B 2 121 ? 27.113 98.796  29.906 1.00 32.56  ?  121 THR B C   1 
ATOM   2022 O  O   . THR B 2 121 ? 28.197 99.167  30.377 1.00 36.72  ?  121 THR B O   1 
ATOM   2023 C  CB  . THR B 2 121 ? 26.622 96.482  30.655 1.00 27.62  ?  121 THR B CB  1 
ATOM   2024 O  OG1 . THR B 2 121 ? 26.841 95.117  30.296 1.00 36.43  ?  121 THR B OG1 1 
ATOM   2025 C  CG2 . THR B 2 121 ? 25.189 96.673  31.103 1.00 30.24  ?  121 THR B CG2 1 
ATOM   2026 N  N   . TRP B 2 122 ? 26.049 99.592  29.765 1.00 36.24  ?  122 TRP B N   1 
ATOM   2027 C  CA  . TRP B 2 122 ? 26.005 100.976 30.218 1.00 39.14  ?  122 TRP B CA  1 
ATOM   2028 C  C   . TRP B 2 122 ? 24.844 101.199 31.181 1.00 44.04  ?  122 TRP B C   1 
ATOM   2029 O  O   . TRP B 2 122 ? 23.780 100.585 31.058 1.00 46.96  ?  122 TRP B O   1 
ATOM   2030 C  CB  . TRP B 2 122 ? 25.858 101.941 29.039 1.00 39.59  ?  122 TRP B CB  1 
ATOM   2031 C  CG  . TRP B 2 122 ? 27.051 101.960 28.189 1.00 34.45  ?  122 TRP B CG  1 
ATOM   2032 C  CD1 . TRP B 2 122 ? 27.324 101.135 27.137 1.00 34.26  ?  122 TRP B CD1 1 
ATOM   2033 C  CD2 . TRP B 2 122 ? 28.166 102.837 28.316 1.00 31.23  ?  122 TRP B CD2 1 
ATOM   2034 N  NE1 . TRP B 2 122 ? 28.542 101.455 26.591 1.00 39.21  ?  122 TRP B NE1 1 
ATOM   2035 C  CE2 . TRP B 2 122 ? 29.082 102.497 27.302 1.00 40.10  ?  122 TRP B CE2 1 
ATOM   2036 C  CE3 . TRP B 2 122 ? 28.483 103.876 29.190 1.00 35.70  ?  122 TRP B CE3 1 
ATOM   2037 C  CZ2 . TRP B 2 122 ? 30.301 103.160 27.144 1.00 39.09  ?  122 TRP B CZ2 1 
ATOM   2038 C  CZ3 . TRP B 2 122 ? 29.688 104.539 29.024 1.00 34.01  ?  122 TRP B CZ3 1 
ATOM   2039 C  CH2 . TRP B 2 122 ? 30.581 104.178 28.011 1.00 31.14  ?  122 TRP B CH2 1 
ATOM   2040 N  N   . GLY B 2 123 ? 25.053 102.102 32.129 1.00 39.73  ?  123 GLY B N   1 
ATOM   2041 C  CA  . GLY B 2 123 ? 23.988 102.541 32.993 1.00 40.17  ?  123 GLY B CA  1 
ATOM   2042 C  C   . GLY B 2 123 ? 23.244 103.701 32.385 1.00 44.59  ?  123 GLY B C   1 
ATOM   2043 O  O   . GLY B 2 123 ? 23.624 104.224 31.337 1.00 50.80  ?  123 GLY B O   1 
ATOM   2044 N  N   . PRO B 2 124 ? 22.147 104.121 33.027 1.00 47.56  ?  124 PRO B N   1 
ATOM   2045 C  CA  . PRO B 2 124 ? 21.360 105.244 32.475 1.00 41.36  ?  124 PRO B CA  1 
ATOM   2046 C  C   . PRO B 2 124 ? 22.032 106.599 32.596 1.00 44.42  ?  124 PRO B C   1 
ATOM   2047 O  O   . PRO B 2 124 ? 21.808 107.460 31.737 1.00 51.35  ?  124 PRO B O   1 
ATOM   2048 C  CB  . PRO B 2 124 ? 20.054 105.212 33.289 1.00 33.47  ?  124 PRO B CB  1 
ATOM   2049 C  CG  . PRO B 2 124 ? 20.330 104.307 34.465 1.00 33.13  ?  124 PRO B CG  1 
ATOM   2050 C  CD  . PRO B 2 124 ? 21.401 103.364 34.044 1.00 39.51  ?  124 PRO B CD  1 
ATOM   2051 N  N   . GLY B 2 125 ? 22.797 106.831 33.646 1.00 46.57  ?  125 GLY B N   1 
ATOM   2052 C  CA  . GLY B 2 125 ? 23.490 108.084 33.853 1.00 44.25  ?  125 GLY B CA  1 
ATOM   2053 C  C   . GLY B 2 125 ? 22.980 108.827 35.083 1.00 52.85  ?  125 GLY B C   1 
ATOM   2054 O  O   . GLY B 2 125 ? 21.817 108.689 35.493 1.00 57.74  ?  125 GLY B O   1 
ATOM   2055 N  N   . THR B 2 126 ? 23.874 109.617 35.692 1.00 49.96  ?  126 THR B N   1 
ATOM   2056 C  CA  . THR B 2 126 ? 23.541 110.566 36.755 1.00 47.63  ?  126 THR B CA  1 
ATOM   2057 C  C   . THR B 2 126 ? 24.227 111.889 36.426 1.00 49.57  ?  126 THR B C   1 
ATOM   2058 O  O   . THR B 2 126 ? 25.411 111.900 36.076 1.00 51.96  ?  126 THR B O   1 
ATOM   2059 C  CB  . THR B 2 126 ? 23.962 110.025 38.142 1.00 46.18  ?  126 THR B CB  1 
ATOM   2060 O  OG1 . THR B 2 126 ? 23.478 110.876 39.189 1.00 50.15  ?  126 THR B OG1 1 
ATOM   2061 C  CG2 . THR B 2 126 ? 25.471 109.863 38.279 1.00 45.55  ?  126 THR B CG2 1 
ATOM   2062 N  N   . GLN B 2 127 ? 23.482 112.996 36.472 1.00 48.85  ?  127 GLN B N   1 
ATOM   2063 C  CA  . GLN B 2 127 ? 24.032 114.273 36.024 1.00 44.35  ?  127 GLN B CA  1 
ATOM   2064 C  C   . GLN B 2 127 ? 24.822 114.956 37.136 1.00 51.71  ?  127 GLN B C   1 
ATOM   2065 O  O   . GLN B 2 127 ? 24.402 114.976 38.296 1.00 52.95  ?  127 GLN B O   1 
ATOM   2066 C  CB  . GLN B 2 127 ? 22.918 115.188 35.514 1.00 31.56  ?  127 GLN B CB  1 
ATOM   2067 C  CG  . GLN B 2 127 ? 23.404 116.600 35.160 1.00 39.30  ?  127 GLN B CG  1 
ATOM   2068 C  CD  . GLN B 2 127 ? 24.072 116.673 33.786 1.00 49.40  ?  127 GLN B CD  1 
ATOM   2069 O  OE1 . GLN B 2 127 ? 23.913 115.777 32.969 1.00 60.82  ?  127 GLN B OE1 1 
ATOM   2070 N  NE2 . GLN B 2 127 ? 24.809 117.750 33.527 1.00 51.29  ?  127 GLN B NE2 1 
ATOM   2071 N  N   . VAL B 2 128 ? 25.989 115.492 36.774 1.00 51.64  ?  128 VAL B N   1 
ATOM   2072 C  CA  . VAL B 2 128 ? 26.829 116.275 37.675 1.00 41.83  ?  128 VAL B CA  1 
ATOM   2073 C  C   . VAL B 2 128 ? 26.962 117.669 37.076 1.00 45.38  ?  128 VAL B C   1 
ATOM   2074 O  O   . VAL B 2 128 ? 27.407 117.810 35.927 1.00 45.49  ?  128 VAL B O   1 
ATOM   2075 C  CB  . VAL B 2 128 ? 28.216 115.644 37.861 1.00 38.67  ?  128 VAL B CB  1 
ATOM   2076 C  CG1 . VAL B 2 128 ? 29.080 116.552 38.701 1.00 32.27  ?  128 VAL B CG1 1 
ATOM   2077 C  CG2 . VAL B 2 128 ? 28.122 114.266 38.482 1.00 32.23  ?  128 VAL B CG2 1 
ATOM   2078 N  N   . THR B 2 129 ? 26.580 118.693 37.850 1.00 43.84  ?  129 THR B N   1 
ATOM   2079 C  CA  . THR B 2 129 ? 26.691 120.093 37.440 1.00 52.81  ?  129 THR B CA  1 
ATOM   2080 C  C   . THR B 2 129 ? 27.532 120.856 38.465 1.00 53.76  ?  129 THR B C   1 
ATOM   2081 O  O   . THR B 2 129 ? 27.221 120.846 39.668 1.00 43.58  ?  129 THR B O   1 
ATOM   2082 C  CB  . THR B 2 129 ? 25.301 120.756 37.279 1.00 53.62  ?  129 THR B CB  1 
ATOM   2083 O  OG1 . THR B 2 129 ? 24.784 121.115 38.565 1.00 66.82  ?  129 THR B OG1 1 
ATOM   2084 C  CG2 . THR B 2 129 ? 24.301 119.801 36.625 1.00 37.91  ?  129 THR B CG2 1 
ATOM   2085 N  N   . VAL B 2 130 ? 28.589 121.525 37.986 1.00 48.17  ?  130 VAL B N   1 
ATOM   2086 C  CA  . VAL B 2 130 ? 29.537 122.242 38.846 1.00 48.39  ?  130 VAL B CA  1 
ATOM   2087 C  C   . VAL B 2 130 ? 29.506 123.737 38.519 1.00 54.35  ?  130 VAL B C   1 
ATOM   2088 O  O   . VAL B 2 130 ? 29.817 124.137 37.388 1.00 57.72  ?  130 VAL B O   1 
ATOM   2089 C  CB  . VAL B 2 130 ? 30.960 121.683 38.699 1.00 40.85  ?  130 VAL B CB  1 
ATOM   2090 C  CG1 . VAL B 2 130 ? 31.889 122.393 39.646 1.00 39.01  ?  130 VAL B CG1 1 
ATOM   2091 C  CG2 . VAL B 2 130 ? 30.960 120.176 38.965 1.00 32.86  ?  130 VAL B CG2 1 
ATOM   2092 N  N   . SER B 2 131 ? 29.147 124.560 39.518 1.00 54.16  ?  131 SER B N   1 
ATOM   2093 C  CA  . SER B 2 131 ? 29.044 126.012 39.341 1.00 55.47  ?  131 SER B CA  1 
ATOM   2094 C  C   . SER B 2 131 ? 30.408 126.678 39.354 1.00 59.56  ?  131 SER B C   1 
ATOM   2095 O  O   . SER B 2 131 ? 31.264 126.342 40.174 1.00 62.45  ?  131 SER B O   1 
ATOM   2096 C  CB  . SER B 2 131 ? 28.222 126.661 40.456 1.00 50.25  ?  131 SER B CB  1 
ATOM   2097 O  OG  . SER B 2 131 ? 26.946 126.091 40.565 1.00 72.00  ?  131 SER B OG  1 
ATOM   2098 N  N   . SER B 2 132 ? 30.582 127.672 38.482 1.00 65.79  ?  132 SER B N   1 
ATOM   2099 C  CA  . SER B 2 132 ? 31.699 128.600 38.618 1.00 58.50  ?  132 SER B CA  1 
ATOM   2100 C  C   . SER B 2 132 ? 31.502 129.476 39.847 1.00 50.22  ?  132 SER B C   1 
ATOM   2101 O  O   . SER B 2 132 ? 30.373 129.720 40.282 1.00 61.55  ?  132 SER B O   1 
ATOM   2102 C  CB  . SER B 2 132 ? 31.817 129.483 37.382 1.00 55.63  ?  132 SER B CB  1 
ATOM   2103 O  OG  . SER B 2 132 ? 32.208 128.705 36.269 1.00 66.16  ?  132 SER B OG  1 
ATOM   2104 N  N   . HIS B 2 133 ? 32.614 129.945 40.424 1.00 44.20  ?  133 HIS B N   1 
ATOM   2105 C  CA  . HIS B 2 133 ? 32.507 130.974 41.460 1.00 60.16  ?  133 HIS B CA  1 
ATOM   2106 C  C   . HIS B 2 133 ? 31.918 132.248 40.886 1.00 72.82  ?  133 HIS B C   1 
ATOM   2107 O  O   . HIS B 2 133 ? 31.318 133.057 41.610 1.00 67.70  ?  133 HIS B O   1 
ATOM   2108 C  CB  . HIS B 2 133 ? 33.874 131.269 42.060 1.00 59.29  ?  133 HIS B CB  1 
ATOM   2109 C  CG  . HIS B 2 133 ? 34.567 130.060 42.583 1.00 58.50  ?  133 HIS B CG  1 
ATOM   2110 N  ND1 . HIS B 2 133 ? 34.131 129.383 43.701 1.00 59.78  ?  133 HIS B ND1 1 
ATOM   2111 C  CD2 . HIS B 2 133 ? 35.659 129.395 42.138 1.00 66.29  ?  133 HIS B CD2 1 
ATOM   2112 C  CE1 . HIS B 2 133 ? 34.931 128.355 43.928 1.00 68.16  ?  133 HIS B CE1 1 
ATOM   2113 N  NE2 . HIS B 2 133 ? 35.869 128.343 42.996 1.00 73.13  ?  133 HIS B NE2 1 
ATOM   2114 N  N   . HIS B 2 134 ? 32.080 132.418 39.583 1.00 87.14  ?  134 HIS B N   1 
ATOM   2115 C  CA  . HIS B 2 134 ? 31.667 133.543 38.772 1.00 85.07  ?  134 HIS B CA  1 
ATOM   2116 C  C   . HIS B 2 134 ? 30.178 133.494 38.426 1.00 80.76  ?  134 HIS B C   1 
ATOM   2117 O  O   . HIS B 2 134 ? 29.713 134.315 37.630 1.00 83.26  ?  134 HIS B O   1 
ATOM   2118 C  CB  . HIS B 2 134 ? 32.568 133.554 37.527 1.00 93.34  ?  134 HIS B CB  1 
ATOM   2119 C  CG  . HIS B 2 134 ? 33.973 133.064 37.805 1.00 96.85  ?  134 HIS B CG  1 
ATOM   2120 N  ND1 . HIS B 2 134 ? 34.339 131.733 37.711 1.00 92.03  ?  134 HIS B ND1 1 
ATOM   2121 C  CD2 . HIS B 2 134 ? 35.088 133.725 38.208 1.00 82.49  ?  134 HIS B CD2 1 
ATOM   2122 C  CE1 . HIS B 2 134 ? 35.616 131.599 38.028 1.00 71.72  ?  134 HIS B CE1 1 
ATOM   2123 N  NE2 . HIS B 2 134 ? 36.094 132.793 38.331 1.00 69.06  ?  134 HIS B NE2 1 
ATOM   2124 N  N   . HIS B 2 135 ? 29.438 132.545 39.024 1.00 86.72  ?  135 HIS B N   1 
ATOM   2125 C  CA  . HIS B 2 135 ? 27.974 132.432 38.923 1.00 92.33  ?  135 HIS B CA  1 
ATOM   2126 C  C   . HIS B 2 135 ? 27.353 132.988 40.207 1.00 102.22 ?  135 HIS B C   1 
ATOM   2127 O  O   . HIS B 2 135 ? 26.955 132.250 41.111 1.00 87.84  ?  135 HIS B O   1 
ATOM   2128 C  CB  . HIS B 2 135 ? 27.542 130.974 38.705 1.00 86.72  ?  135 HIS B CB  1 
ATOM   2129 C  CG  . HIS B 2 135 ? 27.611 130.497 37.282 1.00 84.51  ?  135 HIS B CG  1 
ATOM   2130 N  ND1 . HIS B 2 135 ? 28.265 129.336 36.919 1.00 82.19  ?  135 HIS B ND1 1 
ATOM   2131 C  CD2 . HIS B 2 135 ? 27.070 130.994 36.141 1.00 79.49  ?  135 HIS B CD2 1 
ATOM   2132 C  CE1 . HIS B 2 135 ? 28.146 129.154 35.614 1.00 75.15  ?  135 HIS B CE1 1 
ATOM   2133 N  NE2 . HIS B 2 135 ? 27.424 130.144 35.118 1.00 73.58  ?  135 HIS B NE2 1 
ATOM   2134 N  N   . HIS B 2 136 ? 27.269 134.314 40.283 1.00 129.67 ?  136 HIS B N   1 
ATOM   2135 C  CA  . HIS B 2 136 ? 26.687 134.978 41.456 1.00 137.23 ?  136 HIS B CA  1 
ATOM   2136 C  C   . HIS B 2 136 ? 25.157 134.853 41.439 1.00 135.91 ?  136 HIS B C   1 
ATOM   2137 O  O   . HIS B 2 136 ? 24.429 135.835 41.617 1.00 132.36 ?  136 HIS B O   1 
ATOM   2138 C  CB  . HIS B 2 136 ? 27.107 136.461 41.524 1.00 134.17 ?  136 HIS B CB  1 
ATOM   2139 C  CG  . HIS B 2 136 ? 28.564 136.674 41.814 1.00 126.61 ?  136 HIS B CG  1 
ATOM   2140 N  ND1 . HIS B 2 136 ? 29.347 135.735 42.452 1.00 125.67 ?  136 HIS B ND1 1 
ATOM   2141 C  CD2 . HIS B 2 136 ? 29.378 137.725 41.554 1.00 121.34 ?  136 HIS B CD2 1 
ATOM   2142 C  CE1 . HIS B 2 136 ? 30.580 136.195 42.570 1.00 123.16 ?  136 HIS B CE1 1 
ATOM   2143 N  NE2 . HIS B 2 136 ? 30.625 137.400 42.031 1.00 123.25 ?  136 HIS B NE2 1 
HETATM 2144 CU CU  A CU  C 3 .   ? 43.808 70.859  37.351 0.78 43.03  ?  201 CU  A CU  1 
HETATM 2145 ZN ZN  A ZN  D 4 .   ? 47.313 66.649  41.239 0.82 51.57  ?  202 ZN  A ZN  1 
# 
# 
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   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 2 1   MET 1   1   1   MET MET B . n 
B 2 2   ALA 2   2   2   ALA ALA B . n 
B 2 3   GLN 3   3   3   GLN GLN B . n 
B 2 4   VAL 4   4   4   VAL VAL B . n 
B 2 5   GLN 5   5   5   GLN GLN B . n 
B 2 6   LEU 6   6   6   LEU LEU B . n 
B 2 7   GLN 7   7   7   GLN GLN B . n 
B 2 8   GLU 8   8   8   GLU GLU B . n 
B 2 9   SER 9   9   9   SER SER B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  GLY 11  11  11  GLY GLY B . n 
B 2 12  GLY 12  12  12  GLY GLY B . n 
B 2 13  SER 13  13  13  SER SER B . n 
B 2 14  VAL 14  14  14  VAL VAL B . n 
B 2 15  GLN 15  15  15  GLN GLN B . n 
B 2 16  ALA 16  16  16  ALA ALA B . n 
B 2 17  GLY 17  17  17  GLY GLY B . n 
B 2 18  GLY 18  18  18  GLY GLY B . n 
B 2 19  SER 19  19  19  SER SER B . n 
B 2 20  LEU 20  20  20  LEU LEU B . n 
B 2 21  ARG 21  21  21  ARG ARG B . n 
B 2 22  LEU 22  22  22  LEU LEU B . n 
B 2 23  ALA 23  23  23  ALA ALA B . n 
B 2 24  CYS 24  24  24  CYS CYS B . n 
B 2 25  VAL 25  25  25  VAL VAL B . n 
B 2 26  ALA 26  26  26  ALA ALA B . n 
B 2 27  SER 27  27  27  SER SER B . n 
B 2 28  GLY 28  28  28  GLY GLY B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  ASP 30  30  30  ASP ASP B . n 
B 2 31  THR 31  31  31  THR THR B . n 
B 2 32  ARG 32  32  32  ARG ARG B . n 
B 2 33  PRO 33  33  33  PRO PRO B . n 
B 2 34  TYR 34  34  34  TYR TYR B . n 
B 2 35  ILE 35  35  35  ILE ILE B . n 
B 2 36  THR 36  36  36  THR THR B . n 
B 2 37  TYR 37  37  37  TYR TYR B . n 
B 2 38  TRP 38  38  38  TRP TRP B . n 
B 2 39  MET 39  39  39  MET MET B . n 
B 2 40  GLY 40  40  40  GLY GLY B . n 
B 2 41  TRP 41  41  41  TRP TRP B . n 
B 2 42  TYR 42  42  42  TYR TYR B . n 
B 2 43  ARG 43  43  43  ARG ARG B . n 
B 2 44  GLN 44  44  44  GLN GLN B . n 
B 2 45  ALA 45  45  45  ALA ALA B . n 
B 2 46  PRO 46  46  46  PRO PRO B . n 
B 2 47  GLY 47  47  47  GLY GLY B . n 
B 2 48  LYS 48  48  48  LYS LYS B . n 
B 2 49  GLU 49  49  49  GLU GLU B . n 
B 2 50  ARG 50  50  50  ARG ARG B . n 
B 2 51  GLU 51  51  51  GLU GLU B . n 
B 2 52  GLY 52  52  52  GLY GLY B . n 
B 2 53  VAL 53  53  53  VAL VAL B . n 
B 2 54  ALA 54  54  54  ALA ALA B . n 
B 2 55  THR 55  55  55  THR THR B . n 
B 2 56  ILE 56  56  56  ILE ILE B . n 
B 2 57  TYR 57  57  57  TYR TYR B . n 
B 2 58  THR 58  58  58  THR THR B . n 
B 2 59  GLY 59  59  59  GLY GLY B . n 
B 2 60  GLY 60  60  60  GLY GLY B . n 
B 2 61  SER 61  61  61  SER SER B . n 
B 2 62  GLY 62  62  62  GLY GLY B . n 
B 2 63  THR 63  63  63  THR THR B . n 
B 2 64  TYR 64  64  64  TYR TYR B . n 
B 2 65  TYR 65  65  65  TYR TYR B . n 
B 2 66  SER 66  66  66  SER SER B . n 
B 2 67  ASP 67  67  67  ASP ASP B . n 
B 2 68  SER 68  68  68  SER SER B . n 
B 2 69  VAL 69  69  69  VAL VAL B . n 
B 2 70  GLU 70  70  70  GLU GLU B . n 
B 2 71  GLY 71  71  71  GLY GLY B . n 
B 2 72  ARG 72  72  72  ARG ARG B . n 
B 2 73  PHE 73  73  73  PHE PHE B . n 
B 2 74  THR 74  74  74  THR THR B . n 
B 2 75  ILE 75  75  75  ILE ILE B . n 
B 2 76  SER 76  76  76  SER SER B . n 
B 2 77  GLN 77  77  77  GLN GLN B . n 
B 2 78  ASP 78  78  78  ASP ASP B . n 
B 2 79  LYS 79  79  79  LYS LYS B . n 
B 2 80  ALA 80  80  80  ALA ALA B . n 
B 2 81  GLN 81  81  81  GLN GLN B . n 
B 2 82  ARG 82  82  82  ARG ARG B . n 
B 2 83  THR 83  83  83  THR THR B . n 
B 2 84  VAL 84  84  84  VAL VAL B . n 
B 2 85  TYR 85  85  85  TYR TYR B . n 
B 2 86  LEU 86  86  86  LEU LEU B . n 
B 2 87  GLN 87  87  87  GLN GLN B . n 
B 2 88  MET 88  88  88  MET MET B . n 
B 2 89  ASN 89  89  89  ASN ASN B . n 
B 2 90  ASP 90  90  90  ASP ASP B . n 
B 2 91  LEU 91  91  91  LEU LEU B . n 
B 2 92  LYS 92  92  92  LYS LYS B . n 
B 2 93  PRO 93  93  93  PRO PRO B . n 
B 2 94  GLU 94  94  94  GLU GLU B . n 
B 2 95  ASP 95  95  95  ASP ASP B . n 
B 2 96  THR 96  96  96  THR THR B . n 
B 2 97  ALA 97  97  97  ALA ALA B . n 
B 2 98  MET 98  98  98  MET MET B . n 
B 2 99  TYR 99  99  99  TYR TYR B . n 
B 2 100 TYR 100 100 100 TYR TYR B . n 
B 2 101 CYS 101 101 101 CYS CYS B . n 
B 2 102 ALA 102 102 102 ALA ALA B . n 
B 2 103 ALA 103 103 103 ALA ALA B . n 
B 2 104 GLY 104 104 104 GLY GLY B . n 
B 2 105 ASN 105 105 105 ASN ASN B . n 
B 2 106 GLY 106 106 106 GLY GLY B . n 
B 2 107 ALA 107 107 107 ALA ALA B . n 
B 2 108 LEU 108 108 108 LEU LEU B . n 
B 2 109 PRO 109 109 109 PRO PRO B . n 
B 2 110 PRO 110 110 110 PRO PRO B . n 
B 2 111 GLY 111 111 111 GLY GLY B . n 
B 2 112 ARG 112 112 112 ARG ARG B . n 
B 2 113 ARG 113 113 113 ARG ARG B . n 
B 2 114 LEU 114 114 114 LEU LEU B . n 
B 2 115 SER 115 115 115 SER SER B . n 
B 2 116 PRO 116 116 116 PRO PRO B . n 
B 2 117 GLN 117 117 117 GLN GLN B . n 
B 2 118 ASN 118 118 118 ASN ASN B . n 
B 2 119 MET 119 119 119 MET MET B . n 
B 2 120 ASP 120 120 120 ASP ASP B . n 
B 2 121 THR 121 121 121 THR THR B . n 
B 2 122 TRP 122 122 122 TRP TRP B . n 
B 2 123 GLY 123 123 123 GLY GLY B . n 
B 2 124 PRO 124 124 124 PRO PRO B . n 
B 2 125 GLY 125 125 125 GLY GLY B . n 
B 2 126 THR 126 126 126 THR THR B . n 
B 2 127 GLN 127 127 127 GLN GLN B . n 
B 2 128 VAL 128 128 128 VAL VAL B . n 
B 2 129 THR 129 129 129 THR THR B . n 
B 2 130 VAL 130 130 130 VAL VAL B . n 
B 2 131 SER 131 131 131 SER SER B . n 
B 2 132 SER 132 132 132 SER SER B . n 
B 2 133 HIS 133 133 133 HIS HIS B . n 
B 2 134 HIS 134 134 134 HIS HIS B . n 
B 2 135 HIS 135 135 135 HIS HIS B . n 
B 2 136 HIS 136 136 136 HIS HIS B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 CU 1 201 1154 CU CU A . 
D 4 ZN 1 202 1155 ZN ZN A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z            1.0000000000 0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 8_665 -y+1,-x+1,-z+1/2 0.0000000000 -1.0000000000 0.0000000000 115.8300000000 -1.0000000000 
0.0000000000 0.0000000000 115.8300000000 0.0000000000 0.0000000000 -1.0000000000 41.8950000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU A C CU . ? A CU 201 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 135.9 ? 
2 ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU A C CU . ? A CU 201 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 105.6 ? 
3 NE2 ? A HIS 48 ? A HIS 48 ? 1_555 CU A C CU . ? A CU 201 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 117.7 ? 
4 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN A D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 121.0 ? 
5 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN A D ZN . ? A ZN 202 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 99.2  ? 
6 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN A D ZN . ? A ZN 202 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 95.7  ? 
# 
_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       2022-09-28 
# 
_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             ? 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 49.0235 72.6601 34.5554 0.3516 ? 0.0899  ? -0.3154 ? 0.2439 ? 0.0429  ? 0.8045 ? 0.4120 ? -0.0397 
? 0.1609 ? 0.4966 ? 0.1095  ? 0.1412 ? 0.1011  ? -0.2236 ? -0.6777 ? 0.3247 ? 0.1841  ? -0.4072 ? 0.3091  ? 0.1577 ? 0.3466 ? 
2 'X-RAY DIFFRACTION' ? refined 25.2147 47.7062 26.4460 0.3630 ? -0.0040 ? -0.1259 ? 0.2638 ? -0.0105 ? 0.1387 ? 0.3833 ? -0.5514 
? 0.0841 ? 0.8440 ? -0.2414 ? 0.3196 ? -0.0109 ? -0.0463 ? 0.1739  ? 0.1535 ? -0.1249 ? -0.3322 ? -0.0679 ? 0.0743 ? 0.0003 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 1 ? ? ? A 153 ? ? '(chain A and resseq 1:153)' 
2 'X-RAY DIFFRACTION' 2 ? ? B 1 ? ? ? B 136 ? ? '(chain B and resseq 1:136)' 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.10.1_2155 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27        2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .           3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .           5 
# 
_pdbx_entry_details.entry_id                 7NXX 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   C 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   MET 
_pdbx_validate_close_contact.auth_seq_id_1    39 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   CA 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   GLY 
_pdbx_validate_close_contact.auth_seq_id_2    40 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.28 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 N  B GLY 40 ? ? CA B GLY 40 ? ? 0.875 1.456 -0.581 0.015 N 
2 1 CA B GLY 40 ? ? C  B GLY 40 ? ? 2.373 1.514 0.859  0.016 N 
# 
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 NE A ARG 79 ? ? CZ A ARG 79 ? ? NH1 A ARG 79 ? ? 116.87 120.30 -3.43  0.50 N 
2 1 C  B MET 39 ? ? N  B GLY 40 ? ? CA  B GLY 40 ? ? 67.47  122.30 -54.83 2.10 Y 
3 1 N  B GLY 40 ? ? CA B GLY 40 ? ? C   B GLY 40 ? ? 86.19  113.10 -26.91 2.50 N 
4 1 CA B GLY 40 ? ? C  B GLY 40 ? ? O   B GLY 40 ? ? 100.57 120.60 -20.03 1.80 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 ALA A 55  ? ? -96.55  38.29  
2 1 ALA B 2   ? ? -77.45  -89.59 
3 1 SER B 61  ? ? -151.32 -3.27  
4 1 ASP B 90  ? ? 37.23   61.30  
5 1 HIS B 135 ? ? -101.75 79.46  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 MET B 39 ? ? GLY B 40 ? ? 139.92  
2 1 GLY B 40 ? ? TRP B 41 ? ? -143.36 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             GLY 
_pdbx_validate_main_chain_plane.auth_asym_id             B 
_pdbx_validate_main_chain_plane.auth_seq_id              40 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   20.87 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium G0C1319N   1 
'KU Leuven'                            Belgium C14/17/093 2 
'Research Foundation - Flanders (FWO)' Belgium G0H1716N   3 
'KU Leuven'                            Belgium C24/17/075 4 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CU ? ? CU ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ZN ? ? ZN ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'COPPER (II) ION' CU 
4 'ZINC ION'        ZN 
# 
_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                ? 
# 
